data_9GVW
# 
_entry.id   9GVW 
# 
_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   9GVW         pdb_00009gvw 10.2210/pdb9gvw/pdb 
WWPDB D_1292142045 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-14 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_citation.journal_volume' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9GVW 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-26 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          9GVM 
_pdbx_database_related.content_type   unspecified 
# 
_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   0000-0002-7850-1169 
# 
_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' 31239.545 2   2.1.1.1 ? ? ? 
2 non-polymer syn 4-methoxy-2,3-dimethyl-pyridine    137.179   2   ?       ? ? ? 
3 non-polymer syn S-ADENOSYL-L-HOMOCYSTEINE          384.411   2   ?       ? ? ? 
4 water       nat water                              18.015    464 ?       ? ? ? 
# 
_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
EAAVKEAGYTIEWFEVISQSYSSTMANNEGLFSLVARKL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HNHNHNHNHNHNAAAENLYFQSGFTSKDTYLSHFNPRDYLEKYYKFGSRHSAESQILKHLLKNLFKIFCLDGVKGDLLID
IGSGPTIYQLLSACESFKEIVVTDYSDQNLQELEKWLKAAPAAFDWSPVVTYVCDLEGNRVKGPEKEEKLRQAVKQVLKC
DVTQSQPLGAVPLPPADCVLSTLCLDAACPDLPTYCRALRNLGSLLKPGGFLVIMDALKSSYYMIGEQKFSSLPLGREAV
EAAVKEAGYTIEWFEVISQSYSSTMANNEGLFSLVARKL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 4-methoxy-2,3-dimethyl-pyridine A1IPO 
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 
# 
_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                   279 
_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 
A1IPO non-polymer         . 4-methoxy-2,3-dimethyl-pyridine ? 'C8 H11 N O'      137.179 
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 ?   ?   ?   A . n 
A 1 2   ASN 2   -17 ?   ?   ?   A . n 
A 1 3   HIS 3   -16 ?   ?   ?   A . n 
A 1 4   ASN 4   -15 ?   ?   ?   A . n 
A 1 5   HIS 5   -14 ?   ?   ?   A . n 
A 1 6   ASN 6   -13 ?   ?   ?   A . n 
A 1 7   HIS 7   -12 ?   ?   ?   A . n 
A 1 8   ASN 8   -11 ?   ?   ?   A . n 
A 1 9   HIS 9   -10 ?   ?   ?   A . n 
A 1 10  ASN 10  -9  ?   ?   ?   A . n 
A 1 11  HIS 11  -8  ?   ?   ?   A . n 
A 1 12  ASN 12  -7  ?   ?   ?   A . n 
A 1 13  ALA 13  -6  ?   ?   ?   A . n 
A 1 14  ALA 14  -5  ?   ?   ?   A . n 
A 1 15  ALA 15  -4  ?   ?   ?   A . n 
A 1 16  GLU 16  -3  ?   ?   ?   A . n 
A 1 17  ASN 17  -2  ?   ?   ?   A . n 
A 1 18  LEU 18  -1  ?   ?   ?   A . n 
A 1 19  TYR 19  0   ?   ?   ?   A . n 
A 1 20  PHE 20  1   ?   ?   ?   A . n 
A 1 21  GLN 21  2   ?   ?   ?   A . n 
A 1 22  SER 22  3   ?   ?   ?   A . n 
A 1 23  GLY 23  4   4   GLY GLY A . n 
A 1 24  PHE 24  5   5   PHE PHE A . n 
A 1 25  THR 25  6   6   THR THR A . n 
A 1 26  SER 26  7   7   SER SER A . n 
A 1 27  LYS 27  8   8   LYS LYS A . n 
A 1 28  ASP 28  9   9   ASP ASP A . n 
A 1 29  THR 29  10  10  THR THR A . n 
A 1 30  TYR 30  11  11  TYR TYR A . n 
A 1 31  LEU 31  12  12  LEU LEU A . n 
A 1 32  SER 32  13  13  SER SER A . n 
A 1 33  HIS 33  14  14  HIS HIS A . n 
A 1 34  PHE 34  15  15  PHE PHE A . n 
A 1 35  ASN 35  16  16  ASN ASN A . n 
A 1 36  PRO 36  17  17  PRO PRO A . n 
A 1 37  ARG 37  18  18  ARG ARG A . n 
A 1 38  ASP 38  19  19  ASP ASP A . n 
A 1 39  TYR 39  20  20  TYR TYR A . n 
A 1 40  LEU 40  21  21  LEU LEU A . n 
A 1 41  GLU 41  22  22  GLU GLU A . n 
A 1 42  LYS 42  23  23  LYS LYS A . n 
A 1 43  TYR 43  24  24  TYR TYR A . n 
A 1 44  TYR 44  25  25  TYR TYR A . n 
A 1 45  LYS 45  26  26  LYS LYS A . n 
A 1 46  PHE 46  27  27  PHE PHE A . n 
A 1 47  GLY 47  28  28  GLY GLY A . n 
A 1 48  SER 48  29  ?   ?   ?   A . n 
A 1 49  ARG 49  30  ?   ?   ?   A . n 
A 1 50  HIS 50  31  ?   ?   ?   A . n 
A 1 51  SER 51  32  32  SER SER A . n 
A 1 52  ALA 52  33  33  ALA ALA A . n 
A 1 53  GLU 53  34  34  GLU GLU A . n 
A 1 54  SER 54  35  35  SER SER A . n 
A 1 55  GLN 55  36  36  GLN GLN A . n 
A 1 56  ILE 56  37  37  ILE ILE A . n 
A 1 57  LEU 57  38  38  LEU LEU A . n 
A 1 58  LYS 58  39  39  LYS LYS A . n 
A 1 59  HIS 59  40  40  HIS HIS A . n 
A 1 60  LEU 60  41  41  LEU LEU A . n 
A 1 61  LEU 61  42  42  LEU LEU A . n 
A 1 62  LYS 62  43  43  LYS LYS A . n 
A 1 63  ASN 63  44  44  ASN ASN A . n 
A 1 64  LEU 64  45  45  LEU LEU A . n 
A 1 65  PHE 65  46  46  PHE PHE A . n 
A 1 66  LYS 66  47  47  LYS LYS A . n 
A 1 67  ILE 67  48  48  ILE ILE A . n 
A 1 68  PHE 68  49  49  PHE PHE A . n 
A 1 69  CYS 69  50  50  CYS CYS A . n 
A 1 70  LEU 70  51  51  LEU LEU A . n 
A 1 71  ASP 71  52  52  ASP ASP A . n 
A 1 72  GLY 72  53  53  GLY GLY A . n 
A 1 73  VAL 73  54  54  VAL VAL A . n 
A 1 74  LYS 74  55  55  LYS LYS A . n 
A 1 75  GLY 75  56  56  GLY GLY A . n 
A 1 76  ASP 76  57  57  ASP ASP A . n 
A 1 77  LEU 77  58  58  LEU LEU A . n 
A 1 78  LEU 78  59  59  LEU LEU A . n 
A 1 79  ILE 79  60  60  ILE ILE A . n 
A 1 80  ASP 80  61  61  ASP ASP A . n 
A 1 81  ILE 81  62  62  ILE ILE A . n 
A 1 82  GLY 82  63  63  GLY GLY A . n 
A 1 83  SER 83  64  64  SER SER A . n 
A 1 84  GLY 84  65  65  GLY GLY A . n 
A 1 85  PRO 85  66  66  PRO PRO A . n 
A 1 86  THR 86  67  67  THR THR A . n 
A 1 87  ILE 87  68  68  ILE ILE A . n 
A 1 88  TYR 88  69  69  TYR TYR A . n 
A 1 89  GLN 89  70  70  GLN GLN A . n 
A 1 90  LEU 90  71  71  LEU LEU A . n 
A 1 91  LEU 91  72  72  LEU LEU A . n 
A 1 92  SER 92  73  73  SER SER A . n 
A 1 93  ALA 93  74  74  ALA ALA A . n 
A 1 94  CYS 94  75  75  CYS CYS A . n 
A 1 95  GLU 95  76  76  GLU GLU A . n 
A 1 96  SER 96  77  77  SER SER A . n 
A 1 97  PHE 97  78  78  PHE PHE A . n 
A 1 98  LYS 98  79  79  LYS LYS A . n 
A 1 99  GLU 99  80  80  GLU GLU A . n 
A 1 100 ILE 100 81  81  ILE ILE A . n 
A 1 101 VAL 101 82  82  VAL VAL A . n 
A 1 102 VAL 102 83  83  VAL VAL A . n 
A 1 103 THR 103 84  84  THR THR A . n 
A 1 104 ASP 104 85  85  ASP ASP A . n 
A 1 105 TYR 105 86  86  TYR TYR A . n 
A 1 106 SER 106 87  87  SER SER A . n 
A 1 107 ASP 107 88  88  ASP ASP A . n 
A 1 108 GLN 108 89  89  GLN GLN A . n 
A 1 109 ASN 109 90  90  ASN ASN A . n 
A 1 110 LEU 110 91  91  LEU LEU A . n 
A 1 111 GLN 111 92  92  GLN GLN A . n 
A 1 112 GLU 112 93  93  GLU GLU A . n 
A 1 113 LEU 113 94  94  LEU LEU A . n 
A 1 114 GLU 114 95  95  GLU GLU A . n 
A 1 115 LYS 115 96  96  LYS LYS A . n 
A 1 116 TRP 116 97  97  TRP TRP A . n 
A 1 117 LEU 117 98  98  LEU LEU A . n 
A 1 118 LYS 118 99  99  LYS LYS A . n 
A 1 119 ALA 119 100 100 ALA ALA A . n 
A 1 120 ALA 120 101 101 ALA ALA A . n 
A 1 121 PRO 121 102 102 PRO PRO A . n 
A 1 122 ALA 122 103 103 ALA ALA A . n 
A 1 123 ALA 123 104 104 ALA ALA A . n 
A 1 124 PHE 124 105 105 PHE PHE A . n 
A 1 125 ASP 125 106 106 ASP ASP A . n 
A 1 126 TRP 126 107 107 TRP TRP A . n 
A 1 127 SER 127 108 108 SER SER A . n 
A 1 128 PRO 128 109 109 PRO PRO A . n 
A 1 129 VAL 129 110 110 VAL VAL A . n 
A 1 130 VAL 130 111 111 VAL VAL A . n 
A 1 131 THR 131 112 112 THR THR A . n 
A 1 132 TYR 132 113 113 TYR TYR A . n 
A 1 133 VAL 133 114 114 VAL VAL A . n 
A 1 134 CYS 134 115 115 CYS CYS A . n 
A 1 135 ASP 135 116 116 ASP ASP A . n 
A 1 136 LEU 136 117 117 LEU LEU A . n 
A 1 137 GLU 137 118 118 GLU GLU A . n 
A 1 138 GLY 138 119 119 GLY GLY A . n 
A 1 139 ASN 139 120 120 ASN ASN A . n 
A 1 140 ARG 140 121 121 ARG ARG A . n 
A 1 141 VAL 141 122 122 VAL VAL A . n 
A 1 142 LYS 142 123 123 LYS LYS A . n 
A 1 143 GLY 143 124 124 GLY GLY A . n 
A 1 144 PRO 144 125 125 PRO PRO A . n 
A 1 145 GLU 145 126 126 GLU GLU A . n 
A 1 146 LYS 146 127 127 LYS LYS A . n 
A 1 147 GLU 147 128 128 GLU GLU A . n 
A 1 148 GLU 148 129 129 GLU GLU A . n 
A 1 149 LYS 149 130 130 LYS LYS A . n 
A 1 150 LEU 150 131 131 LEU LEU A . n 
A 1 151 ARG 151 132 132 ARG ARG A . n 
A 1 152 GLN 152 133 133 GLN GLN A . n 
A 1 153 ALA 153 134 134 ALA ALA A . n 
A 1 154 VAL 154 135 135 VAL VAL A . n 
A 1 155 LYS 155 136 136 LYS LYS A . n 
A 1 156 GLN 156 137 137 GLN GLN A . n 
A 1 157 VAL 157 138 138 VAL VAL A . n 
A 1 158 LEU 158 139 139 LEU LEU A . n 
A 1 159 LYS 159 140 140 LYS LYS A . n 
A 1 160 CYS 160 141 141 CYS CYS A . n 
A 1 161 ASP 161 142 142 ASP ASP A . n 
A 1 162 VAL 162 143 143 VAL VAL A . n 
A 1 163 THR 163 144 144 THR THR A . n 
A 1 164 GLN 164 145 145 GLN GLN A . n 
A 1 165 SER 165 146 146 SER SER A . n 
A 1 166 GLN 166 147 147 GLN GLN A . n 
A 1 167 PRO 167 148 148 PRO PRO A . n 
A 1 168 LEU 168 149 149 LEU LEU A . n 
A 1 169 GLY 169 150 150 GLY GLY A . n 
A 1 170 ALA 170 151 151 ALA ALA A . n 
A 1 171 VAL 171 152 152 VAL VAL A . n 
A 1 172 PRO 172 153 153 PRO PRO A . n 
A 1 173 LEU 173 154 154 LEU LEU A . n 
A 1 174 PRO 174 155 155 PRO PRO A . n 
A 1 175 PRO 175 156 156 PRO PRO A . n 
A 1 176 ALA 176 157 157 ALA ALA A . n 
A 1 177 ASP 177 158 158 ASP ASP A . n 
A 1 178 CYS 178 159 159 CYS CYS A . n 
A 1 179 VAL 179 160 160 VAL VAL A . n 
A 1 180 LEU 180 161 161 LEU LEU A . n 
A 1 181 SER 181 162 162 SER SER A . n 
A 1 182 THR 182 163 163 THR THR A . n 
A 1 183 LEU 183 164 164 LEU LEU A . n 
A 1 184 CYS 184 165 165 CYS CYS A . n 
A 1 185 LEU 185 166 166 LEU LEU A . n 
A 1 186 ASP 186 167 167 ASP ASP A . n 
A 1 187 ALA 187 168 168 ALA ALA A . n 
A 1 188 ALA 188 169 169 ALA ALA A . n 
A 1 189 CYS 189 170 170 CYS CYS A . n 
A 1 190 PRO 190 171 171 PRO PRO A . n 
A 1 191 ASP 191 172 172 ASP ASP A . n 
A 1 192 LEU 192 173 173 LEU LEU A . n 
A 1 193 PRO 193 174 174 PRO PRO A . n 
A 1 194 THR 194 175 175 THR THR A . n 
A 1 195 TYR 195 176 176 TYR TYR A . n 
A 1 196 CYS 196 177 177 CYS CYS A . n 
A 1 197 ARG 197 178 178 ARG ARG A . n 
A 1 198 ALA 198 179 179 ALA ALA A . n 
A 1 199 LEU 199 180 180 LEU LEU A . n 
A 1 200 ARG 200 181 181 ARG ARG A . n 
A 1 201 ASN 201 182 182 ASN ASN A . n 
A 1 202 LEU 202 183 183 LEU LEU A . n 
A 1 203 GLY 203 184 184 GLY GLY A . n 
A 1 204 SER 204 185 185 SER SER A . n 
A 1 205 LEU 205 186 186 LEU LEU A . n 
A 1 206 LEU 206 187 187 LEU LEU A . n 
A 1 207 LYS 207 188 188 LYS LYS A . n 
A 1 208 PRO 208 189 189 PRO PRO A . n 
A 1 209 GLY 209 190 190 GLY GLY A . n 
A 1 210 GLY 210 191 191 GLY GLY A . n 
A 1 211 PHE 211 192 192 PHE PHE A . n 
A 1 212 LEU 212 193 193 LEU LEU A . n 
A 1 213 VAL 213 194 194 VAL VAL A . n 
A 1 214 ILE 214 195 195 ILE ILE A . n 
A 1 215 MET 215 196 196 MET MET A . n 
A 1 216 ASP 216 197 197 ASP ASP A . n 
A 1 217 ALA 217 198 198 ALA ALA A . n 
A 1 218 LEU 218 199 199 LEU LEU A . n 
A 1 219 LYS 219 200 200 LYS LYS A . n 
A 1 220 SER 220 201 201 SER SER A . n 
A 1 221 SER 221 202 202 SER SER A . n 
A 1 222 TYR 222 203 203 TYR TYR A . n 
A 1 223 TYR 223 204 204 TYR TYR A . n 
A 1 224 MET 224 205 205 MET MET A . n 
A 1 225 ILE 225 206 206 ILE ILE A . n 
A 1 226 GLY 226 207 207 GLY GLY A . n 
A 1 227 GLU 227 208 208 GLU GLU A . n 
A 1 228 GLN 228 209 209 GLN GLN A . n 
A 1 229 LYS 229 210 210 LYS LYS A . n 
A 1 230 PHE 230 211 211 PHE PHE A . n 
A 1 231 SER 231 212 212 SER SER A . n 
A 1 232 SER 232 213 213 SER SER A . n 
A 1 233 LEU 233 214 214 LEU LEU A . n 
A 1 234 PRO 234 215 215 PRO PRO A . n 
A 1 235 LEU 235 216 216 LEU LEU A . n 
A 1 236 GLY 236 217 217 GLY GLY A . n 
A 1 237 ARG 237 218 218 ARG ARG A . n 
A 1 238 GLU 238 219 219 GLU GLU A . n 
A 1 239 ALA 239 220 220 ALA ALA A . n 
A 1 240 VAL 240 221 221 VAL VAL A . n 
A 1 241 GLU 241 222 222 GLU GLU A . n 
A 1 242 ALA 242 223 223 ALA ALA A . n 
A 1 243 ALA 243 224 224 ALA ALA A . n 
A 1 244 VAL 244 225 225 VAL VAL A . n 
A 1 245 LYS 245 226 226 LYS LYS A . n 
A 1 246 GLU 246 227 227 GLU GLU A . n 
A 1 247 ALA 247 228 228 ALA ALA A . n 
A 1 248 GLY 248 229 229 GLY GLY A . n 
A 1 249 TYR 249 230 230 TYR TYR A . n 
A 1 250 THR 250 231 231 THR THR A . n 
A 1 251 ILE 251 232 232 ILE ILE A . n 
A 1 252 GLU 252 233 233 GLU GLU A . n 
A 1 253 TRP 253 234 234 TRP TRP A . n 
A 1 254 PHE 254 235 235 PHE PHE A . n 
A 1 255 GLU 255 236 236 GLU GLU A . n 
A 1 256 VAL 256 237 237 VAL VAL A . n 
A 1 257 ILE 257 238 238 ILE ILE A . n 
A 1 258 SER 258 239 239 SER SER A . n 
A 1 259 GLN 259 240 240 GLN GLN A . n 
A 1 260 SER 260 241 241 SER SER A . n 
A 1 261 TYR 261 242 242 TYR TYR A . n 
A 1 262 SER 262 243 243 SER SER A . n 
A 1 263 SER 263 244 244 SER SER A . n 
A 1 264 THR 264 245 245 THR THR A . n 
A 1 265 MET 265 246 246 MET MET A . n 
A 1 266 ALA 266 247 247 ALA ALA A . n 
A 1 267 ASN 267 248 248 ASN ASN A . n 
A 1 268 ASN 268 249 249 ASN ASN A . n 
A 1 269 GLU 269 250 250 GLU GLU A . n 
A 1 270 GLY 270 251 251 GLY GLY A . n 
A 1 271 LEU 271 252 252 LEU LEU A . n 
A 1 272 PHE 272 253 253 PHE PHE A . n 
A 1 273 SER 273 254 254 SER SER A . n 
A 1 274 LEU 274 255 255 LEU LEU A . n 
A 1 275 VAL 275 256 256 VAL VAL A . n 
A 1 276 ALA 276 257 257 ALA ALA A . n 
A 1 277 ARG 277 258 258 ARG ARG A . n 
A 1 278 LYS 278 259 259 LYS LYS A . n 
A 1 279 LEU 279 260 260 LEU LEU A . n 
B 1 1   HIS 1   -18 ?   ?   ?   B . n 
B 1 2   ASN 2   -17 ?   ?   ?   B . n 
B 1 3   HIS 3   -16 ?   ?   ?   B . n 
B 1 4   ASN 4   -15 ?   ?   ?   B . n 
B 1 5   HIS 5   -14 ?   ?   ?   B . n 
B 1 6   ASN 6   -13 ?   ?   ?   B . n 
B 1 7   HIS 7   -12 ?   ?   ?   B . n 
B 1 8   ASN 8   -11 ?   ?   ?   B . n 
B 1 9   HIS 9   -10 ?   ?   ?   B . n 
B 1 10  ASN 10  -9  ?   ?   ?   B . n 
B 1 11  HIS 11  -8  ?   ?   ?   B . n 
B 1 12  ASN 12  -7  ?   ?   ?   B . n 
B 1 13  ALA 13  -6  ?   ?   ?   B . n 
B 1 14  ALA 14  -5  ?   ?   ?   B . n 
B 1 15  ALA 15  -4  ?   ?   ?   B . n 
B 1 16  GLU 16  -3  ?   ?   ?   B . n 
B 1 17  ASN 17  -2  ?   ?   ?   B . n 
B 1 18  LEU 18  -1  ?   ?   ?   B . n 
B 1 19  TYR 19  0   ?   ?   ?   B . n 
B 1 20  PHE 20  1   ?   ?   ?   B . n 
B 1 21  GLN 21  2   ?   ?   ?   B . n 
B 1 22  SER 22  3   ?   ?   ?   B . n 
B 1 23  GLY 23  4   ?   ?   ?   B . n 
B 1 24  PHE 24  5   5   PHE PHE B . n 
B 1 25  THR 25  6   6   THR THR B . n 
B 1 26  SER 26  7   7   SER SER B . n 
B 1 27  LYS 27  8   8   LYS LYS B . n 
B 1 28  ASP 28  9   9   ASP ASP B . n 
B 1 29  THR 29  10  10  THR THR B . n 
B 1 30  TYR 30  11  11  TYR TYR B . n 
B 1 31  LEU 31  12  12  LEU LEU B . n 
B 1 32  SER 32  13  13  SER SER B . n 
B 1 33  HIS 33  14  14  HIS HIS B . n 
B 1 34  PHE 34  15  15  PHE PHE B . n 
B 1 35  ASN 35  16  16  ASN ASN B . n 
B 1 36  PRO 36  17  17  PRO PRO B . n 
B 1 37  ARG 37  18  18  ARG ARG B . n 
B 1 38  ASP 38  19  19  ASP ASP B . n 
B 1 39  TYR 39  20  20  TYR TYR B . n 
B 1 40  LEU 40  21  21  LEU LEU B . n 
B 1 41  GLU 41  22  22  GLU GLU B . n 
B 1 42  LYS 42  23  23  LYS LYS B . n 
B 1 43  TYR 43  24  24  TYR TYR B . n 
B 1 44  TYR 44  25  25  TYR TYR B . n 
B 1 45  LYS 45  26  26  LYS LYS B . n 
B 1 46  PHE 46  27  27  PHE PHE B . n 
B 1 47  GLY 47  28  28  GLY GLY B . n 
B 1 48  SER 48  29  ?   ?   ?   B . n 
B 1 49  ARG 49  30  ?   ?   ?   B . n 
B 1 50  HIS 50  31  31  HIS HIS B . n 
B 1 51  SER 51  32  32  SER SER B . n 
B 1 52  ALA 52  33  33  ALA ALA B . n 
B 1 53  GLU 53  34  34  GLU GLU B . n 
B 1 54  SER 54  35  35  SER SER B . n 
B 1 55  GLN 55  36  36  GLN GLN B . n 
B 1 56  ILE 56  37  37  ILE ILE B . n 
B 1 57  LEU 57  38  38  LEU LEU B . n 
B 1 58  LYS 58  39  39  LYS LYS B . n 
B 1 59  HIS 59  40  40  HIS HIS B . n 
B 1 60  LEU 60  41  41  LEU LEU B . n 
B 1 61  LEU 61  42  42  LEU LEU B . n 
B 1 62  LYS 62  43  43  LYS LYS B . n 
B 1 63  ASN 63  44  44  ASN ASN B . n 
B 1 64  LEU 64  45  45  LEU LEU B . n 
B 1 65  PHE 65  46  46  PHE PHE B . n 
B 1 66  LYS 66  47  47  LYS LYS B . n 
B 1 67  ILE 67  48  48  ILE ILE B . n 
B 1 68  PHE 68  49  49  PHE PHE B . n 
B 1 69  CYS 69  50  50  CYS CYS B . n 
B 1 70  LEU 70  51  51  LEU LEU B . n 
B 1 71  ASP 71  52  ?   ?   ?   B . n 
B 1 72  GLY 72  53  53  GLY GLY B . n 
B 1 73  VAL 73  54  54  VAL VAL B . n 
B 1 74  LYS 74  55  55  LYS LYS B . n 
B 1 75  GLY 75  56  56  GLY GLY B . n 
B 1 76  ASP 76  57  57  ASP ASP B . n 
B 1 77  LEU 77  58  58  LEU LEU B . n 
B 1 78  LEU 78  59  59  LEU LEU B . n 
B 1 79  ILE 79  60  60  ILE ILE B . n 
B 1 80  ASP 80  61  61  ASP ASP B . n 
B 1 81  ILE 81  62  62  ILE ILE B . n 
B 1 82  GLY 82  63  63  GLY GLY B . n 
B 1 83  SER 83  64  64  SER SER B . n 
B 1 84  GLY 84  65  65  GLY GLY B . n 
B 1 85  PRO 85  66  66  PRO PRO B . n 
B 1 86  THR 86  67  67  THR THR B . n 
B 1 87  ILE 87  68  68  ILE ILE B . n 
B 1 88  TYR 88  69  69  TYR TYR B . n 
B 1 89  GLN 89  70  70  GLN GLN B . n 
B 1 90  LEU 90  71  71  LEU LEU B . n 
B 1 91  LEU 91  72  72  LEU LEU B . n 
B 1 92  SER 92  73  73  SER SER B . n 
B 1 93  ALA 93  74  74  ALA ALA B . n 
B 1 94  CYS 94  75  75  CYS CYS B . n 
B 1 95  GLU 95  76  76  GLU GLU B . n 
B 1 96  SER 96  77  77  SER SER B . n 
B 1 97  PHE 97  78  78  PHE PHE B . n 
B 1 98  LYS 98  79  79  LYS LYS B . n 
B 1 99  GLU 99  80  80  GLU GLU B . n 
B 1 100 ILE 100 81  81  ILE ILE B . n 
B 1 101 VAL 101 82  82  VAL VAL B . n 
B 1 102 VAL 102 83  83  VAL VAL B . n 
B 1 103 THR 103 84  84  THR THR B . n 
B 1 104 ASP 104 85  85  ASP ASP B . n 
B 1 105 TYR 105 86  86  TYR TYR B . n 
B 1 106 SER 106 87  87  SER SER B . n 
B 1 107 ASP 107 88  88  ASP ASP B . n 
B 1 108 GLN 108 89  89  GLN GLN B . n 
B 1 109 ASN 109 90  90  ASN ASN B . n 
B 1 110 LEU 110 91  91  LEU LEU B . n 
B 1 111 GLN 111 92  92  GLN GLN B . n 
B 1 112 GLU 112 93  93  GLU GLU B . n 
B 1 113 LEU 113 94  94  LEU LEU B . n 
B 1 114 GLU 114 95  95  GLU GLU B . n 
B 1 115 LYS 115 96  96  LYS LYS B . n 
B 1 116 TRP 116 97  97  TRP TRP B . n 
B 1 117 LEU 117 98  98  LEU LEU B . n 
B 1 118 LYS 118 99  99  LYS LYS B . n 
B 1 119 ALA 119 100 100 ALA ALA B . n 
B 1 120 ALA 120 101 101 ALA ALA B . n 
B 1 121 PRO 121 102 102 PRO PRO B . n 
B 1 122 ALA 122 103 103 ALA ALA B . n 
B 1 123 ALA 123 104 104 ALA ALA B . n 
B 1 124 PHE 124 105 105 PHE PHE B . n 
B 1 125 ASP 125 106 106 ASP ASP B . n 
B 1 126 TRP 126 107 107 TRP TRP B . n 
B 1 127 SER 127 108 108 SER SER B . n 
B 1 128 PRO 128 109 109 PRO PRO B . n 
B 1 129 VAL 129 110 110 VAL VAL B . n 
B 1 130 VAL 130 111 111 VAL VAL B . n 
B 1 131 THR 131 112 112 THR THR B . n 
B 1 132 TYR 132 113 113 TYR TYR B . n 
B 1 133 VAL 133 114 114 VAL VAL B . n 
B 1 134 CYS 134 115 115 CYS CYS B . n 
B 1 135 ASP 135 116 116 ASP ASP B . n 
B 1 136 LEU 136 117 117 LEU LEU B . n 
B 1 137 GLU 137 118 118 GLU GLU B . n 
B 1 138 GLY 138 119 119 GLY GLY B . n 
B 1 139 ASN 139 120 120 ASN ASN B . n 
B 1 140 ARG 140 121 121 ARG ARG B . n 
B 1 141 VAL 141 122 122 VAL VAL B . n 
B 1 142 LYS 142 123 123 LYS LYS B . n 
B 1 143 GLY 143 124 124 GLY GLY B . n 
B 1 144 PRO 144 125 125 PRO PRO B . n 
B 1 145 GLU 145 126 126 GLU GLU B . n 
B 1 146 LYS 146 127 127 LYS LYS B . n 
B 1 147 GLU 147 128 128 GLU GLU B . n 
B 1 148 GLU 148 129 129 GLU GLU B . n 
B 1 149 LYS 149 130 130 LYS LYS B . n 
B 1 150 LEU 150 131 131 LEU LEU B . n 
B 1 151 ARG 151 132 132 ARG ARG B . n 
B 1 152 GLN 152 133 133 GLN GLN B . n 
B 1 153 ALA 153 134 134 ALA ALA B . n 
B 1 154 VAL 154 135 135 VAL VAL B . n 
B 1 155 LYS 155 136 136 LYS LYS B . n 
B 1 156 GLN 156 137 137 GLN GLN B . n 
B 1 157 VAL 157 138 138 VAL VAL B . n 
B 1 158 LEU 158 139 139 LEU LEU B . n 
B 1 159 LYS 159 140 140 LYS LYS B . n 
B 1 160 CYS 160 141 141 CYS CYS B . n 
B 1 161 ASP 161 142 142 ASP ASP B . n 
B 1 162 VAL 162 143 143 VAL VAL B . n 
B 1 163 THR 163 144 144 THR THR B . n 
B 1 164 GLN 164 145 145 GLN GLN B . n 
B 1 165 SER 165 146 146 SER SER B . n 
B 1 166 GLN 166 147 147 GLN GLN B . n 
B 1 167 PRO 167 148 148 PRO PRO B . n 
B 1 168 LEU 168 149 149 LEU LEU B . n 
B 1 169 GLY 169 150 150 GLY GLY B . n 
B 1 170 ALA 170 151 151 ALA ALA B . n 
B 1 171 VAL 171 152 152 VAL VAL B . n 
B 1 172 PRO 172 153 153 PRO PRO B . n 
B 1 173 LEU 173 154 154 LEU LEU B . n 
B 1 174 PRO 174 155 155 PRO PRO B . n 
B 1 175 PRO 175 156 156 PRO PRO B . n 
B 1 176 ALA 176 157 157 ALA ALA B . n 
B 1 177 ASP 177 158 158 ASP ASP B . n 
B 1 178 CYS 178 159 159 CYS CYS B . n 
B 1 179 VAL 179 160 160 VAL VAL B . n 
B 1 180 LEU 180 161 161 LEU LEU B . n 
B 1 181 SER 181 162 162 SER SER B . n 
B 1 182 THR 182 163 163 THR THR B . n 
B 1 183 LEU 183 164 164 LEU LEU B . n 
B 1 184 CYS 184 165 165 CYS CYS B . n 
B 1 185 LEU 185 166 166 LEU LEU B . n 
B 1 186 ASP 186 167 167 ASP ASP B . n 
B 1 187 ALA 187 168 168 ALA ALA B . n 
B 1 188 ALA 188 169 169 ALA ALA B . n 
B 1 189 CYS 189 170 170 CYS CYS B . n 
B 1 190 PRO 190 171 171 PRO PRO B . n 
B 1 191 ASP 191 172 172 ASP ASP B . n 
B 1 192 LEU 192 173 173 LEU LEU B . n 
B 1 193 PRO 193 174 174 PRO PRO B . n 
B 1 194 THR 194 175 175 THR THR B . n 
B 1 195 TYR 195 176 176 TYR TYR B . n 
B 1 196 CYS 196 177 177 CYS CYS B . n 
B 1 197 ARG 197 178 178 ARG ARG B . n 
B 1 198 ALA 198 179 179 ALA ALA B . n 
B 1 199 LEU 199 180 180 LEU LEU B . n 
B 1 200 ARG 200 181 181 ARG ARG B . n 
B 1 201 ASN 201 182 182 ASN ASN B . n 
B 1 202 LEU 202 183 183 LEU LEU B . n 
B 1 203 GLY 203 184 184 GLY GLY B . n 
B 1 204 SER 204 185 185 SER SER B . n 
B 1 205 LEU 205 186 186 LEU LEU B . n 
B 1 206 LEU 206 187 187 LEU LEU B . n 
B 1 207 LYS 207 188 188 LYS LYS B . n 
B 1 208 PRO 208 189 189 PRO PRO B . n 
B 1 209 GLY 209 190 190 GLY GLY B . n 
B 1 210 GLY 210 191 191 GLY GLY B . n 
B 1 211 PHE 211 192 192 PHE PHE B . n 
B 1 212 LEU 212 193 193 LEU LEU B . n 
B 1 213 VAL 213 194 194 VAL VAL B . n 
B 1 214 ILE 214 195 195 ILE ILE B . n 
B 1 215 MET 215 196 196 MET MET B . n 
B 1 216 ASP 216 197 197 ASP ASP B . n 
B 1 217 ALA 217 198 198 ALA ALA B . n 
B 1 218 LEU 218 199 199 LEU LEU B . n 
B 1 219 LYS 219 200 200 LYS LYS B . n 
B 1 220 SER 220 201 201 SER SER B . n 
B 1 221 SER 221 202 202 SER SER B . n 
B 1 222 TYR 222 203 203 TYR TYR B . n 
B 1 223 TYR 223 204 204 TYR TYR B . n 
B 1 224 MET 224 205 205 MET MET B . n 
B 1 225 ILE 225 206 206 ILE ILE B . n 
B 1 226 GLY 226 207 207 GLY GLY B . n 
B 1 227 GLU 227 208 208 GLU GLU B . n 
B 1 228 GLN 228 209 209 GLN GLN B . n 
B 1 229 LYS 229 210 210 LYS LYS B . n 
B 1 230 PHE 230 211 211 PHE PHE B . n 
B 1 231 SER 231 212 212 SER SER B . n 
B 1 232 SER 232 213 213 SER SER B . n 
B 1 233 LEU 233 214 214 LEU LEU B . n 
B 1 234 PRO 234 215 215 PRO PRO B . n 
B 1 235 LEU 235 216 216 LEU LEU B . n 
B 1 236 GLY 236 217 217 GLY GLY B . n 
B 1 237 ARG 237 218 218 ARG ARG B . n 
B 1 238 GLU 238 219 219 GLU GLU B . n 
B 1 239 ALA 239 220 220 ALA ALA B . n 
B 1 240 VAL 240 221 221 VAL VAL B . n 
B 1 241 GLU 241 222 222 GLU GLU B . n 
B 1 242 ALA 242 223 223 ALA ALA B . n 
B 1 243 ALA 243 224 224 ALA ALA B . n 
B 1 244 VAL 244 225 225 VAL VAL B . n 
B 1 245 LYS 245 226 226 LYS LYS B . n 
B 1 246 GLU 246 227 227 GLU GLU B . n 
B 1 247 ALA 247 228 228 ALA ALA B . n 
B 1 248 GLY 248 229 229 GLY GLY B . n 
B 1 249 TYR 249 230 230 TYR TYR B . n 
B 1 250 THR 250 231 231 THR THR B . n 
B 1 251 ILE 251 232 232 ILE ILE B . n 
B 1 252 GLU 252 233 233 GLU GLU B . n 
B 1 253 TRP 253 234 234 TRP TRP B . n 
B 1 254 PHE 254 235 235 PHE PHE B . n 
B 1 255 GLU 255 236 236 GLU GLU B . n 
B 1 256 VAL 256 237 237 VAL VAL B . n 
B 1 257 ILE 257 238 238 ILE ILE B . n 
B 1 258 SER 258 239 239 SER SER B . n 
B 1 259 GLN 259 240 240 GLN GLN B . n 
B 1 260 SER 260 241 241 SER SER B . n 
B 1 261 TYR 261 242 242 TYR TYR B . n 
B 1 262 SER 262 243 243 SER SER B . n 
B 1 263 SER 263 244 244 SER SER B . n 
B 1 264 THR 264 245 245 THR THR B . n 
B 1 265 MET 265 246 246 MET MET B . n 
B 1 266 ALA 266 247 247 ALA ALA B . n 
B 1 267 ASN 267 248 248 ASN ASN B . n 
B 1 268 ASN 268 249 249 ASN ASN B . n 
B 1 269 GLU 269 250 250 GLU GLU B . n 
B 1 270 GLY 270 251 251 GLY GLY B . n 
B 1 271 LEU 271 252 252 LEU LEU B . n 
B 1 272 PHE 272 253 253 PHE PHE B . n 
B 1 273 SER 273 254 254 SER SER B . n 
B 1 274 LEU 274 255 255 LEU LEU B . n 
B 1 275 VAL 275 256 256 VAL VAL B . n 
B 1 276 ALA 276 257 257 ALA ALA B . n 
B 1 277 ARG 277 258 258 ARG ARG B . n 
B 1 278 LYS 278 259 259 LYS LYS B . n 
B 1 279 LEU 279 260 260 LEU LEU B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IPO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IPO 
_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 A1IPO 1   301 301 A1IPO INH A . 
D 3 SAH   1   302 301 SAH   SAH A . 
E 2 A1IPO 1   301 301 A1IPO INH B . 
F 3 SAH   1   302 302 SAH   SAH B . 
G 4 HOH   1   401 135 HOH   HOH A . 
G 4 HOH   2   402 444 HOH   HOH A . 
G 4 HOH   3   403 50  HOH   HOH A . 
G 4 HOH   4   404 473 HOH   HOH A . 
G 4 HOH   5   405 564 HOH   HOH A . 
G 4 HOH   6   406 528 HOH   HOH A . 
G 4 HOH   7   407 403 HOH   HOH A . 
G 4 HOH   8   408 401 HOH   HOH A . 
G 4 HOH   9   409 248 HOH   HOH A . 
G 4 HOH   10  410 128 HOH   HOH A . 
G 4 HOH   11  411 216 HOH   HOH A . 
G 4 HOH   12  412 247 HOH   HOH A . 
G 4 HOH   13  413 171 HOH   HOH A . 
G 4 HOH   14  414 265 HOH   HOH A . 
G 4 HOH   15  415 525 HOH   HOH A . 
G 4 HOH   16  416 404 HOH   HOH A . 
G 4 HOH   17  417 383 HOH   HOH A . 
G 4 HOH   18  418 300 HOH   HOH A . 
G 4 HOH   19  419 238 HOH   HOH A . 
G 4 HOH   20  420 517 HOH   HOH A . 
G 4 HOH   21  421 61  HOH   HOH A . 
G 4 HOH   22  422 307 HOH   HOH A . 
G 4 HOH   23  423 458 HOH   HOH A . 
G 4 HOH   24  424 243 HOH   HOH A . 
G 4 HOH   25  425 197 HOH   HOH A . 
G 4 HOH   26  426 174 HOH   HOH A . 
G 4 HOH   27  427 9   HOH   HOH A . 
G 4 HOH   28  428 402 HOH   HOH A . 
G 4 HOH   29  429 366 HOH   HOH A . 
G 4 HOH   30  430 282 HOH   HOH A . 
G 4 HOH   31  431 35  HOH   HOH A . 
G 4 HOH   32  432 428 HOH   HOH A . 
G 4 HOH   33  433 338 HOH   HOH A . 
G 4 HOH   34  434 400 HOH   HOH A . 
G 4 HOH   35  435 311 HOH   HOH A . 
G 4 HOH   36  436 87  HOH   HOH A . 
G 4 HOH   37  437 80  HOH   HOH A . 
G 4 HOH   38  438 196 HOH   HOH A . 
G 4 HOH   39  439 191 HOH   HOH A . 
G 4 HOH   40  440 330 HOH   HOH A . 
G 4 HOH   41  441 371 HOH   HOH A . 
G 4 HOH   42  442 39  HOH   HOH A . 
G 4 HOH   43  443 297 HOH   HOH A . 
G 4 HOH   44  444 286 HOH   HOH A . 
G 4 HOH   45  445 552 HOH   HOH A . 
G 4 HOH   46  446 231 HOH   HOH A . 
G 4 HOH   47  447 129 HOH   HOH A . 
G 4 HOH   48  448 236 HOH   HOH A . 
G 4 HOH   49  449 79  HOH   HOH A . 
G 4 HOH   50  450 29  HOH   HOH A . 
G 4 HOH   51  451 269 HOH   HOH A . 
G 4 HOH   52  452 318 HOH   HOH A . 
G 4 HOH   53  453 140 HOH   HOH A . 
G 4 HOH   54  454 456 HOH   HOH A . 
G 4 HOH   55  455 467 HOH   HOH A . 
G 4 HOH   56  456 65  HOH   HOH A . 
G 4 HOH   57  457 116 HOH   HOH A . 
G 4 HOH   58  458 385 HOH   HOH A . 
G 4 HOH   59  459 407 HOH   HOH A . 
G 4 HOH   60  460 88  HOH   HOH A . 
G 4 HOH   61  461 5   HOH   HOH A . 
G 4 HOH   62  462 62  HOH   HOH A . 
G 4 HOH   63  463 188 HOH   HOH A . 
G 4 HOH   64  464 7   HOH   HOH A . 
G 4 HOH   65  465 40  HOH   HOH A . 
G 4 HOH   66  466 54  HOH   HOH A . 
G 4 HOH   67  467 23  HOH   HOH A . 
G 4 HOH   68  468 43  HOH   HOH A . 
G 4 HOH   69  469 375 HOH   HOH A . 
G 4 HOH   70  470 235 HOH   HOH A . 
G 4 HOH   71  471 124 HOH   HOH A . 
G 4 HOH   72  472 215 HOH   HOH A . 
G 4 HOH   73  473 252 HOH   HOH A . 
G 4 HOH   74  474 107 HOH   HOH A . 
G 4 HOH   75  475 254 HOH   HOH A . 
G 4 HOH   76  476 21  HOH   HOH A . 
G 4 HOH   77  477 138 HOH   HOH A . 
G 4 HOH   78  478 422 HOH   HOH A . 
G 4 HOH   79  479 73  HOH   HOH A . 
G 4 HOH   80  480 27  HOH   HOH A . 
G 4 HOH   81  481 91  HOH   HOH A . 
G 4 HOH   82  482 221 HOH   HOH A . 
G 4 HOH   83  483 347 HOH   HOH A . 
G 4 HOH   84  484 332 HOH   HOH A . 
G 4 HOH   85  485 526 HOH   HOH A . 
G 4 HOH   86  486 424 HOH   HOH A . 
G 4 HOH   87  487 322 HOH   HOH A . 
G 4 HOH   88  488 195 HOH   HOH A . 
G 4 HOH   89  489 170 HOH   HOH A . 
G 4 HOH   90  490 202 HOH   HOH A . 
G 4 HOH   91  491 548 HOH   HOH A . 
G 4 HOH   92  492 69  HOH   HOH A . 
G 4 HOH   93  493 506 HOH   HOH A . 
G 4 HOH   94  494 234 HOH   HOH A . 
G 4 HOH   95  495 161 HOH   HOH A . 
G 4 HOH   96  496 250 HOH   HOH A . 
G 4 HOH   97  497 271 HOH   HOH A . 
G 4 HOH   98  498 435 HOH   HOH A . 
G 4 HOH   99  499 33  HOH   HOH A . 
G 4 HOH   100 500 310 HOH   HOH A . 
G 4 HOH   101 501 417 HOH   HOH A . 
G 4 HOH   102 502 136 HOH   HOH A . 
G 4 HOH   103 503 75  HOH   HOH A . 
G 4 HOH   104 504 299 HOH   HOH A . 
G 4 HOH   105 505 187 HOH   HOH A . 
G 4 HOH   106 506 71  HOH   HOH A . 
G 4 HOH   107 507 245 HOH   HOH A . 
G 4 HOH   108 508 362 HOH   HOH A . 
G 4 HOH   109 509 295 HOH   HOH A . 
G 4 HOH   110 510 352 HOH   HOH A . 
G 4 HOH   111 511 280 HOH   HOH A . 
G 4 HOH   112 512 259 HOH   HOH A . 
G 4 HOH   113 513 112 HOH   HOH A . 
G 4 HOH   114 514 378 HOH   HOH A . 
G 4 HOH   115 515 562 HOH   HOH A . 
G 4 HOH   116 516 118 HOH   HOH A . 
G 4 HOH   117 517 334 HOH   HOH A . 
G 4 HOH   118 518 16  HOH   HOH A . 
G 4 HOH   119 519 336 HOH   HOH A . 
G 4 HOH   120 520 122 HOH   HOH A . 
G 4 HOH   121 521 52  HOH   HOH A . 
G 4 HOH   122 522 67  HOH   HOH A . 
G 4 HOH   123 523 179 HOH   HOH A . 
G 4 HOH   124 524 76  HOH   HOH A . 
G 4 HOH   125 525 281 HOH   HOH A . 
G 4 HOH   126 526 563 HOH   HOH A . 
G 4 HOH   127 527 426 HOH   HOH A . 
G 4 HOH   128 528 479 HOH   HOH A . 
G 4 HOH   129 529 3   HOH   HOH A . 
G 4 HOH   130 530 538 HOH   HOH A . 
G 4 HOH   131 531 333 HOH   HOH A . 
G 4 HOH   132 532 101 HOH   HOH A . 
G 4 HOH   133 533 154 HOH   HOH A . 
G 4 HOH   134 534 408 HOH   HOH A . 
G 4 HOH   135 535 270 HOH   HOH A . 
G 4 HOH   136 536 484 HOH   HOH A . 
G 4 HOH   137 537 561 HOH   HOH A . 
G 4 HOH   138 538 446 HOH   HOH A . 
G 4 HOH   139 539 512 HOH   HOH A . 
G 4 HOH   140 540 523 HOH   HOH A . 
G 4 HOH   141 541 98  HOH   HOH A . 
G 4 HOH   142 542 214 HOH   HOH A . 
G 4 HOH   143 543 346 HOH   HOH A . 
G 4 HOH   144 544 496 HOH   HOH A . 
G 4 HOH   145 545 263 HOH   HOH A . 
G 4 HOH   146 546 108 HOH   HOH A . 
G 4 HOH   147 547 530 HOH   HOH A . 
G 4 HOH   148 548 536 HOH   HOH A . 
G 4 HOH   149 549 41  HOH   HOH A . 
G 4 HOH   150 550 453 HOH   HOH A . 
G 4 HOH   151 551 329 HOH   HOH A . 
G 4 HOH   152 552 105 HOH   HOH A . 
G 4 HOH   153 553 519 HOH   HOH A . 
G 4 HOH   154 554 85  HOH   HOH A . 
G 4 HOH   155 555 206 HOH   HOH A . 
G 4 HOH   156 556 369 HOH   HOH A . 
G 4 HOH   157 557 356 HOH   HOH A . 
G 4 HOH   158 558 511 HOH   HOH A . 
G 4 HOH   159 559 559 HOH   HOH A . 
G 4 HOH   160 560 48  HOH   HOH A . 
G 4 HOH   161 561 37  HOH   HOH A . 
G 4 HOH   162 562 68  HOH   HOH A . 
G 4 HOH   163 563 194 HOH   HOH A . 
G 4 HOH   164 564 6   HOH   HOH A . 
G 4 HOH   165 565 30  HOH   HOH A . 
G 4 HOH   166 566 317 HOH   HOH A . 
G 4 HOH   167 567 555 HOH   HOH A . 
G 4 HOH   168 568 163 HOH   HOH A . 
G 4 HOH   169 569 15  HOH   HOH A . 
G 4 HOH   170 570 502 HOH   HOH A . 
G 4 HOH   171 571 455 HOH   HOH A . 
G 4 HOH   172 572 354 HOH   HOH A . 
G 4 HOH   173 573 192 HOH   HOH A . 
G 4 HOH   174 574 373 HOH   HOH A . 
G 4 HOH   175 575 438 HOH   HOH A . 
G 4 HOH   176 576 313 HOH   HOH A . 
G 4 HOH   177 577 522 HOH   HOH A . 
G 4 HOH   178 578 513 HOH   HOH A . 
G 4 HOH   179 579 553 HOH   HOH A . 
G 4 HOH   180 580 376 HOH   HOH A . 
G 4 HOH   181 581 374 HOH   HOH A . 
G 4 HOH   182 582 70  HOH   HOH A . 
G 4 HOH   183 583 489 HOH   HOH A . 
G 4 HOH   184 584 209 HOH   HOH A . 
G 4 HOH   185 585 380 HOH   HOH A . 
G 4 HOH   186 586 459 HOH   HOH A . 
G 4 HOH   187 587 169 HOH   HOH A . 
G 4 HOH   188 588 533 HOH   HOH A . 
G 4 HOH   189 589 560 HOH   HOH A . 
G 4 HOH   190 590 226 HOH   HOH A . 
G 4 HOH   191 591 278 HOH   HOH A . 
G 4 HOH   192 592 359 HOH   HOH A . 
G 4 HOH   193 593 543 HOH   HOH A . 
G 4 HOH   194 594 463 HOH   HOH A . 
G 4 HOH   195 595 460 HOH   HOH A . 
G 4 HOH   196 596 532 HOH   HOH A . 
G 4 HOH   197 597 572 HOH   HOH A . 
G 4 HOH   198 598 421 HOH   HOH A . 
G 4 HOH   199 599 474 HOH   HOH A . 
G 4 HOH   200 600 566 HOH   HOH A . 
G 4 HOH   201 601 96  HOH   HOH A . 
G 4 HOH   202 602 390 HOH   HOH A . 
G 4 HOH   203 603 211 HOH   HOH A . 
G 4 HOH   204 604 103 HOH   HOH A . 
G 4 HOH   205 605 396 HOH   HOH A . 
G 4 HOH   206 606 92  HOH   HOH A . 
G 4 HOH   207 607 198 HOH   HOH A . 
G 4 HOH   208 608 351 HOH   HOH A . 
G 4 HOH   209 609 222 HOH   HOH A . 
G 4 HOH   210 610 447 HOH   HOH A . 
G 4 HOH   211 611 130 HOH   HOH A . 
G 4 HOH   212 612 114 HOH   HOH A . 
G 4 HOH   213 613 293 HOH   HOH A . 
G 4 HOH   214 614 126 HOH   HOH A . 
G 4 HOH   215 615 391 HOH   HOH A . 
G 4 HOH   216 616 570 HOH   HOH A . 
G 4 HOH   217 617 384 HOH   HOH A . 
G 4 HOH   218 618 227 HOH   HOH A . 
H 4 HOH   1   401 134 HOH   HOH B . 
H 4 HOH   2   402 539 HOH   HOH B . 
H 4 HOH   3   403 182 HOH   HOH B . 
H 4 HOH   4   404 177 HOH   HOH B . 
H 4 HOH   5   405 430 HOH   HOH B . 
H 4 HOH   6   406 298 HOH   HOH B . 
H 4 HOH   7   407 527 HOH   HOH B . 
H 4 HOH   8   408 514 HOH   HOH B . 
H 4 HOH   9   409 268 HOH   HOH B . 
H 4 HOH   10  410 132 HOH   HOH B . 
H 4 HOH   11  411 296 HOH   HOH B . 
H 4 HOH   12  412 540 HOH   HOH B . 
H 4 HOH   13  413 355 HOH   HOH B . 
H 4 HOH   14  414 93  HOH   HOH B . 
H 4 HOH   15  415 125 HOH   HOH B . 
H 4 HOH   16  416 360 HOH   HOH B . 
H 4 HOH   17  417 516 HOH   HOH B . 
H 4 HOH   18  418 178 HOH   HOH B . 
H 4 HOH   19  419 244 HOH   HOH B . 
H 4 HOH   20  420 508 HOH   HOH B . 
H 4 HOH   21  421 411 HOH   HOH B . 
H 4 HOH   22  422 294 HOH   HOH B . 
H 4 HOH   23  423 551 HOH   HOH B . 
H 4 HOH   24  424 56  HOH   HOH B . 
H 4 HOH   25  425 521 HOH   HOH B . 
H 4 HOH   26  426 279 HOH   HOH B . 
H 4 HOH   27  427 230 HOH   HOH B . 
H 4 HOH   28  428 229 HOH   HOH B . 
H 4 HOH   29  429 207 HOH   HOH B . 
H 4 HOH   30  430 99  HOH   HOH B . 
H 4 HOH   31  431 452 HOH   HOH B . 
H 4 HOH   32  432 13  HOH   HOH B . 
H 4 HOH   33  433 485 HOH   HOH B . 
H 4 HOH   34  434 2   HOH   HOH B . 
H 4 HOH   35  435 319 HOH   HOH B . 
H 4 HOH   36  436 60  HOH   HOH B . 
H 4 HOH   37  437 115 HOH   HOH B . 
H 4 HOH   38  438 77  HOH   HOH B . 
H 4 HOH   39  439 290 HOH   HOH B . 
H 4 HOH   40  440 58  HOH   HOH B . 
H 4 HOH   41  441 156 HOH   HOH B . 
H 4 HOH   42  442 109 HOH   HOH B . 
H 4 HOH   43  443 175 HOH   HOH B . 
H 4 HOH   44  444 111 HOH   HOH B . 
H 4 HOH   45  445 518 HOH   HOH B . 
H 4 HOH   46  446 545 HOH   HOH B . 
H 4 HOH   47  447 151 HOH   HOH B . 
H 4 HOH   48  448 14  HOH   HOH B . 
H 4 HOH   49  449 90  HOH   HOH B . 
H 4 HOH   50  450 18  HOH   HOH B . 
H 4 HOH   51  451 363 HOH   HOH B . 
H 4 HOH   52  452 149 HOH   HOH B . 
H 4 HOH   53  453 168 HOH   HOH B . 
H 4 HOH   54  454 242 HOH   HOH B . 
H 4 HOH   55  455 44  HOH   HOH B . 
H 4 HOH   56  456 113 HOH   HOH B . 
H 4 HOH   57  457 398 HOH   HOH B . 
H 4 HOH   58  458 303 HOH   HOH B . 
H 4 HOH   59  459 64  HOH   HOH B . 
H 4 HOH   60  460 341 HOH   HOH B . 
H 4 HOH   61  461 141 HOH   HOH B . 
H 4 HOH   62  462 497 HOH   HOH B . 
H 4 HOH   63  463 139 HOH   HOH B . 
H 4 HOH   64  464 38  HOH   HOH B . 
H 4 HOH   65  465 102 HOH   HOH B . 
H 4 HOH   66  466 498 HOH   HOH B . 
H 4 HOH   67  467 469 HOH   HOH B . 
H 4 HOH   68  468 370 HOH   HOH B . 
H 4 HOH   69  469 327 HOH   HOH B . 
H 4 HOH   70  470 343 HOH   HOH B . 
H 4 HOH   71  471 239 HOH   HOH B . 
H 4 HOH   72  472 503 HOH   HOH B . 
H 4 HOH   73  473 78  HOH   HOH B . 
H 4 HOH   74  474 10  HOH   HOH B . 
