data_9H5O
# 
_entry.id   9H5O 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9H5O         pdb_00009h5o 10.2210/pdb9h5o/pdb 
WWPDB D_1292142683 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-21 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9H5O 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-23 
_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              patrik.johansson@astrazeneca.com 
_pdbx_contact_author.name_first         Patrik 
_pdbx_contact_author.name_last          Johansson 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7850-1169 
# 
_audit_author.name               'Johansson, P.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_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.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            301 
_citation.language                  ? 
_citation.page_first                108492 
_citation.page_last                 108492 
_citation.title                     
'Mechanism and kinetics of turnover inhibitors of nicotinamide N-methyl transferase in vitro and in vivo.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2025.108492 
_citation.pdbx_database_id_PubMed   40209950 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Akerud, T.'     1  ? 
primary 'De Fusco, C.'   2  ? 
primary 'Brandt, P.'     3  ? 
primary 'Bergstrom, F.'  4  ? 
primary 'Johansson, P.'  5  ? 
primary 'Ek, M.'         6  ? 
primary 'Borjesson, U.'  7  ? 
primary 'Johansson, A.'  8  ? 
primary 'Danielsson, J.' 9  ? 
primary 'Bauer, M.'      10 ? 
primary 'Arnaud, B.'     11 ? 
primary 'Castaldo, M.'   12 ? 
primary 'Stromstedt, M.' 13 ? 
primary 'Rosengren, B.'  14 ? 
primary 'Jansen, F.'     15 ? 
primary 'Fredlund, L.'   16 ? 
# 
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 'Nicotinamide N-methyltransferase'                   31326.623 2   2.1.1.1 ? ? ? 
2 non-polymer syn '1,4-dimethyl-6-(methylamino)pyridine-3-carboxamide' 180.227   2   ?       ? ? ? 
3 non-polymer syn S-ADENOSYL-L-HOMOCYSTEINE                            384.411   2   ?       ? ? ? 
4 water       nat water                                                18.015    346 ?       ? ? ? 
# 
_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       
;HNHNHNHNHNHNAAAENLYFQSGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLID
IGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKAAPAAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKC
DVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAV
EAAVKEAGYTIEWFEVISQSYSSTMANNEGLFSLVARKLS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HNHNHNHNHNHNAAAENLYFQSGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLID
IGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKAAPAAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKC
DVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAV
EAAVKEAGYTIEWFEVISQSYSSTMANNEGLFSLVARKLS
;
_entity_poly.pdbx_strand_id                 B,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '1,4-dimethyl-6-(methylamino)pyridine-3-carboxamide' A1IPM 
3 S-ADENOSYL-L-HOMOCYSTEINE                            SAH   
4 water                                                HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   ASN n 
1 3   HIS n 
1 4   ASN n 
1 5   HIS n 
1 6   ASN n 
1 7   HIS n 
1 8   ASN n 
1 9   HIS n 
1 10  ASN n 
1 11  HIS n 
1 12  ASN n 
1 13  ALA n 
1 14  ALA n 
1 15  ALA n 
1 16  GLU n 
1 17  ASN n 
1 18  LEU n 
1 19  TYR n 
1 20  PHE n 
1 21  GLN n 
1 22  SER n 
1 23  GLY n 
1 24  PHE n 
1 25  THR n 
1 26  SER n 
1 27  LYS n 
1 28  ASP n 
1 29  THR n 
1 30  TYR n 
1 31  LEU n 
1 32  SER n 
1 33  HIS n 
1 34  PHE n 
1 35  ASN n 
1 36  PRO n 
1 37  ARG n 
1 38  ASP n 
1 39  TYR n 
1 40  LEU n 
1 41  GLU n 
1 42  LYS n 
1 43  TYR n 
1 44  TYR n 
1 45  LYS n 
1 46  PHE n 
1 47  GLY n 
1 48  SER n 
1 49  ARG n 
1 50  HIS n 
1 51  SER n 
1 52  ALA n 
1 53  GLU n 
1 54  SER n 
1 55  GLN n 
1 56  ILE n 
1 57  LEU n 
1 58  LYS n 
1 59  HIS n 
1 60  LEU n 
1 61  LEU n 
1 62  LYS n 
1 63  ASN n 
1 64  LEU n 
1 65  PHE n 
1 66  LYS n 
1 67  ILE n 
1 68  PHE n 
1 69  CYS n 
1 70  LEU n 
1 71  ASP n 
1 72  GLY n 
1 73  VAL n 
1 74  LYS n 
1 75  GLY n 
1 76  ASP n 
1 77  LEU n 
1 78  LEU n 
1 79  ILE n 
1 80  ASP n 
1 81  ILE n 
1 82  GLY n 
1 83  SER n 
1 84  GLY n 
1 85  PRO n 
1 86  THR n 
1 87  ILE n 
1 88  TYR n 
1 89  GLN n 
1 90  LEU n 
1 91  LEU n 
1 92  SER n 
1 93  ALA n 
1 94  CYS n 
1 95  GLU n 
1 96  SER n 
1 97  PHE n 
1 98  LYS n 
1 99  GLU n 
1 100 ILE n 
1 101 VAL n 
1 102 VAL n 
1 103 THR n 
1 104 ASP n 
1 105 TYR n 
1 106 SER n 
1 107 ASP n 
1 108 GLN n 
1 109 ASN n 
1 110 LEU n 
1 111 GLN n 
1 112 GLU n 
1 113 LEU n 
1 114 GLU n 
1 115 LYS n 
1 116 TRP n 
1 117 LEU n 
1 118 LYS n 
1 119 ALA n 
1 120 ALA n 
1 121 PRO n 
1 122 ALA n 
1 123 ALA n 
1 124 PHE n 
1 125 ASP n 
1 126 TRP n 
1 127 SER n 
1 128 PRO n 
1 129 VAL n 
1 130 VAL n 
1 131 THR n 
1 132 TYR n 
1 133 VAL n 
1 134 CYS n 
1 135 ASP n 
1 136 LEU n 
1 137 GLU n 
1 138 GLY n 
1 139 ASN n 
1 140 ARG n 
1 141 VAL n 
1 142 LYS n 
1 143 GLY n 
1 144 PRO n 
1 145 GLU n 
1 146 LYS n 
1 147 GLU n 
1 148 GLU n 
1 149 LYS n 
1 150 LEU n 
1 151 ARG n 
1 152 GLN n 
1 153 ALA n 
1 154 VAL n 
1 155 LYS n 
1 156 GLN n 
1 157 VAL n 
1 158 LEU n 
1 159 LYS n 
1 160 CYS n 
1 161 ASP n 
1 162 VAL n 
1 163 THR n 
1 164 GLN n 
1 165 SER n 
1 166 GLN n 
1 167 PRO n 
1 168 LEU n 
1 169 GLY n 
1 170 ALA n 
1 171 VAL n 
1 172 PRO n 
1 173 LEU n 
1 174 PRO n 
1 175 PRO n 
1 176 ALA n 
1 177 ASP n 
1 178 CYS n 
1 179 VAL n 
1 180 LEU n 
1 181 SER n 
1 182 THR n 
1 183 LEU n 
1 184 CYS n 
1 185 LEU n 
1 186 ASP n 
1 187 ALA n 
1 188 ALA n 
1 189 CYS n 
1 190 PRO n 
1 191 ASP n 
1 192 LEU n 
1 193 PRO n 
1 194 THR n 
1 195 TYR n 
1 196 CYS n 
1 197 ARG n 
1 198 ALA n 
1 199 LEU n 
1 200 ARG n 
1 201 ASN n 
1 202 LEU n 
1 203 GLY n 
1 204 SER n 
1 205 LEU n 
1 206 LEU n 
1 207 LYS n 
1 208 PRO n 
1 209 GLY n 
1 210 GLY n 
1 211 PHE n 
1 212 LEU n 
1 213 VAL n 
1 214 ILE n 
1 215 MET n 
1 216 ASP n 
1 217 ALA n 
1 218 LEU n 
1 219 LYS n 
1 220 SER n 
1 221 SER n 
1 222 TYR n 
1 223 TYR n 
1 224 MET n 
1 225 ILE n 
1 226 GLY n 
1 227 GLU n 
1 228 GLN n 
1 229 LYS n 
1 230 PHE n 
1 231 SER n 
1 232 SER n 
1 233 LEU n 
1 234 PRO n 
1 235 LEU n 
1 236 GLY n 
1 237 ARG n 
1 238 GLU n 
1 239 ALA n 
1 240 VAL n 
1 241 GLU n 
1 242 ALA n 
1 243 ALA n 
1 244 VAL n 
1 245 LYS n 
1 246 GLU n 
1 247 ALA n 
1 248 GLY n 
1 249 TYR n 
1 250 THR n 
1 251 ILE n 
1 252 GLU n 
1 253 TRP n 
1 254 PHE n 
1 255 GLU n 
1 256 VAL n 
1 257 ILE n 
1 258 SER n 
1 259 GLN n 
1 260 SER n 
1 261 TYR n 
1 262 SER n 
1 263 SER n 
1 264 THR n 
1 265 MET n 
1 266 ALA n 
1 267 ASN n 
1 268 ASN n 
1 269 GLU n 
1 270 GLY n 
1 271 LEU n 
1 272 PHE n 
1 273 SER n 
1 274 LEU n 
1 275 VAL n 
1 276 ALA n 
1 277 ARG n 
1 278 LYS n 
1 279 LEU n 
1 280 SER 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                   280 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 NNMT 
_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-Pichia pastoris shuttle vector pPpARG4' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     1182032 
_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 
A1IPM non-polymer         . '1,4-dimethyl-6-(methylamino)pyridine-3-carboxamide' ? 'C9 H14 N3 O 1'   180.227 
ALA   'L-peptide linking' y ALANINE                                              ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                             ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                           ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                      ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                                             ? 'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE                                            ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                      ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                              ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                            ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                           ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                              ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                               ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                           ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                        ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                              ? 'C5 H9 N O2'      115.130 
SAH   non-polymer         . S-ADENOSYL-L-HOMOCYSTEINE                            ? 'C14 H20 N6 O5 S' 384.411 
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   HIS 1   -18 ?   ?   ?   B . n 
A 1 2   ASN 2   -17 ?   ?   ?   B . n 
A 1 3   HIS 3   -16 ?   ?   ?   B . n 
A 1 4   ASN 4   -15 ?   ?   ?   B . n 
A 1 5   HIS 5   -14 ?   ?   ?   B . n 
A 1 6   ASN 6   -13 ?   ?   ?   B . n 
A 1 7   HIS 7   -12 ?   ?   ?   B . n 
A 1 8   ASN 8   -11 ?   ?   ?   B . n 
A 1 9   HIS 9   -10 ?   ?   ?   B . n 
A 1 10  ASN 10  -9  ?   ?   ?   B . n 
A 1 11  HIS 11  -8  ?   ?   ?   B . n 
A 1 12  ASN 12  -7  ?   ?   ?   B . n 
A 1 13  ALA 13  -6  ?   ?   ?   B . n 
A 1 14  ALA 14  -5  ?   ?   ?   B . n 
A 1 15  ALA 15  -4  ?   ?   ?   B . n 
A 1 16  GLU 16  -3  ?   ?   ?   B . n 
A 1 17  ASN 17  -2  ?   ?   ?   B . n 
A 1 18  LEU 18  -1  ?   ?   ?   B . n 
A 1 19  TYR 19  0   ?   ?   ?   B . n 
A 1 20  PHE 20  1   ?   ?   ?   B . n 
A 1 21  GLN 21  2   ?   ?   ?   B . n 
A 1 22  SER 22  3   ?   ?   ?   B . n 
A 1 23  GLY 23  4   ?   ?   ?   B . n 
A 1 24  PHE 24  5   5   PHE PHE B . n 
A 1 25  THR 25  6   6   THR THR B . n 
A 1 26  SER 26  7   7   SER SER B . n 
A 1 27  LYS 27  8   8   LYS LYS B . n 
A 1 28  ASP 28  9   9   ASP ASP B . n 
A 1 29  THR 29  10  10  THR THR B . n 
A 1 30  TYR 30  11  11  TYR TYR B . n 
A 1 31  LEU 31  12  12  LEU LEU B . n 
A 1 32  SER 32  13  13  SER SER B . n 
A 1 33  HIS 33  14  14  HIS HIS B . n 
A 1 34  PHE 34  15  15  PHE PHE B . n 
A 1 35  ASN 35  16  16  ASN ASN B . n 
A 1 36  PRO 36  17  17  PRO PRO B . n 
A 1 37  ARG 37  18  18  ARG ARG B . n 
A 1 38  ASP 38  19  19  ASP ASP B . n 
A 1 39  TYR 39  20  20  TYR TYR B . n 
A 1 40  LEU 40  21  21  LEU LEU B . n 
A 1 41  GLU 41  22  22  GLU GLU B . n 
A 1 42  LYS 42  23  23  LYS LYS B . n 
A 1 43  TYR 43  24  24  TYR TYR B . n 
A 1 44  TYR 44  25  25  TYR TYR B . n 
A 1 45  LYS 45  26  ?   ?   ?   B . n 
A 1 46  PHE 46  27  ?   ?   ?   B . n 
A 1 47  GLY 47  28  ?   ?   ?   B . n 
A 1 48  SER 48  29  ?   ?   ?   B . n 
A 1 49  ARG 49  30  ?   ?   ?   B . n 
A 1 50  HIS 50  31  ?   ?   ?   B . n 
A 1 51  SER 51  32  ?   ?   ?   B . n 
A 1 52  ALA 52  33  ?   ?   ?   B . n 
A 1 53  GLU 53  34  34  GLU GLU B . n 
A 1 54  SER 54  35  35  SER SER B . n 
A 1 55  GLN 55  36  36  GLN GLN B . n 
A 1 56  ILE 56  37  37  ILE ILE B . n 
A 1 57  LEU 57  38  38  LEU LEU B . n 
A 1 58  LYS 58  39  39  LYS LYS B . n 
A 1 59  HIS 59  40  40  HIS HIS B . n 
A 1 60  LEU 60  41  41  LEU LEU B . n 
A 1 61  LEU 61  42  42  LEU LEU B . n 
A 1 62  LYS 62  43  43  LYS LYS B . n 
A 1 63  ASN 63  44  44  ASN ASN B . n 
A 1 64  LEU 64  45  45  LEU LEU B . n 
A 1 65  PHE 65  46  46  PHE PHE B . n 
A 1 66  LYS 66  47  47  LYS LYS B . n 
A 1 67  ILE 67  48  48  ILE ILE B . n 
A 1 68  PHE 68  49  49  PHE PHE B . n 
A 1 69  CYS 69  50  50  CYS CYS B . n 
A 1 70  LEU 70  51  51  LEU LEU B . n 
A 1 71  ASP 71  52  ?   ?   ?   B . n 
A 1 72  GLY 72  53  53  GLY GLY B . n 
A 1 73  VAL 73  54  54  VAL VAL B . n 
A 1 74  LYS 74  55  55  LYS LYS B . n 
A 1 75  GLY 75  56  56  GLY GLY B . n 
A 1 76  ASP 76  57  57  ASP ASP B . n 
A 1 77  LEU 77  58  58  LEU LEU B . n 
A 1 78  LEU 78  59  59  LEU LEU B . n 
A 1 79  ILE 79  60  60  ILE ILE B . n 
A 1 80  ASP 80  61  61  ASP ASP B . n 
A 1 81  ILE 81  62  62  ILE ILE B . n 
A 1 82  GLY 82  63  63  GLY GLY B . n 
A 1 83  SER 83  64  64  SER SER B . n 
A 1 84  GLY 84  65  65  GLY GLY B . n 
A 1 85  PRO 85  66  66  PRO PRO B . n 
A 1 86  THR 86  67  67  THR THR B . n 
A 1 87  ILE 87  68  68  ILE ILE B . n 
A 1 88  TYR 88  69  69  TYR TYR B . n 
A 1 89  GLN 89  70  70  GLN GLN B . n 
A 1 90  LEU 90  71  71  LEU LEU B . n 
A 1 91  LEU 91  72  72  LEU LEU B . n 
A 1 92  SER 92  73  73  SER SER B . n 
A 1 93  ALA 93  74  74  ALA ALA B . n 
A 1 94  CYS 94  75  75  CYS CYS B . n 
A 1 95  GLU 95  76  76  GLU GLU B . n 
A 1 96  SER 96  77  77  SER SER B . n 
A 1 97  PHE 97  78  78  PHE PHE B . n 
A 1 98  LYS 98  79  79  LYS LYS B . n 
A 1 99  GLU 99  80  80  GLU GLU B . n 
A 1 100 ILE 100 81  81  ILE ILE B . n 
A 1 101 VAL 101 82  82  VAL VAL B . n 
A 1 102 VAL 102 83  83  VAL VAL B . n 
A 1 103 THR 103 84  84  THR THR B . n 
A 1 104 ASP 104 85  85  ASP ASP B . n 
A 1 105 TYR 105 86  86  TYR TYR B . n 
A 1 106 SER 106 87  87  SER SER B . n 
A 1 107 ASP 107 88  88  ASP ASP B . n 
A 1 108 GLN 108 89  89  GLN GLN B . n 
A 1 109 ASN 109 90  90  ASN ASN B . n 
A 1 110 LEU 110 91  91  LEU LEU B . n 
A 1 111 GLN 111 92  92  GLN GLN B . n 
A 1 112 GLU 112 93  93  GLU GLU B . n 
A 1 113 LEU 113 94  94  LEU LEU B . n 
A 1 114 GLU 114 95  95  GLU GLU B . n 
A 1 115 LYS 115 96  96  LYS LYS B . n 
A 1 116 TRP 116 97  97  TRP TRP B . n 
A 1 117 LEU 117 98  98  LEU LEU B . n 
A 1 118 LYS 118 99  99  LYS LYS B . n 
A 1 119 ALA 119 100 100 ALA ALA B . n 
A 1 120 ALA 120 101 101 ALA ALA B . n 
A 1 121 PRO 121 102 102 PRO PRO B . n 
A 1 122 ALA 122 103 103 ALA ALA B . n 
A 1 123 ALA 123 104 104 ALA ALA B . n 
A 1 124 PHE 124 105 105 PHE PHE B . n 
A 1 125 ASP 125 106 106 ASP ASP B . n 
A 1 126 TRP 126 107 107 TRP TRP B . n 
A 1 127 SER 127 108 108 SER SER B . n 
A 1 128 PRO 128 109 109 PRO PRO B . n 
A 1 129 VAL 129 110 110 VAL VAL B . n 
A 1 130 VAL 130 111 111 VAL VAL B . n 
A 1 131 THR 131 112 112 THR THR B . n 
A 1 132 TYR 132 113 113 TYR TYR B . n 
A 1 133 VAL 133 114 114 VAL VAL B . n 
A 1 134 CYS 134 115 115 CYS CYS B . n 
A 1 135 ASP 135 116 116 ASP ASP B . n 
A 1 136 LEU 136 117 117 LEU LEU B . n 
A 1 137 GLU 137 118 118 GLU GLU B . n 
A 1 138 GLY 138 119 119 GLY GLY B . n 
A 1 139 ASN 139 120 120 ASN ASN B . n 
A 1 140 ARG 140 121 121 ARG ARG B . n 
A 1 141 VAL 141 122 122 VAL VAL B . n 
A 1 142 LYS 142 123 123 LYS LYS B . n 
A 1 143 GLY 143 124 124 GLY GLY B . n 
A 1 144 PRO 144 125 125 PRO PRO B . n 
A 1 145 GLU 145 126 126 GLU GLU B . n 
A 1 146 LYS 146 127 127 LYS LYS B . n 
A 1 147 GLU 147 128 128 GLU GLU B . n 
A 1 148 GLU 148 129 129 GLU GLU B . n 
A 1 149 LYS 149 130 130 LYS LYS B . n 
A 1 150 LEU 150 131 131 LEU LEU B . n 
A 1 151 ARG 151 132 132 ARG ARG B . n 
A 1 152 GLN 152 133 133 GLN GLN B . n 
A 1 153 ALA 153 134 134 ALA ALA B . n 
A 1 154 VAL 154 135 135 VAL VAL B . n 
A 1 155 LYS 155 136 136 LYS LYS B . n 
A 1 156 GLN 156 137 137 GLN GLN B . n 
A 1 157 VAL 157 138 138 VAL VAL B . n 
A 1 158 LEU 158 139 139 LEU LEU B . n 
A 1 159 LYS 159 140 140 LYS LYS B . n 
A 1 160 CYS 160 141 141 CYS CYS B . n 
A 1 161 ASP 161 142 142 ASP ASP B . n 
A 1 162 VAL 162 143 143 VAL VAL B . n 
A 1 163 THR 163 144 144 THR THR B . n 
A 1 164 GLN 164 145 145 GLN GLN B . n 
A 1 165 SER 165 146 146 SER SER B . n 
A 1 166 GLN 166 147 147 GLN GLN B . n 
A 1 167 PRO 167 148 148 PRO PRO B . n 
A 1 168 LEU 168 149 149 LEU LEU B . n 
A 1 169 GLY 169 150 150 GLY GLY B . n 
A 1 170 ALA 170 151 151 ALA ALA B . n 
A 1 171 VAL 171 152 152 VAL VAL B . n 
A 1 172 PRO 172 153 153 PRO PRO B . n 
A 1 173 LEU 173 154 154 LEU LEU B . n 
A 1 174 PRO 174 155 155 PRO PRO B . n 
A 1 175 PRO 175 156 156 PRO PRO B . n 
A 1 176 ALA 176 157 157 ALA ALA B . n 
A 1 177 ASP 177 158 158 ASP ASP B . n 
A 1 178 CYS 178 159 159 CYS CYS B . n 
A 1 179 VAL 179 160 160 VAL VAL B . n 
A 1 180 LEU 180 161 161 LEU LEU B . n 
A 1 181 SER 181 162 162 SER SER B . n 
A 1 182 THR 182 163 163 THR THR B . n 
A 1 183 LEU 183 164 164 LEU LEU B . n 
A 1 184 CYS 184 165 165 CYS CYS B . n 
A 1 185 LEU 185 166 166 LEU LEU B . n 
A 1 186 ASP 186 167 167 ASP ASP B . n 
A 1 187 ALA 187 168 168 ALA ALA B . n 
A 1 188 ALA 188 169 169 ALA ALA B . n 
A 1 189 CYS 189 170 170 CYS CYS B . n 
A 1 190 PRO 190 171 171 PRO PRO B . n 
A 1 191 ASP 191 172 172 ASP ASP B . n 
A 1 192 LEU 192 173 173 LEU LEU B . n 
A 1 193 PRO 193 174 174 PRO PRO B . n 
A 1 194 THR 194 175 175 THR THR B . n 
A 1 195 TYR 195 176 176 TYR TYR B . n 
A 1 196 CYS 196 177 177 CYS CYS B . n 
A 1 197 ARG 197 178 178 ARG ARG B . n 
A 1 198 ALA 198 179 179 ALA ALA B . n 
A 1 199 LEU 199 180 180 LEU LEU B . n 
A 1 200 ARG 200 181 181 ARG ARG B . n 
A 1 201 ASN 201 182 182 ASN ASN B . n 
A 1 202 LEU 202 183 183 LEU LEU B . n 
A 1 203 GLY 203 184 184 GLY GLY B . n 
A 1 204 SER 204 185 185 SER SER B . n 
A 1 205 LEU 205 186 186 LEU LEU B . n 
A 1 206 LEU 206 187 187 LEU LEU B . n 
A 1 207 LYS 207 188 188 LYS LYS B . n 
A 1 208 PRO 208 189 189 PRO PRO B . n 
A 1 209 GLY 209 190 190 GLY GLY B . n 
A 1 210 GLY 210 191 191 GLY GLY B . n 
A 1 211 PHE 211 192 192 PHE PHE B . n 
A 1 212 LEU 212 193 193 LEU LEU B . n 
A 1 213 VAL 213 194 194 VAL VAL B . n 
A 1 214 ILE 214 195 195 ILE ILE B . n 
A 1 215 MET 215 196 196 MET MET B . n 
A 1 216 ASP 216 197 197 ASP ASP B . n 
A 1 217 ALA 217 198 198 ALA ALA B . n 
A 1 218 LEU 218 199 199 LEU LEU B . n 
A 1 219 LYS 219 200 200 LYS LYS B . n 
A 1 220 SER 220 201 201 SER SER B . n 
A 1 221 SER 221 202 202 SER SER B . n 
A 1 222 TYR 222 203 203 TYR TYR B . n 
A 1 223 TYR 223 204 204 TYR TYR B . n 
A 1 224 MET 224 205 205 MET MET B . n 
A 1 225 ILE 225 206 206 ILE ILE B . n 
A 1 226 GLY 226 207 207 GLY GLY B . n 
A 1 227 GLU 227 208 208 GLU GLU B . n 
A 1 228 GLN 228 209 209 GLN GLN B . n 
A 1 229 LYS 229 210 210 LYS LYS B . n 
A 1 230 PHE 230 211 211 PHE PHE B . n 
A 1 231 SER 231 212 212 SER SER B . n 
A 1 232 SER 232 213 213 SER SER B . n 
A 1 233 LEU 233 214 214 LEU LEU B . n 
A 1 234 PRO 234 215 215 PRO PRO B . n 
A 1 235 LEU 235 216 216 LEU LEU B . n 
A 1 236 GLY 236 217 217 GLY GLY B . n 
A 1 237 ARG 237 218 218 ARG ARG B . n 
A 1 238 GLU 238 219 219 GLU GLU B . n 
A 1 239 ALA 239 220 220 ALA ALA B . n 
A 1 240 VAL 240 221 221 VAL VAL B . n 
A 1 241 GLU 241 222 222 GLU GLU B . n 
A 1 242 ALA 242 223 223 ALA ALA B . n 
A 1 243 ALA 243 224 224 ALA ALA B . n 
A 1 244 VAL 244 225 225 VAL VAL B . n 
A 1 245 LYS 245 226 226 LYS LYS B . n 
A 1 246 GLU 246 227 227 GLU GLU B . n 
A 1 247 ALA 247 228 228 ALA ALA B . n 
A 1 248 GLY 248 229 229 GLY GLY B . n 
A 1 249 TYR 249 230 230 TYR TYR B . n 
A 1 250 THR 250 231 231 THR THR B . n 
A 1 251 ILE 251 232 232 ILE ILE B . n 
A 1 252 GLU 252 233 233 GLU GLU B . n 
A 1 253 TRP 253 234 234 TRP TRP B . n 
A 1 254 PHE 254 235 235 PHE PHE B . n 
A 1 255 GLU 255 236 236 GLU GLU B . n 
A 1 256 VAL 256 237 237 VAL VAL B . n 
A 1 257 ILE 257 238 238 ILE ILE B . n 
A 1 258 SER 258 239 239 SER SER B . n 
A 1 259 GLN 259 240 240 GLN GLN B . n 
A 1 260 SER 260 241 241 SER SER B . n 
A 1 261 TYR 261 242 242 TYR TYR B . n 
A 1 262 SER 262 243 243 SER SER B . n 
A 1 263 SER 263 244 244 SER SER B . n 
A 1 264 THR 264 245 245 THR THR B . n 
A 1 265 MET 265 246 246 MET MET B . n 
A 1 266 ALA 266 247 247 ALA ALA B . n 
A 1 267 ASN 267 248 248 ASN ASN B . n 
A 1 268 ASN 268 249 249 ASN ASN B . n 
A 1 269 GLU 269 250 250 GLU GLU B . n 
A 1 270 GLY 270 251 251 GLY GLY B . n 
A 1 271 LEU 271 252 252 LEU LEU B . n 
A 1 272 PHE 272 253 253 PHE PHE B . n 
A 1 273 SER 273 254 254 SER SER B . n 
A 1 274 LEU 274 255 255 LEU LEU B . n 
A 1 275 VAL 275 256 256 VAL VAL B . n 
A 1 276 ALA 276 257 257 ALA ALA B . n 
A 1 277 ARG 277 258 258 ARG ARG B . n 
A 1 278 LYS 278 259 259 LYS LYS B . n 
A 1 279 LEU 279 260 260 LEU LEU B . n 
A 1 280 SER 280 261 ?   ?   ?   B . n 
B 1 1   HIS 1   -18 ?   ?   ?   D . n 
B 1 2   ASN 2   -17 ?   ?   ?   D . n 
B 1 3   HIS 3   -16 ?   ?   ?   D . n 
B 1 4   ASN 4   -15 ?   ?   ?   D . n 
B 1 5   HIS 5   -14 ?   ?   ?   D . n 
B 1 6   ASN 6   -13 ?   ?   ?   D . n 
B 1 7   HIS 7   -12 ?   ?   ?   D . n 
B 1 8   ASN 8   -11 ?   ?   ?   D . n 
B 1 9   HIS 9   -10 ?   ?   ?   D . n 
B 1 10  ASN 10  -9  ?   ?   ?   D . n 
B 1 11  HIS 11  -8  ?   ?   ?   D . n 
B 1 12  ASN 12  -7  ?   ?   ?   D . n 
B 1 13  ALA 13  -6  ?   ?   ?   D . n 
B 1 14  ALA 14  -5  ?   ?   ?   D . n 
B 1 15  ALA 15  -4  ?   ?   ?   D . n 
B 1 16  GLU 16  -3  ?   ?   ?   D . n 
B 1 17  ASN 17  -2  ?   ?   ?   D . n 
B 1 18  LEU 18  -1  ?   ?   ?   D . n 
B 1 19  TYR 19  0   ?   ?   ?   D . n 
B 1 20  PHE 20  1   ?   ?   ?   D . n 
B 1 21  GLN 21  2   ?   ?   ?   D . n 
B 1 22  SER 22  3   ?   ?   ?   D . n 
B 1 23  GLY 23  4   ?   ?   ?   D . n 
B 1 24  PHE 24  5   5   PHE PHE D . n 
B 1 25  THR 25  6   6   THR THR D . n 
B 1 26  SER 26  7   7   SER SER D . n 
B 1 27  LYS 27  8   8   LYS LYS D . n 
B 1 28  ASP 28  9   9   ASP ASP D . n 
B 1 29  THR 29  10  10  THR THR D . n 
B 1 30  TYR 30  11  11  TYR TYR D . n 
B 1 31  LEU 31  12  12  LEU LEU D . n 
B 1 32  SER 32  13  13  SER SER D . n 
B 1 33  HIS 33  14  14  HIS HIS D . n 
B 1 34  PHE 34  15  15  PHE PHE D . n 
B 1 35  ASN 35  16  16  ASN ASN D . n 
B 1 36  PRO 36  17  17  PRO PRO D . n 
B 1 37  ARG 37  18  18  ARG ARG D . n 
B 1 38  ASP 38  19  19  ASP ASP D . n 
B 1 39  TYR 39  20  20  TYR TYR D . n 
B 1 40  LEU 40  21  21  LEU LEU D . n 
B 1 41  GLU 41  22  22  GLU GLU D . n 
B 1 42  LYS 42  23  23  LYS LYS D . n 
B 1 43  TYR 43  24  24  TYR TYR D . n 
B 1 44  TYR 44  25  25  TYR TYR D . n 
B 1 45  LYS 45  26  26  LYS LYS D . n 
B 1 46  PHE 46  27  27  PHE PHE D . n 
B 1 47  GLY 47  28  ?   ?   ?   D . n 
B 1 48  SER 48  29  ?   ?   ?   D . n 
B 1 49  ARG 49  30  ?   ?   ?   D . n 
B 1 50  HIS 50  31  ?   ?   ?   D . n 
B 1 51  SER 51  32  ?   ?   ?   D . n 
B 1 52  ALA 52  33  ?   ?   ?   D . n 
B 1 53  GLU 53  34  34  GLU GLU D . n 
B 1 54  SER 54  35  35  SER SER D . n 
B 1 55  GLN 55  36  36  GLN GLN D . n 
B 1 56  ILE 56  37  37  ILE ILE D . n 
B 1 57  LEU 57  38  38  LEU LEU D . n 
B 1 58  LYS 58  39  39  LYS LYS D . n 
B 1 59  HIS 59  40  40  HIS HIS D . n 
B 1 60  LEU 60  41  41  LEU LEU D . n 
B 1 61  LEU 61  42  42  LEU LEU D . n 
B 1 62  LYS 62  43  43  LYS LYS D . n 
B 1 63  ASN 63  44  44  ASN ASN D . n 
B 1 64  LEU 64  45  45  LEU LEU D . n 
B 1 65  PHE 65  46  46  PHE PHE D . n 
B 1 66  LYS 66  47  47  LYS LYS D . n 
B 1 67  ILE 67  48  48  ILE ILE D . n 
B 1 68  PHE 68  49  49  PHE PHE D . n 
B 1 69  CYS 69  50  50  CYS CYS D . n 
B 1 70  LEU 70  51  51  LEU LEU D . n 
B 1 71  ASP 71  52  ?   ?   ?   D . n 
B 1 72  GLY 72  53  53  GLY GLY D . n 
B 1 73  VAL 73  54  54  VAL VAL D . n 
B 1 74  LYS 74  55  55  LYS LYS D . n 
B 1 75  GLY 75  56  56  GLY GLY D . n 
B 1 76  ASP 76  57  57  ASP ASP D . n 
B 1 77  LEU 77  58  58  LEU LEU D . n 
B 1 78  LEU 78  59  59  LEU LEU D . n 
B 1 79  ILE 79  60  60  ILE ILE D . n 
B 1 80  ASP 80  61  61  ASP ASP D . n 
B 1 81  ILE 81  62  62  ILE ILE D . n 
B 1 82  GLY 82  63  63  GLY GLY D . n 
B 1 83  SER 83  64  64  SER SER D . n 
B 1 84  GLY 84  65  65  GLY GLY D . n 
B 1 85  PRO 85  66  66  PRO PRO D . n 
B 1 86  THR 86  67  67  THR THR D . n 
B 1 87  ILE 87  68  68  ILE ILE D . n 
B 1 88  TYR 88  69  69  TYR TYR D . n 
B 1 89  GLN 89  70  70  GLN GLN D . n 
B 1 90  LEU 90  71  71  LEU LEU D . n 
B 1 91  LEU 91  72  72  LEU LEU D . n 
B 1 92  SER 92  73  73  SER SER D . n 
B 1 93  ALA 93  74  74  ALA ALA D . n 
B 1 94  CYS 94  75  75  CYS CYS D . n 
B 1 95  GLU 95  76  76  GLU GLU D . n 
B 1 96  SER 96  77  77  SER SER D . n 
B 1 97  PHE 97  78  78  PHE PHE D . n 
B 1 98  LYS 98  79  79  LYS LYS D . n 
B 1 99  GLU 99  80  80  GLU GLU D . n 
B 1 100 ILE 100 81  81  ILE ILE D . n 
B 1 101 VAL 101 82  82  VAL VAL D . n 
B 1 102 VAL 102 83  83  VAL VAL D . n 
B 1 103 THR 103 84  84  THR THR D . n 
B 1 104 ASP 104 85  85  ASP ASP D . n 
B 1 105 TYR 105 86  86  TYR TYR D . n 
B 1 106 SER 106 87  87  SER SER D . n 
B 1 107 ASP 107 88  88  ASP ASP D . n 
B 1 108 GLN 108 89  89  GLN GLN D . n 
B 1 109 ASN 109 90  90  ASN ASN D . n 
B 1 110 LEU 110 91  91  LEU LEU D . n 
B 1 111 GLN 111 92  92  GLN GLN D . n 
B 1 112 GLU 112 93  93  GLU GLU D . n 
B 1 113 LEU 113 94  94  LEU LEU D . n 
B 1 114 GLU 114 95  95  GLU GLU D . n 
B 1 115 LYS 115 96  96  LYS LYS D . n 
B 1 116 TRP 116 97  97  TRP TRP D . n 
B 1 117 LEU 117 98  98  LEU LEU D . n 
B 1 118 LYS 118 99  99  LYS LYS D . n 
B 1 119 ALA 119 100 100 ALA ALA D . n 
B 1 120 ALA 120 101 101 ALA ALA D . n 
B 1 121 PRO 121 102 102 PRO PRO D . n 
B 1 122 ALA 122 103 103 ALA ALA D . n 
B 1 123 ALA 123 104 104 ALA ALA D . n 
B 1 124 PHE 124 105 105 PHE PHE D . n 
B 1 125 ASP 125 106 106 ASP ASP D . n 
B 1 126 TRP 126 107 107 TRP TRP D . n 
B 1 127 SER 127 108 108 SER SER D . n 
B 1 128 PRO 128 109 109 PRO PRO D . n 
B 1 129 VAL 129 110 110 VAL VAL D . n 
B 1 130 VAL 130 111 111 VAL VAL D . n 
B 1 131 THR 131 112 112 THR THR D . n 
B 1 132 TYR 132 113 113 TYR TYR D . n 
B 1 133 VAL 133 114 114 VAL VAL D . n 
B 1 134 CYS 134 115 115 CYS CYS D . n 
B 1 135 ASP 135 116 116 ASP ASP D . n 
B 1 136 LEU 136 117 117 LEU LEU D . n 
B 1 137 GLU 137 118 118 GLU GLU D . n 
B 1 138 GLY 138 119 119 GLY GLY D . n 
B 1 139 ASN 139 120 120 ASN ASN D . n 
B 1 140 ARG 140 121 121 ARG ARG D . n 
B 1 141 VAL 141 122 122 VAL VAL D . n 
B 1 142 LYS 142 123 123 LYS LYS D . n 
B 1 143 GLY 143 124 124 GLY GLY D . n 
B 1 144 PRO 144 125 125 PRO PRO D . n 
B 1 145 GLU 145 126 126 GLU GLU D . n 
B 1 146 LYS 146 127 127 LYS LYS D . n 
B 1 147 GLU 147 128 128 GLU GLU D . n 
B 1 148 GLU 148 129 129 GLU GLU D . n 
B 1 149 LYS 149 130 130 LYS LYS D . n 
B 1 150 LEU 150 131 131 LEU LEU D . n 
B 1 151 ARG 151 132 132 ARG ARG D . n 
B 1 152 GLN 152 133 133 GLN GLN D . n 
B 1 153 ALA 153 134 134 ALA ALA D . n 
B 1 154 VAL 154 135 135 VAL VAL D . n 
B 1 155 LYS 155 136 136 LYS LYS D . n 
B 1 156 GLN 156 137 137 GLN GLN D . n 
B 1 157 VAL 157 138 138 VAL VAL D . n 
B 1 158 LEU 158 139 139 LEU LEU D . n 
B 1 159 LYS 159 140 140 LYS LYS D . n 
B 1 160 CYS 160 141 141 CYS CYS D . n 
B 1 161 ASP 161 142 142 ASP ASP D . n 
B 1 162 VAL 162 143 143 VAL VAL D . n 
B 1 163 THR 163 144 144 THR THR D . n 
B 1 164 GLN 164 145 145 GLN GLN D . n 
B 1 165 SER 165 146 146 SER SER D . n 
B 1 166 GLN 166 147 147 GLN GLN D . n 
B 1 167 PRO 167 148 148 PRO PRO D . n 
B 1 168 LEU 168 149 149 LEU LEU D . n 
B 1 169 GLY 169 150 150 GLY GLY D . n 
B 1 170 ALA 170 151 151 ALA ALA D . n 
B 1 171 VAL 171 152 152 VAL VAL D . n 
B 1 172 PRO 172 153 153 PRO PRO D . n 
B 1 173 LEU 173 154 154 LEU LEU D . n 
B 1 174 PRO 174 155 155 PRO PRO D . n 
B 1 175 PRO 175 156 156 PRO PRO D . n 
B 1 176 ALA 176 157 157 ALA ALA D . n 
B 1 177 ASP 177 158 158 ASP ASP D . n 
B 1 178 CYS 178 159 159 CYS CYS D . n 
B 1 179 VAL 179 160 160 VAL VAL D . n 
B 1 180 LEU 180 161 161 LEU LEU D . n 
B 1 181 SER 181 162 162 SER SER D . n 
B 1 182 THR 182 163 163 THR THR D . n 
B 1 183 LEU 183 164 164 LEU LEU D . n 
B 1 184 CYS 184 165 165 CYS CYS D . n 
B 1 185 LEU 185 166 166 LEU LEU D . n 
B 1 186 ASP 186 167 167 ASP ASP D . n 
B 1 187 ALA 187 168 168 ALA ALA D . n 
B 1 188 ALA 188 169 169 ALA ALA D . n 
B 1 189 CYS 189 170 170 CYS CYS D . n 
B 1 190 PRO 190 171 171 PRO PRO D . n 
B 1 191 ASP 191 172 172 ASP ASP D . n 
B 1 192 LEU 192 173 173 LEU LEU D . n 
B 1 193 PRO 193 174 174 PRO PRO D . n 
B 1 194 THR 194 175 175 THR THR D . n 
B 1 195 TYR 195 176 176 TYR TYR D . n 
B 1 196 CYS 196 177 177 CYS CYS D . n 
B 1 197 ARG 197 178 178 ARG ARG D . n 
B 1 198 ALA 198 179 179 ALA ALA D . n 
B 1 199 LEU 199 180 180 LEU LEU D . n 
B 1 200 ARG 200 181 181 ARG ARG D . n 
B 1 201 ASN 201 182 182 ASN ASN D . n 
B 1 202 LEU 202 183 183 LEU LEU D . n 
B 1 203 GLY 203 184 184 GLY GLY D . n 
B 1 204 SER 204 185 185 SER SER D . n 
B 1 205 LEU 205 186 186 LEU LEU D . n 
B 1 206 LEU 206 187 187 LEU LEU D . n 
B 1 207 LYS 207 188 188 LYS LYS D . n 
B 1 208 PRO 208 189 189 PRO PRO D . n 
B 1 209 GLY 209 190 190 GLY GLY D . n 
B 1 210 GLY 210 191 191 GLY GLY D . n 
B 1 211 PHE 211 192 192 PHE PHE D . n 
B 1 212 LEU 212 193 193 LEU LEU D . n 
B 1 213 VAL 213 194 194 VAL VAL D . n 
B 1 214 ILE 214 195 195 ILE ILE D . n 
B 1 215 MET 215 196 196 MET MET D . n 
B 1 216 ASP 216 197 197 ASP ASP D . n 
B 1 217 ALA 217 198 198 ALA ALA D . n 
B 1 218 LEU 218 199 199 LEU LEU D . n 
B 1 219 LYS 219 200 200 LYS LYS D . n 
B 1 220 SER 220 201 201 SER SER D . n 
B 1 221 SER 221 202 202 SER SER D . n 
B 1 222 TYR 222 203 203 TYR TYR D . n 
B 1 223 TYR 223 204 204 TYR TYR D . n 
B 1 224 MET 224 205 205 MET MET D . n 
B 1 225 ILE 225 206 206 ILE ILE D . n 
B 1 226 GLY 226 207 207 GLY GLY D . n 
B 1 227 GLU 227 208 208 GLU GLU D . n 
B 1 228 GLN 228 209 209 GLN GLN D . n 
B 1 229 LYS 229 210 210 LYS LYS D . n 
B 1 230 PHE 230 211 211 PHE PHE D . n 
B 1 231 SER 231 212 212 SER SER D . n 
B 1 232 SER 232 213 213 SER SER D . n 
B 1 233 LEU 233 214 214 LEU LEU D . n 
B 1 234 PRO 234 215 215 PRO PRO D . n 
B 1 235 LEU 235 216 216 LEU LEU D . n 
B 1 236 GLY 236 217 217 GLY GLY D . n 
B 1 237 ARG 237 218 218 ARG ARG D . n 
B 1 238 GLU 238 219 219 GLU GLU D . n 
B 1 239 ALA 239 220 220 ALA ALA D . n 
B 1 240 VAL 240 221 221 VAL VAL D . n 
B 1 241 GLU 241 222 222 GLU GLU D . n 
B 1 242 ALA 242 223 223 ALA ALA D . n 
B 1 243 ALA 243 224 224 ALA ALA D . n 
B 1 244 VAL 244 225 225 VAL VAL D . n 
B 1 245 LYS 245 226 226 LYS LYS D . n 
B 1 246 GLU 246 227 227 GLU GLU D . n 
B 1 247 ALA 247 228 228 ALA ALA D . n 
B 1 248 GLY 248 229 229 GLY GLY D . n 
B 1 249 TYR 249 230 230 TYR TYR D . n 
B 1 250 THR 250 231 231 THR THR D . n 
B 1 251 ILE 251 232 232 ILE ILE D . n 
B 1 252 GLU 252 233 233 GLU GLU D . n 
B 1 253 TRP 253 234 234 TRP TRP D . n 
B 1 254 PHE 254 235 235 PHE PHE D . n 
B 1 255 GLU 255 236 236 GLU GLU D . n 
B 1 256 VAL 256 237 237 VAL VAL D . n 
B 1 257 ILE 257 238 238 ILE ILE D . n 
B 1 258 SER 258 239 239 SER SER D . n 
B 1 259 GLN 259 240 240 GLN GLN D . n 
B 1 260 SER 260 241 241 SER SER D . n 
B 1 261 TYR 261 242 242 TYR TYR D . n 
B 1 262 SER 262 243 243 SER SER D . n 
B 1 263 SER 263 244 244 SER SER D . n 
B 1 264 THR 264 245 245 THR THR D . n 
B 1 265 MET 265 246 246 MET MET D . n 
B 1 266 ALA 266 247 247 ALA ALA D . n 
B 1 267 ASN 267 248 248 ASN ASN D . n 
B 1 268 ASN 268 249 249 ASN ASN D . n 
B 1 269 GLU 269 250 250 GLU GLU D . n 
B 1 270 GLY 270 251 251 GLY GLY D . n 
B 1 271 LEU 271 252 252 LEU LEU D . n 
B 1 272 PHE 272 253 253 PHE PHE D . n 
B 1 273 SER 273 254 254 SER SER D . n 
B 1 274 LEU 274 255 255 LEU LEU D . n 
B 1 275 VAL 275 256 256 VAL VAL D . n 
B 1 276 ALA 276 257 257 ALA ALA D . n 
B 1 277 ARG 277 258 258 ARG ARG D . n 
B 1 278 LYS 278 259 259 LYS LYS D . n 
B 1 279 LEU 279 260 260 LEU LEU D . n 
B 1 280 SER 280 261 ?   ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IPM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IPM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1IPM 1   301 1    A1IPM UNL B . 
D 3 SAH   1   302 302  SAH   SAH B . 
E 2 A1IPM 1   301 2    A1IPM UNL D . 
F 3 SAH   1   302 304  SAH   SAH D . 
G 4 HOH   1   401 1369 HOH   HOH B . 
G 4 HOH   2   402 1321 HOH   HOH B . 
G 4 HOH   3   403 1344 HOH   HOH B . 
G 4 HOH   4   404 1324 HOH   HOH B . 
G 4 HOH   5   405 1674 HOH   HOH B . 
G 4 HOH   6   406 1601 HOH   HOH B . 
G 4 HOH   7   407 1380 HOH   HOH B . 
G 4 HOH   8   408 1523 HOH   HOH B . 
G 4 HOH   9   409 1487 HOH   HOH B . 
G 4 HOH   10  410 1495 HOH   HOH B . 
G 4 HOH   11  411 1511 HOH   HOH B . 
G 4 HOH   12  412 1406 HOH   HOH B . 
G 4 HOH   13  413 1491 HOH   HOH B . 
G 4 HOH   14  414 1323 HOH   HOH B . 
G 4 HOH   15  415 1504 HOH   HOH B . 
G 4 HOH   16  416 1508 HOH   HOH B . 
G 4 HOH   17  417 1313 HOH   HOH B . 
G 4 HOH   18  418 1425 HOH   HOH B . 
G 4 HOH   19  419 1381 HOH   HOH B . 
G 4 HOH   20  420 1394 HOH   HOH B . 
G 4 HOH   21  421 1328 HOH   HOH B . 
G 4 HOH   22  422 1563 HOH   HOH B . 
G 4 HOH   23  423 1671 HOH   HOH B . 
G 4 HOH   24  424 1388 HOH   HOH B . 
G 4 HOH   25  425 1322 HOH   HOH B . 
G 4 HOH   26  426 1331 HOH   HOH B . 
G 4 HOH   27  427 1647 HOH   HOH B . 
G 4 HOH   28  428 1570 HOH   HOH B . 
G 4 HOH   29  429 1363 HOH   HOH B . 
G 4 HOH   30  430 1660 HOH   HOH B . 
G 4 HOH   31  431 1433 HOH   HOH B . 
G 4 HOH   32  432 1573 HOH   HOH B . 
G 4 HOH   33  433 1663 HOH   HOH B . 
G 4 HOH   34  434 1584 HOH   HOH B . 
G 4 HOH   35  435 1458 HOH   HOH B . 
G 4 HOH   36  436 1395 HOH   HOH B . 
G 4 HOH   37  437 1405 HOH   HOH B . 
G 4 HOH   38  438 1489 HOH   HOH B . 
G 4 HOH   39  439 1338 HOH   HOH B . 
G 4 HOH   40  440 1419 HOH   HOH B . 
G 4 HOH   41  441 1360 HOH   HOH B . 
G 4 HOH   42  442 1326 HOH   HOH B . 
G 4 HOH   43  443 1620 HOH   HOH B . 
G 4 HOH   44  444 1327 HOH   HOH B . 
G 4 HOH   45  445 1587 HOH   HOH B . 
G 4 HOH   46  446 1393 HOH   HOH B . 
G 4 HOH   47  447 1361 HOH   HOH B . 
G 4 HOH   48  448 1528 HOH   HOH B . 
G 4 HOH   49  449 1597 HOH   HOH B . 
G 4 HOH   50  450 1543 HOH   HOH B . 
G 4 HOH   51  451 1641 HOH   HOH B . 
G 4 HOH   52  452 1385 HOH   HOH B . 
G 4 HOH   53  453 1680 HOH   HOH B . 
G 4 HOH   54  454 1448 HOH   HOH B . 
G 4 HOH   55  455 1376 HOH   HOH B . 
G 4 HOH   56  456 910  HOH   HOH B . 
G 4 HOH   57  457 1743 HOH   HOH B . 
G 4 HOH   58  458 1341 HOH   HOH B . 
G 4 HOH   59  459 1494 HOH   HOH B . 
G 4 HOH   60  460 1507 HOH   HOH B . 
G 4 HOH   61  461 1593 HOH   HOH B . 
G 4 HOH   62  462 1518 HOH   HOH B . 
G 4 HOH   63  463 1546 HOH   HOH B . 
G 4 HOH   64  464 1396 HOH   HOH B . 
G 4 HOH   65  465 1354 HOH   HOH B . 
G 4 HOH   66  466 1521 HOH   HOH B . 
G 4 HOH   67  467 1348 HOH   HOH B . 
G 4 HOH   68  468 1440 HOH   HOH B . 
G 4 HOH   69  469 1623 HOH   HOH B . 
G 4 HOH   70  470 1371 HOH   HOH B . 
G 4 HOH   71  471 1608 HOH   HOH B . 
G 4 HOH   72  472 1571 HOH   HOH B . 
G 4 HOH   73  473 1306 HOH   HOH B . 
G 4 HOH   74  474 1379 HOH   HOH B . 
G 4 HOH   75  475 1312 HOH   HOH B . 
G 4 HOH   76  476 1551 HOH   HOH B . 
G 4 HOH   77  477 1759 HOH   HOH B . 
G 4 HOH   78  478 1612 HOH   HOH B . 
G 4 HOH   79  479 1436 HOH   HOH B . 
G 4 HOH   80  480 1382 HOH   HOH B . 
G 4 HOH   81  481 1422 HOH   HOH B . 
G 4 HOH   82  482 1447 HOH   HOH B . 
G 4 HOH   83  483 1562 HOH   HOH B . 
G 4 HOH   84  484 1346 HOH   HOH B . 
G 4 HOH   85  485 1345 HOH   HOH B . 
G 4 HOH   86  486 1470 HOH   HOH B . 
G 4 HOH   87  487 1375 HOH   HOH B . 
G 4 HOH   88  488 1568 HOH   HOH B . 
G 4 HOH   89  489 1684 HOH   HOH B . 
G 4 HOH   90  490 1340 HOH   HOH B . 
G 4 HOH   91  491 1397 HOH   HOH B . 
G 4 HOH   92  492 1549 HOH   HOH B . 
G 4 HOH   93  493 1541 HOH   HOH B . 
G 4 HOH   94  494 1377 HOH   HOH B . 
G 4 HOH   95  495 1343 HOH   HOH B . 
G 4 HOH   96  496 1368 HOH   HOH B . 
G 4 HOH   97  497 1418 HOH   HOH B . 
G 4 HOH   98  498 1415 HOH   HOH B . 
G 4 HOH   99  499 1474 HOH   HOH B . 
G 4 HOH   100 500 1329 HOH   HOH B . 
G 4 HOH   101 501 1526 HOH   HOH B . 
G 4 HOH   102 502 1480 HOH   HOH B . 
G 4 HOH   103 503 1540 HOH   HOH B . 
G 4 HOH   104 504 1509 HOH   HOH B . 
G 4 HOH   105 505 1530 HOH   HOH B . 
G 4 HOH   106 506 1626 HOH   HOH B . 
G 4 HOH   107 507 1417 HOH   HOH B . 
G 4 HOH   108 508 1428 HOH   HOH B . 
G 4 HOH   109 509 1475 HOH   HOH B . 
G 4 HOH   110 510 1514 HOH   HOH B . 
G 4 HOH   111 511 1424 HOH   HOH B . 
G 4 HOH   112 512 1632 HOH   HOH B . 
G 4 HOH   113 513 1378 HOH   HOH B . 
G 4 HOH   114 514 1350 HOH   HOH B . 
G 4 HOH   115 515 1460 HOH   HOH B . 
G 4 HOH   116 516 1515 HOH   HOH B . 
G 4 HOH   117 517 1316 HOH   HOH B . 
G 4 HOH   118 518 1615 HOH   HOH B . 
G 4 HOH   119 519 1080 HOH   HOH B . 
G 4 HOH   120 520 1582 HOH   HOH B . 
G 4 HOH   121 521 1569 HOH   HOH B . 
G 4 HOH   122 522 1481 HOH   HOH B . 
G 4 HOH   123 523 1314 HOH   HOH B . 
G 4 HOH   124 524 1710 HOH   HOH B . 
G 4 HOH   125 525 1353 HOH   HOH B . 
G 4 HOH   126 526 1627 HOH   HOH B . 
G 4 HOH   127 527 1088 HOH   HOH B . 
G 4 HOH   128 528 1544 HOH   HOH B . 
G 4 HOH   129 529 1692 HOH   HOH B . 
G 4 HOH   130 530 1407 HOH   HOH B . 
G 4 HOH   131 531 1690 HOH   HOH B . 
G 4 HOH   132 532 1659 HOH   HOH B . 
G 4 HOH   133 533 1408 HOH   HOH B . 
G 4 HOH   134 534 1555 HOH   HOH B . 
G 4 HOH   135 535 1577 HOH   HOH B . 
G 4 HOH   136 536 1670 HOH   HOH B . 
G 4 HOH   137 537 1614 HOH   HOH B . 
G 4 HOH   138 538 1411 HOH   HOH B . 
G 4 HOH   139 539 1633 HOH   HOH B . 
G 4 HOH   140 540 1467 HOH   HOH B . 
G 4 HOH   141 541 1524 HOH   HOH B . 
G 4 HOH   142 542 1580 HOH   HOH B . 
G 4 HOH   143 543 1450 HOH   HOH B . 
G 4 HOH   144 544 1432 HOH   HOH B . 
G 4 HOH   145 545 1520 HOH   HOH B . 
G 4 HOH   146 546 1412 HOH   HOH B . 
G 4 HOH   147 547 1666 HOH   HOH B . 
G 4 HOH   148 548 1531 HOH   HOH B . 
G 4 HOH   149 549 1478 HOH   HOH B . 
G 4 HOH   150 550 1596 HOH   HOH B . 
H 4 HOH   1   401 1485 HOH   HOH D . 
H 4 HOH   2   402 1501 HOH   HOH D . 
H 4 HOH   3   403 1442 HOH   HOH D . 
H 4 HOH   4   404 1383 HOH   HOH D . 
H 4 HOH   5   405 909  HOH   HOH D . 
H 4 HOH   6   406 1373 HOH   HOH D . 
H 4 HOH   7   407 1339 HOH   HOH D . 
H 4 HOH   8   408 1318 HOH   HOH D . 
H 4 HOH   9   409 1335 HOH   HOH D . 
H 4 HOH   10  410 1430 HOH   HOH D . 
H 4 HOH   11  411 1362 HOH   HOH D . 
H 4 HOH   12  412 1727 HOH   HOH D . 
H 4 HOH   13  413 1310 HOH   HOH D . 
H 4 HOH   14  414 1357 HOH   HOH D . 
H 4 HOH   15  415 1527 HOH   HOH D . 
H 4 HOH   16  416 1595 HOH   HOH D . 
H 4 HOH   17  417 1429 HOH   HOH D . 
H 4 HOH   18  418 1548 HOH   HOH D . 
H 4 HOH   19  419 1483 HOH   HOH D . 
H 4 HOH   20  420 1387 HOH   HOH D . 
H 4 HOH   21  421 1466 HOH   HOH D . 
H 4 HOH   22  422 1721 HOH   HOH D . 
H 4 HOH   23  423 1317 HOH   HOH D . 
H 4 HOH   24  424 1646 HOH   HOH D . 
H 4 HOH   25  425 1463 HOH   HOH D . 
H 4 HOH   26  426 1391 HOH   HOH D . 
H 4 HOH   27  427 1332 HOH   HOH D . 
H 4 HOH   28  428 1714 HOH   HOH D . 
H 4 HOH   29  429 965  HOH   HOH D . 
H 4 HOH   30  430 1492 HOH   HOH D . 
H 4 HOH   31  431 1516 HOH   HOH D . 
H 4 HOH   32  432 1392 HOH   HOH D . 
H 4 HOH   33  433 1590 HOH   HOH D . 
H 4 HOH   34  434 1410 HOH   HOH D . 
H 4 HOH   35  435 1525 HOH   HOH D . 
H 4 HOH   36  436 1336 HOH   HOH D . 
H 4 HOH   37  437 1656 HOH   HOH D . 
H 4 HOH   38  438 970  HOH   HOH D . 
H 4 HOH   39  439 1557 HOH   HOH D . 
H 4 HOH   40  440 1309 HOH   HOH D . 
H 4 HOH   41  441 1386 HOH   HOH D . 
H 4 HOH   42  442 1476 HOH   HOH D . 
H 4 HOH   43  443 1496 HOH   HOH D . 
H 4 HOH   44  444 1365 HOH   HOH D . 
H 4 HOH   45  445 1403 HOH   HOH D . 
H 4 HOH   46  446 1427 HOH   HOH D . 
H 4 HOH   47  447 1559 HOH   HOH D . 
H 4 HOH   48  448 1444 HOH   HOH D . 
H 4 HOH   49  449 1586 HOH   HOH D . 
H 4 HOH   50  450 1315 HOH   HOH D . 
H 4 HOH   51  451 1542 HOH   HOH D . 
H 4 HOH   52  452 1325 HOH   HOH D . 
H 4 HOH   53  453 1718 HOH   HOH D . 
H 4 HOH   54  454 1402 HOH   HOH D . 
H 4 HOH   55  455 1359 HOH   HOH D . 
H 4 HOH   56  456 1560 HOH   HOH D . 
H 4 HOH   57  457 1630 HOH   HOH D . 
H 4 HOH   58  458 1490 HOH   HOH D . 
H 4 HOH   59  459 1308 HOH   HOH D . 
H 4 HOH   60  460 1725 HOH   HOH D . 
H 4 HOH   61  461 1611 HOH   HOH D . 
H 4 HOH   62  462 1366 HOH   HOH D . 
H 4 HOH   63  463 1374 HOH   HOH D . 
H 4 HOH   64  464 1579 HOH   HOH D . 
H 4 HOH   65  465 1461 HOH   HOH D . 
H 4 HOH   66  466 1488 HOH   HOH D . 
H 4 HOH   67  467 1319 HOH   HOH D . 
H 4 HOH   68  468 1457 HOH   HOH D . 
H 4 HOH   69  469 1453 HOH   HOH D . 
H 4 HOH   70  470 1337 HOH   HOH D . 
H 4 HOH   71  471 1512 HOH   HOH D . 
H 4 HOH   72  472 1420 HOH   HOH D . 
H 4 HOH   73  473 1554 HOH   HOH D . 
H 4 HOH   74  474 1452 HOH   HOH D . 
H 4 HOH   75  475 1431 HOH   HOH D . 
H 4 HOH   76  476 1384 HOH   HOH D . 
H 4 HOH   77  477 964  HOH   HOH D . 
H 4 HOH   78  478 598  HOH   HOH D . 
H 4 HOH   79  479 1519 HOH   HOH D . 
H 4 HOH   80  480 1534 HOH   HOH D . 
H 4 HOH   81  481 1535 HOH   HOH D . 
H 4 HOH   82  482 1653 HOH   HOH D . 
H 4 HOH   83  483 1333 HOH   HOH D . 
H 4 HOH   84  484 1390 HOH   HOH D . 
H 4 HOH   85  485 1048 HOH   HOH D . 
H 4 HOH   86  486 1044 HOH   HOH D . 
H 4 HOH   87  487 1702 HOH   HOH D . 
H 4 HOH   88  488 1441 HOH   HOH D . 
H 4 HOH   89  489 1729 HOH   HOH D . 
H 4 HOH   90  490 1065 HOH   HOH D . 
H 4 HOH   91  491 1486 HOH   HOH D . 
H 4 HOH   92  492 192  HOH   HOH D . 
H 4 HOH   93  493 1320 HOH   HOH D . 
H 4 HOH   94  494 1610 HOH   HOH D . 
H 4 HOH   95  495 1342 HOH   HOH D . 
H 4 HOH   96  496 1073 HOH   HOH D . 
H 4 HOH   97  497 962  HOH   HOH D . 
H 4 HOH   98  498 1517 HOH   HOH D . 
H 4 HOH   99  499 1184 HOH   HOH D . 
H 4 HOH   100 500 1434 HOH   HOH D . 
H 4 HOH   101 501 1189 HOH   HOH D . 
H 4 HOH   102 502 1099 HOH   HOH D . 
H 4 HOH   103 503 1347 HOH   HOH D . 
H 4 HOH   104 504 1401 HOH   HOH D . 
H 4 HOH   105 505 1330 HOH   HOH D . 
H 4 HOH   106 506 1400 HOH   HOH D . 
H 4 HOH   107 507 1351 HOH   HOH D . 
H 4 HOH   108 508 1261 HOH   HOH D . 
H 4 HOH   109 509 1356 HOH   HOH D . 
H 4 HOH   110 510 932  HOH   HOH D . 
H 4 HOH   111 511 1631 HOH   HOH D . 
H 4 HOH   112 512 1334 HOH   HOH D . 
H 4 HOH   113 513 1404 HOH   HOH D . 
H 4 HOH   114 514 1561 HOH   HOH D . 
H 4 HOH   115 515 1459 HOH   HOH D . 
H 4 HOH   116 516 1001 HOH   HOH D . 
H 4 HOH   117 517 1454 HOH   HOH D . 
H 4 HOH   118 518 1532 HOH   HOH D . 
H 4 HOH   119 519 1364 HOH   HOH D . 
H 4 HOH   120 520 1414 HOH   HOH D . 
H 4 HOH   121 521 1624 HOH   HOH D . 
H 4 HOH   122 522 1367 HOH   HOH D . 
H 4 HOH   123 523 1451 HOH   HOH D . 
H 4 HOH   124 524 1145 HOH   HOH D . 
H 4 HOH   125 525 1446 HOH   HOH D . 
H 4 HOH   126 526 1498 HOH   HOH D . 
H 4 HOH   127 527 1079 HOH   HOH D . 
H 4 HOH   128 528 1591 HOH   HOH D . 
H 4 HOH   129 529 931  HOH   HOH D . 
H 4 HOH   130 530 1311 HOH   HOH D . 
H 4 HOH   131 531 1389 HOH   HOH D . 
H 4 HOH   132 532 1358 HOH   HOH D . 
H 4 HOH   133 533 1399 HOH   HOH D . 
H 4 HOH   134 534 1421 HOH   HOH D . 
H 4 HOH   135 535 1537 HOH   HOH D . 
H 4 HOH   136 536 954  HOH   HOH D . 
H 4 HOH   137 537 1553 HOH   HOH D . 
H 4 HOH   138 538 1372 HOH   HOH D . 
H 4 HOH   139 539 1574 HOH   HOH D . 
H 4 HOH   140 540 1566 HOH   HOH D . 
H 4 HOH   141 541 1565 HOH   HOH D . 
H 4 HOH   142 542 1471 HOH   HOH D . 
H 4 HOH   143 543 1413 HOH   HOH D . 
H 4 HOH   144 544 1307 HOH   HOH D . 
H 4 HOH   145 545 1699 HOH   HOH D . 
H 4 HOH   146 546 1681 HOH   HOH D . 
H 4 HOH   147 547 1636 HOH   HOH D . 
H 4 HOH   148 548 1604 HOH   HOH D . 
H 4 HOH   149 549 1538 HOH   HOH D . 
H 4 HOH   150 550 1536 HOH   HOH D . 
H 4 HOH   151 551 1416 HOH   HOH D . 
H 4 HOH   152 552 1438 HOH   HOH D . 
H 4 HOH   153 553 1600 HOH   HOH D . 
H 4 HOH   154 554 1529 HOH   HOH D . 
H 4 HOH   155 555 938  HOH   HOH D . 
H 4 HOH   156 556 1439 HOH   HOH D . 
H 4 HOH   157 557 1464 HOH   HOH D . 
H 4 HOH   158 558 1545 HOH   HOH D . 
H 4 HOH   159 559 1707 HOH   HOH D . 
H 4 HOH   160 560 1598 HOH   HOH D . 
H 4 HOH   161 561 1409 HOH   HOH D . 
H 4 HOH   162 562 1567 HOH   HOH D . 
H 4 HOH   163 563 1355 HOH   HOH D . 
H 4 HOH   164 564 1606 HOH   HOH D . 
H 4 HOH   165 565 1437 HOH   HOH D . 
H 4 HOH   166 566 1522 HOH   HOH D . 
H 4 HOH   167 567 1662 HOH   HOH D . 
H 4 HOH   168 568 1349 HOH   HOH D . 
H 4 HOH   169 569 1398 HOH   HOH D . 
H 4 HOH   170 570 1583 HOH   HOH D . 
H 4 HOH   171 571 1472 HOH   HOH D . 
H 4 HOH   172 572 1589 HOH   HOH D . 
H 4 HOH   173 573 1668 HOH   HOH D . 
H 4 HOH   174 574 1726 HOH   HOH D . 
H 4 HOH   175 575 1435 HOH   HOH D . 
H 4 HOH   176 576 862  HOH   HOH D . 
H 4 HOH   177 577 1747 HOH   HOH D . 
H 4 HOH   178 578 1719 HOH   HOH D . 
H 4 HOH   179 579 1749 HOH   HOH D . 
H 4 HOH   180 580 1700 HOH   HOH D . 
H 4 HOH   181 581 1473 HOH   HOH D . 
H 4 HOH   182 582 1370 HOH   HOH D . 
H 4 HOH   183 583 1753 HOH   HOH D . 
H 4 HOH   184 584 1575 HOH   HOH D . 
H 4 HOH   185 585 1499 HOH   HOH D . 
H 4 HOH   186 586 1027 HOH   HOH D . 
H 4 HOH   187 587 1643 HOH   HOH D . 
H 4 HOH   188 588 1426 HOH   HOH D . 
H 4 HOH   189 589 1744 HOH   HOH D . 
H 4 HOH   190 590 1599 HOH   HOH D . 
H 4 HOH   191 591 1713 HOH   HOH D . 
H 4 HOH   192 592 1708 HOH   HOH D . 
H 4 HOH   193 593 1748 HOH   HOH D . 
H 4 HOH   194 594 1746 HOH   HOH D . 
H 4 HOH   195 595 1756 HOH   HOH D . 
H 4 HOH   196 596 1745 HOH   HOH D . 
# 
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  ? ? ? 2.11.7 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? BUSTER  ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H5O 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.28 
_cell.length_a_esd                 ? 
_cell.length_b                     69.71 
_cell.length_b_esd                 ? 
_cell.length_c                     114.53 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9H5O 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9H5O 
_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             1.98 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.01 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '32% PEG3350, 0.2 M NaAc, and 0.1 M Hepes pH 6.8-7.5' 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2018-07-16 
_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   0.96860 
_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 I24' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.96860 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H5O 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.63 
_reflns.d_resolution_low                               44.3 
_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                                     40039 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.99 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.63 
_reflns_shell.d_res_low                                     1.67 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             818 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.89 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            7.6188 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            9.901 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -17.5198 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               12.39 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.726 
_refine.correlation_coeff_Fo_to_Fc_free          0.677 
_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                                 9H5O 
_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                            1.9 
_refine.ls_d_res_low                             43.04 
_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                     40039 
_refine.ls_number_reflns_R_free                  2022 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    100 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.255 
_refine.ls_R_factor_R_free                       0.283 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.254 
_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                          ? 
_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   0.177 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.181 
_refine.pdbx_overall_SU_R_Blow_DPI               0.224 
_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             0.211 
_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                        9H5O 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.33 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.9 
_refine_hist.d_res_low                        43.04 
_refine_hist.number_atoms_solvent             346 
_refine_hist.number_atoms_total               4318 
_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        3894 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         78 
_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' ? 0.01  ? 4085 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.97  ? 5541 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1410 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 705  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 4085 ? t_it                      20 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 522  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 4988 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 3.13  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 16.04 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.9 
_refine_ls_shell.d_res_low                        1.91 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                801 
_refine_ls_shell.number_reflns_R_free             38 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               100 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     0.2945 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2955 
_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                  0.2738 
# 
_struct.entry_id                     9H5O 
_struct.title                        'NNMT-SAM IN COMPLEX WITH 20s' 
_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        9H5O 
_struct_keywords.text            'NNMT SAH SAM, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NNMT_HUMAN 
_struct_ref.pdbx_db_accession          P40261 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLIDIGSGPTIYQLLSACESFKEIV
VTDYSDQNLQELEKWLKKEPEAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKCDVTQSQPLGAVPLPPADCVLS
TLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAVEAAVKEAGYTIEWFEVISQSY
SSTMANNEGLFSLVARKLS
;
_struct_ref.pdbx_align_begin           3 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9H5O B 22 ? 280 ? P40261 3 ? 261 ? 3 261 
2 1 9H5O D 22 ? 280 ? P40261 3 ? 261 ? 3 261 
# 
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 9H5O HIS B 1   ? UNP P40261 ?   ?   'expression tag'      -18 1  
1 9H5O ASN B 2   ? UNP P40261 ?   ?   'expression tag'      -17 2  
1 9H5O HIS B 3   ? UNP P40261 ?   ?   'expression tag'      -16 3  
1 9H5O ASN B 4   ? UNP P40261 ?   ?   'expression tag'      -15 4  
1 9H5O HIS B 5   ? UNP P40261 ?   ?   'expression tag'      -14 5  
1 9H5O ASN B 6   ? UNP P40261 ?   ?   'expression tag'      -13 6  
1 9H5O HIS B 7   ? UNP P40261 ?   ?   'expression tag'      -12 7  
1 9H5O ASN B 8   ? UNP P40261 ?   ?   'expression tag'      -11 8  
1 9H5O HIS B 9   ? UNP P40261 ?   ?   'expression tag'      -10 9  
1 9H5O ASN B 10  ? UNP P40261 ?   ?   'expression tag'      -9  10 
1 9H5O HIS B 11  ? UNP P40261 ?   ?   'expression tag'      -8  11 
1 9H5O ASN B 12  ? UNP P40261 ?   ?   'expression tag'      -7  12 
1 9H5O ALA B 13  ? UNP P40261 ?   ?   'expression tag'      -6  13 
1 9H5O ALA B 14  ? UNP P40261 ?   ?   'expression tag'      -5  14 
1 9H5O ALA B 15  ? UNP P40261 ?   ?   'expression tag'      -4  15 
1 9H5O GLU B 16  ? UNP P40261 ?   ?   'expression tag'      -3  16 
1 9H5O ASN B 17  ? UNP P40261 ?   ?   'expression tag'      -2  17 
1 9H5O LEU B 18  ? UNP P40261 ?   ?   'expression tag'      -1  18 
1 9H5O TYR B 19  ? UNP P40261 ?   ?   'expression tag'      0   19 
1 9H5O PHE B 20  ? UNP P40261 ?   ?   'expression tag'      1   20 
1 9H5O GLN B 21  ? UNP P40261 ?   ?   'expression tag'      2   21 
1 9H5O ALA B 119 ? UNP P40261 LYS 100 'engineered mutation' 100 22 
1 9H5O ALA B 120 ? UNP P40261 GLU 101 'engineered mutation' 101 23 
1 9H5O ALA B 122 ? UNP P40261 GLU 103 'engineered mutation' 103 24 
2 9H5O HIS D 1   ? UNP P40261 ?   ?   'expression tag'      -18 25 
2 9H5O ASN D 2   ? UNP P40261 ?   ?   'expression tag'      -17 26 
2 9H5O HIS D 3   ? UNP P40261 ?   ?   'expression tag'      -16 27 
2 9H5O ASN D 4   ? UNP P40261 ?   ?   'expression tag'      -15 28 
2 9H5O HIS D 5   ? UNP P40261 ?   ?   'expression tag'      -14 29 
2 9H5O ASN D 6   ? UNP P40261 ?   ?   'expression tag'      -13 30 
2 9H5O HIS D 7   ? UNP P40261 ?   ?   'expression tag'      -12 31 
2 9H5O ASN D 8   ? UNP P40261 ?   ?   'expression tag'      -11 32 
2 9H5O HIS D 9   ? UNP P40261 ?   ?   'expression tag'      -10 33 
2 9H5O ASN D 10  ? UNP P40261 ?   ?   'expression tag'      -9  34 
2 9H5O HIS D 11  ? UNP P40261 ?   ?   'expression tag'      -8  35 
2 9H5O ASN D 12  ? UNP P40261 ?   ?   'expression tag'      -7  36 
2 9H5O ALA D 13  ? UNP P40261 ?   ?   'expression tag'      -6  37 
2 9H5O ALA D 14  ? UNP P40261 ?   ?   'expression tag'      -5  38 
2 9H5O ALA D 15  ? UNP P40261 ?   ?   'expression tag'      -4  39 
2 9H5O GLU D 16  ? UNP P40261 ?   ?   'expression tag'      -3  40 
2 9H5O ASN D 17  ? UNP P40261 ?   ?   'expression tag'      -2  41 
2 9H5O LEU D 18  ? UNP P40261 ?   ?   'expression tag'      -1  42 
2 9H5O TYR D 19  ? UNP P40261 ?   ?   'expression tag'      0   43 
2 9H5O PHE D 20  ? UNP P40261 ?   ?   'expression tag'      1   44 
2 9H5O GLN D 21  ? UNP P40261 ?   ?   'expression tag'      2   45 
2 9H5O ALA D 119 ? UNP P40261 LYS 100 'engineered mutation' 100 46 
2 9H5O ALA D 120 ? UNP P40261 GLU 101 'engineered mutation' 101 47 
2 9H5O ALA D 122 ? UNP P40261 GLU 103 'engineered mutation' 103 48 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LYS A 27  ? HIS A 33  ? LYS B 8   HIS B 14  1 ? 7  
HELX_P HELX_P2  AA2 ASN A 35  ? TYR A 44  ? ASN B 16  TYR B 25  1 ? 10 
HELX_P HELX_P3  AA3 SER A 54  ? LEU A 70  ? SER B 35  LEU B 51  1 ? 17 
HELX_P HELX_P4  AA4 ILE A 87  ? LEU A 91  ? ILE B 68  LEU B 72  5 ? 5  
HELX_P HELX_P5  AA5 SER A 92  ? GLU A 95  ? SER B 73  GLU B 76  5 ? 4  
HELX_P HELX_P6  AA6 SER A 106 ? LYS A 118 ? SER B 87  LYS B 99  1 ? 13 
HELX_P HELX_P7  AA7 TRP A 126 ? GLU A 137 ? TRP B 107 GLU B 118 1 ? 12 
HELX_P HELX_P8  AA8 LYS A 142 ? ALA A 153 ? LYS B 123 ALA B 134 1 ? 12 
HELX_P HELX_P9  AA9 CYS A 184 ? CYS A 189 ? CYS B 165 CYS B 170 1 ? 6  
HELX_P HELX_P10 AB1 ASP A 191 ? SER A 204 ? ASP B 172 SER B 185 1 ? 14 
HELX_P HELX_P11 AB2 GLY A 236 ? ALA A 247 ? GLY B 217 ALA B 228 1 ? 12 
HELX_P HELX_P12 AB3 SER B 26  ? PHE B 34  ? SER D 7   PHE D 15  1 ? 9  
HELX_P HELX_P13 AB4 ASN B 35  ? TYR B 44  ? ASN D 16  TYR D 25  1 ? 10 
HELX_P HELX_P14 AB5 SER B 54  ? LEU B 70  ? SER D 35  LEU D 51  1 ? 17 
HELX_P HELX_P15 AB6 ILE B 87  ? LEU B 91  ? ILE D 68  LEU D 72  5 ? 5  
HELX_P HELX_P16 AB7 SER B 92  ? GLU B 95  ? SER D 73  GLU D 76  5 ? 4  
HELX_P HELX_P17 AB8 SER B 106 ? LYS B 118 ? SER D 87  LYS D 99  1 ? 13 
HELX_P HELX_P18 AB9 TRP B 126 ? GLU B 137 ? TRP D 107 GLU D 118 1 ? 12 
HELX_P HELX_P19 AC1 LYS B 142 ? ALA B 153 ? LYS D 123 ALA D 134 1 ? 12 
HELX_P HELX_P20 AC2 CYS B 184 ? CYS B 189 ? CYS D 165 CYS D 170 1 ? 6  
HELX_P HELX_P21 AC3 ASP B 191 ? SER B 204 ? ASP D 172 SER D 185 1 ? 14 
HELX_P HELX_P22 AC4 GLY B 236 ? ALA B 247 ? GLY D 217 ALA D 228 1 ? 12 
# 
_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 ? 14 ? 
AA2 ? 2  ? 
AA3 ? 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  ? parallel      
AA1 3  4  ? parallel      
AA1 4  5  ? parallel      
AA1 5  6  ? anti-parallel 
AA1 6  7  ? anti-parallel 
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? parallel      
AA1 11 12 ? parallel      
AA1 12 13 ? parallel      
AA1 13 14 ? parallel      
AA2 1  2  ? anti-parallel 
AA3 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  VAL A 154 ? LYS A 159 ? VAL B 135 LYS B 140 
AA1 2  PHE A 97  ? ASP A 104 ? PHE B 78  ASP B 85  
AA1 3  GLY A 75  ? ASP A 80  ? GLY B 56  ASP B 61  
AA1 4  ALA A 176 ? THR A 182 ? ALA B 157 THR B 163 
AA1 5  LEU A 206 ? ALA A 217 ? LEU B 187 ALA B 198 
AA1 6  LEU A 271 ? LYS A 278 ? LEU B 252 LYS B 259 
AA1 7  TYR A 249 ? ILE A 257 ? TYR B 230 ILE B 238 
AA1 8  TYR B 249 ? ILE B 257 ? TYR D 230 ILE D 238 
AA1 9  LEU B 271 ? LYS B 278 ? LEU D 252 LYS D 259 
AA1 10 LEU B 206 ? ALA B 217 ? LEU D 187 ALA D 198 
AA1 11 ALA B 176 ? THR B 182 ? ALA D 157 THR D 163 
AA1 12 GLY B 75  ? ASP B 80  ? GLY D 56  ASP D 61  
AA1 13 PHE B 97  ? ASP B 104 ? PHE D 78  ASP D 85  
AA1 14 VAL B 154 ? LYS B 159 ? VAL D 135 LYS D 140 
AA2 1  TYR A 222 ? ILE A 225 ? TYR B 203 ILE B 206 
AA2 2  GLN A 228 ? SER A 231 ? GLN B 209 SER B 212 
AA3 1  TYR B 222 ? ILE B 225 ? TYR D 203 ILE D 206 
AA3 2  GLN B 228 ? SER B 231 ? GLN D 209 SER D 212 
# 
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  O LEU A 158 ? O LEU B 139 N VAL A 102 ? N VAL B 83  
AA1 2  3  O VAL A 101 ? O VAL B 82  N ASP A 80  ? N ASP B 61  
AA1 3  4  N ILE A 79  ? N ILE B 60  O LEU A 180 ? O LEU B 161 
AA1 4  5  N VAL A 179 ? N VAL B 160 O VAL A 213 ? O VAL B 194 
AA1 5  6  N LEU A 212 ? N LEU B 193 O ALA A 276 ? O ALA B 257 
AA1 6  7  O VAL A 275 ? O VAL B 256 N GLU A 252 ? N GLU B 233 
AA1 7  8  N VAL A 256 ? N VAL B 237 O PHE B 254 ? O PHE D 235 
AA1 8  9  N GLU B 252 ? N GLU D 233 O VAL B 275 ? O VAL D 256 
AA1 9  10 O ALA B 276 ? O ALA D 257 N LEU B 212 ? N LEU D 193 
AA1 10 11 O VAL B 213 ? O VAL D 194 N VAL B 179 ? N VAL D 160 
AA1 11 12 O LEU B 180 ? O LEU D 161 N ILE B 79  ? N ILE D 60  
AA1 12 13 N ASP B 80  ? N ASP D 61  O VAL B 101 ? O VAL D 82  
AA1 13 14 N VAL B 102 ? N VAL D 83  O LEU B 158 ? O LEU D 139 
AA2 1  2  N ILE A 225 ? N ILE B 206 O GLN A 228 ? O GLN B 209 
AA3 1  2  N ILE B 225 ? N ILE D 206 O GLN B 228 ? O GLN D 209 
# 
_pdbx_entry_details.entry_id                   9H5O 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU B 250 ? ? -113.90 71.98 
2 1 GLU D 250 ? ? -114.84 71.94 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? ? 2.5087  -24.3657 72.5708 -0.4398 ? -0.0185 ? 0.175   ? -0.5031 ? -0.1978 ? -0.3422 ? 0 ? -2.2465 ? 3.385 
? 0.6517 ? -2.9715 ? 0 ? 0.0394 ? -0.6808 ? -0.2941 ? -0.6808 ? -0.0984 ? -0.4297 ? -0.2941 ? -0.4297 ? 0.059   ? 
2 'X-RAY DIFFRACTION' ? ? 27.9385 -46.9593 72.4291 -0.5625 ? -0.1506 ? -0.1384 ? -0.5717 ? -0.1683 ? -0.5683 ? 0 ? -0.4963 ? 
-5.1741 ? 0      ? 2.1745  ? 0 ? 0.0914 ? -0.6745 ? 0.2546  ? -0.6745 ? -0.0508 ? 0.0871  ? 0.2546  ? 0.0871  ? -0.0406 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? '{ B|* }' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '{ D|* }' 
# 
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 B HIS -18 ? A HIS 1   
2  1 Y 1 B ASN -17 ? A ASN 2   
3  1 Y 1 B HIS -16 ? A HIS 3   
4  1 Y 1 B ASN -15 ? A ASN 4   
5  1 Y 1 B HIS -14 ? A HIS 5   
6  1 Y 1 B ASN -13 ? A ASN 6   
7  1 Y 1 B HIS -12 ? A HIS 7   
8  1 Y 1 B ASN -11 ? A ASN 8   
9  1 Y 1 B HIS -10 ? A HIS 9   
10 1 Y 1 B ASN -9  ? A ASN 10  
11 1 Y 1 B HIS -8  ? A HIS 11  
12 1 Y 1 B ASN -7  ? A ASN 12  
13 1 Y 1 B ALA -6  ? A ALA 13  
14 1 Y 1 B ALA -5  ? A ALA 14  
15 1 Y 1 B ALA -4  ? A ALA 15  
16 1 Y 1 B GLU -3  ? A GLU 16  
17 1 Y 1 B ASN -2  ? A ASN 17  
18 1 Y 1 B LEU -1  ? A LEU 18  
19 1 Y 1 B TYR 0   ? A TYR 19  
20 1 Y 1 B PHE 1   ? A PHE 20  
21 1 Y 1 B GLN 2   ? A GLN 21  
22 1 Y 1 B SER 3   ? A SER 22  
23 1 Y 1 B GLY 4   ? A GLY 23  
24 1 Y 1 B LYS 26  ? A LYS 45  
25 1 Y 1 B PHE 27  ? A PHE 46  
26 1 Y 1 B GLY 28  ? A GLY 47  
27 1 Y 1 B SER 29  ? A SER 48  
28 1 Y 1 B ARG 30  ? A ARG 49  
29 1 Y 1 B HIS 31  ? A HIS 50  
30 1 Y 1 B SER 32  ? A SER 51  
31 1 Y 1 B ALA 33  ? A ALA 52  
32 1 Y 1 B ASP 52  ? A ASP 71  
33 1 Y 1 B SER 261 ? A SER 280 
34 1 Y 1 D HIS -18 ? B HIS 1   
35 1 Y 1 D ASN -17 ? B ASN 2   
36 1 Y 1 D HIS -16 ? B HIS 3   
37 1 Y 1 D ASN -15 ? B ASN 4   
38 1 Y 1 D HIS -14 ? B HIS 5   
39 1 Y 1 D ASN -13 ? B ASN 6   
40 1 Y 1 D HIS -12 ? B HIS 7   
41 1 Y 1 D ASN -11 ? B ASN 8   
42 1 Y 1 D HIS -10 ? B HIS 9   
43 1 Y 1 D ASN -9  ? B ASN 10  
44 1 Y 1 D HIS -8  ? B HIS 11  
45 1 Y 1 D ASN -7  ? B ASN 12  
46 1 Y 1 D ALA -6  ? B ALA 13  
47 1 Y 1 D ALA -5  ? B ALA 14  
48 1 Y 1 D ALA -4  ? B ALA 15  
49 1 Y 1 D GLU -3  ? B GLU 16  
50 1 Y 1 D ASN -2  ? B ASN 17  
51 1 Y 1 D LEU -1  ? B LEU 18  
52 1 Y 1 D TYR 0   ? B TYR 19  
53 1 Y 1 D PHE 1   ? B PHE 20  
54 1 Y 1 D GLN 2   ? B GLN 21  
55 1 Y 1 D SER 3   ? B SER 22  
56 1 Y 1 D GLY 4   ? B GLY 23  
57 1 Y 1 D GLY 28  ? B GLY 47  
58 1 Y 1 D SER 29  ? B SER 48  
59 1 Y 1 D ARG 30  ? B ARG 49  
60 1 Y 1 D HIS 31  ? B HIS 50  
61 1 Y 1 D SER 32  ? B SER 51  
62 1 Y 1 D ALA 33  ? B ALA 52  
63 1 Y 1 D ASP 52  ? B ASP 71  
64 1 Y 1 D SER 261 ? B SER 280 
# 
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 
A1IPM C1     C N N 1   
A1IPM C3     C Y N 2   
A1IPM C7     C Y N 3   
A1IPM C8     C Y N 4   
A1IPM C10    C N N 5   
A1IPM C11    C N N 6   
A1IPM N2     N N N 7   
A1IPM C4     C Y N 8   
A1IPM C5     C Y N 9   
A1IPM C6     C N N 10  
A1IPM N9     N Y N 11  
A1IPM O12    O N N 12  
A1IPM N13    N N N 13  
A1IPM H1     H N N 14  
A1IPM H2     H N N 15  
A1IPM H3     H N N 16  
A1IPM H4     H N N 17  
A1IPM H5     H N N 18  
A1IPM H6     H N N 19  
A1IPM H7     H N N 20  
A1IPM H8     H N N 21  
A1IPM H9     H N N 22  
A1IPM H10    H N N 23  
A1IPM H11    H N N 24  
A1IPM H12    H N N 25  
A1IPM H13    H N N 26  
A1IPM H14    H N N 27  
ALA   N      N N N 28  
ALA   CA     C N S 29  
ALA   C      C N N 30  
ALA   O      O N N 31  
ALA   CB     C N N 32  
ALA   OXT    O N N 33  
ALA   H      H N N 34  
ALA   H2     H N N 35  
ALA   HA     H N N 36  
ALA   HB1    H N N 37  
ALA   HB2    H N N 38  
ALA   HB3    H N N 39  
ALA   HXT    H N N 40  
ARG   N      N N N 41  
ARG   CA     C N S 42  
ARG   C      C N N 43  
ARG   O      O N N 44  
ARG   CB     C N N 45  
ARG   CG     C N N 46  
ARG   CD     C N N 47  
ARG   NE     N N N 48  
ARG   CZ     C N N 49  
ARG   NH1    N N N 50  
ARG   NH2    N N N 51  
ARG   OXT    O N N 52  
ARG   H      H N N 53  
ARG   H2     H N N 54  
ARG   HA     H N N 55  
ARG   HB2    H N N 56  
ARG   HB3    H N N 57  
ARG   HG2    H N N 58  
ARG   HG3    H N N 59  
ARG   HD2    H N N 60  
ARG   HD3    H N N 61  
ARG   HE     H N N 62  
ARG   HH11   H N N 63  
ARG   HH12   H N N 64  
ARG   HH21   H N N 65  
ARG   HH22   H N N 66  
ARG   HXT    H N N 67  
ASN   N      N N N 68  
ASN   CA     C N S 69  
ASN   C      C N N 70  
ASN   O      O N N 71  
ASN   CB     C N N 72  
ASN   CG     C N N 73  
ASN   OD1    O N N 74  
ASN   ND2    N N N 75  
ASN   OXT    O N N 76  
ASN   H      H N N 77  
ASN   H2     H N N 78  
ASN   HA     H N N 79  
ASN   HB2    H N N 80  
ASN   HB3    H N N 81  
ASN   HD21   H N N 82  
ASN   HD22   H N N 83  
ASN   HXT    H N N 84  
ASP   N      N N N 85  
ASP   CA     C N S 86  
ASP   C      C N N 87  
ASP   O      O N N 88  
ASP   CB     C N N 89  
ASP   CG     C N N 90  
ASP   OD1    O N N 91  
ASP   OD2    O N N 92  
ASP   OXT    O N N 93  
ASP   H      H N N 94  
ASP   H2     H N N 95  
ASP   HA     H N N 96  
ASP   HB2    H N N 97  
ASP   HB3    H N N 98  
ASP   HD2    H N N 99  
ASP   HXT    H N N 100 
CYS   N      N N N 101 
CYS   CA     C N R 102 
CYS   C      C N N 103 
CYS   O      O N N 104 
CYS   CB     C N N 105 
CYS   SG     S N N 106 
CYS   OXT    O N N 107 
CYS   H      H N N 108 
CYS   H2     H N N 109 
CYS   HA     H N N 110 
CYS   HB2    H N N 111 
CYS   HB3    H N N 112 
CYS   HG     H N N 113 
CYS   HXT    H N N 114 
GLN   N      N N N 115 
GLN   CA     C N S 116 
GLN   C      C N N 117 
GLN   O      O N N 118 
GLN   CB     C N N 119 
GLN   CG     C N N 120 
GLN   CD     C N N 121 
GLN   OE1    O N N 122 
GLN   NE2    N N N 123 
GLN   OXT    O N N 124 
GLN   H      H N N 125 
GLN   H2     H N N 126 
GLN   HA     H N N 127 
GLN   HB2    H N N 128 
GLN   HB3    H N N 129 
GLN   HG2    H N N 130 
GLN   HG3    H N N 131 
GLN   HE21   H N N 132 
GLN   HE22   H N N 133 
GLN   HXT    H N N 134 
GLU   N      N N N 135 
GLU   CA     C N S 136 
GLU   C      C N N 137 
GLU   O      O N N 138 
GLU   CB     C N N 139 
GLU   CG     C N N 140 
GLU   CD     C N N 141 
GLU   OE1    O N N 142 
GLU   OE2    O N N 143 
GLU   OXT    O N N 144 
GLU   H      H N N 145 
GLU   H2     H N N 146 
GLU   HA     H N N 147 
GLU   HB2    H N N 148 
GLU   HB3    H N N 149 
GLU   HG2    H N N 150 
GLU   HG3    H N N 151 
GLU   HE2    H N N 152 
GLU   HXT    H N N 153 
GLY   N      N N N 154 
GLY   CA     C N N 155 
GLY   C      C N N 156 
GLY   O      O N N 157 
GLY   OXT    O N N 158 
GLY   H      H N N 159 
GLY   H2     H N N 160 
GLY   HA2    H N N 161 
GLY   HA3    H N N 162 
GLY   HXT    H N N 163 
HIS   N      N N N 164 
HIS   CA     C N S 165 
HIS   C      C N N 166 
HIS   O      O N N 167 
HIS   CB     C N N 168 
HIS   CG     C Y N 169 
HIS   ND1    N Y N 170 
HIS   CD2    C Y N 171 
HIS   CE1    C Y N 172 
HIS   NE2    N Y N 173 
HIS   OXT    O N N 174 
HIS   H      H N N 175 
HIS   H2     H N N 176 
HIS   HA     H N N 177 
HIS   HB2    H N N 178 
HIS   HB3    H N N 179 
HIS   HD1    H N N 180 
HIS   HD2    H N N 181 
HIS   HE1    H N N 182 
HIS   HE2    H N N 183 
HIS   HXT    H N N 184 
HOH   O      O N N 185 
HOH   H1     H N N 186 
HOH   H2     H N N 187 
ILE   N      N N N 188 
ILE   CA     C N S 189 
ILE   C      C N N 190 
ILE   O      O N N 191 
ILE   CB     C N S 192 
ILE   CG1    C N N 193 
ILE   CG2    C N N 194 
ILE   CD1    C N N 195 
ILE   OXT    O N N 196 
ILE   H      H N N 197 
ILE   H2     H N N 198 
ILE   HA     H N N 199 
ILE   HB     H N N 200 
ILE   HG12   H N N 201 
ILE   HG13   H N N 202 
ILE   HG21   H N N 203 
ILE   HG22   H N N 204 
ILE   HG23   H N N 205 
ILE   HD11   H N N 206 
ILE   HD12   H N N 207 
ILE   HD13   H N N 208 
ILE   HXT    H N N 209 
LEU   N      N N N 210 
LEU   CA     C N S 211 
LEU   C      C N N 212 
LEU   O      O N N 213 
LEU   CB     C N N 214 
LEU   CG     C N N 215 
LEU   CD1    C N N 216 
LEU   CD2    C N N 217 
LEU   OXT    O N N 218 
LEU   H      H N N 219 
LEU   H2     H N N 220 
LEU   HA     H N N 221 
LEU   HB2    H N N 222 
LEU   HB3    H N N 223 
LEU   HG     H N N 224 
LEU   HD11   H N N 225 
LEU   HD12   H N N 226 
LEU   HD13   H N N 227 
LEU   HD21   H N N 228 
LEU   HD22   H N N 229 
LEU   HD23   H N N 230 
LEU   HXT    H N N 231 
LYS   N      N N N 232 
LYS   CA     C N S 233 
LYS   C      C N N 234 
LYS   O      O N N 235 
LYS   CB     C N N 236 
LYS   CG     C N N 237 
LYS   CD     C N N 238 
LYS   CE     C N N 239 
LYS   NZ     N N N 240 
LYS   OXT    O N N 241 
LYS   H      H N N 242 
LYS   H2     H N N 243 
LYS   HA     H N N 244 
LYS   HB2    H N N 245 
LYS   HB3    H N N 246 
LYS   HG2    H N N 247 
LYS   HG3    H N N 248 
LYS   HD2    H N N 249 
LYS   HD3    H N N 250 
LYS   HE2    H N N 251 
LYS   HE3    H N N 252 
LYS   HZ1    H N N 253 
LYS   HZ2    H N N 254 
LYS   HZ3    H N N 255 
LYS   HXT    H N N 256 
MET   N      N N N 257 
MET   CA     C N S 258 
MET   C      C N N 259 
MET   O      O N N 260 
MET   CB     C N N 261 
MET   CG     C N N 262 
MET   SD     S N N 263 
MET   CE     C N N 264 
MET   OXT    O N N 265 
MET   H      H N N 266 
MET   H2     H N N 267 
MET   HA     H N N 268 
MET   HB2    H N N 269 
MET   HB3    H N N 270 
MET   HG2    H N N 271 
MET   HG3    H N N 272 
MET   HE1    H N N 273 
MET   HE2    H N N 274 
MET   HE3    H N N 275 
MET   HXT    H N N 276 
PHE   N      N N N 277 
PHE   CA     C N S 278 
PHE   C      C N N 279 
PHE   O      O N N 280 
PHE   CB     C N N 281 
PHE   CG     C Y N 282 
PHE   CD1    C Y N 283 
PHE   CD2    C Y N 284 
PHE   CE1    C Y N 285 
PHE   CE2    C Y N 286 
PHE   CZ     C Y N 287 
PHE   OXT    O N N 288 
PHE   H      H N N 289 
PHE   H2     H N N 290 
PHE   HA     H N N 291 
PHE   HB2    H N N 292 
PHE   HB3    H N N 293 
PHE   HD1    H N N 294 
PHE   HD2    H N N 295 
PHE   HE1    H N N 296 
PHE   HE2    H N N 297 
PHE   HZ     H N N 298 
PHE   HXT    H N N 299 
PRO   N      N N N 300 
PRO   CA     C N S 301 
PRO   C      C N N 302 
PRO   O      O N N 303 
PRO   CB     C N N 304 
PRO   CG     C N N 305 
PRO   CD     C N N 306 
PRO   OXT    O N N 307 
PRO   H      H N N 308 
PRO   HA     H N N 309 
PRO   HB2    H N N 310 
PRO   HB3    H N N 311 
PRO   HG2    H N N 312 
PRO   HG3    H N N 313 
PRO   HD2    H N N 314 
PRO   HD3    H N N 315 
PRO   HXT    H N N 316 
SAH   N      N N N 317 
SAH   CA     C N S 318 
SAH   CB     C N N 319 
SAH   CG     C N N 320 
SAH   SD     S N N 321 
SAH   C      C N N 322 
SAH   O      O N N 323 
SAH   OXT    O N N 324 
SAH   "C5'"  C N N 325 
SAH   "C4'"  C N S 326 
SAH   "O4'"  O N N 327 
SAH   "C3'"  C N S 328 
SAH   "O3'"  O N N 329 
SAH   "C2'"  C N R 330 
SAH   "O2'"  O N N 331 
SAH   "C1'"  C N R 332 
SAH   N9     N Y N 333 
SAH   C8     C Y N 334 
SAH   N7     N Y N 335 
SAH   C5     C Y N 336 
SAH   C6     C Y N 337 
SAH   N6     N N N 338 
SAH   N1     N Y N 339 
SAH   C2     C Y N 340 
SAH   N3     N Y N 341 
SAH   C4     C Y N 342 
SAH   HN1    H N N 343 
SAH   HN2    H N N 344 
SAH   HA     H N N 345 
SAH   HB1    H N N 346 
SAH   HB2    H N N 347 
SAH   HG1    H N N 348 
SAH   HG2    H N N 349 
SAH   HXT    H N N 350 
SAH   "H5'1" H N N 351 
SAH   "H5'2" H N N 352 
SAH   "H4'"  H N N 353 
SAH   "H3'"  H N N 354 
SAH   "HO3'" H N N 355 
SAH   "H2'"  H N N 356 
SAH   "HO2'" H N N 357 
SAH   "H1'"  H N N 358 
SAH   H8     H N N 359 
SAH   HN61   H N N 360 
SAH   HN62   H N N 361 
SAH   H2     H N N 362 
SER   N      N N N 363 
SER   CA     C N S 364 
SER   C      C N N 365 
SER   O      O N N 366 
SER   CB     C N N 367 
SER   OG     O N N 368 
SER   OXT    O N N 369 
SER   H      H N N 370 
SER   H2     H N N 371 
SER   HA     H N N 372 
SER   HB2    H N N 373 
SER   HB3    H N N 374 
SER   HG     H N N 375 
SER   HXT    H N N 376 
THR   N      N N N 377 
THR   CA     C N S 378 
THR   C      C N N 379 
THR   O      O N N 380 
THR   CB     C N R 381 
THR   OG1    O N N 382 
THR   CG2    C N N 383 
THR   OXT    O N N 384 
THR   H      H N N 385 
THR   H2     H N N 386 
THR   HA     H N N 387 
THR   HB     H N N 388 
THR   HG1    H N N 389 
THR   HG21   H N N 390 
THR   HG22   H N N 391 
THR   HG23   H N N 392 
THR   HXT    H N N 393 
TRP   N      N N N 394 
TRP   CA     C N S 395 
TRP   C      C N N 396 
TRP   O      O N N 397 
TRP   CB     C N N 398 
TRP   CG     C Y N 399 
TRP   CD1    C Y N 400 
TRP   CD2    C Y N 401 
TRP   NE1    N Y N 402 
TRP   CE2    C Y N 403 
TRP   CE3    C Y N 404 
TRP   CZ2    C Y N 405 
TRP   CZ3    C Y N 406 
TRP   CH2    C Y N 407 
TRP   OXT    O N N 408 
TRP   H      H N N 409 
TRP   H2     H N N 410 
TRP   HA     H N N 411 
TRP   HB2    H N N 412 
TRP   HB3    H N N 413 
TRP   HD1    H N N 414 
TRP   HE1    H N N 415 
TRP   HE3    H N N 416 
TRP   HZ2    H N N 417 
TRP   HZ3    H N N 418 
TRP   HH2    H N N 419 
TRP   HXT    H N N 420 
TYR   N      N N N 421 
TYR   CA     C N S 422 
TYR   C      C N N 423 
TYR   O      O N N 424 
TYR   CB     C N N 425 
TYR   CG     C Y N 426 
TYR   CD1    C Y N 427 
TYR   CD2    C Y N 428 
TYR   CE1    C Y N 429 
TYR   CE2    C Y N 430 
TYR   CZ     C Y N 431 
TYR   OH     O N N 432 
TYR   OXT    O N N 433 
TYR   H      H N N 434 
TYR   H2     H N N 435 
TYR   HA     H N N 436 
TYR   HB2    H N N 437 
TYR   HB3    H N N 438 
TYR   HD1    H N N 439 
TYR   HD2    H N N 440 
TYR   HE1    H N N 441 
TYR   HE2    H N N 442 
TYR   HH     H N N 443 
TYR   HXT    H N N 444 
VAL   N      N N N 445 
VAL   CA     C N S 446 
VAL   C      C N N 447 
VAL   O      O N N 448 
VAL   CB     C N N 449 
VAL   CG1    C N N 450 
VAL   CG2    C N N 451 
VAL   OXT    O N N 452 
VAL   H      H N N 453 
VAL   H2     H N N 454 
VAL   HA     H N N 455 
VAL   HB     H N N 456 
VAL   HG11   H N N 457 
VAL   HG12   H N N 458 
VAL   HG13   H N N 459 
VAL   HG21   H N N 460 
VAL   HG22   H N N 461 
VAL   HG23   H N N 462 
VAL   HXT    H N N 463 
# 
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 
A1IPM O12   C11    doub N N 1   
A1IPM N13   C11    sing N N 2   
A1IPM C11   C7     sing N N 3   
A1IPM C7    C8     doub Y N 4   
A1IPM C7    C5     sing Y N 5   
A1IPM C6    C5     sing N N 6   
A1IPM C8    N9     sing Y N 7   
A1IPM C5    C4     doub Y N 8   
A1IPM N9    C10    sing N N 9   
A1IPM N9    C3     doub Y N 10  
A1IPM C4    C3     sing Y N 11  
A1IPM C3    N2     sing N N 12  
A1IPM N2    C1     sing N N 13  
A1IPM C1    H1     sing N N 14  
A1IPM C1    H2     sing N N 15  
A1IPM C1    H3     sing N N 16  
A1IPM C8    H4     sing N N 17  
A1IPM C10   H5     sing N N 18  
A1IPM C10   H6     sing N N 19  
A1IPM C10   H7     sing N N 20  
A1IPM N2    H8     sing N N 21  
A1IPM C4    H9     sing N N 22  
A1IPM C6    H10    sing N N 23  
A1IPM C6    H11    sing N N 24  
A1IPM C6    H12    sing N N 25  
A1IPM N13   H13    sing N N 26  
A1IPM N13   H14    sing N N 27  
ALA   N     CA     sing N N 28  
ALA   N     H      sing N N 29  
ALA   N     H2     sing N N 30  
ALA   CA    C      sing N N 31  
ALA   CA    CB     sing N N 32  
ALA   CA    HA     sing N N 33  
ALA   C     O      doub N N 34  
ALA   C     OXT    sing N N 35  
ALA   CB    HB1    sing N N 36  
ALA   CB    HB2    sing N N 37  
ALA   CB    HB3    sing N N 38  
ALA   OXT   HXT    sing N N 39  
ARG   N     CA     sing N N 40  
ARG   N     H      sing N N 41  
ARG   N     H2     sing N N 42  
ARG   CA    C      sing N N 43  
ARG   CA    CB     sing N N 44  
ARG   CA    HA     sing N N 45  
ARG   C     O      doub N N 46  
ARG   C     OXT    sing N N 47  
ARG   CB    CG     sing N N 48  
ARG   CB    HB2    sing N N 49  
ARG   CB    HB3    sing N N 50  
ARG   CG    CD     sing N N 51  
ARG   CG    HG2    sing N N 52  
ARG   CG    HG3    sing N N 53  
ARG   CD    NE     sing N N 54  
ARG   CD    HD2    sing N N 55  
ARG   CD    HD3    sing N N 56  
ARG   NE    CZ     sing N N 57  
ARG   NE    HE     sing N N 58  
ARG   CZ    NH1    sing N N 59  
ARG   CZ    NH2    doub N N 60  
ARG   NH1   HH11   sing N N 61  
ARG   NH1   HH12   sing N N 62  
ARG   NH2   HH21   sing N N 63  
ARG   NH2   HH22   sing N N 64  
ARG   OXT   HXT    sing N N 65  
ASN   N     CA     sing N N 66  
ASN   N     H      sing N N 67  
ASN   N     H2     sing N N 68  
ASN   CA    C      sing N N 69  
ASN   CA    CB     sing N N 70  
ASN   CA    HA     sing N N 71  
ASN   C     O      doub N N 72  
ASN   C     OXT    sing N N 73  
ASN   CB    CG     sing N N 74  
ASN   CB    HB2    sing N N 75  
ASN   CB    HB3    sing N N 76  
ASN   CG    OD1    doub N N 77  
ASN   CG    ND2    sing N N 78  
ASN   ND2   HD21   sing N N 79  
ASN   ND2   HD22   sing N N 80  
ASN   OXT   HXT    sing N N 81  
ASP   N     CA     sing N N 82  
ASP   N     H      sing N N 83  
ASP   N     H2     sing N N 84  
ASP   CA    C      sing N N 85  
ASP   CA    CB     sing N N 86  
ASP   CA    HA     sing N N 87  
ASP   C     O      doub N N 88  
ASP   C     OXT    sing N N 89  
ASP   CB    CG     sing N N 90  
ASP   CB    HB2    sing N N 91  
ASP   CB    HB3    sing N N 92  
ASP   CG    OD1    doub N N 93  
ASP   CG    OD2    sing N N 94  
ASP   OD2   HD2    sing N N 95  
ASP   OXT   HXT    sing N N 96  
CYS   N     CA     sing N N 97  
CYS   N     H      sing N N 98  
CYS   N     H2     sing N N 99  
CYS   CA    C      sing N N 100 
CYS   CA    CB     sing N N 101 
CYS   CA    HA     sing N N 102 
CYS   C     O      doub N N 103 
CYS   C     OXT    sing N N 104 
CYS   CB    SG     sing N N 105 
CYS   CB    HB2    sing N N 106 
CYS   CB    HB3    sing N N 107 
CYS   SG    HG     sing N N 108 
CYS   OXT   HXT    sing N N 109 
GLN   N     CA     sing N N 110 
GLN   N     H      sing N N 111 
GLN   N     H2     sing N N 112 
GLN   CA    C      sing N N 113 
GLN   CA    CB     sing N N 114 
GLN   CA    HA     sing N N 115 
GLN   C     O      doub N N 116 
GLN   C     OXT    sing N N 117 
GLN   CB    CG     sing N N 118 
GLN   CB    HB2    sing N N 119 
GLN   CB    HB3    sing N N 120 
GLN   CG    CD     sing N N 121 
GLN   CG    HG2    sing N N 122 
GLN   CG    HG3    sing N N 123 
GLN   CD    OE1    doub N N 124 
GLN   CD    NE2    sing N N 125 
GLN   NE2   HE21   sing N N 126 
GLN   NE2   HE22   sing N N 127 
GLN   OXT   HXT    sing N N 128 
GLU   N     CA     sing N N 129 
GLU   N     H      sing N N 130 
GLU   N     H2     sing N N 131 
GLU   CA    C      sing N N 132 
GLU   CA    CB     sing N N 133 
GLU   CA    HA     sing N N 134 
GLU   C     O      doub N N 135 
GLU   C     OXT    sing N N 136 
GLU   CB    CG     sing N N 137 
GLU   CB    HB2    sing N N 138 
GLU   CB    HB3    sing N N 139 
GLU   CG    CD     sing N N 140 
GLU   CG    HG2    sing N N 141 
GLU   CG    HG3    sing N N 142 
GLU   CD    OE1    doub N N 143 
GLU   CD    OE2    sing N N 144 
GLU   OE2   HE2    sing N N 145 
GLU   OXT   HXT    sing N N 146 
GLY   N     CA     sing N N 147 
GLY   N     H      sing N N 148 
GLY   N     H2     sing N N 149 
GLY   CA    C      sing N N 150 
GLY   CA    HA2    sing N N 151 
GLY   CA    HA3    sing N N 152 
GLY   C     O      doub N N 153 
GLY   C     OXT    sing N N 154 
GLY   OXT   HXT    sing N N 155 
HIS   N     CA     sing N N 156 
HIS   N     H      sing N N 157 
HIS   N     H2     sing N N 158 
HIS   CA    C      sing N N 159 
HIS   CA    CB     sing N N 160 
HIS   CA    HA     sing N N 161 
HIS   C     O      doub N N 162 
HIS   C     OXT    sing N N 163 
HIS   CB    CG     sing N N 164 
HIS   CB    HB2    sing N N 165 
HIS   CB    HB3    sing N N 166 
HIS   CG    ND1    sing Y N 167 
HIS   CG    CD2    doub Y N 168 
HIS   ND1   CE1    doub Y N 169 
HIS   ND1   HD1    sing N N 170 
HIS   CD2   NE2    sing Y N 171 
HIS   CD2   HD2    sing N N 172 
HIS   CE1   NE2    sing Y N 173 
HIS   CE1   HE1    sing N N 174 
HIS   NE2   HE2    sing N N 175 
HIS   OXT   HXT    sing N N 176 
HOH   O     H1     sing N N 177 
HOH   O     H2     sing N N 178 
ILE   N     CA     sing N N 179 
ILE   N     H      sing N N 180 
ILE   N     H2     sing N N 181 
ILE   CA    C      sing N N 182 
ILE   CA    CB     sing N N 183 
ILE   CA    HA     sing N N 184 
ILE   C     O      doub N N 185 
ILE   C     OXT    sing N N 186 
ILE   CB    CG1    sing N N 187 
ILE   CB    CG2    sing N N 188 
ILE   CB    HB     sing N N 189 
ILE   CG1   CD1    sing N N 190 
ILE   CG1   HG12   sing N N 191 
ILE   CG1   HG13   sing N N 192 
ILE   CG2   HG21   sing N N 193 
ILE   CG2   HG22   sing N N 194 
ILE   CG2   HG23   sing N N 195 
ILE   CD1   HD11   sing N N 196 
ILE   CD1   HD12   sing N N 197 
ILE   CD1   HD13   sing N N 198 
ILE   OXT   HXT    sing N N 199 
LEU   N     CA     sing N N 200 
LEU   N     H      sing N N 201 
LEU   N     H2     sing N N 202 
LEU   CA    C      sing N N 203 
LEU   CA    CB     sing N N 204 
LEU   CA    HA     sing N N 205 
LEU   C     O      doub N N 206 
LEU   C     OXT    sing N N 207 
LEU   CB    CG     sing N N 208 
LEU   CB    HB2    sing N N 209 
LEU   CB    HB3    sing N N 210 
LEU   CG    CD1    sing N N 211 
LEU   CG    CD2    sing N N 212 
LEU   CG    HG     sing N N 213 
LEU   CD1   HD11   sing N N 214 
LEU   CD1   HD12   sing N N 215 
LEU   CD1   HD13   sing N N 216 
LEU   CD2   HD21   sing N N 217 
LEU   CD2   HD22   sing N N 218 
LEU   CD2   HD23   sing N N 219 
LEU   OXT   HXT    sing N N 220 
LYS   N     CA     sing N N 221 
LYS   N     H      sing N N 222 
LYS   N     H2     sing N N 223 
LYS   CA    C      sing N N 224 
LYS   CA    CB     sing N N 225 
LYS   CA    HA     sing N N 226 
LYS   C     O      doub N N 227 
LYS   C     OXT    sing N N 228 
LYS   CB    CG     sing N N 229 
LYS   CB    HB2    sing N N 230 
LYS   CB    HB3    sing N N 231 
LYS   CG    CD     sing N N 232 
LYS   CG    HG2    sing N N 233 
LYS   CG    HG3    sing N N 234 
LYS   CD    CE     sing N N 235 
LYS   CD    HD2    sing N N 236 
LYS   CD    HD3    sing N N 237 
LYS   CE    NZ     sing N N 238 
LYS   CE    HE2    sing N N 239 
LYS   CE    HE3    sing N N 240 
LYS   NZ    HZ1    sing N N 241 
LYS   NZ    HZ2    sing N N 242 
LYS   NZ    HZ3    sing N N 243 
LYS   OXT   HXT    sing N N 244 
MET   N     CA     sing N N 245 
MET   N     H      sing N N 246 
MET   N     H2     sing N N 247 
MET   CA    C      sing N N 248 
MET   CA    CB     sing N N 249 
MET   CA    HA     sing N N 250 
MET   C     O      doub N N 251 
MET   C     OXT    sing N N 252 
MET   CB    CG     sing N N 253 
MET   CB    HB2    sing N N 254 
MET   CB    HB3    sing N N 255 
MET   CG    SD     sing N N 256 
MET   CG    HG2    sing N N 257 
MET   CG    HG3    sing N N 258 
MET   SD    CE     sing N N 259 
MET   CE    HE1    sing N N 260 
MET   CE    HE2    sing N N 261 
MET   CE    HE3    sing N N 262 
MET   OXT   HXT    sing N N 263 
PHE   N     CA     sing N N 264 
PHE   N     H      sing N N 265 
PHE   N     H2     sing N N 266 
PHE   CA    C      sing N N 267 
PHE   CA    CB     sing N N 268 
PHE   CA    HA     sing N N 269 
PHE   C     O      doub N N 270 
PHE   C     OXT    sing N N 271 
PHE   CB    CG     sing N N 272 
PHE   CB    HB2    sing N N 273 
PHE   CB    HB3    sing N N 274 
PHE   CG    CD1    doub Y N 275 
PHE   CG    CD2    sing Y N 276 
PHE   CD1   CE1    sing Y N 277 
PHE   CD1   HD1    sing N N 278 
PHE   CD2   CE2    doub Y N 279 
PHE   CD2   HD2    sing N N 280 
PHE   CE1   CZ     doub Y N 281 
PHE   CE1   HE1    sing N N 282 
PHE   CE2   CZ     sing Y N 283 
PHE   CE2   HE2    sing N N 284 
PHE   CZ    HZ     sing N N 285 
PHE   OXT   HXT    sing N N 286 
PRO   N     CA     sing N N 287 
PRO   N     CD     sing N N 288 
PRO   N     H      sing N N 289 
PRO   CA    C      sing N N 290 
PRO   CA    CB     sing N N 291 
PRO   CA    HA     sing N N 292 
PRO   C     O      doub N N 293 
PRO   C     OXT    sing N N 294 
PRO   CB    CG     sing N N 295 
PRO   CB    HB2    sing N N 296 
PRO   CB    HB3    sing N N 297 
PRO   CG    CD     sing N N 298 
PRO   CG    HG2    sing N N 299 
PRO   CG    HG3    sing N N 300 
PRO   CD    HD2    sing N N 301 
PRO   CD    HD3    sing N N 302 
PRO   OXT   HXT    sing N N 303 
SAH   N     CA     sing N N 304 
SAH   N     HN1    sing N N 305 
SAH   N     HN2    sing N N 306 
SAH   CA    CB     sing N N 307 
SAH   CA    C      sing N N 308 
SAH   CA    HA     sing N N 309 
SAH   CB    CG     sing N N 310 
SAH   CB    HB1    sing N N 311 
SAH   CB    HB2    sing N N 312 
SAH   CG    SD     sing N N 313 
SAH   CG    HG1    sing N N 314 
SAH   CG    HG2    sing N N 315 
SAH   SD    "C5'"  sing N N 316 
SAH   C     O      doub N N 317 
SAH   C     OXT    sing N N 318 
SAH   OXT   HXT    sing N N 319 
SAH   "C5'" "C4'"  sing N N 320 
SAH   "C5'" "H5'1" sing N N 321 
SAH   "C5'" "H5'2" sing N N 322 
SAH   "C4'" "O4'"  sing N N 323 
SAH   "C4'" "C3'"  sing N N 324 
SAH   "C4'" "H4'"  sing N N 325 
SAH   "O4'" "C1'"  sing N N 326 
SAH   "C3'" "O3'"  sing N N 327 
SAH   "C3'" "C2'"  sing N N 328 
SAH   "C3'" "H3'"  sing N N 329 
SAH   "O3'" "HO3'" sing N N 330 
SAH   "C2'" "O2'"  sing N N 331 
SAH   "C2'" "C1'"  sing N N 332 
SAH   "C2'" "H2'"  sing N N 333 
SAH   "O2'" "HO2'" sing N N 334 
SAH   "C1'" N9     sing N N 335 
SAH   "C1'" "H1'"  sing N N 336 
SAH   N9    C8     sing Y N 337 
SAH   N9    C4     sing Y N 338 
SAH   C8    N7     doub Y N 339 
SAH   C8    H8     sing N N 340 
SAH   N7    C5     sing Y N 341 
SAH   C5    C6     sing Y N 342 
SAH   C5    C4     doub Y N 343 
SAH   C6    N6     sing N N 344 
SAH   C6    N1     doub Y N 345 
SAH   N6    HN61   sing N N 346 
SAH   N6    HN62   sing N N 347 
SAH   N1    C2     sing Y N 348 
SAH   C2    N3     doub Y N 349 
SAH   C2    H2     sing N N 350 
SAH   N3    C4     sing Y N 351 
SER   N     CA     sing N N 352 
SER   N     H      sing N N 353 
SER   N     H2     sing N N 354 
SER   CA    C      sing N N 355 
SER   CA    CB     sing N N 356 
SER   CA    HA     sing N N 357 
SER   C     O      doub N N 358 
SER   C     OXT    sing N N 359 
SER   CB    OG     sing N N 360 
SER   CB    HB2    sing N N 361 
SER   CB    HB3    sing N N 362 
SER   OG    HG     sing N N 363 
SER   OXT   HXT    sing N N 364 
THR   N     CA     sing N N 365 
THR   N     H      sing N N 366 
THR   N     H2     sing N N 367 
THR   CA    C      sing N N 368 
THR   CA    CB     sing N N 369 
THR   CA    HA     sing N N 370 
THR   C     O      doub N N 371 
THR   C     OXT    sing N N 372 
THR   CB    OG1    sing N N 373 
THR   CB    CG2    sing N N 374 
THR   CB    HB     sing N N 375 
THR   OG1   HG1    sing N N 376 
THR   CG2   HG21   sing N N 377 
THR   CG2   HG22   sing N N 378 
THR   CG2   HG23   sing N N 379 
THR   OXT   HXT    sing N N 380 
TRP   N     CA     sing N N 381 
TRP   N     H      sing N N 382 
TRP   N     H2     sing N N 383 
TRP   CA    C      sing N N 384 
TRP   CA    CB     sing N N 385 
TRP   CA    HA     sing N N 386 
TRP   C     O      doub N N 387 
TRP   C     OXT    sing N N 388 
TRP   CB    CG     sing N N 389 
TRP   CB    HB2    sing N N 390 
TRP   CB    HB3    sing N N 391 
TRP   CG    CD1    doub Y N 392 
TRP   CG    CD2    sing Y N 393 
TRP   CD1   NE1    sing Y N 394 
TRP   CD1   HD1    sing N N 395 
TRP   CD2   CE2    doub Y N 396 
TRP   CD2   CE3    sing Y N 397 
TRP   NE1   CE2    sing Y N 398 
TRP   NE1   HE1    sing N N 399 
TRP   CE2   CZ2    sing Y N 400 
TRP   CE3   CZ3    doub Y N 401 
TRP   CE3   HE3    sing N N 402 
TRP   CZ2   CH2    doub Y N 403 
TRP   CZ2   HZ2    sing N N 404 
TRP   CZ3   CH2    sing Y N 405 
TRP   CZ3   HZ3    sing N N 406 
TRP   CH2   HH2    sing N N 407 
TRP   OXT   HXT    sing N N 408 
TYR   N     CA     sing N N 409 
TYR   N     H      sing N N 410 
TYR   N     H2     sing N N 411 
TYR   CA    C      sing N N 412 
TYR   CA    CB     sing N N 413 
TYR   CA    HA     sing N N 414 
TYR   C     O      doub N N 415 
TYR   C     OXT    sing N N 416 
TYR   CB    CG     sing N N 417 
TYR   CB    HB2    sing N N 418 
TYR   CB    HB3    sing N N 419 
TYR   CG    CD1    doub Y N 420 
TYR   CG    CD2    sing Y N 421 
TYR   CD1   CE1    sing Y N 422 
TYR   CD1   HD1    sing N N 423 
TYR   CD2   CE2    doub Y N 424 
TYR   CD2   HD2    sing N N 425 
TYR   CE1   CZ     doub Y N 426 
TYR   CE1   HE1    sing N N 427 
TYR   CE2   CZ     sing Y N 428 
TYR   CE2   HE2    sing N N 429 
TYR   CZ    OH     sing N N 430 
TYR   OH    HH     sing N N 431 
TYR   OXT   HXT    sing N N 432 
VAL   N     CA     sing N N 433 
VAL   N     H      sing N N 434 
VAL   N     H2     sing N N 435 
VAL   CA    C      sing N N 436 
VAL   CA    CB     sing N N 437 
VAL   CA    HA     sing N N 438 
VAL   C     O      doub N N 439 
VAL   C     OXT    sing N N 440 
VAL   CB    CG1    sing N N 441 
VAL   CB    CG2    sing N N 442 
VAL   CB    HB     sing N N 443 
VAL   CG1   HG11   sing N N 444 
VAL   CG1   HG12   sing N N 445 
VAL   CG1   HG13   sing N N 446 
VAL   CG2   HG21   sing N N 447 
VAL   CG2   HG22   sing N N 448 
VAL   CG2   HG23   sing N N 449 
VAL   OXT   HXT    sing N N 450 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   5XVK 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9H5O 
_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]   0.016057 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014345 
_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]   0.008731 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . PHE   A 1 24  ? 0.467   -12.315 90.96  1   4.22  ? 5   PHE   B N     1 
ATOM   2    C CA    . PHE   A 1 24  ? 0.578   -13.003 89.664 1   3     ? 5   PHE   B CA    1 
ATOM   3    C C     . PHE   A 1 24  ? -0.29   -12.311 88.609 1   5.42  ? 5   PHE   B C     1 
ATOM   4    O O     . PHE   A 1 24  ? -1.433  -11.924 88.917 1   4.76  ? 5   PHE   B O     1 
ATOM   5    C CB    . PHE   A 1 24  ? 0.15    -14.477 89.804 1   3.5   ? 5   PHE   B CB    1 
ATOM   6    C CG    . PHE   A 1 24  ? 0.737   -15.408 88.757 1   3.19  ? 5   PHE   B CG    1 
ATOM   7    C CD1   . PHE   A 1 24  ? 1.918   -16.104 89.006 1   4.58  ? 5   PHE   B CD1   1 
ATOM   8    C CD2   . PHE   A 1 24  ? 0.091   -15.611 87.535 1   3.58  ? 5   PHE   B CD2   1 
ATOM   9    C CE1   . PHE   A 1 24  ? 2.465   -16.96  88.034 1   4.28  ? 5   PHE   B CE1   1 
ATOM   10   C CE2   . PHE   A 1 24  ? 0.637   -16.473 86.567 1   5.18  ? 5   PHE   B CE2   1 
ATOM   11   C CZ    . PHE   A 1 24  ? 1.823   -17.129 86.822 1   3     ? 5   PHE   B CZ    1 
ATOM   12   N N     . THR   A 1 25  ? 0.243   -12.149 87.371 1   3     ? 6   THR   B N     1 
ATOM   13   C CA    . THR   A 1 25  ? -0.481  -11.553 86.223 1   3     ? 6   THR   B CA    1 
ATOM   14   C C     . THR   A 1 25  ? -1.919  -12.079 86.15  1   5.89  ? 6   THR   B C     1 
ATOM   15   O O     . THR   A 1 25  ? -2.124  -13.3   86.092 1   4.59  ? 6   THR   B O     1 
ATOM   16   C CB    . THR   A 1 25  ? 0.257   -11.852 84.884 1   5.15  ? 6   THR   B CB    1 
ATOM   17   O OG1   . THR   A 1 25  ? 1.544   -11.242 84.9   1   3     ? 6   THR   B OG1   1 
ATOM   18   C CG2   . THR   A 1 25  ? -0.537  -11.401 83.64  1   3     ? 6   THR   B CG2   1 
ATOM   19   N N     . SER   A 1 26  ? -2.913  -11.169 86.14  1   4.71  ? 7   SER   B N     1 
ATOM   20   C CA    . SER   A 1 26  ? -4.314  -11.586 85.999 1   5.18  ? 7   SER   B CA    1 
ATOM   21   C C     . SER   A 1 26  ? -4.561  -11.968 84.52  1   6.35  ? 7   SER   B C     1 
ATOM   22   O O     . SER   A 1 26  ? -3.952  -11.363 83.627 1   3.24  ? 7   SER   B O     1 
ATOM   23   C CB    . SER   A 1 26  ? -5.251  -10.464 86.433 1   10.48 ? 7   SER   B CB    1 
ATOM   24   O OG    . SER   A 1 26  ? -5.124  -9.335  85.584 1   12.2  ? 7   SER   B OG    1 
ATOM   25   N N     . LYS   A 1 27  ? -5.456  -12.943 84.251 1   4.99  ? 8   LYS   B N     1 
ATOM   26   C CA    . LYS   A 1 27  ? -5.683  -13.376 82.859 1   5.84  ? 8   LYS   B CA    1 
ATOM   27   C C     . LYS   A 1 27  ? -6.197  -12.259 81.958 1   7.96  ? 8   LYS   B C     1 
ATOM   28   O O     . LYS   A 1 27  ? -5.809  -12.224 80.788 1   6.9   ? 8   LYS   B O     1 
ATOM   29   C CB    . LYS   A 1 27  ? -6.538  -14.653 82.731 1   6.7   ? 8   LYS   B CB    1 
ATOM   30   C CG    . LYS   A 1 27  ? -7.941  -14.638 83.313 1   23.29 ? 8   LYS   B CG    1 
ATOM   31   C CD    . LYS   A 1 27  ? -8.363  -16.101 83.578 1   30.48 ? 8   LYS   B CD    1 
ATOM   32   C CE    . LYS   A 1 27  ? -9.78   -16.239 84.071 1   38.84 ? 8   LYS   B CE    1 
ATOM   33   N NZ    . LYS   A 1 27  ? -10.035 -17.604 84.596 1   40.68 ? 8   LYS   B NZ    1 
ATOM   34   N N     . ASP   A 1 28  ? -6.971  -11.283 82.499 1   6.6   ? 9   ASP   B N     1 
ATOM   35   C CA    . ASP   A 1 28  ? -7.434  -10.164 81.657 1   6.99  ? 9   ASP   B CA    1 
ATOM   36   C C     . ASP   A 1 28  ? -6.259  -9.32   81.088 1   8.03  ? 9   ASP   B C     1 
ATOM   37   O O     . ASP   A 1 28  ? -6.433  -8.626  80.08  1   6.93  ? 9   ASP   B O     1 
ATOM   38   C CB    . ASP   A 1 28  ? -8.46   -9.291  82.389 1   12.6  ? 9   ASP   B CB    1 
ATOM   39   C CG    . ASP   A 1 28  ? -7.906  -8.589  83.607 1   23.75 ? 9   ASP   B CG    1 
ATOM   40   O OD1   . ASP   A 1 28  ? -7.731  -7.364  83.547 1   29.75 ? 9   ASP   B OD1   1 
ATOM   41   O OD2   . ASP   A 1 28  ? -7.671  -9.266  84.626 1   33.57 ? 9   ASP   B OD2   1 
ATOM   42   N N     . THR   A 1 29  ? -5.056  -9.409  81.715 1   4.65  ? 10  THR   B N     1 
ATOM   43   C CA    . THR   A 1 29  ? -3.851  -8.696  81.248 1   4.43  ? 10  THR   B CA    1 
ATOM   44   C C     . THR   A 1 29  ? -3.42   -9.242  79.871 1   5.53  ? 10  THR   B C     1 
ATOM   45   O O     . THR   A 1 29  ? -2.904  -8.484  79.054 1   3.67  ? 10  THR   B O     1 
ATOM   46   C CB    . THR   A 1 29  ? -2.74   -8.726  82.324 1   8.59  ? 10  THR   B CB    1 
ATOM   47   O OG1   . THR   A 1 29  ? -3.281  -8.219  83.546 1   9.59  ? 10  THR   B OG1   1 
ATOM   48   C CG2   . THR   A 1 29  ? -1.497  -7.895  81.939 1   8.58  ? 10  THR   B CG2   1 
ATOM   49   N N     . TYR   A 1 30  ? -3.658  -10.548 79.608 1   3     ? 11  TYR   B N     1 
ATOM   50   C CA    . TYR   A 1 30  ? -3.368  -11.194 78.329 1   3     ? 11  TYR   B CA    1 
ATOM   51   C C     . TYR   A 1 30  ? -4.261  -10.676 77.208 1   6.33  ? 11  TYR   B C     1 
ATOM   52   O O     . TYR   A 1 30  ? -3.85   -10.658 76.044 1   4.05  ? 11  TYR   B O     1 
ATOM   53   C CB    . TYR   A 1 30  ? -3.456  -12.728 78.464 1   3     ? 11  TYR   B CB    1 
ATOM   54   C CG    . TYR   A 1 30  ? -2.175  -13.277 79.061 1   3     ? 11  TYR   B CG    1 
ATOM   55   C CD1   . TYR   A 1 30  ? -2.066  -13.513 80.429 1   4.08  ? 11  TYR   B CD1   1 
ATOM   56   C CD2   . TYR   A 1 30  ? -1.025  -13.404 78.287 1   3     ? 11  TYR   B CD2   1 
ATOM   57   C CE1   . TYR   A 1 30  ? -0.869  -13.965 80.995 1   4.03  ? 11  TYR   B CE1   1 
ATOM   58   C CE2   . TYR   A 1 30  ? 0.176   -13.843 78.839 1   3     ? 11  TYR   B CE2   1 
ATOM   59   C CZ    . TYR   A 1 30  ? 0.25    -14.132 80.19  1   4.8   ? 11  TYR   B CZ    1 
ATOM   60   O OH    . TYR   A 1 30  ? 1.457   -14.529 80.716 1   3     ? 11  TYR   B OH    1 
ATOM   61   N N     . LEU   A 1 31  ? -5.484  -10.241 77.558 1   3.2   ? 12  LEU   B N     1 
ATOM   62   C CA    . LEU   A 1 31  ? -6.404  -9.712  76.56  1   4.38  ? 12  LEU   B CA    1 
ATOM   63   C C     . LEU   A 1 31  ? -5.964  -8.342  76.022 1   7.91  ? 12  LEU   B C     1 
ATOM   64   O O     . LEU   A 1 31  ? -6.074  -8.082  74.824 1   7.8   ? 12  LEU   B O     1 
ATOM   65   C CB    . LEU   A 1 31  ? -7.821  -9.61   77.167 1   5.05  ? 12  LEU   B CB    1 
ATOM   66   C CG    . LEU   A 1 31  ? -8.465  -10.912 77.659 1   7.85  ? 12  LEU   B CG    1 
ATOM   67   C CD1   . LEU   A 1 31  ? -9.846  -10.638 78.248 1   9.62  ? 12  LEU   B CD1   1 
ATOM   68   C CD2   . LEU   A 1 31  ? -8.596  -11.931 76.52  1   7.2   ? 12  LEU   B CD2   1 
ATOM   69   N N     . SER   A 1 32  ? -5.462  -7.48   76.916 1   3.52  ? 13  SER   B N     1 
ATOM   70   C CA    . SER   A 1 32  ? -5.107  -6.095  76.622 1   4.28  ? 13  SER   B CA    1 
ATOM   71   C C     . SER   A 1 32  ? -3.614  -5.769  76.468 1   8.08  ? 13  SER   B C     1 
ATOM   72   O O     . SER   A 1 32  ? -3.273  -4.923  75.632 1   8.32  ? 13  SER   B O     1 
ATOM   73   C CB    . SER   A 1 32  ? -5.694  -5.194  77.706 1   7.55  ? 13  SER   B CB    1 
ATOM   74   O OG    . SER   A 1 32  ? -5.293  -5.66   78.988 1   9.9   ? 13  SER   B OG    1 
ATOM   75   N N     . HIS   A 1 33  ? -2.731  -6.372  77.297 1   3.82  ? 14  HIS   B N     1 
ATOM   76   C CA    . HIS   A 1 33  ? -1.312  -5.98   77.356 1   3.98  ? 14  HIS   B CA    1 
ATOM   77   C C     . HIS   A 1 33  ? -0.303  -6.917  76.694 1   5.58  ? 14  HIS   B C     1 
ATOM   78   O O     . HIS   A 1 33  ? 0.885   -6.586  76.656 1   3     ? 14  HIS   B O     1 
ATOM   79   C CB    . HIS   A 1 33  ? -0.912  -5.737  78.813 1   6.64  ? 14  HIS   B CB    1 
ATOM   80   C CG    . HIS   A 1 33  ? -1.548  -4.509  79.377 1   11.48 ? 14  HIS   B CG    1 
ATOM   81   N ND1   . HIS   A 1 33  ? -2.918  -4.422  79.54  1   11.96 ? 14  HIS   B ND1   1 
ATOM   82   C CD2   . HIS   A 1 33  ? -0.987  -3.338  79.751 1   12.94 ? 14  HIS   B CD2   1 
ATOM   83   C CE1   . HIS   A 1 33  ? -3.152  -3.21   80.019 1   13.66 ? 14  HIS   B CE1   1 
ATOM   84   N NE2   . HIS   A 1 33  ? -2.019  -2.515  80.164 1   14.23 ? 14  HIS   B NE2   1 
ATOM   85   N N     . PHE   A 1 34  ? -0.761  -8.046  76.153 1   3     ? 15  PHE   B N     1 
ATOM   86   C CA    . PHE   A 1 34  ? 0.125   -8.968  75.452 1   3     ? 15  PHE   B CA    1 
ATOM   87   C C     . PHE   A 1 34  ? 0.067   -8.528  73.999 1   5.63  ? 15  PHE   B C     1 
ATOM   88   O O     . PHE   A 1 34  ? -0.971  -8.712  73.343 1   3     ? 15  PHE   B O     1 
ATOM   89   C CB    . PHE   A 1 34  ? -0.364  -10.427 75.614 1   3.04  ? 15  PHE   B CB    1 
ATOM   90   C CG    . PHE   A 1 34  ? 0.577   -11.479 75.066 1   3     ? 15  PHE   B CG    1 
ATOM   91   C CD1   . PHE   A 1 34  ? 0.628   -11.749 73.698 1   3.79  ? 15  PHE   B CD1   1 
ATOM   92   C CD2   . PHE   A 1 34  ? 1.368   -12.241 75.92  1   3     ? 15  PHE   B CD2   1 
ATOM   93   C CE1   . PHE   A 1 34  ? 1.484   -12.736 73.193 1   4.12  ? 15  PHE   B CE1   1 
ATOM   94   C CE2   . PHE   A 1 34  ? 2.197   -13.251 75.419 1   5.63  ? 15  PHE   B CE2   1 
ATOM   95   C CZ    . PHE   A 1 34  ? 2.255   -13.486 74.059 1   3.39  ? 15  PHE   B CZ    1 
ATOM   96   N N     . ASN   A 1 35  ? 1.157   -7.902  73.511 1   3     ? 16  ASN   B N     1 
ATOM   97   C CA    . ASN   A 1 35  ? 1.245   -7.432  72.12  1   3     ? 16  ASN   B CA    1 
ATOM   98   C C     . ASN   A 1 35  ? 1.754   -8.591  71.219 1   4.99  ? 16  ASN   B C     1 
ATOM   99   O O     . ASN   A 1 35  ? 2.957   -8.905  71.277 1   3.72  ? 16  ASN   B O     1 
ATOM   100  C CB    . ASN   A 1 35  ? 2.147   -6.184  72.012 1   3     ? 16  ASN   B CB    1 
ATOM   101  C CG    . ASN   A 1 35  ? 2.131   -5.542  70.641 1   15.7  ? 16  ASN   B CG    1 
ATOM   102  O OD1   . ASN   A 1 35  ? 2.281   -6.197  69.602 1   15.27 ? 16  ASN   B OD1   1 
ATOM   103  N ND2   . ASN   A 1 35  ? 1.95    -4.234  70.608 1   21.42 ? 16  ASN   B ND2   1 
ATOM   104  N N     . PRO   A 1 36  ? 0.882   -9.233  70.391 1   3     ? 17  PRO   B N     1 
ATOM   105  C CA    . PRO   A 1 36  ? 1.35    -10.388 69.586 1   3     ? 17  PRO   B CA    1 
ATOM   106  C C     . PRO   A 1 36  ? 2.507   -10.09  68.629 1   6.24  ? 17  PRO   B C     1 
ATOM   107  O O     . PRO   A 1 36  ? 3.471   -10.866 68.589 1   5.46  ? 17  PRO   B O     1 
ATOM   108  C CB    . PRO   A 1 36  ? 0.092   -10.875 68.851 1   4.35  ? 17  PRO   B CB    1 
ATOM   109  C CG    . PRO   A 1 36  ? -0.891  -9.775  68.941 1   5.61  ? 17  PRO   B CG    1 
ATOM   110  C CD    . PRO   A 1 36  ? -0.568  -9.002  70.196 1   4.59  ? 17  PRO   B CD    1 
ATOM   111  N N     . ARG   A 1 37  ? 2.449   -8.94   67.906 1   7.65  ? 18  ARG   B N     1 
ATOM   112  C CA    . ARG   A 1 37  ? 3.5     -8.537  66.967 1   8.53  ? 18  ARG   B CA    1 
ATOM   113  C C     . ARG   A 1 37  ? 4.843   -8.35   67.675 1   7.46  ? 18  ARG   B C     1 
ATOM   114  O O     . ARG   A 1 37  ? 5.866   -8.833  67.176 1   7.09  ? 18  ARG   B O     1 
ATOM   115  C CB    . ARG   A 1 37  ? 3.094   -7.255  66.205 1   6.8   ? 18  ARG   B CB    1 
ATOM   116  C CG    . ARG   A 1 37  ? 1.902   -7.445  65.266 1   15.72 ? 18  ARG   B CG    1 
ATOM   117  C CD    . ARG   A 1 37  ? 1.418   -6.114  64.704 1   36.78 ? 18  ARG   B CD    1 
ATOM   118  N NE    . ARG   A 1 37  ? 0.623   -6.287  63.485 1   58.14 ? 18  ARG   B NE    1 
ATOM   119  C CZ    . ARG   A 1 37  ? 0.038   -5.295  62.817 1   75.78 ? 18  ARG   B CZ    1 
ATOM   120  N NH1   . ARG   A 1 37  ? -0.66   -5.549  61.717 1   61.18 ? 18  ARG   B NH1   1 
ATOM   121  N NH2   . ARG   A 1 37  ? 0.145   -4.042  63.245 1   64.79 ? 18  ARG   B NH2   1 
ATOM   122  N N     . ASP   A 1 38  ? 4.832   -7.689  68.854 1   6.47  ? 19  ASP   B N     1 
ATOM   123  C CA    . ASP   A 1 38  ? 6.033   -7.454  69.66  1   7.87  ? 19  ASP   B CA    1 
ATOM   124  C C     . ASP   A 1 38  ? 6.592   -8.783  70.192 1   6.71  ? 19  ASP   B C     1 
ATOM   125  O O     . ASP   A 1 38  ? 7.806   -8.995  70.184 1   7.18  ? 19  ASP   B O     1 
ATOM   126  C CB    . ASP   A 1 38  ? 5.733   -6.484  70.815 1   6.68  ? 19  ASP   B CB    1 
ATOM   127  C CG    . ASP   A 1 38  ? 6.947   -5.728  71.312 1   20.89 ? 19  ASP   B CG    1 
ATOM   128  O OD1   . ASP   A 1 38  ? 7.859   -5.461  70.494 1   29.19 ? 19  ASP   B OD1   1 
ATOM   129  O OD2   . ASP   A 1 38  ? 6.988   -5.394  72.521 1   30.68 ? 19  ASP   B OD2   1 
ATOM   130  N N     . TYR   A 1 39  ? 5.696   -9.695  70.608 1   3.98  ? 20  TYR   B N     1 
ATOM   131  C CA    . TYR   A 1 39  ? 6.097   -11.029 71.088 1   3.04  ? 20  TYR   B CA    1 
ATOM   132  C C     . TYR   A 1 39  ? 6.852   -11.8   69.982 1   7.63  ? 20  TYR   B C     1 
ATOM   133  O O     . TYR   A 1 39  ? 7.94    -12.322 70.227 1   7.63  ? 20  TYR   B O     1 
ATOM   134  C CB    . TYR   A 1 39  ? 4.853   -11.803 71.545 1   3     ? 20  TYR   B CB    1 
ATOM   135  C CG    . TYR   A 1 39  ? 5.15    -13.197 72.053 1   3     ? 20  TYR   B CG    1 
ATOM   136  C CD1   . TYR   A 1 39  ? 5.771   -13.395 73.288 1   3.54  ? 20  TYR   B CD1   1 
ATOM   137  C CD2   . TYR   A 1 39  ? 4.745   -14.323 71.337 1   3     ? 20  TYR   B CD2   1 
ATOM   138  C CE1   . TYR   A 1 39  ? 6.02    -14.678 73.775 1   3     ? 20  TYR   B CE1   1 
ATOM   139  C CE2   . TYR   A 1 39  ? 4.982   -15.612 71.821 1   3     ? 20  TYR   B CE2   1 
ATOM   140  C CZ    . TYR   A 1 39  ? 5.612   -15.783 73.045 1   4.39  ? 20  TYR   B CZ    1 
ATOM   141  O OH    . TYR   A 1 39  ? 5.833   -17.052 73.54  1   3     ? 20  TYR   B OH    1 
ATOM   142  N N     . LEU   A 1 40  ? 6.298   -11.808 68.754 1   7.99  ? 21  LEU   B N     1 
ATOM   143  C CA    . LEU   A 1 40  ? 6.899   -12.481 67.596 1   9.45  ? 21  LEU   B CA    1 
ATOM   144  C C     . LEU   A 1 40  ? 8.254   -11.866 67.228 1   6.97  ? 21  LEU   B C     1 
ATOM   145  O O     . LEU   A 1 40  ? 9.205   -12.6   66.928 1   8.71  ? 21  LEU   B O     1 
ATOM   146  C CB    . LEU   A 1 40  ? 5.944   -12.437 66.394 1   9.97  ? 21  LEU   B CB    1 
ATOM   147  C CG    . LEU   A 1 40  ? 4.622   -13.188 66.563 1   7.29  ? 21  LEU   B CG    1 
ATOM   148  C CD1   . LEU   A 1 40  ? 3.708   -12.937 65.394 1   7.68  ? 21  LEU   B CD1   1 
ATOM   149  C CD2   . LEU   A 1 40  ? 4.852   -14.695 66.784 1   5.99  ? 21  LEU   B CD2   1 
ATOM   150  N N     . GLU   A 1 41  ? 8.352   -10.519 67.315 1   8.79  ? 22  GLU   B N     1 
ATOM   151  C CA    . GLU   A 1 41  ? 9.587   -9.792  66.999 1   8.26  ? 22  GLU   B CA    1 
ATOM   152  C C     . GLU   A 1 41  ? 10.7    -10.125 67.992 1   8.11  ? 22  GLU   B C     1 
ATOM   153  O O     . GLU   A 1 41  ? 11.852  -10.339 67.593 1   10.92 ? 22  GLU   B O     1 
ATOM   154  C CB    . GLU   A 1 41  ? 9.336   -8.272  66.982 1   9.36  ? 22  GLU   B CB    1 
ATOM   155  C CG    . GLU   A 1 41  ? 8.644   -7.759  65.723 1   21    ? 22  GLU   B CG    1 
ATOM   156  C CD    . GLU   A 1 41  ? 9.357   -8.016  64.406 1   48.22 ? 22  GLU   B CD    1 
ATOM   157  O OE1   . GLU   A 1 41  ? 8.675   -8.427  63.439 1   48.2  ? 22  GLU   B OE1   1 
ATOM   158  O OE2   . GLU   A 1 41  ? 10.593  -7.814  64.342 1   44.98 ? 22  GLU   B OE2   1 
ATOM   159  N N     . LYS   A 1 42  ? 10.34   -10.191 69.283 1   9.6   ? 23  LYS   B N     1 
ATOM   160  C CA    . LYS   A 1 42  ? 11.269  -10.441 70.38  1   10.01 ? 23  LYS   B CA    1 
ATOM   161  C C     . LYS   A 1 42  ? 11.761  -11.876 70.484 1   7.5   ? 23  LYS   B C     1 
ATOM   162  O O     . LYS   A 1 42  ? 12.907  -12.08  70.858 1   8.14  ? 23  LYS   B O     1 
ATOM   163  C CB    . LYS   A 1 42  ? 10.655  -9.984  71.723 1   8.49  ? 23  LYS   B CB    1 
ATOM   164  C CG    . LYS   A 1 42  ? 11.204  -8.651  72.227 1   19.69 ? 23  LYS   B CG    1 
ATOM   165  C CD    . LYS   A 1 42  ? 10.406  -7.457  71.759 1   32.42 ? 23  LYS   B CD    1 
ATOM   166  C CE    . LYS   A 1 42  ? 11.059  -6.173  72.202 1   36.13 ? 23  LYS   B CE    1 
ATOM   167  N NZ    . LYS   A 1 42  ? 10.371  -4.99   71.629 1   41.32 ? 23  LYS   B NZ    1 
ATOM   168  N N     . TYR   A 1 43  ? 10.915  -12.864 70.178 1   4.66  ? 24  TYR   B N     1 
ATOM   169  C CA    . TYR   A 1 43  ? 11.278  -14.266 70.375 1   3     ? 24  TYR   B CA    1 
ATOM   170  C C     . TYR   A 1 43  ? 11.36   -15.145 69.12  1   5.79  ? 24  TYR   B C     1 
ATOM   171  O O     . TYR   A 1 43  ? 12.027  -16.199 69.157 1   3.46  ? 24  TYR   B O     1 
ATOM   172  C CB    . TYR   A 1 43  ? 10.278  -14.903 71.373 1   3     ? 24  TYR   B CB    1 
ATOM   173  C CG    . TYR   A 1 43  ? 10.387  -14.371 72.789 1   3     ? 24  TYR   B CG    1 
ATOM   174  C CD1   . TYR   A 1 43  ? 11.325  -14.887 73.679 1   3.51  ? 24  TYR   B CD1   1 
ATOM   175  C CD2   . TYR   A 1 43  ? 9.519   -13.38  73.257 1   3     ? 24  TYR   B CD2   1 
ATOM   176  C CE1   . TYR   A 1 43  ? 11.402  -14.433 74.997 1   3     ? 24  TYR   B CE1   1 
ATOM   177  C CE2   . TYR   A 1 43  ? 9.592   -12.91  74.573 1   3     ? 24  TYR   B CE2   1 
ATOM   178  C CZ    . TYR   A 1 43  ? 10.531  -13.446 75.443 1   7.22  ? 24  TYR   B CZ    1 
ATOM   179  O OH    . TYR   A 1 43  ? 10.597  -12.988 76.74  1   3     ? 24  TYR   B OH    1 
ATOM   180  N N     . TYR   A 1 44  ? 10.643  -14.777 68.041 1   3     ? 25  TYR   B N     1 
ATOM   181  C CA    . TYR   A 1 44  ? 10.582  -15.655 66.872 1   3     ? 25  TYR   B CA    1 
ATOM   182  C C     . TYR   A 1 44  ? 11.053  -15.016 65.544 1   13.27 ? 25  TYR   B C     1 
ATOM   183  O O     . TYR   A 1 44  ? 10.813  -15.598 64.48  1   11.02 ? 25  TYR   B O     1 
ATOM   184  C CB    . TYR   A 1 44  ? 9.153   -16.226 66.759 1   3.45  ? 25  TYR   B CB    1 
ATOM   185  C CG    . TYR   A 1 44  ? 8.792   -17.054 67.979 1   3     ? 25  TYR   B CG    1 