H 4 HOH   75  475 51  HOH   HOH B . 
H 4 HOH   76  476 84  HOH   HOH B . 
H 4 HOH   77  477 387 HOH   HOH B . 
H 4 HOH   78  478 416 HOH   HOH B . 
H 4 HOH   79  479 127 HOH   HOH B . 
H 4 HOH   80  480 57  HOH   HOH B . 
H 4 HOH   81  481 439 HOH   HOH B . 
H 4 HOH   82  482 328 HOH   HOH B . 
H 4 HOH   83  483 431 HOH   HOH B . 
H 4 HOH   84  484 83  HOH   HOH B . 
H 4 HOH   85  485 246 HOH   HOH B . 
H 4 HOH   86  486 529 HOH   HOH B . 
H 4 HOH   87  487 11  HOH   HOH B . 
H 4 HOH   88  488 36  HOH   HOH B . 
H 4 HOH   89  489 104 HOH   HOH B . 
H 4 HOH   90  490 47  HOH   HOH B . 
H 4 HOH   91  491 12  HOH   HOH B . 
H 4 HOH   92  492 208 HOH   HOH B . 
H 4 HOH   93  493 17  HOH   HOH B . 
H 4 HOH   94  494 63  HOH   HOH B . 
H 4 HOH   95  495 233 HOH   HOH B . 
H 4 HOH   96  496 412 HOH   HOH B . 
H 4 HOH   97  497 292 HOH   HOH B . 
H 4 HOH   98  498 466 HOH   HOH B . 
H 4 HOH   99  499 155 HOH   HOH B . 
H 4 HOH   100 500 429 HOH   HOH B . 
H 4 HOH   101 501 26  HOH   HOH B . 
H 4 HOH   102 502 324 HOH   HOH B . 
H 4 HOH   103 503 32  HOH   HOH B . 
H 4 HOH   104 504 86  HOH   HOH B . 
H 4 HOH   105 505 262 HOH   HOH B . 
H 4 HOH   106 506 34  HOH   HOH B . 
H 4 HOH   107 507 164 HOH   HOH B . 
H 4 HOH   108 508 256 HOH   HOH B . 
H 4 HOH   109 509 42  HOH   HOH B . 
H 4 HOH   110 510 158 HOH   HOH B . 
H 4 HOH   111 511 176 HOH   HOH B . 
H 4 HOH   112 512 316 HOH   HOH B . 
H 4 HOH   113 513 59  HOH   HOH B . 
H 4 HOH   114 514 162 HOH   HOH B . 
H 4 HOH   115 515 249 HOH   HOH B . 
H 4 HOH   116 516 314 HOH   HOH B . 
H 4 HOH   117 517 531 HOH   HOH B . 
H 4 HOH   118 518 82  HOH   HOH B . 
H 4 HOH   119 519 89  HOH   HOH B . 
H 4 HOH   120 520 284 HOH   HOH B . 
H 4 HOH   121 521 186 HOH   HOH B . 
H 4 HOH   122 522 219 HOH   HOH B . 
H 4 HOH   123 523 167 HOH   HOH B . 
H 4 HOH   124 524 19  HOH   HOH B . 
H 4 HOH   125 525 348 HOH   HOH B . 
H 4 HOH   126 526 4   HOH   HOH B . 
H 4 HOH   127 527 335 HOH   HOH B . 
H 4 HOH   128 528 490 HOH   HOH B . 
H 4 HOH   129 529 53  HOH   HOH B . 
H 4 HOH   130 530 550 HOH   HOH B . 
H 4 HOH   131 531 331 HOH   HOH B . 
H 4 HOH   132 532 145 HOH   HOH B . 
H 4 HOH   133 533 471 HOH   HOH B . 
H 4 HOH   134 534 253 HOH   HOH B . 
H 4 HOH   135 535 567 HOH   HOH B . 
H 4 HOH   136 536 285 HOH   HOH B . 
H 4 HOH   137 537 153 HOH   HOH B . 
H 4 HOH   138 538 72  HOH   HOH B . 
H 4 HOH   139 539 49  HOH   HOH B . 
H 4 HOH   140 540 205 HOH   HOH B . 
H 4 HOH   141 541 200 HOH   HOH B . 
H 4 HOH   142 542 304 HOH   HOH B . 
H 4 HOH   143 543 173 HOH   HOH B . 
H 4 HOH   144 544 45  HOH   HOH B . 
H 4 HOH   145 545 414 HOH   HOH B . 
H 4 HOH   146 546 1   HOH   HOH B . 
H 4 HOH   147 547 28  HOH   HOH B . 
H 4 HOH   148 548 22  HOH   HOH B . 
H 4 HOH   149 549 306 HOH   HOH B . 
H 4 HOH   150 550 358 HOH   HOH B . 
H 4 HOH   151 551 325 HOH   HOH B . 
H 4 HOH   152 552 475 HOH   HOH B . 
H 4 HOH   153 553 204 HOH   HOH B . 
H 4 HOH   154 554 232 HOH   HOH B . 
H 4 HOH   155 555 147 HOH   HOH B . 
H 4 HOH   156 556 144 HOH   HOH B . 
H 4 HOH   157 557 361 HOH   HOH B . 
H 4 HOH   158 558 510 HOH   HOH B . 
H 4 HOH   159 559 464 HOH   HOH B . 
H 4 HOH   160 560 344 HOH   HOH B . 
H 4 HOH   161 561 544 HOH   HOH B . 
H 4 HOH   162 562 423 HOH   HOH B . 
H 4 HOH   163 563 406 HOH   HOH B . 
H 4 HOH   164 564 507 HOH   HOH B . 
H 4 HOH   165 565 81  HOH   HOH B . 
H 4 HOH   166 566 337 HOH   HOH B . 
H 4 HOH   167 567 159 HOH   HOH B . 
H 4 HOH   168 568 257 HOH   HOH B . 
H 4 HOH   169 569 372 HOH   HOH B . 
H 4 HOH   170 570 189 HOH   HOH B . 
H 4 HOH   171 571 199 HOH   HOH B . 
H 4 HOH   172 572 220 HOH   HOH B . 
H 4 HOH   173 573 152 HOH   HOH B . 
H 4 HOH   174 574 349 HOH   HOH B . 
H 4 HOH   175 575 100 HOH   HOH B . 
H 4 HOH   176 576 55  HOH   HOH B . 
H 4 HOH   177 577 350 HOH   HOH B . 
H 4 HOH   178 578 25  HOH   HOH B . 
H 4 HOH   179 579 20  HOH   HOH B . 
H 4 HOH   180 580 203 HOH   HOH B . 
H 4 HOH   181 581 46  HOH   HOH B . 
H 4 HOH   182 582 74  HOH   HOH B . 
H 4 HOH   183 583 276 HOH   HOH B . 
H 4 HOH   184 584 8   HOH   HOH B . 
H 4 HOH   185 585 172 HOH   HOH B . 
H 4 HOH   186 586 24  HOH   HOH B . 
H 4 HOH   187 587 302 HOH   HOH B . 
H 4 HOH   188 588 451 HOH   HOH B . 
H 4 HOH   189 589 165 HOH   HOH B . 
H 4 HOH   190 590 386 HOH   HOH B . 
H 4 HOH   191 591 504 HOH   HOH B . 
H 4 HOH   192 592 277 HOH   HOH B . 
H 4 HOH   193 593 106 HOH   HOH B . 
H 4 HOH   194 594 94  HOH   HOH B . 
H 4 HOH   195 595 520 HOH   HOH B . 
H 4 HOH   196 596 261 HOH   HOH B . 
H 4 HOH   197 597 31  HOH   HOH B . 
H 4 HOH   198 598 457 HOH   HOH B . 
H 4 HOH   199 599 183 HOH   HOH B . 
H 4 HOH   200 600 157 HOH   HOH B . 
H 4 HOH   201 601 251 HOH   HOH B . 
H 4 HOH   202 602 273 HOH   HOH B . 
H 4 HOH   203 603 541 HOH   HOH B . 
H 4 HOH   204 604 291 HOH   HOH B . 
H 4 HOH   205 605 565 HOH   HOH B . 
H 4 HOH   206 606 185 HOH   HOH B . 
H 4 HOH   207 607 405 HOH   HOH B . 
H 4 HOH   208 608 427 HOH   HOH B . 
H 4 HOH   209 609 272 HOH   HOH B . 
H 4 HOH   210 610 480 HOH   HOH B . 
H 4 HOH   211 611 368 HOH   HOH B . 
H 4 HOH   212 612 524 HOH   HOH B . 
H 4 HOH   213 613 535 HOH   HOH B . 
H 4 HOH   214 614 409 HOH   HOH B . 
H 4 HOH   215 615 143 HOH   HOH B . 
H 4 HOH   216 616 425 HOH   HOH B . 
H 4 HOH   217 617 494 HOH   HOH B . 
H 4 HOH   218 618 241 HOH   HOH B . 
H 4 HOH   219 619 556 HOH   HOH B . 
H 4 HOH   220 620 225 HOH   HOH B . 
H 4 HOH   221 621 301 HOH   HOH B . 
H 4 HOH   222 622 397 HOH   HOH B . 
H 4 HOH   223 623 312 HOH   HOH B . 
H 4 HOH   224 624 399 HOH   HOH B . 
H 4 HOH   225 625 193 HOH   HOH B . 
H 4 HOH   226 626 110 HOH   HOH B . 
H 4 HOH   227 627 571 HOH   HOH B . 
H 4 HOH   228 628 509 HOH   HOH B . 
H 4 HOH   229 629 217 HOH   HOH B . 
H 4 HOH   230 630 395 HOH   HOH B . 
H 4 HOH   231 631 505 HOH   HOH B . 
H 4 HOH   232 632 266 HOH   HOH B . 
H 4 HOH   233 633 393 HOH   HOH B . 
H 4 HOH   234 634 121 HOH   HOH B . 
H 4 HOH   235 635 267 HOH   HOH B . 
H 4 HOH   236 636 419 HOH   HOH B . 
H 4 HOH   237 637 288 HOH   HOH B . 
H 4 HOH   238 638 418 HOH   HOH B . 
H 4 HOH   239 639 123 HOH   HOH B . 
H 4 HOH   240 640 420 HOH   HOH B . 
H 4 HOH   241 641 66  HOH   HOH B . 
H 4 HOH   242 642 181 HOH   HOH B . 
H 4 HOH   243 643 392 HOH   HOH B . 
H 4 HOH   244 644 223 HOH   HOH B . 
H 4 HOH   245 645 210 HOH   HOH B . 
H 4 HOH   246 646 224 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER  ? ? ? '2.11.8 (8-JUN-2022)' 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                     9GVW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.887 
_cell.length_a_esd                 ? 
_cell.length_b                     69.818 
_cell.length_b_esd                 ? 
_cell.length_c                     116.789 
_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                         9GVW 
_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                   9GVW 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.02 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.08 
_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, HANGING 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         2017-08-25 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97625 
_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                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97625 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9GVW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.24 
_reflns.d_resolution_low                               46.3 
_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                                     112304 
_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                           78.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.3 
_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                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.049 
_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                                    1.24 
_reflns_shell.d_res_low                                     1.28 
_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                             2000 
_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                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.86 
_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]                            1.026 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            3.9056 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -4.9316 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               25.22 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.953 
_refine.correlation_coeff_Fo_to_Fc_free          0.954 
_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                                 9GVW 
_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                            1.241 
_refine.ls_d_res_low                             46.31 
_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                     112304 
_refine.ls_number_reflns_R_free                  5598 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    78.4 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1973 
_refine.ls_R_factor_R_free                       0.2108 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1965 
_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   0.057 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.059 
_refine.pdbx_overall_SU_R_Blow_DPI               0.06 
_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             0.058 
_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                        9GVW 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.18 
_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                       1.241 
_refine_hist.d_res_low                        46.31 
_refine_hist.number_atoms_solvent             464 
_refine_hist.number_atoms_total               4502 
_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        3966 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         72 
_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' ? 0.012 ? 4154 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 1.18  ? 5632 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1434 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 698  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 4154 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 530  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 4216 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 4.82  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 15.39 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.241 
_refine_ls_shell.d_res_low                        1.29 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             121 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               14.93 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.3762 
_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                  0.3567 
# 
_struct.entry_id                     9GVW 
_struct.title                        'NNMT-SAH IN COMPLEX WITH 4' 
_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        9GVW 
_struct_keywords.text            'NNMT, SAM, SAH, 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
SSTMANNEGLFSLVARKL
;
_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 9GVW A 22 ? 279 ? P40261 3 ? 260 ? 3 260 
2 1 9GVW B 22 ? 279 ? P40261 3 ? 260 ? 3 260 
# 
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 9GVW HIS A 1   ? UNP P40261 ?   ?   'expression tag'      -18 1  
1 9GVW ASN A 2   ? UNP P40261 ?   ?   'expression tag'      -17 2  
1 9GVW HIS A 3   ? UNP P40261 ?   ?   'expression tag'      -16 3  
1 9GVW ASN A 4   ? UNP P40261 ?   ?   'expression tag'      -15 4  
1 9GVW HIS A 5   ? UNP P40261 ?   ?   'expression tag'      -14 5  
1 9GVW ASN A 6   ? UNP P40261 ?   ?   'expression tag'      -13 6  
1 9GVW HIS A 7   ? UNP P40261 ?   ?   'expression tag'      -12 7  
1 9GVW ASN A 8   ? UNP P40261 ?   ?   'expression tag'      -11 8  
1 9GVW HIS A 9   ? UNP P40261 ?   ?   'expression tag'      -10 9  
1 9GVW ASN A 10  ? UNP P40261 ?   ?   'expression tag'      -9  10 
1 9GVW HIS A 11  ? UNP P40261 ?   ?   'expression tag'      -8  11 
1 9GVW ASN A 12  ? UNP P40261 ?   ?   'expression tag'      -7  12 
1 9GVW ALA A 13  ? UNP P40261 ?   ?   'expression tag'      -6  13 
1 9GVW ALA A 14  ? UNP P40261 ?   ?   'expression tag'      -5  14 
1 9GVW ALA A 15  ? UNP P40261 ?   ?   'expression tag'      -4  15 
1 9GVW GLU A 16  ? UNP P40261 ?   ?   'expression tag'      -3  16 
1 9GVW ASN A 17  ? UNP P40261 ?   ?   'expression tag'      -2  17 
1 9GVW LEU A 18  ? UNP P40261 ?   ?   'expression tag'      -1  18 
1 9GVW TYR A 19  ? UNP P40261 ?   ?   'expression tag'      0   19 
1 9GVW PHE A 20  ? UNP P40261 ?   ?   'expression tag'      1   20 
1 9GVW GLN A 21  ? UNP P40261 ?   ?   'expression tag'      2   21 
1 9GVW ALA A 119 ? UNP P40261 LYS 100 'engineered mutation' 100 22 
1 9GVW ALA A 120 ? UNP P40261 GLU 101 'engineered mutation' 101 23 
1 9GVW ALA A 122 ? UNP P40261 GLU 103 'engineered mutation' 103 24 
2 9GVW HIS B 1   ? UNP P40261 ?   ?   'expression tag'      -18 25 
2 9GVW ASN B 2   ? UNP P40261 ?   ?   'expression tag'      -17 26 
2 9GVW HIS B 3   ? UNP P40261 ?   ?   'expression tag'      -16 27 
2 9GVW ASN B 4   ? UNP P40261 ?   ?   'expression tag'      -15 28 
2 9GVW HIS B 5   ? UNP P40261 ?   ?   'expression tag'      -14 29 
2 9GVW ASN B 6   ? UNP P40261 ?   ?   'expression tag'      -13 30 
2 9GVW HIS B 7   ? UNP P40261 ?   ?   'expression tag'      -12 31 
2 9GVW ASN B 8   ? UNP P40261 ?   ?   'expression tag'      -11 32 
2 9GVW HIS B 9   ? UNP P40261 ?   ?   'expression tag'      -10 33 
2 9GVW ASN B 10  ? UNP P40261 ?   ?   'expression tag'      -9  34 
2 9GVW HIS B 11  ? UNP P40261 ?   ?   'expression tag'      -8  35 
2 9GVW ASN B 12  ? UNP P40261 ?   ?   'expression tag'      -7  36 
2 9GVW ALA B 13  ? UNP P40261 ?   ?   'expression tag'      -6  37 
2 9GVW ALA B 14  ? UNP P40261 ?   ?   'expression tag'      -5  38 
2 9GVW ALA B 15  ? UNP P40261 ?   ?   'expression tag'      -4  39 
2 9GVW GLU B 16  ? UNP P40261 ?   ?   'expression tag'      -3  40 
2 9GVW ASN B 17  ? UNP P40261 ?   ?   'expression tag'      -2  41 
2 9GVW LEU B 18  ? UNP P40261 ?   ?   'expression tag'      -1  42 
2 9GVW TYR B 19  ? UNP P40261 ?   ?   'expression tag'      0   43 
2 9GVW PHE B 20  ? UNP P40261 ?   ?   'expression tag'      1   44 
2 9GVW GLN B 21  ? UNP P40261 ?   ?   'expression tag'      2   45 
2 9GVW ALA B 119 ? UNP P40261 LYS 100 'engineered mutation' 100 46 
2 9GVW ALA B 120 ? UNP P40261 GLU 101 'engineered mutation' 101 47 
2 9GVW ALA B 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 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 'gel filtration' ? 
2 2 'gel filtration' ? 
# 
_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 A 8   HIS A 14  1 ? 7  
HELX_P HELX_P2  AA2 ASN A 35  ? TYR A 44  ? ASN A 16  TYR A 25  1 ? 10 
HELX_P HELX_P3  AA3 ALA A 52  ? LEU A 70  ? ALA A 33  LEU A 51  1 ? 19 
HELX_P HELX_P4  AA4 ILE A 87  ? LEU A 91  ? ILE A 68  LEU A 72  5 ? 5  
HELX_P HELX_P5  AA5 SER A 92  ? GLU A 95  ? SER A 73  GLU A 76  5 ? 4  
HELX_P HELX_P6  AA6 SER A 106 ? LYS A 118 ? SER A 87  LYS A 99  1 ? 13 
HELX_P HELX_P7  AA7 TRP A 126 ? GLU A 137 ? TRP A 107 GLU A 118 1 ? 12 
HELX_P HELX_P8  AA8 LYS A 142 ? ALA A 153 ? LYS A 123 ALA A 134 1 ? 12 
HELX_P HELX_P9  AA9 CYS A 184 ? CYS A 189 ? CYS A 165 CYS A 170 1 ? 6  
HELX_P HELX_P10 AB1 ASP A 191 ? SER A 204 ? ASP A 172 SER A 185 1 ? 14 
HELX_P HELX_P11 AB2 GLY A 236 ? ALA A 247 ? GLY A 217 ALA A 228 1 ? 12 
HELX_P HELX_P12 AB3 LYS B 27  ? PHE B 34  ? LYS B 8   PHE B 15  1 ? 8  
HELX_P HELX_P13 AB4 ASN B 35  ? TYR B 44  ? ASN B 16  TYR B 25  1 ? 10 
HELX_P HELX_P14 AB5 SER B 51  ? CYS B 69  ? SER B 32  CYS B 50  1 ? 19 
HELX_P HELX_P15 AB6 ILE B 87  ? LEU B 91  ? ILE B 68  LEU B 72  5 ? 5  
HELX_P HELX_P16 AB7 SER B 92  ? GLU B 95  ? SER B 73  GLU B 76  5 ? 4  
HELX_P HELX_P17 AB8 SER B 106 ? LYS B 118 ? SER B 87  LYS B 99  1 ? 13 
HELX_P HELX_P18 AB9 TRP B 126 ? GLU B 137 ? TRP B 107 GLU B 118 1 ? 12 
HELX_P HELX_P19 AC1 LYS B 142 ? ALA B 153 ? LYS B 123 ALA B 134 1 ? 12 
HELX_P HELX_P20 AC2 CYS B 184 ? CYS B 189 ? CYS B 165 CYS B 170 1 ? 6  
HELX_P HELX_P21 AC3 ASP B 191 ? SER B 204 ? ASP B 172 SER B 185 1 ? 14 
HELX_P HELX_P22 AC4 GLY B 236 ? ALA B 247 ? GLY B 217 ALA B 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 A 135 LYS A 140 
AA1 2  PHE A 97  ? ASP A 104 ? PHE A 78  ASP A 85  
AA1 3  GLY A 75  ? ASP A 80  ? GLY A 56  ASP A 61  
AA1 4  ALA A 176 ? THR A 182 ? ALA A 157 THR A 163 
AA1 5  LEU A 206 ? ALA A 217 ? LEU A 187 ALA A 198 
AA1 6  LEU A 271 ? LYS A 278 ? LEU A 252 LYS A 259 
AA1 7  TYR A 249 ? ILE A 257 ? TYR A 230 ILE A 238 
AA1 8  TYR B 249 ? ILE B 257 ? TYR B 230 ILE B 238 
AA1 9  LEU B 271 ? LYS B 278 ? LEU B 252 LYS B 259 
AA1 10 LEU B 206 ? ALA B 217 ? LEU B 187 ALA B 198 
AA1 11 ALA B 176 ? THR B 182 ? ALA B 157 THR B 163 
AA1 12 GLY B 75  ? ASP B 80  ? GLY B 56  ASP B 61  
AA1 13 PHE B 97  ? ASP B 104 ? PHE B 78  ASP B 85  
AA1 14 VAL B 154 ? LYS B 159 ? VAL B 135 LYS B 140 
AA2 1  TYR A 222 ? ILE A 225 ? TYR A 203 ILE A 206 
AA2 2  GLN A 228 ? SER A 231 ? GLN A 209 SER A 212 
AA3 1  TYR B 222 ? ILE B 225 ? TYR B 203 ILE B 206 
AA3 2  GLN B 228 ? SER B 231 ? GLN B 209 SER B 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 A 139 N VAL A 102 ? N VAL A 83  
AA1 2  3  O VAL A 101 ? O VAL A 82  N ASP A 80  ? N ASP A 61  
AA1 3  4  N ILE A 79  ? N ILE A 60  O LEU A 180 ? O LEU A 161 
AA1 4  5  N VAL A 179 ? N VAL A 160 O VAL A 213 ? O VAL A 194 
AA1 5  6  N LEU A 212 ? N LEU A 193 O ALA A 276 ? O ALA A 257 
AA1 6  7  O VAL A 275 ? O VAL A 256 N GLU A 252 ? N GLU A 233 
AA1 7  8  N PHE A 254 ? N PHE A 235 O VAL B 256 ? O VAL B 237 
AA1 8  9  N GLU B 252 ? N GLU B 233 O VAL B 275 ? O VAL B 256 
AA1 9  10 O ALA B 276 ? O ALA B 257 N LEU B 212 ? N LEU B 193 
AA1 10 11 O VAL B 213 ? O VAL B 194 N VAL B 179 ? N VAL B 160 
AA1 11 12 O LEU B 180 ? O LEU B 161 N ILE B 79  ? N ILE B 60  
AA1 12 13 N ASP B 80  ? N ASP B 61  O VAL B 101 ? O VAL B 82  
AA1 13 14 N VAL B 102 ? N VAL B 83  O LEU B 158 ? O LEU B 139 
AA2 1  2  N ILE A 225 ? N ILE A 206 O GLN A 228 ? O GLN A 209 
AA3 1  2  N ILE B 225 ? N ILE B 206 O GLN B 228 ? O GLN B 209 
# 
_pdbx_entry_details.entry_id                   9GVW 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 248 ? ? -103.77 40.73 
2 1 ASN B 248 ? ? -104.50 41.64 
# 
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' ? ? 2.8454  24.7007 42.5811 -0.0282 ? -0.0133 ? -0.0036 ? -0.0227 ? -0.0138 ? 0.0163 ? 0.728  ? 0.6654 ? 
0.0138 ? 1.9854 ? -0.1206 ? 0.3454 ? 0.0851 ? 0.1363 ? 0.0403  ? 0.1363 ? -0.0859 ? -0.0092 ? 0.0403  ? -0.0092 ? 0.0007  ? 
2 'X-RAY DIFFRACTION' ? ? 27.5336 47.5271 42.7173 -0.0406 ? -0.0054 ? 0.0136  ? -0.0207 ? -0.0025 ? 0.0105 ? 0.5949 ? 0.141  ? 
0.2326 ? 0.9032 ? -0.0926 ? 0.7665 ? 0.049  ? 0.0454 ? -0.0186 ? 0.0454 ? -0.0085 ? 0.015   ? -0.0186 ? 0.015   ? -0.0405 ? 
# 
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 ? ? ? ? ? ? ? ? ? ? ? '{ A|* }' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '{ B|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A HIS -18 ? A HIS 1  
2  1 Y 1 A ASN -17 ? A ASN 2  
3  1 Y 1 A HIS -16 ? A HIS 3  
4  1 Y 1 A ASN -15 ? A ASN 4  
5  1 Y 1 A HIS -14 ? A HIS 5  
6  1 Y 1 A ASN -13 ? A ASN 6  
7  1 Y 1 A HIS -12 ? A HIS 7  
8  1 Y 1 A ASN -11 ? A ASN 8  
9  1 Y 1 A HIS -10 ? A HIS 9  
10 1 Y 1 A ASN -9  ? A ASN 10 
11 1 Y 1 A HIS -8  ? A HIS 11 
12 1 Y 1 A ASN -7  ? A ASN 12 
13 1 Y 1 A ALA -6  ? A ALA 13 
14 1 Y 1 A ALA -5  ? A ALA 14 
15 1 Y 1 A ALA -4  ? A ALA 15 
16 1 Y 1 A GLU -3  ? A GLU 16 
17 1 Y 1 A ASN -2  ? A ASN 17 
18 1 Y 1 A LEU -1  ? A LEU 18 
19 1 Y 1 A TYR 0   ? A TYR 19 
20 1 Y 1 A PHE 1   ? A PHE 20 
21 1 Y 1 A GLN 2   ? A GLN 21 
22 1 Y 1 A SER 3   ? A SER 22 
23 1 Y 1 A SER 29  ? A SER 48 
24 1 Y 1 A ARG 30  ? A ARG 49 
25 1 Y 1 A HIS 31  ? A HIS 50 
26 1 Y 1 B HIS -18 ? B HIS 1  
27 1 Y 1 B ASN -17 ? B ASN 2  
28 1 Y 1 B HIS -16 ? B HIS 3  
29 1 Y 1 B ASN -15 ? B ASN 4  
30 1 Y 1 B HIS -14 ? B HIS 5  
31 1 Y 1 B ASN -13 ? B ASN 6  
32 1 Y 1 B HIS -12 ? B HIS 7  
33 1 Y 1 B ASN -11 ? B ASN 8  
34 1 Y 1 B HIS -10 ? B HIS 9  
35 1 Y 1 B ASN -9  ? B ASN 10 
36 1 Y 1 B HIS -8  ? B HIS 11 
37 1 Y 1 B ASN -7  ? B ASN 12 
38 1 Y 1 B ALA -6  ? B ALA 13 
39 1 Y 1 B ALA -5  ? B ALA 14 
40 1 Y 1 B ALA -4  ? B ALA 15 
41 1 Y 1 B GLU -3  ? B GLU 16 
42 1 Y 1 B ASN -2  ? B ASN 17 
43 1 Y 1 B LEU -1  ? B LEU 18 
44 1 Y 1 B TYR 0   ? B TYR 19 
45 1 Y 1 B PHE 1   ? B PHE 20 
46 1 Y 1 B GLN 2   ? B GLN 21 
47 1 Y 1 B SER 3   ? B SER 22 
48 1 Y 1 B GLY 4   ? B GLY 23 
49 1 Y 1 B SER 29  ? B SER 48 
50 1 Y 1 B ARG 30  ? B ARG 49 
51 1 Y 1 B ASP 52  ? B ASP 71 
# 
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 
A1IPO C1     C N N 1   
A1IPO C3     C Y N 2   
A1IPO N6     N Y N 3   
A1IPO C7     C Y N 4   
A1IPO C8     C N N 5   
A1IPO C9     C Y N 6   
A1IPO C10    C N N 7   
A1IPO O2     O N N 8   
A1IPO C4     C Y N 9   
A1IPO C5     C Y N 10  
A1IPO H1     H N N 11  
A1IPO H2     H N N 12  
A1IPO H3     H N N 13  
A1IPO H4     H N N 14  
A1IPO H5     H N N 15  
A1IPO H6     H N N 16  
A1IPO H7     H N N 17  
A1IPO H8     H N N 18  
A1IPO H9     H N N 19  
A1IPO H10    H N N 20  
A1IPO H11    H N N 21  
ALA   N      N N N 22  
ALA   CA     C N S 23  
ALA   C      C N N 24  
ALA   O      O N N 25  
ALA   CB     C N N 26  
ALA   OXT    O N N 27  
ALA   H      H N N 28  
ALA   H2     H N N 29  
ALA   HA     H N N 30  
ALA   HB1    H N N 31  
ALA   HB2    H N N 32  
ALA   HB3    H N N 33  
ALA   HXT    H N N 34  
ARG   N      N N N 35  
ARG   CA     C N S 36  
ARG   C      C N N 37  
ARG   O      O N N 38  
ARG   CB     C N N 39  
ARG   CG     C N N 40  
ARG   CD     C N N 41  
ARG   NE     N N N 42  
ARG   CZ     C N N 43  
ARG   NH1    N N N 44  
ARG   NH2    N N N 45  
ARG   OXT    O N N 46  
ARG   H      H N N 47  
ARG   H2     H N N 48  
ARG   HA     H N N 49  
ARG   HB2    H N N 50  
ARG   HB3    H N N 51  
ARG   HG2    H N N 52  
ARG   HG3    H N N 53  
ARG   HD2    H N N 54  
ARG   HD3    H N N 55  
ARG   HE     H N N 56  
ARG   HH11   H N N 57  
ARG   HH12   H N N 58  
ARG   HH21   H N N 59  
ARG   HH22   H N N 60  
ARG   HXT    H N N 61  
ASN   N      N N N 62  
ASN   CA     C N S 63  
ASN   C      C N N 64  
ASN   O      O N N 65  
ASN   CB     C N N 66  
ASN   CG     C N N 67  
ASN   OD1    O N N 68  
ASN   ND2    N N N 69  
ASN   OXT    O N N 70  
ASN   H      H N N 71  
ASN   H2     H N N 72  
ASN   HA     H N N 73  
ASN   HB2    H N N 74  
ASN   HB3    H N N 75  
ASN   HD21   H N N 76  
ASN   HD22   H N N 77  
ASN   HXT    H N N 78  
ASP   N      N N N 79  
ASP   CA     C N S 80  
ASP   C      C N N 81  
ASP   O      O N N 82  
ASP   CB     C N N 83  
ASP   CG     C N N 84  
ASP   OD1    O N N 85  
ASP   OD2    O N N 86  
ASP   OXT    O N N 87  
ASP   H      H N N 88  
ASP   H2     H N N 89  
ASP   HA     H N N 90  
ASP   HB2    H N N 91  
ASP   HB3    H N N 92  
ASP   HD2    H N N 93  
ASP   HXT    H N N 94  
CYS   N      N N N 95  
CYS   CA     C N R 96  
CYS   C      C N N 97  
CYS   O      O N N 98  
CYS   CB     C N N 99  
CYS   SG     S N N 100 
CYS   OXT    O N N 101 
CYS   H      H N N 102 
CYS   H2     H N N 103 
CYS   HA     H N N 104 
CYS   HB2    H N N 105 
CYS   HB3    H N N 106 
CYS   HG     H N N 107 
CYS   HXT    H N N 108 
GLN   N      N N N 109 
GLN   CA     C N S 110 
GLN   C      C N N 111 
GLN   O      O N N 112 
GLN   CB     C N N 113 
GLN   CG     C N N 114 
GLN   CD     C N N 115 
GLN   OE1    O N N 116 
GLN   NE2    N N N 117 
GLN   OXT    O N N 118 
GLN   H      H N N 119 
GLN   H2     H N N 120 
GLN   HA     H N N 121 
GLN   HB2    H N N 122 
GLN   HB3    H N N 123 
GLN   HG2    H N N 124 
GLN   HG3    H N N 125 
GLN   HE21   H N N 126 
GLN   HE22   H N N 127 
GLN   HXT    H N N 128 
GLU   N      N N N 129 
GLU   CA     C N S 130 
GLU   C      C N N 131 
GLU   O      O N N 132 
GLU   CB     C N N 133 
GLU   CG     C N N 134 
GLU   CD     C N N 135 
GLU   OE1    O N N 136 
GLU   OE2    O N N 137 
GLU   OXT    O N N 138 
GLU   H      H N N 139 
GLU   H2     H N N 140 
GLU   HA     H N N 141 
GLU   HB2    H N N 142 
GLU   HB3    H N N 143 
GLU   HG2    H N N 144 
GLU   HG3    H N N 145 
GLU   HE2    H N N 146 
GLU   HXT    H N N 147 
GLY   N      N N N 148 
GLY   CA     C N N 149 
GLY   C      C N N 150 
GLY   O      O N N 151 
GLY   OXT    O N N 152 
GLY   H      H N N 153 
GLY   H2     H N N 154 
GLY   HA2    H N N 155 
GLY   HA3    H N N 156 
GLY   HXT    H N N 157 
HIS   N      N N N 158 
HIS   CA     C N S 159 
HIS   C      C N N 160 
HIS   O      O N N 161 
HIS   CB     C N N 162 
HIS   CG     C Y N 163 
HIS   ND1    N Y N 164 
HIS   CD2    C Y N 165 
HIS   CE1    C Y N 166 
HIS   NE2    N Y N 167 
HIS   OXT    O N N 168 
HIS   H      H N N 169 
HIS   H2     H N N 170 
HIS   HA     H N N 171 
HIS   HB2    H N N 172 
HIS   HB3    H N N 173 
HIS   HD1    H N N 174 
HIS   HD2    H N N 175 
HIS   HE1    H N N 176 
HIS   HE2    H N N 177 
HIS   HXT    H N N 178 
HOH   O      O N N 179 
HOH   H1     H N N 180 
HOH   H2     H N N 181 
ILE   N      N N N 182 
ILE   CA     C N S 183 
ILE   C      C N N 184 
ILE   O      O N N 185 
ILE   CB     C N S 186 
ILE   CG1    C N N 187 
ILE   CG2    C N N 188 
ILE   CD1    C N N 189 
ILE   OXT    O N N 190 
ILE   H      H N N 191 
ILE   H2     H N N 192 
ILE   HA     H N N 193 
ILE   HB     H N N 194 
ILE   HG12   H N N 195 
ILE   HG13   H N N 196 
ILE   HG21   H N N 197 
ILE   HG22   H N N 198 
ILE   HG23   H N N 199 
ILE   HD11   H N N 200 
ILE   HD12   H N N 201 
ILE   HD13   H N N 202 
ILE   HXT    H N N 203 
LEU   N      N N N 204 
LEU   CA     C N S 205 
LEU   C      C N N 206 
LEU   O      O N N 207 
LEU   CB     C N N 208 
LEU   CG     C N N 209 
LEU   CD1    C N N 210 
LEU   CD2    C N N 211 
LEU   OXT    O N N 212 
LEU   H      H N N 213 
LEU   H2     H N N 214 
LEU   HA     H N N 215 
LEU   HB2    H N N 216 
LEU   HB3    H N N 217 
LEU   HG     H N N 218 
LEU   HD11   H N N 219 
LEU   HD12   H N N 220 
LEU   HD13   H N N 221 
LEU   HD21   H N N 222 
LEU   HD22   H N N 223 
LEU   HD23   H N N 224 
LEU   HXT    H N N 225 
LYS   N      N N N 226 
LYS   CA     C N S 227 
LYS   C      C N N 228 
LYS   O      O N N 229 
LYS   CB     C N N 230 
LYS   CG     C N N 231 
LYS   CD     C N N 232 
LYS   CE     C N N 233 
LYS   NZ     N N N 234 
LYS   OXT    O N N 235 
LYS   H      H N N 236 
LYS   H2     H N N 237 
LYS   HA     H N N 238 
LYS   HB2    H N N 239 
LYS   HB3    H N N 240 
LYS   HG2    H N N 241 
LYS   HG3    H N N 242 
LYS   HD2    H N N 243 
LYS   HD3    H N N 244 
LYS   HE2    H N N 245 
LYS   HE3    H N N 246 
LYS   HZ1    H N N 247 
LYS   HZ2    H N N 248 
LYS   HZ3    H N N 249 
LYS   HXT    H N N 250 
MET   N      N N N 251 
MET   CA     C N S 252 
MET   C      C N N 253 
MET   O      O N N 254 
MET   CB     C N N 255 
MET   CG     C N N 256 
MET   SD     S N N 257 
MET   CE     C N N 258 
MET   OXT    O N N 259 
MET   H      H N N 260 
MET   H2     H N N 261 
MET   HA     H N N 262 
MET   HB2    H N N 263 
MET   HB3    H N N 264 
MET   HG2    H N N 265 
MET   HG3    H N N 266 
MET   HE1    H N N 267 
MET   HE2    H N N 268 
MET   HE3    H N N 269 
MET   HXT    H N N 270 
PHE   N      N N N 271 
PHE   CA     C N S 272 
PHE   C      C N N 273 
PHE   O      O N N 274 
PHE   CB     C N N 275 
PHE   CG     C Y N 276 
PHE   CD1    C Y N 277 
PHE   CD2    C Y N 278 
PHE   CE1    C Y N 279 
PHE   CE2    C Y N 280 
PHE   CZ     C Y N 281 
PHE   OXT    O N N 282 
PHE   H      H N N 283 
PHE   H2     H N N 284 
PHE   HA     H N N 285 
PHE   HB2    H N N 286 
PHE   HB3    H N N 287 
PHE   HD1    H N N 288 
PHE   HD2    H N N 289 
PHE   HE1    H N N 290 
PHE   HE2    H N N 291 
PHE   HZ     H N N 292 
PHE   HXT    H N N 293 
PRO   N      N N N 294 
PRO   CA     C N S 295 
PRO   C      C N N 296 
PRO   O      O N N 297 
PRO   CB     C N N 298 
PRO   CG     C N N 299 
PRO   CD     C N N 300 
PRO   OXT    O N N 301 
PRO   H      H N N 302 
PRO   HA     H N N 303 
PRO   HB2    H N N 304 
PRO   HB3    H N N 305 
PRO   HG2    H N N 306 
PRO   HG3    H N N 307 
PRO   HD2    H N N 308 
PRO   HD3    H N N 309 
PRO   HXT    H N N 310 
SAH   N      N N N 311 
SAH   CA     C N S 312 
SAH   CB     C N N 313 
SAH   CG     C N N 314 
SAH   SD     S N N 315 
SAH   C      C N N 316 
SAH   O      O N N 317 
SAH   OXT    O N N 318 
SAH   "C5'"  C N N 319 
SAH   "C4'"  C N S 320 
SAH   "O4'"  O N N 321 
SAH   "C3'"  C N S 322 
SAH   "O3'"  O N N 323 
SAH   "C2'"  C N R 324 
SAH   "O2'"  O N N 325 
SAH   "C1'"  C N R 326 
SAH   N9     N Y N 327 
SAH   C8     C Y N 328 
SAH   N7     N Y N 329 
SAH   C5     C Y N 330 
SAH   C6     C Y N 331 
SAH   N6     N N N 332 
SAH   N1     N Y N 333 
SAH   C2     C Y N 334 
SAH   N3     N Y N 335 
SAH   C4     C Y N 336 
SAH   HN1    H N N 337 
SAH   HN2    H N N 338 
SAH   HA     H N N 339 
SAH   HB1    H N N 340 
SAH   HB2    H N N 341 
SAH   HG1    H N N 342 
SAH   HG2    H N N 343 
SAH   HXT    H N N 344 
SAH   "H5'1" H N N 345 
SAH   "H5'2" H N N 346 
SAH   "H4'"  H N N 347 
SAH   "H3'"  H N N 348 
SAH   "HO3'" H N N 349 
SAH   "H2'"  H N N 350 
SAH   "HO2'" H N N 351 
SAH   "H1'"  H N N 352 
SAH   H8     H N N 353 
SAH   HN61   H N N 354 
SAH   HN62   H N N 355 
SAH   H2     H N N 356 
SER   N      N N N 357 
SER   CA     C N S 358 
SER   C      C N N 359 
SER   O      O N N 360 
SER   CB     C N N 361 
SER   OG     O N N 362 
SER   OXT    O N N 363 
SER   H      H N N 364 
SER   H2     H N N 365 
SER   HA     H N N 366 
SER   HB2    H N N 367 
SER   HB3    H N N 368 
SER   HG     H N N 369 
SER   HXT    H N N 370 
THR   N      N N N 371 
THR   CA     C N S 372 
THR   C      C N N 373 
THR   O      O N N 374 
THR   CB     C N R 375 
THR   OG1    O N N 376 
THR   CG2    C N N 377 
THR   OXT    O N N 378 
THR   H      H N N 379 
THR   H2     H N N 380 
THR   HA     H N N 381 
THR   HB     H N N 382 
THR   HG1    H N N 383 
THR   HG21   H N N 384 
THR   HG22   H N N 385 
THR   HG23   H N N 386 
THR   HXT    H N N 387 
TRP   N      N N N 388 
TRP   CA     C N S 389 
TRP   C      C N N 390 
TRP   O      O N N 391 
TRP   CB     C N N 392 
TRP   CG     C Y N 393 
TRP   CD1    C Y N 394 
TRP   CD2    C Y N 395 
TRP   NE1    N Y N 396 
TRP   CE2    C Y N 397 
TRP   CE3    C Y N 398 
TRP   CZ2    C Y N 399 
TRP   CZ3    C Y N 400 
TRP   CH2    C Y N 401 
TRP   OXT    O N N 402 
TRP   H      H N N 403 
TRP   H2     H N N 404 
TRP   HA     H N N 405 
TRP   HB2    H N N 406 
TRP   HB3    H N N 407 
TRP   HD1    H N N 408 
TRP   HE1    H N N 409 
TRP   HE3    H N N 410 
TRP   HZ2    H N N 411 
TRP   HZ3    H N N 412 
TRP   HH2    H N N 413 
TRP   HXT    H N N 414 
TYR   N      N N N 415 
TYR   CA     C N S 416 
TYR   C      C N N 417 
TYR   O      O N N 418 
TYR   CB     C N N 419 
TYR   CG     C Y N 420 
TYR   CD1    C Y N 421 
TYR   CD2    C Y N 422 
TYR   CE1    C Y N 423 
TYR   CE2    C Y N 424 
TYR   CZ     C Y N 425 
TYR   OH     O N N 426 
TYR   OXT    O N N 427 
TYR   H      H N N 428 
TYR   H2     H N N 429 
TYR   HA     H N N 430 
TYR   HB2    H N N 431 
TYR   HB3    H N N 432 
TYR   HD1    H N N 433 
TYR   HD2    H N N 434 
TYR   HE1    H N N 435 
TYR   HE2    H N N 436 
TYR   HH     H N N 437 
TYR   HXT    H N N 438 
VAL   N      N N N 439 
VAL   CA     C N S 440 
VAL   C      C N N 441 
VAL   O      O N N 442 
VAL   CB     C N N 443 
VAL   CG1    C N N 444 
VAL   CG2    C N N 445 
VAL   OXT    O N N 446 
VAL   H      H N N 447 
VAL   H2     H N N 448 
VAL   HA     H N N 449 
VAL   HB     H N N 450 
VAL   HG11   H N N 451 
VAL   HG12   H N N 452 
VAL   HG13   H N N 453 
VAL   HG21   H N N 454 
VAL   HG22   H N N 455 
VAL   HG23   H N N 456 
VAL   HXT    H N N 457 
# 
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 
A1IPO C1    O2     sing N N 1   
A1IPO O2    C3     sing N N 2   
A1IPO C3    C4     doub Y N 3   
A1IPO C3    C9     sing Y N 4   
A1IPO C4    C5     sing Y N 5   
A1IPO C10   C9     sing N N 6   
A1IPO C9    C7     doub Y N 7   
A1IPO C5    N6     doub Y N 8   
A1IPO C7    N6     sing Y N 9   
A1IPO C7    C8     sing N N 10  
A1IPO C1    H1     sing N N 11  
A1IPO C1    H2     sing N N 12  
A1IPO C1    H3     sing N N 13  
A1IPO C8    H4     sing N N 14  
A1IPO C8    H5     sing N N 15  
A1IPO C8    H6     sing N N 16  
A1IPO C10   H7     sing N N 17  
A1IPO C10   H8     sing N N 18  
A1IPO C10   H9     sing N N 19  
A1IPO C4    H10    sing N N 20  
A1IPO C5    H11    sing N N 21  
ALA   N     CA     sing N N 22  
ALA   N     H      sing N N 23  
ALA   N     H2     sing N N 24  
ALA   CA    C      sing N N 25  
ALA   CA    CB     sing N N 26  
ALA   CA    HA     sing N N 27  
ALA   C     O      doub N N 28  
ALA   C     OXT    sing N N 29  
ALA   CB    HB1    sing N N 30  
ALA   CB    HB2    sing N N 31  
ALA   CB    HB3    sing N N 32  
ALA   OXT   HXT    sing N N 33  
ARG   N     CA     sing N N 34  
ARG   N     H      sing N N 35  
ARG   N     H2     sing N N 36  
ARG   CA    C      sing N N 37  
ARG   CA    CB     sing N N 38  
ARG   CA    HA     sing N N 39  
ARG   C     O      doub N N 40  
ARG   C     OXT    sing N N 41  
ARG   CB    CG     sing N N 42  
ARG   CB    HB2    sing N N 43  
ARG   CB    HB3    sing N N 44  
ARG   CG    CD     sing N N 45  
ARG   CG    HG2    sing N N 46  
ARG   CG    HG3    sing N N 47  
ARG   CD    NE     sing N N 48  
ARG   CD    HD2    sing N N 49  
ARG   CD    HD3    sing N N 50  
ARG   NE    CZ     sing N N 51  
ARG   NE    HE     sing N N 52  
ARG   CZ    NH1    sing N N 53  
ARG   CZ    NH2    doub N N 54  
ARG   NH1   HH11   sing N N 55  
ARG   NH1   HH12   sing N N 56  
ARG   NH2   HH21   sing N N 57  
ARG   NH2   HH22   sing N N 58  
ARG   OXT   HXT    sing N N 59  
ASN   N     CA     sing N N 60  
ASN   N     H      sing N N 61  
ASN   N     H2     sing N N 62  
ASN   CA    C      sing N N 63  
ASN   CA    CB     sing N N 64  
ASN   CA    HA     sing N N 65  
ASN   C     O      doub N N 66  
ASN   C     OXT    sing N N 67  
ASN   CB    CG     sing N N 68  
ASN   CB    HB2    sing N N 69  
ASN   CB    HB3    sing N N 70  
ASN   CG    OD1    doub N N 71  
ASN   CG    ND2    sing N N 72  
ASN   ND2   HD21   sing N N 73  
ASN   ND2   HD22   sing N N 74  
ASN   OXT   HXT    sing N N 75  
ASP   N     CA     sing N N 76  
ASP   N     H      sing N N 77  
ASP   N     H2     sing N N 78  
ASP   CA    C      sing N N 79  
ASP   CA    CB     sing N N 80  
ASP   CA    HA     sing N N 81  
ASP   C     O      doub N N 82  
ASP   C     OXT    sing N N 83  
ASP   CB    CG     sing N N 84  
ASP   CB    HB2    sing N N 85  
ASP   CB    HB3    sing N N 86  
ASP   CG    OD1    doub N N 87  
ASP   CG    OD2    sing N N 88  
ASP   OD2   HD2    sing N N 89  
ASP   OXT   HXT    sing N N 90  
CYS   N     CA     sing N N 91  
CYS   N     H      sing N N 92  
CYS   N     H2     sing N N 93  
CYS   CA    C      sing N N 94  
CYS   CA    CB     sing N N 95  
CYS   CA    HA     sing N N 96  
CYS   C     O      doub N N 97  
CYS   C     OXT    sing N N 98  
CYS   CB    SG     sing N N 99  
CYS   CB    HB2    sing N N 100 
CYS   CB    HB3    sing N N 101 
CYS   SG    HG     sing N N 102 
CYS   OXT   HXT    sing N N 103 
GLN   N     CA     sing N N 104 
GLN   N     H      sing N N 105 
GLN   N     H2     sing N N 106 
GLN   CA    C      sing N N 107 
GLN   CA    CB     sing N N 108 
GLN   CA    HA     sing N N 109 
GLN   C     O      doub N N 110 
GLN   C     OXT    sing N N 111 
GLN   CB    CG     sing N N 112 
GLN   CB    HB2    sing N N 113 
GLN   CB    HB3    sing N N 114 
GLN   CG    CD     sing N N 115 
GLN   CG    HG2    sing N N 116 
GLN   CG    HG3    sing N N 117 
GLN   CD    OE1    doub N N 118 
GLN   CD    NE2    sing N N 119 
GLN   NE2   HE21   sing N N 120 
GLN   NE2   HE22   sing N N 121 
GLN   OXT   HXT    sing N N 122 
GLU   N     CA     sing N N 123 
GLU   N     H      sing N N 124 
GLU   N     H2     sing N N 125 
GLU   CA    C      sing N N 126 
GLU   CA    CB     sing N N 127 
GLU   CA    HA     sing N N 128 
GLU   C     O      doub N N 129 
GLU   C     OXT    sing N N 130 
GLU   CB    CG     sing N N 131 
GLU   CB    HB2    sing N N 132 
GLU   CB    HB3    sing N N 133 
GLU   CG    CD     sing N N 134 
GLU   CG    HG2    sing N N 135 
GLU   CG    HG3    sing N N 136 
GLU   CD    OE1    doub N N 137 
GLU   CD    OE2    sing N N 138 
GLU   OE2   HE2    sing N N 139 
GLU   OXT   HXT    sing N N 140 
GLY   N     CA     sing N N 141 
GLY   N     H      sing N N 142 
GLY   N     H2     sing N N 143 
GLY   CA    C      sing N N 144 
GLY   CA    HA2    sing N N 145 
GLY   CA    HA3    sing N N 146 
GLY   C     O      doub N N 147 
GLY   C     OXT    sing N N 148 
GLY   OXT   HXT    sing N N 149 
HIS   N     CA     sing N N 150 
HIS   N     H      sing N N 151 
HIS   N     H2     sing N N 152 
HIS   CA    C      sing N N 153 
HIS   CA    CB     sing N N 154 
HIS   CA    HA     sing N N 155 
HIS   C     O      doub N N 156 
HIS   C     OXT    sing N N 157 
HIS   CB    CG     sing N N 158 
HIS   CB    HB2    sing N N 159 
HIS   CB    HB3    sing N N 160 
HIS   CG    ND1    sing Y N 161 
HIS   CG    CD2    doub Y N 162 
HIS   ND1   CE1    doub Y N 163 
HIS   ND1   HD1    sing N N 164 
HIS   CD2   NE2    sing Y N 165 
HIS   CD2   HD2    sing N N 166 
HIS   CE1   NE2    sing Y N 167 
HIS   CE1   HE1    sing N N 168 
HIS   NE2   HE2    sing N N 169 
HIS   OXT   HXT    sing N N 170 
HOH   O     H1     sing N N 171 
HOH   O     H2     sing N N 172 
ILE   N     CA     sing N N 173 
ILE   N     H      sing N N 174 
ILE   N     H2     sing N N 175 
ILE   CA    C      sing N N 176 
ILE   CA    CB     sing N N 177 
ILE   CA    HA     sing N N 178 
ILE   C     O      doub N N 179 
ILE   C     OXT    sing N N 180 
ILE   CB    CG1    sing N N 181 
ILE   CB    CG2    sing N N 182 
ILE   CB    HB     sing N N 183 
ILE   CG1   CD1    sing N N 184 
ILE   CG1   HG12   sing N N 185 
ILE   CG1   HG13   sing N N 186 
ILE   CG2   HG21   sing N N 187 
ILE   CG2   HG22   sing N N 188 
ILE   CG2   HG23   sing N N 189 
ILE   CD1   HD11   sing N N 190 
ILE   CD1   HD12   sing N N 191 
ILE   CD1   HD13   sing N N 192 
ILE   OXT   HXT    sing N N 193 
LEU   N     CA     sing N N 194 
LEU   N     H      sing N N 195 
LEU   N     H2     sing N N 196 
LEU   CA    C      sing N N 197 
LEU   CA    CB     sing N N 198 
LEU   CA    HA     sing N N 199 
LEU   C     O      doub N N 200 
LEU   C     OXT    sing N N 201 
LEU   CB    CG     sing N N 202 
LEU   CB    HB2    sing N N 203 
LEU   CB    HB3    sing N N 204 
LEU   CG    CD1    sing N N 205 
LEU   CG    CD2    sing N N 206 
LEU   CG    HG     sing N N 207 
LEU   CD1   HD11   sing N N 208 
LEU   CD1   HD12   sing N N 209 
LEU   CD1   HD13   sing N N 210 
LEU   CD2   HD21   sing N N 211 
LEU   CD2   HD22   sing N N 212 
LEU   CD2   HD23   sing N N 213 
LEU   OXT   HXT    sing N N 214 
LYS   N     CA     sing N N 215 
LYS   N     H      sing N N 216 
LYS   N     H2     sing N N 217 
LYS   CA    C      sing N N 218 
LYS   CA    CB     sing N N 219 
LYS   CA    HA     sing N N 220 
LYS   C     O      doub N N 221 
LYS   C     OXT    sing N N 222 
LYS   CB    CG     sing N N 223 
LYS   CB    HB2    sing N N 224 
LYS   CB    HB3    sing N N 225 
LYS   CG    CD     sing N N 226 
LYS   CG    HG2    sing N N 227 
LYS   CG    HG3    sing N N 228 
LYS   CD    CE     sing N N 229 
LYS   CD    HD2    sing N N 230 
LYS   CD    HD3    sing N N 231 
LYS   CE    NZ     sing N N 232 
LYS   CE    HE2    sing N N 233 
LYS   CE    HE3    sing N N 234 
LYS   NZ    HZ1    sing N N 235 
LYS   NZ    HZ2    sing N N 236 
LYS   NZ    HZ3    sing N N 237 
LYS   OXT   HXT    sing N N 238 
MET   N     CA     sing N N 239 
MET   N     H      sing N N 240 
MET   N     H2     sing N N 241 
MET   CA    C      sing N N 242 
MET   CA    CB     sing N N 243 
MET   CA    HA     sing N N 244 
MET   C     O      doub N N 245 
MET   C     OXT    sing N N 246 
MET   CB    CG     sing N N 247 
MET   CB    HB2    sing N N 248 
MET   CB    HB3    sing N N 249 
MET   CG    SD     sing N N 250 
MET   CG    HG2    sing N N 251 
MET   CG    HG3    sing N N 252 
MET   SD    CE     sing N N 253 
MET   CE    HE1    sing N N 254 
MET   CE    HE2    sing N N 255 
MET   CE    HE3    sing N N 256 
MET   OXT   HXT    sing N N 257 
PHE   N     CA     sing N N 258 
PHE   N     H      sing N N 259 
PHE   N     H2     sing N N 260 
PHE   CA    C      sing N N 261 
PHE   CA    CB     sing N N 262 
PHE   CA    HA     sing N N 263 
PHE   C     O      doub N N 264 
PHE   C     OXT    sing N N 265 
PHE   CB    CG     sing N N 266 
PHE   CB    HB2    sing N N 267 
PHE   CB    HB3    sing N N 268 
PHE   CG    CD1    doub Y N 269 
PHE   CG    CD2    sing Y N 270 
PHE   CD1   CE1    sing Y N 271 
PHE   CD1   HD1    sing N N 272 
PHE   CD2   CE2    doub Y N 273 
PHE   CD2   HD2    sing N N 274 
PHE   CE1   CZ     doub Y N 275 
PHE   CE1   HE1    sing N N 276 
PHE   CE2   CZ     sing Y N 277 
PHE   CE2   HE2    sing N N 278 
PHE   CZ    HZ     sing N N 279 
PHE   OXT   HXT    sing N N 280 
PRO   N     CA     sing N N 281 
PRO   N     CD     sing N N 282 
PRO   N     H      sing N N 283 
PRO   CA    C      sing N N 284 
PRO   CA    CB     sing N N 285 
PRO   CA    HA     sing N N 286 
PRO   C     O      doub N N 287 
PRO   C     OXT    sing N N 288 
PRO   CB    CG     sing N N 289 
PRO   CB    HB2    sing N N 290 
PRO   CB    HB3    sing N N 291 
PRO   CG    CD     sing N N 292 
PRO   CG    HG2    sing N N 293 
PRO   CG    HG3    sing N N 294 
PRO   CD    HD2    sing N N 295 
PRO   CD    HD3    sing N N 296 
PRO   OXT   HXT    sing N N 297 
SAH   N     CA     sing N N 298 
SAH   N     HN1    sing N N 299 
SAH   N     HN2    sing N N 300 
SAH   CA    CB     sing N N 301 
SAH   CA    C      sing N N 302 
SAH   CA    HA     sing N N 303 
SAH   CB    CG     sing N N 304 
SAH   CB    HB1    sing N N 305 
SAH   CB    HB2    sing N N 306 
SAH   CG    SD     sing N N 307 
SAH   CG    HG1    sing N N 308 
SAH   CG    HG2    sing N N 309 
SAH   SD    "C5'"  sing N N 310 
SAH   C     O      doub N N 311 
SAH   C     OXT    sing N N 312 
SAH   OXT   HXT    sing N N 313 
SAH   "C5'" "C4'"  sing N N 314 
SAH   "C5'" "H5'1" sing N N 315 
SAH   "C5'" "H5'2" sing N N 316 
SAH   "C4'" "O4'"  sing N N 317 
SAH   "C4'" "C3'"  sing N N 318 
SAH   "C4'" "H4'"  sing N N 319 
SAH   "O4'" "C1'"  sing N N 320 
SAH   "C3'" "O3'"  sing N N 321 
SAH   "C3'" "C2'"  sing N N 322 
SAH   "C3'" "H3'"  sing N N 323 
SAH   "O3'" "HO3'" sing N N 324 
SAH   "C2'" "O2'"  sing N N 325 
SAH   "C2'" "C1'"  sing N N 326 
SAH   "C2'" "H2'"  sing N N 327 
SAH   "O2'" "HO2'" sing N N 328 
SAH   "C1'" N9     sing N N 329 
SAH   "C1'" "H1'"  sing N N 330 
SAH   N9    C8     sing Y N 331 
SAH   N9    C4     sing Y N 332 
SAH   C8    N7     doub Y N 333 
SAH   C8    H8     sing N N 334 
SAH   N7    C5     sing Y N 335 
SAH   C5    C6     sing Y N 336 
SAH   C5    C4     doub Y N 337 
SAH   C6    N6     sing N N 338 
SAH   C6    N1     doub Y N 339 
SAH   N6    HN61   sing N N 340 
SAH   N6    HN62   sing N N 341 
SAH   N1    C2     sing Y N 342 
SAH   C2    N3     doub Y N 343 
SAH   C2    H2     sing N N 344 
SAH   N3    C4     sing Y N 345 
SER   N     CA     sing N N 346 
SER   N     H      sing N N 347 
SER   N     H2     sing N N 348 
SER   CA    C      sing N N 349 
SER   CA    CB     sing N N 350 
SER   CA    HA     sing N N 351 
SER   C     O      doub N N 352 
SER   C     OXT    sing N N 353 
SER   CB    OG     sing N N 354 
SER   CB    HB2    sing N N 355 
SER   CB    HB3    sing N N 356 
SER   OG    HG     sing N N 357 
SER   OXT   HXT    sing N N 358 
THR   N     CA     sing N N 359 
THR   N     H      sing N N 360 
THR   N     H2     sing N N 361 
THR   CA    C      sing N N 362 
THR   CA    CB     sing N N 363 
THR   CA    HA     sing N N 364 
THR   C     O      doub N N 365 
THR   C     OXT    sing N N 366 
THR   CB    OG1    sing N N 367 
THR   CB    CG2    sing N N 368 
THR   CB    HB     sing N N 369 
THR   OG1   HG1    sing N N 370 
THR   CG2   HG21   sing N N 371 
THR   CG2   HG22   sing N N 372 
THR   CG2   HG23   sing N N 373 
THR   OXT   HXT    sing N N 374 
TRP   N     CA     sing N N 375 
TRP   N     H      sing N N 376 
TRP   N     H2     sing N N 377 
TRP   CA    C      sing N N 378 
TRP   CA    CB     sing N N 379 
TRP   CA    HA     sing N N 380 
TRP   C     O      doub N N 381 
TRP   C     OXT    sing N N 382 
TRP   CB    CG     sing N N 383 
TRP   CB    HB2    sing N N 384 
TRP   CB    HB3    sing N N 385 
TRP   CG    CD1    doub Y N 386 
TRP   CG    CD2    sing Y N 387 
TRP   CD1   NE1    sing Y N 388 
TRP   CD1   HD1    sing N N 389 
TRP   CD2   CE2    doub Y N 390 
TRP   CD2   CE3    sing Y N 391 
TRP   NE1   CE2    sing Y N 392 
TRP   NE1   HE1    sing N N 393 
TRP   CE2   CZ2    sing Y N 394 
TRP   CE3   CZ3    doub Y N 395 
TRP   CE3   HE3    sing N N 396 
TRP   CZ2   CH2    doub Y N 397 
TRP   CZ2   HZ2    sing N N 398 
TRP   CZ3   CH2    sing Y N 399 
TRP   CZ3   HZ3    sing N N 400 
TRP   CH2   HH2    sing N N 401 
TRP   OXT   HXT    sing N N 402 
TYR   N     CA     sing N N 403 
TYR   N     H      sing N N 404 
TYR   N     H2     sing N N 405 
TYR   CA    C      sing N N 406 
TYR   CA    CB     sing N N 407 
TYR   CA    HA     sing N N 408 
TYR   C     O      doub N N 409 
TYR   C     OXT    sing N N 410 
TYR   CB    CG     sing N N 411 
TYR   CB    HB2    sing N N 412 
TYR   CB    HB3    sing N N 413 
TYR   CG    CD1    doub Y N 414 
TYR   CG    CD2    sing Y N 415 
TYR   CD1   CE1    sing Y N 416 
TYR   CD1   HD1    sing N N 417 
TYR   CD2   CE2    doub Y N 418 
TYR   CD2   HD2    sing N N 419 
TYR   CE1   CZ     doub Y N 420 
TYR   CE1   HE1    sing N N 421 
TYR   CE2   CZ     sing Y N 422 
TYR   CE2   HE2    sing N N 423 
TYR   CZ    OH     sing N N 424 
TYR   OH    HH     sing N N 425 
TYR   OXT   HXT    sing N N 426 
VAL   N     CA     sing N N 427 
VAL   N     H      sing N N 428 
VAL   N     H2     sing N N 429 
VAL   CA    C      sing N N 430 
VAL   CA    CB     sing N N 431 
VAL   CA    HA     sing N N 432 
VAL   C     O      doub N N 433 
VAL   C     OXT    sing N N 434 
VAL   CB    CG1    sing N N 435 
VAL   CB    CG2    sing N N 436 
VAL   CB    HB     sing N N 437 
VAL   CG1   HG11   sing N N 438 
VAL   CG1   HG12   sing N N 439 
VAL   CG1   HG13   sing N N 440 
VAL   CG2   HG21   sing N N 441 
VAL   CG2   HG22   sing N N 442 
VAL   CG2   HG23   sing N N 443 
VAL   OXT   HXT    sing N N 444 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                Sweden 
_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                    9GVW 
_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]   0.016158 
_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]   0.014323 
_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]   0.008562 
_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     . GLY   A 1 23  ? -0.413  12.32  21.289 1   29.53 ? 4   GLY   A N     1 
ATOM   2    C CA    . GLY   A 1 23  ? 0.889   11.868 21.78  1   28.02 ? 4   GLY   A CA    1 
ATOM   3    C C     . GLY   A 1 23  ? 1.264   12.367 23.16  1   26.11 ? 4   GLY   A C     1 
ATOM   4    O O     . GLY   A 1 23  ? 2.422   12.218 23.549 1   28.49 ? 4   GLY   A O     1 
ATOM   5    N N     . PHE   A 1 24  ? 0.293   12.934 23.934 1   20.49 ? 5   PHE   A N     1 
ATOM   6    C CA    . PHE   A 1 24  ? 0.499   13.518 25.277 1   20.08 ? 5   PHE   A CA    1 
ATOM   7    C C     . PHE   A 1 24  ? -0.323  12.73  26.309 1   19.74 ? 5   PHE   A C     1 
ATOM   8    O O     . PHE   A 1 24  ? -1.454  12.281 25.995 1   20.59 ? 5   PHE   A O     1 
ATOM   9    C CB    . PHE   A 1 24  ? -0.001  14.989 25.233 1   19.19 ? 5   PHE   A CB    1 
ATOM   10   C CG    . PHE   A 1 24  ? 0.622   15.883 26.283 1   19.07 ? 5   PHE   A CG    1 
ATOM   11   C CD1   . PHE   A 1 24  ? 1.804   16.573 26.02  1   18.81 ? 5   PHE   A CD1   1 
ATOM   12   C CD2   . PHE   A 1 24  ? 0.017   16.063 27.522 1   19.67 ? 5   PHE   A CD2   1 
ATOM   13   C CE1   . PHE   A 1 24  ? 2.353   17.459 26.969 1   18.1  ? 5   PHE   A CE1   1 
ATOM   14   C CE2   . PHE   A 1 24  ? 0.574   16.932 28.479 1   20.01 ? 5   PHE   A CE2   1 
ATOM   15   C CZ    . PHE   A 1 24  ? 1.755   17.625 28.201 1   17.77 ? 5   PHE   A CZ    1 
ATOM   16   N N     . THR   A 1 25  ? 0.166   12.596 27.552 1   18.54 ? 6   THR   A N     1 
ATOM   17   C CA    . THR   A 1 25  ? -0.547  11.925 28.668 1   19.04 ? 6   THR   A CA    1 
ATOM   18   C C     . THR   A 1 25  ? -1.99   12.404 28.751 1   21.14 ? 6   THR   A C     1 
ATOM   19   O O     . THR   A 1 25  ? -2.255  13.599 28.773 1   21.47 ? 6   THR   A O     1 
ATOM   20   C CB    . THR   A 1 25  ? 0.155   12.264 29.992 1   18.38 ? 6   THR   A CB    1 
ATOM   21   O OG1   . THR   A 1 25  ? 1.463   11.7   29.953 1   18.35 ? 6   THR   A OG1   1 
ATOM   22   C CG2   . THR   A 1 25  ? -0.56   11.777 31.239 1   18.93 ? 6   THR   A CG2   1 
ATOM   23   N N     . SER   A 1 26  ? -2.924  11.452 28.774 1   22.24 ? 7   SER   A N     1 
ATOM   24   C CA    . SER   A 1 26  ? -4.344  11.822 28.917 1   22.03 ? 7   SER   A CA    1 
ATOM   25   C C     . SER   A 1 26  ? -4.596  12.31  30.369 1   21.35 ? 7   SER   A C     1 
ATOM   26   O O     . SER   A 1 26  ? -3.974  11.813 31.3   1   20.66 ? 7   SER   A O     1 
ATOM   27   C CB    . SER   A 1 26  ? -5.207  10.606 28.612 1   22.51 ? 7   SER   A CB    1 
ATOM   28   O OG    . SER   A 1 26  ? -4.943  9.522  29.501 1   24.04 ? 7   SER   A OG    1 
ATOM   29   N N     . LYS   A 1 27  ? -5.526  13.259 30.577 1   22.59 ? 8   LYS   A N     1 
ATOM   30   C CA    . LYS   A 1 27  ? -5.756  13.793 31.923 1   23.48 ? 8   LYS   A CA    1 
ATOM   31   C C     . LYS   A 1 27  ? -6.176  12.702 32.915 1   22.36 ? 8   LYS   A C     1 
ATOM   32   O O     . LYS   A 1 27  ? -5.81   12.745 34.079 1   21.64 ? 8   LYS   A O     1 
ATOM   33   C CB    . LYS   A 1 27  ? -6.674  15.042 31.979 1   29.89 ? 8   LYS   A CB    1 
ATOM   34   C CG    . LYS   A 1 27  ? -8.139  14.843 31.828 1   32.91 ? 8   LYS   A CG    1 
ATOM   35   C CD    . LYS   A 1 27  ? -8.856  16.244 31.833 1   32.89 ? 8   LYS   A CD    1 
ATOM   36   C CE    . LYS   A 1 27  ? -8.458  17.245 30.768 1   32.57 ? 8   LYS   A CE    1 
ATOM   37   N NZ    . LYS   A 1 27  ? -9.557  18.227 30.509 1   30.64 ? 8   LYS   A NZ    1 
ATOM   38   N N     . ASP   A 1 28  ? -6.941  11.715 32.45  1   22.07 ? 9   ASP   A N     1 
ATOM   39   C CA    . ASP   A 1 28  ? -7.397  10.632 33.321 1   21.61 ? 9   ASP   A CA    1 
ATOM   40   C C     . ASP   A 1 28  ? -6.231  9.818  33.897 1   21.64 ? 9   ASP   A C     1 
ATOM   41   O O     . ASP   A 1 28  ? -6.375  9.152  34.937 1   22.67 ? 9   ASP   A O     1 
ATOM   42   C CB    . ASP   A 1 28  ? -8.364  9.693  32.568 1   25.56 ? 9   ASP   A CB    1 
ATOM   43   C CG    . ASP   A 1 28  ? -7.65   8.915  31.492 1   31.53 ? 9   ASP   A CG    1 
ATOM   44   O OD1   . ASP   A 1 28  ? -7.248  7.777  31.76  1   38.13 ? 9   ASP   A OD1   1 
ATOM   45   O OD2   . ASP   A 1 28  ? -7.43   9.462  30.423 1   34.55 ? 9   ASP   A OD2   1 
ATOM   46   N N     . THR   A 1 29  ? -5.037  9.857  33.251 1   19.93 ? 10  THR   A N     1 
ATOM   47   C CA    . THR   A 1 29  ? -3.857  9.197  33.772 1   19.75 ? 10  THR   A CA    1 
ATOM   48   C C     . THR   A 1 29  ? -3.483  9.732  35.134 1   19.19 ? 10  THR   A C     1 
ATOM   49   O O     . THR   A 1 29  ? -2.919  9.022  35.962 1   18.53 ? 10  THR   A O     1 
ATOM   50   C CB    . THR   A 1 29  ? -2.689  9.301  32.766 1   21.49 ? 10  THR   A CB    1 
ATOM   51   O OG1   . THR   A 1 29  ? -3.135  8.788  31.524 1   24.55 ? 10  THR   A OG1   1 
ATOM   52   C CG2   . THR   A 1 29  ? -1.485  8.507  33.168 1   20.87 ? 10  THR   A CG2   1 
ATOM   53   N N     . TYR   A 1 30  ? -3.731  11.043 35.367 1   18.06 ? 11  TYR   A N     1 
ATOM   54   C CA    . TYR   A 1 30  ? -3.422  11.619 36.663 1   17.79 ? 11  TYR   A CA    1 
ATOM   55   C C     . TYR   A 1 30  ? -4.305  11.109 37.765 1   20.23 ? 11  TYR   A C     1 
ATOM   56   O O     . TYR   A 1 30  ? -3.856  11.083 38.908 1   22.24 ? 11  TYR   A O     1 
ATOM   57   C CB    . TYR   A 1 30  ? -3.498  13.152 36.6   1   17.39 ? 11  TYR   A CB    1 
ATOM   58   C CG    . TYR   A 1 30  ? -2.228  13.728 36.012 1   16.11 ? 11  TYR   A CG    1 
ATOM   59   C CD1   . TYR   A 1 30  ? -1.115  13.911 36.796 1   15.47 ? 11  TYR   A CD1   1 
ATOM   60   C CD2   . TYR   A 1 30  ? -2.115  13.967 34.637 1   15.64 ? 11  TYR   A CD2   1 
ATOM   61   C CE1   . TYR   A 1 30  ? 0.096   14.298 36.238 1   15.82 ? 11  TYR   A CE1   1 
ATOM   62   C CE2   . TYR   A 1 30  ? -0.929  14.439 34.077 1   15.97 ? 11  TYR   A CE2   1 
ATOM   63   C CZ    . TYR   A 1 30  ? 0.167   14.581 34.889 1   15.98 ? 11  TYR   A CZ    1 
ATOM   64   O OH    . TYR   A 1 30  ? 1.355   15.015 34.369 1   15.82 ? 11  TYR   A OH    1 
ATOM   65   N N     . LEU   A 1 31  ? -5.548  10.66  37.454 1   21.28 ? 12  LEU   A N     1 
ATOM   66   C CA    . LEU   A 1 31  ? -6.413  10.157 38.512 1   23.17 ? 12  LEU   A CA    1 
ATOM   67   C C     . LEU   A 1 31  ? -5.952  8.786  39.022 1   23.01 ? 12  LEU   A C     1 
ATOM   68   O O     . LEU   A 1 31  ? -6.038  8.506  40.207 1   24.21 ? 12  LEU   A O     1 
ATOM   69   C CB    . LEU   A 1 31  ? -7.862  10.005 37.989 1   24.99 ? 12  LEU   A CB    1 
ATOM   70   C CG    . LEU   A 1 31  ? -8.466  11.268 37.425 1   28.72 ? 12  LEU   A CG    1 
ATOM   71   C CD1   . LEU   A 1 31  ? -9.839  10.991 36.803 1   31.14 ? 12  LEU   A CD1   1 
ATOM   72   C CD2   . LEU   A 1 31  ? -8.604  12.331 38.5   1   30.65 ? 12  LEU   A CD2   1 
ATOM   73   N N     . SER   A 1 32  ? -5.392  7.989  38.143 1   22.27 ? 13  SER   A N     1 
ATOM   74   C CA    . SER   A 1 32  ? -5.076  6.602  38.362 1   22.4  ? 13  SER   A CA    1 
ATOM   75   C C     . SER   A 1 32  ? -3.632  6.226  38.528 1   23.64 ? 13  SER   A C     1 
ATOM   76   O O     . SER   A 1 32  ? -3.297  5.288  39.283 1   27.48 ? 13  SER   A O     1 
ATOM   77   C CB    . SER   A 1 32  ? -5.646  5.829  37.169 1   24.41 ? 13  SER   A CB    1 
ATOM   78   O OG    . SER   A 1 32  ? -5.231  6.365  35.909 1   24.16 ? 13  SER   A OG    1 
ATOM   79   N N     . HIS   A 1 33  ? -2.741  6.914  37.83  1   18.78 ? 14  HIS   A N     1 
ATOM   80   C CA    . HIS   A 1 33  ? -1.353  6.492  37.719 1   18.4  ? 14  HIS   A CA    1 
ATOM   81   C C     . HIS   A 1 33  ? -0.322  7.413  38.34  1   18.1  ? 14  HIS   A C     1 
ATOM   82   O O     . HIS   A 1 33  ? 0.878   7.142  38.276 1   18.07 ? 14  HIS   A O     1 
ATOM   83   C CB    . HIS   A 1 33  ? -1.027  6.296  36.218 1   19.52 ? 14  HIS   A CB    1 
ATOM   84   C CG    . HIS   A 1 33  ? -1.676  5.041  35.674 1   21.39 ? 14  HIS   A CG    1 
ATOM   85   N ND1   . HIS   A 1 33  ? -3.037  4.977  35.467 1   22.25 ? 14  HIS   A ND1   1 
ATOM   86   C CD2   . HIS   A 1 33  ? -1.124  3.833  35.404 1   23.5  ? 14  HIS   A CD2   1 
ATOM   87   C CE1   . HIS   A 1 33  ? -3.289  3.742  35.051 1   23.67 ? 14  HIS   A CE1   1 
ATOM   88   N NE2   . HIS   A 1 33  ? -2.179  2.994  35.017 1   24.56 ? 14  HIS   A NE2   1 
ATOM   89   N N     . PHE   A 1 34  ? -0.769  8.592  38.837 1   18.3  ? 15  PHE   A N     1 
ATOM   90   C CA    . PHE   A 1 34  ? 0.138   9.496  39.527 1   18.04 ? 15  PHE   A CA    1 
ATOM   91   C C     . PHE   A 1 34  ? 0.091   9.093  40.988 1   18.49 ? 15  PHE   A C     1 
ATOM   92   O O     . PHE   A 1 34  ? -0.936  9.287  41.631 1   18.17 ? 15  PHE   A O     1 
ATOM   93   C CB    . PHE   A 1 34  ? -0.317  10.945 39.325 1   16.74 ? 15  PHE   A CB    1 
ATOM   94   C CG    . PHE   A 1 34  ? 0.649   11.991 39.886 1   16.23 ? 15  PHE   A CG    1 
ATOM   95   C CD1   . PHE   A 1 34  ? 0.72    12.23  41.253 1   17.47 ? 15  PHE   A CD1   1 
ATOM   96   C CD2   . PHE   A 1 34  ? 1.414   12.752 39.044 1   16.23 ? 15  PHE   A CD2   1 
ATOM   97   C CE1   . PHE   A 1 34  ? 1.527   13.249 41.748 1   18.15 ? 15  PHE   A CE1   1 
ATOM   98   C CE2   . PHE   A 1 34  ? 2.201   13.786 39.544 1   16.44 ? 15  PHE   A CE2   1 
ATOM   99   C CZ    . PHE   A 1 34  ? 2.275   14.004 40.888 1   16.56 ? 15  PHE   A CZ    1 
ATOM   100  N N     . ASN   A 1 35  ? 1.166   8.462  41.456 1   17.79 ? 16  ASN   A N     1 
ATOM   101  C CA    . ASN   A 1 35  ? 1.224   7.916  42.811 1   18.94 ? 16  ASN   A CA    1 
ATOM   102  C C     . ASN   A 1 35  ? 1.712   9.003  43.727 1   19.1  ? 16  ASN   A C     1 
ATOM   103  O O     . ASN   A 1 35  ? 2.889   9.364  43.666 1   18.98 ? 16  ASN   A O     1 
ATOM   104  C CB    . ASN   A 1 35  ? 2.162   6.694  42.82  1   20.45 ? 16  ASN   A CB    1 
ATOM   105  C CG    . ASN   A 1 35  ? 2.252   6.059  44.168 1   23.39 ? 16  ASN   A CG    1 
ATOM   106  O OD1   . ASN   A 1 35  ? 2.276   6.695  45.222 1   24.56 ? 16  ASN   A OD1   1 
ATOM   107  N ND2   . ASN   A 1 35  ? 2.364   4.726  44.143 1   27.7  ? 16  ASN   A ND2   1 
ATOM   108  N N     . PRO   A 1 36  ? 0.839   9.581  44.57  1   18.6  ? 17  PRO   A N     1 
ATOM   109  C CA    . PRO   A 1 36  ? 1.305   10.767 45.352 1   20.42 ? 17  PRO   A CA    1 
ATOM   110  C C     . PRO   A 1 36  ? 2.477   10.527 46.291 1   20.69 ? 17  PRO   A C     1 
ATOM   111  O O     . PRO   A 1 36  ? 3.389   11.353 46.372 1   19.85 ? 17  PRO   A O     1 
ATOM   112  C CB    . PRO   A 1 36  ? 0.082   11.223 46.129 1   22.43 ? 17  PRO   A CB    1 
ATOM   113  C CG    . PRO   A 1 36  ? -1.001  10.34  45.755 1   22.34 ? 17  PRO   A CG    1 
ATOM   114  C CD    . PRO   A 1 36  ? -0.604  9.338  44.741 1   20.36 ? 17  PRO   A CD    1 
ATOM   115  N N     . ARG   A 1 37  ? 2.446   9.401  47.032 1   21.12 ? 18  ARG   A N     1 
ATOM   116  C CA    . ARG   A 1 37  ? 3.534   9.142  47.96  1   22.28 ? 18  ARG   A CA    1 
ATOM   117  C C     . ARG   A 1 37  ? 4.845   8.887  47.21  1   21.71 ? 18  ARG   A C     1 
ATOM   118  O O     . ARG   A 1 37  ? 5.909   9.356  47.643 1   22.2  ? 18  ARG   A O     1 
ATOM   119  C CB    . ARG   A 1 37  ? 3.208   7.94   48.871 1   26.5  ? 18  ARG   A CB    1 
ATOM   120  C CG    . ARG   A 1 37  ? 4.297   7.71   49.938 1   32.32 ? 18  ARG   A CG    1 
ATOM   121  C CD    . ARG   A 1 37  ? 4.822   8.976  50.635 1   38.09 ? 18  ARG   A CD    1 
ATOM   122  N NE    . ARG   A 1 37  ? 3.763   9.526  51.463 1   44.03 ? 18  ARG   A NE    1 
ATOM   123  C CZ    . ARG   A 1 37  ? 3.678   9.352  52.778 1   47.38 ? 18  ARG   A CZ    1 
ATOM   124  N NH1   . ARG   A 1 37  ? 2.627   9.805  53.442 1   47.28 ? 18  ARG   A NH1   1 
ATOM   125  N NH2   . ARG   A 1 37  ? 4.653   8.742  53.44  1   47.31 ? 18  ARG   A NH2   1 
ATOM   126  N N     . ASP   A 1 38  ? 4.768   8.218  46.047 1   19.93 ? 19  ASP   A N     1 
ATOM   127  C CA    . ASP   A 1 38  ? 5.991   7.982  45.273 1   20.27 ? 19  ASP   A CA    1 
ATOM   128  C C     . ASP   A 1 38  ? 6.527   9.306  44.712 1   19.83 ? 19  ASP   A C     1 
ATOM   129  O O     . ASP   A 1 38  ? 7.724   9.542  44.738 1   19.95 ? 19  ASP   A O     1 
ATOM   130  C CB    . ASP   A 1 38  ? 5.709   7.021  44.151 1   22.98 ? 19  ASP   A CB    1 
ATOM   131  C CG    . ASP   A 1 38  ? 6.931   6.354  43.606 1   28.69 ? 19  ASP   A CG    1 
ATOM   132  O OD1   . ASP   A 1 38  ? 7.92    6.186  44.384 1   30.97 ? 19  ASP   A OD1   1 
ATOM   133  O OD2   . ASP   A 1 38  ? 6.89    5.922  42.426 1   29.32 ? 19  ASP   A OD2   1 
ATOM   134  N N     . TYR   A 1 39  ? 5.632   10.196 44.284 1   18.57 ? 20  TYR   A N     1 
ATOM   135  C CA    . TYR   A 1 39  ? 6.076   11.545 43.819 1   16.22 ? 20  TYR   A CA    1 
ATOM   136  C C     . TYR   A 1 39  ? 6.842   12.261 44.951 1   17.59 ? 20  TYR   A C     1 
ATOM   137  O O     . TYR   A 1 39  ? 7.903   12.825 44.709 1   17.55 ? 20  TYR   A O     1 
ATOM   138  C CB    . TYR   A 1 39  ? 4.815   12.329 43.445 1   15.77 ? 20  TYR   A CB    1 
ATOM   139  C CG    . TYR   A 1 39  ? 5.105   13.716 42.902 1   15.65 ? 20  TYR   A CG    1 
ATOM   140  C CD1   . TYR   A 1 39  ? 5.701   13.885 41.659 1   15.44 ? 20  TYR   A CD1   1 
ATOM   141  C CD2   . TYR   A 1 39  ? 4.806   14.848 43.642 1   16.26 ? 20  TYR   A CD2   1 
ATOM   142  C CE1   . TYR   A 1 39  ? 5.927   15.168 41.131 1   15.52 ? 20  TYR   A CE1   1 
ATOM   143  C CE2   . TYR   A 1 39  ? 4.982   16.128 43.115 1   15.43 ? 20  TYR   A CE2   1 
ATOM   144  C CZ    . TYR   A 1 39  ? 5.547   16.281 41.859 1   15.63 ? 20  TYR   A CZ    1 
ATOM   145  O OH    . TYR   A 1 39  ? 5.76    17.553 41.367 1   15.15 ? 20  TYR   A OH    1 
ATOM   146  N N     . LEU   A 1 40  ? 6.295   12.231 46.171 1   18.65 ? 21  LEU   A N     1 
ATOM   147  C CA    . LEU   A 1 40  ? 6.95    12.901 47.291 1   19.71 ? 21  LEU   A CA    1 
ATOM   148  C C     . LEU   A 1 40  ? 8.303   12.263 47.626 1   20.68 ? 21  LEU   A C     1 
ATOM   149  O O     . LEU   A 1 40  ? 9.288   12.976 47.834 1   21.15 ? 21  LEU   A O     1 
ATOM   150  C CB    . LEU   A 1 40  ? 6.036   12.827 48.498 1   20.94 ? 21  LEU   A CB    1 
ATOM   151  C CG    . LEU   A 1 40  ? 4.741   13.637 48.335 1   21.27 ? 21  LEU   A CG    1 
ATOM   152  C CD1   . LEU   A 1 40  ? 3.827   13.409 49.531 1   24.51 ? 21  LEU   A CD1   1 
ATOM   153  C CD2   . LEU   A 1 40  ? 5.042   15.124 48.114 1   22.48 ? 21  LEU   A CD2   1 
ATOM   154  N N     . GLU   A 1 41  ? 8.348   10.92  47.578 1   20.5  ? 22  GLU   A N     1 
ATOM   155  C CA    . GLU   A 1 41  ? 9.609   10.234 47.832 1   22.29 ? 22  GLU   A CA    1 
ATOM   156  C C     . GLU   A 1 41  ? 10.67   10.581 46.807 1   22.99 ? 22  GLU   A C     1 
ATOM   157  O O     . GLU   A 1 41  ? 11.834  10.722 47.156 1   24.78 ? 22  GLU   A O     1 
ATOM   158  C CB    . GLU   A 1 41  ? 9.36    8.713  47.842 1   25.6  ? 22  GLU   A CB    1 
ATOM   159  C CG    . GLU   A 1 41  ? 8.606   8.259  49.081 1   32.75 ? 22  GLU   A CG    1 
ATOM   160  C CD    . GLU   A 1 41  ? 9.38    8.519  50.369 1   41.38 ? 22  GLU   A CD    1 
ATOM   161  O OE1   . GLU   A 1 41  ? 8.761   9.018  51.334 1   41.39 ? 22  GLU   A OE1   1 
ATOM   162  O OE2   . GLU   A 1 41  ? 10.609  8.277  50.398 1   44.24 ? 22  GLU   A OE2   1 
ATOM   163  N N     . LYS   A 1 42  ? 10.283  10.684 45.521 1   21.92 ? 23  LYS   A N     1 
ATOM   164  C CA    . LYS   A 1 42  ? 11.246  10.933 44.461 1   21.37 ? 23  LYS   A CA    1 
ATOM   165  C C     . LYS   A 1 42  ? 11.771  12.358 44.42  1   20.14 ? 23  LYS   A C     1 
ATOM   166  O O     . LYS   A 1 42  ? 12.94   12.607 44.127 1   22.68 ? 23  LYS   A O     1 
ATOM   167  C CB    . LYS   A 1 42  ? 10.625  10.591 43.089 1   23.33 ? 23  LYS   A CB    1 
ATOM   168  C CG    . LYS   A 1 42  ? 10.983  9.197  42.589 1   32.29 ? 23  LYS   A CG    1 
ATOM   169  C CD    . LYS   A 1 42  ? 10.081  8.124  42.978 1   37.67 ? 23  LYS   A CD    1 
ATOM   170  C CE    . LYS   A 1 42  ? 10.756  6.793  42.651 1   37.11 ? 23  LYS   A CE    1 
ATOM   171  N NZ    . LYS   A 1 42  ? 10.549  5.846  43.762 1   37.02 ? 23  LYS   A NZ    1 
ATOM   172  N N     . TYR   A 1 43  ? 10.877  13.323 44.664 1   19.17 ? 24  TYR   A N     1 
ATOM   173  C CA    . TYR   A 1 43  ? 11.256  14.722 44.492 1   18.15 ? 24  TYR   A CA    1 
ATOM   174  C C     . TYR   A 1 43  ? 11.392  15.58  45.742 1   18.43 ? 24  TYR   A C     1 
ATOM   175  O O     . TYR   A 1 43  ? 12.017  16.659 45.662 1   19.19 ? 24  TYR   A O     1 
ATOM   176  C CB    . TYR   A 1 43  ? 10.185  15.393 43.553 1   17.03 ? 24  TYR   A CB    1 
ATOM   177  C CG    . TYR   A 1 43  ? 10.272  14.9   42.123 1   16.45 ? 24  TYR   A CG    1 
ATOM   178  C CD1   . TYR   A 1 43  ? 11.203  15.418 41.258 1   17.18 ? 24  TYR   A CD1   1 
ATOM   179  C CD2   . TYR   A 1 43  ? 9.429   13.891 41.658 1   16.81 ? 24  TYR   A CD2   1 
ATOM   180  C CE1   . TYR   A 1 43  ? 11.286  14.994 39.936 1   16.76 ? 24  TYR   A CE1   1 
ATOM   181  C CE2   . TYR   A 1 43  ? 9.495   13.445 40.345 1   16.41 ? 24  TYR   A CE2   1 
ATOM   182  C CZ    . TYR   A 1 43  ? 10.429  13.997 39.477 1   17    ? 24  TYR   A CZ    1 
ATOM   183  O OH    . TYR   A 1 43  ? 10.521  13.547 38.167 1   17.72 ? 24  TYR   A OH    1 
ATOM   184  N N     . TYR   A 1 44  ? 10.778  15.161 46.864 1   19.48 ? 25  TYR   A N     1 
ATOM   185  C CA    . TYR   A 1 44  ? 10.686  16.057 48.012 1   21.5  ? 25  TYR   A CA    1 
ATOM   186  C C     . TYR   A 1 44  ? 11.2    15.503 49.329 1   24.49 ? 25  TYR   A C     1 
ATOM   187  O O     . TYR   A 1 44  ? 10.881  16.063 50.376 1   24.83 ? 25  TYR   A O     1 
ATOM   188  C CB    . TYR   A 1 44  ? 9.214   16.526 48.147 1   20.02 ? 25  TYR   A CB    1 
ATOM   189  C CG    . TYR   A 1 44  ? 8.802   17.409 46.973 1   17.53 ? 25  TYR   A CG    1 
ATOM   190  C CD1   . TYR   A 1 44  ? 9.277   18.712 46.857 1   18.86 ? 25  TYR   A CD1   1 
ATOM   191  C CD2   . TYR   A 1 44  ? 8.035   16.896 45.921 1   18.18 ? 25  TYR   A CD2   1 
ATOM   192  C CE1   . TYR   A 1 44  ? 9.026   19.475 45.72  1   18.42 ? 25  TYR   A CE1   1 
ATOM   193  C CE2   . TYR   A 1 44  ? 7.742   17.67  44.803 1   17.11 ? 25  TYR   A CE2   1 
ATOM   194  C CZ    . TYR   A 1 44  ? 8.239   18.961 44.713 1   17.75 ? 25  TYR   A CZ    1 
ATOM   195  O OH    . TYR   A 1 44  ? 7.995   19.734 43.601 1   17.37 ? 25  TYR   A OH    1 
ATOM   196  N N     . LYS   A 1 45  ? 12      14.452 49.283 1   27.18 ? 26  LYS   A N     1 
ATOM   197  C CA    . LYS   A 1 45  ? 12.55   13.849 50.519 1   31.53 ? 26  LYS   A CA    1 
ATOM   198  C C     . LYS   A 1 45  ? 13.481  14.805 51.25  1   34.23 ? 26  LYS   A C     1 
ATOM   199  O O     . LYS   A 1 45  ? 13.538  14.793 52.499 1   35.75 ? 26  LYS   A O     1 
ATOM   200  C CB    . LYS   A 1 45  ? 13.23   12.528 50.18  1   35.12 ? 26  LYS   A CB    1 
ATOM   201  C CG    . LYS   A 1 45  ? 13.395  11.601 51.377 1   41.37 ? 26  LYS   A CG    1 
ATOM   202  C CD    . LYS   A 1 45  ? 13.643  10.176 50.924 1   48.41 ? 26  LYS   A CD    1 
ATOM   203  C CE    . LYS   A 1 45  ? 13.748  9.222  52.09  1   54.44 ? 26  LYS   A CE    1 
ATOM   204  N NZ    . LYS   A 1 45  ? 12.488  9.164  52.885 1   58.25 ? 26  LYS   A NZ    1 
ATOM   205  N N     . PHE   A 1 46  ? 14.218  15.633 50.488 1   33.94 ? 27  PHE   A N     1 
ATOM   206  C CA    . PHE   A 1 46  ? 15.096  16.677 51.032 1   35.79 ? 27  PHE   A CA    1 
ATOM   207  C C     . PHE   A 1 46  ? 16.1    16.107 52.03  1   38.82 ? 27  PHE   A C     1 
ATOM   208  O O     . PHE   A 1 46  ? 16.244  16.638 53.121 1   39.8  ? 27  PHE   A O     1 
ATOM   209  C CB    . PHE   A 1 46  ? 14.251  17.805 51.663 1   36.83 ? 27  PHE   A CB    1 
ATOM   210  C CG    . PHE   A 1 46  ? 14.859  19.187 51.662 1   38.24 ? 27  PHE   A CG    1 
ATOM   211  C CD1   . PHE   A 1 46  ? 15.316  19.761 50.488 1   39.02 ? 27  PHE   A CD1   1 
ATOM   212  C CD2   . PHE   A 1 46  ? 14.91   19.946 52.823 1   39.69 ? 27  PHE   A CD2   1 
ATOM   213  C CE1   . PHE   A 1 46  ? 15.784  21.075 50.47  1   39.78 ? 27  PHE   A CE1   1 
ATOM   214  C CE2   . PHE   A 1 46  ? 15.391  21.261 52.801 1   39.95 ? 27  PHE   A CE2   1 
ATOM   215  C CZ    . PHE   A 1 46  ? 15.828  21.81  51.626 1   39.97 ? 27  PHE   A CZ    1 
ATOM   216  N N     . GLY   A 1 47  ? 16.725  14.993 51.67  1   39.68 ? 28  GLY   A N     1 
ATOM   217  C CA    . GLY   A 1 47  ? 17.72   14.349 52.526 1   41.89 ? 28  GLY   A CA    1 
ATOM   218  C C     . GLY   A 1 47  ? 19.01   15.145 52.608 1   44.32 ? 28  GLY   A C     1 
ATOM   219  O O     . GLY   A 1 47  ? 19.168  16.163 51.92  1   45.72 ? 28  GLY   A O     1 
ATOM   220  N N     . SER   A 1 51  ? 21.307  16.652 46.185 1   29.14 ? 32  SER   A N     1 
ATOM   221  C CA    . SER   A 1 51  ? 20.798  16.158 44.891 1   27.55 ? 32  SER   A CA    1 
ATOM   222  C C     . SER   A 1 51  ? 20.292  17.322 44.047 1   24.57 ? 32  SER   A C     1 
ATOM   223  O O     . SER   A 1 51  ? 19.939  18.379 44.58  1   24.47 ? 32  SER   A O     1 
ATOM   224  C CB    . SER   A 1 51  ? 19.621  15.208 45.123 1   28.83 ? 32  SER   A CB    1 
ATOM   225  O OG    . SER   A 1 51  ? 18.533  15.931 45.689 1   28.36 ? 32  SER   A OG    1 
ATOM   226  N N     . ALA   A 1 52  ? 20.127  17.101 42.736 1   23.18 ? 33  ALA   A N     1 
ATOM   227  C CA    . ALA   A 1 52  ? 19.519  18.106 41.851 1   22.1  ? 33  ALA   A CA    1 
ATOM   228  C C     . ALA   A 1 52  ? 18.118  18.465 42.324 1   21.28 ? 33  ALA   A C     1 
ATOM   229  O O     . ALA   A 1 52  ? 17.757  19.642 42.351 1   21.31 ? 33  ALA   A O     1 
ATOM   230  C CB    . ALA   A 1 52  ? 19.458  17.59  40.417 1   22.72 ? 33  ALA   A CB    1 
ATOM   231  N N     . GLU   A 1 53  ? 17.33   17.46  42.737 1   20.71 ? 34  GLU   A N     1 
ATOM   232  C CA    . GLU   A 1 53  ? 15.979  17.718 43.225 1   19.77 ? 34  GLU   A CA    1 
ATOM   233  C C     . GLU   A 1 53  ? 15.956  18.619 44.442 1   19.42 ? 34  GLU   A C     1 
ATOM   234  O O     . GLU   A 1 53  ? 15.108  19.526 44.536 1   20.43 ? 34  GLU   A O     1 
ATOM   235  C CB    . GLU   A 1 53  ? 15.277  16.389 43.586 1   20.41 ? 34  GLU   A CB    1 
ATOM   236  C CG    . GLU   A 1 53  ? 14.899  15.532 42.389 1   22.65 ? 34  GLU   A CG    1 
ATOM   237  C CD    . GLU   A 1 53  ? 16.03   15.194 41.459 1   23.8  ? 34  GLU   A CD    1 
ATOM   238  O OE1   . GLU   A 1 53  ? 17.076  14.663 41.948 1   24.65 ? 34  GLU   A OE1   1 
ATOM   239  O OE2   . GLU   A 1 53  ? 15.9    15.492 40.25  1   23.62 ? 34  GLU   A OE2   1 
ATOM   240  N N     . SER   A 1 54  ? 16.904  18.41  45.396 1   20.94 ? 35  SER   A N     1 
ATOM   241  C CA    . SER   A 1 54  ? 16.92   19.244 46.576 1   22.14 ? 35  SER   A CA    1 
ATOM   242  C C     . SER   A 1 54  ? 17.44   20.632 46.256 1   20.45 ? 35  SER   A C     1 
ATOM   243  O O     . SER   A 1 54  ? 16.971  21.612 46.865 1   22.55 ? 35  SER   A O     1 
ATOM   244  C CB    . SER   A 1 54  ? 17.757  18.597 47.679 1   25.62 ? 35  SER   A CB    1 
ATOM   245  O OG    . SER   A 1 54  ? 17.101  17.408 48.102 1   30.39 ? 35  SER   A OG    1 
ATOM   246  N N     . GLN   A 1 55  ? 18.376  20.763 45.293 1   20.77 ? 36  GLN   A N     1 
ATOM   247  C CA    . GLN   A 1 55  ? 18.87   22.101 44.921 1   21.59 ? 36  GLN   A CA    1 
ATOM   248  C C     . GLN   A 1 55  ? 17.731  22.918 44.302 1   20.2  ? 36  GLN   A C     1 
ATOM   249  O O     . GLN   A 1 55  ? 17.588  24.121 44.607 1   21.05 ? 36  GLN   A O     1 
ATOM   250  C CB    . GLN   A 1 55  ? 20.037  21.987 43.93  1   23.62 ? 36  GLN   A CB    1 
ATOM   251  C CG    . GLN   A 1 55  ? 21.318  21.381 44.564 1   27.76 ? 36  GLN   A CG    1 
ATOM   252  C CD    . GLN   A 1 55  ? 21.785  22.241 45.712 1   32.9  ? 36  GLN   A CD    1 
ATOM   253  O OE1   . GLN   A 1 55  ? 21.606  21.901 46.888 1   35.61 ? 36  GLN   A OE1   1 
ATOM   254  N NE2   . GLN   A 1 55  ? 22.314  23.397 45.386 1   35.29 ? 36  GLN   A NE2   1 
ATOM   255  N N     . ILE   A 1 56  ? 16.912  22.271 43.456 1   18.93 ? 37  ILE   A N     1 
ATOM   256  C CA    . ILE   A 1 56  ? 15.774  22.987 42.857 1   18.1  ? 37  ILE   A CA    1 
ATOM   257  C C     . ILE   A 1 56  ? 14.771  23.353 43.924 1   17.88 ? 37  ILE   A C     1 
ATOM   258  O O     . ILE   A 1 56  ? 14.315  24.506 43.94  1   18.23 ? 37  ILE   A O     1 
ATOM   259  C CB    . ILE   A 1 56  ? 15.168  22.079 41.761 1   18.16 ? 37  ILE   A CB    1 
ATOM   260  C CG1   . ILE   A 1 56  ? 16.157  22.015 40.549 1   19.33 ? 37  ILE   A CG1   1 
ATOM   261  C CG2   . ILE   A 1 56  ? 13.76   22.552 41.364 1   18.59 ? 37  ILE   A CG2   1 
ATOM   262  C CD1   . ILE   A 1 56  ? 15.854  20.911 39.564 1   18.77 ? 37  ILE   A CD1   1 
ATOM   263  N N     . LEU   A 1 57  ? 14.465  22.415 44.856 1   18.71 ? 38  LEU   A N     1 
ATOM   264  C CA    . LEU   A 1 57  ? 13.544  22.721 45.962 1   19.5  ? 38  LEU   A CA    1 
ATOM   265  C C     . LEU   A 1 57  ? 14.016  23.946 46.782 1   19.51 ? 38  LEU   A C     1 
ATOM   266  O O     . LEU   A 1 57  ? 13.221  24.863 47.067 1   20.08 ? 38  LEU   A O     1 
ATOM   267  C CB    . LEU   A 1 57  ? 13.347  21.485 46.838 1   20.72 ? 38  LEU   A CB    1 
ATOM   268  C CG    . LEU   A 1 57  ? 12.451  21.639 48.045 1   23.23 ? 38  LEU   A CG    1 
ATOM   269  C CD1   . LEU   A 1 57  ? 11.055  22.27  47.672 1   23.28 ? 38  LEU   A CD1   1 
ATOM   270  C CD2   . LEU   A 1 57  ? 12.246  20.303 48.734 1   25    ? 38  LEU   A CD2   1 
ATOM   271  N N     . LYS   A 1 58  ? 15.304  24.014 47.12  1   20.21 ? 39  LYS   A N     1 
ATOM   272  C CA    . LYS   A 1 58  ? 15.832  25.156 47.856 1   20.5  ? 39  LYS   A CA    1 
ATOM   273  C C     . LYS   A 1 58  ? 15.621  26.452 47.085 1   20.66 ? 39  LYS   A C     1 
ATOM   274  O O     . LYS   A 1 58  ? 15.211  27.477 47.669 1   21.03 ? 39  LYS   A O     1 
ATOM   275  C CB    . LYS   A 1 58  ? 17.327  24.969 48.143 1   23.97 ? 39  LYS   A CB    1 
ATOM   276  C CG    . LYS   A 1 58  ? 17.574  23.863 49.159 1   28.76 ? 39  LYS   A CG    1 
ATOM   277  C CD    . LYS   A 1 58  ? 19.079  23.673 49.367 1   35.38 ? 39  LYS   A CD    1 
ATOM   278  C CE    . LYS   A 1 58  ? 19.418  22.275 49.794 1   43.39 ? 39  LYS   A CE    1 
ATOM   279  N NZ    . LYS   A 1 58  ? 20.893  22.098 49.895 1   48.74 ? 39  LYS   A NZ    1 
ATOM   280  N N     . HIS   A 1 59  ? 15.872  26.403 45.752 1   20.15 ? 40  HIS   A N     1 
ATOM   281  C CA    . HIS   A 1 59  ? 15.678  27.623 44.956 1   20.45 ? 40  HIS   A CA    1 
ATOM   282  C C     . HIS   A 1 59  ? 14.224  28.069 44.924 1   18.81 ? 40  HIS   A C     1 
ATOM   283  O O     . HIS   A 1 59  ? 13.942  29.253 45.135 1   19.67 ? 40  HIS   A O     1 
ATOM   284  C CB    . HIS   A 1 59  ? 16.251  27.514 43.546 1   21.14 ? 40  HIS   A CB    1 
ATOM   285  C CG    . HIS   A 1 59  ? 16.347  28.877 42.928 1   22.59 ? 40  HIS   A CG    1 
ATOM   286  N ND1   . HIS   A 1 59  ? 17.408  29.685 43.195 1   24.87 ? 40  HIS   A ND1   1 
ATOM   287  C CD2   . HIS   A 1 59  ? 15.406  29.597 42.257 1   24.31 ? 40  HIS   A CD2   1 
ATOM   288  C CE1   . HIS   A 1 59  ? 17.134  30.849 42.601 1   26.52 ? 40  HIS   A CE1   1 
ATOM   289  N NE2   . HIS   A 1 59  ? 15.956  30.827 42.016 1   26.56 ? 40  HIS   A NE2   1 
ATOM   290  N N     . LEU   A 1 60  ? 13.283  27.099 44.741 1   18.56 ? 41  LEU   A N     1 
ATOM   291  C CA    . LEU   A 1 60  ? 11.859  27.422 44.76  1   19.03 ? 41  LEU   A CA    1 
ATOM   292  C C     . LEU   A 1 60  ? 11.475  28.056 46.101 1   17.97 ? 41  LEU   A C     1 
ATOM   293  O O     . LEU   A 1 60  ? 10.804  29.097 46.127 1   18.11 ? 41  LEU   A O     1 