ATOM   186  C CD1   . TYR   A 1 44  ? 9.291   -18.348 68.141 1   3.93  ? 25  TYR   B CD1   1 
ATOM   187  C CD2   . TYR   A 1 44  ? 8.015   -16.518 69.007 1   3     ? 25  TYR   B CD2   1 
ATOM   188  C CE1   . TYR   A 1 44  ? 9.029   -19.089 69.295 1   3.81  ? 25  TYR   B CE1   1 
ATOM   189  C CE2   . TYR   A 1 44  ? 7.721   -17.263 70.157 1   3     ? 25  TYR   B CE2   1 
ATOM   190  C CZ    . TYR   A 1 44  ? 8.24    -18.544 70.297 1   5.61  ? 25  TYR   B CZ    1 
ATOM   191  O OH    . TYR   A 1 44  ? 7.969   -19.301 71.408 1   3     ? 25  TYR   B OH    1 
ATOM   192  N N     . GLU   A 1 53  ? 17.455  -16.947 72.043 1   3.39  ? 34  GLU   B N     1 
ATOM   193  C CA    . GLU   A 1 53  ? 16.08   -17.138 71.602 1   3     ? 34  GLU   B CA    1 
ATOM   194  C C     . GLU   A 1 53  ? 16.035  -18.066 70.378 1   6.73  ? 34  GLU   B C     1 
ATOM   195  O O     . GLU   A 1 53  ? 15.135  -18.899 70.293 1   5.85  ? 34  GLU   B O     1 
ATOM   196  C CB    . GLU   A 1 53  ? 15.395  -15.784 71.297 1   4.12  ? 34  GLU   B CB    1 
ATOM   197  C CG    . GLU   A 1 53  ? 15.012  -14.974 72.527 1   8.13  ? 34  GLU   B CG    1 
ATOM   198  C CD    . GLU   A 1 53  ? 16.126  -14.679 73.503 1   10.75 ? 34  GLU   B CD    1 
ATOM   199  O OE1   . GLU   A 1 53  ? 17.168  -14.128 73.073 1   14.43 ? 34  GLU   B OE1   1 
ATOM   200  O OE2   . GLU   A 1 53  ? 15.966  -15.034 74.691 1   9.82  ? 34  GLU   B OE2   1 
ATOM   201  N N     . SER   A 1 54  ? 17.014  -17.94  69.442 1   4.64  ? 35  SER   B N     1 
ATOM   202  C CA    . SER   A 1 54  ? 17.049  -18.798 68.249 1   5.86  ? 35  SER   B CA    1 
ATOM   203  C C     . SER   A 1 54  ? 17.52   -20.215 68.569 1   6.58  ? 35  SER   B C     1 
ATOM   204  O O     . SER   A 1 54  ? 17.044  -21.165 67.943 1   6.44  ? 35  SER   B O     1 
ATOM   205  C CB    . SER   A 1 54  ? 17.887  -18.169 67.135 1   9.17  ? 35  SER   B CB    1 
ATOM   206  O OG    . SER   A 1 54  ? 17.189  -17.025 66.659 1   16.49 ? 35  SER   B OG    1 
ATOM   207  N N     . GLN   A 1 55  ? 18.439  -20.362 69.547 1   4.23  ? 36  GLN   B N     1 
ATOM   208  C CA    . GLN   A 1 55  ? 18.941  -21.682 69.975 1   3.85  ? 36  GLN   B CA    1 
ATOM   209  C C     . GLN   A 1 55  ? 17.788  -22.5   70.584 1   5.41  ? 36  GLN   B C     1 
ATOM   210  O O     . GLN   A 1 55  ? 17.651  -23.704 70.305 1   3.22  ? 36  GLN   B O     1 
ATOM   211  C CB    . GLN   A 1 55  ? 20.085  -21.522 70.994 1   5.8   ? 36  GLN   B CB    1 
ATOM   212  C CG    . GLN   A 1 55  ? 21.397  -20.983 70.387 1   17.5  ? 36  GLN   B CG    1 
ATOM   213  C CD    . GLN   A 1 55  ? 22.023  -21.986 69.448 1   42.51 ? 36  GLN   B CD    1 
ATOM   214  O OE1   . GLN   A 1 55  ? 21.907  -21.88  68.218 1   42.26 ? 36  GLN   B OE1   1 
ATOM   215  N NE2   . GLN   A 1 55  ? 22.677  -22.995 70.015 1   36.53 ? 36  GLN   B NE2   1 
ATOM   216  N N     . ILE   A 1 56  ? 16.926  -21.822 71.362 1   3.06  ? 37  ILE   B N     1 
ATOM   217  C CA    . ILE   A 1 56  ? 15.756  -22.454 71.987 1   3     ? 37  ILE   B CA    1 
ATOM   218  C C     . ILE   A 1 56  ? 14.763  -22.898 70.919 1   5.55  ? 37  ILE   B C     1 
ATOM   219  O O     . ILE   A 1 56  ? 14.331  -24.051 70.922 1   3.47  ? 37  ILE   B O     1 
ATOM   220  C CB    . ILE   A 1 56  ? 15.134  -21.527 73.092 1   4.18  ? 37  ILE   B CB    1 
ATOM   221  C CG1   . ILE   A 1 56  ? 16.102  -21.422 74.298 1   3     ? 37  ILE   B CG1   1 
ATOM   222  C CG2   . ILE   A 1 56  ? 13.732  -22.021 73.529 1   3.41  ? 37  ILE   B CG2   1 
ATOM   223  C CD1   . ILE   A 1 56  ? 15.915  -20.269 75.215 1   6.72  ? 37  ILE   B CD1   1 
ATOM   224  N N     . LEU   A 1 57  ? 14.433  -21.985 69.981 1   3     ? 38  LEU   B N     1 
ATOM   225  C CA    . LEU   A 1 57  ? 13.503  -22.246 68.885 1   3     ? 38  LEU   B CA    1 
ATOM   226  C C     . LEU   A 1 57  ? 13.958  -23.458 68.061 1   4.69  ? 38  LEU   B C     1 
ATOM   227  O O     . LEU   A 1 57  ? 13.135  -24.32  67.759 1   3     ? 38  LEU   B O     1 
ATOM   228  C CB    . LEU   A 1 57  ? 13.343  -20.979 68.004 1   3.37  ? 38  LEU   B CB    1 
ATOM   229  C CG    . LEU   A 1 57  ? 12.364  -21.054 66.83  1   7.02  ? 38  LEU   B CG    1 
ATOM   230  C CD1   . LEU   A 1 57  ? 10.995  -21.574 67.269 1   6.66  ? 38  LEU   B CD1   1 
ATOM   231  C CD2   . LEU   A 1 57  ? 12.217  -19.678 66.165 1   6.2   ? 38  LEU   B CD2   1 
ATOM   232  N N     . LYS   A 1 58  ? 15.274  -23.555 67.756 1   3     ? 39  LYS   B N     1 
ATOM   233  C CA    . LYS   A 1 58  ? 15.836  -24.699 67.016 1   3     ? 39  LYS   B CA    1 
ATOM   234  C C     . LYS   A 1 58  ? 15.589  -25.998 67.792 1   7.72  ? 39  LYS   B C     1 
ATOM   235  O O     . LYS   A 1 58  ? 15.073  -26.98  67.227 1   6.49  ? 39  LYS   B O     1 
ATOM   236  C CB    . LYS   A 1 58  ? 17.344  -24.492 66.774 1   5.41  ? 39  LYS   B CB    1 
ATOM   237  C CG    . LYS   A 1 58  ? 17.644  -23.455 65.696 1   15.55 ? 39  LYS   B CG    1 
ATOM   238  C CD    . LYS   A 1 58  ? 19.142  -23.14  65.605 1   23.27 ? 39  LYS   B CD    1 
ATOM   239  C CE    . LYS   A 1 58  ? 19.388  -21.935 64.734 1   44.46 ? 39  LYS   B CE    1 
ATOM   240  N NZ    . LYS   A 1 58  ? 20.813  -21.518 64.762 1   55.44 ? 39  LYS   B NZ    1 
ATOM   241  N N     . HIS   A 1 59  ? 15.891  -25.979 69.11  1   6.33  ? 40  HIS   B N     1 
ATOM   242  C CA    . HIS   A 1 59  ? 15.662  -27.15  69.945 1   6.77  ? 40  HIS   B CA    1 
ATOM   243  C C     . HIS   A 1 59  ? 14.191  -27.562 69.977 1   7.47  ? 40  HIS   B C     1 
ATOM   244  O O     . HIS   A 1 59  ? 13.899  -28.744 69.79  1   6.2   ? 40  HIS   B O     1 
ATOM   245  C CB    . HIS   A 1 59  ? 16.213  -26.978 71.352 1   9.39  ? 40  HIS   B CB    1 
ATOM   246  C CG    . HIS   A 1 59  ? 16.434  -28.306 72     1   8.33  ? 40  HIS   B CG    1 
ATOM   247  N ND1   . HIS   A 1 59  ? 17.629  -28.984 71.851 1   7.19  ? 40  HIS   B ND1   1 
ATOM   248  C CD2   . HIS   A 1 59  ? 15.577  -29.074 72.716 1   7.16  ? 40  HIS   B CD2   1 
ATOM   249  C CE1   . HIS   A 1 59  ? 17.477  -30.126 72.51  1   7.72  ? 40  HIS   B CE1   1 
ATOM   250  N NE2   . HIS   A 1 59  ? 16.262  -30.223 73.052 1   7.49  ? 40  HIS   B NE2   1 
ATOM   251  N N     . LEU   A 1 60  ? 13.264  -26.587 70.163 1   3     ? 41  LEU   B N     1 
ATOM   252  C CA    . LEU   A 1 60  ? 11.829  -26.897 70.179 1   3     ? 41  LEU   B CA    1 
ATOM   253  C C     . LEU   A 1 60  ? 11.411  -27.585 68.867 1   4.64  ? 41  LEU   B C     1 
ATOM   254  O O     . LEU   A 1 60  ? 10.772  -28.635 68.899 1   3     ? 41  LEU   B O     1 
ATOM   255  C CB    . LEU   A 1 60  ? 10.977  -25.634 70.466 1   3     ? 41  LEU   B CB    1 
ATOM   256  C CG    . LEU   A 1 60  ? 11.166  -24.984 71.868 1   7.36  ? 41  LEU   B CG    1 
ATOM   257  C CD1   . LEU   A 1 60  ? 10.458  -23.643 71.952 1   6.7   ? 41  LEU   B CD1   1 
ATOM   258  C CD2   . LEU   A 1 60  ? 10.681  -25.903 72.996 1   6.42  ? 41  LEU   B CD2   1 
ATOM   259  N N     . LEU   A 1 61  ? 11.867  -27.049 67.733 1   3     ? 42  LEU   B N     1 
ATOM   260  C CA    . LEU   A 1 61  ? 11.57   -27.593 66.399 1   3.25  ? 42  LEU   B CA    1 
ATOM   261  C C     . LEU   A 1 61  ? 12.076  -29.039 66.209 1   4.28  ? 42  LEU   B C     1 
ATOM   262  O O     . LEU   A 1 61  ? 11.328  -29.892 65.697 1   3     ? 42  LEU   B O     1 
ATOM   263  C CB    . LEU   A 1 61  ? 12.09   -26.634 65.298 1   3.46  ? 42  LEU   B CB    1 
ATOM   264  C CG    . LEU   A 1 61  ? 11.354  -25.265 65.217 1   7.63  ? 42  LEU   B CG    1 
ATOM   265  C CD1   . LEU   A 1 61  ? 12.111  -24.271 64.342 1   7.73  ? 42  LEU   B CD1   1 
ATOM   266  C CD2   . LEU   A 1 61  ? 9.886   -25.41  64.801 1   6.34  ? 42  LEU   B CD2   1 
ATOM   267  N N     . LYS   A 1 62  ? 13.315  -29.332 66.682 1   3     ? 43  LYS   B N     1 
ATOM   268  C CA    . LYS   A 1 62  ? 13.886  -30.69  66.609 1   3     ? 43  LYS   B CA    1 
ATOM   269  C C     . LYS   A 1 62  ? 13.028  -31.665 67.429 1   6.6   ? 43  LYS   B C     1 
ATOM   270  O O     . LYS   A 1 62  ? 12.673  -32.752 66.94  1   4.46  ? 43  LYS   B O     1 
ATOM   271  C CB    . LYS   A 1 62  ? 15.343  -30.72  67.12  1   5.66  ? 43  LYS   B CB    1 
ATOM   272  C CG    . LYS   A 1 62  ? 16.338  -29.919 66.291 1   10.44 ? 43  LYS   B CG    1 
ATOM   273  C CD    . LYS   A 1 62  ? 17.679  -29.915 67.006 1   17.26 ? 43  LYS   B CD    1 
ATOM   274  C CE    . LYS   A 1 62  ? 18.607  -28.816 66.565 1   25.76 ? 43  LYS   B CE    1 
ATOM   275  N NZ    . LYS   A 1 62  ? 19.804  -28.738 67.441 1   35.34 ? 43  LYS   B NZ    1 
ATOM   276  N N     . ASN   A 1 63  ? 12.636  -31.247 68.657 1   3.13  ? 44  ASN   B N     1 
ATOM   277  C CA    . ASN   A 1 63  ? 11.797  -32.085 69.531 1   3     ? 44  ASN   B CA    1 
ATOM   278  C C     . ASN   A 1 63  ? 10.421  -32.347 68.944 1   5.5   ? 44  ASN   B C     1 
ATOM   279  O O     . ASN   A 1 63  ? 9.957   -33.49  68.973 1   4.21  ? 44  ASN   B O     1 
ATOM   280  C CB    . ASN   A 1 63  ? 11.692  -31.485 70.938 1   6.84  ? 44  ASN   B CB    1 
ATOM   281  C CG    . ASN   A 1 63  ? 12.83   -31.851 71.864 1   13.41 ? 44  ASN   B CG    1 
ATOM   282  O OD1   . ASN   A 1 63  ? 13.58   -32.802 71.625 1   16.82 ? 44  ASN   B OD1   1 
ATOM   283  N ND2   . ASN   A 1 63  ? 12.967  -31.106 72.955 1   12.73 ? 44  ASN   B ND2   1 
ATOM   284  N N     . LEU   A 1 64  ? 9.78    -31.317 68.374 1   3     ? 45  LEU   B N     1 
ATOM   285  C CA    . LEU   A 1 64  ? 8.458   -31.477 67.767 1   3     ? 45  LEU   B CA    1 
ATOM   286  C C     . LEU   A 1 64  ? 8.533   -32.384 66.519 1   7.35  ? 45  LEU   B C     1 
ATOM   287  O O     . LEU   A 1 64  ? 7.626   -33.191 66.295 1   6.26  ? 45  LEU   B O     1 
ATOM   288  C CB    . LEU   A 1 64  ? 7.826   -30.123 67.423 1   3.12  ? 45  LEU   B CB    1 
ATOM   289  C CG    . LEU   A 1 64  ? 7.489   -29.212 68.615 1   7.16  ? 45  LEU   B CG    1 
ATOM   290  C CD1   . LEU   A 1 64  ? 7.612   -27.747 68.235 1   6.93  ? 45  LEU   B CD1   1 
ATOM   291  C CD2   . LEU   A 1 64  ? 6.111   -29.546 69.212 1   5.13  ? 45  LEU   B CD2   1 
ATOM   292  N N     . PHE   A 1 65  ? 9.631   -32.278 65.74  1   7.3   ? 46  PHE   B N     1 
ATOM   293  C CA    . PHE   A 1 65  ? 9.861   -33.153 64.577 1   8.16  ? 46  PHE   B CA    1 
ATOM   294  C C     . PHE   A 1 65  ? 9.989   -34.603 65.062 1   7.06  ? 46  PHE   B C     1 
ATOM   295  O O     . PHE   A 1 65  ? 9.313   -35.491 64.518 1   7.49  ? 46  PHE   B O     1 
ATOM   296  C CB    . PHE   A 1 65  ? 11.117  -32.732 63.788 1   7.63  ? 46  PHE   B CB    1 
ATOM   297  C CG    . PHE   A 1 65  ? 11.596  -33.752 62.774 1   9.37  ? 46  PHE   B CG    1 
ATOM   298  C CD1   . PHE   A 1 65  ? 10.8    -34.111 61.688 1   13.41 ? 46  PHE   B CD1   1 
ATOM   299  C CD2   . PHE   A 1 65  ? 12.843  -34.35  62.901 1   10.55 ? 46  PHE   B CD2   1 
ATOM   300  C CE1   . PHE   A 1 65  ? 11.252  -35.049 60.74  1   16.65 ? 46  PHE   B CE1   1 
ATOM   301  C CE2   . PHE   A 1 65  ? 13.29   -35.291 61.958 1   14.85 ? 46  PHE   B CE2   1 
ATOM   302  C CZ    . PHE   A 1 65  ? 12.494  -35.63  60.882 1   15.61 ? 46  PHE   B CZ    1 
ATOM   303  N N     . LYS   A 1 66  ? 10.805  -34.827 66.122 1   3.45  ? 47  LYS   B N     1 
ATOM   304  C CA    . LYS   A 1 66  ? 10.999  -36.16  66.7   1   4.31  ? 47  LYS   B CA    1 
ATOM   305  C C     . LYS   A 1 66  ? 9.653   -36.778 67.142 1   7.31  ? 47  LYS   B C     1 
ATOM   306  O O     . LYS   A 1 66  ? 9.35    -37.922 66.789 1   6.98  ? 47  LYS   B O     1 
ATOM   307  C CB    . LYS   A 1 66  ? 11.995  -36.094 67.874 1   8.37  ? 47  LYS   B CB    1 
ATOM   308  C CG    . LYS   A 1 66  ? 12.304  -37.459 68.5   1   14.27 ? 47  LYS   B CG    1 
ATOM   309  C CD    . LYS   A 1 66  ? 13.371  -37.351 69.579 1   27.43 ? 47  LYS   B CD    1 
ATOM   310  C CE    . LYS   A 1 66  ? 13.092  -38.288 70.738 1   42.84 ? 47  LYS   B CE    1 
ATOM   311  N NZ    . LYS   A 1 66  ? 13.49   -37.688 72.053 1   47.2  ? 47  LYS   B NZ    1 
ATOM   312  N N     . ILE   A 1 67  ? 8.843   -36.006 67.903 1   3.85  ? 48  ILE   B N     1 
ATOM   313  C CA    . ILE   A 1 67  ? 7.553   -36.457 68.441 1   3     ? 48  ILE   B CA    1 
ATOM   314  C C     . ILE   A 1 67  ? 6.521   -36.819 67.366 1   7.5   ? 48  ILE   B C     1 
ATOM   315  O O     . ILE   A 1 67  ? 5.866   -37.868 67.475 1   7.32  ? 48  ILE   B O     1 
ATOM   316  C CB    . ILE   A 1 67  ? 6.988   -35.389 69.429 1   4.81  ? 48  ILE   B CB    1 
ATOM   317  C CG1   . ILE   A 1 67  ? 7.873   -35.275 70.682 1   5.05  ? 48  ILE   B CG1   1 
ATOM   318  C CG2   . ILE   A 1 67  ? 5.516   -35.675 69.797 1   3     ? 48  ILE   B CG2   1 
ATOM   319  C CD1   . ILE   A 1 67  ? 7.663   -33.989 71.533 1   9.08  ? 48  ILE   B CD1   1 
ATOM   320  N N     . PHE   A 1 68  ? 6.317   -35.924 66.379 1   6.34  ? 49  PHE   B N     1 
ATOM   321  C CA    . PHE   A 1 68  ? 5.263   -36.107 65.382 1   8.28  ? 49  PHE   B CA    1 
ATOM   322  C C     . PHE   A 1 68  ? 5.68    -36.862 64.111 1   10.43 ? 49  PHE   B C     1 
ATOM   323  O O     . PHE   A 1 68  ? 4.862   -37.612 63.568 1   11.02 ? 49  PHE   B O     1 
ATOM   324  C CB    . PHE   A 1 68  ? 4.617   -34.757 65.013 1   9.24  ? 49  PHE   B CB    1 
ATOM   325  C CG    . PHE   A 1 68  ? 3.952   -34.058 66.185 1   8.15  ? 49  PHE   B CG    1 
ATOM   326  C CD1   . PHE   A 1 68  ? 2.887   -34.652 66.859 1   8.02  ? 49  PHE   B CD1   1 
ATOM   327  C CD2   . PHE   A 1 68  ? 4.38    -32.799 66.603 1   7.62  ? 49  PHE   B CD2   1 
ATOM   328  C CE1   . PHE   A 1 68  ? 2.296   -34.02  67.965 1   8.18  ? 49  PHE   B CE1   1 
ATOM   329  C CE2   . PHE   A 1 68  ? 3.783   -32.164 67.71  1   7.7   ? 49  PHE   B CE2   1 
ATOM   330  C CZ    . PHE   A 1 68  ? 2.744   -32.777 68.378 1   8.01  ? 49  PHE   B CZ    1 
ATOM   331  N N     . CYS   A 1 69  ? 6.918   -36.684 63.645 1   12.01 ? 50  CYS   B N     1 
ATOM   332  C CA    . CYS   A 1 69  ? 7.312   -37.34  62.395 1   13.94 ? 50  CYS   B CA    1 
ATOM   333  C C     . CYS   A 1 69  ? 8.143   -38.615 62.582 1   15.54 ? 50  CYS   B C     1 
ATOM   334  O O     . CYS   A 1 69  ? 8.126   -39.47  61.688 1   18.19 ? 50  CYS   B O     1 
ATOM   335  C CB    . CYS   A 1 69  ? 7.995   -36.346 61.462 1   14.87 ? 50  CYS   B CB    1 
ATOM   336  S SG    . CYS   A 1 69  ? 6.93    -34.964 60.965 1   19.01 ? 50  CYS   B SG    1 
ATOM   337  N N     . LEU   A 1 70  ? 8.831   -38.773 63.726 1   13.31 ? 51  LEU   B N     1 
ATOM   338  C CA    . LEU   A 1 70  ? 9.64    -39.977 63.964 1   21.3  ? 51  LEU   B CA    1 
ATOM   339  C C     . LEU   A 1 70  ? 8.961   -40.923 64.94  1   43.08 ? 51  LEU   B C     1 
ATOM   340  O O     . LEU   A 1 70  ? 8.767   -42.093 64.623 1   16.63 ? 51  LEU   B O     1 
ATOM   341  C CB    . LEU   A 1 70  ? 11.068  -39.637 64.442 1   19.25 ? 51  LEU   B CB    1 
ATOM   342  C CG    . LEU   A 1 70  ? 11.887  -38.624 63.625 1   25.1  ? 51  LEU   B CG    1 
ATOM   343  C CD1   . LEU   A 1 70  ? 13.187  -38.308 64.322 1   24.19 ? 51  LEU   B CD1   1 
ATOM   344  C CD2   . LEU   A 1 70  ? 12.178  -39.126 62.22  1   28.31 ? 51  LEU   B CD2   1 
ATOM   345  N N     . GLY   A 1 72  ? 5.657   -40.619 64.876 1   25.72 ? 53  GLY   B N     1 
ATOM   346  C CA    . GLY   A 1 72  ? 5.223   -41.357 66.056 1   23.47 ? 53  GLY   B CA    1 
ATOM   347  C C     . GLY   A 1 72  ? 3.824   -40.992 66.526 1   24.56 ? 53  GLY   B C     1 
ATOM   348  O O     . GLY   A 1 72  ? 2.906   -41.818 66.454 1   26.8  ? 53  GLY   B O     1 
ATOM   349  N N     . VAL   A 1 73  ? 3.656   -39.748 67.029 1   17.08 ? 54  VAL   B N     1 
ATOM   350  C CA    . VAL   A 1 73  ? 2.374   -39.241 67.533 1   15.52 ? 54  VAL   B CA    1 
ATOM   351  C C     . VAL   A 1 73  ? 1.557   -38.747 66.339 1   18.38 ? 54  VAL   B C     1 
ATOM   352  O O     . VAL   A 1 73  ? 2.026   -37.897 65.566 1   18.92 ? 54  VAL   B O     1 
ATOM   353  C CB    . VAL   A 1 73  ? 2.55    -38.166 68.652 1   13.74 ? 54  VAL   B CB    1 
ATOM   354  C CG1   . VAL   A 1 73  ? 1.2     -37.637 69.139 1   13.99 ? 54  VAL   B CG1   1 
ATOM   355  C CG2   . VAL   A 1 73  ? 3.359   -38.726 69.829 1   13.11 ? 54  VAL   B CG2   1 
ATOM   356  N N     . LYS   A 1 74  ? 0.338   -39.303 66.191 1   16.28 ? 55  LYS   B N     1 
ATOM   357  C CA    . LYS   A 1 74  ? -0.547  -39.025 65.064 1   17.37 ? 55  LYS   B CA    1 
ATOM   358  C C     . LYS   A 1 74  ? -2.02   -39.191 65.432 1   17.92 ? 55  LYS   B C     1 
ATOM   359  O O     . LYS   A 1 74  ? -2.367  -39.699 66.507 1   16.39 ? 55  LYS   B O     1 
ATOM   360  C CB    . LYS   A 1 74  ? -0.188  -39.956 63.879 1   20.82 ? 55  LYS   B CB    1 
ATOM   361  C CG    . LYS   A 1 74  ? -0.507  -41.434 64.116 1   33.86 ? 55  LYS   B CG    1 
ATOM   362  C CD    . LYS   A 1 74  ? 0.43    -42.347 63.34  1   47.44 ? 55  LYS   B CD    1 
ATOM   363  C CE    . LYS   A 1 74  ? 0.634   -43.669 64.043 1   59.62 ? 55  LYS   B CE    1 
ATOM   364  N NZ    . LYS   A 1 74  ? 1.978   -44.25  63.763 1   66.56 ? 55  LYS   B NZ    1 
ATOM   365  N N     . GLY   A 1 75  ? -2.874  -38.809 64.504 1   17.9  ? 56  GLY   B N     1 
ATOM   366  C CA    . GLY   A 1 75  ? -4.302  -38.955 64.703 1   18.36 ? 56  GLY   B CA    1 
ATOM   367  C C     . GLY   A 1 75  ? -5.12   -38.096 63.781 1   19.32 ? 56  GLY   B C     1 
ATOM   368  O O     . GLY   A 1 75  ? -4.596  -37.492 62.842 1   18.87 ? 56  GLY   B O     1 
ATOM   369  N N     . ASP   A 1 76  ? -6.42   -38.05  64.048 1   18    ? 57  ASP   B N     1 
ATOM   370  C CA    . ASP   A 1 76  ? -7.335  -37.236 63.271 1   18.33 ? 57  ASP   B CA    1 
ATOM   371  C C     . ASP   A 1 76  ? -7.375  -35.817 63.796 1   15.85 ? 57  ASP   B C     1 
ATOM   372  O O     . ASP   A 1 76  ? -7.59   -34.89  63.011 1   15.6  ? 57  ASP   B O     1 
ATOM   373  C CB    . ASP   A 1 76  ? -8.747  -37.838 63.305 1   21.37 ? 57  ASP   B CB    1 
ATOM   374  C CG    . ASP   A 1 76  ? -8.932  -39.035 62.39  1   33.21 ? 57  ASP   B CG    1 
ATOM   375  O OD1   . ASP   A 1 76  ? -7.968  -39.39  61.667 1   36.97 ? 57  ASP   B OD1   1 
ATOM   376  O OD2   . ASP   A 1 76  ? -10.041 -39.619 62.395 1   41.18 ? 57  ASP   B OD2   1 
ATOM   377  N N     . LEU   A 1 77  ? -7.17   -35.645 65.126 1   12.17 ? 58  LEU   B N     1 
ATOM   378  C CA    . LEU   A 1 77  ? -7.273  -34.336 65.767 1   8.54  ? 58  LEU   B CA    1 
ATOM   379  C C     . LEU   A 1 77  ? -6.209  -34.027 66.824 1   8.36  ? 58  LEU   B C     1 
ATOM   380  O O     . LEU   A 1 77  ? -6.049  -34.777 67.802 1   4.73  ? 58  LEU   B O     1 
ATOM   381  C CB    . LEU   A 1 77  ? -8.684  -34.195 66.382 1   9.13  ? 58  LEU   B CB    1 
ATOM   382  C CG    . LEU   A 1 77  ? -9.029  -32.897 67.12  1   11.59 ? 58  LEU   B CG    1 
ATOM   383  C CD1   . LEU   A 1 77  ? -9.06   -31.699 66.167 1   11.46 ? 58  LEU   B CD1   1 
ATOM   384  C CD2   . LEU   A 1 77  ? -10.366 -33.042 67.825 1   12.61 ? 58  LEU   B CD2   1 
ATOM   385  N N     . LEU   A 1 78  ? -5.561  -32.853 66.656 1   4.72  ? 59  LEU   B N     1 
ATOM   386  C CA    . LEU   A 1 78  ? -4.61   -32.286 67.613 1   4.45  ? 59  LEU   B CA    1 
ATOM   387  C C     . LEU   A 1 78  ? -5.174  -30.938 68.062 1   7.93  ? 59  LEU   B C     1 
ATOM   388  O O     . LEU   A 1 78  ? -5.577  -30.128 67.211 1   6.91  ? 59  LEU   B O     1 
ATOM   389  C CB    . LEU   A 1 78  ? -3.202  -32.082 67.006 1   5.03  ? 59  LEU   B CB    1 
ATOM   390  C CG    . LEU   A 1 78  ? -2.165  -31.386 67.942 1   6.99  ? 59  LEU   B CG    1 
ATOM   391  C CD1   . LEU   A 1 78  ? -0.849  -32.093 67.925 1   6.87  ? 59  LEU   B CD1   1 
ATOM   392  C CD2   . LEU   A 1 78  ? -1.931  -29.929 67.539 1   7.07  ? 59  LEU   B CD2   1 
ATOM   393  N N     . ILE   A 1 79  ? -5.195  -30.699 69.382 1   3.09  ? 60  ILE   B N     1 
ATOM   394  C CA    . ILE   A 1 79  ? -5.61   -29.402 69.914 1   3     ? 60  ILE   B CA    1 
ATOM   395  C C     . ILE   A 1 79  ? -4.343  -28.726 70.463 1   5.74  ? 60  ILE   B C     1 
ATOM   396  O O     . ILE   A 1 79  ? -3.669  -29.303 71.333 1   3     ? 60  ILE   B O     1 
ATOM   397  C CB    . ILE   A 1 79  ? -6.745  -29.502 70.973 1   4.78  ? 60  ILE   B CB    1 
ATOM   398  C CG1   . ILE   A 1 79  ? -8.035  -30.11  70.36  1   3.19  ? 60  ILE   B CG1   1 
ATOM   399  C CG2   . ILE   A 1 79  ? -7.041  -28.113 71.617 1   4.72  ? 60  ILE   B CG2   1 
ATOM   400  C CD1   . ILE   A 1 79  ? -9.096  -30.552 71.396 1   8.97  ? 60  ILE   B CD1   1 
ATOM   401  N N     . ASP   A 1 80  ? -3.996  -27.534 69.919 1   3     ? 61  ASP   B N     1 
ATOM   402  C CA    . ASP   A 1 80  ? -2.853  -26.759 70.431 1   3     ? 61  ASP   B CA    1 
ATOM   403  C C     . ASP   A 1 80  ? -3.4    -25.748 71.433 1   6.66  ? 61  ASP   B C     1 
ATOM   404  O O     . ASP   A 1 80  ? -4.194  -24.879 71.052 1   5.42  ? 61  ASP   B O     1 
ATOM   405  C CB    . ASP   A 1 80  ? -2.074  -26.032 69.327 1   4.71  ? 61  ASP   B CB    1 
ATOM   406  C CG    . ASP   A 1 80  ? -0.877  -25.254 69.881 1   12.14 ? 61  ASP   B CG    1 
ATOM   407  O OD1   . ASP   A 1 80  ? -0.202  -25.774 70.817 1   16.08 ? 61  ASP   B OD1   1 
ATOM   408  O OD2   . ASP   A 1 80  ? -0.618  -24.128 69.388 1   16.53 ? 61  ASP   B OD2   1 
ATOM   409  N N     . ILE   A 1 81  ? -2.991  -25.882 72.707 1   3     ? 62  ILE   B N     1 
ATOM   410  C CA    . ILE   A 1 81  ? -3.446  -25.073 73.852 1   3     ? 62  ILE   B CA    1 
ATOM   411  C C     . ILE   A 1 81  ? -2.502  -23.874 74.12  1   5.59  ? 62  ILE   B C     1 
ATOM   412  O O     . ILE   A 1 81  ? -1.303  -24.079 74.334 1   3     ? 62  ILE   B O     1 
ATOM   413  C CB    . ILE   A 1 81  ? -3.555  -26.025 75.097 1   5.21  ? 62  ILE   B CB    1 
ATOM   414  C CG1   . ILE   A 1 81  ? -4.709  -27.056 74.946 1   5.01  ? 62  ILE   B CG1   1 
ATOM   415  C CG2   . ILE   A 1 81  ? -3.653  -25.247 76.425 1   5.7   ? 62  ILE   B CG2   1 
ATOM   416  C CD1   . ILE   A 1 81  ? -6.167  -26.458 74.867 1   8.85  ? 62  ILE   B CD1   1 
ATOM   417  N N     . GLY   A 1 82  ? -3.049  -22.657 74.15  1   3     ? 63  GLY   B N     1 
ATOM   418  C CA    . GLY   A 1 82  ? -2.236  -21.463 74.409 1   3     ? 63  GLY   B CA    1 
ATOM   419  C C     . GLY   A 1 82  ? -1.265  -21.171 73.284 1   5.07  ? 63  GLY   B C     1 
ATOM   420  O O     . GLY   A 1 82  ? -0.094  -20.851 73.516 1   3     ? 63  GLY   B O     1 
ATOM   421  N N     . SER   A 1 83  ? -1.761  -21.319 72.046 1   3     ? 64  SER   B N     1 
ATOM   422  C CA    . SER   A 1 83  ? -1.054  -21.116 70.788 1   3     ? 64  SER   B CA    1 
ATOM   423  C C     . SER   A 1 83  ? -0.399  -19.744 70.707 1   4.85  ? 64  SER   B C     1 
ATOM   424  O O     . SER   A 1 83  ? 0.611   -19.599 70.021 1   3     ? 64  SER   B O     1 
ATOM   425  C CB    . SER   A 1 83  ? -2.039  -21.22  69.618 1   6.76  ? 64  SER   B CB    1 
ATOM   426  O OG    . SER   A 1 83  ? -2.752  -22.448 69.647 1   8.47  ? 64  SER   B OG    1 
ATOM   427  N N     . GLY   A 1 84  ? -1.031  -18.741 71.33  1   3     ? 65  GLY   B N     1 
ATOM   428  C CA    . GLY   A 1 84  ? -0.598  -17.352 71.229 1   3     ? 65  GLY   B CA    1 
ATOM   429  C C     . GLY   A 1 84  ? -0.651  -16.964 69.762 1   5.66  ? 65  GLY   B C     1 
ATOM   430  O O     . GLY   A 1 84  ? -1.514  -17.483 69.037 1   3     ? 65  GLY   B O     1 
ATOM   431  N N     . PRO   A 1 85  ? 0.293   -16.132 69.264 1   3     ? 66  PRO   B N     1 
ATOM   432  C CA    . PRO   A 1 85  ? 0.286   -15.793 67.829 1   3     ? 66  PRO   B CA    1 
ATOM   433  C C     . PRO   A 1 85  ? 1.258   -16.664 67.001 1   6.86  ? 66  PRO   B C     1 
ATOM   434  O O     . PRO   A 1 85  ? 1.621   -16.288 65.881 1   4.72  ? 66  PRO   B O     1 
ATOM   435  C CB    . PRO   A 1 85  ? 0.761   -14.336 67.841 1   3.93  ? 66  PRO   B CB    1 
ATOM   436  C CG    . PRO   A 1 85  ? 1.738   -14.281 69.003 1   6.06  ? 66  PRO   B CG    1 
ATOM   437  C CD    . PRO   A 1 85  ? 1.369   -15.402 69.974 1   3.92  ? 66  PRO   B CD    1 
ATOM   438  N N     . THR   A 1 86  ? 1.707   -17.815 67.549 1   4.03  ? 67  THR   B N     1 
ATOM   439  C CA    . THR   A 1 86  ? 2.729   -18.615 66.865 1   3     ? 67  THR   B CA    1 
ATOM   440  C C     . THR   A 1 86  ? 2.198   -19.828 66.103 1   6.76  ? 67  THR   B C     1 
ATOM   441  O O     . THR   A 1 86  ? 1.171   -20.406 66.476 1   6.79  ? 67  THR   B O     1 
ATOM   442  C CB    . THR   A 1 86  ? 3.838   -19.039 67.85  1   6.35  ? 67  THR   B CB    1 
ATOM   443  O OG1   . THR   A 1 86  ? 3.335   -20.049 68.721 1   8.7   ? 67  THR   B OG1   1 
ATOM   444  C CG2   . THR   A 1 86  ? 4.416   -17.874 68.644 1   3.44  ? 67  THR   B CG2   1 
ATOM   445  N N     . ILE   A 1 87  ? 2.948   -20.239 65.061 1   3.62  ? 68  ILE   B N     1 
ATOM   446  C CA    . ILE   A 1 87  ? 2.623   -21.408 64.221 1   3.91  ? 68  ILE   B CA    1 
ATOM   447  C C     . ILE   A 1 87  ? 3.76    -22.442 64.18  1   7.04  ? 68  ILE   B C     1 
ATOM   448  O O     . ILE   A 1 87  ? 3.558   -23.55  63.651 1   5.94  ? 68  ILE   B O     1 
ATOM   449  C CB    . ILE   A 1 87  ? 2.161   -21.003 62.784 1   7.42  ? 68  ILE   B CB    1 
ATOM   450  C CG1   . ILE   A 1 87  ? 3.273   -20.266 61.989 1   6.76  ? 68  ILE   B CG1   1 
ATOM   451  C CG2   . ILE   A 1 87  ? 0.881   -20.17  62.824 1   7.41  ? 68  ILE   B CG2   1 
ATOM   452  C CD1   . ILE   A 1 87  ? 4.114   -21.134 61.063 1   10.87 ? 68  ILE   B CD1   1 
ATOM   453  N N     . TYR   A 1 88  ? 4.945   -22.08  64.709 1   3     ? 69  TYR   B N     1 
ATOM   454  C CA    . TYR   A 1 88  ? 6.145   -22.932 64.693 1   3.16  ? 69  TYR   B CA    1 
ATOM   455  C C     . TYR   A 1 88  ? 5.901   -24.326 65.301 1   6.39  ? 69  TYR   B C     1 
ATOM   456  O O     . TYR   A 1 88  ? 6.454   -25.313 64.811 1   3     ? 69  TYR   B O     1 
ATOM   457  C CB    . TYR   A 1 88  ? 7.342   -22.224 65.372 1   3.47  ? 69  TYR   B CB    1 
ATOM   458  C CG    . TYR   A 1 88  ? 7.328   -22.328 66.886 1   4.47  ? 69  TYR   B CG    1 
ATOM   459  C CD1   . TYR   A 1 88  ? 7.906   -23.417 67.535 1   6.09  ? 69  TYR   B CD1   1 
ATOM   460  C CD2   . TYR   A 1 88  ? 6.667   -21.38  67.664 1   4.36  ? 69  TYR   B CD2   1 
ATOM   461  C CE1   . TYR   A 1 88  ? 7.851   -23.549 68.92  1   4.65  ? 69  TYR   B CE1   1 
ATOM   462  C CE2   . TYR   A 1 88  ? 6.614   -21.496 69.057 1   5.08  ? 69  TYR   B CE2   1 
ATOM   463  C CZ    . TYR   A 1 88  ? 7.217   -22.58  69.68  1   6.67  ? 69  TYR   B CZ    1 
ATOM   464  O OH    . TYR   A 1 88  ? 7.164   -22.734 71.043 1   3     ? 69  TYR   B OH    1 
ATOM   465  N N     . GLN   A 1 89  ? 5.066   -24.392 66.364 1   3     ? 70  GLN   B N     1 
ATOM   466  C CA    . GLN   A 1 89  ? 4.786   -25.625 67.105 1   3     ? 70  GLN   B CA    1 
ATOM   467  C C     . GLN   A 1 89  ? 3.869   -26.586 66.336 1   5.78  ? 70  GLN   B C     1 
ATOM   468  O O     . GLN   A 1 89  ? 3.617   -27.695 66.812 1   3.13  ? 70  GLN   B O     1 
ATOM   469  C CB    . GLN   A 1 89  ? 4.239   -25.308 68.525 1   3.6   ? 70  GLN   B CB    1 
ATOM   470  C CG    . GLN   A 1 89  ? 2.802   -24.748 68.579 1   3     ? 70  GLN   B CG    1 
ATOM   471  C CD    . GLN   A 1 89  ? 2.68    -23.235 68.4   1   6.26  ? 70  GLN   B CD    1 
ATOM   472  O OE1   . GLN   A 1 89  ? 3.461   -22.579 67.709 1   3.09  ? 70  GLN   B OE1   1 
ATOM   473  N NE2   . GLN   A 1 89  ? 1.669   -22.632 69.02  1   8.72  ? 70  GLN   B NE2   1 
ATOM   474  N N     . LEU   A 1 90  ? 3.358   -26.148 65.166 1   3     ? 71  LEU   B N     1 
ATOM   475  C CA    . LEU   A 1 90  ? 2.417   -26.919 64.337 1   3     ? 71  LEU   B CA    1 
ATOM   476  C C     . LEU   A 1 90  ? 3.009   -27.416 63.01  1   7.22  ? 71  LEU   B C     1 
ATOM   477  O O     . LEU   A 1 90  ? 2.373   -28.226 62.32  1   6.95  ? 71  LEU   B O     1 
ATOM   478  C CB    . LEU   A 1 90  ? 1.188   -26.035 64.054 1   3.23  ? 71  LEU   B CB    1 
ATOM   479  C CG    . LEU   A 1 90  ? 0.585   -25.276 65.26  1   6.87  ? 71  LEU   B CG    1 
ATOM   480  C CD1   . LEU   A 1 90  ? -0.4    -24.227 64.789 1   6.87  ? 71  LEU   B CD1   1 
ATOM   481  C CD2   . LEU   A 1 90  ? -0.082  -26.229 66.251 1   7.12  ? 71  LEU   B CD2   1 
ATOM   482  N N     . LEU   A 1 91  ? 4.214   -26.93  62.649 1   8.6   ? 72  LEU   B N     1 
ATOM   483  C CA    . LEU   A 1 91  ? 4.844   -27.254 61.367 1   9.04  ? 72  LEU   B CA    1 
ATOM   484  C C     . LEU   A 1 91  ? 5.083   -28.759 61.15  1   9.99  ? 72  LEU   B C     1 
ATOM   485  O O     . LEU   A 1 91  ? 4.776   -29.257 60.057 1   11.45 ? 72  LEU   B O     1 
ATOM   486  C CB    . LEU   A 1 91  ? 6.117   -26.429 61.137 1   9.64  ? 72  LEU   B CB    1 
ATOM   487  C CG    . LEU   A 1 91  ? 5.847   -24.926 60.83  1   9.47  ? 72  LEU   B CG    1 
ATOM   488  C CD1   . LEU   A 1 91  ? 7.11    -24.097 60.949 1   10.05 ? 72  LEU   B CD1   1 
ATOM   489  C CD2   . LEU   A 1 91  ? 5.205   -24.727 59.429 1   14.42 ? 72  LEU   B CD2   1 
ATOM   490  N N     . SER   A 1 92  ? 5.554   -29.494 62.171 1   8.99  ? 73  SER   B N     1 
ATOM   491  C CA    . SER   A 1 92  ? 5.722   -30.947 62.003 1   10.43 ? 73  SER   B CA    1 
ATOM   492  C C     . SER   A 1 92  ? 4.415   -31.705 62.274 1   10.31 ? 73  SER   B C     1 
ATOM   493  O O     . SER   A 1 92  ? 4.184   -32.758 61.661 1   12.28 ? 73  SER   B O     1 
ATOM   494  C CB    . SER   A 1 92  ? 6.847   -31.476 62.88  1   8.22  ? 73  SER   B CB    1 
ATOM   495  O OG    . SER   A 1 92  ? 8.099   -31.05  62.373 1   9.96  ? 73  SER   B OG    1 
ATOM   496  N N     . ALA   A 1 93  ? 3.552   -31.159 63.176 1   9.26  ? 74  ALA   B N     1 
ATOM   497  C CA    . ALA   A 1 93  ? 2.255   -31.745 63.537 1   9.82  ? 74  ALA   B CA    1 
ATOM   498  C C     . ALA   A 1 93  ? 1.294   -31.872 62.341 1   11.21 ? 74  ALA   B C     1 
ATOM   499  O O     . ALA   A 1 93  ? 0.506   -32.821 62.306 1   11.9  ? 74  ALA   B O     1 
ATOM   500  C CB    . ALA   A 1 93  ? 1.591   -30.931 64.642 1   8.89  ? 74  ALA   B CB    1 
ATOM   501  N N     . CYS   A 1 94  ? 1.33    -30.907 61.387 1   11.87 ? 75  CYS   B N     1 
ATOM   502  C CA    . CYS   A 1 94  ? 0.43    -30.944 60.225 1   13.17 ? 75  CYS   B CA    1 
ATOM   503  C C     . CYS   A 1 94  ? 0.721   -32.137 59.279 1   16.07 ? 75  CYS   B C     1 
ATOM   504  O O     . CYS   A 1 94  ? -0.119  -32.482 58.443 1   18.1  ? 75  CYS   B O     1 
ATOM   505  C CB    . CYS   A 1 94  ? 0.416   -29.608 59.482 1   13.44 ? 75  CYS   B CB    1 
ATOM   506  S SG    . CYS   A 1 94  ? 1.962   -29.214 58.628 1   15.8  ? 75  CYS   B SG    1 
ATOM   507  N N     . GLU   A 1 95  ? 1.882   -32.788 59.456 1   15.28 ? 76  GLU   B N     1 
ATOM   508  C CA    . GLU   A 1 95  ? 2.251   -33.962 58.667 1   17.32 ? 76  GLU   B CA    1 
ATOM   509  C C     . GLU   A 1 95  ? 1.614   -35.23  59.247 1   20.15 ? 76  GLU   B C     1 
ATOM   510  O O     . GLU   A 1 95  ? 1.521   -36.247 58.545 1   22.49 ? 76  GLU   B O     1 
ATOM   511  C CB    . GLU   A 1 95  ? 3.785   -34.119 58.611 1   17.98 ? 76  GLU   B CB    1 
ATOM   512  C CG    . GLU   A 1 95  ? 4.52    -32.986 57.913 1   21.77 ? 76  GLU   B CG    1 
ATOM   513  C CD    . GLU   A 1 95  ? 4.218   -32.786 56.44  1   52.87 ? 76  GLU   B CD    1 
ATOM   514  O OE1   . GLU   A 1 95  ? 3.962   -33.787 55.729 1   53.3  ? 76  GLU   B OE1   1 
ATOM   515  O OE2   . GLU   A 1 95  ? 4.248   -31.618 55.992 1   58.11 ? 76  GLU   B OE2   1 
ATOM   516  N N     . SER   A 1 96  ? 1.194   -35.175 60.532 1   17.24 ? 77  SER   B N     1 
ATOM   517  C CA    . SER   A 1 96  ? 0.657   -36.32  61.284 1   17.15 ? 77  SER   B CA    1 
ATOM   518  C C     . SER   A 1 96  ? -0.802  -36.221 61.724 1   18.63 ? 77  SER   B C     1 
ATOM   519  O O     . SER   A 1 96  ? -1.369  -37.222 62.187 1   19.02 ? 77  SER   B O     1 
ATOM   520  C CB    . SER   A 1 96  ? 1.529   -36.585 62.504 1   16.43 ? 77  SER   B CB    1 
ATOM   521  O OG    . SER   A 1 96  ? 2.874   -36.725 62.086 1   19.43 ? 77  SER   B OG    1 
ATOM   522  N N     . PHE   A 1 97  ? -1.407  -35.032 61.605 1   16.67 ? 78  PHE   B N     1 
ATOM   523  C CA    . PHE   A 1 97  ? -2.788  -34.826 62.029 1   16.46 ? 78  PHE   B CA    1 
ATOM   524  C C     . PHE   A 1 97  ? -3.613  -34.239 60.908 1   21.16 ? 78  PHE   B C     1 
ATOM   525  O O     . PHE   A 1 97  ? -3.232  -33.208 60.344 1   21.73 ? 78  PHE   B O     1 
ATOM   526  C CB    . PHE   A 1 97  ? -2.848  -33.936 63.294 1   14.98 ? 78  PHE   B CB    1 
ATOM   527  C CG    . PHE   A 1 97  ? -2.316  -34.633 64.524 1   14.38 ? 78  PHE   B CG    1 
ATOM   528  C CD1   . PHE   A 1 97  ? -0.963  -34.585 64.838 1   13.75 ? 78  PHE   B CD1   1 
ATOM   529  C CD2   . PHE   A 1 97  ? -3.159  -35.387 65.336 1   14.21 ? 78  PHE   B CD2   1 
ATOM   530  C CE1   . PHE   A 1 97  ? -0.462  -35.28  65.94  1   13.28 ? 78  PHE   B CE1   1 
ATOM   531  C CE2   . PHE   A 1 97  ? -2.66   -36.059 66.457 1   13.66 ? 78  PHE   B CE2   1 
ATOM   532  C CZ    . PHE   A 1 97  ? -1.314  -36.002 66.748 1   13.4  ? 78  PHE   B CZ    1 
ATOM   533  N N     . LYS   A 1 98  ? -4.756  -34.888 60.6   1   21.78 ? 79  LYS   B N     1 
ATOM   534  C CA    . LYS   A 1 98  ? -5.694  -34.464 59.557 1   23.42 ? 79  LYS   B CA    1 
ATOM   535  C C     . LYS   A 1 98  ? -6.245  -33.075 59.882 1   22.3  ? 79  LYS   B C     1 
ATOM   536  O O     . LYS   A 1 98  ? -6.308  -32.221 58.994 1   23.21 ? 79  LYS   B O     1 
ATOM   537  C CB    . LYS   A 1 98  ? -6.833  -35.496 59.416 1   26.93 ? 79  LYS   B CB    1 
ATOM   538  C CG    . LYS   A 1 98  ? -7.953  -35.112 58.433 1   42.65 ? 79  LYS   B CG    1 
ATOM   539  C CD    . LYS   A 1 98  ? -9.113  -36.121 58.45  1   57.22 ? 79  LYS   B CD    1 
ATOM   540  C CE    . LYS   A 1 98  ? -10.107 -35.874 59.567 1   67.19 ? 79  LYS   B CE    1 
ATOM   541  N NZ    . LYS   A 1 98  ? -10.97  -37.058 59.825 1   75.75 ? 79  LYS   B NZ    1 
ATOM   542  N N     . GLU   A 1 99  ? -6.604  -32.852 61.16  1   17.6  ? 80  GLU   B N     1 
ATOM   543  C CA    . GLU   A 1 99  ? -7.17   -31.601 61.65  1   15.72 ? 80  GLU   B CA    1 
ATOM   544  C C     . GLU   A 1 99  ? -6.402  -31.097 62.875 1   13.72 ? 80  GLU   B C     1 
ATOM   545  O O     . GLU   A 1 99  ? -6.069  -31.869 63.783 1   13.57 ? 80  GLU   B O     1 
ATOM   546  C CB    . GLU   A 1 99  ? -8.67   -31.807 61.969 1   17.16 ? 80  GLU   B CB    1 
ATOM   547  C CG    . GLU   A 1 99  ? -9.38   -30.63  62.629 1   26.75 ? 80  GLU   B CG    1 
ATOM   548  C CD    . GLU   A 1 99  ? -10.9   -30.652 62.628 1   52.88 ? 80  GLU   B CD    1 
ATOM   549  O OE1   . GLU   A 1 99  ? -11.507 -31.487 61.915 1   58.8  ? 80  GLU   B OE1   1 
ATOM   550  O OE2   . GLU   A 1 99  ? -11.489 -29.812 63.341 1   39.45 ? 80  GLU   B OE2   1 
ATOM   551  N N     . ILE   A 1 100 ? -6.141  -29.783 62.886 1   12.44 ? 81  ILE   B N     1 
ATOM   552  C CA    . ILE   A 1 100 ? -5.485  -29.094 63.984 1   11.38 ? 81  ILE   B CA    1 
ATOM   553  C C     . ILE   A 1 100 ? -6.416  -27.973 64.42  1   9.13  ? 81  ILE   B C     1 
ATOM   554  O O     . ILE   A 1 100 ? -6.886  -27.203 63.571 1   9.25  ? 81  ILE   B O     1 
ATOM   555  C CB    . ILE   A 1 100 ? -4.086  -28.539 63.586 1   10.54 ? 81  ILE   B CB    1 
ATOM   556  C CG1   . ILE   A 1 100 ? -3.106  -29.679 63.222 1   11.47 ? 81  ILE   B CG1   1 
ATOM   557  C CG2   . ILE   A 1 100 ? -3.503  -27.619 64.702 1   8.55  ? 81  ILE   B CG2   1 
ATOM   558  C CD1   . ILE   A 1 100 ? -1.753  -29.201 62.65  1   11.75 ? 81  ILE   B CD1   1 
ATOM   559  N N     . VAL   A 1 101 ? -6.673  -27.882 65.736 1   5.42  ? 82  VAL   B N     1 
ATOM   560  C CA    . VAL   A 1 101 ? -7.473  -26.808 66.327 1   4.39  ? 82  VAL   B CA    1 
ATOM   561  C C     . VAL   A 1 101 ? -6.495  -25.944 67.163 1   6.48  ? 82  VAL   B C     1 
ATOM   562  O O     . VAL   A 1 101 ? -5.789  -26.479 68.031 1   4.39  ? 82  VAL   B O     1 
ATOM   563  C CB    . VAL   A 1 101 ? -8.675  -27.359 67.146 1   7.62  ? 82  VAL   B CB    1 
ATOM   564  C CG1   . VAL   A 1 101 ? -9.349  -26.259 67.968 1   7.5   ? 82  VAL   B CG1   1 
ATOM   565  C CG2   . VAL   A 1 101 ? -9.695  -28.025 66.219 1   8.7   ? 82  VAL   B CG2   1 
ATOM   566  N N     . VAL   A 1 102 ? -6.43   -24.623 66.859 1   4.43  ? 83  VAL   B N     1 
ATOM   567  C CA    . VAL   A 1 102 ? -5.556  -23.679 67.572 1   4.18  ? 83  VAL   B CA    1 
ATOM   568  C C     . VAL   A 1 102 ? -6.379  -22.894 68.587 1   6.39  ? 83  VAL   B C     1 
ATOM   569  O O     . VAL   A 1 102 ? -7.524  -22.517 68.29  1   6.95  ? 83  VAL   B O     1 
ATOM   570  C CB    . VAL   A 1 102 ? -4.701  -22.784 66.646 1   6.78  ? 83  VAL   B CB    1 
ATOM   571  C CG1   . VAL   A 1 102 ? -3.851  -23.638 65.709 1   6.9   ? 83  VAL   B CG1   1 
ATOM   572  C CG2   . VAL   A 1 102 ? -5.562  -21.801 65.846 1   6.79  ? 83  VAL   B CG2   1 
ATOM   573  N N     . THR   A 1 103 ? -5.85   -22.738 69.819 1   3     ? 84  THR   B N     1 
ATOM   574  C CA    . THR   A 1 103 ? -6.614  -22.094 70.89  1   3     ? 84  THR   B CA    1 
ATOM   575  C C     . THR   A 1 103 ? -5.771  -21.123 71.727 1   5.66  ? 84  THR   B C     1 
ATOM   576  O O     . THR   A 1 103 ? -4.554  -21.307 71.864 1   3     ? 84  THR   B O     1 
ATOM   577  C CB    . THR   A 1 103 ? -7.249  -23.162 71.828 1   8.01  ? 84  THR   B CB    1 
ATOM   578  O OG1   . THR   A 1 103 ? -6.24   -23.673 72.703 1   12.22 ? 84  THR   B OG1   1 
ATOM   579  C CG2   . THR   A 1 103 ? -7.962  -24.313 71.091 1   10.16 ? 84  THR   B CG2   1 
ATOM   580  N N     . ASP   A 1 104 ? -6.418  -20.104 72.307 1   3     ? 85  ASP   B N     1 
ATOM   581  C CA    . ASP   A 1 104 ? -5.717  -19.155 73.169 1   3     ? 85  ASP   B CA    1 
ATOM   582  C C     . ASP   A 1 104 ? -6.715  -18.35  73.984 1   6.16  ? 85  ASP   B C     1 
ATOM   583  O O     . ASP   A 1 104 ? -7.889  -18.267 73.613 1   3     ? 85  ASP   B O     1 
ATOM   584  C CB    . ASP   A 1 104 ? -4.793  -18.217 72.365 1   3.41  ? 85  ASP   B CB    1 
ATOM   585  C CG    . ASP   A 1 104 ? -3.722  -17.581 73.234 1   5.97  ? 85  ASP   B CG    1 
ATOM   586  O OD1   . ASP   A 1 104 ? -2.789  -18.307 73.646 1   3     ? 85  ASP   B OD1   1 
ATOM   587  O OD2   . ASP   A 1 104 ? -3.829  -16.355 73.516 1   8.07  ? 85  ASP   B OD2   1 
ATOM   588  N N     . TYR   A 1 105 ? -6.251  -17.767 75.094 1   3     ? 86  TYR   B N     1 
ATOM   589  C CA    . TYR   A 1 105 ? -7.107  -16.925 75.912 1   3     ? 86  TYR   B CA    1 
ATOM   590  C C     . TYR   A 1 105 ? -7.321  -15.564 75.258 1   6.87  ? 86  TYR   B C     1 
ATOM   591  O O     . TYR   A 1 105 ? -8.395  -14.983 75.417 1   5.55  ? 86  TYR   B O     1 
ATOM   592  C CB    . TYR   A 1 105 ? -6.536  -16.74  77.325 1   3.06  ? 86  TYR   B CB    1 
ATOM   593  C CG    . TYR   A 1 105 ? -7.527  -16.071 78.251 1   5.37  ? 86  TYR   B CG    1 
ATOM   594  C CD1   . TYR   A 1 105 ? -8.694  -16.725 78.641 1   7.2   ? 86  TYR   B CD1   1 
ATOM   595  C CD2   . TYR   A 1 105 ? -7.353  -14.747 78.655 1   6.27  ? 86  TYR   B CD2   1 
ATOM   596  C CE1   . TYR   A 1 105 ? -9.622  -16.114 79.48  1   7.4   ? 86  TYR   B CE1   1 
ATOM   597  C CE2   . TYR   A 1 105 ? -8.279  -14.119 79.491 1   7.05  ? 86  TYR   B CE2   1 
ATOM   598  C CZ    . TYR   A 1 105 ? -9.417  -14.805 79.894 1   6.84  ? 86  TYR   B CZ    1 
ATOM   599  O OH    . TYR   A 1 105 ? -10.347 -14.202 80.71  1   10.27 ? 86  TYR   B OH    1 
ATOM   600  N N     . SER   A 1 106 ? -6.306  -15.054 74.544 1   3.41  ? 87  SER   B N     1 
ATOM   601  C CA    . SER   A 1 106 ? -6.32   -13.719 73.931 1   3.87  ? 87  SER   B CA    1 
ATOM   602  C C     . SER   A 1 106 ? -6.882  -13.665 72.514 1   7.61  ? 87  SER   B C     1 
ATOM   603  O O     . SER   A 1 106 ? -6.355  -14.322 71.617 1   7.4   ? 87  SER   B O     1 
ATOM   604  C CB    . SER   A 1 106 ? -4.917  -13.113 73.958 1   8.37  ? 87  SER   B CB    1 
ATOM   605  O OG    . SER   A 1 106 ? -4.778  -12.097 72.973 1   7.45  ? 87  SER   B OG    1 
ATOM   606  N N     . ASP   A 1 107 ? -7.911  -12.811 72.302 1   8.66  ? 88  ASP   B N     1 
ATOM   607  C CA    . ASP   A 1 107 ? -8.526  -12.579 70.982 1   8.89  ? 88  ASP   B CA    1 
ATOM   608  C C     . ASP   A 1 107 ? -7.511  -11.909 70.025 1   6.19  ? 88  ASP   B C     1 
ATOM   609  O O     . ASP   A 1 107 ? -7.424  -12.296 68.853 1   7.6   ? 88  ASP   B O     1 
ATOM   610  C CB    . ASP   A 1 107 ? -9.813  -11.742 71.123 1   6.81  ? 88  ASP   B CB    1 
ATOM   611  C CG    . ASP   A 1 107 ? -10.794 -12.381 72.093 1   17.58 ? 88  ASP   B CG    1 
ATOM   612  O OD1   . ASP   A 1 107 ? -11.505 -13.333 71.679 1   22.39 ? 88  ASP   B OD1   1 
ATOM   613  O OD2   . ASP   A 1 107 ? -10.809 -11.97  73.283 1   28    ? 88  ASP   B OD2   1 
ATOM   614  N N     . GLN   A 1 108 ? -6.692  -10.964 70.544 1   7.7   ? 89  GLN   B N     1 
ATOM   615  C CA    . GLN   A 1 108 ? -5.632  -10.304 69.755 1   7.37  ? 89  GLN   B CA    1 
ATOM   616  C C     . GLN   A 1 108 ? -4.66   -11.356 69.176 1   8.58  ? 89  GLN   B C     1 
ATOM   617  O O     . GLN   A 1 108 ? -4.246  -11.247 68.02  1   4.48  ? 89  GLN   B O     1 
ATOM   618  C CB    . GLN   A 1 108 ? -4.817  -9.331  70.624 1   7.88  ? 89  GLN   B CB    1 
ATOM   619  C CG    . GLN   A 1 108 ? -5.475  -7.989  70.913 1   15.99 ? 89  GLN   B CG    1 
ATOM   620  C CD    . GLN   A 1 108 ? -4.453  -7.039  71.505 1   40.77 ? 89  GLN   B CD    1 
ATOM   621  O OE1   . GLN   A 1 108 ? -4.241  -6.991  72.723 1   34.64 ? 89  GLN   B OE1   1 
ATOM   622  N NE2   . GLN   A 1 108 ? -3.775  -6.278  70.654 1   35.22 ? 89  GLN   B NE2   1 
ATOM   623  N N     . ASN   A 1 109 ? -4.283  -12.357 70.006 1   7.2   ? 90  ASN   B N     1 
ATOM   624  C CA    . ASN   A 1 109 ? -3.359  -13.425 69.601 1   7.99  ? 90  ASN   B CA    1 
ATOM   625  C C     . ASN   A 1 109 ? -3.931  -14.258 68.472 1   9.06  ? 90  ASN   B C     1 
ATOM   626  O O     . ASN   A 1 109 ? -3.239  -14.483 67.475 1   8.99  ? 90  ASN   B O     1 
ATOM   627  C CB    . ASN   A 1 109 ? -2.947  -14.298 70.804 1   8.47  ? 90  ASN   B CB    1 
ATOM   628  C CG    . ASN   A 1 109 ? -1.925  -13.627 71.697 1   4.2   ? 90  ASN   B CG    1 
ATOM   629  O OD1   . ASN   A 1 109 ? -1.283  -12.64  71.307 1   9.56  ? 90  ASN   B OD1   1 
ATOM   630  N ND2   . ASN   A 1 109 ? -1.738  -14.147 72.913 1   9.75  ? 90  ASN   B ND2   1 
ATOM   631  N N     . LEU   A 1 110 ? -5.218  -14.645 68.587 1   12.86 ? 91  LEU   B N     1 
ATOM   632  C CA    . LEU   A 1 110 ? -5.934  -15.419 67.567 1   13.3  ? 91  LEU   B CA    1 
ATOM   633  C C     . LEU   A 1 110 ? -6.082  -14.627 66.252 1   10.78 ? 91  LEU   B C     1 
ATOM   634  O O     . LEU   A 1 110 ? -6.031  -15.217 65.17  1   11.9  ? 91  LEU   B O     1 
ATOM   635  C CB    . LEU   A 1 110 ? -7.305  -15.873 68.091 1   13.29 ? 91  LEU   B CB    1 
ATOM   636  C CG    . LEU   A 1 110 ? -7.302  -16.748 69.359 1   9.22  ? 91  LEU   B CG    1 
ATOM   637  C CD1   . LEU   A 1 110 ? -8.719  -17.115 69.771 1   9.21  ? 91  LEU   B CD1   1 
ATOM   638  C CD2   . LEU   A 1 110 ? -6.474  -18.005 69.166 1   9.89  ? 91  LEU   B CD2   1 
ATOM   639  N N     . GLN   A 1 111 ? -6.23   -13.29  66.349 1   12.27 ? 92  GLN   B N     1 
ATOM   640  C CA    . GLN   A 1 111 ? -6.318  -12.421 65.167 1   12.56 ? 92  GLN   B CA    1 
ATOM   641  C C     . GLN   A 1 111 ? -4.984  -12.42  64.406 1   14.38 ? 92  GLN   B C     1 
ATOM   642  O O     . GLN   A 1 111 ? -4.989  -12.503 63.173 1   16.05 ? 92  GLN   B O     1 
ATOM   643  C CB    . GLN   A 1 111 ? -6.74   -10.995 65.561 1   11.92 ? 92  GLN   B CB    1 
ATOM   644  C CG    . GLN   A 1 111 ? -8.231  -10.882 65.888 1   22.2  ? 92  GLN   B CG    1 
ATOM   645  C CD    . GLN   A 1 111 ? -8.577  -9.621  66.648 1   45.35 ? 92  GLN   B CD    1 
ATOM   646  O OE1   . GLN   A 1 111 ? -7.971  -8.554  66.461 1   39.35 ? 92  GLN   B OE1   1 
ATOM   647  N NE2   . GLN   A 1 111 ? -9.573  -9.715  67.521 1   38.49 ? 92  GLN   B NE2   1 
ATOM   648  N N     . GLU   A 1 112 ? -3.843  -12.388 65.143 1   12.84 ? 93  GLU   B N     1 
ATOM   649  C CA    . GLU   A 1 112 ? -2.504  -12.446 64.54  1   12.18 ? 93  GLU   B CA    1 
ATOM   650  C C     . GLU   A 1 112 ? -2.289  -13.805 63.84  1   16.82 ? 93  GLU   B C     1 
ATOM   651  O O     . GLU   A 1 112 ? -1.786  -13.828 62.713 1   19.19 ? 93  GLU   B O     1 
ATOM   652  C CB    . GLU   A 1 112 ? -1.4    -12.166 65.578 1   11.88 ? 93  GLU   B CB    1 
ATOM   653  C CG    . GLU   A 1 112 ? -0.004  -12.012 64.976 1   20.13 ? 93  GLU   B CG    1 
ATOM   654  C CD    . GLU   A 1 112 ? 0.251   -10.834 64.046 1   44.13 ? 93  GLU   B CD    1 
ATOM   655  O OE1   . GLU   A 1 112 ? -0.407  -9.778  64.208 1   42.92 ? 93  GLU   B OE1   1 
ATOM   656  O OE2   . GLU   A 1 112 ? 1.129   -10.964 63.162 1   34.54 ? 93  GLU   B OE2   1 
ATOM   657  N N     . LEU   A 1 113 ? -2.718  -14.917 64.49  1   16.4  ? 94  LEU   B N     1 
ATOM   658  C CA    . LEU   A 1 113 ? -2.658  -16.288 63.946 1   18.39 ? 94  LEU   B CA    1 
ATOM   659  C C     . LEU   A 1 113 ? -3.401  -16.347 62.609 1   24    ? 94  LEU   B C     1 
ATOM   660  O O     . LEU   A 1 113 ? -2.845  -16.827 61.614 1   25.13 ? 94  LEU   B O     1 
ATOM   661  C CB    . LEU   A 1 113 ? -3.364  -17.28  64.903 1   19.92 ? 94  LEU   B CB    1 
ATOM   662  C CG    . LEU   A 1 113 ? -2.551  -18.025 65.952 1   25.08 ? 94  LEU   B CG    1 
ATOM   663  C CD1   . LEU   A 1 113 ? -3.476  -18.785 66.889 1   25.62 ? 94  LEU   B CD1   1 
ATOM   664  C CD2   . LEU   A 1 113 ? -1.622  -19.026 65.322 1   26.93 ? 94  LEU   B CD2   1 
ATOM   665  N N     . GLU   A 1 114 ? -4.669  -15.87  62.612 1   20.36 ? 95  GLU   B N     1 
ATOM   666  C CA    . GLU   A 1 114 ? -5.575  -15.849 61.466 1   21.62 ? 95  GLU   B CA    1 
ATOM   667  C C     . GLU   A 1 114 ? -5.03   -15.034 60.294 1   24.68 ? 95  GLU   B C     1 
ATOM   668  O O     . GLU   A 1 114 ? -5.243  -15.434 59.145 1   25.44 ? 95  GLU   B O     1 
ATOM   669  C CB    . GLU   A 1 114 ? -6.984  -15.408 61.876 1   22.62 ? 95  GLU   B CB    1 
ATOM   670  C CG    . GLU   A 1 114 ? -7.767  -16.556 62.492 1   34.21 ? 95  GLU   B CG    1 
ATOM   671  C CD    . GLU   A 1 114 ? -9.098  -16.227 63.141 1   60    ? 95  GLU   B CD    1 
ATOM   672  O OE1   . GLU   A 1 114 ? -9.167  -15.239 63.911 1   60.5  ? 95  GLU   B OE1   1 
ATOM   673  O OE2   . GLU   A 1 114 ? -10.066 -16.987 62.905 1   53.3  ? 95  GLU   B OE2   1 
ATOM   674  N N     . LYS   A 1 115 ? -4.278  -13.937 60.575 1   18.94 ? 96  LYS   B N     1 
ATOM   675  C CA    . LYS   A 1 115 ? -3.614  -13.129 59.542 1   18.19 ? 96  LYS   B CA    1 
ATOM   676  C C     . LYS   A 1 115 ? -2.64   -14.032 58.755 1   22.59 ? 96  LYS   B C     1 
ATOM   677  O O     . LYS   A 1 115 ? -2.65   -14.012 57.52  1   22.56 ? 96  LYS   B O     1 
ATOM   678  C CB    . LYS   A 1 115 ? -2.865  -11.935 60.161 1   18.59 ? 96  LYS   B CB    1 
ATOM   679  C CG    . LYS   A 1 115 ? -3.769  -10.769 60.54  1   27.84 ? 96  LYS   B CG    1 
ATOM   680  C CD    . LYS   A 1 115 ? -2.965  -9.625  61.133 1   36.88 ? 96  LYS   B CD    1 
ATOM   681  C CE    . LYS   A 1 115 ? -3.865  -8.496  61.567 1   50.97 ? 96  LYS   B CE    1 
ATOM   682  N NZ    . LYS   A 1 115 ? -3.098  -7.386  62.184 1   59.76 ? 96  LYS   B NZ    1 
ATOM   683  N N     . TRP   A 1 116 ? -1.865  -14.891 59.471 1   17.55 ? 97  TRP   B N     1 
ATOM   684  C CA    . TRP   A 1 116 ? -0.963  -15.825 58.801 1   17.36 ? 97  TRP   B CA    1 
ATOM   685  C C     . TRP   A 1 116 ? -1.729  -16.942 58.079 1   24.68 ? 97  TRP   B C     1 
ATOM   686  O O     . TRP   A 1 116 ? -1.39   -17.261 56.939 1   25.17 ? 97  TRP   B O     1 
ATOM   687  C CB    . TRP   A 1 116 ? 0.118   -16.377 59.742 1   15.05 ? 97  TRP   B CB    1 
ATOM   688  C CG    . TRP   A 1 116 ? 1.161   -17.161 59.005 1   16.16 ? 97  TRP   B CG    1 
ATOM   689  C CD1   . TRP   A 1 116 ? 2.301   -16.679 58.427 1   19.1  ? 97  TRP   B CD1   1 
ATOM   690  C CD2   . TRP   A 1 116 ? 1.106   -18.558 58.684 1   18.09 ? 97  TRP   B CD2   1 
ATOM   691  N NE1   . TRP   A 1 116 ? 2.972   -17.693 57.784 1   20.05 ? 97  TRP   B NE1   1 
ATOM   692  C CE2   . TRP   A 1 116 ? 2.261   -18.861 57.928 1   22.27 ? 97  TRP   B CE2   1 
ATOM   693  C CE3   . TRP   A 1 116 ? 0.19    -19.591 58.968 1   19.72 ? 97  TRP   B CE3   1 
ATOM   694  C CZ2   . TRP   A 1 116 ? 2.529   -20.158 57.459 1   23.11 ? 97  TRP   B CZ2   1 
ATOM   695  C CZ3   . TRP   A 1 116 ? 0.445   -20.87  58.488 1   22.1  ? 97  TRP   B CZ3   1 
ATOM   696  C CH2   . TRP   A 1 116 ? 1.601   -21.145 57.746 1   23.37 ? 97  TRP   B CH2   1 
ATOM   697  N N     . LEU   A 1 117 ? -2.754  -17.519 58.732 1   23.85 ? 98  LEU   B N     1 
ATOM   698  C CA    . LEU   A 1 117 ? -3.604  -18.581 58.184 1   25.97 ? 98  LEU   B CA    1 
ATOM   699  C C     . LEU   A 1 117 ? -4.282  -18.161 56.862 1   32.81 ? 98  LEU   B C     1 
ATOM   700  O O     . LEU   A 1 117 ? -4.366  -18.968 55.936 1   33.74 ? 98  LEU   B O     1 
ATOM   701  C CB    . LEU   A 1 117 ? -4.675  -18.957 59.227 1   25.49 ? 98  LEU   B CB    1 
ATOM   702  C CG    . LEU   A 1 117 ? -4.527  -20.247 60.065 1   28.46 ? 98  LEU   B CG    1 
ATOM   703  C CD1   . LEU   A 1 117 ? -3.091  -20.727 60.176 1   28.5  ? 98  LEU   B CD1   1 
ATOM   704  C CD2   . LEU   A 1 117 ? -5.16   -20.079 61.434 1   28.81 ? 98  LEU   B CD2   1 
ATOM   705  N N     . LYS   A 1 118 ? -4.751  -16.901 56.783 1   32.21 ? 99  LYS   B N     1 
ATOM   706  C CA    . LYS   A 1 118 ? -5.429  -16.337 55.607 1   33.55 ? 99  LYS   B CA    1 
ATOM   707  C C     . LYS   A 1 118 ? -4.45   -15.697 54.606 1   40.62 ? 99  LYS   B C     1 
ATOM   708  O O     . LYS   A 1 118 ? -4.886  -15.182 53.574 1   41.52 ? 99  LYS   B O     1 
ATOM   709  C CB    . LYS   A 1 118 ? -6.516  -15.329 56.048 1   34.63 ? 99  LYS   B CB    1 
ATOM   710  C CG    . LYS   A 1 118 ? -7.744  -15.993 56.675 1   48.3  ? 99  LYS   B CG    1 
ATOM   711  C CD    . LYS   A 1 118 ? -8.543  -15.026 57.545 1   55.01 ? 99  LYS   B CD    1 
ATOM   712  C CE    . LYS   A 1 118 ? -9.763  -15.692 58.136 1   63.32 ? 99  LYS   B CE    1 
ATOM   713  N NZ    . LYS   A 1 118 ? -10.466 -14.808 59.104 1   70.68 ? 99  LYS   B NZ    1 
ATOM   714  N N     . ALA   A 1 119 ? -3.128  -15.766 54.9   1   38.45 ? 100 ALA   B N     1 
ATOM   715  C CA    . ALA   A 1 119 ? -2.025  -15.202 54.11  1   39.55 ? 100 ALA   B CA    1 
ATOM   716  C C     . ALA   A 1 119 ? -2.193  -13.7   53.858 1   44.54 ? 100 ALA   B C     1 
ATOM   717  O O     . ALA   A 1 119 ? -2.019  -13.213 52.737 1   45.17 ? 100 ALA   B O     1 
ATOM   718  C CB    . ALA   A 1 119 ? -1.823  -15.977 52.807 1   41.96 ? 100 ALA   B CB    1 
ATOM   719  N N     . ALA   A 1 120 ? -2.493  -12.968 54.938 1   40.73 ? 101 ALA   B N     1 
ATOM   720  C CA    . ALA   A 1 120 ? -2.669  -11.519 54.945 1   39.83 ? 101 ALA   B CA    1 
ATOM   721  C C     . ALA   A 1 120 ? -1.32   -10.806 54.695 1   44.81 ? 101 ALA   B C     1 
ATOM   722  O O     . ALA   A 1 120 ? -0.264  -11.426 54.871 1   44.8  ? 101 ALA   B O     1 
ATOM   723  C CB    . ALA   A 1 120 ? -3.263  -11.078 56.279 1   39.25 ? 101 ALA   B CB    1 
ATOM   724  N N     . PRO   A 1 121 ? -1.33   -9.517  54.269 1   41.48 ? 102 PRO   B N     1 
ATOM   725  C CA    . PRO   A 1 121 ? -0.06   -8.803  54.029 1   41.61 ? 102 PRO   B CA    1 
ATOM   726  C C     . PRO   A 1 121 ? 0.755   -8.512  55.297 1   42.74 ? 102 PRO   B C     1 
ATOM   727  O O     . PRO   A 1 121 ? 1.978   -8.668  55.288 1   43.33 ? 102 PRO   B O     1 
ATOM   728  C CB    . PRO   A 1 121 ? -0.535  -7.494  53.406 1   42.76 ? 102 PRO   B CB    1 
ATOM   729  C CG    . PRO   A 1 121 ? -1.903  -7.28   54.033 1   46.01 ? 102 PRO   B CG    1 
ATOM   730  C CD    . PRO   A 1 121 ? -2.488  -8.644  53.973 1   42.1  ? 102 PRO   B CD    1 
ATOM   731  N N     . ALA   A 1 122 ? 0.07    -8.06   56.374 1   36.1  ? 103 ALA   B N     1 
ATOM   732  C CA    . ALA   A 1 122 ? 0.652   -7.706  57.668 1   34.59 ? 103 ALA   B CA    1 
ATOM   733  C C     . ALA   A 1 122 ? 0.959   -8.936  58.546 1   35.85 ? 103 ALA   B C     1 
ATOM   734  O O     . ALA   A 1 122 ? 1.36    -8.771  59.701 1   34.94 ? 103 ALA   B O     1 
ATOM   735  C CB    . ALA   A 1 122 ? -0.262  -6.732  58.405 1   34.02 ? 103 ALA   B CB    1 
ATOM   736  N N     . ALA   A 1 123 ? 0.792   -10.163 57.986 1   30.71 ? 104 ALA   B N     1 
ATOM   737  C CA    . ALA   A 1 123 ? 1.08    -11.427 58.673 1   29.48 ? 104 ALA   B CA    1 
ATOM   738  C C     . ALA   A 1 123 ? 2.582   -11.552 58.912 1   29.67 ? 104 ALA   B C     1 
ATOM   739  O O     . ALA   A 1 123 ? 3.382   -10.996 58.153 1   29.89 ? 104 ALA   B O     1 
ATOM   740  C CB    . ALA   A 1 123 ? 0.579   -12.606 57.851 1   31.03 ? 104 ALA   B CB    1 
ATOM   741  N N     . PHE   A 1 124 ? 2.961   -12.254 59.988 1   22.54 ? 105 PHE   B N     1 
ATOM   742  C CA    . PHE   A 1 124 ? 4.36    -12.433 60.359 1   20.73 ? 105 PHE   B CA    1 
ATOM   743  C C     . PHE   A 1 124 ? 5.096   -13.326 59.361 1   23.1  ? 105 PHE   B C     1 
ATOM   744  O O     . PHE   A 1 124 ? 4.507   -14.264 58.811 1   23.11 ? 105 PHE   B O     1 
ATOM   745  C CB    . PHE   A 1 124 ? 4.472   -13.005 61.786 1   20.71 ? 105 PHE   B CB    1 
ATOM   746  C CG    . PHE   A 1 124 ? 5.872   -13.057 62.348 1   21.27 ? 105 PHE   B CG    1 
ATOM   747  C CD1   . PHE   A 1 124 ? 6.525   -11.892 62.741 1   23.66 ? 105 PHE   B CD1   1 
ATOM   748  C CD2   . PHE   A 1 124 ? 6.529   -14.272 62.51  1   22.83 ? 105 PHE   B CD2   1 
ATOM   749  C CE1   . PHE   A 1 124 ? 7.826   -11.937 63.254 1   23.89 ? 105 PHE   B CE1   1 
ATOM   750  C CE2   . PHE   A 1 124 ? 7.824   -14.32  63.035 1   24.96 ? 105 PHE   B CE2   1 
ATOM   751  C CZ    . PHE   A 1 124 ? 8.463   -13.151 63.407 1   22.69 ? 105 PHE   B CZ    1 
ATOM   752  N N     . ASP   A 1 125 ? 6.382   -13.018 59.13  1   19.1  ? 106 ASP   B N     1 
ATOM   753  C CA    . ASP   A 1 125 ? 7.248   -13.782 58.234 1   20.22 ? 106 ASP   B CA    1 
ATOM   754  C C     . ASP   A 1 125 ? 7.865   -14.984 58.962 1   21.7  ? 106 ASP   B C     1 
ATOM   755  O O     . ASP   A 1 125 ? 8.857   -14.834 59.684 1   21.13 ? 106 ASP   B O     1 
ATOM   756  C CB    . ASP   A 1 125 ? 8.341   -12.884 57.618 1   22.96 ? 106 ASP   B CB    1 
ATOM   757  C CG    . ASP   A 1 125 ? 9.21    -13.581 56.584 1   39.2  ? 106 ASP   B CG    1 
ATOM   758  O OD1   . ASP   A 1 125 ? 8.713   -14.523 55.924 1   40.57 ? 106 ASP   B OD1   1 
ATOM   759  O OD2   . ASP   A 1 125 ? 10.385  -13.175 56.426 1   49.37 ? 106 ASP   B OD2   1 
ATOM   760  N N     . TRP   A 1 126 ? 7.267   -16.174 58.753 1   18.36 ? 107 TRP   B N     1 
ATOM   761  C CA    . TRP   A 1 126 ? 7.714   -17.448 59.331 1   17.71 ? 107 TRP   B CA    1 
ATOM   762  C C     . TRP   A 1 126 ? 8.65    -18.224 58.383 1   22.82 ? 107 TRP   B C     1 
ATOM   763  O O     . TRP   A 1 126 ? 9.173   -19.275 58.773 1   23.1  ? 107 TRP   B O     1 
ATOM   764  C CB    . TRP   A 1 126 ? 6.5     -18.314 59.716 1   16    ? 107 TRP   B CB    1 
ATOM   765  C CG    . TRP   A 1 126 ? 5.777   -17.84  60.947 1   14.55 ? 107 TRP   B CG    1 
ATOM   766  C CD1   . TRP   A 1 126 ? 4.587   -17.17  60.998 1   15.53 ? 107 TRP   B CD1   1 
ATOM   767  C CD2   . TRP   A 1 126 ? 6.198   -18.018 62.308 1   13.07 ? 107 TRP   B CD2   1 
ATOM   768  N NE1   . TRP   A 1 126 ? 4.24    -16.917 62.309 1   13.69 ? 107 TRP   B NE1   1 
ATOM   769  C CE2   . TRP   A 1 126 ? 5.212   -17.428 63.134 1   13.77 ? 107 TRP   B CE2   1 
ATOM   770  C CE3   . TRP   A 1 126 ? 7.324   -18.616 62.913 1   13.32 ? 107 TRP   B CE3   1 
ATOM   771  C CZ2   . TRP   A 1 126 ? 5.308   -17.43  64.531 1   12.02 ? 107 TRP   B CZ2   1 
ATOM   772  C CZ3   . TRP   A 1 126 ? 7.412   -18.622 64.3   1   12.1  ? 107 TRP   B CZ3   1 
ATOM   773  C CH2   . TRP   A 1 126 ? 6.416   -18.032 65.092 1   11.21 ? 107 TRP   B CH2   1 
ATOM   774  N N     . SER   A 1 127 ? 8.89    -17.693 57.156 1   20.88 ? 108 SER   B N     1 
ATOM   775  C CA    . SER   A 1 127 ? 9.73    -18.337 56.133 1   22.58 ? 108 SER   B CA    1 
ATOM   776  C C     . SER   A 1 127 ? 11.093  -18.901 56.643 1   26.27 ? 108 SER   B C     1 
ATOM   777  O O     . SER   A 1 127 ? 11.38   -20.041 56.266 1   27.69 ? 108 SER   B O     1 
ATOM   778  C CB    . SER   A 1 127 ? 9.937   -17.427 54.92  1   27.95 ? 108 SER   B CB    1 
ATOM   779  O OG    . SER   A 1 127 ? 10.771  -16.312 55.189 1   35.35 ? 108 SER   B OG    1 
ATOM   780  N N     . PRO   A 1 128 ? 11.92   -18.229 57.511 1   23.25 ? 109 PRO   B N     1 
ATOM   781  C CA    . PRO   A 1 128 ? 13.173  -18.876 57.965 1   22.62 ? 109 PRO   B CA    1 
ATOM   782  C C     . PRO   A 1 128 ? 12.932  -20.09  58.876 1   21.44 ? 109 PRO   B C     1 
ATOM   783  O O     . PRO   A 1 128 ? 13.735  -21.03  58.876 1   21.76 ? 109 PRO   B O     1 
ATOM   784  C CB    . PRO   A 1 128 ? 13.915  -17.759 58.715 1   23.65 ? 109 PRO   B CB    1 
ATOM   785  C CG    . PRO   A 1 128 ? 13.202  -16.496 58.389 1   26.8  ? 109 PRO   B CG    1 
ATOM   786  C CD    . PRO   A 1 128 ? 11.786  -16.882 58.113 1   23.69 ? 109 PRO   B CD    1 
ATOM   787  N N     . VAL   A 1 129 ? 11.822  -20.064 59.655 1   17.06 ? 110 VAL   B N     1 
ATOM   788  C CA    . VAL   A 1 129 ? 11.429  -21.16  60.547 1   14.95 ? 110 VAL   B CA    1 
ATOM   789  C C     . VAL   A 1 129 ? 10.891  -22.318 59.675 1   17.57 ? 110 VAL   B C     1 
ATOM   790  O O     . VAL   A 1 129 ? 11.27   -23.474 59.884 1   17.1  ? 110 VAL   B O     1 
ATOM   791  C CB    . VAL   A 1 129 ? 10.408  -20.677 61.63  1   14.3  ? 110 VAL   B CB    1 
ATOM   792  C CG1   . VAL   A 1 129 ? 9.858   -21.844 62.455 1   12.25 ? 110 VAL   B CG1   1 
ATOM   793  C CG2   . VAL   A 1 129 ? 11.033  -19.609 62.539 1   13.23 ? 110 VAL   B CG2   1 
ATOM   794  N N     . VAL   A 1 130 ? 10.042  -21.987 58.673 1   17.16 ? 111 VAL   B N     1 
ATOM   795  C CA    . VAL   A 1 130 ? 9.469   -22.958 57.723 1   18.41 ? 111 VAL   B CA    1 
ATOM   796  C C     . VAL   A 1 130 ? 10.591  -23.7   56.966 1   23.1  ? 111 VAL   B C     1 
ATOM   797  O O     . VAL   A 1 130 ? 10.535  -24.933 56.847 1   23.84 ? 111 VAL   B O     1 
ATOM   798  C CB    . VAL   A 1 130 ? 8.434   -22.286 56.772 1   20.75 ? 111 VAL   B CB    1 
ATOM   799  C CG1   . VAL   A 1 130 ? 8.002   -23.232 55.648 1   22.83 ? 111 VAL   B CG1   1 
ATOM   800  C CG2   . VAL   A 1 130 ? 7.219   -21.791 57.553 1   18.4  ? 111 VAL   B CG2   1 
ATOM   801  N N     . THR   A 1 131 ? 11.623  -22.95  56.498 1   22.29 ? 112 THR   B N     1 
ATOM   802  C CA    . THR   A 1 131 ? 12.783  -23.502 55.78  1   24.27 ? 112 THR   B CA    1 
ATOM   803  C C     . THR   A 1 131 ? 13.534  -24.479 56.693 1   24.97 ? 112 THR   B C     1 
ATOM   804  O O     . THR   A 1 131 ? 13.912  -25.568 56.246 1   26.02 ? 112 THR   B O     1 
ATOM   805  C CB    . THR   A 1 131 ? 13.689  -22.368 55.249 1   30.92 ? 112 THR   B CB    1 
ATOM   806  O OG1   . THR   A 1 131 ? 12.947  -21.574 54.32  1   31.59 ? 112 THR   B OG1   1 
ATOM   807  C CG2   . THR   A 1 131 ? 14.971  -22.89  54.573 1   33.8  ? 112 THR   B CG2   1 
ATOM   808  N N     . TYR   A 1 132 ? 13.726  -24.089 57.973 1   20.06 ? 113 TYR   B N     1 
ATOM   809  C CA    . TYR   A 1 132 ? 14.421  -24.908 58.96  1   18.7  ? 113 TYR   B CA    1 
ATOM   810  C C     . TYR   A 1 132 ? 13.724  -26.268 59.142 1   17.9  ? 113 TYR   B C     1 
ATOM   811  O O     . TYR   A 1 132 ? 14.4    -27.3   59.116 1   17.7  ? 113 TYR   B O     1 
ATOM   812  C CB    . TYR   A 1 132 ? 14.578  -24.147 60.291 1   17.48 ? 113 TYR   B CB    1 
ATOM   813  C CG    . TYR   A 1 132 ? 15.474  -24.844 61.292 1   17.29 ? 113 TYR   B CG    1 
ATOM   814  C CD1   . TYR   A 1 132 ? 16.855  -24.669 61.261 1   18.97 ? 113 TYR   B CD1   1 
ATOM   815  C CD2   . TYR   A 1 132 ? 14.939  -25.648 62.294 1   15.68 ? 113 TYR   B CD2   1 
ATOM   816  C CE1   . TYR   A 1 132 ? 17.684  -25.299 62.185 1   18.11 ? 113 TYR   B CE1   1 
ATOM   817  C CE2   . TYR   A 1 132 ? 15.761  -26.305 63.208 1   15.47 ? 113 TYR   B CE2   1 
ATOM   818  C CZ    . TYR   A 1 132 ? 17.132  -26.112 63.16  1   18.27 ? 113 TYR   B CZ    1 
ATOM   819  O OH    . TYR   A 1 132 ? 17.952  -26.731 64.067 1   19.16 ? 113 TYR   B OH    1 
ATOM   820  N N     . VAL   A 1 133 ? 12.376  -26.269 59.271 1   14.84 ? 114 VAL   B N     1 
ATOM   821  C CA    . VAL   A 1 133 ? 11.576  -27.5   59.424 1   14.19 ? 114 VAL   B CA    1 
ATOM   822  C C     . VAL   A 1 133 ? 11.68   -28.392 58.157 1   18.33 ? 114 VAL   B C     1 
ATOM   823  O O     . VAL   A 1 133 ? 11.872  -29.607 58.275 1   17.83 ? 114 VAL   B O     1 
ATOM   824  C CB    . VAL   A 1 133 ? 10.113  -27.203 59.85  1   13.17 ? 114 VAL   B CB    1 
ATOM   825  C CG1   . VAL   A 1 133 ? 9.259   -28.479 59.884 1   13.14 ? 114 VAL   B CG1   1 
ATOM   826  C CG2   . VAL   A 1 133 ? 10.076  -26.492 61.206 1   11.97 ? 114 VAL   B CG2   1 
ATOM   827  N N     . CYS   A 1 134 ? 11.599  -27.777 56.957 1   20.13 ? 115 CYS   B N     1 
ATOM   828  C CA    . CYS   A 1 134 ? 11.753  -28.502 55.688 1   23.72 ? 115 CYS   B CA    1 
ATOM   829  C C     . CYS   A 1 134 ? 13.101  -29.24  55.621 1   27    ? 115 CYS   B C     1 
ATOM   830  O O     . CYS   A 1 134 ? 13.124  -30.396 55.196 1   28.05 ? 115 CYS   B O     1 
ATOM   831  C CB    . CYS   A 1 134 ? 11.554  -27.57  54.502 1   25.92 ? 115 CYS   B CB    1 
ATOM   832  S SG    . CYS   A 1 134 ? 9.847   -27.013 54.301 1   27.78 ? 115 CYS   B SG    1 
ATOM   833  N N     . ASP   A 1 135 ? 14.195  -28.61  56.127 1   25.63 ? 116 ASP   B N     1 
ATOM   834  C CA    . ASP   A 1 135 ? 15.536  -29.212 56.202 1   27.11 ? 116 ASP   B CA    1 
ATOM   835  C C     . ASP   A 1 135 ? 15.555  -30.435 57.139 1   30.16 ? 116 ASP   B C     1 
ATOM   836  O O     . ASP   A 1 135 ? 16.085  -31.484 56.758 1   31.4  ? 116 ASP   B O     1 
ATOM   837  C CB    . ASP   A 1 135 ? 16.594  -28.189 56.671 1   28.22 ? 116 ASP   B CB    1 
ATOM   838  C CG    . ASP   A 1 135 ? 16.768  -26.947 55.815 1   43.64 ? 116 ASP   B CG    1 
ATOM   839  O OD1   . ASP   A 1 135 ? 16.735  -27.07  54.563 1   47.13 ? 116 ASP   B OD1   1 
ATOM   840  O OD2   . ASP   A 1 135 ? 16.962  -25.852 56.392 1   48.97 ? 116 ASP   B OD2   1 
ATOM   841  N N     . LEU   A 1 136 ? 14.99   -30.292 58.367 1   24.41 ? 117 LEU   B N     1 
ATOM   842  C CA    . LEU   A 1 136 ? 14.905  -31.368 59.371 1   22.65 ? 117 LEU   B CA    1 
ATOM   843  C C     . LEU   A 1 136 ? 14.195  -32.613 58.822 1   27.95 ? 117 LEU   B C     1 
ATOM   844  O O     . LEU   A 1 136 ? 14.656  -33.732 59.05  1   27.69 ? 117 LEU   B O     1 
ATOM   845  C CB    . LEU   A 1 136 ? 14.138  -30.905 60.641 1   19.78 ? 117 LEU   B CB    1 
ATOM   846  C CG    . LEU   A 1 136 ? 14.626  -29.683 61.448 1   21.79 ? 117 LEU   B CG    1 
ATOM   847  C CD1   . LEU   A 1 136 ? 13.669  -29.396 62.603 1   19.04 ? 117 LEU   B CD1   1 
ATOM   848  C CD2   . LEU   A 1 136 ? 16.043  -29.865 61.984 1   24.03 ? 117 LEU   B CD2   1 
ATOM   849  N N     . GLU   A 1 137 ? 13.074  -32.401 58.094 1   27.36 ? 118 GLU   B N     1 
ATOM   850  C CA    . GLU   A 1 137 ? 12.184  -33.427 57.535 1   29.02 ? 118 GLU   B CA    1 
ATOM   851  C C     . GLU   A 1 137 ? 12.709  -34.134 56.26  1   36.45 ? 118 GLU   B C     1 
ATOM   852  O O     . GLU   A 1 137 ? 11.951  -34.861 55.607 1   38.12 ? 118 GLU   B O     1 
ATOM   853  C CB    . GLU   A 1 137 ? 10.781  -32.837 57.302 1   29.8  ? 118 GLU   B CB    1 
ATOM   854  C CG    . GLU   A 1 137 ? 10.108  -32.393 58.592 1   34.19 ? 118 GLU   B CG    1 
ATOM   855  C CD    . GLU   A 1 137 ? 8.634   -32.032 58.554 1   44.09 ? 118 GLU   B CD    1 
ATOM   856  O OE1   . GLU   A 1 137 ? 8.038   -32.067 57.454 1   45.78 ? 118 GLU   B OE1   1 
ATOM   857  O OE2   . GLU   A 1 137 ? 8.073   -31.72  59.632 1   21.59 ? 118 GLU   B OE2   1 
ATOM   858  N N     . GLY   A 1 138 ? 13.993  -33.94  55.949 1   35.86 ? 119 GLY   B N     1 
ATOM   859  C CA    . GLY   A 1 138 ? 14.664  -34.574 54.817 1   39.01 ? 119 GLY   B CA    1 
ATOM   860  C C     . GLY   A 1 138 ? 14.572  -33.865 53.479 1   45.91 ? 119 GLY   B C     1 
ATOM   861  O O     . GLY   A 1 138 ? 14.906  -34.467 52.448 1   48.65 ? 119 GLY   B O     1 
ATOM   862  N N     . ASN   A 1 139 ? 14.142  -32.575 53.479 1   43.52 ? 120 ASN   B N     1 
ATOM   863  C CA    . ASN   A 1 139 ? 13.974  -31.735 52.279 1   45.85 ? 120 ASN   B CA    1 
ATOM   864  C C     . ASN   A 1 139 ? 13.028  -32.38  51.234 1   50.84 ? 120 ASN   B C     1 
ATOM   865  O O     . ASN   A 1 139 ? 13.26   -32.278 50.019 1   53.38 ? 120 ASN   B O     1 
ATOM   866  C CB    . ASN   A 1 139 ? 15.335  -31.325 51.668 1   50.31 ? 120 ASN   B CB    1 
ATOM   867  C CG    . ASN   A 1 139 ? 16.009  -30.171 52.368 1   71.88 ? 120 ASN   B CG    1 
ATOM   868  O OD1   . ASN   A 1 139 ? 15.545  -29.023 52.327 1   65.49 ? 120 ASN   B OD1   1 
ATOM   869  N ND2   . ASN   A 1 139 ? 17.132  -30.447 53.011 1   66.18 ? 120 ASN   B ND2   1 
ATOM   870  N N     . ARG   A 1 140 ? 11.969  -33.064 51.73  1   46.92 ? 121 ARG   B N     1 
ATOM   871  C CA    . ARG   A 1 140 ? 10.954  -33.733 50.909 1   48.23 ? 121 ARG   B CA    1 
ATOM   872  C C     . ARG   A 1 140 ? 10.123  -32.696 50.158 1   50.97 ? 121 ARG   B C     1 
ATOM   873  O O     . ARG   A 1 140 ? 9.786   -32.907 48.99  1   53.11 ? 121 ARG   B O     1 
ATOM   874  C CB    . ARG   A 1 140 ? 10.033  -34.616 51.773 1   46.68 ? 121 ARG   B CB    1 
ATOM   875  C CG    . ARG   A 1 140 ? 10.7    -35.858 52.357 1   54.7  ? 121 ARG   B CG    1 
ATOM   876  C CD    . ARG   A 1 140 ? 9.701   -36.677 53.154 1   61.05 ? 121 ARG   B CD    1 
ATOM   877  N NE    . ARG   A 1 140 ? 10.33   -37.548 54.154 1   61.31 ? 121 ARG   B NE    1 
ATOM   878  C CZ    . ARG   A 1 140 ? 10.746  -38.792 53.919 1   69.54 ? 121 ARG   B CZ    1 
ATOM   879  N NH1   . ARG   A 1 140 ? 10.637  -39.32  52.704 1   56.32 ? 121 ARG   B NH1   1 
ATOM   880  N NH2   . ARG   A 1 140 ? 11.29   -39.51  54.895 1   57.89 ? 121 ARG   B NH2   1 
ATOM   881  N N     . VAL   A 1 141 ? 9.792   -31.577 50.841 1   45.79 ? 122 VAL   B N     1 
ATOM   882  C CA    . VAL   A 1 141 ? 8.992   -30.462 50.314 1   45.43 ? 122 VAL   B CA    1 
ATOM   883  C C     . VAL   A 1 141 ? 9.735   -29.114 50.468 1   47.69 ? 122 VAL   B C     1 
ATOM   884  O O     . VAL   A 1 141 ? 10.713  -29.03  51.217 1   46.27 ? 122 VAL   B O     1 
ATOM   885  C CB    . VAL   A 1 141 ? 7.554   -30.406 50.938 1   46.39 ? 122 VAL   B CB    1 
ATOM   886  C CG1   . VAL   A 1 141 ? 6.829   -31.746 50.811 1   47.23 ? 122 VAL   B CG1   1 
ATOM   887  C CG2   . VAL   A 1 141 ? 7.574   -29.935 52.395 1   42.87 ? 122 VAL   B CG2   1 
ATOM   888  N N     . LYS   A 1 142 ? 9.243   -28.064 49.78  1   45.08 ? 123 LYS   B N     1 
ATOM   889  C CA    . LYS   A 1 142 ? 9.769   -26.701 49.87  1   44.26 ? 123 LYS   B CA    1 
ATOM   890  C C     . LYS   A 1 142 ? 8.797   -25.849 50.708 1   45.29 ? 123 LYS   B C     1 
ATOM   891  O O     . LYS   A 1 142 ? 7.676   -26.292 50.976 1   44.27 ? 123 LYS   B O     1 
ATOM   892  C CB    . LYS   A 1 142 ? 9.975   -26.094 48.47  1   48.78 ? 123 LYS   B CB    1 
ATOM   893  C CG    . LYS   A 1 142 ? 11.277  -26.53  47.805 1   61.6  ? 123 LYS   B CG    1 
ATOM   894  C CD    . LYS   A 1 142 ? 11.54   -25.747 46.523 1   70.72 ? 123 LYS   B CD    1 
ATOM   895  C CE    . LYS   A 1 142 ? 12.778  -26.212 45.79  1   82.93 ? 123 LYS   B CE    1 
ATOM   896  N NZ    . LYS   A 1 142 ? 14.035  -25.822 46.49  1   90.7  ? 123 LYS   B NZ    1 
ATOM   897  N N     . GLY   A 1 143 ? 9.246   -24.655 51.109 1   41.64 ? 124 GLY   B N     1 
ATOM   898  C CA    . GLY   A 1 143 ? 8.512   -23.688 51.927 1   38.9  ? 124 GLY   B CA    1 
ATOM   899  C C     . GLY   A 1 143 ? 7.036   -23.467 51.628 1   41.29 ? 124 GLY   B C     1 
ATOM   900  O O     . GLY   A 1 143 ? 6.214   -23.646 52.538 1   38.79 ? 124 GLY   B O     1 
ATOM   901  N N     . PRO   A 1 144 ? 6.647   -23.07  50.377 1   39.98 ? 125 PRO   B N     1 
ATOM   902  C CA    . PRO   A 1 144 ? 5.214   -22.835 50.088 1   39.08 ? 125 PRO   B CA    1 
ATOM   903  C C     . PRO   A 1 144 ? 4.317   -24.066 50.265 1   40.71 ? 125 PRO   B C     1 
ATOM   904  O O     . PRO   A 1 144 ? 3.176   -23.915 50.71  1   38.57 ? 125 PRO   B O     1 
ATOM   905  C CB    . PRO   A 1 144 ? 5.213   -22.335 48.632 1   42.56 ? 125 PRO   B CB    1 
ATOM   906  C CG    . PRO   A 1 144 ? 6.612   -21.895 48.363 1   48.02 ? 125 PRO   B CG    1 
ATOM   907  C CD    . PRO   A 1 144 ? 7.478   -22.796 49.184 1   43.55 ? 125 PRO   B CD    1 
ATOM   908  N N     . GLU   A 1 145 ? 4.836   -25.279 49.934 1   38.32 ? 126 GLU   B N     1 
ATOM   909  C CA    . GLU   A 1 145 ? 4.119   -26.552 50.082 1   38.24 ? 126 GLU   B CA    1 
ATOM   910  C C     . GLU   A 1 145 ? 3.852   -26.848 51.571 1   38.44 ? 126 GLU   B C     1 
ATOM   911  O O     . GLU   A 1 145 ? 2.738   -27.248 51.927 1   38.02 ? 126 GLU   B O     1 
ATOM   912  C CB    . GLU   A 1 145 ? 4.92    -27.696 49.453 1   41.71 ? 126 GLU   B CB    1 
ATOM   913  C CG    . GLU   A 1 145 ? 4.066   -28.893 49.074 1   52.83 ? 126 GLU   B CG    1 
ATOM   914  C CD    . GLU   A 1 145 ? 4.782   -30.04  48.386 1   73.04 ? 126 GLU   B CD    1 
ATOM   915  O OE1   . GLU   A 1 145 ? 5.73    -29.786 47.607 1   63.41 ? 126 GLU   B OE1   1 
ATOM   916  O OE2   . GLU   A 1 145 ? 4.381   -31.203 48.622 1   67.19 ? 126 GLU   B OE2   1 
ATOM   917  N N     . LYS   A 1 146 ? 4.878   -26.644 52.429 1   33.31 ? 127 LYS   B N     1 
ATOM   918  C CA    . LYS   A 1 146 ? 4.809   -26.843 53.876 1   30.38 ? 127 LYS   B CA    1 
ATOM   919  C C     . LYS   A 1 146 ? 3.719   -25.937 54.473 1   30    ? 127 LYS   B C     1 
ATOM   920  O O     . LYS   A 1 146 ? 2.845   -26.425 55.196 1   29.1  ? 127 LYS   B O     1 
ATOM   921  C CB    . LYS   A 1 146 ? 6.187   -26.552 54.516 1   30.95 ? 127 LYS   B CB    1 
ATOM   922  C CG    . LYS   A 1 146 ? 6.193   -26.499 56.057 1   29.32 ? 127 LYS   B CG    1 
ATOM   923  C CD    . LYS   A 1 146 ? 6.762   -27.762 56.683 1   33.23 ? 127 LYS   B CD    1 
ATOM   924  C CE    . LYS   A 1 146 ? 5.701   -28.812 56.901 1   35.08 ? 127 LYS   B CE    1 
ATOM   925  N NZ    . LYS   A 1 146 ? 6.219   -29.971 57.665 1   31.55 ? 127 LYS   B NZ    1 
ATOM   926  N N     . GLU   A 1 147 ? 3.763   -24.63  54.134 1   25.93 ? 128 GLU   B N     1 
ATOM   927  C CA    . GLU   A 1 147 ? 2.802   -23.627 54.592 1   23.84 ? 128 GLU   B CA    1 
ATOM   928  C C     . GLU   A 1 147 ? 1.379   -23.98  54.184 1   26.92 ? 128 GLU   B C     1 
ATOM   929  O O     . GLU   A 1 147 ? 0.468   -23.876 55.014 1   24.42 ? 128 GLU   B O     1 
ATOM   930  C CB    . GLU   A 1 147 ? 3.166   -22.236 54.061 1   24.35 ? 128 GLU   B CB    1 
ATOM   931  C CG    . GLU   A 1 147 ? 4.427   -21.65  54.674 1   29.13 ? 128 GLU   B CG    1 
ATOM   932  C CD    . GLU   A 1 147 ? 4.629   -20.16  54.467 1   45.84 ? 128 GLU   B CD    1 
ATOM   933  O OE1   . GLU   A 1 147 ? 3.714   -19.495 53.928 1   32.83 ? 128 GLU   B OE1   1 
ATOM   934  O OE2   . GLU   A 1 147 ? 5.704   -19.651 54.859 1   46.3  ? 128 GLU   B OE2   1 
ATOM   935  N N     . GLU   A 1 148 ? 1.184   -24.42  52.916 1   26.54 ? 129 GLU   B N     1 
ATOM   936  C CA    . GLU   A 1 148 ? -0.148  -24.802 52.433 1   27.24 ? 129 GLU   B CA    1 
ATOM   937  C C     . GLU   A 1 148 ? -0.713  -25.994 53.213 1   28.78 ? 129 GLU   B C     1 
ATOM   938  O O     . GLU   A 1 148 ? -1.9    -25.976 53.565 1   28.33 ? 129 GLU   B O     1 
ATOM   939  C CB    . GLU   A 1 148 ? -0.171  -25.04  50.905 1   30.35 ? 129 GLU   B CB    1 
ATOM   940  C CG    . GLU   A 1 148 ? -1.565  -25.236 50.311 1   39.02 ? 129 GLU   B CG    1 
ATOM   941  C CD    . GLU   A 1 148 ? -2.655  -24.222 50.633 1   65.01 ? 129 GLU   B CD    1 
ATOM   942  O OE1   . GLU   A 1 148 ? -2.342  -23.025 50.835 1   52.19 ? 129 GLU   B OE1   1 
ATOM   943  O OE2   . GLU   A 1 148 ? -3.838  -24.632 50.669 1   66.49 ? 129 GLU   B OE2   1 
ATOM   944  N N     . LYS   A 1 149 ? 0.141   -26.991 53.532 1   25.58 ? 130 LYS   B N     1 
ATOM   945  C CA    . LYS   A 1 149 ? -0.281  -28.144 54.327 1   24.73 ? 130 LYS   B CA    1 
ATOM   946  C C     . LYS   A 1 149 ? -0.757  -27.697 55.729 1   25.03 ? 130 LYS   B C     1 
ATOM   947  O O     . LYS   A 1 149 ? -1.795  -28.178 56.197 1   24.76 ? 130 LYS   B O     1 
ATOM   948  C CB    . LYS   A 1 149 ? 0.81    -29.218 54.419 1   27.79 ? 130 LYS   B CB    1 
ATOM   949  C CG    . LYS   A 1 149 ? 0.222   -30.56  54.859 1   35.17 ? 130 LYS   B CG    1 
ATOM   950  C CD    . LYS   A 1 149 ? 1.084   -31.75  54.525 1   37.97 ? 130 LYS   B CD    1 
ATOM   951  C CE    . LYS   A 1 149 ? 0.341   -33.025 54.846 1   44.76 ? 130 LYS   B CE    1 
ATOM   952  N NZ    . LYS   A 1 149 ? 1.175   -34.233 54.604 1   57.88 ? 130 LYS   B NZ    1 
ATOM   953  N N     . LEU   A 1 150 ? -0.04   -26.745 56.365 1   18.97 ? 131 LEU   B N     1 
ATOM   954  C CA    . LEU   A 1 150 ? -0.452  -26.228 57.684 1   16.62 ? 131 LEU   B CA    1 
ATOM   955  C C     . LEU   A 1 150 ? -1.785  -25.478 57.598 1   19.79 ? 131 LEU   B C     1 
ATOM   956  O O     . LEU   A 1 150 ? -2.705  -25.787 58.364 1   18.86 ? 131 LEU   B O     1 
ATOM   957  C CB    . LEU   A 1 150 ? 0.639   -25.36  58.359 1   14.93 ? 131 LEU   B CB    1 
ATOM   958  C CG    . LEU   A 1 150 ? 0.293   -24.78  59.747 1   15.42 ? 131 LEU   B CG    1 
ATOM   959  C CD1   . LEU   A 1 150 ? -0.199  -25.882 60.714 1   15.07 ? 131 LEU   B CD1   1 
ATOM   960  C CD2   . LEU   A 1 150 ? 1.47    -24.025 60.334 1   14.76 ? 131 LEU   B CD2   1 
ATOM   961  N N     . ARG   A 1 151 ? -1.899  -24.535 56.637 1   18.25 ? 132 ARG   B N     1 
ATOM   962  C CA    . ARG   A 1 151 ? -3.128  -23.764 56.418 1   17.73 ? 132 ARG   B CA    1 
ATOM   963  C C     . ARG   A 1 151 ? -4.344  -24.66  56.167 1   22.88 ? 132 ARG   B C     1 
ATOM   964  O O     . ARG   A 1 151 ? -5.429  -24.352 56.664 1   22.21 ? 132 ARG   B O     1 
ATOM   965  C CB    . ARG   A 1 151 ? -2.948  -22.733 55.295 1   18.12 ? 132 ARG   B CB    1 
ATOM   966  C CG    . ARG   A 1 151 ? -2.014  -21.597 55.677 1   20.97 ? 132 ARG   B CG    1 
ATOM   967  C CD    . ARG   A 1 151 ? -1.901  -20.573 54.569 1   23.6  ? 132 ARG   B CD    1 
ATOM   968  N NE    . ARG   A 1 151 ? -1.174  -19.393 55.033 1   23.25 ? 132 ARG   B NE    1 
ATOM   969  C CZ    . ARG   A 1 151 ? 0.031   -19.03  54.604 1   31.25 ? 132 ARG   B CZ    1 
ATOM   970  N NH1   . ARG   A 1 151 ? 0.65    -19.736 53.663 1   24.05 ? 132 ARG   B NH1   1 
ATOM   971  N NH2   . ARG   A 1 151 ? 0.621   -17.953 55.103 1   18.75 ? 132 ARG   B NH2   1 
ATOM   972  N N     . GLN   A 1 152 ? -4.157  -25.79  55.45  1   21.97 ? 133 GLN   B N     1 
ATOM   973  C CA    . GLN   A 1 152 ? -5.243  -26.742 55.189 1   23.27 ? 133 GLN   B CA    1 
ATOM   974  C C     . GLN   A 1 152 ? -5.629  -27.537 56.446 1   26.09 ? 133 GLN   B C     1 
ATOM   975  O O     . GLN   A 1 152 ? -6.811  -27.861 56.623 1   26.49 ? 133 GLN   B O     1 
ATOM   976  C CB    . GLN   A 1 152 ? -4.889  -27.7   54.034 1   26.39 ? 133 GLN   B CB    1 
ATOM   977  C CG    . GLN   A 1 152 ? -5.01   -27.071 52.642 1   44.19 ? 133 GLN   B CG    1 
ATOM   978  C CD    . GLN   A 1 152 ? -6.393  -26.528 52.337 1   68.58 ? 133 GLN   B CD    1 
ATOM   979  O OE1   . GLN   A 1 152 ? -7.406  -27.233 52.429 1   65.05 ? 133 GLN   B OE1   1 
ATOM   980  N NE2   . GLN   A 1 152 ? -6.462  -25.254 51.968 1   61.74 ? 133 GLN   B NE2   1 
ATOM   981  N N     . ALA   A 1 153 ? -4.636  -27.846 57.315 1   21.34 ? 134 ALA   B N     1 
ATOM   982  C CA    . ALA   A 1 153 ? -4.862  -28.61  58.546 1   19.58 ? 134 ALA   B CA    1 
ATOM   983  C C     . ALA   A 1 153 ? -5.644  -27.821 59.598 1   20.67 ? 134 ALA   B C     1 
ATOM   984  O O     . ALA   A 1 153 ? -6.505  -28.402 60.274 1   18.4  ? 134 ALA   B O     1 
ATOM   985  C CB    . ALA   A 1 153 ? -3.537  -29.081 59.129 1   19.61 ? 134 ALA   B CB    1 
ATOM   986  N N     . VAL   A 1 154 ? -5.358  -26.506 59.735 1   17.94 ? 135 VAL   B N     1 
ATOM   987  C CA    . VAL   A 1 154 ? -6.013  -25.674 60.751 1   17.28 ? 135 VAL   B CA    1 
ATOM   988  C C     . VAL   A 1 154 ? -7.462  -25.362 60.357 1   23.24 ? 135 VAL   B C     1 
ATOM   989  O O     . VAL   A 1 154 ? -7.726  -24.513 59.49  1   22.78 ? 135 VAL   B O     1 
ATOM   990  C CB    . VAL   A 1 154 ? -5.21   -24.41  61.157 1   19.74 ? 135 VAL   B CB    1 
ATOM   991  C CG1   . VAL   A 1 154 ? -5.885  -23.693 62.327 1   17.86 ? 135 VAL   B CG1   1 
ATOM   992  C CG2   . VAL   A 1 154 ? -3.767  -24.77  61.515 1   19.47 ? 135 VAL   B CG2   1 
ATOM   993  N N     . LYS   A 1 155 ? -8.395  -26.053 61.033 1   21.16 ? 136 LYS   B N     1 
ATOM   994  C CA    . LYS   A 1 155 ? -9.83   -25.94  60.772 1   21.63 ? 136 LYS   B CA    1 
ATOM   995  C C     . LYS   A 1 155 ? -10.558 -24.96  61.671 1   23.53 ? 136 LYS   B C     1 
ATOM   996  O O     . LYS   A 1 155 ? -11.521 -24.325 61.217 1   25.71 ? 136 LYS   B O     1 
ATOM   997  C CB    . LYS   A 1 155 ? -10.504 -27.324 60.832 1   24.89 ? 136 LYS   B CB    1 
ATOM   998  C CG    . LYS   A 1 155 ? -9.866  -28.402 59.939 1   37.68 ? 136 LYS   B CG    1 
ATOM   999  C CD    . LYS   A 1 155 ? -9.839  -28.067 58.436 1   48.56 ? 136 LYS   B CD    1 
ATOM   1000 C CE    . LYS   A 1 155 ? -9.759  -29.3   57.559 1   56.32 ? 136 LYS   B CE    1 
ATOM   1001 N NZ    . LYS   A 1 155 ? -8.49   -30.058 57.744 1   60.23 ? 136 LYS   B NZ    1 
ATOM   1002 N N     . GLN   A 1 156 ? -10.142 -24.85  62.952 1   16.16 ? 137 GLN   B N     1 
ATOM   1003 C CA    . GLN   A 1 156 ? -10.814 -23.963 63.905 1   13.97 ? 137 GLN   B CA    1 
ATOM   1004 C C     . GLN   A 1 156 ? -9.818  -23.165 64.741 1   14.86 ? 137 GLN   B C     1 
ATOM   1005 O O     . GLN   A 1 156 ? -8.738  -23.661 65.066 1   13.99 ? 137 GLN   B O     1 
ATOM   1006 C CB    . GLN   A 1 156 ? -11.764 -24.755 64.826 1   14.83 ? 137 GLN   B CB    1 
ATOM   1007 C CG    . GLN   A 1 156 ? -12.963 -25.397 64.115 1   24.29 ? 137 GLN   B CG    1 
ATOM   1008 C CD    . GLN   A 1 156 ? -13.88  -26.125 65.061 1   49.6  ? 137 GLN   B CD    1 
ATOM   1009 O OE1   . GLN   A 1 156 ? -14.615 -25.521 65.847 1   51.81 ? 137 GLN   B OE1   1 
ATOM   1010 N NE2   . GLN   A 1 156 ? -13.87  -27.441 64.996 1   39.78 ? 137 GLN   B NE2   1 
ATOM   1011 N N     . VAL   A 1 157 ? -10.189 -21.913 65.068 1   13.81 ? 138 VAL   B N     1 
ATOM   1012 C CA    . VAL   A 1 157 ? -9.395  -20.986 65.879 1   13.38 ? 138 VAL   B CA    1 
ATOM   1013 C C     . VAL   A 1 157 ? -10.322 -20.64  67.04  1   11.26 ? 138 VAL   B C     1 
ATOM   1014 O O     . VAL   A 1 157 ? -11.354 -19.986 66.825 1   11.86 ? 138 VAL   B O     1 
ATOM   1015 C CB    . VAL   A 1 157 ? -8.939  -19.738 65.067 1   13.53 ? 138 VAL   B CB    1 
ATOM   1016 C CG1   . VAL   A 1 157 ? -8.084  -18.819 65.923 1   13.23 ? 138 VAL   B CG1   1 
ATOM   1017 C CG2   . VAL   A 1 157 ? -8.171  -20.139 63.813 1   14.17 ? 138 VAL   B CG2   1 
ATOM   1018 N N     . LEU   A 1 158 ? -10.006 -21.14  68.25  1   11.8  ? 139 LEU   B N     1 
ATOM   1019 C CA    . LEU   A 1 158 ? -10.906 -21.004 69.393 1   11.95 ? 139 LEU   B CA    1 
ATOM   1020 C C     . LEU   A 1 158 ? -10.354 -20.325 70.643 1   8.63  ? 139 LEU   B C     1 
ATOM   1021 O O     . LEU   A 1 158 ? -9.152  -20.374 70.925 1   9.03  ? 139 LEU   B O     1 
ATOM   1022 C CB    . LEU   A 1 158 ? -11.436 -22.399 69.801 1   11.65 ? 139 LEU   B CB    1 
ATOM   1023 C CG    . LEU   A 1 158 ? -12.138 -23.278 68.754 1   9.39  ? 139 LEU   B CG    1 
ATOM   1024 C CD1   . LEU   A 1 158 ? -12.436 -24.651 69.347 1   10.1  ? 139 LEU   B CD1   1 
ATOM   1025 C CD2   . LEU   A 1 158 ? -13.439 -22.638 68.254 1   10.09 ? 139 LEU   B CD2   1 
ATOM   1026 N N     . LYS   A 1 159 ? -11.268 -19.763 71.439 1   4.82  ? 140 LYS   B N     1 
ATOM   1027 C CA    . LYS   A 1 159 ? -10.96  -19.172 72.729 1   4.21  ? 140 LYS   B CA    1 
ATOM   1028 C C     . LYS   A 1 159 ? -10.811 -20.348 73.728 1   7.44  ? 140 LYS   B C     1 
ATOM   1029 O O     . LYS   A 1 159 ? -11.581 -21.324 73.671 1   5.19  ? 140 LYS   B O     1 
ATOM   1030 C CB    . LYS   A 1 159 ? -12.102 -18.241 73.169 1   8.03  ? 140 LYS   B CB    1 
ATOM   1031 C CG    . LYS   A 1 159 ? -11.836 -17.455 74.451 1   14.37 ? 140 LYS   B CG    1 
ATOM   1032 C CD    . LYS   A 1 159 ? -11.4   -16.013 74.141 1   30.32 ? 140 LYS   B CD    1 
ATOM   1033 C CE    . LYS   A 1 159 ? -11.762 -15.048 75.247 1   44.81 ? 140 LYS   B CE    1 
ATOM   1034 N NZ    . LYS   A 1 159 ? -10.974 -15.299 76.486 1   52.77 ? 140 LYS   B NZ    1 
ATOM   1035 N N     A CYS   A 1 160 ? -9.841  -20.245 74.636 0.5 3.91  ? 141 CYS   B N     1 
ATOM   1036 N N     B CYS   A 1 160 ? -9.8    -20.274 74.614 0.5 6.26  ? 141 CYS   B N     1 
ATOM   1037 C CA    A CYS   A 1 160 ? -9.647  -21.267 75.66  0.5 3     ? 141 CYS   B CA    1 
ATOM   1038 C CA    B CYS   A 1 160 ? -9.52   -21.317 75.614 0.5 6.59  ? 141 CYS   B CA    1 
ATOM   1039 C C     A CYS   A 1 160 ? -9.19   -20.662 76.973 0.5 6.41  ? 141 CYS   B C     1 
ATOM   1040 C C     B CYS   A 1 160 ? -9.071  -20.722 76.948 0.5 7.07  ? 141 CYS   B C     1 
ATOM   1041 O O     A CYS   A 1 160 ? -8.616  -19.57  76.99  0.5 5.62  ? 141 CYS   B O     1 
ATOM   1042 O O     B CYS   A 1 160 ? -8.405  -19.683 76.96  0.5 7.22  ? 141 CYS   B O     1 
ATOM   1043 C CB    A CYS   A 1 160 ? -8.698  -22.361 75.185 0.5 3     ? 141 CYS   B CB    1 
ATOM   1044 C CB    B CYS   A 1 160 ? -8.5    -22.318 75.069 0.5 8.16  ? 141 CYS   B CB    1 
ATOM   1045 S SG    A CYS   A 1 160 ? -6.948  -21.904 75.257 0.5 4.58  ? 141 CYS   B SG    1 
ATOM   1046 S SG    B CYS   A 1 160 ? -7.682  -23.347 76.325 0.5 6.05  ? 141 CYS   B SG    1 
ATOM   1047 N N     . ASP   A 1 161 ? -9.432  -21.381 78.067 1   3     ? 142 ASP   B N     1 
ATOM   1048 C CA    . ASP   A 1 161 ? -9.017  -20.981 79.407 1   3     ? 142 ASP   B CA    1 
ATOM   1049 C C     . ASP   A 1 161 ? -8.668  -22.278 80.127 1   5.89  ? 142 ASP   B C     1 
ATOM   1050 O O     . ASP   A 1 161 ? -9.562  -23.006 80.545 1   3.71  ? 142 ASP   B O     1 
ATOM   1051 C CB    . ASP   A 1 161 ? -10.09  -20.181 80.162 1   3.59  ? 142 ASP   B CB    1 
ATOM   1052 C CG    . ASP   A 1 161 ? -9.622  -19.68  81.527 1   5.96  ? 142 ASP   B CG    1 
ATOM   1053 O OD1   . ASP   A 1 161 ? -8.499  -20.07  81.968 1   4.18  ? 142 ASP   B OD1   1 
ATOM   1054 O OD2   . ASP   A 1 161 ? -10.354 -18.887 82.145 1   3     ? 142 ASP   B OD2   1 
ATOM   1055 N N     . VAL   A 1 162 ? -7.36   -22.572 80.252 1   3     ? 143 VAL   B N     1 
ATOM   1056 C CA    . VAL   A 1 162 ? -6.89   -23.824 80.879 1   3     ? 143 VAL   B CA    1 
ATOM   1057 C C     . VAL   A 1 162 ? -7.304  -23.973 82.353 1   5.06  ? 143 VAL   B C     1 
ATOM   1058 O O     . VAL   A 1 162 ? -7.262  -25.092 82.892 1   3     ? 143 VAL   B O     1 
ATOM   1059 C CB    . VAL   A 1 162 ? -5.352  -24.02  80.709 1   4.16  ? 143 VAL   B CB    1 
ATOM   1060 C CG1   . VAL   A 1 162 ? -4.946  -23.874 79.255 1   3     ? 143 VAL   B CG1   1 
ATOM   1061 C CG2   . VAL   A 1 162 ? -4.57   -23.044 81.565 1   3.58  ? 143 VAL   B CG2   1 
ATOM   1062 N N     . THR   A 1 163 ? -7.646  -22.845 83.021 1   3     ? 144 THR   B N     1 
ATOM   1063 C CA    . THR   A 1 163 ? -8.044  -22.894 84.431 1   3     ? 144 THR   B CA    1 
ATOM   1064 C C     . THR   A 1 163 ? -9.496  -23.367 84.595 1   4.57  ? 144 THR   B C     1 
ATOM   1065 O O     . THR   A 1 163 ? -9.922  -23.586 85.722 1   3     ? 144 THR   B O     1 
ATOM   1066 C CB    . THR   A 1 163 ? -7.838  -21.532 85.118 1   5.18  ? 144 THR   B CB    1 
ATOM   1067 O OG1   . THR   A 1 163 ? -8.728  -20.578 84.546 1   4.63  ? 144 THR   B OG1   1 
ATOM   1068 C CG2   . THR   A 1 163 ? -6.429  -21.039 85.018 1   4.58  ? 144 THR   B CG2   1 
ATOM   1069 N N     . GLN   A 1 164 ? -10.247 -23.497 83.489 1   3     ? 145 GLN   B N     1 
ATOM   1070 C CA    . GLN   A 1 164 ? -11.658 -23.887 83.547 1   3     ? 145 GLN   B CA    1 
ATOM   1071 C C     . GLN   A 1 164 ? -11.838 -25.388 83.331 1   6.55  ? 145 GLN   B C     1 
ATOM   1072 O O     . GLN   A 1 164 ? -11.136 -25.957 82.488 1   3.5   ? 145 GLN   B O     1 
ATOM   1073 C CB    . GLN   A 1 164 ? -12.492 -23.086 82.528 1   3.75  ? 145 GLN   B CB    1 
ATOM   1074 C CG    . GLN   A 1 164 ? -12.514 -21.553 82.76  1   11.52 ? 145 GLN   B CG    1 
ATOM   1075 C CD    . GLN   A 1 164 ? -12.741 -21.111 84.198 1   22.93 ? 145 GLN   B CD    1 
ATOM   1076 O OE1   . GLN   A 1 164 ? -12.033 -20.257 84.723 1   23.69 ? 145 GLN   B OE1   1 
ATOM   1077 N NE2   . GLN   A 1 164 ? -13.712 -21.676 84.878 1   19.28 ? 145 GLN   B NE2   1 
ATOM   1078 N N     . SER   A 1 165 ? -12.839 -26.02  84.03  1   4.45  ? 146 SER   B N     1 
ATOM   1079 C CA    . SER   A 1 165 ? -13.127 -27.461 83.866 1   4.88  ? 146 SER   B CA    1 
ATOM   1080 C C     . SER   A 1 165 ? -13.402 -27.818 82.399 1   7.82  ? 146 SER   B C     1 
ATOM   1081 O O     . SER   A 1 165 ? -13.085 -28.929 81.967 1   5.64  ? 146 SER   B O     1 
ATOM   1082 C CB    . SER   A 1 165 ? -14.291 -27.896 84.754 1   10.2  ? 146 SER   B CB    1 
ATOM   1083 O OG    . SER   A 1 165 ? -13.944 -27.696 86.114 1   10.46 ? 146 SER   B OG    1 
ATOM   1084 N N     . GLN   A 1 166 ? -13.987 -26.866 81.643 1   4.99  ? 147 GLN   B N     1 
ATOM   1085 C CA    . GLN   A 1 166 ? -14.249 -26.979 80.208 1   4.79  ? 147 GLN   B CA    1 
ATOM   1086 C C     . GLN   A 1 166 ? -13.379 -25.878 79.588 1   6.15  ? 147 GLN   B C     1 
ATOM   1087 O O     . GLN   A 1 166 ? -13.828 -24.73  79.502 1   3.46  ? 147 GLN   B O     1 
ATOM   1088 C CB    . GLN   A 1 166 ? -15.739 -26.752 79.868 1   7.79  ? 147 GLN   B CB    1 
ATOM   1089 C CG    . GLN   A 1 166 ? -16.662 -27.915 80.24  1   17.82 ? 147 GLN   B CG    1 
ATOM   1090 C CD    . GLN   A 1 166 ? -17.046 -27.919 81.702 1   36.48 ? 147 GLN   B CD    1 
ATOM   1091 O OE1   . GLN   A 1 166 ? -16.737 -28.864 82.443 1   35.8  ? 147 GLN   B OE1   1 
ATOM   1092 N NE2   . GLN   A 1 166 ? -17.726 -26.863 82.151 1   27.42 ? 147 GLN   B NE2   1 
ATOM   1093 N N     . PRO   A 1 167 ? -12.098 -26.171 79.238 1   3     ? 148 PRO   B N     1 
ATOM   1094 C CA    . PRO   A 1 167 ? -11.231 -25.106 78.685 1   3     ? 148 PRO   B CA    1 
ATOM   1095 C C     . PRO   A 1 167 ? -11.793 -24.406 77.456 1   7.31  ? 148 PRO   B C     1 
ATOM   1096 O O     . PRO   A 1 167 ? -11.552 -23.217 77.282 1   7.35  ? 148 PRO   B O     1 
ATOM   1097 C CB    . PRO   A 1 167 ? -9.914  -25.832 78.357 1   4.32  ? 148 PRO   B CB    1 
ATOM   1098 C CG    . PRO   A 1 167 ? -9.908  -27.039 79.26  1   5.62  ? 148 PRO   B CG    1 
ATOM   1099 C CD    . PRO   A 1 167 ? -11.379 -27.459 79.333 1   4.2   ? 148 PRO   B CD    1 
ATOM   1100 N N     . LEU   A 1 168 ? -12.587 -25.119 76.638 1   6.71  ? 149 LEU   B N     1 
ATOM   1101 C CA    . LEU   A 1 168 ? -13.166 -24.539 75.42  1   7.74  ? 149 LEU   B CA    1 
ATOM   1102 C C     . LEU   A 1 168 ? -14.592 -23.974 75.616 1   10.59 ? 149 LEU   B C     1 
ATOM   1103 O O     . LEU   A 1 168 ? -15.282 -23.677 74.634 1   11.33 ? 149 LEU   B O     1 
ATOM   1104 C CB    . LEU   A 1 168 ? -13.107 -25.557 74.262 1   8.06  ? 149 LEU   B CB    1 
ATOM   1105 C CG    . LEU   A 1 168 ? -11.728 -26.195 73.996 1   9.3   ? 149 LEU   B CG    1 
ATOM   1106 C CD1   . LEU   A 1 168 ? -11.815 -27.181 72.867 1   10.35 ? 149 LEU   B CD1   1 
ATOM   1107 C CD2   . LEU   A 1 168 ? -10.683 -25.15  73.673 1   8.98  ? 149 LEU   B CD2   1 
ATOM   1108 N N     . GLY   A 1 169 ? -14.982 -23.768 76.877 1   11.85 ? 150 GLY   B N     1 
ATOM   1109 C CA    . GLY   A 1 169 ? -16.285 -23.218 77.241 1   12.92 ? 150 GLY   B CA    1 
ATOM   1110 C C     . GLY   A 1 169 ? -17.42  -24.091 76.741 1   15.05 ? 150 GLY   B C     1 
ATOM   1111 O O     . GLY   A 1 169 ? -17.425 -25.305 76.982 1   15.26 ? 150 GLY   B O     1 
ATOM   1112 N N     . ALA   A 1 170 ? -18.347 -23.487 75.992 1   15.85 ? 151 ALA   B N     1 
ATOM   1113 C CA    . ALA   A 1 170 ? -19.52  -24.168 75.434 1   18.32 ? 151 ALA   B CA    1 
ATOM   1114 C C     . ALA   A 1 170 ? -19.263 -24.792 74.044 1   20.08 ? 151 ALA   B C     1 
ATOM   1115 O O     . ALA   A 1 170 ? -20.156 -25.443 73.498 1   22.3  ? 151 ALA   B O     1 
ATOM   1116 C CB    . ALA   A 1 170 ? -20.698 -23.2   75.371 1   20.12 ? 151 ALA   B CB    1 
ATOM   1117 N N     . VAL   A 1 171 ? -18.047 -24.606 73.475 1   16.04 ? 152 VAL   B N     1 
ATOM   1118 C CA    . VAL   A 1 171 ? -17.712 -25.132 72.146 1   15.13 ? 152 VAL   B CA    1 
ATOM   1119 C C     . VAL   A 1 171 ? -17.484 -26.649 72.192 1   15.39 ? 152 VAL   B C     1 
ATOM   1120 O O     . VAL   A 1 171 ? -16.532 -27.103 72.836 1   14.84 ? 152 VAL   B O     1 
ATOM   1121 C CB    . VAL   A 1 171 ? -16.549 -24.375 71.446 1   14.24 ? 152 VAL   B CB    1 
ATOM   1122 C CG1   . VAL   A 1 171 ? -16.231 -24.99  70.077 1   14.32 ? 152 VAL   B CG1   1 
ATOM   1123 C CG2   . VAL   A 1 171 ? -16.859 -22.886 71.312 1   13.64 ? 152 VAL   B CG2   1 
ATOM   1124 N N     . PRO   A 1 172 ? -18.32  -27.447 71.487 1   14.36 ? 153 PRO   B N     1 
ATOM   1125 C CA    . PRO   A 1 172 ? -18.108 -28.903 71.507 1   15.26 ? 153 PRO   B CA    1 
ATOM   1126 C C     . PRO   A 1 172 ? -17.067 -29.335 70.476 1   15.02 ? 153 PRO   B C     1 
ATOM   1127 O O     . PRO   A 1 172 ? -17.017 -28.795 69.365 1   14.11 ? 153 PRO   B O     1 
ATOM   1128 C CB    . PRO   A 1 172 ? -19.498 -29.466 71.188 1   18.13 ? 153 PRO   B CB    1 
ATOM   1129 C CG    . PRO   A 1 172 ? -20.167 -28.408 70.362 1   19.92 ? 153 PRO   B CG    1 
ATOM   1130 C CD    . PRO   A 1 172 ? -19.494 -27.082 70.659 1   15.89 ? 153 PRO   B CD    1 
ATOM   1131 N N     . LEU   A 1 173 ? -16.229 -30.303 70.856 1   13.43 ? 154 LEU   B N     1 
ATOM   1132 C CA    . LEU   A 1 173 ? -15.203 -30.882 69.992 1   11.93 ? 154 LEU   B CA    1 
ATOM   1133 C C     . LEU   A 1 173 ? -15.107 -32.388 70.229 1   14.6  ? 154 LEU   B C     1 
ATOM   1134 O O     . LEU   A 1 173 ? -15.312 -32.839 71.362 1   14.38 ? 154 LEU   B O     1 
ATOM   1135 C CB    . LEU   A 1 173 ? -13.818 -30.249 70.263 1   9.85  ? 154 LEU   B CB    1 
ATOM   1136 C CG    . LEU   A 1 173 ? -13.415 -28.978 69.494 1   11.02 ? 154 LEU   B CG    1 
ATOM   1137 C CD1   . LEU   A 1 173 ? -11.932 -28.719 69.666 1   10.04 ? 154 LEU   B CD1   1 
ATOM   1138 C CD2   . LEU   A 1 173 ? -13.665 -29.102 67.994 1   11.79 ? 154 LEU   B CD2   1 
ATOM   1139 N N     . PRO   A 1 174 ? -14.758 -33.195 69.194 1   13.24 ? 155 PRO   B N     1 
ATOM   1140 C CA    . PRO   A 1 174 ? -14.549 -34.633 69.438 1   14.98 ? 155 PRO   B CA    1 
ATOM   1141 C C     . PRO   A 1 174 ? -13.329 -34.822 70.357 1   14.83 ? 155 PRO   B C     1 
ATOM   1142 O O     . PRO   A 1 174 ? -12.449 -33.954 70.318 1   12.72 ? 155 PRO   B O     1 
ATOM   1143 C CB    . PRO   A 1 174 ? -14.241 -35.195 68.035 1   16.82 ? 155 PRO   B CB    1 
ATOM   1144 C CG    . PRO   A 1 174 ? -14.639 -34.132 67.072 1   18.2  ? 155 PRO   B CG    1 
ATOM   1145 C CD    . PRO   A 1 174 ? -14.473 -32.837 67.789 1   14.33 ? 155 PRO   B CD    1 
ATOM   1146 N N     . PRO   A 1 175 ? -13.237 -35.898 71.191 1   14.13 ? 156 PRO   B N     1 
ATOM   1147 C CA    . PRO   A 1 175 ? -12.022 -36.08  72.01  1   13.02 ? 156 PRO   B CA    1 
ATOM   1148 C C     . PRO   A 1 175 ? -10.801 -36.158 71.091 1   12.09 ? 156 PRO   B C     1 
ATOM   1149 O O     . PRO   A 1 175 ? -10.838 -36.857 70.069 1   13.25 ? 156 PRO   B O     1 
ATOM   1150 C CB    . PRO   A 1 175 ? -12.269 -37.406 72.75  1   14    ? 156 PRO   B CB    1 
ATOM   1151 C CG    . PRO   A 1 175 ? -13.754 -37.63  72.669 1   18.18 ? 156 PRO   B CG    1 
ATOM   1152 C CD    . PRO   A 1 175 ? -14.173 -37.027 71.362 1   17.26 ? 156 PRO   B CD    1 
ATOM   1153 N N     . ALA   A 1 176 ? -9.749  -35.376 71.417 1   10.34 ? 157 ALA   B N     1 
ATOM   1154 C CA    . ALA   A 1 176 ? -8.538  -35.285 70.606 1   8.47  ? 157 ALA   B CA    1 
ATOM   1155 C C     . ALA   A 1 176 ? -7.617  -36.49  70.768 1   8.84  ? 157 ALA   B C     1 
ATOM   1156 O O     . ALA   A 1 176 ? -7.632  -37.158 71.81  1   6.81  ? 157 ALA   B O     1 
ATOM   1157 C CB    . ALA   A 1 176 ? -7.778  -34     70.934 1   7.85  ? 157 ALA   B CB    1 
ATOM   1158 N N     . ASP   A 1 177 ? -6.793  -36.737 69.738 1   5.47  ? 158 ASP   B N     1 
ATOM   1159 C CA    . ASP   A 1 177 ? -5.784  -37.798 69.753 1   5.47  ? 158 ASP   B CA    1 
ATOM   1160 C C     . ASP   A 1 177 ? -4.531  -37.259 70.479 1   7.17  ? 158 ASP   B C     1 
ATOM   1161 O O     . ASP   A 1 177 ? -3.756  -38.03  71.058 1   5.85  ? 158 ASP   B O     1 
ATOM   1162 C CB    . ASP   A 1 177 ? -5.434  -38.211 68.317 1   8.38  ? 158 ASP   B CB    1 
ATOM   1163 C CG    . ASP   A 1 177 ? -6.616  -38.838 67.585 1   15.25 ? 158 ASP   B CG    1 
ATOM   1164 O OD1   . ASP   A 1 177 ? -6.91   -40.031 67.842 1   18.94 ? 158 ASP   B OD1   1 
ATOM   1165 O OD2   . ASP   A 1 177 ? -7.264  -38.126 66.785 1   17.39 ? 158 ASP   B OD2   1 
ATOM   1166 N N     . CYS   A 1 178 ? -4.343  -35.924 70.433 1   3.04  ? 159 CYS   B N     1 
ATOM   1167 C CA    . CYS   A 1 178 ? -3.192  -35.271 71.062 1   3.07  ? 159 CYS   B CA    1 
ATOM   1168 C C     . CYS   A 1 178 ? -3.537  -33.861 71.515 1   5.59  ? 159 CYS   B C     1 
ATOM   1169 O O     . CYS   A 1 178 ? -4.262  -33.147 70.813 1   3     ? 159 CYS   B O     1 
ATOM   1170 C CB    . CYS   A 1 178 ? -1.992  -35.267 70.116 1   3.92  ? 159 CYS   B CB    1 
ATOM   1171 S SG    . CYS   A 1 178 ? -0.501  -34.467 70.79  1   6.89  ? 159 CYS   B SG    1 
ATOM   1172 N N     . VAL   A 1 179 ? -3.01   -33.465 72.686 1   3     ? 160 VAL   B N     1 
ATOM   1173 C CA    . VAL   A 1 179 ? -3.133  -32.095 73.202 1   3     ? 160 VAL   B CA    1 
ATOM   1174 C C     . VAL   A 1 179 ? -1.694  -31.582 73.319 1   4.56  ? 160 VAL   B C     1 
ATOM   1175 O O     . VAL   A 1 179 ? -0.869  -32.232 73.97  1   3     ? 160 VAL   B O     1 
ATOM   1176 C CB    . VAL   A 1 179 ? -3.934  -31.97  74.526 1   4.33  ? 160 VAL   B CB    1 
ATOM   1177 C CG1   . VAL   A 1 179 ? -3.65   -30.629 75.21  1   3     ? 160 VAL   B CG1   1 
ATOM   1178 C CG2   . VAL   A 1 179 ? -5.441  -32.117 74.26  1   3     ? 160 VAL   B CG2   1 
ATOM   1179 N N     . LEU   A 1 180 ? -1.387  -30.474 72.624 1   3     ? 161 LEU   B N     1 
ATOM   1180 C CA    . LEU   A 1 180 ? -0.045  -29.885 72.622 1   3     ? 161 LEU   B CA    1 
ATOM   1181 C C     . LEU   A 1 180 ? -0.075  -28.542 73.337 1   4.57  ? 161 LEU   B C     1 
ATOM   1182 O O     . LEU   A 1 180 ? -1.003  -27.773 73.123 1   3     ? 161 LEU   B O     1 
ATOM   1183 C CB    . LEU   A 1 180 ? 0.414   -29.705 71.163 1   3     ? 161 LEU   B CB    1 
ATOM   1184 C CG    . LEU   A 1 180 ? 1.678   -28.875 70.905 1   6.37  ? 161 LEU   B CG    1 
ATOM   1185 C CD1   . LEU   A 1 180 ? 2.938   -29.576 71.458 1   5.07  ? 161 LEU   B CD1   1 
ATOM   1186 C CD2   . LEU   A 1 180 ? 1.84    -28.557 69.414 1   6.89  ? 161 LEU   B CD2   1 
ATOM   1187 N N     . SER   A 1 181 ? 0.962   -28.219 74.136 1   3     ? 162 SER   B N     1 
ATOM   1188 C CA    . SER   A 1 181 ? 0.986   -26.903 74.787 1   3     ? 162 SER   B CA    1 
ATOM   1189 C C     . SER   A 1 181 ? 2.418   -26.441 74.975 1   5.64  ? 162 SER   B C     1 
ATOM   1190 O O     . SER   A 1 181 ? 3.159   -27.054 75.741 1   3     ? 162 SER   B O     1 
ATOM   1191 C CB    . SER   A 1 181 ? 0.225   -26.908 76.11  1   3.36  ? 162 SER   B CB    1 
ATOM   1192 O OG    . SER   A 1 181 ? 0.077   -25.577 76.58  1   8.07  ? 162 SER   B OG    1 
ATOM   1193 N N     . THR   A 1 182 ? 2.816   -25.385 74.235 1   3     ? 163 THR   B N     1 
ATOM   1194 C CA    . THR   A 1 182 ? 4.188   -24.883 74.324 1   3     ? 163 THR   B CA    1 
ATOM   1195 C C     . THR   A 1 182 ? 4.226   -23.523 75.026 1   5.04  ? 163 THR   B C     1 
ATOM   1196 O O     . THR   A 1 182 ? 3.514   -22.606 74.606 1   3     ? 163 THR   B O     1 
ATOM   1197 C CB    . THR   A 1 182 ? 4.855   -24.847 72.933 1   5.38  ? 163 THR   B CB    1 
ATOM   1198 O OG1   . THR   A 1 182 ? 4.109   -23.966 72.068 1   3     ? 163 THR   B OG1   1 
ATOM   1199 C CG2   . THR   A 1 182 ? 4.981   -26.264 72.284 1   3     ? 163 THR   B CG2   1 
ATOM   1200 N N     . LEU   A 1 183 ? 5.071   -23.392 76.071 1   3     ? 164 LEU   B N     1 
ATOM   1201 C CA    . LEU   A 1 183 ? 5.312   -22.132 76.808 1   3     ? 164 LEU   B CA    1 
ATOM   1202 C C     . LEU   A 1 183 ? 4.03    -21.404 77.287 1   5.91  ? 164 LEU   B C     1 
ATOM   1203 O O     . LEU   A 1 183 ? 4.011   -20.164 77.371 1   3     ? 164 LEU   B O     1 
ATOM   1204 C CB    . LEU   A 1 183 ? 6.19    -21.189 75.947 1   3     ? 164 LEU   B CB    1 
ATOM   1205 C CG    . LEU   A 1 183 ? 7.6     -21.685 75.654 1   5.49  ? 164 LEU   B CG    1 
ATOM   1206 C CD1   . LEU   A 1 183 ? 8.179   -20.983 74.425 1   6.53  ? 164 LEU   B CD1   1 
ATOM   1207 C CD2   . LEU   A 1 183 ? 8.495   -21.524 76.879 1   4.22  ? 164 LEU   B CD2   1 
ATOM   1208 N N     . CYS   A 1 184 ? 2.997   -22.187 77.671 1   3     ? 165 CYS   B N     1 
ATOM   1209 C CA    . CYS   A 1 184 ? 1.717   -21.626 78.126 1   3     ? 165 CYS   B CA    1 
ATOM   1210 C C     . CYS   A 1 184 ? 1.425   -21.829 79.605 1   5.74  ? 165 CYS   B C     1 
ATOM   1211 O O     . CYS   A 1 184 ? 1.101   -20.863 80.305 1   3     ? 165 CYS   B O     1 
ATOM   1212 C CB    . CYS   A 1 184 ? 0.57    -22.173 77.282 1   3     ? 165 CYS   B CB    1 
ATOM   1213 S SG    . CYS   A 1 184 ? -1.079  -21.846 77.977 1   4.46  ? 165 CYS   B SG    1 
ATOM   1214 N N     . LEU   A 1 185 ? 1.409   -23.104 80.052 1   3     ? 166 LEU   B N     1 
ATOM   1215 C CA    . LEU   A 1 185 ? 0.987   -23.463 81.398 1   3     ? 166 LEU   B CA    1 
ATOM   1216 C C     . LEU   A 1 185 ? 1.721   -22.713 82.518 1   4.53  ? 166 LEU   B C     1 
ATOM   1217 O O     . LEU   A 1 185 ? 1.052   -22.275 83.448 1   3     ? 166 LEU   B O     1 
ATOM   1218 C CB    . LEU   A 1 185 ? 1.025   -24.986 81.624 1   3     ? 166 LEU   B CB    1 
ATOM   1219 C CG    . LEU   A 1 185 ? 0.125   -25.815 80.694 1   4.91  ? 166 LEU   B CG    1 
ATOM   1220 C CD1   . LEU   A 1 185 ? 0.247   -27.307 80.995 1   3.76  ? 166 LEU   B CD1   1 
ATOM   1221 C CD2   . LEU   A 1 185 ? -1.362  -25.412 80.823 1   3     ? 166 LEU   B CD2   1 
ATOM   1222 N N     . ASP   A 1 186 ? 3.054   -22.523 82.426 1   3     ? 167 ASP   B N     1 
ATOM   1223 C CA    . ASP   A 1 186 ? 3.803   -21.766 83.453 1   3     ? 167 ASP   B CA    1 
ATOM   1224 C C     . ASP   A 1 186 ? 3.235   -20.34  83.594 1   5.35  ? 167 ASP   B C     1 
ATOM   1225 O O     . ASP   A 1 186 ? 3.198   -19.793 84.694 1   3     ? 167 ASP   B O     1 
ATOM   1226 C CB    . ASP   A 1 186 ? 5.267   -21.591 83.038 1   4.38  ? 167 ASP   B CB    1 
ATOM   1227 C CG    . ASP   A 1 186 ? 6.198   -22.768 83.205 1   5.95  ? 167 ASP   B CG    1 
ATOM   1228 O OD1   . ASP   A 1 186 ? 5.75    -23.822 83.738 1   7.2   ? 167 ASP   B OD1   1 
ATOM   1229 O OD2   . ASP   A 1 186 ? 7.371   -22.639 82.803 1   7.55  ? 167 ASP   B OD2   1 
ATOM   1230 N N     . ALA   A 1 187 ? 2.87    -19.73  82.461 1   3     ? 168 ALA   B N     1 
ATOM   1231 C CA    . ALA   A 1 187 ? 2.349   -18.362 82.406 1   3     ? 168 ALA   B CA    1 
ATOM   1232 C C     . ALA   A 1 187 ? 0.858   -18.282 82.805 1   6.19  ? 168 ALA   B C     1 
ATOM   1233 O O     . ALA   A 1 187 ? 0.409   -17.249 83.31  1   3     ? 168 ALA   B O     1 
ATOM   1234 C CB    . ALA   A 1 187 ? 2.53    -17.808 81     1   3.59  ? 168 ALA   B CB    1 
ATOM   1235 N N     . ALA   A 1 188 ? 0.098   -19.369 82.575 1   3     ? 169 ALA   B N     1 
ATOM   1236 C CA    . ALA   A 1 188 ? -1.34   -19.366 82.862 1   3     ? 169 ALA   B CA    1 
ATOM   1237 C C     . ALA   A 1 188 ? -1.727  -19.773 84.282 1   5.69  ? 169 ALA   B C     1 
ATOM   1238 O O     . ALA   A 1 188 ? -2.867  -19.515 84.683 1   3.1   ? 169 ALA   B O     1 
ATOM   1239 C CB    . ALA   A 1 188 ? -2.069  -20.242 81.855 1   3.04  ? 169 ALA   B CB    1 
ATOM   1240 N N     . CYS   A 1 189 ? -0.832  -20.457 85.02  1   3     ? 170 CYS   B N     1 
ATOM   1241 C CA    . CYS   A 1 189 ? -1.129  -21.003 86.341 1   3     ? 170 CYS   B CA    1 
ATOM   1242 C C     . CYS   A 1 189 ? -0.433  -20.265 87.482 1   5.54  ? 170 CYS   B C     1 
ATOM   1243 O O     . CYS   A 1 189 ? 0.799   -20.273 87.534 1   3     ? 170 CYS   B O     1 
ATOM   1244 C CB    . CYS   A 1 189 ? -0.834  -22.497 86.368 1   3     ? 170 CYS   B CB    1 
ATOM   1245 S SG    . CYS   A 1 189 ? -1.616  -23.414 85.01  1   3.63  ? 170 CYS   B SG    1 
ATOM   1246 N N     . PRO   A 1 190 ? -1.209  -19.634 88.412 1   3     ? 171 PRO   B N     1 
ATOM   1247 C CA    . PRO   A 1 190 ? -0.573  -18.859 89.501 1   3     ? 171 PRO   B CA    1 
ATOM   1248 C C     . PRO   A 1 190 ? 0.084   -19.679 90.603 1   6.78  ? 171 PRO   B C     1 
ATOM   1249 O O     . PRO   A 1 190 ? 0.898   -19.132 91.353 1   6.7   ? 171 PRO   B O     1 
ATOM   1250 C CB    . PRO   A 1 190 ? -1.717  -17.984 90.059 1   5.2   ? 171 PRO   B CB    1 
ATOM   1251 C CG    . PRO   A 1 190 ? -2.897  -18.194 89.152 1   4.67  ? 171 PRO   B CG    1 
ATOM   1252 C CD    . PRO   A 1 190 ? -2.68   -19.517 88.463 1   6.06  ? 171 PRO   B CD    1 
ATOM   1253 N N     . ASP   A 1 191 ? -0.274  -20.969 90.732 1   3     ? 172 ASP   B N     1 
ATOM   1254 C CA    . ASP   A 1 191 ? 0.291   -21.836 91.771 1   3     ? 172 ASP   B CA    1 
ATOM   1255 C C     . ASP   A 1 191 ? 0.284   -23.301 91.339 1   4.98  ? 172 ASP   B C     1 
ATOM   1256 O O     . ASP   A 1 191 ? -0.399  -23.651 90.373 1   3     ? 172 ASP   B O     1 
ATOM   1257 C CB    . ASP   A 1 191 ? -0.447  -21.645 93.124 1   5.43  ? 172 ASP   B CB    1 
ATOM   1258 C CG    . ASP   A 1 191 ? -1.965  -21.736 93.029 1   9.41  ? 172 ASP   B CG    1 
ATOM   1259 O OD1   . ASP   A 1 191 ? -2.468  -22.731 92.464 1   10.7  ? 172 ASP   B OD1   1 
ATOM   1260 O OD2   . ASP   A 1 191 ? -2.655  -20.797 93.512 1   17    ? 172 ASP   B OD2   1 
ATOM   1261 N N     . LEU   A 1 192 ? 1.017   -24.155 92.081 1   3     ? 173 LEU   B N     1 
ATOM   1262 C CA    . LEU   A 1 192 ? 1.119   -25.591 91.796 1   3.32  ? 173 LEU   B CA    1 
ATOM   1263 C C     . LEU   A 1 192 ? -0.265  -26.321 91.783 1   7.05  ? 173 LEU   B C     1 
ATOM   1264 O O     . LEU   A 1 192 ? -0.502  -27.083 90.839 1   4.22  ? 173 LEU   B O     1 
ATOM   1265 C CB    . LEU   A 1 192 ? 2.136   -26.276 92.725 1   3.57  ? 173 LEU   B CB    1 
ATOM   1266 C CG    . LEU   A 1 192 ? 2.601   -27.693 92.334 1   6.89  ? 173 LEU   B CG    1 
ATOM   1267 C CD1   . LEU   A 1 192 ? 2.986   -27.797 90.83  1   6.42  ? 173 LEU   B CD1   1 
ATOM   1268 C CD2   . LEU   A 1 192 ? 3.778   -28.15  93.214 1   6.93  ? 173 LEU   B CD2   1 
ATOM   1269 N N     . PRO   A 1 193 ? -1.221  -26.071 92.727 1   6.92  ? 174 PRO   B N     1 
ATOM   1270 C CA    . PRO   A 1 193 ? -2.542  -26.731 92.612 1   6.16  ? 174 PRO   B CA    1 
ATOM   1271 C C     . PRO   A 1 193 ? -3.29   -26.377 91.312 1   7.37  ? 174 PRO   B C     1 
ATOM   1272 O O     . PRO   A 1 193 ? -3.88   -27.269 90.689 1   6.3   ? 174 PRO   B O     1 
ATOM   1273 C CB    . PRO   A 1 193 ? -3.3    -26.237 93.852 1   7.65  ? 174 PRO   B CB    1 
ATOM   1274 C CG    . PRO   A 1 193 ? -2.234  -25.821 94.818 1   3.67  ? 174 PRO   B CG    1 
ATOM   1275 C CD    . PRO   A 1 193 ? -1.161  -25.227 93.941 1   6.91  ? 174 PRO   B CD    1 
ATOM   1276 N N     . THR   A 1 194 ? -3.248  -25.085 90.878 1   3     ? 175 THR   B N     1 
ATOM   1277 C CA    . THR   A 1 194 ? -3.9    -24.664 89.622 1   3     ? 175 THR   B CA    1 
ATOM   1278 C C     . THR   A 1 194 ? -3.217  -25.366 88.424 1   5.66  ? 175 THR   B C     1 
ATOM   1279 O O     . THR   A 1 194 ? -3.899  -25.775 87.486 1   3     ? 175 THR   B O     1 
ATOM   1280 C CB    . THR   A 1 194 ? -3.894  -23.132 89.469 1   4.95  ? 175 THR   B CB    1 
ATOM   1281 O OG1   . THR   A 1 194 ? -4.505  -22.533 90.616 1   3     ? 175 THR   B OG1   1 
ATOM   1282 C CG2   . THR   A 1 194 ? -4.639  -22.652 88.226 1   3     ? 175 THR   B CG2   1 
ATOM   1283 N N     . TYR   A 1 195 ? -1.88   -25.495 88.469 1   3     ? 176 TYR   B N     1 
ATOM   1284 C CA    . TYR   A 1 195 ? -1.11   -26.159 87.405 1   3     ? 176 TYR   B CA    1 
ATOM   1285 C C     . TYR   A 1 195 ? -1.587  -27.605 87.231 1   5.45  ? 176 TYR   B C     1 