ATOM   294  C CB    . LEU   A 1 60  ? 11.042  26.144 44.541 1   20.65 ? 41  LEU   A CB    1 
ATOM   295  C CG    . LEU   A 1 60  ? 11.254  25.496 43.166 1   23.29 ? 41  LEU   A CG    1 
ATOM   296  C CD1   . LEU   A 1 60  ? 10.478  24.169 43.069 1   24.22 ? 41  LEU   A CD1   1 
ATOM   297  C CD2   . LEU   A 1 60  ? 10.722  26.405 42.074 1   27.07 ? 41  LEU   A CD2   1 
ATOM   298  N N     . LEU   A 1 61  ? 11.978  27.485 47.214 1   19.09 ? 42  LEU   A N     1 
ATOM   299  C CA    . LEU   A 1 61  ? 11.653  28.046 48.545 1   18.64 ? 42  LEU   A CA    1 
ATOM   300  C C     . LEU   A 1 61  ? 12.18   29.472 48.746 1   17.45 ? 42  LEU   A C     1 
ATOM   301  O O     . LEU   A 1 61  ? 11.48   30.323 49.32  1   19.67 ? 42  LEU   A O     1 
ATOM   302  C CB    . LEU   A 1 61  ? 12.15   27.108 49.638 1   19.54 ? 42  LEU   A CB    1 
ATOM   303  C CG    . LEU   A 1 61  ? 11.431  25.743 49.673 1   21.53 ? 42  LEU   A CG    1 
ATOM   304  C CD1   . LEU   A 1 61  ? 12.206  24.781 50.597 1   23.12 ? 42  LEU   A CD1   1 
ATOM   305  C CD2   . LEU   A 1 61  ? 9.981   25.927 50.081 1   21.74 ? 42  LEU   A CD2   1 
ATOM   306  N N     . LYS   A 1 62  ? 13.375  29.748 48.241 1   18.47 ? 43  LYS   A N     1 
ATOM   307  C CA    . LYS   A 1 62  ? 13.929  31.107 48.365 1   19.06 ? 43  LYS   A CA    1 
ATOM   308  C C     . LYS   A 1 62  ? 13.055  32.11  47.566 1   19.55 ? 43  LYS   A C     1 
ATOM   309  O O     . LYS   A 1 62  ? 12.727  33.216 48.047 1   20.21 ? 43  LYS   A O     1 
ATOM   310  C CB    . LYS   A 1 62  ? 15.377  31.17  47.877 1   20.65 ? 43  LYS   A CB    1 
ATOM   311  C CG    . LYS   A 1 62  ? 16.295  30.41  48.829 1   23.33 ? 43  LYS   A CG    1 
ATOM   312  C CD    . LYS   A 1 62  ? 17.711  30.448 48.336 1   31.02 ? 43  LYS   A CD    1 
ATOM   313  C CE    . LYS   A 1 62  ? 18.347  29.095 48.267 1   37.7  ? 43  LYS   A CE    1 
ATOM   314  N NZ    . LYS   A 1 62  ? 19.778  29.23  47.841 1   42.65 ? 43  LYS   A NZ    1 
ATOM   315  N N     . ASN   A 1 63  ? 12.602  31.695 46.349 1   18.97 ? 44  ASN   A N     1 
ATOM   316  C CA    . ASN   A 1 63  ? 11.75   32.6   45.564 1   18.32 ? 44  ASN   A CA    1 
ATOM   317  C C     . ASN   A 1 63  ? 10.405  32.796 46.213 1   19.15 ? 44  ASN   A C     1 
ATOM   318  O O     . ASN   A 1 63  ? 9.877   33.924 46.226 1   19.61 ? 44  ASN   A O     1 
ATOM   319  C CB    . ASN   A 1 63  ? 11.606  32.025 44.127 1   20.53 ? 44  ASN   A CB    1 
ATOM   320  C CG    . ASN   A 1 63  ? 12.758  32.373 43.232 1   22.39 ? 44  ASN   A CG    1 
ATOM   321  O OD1   . ASN   A 1 63  ? 13.686  33.098 43.634 1   26.56 ? 44  ASN   A OD1   1 
ATOM   322  N ND2   . ASN   A 1 63  ? 12.714  31.909 42.006 1   22.8  ? 44  ASN   A ND2   1 
ATOM   323  N N     . LEU   A 1 64  ? 9.814   31.736 46.763 1   18.18 ? 45  LEU   A N     1 
ATOM   324  C CA    . LEU   A 1 64  ? 8.505   31.873 47.409 1   19.07 ? 45  LEU   A CA    1 
ATOM   325  C C     . LEU   A 1 64  ? 8.595   32.802 48.615 1   20.13 ? 45  LEU   A C     1 
ATOM   326  O O     . LEU   A 1 64  ? 7.682   33.604 48.864 1   20.63 ? 45  LEU   A O     1 
ATOM   327  C CB    . LEU   A 1 64  ? 7.936   30.52  47.792 1   19.07 ? 45  LEU   A CB    1 
ATOM   328  C CG    . LEU   A 1 64  ? 7.639   29.666 46.541 1   19.23 ? 45  LEU   A CG    1 
ATOM   329  C CD1   . LEU   A 1 64  ? 7.634   28.189 46.927 1   20.91 ? 45  LEU   A CD1   1 
ATOM   330  C CD2   . LEU   A 1 64  ? 6.304   30.056 45.907 1   20.2  ? 45  LEU   A CD2   1 
ATOM   331  N N     . PHE   A 1 65  ? 9.692   32.7   49.366 1   20.53 ? 46  PHE   A N     1 
ATOM   332  C CA    . PHE   A 1 65  ? 9.927   33.584 50.51  1   21.44 ? 46  PHE   A CA    1 
ATOM   333  C C     . PHE   A 1 65  ? 10.05   35.033 50.036 1   21.58 ? 46  PHE   A C     1 
ATOM   334  O O     . PHE   A 1 65  ? 9.356   35.925 50.565 1   21.34 ? 46  PHE   A O     1 
ATOM   335  C CB    . PHE   A 1 65  ? 11.185  33.122 51.248 1   22.94 ? 46  PHE   A CB    1 
ATOM   336  C CG    . PHE   A 1 65  ? 11.606  34.128 52.282 1   26.5  ? 46  PHE   A CG    1 
ATOM   337  C CD1   . PHE   A 1 65  ? 10.755  34.479 53.31  1   29.17 ? 46  PHE   A CD1   1 
ATOM   338  C CD2   . PHE   A 1 65  ? 12.79   34.81  52.153 1   29.45 ? 46  PHE   A CD2   1 
ATOM   339  C CE1   . PHE   A 1 65  ? 11.126  35.452 54.244 1   31.87 ? 46  PHE   A CE1   1 
ATOM   340  C CE2   . PHE   A 1 65  ? 13.162  35.775 53.095 1   31.32 ? 46  PHE   A CE2   1 
ATOM   341  C CZ    . PHE   A 1 65  ? 12.318  36.089 54.12  1   31.09 ? 46  PHE   A CZ    1 
ATOM   342  N N     . LYS   A 1 66  ? 10.797  35.272 48.989 1   19.92 ? 47  LYS   A N     1 
ATOM   343  C CA    . LYS   A 1 66  ? 10.924  36.619 48.455 1   21.24 ? 47  LYS   A CA    1 
ATOM   344  C C     . LYS   A 1 66  ? 9.553   37.186 48.047 1   21.69 ? 47  LYS   A C     1 
ATOM   345  O O     . LYS   A 1 66  ? 9.198   38.285 48.438 1   23.2  ? 47  LYS   A O     1 
ATOM   346  C CB    . LYS   A 1 66  ? 11.912  36.665 47.322 1   21.32 ? 47  LYS   A CB    1 
ATOM   347  C CG    . LYS   A 1 66  ? 11.937  38.073 46.708 1   25.44 ? 47  LYS   A CG    1 
ATOM   348  C CD    . LYS   A 1 66  ? 13.084  38.345 45.782 1   27.11 ? 47  LYS   A CD    1 
ATOM   349  C CE    . LYS   A 1 66  ? 12.867  39.695 45.093 1   30.12 ? 47  LYS   A CE    1 
ATOM   350  N NZ    . LYS   A 1 66  ? 11.661  39.727 44.186 1   33.21 ? 47  LYS   A NZ    1 
ATOM   351  N N     . ILE   A 1 67  ? 8.758   36.401 47.319 1   19.59 ? 48  ILE   A N     1 
ATOM   352  C CA    . ILE   A 1 67  ? 7.462   36.882 46.851 1   19.01 ? 48  ILE   A CA    1 
ATOM   353  C C     . ILE   A 1 67  ? 6.479   37.178 47.957 1   20.92 ? 48  ILE   A C     1 
ATOM   354  O O     . ILE   A 1 67  ? 5.86    38.262 47.967 1   21.92 ? 48  ILE   A O     1 
ATOM   355  C CB    . ILE   A 1 67  ? 6.922   35.808 45.867 1   19.98 ? 48  ILE   A CB    1 
ATOM   356  C CG1   . ILE   A 1 67  ? 7.821   35.736 44.633 1   20.32 ? 48  ILE   A CG1   1 
ATOM   357  C CG2   . ILE   A 1 67  ? 5.484   36.088 45.458 1   21.63 ? 48  ILE   A CG2   1 
ATOM   358  C CD1   . ILE   A 1 67  ? 7.571   34.46  43.751 1   22.04 ? 48  ILE   A CD1   1 
ATOM   359  N N     . PHE   A 1 68  ? 6.287   36.229 48.899 1   20.56 ? 49  PHE   A N     1 
ATOM   360  C CA    . PHE   A 1 68  ? 5.208   36.386 49.895 1   23.79 ? 49  PHE   A CA    1 
ATOM   361  C C     . PHE   A 1 68  ? 5.613   37.15  51.116 1   26.23 ? 49  PHE   A C     1 
ATOM   362  O O     . PHE   A 1 68  ? 4.754   37.785 51.751 1   29.24 ? 49  PHE   A O     1 
ATOM   363  C CB    . PHE   A 1 68  ? 4.633   35.015 50.267 1   23.65 ? 49  PHE   A CB    1 
ATOM   364  C CG    . PHE   A 1 68  ? 3.993   34.347 49.062 1   22.86 ? 49  PHE   A CG    1 
ATOM   365  C CD1   . PHE   A 1 68  ? 2.968   34.965 48.369 1   22.93 ? 49  PHE   A CD1   1 
ATOM   366  C CD2   . PHE   A 1 68  ? 4.4     33.084 48.644 1   23.66 ? 49  PHE   A CD2   1 
ATOM   367  C CE1   . PHE   A 1 68  ? 2.39    34.36  47.265 1   23.44 ? 49  PHE   A CE1   1 
ATOM   368  C CE2   . PHE   A 1 68  ? 3.84    32.497 47.514 1   24.79 ? 49  PHE   A CE2   1 
ATOM   369  C CZ    . PHE   A 1 68  ? 2.841   33.141 46.826 1   24.6  ? 49  PHE   A CZ    1 
ATOM   370  N N     . CYS   A 1 69  ? 6.898   37.099 51.476 1   24.35 ? 50  CYS   A N     1 
ATOM   371  C CA    . CYS   A 1 69  ? 7.314   37.793 52.68  1   25.86 ? 50  CYS   A CA    1 
ATOM   372  C C     . CYS   A 1 69  ? 8.028   39.115 52.419 1   26.59 ? 50  CYS   A C     1 
ATOM   373  O O     . CYS   A 1 69  ? 7.936   40.005 53.263 1   28.71 ? 50  CYS   A O     1 
ATOM   374  C CB    . CYS   A 1 69  ? 8.136   36.861 53.552 1   27.12 ? 50  CYS   A CB    1 
ATOM   375  S SG    . CYS   A 1 69  ? 7.259   35.324 54.003 1   36.58 ? 50  CYS   A SG    1 
ATOM   376  N N     . LEU   A 1 70  ? 8.781   39.228 51.323 1   26.29 ? 51  LEU   A N     1 
ATOM   377  C CA    . LEU   A 1 70  ? 9.521   40.469 51.08  1   25.67 ? 51  LEU   A CA    1 
ATOM   378  C C     . LEU   A 1 70  ? 8.798   41.399 50.147 1   27    ? 51  LEU   A C     1 
ATOM   379  O O     . LEU   A 1 70  ? 8.809   42.613 50.346 1   27.49 ? 51  LEU   A O     1 
ATOM   380  C CB    . LEU   A 1 70  ? 10.92   40.153 50.56  1   25.51 ? 51  LEU   A CB    1 
ATOM   381  C CG    . LEU   A 1 70  ? 11.717  39.222 51.448 1   25.85 ? 51  LEU   A CG    1 
ATOM   382  C CD1   . LEU   A 1 70  ? 13.115  39.013 50.899 1   26.87 ? 51  LEU   A CD1   1 
ATOM   383  C CD2   . LEU   A 1 70  ? 11.77   39.737 52.94  1   26.88 ? 51  LEU   A CD2   1 
ATOM   384  N N     . ASP   A 1 71  ? 8.247   40.855 49.079 1   27.71 ? 52  ASP   A N     1 
ATOM   385  C CA    . ASP   A 1 71  ? 7.507   41.626 48.108 1   29.38 ? 52  ASP   A CA    1 
ATOM   386  C C     . ASP   A 1 71  ? 6.094   41.798 48.744 1   34.51 ? 52  ASP   A C     1 
ATOM   387  O O     . ASP   A 1 71  ? 5.789   41.179 49.771 1   37.3  ? 52  ASP   A O     1 
ATOM   388  C CB    . ASP   A 1 71  ? 7.512   40.899 46.728 1   27.69 ? 52  ASP   A CB    1 
ATOM   389  C CG    . ASP   A 1 71  ? 8.913   40.665 46.16  1   29.4  ? 52  ASP   A CG    1 
ATOM   390  O OD1   . ASP   A 1 71  ? 9.854   41.353 46.61  1   28.96 ? 52  ASP   A OD1   1 
ATOM   391  O OD2   . ASP   A 1 71  ? 9.059   39.802 45.259 1   30.77 ? 52  ASP   A OD2   1 
ATOM   392  N N     . GLY   A 1 72  ? 5.271   42.636 48.169 1   35.9  ? 53  GLY   A N     1 
ATOM   393  C CA    . GLY   A 1 72  ? 3.924   42.87  48.717 1   35.45 ? 53  GLY   A CA    1 
ATOM   394  C C     . GLY   A 1 72  ? 2.835   41.864 48.383 1   34.11 ? 53  GLY   A C     1 
ATOM   395  O O     . GLY   A 1 72  ? 1.657   42.228 48.452 1   35.04 ? 53  GLY   A O     1 
ATOM   396  N N     . VAL   A 1 73  ? 3.187   40.595 48.056 1   31.65 ? 54  VAL   A N     1 
ATOM   397  C CA    . VAL   A 1 73  ? 2.154   39.647 47.668 1   29.51 ? 54  VAL   A CA    1 
ATOM   398  C C     . VAL   A 1 73  ? 1.444   39.106 48.898 1   29.57 ? 54  VAL   A C     1 
ATOM   399  O O     . VAL   A 1 73  ? 1.919   38.176 49.57  1   29.64 ? 54  VAL   A O     1 
ATOM   400  C CB    . VAL   A 1 73  ? 2.693   38.563 46.712 1   28.74 ? 54  VAL   A CB    1 
ATOM   401  C CG1   . VAL   A 1 73  ? 1.532   37.736 46.192 1   28.56 ? 54  VAL   A CG1   1 
ATOM   402  C CG2   . VAL   A 1 73  ? 3.432   39.21  45.533 1   29.3  ? 54  VAL   A CG2   1 
ATOM   403  N N     . LYS   A 1 74  ? 0.259   39.668 49.168 1   28.7  ? 55  LYS   A N     1 
ATOM   404  C CA    . LYS   A 1 74  ? -0.504  39.365 50.353 1   28.39 ? 55  LYS   A CA    1 
ATOM   405  C C     . LYS   A 1 74  ? -1.996  39.516 50.063 1   28.13 ? 55  LYS   A C     1 
ATOM   406  O O     . LYS   A 1 74  ? -2.386  40.027 48.997 1   28.38 ? 55  LYS   A O     1 
ATOM   407  C CB    . LYS   A 1 74  ? -0.09   40.362 51.455 1   29.84 ? 55  LYS   A CB    1 
ATOM   408  C CG    . LYS   A 1 74  ? -0.433  41.782 51.057 1   33.54 ? 55  LYS   A CG    1 
ATOM   409  C CD    . LYS   A 1 74  ? 0.049   42.794 52.063 1   38.11 ? 55  LYS   A CD    1 
ATOM   410  C CE    . LYS   A 1 74  ? 0.448   44.049 51.33  1   41.73 ? 55  LYS   A CE    1 
ATOM   411  N NZ    . LYS   A 1 74  ? 0.386   45.238 52.215 1   41.39 ? 55  LYS   A NZ    1 
ATOM   412  N N     . GLY   A 1 75  ? -2.813  39.108 51.016 1   28.76 ? 56  GLY   A N     1 
ATOM   413  C CA    . GLY   A 1 75  ? -4.243  39.272 50.856 1   30.5  ? 56  GLY   A CA    1 
ATOM   414  C C     . GLY   A 1 75  ? -5.093  38.347 51.658 1   31.27 ? 56  GLY   A C     1 
ATOM   415  O O     . GLY   A 1 75  ? -4.627  37.645 52.557 1   32.14 ? 56  GLY   A O     1 
ATOM   416  N N     . ASP   A 1 76  ? -6.365  38.363 51.327 1   30.27 ? 57  ASP   A N     1 
ATOM   417  C CA    . ASP   A 1 76  ? -7.33   37.531 52.002 1   30.65 ? 57  ASP   A CA    1 
ATOM   418  C C     . ASP   A 1 76  ? -7.342  36.127 51.431 1   30.02 ? 57  ASP   A C     1 
ATOM   419  O O     . ASP   A 1 76  ? -7.616  35.189 52.179 1   31.66 ? 57  ASP   A O     1 
ATOM   420  C CB    . ASP   A 1 76  ? -8.734  38.122 51.83  1   33.54 ? 57  ASP   A CB    1 
ATOM   421  C CG    . ASP   A 1 76  ? -8.997  39.369 52.648 1   42.78 ? 57  ASP   A CG    1 
ATOM   422  O OD1   . ASP   A 1 76  ? -8.202  39.654 53.565 1   44.63 ? 57  ASP   A OD1   1 
ATOM   423  O OD2   . ASP   A 1 76  ? -10.006 40.047 52.376 1   46.95 ? 57  ASP   A OD2   1 
ATOM   424  N N     . LEU   A 1 77  ? -7.059  35.968 50.102 1   28.91 ? 58  LEU   A N     1 
ATOM   425  C CA    . LEU   A 1 77  ? -7.165  34.672 49.495 1   26.4  ? 58  LEU   A CA    1 
ATOM   426  C C     . LEU   A 1 77  ? -6.096  34.418 48.427 1   23.66 ? 58  LEU   A C     1 
ATOM   427  O O     . LEU   A 1 77  ? -5.925  35.207 47.482 1   22.93 ? 58  LEU   A O     1 
ATOM   428  C CB    . LEU   A 1 77  ? -8.543  34.592 48.825 1   27.29 ? 58  LEU   A CB    1 
ATOM   429  C CG    . LEU   A 1 77  ? -8.849  33.318 48.057 1   28.31 ? 58  LEU   A CG    1 
ATOM   430  C CD1   . LEU   A 1 77  ? -8.866  32.083 49.004 1   30.34 ? 58  LEU   A CD1   1 
ATOM   431  C CD2   . LEU   A 1 77  ? -10.19  33.423 47.349 1   31.08 ? 58  LEU   A CD2   1 
ATOM   432  N N     . LEU   A 1 78  ? -5.452  33.25  48.55  1   22.31 ? 59  LEU   A N     1 
ATOM   433  C CA    . LEU   A 1 78  ? -4.532  32.741 47.544 1   21.71 ? 59  LEU   A CA    1 
ATOM   434  C C     . LEU   A 1 78  ? -5.103  31.403 47.137 1   21.67 ? 59  LEU   A C     1 
ATOM   435  O O     . LEU   A 1 78  ? -5.492  30.604 47.996 1   22.79 ? 59  LEU   A O     1 
ATOM   436  C CB    . LEU   A 1 78  ? -3.127  32.532 48.137 1   21.09 ? 59  LEU   A CB    1 
ATOM   437  C CG    . LEU   A 1 78  ? -2.091  31.863 47.159 1   21.71 ? 59  LEU   A CG    1 
ATOM   438  C CD1   . LEU   A 1 78  ? -0.707  32.42  47.398 1   23.41 ? 59  LEU   A CD1   1 
ATOM   439  C CD2   . LEU   A 1 78  ? -2.029  30.389 47.346 1   24.62 ? 59  LEU   A CD2   1 
ATOM   440  N N     . ILE   A 1 79  ? -5.14   31.155 45.814 1   20.75 ? 60  ILE   A N     1 
ATOM   441  C CA    . ILE   A 1 79  ? -5.527  29.858 45.302 1   20.78 ? 60  ILE   A CA    1 
ATOM   442  C C     . ILE   A 1 79  ? -4.251  29.235 44.715 1   19.96 ? 60  ILE   A C     1 
ATOM   443  O O     . ILE   A 1 79  ? -3.601  29.836 43.859 1   18.85 ? 60  ILE   A O     1 
ATOM   444  C CB    . ILE   A 1 79  ? -6.594  29.969 44.206 1   22.8  ? 60  ILE   A CB    1 
ATOM   445  C CG1   . ILE   A 1 79  ? -7.882  30.604 44.775 1   25.12 ? 60  ILE   A CG1   1 
ATOM   446  C CG2   . ILE   A 1 79  ? -6.914  28.557 43.679 1   23.23 ? 60  ILE   A CG2   1 
ATOM   447  C CD1   . ILE   A 1 79  ? -8.904  30.996 43.638 1   27.08 ? 60  ILE   A CD1   1 
ATOM   448  N N     . ASP   A 1 80  ? -3.922  28.007 45.171 1   18.89 ? 61  ASP   A N     1 
ATOM   449  C CA    . ASP   A 1 80  ? -2.785  27.242 44.647 1   18.6  ? 61  ASP   A CA    1 
ATOM   450  C C     . ASP   A 1 80  ? -3.352  26.238 43.682 1   19.21 ? 61  ASP   A C     1 
ATOM   451  O O     . ASP   A 1 80  ? -4.282  25.458 44.023 1   20.33 ? 61  ASP   A O     1 
ATOM   452  C CB    . ASP   A 1 80  ? -2.063  26.523 45.789 1   18.99 ? 61  ASP   A CB    1 
ATOM   453  C CG    . ASP   A 1 80  ? -0.836  25.768 45.283 1   24.59 ? 61  ASP   A CG    1 
ATOM   454  O OD1   . ASP   A 1 80  ? -0.151  26.274 44.34  1   23.08 ? 61  ASP   A OD1   1 
ATOM   455  O OD2   . ASP   A 1 80  ? -0.575  24.664 45.792 1   23.95 ? 61  ASP   A OD2   1 
ATOM   456  N N     . ILE   A 1 81  ? -2.898  26.283 42.449 1   18.4  ? 62  ILE   A N     1 
ATOM   457  C CA    . ILE   A 1 81  ? -3.415  25.501 41.317 1   18.93 ? 62  ILE   A CA    1 
ATOM   458  C C     . ILE   A 1 81  ? -2.519  24.366 40.993 1   17.68 ? 62  ILE   A C     1 
ATOM   459  O O     . ILE   A 1 81  ? -1.319  24.568 40.786 1   18.21 ? 62  ILE   A O     1 
ATOM   460  C CB    . ILE   A 1 81  ? -3.555  26.443 40.088 1   20.58 ? 62  ILE   A CB    1 
ATOM   461  C CG1   . ILE   A 1 81  ? -4.614  27.555 40.335 1   21.93 ? 62  ILE   A CG1   1 
ATOM   462  C CG2   . ILE   A 1 81  ? -3.822  25.692 38.772 1   20.31 ? 62  ILE   A CG2   1 
ATOM   463  C CD1   . ILE   A 1 81  ? -6.044  27.051 40.326 1   24.19 ? 62  ILE   A CD1   1 
ATOM   464  N N     . GLY   A 1 82  ? -3.06   23.146 41.002 1   16.82 ? 63  GLY   A N     1 
ATOM   465  C CA    . GLY   A 1 82  ? -2.233  21.984 40.699 1   16.07 ? 63  GLY   A CA    1 
ATOM   466  C C     . GLY   A 1 82  ? -1.242  21.686 41.805 1   16.12 ? 63  GLY   A C     1 
ATOM   467  O O     . GLY   A 1 82  ? -0.079  21.331 41.539 1   16.02 ? 63  GLY   A O     1 
ATOM   468  N N     . SER   A 1 83  ? -1.696  21.796 43.066 1   15.61 ? 64  SER   A N     1 
ATOM   469  C CA    . SER   A 1 83  ? -0.894  21.596 44.261 1   16.85 ? 64  SER   A CA    1 
ATOM   470  C C     . SER   A 1 83  ? -0.304  20.193 44.332 1   17.83 ? 64  SER   A C     1 
ATOM   471  O O     . SER   A 1 83  ? 0.655   19.974 45.074 1   18.37 ? 64  SER   A O     1 
ATOM   472  C CB    . SER   A 1 83  ? -1.781  21.76  45.501 1   19.35 ? 64  SER   A CB    1 
ATOM   473  O OG    . SER   A 1 83  ? -2.571  22.95  45.507 1   21.07 ? 64  SER   A OG    1 
ATOM   474  N N     . GLY   A 1 84  ? -0.948  19.221 43.686 1   17    ? 65  GLY   A N     1 
ATOM   475  C CA    . GLY   A 1 84  ? -0.523  17.823 43.853 1   17.68 ? 65  GLY   A CA    1 
ATOM   476  C C     . GLY   A 1 84  ? -0.629  17.47  45.337 1   17.64 ? 65  GLY   A C     1 
ATOM   477  O O     . GLY   A 1 84  ? -1.482  17.99  46.059 1   18.45 ? 65  GLY   A O     1 
ATOM   478  N N     . PRO   A 1 85  ? 0.301   16.628 45.789 1   17.17 ? 66  PRO   A N     1 
ATOM   479  C CA    . PRO   A 1 85  ? 0.326   16.277 47.204 1   17.67 ? 66  PRO   A CA    1 
ATOM   480  C C     . PRO   A 1 85  ? 1.316   17.131 47.991 1   19.47 ? 66  PRO   A C     1 
ATOM   481  O O     . PRO   A 1 85  ? 1.721   16.693 49.084 1   20.53 ? 66  PRO   A O     1 
ATOM   482  C CB    . PRO   A 1 85  ? 0.811   14.831 47.162 1   18.06 ? 66  PRO   A CB    1 
ATOM   483  C CG    . PRO   A 1 85  ? 1.835   14.851 46.008 1   18.26 ? 66  PRO   A CG    1 
ATOM   484  C CD    . PRO   A 1 85  ? 1.305   15.882 45     1   16.94 ? 66  PRO   A CD    1 
ATOM   485  N N     . THR   A 1 86  ? 1.762   18.286 47.449 1   17.64 ? 67  THR   A N     1 
ATOM   486  C CA    . THR   A 1 86  ? 2.801   19.041 48.134 1   17.88 ? 67  THR   A CA    1 
ATOM   487  C C     . THR   A 1 86  ? 2.295   20.252 48.897 1   19.02 ? 67  THR   A C     1 
ATOM   488  O O     . THR   A 1 86  ? 1.309   20.888 48.505 1   20.75 ? 67  THR   A O     1 
ATOM   489  C CB    . THR   A 1 86  ? 3.949   19.445 47.17  1   19.01 ? 67  THR   A CB    1 
ATOM   490  O OG1   . THR   A 1 86  ? 3.461   20.451 46.265 1   18.81 ? 67  THR   A OG1   1 
ATOM   491  C CG2   . THR   A 1 86  ? 4.413   18.266 46.296 1   19.05 ? 67  THR   A CG2   1 
ATOM   492  N N     . ILE   A 1 87  ? 3.052   20.61  49.937 1   19.52 ? 68  ILE   A N     1 
ATOM   493  C CA    . ILE   A 1 87  ? 2.739   21.83  50.698 1   19.97 ? 68  ILE   A CA    1 
ATOM   494  C C     . ILE   A 1 87  ? 3.918   22.798 50.736 1   19.74 ? 68  ILE   A C     1 
ATOM   495  O O     . ILE   A 1 87  ? 3.769   23.878 51.282 1   20.13 ? 68  ILE   A O     1 
ATOM   496  C CB    . ILE   A 1 87  ? 2.239   21.519 52.14  1   22.11 ? 68  ILE   A CB    1 
ATOM   497  C CG1   . ILE   A 1 87  ? 3.308   20.749 52.916 1   25.37 ? 68  ILE   A CG1   1 
ATOM   498  C CG2   . ILE   A 1 87  ? 0.929   20.71  52.098 1   23.43 ? 68  ILE   A CG2   1 
ATOM   499  C CD1   . ILE   A 1 87  ? 4.27    21.524 53.649 1   28.73 ? 68  ILE   A CD1   1 
ATOM   500  N N     . TYR   A 1 88  ? 5.111   22.435 50.193 1   19.09 ? 69  TYR   A N     1 
ATOM   501  C CA    . TYR   A 1 88  ? 6.269   23.317 50.267 1   20.07 ? 69  TYR   A CA    1 
ATOM   502  C C     . TYR   A 1 88  ? 5.988   24.711 49.71  1   19.28 ? 69  TYR   A C     1 
ATOM   503  O O     . TYR   A 1 88  ? 6.507   25.714 50.202 1   19.82 ? 69  TYR   A O     1 
ATOM   504  C CB    . TYR   A 1 88  ? 7.499   22.682 49.582 1   19.69 ? 69  TYR   A CB    1 
ATOM   505  C CG    . TYR   A 1 88  ? 7.448   22.799 48.064 1   18.71 ? 69  TYR   A CG    1 
ATOM   506  C CD1   . TYR   A 1 88  ? 7.957   23.923 47.414 1   18.14 ? 69  TYR   A CD1   1 
ATOM   507  C CD2   . TYR   A 1 88  ? 6.845   21.811 47.288 1   19.17 ? 69  TYR   A CD2   1 
ATOM   508  C CE1   . TYR   A 1 88  ? 7.86    24.068 46.037 1   17.65 ? 69  TYR   A CE1   1 
ATOM   509  C CE2   . TYR   A 1 88  ? 6.719   21.951 45.905 1   18.18 ? 69  TYR   A CE2   1 
ATOM   510  C CZ    . TYR   A 1 88  ? 7.257   23.068 45.273 1   17.51 ? 69  TYR   A CZ    1 
ATOM   511  O OH    . TYR   A 1 88  ? 7.152   23.225 43.904 1   17.12 ? 69  TYR   A OH    1 
ATOM   512  N N     . GLN   A 1 89  ? 5.161   24.76  48.655 1   18.16 ? 70  GLN   A N     1 
ATOM   513  C CA    . GLN   A 1 89  ? 4.901   26.015 47.972 1   19.01 ? 70  GLN   A CA    1 
ATOM   514  C C     . GLN   A 1 89  ? 3.966   26.948 48.749 1   19.25 ? 70  GLN   A C     1 
ATOM   515  O O     . GLN   A 1 89  ? 3.731   28.071 48.304 1   19.3  ? 70  GLN   A O     1 
ATOM   516  C CB    . GLN   A 1 89  ? 4.354   25.727 46.527 1   18.45 ? 70  GLN   A CB    1 
ATOM   517  C CG    . GLN   A 1 89  ? 2.927   25.178 46.435 1   19.12 ? 70  GLN   A CG    1 
ATOM   518  C CD    . GLN   A 1 89  ? 2.799   23.671 46.647 1   20.36 ? 70  GLN   A CD    1 
ATOM   519  O OE1   . GLN   A 1 89  ? 3.648   22.99  47.206 1   19.2  ? 70  GLN   A OE1   1 
ATOM   520  N NE2   . GLN   A 1 89  ? 1.689   23.087 46.189 1   22.98 ? 70  GLN   A NE2   1 
ATOM   521  N N     . LEU   A 1 90  ? 3.481   26.524 49.917 1   19.16 ? 71  LEU   A N     1 
ATOM   522  C CA    . LEU   A 1 90  ? 2.545   27.295 50.757 1   20.51 ? 71  LEU   A CA    1 
ATOM   523  C C     . LEU   A 1 90  ? 3.141   27.782 52.059 1   22.73 ? 71  LEU   A C     1 
ATOM   524  O O     . LEU   A 1 90  ? 2.457   28.51  52.793 1   23.61 ? 71  LEU   A O     1 
ATOM   525  C CB    . LEU   A 1 90  ? 1.361   26.383 51.133 1   20.49 ? 71  LEU   A CB    1 
ATOM   526  C CG    . LEU   A 1 90  ? 0.729   25.62  49.947 1   22.38 ? 71  LEU   A CG    1 
ATOM   527  C CD1   . LEU   A 1 90  ? -0.318  24.617 50.459 1   24.79 ? 71  LEU   A CD1   1 
ATOM   528  C CD2   . LEU   A 1 90  ? 0.18    26.59  48.903 1   23.72 ? 71  LEU   A CD2   1 
ATOM   529  N N     . LEU   A 1 91  ? 4.357   27.361 52.387 1   21.2  ? 72  LEU   A N     1 
ATOM   530  C CA    . LEU   A 1 91  ? 4.923   27.65  53.696 1   22.85 ? 72  LEU   A CA    1 
ATOM   531  C C     . LEU   A 1 91  ? 5.199   29.128 53.932 1   24.67 ? 72  LEU   A C     1 
ATOM   532  O O     . LEU   A 1 91  ? 4.866   29.608 55.018 1   25.19 ? 72  LEU   A O     1 
ATOM   533  C CB    . LEU   A 1 91  ? 6.149   26.786 53.917 1   23.4  ? 72  LEU   A CB    1 
ATOM   534  C CG    . LEU   A 1 91  ? 5.809   25.304 54.16  1   24.85 ? 72  LEU   A CG    1 
ATOM   535  C CD1   . LEU   A 1 91  ? 7.033   24.468 54.051 1   24.59 ? 72  LEU   A CD1   1 
ATOM   536  C CD2   . LEU   A 1 91  ? 5.172   25.104 55.544 1   25.38 ? 72  LEU   A CD2   1 
ATOM   537  N N     . SER   A 1 92  ? 5.693   29.866 52.945 1   22.5  ? 73  SER   A N     1 
ATOM   538  C CA    . SER   A 1 92  ? 5.822   31.304 53.129 1   22.7  ? 73  SER   A CA    1 
ATOM   539  C C     . SER   A 1 92  ? 4.479   32.002 52.891 1   24.12 ? 73  SER   A C     1 
ATOM   540  O O     . SER   A 1 92  ? 4.17    32.972 53.568 1   24.19 ? 73  SER   A O     1 
ATOM   541  C CB    . SER   A 1 92  ? 6.902   31.863 52.229 1   22.75 ? 73  SER   A CB    1 
ATOM   542  O OG    . SER   A 1 92  ? 8.194   31.464 52.657 1   24.79 ? 73  SER   A OG    1 
ATOM   543  N N     . ALA   A 1 93  ? 3.679   31.503 51.953 1   23    ? 74  ALA   A N     1 
ATOM   544  C CA    . ALA   A 1 93  ? 2.389   32.114 51.647 1   24.49 ? 74  ALA   A CA    1 
ATOM   545  C C     . ALA   A 1 93  ? 1.46    32.19  52.848 1   26.62 ? 74  ALA   A C     1 
ATOM   546  O O     . ALA   A 1 93  ? 0.681   33.157 52.952 1   27.09 ? 74  ALA   A O     1 
ATOM   547  C CB    . ALA   A 1 93  ? 1.719   31.338 50.504 1   24.19 ? 74  ALA   A CB    1 
ATOM   548  N N     . CYS   A 1 94  ? 1.5     31.197 53.765 1   26.3  ? 75  CYS   A N     1 
ATOM   549  C CA    . CYS   A 1 94  ? 0.575   31.23  54.899 1   26.99 ? 75  CYS   A CA    1 
ATOM   550  C C     . CYS   A 1 94  ? 0.849   32.408 55.868 1   28.46 ? 75  CYS   A C     1 
ATOM   551  O O     . CYS   A 1 94  ? -0.005  32.724 56.7   1   30.69 ? 75  CYS   A O     1 
ATOM   552  C CB    . CYS   A 1 94  ? 0.541   29.884 55.611 1   27.32 ? 75  CYS   A CB    1 
ATOM   553  S SG    . CYS   A 1 94  ? 2.009   29.565 56.608 1   29.96 ? 75  CYS   A SG    1 
ATOM   554  N N     . GLU   A 1 95  ? 2.007   33.056 55.743 1   27.4  ? 76  GLU   A N     1 
ATOM   555  C CA    . GLU   A 1 95  ? 2.28    34.246 56.556 1   28.38 ? 76  GLU   A CA    1 
ATOM   556  C C     . GLU   A 1 95  ? 1.551   35.475 56     1   30.01 ? 76  GLU   A C     1 
ATOM   557  O O     . GLU   A 1 95  ? 1.37    36.458 56.729 1   31.84 ? 76  GLU   A O     1 
ATOM   558  C CB    . GLU   A 1 95  ? 3.787   34.545 56.575 1   29.27 ? 76  GLU   A CB    1 
ATOM   559  C CG    . GLU   A 1 95  ? 4.631   33.439 57.16  1   32.09 ? 76  GLU   A CG    1 
ATOM   560  C CD    . GLU   A 1 95  ? 4.287   33.105 58.596 1   38.69 ? 76  GLU   A CD    1 
ATOM   561  O OE1   . GLU   A 1 95  ? 3.872   34.019 59.349 1   42.02 ? 76  GLU   A OE1   1 
ATOM   562  O OE2   . GLU   A 1 95  ? 4.44    31.925 58.97  1   40.01 ? 76  GLU   A OE2   1 
ATOM   563  N N     . SER   A 1 96  ? 1.173   35.457 54.703 1   28.66 ? 77  SER   A N     1 
ATOM   564  C CA    . SER   A 1 96  ? 0.636   36.633 54.023 1   28.98 ? 77  SER   A CA    1 
ATOM   565  C C     . SER   A 1 96  ? -0.782  36.532 53.564 1   29.48 ? 77  SER   A C     1 
ATOM   566  O O     . SER   A 1 96  ? -1.336  37.54  53.111 1   29.23 ? 77  SER   A O     1 
ATOM   567  C CB    . SER   A 1 96  ? 1.505   36.959 52.821 1   30.07 ? 77  SER   A CB    1 
ATOM   568  O OG    . SER   A 1 96  ? 2.825   37.187 53.271 1   31.15 ? 77  SER   A OG    1 
ATOM   569  N N     . PHE   A 1 97  ? -1.382  35.346 53.641 1   28.17 ? 78  PHE   A N     1 
ATOM   570  C CA    . PHE   A 1 97  ? -2.753  35.178 53.211 1   28.85 ? 78  PHE   A CA    1 
ATOM   571  C C     . PHE   A 1 97  ? -3.607  34.605 54.338 1   31.78 ? 78  PHE   A C     1 
ATOM   572  O O     . PHE   A 1 97  ? -3.222  33.601 54.928 1   33.03 ? 78  PHE   A O     1 
ATOM   573  C CB    . PHE   A 1 97  ? -2.79   34.248 51.977 1   27.4  ? 78  PHE   A CB    1 
ATOM   574  C CG    . PHE   A 1 97  ? -2.297  34.949 50.736 1   25.48 ? 78  PHE   A CG    1 
ATOM   575  C CD1   . PHE   A 1 97  ? -0.952  34.963 50.42  1   25.98 ? 78  PHE   A CD1   1 
ATOM   576  C CD2   . PHE   A 1 97  ? -3.162  35.691 49.954 1   26.08 ? 78  PHE   A CD2   1 
ATOM   577  C CE1   . PHE   A 1 97  ? -0.489  35.645 49.307 1   27.02 ? 78  PHE   A CE1   1 
ATOM   578  C CE2   . PHE   A 1 97  ? -2.702  36.36  48.832 1   27    ? 78  PHE   A CE2   1 
ATOM   579  C CZ    . PHE   A 1 97  ? -1.363  36.354 48.532 1   27.14 ? 78  PHE   A CZ    1 
ATOM   580  N N     . LYS   A 1 98  ? -4.786  35.186 54.568 1   31.9  ? 79  LYS   A N     1 
ATOM   581  C CA    . LYS   A 1 98  ? -5.69   34.694 55.6   1   33.42 ? 79  LYS   A CA    1 
ATOM   582  C C     . LYS   A 1 98  ? -6.2    33.3   55.231 1   33.19 ? 79  LYS   A C     1 
ATOM   583  O O     . LYS   A 1 98  ? -6.314  32.434 56.101 1   34.97 ? 79  LYS   A O     1 
ATOM   584  C CB    . LYS   A 1 98  ? -6.845  35.696 55.779 1   36.55 ? 79  LYS   A CB    1 
ATOM   585  C CG    . LYS   A 1 98  ? -8.082  35.177 56.49  1   43.66 ? 79  LYS   A CG    1 
ATOM   586  C CD    . LYS   A 1 98  ? -9.057  36.308 56.737 1   51.48 ? 79  LYS   A CD    1 
ATOM   587  C CE    . LYS   A 1 98  ? -10.245 35.822 57.518 1   57.61 ? 79  LYS   A CE    1 
ATOM   588  N NZ    . LYS   A 1 98  ? -9.821  34.931 58.632 1   60.66 ? 79  LYS   A NZ    1 
ATOM   589  N N     . GLU   A 1 99  ? -6.494  33.065 53.938 1   30.5  ? 80  GLU   A N     1 
ATOM   590  C CA    . GLU   A 1 99  ? -6.987  31.77  53.499 1   29.1  ? 80  GLU   A CA    1 
ATOM   591  C C     . GLU   A 1 99  ? -6.205  31.349 52.267 1   28.46 ? 80  GLU   A C     1 
ATOM   592  O O     . GLU   A 1 99  ? -5.919  32.159 51.397 1   27.9  ? 80  GLU   A O     1 
ATOM   593  C CB    . GLU   A 1 99  ? -8.48   31.829 53.146 1   29.18 ? 80  GLU   A CB    1 
ATOM   594  C CG    . GLU   A 1 99  ? -9.052  30.499 52.712 1   35.6  ? 80  GLU   A CG    1 
ATOM   595  C CD    . GLU   A 1 99  ? -10.523 30.492 52.357 1   41.85 ? 80  GLU   A CD    1 
ATOM   596  O OE1   . GLU   A 1 99  ? -11.028 29.417 51.958 1   41.87 ? 80  GLU   A OE1   1 
ATOM   597  O OE2   . GLU   A 1 99  ? -11.154 31.576 52.381 1   46.22 ? 80  GLU   A OE2   1 
ATOM   598  N N     . ILE   A 1 100 ? -5.901  30.062 52.206 1   26.02 ? 81  ILE   A N     1 
ATOM   599  C CA    . ILE   A 1 100 ? -5.263  29.438 51.053 1   26.02 ? 81  ILE   A CA    1 
ATOM   600  C C     . ILE   A 1 100 ? -6.169  28.281 50.633 1   25.37 ? 81  ILE   A C     1 
ATOM   601  O O     . ILE   A 1 100 ? -6.598  27.501 51.489 1   27.56 ? 81  ILE   A O     1 
ATOM   602  C CB    . ILE   A 1 100 ? -3.878  28.888 51.422 1   26.42 ? 81  ILE   A CB    1 
ATOM   603  C CG1   . ILE   A 1 100 ? -2.946  30.02  51.763 1   27.2  ? 81  ILE   A CG1   1 
ATOM   604  C CG2   . ILE   A 1 100 ? -3.305  28.008 50.257 1   26.76 ? 81  ILE   A CG2   1 
ATOM   605  C CD1   . ILE   A 1 100 ? -1.54   29.563 52.199 1   27.52 ? 81  ILE   A CD1   1 
ATOM   606  N N     . VAL   A 1 101 ? -6.522  28.218 49.345 1   23.57 ? 82  VAL   A N     1 
ATOM   607  C CA    . VAL   A 1 101 ? -7.327  27.144 48.794 1   23.83 ? 82  VAL   A CA    1 
ATOM   608  C C     . VAL   A 1 101 ? -6.334  26.312 47.996 1   22.34 ? 82  VAL   A C     1 
ATOM   609  O O     . VAL   A 1 101 ? -5.614  26.875 47.172 1   22.43 ? 82  VAL   A O     1 
ATOM   610  C CB    . VAL   A 1 101 ? -8.437  27.697 47.9   1   25.77 ? 82  VAL   A CB    1 
ATOM   611  C CG1   . VAL   A 1 101 ? -9.119  26.586 47.145 1   26.91 ? 82  VAL   A CG1   1 
ATOM   612  C CG2   . VAL   A 1 101 ? -9.451  28.457 48.737 1   26.78 ? 82  VAL   A CG2   1 
ATOM   613  N N     . VAL   A 1 102 ? -6.298  24.995 48.248 1   21.09 ? 83  VAL   A N     1 
ATOM   614  C CA    . VAL   A 1 102 ? -5.417  24.096 47.516 1   22.55 ? 83  VAL   A CA    1 
ATOM   615  C C     . VAL   A 1 102 ? -6.258  23.289 46.568 1   21.74 ? 83  VAL   A C     1 
ATOM   616  O O     . VAL   A 1 102 ? -7.412  22.955 46.877 1   21.85 ? 83  VAL   A O     1 
ATOM   617  C CB    . VAL   A 1 102 ? -4.57   23.2   48.426 1   23.78 ? 83  VAL   A CB    1 
ATOM   618  C CG1   . VAL   A 1 102 ? -3.623  24.043 49.266 1   23.76 ? 83  VAL   A CG1   1 
ATOM   619  C CG2   . VAL   A 1 102 ? -5.448  22.279 49.295 1   25.88 ? 83  VAL   A CG2   1 
ATOM   620  N N     . THR   A 1 103 ? -5.739  23.083 45.367 1   20.64 ? 84  THR   A N     1 
ATOM   621  C CA    . THR   A 1 103 ? -6.527  22.422 44.329 1   20.7  ? 84  THR   A CA    1 
ATOM   622  C C     . THR   A 1 103 ? -5.692  21.495 43.491 1   20.36 ? 84  THR   A C     1 
ATOM   623  O O     . THR   A 1 103 ? -4.486  21.736 43.302 1   19.74 ? 84  THR   A O     1 
ATOM   624  C CB    . THR   A 1 103 ? -7.13   23.478 43.37  1   22.23 ? 84  THR   A CB    1 
ATOM   625  O OG1   . THR   A 1 103 ? -6.093  24.024 42.526 1   23.17 ? 84  THR   A OG1   1 
ATOM   626  C CG2   . THR   A 1 103 ? -7.838  24.621 44.076 1   23.23 ? 84  THR   A CG2   1 
ATOM   627  N N     . ASP   A 1 104 ? -6.325  20.506 42.871 1   19.91 ? 85  ASP   A N     1 
ATOM   628  C CA    . ASP   A 1 104 ? -5.607  19.604 41.986 1   19.19 ? 85  ASP   A CA    1 
ATOM   629  C C     . ASP   A 1 104 ? -6.602  18.824 41.161 1   18.74 ? 85  ASP   A C     1 
ATOM   630  O O     . ASP   A 1 104 ? -7.77   18.639 41.585 1   19.08 ? 85  ASP   A O     1 
ATOM   631  C CB    . ASP   A 1 104 ? -4.723  18.61  42.758 1   19.16 ? 85  ASP   A CB    1 
ATOM   632  C CG    . ASP   A 1 104 ? -3.651  18.035 41.845 1   18.21 ? 85  ASP   A CG    1 
ATOM   633  O OD1   . ASP   A 1 104 ? -2.731  18.783 41.475 1   17.45 ? 85  ASP   A OD1   1 
ATOM   634  O OD2   . ASP   A 1 104 ? -3.701  16.829 41.543 1   18.29 ? 85  ASP   A OD2   1 
ATOM   635  N N     . TYR   A 1 105 ? -6.167  18.299 40.021 1   18.46 ? 86  TYR   A N     1 
ATOM   636  C CA    . TYR   A 1 105 ? -7.023  17.418 39.228 1   19.21 ? 86  TYR   A CA    1 
ATOM   637  C C     . TYR   A 1 105 ? -7.2    16.056 39.907 1   19.03 ? 86  TYR   A C     1 
ATOM   638  O O     . TYR   A 1 105 ? -8.248  15.423 39.699 1   20.41 ? 86  TYR   A O     1 
ATOM   639  C CB    . TYR   A 1 105 ? -6.422  17.248 37.829 1   18.96 ? 86  TYR   A CB    1 
ATOM   640  C CG    . TYR   A 1 105 ? -7.404  16.585 36.889 1   19.91 ? 86  TYR   A CG    1 
ATOM   641  C CD1   . TYR   A 1 105 ? -8.536  17.257 36.458 1   22.44 ? 86  TYR   A CD1   1 
ATOM   642  C CD2   . TYR   A 1 105 ? -7.247  15.264 36.507 1   21.66 ? 86  TYR   A CD2   1 
ATOM   643  C CE1   . TYR   A 1 105 ? -9.474  16.644 35.643 1   24.14 ? 86  TYR   A CE1   1 
ATOM   644  C CE2   . TYR   A 1 105 ? -8.183  14.633 35.691 1   23.49 ? 86  TYR   A CE2   1 
ATOM   645  C CZ    . TYR   A 1 105 ? -9.287  15.333 35.255 1   24.8  ? 86  TYR   A CZ    1 
ATOM   646  O OH    . TYR   A 1 105 ? -10.257 14.749 34.464 1   27.5  ? 86  TYR   A OH    1 
ATOM   647  N N     . SER   A 1 106 ? -6.176  15.579 40.606 1   19.1  ? 87  SER   A N     1 
ATOM   648  C CA    . SER   A 1 106 ? -6.197  14.23  41.179 1   18.74 ? 87  SER   A CA    1 
ATOM   649  C C     . SER   A 1 106 ? -6.776  14.187 42.582 1   19.82 ? 87  SER   A C     1 
ATOM   650  O O     . SER   A 1 106 ? -6.209  14.76  43.506 1   20.15 ? 87  SER   A O     1 
ATOM   651  C CB    . SER   A 1 106 ? -4.779  13.669 41.184 1   19.77 ? 87  SER   A CB    1 
ATOM   652  O OG    . SER   A 1 106 ? -4.711  12.539 42.052 1   23.36 ? 87  SER   A OG    1 
ATOM   653  N N     . ASP   A 1 107 ? -7.846  13.377 42.767 1   21.38 ? 88  ASP   A N     1 
ATOM   654  C CA    . ASP   A 1 107 ? -8.411  13.204 44.105 1   22.37 ? 88  ASP   A CA    1 
ATOM   655  C C     . ASP   A 1 107 ? -7.425  12.437 44.983 1   21.03 ? 88  ASP   A C     1 
ATOM   656  O O     . ASP   A 1 107 ? -7.362  12.749 46.172 1   23.31 ? 88  ASP   A O     1 
ATOM   657  C CB    . ASP   A 1 107 ? -9.735  12.406 44.001 1   27.43 ? 88  ASP   A CB    1 
ATOM   658  C CG    . ASP   A 1 107 ? -10.686 12.997 42.981 1   39    ? 88  ASP   A CG    1 
ATOM   659  O OD1   . ASP   A 1 107 ? -11.404 13.95  43.327 1   42.21 ? 88  ASP   A OD1   1 
ATOM   660  O OD2   . ASP   A 1 107 ? -10.657 12.548 41.81  1   44.1  ? 88  ASP   A OD2   1 
ATOM   661  N N     . GLN   A 1 108 ? -6.588  11.509 44.433 1   20.25 ? 89  GLN   A N     1 
ATOM   662  C CA    . GLN   A 1 108 ? -5.576  10.825 45.252 1   21.77 ? 89  GLN   A CA    1 
ATOM   663  C C     . GLN   A 1 108 ? -4.568  11.831 45.827 1   21.39 ? 89  GLN   A C     1 
ATOM   664  O O     . GLN   A 1 108 ? -4.164  11.734 46.996 1   21.82 ? 89  GLN   A O     1 
ATOM   665  C CB    . GLN   A 1 108 ? -4.756  9.8    44.429 1   25.64 ? 89  GLN   A CB    1 
ATOM   666  C CG    . GLN   A 1 108 ? -5.407  8.467  44.116 1   31.51 ? 89  GLN   A CG    1 
ATOM   667  C CD    . GLN   A 1 108 ? -4.283  7.546  43.626 1   36.5  ? 89  GLN   A CD    1 
ATOM   668  O OE1   . GLN   A 1 108 ? -3.968  7.485  42.427 1   37.99 ? 89  GLN   A OE1   1 
ATOM   669  N NE2   . GLN   A 1 108 ? -3.617  6.859  44.536 1   35.59 ? 89  GLN   A NE2   1 
ATOM   670  N N     . ASN   A 1 109 ? -4.193  12.829 45.012 1   19.95 ? 90  ASN   A N     1 
ATOM   671  C CA    . ASN   A 1 109 ? -3.272  13.845 45.506 1   20.79 ? 90  ASN   A CA    1 
ATOM   672  C C     . ASN   A 1 109 ? -3.903  14.67  46.622 1   21.79 ? 90  ASN   A C     1 
ATOM   673  O O     . ASN   A 1 109 ? -3.244  14.94  47.633 1   23.33 ? 90  ASN   A O     1 
ATOM   674  C CB    . ASN   A 1 109 ? -2.888  14.775 44.354 1   20.58 ? 90  ASN   A CB    1 
ATOM   675  C CG    . ASN   A 1 109 ? -1.762  14.215 43.565 1   22.53 ? 90  ASN   A CG    1 
ATOM   676  O OD1   . ASN   A 1 109 ? -0.933  13.427 44.089 1   25.31 ? 90  ASN   A OD1   1 
ATOM   677  N ND2   . ASN   A 1 109 ? -1.585  14.66  42.305 1   21.17 ? 90  ASN   A ND2   1 
ATOM   678  N N     . LEU   A 1 110 ? -5.166  15.074 46.449 1   22.05 ? 91  LEU   A N     1 
ATOM   679  C CA    . LEU   A 1 110 ? -5.851  15.852 47.482 1   24.21 ? 91  LEU   A CA    1 
ATOM   680  C C     . LEU   A 1 110 ? -5.966  15.047 48.777 1   25.56 ? 91  LEU   A C     1 
ATOM   681  O O     . LEU   A 1 110 ? -5.831  15.614 49.862 1   27.15 ? 91  LEU   A O     1 
ATOM   682  C CB    . LEU   A 1 110 ? -7.231  16.296 47.011 1   25.89 ? 91  LEU   A CB    1 
ATOM   683  C CG    . LEU   A 1 110 ? -7.233  17.242 45.769 1   30.58 ? 91  LEU   A CG    1 
ATOM   684  C CD1   . LEU   A 1 110 ? -8.671  17.554 45.312 1   32.1  ? 91  LEU   A CD1   1 
ATOM   685  C CD2   . LEU   A 1 110 ? -6.432  18.455 46.015 1   32.2  ? 91  LEU   A CD2   1 
ATOM   686  N N     . GLN   A 1 111 ? -6.19   13.732 48.671 1   24.48 ? 92  GLN   A N     1 
ATOM   687  C CA    . GLN   A 1 111 ? -6.272  12.901 49.886 1   24.3  ? 92  GLN   A CA    1 
ATOM   688  C C     . GLN   A 1 111 ? -4.917  12.837 50.608 1   24.86 ? 92  GLN   A C     1 
ATOM   689  O O     . GLN   A 1 111 ? -4.866  12.887 51.839 1   26.74 ? 92  GLN   A O     1 
ATOM   690  C CB    . GLN   A 1 111 ? -6.765  11.506 49.533 1   26.62 ? 92  GLN   A CB    1 
ATOM   691  C CG    . GLN   A 1 111 ? -8.223  11.541 49.092 1   34.06 ? 92  GLN   A CG    1 
ATOM   692  C CD    . GLN   A 1 111 ? -8.784  10.173 48.818 1   43.81 ? 92  GLN   A CD    1 