ATOM   1286 O O     . TYR   A 1 195 ? -1.901  -28.026 86.108 1   3     ? 176 TYR   B O     1 
ATOM   1287 C CB    . TYR   A 1 195 ? 0.393   -26.119 87.737 1   3     ? 176 TYR   B CB    1 
ATOM   1288 C CG    . TYR   A 1 195 ? 1.273   -26.643 86.621 1   3     ? 176 TYR   B CG    1 
ATOM   1289 C CD1   . TYR   A 1 195 ? 1.681   -25.812 85.578 1   3.63  ? 176 TYR   B CD1   1 
ATOM   1290 C CD2   . TYR   A 1 195 ? 1.737   -27.955 86.63  1   3.05  ? 176 TYR   B CD2   1 
ATOM   1291 C CE1   . TYR   A 1 195 ? 2.512   -26.285 84.558 1   3     ? 176 TYR   B CE1   1 
ATOM   1292 C CE2   . TYR   A 1 195 ? 2.563   -28.439 85.619 1   3     ? 176 TYR   B CE2   1 
ATOM   1293 C CZ    . TYR   A 1 195 ? 2.947   -27.602 84.584 1   6.86  ? 176 TYR   B CZ    1 
ATOM   1294 O OH    . TYR   A 1 195 ? 3.762   -28.095 83.595 1   3     ? 176 TYR   B OH    1 
ATOM   1295 N N     . CYS   A 1 196 ? -1.682  -28.348 88.361 1   3     ? 177 CYS   B N     1 
ATOM   1296 C CA    . CYS   A 1 196 ? -2.178  -29.722 88.345 1   3     ? 177 CYS   B CA    1 
ATOM   1297 C C     . CYS   A 1 196 ? -3.622  -29.774 87.83  1   4.16  ? 177 CYS   B C     1 
ATOM   1298 O O     . CYS   A 1 196 ? -3.941  -30.61  86.987 1   3     ? 177 CYS   B O     1 
ATOM   1299 C CB    . CYS   A 1 196 ? -2.055  -30.368 89.719 1   3     ? 177 CYS   B CB    1 
ATOM   1300 S SG    . CYS   A 1 196 ? -2.564  -32.111 89.742 1   6.69  ? 177 CYS   B SG    1 
ATOM   1301 N N     . ARG   A 1 197 ? -4.479  -28.835 88.297 1   3     ? 178 ARG   B N     1 
ATOM   1302 C CA    . ARG   A 1 197 ? -5.872  -28.766 87.841 1   3.45  ? 178 ARG   B CA    1 
ATOM   1303 C C     . ARG   A 1 197 ? -5.926  -28.485 86.333 1   4.24  ? 178 ARG   B C     1 
ATOM   1304 O O     . ARG   A 1 197 ? -6.742  -29.075 85.637 1   3     ? 178 ARG   B O     1 
ATOM   1305 C CB    . ARG   A 1 197 ? -6.646  -27.661 88.588 1   6.94  ? 178 ARG   B CB    1 
ATOM   1306 C CG    . ARG   A 1 197 ? -7.113  -28.035 89.987 1   21.49 ? 178 ARG   B CG    1 
ATOM   1307 C CD    . ARG   A 1 197 ? -8.243  -27.128 90.485 1   43.61 ? 178 ARG   B CD    1 
ATOM   1308 N NE    . ARG   A 1 197 ? -7.986  -25.699 90.259 1   58.31 ? 178 ARG   B NE    1 
ATOM   1309 C CZ    . ARG   A 1 197 ? -7.28   -24.915 91.07  1   76.12 ? 178 ARG   B CZ    1 
ATOM   1310 N NH1   . ARG   A 1 197 ? -7.104  -23.633 90.774 1   68.74 ? 178 ARG   B NH1   1 
ATOM   1311 N NH2   . ARG   A 1 197 ? -6.753  -25.402 92.187 1   66.8  ? 178 ARG   B NH2   1 
ATOM   1312 N N     . ALA   A 1 198 ? -5.043  -27.592 85.825 1   3     ? 179 ALA   B N     1 
ATOM   1313 C CA    . ALA   A 1 198 ? -4.996  -27.237 84.394 1   3     ? 179 ALA   B CA    1 
ATOM   1314 C C     . ALA   A 1 198 ? -4.683  -28.483 83.563 1   5.25  ? 179 ALA   B C     1 
ATOM   1315 O O     . ALA   A 1 198 ? -5.308  -28.692 82.529 1   3     ? 179 ALA   B O     1 
ATOM   1316 C CB    . ALA   A 1 198 ? -3.952  -26.162 84.142 1   3.69  ? 179 ALA   B CB    1 
ATOM   1317 N N     . LEU   A 1 199 ? -3.755  -29.337 84.043 1   3     ? 180 LEU   B N     1 
ATOM   1318 C CA    . LEU   A 1 199 ? -3.399  -30.591 83.358 1   3     ? 180 LEU   B CA    1 
ATOM   1319 C C     . LEU   A 1 199 ? -4.622  -31.531 83.309 1   5.12  ? 180 LEU   B C     1 
ATOM   1320 O O     . LEU   A 1 199 ? -4.849  -32.191 82.293 1   3     ? 180 LEU   B O     1 
ATOM   1321 C CB    . LEU   A 1 199 ? -2.233  -31.278 84.069 1   3     ? 180 LEU   B CB    1 
ATOM   1322 C CG    . LEU   A 1 199 ? -0.851  -30.625 83.878 1   4.86  ? 180 LEU   B CG    1 
ATOM   1323 C CD1   . LEU   A 1 199 ? 0.151   -31.202 84.887 1   4.93  ? 180 LEU   B CD1   1 
ATOM   1324 C CD2   . LEU   A 1 199 ? -0.339  -30.822 82.443 1   4.22  ? 180 LEU   B CD2   1 
ATOM   1325 N N     . ARG   A 1 200 ? -5.411  -31.572 84.403 1   3     ? 181 ARG   B N     1 
ATOM   1326 C CA    . ARG   A 1 200 ? -6.64   -32.379 84.449 1   3     ? 181 ARG   B CA    1 
ATOM   1327 C C     . ARG   A 1 200 ? -7.638  -31.805 83.454 1   5.22  ? 181 ARG   B C     1 
ATOM   1328 O O     . ARG   A 1 200 ? -8.238  -32.566 82.695 1   3.1   ? 181 ARG   B O     1 
ATOM   1329 C CB    . ARG   A 1 200 ? -7.266  -32.351 85.838 1   4.64  ? 181 ARG   B CB    1 
ATOM   1330 C CG    . ARG   A 1 200 ? -6.615  -33.297 86.814 1   9.87  ? 181 ARG   B CG    1 
ATOM   1331 C CD    . ARG   A 1 200 ? -7.487  -33.404 88.033 1   15.56 ? 181 ARG   B CD    1 
ATOM   1332 N NE    . ARG   A 1 200 ? -6.688  -33.597 89.235 1   22.09 ? 181 ARG   B NE    1 
ATOM   1333 C CZ    . ARG   A 1 200 ? -6.382  -34.786 89.741 1   19.93 ? 181 ARG   B CZ    1 
ATOM   1334 N NH1   . ARG   A 1 200 ? -6.801  -35.899 89.144 1   10.04 ? 181 ARG   B NH1   1 
ATOM   1335 N NH2   . ARG   A 1 200 ? -5.652  -34.873 90.843 1   20.27 ? 181 ARG   B NH2   1 
ATOM   1336 N N     . ASN   A 1 201 ? -7.795  -30.457 83.437 1   3     ? 182 ASN   B N     1 
ATOM   1337 C CA    . ASN   A 1 201 ? -8.713  -29.748 82.526 1   3     ? 182 ASN   B CA    1 
ATOM   1338 C C     . ASN   A 1 201 ? -8.358  -30.038 81.066 1   6.5   ? 182 ASN   B C     1 
ATOM   1339 O O     . ASN   A 1 201 ? -9.264  -30.244 80.253 1   4.7   ? 182 ASN   B O     1 
ATOM   1340 C CB    . ASN   A 1 201 ? -8.715  -28.235 82.806 1   3     ? 182 ASN   B CB    1 
ATOM   1341 C CG    . ASN   A 1 201 ? -9.195  -27.859 84.194 1   6.79  ? 182 ASN   B CG    1 
ATOM   1342 O OD1   . ASN   A 1 201 ? -9.847  -28.649 84.909 1   5.07  ? 182 ASN   B OD1   1 
ATOM   1343 N ND2   . ASN   A 1 201 ? -8.861  -26.65  84.626 1   3     ? 182 ASN   B ND2   1 
ATOM   1344 N N     . LEU   A 1 202 ? -7.04   -30.093 80.738 1   3     ? 183 LEU   B N     1 
ATOM   1345 C CA    . LEU   A 1 202 ? -6.589  -30.424 79.383 1   3     ? 183 LEU   B CA    1 
ATOM   1346 C C     . LEU   A 1 202 ? -6.927  -31.873 79.058 1   5.19  ? 183 LEU   B C     1 
ATOM   1347 O O     . LEU   A 1 202 ? -7.279  -32.161 77.926 1   3.16  ? 183 LEU   B O     1 
ATOM   1348 C CB    . LEU   A 1 202 ? -5.08   -30.191 79.181 1   3.14  ? 183 LEU   B CB    1 
ATOM   1349 C CG    . LEU   A 1 202 ? -4.52   -28.752 79.338 1   6.73  ? 183 LEU   B CG    1 
ATOM   1350 C CD1   . LEU   A 1 202 ? -3.108  -28.641 78.75  1   7.19  ? 183 LEU   B CD1   1 
ATOM   1351 C CD2   . LEU   A 1 202 ? -5.44   -27.698 78.76  1   6.74  ? 183 LEU   B CD2   1 
ATOM   1352 N N     . GLY   A 1 203 ? -6.836  -32.758 80.061 1   3     ? 184 GLY   B N     1 
ATOM   1353 C CA    . GLY   A 1 203 ? -7.164  -34.178 79.931 1   3     ? 184 GLY   B CA    1 
ATOM   1354 C C     . GLY   A 1 203 ? -8.594  -34.429 79.494 1   6.53  ? 184 GLY   B C     1 
ATOM   1355 O O     . GLY   A 1 203 ? -8.849  -35.349 78.707 1   5.1   ? 184 GLY   B O     1 
ATOM   1356 N N     . SER   A 1 204 ? -9.537  -33.568 79.943 1   3.5   ? 185 SER   B N     1 
ATOM   1357 C CA    . SER   A 1 204 ? -10.957 -33.662 79.553 1   3.89  ? 185 SER   B CA    1 
ATOM   1358 C C     . SER   A 1 204 ? -11.149 -33.551 78.021 1   7.98  ? 185 SER   B C     1 
ATOM   1359 O O     . SER   A 1 204 ? -12.16  -34.029 77.504 1   8.26  ? 185 SER   B O     1 
ATOM   1360 C CB    . SER   A 1 204 ? -11.785 -32.599 80.28  1   5.21  ? 185 SER   B CB    1 
ATOM   1361 O OG    . SER   A 1 204 ? -11.695 -31.312 79.678 1   7.01  ? 185 SER   B OG    1 
ATOM   1362 N N     . LEU   A 1 205 ? -10.18  -32.923 77.304 1   3.16  ? 186 LEU   B N     1 
ATOM   1363 C CA    . LEU   A 1 205 ? -10.227 -32.74  75.837 1   3.33  ? 186 LEU   B CA    1 
ATOM   1364 C C     . LEU   A 1 205 ? -9.611  -33.905 75.091 1   5.92  ? 186 LEU   B C     1 
ATOM   1365 O O     . LEU   A 1 205 ? -9.622  -33.919 73.853 1   3.96  ? 186 LEU   B O     1 
ATOM   1366 C CB    . LEU   A 1 205 ? -9.466  -31.472 75.415 1   3     ? 186 LEU   B CB    1 
ATOM   1367 C CG    . LEU   A 1 205 ? -9.869  -30.145 76.041 1   7.18  ? 186 LEU   B CG    1 
ATOM   1368 C CD1   . LEU   A 1 205 ? -8.907  -29.047 75.59  1   6.39  ? 186 LEU   B CD1   1 
ATOM   1369 C CD2   . LEU   A 1 205 ? -11.311 -29.767 75.645 1   7.62  ? 186 LEU   B CD2   1 
ATOM   1370 N N     . LEU   A 1 206 ? -8.993  -34.837 75.844 1   3.49  ? 187 LEU   B N     1 
ATOM   1371 C CA    . LEU   A 1 206 ? -8.255  -35.958 75.289 1   4.13  ? 187 LEU   B CA    1 
ATOM   1372 C C     . LEU   A 1 206 ? -9.022  -37.267 75.407 1   9.98  ? 187 LEU   B C     1 
ATOM   1373 O O     . LEU   A 1 206 ? -9.622  -37.556 76.458 1   9.75  ? 187 LEU   B O     1 
ATOM   1374 C CB    . LEU   A 1 206 ? -6.939  -36.126 76.084 1   3.06  ? 187 LEU   B CB    1 
ATOM   1375 C CG    . LEU   A 1 206 ? -5.634  -35.597 75.525 1   7.29  ? 187 LEU   B CG    1 
ATOM   1376 C CD1   . LEU   A 1 206 ? -4.496  -35.988 76.475 1   5.81  ? 187 LEU   B CD1   1 
ATOM   1377 C CD2   . LEU   A 1 206 ? -5.343  -36.131 74.114 1   7.18  ? 187 LEU   B CD2   1 
ATOM   1378 N N     . LYS   A 1 207 ? -8.88   -38.107 74.375 1   8.71  ? 188 LYS   B N     1 
ATOM   1379 C CA    . LYS   A 1 207 ? -9.445  -39.446 74.36  1   10.57 ? 188 LYS   B CA    1 
ATOM   1380 C C     . LYS   A 1 207 ? -8.615  -40.324 75.352 1   12.04 ? 188 LYS   B C     1 
ATOM   1381 O O     . LYS   A 1 207 ? -7.432  -40.014 75.589 1   11.39 ? 188 LYS   B O     1 
ATOM   1382 C CB    . LYS   A 1 207 ? -9.381  -40.037 72.923 1   13.43 ? 188 LYS   B CB    1 
ATOM   1383 C CG    . LYS   A 1 207 ? -7.961  -40.32  72.421 1   18.88 ? 188 LYS   B CG    1 
ATOM   1384 C CD    . LYS   A 1 207 ? -7.901  -41.078 71.112 1   25.18 ? 188 LYS   B CD    1 
ATOM   1385 C CE    . LYS   A 1 207 ? -6.48   -41.555 70.886 1   27.93 ? 188 LYS   B CE    1 
ATOM   1386 N NZ    . LYS   A 1 207 ? -6.326  -42.253 69.584 1   36.44 ? 188 LYS   B NZ    1 
ATOM   1387 N N     . PRO   A 1 208 ? -9.185  -41.426 75.917 1   13.11 ? 189 PRO   B N     1 
ATOM   1388 C CA    . PRO   A 1 208 ? -8.361  -42.316 76.768 1   12.69 ? 189 PRO   B CA    1 
ATOM   1389 C C     . PRO   A 1 208 ? -7.172  -42.836 75.944 1   11.94 ? 189 PRO   B C     1 
ATOM   1390 O O     . PRO   A 1 208 ? -7.335  -43.145 74.755 1   12.92 ? 189 PRO   B O     1 
ATOM   1391 C CB    . PRO   A 1 208 ? -9.322  -43.459 77.141 1   14.37 ? 189 PRO   B CB    1 
ATOM   1392 C CG    . PRO   A 1 208 ? -10.7   -42.944 76.855 1   18.31 ? 189 PRO   B CG    1 
ATOM   1393 C CD    . PRO   A 1 208 ? -10.558 -41.955 75.74  1   15.81 ? 189 PRO   B CD    1 
ATOM   1394 N N     . GLY   A 1 209 ? -5.983  -42.82  76.542 1   7.7   ? 190 GLY   B N     1 
ATOM   1395 C CA    . GLY   A 1 209 ? -4.75   -43.22  75.864 1   6.16  ? 190 GLY   B CA    1 
ATOM   1396 C C     . GLY   A 1 209 ? -4.2    -42.161 74.922 1   8.1   ? 190 GLY   B C     1 
ATOM   1397 O O     . GLY   A 1 209 ? -3.207  -42.405 74.235 1   5.79  ? 190 GLY   B O     1 
ATOM   1398 N N     . GLY   A 1 210 ? -4.863  -40.992 74.876 1   4.65  ? 191 GLY   B N     1 
ATOM   1399 C CA    . GLY   A 1 210 ? -4.452  -39.858 74.054 1   3.57  ? 191 GLY   B CA    1 
ATOM   1400 C C     . GLY   A 1 210 ? -3.146  -39.284 74.581 1   6.03  ? 191 GLY   B C     1 
ATOM   1401 O O     . GLY   A 1 210 ? -2.818  -39.469 75.765 1   4.03  ? 191 GLY   B O     1 
ATOM   1402 N N     . PHE   A 1 211 ? -2.395  -38.605 73.71  1   3     ? 192 PHE   B N     1 
ATOM   1403 C CA    . PHE   A 1 211 ? -1.093  -38.037 74.065 1   3     ? 192 PHE   B CA    1 
ATOM   1404 C C     . PHE   A 1 211 ? -1.169  -36.584 74.535 1   5.44  ? 192 PHE   B C     1 
ATOM   1405 O O     . PHE   A 1 211 ? -1.913  -35.778 73.971 1   3     ? 192 PHE   B O     1 
ATOM   1406 C CB    . PHE   A 1 211 ? -0.133  -38.121 72.87  1   4.54  ? 192 PHE   B CB    1 
ATOM   1407 C CG    . PHE   A 1 211 ? 0.296   -39.523 72.495 1   6.59  ? 192 PHE   B CG    1 
ATOM   1408 C CD1   . PHE   A 1 211 ? 1.42    -40.101 73.073 1   6.82  ? 192 PHE   B CD1   1 
ATOM   1409 C CD2   . PHE   A 1 211 ? -0.404  -40.25  71.535 1   8.16  ? 192 PHE   B CD2   1 
ATOM   1410 C CE1   . PHE   A 1 211 ? 1.836   -41.389 72.709 1   7.11  ? 192 PHE   B CE1   1 
ATOM   1411 C CE2   . PHE   A 1 211 ? 0.004   -41.544 71.177 1   9.01  ? 192 PHE   B CE2   1 
ATOM   1412 C CZ    . PHE   A 1 211 ? 1.123   -42.102 71.766 1   8.41  ? 192 PHE   B CZ    1 
ATOM   1413 N N     . LEU   A 1 212 ? -0.345  -36.249 75.528 1   3     ? 193 LEU   B N     1 
ATOM   1414 C CA    . LEU   A 1 212 ? -0.197  -34.889 76.055 1   3     ? 193 LEU   B CA    1 
ATOM   1415 C C     . LEU   A 1 212 ? 1.264   -34.497 75.778 1   5.42  ? 193 LEU   B C     1 
ATOM   1416 O O     . LEU   A 1 212 ? 2.171   -35.225 76.206 1   3     ? 193 LEU   B O     1 
ATOM   1417 C CB    . LEU   A 1 212 ? -0.461  -34.858 77.569 1   3     ? 193 LEU   B CB    1 
ATOM   1418 C CG    . LEU   A 1 212 ? -0.332  -33.476 78.244 1   6.3   ? 193 LEU   B CG    1 
ATOM   1419 C CD1   . LEU   A 1 212 ? -1.537  -32.584 77.911 1   6.39  ? 193 LEU   B CD1   1 
ATOM   1420 C CD2   . LEU   A 1 212 ? -0.143  -33.622 79.76  1   5.41  ? 193 LEU   B CD2   1 
ATOM   1421 N N     . VAL   A 1 213 ? 1.481   -33.397 75.033 1   3     ? 194 VAL   B N     1 
ATOM   1422 C CA    . VAL   A 1 213 ? 2.835   -32.939 74.708 1   3     ? 194 VAL   B CA    1 
ATOM   1423 C C     . VAL   A 1 213 ? 3.008   -31.545 75.306 1   5.02  ? 194 VAL   B C     1 
ATOM   1424 O O     . VAL   A 1 213 ? 2.273   -30.63  74.934 1   3     ? 194 VAL   B O     1 
ATOM   1425 C CB    . VAL   A 1 213 ? 3.138   -32.965 73.184 1   3.81  ? 194 VAL   B CB    1 
ATOM   1426 C CG1   . VAL   A 1 213 ? 4.566   -32.489 72.907 1   3     ? 194 VAL   B CG1   1 
ATOM   1427 C CG2   . VAL   A 1 213 ? 2.914   -34.367 72.596 1   3     ? 194 VAL   B CG2   1 
ATOM   1428 N N     . ILE   A 1 214 ? 3.957   -31.393 76.25  1   3     ? 195 ILE   B N     1 
ATOM   1429 C CA    . ILE   A 1 214 ? 4.192   -30.097 76.896 1   3     ? 195 ILE   B CA    1 
ATOM   1430 C C     . ILE   A 1 214 ? 5.663   -29.723 76.777 1   4.69  ? 195 ILE   B C     1 
ATOM   1431 O O     . ILE   A 1 214 ? 6.521   -30.571 76.991 1   3     ? 195 ILE   B O     1 
ATOM   1432 C CB    . ILE   A 1 214 ? 3.762   -30.082 78.397 1   4.09  ? 195 ILE   B CB    1 
ATOM   1433 C CG1   . ILE   A 1 214 ? 2.328   -30.637 78.635 1   5.37  ? 195 ILE   B CG1   1 
ATOM   1434 C CG2   . ILE   A 1 214 ? 3.946   -28.676 79.041 1   3     ? 195 ILE   B CG2   1 
ATOM   1435 C CD1   . ILE   A 1 214 ? 1.126   -29.853 77.997 1   9.42  ? 195 ILE   B CD1   1 
ATOM   1436 N N     . MET   A 1 215 ? 5.937   -28.453 76.452 1   3     ? 196 MET   B N     1 
ATOM   1437 C CA    . MET   A 1 215 ? 7.297   -27.894 76.418 1   3     ? 196 MET   B CA    1 
ATOM   1438 C C     . MET   A 1 215 ? 7.176   -26.554 77.108 1   5.01  ? 196 MET   B C     1 
ATOM   1439 O O     . MET   A 1 215 ? 6.278   -25.794 76.761 1   3     ? 196 MET   B O     1 
ATOM   1440 C CB    . MET   A 1 215 ? 7.807   -27.719 74.986 1   5.27  ? 196 MET   B CB    1 
ATOM   1441 C CG    . MET   A 1 215 ? 7.983   -29.036 74.272 1   8.76  ? 196 MET   B CG    1 
ATOM   1442 S SD    . MET   A 1 215 ? 8.463   -28.862 72.542 1   7.3   ? 196 MET   B SD    1 
ATOM   1443 C CE    . MET   A 1 215 ? 8.353   -30.573 72.04  1   10.49 ? 196 MET   B CE    1 
ATOM   1444 N N     . ASP   A 1 216 ? 8       -26.29  78.128 1   3     ? 197 ASP   B N     1 
ATOM   1445 C CA    . ASP   A 1 216 ? 7.877   -25.033 78.879 1   3     ? 197 ASP   B CA    1 
ATOM   1446 C C     . ASP   A 1 216 ? 9.157   -24.708 79.632 1   4.53  ? 197 ASP   B C     1 
ATOM   1447 O O     . ASP   A 1 216 ? 10.088  -25.504 79.633 1   3     ? 197 ASP   B O     1 
ATOM   1448 C CB    . ASP   A 1 216 ? 6.674   -25.088 79.857 1   3     ? 197 ASP   B CB    1 
ATOM   1449 C CG    . ASP   A 1 216 ? 5.933   -23.769 80.063 1   5.25  ? 197 ASP   B CG    1 
ATOM   1450 O OD1   . ASP   A 1 216 ? 6.569   -22.686 79.927 1   3     ? 197 ASP   B OD1   1 
ATOM   1451 O OD2   . ASP   A 1 216 ? 4.719   -23.815 80.373 1   3     ? 197 ASP   B OD2   1 
ATOM   1452 N N     . ALA   A 1 217 ? 9.213   -23.511 80.226 1   3     ? 198 ALA   B N     1 
ATOM   1453 C CA    . ALA   A 1 217 ? 10.396  -23.055 80.942 1   3     ? 198 ALA   B CA    1 
ATOM   1454 C C     . ALA   A 1 217 ? 10.516  -23.698 82.323 1   5.1   ? 198 ALA   B C     1 
ATOM   1455 O O     . ALA   A 1 217 ? 9.509   -23.99  82.98  1   3     ? 198 ALA   B O     1 
ATOM   1456 C CB    . ALA   A 1 217 ? 10.367  -21.534 81.068 1   3     ? 198 ALA   B CB    1 
ATOM   1457 N N     . LEU   A 1 218 ? 11.755  -23.913 82.771 1   3     ? 199 LEU   B N     1 
ATOM   1458 C CA    . LEU   A 1 218 ? 11.969  -24.439 84.118 1   3     ? 199 LEU   B CA    1 
ATOM   1459 C C     . LEU   A 1 218 ? 12.402  -23.281 85.022 1   5.16  ? 199 LEU   B C     1 
ATOM   1460 O O     . LEU   A 1 218 ? 13.181  -22.428 84.585 1   3     ? 199 LEU   B O     1 
ATOM   1461 C CB    . LEU   A 1 218 ? 13.05   -25.529 84.148 1   3     ? 199 LEU   B CB    1 
ATOM   1462 C CG    . LEU   A 1 218 ? 12.653  -26.927 83.614 1   4.39  ? 199 LEU   B CG    1 
ATOM   1463 C CD1   . LEU   A 1 218 ? 13.862  -27.812 83.528 1   3     ? 199 LEU   B CD1   1 
ATOM   1464 C CD2   . LEU   A 1 218 ? 11.59   -27.599 84.5   1   3.1   ? 199 LEU   B CD2   1 
ATOM   1465 N N     . LYS   A 1 219 ? 11.875  -23.253 86.262 1   3     ? 200 LYS   B N     1 
ATOM   1466 C CA    . LYS   A 1 219 ? 12.23   -22.289 87.311 1   3     ? 200 LYS   B CA    1 
ATOM   1467 C C     . LYS   A 1 219 ? 12.241  -20.829 86.82  1   5.54  ? 200 LYS   B C     1 
ATOM   1468 O O     . LYS   A 1 219 ? 13.198  -20.095 87.075 1   3     ? 200 LYS   B O     1 
ATOM   1469 C CB    . LYS   A 1 219 ? 13.588  -22.677 87.932 1   6.1   ? 200 LYS   B CB    1 
ATOM   1470 C CG    . LYS   A 1 219 ? 13.581  -24.044 88.62  1   14.94 ? 200 LYS   B CG    1 
ATOM   1471 C CD    . LYS   A 1 219 ? 14.96   -24.408 89.142 1   17.09 ? 200 LYS   B CD    1 
ATOM   1472 C CE    . LYS   A 1 219 ? 14.945  -25.695 89.934 1   35.92 ? 200 LYS   B CE    1 
ATOM   1473 N NZ    . LYS   A 1 219 ? 16.296  -26.324 89.992 1   45    ? 200 LYS   B NZ    1 
ATOM   1474 N N     . SER   A 1 220 ? 11.194  -20.432 86.086 1   3     ? 201 SER   B N     1 
ATOM   1475 C CA    . SER   A 1 220 ? 11.069  -19.063 85.575 1   3     ? 201 SER   B CA    1 
ATOM   1476 C C     . SER   A 1 220 ? 9.957   -18.368 86.345 1   5.08  ? 201 SER   B C     1 
ATOM   1477 O O     . SER   A 1 220 ? 8.854   -18.924 86.426 1   3     ? 201 SER   B O     1 
ATOM   1478 C CB    . SER   A 1 220 ? 10.752  -19.078 84.081 1   3     ? 201 SER   B CB    1 
ATOM   1479 O OG    . SER   A 1 220 ? 10.914  -17.783 83.524 1   5.23  ? 201 SER   B OG    1 
ATOM   1480 N N     . SER   A 1 221 ? 10.24   -17.187 86.965 1   3     ? 202 SER   B N     1 
ATOM   1481 C CA    . SER   A 1 221 ? 9.188   -16.472 87.703 1   3     ? 202 SER   B CA    1 
ATOM   1482 C C     . SER   A 1 221 ? 8.619   -15.29  86.896 1   4.69  ? 202 SER   B C     1 
ATOM   1483 O O     . SER   A 1 221 ? 7.612   -14.698 87.302 1   3     ? 202 SER   B O     1 
ATOM   1484 C CB    . SER   A 1 221 ? 9.664   -16.028 89.084 1   6.6   ? 202 SER   B CB    1 
ATOM   1485 O OG    . SER   A 1 221 ? 10.738  -15.117 88.928 1   8.03  ? 202 SER   B OG    1 
ATOM   1486 N N     . TYR   A 1 222 ? 9.234   -14.978 85.738 1   3     ? 203 TYR   B N     1 
ATOM   1487 C CA    . TYR   A 1 222 ? 8.744   -13.921 84.841 1   3     ? 203 TYR   B CA    1 
ATOM   1488 C C     . TYR   A 1 222 ? 9.323   -14.033 83.437 1   5.92  ? 203 TYR   B C     1 
ATOM   1489 O O     . TYR   A 1 222 ? 10.365  -14.665 83.235 1   3     ? 203 TYR   B O     1 
ATOM   1490 C CB    . TYR   A 1 222 ? 9.036   -12.497 85.423 1   3     ? 203 TYR   B CB    1 
ATOM   1491 C CG    . TYR   A 1 222 ? 10.489  -12.076 85.292 1   5.07  ? 203 TYR   B CG    1 
ATOM   1492 C CD1   . TYR   A 1 222 ? 10.946  -11.42  84.151 1   6.17  ? 203 TYR   B CD1   1 
ATOM   1493 C CD2   . TYR   A 1 222 ? 11.412  -12.366 86.292 1   6.01  ? 203 TYR   B CD2   1 
ATOM   1494 C CE1   . TYR   A 1 222 ? 12.294  -11.088 83.995 1   7.23  ? 203 TYR   B CE1   1 
ATOM   1495 C CE2   . TYR   A 1 222 ? 12.763  -12.031 86.152 1   7.32  ? 203 TYR   B CE2   1 
ATOM   1496 C CZ    . TYR   A 1 222 ? 13.201  -11.403 84.994 1   7.16  ? 203 TYR   B CZ    1 
ATOM   1497 O OH    . TYR   A 1 222 ? 14.531  -11.095 84.822 1   10.06 ? 203 TYR   B OH    1 
ATOM   1498 N N     . TYR   A 1 223 ? 8.689   -13.328 82.487 1   3     ? 204 TYR   B N     1 
ATOM   1499 C CA    . TYR   A 1 223 ? 9.163   -13.176 81.12  1   3     ? 204 TYR   B CA    1 
ATOM   1500 C C     . TYR   A 1 223 ? 8.71    -11.821 80.628 1   5.38  ? 204 TYR   B C     1 
ATOM   1501 O O     . TYR   A 1 223 ? 7.654   -11.329 81.061 1   3     ? 204 TYR   B O     1 
ATOM   1502 C CB    . TYR   A 1 223 ? 8.774   -14.331 80.181 1   3     ? 204 TYR   B CB    1 
ATOM   1503 C CG    . TYR   A 1 223 ? 7.319   -14.348 79.775 1   3     ? 204 TYR   B CG    1 
ATOM   1504 C CD1   . TYR   A 1 223 ? 6.356   -14.928 80.594 1   3.28  ? 204 TYR   B CD1   1 
ATOM   1505 C CD2   . TYR   A 1 223 ? 6.911   -13.832 78.546 1   3     ? 204 TYR   B CD2   1 
ATOM   1506 C CE1   . TYR   A 1 223 ? 5.018   -14.984 80.21  1   3     ? 204 TYR   B CE1   1 
ATOM   1507 C CE2   . TYR   A 1 223 ? 5.575   -13.881 78.149 1   3     ? 204 TYR   B CE2   1 
ATOM   1508 C CZ    . TYR   A 1 223 ? 4.628   -14.449 78.993 1   6.39  ? 204 TYR   B CZ    1 
ATOM   1509 O OH    . TYR   A 1 223 ? 3.303   -14.496 78.632 1   3     ? 204 TYR   B OH    1 
ATOM   1510 N N     . MET   A 1 224 ? 9.515   -11.219 79.739 1   3     ? 205 MET   B N     1 
ATOM   1511 C CA    . MET   A 1 224 ? 9.305   -9.869  79.241 1   3     ? 205 MET   B CA    1 
ATOM   1512 C C     . MET   A 1 224 ? 8.935   -9.814  77.77  1   5.82  ? 205 MET   B C     1 
ATOM   1513 O O     . MET   A 1 224 ? 9.422   -10.611 76.961 1   3     ? 205 MET   B O     1 
ATOM   1514 C CB    . MET   A 1 224 ? 10.611  -9.049  79.411 1   3.33  ? 205 MET   B CB    1 
ATOM   1515 C CG    . MET   A 1 224 ? 11.187  -9.016  80.823 1   4.21  ? 205 MET   B CG    1 
ATOM   1516 S SD    . MET   A 1 224 ? 10.123  -8.2    82.057 1   6.32  ? 205 MET   B SD    1 
ATOM   1517 C CE    . MET   A 1 224 ? 10.132  -6.448  81.45  1   5.6   ? 205 MET   B CE    1 
ATOM   1518 N N     . ILE   A 1 225 ? 8.127   -8.805  77.406 1   3     ? 206 ILE   B N     1 
ATOM   1519 C CA    . ILE   A 1 225 ? 7.816   -8.471  76.012 1   3     ? 206 ILE   B CA    1 
ATOM   1520 C C     . ILE   A 1 225 ? 8.113   -6.969  75.994 1   5.93  ? 206 ILE   B C     1 
ATOM   1521 O O     . ILE   A 1 225 ? 7.262   -6.173  76.41  1   3.1   ? 206 ILE   B O     1 
ATOM   1522 C CB    . ILE   A 1 225 ? 6.364   -8.799  75.563 1   6.12  ? 206 ILE   B CB    1 
ATOM   1523 C CG1   . ILE   A 1 225 ? 6.034   -10.303 75.79  1   5.49  ? 206 ILE   B CG1   1 
ATOM   1524 C CG2   . ILE   A 1 225 ? 6.209   -8.415  74.069 1   5.94  ? 206 ILE   B CG2   1 
ATOM   1525 C CD1   . ILE   A 1 225 ? 4.615   -10.699 75.468 1   3     ? 206 ILE   B CD1   1 
ATOM   1526 N N     . GLY   A 1 226 ? 9.359   -6.626  75.658 1   3     ? 207 GLY   B N     1 
ATOM   1527 C CA    . GLY   A 1 226 ? 9.839   -5.251  75.726 1   5.36  ? 207 GLY   B CA    1 
ATOM   1528 C C     . GLY   A 1 226 ? 9.842   -4.831  77.189 1   9.41  ? 207 GLY   B C     1 
ATOM   1529 O O     . GLY   A 1 226 ? 10.367  -5.556  78.037 1   5.66  ? 207 GLY   B O     1 
ATOM   1530 N N     . GLU   A 1 227 ? 9.167   -3.714  77.514 1   8.28  ? 208 GLU   B N     1 
ATOM   1531 C CA    . GLU   A 1 227 ? 9.091   -3.24   78.904 1   9.72  ? 208 GLU   B CA    1 
ATOM   1532 C C     . GLU   A 1 227 ? 7.98    -3.954  79.711 1   11.12 ? 208 GLU   B C     1 
ATOM   1533 O O     . GLU   A 1 227 ? 7.898   -3.78   80.932 1   9.55  ? 208 GLU   B O     1 
ATOM   1534 C CB    . GLU   A 1 227 ? 8.854   -1.722  78.93  1   14.14 ? 208 GLU   B CB    1 
ATOM   1535 C CG    . GLU   A 1 227 ? 10.086  -0.893  78.633 1   20.91 ? 208 GLU   B CG    1 
ATOM   1536 C CD    . GLU   A 1 227 ? 9.827   0.597   78.765 1   41.4  ? 208 GLU   B CD    1 
ATOM   1537 O OE1   . GLU   A 1 227 ? 10.166  1.166   79.828 1   45.71 ? 208 GLU   B OE1   1 
ATOM   1538 O OE2   . GLU   A 1 227 ? 9.268   1.191   77.815 1   36.65 ? 208 GLU   B OE2   1 
ATOM   1539 N N     . GLN   A 1 228 ? 7.107   -4.713  79.03  1   6.51  ? 209 GLN   B N     1 
ATOM   1540 C CA    . GLN   A 1 228 ? 5.989   -5.376  79.698 1   5.58  ? 209 GLN   B CA    1 
ATOM   1541 C C     . GLN   A 1 228 ? 6.414   -6.672  80.381 1   5.78  ? 209 GLN   B C     1 
ATOM   1542 O O     . GLN   A 1 228 ? 6.929   -7.583  79.724 1   3     ? 209 GLN   B O     1 
ATOM   1543 C CB    . GLN   A 1 228 ? 4.832   -5.62   78.715 1   5.19  ? 209 GLN   B CB    1 
ATOM   1544 C CG    . GLN   A 1 228 ? 3.581   -6.27   79.349 1   4.03  ? 209 GLN   B CG    1 
ATOM   1545 C CD    . GLN   A 1 228 ? 2.857   -5.38   80.332 1   13.71 ? 209 GLN   B CD    1 
ATOM   1546 O OE1   . GLN   A 1 228 ? 2.801   -5.654  81.543 1   12.33 ? 209 GLN   B OE1   1 
ATOM   1547 N NE2   . GLN   A 1 228 ? 2.282   -4.302  79.826 1   7.4   ? 209 GLN   B NE2   1 
ATOM   1548 N N     . LYS   A 1 229 ? 6.171   -6.756  81.689 1   4.34  ? 210 LYS   B N     1 
ATOM   1549 C CA    . LYS   A 1 229 ? 6.492   -7.952  82.475 1   3     ? 210 LYS   B CA    1 
ATOM   1550 C C     . LYS   A 1 229 ? 5.258   -8.855  82.601 1   5.34  ? 210 LYS   B C     1 
ATOM   1551 O O     . LYS   A 1 229 ? 4.131   -8.365  82.772 1   3     ? 210 LYS   B O     1 
ATOM   1552 C CB    . LYS   A 1 229 ? 6.996   -7.558  83.881 1   4.24  ? 210 LYS   B CB    1 
ATOM   1553 C CG    . LYS   A 1 229 ? 7.555   -8.718  84.715 1   5.4   ? 210 LYS   B CG    1 
ATOM   1554 C CD    . LYS   A 1 229 ? 7.895   -8.236  86.114 1   10.37 ? 210 LYS   B CD    1 
ATOM   1555 C CE    . LYS   A 1 229 ? 8.851   -9.168  86.82  1   12.61 ? 210 LYS   B CE    1 
ATOM   1556 N NZ    . LYS   A 1 229 ? 9.357   -8.584  88.084 1   12.01 ? 210 LYS   B NZ    1 
ATOM   1557 N N     . PHE   A 1 230 ? 5.489   -10.184 82.526 1   3     ? 211 PHE   B N     1 
ATOM   1558 C CA    . PHE   A 1 230 ? 4.435   -11.19  82.73  1   3     ? 211 PHE   B CA    1 
ATOM   1559 C C     . PHE   A 1 230 ? 4.936   -12.179 83.757 1   4.97  ? 211 PHE   B C     1 
ATOM   1560 O O     . PHE   A 1 230 ? 6.112   -12.55  83.712 1   3     ? 211 PHE   B O     1 
ATOM   1561 C CB    . PHE   A 1 230 ? 4.082   -11.927 81.43  1   3.08  ? 211 PHE   B CB    1 
ATOM   1562 C CG    . PHE   A 1 230 ? 3.311   -11.08  80.452 1   3.34  ? 211 PHE   B CG    1 
ATOM   1563 C CD1   . PHE   A 1 230 ? 1.924   -10.95  80.558 1   4.69  ? 211 PHE   B CD1   1 
ATOM   1564 C CD2   . PHE   A 1 230 ? 3.972   -10.359 79.461 1   4.9   ? 211 PHE   B CD2   1 
ATOM   1565 C CE1   . PHE   A 1 230 ? 1.213   -10.128 79.68  1   4.04  ? 211 PHE   B CE1   1 
ATOM   1566 C CE2   . PHE   A 1 230 ? 3.253   -9.548  78.57  1   6.64  ? 211 PHE   B CE2   1 
ATOM   1567 C CZ    . PHE   A 1 230 ? 1.882   -9.434  78.695 1   4.03  ? 211 PHE   B CZ    1 
ATOM   1568 N N     . SER   A 1 231 ? 4.055   -12.612 84.661 1   3     ? 212 SER   B N     1 
ATOM   1569 C CA    . SER   A 1 231 ? 4.396   -13.583 85.696 1   3     ? 212 SER   B CA    1 
ATOM   1570 C C     . SER   A 1 231 ? 4.568   -14.987 85.081 1   5.74  ? 212 SER   B C     1 
ATOM   1571 O O     . SER   A 1 231 ? 4.015   -15.287 84.025 1   3     ? 212 SER   B O     1 
ATOM   1572 C CB    . SER   A 1 231 ? 3.275   -13.654 86.726 1   6.58  ? 212 SER   B CB    1 
ATOM   1573 O OG    . SER   A 1 231 ? 3.11    -12.408 87.383 1   7.29  ? 212 SER   B OG    1 
ATOM   1574 N N     . SER   A 1 232 ? 5.314   -15.838 85.773 1   3.23  ? 213 SER   B N     1 
ATOM   1575 C CA    . SER   A 1 232 ? 5.466   -17.239 85.397 1   3     ? 213 SER   B CA    1 
ATOM   1576 C C     . SER   A 1 232 ? 5.612   -18.03  86.691 1   5.58  ? 213 SER   B C     1 
ATOM   1577 O O     . SER   A 1 232 ? 6.181   -17.526 87.665 1   3     ? 213 SER   B O     1 
ATOM   1578 C CB    . SER   A 1 232 ? 6.672   -17.442 84.482 1   4.56  ? 213 SER   B CB    1 
ATOM   1579 O OG    . SER   A 1 232 ? 7.021   -18.815 84.376 1   3     ? 213 SER   B OG    1 
ATOM   1580 N N     . LEU   A 1 233 ? 5.052   -19.239 86.711 1   3     ? 214 LEU   B N     1 
ATOM   1581 C CA    . LEU   A 1 233 ? 5.126   -20.141 87.867 1   3     ? 214 LEU   B CA    1 
ATOM   1582 C C     . LEU   A 1 233 ? 6.495   -20.848 87.831 1   4.05  ? 214 LEU   B C     1 
ATOM   1583 O O     . LEU   A 1 233 ? 6.773   -21.592 86.874 1   3     ? 214 LEU   B O     1 
ATOM   1584 C CB    . LEU   A 1 233 ? 3.96    -21.146 87.823 1   3     ? 214 LEU   B CB    1 
ATOM   1585 C CG    . LEU   A 1 233 ? 3.876   -22.209 88.932 1   7.16  ? 214 LEU   B CG    1 
ATOM   1586 C CD1   . LEU   A 1 233 ? 3.736   -21.555 90.333 1   6.39  ? 214 LEU   B CD1   1 
ATOM   1587 C CD2   . LEU   A 1 233 ? 2.726   -23.184 88.648 1   6.79  ? 214 LEU   B CD2   1 
ATOM   1588 N N     . PRO   A 1 234 ? 7.38    -20.596 88.821 1   3     ? 215 PRO   B N     1 
ATOM   1589 C CA    . PRO   A 1 234 ? 8.717   -21.197 88.764 1   3.88  ? 215 PRO   B CA    1 
ATOM   1590 C C     . PRO   A 1 234 ? 8.677   -22.644 89.244 1   7.59  ? 215 PRO   B C     1 
ATOM   1591 O O     . PRO   A 1 234 ? 8.594   -22.897 90.451 1   7.25  ? 215 PRO   B O     1 
ATOM   1592 C CB    . PRO   A 1 234 ? 9.566   -20.268 89.647 1   6.08  ? 215 PRO   B CB    1 
ATOM   1593 C CG    . PRO   A 1 234 ? 8.605   -19.694 90.63  1   5.42  ? 215 PRO   B CG    1 
ATOM   1594 C CD    . PRO   A 1 234 ? 7.23    -19.712 90.007 1   5.94  ? 215 PRO   B CD    1 
ATOM   1595 N N     . LEU   A 1 235 ? 8.644   -23.586 88.287 1   8.63  ? 216 LEU   B N     1 
ATOM   1596 C CA    . LEU   A 1 235 ? 8.576   -25.022 88.584 1   8.69  ? 216 LEU   B CA    1 
ATOM   1597 C C     . LEU   A 1 235 ? 9.844   -25.737 88.163 1   7.18  ? 216 LEU   B C     1 
ATOM   1598 O O     . LEU   A 1 235 ? 10.368  -25.484 87.07  1   3.29  ? 216 LEU   B O     1 
ATOM   1599 C CB    . LEU   A 1 235 ? 7.386   -25.701 87.857 1   9.5   ? 216 LEU   B CB    1 
ATOM   1600 C CG    . LEU   A 1 235 ? 5.961   -25.334 88.258 1   8.31  ? 216 LEU   B CG    1 
ATOM   1601 C CD1   . LEU   A 1 235 ? 4.973   -26.291 87.616 1   8.8   ? 216 LEU   B CD1   1 
ATOM   1602 C CD2   . LEU   A 1 235 ? 5.768   -25.346 89.785 1   7.52  ? 216 LEU   B CD2   1 
ATOM   1603 N N     . GLY   A 1 236 ? 10.271  -26.678 89.001 1   3     ? 217 GLY   B N     1 
ATOM   1604 C CA    . GLY   A 1 236 ? 11.401  -27.54  88.696 1   3.03  ? 217 GLY   B CA    1 
ATOM   1605 C C     . GLY   A 1 236 ? 10.893  -28.817 88.04  1   6.05  ? 217 GLY   B C     1 
ATOM   1606 O O     . GLY   A 1 236 ? 9.691   -29.112 88.094 1   3     ? 217 GLY   B O     1 
ATOM   1607 N N     . ARG   A 1 237 ? 11.801  -29.602 87.454 1   3     ? 218 ARG   B N     1 
ATOM   1608 C CA    . ARG   A 1 237 ? 11.442  -30.846 86.772 1   3.3   ? 218 ARG   B CA    1 
ATOM   1609 C C     . ARG   A 1 237 ? 10.642  -31.841 87.654 1   5.59  ? 218 ARG   B C     1 
ATOM   1610 O O     . ARG   A 1 237 ? 9.718   -32.496 87.159 1   3     ? 218 ARG   B O     1 
ATOM   1611 C CB    . ARG   A 1 237 ? 12.681  -31.517 86.153 1   6.69  ? 218 ARG   B CB    1 
ATOM   1612 C CG    . ARG   A 1 237 ? 13.716  -32.008 87.165 1   13.2  ? 218 ARG   B CG    1 
ATOM   1613 C CD    . ARG   A 1 237 ? 14.661  -33.04  86.572 1   33.59 ? 218 ARG   B CD    1 
ATOM   1614 N NE    . ARG   A 1 237 ? 14.007  -34.335 86.362 1   46.88 ? 218 ARG   B NE    1 
ATOM   1615 C CZ    . ARG   A 1 237 ? 13.869  -34.912 85.173 1   60.66 ? 218 ARG   B CZ    1 
ATOM   1616 N NH1   . ARG   A 1 237 ? 14.362  -34.332 84.085 1   62.86 ? 218 ARG   B NH1   1 
ATOM   1617 N NH2   . ARG   A 1 237 ? 13.281  -36.097 85.067 1   63.04 ? 218 ARG   B NH2   1 
ATOM   1618 N N     . GLU   A 1 238 ? 10.986  -31.933 88.951 1   3     ? 219 GLU   B N     1 
ATOM   1619 C CA    . GLU   A 1 238 ? 10.318  -32.846 89.892 1   3     ? 219 GLU   B CA    1 
ATOM   1620 C C     . GLU   A 1 238 ? 8.838   -32.467 90.085 1   5.6   ? 219 GLU   B C     1 
ATOM   1621 O O     . GLU   A 1 238 ? 7.974   -33.355 90.059 1   3     ? 219 GLU   B O     1 
ATOM   1622 C CB    . GLU   A 1 238 ? 11.048  -32.88  91.245 1   4.48  ? 219 GLU   B CB    1 
ATOM   1623 C CG    . GLU   A 1 238 ? 12.511  -33.289 91.138 1   9.29  ? 219 GLU   B CG    1 
ATOM   1624 C CD    . GLU   A 1 238 ? 13.529  -32.172 90.954 1   25.43 ? 219 GLU   B CD    1 
ATOM   1625 O OE1   . GLU   A 1 238 ? 13.138  -31.018 90.644 1   13.56 ? 219 GLU   B OE1   1 
ATOM   1626 O OE2   . GLU   A 1 238 ? 14.735  -32.466 91.123 1   40.03 ? 219 GLU   B OE2   1 
ATOM   1627 N N     . ALA   A 1 239 ? 8.547   -31.148 90.221 1   3     ? 220 ALA   B N     1 
ATOM   1628 C CA    . ALA   A 1 239 ? 7.17    -30.648 90.412 1   3     ? 220 ALA   B CA    1 
ATOM   1629 C C     . ALA   A 1 239 ? 6.328   -30.857 89.144 1   5.32  ? 220 ALA   B C     1 
ATOM   1630 O O     . ALA   A 1 239 ? 5.129   -31.179 89.244 1   3     ? 220 ALA   B O     1 
ATOM   1631 C CB    . ALA   A 1 239 ? 7.186   -29.173 90.811 1   3     ? 220 ALA   B CB    1 
ATOM   1632 N N     . VAL   A 1 240 ? 6.964   -30.692 87.955 1   3     ? 221 VAL   B N     1 
ATOM   1633 C CA    . VAL   A 1 240 ? 6.29    -30.893 86.663 1   3     ? 221 VAL   B CA    1 
ATOM   1634 C C     . VAL   A 1 240 ? 5.88    -32.375 86.558 1   5.55  ? 221 VAL   B C     1 
ATOM   1635 O O     . VAL   A 1 240 ? 4.701   -32.67  86.357 1   3     ? 221 VAL   B O     1 
ATOM   1636 C CB    . VAL   A 1 240 ? 7.154   -30.441 85.452 1   4.26  ? 221 VAL   B CB    1 
ATOM   1637 C CG1   . VAL   A 1 240 ? 6.465   -30.797 84.127 1   3     ? 221 VAL   B CG1   1 
ATOM   1638 C CG2   . VAL   A 1 240 ? 7.458   -28.938 85.518 1   3     ? 221 VAL   B CG2   1 
ATOM   1639 N N     . GLU   A 1 241 ? 6.85    -33.288 86.755 1   3     ? 222 GLU   B N     1 
ATOM   1640 C CA    . GLU   A 1 241 ? 6.621   -34.741 86.718 1   3.56  ? 222 GLU   B CA    1 
ATOM   1641 C C     . GLU   A 1 241 ? 5.515   -35.165 87.698 1   5.43  ? 222 GLU   B C     1 
ATOM   1642 O O     . GLU   A 1 241 ? 4.593   -35.876 87.295 1   3     ? 222 GLU   B O     1 
ATOM   1643 C CB    . GLU   A 1 241 ? 7.91    -35.509 87.033 1   5.52  ? 222 GLU   B CB    1 
ATOM   1644 C CG    . GLU   A 1 241 ? 8.885   -35.527 85.874 1   9.45  ? 222 GLU   B CG    1 
ATOM   1645 C CD    . GLU   A 1 241 ? 10.269  -36.014 86.262 1   35.54 ? 222 GLU   B CD    1 
ATOM   1646 O OE1   . GLU   A 1 241 ? 10.519  -37.236 86.151 1   49.37 ? 222 GLU   B OE1   1 
ATOM   1647 O OE2   . GLU   A 1 241 ? 11.105  -35.174 86.671 1   43.73 ? 222 GLU   B OE2   1 
ATOM   1648 N N     . ALA   A 1 242 ? 5.599   -34.704 88.967 1   3     ? 223 ALA   B N     1 
ATOM   1649 C CA    . ALA   A 1 242 ? 4.6     -35.028 89.995 1   3     ? 223 ALA   B CA    1 
ATOM   1650 C C     . ALA   A 1 242 ? 3.184   -34.544 89.598 1   5.67  ? 223 ALA   B C     1 
ATOM   1651 O O     . ALA   A 1 242 ? 2.224   -35.322 89.711 1   3     ? 223 ALA   B O     1 
ATOM   1652 C CB    . ALA   A 1 242 ? 5.012   -34.445 91.346 1   3.86  ? 223 ALA   B CB    1 
ATOM   1653 N N     . ALA   A 1 243 ? 3.059   -33.294 89.091 1   3     ? 224 ALA   B N     1 
ATOM   1654 C CA    . ALA   A 1 243 ? 1.767   -32.739 88.666 1   3     ? 224 ALA   B CA    1 
ATOM   1655 C C     . ALA   A 1 243 ? 1.126   -33.554 87.516 1   5.54  ? 224 ALA   B C     1 
ATOM   1656 O O     . ALA   A 1 243 ? -0.084  -33.814 87.544 1   3     ? 224 ALA   B O     1 
ATOM   1657 C CB    . ALA   A 1 243 ? 1.925   -31.275 88.259 1   3.25  ? 224 ALA   B CB    1 
ATOM   1658 N N     . VAL   A 1 244 ? 1.941   -33.973 86.528 1   3     ? 225 VAL   B N     1 
ATOM   1659 C CA    . VAL   A 1 244 ? 1.496   -34.767 85.378 1   3     ? 225 VAL   B CA    1 
ATOM   1660 C C     . VAL   A 1 244 ? 0.969   -36.142 85.877 1   5.88  ? 225 VAL   B C     1 
ATOM   1661 O O     . VAL   A 1 244 ? -0.109  -36.576 85.444 1   3     ? 225 VAL   B O     1 
ATOM   1662 C CB    . VAL   A 1 244 ? 2.629   -34.9   84.311 1   4.44  ? 225 VAL   B CB    1 
ATOM   1663 C CG1   . VAL   A 1 244 ? 2.279   -35.918 83.227 1   3     ? 225 VAL   B CG1   1 
ATOM   1664 C CG2   . VAL   A 1 244 ? 2.965   -33.543 83.678 1   3.26  ? 225 VAL   B CG2   1 
ATOM   1665 N N     . LYS   A 1 245 ? 1.705   -36.793 86.819 1   3     ? 226 LYS   B N     1 
ATOM   1666 C CA    . LYS   A 1 245 ? 1.25    -38.094 87.368 1   3     ? 226 LYS   B CA    1 
ATOM   1667 C C     . LYS   A 1 245 ? -0.022  -37.917 88.222 1   6.17  ? 226 LYS   B C     1 
ATOM   1668 O O     . LYS   A 1 245 ? -0.947  -38.732 88.121 1   3     ? 226 LYS   B O     1 
ATOM   1669 C CB    . LYS   A 1 245 ? 2.354   -38.772 88.184 1   3.28  ? 226 LYS   B CB    1 
ATOM   1670 C CG    . LYS   A 1 245 ? 3.56    -39.171 87.338 1   3.82  ? 226 LYS   B CG    1 
ATOM   1671 C CD    . LYS   A 1 245 ? 4.715   -39.616 88.238 1   11.39 ? 226 LYS   B CD    1 
ATOM   1672 C CE    . LYS   A 1 245 ? 6.041   -39.566 87.519 1   25.32 ? 226 LYS   B CE    1 
ATOM   1673 N NZ    . LYS   A 1 245 ? 6.218   -40.686 86.549 1   33.76 ? 226 LYS   B NZ    1 
ATOM   1674 N N     . GLU   A 1 246 ? -0.071  -36.837 89.039 1   3     ? 227 GLU   B N     1 
ATOM   1675 C CA    . GLU   A 1 246 ? -1.231  -36.519 89.878 1   3     ? 227 GLU   B CA    1 
ATOM   1676 C C     . GLU   A 1 246 ? -2.473  -36.277 88.995 1   6.59  ? 227 GLU   B C     1 
ATOM   1677 O O     . GLU   A 1 246 ? -3.58   -36.705 89.354 1   6.65  ? 227 GLU   B O     1 
ATOM   1678 C CB    . GLU   A 1 246 ? -0.936  -35.281 90.746 1   4.35  ? 227 GLU   B CB    1 
ATOM   1679 C CG    . GLU   A 1 246 ? -1.978  -35.008 91.831 1   7.77  ? 227 GLU   B CG    1 
ATOM   1680 C CD    . GLU   A 1 246 ? -1.652  -33.823 92.728 1   15.26 ? 227 GLU   B CD    1 
ATOM   1681 O OE1   . GLU   A 1 246 ? -0.454  -33.487 92.868 1   12.09 ? 227 GLU   B OE1   1 
ATOM   1682 O OE2   . GLU   A 1 246 ? -2.6    -33.219 93.28  1   12.47 ? 227 GLU   B OE2   1 
ATOM   1683 N N     . ALA   A 1 247 ? -2.277  -35.63  87.836 1   3     ? 228 ALA   B N     1 
ATOM   1684 C CA    . ALA   A 1 247 ? -3.347  -35.283 86.897 1   3     ? 228 ALA   B CA    1 
ATOM   1685 C C     . ALA   A 1 247 ? -3.899  -36.482 86.076 1   7.03  ? 228 ALA   B C     1 
ATOM   1686 O O     . ALA   A 1 247 ? -4.798  -36.287 85.247 1   6.28  ? 228 ALA   B O     1 
ATOM   1687 C CB    . ALA   A 1 247 ? -2.89   -34.159 85.976 1   3.24  ? 228 ALA   B CB    1 
ATOM   1688 N N     . GLY   A 1 248 ? -3.372  -37.693 86.317 1   3.22  ? 229 GLY   B N     1 
ATOM   1689 C CA    . GLY   A 1 248 ? -3.838  -38.904 85.636 1   3     ? 229 GLY   B CA    1 
ATOM   1690 C C     . GLY   A 1 248 ? -3.197  -39.266 84.309 1   5.1   ? 229 GLY   B C     1 
ATOM   1691 O O     . GLY   A 1 248 ? -3.87   -39.841 83.45  1   3     ? 229 GLY   B O     1 
ATOM   1692 N N     . TYR   A 1 249 ? -1.874  -38.995 84.151 1   3     ? 230 TYR   B N     1 
ATOM   1693 C CA    . TYR   A 1 249 ? -1.105  -39.363 82.947 1   3     ? 230 TYR   B CA    1 
ATOM   1694 C C     . TYR   A 1 249 ? 0.066   -40.267 83.306 1   5.49  ? 230 TYR   B C     1 
ATOM   1695 O O     . TYR   A 1 249 ? 0.468   -40.313 84.473 1   4.95  ? 230 TYR   B O     1 
ATOM   1696 C CB    . TYR   A 1 249 ? -0.5    -38.124 82.258 1   3     ? 230 TYR   B CB    1 
ATOM   1697 C CG    . TYR   A 1 249 ? -1.511  -37.09  81.82  1   3     ? 230 TYR   B CG    1 
ATOM   1698 C CD1   . TYR   A 1 249 ? -1.914  -36.074 82.68  1   3.96  ? 230 TYR   B CD1   1 
ATOM   1699 C CD2   . TYR   A 1 249 ? -2.011  -37.084 80.52  1   3.03  ? 230 TYR   B CD2   1 
ATOM   1700 C CE1   . TYR   A 1 249 ? -2.814  -35.097 82.271 1   3     ? 230 TYR   B CE1   1 
ATOM   1701 C CE2   . TYR   A 1 249 ? -2.916  -36.109 80.097 1   4.17  ? 230 TYR   B CE2   1 
ATOM   1702 C CZ    . TYR   A 1 249 ? -3.323  -35.122 80.979 1   6.7   ? 230 TYR   B CZ    1 
ATOM   1703 O OH    . TYR   A 1 249 ? -4.203  -34.148 80.564 1   3     ? 230 TYR   B OH    1 
ATOM   1704 N N     . THR   A 1 250 ? 0.632   -40.969 82.295 1   3     ? 231 THR   B N     1 
ATOM   1705 C CA    . THR   A 1 250 ? 1.879   -41.731 82.45  1   3     ? 231 THR   B CA    1 
ATOM   1706 C C     . THR   A 1 250 ? 2.893   -41.101 81.507 1   4.31  ? 231 THR   B C     1 
ATOM   1707 O O     . THR   A 1 250 ? 2.593   -40.907 80.331 1   3     ? 231 THR   B O     1 
ATOM   1708 C CB    . THR   A 1 250 ? 1.751   -43.228 82.16  1   9.63  ? 231 THR   B CB    1 
ATOM   1709 O OG1   . THR   A 1 250 ? 1.251   -43.418 80.83  1   11.07 ? 231 THR   B OG1   1 
ATOM   1710 C CG2   . THR   A 1 250 ? 0.885   -43.907 83.149 1   12.05 ? 231 THR   B CG2   1 
ATOM   1711 N N     . ILE   A 1 251 ? 4.077   -40.773 82.026 1   3     ? 232 ILE   B N     1 
ATOM   1712 C CA    . ILE   A 1 251 ? 5.134   -40.118 81.249 1   3     ? 232 ILE   B CA    1 
ATOM   1713 C C     . ILE   A 1 251 ? 5.883   -41.133 80.37  1   5.29  ? 232 ILE   B C     1 
ATOM   1714 O O     . ILE   A 1 251 ? 6.377   -42.14  80.886 1   3     ? 232 ILE   B O     1 
ATOM   1715 C CB    . ILE   A 1 251 ? 6.094   -39.317 82.187 1   5.17  ? 232 ILE   B CB    1 
ATOM   1716 C CG1   . ILE   A 1 251 ? 5.315   -38.204 82.965 1   4.8   ? 232 ILE   B CG1   1 
ATOM   1717 C CG2   . ILE   A 1 251 ? 7.294   -38.751 81.386 1   4.93  ? 232 ILE   B CG2   1 
ATOM   1718 C CD1   . ILE   A 1 251 ? 6.029   -37.626 84.257 1   5.95  ? 232 ILE   B CD1   1 
ATOM   1719 N N     . GLU   A 1 252 ? 5.988   -40.844 79.062 1   3     ? 233 GLU   B N     1 
ATOM   1720 C CA    . GLU   A 1 252 ? 6.708   -41.686 78.093 1   3.61  ? 233 GLU   B CA    1 
ATOM   1721 C C     . GLU   A 1 252 ? 8.193   -41.265 78.089 1   5.86  ? 233 GLU   B C     1 
ATOM   1722 O O     . GLU   A 1 252 ? 9.076   -42.115 78.138 1   3     ? 233 GLU   B O     1 
ATOM   1723 C CB    . GLU   A 1 252 ? 6.083   -41.571 76.683 1   6.11  ? 233 GLU   B CB    1 
ATOM   1724 C CG    . GLU   A 1 252 ? 4.635   -42.047 76.602 1   10.98 ? 233 GLU   B CG    1 
ATOM   1725 C CD    . GLU   A 1 252 ? 4.436   -43.437 76.038 1   39.65 ? 233 GLU   B CD    1 
ATOM   1726 O OE1   . GLU   A 1 252 ? 3.786   -44.265 76.715 1   54.14 ? 233 GLU   B OE1   1 
ATOM   1727 O OE2   . GLU   A 1 252 ? 4.92    -43.697 74.914 1   46.36 ? 233 GLU   B OE2   1 
ATOM   1728 N N     . TRP   A 1 253 ? 8.464   -39.954 78.045 1   3     ? 234 TRP   B N     1 
ATOM   1729 C CA    . TRP   A 1 253 ? 9.83    -39.418 78.117 1   5.77  ? 234 TRP   B CA    1 
ATOM   1730 C C     . TRP   A 1 253 ? 9.824   -37.992 78.634 1   6.01  ? 234 TRP   B C     1 
ATOM   1731 O O     . TRP   A 1 253 ? 8.808   -37.307 78.525 1   3     ? 234 TRP   B O     1 
ATOM   1732 C CB    . TRP   A 1 253 ? 10.625  -39.567 76.816 1   7.38  ? 234 TRP   B CB    1 
ATOM   1733 C CG    . TRP   A 1 253 ? 10.114  -38.802 75.636 1   10.74 ? 234 TRP   B CG    1 
ATOM   1734 C CD1   . TRP   A 1 253 ? 9.344   -39.294 74.621 1   7.67  ? 234 TRP   B CD1   1 
ATOM   1735 C CD2   . TRP   A 1 253 ? 10.494  -37.471 75.243 1   10.9  ? 234 TRP   B CD2   1 
ATOM   1736 N NE1   . TRP   A 1 253 ? 9.16    -38.33  73.655 1   8.15  ? 234 TRP   B NE1   1 
ATOM   1737 C CE2   . TRP   A 1 253 ? 9.844   -37.195 74.018 1   7.41  ? 234 TRP   B CE2   1 
ATOM   1738 C CE3   . TRP   A 1 253 ? 11.247  -36.449 75.851 1   9.36  ? 234 TRP   B CE3   1 
ATOM   1739 C CZ2   . TRP   A 1 253 ? 9.958   -35.954 73.369 1   7.64  ? 234 TRP   B CZ2   1 
ATOM   1740 C CZ3   . TRP   A 1 253 ? 11.37   -35.22  75.202 1   8.11  ? 234 TRP   B CZ3   1 
ATOM   1741 C CH2   . TRP   A 1 253 ? 10.732  -34.98  73.979 1   7.81  ? 234 TRP   B CH2   1 
ATOM   1742 N N     . PHE   A 1 254 ? 10.956  -37.567 79.214 1   3     ? 235 PHE   B N     1 
ATOM   1743 C CA    . PHE   A 1 254 ? 11.113  -36.249 79.817 1   3     ? 235 PHE   B CA    1 
ATOM   1744 C C     . PHE   A 1 254 ? 12.545  -35.785 79.521 1   5.65  ? 235 PHE   B C     1 
ATOM   1745 O O     . PHE   A 1 254 ? 13.491  -36.534 79.776 1   3     ? 235 PHE   B O     1 
ATOM   1746 C CB    . PHE   A 1 254 ? 10.869  -36.345 81.338 1   3     ? 235 PHE   B CB    1 
ATOM   1747 C CG    . PHE   A 1 254 ? 10.587  -35.014 81.993 1   3     ? 235 PHE   B CG    1 
ATOM   1748 C CD1   . PHE   A 1 254 ? 11.622  -34.135 82.289 1   3.48  ? 235 PHE   B CD1   1 
ATOM   1749 C CD2   . PHE   A 1 254 ? 9.285   -34.641 82.321 1   3     ? 235 PHE   B CD2   1 
ATOM   1750 C CE1   . PHE   A 1 254 ? 11.36   -32.891 82.88  1   4.16  ? 235 PHE   B CE1   1 
ATOM   1751 C CE2   . PHE   A 1 254 ? 9.025   -33.392 82.914 1   5.77  ? 235 PHE   B CE2   1 
ATOM   1752 C CZ    . PHE   A 1 254 ? 10.063  -32.523 83.165 1   3     ? 235 PHE   B CZ    1 
ATOM   1753 N N     . GLU   A 1 255 ? 12.678  -34.604 78.888 1   3     ? 236 GLU   B N     1 
ATOM   1754 C CA    . GLU   A 1 255 ? 13.967  -34.025 78.529 1   3     ? 236 GLU   B CA    1 
ATOM   1755 C C     . GLU   A 1 255 ? 14.127  -32.656 79.163 1   5.09  ? 236 GLU   B C     1 
ATOM   1756 O O     . GLU   A 1 255 ? 13.195  -31.864 79.162 1   3     ? 236 GLU   B O     1 
ATOM   1757 C CB    . GLU   A 1 255 ? 14.132  -33.884 76.997 1   3.13  ? 236 GLU   B CB    1 
ATOM   1758 C CG    . GLU   A 1 255 ? 15.509  -33.372 76.578 1   8.73  ? 236 GLU   B CG    1 
ATOM   1759 C CD    . GLU   A 1 255 ? 15.628  -32.867 75.152 1   12.51 ? 236 GLU   B CD    1 
ATOM   1760 O OE1   . GLU   A 1 255 ? 16.462  -33.417 74.397 1   18.23 ? 236 GLU   B OE1   1 
ATOM   1761 O OE2   . GLU   A 1 255 ? 14.893  -31.918 74.793 1   18.63 ? 236 GLU   B OE2   1 
ATOM   1762 N N     . VAL   A 1 256 ? 15.342  -32.36  79.64  1   3     ? 237 VAL   B N     1 
ATOM   1763 C CA    . VAL   A 1 256 ? 15.639  -31.049 80.189 1   3     ? 237 VAL   B CA    1 
ATOM   1764 C C     . VAL   A 1 256 ? 16.834  -30.524 79.397 1   5.61  ? 237 VAL   B C     1 
ATOM   1765 O O     . VAL   A 1 256 ? 17.782  -31.271 79.173 1   3     ? 237 VAL   B O     1 
ATOM   1766 C CB    . VAL   A 1 256 ? 15.926  -31.126 81.72  1   6.45  ? 237 VAL   B CB    1 
ATOM   1767 C CG1   . VAL   A 1 256 ? 16.56   -29.837 82.24  1   7.01  ? 237 VAL   B CG1   1 
ATOM   1768 C CG2   . VAL   A 1 256 ? 14.652  -31.445 82.5   1   6.13  ? 237 VAL   B CG2   1 
ATOM   1769 N N     . ILE   A 1 257 ? 16.754  -29.267 78.933 1   3     ? 238 ILE   B N     1 
ATOM   1770 C CA    . ILE   A 1 257 ? 17.874  -28.592 78.266 1   3     ? 238 ILE   B CA    1 
ATOM   1771 C C     . ILE   A 1 257 ? 18.327  -27.497 79.206 1   5.38  ? 238 ILE   B C     1 
ATOM   1772 O O     . ILE   A 1 257 ? 17.491  -26.902 79.892 1   3     ? 238 ILE   B O     1 
ATOM   1773 C CB    . ILE   A 1 257 ? 17.589  -28.094 76.824 1   5.67  ? 238 ILE   B CB    1 
ATOM   1774 C CG1   . ILE   A 1 257 ? 16.525  -26.963 76.787 1   5.99  ? 238 ILE   B CG1   1 
ATOM   1775 C CG2   . ILE   A 1 257 ? 17.166  -29.283 75.954 1   4.81  ? 238 ILE   B CG2   1 
ATOM   1776 C CD1   . ILE   A 1 257 ? 16.539  -26.132 75.49  1   8.6   ? 238 ILE   B CD1   1 
ATOM   1777 N N     A SER   A 1 258 ? 19.635  -27.243 79.266 0.5 3     ? 239 SER   B N     1 
ATOM   1778 N N     B SER   A 1 258 ? 19.641  -27.242 79.266 0.5 3     ? 239 SER   B N     1 
ATOM   1779 C CA    A SER   A 1 258 ? 20.197  -26.224 80.155 0.5 3     ? 239 SER   B CA    1 
ATOM   1780 C CA    B SER   A 1 258 ? 20.184  -26.229 80.172 0.5 3     ? 239 SER   B CA    1 
ATOM   1781 C C     A SER   A 1 258 ? 20.027  -24.806 79.599 0.5 5.76  ? 239 SER   B C     1 
ATOM   1782 C C     B SER   A 1 258 ? 20.109  -24.802 79.595 0.5 6.06  ? 239 SER   B C     1 
ATOM   1783 O O     A SER   A 1 258 ? 20.027  -23.846 80.374 0.5 4.16  ? 239 SER   B O     1 
ATOM   1784 O O     B SER   A 1 258 ? 20.211  -23.835 80.355 0.5 4.87  ? 239 SER   B O     1 
ATOM   1785 C CB    A SER   A 1 258 ? 21.681  -26.49  80.379 0.5 3.62  ? 239 SER   B CB    1 
ATOM   1786 C CB    B SER   A 1 258 ? 21.607  -26.591 80.589 0.5 5.04  ? 239 SER   B CB    1 
ATOM   1787 O OG    A SER   A 1 258 ? 22.299  -26.761 79.133 0.5 3     ? 239 SER   B OG    1 
ATOM   1788 O OG    B SER   A 1 258 ? 21.631  -27.907 81.124 0.5 5.02  ? 239 SER   B OG    1 
ATOM   1789 N N     . GLN   A 1 259 ? 19.91   -24.672 78.263 1   3     ? 240 GLN   B N     1 
ATOM   1790 C CA    . GLN   A 1 259 ? 19.811  -23.365 77.574 1   3     ? 240 GLN   B CA    1 
ATOM   1791 C C     . GLN   A 1 259 ? 18.681  -22.479 78.102 1   5.67  ? 240 GLN   B C     1 
ATOM   1792 O O     . GLN   A 1 259 ? 17.522  -22.892 78.088 1   3     ? 240 GLN   B O     1 
ATOM   1793 C CB    . GLN   A 1 259 ? 19.706  -23.56  76.048 1   3.13  ? 240 GLN   B CB    1 
ATOM   1794 C CG    . GLN   A 1 259 ? 19.638  -22.245 75.251 1   6.12  ? 240 GLN   B CG    1 
ATOM   1795 C CD    . GLN   A 1 259 ? 20.9    -21.413 75.296 1   9.58  ? 240 GLN   B CD    1 
ATOM   1796 O OE1   . GLN   A 1 259 ? 21.992  -21.85  74.889 1   11.68 ? 240 GLN   B OE1   1 
ATOM   1797 N NE2   . GLN   A 1 259 ? 20.775  -20.168 75.766 1   8.58  ? 240 GLN   B NE2   1 
ATOM   1798 N N     . SER   A 1 260 ? 19.04   -21.264 78.591 1   3     ? 241 SER   B N     1 
ATOM   1799 C CA    . SER   A 1 260 ? 18.073  -20.296 79.113 1   3     ? 241 SER   B CA    1 
ATOM   1800 C C     . SER   A 1 260 ? 17.866  -19.149 78.109 1   6.29  ? 241 SER   B C     1 
ATOM   1801 O O     . SER   A 1 260 ? 18.674  -18.983 77.189 1   3     ? 241 SER   B O     1 
ATOM   1802 C CB    . SER   A 1 260 ? 18.559  -19.749 80.451 1   6.19  ? 241 SER   B CB    1 
ATOM   1803 O OG    . SER   A 1 260 ? 18.534  -20.793 81.413 1   5.11  ? 241 SER   B OG    1 
ATOM   1804 N N     . TYR   A 1 261 ? 16.765  -18.368 78.267 1   3     ? 242 TYR   B N     1 
ATOM   1805 C CA    . TYR   A 1 261 ? 16.523  -17.216 77.39  1   3     ? 242 TYR   B CA    1 
ATOM   1806 C C     . TYR   A 1 261 ? 17.518  -16.119 77.784 1   7.88  ? 242 TYR   B C     1 
ATOM   1807 O O     . TYR   A 1 261 ? 18.084  -16.187 78.888 1   5.84  ? 242 TYR   B O     1 
ATOM   1808 C CB    . TYR   A 1 261 ? 15.07   -16.694 77.559 1   3     ? 242 TYR   B CB    1 
ATOM   1809 C CG    . TYR   A 1 261 ? 14.041  -17.59  76.903 1   3     ? 242 TYR   B CG    1 
ATOM   1810 C CD1   . TYR   A 1 261 ? 13.643  -17.38  75.587 1   3.89  ? 242 TYR   B CD1   1 
ATOM   1811 C CD2   . TYR   A 1 261 ? 13.503  -18.683 77.581 1   3     ? 242 TYR   B CD2   1 
ATOM   1812 C CE1   . TYR   A 1 261 ? 12.713  -18.22  74.967 1   3     ? 242 TYR   B CE1   1 
ATOM   1813 C CE2   . TYR   A 1 261 ? 12.583  -19.534 76.967 1   3     ? 242 TYR   B CE2   1 
ATOM   1814 C CZ    . TYR   A 1 261 ? 12.188  -19.296 75.663 1   4.83  ? 242 TYR   B CZ    1 
ATOM   1815 O OH    . TYR   A 1 261 ? 11.284  -20.138 75.056 1   3     ? 242 TYR   B OH    1 
ATOM   1816 N N     . SER   A 1 262 ? 17.702  -15.1   76.903 1   6.5   ? 243 SER   B N     1 
ATOM   1817 C CA    . SER   A 1 262 ? 18.603  -13.96  77.166 1   8.11  ? 243 SER   B CA    1 
ATOM   1818 C C     . SER   A 1 262 ? 18.223  -13.317 78.495 1   7.5   ? 243 SER   B C     1 
ATOM   1819 O O     . SER   A 1 262 ? 17.043  -13.365 78.88  1   9.29  ? 243 SER   B O     1 
ATOM   1820 C CB    . SER   A 1 262 ? 18.484  -12.921 76.059 1   8.7   ? 243 SER   B CB    1 
ATOM   1821 O OG    . SER   A 1 262 ? 18.928  -13.468 74.832 1   8.78  ? 243 SER   B OG    1 
ATOM   1822 N N     . SER   A 1 263 ? 19.214  -12.724 79.197 1   10.67 ? 244 SER   B N     1 
ATOM   1823 C CA    . SER   A 1 263 ? 19.026  -12.075 80.511 1   11.17 ? 244 SER   B CA    1 
ATOM   1824 C C     . SER   A 1 263 ? 17.955  -10.982 80.501 1   13.21 ? 244 SER   B C     1 
ATOM   1825 O O     . SER   A 1 263 ? 17.306  -10.746 81.519 1   13.59 ? 244 SER   B O     1 
ATOM   1826 C CB    . SER   A 1 263 ? 20.344  -11.479 81     1   14.05 ? 244 SER   B CB    1 
ATOM   1827 O OG    . SER   A 1 263 ? 20.757  -10.418 80.152 1   21.6  ? 244 SER   B OG    1 
ATOM   1828 N N     . THR   A 1 264 ? 17.779  -10.326 79.352 1   15.16 ? 245 THR   B N     1 
ATOM   1829 C CA    . THR   A 1 264 ? 16.82   -9.232  79.159 1   16.56 ? 245 THR   B CA    1 
ATOM   1830 C C     . THR   A 1 264 ? 15.358  -9.714  79.01  1   13.96 ? 245 THR   B C     1 
ATOM   1831 O O     . THR   A 1 264 ? 14.438  -8.884  79.028 1   15.91 ? 245 THR   B O     1 
ATOM   1832 C CB    . THR   A 1 264 ? 17.24   -8.399  77.93  1   23.38 ? 245 THR   B CB    1 
ATOM   1833 O OG1   . THR   A 1 264 ? 17.246  -9.245  76.772 1   22.4  ? 245 THR   B OG1   1 
ATOM   1834 C CG2   . THR   A 1 264 ? 18.605  -7.731  78.108 1   24.75 ? 245 THR   B CG2   1 
ATOM   1835 N N     . MET   A 1 265 ? 15.145  -11.041 78.829 1   10.62 ? 246 MET   B N     1 
ATOM   1836 C CA    . MET   A 1 265 ? 13.818  -11.623 78.582 1   9.5   ? 246 MET   B CA    1 
ATOM   1837 C C     . MET   A 1 265 ? 13.212  -12.354 79.78  1   8.69  ? 246 MET   B C     1 
ATOM   1838 O O     . MET   A 1 265 ? 12.023  -12.212 80.022 1   10.58 ? 246 MET   B O     1 
ATOM   1839 C CB    . MET   A 1 265 ? 13.839  -12.612 77.381 1   8.2   ? 246 MET   B CB    1 
ATOM   1840 C CG    . MET   A 1 265 ? 14.732  -12.211 76.223 1   12.7  ? 246 MET   B CG    1 
ATOM   1841 S SD    . MET   A 1 265 ? 14.171  -10.705 75.42  1   23.9  ? 246 MET   B SD    1 
ATOM   1842 C CE    . MET   A 1 265 ? 13.117  -11.378 74.192 1   21.81 ? 246 MET   B CE    1 
ATOM   1843 N N     . ALA   A 1 266 ? 13.996  -13.185 80.483 1   4.93  ? 247 ALA   B N     1 
ATOM   1844 C CA    . ALA   A 1 266 ? 13.481  -14.017 81.57  1   3.13  ? 247 ALA   B CA    1 
ATOM   1845 C C     . ALA   A 1 266 ? 14.589  -14.473 82.522 1   5.75  ? 247 ALA   B C     1 
ATOM   1846 O O     . ALA   A 1 266 ? 15.768  -14.196 82.273 1   5.34  ? 247 ALA   B O     1 
ATOM   1847 C CB    . ALA   A 1 266 ? 12.782  -15.24  80.969 1   3     ? 247 ALA   B CB    1 
ATOM   1848 N N     . ASN   A 1 267 ? 14.199  -15.181 83.605 1   3.18  ? 248 ASN   B N     1 
ATOM   1849 C CA    . ASN   A 1 267 ? 15.124  -15.71  84.613 1   3     ? 248 ASN   B CA    1 
ATOM   1850 C C     . ASN   A 1 267 ? 15.039  -17.247 84.686 1   6.27  ? 248 ASN   B C     1 
ATOM   1851 O O     . ASN   A 1 267 ? 15.251  -17.818 85.759 1   5.88  ? 248 ASN   B O     1 
ATOM   1852 C CB    . ASN   A 1 267 ? 14.828  -15.079 85.988 1   4.23  ? 248 ASN   B CB    1 
ATOM   1853 C CG    . ASN   A 1 267 ? 13.469  -15.409 86.598 1   10.7  ? 248 ASN   B CG    1 
ATOM   1854 O OD1   . ASN   A 1 267 ? 12.555  -15.941 85.943 1   13.97 ? 248 ASN   B OD1   1 
ATOM   1855 N ND2   . ASN   A 1 267 ? 13.311  -15.064 87.875 1   17.11 ? 248 ASN   B ND2   1 
ATOM   1856 N N     . ASN   A 1 268 ? 14.701  -17.916 83.559 1   3     ? 249 ASN   B N     1 
ATOM   1857 C CA    . ASN   A 1 268 ? 14.55   -19.376 83.577 1   3     ? 249 ASN   B CA    1 
ATOM   1858 C C     . ASN   A 1 268 ? 15.853  -20.135 83.699 1   6.11  ? 249 ASN   B C     1 
ATOM   1859 O O     . ASN   A 1 268 ? 16.907  -19.624 83.319 1   4.39  ? 249 ASN   B O     1 
ATOM   1860 C CB    . ASN   A 1 268 ? 13.77   -19.875 82.359 1   3     ? 249 ASN   B CB    1 
ATOM   1861 C CG    . ASN   A 1 268 ? 14.511  -19.76  81.047 1   5.64  ? 249 ASN   B CG    1 
ATOM   1862 O OD1   . ASN   A 1 268 ? 15.026  -18.693 80.685 1   3     ? 249 ASN   B OD1   1 
ATOM   1863 N ND2   . ASN   A 1 268 ? 14.565  -20.862 80.303 1   3     ? 249 ASN   B ND2   1 
ATOM   1864 N N     . GLU   A 1 269 ? 15.767  -21.37  84.217 1   3     ? 250 GLU   B N     1 
ATOM   1865 C CA    . GLU   A 1 269 ? 16.908  -22.273 84.313 1   3     ? 250 GLU   B CA    1 
ATOM   1866 C C     . GLU   A 1 269 ? 16.609  -23.451 83.367 1   5.44  ? 250 GLU   B C     1 
ATOM   1867 O O     . GLU   A 1 269 ? 16.288  -24.559 83.807 1   3     ? 250 GLU   B O     1 
ATOM   1868 C CB    . GLU   A 1 269 ? 17.13   -22.747 85.754 1   4.31  ? 250 GLU   B CB    1 
ATOM   1869 C CG    . GLU   A 1 269 ? 17.613  -21.649 86.692 1   8.74  ? 250 GLU   B CG    1 
ATOM   1870 C CD    . GLU   A 1 269 ? 17.925  -22.153 88.087 1   25.63 ? 250 GLU   B CD    1 
ATOM   1871 O OE1   . GLU   A 1 269 ? 17.302  -21.651 89.051 1   33.79 ? 250 GLU   B OE1   1 
ATOM   1872 O OE2   . GLU   A 1 269 ? 18.781  -23.061 88.215 1   33.72 ? 250 GLU   B OE2   1 
ATOM   1873 N N     . GLY   A 1 270 ? 16.687  -23.173 82.073 1   3     ? 251 GLY   B N     1 
ATOM   1874 C CA    . GLY   A 1 270 ? 16.441  -24.167 81.035 1   3     ? 251 GLY   B CA    1 
ATOM   1875 C C     . GLY   A 1 270 ? 14.981  -24.36  80.685 1   5.68  ? 251 GLY   B C     1 
ATOM   1876 O O     . GLY   A 1 270 ? 14.12   -23.545 81.042 1   3     ? 251 GLY   B O     1 
ATOM   1877 N N     . LEU   A 1 271 ? 14.706  -25.441 79.957 1   3     ? 252 LEU   B N     1 
ATOM   1878 C CA    . LEU   A 1 271 ? 13.352  -25.784 79.512 1   3     ? 252 LEU   B CA    1 
ATOM   1879 C C     . LEU   A 1 271 ? 13.176  -27.294 79.589 1   5.63  ? 252 LEU   B C     1 
ATOM   1880 O O     . LEU   A 1 271 ? 14.161  -28.032 79.59  1   3     ? 252 LEU   B O     1 
ATOM   1881 C CB    . LEU   A 1 271 ? 13.182  -25.362 78.037 1   3     ? 252 LEU   B CB    1 
ATOM   1882 C CG    . LEU   A 1 271 ? 12.944  -23.874 77.754 1   7.04  ? 252 LEU   B CG    1 
ATOM   1883 C CD1   . LEU   A 1 271 ? 14.273  -23.159 77.386 1   6.81  ? 252 LEU   B CD1   1 
ATOM   1884 C CD2   . LEU   A 1 271 ? 11.951  -23.709 76.623 1   3     ? 252 LEU   B CD2   1 
ATOM   1885 N N     . PHE   A 1 272 ? 11.923  -27.757 79.624 1   3     ? 253 PHE   B N     1 
ATOM   1886 C CA    . PHE   A 1 272 ? 11.676  -29.193 79.577 1   3     ? 253 PHE   B CA    1 
ATOM   1887 C C     . PHE   A 1 272 ? 10.766  -29.496 78.401 1   4.88  ? 253 PHE   B C     1 
ATOM   1888 O O     . PHE   A 1 272 ? 10.038  -28.621 77.916 1   3     ? 253 PHE   B O     1 
ATOM   1889 C CB    . PHE   A 1 272 ? 11.066  -29.733 80.883 1   3.09  ? 253 PHE   B CB    1 
ATOM   1890 C CG    . PHE   A 1 272 ? 9.641   -29.268 81.113 1   3     ? 253 PHE   B CG    1 
ATOM   1891 C CD1   . PHE   A 1 272 ? 8.563   -29.974 80.582 1   3.11  ? 253 PHE   B CD1   1 
ATOM   1892 C CD2   . PHE   A 1 272 ? 9.379   -28.109 81.842 1   3     ? 253 PHE   B CD2   1 
ATOM   1893 C CE1   . PHE   A 1 272 ? 7.25    -29.518 80.756 1   3     ? 253 PHE   B CE1   1 
ATOM   1894 C CE2   . PHE   A 1 272 ? 8.064   -27.675 82.053 1   5.29  ? 253 PHE   B CE2   1 
ATOM   1895 C CZ    . PHE   A 1 272 ? 7.008   -28.374 81.495 1   3     ? 253 PHE   B CZ    1 
ATOM   1896 N N     . SER   A 1 273 ? 10.749  -30.754 78.011 1   3     ? 254 SER   B N     1 
ATOM   1897 C CA    . SER   A 1 273 ? 9.856   -31.256 76.983 1   3     ? 254 SER   B CA    1 
ATOM   1898 C C     . SER   A 1 273 ? 9.408   -32.632 77.486 1   4.73  ? 254 SER   B C     1 
ATOM   1899 O O     . SER   A 1 273 ? 10.233  -33.388 78.016 1   3     ? 254 SER   B O     1 
ATOM   1900 C CB    . SER   A 1 273 ? 10.589  -31.357 75.647 1   8.38  ? 254 SER   B CB    1 
ATOM   1901 O OG    . SER   A 1 273 ? 9.801   -32.078 74.715 1   10.65 ? 254 SER   B OG    1 
ATOM   1902 N N     . LEU   A 1 274 ? 8.104   -32.92  77.406 1   3     ? 255 LEU   B N     1 
ATOM   1903 C CA    . LEU   A 1 274 ? 7.618   -34.232 77.838 1   3     ? 255 LEU   B CA    1 
ATOM   1904 C C     . LEU   A 1 274 ? 6.509   -34.742 76.923 1   4.53  ? 255 LEU   B C     1 
ATOM   1905 O O     . LEU   A 1 274 ? 5.781   -33.946 76.327 1   3     ? 255 LEU   B O     1 
ATOM   1906 C CB    . LEU   A 1 274 ? 7.154   -34.229 79.303 1   3     ? 255 LEU   B CB    1 
ATOM   1907 C CG    . LEU   A 1 274 ? 5.856   -33.463 79.666 1   5.15  ? 255 LEU   B CG    1 
ATOM   1908 C CD1   . LEU   A 1 274 ? 4.587   -34.34  79.519 1   5.74  ? 255 LEU   B CD1   1 
ATOM   1909 C CD2   . LEU   A 1 274 ? 5.906   -32.969 81.104 1   6.55  ? 255 LEU   B CD2   1 
ATOM   1910 N N     . VAL   A 1 275 ? 6.385   -36.07  76.841 1   3     ? 256 VAL   B N     1 
ATOM   1911 C CA    . VAL   A 1 275 ? 5.303   -36.743 76.118 1   3     ? 256 VAL   B CA    1 
ATOM   1912 C C     . VAL   A 1 275 ? 4.691   -37.683 77.136 1   4.77  ? 256 VAL   B C     1 
ATOM   1913 O O     . VAL   A 1 275 ? 5.401   -38.484 77.725 1   3     ? 256 VAL   B O     1 
ATOM   1914 C CB    . VAL   A 1 275 ? 5.74    -37.477 74.821 1   6.15  ? 256 VAL   B CB    1 
ATOM   1915 C CG1   . VAL   A 1 275 ? 4.571   -38.277 74.213 1   5.7   ? 256 VAL   B CG1   1 
ATOM   1916 C CG2   . VAL   A 1 275 ? 6.276   -36.479 73.807 1   5.55  ? 256 VAL   B CG2   1 
ATOM   1917 N N     . ALA   A 1 276 ? 3.38    -37.562 77.364 1   3     ? 257 ALA   B N     1 
ATOM   1918 C CA    . ALA   A 1 276 ? 2.684   -38.402 78.335 1   3     ? 257 ALA   B CA    1 
ATOM   1919 C C     . ALA   A 1 276 ? 1.403   -38.941 77.698 1   5.29  ? 257 ALA   B C     1 
ATOM   1920 O O     . ALA   A 1 276 ? 0.952   -38.392 76.69  1   3     ? 257 ALA   B O     1 
ATOM   1921 C CB    . ALA   A 1 276 ? 2.348   -37.582 79.573 1   3     ? 257 ALA   B CB    1 
ATOM   1922 N N     . ARG   A 1 277 ? 0.811   -39.992 78.29  1   3     ? 258 ARG   B N     1 
ATOM   1923 C CA    . ARG   A 1 277 ? -0.464  -40.531 77.792 1   3     ? 258 ARG   B CA    1 
ATOM   1924 C C     . ARG   A 1 277 ? -1.498  -40.486 78.899 1   5.27  ? 258 ARG   B C     1 
ATOM   1925 O O     . ARG   A 1 277 ? -1.169  -40.773 80.052 1   3     ? 258 ARG   B O     1 
ATOM   1926 C CB    . ARG   A 1 277 ? -0.319  -41.973 77.274 1   5.73  ? 258 ARG   B CB    1 
ATOM   1927 C CG    . ARG   A 1 277 ? 0.599   -42.079 76.053 1   11.52 ? 258 ARG   B CG    1 
ATOM   1928 C CD    . ARG   A 1 277 ? 0.554   -43.461 75.43  1   20.88 ? 258 ARG   B CD    1 
ATOM   1929 N NE    . ARG   A 1 277 ? -0.728  -43.719 74.767 1   35.4  ? 258 ARG   B NE    1 
ATOM   1930 C CZ    . ARG   A 1 277 ? -0.941  -44.731 73.929 1   50.57 ? 258 ARG   B CZ    1 
ATOM   1931 N NH1   . ARG   A 1 277 ? 0.041   -45.578 73.636 1   43.11 ? 258 ARG   B NH1   1 
ATOM   1932 N NH2   . ARG   A 1 277 ? -2.132  -44.897 73.37  1   42.05 ? 258 ARG   B NH2   1 
ATOM   1933 N N     . LYS   A 1 278 ? -2.752  -40.131 78.55  1   3     ? 259 LYS   B N     1 
ATOM   1934 C CA    . LYS   A 1 278 ? -3.836  -40.06  79.524 1   3     ? 259 LYS   B CA    1 
ATOM   1935 C C     . LYS   A 1 278 ? -4.238  -41.484 79.975 1   5.64  ? 259 LYS   B C     1 
ATOM   1936 O O     . LYS   A 1 278 ? -4.385  -42.376 79.139 1   3.56  ? 259 LYS   B O     1 
ATOM   1937 C CB    . LYS   A 1 278 ? -5.041  -39.319 78.903 1   3.62  ? 259 LYS   B CB    1 
ATOM   1938 C CG    . LYS   A 1 278 ? -6.19   -39.07  79.865 1   10.16 ? 259 LYS   B CG    1 
ATOM   1939 C CD    . LYS   A 1 278 ? -7.411  -38.637 79.098 1   9.91  ? 259 LYS   B CD    1 
ATOM   1940 C CE    . LYS   A 1 278 ? -8.613  -38.491 79.996 1   13.52 ? 259 LYS   B CE    1 
ATOM   1941 N NZ    . LYS   A 1 278 ? -9.779  -37.926 79.254 1   5.04  ? 259 LYS   B NZ    1 
ATOM   1942 N N     . LEU   A 1 279 ? -4.404  -41.69  81.293 1   3     ? 260 LEU   B N     1 
ATOM   1943 C CA    . LEU   A 1 279 ? -4.841  -42.984 81.828 1   21.44 ? 260 LEU   B CA    1 
ATOM   1944 C C     . LEU   A 1 279 ? -6.362  -43.168 81.722 1   46.79 ? 260 LEU   B C     1 
ATOM   1945 O O     . LEU   A 1 279 ? -7.111  -42.192 81.722 1   27.1  ? 260 LEU   B O     1 
ATOM   1946 C CB    . LEU   A 1 279 ? -4.364  -43.183 83.272 1   20.95 ? 260 LEU   B CB    1 
ATOM   1947 C CG    . LEU   A 1 279 ? -2.881  -43.483 83.44  1   21.93 ? 260 LEU   B CG    1 
ATOM   1948 C CD1   . LEU   A 1 279 ? -2.521  -43.555 84.884 1   21.93 ? 260 LEU   B CD1   1 
ATOM   1949 C CD2   . LEU   A 1 279 ? -2.506  -44.778 82.755 1   22.04 ? 260 LEU   B CD2   1 
ATOM   1950 N N     . PHE   B 1 24  ? 31.395  -57.855 91.352 1   8.23  ? 5   PHE   D N     1 
ATOM   1951 C CA    . PHE   B 1 24  ? 31.241  -57.215 90.043 1   8.89  ? 5   PHE   D CA    1 
ATOM   1952 C C     . PHE   B 1 24  ? 32.085  -57.932 88.972 1   8.49  ? 5   PHE   D C     1 
ATOM   1953 O O     . PHE   B 1 24  ? 33.237  -58.304 89.251 1   6.22  ? 5   PHE   D O     1 
ATOM   1954 C CB    . PHE   B 1 24  ? 31.615  -55.718 90.121 1   10.56 ? 5   PHE   D CB    1 
ATOM   1955 C CG    . PHE   B 1 24  ? 30.938  -54.857 89.066 1   9.3   ? 5   PHE   D CG    1 
ATOM   1956 C CD1   . PHE   B 1 24  ? 29.741  -54.201 89.341 1   7.63  ? 5   PHE   D CD1   1 
ATOM   1957 C CD2   . PHE   B 1 24  ? 31.52   -54.676 87.813 1   8.58  ? 5   PHE   D CD2   1 
ATOM   1958 C CE1   . PHE   B 1 24  ? 29.11   -53.402 88.362 1   7.66  ? 5   PHE   D CE1   1 
ATOM   1959 C CE2   . PHE   B 1 24  ? 30.889  -53.891 86.832 1   7.01  ? 5   PHE   D CE2   1 
ATOM   1960 C CZ    . PHE   B 1 24  ? 29.683  -53.269 87.109 1   9.5   ? 5   PHE   D CZ    1 
ATOM   1961 N N     . THR   B 1 25  ? 31.524  -58.131 87.756 1   3     ? 6   THR   D N     1 
ATOM   1962 C CA    . THR   B 1 25  ? 32.234  -58.775 86.633 1   3     ? 6   THR   D CA    1 
ATOM   1963 C C     . THR   B 1 25  ? 33.63   -58.113 86.383 1   5.78  ? 6   THR   D C     1 
ATOM   1964 O O     . THR   B 1 25  ? 33.708  -56.901 86.146 1   3     ? 6   THR   D O     1 
ATOM   1965 C CB    . THR   B 1 25  ? 31.357  -58.735 85.354 1   6.87  ? 6   THR   D CB    1 
ATOM   1966 O OG1   . THR   B 1 25  ? 30.073  -59.323 85.609 1   3     ? 6   THR   D OG1   1 
ATOM   1967 C CG2   . THR   B 1 25  ? 32.019  -59.418 84.166 1   3     ? 6   THR   D CG2   1 
ATOM   1968 N N     . SER   B 1 26  ? 34.722  -58.917 86.476 1   3     ? 7   SER   D N     1 
ATOM   1969 C CA    . SER   B 1 26  ? 36.079  -58.424 86.238 1   3     ? 7   SER   D CA    1 
ATOM   1970 C C     . SER   B 1 26  ? 36.251  -58.147 84.732 1   5.19  ? 7   SER   D C     1 
ATOM   1971 O O     . SER   B 1 26  ? 35.65   -58.848 83.913 1   3     ? 7   SER   D O     1 
ATOM   1972 C CB    . SER   B 1 26  ? 37.102  -59.454 86.712 1   8.45  ? 7   SER   D CB    1 
ATOM   1973 O OG    . SER   B 1 26  ? 36.981  -60.657 85.966 1   9.7   ? 7   SER   D OG    1 
ATOM   1974 N N     . LYS   B 1 27  ? 37.072  -57.141 84.355 1   3.96  ? 8   LYS   D N     1 
ATOM   1975 C CA    . LYS   B 1 27  ? 37.235  -56.804 82.932 1   3     ? 8   LYS   D CA    1 
ATOM   1976 C C     . LYS   B 1 27  ? 37.768  -57.983 82.085 1   5.25  ? 8   LYS   D C     1 
ATOM   1977 O O     . LYS   B 1 27  ? 37.325  -58.13  80.946 1   3     ? 8   LYS   D O     1 
ATOM   1978 C CB    . LYS   B 1 27  ? 38.036  -55.507 82.695 1   5.47  ? 8   LYS   D CB    1 
ATOM   1979 C CG    . LYS   B 1 27  ? 39.481  -55.466 83.204 1   8.5   ? 8   LYS   D CG    1 
ATOM   1980 C CD    . LYS   B 1 27  ? 39.91   -53.999 83.377 1   9.73  ? 8   LYS   D CD    1 
ATOM   1981 C CE    . LYS   B 1 27  ? 41.357  -53.817 83.781 1   17.09 ? 8   LYS   D CE    1 
ATOM   1982 N NZ    . LYS   B 1 27  ? 41.635  -52.414 84.197 1   20.98 ? 8   LYS   D NZ    1 
ATOM   1983 N N     . ASP   B 1 28  ? 38.608  -58.88  82.656 1   3.09  ? 9   ASP   D N     1 
ATOM   1984 C CA    . ASP   B 1 28  ? 39.091  -60.041 81.885 1   4.62  ? 9   ASP   D CA    1 
ATOM   1985 C C     . ASP   B 1 28  ? 37.942  -60.978 81.43  1   7.11  ? 9   ASP   D C     1 
ATOM   1986 O O     . ASP   B 1 28  ? 38.105  -61.73  80.451 1   5.54  ? 9   ASP   D O     1 
ATOM   1987 C CB    . ASP   B 1 28  ? 40.19   -60.805 82.635 1   8.74  ? 9   ASP   D CB    1 
ATOM   1988 C CG    . ASP   B 1 28  ? 39.715  -61.436 83.926 1   18.52 ? 9   ASP   D CG    1 
ATOM   1989 O OD1   . ASP   B 1 28  ? 39.575  -62.685 83.962 1   29.63 ? 9   ASP   D OD1   1 
ATOM   1990 O OD2   . ASP   B 1 28  ? 39.487  -60.687 84.904 1   25.89 ? 9   ASP   D OD2   1 
ATOM   1991 N N     . THR   B 1 29  ? 36.765  -60.899 82.105 1   3     ? 10  THR   D N     1 
ATOM   1992 C CA    . THR   B 1 29  ? 35.572  -61.692 81.749 1   3     ? 10  THR   D CA    1 
ATOM   1993 C C     . THR   B 1 29  ? 35.053  -61.249 80.385 1   5.85  ? 10  THR   D C     1 
ATOM   1994 O O     . THR   B 1 29  ? 34.526  -62.067 79.635 1   4.39  ? 10  THR   D O     1 
ATOM   1995 C CB    . THR   B 1 29  ? 34.503  -61.625 82.874 1   6.95  ? 10  THR   D CB    1 
ATOM   1996 O OG1   . THR   B 1 29  ? 35.131  -62.034 84.089 1   8.99  ? 10  THR   D OG1   1 
ATOM   1997 C CG2   . THR   B 1 29  ? 33.247  -62.509 82.594 1   8.74  ? 10  THR   D CG2   1 
ATOM   1998 N N     . TYR   B 1 30  ? 35.234  -59.95  80.048 1   3     ? 11  TYR   D N     1 
ATOM   1999 C CA    . TYR   B 1 30  ? 34.818  -59.45  78.748 1   3     ? 11  TYR   D CA    1 
ATOM   2000 C C     . TYR   B 1 30  ? 35.631  -60.041 77.633 1   5.97  ? 11  TYR   D C     1 
ATOM   2001 O O     . TYR   B 1 30  ? 35.081  -60.296 76.577 1   6.45  ? 11  TYR   D O     1 
ATOM   2002 C CB    . TYR   B 1 30  ? 34.818  -57.914 78.716 1   3     ? 11  TYR   D CB    1 
ATOM   2003 C CG    . TYR   B 1 30  ? 33.539  -57.397 79.328 1   3     ? 11  TYR   D CG    1 
ATOM   2004 C CD1   . TYR   B 1 30  ? 33.468  -57.084 80.686 1   3.84  ? 11  TYR   D CD1   1 
ATOM   2005 C CD2   . TYR   B 1 30  ? 32.367  -57.333 78.581 1   3     ? 11  TYR   D CD2   1 
ATOM   2006 C CE1   . TYR   B 1 30  ? 32.271  -56.656 81.267 1   3     ? 11  TYR   D CE1   1 
ATOM   2007 C CE2   . TYR   B 1 30  ? 31.168  -56.91  79.149 1   3     ? 11  TYR   D CE2   1 
ATOM   2008 C CZ    . TYR   B 1 30  ? 31.126  -56.56  80.488 1   5.16  ? 11  TYR   D CZ    1 
ATOM   2009 O OH    . TYR   B 1 30  ? 29.934  -56.148 81.016 1   3     ? 11  TYR   D OH    1 
ATOM   2010 N N     . LEU   B 1 31  ? 36.919  -60.297 77.877 1   3     ? 12  LEU   D N     1 
ATOM   2011 C CA    . LEU   B 1 31  ? 37.823  -60.855 76.872 1   3     ? 12  LEU   D CA    1 
ATOM   2012 C C     . LEU   B 1 31  ? 37.428  -62.271 76.44  1   7.14  ? 12  LEU   D C     1 
ATOM   2013 O O     . LEU   B 1 31  ? 37.472  -62.584 75.246 1   6.06  ? 12  LEU   D O     1 
ATOM   2014 C CB    . LEU   B 1 31  ? 39.267  -60.854 77.405 1   3.03  ? 12  LEU   D CB    1 
ATOM   2015 C CG    . LEU   B 1 31  ? 39.876  -59.506 77.776 1   7.2   ? 12  LEU   D CG    1 
ATOM   2016 C CD1   . LEU   B 1 31  ? 41.3    -59.696 78.308 1   5.15  ? 12  LEU   D CD1   1 
ATOM   2017 C CD2   . LEU   B 1 31  ? 39.909  -58.553 76.559 1   6.86  ? 12  LEU   D CD2   1 
ATOM   2018 N N     . SER   B 1 32  ? 37.017  -63.107 77.414 1   3     ? 13  SER   D N     1 
ATOM   2019 C CA    . SER   B 1 32  ? 36.691  -64.512 77.217 1   3.53  ? 13  SER   D CA    1 
ATOM   2020 C C     . SER   B 1 32  ? 35.205  -64.884 77.146 1   6.68  ? 13  SER   D C     1 
ATOM   2021 O O     . SER   B 1 32  ? 34.862  -65.781 76.37  1   7.14  ? 13  SER   D O     1 
ATOM   2022 C CB    . SER   B 1 32  ? 37.345  -65.327 78.327 1   8.66  ? 13  SER   D CB    1 
ATOM   2023 O OG    . SER   B 1 32  ? 36.992  -64.797 79.6   1   9.46  ? 13  SER   D OG    1 
ATOM   2024 N N     . HIS   B 1 33  ? 34.335  -64.25  77.975 1   3     ? 14  HIS   D N     1 
ATOM   2025 C CA    . HIS   B 1 33  ? 32.925  -64.665 78.11  1   3     ? 14  HIS   D CA    1 
ATOM   2026 C C     . HIS   B 1 33  ? 31.868  -63.806 77.43  1   5.36  ? 14  HIS   D C     1 
ATOM   2027 O O     . HIS   B 1 33  ? 30.697  -64.211 77.413 1   3     ? 14  HIS   D O     1 
ATOM   2028 C CB    . HIS   B 1 33  ? 32.576  -64.826 79.585 1   3.46  ? 14  HIS   D CB    1 
ATOM   2029 C CG    . HIS   B 1 33  ? 33.268  -65.997 80.2   1   7.28  ? 14  HIS   D CG    1 
ATOM   2030 N ND1   . HIS   B 1 33  ? 34.646  -66.026 80.336 1   6.66  ? 14  HIS   D ND1   1 
ATOM   2031 C CD2   . HIS   B 1 33  ? 32.757  -67.159 80.67  1   9.06  ? 14  HIS   D CD2   1 
ATOM   2032 C CE1   . HIS   B 1 33  ? 34.927  -67.189 80.901 1   9.02  ? 14  HIS   D CE1   1 
ATOM   2033 N NE2   . HIS   B 1 33  ? 33.824  -67.91  81.106 1   9.88  ? 14  HIS   D NE2   1 
ATOM   2034 N N     . PHE   B 1 34  ? 32.255  -62.66  76.856 1   3     ? 15  PHE   D N     1 
ATOM   2035 C CA    . PHE   B 1 34  ? 31.301  -61.824 76.114 1   3     ? 15  PHE   D CA    1 
ATOM   2036 C C     . PHE   B 1 34  ? 31.316  -62.361 74.681 1   5.11  ? 15  PHE   D C     1 
ATOM   2037 O O     . PHE   B 1 34  ? 32.332  -62.184 73.989 1   3     ? 15  PHE   D O     1 
ATOM   2038 C CB    . PHE   B 1 34  ? 31.735  -60.351 76.127 1   3     ? 15  PHE   D CB    1 
ATOM   2039 C CG    . PHE   B 1 34  ? 30.71   -59.377 75.582 1   3     ? 15  PHE   D CG    1 
ATOM   2040 C CD1   . PHE   B 1 34  ? 30.565  -59.186 74.211 1   4.65  ? 15  PHE   D CD1   1 
ATOM   2041 C CD2   . PHE   B 1 34  ? 29.938  -58.602 76.442 1   3     ? 15  PHE   D CD2   1 
ATOM   2042 C CE1   . PHE   B 1 34  ? 29.631  -58.267 73.712 1   4.36  ? 15  PHE   D CE1   1 
ATOM   2043 C CE2   . PHE   B 1 34  ? 29.04   -57.654 75.944 1   5.2   ? 15  PHE   D CE2   1 
ATOM   2044 C CZ    . PHE   B 1 34  ? 28.894  -57.491 74.584 1   3     ? 15  PHE   D CZ    1 
ATOM   2045 N N     . ASN   B 1 35  ? 30.235  -63.063 74.26  1   3     ? 16  ASN   D N     1 
ATOM   2046 C CA    . ASN   B 1 35  ? 30.137  -63.636 72.901 1   3     ? 16  ASN   D CA    1 
ATOM   2047 C C     . ASN   B 1 35  ? 29.534  -62.58  71.952 1   3.98  ? 16  ASN   D C     1 
ATOM   2048 O O     . ASN   B 1 35  ? 28.326  -62.326 72.042 1   3     ? 16  ASN   D O     1 
ATOM   2049 C CB    . ASN   B 1 35  ? 29.305  -64.938 72.898 1   4.56  ? 16  ASN   D CB    1 
ATOM   2050 C CG    . ASN   B 1 35  ? 29.305  -65.663 71.566 1   16.84 ? 16  ASN   D CG    1 
ATOM   2051 O OD1   . ASN   B 1 35  ? 29.091  -65.075 70.498 1   12.02 ? 16  ASN   D OD1   1 
ATOM   2052 N ND2   . ASN   B 1 35  ? 29.536  -66.965 71.599 1   19.56 ? 16  ASN   D ND2   1 
ATOM   2053 N N     . PRO   B 1 36  ? 30.333  -61.985 71.029 1   3     ? 17  PRO   D N     1 
ATOM   2054 C CA    . PRO   B 1 36  ? 29.794  -60.906 70.169 1   3     ? 17  PRO   D CA    1 
ATOM   2055 C C     . PRO   B 1 36  ? 28.607  -61.301 69.307 1   5.74  ? 17  PRO   D C     1 
ATOM   2056 O O     . PRO   B 1 36  ? 27.618  -60.57  69.259 1   3.71  ? 17  PRO   D O     1 
ATOM   2057 C CB    . PRO   B 1 36  ? 31.004  -60.458 69.326 1   3.7   ? 17  PRO   D CB    1 
ATOM   2058 C CG    . PRO   B 1 36  ? 31.989  -61.556 69.427 1   7.05  ? 17  PRO   D CG    1 
ATOM   2059 C CD    . PRO   B 1 36  ? 31.784  -62.159 70.802 1   3.17  ? 17  PRO   D CD    1 
ATOM   2060 N N     . ARG   B 1 37  ? 28.691  -62.472 68.655 1   3.38  ? 18  ARG   D N     1 
ATOM   2061 C CA    . ARG   B 1 37  ? 27.634  -62.981 67.791 1   4.95  ? 18  ARG   D CA    1 
ATOM   2062 C C     . ARG   B 1 37  ? 26.334  -63.189 68.576 1   7.7   ? 18  ARG   D C     1 
ATOM   2063 O O     . ARG   B 1 37  ? 25.271  -62.785 68.101 1   7.61  ? 18  ARG   D O     1 
ATOM   2064 C CB    . ARG   B 1 37  ? 28.085  -64.276 67.082 1   10.76 ? 18  ARG   D CB    1 
ATOM   2065 C CG    . ARG   B 1 37  ? 29.246  -64.073 66.103 1   19.59 ? 18  ARG   D CG    1 
ATOM   2066 C CD    . ARG   B 1 37  ? 29.753  -65.411 65.57  1   31.59 ? 18  ARG   D CD    1 
ATOM   2067 N NE    . ARG   B 1 37  ? 30.531  -65.271 64.336 1   54.67 ? 18  ARG   D NE    1 
ATOM   2068 C CZ    . ARG   B 1 37  ? 31.168  -66.274 63.735 1   76.9  ? 18  ARG   D CZ    1 
ATOM   2069 N NH1   . ARG   B 1 37  ? 31.837  -66.064 62.61  1   63.92 ? 18  ARG   D NH1   1 
ATOM   2070 N NH2   . ARG   B 1 37  ? 31.145  -67.495 64.259 1   68.88 ? 18  ARG   D NH2   1 
ATOM   2071 N N     . ASP   B 1 38  ? 26.424  -63.777 69.786 1   5.68  ? 19  ASP   D N     1 
ATOM   2072 C CA    . ASP   B 1 38  ? 25.268  -64.027 70.654 1   7.14  ? 19  ASP   D CA    1 
ATOM   2073 C C     . ASP   B 1 38  ? 24.662  -62.701 71.138 1   7.64  ? 19  ASP   D C     1 
ATOM   2074 O O     . ASP   B 1 38  ? 23.439  -62.551 71.163 1   5.73  ? 19  ASP   D O     1 
ATOM   2075 C CB    . ASP   B 1 38  ? 25.664  -64.907 71.855 1   11.51 ? 19  ASP   D CB    1 
ATOM   2076 C CG    . ASP   B 1 38  ? 24.503  -65.692 72.44  1   25.76 ? 19  ASP   D CG    1 
ATOM   2077 O OD1   . ASP   B 1 38  ? 23.58   -66.059 71.666 1   30.23 ? 19  ASP   D OD1   1 
ATOM   2078 O OD2   . ASP   B 1 38  ? 24.51   -65.94  73.677 1   35.24 ? 19  ASP   D OD2   1 
ATOM   2079 N N     . TYR   B 1 39  ? 25.526  -61.726 71.47  1   3     ? 20  TYR   D N     1 
ATOM   2080 C CA    . TYR   B 1 39  ? 25.076  -60.389 71.899 1   3     ? 20  TYR   D CA    1 
ATOM   2081 C C     . TYR   B 1 39  ? 24.241  -59.713 70.788 1   4.57  ? 20  TYR   D C     1 
ATOM   2082 O O     . TYR   B 1 39  ? 23.143  -59.22  71.052 1   3     ? 20  TYR   D O     1 
ATOM   2083 C CB    . TYR   B 1 39  ? 26.295  -59.539 72.27  1   3     ? 20  TYR   D CB    1 
ATOM   2084 C CG    . TYR   B 1 39  ? 25.953  -58.136 72.718 1   3     ? 20  TYR   D CG    1 
ATOM   2085 C CD1   . TYR   B 1 39  ? 25.357  -57.902 73.96  1   4.61  ? 20  TYR   D CD1   1 
ATOM   2086 C CD2   . TYR   B 1 39  ? 26.288  -57.034 71.936 1   3     ? 20  TYR   D CD2   1 
ATOM   2087 C CE1   . TYR   B 1 39  ? 25.074  -56.605 74.394 1   3     ? 20  TYR   D CE1   1 
ATOM   2088 C CE2   . TYR   B 1 39  ? 26.011  -55.736 72.359 1   3     ? 20  TYR   D CE2   1 
ATOM   2089 C CZ    . TYR   B 1 39  ? 25.42   -55.525 73.596 1   6.65  ? 20  TYR   D CZ    1 
ATOM   2090 O OH    . TYR   B 1 39  ? 25.177  -54.237 74.024 1   3     ? 20  TYR   D OH    1 
ATOM   2091 N N     . LEU   B 1 40  ? 24.75   -59.747 69.544 1   3     ? 21  LEU   D N     1 
ATOM   2092 C CA    . LEU   B 1 40  ? 24.078  -59.166 68.376 1   3.27  ? 21  LEU   D CA    1 
ATOM   2093 C C     . LEU   B 1 40  ? 22.742  -59.869 68.093 1   7.08  ? 21  LEU   D C     1 
ATOM   2094 O O     . LEU   B 1 40  ? 21.748  -59.203 67.789 1   5.68  ? 21  LEU   D O     1 
ATOM   2095 C CB    . LEU   B 1 40  ? 24.992  -59.233 67.138 1   3.44  ? 21  LEU   D CB    1 
ATOM   2096 C CG    . LEU   B 1 40  ? 26.29   -58.421 67.217 1   7.31  ? 21  LEU   D CG    1 
ATOM   2097 C CD1   . LEU   B 1 40  ? 27.178  -58.688 66.02  1   7.36  ? 21  LEU   D CD1   1 
ATOM   2098 C CD2   . LEU   B 1 40  ? 26.005  -56.939 67.372 1   6.49  ? 21  LEU   D CD2   1 
ATOM   2099 N N     . GLU   B 1 41  ? 22.714  -61.206 68.25  1   6.66  ? 22  GLU   D N     1 
ATOM   2100 C CA    . GLU   B 1 41  ? 21.499  -62.006 68.026 1   8.92  ? 22  GLU   D CA    1 
ATOM   2101 C C     . GLU   B 1 41  ? 20.413  -61.671 69.044 1   11.28 ? 22  GLU   D C     1 
ATOM   2102 O O     . GLU   B 1 41  ? 19.241  -61.535 68.68  1   10.13 ? 22  GLU   D O     1 
ATOM   2103 C CB    . GLU   B 1 41  ? 21.822  -63.512 68.076 1   12.68 ? 22  GLU   D CB    1 
ATOM   2104 C CG    . GLU   B 1 41  ? 22.491  -64.052 66.82  1   21.35 ? 22  GLU   D CG    1 
ATOM   2105 C CD    . GLU   B 1 41  ? 21.714  -63.918 65.524 1   45.11 ? 22  GLU   D CD    1 
ATOM   2106 O OE1   . GLU   B 1 41  ? 22.332  -63.54  64.502 1   50.84 ? 22  GLU   D OE1   1 
ATOM   2107 O OE2   . GLU   B 1 41  ? 20.491  -64.186 65.528 1   46.88 ? 22  GLU   D OE2   1 
ATOM   2108 N N     . LYS   B 1 42  ? 20.82   -61.511 70.317 1   7.31  ? 23  LYS   D N     1 
ATOM   2109 C CA    . LYS   B 1 42  ? 19.92   -61.25  71.437 1   7.66  ? 23  LYS   D CA    1 
ATOM   2110 C C     . LYS   B 1 42  ? 19.353  -59.84  71.498 1   8.7   ? 23  LYS   D C     1 
ATOM   2111 O O     . LYS   B 1 42  ? 18.207  -59.667 71.91  1   6.41  ? 23  LYS   D O     1 
ATOM   2112 C CB    . LYS   B 1 42  ? 20.604  -61.599 72.768 1   10.49 ? 23  LYS   D CB    1 
ATOM   2113 C CG    . LYS   B 1 42  ? 20.129  -62.927 73.346 1   29.47 ? 23  LYS   D CG    1 
ATOM   2114 C CD    . LYS   B 1 42  ? 20.971  -64.116 72.903 1   38.46 ? 23  LYS   D CD    1 
ATOM   2115 C CE    . LYS   B 1 42  ? 20.382  -65.409 73.409 1   49.45 ? 23  LYS   D CE    1 
ATOM   2116 N NZ    . LYS   B 1 42  ? 21.129  -66.587 72.899 1   57.66 ? 23  LYS   D NZ    1 
ATOM   2117 N N     . TYR   B 1 43  ? 20.139  -58.833 71.111 1   4.3   ? 24  TYR   D N     1 
ATOM   2118 C CA    . TYR   B 1 43  ? 19.704  -57.448 71.245 1   3.16  ? 24  TYR   D CA    1 
ATOM   2119 C C     . TYR   B 1 43  ? 19.528  -56.656 69.949 1   6.49  ? 24  TYR   D C     1 
ATOM   2120 O O     . TYR   B 1 43  ? 18.806  -55.65  69.959 1   4.81  ? 24  TYR   D O     1 
ATOM   2121 C CB    . TYR   B 1 43  ? 20.707  -56.699 72.163 1   3     ? 24  TYR   D CB    1 
ATOM   2122 C CG    . TYR   B 1 43  ? 20.685  -57.134 73.609 1   3     ? 24  TYR   D CG    1 
ATOM   2123 C CD1   . TYR   B 1 43  ? 19.755  -56.6   74.506 1   3     ? 24  TYR   D CD1   1 
ATOM   2124 C CD2   . TYR   B 1 43  ? 21.612  -58.055 74.094 1   3     ? 24  TYR   D CD2   1 
ATOM   2125 C CE1   . TYR   B 1 43  ? 19.755  -56.967 75.851 1   3     ? 24  TYR   D CE1   1 
ATOM   2126 C CE2   . TYR   B 1 43  ? 21.602  -58.453 75.431 1   3     ? 24  TYR   D CE2   1 
ATOM   2127 C CZ    . TYR   B 1 43  ? 20.674  -57.903 76.309 1   4.79  ? 24  TYR   D CZ    1 
ATOM   2128 O OH    . TYR   B 1 43  ? 20.642  -58.261 77.64  1   3     ? 24  TYR   D OH    1 
ATOM   2129 N N     . TYR   B 1 44  ? 20.223  -57.046 68.861 1   4.1   ? 25  TYR   D N     1 
ATOM   2130 C CA    . TYR   B 1 44  ? 20.221  -56.234 67.642 1   4.32  ? 25  TYR   D CA    1 
ATOM   2131 C C     . TYR   B 1 44  ? 19.742  -56.953 66.365 1   11.21 ? 25  TYR   D C     1 
ATOM   2132 O O     . TYR   B 1 44  ? 19.95   -56.423 65.274 1   11.12 ? 25  TYR   D O     1 
ATOM   2133 C CB    . TYR   B 1 44  ? 21.618  -55.61  67.449 1   3     ? 25  TYR   D CB    1 
ATOM   2134 C CG    . TYR   B 1 44  ? 21.986  -54.704 68.613 1   3     ? 25  TYR   D CG    1 
ATOM   2135 C CD1   . TYR   B 1 44  ? 21.428  -53.438 68.738 1   4.42  ? 25  TYR   D CD1   1 
ATOM   2136 C CD2   . TYR   B 1 44  ? 22.828  -55.146 69.63  1   3     ? 25  TYR   D CD2   1 
ATOM   2137 C CE1   . TYR   B 1 44  ? 21.696  -52.63  69.847 1   3     ? 25  TYR   D CE1   1 
ATOM   2138 C CE2   . TYR   B 1 44  ? 23.133  -54.332 70.727 1   3     ? 25  TYR   D CE2   1 
ATOM   2139 C CZ    . TYR   B 1 44  ? 22.552  -53.078 70.837 1   4.05  ? 25  TYR   D CZ    1 
ATOM   2140 O OH    . TYR   B 1 44  ? 22.821  -52.268 71.916 1   3     ? 25  TYR   D OH    1 
ATOM   2141 N N     . LYS   B 1 45  ? 19.005  -58.073 66.494 1   13.64 ? 26  LYS   D N     1 
ATOM   2142 C CA    . LYS   B 1 45  ? 18.487  -58.775 65.301 1   16.01 ? 26  LYS   D CA    1 
ATOM   2143 C C     . LYS   B 1 45  ? 17.393  -57.937 64.584 1   21.03 ? 26  LYS   D C     1 
ATOM   2144 O O     . LYS   B 1 45  ? 17.2    -58.078 63.366 1   23.43 ? 26  LYS   D O     1 
ATOM   2145 C CB    . LYS   B 1 45  ? 17.992  -60.192 65.649 1   19.37 ? 26  LYS   D CB    1 
ATOM   2146 C CG    . LYS   B 1 45  ? 18.294  -61.207 64.547 1   32.27 ? 26  LYS   D CG    1 
ATOM   2147 C CD    . LYS   B 1 45  ? 17.638  -62.56  64.785 1   42.48 ? 26  LYS   D CD    1 
ATOM   2148 C CE    . LYS   B 1 45  ? 17.901  -63.472 63.607 1   61.08 ? 26  LYS   D CE    1 
ATOM   2149 N NZ    . LYS   B 1 45  ? 17.466  -64.872 63.864 1   74.6  ? 26  LYS   D NZ    1 
ATOM   2150 N N     . PHE   B 1 46  ? 16.703  -57.06  65.355 1   19.25 ? 27  PHE   D N     1 
ATOM   2151 C CA    . PHE   B 1 46  ? 15.678  -56.103 64.923 1   27.42 ? 27  PHE   D CA    1 
ATOM   2152 C C     . PHE   B 1 46  ? 14.511  -56.761 64.155 1   49.7  ? 27  PHE   D C     1 
ATOM   2153 O O     . PHE   B 1 46  ? 14.342  -56.549 62.957 1   26.22 ? 27  PHE   D O     1 
ATOM   2154 C CB    . PHE   B 1 46  ? 16.335  -54.945 64.126 1   28.68 ? 27  PHE   D CB    1 
ATOM   2155 C CG    . PHE   B 1 46  ? 15.641  -53.6   64.151 1   30.09 ? 27  PHE   D CG    1 
ATOM   2156 C CD1   . PHE   B 1 46  ? 15.078  -53.108 65.326 1   31.26 ? 27  PHE   D CD1   1 
ATOM   2157 C CD2   . PHE   B 1 46  ? 15.625  -52.789 63.022 1   33.97 ? 27  PHE   D CD2   1 
ATOM   2158 C CE1   . PHE   B 1 46  ? 14.47   -51.852 65.354 1   32.54 ? 27  PHE   D CE1   1 
ATOM   2159 C CE2   . PHE   B 1 46  ? 15.015  -51.533 63.05  1   36.68 ? 27  PHE   D CE2   1 
ATOM   2160 C CZ    . PHE   B 1 46  ? 14.437  -51.075 64.214 1   34.01 ? 27  PHE   D CZ    1 
ATOM   2161 N N     . GLU   B 1 53  ? 13.474  -55.076 73.249 1   4.85  ? 34  GLU   D N     1 
ATOM   2162 C CA    . GLU   B 1 53  ? 14.826  -54.848 72.712 1   3.9   ? 34  GLU   D CA    1 
ATOM   2163 C C     . GLU   B 1 53  ? 14.773  -53.999 71.434 1   6.2   ? 34  GLU   D C     1 
ATOM   2164 O O     . GLU   B 1 53  ? 15.624  -53.132 71.254 1   4.04  ? 34  GLU   D O     1 
ATOM   2165 C CB    . GLU   B 1 53  ? 15.542  -56.19  72.455 1   5.94  ? 34  GLU   D CB    1 
ATOM   2166 C CG    . GLU   B 1 53  ? 16.014  -56.899 73.722 1   9.85  ? 34  GLU   D CG    1 
ATOM   2167 C CD    . GLU   B 1 53  ? 14.95   -57.129 74.796 1   19.13 ? 34  GLU   D CD    1 
ATOM   2168 O OE1   . GLU   B 1 53  ? 13.908  -57.748 74.474 1   11.43 ? 34  GLU   D OE1   1 
ATOM   2169 O OE2   . GLU   B 1 53  ? 15.13   -56.648 75.941 1   13.9  ? 34  GLU   D OE2   1 
ATOM   2170 N N     . SER   B 1 54  ? 13.761  -54.233 70.556 1   5.97  ? 35  SER   D N     1 
ATOM   2171 C CA    . SER   B 1 54  ? 13.605  -53.46  69.313 1   6.55  ? 35  SER   D CA    1 
ATOM   2172 C C     . SER   B 1 54  ? 13.083  -52.052 69.568 1   7.47  ? 35  SER   D C     1 
ATOM   2173 O O     . SER   B 1 54  ? 13.473  -51.121 68.851 1   4.97  ? 35  SER   D O     1 
ATOM   2174 C CB    . SER   B 1 54  ? 12.72   -54.204 68.316 1   12.36 ? 35  SER   D CB    1 
ATOM   2175 O OG    . SER   B 1 54  ? 13.416  -55.364 67.881 1   17.88 ? 35  SER   D OG    1 
ATOM   2176 N N     . GLN   B 1 55  ? 12.2    -51.883 70.582 1   5.12  ? 36  GLN   D N     1 
ATOM   2177 C CA    . GLN   B 1 55  ? 11.656  -50.566 70.955 1   4.02  ? 36  GLN   D CA    1 
ATOM   2178 C C     . GLN   B 1 55  ? 12.793  -49.668 71.452 1   5.31  ? 36  GLN   D C     1 
ATOM   2179 O O     . GLN   B 1 55  ? 12.857  -48.484 71.102 1   3     ? 36  GLN   D O     1 
ATOM   2180 C CB    . GLN   B 1 55  ? 10.575  -50.705 72.048 1   5.2   ? 36  GLN   D CB    1 
ATOM   2181 C CG    . GLN   B 1 55  ? 9.265   -51.341 71.538 1   15.78 ? 36  GLN   D CG    1 
ATOM   2182 C CD    . GLN   B 1 55  ? 8.548   -50.44  70.555 1   42.32 ? 36  GLN   D CD    1 
ATOM   2183 O OE1   . GLN   B 1 55  ? 8.609   -50.645 69.338 1   45.26 ? 36  GLN   D OE1   1 
ATOM   2184 N NE2   . GLN   B 1 55  ? 7.872   -49.409 71.06  1   36.69 ? 36  GLN   D NE2   1 
ATOM   2185 N N     . ILE   B 1 56  ? 13.723  -50.257 72.232 1   3     ? 37  ILE   D N     1 
ATOM   2186 C CA    . ILE   B 1 56  ? 14.88   -49.517 72.753 1   3     ? 37  ILE   D CA    1 
ATOM   2187 C C     . ILE   B 1 56  ? 15.817  -49.114 71.608 1   4.39  ? 37  ILE   D C     1 
ATOM   2188 O O     . ILE   B 1 56  ? 16.209  -47.951 71.533 1   3     ? 37  ILE   D O     1 
ATOM   2189 C CB    . ILE   B 1 56  ? 15.586  -50.292 73.888 1   4.56  ? 37  ILE   D CB    1 
ATOM   2190 C CG1   . ILE   B 1 56  ? 14.678  -50.316 75.139 1   3     ? 37  ILE   D CG1   1 
ATOM   2191 C CG2   . ILE   B 1 56  ? 16.972  -49.67  74.223 1   3.74  ? 37  ILE   D CG2   1 
ATOM   2192 C CD1   . ILE   B 1 56  ? 14.963  -51.374 76.107 1   6.29  ? 37  ILE   D CD1   1 
ATOM   2193 N N     . LEU   B 1 57  ? 16.135  -50.064 70.708 1   3     ? 38  LEU   D N     1 
ATOM   2194 C CA    . LEU   B 1 57  ? 16.997  -49.822 69.55  1   3     ? 38  LEU   D CA    1 
ATOM   2195 C C     . LEU   B 1 57  ? 16.442  -48.676 68.695 1   5.23  ? 38  LEU   D C     1 
ATOM   2196 O O     . LEU   B 1 57  ? 17.203  -47.798 68.31  1   3     ? 38  LEU   D O     1 
ATOM   2197 C CB    . LEU   B 1 57  ? 17.173  -51.109 68.712 1   3     ? 38  LEU   D CB    1 
ATOM   2198 C CG    . LEU   B 1 57  ? 18.109  -51.02  67.482 1   7     ? 38  LEU   D CG    1 
ATOM   2199 C CD1   . LEU   B 1 57  ? 19.481  -50.403 67.838 1   6.4   ? 38  LEU   D CD1   1 
ATOM   2200 C CD2   . LEU   B 1 57  ? 18.306  -52.39  66.86  1   7.77  ? 38  LEU   D CD2   1 
ATOM   2201 N N     . LYS   B 1 58  ? 15.107  -48.661 68.447 1   3     ? 39  LYS   D N     1 
ATOM   2202 C CA    . LYS   B 1 58  ? 14.454  -47.592 67.677 1   3     ? 39  LYS   D CA    1 
ATOM   2203 C C     . LYS   B 1 58  ? 14.667  -46.248 68.384 1   9.33  ? 39  LYS   D C     1 
ATOM   2204 O O     . LYS   B 1 58  ? 15.09   -45.275 67.745 1   5.82  ? 39  LYS   D O     1 
ATOM   2205 C CB    . LYS   B 1 58  ? 12.947  -47.886 67.527 1   4.87  ? 39  LYS   D CB    1 
ATOM   2206 C CG    . LYS   B 1 58  ? 12.642  -48.983 66.519 1   11.23 ? 39  LYS   D CG    1 
ATOM   2207 C CD    . LYS   B 1 58  ? 11.166  -49.375 66.52  1   14.64 ? 39  LYS   D CD    1 
ATOM   2208 C CE    . LYS   B 1 58  ? 10.95   -50.643 65.73  1   30.45 ? 39  LYS   D CE    1 
ATOM   2209 N NZ    . LYS   B 1 58  ? 9.547   -51.125 65.855 1   36.85 ? 39  LYS   D NZ    1 
ATOM   2210 N N     . HIS   B 1 59  ? 14.434  -46.211 69.726 1   10.74 ? 40  HIS   D N     1 
ATOM   2211 C CA    . HIS   B 1 59  ? 14.638  -44.988 70.49  1   14.42 ? 40  HIS   D CA    1 
ATOM   2212 C C     . HIS   B 1 59  ? 16.087  -44.51  70.423 1   9.15  ? 40  HIS   D C     1 
ATOM   2213 O O     . HIS   B 1 59  ? 16.308  -43.336 70.16  1   6.01  ? 40  HIS   D O     1 
ATOM   2214 C CB    . HIS   B 1 59  ? 14.181  -45.104 71.94  1   13.9  ? 40  HIS   D CB    1 
ATOM   2215 C CG    . HIS   B 1 59  ? 13.894  -43.752 72.515 1   10.38 ? 40  HIS   D CG    1 
ATOM   2216 N ND1   . HIS   B 1 59  ? 12.645  -43.146 72.36  1   11.41 ? 40  HIS   D ND1   1 
ATOM   2217 C CD2   . HIS   B 1 59  ? 14.724  -42.887 73.136 1   10.22 ? 40  HIS   D CD2   1 
ATOM   2218 C CE1   . HIS   B 1 59  ? 12.753  -41.949 72.917 1   11.28 ? 40  HIS   D CE1   1 
ATOM   2219 N NE2   . HIS   B 1 59  ? 13.987  -41.741 73.394 1   10.59 ? 40  HIS   D NE2   1 
ATOM   2220 N N     . LEU   B 1 60  ? 17.064  -45.416 70.607 1   3     ? 41  LEU   D N     1 
ATOM   2221 C CA    . LEU   B 1 60  ? 18.485  -45.028 70.528 1   3     ? 41  LEU   D CA    1 
ATOM   2222 C C     . LEU   B 1 60  ? 18.803  -44.402 69.157 1   4.94  ? 41  LEU   D C     1 
ATOM   2223 O O     . LEU   B 1 60  ? 19.401  -43.337 69.102 1   3     ? 41  LEU   D O     1 
ATOM   2224 C CB    . LEU   B 1 60  ? 19.425  -46.218 70.824 1   3     ? 41  LEU   D CB    1 
ATOM   2225 C CG    . LEU   B 1 60  ? 19.36   -46.792 72.259 1   6.49  ? 41  LEU   D CG    1 
ATOM   2226 C CD1   . LEU   B 1 60  ? 20.122  -48.092 72.359 1   4.95  ? 41  LEU   D CD1   1 
ATOM   2227 C CD2   . LEU   B 1 60  ? 19.864  -45.772 73.304 1   6.04  ? 41  LEU   D CD2   1 
ATOM   2228 N N     . LEU   B 1 61  ? 18.317  -45.027 68.07  1   3     ? 42  LEU   D N     1 
ATOM   2229 C CA    . LEU   B 1 61  ? 18.524  -44.535 66.702 1   3     ? 42  LEU   D CA    1 
ATOM   2230 C C     . LEU   B 1 61  ? 17.917  -43.14  66.473 1   4.87  ? 42  LEU   D C     1 
ATOM   2231 O O     . LEU   B 1 61  ? 18.583  -42.274 65.897 1   3.02  ? 42  LEU   D O     1 
ATOM   2232 C CB    . LEU   B 1 61  ? 18.021  -45.575 65.675 1   3     ? 42  LEU   D CB    1 
ATOM   2233 C CG    . LEU   B 1 61  ? 18.825  -46.895 65.622 1   6.44  ? 42  LEU   D CG    1 
ATOM   2234 C CD1   . LEU   B 1 61  ? 18.089  -47.974 64.83  1   5.77  ? 42  LEU   D CD1   1 
ATOM   2235 C CD2   . LEU   B 1 61  ? 20.266  -46.686 65.104 1   6.87  ? 42  LEU   D CD2   1 
ATOM   2236 N N     . LYS   B 1 62  ? 16.687  -42.893 66.99  1   3     ? 43  LYS   D N     1 
ATOM   2237 C CA    . LYS   B 1 62  ? 16.035  -41.58  66.88  1   3     ? 43  LYS   D CA    1 
ATOM   2238 C C     . LYS   B 1 62  ? 16.861  -40.522 67.614 1   5.85  ? 43  LYS   D C     1 
ATOM   2239 O O     . LYS   B 1 62  ? 17.12   -39.454 67.049 1   3.62  ? 43  LYS   D O     1 
ATOM   2240 C CB    . LYS   B 1 62  ? 14.607  -41.603 67.446 1   5.7   ? 43  LYS   D CB    1 
ATOM   2241 C CG    . LYS   B 1 62  ? 13.621  -42.483 66.688 1   14.57 ? 43  LYS   D CG    1 
ATOM   2242 C CD    . LYS   B 1 62  ? 12.317  -42.518 67.484 1   25.89 ? 43  LYS   D CD    1 
ATOM   2243 C CE    . LYS   B 1 62  ? 11.428  -43.677 67.145 1   37.86 ? 43  LYS   D CE    1 
ATOM   2244 N NZ    . LYS   B 1 62  ? 10.294  -43.784 68.101 1   42    ? 43  LYS   D NZ    1 
ATOM   2245 N N     . ASN   B 1 63  ? 17.341  -40.849 68.844 1   3     ? 44  ASN   D N     1 
ATOM   2246 C CA    . ASN   B 1 63  ? 18.167  -39.917 69.629 1   3.05  ? 44  ASN   D CA    1 
ATOM   2247 C C     . ASN   B 1 63  ? 19.499  -39.606 68.964 1   4.97  ? 44  ASN   D C     1 
ATOM   2248 O O     . ASN   B 1 63  ? 19.889  -38.44  68.92  1   3     ? 44  ASN   D O     1 
ATOM   2249 C CB    . ASN   B 1 63  ? 18.388  -40.422 71.05  1   9.27  ? 44  ASN   D CB    1 
ATOM   2250 C CG    . ASN   B 1 63  ? 17.281  -40.06  72.012 1   24.5  ? 44  ASN   D CG    1 
ATOM   2251 O OD1   . ASN   B 1 63  ? 16.453  -39.171 71.759 1   27.59 ? 44  ASN   D OD1   1 
ATOM   2252 N ND2   . ASN   B 1 63  ? 17.256  -40.732 73.152 1   23.91 ? 44  ASN   D ND2   1 
ATOM   2253 N N     . LEU   B 1 64  ? 20.175  -40.628 68.41  1   3     ? 45  LEU   D N     1 
ATOM   2254 C CA    . LEU   B 1 64  ? 21.456  -40.418 67.723 1   3     ? 45  LEU   D CA    1 
ATOM   2255 C C     . LEU   B 1 64  ? 21.251  -39.587 66.443 1   5.63  ? 45  LEU   D C     1 
ATOM   2256 O O     . LEU   B 1 64  ? 22.088  -38.746 66.125 1   3.3   ? 45  LEU   D O     1 
ATOM   2257 C CB    . LEU   B 1 64  ? 22.143  -41.751 67.403 1   3     ? 45  LEU   D CB    1 
ATOM   2258 C CG    . LEU   B 1 64  ? 22.614  -42.57  68.618 1   5.06  ? 45  LEU   D CG    1 
ATOM   2259 C CD1   . LEU   B 1 64  ? 22.57   -44.055 68.309 1   3.69  ? 45  LEU   D CD1   1 
ATOM   2260 C CD2   . LEU   B 1 64  ? 24.01   -42.115 69.101 1   4.04  ? 45  LEU   D CD2   1 
ATOM   2261 N N     . PHE   B 1 65  ? 20.112  -39.798 65.739 1   3.91  ? 46  PHE   D N     1 
ATOM   2262 C CA    . PHE   B 1 65  ? 19.777  -39.009 64.542 1   5.54  ? 46  PHE   D CA    1 
ATOM   2263 C C     . PHE   B 1 65  ? 19.581  -37.552 64.96  1   7.77  ? 46  PHE   D C     1 
ATOM   2264 O O     . PHE   B 1 65  ? 20.167  -36.658 64.343 1   7.36  ? 46  PHE   D O     1 
ATOM   2265 C CB    . PHE   B 1 65  ? 18.527  -39.557 63.829 1   9.32  ? 46  PHE   D CB    1 
ATOM   2266 C CG    . PHE   B 1 65  ? 17.931  -38.632 62.783 1   8.27  ? 46  PHE   D CG    1 
ATOM   2267 C CD1   . PHE   B 1 65  ? 18.65   -38.288 61.644 1   10.78 ? 46  PHE   D CD1   1 
ATOM   2268 C CD2   . PHE   B 1 65  ? 16.654  -38.104 62.943 1   9.99  ? 46  PHE   D CD2   1 
ATOM   2269 C CE1   . PHE   B 1 65  ? 18.096  -37.436 60.673 1   13.45 ? 46  PHE   D CE1   1 
ATOM   2270 C CE2   . PHE   B 1 65  ? 16.103  -37.255 61.973 1   13.39 ? 46  PHE   D CE2   1 
ATOM   2271 C CZ    . PHE   B 1 65  ? 16.828  -36.926 60.845 1   13.85 ? 46  PHE   D CZ    1 
ATOM   2272 N N     . LYS   B 1 66  ? 18.811  -37.32  66.049 1   3.68  ? 47  LYS   D N     1 
ATOM   2273 C CA    . LYS   B 1 66  ? 18.561  -35.972 66.571 1   3.98  ? 47  LYS   D CA    1 
ATOM   2274 C C     . LYS   B 1 66  ? 19.875  -35.245 66.916 1   7.15  ? 47  LYS   D C     1 
ATOM   2275 O O     . LYS   B 1 66  ? 20.069  -34.099 66.491 1   6.67  ? 47  LYS   D O     1 
ATOM   2276 C CB    . LYS   B 1 66  ? 17.637  -36.035 67.803 1   6.36  ? 47  LYS   D CB    1 
ATOM   2277 C CG    . LYS   B 1 66  ? 17.242  -34.675 68.365 1   11.18 ? 47  LYS   D CG    1 
ATOM   2278 C CD    . LYS   B 1 66  ? 16.191  -34.813 69.463 1   14.45 ? 47  LYS   D CD    1 
ATOM   2279 C CE    . LYS   B 1 66  ? 16.479  -33.87  70.61  1   16.87 ? 47  LYS   D CE    1 
ATOM   2280 N NZ    . LYS   B 1 66  ? 15.83   -34.334 71.857 1   18.66 ? 47  LYS   D NZ    1 
ATOM   2281 N N     . ILE   B 1 67  ? 20.772  -35.918 67.672 1   3.6   ? 48  ILE   D N     1 
ATOM   2282 C CA    . ILE   B 1 67  ? 22.066  -35.361 68.107 1   3     ? 48  ILE   D CA    1 
ATOM   2283 C C     . ILE   B 1 67  ? 23.022  -35.008 66.96  1   8.82  ? 48  ILE   D C     1 
ATOM   2284 O O     . ILE   B 1 67  ? 23.631  -33.935 66.995 1   9.12  ? 48  ILE   D O     1 
ATOM   2285 C CB    . ILE   B 1 67  ? 22.758  -36.337 69.111 1   4.95  ? 48  ILE   D CB    1 
ATOM   2286 C CG1   . ILE   B 1 67  ? 21.953  -36.434 70.414 1   4.4   ? 48  ILE   D CG1   1 
ATOM   2287 C CG2   . ILE   B 1 67  ? 24.231  -35.934 69.386 1   3.83  ? 48  ILE   D CG2   1 
ATOM   2288 C CD1   . ILE   B 1 67  ? 22.317  -37.648 71.306 1   7.08  ? 48  ILE   D CD1   1 
ATOM   2289 N N     . PHE   B 1 68  ? 23.228  -35.94  66.016 1   11.6  ? 49  PHE   D N     1 
ATOM   2290 C CA    . PHE   B 1 68  ? 24.213  -35.752 64.946 1   12.34 ? 49  PHE   D CA    1 
ATOM   2291 C C     . PHE   B 1 68  ? 23.684  -35.102 63.665 1   7.97  ? 49  PHE   D C     1 
ATOM   2292 O O     . PHE   B 1 68  ? 24.423  -34.338 63.031 1   10.97 ? 49  PHE   D O     1 
ATOM   2293 C CB    . PHE   B 1 68  ? 24.927  -37.078 64.609 1   11.75 ? 49  PHE   D CB    1 
ATOM   2294 C CG    . PHE   B 1 68  ? 25.706  -37.664 65.766 1   11.9  ? 49  PHE   D CG    1 
ATOM   2295 C CD1   . PHE   B 1 68  ? 26.767  -36.964 66.341 1   9.91  ? 49  PHE   D CD1   1 
ATOM   2296 C CD2   . PHE   B 1 68  ? 25.384  -38.914 66.275 1   11.34 ? 49  PHE   D CD2   1 
ATOM   2297 C CE1   . PHE   B 1 68  ? 27.476  -37.498 67.427 1   9.2   ? 49  PHE   D CE1   1 
ATOM   2298 C CE2   . PHE   B 1 68  ? 26.081  -39.443 67.37  1   8.7   ? 49  PHE   D CE2   1 
ATOM   2299 C CZ    . PHE   B 1 68  ? 27.128  -38.735 67.932 1   10.26 ? 49  PHE   D CZ    1 
ATOM   2300 N N     . CYS   B 1 69  ? 22.439  -35.394 63.273 1   11.29 ? 50  CYS   D N     1 
ATOM   2301 C CA    . CYS   B 1 69  ? 21.949  -34.839 62.01  1   17.5  ? 50  CYS   D CA    1 
ATOM   2302 C C     . CYS   B 1 69  ? 21.039  -33.612 62.16  1   25.43 ? 50  CYS   D C     1 
ATOM   2303 O O     . CYS   B 1 69  ? 20.948  -32.825 61.208 1   29.96 ? 50  CYS   D O     1 
ATOM   2304 C CB    . CYS   B 1 69  ? 21.301  -35.925 61.162 1   22.28 ? 50  CYS   D CB    1 
ATOM   2305 S SG    . CYS   B 1 69  ? 22.438  -37.263 60.691 1   26.52 ? 50  CYS   D SG    1 
ATOM   2306 N N     . LEU   B 1 70  ? 20.39   -33.428 63.327 1   20.3  ? 51  LEU   D N     1 
ATOM   2307 C CA    . LEU   B 1 70  ? 19.522  -32.265 63.534 1   40.38 ? 51  LEU   D CA    1 
ATOM   2308 C C     . LEU   B 1 70  ? 20.195  -31.208 64.401 1   93.91 ? 51  LEU   D C     1 
ATOM   2309 O O     . LEU   B 1 70  ? 20.342  -30.065 63.965 1   68.23 ? 51  LEU   D O     1 
ATOM   2310 C CB    . LEU   B 1 70  ? 18.153  -32.656 64.116 1   39.76 ? 51  LEU   D CB    1 
ATOM   2311 C CG    . LEU   B 1 70  ? 17.358  -33.764 63.407 1   46.79 ? 51  LEU   D CG    1 
ATOM   2312 C CD1   . LEU   B 1 70  ? 16.121  -34.117 64.193 1   47.46 ? 51  LEU   D CD1   1 
ATOM   2313 C CD2   . LEU   B 1 70  ? 16.964  -33.37  61.981 1   51.04 ? 51  LEU   D CD2   1 
ATOM   2314 N N     . GLY   B 1 72  ? 23.491  -31.318 64.238 1   34.5  ? 53  GLY   D N     1 
ATOM   2315 C CA    . GLY   B 1 72  ? 23.921  -30.513 65.375 1   32.86 ? 53  GLY   D CA    1 
ATOM   2316 C C     . GLY   B 1 72  ? 25.365  -30.744 65.779 1   30.98 ? 53  GLY   D C     1 
ATOM   2317 O O     . GLY   B 1 72  ? 26.189  -29.839 65.648 1   35.11 ? 53  GLY   D O     1 
ATOM   2318 N N     . VAL   B 1 73  ? 25.674  -31.948 66.309 1   17.97 ? 54  VAL   D N     1 
ATOM   2319 C CA    . VAL   B 1 73  ? 27.03   -32.327 66.746 1   16.12 ? 54  VAL   D CA    1 
ATOM   2320 C C     . VAL   B 1 73  ? 27.793  -32.829 65.507 1   16.78 ? 54  VAL   D C     1 
ATOM   2321 O O     . VAL   B 1 73  ? 27.345  -33.759 64.831 1   16.73 ? 54  VAL   D O     1 
ATOM   2322 C CB    . VAL   B 1 73  ? 27.016  -33.345 67.929 1   15.34 ? 54  VAL   D CB    1 
ATOM   2323 C CG1   . VAL   B 1 73  ? 28.436  -33.748 68.338 1   14.54 ? 54  VAL   D CG1   1 
ATOM   2324 C CG2   . VAL   B 1 73  ? 26.254  -32.779 69.137 1   14.21 ? 54  VAL   D CG2   1 
ATOM   2325 N N     . LYS   B 1 74  ? 28.889  -32.137 65.164 1   14.65 ? 55  LYS   D N     1 
ATOM   2326 C CA    . LYS   B 1 74  ? 29.73   -32.443 63.994 1   15.22 ? 55  LYS   D CA    1 
ATOM   2327 C C     . LYS   B 1 74  ? 31.216  -32.115 64.288 1   13.69 ? 55  LYS   D C     1 
ATOM   2328 O O     . LYS   B 1 74  ? 31.507  -31.414 65.262 1   14.61 ? 55  LYS   D O     1 
ATOM   2329 C CB    . LYS   B 1 74  ? 29.217  -31.679 62.754 1   19.66 ? 55  LYS   D CB    1 
ATOM   2330 C CG    . LYS   B 1 74  ? 29.431  -30.169 62.827 1   39.4  ? 55  LYS   D CG    1 
ATOM   2331 C CD    . LYS   B 1 74  ? 28.228  -29.388 63.358 1   48.55 ? 55  LYS   D CD    1 
ATOM   2332 C CE    . LYS   B 1 74  ? 28.647  -28.18  64.171 1   57.4  ? 55  LYS   D CE    1 
ATOM   2333 N NZ    . LYS   B 1 74  ? 27.487  -27.498 64.808 1   61.22 ? 55  LYS   D NZ    1 
ATOM   2334 N N     . GLY   B 1 75  ? 32.122  -32.616 63.444 1   12.5  ? 56  GLY   D N     1 
ATOM   2335 C CA    . GLY   B 1 75  ? 33.555  -32.385 63.579 1   13.5  ? 56  GLY   D CA    1 
ATOM   2336 C C     . GLY   B 1 75  ? 34.372  -33.241 62.641 1   11.39 ? 56  GLY   D C     1 
ATOM   2337 O O     . GLY   B 1 75  ? 33.831  -33.92  61.762 1   10.96 ? 56  GLY   D O     1 
ATOM   2338 N N     . ASP   B 1 76  ? 35.683  -33.203 62.824 1   7.33  ? 57  ASP   D N     1 
ATOM   2339 C CA    . ASP   B 1 76  ? 36.595  -34.001 62.019 1   7.77  ? 57  ASP   D CA    1 
ATOM   2340 C C     . ASP   B 1 76  ? 36.764  -35.391 62.615 1   7.98  ? 57  ASP   D C     1 
ATOM   2341 O O     . ASP   B 1 76  ? 36.995  -36.345 61.867 1   7.78  ? 57  ASP   D O     1 
ATOM   2342 C CB    . ASP   B 1 76  ? 37.966  -33.315 61.929 1   10.49 ? 57  ASP   D CB    1 
ATOM   2343 C CG    . ASP   B 1 76  ? 38.005  -32.152 60.949 1   21.35 ? 57  ASP   D CG    1 
ATOM   2344 O OD1   . ASP   B 1 76  ? 36.978  -31.912 60.263 1   23.39 ? 57  ASP   D OD1   1 
ATOM   2345 O OD2   . ASP   B 1 76  ? 39.059  -31.481 60.866 1   28.92 ? 57  ASP   D OD2   1 
ATOM   2346 N N     . LEU   B 1 77  ? 36.661  -35.506 63.962 1   3.85  ? 58  LEU   D N     1 
ATOM   2347 C CA    . LEU   B 1 77  ? 36.897  -36.775 64.652 1   3     ? 58  LEU   D CA    1 
ATOM   2348 C C     . LEU   B 1 77  ? 35.92   -37.097 65.789 1   5.42  ? 58  LEU   D C     1 
ATOM   2349 O O     . LEU   B 1 77  ? 35.778  -36.307 66.734 1   3     ? 58  LEU   D O     1 
ATOM   2350 C CB    . LEU   B 1 77  ? 38.353  -36.796 65.188 1   3     ? 58  LEU   D CB    1 
ATOM   2351 C CG    . LEU   B 1 77  ? 38.828  -38.052 65.987 1   6.74  ? 58  LEU   D CG    1 
ATOM   2352 C CD1   . LEU   B 1 77  ? 38.873  -39.292 65.112 1   6.88  ? 58  LEU   D CD1   1 
ATOM   2353 C CD2   . LEU   B 1 77  ? 40.207  -37.843 66.585 1   6.01  ? 58  LEU   D CD2   1 
ATOM   2354 N N     . LEU   B 1 78  ? 35.33   -38.307 65.723 1   3     ? 59  LEU   D N     1 
ATOM   2355 C CA    . LEU   B 1 78  ? 34.475  -38.879 66.767 1   3     ? 59  LEU   D CA    1 
ATOM   2356 C C     . LEU   B 1 78  ? 35.154  -40.17  67.259 1   5.04  ? 59  LEU   D C     1 
ATOM   2357 O O     . LEU   B 1 78  ? 35.571  -40.996 66.437 1   3     ? 59  LEU   D O     1 
ATOM   2358 C CB    . LEU   B 1 78  ? 33.058  -39.198 66.252 1   3     ? 59  LEU   D CB    1 
ATOM   2359 C CG    . LEU   B 1 78  ? 32.112  -39.896 67.276 1   5.99  ? 59  LEU   D CG    1 
ATOM   2360 C CD1   . LEU   B 1 78  ? 30.741  -39.255 67.296 1   5.79  ? 59  LEU   D CD1   1 
ATOM   2361 C CD2   . LEU   B 1 78  ? 31.959  -41.386 66.969 1   6.62  ? 59  LEU   D CD2   1 
ATOM   2362 N N     . ILE   B 1 79  ? 35.259  -40.342 68.58  1   3     ? 60  ILE   D N     1 
ATOM   2363 C CA    . ILE   B 1 79  ? 35.783  -41.581 69.163 1   3     ? 60  ILE   D CA    1 
ATOM   2364 C C     . ILE   B 1 79  ? 34.587  -42.3   69.816 1   5.68  ? 60  ILE   D C     1 
ATOM   2365 O O     . ILE   B 1 79  ? 33.931  -41.715 70.685 1   3     ? 60  ILE   D O     1 
ATOM   2366 C CB    . ILE   B 1 79  ? 36.965  -41.373 70.153 1   3.93  ? 60  ILE   D CB    1 
ATOM   2367 C CG1   . ILE   B 1 79  ? 38.183  -40.734 69.426 1   3     ? 60  ILE   D CG1   1 
ATOM   2368 C CG2   . ILE   B 1 79  ? 37.379  -42.714 70.853 1   3     ? 60  ILE   D CG2   1 
ATOM   2369 C CD1   . ILE   B 1 79  ? 39.289  -40.219 70.368 1   4.02  ? 60  ILE   D CD1   1 
ATOM   2370 N N     . ASP   B 1 80  ? 34.287  -43.531 69.364 1   3     ? 61  ASP   D N     1 
ATOM   2371 C CA    . ASP   B 1 80  ? 33.219  -44.333 69.978 1   3     ? 61  ASP   D CA    1 
ATOM   2372 C C     . ASP   B 1 80  ? 33.876  -45.26  71.004 1   5.22  ? 61  ASP   D C     1 
ATOM   2373 O O     . ASP   B 1 80  ? 34.7    -46.109 70.631 1   3     ? 61  ASP   D O     1 
ATOM   2374 C CB    . ASP   B 1 80  ? 32.42   -45.157 68.956 1   3.4   ? 61  ASP   D CB    1 
ATOM   2375 C CG    . ASP   B 1 80  ? 31.299  -45.963 69.614 1   7.2   ? 61  ASP   D CG    1 
ATOM   2376 O OD1   . ASP   B 1 80  ? 30.648  -45.429 70.56  1   7.82  ? 61  ASP   D OD1   1 
ATOM   2377 O OD2   . ASP   B 1 80  ? 31.077  -47.122 69.198 1   9.44  ? 61  ASP   D OD2   1 
ATOM   2378 N N     . ILE   B 1 81  ? 33.518  -45.085 72.284 1   3     ? 62  ILE   D N     1 
ATOM   2379 C CA    . ILE   B 1 81  ? 34.074  -45.815 73.438 1   3     ? 62  ILE   D CA    1 
ATOM   2380 C C     . ILE   B 1 81  ? 33.204  -47.041 73.823 1   4.48  ? 62  ILE   D C     1 
ATOM   2381 O O     . ILE   B 1 81  ? 32.02   -46.874 74.112 1   3     ? 62  ILE   D O     1 
ATOM   2382 C CB    . ILE   B 1 81  ? 34.203  -44.8   74.627 1   3.83  ? 62  ILE   D CB    1 
ATOM   2383 C CG1   . ILE   B 1 81  ? 35.291  -43.728 74.352 1   3.07  ? 62  ILE   D CG1   1 
ATOM   2384 C CG2   . ILE   B 1 81  ? 34.408  -45.515 75.991 1   3     ? 62  ILE   D CG2   1 
ATOM   2385 C CD1   . ILE   B 1 81  ? 36.779  -44.265 74.227 1   5.42  ? 62  ILE   D CD1   1 