ATOM   693  O OE1   . GLN   A 1 111 ? -8.507  9.199  49.54  1   48.15 ? 92  GLN   A OE1   1 
ATOM   694  N NE2   . GLN   A 1 111 ? -9.597  10.082 47.771 1   45.91 ? 92  GLN   A NE2   1 
ATOM   695  N N     . GLU   A 1 112 ? -3.812  12.794 49.854 1   24.31 ? 93  GLU   A N     1 
ATOM   696  C CA    . GLU   A 1 112 ? -2.477  12.807 50.448 1   24.74 ? 93  GLU   A CA    1 
ATOM   697  C C     . GLU   A 1 112 ? -2.211  14.166 51.149 1   26.8  ? 93  GLU   A C     1 
ATOM   698  O O     . GLU   A 1 112 ? -1.712  14.185 52.285 1   26.21 ? 93  GLU   A O     1 
ATOM   699  C CB    . GLU   A 1 112 ? -1.426  12.478 49.374 1   25.3  ? 93  GLU   A CB    1 
ATOM   700  C CG    . GLU   A 1 112 ? -0      12.334 49.91  1   26.87 ? 93  GLU   A CG    1 
ATOM   701  C CD    . GLU   A 1 112 ? 0.309   11.158 50.829 1   29.4  ? 93  GLU   A CD    1 
ATOM   702  O OE1   . GLU   A 1 112 ? -0.35   10.101 50.696 1   31.7  ? 93  GLU   A OE1   1 
ATOM   703  O OE2   . GLU   A 1 112 ? 1.233   11.283 51.667 1   30.47 ? 93  GLU   A OE2   1 
ATOM   704  N N     . LEU   A 1 113 ? -2.661  15.287 50.536 1   27.43 ? 94  LEU   A N     1 
ATOM   705  C CA    . LEU   A 1 113 ? -2.587  16.625 51.145 1   30.31 ? 94  LEU   A CA    1 
ATOM   706  C C     . LEU   A 1 113 ? -3.352  16.619 52.447 1   29.7  ? 94  LEU   A C     1 
ATOM   707  O O     . LEU   A 1 113 ? -2.854  17.105 53.475 1   29.23 ? 94  LEU   A O     1 
ATOM   708  C CB    . LEU   A 1 113 ? -3.299  17.666 50.246 1   32.5  ? 94  LEU   A CB    1 
ATOM   709  C CG    . LEU   A 1 113 ? -2.571  18.25  49.119 1   35.66 ? 94  LEU   A CG    1 
ATOM   710  C CD1   . LEU   A 1 113 ? -3.475  19.239 48.35  1   36.52 ? 94  LEU   A CD1   1 
ATOM   711  C CD2   . LEU   A 1 113 ? -1.383  18.989 49.61  1   35.72 ? 94  LEU   A CD2   1 
ATOM   712  N N     . GLU   A 1 114 ? -4.58   16.089 52.401 1   29.14 ? 95  GLU   A N     1 
ATOM   713  C CA    . GLU   A 1 114 ? -5.442  16.092 53.562 1   30.07 ? 95  GLU   A CA    1 
ATOM   714  C C     . GLU   A 1 114 ? -4.873  15.277 54.694 1   29.5  ? 95  GLU   A C     1 
ATOM   715  O O     . GLU   A 1 114 ? -5.02   15.691 55.834 1   30.31 ? 95  GLU   A O     1 
ATOM   716  C CB    . GLU   A 1 114 ? -6.863  15.698 53.188 1   33.74 ? 95  GLU   A CB    1 
ATOM   717  C CG    . GLU   A 1 114 ? -7.49   16.82  52.38  1   41.76 ? 95  GLU   A CG    1 
ATOM   718  C CD    . GLU   A 1 114 ? -8.979  16.751 52.132 1   51.69 ? 95  GLU   A CD    1 
ATOM   719  O OE1   . GLU   A 1 114 ? -9.385  15.968 51.244 1   54.36 ? 95  GLU   A OE1   1 
ATOM   720  O OE2   . GLU   A 1 114 ? -9.732  17.506 52.79  1   54.02 ? 95  GLU   A OE2   1 
ATOM   721  N N     . LYS   A 1 115 ? -4.119  14.204 54.41  1   29.04 ? 96  LYS   A N     1 
ATOM   722  C CA    . LYS   A 1 115 ? -3.458  13.431 55.491 1   29.19 ? 96  LYS   A CA    1 
ATOM   723  C C     . LYS   A 1 115 ? -2.482  14.34  56.247 1   28.87 ? 96  LYS   A C     1 
ATOM   724  O O     . LYS   A 1 115 ? -2.414  14.297 57.49  1   30.42 ? 96  LYS   A O     1 
ATOM   725  C CB    . LYS   A 1 115 ? -2.682  12.252 54.913 1   29.72 ? 96  LYS   A CB    1 
ATOM   726  C CG    . LYS   A 1 115 ? -3.582  11.102 54.534 1   34.89 ? 96  LYS   A CG    1 
ATOM   727  C CD    . LYS   A 1 115 ? -2.755  9.907  54.074 1   41.76 ? 96  LYS   A CD    1 
ATOM   728  C CE    . LYS   A 1 115 ? -3.695  8.744  53.857 1   48.1  ? 96  LYS   A CE    1 
ATOM   729  N NZ    . LYS   A 1 115 ? -3.263  7.88   52.735 1   51.6  ? 96  LYS   A NZ    1 
ATOM   730  N N     . TRP   A 1 116 ? -1.765  15.226 55.518 1   27.57 ? 97  TRP   A N     1 
ATOM   731  C CA    . TRP   A 1 116 ? -0.849  16.138 56.182 1   27.47 ? 97  TRP   A CA    1 
ATOM   732  C C     . TRP   A 1 116 ? -1.595  17.228 56.913 1   28.23 ? 97  TRP   A C     1 
ATOM   733  O O     . TRP   A 1 116 ? -1.241  17.552 58.058 1   27.81 ? 97  TRP   A O     1 
ATOM   734  C CB    . TRP   A 1 116 ? 0.148   16.772 55.192 1   26.8  ? 97  TRP   A CB    1 
ATOM   735  C CG    . TRP   A 1 116 ? 1.199   17.528 55.944 1   27.02 ? 97  TRP   A CG    1 
ATOM   736  C CD1   . TRP   A 1 116 ? 2.324   17.009 56.507 1   28.61 ? 97  TRP   A CD1   1 
ATOM   737  C CD2   . TRP   A 1 116 ? 1.181   18.924 56.288 1   27.34 ? 97  TRP   A CD2   1 
ATOM   738  N NE1   . TRP   A 1 116 ? 3.026   17.998 57.153 1   29.59 ? 97  TRP   A NE1   1 
ATOM   739  C CE2   . TRP   A 1 116 ? 2.352   19.188 57.025 1   28.98 ? 97  TRP   A CE2   1 
ATOM   740  C CE3   . TRP   A 1 116 ? 0.312   19.982 56.003 1   28.35 ? 97  TRP   A CE3   1 
ATOM   741  C CZ2   . TRP   A 1 116 ? 2.641   20.461 57.534 1   29.97 ? 97  TRP   A CZ2   1 
ATOM   742  C CZ3   . TRP   A 1 116 ? 0.584   21.229 56.53  1   29.26 ? 97  TRP   A CZ3   1 
ATOM   743  C CH2   . TRP   A 1 116 ? 1.742   21.46  57.273 1   29.97 ? 97  TRP   A CH2   1 
ATOM   744  N N     . LEU   A 1 117 ? -2.63   17.805 56.29  1   28.52 ? 98  LEU   A N     1 
ATOM   745  C CA    . LEU   A 1 117 ? -3.396  18.869 56.916 1   29.94 ? 98  LEU   A CA    1 
ATOM   746  C C     . LEU   A 1 117 ? -4.027  18.411 58.227 1   31.28 ? 98  LEU   A C     1 
ATOM   747  O O     . LEU   A 1 117 ? -4.04   19.166 59.188 1   32.66 ? 98  LEU   A O     1 
ATOM   748  C CB    . LEU   A 1 117 ? -4.48   19.395 55.994 1   30.65 ? 98  LEU   A CB    1 
ATOM   749  C CG    . LEU   A 1 117 ? -3.943  20.122 54.748 1   30.92 ? 98  LEU   A CG    1 
ATOM   750  C CD1   . LEU   A 1 117 ? -5.08   20.354 53.746 1   32.69 ? 98  LEU   A CD1   1 
ATOM   751  C CD2   . LEU   A 1 117 ? -3.248  21.425 55.124 1   31.7  ? 98  LEU   A CD2   1 
ATOM   752  N N     . LYS   A 1 118 ? -4.512  17.163 58.259 1   31.81 ? 99  LYS   A N     1 
ATOM   753  C CA    . LYS   A 1 118 ? -5.111  16.591 59.478 1   33.7  ? 99  LYS   A CA    1 
ATOM   754  C C     . LYS   A 1 118 ? -4.083  16     60.45  1   35.23 ? 99  LYS   A C     1 
ATOM   755  O O     . LYS   A 1 118 ? -4.484  15.48  61.512 1   34.5  ? 99  LYS   A O     1 
ATOM   756  C CB    . LYS   A 1 118 ? -6.191  15.552 59.121 1   36.89 ? 99  LYS   A CB    1 
ATOM   757  C CG    . LYS   A 1 118 ? -7.352  16.189 58.373 1   45.09 ? 99  LYS   A CG    1 
ATOM   758  C CD    . LYS   A 1 118 ? -8.419  15.203 57.904 1   53.81 ? 99  LYS   A CD    1 
ATOM   759  C CE    . LYS   A 1 118 ? -9.4    15.914 56.984 1   60.35 ? 99  LYS   A CE    1 
ATOM   760  N NZ    . LYS   A 1 118 ? -10.359 14.976 56.342 1   64.48 ? 99  LYS   A NZ    1 
ATOM   761  N N     . ALA   A 1 119 ? -2.777  16.129 60.152 1   35.83 ? 100 ALA   A N     1 
ATOM   762  C CA    . ALA   A 1 119 ? -1.657  15.622 60.955 1   37.9  ? 100 ALA   A CA    1 
ATOM   763  C C     . ALA   A 1 119 ? -1.784  14.134 61.266 1   39.76 ? 100 ALA   A C     1 
ATOM   764  O O     . ALA   A 1 119 ? -1.577  13.703 62.404 1   40.78 ? 100 ALA   A O     1 
ATOM   765  C CB    . ALA   A 1 119 ? -1.455  16.449 62.227 1   38.2  ? 100 ALA   A CB    1 
ATOM   766  N N     . ALA   A 1 120 ? -2.155  13.358 60.255 1   39.77 ? 101 ALA   A N     1 
ATOM   767  C CA    . ALA   A 1 120 ? -2.279  11.916 60.387 1   41.08 ? 101 ALA   A CA    1 
ATOM   768  C C     . ALA   A 1 120 ? -0.878  11.298 60.449 1   42.6  ? 101 ALA   A C     1 
ATOM   769  O O     . ALA   A 1 120 ? 0.043   11.75  59.765 1   42.21 ? 101 ALA   A O     1 
ATOM   770  C CB    . ALA   A 1 120 ? -3.056  11.351 59.203 1   41.56 ? 101 ALA   A CB    1 
ATOM   771  N N     . PRO   A 1 121 ? -0.673  10.275 61.295 1   43.74 ? 102 PRO   A N     1 
ATOM   772  C CA    . PRO   A 1 121 ? 0.654   9.626  61.364 1   43.73 ? 102 PRO   A CA    1 
ATOM   773  C C     . PRO   A 1 121 ? 1.204   9.137  60.02  1   42.64 ? 102 PRO   A C     1 
ATOM   774  O O     . PRO   A 1 121 ? 2.42    9.154  59.851 1   43.46 ? 102 PRO   A O     1 
ATOM   775  C CB    . PRO   A 1 121 ? 0.411   8.433  62.299 1   44.94 ? 102 PRO   A CB    1 
ATOM   776  C CG    . PRO   A 1 121 ? -0.743  8.865  63.134 1   45.82 ? 102 PRO   A CG    1 
ATOM   777  C CD    . PRO   A 1 121 ? -1.636  9.64   62.212 1   43.58 ? 102 PRO   A CD    1 
ATOM   778  N N     . ALA   A 1 122 ? 0.34    8.758  59.063 1   40.29 ? 103 ALA   A N     1 
ATOM   779  C CA    . ALA   A 1 122 ? 0.765   8.313  57.73  1   38.03 ? 103 ALA   A CA    1 
ATOM   780  C C     . ALA   A 1 122 ? 1.115   9.468  56.756 1   35.38 ? 103 ALA   A C     1 
ATOM   781  O O     . ALA   A 1 122 ? 1.435   9.204  55.6   1   36.56 ? 103 ALA   A O     1 
ATOM   782  C CB    . ALA   A 1 122 ? -0.307  7.459  57.103 1   38.27 ? 103 ALA   A CB    1 
ATOM   783  N N     . ALA   A 1 123 ? 0.969   10.71  57.201 1   33.11 ? 104 ALA   A N     1 
ATOM   784  C CA    . ALA   A 1 123 ? 1.272   11.873 56.368 1   32.23 ? 104 ALA   A CA    1 
ATOM   785  C C     . ALA   A 1 123 ? 2.75    11.922 56.044 1   30.98 ? 104 ALA   A C     1 
ATOM   786  O O     . ALA   A 1 123 ? 3.58    11.431 56.799 1   31.78 ? 104 ALA   A O     1 
ATOM   787  C CB    . ALA   A 1 123 ? 0.89    13.138 57.112 1   33.29 ? 104 ALA   A CB    1 
ATOM   788  N N     . PHE   A 1 124 ? 3.106   12.589 54.938 1   27.8  ? 105 PHE   A N     1 
ATOM   789  C CA    . PHE   A 1 124 ? 4.504   12.736 54.574 1   26.92 ? 105 PHE   A CA    1 
ATOM   790  C C     . PHE   A 1 124 ? 5.236   13.621 55.598 1   27.78 ? 105 PHE   A C     1 
ATOM   791  O O     . PHE   A 1 124 ? 4.651   14.555 56.159 1   29.04 ? 105 PHE   A O     1 
ATOM   792  C CB    . PHE   A 1 124 ? 4.576   13.408 53.189 1   24.95 ? 105 PHE   A CB    1 
ATOM   793  C CG    . PHE   A 1 124 ? 5.962   13.504 52.617 1   24.39 ? 105 PHE   A CG    1 
ATOM   794  C CD1   . PHE   A 1 124 ? 6.622   12.378 52.179 1   24.55 ? 105 PHE   A CD1   1 
ATOM   795  C CD2   . PHE   A 1 124 ? 6.576   14.725 52.454 1   25.7  ? 105 PHE   A CD2   1 
ATOM   796  C CE1   . PHE   A 1 124 ? 7.887   12.466 51.634 1   24.52 ? 105 PHE   A CE1   1 
ATOM   797  C CE2   . PHE   A 1 124 ? 7.828   14.818 51.868 1   25.45 ? 105 PHE   A CE2   1 
ATOM   798  C CZ    . PHE   A 1 124 ? 8.467   13.687 51.443 1   23.76 ? 105 PHE   A CZ    1 
ATOM   799  N N     . ASP   A 1 125 ? 6.521   13.365 55.786 1   28.75 ? 106 ASP   A N     1 
ATOM   800  C CA    . ASP   A 1 125 ? 7.318   14.165 56.71  1   29.07 ? 106 ASP   A CA    1 
ATOM   801  C C     . ASP   A 1 125 ? 7.925   15.363 55.99  1   27.95 ? 106 ASP   A C     1 
ATOM   802  O O     . ASP   A 1 125 ? 8.953   15.239 55.326 1   29.4  ? 106 ASP   A O     1 
ATOM   803  C CB    . ASP   A 1 125 ? 8.423   13.316 57.351 1   32.22 ? 106 ASP   A CB    1 
ATOM   804  C CG    . ASP   A 1 125 ? 9.285   14.055 58.353 1   36.73 ? 106 ASP   A CG    1 
ATOM   805  O OD1   . ASP   A 1 125 ? 8.966   15.224 58.673 1   35.26 ? 106 ASP   A OD1   1 
ATOM   806  O OD2   . ASP   A 1 125 ? 10.27   13.458 58.835 1   41.98 ? 106 ASP   A OD2   1 
ATOM   807  N N     . TRP   A 1 126 ? 7.301   16.527 56.148 1   26.32 ? 107 TRP   A N     1 
ATOM   808  C CA    . TRP   A 1 126 ? 7.813   17.768 55.563 1   25.73 ? 107 TRP   A CA    1 
ATOM   809  C C     . TRP   A 1 126 ? 8.751   18.525 56.525 1   27.34 ? 107 TRP   A C     1 
ATOM   810  O O     . TRP   A 1 126 ? 9.221   19.616 56.172 1   26.56 ? 107 TRP   A O     1 
ATOM   811  C CB    . TRP   A 1 126 ? 6.628   18.693 55.261 1   23.67 ? 107 TRP   A CB    1 
ATOM   812  C CG    . TRP   A 1 126 ? 5.859   18.276 54.037 1   21.87 ? 107 TRP   A CG    1 
ATOM   813  C CD1   . TRP   A 1 126 ? 4.651   17.643 53.994 1   21.55 ? 107 TRP   A CD1   1 
ATOM   814  C CD2   . TRP   A 1 126 ? 6.261   18.471 52.679 1   20.89 ? 107 TRP   A CD2   1 
ATOM   815  N NE1   . TRP   A 1 126 ? 4.306   17.366 52.682 1   21.7  ? 107 TRP   A NE1   1 
ATOM   816  C CE2   . TRP   A 1 126 ? 5.27    17.89  51.858 1   20.62 ? 107 TRP   A CE2   1 
ATOM   817  C CE3   . TRP   A 1 126 ? 7.421   18.96  52.076 1   21.09 ? 107 TRP   A CE3   1 
ATOM   818  C CZ2   . TRP   A 1 126 ? 5.374   17.859 50.465 1   20.36 ? 107 TRP   A CZ2   1 
ATOM   819  C CZ3   . TRP   A 1 126 ? 7.506   18.951 50.69  1   20.69 ? 107 TRP   A CZ3   1 
ATOM   820  C CH2   . TRP   A 1 126 ? 6.485   18.406 49.906 1   20.36 ? 107 TRP   A CH2   1 
ATOM   821  N N     . SER   A 1 127 ? 9.052   17.975 57.733 1   28.57 ? 108 SER   A N     1 
ATOM   822  C CA    . SER   A 1 127 ? 9.837   18.742 58.722 1   29.98 ? 108 SER   A CA    1 
ATOM   823  C C     . SER   A 1 127 ? 11.19   19.299 58.23  1   30.17 ? 108 SER   A C     1 
ATOM   824  O O     . SER   A 1 127 ? 11.489  20.457 58.576 1   30.51 ? 108 SER   A O     1 
ATOM   825  C CB    . SER   A 1 127 ? 10.016  17.977 60.042 1   32.49 ? 108 SER   A CB    1 
ATOM   826  O OG    . SER   A 1 127 ? 10.715  16.765 59.847 1   36.87 ? 108 SER   A OG    1 
ATOM   827  N N     . PRO   A 1 128 ? 11.999  18.616 57.382 1   31.45 ? 109 PRO   A N     1 
ATOM   828  C CA    . PRO   A 1 128 ? 13.256  19.251 56.924 1   30.96 ? 109 PRO   A CA    1 
ATOM   829  C C     . PRO   A 1 128 ? 12.993  20.497 56.062 1   29.8  ? 109 PRO   A C     1 
ATOM   830  O O     . PRO   A 1 128 ? 13.74   21.45  56.098 1   30.78 ? 109 PRO   A O     1 
ATOM   831  C CB    . PRO   A 1 128 ? 13.944  18.145 56.111 1   32.37 ? 109 PRO   A CB    1 
ATOM   832  C CG    . PRO   A 1 128 ? 13.206  16.895 56.379 1   33.66 ? 109 PRO   A CG    1 
ATOM   833  C CD    . PRO   A 1 128 ? 11.85   17.259 56.819 1   32.05 ? 109 PRO   A CD    1 
ATOM   834  N N     . VAL   A 1 129 ? 11.898  20.473 55.271 1   28.37 ? 110 VAL   A N     1 
ATOM   835  C CA    . VAL   A 1 129 ? 11.543  21.59  54.423 1   26.61 ? 110 VAL   A CA    1 
ATOM   836  C C     . VAL   A 1 129 ? 10.994  22.723 55.283 1   27.08 ? 110 VAL   A C     1 
ATOM   837  O O     . VAL   A 1 129 ? 11.338  23.888 55.072 1   26.77 ? 110 VAL   A O     1 
ATOM   838  C CB    . VAL   A 1 129 ? 10.503  21.121 53.383 1   25.54 ? 110 VAL   A CB    1 
ATOM   839  C CG1   . VAL   A 1 129 ? 9.955   22.312 52.613 1   25.62 ? 110 VAL   A CG1   1 
ATOM   840  C CG2   . VAL   A 1 129 ? 11.099  20.063 52.446 1   26.39 ? 110 VAL   A CG2   1 
ATOM   841  N N     . VAL   A 1 130 ? 10.119  22.387 56.269 1   27.26 ? 111 VAL   A N     1 
ATOM   842  C CA    . VAL   A 1 130 ? 9.564   23.411 57.158 1   28.27 ? 111 VAL   A CA    1 
ATOM   843  C C     . VAL   A 1 130 ? 10.691  24.139 57.927 1   29.26 ? 111 VAL   A C     1 
ATOM   844  O O     . VAL   A 1 130 ? 10.689  25.368 58.033 1   29.92 ? 111 VAL   A O     1 
ATOM   845  C CB    . VAL   A 1 130 ? 8.577   22.778 58.161 1   29.15 ? 111 VAL   A CB    1 
ATOM   846  C CG1   . VAL   A 1 130 ? 8.141   23.797 59.225 1   30.36 ? 111 VAL   A CG1   1 
ATOM   847  C CG2   . VAL   A 1 130 ? 7.374   22.201 57.435 1   28.71 ? 111 VAL   A CG2   1 
ATOM   848  N N     . THR   A 1 131 ? 11.669  23.379 58.397 1   29.81 ? 112 THR   A N     1 
ATOM   849  C CA    . THR   A 1 131 ? 12.819  23.936 59.127 1   30.43 ? 112 THR   A CA    1 
ATOM   850  C C     . THR   A 1 131 ? 13.592  24.892 58.218 1   30.74 ? 112 THR   A C     1 
ATOM   851  O O     . THR   A 1 131 ? 13.946  25.989 58.644 1   32.04 ? 112 THR   A O     1 
ATOM   852  C CB    . THR   A 1 131 ? 13.717  22.814 59.638 1   33.56 ? 112 THR   A CB    1 
ATOM   853  O OG1   . THR   A 1 131 ? 12.971  22.08  60.607 1   34.61 ? 112 THR   A OG1   1 
ATOM   854  C CG2   . THR   A 1 131 ? 15.006  23.35  60.274 1   35.5  ? 112 THR   A CG2   1 
ATOM   855  N N     . TYR   A 1 132 ? 13.794  24.497 56.94  1   29.36 ? 113 TYR   A N     1 
ATOM   856  C CA    . TYR   A 1 132 ? 14.508  25.329 55.971 1   29.22 ? 113 TYR   A CA    1 
ATOM   857  C C     . TYR   A 1 132 ? 13.781  26.667 55.764 1   27.6  ? 113 TYR   A C     1 
ATOM   858  O O     . TYR   A 1 132 ? 14.416  27.722 55.796 1   28.06 ? 113 TYR   A O     1 
ATOM   859  C CB    . TYR   A 1 132 ? 14.724  24.533 54.668 1   29.97 ? 113 TYR   A CB    1 
ATOM   860  C CG    . TYR   A 1 132 ? 15.612  25.218 53.663 1   30.25 ? 113 TYR   A CG    1 
ATOM   861  C CD1   . TYR   A 1 132 ? 15.074  26.015 52.662 1   31.34 ? 113 TYR   A CD1   1 
ATOM   862  C CD2   . TYR   A 1 132 ? 17      25.056 53.696 1   31.18 ? 113 TYR   A CD2   1 
ATOM   863  C CE1   . TYR   A 1 132 ? 15.886  26.657 51.742 1   32.2  ? 113 TYR   A CE1   1 
ATOM   864  C CE2   . TYR   A 1 132 ? 17.814  25.664 52.755 1   32.27 ? 113 TYR   A CE2   1 
ATOM   865  C CZ    . TYR   A 1 132 ? 17.252  26.488 51.8   1   33.11 ? 113 TYR   A CZ    1 
ATOM   866  O OH    . TYR   A 1 132 ? 18.048  27.105 50.87  1   34.22 ? 113 TYR   A OH    1 
ATOM   867  N N     . VAL   A 1 133 ? 12.435  26.65  55.63  1   24.81 ? 114 VAL   A N     1 
ATOM   868  C CA    . VAL   A 1 133 ? 11.67   27.897 55.488 1   24.54 ? 114 VAL   A CA    1 
ATOM   869  C C     . VAL   A 1 133 ? 11.747  28.75  56.77  1   26.56 ? 114 VAL   A C     1 
ATOM   870  O O     . VAL   A 1 133 ? 11.874  29.969 56.68  1   26.34 ? 114 VAL   A O     1 
ATOM   871  C CB    . VAL   A 1 133 ? 10.221  27.62  55.079 1   25.01 ? 114 VAL   A CB    1 
ATOM   872  C CG1   . VAL   A 1 133 ? 9.407   28.923 55.059 1   26.14 ? 114 VAL   A CG1   1 
ATOM   873  C CG2   . VAL   A 1 133 ? 10.195  26.938 53.698 1   25.18 ? 114 VAL   A CG2   1 
ATOM   874  N N     . CYS   A 1 134 ? 11.682  28.115 57.953 1   27.79 ? 115 CYS   A N     1 
ATOM   875  C CA    . CYS   A 1 134 ? 11.805  28.864 59.213 1   29.45 ? 115 CYS   A CA    1 
ATOM   876  C C     . CYS   A 1 134 ? 13.151  29.603 59.283 1   30.28 ? 115 CYS   A C     1 
ATOM   877  O O     . CYS   A 1 134 ? 13.202  30.752 59.716 1   31    ? 115 CYS   A O     1 
ATOM   878  C CB    . CYS   A 1 134 ? 11.623  27.936 60.402 1   30.78 ? 115 CYS   A CB    1 
ATOM   879  S SG    . CYS   A 1 134 ? 9.914   27.421 60.638 1   33.65 ? 115 CYS   A SG    1 
ATOM   880  N N     . ASP   A 1 135 ? 14.215  28.929 58.82  1   30.17 ? 116 ASP   A N     1 
ATOM   881  C CA    . ASP   A 1 135 ? 15.555  29.517 58.744 1   30.99 ? 116 ASP   A CA    1 
ATOM   882  C C     . ASP   A 1 135 ? 15.587  30.72  57.782 1   32.61 ? 116 ASP   A C     1 
ATOM   883  O O     . ASP   A 1 135 ? 16.126  31.764 58.136 1   34.8  ? 116 ASP   A O     1 
ATOM   884  C CB    . ASP   A 1 135 ? 16.565  28.465 58.269 1   32.21 ? 116 ASP   A CB    1 
ATOM   885  C CG    . ASP   A 1 135 ? 16.911  27.401 59.271 1   40.01 ? 116 ASP   A CG    1 
ATOM   886  O OD1   . ASP   A 1 135 ? 16.494  27.535 60.458 1   39.41 ? 116 ASP   A OD1   1 
ATOM   887  O OD2   . ASP   A 1 135 ? 17.609  26.427 58.884 1   45.22 ? 116 ASP   A OD2   1 
ATOM   888  N N     . LEU   A 1 136 ? 15.009  30.564 56.562 1   32.06 ? 117 LEU   A N     1 
ATOM   889  C CA    . LEU   A 1 136 ? 14.987  31.647 55.566 1   32.6  ? 117 LEU   A CA    1 
ATOM   890  C C     . LEU   A 1 136 ? 14.309  32.895 56.119 1   31.75 ? 117 LEU   A C     1 
ATOM   891  O O     . LEU   A 1 136 ? 14.755  34.023 55.863 1   31.3  ? 117 LEU   A O     1 
ATOM   892  C CB    . LEU   A 1 136 ? 14.177  31.201 54.322 1   33.22 ? 117 LEU   A CB    1 
ATOM   893  C CG    . LEU   A 1 136 ? 14.696  30.016 53.501 1   35.93 ? 117 LEU   A CG    1 
ATOM   894  C CD1   . LEU   A 1 136 ? 13.739  29.742 52.316 1   35.99 ? 117 LEU   A CD1   1 
ATOM   895  C CD2   . LEU   A 1 136 ? 16.089  30.26  52.958 1   37.54 ? 117 LEU   A CD2   1 
ATOM   896  N N     . GLU   A 1 137 ? 13.18   32.681 56.842 1   31.45 ? 118 GLU   A N     1 
ATOM   897  C CA    . GLU   A 1 137 ? 12.328  33.735 57.374 1   32.15 ? 118 GLU   A CA    1 
ATOM   898  C C     . GLU   A 1 137 ? 12.872  34.429 58.627 1   34.4  ? 118 GLU   A C     1 
ATOM   899  O O     . GLU   A 1 137 ? 12.243  35.367 59.119 1   36.99 ? 118 GLU   A O     1 
ATOM   900  C CB    . GLU   A 1 137 ? 10.897  33.2   57.59  1   32.96 ? 118 GLU   A CB    1 
ATOM   901  C CG    . GLU   A 1 137 ? 10.245  32.806 56.276 1   33.97 ? 118 GLU   A CG    1 
ATOM   902  C CD    . GLU   A 1 137 ? 8.792   32.37  56.357 1   34.87 ? 118 GLU   A CD    1 
ATOM   903  O OE1   . GLU   A 1 137 ? 8.3     32.18  57.49  1   35.82 ? 118 GLU   A OE1   1 
ATOM   904  O OE2   . GLU   A 1 137 ? 8.155   32.183 55.296 1   30.64 ? 118 GLU   A OE2   1 
ATOM   905  N N     . GLY   A 1 138 ? 14.055  34.039 59.084 1   33.58 ? 119 GLY   A N     1 
ATOM   906  C CA    . GLY   A 1 138 ? 14.71   34.72  60.19  1   34.37 ? 119 GLY   A CA    1 
ATOM   907  C C     . GLY   A 1 138 ? 14.65   34.032 61.533 1   35.33 ? 119 GLY   A C     1 
ATOM   908  O O     . GLY   A 1 138 ? 15.007  34.631 62.556 1   35.95 ? 119 GLY   A O     1 
ATOM   909  N N     . ASN   A 1 139 ? 14.2    32.771 61.55  1   35.56 ? 120 ASN   A N     1 
ATOM   910  C CA    . ASN   A 1 139 ? 14.03   32.013 62.79  1   37.12 ? 120 ASN   A CA    1 
ATOM   911  C C     . ASN   A 1 139 ? 13.12   32.734 63.774 1   38.87 ? 120 ASN   A C     1 
ATOM   912  O O     . ASN   A 1 139 ? 13.359  32.708 64.984 1   39.81 ? 120 ASN   A O     1 
ATOM   913  C CB    . ASN   A 1 139 ? 15.369  31.6   63.41  1   38.72 ? 120 ASN   A CB    1 
ATOM   914  C CG    . ASN   A 1 139 ? 16.085  30.591 62.547 1   41.58 ? 120 ASN   A CG    1 
ATOM   915  O OD1   . ASN   A 1 139 ? 15.69   29.413 62.449 1   43.02 ? 120 ASN   A OD1   1 
ATOM   916  N ND2   . ASN   A 1 139 ? 17.134  31.035 61.881 1   41.25 ? 120 ASN   A ND2   1 
ATOM   917  N N     . ARG   A 1 140 ? 12.103  33.441 63.24  1   39.24 ? 121 ARG   A N     1 
ATOM   918  C CA    . ARG   A 1 140 ? 11.111  34.122 64.066 1   39.75 ? 121 ARG   A CA    1 
ATOM   919  C C     . ARG   A 1 140 ? 10.254  33.069 64.774 1   41.15 ? 121 ARG   A C     1 
ATOM   920  O O     . ARG   A 1 140 ? 9.808   33.304 65.9   1   42.6  ? 121 ARG   A O     1 
ATOM   921  C CB    . ARG   A 1 140 ? 10.204  35.022 63.221 1   40.58 ? 121 ARG   A CB    1 
ATOM   922  C CG    . ARG   A 1 140 ? 10.938  36.023 62.317 1   41.5  ? 121 ARG   A CG    1 
ATOM   923  C CD    . ARG   A 1 140 ? 9.906   36.884 61.605 1   42.68 ? 121 ARG   A CD    1 
ATOM   924  N NE    . ARG   A 1 140 ? 10.486  37.81  60.629 1   43.76 ? 121 ARG   A NE    1 
ATOM   925  C CZ    . ARG   A 1 140 ? 10.832  39.063 60.898 1   45.25 ? 121 ARG   A CZ    1 
ATOM   926  N NH1   . ARG   A 1 140 ? 10.703  39.546 62.131 1   44.83 ? 121 ARG   A NH1   1 
ATOM   927  N NH2   . ARG   A 1 140 ? 11.323  39.839 59.944 1   45.21 ? 121 ARG   A NH2   1 
ATOM   928  N N     . VAL   A 1 141 ? 9.977   31.928 64.103 1   40.73 ? 122 VAL   A N     1 
ATOM   929  C CA    . VAL   A 1 141 ? 9.19    30.825 64.642 1   40.94 ? 122 VAL   A CA    1 
ATOM   930  C C     . VAL   A 1 141 ? 9.908   29.476 64.425 1   40.68 ? 122 VAL   A C     1 
ATOM   931  O O     . VAL   A 1 141 ? 10.814  29.361 63.591 1   41.23 ? 122 VAL   A O     1 
ATOM   932  C CB    . VAL   A 1 141 ? 7.76    30.785 64.039 1   41.54 ? 122 VAL   A CB    1 
ATOM   933  C CG1   . VAL   A 1 141 ? 7.032   32.112 64.209 1   41.98 ? 122 VAL   A CG1   1 
ATOM   934  C CG2   . VAL   A 1 141 ? 7.804   30.368 62.576 1   42.42 ? 122 VAL   A CG2   1 
ATOM   935  N N     . LYS   A 1 142 ? 9.483   28.448 65.164 1   39.45 ? 123 LYS   A N     1 
ATOM   936  C CA    . LYS   A 1 142 ? 9.997   27.104 65.004 1   39.32 ? 123 LYS   A CA    1 
ATOM   937  C C     . LYS   A 1 142 ? 8.994   26.289 64.166 1   38.56 ? 123 LYS   A C     1 
ATOM   938  O O     . LYS   A 1 142 ? 7.868   26.742 63.933 1   38.08 ? 123 LYS   A O     1 
ATOM   939  C CB    . LYS   A 1 142 ? 10.233  26.458 66.367 1   41.57 ? 123 LYS   A CB    1 
ATOM   940  C CG    . LYS   A 1 142 ? 11.245  27.209 67.211 1   46.99 ? 123 LYS   A CG    1 
ATOM   941  C CD    . LYS   A 1 142 ? 11.479  26.469 68.512 1   52.92 ? 123 LYS   A CD    1 
ATOM   942  C CE    . LYS   A 1 142 ? 12.333  27.276 69.452 1   58.48 ? 123 LYS   A CE    1 
ATOM   943  N NZ    . LYS   A 1 142 ? 13.629  27.656 68.827 1   61.21 ? 123 LYS   A NZ    1 
ATOM   944  N N     . GLY   A 1 143 ? 9.408   25.097 63.755 1   38.43 ? 124 GLY   A N     1 
ATOM   945  C CA    . GLY   A 1 143 ? 8.627   24.212 62.889 1   39.5  ? 124 GLY   A CA    1 
ATOM   946  C C     . GLY   A 1 143 ? 7.161   24.026 63.255 1   40.79 ? 124 GLY   A C     1 
ATOM   947  O O     . GLY   A 1 143 ? 6.287   24.25  62.412 1   40.66 ? 124 GLY   A O     1 
ATOM   948  N N     . PRO   A 1 144 ? 6.845   23.602 64.501 1   40.84 ? 125 PRO   A N     1 
ATOM   949  C CA    . PRO   A 1 144 ? 5.434   23.351 64.841 1   41.05 ? 125 PRO   A CA    1 
ATOM   950  C C     . PRO   A 1 144 ? 4.507   24.564 64.676 1   39.9  ? 125 PRO   A C     1 
ATOM   951  O O     . PRO   A 1 144 ? 3.366   24.4   64.223 1   40    ? 125 PRO   A O     1 
ATOM   952  C CB    . PRO   A 1 144 ? 5.498   22.862 66.297 1   42.32 ? 125 PRO   A CB    1 
ATOM   953  C CG    . PRO   A 1 144 ? 6.886   22.321 66.461 1   43.12 ? 125 PRO   A CG    1 
ATOM   954  C CD    . PRO   A 1 144 ? 7.743   23.227 65.618 1   41.1  ? 125 PRO   A CD    1 
ATOM   955  N N     . GLU   A 1 145 ? 4.981   25.76  65.02  1   38.3  ? 126 GLU   A N     1 
ATOM   956  C CA    . GLU   A 1 145 ? 4.189   26.984 64.883 1   37.34 ? 126 GLU   A CA    1 
ATOM   957  C C     . GLU   A 1 145 ? 3.943   27.272 63.389 1   36.6  ? 126 GLU   A C     1 
ATOM   958  O O     . GLU   A 1 145 ? 2.83    27.638 63.008 1   36.96 ? 126 GLU   A O     1 
ATOM   959  C CB    . GLU   A 1 145 ? 4.889   28.177 65.558 1   39.46 ? 126 GLU   A CB    1 
ATOM   960  C CG    . GLU   A 1 145 ? 4.106   29.465 65.403 1   42.56 ? 126 GLU   A CG    1 
ATOM   961  C CD    . GLU   A 1 145 ? 4.573   30.633 66.241 1   49.29 ? 126 GLU   A CD    1 
ATOM   962  O OE1   . GLU   A 1 145 ? 5.531   30.458 67.03  1   49.51 ? 126 GLU   A OE1   1 
ATOM   963  O OE2   . GLU   A 1 145 ? 3.975   31.724 66.107 1   51    ? 126 GLU   A OE2   1 
ATOM   964  N N     . LYS   A 1 146 ? 4.978   27.111 62.56  1   34.16 ? 127 LYS   A N     1 
ATOM   965  C CA    . LYS   A 1 146 ? 4.841   27.301 61.106 1   33.42 ? 127 LYS   A CA    1 
ATOM   966  C C     . LYS   A 1 146 ? 3.792   26.331 60.515 1   32.99 ? 127 LYS   A C     1 
ATOM   967  O O     . LYS   A 1 146 ? 2.893   26.759 59.783 1   32.8  ? 127 LYS   A O     1 
ATOM   968  C CB    . LYS   A 1 146 ? 6.223   27.114 60.435 1   33.51 ? 127 LYS   A CB    1 
ATOM   969  C CG    . LYS   A 1 146 ? 6.193   26.926 58.927 1   36.43 ? 127 LYS   A CG    1 
ATOM   970  C CD    . LYS   A 1 146 ? 6.74    28.101 58.205 1   41.09 ? 127 LYS   A CD    1 
ATOM   971  C CE    . LYS   A 1 146 ? 5.654   29.098 57.949 1   42.57 ? 127 LYS   A CE    1 
ATOM   972  N NZ    . LYS   A 1 146 ? 6.213   30.416 57.514 1   39.81 ? 127 LYS   A NZ    1 
ATOM   973  N N     . GLU   A 1 147 ? 3.892   25.045 60.845 1   33.2  ? 128 GLU   A N     1 
ATOM   974  C CA    . GLU   A 1 147 ? 2.937   24.057 60.348 1   33.21 ? 128 GLU   A CA    1 
ATOM   975  C C     . GLU   A 1 147 ? 1.526   24.352 60.793 1   33.8  ? 128 GLU   A C     1 
ATOM   976  O O     . GLU   A 1 147 ? 0.592   24.2   60.007 1   33.73 ? 128 GLU   A O     1 
ATOM   977  C CB    . GLU   A 1 147 ? 3.296   22.649 60.818 1   33.9  ? 128 GLU   A CB    1 
ATOM   978  C CG    . GLU   A 1 147 ? 4.588   22.12  60.229 1   36.44 ? 128 GLU   A CG    1 
ATOM   979  C CD    . GLU   A 1 147 ? 4.806   20.634 60.437 1   41.06 ? 128 GLU   A CD    1 
ATOM   980  O OE1   . GLU   A 1 147 ? 4.018   20.009 61.191 1   41.23 ? 128 GLU   A OE1   1 
ATOM   981  O OE2   . GLU   A 1 147 ? 5.768   20.088 59.837 1   41.64 ? 128 GLU   A OE2   1 
ATOM   982  N N     . GLU   A 1 148 ? 1.361   24.788 62.068 1   34.57 ? 129 GLU   A N     1 
ATOM   983  C CA    . GLU   A 1 148 ? 0.014   25.098 62.547 1   35.38 ? 129 GLU   A CA    1 
ATOM   984  C C     . GLU   A 1 148 ? -0.563  26.29  61.794 1   35.05 ? 129 GLU   A C     1 
ATOM   985  O O     . GLU   A 1 148 ? -1.748  26.27  61.45  1   36.88 ? 129 GLU   A O     1 
ATOM   986  C CB    . GLU   A 1 148 ? -0.002  25.339 64.066 1   36.88 ? 129 GLU   A CB    1 
ATOM   987  C CG    . GLU   A 1 148 ? -1.373  25.698 64.621 1   45.7  ? 129 GLU   A CG    1 
ATOM   988  C CD    . GLU   A 1 148 ? -2.484  24.663 64.528 1   53.76 ? 129 GLU   A CD    1 
ATOM   989  O OE1   . GLU   A 1 148 ? -2.22   23.505 64.122 1   53.15 ? 129 GLU   A OE1   1 
ATOM   990  O OE2   . GLU   A 1 148 ? -3.631  25.022 64.881 1   57.24 ? 129 GLU   A OE2   1 
ATOM   991  N N     . LYS   A 1 149 ? 0.262   27.288 61.495 1   33.57 ? 130 LYS   A N     1 
ATOM   992  C CA    . LYS   A 1 149 ? -0.193  28.446 60.731 1   34.19 ? 130 LYS   A CA    1 
ATOM   993  C C     . LYS   A 1 149 ? -0.692  28.028 59.321 1   33.04 ? 130 LYS   A C     1 
ATOM   994  O O     . LYS   A 1 149 ? -1.758  28.476 58.868 1   33.13 ? 130 LYS   A O     1 
ATOM   995  C CB    . LYS   A 1 149 ? 0.907   29.487 60.615 1   36.99 ? 130 LYS   A CB    1 
ATOM   996  C CG    . LYS   A 1 149 ? 0.33    30.792 60.126 1   42.58 ? 130 LYS   A CG    1 
ATOM   997  C CD    . LYS   A 1 149 ? 1.26    31.929 60.358 1   49.6  ? 130 LYS   A CD    1 
ATOM   998  C CE    . LYS   A 1 149 ? 0.517   33.206 60.635 1   54.78 ? 130 LYS   A CE    1 
ATOM   999  N NZ    . LYS   A 1 149 ? 1.472   34.334 60.817 1   57.98 ? 130 LYS   A NZ    1 
ATOM   1000 N N     . LEU   A 1 150 ? 0.026   27.098 58.688 1   30.39 ? 131 LEU   A N     1 
ATOM   1001 C CA    . LEU   A 1 150 ? -0.411  26.615 57.382 1   29.31 ? 131 LEU   A CA    1 
ATOM   1002 C C     . LEU   A 1 150 ? -1.699  25.811 57.486 1   30.39 ? 131 LEU   A C     1 
ATOM   1003 O O     . LEU   A 1 150 ? -2.631  26.016 56.7   1   30.38 ? 131 LEU   A O     1 
ATOM   1004 C CB    . LEU   A 1 150 ? 0.697   25.814 56.714 1   28.12 ? 131 LEU   A CB    1 
ATOM   1005 C CG    . LEU   A 1 150 ? 0.294   25.188 55.355 1   26.44 ? 131 LEU   A CG    1 
ATOM   1006 C CD1   . LEU   A 1 150 ? -0.222  26.274 54.346 1   27.67 ? 131 LEU   A CD1   1 
ATOM   1007 C CD2   . LEU   A 1 150 ? 1.46    24.433 54.751 1   27.77 ? 131 LEU   A CD2   1 
ATOM   1008 N N     . ARG   A 1 151 ? -1.796  24.928 58.481 1   30.72 ? 132 ARG   A N     1 
ATOM   1009 C CA    . ARG   A 1 151 ? -3.007  24.123 58.655 1   32.57 ? 132 ARG   A CA    1 
ATOM   1010 C C     . ARG   A 1 151 ? -4.225  25.011 58.89  1   33.9  ? 132 ARG   A C     1 
ATOM   1011 O O     . ARG   A 1 151 ? -5.288  24.734 58.341 1   34.85 ? 132 ARG   A O     1 
ATOM   1012 C CB    . ARG   A 1 151 ? -2.812  23.119 59.792 1   32.63 ? 132 ARG   A CB    1 
ATOM   1013 C CG    . ARG   A 1 151 ? -1.841  22.005 59.417 1   33.73 ? 132 ARG   A CG    1 
ATOM   1014 C CD    . ARG   A 1 151 ? -1.703  20.969 60.529 1   35.3  ? 132 ARG   A CD    1 
ATOM   1015 N NE    . ARG   A 1 151 ? -0.975  19.792 60.037 1   35.15 ? 132 ARG   A NE    1 
ATOM   1016 C CZ    . ARG   A 1 151 ? 0.233   19.427 60.457 1   36.2  ? 132 ARG   A CZ    1 
ATOM   1017 N NH1   . ARG   A 1 151 ? 0.836   20.098 61.439 1   35.9  ? 132 ARG   A NH1   1 
ATOM   1018 N NH2   . ARG   A 1 151 ? 0.834   18.367 59.926 1   35.73 ? 132 ARG   A NH2   1 
ATOM   1019 N N     . GLN   A 1 152 ? -4.05   26.117 59.656 1   35.05 ? 133 GLN   A N     1 
ATOM   1020 C CA    . GLN   A 1 152 ? -5.165  27.028 59.889 1   36.79 ? 133 GLN   A CA    1 
ATOM   1021 C C     . GLN   A 1 152 ? -5.546  27.829 58.653 1   36.22 ? 133 GLN   A C     1 
ATOM   1022 O O     . GLN   A 1 152 ? -6.708  28.199 58.51  1   37.19 ? 133 GLN   A O     1 
ATOM   1023 C CB    . GLN   A 1 152 ? -4.882  27.976 61.069 1   40.73 ? 133 GLN   A CB    1 
ATOM   1024 C CG    . GLN   A 1 152 ? -4.775  27.26  62.408 1   47.44 ? 133 GLN   A CG    1 
ATOM   1025 C CD    . GLN   A 1 152 ? -6.103  26.681 62.836 1   54.75 ? 133 GLN   A CD    1 
ATOM   1026 O OE1   . GLN   A 1 152 ? -7.171  27.246 62.565 1   57.32 ? 133 GLN   A OE1   1 
ATOM   1027 N NE2   . GLN   A 1 152 ? -6.066  25.543 63.524 1   55.98 ? 133 GLN   A NE2   1 
ATOM   1028 N N     . ALA   A 1 153 ? -4.599  28.055 57.735 1   33.99 ? 134 ALA   A N     1 
ATOM   1029 C CA    . ALA   A 1 153 ? -4.878  28.832 56.53  1   34.07 ? 134 ALA   A CA    1 
ATOM   1030 C C     . ALA   A 1 153 ? -5.644  28.077 55.477 1   33.27 ? 134 ALA   A C     1 
ATOM   1031 O O     . ALA   A 1 153 ? -6.418  28.676 54.742 1   32.9  ? 134 ALA   A O     1 
ATOM   1032 C CB    . ALA   A 1 153 ? -3.589  29.339 55.935 1   33.41 ? 134 ALA   A CB    1 
ATOM   1033 N N     . VAL   A 1 154 ? -5.47   26.753 55.421 1   33.66 ? 135 VAL   A N     1 
ATOM   1034 C CA    . VAL   A 1 154 ? -6.128  25.952 54.392 1   34.74 ? 135 VAL   A CA    1 
ATOM   1035 C C     . VAL   A 1 154 ? -7.515  25.502 54.83  1   37.25 ? 135 VAL   A C     1 
ATOM   1036 O O     . VAL   A 1 154 ? -7.61   24.648 55.701 1   37.34 ? 135 VAL   A O     1 
ATOM   1037 C CB    . VAL   A 1 154 ? -5.219  24.767 53.978 1   33.95 ? 135 VAL   A CB    1 
ATOM   1038 C CG1   . VAL   A 1 154 ? -5.872  23.966 52.864 1   34.44 ? 135 VAL   A CG1   1 
ATOM   1039 C CG2   . VAL   A 1 154 ? -3.82   25.258 53.569 1   33.03 ? 135 VAL   A CG2   1 
ATOM   1040 N N     . LYS   A 1 155 ? -8.595  26.046 54.232 1   38.84 ? 136 LYS   A N     1 
ATOM   1041 C CA    . LYS   A 1 155 ? -9.969  25.639 54.59  1   39.97 ? 136 LYS   A CA    1 
ATOM   1042 C C     . LYS   A 1 155 ? -10.657 24.807 53.525 1   38.39 ? 136 LYS   A C     1 
ATOM   1043 O O     . LYS   A 1 155 ? -11.604 24.079 53.828 1   40.26 ? 136 LYS   A O     1 
ATOM   1044 C CB    . LYS   A 1 155 ? -10.862 26.846 54.904 1   44.42 ? 136 LYS   A CB    1 
ATOM   1045 C CG    . LYS   A 1 155 ? -10.235 27.836 55.858 1   51.54 ? 136 LYS   A CG    1 
ATOM   1046 C CD    . LYS   A 1 155 ? -10.17  27.299 57.275 1   57.37 ? 136 LYS   A CD    1 
ATOM   1047 C CE    . LYS   A 1 155 ? -10.036 28.438 58.255 1   61.8  ? 136 LYS   A CE    1 
ATOM   1048 N NZ    . LYS   A 1 155 ? -9.068  29.459 57.768 1   64.39 ? 136 LYS   A NZ    1 
ATOM   1049 N N     . GLN   A 1 156 ? -10.209 24.929 52.252 1   34.62 ? 137 GLN   A N     1 
ATOM   1050 C CA    . GLN   A 1 156 ? -10.835 24.205 51.166 1   30.73 ? 137 GLN   A CA    1 
ATOM   1051 C C     . GLN   A 1 156 ? -9.793  23.479 50.333 1   28.8  ? 137 GLN   A C     1 
ATOM   1052 O O     . GLN   A 1 156 ? -8.721  24.025 50.074 1   28.9  ? 137 GLN   A O     1 
ATOM   1053 C CB    . GLN   A 1 156 ? -11.639 25.151 50.281 1   31.52 ? 137 GLN   A CB    1 
ATOM   1054 C CG    . GLN   A 1 156 ? -12.635 26.023 51.089 1   33.62 ? 137 GLN   A CG    1 
ATOM   1055 C CD    . GLN   A 1 156 ? -13.452 26.912 50.206 1   38.54 ? 137 GLN   A CD    1 
ATOM   1056 O OE1   . GLN   A 1 156 ? -14.243 26.457 49.378 1   38.51 ? 137 GLN   A OE1   1 
ATOM   1057 N NE2   . GLN   A 1 156 ? -13.259 28.204 50.354 1   39.58 ? 137 GLN   A NE2   1 
ATOM   1058 N N     . VAL   A 1 157 ? -10.094 22.252 49.968 1   27.33 ? 138 VAL   A N     1 
ATOM   1059 C CA    . VAL   A 1 157 ? -9.25   21.364 49.186 1   26.93 ? 138 VAL   A CA    1 
ATOM   1060 C C     . VAL   A 1 157 ? -10.162 20.928 48.048 1   27.36 ? 138 VAL   A C     1 
ATOM   1061 O O     . VAL   A 1 157 ? -11.132 20.206 48.284 1   29.2  ? 138 VAL   A O     1 
ATOM   1062 C CB    . VAL   A 1 157 ? -8.8    20.195 50.081 1   28.12 ? 138 VAL   A CB    1 
ATOM   1063 C CG1   . VAL   A 1 157 ? -7.997  19.185 49.287 1   29.41 ? 138 VAL   A CG1   1 
ATOM   1064 C CG2   . VAL   A 1 157 ? -7.992  20.702 51.279 1   29.47 ? 138 VAL   A CG2   1 
ATOM   1065 N N     . LEU   A 1 158 ? -9.918  21.446 46.827 1   26.1  ? 139 LEU   A N     1 
ATOM   1066 C CA    . LEU   A 1 158 ? -10.836 21.338 45.716 1   24.61 ? 139 LEU   A CA    1 
ATOM   1067 C C     . LEU   A 1 158 ? -10.293 20.726 44.478 1   23.69 ? 139 LEU   A C     1 
ATOM   1068 O O     . LEU   A 1 158 ? -9.13   20.911 44.141 1   22.83 ? 139 LEU   A O     1 
ATOM   1069 C CB    . LEU   A 1 158 ? -11.317 22.771 45.334 1   25.27 ? 139 LEU   A CB    1 
ATOM   1070 C CG    . LEU   A 1 158 ? -11.911 23.611 46.45  1   28.09 ? 139 LEU   A CG    1 
ATOM   1071 C CD1   . LEU   A 1 158 ? -12.228 24.994 45.96  1   28.02 ? 139 LEU   A CD1   1 
ATOM   1072 C CD2   . LEU   A 1 158 ? -13.175 22.969 46.943 1   28.4  ? 139 LEU   A CD2   1 
ATOM   1073 N N     . LYS   A 1 159 ? -11.154 20.136 43.693 1   23.45 ? 140 LYS   A N     1 
ATOM   1074 C CA    . LYS   A 1 159 ? -10.865 19.66  42.38  1   24.02 ? 140 LYS   A CA    1 
ATOM   1075 C C     . LYS   A 1 159 ? -10.691 20.844 41.427 1   24.97 ? 140 LYS   A C     1 
ATOM   1076 O O     . LYS   A 1 159 ? -11.446 21.834 41.474 1   25.95 ? 140 LYS   A O     1 
ATOM   1077 C CB    . LYS   A 1 159 ? -12.068 18.827 41.919 1   27.34 ? 140 LYS   A CB    1 
ATOM   1078 C CG    . LYS   A 1 159 ? -11.96  18.293 40.512 1   34.78 ? 140 LYS   A CG    1 
ATOM   1079 C CD    . LYS   A 1 159 ? -11.06  17.102 40.544 1   43.01 ? 140 LYS   A CD    1 
ATOM   1080 C CE    . LYS   A 1 159 ? -11.56  16.014 39.651 1   48.1  ? 140 LYS   A CE    1 
ATOM   1081 N NZ    . LYS   A 1 159 ? -10.877 14.757 39.977 1   49.65 ? 140 LYS   A NZ    1 
ATOM   1082 N N     A CYS   A 1 160 ? -9.701  20.754 40.55  0.5 22.96 ? 141 CYS   A N     1 
ATOM   1083 N N     B CYS   A 1 160 ? -9.701  20.73  40.551 0.5 23.43 ? 141 CYS   A N     1 
ATOM   1084 C CA    A CYS   A 1 160 ? -9.524  21.755 39.522 0.5 22.28 ? 141 CYS   A CA    1 
ATOM   1085 C CA    B CYS   A 1 160 ? -9.388  21.756 39.591 0.5 23.09 ? 141 CYS   A CA    1 
ATOM   1086 C C     A CYS   A 1 160 ? -9.089  21.128 38.22  0.5 20.61 ? 141 CYS   A C     1 
ATOM   1087 C C     B CYS   A 1 160 ? -9.008  21.149 38.241 0.5 21.02 ? 141 CYS   A C     1 
ATOM   1088 O O     A CYS   A 1 160 ? -8.483  20.051 38.2   0.5 20.84 ? 141 CYS   A O     1 
ATOM   1089 O O     B CYS   A 1 160 ? -8.307  20.136 38.208 0.5 21.21 ? 141 CYS   A O     1 
ATOM   1090 C CB    A CYS   A 1 160 ? -8.563  22.844 39.973 0.5 22.78 ? 141 CYS   A CB    1 
ATOM   1091 C CB    B CYS   A 1 160 ? -8.247  22.592 40.157 0.5 24.47 ? 141 CYS   A CB    1 
ATOM   1092 S SG    A CYS   A 1 160 ? -6.832  22.329 39.97  0.5 21.06 ? 141 CYS   A SG    1 
ATOM   1093 S SG    B CYS   A 1 160 ? -7.487  23.721 38.972 0.5 25.29 ? 141 CYS   A SG    1 
ATOM   1094 N N     . ASP   A 1 161 ? -9.38   21.821 37.113 1   19.88 ? 142 ASP   A N     1 
ATOM   1095 C CA    . ASP   A 1 161 ? -8.916  21.407 35.806 1   18.36 ? 142 ASP   A CA    1 
ATOM   1096 C C     . ASP   A 1 161 ? -8.552  22.715 35.087 1   19.01 ? 142 ASP   A C     1 
ATOM   1097 O O     . ASP   A 1 161 ? -9.44   23.463 34.666 1   20.71 ? 142 ASP   A O     1 
ATOM   1098 C CB    . ASP   A 1 161 ? -9.969  20.627 35.001 1   19.48 ? 142 ASP   A CB    1 
ATOM   1099 C CG    . ASP   A 1 161 ? -9.483  20.172 33.647 1   19.5  ? 142 ASP   A CG    1 
ATOM   1100 O OD1   . ASP   A 1 161 ? -8.393  20.647 33.195 1   19.92 ? 142 ASP   A OD1   1 
ATOM   1101 O OD2   . ASP   A 1 161 ? -10.228 19.427 32.969 1   21.04 ? 142 ASP   A OD2   1 
ATOM   1102 N N     . VAL   A 1 162 ? -7.256  22.979 34.952 1   17.37 ? 143 VAL   A N     1 
ATOM   1103 C CA    . VAL   A 1 162 ? -6.814  24.264 34.353 1   18.19 ? 143 VAL   A CA    1 
ATOM   1104 C C     . VAL   A 1 162 ? -7.222  24.431 32.906 1   19.87 ? 143 VAL   A C     1 
ATOM   1105 O O     . VAL   A 1 162 ? -7.128  25.559 32.376 1   19.44 ? 143 VAL   A O     1 
ATOM   1106 C CB    . VAL   A 1 162 ? -5.292  24.481 34.48  1   18.09 ? 143 VAL   A CB    1 
ATOM   1107 C CG1   . VAL   A 1 162 ? -4.848  24.388 35.905 1   18.85 ? 143 VAL   A CG1   1 
ATOM   1108 C CG2   . VAL   A 1 162 ? -4.51   23.52  33.611 1   18.46 ? 143 VAL   A CG2   1 
ATOM   1109 N N     . THR   A 1 163 ? -7.557  23.322 32.214 1   19.22 ? 144 THR   A N     1 
ATOM   1110 C CA    . THR   A 1 163 ? -7.911  23.448 30.79  1   20.74 ? 144 THR   A CA    1 
ATOM   1111 C C     . THR   A 1 163 ? -9.353  23.908 30.581 1   22.22 ? 144 THR   A C     1 
ATOM   1112 O O     . THR   A 1 163 ? -9.741  24.114 29.416 1   23.62 ? 144 THR   A O     1 
ATOM   1113 C CB    . THR   A 1 163 ? -7.697  22.121 30.051 1   22.29 ? 144 THR   A CB    1 
ATOM   1114 O OG1   . THR   A 1 163 ? -8.642  21.163 30.509 1   24.03 ? 144 THR   A OG1   1 
ATOM   1115 C CG2   . THR   A 1 163 ? -6.312  21.551 30.27  1   21.93 ? 144 THR   A CG2   1 
ATOM   1116 N N     . GLN   A 1 164 ? -10.135 24.059 31.653 1   21.06 ? 145 GLN   A N     1 
ATOM   1117 C CA    . GLN   A 1 164 ? -11.536 24.447 31.499 1   22.06 ? 145 GLN   A CA    1 
ATOM   1118 C C     . GLN   A 1 164 ? -11.703 25.911 31.799 1   23.29 ? 145 GLN   A C     1 
ATOM   1119 O O     . GLN   A 1 164 ? -11.029 26.489 32.681 1   23.4  ? 145 GLN   A O     1 
ATOM   1120 C CB    . GLN   A 1 164 ? -12.387 23.655 32.471 1   23.45 ? 145 GLN   A CB    1 
ATOM   1121 C CG    . GLN   A 1 164 ? -12.283 22.136 32.239 1   26.04 ? 145 GLN   A CG    1 
ATOM   1122 C CD    . GLN   A 1 164 ? -12.608 21.742 30.82  1   28.21 ? 145 GLN   A CD    1 
ATOM   1123 O OE1   . GLN   A 1 164 ? -13.621 22.167 30.244 1   29.58 ? 145 GLN   A OE1   1 
ATOM   1124 N NE2   . GLN   A 1 164 ? -11.784 20.959 30.172 1   34.3  ? 145 GLN   A NE2   1 
ATOM   1125 N N     . SER   A 1 165 ? -12.683 26.527 31.105 1   24.1  ? 146 SER   A N     1 
ATOM   1126 C CA    . SER   A 1 165 ? -12.989 27.946 31.287 1   25.51 ? 146 SER   A CA    1 
ATOM   1127 C C     . SER   A 1 165 ? -13.306 28.258 32.764 1   26.86 ? 146 SER   A C     1 
ATOM   1128 O O     . SER   A 1 165 ? -12.994 29.369 33.243 1   27.44 ? 146 SER   A O     1 
ATOM   1129 C CB    . SER   A 1 165 ? -14.149 28.367 30.379 1   29.43 ? 146 SER   A CB    1 
ATOM   1130 O OG    . SER   A 1 165 ? -13.763 28.198 29.017 1   32.19 ? 146 SER   A OG    1 
ATOM   1131 N N     . GLN   A 1 166 ? -13.932 27.323 33.452 1   27.08 ? 147 GLN   A N     1 
ATOM   1132 C CA    . GLN   A 1 166 ? -14.168 27.431 34.878 1   27.5  ? 147 GLN   A CA    1 
ATOM   1133 C C     . GLN   A 1 166 ? -13.299 26.319 35.505 1   26.91 ? 147 GLN   A C     1 
ATOM   1134 O O     . GLN   A 1 166 ? -13.75  25.17  35.608 1   27.87 ? 147 GLN   A O     1 
ATOM   1135 C CB    . GLN   A 1 166 ? -15.635 27.226 35.201 1   30.31 ? 147 GLN   A CB    1 
ATOM   1136 C CG    . GLN   A 1 166 ? -16.493 28.413 34.766 1   32.75 ? 147 GLN   A CG    1 
ATOM   1137 C CD    . GLN   A 1 166 ? -16.756 28.499 33.261 1   35.31 ? 147 GLN   A CD    1 
ATOM   1138 O OE1   . GLN   A 1 166 ? -16.398 29.507 32.588 1   39.81 ? 147 GLN   A OE1   1 
ATOM   1139 N NE2   . GLN   A 1 166 ? -17.359 27.468 32.705 1   33.59 ? 147 GLN   A NE2   1 
ATOM   1140 N N     . PRO   A 1 167 ? -12.057 26.603 35.938 1   24.15 ? 148 PRO   A N     1 
ATOM   1141 C CA    . PRO   A 1 167 ? -11.202 25.51  36.448 1   24.09 ? 148 PRO   A CA    1 
ATOM   1142 C C     . PRO   A 1 167 ? -11.733 24.821 37.69  1   25.37 ? 148 PRO   A C     1 
ATOM   1143 O O     . PRO   A 1 167 ? -11.458 23.622 37.878 1   25.67 ? 148 PRO   A O     1 
ATOM   1144 C CB    . PRO   A 1 167 ? -9.877  26.211 36.754 1   23.51 ? 148 PRO   A CB    1 
ATOM   1145 C CG    . PRO   A 1 167 ? -9.85   27.385 35.832 1   24.83 ? 148 PRO   A CG    1 
ATOM   1146 C CD    . PRO   A 1 167 ? -11.301 27.871 35.817 1   23.85 ? 148 PRO   A CD    1 
ATOM   1147 N N     . LEU   A 1 168 ? -12.5   25.503 38.512 1   26.16 ? 149 LEU   A N     1 
ATOM   1148 C CA    . LEU   A 1 168 ? -13.048 24.923 39.721 1   26.79 ? 149 LEU   A CA    1 
ATOM   1149 C C     . LEU   A 1 168 ? -14.452 24.38  39.533 1   27.21 ? 149 LEU   A C     1 
ATOM   1150 O O     . LEU   A 1 168 ? -15.091 24.057 40.532 1   28.46 ? 149 LEU   A O     1 
ATOM   1151 C CB    . LEU   A 1 168 ? -12.984 25.897 40.893 1   27.4  ? 149 LEU   A CB    1 
ATOM   1152 C CG    . LEU   A 1 168 ? -11.601 26.539 41.119 1   28.79 ? 149 LEU   A CG    1 
ATOM   1153 C CD1   . LEU   A 1 168 ? -11.642 27.501 42.251 1   31.23 ? 149 LEU   A CD1   1 
ATOM   1154 C CD2   . LEU   A 1 168 ? -10.53  25.493 41.333 1   28.99 ? 149 LEU   A CD2   1 
ATOM   1155 N N     . GLY   A 1 169 ? -14.898 24.275 38.279 1   28.8  ? 150 GLY   A N     1 
ATOM   1156 C CA    . GLY   A 1 169 ? -16.21  23.731 37.933 1   29.52 ? 150 GLY   A CA    1 
ATOM   1157 C C     . GLY   A 1 169 ? -17.366 24.493 38.541 1   31.71 ? 150 GLY   A C     1 
ATOM   1158 O O     . GLY   A 1 169 ? -17.475 25.704 38.378 1   33.54 ? 150 GLY   A O     1 
ATOM   1159 N N     . ALA   A 1 170 ? -18.259 23.776 39.236 1   32.66 ? 151 ALA   A N     1 
ATOM   1160 C CA    . ALA   A 1 170 ? -19.407 24.411 39.853 1   33.45 ? 151 ALA   A CA    1 
ATOM   1161 C C     . ALA   A 1 170 ? -19.109 25.097 41.176 1   34.45 ? 151 ALA   A C     1 
ATOM   1162 O O     . ALA   A 1 170 ? -19.979 25.792 41.69  1   36.01 ? 151 ALA   A O     1 
ATOM   1163 C CB    . ALA   A 1 170 ? -20.533 23.384 40.029 1   34.74 ? 151 ALA   A CB    1 
ATOM   1164 N N     . VAL   A 1 171 ? -17.864 24.972 41.72  1   32.26 ? 152 VAL   A N     1 
ATOM   1165 C CA    . VAL   A 1 171 ? -17.579 25.555 43.02  1   32.41 ? 152 VAL   A CA    1 
ATOM   1166 C C     . VAL   A 1 171 ? -17.277 27.032 42.916 1   32.67 ? 152 VAL   A C     1 
ATOM   1167 O O     . VAL   A 1 171 ? -16.305 27.42  42.271 1   33.43 ? 152 VAL   A O     1 
ATOM   1168 C CB    . VAL   A 1 171 ? -16.428 24.819 43.744 1   33.81 ? 152 VAL   A CB    1 
ATOM   1169 C CG1   . VAL   A 1 171 ? -16.083 25.504 45.075 1   34.73 ? 152 VAL   A CG1   1 
ATOM   1170 C CG2   . VAL   A 1 171 ? -16.758 23.351 43.938 1   34.45 ? 152 VAL   A CG2   1 
ATOM   1171 N N     . PRO   A 1 172 ? -18.029 27.856 43.646 1   31.65 ? 153 PRO   A N     1 
ATOM   1172 C CA    . PRO   A 1 172 ? -17.76  29.289 43.603 1   32.47 ? 153 PRO   A CA    1 
ATOM   1173 C C     . PRO   A 1 172 ? -16.734 29.719 44.641 1   33.86 ? 153 PRO   A C     1 
ATOM   1174 O O     . PRO   A 1 172 ? -16.682 29.181 45.742 1   35.53 ? 153 PRO   A O     1 
ATOM   1175 C CB    . PRO   A 1 172 ? -19.116 29.897 43.934 1   34.16 ? 153 PRO   A CB    1 
ATOM   1176 C CG    . PRO   A 1 172 ? -19.741 28.925 44.871 1   33.89 ? 153 PRO   A CG    1 
ATOM   1177 C CD    . PRO   A 1 172 ? -19.229 27.549 44.452 1   31.71 ? 153 PRO   A CD    1 
ATOM   1178 N N     . LEU   A 1 173 ? -15.915 30.685 44.278 1   32.3  ? 154 LEU   A N     1 
ATOM   1179 C CA    . LEU   A 1 173 ? -14.958 31.275 45.199 1   31.28 ? 154 LEU   A CA    1 
ATOM   1180 C C     . LEU   A 1 173 ? -14.943 32.761 44.958 1   31.01 ? 154 LEU   A C     1 
ATOM   1181 O O     . LEU   A 1 173 ? -15.126 33.211 43.822 1   32.63 ? 154 LEU   A O     1 
ATOM   1182 C CB    . LEU   A 1 173 ? -13.519 30.762 44.916 1   32.19 ? 154 LEU   A CB    1 
ATOM   1183 C CG    . LEU   A 1 173 ? -13.132 29.388 45.45  1   33.38 ? 154 LEU   A CG    1 
ATOM   1184 C CD1   . LEU   A 1 173 ? -11.633 29.181 45.245 1   32.91 ? 154 LEU   A CD1   1 
ATOM   1185 C CD2   . LEU   A 1 173 ? -13.399 29.243 46.924 1   34.61 ? 154 LEU   A CD2   1 
ATOM   1186 N N     . PRO   A 1 174 ? -14.587 33.575 45.97  1   31.28 ? 155 PRO   A N     1 
ATOM   1187 C CA    . PRO   A 1 174 ? -14.385 35.008 45.728 1   31.94 ? 155 PRO   A CA    1 
ATOM   1188 C C     . PRO   A 1 174 ? -13.194 35.18  44.78  1   30.6  ? 155 PRO   A C     1 
ATOM   1189 O O     . PRO   A 1 174 ? -12.319 34.307 44.741 1   30.17 ? 155 PRO   A O     1 
ATOM   1190 C CB    . PRO   A 1 174 ? -13.964 35.534 47.113 1   32.72 ? 155 PRO   A CB    1 
ATOM   1191 C CG    . PRO   A 1 174 ? -14.415 34.538 48.081 1   34.34 ? 155 PRO   A CG    1 
ATOM   1192 C CD    . PRO   A 1 174 ? -14.322 33.221 47.377 1   32.15 ? 155 PRO   A CD    1 
ATOM   1193 N N     . PRO   A 1 175 ? -13.101 36.278 44.027 1   29.86 ? 156 PRO   A N     1 
ATOM   1194 C CA    . PRO   A 1 175 ? -11.89  36.519 43.22  1   29    ? 156 PRO   A CA    1 
ATOM   1195 C C     . PRO   A 1 175 ? -10.67  36.554 44.152 1   29.28 ? 156 PRO   A C     1 
ATOM   1196 O O     . PRO   A 1 175 ? -10.707 37.188 45.198 1   31.38 ? 156 PRO   A O     1 
ATOM   1197 C CB    . PRO   A 1 175 ? -12.158 37.898 42.581 1   30.08 ? 156 PRO   A CB    1 
ATOM   1198 C CG    . PRO   A 1 175 ? -13.729 38.073 42.669 1   31.03 ? 156 PRO   A CG    1 
ATOM   1199 C CD    . PRO   A 1 175 ? -14.013 37.439 43.995 1   30.07 ? 156 PRO   A CD    1 
ATOM   1200 N N     . ALA   A 1 176 ? -9.607  35.825 43.789 1   25.61 ? 157 ALA   A N     1 
ATOM   1201 C CA    . ALA   A 1 176 ? -8.443  35.732 44.645 1   24.27 ? 157 ALA   A CA    1 
ATOM   1202 C C     . ALA   A 1 176 ? -7.523  36.934 44.514 1   22.29 ? 157 ALA   A C     1 
ATOM   1203 O O     . ALA   A 1 176 ? -7.492  37.643 43.481 1   23.08 ? 157 ALA   A O     1 
ATOM   1204 C CB    . ALA   A 1 176 ? -7.675  34.453 44.312 1   24.43 ? 157 ALA   A CB    1 
ATOM   1205 N N     . ASP   A 1 177 ? -6.759  37.169 45.549 1   22.48 ? 158 ASP   A N     1 
ATOM   1206 C CA    . ASP   A 1 177 ? -5.72   38.174 45.512 1   23.15 ? 158 ASP   A CA    1 
ATOM   1207 C C     . ASP   A 1 177 ? -4.465  37.663 44.76  1   22.33 ? 158 ASP   A C     1 
ATOM   1208 O O     . ASP   A 1 177 ? -3.681  38.451 44.246 1   22.85 ? 158 ASP   A O     1 
ATOM   1209 C CB    . ASP   A 1 177 ? -5.391  38.595 46.935 1   26.47 ? 158 ASP   A CB    1 
ATOM   1210 C CG    . ASP   A 1 177 ? -6.637  39.133 47.619 1   33.72 ? 158 ASP   A CG    1 
ATOM   1211 O OD1   . ASP   A 1 177 ? -7.076  40.265 47.26  1   36.93 ? 158 ASP   A OD1   1 
ATOM   1212 O OD2   . ASP   A 1 177 ? -7.218  38.398 48.445 1   32.25 ? 158 ASP   A OD2   1 
ATOM   1213 N N     . CYS   A 1 178 ? -4.234  36.315 44.784 1   21.02 ? 159 CYS   A N     1 
ATOM   1214 C CA    . CYS   A 1 178 ? -3.094  35.707 44.13  1   20.16 ? 159 CYS   A CA    1 
ATOM   1215 C C     . CYS   A 1 178 ? -3.489  34.322 43.684 1   20.19 ? 159 CYS   A C     1 
ATOM   1216 O O     . CYS   A 1 178 ? -4.188  33.614 44.404 1   20.36 ? 159 CYS   A O     1 
ATOM   1217 C CB    . CYS   A 1 178 ? -1.924  35.634 45.11  1   18.51 ? 159 CYS   A CB    1 
ATOM   1218 S SG    . CYS   A 1 178 ? -0.436  34.853 44.41  1   21.92 ? 159 CYS   A SG    1 
ATOM   1219 N N     . VAL   A 1 179 ? -2.989  33.943 42.509 1   17.8  ? 160 VAL   A N     1 
ATOM   1220 C CA    . VAL   A 1 179 ? -3.092  32.56  42.01  1   18.29 ? 160 VAL   A CA    1 
ATOM   1221 C C     . VAL   A 1 179 ? -1.632  32.1   41.857 1   17.69 ? 160 VAL   A C     1 
ATOM   1222 O O     . VAL   A 1 179 ? -0.829  32.786 41.204 1   17.87 ? 160 VAL   A O     1 
ATOM   1223 C CB    . VAL   A 1 179 ? -3.869  32.486 40.702 1   19.94 ? 160 VAL   A CB    1 
ATOM   1224 C CG1   . VAL   A 1 179 ? -3.63   31.127 40.047 1   20.35 ? 160 VAL   A CG1   1 
ATOM   1225 C CG2   . VAL   A 1 179 ? -5.392  32.667 40.96  1   19.91 ? 160 VAL   A CG2   1 
ATOM   1226 N N     . LEU   A 1 180 ? -1.317  30.965 42.467 1   17.47 ? 161 LEU   A N     1 
ATOM   1227 C CA    . LEU   A 1 180 ? 0.024   30.374 42.449 1   16.52 ? 161 LEU   A CA    1 
ATOM   1228 C C     . LEU   A 1 180 ? -0.06   29.039 41.746 1   16    ? 161 LEU   A C     1 
ATOM   1229 O O     . LEU   A 1 180 ? -1.009  28.278 41.963 1   17.13 ? 161 LEU   A O     1 
ATOM   1230 C CB    . LEU   A 1 180 ? 0.435   30.096 43.918 1   17.03 ? 161 LEU   A CB    1 
ATOM   1231 C CG    . LEU   A 1 180 ? 1.7     29.281 44.164 1   17.21 ? 161 LEU   A CG    1 
ATOM   1232 C CD1   . LEU   A 1 180 ? 2.97    30.012 43.639 1   18.38 ? 161 LEU   A CD1   1 
ATOM   1233 C CD2   . LEU   A 1 180 ? 1.835   28.982 45.652 1   19.92 ? 161 LEU   A CD2   1 
ATOM   1234 N N     . SER   A 1 181 ? 0.946   28.725 40.934 1   15.22 ? 162 SER   A N     1 
ATOM   1235 C CA    . SER   A 1 181 ? 0.985   27.375 40.347 1   14.69 ? 162 SER   A CA    1 
ATOM   1236 C C     . SER   A 1 181 ? 2.413   26.938 40.169 1   14.49 ? 162 SER   A C     1 
ATOM   1237 O O     . SER   A 1 181 ? 3.167   27.579 39.403 1   15.87 ? 162 SER   A O     1 
ATOM   1238 C CB    . SER   A 1 181 ? 0.231   27.307 39.027 1   16.85 ? 162 SER   A CB    1 
ATOM   1239 O OG    . SER   A 1 181 ? 0.087   25.954 38.603 1   17.2  ? 162 SER   A OG    1 
ATOM   1240 N N     . THR   A 1 182 ? 2.808   25.844 40.832 1   14.57 ? 163 THR   A N     1 
ATOM   1241 C CA    . THR   A 1 182 ? 4.191   25.338 40.742 1   14.29 ? 163 THR   A CA    1 
ATOM   1242 C C     . THR   A 1 182 ? 4.198   23.977 40.063 1   14.06 ? 163 THR   A C     1 
ATOM   1243 O O     . THR   A 1 182 ? 3.478   23.049 40.457 1   14.77 ? 163 THR   A O     1 
ATOM   1244 C CB    . THR   A 1 182 ? 4.861   25.255 42.14  1   17.04 ? 163 THR   A CB    1 
ATOM   1245 O OG1   . THR   A 1 182 ? 4.128   24.436 43.045 1   16.87 ? 163 THR   A OG1   1 
ATOM   1246 C CG2   . THR   A 1 182 ? 4.945   26.635 42.804 1   16.22 ? 163 THR   A CG2   1 
ATOM   1247 N N     . LEU   A 1 183 ? 4.956   23.886 38.98  1   13.79 ? 164 LEU   A N     1 
ATOM   1248 C CA    . LEU   A 1 183 ? 5.205   22.606 38.294 1   13.92 ? 164 LEU   A CA    1 
ATOM   1249 C C     . LEU   A 1 183 ? 3.945   21.927 37.819 1   13.55 ? 164 LEU   A C     1 
ATOM   1250 O O     . LEU   A 1 183 ? 3.913   20.706 37.708 1   14.91 ? 164 LEU   A O     1 
ATOM   1251 C CB    . LEU   A 1 183 ? 6.055   21.682 39.184 1   13.44 ? 164 LEU   A CB    1 
ATOM   1252 C CG    . LEU   A 1 183 ? 7.519   22.178 39.352 1   14.92 ? 164 LEU   A CG    1 
ATOM   1253 C CD1   . LEU   A 1 183 ? 8.134   21.539 40.592 1   17.16 ? 164 LEU   A CD1   1 
ATOM   1254 C CD2   . LEU   A 1 183 ? 8.34    21.845 38.078 1   16.13 ? 164 LEU   A CD2   1 
ATOM   1255 N N     . CYS   A 1 184 ? 2.931   22.697 37.463 1   12.54 ? 165 CYS   A N     1 
ATOM   1256 C CA    . CYS   A 1 184 ? 1.65    22.179 36.996 1   13.45 ? 165 CYS   A CA    1 
ATOM   1257 C C     . CYS   A 1 184 ? 1.407   22.418 35.52  1   14.39 ? 165 CYS   A C     1 
ATOM   1258 O O     . CYS   A 1 184 ? 1.001   21.485 34.803 1   14.55 ? 165 CYS   A O     1 
ATOM   1259 C CB    . CYS   A 1 184 ? 0.528   22.765 37.827 1   14.65 ? 165 CYS   A CB    1 
ATOM   1260 S SG    . CYS   A 1 184 ? -1.139  22.403 37.205 1   17.19 ? 165 CYS   A SG    1 
ATOM   1261 N N     . LEU   A 1 185 ? 1.548   23.655 35.039 1   13.62 ? 166 LEU   A N     1 
ATOM   1262 C CA    . LEU   A 1 185 ? 1.056   23.958 33.715 1   15.38 ? 166 LEU   A CA    1 
ATOM   1263 C C     . LEU   A 1 185 ? 1.761   23.239 32.614 1   15.23 ? 166 LEU   A C     1 
ATOM   1264 O O     . LEU   A 1 185 ? 1.071   22.831 31.661 1   16.35 ? 166 LEU   A O     1 
ATOM   1265 C CB    . LEU   A 1 185 ? 1.036   25.474 33.493 1   16.57 ? 166 LEU   A CB    1 
ATOM   1266 C CG    . LEU   A 1 185 ? 0.205   26.271 34.469 1   18.23 ? 166 LEU   A CG    1 
ATOM   1267 C CD1   . LEU   A 1 185 ? 0.299   27.779 34.076 1   18.47 ? 166 LEU   A CD1   1 
ATOM   1268 C CD2   . LEU   A 1 185 ? -1.282  25.844 34.436 1   19.88 ? 166 LEU   A CD2   1 
ATOM   1269 N N     . ASP   A 1 186 ? 3.064   22.951 32.724 1   16.11 ? 167 ASP   A N     1 
ATOM   1270 C CA    . ASP   A 1 186 ? 3.709   22.203 31.629 1   15.61 ? 167 ASP   A CA    1 
ATOM   1271 C C     . ASP   A 1 186 ? 3.157   20.744 31.578 1   15.94 ? 167 ASP   A C     1 
ATOM   1272 O O     . ASP   A 1 186 ? 3.075   20.153 30.494 1   18.12 ? 167 ASP   A O     1 
ATOM   1273 C CB    . ASP   A 1 186 ? 5.193   22.017 31.934 1   19.77 ? 167 ASP   A CB    1 
ATOM   1274 C CG    . ASP   A 1 186 ? 6.132   23.171 31.853 1   24.76 ? 167 ASP   A CG    1 
ATOM   1275 O OD1   . ASP   A 1 186 ? 5.757   24.175 31.252 1   26.07 ? 167 ASP   A OD1   1 
ATOM   1276 O OD2   . ASP   A 1 186 ? 7.301   23     32.318 1   24.06 ? 167 ASP   A OD2   1 
ATOM   1277 N N     . ALA   A 1 187 ? 2.805   20.189 32.734 1   15.1  ? 168 ALA   A N     1 
ATOM   1278 C CA    . ALA   A 1 187 ? 2.267   18.82  32.754 1   15.5  ? 168 ALA   A CA    1 
ATOM   1279 C C     . ALA   A 1 187 ? 0.812   18.811 32.247 1   16.26 ? 168 ALA   A C     1 
ATOM   1280 O O     . ALA   A 1 187 ? 0.335   17.806 31.718 1   16.52 ? 168 ALA   A O     1 
ATOM   1281 C CB    . ALA   A 1 187 ? 2.311   18.339 34.192 1   15.34 ? 168 ALA   A CB    1 
ATOM   1282 N N     . ALA   A 1 188 ? 0.051   19.886 32.508 1   15.33 ? 169 ALA   A N     1 
ATOM   1283 C CA    . ALA   A 1 188 ? -1.379  19.905 32.219 1   17.53 ? 169 ALA   A CA    1 
ATOM   1284 C C     . ALA   A 1 188 ? -1.725  20.291 30.819 1   17.49 ? 169 ALA   A C     1 
ATOM   1285 O O     . ALA   A 1 188 ? -2.895  20.068 30.419 1   19.96 ? 169 ALA   A O     1 
ATOM   1286 C CB    . ALA   A 1 188 ? -2.06   20.869 33.19  1   17.93 ? 169 ALA   A CB    1 
ATOM   1287 N N     . CYS   A 1 189 ? -0.859  20.969 30.072 1   16.47 ? 170 CYS   A N     1 
ATOM   1288 C CA    . CYS   A 1 189 ? -1.22   21.553 28.793 1   17.34 ? 170 CYS   A CA    1 
ATOM   1289 C C     . CYS   A 1 189 ? -0.552  20.87  27.65  1   18.14 ? 170 CYS   A C     1 
ATOM   1290 O O     . CYS   A 1 189 ? 0.662   20.91  27.573 1   18.67 ? 170 CYS   A O     1 
ATOM   1291 C CB    . CYS   A 1 189 ? -0.853  23.042 28.812 1   17.94 ? 170 CYS   A CB    1 
ATOM   1292 S SG    . CYS   A 1 189 ? -1.684  23.98  30.14  1   18.54 ? 170 CYS   A SG    1 
ATOM   1293 N N     . PRO   A 1 190 ? -1.3    20.214 26.738 1   20.16 ? 171 PRO   A N     1 
ATOM   1294 C CA    . PRO   A 1 190 ? -0.642  19.432 25.671 1   21.45 ? 171 PRO   A CA    1 
ATOM   1295 C C     . PRO   A 1 190 ? 0.004   20.245 24.564 1   23.35 ? 171 PRO   A C     1 
ATOM   1296 O O     . PRO   A 1 190 ? 0.845   19.717 23.829 1   25.02 ? 171 PRO   A O     1 
ATOM   1297 C CB    . PRO   A 1 190 ? -1.77   18.536 25.126 1   23    ? 171 PRO   A CB    1 
ATOM   1298 C CG    . PRO   A 1 190 ? -2.794  18.502 26.2   1   24.47 ? 171 PRO   A CG    1 
ATOM   1299 C CD    . PRO   A 1 190 ? -2.742  19.927 26.798 1   21.83 ? 171 PRO   A CD    1 
ATOM   1300 N N     . ASP   A 1 191 ? -0.347  21.521 24.448 1   21.82 ? 172 ASP   A N     1 
ATOM   1301 C CA    . ASP   A 1 191 ? 0.216   22.358 23.411 1   22.31 ? 172 ASP   A CA    1 
ATOM   1302 C C     . ASP   A 1 191 ? 0.176   23.821 23.831 1   21.83 ? 172 ASP   A C     1 
ATOM   1303 O O     . ASP   A 1 191 ? -0.421  24.142 24.859 1   21.13 ? 172 ASP   A O     1 
ATOM   1304 C CB    . ASP   A 1 191 ? -0.516  22.127 22.075 1   25.98 ? 172 ASP   A CB    1 
ATOM   1305 C CG    . ASP   A 1 191 ? -2.021  22.235 22.193 1   31.2  ? 172 ASP   A CG    1 
ATOM   1306 O OD1   . ASP   A 1 191 ? -2.496  23.12  22.91  1   28.53 ? 172 ASP   A OD1   1 
ATOM   1307 O OD2   . ASP   A 1 191 ? -2.732  21.405 21.578 1   35.88 ? 172 ASP   A OD2   1 
ATOM   1308 N N     . LEU   A 1 192 ? 0.872   24.672 23.08  1   22.44 ? 173 LEU   A N     1 
ATOM   1309 C CA    . LEU   A 1 192 ? 0.975   26.082 23.406 1   23.14 ? 173 LEU   A CA    1 
ATOM   1310 C C     . LEU   A 1 192 ? -0.382  26.826 23.412 1   23.84 ? 173 LEU   A C     1 
ATOM   1311 O O     . LEU   A 1 192 ? -0.632  27.581 24.365 1   22.4  ? 173 LEU   A O     1 
ATOM   1312 C CB    . LEU   A 1 192 ? 2.01    26.776 22.503 1   24.72 ? 173 LEU   A CB    1 
ATOM   1313 C CG    . LEU   A 1 192 ? 2.331   28.204 22.859 1   25.94 ? 173 LEU   A CG    1 
ATOM   1314 C CD1   . LEU   A 1 192 ? 2.82    28.343 24.301 1   25.37 ? 173 LEU   A CD1   1 
ATOM   1315 C CD2   . LEU   A 1 192 ? 3.398   28.776 21.903 1   28.97 ? 173 LEU   A CD2   1 
ATOM   1316 N N     . PRO   A 1 193 ? -1.314  26.564 22.475 1   25.07 ? 174 PRO   A N     1 
ATOM   1317 C CA    . PRO   A 1 193 ? -2.619  27.217 22.586 1   24.64 ? 174 PRO   A CA    1 
ATOM   1318 C C     . PRO   A 1 193 ? -3.347  26.824 23.879 1   22.92 ? 174 PRO   A C     1 
ATOM   1319 O O     . PRO   A 1 193 ? -3.92   27.714 24.499 1   23.15 ? 174 PRO   A O     1 
ATOM   1320 C CB    . PRO   A 1 193 ? -3.351  26.785 21.308 1   26.81 ? 174 PRO   A CB    1 
ATOM   1321 C CG    . PRO   A 1 193 ? -2.251  26.483 20.333 1   27.92 ? 174 PRO   A CG    1 
ATOM   1322 C CD    . PRO   A 1 193 ? -1.234  25.779 21.225 1   25.31 ? 174 PRO   A CD    1 
ATOM   1323 N N     . THR   A 1 194 ? -3.242  25.562 24.332 1   21.4  ? 175 THR   A N     1 
ATOM   1324 C CA    . THR   A 1 194 ? -3.879  25.171 25.596 1   20.34 ? 175 THR   A CA    1 
ATOM   1325 C C     . THR   A 1 194 ? -3.186  25.893 26.768 1   19.67 ? 175 THR   A C     1 
ATOM   1326 O O     . THR   A 1 194 ? -3.844  26.293 27.726 1   20.05 ? 175 THR   A O     1 
ATOM   1327 C CB    . THR   A 1 194 ? -3.834  23.662 25.799 1   22.51 ? 175 THR   A CB    1 
ATOM   1328 O OG1   . THR   A 1 194 ? -4.549  23.016 24.703 1   24.61 ? 175 THR   A OG1   1 
ATOM   1329 C CG2   . THR   A 1 194 ? -4.485  23.242 27.099 1   23.05 ? 175 THR   A CG2   1 
ATOM   1330 N N     . TYR   A 1 195 ? -1.866  26.039 26.707 1   18.37 ? 176 TYR   A N     1 
ATOM   1331 C CA    . TYR   A 1 195 ? -1.124  26.754 27.759 1   16.67 ? 176 TYR   A CA    1 
ATOM   1332 C C     . TYR   A 1 195 ? -1.613  28.214 27.889 1   17.37 ? 176 TYR   A C     1 
ATOM   1333 O O     . TYR   A 1 195 ? -1.901  28.68  29.008 1   17.86 ? 176 TYR   A O     1 
ATOM   1334 C CB    . TYR   A 1 195 ? 0.369   26.691 27.397 1   16.47 ? 176 TYR   A CB    1 
ATOM   1335 C CG    . TYR   A 1 195 ? 1.264   27.191 28.497 1   16.32 ? 176 TYR   A CG    1 
ATOM   1336 C CD1   . TYR   A 1 195 ? 1.641   26.362 29.539 1   17.64 ? 176 TYR   A CD1   1 
ATOM   1337 C CD2   . TYR   A 1 195 ? 1.721   28.498 28.502 1   17.12 ? 176 TYR   A CD2   1 
ATOM   1338 C CE1   . TYR   A 1 195 ? 2.487   26.813 30.546 1   18.7  ? 176 TYR   A CE1   1 
ATOM   1339 C CE2   . TYR   A 1 195 ? 2.564   28.962 29.502 1   17.07 ? 176 TYR   A CE2   1 
ATOM   1340 C CZ    . TYR   A 1 195 ? 2.924   28.134 30.534 1   18.11 ? 176 TYR   A CZ    1 
ATOM   1341 O OH    . TYR   A 1 195 ? 3.82    28.597 31.487 1   19.22 ? 176 TYR   A OH    1 
ATOM   1342 N N     . CYS   A 1 196 ? -1.749  28.903 26.753 1   18.86 ? 177 CYS   A N     1 
ATOM   1343 C CA    . CYS   A 1 196 ? -2.234  30.273 26.821 1   19.29 ? 177 CYS   A CA    1 
ATOM   1344 C C     . CYS   A 1 196 ? -3.68   30.32  27.348 1   20.01 ? 177 CYS   A C     1 
ATOM   1345 O O     . CYS   A 1 196 ? -4.018  31.154 28.221 1   19.9  ? 177 CYS   A O     1 
ATOM   1346 C CB    . CYS   A 1 196 ? -2.111  30.952 25.468 1   20.26 ? 177 CYS   A CB    1 
ATOM   1347 S SG    . CYS   A 1 196 ? -2.651  32.689 25.503 1   26    ? 177 CYS   A SG    1 
ATOM   1348 N N     . ARG   A 1 197 ? -4.531  29.364 26.897 1   20.45 ? 178 ARG   A N     1 
ATOM   1349 C CA    . ARG   A 1 197 ? -5.879  29.342 27.415 1   20.62 ? 178 ARG   A CA    1 
ATOM   1350 C C     . ARG   A 1 197 ? -5.877  29.05  28.922 1   19.3  ? 178 ARG   A C     1 
ATOM   1351 O O     . ARG   A 1 197 ? -6.662  29.653 29.646 1   19.73 ? 178 ARG   A O     1 
ATOM   1352 C CB    . ARG   A 1 197 ? -6.703  28.279 26.705 1   24.39 ? 178 ARG   A CB    1 
ATOM   1353 C CG    . ARG   A 1 197 ? -6.988  28.562 25.282 1   33.55 ? 178 ARG   A CG    1 
ATOM   1354 C CD    . ARG   A 1 197 ? -8.16   27.694 24.802 1   37.76 ? 178 ARG   A CD    1 
ATOM   1355 N NE    . ARG   A 1 197 ? -7.937  26.26  25.035 1   41.06 ? 178 ARG   A NE    1 
ATOM   1356 C CZ    . ARG   A 1 197 ? -7.274  25.461 24.209 1   43.21 ? 178 ARG   A CZ    1 
ATOM   1357 N NH1   . ARG   A 1 197 ? -7.143  24.171 24.488 1   44.29 ? 178 ARG   A NH1   1 
ATOM   1358 N NH2   . ARG   A 1 197 ? -6.765  25.937 23.079 1   44.02 ? 178 ARG   A NH2   1 
ATOM   1359 N N     . ALA   A 1 198 ? -5.004  28.14  29.414 1   17.14 ? 179 ALA   A N     1 
ATOM   1360 C CA    . ALA   A 1 198 ? -4.967  27.846 30.839 1   17.25 ? 179 ALA   A CA    1 
ATOM   1361 C C     . ALA   A 1 198 ? -4.595  29.099 31.633 1   18.59 ? 179 ALA   A C     1 
ATOM   1362 O O     . ALA   A 1 198 ? -5.166  29.306 32.687 1   18.48 ? 179 ALA   A O     1 
ATOM   1363 C CB    . ALA   A 1 198 ? -3.955  26.73  31.107 1   18.14 ? 179 ALA   A CB    1 
ATOM   1364 N N     . LEU   A 1 199 ? -3.703  29.947 31.088 1   17.29 ? 180 LEU   A N     1 
ATOM   1365 C CA    . LEU   A 1 199 ? -3.362  31.179 31.786 1   17.7  ? 180 LEU   A CA    1 
ATOM   1366 C C     . LEU   A 1 199 ? -4.585  32.12  31.862 1   19.32 ? 180 LEU   A C     1 
ATOM   1367 O O     . LEU   A 1 199 ? -4.833  32.733 32.905 1   19.82 ? 180 LEU   A O     1 
ATOM   1368 C CB    . LEU   A 1 199 ? -2.201  31.857 31.067 1   18.08 ? 180 LEU   A CB    1 
ATOM   1369 C CG    . LEU   A 1 199 ? -0.879  31.136 31.228 1   18.53 ? 180 LEU   A CG    1 
ATOM   1370 C CD1   . LEU   A 1 199 ? 0.165   31.737 30.34  1   20.23 ? 180 LEU   A CD1   1 
ATOM   1371 C CD2   . LEU   A 1 199 ? -0.381  31.21  32.661 1   19.89 ? 180 LEU   A CD2   1 
ATOM   1372 N N     . ARG   A 1 200 ? -5.384  32.159 30.79  1   19.07 ? 181 ARG   A N     1 
ATOM   1373 C CA    . ARG   A 1 200 ? -6.638  32.943 30.832 1   20.59 ? 181 ARG   A CA    1 
ATOM   1374 C C     . ARG   A 1 200 ? -7.595  32.328 31.848 1   21.94 ? 181 ARG   A C     1 
ATOM   1375 O O     . ARG   A 1 200 ? -8.268  33.061 32.586 1   22.89 ? 181 ARG   A O     1 
ATOM   1376 C CB    . ARG   A 1 200 ? -7.318  32.992 29.482 1   21.99 ? 181 ARG   A CB    1 
ATOM   1377 C CG    . ARG   A 1 200 ? -6.52   33.631 28.369 1   24.57 ? 181 ARG   A CG    1 
ATOM   1378 C CD    . ARG   A 1 200 ? -7.403  33.857 27.179 1   27.5  ? 181 ARG   A CD    1 
ATOM   1379 N NE    . ARG   A 1 200 ? -6.642  34.003 25.946 1   29.4  ? 181 ARG   A NE    1 
ATOM   1380 C CZ    . ARG   A 1 200 ? -6.365  35.155 25.342 1   28.26 ? 181 ARG   A CZ    1 
ATOM   1381 N NH1   . ARG   A 1 200 ? -6.728  36.318 25.893 1   24.42 ? 181 ARG   A NH1   1 
ATOM   1382 N NH2   . ARG   A 1 200 ? -5.756  35.161 24.167 1   29.94 ? 181 ARG   A NH2   1 
ATOM   1383 N N     . ASN   A 1 201 ? -7.673  30.972 31.892 1   20.17 ? 182 ASN   A N     1 
ATOM   1384 C CA    . ASN   A 1 201 ? -8.597  30.32  32.804 1   20.54 ? 182 ASN   A CA    1 
ATOM   1385 C C     . ASN   A 1 201 ? -8.196  30.562 34.245 1   21.46 ? 182 ASN   A C     1 
ATOM   1386 O O     . ASN   A 1 201 ? -9.073  30.792 35.072 1   23.04 ? 182 ASN   A O     1 
ATOM   1387 C CB    . ASN   A 1 201 ? -8.656  28.831 32.503 1   21.13 ? 182 ASN   A CB    1 
ATOM   1388 C CG    . ASN   A 1 201 ? -9.131  28.499 31.12  1   22.8  ? 182 ASN   A CG    1 
ATOM   1389 O OD1   . ASN   A 1 201 ? -9.853  29.287 30.49  1   23.88 ? 182 ASN   A OD1   1 
ATOM   1390 N ND2   . ASN   A 1 201 ? -8.783  27.31  30.622 1   22.63 ? 182 ASN   A ND2   1 
ATOM   1391 N N     . LEU   A 1 202 ? -6.894  30.552 34.573 1   19.61 ? 183 LEU   A N     1 
ATOM   1392 C CA    . LEU   A 1 202 ? -6.456  30.893 35.919 1   20.56 ? 183 LEU   A CA    1 
ATOM   1393 C C     . LEU   A 1 202 ? -6.82   32.366 36.213 1   21    ? 183 LEU   A C     1 
ATOM   1394 O O     . LEU   A 1 202 ? -7.171  32.689 37.326 1   21.23 ? 183 LEU   A O     1 
ATOM   1395 C CB    . LEU   A 1 202 ? -4.931  30.715 36.067 1   20.6  ? 183 LEU   A CB    1 
ATOM   1396 C CG    . LEU   A 1 202 ? -4.44   29.316 36.544 1   22.43 ? 183 LEU   A CG    1 
ATOM   1397 C CD1   . LEU   A 1 202 ? -5.092  28.186 35.804 1   25.79 ? 183 LEU   A CD1   1 
ATOM   1398 C CD2   . LEU   A 1 202 ? -2.947  29.245 36.51  1   21.93 ? 183 LEU   A CD2   1 
ATOM   1399 N N     . GLY   A 1 203 ? -6.728  33.23  35.212 1   20.38 ? 184 GLY   A N     1 
ATOM   1400 C CA    . GLY   A 1 203 ? -7.048  34.642 35.377 1   20.59 ? 184 GLY   A CA    1 
ATOM   1401 C C     . GLY   A 1 203 ? -8.498  34.845 35.76  1   22.24 ? 184 GLY   A C     1 
ATOM   1402 O O     . GLY   A 1 203 ? -8.805  35.792 36.489 1   23.29 ? 184 GLY   A O     1 
ATOM   1403 N N     . SER   A 1 204 ? -9.404  33.935 35.334 1   23.29 ? 185 SER   A N     1 
ATOM   1404 C CA    . SER   A 1 204 ? -10.837 34.082 35.699 1   23.44 ? 185 SER   A CA    1 
ATOM   1405 C C     . SER   A 1 204 ? -11.022 33.911 37.227 1   24.71 ? 185 SER   A C     1 
ATOM   1406 O O     . SER   A 1 204 ? -12.087 34.227 37.744 1   26.99 ? 185 SER   A O     1 
ATOM   1407 C CB    . SER   A 1 204 ? -11.673 33.039 34.967 1   22.52 ? 185 SER   A CB    1 
ATOM   1408 O OG    . SER   A 1 204 ? -11.545 31.75  35.557 1   24.82 ? 185 SER   A OG    1 
ATOM   1409 N N     . LEU   A 1 205 ? -10.052 33.373 37.943 1   22.66 ? 186 LEU   A N     1 
ATOM   1410 C CA    . LEU   A 1 205 ? -10.127 33.164 39.397 1   22.1  ? 186 LEU   A CA    1 
ATOM   1411 C C     . LEU   A 1 205 ? -9.538  34.333 40.173 1   23.95 ? 186 LEU   A C     1 
ATOM   1412 O O     . LEU   A 1 205 ? -9.562  34.294 41.401 1   25.4  ? 186 LEU   A O     1 
ATOM   1413 C CB    . LEU   A 1 205 ? -9.295  31.924 39.799 1   22.12 ? 186 LEU   A CB    1 
ATOM   1414 C CG    . LEU   A 1 205 ? -9.743  30.66  39.113 1   24.78 ? 186 LEU   A CG    1 
ATOM   1415 C CD1   . LEU   A 1 205 ? -8.825  29.488 39.485 1   25.55 ? 186 LEU   A CD1   1 
ATOM   1416 C CD2   . LEU   A 1 205 ? -11.165 30.295 39.478 1   25.8  ? 186 LEU   A CD2   1 
ATOM   1417 N N     . LEU   A 1 206 ? -8.931  35.292 39.478 1   23.04 ? 187 LEU   A N     1 
ATOM   1418 C CA    . LEU   A 1 206 ? -8.115  36.342 40.043 1   23.49 ? 187 LEU   A CA    1 
ATOM   1419 C C     . LEU   A 1 206 ? -8.852  37.685 39.916 1   25.42 ? 187 LEU   A C     1 
ATOM   1420 O O     . LEU   A 1 206 ? -9.413  38.017 38.863 1   26.97 ? 187 LEU   A O     1 
ATOM   1421 C CB    . LEU   A 1 206 ? -6.84   36.424 39.185 1   24.73 ? 187 LEU   A CB    1 
ATOM   1422 C CG    . LEU   A 1 206 ? -5.475  36.288 39.767 1   28.92 ? 187 LEU   A CG    1 
ATOM   1423 C CD1   . LEU   A 1 206 ? -4.41   36.662 38.724 1   25.41 ? 187 LEU   A CD1   1 
ATOM   1424 C CD2   . LEU   A 1 206 ? -5.28   36.874 41.135 1   26.63 ? 187 LEU   A CD2   1 
ATOM   1425 N N     . LYS   A 1 207 ? -8.731  38.475 40.945 1   24.81 ? 188 LYS   A N     1 
ATOM   1426 C CA    . LYS   A 1 207 ? -9.329  39.809 40.934 1   26.48 ? 188 LYS   A CA    1 
ATOM   1427 C C     . LYS   A 1 207 ? -8.555  40.681 39.915 1   26.79 ? 188 LYS   A C     1 
ATOM   1428 O O     . LYS   A 1 207 ? -7.373  40.459 39.686 1   25.65 ? 188 LYS   A O     1 
ATOM   1429 C CB    . LYS   A 1 207 ? -9.227  40.416 42.344 1   27.98 ? 188 LYS   A CB    1 
ATOM   1430 C CG    . LYS   A 1 207 ? -7.842  40.779 42.754 1   29    ? 188 LYS   A CG    1 
ATOM   1431 C CD    . LYS   A 1 207 ? -7.794  41.376 44.139 1   30.72 ? 188 LYS   A CD    1 
ATOM   1432 C CE    . LYS   A 1 207 ? -6.428  41.992 44.364 1   34.69 ? 188 LYS   A CE    1 
ATOM   1433 N NZ    . LYS   A 1 207 ? -6.276  42.492 45.765 1   38.99 ? 188 LYS   A NZ    1 
ATOM   1434 N N     . PRO   A 1 208 ? -9.175  41.778 39.37  1   29.26 ? 189 PRO   A N     1 
ATOM   1435 C CA    . PRO   A 1 208 ? -8.403  42.687 38.492 1   29.09 ? 189 PRO   A CA    1 
ATOM   1436 C C     . PRO   A 1 208 ? -7.169  43.203 39.266 1   27.49 ? 189 PRO   A C     1 
ATOM   1437 O O     . PRO   A 1 208 ? -7.276  43.54  40.47  1   27.03 ? 189 PRO   A O     1 
ATOM   1438 C CB    . PRO   A 1 208 ? -9.403  43.839 38.187 1   30.57 ? 189 PRO   A CB    1 
ATOM   1439 C CG    . PRO   A 1 208 ? -10.711 43.4   38.624 1   32.74 ? 189 PRO   A CG    1 
ATOM   1440 C CD    . PRO   A 1 208 ? -10.572 42.217 39.561 1   31.1  ? 189 PRO   A CD    1 
ATOM   1441 N N     . GLY   A 1 209 ? -6.007  43.222 38.632 1   27.39 ? 190 GLY   A N     1 
ATOM   1442 C CA    . GLY   A 1 209 ? -4.797  43.642 39.319 1   26.19 ? 190 GLY   A CA    1 
ATOM   1443 C C     . GLY   A 1 209 ? -4.18   42.606 40.265 1   24.55 ? 190 GLY   A C     1 
ATOM   1444 O O     . GLY   A 1 209 ? -3.165  42.892 40.907 1   24.37 ? 190 GLY   A O     1 
ATOM   1445 N N     . GLY   A 1 210 ? -4.792  41.44  40.367 1   22.8  ? 191 GLY   A N     1 
ATOM   1446 C CA    . GLY   A 1 210 ? -4.292  40.39  41.233 1   23.33 ? 191 GLY   A CA    1 
ATOM   1447 C C     . GLY   A 1 210 ? -2.984  39.796 40.722 1   21.67 ? 191 GLY   A C     1 
ATOM   1448 O O     . GLY   A 1 210 ? -2.622  39.939 39.544 1   21.61 ? 191 GLY   A O     1 
ATOM   1449 N N     . PHE   A 1 211 ? -2.307  39.082 41.597 1   19.74 ? 192 PHE   A N     1 
ATOM   1450 C CA    . PHE   A 1 211 ? -0.989  38.504 41.233 1   19.66 ? 192 PHE   A CA    1 
ATOM   1451 C C     . PHE   A 1 211 ? -1.063  37.086 40.749 1   18.78 ? 192 PHE   A C     1 
ATOM   1452 O O     . PHE   A 1 211 ? -1.804  36.262 41.295 1   20.43 ? 192 PHE   A O     1 
ATOM   1453 C CB    . PHE   A 1 211 ? -0.037  38.532 42.44  1   20.75 ? 192 PHE   A CB    1 
ATOM   1454 C CG    . PHE   A 1 211 ? 0.43    39.932 42.774 1   23.77 ? 192 PHE   A CG    1 
ATOM   1455 C CD1   . PHE   A 1 211 ? 1.524   40.473 42.14  1   25.29 ? 192 PHE   A CD1   1 
ATOM   1456 C CD2   . PHE   A 1 211 ? -0.202  40.67  43.752 1   26.9  ? 192 PHE   A CD2   1 
ATOM   1457 C CE1   . PHE   A 1 211 ? 1.967   41.766 42.46  1   27.6  ? 192 PHE   A CE1   1 
ATOM   1458 C CE2   . PHE   A 1 211 ? 0.265   41.946 44.101 1   27.97 ? 192 PHE   A CE2   1 
ATOM   1459 C CZ    . PHE   A 1 211 ? 1.337   42.471 43.449 1   27.89 ? 192 PHE   A CZ    1 
ATOM   1460 N N     . LEU   A 1 212 ? -0.273  36.819 39.716 1   17.18 ? 193 LEU   A N     1 
ATOM   1461 C CA    . LEU   A 1 212 ? -0.098  35.456 39.17  1   16.61 ? 193 LEU   A CA    1 
ATOM   1462 C C     . LEU   A 1 212 ? 1.356   35.067 39.427 1   15.88 ? 193 LEU   A C     1 
ATOM   1463 O O     . LEU   A 1 212 ? 2.268   35.798 39.035 1   15.88 ? 193 LEU   A O     1 
ATOM   1464 C CB    . LEU   A 1 212 ? -0.327  35.457 37.665 1   17.07 ? 193 LEU   A CB    1 
ATOM   1465 C CG    . LEU   A 1 212 ? -0.238  34.098 37.011 1   19.56 ? 193 LEU   A CG    1 
ATOM   1466 C CD1   . LEU   A 1 212 ? -1.481  33.278 37.369 1   21.83 ? 193 LEU   A CD1   1 
ATOM   1467 C CD2   . LEU   A 1 212 ? -0.047  34.258 35.487 1   20.42 ? 193 LEU   A CD2   1 
ATOM   1468 N N     . VAL   A 1 213 ? 1.558   33.941 40.117 1   15.24 ? 194 VAL   A N     1 
ATOM   1469 C CA    . VAL   A 1 213 ? 2.911   33.464 40.427 1   15.21 ? 194 VAL   A CA    1 
ATOM   1470 C C     . VAL   A 1 213 ? 3.055   32.075 39.819 1   15.16 ? 194 VAL   A C     1 
ATOM   1471 O O     . VAL   A 1 213 ? 2.29    31.181 40.198 1   15.26 ? 194 VAL   A O     1 
ATOM   1472 C CB    . VAL   A 1 213 ? 3.138   33.407 41.925 1   15.88 ? 194 VAL   A CB    1 
ATOM   1473 C CG1   . VAL   A 1 213 ? 4.554   32.909 42.221 1   17.47 ? 194 VAL   A CG1   1 
ATOM   1474 C CG2   . VAL   A 1 213 ? 2.935   34.791 42.578 1   18.5  ? 194 VAL   A CG2   1 
ATOM   1475 N N     . ILE   A 1 214 ? 3.979   31.9   38.863 1   14.52 ? 195 ILE   A N     1 
ATOM   1476 C CA    . ILE   A 1 214 ? 4.163   30.615 38.192 1   13.91 ? 195 ILE   A CA    1 
ATOM   1477 C C     . ILE   A 1 214 ? 5.61    30.219 38.306 1   14.38 ? 195 ILE   A C     1 
ATOM   1478 O O     . ILE   A 1 214 ? 6.508   31.02  38.086 1   14.14 ? 195 ILE   A O     1 
ATOM   1479 C CB    . ILE   A 1 214 ? 3.808   30.704 36.71  1   15.36 ? 195 ILE   A CB    1 
ATOM   1480 C CG1   . ILE   A 1 214 ? 2.36    31.251 36.448 1   18.61 ? 195 ILE   A CG1   1 
ATOM   1481 C CG2   . ILE   A 1 214 ? 3.964   29.3   36.024 1   16.9  ? 195 ILE   A CG2   1 
ATOM   1482 C CD1   . ILE   A 1 214 ? 1.144   30.461 36.968 1   20.98 ? 195 ILE   A CD1   1 
ATOM   1483 N N     . MET   A 1 215 ? 5.85    28.94  38.624 1   13.22 ? 196 MET   A N     1 
ATOM   1484 C CA    . MET   A 1 215 ? 7.206   28.385 38.614 1   13.28 ? 196 MET   A CA    1 
ATOM   1485 C C     . MET   A 1 215 ? 7.104   27.05  37.899 1   14.12 ? 196 MET   A C     1 
ATOM   1486 O O     . MET   A 1 215 ? 6.19    26.3   38.191 1   14.98 ? 196 MET   A O     1 
ATOM   1487 C CB    . MET   A 1 215 ? 7.773   28.19  40.019 1   16.26 ? 196 MET   A CB    1 
ATOM   1488 C CG    . MET   A 1 215 ? 7.793   29.494 40.803 1   18.23 ? 196 MET   A CG    1 
ATOM   1489 S SD    . MET   A 1 215 ? 8.363   29.307 42.533 1   22.77 ? 196 MET   A SD    1 