ATOM   2386 N N     . GLY   B 1 82  ? 33.808  -48.23  73.887 1   3     ? 63  GLY   D N     1 
ATOM   2387 C CA    . GLY   B 1 82  ? 33.079  -49.443 74.26  1   3     ? 63  GLY   D CA    1 
ATOM   2388 C C     . GLY   B 1 82  ? 32.071  -49.839 73.192 1   4.97  ? 63  GLY   D C     1 
ATOM   2389 O O     . GLY   B 1 82  ? 30.918  -50.192 73.489 1   3     ? 63  GLY   D O     1 
ATOM   2390 N N     . SER   B 1 83  ? 32.515  -49.739 71.921 1   3     ? 64  SER   D N     1 
ATOM   2391 C CA    . SER   B 1 83  ? 31.758  -50.028 70.713 1   3     ? 64  SER   D CA    1 
ATOM   2392 C C     . SER   B 1 83  ? 31.157  -51.426 70.74  1   5.25  ? 64  SER   D C     1 
ATOM   2393 O O     . SER   B 1 83  ? 30.112  -51.64  70.132 1   3     ? 64  SER   D O     1 
ATOM   2394 C CB    . SER   B 1 83  ? 32.674  -49.937 69.494 1   5.16  ? 64  SER   D CB    1 
ATOM   2395 O OG    . SER   B 1 83  ? 33.313  -48.671 69.415 1   7.59  ? 64  SER   D OG    1 
ATOM   2396 N N     . GLY   B 1 84  ? 31.832  -52.363 71.414 1   3     ? 65  GLY   D N     1 
ATOM   2397 C CA    . GLY   B 1 84  ? 31.444  -53.768 71.386 1   3     ? 65  GLY   D CA    1 
ATOM   2398 C C     . GLY   B 1 84  ? 31.489  -54.212 69.924 1   5.27  ? 65  GLY   D C     1 
ATOM   2399 O O     . GLY   B 1 84  ? 32.264  -53.64  69.14  1   3     ? 65  GLY   D O     1 
ATOM   2400 N N     . PRO   B 1 85  ? 30.594  -55.13  69.487 1   3     ? 66  PRO   D N     1 
ATOM   2401 C CA    . PRO   B 1 85  ? 30.6    -55.538 68.068 1   3     ? 66  PRO   D CA    1 
ATOM   2402 C C     . PRO   B 1 85  ? 29.556  -54.772 67.249 1   5.52  ? 66  PRO   D C     1 
ATOM   2403 O O     . PRO   B 1 85  ? 29.21   -55.211 66.149 1   3     ? 66  PRO   D O     1 
ATOM   2404 C CB    . PRO   B 1 85  ? 30.215  -57.021 68.164 1   4.02  ? 66  PRO   D CB    1 
ATOM   2405 C CG    . PRO   B 1 85  ? 29.244  -57.071 69.326 1   7.12  ? 66  PRO   D CG    1 
ATOM   2406 C CD    . PRO   B 1 85  ? 29.592  -55.907 70.255 1   3.24  ? 66  PRO   D CD    1 
ATOM   2407 N N     . THR   B 1 86  ? 29.027  -53.635 67.793 1   3     ? 67  THR   D N     1 
ATOM   2408 C CA    . THR   B 1 86  ? 27.924  -52.921 67.142 1   3     ? 67  THR   D CA    1 
ATOM   2409 C C     . THR   B 1 86  ? 28.357  -51.723 66.297 1   5.25  ? 67  THR   D C     1 
ATOM   2410 O O     . THR   B 1 86  ? 29.371  -51.071 66.587 1   3     ? 67  THR   D O     1 
ATOM   2411 C CB    . THR   B 1 86  ? 26.833  -52.503 68.161 1   6.73  ? 67  THR   D CB    1 
ATOM   2412 O OG1   . THR   B 1 86  ? 27.319  -51.424 68.95  1   3.83  ? 67  THR   D OG1   1 
ATOM   2413 C CG2   . THR   B 1 86  ? 26.347  -53.646 69.037 1   3     ? 67  THR   D CG2   1 
ATOM   2414 N N     . ILE   B 1 87  ? 27.534  -51.405 65.279 1   3     ? 68  ILE   D N     1 
ATOM   2415 C CA    . ILE   B 1 87  ? 27.759  -50.272 64.371 1   3     ? 68  ILE   D CA    1 
ATOM   2416 C C     . ILE   B 1 87  ? 26.557  -49.312 64.336 1   4.53  ? 68  ILE   D C     1 
ATOM   2417 O O     . ILE   B 1 87  ? 26.664  -48.239 63.741 1   3     ? 68  ILE   D O     1 
ATOM   2418 C CB    . ILE   B 1 87  ? 28.187  -50.731 62.929 1   6.77  ? 68  ILE   D CB    1 
ATOM   2419 C CG1   . ILE   B 1 87  ? 27.095  -51.561 62.22  1   8.16  ? 68  ILE   D CG1   1 
ATOM   2420 C CG2   . ILE   B 1 87  ? 29.513  -51.497 62.951 1   7.67  ? 68  ILE   D CG2   1 
ATOM   2421 C CD1   . ILE   B 1 87  ? 26.177  -50.8   61.301 1   14.07 ? 68  ILE   D CD1   1 
ATOM   2422 N N     . TYR   B 1 88  ? 25.415  -49.714 64.944 1   3     ? 69  TYR   D N     1 
ATOM   2423 C CA    . TYR   B 1 88  ? 24.168  -48.935 64.936 1   3     ? 69  TYR   D CA    1 
ATOM   2424 C C     . TYR   B 1 88  ? 24.354  -47.499 65.458 1   5.25  ? 69  TYR   D C     1 
ATOM   2425 O O     . TYR   B 1 88  ? 23.709  -46.578 64.949 1   3     ? 69  TYR   D O     1 
ATOM   2426 C CB    . TYR   B 1 88  ? 23.042  -49.661 65.709 1   3.04  ? 69  TYR   D CB    1 
ATOM   2427 C CG    . TYR   B 1 88  ? 23.12   -49.466 67.213 1   3     ? 69  TYR   D CG    1 
ATOM   2428 C CD1   . TYR   B 1 88  ? 22.502  -48.379 67.829 1   4.61  ? 69  TYR   D CD1   1 
ATOM   2429 C CD2   . TYR   B 1 88  ? 23.871  -50.326 68.01  1   3     ? 69  TYR   D CD2   1 
ATOM   2430 C CE1   . TYR   B 1 88  ? 22.612  -48.165 69.206 1   3     ? 69  TYR   D CE1   1 
ATOM   2431 C CE2   . TYR   B 1 88  ? 23.975  -50.132 69.393 1   3     ? 69  TYR   D CE2   1 
ATOM   2432 C CZ    . TYR   B 1 88  ? 23.341  -49.049 69.984 1   3.03  ? 69  TYR   D CZ    1 
ATOM   2433 O OH    . TYR   B 1 88  ? 23.457  -48.803 71.332 1   3     ? 69  TYR   D OH    1 
ATOM   2434 N N     . GLN   B 1 89  ? 25.225  -47.325 66.478 1   3     ? 70  GLN   D N     1 
ATOM   2435 C CA    . GLN   B 1 89  ? 25.477  -46.037 67.135 1   3     ? 70  GLN   D CA    1 
ATOM   2436 C C     . GLN   B 1 89  ? 26.3    -45.074 66.274 1   4.89  ? 70  GLN   D C     1 
ATOM   2437 O O     . GLN   B 1 89  ? 26.502  -43.927 66.673 1   3     ? 70  GLN   D O     1 
ATOM   2438 C CB    . GLN   B 1 89  ? 26.118  -46.241 68.537 1   3.21  ? 70  GLN   D CB    1 
ATOM   2439 C CG    . GLN   B 1 89  ? 27.586  -46.722 68.542 1   3     ? 70  GLN   D CG    1 
ATOM   2440 C CD    . GLN   B 1 89  ? 27.777  -48.229 68.445 1   5.97  ? 70  GLN   D CD    1 
ATOM   2441 O OE1   . GLN   B 1 89  ? 27.003  -48.965 67.823 1   3     ? 70  GLN   D OE1   1 
ATOM   2442 N NE2   . GLN   B 1 89  ? 28.857  -48.738 69.036 1   9.21  ? 70  GLN   D NE2   1 
ATOM   2443 N N     . LEU   B 1 90  ? 26.779  -45.552 65.102 1   3     ? 71  LEU   D N     1 
ATOM   2444 C CA    . LEU   B 1 90  ? 27.633  -44.779 64.186 1   3     ? 71  LEU   D CA    1 
ATOM   2445 C C     . LEU   B 1 90  ? 26.941  -44.402 62.863 1   5.27  ? 71  LEU   D C     1 
ATOM   2446 O O     . LEU   B 1 90  ? 27.48   -43.598 62.099 1   3     ? 71  LEU   D O     1 
ATOM   2447 C CB    . LEU   B 1 90  ? 28.897  -45.596 63.887 1   3     ? 71  LEU   D CB    1 
ATOM   2448 C CG    . LEU   B 1 90  ? 29.606  -46.254 65.094 1   5.57  ? 71  LEU   D CG    1 
ATOM   2449 C CD1   . LEU   B 1 90  ? 30.63   -47.269 64.626 1   5.66  ? 71  LEU   D CD1   1 
ATOM   2450 C CD2   . LEU   B 1 90  ? 30.261  -45.212 65.99  1   5.82  ? 71  LEU   D CD2   1 
ATOM   2451 N N     . LEU   B 1 91  ? 25.75   -44.976 62.599 1   3     ? 72  LEU   D N     1 
ATOM   2452 C CA    . LEU   B 1 91  ? 25.034  -44.76  61.334 1   3.6   ? 72  LEU   D CA    1 
ATOM   2453 C C     . LEU   B 1 91  ? 24.677  -43.29  61.063 1   6.65  ? 72  LEU   D C     1 
ATOM   2454 O O     . LEU   B 1 91  ? 24.893  -42.83  59.936 1   6.87  ? 72  LEU   D O     1 
ATOM   2455 C CB    . LEU   B 1 91  ? 23.813  -45.68  61.2   1   3     ? 72  LEU   D CB    1 
ATOM   2456 C CG    . LEU   B 1 91  ? 24.171  -47.164 60.958 1   6.5   ? 72  LEU   D CG    1 
ATOM   2457 C CD1   . LEU   B 1 91  ? 22.978  -48.068 61.183 1   6.05  ? 72  LEU   D CD1   1 
ATOM   2458 C CD2   . LEU   B 1 91  ? 24.761  -47.399 59.539 1   7.22  ? 72  LEU   D CD2   1 
ATOM   2459 N N     . SER   B 1 92  ? 24.209  -42.537 62.07  1   3.89  ? 73  SER   D N     1 
ATOM   2460 C CA    . SER   B 1 92  ? 23.932  -41.111 61.851 1   3     ? 73  SER   D CA    1 
ATOM   2461 C C     . SER   B 1 92  ? 25.206  -40.261 62.008 1   5.5   ? 73  SER   D C     1 
ATOM   2462 O O     . SER   B 1 92  ? 25.347  -39.239 61.325 1   3     ? 73  SER   D O     1 
ATOM   2463 C CB    . SER   B 1 92  ? 22.818  -40.611 62.766 1   4.03  ? 73  SER   D CB    1 
ATOM   2464 O OG    . SER   B 1 92  ? 21.568  -41.142 62.358 1   7.23  ? 73  SER   D OG    1 
ATOM   2465 N N     . ALA   B 1 93  ? 26.139  -40.701 62.884 1   3     ? 74  ALA   D N     1 
ATOM   2466 C CA    . ALA   B 1 93  ? 27.417  -40.012 63.137 1   3     ? 74  ALA   D CA    1 
ATOM   2467 C C     . ALA   B 1 93  ? 28.303  -39.904 61.885 1   5.41  ? 74  ALA   D C     1 
ATOM   2468 O O     . ALA   B 1 93  ? 29.026  -38.918 61.759 1   3.44  ? 74  ALA   D O     1 
ATOM   2469 C CB    . ALA   B 1 93  ? 28.198  -40.714 64.243 1   3     ? 74  ALA   D CB    1 
ATOM   2470 N N     . CYS   B 1 94  ? 28.286  -40.928 60.982 1   5.39  ? 75  CYS   D N     1 
ATOM   2471 C CA    . CYS   B 1 94  ? 29.124  -40.9   59.767 1   8.19  ? 75  CYS   D CA    1 
ATOM   2472 C C     . CYS   B 1 94  ? 28.7    -39.779 58.786 1   8.08  ? 75  CYS   D C     1 
ATOM   2473 O O     . CYS   B 1 94  ? 29.466  -39.422 57.892 1   8.3   ? 75  CYS   D O     1 
ATOM   2474 C CB    . CYS   B 1 94  ? 29.197  -42.263 59.088 1   10.53 ? 75  CYS   D CB    1 
ATOM   2475 S SG    . CYS   B 1 94  ? 27.637  -42.806 58.342 1   8.76  ? 75  CYS   D SG    1 
ATOM   2476 N N     . GLU   B 1 95  ? 27.507  -39.191 58.997 1   8.05  ? 76  GLU   D N     1 
ATOM   2477 C CA    . GLU   B 1 95  ? 27.029  -38.082 58.165 1   7.58  ? 76  GLU   D CA    1 
ATOM   2478 C C     . GLU   B 1 95  ? 27.613  -36.751 58.648 1   7.88  ? 76  GLU   D C     1 
ATOM   2479 O O     . GLU   B 1 95  ? 27.623  -35.777 57.887 1   9.69  ? 76  GLU   D O     1 
ATOM   2480 C CB    . GLU   B 1 95  ? 25.491  -38.018 58.176 1   8.73  ? 76  GLU   D CB    1 
ATOM   2481 C CG    . GLU   B 1 95  ? 24.808  -39.237 57.577 1   11.24 ? 76  GLU   D CG    1 
ATOM   2482 C CD    . GLU   B 1 95  ? 25.055  -39.496 56.099 1   29.7  ? 76  GLU   D CD    1 
ATOM   2483 O OE1   . GLU   B 1 95  ? 25.215  -38.52  55.328 1   28.38 ? 76  GLU   D OE1   1 
ATOM   2484 O OE2   . GLU   B 1 95  ? 25.078  -40.685 55.711 1   16.17 ? 76  GLU   D OE2   1 
ATOM   2485 N N     . SER   B 1 96  ? 28.096  -36.712 59.911 1   6.64  ? 77  SER   D N     1 
ATOM   2486 C CA    . SER   B 1 96  ? 28.597  -35.496 60.571 1   6.57  ? 77  SER   D CA    1 
ATOM   2487 C C     . SER   B 1 96  ? 30.083  -35.485 60.929 1   7.52  ? 77  SER   D C     1 
ATOM   2488 O O     . SER   B 1 96  ? 30.611  -34.433 61.309 1   7.7   ? 77  SER   D O     1 
ATOM   2489 C CB    . SER   B 1 96  ? 27.772  -35.219 61.829 1   9.36  ? 77  SER   D CB    1 
ATOM   2490 O OG    . SER   B 1 96  ? 26.399  -35.172 61.486 1   9.23  ? 77  SER   D OG    1 
ATOM   2491 N N     . PHE   B 1 97  ? 30.75   -36.634 60.836 1   4.26  ? 78  PHE   D N     1 
ATOM   2492 C CA    . PHE   B 1 97  ? 32.17   -36.737 61.192 1   3     ? 78  PHE   D CA    1 
ATOM   2493 C C     . PHE   B 1 97  ? 32.964  -37.344 60.059 1   6.88  ? 78  PHE   D C     1 
ATOM   2494 O O     . PHE   B 1 97  ? 32.624  -38.43  59.581 1   6.6   ? 78  PHE   D O     1 
ATOM   2495 C CB    . PHE   B 1 97  ? 32.356  -37.559 62.496 1   3.15  ? 78  PHE   D CB    1 
ATOM   2496 C CG    . PHE   B 1 97  ? 31.854  -36.828 63.715 1   3     ? 78  PHE   D CG    1 
ATOM   2497 C CD1   . PHE   B 1 97  ? 30.521  -36.932 64.109 1   3.23  ? 78  PHE   D CD1   1 
ATOM   2498 C CD2   . PHE   B 1 97  ? 32.693  -35.977 64.431 1   4.21  ? 78  PHE   D CD2   1 
ATOM   2499 C CE1   . PHE   B 1 97  ? 30.04   -36.202 65.196 1   4.59  ? 78  PHE   D CE1   1 
ATOM   2500 C CE2   . PHE   B 1 97  ? 32.219  -35.268 65.54  1   6.07  ? 78  PHE   D CE2   1 
ATOM   2501 C CZ    . PHE   B 1 97  ? 30.898  -35.383 65.914 1   3.94  ? 78  PHE   D CZ    1 
ATOM   2502 N N     . LYS   B 1 98  ? 34.038  -36.645 59.645 1   6.87  ? 79  LYS   D N     1 
ATOM   2503 C CA    . LYS   B 1 98  ? 34.932  -37.078 58.571 1   8.13  ? 79  LYS   D CA    1 
ATOM   2504 C C     . LYS   B 1 98  ? 35.598  -38.413 58.939 1   6.88  ? 79  LYS   D C     1 
ATOM   2505 O O     . LYS   B 1 98  ? 35.672  -39.314 58.095 1   8.2   ? 79  LYS   D O     1 
ATOM   2506 C CB    . LYS   B 1 98  ? 35.992  -35.985 58.298 1   7.28  ? 79  LYS   D CB    1 
ATOM   2507 C CG    . LYS   B 1 98  ? 37.077  -36.359 57.266 1   26.44 ? 79  LYS   D CG    1 
ATOM   2508 C CD    . LYS   B 1 98  ? 38.173  -35.278 57.163 1   46.69 ? 79  LYS   D CD    1 
ATOM   2509 C CE    . LYS   B 1 98  ? 39.242  -35.391 58.233 1   61.1  ? 79  LYS   D CE    1 
ATOM   2510 N NZ    . LYS   B 1 98  ? 40.023  -34.131 58.375 1   72.48 ? 79  LYS   D NZ    1 
ATOM   2511 N N     . GLU   B 1 99  ? 36.061  -38.533 60.196 1   5.13  ? 80  GLU   D N     1 
ATOM   2512 C CA    . GLU   B 1 99  ? 36.745  -39.718 60.711 1   4.57  ? 80  GLU   D CA    1 
ATOM   2513 C C     . GLU   B 1 99  ? 36.078  -40.208 62.006 1   5.66  ? 80  GLU   D C     1 
ATOM   2514 O O     . GLU   B 1 99  ? 35.738  -39.407 62.886 1   3     ? 80  GLU   D O     1 
ATOM   2515 C CB    . GLU   B 1 99  ? 38.241  -39.4   60.941 1   7.27  ? 80  GLU   D CB    1 
ATOM   2516 C CG    . GLU   B 1 99  ? 39.065  -40.492 61.637 1   10.34 ? 80  GLU   D CG    1 
ATOM   2517 C CD    . GLU   B 1 99  ? 40.587  -40.389 61.573 1   45.59 ? 80  GLU   D CD    1 
ATOM   2518 O OE1   . GLU   B 1 99  ? 41.098  -39.549 60.791 1   52.79 ? 80  GLU   D OE1   1 
ATOM   2519 O OE2   . GLU   B 1 99  ? 41.268  -41.165 62.291 1   37.09 ? 80  GLU   D OE2   1 
ATOM   2520 N N     . ILE   B 1 100 ? 35.91   -41.526 62.108 1   3     ? 81  ILE   D N     1 
ATOM   2521 C CA    . ILE   B 1 100 ? 35.366  -42.199 63.28  1   3     ? 81  ILE   D CA    1 
ATOM   2522 C C     . ILE   B 1 100 ? 36.392  -43.236 63.727 1   5.51  ? 81  ILE   D C     1 
ATOM   2523 O O     . ILE   B 1 100 ? 36.877  -44.006 62.896 1   3     ? 81  ILE   D O     1 
ATOM   2524 C CB    . ILE   B 1 100 ? 33.987  -42.857 62.983 1   3.65  ? 81  ILE   D CB    1 
ATOM   2525 C CG1   . ILE   B 1 100 ? 32.913  -41.788 62.609 1   3     ? 81  ILE   D CG1   1 
ATOM   2526 C CG2   . ILE   B 1 100 ? 33.528  -43.751 64.178 1   3     ? 81  ILE   D CG2   1 
ATOM   2527 C CD1   . ILE   B 1 100 ? 31.549  -42.377 62.148 1   3     ? 81  ILE   D CD1   1 
ATOM   2528 N N     . VAL   B 1 101 ? 36.72   -43.25  65.023 1   3     ? 82  VAL   D N     1 
ATOM   2529 C CA    . VAL   B 1 101 ? 37.611  -44.257 65.633 1   3     ? 82  VAL   D CA    1 
ATOM   2530 C C     . VAL   B 1 101 ? 36.73   -45.128 66.563 1   5.19  ? 82  VAL   D C     1 
ATOM   2531 O O     . VAL   B 1 101 ? 36.03   -44.589 67.429 1   3     ? 82  VAL   D O     1 
ATOM   2532 C CB    . VAL   B 1 101 ? 38.821  -43.606 66.354 1   3.66  ? 82  VAL   D CB    1 
ATOM   2533 C CG1   . VAL   B 1 101 ? 39.603  -44.629 67.191 1   3     ? 82  VAL   D CG1   1 
ATOM   2534 C CG2   . VAL   B 1 101 ? 39.742  -42.92  65.345 1   3     ? 82  VAL   D CG2   1 
ATOM   2535 N N     . VAL   B 1 102 ? 36.733  -46.454 66.344 1   3     ? 83  VAL   D N     1 
ATOM   2536 C CA    . VAL   B 1 102 ? 35.951  -47.403 67.143 1   3     ? 83  VAL   D CA    1 
ATOM   2537 C C     . VAL   B 1 102 ? 36.865  -48.094 68.158 1   5.16  ? 83  VAL   D C     1 
ATOM   2538 O O     . VAL   B 1 102 ? 38.001  -48.439 67.822 1   3     ? 83  VAL   D O     1 
ATOM   2539 C CB    . VAL   B 1 102 ? 35.097  -48.389 66.308 1   4.11  ? 83  VAL   D CB    1 
ATOM   2540 C CG1   . VAL   B 1 102 ? 34.154  -47.629 65.372 1   3     ? 83  VAL   D CG1   1 
ATOM   2541 C CG2   . VAL   B 1 102 ? 35.967  -49.371 65.519 1   3.24  ? 83  VAL   D CG2   1 
ATOM   2542 N N     . THR   B 1 103 ? 36.402  -48.22  69.42  1   3     ? 84  THR   D N     1 
ATOM   2543 C CA    . THR   B 1 103 ? 37.256  -48.779 70.478 1   3     ? 84  THR   D CA    1 
ATOM   2544 C C     . THR   B 1 103 ? 36.501  -49.747 71.408 1   5.4   ? 84  THR   D C     1 
ATOM   2545 O O     . THR   B 1 103 ? 35.287  -49.614 71.595 1   3     ? 84  THR   D O     1 
ATOM   2546 C CB    . THR   B 1 103 ? 37.88   -47.64  71.329 1   3     ? 84  THR   D CB    1 
ATOM   2547 O OG1   . THR   B 1 103 ? 36.879  -47.15  72.226 1   3     ? 84  THR   D OG1   1 
ATOM   2548 C CG2   . THR   B 1 103 ? 38.486  -46.487 70.499 1   3     ? 84  THR   D CG2   1 
ATOM   2549 N N     . ASP   B 1 104 ? 37.225  -50.699 72.008 1   3     ? 85  ASP   D N     1 
ATOM   2550 C CA    . ASP   B 1 104 ? 36.617  -51.634 72.947 1   3     ? 85  ASP   D CA    1 
ATOM   2551 C C     . ASP   B 1 104 ? 37.686  -52.354 73.745 1   5.01  ? 85  ASP   D C     1 
ATOM   2552 O O     . ASP   B 1 104 ? 38.846  -52.414 73.323 1   3     ? 85  ASP   D O     1 
ATOM   2553 C CB    . ASP   B 1 104 ? 35.699  -52.655 72.24  1   3     ? 85  ASP   D CB    1 
ATOM   2554 C CG    . ASP   B 1 104 ? 34.7    -53.301 73.185 1   3.04  ? 85  ASP   D CG    1 
ATOM   2555 O OD1   . ASP   B 1 104 ? 33.758  -52.606 73.613 1   3     ? 85  ASP   D OD1   1 
ATOM   2556 O OD2   . ASP   B 1 104 ? 34.879  -54.5   73.512 1   3     ? 85  ASP   D OD2   1 
ATOM   2557 N N     . TYR   B 1 105 ? 37.297  -52.891 74.898 1   3     ? 86  TYR   D N     1 
ATOM   2558 C CA    . TYR   B 1 105 ? 38.227  -53.655 75.724 1   3     ? 86  TYR   D CA    1 
ATOM   2559 C C     . TYR   B 1 105 ? 38.473  -55.035 75.135 1   5.55  ? 86  TYR   D C     1 
ATOM   2560 O O     . TYR   B 1 105 ? 39.578  -55.565 75.285 1   3     ? 86  TYR   D O     1 
ATOM   2561 C CB    . TYR   B 1 105 ? 37.708  -53.799 77.171 1   3     ? 86  TYR   D CB    1 
ATOM   2562 C CG    . TYR   B 1 105 ? 38.76   -54.367 78.09  1   3     ? 86  TYR   D CG    1 
ATOM   2563 C CD1   . TYR   B 1 105 ? 39.919  -53.65  78.382 1   4.02  ? 86  TYR   D CD1   1 
ATOM   2564 C CD2   . TYR   B 1 105 ? 38.653  -55.663 78.586 1   3.71  ? 86  TYR   D CD2   1 
ATOM   2565 C CE1   . TYR   B 1 105 ? 40.908  -54.177 79.212 1   4.7   ? 86  TYR   D CE1   1 
ATOM   2566 C CE2   . TYR   B 1 105 ? 39.637  -56.205 79.414 1   4.15  ? 86  TYR   D CE2   1 
ATOM   2567 C CZ    . TYR   B 1 105 ? 40.767  -55.46  79.715 1   6.24  ? 86  TYR   D CZ    1 
ATOM   2568 O OH    . TYR   B 1 105 ? 41.755  -55.98  80.502 1   7.84  ? 86  TYR   D OH    1 
ATOM   2569 N N     . SER   B 1 106 ? 37.452  -55.618 74.489 1   3     ? 87  SER   D N     1 
ATOM   2570 C CA    . SER   B 1 106 ? 37.51   -56.985 73.973 1   3     ? 87  SER   D CA    1 
ATOM   2571 C C     . SER   B 1 106 ? 38.014  -57.107 72.539 1   5.24  ? 87  SER   D C     1 
ATOM   2572 O O     . SER   B 1 106 ? 37.415  -56.535 71.623 1   3     ? 87  SER   D O     1 
ATOM   2573 C CB    . SER   B 1 106 ? 36.151  -57.669 74.117 1   6.34  ? 87  SER   D CB    1 
ATOM   2574 O OG    . SER   B 1 106 ? 36.035  -58.783 73.239 1   7.34  ? 87  SER   D OG    1 
ATOM   2575 N N     . ASP   B 1 107 ? 39.068  -57.928 72.341 1   3     ? 88  ASP   D N     1 
ATOM   2576 C CA    . ASP   B 1 107 ? 39.637  -58.208 71.017 1   4.19  ? 88  ASP   D CA    1 
ATOM   2577 C C     . ASP   B 1 107 ? 38.609  -58.957 70.149 1   5.28  ? 88  ASP   D C     1 
ATOM   2578 O O     . ASP   B 1 107 ? 38.469  -58.637 68.962 1   4.28  ? 88  ASP   D O     1 
ATOM   2579 C CB    . ASP   B 1 107 ? 40.96   -58.995 71.15  1   9.13  ? 88  ASP   D CB    1 
ATOM   2580 C CG    . ASP   B 1 107 ? 41.959  -58.271 72.041 1   12.85 ? 88  ASP   D CG    1 
ATOM   2581 O OD1   . ASP   B 1 107 ? 42.626  -57.319 71.545 1   15    ? 88  ASP   D OD1   1 
ATOM   2582 O OD2   . ASP   B 1 107 ? 42.025  -58.602 73.256 1   22.29 ? 88  ASP   D OD2   1 
ATOM   2583 N N     . GLN   B 1 108 ? 37.841  -59.9   70.752 1   3     ? 89  GLN   D N     1 
ATOM   2584 C CA    . GLN   B 1 108 ? 36.775  -60.639 70.047 1   3     ? 89  GLN   D CA    1 
ATOM   2585 C C     . GLN   B 1 108 ? 35.75   -59.651 69.464 1   5.21  ? 89  GLN   D C     1 
ATOM   2586 O O     . GLN   B 1 108 ? 35.282  -59.841 68.336 1   3     ? 89  GLN   D O     1 
ATOM   2587 C CB    . GLN   B 1 108 ? 36.021  -61.581 71.01  1   5.47  ? 89  GLN   D CB    1 
ATOM   2588 C CG    . GLN   B 1 108 ? 36.742  -62.871 71.376 1   14.6  ? 89  GLN   D CG    1 
ATOM   2589 C CD    . GLN   B 1 108 ? 35.788  -63.831 72.066 1   39.94 ? 89  GLN   D CD    1 
ATOM   2590 O OE1   . GLN   B 1 108 ? 35.619  -63.822 73.295 1   36.96 ? 89  GLN   D OE1   1 
ATOM   2591 N NE2   . GLN   B 1 108 ? 35.131  -64.676 71.282 1   35.83 ? 89  GLN   D NE2   1 
ATOM   2592 N N     . ASN   B 1 109 ? 35.367  -58.604 70.25  1   3     ? 90  ASN   D N     1 
ATOM   2593 C CA    . ASN   B 1 109 ? 34.375  -57.637 69.765 1   3     ? 90  ASN   D CA    1 
ATOM   2594 C C     . ASN   B 1 109 ? 34.897  -56.876 68.584 1   4.64  ? 90  ASN   D C     1 
ATOM   2595 O O     . ASN   B 1 109 ? 34.184  -56.752 67.594 1   4.09  ? 90  ASN   D O     1 
ATOM   2596 C CB    . ASN   B 1 109 ? 33.914  -56.676 70.87  1   3     ? 90  ASN   D CB    1 
ATOM   2597 C CG    . ASN   B 1 109 ? 32.953  -57.306 71.855 1   5.43  ? 90  ASN   D CG    1 
ATOM   2598 O OD1   . ASN   B 1 109 ? 32.32   -58.34  71.583 1   3     ? 90  ASN   D OD1   1 
ATOM   2599 N ND2   . ASN   B 1 109 ? 32.815  -56.683 73.014 1   3     ? 90  ASN   D ND2   1 
ATOM   2600 N N     . LEU   B 1 110 ? 36.14   -56.388 68.671 1   3     ? 91  LEU   D N     1 
ATOM   2601 C CA    . LEU   B 1 110 ? 36.785  -55.636 67.578 1   3     ? 91  LEU   D CA    1 
ATOM   2602 C C     . LEU   B 1 110 ? 36.911  -56.494 66.302 1   5.01  ? 91  LEU   D C     1 
ATOM   2603 O O     . LEU   B 1 110 ? 36.778  -55.969 65.205 1   3     ? 91  LEU   D O     1 
ATOM   2604 C CB    . LEU   B 1 110 ? 38.16   -55.116 67.998 1   3     ? 91  LEU   D CB    1 
ATOM   2605 C CG    . LEU   B 1 110 ? 38.171  -54.166 69.215 1   5.99  ? 91  LEU   D CG    1 
ATOM   2606 C CD1   . LEU   B 1 110 ? 39.574  -53.724 69.52  1   5.58  ? 91  LEU   D CD1   1 
ATOM   2607 C CD2   . LEU   B 1 110 ? 37.271  -52.949 68.987 1   6.91  ? 91  LEU   D CD2   1 
ATOM   2608 N N     . GLN   B 1 111 ? 37.142  -57.807 66.46  1   3     ? 92  GLN   D N     1 
ATOM   2609 C CA    . GLN   B 1 111 ? 37.223  -58.735 65.322 1   3.62  ? 92  GLN   D CA    1 
ATOM   2610 C C     . GLN   B 1 111 ? 35.847  -58.829 64.634 1   6.9   ? 92  GLN   D C     1 
ATOM   2611 O O     . GLN   B 1 111 ? 35.792  -58.812 63.404 1   5.41  ? 92  GLN   D O     1 
ATOM   2612 C CB    . GLN   B 1 111 ? 37.706  -60.119 65.775 1   6.05  ? 92  GLN   D CB    1 
ATOM   2613 C CG    . GLN   B 1 111 ? 39.21   -60.168 66.053 1   14.14 ? 92  GLN   D CG    1 
ATOM   2614 C CD    . GLN   B 1 111 ? 39.607  -61.392 66.859 1   46.26 ? 92  GLN   D CD    1 
ATOM   2615 O OE1   . GLN   B 1 111 ? 39.02   -62.484 66.75  1   45.01 ? 92  GLN   D OE1   1 
ATOM   2616 N NE2   . GLN   B 1 111 ? 40.628  -61.236 67.69  1   42.46 ? 92  GLN   D NE2   1 
ATOM   2617 N N     . GLU   B 1 112 ? 34.743  -58.875 65.424 1   3.83  ? 93  GLU   D N     1 
ATOM   2618 C CA    . GLU   B 1 112 ? 33.373  -58.917 64.882 1   4.68  ? 93  GLU   D CA    1 
ATOM   2619 C C     . GLU   B 1 112 ? 33.065  -57.616 64.123 1   7.87  ? 93  GLU   D C     1 
ATOM   2620 O O     . GLU   B 1 112 ? 32.518  -57.682 63.015 1   8.65  ? 93  GLU   D O     1 
ATOM   2621 C CB    . GLU   B 1 112 ? 32.333  -59.188 65.981 1   6.01  ? 93  GLU   D CB    1 
ATOM   2622 C CG    . GLU   B 1 112 ? 30.916  -59.446 65.475 1   7.91  ? 93  GLU   D CG    1 
ATOM   2623 C CD    . GLU   B 1 112 ? 30.686  -60.685 64.623 1   13.21 ? 93  GLU   D CD    1 
ATOM   2624 O OE1   . GLU   B 1 112 ? 31.402  -61.697 64.807 1   10.07 ? 93  GLU   D OE1   1 
ATOM   2625 O OE2   . GLU   B 1 112 ? 29.768  -60.64  63.772 1   11.49 ? 93  GLU   D OE2   1 
ATOM   2626 N N     . LEU   B 1 113 ? 33.469  -56.446 64.696 1   10.34 ? 94  LEU   D N     1 
ATOM   2627 C CA    . LEU   B 1 113 ? 33.312  -55.116 64.083 1   12.38 ? 94  LEU   D CA    1 
ATOM   2628 C C     . LEU   B 1 113 ? 33.995  -55.092 62.71  1   9.15  ? 94  LEU   D C     1 
ATOM   2629 O O     . LEU   B 1 113 ? 33.378  -54.696 61.721 1   9.55  ? 94  LEU   D O     1 
ATOM   2630 C CB    . LEU   B 1 113 ? 33.999  -54.038 64.947 1   12.71 ? 94  LEU   D CB    1 
ATOM   2631 C CG    . LEU   B 1 113 ? 33.194  -53.293 65.999 1   8.57  ? 94  LEU   D CG    1 
ATOM   2632 C CD1   . LEU   B 1 113 ? 34.116  -52.436 66.854 1   8.93  ? 94  LEU   D CD1   1 
ATOM   2633 C CD2   . LEU   B 1 113 ? 32.184  -52.371 65.371 1   8.84  ? 94  LEU   D CD2   1 
ATOM   2634 N N     . GLU   B 1 114 ? 35.289  -55.496 62.681 1   11.74 ? 95  GLU   D N     1 
ATOM   2635 C CA    . GLU   B 1 114 ? 36.143  -55.539 61.496 1   11.49 ? 95  GLU   D CA    1 
ATOM   2636 C C     . GLU   B 1 114 ? 35.594  -56.447 60.396 1   7.95  ? 95  GLU   D C     1 
ATOM   2637 O O     . GLU   B 1 114 ? 35.741  -56.098 59.225 1   9.47  ? 95  GLU   D O     1 
ATOM   2638 C CB    . GLU   B 1 114 ? 37.588  -55.894 61.862 1   10.22 ? 95  GLU   D CB    1 
ATOM   2639 C CG    . GLU   B 1 114 ? 38.333  -54.681 62.386 1   11.22 ? 95  GLU   D CG    1 
ATOM   2640 C CD    . GLU   B 1 114 ? 39.708  -54.909 62.987 1   47.89 ? 95  GLU   D CD    1 
ATOM   2641 O OE1   . GLU   B 1 114 ? 39.86   -55.847 63.805 1   57.32 ? 95  GLU   D OE1   1 
ATOM   2642 O OE2   . GLU   B 1 114 ? 40.626  -54.119 62.666 1   45.91 ? 95  GLU   D OE2   1 
ATOM   2643 N N     . LYS   B 1 115 ? 34.914  -57.563 60.772 1   9.69  ? 96  LYS   D N     1 
ATOM   2644 C CA    . LYS   B 1 115 ? 34.25   -58.465 59.811 1   9.22  ? 96  LYS   D CA    1 
ATOM   2645 C C     . LYS   B 1 115 ? 33.2    -57.649 59.025 1   8.21  ? 96  LYS   D C     1 
ATOM   2646 O O     . LYS   B 1 115 ? 33.151  -57.738 57.792 1   9.36  ? 96  LYS   D O     1 
ATOM   2647 C CB    . LYS   B 1 115 ? 33.58   -59.651 60.53  1   11.19 ? 96  LYS   D CB    1 
ATOM   2648 C CG    . LYS   B 1 115 ? 34.551  -60.753 60.925 1   18.02 ? 96  LYS   D CG    1 
ATOM   2649 C CD    . LYS   B 1 115 ? 33.833  -61.899 61.629 1   27.11 ? 96  LYS   D CD    1 
ATOM   2650 C CE    . LYS   B 1 115 ? 34.814  -62.951 62.083 1   36.42 ? 96  LYS   D CE    1 
ATOM   2651 N NZ    . LYS   B 1 115 ? 34.142  -64.035 62.849 1   52.65 ? 96  LYS   D NZ    1 
ATOM   2652 N N     . TRP   B 1 116 ? 32.415  -56.784 59.734 1   6.01  ? 97  TRP   D N     1 
ATOM   2653 C CA    . TRP   B 1 116 ? 31.436  -55.939 59.06  1   4.3   ? 97  TRP   D CA    1 
ATOM   2654 C C     . TRP   B 1 116 ? 32.105  -54.837 58.237 1   8.01  ? 97  TRP   D C     1 
ATOM   2655 O O     . TRP   B 1 116 ? 31.701  -54.606 57.096 1   4.94  ? 97  TRP   D O     1 
ATOM   2656 C CB    . TRP   B 1 116 ? 30.371  -55.392 60.029 1   3.08  ? 97  TRP   D CB    1 
ATOM   2657 C CG    . TRP   B 1 116 ? 29.253  -54.708 59.305 1   3.8   ? 97  TRP   D CG    1 
ATOM   2658 C CD1   . TRP   B 1 116 ? 28.117  -55.284 58.815 1   6.99  ? 97  TRP   D CD1   1 
ATOM   2659 C CD2   . TRP   B 1 116 ? 29.214  -53.331 58.905 1   3.22  ? 97  TRP   D CD2   1 
ATOM   2660 N NE1   . TRP   B 1 116 ? 27.364  -54.346 58.148 1   7.15  ? 97  TRP   D NE1   1 
ATOM   2661 C CE2   . TRP   B 1 116 ? 28.013  -53.136 58.191 1   7.3   ? 97  TRP   D CE2   1 
ATOM   2662 C CE3   . TRP   B 1 116 ? 30.082  -52.242 59.081 1   3.96  ? 97  TRP   D CE3   1 
ATOM   2663 C CZ2   . TRP   B 1 116 ? 27.647  -51.889 57.67  1   6.77  ? 97  TRP   D CZ2   1 
ATOM   2664 C CZ3   . TRP   B 1 116 ? 29.729  -51.013 58.549 1   5.85  ? 97  TRP   D CZ3   1 
ATOM   2665 C CH2   . TRP   B 1 116 ? 28.522  -50.844 57.855 1   6.49  ? 97  TRP   D CH2   1 
ATOM   2666 N N     . LEU   B 1 117 ? 33.122  -54.166 58.81  1   7.88  ? 98  LEU   D N     1 
ATOM   2667 C CA    . LEU   B 1 117 ? 33.885  -53.097 58.163 1   10.07 ? 98  LEU   D CA    1 
ATOM   2668 C C     . LEU   B 1 117 ? 34.527  -53.56  56.833 1   9.85  ? 98  LEU   D C     1 
ATOM   2669 O O     . LEU   B 1 117 ? 34.527  -52.803 55.85  1   10.29 ? 98  LEU   D O     1 
ATOM   2670 C CB    . LEU   B 1 117 ? 34.978  -52.61  59.126 1   10.95 ? 98  LEU   D CB    1 
ATOM   2671 C CG    . LEU   B 1 117 ? 34.784  -51.286 59.904 1   8.37  ? 98  LEU   D CG    1 
ATOM   2672 C CD1   . LEU   B 1 117 ? 33.342  -50.874 60.048 1   8.17  ? 98  LEU   D CD1   1 
ATOM   2673 C CD2   . LEU   B 1 117 ? 35.475  -51.343 61.249 1   8.62  ? 98  LEU   D CD2   1 
ATOM   2674 N N     . LYS   B 1 118 ? 35.068  -54.791 56.813 1   12    ? 99  LYS   D N     1 
ATOM   2675 C CA    . LYS   B 1 118 ? 35.73   -55.38  55.64  1   13.11 ? 99  LYS   D CA    1 
ATOM   2676 C C     . LYS   B 1 118 ? 34.75   -56.13  54.718 1   17.8  ? 99  LYS   D C     1 
ATOM   2677 O O     . LYS   B 1 118 ? 35.177  -56.678 53.695 1   18.46 ? 99  LYS   D O     1 
ATOM   2678 C CB    . LYS   B 1 118 ? 36.891  -56.305 56.086 1   13.19 ? 99  LYS   D CB    1 
ATOM   2679 C CG    . LYS   B 1 118 ? 38.104  -55.54  56.616 1   24.59 ? 99  LYS   D CG    1 
ATOM   2680 C CD    . LYS   B 1 118 ? 38.989  -56.416 57.498 1   30.27 ? 99  LYS   D CD    1 
ATOM   2681 C CE    . LYS   B 1 118 ? 40.198  -55.659 57.995 1   45.78 ? 99  LYS   D CE    1 
ATOM   2682 N NZ    . LYS   B 1 118 ? 40.987  -56.455 58.976 1   54.66 ? 99  LYS   D NZ    1 
ATOM   2683 N N     . ALA   B 1 119 ? 33.435  -56.124 55.069 1   17.9  ? 100 ALA   D N     1 
ATOM   2684 C CA    . ALA   B 1 119 ? 32.337  -56.803 54.365 1   19.73 ? 100 ALA   D CA    1 
ATOM   2685 C C     . ALA   B 1 119 ? 32.649  -58.318 54.184 1   24.25 ? 100 ALA   D C     1 
ATOM   2686 O O     . ALA   B 1 119 ? 32.455  -58.895 53.105 1   25.61 ? 100 ALA   D O     1 
ATOM   2687 C CB    . ALA   B 1 119 ? 32.04   -56.114 53.03  1   20.45 ? 100 ALA   D CB    1 
ATOM   2688 N N     . ALA   B 1 120 ? 33.187  -58.937 55.261 1   23.18 ? 101 ALA   D N     1 
ATOM   2689 C CA    . ALA   B 1 120 ? 33.588  -60.346 55.33  1   23.87 ? 101 ALA   D CA    1 
ATOM   2690 C C     . ALA   B 1 120 ? 32.366  -61.281 55.302 1   27.82 ? 101 ALA   D C     1 
ATOM   2691 O O     . ALA   B 1 120 ? 31.274  -60.827 55.653 1   28.52 ? 101 ALA   D O     1 
ATOM   2692 C CB    . ALA   B 1 120 ? 34.422  -60.592 56.583 1   23.83 ? 101 ALA   D CB    1 
ATOM   2693 N N     . PRO   B 1 121 ? 32.506  -62.577 54.89  1   27.45 ? 102 PRO   D N     1 
ATOM   2694 C CA    . PRO   B 1 121 ? 31.325  -63.464 54.827 1   28.9  ? 102 PRO   D CA    1 
ATOM   2695 C C     . PRO   B 1 121 ? 30.581  -63.732 56.144 1   28.9  ? 102 PRO   D C     1 
ATOM   2696 O O     . PRO   B 1 121 ? 29.36   -63.923 56.12  1   30.9  ? 102 PRO   D O     1 
ATOM   2697 C CB    . PRO   B 1 121 ? 31.891  -64.763 54.241 1   31.31 ? 102 PRO   D CB    1 
ATOM   2698 C CG    . PRO   B 1 121 ? 33.344  -64.724 54.534 1   31.54 ? 102 PRO   D CG    1 
ATOM   2699 C CD    . PRO   B 1 121 ? 33.718  -63.277 54.41  1   28.28 ? 102 PRO   D CD    1 
ATOM   2700 N N     . ALA   B 1 122 ? 31.294  -63.743 57.286 1   24.05 ? 103 ALA   D N     1 
ATOM   2701 C CA    . ALA   B 1 122 ? 30.677  -64.011 58.595 1   22.55 ? 103 ALA   D CA    1 
ATOM   2702 C C     . ALA   B 1 122 ? 30.188  -62.734 59.325 1   18.73 ? 103 ALA   D C     1 
ATOM   2703 O O     . ALA   B 1 122 ? 29.896  -62.795 60.52  1   18.14 ? 103 ALA   D O     1 
ATOM   2704 C CB    . ALA   B 1 122 ? 31.637  -64.808 59.472 1   22.69 ? 103 ALA   D CB    1 
ATOM   2705 N N     . ALA   B 1 123 ? 30.074  -61.6   58.594 1   14.52 ? 104 ALA   D N     1 
ATOM   2706 C CA    . ALA   B 1 123 ? 29.626  -60.3   59.113 1   13.03 ? 104 ALA   D CA    1 
ATOM   2707 C C     . ALA   B 1 123 ? 28.146  -60.323 59.496 1   11.73 ? 104 ALA   D C     1 
ATOM   2708 O O     . ALA   B 1 123 ? 27.345  -60.972 58.816 1   12.63 ? 104 ALA   D O     1 
ATOM   2709 C CB    . ALA   B 1 123 ? 29.872  -59.205 58.079 1   12.73 ? 104 ALA   D CB    1 
ATOM   2710 N N     . PHE   B 1 124 ? 27.783  -59.626 60.602 1   8.5   ? 105 PHE   D N     1 
ATOM   2711 C CA    . PHE   B 1 124 ? 26.391  -59.533 61.051 1   6.76  ? 105 PHE   D CA    1 
ATOM   2712 C C     . PHE   B 1 124 ? 25.57   -58.734 60.039 1   9.88  ? 105 PHE   D C     1 
ATOM   2713 O O     . PHE   B 1 124 ? 26.082  -57.793 59.422 1   6.65  ? 105 PHE   D O     1 
ATOM   2714 C CB    . PHE   B 1 124 ? 26.299  -58.878 62.453 1   5.78  ? 105 PHE   D CB    1 
ATOM   2715 C CG    . PHE   B 1 124 ? 24.911  -58.865 63.066 1   6.99  ? 105 PHE   D CG    1 
ATOM   2716 C CD1   . PHE   B 1 124 ? 24.329  -60.035 63.546 1   10.7  ? 105 PHE   D CD1   1 
ATOM   2717 C CD2   . PHE   B 1 124 ? 24.198  -57.678 63.192 1   8.92  ? 105 PHE   D CD2   1 
ATOM   2718 C CE1   . PHE   B 1 124 ? 23.042  -60.02  64.105 1   11.16 ? 105 PHE   D CE1   1 
ATOM   2719 C CE2   . PHE   B 1 124 ? 22.914  -57.663 63.762 1   9.87  ? 105 PHE   D CE2   1 
ATOM   2720 C CZ    . PHE   B 1 124 ? 22.35   -58.833 64.219 1   10.87 ? 105 PHE   D CZ    1 
ATOM   2721 N N     . ASP   B 1 125 ? 24.287  -59.11  59.886 1   10.22 ? 106 ASP   D N     1 
ATOM   2722 C CA    . ASP   B 1 125 ? 23.359  -58.447 58.976 1   11.36 ? 106 ASP   D CA    1 
ATOM   2723 C C     . ASP   B 1 125 ? 22.7    -57.247 59.667 1   12.26 ? 106 ASP   D C     1 
ATOM   2724 O O     . ASP   B 1 125 ? 21.75   -57.416 60.434 1   11.5  ? 106 ASP   D O     1 
ATOM   2725 C CB    . ASP   B 1 125 ? 22.296  -59.442 58.45  1   15.67 ? 106 ASP   D CB    1 
ATOM   2726 C CG    . ASP   B 1 125 ? 21.352  -58.846 57.416 1   24.6  ? 106 ASP   D CG    1 
ATOM   2727 O OD1   . ASP   B 1 125 ? 21.769  -57.898 56.7   1   24.04 ? 106 ASP   D OD1   1 
ATOM   2728 O OD2   . ASP   B 1 125 ? 20.198  -59.339 57.307 1   34.78 ? 106 ASP   D OD2   1 
ATOM   2729 N N     . TRP   B 1 126 ? 23.213  -56.041 59.38  1   8.17  ? 107 TRP   D N     1 
ATOM   2730 C CA    . TRP   B 1 126 ? 22.709  -54.772 59.926 1   7.76  ? 107 TRP   D CA    1 
ATOM   2731 C C     . TRP   B 1 126 ? 21.683  -54.105 58.992 1   11.53 ? 107 TRP   D C     1 
ATOM   2732 O O     . TRP   B 1 126 ? 21.113  -53.072 59.36  1   8.49  ? 107 TRP   D O     1 
ATOM   2733 C CB    . TRP   B 1 126 ? 23.885  -53.811 60.2   1   5.14  ? 107 TRP   D CB    1 
ATOM   2734 C CG    . TRP   B 1 126 ? 24.688  -54.177 61.417 1   4.11  ? 107 TRP   D CG    1 
ATOM   2735 C CD1   . TRP   B 1 126 ? 25.918  -54.776 61.45  1   6.05  ? 107 TRP   D CD1   1 
ATOM   2736 C CD2   . TRP   B 1 126 ? 24.314  -53.946 62.79  1   3     ? 107 TRP   D CD2   1 
ATOM   2737 N NE1   . TRP   B 1 126 ? 26.332  -54.938 62.758 1   4.94  ? 107 TRP   D NE1   1 
ATOM   2738 C CE2   . TRP   B 1 126 ? 25.364  -54.435 63.6   1   6.28  ? 107 TRP   D CE2   1 
ATOM   2739 C CE3   . TRP   B 1 126 ? 23.185  -53.378 63.412 1   3.67  ? 107 TRP   D CE3   1 
ATOM   2740 C CZ2   . TRP   B 1 126 ? 25.323  -54.359 65.002 1   5.16  ? 107 TRP   D CZ2   1 
ATOM   2741 C CZ3   . TRP   B 1 126 ? 23.149  -53.3   64.803 1   4.51  ? 107 TRP   D CZ3   1 
ATOM   2742 C CH2   . TRP   B 1 126 ? 24.201  -53.794 65.58  1   4.82  ? 107 TRP   D CH2   1 
ATOM   2743 N N     . SER   B 1 127 ? 21.421  -54.712 57.796 1   10.83 ? 108 SER   D N     1 
ATOM   2744 C CA    . SER   B 1 127 ? 20.488  -54.177 56.791 1   13.19 ? 108 SER   D CA    1 
ATOM   2745 C C     . SER   B 1 127 ? 19.121  -53.683 57.352 1   16.66 ? 108 SER   D C     1 
ATOM   2746 O O     . SER   B 1 127 ? 18.746  -52.584 56.933 1   16.98 ? 108 SER   D O     1 
ATOM   2747 C CB    . SER   B 1 127 ? 20.287  -55.15  55.627 1   17.87 ? 108 SER   D CB    1 
ATOM   2748 O OG    . SER   B 1 127 ? 19.532  -56.294 55.992 1   25.7  ? 108 SER   D OG    1 
ATOM   2749 N N     . PRO   B 1 128 ? 18.383  -54.357 58.3   1   15.4  ? 109 PRO   D N     1 
ATOM   2750 C CA    . PRO   B 1 128 ? 17.114  -53.768 58.787 1   15.97 ? 109 PRO   D CA    1 
ATOM   2751 C C     . PRO   B 1 128 ? 17.319  -52.496 59.619 1   15.03 ? 109 PRO   D C     1 
ATOM   2752 O O     . PRO   B 1 128 ? 16.455  -51.607 59.623 1   15.13 ? 109 PRO   D O     1 
ATOM   2753 C CB    . PRO   B 1 128 ? 16.491  -54.887 59.636 1   16.96 ? 109 PRO   D CB    1 
ATOM   2754 C CG    . PRO   B 1 128 ? 17.274  -56.121 59.324 1   18.64 ? 109 PRO   D CG    1 
ATOM   2755 C CD    . PRO   B 1 128 ? 18.634  -55.658 58.955 1   15.34 ? 109 PRO   D CD    1 
ATOM   2756 N N     . VAL   B 1 129 ? 18.463  -52.414 60.338 1   11.03 ? 110 VAL   D N     1 
ATOM   2757 C CA    . VAL   B 1 129 ? 18.827  -51.243 61.153 1   8.14  ? 110 VAL   D CA    1 
ATOM   2758 C C     . VAL   B 1 129 ? 19.247  -50.107 60.195 1   9.49  ? 110 VAL   D C     1 
ATOM   2759 O O     . VAL   B 1 129 ? 18.801  -48.97  60.367 1   7.84  ? 110 VAL   D O     1 
ATOM   2760 C CB    . VAL   B 1 129 ? 19.922  -51.594 62.207 1   9.06  ? 110 VAL   D CB    1 
ATOM   2761 C CG1   . VAL   B 1 129 ? 20.426  -50.35  62.947 1   6.47  ? 110 VAL   D CG1   1 
ATOM   2762 C CG2   . VAL   B 1 129 ? 19.404  -52.632 63.204 1   8.69  ? 110 VAL   D CG2   1 
ATOM   2763 N N     . VAL   B 1 130 ? 20.059  -50.435 59.166 1   8.42  ? 111 VAL   D N     1 
ATOM   2764 C CA    . VAL   B 1 130 ? 20.526  -49.49  58.141 1   8.51  ? 111 VAL   D CA    1 
ATOM   2765 C C     . VAL   B 1 130 ? 19.322  -48.865 57.405 1   13.54 ? 111 VAL   D C     1 
ATOM   2766 O O     . VAL   B 1 130 ? 19.296  -47.647 57.215 1   12.37 ? 111 VAL   D O     1 
ATOM   2767 C CB    . VAL   B 1 130 ? 21.561  -50.147 57.176 1   11.74 ? 111 VAL   D CB    1 
ATOM   2768 C CG1   . VAL   B 1 130 ? 21.882  -49.251 55.98  1   12.62 ? 111 VAL   D CG1   1 
ATOM   2769 C CG2   . VAL   B 1 130 ? 22.848  -50.522 57.92  1   9.75  ? 111 VAL   D CG2   1 
ATOM   2770 N N     . THR   B 1 131 ? 18.315  -49.697 57.042 1   12.93 ? 112 THR   D N     1 
ATOM   2771 C CA    . THR   B 1 131 ? 17.09   -49.258 56.356 1   15.49 ? 112 THR   D CA    1 
ATOM   2772 C C     . THR   B 1 131 ? 16.328  -48.286 57.252 1   17.76 ? 112 THR   D C     1 
ATOM   2773 O O     . THR   B 1 131 ? 15.868  -47.247 56.766 1   19.36 ? 112 THR   D O     1 
ATOM   2774 C CB    . THR   B 1 131 ? 16.23   -50.472 55.928 1   20.47 ? 112 THR   D CB    1 
ATOM   2775 O OG1   . THR   B 1 131 ? 16.966  -51.268 55.004 1   18.5  ? 112 THR   D OG1   1 
ATOM   2776 C CG2   . THR   B 1 131 ? 14.893  -50.068 55.286 1   23.56 ? 112 THR   D CG2   1 
ATOM   2777 N N     . TYR   B 1 132 ? 16.221  -48.616 58.561 1   13.3  ? 113 TYR   D N     1 
ATOM   2778 C CA    . TYR   B 1 132 ? 15.518  -47.788 59.539 1   12.37 ? 113 TYR   D CA    1 
ATOM   2779 C C     . TYR   B 1 132 ? 16.138  -46.384 59.619 1   13.64 ? 113 TYR   D C     1 
ATOM   2780 O O     . TYR   B 1 132 ? 15.404  -45.399 59.566 1   12.43 ? 113 TYR   D O     1 
ATOM   2781 C CB    . TYR   B 1 132 ? 15.461  -48.482 60.917 1   11.52 ? 113 TYR   D CB    1 
ATOM   2782 C CG    . TYR   B 1 132 ? 14.569  -47.775 61.922 1   12.72 ? 113 TYR   D CG    1 
ATOM   2783 C CD1   . TYR   B 1 132 ? 13.197  -48.02  61.964 1   14.47 ? 113 TYR   D CD1   1 
ATOM   2784 C CD2   . TYR   B 1 132 ? 15.102  -46.892 62.858 1   11.25 ? 113 TYR   D CD2   1 
ATOM   2785 C CE1   . TYR   B 1 132 ? 12.373  -47.372 62.893 1   13.97 ? 113 TYR   D CE1   1 
ATOM   2786 C CE2   . TYR   B 1 132 ? 14.289  -46.23  63.779 1   10.86 ? 113 TYR   D CE2   1 
ATOM   2787 C CZ    . TYR   B 1 132 ? 12.929  -46.486 63.807 1   14.61 ? 113 TYR   D CZ    1 
ATOM   2788 O OH    . TYR   B 1 132 ? 12.141  -45.834 64.731 1   15.27 ? 113 TYR   D OH    1 
ATOM   2789 N N     . VAL   B 1 133 ? 17.486  -46.297 59.683 1   9.05  ? 114 VAL   D N     1 
ATOM   2790 C CA    . VAL   B 1 133 ? 18.215  -45.015 59.727 1   7.69  ? 114 VAL   D CA    1 
ATOM   2791 C C     . VAL   B 1 133 ? 18.001  -44.205 58.418 1   11.75 ? 114 VAL   D C     1 
ATOM   2792 O O     . VAL   B 1 133 ? 17.741  -43.003 58.484 1   9.93  ? 114 VAL   D O     1 
ATOM   2793 C CB    . VAL   B 1 133 ? 19.715  -45.209 60.096 1   8.46  ? 114 VAL   D CB    1 
ATOM   2794 C CG1   . VAL   B 1 133 ? 20.49   -43.897 60.025 1   7.39  ? 114 VAL   D CG1   1 
ATOM   2795 C CG2   . VAL   B 1 133 ? 19.856  -45.84  61.48  1   6.19  ? 114 VAL   D CG2   1 
ATOM   2796 N N     . CYS   B 1 134 ? 18.063  -44.875 57.247 1   11.47 ? 115 CYS   D N     1 
ATOM   2797 C CA    . CYS   B 1 134 ? 17.819  -44.23  55.949 1   14.27 ? 115 CYS   D CA    1 
ATOM   2798 C C     . CYS   B 1 134 ? 16.425  -43.579 55.911 1   19.87 ? 115 CYS   D C     1 
ATOM   2799 O O     . CYS   B 1 134 ? 16.313  -42.454 55.428 1   20.59 ? 115 CYS   D O     1 
ATOM   2800 C CB    . CYS   B 1 134 ? 18.019  -45.213 54.799 1   16.28 ? 115 CYS   D CB    1 
ATOM   2801 S SG    . CYS   B 1 134 ? 19.745  -45.686 54.536 1   17.77 ? 115 CYS   D SG    1 
ATOM   2802 N N     . ASP   B 1 135 ? 15.395  -44.243 56.503 1   19.95 ? 116 ASP   D N     1 
ATOM   2803 C CA    . ASP   B 1 135 ? 14.024  -43.721 56.607 1   22.19 ? 116 ASP   D CA    1 
ATOM   2804 C C     . ASP   B 1 135 ? 13.969  -42.457 57.48  1   23.96 ? 116 ASP   D C     1 
ATOM   2805 O O     . ASP   B 1 135 ? 13.353  -41.469 57.073 1   25.65 ? 116 ASP   D O     1 
ATOM   2806 C CB    . ASP   B 1 135 ? 13.049  -44.777 57.179 1   24.12 ? 116 ASP   D CB    1 
ATOM   2807 C CG    . ASP   B 1 135 ? 12.908  -46.069 56.395 1   39.39 ? 116 ASP   D CG    1 
ATOM   2808 O OD1   . ASP   B 1 135 ? 12.883  -46.009 55.139 1   41.83 ? 116 ASP   D OD1   1 
ATOM   2809 O OD2   . ASP   B 1 135 ? 12.806  -47.142 57.037 1   46.98 ? 116 ASP   D OD2   1 
ATOM   2810 N N     . LEU   B 1 136 ? 14.592  -42.499 58.687 1   18.39 ? 117 LEU   D N     1 
ATOM   2811 C CA    . LEU   B 1 136 ? 14.643  -41.376 59.634 1   16.71 ? 117 LEU   D CA    1 
ATOM   2812 C C     . LEU   B 1 136 ? 15.246  -40.117 58.985 1   18.77 ? 117 LEU   D C     1 
ATOM   2813 O O     . LEU   B 1 136 ? 14.72   -39.019 59.173 1   17.98 ? 117 LEU   D O     1 
ATOM   2814 C CB    . LEU   B 1 136 ? 15.505  -41.723 60.886 1   13.93 ? 117 LEU   D CB    1 
ATOM   2815 C CG    . LEU   B 1 136 ? 15.139  -42.909 61.785 1   14.11 ? 117 LEU   D CG    1 
ATOM   2816 C CD1   . LEU   B 1 136 ? 16.173  -43.069 62.905 1   11.56 ? 117 LEU   D CD1   1 
ATOM   2817 C CD2   . LEU   B 1 136 ? 13.731  -42.763 62.385 1   16.52 ? 117 LEU   D CD2   1 
ATOM   2818 N N     . GLU   B 1 137 ? 16.346  -40.298 58.218 1   17.95 ? 118 GLU   D N     1 
ATOM   2819 C CA    . GLU   B 1 137 ? 17.145  -39.248 57.577 1   18.53 ? 118 GLU   D CA    1 
ATOM   2820 C C     . GLU   B 1 137 ? 16.528  -38.642 56.296 1   28.25 ? 118 GLU   D C     1 
ATOM   2821 O O     . GLU   B 1 137 ? 17.211  -37.9   55.577 1   28.98 ? 118 GLU   D O     1 
ATOM   2822 C CB    . GLU   B 1 137 ? 18.577  -39.76  57.315 1   18.16 ? 118 GLU   D CB    1 
ATOM   2823 C CG    . GLU   B 1 137 ? 19.325  -40.104 58.595 1   22.99 ? 118 GLU   D CG    1 
ATOM   2824 C CD    . GLU   B 1 137 ? 20.814  -40.384 58.502 1   38.13 ? 118 GLU   D CD    1 
ATOM   2825 O OE1   . GLU   B 1 137 ? 21.352  -40.383 57.37  1   27.05 ? 118 GLU   D OE1   1 
ATOM   2826 O OE2   . GLU   B 1 137 ? 21.445  -40.596 59.568 1   17.11 ? 118 GLU   D OE2   1 
ATOM   2827 N N     . GLY   B 1 138 ? 15.247  -38.93  56.05  1   29.4  ? 119 GLY   D N     1 
ATOM   2828 C CA    . GLY   B 1 138 ? 14.494  -38.397 54.917 1   33.21 ? 119 GLY   D CA    1 
ATOM   2829 C C     . GLY   B 1 138 ? 14.583  -39.168 53.615 1   39.12 ? 119 GLY   D C     1 
ATOM   2830 O O     . GLY   B 1 138 ? 14.176  -38.639 52.573 1   42.71 ? 119 GLY   D O     1 
ATOM   2831 N N     . ASN   B 1 139 ? 15.088  -40.431 53.659 1   34.92 ? 120 ASN   D N     1 
ATOM   2832 C CA    . ASN   B 1 139 ? 15.255  -41.32  52.495 1   36.89 ? 120 ASN   D CA    1 
ATOM   2833 C C     . ASN   B 1 139 ? 16.116  -40.676 51.382 1   40.33 ? 120 ASN   D C     1 
ATOM   2834 O O     . ASN   B 1 139 ? 15.835  -40.848 50.18  1   43.59 ? 120 ASN   D O     1 
ATOM   2835 C CB    . ASN   B 1 139 ? 13.895  -41.837 51.966 1   41.15 ? 120 ASN   D CB    1 
ATOM   2836 C CG    . ASN   B 1 139 ? 13.32   -42.991 52.754 1   55.79 ? 120 ASN   D CG    1 
ATOM   2837 O OD1   . ASN   B 1 139 ? 13.853  -44.111 52.752 1   54.07 ? 120 ASN   D OD1   1 
ATOM   2838 N ND2   . ASN   B 1 139 ? 12.208  -42.746 53.435 1   47.13 ? 120 ASN   D ND2   1 
ATOM   2839 N N     . ARG   B 1 140 ? 17.158  -39.918 51.799 1   33.86 ? 121 ARG   D N     1 
ATOM   2840 C CA    . ARG   B 1 140 ? 18.092  -39.232 50.898 1   33.98 ? 121 ARG   D CA    1 
ATOM   2841 C C     . ARG   B 1 140 ? 18.942  -40.256 50.149 1   35.83 ? 121 ARG   D C     1 
ATOM   2842 O O     . ARG   B 1 140 ? 19.214  -40.082 48.958 1   36.82 ? 121 ARG   D O     1 
ATOM   2843 C CB    . ARG   B 1 140 ? 19.007  -38.264 51.673 1   31.49 ? 121 ARG   D CB    1 
ATOM   2844 C CG    . ARG   B 1 140 ? 18.311  -37.035 52.248 1   41.43 ? 121 ARG   D CG    1 
ATOM   2845 C CD    . ARG   B 1 140 ? 19.325  -36.165 52.975 1   47.7  ? 121 ARG   D CD    1 
ATOM   2846 N NE    . ARG   B 1 140 ? 18.707  -35.268 53.955 1   57.48 ? 121 ARG   D NE    1 
ATOM   2847 C CZ    . ARG   B 1 140 ? 18.297  -34.031 53.687 1   73.45 ? 121 ARG   D CZ    1 
ATOM   2848 N NH1   . ARG   B 1 140 ? 18.405  -33.539 52.457 1   59.22 ? 121 ARG   D NH1   1 
ATOM   2849 N NH2   . ARG   B 1 140 ? 17.764  -33.281 54.644 1   59.8  ? 121 ARG   D NH2   1 
ATOM   2850 N N     . VAL   B 1 141 ? 19.375  -41.319 50.868 1   30.98 ? 122 VAL   D N     1 
ATOM   2851 C CA    . VAL   B 1 141 ? 20.21   -42.41  50.344 1   29.7  ? 122 VAL   D CA    1 
ATOM   2852 C C     . VAL   B 1 141 ? 19.554  -43.79  50.595 1   32.01 ? 122 VAL   D C     1 
ATOM   2853 O O     . VAL   B 1 141 ? 18.618  -43.892 51.401 1   32.49 ? 122 VAL   D O     1 
ATOM   2854 C CB    . VAL   B 1 141 ? 21.674  -42.356 50.89  1   28.35 ? 122 VAL   D CB    1 
ATOM   2855 C CG1   . VAL   B 1 141 ? 22.314  -40.988 50.662 1   27.43 ? 122 VAL   D CG1   1 
ATOM   2856 C CG2   . VAL   B 1 141 ? 21.75   -42.752 52.367 1   25.64 ? 122 VAL   D CG2   1 
ATOM   2857 N N     . LYS   B 1 142 ? 20.07   -44.842 49.927 1   27.62 ? 123 LYS   D N     1 
ATOM   2858 C CA    . LYS   B 1 142 ? 19.633  -46.227 50.118 1   27.57 ? 123 LYS   D CA    1 
ATOM   2859 C C     . LYS   B 1 142 ? 20.696  -46.973 50.962 1   26.75 ? 123 LYS   D C     1 
ATOM   2860 O O     . LYS   B 1 142 ? 21.799  -46.449 51.146 1   23.26 ? 123 LYS   D O     1 
ATOM   2861 C CB    . LYS   B 1 142 ? 19.4    -46.929 48.773 1   31.66 ? 123 LYS   D CB    1 
ATOM   2862 C CG    . LYS   B 1 142 ? 18.05   -46.597 48.143 1   41.13 ? 123 LYS   D CG    1 
ATOM   2863 C CD    . LYS   B 1 142 ? 17.808  -47.432 46.891 1   50.78 ? 123 LYS   D CD    1 
ATOM   2864 C CE    . LYS   B 1 142 ? 16.536  -47.055 46.164 1   61.86 ? 123 LYS   D CE    1 
ATOM   2865 N NZ    . LYS   B 1 142 ? 15.321  -47.527 46.882 1   68.32 ? 123 LYS   D NZ    1 
ATOM   2866 N N     . GLY   B 1 143 ? 20.34   -48.171 51.447 1   25.23 ? 124 GLY   D N     1 
ATOM   2867 C CA    . GLY   B 1 143 ? 21.171  -49.044 52.281 1   22.7  ? 124 GLY   D CA    1 
ATOM   2868 C C     . GLY   B 1 143 ? 22.643  -49.195 51.918 1   22.59 ? 124 GLY   D C     1 
ATOM   2869 O O     . GLY   B 1 143 ? 23.499  -48.913 52.77  1   19.02 ? 124 GLY   D O     1 
ATOM   2870 N N     . PRO   B 1 144 ? 22.993  -49.639 50.67  1   20.93 ? 125 PRO   D N     1 
ATOM   2871 C CA    . PRO   B 1 144 ? 24.419  -49.803 50.315 1   18.52 ? 125 PRO   D CA    1 
ATOM   2872 C C     . PRO   B 1 144 ? 25.248  -48.516 50.372 1   19.5  ? 125 PRO   D C     1 
ATOM   2873 O O     . PRO   B 1 144 ? 26.418  -48.571 50.765 1   17.65 ? 125 PRO   D O     1 
ATOM   2874 C CB    . PRO   B 1 144 ? 24.374  -50.395 48.897 1   21.37 ? 125 PRO   D CB    1 
ATOM   2875 C CG    . PRO   B 1 144 ? 22.998  -50.956 48.759 1   27.18 ? 125 PRO   D CG    1 
ATOM   2876 C CD    . PRO   B 1 144 ? 22.124  -50.04  49.543 1   25.06 ? 125 PRO   D CD    1 
ATOM   2877 N N     . GLU   B 1 145 ? 24.64   -47.36  50.012 1   17.93 ? 126 GLU   D N     1 
ATOM   2878 C CA    . GLU   B 1 145 ? 25.292  -46.046 50.05  1   16.52 ? 126 GLU   D CA    1 
ATOM   2879 C C     . GLU   B 1 145 ? 25.61   -45.652 51.508 1   15.17 ? 126 GLU   D C     1 
ATOM   2880 O O     . GLU   B 1 145 ? 26.714  -45.169 51.784 1   12.22 ? 126 GLU   D O     1 
ATOM   2881 C CB    . GLU   B 1 145 ? 24.392  -44.98  49.408 1   20.07 ? 126 GLU   D CB    1 
ATOM   2882 C CG    . GLU   B 1 145 ? 25.158  -43.756 48.931 1   28.72 ? 126 GLU   D CG    1 
ATOM   2883 C CD    . GLU   B 1 145 ? 24.342  -42.688 48.223 1   44.95 ? 126 GLU   D CD    1 
ATOM   2884 O OE1   . GLU   B 1 145 ? 23.375  -43.038 47.502 1   37.14 ? 126 GLU   D OE1   1 
ATOM   2885 O OE2   . GLU   B 1 145 ? 24.682  -41.493 48.387 1   33.07 ? 126 GLU   D OE2   1 
ATOM   2886 N N     . LYS   B 1 146 ? 24.633  -45.861 52.427 1   12.1  ? 127 LYS   D N     1 
ATOM   2887 C CA    . LYS   B 1 146 ? 24.764  -45.576 53.864 1   9.11  ? 127 LYS   D CA    1 
ATOM   2888 C C     . LYS   B 1 146 ? 25.939  -46.388 54.445 1   9.07  ? 127 LYS   D C     1 
ATOM   2889 O O     . LYS   B 1 146 ? 26.818  -45.817 55.092 1   5.41  ? 127 LYS   D O     1 
ATOM   2890 C CB    . LYS   B 1 146 ? 23.446  -45.913 54.591 1   11.82 ? 127 LYS   D CB    1 
ATOM   2891 C CG    . LYS   B 1 146 ? 23.516  -45.881 56.129 1   13.58 ? 127 LYS   D CG    1 
ATOM   2892 C CD    . LYS   B 1 146 ? 22.881  -44.631 56.727 1   18.16 ? 127 LYS   D CD    1 
ATOM   2893 C CE    . LYS   B 1 146 ? 23.868  -43.512 56.839 1   16.2  ? 127 LYS   D CE    1 
ATOM   2894 N NZ    . LYS   B 1 146 ? 23.305  -42.358 57.579 1   17.19 ? 127 LYS   D NZ    1 
ATOM   2895 N N     . GLU   B 1 147 ? 25.961  -47.71  54.175 1   7.05  ? 128 GLU   D N     1 
ATOM   2896 C CA    . GLU   B 1 147 ? 27.006  -48.627 54.633 1   6.61  ? 128 GLU   D CA    1 
ATOM   2897 C C     . GLU   B 1 147 ? 28.382  -48.215 54.132 1   8.79  ? 128 GLU   D C     1 
ATOM   2898 O O     . GLU   B 1 147 ? 29.343  -48.218 54.916 1   8.07  ? 128 GLU   D O     1 
ATOM   2899 C CB    . GLU   B 1 147 ? 26.706  -50.064 54.199 1   9.23  ? 128 GLU   D CB    1 
ATOM   2900 C CG    . GLU   B 1 147 ? 25.518  -50.68  54.917 1   14.56 ? 128 GLU   D CG    1 
ATOM   2901 C CD    . GLU   B 1 147 ? 25.402  -52.19  54.792 1   35.05 ? 128 GLU   D CD    1 
ATOM   2902 O OE1   . GLU   B 1 147 ? 26.326  -52.83  54.236 1   26.02 ? 128 GLU   D OE1   1 
ATOM   2903 O OE2   . GLU   B 1 147 ? 24.378  -52.733 55.264 1   30.6  ? 128 GLU   D OE2   1 
ATOM   2904 N N     . GLU   B 1 148 ? 28.486  -47.833 52.839 1   9.91  ? 129 GLU   D N     1 
ATOM   2905 C CA    . GLU   B 1 148 ? 29.768  -47.406 52.273 1   9.76  ? 129 GLU   D CA    1 
ATOM   2906 C C     . GLU   B 1 148 ? 30.292  -46.141 52.958 1   8.6   ? 129 GLU   D C     1 
ATOM   2907 O O     . GLU   B 1 148 ? 31.498  -46.066 53.252 1   8.43  ? 129 GLU   D O     1 
ATOM   2908 C CB    . GLU   B 1 148 ? 29.703  -47.264 50.73  1   10.84 ? 129 GLU   D CB    1 
ATOM   2909 C CG    . GLU   B 1 148 ? 31.049  -46.991 50.063 1   15.16 ? 129 GLU   D CG    1 
ATOM   2910 C CD    . GLU   B 1 148 ? 32.216  -47.916 50.369 1   34.23 ? 129 GLU   D CD    1 
ATOM   2911 O OE1   . GLU   B 1 148 ? 31.991  -49.118 50.645 1   29.28 ? 129 GLU   D OE1   1 
ATOM   2912 O OE2   . GLU   B 1 148 ? 33.37   -47.43  50.318 1   32.75 ? 129 GLU   D OE2   1 
ATOM   2913 N N     . LYS   B 1 149 ? 29.393  -45.177 53.264 1   7.19  ? 130 LYS   D N     1 
ATOM   2914 C CA    . LYS   B 1 149 ? 29.777  -43.957 53.975 1   5.52  ? 130 LYS   D CA    1 
ATOM   2915 C C     . LYS   B 1 149 ? 30.349  -44.3   55.371 1   5.63  ? 130 LYS   D C     1 
ATOM   2916 O O     . LYS   B 1 149 ? 31.369  -43.727 55.76  1   3.01  ? 130 LYS   D O     1 
ATOM   2917 C CB    . LYS   B 1 149 ? 28.61   -42.954 54.081 1   8.06  ? 130 LYS   D CB    1 
ATOM   2918 C CG    . LYS   B 1 149 ? 29.121  -41.553 54.428 1   9.21  ? 130 LYS   D CG    1 
ATOM   2919 C CD    . LYS   B 1 149 ? 28.16   -40.44  54.084 1   20.95 ? 130 LYS   D CD    1 
ATOM   2920 C CE    . LYS   B 1 149 ? 28.835  -39.109 54.305 1   29.22 ? 130 LYS   D CE    1 
ATOM   2921 N NZ    . LYS   B 1 149 ? 27.918  -37.965 54.044 1   40.8  ? 130 LYS   D NZ    1 
ATOM   2922 N N     . LEU   B 1 150 ? 29.722  -45.255 56.094 1   3.1   ? 131 LEU   D N     1 
ATOM   2923 C CA    . LEU   B 1 150 ? 30.229  -45.678 57.417 1   3     ? 131 LEU   D CA    1 
ATOM   2924 C C     . LEU   B 1 150 ? 31.598  -46.353 57.295 1   5.97  ? 131 LEU   D C     1 
ATOM   2925 O O     . LEU   B 1 150 ? 32.538  -45.96  57.993 1   3     ? 131 LEU   D O     1 
ATOM   2926 C CB    . LEU   B 1 150 ? 29.229  -46.57  58.188 1   3     ? 131 LEU   D CB    1 
ATOM   2927 C CG    . LEU   B 1 150 ? 29.677  -47.039 59.597 1   6.97  ? 131 LEU   D CG    1 
ATOM   2928 C CD1   . LEU   B 1 150 ? 30.13   -45.865 60.469 1   5.79  ? 131 LEU   D CD1   1 
ATOM   2929 C CD2   . LEU   B 1 150 ? 28.575  -47.822 60.288 1   5.88  ? 131 LEU   D CD2   1 
ATOM   2930 N N     . ARG   B 1 151 ? 31.725  -47.339 56.371 1   3     ? 132 ARG   D N     1 
ATOM   2931 C CA    . ARG   B 1 151 ? 32.991  -48.046 56.137 1   3     ? 132 ARG   D CA    1 
ATOM   2932 C C     . ARG   B 1 151 ? 34.13   -47.096 55.783 1   7.32  ? 132 ARG   D C     1 
ATOM   2933 O O     . ARG   B 1 151 ? 35.251  -47.307 56.246 1   6.24  ? 132 ARG   D O     1 
ATOM   2934 C CB    . ARG   B 1 151 ? 32.835  -49.15  55.087 1   3     ? 132 ARG   D CB    1 
ATOM   2935 C CG    . ARG   B 1 151 ? 31.998  -50.315 55.574 1   3     ? 132 ARG   D CG    1 
ATOM   2936 C CD    . ARG   B 1 151 ? 31.903  -51.409 54.526 1   8.7   ? 132 ARG   D CD    1 
ATOM   2937 N NE    . ARG   B 1 151 ? 31.272  -52.602 55.089 1   10.11 ? 132 ARG   D NE    1 
ATOM   2938 C CZ    . ARG   B 1 151 ? 30.071  -53.047 54.749 1   10.98 ? 132 ARG   D CZ    1 
ATOM   2939 N NH1   . ARG   B 1 151 ? 29.37   -52.432 53.8   1   6.57  ? 132 ARG   D NH1   1 
ATOM   2940 N NH2   . ARG   B 1 151 ? 29.566  -54.123 55.339 1   3.83  ? 132 ARG   D NH2   1 
ATOM   2941 N N     . GLN   B 1 152 ? 33.839  -46.019 55.015 1   5.6   ? 133 GLN   D N     1 
ATOM   2942 C CA    . GLN   B 1 152 ? 34.859  -45.027 54.653 1   6.08  ? 133 GLN   D CA    1 
ATOM   2943 C C     . GLN   B 1 152 ? 35.254  -44.153 55.85  1   6.16  ? 133 GLN   D C     1 
ATOM   2944 O O     . GLN   B 1 152 ? 36.428  -43.765 55.96  1   7.05  ? 133 GLN   D O     1 
ATOM   2945 C CB    . GLN   B 1 152 ? 34.398  -44.145 53.478 1   8.13  ? 133 GLN   D CB    1 
ATOM   2946 C CG    . GLN   B 1 152 ? 34.486  -44.842 52.111 1   20.05 ? 133 GLN   D CG    1 
ATOM   2947 C CD    . GLN   B 1 152 ? 35.886  -45.324 51.767 1   40.62 ? 133 GLN   D CD    1 
ATOM   2948 O OE1   . GLN   B 1 152 ? 36.864  -44.557 51.786 1   39.1  ? 133 GLN   D OE1   1 
ATOM   2949 N NE2   . GLN   B 1 152 ? 36.011  -46.612 51.451 1   29.67 ? 133 GLN   D NE2   1 
ATOM   2950 N N     . ALA   B 1 153 ? 34.279  -43.852 56.743 1   5.91  ? 134 ALA   D N     1 
ATOM   2951 C CA    . ALA   B 1 153 ? 34.506  -43.01  57.924 1   5.04  ? 134 ALA   D CA    1 
ATOM   2952 C C     . ALA   B 1 153 ? 35.39   -43.694 58.973 1   6.9   ? 134 ALA   D C     1 
ATOM   2953 O O     . ALA   B 1 153 ? 36.25   -43.03  59.57  1   6.06  ? 134 ALA   D O     1 
ATOM   2954 C CB    . ALA   B 1 153 ? 33.174  -42.586 58.541 1   5.44  ? 134 ALA   D CB    1 
ATOM   2955 N N     . VAL   B 1 154 ? 35.188  -45.012 59.197 1   3     ? 135 VAL   D N     1 
ATOM   2956 C CA    . VAL   B 1 154 ? 35.948  -45.747 60.22  1   3     ? 135 VAL   D CA    1 
ATOM   2957 C C     . VAL   B 1 154 ? 37.399  -45.99  59.773 1   7.62  ? 135 VAL   D C     1 
ATOM   2958 O O     . VAL   B 1 154 ? 37.672  -46.871 58.952 1   6.55  ? 135 VAL   D O     1 
ATOM   2959 C CB    . VAL   B 1 154 ? 35.25   -47.034 60.722 1   3.96  ? 135 VAL   D CB    1 
ATOM   2960 C CG1   . VAL   B 1 154 ? 36.031  -47.653 61.885 1   3     ? 135 VAL   D CG1   1 
ATOM   2961 C CG2   . VAL   B 1 154 ? 33.799  -46.741 61.14  1   3     ? 135 VAL   D CG2   1 
ATOM   2962 N N     . LYS   B 1 155 ? 38.317  -45.22  60.362 1   5.07  ? 136 LYS   D N     1 
ATOM   2963 C CA    . LYS   B 1 155 ? 39.741  -45.257 60.032 1   6.57  ? 136 LYS   D CA    1 
ATOM   2964 C C     . LYS   B 1 155 ? 40.576  -46.149 60.941 1   6.63  ? 136 LYS   D C     1 
ATOM   2965 O O     . LYS   B 1 155 ? 41.557  -46.74  60.47  1   7.21  ? 136 LYS   D O     1 
ATOM   2966 C CB    . LYS   B 1 155 ? 40.323  -43.829 60     1   8.12  ? 136 LYS   D CB    1 
ATOM   2967 C CG    . LYS   B 1 155 ? 39.578  -42.841 59.073 1   11.69 ? 136 LYS   D CG    1 
ATOM   2968 C CD    . LYS   B 1 155 ? 39.504  -43.269 57.589 1   24.99 ? 136 LYS   D CD    1 
ATOM   2969 C CE    . LYS   B 1 155 ? 39.301  -42.091 56.651 1   39.31 ? 136 LYS   D CE    1 
ATOM   2970 N NZ    . LYS   B 1 155 ? 37.996  -41.393 56.86  1   45.49 ? 136 LYS   D NZ    1 
ATOM   2971 N N     . GLN   B 1 156 ? 40.224  -46.231 62.247 1   3.55  ? 137 GLN   D N     1 
ATOM   2972 C CA    . GLN   B 1 156 ? 40.994  -47.037 63.206 1   3     ? 137 GLN   D CA    1 
ATOM   2973 C C     . GLN   B 1 156 ? 40.087  -47.849 64.127 1   5.13  ? 137 GLN   D C     1 
ATOM   2974 O O     . GLN   B 1 156 ? 38.997  -47.394 64.48  1   3     ? 137 GLN   D O     1 
ATOM   2975 C CB    . GLN   B 1 156 ? 41.932  -46.145 64.038 1   4.5   ? 137 GLN   D CB    1 
ATOM   2976 C CG    . GLN   B 1 156 ? 43.057  -45.484 63.232 1   12.1  ? 137 GLN   D CG    1 
ATOM   2977 C CD    . GLN   B 1 156 ? 43.987  -44.664 64.087 1   18.98 ? 137 GLN   D CD    1 
ATOM   2978 O OE1   . GLN   B 1 156 ? 44.789  -45.195 64.864 1   21.36 ? 137 GLN   D OE1   1 
ATOM   2979 N NE2   . GLN   B 1 156 ? 43.91   -43.346 63.944 1   17.23 ? 137 GLN   D NE2   1 
ATOM   2980 N N     . VAL   B 1 157 ? 40.543  -49.06  64.499 1   3     ? 138 VAL   D N     1 
ATOM   2981 C CA    . VAL   B 1 157 ? 39.838  -49.984 65.397 1   3.21  ? 138 VAL   D CA    1 
ATOM   2982 C C     . VAL   B 1 157 ? 40.835  -50.23  66.526 1   6.17  ? 138 VAL   D C     1 
ATOM   2983 O O     . VAL   B 1 157 ? 41.885  -50.844 66.292 1   3     ? 138 VAL   D O     1 
ATOM   2984 C CB    . VAL   B 1 157 ? 39.41   -51.3   64.684 1   7.17  ? 138 VAL   D CB    1 
ATOM   2985 C CG1   . VAL   B 1 157 ? 38.637  -52.204 65.632 1   7.04  ? 138 VAL   D CG1   1 
ATOM   2986 C CG2   . VAL   B 1 157 ? 38.576  -51.004 63.438 1   7.11  ? 138 VAL   D CG2   1 
ATOM   2987 N N     . LEU   B 1 158 ? 40.547  -49.698 67.724 1   3     ? 139 LEU   D N     1 
ATOM   2988 C CA    . LEU   B 1 158 ? 41.522  -49.734 68.815 1   3     ? 139 LEU   D CA    1 
ATOM   2989 C C     . LEU   B 1 158 ? 41.067  -50.379 70.125 1   6.25  ? 139 LEU   D C     1 
ATOM   2990 O O     . LEU   B 1 158 ? 39.881  -50.358 70.468 1   3     ? 139 LEU   D O     1 
ATOM   2991 C CB    . LEU   B 1 158 ? 42.006  -48.298 69.127 1   3     ? 139 LEU   D CB    1 
ATOM   2992 C CG    . LEU   B 1 158 ? 42.599  -47.442 68.003 1   6.95  ? 139 LEU   D CG    1 
ATOM   2993 C CD1   . LEU   B 1 158 ? 42.855  -46.023 68.499 1   5.96  ? 139 LEU   D CD1   1 
ATOM   2994 C CD2   . LEU   B 1 158 ? 43.912  -48.038 67.466 1   5.54  ? 139 LEU   D CD2   1 
ATOM   2995 N N     . LYS   B 1 159 ? 42.047  -50.887 70.888 1   3     ? 140 LYS   D N     1 
ATOM   2996 C CA    . LYS   B 1 159 ? 41.829  -51.428 72.222 1   3     ? 140 LYS   D CA    1 
ATOM   2997 C C     . LYS   B 1 159 ? 41.676  -50.21  73.166 1   5.36  ? 140 LYS   D C     1 
ATOM   2998 O O     . LYS   B 1 159 ? 42.4    -49.207 73.021 1   3     ? 140 LYS   D O     1 
ATOM   2999 C CB    . LYS   B 1 159 ? 43.038  -52.288 72.654 1   5.65  ? 140 LYS   D CB    1 
ATOM   3000 C CG    . LYS   B 1 159 ? 42.865  -53.01  74.001 1   12.26 ? 140 LYS   D CG    1 
ATOM   3001 C CD    . LYS   B 1 159 ? 42.481  -54.484 73.816 1   23.34 ? 140 LYS   D CD    1 
ATOM   3002 C CE    . LYS   B 1 159 ? 42.93   -55.357 74.966 1   36.07 ? 140 LYS   D CE    1 
ATOM   3003 N NZ    . LYS   B 1 159 ? 42.17   -55.086 76.219 1   33.26 ? 140 LYS   D NZ    1 
ATOM   3004 N N     A CYS   B 1 160 ? 40.756  -50.308 74.124 0.5 3     ? 141 CYS   D N     1 
ATOM   3005 N N     B CYS   B 1 160 ? 40.713  -50.282 74.103 0.5 3     ? 141 CYS   D N     1 
ATOM   3006 C CA    A CYS   B 1 160 ? 40.569  -49.244 75.107 0.5 3     ? 141 CYS   D CA    1 
ATOM   3007 C CA    B CYS   B 1 160 ? 40.441  -49.2   75.065 0.5 3     ? 141 CYS   D CA    1 
ATOM   3008 C C     A CYS   B 1 160 ? 40.212  -49.802 76.47  0.5 5.15  ? 141 CYS   D C     1 
ATOM   3009 C C     B CYS   B 1 160 ? 40.091  -49.749 76.449 0.5 5.22  ? 141 CYS   D C     1 
ATOM   3010 O O     A CYS   B 1 160 ? 39.682  -50.911 76.574 0.5 3     ? 141 CYS   D O     1 
ATOM   3011 O O     B CYS   B 1 160 ? 39.466  -50.806 76.547 0.5 3     ? 141 CYS   D O     1 
ATOM   3012 C CB    A CYS   B 1 160 ? 39.552  -48.211 74.635 0.5 3     ? 141 CYS   D CB    1 
ATOM   3013 C CB    B CYS   B 1 160 ? 39.353  -48.27  74.527 0.5 4.02  ? 141 CYS   D CB    1 
ATOM   3014 S SG    A CYS   B 1 160 ? 37.827  -48.728 74.821 0.5 5.78  ? 141 CYS   D SG    1 
ATOM   3015 S SG    B CYS   B 1 160 ? 38.538  -47.227 75.767 0.5 6.31  ? 141 CYS   D SG    1 
ATOM   3016 N N     . ASP   B 1 161 ? 40.494  -49.023 77.51  1   3     ? 142 ASP   D N     1 
ATOM   3017 C CA    . ASP   B 1 161 ? 40.17   -49.378 78.887 1   3     ? 142 ASP   D CA    1 
ATOM   3018 C C     . ASP   B 1 161 ? 39.794  -48.074 79.566 1   4.48  ? 142 ASP   D C     1 
ATOM   3019 O O     . ASP   B 1 161 ? 40.671  -47.284 79.893 1   3     ? 142 ASP   D O     1 
ATOM   3020 C CB    . ASP   B 1 161 ? 41.316  -50.093 79.623 1   3.2   ? 142 ASP   D CB    1 
ATOM   3021 C CG    . ASP   B 1 161 ? 40.949  -50.539 81.044 1   5.69  ? 142 ASP   D CG    1 
ATOM   3022 O OD1   . ASP   B 1 161 ? 39.832  -50.181 81.526 1   3     ? 142 ASP   D OD1   1 
ATOM   3023 O OD2   . ASP   B 1 161 ? 41.76   -51.255 81.664 1   7.36  ? 142 ASP   D OD2   1 
ATOM   3024 N N     . VAL   B 1 162 ? 38.475  -47.841 79.747 1   3     ? 143 VAL   D N     1 
ATOM   3025 C CA    . VAL   B 1 162 ? 37.964  -46.59  80.338 1   3     ? 143 VAL   D CA    1 
ATOM   3026 C C     . VAL   B 1 162 ? 38.463  -46.352 81.78  1   4.39  ? 143 VAL   D C     1 
ATOM   3027 O O     . VAL   B 1 162 ? 38.404  -45.221 82.268 1   3     ? 143 VAL   D O     1 
ATOM   3028 C CB    . VAL   B 1 162 ? 36.411  -46.493 80.245 1   3.51  ? 143 VAL   D CB    1 
ATOM   3029 C CG1   . VAL   B 1 162 ? 35.937  -46.704 78.807 1   3     ? 143 VAL   D CG1   1 
ATOM   3030 C CG2   . VAL   B 1 162 ? 35.722  -47.488 81.188 1   3     ? 143 VAL   D CG2   1 
ATOM   3031 N N     . THR   B 1 163 ? 38.899  -47.42  82.477 1   3     ? 144 THR   D N     1 
ATOM   3032 C CA    . THR   B 1 163 ? 39.368  -47.267 83.868 1   3     ? 144 THR   D CA    1 
ATOM   3033 C C     . THR   B 1 163 ? 40.816  -46.724 83.923 1   6.67  ? 144 THR   D C     1 
ATOM   3034 O O     . THR   B 1 163 ? 41.313  -46.421 85.016 1   4.3   ? 144 THR   D O     1 
ATOM   3035 C CB    . THR   B 1 163 ? 39.242  -48.592 84.636 1   5.93  ? 144 THR   D CB    1 
ATOM   3036 O OG1   . THR   B 1 163 ? 40.174  -49.522 84.068 1   3     ? 144 THR   D OG1   1 
ATOM   3037 C CG2   . THR   B 1 163 ? 37.805  -49.148 84.641 1   3     ? 144 THR   D CG2   1 
ATOM   3038 N N     . GLN   B 1 164 ? 41.492  -46.622 82.758 1   3     ? 145 GLN   D N     1 
ATOM   3039 C CA    . GLN   B 1 164 ? 42.888  -46.153 82.706 1   3     ? 145 GLN   D CA    1 
ATOM   3040 C C     . GLN   B 1 164 ? 42.98   -44.67  82.393 1   5.49  ? 145 GLN   D C     1 
ATOM   3041 O O     . GLN   B 1 164 ? 42.205  -44.191 81.569 1   3     ? 145 GLN   D O     1 
ATOM   3042 C CB    . GLN   B 1 164 ? 43.71   -46.973 81.695 1   4.36  ? 145 GLN   D CB    1 
ATOM   3043 C CG    . GLN   B 1 164 ? 43.806  -48.487 82.013 1   10.33 ? 145 GLN   D CG    1 
ATOM   3044 C CD    . GLN   B 1 164 ? 44.142  -48.826 83.463 1   26.61 ? 145 GLN   D CD    1 
ATOM   3045 O OE1   . GLN   B 1 164 ? 43.483  -49.653 84.112 1   26.47 ? 145 GLN   D OE1   1 
ATOM   3046 N NE2   . GLN   B 1 164 ? 45.175  -48.197 84.006 1   29.68 ? 145 GLN   D NE2   1 
ATOM   3047 N N     . SER   B 1 165 ? 43.975  -43.946 83     1   3     ? 146 SER   D N     1 
ATOM   3048 C CA    . SER   B 1 165 ? 44.171  -42.501 82.751 1   3.73  ? 146 SER   D CA    1 
ATOM   3049 C C     . SER   B 1 165 ? 44.353  -42.205 81.248 1   6.71  ? 146 SER   D C     1 
ATOM   3050 O O     . SER   B 1 165 ? 43.945  -41.136 80.765 1   6.37  ? 146 SER   D O     1 
ATOM   3051 C CB    . SER   B 1 165 ? 45.364  -41.977 83.547 1   10.48 ? 146 SER   D CB    1 
ATOM   3052 O OG    . SER   B 1 165 ? 45.097  -42.125 84.933 1   12.85 ? 146 SER   D OG    1 
ATOM   3053 N N     . GLN   B 1 166 ? 44.968  -43.168 80.518 1   3.19  ? 147 GLN   D N     1 
ATOM   3054 C CA    . GLN   B 1 166 ? 45.144  -43.114 79.073 1   3     ? 147 GLN   D CA    1 
ATOM   3055 C C     . GLN   B 1 166 ? 44.303  -44.284 78.554 1   5.57  ? 147 GLN   D C     1 
ATOM   3056 O O     . GLN   B 1 166 ? 44.808  -45.409 78.505 1   3     ? 147 GLN   D O     1 
ATOM   3057 C CB    . GLN   B 1 166 ? 46.63   -43.282 78.666 1   5.93  ? 147 GLN   D CB    1 
ATOM   3058 C CG    . GLN   B 1 166 ? 47.502  -42.048 78.915 1   19.92 ? 147 GLN   D CG    1 
ATOM   3059 C CD    . GLN   B 1 166 ? 47.955  -41.931 80.356 1   41.1  ? 147 GLN   D CD    1 
ATOM   3060 O OE1   . GLN   B 1 166 ? 47.62   -40.972 81.067 1   42.09 ? 147 GLN   D OE1   1 
ATOM   3061 N NE2   . GLN   B 1 166 ? 48.724  -42.909 80.821 1   42.24 ? 147 GLN   D NE2   1 
ATOM   3062 N N     . PRO   B 1 167 ? 42.982  -44.078 78.266 1   3     ? 148 PRO   D N     1 
ATOM   3063 C CA    . PRO   B 1 167 ? 42.147  -45.215 77.835 1   3     ? 148 PRO   D CA    1 
ATOM   3064 C C     . PRO   B 1 167 ? 42.696  -45.955 76.617 1   6.13  ? 148 PRO   D C     1 
ATOM   3065 O O     . PRO   B 1 167 ? 42.504  -47.162 76.521 1   3     ? 148 PRO   D O     1 
ATOM   3066 C CB    . PRO   B 1 167 ? 40.775  -44.571 77.54  1   3.45  ? 148 PRO   D CB    1 
ATOM   3067 C CG    . PRO   B 1 167 ? 40.755  -43.331 78.358 1   7     ? 148 PRO   D CG    1 
ATOM   3068 C CD    . PRO   B 1 167 ? 42.189  -42.831 78.332 1   3.38  ? 148 PRO   D CD    1 
ATOM   3069 N N     . LEU   B 1 168 ? 43.398  -45.238 75.709 1   3     ? 149 LEU   D N     1 
ATOM   3070 C CA    . LEU   B 1 168 ? 43.943  -45.848 74.492 1   3.46  ? 149 LEU   D CA    1 
ATOM   3071 C C     . LEU   B 1 168 ? 45.409  -46.333 74.637 1   7.68  ? 149 LEU   D C     1 
ATOM   3072 O O     . LEU   B 1 168 ? 46.06   -46.635 73.629 1   8.84  ? 149 LEU   D O     1 
ATOM   3073 C CB    . LEU   B 1 168 ? 43.771  -44.893 73.296 1   3     ? 149 LEU   D CB    1 
ATOM   3074 C CG    . LEU   B 1 168 ? 42.347  -44.331 73.079 1   6.85  ? 149 LEU   D CG    1 
ATOM   3075 C CD1   . LEU   B 1 168 ? 42.305  -43.404 71.894 1   6.68  ? 149 LEU   D CD1   1 
ATOM   3076 C CD2   . LEU   B 1 168 ? 41.323  -45.429 72.88  1   6.34  ? 149 LEU   D CD2   1 
ATOM   3077 N N     . GLY   B 1 169 ? 45.873  -46.47  75.884 1   10.14 ? 150 GLY   D N     1 
ATOM   3078 C CA    . GLY   B 1 169 ? 47.22   -46.937 76.2   1   10.71 ? 150 GLY   D CA    1 
ATOM   3079 C C     . GLY   B 1 169 ? 48.295  -46.054 75.598 1   14.07 ? 150 GLY   D C     1 
ATOM   3080 O O     . GLY   B 1 169 ? 48.276  -44.842 75.8   1   16.37 ? 150 GLY   D O     1 
ATOM   3081 N N     . ALA   B 1 170 ? 49.207  -46.657 74.809 1   15.4  ? 151 ALA   D N     1 
ATOM   3082 C CA    . ALA   B 1 170 ? 50.313  -45.949 74.155 1   18.44 ? 151 ALA   D CA    1 
ATOM   3083 C C     . ALA   B 1 170 ? 49.944  -45.344 72.784 1   20.91 ? 151 ALA   D C     1 
ATOM   3084 O O     . ALA   B 1 170 ? 50.76   -44.623 72.202 1   21.38 ? 151 ALA   D O     1 
ATOM   3085 C CB    . ALA   B 1 170 ? 51.514  -46.879 74.018 1   19.28 ? 151 ALA   D CB    1 
ATOM   3086 N N     . VAL   B 1 171 ? 48.719  -45.62  72.275 1   16.48 ? 152 VAL   D N     1 
ATOM   3087 C CA    . VAL   B 1 171 ? 48.278  -45.122 70.971 1   16.12 ? 152 VAL   D CA    1 
ATOM   3088 C C     . VAL   B 1 171 ? 47.958  -43.612 71.012 1   20.08 ? 152 VAL   D C     1 
ATOM   3089 O O     . VAL   B 1 171 ? 47.009  -43.2   71.689 1   20.88 ? 152 VAL   D O     1 
ATOM   3090 C CB    . VAL   B 1 171 ? 47.118  -45.961 70.355 1   14.41 ? 152 VAL   D CB    1 
ATOM   3091 C CG1   . VAL   B 1 171 ? 46.698  -45.409 69     1   14.22 ? 152 VAL   D CG1   1 
ATOM   3092 C CG2   . VAL   B 1 171 ? 47.507  -47.43  70.226 1   13.58 ? 152 VAL   D CG2   1 
ATOM   3093 N N     . PRO   B 1 172 ? 48.709  -42.771 70.269 1   20.22 ? 153 PRO   D N     1 
ATOM   3094 C CA    . PRO   B 1 172 ? 48.375  -41.34  70.256 1   21.27 ? 153 PRO   D CA    1 
ATOM   3095 C C     . PRO   B 1 172 ? 47.275  -41.031 69.226 1   20.1  ? 153 PRO   D C     1 
ATOM   3096 O O     . PRO   B 1 172 ? 47.232  -41.631 68.14  1   19.92 ? 153 PRO   D O     1 
ATOM   3097 C CB    . PRO   B 1 172 ? 49.711  -40.67  69.908 1   23.32 ? 153 PRO   D CB    1 
ATOM   3098 C CG    . PRO   B 1 172 ? 50.444  -41.695 69.071 1   24.06 ? 153 PRO   D CG    1 
ATOM   3099 C CD    . PRO   B 1 172 ? 49.87   -43.066 69.395 1   20.7  ? 153 PRO   D CD    1 
ATOM   3100 N N     . LEU   B 1 173 ? 46.371  -40.117 69.583 1   15.43 ? 154 LEU   D N     1 
ATOM   3101 C CA    . LEU   B 1 173 ? 45.299  -39.663 68.704 1   13.99 ? 154 LEU   D CA    1 
ATOM   3102 C C     . LEU   B 1 173 ? 45.115  -38.154 68.849 1   13.82 ? 154 LEU   D C     1 
ATOM   3103 O O     . LEU   B 1 173 ? 45.288  -37.642 69.965 1   14.7  ? 154 LEU   D O     1 
ATOM   3104 C CB    . LEU   B 1 173 ? 43.969  -40.352 69.061 1   11.89 ? 154 LEU   D CB    1 
ATOM   3105 C CG    . LEU   B 1 173 ? 43.597  -41.671 68.387 1   9.89  ? 154 LEU   D CG    1 
ATOM   3106 C CD1   . LEU   B 1 173 ? 42.123  -41.98  68.643 1   9.28  ? 154 LEU   D CD1   1 
ATOM   3107 C CD2   . LEU   B 1 173 ? 43.766  -41.614 66.88  1   9.96  ? 154 LEU   D CD2   1 
ATOM   3108 N N     . PRO   B 1 174 ? 44.684  -37.433 67.779 1   13.26 ? 155 PRO   D N     1 
ATOM   3109 C CA    . PRO   B 1 174 ? 44.389  -35.999 67.938 1   14.17 ? 155 PRO   D CA    1 
ATOM   3110 C C     . PRO   B 1 174 ? 43.193  -35.822 68.884 1   11.76 ? 155 PRO   D C     1 
ATOM   3111 O O     . PRO   B 1 174 ? 42.358  -36.734 68.927 1   9.57  ? 155 PRO   D O     1 
ATOM   3112 C CB    . PRO   B 1 174 ? 44.003  -35.548 66.516 1   14.02 ? 155 PRO   D CB    1 
ATOM   3113 C CG    . PRO   B 1 174 ? 44.452  -36.635 65.61  1   13.15 ? 155 PRO   D CG    1 
ATOM   3114 C CD    . PRO   B 1 174 ? 44.378  -37.889 66.406 1   11.6  ? 155 PRO   D CD    1 
ATOM   3115 N N     . PRO   B 1 175 ? 43.084  -34.714 69.666 1   11.5  ? 156 PRO   D N     1 
ATOM   3116 C CA    . PRO   B 1 175 ? 41.903  -34.55  70.536 1   9.2   ? 156 PRO   D CA    1 
ATOM   3117 C C     . PRO   B 1 175 ? 40.633  -34.575 69.675 1   7.89  ? 156 PRO   D C     1 
ATOM   3118 O O     . PRO   B 1 175 ? 40.587  -33.937 68.614 1   8.14  ? 156 PRO   D O     1 
ATOM   3119 C CB    . PRO   B 1 175 ? 42.124  -33.183 71.194 1   11.72 ? 156 PRO   D CB    1 
ATOM   3120 C CG    . PRO   B 1 175 ? 43.587  -32.924 71.066 1   12.78 ? 156 PRO   D CG    1 
ATOM   3121 C CD    . PRO   B 1 175 ? 43.97   -33.537 69.747 1   12.76 ? 156 PRO   D CD    1 
ATOM   3122 N N     . ALA   B 1 176 ? 39.635  -35.366 70.098 1   3.85  ? 157 ALA   D N     1 
ATOM   3123 C CA    . ALA   B 1 176 ? 38.387  -35.549 69.363 1   3     ? 157 ALA   D CA    1 
ATOM   3124 C C     . ALA   B 1 176 ? 37.418  -34.392 69.517 1   5.12  ? 157 ALA   D C     1 
ATOM   3125 O O     . ALA   B 1 176 ? 37.454  -33.678 70.523 1   3     ? 157 ALA   D O     1 
ATOM   3126 C CB    . ALA   B 1 176 ? 37.717  -36.849 69.794 1   3.44  ? 157 ALA   D CB    1 
ATOM   3127 N N     . ASP   B 1 177 ? 36.529  -34.222 68.516 1   3     ? 158 ASP   D N     1 
ATOM   3128 C CA    . ASP   B 1 177 ? 35.465  -33.223 68.55  1   3     ? 158 ASP   D CA    1 
ATOM   3129 C C     . ASP   B 1 177 ? 34.284  -33.789 69.371 1   5.06  ? 158 ASP   D C     1 
ATOM   3130 O O     . ASP   B 1 177 ? 33.489  -33.029 69.952 1   3     ? 158 ASP   D O     1 
ATOM   3131 C CB    . ASP   B 1 177 ? 34.994  -32.888 67.122 1   3.28  ? 158 ASP   D CB    1 
ATOM   3132 C CG    . ASP   B 1 177 ? 36.091  -32.237 66.294 1   7.22  ? 158 ASP   D CG    1 
ATOM   3133 O OD1   . ASP   B 1 177 ? 36.335  -31.028 66.486 1   9.84  ? 158 ASP   D OD1   1 
ATOM   3134 O OD2   . ASP   B 1 177 ? 36.719  -32.946 65.477 1   8.14  ? 158 ASP   D OD2   1 
ATOM   3135 N N     . CYS   B 1 178 ? 34.164  -35.127 69.396 1   3     ? 159 CYS   D N     1 
ATOM   3136 C CA    . CYS   B 1 178 ? 33.085  -35.803 70.123 1   3     ? 159 CYS   D CA    1 
ATOM   3137 C C     . CYS   B 1 178 ? 33.529  -37.17  70.626 1   5.54  ? 159 CYS   D C     1 
ATOM   3138 O O     . CYS   B 1 178 ? 34.257  -37.879 69.925 1   3     ? 159 CYS   D O     1 
ATOM   3139 C CB    . CYS   B 1 178 ? 31.836  -35.909 69.247 1   3     ? 159 CYS   D CB    1 
ATOM   3140 S SG    . CYS   B 1 178 ? 30.432  -36.755 70.027 1   3.55  ? 159 CYS   D SG    1 
ATOM   3141 N N     . VAL   B 1 179 ? 33.095  -37.532 71.846 1   3     ? 160 VAL   D N     1 
ATOM   3142 C CA    . VAL   B 1 179 ? 33.33   -38.868 72.427 1   3     ? 160 VAL   D CA    1 
ATOM   3143 C C     . VAL   B 1 179 ? 31.926  -39.44  72.649 1   4.99  ? 160 VAL   D C     1 
ATOM   3144 O O     . VAL   B 1 179 ? 31.097  -38.798 73.297 1   3     ? 160 VAL   D O     1 
ATOM   3145 C CB    . VAL   B 1 179 ? 34.211  -38.888 73.716 1   3.97  ? 160 VAL   D CB    1 
ATOM   3146 C CG1   . VAL   B 1 179 ? 34.039  -40.201 74.495 1   3     ? 160 VAL   D CG1   1 
ATOM   3147 C CG2   . VAL   B 1 179 ? 35.688  -38.69  73.362 1   3     ? 160 VAL   D CG2   1 
ATOM   3148 N N     . LEU   B 1 180 ? 31.649  -40.599 72.046 1   3     ? 161 LEU   D N     1 
ATOM   3149 C CA    . LEU   B 1 180 ? 30.35   -41.245 72.139 1   3     ? 161 LEU   D CA    1 
ATOM   3150 C C     . LEU   B 1 180 ? 30.492  -42.551 72.932 1   5.04  ? 161 LEU   D C     1 
ATOM   3151 O O     . LEU   B 1 180 ? 31.46   -43.278 72.713 1   3     ? 161 LEU   D O     1 
ATOM   3152 C CB    . LEU   B 1 180 ? 29.823  -41.535 70.719 1   3     ? 161 LEU   D CB    1 
ATOM   3153 C CG    . LEU   B 1 180 ? 28.592  -42.434 70.577 1   3.78  ? 161 LEU   D CG    1 
ATOM   3154 C CD1   . LEU   B 1 180 ? 27.337  -41.76  71.147 1   3.08  ? 161 LEU   D CD1   1 
ATOM   3155 C CD2   . LEU   B 1 180 ? 28.363  -42.819 69.114 1   3.44  ? 161 LEU   D CD2   1 
ATOM   3156 N N     . SER   B 1 181 ? 29.52   -42.878 73.802 1   3     ? 162 SER   D N     1 
ATOM   3157 C CA    . SER   B 1 181 ? 29.597  -44.156 74.515 1   3     ? 162 SER   D CA    1 
ATOM   3158 C C     . SER   B 1 181 ? 28.185  -44.668 74.803 1   4.66  ? 162 SER   D C     1 
ATOM   3159 O O     . SER   B 1 181 ? 27.446  -44.046 75.565 1   3     ? 162 SER   D O     1 
ATOM   3160 C CB    . SER   B 1 181 ? 30.429  -44.053 75.792 1   3     ? 162 SER   D CB    1 
ATOM   3161 O OG    . SER   B 1 181 ? 30.656  -45.351 76.323 1   3     ? 162 SER   D OG    1 
ATOM   3162 N N     . THR   B 1 182 ? 27.809  -45.779 74.157 1   3     ? 163 THR   D N     1 
ATOM   3163 C CA    . THR   B 1 182 ? 26.463  -46.32  74.341 1   3     ? 163 THR   D CA    1 
ATOM   3164 C C     . THR   B 1 182 ? 26.522  -47.638 75.115 1   4.03  ? 163 THR   D C     1 
ATOM   3165 O O     . THR   B 1 182 ? 27.253  -48.545 74.712 1   3     ? 163 THR   D O     1 
ATOM   3166 C CB    . THR   B 1 182 ? 25.724  -46.464 72.978 1   3     ? 163 THR   D CB    1 
ATOM   3167 O OG1   . THR   B 1 182 ? 26.473  -47.34  72.121 1   3     ? 163 THR   D OG1   1 
ATOM   3168 C CG2   . THR   B 1 182 ? 25.507  -45.106 72.272 1   3     ? 163 THR   D CG2   1 
ATOM   3169 N N     . LEU   B 1 183 ? 25.724  -47.751 76.202 1   3     ? 164 LEU   D N     1 
ATOM   3170 C CA    . LEU   B 1 183 ? 25.576  -48.971 77.011 1   3     ? 164 LEU   D CA    1 
ATOM   3171 C C     . LEU   B 1 183 ? 26.907  -49.614 77.47  1   5.05  ? 164 LEU   D C     1 
ATOM   3172 O O     . LEU   B 1 183 ? 26.975  -50.842 77.633 1   3     ? 164 LEU   D O     1 
ATOM   3173 C CB    . LEU   B 1 183 ? 24.704  -49.998 76.236 1   3     ? 164 LEU   D CB    1 
ATOM   3174 C CG    . LEU   B 1 183 ? 23.248  -49.59  75.996 1   4.81  ? 164 LEU   D CG    1 
ATOM   3175 C CD1   . LEU   B 1 183 ? 22.642  -50.399 74.847 1   5.64  ? 164 LEU   D CD1   1 
ATOM   3176 C CD2   . LEU   B 1 183 ? 22.41   -49.719 77.275 1   3.02  ? 164 LEU   D CD2   1 
ATOM   3177 N N     . CYS   B 1 184 ? 27.932  -48.778 77.747 1   3     ? 165 CYS   D N     1 
ATOM   3178 C CA    . CYS   B 1 184 ? 29.249  -49.269 78.174 1   3     ? 165 CYS   D CA    1 
ATOM   3179 C C     . CYS   B 1 184 ? 29.586  -48.975 79.634 1   4.95  ? 165 CYS   D C     1 
ATOM   3180 O O     . CYS   B 1 184 ? 29.971  -49.886 80.376 1   3     ? 165 CYS   D O     1 
ATOM   3181 C CB    . CYS   B 1 184 ? 30.343  -48.724 77.256 1   3     ? 165 CYS   D CB    1 
ATOM   3182 S SG    . CYS   B 1 184 ? 32.025  -48.983 77.887 1   3     ? 165 CYS   D SG    1 
ATOM   3183 N N     . LEU   B 1 185 ? 29.582  -47.677 80.002 1   3     ? 166 LEU   D N     1 
ATOM   3184 C CA    . LEU   B 1 185 ? 30.055  -47.226 81.311 1   3     ? 166 LEU   D CA    1 
ATOM   3185 C C     . LEU   B 1 185 ? 29.392  -47.929 82.506 1   4.5   ? 166 LEU   D C     1 
ATOM   3186 O O     . LEU   B 1 185 ? 30.116  -48.291 83.427 1   3     ? 166 LEU   D O     1 
ATOM   3187 C CB    . LEU   B 1 185 ? 29.978  -45.701 81.447 1   3     ? 166 LEU   D CB    1 
ATOM   3188 C CG    . LEU   B 1 185 ? 30.8    -44.904 80.43  1   4.8   ? 166 LEU   D CG    1 
ATOM   3189 C CD1   . LEU   B 1 185 ? 30.62   -43.412 80.641 1   4.54  ? 166 LEU   D CD1   1 
ATOM   3190 C CD2   . LEU   B 1 185 ? 32.326  -45.27  80.487 1   3     ? 166 LEU   D CD2   1 
ATOM   3191 N N     . ASP   B 1 186 ? 28.058  -48.169 82.48  1   3     ? 167 ASP   D N     1 
ATOM   3192 C CA    . ASP   B 1 186 ? 27.386  -48.883 83.59  1   3     ? 167 ASP   D CA    1 
ATOM   3193 C C     . ASP   B 1 186 ? 28.017  -50.269 83.794 1   5.08  ? 167 ASP   D C     1 
ATOM   3194 O O     . ASP   B 1 186 ? 28.132  -50.742 84.929 1   3     ? 167 ASP   D O     1 
ATOM   3195 C CB    . ASP   B 1 186 ? 25.904  -49.138 83.261 1   3.67  ? 167 ASP   D CB    1 
ATOM   3196 C CG    . ASP   B 1 186 ? 24.933  -47.995 83.402 1   7.62  ? 167 ASP   D CG    1 
ATOM   3197 O OD1   . ASP   B 1 186 ? 25.357  -46.899 83.853 1   8.24  ? 167 ASP   D OD1   1 
ATOM   3198 O OD2   . ASP   B 1 186 ? 23.746  -48.192 83.067 1   10.1  ? 167 ASP   D OD2   1 
ATOM   3199 N N     . ALA   B 1 187 ? 28.339  -50.936 82.681 1   3     ? 168 ALA   D N     1 
ATOM   3200 C CA    . ALA   B 1 187 ? 28.912  -52.286 82.669 1   3     ? 168 ALA   D CA    1 
ATOM   3201 C C     . ALA   B 1 187 ? 30.413  -52.296 83.011 1   6.99  ? 168 ALA   D C     1 
ATOM   3202 O O     . ALA   B 1 187 ? 30.908  -53.293 83.56  1   6.47  ? 168 ALA   D O     1 
ATOM   3203 C CB    . ALA   B 1 187 ? 28.684  -52.93  81.312 1   3     ? 168 ALA   D CB    1 
ATOM   3204 N N     . ALA   B 1 188 ? 31.134  -51.213 82.684 1   3     ? 169 ALA   D N     1 
ATOM   3205 C CA    . ALA   B 1 188 ? 32.588  -51.157 82.889 1   3     ? 169 ALA   D CA    1 
ATOM   3206 C C     . ALA   B 1 188 ? 33.032  -50.652 84.274 1   5.82  ? 169 ALA   D C     1 
ATOM   3207 O O     . ALA   B 1 188 ? 34.208  -50.819 84.633 1   3     ? 169 ALA   D O     1 
ATOM   3208 C CB    . ALA   B 1 188 ? 33.245  -50.3   81.804 1   3     ? 169 ALA   D CB    1 
ATOM   3209 N N     . CYS   B 1 189 ? 32.133  -49.977 85.012 1   3     ? 170 CYS   D N     1 
ATOM   3210 C CA    . CYS   B 1 189 ? 32.481  -49.347 86.291 1   3     ? 170 CYS   D CA    1 
ATOM   3211 C C     . CYS   B 1 189 ? 31.861  -50.041 87.507 1   4.68  ? 170 CYS   D C     1 
ATOM   3212 O O     . CYS   B 1 189 ? 30.632  -50.079 87.611 1   3     ? 170 CYS   D O     1 
ATOM   3213 C CB    . CYS   B 1 189 ? 32.128  -47.867 86.242 1   3     ? 170 CYS   D CB    1 
ATOM   3214 S SG    . CYS   B 1 189 ? 32.813  -47.016 84.797 1   3.32  ? 170 CYS   D SG    1 
ATOM   3215 N N     . PRO   B 1 190 ? 32.693  -50.581 88.436 1   3     ? 171 PRO   D N     1 
ATOM   3216 C CA    . PRO   B 1 190 ? 32.129  -51.311 89.599 1   3     ? 171 PRO   D CA    1 
ATOM   3217 C C     . PRO   B 1 190 ? 31.485  -50.447 90.676 1   6.28  ? 171 PRO   D C     1 
ATOM   3218 O O     . PRO   B 1 190 ? 30.723  -50.972 91.485 1   5.33  ? 171 PRO   D O     1 
ATOM   3219 C CB    . PRO   B 1 190 ? 33.321  -52.107 90.164 1   5.34  ? 171 PRO   D CB    1 
ATOM   3220 C CG    . PRO   B 1 190 ? 34.457  -51.899 89.198 1   5.12  ? 171 PRO   D CG    1 
ATOM   3221 C CD    . PRO   B 1 190 ? 34.17   -50.642 88.427 1   5.32  ? 171 PRO   D CD    1 
ATOM   3222 N N     . ASP   B 1 191 ? 31.803  -49.137 90.711 1   3     ? 172 ASP   D N     1 
ATOM   3223 C CA    . ASP   B 1 191 ? 31.254  -48.212 91.711 1   3.81  ? 172 ASP   D CA    1 
ATOM   3224 C C     . ASP   B 1 191 ? 31.197  -46.789 91.189 1   5.96  ? 172 ASP   D C     1 
ATOM   3225 O O     . ASP   B 1 191 ? 31.825  -46.482 90.168 1   3     ? 172 ASP   D O     1 
ATOM   3226 C CB    . ASP   B 1 191 ? 32.049  -48.286 93.039 1   6.18  ? 172 ASP   D CB    1 
ATOM   3227 C CG    . ASP   B 1 191 ? 33.552  -48.16  92.882 1   11.44 ? 172 ASP   D CG    1 
ATOM   3228 O OD1   . ASP   B 1 191 ? 34.007  -47.187 92.225 1   11.34 ? 172 ASP   D OD1   1 
ATOM   3229 O OD2   . ASP   B 1 191 ? 34.276  -49.033 93.409 1   13.97 ? 172 ASP   D OD2   1 
ATOM   3230 N N     . LEU   B 1 192 ? 30.468  -45.91  91.907 1   3     ? 173 LEU   D N     1 
ATOM   3231 C CA    . LEU   B 1 192 ? 30.298  -44.504 91.539 1   3.54  ? 173 LEU   D CA    1 
ATOM   3232 C C     . LEU   B 1 192 ? 31.646  -43.729 91.42  1   5.22  ? 173 LEU   D C     1 
ATOM   3233 O O     . LEU   B 1 192 ? 31.804  -43.019 90.419 1   3     ? 173 LEU   D O     1 
ATOM   3234 C CB    . LEU   B 1 192 ? 29.293  -43.807 92.478 1   4.5   ? 173 LEU   D CB    1 
ATOM   3235 C CG    . LEU   B 1 192 ? 28.742  -42.447 92.043 1   6.19  ? 173 LEU   D CG    1 
ATOM   3236 C CD1   . LEU   B 1 192 ? 28.274  -42.465 90.567 1   5.99  ? 173 LEU   D CD1   1 
ATOM   3237 C CD2   . LEU   B 1 192 ? 27.583  -42.013 92.98  1   5.36  ? 173 LEU   D CD2   1 
ATOM   3238 N N     . PRO   B 1 193 ? 32.649  -43.879 92.331 1   3.14  ? 174 PRO   D N     1 
ATOM   3239 C CA    . PRO   B 1 193 ? 33.945  -43.183 92.112 1   3     ? 174 PRO   D CA    1 
ATOM   3240 C C     . PRO   B 1 193 ? 34.649  -43.592 90.805 1   5.02  ? 174 PRO   D C     1 
ATOM   3241 O O     . PRO   B 1 193 ? 35.185  -42.718 90.105 1   3     ? 174 PRO   D O     1 
ATOM   3242 C CB    . PRO   B 1 193 ? 34.774  -43.574 93.345 1   5.13  ? 174 PRO   D CB    1 
ATOM   3243 C CG    . PRO   B 1 193 ? 33.756  -43.95  94.387 1   5.03  ? 174 PRO   D CG    1 
ATOM   3244 C CD    . PRO   B 1 193 ? 32.673  -44.639 93.6   1   5.76  ? 174 PRO   D CD    1 
ATOM   3245 N N     . THR   B 1 194 ? 34.639  -44.907 90.458 1   3     ? 175 THR   D N     1 
ATOM   3246 C CA    . THR   B 1 194 ? 35.25   -45.393 89.21  1   3     ? 175 THR   D CA    1 
ATOM   3247 C C     . THR   B 1 194 ? 34.501  -44.803 88.002 1   3.95  ? 175 THR   D C     1 
ATOM   3248 O O     . THR   B 1 194 ? 35.135  -44.431 87.016 1   3     ? 175 THR   D O     1 
ATOM   3249 C CB    . THR   B 1 194 ? 35.298  -46.935 89.159 1   6.8   ? 175 THR   D CB    1 
ATOM   3250 O OG1   . THR   B 1 194 ? 35.976  -47.422 90.322 1   5.83  ? 175 THR   D OG1   1 
ATOM   3251 C CG2   . THR   B 1 194 ? 36.022  -47.466 87.894 1   4.19  ? 175 THR   D CG2   1 
ATOM   3252 N N     . TYR   B 1 195 ? 33.161  -44.717 88.092 1   3     ? 176 TYR   D N     1 
ATOM   3253 C CA    . TYR   B 1 195 ? 32.318  -44.152 87.025 1   3     ? 176 TYR   D CA    1 
ATOM   3254 C C     . TYR   B 1 195 ? 32.737  -42.709 86.737 1   5.07  ? 176 TYR   D C     1 
ATOM   3255 O O     . TYR   B 1 195 ? 32.985  -42.343 85.578 1   3     ? 176 TYR   D O     1 
ATOM   3256 C CB    . TYR   B 1 195 ? 30.828  -44.22  87.436 1   3     ? 176 TYR   D CB    1 
ATOM   3257 C CG    . TYR   B 1 195 ? 29.873  -43.796 86.342 1   3     ? 176 TYR   D CG    1 
ATOM   3258 C CD1   . TYR   B 1 195 ? 29.445  -44.698 85.379 1   3.13  ? 176 TYR   D CD1   1 
ATOM   3259 C CD2   . TYR   B 1 195 ? 29.355  -42.507 86.303 1   3     ? 176 TYR   D CD2   1 
ATOM   3260 C CE1   . TYR   B 1 195 ? 28.553  -44.316 84.375 1   4.2   ? 176 TYR   D CE1   1 
ATOM   3261 C CE2   . TYR   B 1 195 ? 28.456  -42.115 85.314 1   3     ? 176 TYR   D CE2   1 
ATOM   3262 C CZ    . TYR   B 1 195 ? 28.059  -43.023 84.348 1   6.5   ? 176 TYR   D CZ    1 
ATOM   3263 O OH    . TYR   B 1 195 ? 27.17   -42.641 83.378 1   3     ? 176 TYR   D OH    1 
ATOM   3264 N N     . CYS   B 1 196 ? 32.856  -41.9   87.809 1   3     ? 177 CYS   D N     1 
ATOM   3265 C CA    . CYS   B 1 196 ? 33.297  -40.517 87.686 1   3.67  ? 177 CYS   D CA    1 
ATOM   3266 C C     . CYS   B 1 196 ? 34.726  -40.45  87.103 1   4.78  ? 177 CYS   D C     1 
ATOM   3267 O O     . CYS   B 1 196 ? 34.976  -39.66  86.19  1   3     ? 177 CYS   D O     1 
ATOM   3268 C CB    . CYS   B 1 196 ? 33.205  -39.803 89.029 1   6.23  ? 177 CYS   D CB    1 
ATOM   3269 S SG    . CYS   B 1 196 ? 33.639  -38.056 88.94  1   7.06  ? 177 CYS   D SG    1 
ATOM   3270 N N     . ARG   B 1 197 ? 35.634  -41.316 87.583 1   3     ? 178 ARG   D N     1 
ATOM   3271 C CA    . ARG   B 1 197 ? 37.014  -41.374 87.061 1   3.4   ? 178 ARG   D CA    1 
ATOM   3272 C C     . ARG   B 1 197 ? 37.016  -41.744 85.562 1   4.89  ? 178 ARG   D C     1 
ATOM   3273 O O     . ARG   B 1 197 ? 37.776  -41.158 84.784 1   3     ? 178 ARG   D O     1 
ATOM   3274 C CB    . ARG   B 1 197 ? 37.862  -42.396 87.828 1   7.87  ? 178 ARG   D CB    1 
ATOM   3275 C CG    . ARG   B 1 197 ? 38.365  -41.918 89.19  1   13.39 ? 178 ARG   D CG    1 
ATOM   3276 C CD    . ARG   B 1 197 ? 39.546  -42.749 89.694 1   29.68 ? 178 ARG   D CD    1 
ATOM   3277 N NE    . ARG   B 1 197 ? 39.327  -44.197 89.579 1   34.34 ? 178 ARG   D NE    1 
ATOM   3278 C CZ    . ARG   B 1 197 ? 38.68   -44.941 90.476 1   47.23 ? 178 ARG   D CZ    1 
ATOM   3279 N NH1   . ARG   B 1 197 ? 38.536  -46.245 90.283 1   39.38 ? 178 ARG   D NH1   1 
ATOM   3280 N NH2   . ARG   B 1 197 ? 38.19   -44.388 91.582 1   37.28 ? 178 ARG   D NH2   1 
ATOM   3281 N N     . ALA   B 1 198 ? 36.153  -42.69  85.164 1   3     ? 179 ALA   D N     1 
ATOM   3282 C CA    . ALA   B 1 198 ? 36.049  -43.128 83.762 1   3     ? 179 ALA   D CA    1 
ATOM   3283 C C     . ALA   B 1 198 ? 35.636  -41.951 82.871 1   4.26  ? 179 ALA   D C     1 
ATOM   3284 O O     . ALA   B 1 198 ? 36.209  -41.77  81.796 1   3     ? 179 ALA   D O     1 
ATOM   3285 C CB    . ALA   B 1 198 ? 35.052  -44.267 83.637 1   3     ? 179 ALA   D CB    1 
ATOM   3286 N N     . LEU   B 1 199 ? 34.691  -41.112 83.351 1   3     ? 180 LEU   D N     1 
ATOM   3287 C CA    . LEU   B 1 199 ? 34.251  -39.909 82.617 1   3     ? 180 LEU   D CA    1 
ATOM   3288 C C     . LEU   B 1 199 ? 35.414  -38.927 82.445 1   4.86  ? 180 LEU   D C     1 
ATOM   3289 O O     . LEU   B 1 199 ? 35.545  -38.296 81.383 1   3     ? 180 LEU   D O     1 
ATOM   3290 C CB    . LEU   B 1 199 ? 33.081  -39.228 83.334 1   3     ? 180 LEU   D CB    1 
ATOM   3291 C CG    . LEU   B 1 199 ? 31.72   -39.945 83.258 1   4.91  ? 180 LEU   D CG    1 
ATOM   3292 C CD1   . LEU   B 1 199 ? 30.739  -39.34  84.275 1   4.06  ? 180 LEU   D CD1   1 
ATOM   3293 C CD2   . LEU   B 1 199 ? 31.118  -39.831 81.847 1   3     ? 180 LEU   D CD2   1 
ATOM   3294 N N     . ARG   B 1 200 ? 36.256  -38.794 83.493 1   3     ? 181 ARG   D N     1 
ATOM   3295 C CA    . ARG   B 1 200 ? 37.442  -37.923 83.43  1   3     ? 181 ARG   D CA    1 
ATOM   3296 C C     . ARG   B 1 200 ? 38.416  -38.503 82.401 1   4.98  ? 181 ARG   D C     1 
ATOM   3297 O O     . ARG   B 1 200 ? 38.943  -37.762 81.577 1   3     ? 181 ARG   D O     1 
ATOM   3298 C CB    . ARG   B 1 200 ? 38.146  -37.853 84.786 1   3     ? 181 ARG   D CB    1 
ATOM   3299 C CG    . ARG   B 1 200 ? 37.498  -36.902 85.755 1   8.25  ? 181 ARG   D CG    1 
ATOM   3300 C CD    . ARG   B 1 200 ? 38.42   -36.7   86.939 1   11.01 ? 181 ARG   D CD    1 
ATOM   3301 N NE    . ARG   B 1 200 ? 37.663  -36.474 88.171 1   11.03 ? 181 ARG   D NE    1 
ATOM   3302 C CZ    . ARG   B 1 200 ? 37.311  -35.274 88.614 1   22.26 ? 181 ARG   D CZ    1 
ATOM   3303 N NH1   . ARG   B 1 200 ? 37.644  -34.183 87.932 1   26.46 ? 181 ARG   D NH1   1 
ATOM   3304 N NH2   . ARG   B 1 200 ? 36.615  -35.152 89.738 1   13.95 ? 181 ARG   D NH2   1 
ATOM   3305 N N     . ASN   B 1 201 ? 38.638  -39.831 82.447 1   3     ? 182 ASN   D N     1 
ATOM   3306 C CA    . ASN   B 1 201 ? 39.544  -40.542 81.53  1   3     ? 182 ASN   D CA    1 
ATOM   3307 C C     . ASN   B 1 201 ? 39.099  -40.349 80.071 1   6.53  ? 182 ASN   D C     1 
ATOM   3308 O O     . ASN   B 1 201 ? 39.952  -40.126 79.199 1   5.12  ? 182 ASN   D O     1 
ATOM   3309 C CB    . ASN   B 1 201 ? 39.648  -42.028 81.897 1   3     ? 182 ASN   D CB    1 
ATOM   3310 C CG    . ASN   B 1 201 ? 40.235  -42.294 83.272 1   6.48  ? 182 ASN   D CG    1 
ATOM   3311 O OD1   . ASN   B 1 201 ? 40.865  -41.432 83.892 1   3     ? 182 ASN   D OD1   1 
ATOM   3312 N ND2   . ASN   B 1 201 ? 40.002  -43.48  83.797 1   3     ? 182 ASN   D ND2   1 
ATOM   3313 N N     . LEU   B 1 202 ? 37.77   -40.382 79.817 1   3     ? 183 LEU   D N     1 
ATOM   3314 C CA    . LEU   B 1 202 ? 37.219  -40.135 78.478 1   3     ? 183 LEU   D CA    1 
ATOM   3315 C C     . LEU   B 1 202 ? 37.466  -38.683 78.059 1   4.23  ? 183 LEU   D C     1 
ATOM   3316 O O     . LEU   B 1 202 ? 37.737  -38.439 76.896 1   3     ? 183 LEU   D O     1 
ATOM   3317 C CB    . LEU   B 1 202 ? 35.709  -40.437 78.381 1   3     ? 183 LEU   D CB    1 
ATOM   3318 C CG    . LEU   B 1 202 ? 35.223  -41.877 78.652 1   6.35  ? 183 LEU   D CG    1 
ATOM   3319 C CD1   . LEU   B 1 202 ? 33.786  -42.068 78.163 1   5.15  ? 183 LEU   D CD1   1 
ATOM   3320 C CD2   . LEU   B 1 202 ? 36.188  -42.924 78.09  1   6.95  ? 183 LEU   D CD2   1 
ATOM   3321 N N     . GLY   B 1 203 ? 37.373  -37.754 79.019 1   3     ? 184 GLY   D N     1 
ATOM   3322 C CA    . GLY   B 1 203 ? 37.615  -36.331 78.799 1   3     ? 184 GLY   D CA    1 
ATOM   3323 C C     . GLY   B 1 203 ? 39.001  -36.03  78.268 1   4.06  ? 184 GLY   D C     1 
ATOM   3324 O O     . GLY   B 1 203 ? 39.163  -35.13  77.436 1   3     ? 184 GLY   D O     1 
ATOM   3325 N N     . SER   B 1 204 ? 40.005  -36.82  78.701 1   3     ? 185 SER   D N     1 
ATOM   3326 C CA    . SER   B 1 204 ? 41.396  -36.668 78.227 1   3     ? 185 SER   D CA    1 
ATOM   3327 C C     . SER   B 1 204 ? 41.511  -36.838 76.691 1   5.81  ? 185 SER   D C     1 
ATOM   3328 O O     . SER   B 1 204 ? 42.467  -36.34  76.094 1   4.36  ? 185 SER   D O     1 
ATOM   3329 C CB    . SER   B 1 204 ? 42.332  -37.631 78.956 1   3.11  ? 185 SER   D CB    1 
ATOM   3330 O OG    . SER   B 1 204 ? 42.286  -38.956 78.441 1   3.84  ? 185 SER   D OG    1 
ATOM   3331 N N     . LEU   B 1 205 ? 40.535  -37.538 76.06  1   3     ? 186 LEU   D N     1 
ATOM   3332 C CA    . LEU   B 1 205 ? 40.523  -37.78  74.606 1   3     ? 186 LEU   D CA    1 
ATOM   3333 C C     . LEU   B 1 205 ? 39.791  -36.69  73.84  1   5.53  ? 186 LEU   D C     1 
ATOM   3334 O O     . LEU   B 1 205 ? 39.734  -36.732 72.597 1   3     ? 186 LEU   D O     1 
ATOM   3335 C CB    . LEU   B 1 205 ? 39.819  -39.117 74.294 1   3     ? 186 LEU   D CB    1 
ATOM   3336 C CG    . LEU   B 1 205 ? 40.337  -40.39  74.973 1   6.61  ? 186 LEU   D CG    1 
ATOM   3337 C CD1   . LEU   B 1 205 ? 39.426  -41.566 74.645 1   4.28  ? 186 LEU   D CD1   1 
ATOM   3338 C CD2   . LEU   B 1 205 ? 41.786  -40.707 74.534 1   6.07  ? 186 LEU   D CD2   1 
ATOM   3339 N N     . LEU   B 1 206 ? 39.172  -35.755 74.579 1   3     ? 187 LEU   D N     1 
ATOM   3340 C CA    . LEU   B 1 206 ? 38.339  -34.709 74.023 1   3     ? 187 LEU   D CA    1 
ATOM   3341 C C     . LEU   B 1 206 ? 39.025  -33.357 74.032 1   6.21  ? 187 LEU   D C     1 
ATOM   3342 O O     . LEU   B 1 206 ? 39.679  -32.996 75.026 1   3.36  ? 187 LEU   D O     1 
ATOM   3343 C CB    . LEU   B 1 206 ? 37.062  -34.574 74.875 1   3     ? 187 LEU   D CB    1 
ATOM   3344 C CG    . LEU   B 1 206 ? 35.762  -35.171 74.422 1   6.87  ? 187 LEU   D CG    1 
ATOM   3345 C CD1   . LEU   B 1 206 ? 34.668  -34.789 75.415 1   5.79  ? 187 LEU   D CD1   1 
ATOM   3346 C CD2   . LEU   B 1 206 ? 35.355  -34.708 72.997 1   6.66  ? 187 LEU   D CD2   1 
ATOM   3347 N N     . LYS   B 1 207 ? 38.775  -32.57  72.965 1   3     ? 188 LYS   D N     1 
ATOM   3348 C CA    . LYS   B 1 207 ? 39.284  -31.207 72.857 1   4.73  ? 188 LYS   D CA    1 
ATOM   3349 C C     . LYS   B 1 207 ? 38.471  -30.325 73.844 1   7.28  ? 188 LYS   D C     1 
ATOM   3350 O O     . LYS   B 1 207 ? 37.31   -30.68  74.152 1   3.32  ? 188 LYS   D O     1 
ATOM   3351 C CB    . LYS   B 1 207 ? 39.129  -30.679 71.406 1   7.58  ? 188 LYS   D CB    1 
ATOM   3352 C CG    . LYS   B 1 207 ? 37.671  -30.492 70.958 1   18.32 ? 188 LYS   D CG    1 
ATOM   3353 C CD    . LYS   B 1 207 ? 37.504  -29.797 69.616 1   25.27 ? 188 LYS   D CD    1 
ATOM   3354 C CE    . LYS   B 1 207 ? 36.051  -29.395 69.455 1   37.05 ? 188 LYS   D CE    1 
ATOM   3355 N NZ    . LYS   B 1 207 ? 35.778  -28.759 68.143 1   51.85 ? 188 LYS   D NZ    1 
ATOM   3356 N N     . PRO   B 1 208 ? 39.013  -29.168 74.316 1   7.13  ? 189 PRO   D N     1 
ATOM   3357 C CA    . PRO   B 1 208 ? 38.2    -28.273 75.161 1   7.45  ? 189 PRO   D CA    1 
ATOM   3358 C C     . PRO   B 1 208 ? 36.947  -27.846 74.388 1   9.98  ? 189 PRO   D C     1 
ATOM   3359 O O     . PRO   B 1 208 ? 37.029  -27.567 73.183 1   8.58  ? 189 PRO   D O     1 
ATOM   3360 C CB    . PRO   B 1 208 ? 39.13   -27.071 75.409 1   11.79 ? 189 PRO   D CB    1 
ATOM   3361 C CG    . PRO   B 1 208 ? 40.495  -27.609 75.22  1   13.95 ? 189 PRO   D CG    1 
ATOM   3362 C CD    . PRO   B 1 208 ? 40.35   -28.587 74.07  1   10.45 ? 189 PRO   D CD    1 
ATOM   3363 N N     . GLY   B 1 209 ? 35.792  -27.892 75.049 1   5.26  ? 190 GLY   D N     1 
ATOM   3364 C CA    . GLY   B 1 209 ? 34.525  -27.572 74.413 1   4.41  ? 190 GLY   D CA    1 
ATOM   3365 C C     . GLY   B 1 209 ? 33.973  -28.708 73.563 1   5.29  ? 190 GLY   D C     1 
ATOM   3366 O O     . GLY   B 1 209 ? 32.924  -28.547 72.927 1   3     ? 190 GLY   D O     1 
ATOM   3367 N N     . GLY   B 1 210 ? 34.687  -29.843 73.53  1   3     ? 191 GLY   D N     1 
ATOM   3368 C CA    . GLY   B 1 210 ? 34.283  -31.043 72.798 1   3     ? 191 GLY   D CA    1 
ATOM   3369 C C     . GLY   B 1 210 ? 33.042  -31.65  73.431 1   5.86  ? 191 GLY   D C     1 
ATOM   3370 O O     . GLY   B 1 210 ? 32.778  -31.423 74.615 1   3     ? 191 GLY   D O     1 
ATOM   3371 N N     . PHE   B 1 211 ? 32.271  -32.399 72.649 1   3     ? 192 PHE   D N     1 
ATOM   3372 C CA    . PHE   B 1 211 ? 31.015  -33.002 73.104 1   3.43  ? 192 PHE   D CA    1 
ATOM   3373 C C     . PHE   B 1 211 ? 31.194  -34.422 73.633 1   5.85  ? 192 PHE   D C     1 
ATOM   3374 O O     . PHE   B 1 211 ? 31.931  -35.223 73.044 1   3     ? 192 PHE   D O     1 
ATOM   3375 C CB    . PHE   B 1 211 ? 29.981  -33.024 71.966 1   7.85  ? 192 PHE   D CB    1 
ATOM   3376 C CG    . PHE   B 1 211 ? 29.461  -31.673 71.55  1   9.67  ? 192 PHE   D CG    1 
ATOM   3377 C CD1   . PHE   B 1 211 ? 28.347  -31.117 72.171 1   7.62  ? 192 PHE   D CD1   1 
ATOM   3378 C CD2   . PHE   B 1 211 ? 30.065  -30.967 70.512 1   8.29  ? 192 PHE   D CD2   1 
ATOM   3379 C CE1   . PHE   B 1 211 ? 27.848  -29.868 71.766 1   6.88  ? 192 PHE   D CE1   1 
ATOM   3380 C CE2   . PHE   B 1 211 ? 29.571  -29.718 70.11  1   6.91  ? 192 PHE   D CE2   1 
ATOM   3381 C CZ    . PHE   B 1 211 ? 28.465  -29.175 70.738 1   7.85  ? 192 PHE   D CZ    1 
ATOM   3382 N N     . LEU   B 1 212 ? 30.458  -34.746 74.698 1   3     ? 193 LEU   D N     1 
ATOM   3383 C CA    . LEU   B 1 212 ? 30.41   -36.077 75.296 1   3     ? 193 LEU   D CA    1 
ATOM   3384 C C     . LEU   B 1 212 ? 28.963  -36.547 75.127 1   5.29  ? 193 LEU   D C     1 
ATOM   3385 O O     . LEU   B 1 212 ? 28.05   -35.839 75.574 1   3     ? 193 LEU   D O     1 
ATOM   3386 C CB    . LEU   B 1 212 ? 30.774  -36.028 76.788 1   3     ? 193 LEU   D CB    1 
ATOM   3387 C CG    . LEU   B 1 212 ? 30.742  -37.382 77.532 1   6.91  ? 193 LEU   D CG    1 
ATOM   3388 C CD1   . LEU   B 1 212 ? 31.969  -38.24  77.18  1   6.41  ? 193 LEU   D CD1   1 
ATOM   3389 C CD2   . LEU   B 1 212 ? 30.646  -37.179 79.045 1   6.67  ? 193 LEU   D CD2   1 
ATOM   3390 N N     . VAL   B 1 213 ? 28.755  -37.692 74.451 1   3     ? 194 VAL   D N     1 
ATOM   3391 C CA    . VAL   B 1 213 ? 27.415  -38.235 74.213 1   3     ? 194 VAL   D CA    1 
ATOM   3392 C C     . VAL   B 1 213 ? 27.345  -39.598 74.881 1   5.16  ? 194 VAL   D C     1 
ATOM   3393 O O     . VAL   B 1 213 ? 28.105  -40.493 74.51  1   3     ? 194 VAL   D O     1 
ATOM   3394 C CB    . VAL   B 1 213 ? 27.022  -38.3   72.71  1   4.08  ? 194 VAL   D CB    1 
ATOM   3395 C CG1   . VAL   B 1 213 ? 25.611  -38.865 72.538 1   3     ? 194 VAL   D CG1   1 
ATOM   3396 C CG2   . VAL   B 1 213 ? 27.116  -36.92  72.054 1   3.33  ? 194 VAL   D CG2   1 
ATOM   3397 N N     . ILE   B 1 214 ? 26.456  -39.745 75.879 1   3     ? 195 ILE   D N     1 
ATOM   3398 C CA    . ILE   B 1 214 ? 26.318  -41.014 76.607 1   3     ? 195 ILE   D CA    1 
ATOM   3399 C C     . ILE   B 1 214 ? 24.859  -41.447 76.584 1   4.01  ? 195 ILE   D C     1 
ATOM   3400 O O     . ILE   B 1 214 ? 23.976  -40.619 76.779 1   3     ? 195 ILE   D O     1 
ATOM   3401 C CB    . ILE   B 1 214 ? 26.825  -40.93  78.081 1   4.36  ? 195 ILE   D CB    1 
ATOM   3402 C CG1   . ILE   B 1 214 ? 28.244  -40.3   78.215 1   5.6   ? 195 ILE   D CG1   1 
ATOM   3403 C CG2   . ILE   B 1 214 ? 26.744  -42.297 78.802 1   3.7   ? 195 ILE   D CG2   1 
ATOM   3404 C CD1   . ILE   B 1 214 ? 29.445  -41.064 77.57  1   7.3   ? 195 ILE   D CD1   1 
ATOM   3405 N N     . MET   B 1 215 ? 24.623  -42.734 76.34  1   3     ? 196 MET   D N     1 
ATOM   3406 C CA    . MET   B 1 215 ? 23.289  -43.348 76.402 1   3     ? 196 MET   D CA    1 
ATOM   3407 C C     . MET   B 1 215 ? 23.501  -44.641 77.153 1   5.06  ? 196 MET   D C     1 
ATOM   3408 O O     . MET   B 1 215 ? 24.416  -45.385 76.804 1   3     ? 196 MET   D O     1 
ATOM   3409 C CB    . MET   B 1 215 ? 22.714  -43.629 75.016 1   3.33  ? 196 MET   D CB    1 
ATOM   3410 C CG    . MET   B 1 215 ? 22.44   -42.366 74.245 1   5.89  ? 196 MET   D CG    1 
ATOM   3411 S SD    . MET   B 1 215 ? 21.86   -42.703 72.571 1   7.05  ? 196 MET   D SD    1 
ATOM   3412 C CE    . MET   B 1 215 ? 21.853  -41.047 71.978 1   6.06  ? 196 MET   D CE    1 
ATOM   3413 N N     . ASP   B 1 216 ? 22.738  -44.875 78.224 1   3     ? 197 ASP   D N     1 
ATOM   3414 C CA    . ASP   B 1 216 ? 22.948  -46.079 79.039 1   3     ? 197 ASP   D CA    1 
ATOM   3415 C C     . ASP   B 1 216 ? 21.716  -46.399 79.872 1   4.49  ? 197 ASP   D C     1 
ATOM   3416 O O     . ASP   B 1 216 ? 20.753  -45.636 79.874 1   3     ? 197 ASP   D O     1 
ATOM   3417 C CB    . ASP   B 1 216 ? 24.196  -45.917 79.946 1   3     ? 197 ASP   D CB    1 
ATOM   3418 C CG    . ASP   B 1 216 ? 25.01   -47.181 80.193 1   4.64  ? 197 ASP   D CG    1 
ATOM   3419 O OD1   . ASP   B 1 216 ? 24.42   -48.286 80.153 1   3     ? 197 ASP   D OD1   1 
ATOM   3420 O OD2   . ASP   B 1 216 ? 26.243  -47.06  80.437 1   3.92  ? 197 ASP   D OD2   1 
ATOM   3421 N N     . ALA   B 1 217 ? 21.738  -47.555 80.541 1   3     ? 198 ALA   D N     1 
ATOM   3422 C CA    . ALA   B 1 217 ? 20.61   -48.003 81.34  1   3     ? 198 ALA   D CA    1 
ATOM   3423 C C     . ALA   B 1 217 ? 20.531  -47.285 82.689 1   5     ? 198 ALA   D C     1 
ATOM   3424 O O     . ALA   B 1 217 ? 21.559  -46.943 83.279 1   3     ? 198 ALA   D O     1 
ATOM   3425 C CB    . ALA   B 1 217 ? 20.705  -49.508 81.554 1   3     ? 198 ALA   D CB    1 
ATOM   3426 N N     . LEU   B 1 218 ? 19.305  -47.082 83.193 1   3     ? 199 LEU   D N     1 
ATOM   3427 C CA    . LEU   B 1 218 ? 19.132  -46.498 84.522 1   3     ? 199 LEU   D CA    1 
ATOM   3428 C C     . LEU   B 1 218 ? 18.798  -47.619 85.508 1   5.03  ? 199 LEU   D C     1 
ATOM   3429 O O     . LEU   B 1 218 ? 18.029  -48.522 85.163 1   3     ? 199 LEU   D O     1 
ATOM   3430 C CB    . LEU   B 1 218 ? 18.009  -45.445 84.552 1   3     ? 199 LEU   D CB    1 
ATOM   3431 C CG    . LEU   B 1 218 ? 18.329  -44.072 83.908 1   3.83  ? 199 LEU   D CG    1 
ATOM   3432 C CD1   . LEU   B 1 218 ? 17.091  -43.229 83.835 1   3     ? 199 LEU   D CD1   1 
ATOM   3433 C CD2   . LEU   B 1 218 ? 19.379  -43.319 84.7   1   3.95  ? 199 LEU   D CD2   1 
ATOM   3434 N N     . LYS   B 1 219 ? 19.394  -47.565 86.717 1   3     ? 200 LYS   D N     1 
ATOM   3435 C CA    . LYS   B 1 219 ? 19.131  -48.492 87.82  1   3     ? 200 LYS   D CA    1 
ATOM   3436 C C     . LYS   B 1 219 ? 19.146  -49.976 87.411 1   6.22  ? 200 LYS   D C     1 
ATOM   3437 O O     . LYS   B 1 219 ? 18.227  -50.737 87.755 1   3     ? 200 LYS   D O     1 
ATOM   3438 C CB    . LYS   B 1 219 ? 17.795  -48.125 88.503 1   4.15  ? 200 LYS   D CB    1 
ATOM   3439 C CG    . LYS   B 1 219 ? 17.784  -46.732 89.122 1   17.79 ? 200 LYS   D CG    1 
ATOM   3440 C CD    . LYS   B 1 219 ? 16.432  -46.408 89.737 1   14.9  ? 200 LYS   D CD    1 
ATOM   3441 C CE    . LYS   B 1 219 ? 16.487  -45.133 90.556 1   23.3  ? 200 LYS   D CE    1 
ATOM   3442 N NZ    . LYS   B 1 219 ? 15.124  -44.58  90.786 1   34.8  ? 200 LYS   D NZ    1 
ATOM   3443 N N     . SER   B 1 220 ? 20.167  -50.373 86.645 1   3     ? 201 SER   D N     1 
ATOM   3444 C CA    . SER   B 1 220 ? 20.314  -51.759 86.202 1   3     ? 201 SER   D CA    1 
ATOM   3445 C C     . SER   B 1 220 ? 21.497  -52.373 86.944 1   5.65  ? 201 SER   D C     1 
ATOM   3446 O O     . SER   B 1 220 ? 22.579  -51.767 86.933 1   3     ? 201 SER   D O     1 
ATOM   3447 C CB    . SER   B 1 220 ? 20.563  -51.805 84.695 1   3     ? 201 SER   D CB    1 
ATOM   3448 O OG    . SER   B 1 220 ? 20.429  -53.132 84.214 1   3     ? 201 SER   D OG    1 
ATOM   3449 N N     . SER   B 1 221 ? 21.293  -53.529 87.635 1   3     ? 202 SER   D N     1 
ATOM   3450 C CA    . SER   B 1 221 ? 22.41   -54.164 88.349 1   3     ? 202 SER   D CA    1 
ATOM   3451 C C     . SER   B 1 221 ? 22.987  -55.358 87.574 1   5.35  ? 202 SER   D C     1 
ATOM   3452 O O     . SER   B 1 221 ? 24.029  -55.9   87.962 1   3     ? 202 SER   D O     1 
ATOM   3453 C CB    . SER   B 1 221 ? 22.024  -54.553 89.775 1   3.6   ? 202 SER   D CB    1 
ATOM   3454 O OG    . SER   B 1 221 ? 20.996  -55.518 89.715 1   4.33  ? 202 SER   D OG    1 
ATOM   3455 N N     . TYR   B 1 222 ? 22.325  -55.742 86.456 1   3     ? 203 TYR   D N     1 
ATOM   3456 C CA    . TYR   B 1 222 ? 22.806  -56.824 85.59  1   3     ? 203 TYR   D CA    1 
ATOM   3457 C C     . TYR   B 1 222 ? 22.159  -56.805 84.211 1   5.4   ? 203 TYR   D C     1 
ATOM   3458 O O     . TYR   B 1 222 ? 21.085  -56.228 84.024 1   3     ? 203 TYR   D O     1 
ATOM   3459 C CB    . TYR   B 1 222 ? 22.626  -58.228 86.251 1   3     ? 203 TYR   D CB    1 
ATOM   3460 C CG    . TYR   B 1 222 ? 21.19   -58.716 86.22  1   3     ? 203 TYR   D CG    1 
ATOM   3461 C CD1   . TYR   B 1 222 ? 20.7    -59.439 85.133 1   4.4   ? 203 TYR   D CD1   1 
ATOM   3462 C CD2   . TYR   B 1 222 ? 20.313  -58.429 87.267 1   3.17  ? 203 TYR   D CD2   1 
ATOM   3463 C CE1   . TYR   B 1 222 ? 19.358  -59.833 85.07  1   4.7   ? 203 TYR   D CE1   1 
ATOM   3464 C CE2   . TYR   B 1 222 ? 18.978  -58.828 87.222 1   4.13  ? 203 TYR   D CE2   1 
ATOM   3465 C CZ    . TYR   B 1 222 ? 18.506  -59.534 86.125 1   5.46  ? 203 TYR   D CZ    1 
ATOM   3466 O OH    . TYR   B 1 222 ? 17.189  -59.933 86.105 1   7.14  ? 203 TYR   D OH    1 
ATOM   3467 N N     . TYR   B 1 223 ? 22.782  -57.522 83.263 1   3     ? 204 TYR   D N     1 
ATOM   3468 C CA    . TYR   B 1 223 ? 22.244  -57.758 81.929 1   3     ? 204 TYR   D CA    1 
ATOM   3469 C C     . TYR   B 1 223 ? 22.738  -59.126 81.483 1   5.74  ? 204 TYR   D C     1 
ATOM   3470 O O     . TYR   B 1 223 ? 23.826  -59.555 81.898 1   3     ? 204 TYR   D O     1 
ATOM   3471 C CB    . TYR   B 1 223 ? 22.549  -56.642 80.91  1   3     ? 204 TYR   D CB    1 
ATOM   3472 C CG    . TYR   B 1 223 ? 23.992  -56.595 80.443 1   3     ? 204 TYR   D CG    1 
ATOM   3473 C CD1   . TYR   B 1 223 ? 24.971  -55.954 81.201 1   3.13  ? 204 TYR   D CD1   1 
ATOM   3474 C CD2   . TYR   B 1 223 ? 24.375  -57.17  79.231 1   3     ? 204 TYR   D CD2   1 
ATOM   3475 C CE1   . TYR   B 1 223 ? 26.295  -55.872 80.757 1   3     ? 204 TYR   D CE1   1 
ATOM   3476 C CE2   . TYR   B 1 223 ? 25.7    -57.109 78.786 1   3     ? 204 TYR   D CE2   1 
ATOM   3477 C CZ    . TYR   B 1 223 ? 26.657  -56.46  79.557 1   5.49  ? 204 TYR   D CZ    1 
ATOM   3478 O OH    . TYR   B 1 223 ? 27.97   -56.399 79.139 1   3     ? 204 TYR   D OH    1 
ATOM   3479 N N     . MET   B 1 224 ? 21.925  -59.799 80.663 1   3     ? 205 MET   D N     1 
ATOM   3480 C CA    . MET   B 1 224 ? 22.175  -61.17  80.22  1   3     ? 205 MET   D CA    1 
ATOM   3481 C C     . MET   B 1 224 ? 22.507  -61.288 78.746 1   4.32  ? 205 MET   D C     1 
ATOM   3482 O O     . MET   B 1 224 ? 21.951  -60.563 77.925 1   3     ? 205 MET   D O     1 
ATOM   3483 C CB    . MET   B 1 224 ? 20.91   -62.031 80.487 1   3     ? 205 MET   D CB    1 
ATOM   3484 C CG    . MET   B 1 224 ? 20.382  -62     81.918 1   3.04  ? 205 MET   D CG    1 
ATOM   3485 S SD    . MET   B 1 224 ? 21.515  -62.707 83.151 1   3.13  ? 205 MET   D SD    1 
ATOM   3486 C CE    . MET   B 1 224 ? 21.544  -64.481 82.623 1   4.84  ? 205 MET   D CE    1 
ATOM   3487 N N     . ILE   B 1 225 ? 23.343  -62.274 78.397 1   3     ? 206 ILE   D N     1 
ATOM   3488 C CA    . ILE   B 1 225 ? 23.615  -62.672 77.006 1   3     ? 206 ILE   D CA    1 
ATOM   3489 C C     . ILE   B 1 225 ? 23.366  -64.188 77.068 1   7.48  ? 206 ILE   D C     1 
ATOM   3490 O O     . ILE   B 1 225 ? 24.253  -64.938 77.493 1   5.28  ? 206 ILE   D O     1 
ATOM   3491 C CB    . ILE   B 1 225 ? 25.025  -62.329 76.485 1   5.16  ? 206 ILE   D CB    1 
ATOM   3492 C CG1   . ILE   B 1 225 ? 25.317  -60.812 76.635 1   4.83  ? 206 ILE   D CG1   1 
ATOM   3493 C CG2   . ILE   B 1 225 ? 25.181  -62.817 75.019 1   5.23  ? 206 ILE   D CG2   1 
ATOM   3494 C CD1   . ILE   B 1 225 ? 26.735  -60.407 76.251 1   3     ? 206 ILE   D CD1   1 
ATOM   3495 N N     . GLY   B 1 226 ? 22.126  -64.587 76.796 1   6.66  ? 207 GLY   D N     1 
ATOM   3496 C CA    . GLY   B 1 226 ? 21.702  -65.977 76.95  1   9.17  ? 207 GLY   D CA    1 
ATOM   3497 C C     . GLY   B 1 226 ? 21.74   -66.3   78.432 1   11.62 ? 207 GLY   D C     1 
ATOM   3498 O O     . GLY   B 1 226 ? 21.216  -65.53  79.25  1   8.75  ? 207 GLY   D O     1 
ATOM   3499 N N     . GLU   B 1 227 ? 22.449  -67.371 78.805 1   10.34 ? 208 GLU   D N     1 
ATOM   3500 C CA    . GLU   B 1 227 ? 22.579  -67.755 80.21  1   10.72 ? 208 GLU   D CA    1 
ATOM   3501 C C     . GLU   B 1 227 ? 23.717  -66.983 80.931 1   10.96 ? 208 GLU   D C     1 
ATOM   3502 O O     . GLU   B 1 227 ? 23.849  -67.087 82.147 1   8.06  ? 208 GLU   D O     1 
ATOM   3503 C CB    . GLU   B 1 227 ? 22.788  -69.275 80.33  1   15.42 ? 208 GLU   D CB    1 
ATOM   3504 C CG    . GLU   B 1 227 ? 21.509  -70.075 80.162 1   23.67 ? 208 GLU   D CG    1 
ATOM   3505 C CD    . GLU   B 1 227 ? 21.686  -71.564 80.371 1   51.05 ? 208 GLU   D CD    1 
ATOM   3506 O OE1   . GLU   B 1 227 ? 21.316  -72.052 81.463 1   62.92 ? 208 GLU   D OE1   1 
ATOM   3507 O OE2   . GLU   B 1 227 ? 22.192  -72.245 79.448 1   55.41 ? 208 GLU   D OE2   1 
ATOM   3508 N N     . GLN   B 1 228 ? 24.546  -66.235 80.178 1   6.42  ? 209 GLN   D N     1 
ATOM   3509 C CA    . GLN   B 1 228 ? 25.669  -65.508 80.762 1   4.37  ? 209 GLN   D CA    1 
ATOM   3510 C C     . GLN   B 1 228 ? 25.217  -64.194 81.401 1   5.19  ? 209 GLN   D C     1 
ATOM   3511 O O     . GLN   B 1 228 ? 24.645  -63.337 80.721 1   3     ? 209 GLN   D O     1 
ATOM   3512 C CB    . GLN   B 1 228 ? 26.78   -65.284 79.723 1   4.7   ? 209 GLN   D CB    1 
ATOM   3513 C CG    . GLN   B 1 228 ? 28.017  -64.515 80.221 1   11.04 ? 209 GLN   D CG    1 
ATOM   3514 C CD    . GLN   B 1 228 ? 28.84   -65.278 81.218 1   17.03 ? 209 GLN   D CD    1 
ATOM   3515 O OE1   . GLN   B 1 228 ? 28.935  -64.914 82.402 1   14.46 ? 209 GLN   D OE1   1 
ATOM   3516 N NE2   . GLN   B 1 228 ? 29.453  -66.347 80.755 1   4.24  ? 209 GLN   D NE2   1 
ATOM   3517 N N     . LYS   B 1 229 ? 25.517  -64.032 82.693 1   3     ? 210 LYS   D N     1 
ATOM   3518 C CA    . LYS   B 1 229 ? 25.183  -62.802 83.422 1   3     ? 210 LYS   D CA    1 
ATOM   3519 C C     . LYS   B 1 229 ? 26.391  -61.852 83.448 1   5.66  ? 210 LYS   D C     1 
ATOM   3520 O O     . LYS   B 1 229 ? 27.535  -62.304 83.601 1   3     ? 210 LYS   D O     1 
ATOM   3521 C CB    . LYS   B 1 229 ? 24.733  -63.145 84.853 1   3.98  ? 210 LYS   D CB    1 
ATOM   3522 C CG    . LYS   B 1 229 ? 24.209  -61.971 85.671 1   14.45 ? 210 LYS   D CG    1 
ATOM   3523 C CD    . LYS   B 1 229 ? 23.939  -62.417 87.104 1   17.46 ? 210 LYS   D CD    1 
ATOM   3524 C CE    . LYS   B 1 229 ? 22.973  -61.517 87.819 1   27.3  ? 210 LYS   D CE    1 
ATOM   3525 N NZ    . LYS   B 1 229 ? 22.461  -62.144 89.067 1   38.4  ? 210 LYS   D NZ    1 
ATOM   3526 N N     . PHE   B 1 230 ? 26.135  -60.545 83.333 1   3     ? 211 PHE   D N     1 
ATOM   3527 C CA    . PHE   B 1 230 ? 27.161  -59.509 83.42  1   3     ? 211 PHE   D CA    1 
ATOM   3528 C C     . PHE   B 1 230 ? 26.65   -58.458 84.38  1   5.33  ? 211 PHE   D C     1 
ATOM   3529 O O     . PHE   B 1 230 ? 25.474  -58.093 84.311 1   3     ? 211 PHE   D O     1 
ATOM   3530 C CB    . PHE   B 1 230 ? 27.423  -58.867 82.065 1   3.02  ? 211 PHE   D CB    1 
ATOM   3531 C CG    . PHE   B 1 230 ? 28.211  -59.74  81.124 1   3     ? 211 PHE   D CG    1 
ATOM   3532 C CD1   . PHE   B 1 230 ? 29.602  -59.754 81.163 1   3.36  ? 211 PHE   D CD1   1 
ATOM   3533 C CD2   . PHE   B 1 230 ? 27.565  -60.548 80.195 1   3.94  ? 211 PHE   D CD2   1 
ATOM   3534 C CE1   . PHE   B 1 230 ? 30.334  -60.578 80.304 1   3     ? 211 PHE   D CE1   1 
ATOM   3535 C CE2   . PHE   B 1 230 ? 28.301  -61.344 79.315 1   5.99  ? 211 PHE   D CE2   1 
ATOM   3536 C CZ    . PHE   B 1 230 ? 29.678  -61.365 79.389 1   3     ? 211 PHE   D CZ    1 
ATOM   3537 N N     . SER   B 1 231 ? 27.534  -57.973 85.259 1   3     ? 212 SER   D N     1 
ATOM   3538 C CA    . SER   B 1 231 ? 27.209  -56.953 86.259 1   3     ? 212 SER   D CA    1 
ATOM   3539 C C     . SER   B 1 231 ? 26.95   -55.597 85.594 1   4.19  ? 212 SER   D C     1 
ATOM   3540 O O     . SER   B 1 231 ? 27.427  -55.337 84.504 1   3     ? 212 SER   D O     1 
ATOM   3541 C CB    . SER   B 1 231 ? 28.368  -56.798 87.241 1   9.25  ? 212 SER   D CB    1 
ATOM   3542 O OG    . SER   B 1 231 ? 28.615  -58.019 87.928 1   9.46  ? 212 SER   D OG    1 
ATOM   3543 N N     . SER   B 1 232 ? 26.209  -54.74  86.27  1   3     ? 213 SER   D N     1 
ATOM   3544 C CA    . SER   B 1 232 ? 25.983  -53.373 85.839 1   3     ? 213 SER   D CA    1 
ATOM   3545 C C     . SER   B 1 232 ? 25.87   -52.52  87.102 1   5.71  ? 213 SER   D C     1 
ATOM   3546 O O     . SER   B 1 232 ? 25.36   -52.997 88.126 1   3     ? 213 SER   D O     1 
ATOM   3547 C CB    . SER   B 1 232 ? 24.729  -53.258 84.979 1   3.55  ? 213 SER   D CB    1 
ATOM   3548 O OG    . SER   B 1 232 ? 24.339  -51.903 84.825 1   3     ? 213 SER   D OG    1 
ATOM   3549 N N     . LEU   B 1 233 ? 26.377  -51.291 87.034 1   3     ? 214 LEU   D N     1 
ATOM   3550 C CA    . LEU   B 1 233 ? 26.322  -50.336 88.139 1   3     ? 214 LEU   D CA    1 
ATOM   3551 C C     . LEU   B 1 233 ? 24.919  -49.691 88.125 1   4.87  ? 214 LEU   D C     1 
ATOM   3552 O O     . LEU   B 1 233 ? 24.567  -49.007 87.149 1   3     ? 214 LEU   D O     1 
ATOM   3553 C CB    . LEU   B 1 233 ? 27.446  -49.287 87.99  1   3     ? 214 LEU   D CB    1 
ATOM   3554 C CG    . LEU   B 1 233 ? 27.535  -48.163 89.034 1   6.83  ? 214 LEU   D CG    1 
ATOM   3555 C CD1   . LEU   B 1 233 ? 27.764  -48.728 90.462 1   6.11  ? 214 LEU   D CD1   1 
ATOM   3556 C CD2   . LEU   B 1 233 ? 28.639  -47.165 88.641 1   7.27  ? 214 LEU   D CD2   1 
ATOM   3557 N N     . PRO   B 1 234 ? 24.094  -49.932 89.17  1   3     ? 215 PRO   D N     1 
ATOM   3558 C CA    . PRO   B 1 234 ? 22.732  -49.377 89.154 1   3     ? 215 PRO   D CA    1 
ATOM   3559 C C     . PRO   B 1 234 ? 22.747  -47.906 89.56  1   6.91  ? 215 PRO   D C     1 
ATOM   3560 O O     . PRO   B 1 234 ? 22.88   -47.59  90.74  1   6.7   ? 215 PRO   D O     1 
ATOM   3561 C CB    . PRO   B 1 234 ? 21.963  -50.287 90.127 1   4.03  ? 215 PRO   D CB    1 
ATOM   3562 C CG    . PRO   B 1 234 ? 22.997  -50.782 91.085 1   6.73  ? 215 PRO   D CG    1 
ATOM   3563 C CD    . PRO   B 1 234 ? 24.336  -50.749 90.386 1   3.94  ? 215 PRO   D CD    1 
ATOM   3564 N N     . LEU   B 1 235 ? 22.689  -47.01  88.559 1   3.63  ? 216 LEU   D N     1 
ATOM   3565 C CA    . LEU   B 1 235 ? 22.712  -45.562 88.785 1   3     ? 216 LEU   D CA    1 
ATOM   3566 C C     . LEU   B 1 235 ? 21.404  -44.918 88.373 1   5.75  ? 216 LEU   D C     1 
ATOM   3567 O O     . LEU   B 1 235 ? 20.855  -45.25  87.311 1   3     ? 216 LEU   D O     1 
ATOM   3568 C CB    . LEU   B 1 235 ? 23.841  -44.89  87.949 1   3     ? 216 LEU   D CB    1 
ATOM   3569 C CG    . LEU   B 1 235 ? 25.303  -45.175 88.299 1   7.12  ? 216 LEU   D CG    1 
ATOM   3570 C CD1   . LEU   B 1 235 ? 26.221  -44.231 87.554 1   7.16  ? 216 LEU   D CD1   1 
ATOM   3571 C CD2   . LEU   B 1 235 ? 25.553  -45.078 89.82  1   5.29  ? 216 LEU   D CD2   1 
ATOM   3572 N N     . GLY   B 1 236 ? 20.965  -43.952 89.18  1   3     ? 217 GLY   D N     1 
ATOM   3573 C CA    . GLY   B 1 236 ? 19.78   -43.152 88.89  1   3     ? 217 GLY   D CA    1 
ATOM   3574 C C     . GLY   B 1 236 ? 20.188  -41.903 88.129 1   4.92  ? 217 GLY   D C     1 
ATOM   3575 O O     . GLY   B 1 236 ? 21.376  -41.563 88.088 1   3     ? 217 GLY   D O     1 
ATOM   3576 N N     . ARG   B 1 237 ? 19.214  -41.182 87.555 1   3     ? 218 ARG   D N     1 
ATOM   3577 C CA    . ARG   B 1 237 ? 19.502  -39.967 86.781 1   3     ? 218 ARG   D CA    1 
ATOM   3578 C C     . ARG   B 1 237 ? 20.313  -38.904 87.56  1   4.72  ? 218 ARG   D C     1 
ATOM   3579 O O     . ARG   B 1 237 ? 21.187  -38.255 86.979 1   3     ? 218 ARG   D O     1 
ATOM   3580 C CB    . ARG   B 1 237 ? 18.224  -39.355 86.181 1   6.43  ? 218 ARG   D CB    1 
ATOM   3581 C CG    . ARG   B 1 237 ? 17.209  -38.851 87.212 1   9.09  ? 218 ARG   D CG    1 
ATOM   3582 C CD    . ARG   B 1 237 ? 16.214  -37.865 86.611 1   19.58 ? 218 ARG   D CD    1 
ATOM   3583 N NE    . ARG   B 1 237 ? 16.823  -36.565 86.305 1   33.46 ? 218 ARG   D NE    1 
ATOM   3584 C CZ    . ARG   B 1 237 ? 16.892  -36.045 85.082 1   63.3  ? 218 ARG   D CZ    1 
ATOM   3585 N NH1   . ARG   B 1 237 ? 16.374  -36.695 84.049 1   55.67 ? 218 ARG   D NH1   1 
ATOM   3586 N NH2   . ARG   B 1 237 ? 17.44   -34.853 84.889 1   45.83 ? 218 ARG   D NH2   1 
ATOM   3587 N N     . GLU   B 1 238 ? 20.026  -38.748 88.861 1   3     ? 219 GLU   D N     1 
ATOM   3588 C CA    . GLU   B 1 238 ? 20.707  -37.76  89.719 1   3     ? 219 GLU   D CA    1 
ATOM   3589 C C     . GLU   B 1 238 ? 22.209  -38.085 89.852 1   5.05  ? 219 GLU   D C     1 
ATOM   3590 O O     . GLU   B 1 238 ? 23.039  -37.177 89.726 1   3     ? 219 GLU   D O     1 
ATOM   3591 C CB    . GLU   B 1 238 ? 20.033  -37.697 91.107 1   4.55  ? 219 GLU   D CB    1 
ATOM   3592 C CG    . GLU   B 1 238 ? 18.553  -37.335 91.047 1   9.44  ? 219 GLU   D CG    1 
ATOM   3593 C CD    . GLU   B 1 238 ? 17.564  -38.494 90.968 1   11.85 ? 219 GLU   D CD    1 
ATOM   3594 O OE1   . GLU   B 1 238 ? 17.977  -39.653 90.7   1   8.33  ? 219 GLU   D OE1   1 
ATOM   3595 O OE2   . GLU   B 1 238 ? 16.355  -38.229 91.173 1   28.1  ? 219 GLU   D OE2   1 
ATOM   3596 N N     . ALA   B 1 239 ? 22.553  -39.383 90.062 1   3     ? 220 ALA   D N     1 
ATOM   3597 C CA    . ALA   B 1 239 ? 23.955  -39.818 90.203 1   3     ? 220 ALA   D CA    1 
ATOM   3598 C C     . ALA   B 1 239 ? 24.722  -39.67  88.877 1   5.56  ? 220 ALA   D C     1 
ATOM   3599 O O     . ALA   B 1 239 ? 25.915  -39.314 88.885 1   3     ? 220 ALA   D O     1 
ATOM   3600 C CB    . ALA   B 1 239 ? 24.024  -41.252 90.7   1   3.7   ? 220 ALA   D CB    1 
ATOM   3601 N N     . VAL   B 1 240 ? 24.033  -39.926 87.732 1   3     ? 221 VAL   D N     1 
ATOM   3602 C CA    . VAL   B 1 240 ? 24.648  -39.782 86.399 1   3     ? 221 VAL   D CA    1 
ATOM   3603 C C     . VAL   B 1 240 ? 25.002  -38.297 86.178 1   4.3   ? 221 VAL   D C     1 
ATOM   3604 O O     . VAL   B 1 240 ? 26.16   -37.979 85.908 1   3     ? 221 VAL   D O     1 
ATOM   3605 C CB    . VAL   B 1 240 ? 23.745  -40.328 85.26  1   4.15  ? 221 VAL   D CB    1 
ATOM   3606 C CG1   . VAL   B 1 240 ? 24.372  -40.039 83.893 1   3.4   ? 221 VAL   D CG1   1 
ATOM   3607 C CG2   . VAL   B 1 240 ? 23.496  -41.828 85.424 1   3     ? 221 VAL   D CG2   1 
ATOM   3608 N N     . GLU   B 1 241 ? 24.011  -37.404 86.372 1   3     ? 222 GLU   D N     1 
ATOM   3609 C CA    . GLU   B 1 241 ? 24.189  -35.946 86.249 1   3.35  ? 222 GLU   D CA    1 
ATOM   3610 C C     . GLU   B 1 241 ? 25.323  -35.436 87.139 1   5.22  ? 222 GLU   D C     1 
ATOM   3611 O O     . GLU   B 1 241 ? 26.197  -34.721 86.648 1   3     ? 222 GLU   D O     1 
ATOM   3612 C CB    . GLU   B 1 241 ? 22.899  -35.197 86.597 1   5.33  ? 222 GLU   D CB    1 
ATOM   3613 C CG    . GLU   B 1 241 ? 21.867  -35.261 85.503 1   8.64  ? 222 GLU   D CG    1 
ATOM   3614 C CD    . GLU   B 1 241 ? 20.493  -34.794 85.942 1   29.38 ? 222 GLU   D CD    1 
ATOM   3615 O OE1   . GLU   B 1 241 ? 20.208  -33.584 85.793 1   40.66 ? 222 GLU   D OE1   1 
ATOM   3616 O OE2   . GLU   B 1 241 ? 19.7    -35.637 86.426 1   26.64 ? 222 GLU   D OE2   1 
ATOM   3617 N N     . ALA   B 1 242 ? 25.314  -35.823 88.436 1   3     ? 223 ALA   D N     1 
ATOM   3618 C CA    . ALA   B 1 242 ? 26.349  -35.416 89.391 1   3     ? 223 ALA   D CA    1 
ATOM   3619 C C     . ALA   B 1 242 ? 27.756  -35.88  88.946 1   4.92  ? 223 ALA   D C     1 
ATOM   3620 O O     . ALA   B 1 242 ? 28.68   -35.078 88.951 1   3     ? 223 ALA   D O     1 
ATOM   3621 C CB    . ALA   B 1 242 ? 26.022  -35.93  90.793 1   3.12  ? 223 ALA   D CB    1 
ATOM   3622 N N     . ALA   B 1 243 ? 27.902  -37.145 88.51  1   3     ? 224 ALA   D N     1 
ATOM   3623 C CA    . ALA   B 1 243 ? 29.2    -37.675 88.05  1   3     ? 224 ALA   D CA    1 
ATOM   3624 C C     . ALA   B 1 243 ? 29.758  -36.914 86.822 1   5.64  ? 224 ALA   D C     1 
ATOM   3625 O O     . ALA   B 1 243 ? 30.965  -36.625 86.774 1   3     ? 224 ALA   D O     1 
ATOM   3626 C CB    . ALA   B 1 243 ? 29.081  -39.152 87.742 1   3.23  ? 224 ALA   D CB    1 
ATOM   3627 N N     . VAL   B 1 244 ? 28.882  -36.583 85.847 1   3     ? 225 VAL   D N     1 
ATOM   3628 C CA    . VAL   B 1 244 ? 29.24   -35.828 84.641 1   3     ? 225 VAL   D CA    1 
ATOM   3629 C C     . VAL   B 1 244 ? 29.746  -34.411 85.048 1   5.5   ? 225 VAL   D C     1 
ATOM   3630 O O     . VAL   B 1 244 ? 30.794  -33.967 84.551 1   3     ? 225 VAL   D O     1 
ATOM   3631 C CB    . VAL   B 1 244 ? 28.053  -35.785 83.639 1   4.15  ? 225 VAL   D CB    1 
ATOM   3632 C CG1   . VAL   B 1 244 ? 28.302  -34.799 82.49  1   3.11  ? 225 VAL   D CG1   1 
ATOM   3633 C CG2   . VAL   B 1 244 ? 27.748  -37.186 83.095 1   3     ? 225 VAL   D CG2   1 
ATOM   3634 N N     . LYS   B 1 245 ? 29.037  -33.737 85.99  1   3     ? 226 LYS   D N     1 
ATOM   3635 C CA    . LYS   B 1 245 ? 29.464  -32.398 86.456 1   3     ? 226 LYS   D CA    1 
ATOM   3636 C C     . LYS   B 1 245 ? 30.778  -32.492 87.253 1   5.32  ? 226 LYS   D C     1 
ATOM   3637 O O     . LYS   B 1 245 ? 31.67   -31.655 87.08  1   3     ? 226 LYS   D O     1 
ATOM   3638 C CB    . LYS   B 1 245 ? 28.382  -31.711 87.291 1   3.56  ? 226 LYS   D CB    1 
ATOM   3639 C CG    . LYS   B 1 245 ? 27.118  -31.395 86.518 1   12.99 ? 226 LYS   D CG    1 
ATOM   3640 C CD    . LYS   B 1 245 ? 26.015  -30.932 87.468 1   14.66 ? 226 LYS   D CD    1 
ATOM   3641 C CE    . LYS   B 1 245 ? 24.642  -31.043 86.85  1   19.21 ? 226 LYS   D CE    1 
ATOM   3642 N NZ    . LYS   B 1 245 ? 24.378  -29.938 85.888 1   26.55 ? 226 LYS   D NZ    1 
ATOM   3643 N N     . GLU   B 1 246 ? 30.902  -33.528 88.108 1   3     ? 227 GLU   D N     1 
ATOM   3644 C CA    . GLU   B 1 246 ? 32.103  -33.753 88.91  1   3     ? 227 GLU   D CA    1 
ATOM   3645 C C     . GLU   B 1 246 ? 33.311  -34.005 87.984 1   5.18  ? 227 GLU   D C     1 
ATOM   3646 O O     . GLU   B 1 246 ? 34.409  -33.536 88.267 1   3     ? 227 GLU   D O     1 
ATOM   3647 C CB    . GLU   B 1 246 ? 31.899  -34.94  89.859 1   4.47  ? 227 GLU   D CB    1 
ATOM   3648 C CG    . GLU   B 1 246 ? 32.974  -35.108 90.92  1   8.74  ? 227 GLU   D CG    1 
ATOM   3649 C CD    . GLU   B 1 246 ? 32.729  -36.259 91.885 1   15.25 ? 227 GLU   D CD    1 
ATOM   3650 O OE1   . GLU   B 1 246 ? 31.547  -36.622 92.098 1   12.58 ? 227 GLU   D OE1   1 
ATOM   3651 O OE2   . GLU   B 1 246 ? 33.723  -36.807 92.417 1   20.55 ? 227 GLU   D OE2   1 
ATOM   3652 N N     . ALA   B 1 247 ? 33.088  -34.719 86.864 1   3     ? 228 ALA   D N     1 
ATOM   3653 C CA    . ALA   B 1 247 ? 34.135  -35.063 85.905 1   3     ? 228 ALA   D CA    1 
ATOM   3654 C C     . ALA   B 1 247 ? 34.601  -33.896 85.005 1   5.88  ? 228 ALA   D C     1 
ATOM   3655 O O     . ALA   B 1 247 ? 35.47   -34.107 84.151 1   3     ? 228 ALA   D O     1 
ATOM   3656 C CB    . ALA   B 1 247 ? 33.683  -36.246 85.056 1   3     ? 228 ALA   D CB    1 
ATOM   3657 N N     . GLY   B 1 248 ? 34.033  -32.694 85.197 1   3     ? 229 GLY   D N     1 
ATOM   3658 C CA    . GLY   B 1 248 ? 34.451  -31.513 84.436 1   3     ? 229 GLY   D CA    1 
ATOM   3659 C C     . GLY   B 1 248 ? 33.737  -31.215 83.137 1   5.84  ? 229 GLY   D C     1 
ATOM   3660 O O     . GLY   B 1 248 ? 34.353  -30.659 82.221 1   3     ? 229 GLY   D O     1 
ATOM   3661 N N     . TYR   B 1 249 ? 32.415  -31.532 83.061 1   3     ? 230 TYR   D N     1 
ATOM   3662 C CA    . TYR   B 1 249 ? 31.58   -31.239 81.896 1   3     ? 230 TYR   D CA    1 
ATOM   3663 C C     . TYR   B 1 249 ? 30.404  -30.347 82.288 1   5.25  ? 230 TYR   D C     1 
ATOM   3664 O O     . TYR   B 1 249 ? 30.046  -30.292 83.472 1   3     ? 230 TYR   D O     1 
ATOM   3665 C CB    . TYR   B 1 249 ? 30.969  -32.536 81.302 1   3     ? 230 TYR   D CB    1 
ATOM   3666 C CG    . TYR   B 1 249 ? 31.983  -33.558 80.853 1   3     ? 230 TYR   D CG    1 
ATOM   3667 C CD1   . TYR   B 1 249 ? 32.477  -34.516 81.74  1   4.05  ? 230 TYR   D CD1   1 
ATOM   3668 C CD2   . TYR   B 1 249 ? 32.412  -33.607 79.529 1   3     ? 230 TYR   D CD2   1 
ATOM   3669 C CE1   . TYR   B 1 249 ? 33.388  -35.485 81.325 1   3     ? 230 TYR   D CE1   1 
ATOM   3670 C CE2   . TYR   B 1 249 ? 33.324  -34.572 79.1   1   3     ? 230 TYR   D CE2   1 
ATOM   3671 C CZ    . TYR   B 1 249 ? 33.821  -35.5   80.007 1   7.24  ? 230 TYR   D CZ    1 
ATOM   3672 O OH    . TYR   B 1 249 ? 34.709  -36.46  79.597 1   3     ? 230 TYR   D OH    1 
ATOM   3673 N N     . THR   B 1 250 ? 29.772  -29.697 81.289 1   3     ? 231 THR   D N     1 
ATOM   3674 C CA    . THR   B 1 250 ? 28.51   -28.968 81.487 1   3     ? 231 THR   D CA    1 
ATOM   3675 C C     . THR   B 1 250 ? 27.462  -29.692 80.661 1   5.35  ? 231 THR   D C     1 
ATOM   3676 O O     . THR   B 1 250 ? 27.699  -29.966 79.476 1   3.44  ? 231 THR   D O     1 
ATOM   3677 C CB    . THR   B 1 250 ? 28.582  -27.492 81.112 1   7.15  ? 231 THR   D CB    1 
ATOM   3678 O OG1   . THR   B 1 250 ? 28.983  -27.372 79.746 1   3     ? 231 THR   D OG1   1 
ATOM   3679 C CG2   . THR   B 1 250 ? 29.492  -26.719 82.027 1   7.9   ? 231 THR   D CG2   1 
ATOM   3680 N N     . ILE   B 1 251 ? 26.309  -29.992 81.27  1   3     ? 232 ILE   D N     1 
ATOM   3681 C CA    . ILE   B 1 251 ? 25.237  -30.725 80.582 1   3     ? 232 ILE   D CA    1 
ATOM   3682 C C     . ILE   B 1 251 ? 24.424  -29.788 79.685 1   5.89  ? 232 ILE   D C     1 
ATOM   3683 O O     . ILE   B 1 251 ? 23.964  -28.744 80.161 1   3     ? 232 ILE   D O     1 
ATOM   3684 C CB    . ILE   B 1 251 ? 24.348  -31.507 81.604 1   5.9   ? 232 ILE   D CB    1 
ATOM   3685 C CG1   . ILE   B 1 251 ? 25.197  -32.579 82.348 1   6.26  ? 232 ILE   D CG1   1 
ATOM   3686 C CG2   . ILE   B 1 251 ? 23.129  -32.168 80.89  1   6.63  ? 232 ILE   D CG2   1 
ATOM   3687 C CD1   . ILE   B 1 251 ? 24.576  -33.132 83.68  1   6.94  ? 232 ILE   D CD1   1 
ATOM   3688 N N     . GLU   B 1 252 ? 24.24   -30.166 78.406 1   3     ? 233 GLU   D N     1 
ATOM   3689 C CA    . GLU   B 1 252 ? 23.442  -29.41  77.429 1   3     ? 233 GLU   D CA    1 
ATOM   3690 C C     . GLU   B 1 252 ? 22.005  -29.911 77.527 1   5.91  ? 233 GLU   D C     1 
ATOM   3691 O O     . GLU   B 1 252 ? 21.079  -29.115 77.56  1   3     ? 233 GLU   D O     1 
ATOM   3692 C CB    . GLU   B 1 252 ? 23.976  -29.607 76     1   4.81  ? 233 GLU   D CB    1 
ATOM   3693 C CG    . GLU   B 1 252 ? 25.383  -29.066 75.802 1   5.63  ? 233 GLU   D CG    1 
ATOM   3694 C CD    . GLU   B 1 252 ? 25.47   -27.685 75.168 1   31.28 ? 233 GLU   D CD    1 
ATOM   3695 O OE1   . GLU   B 1 252 ? 26.124  -26.803 75.773 1   29.68 ? 233 GLU   D OE1   1 
ATOM   3696 O OE2   . GLU   B 1 252 ? 24.902  -27.486 74.066 1   40.78 ? 233 GLU   D OE2   1 
ATOM   3697 N N     . TRP   B 1 253 ? 21.837  -31.246 77.553 1   5.83  ? 234 TRP   D N     1 
ATOM   3698 C CA    . TRP   B 1 253 ? 20.526  -31.857 77.739 1   10.61 ? 234 TRP   D CA    1 
ATOM   3699 C C     . TRP   B 1 253 ? 20.611  -33.262 78.262 1   6.78  ? 234 TRP   D C     1 
ATOM   3700 O O     . TRP   B 1 253 ? 21.642  -33.928 78.159 1   3     ? 234 TRP   D O     1 
ATOM   3701 C CB    . TRP   B 1 253 ? 19.583  -31.773 76.551 1   14.92 ? 234 TRP   D CB    1 
ATOM   3702 C CG    . TRP   B 1 253 ? 20.035  -32.401 75.286 1   13.59 ? 234 TRP   D CG    1 
ATOM   3703 C CD1   . TRP   B 1 253 ? 19.726  -33.653 74.843 1   10.43 ? 234 TRP   D CD1   1 
ATOM   3704 C CD2   . TRP   B 1 253 ? 20.612  -31.709 74.176 1   13.09 ? 234 TRP   D CD2   1 
ATOM   3705 N NE1   . TRP   B 1 253 ? 20.174  -33.817 73.546 1   10.27 ? 234 TRP   D NE1   1 
ATOM   3706 C CE2   . TRP   B 1 253 ? 20.721  -32.634 73.113 1   8.84  ? 234 TRP   D CE2   1 
ATOM   3707 C CE3   . TRP   B 1 253 ? 21.077  -30.395 73.984 1   11.43 ? 234 TRP   D CE3   1 
ATOM   3708 C CZ2   . TRP   B 1 253 ? 21.313  -32.3   71.887 1   9     ? 234 TRP   D CZ2   1 
ATOM   3709 C CZ3   . TRP   B 1 253 ? 21.664  -30.061 72.772 1   9.65  ? 234 TRP   D CZ3   1 
ATOM   3710 C CH2   . TRP   B 1 253 ? 21.795  -31.012 71.745 1   8.84  ? 234 TRP   D CH2   1 
ATOM   3711 N N     . PHE   B 1 254 ? 19.517  -33.666 78.88  1   3     ? 235 PHE   D N     1 
ATOM   3712 C CA    . PHE   B 1 254 ? 19.403  -34.937 79.561 1   3     ? 235 PHE   D CA    1 
ATOM   3713 C C     . PHE   B 1 254 ? 17.977  -35.41  79.356 1   4.34  ? 235 PHE   D C     1 
ATOM   3714 O O     . PHE   B 1 254 ? 17.038  -34.652 79.595 1   3     ? 235 PHE   D O     1 
ATOM   3715 C CB    . PHE   B 1 254 ? 19.708  -34.747 81.056 1   3     ? 235 PHE   D CB    1 
ATOM   3716 C CG    . PHE   B 1 254 ? 20.043  -36.033 81.766 1   3     ? 235 PHE   D CG    1 
ATOM   3717 C CD1   . PHE   B 1 254 ? 19.043  -36.917 82.153 1   5.5   ? 235 PHE   D CD1   1 
ATOM   3718 C CD2   . PHE   B 1 254 ? 21.36   -36.367 82.044 1   3.43  ? 235 PHE   D CD2   1 
ATOM   3719 C CE1   . PHE   B 1 254 ? 19.361  -38.127 82.784 1   5.75  ? 235 PHE   D CE1   1 
ATOM   3720 C CE2   . PHE   B 1 254 ? 21.672  -37.572 82.678 1   5.42  ? 235 PHE   D CE2   1 
ATOM   3721 C CZ    . PHE   B 1 254 ? 20.672  -38.449 83.025 1   3     ? 235 PHE   D CZ    1 
ATOM   3722 N N     . GLU   B 1 255 ? 17.837  -36.625 78.857 1   3     ? 236 GLU   D N     1 
ATOM   3723 C CA    . GLU   B 1 255 ? 16.544  -37.229 78.578 1   3     ? 236 GLU   D CA    1 
ATOM   3724 C C     . GLU   B 1 255 ? 16.456  -38.593 79.249 1   5.3   ? 236 GLU   D C     1 
ATOM   3725 O O     . GLU   B 1 255 ? 17.438  -39.329 79.255 1   3     ? 236 GLU   D O     1 
ATOM   3726 C CB    . GLU   B 1 255 ? 16.346  -37.39  77.059 1   3.95  ? 236 GLU   D CB    1 
ATOM   3727 C CG    . GLU   B 1 255 ? 14.952  -37.88  76.694 1   7.41  ? 236 GLU   D CG    1 
ATOM   3728 C CD    . GLU   B 1 255 ? 14.669  -38.036 75.214 1   25.18 ? 236 GLU   D CD    1 
ATOM   3729 O OE1   . GLU   B 1 255 ? 14.849  -37.05  74.459 1   36.75 ? 236 GLU   D OE1   1 
ATOM   3730 O OE2   . GLU   B 1 255 ? 14.251  -39.145 74.813 1   30.44 ? 236 GLU   D OE2   1 
ATOM   3731 N N     . VAL   B 1 256 ? 15.265  -38.932 79.795 1   3     ? 237 VAL   D N     1 
ATOM   3732 C CA    . VAL   B 1 256 ? 15.033  -40.232 80.425 1   3     ? 237 VAL   D CA    1 
ATOM   3733 C C     . VAL   B 1 256 ? 13.806  -40.837 79.749 1   5.62  ? 237 VAL   D C     1 
ATOM   3734 O O     . VAL   B 1 256 ? 12.824  -40.12  79.535 1   3     ? 237 VAL   D O     1 
ATOM   3735 C CB    . VAL   B 1 256 ? 14.828  -40.073 81.959 1   6.98  ? 237 VAL   D CB    1 
ATOM   3736 C CG1   . VAL   B 1 256 ? 14.275  -41.347 82.598 1   6.52  ? 237 VAL   D CG1   1 
ATOM   3737 C CG2   . VAL   B 1 256 ? 16.134  -39.677 82.637 1   6.65  ? 237 VAL   D CG2   1 
ATOM   3738 N N     . ILE   B 1 257 ? 13.884  -42.126 79.382 1   3     ? 238 ILE   D N     1 
ATOM   3739 C CA    . ILE   B 1 257 ? 12.755  -42.871 78.825 1   4.15  ? 238 ILE   D CA    1 
ATOM   3740 C C     . ILE   B 1 257 ? 12.404  -43.927 79.86  1   7.31  ? 238 ILE   D C     1 
ATOM   3741 O O     . ILE   B 1 257 ? 13.294  -44.44  80.55  1   3.2   ? 238 ILE   D O     1 
ATOM   3742 C CB    . ILE   B 1 257 ? 12.991  -43.455 77.407 1   8.57  ? 238 ILE   D CB    1 
ATOM   3743 C CG1   . ILE   B 1 257 ? 14.098  -44.544 77.385 1   8.79  ? 238 ILE   D CG1   1 
ATOM   3744 C CG2   . ILE   B 1 257 ? 13.287  -42.331 76.429 1   7.37  ? 238 ILE   D CG2   1 
ATOM   3745 C CD1   . ILE   B 1 257 ? 14.074  -45.524 76.138 1   12.27 ? 238 ILE   D CD1   1 
ATOM   3746 N N     A SER   B 1 258 ? 11.115  -44.228 79.998 0.5 4.53  ? 239 SER   D N     1 
ATOM   3747 N N     B SER   B 1 258 ? 11.11   -44.229 79.998 0.5 5.19  ? 239 SER   D N     1 
ATOM   3748 C CA    A SER   B 1 258 ? 10.62   -45.22  80.952 0.5 5.08  ? 239 SER   D CA    1 
ATOM   3749 C CA    B SER   B 1 258 ? 10.637  -45.21  80.972 0.5 6.09  ? 239 SER   D CA    1 
ATOM   3750 C C     A SER   B 1 258 ? 10.838  -46.662 80.465 0.5 7.27  ? 239 SER   D C     1 
ATOM   3751 C C     B SER   B 1 258 ? 10.757  -46.669 80.465 0.5 7.46  ? 239 SER   D C     1 
ATOM   3752 O O     A SER   B 1 258 ? 10.912  -47.575 81.291 0.5 7.48  ? 239 SER   D O     1 
ATOM   3753 O O     B SER   B 1 258 ? 10.728  -47.594 81.281 0.5 7.76  ? 239 SER   D O     1 
ATOM   3754 C CB    A SER   B 1 258 ? 9.13    -44.999 81.191 0.5 7.52  ? 239 SER   D CB    1 
ATOM   3755 C CB    B SER   B 1 258 ? 9.206   -44.888 81.4   0.5 7.94  ? 239 SER   D CB    1 
ATOM   3756 O OG    A SER   B 1 258 ? 8.474   -44.807 79.948 0.5 3.23  ? 239 SER   D OG    1 
ATOM   3757 O OG    B SER   B 1 258 ? 9.065   -43.514 81.736 0.5 4.91  ? 239 SER   D OG    1 
ATOM   3758 N N     . GLN   B 1 259 ? 10.903  -46.865 79.13  1   6.54  ? 240 GLN   D N     1 
ATOM   3759 C CA    . GLN   B 1 259 ? 11.043  -48.2   78.5   1   6.7   ? 240 GLN   D CA    1 
ATOM   3760 C C     . GLN   B 1 259 ? 12.228  -49.019 79.028 1   7.74  ? 240 GLN   D C     1 
ATOM   3761 O O     . GLN   B 1 259 ? 13.362  -48.562 78.955 1   7.27  ? 240 GLN   D O     1 
ATOM   3762 C CB    . GLN   B 1 259 ? 11.103  -48.083 76.958 1   9.05  ? 240 GLN   D CB    1 
ATOM   3763 C CG    . GLN   B 1 259 ? 11.205  -49.43  76.212 1   16.29 ? 240 GLN   D CG    1 
ATOM   3764 C CD    . GLN   B 1 259 ? 9.969   -50.288 76.338 1   25.32 ? 240 GLN   D CD    1 
ATOM   3765 O OE1   . GLN   B 1 259 ? 8.872   -49.887 75.937 1   26.35 ? 240 GLN   D OE1   1 
ATOM   3766 N NE2   . GLN   B 1 259 ? 10.131  -51.492 76.897 1   20.38 ? 240 GLN   D NE2   1 
ATOM   3767 N N     . SER   B 1 260 ? 11.951  -50.218 79.576 1   3.97  ? 241 SER   D N     1 
ATOM   3768 C CA    . SER   B 1 260 ? 12.97   -51.12  80.101 1   3.66  ? 241 SER   D CA    1 
ATOM   3769 C C     . SER   B 1 260 ? 13.185  -52.321 79.15  1   6.18  ? 241 SER   D C     1 
ATOM   3770 O O     . SER   B 1 260 ? 12.334  -52.571 78.286 1   3     ? 241 SER   D O     1 
ATOM   3771 C CB    . SER   B 1 260 ? 12.557  -51.605 81.489 1   7.41  ? 241 SER   D CB    1 
ATOM   3772 O OG    . SER   B 1 260 ? 12.59   -50.51  82.395 1   7.72  ? 241 SER   D OG    1 
ATOM   3773 N N     . TYR   B 1 261 ? 14.322  -53.057 79.293 1   3     ? 242 TYR   D N     1 
ATOM   3774 C CA    . TYR   B 1 261 ? 14.565  -54.265 78.483 1   3     ? 242 TYR   D CA    1 
ATOM   3775 C C     . TYR   B 1 261 ? 13.648  -55.365 79.024 1   5.46  ? 242 TYR   D C     1 
ATOM   3776 O O     . TYR   B 1 261 ? 13.097  -55.202 80.123 1   4.48  ? 242 TYR   D O     1 
ATOM   3777 C CB    . TYR   B 1 261 ? 16.037  -54.731 78.599 1   3     ? 242 TYR   D CB    1 
ATOM   3778 C CG    . TYR   B 1 261 ? 17.014  -53.855 77.847 1   3     ? 242 TYR   D CG    1 
ATOM   3779 C CD1   . TYR   B 1 261 ? 17.372  -54.143 76.53  1   3.62  ? 242 TYR   D CD1   1 
ATOM   3780 C CD2   . TYR   B 1 261 ? 17.546  -52.707 78.435 1   3     ? 242 TYR   D CD2   1 
ATOM   3781 C CE1   . TYR   B 1 261 ? 18.25   -53.316 75.819 1   3.19  ? 242 TYR   D CE1   1 
ATOM   3782 C CE2   . TYR   B 1 261 ? 18.404  -51.859 77.726 1   3     ? 242 TYR   D CE2   1 
ATOM   3783 C CZ    . TYR   B 1 261 ? 18.756  -52.168 76.42  1   4.22  ? 242 TYR   D CZ    1 
ATOM   3784 O OH    . TYR   B 1 261 ? 19.609  -51.336 75.724 1   3     ? 242 TYR   D OH    1 
ATOM   3785 N N     . SER   B 1 262 ? 13.543  -56.507 78.324 1   3     ? 243 SER   D N     1 
ATOM   3786 C CA    . SER   B 1 262 ? 12.729  -57.628 78.809 1   4.36  ? 243 SER   D CA    1 
ATOM   3787 C C     . SER   B 1 262 ? 13.204  -58.05  80.219 1   6.75  ? 243 SER   D C     1 
ATOM   3788 O O     . SER   B 1 262 ? 14.401  -58.019 80.478 1   3     ? 243 SER   D O     1 
ATOM   3789 C CB    . SER   B 1 262 ? 12.818  -58.8   77.839 1   8.56  ? 243 SER   D CB    1 
ATOM   3790 O OG    . SER   B 1 262 ? 12.323  -58.412 76.567 1   11.24 ? 243 SER   D OG    1 
ATOM   3791 N N     . SER   B 1 263 ? 12.276  -58.423 81.14  1   5.65  ? 244 SER   D N     1 
ATOM   3792 C CA    . SER   B 1 263 ? 12.688  -58.797 82.507 1   5.58  ? 244 SER   D CA    1 
ATOM   3793 C C     . SER   B 1 263 ? 13.653  -60.004 82.572 1   8.99  ? 244 SER   D C     1 
ATOM   3794 O O     . SER   B 1 263 ? 14.391  -60.155 83.554 1   7.8   ? 244 SER   D O     1 
ATOM   3795 C CB    . SER   B 1 263 ? 11.472  -59.023 83.402 1   11.18 ? 244 SER   D CB    1 
ATOM   3796 O OG    . SER   B 1 263 ? 10.735  -60.133 82.928 1   17.44 ? 244 SER   D OG    1 
ATOM   3797 N N     . THR   B 1 264 ? 13.661  -60.827 81.514 1   7.74  ? 245 THR   D N     1 
ATOM   3798 C CA    . THR   B 1 264 ? 14.513  -62.008 81.371 1   10.27 ? 245 THR   D CA    1 
ATOM   3799 C C     . THR   B 1 264 ? 15.931  -61.614 80.922 1   12.49 ? 245 THR   D C     1 
ATOM   3800 O O     . THR   B 1 264 ? 16.845  -62.458 80.936 1   13.18 ? 245 THR   D O     1 
ATOM   3801 C CB    . THR   B 1 264 ? 13.84   -63.028 80.414 1   17.02 ? 245 THR   D CB    1 
ATOM   3802 O OG1   . THR   B 1 264 ? 13.771  -62.488 79.089 1   16.62 ? 245 THR   D OG1   1 
ATOM   3803 C CG2   . THR   B 1 264 ? 12.437  -63.435 80.884 1   19.4  ? 245 THR   D CG2   1 
ATOM   3804 N N     . MET   B 1 265 ? 16.125  -60.335 80.517 1   11.83 ? 246 MET   D N     1 
ATOM   3805 C CA    . MET   B 1 265 ? 17.434  -59.906 80.022 1   11.18 ? 246 MET   D CA    1 
ATOM   3806 C C     . MET   B 1 265 ? 18.153  -58.864 80.901 1   7.85  ? 246 MET   D C     1 
ATOM   3807 O O     . MET   B 1 265 ? 19.383  -58.799 80.863 1   3     ? 246 MET   D O     1 
ATOM   3808 C CB    . MET   B 1 265 ? 17.308  -59.441 78.58  1   11.72 ? 246 MET   D CB    1 
ATOM   3809 C CG    . MET   B 1 265 ? 16.996  -60.627 77.677 1   15.99 ? 246 MET   D CG    1 
ATOM   3810 S SD    . MET   B 1 265 ? 16.37   -60.179 76.073 1   20.91 ? 246 MET   D SD    1 
ATOM   3811 C CE    . MET   B 1 265 ? 17.918  -60.119 75.178 1   17.44 ? 246 MET   D CE    1 
ATOM   3812 N N     . ALA   B 1 266 ? 17.408  -58.095 81.7   1   3     ? 247 ALA   D N     1 
ATOM   3813 C CA    . ALA   B 1 266 ? 17.974  -57.066 82.602 1   3     ? 247 ALA   D CA    1 
ATOM   3814 C C     . ALA   B 1 266 ? 16.909  -56.652 83.616 1   5.33  ? 247 ALA   D C     1 
ATOM   3815 O O     . ALA   B 1 266 ? 15.767  -57.076 83.495 1   3     ? 247 ALA   D O     1 
ATOM   3816 C CB    . ALA   B 1 266 ? 18.408  -55.836 81.79  1   3     ? 247 ALA   D CB    1 
ATOM   3817 N N     . ASN   B 1 267 ? 17.291  -55.837 84.618 1   3     ? 248 ASN   D N     1 
ATOM   3818 C CA    . ASN   B 1 267 ? 16.384  -55.322 85.638 1   3     ? 248 ASN   D CA    1 
ATOM   3819 C C     . ASN   B 1 267 ? 16.386  -53.775 85.643 1   5.22  ? 248 ASN   D C     1 
ATOM   3820 O O     . ASN   B 1 267 ? 16.206  -53.167 86.706 1   3     ? 248 ASN   D O     1 
ATOM   3821 C CB    . ASN   B 1 267 ? 16.773  -55.877 87.03  1   5.23  ? 248 ASN   D CB    1 
ATOM   3822 C CG    . ASN   B 1 267 ? 18.138  -55.461 87.544 1   4.69  ? 248 ASN   D CG    1 
ATOM   3823 O OD1   . ASN   B 1 267 ? 18.99   -54.913 86.813 1   3     ? 248 ASN   D OD1   1 
ATOM   3824 N ND2   . ASN   B 1 267 ? 18.376  -55.737 88.821 1   6.69  ? 248 ASN   D ND2   1 
ATOM   3825 N N     . ASN   B 1 268 ? 16.619  -53.148 84.478 1   3     ? 249 ASN   D N     1 
ATOM   3826 C CA    . ASN   B 1 268 ? 16.723  -51.686 84.409 1   3     ? 249 ASN   D CA    1 
ATOM   3827 C C     . ASN   B 1 268 ? 15.405  -50.971 84.562 1   6.65  ? 249 ASN   D C     1 
ATOM   3828 O O     . ASN   B 1 268 ? 14.35   -51.552 84.269 1   3     ? 249 ASN   D O     1 
ATOM   3829 C CB    . ASN   B 1 268 ? 17.429  -51.219 83.124 1   3     ? 249 ASN   D CB    1 
ATOM   3830 C CG    . ASN   B 1 268 ? 16.631  -51.423 81.872 1   5.12  ? 249 ASN   D CG    1 
ATOM   3831 O OD1   . ASN   B 1 268 ? 16.155  -52.526 81.589 1   3     ? 249 ASN   D OD1   1 
ATOM   3832 N ND2   . ASN   B 1 268 ? 16.495  -50.365 81.075 1   3     ? 249 ASN   D ND2   1 
ATOM   3833 N N     . GLU   B 1 269 ? 15.472  -49.7   85.007 1   3     ? 250 GLU   D N     1 
ATOM   3834 C CA    . GLU   B 1 269 ? 14.301  -48.838 85.126 1   3.35  ? 250 GLU   D CA    1 
ATOM   3835 C C     . GLU   B 1 269 ? 14.504  -47.69  84.113 1   7.14  ? 250 GLU   D C     1 
ATOM   3836 O O     . GLU   B 1 269 ? 14.806  -46.548 84.489 1   6.73  ? 250 GLU   D O     1 
ATOM   3837 C CB    . GLU   B 1 269 ? 14.138  -48.301 86.55  1   5.63  ? 250 GLU   D CB    1 
ATOM   3838 C CG    . GLU   B 1 269 ? 13.755  -49.359 87.574 1   8.49  ? 250 GLU   D CG    1 
ATOM   3839 C CD    . GLU   B 1 269 ? 13.51   -48.8   88.965 1   47.58 ? 250 GLU   D CD    1 
ATOM   3840 O OE1   . GLU   B 1 269 ? 14.204  -49.241 89.911 1   60.71 ? 250 GLU   D OE1   1 
ATOM   3841 O OE2   . GLU   B 1 269 ? 12.636  -47.913 89.109 1   54.92 ? 250 GLU   D OE2   1 
ATOM   3842 N N     . GLY   B 1 270 ? 14.372  -48.027 82.843 1   3     ? 251 GLY   D N     1 
ATOM   3843 C CA    . GLY   B 1 270 ? 14.525  -47.081 81.751 1   3     ? 251 GLY   D CA    1 
ATOM   3844 C C     . GLY   B 1 270 ? 15.957  -46.867 81.299 1   5.81  ? 251 GLY   D C     1 
ATOM   3845 O O     . GLY   B 1 270 ? 16.873  -47.62  81.659 1   3     ? 251 GLY   D O     1 
ATOM   3846 N N     . LEU   B 1 271 ? 16.148  -45.824 80.49  1   3     ? 252 LEU   D N     1 
ATOM   3847 C CA    . LEU   B 1 271 ? 17.455  -45.468 79.931 1   3     ? 252 LEU   D CA    1 
ATOM   3848 C C     . LEU   B 1 271 ? 17.58   -43.952 79.905 1   5.11  ? 252 LEU   D C     1 
ATOM   3849 O O     . LEU   B 1 271 ? 16.571  -43.249 79.929 1   3     ? 252 LEU   D O     1 
ATOM   3850 C CB    . LEU   B 1 271 ? 17.562  -45.975 78.484 1   3.95  ? 252 LEU   D CB    1 
ATOM   3851 C CG    . LEU   B 1 271 ? 17.856  -47.48  78.274 1   6.09  ? 252 LEU   D CG    1 
ATOM   3852 C CD1   . LEU   B 1 271 ? 16.561  -48.256 78.013 1   5.64  ? 252 LEU   D CD1   1 
ATOM   3853 C CD2   . LEU   B 1 271 ? 18.818  -47.692 77.104 1   7.28  ? 252 LEU   D CD2   1 
ATOM   3854 N N     . PHE   B 1 272 ? 18.814  -43.446 79.827 1   3     ? 253 PHE   D N     1 
ATOM   3855 C CA    . PHE   B 1 272 ? 19.003  -42.017 79.695 1   3     ? 253 PHE   D CA    1 
ATOM   3856 C C     . PHE   B 1 272 ? 19.849  -41.755 78.46  1   5.46  ? 253 PHE   D C     1 
ATOM   3857 O O     . PHE   B 1 272 ? 20.587  -42.625 77.986 1   3     ? 253 PHE   D O     1 
ATOM   3858 C CB    . PHE   B 1 272 ? 19.674  -41.389 80.938 1   3     ? 253 PHE   D CB    1 
ATOM   3859 C CG    . PHE   B 1 272 ? 21.119  -41.796 81.114 1   3     ? 253 PHE   D CG    1 
ATOM   3860 C CD1   . PHE   B 1 272 ? 22.143  -41.084 80.498 1   3     ? 253 PHE   D CD1   1 
ATOM   3861 C CD2   . PHE   B 1 272 ? 21.457  -42.897 81.892 1   3     ? 253 PHE   D CD2   1 
ATOM   3862 C CE1   . PHE   B 1 272 ? 23.481  -41.483 80.635 1   3     ? 253 PHE   D CE1   1 
ATOM   3863 C CE2   . PHE   B 1 272 ? 22.801  -43.272 82.06  1   5.16  ? 253 PHE   D CE2   1 
ATOM   3864 C CZ    . PHE   B 1 272 ? 23.802  -42.569 81.42  1   3     ? 253 PHE   D CZ    1 
ATOM   3865 N N     . SER   B 1 273 ? 19.805  -40.509 78.018 1   3     ? 254 SER   D N     1 
ATOM   3866 C CA    . SER   B 1 273 ? 20.624  -40.04  76.921 1   3     ? 254 SER   D CA    1 
ATOM   3867 C C     . SER   B 1 273 ? 21.052  -38.629 77.327 1   5.23  ? 254 SER   D C     1 
ATOM   3868 O O     . SER   B 1 273 ? 20.233  -37.864 77.849 1   3     ? 254 SER   D O     1 
ATOM   3869 C CB    . SER   B 1 273 ? 19.807  -40.035 75.634 1   8.75  ? 254 SER   D CB    1 
ATOM   3870 O OG    . SER   B 1 273 ? 20.511  -39.354 74.616 1   8.93  ? 254 SER   D OG    1 
ATOM   3871 N N     . LEU   B 1 274 ? 22.348  -38.313 77.17  1   3     ? 255 LEU   D N     1 
ATOM   3872 C CA    . LEU   B 1 274 ? 22.8    -36.973 77.514 1   3     ? 255 LEU   D CA    1 
ATOM   3873 C C     . LEU   B 1 274 ? 23.815  -36.454 76.528 1   6.08  ? 255 LEU   D C     1 
ATOM   3874 O O     . LEU   B 1 274 ? 24.556  -37.242 75.929 1   3     ? 255 LEU   D O     1 
ATOM   3875 C CB    . LEU   B 1 274 ? 23.347  -36.878 78.953 1   3     ? 255 LEU   D CB    1 
ATOM   3876 C CG    . LEU   B 1 274 ? 24.674  -37.572 79.282 1   5.39  ? 255 LEU   D CG    1 
ATOM   3877 C CD1   . LEU   B 1 274 ? 25.881  -36.654 79.035 1   4.77  ? 255 LEU   D CD1   1 
ATOM   3878 C CD2   . LEU   B 1 274 ? 24.707  -37.998 80.738 1   6.91  ? 255 LEU   D CD2   1 
ATOM   3879 N N     . VAL   B 1 275 ? 23.873  -35.131 76.421 1   3     ? 256 VAL   D N     1 
ATOM   3880 C CA    . VAL   B 1 275 ? 24.868  -34.426 75.621 1   3     ? 256 VAL   D CA    1 
ATOM   3881 C C     . VAL   B 1 275 ? 25.487  -33.427 76.583 1   5.23  ? 256 VAL   D C     1 
ATOM   3882 O O     . VAL   B 1 275 ? 24.765  -32.644 77.204 1   3     ? 256 VAL   D O     1 
ATOM   3883 C CB    . VAL   B 1 275 ? 24.267  -33.741 74.362 1   3.63  ? 256 VAL   D CB    1 
ATOM   3884 C CG1   . VAL   B 1 275 ? 25.325  -32.936 73.617 1   3     ? 256 VAL   D CG1   1 
ATOM   3885 C CG2   . VAL   B 1 275 ? 23.64   -34.777 73.435 1   3.02  ? 256 VAL   D CG2   1 
ATOM   3886 N N     . ALA   B 1 276 ? 26.815  -33.477 76.726 1   3     ? 257 ALA   D N     1 
ATOM   3887 C CA    . ALA   B 1 276 ? 27.544  -32.569 77.605 1   3     ? 257 ALA   D CA    1 
ATOM   3888 C C     . ALA   B 1 276 ? 28.756  -32.023 76.86  1   4.61  ? 257 ALA   D C     1 
ATOM   3889 O O     . ALA   B 1 276 ? 29.152  -32.601 75.846 1   3     ? 257 ALA   D O     1 
ATOM   3890 C CB    . ALA   B 1 276 ? 27.991  -33.31  78.851 1   3     ? 257 ALA   D CB    1 
ATOM   3891 N N     . ARG   B 1 277 ? 29.335  -30.925 77.351 1   3     ? 258 ARG   D N     1 
ATOM   3892 C CA    . ARG   B 1 277 ? 30.542  -30.361 76.739 1   3     ? 258 ARG   D CA    1 
ATOM   3893 C C     . ARG   B 1 277 ? 31.65   -30.308 77.778 1   4.91  ? 258 ARG   D C     1 
ATOM   3894 O O     . ARG   B 1 277 ? 31.397  -29.964 78.941 1   3     ? 258 ARG   D O     1 
ATOM   3895 C CB    . ARG   B 1 277 ? 30.29   -28.955 76.153 1   5.64  ? 258 ARG   D CB    1 
ATOM   3896 C CG    . ARG   B 1 277 ? 29.3    -28.947 74.992 1   8.86  ? 258 ARG   D CG    1 
ATOM   3897 C CD    . ARG   B 1 277 ? 29.239  -27.597 74.295 1   21.59 ? 258 ARG   D CD    1 
ATOM   3898 N NE    . ARG   B 1 277 ? 30.446  -27.326 73.512 1   28.81 ? 258 ARG   D NE    1 
ATOM   3899 C CZ    . ARG   B 1 277 ? 30.561  -26.354 72.611 1   46.83 ? 258 ARG   D CZ    1 
ATOM   3900 N NH1   . ARG   B 1 277 ? 29.535  -25.551 72.355 1   39.22 ? 258 ARG   D NH1   1 
ATOM   3901 N NH2   . ARG   B 1 277 ? 31.699  -26.182 71.953 1   34.73 ? 258 ARG   D NH2   1 
ATOM   3902 N N     . LYS   B 1 278 ? 32.883  -30.628 77.37  1   3     ? 259 LYS   D N     1 
ATOM   3903 C CA    . LYS   B 1 278 ? 34.024  -30.6   78.282 1   3     ? 259 LYS   D CA    1 
ATOM   3904 C C     . LYS   B 1 278 ? 34.393  -29.141 78.646 1   6.45  ? 259 LYS   D C     1 
ATOM   3905 O O     . LYS   B 1 278 ? 34.402  -28.284 77.762 1   4.89  ? 259 LYS   D O     1 
ATOM   3906 C CB    . LYS   B 1 278 ? 35.21   -31.324 77.629 1   3.75  ? 259 LYS   D CB    1 
ATOM   3907 C CG    . LYS   B 1 278 ? 36.425  -31.483 78.538 1   6.67  ? 259 LYS   D CG    1 
ATOM   3908 C CD    . LYS   B 1 278 ? 37.627  -31.891 77.721 1   3     ? 259 LYS   D CD    1 
ATOM   3909 C CE    . LYS   B 1 278 ? 38.873  -31.955 78.555 1   10.08 ? 259 LYS   D CE    1 
ATOM   3910 N NZ    . LYS   B 1 278 ? 40.02   -32.487 77.771 1   4.72  ? 259 LYS   D NZ    1 
ATOM   3911 N N     . LEU   B 1 279 ? 34.658  -28.868 79.942 1   3     ? 260 LEU   D N     1 
ATOM   3912 C CA    . LEU   B 1 279 ? 35.077  -27.539 80.397 1   29.03 ? 260 LEU   D CA    1 
ATOM   3913 C C     . LEU   B 1 279 ? 36.567  -27.299 80.17  1   71.02 ? 260 LEU   D C     1 
ATOM   3914 O O     . LEU   B 1 279 ? 37.361  -28.241 80.164 1   44.01 ? 260 LEU   D O     1 
ATOM   3915 C CB    . LEU   B 1 279 ? 34.728  -27.322 81.87  1   28.58 ? 260 LEU   D CB    1 
ATOM   3916 C CG    . LEU   B 1 279 ? 33.253  -27.046 82.147 1   28.81 ? 260 LEU   D CG    1 
ATOM   3917 C CD1   . LEU   B 1 279 ? 32.993  -26.942 83.627 1   28.67 ? 260 LEU   D CD1   1 
ATOM   3918 C CD2   . LEU   B 1 279 ? 32.798  -25.761 81.456 1   30.93 ? 260 LEU   D CD2   1 
HETATM 3919 C C1    . A1IPM C 2 .   ? 9.051   -17.227 74.714 1   3     ? 301 A1IPM B C1    1 
HETATM 3920 C C3    . A1IPM C 2 .   ? 7.963   -17.482 76.87  1   3     ? 301 A1IPM B C3    1 
HETATM 3921 C C7    . A1IPM C 2 .   ? 8.076   -17.924 79.628 1   4.29  ? 301 A1IPM B C7    1 
HETATM 3922 C C8    . A1IPM C 2 .   ? 6.854   -17.798 78.953 1   3     ? 301 A1IPM B C8    1 
HETATM 3923 C C10   . A1IPM C 2 .   ? 5.553   -17.439 76.958 1   3     ? 301 A1IPM B C10   1 
HETATM 3924 C C11   . A1IPM C 2 .   ? 8.039   -18.164 81.099 1   4.76  ? 301 A1IPM B C11   1 
HETATM 3925 N N2    . A1IPM C 2 .   ? 7.815   -17.273 75.475 1   3     ? 301 A1IPM B N2    1 
HETATM 3926 C C4    . A1IPM C 2 .   ? 9.201   -17.595 77.512 1   3     ? 301 A1IPM B C4    1 
HETATM 3927 C C5    . A1IPM C 2 .   ? 9.274   -17.8   78.895 1   3.19  ? 301 A1IPM B C5    1 
HETATM 3928 C C6    . A1IPM C 2 .   ? 10.639  -17.912 79.484 1   3     ? 301 A1IPM B C6    1 
HETATM 3929 N N9    . A1IPM C 2 .   ? 6.836   -17.564 77.622 1   3     ? 301 A1IPM B N9    1 
HETATM 3930 O O12   . A1IPM C 2 .   ? 8.734   -17.504 81.858 1   3     ? 301 A1IPM B O12   1 
HETATM 3931 N N13   . A1IPM C 2 .   ? 7.143   -19.128 81.507 1   3     ? 301 A1IPM B N13   1 
HETATM 3932 N N     . SAH   D 3 .   ? 2.397   -21.208 72.403 1   3     ? 302 SAH   B N     1 
HETATM 3933 C CA    . SAH   D 3 .   ? 3.087   -19.957 72.054 1   3.6   ? 302 SAH   B CA    1 
HETATM 3934 C CB    . SAH   D 3 .   ? 2.697   -18.719 72.905 1   3     ? 302 SAH   B CB    1 
HETATM 3935 C CG    . SAH   D 3 .   ? 3.034   -18.889 74.381 1   3.86  ? 302 SAH   B CG    1 
HETATM 3936 S SD    . SAH   D 3 .   ? 2.784   -17.236 75.11  1   3     ? 302 SAH   B SD    1 
HETATM 3937 C C     . SAH   D 3 .   ? 4.639   -20.233 72.052 1   3.3   ? 302 SAH   B C     1 
HETATM 3938 O O     . SAH   D 3 .   ? 5.107   -21.348 72.191 1   3     ? 302 SAH   B O     1 
HETATM 3939 O OXT   . SAH   D 3 .   ? 5.371   -19.132 71.863 1   3     ? 302 SAH   B OXT   1 
HETATM 3940 C "C5'" . SAH   D 3 .   ? 1.696   -17.569 76.523 1   3.2   ? 302 SAH   B "C5'" 1 
HETATM 3941 C "C4'" . SAH   D 3 .   ? 0.263   -17.694 76.047 1   3     ? 302 SAH   B "C4'" 1 
HETATM 3942 O "O4'" . SAH   D 3 .   ? -0.596  -18.197 77.097 1   3     ? 302 SAH   B "O4'" 1 
HETATM 3943 C "C3'" . SAH   D 3 .   ? -0.378  -16.388 75.547 1   3     ? 302 SAH   B "C3'" 1 
HETATM 3944 O "O3'" . SAH   D 3 .   ? -0.854  -16.52  74.213 1   3     ? 302 SAH   B "O3'" 1 
HETATM 3945 C "C2'" . SAH   D 3 .   ? -1.577  -16.19  76.483 1   3.31  ? 302 SAH   B "C2'" 1 
HETATM 3946 O "O2'" . SAH   D 3 .   ? -2.677  -15.562 75.833 1   3     ? 302 SAH   B "O2'" 1 
HETATM 3947 C "C1'" . SAH   D 3 .   ? -1.873  -17.631 76.888 1   3     ? 302 SAH   B "C1'" 1 
HETATM 3948 N N9    . SAH   D 3 .   ? -2.67   -17.788 78.103 1   3     ? 302 SAH   B N9    1 
HETATM 3949 C C8    . SAH   D 3 .   ? -2.532  -17.111 79.288 1   3     ? 302 SAH   B C8    1 
HETATM 3950 N N7    . SAH   D 3 .   ? -3.384  -17.476 80.215 1   3     ? 302 SAH   B N7    1 
HETATM 3951 C C5    . SAH   D 3 .   ? -4.139  -18.464 79.598 1   3     ? 302 SAH   B C5    1 
HETATM 3952 C C6    . SAH   D 3 .   ? -5.214  -19.263 80.047 1   3     ? 302 SAH   B C6    1 
HETATM 3953 N N6    . SAH   D 3 .   ? -5.73   -19.197 81.284 1   3     ? 302 SAH   B N6    1 
HETATM 3954 N N1    . SAH   D 3 .   ? -5.729  -20.163 79.18  1   3     ? 302 SAH   B N1    1 
HETATM 3955 C C2    . SAH   D 3 .   ? -5.218  -20.241 77.946 1   3     ? 302 SAH   B C2    1 
HETATM 3956 N N3    . SAH   D 3 .   ? -4.213  -19.542 77.41  1   3     ? 302 SAH   B N3    1 
HETATM 3957 C C4    . SAH   D 3 .   ? -3.71   -18.666 78.295 1   3.24  ? 302 SAH   B C4    1 
HETATM 3958 C C1    . A1IPM E 2 .   ? 21.999  -54.207 75.4   1   3.49  ? 301 A1IPM D C1    1 
HETATM 3959 C C3    . A1IPM E 2 .   ? 23.16   -53.725 77.469 1   3     ? 301 A1IPM D C3    1 
HETATM 3960 C C7    . A1IPM E 2 .   ? 23.122  -53.1   80.196 1   3     ? 301 A1IPM D C7    1 
HETATM 3961 C C8    . A1IPM E 2 .   ? 24.319  -53.205 79.484 1   3     ? 301 A1IPM D C8    1 
HETATM 3962 C C10   . A1IPM E 2 .   ? 25.583  -53.644 77.477 1   3     ? 301 A1IPM D C10   1 
HETATM 3963 C C11   . A1IPM E 2 .   ? 23.191  -52.779 81.648 1   4.31  ? 301 A1IPM D C11   1 
HETATM 3964 N N2    . A1IPM E 2 .   ? 23.275  -54.042 76.09  1   3     ? 301 A1IPM D N2    1 
HETATM 3965 C C4    . A1IPM E 2 .   ? 21.941  -53.617 78.148 1   3     ? 301 A1IPM D C4    1 
HETATM 3966 C C5    . A1IPM E 2 .   ? 21.909  -53.315 79.52  1   3     ? 301 A1IPM D C5    1 
HETATM 3967 C C6    . A1IPM E 2 .   ? 20.567  -53.2   80.173 1   3     ? 301 A1IPM D C6    1 
HETATM 3968 N N9    . A1IPM E 2 .   ? 24.306  -53.522 78.171 1   3     ? 301 A1IPM D N9    1 
HETATM 3969 O O12   . A1IPM E 2 .   ? 22.528  -53.421 82.458 1   3     ? 301 A1IPM D O12   1 
HETATM 3970 N N13   . A1IPM E 2 .   ? 24.084  -51.781 81.975 1   3     ? 301 A1IPM D N13   1 
HETATM 3971 N N     . SAH   F 3 .   ? 28.308  -49.904 72.57  1   3     ? 302 SAH   D N     1 
HETATM 3972 C CA    . SAH   F 3 .   ? 27.718  -51.224 72.298 1   3.42  ? 302 SAH   D CA    1 
HETATM 3973 C CB    . SAH   F 3 .   ? 28.232  -52.388 73.211 1   3     ? 302 SAH   D CB    1 
HETATM 3974 C CG    . SAH   F 3 .   ? 27.907  -52.208 74.692 1   3     ? 302 SAH   D CG    1 
HETATM 3975 S SD    . SAH   F 3 .   ? 28.304  -53.803 75.488 1   3     ? 302 SAH   D SD    1 
HETATM 3976 C C     . SAH   F 3 .   ? 26.151  -51.024 72.341 1   3.66  ? 302 SAH   D C     1 
HETATM 3977 O O     . SAH   F 3 .   ? 25.634  -49.913 72.322 1   3     ? 302 SAH   D O     1 
HETATM 3978 O OXT   . SAH   F 3 .   ? 25.473  -52.16  72.369 1   3     ? 302 SAH   D OXT   1 
HETATM 3979 C "C5'" . SAH   F 3 .   ? 29.435  -53.308 76.817 1   3     ? 302 SAH   D "C5'" 1 
HETATM 3980 C "C4'" . SAH   F 3 .   ? 30.84   -53.173 76.265 1   3     ? 302 SAH   D "C4'" 1 
HETATM 3981 O "O4'" . SAH   F 3 .   ? 31.747  -52.579 77.218 1   3     ? 302 SAH   D "O4'" 1 
HETATM 3982 C "C3'" . SAH   F 3 .   ? 31.525  -54.446 75.74  1   3.07  ? 302 SAH   D "C3'" 1 
HETATM 3983 O "O3'" . SAH   F 3 .   ? 31.872  -54.293 74.368 1   3     ? 302 SAH   D "O3'" 1 
HETATM 3984 C "C2'" . SAH   F 3 .   ? 32.793  -54.556 76.603 1   3     ? 302 SAH   D "C2'" 1 
HETATM 3985 O "O2'" . SAH   F 3 .   ? 33.9    -55.161 75.938 1   3     ? 302 SAH   D "O2'" 1 
HETATM 3986 C "C1'" . SAH   F 3 .   ? 33.037  -53.089 76.952 1   3     ? 302 SAH   D "C1'" 1 
HETATM 3987 N N9    . SAH   F 3 .   ? 33.886  -52.862 78.123 1   3     ? 302 SAH   D N9    1 
HETATM 3988 C C8    . SAH   F 3 .   ? 33.795  -53.482 79.345 1   3     ? 302 SAH   D C8    1 
HETATM 3989 N N7    . SAH   F 3 .   ? 34.674  -53.066 80.223 1   3     ? 302 SAH   D N7    1 
HETATM 3990 C C5    . SAH   F 3 .   ? 35.405  -52.109 79.53  1   3     ? 302 SAH   D C5    1 
HETATM 3991 C C6    . SAH   F 3 .   ? 36.475  -51.268 79.909 1   3     ? 302 SAH   D C6    1 
HETATM 3992 N N6    . SAH   F 3 .   ? 37.071  -51.311 81.105 1   3     ? 302 SAH   D N6    1 
HETATM 3993 N N1    . SAH   F 3 .   ? 36.929  -50.377 78.995 1   3     ? 302 SAH   D N1    1 
HETATM 3994 C C2    . SAH   F 3 .   ? 36.371  -50.356 77.78  1   3.32  ? 302 SAH   D C2    1 
HETATM 3995 N N3    . SAH   F 3 .   ? 35.378  -51.113 77.303 1   3     ? 302 SAH   D N3    1 
HETATM 3996 C C4    . SAH   F 3 .   ? 34.927  -51.969 78.236 1   3     ? 302 SAH   D C4    1 
HETATM 3997 O O     . HOH   G 4 .   ? -4.745  -17.833 83.986 1   5.24  ? 401 HOH   B O     1 
HETATM 3998 O O     . HOH   G 4 .   ? 1.473   -14.799 83.331 1   3     ? 402 HOH   B O     1 
HETATM 3999 O O     . HOH   G 4 .   ? -12.66  -18.048 81.105 1   3     ? 403 HOH   B O     1 
HETATM 4000 O O     . HOH   G 4 .   ? -14.091 -21.948 72.991 1   3.3   ? 404 HOH   B O     1 
HETATM 4001 O O     . HOH   G 4 .   ? -3.989  -21.899 84.218 1   70.23 ? 405 HOH   B O     1 
HETATM 4002 O O     . HOH   G 4 .   ? -2.931  -32.157 57.898 1   23.31 ? 406 HOH   B O     1 
HETATM 4003 O O     . HOH   G 4 .   ? -4.844  -37.094 92.114 1   13.99 ? 407 HOH   B O     1 
HETATM 4004 O O     . HOH   G 4 .   ? 15.126  -10.578 70.688 1   17.26 ? 408 HOH   B O     1 
HETATM 4005 O O     . HOH   G 4 .   ? -2.032  -8.04   85.925 1   3     ? 409 HOH   B O     1 
HETATM 4006 O O     . HOH   G 4 .   ? 1.051   -13.287 61.799 1   13.87 ? 410 HOH   B O     1 
HETATM 4007 O O     . HOH   G 4 .   ? -12.593 -31.146 83.419 1   16.65 ? 411 HOH   B O     1 
HETATM 4008 O O     . HOH   G 4 .   ? -8.587  -35.235 82.848 1   11.31 ? 412 HOH   B O     1 
HETATM 4009 O O     . HOH   G 4 .   ? 9.949   -3.148  82.572 1   12.34 ? 413 HOH   B O     1 
HETATM 4010 O O     . HOH   G 4 .   ? 12.559  -18.374 70.923 1   3     ? 414 HOH   B O     1 
HETATM 4011 O O     . HOH   G 4 .   ? 10.509  -0.081  82.202 1   22.33 ? 415 HOH   B O     1 
HETATM 4012 O O     . HOH   G 4 .   ? -3.504  -9.702  73.537 1   14.88 ? 416 HOH   B O     1 
HETATM 4013 O O     . HOH   G 4 .   ? 4.914   -29.578 65.365 1   3     ? 417 HOH   B O     1 
HETATM 4014 O O     . HOH   G 4 .   ? -4.759  -29.285 92.269 1   12.49 ? 418 HOH   B O     1 
HETATM 4015 O O     . HOH   G 4 .   ? 9.507   -29.214 63.781 1   8.61  ? 419 HOH   B O     1 
HETATM 4016 O O     . HOH   G 4 .   ? 15.951  -26.086 86.02  1   12.65 ? 420 HOH   B O     1 
HETATM 4017 O O     . HOH   G 4 .   ? 0.963   -24.028 72.532 1   6.12  ? 421 HOH   B O     1 
HETATM 4018 O O     . HOH   G 4 .   ? -13.937 -35.428 78.998 1   21.75 ? 422 HOH   B O     1 
HETATM 4019 O O     . HOH   G 4 .   ? 8.236   -32.362 54.766 1   24.95 ? 423 HOH   B O     1 
HETATM 4020 O O     . HOH   G 4 .   ? 8.59    -35.923 90.674 1   10.08 ? 424 HOH   B O     1 
HETATM 4021 O O     . HOH   G 4 .   ? 1.504   -8.719  83.907 1   3     ? 425 HOH   B O     1 
HETATM 4022 O O     . HOH   G 4 .   ? 3.626   -31.165 91.501 1   3.75  ? 426 HOH   B O     1 
HETATM 4023 O O     . HOH   G 4 .   ? 5.096   -44.445 81.522 1   43.24 ? 427 HOH   B O     1 
HETATM 4024 O O     . HOH   G 4 .   ? -5.218  -33.748 93.774 1   26.58 ? 428 HOH   B O     1 
HETATM 4025 O O     . HOH   G 4 .   ? -0.747  -41.148 86.894 1   3     ? 429 HOH   B O     1 
HETATM 4026 O O     . HOH   G 4 .   ? 19.943  -23.744 83.09  1   32    ? 430 HOH   B O     1 
HETATM 4027 O O     . HOH   G 4 .   ? 22.429  -23.859 73.108 1   20.59 ? 431 HOH   B O     1 
HETATM 4028 O O     . HOH   G 4 .   ? 14.903  -8.588  85.813 1   30.61 ? 432 HOH   B O     1 
HETATM 4029 O O     . HOH   G 4 .   ? 17.955  -25.623 87.815 1   17.46 ? 433 HOH   B O     1 
HETATM 4030 O O     . HOH   G 4 .   ? -5.899  -7.32   65.199 1   42.72 ? 434 HOH   B O     1 
HETATM 4031 O O     . HOH   G 4 .   ? 17.24   -12.28  71.073 1   19.73 ? 435 HOH   B O     1 
HETATM 4032 O O     . HOH   G 4 .   ? -10.227 -37.741 67.565 1   16.94 ? 436 HOH   B O     1 
HETATM 4033 O O     . HOH   G 4 .   ? -11.377 -27.427 86.992 1   16.78 ? 437 HOH   B O     1 
HETATM 4034 O O     . HOH   G 4 .   ? 13.536  -30.029 76.216 1   8.77  ? 438 HOH   B O     1 
HETATM 4035 O O     . HOH   G 4 .   ? -13.845 -30.113 78.504 1   3     ? 439 HOH   B O     1 
HETATM 4036 O O     . HOH   G 4 .   ? 1.935   -34.687 93.414 1   19.98 ? 440 HOH   B O     1 
HETATM 4037 O O     . HOH   G 4 .   ? 0.676   -31.225 91.841 1   16.24 ? 441 HOH   B O     1 
HETATM 4038 O O     . HOH   G 4 .   ? 3.214   -7.195  75.369 1   3     ? 442 HOH   B O     1 
HETATM 4039 O O     . HOH   G 4 .   ? -4.291  -45.079 78.743 1   28.19 ? 443 HOH   B O     1 
HETATM 4040 O O     . HOH   G 4 .   ? 8.982   -22.4   85.481 1   3     ? 444 HOH   B O     1 
HETATM 4041 O O     . HOH   G 4 .   ? 13.153  -27.847 50.865 1   32.05 ? 445 HOH   B O     1 
HETATM 4042 O O     . HOH   G 4 .   ? 23.708  -24.626 78.164 1   24.07 ? 446 HOH   B O     1 
HETATM 4043 O O     . HOH   G 4 .   ? -14.277 -24.237 85.662 1   16.94 ? 447 HOH   B O     1 
HETATM 4044 O O     . HOH   G 4 .   ? 19.632  -25.549 69.899 1   18.49 ? 448 HOH   B O     1 
HETATM 4045 O O     . HOH   G 4 .   ? -7.291  -41.946 65.923 1   35.08 ? 449 HOH   B O     1 
HETATM 4046 O O     . HOH   G 4 .   ? -15.323 -28.618 74.773 1   25.12 ? 450 HOH   B O     1 
HETATM 4047 O O     . HOH   G 4 .   ? -12.347 -37.273 76.393 1   31.92 ? 451 HOH   B O     1 
HETATM 4048 O O     . HOH   G 4 .   ? 21.046  -14.262 73.283 1   12.67 ? 452 HOH   B O     1 
HETATM 4049 O O     . HOH   G 4 .   ? 15.226  -36.651 50.82  1   45.35 ? 453 HOH   B O     1 
HETATM 4050 O O     . HOH   G 4 .   ? 1.873   -3.726  77.169 1   14.96 ? 454 HOH   B O     1 
HETATM 4051 O O     . HOH   G 4 .   ? 15.3    -35.712 81.681 1   14.62 ? 455 HOH   B O     1 
HETATM 4052 O O     . HOH   G 4 .   ? 5.027   -20.404 80.082 1   3     ? 456 HOH   B O     1 
HETATM 4053 O O     . HOH   G 4 .   ? 17.818  -26.762 83.139 1   30.72 ? 457 HOH   B O     1 
HETATM 4054 O O     . HOH   G 4 .   ? 4.56    -41.737 84.574 1   6.93  ? 458 HOH   B O     1 
HETATM 4055 O O     . HOH   G 4 .   ? -2.751  -30.478 93.641 1   21.41 ? 459 HOH   B O     1 
HETATM 4056 O O     . HOH   G 4 .   ? -10.631 -31.274 85.311 1   22.4  ? 460 HOH   B O     1 
HETATM 4057 O O     . HOH   G 4 .   ? -9.683  -22.931 91.523 1   26.08 ? 461 HOH   B O     1 
HETATM 4058 O O     . HOH   G 4 .   ? 9.152   -44.661 77.026 1   23.46 ? 462 HOH   B O     1 
HETATM 4059 O O     . HOH   G 4 .   ? -19.375 -28.212 83.936 1   24.49 ? 463 HOH   B O     1 
HETATM 4060 O O     . HOH   G 4 .   ? 5.44    -16.14  89.963 1   8.16  ? 464 HOH   B O     1 
HETATM 4061 O O     . HOH   G 4 .   ? -6.618  -39.486 83.733 1   3     ? 465 HOH   B O     1 
HETATM 4062 O O     . HOH   G 4 .   ? -6.594  -14.07  86.533 1   30.53 ? 466 HOH   B O     1 
HETATM 4063 O O     . HOH   G 4 .   ? -1.502  -15.243 84.188 1   3     ? 467 HOH   B O     1 
HETATM 4064 O O     . HOH   G 4 .   ? -3.866  -8.816  66.701 1   20.36 ? 468 HOH   B O     1 
HETATM 4065 O O     . HOH   G 4 .   ? -17.058 -27.233 67.051 1   29.78 ? 469 HOH   B O     1 
HETATM 4066 O O     . HOH   G 4 .   ? 18.443  -15.543 69.269 1   18.11 ? 470 HOH   B O     1 
HETATM 4067 O O     . HOH   G 4 .   ? -8.127  -23.914 87.842 1   34.63 ? 471 HOH   B O     1 
HETATM 4068 O O     . HOH   G 4 .   ? 7.484   -4.448  67.911 1   28.25 ? 472 HOH   B O     1 
HETATM 4069 O O     . HOH   G 4 .   ? 20.222  -16.522 71.976 1   4.81  ? 473 HOH   B O     1 
HETATM 4070 O O     . HOH   G 4 .   ? 21.68   -20.486 79.132 1   19.98 ? 474 HOH   B O     1 
HETATM 4071 O O     . HOH   G 4 .   ? 10.704  -19.731 72.34  1   3     ? 475 HOH   B O     1 
HETATM 4072 O O     . HOH   G 4 .   ? 15.189  -19.758 89.026 1   40.43 ? 476 HOH   B O     1 
HETATM 4073 O O     . HOH   G 4 .   ? 4.451   -45.532 79.131 1   26.75 ? 477 HOH   B O     1 
HETATM 4074 O O     . HOH   G 4 .   ? -11.192 -40.35  79.071 1   22.96 ? 478 HOH   B O     1 
HETATM 4075 O O     . HOH   G 4 .   ? 11.398  -8.56   75.539 1   20.93 ? 479 HOH   B O     1 
HETATM 4076 O O     . HOH   G 4 .   ? 1.856   -15.576 63.168 1   3.13  ? 480 HOH   B O     1 
HETATM 4077 O O     . HOH   G 4 .   ? 15.18   -35.513 88.634 1   27.64 ? 481 HOH   B O     1 
HETATM 4078 O O     . HOH   G 4 .   ? -15.8   -31.049 73.537 1   23.66 ? 482 HOH   B O     1 
HETATM 4079 O O     . HOH   G 4 .   ? 10.639  -31.565 53.712 1   25.83 ? 483 HOH   B O     1 
HETATM 4080 O O     . HOH   G 4 .   ? 6.993   -28.009 64.093 1   10.09 ? 484 HOH   B O     1 
HETATM 4081 O O     . HOH   G 4 .   ? -3.581  -15.904 82.552 1   3.38  ? 485 HOH   B O     1 
HETATM 4082 O O     . HOH   G 4 .   ? 12.926  -6.752  77.818 1   26.28 ? 486 HOH   B O     1 
HETATM 4083 O O     . HOH   G 4 .   ? 19.907  -30.782 80.987 1   8.69  ? 487 HOH   B O     1 
HETATM 4084 O O     . HOH   G 4 .   ? 8.417   -3.017  73.136 1   28.2  ? 488 HOH   B O     1 
HETATM 4085 O O     . HOH   G 4 .   ? 8.813   -39.479 85.73  1   41.81 ? 489 HOH   B O     1 
HETATM 4086 O O     . HOH   G 4 .   ? 14.457  -28.586 87.266 1   3     ? 490 HOH   B O     1 
HETATM 4087 O O     . HOH   G 4 .   ? -14.709 -31.133 81.126 1   28.42 ? 491 HOH   B O     1 
HETATM 4088 O O     . HOH   G 4 .   ? 3.62    -14.641 56.113 1   22.08 ? 492 HOH   B O     1 
HETATM 4089 O O     . HOH   G 4 .   ? -3.461  -30.477 55.786 1   20.14 ? 493 HOH   B O     1 
HETATM 4090 O O     . HOH   G 4 .   ? 18.429  -17.189 83.363 1   8.38  ? 494 HOH   B O     1 
HETATM 4091 O O     . HOH   G 4 .   ? -7.549  -9.844  73.101 1   3     ? 495 HOH   B O     1 
HETATM 4092 O O     . HOH   G 4 .   ? -11.785 -32.426 72.693 1   6.73  ? 496 HOH   B O     1 
HETATM 4093 O O     . HOH   G 4 .   ? 7.658   -2.149  75.633 1   14.82 ? 497 HOH   B O     1 
HETATM 4094 O O     . HOH   G 4 .   ? 14.418  -16.441 67.186 1   14.72 ? 498 HOH   B O     1 
HETATM 4095 O O     . HOH   G 4 .   ? -5.63   -44.441 72.813 1   40.81 ? 499 HOH   B O     1 
HETATM 4096 O O     . HOH   G 4 .   ? -13.867 -27.695 76.992 1   3     ? 500 HOH   B O     1 
HETATM 4097 O O     . HOH   G 4 .   ? -8.056  -36.425 86.585 1   22.93 ? 501 HOH   B O     1 
HETATM 4098 O O     . HOH   G 4 .   ? 19.943  -17.929 70.019 1   3     ? 502 HOH   B O     1 
HETATM 4099 O O     . HOH   G 4 .   ? 1.075   -21.964 50.247 1   20.81 ? 503 HOH   B O     1 
HETATM 4100 O O     . HOH   G 4 .   ? -7.112  -11.429 61.5   1   25.29 ? 504 HOH   B O     1 
HETATM 4101 O O     . HOH   G 4 .   ? -12.606 -37.788 79.932 1   19.06 ? 505 HOH   B O     1 
HETATM 4102 O O     . HOH   G 4 .   ? -1.013  -4.733  73.803 1   38.51 ? 506 HOH   B O     1 
HETATM 4103 O O     . HOH   G 4 .   ? 5.033   -5.162  74.775 1   12.63 ? 507 HOH   B O     1 
HETATM 4104 O O     . HOH   G 4 .   ? 2.591   -23.125 94.349 1   14.89 ? 508 HOH   B O     1 
HETATM 4105 O O     . HOH   G 4 .   ? 10.711  -16.149 61.563 1   34.92 ? 509 HOH   B O     1 
HETATM 4106 O O     . HOH   G 4 .   ? -5.845  -31.518 91.152 1   31.41 ? 510 HOH   B O     1 
HETATM 4107 O O     . HOH   G 4 .   ? -13.548 -21.791 79.514 1   26.12 ? 511 HOH   B O     1 
HETATM 4108 O O     . HOH   G 4 .   ? 15.681  -26.358 48.888 1   35.28 ? 512 HOH   B O     1 
HETATM 4109 O O     . HOH   G 4 .   ? -10.63  -36.655 81.787 1   12.56 ? 513 HOH   B O     1 
HETATM 4110 O O     . HOH   G 4 .   ? -6.411  -36.792 82.818 1   8.49  ? 514 HOH   B O     1 
HETATM 4111 O O     . HOH   G 4 .   ? -13.38  -35.126 75.039 1   24.2  ? 515 HOH   B O     1 
HETATM 4112 O O     . HOH   G 4 .   ? 9.36    -26.699 91.82  1   6.4   ? 516 HOH   B O     1 
HETATM 4113 O O     . HOH   G 4 .   ? 5.365   -4.315  83.167 1   3     ? 517 HOH   B O     1 
HETATM 4114 O O     . HOH   G 4 .   ? 17.426  -12.27  84.079 1   27.95 ? 518 HOH   B O     1 
HETATM 4115 O O     . HOH   G 4 .   ? 4.627   -13.298 89.802 1   17.06 ? 519 HOH   B O     1 
HETATM 4116 O O     . HOH   G 4 .   ? -0.937  -18.669 94.727 1   32.62 ? 520 HOH   B O     1 
HETATM 4117 O O     . HOH   G 4 .   ? 13.149  -38.789 86.375 1   25.2  ? 521 HOH   B O     1 
HETATM 4118 O O     . HOH   G 4 .   ? 19.416  -17.595 74.222 1   9.55  ? 522 HOH   B O     1 
HETATM 4119 O O     . HOH   G 4 .   ? 2.817   -25.154 78.186 1   3     ? 523 HOH   B O     1 
HETATM 4120 O O     . HOH   G 4 .   ? -2.375  -12.358 92.071 1   34.03 ? 524 HOH   B O     1 
HETATM 4121 O O     . HOH   G 4 .   ? 10.718  -29.347 91.472 1   4.09  ? 525 HOH   B O     1 
HETATM 4122 O O     . HOH   G 4 .   ? 4.783   -37.24  59.75  1   31.53 ? 526 HOH   B O     1 
HETATM 4123 O O     . HOH   G 4 .   ? 17.092  -34.71  57.461 1   32.35 ? 527 HOH   B O     1 
HETATM 4124 O O     . HOH   G 4 .   ? 6.509   -42.531 62.541 1   30.41 ? 528 HOH   B O     1 
HETATM 4125 O O     . HOH   G 4 .   ? 22.653  -23.408 82.338 1   35.9  ? 529 HOH   B O     1 
HETATM 4126 O O     . HOH   G 4 .   ? -13.231 -20.506 77.137 1   21.81 ? 530 HOH   B O     1 
HETATM 4127 O O     . HOH   G 4 .   ? -10.189 -20.423 87.409 1   47.24 ? 531 HOH   B O     1 
HETATM 4128 O O     . HOH   G 4 .   ? 0.044   -1.647  70.793 1   31.55 ? 532 HOH   B O     1 
HETATM 4129 O O     . HOH   G 4 .   ? 9.211   -39.878 69.371 1   11.02 ? 533 HOH   B O     1 
HETATM 4130 O O     . HOH   G 4 .   ? 21.296  -16.75  79.01  1   20.17 ? 534 HOH   B O     1 
HETATM 4131 O O     . HOH   G 4 .   ? -3.92   -14.079 89.331 1   37.85 ? 535 HOH   B O     1 
HETATM 4132 O O     . HOH   G 4 .   ? -12.964 -17.211 68.03  1   51.37 ? 536 HOH   B O     1 
HETATM 4133 O O     . HOH   G 4 .   ? 15.008  -9.179  68.34  1   29.35 ? 537 HOH   B O     1 
HETATM 4134 O O     . HOH   G 4 .   ? 7.589   -41.331 67.801 1   29.43 ? 538 HOH   B O     1 
HETATM 4135 O O     . HOH   G 4 .   ? 3.8     -8.802  62.194 1   30.45 ? 539 HOH   B O     1 
HETATM 4136 O O     . HOH   G 4 .   ? 14.713  -13.594 68.278 1   38.3  ? 540 HOH   B O     1 
HETATM 4137 O O     . HOH   G 4 .   ? -5.271  -23.108 94.575 1   31.16 ? 541 HOH   B O     1 
HETATM 4138 O O     . HOH   G 4 .   ? -18.786 -24.051 80.279 1   46.04 ? 542 HOH   B O     1 
HETATM 4139 O O     . HOH   G 4 .   ? -14.865 -31.979 76.423 1   24.36 ? 543 HOH   B O     1 
HETATM 4140 O O     . HOH   G 4 .   ? 20.777  -18.732 83.27  1   32.84 ? 544 HOH   B O     1 
HETATM 4141 O O     . HOH   G 4 .   ? 9.57    -43.345 74.663 1   43.26 ? 545 HOH   B O     1 
HETATM 4142 O O     . HOH   G 4 .   ? -0.169  -29.547 93.874 1   15.6  ? 546 HOH   B O     1 
HETATM 4143 O O     . HOH   G 4 .   ? 9.615   -2.746  68.103 1   46.36 ? 547 HOH   B O     1 
HETATM 4144 O O     . HOH   G 4 .   ? -10.241 -35.571 84.902 1   12.63 ? 548 HOH   B O     1 
HETATM 4145 O O     . HOH   G 4 .   ? 21.272  -21.307 84.611 1   18.49 ? 549 HOH   B O     1 
HETATM 4146 O O     . HOH   G 4 .   ? 22.227  -18.442 80.942 1   17.49 ? 550 HOH   B O     1 
HETATM 4147 O O     . HOH   H 4 .   ? 12.725  -52.729 73.662 1   3     ? 401 HOH   D O     1 
HETATM 4148 O O     . HOH   H 4 .   ? 29.787  -48.072 74.727 1   71.6  ? 402 HOH   D O     1 
HETATM 4149 O O     . HOH   H 4 .   ? 44.103  -54.879 80.768 1   19.93 ? 403 HOH   D O     1 
HETATM 4150 O O     . HOH   H 4 .   ? 31.989  -39.558 57.213 1   8.21  ? 404 HOH   D O     1 
HETATM 4151 O O     . HOH   H 4 .   ? 29.868  -55.913 83.637 1   3     ? 405 HOH   D O     1 
HETATM 4152 O O     . HOH   H 4 .   ? 42.083  -58.459 81.335 1   8.28  ? 406 HOH   D O     1 
HETATM 4153 O O     . HOH   H 4 .   ? 39.199  -35.138 81.742 1   3     ? 407 HOH   D O     1 
HETATM 4154 O O     . HOH   H 4 .   ? 36.173  -52.387 83.802 1   3     ? 408 HOH   D O     1 
HETATM 4155 O O     . HOH   H 4 .   ? 27.434  -39.167 91.063 1   3     ? 409 HOH   D O     1 
HETATM 4156 O O     . HOH   H 4 .   ? 47.149  -42.697 74.7   1   14.26 ? 410 HOH   D O     1 
HETATM 4157 O O     . HOH   H 4 .   ? 34.883  -61.169 74.071 1   6.57  ? 411 HOH   D O     1 
HETATM 4158 O O     . HOH   H 4 .   ? 31.264  -52.145 79.818 1   69.75 ? 412 HOH   D O     1 
HETATM 4159 O O     . HOH   H 4 .   ? 29.593  -47.16  72.288 1   3     ? 413 HOH   D O     1 
HETATM 4160 O O     . HOH   H 4 .   ? 43.974  -52.226 80.533 1   6.36  ? 414 HOH   D O     1 
HETATM 4161 O O     . HOH   H 4 .   ? 20.327  -56.371 92.155 1   13.39 ? 415 HOH   D O     1 
HETATM 4162 O O     . HOH   H 4 .   ? 6.937   -46.103 78.186 1   26.51 ? 416 HOH   D O     1 
HETATM 4163 O O     . HOH   H 4 .   ? 14.256  -52.944 88.523 1   34.21 ? 417 HOH   D O     1 
HETATM 4164 O O     . HOH   H 4 .   ? 53.368  -44.227 72.652 1   19.18 ? 418 HOH   D O     1 
HETATM 4165 O O     . HOH   H 4 .   ? 26.352  -44.775 81.981 1   4.82  ? 419 HOH   D O     1 
HETATM 4166 O O     . HOH   H 4 .   ? 16.249  -61.472 72.202 1   11.48 ? 420 HOH   D O     1 
HETATM 4167 O O     . HOH   H 4 .   ? 36.476  -49.177 57.723 1   21.34 ? 421 HOH   D O     1 
HETATM 4168 O O     . HOH   H 4 .   ? 28.563  -64.317 85.046 1   37.11 ? 422 HOH   D O     1 
HETATM 4169 O O     . HOH   H 4 .   ? 44.861  -48.507 72.121 1   3     ? 423 HOH   D O     1 
HETATM 4170 O O     . HOH   H 4 .   ? 39.512  -28.511 78.571 1   22.4  ? 424 HOH   D O     1 
HETATM 4171 O O     . HOH   H 4 .   ? 19.431  -52.031 54.241 1   14.42 ? 425 HOH   D O     1 
HETATM 4172 O O     . HOH   H 4 .   ? 16.556  -61.674 84.151 1   20.64 ? 426 HOH   D O     1 
HETATM 4173 O O     . HOH   H 4 .   ? 32.778  -55.217 84.251 1   3     ? 427 HOH   D O     1 
HETATM 4174 O O     . HOH   H 4 .   ? 28.016  -62.55  63.011 1   24.15 ? 428 HOH   D O     1 
HETATM 4175 O O     . HOH   H 4 .   ? 29.699  -66.93  78.125 1   15.24 ? 429 HOH   D O     1 
HETATM 4176 O O     . HOH   H 4 .   ? 41.162  -44.266 86.645 1   16.77 ? 430 HOH   D O     1 
HETATM 4177 O O     . HOH   H 4 .   ? 33.537  -25.792 77.158 1   26.65 ? 431 HOH   D O     1 
HETATM 4178 O O     . HOH   H 4 .   ? 22.389  -34.594 90.208 1   4.55  ? 432 HOH   D O     1 
HETATM 4179 O O     . HOH   H 4 .   ? 47.427  -41.883 65.451 1   32.36 ? 433 HOH   D O     1 
HETATM 4180 O O     . HOH   H 4 .   ? 16.2    -51.282 89.466 1   19.84 ? 434 HOH   D O     1 
HETATM 4181 O O     . HOH   H 4 .   ? 16.139  -44.991 51.356 1   15.55 ? 435 HOH   D O     1 
HETATM 4182 O O     . HOH   H 4 .   ? 22.947  -44.041 64.355 1   3     ? 436 HOH   D O     1 
HETATM 4183 O O     . HOH   H 4 .   ? 41.644  -61.229 73.836 1   27.28 ? 437 HOH   D O     1 
HETATM 4184 O O     . HOH   H 4 .   ? 18.234  -53.686 71.77  1   3     ? 438 HOH   D O     1 
HETATM 4185 O O     . HOH   H 4 .   ? 33.462  -29.664 65.972 1   47.96 ? 439 HOH   D O     1 
HETATM 4186 O O     . HOH   H 4 .   ? 25.052  -42.257 65.092 1   3     ? 440 HOH   D O     1 
HETATM 4187 O O     . HOH   H 4 .   ? 30.207  -51.031 51.386 1   4.81  ? 441 HOH   D O     1 
HETATM 4188 O O     . HOH   H 4 .   ? 10.22   -49.793 83.518 1   31.94 ? 442 HOH   D O     1 
HETATM 4189 O O     . HOH   H 4 .   ? 27.527  -51.042 50.523 1   21.06 ? 443 HOH   D O     1 
HETATM 4190 O O     . HOH   H 4 .   ? 32.649  -41.364 55.322 1   7.1   ? 444 HOH   D O     1 
HETATM 4191 O O     . HOH   H 4 .   ? 44.309  -38.607 72.317 1   7.65  ? 445 HOH   D O     1 
HETATM 4192 O O     . HOH   H 4 .   ? 35.151  -62.233 67.032 1   12.63 ? 446 HOH   D O     1 
HETATM 4193 O O     . HOH   H 4 .   ? 42.387  -32.67  75.038 1   33.36 ? 447 HOH   D O     1 
HETATM 4194 O O     . HOH   H 4 .   ? 16.914  -55.76  55.44  1   34.09 ? 448 HOH   D O     1 
HETATM 4195 O O     . HOH   H 4 .   ? 11.331  -47.014 83.928 1   22.6  ? 449 HOH   D O     1 
HETATM 4196 O O     . HOH   H 4 .   ? 22.296  -48.383 85.771 1   3     ? 450 HOH   D O     1 
HETATM 4197 O O     . HOH   H 4 .   ? 22.068  -52.5   53.83  1   37.22 ? 451 HOH   D O     1 
HETATM 4198 O O     . HOH   H 4 .   ? 20.401  -43.123 64.047 1   3     ? 452 HOH   D O     1 
HETATM 4199 O O     . HOH   H 4 .   ? 27.57   -24.694 74.817 1   32.28 ? 453 HOH   D O     1 
HETATM 4200 O O     . HOH   H 4 .   ? 42.849  -39.359 82.528 1   37.83 ? 454 HOH   D O     1 
HETATM 4201 O O     . HOH   H 4 .   ? 38.965  -26.791 71.416 1   8.74  ? 455 HOH   D O     1 
HETATM 4202 O O     . HOH   H 4 .   ? 24.984  -34.217 59.35  1   31.05 ? 456 HOH   D O     1 
HETATM 4203 O O     . HOH   H 4 .   ? 15.352  -59.119 61.64  1   36.3  ? 457 HOH   D O     1 
HETATM 4204 O O     . HOH   H 4 .   ? 9.459   -46.262 64.408 1   25.63 ? 458 HOH   D O     1 
HETATM 4205 O O     . HOH   H 4 .   ? 26.082  -50.444 80.406 1   3     ? 459 HOH   D O     1 
HETATM 4206 O O     . HOH   H 4 .   ? 33.488  -51.369 94.601 1   35.69 ? 460 HOH   D O     1 
HETATM 4207 O O     . HOH   H 4 .   ? 13.429  -56.236 60.394 1   29.68 ? 461 HOH   D O     1 
HETATM 4208 O O     . HOH   H 4 .   ? 29.936  -58.273 62.315 1   4.13  ? 462 HOH   D O     1 
HETATM 4209 O O     . HOH   H 4 .   ? 31.152  -29.274 85.818 1   16.14 ? 463 HOH   D O     1 
HETATM 4210 O O     . HOH   H 4 .   ? 31.265  -26.675 78.388 1   41.5  ? 464 HOH   D O     1 
HETATM 4211 O O     . HOH   H 4 .   ? 18.332  -41.692 53.73  1   10.82 ? 465 HOH   D O     1 
HETATM 4212 O O     . HOH   H 4 .   ? 26.057  -54.355 90.418 1   5.46  ? 466 HOH   D O     1 
HETATM 4213 O O     . HOH   H 4 .   ? 44.383  -40.035 77.019 1   3     ? 467 HOH   D O     1 
HETATM 4214 O O     . HOH   H 4 .   ? 29.714  -30.034 66.84  1   46.34 ? 468 HOH   D O     1 
HETATM 4215 O O     . HOH   H 4 .   ? 24.977  -58.108 89.327 1   9.9   ? 469 HOH   D O     1 
HETATM 4216 O O     . HOH   H 4 .   ? 30.037  -61.969 84.807 1   3     ? 470 HOH   D O     1 
HETATM 4217 O O     . HOH   H 4 .   ? 16.259  -41.782 90.296 1   21.27 ? 471 HOH   D O     1 
HETATM 4218 O O     . HOH   H 4 .   ? 10.638  -46.851 70.775 1   19.2  ? 472 HOH   D O     1 
HETATM 4219 O O     . HOH   H 4 .   ? 34.204  -39.36  93.392 1   17.53 ? 473 HOH   D O     1 
HETATM 4220 O O     . HOH   H 4 .   ? 10.653  -40.5   81.228 1   9.72  ? 474 HOH   D O     1 
HETATM 4221 O O     . HOH   H 4 .   ? 31.431  -53.02  93.229 1   34.08 ? 475 HOH   D O     1 
HETATM 4222 O O     . HOH   H 4 .   ? 29.01   -46.823 94.1   1   10.64 ? 476 HOH   D O     1 
HETATM 4223 O O     . HOH   H 4 .   ? 21.744  -67.86  83.803 1   6.65  ? 477 HOH   D O     1 
HETATM 4224 O O     . HOH   H 4 .   ? 37.115  -31.050 82.329 1   4.12  ? 478 HOH   D O     1 
HETATM 4225 O O     . HOH   H 4 .   ? 36.494  -36.715 92.077 1   31.72 ? 479 HOH   D O     1 
HETATM 4226 O O     . HOH   H 4 .   ? 39.732  -36.444 61.317 1   31.64 ? 480 HOH   D O     1 
HETATM 4227 O O     . HOH   H 4 .   ? 18.261  -37.041 71.61  1   39.16 ? 481 HOH   D O     1 
HETATM 4228 O O     . HOH   H 4 .   ? 37.775  -38.739 89.811 1   29.01 ? 482 HOH   D O     1 
HETATM 4229 O O     . HOH   H 4 .   ? 28.958  -55.909 63.45  1   3     ? 483 HOH   D O     1 
HETATM 4230 O O     . HOH   H 4 .   ? 20.23   -62.39  76.679 1   7.98  ? 484 HOH   D O     1 
HETATM 4231 O O     . HOH   H 4 .   ? 26.126  -28.729 84.06  1   13    ? 485 HOH   D O     1 
HETATM 4232 O O     . HOH   H 4 .   ? 23.814  -68.935 76.913 1   18.91 ? 486 HOH   D O     1 
HETATM 4233 O O     . HOH   H 4 .   ? 7.824   -43.86  69.443 1   21.02 ? 487 HOH   D O     1 
HETATM 4234 O O     . HOH   H 4 .   ? 21.681  -29.639 85.14  1   30.17 ? 488 HOH   D O     1 
HETATM 4235 O O     . HOH   H 4 .   ? 40.625  -62.907 80.009 1   25.39 ? 489 HOH   D O     1 
HETATM 4236 O O     . HOH   H 4 .   ? 35.32   -39.863 55.353 1   27.31 ? 490 HOH   D O     1 
HETATM 4237 O O     . HOH   H 4 .   ? 15.732  -59.642 88.501 1   3     ? 491 HOH   D O     1 
HETATM 4238 O O     . HOH   H 4 .   ? 14.666  -36.475 57.956 1   20.23 ? 492 HOH   D O     1 
HETATM 4239 O O     . HOH   H 4 .   ? 20.246  -52.079 73.057 1   3     ? 493 HOH   D O     1 
HETATM 4240 O O     . HOH   H 4 .   ? 40.225  -60.512 87.623 1   29.61 ? 494 HOH   D O     1 
HETATM 4241 O O     . HOH   H 4 .   ? 28.122  -63.747 76.351 1   3.31  ? 495 HOH   D O     1 
HETATM 4242 O O     . HOH   H 4 .   ? 35.978  -40.417 91.543 1   9.7   ? 496 HOH   D O     1 
HETATM 4243 O O     . HOH   H 4 .   ? 38.843  -60.907 73.423 1   9.06  ? 497 HOH   D O     1 
HETATM 4244 O O     . HOH   H 4 .   ? 10.729  -55.716 73.519 1   8.98  ? 498 HOH   D O     1 
HETATM 4245 O O     . HOH   H 4 .   ? 39.666  -46.302 87.686 1   33.07 ? 499 HOH   D O     1 
HETATM 4246 O O     . HOH   H 4 .   ? 30.134  -38.954 91.323 1   15.34 ? 500 HOH   D O     1 
HETATM 4247 O O     . HOH   H 4 .   ? 23.524  -27.93  84.073 1   27.64 ? 501 HOH   D O     1 
HETATM 4248 O O     . HOH   H 4 .   ? 43.113  -49.78  63.519 1   9.06  ? 502 HOH   D O     1 
HETATM 4249 O O     . HOH   H 4 .   ? 21.064  -26.665 76.11  1   3     ? 503 HOH   D O     1 
HETATM 4250 O O     . HOH   H 4 .   ? 37.955  -59.932 61.913 1   6.56  ? 504 HOH   D O     1 
HETATM 4251 O O     . HOH   H 4 .   ? 26.278  -66.169 84.435 1   3.25  ? 505 HOH   D O     1 
HETATM 4252 O O     . HOH   H 4 .   ? 41.083  -33.778 80.092 1   8.06  ? 506 HOH   D O     1 
HETATM 4253 O O     . HOH   H 4 .   ? 41.84   -38.252 71.397 1   3     ? 507 HOH   D O     1 
HETATM 4254 O O     . HOH   H 4 .   ? 39.065  -64.88  81.575 1   20.62 ? 508 HOH   D O     1 
HETATM 4255 O O     . HOH   H 4 .   ? 36.893  -33.704 81.695 1   4.43  ? 509 HOH   D O     1 
HETATM 4256 O O     . HOH   H 4 .   ? 34.866  -54.505 82.698 1   3     ? 510 HOH   D O     1 
HETATM 4257 O O     . HOH   H 4 .   ? 43.793  -49.663 86.975 1   23.67 ? 511 HOH   D O     1 
HETATM 4258 O O     . HOH   H 4 .   ? 44.464  -42.556 75.727 1   3     ? 512 HOH   D O     1 
HETATM 4259 O O     . HOH   H 4 .   ? 12.859  -54.029 84.308 1   7.71  ? 513 HOH   D O     1 
HETATM 4260 O O     . HOH   H 4 .   ? 39.632  -45.017 52.489 1   30.22 ? 514 HOH   D O     1 
HETATM 4261 O O     . HOH   H 4 .   ? 43.486  -34.003 77.468 1   31.97 ? 515 HOH   D O     1 
HETATM 4262 O O     . HOH   H 4 .   ? 38.378  -55.767 86.548 1   12.17 ? 516 HOH   D O     1 
HETATM 4263 O O     . HOH   H 4 .   ? 19.392  -36.714 74.172 1   26.9  ? 517 HOH   D O     1 
HETATM 4264 O O     . HOH   H 4 .   ? 37.745  -45.183 85.984 1   43.71 ? 518 HOH   D O     1 
HETATM 4265 O O     . HOH   H 4 .   ? 26.472  -65.858 75.822 1   11.31 ? 519 HOH   D O     1 
HETATM 4266 O O     . HOH   H 4 .   ? 15.098  -44.661 86.695 1   8.86  ? 520 HOH   D O     1 
HETATM 4267 O O     . HOH   H 4 .   ? 44.579  -48.313 78.687 1   25.63 ? 521 HOH   D O     1 
HETATM 4268 O O     . HOH   H 4 .   ? 16.551  -56.184 68.175 1   3.61  ? 522 HOH   D O     1 
HETATM 4269 O O     . HOH   H 4 .   ? 40.887  -58.146 85.321 1   23.21 ? 523 HOH   D O     1 
HETATM 4270 O O     . HOH   H 4 .   ? 9.858   -57.726 75.122 1   3.56  ? 524 HOH   D O     1 
HETATM 4271 O O     . HOH   H 4 .   ? 32.617  -65.945 74.481 1   38.08 ? 525 HOH   D O     1 
HETATM 4272 O O     . HOH   H 4 .   ? 26.893  -55.711 54.379 1   25.71 ? 526 HOH   D O     1 
HETATM 4273 O O     . HOH   H 4 .   ? 47.12   -45.247 81.616 1   12.89 ? 527 HOH   D O     1 
HETATM 4274 O O     . HOH   H 4 .   ? 36.721  -50.853 55.576 1   41.12 ? 528 HOH   D O     1 
HETATM 4275 O O     . HOH   H 4 .   ? 21.874  -43.864 91.995 1   6.88  ? 529 HOH   D O     1 
HETATM 4276 O O     . HOH   H 4 .   ? 27.987  -45.826 78.02  1   3     ? 530 HOH   D O     1 
HETATM 4277 O O     . HOH   H 4 .   ? 28.655  -43.452 50.33  1   13.42 ? 531 HOH   D O     1 
HETATM 4278 O O     . HOH   H 4 .   ? 16.52   -42.444 87.607 1   3     ? 532 HOH   D O     1 
HETATM 4279 O O     . HOH   H 4 .   ? 16.643  -57.669 90.291 1   6.51  ? 533 HOH   D O     1 
HETATM 4280 O O     . HOH   H 4 .   ? 25.252  -63.367 65.089 1   36.56 ? 534 HOH   D O     1 
HETATM 4281 O O     . HOH   H 4 .   ? 25.169  -47.801 92.642 1   23.66 ? 535 HOH   D O     1 
HETATM 4282 O O     . HOH   H 4 .   ? 33.312  -62.586 86.404 1   13.65 ? 536 HOH   D O     1 
HETATM 4283 O O     . HOH   H 4 .   ? 34.273  -53.207 52.887 1   32.37 ? 537 HOH   D O     1 
HETATM 4284 O O     . HOH   H 4 .   ? 9.207   -51.278 80.173 1   6.79  ? 538 HOH   D O     1 
HETATM 4285 O O     . HOH   H 4 .   ? 18.579  -64.182 78.72  1   30.03 ? 539 HOH   D O     1 
HETATM 4286 O O     . HOH   H 4 .   ? 29.935  -67.937 74.42  1   32.38 ? 540 HOH   D O     1 
HETATM 4287 O O     . HOH   H 4 .   ? 23.277  -61.727 60.99  1   27.63 ? 541 HOH   D O     1 
HETATM 4288 O O     . HOH   H 4 .   ? 22.525  -59.406 90.356 1   26.92 ? 542 HOH   D O     1 
HETATM 4289 O O     . HOH   H 4 .   ? 44.247  -49.638 76.361 1   19.22 ? 543 HOH   D O     1 
HETATM 4290 O O     . HOH   H 4 .   ? 10.77   -54.419 71.452 1   3     ? 544 HOH   D O     1 
HETATM 4291 O O     . HOH   H 4 .   ? 18.425  -43.641 76.08  1   32.6  ? 545 HOH   D O     1 
HETATM 4292 O O     . HOH   H 4 .   ? 34.932  -48.822 48.079 1   36.59 ? 546 HOH   D O     1 
HETATM 4293 O O     . HOH   H 4 .   ? 46.824  -47.306 79.854 1   38.36 ? 547 HOH   D O     1 
HETATM 4294 O O     . HOH   H 4 .   ? 8.93    -47.582 73.876 1   26.48 ? 548 HOH   D O     1 
HETATM 4295 O O     . HOH   H 4 .   ? 48.972  -49.602 73.893 1   22.96 ? 549 HOH   D O     1 
HETATM 4296 O O     . HOH   H 4 .   ? 22.607  -47.25  47.675 1   27.42 ? 550 HOH   D O     1 
HETATM 4297 O O     . HOH   H 4 .   ? 34.265  -58.451 92.374 1   12.36 ? 551 HOH   D O     1 
HETATM 4298 O O     . HOH   H 4 .   ? 24.812  -26.381 81.987 1   20.1  ? 552 HOH   D O     1 
HETATM 4299 O O     . HOH   H 4 .   ? 20.247  -33.504 88.899 1   48.43 ? 553 HOH   D O     1 
HETATM 4300 O O     . HOH   H 4 .   ? 17.065  -59.041 68.725 1   30.03 ? 554 HOH   D O     1 
HETATM 4301 O O     . HOH   H 4 .   ? 20.532  -41.185 91.617 1   4.56  ? 555 HOH   D O     1 
HETATM 4302 O O     . HOH   H 4 .   ? 35.07   -54.447 87.509 1   24.79 ? 556 HOH   D O     1 
HETATM 4303 O O     . HOH   H 4 .   ? 26.748  -57.686 56.325 1   21.85 ? 557 HOH   D O     1 
HETATM 4304 O O     . HOH   H 4 .   ? 23.288  -25.194 75.555 1   41.76 ? 558 HOH   D O     1 
HETATM 4305 O O     . HOH   H 4 .   ? 27.829  -52.344 91.485 1   45.79 ? 559 HOH   D O     1 
HETATM 4306 O O     . HOH   H 4 .   ? 43.811  -44.8   86.208 1   27.89 ? 560 HOH   D O     1 
HETATM 4307 O O     . HOH   H 4 .   ? 10.018  -46.565 87.805 1   21.59 ? 561 HOH   D O     1 
HETATM 4308 O O     . HOH   H 4 .   ? 32.796  -30.052 68.889 1   39.6  ? 562 HOH   D O     1 
HETATM 4309 O O     . HOH   H 4 .   ? 11.466  -54.424 75.708 1   8.63  ? 563 HOH   D O     1 
HETATM 4310 O O     . HOH   H 4 .   ? 21.304  -31.233 87.82  1   36.64 ? 564 HOH   D O     1 
HETATM 4311 O O     . HOH   H 4 .   ? 16.811  -41.21  76.38  1   20.45 ? 565 HOH   D O     1 
HETATM 4312 O O     . HOH   H 4 .   ? 45.847  -38.72  79.427 1   33.66 ? 566 HOH   D O     1 
HETATM 4313 O O     . HOH   H 4 .   ? 32.812  -44.413 48.979 1   26.24 ? 567 HOH   D O     1 
HETATM 4314 O O     . HOH   H 4 .   ? 12.18   -57.203 70.779 1   4.66  ? 568 HOH   D O     1 
HETATM 4315 O O     . HOH   H 4 .   ? 45.415  -50.388 70.229 1   6.84  ? 569 HOH   D O     1 
HETATM 4316 O O     . HOH   H 4 .   ? 25.876  -25.86  79.268 1   37.43 ? 570 HOH   D O     1 
HETATM 4317 O O     . HOH   H 4 .   ? 24.261  -32.658 89.757 1   32.26 ? 571 HOH   D O     1 
HETATM 4318 O O     . HOH   H 4 .   ? 15.525  -44.335 48.667 1   43.21 ? 572 HOH   D O     1 
HETATM 4319 O O     . HOH   H 4 .   ? 38.493  -49.327 51.366 1   24.86 ? 573 HOH   D O     1 
HETATM 4320 O O     . HOH   H 4 .   ? 31.707  -40.455 93.397 1   15.01 ? 574 HOH   D O     1 
HETATM 4321 O O     . HOH   H 4 .   ? 18.878  -52.357 91.036 1   31.88 ? 575 HOH   D O     1 
HETATM 4322 O O     . HOH   H 4 .   ? 38.134  -31.503 85.061 1   20.68 ? 576 HOH   D O     1 
HETATM 4323 O O     . HOH   H 4 .   ? 46.045  -50.415 74.366 1   25.55 ? 577 HOH   D O     1 
HETATM 4324 O O     . HOH   H 4 .   ? 20.623  -61.4   61.641 1   32.4  ? 578 HOH   D O     1 
HETATM 4325 O O     . HOH   H 4 .   ? 41.291  -49.287 87.954 1   16.16 ? 579 HOH   D O     1 
HETATM 4326 O O     . HOH   H 4 .   ? 40.084  -42.163 51.157 1   34.52 ? 580 HOH   D O     1 
HETATM 4327 O O     . HOH   H 4 .   ? 18.917  -52.797 51.638 1   18.87 ? 581 HOH   D O     1 
HETATM 4328 O O     . HOH   H 4 .   ? 37.547  -52.915 86.165 1   3     ? 582 HOH   D O     1 
HETATM 4329 O O     . HOH   H 4 .   ? 29.922  -39.27  95.101 1   39.17 ? 583 HOH   D O     1 
HETATM 4330 O O     . HOH   H 4 .   ? 9.880   -48.358 85.793 1   30.85 ? 584 HOH   D O     1 
HETATM 4331 O O     . HOH   H 4 .   ? 28.819  -44.835 47.972 1   32.92 ? 585 HOH   D O     1 
HETATM 4332 O O     . HOH   H 4 .   ? 32.086  -41.267 52.145 1   30.47 ? 586 HOH   D O     1 
HETATM 4333 O O     . HOH   H 4 .   ? 32.914  -39.681 95.788 1   46.07 ? 587 HOH   D O     1 
HETATM 4334 O O     . HOH   H 4 .   ? 26.034  -38.705 93.416 1   11.39 ? 588 HOH   D O     1 
HETATM 4335 O O     . HOH   H 4 .   ? 9.645   -56.886 71.312 1   23.11 ? 589 HOH   D O     1 
HETATM 4336 O O     . HOH   H 4 .   ? 26.249  -45.544 93.927 1   28    ? 590 HOH   D O     1 
HETATM 4337 O O     . HOH   H 4 .   ? 5.974   -54.253 65.862 1   38.18 ? 591 HOH   D O     1 
HETATM 4338 O O     . HOH   H 4 .   ? 21.022  -49.537 46.308 1   21.94 ? 592 HOH   D O     1 
HETATM 4339 O O     . HOH   H 4 .   ? 24.193  -43.792 93.41  1   25.39 ? 593 HOH   D O     1 
HETATM 4340 O O     . HOH   H 4 .   ? 14.388  -41.404 85.977 1   26.36 ? 594 HOH   D O     1 
HETATM 4341 O O     . HOH   H 4 .   ? 33.373  -41.674 97.59  1   35.14 ? 595 HOH   D O     1 
HETATM 4342 O O     . HOH   H 4 .   ? 7.601   -56.174 68.093 1   18.36 ? 596 HOH   D 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   . PHE A 24  ? 0.0709 0.0509 0.0387 0.0206  -0.0046 -0.0029 5   PHE B N   
2    C CA  . PHE A 24  ? 0.038  0.038  0.038  0       0       0       5   PHE B CA  
3    C C   . PHE A 24  ? 0.0687 0.0687 0.0686 0       0       0       5   PHE B C   
4    O O   . PHE A 24  ? 0.0828 0.059  0.0391 0.0307  -0.007  -0.0048 5   PHE B O   
5    C CB  . PHE A 24  ? 0.0443 0.0443 0.0443 0       0       0       5   PHE B CB  
6    C CG  . PHE A 24  ? 0.0405 0.0405 0.0405 0       0       0       5   PHE B CG  
7    C CD1 . PHE A 24  ? 0.0581 0.0581 0.0581 0       0       0       5   PHE B CD1 
8    C CD2 . PHE A 24  ? 0.0454 0.0454 0.0454 0       0       0       5   PHE B CD2 
9    C CE1 . PHE A 24  ? 0.0542 0.0542 0.0542 0       0       0       5   PHE B CE1 
10   C CE2 . PHE A 24  ? 0.0656 0.0656 0.0656 0       0       0       5   PHE B CE2 
11   C CZ  . PHE A 24  ? 0.038  0.038  0.038  0       0       0       5   PHE B CZ  
12   N N   . THR A 25  ? 0.038  0.038  0.038  0       0       0       6   THR B N   
13   C CA  . THR A 25  ? 0.038  0.038  0.038  0       0       0       6   THR B CA  
14   C C   . THR A 25  ? 0.0746 0.0746 0.0746 0       0       0       6   THR B C   
15   O O   . THR A 25  ? 0.0581 0.0581 0.0581 0       0       0       6   THR B O   
16   C CB  . THR A 25  ? 0.0653 0.0653 0.0653 0       0       0       6   THR B CB  
17   O OG1 . THR A 25  ? 0.038  0.038  0.038  0       0       0       6   THR B OG1 
18   C CG2 . THR A 25  ? 0.038  0.038  0.038  0       0       0       6   THR B CG2 
19   N N   . SER A 26  ? 0.0795 0.0596 0.0398 0.03    -0.0087 -0.0063 7   SER B N   
20   C CA  . SER A 26  ? 0.0884 0.069  0.0393 0.0395  -0.0083 -0.0065 7   SER B CA  
21   C C   . SER A 26  ? 0.0874 0.0817 0.0721 0.0126  -0.0027 -0.0022 7   SER B C   
22   O O   . SER A 26  ? 0.0436 0.0413 0.0383 0.0043  -0.0013 -0.001  7   SER B O   
23   C CB  . SER A 26  ? 0.181  0.1413 0.0761 0.0861  -0.0192 -0.0153 7   SER B CB  
24   O OG  . SER A 26  ? 0.2247 0.1604 0.0786 0.1182  -0.0363 -0.0278 7   SER B OG  
25   N N   . LYS A 27  ? 0.0646 0.0637 0.0614 0.0028  -0.0004 -0.0003 8   LYS B N   
26   C CA  . LYS A 27  ? 0.0739 0.0739 0.0739 0       0       0       8   LYS B CA  
27   C C   . LYS A 27  ? 0.1008 0.1008 0.1008 0       0       0       8   LYS B C   
28   O O   . LYS A 27  ? 0.0874 0.0874 0.0874 0       0       0       8   LYS B O   
29   C CB  . LYS A 27  ? 0.0848 0.0848 0.0848 0       0       0       8   LYS B CB  
30   C CG  . LYS A 27  ? 0.3088 0.3168 0.2594 0.1916  0.0234  -0.0158 8   LYS B CG  
31   C CD  . LYS A 27  ? 0.3644 0.4049 0.3888 0.2033  0.0487  -0.0145 8   LYS B CD  
32   C CE  . LYS A 27  ? 0.4312 0.5291 0.5154 0.2889  0.0705  -0.0068 8   LYS B CE  
33   N NZ  . LYS A 27  ? 0.4296 0.5603 0.5557 0.271   0.0835  0.0055  8   LYS B NZ  
34   N N   . ASP A 28  ? 0.0965 0.0893 0.0649 0.0289  -0.0062 -0.0055 9   ASP B N   
35   C CA  . ASP A 28  ? 0.1072 0.0958 0.0626 0.0412  -0.0113 -0.0098 9   ASP B CA  
36   C C   . ASP A 28  ? 0.1191 0.1043 0.0816 0.0335  -0.0131 -0.0105 9   ASP B C   
37   O O   . ASP A 28  ? 0.1047 0.0894 0.0692 0.0322  -0.0147 -0.0116 9   ASP B O   
38   C CB  . ASP A 28  ? 0.198  0.1764 0.1045 0.0866  -0.0211 -0.0186 9   ASP B CB  
39   C CG  . ASP A 28  ? 0.4317 0.3337 0.137  0.2887  -0.0726 -0.0609 9   ASP B CG  
40   O OD1 . ASP A 28  ? 0.5309 0.3923 0.2072 0.3193  -0.1002 -0.077  9   ASP B OD1 
41   O OD2 . ASP A 28  ? 0.5472 0.4443 0.2842 0.3294  -0.0587 -0.0518 9   ASP B OD2 
42   N N   . THR A 29  ? 0.0752 0.0595 0.0419 0.0283  -0.0121 -0.0092 10  THR B N   
43   C CA  . THR A 29  ? 0.0713 0.0541 0.043  0.0232  -0.0129 -0.009  10  THR B CA  
44   C C   . THR A 29  ? 0.0701 0.0701 0.0701 0       0       0       10  THR B C   
45   O O   . THR A 29  ? 0.0465 0.0465 0.0465 0       0       0       10  THR B O   
46   C CB  . THR A 29  ? 0.141  0.1023 0.0831 0.0446  -0.0261 -0.0171 10  THR B CB  
47   O OG1 . THR A 29  ? 0.1691 0.1138 0.0814 0.0671  -0.0355 -0.0238 10  THR B OG1 
48   C CG2 . THR A 29  ? 0.1302 0.1012 0.0946 0.0261  -0.0197 -0.0116 10  THR B CG2 
49   N N   . TYR A 30  ? 0.038  0.038  0.038  0       0       0       11  TYR B N   
50   C CA  . TYR A 30  ? 0.038  0.038  0.038  0       0       0       11  TYR B CA  
51   C C   . TYR A 30  ? 0.0802 0.0802 0.0802 0       0       0       11  TYR B C   
52   O O   . TYR A 30  ? 0.0513 0.0513 0.0513 0       0       0       11  TYR B O   
53   C CB  . TYR A 30  ? 0.038  0.038  0.038  0       0       0       11  TYR B CB  
54   C CG  . TYR A 30  ? 0.038  0.038  0.038  0       0       0       11  TYR B CG  
55   C CD1 . TYR A 30  ? 0.0517 0.0517 0.0517 0       0       0       11  TYR B CD1 
56   C CD2 . TYR A 30  ? 0.038  0.038  0.038  0       0       0       11  TYR B CD2 
57   C CE1 . TYR A 30  ? 0.0511 0.0511 0.0511 0       0       0       11  TYR B CE1 
58   C CE2 . TYR A 30  ? 0.038  0.038  0.038  0       0       0       11  TYR B CE2 
59   C CZ  . TYR A 30  ? 0.0608 0.0608 0.0608 0       0       0       11  TYR B CZ  
60   O OH  . TYR A 30  ? 0.038  0.038  0.038  0       0       0       11  TYR B OH  
61   N N   . LEU A 31  ? 0.0405 0.0405 0.0405 0       0       0       12  LEU B N   
62   C CA  . LEU A 31  ? 0.0555 0.0555 0.0555 0       0       0       12  LEU B CA  
63   C C   . LEU A 31  ? 0.1001 0.1001 0.1001 0       0       0       12  LEU B C   
64   O O   . LEU A 31  ? 0.0987 0.0987 0.0987 0       0       0       12  LEU B O   
65   C CB  . LEU A 31  ? 0.064  0.064  0.064  0       0       0       12  LEU B CB  
66   C CG  . LEU A 31  ? 0.1006 0.1003 0.0972 0.0037  -0.0014 -0.0013 12  LEU B CG  
67   C CD1 . LEU A 31  ? 0.129  0.1287 0.1077 0.0229  -0.0062 -0.0062 12  LEU B CD1 
68   C CD2 . LEU A 31  ? 0.0959 0.0975 0.08   0.0202  -0.0083 -0.0086 12  LEU B CD2 
69   N N   . SER A 32  ? 0.0467 0.0441 0.0428 0.0039  -0.0028 -0.002  13  SER B N   
70   C CA  . SER A 32  ? 0.0658 0.0502 0.0465 0.0184  -0.0154 -0.0102 13  SER B CA  
71   C C   . SER A 32  ? 0.1133 0.0967 0.0968 0.0151  -0.0152 -0.009  13  SER B C   
72   O O   . SER A 32  ? 0.1192 0.0967 0.1003 0.0175  -0.0205 -0.0112 13  SER B O   
73   C CB  . SER A 32  ? 0.1264 0.0862 0.0741 0.0472  -0.037  -0.0245 13  SER B CB  
74   O OG  . SER A 32  ? 0.1679 0.1144 0.094  0.0639  -0.0461 -0.0307 13  SER B OG  
75   N N   . HIS A 33  ? 0.0567 0.0442 0.0443 0.0108  -0.0108 -0.0062 14  HIS B N   
76   C CA  . HIS A 33  ? 0.0609 0.0438 0.0466 0.0116  -0.0141 -0.0071 14  HIS B CA  
77   C C   . HIS A 33  ? 0.0707 0.0707 0.0707 0       0       0       14  HIS B C   
78   O O   . HIS A 33  ? 0.038  0.038  0.038  0       0       0       14  HIS B O   
79   C CB  . HIS A 33  ? 0.1085 0.0694 0.0744 0.0257  -0.0304 -0.0151 14  HIS B CB  
80   C CG  . HIS A 33  ? 0.2048 0.1106 0.1208 0.0628  -0.0722 -0.0361 14  HIS B CG  
81   N ND1 . HIS A 33  ? 0.2283 0.114  0.112  0.0905  -0.0886 -0.0489 14  HIS B ND1 
82   C CD2 . HIS A 33  ? 0.2624 0.0995 0.1297 0.0947  -0.1233 -0.0566 14  HIS B CD2 
83   C CE1 . HIS A 33  ? 0.2788 0.1197 0.1207 0.1206  -0.1215 -0.0654 14  HIS B CE1 
84   N NE2 . HIS A 33  ? 0.3038 0.1061 0.1309 0.1258  -0.1491 -0.0725 14  HIS B NE2 
85   N N   . PHE A 34  ? 0.038  0.038  0.038  0       0       0       15  PHE B N   
86   C CA  . PHE A 34  ? 0.038  0.038  0.038  0       0       0       15  PHE B CA  
87   C C   . PHE A 34  ? 0.0713 0.0713 0.0713 0       0       0       15  PHE B C   
88   O O   . PHE A 34  ? 0.038  0.038  0.038  0       0       0       15  PHE B O   
89   C CB  . PHE A 34  ? 0.0385 0.0385 0.0385 0       0       0       15  PHE B CB  
90   C CG  . PHE A 34  ? 0.038  0.038  0.038  0       0       0       15  PHE B CG  
91   C CD1 . PHE A 34  ? 0.048  0.048  0.048  0       0       0       15  PHE B CD1 
92   C CD2 . PHE A 34  ? 0.038  0.038  0.038  0       0       0       15  PHE B CD2 
93   C CE1 . PHE A 34  ? 0.0522 0.0522 0.0522 0       0       0       15  PHE B CE1 
94   C CE2 . PHE A 34  ? 0.0713 0.0713 0.0713 0       0       0       15  PHE B CE2 
95   C CZ  . PHE A 34  ? 0.043  0.043  0.043  0       0       0       15  PHE B CZ  
96   N N   . ASN A 35  ? 0.038  0.038  0.038  0       0       0       16  ASN B N   
97   C CA  . ASN A 35  ? 0.038  0.038  0.038  0       0       0       16  ASN B CA  
98   C C   . ASN A 35  ? 0.0632 0.0632 0.0632 0       0       0       16  ASN B C   
99   O O   . ASN A 35  ? 0.0471 0.0471 0.0471 0       0       0       16  ASN B O   
100  C CB  . ASN A 35  ? 0.038  0.038  0.038  0       0       0       16  ASN B CB  
101  C CG  . ASN A 35  ? 0.2514 0.1111 0.2339 0.0295  -0.1372 -0.0277 16  ASN B CG  
102  O OD1 . ASN A 35  ? 0.2037 0.1738 0.2026 0.0057  -0.0304 -0.0056 16  ASN B OD1 
103  N ND2 . ASN A 35  ? 0.328  0.1762 0.3097 0.027   -0.1471 -0.0254 16  ASN B ND2 
104  N N   . PRO A 36  ? 0.038  0.038  0.038  0       0       0       17  PRO B N   
105  C CA  . PRO A 36  ? 0.038  0.038  0.038  0       0       0       17  PRO B CA  
106  C C   . PRO A 36  ? 0.0791 0.0791 0.0791 0       0       0       17  PRO B C   
107  O O   . PRO A 36  ? 0.0691 0.0691 0.0691 0       0       0       17  PRO B O   
108  C CB  . PRO A 36  ? 0.0552 0.0552 0.0552 0       0       0       17  PRO B CB  
109  C CG  . PRO A 36  ? 0.0711 0.0711 0.0711 0       0       0       17  PRO B CG  
110  C CD  . PRO A 36  ? 0.0582 0.0582 0.0582 0       0       0       17  PRO B CD  
111  N N   . ARG A 37  ? 0.0969 0.0969 0.0969 0       0       0       18  ARG B N   
112  C CA  . ARG A 37  ? 0.1081 0.1081 0.1081 0       0       0       18  ARG B CA  
113  C C   . ARG A 37  ? 0.0945 0.0945 0.0945 0       0       0       18  ARG B C   
114  O O   . ARG A 37  ? 0.0899 0.0899 0.0899 0       0       0       18  ARG B O   
115  C CB  . ARG A 37  ? 0.0861 0.0861 0.0861 0       0       0       18  ARG B CB  
116  C CG  . ARG A 37  ? 0.1974 0.1716 0.2282 0.034   -0.0951 0.0014  18  ARG B CG  
117  C CD  . ARG A 37  ? 0.4559 0.4482 0.4934 0.0295  -0.1322 0.0036  18  ARG B CD  
118  N NE  . ARG A 37  ? 0.7172 0.7387 0.7533 0.0202  -0.1193 -0.016  18  ARG B NE  
119  C CZ  . ARG A 37  ? 0.9314 0.9737 0.9741 0.0122  -0.1445 -0.0204 18  ARG B CZ  
120  N NH1 . ARG A 37  ? 0.7404 0.8029 0.7813 0.0038  -0.1296 -0.039  18  ARG B NH1 
121  N NH2 . ARG A 37  ? 0.7906 0.8303 0.8407 0.0128  -0.1877 -0.0066 18  ARG B NH2 
122  N N   . ASP A 38  ? 0.082  0.082  0.082  0       0       0       19  ASP B N   
123  C CA  . ASP A 38  ? 0.0996 0.0996 0.0996 0       0       0       19  ASP B CA  
124  C C   . ASP A 38  ? 0.085  0.085  0.085  0       0       0       19  ASP B C   
125  O O   . ASP A 38  ? 0.091  0.091  0.091  0       0       0       19  ASP B O   
126  C CB  . ASP A 38  ? 0.0846 0.0846 0.0846 0       0       0       19  ASP B CB  
127  C CG  . ASP A 38  ? 0.306  0.127  0.3609 0.0225  -0.1699 0.0746  19  ASP B CG  
128  O OD1 . ASP A 38  ? 0.3916 0.2417 0.4759 0.0045  -0.1702 0.0976  19  ASP B OD1 
129  O OD2 . ASP A 38  ? 0.4491 0.2263 0.4904 0.0354  -0.1932 0.073   19  ASP B OD2 
130  N N   . TYR A 39  ? 0.0504 0.0504 0.0504 0       0       0       20  TYR B N   
131  C CA  . TYR A 39  ? 0.0384 0.0384 0.0384 0       0       0       20  TYR B CA  
132  C C   . TYR A 39  ? 0.0967 0.0967 0.0967 0       0       0       20  TYR B C   
133  O O   . TYR A 39  ? 0.0967 0.0967 0.0967 0       0       0       20  TYR B O   
134  C CB  . TYR A 39  ? 0.038  0.038  0.038  0       0       0       20  TYR B CB  
135  C CG  . TYR A 39  ? 0.038  0.038  0.038  0       0       0       20  TYR B CG  
136  C CD1 . TYR A 39  ? 0.0449 0.0449 0.0449 0       0       0       20  TYR B CD1 
137  C CD2 . TYR A 39  ? 0.038  0.038  0.038  0       0       0       20  TYR B CD2 
138  C CE1 . TYR A 39  ? 0.038  0.038  0.038  0       0       0       20  TYR B CE1 
139  C CE2 . TYR A 39  ? 0.038  0.038  0.038  0       0       0       20  TYR B CE2 
140  C CZ  . TYR A 39  ? 0.0555 0.0555 0.0555 0       0       0       20  TYR B CZ  
141  O OH  . TYR A 39  ? 0.038  0.038  0.038  0       0       0       20  TYR B OH  
142  N N   . LEU A 40  ? 0.1012 0.1012 0.1012 0       0       0       21  LEU B N   
143  C CA  . LEU A 40  ? 0.1197 0.1197 0.1197 0       0       0       21  LEU B CA  
144  C C   . LEU A 40  ? 0.0883 0.0883 0.0883 0       0       0       21  LEU B C   
145  O O   . LEU A 40  ? 0.1104 0.1104 0.1104 0       0       0       21  LEU B O   
146  C CB  . LEU A 40  ? 0.1263 0.1263 0.1263 0       0       0       21  LEU B CB  
147  C CG  . LEU A 40  ? 0.0923 0.0923 0.0923 0       0       0       21  LEU B CG  
148  C CD1 . LEU A 40  ? 0.0972 0.0972 0.0972 0       0       0       21  LEU B CD1 
149  C CD2 . LEU A 40  ? 0.0759 0.0759 0.0759 0       0       0       21  LEU B CD2 
150  N N   . GLU A 41  ? 0.1114 0.1114 0.1114 0       0       0       22  GLU B N   
151  C CA  . GLU A 41  ? 0.1046 0.1046 0.1046 0       0       0       22  GLU B CA  
152  C C   . GLU A 41  ? 0.0829 0.0991 0.1263 -0.0008 -0.0013 0.0266  22  GLU B C   
153  O O   . GLU A 41  ? 0.1133 0.1366 0.1651 0.0007  0.0011  0.0348  22  GLU B O   
154  C CB  . GLU A 41  ? 0.1015 0.113  0.1413 -0.0071 -0.0121 0.0254  22  GLU B CB  
155  C CG  . GLU A 41  ? 0.2231 0.2365 0.3382 -0.0022 -0.0629 0.1283  22  GLU B CG  
156  C CD  . GLU A 41  ? 0.5776 0.5838 0.6708 0.0472  -0.0849 0.2256  22  GLU B CD  
157  O OE1 . GLU A 41  ? 0.5706 0.6098 0.6511 0.0493  -0.065  0.1988  22  GLU B OE1 
158  O OE2 . GLU A 41  ? 0.5287 0.5412 0.6392 0.05    -0.0939 0.2782  22  GLU B OE2 
159  N N   . LYS A 42  ? 0.1216 0.1216 0.1216 0       0       0       23  LYS B N   
160  C CA  . LYS A 42  ? 0.1267 0.1267 0.1267 0       0       0       23  LYS B CA  
161  C C   . LYS A 42  ? 0.095  0.095  0.095  0       0       0       23  LYS B C   
162  O O   . LYS A 42  ? 0.1031 0.1031 0.1031 0       0       0       23  LYS B O   
163  C CB  . LYS A 42  ? 0.1075 0.1075 0.1075 0       0       0       23  LYS B CB  
164  C CG  . LYS A 42  ? 0.2341 0.1581 0.3558 -0.0086 -0.0748 0.0941  23  LYS B CG  
165  C CD  . LYS A 42  ? 0.4217 0.2791 0.5311 0.0029  -0.118  0.1235  23  LYS B CD  
166  C CE  . LYS A 42  ? 0.4732 0.2983 0.6014 -0.0027 -0.1687 0.1522  23  LYS B CE  
167  N NZ  . LYS A 42  ? 0.5507 0.3456 0.6735 0.0075  -0.2134 0.1732  23  LYS B NZ  
168  N N   . TYR A 43  ? 0.059  0.059  0.059  0       0       0       24  TYR B N   
169  C CA  . TYR A 43  ? 0.038  0.038  0.038  0       0       0       24  TYR B CA  
170  C C   . TYR A 43  ? 0.0733 0.0733 0.0733 0       0       0       24  TYR B C   
171  O O   . TYR A 43  ? 0.0439 0.0439 0.0439 0       0       0       24  TYR B O   
172  C CB  . TYR A 43  ? 0.038  0.038  0.038  0       0       0       24  TYR B CB  
173  C CG  . TYR A 43  ? 0.038  0.038  0.038  0       0       0       24  TYR B CG  
174  C CD1 . TYR A 43  ? 0.0444 0.0444 0.0444 0       0       0       24  TYR B CD1 
175  C CD2 . TYR A 43  ? 0.038  0.038  0.038  0       0       0       24  TYR B CD2 
176  C CE1 . TYR A 43  ? 0.038  0.038  0.038  0       0       0       24  TYR B CE1 
177  C CE2 . TYR A 43  ? 0.038  0.038  0.038  0       0       0       24  TYR B CE2 
178  C CZ  . TYR A 43  ? 0.0915 0.0915 0.0915 0       0       0       24  TYR B CZ  
179  O OH  . TYR A 43  ? 0.038  0.038  0.038  0       0       0       24  TYR B OH  
180  N N   . TYR A 44  ? 0.038  0.038  0.038  0       0       0       25  TYR B N   
181  C CA  . TYR A 44  ? 0.038  0.038  0.038  0       0       0       25  TYR B CA  
182  C C   . TYR A 44  ? 0.179  0.1415 0.1837 0.0553  0.1032  0.1118  25  TYR B C   
183  O O   . TYR A 44  ? 0.1395 0.1395 0.1395 0       0       0       25  TYR B O   
184  C CB  . TYR A 44  ? 0.0437 0.0437 0.0437 0       0       0       25  TYR B CB  
185  C CG  . TYR A 44  ? 0.038  0.038  0.038  0       0       0       25  TYR B CG  
186  C CD1 . TYR A 44  ? 0.0498 0.0498 0.0498 0       0       0       25  TYR B CD1 
187  C CD2 . TYR A 44  ? 0.038  0.038  0.038  0       0       0       25  TYR B CD2 
188  C CE1 . TYR A 44  ? 0.0483 0.0483 0.0483 0       0       0       25  TYR B CE1 
189  C CE2 . TYR A 44  ? 0.038  0.038  0.038  0       0       0       25  TYR B CE2 
190  C CZ  . TYR A 44  ? 0.0711 0.0711 0.0711 0       0       0       25  TYR B CZ  
191  O OH  . TYR A 44  ? 0.038  0.038  0.038  0       0       0       25  TYR B OH  
192  N N   . GLU A 53  ? 0.043  0.043  0.043  0       0       0       34  GLU B N   
193  C CA  . GLU A 53  ? 0.038  0.038  0.038  0       0       0       34  GLU B CA  
194  C C   . GLU A 53  ? 0.0853 0.0853 0.0853 0       0       0       34  GLU B C   
195  O O   . GLU A 53  ? 0.0741 0.0741 0.0741 0       0       0       34  GLU B O   
196  C CB  . GLU A 53  ? 0.0521 0.0521 0.0521 0       0       0       34  GLU B CB  
197  C CG  . GLU A 53  ? 0.103  0.103  0.103  0       0       0       34  GLU B CG  
198  C CD  . GLU A 53  ? 0.1016 0.0826 0.2243 0.0324  0.0848  0.0634  34  GLU B CD  
199  O OE1 . GLU A 53  ? 0.1573 0.1628 0.2283 0.0142  0.0312  0.0378  34  GLU B OE1 
200  O OE2 . GLU A 53  ? 0.1243 0.1243 0.1243 0       0       0       34  GLU B OE2 
201  N N   . SER A 54  ? 0.0588 0.0588 0.0588 0       0       0       35  SER B N   
202  C CA  . SER A 54  ? 0.0742 0.0742 0.0742 0       0       0       35  SER B CA  
203  C C   . SER A 54  ? 0.0833 0.0833 0.0833 0       0       0       35  SER B C   
204  O O   . SER A 54  ? 0.0816 0.0816 0.0816 0       0       0       35  SER B O   
205  C CB  . SER A 54  ? 0.1108 0.1052 0.1326 0.0292  0.0416  0.0378  35  SER B CB  
206  O OG  . SER A 54  ? 0.1712 0.1896 0.2657 0.0952  0.125   0.1377  35  SER B OG  
207  N N   . GLN A 55  ? 0.0536 0.0536 0.0536 0       0       0       36  GLN B N   
208  C CA  . GLN A 55  ? 0.0487 0.0487 0.0487 0       0       0       36  GLN B CA  
209  C C   . GLN A 55  ? 0.0686 0.0686 0.0686 0       0       0       36  GLN B C   
210  O O   . GLN A 55  ? 0.0408 0.0408 0.0408 0       0       0       36  GLN B O   
211  C CB  . GLN A 55  ? 0.0735 0.0735 0.0735 0       0       0       36  GLN B CB  
212  C CG  . GLN A 55  ? 0.2623 0.1109 0.2917 0.0701  0.2089  0.1142  36  GLN B CG  
213  C CD  . GLN A 55  ? 0.6221 0.4281 0.5652 0.0268  0.2776  0.2131  36  GLN B CD  
214  O OE1 . GLN A 55  ? 0.6075 0.457  0.5412 0.0493  0.2704  0.2313  36  GLN B OE1 
215  N NE2 . GLN A 55  ? 0.5523 0.3392 0.4962 0.0341  0.2755  0.1679  36  GLN B NE2 
216  N N   . ILE A 56  ? 0.0387 0.0387 0.0387 0       0       0       37  ILE B N   
217  C CA  . ILE A 56  ? 0.038  0.038  0.038  0       0       0       37  ILE B CA  
218  C C   . ILE A 56  ? 0.0703 0.0703 0.0703 0       0       0       37  ILE B C   
219  O O   . ILE A 56  ? 0.044  0.044  0.044  0       0       0       37  ILE B O   
220  C CB  . ILE A 56  ? 0.0529 0.0529 0.0529 0       0       0       37  ILE B CB  
221  C CG1 . ILE A 56  ? 0.038  0.038  0.038  0       0       0       37  ILE B CG1 
222  C CG2 . ILE A 56  ? 0.0432 0.0432 0.0432 0       0       0       37  ILE B CG2 
223  C CD1 . ILE A 56  ? 0.0851 0.0851 0.0851 0       0       0       37  ILE B CD1 
224  N N   . LEU A 57  ? 0.038  0.038  0.038  0       0       0       38  LEU B N   
225  C CA  . LEU A 57  ? 0.038  0.038  0.038  0       0       0       38  LEU B CA  
226  C C   . LEU A 57  ? 0.0595 0.0595 0.0595 0       0       0       38  LEU B C   
227  O O   . LEU A 57  ? 0.038  0.038  0.038  0       0       0       38  LEU B O   
228  C CB  . LEU A 57  ? 0.0427 0.0427 0.0427 0       0       0       38  LEU B CB  
229  C CG  . LEU A 57  ? 0.0889 0.0889 0.0889 0       0       0       38  LEU B CG  
230  C CD1 . LEU A 57  ? 0.0844 0.0844 0.0844 0       0       0       38  LEU B CD1 
231  C CD2 . LEU A 57  ? 0.0786 0.0786 0.0786 0       0       0       38  LEU B CD2 
232  N N   . LYS A 58  ? 0.038  0.038  0.038  0       0       0       39  LYS B N   
233  C CA  . LYS A 58  ? 0.038  0.038  0.038  0       0       0       39  LYS B CA  
234  C C   . LYS A 58  ? 0.0977 0.0977 0.0977 0       0       0       39  LYS B C   
235  O O   . LYS A 58  ? 0.0822 0.0822 0.0822 0       0       0       39  LYS B O   
236  C CB  . LYS A 58  ? 0.0685 0.0685 0.0685 0       0       0       39  LYS B CB  
237  C CG  . LYS A 58  ? 0.2656 0.1292 0.1959 0.0878  0.1403  0.0687  39  LYS B CG  
238  C CD  . LYS A 58  ? 0.3724 0.2656 0.246  0.0939  0.2324  0.153   39  LYS B CD  
239  C CE  . LYS A 58  ? 0.6335 0.5829 0.4729 0.0959  0.2687  0.2405  39  LYS B CE  
240  N NZ  . LYS A 58  ? 0.7895 0.7415 0.5755 0.0753  0.3212  0.3558  39  LYS B NZ  
241  N N   . HIS A 59  ? 0.0801 0.0801 0.0801 0       0       0       40  HIS B N   
242  C CA  . HIS A 59  ? 0.0858 0.0858 0.0858 0       0       0       40  HIS B CA  
243  C C   . HIS A 59  ? 0.0946 0.0946 0.0946 0       0       0       40  HIS B C   
244  O O   . HIS A 59  ? 0.0786 0.0786 0.0786 0       0       0       40  HIS B O   
245  C CB  . HIS A 59  ? 0.119  0.119  0.119  0       0       0       40  HIS B CB  
246  C CG  . HIS A 59  ? 0.1054 0.1054 0.1054 0       0       0       40  HIS B CG  
247  N ND1 . HIS A 59  ? 0.093  0.089  0.0914 -0.0013 0.0035  -0.001  40  HIS B ND1 
248  C CD2 . HIS A 59  ? 0.0934 0.0871 0.0915 -0.0031 0.0066  -0.0027 40  HIS B CD2 
249  C CE1 . HIS A 59  ? 0.0977 0.0977 0.0977 0       0       0       40  HIS B CE1 
250  N NE2 . HIS A 59  ? 0.0949 0.0949 0.0949 0       0       0       40  HIS B NE2 
251  N N   . LEU A 60  ? 0.038  0.038  0.038  0       0       0       41  LEU B N   
252  C CA  . LEU A 60  ? 0.038  0.038  0.038  0       0       0       41  LEU B CA  
253  C C   . LEU A 60  ? 0.0588 0.0588 0.0588 0       0       0       41  LEU B C   
254  O O   . LEU A 60  ? 0.038  0.038  0.038  0       0       0       41  LEU B O   
255  C CB  . LEU A 60  ? 0.038  0.038  0.038  0       0       0       41  LEU B CB  
256  C CG  . LEU A 60  ? 0.0933 0.0933 0.0933 0       0       0       41  LEU B CG  
257  C CD1 . LEU A 60  ? 0.0849 0.0849 0.0849 0       0       0       41  LEU B CD1 
258  C CD2 . LEU A 60  ? 0.0813 0.0813 0.0813 0       0       0       41  LEU B CD2 
259  N N   . LEU A 61  ? 0.038  0.038  0.038  0       0       0       42  LEU B N   
260  C CA  . LEU A 61  ? 0.0412 0.0412 0.0412 0       0       0       42  LEU B CA  
261  C C   . LEU A 61  ? 0.0542 0.0542 0.0542 0       0       0       42  LEU B C   
262  O O   . LEU A 61  ? 0.038  0.038  0.038  0       0       0       42  LEU B O   
263  C CB  . LEU A 61  ? 0.0438 0.0438 0.0438 0       0       0       42  LEU B CB  
264  C CG  . LEU A 61  ? 0.0967 0.0967 0.0967 0       0       0       42  LEU B CG  
265  C CD1 . LEU A 61  ? 0.0979 0.0979 0.0979 0       0       0       42  LEU B CD1 
266  C CD2 . LEU A 61  ? 0.0802 0.0802 0.0802 0       0       0       42  LEU B CD2 
267  N N   . LYS A 62  ? 0.038  0.038  0.038  0       0       0       43  LYS B N   
268  C CA  . LYS A 62  ? 0.038  0.038  0.038  0       0       0       43  LYS B CA  