ATOM   1490 C CE    . MET   A 1 215 ? 8.147   31.03  43.121 1   24.26 ? 196 MET   A CE    1 
ATOM   1491 N N     . ASP   A 1 216 ? 7.971   26.769 36.951 1   12.97 ? 197 ASP   A N     1 
ATOM   1492 C CA    . ASP   A 1 216 ? 7.861   25.499 36.181 1   13.23 ? 197 ASP   A CA    1 
ATOM   1493 C C     . ASP   A 1 216 ? 9.12    25.217 35.424 1   13.28 ? 197 ASP   A C     1 
ATOM   1494 O O     . ASP   A 1 216 ? 10.065  25.981 35.423 1   13.84 ? 197 ASP   A O     1 
ATOM   1495 C CB    . ASP   A 1 216 ? 6.684   25.575 35.213 1   14.51 ? 197 ASP   A CB    1 
ATOM   1496 C CG    . ASP   A 1 216 ? 5.877   24.33  35.035 1   16.78 ? 197 ASP   A CG    1 
ATOM   1497 O OD1   . ASP   A 1 216 ? 6.416   23.234 35.245 1   15.97 ? 197 ASP   A OD1   1 
ATOM   1498 O OD2   . ASP   A 1 216 ? 4.711   24.469 34.6   1   19.19 ? 197 ASP   A OD2   1 
ATOM   1499 N N     . ALA   A 1 217 ? 9.173   23.999 34.889 1   14.28 ? 198 ALA   A N     1 
ATOM   1500 C CA    . ALA   A 1 217 ? 10.318  23.559 34.142 1   13.54 ? 198 ALA   A CA    1 
ATOM   1501 C C     . ALA   A 1 217 ? 10.399  24.181 32.758 1   15.19 ? 198 ALA   A C     1 
ATOM   1502 O O     . ALA   A 1 217 ? 9.364   24.474 32.127 1   17.82 ? 198 ALA   A O     1 
ATOM   1503 C CB    . ALA   A 1 217 ? 10.255  22.028 33.974 1   15.14 ? 198 ALA   A CB    1 
ATOM   1504 N N     . LEU   A 1 218 ? 11.623  24.386 32.275 1   15.02 ? 199 LEU   A N     1 
ATOM   1505 C CA    . LEU   A 1 218 ? 11.818  24.857 30.902 1   16    ? 199 LEU   A CA    1 
ATOM   1506 C C     . LEU   A 1 218 ? 12.295  23.694 30.035 1   16.25 ? 199 LEU   A C     1 
ATOM   1507 O O     . LEU   A 1 218 ? 13.088  22.856 30.493 1   15.84 ? 199 LEU   A O     1 
ATOM   1508 C CB    . LEU   A 1 218 ? 12.935  25.93  30.878 1   15.81 ? 199 LEU   A CB    1 
ATOM   1509 C CG    . LEU   A 1 218 ? 12.502  27.275 31.503 1   16.41 ? 199 LEU   A CG    1 
ATOM   1510 C CD1   . LEU   A 1 218 ? 13.796  28.083 31.787 1   16.4  ? 199 LEU   A CD1   1 
ATOM   1511 C CD2   . LEU   A 1 218 ? 11.559  28.016 30.591 1   17.56 ? 199 LEU   A CD2   1 
ATOM   1512 N N     . LYS   A 1 219 ? 11.751  23.621 28.806 1   16.32 ? 200 LYS   A N     1 
ATOM   1513 C CA    . LYS   A 1 219 ? 12.175  22.702 27.752 1   17.52 ? 200 LYS   A CA    1 
ATOM   1514 C C     . LYS   A 1 219 ? 12.118  21.251 28.161 1   19.21 ? 200 LYS   A C     1 
ATOM   1515 O O     . LYS   A 1 219 ? 12.921  20.457 27.671 1   22.25 ? 200 LYS   A O     1 
ATOM   1516 C CB    . LYS   A 1 219 ? 13.576  23.082 27.256 1   20.09 ? 200 LYS   A CB    1 
ATOM   1517 C CG    . LYS   A 1 219 ? 13.594  24.484 26.646 1   21.47 ? 200 LYS   A CG    1 
ATOM   1518 C CD    . LYS   A 1 219 ? 14.934  24.835 26.056 1   30.64 ? 200 LYS   A CD    1 
ATOM   1519 C CE    . LYS   A 1 219 ? 14.854  26.219 25.444 1   37.05 ? 200 LYS   A CE    1 
ATOM   1520 N NZ    . LYS   A 1 219 ? 16.113  26.579 24.71  1   41.02 ? 200 LYS   A NZ    1 
ATOM   1521 N N     . SER   A 1 220 ? 11.184  20.888 29.019 1   17.75 ? 201 SER   A N     1 
ATOM   1522 C CA    . SER   A 1 220 ? 11.016  19.486 29.438 1   17.3  ? 201 SER   A CA    1 
ATOM   1523 C C     . SER   A 1 220 ? 9.901   18.874 28.614 1   17.93 ? 201 SER   A C     1 
ATOM   1524 O O     . SER   A 1 220 ? 8.805   19.427 28.52  1   17.17 ? 201 SER   A O     1 
ATOM   1525 C CB    . SER   A 1 220 ? 10.622  19.463 30.924 1   23.09 ? 201 SER   A CB    1 
ATOM   1526 O OG    . SER   A 1 220 ? 10.389  18.152 31.41  1   30.53 ? 201 SER   A OG    1 
ATOM   1527 N N     . SER   A 1 221 ? 10.158  17.68  28.028 1   17.83 ? 202 SER   A N     1 
ATOM   1528 C CA    . SER   A 1 221 ? 9.116   16.971 27.307 1   18.67 ? 202 SER   A CA    1 
ATOM   1529 C C     . SER   A 1 221 ? 8.583   15.76  28.082 1   17.25 ? 202 SER   A C     1 
ATOM   1530 O O     . SER   A 1 221 ? 7.566   15.197 27.659 1   17.97 ? 202 SER   A O     1 
ATOM   1531 C CB    . SER   A 1 221 ? 9.549   16.563 25.896 1   21.44 ? 202 SER   A CB    1 
ATOM   1532 O OG    . SER   A 1 221 ? 10.6    15.611 25.998 1   24.29 ? 202 SER   A OG    1 
ATOM   1533 N N     . TYR   A 1 222 ? 9.165   15.43  29.22  1   16.67 ? 203 TYR   A N     1 
ATOM   1534 C CA    . TYR   A 1 222 ? 8.608   14.425 30.108 1   17.45 ? 203 TYR   A CA    1 
ATOM   1535 C C     . TYR   A 1 222 ? 9.171   14.567 31.506 1   16.9  ? 203 TYR   A C     1 
ATOM   1536 O O     . TYR   A 1 222 ? 10.217  15.234 31.713 1   16.64 ? 203 TYR   A O     1 
ATOM   1537 C CB    . TYR   A 1 222 ? 8.865   12.974 29.574 1   18.39 ? 203 TYR   A CB    1 
ATOM   1538 C CG    . TYR   A 1 222 ? 10.336  12.593 29.647 1   20    ? 203 TYR   A CG    1 
ATOM   1539 C CD1   . TYR   A 1 222 ? 10.873  12.015 30.789 1   20.35 ? 203 TYR   A CD1   1 
ATOM   1540 C CD2   . TYR   A 1 222 ? 11.182  12.812 28.576 1   22.09 ? 203 TYR   A CD2   1 
ATOM   1541 C CE1   . TYR   A 1 222 ? 12.212  11.664 30.862 1   22.76 ? 203 TYR   A CE1   1 
ATOM   1542 C CE2   . TYR   A 1 222 ? 12.523  12.454 28.631 1   24.57 ? 203 TYR   A CE2   1 
ATOM   1543 C CZ    . TYR   A 1 222 ? 13.055  11.96  29.806 1   26.18 ? 203 TYR   A CZ    1 
ATOM   1544 O OH    . TYR   A 1 222 ? 14.402  11.615 29.844 1   30.65 ? 203 TYR   A OH    1 
ATOM   1545 N N     . TYR   A 1 223 ? 8.538   13.93  32.464 1   15.71 ? 204 TYR   A N     1 
ATOM   1546 C CA    . TYR   A 1 223 ? 9.076   13.711 33.781 1   15.84 ? 204 TYR   A CA    1 
ATOM   1547 C C     . TYR   A 1 223 ? 8.628   12.315 34.244 1   15.77 ? 204 TYR   A C     1 
ATOM   1548 O O     . TYR   A 1 223 ? 7.611   11.786 33.768 1   16.27 ? 204 TYR   A O     1 
ATOM   1549 C CB    . TYR   A 1 223 ? 8.759   14.839 34.789 1   16.33 ? 204 TYR   A CB    1 
ATOM   1550 C CG    . TYR   A 1 223 ? 7.297   14.934 35.184 1   14.58 ? 204 TYR   A CG    1 
ATOM   1551 C CD1   . TYR   A 1 223 ? 6.337   15.421 34.288 1   14.48 ? 204 TYR   A CD1   1 
ATOM   1552 C CD2   . TYR   A 1 223 ? 6.885   14.57  36.449 1   15.38 ? 204 TYR   A CD2   1 
ATOM   1553 C CE1   . TYR   A 1 223 ? 5.002   15.522 34.647 1   14.56 ? 204 TYR   A CE1   1 
ATOM   1554 C CE2   . TYR   A 1 223 ? 5.555   14.674 36.829 1   16.08 ? 204 TYR   A CE2   1 
ATOM   1555 C CZ    . TYR   A 1 223 ? 4.619   15.153 35.926 1   15.1  ? 204 TYR   A CZ    1 
ATOM   1556 O OH    . TYR   A 1 223 ? 3.286   15.204 36.31  1   16.53 ? 204 TYR   A OH    1 
ATOM   1557 N N     . MET   A 1 224 ? 9.384   11.76  35.171 1   15.91 ? 205 MET   A N     1 
ATOM   1558 C CA    . MET   A 1 224 ? 9.176   10.376 35.63  1   16.35 ? 205 MET   A CA    1 
ATOM   1559 C C     . MET   A 1 224 ? 8.834   10.312 37.08  1   16.95 ? 205 MET   A C     1 
ATOM   1560 O O     . MET   A 1 224 ? 9.328   11.105 37.902 1   18.04 ? 205 MET   A O     1 
ATOM   1561 C CB    . MET   A 1 224 ? 10.493  9.615  35.476 1   17.45 ? 205 MET   A CB    1 
ATOM   1562 C CG    . MET   A 1 224 ? 11.062  9.561  34.066 1   19.22 ? 205 MET   A CG    1 
ATOM   1563 S SD    . MET   A 1 224 ? 9.977   8.808  32.822 1   20.03 ? 205 MET   A SD    1 
ATOM   1564 C CE    . MET   A 1 224 ? 9.852   7.104  33.49  1   21.53 ? 205 MET   A CE    1 
ATOM   1565 N N     . ILE   A 1 225 ? 7.996   9.305  37.451 1   16.51 ? 206 ILE   A N     1 
ATOM   1566 C CA    . ILE   A 1 225 ? 7.806   9      38.852 1   17.19 ? 206 ILE   A CA    1 
ATOM   1567 C C     . ILE   A 1 225 ? 8.11    7.506  38.893 1   17.98 ? 206 ILE   A C     1 
ATOM   1568 O O     . ILE   A 1 225 ? 7.266   6.678  38.537 1   18.55 ? 206 ILE   A O     1 
ATOM   1569 C CB    . ILE   A 1 225 ? 6.393   9.309  39.374 1   16.85 ? 206 ILE   A CB    1 
ATOM   1570 C CG1   . ILE   A 1 225 ? 6.038   10.772 39.082 1   18.04 ? 206 ILE   A CG1   1 
ATOM   1571 C CG2   . ILE   A 1 225 ? 6.33    9.044  40.883 1   19.53 ? 206 ILE   A CG2   1 
ATOM   1572 C CD1   . ILE   A 1 225 ? 4.578   11.104 39.508 1   19    ? 206 ILE   A CD1   1 
ATOM   1573 N N     . GLY   A 1 226 ? 9.371   7.181  39.15  1   19.22 ? 207 GLY   A N     1 
ATOM   1574 C CA    . GLY   A 1 226 ? 9.801   5.781  39.072 1   20.62 ? 207 GLY   A CA    1 
ATOM   1575 C C     . GLY   A 1 226 ? 9.729   5.362  37.61  1   20.99 ? 207 GLY   A C     1 
ATOM   1576 O O     . GLY   A 1 226 ? 10.271  6.085  36.756 1   21.51 ? 207 GLY   A O     1 
ATOM   1577 N N     . GLU   A 1 227 ? 9.058   4.222  37.293 1   20.9  ? 208 GLU   A N     1 
ATOM   1578 C CA    . GLU   A 1 227 ? 8.984   3.813  35.892 1   19.68 ? 208 GLU   A CA    1 
ATOM   1579 C C     . GLU   A 1 227 ? 7.818   4.465  35.152 1   19.55 ? 208 GLU   A C     1 
ATOM   1580 O O     . GLU   A 1 227 ? 7.704   4.266  33.93  1   19.74 ? 208 GLU   A O     1 
ATOM   1581 C CB    . GLU   A 1 227 ? 8.769   2.292  35.794 1   20.28 ? 208 GLU   A CB    1 
ATOM   1582 C CG    . GLU   A 1 227 ? 9.93    1.472  36.341 1   24.34 ? 208 GLU   A CG    1 
ATOM   1583 C CD    . GLU   A 1 227 ? 9.667   -0.016 36.147 1   30.82 ? 208 GLU   A CD    1 
ATOM   1584 O OE1   . GLU   A 1 227 ? 9.702   -0.478 34.981 1   31.26 ? 208 GLU   A OE1   1 
ATOM   1585 O OE2   . GLU   A 1 227 ? 9.375   -0.709 37.151 1   30.78 ? 208 GLU   A OE2   1 
ATOM   1586 N N     . GLN   A 1 228 ? 6.971   5.261  35.855 1   17.12 ? 209 GLN   A N     1 
ATOM   1587 C CA    . GLN   A 1 228 ? 5.848   5.877  35.19  1   17.01 ? 209 GLN   A CA    1 
ATOM   1588 C C     . GLN   A 1 228 ? 6.263   7.196  34.51  1   16.43 ? 209 GLN   A C     1 
ATOM   1589 O O     . GLN   A 1 228 ? 6.734   8.121  35.172 1   16.54 ? 209 GLN   A O     1 
ATOM   1590 C CB    . GLN   A 1 228 ? 4.727   6.175  36.183 1   16.87 ? 209 GLN   A CB    1 
ATOM   1591 C CG    . GLN   A 1 228 ? 3.49    6.778  35.489 1   17.28 ? 209 GLN   A CG    1 
ATOM   1592 C CD    . GLN   A 1 228 ? 2.776   5.844  34.57  1   19.41 ? 209 GLN   A CD    1 
ATOM   1593 O OE1   . GLN   A 1 228 ? 2.621   6.123  33.363 1   20.97 ? 209 GLN   A OE1   1 
ATOM   1594 N NE2   . GLN   A 1 228 ? 2.315   4.731  35.111 1   16.58 ? 209 GLN   A NE2   1 
ATOM   1595 N N     . LYS   A 1 229 ? 6.063   7.276  33.207 1   16.27 ? 210 LYS   A N     1 
ATOM   1596 C CA    . LYS   A 1 229 ? 6.34    8.481  32.429 1   16.52 ? 210 LYS   A CA    1 
ATOM   1597 C C     . LYS   A 1 229 ? 5.115   9.34   32.361 1   16.74 ? 210 LYS   A C     1 
ATOM   1598 O O     . LYS   A 1 229 ? 3.99    8.852  32.187 1   17.48 ? 210 LYS   A O     1 
ATOM   1599 C CB    . LYS   A 1 229 ? 6.771   8.099  30.993 1   18.13 ? 210 LYS   A CB    1 
ATOM   1600 C CG    . LYS   A 1 229 ? 7.268   9.291  30.136 1   21.52 ? 210 LYS   A CG    1 
ATOM   1601 C CD    . LYS   A 1 229 ? 7.915   8.762  28.885 1   24.22 ? 210 LYS   A CD    1 
ATOM   1602 C CE    . LYS   A 1 229 ? 8.521   9.758  27.936 1   26.63 ? 210 LYS   A CE    1 
ATOM   1603 N NZ    . LYS   A 1 229 ? 9.319   9.071  26.878 1   28.86 ? 210 LYS   A NZ    1 
ATOM   1604 N N     . PHE   A 1 230 ? 5.346   10.668 32.415 1   15.81 ? 211 PHE   A N     1 
ATOM   1605 C CA    . PHE   A 1 230 ? 4.281   11.662 32.189 1   16.6  ? 211 PHE   A CA    1 
ATOM   1606 C C     . PHE   A 1 230 ? 4.813   12.649 31.165 1   16.2  ? 211 PHE   A C     1 
ATOM   1607 O O     . PHE   A 1 230 ? 5.962   13.076 31.243 1   16.57 ? 211 PHE   A O     1 
ATOM   1608 C CB    . PHE   A 1 230 ? 3.957   12.444 33.465 1   16.08 ? 211 PHE   A CB    1 
ATOM   1609 C CG    . PHE   A 1 230 ? 3.217   11.607 34.501 1   16.08 ? 211 PHE   A CG    1 
ATOM   1610 C CD1   . PHE   A 1 230 ? 1.849   11.515 34.484 1   17.83 ? 211 PHE   A CD1   1 
ATOM   1611 C CD2   . PHE   A 1 230 ? 3.915   10.868 35.436 1   18.21 ? 211 PHE   A CD2   1 
ATOM   1612 C CE1   . PHE   A 1 230 ? 1.177   10.657 35.368 1   19.52 ? 211 PHE   A CE1   1 
ATOM   1613 C CE2   . PHE   A 1 230 ? 3.233   10.057 36.336 1   19.21 ? 211 PHE   A CE2   1 
ATOM   1614 C CZ    . PHE   A 1 230 ? 1.877   9.974  36.284 1   19.35 ? 211 PHE   A CZ    1 
ATOM   1615 N N     . SER   A 1 231 ? 3.989   13.078 30.241 1   16.08 ? 212 SER   A N     1 
ATOM   1616 C CA    . SER   A 1 231 ? 4.379   14.098 29.248 1   16.06 ? 212 SER   A CA    1 
ATOM   1617 C C     . SER   A 1 231 ? 4.514   15.478 29.927 1   16.6  ? 212 SER   A C     1 
ATOM   1618 O O     . SER   A 1 231 ? 3.887   15.776 30.953 1   15.6  ? 212 SER   A O     1 
ATOM   1619 C CB    . SER   A 1 231 ? 3.282   14.266 28.199 1   16.33 ? 212 SER   A CB    1 
ATOM   1620 O OG    . SER   A 1 231 ? 3.078   13.028 27.527 1   20.29 ? 212 SER   A OG    1 
ATOM   1621 N N     . SER   A 1 232 ? 5.307   16.32  29.271 1   15.97 ? 213 SER   A N     1 
ATOM   1622 C CA    . SER   A 1 232 ? 5.379   17.747 29.663 1   15.16 ? 213 SER   A CA    1 
ATOM   1623 C C     . SER   A 1 232 ? 5.47    18.527 28.365 1   16.22 ? 213 SER   A C     1 
ATOM   1624 O O     . SER   A 1 232 ? 6.032   18.071 27.363 1   16.96 ? 213 SER   A O     1 
ATOM   1625 C CB    . SER   A 1 232 ? 6.626   17.945 30.53  1   16.71 ? 213 SER   A CB    1 
ATOM   1626 O OG    . SER   A 1 232 ? 6.825   19.332 30.804 1   19.42 ? 213 SER   A OG    1 
ATOM   1627 N N     . LEU   A 1 233 ? 4.963   19.77  28.426 1   15.75 ? 214 LEU   A N     1 
ATOM   1628 C CA    . LEU   A 1 233 ? 5.065   20.661 27.255 1   16.53 ? 214 LEU   A CA    1 
ATOM   1629 C C     . LEU   A 1 233 ? 6.436   21.375 27.298 1   17.08 ? 214 LEU   A C     1 
ATOM   1630 O O     . LEU   A 1 233 ? 6.742   22.063 28.279 1   17.81 ? 214 LEU   A O     1 
ATOM   1631 C CB    . LEU   A 1 233 ? 3.972   21.729 27.364 1   17.36 ? 214 LEU   A CB    1 
ATOM   1632 C CG    . LEU   A 1 233 ? 3.877   22.719 26.232 1   19.97 ? 214 LEU   A CG    1 
ATOM   1633 C CD1   . LEU   A 1 233 ? 3.522   22.049 24.927 1   21.98 ? 214 LEU   A CD1   1 
ATOM   1634 C CD2   . LEU   A 1 233 ? 2.787   23.808 26.551 1   20.2  ? 214 LEU   A CD2   1 
ATOM   1635 N N     . PRO   A 1 234 ? 7.277   21.213 26.268 1   18.71 ? 215 PRO   A N     1 
ATOM   1636 C CA    . PRO   A 1 234 ? 8.649   21.72  26.37  1   19.56 ? 215 PRO   A CA    1 
ATOM   1637 C C     . PRO   A 1 234 ? 8.845   23.194 25.971 1   22.68 ? 215 PRO   A C     1 
ATOM   1638 O O     . PRO   A 1 234 ? 9.634   23.478 25.055 1   28.46 ? 215 PRO   A O     1 
ATOM   1639 C CB    . PRO   A 1 234 ? 9.421   20.788 25.417 1   21.01 ? 215 PRO   A CB    1 
ATOM   1640 C CG    . PRO   A 1 234 ? 8.445   20.446 24.37  1   22.06 ? 215 PRO   A CG    1 
ATOM   1641 C CD    . PRO   A 1 234 ? 7.131   20.303 25.108 1   19.93 ? 215 PRO   A CD    1 
ATOM   1642 N N     . LEU   A 1 235 ? 8.407   24.088 26.798 1   19.99 ? 216 LEU   A N     1 
ATOM   1643 C CA    . LEU   A 1 235 ? 8.506   25.534 26.467 1   19.04 ? 216 LEU   A CA    1 
ATOM   1644 C C     . LEU   A 1 235 ? 9.782   26.181 26.884 1   18.45 ? 216 LEU   A C     1 
ATOM   1645 O O     . LEU   A 1 235 ? 10.318  25.91  27.967 1   19.08 ? 216 LEU   A O     1 
ATOM   1646 C CB    . LEU   A 1 235 ? 7.382   26.295 27.185 1   20.3  ? 216 LEU   A CB    1 
ATOM   1647 C CG    . LEU   A 1 235 ? 5.943   25.903 26.809 1   22.96 ? 216 LEU   A CG    1 
ATOM   1648 C CD1   . LEU   A 1 235 ? 4.925   26.837 27.468 1   25.63 ? 216 LEU   A CD1   1 
ATOM   1649 C CD2   . LEU   A 1 235 ? 5.721   25.877 25.3   1   23.86 ? 216 LEU   A CD2   1 
ATOM   1650 N N     . GLY   A 1 236 ? 10.247  27.122 26.058 1   18.75 ? 217 GLY   A N     1 
ATOM   1651 C CA    . GLY   A 1 236 ? 11.341  27.973 26.437 1   18.71 ? 217 GLY   A CA    1 
ATOM   1652 C C     . GLY   A 1 236 ? 10.83   29.276 27.073 1   18.12 ? 217 GLY   A C     1 
ATOM   1653 O O     . GLY   A 1 236 ? 9.619   29.573 27.06  1   17.61 ? 217 GLY   A O     1 
ATOM   1654 N N     . ARG   A 1 237 ? 11.749  30.065 27.625 1   17.47 ? 218 ARG   A N     1 
ATOM   1655 C CA    . ARG   A 1 237 ? 11.361  31.261 28.349 1   17.38 ? 218 ARG   A CA    1 
ATOM   1656 C C     . ARG   A 1 237 ? 10.62   32.256 27.452 1   17.54 ? 218 ARG   A C     1 
ATOM   1657 O O     . ARG   A 1 237 ? 9.706   32.934 27.928 1   17.67 ? 218 ARG   A O     1 
ATOM   1658 C CB    . ARG   A 1 237 ? 12.554  31.911 29.05  1   19.99 ? 218 ARG   A CB    1 
ATOM   1659 C CG    . ARG   A 1 237 ? 13.583  32.407 28.097 1   24.03 ? 218 ARG   A CG    1 
ATOM   1660 C CD    . ARG   A 1 237 ? 14.591  33.349 28.773 1   30.27 ? 218 ARG   A CD    1 
ATOM   1661 N NE    . ARG   A 1 237 ? 15.373  34.133 27.808 1   36.33 ? 218 ARG   A NE    1 
ATOM   1662 C CZ    . ARG   A 1 237 ? 14.966  35.28  27.264 1   41.21 ? 218 ARG   A CZ    1 
ATOM   1663 N NH1   . ARG   A 1 237 ? 13.774  35.782 27.566 1   42.06 ? 218 ARG   A NH1   1 
ATOM   1664 N NH2   . ARG   A 1 237 ? 15.74   35.923 26.401 1   41.8  ? 218 ARG   A NH2   1 
ATOM   1665 N N     . GLU   A 1 238 ? 10.974  32.353 26.18  1   17.07 ? 219 GLU   A N     1 
ATOM   1666 C CA    . GLU   A 1 238 ? 10.306  33.338 25.31  1   17.93 ? 219 GLU   A CA    1 
ATOM   1667 C C     . GLU   A 1 238 ? 8.831   32.968 25.122 1   18.86 ? 219 GLU   A C     1 
ATOM   1668 O O     . GLU   A 1 238 ? 7.97    33.864 25.156 1   19.38 ? 219 GLU   A O     1 
ATOM   1669 C CB    . GLU   A 1 238 ? 11.03   33.444 23.946 1   21.7  ? 219 GLU   A CB    1 
ATOM   1670 C CG    . GLU   A 1 238 ? 12.488  33.89  24.058 1   26.49 ? 219 GLU   A CG    1 
ATOM   1671 C CD    . GLU   A 1 238 ? 13.542  32.859 24.484 1   35.81 ? 219 GLU   A CD    1 
ATOM   1672 O OE1   . GLU   A 1 238 ? 13.229  31.658 24.713 1   32.47 ? 219 GLU   A OE1   1 
ATOM   1673 O OE2   . GLU   A 1 238 ? 14.721  33.28  24.567 1   45.59 ? 219 GLU   A OE2   1 
ATOM   1674 N N     . ALA   A 1 239 ? 8.533   31.676 24.91  1   16.95 ? 220 ALA   A N     1 
ATOM   1675 C CA    . ALA   A 1 239 ? 7.136   31.264 24.704 1   17.69 ? 220 ALA   A CA    1 
ATOM   1676 C C     . ALA   A 1 239 ? 6.331   31.422 25.987 1   17.27 ? 220 ALA   A C     1 
ATOM   1677 O O     . ALA   A 1 239 ? 5.145   31.795 25.909 1   17.55 ? 220 ALA   A O     1 
ATOM   1678 C CB    . ALA   A 1 239 ? 7.085   29.826 24.248 1   19.07 ? 220 ALA   A CB    1 
ATOM   1679 N N     . VAL   A 1 240 ? 6.929   31.199 27.162 1   15.66 ? 221 VAL   A N     1 
ATOM   1680 C CA    . VAL   A 1 240 ? 6.214   31.423 28.431 1   14.9  ? 221 VAL   A CA    1 
ATOM   1681 C C     . VAL   A 1 240 ? 5.855   32.905 28.585 1   15.3  ? 221 VAL   A C     1 
ATOM   1682 O O     . VAL   A 1 240 ? 4.681   33.243 28.824 1   16.78 ? 221 VAL   A O     1 
ATOM   1683 C CB    . VAL   A 1 240 ? 7.047   30.969 29.65  1   15.46 ? 221 VAL   A CB    1 
ATOM   1684 C CG1   . VAL   A 1 240 ? 6.385   31.376 30.975 1   16.32 ? 221 VAL   A CG1   1 
ATOM   1685 C CG2   . VAL   A 1 240 ? 7.309   29.45  29.586 1   16.73 ? 221 VAL   A CG2   1 
ATOM   1686 N N     . GLU   A 1 241 ? 6.832   33.784 28.383 1   15.42 ? 222 GLU   A N     1 
ATOM   1687 C CA    . GLU   A 1 241 ? 6.559   35.207 28.511 1   16.66 ? 222 GLU   A CA    1 
ATOM   1688 C C     . GLU   A 1 241 ? 5.52    35.659 27.498 1   17.5  ? 222 GLU   A C     1 
ATOM   1689 O O     . GLU   A 1 241 ? 4.614   36.455 27.857 1   18.49 ? 222 GLU   A O     1 
ATOM   1690 C CB    . GLU   A 1 241 ? 7.851   35.951 28.243 1   18.24 ? 222 GLU   A CB    1 
ATOM   1691 C CG    . GLU   A 1 241 ? 8.848   35.925 29.356 1   26.4  ? 222 GLU   A CG    1 
ATOM   1692 C CD    . GLU   A 1 241 ? 10.233  36.341 28.877 1   37.48 ? 222 GLU   A CD    1 
ATOM   1693 O OE1   . GLU   A 1 241 ? 10.333  37.458 28.314 1   37.63 ? 222 GLU   A OE1   1 
ATOM   1694 O OE2   . GLU   A 1 241 ? 11.201  35.55  29.038 1   37.43 ? 222 GLU   A OE2   1 
ATOM   1695 N N     . ALA   A 1 242 ? 5.615   35.196 26.251 1   17.08 ? 223 ALA   A N     1 
ATOM   1696 C CA    . ALA   A 1 242 ? 4.636   35.605 25.232 1   17.28 ? 223 ALA   A CA    1 
ATOM   1697 C C     . ALA   A 1 242 ? 3.237   35.11  25.628 1   17.94 ? 223 ALA   A C     1 
ATOM   1698 O O     . ALA   A 1 242 ? 2.252   35.856 25.409 1   19.55 ? 223 ALA   A O     1 
ATOM   1699 C CB    . ALA   A 1 242 ? 5.005   35.051 23.853 1   18.66 ? 223 ALA   A CB    1 
ATOM   1700 N N     . ALA   A 1 243 ? 3.112   33.906 26.192 1   16.93 ? 224 ALA   A N     1 
ATOM   1701 C CA    . ALA   A 1 243 ? 1.774   33.381 26.51  1   16.95 ? 224 ALA   A CA    1 
ATOM   1702 C C     . ALA   A 1 243 ? 1.164   34.178 27.672 1   17.56 ? 224 ALA   A C     1 
ATOM   1703 O O     . ALA   A 1 243 ? -0.044  34.474 27.666 1   18.09 ? 224 ALA   A O     1 
ATOM   1704 C CB    . ALA   A 1 243 ? 1.896   31.906 26.877 1   16.99 ? 224 ALA   A CB    1 
ATOM   1705 N N     . VAL   A 1 244 ? 1.973   34.607 28.63  1   17.13 ? 225 VAL   A N     1 
ATOM   1706 C CA    . VAL   A 1 244 ? 1.485   35.406 29.762 1   17.2  ? 225 VAL   A CA    1 
ATOM   1707 C C     . VAL   A 1 244 ? 1.013   36.769 29.275 1   17.61 ? 225 VAL   A C     1 
ATOM   1708 O O     . VAL   A 1 244 ? -0.057  37.211 29.699 1   18.15 ? 225 VAL   A O     1 
ATOM   1709 C CB    . VAL   A 1 244 ? 2.611   35.538 30.803 1   17.85 ? 225 VAL   A CB    1 
ATOM   1710 C CG1   . VAL   A 1 244 ? 2.282   36.552 31.88  1   18.28 ? 225 VAL   A CG1   1 
ATOM   1711 C CG2   . VAL   A 1 244 ? 2.912   34.179 31.452 1   17.35 ? 225 VAL   A CG2   1 
ATOM   1712 N N     . LYS   A 1 245 ? 1.746   37.395 28.36  1   17.8  ? 226 LYS   A N     1 
ATOM   1713 C CA    . LYS   A 1 245 ? 1.268   38.685 27.796 1   18.69 ? 226 LYS   A CA    1 
ATOM   1714 C C     . LYS   A 1 245 ? 0.02    38.479 26.952 1   19.73 ? 226 LYS   A C     1 
ATOM   1715 O O     . LYS   A 1 245 ? -0.908  39.34  26.973 1   20.61 ? 226 LYS   A O     1 
ATOM   1716 C CB    . LYS   A 1 245 ? 2.376   39.327 26.937 1   19.89 ? 226 LYS   A CB    1 
ATOM   1717 C CG    . LYS   A 1 245 ? 3.52    39.79  27.799 1   20.76 ? 226 LYS   A CG    1 
ATOM   1718 C CD    . LYS   A 1 245 ? 4.698   40.288 26.958 1   32.45 ? 226 LYS   A CD    1 
ATOM   1719 C CE    . LYS   A 1 245 ? 5.967   40.299 27.752 1   41.97 ? 226 LYS   A CE    1 
ATOM   1720 N NZ    . LYS   A 1 245 ? 6.084   41.464 28.685 1   47.1  ? 226 LYS   A NZ    1 
ATOM   1721 N N     . GLU   A 1 246 ? -0.039  37.397 26.148 1   18.74 ? 227 GLU   A N     1 
ATOM   1722 C CA    . GLU   A 1 246 ? -1.219  37.153 25.327 1   20.11 ? 227 GLU   A CA    1 
ATOM   1723 C C     . GLU   A 1 246 ? -2.446  36.941 26.214 1   19.12 ? 227 GLU   A C     1 
ATOM   1724 O O     . GLU   A 1 246 ? -3.558  37.424 25.857 1   20.92 ? 227 GLU   A O     1 
ATOM   1725 C CB    . GLU   A 1 246 ? -0.943  35.931 24.424 1   21.33 ? 227 GLU   A CB    1 
ATOM   1726 C CG    . GLU   A 1 246 ? -2.046  35.592 23.427 1   23.28 ? 227 GLU   A CG    1 
ATOM   1727 C CD    . GLU   A 1 246 ? -1.772  34.349 22.587 1   29.06 ? 227 GLU   A CD    1 
ATOM   1728 O OE1   . GLU   A 1 246 ? -2.736  33.782 22.021 1   29.76 ? 227 GLU   A OE1   1 
ATOM   1729 O OE2   . GLU   A 1 246 ? -0.608  33.896 22.549 1   28.08 ? 227 GLU   A OE2   1 
ATOM   1730 N N     . ALA   A 1 247 ? -2.266  36.303 27.402 1   18.5  ? 228 ALA   A N     1 
ATOM   1731 C CA    . ALA   A 1 247 ? -3.366  35.99  28.287 1   18.94 ? 228 ALA   A CA    1 
ATOM   1732 C C     . ALA   A 1 247 ? -3.842  37.159 29.144 1   21.08 ? 228 ALA   A C     1 
ATOM   1733 O O     . ALA   A 1 247 ? -4.793  36.985 29.925 1   22.53 ? 228 ALA   A O     1 
ATOM   1734 C CB    . ALA   A 1 247 ? -3.039  34.76  29.155 1   19.43 ? 228 ALA   A CB    1 
ATOM   1735 N N     . GLY   A 1 248 ? -3.2    38.312 29.001 1   19.19 ? 229 GLY   A N     1 
ATOM   1736 C CA    . GLY   A 1 248 ? -3.699  39.526 29.625 1   20.79 ? 229 GLY   A CA    1 
ATOM   1737 C C     . GLY   A 1 248 ? -3.062  39.862 30.935 1   20.03 ? 229 GLY   A C     1 
ATOM   1738 O O     . GLY   A 1 248 ? -3.715  40.421 31.786 1   20.86 ? 229 GLY   A O     1 
ATOM   1739 N N     . TYR   A 1 249 ? -1.768  39.592 31.076 1   18.85 ? 230 TYR   A N     1 
ATOM   1740 C CA    . TYR   A 1 249 ? -1.025  39.975 32.283 1   17.25 ? 230 TYR   A CA    1 
ATOM   1741 C C     . TYR   A 1 249 ? 0.137   40.878 31.922 1   17.5  ? 230 TYR   A C     1 
ATOM   1742 O O     . TYR   A 1 249 ? 0.491   41     30.742 1   19.48 ? 230 TYR   A O     1 
ATOM   1743 C CB    . TYR   A 1 249 ? -0.426  38.702 32.985 1   17.47 ? 230 TYR   A CB    1 
ATOM   1744 C CG    . TYR   A 1 249 ? -1.454  37.691 33.395 1   17.07 ? 230 TYR   A CG    1 
ATOM   1745 C CD1   . TYR   A 1 249 ? -1.852  36.698 32.526 1   17.89 ? 230 TYR   A CD1   1 
ATOM   1746 C CD2   . TYR   A 1 249 ? -1.962  37.668 34.689 1   16.71 ? 230 TYR   A CD2   1 
ATOM   1747 C CE1   . TYR   A 1 249 ? -2.758  35.717 32.924 1   18.62 ? 230 TYR   A CE1   1 
ATOM   1748 C CE2   . TYR   A 1 249 ? -2.871  36.71  35.1   1   18.41 ? 230 TYR   A CE2   1 
ATOM   1749 C CZ    . TYR   A 1 249 ? -3.242  35.708 34.223 1   18.17 ? 230 TYR   A CZ    1 
ATOM   1750 O OH    . TYR   A 1 249 ? -4.142  34.721 34.619 1   18.89 ? 230 TYR   A OH    1 
ATOM   1751 N N     . THR   A 1 250 ? 0.682   41.52  32.931 1   17.58 ? 231 THR   A N     1 
ATOM   1752 C CA    . THR   A 1 250 ? 1.891   42.313 32.794 1   17.69 ? 231 THR   A CA    1 
ATOM   1753 C C     . THR   A 1 250 ? 2.913   41.752 33.749 1   18.89 ? 231 THR   A C     1 
ATOM   1754 O O     . THR   A 1 250 ? 2.604   41.558 34.935 1   18.71 ? 231 THR   A O     1 
ATOM   1755 C CB    . THR   A 1 250 ? 1.583   43.808 33.062 1   21.19 ? 231 THR   A CB    1 
ATOM   1756 O OG1   . THR   A 1 250 ? 2.743   44.591 32.711 1   23.35 ? 231 THR   A OG1   1 
ATOM   1757 C CG2   . THR   A 1 250 ? 1.117   44.052 34.492 1   21.45 ? 231 THR   A CG2   1 
ATOM   1758 N N     . ILE   A 1 251 ? 4.127   41.5   33.269 1   17.2  ? 232 ILE   A N     1 
ATOM   1759 C CA    . ILE   A 1 251 ? 5.136   40.8   34.08  1   16.75 ? 232 ILE   A CA    1 
ATOM   1760 C C     . ILE   A 1 251 ? 6.002   41.742 34.894 1   17.25 ? 232 ILE   A C     1 
ATOM   1761 O O     . ILE   A 1 251 ? 6.496   42.735 34.341 1   18.52 ? 232 ILE   A O     1 
ATOM   1762 C CB    . ILE   A 1 251 ? 5.998   39.987 33.095 1   17.51 ? 232 ILE   A CB    1 
ATOM   1763 C CG1   . ILE   A 1 251 ? 5.114   38.907 32.436 1   19.25 ? 232 ILE   A CG1   1 
ATOM   1764 C CG2   . ILE   A 1 251 ? 7.22    39.342 33.825 1   18.64 ? 232 ILE   A CG2   1 
ATOM   1765 C CD1   . ILE   A 1 251 ? 5.836   38.197 31.243 1   22.38 ? 232 ILE   A CD1   1 
ATOM   1766 N N     . GLU   A 1 252 ? 6.112   41.475 36.212 1   17.05 ? 233 GLU   A N     1 
ATOM   1767 C CA    . GLU   A 1 252 ? 6.936   42.291 37.132 1   17.38 ? 233 GLU   A CA    1 
ATOM   1768 C C     . GLU   A 1 252 ? 8.365   41.798 37.177 1   17.35 ? 233 GLU   A C     1 
ATOM   1769 O O     . GLU   A 1 252 ? 9.271   42.615 37.189 1   17.62 ? 233 GLU   A O     1 
ATOM   1770 C CB    . GLU   A 1 252 ? 6.321   42.311 38.511 1   19.86 ? 233 GLU   A CB    1 
ATOM   1771 C CG    . GLU   A 1 252 ? 4.997   43.092 38.445 1   24.3  ? 233 GLU   A CG    1 
ATOM   1772 C CD    . GLU   A 1 252 ? 4.425   43.548 39.772 1   30.93 ? 233 GLU   A CD    1 
ATOM   1773 O OE1   . GLU   A 1 252 ? 3.446   44.325 39.746 1   30.72 ? 233 GLU   A OE1   1 
ATOM   1774 O OE2   . GLU   A 1 252 ? 4.96    43.171 40.836 1   35.26 ? 233 GLU   A OE2   1 
ATOM   1775 N N     . TRP   A 1 253 ? 8.575   40.493 37.217 1   15.77 ? 234 TRP   A N     1 
ATOM   1776 C CA    . TRP   A 1 253 ? 9.937   39.939 37.147 1   15.79 ? 234 TRP   A CA    1 
ATOM   1777 C C     . TRP   A 1 253 ? 9.893   38.518 36.641 1   14.7  ? 234 TRP   A C     1 
ATOM   1778 O O     . TRP   A 1 253 ? 8.832   37.85  36.74  1   14.22 ? 234 TRP   A O     1 
ATOM   1779 C CB    . TRP   A 1 253 ? 10.744  40.107 38.424 1   18.83 ? 234 TRP   A CB    1 
ATOM   1780 C CG    . TRP   A 1 253 ? 10.162  39.392 39.586 1   19.53 ? 234 TRP   A CG    1 
ATOM   1781 C CD1   . TRP   A 1 253 ? 9.4     39.931 40.571 1   21.46 ? 234 TRP   A CD1   1 
ATOM   1782 C CD2   . TRP   A 1 253 ? 10.449  38.042 39.998 1   20.85 ? 234 TRP   A CD2   1 
ATOM   1783 N NE1   . TRP   A 1 253 ? 9.05    38.976 41.487 1   22.39 ? 234 TRP   A NE1   1 
ATOM   1784 C CE2   . TRP   A 1 253 ? 9.734   37.813 41.195 1   21.87 ? 234 TRP   A CE2   1 
ATOM   1785 C CE3   . TRP   A 1 253 ? 11.174  36.984 39.438 1   21.54 ? 234 TRP   A CE3   1 
ATOM   1786 C CZ2   . TRP   A 1 253 ? 9.714   36.566 41.827 1   23.66 ? 234 TRP   A CZ2   1 
ATOM   1787 C CZ3   . TRP   A 1 253 ? 11.097  35.72  40.028 1   23.13 ? 234 TRP   A CZ3   1 
ATOM   1788 C CH2   . TRP   A 1 253 ? 10.382  35.525 41.215 1   23.04 ? 234 TRP   A CH2   1 
ATOM   1789 N N     . PHE   A 1 254 ? 11.014  38.101 36.053 1   13.83 ? 235 PHE   A N     1 
ATOM   1790 C CA    . PHE   A 1 254 ? 11.078  36.794 35.444 1   14.19 ? 235 PHE   A CA    1 
ATOM   1791 C C     . PHE   A 1 254 ? 12.502  36.296 35.659 1   14.61 ? 235 PHE   A C     1 
ATOM   1792 O O     . PHE   A 1 254 ? 13.475  36.967 35.273 1   14.63 ? 235 PHE   A O     1 
ATOM   1793 C CB    . PHE   A 1 254 ? 10.796  36.91  33.947 1   14.78 ? 235 PHE   A CB    1 
ATOM   1794 C CG    . PHE   A 1 254 ? 10.502  35.597 33.235 1   15.25 ? 235 PHE   A CG    1 
ATOM   1795 C CD1   . PHE   A 1 254 ? 11.494  34.646 33.057 1   16.84 ? 235 PHE   A CD1   1 
ATOM   1796 C CD2   . PHE   A 1 254 ? 9.229   35.314 32.77  1   18.34 ? 235 PHE   A CD2   1 
ATOM   1797 C CE1   . PHE   A 1 254 ? 11.206  33.44  32.416 1   17.91 ? 235 PHE   A CE1   1 
ATOM   1798 C CE2   . PHE   A 1 254 ? 8.958   34.116 32.115 1   19.93 ? 235 PHE   A CE2   1 
ATOM   1799 C CZ    . PHE   A 1 254 ? 9.931   33.195 31.959 1   18.42 ? 235 PHE   A CZ    1 
ATOM   1800 N N     . GLU   A 1 255 ? 12.659  35.109 36.289 1   13.57 ? 236 GLU   A N     1 
ATOM   1801 C CA    . GLU   A 1 255 ? 13.978  34.542 36.566 1   13.64 ? 236 GLU   A CA    1 
ATOM   1802 C C     . GLU   A 1 255 ? 14.128  33.166 35.92  1   14.06 ? 236 GLU   A C     1 
ATOM   1803 O O     . GLU   A 1 255 ? 13.163  32.397 35.975 1   14.98 ? 236 GLU   A O     1 
ATOM   1804 C CB    . GLU   A 1 255 ? 14.154  34.362 38.082 1   15.32 ? 236 GLU   A CB    1 
ATOM   1805 C CG    . GLU   A 1 255 ? 15.533  33.863 38.535 1   17.15 ? 236 GLU   A CG    1 
ATOM   1806 C CD    . GLU   A 1 255 ? 15.519  33.355 39.965 1   20.16 ? 236 GLU   A CD    1 
ATOM   1807 O OE1   . GLU   A 1 255 ? 16.366  33.746 40.796 1   25.67 ? 236 GLU   A OE1   1 
ATOM   1808 O OE2   . GLU   A 1 255 ? 14.733  32.396 40.163 1   21.73 ? 236 GLU   A OE2   1 
ATOM   1809 N N     . VAL   A 1 256 ? 15.264  32.864 35.366 1   13.24 ? 237 VAL   A N     1 
ATOM   1810 C CA    . VAL   A 1 256 ? 15.611  31.538 34.862 1   13.59 ? 237 VAL   A CA    1 
ATOM   1811 C C     . VAL   A 1 256 ? 16.747  31.04  35.682 1   15.15 ? 237 VAL   A C     1 
ATOM   1812 O O     . VAL   A 1 256 ? 17.747  31.775 35.906 1   16.33 ? 237 VAL   A O     1 
ATOM   1813 C CB    . VAL   A 1 256 ? 15.94   31.546 33.361 1   16.46 ? 237 VAL   A CB    1 
ATOM   1814 C CG1   . VAL   A 1 256 ? 16.494  30.21  32.895 1   20.9  ? 237 VAL   A CG1   1 
ATOM   1815 C CG2   . VAL   A 1 256 ? 14.701  31.95  32.569 1   18.39 ? 237 VAL   A CG2   1 
ATOM   1816 N N     . ILE   A 1 257 ? 16.676  29.79  36.133 1   15    ? 238 ILE   A N     1 
ATOM   1817 C CA    . ILE   A 1 257 ? 17.81   29.106 36.776 1   16.01 ? 238 ILE   A CA    1 
ATOM   1818 C C     . ILE   A 1 257 ? 18.252  28.003 35.851 1   16.34 ? 238 ILE   A C     1 
ATOM   1819 O O     . ILE   A 1 257 ? 17.424  27.365 35.197 1   17.54 ? 238 ILE   A O     1 
ATOM   1820 C CB    . ILE   A 1 257 ? 17.571  28.589 38.229 1   18.22 ? 238 ILE   A CB    1 
ATOM   1821 C CG1   . ILE   A 1 257 ? 16.592  27.407 38.259 1   19.91 ? 238 ILE   A CG1   1 
ATOM   1822 C CG2   . ILE   A 1 257 ? 17.105  29.73  39.164 1   20.48 ? 238 ILE   A CG2   1 
ATOM   1823 C CD1   . ILE   A 1 257 ? 16.446  26.751 39.637 1   21.09 ? 238 ILE   A CD1   1 
ATOM   1824 N N     A SER   A 1 258 ? 19.544  27.738 35.804 0.5 15.42 ? 239 SER   A N     1 
ATOM   1825 N N     B SER   A 1 258 ? 19.529  27.715 35.85  0.5 16.15 ? 239 SER   A N     1 
ATOM   1826 C CA    A SER   A 1 258 ? 20.055  26.718 34.897 0.5 15.23 ? 239 SER   A CA    1 
ATOM   1827 C CA    B SER   A 1 258 ? 20.097  26.718 34.951 0.5 17.02 ? 239 SER   A CA    1 
ATOM   1828 C C     A SER   A 1 258 ? 19.906  25.308 35.457 0.5 17.03 ? 239 SER   A C     1 
ATOM   1829 C C     B SER   A 1 258 ? 20.059  25.286 35.493 0.5 18.16 ? 239 SER   A C     1 
ATOM   1830 O O     A SER   A 1 258 ? 19.797  24.37  34.663 0.5 17.28 ? 239 SER   A O     1 
ATOM   1831 O O     B SER   A 1 258 ? 20.187  24.324 34.724 0.5 18.8  ? 239 SER   A O     1 
ATOM   1832 C CB    A SER   A 1 258 ? 21.512  26.961 34.532 0.5 15.85 ? 239 SER   A CB    1 
ATOM   1833 C CB    B SER   A 1 258 ? 21.533  27.083 34.603 0.5 19.51 ? 239 SER   A CB    1 
ATOM   1834 O OG    A SER   A 1 258 ? 22.275  27.038 35.715 0.5 16.41 ? 239 SER   A OG    1 
ATOM   1835 O OG    B SER   A 1 258 ? 21.52   28.375 34.026 0.5 23.92 ? 239 SER   A OG    1 
ATOM   1836 N N     . GLN   A 1 259 ? 19.905  25.126 36.806 1   17.02 ? 240 GLN   A N     1 
ATOM   1837 C CA    . GLN   A 1 259 ? 19.861  23.783 37.433 1   17    ? 240 GLN   A CA    1 
ATOM   1838 C C     . GLN   A 1 259 ? 18.703  22.983 36.883 1   17.09 ? 240 GLN   A C     1 
ATOM   1839 O O     . GLN   A 1 259 ? 17.562  23.431 36.856 1   17.86 ? 240 GLN   A O     1 
ATOM   1840 C CB    . GLN   A 1 259 ? 19.649  23.956 38.936 1   19.76 ? 240 GLN   A CB    1 
ATOM   1841 C CG    . GLN   A 1 259 ? 19.542  22.665 39.73  1   22.25 ? 240 GLN   A CG    1 
ATOM   1842 C CD    . GLN   A 1 259 ? 20.816  21.909 39.765 1   24.48 ? 240 GLN   A CD    1 
ATOM   1843 O OE1   . GLN   A 1 259 ? 21.819  22.354 40.336 1   27.49 ? 240 GLN   A OE1   1 
ATOM   1844 N NE2   . GLN   A 1 259 ? 20.824  20.687 39.199 1   25.17 ? 240 GLN   A NE2   1 
ATOM   1845 N N     . SER   A 1 260 ? 19.025  21.753 36.46  1   17.71 ? 241 SER   A N     1 
ATOM   1846 C CA    . SER   A 1 260 ? 18.015  20.853 35.922 1   18.17 ? 241 SER   A CA    1 
ATOM   1847 C C     . SER   A 1 260 ? 17.835  19.687 36.861 1   18.81 ? 241 SER   A C     1 
ATOM   1848 O O     . SER   A 1 260 ? 18.663  19.441 37.729 1   19.68 ? 241 SER   A O     1 
ATOM   1849 C CB    . SER   A 1 260 ? 18.417  20.356 34.533 1   20.12 ? 241 SER   A CB    1 
ATOM   1850 O OG    . SER   A 1 260 ? 18.513  21.458 33.627 1   22.64 ? 241 SER   A OG    1 
ATOM   1851 N N     . TYR   A 1 261 ? 16.714  18.928 36.686 1   17.49 ? 242 TYR   A N     1 
ATOM   1852 C CA    . TYR   A 1 261 ? 16.506  17.742 37.509 1   18.68 ? 242 TYR   A CA    1 
ATOM   1853 C C     . TYR   A 1 261 ? 17.531  16.712 37.089 1   20.54 ? 242 TYR   A C     1 
ATOM   1854 O O     . TYR   A 1 261 ? 18.109  16.755 35.987 1   20.59 ? 242 TYR   A O     1 
ATOM   1855 C CB    . TYR   A 1 261 ? 15.073  17.238 37.214 1   17.02 ? 242 TYR   A CB    1 
ATOM   1856 C CG    . TYR   A 1 261 ? 14.036  18.09  37.908 1   15.3  ? 242 TYR   A CG    1 
ATOM   1857 C CD1   . TYR   A 1 261 ? 13.74   17.901 39.255 1   15.51 ? 242 TYR   A CD1   1 
ATOM   1858 C CD2   . TYR   A 1 261 ? 13.363  19.093 37.231 1   15.99 ? 242 TYR   A CD2   1 
ATOM   1859 C CE1   . TYR   A 1 261 ? 12.819  18.708 39.908 1   16.19 ? 242 TYR   A CE1   1 
ATOM   1860 C CE2   . TYR   A 1 261 ? 12.462  19.897 37.872 1   16.31 ? 242 TYR   A CE2   1 
ATOM   1861 C CZ    . TYR   A 1 261 ? 12.179  19.694 39.206 1   15.6  ? 242 TYR   A CZ    1 
ATOM   1862 O OH    . TYR   A 1 261 ? 11.228  20.49  39.755 1   17.14 ? 242 TYR   A OH    1 
ATOM   1863 N N     . SER   A 1 262 ? 17.608  15.654 37.9   1   21.92 ? 243 SER   A N     1 
ATOM   1864 C CA    . SER   A 1 262 ? 18.459  14.51  37.582 1   22.93 ? 243 SER   A CA    1 
ATOM   1865 C C     . SER   A 1 262 ? 17.981  13.88  36.251 1   23.57 ? 243 SER   A C     1 
ATOM   1866 O O     . SER   A 1 262 ? 16.778  13.878 35.956 1   20.41 ? 243 SER   A O     1 
ATOM   1867 C CB    . SER   A 1 262 ? 18.406  13.488 38.724 1   24.88 ? 243 SER   A CB    1 
ATOM   1868 O OG    . SER   A 1 262 ? 18.873  13.994 39.973 1   26.45 ? 243 SER   A OG    1 
ATOM   1869 N N     . SER   A 1 263 ? 18.893  13.265 35.479 1   26.65 ? 244 SER   A N     1 
ATOM   1870 C CA    . SER   A 1 263 ? 18.534  12.705 34.18  1   28.83 ? 244 SER   A CA    1 
ATOM   1871 C C     . SER   A 1 263 ? 17.49   11.587 34.21  1   28    ? 244 SER   A C     1 
ATOM   1872 O O     . SER   A 1 263 ? 16.753  11.432 33.242 1   30.17 ? 244 SER   A O     1 
ATOM   1873 C CB    . SER   A 1 263 ? 19.775  12.171 33.473 1   30.72 ? 244 SER   A CB    1 
ATOM   1874 O OG    . SER   A 1 263 ? 20.281  11.054 34.181 1   34.72 ? 244 SER   A OG    1 
ATOM   1875 N N     . THR   A 1 264 ? 17.365  10.889 35.362 1   27.33 ? 245 THR   A N     1 
ATOM   1876 C CA    . THR   A 1 264 ? 16.372  9.815  35.58  1   28.08 ? 245 THR   A CA    1 
ATOM   1877 C C     . THR   A 1 264 ? 15.01   10.375 35.907 1   26.67 ? 245 THR   A C     1 
ATOM   1878 O O     . THR   A 1 264 ? 14.029  9.626  35.99  1   26.99 ? 245 THR   A O     1 
ATOM   1879 C CB    . THR   A 1 264 ? 16.829  8.934  36.763 1   32.16 ? 245 THR   A CB    1 
ATOM   1880 O OG1   . THR   A 1 264 ? 17.032  9.792  37.9   1   35.45 ? 245 THR   A OG1   1 
ATOM   1881 C CG2   . THR   A 1 264 ? 18.143  8.224  36.474 1   33.55 ? 245 THR   A CG2   1 
ATOM   1882 N N     . MET   A 1 265 ? 14.905  11.715 36.106 1   22.64 ? 246 MET   A N     1 
ATOM   1883 C CA    . MET   A 1 265 ? 13.66   12.309 36.471 1   21.59 ? 246 MET   A CA    1 
ATOM   1884 C C     . MET   A 1 265 ? 13.045  13.077 35.331 1   21.18 ? 246 MET   A C     1 
ATOM   1885 O O     . MET   A 1 265 ? 11.842  13.018 35.145 1   19.86 ? 246 MET   A O     1 
ATOM   1886 C CB    . MET   A 1 265 ? 13.792  13.241 37.699 1   25.12 ? 246 MET   A CB    1 
ATOM   1887 C CG    . MET   A 1 265 ? 14.993  13.018 38.576 1   35.29 ? 246 MET   A CG    1 
ATOM   1888 S SD    . MET   A 1 265 ? 14.92   11.727 39.791 1   41.02 ? 246 MET   A SD    1 