269  C C   . LYS A 62  ? 0.0836 0.0836 0.0836 0       0       0       43  LYS B C   
270  O O   . LYS A 62  ? 0.0565 0.0565 0.0565 0       0       0       43  LYS B O   
271  C CB  . LYS A 62  ? 0.0717 0.0717 0.0717 0       0       0       43  LYS B CB  
272  C CG  . LYS A 62  ? 0.1469 0.1204 0.1296 -0.0008 0.0156  -0.0005 43  LYS B CG  
273  C CD  . LYS A 62  ? 0.2818 0.1648 0.2091 -0.0048 0.0723  -0.003  43  LYS B CD  
274  C CE  . LYS A 62  ? 0.4595 0.2122 0.307  0.0289  0.1568  0.0181  43  LYS B CE  
275  N NZ  . LYS A 62  ? 0.5931 0.334  0.4158 0.0202  0.2058  0.0208  43  LYS B NZ  
276  N N   . ASN A 63  ? 0.0397 0.0397 0.0397 0       0       0       44  ASN B N   
277  C CA  . ASN A 63  ? 0.038  0.038  0.038  0       0       0       44  ASN B CA  
278  C C   . ASN A 63  ? 0.0697 0.0697 0.0697 0       0       0       44  ASN B C   
279  O O   . ASN A 63  ? 0.0534 0.0534 0.0534 0       0       0       44  ASN B O   
280  C CB  . ASN A 63  ? 0.0866 0.0866 0.0866 0       0       0       44  ASN B CB  
281  C CG  . ASN A 63  ? 0.1946 0.1322 0.1827 -0.0751 0.1064  -0.071  44  ASN B CG  
282  O OD1 . ASN A 63  ? 0.2229 0.2004 0.2158 -0.0282 0.0379  -0.0257 44  ASN B OD1 
283  N ND2 . ASN A 63  ? 0.1631 0.1577 0.1627 -0.0057 0.0088  -0.0056 44  ASN B ND2 
284  N N   . LEU A 64  ? 0.038  0.038  0.038  0       0       0       45  LEU B N   
285  C CA  . LEU A 64  ? 0.038  0.038  0.038  0       0       0       45  LEU B CA  
286  C C   . LEU A 64  ? 0.0931 0.0931 0.0931 0       0       0       45  LEU B C   
287  O O   . LEU A 64  ? 0.0793 0.0793 0.0793 0       0       0       45  LEU B O   
288  C CB  . LEU A 64  ? 0.0395 0.0395 0.0395 0       0       0       45  LEU B CB  
289  C CG  . LEU A 64  ? 0.0907 0.0907 0.0907 0       0       0       45  LEU B CG  
290  C CD1 . LEU A 64  ? 0.0878 0.0878 0.0878 0       0       0       45  LEU B CD1 
291  C CD2 . LEU A 64  ? 0.065  0.065  0.065  0       0       0       45  LEU B CD2 
292  N N   . PHE A 65  ? 0.0924 0.0924 0.0924 0       0       0       46  PHE B N   
293  C CA  . PHE A 65  ? 0.1034 0.1034 0.1034 0       0       0       46  PHE B CA  
294  C C   . PHE A 65  ? 0.0894 0.0894 0.0894 0       0       0       46  PHE B C   
295  O O   . PHE A 65  ? 0.0949 0.0949 0.0949 0       0       0       46  PHE B O   
296  C CB  . PHE A 65  ? 0.0967 0.0967 0.0967 0       0       0       46  PHE B CB  
297  C CG  . PHE A 65  ? 0.147  0.1148 0.0943 0.033   0.0018  0.0011  46  PHE B CG  
298  C CD1 . PHE A 65  ? 0.2416 0.1843 0.0838 0.1062  -0.0034 -0.0235 46  PHE B CD1 
299  C CD2 . PHE A 65  ? 0.1973 0.1258 0.078  0.0623  0.0151  -0.0024 46  PHE B CD2 
300  C CE1 . PHE A 65  ? 0.31   0.2387 0.0841 0.1559  -0.0109 -0.0383 46  PHE B CE1 
301  C CE2 . PHE A 65  ? 0.2799 0.2032 0.0809 0.1132  0.0172  -0.0222 46  PHE B CE2 
302  C CZ  . PHE A 65  ? 0.2962 0.2219 0.0751 0.157   -0.007  -0.0251 46  PHE B CZ  
303  N N   . LYS A 66  ? 0.0437 0.0437 0.0437 0       0       0       47  LYS B N   
304  C CA  . LYS A 66  ? 0.0545 0.0545 0.0545 0       0       0       47  LYS B CA  
305  C C   . LYS A 66  ? 0.0925 0.0925 0.0925 0       0       0       47  LYS B C   
306  O O   . LYS A 66  ? 0.0884 0.0884 0.0884 0       0       0       47  LYS B O   
307  C CB  . LYS A 66  ? 0.106  0.106  0.106  0       0       0       47  LYS B CB  
308  C CG  . LYS A 66  ? 0.1716 0.1993 0.1713 -0.0937 0.0807  -0.0935 47  LYS B CG  
309  C CD  . LYS A 66  ? 0.357  0.3559 0.3293 -0.1425 0.136   -0.1402 47  LYS B CD  
310  C CE  . LYS A 66  ? 0.5726 0.5666 0.4885 -0.1527 0.1741  -0.2422 47  LYS B CE  
311  N NZ  . LYS A 66  ? 0.6507 0.601  0.5418 -0.1779 0.2299  -0.295  47  LYS B NZ  
312  N N   . ILE A 67  ? 0.0488 0.0488 0.0488 0       0       0       48  ILE B N   
313  C CA  . ILE A 67  ? 0.038  0.038  0.038  0       0       0       48  ILE B CA  
314  C C   . ILE A 67  ? 0.095  0.095  0.095  0       0       0       48  ILE B C   
315  O O   . ILE A 67  ? 0.0927 0.0927 0.0927 0       0       0       48  ILE B O   
316  C CB  . ILE A 67  ? 0.0609 0.0609 0.0609 0       0       0       48  ILE B CB  
317  C CG1 . ILE A 67  ? 0.064  0.064  0.064  0       0       0       48  ILE B CG1 
318  C CG2 . ILE A 67  ? 0.038  0.038  0.038  0       0       0       48  ILE B CG2 
319  C CD1 . ILE A 67  ? 0.1072 0.1162 0.1215 -0.0173 0.0192  -0.0248 48  ILE B CD1 
320  N N   . PHE A 68  ? 0.0803 0.0803 0.0803 0       0       0       49  PHE B N   
321  C CA  . PHE A 68  ? 0.1048 0.1048 0.1048 0       0       0       49  PHE B CA  
322  C C   . PHE A 68  ? 0.1229 0.1462 0.1271 0.027   -0.0198 -0.03   49  PHE B C   
323  O O   . PHE A 68  ? 0.1368 0.1498 0.1321 0.039   -0.0306 -0.0361 49  PHE B O   
324  C CB  . PHE A 68  ? 0.117  0.117  0.117  0       0       0       49  PHE B CB  
325  C CG  . PHE A 68  ? 0.1032 0.1032 0.1032 0       0       0       49  PHE B CG  
326  C CD1 . PHE A 68  ? 0.0859 0.1103 0.1083 0.0006  -0.0006 -0.0234 49  PHE B CD1 
327  C CD2 . PHE A 68  ? 0.0918 0.0993 0.0983 -0.0023 0.0021  -0.0076 49  PHE B CD2 
328  C CE1 . PHE A 68  ? 0.0804 0.1143 0.1162 -0.0043 0.0044  -0.0354 49  PHE B CE1 
329  C CE2 . PHE A 68  ? 0.0774 0.1067 0.1086 -0.0141 0.0144  -0.0359 49  PHE B CE2 
330  C CZ  . PHE A 68  ? 0.0904 0.1059 0.1079 -0.0053 0.0055  -0.0181 49  PHE B CZ  
331  N N   . CYS A 69  ? 0.1489 0.1634 0.1439 0.0241  -0.0152 -0.0205 50  CYS B N   
332  C CA  . CYS A 69  ? 0.1977 0.1972 0.1348 0.093   -0.0532 -0.053  50  CYS B CA  
333  C C   . CYS A 69  ? 0.2326 0.2263 0.1316 0.1238  -0.0701 -0.0832 50  CYS B C   
334  O O   . CYS A 69  ? 0.2951 0.2539 0.1422 0.1688  -0.0977 -0.098  50  CYS B O   
335  C CB  . CYS A 69  ? 0.238  0.2105 0.1163 0.1313  -0.0591 -0.0532 50  CYS B CB  
336  S SG  . CYS A 69  ? 0.3086 0.263  0.1509 0.1389  -0.0563 -0.0692 50  CYS B SG  
337  N N   . LEU A 70  ? 0.1666 0.1904 0.1489 0.05    -0.0294 -0.0372 51  LEU B N   
338  C CA  . LEU A 70  ? 0.3035 0.3145 0.1915 0.084   -0.0452 -0.1166 51  LEU B CA  
339  C C   . LEU A 70  ? 0.6069 0.5997 0.4302 0.0639  -0.0535 -0.2083 51  LEU B C   
340  O O   . LEU A 70  ? 0.194  0.2469 0.1909 0.0853  -0.0613 -0.0832 51  LEU B O   
341  C CB  . LEU A 70  ? 0.2768 0.2896 0.165  0.054   -0.015  -0.1041 51  LEU B CB  
342  C CG  . LEU A 70  ? 0.378  0.3572 0.2187 0.0725  -0.0057 -0.0876 51  LEU B CG  
343  C CD1 . LEU A 70  ? 0.3712 0.3403 0.2076 0.04    0.0247  -0.0833 51  LEU B CD1 
344  C CD2 . LEU A 70  ? 0.4517 0.4019 0.222  0.1354  -0.0286 -0.0896 51  LEU B CD2 
345  N N   . GLY A 72  ? 0.3036 0.3571 0.3164 0.0959  -0.0857 -0.1227 53  GLY B N   
346  C CA  . GLY A 72  ? 0.2459 0.3337 0.3121 0.0819  -0.0767 -0.1297 53  GLY B CA  
347  C C   . GLY A 72  ? 0.2682 0.3367 0.3281 0.0717  -0.0935 -0.1678 53  GLY B C   
348  O O   . GLY A 72  ? 0.2987 0.3456 0.374  0.0959  -0.1223 -0.1649 53  GLY B O   
349  N N   . VAL A 73  ? 0.1414 0.2562 0.2515 0.0551  -0.0547 -0.1365 54  VAL B N   
350  C CA  . VAL A 73  ? 0.1222 0.2256 0.2417 0.0478  -0.0508 -0.1299 54  VAL B CA  
351  C C   . VAL A 73  ? 0.179  0.246  0.2733 0.0713  -0.0795 -0.1252 54  VAL B C   
352  O O   . VAL A 73  ? 0.194  0.2581 0.2669 0.0744  -0.0772 -0.1173 54  VAL B O   
353  C CB  . VAL A 73  ? 0.0755 0.2181 0.2285 0.0165  -0.0171 -0.1496 54  VAL B CB  
354  C CG1 . VAL A 73  ? 0.0836 0.2078 0.24   0.0176  -0.0198 -0.1418 54  VAL B CG1 
355  C CG2 . VAL A 73  ? 0.0746 0.2098 0.2139 -0.0057 0.0058  -0.1375 54  VAL B CG2 
356  N N   . LYS A 74  ? 0.1755 0.1985 0.2446 0.0643  -0.0813 -0.0971 55  LYS B N   
357  C CA  . LYS A 74  ? 0.209  0.195  0.2561 0.08    -0.1084 -0.0993 55  LYS B CA  
358  C C   . LYS A 74  ? 0.2166 0.1827 0.2815 0.0801  -0.1272 -0.1031 55  LYS B C   
359  O O   . LYS A 74  ? 0.1862 0.164  0.2724 0.0679  -0.1153 -0.0979 55  LYS B O   
360  C CB  . LYS A 74  ? 0.2815 0.2176 0.2919 0.1196  -0.1609 -0.1235 55  LYS B CB  
361  C CG  . LYS A 74  ? 0.4726 0.3474 0.4664 0.1468  -0.2553 -0.1896 55  LYS B CG  
362  C CD  . LYS A 74  ? 0.7148 0.531  0.5566 0.1304  -0.3402 -0.286  55  LYS B CD  
363  C CE  . LYS A 74  ? 0.8866 0.7031 0.6756 0.0776  -0.4288 -0.3704 55  LYS B CE  
364  N NZ  . LYS A 74  ? 1.0091 0.8125 0.7075 0.0855  -0.4296 -0.4053 55  LYS B NZ  
365  N N   . GLY A 75  ? 0.2324 0.1747 0.2731 0.0761  -0.129  -0.0891 56  GLY B N   
366  C CA  . GLY A 75  ? 0.2407 0.1624 0.2945 0.0715  -0.1451 -0.086  56  GLY B CA  
367  C C   . GLY A 75  ? 0.2666 0.1552 0.3123 0.084   -0.1779 -0.0955 56  GLY B C   
368  O O   . GLY A 75  ? 0.2721 0.1557 0.2891 0.0944  -0.1774 -0.099  56  GLY B O   
369  N N   . ASP A 76  ? 0.2458 0.1349 0.3031 0.0658  -0.1677 -0.0779 57  ASP B N   
370  C CA  . ASP A 76  ? 0.2595 0.1255 0.3115 0.0682  -0.1868 -0.0784 57  ASP B CA  
371  C C   . ASP A 76  ? 0.2121 0.1129 0.2773 0.0605  -0.1571 -0.0743 57  ASP B C   
372  O O   . ASP A 76  ? 0.2158 0.1091 0.2677 0.0647  -0.1611 -0.076  57  ASP B O   
373  C CB  . ASP A 76  ? 0.3068 0.1187 0.3864 0.0684  -0.2469 -0.0803 57  ASP B CB  
374  C CG  . ASP A 76  ? 0.5099 0.1586 0.5936 0.1113  -0.4389 -0.1294 57  ASP B CG  
375  O OD1 . ASP A 76  ? 0.5829 0.2158 0.6061 0.1335  -0.4531 -0.153  57  ASP B OD1 
376  O OD2 . ASP A 76  ? 0.5991 0.2464 0.719  0.0869  -0.5239 -0.1215 57  ASP B OD2 
377  N N   . LEU A 77  ? 0.149  0.1036 0.21   0.0347  -0.0896 -0.0485 58  LEU B N   
378  C CA  . LEU A 77  ? 0.097  0.0762 0.1515 0.0233  -0.0569 -0.0369 58  LEU B CA  
379  C C   . LEU A 77  ? 0.0943 0.0929 0.1302 0.0123  -0.0253 -0.0239 58  LEU B C   
380  O O   . LEU A 77  ? 0.0479 0.0484 0.0835 0.0101  -0.0212 -0.0217 58  LEU B O   
381  C CB  . LEU A 77  ? 0.1013 0.0735 0.1722 0.0204  -0.065  -0.0344 58  LEU B CB  
382  C CG  . LEU A 77  ? 0.1278 0.1128 0.1997 0.0155  -0.049  -0.0307 58  LEU B CG  
383  C CD1 . LEU A 77  ? 0.1312 0.1197 0.1845 0.0137  -0.039  -0.026  58  LEU B CD1 
384  C CD2 . LEU A 77  ? 0.1235 0.0871 0.2687 0.02    -0.0929 -0.0411 58  LEU B CD2 
385  N N   . LEU A 78  ? 0.0532 0.0557 0.0705 0.0056  -0.0099 -0.0123 59  LEU B N   
386  C CA  . LEU A 78  ? 0.0563 0.0563 0.0563 0       0       0       59  LEU B CA  
387  C C   . LEU A 78  ? 0.1004 0.1004 0.1004 0       0       0       59  LEU B C   
388  O O   . LEU A 78  ? 0.0875 0.0875 0.0875 0       0       0       59  LEU B O   
389  C CB  . LEU A 78  ? 0.0637 0.0637 0.0637 0       0       0       59  LEU B CB  
390  C CG  . LEU A 78  ? 0.0861 0.0889 0.0906 0.0002  -0.0002 -0.0036 59  LEU B CG  
391  C CD1 . LEU A 78  ? 0.0806 0.0886 0.0919 0.0001  -0.0001 -0.0096 59  LEU B CD1 
392  C CD2 . LEU A 78  ? 0.0711 0.0929 0.1048 -0.0009 0.0011  -0.0271 59  LEU B CD2 
393  N N   . ILE A 79  ? 0.0392 0.0392 0.0392 0       0       0       60  ILE B N   
394  C CA  . ILE A 79  ? 0.038  0.038  0.038  0       0       0       60  ILE B CA  
395  C C   . ILE A 79  ? 0.0727 0.0727 0.0727 0       0       0       60  ILE B C   
396  O O   . ILE A 79  ? 0.038  0.038  0.038  0       0       0       60  ILE B O   
397  C CB  . ILE A 79  ? 0.0605 0.0605 0.0605 0       0       0       60  ILE B CB  
398  C CG1 . ILE A 79  ? 0.0404 0.0404 0.0404 0       0       0       60  ILE B CG1 
399  C CG2 . ILE A 79  ? 0.0597 0.0597 0.0597 0       0       0       60  ILE B CG2 
400  C CD1 . ILE A 79  ? 0.1136 0.1136 0.1136 0       0       0       60  ILE B CD1 
401  N N   . ASP A 80  ? 0.038  0.038  0.038  0       0       0       61  ASP B N   
402  C CA  . ASP A 80  ? 0.0381 0.0381 0.0381 0       0       0       61  ASP B CA  
403  C C   . ASP A 80  ? 0.0844 0.0844 0.0844 0       0       0       61  ASP B C   
404  O O   . ASP A 80  ? 0.0686 0.0686 0.0686 0       0       0       61  ASP B O   
405  C CB  . ASP A 80  ? 0.0596 0.0596 0.0596 0       0       0       61  ASP B CB  
406  C CG  . ASP A 80  ? 0.1185 0.1465 0.1962 -0.0252 0.037   -0.063  61  ASP B CG  
407  O OD1 . ASP A 80  ? 0.1845 0.1983 0.228  -0.0153 0.023   -0.0355 61  ASP B OD1 
408  O OD2 . ASP A 80  ? 0.1745 0.1993 0.2542 -0.0295 0.0441  -0.0664 61  ASP B OD2 
409  N N   . ILE A 81  ? 0.038  0.038  0.038  0       0       0       62  ILE B N   
410  C CA  . ILE A 81  ? 0.038  0.038  0.038  0       0       0       62  ILE B CA  
411  C C   . ILE A 81  ? 0.0708 0.0708 0.0708 0       0       0       62  ILE B C   
412  O O   . ILE A 81  ? 0.038  0.038  0.038  0       0       0       62  ILE B O   
413  C CB  . ILE A 81  ? 0.066  0.066  0.066  0       0       0       62  ILE B CB  
414  C CG1 . ILE A 81  ? 0.0634 0.0634 0.0634 0       0       0       62  ILE B CG1 
415  C CG2 . ILE A 81  ? 0.0722 0.0722 0.0722 0       0       0       62  ILE B CG2 
416  C CD1 . ILE A 81  ? 0.0949 0.1048 0.1365 -0.0032 0.0064  -0.0215 62  ILE B CD1 
417  N N   . GLY A 82  ? 0.038  0.038  0.038  0       0       0       63  GLY B N   
418  C CA  . GLY A 82  ? 0.038  0.038  0.038  0       0       0       63  GLY B CA  
419  C C   . GLY A 82  ? 0.0642 0.0642 0.0642 0       0       0       63  GLY B C   
420  O O   . GLY A 82  ? 0.038  0.038  0.038  0       0       0       63  GLY B O   
421  N N   . SER A 83  ? 0.038  0.038  0.038  0       0       0       64  SER B N   
422  C CA  . SER A 83  ? 0.038  0.038  0.038  0       0       0       64  SER B CA  
423  C C   . SER A 83  ? 0.0614 0.0614 0.0614 0       0       0       64  SER B C   
424  O O   . SER A 83  ? 0.038  0.038  0.038  0       0       0       64  SER B O   
425  C CB  . SER A 83  ? 0.0856 0.0856 0.0856 0       0       0       64  SER B CB  
426  O OG  . SER A 83  ? 0.103  0.1061 0.1126 -0.0025 0.0039  -0.007  64  SER B OG  
427  N N   . GLY A 84  ? 0.038  0.038  0.038  0       0       0       65  GLY B N   
428  C CA  . GLY A 84  ? 0.038  0.038  0.038  0       0       0       65  GLY B CA  
429  C C   . GLY A 84  ? 0.0717 0.0717 0.0717 0       0       0       65  GLY B C   
430  O O   . GLY A 84  ? 0.038  0.038  0.038  0       0       0       65  GLY B O   
431  N N   . PRO A 85  ? 0.038  0.038  0.038  0       0       0       66  PRO B N   
432  C CA  . PRO A 85  ? 0.038  0.038  0.038  0       0       0       66  PRO B CA  
433  C C   . PRO A 85  ? 0.0869 0.0869 0.0869 0       0       0       66  PRO B C   
434  O O   . PRO A 85  ? 0.0598 0.0598 0.0598 0       0       0       66  PRO B O   
435  C CB  . PRO A 85  ? 0.0497 0.0497 0.0497 0       0       0       66  PRO B CB  
436  C CG  . PRO A 85  ? 0.0768 0.0768 0.0768 0       0       0       66  PRO B CG  
437  C CD  . PRO A 85  ? 0.0497 0.0497 0.0497 0       0       0       66  PRO B CD  
438  N N   . THR A 86  ? 0.0511 0.0511 0.0511 0       0       0       67  THR B N   
439  C CA  . THR A 86  ? 0.038  0.038  0.038  0       0       0       67  THR B CA  
440  C C   . THR A 86  ? 0.0856 0.0856 0.0856 0       0       0       67  THR B C   
441  O O   . THR A 86  ? 0.086  0.086  0.086  0       0       0       67  THR B O   
442  C CB  . THR A 86  ? 0.0804 0.0804 0.0804 0       0       0       67  THR B CB  
443  O OG1 . THR A 86  ? 0.1101 0.1101 0.1101 0       0       0       67  THR B OG1 
444  C CG2 . THR A 86  ? 0.0436 0.0436 0.0436 0       0       0       67  THR B CG2 
445  N N   . ILE A 87  ? 0.0459 0.0459 0.0459 0       0       0       68  ILE B N   
446  C CA  . ILE A 87  ? 0.0495 0.0495 0.0495 0       0       0       68  ILE B CA  
447  C C   . ILE A 87  ? 0.0891 0.0891 0.0891 0       0       0       68  ILE B C   
448  O O   . ILE A 87  ? 0.0753 0.0753 0.0753 0       0       0       68  ILE B O   
449  C CB  . ILE A 87  ? 0.0939 0.0939 0.0939 0       0       0       68  ILE B CB  
450  C CG1 . ILE A 87  ? 0.0857 0.0857 0.0857 0       0       0       68  ILE B CG1 
451  C CG2 . ILE A 87  ? 0.0939 0.0939 0.0939 0       0       0       68  ILE B CG2 
452  C CD1 . ILE A 87  ? 0.1761 0.1385 0.0983 0.0437  0.0389  -0.0232 68  ILE B CD1 
453  N N   . TYR A 88  ? 0.038  0.038  0.038  0       0       0       69  TYR B N   
454  C CA  . TYR A 88  ? 0.04   0.04   0.04   0       0       0       69  TYR B CA  
455  C C   . TYR A 88  ? 0.0809 0.0809 0.0809 0       0       0       69  TYR B C   
456  O O   . TYR A 88  ? 0.038  0.038  0.038  0       0       0       69  TYR B O   
457  C CB  . TYR A 88  ? 0.044  0.044  0.044  0       0       0       69  TYR B CB  
458  C CG  . TYR A 88  ? 0.0567 0.0567 0.0567 0       0       0       69  TYR B CG  
459  C CD1 . TYR A 88  ? 0.0771 0.0771 0.0771 0       0       0       69  TYR B CD1 
460  C CD2 . TYR A 88  ? 0.0553 0.0553 0.0553 0       0       0       69  TYR B CD2 
461  C CE1 . TYR A 88  ? 0.0589 0.0589 0.0589 0       0       0       69  TYR B CE1 
462  C CE2 . TYR A 88  ? 0.0644 0.0644 0.0644 0       0       0       69  TYR B CE2 
463  C CZ  . TYR A 88  ? 0.0844 0.0844 0.0844 0       0       0       69  TYR B CZ  
464  O OH  . TYR A 88  ? 0.038  0.038  0.038  0       0       0       69  TYR B OH  
465  N N   . GLN A 89  ? 0.038  0.038  0.038  0       0       0       70  GLN B N   
466  C CA  . GLN A 89  ? 0.038  0.038  0.038  0       0       0       70  GLN B CA  
467  C C   . GLN A 89  ? 0.0732 0.0732 0.0732 0       0       0       70  GLN B C   
468  O O   . GLN A 89  ? 0.0397 0.0397 0.0397 0       0       0       70  GLN B O   
469  C CB  . GLN A 89  ? 0.0455 0.0455 0.0455 0       0       0       70  GLN B CB  
470  C CG  . GLN A 89  ? 0.038  0.038  0.038  0       0       0       70  GLN B CG  
471  C CD  . GLN A 89  ? 0.0793 0.0793 0.0793 0       0       0       70  GLN B CD  
472  O OE1 . GLN A 89  ? 0.0392 0.0392 0.0392 0       0       0       70  GLN B OE1 
473  N NE2 . GLN A 89  ? 0.1105 0.1105 0.1105 0       0       0       70  GLN B NE2 
474  N N   . LEU A 90  ? 0.038  0.038  0.038  0       0       0       71  LEU B N   
475  C CA  . LEU A 90  ? 0.038  0.038  0.038  0       0       0       71  LEU B CA  
476  C C   . LEU A 90  ? 0.0914 0.0914 0.0914 0       0       0       71  LEU B C   
477  O O   . LEU A 90  ? 0.088  0.088  0.088  0       0       0       71  LEU B O   
478  C CB  . LEU A 90  ? 0.0409 0.0409 0.0409 0       0       0       71  LEU B CB  
479  C CG  . LEU A 90  ? 0.087  0.087  0.087  0       0       0       71  LEU B CG  
480  C CD1 . LEU A 90  ? 0.087  0.087  0.087  0       0       0       71  LEU B CD1 
481  C CD2 . LEU A 90  ? 0.0901 0.0901 0.0901 0       0       0       71  LEU B CD2 
482  N N   . LEU A 91  ? 0.1089 0.1089 0.1089 0       0       0       72  LEU B N   
483  C CA  . LEU A 91  ? 0.1145 0.1145 0.1145 0       0       0       72  LEU B CA  
484  C C   . LEU A 91  ? 0.151  0.1332 0.0955 0.0484  -0.0123 -0.0102 72  LEU B C   
485  O O   . LEU A 91  ? 0.1881 0.1559 0.0913 0.0853  -0.025  -0.0207 72  LEU B O   
486  C CB  . LEU A 91  ? 0.1221 0.1221 0.1221 0       0       0       72  LEU B CB  
487  C CG  . LEU A 91  ? 0.1574 0.1158 0.0865 0.0467  0.0086  0.0056  72  LEU B CG  
488  C CD1 . LEU A 91  ? 0.1638 0.1201 0.098  0.0429  0.0171  0.0105  72  LEU B CD1 
489  C CD2 . LEU A 91  ? 0.2468 0.1963 0.1048 0.0968  0.0203  -0.0213 72  LEU B CD2 
490  N N   . SER A 92  ? 0.1139 0.1139 0.1139 0       0       0       73  SER B N   
491  C CA  . SER A 92  ? 0.1321 0.1321 0.1321 0       0       0       73  SER B CA  
492  C C   . SER A 92  ? 0.1357 0.1433 0.1129 0.0396  -0.0217 -0.0239 73  SER B C   
493  O O   . SER A 92  ? 0.1743 0.1706 0.1219 0.0744  -0.0427 -0.0416 73  SER B O   
494  C CB  . SER A 92  ? 0.1041 0.1041 0.1041 0       0       0       73  SER B CB  
495  O OG  . SER A 92  ? 0.1261 0.1261 0.1261 0       0       0       73  SER B OG  
496  N N   . ALA A 93  ? 0.1173 0.1173 0.1173 0       0       0       74  ALA B N   
497  C CA  . ALA A 93  ? 0.1244 0.1244 0.1244 0       0       0       74  ALA B CA  
498  C C   . ALA A 93  ? 0.1409 0.1497 0.1355 0.0353  -0.0283 -0.032  74  ALA B C   
499  O O   . ALA A 93  ? 0.1521 0.1542 0.146  0.0404  -0.0362 -0.0371 74  ALA B O   
500  C CB  . ALA A 93  ? 0.1126 0.1126 0.1126 0       0       0       74  ALA B CB  
501  N N   . CYS A 94  ? 0.1557 0.1551 0.1403 0.0307  -0.022  -0.0218 75  CYS B N   
502  C CA  . CYS A 94  ? 0.1918 0.1676 0.1409 0.0706  -0.0525 -0.0442 75  CYS B CA  
503  C C   . CYS A 94  ? 0.2665 0.1956 0.1487 0.1313  -0.0959 -0.0735 75  CYS B C   
504  O O   . CYS A 94  ? 0.3163 0.2066 0.1649 0.1565  -0.1237 -0.0877 75  CYS B O   
505  C CB  . CYS A 94  ? 0.2034 0.1719 0.1355 0.0787  -0.052  -0.0426 75  CYS B CB  
506  S SG  . CYS A 94  ? 0.2613 0.2064 0.1326 0.1206  -0.0582 -0.0464 75  CYS B SG  
507  N N   . GLU A 95  ? 0.2455 0.1915 0.1434 0.1105  -0.0737 -0.0579 76  GLU B N   
508  C CA  . GLU A 95  ? 0.2978 0.2108 0.1495 0.1463  -0.0969 -0.0723 76  GLU B CA  
509  C C   . GLU A 95  ? 0.3453 0.2342 0.186  0.1736  -0.1365 -0.0997 76  GLU B C   
510  O O   . GLU A 95  ? 0.4054 0.2485 0.2006 0.2076  -0.1694 -0.1171 76  GLU B O   
511  C CB  . GLU A 95  ? 0.3109 0.228  0.1444 0.1566  -0.0867 -0.0667 76  GLU B CB  
512  C CG  . GLU A 95  ? 0.4042 0.2854 0.1375 0.2185  -0.0913 -0.0867 76  GLU B CG  
513  C CD  . GLU A 95  ? 0.9448 0.6956 0.3685 0.2909  -0.0703 -0.2506 76  GLU B CD  
514  O OE1 . GLU A 95  ? 0.9805 0.6928 0.3518 0.3233  -0.1136 -0.2636 76  GLU B OE1 
515  O OE2 . GLU A 95  ? 1.0027 0.7686 0.4366 0.2954  -0.0457 -0.2333 76  GLU B OE2 
516  N N   . SER A 96  ? 0.2676 0.2056 0.182  0.1205  -0.1042 -0.0808 77  SER B N   
517  C CA  . SER A 96  ? 0.2579 0.1978 0.1962 0.1142  -0.1131 -0.0872 77  SER B CA  
518  C C   . SER A 96  ? 0.2744 0.2022 0.2313 0.1198  -0.1379 -0.1025 77  SER B C   
519  O O   . SER A 96  ? 0.2778 0.1946 0.2503 0.1189  -0.1532 -0.1087 77  SER B O   
520  C CB  . SER A 96  ? 0.2246 0.2031 0.1967 0.097   -0.0933 -0.0836 77  SER B CB  
521  O OG  . SER A 96  ? 0.2776 0.2481 0.2124 0.1368  -0.1153 -0.1035 77  SER B OG  
522  N N   . PHE A 97  ? 0.2398 0.185  0.2088 0.0942  -0.1089 -0.0818 78  PHE B N   
523  C CA  . PHE A 97  ? 0.2308 0.1732 0.2213 0.0857  -0.1143 -0.0822 78  PHE B CA  
524  C C   . PHE A 97  ? 0.3249 0.2013 0.2778 0.1342  -0.1845 -0.1182 78  PHE B C   
525  O O   . PHE A 97  ? 0.3379 0.2189 0.2687 0.1414  -0.175  -0.1162 78  PHE B O   
526  C CB  . PHE A 97  ? 0.1867 0.1721 0.2102 0.0565  -0.0752 -0.0661 78  PHE B CB  
527  C CG  . PHE A 97  ? 0.1691 0.1735 0.204  0.0382  -0.0505 -0.0535 78  PHE B CG  
528  C CD1 . PHE A 97  ? 0.1558 0.175  0.1915 0.0328  -0.0385 -0.0514 78  PHE B CD1 
529  C CD2 . PHE A 97  ? 0.16   0.1612 0.2185 0.045   -0.0676 -0.0685 78  PHE B CD2 
530  C CE1 . PHE A 97  ? 0.1478 0.1719 0.1848 0.0201  -0.0235 -0.0415 78  PHE B CE1 
531  C CE2 . PHE A 97  ? 0.1407 0.1587 0.2195 0.0419  -0.0618 -0.0764 78  PHE B CE2 
532  C CZ  . PHE A 97  ? 0.1487 0.1695 0.1909 0.0189  -0.0244 -0.0413 78  PHE B CZ  
533  N N   . LYS A 98  ? 0.3451 0.1853 0.2971 0.1303  -0.2074 -0.1161 79  LYS B N   
534  C CA  . LYS A 98  ? 0.3918 0.1832 0.3149 0.1422  -0.2391 -0.1212 79  LYS B CA  
535  C C   . LYS A 98  ? 0.3624 0.1751 0.3097 0.1341  -0.2294 -0.1195 79  LYS B C   
536  O O   . LYS A 98  ? 0.3899 0.1867 0.3054 0.1452  -0.2328 -0.1212 79  LYS B O   
537  C CB  . LYS A 98  ? 0.4602 0.1803 0.3829 0.152   -0.3055 -0.134  79  LYS B CB  
538  C CG  . LYS A 98  ? 0.7323 0.3114 0.5769 0.148   -0.4058 -0.2084 79  LYS B CG  
539  C CD  . LYS A 98  ? 0.9148 0.4631 0.7963 0.1458  -0.4772 -0.1863 79  LYS B CD  
540  C CE  . LYS A 98  ? 0.9944 0.5907 0.9677 0.1127  -0.4711 -0.1577 79  LYS B CE  
541  N NZ  . LYS A 98  ? 1.0916 0.6759 1.1105 0.1086  -0.5419 -0.1324 79  LYS B NZ  
542  N N   . GLU A 99  ? 0.2632 0.1395 0.2661 0.0955  -0.1771 -0.0962 80  GLU B N   
543  C CA  . GLU A 99  ? 0.2198 0.1303 0.2472 0.0769  -0.1468 -0.0844 80  GLU B CA  
544  C C   . GLU A 99  ? 0.1687 0.1298 0.223  0.0629  -0.1091 -0.0805 80  GLU B C   
545  O O   . GLU A 99  ? 0.1587 0.136  0.2207 0.0509  -0.0893 -0.0715 80  GLU B O   
546  C CB  . GLU A 99  ? 0.238  0.1216 0.2926 0.073   -0.1768 -0.0852 80  GLU B CB  
547  C CG  . GLU A 99  ? 0.3644 0.2011 0.451  0.0577  -0.2051 -0.1322 80  GLU B CG  
548  C CD  . GLU A 99  ? 0.6998 0.4904 0.8188 0.0385  -0.2435 -0.1283 80  GLU B CD  
549  O OE1 . GLU A 99  ? 0.7905 0.5388 0.905  0.0462  -0.2939 -0.1178 80  GLU B OE1 
550  O OE2 . GLU A 99  ? 0.5055 0.3306 0.6626 0.0278  -0.2186 -0.1126 80  GLU B OE2 
551  N N   . ILE A 100 ? 0.1518 0.1455 0.1753 0.0229  -0.0361 -0.0315 81  ILE B N   
552  C CA  . ILE A 100 ? 0.1427 0.1436 0.146  0.0016  -0.0024 -0.0031 81  ILE B CA  
553  C C   . ILE A 100 ? 0.1048 0.112  0.1303 0.0086  -0.0133 -0.0201 81  ILE B C   
554  O O   . ILE A 100 ? 0.1098 0.1137 0.1281 0.0076  -0.012  -0.0154 81  ILE B O   
555  C CB  . ILE A 100 ? 0.1225 0.1337 0.1442 0.0119  -0.0148 -0.0234 81  ILE B CB  
556  C CG1 . ILE A 100 ? 0.1357 0.1458 0.1542 0.0175  -0.0204 -0.0271 81  ILE B CG1 
557  C CG2 . ILE A 100 ? 0.0954 0.1107 0.1189 0.0043  -0.0053 -0.0201 81  ILE B CG2 
558  C CD1 . ILE A 100 ? 0.1379 0.1543 0.1544 0.0251  -0.0252 -0.0347 81  ILE B CD1 
559  N N   . VAL A 101 ? 0.0686 0.0686 0.0686 0       0       0       82  VAL B N   
560  C CA  . VAL A 101 ? 0.0556 0.0556 0.0556 0       0       0       82  VAL B CA  
561  C C   . VAL A 101 ? 0.0821 0.0821 0.0821 0       0       0       82  VAL B C   
562  O O   . VAL A 101 ? 0.0556 0.0556 0.0556 0       0       0       82  VAL B O   
563  C CB  . VAL A 101 ? 0.0965 0.0965 0.0965 0       0       0       82  VAL B CB  
564  C CG1 . VAL A 101 ? 0.095  0.095  0.095  0       0       0       82  VAL B CG1 
565  C CG2 . VAL A 101 ? 0.1083 0.1084 0.114  0.001   -0.0025 -0.0027 82  VAL B CG2 
566  N N   . VAL A 102 ? 0.056  0.056  0.056  0       0       0       83  VAL B N   
567  C CA  . VAL A 102 ? 0.053  0.053  0.053  0       0       0       83  VAL B CA  
568  C C   . VAL A 102 ? 0.0809 0.0809 0.0809 0       0       0       83  VAL B C   
569  O O   . VAL A 102 ? 0.088  0.088  0.088  0       0       0       83  VAL B O   
570  C CB  . VAL A 102 ? 0.0859 0.0859 0.0859 0       0       0       83  VAL B CB  
571  C CG1 . VAL A 102 ? 0.0874 0.0874 0.0874 0       0       0       83  VAL B CG1 
572  C CG2 . VAL A 102 ? 0.0861 0.0861 0.0861 0       0       0       83  VAL B CG2 
573  N N   . THR A 103 ? 0.038  0.038  0.038  0       0       0       84  THR B N   
574  C CA  . THR A 103 ? 0.038  0.038  0.038  0       0       0       84  THR B CA  
575  C C   . THR A 103 ? 0.0717 0.0717 0.0717 0       0       0       84  THR B C   
576  O O   . THR A 103 ? 0.038  0.038  0.038  0       0       0       84  THR B O   
577  C CB  . THR A 103 ? 0.0957 0.0995 0.1094 -0.001  0.0019  -0.0075 84  THR B CB  
578  O OG1 . THR A 103 ? 0.1307 0.1461 0.1877 -0.0057 0.0106  -0.0318 84  THR B OG1 
579  C CG2 . THR A 103 ? 0.1287 0.1287 0.1287 0       0       0       84  THR B CG2 
580  N N   . ASP A 104 ? 0.038  0.038  0.038  0       0       0       85  ASP B N   
581  C CA  . ASP A 104 ? 0.038  0.038  0.038  0       0       0       85  ASP B CA  
582  C C   . ASP A 104 ? 0.078  0.078  0.078  0       0       0       85  ASP B C   
583  O O   . ASP A 104 ? 0.038  0.038  0.038  0       0       0       85  ASP B O   
584  C CB  . ASP A 104 ? 0.0432 0.0432 0.0432 0       0       0       85  ASP B CB  
585  C CG  . ASP A 104 ? 0.0756 0.0756 0.0756 0       0       0       85  ASP B CG  
586  O OD1 . ASP A 104 ? 0.038  0.038  0.038  0       0       0       85  ASP B OD1 
587  O OD2 . ASP A 104 ? 0.1022 0.1022 0.1022 0       0       0       85  ASP B OD2 
588  N N   . TYR A 105 ? 0.038  0.038  0.038  0       0       0       86  TYR B N   
589  C CA  . TYR A 105 ? 0.038  0.038  0.038  0       0       0       86  TYR B CA  
590  C C   . TYR A 105 ? 0.087  0.087  0.087  0       0       0       86  TYR B C   
591  O O   . TYR A 105 ? 0.0704 0.0704 0.0704 0       0       0       86  TYR B O   
592  C CB  . TYR A 105 ? 0.0387 0.0387 0.0387 0       0       0       86  TYR B CB  
593  C CG  . TYR A 105 ? 0.068  0.068  0.068  0       0       0       86  TYR B CG  
594  C CD1 . TYR A 105 ? 0.0912 0.0912 0.0912 0       0       0       86  TYR B CD1 
595  C CD2 . TYR A 105 ? 0.0794 0.0794 0.0794 0       0       0       86  TYR B CD2 
596  C CE1 . TYR A 105 ? 0.0937 0.0937 0.0937 0       0       0       86  TYR B CE1 
597  C CE2 . TYR A 105 ? 0.0893 0.0893 0.0893 0       0       0       86  TYR B CE2 
598  C CZ  . TYR A 105 ? 0.091  0.0959 0.0729 0.0205  -0.0008 -0.0009 86  TYR B CZ  
599  O OH  . TYR A 105 ? 0.136  0.1427 0.1116 0.0276  0.0005  0.0005  86  TYR B OH  
600  N N   . SER A 106 ? 0.0432 0.0432 0.0432 0       0       0       87  SER B N   
601  C CA  . SER A 106 ? 0.049  0.049  0.049  0       0       0       87  SER B CA  
602  C C   . SER A 106 ? 0.0963 0.0963 0.0963 0       0       0       87  SER B C   
603  O O   . SER A 106 ? 0.0938 0.0938 0.0938 0       0       0       87  SER B O   
604  C CB  . SER A 106 ? 0.106  0.106  0.106  0       0       0       87  SER B CB  
605  O OG  . SER A 106 ? 0.0944 0.0944 0.0944 0       0       0       87  SER B OG  
606  N N   . ASP A 107 ? 0.1097 0.1097 0.1097 0       0       0       88  ASP B N   
607  C CA  . ASP A 107 ? 0.1126 0.1126 0.1126 0       0       0       88  ASP B CA  
608  C C   . ASP A 107 ? 0.0784 0.0784 0.0784 0       0       0       88  ASP B C   
609  O O   . ASP A 107 ? 0.0962 0.0962 0.0962 0       0       0       88  ASP B O   
610  C CB  . ASP A 107 ? 0.0863 0.0863 0.0863 0       0       0       88  ASP B CB  
611  C CG  . ASP A 107 ? 0.2055 0.2159 0.2466 0.1296  0.0081  -0.1016 88  ASP B CG  
612  O OD1 . ASP A 107 ? 0.2568 0.2856 0.3083 0.0951  0.0041  -0.0818 88  ASP B OD1 
613  O OD2 . ASP A 107 ? 0.3443 0.3626 0.357  0.1297  -0.0095 -0.0789 88  ASP B OD2 
614  N N   . GLN A 108 ? 0.0975 0.0975 0.0975 0       0       0       89  GLN B N   
615  C CA  . GLN A 108 ? 0.0933 0.0933 0.0933 0       0       0       89  GLN B CA  
616  C C   . GLN A 108 ? 0.1087 0.1087 0.1087 0       0       0       89  GLN B C   
617  O O   . GLN A 108 ? 0.0568 0.0568 0.0568 0       0       0       89  GLN B O   
618  C CB  . GLN A 108 ? 0.0998 0.0998 0.0998 0       0       0       89  GLN B CB  
619  C CG  . GLN A 108 ? 0.2458 0.1546 0.2073 0.1109  -0.0811 -0.1108 89  GLN B CG  
620  C CD  . GLN A 108 ? 0.5728 0.4532 0.523  0.1248  -0.1114 -0.0974 89  GLN B CD  
621  O OE1 . GLN A 108 ? 0.5059 0.3626 0.4475 0.1499  -0.1169 -0.0924 89  GLN B OE1 
622  N NE2 . GLN A 108 ? 0.5018 0.3828 0.4537 0.1101  -0.134  -0.0886 89  GLN B NE2 
623  N N   . ASN A 109 ? 0.0912 0.0912 0.0912 0       0       0       90  ASN B N   
624  C CA  . ASN A 109 ? 0.1012 0.1012 0.1012 0       0       0       90  ASN B CA  
625  C C   . ASN A 109 ? 0.1147 0.1147 0.1147 0       0       0       90  ASN B C   
626  O O   . ASN A 109 ? 0.1139 0.1139 0.1139 0       0       0       90  ASN B O   
627  C CB  . ASN A 109 ? 0.1072 0.1072 0.1072 0       0       0       90  ASN B CB  
628  C CG  . ASN A 109 ? 0.0533 0.0533 0.0533 0       0       0       90  ASN B CG  
629  O OD1 . ASN A 109 ? 0.1211 0.1211 0.1211 0       0       0       90  ASN B OD1 
630  N ND2 . ASN A 109 ? 0.1235 0.1235 0.1235 0       0       0       90  ASN B ND2 
631  N N   . LEU A 110 ? 0.1629 0.1629 0.1629 0       0       0       91  LEU B N   
632  C CA  . LEU A 110 ? 0.1685 0.1685 0.1685 0       0       0       91  LEU B CA  
633  C C   . LEU A 110 ? 0.1257 0.1382 0.1456 -0.001  0.0012  -0.0159 91  LEU B C   
634  O O   . LEU A 110 ? 0.1507 0.1507 0.1507 0       0       0       91  LEU B O   
635  C CB  . LEU A 110 ? 0.1684 0.1684 0.1684 0       0       0       91  LEU B CB  
636  C CG  . LEU A 110 ? 0.1109 0.1164 0.1229 -0.0007 0.0011  -0.0082 91  LEU B CG  
637  C CD1 . LEU A 110 ? 0.1105 0.116  0.1232 -0.0004 0.0005  -0.0084 91  LEU B CD1 
638  C CD2 . LEU A 110 ? 0.1078 0.1231 0.1449 -0.0041 0.0063  -0.0249 91  LEU B CD2 
639  N N   . GLN A 111 ? 0.1554 0.1554 0.1554 0       0       0       92  GLN B N   
640  C CA  . GLN A 111 ? 0.1481 0.1622 0.1668 0.0015  -0.0018 -0.0163 92  GLN B CA  
641  C C   . GLN A 111 ? 0.1503 0.1892 0.2068 0.0062  -0.0021 -0.074  92  GLN B C   
642  O O   . GLN A 111 ? 0.1698 0.2135 0.2264 0.0032  -0.0002 -0.0738 92  GLN B O   
643  C CB  . GLN A 111 ? 0.1303 0.1577 0.165  0.009   -0.01   -0.0336 92  GLN B CB  
644  C CG  . GLN A 111 ? 0.2844 0.2641 0.295  0.0253  -0.0176 -0.1348 92  GLN B CG  
645  C CD  . GLN A 111 ? 0.5906 0.5556 0.5768 0.038   -0.0358 -0.1455 92  GLN B CD  
646  O OE1 . GLN A 111 ? 0.5178 0.4825 0.4946 0.0367  -0.0554 -0.1441 92  GLN B OE1 
647  N NE2 . GLN A 111 ? 0.5025 0.4711 0.489  0.0521  -0.0338 -0.1409 92  GLN B NE2 
648  N N   . GLU A 112 ? 0.1336 0.1713 0.183  0.0038  -0.0043 -0.0435 93  GLU B N   
649  C CA  . GLU A 112 ? 0.1241 0.1635 0.1751 0.0037  -0.0025 -0.0504 93  GLU B CA  
650  C C   . GLU A 112 ? 0.215  0.2024 0.2218 0.0156  0.0253  -0.1026 93  GLU B C   
651  O O   . GLU A 112 ? 0.2282 0.2486 0.2525 0.005   0.0132  -0.0664 93  GLU B O   
652  C CB  . GLU A 112 ? 0.1346 0.148  0.1687 0.0111  -0.0011 -0.0543 93  GLU B CB  
653  C CG  . GLU A 112 ? 0.2615 0.237  0.2662 0.0255  0.0109  -0.0724 93  GLU B CG  
654  C CD  . GLU A 112 ? 0.5644 0.547  0.5654 0.0285  -0.0063 -0.0679 93  GLU B CD  
655  O OE1 . GLU A 112 ? 0.5473 0.5308 0.5526 0.0262  -0.0297 -0.0699 93  GLU B OE1 
656  O OE2 . GLU A 112 ? 0.4377 0.4374 0.4372 0.0306  -0.0008 -0.0518 93  GLU B OE2 
657  N N   . LEU A 113 ? 0.1997 0.1979 0.2256 0.0071  0.0281  -0.0924 94  LEU B N   
658  C CA  . LEU A 113 ? 0.2279 0.2222 0.2486 0.0062  0.0351  -0.0968 94  LEU B CA  
659  C C   . LEU A 113 ? 0.298  0.2976 0.3162 0.0065  0.0264  -0.0961 94  LEU B C   
660  O O   . LEU A 113 ? 0.3156 0.3161 0.323  0.0098  0.0237  -0.0876 94  LEU B O   
661  C CB  . LEU A 113 ? 0.2326 0.2435 0.2806 -0.004  0.0324  -0.0867 94  LEU B CB  
662  C CG  . LEU A 113 ? 0.2974 0.3048 0.3506 -0.008  0.0416  -0.0858 94  LEU B CG  
663  C CD1 . LEU A 113 ? 0.2952 0.3095 0.3686 -0.0095 0.0424  -0.0932 94  LEU B CD1 
664  C CD2 . LEU A 113 ? 0.3312 0.3262 0.3659 -0.0045 0.0495  -0.092  94  LEU B CD2 
665  N N   . GLU A 114 ? 0.2457 0.2513 0.2766 0.0036  0.02    -0.0982 95  GLU B N   
666  C CA  . GLU A 114 ? 0.266  0.2645 0.2909 0.0052  0.0147  -0.1048 95  GLU B CA  
667  C C   . GLU A 114 ? 0.3164 0.3036 0.3176 0.0107  0.0143  -0.1173 95  GLU B C   
668  O O   . GLU A 114 ? 0.3292 0.3133 0.3242 0.0142  0.0097  -0.1142 95  GLU B O   
669  C CB  . GLU A 114 ? 0.2776 0.271  0.3109 0.0025  0.0115  -0.1129 95  GLU B CB  
670  C CG  . GLU A 114 ? 0.4621 0.377  0.4606 0.0117  0.0174  -0.1715 95  GLU B CG  
671  C CD  . GLU A 114 ? 0.7812 0.7    0.7986 0.0074  0.0114  -0.1649 95  GLU B CD  
672  O OE1 . GLU A 114 ? 0.7809 0.7153 0.8025 0.0091  0.0128  -0.1605 95  GLU B OE1 
673  O OE2 . GLU A 114 ? 0.6976 0.603  0.7247 0.0049  0.0028  -0.1613 95  GLU B OE2 
674  N N   . LYS A 115 ? 0.2449 0.2354 0.2394 0.0121  0.0151  -0.1214 96  LYS B N   
675  C CA  . LYS A 115 ? 0.2345 0.2357 0.2209 0.0157  0.0109  -0.1181 96  LYS B CA  
676  C C   . LYS A 115 ? 0.2901 0.2986 0.2696 0.0248  0.0137  -0.1    96  LYS B C   
677  O O   . LYS A 115 ? 0.2852 0.3046 0.2672 0.0286  0.006   -0.0883 96  LYS B O   
678  C CB  . LYS A 115 ? 0.2462 0.2423 0.2179 0.0181  0.0071  -0.1292 96  LYS B CB  
679  C CG  . LYS A 115 ? 0.359  0.3573 0.3415 0.0066  -0.0111 -0.1346 96  LYS B CG  
680  C CD  . LYS A 115 ? 0.4646 0.4782 0.4586 0.0065  -0.0293 -0.1152 96  LYS B CD  
681  C CE  . LYS A 115 ? 0.6419 0.6548 0.6399 -0.0011 -0.0516 -0.122  96  LYS B CE  
682  N NZ  . LYS A 115 ? 0.7477 0.7686 0.7544 0.0016  -0.0778 -0.1021 96  LYS B NZ  
683  N N   . TRP A 116 ? 0.2301 0.2326 0.2042 0.0274  0.0211  -0.0931 97  TRP B N   
684  C CA  . TRP A 116 ? 0.2368 0.2344 0.1882 0.0414  0.0255  -0.0862 97  TRP B CA  
685  C C   . TRP A 116 ? 0.3401 0.3204 0.277  0.0492  0.0214  -0.0971 97  TRP B C   
686  O O   . TRP A 116 ? 0.356  0.3318 0.2687 0.0671  0.0185  -0.0952 97  TRP B O   
687  C CB  . TRP A 116 ? 0.2045 0.204  0.1635 0.0354  0.0272  -0.0647 97  TRP B CB  
688  C CG  . TRP A 116 ? 0.2261 0.2233 0.1646 0.05    0.026   -0.0488 97  TRP B CG  
689  C CD1 . TRP A 116 ? 0.2647 0.2712 0.1898 0.0657  0.0278  -0.0317 97  TRP B CD1 
690  C CD2 . TRP A 116 ? 0.2527 0.2439 0.1908 0.0507  0.0129  -0.0364 97  TRP B CD2 
691  N NE1 . TRP A 116 ? 0.2856 0.287  0.1891 0.0842  0.0266  -0.0213 97  TRP B NE1 
692  C CE2 . TRP A 116 ? 0.3195 0.3064 0.2204 0.0792  0.0221  -0.0337 97  TRP B CE2 
693  C CE3 . TRP A 116 ? 0.2712 0.2594 0.2185 0.044   0.0078  -0.044  97  TRP B CE3 
694  C CZ2 . TRP A 116 ? 0.3403 0.317  0.2209 0.0951  0.0153  -0.0298 97  TRP B CZ2 
695  C CZ3 . TRP A 116 ? 0.3136 0.2897 0.2362 0.0611  0.0036  -0.0467 97  TRP B CZ3 
696  C CH2 . TRP A 116 ? 0.3452 0.3124 0.2303 0.0875  0.0082  -0.0434 97  TRP B CH2 
697  N N   . LEU A 117 ? 0.3259 0.3001 0.2802 0.038   0.0172  -0.102  98  LEU B N   
698  C CA  . LEU A 117 ? 0.3712 0.3133 0.3023 0.0497  0.0121  -0.1237 98  LEU B CA  
699  C C   . LEU A 117 ? 0.5003 0.3776 0.3686 0.0725  0.0183  -0.1845 98  LEU B C   
700  O O   . LEU A 117 ? 0.5279 0.3831 0.371  0.0895  0.008   -0.1869 98  LEU B O   
701  C CB  . LEU A 117 ? 0.3558 0.2984 0.3144 0.0361  0.0085  -0.1253 98  LEU B CB  
702  C CG  . LEU A 117 ? 0.4066 0.3232 0.3518 0.0425  0.0134  -0.1493 98  LEU B CG  
703  C CD1 . LEU A 117 ? 0.411  0.3337 0.3383 0.0506  0.0237  -0.1459 98  LEU B CD1 
704  C CD2 . LEU A 117 ? 0.3981 0.323  0.3735 0.0301  0.0187  -0.1527 98  LEU B CD2 
705  N N   . LYS A 118 ? 0.4822 0.3729 0.3689 0.058   0.0172  -0.1835 99  LYS B N   
706  C CA  . LYS A 118 ? 0.5053 0.3841 0.3853 0.058   0.0084  -0.1904 99  LYS B CA  
707  C C   . LYS A 118 ? 0.5898 0.4956 0.4579 0.0725  0.0135  -0.1811 99  LYS B C   
708  O O   . LYS A 118 ? 0.6038 0.5054 0.4684 0.0736  0.0075  -0.1868 99  LYS B O   
709  C CB  . LYS A 118 ? 0.5093 0.3907 0.4158 0.0334  0.0028  -0.1943 99  LYS B CB  
710  C CG  . LYS A 118 ? 0.6882 0.5413 0.6056 0.0235  -0.0048 -0.1992 99  LYS B CG  
711  C CD  . LYS A 118 ? 0.7603 0.6272 0.7024 0.004   -0.0059 -0.1967 99  LYS B CD  
712  C CE  . LYS A 118 ? 0.8679 0.7139 0.824  -0.0025 -0.0129 -0.1941 99  LYS B CE  
713  N NZ  . LYS A 118 ? 0.9486 0.8131 0.924  -0.0145 -0.0121 -0.1882 99  LYS B NZ  
714  N N   . ALA A 119 ? 0.5544 0.4885 0.4179 0.0844  0.0244  -0.1645 100 ALA B N   
715  C CA  . ALA A 119 ? 0.5584 0.5282 0.416  0.101   0.0297  -0.1452 100 ALA B CA  
716  C C   . ALA A 119 ? 0.6014 0.6026 0.4883 0.0849  0.0223  -0.138  100 ALA B C   
717  O O   . ALA A 119 ? 0.6037 0.6242 0.4882 0.0961  0.0197  -0.132  100 ALA B O   
718  C CB  . ALA A 119 ? 0.6069 0.5613 0.4261 0.1331  0.0292  -0.1485 100 ALA B CB  
719  N N   . ALA A 120 ? 0.5419 0.5498 0.456  0.0607  0.017   -0.1375 101 ALA B N   
720  C CA  . ALA A 120 ? 0.5121 0.5475 0.4537 0.0432  0.0036  -0.1314 101 ALA B CA  
721  C C   . ALA A 120 ? 0.5549 0.6368 0.5108 0.0523  0.0003  -0.0993 101 ALA B C   
722  O O   . ALA A 120 ? 0.5556 0.6452 0.5014 0.0688  0.0114  -0.0804 101 ALA B O   
723  C CB  . ALA A 120 ? 0.5027 0.5281 0.4605 0.0231  -0.0036 -0.1374 101 ALA B CB  
724  N N   . PRO A 121 ? 0.4933 0.6082 0.4746 0.0416  -0.017  -0.0898 102 PRO B N   
725  C CA  . PRO A 121 ? 0.4715 0.6352 0.4742 0.0501  -0.0258 -0.0519 102 PRO B CA  
726  C C   . PRO A 121 ? 0.4799 0.6471 0.497  0.045   -0.0337 -0.0277 102 PRO B C   
727  O O   . PRO A 121 ? 0.4789 0.668  0.4995 0.0597  -0.029  0.0057  102 PRO B O   
728  C CB  . PRO A 121 ? 0.467  0.6603 0.4974 0.0342  -0.0485 -0.0533 102 PRO B CB  
729  C CG  . PRO A 121 ? 0.5219 0.678  0.5481 0.011   -0.0548 -0.0876 102 PRO B CG  
730  C CD  . PRO A 121 ? 0.4981 0.6096 0.4921 0.0205  -0.0316 -0.1108 102 PRO B CD  
731  N N   . ALA A 122 ? 0.4012 0.5451 0.4252 0.0265  -0.0466 -0.0424 103 ALA B N   
732  C CA  . ALA A 122 ? 0.3812 0.5171 0.416  0.0227  -0.0585 -0.0243 103 ALA B CA  
733  C C   . ALA A 122 ? 0.4142 0.5183 0.4294 0.0308  -0.0341 -0.0291 103 ALA B C   
734  O O   . ALA A 122 ? 0.4057 0.4948 0.4271 0.0285  -0.0408 -0.0182 103 ALA B O   
735  C CB  . ALA A 122 ? 0.3756 0.4983 0.4189 0.0063  -0.0835 -0.0396 103 ALA B CB  
736  N N   . ALA A 123 ? 0.3612 0.4533 0.3525 0.0412  -0.0089 -0.0452 104 ALA B N   
737  C CA  . ALA A 123 ? 0.3602 0.4264 0.3334 0.0481  0.0125  -0.0517 104 ALA B CA  
738  C C   . ALA A 123 ? 0.357  0.4376 0.3329 0.0582  0.0188  -0.0171 104 ALA B C   
739  O O   . ALA A 123 ? 0.3454 0.4598 0.3305 0.0669  0.0122  0.0128  104 ALA B O   
740  C CB  . ALA A 123 ? 0.394  0.4449 0.3401 0.059   0.0283  -0.0739 104 ALA B CB  
741  N N   . PHE A 124 ? 0.2762 0.333  0.2472 0.0566  0.0309  -0.0185 105 PHE B N   
742  C CA  . PHE A 124 ? 0.2508 0.3132 0.2238 0.063   0.0385  0.014   105 PHE B CA  
743  C C   . PHE A 124 ? 0.2834 0.3627 0.2317 0.0827  0.0577  0.0253  105 PHE B C   
744  O O   . PHE A 124 ? 0.2959 0.3576 0.2244 0.087   0.0573  0.0037  105 PHE B O   
745  C CB  . PHE A 124 ? 0.2616 0.2903 0.2351 0.0549  0.0482  0.0041  105 PHE B CB  
746  C CG  . PHE A 124 ? 0.2679 0.2933 0.2469 0.057   0.0539  0.038   105 PHE B CG  
747  C CD1 . PHE A 124 ? 0.2891 0.3178 0.2923 0.0535  0.0305  0.073   105 PHE B CD1 
748  C CD2 . PHE A 124 ? 0.2972 0.3131 0.2571 0.0619  0.0794  0.0365  105 PHE B CD2 
749  C CE1 . PHE A 124 ? 0.2925 0.3127 0.3025 0.0547  0.0339  0.1093  105 PHE B CE1 
750  C CE2 . PHE A 124 ? 0.3245 0.3345 0.2893 0.0618  0.0863  0.0695  105 PHE B CE2 
751  C CZ  . PHE A 124 ? 0.2869 0.2975 0.2776 0.058   0.0642  0.1071  105 PHE B CZ  
752  N N   . ASP A 125 ? 0.2221 0.3263 0.1773 0.0924  0.0584  0.0686  106 ASP B N   
753  C CA  . ASP A 125 ? 0.2361 0.3577 0.1744 0.1173  0.0697  0.0865  106 ASP B CA  
754  C C   . ASP A 125 ? 0.2684 0.3521 0.2039 0.1195  0.0723  0.0809  106 ASP B C   
755  O O   . ASP A 125 ? 0.2493 0.3335 0.22   0.12    0.0694  0.0977  106 ASP B O   
756  C CB  . ASP A 125 ? 0.2501 0.4219 0.2005 0.1285  0.0664  0.1435  106 ASP B CB  
757  C CG  . ASP A 125 ? 0.4556 0.6569 0.3769 0.1604  0.0849  0.1689  106 ASP B CG  
758  O OD1 . ASP A 125 ? 0.4899 0.6798 0.3719 0.1775  0.0982  0.1378  106 ASP B OD1 
759  O OD2 . ASP A 125 ? 0.5681 0.803  0.5047 0.171   0.0835  0.2228  106 ASP B OD2 
760  N N   . TRP A 126 ? 0.2441 0.2844 0.1692 0.1171  0.0507  0.0585  107 TRP B N   
761  C CA  . TRP A 126 ? 0.2496 0.2583 0.1651 0.1134  0.053   0.0543  107 TRP B CA  
762  C C   . TRP A 126 ? 0.3176 0.355  0.1943 0.1497  0.0802  0.0661  107 TRP B C   
763  O O   . TRP A 126 ? 0.3305 0.3442 0.2029 0.1496  0.0782  0.0652  107 TRP B O   
764  C CB  . TRP A 126 ? 0.2392 0.2224 0.1463 0.0894  0.047   0.0266  107 TRP B CB  
765  C CG  . TRP A 126 ? 0.2191 0.1926 0.1413 0.0625  0.0535  0.009   107 TRP B CG  
766  C CD1 . TRP A 126 ? 0.2276 0.2155 0.147  0.0613  0.0679  -0.021  107 TRP B CD1 
767  C CD2 . TRP A 126 ? 0.2032 0.152  0.1413 0.0427  0.0535  0.0131  107 TRP B CD2 
768  N NE1 . TRP A 126 ? 0.2013 0.1758 0.143  0.0408  0.0658  -0.0265 107 TRP B NE1 
769  C CE2 . TRP A 126 ? 0.208  0.1698 0.1455 0.0409  0.0835  -0.0223 107 TRP B CE2 
770  C CE3 . TRP A 126 ? 0.2134 0.1445 0.1482 0.0448  0.0646  0.021   107 TRP B CE3 
771  C CZ2 . TRP A 126 ? 0.1855 0.1253 0.1458 0.0181  0.0753  -0.0149 107 TRP B CZ2 
772  C CZ3 . TRP A 126 ? 0.201  0.1125 0.1464 0.027   0.0764  0.0135  107 TRP B CZ3 
773  C CH2 . TRP A 126 ? 0.1833 0.0995 0.1431 0.0125  0.0782  -0.0002 107 TRP B CH2 
774  N N   . SER A 127 ? 0.2781 0.3498 0.1654 0.1777  0.0706  0.0853  108 SER B N   
775  C CA  . SER A 127 ? 0.2991 0.3975 0.1611 0.2185  0.0834  0.1027  108 SER B CA  
776  C C   . SER A 127 ? 0.3418 0.4428 0.2136 0.224   0.0955  0.1194  108 SER B C   
777  O O   . SER A 127 ? 0.3731 0.4579 0.221  0.2347  0.0928  0.1111  108 SER B O   
778  C CB  . SER A 127 ? 0.3498 0.5099 0.2025 0.2465  0.0987  0.1269  108 SER B CB  
779  O OG  . SER A 127 ? 0.4384 0.6512 0.2537 0.2342  0.1355  0.1834  108 SER B OG  
780  N N   . PRO A 128 ? 0.2866 0.3966 0.2003 0.199   0.0994  0.1306  109 PRO B N   
781  C CA  . PRO A 128 ? 0.277  0.3862 0.1962 0.2054  0.1104  0.1435  109 PRO B CA  
782  C C   . PRO A 128 ? 0.2889 0.3394 0.1864 0.1918  0.1051  0.1198  109 PRO B C   
783  O O   . PRO A 128 ? 0.2988 0.3416 0.1863 0.1981  0.1078  0.1201  109 PRO B O   
784  C CB  . PRO A 128 ? 0.2645 0.4021 0.2319 0.1913  0.117   0.1664  109 PRO B CB  
785  C CG  . PRO A 128 ? 0.2846 0.4627 0.2712 0.1946  0.118   0.1838  109 PRO B CG  
786  C CD  . PRO A 128 ? 0.2736 0.4014 0.2253 0.1775  0.0976  0.1389  109 PRO B CD  
787  N N   . VAL A 129 ? 0.2403 0.2486 0.1594 0.1281  0.0731  0.0755  110 VAL B N   
788  C CA  . VAL A 129 ? 0.227  0.1983 0.1428 0.1028  0.0634  0.0552  110 VAL B CA  
789  C C   . VAL A 129 ? 0.2756 0.2399 0.1521 0.1319  0.0643  0.0562  110 VAL B C   
790  O O   . VAL A 129 ? 0.2728 0.2272 0.1498 0.1212  0.0582  0.0483  110 VAL B O   
791  C CB  . VAL A 129 ? 0.2271 0.171  0.1452 0.0858  0.0656  0.0476  110 VAL B CB  
792  C CG1 . VAL A 129 ? 0.2122 0.1267 0.1267 0.0624  0.0624  0.0329  110 VAL B CG1 
793  C CG2 . VAL A 129 ? 0.2032 0.1531 0.1464 0.0738  0.069   0.0495  110 VAL B CG2 
794  N N   . VAL A 130 ? 0.2644 0.2455 0.1421 0.1319  0.0524  0.0488  111 VAL B N   
795  C CA  . VAL A 130 ? 0.2932 0.2716 0.1347 0.1602  0.047   0.0439  111 VAL B CA  
796  C C   . VAL A 130 ? 0.364  0.3533 0.1604 0.2153  0.0615  0.06    111 VAL B C   
797  O O   . VAL A 130 ? 0.3862 0.3604 0.1593 0.2256  0.0535  0.0505  111 VAL B O   
798  C CB  . VAL A 130 ? 0.3281 0.316  0.1444 0.1877  0.0444  0.043   111 VAL B CB  
799  C CG1 . VAL A 130 ? 0.3686 0.3514 0.1473 0.2179  0.0346  0.0332  111 VAL B CG1 
800  C CG2 . VAL A 130 ? 0.2929 0.268  0.1381 0.1484  0.0328  0.0301  111 VAL B CG2 
801  N N   . THR A 131 ? 0.3368 0.3581 0.1519 0.2207  0.0731  0.0767  112 THR B N   
802  C CA  . THR A 131 ? 0.3629 0.4065 0.1527 0.2626  0.0872  0.0947  112 THR B CA  
803  C C   . THR A 131 ? 0.3795 0.4012 0.1681 0.2552  0.09    0.094   112 THR B C   
804  O O   . THR A 131 ? 0.4054 0.4235 0.1596 0.2844  0.0905  0.0934  112 THR B O   
805  C CB  . THR A 131 ? 0.4285 0.5362 0.2102 0.3211  0.1205  0.1424  112 THR B CB  
806  O OG1 . THR A 131 ? 0.4331 0.5701 0.197  0.3446  0.1238  0.1485  112 THR B OG1 
807  C CG2 . THR A 131 ? 0.4599 0.6065 0.218  0.3735  0.1418  0.1724  112 THR B CG2 
808  N N   . TYR A 132 ? 0.3032 0.3071 0.1517 0.1864  0.078   0.0788  113 TYR B N   
809  C CA  . TYR A 132 ? 0.2884 0.2714 0.1506 0.1618  0.0747  0.0709  113 TYR B CA  
810  C C   . TYR A 132 ? 0.2935 0.2524 0.1343 0.1603  0.0647  0.0569  113 TYR B C   
811  O O   . TYR A 132 ? 0.2933 0.2499 0.1294 0.1617  0.0622  0.0544  113 TYR B O   
812  C CB  . TYR A 132 ? 0.2678 0.2365 0.1599 0.1303  0.0757  0.0671  113 TYR B CB  
813  C CG  . TYR A 132 ? 0.2732 0.2188 0.165  0.124   0.0842  0.0677  113 TYR B CG  
814  C CD1 . TYR A 132 ? 0.29   0.2488 0.1822 0.1488  0.1037  0.0904  113 TYR B CD1 
815  C CD2 . TYR A 132 ? 0.2601 0.178  0.1578 0.0908  0.0735  0.0474  113 TYR B CD2 
816  C CE1 . TYR A 132 ? 0.2846 0.2207 0.1829 0.1328  0.1061  0.0836  113 TYR B CE1 
817  C CE2 . TYR A 132 ? 0.2599 0.1632 0.1647 0.0739  0.0753  0.0407  113 TYR B CE2 
818  C CZ  . TYR A 132 ? 0.3137 0.1926 0.1879 0.1205  0.1166  0.0719  113 TYR B CZ  
819  O OH  . TYR A 132 ? 0.3281 0.1889 0.2111 0.097   0.1166  0.0599  113 TYR B OH  
820  N N   . VAL A 133 ? 0.247  0.2037 0.1132 0.124   0.045   0.0378  114 VAL B N   
821  C CA  . VAL A 133 ? 0.2432 0.191  0.1049 0.1167  0.0327  0.0262  114 VAL B CA  
822  C C   . VAL A 133 ? 0.3295 0.2676 0.0992 0.2032  0.0383  0.0329  114 VAL B C   
823  O O   . VAL A 133 ? 0.3233 0.258  0.0963 0.1952  0.0286  0.0242  114 VAL B O   
824  C CB  . VAL A 133 ? 0.2341 0.1722 0.0941 0.1099  0.0272  0.0206  114 VAL B CB  
825  C CG1 . VAL A 133 ? 0.2315 0.1732 0.0947 0.1047  0.0121  0.0092  114 VAL B CG1 
826  C CG2 . VAL A 133 ? 0.194  0.1433 0.1175 0.0517  0.0231  0.0144  114 VAL B CG2 
827  N N   . CYS A 134 ? 0.3577 0.3102 0.0969 0.2429  0.0433  0.0393  115 CYS B N   
828  C CA  . CYS A 134 ? 0.4228 0.3776 0.101  0.3034  0.0407  0.0377  115 CYS B CA  
829  C C   . CYS A 134 ? 0.4771 0.4356 0.113  0.351   0.0553  0.0521  115 CYS B C   
830  O O   . CYS A 134 ? 0.5058 0.4521 0.1078 0.3746  0.0422  0.0393  115 CYS B O   
831  C CB  . CYS A 134 ? 0.4542 0.4279 0.1026 0.3448  0.0488  0.0469  115 CYS B CB  
832  S SG  . CYS A 134 ? 0.4857 0.4427 0.127  0.3393  0.0315  0.0296  115 CYS B SG  
833  N N   . ASP A 135 ? 0.4408 0.4176 0.1154 0.33    0.0747  0.0722  116 ASP B N   
834  C CA  . ASP A 135 ? 0.4629 0.4476 0.1197 0.3577  0.0901  0.0882  116 ASP B CA  
835  C C   . ASP A 135 ? 0.518  0.4737 0.1544 0.3287  0.0867  0.066   116 ASP B C   
836  O O   . ASP A 135 ? 0.543  0.4959 0.1541 0.3587  0.0796  0.0649  116 ASP B O   
837  C CB  . ASP A 135 ? 0.4601 0.4698 0.1424 0.3535  0.119   0.1173  116 ASP B CB  
838  C CG  . ASP A 135 ? 0.683  0.7621 0.2129 0.3845  0.1969  0.1504  116 ASP B CG  
839  O OD1 . ASP A 135 ? 0.744  0.8486 0.198  0.4374  0.2046  0.1603  116 ASP B OD1 
840  O OD2 . ASP A 135 ? 0.7534 0.8594 0.2478 0.3534  0.2432  0.1802  116 ASP B OD2 
841  N N   . LEU A 136 ? 0.4338 0.3675 0.1263 0.266   0.0757  0.0541  117 LEU B N   
842  C CA  . LEU A 136 ? 0.4136 0.3285 0.1186 0.2256  0.0677  0.0346  117 LEU B CA  
843  C C   . LEU A 136 ? 0.4957 0.4098 0.1563 0.2482  0.0502  0.0103  117 LEU B C   
844  O O   . LEU A 136 ? 0.4929 0.402  0.157  0.2466  0.0399  0.0063  117 LEU B O   
845  C CB  . LEU A 136 ? 0.3647 0.2678 0.1191 0.1637  0.0666  0.0226  117 LEU B CB  
846  C CG  . LEU A 136 ? 0.3916 0.2884 0.1478 0.1413  0.1002  0.0264  117 LEU B CG  
847  C CD1 . LEU A 136 ? 0.3484 0.2343 0.1409 0.0917  0.0993  0.0073  117 LEU B CD1 
848  C CD2 . LEU A 136 ? 0.424  0.3074 0.1815 0.1367  0.1167  0.0377  117 LEU B CD2 
849  N N   . GLU A 137 ? 0.4912 0.4057 0.1427 0.2672  0.0327  0.0028  118 GLU B N   
850  C CA  . GLU A 137 ? 0.5292 0.4322 0.1411 0.2925  0.0082  -0.0229 118 GLU B CA  
851  C C   . GLU A 137 ? 0.6761 0.5672 0.1417 0.3693  0.0176  -0.0473 118 GLU B C   
852  O O   . GLU A 137 ? 0.7211 0.5879 0.1395 0.401   -0.011  -0.0717 118 GLU B O   
853  C CB  . GLU A 137 ? 0.5411 0.4394 0.1519 0.286   -0.0013 -0.0384 118 GLU B CB  
854  C CG  . GLU A 137 ? 0.6085 0.506  0.1846 0.236   0.036   -0.09   118 GLU B CG  
855  C CD  . GLU A 137 ? 0.7916 0.6548 0.2287 0.2484  0.0678  -0.1916 118 GLU B CD  
856  O OE1 . GLU A 137 ? 0.8308 0.6756 0.2332 0.2831  0.0413  -0.1946 118 GLU B OE1 
857  O OE2 . GLU A 137 ? 0.4084 0.3161 0.0959 0.1746  0.0152  -0.0942 118 GLU B OE2 
858  N N   . GLY A 138 ? 0.6644 0.572  0.1262 0.395   0.0361  -0.0174 119 GLY B N   
859  C CA  . GLY A 138 ? 0.732  0.6384 0.1119 0.4666  0.0347  -0.0146 119 GLY B CA  
860  C C   . GLY A 138 ? 0.8573 0.7754 0.1116 0.5294  0.0564  -0.0155 119 GLY B C   
861  O O   . GLY A 138 ? 0.9175 0.8296 0.1015 0.5956  0.046   -0.0141 119 GLY B O   
862  N N   . ASN A 139 ? 0.8033 0.7392 0.1109 0.5079  0.0681  0.0001  120 ASN B N   
863  C CA  . ASN A 139 ? 0.8425 0.797  0.1026 0.5557  0.0783  0.014   120 ASN B CA  
864  C C   . ASN A 139 ? 0.9586 0.8738 0.0991 0.605   0.0525  -0.0247 120 ASN B C   
865  O O   . ASN A 139 ? 1.008  0.9311 0.0891 0.6694  0.0517  -0.0104 120 ASN B O   
866  C CB  . ASN A 139 ? 0.9012 0.9045 0.1056 0.6021  0.1165  0.0565  120 ASN B CB  
867  C CG  . ASN A 139 ? 1.1971 1.2519 0.282  0.5644  0.1957  0.0849  120 ASN B CG  
868  O OD1 . ASN A 139 ? 1.0892 1.1626 0.2365 0.5447  0.2002  0.0984  120 ASN B OD1 
869  N ND2 . ASN A 139 ? 1.1184 1.1881 0.2083 0.5517  0.2185  0.1102  120 ASN B ND2 
870  N N   . ARG A 140 ? 0.9049 0.7768 0.1011 0.5732  0.0118  -0.0549 121 ARG B N   
871  C CA  . ARG A 140 ? 0.9567 0.7784 0.0976 0.6101  -0.0302 -0.0858 121 ARG B CA  
872  C C   . ARG A 140 ? 1.004  0.8221 0.1104 0.6205  -0.0253 -0.0934 121 ARG B C   
873  O O   . ARG A 140 ? 1.0579 0.8469 0.113  0.6768  -0.0501 -0.0982 121 ARG B O   
874  C CB  . ARG A 140 ? 0.9354 0.7211 0.1171 0.5668  -0.0653 -0.1165 121 ARG B CB  
875  C CG  . ARG A 140 ? 1.0798 0.8524 0.1463 0.5671  -0.0646 -0.1553 121 ARG B CG  
876  C CD  . ARG A 140 ? 1.1925 0.9235 0.2037 0.5289  -0.0951 -0.2207 121 ARG B CD  
877  N NE  . ARG A 140 ? 1.1865 0.9288 0.2141 0.4986  -0.0924 -0.2296 121 ARG B NE  
878  C CZ  . ARG A 140 ? 1.3386 1.0532 0.2505 0.5307  -0.1231 -0.2602 121 ARG B CZ  
879  N NH1 . ARG A 140 ? 1.1288 0.8253 0.1858 0.5979  -0.1658 -0.1961 121 ARG B NH1 
880  N NH2 . ARG A 140 ? 1.1172 0.8634 0.2191 0.4937  -0.1242 -0.215  121 ARG B NH2 
881  N N   . VAL A 141 ? 0.895  0.7425 0.1023 0.5638  -0.0057 -0.0771 122 VAL B N   
882  C CA  . VAL A 141 ? 0.8851 0.7366 0.1043 0.5595  -0.001  -0.0776 122 VAL B CA  
883  C C   . VAL A 141 ? 0.8882 0.7996 0.124  0.5451  0.0475  -0.0476 122 VAL B C   
884  O O   . VAL A 141 ? 0.8504 0.7931 0.1144 0.5255  0.0716  -0.0243 122 VAL B O   
885  C CB  . VAL A 141 ? 0.9042 0.7196 0.1387 0.5117  -0.0163 -0.1204 122 VAL B CB  
886  C CG1 . VAL A 141 ? 0.9467 0.7029 0.1449 0.5277  -0.0648 -0.1515 122 VAL B CG1 
887  C CG2 . VAL A 141 ? 0.8243 0.6659 0.1388 0.4434  0.0066  -0.1184 122 VAL B CG2 
888  N N   . LYS A 142 ? 0.8373 0.763  0.1127 0.5498  0.0456  -0.0329 123 LYS B N   
889  C CA  . LYS A 142 ? 0.7924 0.7747 0.1147 0.5334  0.0773  0.0017  123 LYS B CA  
890  C C   . LYS A 142 ? 0.7948 0.7732 0.153  0.4733  0.0889  -0.0241 123 LYS B C   
891  O O   . LYS A 142 ? 0.7945 0.7279 0.1597 0.4522  0.0658  -0.0614 123 LYS B O   
892  C CB  . LYS A 142 ? 0.8569 0.8686 0.1281 0.5895  0.0873  0.0215  123 LYS B CB  
893  C CG  . LYS A 142 ? 1.0443 1.091  0.2052 0.6514  0.1127  0.052   123 LYS B CG  
894  C CD  . LYS A 142 ? 1.1488 1.2391 0.2991 0.702   0.1184  0.0877  123 LYS B CD  
895  C CE  . LYS A 142 ? 1.3147 1.4407 0.3955 0.7703  0.1307  0.1293  123 LYS B CE  
896  N NZ  . LYS A 142 ? 1.3832 1.5673 0.4957 0.7511  0.163   0.1802  123 LYS B NZ  
897  N N   . GLY A 143 ? 0.709  0.7321 0.1409 0.4456  0.1047  0.0114  124 GLY B N   
898  C CA  . GLY A 143 ? 0.6519 0.6776 0.1485 0.3915  0.1076  0.0018  124 GLY B CA  
899  C C   . GLY A 143 ? 0.6963 0.6905 0.182  0.3817  0.0973  -0.0415 124 GLY B C   
900  O O   . GLY A 143 ? 0.6627 0.6283 0.1828 0.342   0.087   -0.0675 124 GLY B O   
901  N N   . PRO A 144 ? 0.68   0.6759 0.1631 0.4109  0.0799  -0.0326 125 PRO B N   
902  C CA  . PRO A 144 ? 0.6758 0.6354 0.1737 0.395   0.0593  -0.0637 125 PRO B CA  
903  C C   . PRO A 144 ? 0.7276 0.6241 0.1951 0.3945  0.0343  -0.1021 125 PRO B C   
904  O O   . PRO A 144 ? 0.6957 0.5669 0.203  0.3584  0.0191  -0.1205 125 PRO B O   
905  C CB  . PRO A 144 ? 0.7275 0.7012 0.1884 0.4405  0.0627  -0.0584 125 PRO B CB  
906  C CG  . PRO A 144 ? 0.7776 0.8147 0.2324 0.4666  0.0863  -0.0127 125 PRO B CG  
907  C CD  . PRO A 144 ? 0.7262 0.7606 0.1678 0.4643  0.0923  -0.0027 125 PRO B CD  
908  N N   . GLU A 145 ? 0.7126 0.5912 0.1521 0.4263  0.0092  -0.0864 126 GLU B N   
909  C CA  . GLU A 145 ? 0.7368 0.5612 0.1548 0.4282  -0.0246 -0.1108 126 GLU B CA  
910  C C   . GLU A 145 ? 0.7267 0.5495 0.1842 0.3768  -0.018  -0.1284 126 GLU B C   
911  O O   . GLU A 145 ? 0.727  0.5162 0.2015 0.3549  -0.0401 -0.1509 126 GLU B O   
912  C CB  . GLU A 145 ? 0.8133 0.6193 0.1522 0.4856  -0.0345 -0.1124 126 GLU B CB  
913  C CG  . GLU A 145 ? 1.0172 0.741  0.249  0.5168  -0.0618 -0.1767 126 GLU B CG  
914  C CD  . GLU A 145 ? 1.3112 1.011  0.4531 0.5767  -0.0825 -0.1779 126 GLU B CD  
915  O OE1 . GLU A 145 ? 1.1933 0.9246 0.2913 0.6228  -0.0637 -0.1532 126 GLU B OE1 
916  O OE2 . GLU A 145 ? 1.2623 0.9132 0.3775 0.5796  -0.1206 -0.2015 126 GLU B OE2 
917  N N   . LYS A 146 ? 0.6201 0.4909 0.1545 0.347   -0.0114 -0.0792 127 LYS B N   
918  C CA  . LYS A 146 ? 0.5572 0.4393 0.1579 0.2944  -0.0116 -0.0733 127 LYS B CA  
919  C C   . LYS A 146 ? 0.536  0.4218 0.1818 0.2527  -0.0069 -0.0853 127 LYS B C   
920  O O   . LYS A 146 ? 0.5185 0.3936 0.1937 0.2259  -0.0207 -0.0973 127 LYS B O   
921  C CB  . LYS A 146 ? 0.554  0.4648 0.1574 0.2888  0.0204  -0.0583 127 LYS B CB  
922  C CG  . LYS A 146 ? 0.5155 0.4335 0.1652 0.2384  0.0342  -0.065  127 LYS B CG  
923  C CD  . LYS A 146 ? 0.5771 0.4848 0.2006 0.2387  0.0386  -0.0811 127 LYS B CD  
924  C CE  . LYS A 146 ? 0.6168 0.4955 0.2207 0.2354  0.019   -0.1216 127 LYS B CE  
925  N NZ  . LYS A 146 ? 0.5441 0.4381 0.2166 0.2131  -0.0077 -0.0863 127 LYS B NZ  
926  N N   . GLU A 147 ? 0.4583 0.3729 0.1542 0.2388  -0.0095 -0.0493 128 GLU B N   
927  C CA  . GLU A 147 ? 0.4116 0.3364 0.1577 0.1999  -0.011  -0.0486 128 GLU B CA  
928  C C   . GLU A 147 ? 0.473  0.3617 0.1882 0.2076  -0.0188 -0.0894 128 GLU B C   
929  O O   . GLU A 147 ? 0.4223 0.3179 0.1876 0.1714  -0.0265 -0.0867 128 GLU B O   
930  C CB  . GLU A 147 ? 0.4101 0.3568 0.1585 0.206   0.0036  -0.0395 128 GLU B CB  
931  C CG  . GLU A 147 ? 0.4698 0.4404 0.1965 0.2133  0.0464  -0.0445 128 GLU B CG  
932  C CD  . GLU A 147 ? 0.6797 0.6864 0.3759 0.2261  0.0963  -0.0649 128 GLU B CD  
933  O OE1 . GLU A 147 ? 0.5106 0.5139 0.2228 0.2206  0.084   -0.0747 128 GLU B OE1 
934  O OE2 . GLU A 147 ? 0.6693 0.7083 0.3815 0.2225  0.1102  -0.033  128 GLU B OE2 
935  N N   . GLU A 148 ? 0.4881 0.3552 0.1651 0.2426  -0.0401 -0.0863 129 GLU B N   
936  C CA  . GLU A 148 ? 0.5126 0.3431 0.1791 0.2453  -0.0649 -0.1032 129 GLU B CA  
937  C C   . GLU A 148 ? 0.5429 0.3447 0.206  0.2378  -0.0798 -0.1255 129 GLU B C   
938  O O   . GLU A 148 ? 0.5327 0.3209 0.2229 0.216   -0.0914 -0.1349 129 GLU B O   
939  C CB  . GLU A 148 ? 0.5901 0.3801 0.183  0.2974  -0.0766 -0.1199 129 GLU B CB  
940  C CG  . GLU A 148 ? 0.7575 0.4458 0.2791 0.3218  -0.0803 -0.2024 129 GLU B CG  
941  C CD  . GLU A 148 ? 1.0742 0.7548 0.6412 0.2858  -0.0709 -0.2179 129 GLU B CD  
942  O OE1 . GLU A 148 ? 0.8845 0.6134 0.4849 0.2667  -0.0432 -0.2069 129 GLU B OE1 
943  O OE2 . GLU A 148 ? 1.1052 0.7383 0.6827 0.2741  -0.0982 -0.2288 129 GLU B OE2 
944  N N   . LYS A 149 ? 0.4925 0.314  0.1652 0.2443  -0.0918 -0.0974 130 LYS B N   
945  C CA  . LYS A 149 ? 0.4787 0.2923 0.1687 0.2335  -0.1107 -0.103  130 LYS B CA  
946  C C   . LYS A 149 ? 0.4516 0.2958 0.2034 0.1867  -0.0919 -0.1056 130 LYS B C   
947  O O   . LYS A 149 ? 0.4423 0.2799 0.2186 0.1742  -0.1092 -0.1114 130 LYS B O   
948  C CB  . LYS A 149 ? 0.5353 0.3368 0.1838 0.2594  -0.1113 -0.1138 130 LYS B CB  
949  C CG  . LYS A 149 ? 0.6741 0.4063 0.2561 0.27    -0.1309 -0.1854 130 LYS B CG  
950  C CD  . LYS A 149 ? 0.7542 0.4466 0.2418 0.3087  -0.1426 -0.2218 130 LYS B CD  
951  C CE  . LYS A 149 ? 0.8735 0.5058 0.3214 0.3084  -0.1877 -0.2701 130 LYS B CE  
952  N NZ  . LYS A 149 ? 1.066  0.6834 0.4498 0.3391  -0.2103 -0.2799 130 LYS B NZ  
953  N N   . LEU A 150 ? 0.3403 0.2361 0.1442 0.1575  -0.0686 -0.0724 131 LEU B N   
954  C CA  . LEU A 150 ? 0.2788 0.2089 0.1437 0.1164  -0.0544 -0.0647 131 LEU B CA  
955  C C   . LEU A 150 ? 0.3153 0.2416 0.195  0.1059  -0.0561 -0.074  131 LEU B C   
956  O O   . LEU A 150 ? 0.2858 0.2282 0.2025 0.09    -0.0622 -0.0709 131 LEU B O   
957  C CB  . LEU A 150 ? 0.2426 0.1957 0.1289 0.096   -0.0313 -0.0496 131 LEU B CB  
958  C CG  . LEU A 150 ? 0.2286 0.2009 0.1564 0.0629  -0.0144 -0.0548 131 LEU B CG  
959  C CD1 . LEU A 150 ? 0.2099 0.1967 0.166  0.0519  -0.0198 -0.0594 131 LEU B CD1 
960  C CD2 . LEU A 150 ? 0.2145 0.1936 0.1527 0.0479  0.0003  -0.0399 131 LEU B CD2 
961  N N   . ARG A 151 ? 0.2984 0.2247 0.1704 0.1113  -0.0575 -0.0627 132 ARG B N   
962  C CA  . ARG A 151 ? 0.286  0.2126 0.1752 0.1004  -0.06   -0.0654 132 ARG B CA  
963  C C   . ARG A 151 ? 0.3745 0.2546 0.2403 0.1137  -0.081  -0.0929 132 ARG B C   
964  O O   . ARG A 151 ? 0.351  0.2423 0.2506 0.096   -0.0824 -0.0893 132 ARG B O   
965  C CB  . ARG A 151 ? 0.2963 0.2213 0.1711 0.1087  -0.0583 -0.0589 132 ARG B CB  
966  C CG  . ARG A 151 ? 0.3243 0.2659 0.2067 0.0991  -0.0348 -0.0608 132 ARG B CG  
967  C CD  . ARG A 151 ? 0.3692 0.3013 0.2262 0.1146  -0.0278 -0.0737 132 ARG B CD  
968  N NE  . ARG A 151 ? 0.3468 0.3079 0.2287 0.0996  -0.0148 -0.0619 132 ARG B NE  
969  C CZ  . ARG A 151 ? 0.4834 0.4251 0.2787 0.1473  0.0326  -0.1172 132 ARG B CZ  
970  N NH1 . ARG A 151 ? 0.383  0.339  0.1918 0.1575  -0.0024 -0.0616 132 ARG B NH1 
971  N NH2 . ARG A 151 ? 0.2767 0.2707 0.165  0.1031  -0.002  -0.0399 132 ARG B NH2 
972  N N   . GLN A 152 ? 0.3817 0.239  0.2141 0.1397  -0.1076 -0.0885 133 GLN B N   
973  C CA  . GLN A 152 ? 0.4153 0.2342 0.2346 0.1507  -0.1418 -0.0979 133 GLN B CA  
974  C C   . GLN A 152 ? 0.4427 0.2591 0.2896 0.1374  -0.1463 -0.1125 133 GLN B C   
975  O O   . GLN A 152 ? 0.4486 0.2458 0.3121 0.1316  -0.1686 -0.1153 133 GLN B O   
976  C CB  . GLN A 152 ? 0.4984 0.2574 0.2469 0.1921  -0.1719 -0.1147 133 GLN B CB  
977  C CG  . GLN A 152 ? 0.8264 0.4105 0.4421 0.2395  -0.1556 -0.2382 133 GLN B CG  
978  C CD  . GLN A 152 ? 1.1359 0.6887 0.781  0.2219  -0.1698 -0.2363 133 GLN B CD  
979  O OE1 . GLN A 152 ? 1.101  0.6113 0.7595 0.2157  -0.2064 -0.2342 133 GLN B OE1 
980  N NE2 . GLN A 152 ? 1.0381 0.6121 0.6957 0.2124  -0.1431 -0.2345 133 GLN B NE2 
981  N N   . ALA A 153 ? 0.3511 0.2273 0.2324 0.1278  -0.13   -0.0864 134 ALA B N   
982  C CA  . ALA A 153 ? 0.3099 0.2052 0.229  0.1155  -0.1314 -0.0889 134 ALA B CA  
983  C C   . ALA A 153 ? 0.3046 0.2167 0.264  0.0896  -0.1112 -0.0981 134 ALA B C   
984  O O   . ALA A 153 ? 0.2645 0.1801 0.2545 0.0856  -0.1257 -0.0978 134 ALA B O   
985  C CB  . ALA A 153 ? 0.303  0.2186 0.2233 0.1135  -0.1147 -0.089  134 ALA B CB  
986  N N   . VAL A 154 ? 0.2565 0.1967 0.2284 0.0742  -0.0824 -0.0886 135 VAL B N   
987  C CA  . VAL A 154 ? 0.2277 0.1913 0.2374 0.0543  -0.0643 -0.0893 135 VAL B CA  
988  C C   . VAL A 154 ? 0.318  0.2419 0.3233 0.0562  -0.0792 -0.1035 135 VAL B C   
989  O O   . VAL A 154 ? 0.3161 0.2391 0.3102 0.0571  -0.0776 -0.0943 135 VAL B O   
990  C CB  . VAL A 154 ? 0.2577 0.2277 0.2647 0.0411  -0.0339 -0.0977 135 VAL B CB  
991  C CG1 . VAL A 154 ? 0.2162 0.205  0.2576 0.0261  -0.0207 -0.0993 135 VAL B CG1 
992  C CG2 . VAL A 154 ? 0.2506 0.2357 0.2534 0.0379  -0.0229 -0.0912 135 VAL B CG2 
993  N N   . LYS A 155 ? 0.282  0.2059 0.316  0.0542  -0.0956 -0.1016 136 LYS B N   
994  C CA  . LYS A 155 ? 0.2937 0.1907 0.3375 0.0527  -0.1165 -0.0988 136 LYS B CA  
995  C C   . LYS A 155 ? 0.3057 0.2102 0.3782 0.0376  -0.0975 -0.1021 136 LYS B C   
996  O O   . LYS A 155 ? 0.3357 0.2313 0.4099 0.0346  -0.1025 -0.0932 136 LYS B O   
997  C CB  . LYS A 155 ? 0.349  0.197  0.3996 0.057   -0.159  -0.1067 136 LYS B CB  
998  C CG  . LYS A 155 ? 0.5791 0.2917 0.5611 0.0654  -0.193  -0.1691 136 LYS B CG  
999  C CD  . LYS A 155 ? 0.7524 0.4126 0.6802 0.0837  -0.2022 -0.1792 136 LYS B CD  
1000 C CE  . LYS A 155 ? 0.8814 0.4885 0.77   0.1074  -0.2486 -0.1847 136 LYS B CE  
1001 N NZ  . LYS A 155 ? 0.936  0.558  0.7944 0.1206  -0.245  -0.2005 136 LYS B NZ  
1002 N N   . GLN A 156 ? 0.1789 0.1492 0.286  0.0335  -0.0756 -0.0871 137 GLN B N   
1003 C CA  . GLN A 156 ? 0.1275 0.1378 0.2654 0.027   -0.0595 -0.0732 137 GLN B CA  
1004 C C   . GLN A 156 ? 0.1374 0.1552 0.2719 0.0171  -0.0317 -0.0882 137 GLN B C   
1005 O O   . GLN A 156 ? 0.1187 0.158  0.2549 0.0146  -0.0243 -0.0866 137 GLN B O   
1006 C CB  . GLN A 156 ? 0.1333 0.1307 0.2993 0.0261  -0.0728 -0.0692 137 GLN B CB  
1007 C CG  . GLN A 156 ? 0.2907 0.1672 0.4651 0.013   -0.119  -0.0908 137 GLN B CG  
1008 C CD  . GLN A 156 ? 0.5809 0.4895 0.8141 0.0113  -0.1383 -0.059  137 GLN B CD  
1009 O OE1 . GLN A 156 ? 0.5873 0.5294 0.8516 0.0116  -0.1265 -0.0368 137 GLN B OE1 
1010 N NE2 . GLN A 156 ? 0.4535 0.3547 0.7032 0.0118  -0.1711 -0.0535 137 GLN B NE2 
1011 N N   . VAL A 157 ? 0.1406 0.1633 0.2209 0.0064  -0.0117 -0.0446 138 VAL B N   
1012 C CA  . VAL A 157 ? 0.145  0.1643 0.199  0.0009  -0.0015 -0.0323 138 VAL B CA  
1013 C C   . VAL A 157 ? 0.1081 0.1321 0.1874 0.001   -0.0018 -0.0437 138 VAL B C   
1014 O O   . VAL A 157 ? 0.1156 0.1376 0.1976 0.0022  -0.0043 -0.0427 138 VAL B O   
1015 C CB  . VAL A 157 ? 0.1233 0.1662 0.2247 -0.0007 0.0011  -0.066  138 VAL B CB  
1016 C CG1 . VAL A 157 ? 0.1233 0.1652 0.2143 -0.0053 0.0078  -0.0625 138 VAL B CG1 
1017 C CG2 . VAL A 157 ? 0.1301 0.1777 0.2306 0.0013  -0.0019 -0.0692 138 VAL B CG2 
1018 N N   . LEU A 158 ? 0.1494 0.1494 0.1494 0       0       0       139 LEU B N   
1019 C CA  . LEU A 158 ? 0.1514 0.1514 0.1514 0       0       0       139 LEU B CA  
1020 C C   . LEU A 158 ? 0.1093 0.1093 0.1093 0       0       0       139 LEU B C   
1021 O O   . LEU A 158 ? 0.1144 0.1144 0.1144 0       0       0       139 LEU B O   
1022 C CB  . LEU A 158 ? 0.1475 0.1475 0.1475 0       0       0       139 LEU B CB  
1023 C CG  . LEU A 158 ? 0.1141 0.1155 0.1273 0.0005  -0.0016 -0.0045 139 LEU B CG  
1024 C CD1 . LEU A 158 ? 0.1222 0.1229 0.1387 0.0007  -0.0026 -0.0044 139 LEU B CD1 
1025 C CD2 . LEU A 158 ? 0.11   0.1122 0.161  0.0021  -0.0082 -0.0136 139 LEU B CD2 
1026 N N   . LYS A 159 ? 0.061  0.061  0.061  0       0       0       140 LYS B N   
1027 C CA  . LYS A 159 ? 0.0533 0.0533 0.0533 0       0       0       140 LYS B CA  
1028 C C   . LYS A 159 ? 0.0943 0.0943 0.0943 0       0       0       140 LYS B C   
1029 O O   . LYS A 159 ? 0.0658 0.0658 0.0658 0       0       0       140 LYS B O   
1030 C CB  . LYS A 159 ? 0.1017 0.1017 0.1017 0       0       0       140 LYS B CB  
1031 C CG  . LYS A 159 ? 0.1142 0.1891 0.2429 0.0904  0.0307  -0.0421 140 LYS B CG  
1032 C CD  . LYS A 159 ? 0.3223 0.3902 0.4396 0.1177  0.0339  -0.0608 140 LYS B CD  
1033 C CE  . LYS A 159 ? 0.4944 0.5825 0.6255 0.1833  0.0437  -0.0605 140 LYS B CE  
1034 N NZ  . LYS A 159 ? 0.5919 0.681  0.732  0.2043  0.0532  -0.0624 140 LYS B NZ  
1035 N N   A CYS A 160 ? 0.0495 0.0495 0.0495 0       0       0       141 CYS B N   
1036 N N   B CYS A 160 ? 0.0793 0.0793 0.0793 0       0       0       141 CYS B N   
1037 C CA  A CYS A 160 ? 0.038  0.038  0.038  0       0       0       141 CYS B CA  
1038 C CA  B CYS A 160 ? 0.0834 0.0834 0.0834 0       0       0       141 CYS B CA  
1039 C C   A CYS A 160 ? 0.0812 0.0812 0.0812 0       0       0       141 CYS B C   
1040 C C   B CYS A 160 ? 0.0896 0.0896 0.0896 0       0       0       141 CYS B C   
1041 O O   A CYS A 160 ? 0.0712 0.0712 0.0712 0       0       0       141 CYS B O   
1042 O O   B CYS A 160 ? 0.0915 0.0915 0.0915 0       0       0       141 CYS B O   
1043 C CB  A CYS A 160 ? 0.038  0.038  0.038  0       0       0       141 CYS B CB  
1044 C CB  B CYS A 160 ? 0.1034 0.1034 0.1034 0       0       0       141 CYS B CB  
1045 S SG  A CYS A 160 ? 0.058  0.058  0.058  0       0       0       141 CYS B SG  
1046 S SG  B CYS A 160 ? 0.0766 0.0766 0.0766 0       0       0       141 CYS B SG  
1047 N N   . ASP A 161 ? 0.038  0.038  0.038  0       0       0       142 ASP B N   
1048 C CA  . ASP A 161 ? 0.038  0.038  0.038  0       0       0       142 ASP B CA  
1049 C C   . ASP A 161 ? 0.0746 0.0746 0.0746 0       0       0       142 ASP B C   
1050 O O   . ASP A 161 ? 0.047  0.047  0.047  0       0       0       142 ASP B O   
1051 C CB  . ASP A 161 ? 0.0454 0.0454 0.0454 0       0       0       142 ASP B CB  
1052 C CG  . ASP A 161 ? 0.0755 0.0755 0.0755 0       0       0       142 ASP B CG  
1053 O OD1 . ASP A 161 ? 0.0529 0.0529 0.0529 0       0       0       142 ASP B OD1 
1054 O OD2 . ASP A 161 ? 0.038  0.038  0.038  0       0       0       142 ASP B OD2 
1055 N N   . VAL A 162 ? 0.038  0.038  0.038  0       0       0       143 VAL B N   
1056 C CA  . VAL A 162 ? 0.038  0.038  0.038  0       0       0       143 VAL B CA  
1057 C C   . VAL A 162 ? 0.064  0.064  0.064  0       0       0       143 VAL B C   
1058 O O   . VAL A 162 ? 0.038  0.038  0.038  0       0       0       143 VAL B O   
1059 C CB  . VAL A 162 ? 0.0527 0.0527 0.0527 0       0       0       143 VAL B CB  
1060 C CG1 . VAL A 162 ? 0.038  0.038  0.038  0       0       0       143 VAL B CG1 
1061 C CG2 . VAL A 162 ? 0.0453 0.0453 0.0453 0       0       0       143 VAL B CG2 
1062 N N   . THR A 163 ? 0.038  0.038  0.038  0       0       0       144 THR B N   
1063 C CA  . THR A 163 ? 0.038  0.038  0.038  0       0       0       144 THR B CA  
1064 C C   . THR A 163 ? 0.0579 0.0579 0.0579 0       0       0       144 THR B C   
1065 O O   . THR A 163 ? 0.038  0.038  0.038  0       0       0       144 THR B O   
1066 C CB  . THR A 163 ? 0.0656 0.0656 0.0656 0       0       0       144 THR B CB  
1067 O OG1 . THR A 163 ? 0.0587 0.0587 0.0587 0       0       0       144 THR B OG1 
1068 C CG2 . THR A 163 ? 0.058  0.058  0.058  0       0       0       144 THR B CG2 
1069 N N   . GLN A 164 ? 0.038  0.038  0.038  0       0       0       145 GLN B N   
1070 C CA  . GLN A 164 ? 0.038  0.038  0.038  0       0       0       145 GLN B CA  
1071 C C   . GLN A 164 ? 0.0829 0.0829 0.0829 0       0       0       145 GLN B C   
1072 O O   . GLN A 164 ? 0.0444 0.0444 0.0444 0       0       0       145 GLN B O   
1073 C CB  . GLN A 164 ? 0.0472 0.0476 0.0479 0.0005  0.0005  0.0009  145 GLN B CB  
1074 C CG  . GLN A 164 ? 0.1433 0.1489 0.1456 0.006   0.0049  0.0076  145 GLN B CG  
1075 C CD  . GLN A 164 ? 0.2177 0.353  0.3005 0.1319  0.0692  0.0841  145 GLN B CD  
1076 O OE1 . GLN A 164 ? 0.2594 0.3601 0.2805 0.1239  0.0626  0.0754  145 GLN B OE1 
1077 N NE2 . GLN A 164 ? 0.2052 0.3058 0.2216 0.0936  0.0636  0.1064  145 GLN B NE2 
1078 N N   . SER A 165 ? 0.0427 0.0551 0.0711 0.0081  0.0114  0.0231  146 SER B N   
1079 C CA  . SER A 165 ? 0.0412 0.0569 0.0873 0.0078  0.0126  0.0305  146 SER B CA  
1080 C C   . SER A 165 ? 0.0791 0.0911 0.1268 0.0048  0.0092  0.0261  146 SER B C   
1081 O O   . SER A 165 ? 0.0539 0.0609 0.0997 0.0022  0.0054  0.0189  146 SER B O   
1082 C CB  . SER A 165 ? 0.0816 0.1333 0.1727 0.0209  0.027   0.0763  146 SER B CB  
1083 O OG  . SER A 165 ? 0.0802 0.1433 0.1741 0.0298  0.0354  0.089   146 SER B OG  
1084 N N   . GLN A 166 ? 0.0404 0.0574 0.0919 0.0068  0.0114  0.0324  147 GLN B N   
1085 C CA  . GLN A 166 ? 0.0392 0.0521 0.0907 0.0041  0.0079  0.0273  147 GLN B CA  
1086 C C   . GLN A 166 ? 0.0769 0.0773 0.0796 0.0002  0.0005  0.0011  147 GLN B C   
1087 O O   . GLN A 166 ? 0.041  0.0427 0.0477 0.0009  0.0017  0.0039  147 GLN B O   
1088 C CB  . GLN A 166 ? 0.0533 0.0925 0.1503 0.0097  0.0151  0.0641  147 GLN B CB  
1089 C CG  . GLN A 166 ? 0.0818 0.2242 0.3712 0.0275  0.0267  0.1812  147 GLN B CG  
1090 C CD  . GLN A 166 ? 0.1823 0.5373 0.6664 0.1037  0.0249  0.2169  147 GLN B CD  
1091 O OE1 . GLN A 166 ? 0.1812 0.5195 0.6594 0.0892  0.0244  0.219   147 GLN B OE1 
1092 N NE2 . GLN A 166 ? 0.1561 0.4102 0.4757 0.0783  0.0541  0.2354  147 GLN B NE2 
1093 N N   . PRO A 167 ? 0.038  0.038  0.038  0       0       0       148 PRO B N   
1094 C CA  . PRO A 167 ? 0.038  0.038  0.038  0       0       0       148 PRO B CA  
1095 C C   . PRO A 167 ? 0.0925 0.0925 0.0925 0       0       0       148 PRO B C   
1096 O O   . PRO A 167 ? 0.0931 0.0931 0.0931 0       0       0       148 PRO B O   
1097 C CB  . PRO A 167 ? 0.0547 0.0547 0.0547 0       0       0       148 PRO B CB  
1098 C CG  . PRO A 167 ? 0.0712 0.0712 0.0712 0       0       0       148 PRO B CG  
1099 C CD  . PRO A 167 ? 0.0531 0.0531 0.0531 0       0       0       148 PRO B CD  
1100 N N   . LEU A 168 ? 0.085  0.085  0.085  0       0       0       149 LEU B N   
1101 C CA  . LEU A 168 ? 0.098  0.098  0.098  0       0       0       149 LEU B CA  
1102 C C   . LEU A 168 ? 0.1128 0.1177 0.172  0.0017  0.0057  0.0182  149 LEU B C   
1103 O O   . LEU A 168 ? 0.1147 0.1222 0.1937 0.0016  0.0052  0.025   149 LEU B O   
1104 C CB  . LEU A 168 ? 0.1021 0.1021 0.1021 0       0       0       149 LEU B CB  
1105 C CG  . LEU A 168 ? 0.1175 0.1175 0.1183 0       0       -0.0001 149 LEU B CG  
1106 C CD1 . LEU A 168 ? 0.1217 0.1223 0.1494 0.0004  -0.0026 -0.0048 149 LEU B CD1 
1107 C CD2 . LEU A 168 ? 0.0944 0.0992 0.1475 -0.0002 0.0005  -0.016  149 LEU B CD2 
1108 N N   . GLY A 169 ? 0.1362 0.1438 0.1702 0.0031  0.0062  0.0174  150 GLY B N   
1109 C CA  . GLY A 169 ? 0.1249 0.1618 0.2043 0.0141  0.02    0.0592  150 GLY B CA  
1110 C C   . GLY A 169 ? 0.0991 0.1838 0.289  0.02    0.0295  0.1317  150 GLY B C   
1111 O O   . GLY A 169 ? 0.094  0.1782 0.3075 0.0135  0.0213  0.1364  150 GLY B O   
1112 N N   . ALA A 170 ? 0.1086 0.199  0.2946 0.0193  0.0273  0.1338  151 ALA B N   
1113 C CA  . ALA A 170 ? 0.1149 0.2262 0.3552 0.0123  0.0181  0.165   151 ALA B CA  
1114 C C   . ALA A 170 ? 0.1277 0.2186 0.4166 -0.0022 -0.0039 0.162   151 ALA B C   
1115 O O   . ALA A 170 ? 0.1365 0.2382 0.4727 -0.0119 -0.0215 0.1865  151 ALA B O   
1116 C CB  . ALA A 170 ? 0.1232 0.2675 0.3738 0.0212  0.0279  0.1934  151 ALA B CB  
1117 N N   . VAL A 171 ? 0.1181 0.1627 0.3286 -0.0028 -0.0062 0.0971  152 VAL B N   
1118 C CA  . VAL A 171 ? 0.12   0.1414 0.3135 -0.0074 -0.0212 0.0682  152 VAL B CA  
1119 C C   . VAL A 171 ? 0.1042 0.1246 0.3559 -0.013  -0.0402 0.0831  152 VAL B C   
1120 O O   . VAL A 171 ? 0.1032 0.1178 0.3429 -0.0098 -0.0347 0.069   152 VAL B O   
1121 C CB  . VAL A 171 ? 0.1157 0.1224 0.3028 -0.0046 -0.0212 0.0413  152 VAL B CB  
1122 C CG1 . VAL A 171 ? 0.119  0.1149 0.3101 -0.0048 -0.038  0.025   152 VAL B CG1 
1123 C CG2 . VAL A 171 ? 0.1207 0.1285 0.2689 -0.0024 -0.0102 0.0357  152 VAL B CG2 
1124 N N   . PRO A 172 ? 0.0969 0.1141 0.3345 -0.0175 -0.052  0.0835  153 PRO B N   
1125 C CA  . PRO A 172 ? 0.1067 0.1171 0.3559 -0.021  -0.0661 0.0844  153 PRO B CA  
1126 C C   . PRO A 172 ? 0.116  0.1057 0.3491 -0.0173 -0.0771 0.0576  153 PRO B C   
1127 O O   . PRO A 172 ? 0.1162 0.0986 0.3212 -0.0142 -0.0766 0.0426  153 PRO B O   
1128 C CB  . PRO A 172 ? 0.1124 0.134  0.4425 -0.0357 -0.0972 0.1309  153 PRO B CB  
1129 C CG  . PRO A 172 ? 0.1232 0.1478 0.4859 -0.0403 -0.1082 0.1462  153 PRO B CG  
1130 C CD  . PRO A 172 ? 0.1034 0.1261 0.3742 -0.0241 -0.0662 0.1042  153 PRO B CD  
1131 N N   . LEU A 173 ? 0.1158 0.1042 0.2904 -0.0114 -0.0601 0.0368  154 LEU B N   
1132 C CA  . LEU A 173 ? 0.1066 0.0859 0.2607 -0.0068 -0.0633 0.019   154 LEU B CA  
1133 C C   . LEU A 173 ? 0.1279 0.0957 0.3311 -0.011  -0.0922 0.0284  154 LEU B C   
1134 O O   . LEU A 173 ? 0.1212 0.0977 0.3275 -0.0135 -0.0835 0.038   154 LEU B O   
1135 C CB  . LEU A 173 ? 0.0964 0.0852 0.1926 -0.0004 -0.0347 0.0013  154 LEU B CB  
1136 C CG  . LEU A 173 ? 0.1084 0.0974 0.2129 0.0021  -0.0364 -0.0067 154 LEU B CG  
1137 C CD1 . LEU A 173 ? 0.1027 0.0994 0.1793 0.0041  -0.0223 -0.0151 154 LEU B CD1 
1138 C CD2 . LEU A 173 ? 0.1069 0.0798 0.2613 0.0046  -0.0713 -0.0119 154 LEU B CD2 
1139 N N   . PRO A 174 ? 0.1194 0.0738 0.3098 -0.0087 -0.1059 0.0196  155 PRO B N   
1140 C CA  . PRO A 174 ? 0.1379 0.0802 0.3512 -0.0111 -0.1277 0.0236  155 PRO B CA  
1141 C C   . PRO A 174 ? 0.1291 0.0755 0.3589 -0.0048 -0.1239 0.0111  155 PRO B C   
1142 O O   . PRO A 174 ? 0.1148 0.079  0.2895 0.0024  -0.087  -0.0059 155 PRO B O   
1143 C CB  . PRO A 174 ? 0.1689 0.0815 0.3885 -0.0077 -0.1647 0.0144  155 PRO B CB  
1144 C CG  . PRO A 174 ? 0.1868 0.0855 0.4191 -0.0073 -0.1845 0.0132  155 PRO B CG  
1145 C CD  . PRO A 174 ? 0.1412 0.0826 0.3208 -0.0042 -0.1184 0.0084  155 PRO B CD  
1146 N N   . PRO A 175 ? 0.1183 0.0667 0.3518 -0.0073 -0.1228 0.017   156 PRO B N   
1147 C CA  . PRO A 175 ? 0.1166 0.0832 0.295  0       -0.0841 -0.0001 156 PRO B CA  
1148 C C   . PRO A 175 ? 0.103  0.0632 0.2933 0.0092  -0.0985 -0.0216 156 PRO B C   
1149 O O   . PRO A 175 ? 0.1244 0.0688 0.3104 0.0106  -0.1185 -0.0219 156 PRO B O   
1150 C CB  . PRO A 175 ? 0.1124 0.0657 0.3539 -0.0049 -0.1168 0.0122  156 PRO B CB  
1151 C CG  . PRO A 175 ? 0.1386 0.0741 0.4782 -0.0218 -0.171  0.0524  156 PRO B CG  
1152 C CD  . PRO A 175 ? 0.1414 0.0713 0.4433 -0.0204 -0.1689 0.0457  156 PRO B CD  
1153 N N   . ALA A 176 ? 0.1053 0.0947 0.193  0.0069  -0.0377 -0.0186 157 ALA B N   
1154 C CA  . ALA A 176 ? 0.0886 0.084  0.1492 0.0075  -0.0268 -0.0199 157 ALA B CA  
1155 C C   . ALA A 176 ? 0.0931 0.0895 0.1533 0.0088  -0.0277 -0.0227 157 ALA B C   
1156 O O   . ALA A 176 ? 0.0666 0.0637 0.1286 0.0078  -0.0258 -0.0215 157 ALA B O   
1157 C CB  . ALA A 176 ? 0.0919 0.0932 0.1134 0.0025  -0.0068 -0.0088 157 ALA B CB  
1158 N N   . ASP A 177 ? 0.0513 0.0478 0.1086 0.0114  -0.0307 -0.0263 158 ASP B N   
1159 C CA  . ASP A 177 ? 0.0516 0.0499 0.1063 0.0127  -0.0304 -0.0285 158 ASP B CA  
1160 C C   . ASP A 177 ? 0.0829 0.0867 0.1027 0.0038  -0.0073 -0.0117 158 ASP B C   
1161 O O   . ASP A 177 ? 0.069  0.0721 0.081  0.0021  -0.0038 -0.0074 158 ASP B O   
1162 C CB  . ASP A 177 ? 0.0883 0.0774 0.1526 0.0215  -0.0504 -0.0393 158 ASP B CB  
1163 C CG  . ASP A 177 ? 0.1648 0.0864 0.3284 0.0576  -0.1722 -0.0911 158 ASP B CG  
1164 O OD1 . ASP A 177 ? 0.2144 0.1086 0.3966 0.059   -0.2038 -0.091  158 ASP B OD1 
1165 O OD2 . ASP A 177 ? 0.2015 0.1098 0.3493 0.0556  -0.177  -0.0834 158 ASP B OD2 
1166 N N   . CYS A 178 ? 0.0381 0.0384 0.0392 0.0002  -0.0003 -0.0007 159 CYS B N   
1167 C CA  . CYS A 178 ? 0.0389 0.0389 0.0389 0       0       0       159 CYS B CA  
1168 C C   . CYS A 178 ? 0.0708 0.0708 0.0708 0       0       0       159 CYS B C   
1169 O O   . CYS A 178 ? 0.038  0.038  0.038  0       0       0       159 CYS B O   
1170 C CB  . CYS A 178 ? 0.0496 0.0496 0.0496 0       0       0       159 CYS B CB  
1171 S SG  . CYS A 178 ? 0.0873 0.0873 0.0873 0       0       0       159 CYS B SG  
1172 N N   . VAL A 179 ? 0.038  0.038  0.038  0       0       0       160 VAL B N   
1173 C CA  . VAL A 179 ? 0.038  0.038  0.038  0       0       0       160 VAL B CA  
1174 C C   . VAL A 179 ? 0.0578 0.0578 0.0578 0       0       0       160 VAL B C   
1175 O O   . VAL A 179 ? 0.038  0.038  0.038  0       0       0       160 VAL B O   
1176 C CB  . VAL A 179 ? 0.0548 0.0548 0.0548 0       0       0       160 VAL B CB  
1177 C CG1 . VAL A 179 ? 0.038  0.038  0.038  0       0       0       160 VAL B CG1 
1178 C CG2 . VAL A 179 ? 0.038  0.038  0.038  0       0       0       160 VAL B CG2 
1179 N N   . LEU A 180 ? 0.038  0.038  0.038  0       0       0       161 LEU B N   
1180 C CA  . LEU A 180 ? 0.038  0.038  0.038  0       0       0       161 LEU B CA  
1181 C C   . LEU A 180 ? 0.0579 0.0579 0.0579 0       0       0       161 LEU B C   
1182 O O   . LEU A 180 ? 0.038  0.038  0.038  0       0       0       161 LEU B O   
1183 C CB  . LEU A 180 ? 0.038  0.038  0.038  0       0       0       161 LEU B CB  
1184 C CG  . LEU A 180 ? 0.0806 0.0806 0.0806 0       0       0       161 LEU B CG  
1185 C CD1 . LEU A 180 ? 0.0642 0.0642 0.0642 0       0       0       161 LEU B CD1 
1186 C CD2 . LEU A 180 ? 0.0873 0.0873 0.0873 0       0       0       161 LEU B CD2 
1187 N N   . SER A 181 ? 0.038  0.038  0.038  0       0       0       162 SER B N   
1188 C CA  . SER A 181 ? 0.038  0.038  0.038  0       0       0       162 SER B CA  
1189 C C   . SER A 181 ? 0.0714 0.0714 0.0714 0       0       0       162 SER B C   
1190 O O   . SER A 181 ? 0.038  0.038  0.038  0       0       0       162 SER B O   
1191 C CB  . SER A 181 ? 0.0425 0.0425 0.0425 0       0       0       162 SER B CB  
1192 O OG  . SER A 181 ? 0.1022 0.1022 0.1022 0       0       0       162 SER B OG  
1193 N N   . THR A 182 ? 0.038  0.038  0.038  0       0       0       163 THR B N   
1194 C CA  . THR A 182 ? 0.038  0.038  0.038  0       0       0       163 THR B CA  
1195 C C   . THR A 182 ? 0.0639 0.0639 0.0639 0       0       0       163 THR B C   
1196 O O   . THR A 182 ? 0.038  0.038  0.038  0       0       0       163 THR B O   
1197 C CB  . THR A 182 ? 0.0682 0.0682 0.0682 0       0       0       163 THR B CB  
1198 O OG1 . THR A 182 ? 0.038  0.038  0.038  0       0       0       163 THR B OG1 
1199 C CG2 . THR A 182 ? 0.038  0.038  0.038  0       0       0       163 THR B CG2 
1200 N N   . LEU A 183 ? 0.038  0.038  0.038  0       0       0       164 LEU B N   
1201 C CA  . LEU A 183 ? 0.038  0.038  0.038  0       0       0       164 LEU B CA  
1202 C C   . LEU A 183 ? 0.0749 0.0749 0.0749 0       0       0       164 LEU B C   
1203 O O   . LEU A 183 ? 0.038  0.038  0.038  0       0       0       164 LEU B O   
1204 C CB  . LEU A 183 ? 0.038  0.038  0.038  0       0       0       164 LEU B CB  
1205 C CG  . LEU A 183 ? 0.0695 0.0695 0.0695 0       0       0       164 LEU B CG  
1206 C CD1 . LEU A 183 ? 0.0827 0.0827 0.0827 0       0       0       164 LEU B CD1 
1207 C CD2 . LEU A 183 ? 0.0534 0.0534 0.0534 0       0       0       164 LEU B CD2 
1208 N N   . CYS A 184 ? 0.038  0.038  0.038  0       0       0       165 CYS B N   
1209 C CA  . CYS A 184 ? 0.038  0.038  0.038  0       0       0       165 CYS B CA  
1210 C C   . CYS A 184 ? 0.0727 0.0727 0.0727 0       0       0       165 CYS B C   
1211 O O   . CYS A 184 ? 0.038  0.038  0.038  0       0       0       165 CYS B O   
1212 C CB  . CYS A 184 ? 0.038  0.038  0.038  0       0       0       165 CYS B CB  
1213 S SG  . CYS A 184 ? 0.0565 0.0565 0.0565 0       0       0       165 CYS B SG  
1214 N N   . LEU A 185 ? 0.038  0.038  0.038  0       0       0       166 LEU B N   
1215 C CA  . LEU A 185 ? 0.038  0.038  0.038  0       0       0       166 LEU B CA  
1216 C C   . LEU A 185 ? 0.0573 0.0573 0.0573 0       0       0       166 LEU B C   
1217 O O   . LEU A 185 ? 0.038  0.038  0.038  0       0       0       166 LEU B O   
1218 C CB  . LEU A 185 ? 0.038  0.038  0.038  0       0       0       166 LEU B CB  
1219 C CG  . LEU A 185 ? 0.0622 0.0622 0.0622 0       0       0       166 LEU B CG  
1220 C CD1 . LEU A 185 ? 0.0476 0.0476 0.0476 0       0       0       166 LEU B CD1 
1221 C CD2 . LEU A 185 ? 0.038  0.038  0.038  0       0       0       166 LEU B CD2 
1222 N N   . ASP A 186 ? 0.038  0.038  0.038  0       0       0       167 ASP B N   
1223 C CA  . ASP A 186 ? 0.038  0.038  0.038  0       0       0       167 ASP B CA  
1224 C C   . ASP A 186 ? 0.0678 0.0678 0.0678 0       0       0       167 ASP B C   
1225 O O   . ASP A 186 ? 0.038  0.038  0.038  0       0       0       167 ASP B O   
1226 C CB  . ASP A 186 ? 0.0555 0.0555 0.0555 0       0       0       167 ASP B CB  
1227 C CG  . ASP A 186 ? 0.0754 0.0754 0.0754 0       0       0       167 ASP B CG  
1228 O OD1 . ASP A 186 ? 0.0911 0.0911 0.0911 0       0       0       167 ASP B OD1 
1229 O OD2 . ASP A 186 ? 0.0956 0.0956 0.0956 0       0       0       167 ASP B OD2 
1230 N N   . ALA A 187 ? 0.038  0.038  0.038  0       0       0       168 ALA B N   
1231 C CA  . ALA A 187 ? 0.038  0.038  0.038  0       0       0       168 ALA B CA  
1232 C C   . ALA A 187 ? 0.0785 0.0785 0.0785 0       0       0       168 ALA B C   
1233 O O   . ALA A 187 ? 0.038  0.038  0.038  0       0       0       168 ALA B O   
1234 C CB  . ALA A 187 ? 0.0455 0.0455 0.0455 0       0       0       168 ALA B CB  
1235 N N   . ALA A 188 ? 0.038  0.038  0.038  0       0       0       169 ALA B N   
1236 C CA  . ALA A 188 ? 0.038  0.038  0.038  0       0       0       169 ALA B CA  
1237 C C   . ALA A 188 ? 0.0721 0.0721 0.0721 0       0       0       169 ALA B C   
1238 O O   . ALA A 188 ? 0.0393 0.0393 0.0393 0       0       0       169 ALA B O   
1239 C CB  . ALA A 188 ? 0.0385 0.0385 0.0385 0       0       0       169 ALA B CB  
1240 N N   . CYS A 189 ? 0.038  0.038  0.038  0       0       0       170 CYS B N   
1241 C CA  . CYS A 189 ? 0.038  0.038  0.038  0       0       0       170 CYS B CA  
1242 C C   . CYS A 189 ? 0.0702 0.0702 0.0702 0       0       0       170 CYS B C   
1243 O O   . CYS A 189 ? 0.038  0.038  0.038  0       0       0       170 CYS B O   
1244 C CB  . CYS A 189 ? 0.038  0.038  0.038  0       0       0       170 CYS B CB  
1245 S SG  . CYS A 189 ? 0.046  0.046  0.046  0       0       0       170 CYS B SG  
1246 N N   . PRO A 190 ? 0.038  0.038  0.038  0       0       0       171 PRO B N   
1247 C CA  . PRO A 190 ? 0.038  0.038  0.038  0       0       0       171 PRO B CA  
1248 C C   . PRO A 190 ? 0.0858 0.0858 0.0858 0       0       0       171 PRO B C   
1249 O O   . PRO A 190 ? 0.0848 0.0848 0.0848 0       0       0       171 PRO B O   
1250 C CB  . PRO A 190 ? 0.0659 0.0659 0.0659 0       0       0       171 PRO B CB  
1251 C CG  . PRO A 190 ? 0.0592 0.0592 0.0592 0       0       0       171 PRO B CG  
1252 C CD  . PRO A 190 ? 0.0768 0.0768 0.0768 0       0       0       171 PRO B CD  
1253 N N   . ASP A 191 ? 0.038  0.038  0.038  0       0       0       172 ASP B N   
1254 C CA  . ASP A 191 ? 0.038  0.038  0.038  0       0       0       172 ASP B CA  
1255 C C   . ASP A 191 ? 0.0631 0.0631 0.0631 0       0       0       172 ASP B C   
1256 O O   . ASP A 191 ? 0.038  0.038  0.038  0       0       0       172 ASP B O   
1257 C CB  . ASP A 191 ? 0.0688 0.0688 0.0688 0       0       0       172 ASP B CB  
1258 C CG  . ASP A 191 ? 0.1096 0.0917 0.1565 0.0036  0.0349  0.0068  172 ASP B CG  
1259 O OD1 . ASP A 191 ? 0.1324 0.1291 0.1449 0.0002  0.0072  0.0004  172 ASP B OD1 
1260 O OD2 . ASP A 191 ? 0.2015 0.165  0.2794 0.0789  0.0891  0.0147  172 ASP B OD2 
1261 N N   . LEU A 192 ? 0.038  0.038  0.038  0       0       0       173 LEU B N   
1262 C CA  . LEU A 192 ? 0.042  0.042  0.042  0       0       0       173 LEU B CA  
1263 C C   . LEU A 192 ? 0.0893 0.0893 0.0893 0       0       0       173 LEU B C   
1264 O O   . LEU A 192 ? 0.0535 0.0535 0.0535 0       0       0       173 LEU B O   
1265 C CB  . LEU A 192 ? 0.0452 0.0452 0.0452 0       0       0       173 LEU B CB  
1266 C CG  . LEU A 192 ? 0.0872 0.0872 0.0872 0       0       0       173 LEU B CG  
1267 C CD1 . LEU A 192 ? 0.0813 0.0813 0.0813 0       0       0       173 LEU B CD1 
1268 C CD2 . LEU A 192 ? 0.0878 0.0878 0.0878 0       0       0       173 LEU B CD2 
1269 N N   . PRO A 193 ? 0.0877 0.0877 0.0877 0       0       0       174 PRO B N   
1270 C CA  . PRO A 193 ? 0.078  0.078  0.078  0       0       0       174 PRO B CA  
1271 C C   . PRO A 193 ? 0.0934 0.0934 0.0934 0       0       0       174 PRO B C   
1272 O O   . PRO A 193 ? 0.0798 0.0798 0.0798 0       0       0       174 PRO B O   
1273 C CB  . PRO A 193 ? 0.0969 0.0969 0.0969 0       0       0       174 PRO B CB  
1274 C CG  . PRO A 193 ? 0.0419 0.0397 0.0579 -0.0006 0.0066  -0.0016 174 PRO B CG  
1275 C CD  . PRO A 193 ? 0.0875 0.0875 0.0875 0       0       0       174 PRO B CD  
1276 N N   . THR A 194 ? 0.038  0.038  0.038  0       0       0       175 THR B N   
1277 C CA  . THR A 194 ? 0.038  0.038  0.038  0       0       0       175 THR B CA  
1278 C C   . THR A 194 ? 0.0716 0.0716 0.0716 0       0       0       175 THR B C   
1279 O O   . THR A 194 ? 0.038  0.038  0.038  0       0       0       175 THR B O   
1280 C CB  . THR A 194 ? 0.0627 0.0627 0.0627 0       0       0       175 THR B CB  
1281 O OG1 . THR A 194 ? 0.038  0.038  0.038  0       0       0       175 THR B OG1 
1282 C CG2 . THR A 194 ? 0.038  0.038  0.038  0       0       0       175 THR B CG2 
1283 N N   . TYR A 195 ? 0.038  0.038  0.038  0       0       0       176 TYR B N   
1284 C CA  . TYR A 195 ? 0.038  0.038  0.038  0       0       0       176 TYR B CA  
1285 C C   . TYR A 195 ? 0.069  0.069  0.069  0       0       0       176 TYR B C   
1286 O O   . TYR A 195 ? 0.038  0.038  0.038  0       0       0       176 TYR B O   
1287 C CB  . TYR A 195 ? 0.038  0.038  0.038  0       0       0       176 TYR B CB  
1288 C CG  . TYR A 195 ? 0.038  0.038  0.038  0       0       0       176 TYR B CG  
1289 C CD1 . TYR A 195 ? 0.046  0.046  0.046  0       0       0       176 TYR B CD1 
1290 C CD2 . TYR A 195 ? 0.0386 0.0386 0.0386 0       0       0       176 TYR B CD2 
1291 C CE1 . TYR A 195 ? 0.038  0.038  0.038  0       0       0       176 TYR B CE1 
1292 C CE2 . TYR A 195 ? 0.038  0.038  0.038  0       0       0       176 TYR B CE2 
1293 C CZ  . TYR A 195 ? 0.0869 0.0869 0.0869 0       0       0       176 TYR B CZ  
1294 O OH  . TYR A 195 ? 0.038  0.038  0.038  0       0       0       176 TYR B OH  
1295 N N   . CYS A 196 ? 0.038  0.038  0.038  0       0       0       177 CYS B N   
1296 C CA  . CYS A 196 ? 0.038  0.038  0.038  0       0       0       177 CYS B CA  
1297 C C   . CYS A 196 ? 0.0526 0.0526 0.0526 0       0       0       177 CYS B C   
1298 O O   . CYS A 196 ? 0.038  0.038  0.038  0       0       0       177 CYS B O   
1299 C CB  . CYS A 196 ? 0.038  0.038  0.038  0       0       0       177 CYS B CB  
1300 S SG  . CYS A 196 ? 0.0848 0.0848 0.0848 0       0       0       177 CYS B SG  
1301 N N   . ARG A 197 ? 0.038  0.038  0.038  0       0       0       178 ARG B N   
1302 C CA  . ARG A 197 ? 0.0437 0.0437 0.0437 0       0       0       178 ARG B CA  
1303 C C   . ARG A 197 ? 0.0537 0.0537 0.0537 0       0       0       178 ARG B C   
1304 O O   . ARG A 197 ? 0.038  0.038  0.038  0       0       0       178 ARG B O   
1305 C CB  . ARG A 197 ? 0.0879 0.0879 0.0879 0       0       0       178 ARG B CB  
1306 C CG  . ARG A 197 ? 0.1312 0.2286 0.4568 0.052   0.0902  -0.0161 178 ARG B CG  
1307 C CD  . ARG A 197 ? 0.2998 0.5832 0.7739 0.1702  0.1401  0.004   178 ARG B CD  
1308 N NE  . ARG A 197 ? 0.4193 0.7964 0.9999 0.2739  0.1875  -0.0217 178 ARG B NE  
1309 C CZ  . ARG A 197 ? 0.6026 1.0226 1.2671 0.3706  0.2355  -0.0543 178 ARG B CZ  
1310 N NH1 . ARG A 197 ? 0.5658 0.9065 1.1396 0.3807  0.2238  -0.0554 178 ARG B NH1 
1311 N NH2 . ARG A 197 ? 0.5183 0.8849 1.1351 0.3304  0.2261  -0.0502 178 ARG B NH2 
1312 N N   . ALA A 198 ? 0.038  0.038  0.038  0       0       0       179 ALA B N   
1313 C CA  . ALA A 198 ? 0.038  0.038  0.038  0       0       0       179 ALA B CA  
1314 C C   . ALA A 198 ? 0.0665 0.0665 0.0665 0       0       0       179 ALA B C   
1315 O O   . ALA A 198 ? 0.038  0.038  0.038  0       0       0       179 ALA B O   
1316 C CB  . ALA A 198 ? 0.0467 0.0467 0.0467 0       0       0       179 ALA B CB  
1317 N N   . LEU A 199 ? 0.038  0.038  0.038  0       0       0       180 LEU B N   
1318 C CA  . LEU A 199 ? 0.038  0.038  0.038  0       0       0       180 LEU B CA  
1319 C C   . LEU A 199 ? 0.0648 0.0648 0.0648 0       0       0       180 LEU B C   
1320 O O   . LEU A 199 ? 0.038  0.038  0.038  0       0       0       180 LEU B O   
1321 C CB  . LEU A 199 ? 0.038  0.038  0.038  0       0       0       180 LEU B CB  
1322 C CG  . LEU A 199 ? 0.0616 0.0616 0.0616 0       0       0       180 LEU B CG  
1323 C CD1 . LEU A 199 ? 0.0624 0.0624 0.0624 0       0       0       180 LEU B CD1 
1324 C CD2 . LEU A 199 ? 0.0534 0.0534 0.0534 0       0       0       180 LEU B CD2 
1325 N N   . ARG A 200 ? 0.038  0.038  0.038  0       0       0       181 ARG B N   
1326 C CA  . ARG A 200 ? 0.038  0.038  0.038  0       0       0       181 ARG B CA  
1327 C C   . ARG A 200 ? 0.0661 0.0661 0.0661 0       0       0       181 ARG B C   
1328 O O   . ARG A 200 ? 0.0393 0.0393 0.0393 0       0       0       181 ARG B O   
1329 C CB  . ARG A 200 ? 0.0588 0.0588 0.0588 0       0       0       181 ARG B CB  
1330 C CG  . ARG A 200 ? 0.125  0.125  0.1252 0       0       0       181 ARG B CG  
1331 C CD  . ARG A 200 ? 0.1336 0.138  0.3197 -0.0041 0.0214  -0.0357 181 ARG B CD  
1332 N NE  . ARG A 200 ? 0.2048 0.2124 0.422  -0.0067 0.0293  -0.0503 181 ARG B NE  
1333 C CZ  . ARG A 200 ? 0.1318 0.1493 0.476  -0.011  0.043   -0.0892 181 ARG B CZ  
1334 N NH1 . ARG A 200 ? 0.1203 0.1213 0.1399 -0.0005 0.0019  -0.0049 181 ARG B NH1 
1335 N NH2 . ARG A 200 ? 0.2088 0.2168 0.3447 -0.0055 0.0197  -0.0388 181 ARG B NH2 
1336 N N   . ASN A 201 ? 0.038  0.038  0.038  0       0       0       182 ASN B N   
1337 C CA  . ASN A 201 ? 0.038  0.038  0.038  0       0       0       182 ASN B CA  
1338 C C   . ASN A 201 ? 0.0823 0.0823 0.0823 0       0       0       182 ASN B C   
1339 O O   . ASN A 201 ? 0.0595 0.0595 0.0595 0       0       0       182 ASN B O   
1340 C CB  . ASN A 201 ? 0.038  0.038  0.038  0       0       0       182 ASN B CB  
1341 C CG  . ASN A 201 ? 0.0673 0.0656 0.1251 -0.0004 0.0102  -0.0021 182 ASN B CG  
1342 O OD1 . ASN A 201 ? 0.0642 0.0642 0.0642 0       0       0       182 ASN B OD1 
1343 N ND2 . ASN A 201 ? 0.038  0.038  0.038  0       0       0       182 ASN B ND2 
1344 N N   . LEU A 202 ? 0.038  0.038  0.038  0       0       0       183 LEU B N   
1345 C CA  . LEU A 202 ? 0.038  0.038  0.038  0       0       0       183 LEU B CA  
1346 C C   . LEU A 202 ? 0.0657 0.0657 0.0657 0       0       0       183 LEU B C   
1347 O O   . LEU A 202 ? 0.0401 0.0401 0.0401 0       0       0       183 LEU B O   
1348 C CB  . LEU A 202 ? 0.0397 0.0397 0.0397 0       0       0       183 LEU B CB  
1349 C CG  . LEU A 202 ? 0.0852 0.0852 0.0852 0       0       0       183 LEU B CG  
1350 C CD1 . LEU A 202 ? 0.091  0.091  0.091  0       0       0       183 LEU B CD1 
1351 C CD2 . LEU A 202 ? 0.0787 0.0816 0.0958 -0.0015 0.0033  -0.008  183 LEU B CD2 
1352 N N   . GLY A 203 ? 0.038  0.038  0.038  0       0       0       184 GLY B N   
1353 C CA  . GLY A 203 ? 0.038  0.038  0.038  0       0       0       184 GLY B CA  
1354 C C   . GLY A 203 ? 0.0827 0.0827 0.0827 0       0       0       184 GLY B C   
1355 O O   . GLY A 203 ? 0.0635 0.0636 0.0668 0.0001  -0.0003 -0.0007 184 GLY B O   
1356 N N   . SER A 204 ? 0.0443 0.0443 0.0443 0       0       0       185 SER B N   
1357 C CA  . SER A 204 ? 0.0382 0.038  0.0714 0       -0.0027 -0.0002 185 SER B CA  
1358 C C   . SER A 204 ? 0.0869 0.0863 0.1299 0.0001  -0.0052 -0.0008 185 SER B C   
1359 O O   . SER A 204 ? 0.0742 0.0723 0.1672 -0.0013 -0.0156 0.0077  185 SER B O   
1360 C CB  . SER A 204 ? 0.0512 0.0516 0.095  -0.0002 -0.0021 0.0046  185 SER B CB  
1361 O OG  . SER A 204 ? 0.0826 0.0827 0.101  0       -0.0005 0.0013  185 SER B OG  
1362 N N   . LEU A 205 ? 0.0381 0.0381 0.0438 0.0001  -0.0006 -0.0008 186 LEU B N   
1363 C CA  . LEU A 205 ? 0.0382 0.0383 0.0499 0.0003  -0.0016 -0.0019 186 LEU B CA  
1364 C C   . LEU A 205 ? 0.0677 0.0679 0.0891 0.0008  -0.0039 -0.0045 186 LEU B C   
1365 O O   . LEU A 205 ? 0.0396 0.0395 0.0712 0.0016  -0.0073 -0.0071 186 LEU B O   
1366 C CB  . LEU A 205 ? 0.038  0.038  0.038  0       0       0       186 LEU B CB  
1367 C CG  . LEU A 205 ? 0.0909 0.0909 0.0909 0       0       0       186 LEU B CG  
1368 C CD1 . LEU A 205 ? 0.0809 0.0809 0.0809 0       0       0       186 LEU B CD1 
1369 C CD2 . LEU A 205 ? 0.0847 0.0849 0.1201 0.0003  -0.0028 -0.0038 186 LEU B CD2 
1370 N N   . LEU A 206 ? 0.0385 0.039  0.0552 0.0007  -0.0028 -0.0041 187 LEU B N   
1371 C CA  . LEU A 206 ? 0.0445 0.0455 0.0668 0.0013  -0.0045 -0.0065 187 LEU B CA  
1372 C C   . LEU A 206 ? 0.1005 0.0977 0.1811 0.004   -0.022  -0.0156 187 LEU B C   
1373 O O   . LEU A 206 ? 0.0979 0.0939 0.1787 0.0024  -0.021  -0.01   187 LEU B O   
1374 C CB  . LEU A 206 ? 0.0387 0.0387 0.0387 0       0       0       187 LEU B CB  
1375 C CG  . LEU A 206 ? 0.0923 0.0923 0.0923 0       0       0       187 LEU B CG  
1376 C CD1 . LEU A 206 ? 0.0736 0.0736 0.0736 0       0       0       187 LEU B CD1 
1377 C CD2 . LEU A 206 ? 0.0909 0.0909 0.0909 0       0       0       187 LEU B CD2 
1378 N N   . LYS A 207 ? 0.0834 0.0767 0.1707 0.0054  -0.0306 -0.0171 188 LYS B N   
1379 C CA  . LYS A 207 ? 0.096  0.0771 0.2286 0.0058  -0.0561 -0.0158 188 LYS B CA  
1380 C C   . LYS A 207 ? 0.101  0.0829 0.2735 0.0096  -0.0659 -0.0284 188 LYS B C   
1381 O O   . LYS A 207 ? 0.105  0.1023 0.2253 0.0095  -0.0378 -0.033  188 LYS B O   
1382 C CB  . LYS A 207 ? 0.1284 0.0932 0.2887 0.009   -0.086  -0.0207 188 LYS B CB  
1383 C CG  . LYS A 207 ? 0.1784 0.1351 0.4039 0.0245  -0.1234 -0.0556 188 LYS B CG  
1384 C CD  . LYS A 207 ? 0.2534 0.1619 0.5414 0.0388  -0.204  -0.0748 188 LYS B CD  
1385 C CE  . LYS A 207 ? 0.2725 0.2103 0.5783 0.0476  -0.2238 -0.116  188 LYS B CE  
1386 N NZ  . LYS A 207 ? 0.3937 0.3075 0.6833 0.0469  -0.288  -0.1294 188 LYS B NZ  
1387 N N   . PRO A 208 ? 0.1144 0.0888 0.2948 0.0058  -0.0746 -0.016  189 PRO B N   
1388 C CA  . PRO A 208 ? 0.1156 0.0983 0.2681 0.0071  -0.0584 -0.0209 189 PRO B CA  
1389 C C   . PRO A 208 ? 0.1085 0.0948 0.2502 0.0116  -0.0574 -0.0328 189 PRO B C   
1390 O O   . PRO A 208 ? 0.122  0.0973 0.2715 0.0133  -0.0742 -0.0324 189 PRO B O   
1391 C CB  . PRO A 208 ? 0.1126 0.0727 0.3606 0.0028  -0.1074 -0.0074 189 PRO B CB  
1392 C CG  . PRO A 208 ? 0.1381 0.0798 0.4779 -0.0088 -0.1542 0.0229  189 PRO B CG  
1393 C CD  . PRO A 208 ? 0.1247 0.0727 0.4034 -0.0033 -0.1314 0.0083  189 PRO B CD  
1394 N N   . GLY A 209 ? 0.0739 0.0743 0.1444 0.0069  -0.0227 -0.0235 190 GLY B N   
1395 C CA  . GLY A 209 ? 0.059  0.0629 0.1122 0.0065  -0.0168 -0.0226 190 GLY B CA  
1396 C C   . GLY A 209 ? 0.0895 0.0944 0.1239 0.0046  -0.0101 -0.0169 190 GLY B C   
1397 O O   . GLY A 209 ? 0.0628 0.0683 0.0888 0.0039  -0.0076 -0.0145 190 GLY B O   
1398 N N   . GLY A 210 ? 0.0471 0.0512 0.0784 0.0037  -0.0086 -0.0145 191 GLY B N   
1399 C CA  . GLY A 210 ? 0.0389 0.042  0.0546 0.0019  -0.0039 -0.0082 191 GLY B CA  
1400 C C   . GLY A 210 ? 0.0764 0.0764 0.0764 0       0       0       191 GLY B C   
1401 O O   . GLY A 210 ? 0.0511 0.0511 0.0511 0       0       0       191 GLY B O   
1402 N N   . PHE A 211 ? 0.038  0.038  0.038  0       0       0       192 PHE B N   
1403 C CA  . PHE A 211 ? 0.038  0.038  0.038  0       0       0       192 PHE B CA  
1404 C C   . PHE A 211 ? 0.0689 0.0689 0.0689 0       0       0       192 PHE B C   
1405 O O   . PHE A 211 ? 0.038  0.038  0.038  0       0       0       192 PHE B O   
1406 C CB  . PHE A 211 ? 0.0575 0.0575 0.0575 0       0       0       192 PHE B CB  
1407 C CG  . PHE A 211 ? 0.0835 0.0835 0.0835 0       0       0       192 PHE B CG  
1408 C CD1 . PHE A 211 ? 0.0864 0.0864 0.0864 0       0       0       192 PHE B CD1 
1409 C CD2 . PHE A 211 ? 0.0979 0.1037 0.1086 0.0015  -0.002  -0.0083 192 PHE B CD2 
1410 C CE1 . PHE A 211 ? 0.0799 0.0929 0.0972 0.0002  -0.0002 -0.015  192 PHE B CE1 
1411 C CE2 . PHE A 211 ? 0.0844 0.1148 0.1432 0.012   -0.0161 -0.0467 192 PHE B CE2 
1412 C CZ  . PHE A 211 ? 0.0917 0.1091 0.1187 0.0038  -0.0047 -0.0224 192 PHE B CZ  
1413 N N   . LEU A 212 ? 0.038  0.038  0.038  0       0       0       193 LEU B N   
1414 C CA  . LEU A 212 ? 0.038  0.038  0.038  0       0       0       193 LEU B CA  
1415 C C   . LEU A 212 ? 0.0686 0.0686 0.0686 0       0       0       193 LEU B C   
1416 O O   . LEU A 212 ? 0.038  0.038  0.038  0       0       0       193 LEU B O   
1417 C CB  . LEU A 212 ? 0.038  0.038  0.038  0       0       0       193 LEU B CB  
1418 C CG  . LEU A 212 ? 0.0798 0.0798 0.0798 0       0       0       193 LEU B CG  
1419 C CD1 . LEU A 212 ? 0.0809 0.0809 0.0809 0       0       0       193 LEU B CD1 
1420 C CD2 . LEU A 212 ? 0.0685 0.0685 0.0685 0       0       0       193 LEU B CD2 
1421 N N   . VAL A 213 ? 0.038  0.038  0.038  0       0       0       194 VAL B N   
1422 C CA  . VAL A 213 ? 0.038  0.038  0.038  0       0       0       194 VAL B CA  
1423 C C   . VAL A 213 ? 0.0636 0.0636 0.0636 0       0       0       194 VAL B C   
1424 O O   . VAL A 213 ? 0.038  0.038  0.038  0       0       0       194 VAL B O   
1425 C CB  . VAL A 213 ? 0.0482 0.0482 0.0482 0       0       0       194 VAL B CB  
1426 C CG1 . VAL A 213 ? 0.038  0.038  0.038  0       0       0       194 VAL B CG1 
1427 C CG2 . VAL A 213 ? 0.038  0.038  0.038  0       0       0       194 VAL B CG2 
1428 N N   . ILE A 214 ? 0.038  0.038  0.038  0       0       0       195 ILE B N   
1429 C CA  . ILE A 214 ? 0.038  0.038  0.038  0       0       0       195 ILE B CA  
1430 C C   . ILE A 214 ? 0.0593 0.0593 0.0593 0       0       0       195 ILE B C   
1431 O O   . ILE A 214 ? 0.038  0.038  0.038  0       0       0       195 ILE B O   
1432 C CB  . ILE A 214 ? 0.0518 0.0518 0.0518 0       0       0       195 ILE B CB  
1433 C CG1 . ILE A 214 ? 0.068  0.068  0.068  0       0       0       195 ILE B CG1 
1434 C CG2 . ILE A 214 ? 0.038  0.038  0.038  0       0       0       195 ILE B CG2 
1435 C CD1 . ILE A 214 ? 0.1098 0.1152 0.1331 -0.0065 0.011   -0.0164 195 ILE B CD1 
1436 N N   . MET A 215 ? 0.038  0.038  0.038  0       0       0       196 MET B N   
1437 C CA  . MET A 215 ? 0.038  0.038  0.038  0       0       0       196 MET B CA  
1438 C C   . MET A 215 ? 0.0635 0.0635 0.0635 0       0       0       196 MET B C   
1439 O O   . MET A 215 ? 0.038  0.038  0.038  0       0       0       196 MET B O   
1440 C CB  . MET A 215 ? 0.0668 0.0668 0.0668 0       0       0       196 MET B CB  
1441 C CG  . MET A 215 ? 0.1109 0.1109 0.1109 0       0       0       196 MET B CG  
1442 S SD  . MET A 215 ? 0.0924 0.0924 0.0924 0       0       0       196 MET B SD  
1443 C CE  . MET A 215 ? 0.1328 0.1328 0.1328 0       0       0       196 MET B CE  
1444 N N   . ASP A 216 ? 0.038  0.038  0.038  0       0       0       197 ASP B N   
1445 C CA  . ASP A 216 ? 0.038  0.038  0.038  0       0       0       197 ASP B CA  
1446 C C   . ASP A 216 ? 0.0574 0.0574 0.0574 0       0       0       197 ASP B C   
1447 O O   . ASP A 216 ? 0.038  0.038  0.038  0       0       0       197 ASP B O   
1448 C CB  . ASP A 216 ? 0.038  0.038  0.038  0       0       0       197 ASP B CB  
1449 C CG  . ASP A 216 ? 0.0665 0.0665 0.0665 0       0       0       197 ASP B CG  
1450 O OD1 . ASP A 216 ? 0.038  0.038  0.038  0       0       0       197 ASP B OD1 
1451 O OD2 . ASP A 216 ? 0.038  0.038  0.038  0       0       0       197 ASP B OD2 
1452 N N   . ALA A 217 ? 0.038  0.038  0.038  0       0       0       198 ALA B N   
1453 C CA  . ALA A 217 ? 0.038  0.038  0.038  0       0       0       198 ALA B CA  
1454 C C   . ALA A 217 ? 0.0646 0.0646 0.0646 0       0       0       198 ALA B C   
1455 O O   . ALA A 217 ? 0.038  0.038  0.038  0       0       0       198 ALA B O   
1456 C CB  . ALA A 217 ? 0.038  0.038  0.038  0       0       0       198 ALA B CB  
1457 N N   . LEU A 218 ? 0.038  0.038  0.038  0       0       0       199 LEU B N   
1458 C CA  . LEU A 218 ? 0.038  0.038  0.038  0       0       0       199 LEU B CA  
1459 C C   . LEU A 218 ? 0.0653 0.0653 0.0653 0       0       0       199 LEU B C   
1460 O O   . LEU A 218 ? 0.038  0.038  0.038  0       0       0       199 LEU B O   
1461 C CB  . LEU A 218 ? 0.038  0.038  0.038  0       0       0       199 LEU B CB  
1462 C CG  . LEU A 218 ? 0.0557 0.0557 0.0557 0       0       0       199 LEU B CG  
1463 C CD1 . LEU A 218 ? 0.038  0.038  0.038  0       0       0       199 LEU B CD1 
1464 C CD2 . LEU A 218 ? 0.0393 0.0393 0.0393 0       0       0       199 LEU B CD2 
1465 N N   . LYS A 219 ? 0.038  0.038  0.038  0       0       0       200 LYS B N   
1466 C CA  . LYS A 219 ? 0.038  0.038  0.038  0       0       0       200 LYS B CA  
1467 C C   . LYS A 219 ? 0.0702 0.0702 0.0702 0       0       0       200 LYS B C   
1468 O O   . LYS A 219 ? 0.038  0.038  0.038  0       0       0       200 LYS B O   
1469 C CB  . LYS A 219 ? 0.0773 0.0773 0.0773 0       0       0       200 LYS B CB  
1470 C CG  . LYS A 219 ? 0.1892 0.1892 0.1892 0       0       0       200 LYS B CG  
1471 C CD  . LYS A 219 ? 0.2139 0.1329 0.3023 -0.0272 0.126   -0.0384 200 LYS B CD  
1472 C CE  . LYS A 219 ? 0.4447 0.3122 0.6081 -0.0544 0.2189  -0.0783 200 LYS B CE  
1473 N NZ  . LYS A 219 ? 0.5652 0.3687 0.7759 -0.081  0.3137  -0.1126 200 LYS B NZ  
1474 N N   . SER A 220 ? 0.038  0.038  0.038  0       0       0       201 SER B N   
1475 C CA  . SER A 220 ? 0.038  0.038  0.038  0       0       0       201 SER B CA  
1476 C C   . SER A 220 ? 0.0644 0.0644 0.0644 0       0       0       201 SER B C   
1477 O O   . SER A 220 ? 0.038  0.038  0.038  0       0       0       201 SER B O   
1478 C CB  . SER A 220 ? 0.038  0.038  0.038  0       0       0       201 SER B CB  
1479 O OG  . SER A 220 ? 0.0662 0.0662 0.0662 0       0       0       201 SER B OG  
1480 N N   . SER A 221 ? 0.038  0.038  0.038  0       0       0       202 SER B N   
1481 C CA  . SER A 221 ? 0.038  0.038  0.038  0       0       0       202 SER B CA  
1482 C C   . SER A 221 ? 0.0594 0.0594 0.0594 0       0       0       202 SER B C   
1483 O O   . SER A 221 ? 0.038  0.038  0.038  0       0       0       202 SER B O   
1484 C CB  . SER A 221 ? 0.0836 0.0836 0.0836 0       0       0       202 SER B CB  
1485 O OG  . SER A 221 ? 0.1017 0.1017 0.1017 0       0       0       202 SER B OG  
1486 N N   . TYR A 222 ? 0.038  0.038  0.038  0       0       0       203 TYR B N   
1487 C CA  . TYR A 222 ? 0.038  0.038  0.038  0       0       0       203 TYR B CA  
1488 C C   . TYR A 222 ? 0.075  0.075  0.075  0       0       0       203 TYR B C   
1489 O O   . TYR A 222 ? 0.038  0.038  0.038  0       0       0       203 TYR B O   
1490 C CB  . TYR A 222 ? 0.038  0.038  0.038  0       0       0       203 TYR B CB  
1491 C CG  . TYR A 222 ? 0.0642 0.0642 0.0642 0       0       0       203 TYR B CG  
1492 C CD1 . TYR A 222 ? 0.0781 0.0781 0.0781 0       0       0       203 TYR B CD1 
1493 C CD2 . TYR A 222 ? 0.0762 0.0762 0.0762 0       0       0       203 TYR B CD2 
1494 C CE1 . TYR A 222 ? 0.0916 0.0916 0.0916 0       0       0       203 TYR B CE1 
1495 C CE2 . TYR A 222 ? 0.0927 0.0927 0.0927 0       0       0       203 TYR B CE2 
1496 C CZ  . TYR A 222 ? 0.0907 0.0907 0.0907 0       0       0       203 TYR B CZ  
1497 O OH  . TYR A 222 ? 0.1247 0.1198 0.1375 -0.0008 -0.0095 0.0015  203 TYR B OH  
1498 N N   . TYR A 223 ? 0.038  0.038  0.038  0       0       0       204 TYR B N   
1499 C CA  . TYR A 223 ? 0.038  0.038  0.038  0       0       0       204 TYR B CA  
1500 C C   . TYR A 223 ? 0.0681 0.0681 0.0681 0       0       0       204 TYR B C   
1501 O O   . TYR A 223 ? 0.038  0.038  0.038  0       0       0       204 TYR B O   
1502 C CB  . TYR A 223 ? 0.038  0.038  0.038  0       0       0       204 TYR B CB  
1503 C CG  . TYR A 223 ? 0.038  0.038  0.038  0       0       0       204 TYR B CG  
1504 C CD1 . TYR A 223 ? 0.0416 0.0416 0.0416 0       0       0       204 TYR B CD1 
1505 C CD2 . TYR A 223 ? 0.038  0.038  0.038  0       0       0       204 TYR B CD2 
1506 C CE1 . TYR A 223 ? 0.038  0.038  0.038  0       0       0       204 TYR B CE1 
1507 C CE2 . TYR A 223 ? 0.038  0.038  0.038  0       0       0       204 TYR B CE2 
1508 C CZ  . TYR A 223 ? 0.0809 0.0809 0.0809 0       0       0       204 TYR B CZ  
1509 O OH  . TYR A 223 ? 0.038  0.038  0.038  0       0       0       204 TYR B OH  
1510 N N   . MET A 224 ? 0.038  0.038  0.038  0       0       0       205 MET B N   
1511 C CA  . MET A 224 ? 0.038  0.038  0.038  0       0       0       205 MET B CA  
1512 C C   . MET A 224 ? 0.0737 0.0737 0.0737 0       0       0       205 MET B C   
1513 O O   . MET A 224 ? 0.038  0.038  0.038  0       0       0       205 MET B O   
1514 C CB  . MET A 224 ? 0.0422 0.0422 0.0422 0       0       0       205 MET B CB  
1515 C CG  . MET A 224 ? 0.0533 0.0533 0.0533 0       0       0       205 MET B CG  
1516 S SD  . MET A 224 ? 0.08   0.08   0.08   0       0       0       205 MET B SD  
1517 C CE  . MET A 224 ? 0.0877 0.0444 0.0808 0.0027  -0.0399 -0.0025 205 MET B CE  
1518 N N   . ILE A 225 ? 0.038  0.038  0.038  0       0       0       206 ILE B N   
1519 C CA  . ILE A 225 ? 0.038  0.038  0.038  0       0       0       206 ILE B CA  
1520 C C   . ILE A 225 ? 0.0751 0.0751 0.0751 0       0       0       206 ILE B C   
1521 O O   . ILE A 225 ? 0.0399 0.038  0.0398 0.0001  -0.0019 -0.0001 206 ILE B O   
1522 C CB  . ILE A 225 ? 0.0775 0.0775 0.0775 0       0       0       206 ILE B CB  
1523 C CG1 . ILE A 225 ? 0.0695 0.0695 0.0695 0       0       0       206 ILE B CG1 
1524 C CG2 . ILE A 225 ? 0.0752 0.0752 0.0752 0       0       0       206 ILE B CG2 
1525 C CD1 . ILE A 225 ? 0.038  0.038  0.038  0       0       0       206 ILE B CD1 
1526 N N   . GLY A 226 ? 0.038  0.038  0.038  0       0       0       207 GLY B N   
1527 C CA  . GLY A 226 ? 0.0754 0.0389 0.0894 -0.0057 -0.0439 0.0067  207 GLY B CA  
1528 C C   . GLY A 226 ? 0.1359 0.0757 0.1462 -0.0049 -0.0656 0.0053  207 GLY B C   
1529 O O   . GLY A 226 ? 0.0843 0.0383 0.0926 -0.0035 -0.0503 0.0038  207 GLY B O   
1530 N N   . GLU A 227 ? 0.1369 0.0381 0.1398 -0.0031 -0.1003 0.0032  208 GLU B N   
1531 C CA  . GLU A 227 ? 0.1717 0.038  0.1595 0.0025  -0.1275 -0.0024 208 GLU B CA  
1532 C C   . GLU A 227 ? 0.1887 0.0725 0.1612 0.0116  -0.1027 -0.0102 208 GLU B C   
1533 O O   . GLU A 227 ? 0.1819 0.0428 0.1383 0.0188  -0.1178 -0.0157 208 GLU B O   
1534 C CB  . GLU A 227 ? 0.2523 0.0557 0.2294 0.0048  -0.1849 -0.0045 208 GLU B CB  
1535 C CG  . GLU A 227 ? 0.373  0.0495 0.3721 -0.0135 -0.3236 0.0135  208 GLU B CG  
1536 C CD  . GLU A 227 ? 0.7036 0.1883 0.6809 0.0247  -0.4817 0.0531  208 GLU B CD  
1537 O OE1 . GLU A 227 ? 0.7819 0.219  0.7359 0.0273  -0.5188 0.0399  208 GLU B OE1 
1538 O OE2 . GLU A 227 ? 0.6308 0.1447 0.6173 -0.0037 -0.4758 0.0299  208 GLU B OE2 
1539 N N   . GLN A 228 ? 0.1142 0.0392 0.094  0.0097  -0.0653 -0.0083 209 GLN B N   
1540 C CA  . GLN A 228 ? 0.0974 0.0405 0.0743 0.0121  -0.0464 -0.0095 209 GLN B CA  
1541 C C   . GLN A 228 ? 0.0819 0.0639 0.074  0.0041  -0.0144 -0.0031 209 GLN B C   
1542 O O   . GLN A 228 ? 0.038  0.038  0.038  0       0       0       209 GLN B O   
1543 C CB  . GLN A 228 ? 0.0828 0.0473 0.0671 0.0091  -0.0288 -0.0069 209 GLN B CB  
1544 C CG  . GLN A 228 ? 0.0628 0.0405 0.0498 0.0079  -0.0171 -0.0055 209 GLN B CG  
1545 C CD  . GLN A 228 ? 0.2682 0.0967 0.1558 0.0689  -0.1278 -0.045  209 GLN B CD  
1546 O OE1 . GLN A 228 ? 0.2035 0.1212 0.1439 0.036   -0.0589 -0.0222 209 GLN B OE1 
1547 N NE2 . GLN A 228 ? 0.1448 0.0511 0.0853 0.0374  -0.0711 -0.0249 209 GLN B NE2 
1548 N N   . LYS A 229 ? 0.0704 0.0401 0.0543 0.0082  -0.023  -0.0058 210 LYS B N   
1549 C CA  . LYS A 229 ? 0.038  0.038  0.038  0       0       0       210 LYS B CA  
1550 C C   . LYS A 229 ? 0.0677 0.0677 0.0677 0       0       0       210 LYS B C   
1551 O O   . LYS A 229 ? 0.038  0.038  0.038  0       0       0       210 LYS B O   
1552 C CB  . LYS A 229 ? 0.0668 0.0423 0.0519 0.0071  -0.0175 -0.0047 210 LYS B CB  
1553 C CG  . LYS A 229 ? 0.0684 0.0684 0.0684 0       0       0       210 LYS B CG  
1554 C CD  . LYS A 229 ? 0.1539 0.1133 0.1269 0.0121  -0.0272 -0.0075 210 LYS B CD  
1555 C CE  . LYS A 229 ? 0.2179 0.1135 0.1479 0.0293  -0.0687 -0.018  210 LYS B CE  
1556 N NZ  . LYS A 229 ? 0.2    0.114  0.1424 0.0238  -0.0565 -0.0146 210 LYS B NZ  
1557 N N   . PHE A 230 ? 0.038  0.038  0.038  0       0       0       211 PHE B N   
1558 C CA  . PHE A 230 ? 0.038  0.038  0.038  0       0       0       211 PHE B CA  
1559 C C   . PHE A 230 ? 0.0629 0.0629 0.0629 0       0       0       211 PHE B C   
1560 O O   . PHE A 230 ? 0.038  0.038  0.038  0       0       0       211 PHE B O   
1561 C CB  . PHE A 230 ? 0.039  0.039  0.039  0       0       0       211 PHE B CB  
1562 C CG  . PHE A 230 ? 0.0422 0.0422 0.0422 0       0       0       211 PHE B CG  
1563 C CD1 . PHE A 230 ? 0.0594 0.0594 0.0594 0       0       0       211 PHE B CD1 
1564 C CD2 . PHE A 230 ? 0.0621 0.0621 0.0621 0       0       0       211 PHE B CD2 
1565 C CE1 . PHE A 230 ? 0.0512 0.0512 0.0512 0       0       0       211 PHE B CE1 
1566 C CE2 . PHE A 230 ? 0.0841 0.0841 0.0841 0       0       0       211 PHE B CE2 
1567 C CZ  . PHE A 230 ? 0.051  0.051  0.051  0       0       0       211 PHE B CZ  
1568 N N   . SER A 231 ? 0.038  0.038  0.038  0       0       0       212 SER B N   
1569 C CA  . SER A 231 ? 0.038  0.038  0.038  0       0       0       212 SER B CA  
1570 C C   . SER A 231 ? 0.0727 0.0727 0.0727 0       0       0       212 SER B C   
1571 O O   . SER A 231 ? 0.038  0.038  0.038  0       0       0       212 SER B O   
1572 C CB  . SER A 231 ? 0.0833 0.0833 0.0833 0       0       0       212 SER B CB  
1573 O OG  . SER A 231 ? 0.0924 0.0924 0.0924 0       0       0       212 SER B OG  
1574 N N   . SER A 232 ? 0.0409 0.0409 0.0409 0       0       0       213 SER B N   
1575 C CA  . SER A 232 ? 0.038  0.038  0.038  0       0       0       213 SER B CA  
1576 C C   . SER A 232 ? 0.0706 0.0706 0.0706 0       0       0       213 SER B C   
1577 O O   . SER A 232 ? 0.038  0.038  0.038  0       0       0       213 SER B O   
1578 C CB  . SER A 232 ? 0.0577 0.0577 0.0577 0       0       0       213 SER B CB  
1579 O OG  . SER A 232 ? 0.038  0.038  0.038  0       0       0       213 SER B OG  
1580 N N   . LEU A 233 ? 0.038  0.038  0.038  0       0       0       214 LEU B N   
1581 C CA  . LEU A 233 ? 0.038  0.038  0.038  0       0       0       214 LEU B CA  
1582 C C   . LEU A 233 ? 0.0513 0.0513 0.0513 0       0       0       214 LEU B C   
1583 O O   . LEU A 233 ? 0.038  0.038  0.038  0       0       0       214 LEU B O   
1584 C CB  . LEU A 233 ? 0.038  0.038  0.038  0       0       0       214 LEU B CB  
1585 C CG  . LEU A 233 ? 0.0907 0.0907 0.0907 0       0       0       214 LEU B CG  
1586 C CD1 . LEU A 233 ? 0.081  0.081  0.081  0       0       0       214 LEU B CD1 
1587 C CD2 . LEU A 233 ? 0.086  0.086  0.086  0       0       0       214 LEU B CD2 
1588 N N   . PRO A 234 ? 0.038  0.038  0.038  0       0       0       215 PRO B N   
1589 C CA  . PRO A 234 ? 0.0491 0.0491 0.0491 0       0       0       215 PRO B CA  
1590 C C   . PRO A 234 ? 0.0962 0.0962 0.0962 0       0       0       215 PRO B C   
1591 O O   . PRO A 234 ? 0.0919 0.0919 0.0919 0       0       0       215 PRO B O   
1592 C CB  . PRO A 234 ? 0.0771 0.0771 0.0771 0       0       0       215 PRO B CB  
1593 C CG  . PRO A 234 ? 0.0686 0.0686 0.0686 0       0       0       215 PRO B CG  
1594 C CD  . PRO A 234 ? 0.0752 0.0752 0.0752 0       0       0       215 PRO B CD  
1595 N N   . LEU A 235 ? 0.1092 0.1092 0.1092 0       0       0       216 LEU B N   
1596 C CA  . LEU A 235 ? 0.11   0.11   0.11   0       0       0       216 LEU B CA  
1597 C C   . LEU A 235 ? 0.0909 0.0909 0.0909 0       0       0       216 LEU B C   
1598 O O   . LEU A 235 ? 0.0417 0.0417 0.0417 0       0       0       216 LEU B O   
1599 C CB  . LEU A 235 ? 0.1203 0.1203 0.1203 0       0       0       216 LEU B CB  
1600 C CG  . LEU A 235 ? 0.1053 0.1053 0.1053 0       0       0       216 LEU B CG  
1601 C CD1 . LEU A 235 ? 0.1114 0.1114 0.1114 0       0       0       216 LEU B CD1 
1602 C CD2 . LEU A 235 ? 0.0869 0.0796 0.1191 -0.0056 0.0209  -0.0114 216 LEU B CD2 
1603 N N   . GLY A 236 ? 0.038  0.038  0.038  0       0       0       217 GLY B N   
1604 C CA  . GLY A 236 ? 0.0383 0.0383 0.0383 0       0       0       217 GLY B CA  
1605 C C   . GLY A 236 ? 0.0766 0.0766 0.0766 0       0       0       217 GLY B C   
1606 O O   . GLY A 236 ? 0.038  0.038  0.038  0       0       0       217 GLY B O   
1607 N N   . ARG A 237 ? 0.038  0.038  0.038  0       0       0       218 ARG B N   
1608 C CA  . ARG A 237 ? 0.0419 0.0419 0.0419 0       0       0       218 ARG B CA  
1609 C C   . ARG A 237 ? 0.0708 0.0708 0.0708 0       0       0       218 ARG B C   
1610 O O   . ARG A 237 ? 0.038  0.038  0.038  0       0       0       218 ARG B O   
1611 C CB  . ARG A 237 ? 0.0847 0.0847 0.0847 0       0       0       218 ARG B CB  
1612 C CG  . ARG A 237 ? 0.1533 0.1146 0.2336 -0.0489 0.1046  -0.0712 218 ARG B CG  
1613 C CD  . ARG A 237 ? 0.4035 0.3239 0.549  -0.1084 0.2161  -0.1509 218 ARG B CD  
1614 N NE  . ARG A 237 ? 0.5453 0.4607 0.7754 -0.171  0.3131  -0.2451 218 ARG B NE  
1615 C CZ  . ARG A 237 ? 0.6991 0.5952 1.0103 -0.2604 0.4468  -0.3664 218 ARG B CZ  
1616 N NH1 . ARG A 237 ? 0.7579 0.6396 0.991  -0.2301 0.3965  -0.3074 218 ARG B NH1 
1617 N NH2 . ARG A 237 ? 0.7214 0.6769 0.9969 -0.2236 0.3592  -0.3252 218 ARG B NH2 
1618 N N   . GLU A 238 ? 0.038  0.038  0.038  0       0       0       219 GLU B N   
1619 C CA  . GLU A 238 ? 0.038  0.038  0.038  0       0       0       219 GLU B CA  
1620 C C   . GLU A 238 ? 0.071  0.071  0.071  0       0       0       219 GLU B C   
1621 O O   . GLU A 238 ? 0.038  0.038  0.038  0       0       0       219 GLU B O   
1622 C CB  . GLU A 238 ? 0.0567 0.0567 0.0567 0       0       0       219 GLU B CB  
1623 C CG  . GLU A 238 ? 0.1017 0.0877 0.1635 -0.026  0.057   -0.0437 219 GLU B CG  
1624 C CD  . GLU A 238 ? 0.2779 0.2073 0.4808 -0.0893 0.2095  -0.1425 219 GLU B CD  
1625 O OE1 . GLU A 238 ? 0.1717 0.1717 0.1717 0       0       0       219 GLU B OE1 
1626 O OE2 . GLU A 238 ? 0.4651 0.3744 0.6816 -0.1047 0.2449  -0.1608 219 GLU B OE2 
1627 N N   . ALA A 239 ? 0.038  0.038  0.038  0       0       0       220 ALA B N   
1628 C CA  . ALA A 239 ? 0.038  0.038  0.038  0       0       0       220 ALA B CA  
1629 C C   . ALA A 239 ? 0.0674 0.0674 0.0674 0       0       0       220 ALA B C   
1630 O O   . ALA A 239 ? 0.038  0.038  0.038  0       0       0       220 ALA B O   
1631 C CB  . ALA A 239 ? 0.038  0.038  0.038  0       0       0       220 ALA B CB  
1632 N N   . VAL A 240 ? 0.038  0.038  0.038  0       0       0       221 VAL B N   
1633 C CA  . VAL A 240 ? 0.038  0.038  0.038  0       0       0       221 VAL B CA  
1634 C C   . VAL A 240 ? 0.0703 0.0703 0.0703 0       0       0       221 VAL B C   
1635 O O   . VAL A 240 ? 0.038  0.038  0.038  0       0       0       221 VAL B O   
1636 C CB  . VAL A 240 ? 0.0539 0.0539 0.0539 0       0       0       221 VAL B CB  
1637 C CG1 . VAL A 240 ? 0.038  0.038  0.038  0       0       0       221 VAL B CG1 
1638 C CG2 . VAL A 240 ? 0.038  0.038  0.038  0       0       0       221 VAL B CG2 
1639 N N   . GLU A 241 ? 0.038  0.038  0.038  0       0       0       222 GLU B N   
1640 C CA  . GLU A 241 ? 0.0451 0.0451 0.0451 0       0       0       222 GLU B CA  
1641 C C   . GLU A 241 ? 0.0688 0.0688 0.0688 0       0       0       222 GLU B C   
1642 O O   . GLU A 241 ? 0.038  0.038  0.038  0       0       0       222 GLU B O   
1643 C CB  . GLU A 241 ? 0.0699 0.0699 0.0699 0       0       0       222 GLU B CB  
1644 C CG  . GLU A 241 ? 0.0866 0.0948 0.1776 -0.0422 0.0703  -0.0775 222 GLU B CG  
1645 C CD  . GLU A 241 ? 0.3439 0.3583 0.6483 -0.1596 0.264   -0.2763 222 GLU B CD  
1646 O OE1 . GLU A 241 ? 0.5067 0.5425 0.8266 -0.1782 0.2785  -0.3079 222 GLU B OE1 
1647 O OE2 . GLU A 241 ? 0.4788 0.4661 0.7167 -0.1284 0.2242  -0.2134 222 GLU B OE2 
1648 N N   . ALA A 242 ? 0.038  0.038  0.038  0       0       0       223 ALA B N   
1649 C CA  . ALA A 242 ? 0.038  0.038  0.038  0       0       0       223 ALA B CA  
1650 C C   . ALA A 242 ? 0.0718 0.0718 0.0718 0       0       0       223 ALA B C   
1651 O O   . ALA A 242 ? 0.038  0.038  0.038  0       0       0       223 ALA B O   
1652 C CB  . ALA A 242 ? 0.0489 0.0489 0.0489 0       0       0       223 ALA B CB  
1653 N N   . ALA A 243 ? 0.038  0.038  0.038  0       0       0       224 ALA B N   
1654 C CA  . ALA A 243 ? 0.038  0.038  0.038  0       0       0       224 ALA B CA  
1655 C C   . ALA A 243 ? 0.0702 0.0702 0.0702 0       0       0       224 ALA B C   
1656 O O   . ALA A 243 ? 0.038  0.038  0.038  0       0       0       224 ALA B O   
1657 C CB  . ALA A 243 ? 0.0411 0.0411 0.0411 0       0       0       224 ALA B CB  
1658 N N   . VAL A 244 ? 0.038  0.038  0.038  0       0       0       225 VAL B N   
1659 C CA  . VAL A 244 ? 0.038  0.038  0.038  0       0       0       225 VAL B CA  
1660 C C   . VAL A 244 ? 0.0745 0.0745 0.0745 0       0       0       225 VAL B C   
1661 O O   . VAL A 244 ? 0.038  0.038  0.038  0       0       0       225 VAL B O   
1662 C CB  . VAL A 244 ? 0.0562 0.0562 0.0562 0       0       0       225 VAL B CB  
1663 C CG1 . VAL A 244 ? 0.038  0.038  0.038  0       0       0       225 VAL B CG1 
1664 C CG2 . VAL A 244 ? 0.0412 0.0412 0.0412 0       0       0       225 VAL B CG2 
1665 N N   . LYS A 245 ? 0.038  0.038  0.038  0       0       0       226 LYS B N   
1666 C CA  . LYS A 245 ? 0.038  0.038  0.038  0       0       0       226 LYS B CA  
1667 C C   . LYS A 245 ? 0.0782 0.0782 0.0782 0       0       0       226 LYS B C   
1668 O O   . LYS A 245 ? 0.038  0.038  0.038  0       0       0       226 LYS B O   
1669 C CB  . LYS A 245 ? 0.0416 0.0416 0.0416 0       0       0       226 LYS B CB  
1670 C CG  . LYS A 245 ? 0.0484 0.0484 0.0484 0       0       0       226 LYS B CG  
1671 C CD  . LYS A 245 ? 0.1442 0.1442 0.1442 0       0       0       226 LYS B CD  
1672 C CE  . LYS A 245 ? 0.248  0.3013 0.4127 -0.0532 0.0806  -0.1305 226 LYS B CE  
1673 N NZ  . LYS A 245 ? 0.3194 0.4116 0.5518 -0.0799 0.1134  -0.1963 226 LYS B NZ  
1674 N N   . GLU A 246 ? 0.038  0.038  0.038  0       0       0       227 GLU B N   
1675 C CA  . GLU A 246 ? 0.038  0.038  0.038  0       0       0       227 GLU B CA  
1676 C C   . GLU A 246 ? 0.0834 0.0834 0.0834 0       0       0       227 GLU B C   
1677 O O   . GLU A 246 ? 0.0842 0.0842 0.0842 0       0       0       227 GLU B O   
1678 C CB  . GLU A 246 ? 0.0551 0.0551 0.0551 0       0       0       227 GLU B CB  
1679 C CG  . GLU A 246 ? 0.0755 0.0828 0.1367 -0.0058 0.0143  -0.0261 227 GLU B CG  
1680 C CD  . GLU A 246 ? 0.0922 0.1163 0.3712 -0.0266 0.0713  -0.1106 227 GLU B CD  
1681 O OE1 . GLU A 246 ? 0.1348 0.139  0.1856 -0.0057 0.0148  -0.0211 227 GLU B OE1 
1682 O OE2 . GLU A 246 ? 0.1418 0.1445 0.1873 -0.0036 0.011   -0.0158 227 GLU B OE2 
1683 N N   . ALA A 247 ? 0.038  0.038  0.038  0       0       0       228 ALA B N   
1684 C CA  . ALA A 247 ? 0.038  0.038  0.038  0       0       0       228 ALA B CA  
1685 C C   . ALA A 247 ? 0.0891 0.0891 0.0891 0       0       0       228 ALA B C   
1686 O O   . ALA A 247 ? 0.0796 0.0796 0.0796 0       0       0       228 ALA B O   
1687 C CB  . ALA A 247 ? 0.0411 0.0411 0.0411 0       0       0       228 ALA B CB  
1688 N N   . GLY A 248 ? 0.0408 0.0408 0.0408 0       0       0       229 GLY B N   
1689 C CA  . GLY A 248 ? 0.038  0.038  0.038  0       0       0       229 GLY B CA  
1690 C C   . GLY A 248 ? 0.0646 0.0646 0.0646 0       0       0       229 GLY B C   
1691 O O   . GLY A 248 ? 0.038  0.038  0.038  0       0       0       229 GLY B O   
1692 N N   . TYR A 249 ? 0.038  0.038  0.038  0       0       0       230 TYR B N   
1693 C CA  . TYR A 249 ? 0.038  0.038  0.038  0       0       0       230 TYR B CA  
1694 C C   . TYR A 249 ? 0.0696 0.0696 0.0696 0       0       0       230 TYR B C   
1695 O O   . TYR A 249 ? 0.0627 0.0627 0.0627 0       0       0       230 TYR B O   
1696 C CB  . TYR A 249 ? 0.038  0.038  0.038  0       0       0       230 TYR B CB  
1697 C CG  . TYR A 249 ? 0.038  0.038  0.038  0       0       0       230 TYR B CG  
1698 C CD1 . TYR A 249 ? 0.0501 0.0501 0.0501 0       0       0       230 TYR B CD1 
1699 C CD2 . TYR A 249 ? 0.0383 0.0383 0.0383 0       0       0       230 TYR B CD2 
1700 C CE1 . TYR A 249 ? 0.038  0.038  0.038  0       0       0       230 TYR B CE1 
1701 C CE2 . TYR A 249 ? 0.0528 0.0528 0.0528 0       0       0       230 TYR B CE2 
1702 C CZ  . TYR A 249 ? 0.0849 0.0849 0.0849 0       0       0       230 TYR B CZ  
1703 O OH  . TYR A 249 ? 0.038  0.038  0.038  0       0       0       230 TYR B OH  
1704 N N   . THR A 250 ? 0.038  0.038  0.038  0       0       0       231 THR B N   
1705 C CA  . THR A 250 ? 0.038  0.038  0.038  0       0       0       231 THR B CA  
1706 C C   . THR A 250 ? 0.0546 0.0546 0.0546 0       0       0       231 THR B C   
1707 O O   . THR A 250 ? 0.038  0.038  0.038  0       0       0       231 THR B O   
1708 C CB  . THR A 250 ? 0.0951 0.1241 0.1467 -0.008  0.0105  -0.0409 231 THR B CB  
1709 O OG1 . THR A 250 ? 0.1115 0.143  0.1661 -0.0065 0.0085  -0.0428 231 THR B OG1 
1710 C CG2 . THR A 250 ? 0.1105 0.1535 0.1939 -0.0097 0.0133  -0.062  231 THR B CG2 
1711 N N   . ILE A 251 ? 0.038  0.038  0.038  0       0       0       232 ILE B N   
1712 C CA  . ILE A 251 ? 0.038  0.038  0.038  0       0       0       232 ILE B CA  
1713 C C   . ILE A 251 ? 0.067  0.067  0.067  0       0       0       232 ILE B C   
1714 O O   . ILE A 251 ? 0.038  0.038  0.038  0       0       0       232 ILE B O   
1715 C CB  . ILE A 251 ? 0.0655 0.0655 0.0655 0       0       0       232 ILE B CB  
1716 C CG1 . ILE A 251 ? 0.0608 0.0608 0.0608 0       0       0       232 ILE B CG1 
1717 C CG2 . ILE A 251 ? 0.0624 0.0624 0.0624 0       0       0       232 ILE B CG2 
1718 C CD1 . ILE A 251 ? 0.0754 0.0754 0.0754 0       0       0       232 ILE B CD1 
1719 N N   . GLU A 252 ? 0.038  0.038  0.038  0       0       0       233 GLU B N   
1720 C CA  . GLU A 252 ? 0.0457 0.0457 0.0457 0       0       0       233 GLU B CA  
1721 C C   . GLU A 252 ? 0.0742 0.0742 0.0742 0       0       0       233 GLU B C   
1722 O O   . GLU A 252 ? 0.038  0.038  0.038  0       0       0       233 GLU B O   
1723 C CB  . GLU A 252 ? 0.0774 0.0774 0.0774 0       0       0       233 GLU B CB  
1724 C CG  . GLU A 252 ? 0.0545 0.1704 0.1922 -0.0404 0.0437  -0.1391 233 GLU B CG  
1725 C CD  . GLU A 252 ? 0.3155 0.5604 0.6305 -0.1358 0.0174  -0.3633 233 GLU B CD  
1726 O OE1 . GLU A 252 ? 0.4791 0.7431 0.8351 -0.1347 -0.0035 -0.3666 233 GLU B OE1 
1727 O OE2 . GLU A 252 ? 0.4185 0.6557 0.6871 -0.1061 0.0176  -0.3347 233 GLU B OE2 
1728 N N   . TRP A 253 ? 0.038  0.038  0.038  0       0       0       234 TRP B N   
1729 C CA  . TRP A 253 ? 0.0731 0.0731 0.0731 0       0       0       234 TRP B CA  
1730 C C   . TRP A 253 ? 0.0761 0.0761 0.0761 0       0       0       234 TRP B C   
1731 O O   . TRP A 253 ? 0.038  0.038  0.038  0       0       0       234 TRP B O   
1732 C CB  . TRP A 253 ? 0.0934 0.0934 0.0934 0       0       0       234 TRP B CB  
1733 C CG  . TRP A 253 ? 0.136  0.136  0.136  0       0       0       234 TRP B CG  
1734 C CD1 . TRP A 253 ? 0.0971 0.0971 0.0971 0       0       0       234 TRP B CD1 
1735 C CD2 . TRP A 253 ? 0.138  0.138  0.138  0       0       0       234 TRP B CD2 
1736 N NE1 . TRP A 253 ? 0.1032 0.1032 0.1032 0       0       0       234 TRP B NE1 
1737 C CE2 . TRP A 253 ? 0.0915 0.0945 0.0955 -0.0055 0.0059  -0.0077 234 TRP B CE2 
1738 C CE3 . TRP A 253 ? 0.1186 0.1186 0.1186 0       0       0       234 TRP B CE3 
1739 C CZ2 . TRP A 253 ? 0.0953 0.0969 0.0981 -0.0046 0.005   -0.006  234 TRP B CZ2 
1740 C CZ3 . TRP A 253 ? 0.1028 0.1028 0.1028 0       0       0       234 TRP B CZ3 
1741 C CH2 . TRP A 253 ? 0.0984 0.0986 0.0998 -0.0029 0.0034  -0.0036 234 TRP B CH2 
1742 N N   . PHE A 254 ? 0.038  0.038  0.038  0       0       0       235 PHE B N   
1743 C CA  . PHE A 254 ? 0.038  0.038  0.038  0       0       0       235 PHE B CA  
1744 C C   . PHE A 254 ? 0.0716 0.0716 0.0716 0       0       0       235 PHE B C   
1745 O O   . PHE A 254 ? 0.038  0.038  0.038  0       0       0       235 PHE B O   
1746 C CB  . PHE A 254 ? 0.038  0.038  0.038  0       0       0       235 PHE B CB  
1747 C CG  . PHE A 254 ? 0.038  0.038  0.038  0       0       0       235 PHE B CG  
1748 C CD1 . PHE A 254 ? 0.0441 0.0441 0.0441 0       0       0       235 PHE B CD1 
1749 C CD2 . PHE A 254 ? 0.038  0.038  0.038  0       0       0       235 PHE B CD2 
1750 C CE1 . PHE A 254 ? 0.0526 0.0526 0.0526 0       0       0       235 PHE B CE1 
1751 C CE2 . PHE A 254 ? 0.0731 0.0731 0.0731 0       0       0       235 PHE B CE2 
1752 C CZ  . PHE A 254 ? 0.038  0.038  0.038  0       0       0       235 PHE B CZ  
1753 N N   . GLU A 255 ? 0.038  0.038  0.038  0       0       0       236 GLU B N   
1754 C CA  . GLU A 255 ? 0.038  0.038  0.038  0       0       0       236 GLU B CA  
1755 C C   . GLU A 255 ? 0.0644 0.0644 0.0644 0       0       0       236 GLU B C   
1756 O O   . GLU A 255 ? 0.038  0.038  0.038  0       0       0       236 GLU B O   
1757 C CB  . GLU A 255 ? 0.0397 0.0397 0.0397 0       0       0       236 GLU B CB  
1758 C CG  . GLU A 255 ? 0.1106 0.1106 0.1106 0       0       0       236 GLU B CG  
1759 C CD  . GLU A 255 ? 0.1911 0.1045 0.1798 -0.0907 0.138   -0.0871 236 GLU B CD  
1760 O OE1 . GLU A 255 ? 0.241  0.2175 0.2342 -0.0233 0.0343  -0.0211 236 GLU B OE1 
1761 O OE2 . GLU A 255 ? 0.2384 0.2319 0.2378 -0.0064 0.0101  -0.0062 236 GLU B OE2 
1762 N N   . VAL A 256 ? 0.038  0.038  0.038  0       0       0       237 VAL B N   
1763 C CA  . VAL A 256 ? 0.038  0.038  0.038  0       0       0       237 VAL B CA  
1764 C C   . VAL A 256 ? 0.0711 0.0711 0.0711 0       0       0       237 VAL B C   
1765 O O   . VAL A 256 ? 0.038  0.038  0.038  0       0       0       237 VAL B O   
1766 C CB  . VAL A 256 ? 0.0817 0.0817 0.0817 0       0       0       237 VAL B CB  
1767 C CG1 . VAL A 256 ? 0.0888 0.0888 0.0888 0       0       0       237 VAL B CG1 
1768 C CG2 . VAL A 256 ? 0.0776 0.0776 0.0776 0       0       0       237 VAL B CG2 
1769 N N   . ILE A 257 ? 0.038  0.038  0.038  0       0       0       238 ILE B N   
1770 C CA  . ILE A 257 ? 0.038  0.038  0.038  0       0       0       238 ILE B CA  
1771 C C   . ILE A 257 ? 0.0681 0.0681 0.0681 0       0       0       238 ILE B C   
1772 O O   . ILE A 257 ? 0.038  0.038  0.038  0       0       0       238 ILE B O   
1773 C CB  . ILE A 257 ? 0.0718 0.0718 0.0718 0       0       0       238 ILE B CB  
1774 C CG1 . ILE A 257 ? 0.0759 0.0759 0.0759 0       0       0       238 ILE B CG1 
1775 C CG2 . ILE A 257 ? 0.0609 0.0609 0.0609 0       0       0       238 ILE B CG2 
1776 C CD1 . ILE A 257 ? 0.1139 0.1006 0.1123 -0.004  0.0136  -0.0038 238 ILE B CD1 
1777 N N   A SER A 258 ? 0.038  0.038  0.038  0       0       0       239 SER B N   
1778 N N   B SER A 258 ? 0.038  0.038  0.038  0       0       0       239 SER B N   
1779 C CA  A SER A 258 ? 0.038  0.038  0.038  0       0       0       239 SER B CA  
1780 C CA  B SER A 258 ? 0.038  0.038  0.038  0       0       0       239 SER B CA  
1781 C C   A SER A 258 ? 0.073  0.073  0.073  0       0       0       239 SER B C   
1782 C C   B SER A 258 ? 0.0767 0.0767 0.0767 0       0       0       239 SER B C   
1783 O O   A SER A 258 ? 0.0527 0.0527 0.0527 0       0       0       239 SER B O   
1784 O O   B SER A 258 ? 0.0617 0.0617 0.0617 0       0       0       239 SER B O   
1785 C CB  A SER A 258 ? 0.0459 0.0459 0.0459 0       0       0       239 SER B CB  
1786 C CB  B SER A 258 ? 0.0638 0.0638 0.0638 0       0       0       239 SER B CB  
1787 O OG  A SER A 258 ? 0.038  0.038  0.038  0       0       0       239 SER B OG  
1788 O OG  B SER A 258 ? 0.0636 0.0636 0.0636 0       0       0       239 SER B OG  
1789 N N   . GLN A 259 ? 0.038  0.038  0.038  0       0       0       240 GLN B N   
1790 C CA  . GLN A 259 ? 0.038  0.038  0.038  0       0       0       240 GLN B CA  
1791 C C   . GLN A 259 ? 0.0718 0.0718 0.0718 0       0       0       240 GLN B C   
1792 O O   . GLN A 259 ? 0.038  0.038  0.038  0       0       0       240 GLN B O   
1793 C CB  . GLN A 259 ? 0.0397 0.0397 0.0397 0       0       0       240 GLN B CB  
1794 C CG  . GLN A 259 ? 0.0775 0.0775 0.0775 0       0       0       240 GLN B CG  
1795 C CD  . GLN A 259 ? 0.15   0.0551 0.1588 0.0104  0.1003  0.0108  240 GLN B CD  
1796 O OE1 . GLN A 259 ? 0.1562 0.1294 0.1583 0.0038  0.0284  0.004   240 GLN B OE1 
1797 N NE2 . GLN A 259 ? 0.1086 0.1086 0.1086 0       0       0       240 GLN B NE2 
1798 N N   . SER A 260 ? 0.038  0.038  0.038  0       0       0       241 SER B N   
1799 C CA  . SER A 260 ? 0.038  0.038  0.038  0       0       0       241 SER B CA  
1800 C C   . SER A 260 ? 0.0797 0.0797 0.0797 0       0       0       241 SER B C   
1801 O O   . SER A 260 ? 0.038  0.038  0.038  0       0       0       241 SER B O   
1802 C CB  . SER A 260 ? 0.0784 0.0784 0.0784 0       0       0       241 SER B CB  
1803 O OG  . SER A 260 ? 0.0647 0.0647 0.0647 0       0       0       241 SER B OG  
1804 N N   . TYR A 261 ? 0.038  0.038  0.038  0       0       0       242 TYR B N   
1805 C CA  . TYR A 261 ? 0.038  0.038  0.038  0       0       0       242 TYR B CA  
1806 C C   . TYR A 261 ? 0.0998 0.0998 0.0998 0       0       0       242 TYR B C   
1807 O O   . TYR A 261 ? 0.0739 0.0739 0.0739 0       0       0       242 TYR B O   
1808 C CB  . TYR A 261 ? 0.038  0.038  0.038  0       0       0       242 TYR B CB  
1809 C CG  . TYR A 261 ? 0.038  0.038  0.038  0       0       0       242 TYR B CG  
1810 C CD1 . TYR A 261 ? 0.0493 0.0493 0.0493 0       0       0       242 TYR B CD1 
1811 C CD2 . TYR A 261 ? 0.038  0.038  0.038  0       0       0       242 TYR B CD2 
1812 C CE1 . TYR A 261 ? 0.038  0.038  0.038  0       0       0       242 TYR B CE1 
1813 C CE2 . TYR A 261 ? 0.038  0.038  0.038  0       0       0       242 TYR B CE2 
1814 C CZ  . TYR A 261 ? 0.0611 0.0611 0.0611 0       0       0       242 TYR B CZ  
1815 O OH  . TYR A 261 ? 0.038  0.038  0.038  0       0       0       242 TYR B OH  
1816 N N   . SER A 262 ? 0.0824 0.0824 0.0824 0       0       0       243 SER B N   
1817 C CA  . SER A 262 ? 0.1028 0.1028 0.1028 0       0       0       243 SER B CA  
1818 C C   . SER A 262 ? 0.095  0.095  0.095  0       0       0       243 SER B C   
1819 O O   . SER A 262 ? 0.1177 0.1177 0.1177 0       0       0       243 SER B O   
1820 C CB  . SER A 262 ? 0.1102 0.1102 0.1102 0       0       0       243 SER B CB  
1821 O OG  . SER A 262 ? 0.1074 0.109  0.1173 0.001   0.0023  0.0046  243 SER B OG  
1822 N N   . SER A 263 ? 0.1352 0.1352 0.1352 0       0       0       244 SER B N   
1823 C CA  . SER A 263 ? 0.1326 0.1349 0.1569 -0.0003 -0.0008 0.0075  244 SER B CA  
1824 C C   . SER A 263 ? 0.1298 0.1338 0.2383 -0.0077 -0.026  0.0338  244 SER B C   
1825 O O   . SER A 263 ? 0.1431 0.14   0.2332 -0.0078 -0.0309 0.0253  244 SER B O   
1826 C CB  . SER A 263 ? 0.1252 0.1376 0.271  -0.0078 -0.0237 0.0492  244 SER B CB  
1827 O OG  . SER A 263 ? 0.1919 0.2068 0.4219 -0.0243 -0.0668 0.0902  244 SER B OG  
1828 N N   . THR A 264 ? 0.1607 0.1625 0.2528 -0.0096 -0.0298 0.0326  245 THR B N   
1829 C CA  . THR A 264 ? 0.177  0.1629 0.2893 -0.0185 -0.0612 0.0421  245 THR B CA  
1830 C C   . THR A 264 ? 0.1376 0.1193 0.2736 -0.019  -0.071  0.0446  245 THR B C   
1831 O O   . THR A 264 ? 0.1777 0.132  0.2947 -0.0224 -0.0971 0.0396  245 THR B O   
1832 C CB  . THR A 264 ? 0.2316 0.2027 0.4542 -0.0434 -0.1272 0.0996  245 THR B CB  
1833 O OG1 . THR A 264 ? 0.2036 0.213  0.4347 -0.0342 -0.0882 0.1011  245 THR B OG1 
1834 C CG2 . THR A 264 ? 0.2345 0.2071 0.4989 -0.0584 -0.1578 0.125   245 THR B CG2 
1835 N N   . MET A 265 ? 0.1192 0.121  0.1632 -0.0024 -0.0086 0.0125  246 MET B N   
1836 C CA  . MET A 265 ? 0.1203 0.1203 0.1203 0       0       0       246 MET B CA  
1837 C C   . MET A 265 ? 0.1101 0.1101 0.1101 0       0       0       246 MET B C   
1838 O O   . MET A 265 ? 0.134  0.134  0.134  0       0       0       246 MET B O   
1839 C CB  . MET A 265 ? 0.0829 0.0821 0.1467 0.0052  0.0197  0.0183  246 MET B CB  
1840 C CG  . MET A 265 ? 0.1435 0.0671 0.2719 0.0079  0.0188  0.0756  246 MET B CG  
1841 S SD  . MET A 265 ? 0.2773 0.2146 0.4162 -0.0025 -0.027  0.0825  246 MET B SD  
1842 C CE  . MET A 265 ? 0.2332 0.2332 0.3623 0.0023  0.0028  0.0558  246 MET B CE  
1843 N N   . ALA A 266 ? 0.0624 0.0624 0.0624 0       0       0       247 ALA B N   
1844 C CA  . ALA A 266 ? 0.0397 0.0397 0.0397 0       0       0       247 ALA B CA  
1845 C C   . ALA A 266 ? 0.0728 0.0728 0.0728 0       0       0       247 ALA B C   
1846 O O   . ALA A 266 ? 0.0676 0.0676 0.0676 0       0       0       247 ALA B O   
1847 C CB  . ALA A 266 ? 0.038  0.038  0.038  0       0       0       247 ALA B CB  
1848 N N   . ASN A 267 ? 0.0403 0.0403 0.0403 0       0       0       248 ASN B N   
1849 C CA  . ASN A 267 ? 0.038  0.038  0.038  0       0       0       248 ASN B CA  
1850 C C   . ASN A 267 ? 0.0794 0.0794 0.0794 0       0       0       248 ASN B C   
1851 O O   . ASN A 267 ? 0.0744 0.0744 0.0744 0       0       0       248 ASN B O   
1852 C CB  . ASN A 267 ? 0.0535 0.0535 0.0535 0       0       0       248 ASN B CB  
1853 C CG  . ASN A 267 ? 0.1313 0.0743 0.201  0.0055  0.0855  0.0081  248 ASN B CG  
1854 O OD1 . ASN A 267 ? 0.177  0.177  0.177  0       0       0       248 ASN B OD1 
1855 N ND2 . ASN A 267 ? 0.2167 0.2167 0.2167 0       0       0       248 ASN B ND2 
1856 N N   . ASN A 268 ? 0.038  0.038  0.038  0       0       0       249 ASN B N   
1857 C CA  . ASN A 268 ? 0.038  0.038  0.038  0       0       0       249 ASN B CA  
1858 C C   . ASN A 268 ? 0.0774 0.0774 0.0774 0       0       0       249 ASN B C   
1859 O O   . ASN A 268 ? 0.0556 0.0556 0.0556 0       0       0       249 ASN B O   
1860 C CB  . ASN A 268 ? 0.038  0.038  0.038  0       0       0       249 ASN B CB  
1861 C CG  . ASN A 268 ? 0.0714 0.0714 0.0714 0       0       0       249 ASN B CG  
1862 O OD1 . ASN A 268 ? 0.038  0.038  0.038  0       0       0       249 ASN B OD1 
1863 N ND2 . ASN A 268 ? 0.038  0.038  0.038  0       0       0       249 ASN B ND2 
1864 N N   . GLU A 269 ? 0.038  0.038  0.038  0       0       0       250 GLU B N   
1865 C CA  . GLU A 269 ? 0.038  0.038  0.038  0       0       0       250 GLU B CA  
1866 C C   . GLU A 269 ? 0.0689 0.0689 0.0689 0       0       0       250 GLU B C   
1867 O O   . GLU A 269 ? 0.038  0.038  0.038  0       0       0       250 GLU B O   
1868 C CB  . GLU A 269 ? 0.0546 0.0546 0.0546 0       0       0       250 GLU B CB  
1869 C CG  . GLU A 269 ? 0.1114 0.1052 0.1154 -0.0009 0.008   -0.0012 250 GLU B CG  
1870 C CD  . GLU A 269 ? 0.3425 0.1647 0.4665 -0.0301 0.2368  -0.0391 250 GLU B CD  
1871 O OE1 . GLU A 269 ? 0.434  0.3355 0.5143 -0.0155 0.1352  -0.0207 250 GLU B OE1 
1872 O OE2 . GLU A 269 ? 0.441  0.3262 0.5138 -0.0226 0.1511  -0.0287 250 GLU B OE2 
1873 N N   . GLY A 270 ? 0.038  0.038  0.038  0       0       0       251 GLY B N   
1874 C CA  . GLY A 270 ? 0.038  0.038  0.038  0       0       0       251 GLY B CA  
1875 C C   . GLY A 270 ? 0.072  0.072  0.072  0       0       0       251 GLY B C   
1876 O O   . GLY A 270 ? 0.038  0.038  0.038  0       0       0       251 GLY B O   
1877 N N   . LEU A 271 ? 0.038  0.038  0.038  0       0       0       252 LEU B N   
1878 C CA  . LEU A 271 ? 0.038  0.038  0.038  0       0       0       252 LEU B CA  
1879 C C   . LEU A 271 ? 0.0713 0.0713 0.0713 0       0       0       252 LEU B C   
1880 O O   . LEU A 271 ? 0.038  0.038  0.038  0       0       0       252 LEU B O   
1881 C CB  . LEU A 271 ? 0.038  0.038  0.038  0       0       0       252 LEU B CB  
1882 C CG  . LEU A 271 ? 0.0892 0.0892 0.0892 0       0       0       252 LEU B CG  
1883 C CD1 . LEU A 271 ? 0.0863 0.0863 0.0863 0       0       0       252 LEU B CD1 
1884 C CD2 . LEU A 271 ? 0.038  0.038  0.038  0       0       0       252 LEU B CD2 
1885 N N   . PHE A 272 ? 0.038  0.038  0.038  0       0       0       253 PHE B N   
1886 C CA  . PHE A 272 ? 0.038  0.038  0.038  0       0       0       253 PHE B CA  
1887 C C   . PHE A 272 ? 0.0619 0.0619 0.0619 0       0       0       253 PHE B C   
1888 O O   . PHE A 272 ? 0.038  0.038  0.038  0       0       0       253 PHE B O   
1889 C CB  . PHE A 272 ? 0.0391 0.0391 0.0391 0       0       0       253 PHE B CB  
1890 C CG  . PHE A 272 ? 0.038  0.038  0.038  0       0       0       253 PHE B CG  
1891 C CD1 . PHE A 272 ? 0.0394 0.0394 0.0394 0       0       0       253 PHE B CD1 
1892 C CD2 . PHE A 272 ? 0.038  0.038  0.038  0       0       0       253 PHE B CD2 
1893 C CE1 . PHE A 272 ? 0.038  0.038  0.038  0       0       0       253 PHE B CE1 
1894 C CE2 . PHE A 272 ? 0.067  0.067  0.067  0       0       0       253 PHE B CE2 
1895 C CZ  . PHE A 272 ? 0.038  0.038  0.038  0       0       0       253 PHE B CZ  
1896 N N   . SER A 273 ? 0.038  0.038  0.038  0       0       0       254 SER B N   
1897 C CA  . SER A 273 ? 0.038  0.038  0.038  0       0       0       254 SER B CA  
1898 C C   . SER A 273 ? 0.0599 0.0599 0.0599 0       0       0       254 SER B C   
1899 O O   . SER A 273 ? 0.038  0.038  0.038  0       0       0       254 SER B O   
1900 C CB  . SER A 273 ? 0.1061 0.1061 0.1061 0       0       0       254 SER B CB  
1901 O OG  . SER A 273 ? 0.1261 0.1108 0.1679 -0.0665 0.0932  -0.0831 254 SER B OG  
1902 N N   . LEU A 274 ? 0.038  0.038  0.038  0       0       0       255 LEU B N   
1903 C CA  . LEU A 274 ? 0.038  0.038  0.038  0       0       0       255 LEU B CA  
1904 C C   . LEU A 274 ? 0.0573 0.0573 0.0573 0       0       0       255 LEU B C   
1905 O O   . LEU A 274 ? 0.038  0.038  0.038  0       0       0       255 LEU B O   
1906 C CB  . LEU A 274 ? 0.038  0.038  0.038  0       0       0       255 LEU B CB  
1907 C CG  . LEU A 274 ? 0.0652 0.0652 0.0652 0       0       0       255 LEU B CG  
1908 C CD1 . LEU A 274 ? 0.0727 0.0727 0.0727 0       0       0       255 LEU B CD1 
1909 C CD2 . LEU A 274 ? 0.0829 0.0829 0.0829 0       0       0       255 LEU B CD2 
1910 N N   . VAL A 275 ? 0.038  0.038  0.038  0       0       0       256 VAL B N   
1911 C CA  . VAL A 275 ? 0.038  0.038  0.038  0       0       0       256 VAL B CA  
1912 C C   . VAL A 275 ? 0.0604 0.0604 0.0604 0       0       0       256 VAL B C   
1913 O O   . VAL A 275 ? 0.038  0.038  0.038  0       0       0       256 VAL B O   
1914 C CB  . VAL A 275 ? 0.0779 0.0779 0.0779 0       0       0       256 VAL B CB  
1915 C CG1 . VAL A 275 ? 0.0722 0.0722 0.0722 0       0       0       256 VAL B CG1 
1916 C CG2 . VAL A 275 ? 0.0703 0.0703 0.0703 0       0       0       256 VAL B CG2 
1917 N N   . ALA A 276 ? 0.038  0.038  0.038  0       0       0       257 ALA B N   
1918 C CA  . ALA A 276 ? 0.038  0.038  0.038  0       0       0       257 ALA B CA  
1919 C C   . ALA A 276 ? 0.067  0.067  0.067  0       0       0       257 ALA B C   
1920 O O   . ALA A 276 ? 0.038  0.038  0.038  0       0       0       257 ALA B O   
1921 C CB  . ALA A 276 ? 0.038  0.038  0.038  0       0       0       257 ALA B CB  
1922 N N   . ARG A 277 ? 0.038  0.038  0.038  0       0       0       258 ARG B N   
1923 C CA  . ARG A 277 ? 0.038  0.038  0.038  0       0       0       258 ARG B CA  
1924 C C   . ARG A 277 ? 0.0668 0.0668 0.0668 0       0       0       258 ARG B C   
1925 O O   . ARG A 277 ? 0.038  0.038  0.038  0       0       0       258 ARG B O   
1926 C CB  . ARG A 277 ? 0.0726 0.0726 0.0726 0       0       0       258 ARG B CB  
1927 C CG  . ARG A 277 ? 0.0771 0.1554 0.2054 -0.0037 0.0048  -0.1004 258 ARG B CG  
1928 C CD  . ARG A 277 ? 0.116  0.2804 0.3971 0.0102  -0.0133 -0.2156 258 ARG B CD  
1929 N NE  . ARG A 277 ? 0.2626 0.4489 0.6337 -0.0466 -0.1277 -0.2664 258 ARG B NE  
1930 C CZ  . ARG A 277 ? 0.4557 0.635  0.8305 -0.0667 -0.2077 -0.2811 258 ARG B CZ  
1931 N NH1 . ARG A 277 ? 0.3874 0.541  0.7095 -0.0284 -0.1721 -0.2683 258 ARG B NH1 
1932 N NH2 . ARG A 277 ? 0.3808 0.4882 0.7285 -0.0066 -0.2046 -0.2223 258 ARG B NH2 
1933 N N   . LYS A 278 ? 0.038  0.038  0.038  0       0       0       259 LYS B N   
1934 C CA  . LYS A 278 ? 0.038  0.038  0.038  0       0       0       259 LYS B CA  
1935 C C   . LYS A 278 ? 0.0715 0.0715 0.0715 0       0       0       259 LYS B C   
1936 O O   . LYS A 278 ? 0.0445 0.0448 0.0458 0.0001  -0.0002 -0.0006 259 LYS B O   
1937 C CB  . LYS A 278 ? 0.0458 0.0458 0.0458 0       0       0       259 LYS B CB  
1938 C CG  . LYS A 278 ? 0.0983 0.1098 0.1779 0.0025  -0.0064 -0.031  259 LYS B CG  
1939 C CD  . LYS A 278 ? 0.0919 0.0982 0.1867 0.0038  -0.013  -0.0279 259 LYS B CD  
1940 C CE  . LYS A 278 ? 0.117  0.1187 0.278  0.0042  -0.0238 -0.029  259 LYS B CE  
1941 N NZ  . LYS A 278 ? 0.0404 0.0384 0.1127 0.001   -0.0134 -0.0056 259 LYS B NZ  
1942 N N   . LEU A 279 ? 0.038  0.038  0.038  0       0       0       260 LEU B N   
1943 C CA  . LEU A 279 ? 0.2024 0.2341 0.378  0.0067  -0.0154 -0.0764 260 LEU B CA  
1944 C C   . LEU A 279 ? 0.3011 0.5568 0.9199 -0.0479 -0.1187 -0.1318 260 LEU B C   
1945 O O   . LEU A 279 ? 0.2202 0.2338 0.5756 0.0138  -0.0559 -0.0898 260 LEU B O   
1946 C CB  . LEU A 279 ? 0.1994 0.2344 0.362  0.0032  -0.0068 -0.0758 260 LEU B CB  
1947 C CG  . LEU A 279 ? 0.1924 0.2533 0.3876 -0.0016 0.0028  -0.1091 260 LEU B CG  
1948 C CD1 . LEU A 279 ? 0.1911 0.2545 0.3877 -0.0055 0.0097  -0.1122 260 LEU B CD1 
1949 C CD2 . LEU A 279 ? 0.174  0.252  0.4117 0.0019  -0.0034 -0.1363 260 LEU B CD2 
1950 N N   . PHE B 24  ? 0.1042 0.1042 0.1042 0       0       0       5   PHE D N   
1951 C CA  . PHE B 24  ? 0.1125 0.1125 0.1125 0       0       0       5   PHE D CA  
1952 C C   . PHE B 24  ? 0.1075 0.1075 0.1075 0       0       0       5   PHE D C   
1953 O O   . PHE B 24  ? 0.0787 0.0787 0.0787 0       0       0       5   PHE D O   
1954 C CB  . PHE B 24  ? 0.1337 0.1337 0.1337 0       0       0       5   PHE D CB  
1955 C CG  . PHE B 24  ? 0.1178 0.1178 0.1178 0       0       0       5   PHE D CG  
1956 C CD1 . PHE B 24  ? 0.0966 0.0966 0.0966 0       0       0       5   PHE D CD1 
1957 C CD2 . PHE B 24  ? 0.1086 0.1086 0.1086 0       0       0       5   PHE D CD2 
1958 C CE1 . PHE B 24  ? 0.097  0.097  0.097  0       0       0       5   PHE D CE1 
1959 C CE2 . PHE B 24  ? 0.0888 0.0888 0.0888 0       0       0       5   PHE D CE2 
1960 C CZ  . PHE B 24  ? 0.1203 0.1203 0.1203 0       0       0       5   PHE D CZ  
1961 N N   . THR B 25  ? 0.038  0.038  0.038  0       0       0       6   THR D N   
1962 C CA  . THR B 25  ? 0.038  0.038  0.038  0       0       0       6   THR D CA  
1963 C C   . THR B 25  ? 0.0732 0.0732 0.0732 0       0       0       6   THR D C   
1964 O O   . THR B 25  ? 0.038  0.038  0.038  0       0       0       6   THR D O   
1965 C CB  . THR B 25  ? 0.087  0.087  0.087  0       0       0       6   THR D CB  
1966 O OG1 . THR B 25  ? 0.038  0.038  0.038  0       0       0       6   THR D OG1 
1967 C CG2 . THR B 25  ? 0.038  0.038  0.038  0       0       0       6   THR D CG2 
1968 N N   . SER B 26  ? 0.038  0.038  0.038  0       0       0       7   SER D N   
1969 C CA  . SER B 26  ? 0.038  0.038  0.038  0       0       0       7   SER D CA  
1970 C C   . SER B 26  ? 0.0657 0.0657 0.0657 0       0       0       7   SER D C   
1971 O O   . SER B 26  ? 0.038  0.038  0.038  0       0       0       7   SER D O   
1972 C CB  . SER B 26  ? 0.107  0.107  0.107  0       0       0       7   SER D CB  
1973 O OG  . SER B 26  ? 0.1229 0.1229 0.1226 0.0003  0       0       7   SER D OG  
1974 N N   . LYS B 27  ? 0.0501 0.0501 0.0501 0       0       0       8   LYS D N   
1975 C CA  . LYS B 27  ? 0.038  0.038  0.038  0       0       0       8   LYS D CA  
1976 C C   . LYS B 27  ? 0.0665 0.0665 0.0665 0       0       0       8   LYS D C   
1977 O O   . LYS B 27  ? 0.038  0.038  0.038  0       0       0       8   LYS D O   
1978 C CB  . LYS B 27  ? 0.0693 0.0693 0.0693 0       0       0       8   LYS D CB  
1979 C CG  . LYS B 27  ? 0.1077 0.1077 0.1077 0       0       0       8   LYS D CG  
1980 C CD  . LYS B 27  ? 0.1232 0.1232 0.1232 0       0       0       8   LYS D CD  
1981 C CE  . LYS B 27  ? 0.1666 0.2963 0.1866 0.0295  -0.013  -0.06   8   LYS D CE  
1982 N NZ  . LYS B 27  ? 0.2006 0.364  0.2323 0.0278  -0.0129 -0.0781 8   LYS D NZ  
1983 N N   . ASP B 28  ? 0.0392 0.0392 0.0392 0       0       0       9   ASP D N   
1984 C CA  . ASP B 28  ? 0.0585 0.0585 0.0585 0       0       0       9   ASP D CA  
1985 C C   . ASP B 28  ? 0.0901 0.0901 0.0901 0       0       0       9   ASP D C   
1986 O O   . ASP B 28  ? 0.0701 0.0701 0.0701 0       0       0       9   ASP D O   
1987 C CB  . ASP B 28  ? 0.1107 0.1107 0.1107 0       0       0       9   ASP D CB  
1988 C CG  . ASP B 28  ? 0.2632 0.3058 0.1347 0.1568  0.0809  -0.0382 9   ASP D CG  
1989 O OD1 . ASP B 28  ? 0.4288 0.4064 0.2906 0.1392  0.064   0.0149  9   ASP D OD1 
1990 O OD2 . ASP B 28  ? 0.3427 0.417  0.224  0.1663  0.0635  -0.0459 9   ASP D OD2 
1991 N N   . THR B 29  ? 0.038  0.038  0.038  0       0       0       10  THR D N   
1992 C CA  . THR B 29  ? 0.038  0.038  0.038  0       0       0       10  THR D CA  
1993 C C   . THR B 29  ? 0.0741 0.0741 0.0741 0       0       0       10  THR D C   
1994 O O   . THR B 29  ? 0.0556 0.0556 0.0556 0       0       0       10  THR D O   
1995 C CB  . THR B 29  ? 0.088  0.088  0.088  0       0       0       10  THR D CB  
1996 O OG1 . THR B 29  ? 0.1138 0.1138 0.1138 0       0       0       10  THR D OG1 
1997 C CG2 . THR B 29  ? 0.1108 0.1108 0.1108 0       0       0       10  THR D CG2 
1998 N N   . TYR B 30  ? 0.038  0.038  0.038  0       0       0       11  TYR D N   
1999 C CA  . TYR B 30  ? 0.038  0.038  0.038  0       0       0       11  TYR D CA  
2000 C C   . TYR B 30  ? 0.0756 0.0756 0.0756 0       0       0       11  TYR D C   
2001 O O   . TYR B 30  ? 0.0817 0.0817 0.0817 0       0       0       11  TYR D O   
2002 C CB  . TYR B 30  ? 0.038  0.038  0.038  0       0       0       11  TYR D CB  
2003 C CG  . TYR B 30  ? 0.038  0.038  0.038  0       0       0       11  TYR D CG  
2004 C CD1 . TYR B 30  ? 0.0486 0.0486 0.0486 0       0       0       11  TYR D CD1 
2005 C CD2 . TYR B 30  ? 0.038  0.038  0.038  0       0       0       11  TYR D CD2 
2006 C CE1 . TYR B 30  ? 0.038  0.038  0.038  0       0       0       11  TYR D CE1 
2007 C CE2 . TYR B 30  ? 0.038  0.038  0.038  0       0       0       11  TYR D CE2 
2008 C CZ  . TYR B 30  ? 0.0654 0.0654 0.0654 0       0       0       11  TYR D CZ  
2009 O OH  . TYR B 30  ? 0.038  0.038  0.038  0       0       0       11  TYR D OH  
2010 N N   . LEU B 31  ? 0.038  0.038  0.038  0       0       0       12  LEU D N   
2011 C CA  . LEU B 31  ? 0.038  0.038  0.038  0       0       0       12  LEU D CA  
2012 C C   . LEU B 31  ? 0.0904 0.0904 0.0904 0       0       0       12  LEU D C   
2013 O O   . LEU B 31  ? 0.0768 0.0768 0.0768 0       0       0       12  LEU D O   
2014 C CB  . LEU B 31  ? 0.0384 0.0384 0.0384 0       0       0       12  LEU D CB  
2015 C CG  . LEU B 31  ? 0.0912 0.0912 0.0912 0       0       0       12  LEU D CG  
2016 C CD1 . LEU B 31  ? 0.0652 0.0652 0.0652 0       0       0       12  LEU D CD1 
2017 C CD2 . LEU B 31  ? 0.0869 0.0869 0.0869 0       0       0       12  LEU D CD2 
2018 N N   . SER B 32  ? 0.038  0.038  0.038  0       0       0       13  SER D N   
2019 C CA  . SER B 32  ? 0.0447 0.0447 0.0447 0       0       0       13  SER D CA  
2020 C C   . SER B 32  ? 0.0845 0.0845 0.0845 0       0       0       13  SER D C   
2021 O O   . SER B 32  ? 0.0905 0.0905 0.0905 0       0       0       13  SER D O   
2022 C CB  . SER B 32  ? 0.1097 0.1097 0.1097 0       0       0       13  SER D CB  
2023 O OG  . SER B 32  ? 0.1474 0.0929 0.1192 0.0035  0.0382  0.0024  13  SER D OG  
2024 N N   . HIS B 33  ? 0.038  0.038  0.038  0       0       0       14  HIS D N   
2025 C CA  . HIS B 33  ? 0.038  0.038  0.038  0       0       0       14  HIS D CA  
2026 C C   . HIS B 33  ? 0.0679 0.0679 0.0679 0       0       0       14  HIS D C   
2027 O O   . HIS B 33  ? 0.038  0.038  0.038  0       0       0       14  HIS D O   
2028 C CB  . HIS B 33  ? 0.0438 0.0438 0.0438 0       0       0       14  HIS D CB  
2029 C CG  . HIS B 33  ? 0.0922 0.0922 0.0922 0       0       0       14  HIS D CG  
2030 N ND1 . HIS B 33  ? 0.0843 0.0843 0.0843 0       0       0       14  HIS D ND1 
2031 C CD2 . HIS B 33  ? 0.1364 0.0876 0.1202 -0.0029 0.0401  -0.0024 14  HIS D CD2 
2032 C CE1 . HIS B 33  ? 0.1314 0.0958 0.1154 0.0028  0.0266  0.0021  14  HIS D CE1 
2033 N NE2 . HIS B 33  ? 0.1632 0.0819 0.1305 0.0032  0.063   0.0025  14  HIS D NE2 
2034 N N   . PHE B 34  ? 0.038  0.038  0.038  0       0       0       15  PHE D N   
2035 C CA  . PHE B 34  ? 0.038  0.038  0.038  0       0       0       15  PHE D CA  
2036 C C   . PHE B 34  ? 0.0647 0.0647 0.0647 0       0       0       15  PHE D C   
2037 O O   . PHE B 34  ? 0.038  0.038  0.038  0       0       0       15  PHE D O   
2038 C CB  . PHE B 34  ? 0.038  0.038  0.038  0       0       0       15  PHE D CB  
2039 C CG  . PHE B 34  ? 0.038  0.038  0.038  0       0       0       15  PHE D CG  
2040 C CD1 . PHE B 34  ? 0.0588 0.0588 0.0588 0       0       0       15  PHE D CD1 
2041 C CD2 . PHE B 34  ? 0.038  0.038  0.038  0       0       0       15  PHE D CD2 
2042 C CE1 . PHE B 34  ? 0.0552 0.0552 0.0552 0       0       0       15  PHE D CE1 
2043 C CE2 . PHE B 34  ? 0.0659 0.0659 0.0659 0       0       0       15  PHE D CE2 
2044 C CZ  . PHE B 34  ? 0.038  0.038  0.038  0       0       0       15  PHE D CZ  
2045 N N   . ASN B 35  ? 0.038  0.038  0.038  0       0       0       16  ASN D N   
2046 C CA  . ASN B 35  ? 0.038  0.038  0.038  0       0       0       16  ASN D CA  
2047 C C   . ASN B 35  ? 0.0504 0.0504 0.0504 0       0       0       16  ASN D C   
2048 O O   . ASN B 35  ? 0.038  0.038  0.038  0       0       0       16  ASN D O   
2049 C CB  . ASN B 35  ? 0.0587 0.0548 0.0596 -0.0076 0.0102  -0.0079 16  ASN D CB  
2050 C CG  . ASN B 35  ? 0.2289 0.1756 0.2355 -0.1128 0.1458  -0.1154 16  ASN D CG  
2051 O OD1 . ASN B 35  ? 0.154  0.1471 0.1556 -0.0266 0.031   -0.0273 16  ASN D OD1 
2052 N ND2 . ASN B 35  ? 0.2733 0.1966 0.2732 -0.1105 0.1552  -0.1105 16  ASN D ND2 
2053 N N   . PRO B 36  ? 0.038  0.038  0.038  0       0       0       17  PRO D N   
2054 C CA  . PRO B 36  ? 0.038  0.038  0.038  0       0       0       17  PRO D CA  
2055 C C   . PRO B 36  ? 0.0727 0.0727 0.0727 0       0       0       17  PRO D C   
2056 O O   . PRO B 36  ? 0.047  0.047  0.047  0       0       0       17  PRO D O   
2057 C CB  . PRO B 36  ? 0.0469 0.0469 0.0469 0       0       0       17  PRO D CB  
2058 C CG  . PRO B 36  ? 0.0893 0.0893 0.0893 0       0       0       17  PRO D CG  
2059 C CD  . PRO B 36  ? 0.0401 0.0401 0.0401 0       0       0       17  PRO D CD  
2060 N N   . ARG B 37  ? 0.0426 0.0431 0.0427 -0.0023 0.0021  -0.0024 18  ARG D N   
2061 C CA  . ARG B 37  ? 0.059  0.0674 0.0618 -0.0249 0.0224  -0.0265 18  ARG D CA  
2062 C C   . ARG B 37  ? 0.0898 0.1033 0.0995 -0.0327 0.0312  -0.0382 18  ARG D C   
2063 O O   . ARG B 37  ? 0.0831 0.1073 0.0989 -0.0396 0.0364  -0.0491 18  ARG D O   
2064 C CB  . ARG B 37  ? 0.1331 0.1415 0.1341 -0.0457 0.0422  -0.0463 18  ARG D CB  
2065 C CG  . ARG B 37  ? 0.2473 0.2736 0.2237 -0.1846 0.1597  -0.1715 18  ARG D CG  
2066 C CD  . ARG B 37  ? 0.4468 0.4221 0.3313 -0.3032 0.2999  -0.3213 18  ARG D CD  
2067 N NE  . ARG B 37  ? 0.7549 0.7249 0.5973 -0.3286 0.2938  -0.3234 18  ARG D NE  
2068 C CZ  . ARG B 37  ? 1.0386 1.0061 0.877  -0.3572 0.3437  -0.3142 18  ARG D CZ  
2069 N NH1 . ARG B 37  ? 0.877  0.8438 0.7079 -0.3869 0.3243  -0.296  18  ARG D NH1 
2070 N NH2 . ARG B 37  ? 0.938  0.8997 0.7793 -0.3563 0.4169  -0.3228 18  ARG D NH2 
2071 N N   . ASP B 38  ? 0.0658 0.0736 0.0764 -0.0315 0.0327  -0.037  19  ASP D N   
2072 C CA  . ASP B 38  ? 0.0806 0.0909 0.1    -0.0383 0.0421  -0.0481 19  ASP D CA  
2073 C C   . ASP B 38  ? 0.0884 0.0989 0.1028 -0.0209 0.0224  -0.0287 19  ASP D C   
2074 O O   . ASP B 38  ? 0.0583 0.0768 0.0825 -0.0281 0.0301  -0.0416 19  ASP D O   
2075 C CB  . ASP B 38  ? 0.1391 0.139  0.1593 -0.0417 0.0509  -0.0508 19  ASP D CB  
2076 C CG  . ASP B 38  ? 0.2942 0.2852 0.3992 -0.1769 0.228   -0.2223 19  ASP D CG  
2077 O OD1 . ASP B 38  ? 0.3356 0.3506 0.4625 -0.1991 0.2472  -0.2567 19  ASP D OD1 
2078 O OD2 . ASP B 38  ? 0.4253 0.3691 0.5446 -0.2023 0.295   -0.2705 19  ASP D OD2 
2079 N N   . TYR B 39  ? 0.038  0.038  0.038  0       0       0       20  TYR D N   
2080 C CA  . TYR B 39  ? 0.038  0.038  0.038  0       0       0       20  TYR D CA  
2081 C C   . TYR B 39  ? 0.0578 0.0578 0.0578 0       0       0       20  TYR D C   
2082 O O   . TYR B 39  ? 0.038  0.038  0.038  0       0       0       20  TYR D O   
2083 C CB  . TYR B 39  ? 0.038  0.038  0.038  0       0       0       20  TYR D CB  
2084 C CG  . TYR B 39  ? 0.038  0.038  0.038  0       0       0       20  TYR D CG  
2085 C CD1 . TYR B 39  ? 0.0584 0.0584 0.0584 0       0       0       20  TYR D CD1 
2086 C CD2 . TYR B 39  ? 0.038  0.038  0.038  0       0       0       20  TYR D CD2 
2087 C CE1 . TYR B 39  ? 0.038  0.038  0.038  0       0       0       20  TYR D CE1 
2088 C CE2 . TYR B 39  ? 0.038  0.038  0.038  0       0       0       20  TYR D CE2 
2089 C CZ  . TYR B 39  ? 0.0842 0.0842 0.0842 0       0       0       20  TYR D CZ  
2090 O OH  . TYR B 39  ? 0.038  0.038  0.038  0       0       0       20  TYR D OH  
2091 N N   . LEU B 40  ? 0.038  0.038  0.038  0       0       0       21  LEU D N   
2092 C CA  . LEU B 40  ? 0.0395 0.0432 0.0416 -0.0028 0.0023  -0.0044 21  LEU D CA  
2093 C C   . LEU B 40  ? 0.0722 0.1043 0.0925 -0.0222 0.0189  -0.0371 21  LEU D C   
2094 O O   . LEU B 40  ? 0.0486 0.0917 0.0757 -0.0239 0.02    -0.045  21  LEU D O   
2095 C CB  . LEU B 40  ? 0.0408 0.0468 0.0432 -0.005  0.0038  -0.0068 21  LEU D CB  
2096 C CG  . LEU B 40  ? 0.0926 0.0926 0.0926 0       0       0       21  LEU D CG  
2097 C CD1 . LEU B 40  ? 0.0932 0.0932 0.0932 0       0       0       21  LEU D CD1 
2098 C CD2 . LEU B 40  ? 0.0822 0.0822 0.0822 0       0       0       21  LEU D CD2 
2099 N N   . GLU B 41  ? 0.0594 0.1034 0.0901 -0.0374 0.0334  -0.0584 22  GLU D N   
2100 C CA  . GLU B 41  ? 0.0714 0.1426 0.125  -0.0591 0.0539  -0.0954 22  GLU D CA  
2101 C C   . GLU B 41  ? 0.0975 0.1699 0.1611 -0.0536 0.0512  -0.0963 22  GLU D C   
2102 O O   . GLU B 41  ? 0.068  0.1656 0.1514 -0.0619 0.0584  -0.1203 22  GLU D O   
2103 C CB  . GLU B 41  ? 0.1161 0.1884 0.1771 -0.0796 0.0759  -0.1178 22  GLU D CB  
2104 C CG  . GLU B 41  ? 0.1843 0.3359 0.2911 -0.1815 0.1659  -0.2491 22  GLU D CG  
2105 C CD  . GLU B 41  ? 0.4579 0.693  0.5631 -0.278  0.2344  -0.4441 22  GLU D CD  
2106 O OE1 . GLU B 41  ? 0.5628 0.7758 0.5931 -0.2885 0.2109  -0.4717 22  GLU D OE1 
2107 O OE2 . GLU B 41  ? 0.4433 0.7317 0.6063 -0.2835 0.246   -0.461  22  GLU D OE2 
2108 N N   . LYS B 42  ? 0.0598 0.1083 0.1097 -0.0392 0.0396  -0.071  23  LYS D N   
2109 C CA  . LYS B 42  ? 0.0639 0.1091 0.1179 -0.034  0.0363  -0.0678 23  LYS D CA  
2110 C C   . LYS B 42  ? 0.0833 0.1211 0.1261 -0.0208 0.0219  -0.0494 23  LYS D C   
2111 O O   . LYS B 42  ? 0.0473 0.0935 0.1028 -0.0227 0.0245  -0.06   23  LYS D O   
2112 C CB  . LYS B 42  ? 0.11   0.1376 0.1511 -0.0262 0.03    -0.0498 23  LYS D CB  
2113 C CG  . LYS B 42  ? 0.2565 0.378  0.4853 -0.1563 0.1895  -0.277  23  LYS D CG  
2114 C CD  . LYS B 42  ? 0.4005 0.4646 0.5963 -0.1899 0.245   -0.3418 23  LYS D CD  
2115 C CE  . LYS B 42  ? 0.571  0.5614 0.7466 -0.1984 0.3049  -0.4114 23  LYS D CE  
2116 N NZ  . LYS B 42  ? 0.7147 0.6436 0.8326 -0.2048 0.3677  -0.4624 23  LYS D NZ  
2117 N N   . TYR B 43  ? 0.0417 0.0607 0.0612 -0.0091 0.0093  -0.0229 24  TYR D N   
2118 C CA  . TYR B 43  ? 0.0383 0.0409 0.041  -0.0009 0.0009  -0.0029 24  TYR D CA  
2119 C C   . TYR B 43  ? 0.0766 0.0856 0.0845 -0.0025 0.0024  -0.0091 24  TYR D C   
2120 O O   . TYR B 43  ? 0.0588 0.0621 0.0618 -0.0007 0.0006  -0.0033 24  TYR D O   
2121 C CB  . TYR B 43  ? 0.038  0.038  0.038  0       0       0       24  TYR D CB  
2122 C CG  . TYR B 43  ? 0.038  0.038  0.038  0       0       0       24  TYR D CG  
2123 C CD1 . TYR B 43  ? 0.038  0.038  0.038  0       0       0       24  TYR D CD1 
2124 C CD2 . TYR B 43  ? 0.038  0.038  0.038  0       0       0       24  TYR D CD2 
2125 C CE1 . TYR B 43  ? 0.038  0.038  0.038  0       0       0       24  TYR D CE1 
2126 C CE2 . TYR B 43  ? 0.038  0.038  0.038  0       0       0       24  TYR D CE2 
2127 C CZ  . TYR B 43  ? 0.0607 0.0607 0.0607 0       0       0       24  TYR D CZ  
2128 O OH  . TYR B 43  ? 0.038  0.038  0.038  0       0       0       24  TYR D OH  
2129 N N   . TYR B 44  ? 0.0401 0.0604 0.0552 -0.0068 0.0059  -0.0196 25  TYR D N   
2130 C CA  . TYR B 44  ? 0.04   0.0669 0.0571 -0.0076 0.0062  -0.0235 25  TYR D CA  
2131 C C   . TYR B 44  ? 0.0895 0.1905 0.1459 -0.0309 0.0238  -0.0845 25  TYR D C   
2132 O O   . TYR B 44  ? 0.0992 0.1836 0.1396 -0.0238 0.0171  -0.065  25  TYR D O   
2133 C CB  . TYR B 44  ? 0.038  0.038  0.038  0       0       0       25  TYR D CB  
2134 C CG  . TYR B 44  ? 0.038  0.038  0.038  0       0       0       25  TYR D CG  
2135 C CD1 . TYR B 44  ? 0.0559 0.0559 0.0559 0       0       0       25  TYR D CD1 
2136 C CD2 . TYR B 44  ? 0.038  0.038  0.038  0       0       0       25  TYR D CD2 
2137 C CE1 . TYR B 44  ? 0.038  0.038  0.038  0       0       0       25  TYR D CE1 
2138 C CE2 . TYR B 44  ? 0.038  0.038  0.038  0       0       0       25  TYR D CE2 
2139 C CZ  . TYR B 44  ? 0.0512 0.0512 0.0512 0       0       0       25  TYR D CZ  
2140 O OH  . TYR B 44  ? 0.038  0.038  0.038  0       0       0       25  TYR D OH  
2141 N N   . LYS B 45  ? 0.0964 0.2398 0.1822 -0.0491 0.0392  -0.1266 26  LYS D N   
2142 C CA  . LYS B 45  ? 0.0894 0.3101 0.209  -0.0777 0.0596  -0.1881 26  LYS D CA  
2143 C C   . LYS B 45  ? 0.1153 0.4144 0.2694 -0.0812 0.0601  -0.2364 26  LYS D C   
2144 O O   . LYS B 45  ? 0.1224 0.481  0.2866 -0.0947 0.0663  -0.2677 26  LYS D O   
2145 C CB  . LYS B 45  ? 0.1065 0.3673 0.262  -0.1086 0.0875  -0.2418 26  LYS D CB  
2146 C CG  . LYS B 45  ? 0.2162 0.6076 0.4021 -0.212  0.1426  -0.4379 26  LYS D CG  
2147 C CD  . LYS B 45  ? 0.3688 0.7239 0.5213 -0.2559 0.1749  -0.5568 26  LYS D CD  
2148 C CE  . LYS B 45  ? 0.6442 0.9772 0.6995 -0.3012 0.1969  -0.6701 26  LYS D CE  
2149 N NZ  . LYS B 45  ? 0.8445 1.1323 0.8578 -0.3196 0.272   -0.7767 26  LYS D NZ  
2150 N N   . PHE B 46  ? 0.1185 0.3585 0.2543 -0.0525 0.0401  -0.1919 27  PHE D N   
2151 C CA  . PHE B 46  ? 0.1491 0.5359 0.357  -0.0645 0.0395  -0.3076 27  PHE D CA  
2152 C C   . PHE B 46  ? 0.453  0.8554 0.5798 -0.1405 -0.0289 -0.4865 27  PHE D C   
2153 O O   . PHE B 46  ? 0.1116 0.5612 0.3236 -0.0626 0.0434  -0.3178 27  PHE D O   
2154 C CB  . PHE B 46  ? 0.192  0.549  0.3486 -0.0569 0.0118  -0.2831 27  PHE D CB  
2155 C CG  . PHE B 46  ? 0.2224 0.5581 0.3627 -0.0371 -0.0149 -0.2707 27  PHE D CG  
2156 C CD1 . PHE B 46  ? 0.2475 0.545  0.3951 -0.027  -0.0242 -0.2627 27  PHE D CD1 
2157 C CD2 . PHE B 46  ? 0.273  0.6238 0.3939 -0.0266 -0.0245 -0.2582 27  PHE D CD2 
2158 C CE1 . PHE B 46  ? 0.2761 0.5507 0.4097 -0.0111 -0.0419 -0.2449 27  PHE D CE1 
2159 C CE2 . PHE B 46  ? 0.3211 0.6534 0.4193 -0.0163 -0.0532 -0.2537 27  PHE D CE2 
2160 C CZ  . PHE B 46  ? 0.295  0.5871 0.4103 -0.0016 -0.0467 -0.2338 27  PHE D CZ  
2161 N N   . GLU B 53  ? 0.0381 0.0657 0.0804 -0.0013 0.0017  -0.0343 34  GLU D N   
2162 C CA  . GLU B 53  ? 0.0398 0.0517 0.0568 -0.0006 0.0007  -0.0143 34  GLU D CA  
2163 C C   . GLU B 53  ? 0.0658 0.0827 0.0872 0       0       -0.0191 34  GLU D C   
2164 O O   . GLU B 53  ? 0.0511 0.0511 0.0511 0       0       0       34  GLU D O   
2165 C CB  . GLU B 53  ? 0.0553 0.0812 0.0893 -0.004  0.0046  -0.0302 34  GLU D CB  
2166 C CG  . GLU B 53  ? 0.0858 0.1327 0.1559 -0.01   0.0121  -0.0594 34  GLU D CG  
2167 C CD  . GLU B 53  ? 0.0962 0.2588 0.3721 -0.0352 0.0455  -0.2194 34  GLU D CD  
2168 O OE1 . GLU B 53  ? 0.0774 0.1543 0.2025 -0.0189 0.0239  -0.1025 34  GLU D OE1 
2169 O OE2 . GLU B 53  ? 0.143  0.1766 0.2086 -0.0061 0.0085  -0.0481 34  GLU D OE2 
2170 N N   . SER B 54  ? 0.038  0.0909 0.0977 -0.0009 0.0009  -0.0562 35  SER D N   
2171 C CA  . SER B 54  ? 0.038  0.1059 0.1048 0.0012  -0.0012 -0.0674 35  SER D CA  
2172 C C   . SER B 54  ? 0.0641 0.1079 0.1118 0.005   -0.0052 -0.0463 35  SER D C   
2173 O O   . SER B 54  ? 0.0389 0.0747 0.0752 0.0057  -0.0057 -0.0369 35  SER D O   
2174 C CB  . SER B 54  ? 0.067  0.2114 0.1913 -0.0031 0.0029  -0.134  35  SER D CB  
2175 O OG  . SER B 54  ? 0.0659 0.3332 0.28   -0.0231 0.0207  -0.2412 35  SER D OG  
2176 N N   . GLN B 55  ? 0.0388 0.0728 0.0831 0.0053  -0.006  -0.0396 36  GLN D N   
2177 C CA  . GLN B 55  ? 0.0391 0.0528 0.0608 0.0041  -0.0051 -0.0184 36  GLN D CA  
2178 C C   . GLN B 55  ? 0.0672 0.0672 0.0672 0       0       0       36  GLN D C   
2179 O O   . GLN B 55  ? 0.038  0.038  0.038  0       0       0       36  GLN D O   
2180 C CB  . GLN B 55  ? 0.0536 0.0662 0.0779 0.0042  -0.0058 -0.0189 36  GLN D CB  
2181 C CG  . GLN B 55  ? 0.0541 0.2218 0.3236 0.0394  -0.0495 -0.2216 36  GLN D CG  
2182 C CD  . GLN B 55  ? 0.4231 0.5518 0.6329 -0.0346 -0.1414 -0.338  36  GLN D CD  
2183 O OE1 . GLN B 55  ? 0.4495 0.6276 0.6424 -0.0418 -0.1473 -0.3689 36  GLN D OE1 
2184 N NE2 . GLN B 55  ? 0.3584 0.4623 0.5733 -0.0124 -0.1405 -0.2914 36  GLN D NE2 
2185 N N   . ILE B 56  ? 0.038  0.038  0.038  0       0       0       37  ILE D N   
2186 C CA  . ILE B 56  ? 0.038  0.038  0.038  0       0       0       37  ILE D CA  
2187 C C   . ILE B 56  ? 0.0556 0.0556 0.0556 0       0       0       37  ILE D C   
2188 O O   . ILE B 56  ? 0.038  0.038  0.038  0       0       0       37  ILE D O   
2189 C CB  . ILE B 56  ? 0.0577 0.0577 0.0577 0       0       0       37  ILE D CB  
2190 C CG1 . ILE B 56  ? 0.038  0.038  0.038  0       0       0       37  ILE D CG1 
2191 C CG2 . ILE B 56  ? 0.0473 0.0473 0.0473 0       0       0       37  ILE D CG2 
2192 C CD1 . ILE B 56  ? 0.0796 0.0796 0.0796 0       0       0       37  ILE D CD1 
2193 N N   . LEU B 57  ? 0.038  0.038  0.038  0       0       0       38  LEU D N   
2194 C CA  . LEU B 57  ? 0.038  0.038  0.038  0       0       0       38  LEU D CA  
2195 C C   . LEU B 57  ? 0.0662 0.0662 0.0662 0       0       0       38  LEU D C   
2196 O O   . LEU B 57  ? 0.038  0.038  0.038  0       0       0       38  LEU D O   
2197 C CB  . LEU B 57  ? 0.038  0.038  0.038  0       0       0       38  LEU D CB  
2198 C CG  . LEU B 57  ? 0.0887 0.0887 0.0887 0       0       0       38  LEU D CG  
2199 C CD1 . LEU B 57  ? 0.0811 0.0811 0.0811 0       0       0       38  LEU D CD1 
2200 C CD2 . LEU B 57  ? 0.0914 0.1042 0.0995 -0.0003 0.0003  -0.0102 38  LEU D CD2 
2201 N N   . LYS B 58  ? 0.038  0.038  0.038  0       0       0       39  LYS D N   
2202 C CA  . LYS B 58  ? 0.038  0.038  0.038  0       0       0       39  LYS D CA  
2203 C C   . LYS B 58  ? 0.1182 0.1182 0.1182 0       0       0       39  LYS D C   
2204 O O   . LYS B 58  ? 0.0738 0.0738 0.0738 0       0       0       39  LYS D O   
2205 C CB  . LYS B 58  ? 0.0502 0.0679 0.0671 0.0066  -0.0065 -0.0195 39  LYS D CB  
2206 C CG  . LYS B 58  ? 0.0813 0.1878 0.1577 0.0243  -0.0208 -0.0956 39  LYS D CG  
2207 C CD  . LYS B 58  ? 0.0572 0.2814 0.2178 0.0442  -0.0441 -0.204  39  LYS D CD  
2208 C CE  . LYS B 58  ? 0.2326 0.5341 0.3903 0.0042  -0.0821 -0.2967 39  LYS D CE  
2209 N NZ  . LYS B 58  ? 0.2964 0.6357 0.4682 -0.0147 -0.1107 -0.3703 39  LYS D NZ  
2210 N N   . HIS B 59  ? 0.1361 0.1361 0.1361 0       0       0       40  HIS D N   
2211 C CA  . HIS B 59  ? 0.1827 0.1827 0.1827 0       0       0       40  HIS D CA  
2212 C C   . HIS B 59  ? 0.1158 0.1158 0.1158 0       0       0       40  HIS D C   
2213 O O   . HIS B 59  ? 0.0761 0.0761 0.0761 0       0       0       40  HIS D O   
2214 C CB  . HIS B 59  ? 0.1761 0.1761 0.1761 0       0       0       40  HIS D CB  
2215 C CG  . HIS B 59  ? 0.1328 0.124  0.1374 0.0004  -0.0109 -0.0004 40  HIS D CG  
2216 N ND1 . HIS B 59  ? 0.1536 0.1032 0.1768 0.0006  -0.0609 -0.0007 40  HIS D ND1 
2217 C CD2 . HIS B 59  ? 0.1378 0.1012 0.1492 -0.0052 -0.0427 0.006   40  HIS D CD2 
2218 C CE1 . HIS B 59  ? 0.155  0.1051 0.1685 -0.0091 -0.0578 0.0103  40  HIS D CE1 
2219 N NE2 . HIS B 59  ? 0.1443 0.1049 0.1531 -0.0108 -0.0463 0.0119  40  HIS D NE2 
2220 N N   . LEU B 60  ? 0.038  0.038  0.038  0       0       0       41  LEU D N   
2221 C CA  . LEU B 60  ? 0.038  0.038  0.038  0       0       0       41  LEU D CA  
2222 C C   . LEU B 60  ? 0.0625 0.0625 0.0625 0       0       0       41  LEU D C   
2223 O O   . LEU B 60  ? 0.038  0.038  0.038  0       0       0       41  LEU D O   
2224 C CB  . LEU B 60  ? 0.038  0.038  0.038  0       0       0       41  LEU D CB  
2225 C CG  . LEU B 60  ? 0.0821 0.0821 0.0821 0       0       0       41  LEU D CG  
2226 C CD1 . LEU B 60  ? 0.0626 0.0626 0.0626 0       0       0       41  LEU D CD1 
2227 C CD2 . LEU B 60  ? 0.0765 0.0765 0.0765 0       0       0       41  LEU D CD2 
2228 N N   . LEU B 61  ? 0.038  0.038  0.038  0       0       0       42  LEU D N   
2229 C CA  . LEU B 61  ? 0.038  0.038  0.038  0       0       0       42  LEU D CA  
2230 C C   . LEU B 61  ? 0.0617 0.0617 0.0617 0       0       0       42  LEU D C   
2231 O O   . LEU B 61  ? 0.0382 0.0382 0.0382 0       0       0       42  LEU D O   
2232 C CB  . LEU B 61  ? 0.038  0.038  0.038  0       0       0       42  LEU D CB  
2233 C CG  . LEU B 61  ? 0.0816 0.0816 0.0816 0       0       0       42  LEU D CG  
2234 C CD1 . LEU B 61  ? 0.0731 0.0731 0.0731 0       0       0       42  LEU D CD1 
2235 C CD2 . LEU B 61  ? 0.087  0.087  0.087  0       0       0       42  LEU D CD2 
2236 N N   . LYS B 62  ? 0.038  0.038  0.038  0       0       0       43  LYS D N   
2237 C CA  . LYS B 62  ? 0.038  0.038  0.038  0       0       0       43  LYS D CA  
2238 C C   . LYS B 62  ? 0.0741 0.0741 0.0741 0       0       0       43  LYS D C   
2239 O O   . LYS B 62  ? 0.0458 0.0458 0.0458 0       0       0       43  LYS D O   
2240 C CB  . LYS B 62  ? 0.0722 0.0722 0.0722 0       0       0       43  LYS D CB  
2241 C CG  . LYS B 62  ? 0.1684 0.2142 0.171  -0.0042 -0.0821 -0.0551 43  LYS D CG  
2242 C CD  . LYS B 62  ? 0.3123 0.3478 0.3237 -0.0102 -0.104  -0.0637 43  LYS D CD  
2243 C CE  . LYS B 62  ? 0.4356 0.5497 0.4533 -0.0334 -0.1813 -0.1425 43  LYS D CE  
2244 N NZ  . LYS B 62  ? 0.4892 0.5776 0.5288 -0.0413 -0.1944 -0.1532 43  LYS D NZ  
2245 N N   . ASN B 63  ? 0.038  0.038  0.038  0       0       0       44  ASN D N   
2246 C CA  . ASN B 63  ? 0.0386 0.0386 0.0386 0       0       0       44  ASN D CA  
2247 C C   . ASN B 63  ? 0.063  0.063  0.063  0       0       0       44  ASN D C   
2248 O O   . ASN B 63  ? 0.038  0.038  0.038  0       0       0       44  ASN D O   
2249 C CB  . ASN B 63  ? 0.1174 0.1174 0.1174 0       0       0       44  ASN D CB  
2250 C CG  . ASN B 63  ? 0.3255 0.2786 0.3268 -0.0864 -0.1162 0.0285  44  ASN D CG  
2251 O OD1 . ASN B 63  ? 0.3723 0.3227 0.3531 -0.0526 -0.0727 0.0461  44  ASN D OD1 
2252 N ND2 . ASN B 63  ? 0.3268 0.2604 0.3212 -0.041  -0.0831 0.0396  44  ASN D ND2 
2253 N N   . LEU B 64  ? 0.038  0.038  0.038  0       0       0       45  LEU D N   
2254 C CA  . LEU B 64  ? 0.038  0.038  0.038  0       0       0       45  LEU D CA  
2255 C C   . LEU B 64  ? 0.0713 0.0713 0.0713 0       0       0       45  LEU D C   
2256 O O   . LEU B 64  ? 0.0417 0.0417 0.0417 0       0       0       45  LEU D O   
2257 C CB  . LEU B 64  ? 0.038  0.038  0.038  0       0       0       45  LEU D CB  
2258 C CG  . LEU B 64  ? 0.0641 0.0641 0.0641 0       0       0       45  LEU D CG  
2259 C CD1 . LEU B 64  ? 0.0467 0.0467 0.0467 0       0       0       45  LEU D CD1 
2260 C CD2 . LEU B 64  ? 0.0512 0.0512 0.0512 0       0       0       45  LEU D CD2 
2261 N N   . PHE B 65  ? 0.0496 0.0496 0.0496 0       0       0       46  PHE D N   
2262 C CA  . PHE B 65  ? 0.0702 0.0702 0.0702 0       0       0       46  PHE D CA  
2263 C C   . PHE B 65  ? 0.0984 0.0984 0.0984 0       0       0       46  PHE D C   
2264 O O   . PHE B 65  ? 0.0932 0.0932 0.0932 0       0       0       46  PHE D O   
2265 C CB  . PHE B 65  ? 0.118  0.118  0.118  0       0       0       46  PHE D CB  
2266 C CG  . PHE B 65  ? 0.0996 0.1155 0.0992 0.0036  -0.0006 -0.0026 46  PHE D CG  
2267 C CD1 . PHE B 65  ? 0.101  0.2179 0.0907 0.0419  -0.0066 -0.0204 46  PHE D CD1 
2268 C CD2 . PHE B 65  ? 0.0925 0.1972 0.0901 0.0206  -0.0025 -0.0129 46  PHE D CD2 
2269 C CE1 . PHE B 65  ? 0.1193 0.3128 0.0788 0.084   -0.0163 -0.0239 46  PHE D CE1 
2270 C CE2 . PHE B 65  ? 0.114  0.3112 0.0835 0.0544  -0.0192 -0.0162 46  PHE D CE2 
2271 C CZ  . PHE B 65  ? 0.1134 0.3331 0.0797 0.0861  -0.0106 -0.0195 46  PHE D CZ  
2272 N N   . LYS B 66  ? 0.0466 0.0466 0.0466 0       0       0       47  LYS D N   
2273 C CA  . LYS B 66  ? 0.0504 0.0504 0.0504 0       0       0       47  LYS D CA  
2274 C C   . LYS B 66  ? 0.0906 0.0906 0.0906 0       0       0       47  LYS D C   
2275 O O   . LYS B 66  ? 0.0845 0.0845 0.0845 0       0       0       47  LYS D O   
2276 C CB  . LYS B 66  ? 0.0806 0.0806 0.0806 0       0       0       47  LYS D CB  
2277 C CG  . LYS B 66  ? 0.1416 0.1416 0.1416 0       0       0       47  LYS D CG  
2278 C CD  . LYS B 66  ? 0.1785 0.1955 0.175  -0.026  -0.017  0.0235  47  LYS D CD  
2279 C CE  . LYS B 66  ? 0.1997 0.2406 0.2007 -0.0531 -0.037  0.0538  47  LYS D CE  
2280 N NZ  . LYS B 66  ? 0.2363 0.2363 0.2363 0       0       0       47  LYS D NZ  
2281 N N   . ILE B 67  ? 0.0456 0.0456 0.0456 0       0       0       48  ILE D N   
2282 C CA  . ILE B 67  ? 0.038  0.038  0.038  0       0       0       48  ILE D CA  
2283 C C   . ILE B 67  ? 0.1117 0.1117 0.1117 0       0       0       48  ILE D C   
2284 O O   . ILE B 67  ? 0.1156 0.1156 0.1156 0       0       0       48  ILE D O   
2285 C CB  . ILE B 67  ? 0.0627 0.0627 0.0627 0       0       0       48  ILE D CB  
2286 C CG1 . ILE B 67  ? 0.0557 0.0557 0.0557 0       0       0       48  ILE D CG1 
2287 C CG2 . ILE B 67  ? 0.0486 0.0486 0.0486 0       0       0       48  ILE D CG2 
2288 C CD1 . ILE B 67  ? 0.0897 0.0897 0.0897 0       0       0       48  ILE D CD1 
2289 N N   . PHE B 68  ? 0.147  0.147  0.147  0       0       0       49  PHE D N   
2290 C CA  . PHE B 68  ? 0.1563 0.1563 0.1563 0       0       0       49  PHE D CA  
2291 C C   . PHE B 68  ? 0.0884 0.1571 0.0573 0.0342  0.0035  0.0088  49  PHE D C   
2292 O O   . PHE B 68  ? 0.1406 0.1778 0.0985 0.0607  0.0112  0.0151  49  PHE D O   
2293 C CB  . PHE B 68  ? 0.1488 0.1488 0.1488 0       0       0       49  PHE D CB  
2294 C CG  . PHE B 68  ? 0.1507 0.1507 0.1507 0       0       0       49  PHE D CG  
2295 C CD1 . PHE B 68  ? 0.1255 0.1255 0.1255 0       0       0       49  PHE D CD1 
2296 C CD2 . PHE B 68  ? 0.1436 0.1436 0.1436 0       0       0       49  PHE D CD2 
2297 C CE1 . PHE B 68  ? 0.1165 0.1165 0.1165 0       0       0       49  PHE D CE1 
2298 C CE2 . PHE B 68  ? 0.1101 0.1101 0.1101 0       0       0       49  PHE D CE2 
2299 C CZ  . PHE B 68  ? 0.13   0.13   0.13   0       0       0       49  PHE D CZ  
2300 N N   . CYS B 69  ? 0.1428 0.2417 0.0446 0.0409  -0.0077 0.0155  50  CYS D N   
2301 C CA  . CYS B 69  ? 0.2288 0.3447 0.0912 0.0845  -0.0026 0.0241  50  CYS D CA  
2302 C C   . CYS B 69  ? 0.3299 0.4701 0.1662 0.1018  0.0148  0.055   50  CYS D C   
2303 O O   . CYS B 69  ? 0.3858 0.5297 0.2227 0.1465  0.0334  0.0636  50  CYS D O   
2304 C CB  . CYS B 69  ? 0.2798 0.4151 0.1518 0.0903  -0.0225 0.0048  50  CYS D CB  
2305 S SG  . CYS B 69  ? 0.3466 0.4491 0.2121 0.0801  -0.0369 -0.0163 50  CYS D SG  
2306 N N   . LEU B 70  ? 0.2493 0.402  0.1201 0.0689  0.0118  0.0653  51  LEU D N   
2307 C CA  . LEU B 70  ? 0.5444 0.7073 0.2827 0.0792  0.0403  0.1338  51  LEU D CA  
2308 C C   . LEU B 70  ? 1.2206 1.3602 0.9874 0.0611  0.1053  0.1541  51  LEU D C   
2309 O O   . LEU B 70  ? 0.9059 1.0413 0.6451 0.0897  0.165   0.1786  51  LEU D O   
2310 C CB  . LEU B 70  ? 0.5163 0.7075 0.287  0.0566  -0.0047 0.1379  51  LEU D CB  
2311 C CG  . LEU B 70  ? 0.6006 0.8241 0.3532 0.0679  -0.0672 0.1103  51  LEU D CG  
2312 C CD1 . LEU B 70  ? 0.5905 0.8304 0.3825 0.0395  -0.1038 0.1076  51  LEU D CD1 
2313 C CD2 . LEU B 70  ? 0.6638 0.9202 0.3551 0.1221  -0.0626 0.1197  51  LEU D CD2 
2314 N N   . GLY B 72  ? 0.4484 0.4702 0.3922 0.0811  0.0576  0.0581  53  GLY D N   
2315 C CA  . GLY B 72  ? 0.434  0.4156 0.399  0.0662  0.0662  0.0544  53  GLY D CA  
2316 C C   . GLY B 72  ? 0.4316 0.3913 0.3541 0.0388  0.1132  0.0456  53  GLY D C   
2317 O O   . GLY B 72  ? 0.5027 0.3859 0.4453 0.0522  0.1041  0.0397  53  GLY D O   
2318 N N   . VAL B 73  ? 0.2627 0.2759 0.144  -0.0007 0.1423  0.0403  54  VAL D N   
2319 C CA  . VAL B 73  ? 0.2432 0.2118 0.1577 -0.0136 0.1167  0.0067  54  VAL D CA  
2320 C C   . VAL B 73  ? 0.2699 0.2134 0.1543 0.0045  0.1104  0.0002  54  VAL D C   
2321 O O   . VAL B 73  ? 0.2662 0.2283 0.1413 0.0121  0.0769  0       54  VAL D O   
2322 C CB  . VAL B 73  ? 0.2146 0.2314 0.1369 -0.0543 0.1199  -0.0014 54  VAL D CB  
2323 C CG1 . VAL B 73  ? 0.2082 0.2019 0.1423 -0.065  0.117   -0.0326 54  VAL D CG1 
2324 C CG2 . VAL B 73  ? 0.1859 0.2051 0.1491 -0.0662 0.107   0.0041  54  VAL D CG2 
2325 N N   . LYS B 74  ? 0.2474 0.1302 0.1792 0.0054  0.076   0.0035  55  LYS D N   
2326 C CA  . LYS B 74  ? 0.2597 0.1395 0.179  0.0129  0.0705  0.0075  55  LYS D CA  
2327 C C   . LYS B 74  ? 0.2196 0.1315 0.169  -0.0018 0.0575  -0.0012 55  LYS D C   
2328 O O   . LYS B 74  ? 0.2147 0.1538 0.1865 -0.006  0.0453  -0.0044 55  LYS D O   
2329 C CB  . LYS B 74  ? 0.3584 0.1746 0.2142 0.0597  0.1074  0.0318  55  LYS D CB  
2330 C CG  . LYS B 74  ? 0.6359 0.4387 0.4222 0.085   0.2194  0.0267  55  LYS D CG  
2331 C CD  . LYS B 74  ? 0.7392 0.6336 0.4717 0.1026  0.3248  0.0344  55  LYS D CD  
2332 C CE  . LYS B 74  ? 0.8414 0.77   0.5697 0.0946  0.4525  0.0312  55  LYS D CE  
2333 N NZ  . LYS B 74  ? 0.8648 0.8464 0.6147 0.0816  0.4839  0.0719  55  LYS D NZ  
2334 N N   . GLY B 75  ? 0.1583 0.1583 0.1583 0       0       0       56  GLY D N   
2335 C CA  . GLY B 75  ? 0.171  0.171  0.171  0       0       0       56  GLY D CA  
2336 C C   . GLY B 75  ? 0.1443 0.1443 0.1443 0       0       0       56  GLY D C   
2337 O O   . GLY B 75  ? 0.1388 0.1388 0.1388 0       0       0       56  GLY D O   
2338 N N   . ASP B 76  ? 0.0928 0.0928 0.0928 0       0       0       57  ASP D N   
2339 C CA  . ASP B 76  ? 0.0984 0.0984 0.0984 0       0       0       57  ASP D CA  
2340 C C   . ASP B 76  ? 0.101  0.101  0.101  0       0       0       57  ASP D C   
2341 O O   . ASP B 76  ? 0.0986 0.0986 0.0986 0       0       0       57  ASP D O   
2342 C CB  . ASP B 76  ? 0.1328 0.1328 0.1328 0       0       0       57  ASP D CB  
2343 C CG  . ASP B 76  ? 0.3994 0.153  0.2588 -0.0272 0.1646  -0.0179 57  ASP D CG  
2344 O OD1 . ASP B 76  ? 0.4312 0.1835 0.274  -0.0061 0.1499  -0.0037 57  ASP D OD1 
2345 O OD2 . ASP B 76  ? 0.5485 0.1887 0.3618 -0.0489 0.2565  -0.0342 57  ASP D OD2 
2346 N N   . LEU B 77  ? 0.0487 0.0487 0.0487 0       0       0       58  LEU D N   
2347 C CA  . LEU B 77  ? 0.038  0.038  0.038  0       0       0       58  LEU D CA  
2348 C C   . LEU B 77  ? 0.0687 0.0687 0.0687 0       0       0       58  LEU D C   
2349 O O   . LEU B 77  ? 0.038  0.038  0.038  0       0       0       58  LEU D O   
2350 C CB  . LEU B 77  ? 0.038  0.038  0.038  0       0       0       58  LEU D CB  
2351 C CG  . LEU B 77  ? 0.0854 0.0854 0.0854 0       0       0       58  LEU D CG  
2352 C CD1 . LEU B 77  ? 0.0871 0.0871 0.0871 0       0       0       58  LEU D CD1 
2353 C CD2 . LEU B 77  ? 0.0762 0.0762 0.0762 0       0       0       58  LEU D CD2 
2354 N N   . LEU B 78  ? 0.038  0.038  0.038  0       0       0       59  LEU D N   
2355 C CA  . LEU B 78  ? 0.038  0.038  0.038  0       0       0       59  LEU D CA  
2356 C C   . LEU B 78  ? 0.0639 0.0639 0.0639 0       0       0       59  LEU D C   
2357 O O   . LEU B 78  ? 0.038  0.038  0.038  0       0       0       59  LEU D O   
2358 C CB  . LEU B 78  ? 0.038  0.038  0.038  0       0       0       59  LEU D CB  
2359 C CG  . LEU B 78  ? 0.0759 0.0759 0.0759 0       0       0       59  LEU D CG  
2360 C CD1 . LEU B 78  ? 0.0734 0.0734 0.0734 0       0       0       59  LEU D CD1 
2361 C CD2 . LEU B 78  ? 0.0838 0.0838 0.0838 0       0       0       59  LEU D CD2 
2362 N N   . ILE B 79  ? 0.038  0.038  0.038  0       0       0       60  ILE D N   
2363 C CA  . ILE B 79  ? 0.038  0.038  0.038  0       0       0       60  ILE D CA  
2364 C C   . ILE B 79  ? 0.0719 0.0719 0.0719 0       0       0       60  ILE D C   
2365 O O   . ILE B 79  ? 0.038  0.038  0.038  0       0       0       60  ILE D O   
2366 C CB  . ILE B 79  ? 0.0498 0.0498 0.0498 0       0       0       60  ILE D CB  
2367 C CG1 . ILE B 79  ? 0.038  0.038  0.038  0       0       0       60  ILE D CG1 
2368 C CG2 . ILE B 79  ? 0.038  0.038  0.038  0       0       0       60  ILE D CG2 
2369 C CD1 . ILE B 79  ? 0.0509 0.0509 0.0509 0       0       0       60  ILE D CD1 
2370 N N   . ASP B 80  ? 0.038  0.038  0.038  0       0       0       61  ASP D N   
2371 C CA  . ASP B 80  ? 0.038  0.038  0.038  0       0       0       61  ASP D CA  
2372 C C   . ASP B 80  ? 0.0661 0.0661 0.0661 0       0       0       61  ASP D C   
2373 O O   . ASP B 80  ? 0.038  0.038  0.038  0       0       0       61  ASP D O   
2374 C CB  . ASP B 80  ? 0.043  0.043  0.043  0       0       0       61  ASP D CB  
2375 C CG  . ASP B 80  ? 0.0911 0.0911 0.0911 0       0       0       61  ASP D CG  
2376 O OD1 . ASP B 80  ? 0.099  0.099  0.099  0       0       0       61  ASP D OD1 
2377 O OD2 . ASP B 80  ? 0.1196 0.1196 0.1196 0       0       0       61  ASP D OD2 
2378 N N   . ILE B 81  ? 0.038  0.038  0.038  0       0       0       62  ILE D N   
2379 C CA  . ILE B 81  ? 0.038  0.038  0.038  0       0       0       62  ILE D CA  
2380 C C   . ILE B 81  ? 0.0567 0.0567 0.0567 0       0       0       62  ILE D C   
2381 O O   . ILE B 81  ? 0.038  0.038  0.038  0       0       0       62  ILE D O   
2382 C CB  . ILE B 81  ? 0.0485 0.0485 0.0485 0       0       0       62  ILE D CB  
2383 C CG1 . ILE B 81  ? 0.0389 0.0389 0.0389 0       0       0       62  ILE D CG1 
2384 C CG2 . ILE B 81  ? 0.038  0.038  0.038  0       0       0       62  ILE D CG2 
2385 C CD1 . ILE B 81  ? 0.0687 0.0687 0.0687 0       0       0       62  ILE D CD1 
2386 N N   . GLY B 82  ? 0.038  0.038  0.038  0       0       0       63  GLY D N   
2387 C CA  . GLY B 82  ? 0.038  0.038  0.038  0       0       0       63  GLY D CA  
2388 C C   . GLY B 82  ? 0.063  0.063  0.063  0       0       0       63  GLY D C   
2389 O O   . GLY B 82  ? 0.038  0.038  0.038  0       0       0       63  GLY D O   
2390 N N   . SER B 83  ? 0.038  0.038  0.038  0       0       0       64  SER D N   
2391 C CA  . SER B 83  ? 0.038  0.038  0.038  0       0       0       64  SER D CA  
2392 C C   . SER B 83  ? 0.0665 0.0665 0.0665 0       0       0       64  SER D C   
2393 O O   . SER B 83  ? 0.038  0.038  0.038  0       0       0       64  SER D O   
2394 C CB  . SER B 83  ? 0.0653 0.0653 0.0653 0       0       0       64  SER D CB  
2395 O OG  . SER B 83  ? 0.0961 0.0961 0.0961 0       0       0       64  SER D OG  
2396 N N   . GLY B 84  ? 0.038  0.038  0.038  0       0       0       65  GLY D N   
2397 C CA  . GLY B 84  ? 0.038  0.038  0.038  0       0       0       65  GLY D CA  
2398 C C   . GLY B 84  ? 0.0668 0.0668 0.0668 0       0       0       65  GLY D C   
2399 O O   . GLY B 84  ? 0.038  0.038  0.038  0       0       0       65  GLY D O   
2400 N N   . PRO B 85  ? 0.038  0.038  0.038  0       0       0       66  PRO D N   
2401 C CA  . PRO B 85  ? 0.038  0.038  0.038  0       0       0       66  PRO D CA  
2402 C C   . PRO B 85  ? 0.0699 0.0699 0.0699 0       0       0       66  PRO D C   
2403 O O   . PRO B 85  ? 0.038  0.038  0.038  0       0       0       66  PRO D O   
2404 C CB  . PRO B 85  ? 0.0509 0.0509 0.0509 0       0       0       66  PRO D CB  
2405 C CG  . PRO B 85  ? 0.0901 0.0901 0.0901 0       0       0       66  PRO D CG  
2406 C CD  . PRO B 85  ? 0.041  0.041  0.041  0       0       0       66  PRO D CD  
2407 N N   . THR B 86  ? 0.038  0.038  0.038  0       0       0       67  THR D N   
2408 C CA  . THR B 86  ? 0.038  0.038  0.038  0       0       0       67  THR D CA  
2409 C C   . THR B 86  ? 0.0664 0.0664 0.0664 0       0       0       67  THR D C   
2410 O O   . THR B 86  ? 0.038  0.038  0.038  0       0       0       67  THR D O   
2411 C CB  . THR B 86  ? 0.0852 0.0852 0.0852 0       0       0       67  THR D CB  
2412 O OG1 . THR B 86  ? 0.0485 0.0485 0.0485 0       0       0       67  THR D OG1 
2413 C CG2 . THR B 86  ? 0.038  0.038  0.038  0       0       0       67  THR D CG2 
2414 N N   . ILE B 87  ? 0.038  0.038  0.038  0       0       0       68  ILE D N   
2415 C CA  . ILE B 87  ? 0.038  0.038  0.038  0       0       0       68  ILE D CA  
2416 C C   . ILE B 87  ? 0.0574 0.0574 0.0574 0       0       0       68  ILE D C   
2417 O O   . ILE B 87  ? 0.038  0.038  0.038  0       0       0       68  ILE D O   
2418 C CB  . ILE B 87  ? 0.0858 0.0858 0.0858 0       0       0       68  ILE D CB  
2419 C CG1 . ILE B 87  ? 0.1033 0.1033 0.1033 0       0       0       68  ILE D CG1 
2420 C CG2 . ILE B 87  ? 0.0972 0.0972 0.0972 0       0       0       68  ILE D CG2 
2421 C CD1 . ILE B 87  ? 0.1558 0.2352 0.1435 -0.043  0.0038  -0.0453 68  ILE D CD1 
2422 N N   . TYR B 88  ? 0.038  0.038  0.038  0       0       0       69  TYR D N   
2423 C CA  . TYR B 88  ? 0.038  0.038  0.038  0       0       0       69  TYR D CA  
2424 C C   . TYR B 88  ? 0.0665 0.0665 0.0665 0       0       0       69  TYR D C   
2425 O O   . TYR B 88  ? 0.038  0.038  0.038  0       0       0       69  TYR D O   
2426 C CB  . TYR B 88  ? 0.0385 0.0385 0.0385 0       0       0       69  TYR D CB  
2427 C CG  . TYR B 88  ? 0.038  0.038  0.038  0       0       0       69  TYR D CG  
2428 C CD1 . TYR B 88  ? 0.0583 0.0583 0.0583 0       0       0       69  TYR D CD1 
2429 C CD2 . TYR B 88  ? 0.038  0.038  0.038  0       0       0       69  TYR D CD2 
2430 C CE1 . TYR B 88  ? 0.038  0.038  0.038  0       0       0       69  TYR D CE1 
2431 C CE2 . TYR B 88  ? 0.038  0.038  0.038  0       0       0       69  TYR D CE2 
2432 C CZ  . TYR B 88  ? 0.0383 0.0383 0.0383 0       0       0       69  TYR D CZ  
2433 O OH  . TYR B 88  ? 0.038  0.038  0.038  0       0       0       69  TYR D OH  
2434 N N   . GLN B 89  ? 0.038  0.038  0.038  0       0       0       70  GLN D N   
2435 C CA  . GLN B 89  ? 0.038  0.038  0.038  0       0       0       70  GLN D CA  
2436 C C   . GLN B 89  ? 0.0619 0.0619 0.0619 0       0       0       70  GLN D C   
2437 O O   . GLN B 89  ? 0.038  0.038  0.038  0       0       0       70  GLN D O   
2438 C CB  . GLN B 89  ? 0.0406 0.0406 0.0406 0       0       0       70  GLN D CB  
2439 C CG  . GLN B 89  ? 0.038  0.038  0.038  0       0       0       70  GLN D CG  
2440 C CD  . GLN B 89  ? 0.0756 0.0756 0.0756 0       0       0       70  GLN D CD  
2441 O OE1 . GLN B 89  ? 0.038  0.038  0.038  0       0       0       70  GLN D OE1 
2442 N NE2 . GLN B 89  ? 0.1167 0.1167 0.1167 0       0       0       70  GLN D NE2 
2443 N N   . LEU B 90  ? 0.038  0.038  0.038  0       0       0       71  LEU D N   
2444 C CA  . LEU B 90  ? 0.038  0.038  0.038  0       0       0       71  LEU D CA  
2445 C C   . LEU B 90  ? 0.0667 0.0667 0.0667 0       0       0       71  LEU D C   
2446 O O   . LEU B 90  ? 0.038  0.038  0.038  0       0       0       71  LEU D O   
2447 C CB  . LEU B 90  ? 0.038  0.038  0.038  0       0       0       71  LEU D CB  
2448 C CG  . LEU B 90  ? 0.0706 0.0706 0.0706 0       0       0       71  LEU D CG  
2449 C CD1 . LEU B 90  ? 0.0716 0.0716 0.0716 0       0       0       71  LEU D CD1 
2450 C CD2 . LEU B 90  ? 0.0738 0.0738 0.0738 0       0       0       71  LEU D CD2 
2451 N N   . LEU B 91  ? 0.038  0.038  0.038  0       0       0       72  LEU D N   
2452 C CA  . LEU B 91  ? 0.0456 0.0456 0.0456 0       0       0       72  LEU D CA  
2453 C C   . LEU B 91  ? 0.0843 0.0843 0.0843 0       0       0       72  LEU D C   
2454 O O   . LEU B 91  ? 0.0871 0.0871 0.0871 0       0       0       72  LEU D O   
2455 C CB  . LEU B 91  ? 0.038  0.038  0.038  0       0       0       72  LEU D CB  
2456 C CG  . LEU B 91  ? 0.0823 0.0823 0.0823 0       0       0       72  LEU D CG  
2457 C CD1 . LEU B 91  ? 0.0767 0.0767 0.0767 0       0       0       72  LEU D CD1 
2458 C CD2 . LEU B 91  ? 0.0914 0.0914 0.0914 0       0       0       72  LEU D CD2 
2459 N N   . SER B 92  ? 0.0492 0.0492 0.0492 0       0       0       73  SER D N   
2460 C CA  . SER B 92  ? 0.038  0.038  0.038  0       0       0       73  SER D CA  
2461 C C   . SER B 92  ? 0.0697 0.0697 0.0697 0       0       0       73  SER D C   
2462 O O   . SER B 92  ? 0.038  0.038  0.038  0       0       0       73  SER D O   
2463 C CB  . SER B 92  ? 0.051  0.051  0.051  0       0       0       73  SER D CB  
2464 O OG  . SER B 92  ? 0.0915 0.0915 0.0915 0       0       0       73  SER D OG  
2465 N N   . ALA B 93  ? 0.038  0.038  0.038  0       0       0       74  ALA D N   
2466 C CA  . ALA B 93  ? 0.038  0.038  0.038  0       0       0       74  ALA D CA  
2467 C C   . ALA B 93  ? 0.0685 0.0685 0.0685 0       0       0       74  ALA D C   
2468 O O   . ALA B 93  ? 0.0435 0.0435 0.0435 0       0       0       74  ALA D O   
2469 C CB  . ALA B 93  ? 0.038  0.038  0.038  0       0       0       74  ALA D CB  
2470 N N   . CYS B 94  ? 0.0683 0.0683 0.0683 0       0       0       75  CYS D N   
2471 C CA  . CYS B 94  ? 0.1037 0.1037 0.1037 0       0       0       75  CYS D CA  
2472 C C   . CYS B 94  ? 0.1024 0.1024 0.1024 0       0       0       75  CYS D C   
2473 O O   . CYS B 94  ? 0.1052 0.1052 0.1052 0       0       0       75  CYS D O   
2474 C CB  . CYS B 94  ? 0.1334 0.1334 0.1334 0       0       0       75  CYS D CB  
2475 S SG  . CYS B 94  ? 0.111  0.111  0.111  0       0       0       75  CYS D SG  
2476 N N   . GLU B 95  ? 0.1019 0.1019 0.1019 0       0       0       76  GLU D N   
2477 C CA  . GLU B 95  ? 0.096  0.096  0.096  0       0       0       76  GLU D CA  
2478 C C   . GLU B 95  ? 0.0997 0.0997 0.0997 0       0       0       76  GLU D C   
2479 O O   . GLU B 95  ? 0.1328 0.1229 0.1124 0.0147  0.0005  0.0003  76  GLU D O   
2480 C CB  . GLU B 95  ? 0.1105 0.1105 0.1105 0       0       0       76  GLU D CB  
2481 C CG  . GLU B 95  ? 0.1559 0.183  0.0883 0.0884  -0.0251 -0.0293 76  GLU D CG  
2482 C CD  . GLU B 95  ? 0.4563 0.4906 0.1817 0.133   -0.0772 -0.0572 76  GLU D CD  
2483 O OE1 . GLU B 95  ? 0.4675 0.4853 0.1254 0.1708  -0.0679 -0.0502 76  GLU D OE1 
2484 O OE2 . GLU B 95  ? 0.2383 0.2735 0.1024 0.1186  -0.0561 -0.054  76  GLU D OE2 
2485 N N   . SER B 96  ? 0.0842 0.0842 0.0842 0       0       0       77  SER D N   
2486 C CA  . SER B 96  ? 0.0832 0.0832 0.0832 0       0       0       77  SER D CA  
2487 C C   . SER B 96  ? 0.0952 0.0952 0.0952 0       0       0       77  SER D C   
2488 O O   . SER B 96  ? 0.0975 0.0975 0.0975 0       0       0       77  SER D O   
2489 C CB  . SER B 96  ? 0.1186 0.1186 0.1186 0       0       0       77  SER D CB  
2490 O OG  . SER B 96  ? 0.1169 0.1169 0.1169 0       0       0       77  SER D OG  
2491 N N   . PHE B 97  ? 0.054  0.054  0.054  0       0       0       78  PHE D N   
2492 C CA  . PHE B 97  ? 0.038  0.038  0.038  0       0       0       78  PHE D CA  
2493 C C   . PHE B 97  ? 0.0871 0.0871 0.0871 0       0       0       78  PHE D C   
2494 O O   . PHE B 97  ? 0.0836 0.0836 0.0836 0       0       0       78  PHE D O   
2495 C CB  . PHE B 97  ? 0.0399 0.0399 0.0399 0       0       0       78  PHE D CB  
2496 C CG  . PHE B 97  ? 0.038  0.038  0.038  0       0       0       78  PHE D CG  
2497 C CD1 . PHE B 97  ? 0.0409 0.0409 0.0409 0       0       0       78  PHE D CD1 
2498 C CD2 . PHE B 97  ? 0.0534 0.0534 0.0534 0       0       0       78  PHE D CD2 
2499 C CE1 . PHE B 97  ? 0.0581 0.0581 0.0581 0       0       0       78  PHE D CE1 
2500 C CE2 . PHE B 97  ? 0.0769 0.0769 0.0769 0       0       0       78  PHE D CE2 
2501 C CZ  . PHE B 97  ? 0.0499 0.0499 0.0499 0       0       0       78  PHE D CZ  
2502 N N   . LYS B 98  ? 0.087  0.087  0.087  0       0       0       79  LYS D N   
2503 C CA  . LYS B 98  ? 0.103  0.103  0.103  0       0       0       79  LYS D CA  
2504 C C   . LYS B 98  ? 0.0871 0.0871 0.0871 0       0       0       79  LYS D C   
2505 O O   . LYS B 98  ? 0.1039 0.1039 0.1039 0       0       0       79  LYS D O   
2506 C CB  . LYS B 98  ? 0.107  0.0837 0.086  0.0015  0.0075  0.0005  79  LYS D CB  
2507 C CG  . LYS B 98  ? 0.5971 0.1964 0.2109 0.0486  0.1354  -0.0764 79  LYS D CG  
2508 C CD  . LYS B 98  ? 0.9042 0.4138 0.4562 0.0713  0.2115  -0.1408 79  LYS D CD  
2509 C CE  . LYS B 98  ? 1.1263 0.5666 0.6285 0.0858  0.2735  -0.2736 79  LYS D CE  
2510 N NZ  . LYS B 98  ? 1.2998 0.6817 0.7725 0.1145  0.362   -0.3312 79  LYS D NZ  
2511 N N   . GLU B 99  ? 0.065  0.065  0.065  0       0       0       80  GLU D N   
2512 C CA  . GLU B 99  ? 0.0579 0.0579 0.0579 0       0       0       80  GLU D CA  
2513 C C   . GLU B 99  ? 0.0717 0.0717 0.0717 0       0       0       80  GLU D C   
2514 O O   . GLU B 99  ? 0.038  0.038  0.038  0       0       0       80  GLU D O   
2515 C CB  . GLU B 99  ? 0.0921 0.0921 0.0921 0       0       0       80  GLU D CB  
2516 C CG  . GLU B 99  ? 0.2268 0.078  0.0882 -0.0552 0.0702  -0.0399 80  GLU D CG  
2517 C CD  . GLU B 99  ? 0.7681 0.4637 0.5002 -0.0513 0.1051  -0.1904 80  GLU D CD  
2518 O OE1 . GLU B 99  ? 0.9222 0.5085 0.575  -0.0321 0.1416  -0.2584 80  GLU D OE1 
2519 O OE2 . GLU B 99  ? 0.5866 0.3989 0.4235 -0.07   0.0931  -0.1121 80  GLU D OE2 
2520 N N   . ILE B 100 ? 0.038  0.038  0.038  0       0       0       81  ILE D N   
2521 C CA  . ILE B 100 ? 0.038  0.038  0.038  0       0       0       81  ILE D CA  
2522 C C   . ILE B 100 ? 0.0698 0.0698 0.0698 0       0       0       81  ILE D C   
2523 O O   . ILE B 100 ? 0.038  0.038  0.038  0       0       0       81  ILE D O   
2524 C CB  . ILE B 100 ? 0.0462 0.0462 0.0462 0       0       0       81  ILE D CB  
2525 C CG1 . ILE B 100 ? 0.038  0.038  0.038  0       0       0       81  ILE D CG1 
2526 C CG2 . ILE B 100 ? 0.038  0.038  0.038  0       0       0       81  ILE D CG2 
2527 C CD1 . ILE B 100 ? 0.038  0.038  0.038  0       0       0       81  ILE D CD1 
2528 N N   . VAL B 101 ? 0.038  0.038  0.038  0       0       0       82  VAL D N   
2529 C CA  . VAL B 101 ? 0.038  0.038  0.038  0       0       0       82  VAL D CA  
2530 C C   . VAL B 101 ? 0.0658 0.0658 0.0658 0       0       0       82  VAL D C   
2531 O O   . VAL B 101 ? 0.038  0.038  0.038  0       0       0       82  VAL D O   
2532 C CB  . VAL B 101 ? 0.0463 0.0463 0.0463 0       0       0       82  VAL D CB  
2533 C CG1 . VAL B 101 ? 0.038  0.038  0.038  0       0       0       82  VAL D CG1 
2534 C CG2 . VAL B 101 ? 0.038  0.038  0.038  0       0       0       82  VAL D CG2 
2535 N N   . VAL B 102 ? 0.038  0.038  0.038  0       0       0       83  VAL D N   
2536 C CA  . VAL B 102 ? 0.038  0.038  0.038  0       0       0       83  VAL D CA  
2537 C C   . VAL B 102 ? 0.0654 0.0654 0.0654 0       0       0       83  VAL D C   
2538 O O   . VAL B 102 ? 0.038  0.038  0.038  0       0       0       83  VAL D O   
2539 C CB  . VAL B 102 ? 0.052  0.052  0.052  0       0       0       83  VAL D CB  
2540 C CG1 . VAL B 102 ? 0.038  0.038  0.038  0       0       0       83  VAL D CG1 
2541 C CG2 . VAL B 102 ? 0.041  0.041  0.041  0       0       0       83  VAL D CG2 
2542 N N   . THR B 103 ? 0.038  0.038  0.038  0       0       0       84  THR D N   
2543 C CA  . THR B 103 ? 0.038  0.038  0.038  0       0       0       84  THR D CA  
2544 C C   . THR B 103 ? 0.0683 0.0683 0.0683 0       0       0       84  THR D C   
2545 O O   . THR B 103 ? 0.038  0.038  0.038  0       0       0       84  THR D O   
2546 C CB  . THR B 103 ? 0.038  0.038  0.038  0       0       0       84  THR D CB  
2547 O OG1 . THR B 103 ? 0.038  0.038  0.038  0       0       0       84  THR D OG1 
2548 C CG2 . THR B 103 ? 0.038  0.038  0.038  0       0       0       84  THR D CG2 
2549 N N   . ASP B 104 ? 0.038  0.038  0.038  0       0       0       85  ASP D N   
2550 C CA  . ASP B 104 ? 0.038  0.038  0.038  0       0       0       85  ASP D CA  
2551 C C   . ASP B 104 ? 0.0634 0.0634 0.0634 0       0       0       85  ASP D C   
2552 O O   . ASP B 104 ? 0.038  0.038  0.038  0       0       0       85  ASP D O   
2553 C CB  . ASP B 104 ? 0.038  0.038  0.038  0       0       0       85  ASP D CB  
2554 C CG  . ASP B 104 ? 0.0385 0.0385 0.0385 0       0       0       85  ASP D CG  
2555 O OD1 . ASP B 104 ? 0.038  0.038  0.038  0       0       0       85  ASP D OD1 
2556 O OD2 . ASP B 104 ? 0.038  0.038  0.038  0       0       0       85  ASP D OD2 
2557 N N   . TYR B 105 ? 0.038  0.038  0.038  0       0       0       86  TYR D N   
2558 C CA  . TYR B 105 ? 0.038  0.038  0.038  0       0       0       86  TYR D CA  
2559 C C   . TYR B 105 ? 0.0703 0.0703 0.0703 0       0       0       86  TYR D C   
2560 O O   . TYR B 105 ? 0.038  0.038  0.038  0       0       0       86  TYR D O   
2561 C CB  . TYR B 105 ? 0.038  0.038  0.038  0       0       0       86  TYR D CB  
2562 C CG  . TYR B 105 ? 0.038  0.038  0.038  0       0       0       86  TYR D CG  
2563 C CD1 . TYR B 105 ? 0.0509 0.0509 0.0509 0       0       0       86  TYR D CD1 
2564 C CD2 . TYR B 105 ? 0.047  0.047  0.047  0       0       0       86  TYR D CD2 
2565 C CE1 . TYR B 105 ? 0.0596 0.0596 0.0596 0       0       0       86  TYR D CE1 
2566 C CE2 . TYR B 105 ? 0.0525 0.0525 0.0525 0       0       0       86  TYR D CE2 
2567 C CZ  . TYR B 105 ? 0.079  0.079  0.079  0       0       0       86  TYR D CZ  
2568 O OH  . TYR B 105 ? 0.0993 0.0993 0.0993 0       0       0       86  TYR D OH  
2569 N N   . SER B 106 ? 0.038  0.038  0.038  0       0       0       87  SER D N   
2570 C CA  . SER B 106 ? 0.038  0.038  0.038  0       0       0       87  SER D CA  
2571 C C   . SER B 106 ? 0.0663 0.0663 0.0663 0       0       0       87  SER D C   
2572 O O   . SER B 106 ? 0.038  0.038  0.038  0       0       0       87  SER D O   
2573 C CB  . SER B 106 ? 0.0803 0.0803 0.0803 0       0       0       87  SER D CB  
2574 O OG  . SER B 106 ? 0.093  0.093  0.093  0       0       0       87  SER D OG  
2575 N N   . ASP B 107 ? 0.038  0.038  0.038  0       0       0       88  ASP D N   
2576 C CA  . ASP B 107 ? 0.0531 0.0531 0.0531 0       0       0       88  ASP D CA  
2577 C C   . ASP B 107 ? 0.0669 0.0669 0.0669 0       0       0       88  ASP D C   
2578 O O   . ASP B 107 ? 0.0542 0.0542 0.0542 0       0       0       88  ASP D O   
2579 C CB  . ASP B 107 ? 0.1156 0.1156 0.1156 0       0       0       88  ASP D CB  
2580 C CG  . ASP B 107 ? 0.1751 0.1683 0.1448 -0.0549 0.0405  -0.0381 88  ASP D CG  
2581 O OD1 . ASP B 107 ? 0.2001 0.199  0.171  -0.0548 0.0381  -0.0378 88  ASP D OD1 
2582 O OD2 . ASP B 107 ? 0.3298 0.3111 0.206  -0.0646 0.0827  -0.1155 88  ASP D OD2 
2583 N N   . GLN B 108 ? 0.038  0.038  0.038  0       0       0       89  GLN D N   
2584 C CA  . GLN B 108 ? 0.038  0.038  0.038  0       0       0       89  GLN D CA  
2585 C C   . GLN B 108 ? 0.066  0.066  0.066  0       0       0       89  GLN D C   
2586 O O   . GLN B 108 ? 0.038  0.038  0.038  0       0       0       89  GLN D O   
2587 C CB  . GLN B 108 ? 0.0693 0.0693 0.0693 0       0       0       89  GLN D CB  
2588 C CG  . GLN B 108 ? 0.2535 0.1399 0.1612 -0.1419 0.1568  -0.1061 89  GLN D CG  
2589 C CD  . GLN B 108 ? 0.605  0.4669 0.4455 -0.1203 0.2345  -0.1634 89  GLN D CD  
2590 O OE1 . GLN B 108 ? 0.5575 0.4198 0.4271 -0.0978 0.2185  -0.1436 89  GLN D OE1 
2591 N NE2 . GLN B 108 ? 0.5526 0.4001 0.4089 -0.1506 0.2539  -0.1685 89  GLN D NE2 
2592 N N   . ASN B 109 ? 0.038  0.038  0.038  0       0       0       90  ASN D N   
2593 C CA  . ASN B 109 ? 0.038  0.038  0.038  0       0       0       90  ASN D CA  
2594 C C   . ASN B 109 ? 0.0588 0.0588 0.0588 0       0       0       90  ASN D C   
2595 O O   . ASN B 109 ? 0.0518 0.0518 0.0518 0       0       0       90  ASN D O   
2596 C CB  . ASN B 109 ? 0.038  0.038  0.038  0       0       0       90  ASN D CB  
2597 C CG  . ASN B 109 ? 0.0687 0.0687 0.0687 0       0       0       90  ASN D CG  
2598 O OD1 . ASN B 109 ? 0.038  0.038  0.038  0       0       0       90  ASN D OD1 
2599 N ND2 . ASN B 109 ? 0.038  0.038  0.038  0       0       0       90  ASN D ND2 
2600 N N   . LEU B 110 ? 0.038  0.038  0.038  0       0       0       91  LEU D N   
2601 C CA  . LEU B 110 ? 0.038  0.038  0.038  0       0       0       91  LEU D CA  
2602 C C   . LEU B 110 ? 0.0635 0.0635 0.0635 0       0       0       91  LEU D C   
2603 O O   . LEU B 110 ? 0.038  0.038  0.038  0       0       0       91  LEU D O   
2604 C CB  . LEU B 110 ? 0.038  0.038  0.038  0       0       0       91  LEU D CB  
2605 C CG  . LEU B 110 ? 0.0759 0.0759 0.0759 0       0       0       91  LEU D CG  
2606 C CD1 . LEU B 110 ? 0.0706 0.0706 0.0706 0       0       0       91  LEU D CD1 
2607 C CD2 . LEU B 110 ? 0.0875 0.0875 0.0875 0       0       0       91  LEU D CD2 
2608 N N   . GLN B 111 ? 0.038  0.038  0.038  0       0       0       92  GLN D N   
2609 C CA  . GLN B 111 ? 0.0459 0.0459 0.0459 0       0       0       92  GLN D CA  
2610 C C   . GLN B 111 ? 0.0874 0.0874 0.0874 0       0       0       92  GLN D C   
2611 O O   . GLN B 111 ? 0.0685 0.0685 0.0685 0       0       0       92  GLN D O   
2612 C CB  . GLN B 111 ? 0.0766 0.0766 0.0766 0       0       0       92  GLN D CB  
2613 C CG  . GLN B 111 ? 0.2707 0.1703 0.0961 -0.166  0.1048  -0.0778 92  GLN D CG  
2614 C CD  . GLN B 111 ? 0.7076 0.5606 0.4894 -0.2128 0.155   -0.1105 92  GLN D CD  
2615 O OE1 . GLN B 111 ? 0.703  0.5349 0.4724 -0.2361 0.1866  -0.1316 92  GLN D OE1 
2616 N NE2 . GLN B 111 ? 0.6601 0.5062 0.4468 -0.2013 0.1523  -0.1053 92  GLN D NE2 
2617 N N   . GLU B 112 ? 0.0485 0.0485 0.0485 0       0       0       93  GLU D N   
2618 C CA  . GLU B 112 ? 0.0593 0.0593 0.0593 0       0       0       93  GLU D CA  
2619 C C   . GLU B 112 ? 0.0996 0.0996 0.0996 0       0       0       93  GLU D C   
2620 O O   . GLU B 112 ? 0.1095 0.1095 0.1095 0       0       0       93  GLU D O   
2621 C CB  . GLU B 112 ? 0.0761 0.0761 0.0761 0       0       0       93  GLU D CB  
2622 C CG  . GLU B 112 ? 0.1002 0.1002 0.1002 0       0       0       93  GLU D CG  
2623 C CD  . GLU B 112 ? 0.1714 0.2051 0.1255 -0.1213 0.0794  -0.0912 93  GLU D CD  
2624 O OE1 . GLU B 112 ? 0.1277 0.128  0.1269 -0.002  0.0014  -0.0015 93  GLU D OE1 
2625 O OE2 . GLU B 112 ? 0.1453 0.1494 0.142  -0.0101 0.0064  -0.0078 93  GLU D OE2 
2626 N N   . LEU B 113 ? 0.1309 0.1309 0.1309 0       0       0       94  LEU D N   
2627 C CA  . LEU B 113 ? 0.1568 0.1568 0.1568 0       0       0       94  LEU D CA  
2628 C C   . LEU B 113 ? 0.1159 0.1159 0.1159 0       0       0       94  LEU D C   
2629 O O   . LEU B 113 ? 0.1209 0.1209 0.1209 0       0       0       94  LEU D O   
2630 C CB  . LEU B 113 ? 0.161  0.161  0.161  0       0       0       94  LEU D CB  
2631 C CG  . LEU B 113 ? 0.1086 0.1086 0.1086 0       0       0       94  LEU D CG  
2632 C CD1 . LEU B 113 ? 0.113  0.113  0.113  0       0       0       94  LEU D CD1 
2633 C CD2 . LEU B 113 ? 0.1158 0.1177 0.1022 -0.0164 0.0053  -0.0056 94  LEU D CD2 
2634 N N   . GLU B 114 ? 0.1487 0.1487 0.1487 0       0       0       95  GLU D N   
2635 C CA  . GLU B 114 ? 0.1456 0.1456 0.1456 0       0       0       95  GLU D CA  
2636 C C   . GLU B 114 ? 0.1007 0.1007 0.1007 0       0       0       95  GLU D C   
2637 O O   . GLU B 114 ? 0.1199 0.1199 0.1199 0       0       0       95  GLU D O   
2638 C CB  . GLU B 114 ? 0.1295 0.1295 0.1295 0       0       0       95  GLU D CB  
2639 C CG  . GLU B 114 ? 0.2427 0.1327 0.0509 -0.1338 0.0396  -0.0266 95  GLU D CG  
2640 C CD  . GLU B 114 ? 0.7773 0.5382 0.5042 -0.2104 -0.0038 -0.1464 95  GLU D CD  
2641 O OE1 . GLU B 114 ? 0.9131 0.6433 0.6217 -0.2402 -0.0097 -0.1943 95  GLU D OE1 
2642 O OE2 . GLU B 114 ? 0.7639 0.4995 0.4809 -0.2024 -0.0056 -0.145  95  GLU D OE2 
2643 N N   . LYS B 115 ? 0.1228 0.1228 0.1228 0       0       0       96  LYS D N   
2644 C CA  . LYS B 115 ? 0.1168 0.1168 0.1168 0       0       0       96  LYS D CA  
2645 C C   . LYS B 115 ? 0.1076 0.1068 0.0975 -0.011  0.0039  -0.0037 96  LYS D C   
2646 O O   . LYS B 115 ? 0.1211 0.1205 0.114  -0.0076 0.0025  -0.0024 96  LYS D O   
2647 C CB  . LYS B 115 ? 0.1417 0.1417 0.1417 0       0       0       96  LYS D CB  
2648 C CG  . LYS B 115 ? 0.2619 0.245  0.1777 -0.099  0.0505  -0.0463 96  LYS D CG  
2649 C CD  . LYS B 115 ? 0.3976 0.377  0.2554 -0.1946 0.1136  -0.1078 96  LYS D CD  
2650 C CE  . LYS B 115 ? 0.5696 0.4768 0.3374 -0.3267 0.189   -0.1894 96  LYS D CE  
2651 N NZ  . LYS B 115 ? 0.7663 0.6833 0.5508 -0.3355 0.2342  -0.2159 96  LYS D NZ  
2652 N N   . TRP B 116 ? 0.0761 0.0761 0.0761 0       0       0       97  TRP D N   
2653 C CA  . TRP B 116 ? 0.0545 0.0545 0.0545 0       0       0       97  TRP D CA  
2654 C C   . TRP B 116 ? 0.1014 0.1014 0.1014 0       0       0       97  TRP D C   
2655 O O   . TRP B 116 ? 0.0625 0.0625 0.0625 0       0       0       97  TRP D O   
2656 C CB  . TRP B 116 ? 0.039  0.039  0.039  0       0       0       97  TRP D CB  
2657 C CG  . TRP B 116 ? 0.0481 0.0481 0.0481 0       0       0       97  TRP D CG  
2658 C CD1 . TRP B 116 ? 0.0875 0.0931 0.0849 -0.006  0.0022  -0.0034 97  TRP D CD1 
2659 C CD2 . TRP B 116 ? 0.0408 0.0408 0.0408 0       0       0       97  TRP D CD2 
2660 N NE1 . TRP B 116 ? 0.0876 0.1006 0.0836 -0.0109 0.0038  -0.0066 97  TRP D NE1 
2661 C CE2 . TRP B 116 ? 0.0924 0.0924 0.0924 0       0       0       97  TRP D CE2 
2662 C CE3 . TRP B 116 ? 0.0501 0.0501 0.0501 0       0       0       97  TRP D CE3 
2663 C CZ2 . TRP B 116 ? 0.0858 0.0858 0.0858 0       0       0       97  TRP D CZ2 
2664 C CZ3 . TRP B 116 ? 0.0741 0.0741 0.0741 0       0       0       97  TRP D CZ3 
2665 C CH2 . TRP B 116 ? 0.0822 0.0822 0.0822 0       0       0       97  TRP D CH2 
2666 N N   . LEU B 117 ? 0.0998 0.0998 0.0998 0       0       0       98  LEU D N   
2667 C CA  . LEU B 117 ? 0.1275 0.1275 0.1275 0       0       0       98  LEU D CA  
2668 C C   . LEU B 117 ? 0.1333 0.1245 0.1164 -0.0117 0.001   -0.0007 98  LEU D C   
2669 O O   . LEU B 117 ? 0.134  0.1298 0.1271 -0.0044 0.0001  0       98  LEU D O   
2670 C CB  . LEU B 117 ? 0.1386 0.1386 0.1386 0       0       0       98  LEU D CB  
2671 C CG  . LEU B 117 ? 0.1061 0.1061 0.1061 0       0       0       98  LEU D CG  
2672 C CD1 . LEU B 117 ? 0.1035 0.1035 0.1035 0       0       0       98  LEU D CD1 
2673 C CD2 . LEU B 117 ? 0.1091 0.1091 0.1091 0       0       0       98  LEU D CD2 
2674 N N   . LYS B 118 ? 0.152  0.152  0.152  0       0       0       99  LYS D N   
2675 C CA  . LYS B 118 ? 0.1845 0.1658 0.148  -0.0259 0.0038  -0.0026 99  LYS D CA  
2676 C C   . LYS B 118 ? 0.2807 0.2332 0.1624 -0.0939 0.0165  -0.0129 99  LYS D C   
2677 O O   . LYS B 118 ? 0.3002 0.2415 0.1596 -0.1101 0.0196  -0.0151 99  LYS D O   
2678 C CB  . LYS B 118 ? 0.2008 0.1654 0.1348 -0.0462 0.0088  -0.006  99  LYS D CB  
2679 C CG  . LYS B 118 ? 0.4255 0.2941 0.2149 -0.1317 0.0218  -0.0135 99  LYS D CG  
2680 C CD  . LYS B 118 ? 0.5648 0.3508 0.2346 -0.2178 0.0428  -0.0383 99  LYS D CD  
2681 C CE  . LYS B 118 ? 0.7894 0.5022 0.4477 -0.2343 0.0181  -0.0738 99  LYS D CE  
2682 N NZ  . LYS B 118 ? 0.9294 0.5668 0.5806 -0.2911 0.0072  -0.1351 99  LYS D NZ  
2683 N N   . ALA B 119 ? 0.2683 0.2433 0.1686 -0.0895 0.0182  -0.0158 100 ALA D N   
2684 C CA  . ALA B 119 ? 0.2891 0.2852 0.1752 -0.1188 0.0288  -0.0283 100 ALA D CA  
2685 C C   . ALA B 119 ? 0.3625 0.3626 0.1963 -0.1817 0.0531  -0.0531 100 ALA D C   
2686 O O   . ALA B 119 ? 0.3819 0.393  0.1981 -0.2084 0.0623  -0.064  100 ALA D O   
2687 C CB  . ALA B 119 ? 0.3028 0.2973 0.1768 -0.1284 0.0257  -0.0252 100 ALA D CB  
2688 N N   . ALA B 120 ? 0.3446 0.3368 0.1994 -0.1576 0.0514  -0.0501 101 ALA D N   
2689 C CA  . ALA B 120 ? 0.3585 0.3482 0.2003 -0.1773 0.0665  -0.0646 101 ALA D CA  
2690 C C   . ALA B 120 ? 0.4018 0.4304 0.2247 -0.2353 0.0991  -0.1053 101 ALA D C   
2691 O O   . ALA B 120 ? 0.3931 0.4576 0.233  -0.2392 0.1013  -0.1159 101 ALA D O   
2692 C CB  . ALA B 120 ? 0.3596 0.3345 0.2114 -0.1587 0.0637  -0.0589 101 ALA D CB  
2693 N N   . PRO B 121 ? 0.397  0.4232 0.2227 -0.2401 0.1098  -0.116  102 PRO D N   
2694 C CA  . PRO B 121 ? 0.3973 0.4617 0.2389 -0.261  0.1292  -0.1461 102 PRO D CA  
2695 C C   . PRO B 121 ? 0.3843 0.4643 0.2494 -0.2587 0.1388  -0.1619 102 PRO D C   
2696 O O   . PRO B 121 ? 0.3884 0.5118 0.2736 -0.2729 0.1501  -0.1878 102 PRO D O   
2697 C CB  . PRO B 121 ? 0.4408 0.4897 0.2592 -0.2916 0.1525  -0.1658 102 PRO D CB  
2698 C CG  . PRO B 121 ? 0.4715 0.4732 0.2537 -0.3001 0.1562  -0.1566 102 PRO D CG  
2699 C CD  . PRO B 121 ? 0.4287 0.4213 0.2247 -0.2542 0.118   -0.1163 102 PRO D CD  
2700 N N   . ALA B 122 ? 0.329  0.3707 0.2142 -0.2055 0.1147  -0.127  103 ALA D N   
2701 C CA  . ALA B 122 ? 0.3006 0.3453 0.2108 -0.188  0.1135  -0.1278 103 ALA D CA  
2702 C C   . ALA B 122 ? 0.2438 0.2972 0.1707 -0.1616 0.0937  -0.1104 103 ALA D C   
2703 O O   . ALA B 122 ? 0.2326 0.2837 0.1727 -0.151  0.093   -0.11   103 ALA D O   
2704 C CB  . ALA B 122 ? 0.3134 0.3278 0.2208 -0.1791 0.1169  -0.1217 103 ALA D CB  
2705 N N   . ALA B 123 ? 0.1872 0.231  0.1335 -0.1103 0.0578  -0.0704 104 ALA D N   
2706 C CA  . ALA B 123 ? 0.1643 0.2012 0.1295 -0.0746 0.0371  -0.0473 104 ALA D CA  
2707 C C   . ALA B 123 ? 0.1361 0.2019 0.1078 -0.0911 0.0477  -0.068  104 ALA D C   
2708 O O   . ALA B 123 ? 0.1399 0.2244 0.1155 -0.1021 0.0548  -0.0819 104 ALA D O   
2709 C CB  . ALA B 123 ? 0.1626 0.1971 0.124  -0.0709 0.0309  -0.0393 104 ALA D CB  
2710 N N   . PHE B 124 ? 0.0996 0.1347 0.0887 -0.0435 0.0232  -0.0344 105 PHE D N   
2711 C CA  . PHE B 124 ? 0.0689 0.123  0.0648 -0.0513 0.0288  -0.0477 105 PHE D CA  
2712 C C   . PHE B 124 ? 0.0997 0.1773 0.0983 -0.0589 0.031   -0.0575 105 PHE D C   
2713 O O   . PHE B 124 ? 0.0647 0.1288 0.0591 -0.0492 0.0237  -0.0437 105 PHE D O   
2714 C CB  . PHE B 124 ? 0.0623 0.0956 0.0619 -0.03   0.0175  -0.0297 105 PHE D CB  
2715 C CG  . PHE B 124 ? 0.0693 0.1193 0.0767 -0.0363 0.0225  -0.0427 105 PHE D CG  
2716 C CD1 . PHE B 124 ? 0.1065 0.1778 0.1224 -0.0544 0.0365  -0.0676 105 PHE D CD1 
2717 C CD2 . PHE B 124 ? 0.094  0.1417 0.1034 -0.0276 0.0167  -0.0365 105 PHE D CD2 
2718 C CE1 . PHE B 124 ? 0.0988 0.1949 0.1304 -0.0628 0.0441  -0.0893 105 PHE D CE1 
2719 C CE2 . PHE B 124 ? 0.0866 0.1754 0.1129 -0.0431 0.0277  -0.0681 105 PHE D CE2 
2720 C CZ  . PHE B 124 ? 0.0977 0.1863 0.1291 -0.0464 0.0319  -0.0745 105 PHE D CZ  
2721 N N   . ASP B 125 ? 0.0868 0.2049 0.0965 -0.0757 0.0415  -0.085  106 ASP D N   
2722 C CA  . ASP B 125 ? 0.0849 0.2437 0.1031 -0.0825 0.0432  -0.1016 106 ASP D CA  
2723 C C   . ASP B 125 ? 0.0959 0.2489 0.1209 -0.0647 0.034   -0.0928 106 ASP D C   
2724 O O   . ASP B 125 ? 0.0773 0.2449 0.1147 -0.0642 0.0359  -0.1058 106 ASP D O   
2725 C CB  . ASP B 125 ? 0.1109 0.3385 0.1459 -0.1122 0.0611  -0.1489 106 ASP D CB  
2726 C CG  . ASP B 125 ? 0.1445 0.5741 0.2162 -0.1733 0.0902  -0.2555 106 ASP D CG  
2727 O OD1 . ASP B 125 ? 0.1467 0.562  0.2046 -0.1564 0.0759  -0.227  106 ASP D OD1 
2728 O OD2 . ASP B 125 ? 0.2274 0.7743 0.3197 -0.2147 0.0972  -0.3522 106 ASP D OD2 
2729 N N   . TRP B 126 ? 0.0555 0.1823 0.0727 -0.0503 0.0247  -0.0707 107 TRP D N   
2730 C CA  . TRP B 126 ? 0.054  0.1673 0.0736 -0.0353 0.0173  -0.0605 107 TRP D CA  
2731 C C   . TRP B 126 ? 0.0793 0.2475 0.1112 -0.0379 0.0181  -0.084  107 TRP D C   
2732 O O   . TRP B 126 ? 0.042  0.2041 0.0764 -0.0257 0.0124  -0.0799 107 TRP D O   
2733 C CB  . TRP B 126 ? 0.044  0.1    0.0512 -0.0192 0.0089  -0.0286 107 TRP D CB  
2734 C CG  . TRP B 126 ? 0.046  0.0625 0.0477 -0.0071 0.0034  -0.0091 107 TRP D CG  
2735 C CD1 . TRP B 126 ? 0.0763 0.0771 0.0763 -0.0004 0.0002  -0.0004 107 TRP D CD1 
2736 C CD2 . TRP B 126 ? 0.038  0.038  0.038  0       0       0       107 TRP D CD2 
2737 N NE1 . TRP B 126 ? 0.0625 0.0625 0.0625 0       0       0       107 TRP D NE1 
2738 C CE2 . TRP B 126 ? 0.0796 0.0796 0.0796 0       0       0       107 TRP D CE2 
2739 C CE3 . TRP B 126 ? 0.0465 0.0465 0.0465 0       0       0       107 TRP D CE3 
2740 C CZ2 . TRP B 126 ? 0.0654 0.0654 0.0654 0       0       0       107 TRP D CZ2 
2741 C CZ3 . TRP B 126 ? 0.0571 0.0571 0.0571 0       0       0       107 TRP D CZ3 
2742 C CH2 . TRP B 126 ? 0.061  0.061  0.061  0       0       0       107 TRP D CH2 
2743 N N   . SER B 127 ? 0.0505 0.2722 0.0889 -0.0518 0.024   -0.1079 108 SER D N   
2744 C CA  . SER B 127 ? 0.0529 0.3436 0.1048 -0.0493 0.0221  -0.134  108 SER D CA  
2745 C C   . SER B 127 ? 0.067  0.4244 0.1416 -0.0401 0.0188  -0.1691 108 SER D C   
2746 O O   . SER B 127 ? 0.0586 0.4498 0.1369 -0.0226 0.0102  -0.1768 108 SER D O   
2747 C CB  . SER B 127 ? 0.0714 0.4703 0.1375 -0.0778 0.0344  -0.1827 108 SER D CB  
2748 O OG  . SER B 127 ? 0.1119 0.6521 0.2126 -0.1173 0.0552  -0.2657 108 SER D OG  
2749 N N   . PRO B 128 ? 0.0589 0.388  0.1382 -0.0409 0.0205  -0.1678 109 PRO D N   
2750 C CA  . PRO B 128 ? 0.0534 0.4069 0.1467 -0.0272 0.0141  -0.1841 109 PRO D CA  
2751 C C   . PRO B 128 ? 0.0563 0.3727 0.1421 -0.0115 0.006   -0.1652 109 PRO D C   
2752 O O   . PRO B 128 ? 0.0589 0.3728 0.1432 0.0036  -0.0018 -0.1627 109 PRO D O   
2753 C CB  . PRO B 128 ? 0.048  0.4317 0.1645 -0.0414 0.0231  -0.2166 109 PRO D CB  
2754 C CG  . PRO B 128 ? 0.052  0.4788 0.1775 -0.0716 0.04    -0.2453 109 PRO D CG  
2755 C CD  . PRO B 128 ? 0.0532 0.3895 0.1403 -0.0616 0.0327  -0.1845 109 PRO D CD  
2756 N N   . VAL B 129 ? 0.0484 0.2629 0.1079 -0.0125 0.0066  -0.1139 110 VAL D N   
2757 C CA  . VAL B 129 ? 0.0381 0.1894 0.0817 -0.003  0.0016  -0.0814 110 VAL D CA  
2758 C C   . VAL B 129 ? 0.0561 0.2105 0.094  0.0035  -0.0017 -0.0766 110 VAL D C   
2759 O O   . VAL B 129 ? 0.0396 0.1841 0.0742 0.0117  -0.0058 -0.0718 110 VAL D O   
2760 C CB  . VAL B 129 ? 0.077  0.1635 0.1039 -0.0054 0.003   -0.0487 110 VAL D CB  
2761 C CG1 . VAL B 129 ? 0.0695 0.0977 0.0787 -0.0005 0.0003  -0.0161 110 VAL D CG1 
2762 C CG2 . VAL B 129 ? 0.0698 0.1582 0.1023 -0.0081 0.0049  -0.0544 110 VAL D CG2 
2763 N N   . VAL B 130 ? 0.038  0.2073 0.0747 -0.001  0.0005  -0.0788 111 VAL D N   
2764 C CA  . VAL B 130 ? 0.0382 0.2139 0.0711 0.0065  -0.0028 -0.0763 111 VAL D CA  
2765 C C   . VAL B 130 ? 0.0745 0.3231 0.1167 0.0232  -0.0098 -0.1056 111 VAL D C   
2766 O O   . VAL B 130 ? 0.0668 0.3025 0.1009 0.037   -0.015  -0.098  111 VAL D O   
2767 C CB  . VAL B 130 ? 0.0729 0.2673 0.106  -0.003  0.0012  -0.0802 111 VAL D CB  
2768 C CG1 . VAL B 130 ? 0.0825 0.2841 0.113  0.0087  -0.0034 -0.0789 111 VAL D CG1 
2769 C CG2 . VAL B 130 ? 0.0826 0.188  0.0998 -0.0096 0.0039  -0.0437 111 VAL D CG2 
2770 N N   . THR B 131 ? 0.0395 0.356  0.0958 0.0221  -0.0094 -0.1355 112 THR D N   
2771 C CA  . THR B 131 ? 0.0423 0.4393 0.1068 0.0417  -0.0173 -0.1661 112 THR D CA  
2772 C C   . THR B 131 ? 0.0727 0.4663 0.136  0.0571  -0.0241 -0.1694 112 THR D C   
2773 O O   . THR B 131 ? 0.0874 0.5071 0.141  0.0793  -0.0322 -0.1729 112 THR D O   
2774 C CB  . THR B 131 ? 0.0591 0.5695 0.1493 0.0347  -0.0148 -0.2179 112 THR D CB  
2775 O OG1 . THR B 131 ? 0.0386 0.54   0.1242 0.017   -0.007  -0.208  112 THR D OG1 
2776 C CG2 . THR B 131 ? 0.069  0.6655 0.1609 0.0556  -0.0293 -0.2524 112 THR D CG2 
2777 N N   . TYR B 132 ? 0.0431 0.3576 0.1045 0.0403  -0.0184 -0.1458 113 TYR D N   
2778 C CA  . TYR B 132 ? 0.0451 0.3231 0.1018 0.045   -0.0213 -0.1348 113 TYR D CA  
2779 C C   . TYR B 132 ? 0.0837 0.3128 0.1219 0.0483  -0.0217 -0.1071 113 TYR D C   
2780 O O   . TYR B 132 ? 0.0655 0.3083 0.0987 0.06    -0.0257 -0.1101 113 TYR D O   
2781 C CB  . TYR B 132 ? 0.0517 0.2754 0.1107 0.0309  -0.0163 -0.12   113 TYR D CB  
2782 C CG  . TYR B 132 ? 0.0764 0.2728 0.134  0.0344  -0.0192 -0.1132 113 TYR D CG  
2783 C CD1 . TYR B 132 ? 0.0643 0.3364 0.149  0.0473  -0.0272 -0.161  113 TYR D CD1 
2784 C CD2 . TYR B 132 ? 0.0886 0.2117 0.1272 0.0265  -0.0155 -0.0752 113 TYR D CD2 
2785 C CE1 . TYR B 132 ? 0.0648 0.3138 0.152  0.0523  -0.0321 -0.1593 113 TYR D CE1 
2786 C CE2 . TYR B 132 ? 0.0921 0.1922 0.1283 0.0264  -0.0167 -0.0675 113 TYR D CE2 
2787 C CZ  . TYR B 132 ? 0.0912 0.3037 0.1602 0.0452  -0.0513 -0.1511 113 TYR D CZ  
2788 O OH  . TYR B 132 ? 0.1123 0.2877 0.18   0.0446  -0.0566 -0.1405 113 TYR D OH  
2789 N N   . VAL B 133 ? 0.0456 0.2236 0.0748 0.0375  -0.0167 -0.0826 114 VAL D N   
2790 C CA  . VAL B 133 ? 0.0469 0.1816 0.0635 0.0358  -0.0151 -0.0606 114 VAL D CA  
2791 C C   . VAL B 133 ? 0.0818 0.2712 0.0935 0.0593  -0.0221 -0.0771 114 VAL D C   
2792 O O   . VAL B 133 ? 0.0635 0.2476 0.0662 0.0665  -0.0228 -0.0704 114 VAL D O   
2793 C CB  . VAL B 133 ? 0.0789 0.1532 0.0894 0.0194  -0.0085 -0.0348 114 VAL D CB  
2794 C CG1 . VAL B 133 ? 0.0784 0.1206 0.082  0.0147  -0.0061 -0.0195 114 VAL D CG1 
2795 C CG2 . VAL B 133 ? 0.0677 0.0942 0.0732 0.0058  -0.0029 -0.0136 114 VAL D CG2 
2796 N N   . CYS B 134 ? 0.0578 0.3044 0.0736 0.0727  -0.0266 -0.0973 115 CYS D N   
2797 C CA  . CYS B 134 ? 0.0769 0.3832 0.0821 0.1038  -0.0343 -0.1118 115 CYS D CA  
2798 C C   . CYS B 134 ? 0.1302 0.5065 0.1182 0.1284  -0.0497 -0.1313 115 CYS D C   
2799 O O   . CYS B 134 ? 0.143  0.5316 0.1077 0.1531  -0.0539 -0.1239 115 CYS D O   
2800 C CB  . CYS B 134 ? 0.0811 0.4435 0.094  0.1099  -0.0366 -0.131  115 CYS D CB  
2801 S SG  . CYS B 134 ? 0.1195 0.4259 0.1298 0.0917  -0.0341 -0.115  115 CYS D SG  
2802 N N   . ASP B 135 ? 0.1186 0.5063 0.1332 0.1182  -0.0398 -0.1418 116 ASP D N   
2803 C CA  . ASP B 135 ? 0.1329 0.5729 0.1375 0.135   -0.0519 -0.1579 116 ASP D CA  
2804 C C   . ASP B 135 ? 0.1796 0.5844 0.1464 0.1295  -0.072  -0.1386 116 ASP D C   
2805 O O   . ASP B 135 ? 0.197  0.6385 0.1392 0.1524  -0.0809 -0.1344 116 ASP D O   
2806 C CB  . ASP B 135 ? 0.1438 0.6185 0.1543 0.1195  -0.0706 -0.1891 116 ASP D CB  
2807 C CG  . ASP B 135 ? 0.3254 0.9195 0.2516 0.0926  -0.1725 -0.2607 116 ASP D CG  
2808 O OD1 . ASP B 135 ? 0.3442 1.0035 0.2416 0.1108  -0.1885 -0.2722 116 ASP D OD1 
2809 O OD2 . ASP B 135 ? 0.4222 1.0344 0.3286 0.0531  -0.2161 -0.3072 116 ASP D OD2 
2810 N N   . LEU B 136 ? 0.1289 0.4357 0.1342 0.1033  -0.0341 -0.1117 117 LEU D N   
2811 C CA  . LEU B 136 ? 0.1304 0.3757 0.1289 0.0863  -0.0266 -0.084  117 LEU D CA  
2812 C C   . LEU B 136 ? 0.1541 0.4478 0.1114 0.1115  -0.0474 -0.0804 117 LEU D C   
2813 O O   . LEU B 136 ? 0.1419 0.4415 0.0999 0.1189  -0.0351 -0.0672 117 LEU D O   
2814 C CB  . LEU B 136 ? 0.1247 0.2754 0.1293 0.0503  -0.0174 -0.0575 117 LEU D CB  
2815 C CG  . LEU B 136 ? 0.114  0.289  0.1331 0.0543  -0.0231 -0.0811 117 LEU D CG  
2816 C CD1 . LEU B 136 ? 0.1116 0.2019 0.1258 0.0285  -0.0136 -0.047  117 LEU D CD1 
2817 C CD2 . LEU B 136 ? 0.1418 0.333  0.153  0.0518  -0.045  -0.0947 117 LEU D CD2 
2818 N N   . GLU B 137 ? 0.1448 0.4295 0.1077 0.1216  -0.0379 -0.0799 118 GLU D N   
2819 C CA  . GLU B 137 ? 0.1619 0.4492 0.093  0.1448  -0.0419 -0.0673 118 GLU D CA  
2820 C C   . GLU B 137 ? 0.2887 0.6521 0.1326 0.1921  -0.0799 -0.0667 118 GLU D C   
2821 O O   . GLU B 137 ? 0.3104 0.6657 0.1249 0.223   -0.0716 -0.0539 118 GLU D O   
2822 C CB  . GLU B 137 ? 0.1715 0.4201 0.0983 0.1367  -0.0453 -0.0674 118 GLU D CB  
2823 C CG  . GLU B 137 ? 0.2596 0.4725 0.1416 0.0989  -0.0793 -0.063  118 GLU D CG  
2824 C CD  . GLU B 137 ? 0.5077 0.7134 0.2278 0.085   -0.1615 -0.0735 118 GLU D CD  
2825 O OE1 . GLU B 137 ? 0.3675 0.5593 0.101  0.1078  -0.1363 -0.0725 118 GLU D OE1 
2826 O OE2 . GLU B 137 ? 0.2056 0.3367 0.1079 0.065   -0.0661 -0.0544 118 GLU D OE2 
2827 N N   . GLY B 138 ? 0.2829 0.7031 0.1309 0.2012  -0.0893 -0.0808 119 GLY D N   
2828 C CA  . GLY B 138 ? 0.3221 0.816  0.1238 0.2492  -0.103  -0.0803 119 GLY D CA  
2829 C C   . GLY B 138 ? 0.396  0.9479 0.1424 0.2706  -0.1412 -0.1004 119 GLY D C   
2830 O O   . GLY B 138 ? 0.439  1.049  0.1348 0.318   -0.1517 -0.0954 119 GLY D O   
2831 N N   . ASN B 139 ? 0.3313 0.8552 0.1403 0.2367  -0.1254 -0.1224 120 ASN D N   
2832 C CA  . ASN B 139 ? 0.3456 0.9145 0.1417 0.2444  -0.1407 -0.1441 120 ASN D CA  
2833 C C   . ASN B 139 ? 0.416  0.9773 0.1388 0.2804  -0.1542 -0.1289 120 ASN D C   
2834 O O   . ASN B 139 ? 0.4477 1.0689 0.1397 0.3095  -0.1678 -0.1404 120 ASN D O   
2835 C CB  . ASN B 139 ? 0.3671 1.0389 0.1576 0.2578  -0.1625 -0.1741 120 ASN D CB  
2836 C CG  . ASN B 139 ? 0.5631 1.3036 0.2532 0.2088  -0.2742 -0.2205 120 ASN D CG  
2837 O OD1 . ASN B 139 ? 0.5371 1.265  0.2524 0.1752  -0.2711 -0.2431 120 ASN D OD1 
2838 N ND2 . ASN B 139 ? 0.4208 1.1443 0.2257 0.2163  -0.2018 -0.2148 120 ASN D ND2 
2839 N N   . ARG B 140 ? 0.3509 0.8223 0.1132 0.2802  -0.1121 -0.1046 121 ARG D N   
2840 C CA  . ARG B 140 ? 0.3778 0.8132 0.1    0.3151  -0.1037 -0.0902 121 ARG D CA  
2841 C C   . ARG B 140 ? 0.4163 0.8356 0.1093 0.2972  -0.1262 -0.104  121 ARG D C   
2842 O O   . ARG B 140 ? 0.4391 0.863  0.097  0.3305  -0.1273 -0.1033 121 ARG D O   
2843 C CB  . ARG B 140 ? 0.3715 0.7278 0.0972 0.3135  -0.0799 -0.0673 121 ARG D CB  
2844 C CG  . ARG B 140 ? 0.5371 0.9238 0.1132 0.3408  -0.1127 -0.033  121 ARG D CG  
2845 C CD  . ARG B 140 ? 0.6865 1.0036 0.1222 0.3402  -0.1186 0.0038  121 ARG D CD  
2846 N NE  . ARG B 140 ? 0.8217 1.1499 0.2124 0.3415  -0.1154 0.0385  121 ARG D NE  
2847 C CZ  . ARG B 140 ? 1.0333 1.3684 0.3892 0.3882  -0.0774 0.0727  121 ARG D CZ  
2848 N NH1 . ARG B 140 ? 0.8733 1.2094 0.1676 0.445   -0.0573 0.0824  121 ARG D NH1 
2849 N NH2 . ARG B 140 ? 0.8504 1.1897 0.2321 0.3789  -0.0562 0.0986  121 ARG D NH2 
2850 N N   . VAL B 141 ? 0.3391 0.7252 0.1127 0.2454  -0.1119 -0.1135 122 VAL D N   
2851 C CA  . VAL B 141 ? 0.3246 0.6864 0.1175 0.2185  -0.1124 -0.1221 122 VAL D CA  
2852 C C   . VAL B 141 ? 0.3283 0.7475 0.1402 0.182   -0.1272 -0.1453 122 VAL D C   
2853 O O   . VAL B 141 ? 0.3159 0.7695 0.149  0.1746  -0.1273 -0.1531 122 VAL D O   
2854 C CB  . VAL B 141 ? 0.3428 0.6107 0.1236 0.1947  -0.1097 -0.1087 122 VAL D CB  
2855 C CG1 . VAL B 141 ? 0.3593 0.5735 0.1094 0.2325  -0.0965 -0.0915 122 VAL D CG1 
2856 C CG2 . VAL B 141 ? 0.2999 0.5421 0.1321 0.1572  -0.0971 -0.1036 122 VAL D CG2 
2857 N N   . LYS B 142 ? 0.257  0.6703 0.1221 0.1622  -0.1056 -0.1481 123 LYS D N   
2858 C CA  . LYS B 142 ? 0.2293 0.6896 0.1288 0.128   -0.1014 -0.1666 123 LYS D CA  
2859 C C   . LYS B 142 ? 0.2397 0.634  0.1426 0.0858  -0.0984 -0.1576 123 LYS D C   
2860 O O   . LYS B 142 ? 0.2184 0.5308 0.1346 0.0882  -0.0816 -0.1304 123 LYS D O   
2861 C CB  . LYS B 142 ? 0.2654 0.7982 0.1394 0.1272  -0.1194 -0.1905 123 LYS D CB  
2862 C CG  . LYS B 142 ? 0.3672 1.0131 0.1825 0.1573  -0.1595 -0.2218 123 LYS D CG  
2863 C CD  . LYS B 142 ? 0.4848 1.2296 0.215  0.1437  -0.2143 -0.265  123 LYS D CD  
2864 C CE  . LYS B 142 ? 0.6163 1.4945 0.2395 0.1772  -0.2826 -0.3021 123 LYS D CE  
2865 N NZ  . LYS B 142 ? 0.6722 1.6396 0.2842 0.1599  -0.318  -0.3459 123 LYS D NZ  
2866 N N   . GLY B 143 ? 0.1953 0.6179 0.1453 0.0589  -0.0772 -0.166  124 GLY D N   
2867 C CA  . GLY B 143 ? 0.1705 0.5425 0.1494 0.0275  -0.0536 -0.1497 124 GLY D CA  
2868 C C   . GLY B 143 ? 0.2019 0.511  0.1453 0.0081  -0.0644 -0.1374 124 GLY D C   
2869 O O   . GLY B 143 ? 0.1743 0.4138 0.1345 0.0061  -0.0482 -0.1094 124 GLY D O   
2870 N N   . PRO B 144 ? 0.1711 0.4903 0.1337 0.0057  -0.0485 -0.1306 125 PRO D N   
2871 C CA  . PRO B 144 ? 0.1638 0.408  0.1321 -0.0072 -0.0337 -0.1009 125 PRO D CA  
2872 C C   . PRO B 144 ? 0.2164 0.3864 0.138  0.0117  -0.0583 -0.093  125 PRO D C   
2873 O O   . PRO B 144 ? 0.2131 0.3146 0.143  -0.0001 -0.0457 -0.0681 125 PRO D O   
2874 C CB  . PRO B 144 ? 0.1978 0.4842 0.1301 -0.0224 -0.0519 -0.1242 125 PRO D CB  
2875 C CG  . PRO B 144 ? 0.2413 0.6388 0.1527 -0.0304 -0.0739 -0.1711 125 PRO D CG  
2876 C CD  . PRO B 144 ? 0.202  0.6118 0.1383 0.0048  -0.0702 -0.1667 125 PRO D CD  
2877 N N   . GLU B 145 ? 0.1827 0.3617 0.137  0.0547  -0.0481 -0.0868 126 GLU D N   
2878 C CA  . GLU B 145 ? 0.1879 0.3018 0.138  0.0825  -0.0479 -0.0723 126 GLU D CA  
2879 C C   . GLU B 145 ? 0.1831 0.2632 0.1299 0.0734  -0.0475 -0.0639 126 GLU D C   
2880 O O   . GLU B 145 ? 0.164  0.1773 0.1231 0.0697  -0.0377 -0.0415 126 GLU D O   
2881 C CB  . GLU B 145 ? 0.2388 0.3957 0.1279 0.1237  -0.0735 -0.094  126 GLU D CB  
2882 C CG  . GLU B 145 ? 0.4211 0.5232 0.147  0.1515  -0.1189 -0.1046 126 GLU D CG  
2883 C CD  . GLU B 145 ? 0.6871 0.8424 0.1785 0.2006  -0.1829 -0.1258 126 GLU D CD  
2884 O OE1 . GLU B 145 ? 0.517  0.7414 0.1529 0.2177  -0.149  -0.1228 126 GLU D OE1 
2885 O OE2 . GLU B 145 ? 0.5034 0.5961 0.1568 0.2388  -0.1116 -0.0935 126 GLU D OE2 
2886 N N   . LYS B 146 ? 0.1184 0.2293 0.1119 0.0655  -0.0269 -0.058  127 LYS D N   
2887 C CA  . LYS B 146 ? 0.0926 0.1652 0.0884 0.0459  -0.02   -0.0413 127 LYS D CA  
2888 C C   . LYS B 146 ? 0.1065 0.1313 0.1068 0.0157  -0.0078 -0.0161 127 LYS D C   
2889 O O   . LYS B 146 ? 0.0685 0.0685 0.0685 0       0       0       127 LYS D O   
2890 C CB  . LYS B 146 ? 0.108  0.2281 0.1131 0.0475  -0.0189 -0.0543 127 LYS D CB  
2891 C CG  . LYS B 146 ? 0.1291 0.257  0.13   0.0442  -0.0246 -0.0622 127 LYS D CG  
2892 C CD  . LYS B 146 ? 0.1997 0.3362 0.1542 0.0533  -0.0524 -0.075  127 LYS D CD  
2893 C CE  . LYS B 146 ? 0.1913 0.2799 0.1444 0.0627  -0.0451 -0.0595 127 LYS D CE  
2894 N NZ  . LYS B 146 ? 0.202  0.2942 0.1569 0.0725  -0.0407 -0.0558 127 LYS D NZ  
2895 N N   . GLU B 147 ? 0.0738 0.1142 0.0797 0.0083  -0.0035 -0.0177 128 GLU D N   
2896 C CA  . GLU B 147 ? 0.0838 0.0838 0.0838 0       0       0       128 GLU D CA  
2897 C C   . GLU B 147 ? 0.1202 0.1127 0.1013 -0.0092 -0.0055 -0.0022 128 GLU D C   
2898 O O   . GLU B 147 ? 0.1118 0.0984 0.0964 -0.0067 -0.0037 0.0015  128 GLU D O   
2899 C CB  . GLU B 147 ? 0.1062 0.1384 0.1059 -0.0107 0.0031  -0.0101 128 GLU D CB  
2900 C CG  . GLU B 147 ? 0.1456 0.2999 0.1078 -0.0499 -0.0205 -0.0795 128 GLU D CG  
2901 C CD  . GLU B 147 ? 0.4226 0.6215 0.2875 -0.1152 -0.0807 -0.163  128 GLU D CD  
2902 O OE1 . GLU B 147 ? 0.2956 0.4686 0.2246 -0.1075 -0.014  -0.1014 128 GLU D OE1 
2903 O OE2 . GLU B 147 ? 0.333  0.5808 0.2488 -0.1079 -0.053  -0.1639 128 GLU D OE2 
2904 N N   . GLU B 148 ? 0.1255 0.1255 0.1255 0       0       0       129 GLU D N   
2905 C CA  . GLU B 148 ? 0.1236 0.1236 0.1236 0       0       0       129 GLU D CA  
2906 C C   . GLU B 148 ? 0.1388 0.0913 0.0968 0.0052  -0.0172 -0.0019 129 GLU D C   
2907 O O   . GLU B 148 ? 0.1382 0.0888 0.0932 0.0006  -0.0148 -0.0002 129 GLU D O   
2908 C CB  . GLU B 148 ? 0.1711 0.1167 0.1239 0.0057  -0.0207 -0.0022 129 GLU D CB  
2909 C CG  . GLU B 148 ? 0.3149 0.1418 0.1193 -0.0018 -0.0678 -0.0213 129 GLU D CG  
2910 C CD  . GLU B 148 ? 0.6336 0.4017 0.2651 -0.0648 -0.1173 -0.0954 129 GLU D CD  
2911 O OE1 . GLU B 148 ? 0.524  0.3439 0.2448 -0.0816 -0.0858 -0.0576 129 GLU D OE1 
2912 O OE2 . GLU B 148 ? 0.6399 0.342  0.2623 -0.0569 -0.1038 -0.0754 129 GLU D OE2 
2913 N N   . LYS B 149 ? 0.091  0.091  0.091  0       0       0       130 LYS D N   
2914 C CA  . LYS B 149 ? 0.0699 0.0699 0.0699 0       0       0       130 LYS D CA  
2915 C C   . LYS B 149 ? 0.0713 0.0713 0.0713 0       0       0       130 LYS D C   
2916 O O   . LYS B 149 ? 0.0381 0.0381 0.0381 0       0       0       130 LYS D O   
2917 C CB  . LYS B 149 ? 0.109  0.0998 0.0975 0.0077  -0.0053 -0.003  130 LYS D CB  
2918 C CG  . LYS B 149 ? 0.1925 0.0923 0.0651 0.0755  -0.0432 -0.0232 130 LYS D CG  
2919 C CD  . LYS B 149 ? 0.3918 0.2859 0.1184 0.1303  -0.0664 -0.0551 130 LYS D CD  
2920 C CE  . LYS B 149 ? 0.5552 0.3977 0.1574 0.1511  -0.0499 -0.0632 130 LYS D CE  
2921 N NZ  . LYS B 149 ? 0.7487 0.6134 0.1879 0.1932  -0.0367 -0.0736 130 LYS D NZ  
2922 N N   . LEU B 150 ? 0.0392 0.0392 0.0392 0       0       0       131 LEU D N   
2923 C CA  . LEU B 150 ? 0.038  0.038  0.038  0       0       0       131 LEU D CA  
2924 C C   . LEU B 150 ? 0.0756 0.0756 0.0756 0       0       0       131 LEU D C   
2925 O O   . LEU B 150 ? 0.038  0.038  0.038  0       0       0       131 LEU D O   
2926 C CB  . LEU B 150 ? 0.038  0.038  0.038  0       0       0       131 LEU D CB  
2927 C CG  . LEU B 150 ? 0.0882 0.0882 0.0882 0       0       0       131 LEU D CG  
2928 C CD1 . LEU B 150 ? 0.0734 0.0734 0.0734 0       0       0       131 LEU D CD1 
2929 C CD2 . LEU B 150 ? 0.0744 0.0744 0.0744 0       0       0       131 LEU D CD2 
2930 N N   . ARG B 151 ? 0.038  0.038  0.038  0       0       0       132 ARG D N   
2931 C CA  . ARG B 151 ? 0.038  0.038  0.038  0       0       0       132 ARG D CA  
2932 C C   . ARG B 151 ? 0.0927 0.0927 0.0927 0       0       0       132 ARG D C   
2933 O O   . ARG B 151 ? 0.079  0.079  0.079  0       0       0       132 ARG D O   
2934 C CB  . ARG B 151 ? 0.038  0.038  0.038  0       0       0       132 ARG D CB  
2935 C CG  . ARG B 151 ? 0.038  0.038  0.038  0       0       0       132 ARG D CG  
2936 C CD  . ARG B 151 ? 0.1102 0.1102 0.1102 0       0       0       132 ARG D CD  
2937 N NE  . ARG B 151 ? 0.1418 0.1338 0.1084 -0.0292 0.0024  -0.0021 132 ARG D NE  
2938 C CZ  . ARG B 151 ? 0.1652 0.1841 0.0679 -0.1092 0.017   -0.0185 132 ARG D CZ  
2939 N NH1 . ARG B 151 ? 0.0843 0.0866 0.0789 -0.0066 0.001   -0.0012 132 ARG D NH1 
2940 N NH2 . ARG B 151 ? 0.0494 0.0538 0.0423 -0.0097 0.0022  -0.0028 132 ARG D NH2 
2941 N N   . GLN B 152 ? 0.0709 0.0709 0.0709 0       0       0       133 GLN D N   
2942 C CA  . GLN B 152 ? 0.077  0.077  0.077  0       0       0       133 GLN D CA  
2943 C C   . GLN B 152 ? 0.078  0.078  0.078  0       0       0       133 GLN D C   
2944 O O   . GLN B 152 ? 0.0893 0.0893 0.0893 0       0       0       133 GLN D O   
2945 C CB  . GLN B 152 ? 0.1029 0.1029 0.1029 0       0       0       133 GLN D CB  
2946 C CG  . GLN B 152 ? 0.4738 0.1467 0.1414 -0.0003 -0.0663 -0.0226 133 GLN D CG  
2947 C CD  . GLN B 152 ? 0.798  0.3819 0.3636 -0.0317 -0.0731 -0.0755 133 GLN D CD  
2948 O OE1 . GLN B 152 ? 0.8061 0.3398 0.3398 -0.0231 -0.0569 -0.0821 133 GLN D OE1 
2949 N NE2 . GLN B 152 ? 0.629  0.2527 0.2456 -0.0517 -0.0684 -0.0341 133 GLN D NE2 
2950 N N   . ALA B 153 ? 0.0748 0.0748 0.0748 0       0       0       134 ALA D N   
2951 C CA  . ALA B 153 ? 0.0638 0.0638 0.0638 0       0       0       134 ALA D CA  
2952 C C   . ALA B 153 ? 0.0875 0.0875 0.0875 0       0       0       134 ALA D C   
2953 O O   . ALA B 153 ? 0.0767 0.0767 0.0767 0       0       0       134 ALA D O   
2954 C CB  . ALA B 153 ? 0.0689 0.0689 0.0689 0       0       0       134 ALA D CB  
2955 N N   . VAL B 154 ? 0.038  0.038  0.038  0       0       0       135 VAL D N   
2956 C CA  . VAL B 154 ? 0.038  0.038  0.038  0       0       0       135 VAL D CA  
2957 C C   . VAL B 154 ? 0.0966 0.0966 0.0966 0       0       0       135 VAL D C   
2958 O O   . VAL B 154 ? 0.0829 0.0829 0.0829 0       0       0       135 VAL D O   
2959 C CB  . VAL B 154 ? 0.0501 0.0501 0.0501 0       0       0       135 VAL D CB  
2960 C CG1 . VAL B 154 ? 0.038  0.038  0.038  0       0       0       135 VAL D CG1 
2961 C CG2 . VAL B 154 ? 0.038  0.038  0.038  0       0       0       135 VAL D CG2 
2962 N N   . LYS B 155 ? 0.0643 0.0643 0.0643 0       0       0       136 LYS D N   
2963 C CA  . LYS B 155 ? 0.0832 0.0832 0.0832 0       0       0       136 LYS D CA  
2964 C C   . LYS B 155 ? 0.084  0.084  0.084  0       0       0       136 LYS D C   
2965 O O   . LYS B 155 ? 0.0913 0.0913 0.0913 0       0       0       136 LYS D O   
2966 C CB  . LYS B 155 ? 0.1029 0.1029 0.1029 0       0       0       136 LYS D CB  
2967 C CG  . LYS B 155 ? 0.2629 0.092  0.0893 -0.0386 0.0318  -0.0069 136 LYS D CG  
2968 C CD  . LYS B 155 ? 0.4737 0.2398 0.2361 -0.0384 0.0241  -0.0039 136 LYS D CD  
2969 C CE  . LYS B 155 ? 0.7418 0.3646 0.387  -0.0282 0.031   -0.0841 136 LYS D CE  
2970 N NZ  . LYS B 155 ? 0.856  0.4304 0.4421 -0.0097 0.0281  -0.1478 136 LYS D NZ  
2971 N N   . GLN B 156 ? 0.045  0.045  0.045  0       0       0       137 GLN D N   
2972 C CA  . GLN B 156 ? 0.038  0.038  0.038  0       0       0       137 GLN D CA  
2973 C C   . GLN B 156 ? 0.065  0.065  0.065  0       0       0       137 GLN D C   
2974 O O   . GLN B 156 ? 0.038  0.038  0.038  0       0       0       137 GLN D O   
2975 C CB  . GLN B 156 ? 0.057  0.057  0.057  0       0       0       137 GLN D CB  
2976 C CG  . GLN B 156 ? 0.1533 0.1533 0.1533 0       0       0       137 GLN D CG  
2977 C CD  . GLN B 156 ? 0.2754 0.2239 0.222  -0.075  0.0737  -0.0526 137 GLN D CD  
2978 O OE1 . GLN B 156 ? 0.2791 0.2667 0.2657 -0.03   0.0293  -0.0239 137 GLN D OE1 
2979 N NE2 . GLN B 156 ? 0.2199 0.2172 0.2176 -0.0039 0.0041  -0.0029 137 GLN D NE2 
2980 N N   . VAL B 157 ? 0.038  0.038  0.038  0       0       0       138 VAL D N   
2981 C CA  . VAL B 157 ? 0.0407 0.0407 0.0407 0       0       0       138 VAL D CA  
2982 C C   . VAL B 157 ? 0.0782 0.0782 0.0782 0       0       0       138 VAL D C   
2983 O O   . VAL B 157 ? 0.038  0.038  0.038  0       0       0       138 VAL D O   
2984 C CB  . VAL B 157 ? 0.0909 0.0909 0.0909 0       0       0       138 VAL D CB  
2985 C CG1 . VAL B 157 ? 0.0891 0.0891 0.0891 0       0       0       138 VAL D CG1 
2986 C CG2 . VAL B 157 ? 0.09   0.09   0.09   0       0       0       138 VAL D CG2 
2987 N N   . LEU B 158 ? 0.038  0.038  0.038  0       0       0       139 LEU D N   
2988 C CA  . LEU B 158 ? 0.038  0.038  0.038  0       0       0       139 LEU D CA  
2989 C C   . LEU B 158 ? 0.0791 0.0791 0.0791 0       0       0       139 LEU D C   
2990 O O   . LEU B 158 ? 0.038  0.038  0.038  0       0       0       139 LEU D O   
2991 C CB  . LEU B 158 ? 0.038  0.038  0.038  0       0       0       139 LEU D CB  
2992 C CG  . LEU B 158 ? 0.0881 0.0881 0.0881 0       0       0       139 LEU D CG  
2993 C CD1 . LEU B 158 ? 0.0755 0.0755 0.0755 0       0       0       139 LEU D CD1 
2994 C CD2 . LEU B 158 ? 0.0702 0.0702 0.0702 0       0       0       139 LEU D CD2 
2995 N N   . LYS B 159 ? 0.038  0.038  0.038  0       0       0       140 LYS D N   
2996 C CA  . LYS B 159 ? 0.038  0.038  0.038  0       0       0       140 LYS D CA  
2997 C C   . LYS B 159 ? 0.0678 0.0678 0.0678 0       0       0       140 LYS D C   
2998 O O   . LYS B 159 ? 0.038  0.038  0.038  0       0       0       140 LYS D O   
2999 C CB  . LYS B 159 ? 0.0715 0.0715 0.0715 0       0       0       140 LYS D CB  
3000 C CG  . LYS B 159 ? 0.1404 0.1726 0.1526 -0.0109 0.0072  -0.0235 140 LYS D CG  
3001 C CD  . LYS B 159 ? 0.3035 0.3624 0.2207 -0.0496 0.0366  -0.1604 140 LYS D CD  
3002 C CE  . LYS B 159 ? 0.4154 0.5298 0.4253 -0.0357 0.0291  -0.104  140 LYS D CE  
3003 N NZ  . LYS B 159 ? 0.4076 0.5219 0.3341 -0.0079 0.04    -0.1695 140 LYS D NZ  
3004 N N   A CYS B 160 ? 0.038  0.038  0.038  0       0       0       141 CYS D N   
3005 N N   B CYS B 160 ? 0.038  0.038  0.038  0       0       0       141 CYS D N   
3006 C CA  A CYS B 160 ? 0.038  0.038  0.038  0       0       0       141 CYS D CA  
3007 C CA  B CYS B 160 ? 0.038  0.038  0.038  0       0       0       141 CYS D CA  
3008 C C   A CYS B 160 ? 0.0653 0.0653 0.0653 0       0       0       141 CYS D C   
3009 C C   B CYS B 160 ? 0.0662 0.0662 0.0662 0       0       0       141 CYS D C   
3010 O O   A CYS B 160 ? 0.038  0.038  0.038  0       0       0       141 CYS D O   
3011 O O   B CYS B 160 ? 0.038  0.038  0.038  0       0       0       141 CYS D O   
3012 C CB  A CYS B 160 ? 0.038  0.038  0.038  0       0       0       141 CYS D CB  
3013 C CB  B CYS B 160 ? 0.0509 0.0509 0.0509 0       0       0       141 CYS D CB  
3014 S SG  A CYS B 160 ? 0.0732 0.0732 0.0732 0       0       0       141 CYS D SG  
3015 S SG  B CYS B 160 ? 0.08   0.08   0.08   0       0       0       141 CYS D SG  
3016 N N   . ASP B 161 ? 0.038  0.038  0.038  0       0       0       142 ASP D N   
3017 C CA  . ASP B 161 ? 0.038  0.038  0.038  0       0       0       142 ASP D CA  
3018 C C   . ASP B 161 ? 0.0567 0.0567 0.0567 0       0       0       142 ASP D C   
3019 O O   . ASP B 161 ? 0.038  0.038  0.038  0       0       0       142 ASP D O   
3020 C CB  . ASP B 161 ? 0.0405 0.0405 0.0405 0       0       0       142 ASP D CB  
3021 C CG  . ASP B 161 ? 0.0721 0.0721 0.0721 0       0       0       142 ASP D CG  
3022 O OD1 . ASP B 161 ? 0.038  0.038  0.038  0       0       0       142 ASP D OD1 
3023 O OD2 . ASP B 161 ? 0.0932 0.0932 0.0932 0       0       0       142 ASP D OD2 
3024 N N   . VAL B 162 ? 0.038  0.038  0.038  0       0       0       143 VAL D N   
3025 C CA  . VAL B 162 ? 0.038  0.038  0.038  0       0       0       143 VAL D CA  
3026 C C   . VAL B 162 ? 0.0556 0.0556 0.0556 0       0       0       143 VAL D C   
3027 O O   . VAL B 162 ? 0.038  0.038  0.038  0       0       0       143 VAL D O   
3028 C CB  . VAL B 162 ? 0.0445 0.0445 0.0445 0       0       0       143 VAL D CB  
3029 C CG1 . VAL B 162 ? 0.038  0.038  0.038  0       0       0       143 VAL D CG1 
3030 C CG2 . VAL B 162 ? 0.038  0.038  0.038  0       0       0       143 VAL D CG2 
3031 N N   . THR B 163 ? 0.038  0.038  0.038  0       0       0       144 THR D N   
3032 C CA  . THR B 163 ? 0.038  0.038  0.038  0       0       0       144 THR D CA  
3033 C C   . THR B 163 ? 0.0844 0.0844 0.0844 0       0       0       144 THR D C   
3034 O O   . THR B 163 ? 0.0545 0.0545 0.0545 0       0       0       144 THR D O   
3035 C CB  . THR B 163 ? 0.0751 0.0751 0.0751 0       0       0       144 THR D CB  
3036 O OG1 . THR B 163 ? 0.038  0.038  0.038  0       0       0       144 THR D OG1 
3037 C CG2 . THR B 163 ? 0.038  0.038  0.038  0       0       0       144 THR D CG2 
3038 N N   . GLN B 164 ? 0.038  0.038  0.038  0       0       0       145 GLN D N   
3039 C CA  . GLN B 164 ? 0.038  0.038  0.038  0       0       0       145 GLN D CA  
3040 C C   . GLN B 164 ? 0.0696 0.0696 0.0696 0       0       0       145 GLN D C   
3041 O O   . GLN B 164 ? 0.038  0.038  0.038  0       0       0       145 GLN D O   
3042 C CB  . GLN B 164 ? 0.0552 0.0552 0.0552 0       0       0       145 GLN D CB  
3043 C CG  . GLN B 164 ? 0.0954 0.1775 0.1198 -0.0004 0.0002  -0.0447 145 GLN D CG  
3044 C CD  . GLN B 164 ? 0.1748 0.5622 0.2741 0.0138  -0.007  -0.1968 145 GLN D CD  
3045 O OE1 . GLN B 164 ? 0.2136 0.5094 0.2829 0.0211  -0.0103 -0.1451 145 GLN D OE1 
3046 N NE2 . GLN B 164 ? 0.1991 0.6242 0.3044 0.0131  -0.0065 -0.2121 145 GLN D NE2 
3047 N N   . SER B 165 ? 0.038  0.038  0.038  0       0       0       146 SER D N   
3048 C CA  . SER B 165 ? 0.0386 0.0576 0.0457 -0.0035 0.0022  -0.0123 146 SER D CA  
3049 C C   . SER B 165 ? 0.0805 0.0899 0.0844 -0.0021 0.0014  -0.0065 146 SER D C   
3050 O O   . SER B 165 ? 0.0773 0.0844 0.0804 -0.0019 0.0013  -0.0052 146 SER D O   
3051 C CB  . SER B 165 ? 0.0961 0.1766 0.1253 -0.0139 0.0086  -0.0511 146 SER D CB  
3052 O OG  . SER B 165 ? 0.0683 0.2805 0.1394 -0.0321 0.019   -0.1283 146 SER D OG  
3053 N N   . GLN B 166 ? 0.0382 0.0429 0.0401 -0.0009 0.0006  -0.0032 147 GLN D N   
3054 C CA  . GLN B 166 ? 0.038  0.038  0.038  0       0       0       147 GLN D CA  
3055 C C   . GLN B 166 ? 0.0706 0.0706 0.0706 0       0       0       147 GLN D C   
3056 O O   . GLN B 166 ? 0.038  0.038  0.038  0       0       0       147 GLN D O   
3057 C CB  . GLN B 166 ? 0.0642 0.0869 0.0744 -0.0048 0.0033  -0.0163 147 GLN D CB  
3058 C CG  . GLN B 166 ? 0.1175 0.3924 0.2471 -0.0655 0.0462  -0.2046 147 GLN D CG  
3059 C CD  . GLN B 166 ? 0.2485 0.8179 0.4951 -0.1162 0.0784  -0.3994 147 GLN D CD  
3060 O OE1 . GLN B 166 ? 0.2792 0.8105 0.5096 -0.1199 0.0813  -0.3778 147 GLN D OE1 
3061 N NE2 . GLN B 166 ? 0.2643 0.844  0.4967 -0.0902 0.0581  -0.3822 147 GLN D NE2 
3062 N N   . PRO B 167 ? 0.038  0.038  0.038  0       0       0       148 PRO D N   
3063 C CA  . PRO B 167 ? 0.038  0.038  0.038  0       0       0       148 PRO D CA  
3064 C C   . PRO B 167 ? 0.0777 0.0777 0.0777 0       0       0       148 PRO D C   
3065 O O   . PRO B 167 ? 0.038  0.038  0.038  0       0       0       148 PRO D O   
3066 C CB  . PRO B 167 ? 0.0437 0.0437 0.0437 0       0       0       148 PRO D CB  
3067 C CG  . PRO B 167 ? 0.0887 0.0887 0.0887 0       0       0       148 PRO D CG  
3068 C CD  . PRO B 167 ? 0.0428 0.0428 0.0428 0       0       0       148 PRO D CD  
3069 N N   . LEU B 168 ? 0.038  0.038  0.038  0       0       0       149 LEU D N   
3070 C CA  . LEU B 168 ? 0.0439 0.0439 0.0439 0       0       0       149 LEU D CA  
3071 C C   . LEU B 168 ? 0.0972 0.0972 0.0972 0       0       0       149 LEU D C   
3072 O O   . LEU B 168 ? 0.1119 0.1119 0.1119 0       0       0       149 LEU D O   
3073 C CB  . LEU B 168 ? 0.038  0.038  0.038  0       0       0       149 LEU D CB  
3074 C CG  . LEU B 168 ? 0.0867 0.0867 0.0867 0       0       0       149 LEU D CG  
3075 C CD1 . LEU B 168 ? 0.0845 0.0845 0.0845 0       0       0       149 LEU D CD1 
3076 C CD2 . LEU B 168 ? 0.0803 0.0803 0.0803 0       0       0       149 LEU D CD2 
3077 N N   . GLY B 169 ? 0.1284 0.1284 0.1284 0       0       0       150 GLY D N   
3078 C CA  . GLY B 169 ? 0.1289 0.1429 0.1353 -0.0024 0.0017  -0.0099 150 GLY D CA  
3079 C C   . GLY B 169 ? 0.1159 0.2406 0.1781 -0.0263 0.019   -0.0937 150 GLY D C   
3080 O O   . GLY B 169 ? 0.147  0.2662 0.2088 -0.0284 0.0209  -0.0925 150 GLY D O   
3081 N N   . ALA B 170 ? 0.1387 0.25   0.1965 -0.0248 0.0183  -0.0858 151 ALA D N   
3082 C CA  . ALA B 170 ? 0.1706 0.2909 0.2392 -0.0319 0.0246  -0.099  151 ALA D CA  
3083 C C   . ALA B 170 ? 0.1989 0.3189 0.2765 -0.044  0.0364  -0.1112 151 ALA D C   
3084 O O   . ALA B 170 ? 0.2052 0.3204 0.2868 -0.0487 0.0421  -0.115  151 ALA D O   
3085 C CB  . ALA B 170 ? 0.1757 0.3073 0.2497 -0.0319 0.0244  -0.1063 151 ALA D CB  
3086 N N   . VAL B 171 ? 0.156  0.2518 0.2183 -0.0392 0.0327  -0.0914 152 VAL D N   
3087 C CA  . VAL B 171 ? 0.1628 0.2347 0.2149 -0.0402 0.0355  -0.0794 152 VAL D CA  
3088 C C   . VAL B 171 ? 0.1965 0.2943 0.2723 -0.0595 0.0541  -0.1145 152 VAL D C   
3089 O O   . VAL B 171 ? 0.2101 0.3042 0.2791 -0.0529 0.047   -0.1046 152 VAL D O   
3090 C CB  . VAL B 171 ? 0.1376 0.2172 0.1929 -0.0515 0.0452  -0.092  152 VAL D CB  
3091 C CG1 . VAL B 171 ? 0.1469 0.2034 0.1901 -0.0555 0.0513  -0.0837 152 VAL D CG1 
3092 C CG2 . VAL B 171 ? 0.1332 0.2039 0.1789 -0.0474 0.0406  -0.081  152 VAL D CG2 
3093 N N   . PRO B 172 ? 0.2062 0.2855 0.2765 -0.0589 0.0565  -0.1061 153 PRO D N   
3094 C CA  . PRO B 172 ? 0.2179 0.2964 0.2938 -0.0664 0.0657  -0.1151 153 PRO D CA  
3095 C C   . PRO B 172 ? 0.2155 0.2712 0.277  -0.0654 0.0673  -0.1018 153 PRO D C   
3096 O O   . PRO B 172 ? 0.2203 0.2629 0.2737 -0.0683 0.0722  -0.0982 153 PRO D O   
3097 C CB  . PRO B 172 ? 0.2286 0.325  0.3326 -0.0898 0.092   -0.1538 153 PRO D CB  
3098 C CG  . PRO B 172 ? 0.2361 0.3327 0.3456 -0.0987 0.1026  -0.1645 153 PRO D CG  
3099 C CD  . PRO B 172 ? 0.2097 0.289  0.2876 -0.069  0.0686  -0.1185 153 PRO D CD  
3100 N N   . LEU B 173 ? 0.1738 0.2043 0.2081 -0.0374 0.0386  -0.0575 154 LEU D N   
3101 C CA  . LEU B 173 ? 0.1692 0.1793 0.1831 -0.0188 0.0202  -0.0263 154 LEU D CA  
3102 C C   . LEU B 173 ? 0.1651 0.1758 0.1843 -0.0265 0.0298  -0.0364 154 LEU D C   
3103 O O   . LEU B 173 ? 0.1757 0.1885 0.1943 -0.0225 0.0246  -0.0326 154 LEU D O   
3104 C CB  . LEU B 173 ? 0.1483 0.1516 0.1518 -0.005  0.0051  -0.007  154 LEU D CB  
3105 C CG  . LEU B 173 ? 0.1171 0.1295 0.1292 -0.0202 0.0201  -0.0272 154 LEU D CG  
3106 C CD1 . LEU B 173 ? 0.1155 0.119  0.1182 -0.005  0.0047  -0.0066 154 LEU D CD1 
3107 C CD2 . LEU B 173 ? 0.1208 0.127  0.1305 -0.0291 0.0306  -0.034  154 LEU D CD2 
3108 N N   . PRO B 174 ? 0.1673 0.1676 0.169  -0.0031 0.0037  -0.0039 155 PRO D N   
3109 C CA  . PRO B 174 ? 0.1777 0.1771 0.1837 -0.0111 0.0141  -0.0137 155 PRO D CA  
3110 C C   . PRO B 174 ? 0.1439 0.1452 0.1578 -0.0246 0.0302  -0.031  155 PRO D C   
3111 O O   . PRO B 174 ? 0.119  0.1204 0.1241 -0.0095 0.0111  -0.0119 155 PRO D O   
3112 C CB  . PRO B 174 ? 0.1784 0.1689 0.1854 -0.0217 0.0303  -0.0244 155 PRO D CB  
3113 C CG  . PRO B 174 ? 0.1704 0.1501 0.179  -0.0399 0.0554  -0.0431 155 PRO D CG  
3114 C CD  . PRO B 174 ? 0.1465 0.1449 0.1494 -0.0082 0.0104  -0.0094 155 PRO D CD  
3115 N N   . PRO B 175 ? 0.1425 0.1432 0.1512 -0.0144 0.0178  -0.0183 156 PRO D N   
3116 C CA  . PRO B 175 ? 0.1155 0.116  0.1178 -0.0038 0.0046  -0.0049 156 PRO D CA  
3117 C C   . PRO B 175 ? 0.1    0.1    0.1    0       0       0       156 PRO D C   
3118 O O   . PRO B 175 ? 0.1031 0.1031 0.1031 0       0       0       156 PRO D O   
3119 C CB  . PRO B 175 ? 0.142  0.1435 0.1599 -0.0286 0.0357  -0.0366 156 PRO D CB  
3120 C CG  . PRO B 175 ? 0.1408 0.1478 0.197  -0.0817 0.1026  -0.1071 156 PRO D CG  
3121 C CD  . PRO B 175 ? 0.1516 0.1498 0.1833 -0.0502 0.065   -0.0639 156 PRO D CD  
3122 N N   . ALA B 176 ? 0.0488 0.0488 0.0488 0       0       0       157 ALA D N   
3123 C CA  . ALA B 176 ? 0.038  0.038  0.038  0       0       0       157 ALA D CA  
3124 C C   . ALA B 176 ? 0.0649 0.0649 0.0649 0       0       0       157 ALA D C   
3125 O O   . ALA B 176 ? 0.038  0.038  0.038  0       0       0       157 ALA D O   
3126 C CB  . ALA B 176 ? 0.0436 0.0436 0.0436 0       0       0       157 ALA D CB  
3127 N N   . ASP B 177 ? 0.038  0.038  0.038  0       0       0       158 ASP D N   
3128 C CA  . ASP B 177 ? 0.038  0.038  0.038  0       0       0       158 ASP D CA  
3129 C C   . ASP B 177 ? 0.0641 0.0641 0.0641 0       0       0       158 ASP D C   
3130 O O   . ASP B 177 ? 0.038  0.038  0.038  0       0       0       158 ASP D O   
3131 C CB  . ASP B 177 ? 0.0415 0.0415 0.0415 0       0       0       158 ASP D CB  
3132 C CG  . ASP B 177 ? 0.0914 0.0914 0.0914 0       0       0       158 ASP D CG  
3133 O OD1 . ASP B 177 ? 0.1332 0.1118 0.1288 -0.0095 0.0227  -0.0087 158 ASP D OD1 
3134 O OD2 . ASP B 177 ? 0.1031 0.1031 0.1031 0       0       0       158 ASP D OD2 
3135 N N   . CYS B 178 ? 0.038  0.038  0.038  0       0       0       159 CYS D N   
3136 C CA  . CYS B 178 ? 0.038  0.038  0.038  0       0       0       159 CYS D CA  
3137 C C   . CYS B 178 ? 0.0701 0.0701 0.0701 0       0       0       159 CYS D C   
3138 O O   . CYS B 178 ? 0.038  0.038  0.038  0       0       0       159 CYS D O   
3139 C CB  . CYS B 178 ? 0.038  0.038  0.038  0       0       0       159 CYS D CB  
3140 S SG  . CYS B 178 ? 0.045  0.045  0.045  0       0       0       159 CYS D SG  
3141 N N   . VAL B 179 ? 0.038  0.038  0.038  0       0       0       160 VAL D N   
3142 C CA  . VAL B 179 ? 0.038  0.038  0.038  0       0       0       160 VAL D CA  
3143 C C   . VAL B 179 ? 0.0633 0.0633 0.0633 0       0       0       160 VAL D C   
3144 O O   . VAL B 179 ? 0.038  0.038  0.038  0       0       0       160 VAL D O   
3145 C CB  . VAL B 179 ? 0.0503 0.0503 0.0503 0       0       0       160 VAL D CB  
3146 C CG1 . VAL B 179 ? 0.038  0.038  0.038  0       0       0       160 VAL D CG1 
3147 C CG2 . VAL B 179 ? 0.038  0.038  0.038  0       0       0       160 VAL D CG2 
3148 N N   . LEU B 180 ? 0.038  0.038  0.038  0       0       0       161 LEU D N   
3149 C CA  . LEU B 180 ? 0.038  0.038  0.038  0       0       0       161 LEU D CA  
3150 C C   . LEU B 180 ? 0.0639 0.0639 0.0639 0       0       0       161 LEU D C   
3151 O O   . LEU B 180 ? 0.038  0.038  0.038  0       0       0       161 LEU D O   
3152 C CB  . LEU B 180 ? 0.038  0.038  0.038  0       0       0       161 LEU D CB  
3153 C CG  . LEU B 180 ? 0.0479 0.0479 0.0479 0       0       0       161 LEU D CG  
3154 C CD1 . LEU B 180 ? 0.039  0.039  0.039  0       0       0       161 LEU D CD1 
3155 C CD2 . LEU B 180 ? 0.0435 0.0435 0.0435 0       0       0       161 LEU D CD2 
3156 N N   . SER B 181 ? 0.038  0.038  0.038  0       0       0       162 SER D N   
3157 C CA  . SER B 181 ? 0.038  0.038  0.038  0       0       0       162 SER D CA  
3158 C C   . SER B 181 ? 0.059  0.059  0.059  0       0       0       162 SER D C   
3159 O O   . SER B 181 ? 0.038  0.038  0.038  0       0       0       162 SER D O   
3160 C CB  . SER B 181 ? 0.038  0.038  0.038  0       0       0       162 SER D CB  
3161 O OG  . SER B 181 ? 0.038  0.038  0.038  0       0       0       162 SER D OG  
3162 N N   . THR B 182 ? 0.038  0.038  0.038  0       0       0       163 THR D N   
3163 C CA  . THR B 182 ? 0.038  0.038  0.038  0       0       0       163 THR D CA  
3164 C C   . THR B 182 ? 0.0511 0.0511 0.0511 0       0       0       163 THR D C   
3165 O O   . THR B 182 ? 0.038  0.038  0.038  0       0       0       163 THR D O   
3166 C CB  . THR B 182 ? 0.038  0.038  0.038  0       0       0       163 THR D CB  
3167 O OG1 . THR B 182 ? 0.038  0.038  0.038  0       0       0       163 THR D OG1 
3168 C CG2 . THR B 182 ? 0.038  0.038  0.038  0       0       0       163 THR D CG2 
3169 N N   . LEU B 183 ? 0.038  0.038  0.038  0       0       0       164 LEU D N   
3170 C CA  . LEU B 183 ? 0.038  0.038  0.038  0       0       0       164 LEU D CA  
3171 C C   . LEU B 183 ? 0.064  0.064  0.064  0       0       0       164 LEU D C   
3172 O O   . LEU B 183 ? 0.038  0.038  0.038  0       0       0       164 LEU D O   
3173 C CB  . LEU B 183 ? 0.038  0.038  0.038  0       0       0       164 LEU D CB  
3174 C CG  . LEU B 183 ? 0.0609 0.0609 0.0609 0       0       0       164 LEU D CG  
3175 C CD1 . LEU B 183 ? 0.0715 0.0715 0.0715 0       0       0       164 LEU D CD1 
3176 C CD2 . LEU B 183 ? 0.0382 0.0382 0.0382 0       0       0       164 LEU D CD2 
3177 N N   . CYS B 184 ? 0.038  0.038  0.038  0       0       0       165 CYS D N   
3178 C CA  . CYS B 184 ? 0.038  0.038  0.038  0       0       0       165 CYS D CA  
3179 C C   . CYS B 184 ? 0.0627 0.0627 0.0627 0       0       0       165 CYS D C   
3180 O O   . CYS B 184 ? 0.038  0.038  0.038  0       0       0       165 CYS D O   
3181 C CB  . CYS B 184 ? 0.038  0.038  0.038  0       0       0       165 CYS D CB  
3182 S SG  . CYS B 184 ? 0.038  0.038  0.038  0       0       0       165 CYS D SG  
3183 N N   . LEU B 185 ? 0.038  0.038  0.038  0       0       0       166 LEU D N   
3184 C CA  . LEU B 185 ? 0.038  0.038  0.038  0       0       0       166 LEU D CA  
3185 C C   . LEU B 185 ? 0.057  0.057  0.057  0       0       0       166 LEU D C   
3186 O O   . LEU B 185 ? 0.038  0.038  0.038  0       0       0       166 LEU D O   
3187 C CB  . LEU B 185 ? 0.038  0.038  0.038  0       0       0       166 LEU D CB  
3188 C CG  . LEU B 185 ? 0.0608 0.0608 0.0608 0       0       0       166 LEU D CG  
3189 C CD1 . LEU B 185 ? 0.0575 0.0575 0.0575 0       0       0       166 LEU D CD1 
3190 C CD2 . LEU B 185 ? 0.038  0.038  0.038  0       0       0       166 LEU D CD2 
3191 N N   . ASP B 186 ? 0.038  0.038  0.038  0       0       0       167 ASP D N   
3192 C CA  . ASP B 186 ? 0.038  0.038  0.038  0       0       0       167 ASP D CA  
3193 C C   . ASP B 186 ? 0.0643 0.0643 0.0643 0       0       0       167 ASP D C   
3194 O O   . ASP B 186 ? 0.038  0.038  0.038  0       0       0       167 ASP D O   
3195 C CB  . ASP B 186 ? 0.0465 0.0465 0.0465 0       0       0       167 ASP D CB  
3196 C CG  . ASP B 186 ? 0.0965 0.0965 0.0965 0       0       0       167 ASP D CG  
3197 O OD1 . ASP B 186 ? 0.1043 0.1043 0.1043 0       0       0       167 ASP D OD1 
3198 O OD2 . ASP B 186 ? 0.1279 0.1279 0.1279 0       0       0       167 ASP D OD2 
3199 N N   . ALA B 187 ? 0.038  0.038  0.038  0       0       0       168 ALA D N   
3200 C CA  . ALA B 187 ? 0.038  0.038  0.038  0       0       0       168 ALA D CA  
3201 C C   . ALA B 187 ? 0.0886 0.0886 0.0886 0       0       0       168 ALA D C   
3202 O O   . ALA B 187 ? 0.082  0.082  0.082  0       0       0       168 ALA D O   
3203 C CB  . ALA B 187 ? 0.038  0.038  0.038  0       0       0       168 ALA D CB  
3204 N N   . ALA B 188 ? 0.038  0.038  0.038  0       0       0       169 ALA D N   
3205 C CA  . ALA B 188 ? 0.038  0.038  0.038  0       0       0       169 ALA D CA  
3206 C C   . ALA B 188 ? 0.0737 0.0737 0.0737 0       0       0       169 ALA D C   
3207 O O   . ALA B 188 ? 0.038  0.038  0.038  0       0       0       169 ALA D O   
3208 C CB  . ALA B 188 ? 0.038  0.038  0.038  0       0       0       169 ALA D CB  
3209 N N   . CYS B 189 ? 0.038  0.038  0.038  0       0       0       170 CYS D N   
3210 C CA  . CYS B 189 ? 0.038  0.038  0.038  0       0       0       170 CYS D CA  
3211 C C   . CYS B 189 ? 0.0593 0.0593 0.0593 0       0       0       170 CYS D C   
3212 O O   . CYS B 189 ? 0.038  0.038  0.038  0       0       0       170 CYS D O   
3213 C CB  . CYS B 189 ? 0.038  0.038  0.038  0       0       0       170 CYS D CB  
3214 S SG  . CYS B 189 ? 0.042  0.042  0.042  0       0       0       170 CYS D SG  
3215 N N   . PRO B 190 ? 0.038  0.038  0.038  0       0       0       171 PRO D N   
3216 C CA  . PRO B 190 ? 0.038  0.038  0.038  0       0       0       171 PRO D CA  
3217 C C   . PRO B 190 ? 0.0795 0.0795 0.0795 0       0       0       171 PRO D C   
3218 O O   . PRO B 190 ? 0.0675 0.0675 0.0675 0       0       0       171 PRO D O   
3219 C CB  . PRO B 190 ? 0.0676 0.0676 0.0676 0       0       0       171 PRO D CB  
3220 C CG  . PRO B 190 ? 0.0649 0.0649 0.0649 0       0       0       171 PRO D CG  
3221 C CD  . PRO B 190 ? 0.0673 0.0673 0.0673 0       0       0       171 PRO D CD  
3222 N N   . ASP B 191 ? 0.038  0.038  0.038  0       0       0       172 ASP D N   
3223 C CA  . ASP B 191 ? 0.0483 0.0483 0.0483 0       0       0       172 ASP D CA  
3224 C C   . ASP B 191 ? 0.0754 0.0754 0.0754 0       0       0       172 ASP D C   
3225 O O   . ASP B 191 ? 0.038  0.038  0.038  0       0       0       172 ASP D O   
3226 C CB  . ASP B 191 ? 0.0783 0.0783 0.0783 0       0       0       172 ASP D CB  
3227 C CG  . ASP B 191 ? 0.1449 0.1449 0.1449 0       0       0       172 ASP D CG  
3228 O OD1 . ASP B 191 ? 0.1436 0.1436 0.1436 0       0       0       172 ASP D OD1 
3229 O OD2 . ASP B 191 ? 0.177  0.177  0.177  0       0       0       172 ASP D OD2 
3230 N N   . LEU B 192 ? 0.038  0.038  0.038  0       0       0       173 LEU D N   
3231 C CA  . LEU B 192 ? 0.0449 0.0449 0.0449 0       0       0       173 LEU D CA  
3232 C C   . LEU B 192 ? 0.0661 0.0661 0.0661 0       0       0       173 LEU D C   
3233 O O   . LEU B 192 ? 0.038  0.038  0.038  0       0       0       173 LEU D O   
3234 C CB  . LEU B 192 ? 0.057  0.057  0.057  0       0       0       173 LEU D CB  
3235 C CG  . LEU B 192 ? 0.0784 0.0784 0.0784 0       0       0       173 LEU D CG  
3236 C CD1 . LEU B 192 ? 0.0758 0.0758 0.0758 0       0       0       173 LEU D CD1 
3237 C CD2 . LEU B 192 ? 0.0679 0.0679 0.0679 0       0       0       173 LEU D CD2 
3238 N N   . PRO B 193 ? 0.0398 0.0398 0.0398 0       0       0       174 PRO D N   
3239 C CA  . PRO B 193 ? 0.038  0.038  0.038  0       0       0       174 PRO D CA  
3240 C C   . PRO B 193 ? 0.0636 0.0636 0.0636 0       0       0       174 PRO D C   
3241 O O   . PRO B 193 ? 0.038  0.038  0.038  0       0       0       174 PRO D O   
3242 C CB  . PRO B 193 ? 0.065  0.065  0.065  0       0       0       174 PRO D CB  
3243 C CG  . PRO B 193 ? 0.0637 0.0637 0.0637 0       0       0       174 PRO D CG  
3244 C CD  . PRO B 193 ? 0.0729 0.0729 0.0729 0       0       0       174 PRO D CD  
3245 N N   . THR B 194 ? 0.038  0.038  0.038  0       0       0       175 THR D N   
3246 C CA  . THR B 194 ? 0.038  0.038  0.038  0       0       0       175 THR D CA  
3247 C C   . THR B 194 ? 0.05   0.05   0.05   0       0       0       175 THR D C   
3248 O O   . THR B 194 ? 0.038  0.038  0.038  0       0       0       175 THR D O   
3249 C CB  . THR B 194 ? 0.0862 0.0862 0.0862 0       0       0       175 THR D CB  
3250 O OG1 . THR B 194 ? 0.0738 0.0738 0.0738 0       0       0       175 THR D OG1 
3251 C CG2 . THR B 194 ? 0.0531 0.0531 0.0531 0       0       0       175 THR D CG2 
3252 N N   . TYR B 195 ? 0.038  0.038  0.038  0       0       0       176 TYR D N   
3253 C CA  . TYR B 195 ? 0.038  0.038  0.038  0       0       0       176 TYR D CA  
3254 C C   . TYR B 195 ? 0.0642 0.0642 0.0642 0       0       0       176 TYR D C   
3255 O O   . TYR B 195 ? 0.038  0.038  0.038  0       0       0       176 TYR D O   
3256 C CB  . TYR B 195 ? 0.038  0.038  0.038  0       0       0       176 TYR D CB  
3257 C CG  . TYR B 195 ? 0.038  0.038  0.038  0       0       0       176 TYR D CG  
3258 C CD1 . TYR B 195 ? 0.0397 0.0397 0.0397 0       0       0       176 TYR D CD1 
3259 C CD2 . TYR B 195 ? 0.038  0.038  0.038  0       0       0       176 TYR D CD2 
3260 C CE1 . TYR B 195 ? 0.0531 0.0531 0.0531 0       0       0       176 TYR D CE1 
3261 C CE2 . TYR B 195 ? 0.038  0.038  0.038  0       0       0       176 TYR D CE2 
3262 C CZ  . TYR B 195 ? 0.0823 0.0823 0.0823 0       0       0       176 TYR D CZ  
3263 O OH  . TYR B 195 ? 0.038  0.038  0.038  0       0       0       176 TYR D OH  
3264 N N   . CYS B 196 ? 0.038  0.038  0.038  0       0       0       177 CYS D N   
3265 C CA  . CYS B 196 ? 0.0465 0.0465 0.0465 0       0       0       177 CYS D CA  
3266 C C   . CYS B 196 ? 0.0605 0.0605 0.0605 0       0       0       177 CYS D C   
3267 O O   . CYS B 196 ? 0.038  0.038  0.038  0       0       0       177 CYS D O   
3268 C CB  . CYS B 196 ? 0.0789 0.0789 0.0789 0       0       0       177 CYS D CB  
3269 S SG  . CYS B 196 ? 0.0894 0.0894 0.0894 0       0       0       177 CYS D SG  
3270 N N   . ARG B 197 ? 0.038  0.038  0.038  0       0       0       178 ARG D N   
3271 C CA  . ARG B 197 ? 0.0431 0.0431 0.0431 0       0       0       178 ARG D CA  
3272 C C   . ARG B 197 ? 0.062  0.062  0.062  0       0       0       178 ARG D C   
3273 O O   . ARG B 197 ? 0.038  0.038  0.038  0       0       0       178 ARG D O   
3274 C CB  . ARG B 197 ? 0.0997 0.0997 0.0997 0       0       0       178 ARG D CB  
3275 C CG  . ARG B 197 ? 0.1031 0.2464 0.1594 -0.0341 0.0222  -0.0982 178 ARG D CG  
3276 C CD  . ARG B 197 ? 0.2958 0.4747 0.3572 -0.0302 0.0181  -0.1105 178 ARG D CD  
3277 N NE  . ARG B 197 ? 0.3128 0.5855 0.4063 -0.0322 0.0191  -0.164  178 ARG D NE  
3278 C CZ  . ARG B 197 ? 0.4285 0.8034 0.5625 -0.0345 0.0208  -0.2277 178 ARG D CZ  
3279 N NH1 . ARG B 197 ? 0.3387 0.6924 0.465  -0.0146 0.0087  -0.212  178 ARG D NH1 
3280 N NH2 . ARG B 197 ? 0.3116 0.6612 0.4435 -0.0402 0.0249  -0.2198 178 ARG D NH2 
3281 N N   . ALA B 198 ? 0.038  0.038  0.038  0       0       0       179 ALA D N   
3282 C CA  . ALA B 198 ? 0.038  0.038  0.038  0       0       0       179 ALA D CA  
3283 C C   . ALA B 198 ? 0.054  0.054  0.054  0       0       0       179 ALA D C   
3284 O O   . ALA B 198 ? 0.038  0.038  0.038  0       0       0       179 ALA D O   
3285 C CB  . ALA B 198 ? 0.038  0.038  0.038  0       0       0       179 ALA D CB  
3286 N N   . LEU B 199 ? 0.038  0.038  0.038  0       0       0       180 LEU D N   
3287 C CA  . LEU B 199 ? 0.038  0.038  0.038  0       0       0       180 LEU D CA  
3288 C C   . LEU B 199 ? 0.0616 0.0616 0.0616 0       0       0       180 LEU D C   
3289 O O   . LEU B 199 ? 0.038  0.038  0.038  0       0       0       180 LEU D O   
3290 C CB  . LEU B 199 ? 0.038  0.038  0.038  0       0       0       180 LEU D CB  
3291 C CG  . LEU B 199 ? 0.0622 0.0622 0.0622 0       0       0       180 LEU D CG  
3292 C CD1 . LEU B 199 ? 0.0514 0.0514 0.0514 0       0       0       180 LEU D CD1 
3293 C CD2 . LEU B 199 ? 0.038  0.038  0.038  0       0       0       180 LEU D CD2 
3294 N N   . ARG B 200 ? 0.038  0.038  0.038  0       0       0       181 ARG D N   
3295 C CA  . ARG B 200 ? 0.038  0.038  0.038  0       0       0       181 ARG D CA  
3296 C C   . ARG B 200 ? 0.063  0.063  0.063  0       0       0       181 ARG D C   
3297 O O   . ARG B 200 ? 0.038  0.038  0.038  0       0       0       181 ARG D O   
3298 C CB  . ARG B 200 ? 0.038  0.038  0.038  0       0       0       181 ARG D CB  
3299 C CG  . ARG B 200 ? 0.1045 0.1045 0.1045 0       0       0       181 ARG D CG  
3300 C CD  . ARG B 200 ? 0.1263 0.1535 0.1386 -0.0138 0.0102  -0.0244 181 ARG D CD  
3301 N NE  . ARG B 200 ? 0.1265 0.1537 0.1389 -0.0145 0.0108  -0.025  181 ARG D NE  
3302 C CZ  . ARG B 200 ? 0.202  0.3641 0.2798 -0.0998 0.0772  -0.1621 181 ARG D CZ  
3303 N NH1 . ARG B 200 ? 0.2698 0.3999 0.3356 -0.0894 0.0712  -0.1399 181 ARG D NH1 
3304 N NH2 . ARG B 200 ? 0.1363 0.2174 0.1764 -0.0522 0.0409  -0.0836 181 ARG D NH2 
3305 N N   . ASN B 201 ? 0.038  0.038  0.038  0       0       0       182 ASN D N   
3306 C CA  . ASN B 201 ? 0.038  0.038  0.038  0       0       0       182 ASN D CA  
3307 C C   . ASN B 201 ? 0.0827 0.0827 0.0827 0       0       0       182 ASN D C   
3308 O O   . ASN B 201 ? 0.0648 0.0648 0.0648 0       0       0       182 ASN D O   
3309 C CB  . ASN B 201 ? 0.038  0.038  0.038  0       0       0       182 ASN D CB  
3310 C CG  . ASN B 201 ? 0.0821 0.0821 0.0821 0       0       0       182 ASN D CG  
3311 O OD1 . ASN B 201 ? 0.038  0.038  0.038  0       0       0       182 ASN D OD1 
3312 N ND2 . ASN B 201 ? 0.038  0.038  0.038  0       0       0       182 ASN D ND2 
3313 N N   . LEU B 202 ? 0.038  0.038  0.038  0       0       0       183 LEU D N   
3314 C CA  . LEU B 202 ? 0.038  0.038  0.038  0       0       0       183 LEU D CA  
3315 C C   . LEU B 202 ? 0.0536 0.0536 0.0536 0       0       0       183 LEU D C   
3316 O O   . LEU B 202 ? 0.038  0.038  0.038  0       0       0       183 LEU D O   
3317 C CB  . LEU B 202 ? 0.038  0.038  0.038  0       0       0       183 LEU D CB  
3318 C CG  . LEU B 202 ? 0.0804 0.0804 0.0804 0       0       0       183 LEU D CG  
3319 C CD1 . LEU B 202 ? 0.0653 0.0653 0.0653 0       0       0       183 LEU D CD1 
3320 C CD2 . LEU B 202 ? 0.088  0.088  0.088  0       0       0       183 LEU D CD2 
3321 N N   . GLY B 203 ? 0.038  0.038  0.038  0       0       0       184 GLY D N   
3322 C CA  . GLY B 203 ? 0.038  0.038  0.038  0       0       0       184 GLY D CA  
3323 C C   . GLY B 203 ? 0.0514 0.0514 0.0514 0       0       0       184 GLY D C   
3324 O O   . GLY B 203 ? 0.038  0.038  0.038  0       0       0       184 GLY D O   
3325 N N   . SER B 204 ? 0.038  0.038  0.038  0       0       0       185 SER D N   
3326 C CA  . SER B 204 ? 0.038  0.038  0.038  0       0       0       185 SER D CA  
3327 C C   . SER B 204 ? 0.0736 0.0736 0.0736 0       0       0       185 SER D C   
3328 O O   . SER B 204 ? 0.052  0.0574 0.0561 -0.0043 0.004   -0.0071 185 SER D O   
3329 C CB  . SER B 204 ? 0.0384 0.0404 0.0395 -0.001  0.0008  -0.0019 185 SER D CB  
3330 O OG  . SER B 204 ? 0.0487 0.0487 0.0487 0       0       0       185 SER D OG  
3331 N N   . LEU B 205 ? 0.038  0.038  0.038  0       0       0       186 LEU D N   
3332 C CA  . LEU B 205 ? 0.038  0.038  0.038  0       0       0       186 LEU D CA  
3333 C C   . LEU B 205 ? 0.0701 0.0701 0.0701 0       0       0       186 LEU D C   
3334 O O   . LEU B 205 ? 0.038  0.038  0.038  0       0       0       186 LEU D O   
3335 C CB  . LEU B 205 ? 0.038  0.038  0.038  0       0       0       186 LEU D CB  
3336 C CG  . LEU B 205 ? 0.0837 0.0837 0.0837 0       0       0       186 LEU D CG  
3337 C CD1 . LEU B 205 ? 0.0542 0.0542 0.0542 0       0       0       186 LEU D CD1 
3338 C CD2 . LEU B 205 ? 0.0769 0.0769 0.0769 0       0       0       186 LEU D CD2 
3339 N N   . LEU B 206 ? 0.038  0.038  0.038  0       0       0       187 LEU D N   
3340 C CA  . LEU B 206 ? 0.038  0.038  0.038  0       0       0       187 LEU D CA  
3341 C C   . LEU B 206 ? 0.0786 0.0786 0.0786 0       0       0       187 LEU D C   
3342 O O   . LEU B 206 ? 0.0412 0.0428 0.0438 -0.0039 0.0043  -0.0053 187 LEU D O   
3343 C CB  . LEU B 206 ? 0.038  0.038  0.038  0       0       0       187 LEU D CB  
3344 C CG  . LEU B 206 ? 0.087  0.087  0.087  0       0       0       187 LEU D CG  
3345 C CD1 . LEU B 206 ? 0.0733 0.0733 0.0733 0       0       0       187 LEU D CD1 
3346 C CD2 . LEU B 206 ? 0.0844 0.0844 0.0844 0       0       0       187 LEU D CD2 
3347 N N   . LYS B 207 ? 0.038  0.038  0.038  0       0       0       188 LYS D N   
3348 C CA  . LYS B 207 ? 0.0575 0.0548 0.0673 -0.0181 0.0239  -0.0222 188 LYS D CA  
3349 C C   . LYS B 207 ? 0.0898 0.0857 0.101  -0.0206 0.0278  -0.0252 188 LYS D C   
3350 O O   . LYS B 207 ? 0.0417 0.0411 0.0434 -0.0034 0.0045  -0.0041 188 LYS D O   
3351 C CB  . LYS B 207 ? 0.0962 0.0858 0.1061 -0.022  0.0324  -0.0256 188 LYS D CB  
3352 C CG  . LYS B 207 ? 0.2405 0.191  0.2647 -0.0695 0.1099  -0.0775 188 LYS D CG  
3353 C CD  . LYS B 207 ? 0.3598 0.214  0.3865 -0.1248 0.2304  -0.1323 188 LYS D CD  
3354 C CE  . LYS B 207 ? 0.5318 0.3324 0.5434 -0.1357 0.3009  -0.1466 188 LYS D CE  
3355 N NZ  . LYS B 207 ? 0.7369 0.5387 0.6944 -0.0911 0.3898  -0.1419 188 LYS D NZ  
3356 N N   . PRO B 208 ? 0.0858 0.0752 0.1099 -0.0422 0.0586  -0.0517 189 PRO D N   
3357 C CA  . PRO B 208 ? 0.0907 0.0761 0.1161 -0.0448 0.0642  -0.0546 189 PRO D CA  
3358 C C   . PRO B 208 ? 0.1276 0.106  0.1456 -0.0354 0.0561  -0.0415 189 PRO D C   
3359 O O   . PRO B 208 ? 0.1138 0.0808 0.1316 -0.0388 0.0669  -0.0443 189 PRO D O   
3360 C CB  . PRO B 208 ? 0.1437 0.117  0.1873 -0.0729 0.1071  -0.0892 189 PRO D CB  
3361 C CG  . PRO B 208 ? 0.1629 0.1422 0.225  -0.0976 0.1361  -0.1224 189 PRO D CG  
3362 C CD  . PRO B 208 ? 0.1246 0.1077 0.1646 -0.0659 0.0927  -0.0816 189 PRO D CD  
3363 N N   . GLY B 209 ? 0.0675 0.054  0.0783 -0.0217 0.0344  -0.0254 190 GLY D N   
3364 C CA  . GLY B 209 ? 0.0578 0.0462 0.0635 -0.0127 0.0225  -0.0144 190 GLY D CA  
3365 C C   . GLY B 209 ? 0.067  0.067  0.067  0       0       0       190 GLY D C   
3366 O O   . GLY B 209 ? 0.038  0.038  0.038  0       0       0       190 GLY D O   
3367 N N   . GLY B 210 ? 0.038  0.038  0.038  0       0       0       191 GLY D N   
3368 C CA  . GLY B 210 ? 0.038  0.038  0.038  0       0       0       191 GLY D CA  
3369 C C   . GLY B 210 ? 0.0742 0.0742 0.0742 0       0       0       191 GLY D C   
3370 O O   . GLY B 210 ? 0.038  0.038  0.038  0       0       0       191 GLY D O   
3371 N N   . PHE B 211 ? 0.038  0.038  0.038  0       0       0       192 PHE D N   
3372 C CA  . PHE B 211 ? 0.0434 0.0434 0.0434 0       0       0       192 PHE D CA  
3373 C C   . PHE B 211 ? 0.0741 0.0741 0.0741 0       0       0       192 PHE D C   
3374 O O   . PHE B 211 ? 0.038  0.038  0.038  0       0       0       192 PHE D O   
3375 C CB  . PHE B 211 ? 0.0994 0.0994 0.0994 0       0       0       192 PHE D CB  
3376 C CG  . PHE B 211 ? 0.1224 0.1224 0.1224 0       0       0       192 PHE D CG  
3377 C CD1 . PHE B 211 ? 0.0965 0.0965 0.0965 0       0       0       192 PHE D CD1 
3378 C CD2 . PHE B 211 ? 0.1051 0.1051 0.1051 0       0       0       192 PHE D CD2 
3379 C CE1 . PHE B 211 ? 0.0871 0.0871 0.0871 0       0       0       192 PHE D CE1 
3380 C CE2 . PHE B 211 ? 0.0943 0.0754 0.0927 -0.007  0.0204  -0.0067 192 PHE D CE2 
3381 C CZ  . PHE B 211 ? 0.0995 0.0995 0.0995 0       0       0       192 PHE D CZ  
3382 N N   . LEU B 212 ? 0.038  0.038  0.038  0       0       0       193 LEU D N   
3383 C CA  . LEU B 212 ? 0.038  0.038  0.038  0       0       0       193 LEU D CA  
3384 C C   . LEU B 212 ? 0.067  0.067  0.067  0       0       0       193 LEU D C   
3385 O O   . LEU B 212 ? 0.038  0.038  0.038  0       0       0       193 LEU D O   
3386 C CB  . LEU B 212 ? 0.038  0.038  0.038  0       0       0       193 LEU D CB  
3387 C CG  . LEU B 212 ? 0.0875 0.0875 0.0875 0       0       0       193 LEU D CG  
3388 C CD1 . LEU B 212 ? 0.0812 0.0812 0.0812 0       0       0       193 LEU D CD1 
3389 C CD2 . LEU B 212 ? 0.0845 0.0845 0.0845 0       0       0       193 LEU D CD2 
3390 N N   . VAL B 213 ? 0.038  0.038  0.038  0       0       0       194 VAL D N   
3391 C CA  . VAL B 213 ? 0.038  0.038  0.038  0       0       0       194 VAL D CA  
3392 C C   . VAL B 213 ? 0.0653 0.0653 0.0653 0       0       0       194 VAL D C   
3393 O O   . VAL B 213 ? 0.038  0.038  0.038  0       0       0       194 VAL D O   
3394 C CB  . VAL B 213 ? 0.0517 0.0517 0.0517 0       0       0       194 VAL D CB  
3395 C CG1 . VAL B 213 ? 0.038  0.038  0.038  0       0       0       194 VAL D CG1 
3396 C CG2 . VAL B 213 ? 0.0422 0.0422 0.0422 0       0       0       194 VAL D CG2 
3397 N N   . ILE B 214 ? 0.038  0.038  0.038  0       0       0       195 ILE D N   
3398 C CA  . ILE B 214 ? 0.038  0.038  0.038  0       0       0       195 ILE D CA  
3399 C C   . ILE B 214 ? 0.0508 0.0508 0.0508 0       0       0       195 ILE D C   
3400 O O   . ILE B 214 ? 0.038  0.038  0.038  0       0       0       195 ILE D O   
3401 C CB  . ILE B 214 ? 0.0553 0.0553 0.0553 0       0       0       195 ILE D CB  
3402 C CG1 . ILE B 214 ? 0.0709 0.0709 0.0709 0       0       0       195 ILE D CG1 
3403 C CG2 . ILE B 214 ? 0.0469 0.0469 0.0469 0       0       0       195 ILE D CG2 
3404 C CD1 . ILE B 214 ? 0.0925 0.0925 0.0925 0       0       0       195 ILE D CD1 
3405 N N   . MET B 215 ? 0.038  0.038  0.038  0       0       0       196 MET D N   
3406 C CA  . MET B 215 ? 0.038  0.038  0.038  0       0       0       196 MET D CA  
3407 C C   . MET B 215 ? 0.0641 0.0641 0.0641 0       0       0       196 MET D C   
3408 O O   . MET B 215 ? 0.038  0.038  0.038  0       0       0       196 MET D O   
3409 C CB  . MET B 215 ? 0.0422 0.0422 0.0422 0       0       0       196 MET D CB  
3410 C CG  . MET B 215 ? 0.0745 0.0745 0.0745 0       0       0       196 MET D CG  
3411 S SD  . MET B 215 ? 0.0893 0.0893 0.0893 0       0       0       196 MET D SD  
3412 C CE  . MET B 215 ? 0.0767 0.0767 0.0767 0       0       0       196 MET D CE  
3413 N N   . ASP B 216 ? 0.038  0.038  0.038  0       0       0       197 ASP D N   
3414 C CA  . ASP B 216 ? 0.038  0.038  0.038  0       0       0       197 ASP D CA  
3415 C C   . ASP B 216 ? 0.0569 0.0569 0.0569 0       0       0       197 ASP D C   
3416 O O   . ASP B 216 ? 0.038  0.038  0.038  0       0       0       197 ASP D O   
3417 C CB  . ASP B 216 ? 0.038  0.038  0.038  0       0       0       197 ASP D CB  
3418 C CG  . ASP B 216 ? 0.0587 0.0587 0.0587 0       0       0       197 ASP D CG  
3419 O OD1 . ASP B 216 ? 0.038  0.038  0.038  0       0       0       197 ASP D OD1 
3420 O OD2 . ASP B 216 ? 0.0497 0.0497 0.0497 0       0       0       197 ASP D OD2 
3421 N N   . ALA B 217 ? 0.038  0.038  0.038  0       0       0       198 ALA D N   
3422 C CA  . ALA B 217 ? 0.038  0.038  0.038  0       0       0       198 ALA D CA  
3423 C C   . ALA B 217 ? 0.0633 0.0633 0.0633 0       0       0       198 ALA D C   
3424 O O   . ALA B 217 ? 0.038  0.038  0.038  0       0       0       198 ALA D O   
3425 C CB  . ALA B 217 ? 0.038  0.038  0.038  0       0       0       198 ALA D CB  
3426 N N   . LEU B 218 ? 0.038  0.038  0.038  0       0       0       199 LEU D N   
3427 C CA  . LEU B 218 ? 0.038  0.038  0.038  0       0       0       199 LEU D CA  
3428 C C   . LEU B 218 ? 0.0637 0.0637 0.0637 0       0       0       199 LEU D C   
3429 O O   . LEU B 218 ? 0.038  0.038  0.038  0       0       0       199 LEU D O   
3430 C CB  . LEU B 218 ? 0.038  0.038  0.038  0       0       0       199 LEU D CB  
3431 C CG  . LEU B 218 ? 0.0484 0.0484 0.0484 0       0       0       199 LEU D CG  
3432 C CD1 . LEU B 218 ? 0.038  0.038  0.038  0       0       0       199 LEU D CD1 
3433 C CD2 . LEU B 218 ? 0.05   0.05   0.05   0       0       0       199 LEU D CD2 
3434 N N   . LYS B 219 ? 0.038  0.038  0.038  0       0       0       200 LYS D N   
3435 C CA  . LYS B 219 ? 0.038  0.038  0.038  0       0       0       200 LYS D CA  
3436 C C   . LYS B 219 ? 0.0788 0.0788 0.0788 0       0       0       200 LYS D C   
3437 O O   . LYS B 219 ? 0.038  0.038  0.038  0       0       0       200 LYS D O   
3438 C CB  . LYS B 219 ? 0.0525 0.0525 0.0525 0       0       0       200 LYS D CB  
3439 C CG  . LYS B 219 ? 0.2254 0.2254 0.2254 0       0       0       200 LYS D CG  
3440 C CD  . LYS B 219 ? 0.1887 0.1887 0.1887 0       0       0       200 LYS D CD  
3441 C CE  . LYS B 219 ? 0.2283 0.2016 0.4554 0.0016  -0.0824 -0.005  200 LYS D CE  
3442 N NZ  . LYS B 219 ? 0.3646 0.3293 0.6282 0       -0.1027 -0.0001 200 LYS D NZ  
3443 N N   . SER B 220 ? 0.038  0.038  0.038  0       0       0       201 SER D N   
3444 C CA  . SER B 220 ? 0.038  0.038  0.038  0       0       0       201 SER D CA  
3445 C C   . SER B 220 ? 0.0715 0.0715 0.0715 0       0       0       201 SER D C   
3446 O O   . SER B 220 ? 0.038  0.038  0.038  0       0       0       201 SER D O   
3447 C CB  . SER B 220 ? 0.038  0.038  0.038  0       0       0       201 SER D CB  
3448 O OG  . SER B 220 ? 0.038  0.038  0.038  0       0       0       201 SER D OG  
3449 N N   . SER B 221 ? 0.038  0.038  0.038  0       0       0       202 SER D N   
3450 C CA  . SER B 221 ? 0.038  0.038  0.038  0       0       0       202 SER D CA  
3451 C C   . SER B 221 ? 0.0677 0.0677 0.0677 0       0       0       202 SER D C   
3452 O O   . SER B 221 ? 0.038  0.038  0.038  0       0       0       202 SER D O   
3453 C CB  . SER B 221 ? 0.0456 0.0456 0.0456 0       0       0       202 SER D CB  
3454 O OG  . SER B 221 ? 0.0548 0.0548 0.0548 0       0       0       202 SER D OG  
3455 N N   . TYR B 222 ? 0.038  0.038  0.038  0       0       0       203 TYR D N   
3456 C CA  . TYR B 222 ? 0.038  0.038  0.038  0       0       0       203 TYR D CA  
3457 C C   . TYR B 222 ? 0.0684 0.0684 0.0684 0       0       0       203 TYR D C   
3458 O O   . TYR B 222 ? 0.038  0.038  0.038  0       0       0       203 TYR D O   
3459 C CB  . TYR B 222 ? 0.038  0.038  0.038  0       0       0       203 TYR D CB  
3460 C CG  . TYR B 222 ? 0.038  0.038  0.038  0       0       0       203 TYR D CG  
3461 C CD1 . TYR B 222 ? 0.0557 0.0557 0.0557 0       0       0       203 TYR D CD1 
3462 C CD2 . TYR B 222 ? 0.0402 0.0402 0.0402 0       0       0       203 TYR D CD2 
3463 C CE1 . TYR B 222 ? 0.0595 0.0595 0.0595 0       0       0       203 TYR D CE1 
3464 C CE2 . TYR B 222 ? 0.0523 0.0523 0.0523 0       0       0       203 TYR D CE2 
3465 C CZ  . TYR B 222 ? 0.0692 0.0692 0.0692 0       0       0       203 TYR D CZ  
3466 O OH  . TYR B 222 ? 0.0905 0.0905 0.0905 0       0       0       203 TYR D OH  
3467 N N   . TYR B 223 ? 0.038  0.038  0.038  0       0       0       204 TYR D N   
3468 C CA  . TYR B 223 ? 0.038  0.038  0.038  0       0       0       204 TYR D CA  
3469 C C   . TYR B 223 ? 0.0727 0.0727 0.0727 0       0       0       204 TYR D C   
3470 O O   . TYR B 223 ? 0.038  0.038  0.038  0       0       0       204 TYR D O   
3471 C CB  . TYR B 223 ? 0.038  0.038  0.038  0       0       0       204 TYR D CB  
3472 C CG  . TYR B 223 ? 0.038  0.038  0.038  0       0       0       204 TYR D CG  
3473 C CD1 . TYR B 223 ? 0.0396 0.0396 0.0396 0       0       0       204 TYR D CD1 
3474 C CD2 . TYR B 223 ? 0.038  0.038  0.038  0       0       0       204 TYR D CD2 
3475 C CE1 . TYR B 223 ? 0.038  0.038  0.038  0       0       0       204 TYR D CE1 
3476 C CE2 . TYR B 223 ? 0.038  0.038  0.038  0       0       0       204 TYR D CE2 
3477 C CZ  . TYR B 223 ? 0.0695 0.0695 0.0695 0       0       0       204 TYR D CZ  
3478 O OH  . TYR B 223 ? 0.038  0.038  0.038  0       0       0       204 TYR D OH  
3479 N N   . MET B 224 ? 0.038  0.038  0.038  0       0       0       205 MET D N   
3480 C CA  . MET B 224 ? 0.038  0.038  0.038  0       0       0       205 MET D CA  
3481 C C   . MET B 224 ? 0.0547 0.0547 0.0547 0       0       0       205 MET D C   
3482 O O   . MET B 224 ? 0.038  0.038  0.038  0       0       0       205 MET D O   
3483 C CB  . MET B 224 ? 0.038  0.038  0.038  0       0       0       205 MET D CB  
3484 C CG  . MET B 224 ? 0.0385 0.0385 0.0385 0       0       0       205 MET D CG  
3485 S SD  . MET B 224 ? 0.0396 0.0396 0.0396 0       0       0       205 MET D SD  
3486 C CE  . MET B 224 ? 0.0581 0.0466 0.0791 -0.0132 0.0287  -0.0188 205 MET D CE  
3487 N N   . ILE B 225 ? 0.038  0.038  0.038  0       0       0       206 ILE D N   
3488 C CA  . ILE B 225 ? 0.038  0.038  0.038  0       0       0       206 ILE D CA  
3489 C C   . ILE B 225 ? 0.0893 0.0857 0.1091 -0.0177 0.0278  -0.0251 206 ILE D C   
3490 O O   . ILE B 225 ? 0.0642 0.0537 0.0829 -0.0203 0.0343  -0.0265 206 ILE D O   
3491 C CB  . ILE B 225 ? 0.0653 0.0653 0.0653 0       0       0       206 ILE D CB  
3492 C CG1 . ILE B 225 ? 0.0612 0.0612 0.0612 0       0       0       206 ILE D CG1 
3493 C CG2 . ILE B 225 ? 0.0662 0.0662 0.0662 0       0       0       206 ILE D CG2 
3494 C CD1 . ILE B 225 ? 0.038  0.038  0.038  0       0       0       206 ILE D CD1 
3495 N N   . GLY B 226 ? 0.0724 0.069  0.1115 -0.0327 0.0503  -0.0477 207 GLY D N   
3496 C CA  . GLY B 226 ? 0.1024 0.0849 0.1611 -0.055  0.0891  -0.076  207 GLY D CA  
3497 C C   . GLY B 226 ? 0.1382 0.1064 0.1968 -0.0544 0.0976  -0.0731 207 GLY D C   
3498 O O   . GLY B 226 ? 0.1003 0.0802 0.1519 -0.0402 0.0728  -0.0569 207 GLY D O   
3499 N N   . GLU B 227 ? 0.1322 0.0761 0.1847 -0.0599 0.1175  -0.0748 208 GLU D N   
3500 C CA  . GLU B 227 ? 0.1449 0.0706 0.1919 -0.0569 0.1264  -0.0685 208 GLU D CA  
3501 C C   . GLU B 227 ? 0.1484 0.0916 0.1767 -0.0367 0.0879  -0.0431 208 GLU D C   
3502 O O   . GLU B 227 ? 0.1157 0.0517 0.1389 -0.0326 0.0885  -0.0372 208 GLU D O   
3503 C CB  . GLU B 227 ? 0.2216 0.0951 0.2693 -0.0752 0.1839  -0.0856 208 GLU D CB  
3504 C CG  . GLU B 227 ? 0.3394 0.1146 0.4452 -0.1485 0.3476  -0.1729 208 GLU D CG  
3505 C CD  . GLU B 227 ? 0.7636 0.3377 0.8385 -0.1546 0.5749  -0.303  208 GLU D CD  
3506 O OE1 . GLU B 227 ? 0.9531 0.4467 0.9907 -0.1055 0.6381  -0.3472 208 GLU D OE1 
3507 O OE2 . GLU B 227 ? 0.8287 0.3862 0.8904 -0.1647 0.6096  -0.3188 208 GLU D OE2 
3508 N N   . GLN B 228 ? 0.0864 0.0516 0.106  -0.0257 0.0574  -0.0304 209 GLN D N   
3509 C CA  . GLN B 228 ? 0.0582 0.0428 0.0651 -0.0098 0.0234  -0.0113 209 GLN D CA  
3510 C C   . GLN B 228 ? 0.0658 0.0658 0.0658 0       0       0       209 GLN D C   
3511 O O   . GLN B 228 ? 0.038  0.038  0.038  0       0       0       209 GLN D O   
3512 C CB  . GLN B 228 ? 0.0608 0.0544 0.0632 -0.0043 0.0098  -0.0049 209 GLN D CB  
3513 C CG  . GLN B 228 ? 0.1407 0.137  0.1417 -0.0022 0.0052  -0.0024 209 GLN D CG  
3514 C CD  . GLN B 228 ? 0.2546 0.1373 0.255  -0.0398 0.1298  -0.0399 209 GLN D CD  
3515 O OE1 . GLN B 228 ? 0.2085 0.1354 0.2055 -0.0192 0.0763  -0.0188 209 GLN D OE1 
3516 N NE2 . GLN B 228 ? 0.0598 0.0431 0.0581 -0.0045 0.0169  -0.0043 209 GLN D NE2 
3517 N N   . LYS B 229 ? 0.038  0.038  0.038  0       0       0       210 LYS D N   
3518 C CA  . LYS B 229 ? 0.038  0.038  0.038  0       0       0       210 LYS D CA  
3519 C C   . LYS B 229 ? 0.0717 0.0717 0.0717 0       0       0       210 LYS D C   
3520 O O   . LYS B 229 ? 0.038  0.038  0.038  0       0       0       210 LYS D O   
3521 C CB  . LYS B 229 ? 0.0503 0.0503 0.0503 0       0       0       210 LYS D CB  
3522 C CG  . LYS B 229 ? 0.183  0.183  0.183  0       0       0       210 LYS D CG  
3523 C CD  . LYS B 229 ? 0.2152 0.1557 0.2925 -0.0351 0.1076  -0.0498 210 LYS D CD  
3524 C CE  . LYS B 229 ? 0.3142 0.2626 0.4605 -0.0467 0.1336  -0.0788 210 LYS D CE  
3525 N NZ  . LYS B 229 ? 0.4714 0.4149 0.5725 -0.035  0.113   -0.054  210 LYS D NZ  
3526 N N   . PHE B 230 ? 0.038  0.038  0.038  0       0       0       211 PHE D N   
3527 C CA  . PHE B 230 ? 0.038  0.038  0.038  0       0       0       211 PHE D CA  
3528 C C   . PHE B 230 ? 0.0675 0.0675 0.0675 0       0       0       211 PHE D C   
3529 O O   . PHE B 230 ? 0.038  0.038  0.038  0       0       0       211 PHE D O   
3530 C CB  . PHE B 230 ? 0.0382 0.0382 0.0382 0       0       0       211 PHE D CB  
3531 C CG  . PHE B 230 ? 0.038  0.038  0.038  0       0       0       211 PHE D CG  
3532 C CD1 . PHE B 230 ? 0.0426 0.0426 0.0426 0       0       0       211 PHE D CD1 
3533 C CD2 . PHE B 230 ? 0.0499 0.0499 0.0499 0       0       0       211 PHE D CD2 
3534 C CE1 . PHE B 230 ? 0.038  0.038  0.038  0       0       0       211 PHE D CE1 
3535 C CE2 . PHE B 230 ? 0.0759 0.0759 0.0759 0       0       0       211 PHE D CE2 
3536 C CZ  . PHE B 230 ? 0.038  0.038  0.038  0       0       0       211 PHE D CZ  
3537 N N   . SER B 231 ? 0.038  0.038  0.038  0       0       0       212 SER D N   
3538 C CA  . SER B 231 ? 0.038  0.038  0.038  0       0       0       212 SER D CA  
3539 C C   . SER B 231 ? 0.053  0.053  0.053  0       0       0       212 SER D C   
3540 O O   . SER B 231 ? 0.038  0.038  0.038  0       0       0       212 SER D O   
3541 C CB  . SER B 231 ? 0.1171 0.1171 0.1171 0       0       0       212 SER D CB  
3542 O OG  . SER B 231 ? 0.1198 0.1198 0.1198 0       0       0       212 SER D OG  
3543 N N   . SER B 232 ? 0.038  0.038  0.038  0       0       0       213 SER D N   
3544 C CA  . SER B 232 ? 0.038  0.038  0.038  0       0       0       213 SER D CA  
3545 C C   . SER B 232 ? 0.0723 0.0723 0.0723 0       0       0       213 SER D C   
3546 O O   . SER B 232 ? 0.038  0.038  0.038  0       0       0       213 SER D O   
3547 C CB  . SER B 232 ? 0.045  0.045  0.045  0       0       0       213 SER D CB  
3548 O OG  . SER B 232 ? 0.038  0.038  0.038  0       0       0       213 SER D OG  
3549 N N   . LEU B 233 ? 0.038  0.038  0.038  0       0       0       214 LEU D N   
3550 C CA  . LEU B 233 ? 0.038  0.038  0.038  0       0       0       214 LEU D CA  
3551 C C   . LEU B 233 ? 0.0617 0.0617 0.0617 0       0       0       214 LEU D C   
3552 O O   . LEU B 233 ? 0.038  0.038  0.038  0       0       0       214 LEU D O   
3553 C CB  . LEU B 233 ? 0.038  0.038  0.038  0       0       0       214 LEU D CB  
3554 C CG  . LEU B 233 ? 0.0865 0.0865 0.0865 0       0       0       214 LEU D CG  
3555 C CD1 . LEU B 233 ? 0.0774 0.0774 0.0774 0       0       0       214 LEU D CD1 
3556 C CD2 . LEU B 233 ? 0.092  0.092  0.092  0       0       0       214 LEU D CD2 
3557 N N   . PRO B 234 ? 0.038  0.038  0.038  0       0       0       215 PRO D N   
3558 C CA  . PRO B 234 ? 0.038  0.038  0.038  0       0       0       215 PRO D CA  
3559 C C   . PRO B 234 ? 0.0875 0.0875 0.0875 0       0       0       215 PRO D C   
3560 O O   . PRO B 234 ? 0.0848 0.0848 0.0848 0       0       0       215 PRO D O   
3561 C CB  . PRO B 234 ? 0.0511 0.0511 0.0511 0       0       0       215 PRO D CB  
3562 C CG  . PRO B 234 ? 0.0853 0.0853 0.0853 0       0       0       215 PRO D CG  
3563 C CD  . PRO B 234 ? 0.0499 0.0499 0.0499 0       0       0       215 PRO D CD  
3564 N N   . LEU B 235 ? 0.046  0.046  0.046  0       0       0       216 LEU D N   
3565 C CA  . LEU B 235 ? 0.038  0.038  0.038  0       0       0       216 LEU D CA  
3566 C C   . LEU B 235 ? 0.0729 0.0729 0.0729 0       0       0       216 LEU D C   
3567 O O   . LEU B 235 ? 0.038  0.038  0.038  0       0       0       216 LEU D O   
3568 C CB  . LEU B 235 ? 0.038  0.038  0.038  0       0       0       216 LEU D CB  
3569 C CG  . LEU B 235 ? 0.0902 0.0902 0.0902 0       0       0       216 LEU D CG  
3570 C CD1 . LEU B 235 ? 0.0907 0.0907 0.0907 0       0       0       216 LEU D CD1 
3571 C CD2 . LEU B 235 ? 0.0669 0.0669 0.0669 0       0       0       216 LEU D CD2 
3572 N N   . GLY B 236 ? 0.038  0.038  0.038  0       0       0       217 GLY D N   
3573 C CA  . GLY B 236 ? 0.038  0.038  0.038  0       0       0       217 GLY D CA  
3574 C C   . GLY B 236 ? 0.0623 0.0623 0.0623 0       0       0       217 GLY D C   
3575 O O   . GLY B 236 ? 0.038  0.038  0.038  0       0       0       217 GLY D O   
3576 N N   . ARG B 237 ? 0.038  0.038  0.038  0       0       0       218 ARG D N   
3577 C CA  . ARG B 237 ? 0.038  0.038  0.038  0       0       0       218 ARG D CA  
3578 C C   . ARG B 237 ? 0.0598 0.0598 0.0598 0       0       0       218 ARG D C   
3579 O O   . ARG B 237 ? 0.038  0.038  0.038  0       0       0       218 ARG D O   
3580 C CB  . ARG B 237 ? 0.0815 0.0815 0.0815 0       0       0       218 ARG D CB  
3581 C CG  . ARG B 237 ? 0.1152 0.1152 0.1152 0       0       0       218 ARG D CG  
3582 C CD  . ARG B 237 ? 0.1755 0.1212 0.4474 -0.071  -0.1382 0.0858  218 ARG D CD  
3583 N NE  . ARG B 237 ? 0.3337 0.2297 0.7078 -0.2258 -0.1192 0.094   218 ARG D NE  
3584 C CZ  . ARG B 237 ? 0.7322 0.6922 0.9806 -0.1081 -0.1131 0.0979  218 ARG D CZ  
3585 N NH1 . ARG B 237 ? 0.6406 0.5694 0.9053 -0.1509 -0.1288 0.0939  218 ARG D NH1 
3586 N NH2 . ARG B 237 ? 0.4987 0.4642 0.7784 -0.1591 -0.0878 0.106   218 ARG D NH2 
3587 N N   . GLU B 238 ? 0.038  0.038  0.038  0       0       0       219 GLU D N   
3588 C CA  . GLU B 238 ? 0.038  0.038  0.038  0       0       0       219 GLU D CA  
3589 C C   . GLU B 238 ? 0.0639 0.0639 0.0639 0       0       0       219 GLU D C   
3590 O O   . GLU B 238 ? 0.038  0.038  0.038  0       0       0       219 GLU D O   
3591 C CB  . GLU B 238 ? 0.0577 0.0577 0.0577 0       0       0       219 GLU D CB  
3592 C CG  . GLU B 238 ? 0.1196 0.1196 0.1196 0       0       0       219 GLU D CG  
3593 C CD  . GLU B 238 ? 0.084  0.07   0.2962 -0.0143 -0.0735 0.0459  219 GLU D CD  
3594 O OE1 . GLU B 238 ? 0.1055 0.1055 0.1055 0       0       0       219 GLU D OE1 
3595 O OE2 . GLU B 238 ? 0.2906 0.2741 0.5029 -0.0163 -0.0795 0.049   219 GLU D OE2 
3596 N N   . ALA B 239 ? 0.038  0.038  0.038  0       0       0       220 ALA D N   
3597 C CA  . ALA B 239 ? 0.038  0.038  0.038  0       0       0       220 ALA D CA  
3598 C C   . ALA B 239 ? 0.0704 0.0704 0.0704 0       0       0       220 ALA D C   
3599 O O   . ALA B 239 ? 0.038  0.038  0.038  0       0       0       220 ALA D O   
3600 C CB  . ALA B 239 ? 0.0468 0.0468 0.0468 0       0       0       220 ALA D CB  
3601 N N   . VAL B 240 ? 0.038  0.038  0.038  0       0       0       221 VAL D N   
3602 C CA  . VAL B 240 ? 0.038  0.038  0.038  0       0       0       221 VAL D CA  
3603 C C   . VAL B 240 ? 0.0544 0.0544 0.0544 0       0       0       221 VAL D C   
3604 O O   . VAL B 240 ? 0.038  0.038  0.038  0       0       0       221 VAL D O   
3605 C CB  . VAL B 240 ? 0.0526 0.0526 0.0526 0       0       0       221 VAL D CB  
3606 C CG1 . VAL B 240 ? 0.043  0.043  0.043  0       0       0       221 VAL D CG1 
3607 C CG2 . VAL B 240 ? 0.038  0.038  0.038  0       0       0       221 VAL D CG2 
3608 N N   . GLU B 241 ? 0.038  0.038  0.038  0       0       0       222 GLU D N   
3609 C CA  . GLU B 241 ? 0.0425 0.0425 0.0425 0       0       0       222 GLU D CA  
3610 C C   . GLU B 241 ? 0.0661 0.0661 0.0661 0       0       0       222 GLU D C   
3611 O O   . GLU B 241 ? 0.038  0.038  0.038  0       0       0       222 GLU D O   
3612 C CB  . GLU B 241 ? 0.0675 0.0675 0.0675 0       0       0       222 GLU D CB  
3613 C CG  . GLU B 241 ? 0.1095 0.1095 0.1095 0       0       0       222 GLU D CG  
3614 C CD  . GLU B 241 ? 0.263  0.2577 0.5955 -0.2087 -0.0284 0.0799  222 GLU D CD  
3615 O OE1 . GLU B 241 ? 0.4384 0.4494 0.6572 -0.0957 -0.0295 0.0746  222 GLU D OE1 
3616 O OE2 . GLU B 241 ? 0.2564 0.2448 0.5109 -0.103  -0.061  0.0752  222 GLU D OE2 
3617 N N   . ALA B 242 ? 0.038  0.038  0.038  0       0       0       223 ALA D N   
3618 C CA  . ALA B 242 ? 0.038  0.038  0.038  0       0       0       223 ALA D CA  
3619 C C   . ALA B 242 ? 0.0624 0.0624 0.0624 0       0       0       223 ALA D C   
3620 O O   . ALA B 242 ? 0.038  0.038  0.038  0       0       0       223 ALA D O   
3621 C CB  . ALA B 242 ? 0.0395 0.0395 0.0395 0       0       0       223 ALA D CB  
3622 N N   . ALA B 243 ? 0.038  0.038  0.038  0       0       0       224 ALA D N   
3623 C CA  . ALA B 243 ? 0.038  0.038  0.038  0       0       0       224 ALA D CA  
3624 C C   . ALA B 243 ? 0.0714 0.0714 0.0714 0       0       0       224 ALA D C   
3625 O O   . ALA B 243 ? 0.038  0.038  0.038  0       0       0       224 ALA D O   
3626 C CB  . ALA B 243 ? 0.0409 0.0409 0.0409 0       0       0       224 ALA D CB  
3627 N N   . VAL B 244 ? 0.038  0.038  0.038  0       0       0       225 VAL D N   
3628 C CA  . VAL B 244 ? 0.038  0.038  0.038  0       0       0       225 VAL D CA  
3629 C C   . VAL B 244 ? 0.0697 0.0697 0.0697 0       0       0       225 VAL D C   
3630 O O   . VAL B 244 ? 0.038  0.038  0.038  0       0       0       225 VAL D O   
3631 C CB  . VAL B 244 ? 0.0526 0.0526 0.0526 0       0       0       225 VAL D CB  
3632 C CG1 . VAL B 244 ? 0.0393 0.0393 0.0393 0       0       0       225 VAL D CG1 
3633 C CG2 . VAL B 244 ? 0.038  0.038  0.038  0       0       0       225 VAL D CG2 
3634 N N   . LYS B 245 ? 0.038  0.038  0.038  0       0       0       226 LYS D N   
3635 C CA  . LYS B 245 ? 0.038  0.038  0.038  0       0       0       226 LYS D CA  
3636 C C   . LYS B 245 ? 0.0674 0.0674 0.0674 0       0       0       226 LYS D C   
3637 O O   . LYS B 245 ? 0.038  0.038  0.038  0       0       0       226 LYS D O   
3638 C CB  . LYS B 245 ? 0.0451 0.0451 0.0451 0       0       0       226 LYS D CB  
3639 C CG  . LYS B 245 ? 0.1645 0.1645 0.1645 0       0       0       226 LYS D CG  
3640 C CD  . LYS B 245 ? 0.1857 0.1857 0.1857 0       0       0       226 LYS D CD  
3641 C CE  . LYS B 245 ? 0.2225 0.2073 0.3001 -0.0179 0.0517  -0.0304 226 LYS D CE  
3642 N NZ  . LYS B 245 ? 0.2864 0.2951 0.4274 -0.0797 0.0844  -0.0162 226 LYS D NZ  
3643 N N   . GLU B 246 ? 0.038  0.038  0.038  0       0       0       227 GLU D N   
3644 C CA  . GLU B 246 ? 0.038  0.038  0.038  0       0       0       227 GLU D CA  
3645 C C   . GLU B 246 ? 0.0656 0.0656 0.0656 0       0       0       227 GLU D C   
3646 O O   . GLU B 246 ? 0.038  0.038  0.038  0       0       0       227 GLU D O   
3647 C CB  . GLU B 246 ? 0.0566 0.0566 0.0566 0       0       0       227 GLU D CB  
3648 C CG  . GLU B 246 ? 0.1106 0.1106 0.1106 0       0       0       227 GLU D CG  
3649 C CD  . GLU B 246 ? 0.1453 0.2168 0.2172 -0.0649 0.065   -0.11   227 GLU D CD  
3650 O OE1 . GLU B 246 ? 0.1594 0.1594 0.1594 0       0       0       227 GLU D OE1 
3651 O OE2 . GLU B 246 ? 0.2602 0.2602 0.2602 0       0       0       227 GLU D OE2 
3652 N N   . ALA B 247 ? 0.038  0.038  0.038  0       0       0       228 ALA D N   
3653 C CA  . ALA B 247 ? 0.038  0.038  0.038  0       0       0       228 ALA D CA  
3654 C C   . ALA B 247 ? 0.0745 0.0745 0.0745 0       0       0       228 ALA D C   
3655 O O   . ALA B 247 ? 0.038  0.038  0.038  0       0       0       228 ALA D O   
3656 C CB  . ALA B 247 ? 0.038  0.038  0.038  0       0       0       228 ALA D CB  
3657 N N   . GLY B 248 ? 0.038  0.038  0.038  0       0       0       229 GLY D N   
3658 C CA  . GLY B 248 ? 0.038  0.038  0.038  0       0       0       229 GLY D CA  
3659 C C   . GLY B 248 ? 0.0739 0.0739 0.0739 0       0       0       229 GLY D C   
3660 O O   . GLY B 248 ? 0.038  0.038  0.038  0       0       0       229 GLY D O   
3661 N N   . TYR B 249 ? 0.038  0.038  0.038  0       0       0       230 TYR D N   
3662 C CA  . TYR B 249 ? 0.038  0.038  0.038  0       0       0       230 TYR D CA  
3663 C C   . TYR B 249 ? 0.0666 0.0666 0.0666 0       0       0       230 TYR D C   
3664 O O   . TYR B 249 ? 0.038  0.038  0.038  0       0       0       230 TYR D O   
3665 C CB  . TYR B 249 ? 0.038  0.038  0.038  0       0       0       230 TYR D CB  
3666 C CG  . TYR B 249 ? 0.038  0.038  0.038  0       0       0       230 TYR D CG  
3667 C CD1 . TYR B 249 ? 0.0512 0.0512 0.0512 0       0       0       230 TYR D CD1 
3668 C CD2 . TYR B 249 ? 0.038  0.038  0.038  0       0       0       230 TYR D CD2 
3669 C CE1 . TYR B 249 ? 0.038  0.038  0.038  0       0       0       230 TYR D CE1 
3670 C CE2 . TYR B 249 ? 0.038  0.038  0.038  0       0       0       230 TYR D CE2 
3671 C CZ  . TYR B 249 ? 0.0917 0.0917 0.0917 0       0       0       230 TYR D CZ  
3672 O OH  . TYR B 249 ? 0.038  0.038  0.038  0       0       0       230 TYR D OH  
3673 N N   . THR B 250 ? 0.038  0.038  0.038  0       0       0       231 THR D N   
3674 C CA  . THR B 250 ? 0.038  0.038  0.038  0       0       0       231 THR D CA  
3675 C C   . THR B 250 ? 0.0678 0.0678 0.0678 0       0       0       231 THR D C   
3676 O O   . THR B 250 ? 0.0436 0.0436 0.0436 0       0       0       231 THR D O   
3677 C CB  . THR B 250 ? 0.0906 0.0906 0.0906 0       0       0       231 THR D CB  
3678 O OG1 . THR B 250 ? 0.038  0.038  0.038  0       0       0       231 THR D OG1 
3679 C CG2 . THR B 250 ? 0.1001 0.1001 0.1001 0       0       0       231 THR D CG2 
3680 N N   . ILE B 251 ? 0.038  0.038  0.038  0       0       0       232 ILE D N   
3681 C CA  . ILE B 251 ? 0.038  0.038  0.038  0       0       0       232 ILE D CA  
3682 C C   . ILE B 251 ? 0.0746 0.0746 0.0746 0       0       0       232 ILE D C   
3683 O O   . ILE B 251 ? 0.038  0.038  0.038  0       0       0       232 ILE D O   
3684 C CB  . ILE B 251 ? 0.0747 0.0747 0.0747 0       0       0       232 ILE D CB  
3685 C CG1 . ILE B 251 ? 0.0793 0.0793 0.0793 0       0       0       232 ILE D CG1 
3686 C CG2 . ILE B 251 ? 0.084  0.084  0.084  0       0       0       232 ILE D CG2 
3687 C CD1 . ILE B 251 ? 0.0879 0.0879 0.0879 0       0       0       232 ILE D CD1 
3688 N N   . GLU B 252 ? 0.038  0.038  0.038  0       0       0       233 GLU D N   
3689 C CA  . GLU B 252 ? 0.038  0.038  0.038  0       0       0       233 GLU D CA  
3690 C C   . GLU B 252 ? 0.0748 0.0748 0.0748 0       0       0       233 GLU D C   
3691 O O   . GLU B 252 ? 0.038  0.038  0.038  0       0       0       233 GLU D O   
3692 C CB  . GLU B 252 ? 0.0609 0.0609 0.0609 0       0       0       233 GLU D CB  
3693 C CG  . GLU B 252 ? 0.0714 0.0714 0.0714 0       0       0       233 GLU D CG  
3694 C CD  . GLU B 252 ? 0.37   0.3514 0.4671 -0.0976 0.203   0.0071  233 GLU D CD  
3695 O OE1 . GLU B 252 ? 0.3967 0.2805 0.4506 -0.0456 0.1601  -0.0493 233 GLU D OE1 
3696 O OE2 . GLU B 252 ? 0.4999 0.469  0.5805 -0.0743 0.1937  0.0207  233 GLU D OE2 
3697 N N   . TRP B 253 ? 0.0739 0.0739 0.0739 0       0       0       234 TRP D N   
3698 C CA  . TRP B 253 ? 0.1343 0.1343 0.1343 0       0       0       234 TRP D CA  
3699 C C   . TRP B 253 ? 0.0859 0.0859 0.0859 0       0       0       234 TRP D C   
3700 O O   . TRP B 253 ? 0.038  0.038  0.038  0       0       0       234 TRP D O   
3701 C CB  . TRP B 253 ? 0.189  0.189  0.189  0       0       0       234 TRP D CB  
3702 C CG  . TRP B 253 ? 0.1721 0.1721 0.1721 0       0       0       234 TRP D CG  
3703 C CD1 . TRP B 253 ? 0.1321 0.1321 0.1321 0       0       0       234 TRP D CD1 
3704 C CD2 . TRP B 253 ? 0.1658 0.1658 0.1658 0       0       0       234 TRP D CD2 
3705 N NE1 . TRP B 253 ? 0.13   0.13   0.13   0       0       0       234 TRP D NE1 
3706 C CE2 . TRP B 253 ? 0.112  0.112  0.112  0       0       0       234 TRP D CE2 
3707 C CE3 . TRP B 253 ? 0.1447 0.1447 0.1447 0       0       0       234 TRP D CE3 
3708 C CZ2 . TRP B 253 ? 0.114  0.114  0.114  0       0       0       234 TRP D CZ2 
3709 C CZ3 . TRP B 253 ? 0.1222 0.1222 0.1222 0       0       0       234 TRP D CZ3 
3710 C CH2 . TRP B 253 ? 0.112  0.112  0.112  0       0       0       234 TRP D CH2 
3711 N N   . PHE B 254 ? 0.038  0.038  0.038  0       0       0       235 PHE D N   
3712 C CA  . PHE B 254 ? 0.038  0.038  0.038  0       0       0       235 PHE D CA  
3713 C C   . PHE B 254 ? 0.0549 0.0549 0.0549 0       0       0       235 PHE D C   
3714 O O   . PHE B 254 ? 0.038  0.038  0.038  0       0       0       235 PHE D O   
3715 C CB  . PHE B 254 ? 0.038  0.038  0.038  0       0       0       235 PHE D CB  
3716 C CG  . PHE B 254 ? 0.038  0.038  0.038  0       0       0       235 PHE D CG  
3717 C CD1 . PHE B 254 ? 0.0697 0.0697 0.0697 0       0       0       235 PHE D CD1 
3718 C CD2 . PHE B 254 ? 0.0434 0.0434 0.0434 0       0       0       235 PHE D CD2 
3719 C CE1 . PHE B 254 ? 0.0728 0.0728 0.0728 0       0       0       235 PHE D CE1 
3720 C CE2 . PHE B 254 ? 0.0687 0.0687 0.0687 0       0       0       235 PHE D CE2 
3721 C CZ  . PHE B 254 ? 0.038  0.038  0.038  0       0       0       235 PHE D CZ  
3722 N N   . GLU B 255 ? 0.038  0.038  0.038  0       0       0       236 GLU D N   
3723 C CA  . GLU B 255 ? 0.038  0.038  0.038  0       0       0       236 GLU D CA  
3724 C C   . GLU B 255 ? 0.0671 0.0671 0.0671 0       0       0       236 GLU D C   
3725 O O   . GLU B 255 ? 0.038  0.038  0.038  0       0       0       236 GLU D O   
3726 C CB  . GLU B 255 ? 0.0501 0.0501 0.0501 0       0       0       236 GLU D CB  
3727 C CG  . GLU B 255 ? 0.0938 0.0938 0.0938 0       0       0       236 GLU D CG  
3728 C CD  . GLU B 255 ? 0.2974 0.2323 0.427  -0.1943 -0.1834 0.0503  236 GLU D CD  
3729 O OE1 . GLU B 255 ? 0.4378 0.4028 0.5555 -0.1982 -0.1697 0.0695  236 GLU D OE1 
3730 O OE2 . GLU B 255 ? 0.3944 0.3068 0.4554 -0.1123 -0.1644 0.054   236 GLU D OE2 
3731 N N   . VAL B 256 ? 0.038  0.038  0.038  0       0       0       237 VAL D N   
3732 C CA  . VAL B 256 ? 0.038  0.038  0.038  0       0       0       237 VAL D CA  
3733 C C   . VAL B 256 ? 0.0712 0.0712 0.0712 0       0       0       237 VAL D C   
3734 O O   . VAL B 256 ? 0.038  0.038  0.038  0       0       0       237 VAL D O   
3735 C CB  . VAL B 256 ? 0.0884 0.0884 0.0884 0       0       0       237 VAL D CB  
3736 C CG1 . VAL B 256 ? 0.0826 0.0826 0.0826 0       0       0       237 VAL D CG1 
3737 C CG2 . VAL B 256 ? 0.0843 0.0843 0.0843 0       0       0       237 VAL D CG2 
3738 N N   . ILE B 257 ? 0.038  0.038  0.038  0       0       0       238 ILE D N   
3739 C CA  . ILE B 257 ? 0.0525 0.0525 0.0525 0       0       0       238 ILE D CA  
3740 C C   . ILE B 257 ? 0.0926 0.0926 0.0926 0       0       0       238 ILE D C   
3741 O O   . ILE B 257 ? 0.0405 0.0405 0.0405 0       0       0       238 ILE D O   
3742 C CB  . ILE B 257 ? 0.1086 0.1086 0.1086 0       0       0       238 ILE D CB  
3743 C CG1 . ILE B 257 ? 0.1114 0.1114 0.1114 0       0       0       238 ILE D CG1 
3744 C CG2 . ILE B 257 ? 0.0933 0.0933 0.0933 0       0       0       238 ILE D CG2 
3745 C CD1 . ILE B 257 ? 0.1478 0.1028 0.2157 0.0084  -0.073  -0.0131 238 ILE D CD1 
3746 N N   A SER B 258 ? 0.0574 0.0574 0.0574 0       0       0       239 SER D N   
3747 N N   B SER B 258 ? 0.0658 0.0658 0.0658 0       0       0       239 SER D N   
3748 C CA  A SER B 258 ? 0.0644 0.0644 0.0644 0       0       0       239 SER D CA  
3749 C CA  B SER B 258 ? 0.0771 0.0771 0.0771 0       0       0       239 SER D CA  
3750 C C   A SER B 258 ? 0.0921 0.0921 0.0921 0       0       0       239 SER D C   
3751 C C   B SER B 258 ? 0.0945 0.0945 0.0945 0       0       0       239 SER D C   
3752 O O   A SER B 258 ? 0.0947 0.0947 0.0947 0       0       0       239 SER D O   
3753 O O   B SER B 258 ? 0.0983 0.0983 0.0983 0       0       0       239 SER D O   
3754 C CB  A SER B 258 ? 0.0952 0.0952 0.0952 0       0       0       239 SER D CB  
3755 C CB  B SER B 258 ? 0.1005 0.1005 0.1005 0       0       0       239 SER D CB  
3756 O OG  A SER B 258 ? 0.0409 0.0409 0.0409 0       0       0       239 SER D OG  
3757 O OG  B SER B 258 ? 0.0608 0.0566 0.0691 -0.0001 -0.0073 0.0002  239 SER D OG  
3758 N N   . GLN B 259 ? 0.0829 0.0829 0.0829 0       0       0       240 GLN D N   
3759 C CA  . GLN B 259 ? 0.0849 0.0849 0.0849 0       0       0       240 GLN D CA  
3760 C C   . GLN B 259 ? 0.098  0.098  0.098  0       0       0       240 GLN D C   
3761 O O   . GLN B 259 ? 0.092  0.092  0.092  0       0       0       240 GLN D O   
3762 C CB  . GLN B 259 ? 0.1146 0.1146 0.1146 0       0       0       240 GLN D CB  
3763 C CG  . GLN B 259 ? 0.1323 0.1483 0.3383 0.037   -0.084  -0.104  240 GLN D CG  
3764 C CD  . GLN B 259 ? 0.2305 0.2361 0.4954 0.0093  -0.1079 -0.1866 240 GLN D CD  
3765 O OE1 . GLN B 259 ? 0.2304 0.2773 0.4936 0.0441  -0.0876 -0.1457 240 GLN D OE1 
3766 N NE2 . GLN B 259 ? 0.154  0.2144 0.4059 0.0304  -0.0579 -0.139  240 GLN D NE2 
3767 N N   . SER B 260 ? 0.0502 0.0502 0.0502 0       0       0       241 SER D N   
3768 C CA  . SER B 260 ? 0.0464 0.0464 0.0464 0       0       0       241 SER D CA  
3769 C C   . SER B 260 ? 0.0783 0.0783 0.0783 0       0       0       241 SER D C   
3770 O O   . SER B 260 ? 0.038  0.038  0.038  0       0       0       241 SER D O   
3771 C CB  . SER B 260 ? 0.0939 0.0939 0.0939 0       0       0       241 SER D CB  
3772 O OG  . SER B 260 ? 0.0978 0.0978 0.0978 0       0       0       241 SER D OG  
3773 N N   . TYR B 261 ? 0.038  0.038  0.038  0       0       0       242 TYR D N   
3774 C CA  . TYR B 261 ? 0.038  0.038  0.038  0       0       0       242 TYR D CA  
3775 C C   . TYR B 261 ? 0.0691 0.0691 0.0691 0       0       0       242 TYR D C   
3776 O O   . TYR B 261 ? 0.0567 0.0567 0.0567 0       0       0       242 TYR D O   
3777 C CB  . TYR B 261 ? 0.038  0.038  0.038  0       0       0       242 TYR D CB  
3778 C CG  . TYR B 261 ? 0.038  0.038  0.038  0       0       0       242 TYR D CG  
3779 C CD1 . TYR B 261 ? 0.0458 0.0458 0.0458 0       0       0       242 TYR D CD1 
3780 C CD2 . TYR B 261 ? 0.038  0.038  0.038  0       0       0       242 TYR D CD2 
3781 C CE1 . TYR B 261 ? 0.0404 0.0404 0.0404 0       0       0       242 TYR D CE1 
3782 C CE2 . TYR B 261 ? 0.038  0.038  0.038  0       0       0       242 TYR D CE2 
3783 C CZ  . TYR B 261 ? 0.0534 0.0534 0.0534 0       0       0       242 TYR D CZ  
3784 O OH  . TYR B 261 ? 0.038  0.038  0.038  0       0       0       242 TYR D OH  
3785 N N   . SER B 262 ? 0.038  0.038  0.038  0       0       0       243 SER D N   
3786 C CA  . SER B 262 ? 0.0388 0.0525 0.0744 -0.0034 0.0054  -0.023  243 SER D CA  
3787 C C   . SER B 262 ? 0.0778 0.0835 0.095  -0.0018 0.0031  -0.0105 243 SER D C   
3788 O O   . SER B 262 ? 0.038  0.038  0.038  0       0       0       243 SER D O   
3789 C CB  . SER B 262 ? 0.0702 0.1047 0.1505 -0.0123 0.0182  -0.0568 243 SER D CB  
3790 O OG  . SER B 262 ? 0.0742 0.1416 0.2114 -0.0196 0.0275  -0.1018 243 SER D OG  
3791 N N   . SER B 263 ? 0.0556 0.0668 0.0924 -0.0041 0.0071  -0.0218 244 SER D N   
3792 C CA  . SER B 263 ? 0.0616 0.0672 0.0833 -0.0026 0.0048  -0.0123 244 SER D CA  
3793 C C   . SER B 263 ? 0.0987 0.1074 0.1355 -0.0063 0.0116  -0.0219 244 SER D C   
3794 O O   . SER B 263 ? 0.0929 0.0958 0.1076 -0.0026 0.005   -0.0084 244 SER D O   
3795 C CB  . SER B 263 ? 0.1105 0.1286 0.1857 -0.009  0.0171  -0.0414 244 SER D CB  
3796 O OG  . SER B 263 ? 0.1079 0.1745 0.3804 -0.0439 0.0801  -0.1613 244 SER D OG  
3797 N N   . THR B 264 ? 0.0678 0.0859 0.1404 -0.0157 0.0273  -0.0471 245 THR D N   
3798 C CA  . THR B 264 ? 0.0952 0.1128 0.1823 -0.0245 0.0424  -0.0603 245 THR D CA  
3799 C C   . THR B 264 ? 0.1195 0.1398 0.215  -0.0274 0.0467  -0.0671 245 THR D C   
3800 O O   . THR B 264 ? 0.1289 0.1435 0.2284 -0.0345 0.0597  -0.0736 245 THR D O   
3801 C CB  . THR B 264 ? 0.1341 0.1764 0.3361 -0.0668 0.1108  -0.1513 245 THR D CB  
3802 O OG1 . THR B 264 ? 0.1466 0.19   0.295  -0.0474 0.0737  -0.1149 245 THR D OG1 
3803 C CG2 . THR B 264 ? 0.1451 0.1954 0.3965 -0.0814 0.1368  -0.1854 245 THR D CG2 
3804 N N   . MET B 265 ? 0.1419 0.1471 0.1606 -0.0043 0.0071  -0.0126 246 MET D N   
3805 C CA  . MET B 265 ? 0.1416 0.1416 0.1416 0       0       0       246 MET D CA  
3806 C C   . MET B 265 ? 0.0994 0.0994 0.0994 0       0       0       246 MET D C   
3807 O O   . MET B 265 ? 0.038  0.038  0.038  0       0       0       246 MET D O   
3808 C CB  . MET B 265 ? 0.1271 0.1444 0.1737 -0.0104 0.0158  -0.0337 246 MET D CB  
3809 C CG  . MET B 265 ? 0.1339 0.1912 0.2825 -0.0443 0.0645  -0.1185 246 MET D CG  
3810 S SD  . MET B 265 ? 0.1593 0.2638 0.3714 -0.0611 0.0823  -0.1785 246 MET D SD  
3811 C CE  . MET B 265 ? 0.1326 0.2262 0.3038 -0.0577 0.0739  -0.1551 246 MET D CE  
3812 N N   . ALA B 266 ? 0.038  0.038  0.038  0       0       0       247 ALA D N   
3813 C CA  . ALA B 266 ? 0.038  0.038  0.038  0       0       0       247 ALA D CA  
3814 C C   . ALA B 266 ? 0.0675 0.0675 0.0675 0       0       0       247 ALA D C   
3815 O O   . ALA B 266 ? 0.038  0.038  0.038  0       0       0       247 ALA D O   
3816 C CB  . ALA B 266 ? 0.038  0.038  0.038  0       0       0       247 ALA D CB  
3817 N N   . ASN B 267 ? 0.038  0.038  0.038  0       0       0       248 ASN D N   
3818 C CA  . ASN B 267 ? 0.038  0.038  0.038  0       0       0       248 ASN D CA  
3819 C C   . ASN B 267 ? 0.0662 0.0662 0.0662 0       0       0       248 ASN D C   
3820 O O   . ASN B 267 ? 0.038  0.038  0.038  0       0       0       248 ASN D O   
3821 C CB  . ASN B 267 ? 0.0662 0.0662 0.0662 0       0       0       248 ASN D CB  
3822 C CG  . ASN B 267 ? 0.0594 0.0594 0.0594 0       0       0       248 ASN D CG  
3823 O OD1 . ASN B 267 ? 0.038  0.038  0.038  0       0       0       248 ASN D OD1 
3824 N ND2 . ASN B 267 ? 0.0847 0.0847 0.0847 0       0       0       248 ASN D ND2 
3825 N N   . ASN B 268 ? 0.038  0.038  0.038  0       0       0       249 ASN D N   
3826 C CA  . ASN B 268 ? 0.038  0.038  0.038  0       0       0       249 ASN D CA  
3827 C C   . ASN B 268 ? 0.0842 0.0842 0.0842 0       0       0       249 ASN D C   
3828 O O   . ASN B 268 ? 0.038  0.038  0.038  0       0       0       249 ASN D O   
3829 C CB  . ASN B 268 ? 0.038  0.038  0.038  0       0       0       249 ASN D CB  
3830 C CG  . ASN B 268 ? 0.0649 0.0649 0.0649 0       0       0       249 ASN D CG  
3831 O OD1 . ASN B 268 ? 0.038  0.038  0.038  0       0       0       249 ASN D OD1 
3832 N ND2 . ASN B 268 ? 0.038  0.038  0.038  0       0       0       249 ASN D ND2 
3833 N N   . GLU B 269 ? 0.038  0.038  0.038  0       0       0       250 GLU D N   
3834 C CA  . GLU B 269 ? 0.0425 0.0425 0.0425 0       0       0       250 GLU D CA  
3835 C C   . GLU B 269 ? 0.0905 0.0905 0.0905 0       0       0       250 GLU D C   
3836 O O   . GLU B 269 ? 0.0852 0.0852 0.0852 0       0       0       250 GLU D O   
3837 C CB  . GLU B 269 ? 0.0713 0.0713 0.0713 0       0       0       250 GLU D CB  
3838 C CG  . GLU B 269 ? 0.0585 0.049  0.215  0.0096  -0.0515 -0.0319 250 GLU D CG  
3839 C CD  . GLU B 269 ? 0.5208 0.3626 0.9245 -0.032  -0.1451 -0.1059 250 GLU D CD  
3840 O OE1 . GLU B 269 ? 0.697  0.4942 1.1156 -0.0472 -0.1383 -0.1233 250 GLU D OE1 
3841 O OE2 . GLU B 269 ? 0.6117 0.4512 1.0239 -0.034  -0.1615 -0.0899 250 GLU D OE2 
3842 N N   . GLY B 270 ? 0.038  0.038  0.038  0       0       0       251 GLY D N   
3843 C CA  . GLY B 270 ? 0.038  0.038  0.038  0       0       0       251 GLY D CA  
3844 C C   . GLY B 270 ? 0.0736 0.0736 0.0736 0       0       0       251 GLY D C   
3845 O O   . GLY B 270 ? 0.038  0.038  0.038  0       0       0       251 GLY D O   
3846 N N   . LEU B 271 ? 0.038  0.038  0.038  0       0       0       252 LEU D N   
3847 C CA  . LEU B 271 ? 0.038  0.038  0.038  0       0       0       252 LEU D CA  
3848 C C   . LEU B 271 ? 0.0648 0.0648 0.0648 0       0       0       252 LEU D C   
3849 O O   . LEU B 271 ? 0.038  0.038  0.038  0       0       0       252 LEU D O   
3850 C CB  . LEU B 271 ? 0.05   0.05   0.05   0       0       0       252 LEU D CB  
3851 C CG  . LEU B 271 ? 0.0771 0.0771 0.0771 0       0       0       252 LEU D CG  
3852 C CD1 . LEU B 271 ? 0.0715 0.0715 0.0715 0       0       0       252 LEU D CD1 
3853 C CD2 . LEU B 271 ? 0.0921 0.0921 0.0921 0       0       0       252 LEU D CD2 
3854 N N   . PHE B 272 ? 0.038  0.038  0.038  0       0       0       253 PHE D N   
3855 C CA  . PHE B 272 ? 0.038  0.038  0.038  0       0       0       253 PHE D CA  
3856 C C   . PHE B 272 ? 0.0692 0.0692 0.0692 0       0       0       253 PHE D C   
3857 O O   . PHE B 272 ? 0.038  0.038  0.038  0       0       0       253 PHE D O   
3858 C CB  . PHE B 272 ? 0.038  0.038  0.038  0       0       0       253 PHE D CB  
3859 C CG  . PHE B 272 ? 0.038  0.038  0.038  0       0       0       253 PHE D CG  
3860 C CD1 . PHE B 272 ? 0.038  0.038  0.038  0       0       0       253 PHE D CD1 
3861 C CD2 . PHE B 272 ? 0.038  0.038  0.038  0       0       0       253 PHE D CD2 
3862 C CE1 . PHE B 272 ? 0.038  0.038  0.038  0       0       0       253 PHE D CE1 
3863 C CE2 . PHE B 272 ? 0.0654 0.0654 0.0654 0       0       0       253 PHE D CE2 
3864 C CZ  . PHE B 272 ? 0.038  0.038  0.038  0       0       0       253 PHE D CZ  
3865 N N   . SER B 273 ? 0.038  0.038  0.038  0       0       0       254 SER D N   
3866 C CA  . SER B 273 ? 0.038  0.038  0.038  0       0       0       254 SER D CA  
3867 C C   . SER B 273 ? 0.0662 0.0662 0.0662 0       0       0       254 SER D C   
3868 O O   . SER B 273 ? 0.038  0.038  0.038  0       0       0       254 SER D O   
3869 C CB  . SER B 273 ? 0.1109 0.1109 0.1109 0       0       0       254 SER D CB  
3870 O OG  . SER B 273 ? 0.1131 0.1131 0.1131 0       0       0       254 SER D OG  
3871 N N   . LEU B 274 ? 0.038  0.038  0.038  0       0       0       255 LEU D N   
3872 C CA  . LEU B 274 ? 0.038  0.038  0.038  0       0       0       255 LEU D CA  
3873 C C   . LEU B 274 ? 0.077  0.077  0.077  0       0       0       255 LEU D C   
3874 O O   . LEU B 274 ? 0.038  0.038  0.038  0       0       0       255 LEU D O   
3875 C CB  . LEU B 274 ? 0.038  0.038  0.038  0       0       0       255 LEU D CB  
3876 C CG  . LEU B 274 ? 0.0683 0.0683 0.0683 0       0       0       255 LEU D CG  
3877 C CD1 . LEU B 274 ? 0.0605 0.0605 0.0605 0       0       0       255 LEU D CD1 
3878 C CD2 . LEU B 274 ? 0.0876 0.0876 0.0876 0       0       0       255 LEU D CD2 
3879 N N   . VAL B 275 ? 0.038  0.038  0.038  0       0       0       256 VAL D N   
3880 C CA  . VAL B 275 ? 0.038  0.038  0.038  0       0       0       256 VAL D CA  
3881 C C   . VAL B 275 ? 0.0662 0.0662 0.0662 0       0       0       256 VAL D C   
3882 O O   . VAL B 275 ? 0.038  0.038  0.038  0       0       0       256 VAL D O   
3883 C CB  . VAL B 275 ? 0.046  0.046  0.046  0       0       0       256 VAL D CB  
3884 C CG1 . VAL B 275 ? 0.038  0.038  0.038  0       0       0       256 VAL D CG1 
3885 C CG2 . VAL B 275 ? 0.0382 0.0382 0.0382 0       0       0       256 VAL D CG2 
3886 N N   . ALA B 276 ? 0.038  0.038  0.038  0       0       0       257 ALA D N   
3887 C CA  . ALA B 276 ? 0.038  0.038  0.038  0       0       0       257 ALA D CA  
3888 C C   . ALA B 276 ? 0.0584 0.0584 0.0584 0       0       0       257 ALA D C   
3889 O O   . ALA B 276 ? 0.038  0.038  0.038  0       0       0       257 ALA D O   
3890 C CB  . ALA B 276 ? 0.038  0.038  0.038  0       0       0       257 ALA D CB  
3891 N N   . ARG B 277 ? 0.038  0.038  0.038  0       0       0       258 ARG D N   
3892 C CA  . ARG B 277 ? 0.038  0.038  0.038  0       0       0       258 ARG D CA  
3893 C C   . ARG B 277 ? 0.0622 0.0622 0.0622 0       0       0       258 ARG D C   
3894 O O   . ARG B 277 ? 0.038  0.038  0.038  0       0       0       258 ARG D O   
3895 C CB  . ARG B 277 ? 0.0714 0.0714 0.0714 0       0       0       258 ARG D CB  
3896 C CG  . ARG B 277 ? 0.1213 0.0818 0.1337 -0.0337 0.0647  -0.037  258 ARG D CG  
3897 C CD  . ARG B 277 ? 0.3006 0.1707 0.3491 -0.091  0.2238  -0.0842 258 ARG D CD  
3898 N NE  . ARG B 277 ? 0.3625 0.2928 0.4394 -0.1251 0.3342  -0.0772 258 ARG D NE  
3899 C CZ  . ARG B 277 ? 0.6043 0.5051 0.6698 -0.112  0.384   -0.0652 258 ARG D CZ  
3900 N NH1 . ARG B 277 ? 0.5363 0.3673 0.5865 -0.0803 0.3429  -0.0476 258 ARG D NH1 
3901 N NH2 . ARG B 277 ? 0.4673 0.3341 0.5182 -0.1104 0.4086  -0.086  258 ARG D NH2 
3902 N N   . LYS B 278 ? 0.038  0.038  0.038  0       0       0       259 LYS D N   
3903 C CA  . LYS B 278 ? 0.038  0.038  0.038  0       0       0       259 LYS D CA  
3904 C C   . LYS B 278 ? 0.0817 0.0817 0.0817 0       0       0       259 LYS D C   
3905 O O   . LYS B 278 ? 0.0619 0.0618 0.0622 -0.0005 0.0007  -0.0006 259 LYS D O   
3906 C CB  . LYS B 278 ? 0.0475 0.0475 0.0475 0       0       0       259 LYS D CB  
3907 C CG  . LYS B 278 ? 0.0844 0.0844 0.0844 0       0       0       259 LYS D CG  
3908 C CD  . LYS B 278 ? 0.038  0.038  0.038  0       0       0       259 LYS D CD  
3909 C CE  . LYS B 278 ? 0.1107 0.1341 0.1381 -0.0401 0.0416  -0.0555 259 LYS D CE  
3910 N NZ  . LYS B 278 ? 0.0512 0.0635 0.0647 -0.0184 0.0188  -0.0261 259 LYS D NZ  
3911 N N   . LEU B 279 ? 0.038  0.038  0.038  0       0       0       260 LEU D N   
3912 C CA  . LEU B 279 ? 0.3478 0.333  0.4221 -0.1287 0.1695  -0.16   260 LEU D CA  
3913 C C   . LEU B 279 ? 0.7597 0.9287 1.0102 -0.2776 0.4417  -0.2944 260 LEU D C   
3914 O O   . LEU B 279 ? 0.4428 0.5753 0.6539 -0.2671 0.3712  -0.3204 260 LEU D O   
3915 C CB  . LEU B 279 ? 0.3382 0.3321 0.4154 -0.1326 0.1699  -0.1661 260 LEU D CB  
3916 C CG  . LEU B 279 ? 0.3473 0.3215 0.4258 -0.1351 0.1838  -0.167  260 LEU D CG  
3917 C CD1 . LEU B 279 ? 0.3413 0.3254 0.4227 -0.1384 0.1828  -0.1726 260 LEU D CD1 
3918 C CD2 . LEU B 279 ? 0.3838 0.3154 0.476  -0.152  0.2315  -0.1852 260 LEU D CD2 
# 