ATOM   1889 C CE    . MET   A 1 265 ? 13.093  11.774 40.093 1   23.87 ? 246 MET   A CE    1 
ATOM   1890 N N     . ALA   A 1 266 ? 13.814  13.934 34.669 1   20.23 ? 247 ALA   A N     1 
ATOM   1891 C CA    . ALA   A 1 266 ? 13.225  14.816 33.646 1   20.66 ? 247 ALA   A CA    1 
ATOM   1892 C C     . ALA   A 1 266 ? 14.275  15.388 32.745 1   22.72 ? 247 ALA   A C     1 
ATOM   1893 O O     . ALA   A 1 266 ? 15.448  15.421 33.139 1   26.27 ? 247 ALA   A O     1 
ATOM   1894 C CB    . ALA   A 1 266 ? 12.436  15.967 34.313 1   20.51 ? 247 ALA   A CB    1 
ATOM   1895 N N     . ASN   A 1 267 ? 13.885  15.77  31.529 1   19.82 ? 248 ASN   A N     1 
ATOM   1896 C CA    . ASN   A 1 267 ? 14.856  16.302 30.567 1   19.54 ? 248 ASN   A CA    1 
ATOM   1897 C C     . ASN   A 1 267 ? 14.773  17.827 30.425 1   21.19 ? 248 ASN   A C     1 
ATOM   1898 O O     . ASN   A 1 267 ? 14.948  18.345 29.322 1   23.64 ? 248 ASN   A O     1 
ATOM   1899 C CB    . ASN   A 1 267 ? 14.676  15.642 29.204 1   20.95 ? 248 ASN   A CB    1 
ATOM   1900 C CG    . ASN   A 1 267 ? 13.356  15.907 28.541 1   23.83 ? 248 ASN   A CG    1 
ATOM   1901 O OD1   . ASN   A 1 267 ? 12.391  16.334 29.18  1   21.99 ? 248 ASN   A OD1   1 
ATOM   1902 N ND2   . ASN   A 1 267 ? 13.252  15.645 27.207 1   24.89 ? 248 ASN   A ND2   1 
ATOM   1903 N N     . ASN   A 1 268 ? 14.593  18.545 31.54  1   17.74 ? 249 ASN   A N     1 
ATOM   1904 C CA    . ASN   A 1 268 ? 14.467  19.999 31.44  1   16.83 ? 249 ASN   A CA    1 
ATOM   1905 C C     . ASN   A 1 268 ? 15.821  20.643 31.23  1   17.8  ? 249 ASN   A C     1 
ATOM   1906 O O     . ASN   A 1 268 ? 16.877  20.072 31.465 1   19.42 ? 249 ASN   A O     1 
ATOM   1907 C CB    . ASN   A 1 268 ? 13.772  20.546 32.68  1   18.42 ? 249 ASN   A CB    1 
ATOM   1908 C CG    . ASN   A 1 268 ? 14.554  20.366 33.967 1   17.42 ? 249 ASN   A CG    1 
ATOM   1909 O OD1   . ASN   A 1 268 ? 15.035  19.27  34.295 1   17.36 ? 249 ASN   A OD1   1 
ATOM   1910 N ND2   . ASN   A 1 268 ? 14.587  21.41  34.811 1   16.58 ? 249 ASN   A ND2   1 
ATOM   1911 N N     . GLU   A 1 269 ? 15.772  21.914 30.841 1   16.62 ? 250 GLU   A N     1 
ATOM   1912 C CA    . GLU   A 1 269 ? 16.911  22.815 30.765 1   18.16 ? 250 GLU   A CA    1 
ATOM   1913 C C     . GLU   A 1 269 ? 16.558  23.97  31.686 1   18.24 ? 250 GLU   A C     1 
ATOM   1914 O O     . GLU   A 1 269 ? 16.169  25.064 31.248 1   18.36 ? 250 GLU   A O     1 
ATOM   1915 C CB    . GLU   A 1 269 ? 17.179  23.362 29.346 1   19.7  ? 250 GLU   A CB    1 
ATOM   1916 C CG    . GLU   A 1 269 ? 17.555  22.2   28.439 1   23.49 ? 250 GLU   A CG    1 
ATOM   1917 C CD    . GLU   A 1 269 ? 17.79   22.591 26.997 1   33.68 ? 250 GLU   A CD    1 
ATOM   1918 O OE1   . GLU   A 1 269 ? 17.249  21.889 26.113 1   36.66 ? 250 GLU   A OE1   1 
ATOM   1919 O OE2   . GLU   A 1 269 ? 18.526  23.578 26.752 1   35.25 ? 250 GLU   A OE2   1 
ATOM   1920 N N     . GLY   A 1 270 ? 16.656  23.699 32.971 1   15.89 ? 251 GLY   A N     1 
ATOM   1921 C CA    . GLY   A 1 270 ? 16.394  24.685 34.009 1   16.86 ? 251 GLY   A CA    1 
ATOM   1922 C C     . GLY   A 1 270 ? 14.929  24.911 34.308 1   14.73 ? 251 GLY   A C     1 
ATOM   1923 O O     . GLY   A 1 270 ? 14.042  24.108 33.955 1   14.92 ? 251 GLY   A O     1 
ATOM   1924 N N     . LEU   A 1 271 ? 14.653  25.972 35.048 1   14.83 ? 252 LEU   A N     1 
ATOM   1925 C CA    . LEU   A 1 271 ? 13.308  26.295 35.495 1   13.87 ? 252 LEU   A CA    1 
ATOM   1926 C C     . LEU   A 1 271 ? 13.144  27.778 35.447 1   13.62 ? 252 LEU   A C     1 
ATOM   1927 O O     . LEU   A 1 271 ? 14.132  28.52  35.485 1   15.12 ? 252 LEU   A O     1 
ATOM   1928 C CB    . LEU   A 1 271 ? 13.099  25.89  36.966 1   15.32 ? 252 LEU   A CB    1 
ATOM   1929 C CG    . LEU   A 1 271 ? 12.87   24.368 37.163 1   17.47 ? 252 LEU   A CG    1 
ATOM   1930 C CD1   . LEU   A 1 271 ? 14.208  23.713 37.517 1   19.69 ? 252 LEU   A CD1   1 
ATOM   1931 C CD2   . LEU   A 1 271 ? 11.912  24.136 38.347 1   18.67 ? 252 LEU   A CD2   1 
ATOM   1932 N N     . PHE   A 1 272 ? 11.932  28.235 35.386 1   13.59 ? 253 PHE   A N     1 
ATOM   1933 C CA    . PHE   A 1 272 ? 11.617  29.643 35.485 1   13.32 ? 253 PHE   A CA    1 
ATOM   1934 C C     . PHE   A 1 272 ? 10.714  29.912 36.677 1   13.49 ? 253 PHE   A C     1 
ATOM   1935 O O     . PHE   A 1 272 ? 9.955   29.053 37.101 1   13.84 ? 253 PHE   A O     1 
ATOM   1936 C CB    . PHE   A 1 272 ? 10.985  30.171 34.215 1   13.62 ? 253 PHE   A CB    1 
ATOM   1937 C CG    . PHE   A 1 272 ? 9.547   29.758 34.026 1   13.96 ? 253 PHE   A CG    1 
ATOM   1938 C CD1   . PHE   A 1 272 ? 8.504   30.542 34.531 1   14.7  ? 253 PHE   A CD1   1 
ATOM   1939 C CD2   . PHE   A 1 272 ? 9.23    28.635 33.292 1   14.47 ? 253 PHE   A CD2   1 
ATOM   1940 C CE1   . PHE   A 1 272 ? 7.164   30.132 34.384 1   15.23 ? 253 PHE   A CE1   1 
ATOM   1941 C CE2   . PHE   A 1 272 ? 7.893   28.233 33.149 1   15.05 ? 253 PHE   A CE2   1 
ATOM   1942 C CZ    . PHE   A 1 272 ? 6.875   28.976 33.717 1   14.34 ? 253 PHE   A CZ    1 
ATOM   1943 N N     . SER   A 1 273 ? 10.724  31.19  37.092 1   13.65 ? 254 SER   A N     1 
ATOM   1944 C CA    . SER   A 1 273 ? 9.799   31.729 38.072 1   14.25 ? 254 SER   A CA    1 
ATOM   1945 C C     . SER   A 1 273 ? 9.38    33.09  37.562 1   13.42 ? 254 SER   A C     1 
ATOM   1946 O O     . SER   A 1 273 ? 10.219  33.866 37.101 1   13.57 ? 254 SER   A O     1 
ATOM   1947 C CB    . SER   A 1 273 ? 10.451  31.935 39.444 1   17.55 ? 254 SER   A CB    1 
ATOM   1948 O OG    . SER   A 1 273 ? 10.907  30.697 39.979 1   19.92 ? 254 SER   A OG    1 
ATOM   1949 N N     . LEU   A 1 274 ? 8.112   33.415 37.719 1   13.07 ? 255 LEU   A N     1 
ATOM   1950 C CA    . LEU   A 1 274 ? 7.631   34.743 37.346 1   14.59 ? 255 LEU   A CA    1 
ATOM   1951 C C     . LEU   A 1 274 ? 6.562   35.221 38.26  1   14.45 ? 255 LEU   A C     1 
ATOM   1952 O O     . LEU   A 1 274 ? 5.803   34.423 38.817 1   14.46 ? 255 LEU   A O     1 
ATOM   1953 C CB    . LEU   A 1 274 ? 7.222   34.809 35.902 1   15.8  ? 255 LEU   A CB    1 
ATOM   1954 C CG    . LEU   A 1 274 ? 5.964   34.015 35.531 1   15.89 ? 255 LEU   A CG    1 
ATOM   1955 C CD1   . LEU   A 1 274 ? 4.65    34.867 35.737 1   17.91 ? 255 LEU   A CD1   1 
ATOM   1956 C CD2   . LEU   A 1 274 ? 5.994   33.609 34.065 1   17.47 ? 255 LEU   A CD2   1 
ATOM   1957 N N     . VAL   A 1 275 ? 6.441   36.57  38.343 1   14.39 ? 256 VAL   A N     1 
ATOM   1958 C CA    . VAL   A 1 275 ? 5.329   37.231 39.039 1   15.09 ? 256 VAL   A CA    1 
ATOM   1959 C C     . VAL   A 1 275 ? 4.777   38.239 38.026 1   15.18 ? 256 VAL   A C     1 
ATOM   1960 O O     . VAL   A 1 275 ? 5.519   39.034 37.414 1   15.23 ? 256 VAL   A O     1 
ATOM   1961 C CB    . VAL   A 1 275 ? 5.752   37.934 40.345 1   18.72 ? 256 VAL   A CB    1 
ATOM   1962 C CG1   . VAL   A 1 275 ? 4.598   38.767 40.919 1   20.88 ? 256 VAL   A CG1   1 
ATOM   1963 C CG2   . VAL   A 1 275 ? 6.239   36.884 41.373 1   20.4  ? 256 VAL   A CG2   1 
ATOM   1964 N N     . ALA   A 1 276 ? 3.459   38.166 37.855 1   16.5  ? 257 ALA   A N     1 
ATOM   1965 C CA    . ALA   A 1 276 ? 2.751   39.052 36.953 1   17.47 ? 257 ALA   A CA    1 
ATOM   1966 C C     . ALA   A 1 276 ? 1.489   39.574 37.639 1   16.95 ? 257 ALA   A C     1 
ATOM   1967 O O     . ALA   A 1 276 ? 1.052   39.032 38.655 1   17.41 ? 257 ALA   A O     1 
ATOM   1968 C CB    . ALA   A 1 276 ? 2.401   38.306 35.663 1   18.27 ? 257 ALA   A CB    1 
ATOM   1969 N N     . ARG   A 1 277 ? 0.89    40.628 37.052 1   17.62 ? 258 ARG   A N     1 
ATOM   1970 C CA    . ARG   A 1 277 ? -0.402  41.133 37.511 1   18.02 ? 258 ARG   A CA    1 
ATOM   1971 C C     . ARG   A 1 277 ? -1.433  41.026 36.382 1   17.75 ? 258 ARG   A C     1 
ATOM   1972 O O     . ARG   A 1 277 ? -1.097  41.28  35.218 1   19.05 ? 258 ARG   A O     1 
ATOM   1973 C CB    . ARG   A 1 277 ? -0.301  42.623 37.955 1   20.56 ? 258 ARG   A CB    1 
ATOM   1974 C CG    . ARG   A 1 277 ? 0.491   42.746 39.257 1   25.32 ? 258 ARG   A CG    1 
ATOM   1975 C CD    . ARG   A 1 277 ? 0.355   44.175 39.758 1   32.53 ? 258 ARG   A CD    1 
ATOM   1976 N NE    . ARG   A 1 277 ? -0.819  44.354 40.609 1   40.97 ? 258 ARG   A NE    1 
ATOM   1977 C CZ    . ARG   A 1 277 ? -1.002  45.386 41.431 1   46.97 ? 258 ARG   A CZ    1 
ATOM   1978 N NH1   . ARG   A 1 277 ? -0.107  46.366 41.49  1   47.38 ? 258 ARG   A NH1   1 
ATOM   1979 N NH2   . ARG   A 1 277 ? -2.096  45.461 42.177 1   49.9  ? 258 ARG   A NH2   1 
ATOM   1980 N N     . LYS   A 1 278 ? -2.653  40.697 36.733 1   19.63 ? 259 LYS   A N     1 
ATOM   1981 C CA    . LYS   A 1 278 ? -3.709  40.638 35.729 1   19.84 ? 259 LYS   A CA    1 
ATOM   1982 C C     . LYS   A 1 278 ? -4.156  42.033 35.309 1   22.52 ? 259 LYS   A C     1 
ATOM   1983 O O     . LYS   A 1 278 ? -4.37   42.843 36.175 1   24.56 ? 259 LYS   A O     1 
ATOM   1984 C CB    . LYS   A 1 278 ? -4.896  39.95  36.373 1   21.94 ? 259 LYS   A CB    1 
ATOM   1985 C CG    . LYS   A 1 278 ? -5.99   39.605 35.397 1   23.56 ? 259 LYS   A CG    1 
ATOM   1986 C CD    . LYS   A 1 278 ? -7.234  39.139 36.196 1   28.04 ? 259 LYS   A CD    1 
ATOM   1987 C CE    . LYS   A 1 278 ? -8.367  38.971 35.285 1   29.81 ? 259 LYS   A CE    1 
ATOM   1988 N NZ    . LYS   A 1 278 ? -9.507  38.417 36.035 1   25.9  ? 259 LYS   A NZ    1 
ATOM   1989 N N     . LEU   A 1 279 ? -4.275  42.267 34.01  1   23.42 ? 260 LEU   A N     1 
ATOM   1990 C CA    . LEU   A 1 279 ? -4.817  43.581 33.529 1   25.87 ? 260 LEU   A CA    1 
ATOM   1991 C C     . LEU   A 1 279 ? -6.355  43.538 33.59  1   29.78 ? 260 LEU   A C     1 
ATOM   1992 O O     . LEU   A 1 279 ? -6.974  42.534 33.297 1   31.03 ? 260 LEU   A O     1 
ATOM   1993 C CB    . LEU   A 1 279 ? -4.326  43.796 32.094 1   27.8  ? 260 LEU   A CB    1 
ATOM   1994 C CG    . LEU   A 1 279 ? -2.797  43.776 31.9   1   31.38 ? 260 LEU   A CG    1 
ATOM   1995 C CD1   . LEU   A 1 279 ? -2.423  43.914 30.485 1   33.33 ? 260 LEU   A CD1   1 
ATOM   1996 C CD2   . LEU   A 1 279 ? -2.163  44.861 32.614 1   32.19 ? 260 LEU   A CD2   1 
ATOM   1997 N N     . PHE   B 1 24  ? 31.215  58.454 23.889 1   24.21 ? 5   PHE   B N     1 
ATOM   1998 C CA    . PHE   B 1 24  ? 31.039  57.856 25.21  1   22.74 ? 5   PHE   B CA    1 
ATOM   1999 C C     . PHE   B 1 24  ? 31.868  58.61  26.26  1   20.51 ? 5   PHE   B C     1 
ATOM   2000 O O     . PHE   B 1 24  ? 32.995  59.02  25.991 1   20.41 ? 5   PHE   B O     1 
ATOM   2001 C CB    . PHE   B 1 24  ? 31.47   56.41  25.165 1   23.5  ? 5   PHE   B CB    1 
ATOM   2002 C CG    . PHE   B 1 24  ? 30.718  55.58  26.205 1   24.65 ? 5   PHE   B CG    1 
ATOM   2003 C CD1   . PHE   B 1 24  ? 29.518  54.946 25.896 1   24.94 ? 5   PHE   B CD1   1 
ATOM   2004 C CD2   . PHE   B 1 24  ? 31.251  55.38  27.455 1   26.09 ? 5   PHE   B CD2   1 
ATOM   2005 C CE1   . PHE   B 1 24  ? 28.888  54.113 26.837 1   24.7  ? 5   PHE   B CE1   1 
ATOM   2006 C CE2   . PHE   B 1 24  ? 30.618  54.584 28.39  1   26.27 ? 5   PHE   B CE2   1 
ATOM   2007 C CZ    . PHE   B 1 24  ? 29.405  53.996 28.114 1   23.83 ? 5   PHE   B CZ    1 
ATOM   2008 N N     . THR   B 1 25  ? 31.346  58.766 27.478 1   18.56 ? 6   THR   B N     1 
ATOM   2009 C CA    . THR   B 1 25  ? 32.04   59.497 28.557 1   17.27 ? 6   THR   B CA    1 
ATOM   2010 C C     . THR   B 1 25  ? 33.393  58.845 28.823 1   18.19 ? 6   THR   B C     1 
ATOM   2011 O O     . THR   B 1 25  ? 33.482  57.654 29.084 1   18.74 ? 6   THR   B O     1 
ATOM   2012 C CB    . THR   B 1 25  ? 31.194  59.383 29.84  1   17.08 ? 6   THR   B CB    1 
ATOM   2013 O OG1   . THR   B 1 25  ? 29.909  59.995 29.623 1   16.92 ? 6   THR   B OG1   1 
ATOM   2014 C CG2   . THR   B 1 25  ? 31.868  60.031 31.033 1   18.07 ? 6   THR   B CG2   1 
ATOM   2015 N N     . SER   B 1 26  ? 34.46   59.667 28.768 1   19.86 ? 7   SER   B N     1 
ATOM   2016 C CA    . SER   B 1 26  ? 35.814  59.151 29.03  1   21.24 ? 7   SER   B CA    1 
ATOM   2017 C C     . SER   B 1 26  ? 35.994  58.852 30.5   1   20.4  ? 7   SER   B C     1 
ATOM   2018 O O     . SER   B 1 26  ? 35.367  59.52  31.329 1   19.87 ? 7   SER   B O     1 
ATOM   2019 C CB    . SER   B 1 26  ? 36.842  60.181 28.581 1   24.36 ? 7   SER   B CB    1 
ATOM   2020 O OG    . SER   B 1 26  ? 36.605  61.427 29.217 1   27.63 ? 7   SER   B OG    1 
ATOM   2021 N N     . LYS   B 1 27  ? 36.868  57.898 30.879 1   18.93 ? 8   LYS   B N     1 
ATOM   2022 C CA    . LYS   B 1 27  ? 37.01   57.518 32.284 1   19.06 ? 8   LYS   B CA    1 
ATOM   2023 C C     . LYS   B 1 27  ? 37.538  58.661 33.115 1   20.3  ? 8   LYS   B C     1 
ATOM   2024 O O     . LYS   B 1 27  ? 37.153  58.777 34.273 1   20.56 ? 8   LYS   B O     1 
ATOM   2025 C CB    . LYS   B 1 27  ? 37.806  56.158 32.505 1   20.86 ? 8   LYS   B CB    1 
ATOM   2026 C CG    . LYS   B 1 27  ? 39.266  56.228 32.067 1   23.18 ? 8   LYS   B CG    1 
ATOM   2027 C CD    . LYS   B 1 27  ? 39.875  54.786 32.081 1   23.74 ? 8   LYS   B CD    1 
ATOM   2028 C CE    . LYS   B 1 27  ? 41.278  54.754 31.522 1   28.53 ? 8   LYS   B CE    1 
ATOM   2029 N NZ    . LYS   B 1 27  ? 41.653  53.344 31.219 1   29.78 ? 8   LYS   B NZ    1 
ATOM   2030 N N     . ASP   B 1 28  ? 38.358  59.564 32.546 1   20.39 ? 9   ASP   B N     1 
ATOM   2031 C CA    . ASP   B 1 28  ? 38.823  60.721 33.327 1   20.28 ? 9   ASP   B CA    1 
ATOM   2032 C C     . ASP   B 1 28  ? 37.656  61.598 33.795 1   19.82 ? 9   ASP   B C     1 
ATOM   2033 O O     . ASP   B 1 28  ? 37.775  62.275 34.824 1   21.2  ? 9   ASP   B O     1 
ATOM   2034 C CB    . ASP   B 1 28  ? 39.837  61.523 32.54  1   22.12 ? 9   ASP   B CB    1 
ATOM   2035 C CG    . ASP   B 1 28  ? 39.203  62.177 31.341 1   30.34 ? 9   ASP   B CG    1 
ATOM   2036 O OD1   . ASP   B 1 28  ? 38.797  63.357 31.453 1   33.74 ? 9   ASP   B OD1   1 
ATOM   2037 O OD2   . ASP   B 1 28  ? 39.032  61.495 30.336 1   33.84 ? 9   ASP   B OD2   1 
ATOM   2038 N N     . THR   B 1 29  ? 36.498  61.58  33.08  1   19.01 ? 10  THR   B N     1 
ATOM   2039 C CA    . THR   B 1 29  ? 35.335  62.357 33.499 1   18.22 ? 10  THR   B CA    1 
ATOM   2040 C C     . THR   B 1 29  ? 34.823  61.912 34.875 1   17.2  ? 10  THR   B C     1 
ATOM   2041 O O     . THR   B 1 29  ? 34.234  62.687 35.632 1   18.73 ? 10  THR   B O     1 
ATOM   2042 C CB    . THR   B 1 29  ? 34.22   62.265 32.443 1   22.24 ? 10  THR   B CB    1 
ATOM   2043 O OG1   . THR   B 1 29  ? 34.794  62.649 31.191 1   26.47 ? 10  THR   B OG1   1 
ATOM   2044 C CG2   . THR   B 1 29  ? 33.021  63.141 32.763 1   21.48 ? 10  THR   B CG2   1 
ATOM   2045 N N     . TYR   B 1 30  ? 34.995  60.623 35.196 1   16.2  ? 11  TYR   B N     1 
ATOM   2046 C CA    . TYR   B 1 30  ? 34.597  60.128 36.518 1   16.84 ? 11  TYR   B CA    1 
ATOM   2047 C C     . TYR   B 1 30  ? 35.451  60.685 37.633 1   19.17 ? 11  TYR   B C     1 
ATOM   2048 O O     . TYR   B 1 30  ? 34.953  60.812 38.74  1   22.01 ? 11  TYR   B O     1 
ATOM   2049 C CB    . TYR   B 1 30  ? 34.607  58.592 36.569 1   15.94 ? 11  TYR   B CB    1 
ATOM   2050 C CG    . TYR   B 1 30  ? 33.34   58.053 35.969 1   13.55 ? 11  TYR   B CG    1 
ATOM   2051 C CD1   . TYR   B 1 30  ? 33.262  57.729 34.605 1   13.88 ? 11  TYR   B CD1   1 
ATOM   2052 C CD2   . TYR   B 1 30  ? 32.194  57.93  36.739 1   13.48 ? 11  TYR   B CD2   1 
ATOM   2053 C CE1   . TYR   B 1 30  ? 32.057  57.314 34.021 1   14.91 ? 11  TYR   B CE1   1 
ATOM   2054 C CE2   . TYR   B 1 30  ? 31.018  57.452 36.189 1   13.54 ? 11  TYR   B CE2   1 
ATOM   2055 C CZ    . TYR   B 1 30  ? 30.939  57.165 34.831 1   14.39 ? 11  TYR   B CZ    1 
ATOM   2056 O OH    . TYR   B 1 30  ? 29.739  56.741 34.321 1   15.83 ? 11  TYR   B OH    1 
ATOM   2057 N N     . LEU   B 1 31  ? 36.718  61.007 37.357 1   18.1  ? 12  LEU   B N     1 
ATOM   2058 C CA    . LEU   B 1 31  ? 37.575  61.543 38.415 1   19.75 ? 12  LEU   B CA    1 
ATOM   2059 C C     . LEU   B 1 31  ? 37.133  62.956 38.837 1   21.61 ? 12  LEU   B C     1 
ATOM   2060 O O     . LEU   B 1 31  ? 37.164  63.306 40.014 1   22.85 ? 12  LEU   B O     1 
ATOM   2061 C CB    . LEU   B 1 31  ? 39.037  61.588 37.971 1   21.09 ? 12  LEU   B CB    1 
ATOM   2062 C CG    . LEU   B 1 31  ? 39.617  60.271 37.516 1   23.66 ? 12  LEU   B CG    1 
ATOM   2063 C CD1   . LEU   B 1 31  ? 41.012  60.451 36.976 1   25.47 ? 12  LEU   B CD1   1 
ATOM   2064 C CD2   . LEU   B 1 31  ? 39.669  59.286 38.652 1   25.34 ? 12  LEU   B CD2   1 
ATOM   2065 N N     . SER   B 1 32  ? 36.677  63.736 37.861 1   21.32 ? 13  SER   B N     1 
ATOM   2066 C CA    . SER   B 1 32  ? 36.404  65.161 38.003 1   21.81 ? 13  SER   B CA    1 
ATOM   2067 C C     . SER   B 1 32  ? 34.938  65.56  38.118 1   21.74 ? 13  SER   B C     1 
ATOM   2068 O O     . SER   B 1 32  ? 34.605  66.521 38.832 1   25.46 ? 13  SER   B O     1 
ATOM   2069 C CB    . SER   B 1 32  ? 36.985  65.845 36.772 1   21.35 ? 13  SER   B CB    1 
ATOM   2070 O OG    . SER   B 1 32  ? 36.651  65.262 35.516 1   21.31 ? 13  SER   B OG    1 
ATOM   2071 N N     . HIS   B 1 33  ? 34.039  64.837 37.425 1   17.85 ? 14  HIS   B N     1 
ATOM   2072 C CA    . HIS   B 1 33  ? 32.676  65.278 37.295 1   16.97 ? 14  HIS   B CA    1 
ATOM   2073 C C     . HIS   B 1 33  ? 31.616  64.43  37.975 1   17.62 ? 14  HIS   B C     1 
ATOM   2074 O O     . HIS   B 1 33  ? 30.418  64.75  37.923 1   18.69 ? 14  HIS   B O     1 
ATOM   2075 C CB    . HIS   B 1 33  ? 32.342  65.392 35.791 1   15.62 ? 14  HIS   B CB    1 
ATOM   2076 C CG    . HIS   B 1 33  ? 33.031  66.564 35.161 1   17.35 ? 14  HIS   B CG    1 
ATOM   2077 N ND1   . HIS   B 1 33  ? 34.415  66.617 34.967 1   18.86 ? 14  HIS   B ND1   1 
ATOM   2078 C CD2   . HIS   B 1 33  ? 32.481  67.737 34.774 1   20.09 ? 14  HIS   B CD2   1 
ATOM   2079 C CE1   . HIS   B 1 33  ? 34.663  67.84  34.496 1   20.36 ? 14  HIS   B CE1   1 
ATOM   2080 N NE2   . HIS   B 1 33  ? 33.525  68.531 34.32  1   21.81 ? 14  HIS   B NE2   1 
ATOM   2081 N N     . PHE   B 1 34  ? 32.013  63.255 38.505 1   17.38 ? 15  PHE   B N     1 
ATOM   2082 C CA    . PHE   B 1 34  ? 31.039  62.419 39.251 1   16.16 ? 15  PHE   B CA    1 
ATOM   2083 C C     . PHE   B 1 34  ? 31.07   62.866 40.721 1   17.72 ? 15  PHE   B C     1 
ATOM   2084 O O     . PHE   B 1 34  ? 32.083  62.689 41.401 1   17.32 ? 15  PHE   B O     1 
ATOM   2085 C CB    . PHE   B 1 34  ? 31.453  60.933 39.133 1   15.27 ? 15  PHE   B CB    1 
ATOM   2086 C CG    . PHE   B 1 34  ? 30.47   59.941 39.702 1   14.62 ? 15  PHE   B CG    1 
ATOM   2087 C CD1   . PHE   B 1 34  ? 30.368  59.739 41.087 1   15.37 ? 15  PHE   B CD1   1 
ATOM   2088 C CD2   . PHE   B 1 34  ? 29.668  59.207 38.867 1   14.28 ? 15  PHE   B CD2   1 
ATOM   2089 C CE1   . PHE   B 1 34  ? 29.494  58.781 41.614 1   15.38 ? 15  PHE   B CE1   1 
ATOM   2090 C CE2   . PHE   B 1 34  ? 28.847  58.21  39.39  1   15.75 ? 15  PHE   B CE2   1 
ATOM   2091 C CZ    . PHE   B 1 34  ? 28.745  58.036 40.761 1   15.23 ? 15  PHE   B CZ    1 
ATOM   2092 N N     . ASN   B 1 35  ? 30.024  63.56  41.139 1   17.39 ? 16  ASN   B N     1 
ATOM   2093 C CA    . ASN   B 1 35  ? 29.956  64.132 42.474 1   18.03 ? 16  ASN   B CA    1 
ATOM   2094 C C     . ASN   B 1 35  ? 29.374  63.095 43.409 1   17.71 ? 16  ASN   B C     1 
ATOM   2095 O O     . ASN   B 1 35  ? 28.203  62.804 43.305 1   18.05 ? 16  ASN   B O     1 
ATOM   2096 C CB    . ASN   B 1 35  ? 29.053  65.368 42.412 1   18.79 ? 16  ASN   B CB    1 
ATOM   2097 C CG    . ASN   B 1 35  ? 28.917  66.069 43.737 1   23.26 ? 16  ASN   B CG    1 
ATOM   2098 O OD1   . ASN   B 1 35  ? 28.836  65.485 44.827 1   22.86 ? 16  ASN   B OD1   1 
ATOM   2099 N ND2   . ASN   B 1 35  ? 28.871  67.409 43.685 1   26.47 ? 16  ASN   B ND2   1 
ATOM   2100 N N     . PRO   B 1 36  ? 30.185  62.506 44.31  1   17.69 ? 17  PRO   B N     1 
ATOM   2101 C CA    . PRO   B 1 36  ? 29.654  61.366 45.11  1   18.32 ? 17  PRO   B CA    1 
ATOM   2102 C C     . PRO   B 1 36  ? 28.485  61.718 46.012 1   19.28 ? 17  PRO   B C     1 
ATOM   2103 O O     . PRO   B 1 36  ? 27.537  60.939 46.11  1   17.99 ? 17  PRO   B O     1 
ATOM   2104 C CB    . PRO   B 1 36  ? 30.835  60.903 45.965 1   20.11 ? 17  PRO   B CB    1 
ATOM   2105 C CG    . PRO   B 1 36  ? 31.982  61.721 45.595 1   20.84 ? 17  PRO   B CG    1 
ATOM   2106 C CD    . PRO   B 1 36  ? 31.641  62.7   44.505 1   18.56 ? 17  PRO   B CD    1 
ATOM   2107 N N     . ARG   B 1 37  ? 28.522  62.911 46.637 1   19.85 ? 18  ARG   B N     1 
ATOM   2108 C CA    . ARG   B 1 37  ? 27.429  63.285 47.532 1   21.41 ? 18  ARG   B CA    1 
ATOM   2109 C C     . ARG   B 1 37  ? 26.154  63.518 46.731 1   20.21 ? 18  ARG   B C     1 
ATOM   2110 O O     . ARG   B 1 37  ? 25.059  63.171 47.191 1   21.11 ? 18  ARG   B O     1 
ATOM   2111 C CB    . ARG   B 1 37  ? 27.803  64.587 48.273 1   25.29 ? 18  ARG   B CB    1 
ATOM   2112 C CG    . ARG   B 1 37  ? 28.919  64.417 49.303 1   32.83 ? 18  ARG   B CG    1 
ATOM   2113 C CD    . ARG   B 1 37  ? 29.349  65.803 49.796 1   42.69 ? 18  ARG   B CD    1 
ATOM   2114 N NE    . ARG   B 1 37  ? 29.577  65.86  51.243 1   51.99 ? 18  ARG   B NE    1 
ATOM   2115 C CZ    . ARG   B 1 37  ? 30.025  66.938 51.888 1   57.97 ? 18  ARG   B CZ    1 
ATOM   2116 N NH1   . ARG   B 1 37  ? 30.22   66.9   53.2   1   58.22 ? 18  ARG   B NH1   1 
ATOM   2117 N NH2   . ARG   B 1 37  ? 30.294  68.058 51.222 1   59.29 ? 18  ARG   B NH2   1 
ATOM   2118 N N     . ASP   B 1 38  ? 26.258  64.12  45.537 1   18.94 ? 19  ASP   B N     1 
ATOM   2119 C CA    . ASP   B 1 38  ? 25.065  64.345 44.728 1   19.15 ? 19  ASP   B CA    1 
ATOM   2120 C C     . ASP   B 1 38  ? 24.507  63.033 44.214 1   18.49 ? 19  ASP   B C     1 
ATOM   2121 O O     . ASP   B 1 38  ? 23.3    62.837 44.191 1   19.42 ? 19  ASP   B O     1 
ATOM   2122 C CB    . ASP   B 1 38  ? 25.426  65.216 43.543 1   21.07 ? 19  ASP   B CB    1 
ATOM   2123 C CG    . ASP   B 1 38  ? 24.253  65.944 42.973 1   29.66 ? 19  ASP   B CG    1 
ATOM   2124 O OD1   . ASP   B 1 38  ? 23.254  66.198 43.741 1   31.51 ? 19  ASP   B OD1   1 
ATOM   2125 O OD2   . ASP   B 1 38  ? 24.315  66.294 41.787 1   31.09 ? 19  ASP   B OD2   1 
ATOM   2126 N N     . TYR   B 1 39  ? 25.396  62.077 43.845 1   16.82 ? 20  TYR   B N     1 
ATOM   2127 C CA    . TYR   B 1 39  ? 24.909  60.737 43.424 1   16.79 ? 20  TYR   B CA    1 
ATOM   2128 C C     . TYR   B 1 39  ? 24.098  60.092 44.541 1   17.21 ? 20  TYR   B C     1 
ATOM   2129 O O     . TYR   B 1 39  ? 23.033  59.547 44.283 1   17.21 ? 20  TYR   B O     1 
ATOM   2130 C CB    . TYR   B 1 39  ? 26.156  59.895 43.115 1   15.86 ? 20  TYR   B CB    1 
ATOM   2131 C CG    . TYR   B 1 39  ? 25.819  58.514 42.613 1   15.13 ? 20  TYR   B CG    1 
ATOM   2132 C CD1   . TYR   B 1 39  ? 25.265  58.321 41.341 1   14.22 ? 20  TYR   B CD1   1 
ATOM   2133 C CD2   . TYR   B 1 39  ? 26.058  57.391 43.398 1   15.36 ? 20  TYR   B CD2   1 
ATOM   2134 C CE1   . TYR   B 1 39  ? 25.001  57.034 40.842 1   14.84 ? 20  TYR   B CE1   1 
ATOM   2135 C CE2   . TYR   B 1 39  ? 25.85   56.104 42.893 1   13.82 ? 20  TYR   B CE2   1 
ATOM   2136 C CZ    . TYR   B 1 39  ? 25.314  55.93  41.62  1   14.54 ? 20  TYR   B CZ    1 
ATOM   2137 O OH    . TYR   B 1 39  ? 25.076  54.667 41.165 1   15.28 ? 20  TYR   B OH    1 
ATOM   2138 N N     . LEU   B 1 40  ? 24.623  60.145 45.788 1   17.98 ? 21  LEU   B N     1 
ATOM   2139 C CA    . LEU   B 1 40  ? 23.911  59.565 46.926 1   18.81 ? 21  LEU   B CA    1 
ATOM   2140 C C     . LEU   B 1 40  ? 22.572  60.254 47.177 1   19.57 ? 21  LEU   B C     1 
ATOM   2141 O O     . LEU   B 1 40  ? 21.559  59.586 47.368 1   21.57 ? 21  LEU   B O     1 
ATOM   2142 C CB    . LEU   B 1 40  ? 24.802  59.658 48.162 1   19.75 ? 21  LEU   B CB    1 
ATOM   2143 C CG    . LEU   B 1 40  ? 26.067  58.766 48.079 1   19.48 ? 21  LEU   B CG    1 
ATOM   2144 C CD1   . LEU   B 1 40  ? 26.973  58.994 49.287 1   22.75 ? 21  LEU   B CD1   1 
ATOM   2145 C CD2   . LEU   B 1 40  ? 25.683  57.287 47.882 1   22.2  ? 21  LEU   B CD2   1 
ATOM   2146 N N     . GLU   B 1 41  ? 22.583  61.58  47.091 1   19.46 ? 22  GLU   B N     1 
ATOM   2147 C CA    . GLU   B 1 41  ? 21.338  62.322 47.269 1   21.25 ? 22  GLU   B CA    1 
ATOM   2148 C C     . GLU   B 1 41  ? 20.291  61.977 46.22  1   22.07 ? 22  GLU   B C     1 
ATOM   2149 O O     . GLU   B 1 41  ? 19.085  61.892 46.539 1   24.29 ? 22  GLU   B O     1 
ATOM   2150 C CB    . GLU   B 1 41  ? 21.631  63.837 47.232 1   24.32 ? 22  GLU   B CB    1 
ATOM   2151 C CG    . GLU   B 1 41  ? 22.339  64.325 48.471 1   29.96 ? 22  GLU   B CG    1 
ATOM   2152 C CD    . GLU   B 1 41  ? 21.565  64.106 49.761 1   38.69 ? 22  GLU   B CD    1 
ATOM   2153 O OE1   . GLU   B 1 41  ? 22.173  63.626 50.747 1   39.86 ? 22  GLU   B OE1   1 
ATOM   2154 O OE2   . GLU   B 1 41  ? 20.347  64.399 49.774 1   42.39 ? 22  GLU   B OE2   1 
ATOM   2155 N N     . LYS   B 1 42  ? 20.707  61.826 44.949 1   20.58 ? 23  LYS   B N     1 
ATOM   2156 C CA    . LYS   B 1 42  ? 19.757  61.568 43.876 1   21.06 ? 23  LYS   B CA    1 
ATOM   2157 C C     . LYS   B 1 42  ? 19.178  60.163 43.868 1   20.98 ? 23  LYS   B C     1 
ATOM   2158 O O     . LYS   B 1 42  ? 18.003  59.961 43.523 1   23.26 ? 23  LYS   B O     1 
ATOM   2159 C CB    . LYS   B 1 42  ? 20.419  61.828 42.508 1   23.02 ? 23  LYS   B CB    1 
ATOM   2160 C CG    . LYS   B 1 42  ? 20.116  63.204 41.955 1   33.38 ? 23  LYS   B CG    1 
ATOM   2161 C CD    . LYS   B 1 42  ? 21.041  64.258 42.352 1   38.04 ? 23  LYS   B CD    1 
ATOM   2162 C CE    . LYS   B 1 42  ? 20.399  65.593 41.985 1   39.97 ? 23  LYS   B CE    1 
ATOM   2163 N NZ    . LYS   B 1 42  ? 20.619  66.6   43.049 1   40.5  ? 23  LYS   B NZ    1 
ATOM   2164 N N     . TYR   B 1 43  ? 20.029  59.17  44.17  1   19    ? 24  TYR   B N     1 
ATOM   2165 C CA    . TYR   B 1 43  ? 19.582  57.783 44.034 1   18.62 ? 24  TYR   B CA    1 
ATOM   2166 C C     . TYR   B 1 43  ? 19.403  56.991 45.301 1   19.27 ? 24  TYR   B C     1 
ATOM   2167 O O     . TYR   B 1 43  ? 18.73   55.96  45.241 1   20.27 ? 24  TYR   B O     1 
ATOM   2168 C CB    . TYR   B 1 43  ? 20.646  57.053 43.135 1   17.56 ? 24  TYR   B CB    1 
ATOM   2169 C CG    . TYR   B 1 43  ? 20.611  57.496 41.687 1   17.68 ? 24  TYR   B CG    1 
ATOM   2170 C CD1   . TYR   B 1 43  ? 19.657  56.984 40.8   1   17.79 ? 24  TYR   B CD1   1 
ATOM   2171 C CD2   . TYR   B 1 43  ? 21.52   58.436 41.198 1   17.36 ? 24  TYR   B CD2   1 
ATOM   2172 C CE1   . TYR   B 1 43  ? 19.608  57.378 39.466 1   17.86 ? 24  TYR   B CE1   1 
ATOM   2173 C CE2   . TYR   B 1 43  ? 21.48   58.839 39.867 1   17.41 ? 24  TYR   B CE2   1 
ATOM   2174 C CZ    . TYR   B 1 43  ? 20.508  58.334 39.004 1   17.86 ? 24  TYR   B CZ    1 
ATOM   2175 O OH    . TYR   B 1 43  ? 20.444  58.693 37.676 1   18.59 ? 24  TYR   B OH    1 
ATOM   2176 N N     . TYR   B 1 44  ? 19.986  57.435 46.434 1   18.64 ? 25  TYR   B N     1 
ATOM   2177 C CA    . TYR   B 1 44  ? 20.049  56.572 47.626 1   20.31 ? 25  TYR   B CA    1 
ATOM   2178 C C     . TYR   B 1 44  ? 19.545  57.196 48.925 1   23.52 ? 25  TYR   B C     1 
ATOM   2179 O O     . TYR   B 1 44  ? 19.807  56.673 50.003 1   23.56 ? 25  TYR   B O     1 
ATOM   2180 C CB    . TYR   B 1 44  ? 21.503  56.046 47.815 1   19.48 ? 25  TYR   B CB    1 
ATOM   2181 C CG    . TYR   B 1 44  ? 21.9    55.121 46.672 1   17.98 ? 25  TYR   B CG    1 
ATOM   2182 C CD1   . TYR   B 1 44  ? 21.387  53.844 46.583 1   18.09 ? 25  TYR   B CD1   1 
ATOM   2183 C CD2   . TYR   B 1 44  ? 22.702  55.568 45.63  1   16.64 ? 25  TYR   B CD2   1 
ATOM   2184 C CE1   . TYR   B 1 44  ? 21.616  53.037 45.474 1   18.59 ? 25  TYR   B CE1   1 
ATOM   2185 C CE2   . TYR   B 1 44  ? 22.975  54.747 44.533 1   16.68 ? 25  TYR   B CE2   1 
ATOM   2186 C CZ    . TYR   B 1 44  ? 22.417  53.487 44.451 1   16.62 ? 25  TYR   B CZ    1 
ATOM   2187 O OH    . TYR   B 1 44  ? 22.65   52.669 43.384 1   17.2  ? 25  TYR   B OH    1 
ATOM   2188 N N     . LYS   B 1 45  ? 18.777  58.279 48.822 1   24.44 ? 26  LYS   B N     1 
ATOM   2189 C CA    . LYS   B 1 45  ? 18.219  58.932 50.021 1   28.37 ? 26  LYS   B CA    1 
ATOM   2190 C C     . LYS   B 1 45  ? 17.183  58.023 50.683 1   30.28 ? 26  LYS   B C     1 
ATOM   2191 O O     . LYS   B 1 45  ? 17.057  58.051 51.918 1   31.88 ? 26  LYS   B O     1 
ATOM   2192 C CB    . LYS   B 1 45  ? 17.616  60.266 49.627 1   33.15 ? 26  LYS   B CB    1 
ATOM   2193 C CG    . LYS   B 1 45  ? 17.416  61.23  50.791 1   40.22 ? 26  LYS   B CG    1 
ATOM   2194 C CD    . LYS   B 1 45  ? 17.259  62.652 50.317 1   47.11 ? 26  LYS   B CD    1 
ATOM   2195 C CE    . LYS   B 1 45  ? 17.184  63.588 51.502 1   52.16 ? 26  LYS   B CE    1 
ATOM   2196 N NZ    . LYS   B 1 45  ? 17.559  64.979 51.13  1   55.83 ? 26  LYS   B NZ    1 
ATOM   2197 N N     . PHE   B 1 46  ? 16.439  57.243 49.897 1   30.53 ? 27  PHE   B N     1 
ATOM   2198 C CA    . PHE   B 1 46  ? 15.48   56.256 50.396 1   31.32 ? 27  PHE   B CA    1 
ATOM   2199 C C     . PHE   B 1 46  ? 14.446  56.882 51.332 1   33.52 ? 27  PHE   B C     1 
ATOM   2200 O O     . PHE   B 1 46  ? 14.192  56.367 52.417 1   34.42 ? 27  PHE   B O     1 
ATOM   2201 C CB    . PHE   B 1 46  ? 16.234  55.111 51.08  1   30.76 ? 27  PHE   B CB    1 
ATOM   2202 C CG    . PHE   B 1 46  ? 15.563  53.761 51.104 1   30.57 ? 27  PHE   B CG    1 
ATOM   2203 C CD1   . PHE   B 1 46  ? 15.096  53.185 49.937 1   31.53 ? 27  PHE   B CD1   1 
ATOM   2204 C CD2   . PHE   B 1 46  ? 15.472  53.041 52.28  1   30.98 ? 27  PHE   B CD2   1 
ATOM   2205 C CE1   . PHE   B 1 46  ? 14.548  51.919 49.942 1   32.42 ? 27  PHE   B CE1   1 
ATOM   2206 C CE2   . PHE   B 1 46  ? 14.914  51.77  52.29  1   32.33 ? 27  PHE   B CE2   1 
ATOM   2207 C CZ    . PHE   B 1 46  ? 14.448  51.217 51.122 1   32.79 ? 27  PHE   B CZ    1 
ATOM   2208 N N     . GLY   B 1 47  ? 13.897  58.008 50.912 1   34.19 ? 28  GLY   B N     1 
ATOM   2209 C CA    . GLY   B 1 47  ? 12.865  58.707 51.677 1   35.42 ? 28  GLY   B CA    1 
ATOM   2210 C C     . GLY   B 1 47  ? 11.521  58.003 51.626 1   37.57 ? 28  GLY   B C     1 
ATOM   2211 O O     . GLY   B 1 47  ? 11.369  56.936 51.014 1   36.97 ? 28  GLY   B O     1 
ATOM   2212 N N     . HIS   B 1 50  ? 7.614   56.975 47.613 1   42.08 ? 31  HIS   B N     1 
ATOM   2213 C CA    . HIS   B 1 50  ? 7.437   55.849 46.687 1   41.46 ? 31  HIS   B CA    1 
ATOM   2214 C C     . HIS   B 1 50  ? 8.036   56.137 45.283 1   40.38 ? 31  HIS   B C     1 
ATOM   2215 O O     . HIS   B 1 50  ? 7.377   55.902 44.26  1   42.6  ? 31  HIS   B O     1 
ATOM   2216 C CB    . HIS   B 1 50  ? 5.947   55.5   46.565 1   43.27 ? 31  HIS   B CB    1 
ATOM   2217 C CG    . HIS   B 1 50  ? 5.206   55.438 47.879 1   47.15 ? 31  HIS   B CG    1 
ATOM   2218 N ND1   . HIS   B 1 50  ? 4.168   56.324 48.17  1   49.68 ? 31  HIS   B ND1   1 
ATOM   2219 C CD2   . HIS   B 1 50  ? 5.388   54.617 48.943 1   48.28 ? 31  HIS   B CD2   1 
ATOM   2220 C CE1   . HIS   B 1 50  ? 3.736   55.987 49.38  1   49.83 ? 31  HIS   B CE1   1 
ATOM   2221 N NE2   . HIS   B 1 50  ? 4.443   54.975 49.89  1   49.51 ? 31  HIS   B NE2   1 
ATOM   2222 N N     . SER   B 1 51  ? 9.305   56.559 45.226 1   36.27 ? 32  SER   B N     1 
ATOM   2223 C CA    . SER   B 1 51  ? 9.93    56.916 43.947 1   32.5  ? 32  SER   B CA    1 
ATOM   2224 C C     . SER   B 1 51  ? 10.416  55.696 43.19  1   29.28 ? 32  SER   B C     1 
ATOM   2225 O O     . SER   B 1 51  ? 10.688  54.67  43.794 1   26.93 ? 32  SER   B O     1 
ATOM   2226 C CB    . SER   B 1 51  ? 11.119  57.84  44.177 1   32.57 ? 32  SER   B CB    1 
ATOM   2227 O OG    . SER   B 1 51  ? 12.144  57.107 44.832 1   31.93 ? 32  SER   B OG    1 
ATOM   2228 N N     . ALA   B 1 52  ? 10.64   55.827 41.859 1   27.59 ? 33  ALA   B N     1 
ATOM   2229 C CA    . ALA   B 1 52  ? 11.194  54.72  41.075 1   25.62 ? 33  ALA   B CA    1 
ATOM   2230 C C     . ALA   B 1 52  ? 12.581  54.349 41.616 1   23.47 ? 33  ALA   B C     1 
ATOM   2231 O O     . ALA   B 1 52  ? 12.893  53.183 41.709 1   23.65 ? 33  ALA   B O     1 
ATOM   2232 C CB    . ALA   B 1 52  ? 11.3    55.12  39.617 1   26.44 ? 33  ALA   B CB    1 
ATOM   2233 N N     . GLU   B 1 53  ? 13.389  55.366 42     1   23.09 ? 34  GLU   B N     1 
ATOM   2234 C CA    . GLU   B 1 53  ? 14.746  55.096 42.556 1   22.55 ? 34  GLU   B CA    1 
ATOM   2235 C C     . GLU   B 1 53  ? 14.685  54.273 43.819 1   23.21 ? 34  GLU   B C     1 
ATOM   2236 O O     . GLU   B 1 53  ? 15.469  53.345 43.971 1   23.23 ? 34  GLU   B O     1 
ATOM   2237 C CB    . GLU   B 1 53  ? 15.435  56.422 42.88  1   23.26 ? 34  GLU   B CB    1 
ATOM   2238 C CG    . GLU   B 1 53  ? 15.91   57.157 41.631 1   24.67 ? 34  GLU   B CG    1 
ATOM   2239 C CD    . GLU   B 1 53  ? 14.812  57.463 40.626 1   26.86 ? 34  GLU   B CD    1 
ATOM   2240 O OE1   . GLU   B 1 53  ? 13.796  58.091 41.032 1   27.51 ? 34  GLU   B OE1   1 
ATOM   2241 O OE2   . GLU   B 1 53  ? 14.95   57.08  39.439 1   25.21 ? 34  GLU   B OE2   1 
ATOM   2242 N N     . SER   B 1 54  ? 13.724  54.566 44.724 1   24.28 ? 35  SER   B N     1 
ATOM   2243 C CA    . SER   B 1 54  ? 13.616  53.765 45.946 1   24.75 ? 35  SER   B CA    1 
ATOM   2244 C C     . SER   B 1 54  ? 13.058  52.387 45.665 1   24.88 ? 35  SER   B C     1 
ATOM   2245 O O     . SER   B 1 54  ? 13.468  51.439 46.307 1   24.86 ? 35  SER   B O     1 
ATOM   2246 C CB    . SER   B 1 54  ? 12.782  54.484 46.995 1   26.45 ? 35  SER   B CB    1 
ATOM   2247 O OG    . SER   B 1 54  ? 13.499  55.655 47.363 1   33.39 ? 35  SER   B OG    1 
ATOM   2248 N N     . GLN   B 1 55  ? 12.152  52.249 44.686 1   24.36 ? 36  GLN   B N     1 
ATOM   2249 C CA    . GLN   B 1 55  ? 11.629  50.926 44.336 1   24.38 ? 36  GLN   B CA    1 
ATOM   2250 C C     . GLN   B 1 55  ? 12.755  50.051 43.785 1   23.58 ? 36  GLN   B C     1 
ATOM   2251 O O     . GLN   B 1 55  ? 12.825  48.869 44.1   1   24.25 ? 36  GLN   B O     1 
ATOM   2252 C CB    . GLN   B 1 55  ? 10.498  51.033 43.297 1   27.34 ? 36  GLN   B CB    1 
ATOM   2253 C CG    . GLN   B 1 55  ? 9.226   51.704 43.874 1   33.06 ? 36  GLN   B CG    1 
ATOM   2254 C CD    . GLN   B 1 55  ? 8.685   50.897 45.023 1   40.92 ? 36  GLN   B CD    1 
ATOM   2255 O OE1   . GLN   B 1 55  ? 8.82    51.279 46.189 1   44.82 ? 36  GLN   B OE1   1 
ATOM   2256 N NE2   . GLN   B 1 55  ? 8.127   49.734 44.717 1   43.33 ? 36  GLN   B NE2   1 
ATOM   2257 N N     . ILE   B 1 56  ? 13.625  50.631 42.945 1   23.31 ? 37  ILE   B N     1 
ATOM   2258 C CA    . ILE   B 1 56  ? 14.755  49.86  42.405 1   22.48 ? 37  ILE   B CA    1 
ATOM   2259 C C     . ILE   B 1 56  ? 15.722  49.503 43.514 1   21.71 ? 37  ILE   B C     1 
ATOM   2260 O O     . ILE   B 1 56  ? 16.148  48.369 43.558 1   21.99 ? 37  ILE   B O     1 
ATOM   2261 C CB    . ILE   B 1 56  ? 15.422  50.641 41.29  1   23.8  ? 37  ILE   B CB    1 
ATOM   2262 C CG1   . ILE   B 1 56  ? 14.522  50.591 40.081 1   24.68 ? 37  ILE   B CG1   1 
ATOM   2263 C CG2   . ILE   B 1 56  ? 16.818  50.06  40.958 1   24.01 ? 37  ILE   B CG2   1 
ATOM   2264 C CD1   . ILE   B 1 56  ? 14.868  51.625 39.066 1   25.77 ? 37  ILE   B CD1   1 
ATOM   2265 N N     . LEU   B 1 57  ? 15.988  50.452 44.42  1   21.12 ? 38  LEU   B N     1 
ATOM   2266 C CA    . LEU   B 1 57  ? 16.869  50.14  45.572 1   20.59 ? 38  LEU   B CA    1 
ATOM   2267 C C     . LEU   B 1 57  ? 16.312  48.944 46.405 1   21.07 ? 38  LEU   B C     1 
ATOM   2268 O O     . LEU   B 1 57  ? 17.035  47.999 46.696 1   21.37 ? 38  LEU   B O     1 
ATOM   2269 C CB    . LEU   B 1 57  ? 17.095  51.369 46.414 1   20.63 ? 38  LEU   B CB    1 
ATOM   2270 C CG    . LEU   B 1 57  ? 17.953  51.178 47.678 1   22.29 ? 38  LEU   B CG    1 
ATOM   2271 C CD1   . LEU   B 1 57  ? 19.331  50.485 47.371 1   20.94 ? 38  LEU   B CD1   1 
ATOM   2272 C CD2   . LEU   B 1 57  ? 18.22   52.491 48.317 1   24.46 ? 38  LEU   B CD2   1 
ATOM   2273 N N     . LYS   B 1 58  ? 14.991  48.936 46.672 1   22.67 ? 39  LYS   B N     1 
ATOM   2274 C CA    . LYS   B 1 58  ? 14.393  47.802 47.393 1   22.6  ? 39  LYS   B CA    1 
ATOM   2275 C C     . LYS   B 1 58  ? 14.565  46.516 46.638 1   22.35 ? 39  LYS   B C     1 
ATOM   2276 O O     . LYS   B 1 58  ? 14.902  45.498 47.231 1   21.55 ? 39  LYS   B O     1 
ATOM   2277 C CB    . LYS   B 1 58  ? 12.902  48.075 47.642 1   24.76 ? 39  LYS   B CB    1 
ATOM   2278 C CG    . LYS   B 1 58  ? 12.683  49.19  48.632 1   29.88 ? 39  LYS   B CG    1 
ATOM   2279 C CD    . LYS   B 1 58  ? 11.156  49.443 48.783 1   34.4  ? 39  LYS   B CD    1 
ATOM   2280 C CE    . LYS   B 1 58  ? 10.894  50.868 49.177 1   40.76 ? 39  LYS   B CE    1 
ATOM   2281 N NZ    . LYS   B 1 58  ? 9.426   51.168 49.221 1   45.01 ? 39  LYS   B NZ    1 
ATOM   2282 N N     . HIS   B 1 59  ? 14.352  46.533 45.29  1   22.56 ? 40  HIS   B N     1 
ATOM   2283 C CA    . HIS   B 1 59  ? 14.554  45.318 44.524 1   24.36 ? 40  HIS   B CA    1 
ATOM   2284 C C     . HIS   B 1 59  ? 15.986  44.813 44.561 1   23.6  ? 40  HIS   B C     1 
ATOM   2285 O O     . HIS   B 1 59  ? 16.208  43.629 44.748 1   24.72 ? 40  HIS   B O     1 
ATOM   2286 C CB    . HIS   B 1 59  ? 14.058  45.384 43.097 1   28.98 ? 40  HIS   B CB    1 
ATOM   2287 C CG    . HIS   B 1 59  ? 13.846  43.981 42.601 1   38.95 ? 40  HIS   B CG    1 
ATOM   2288 N ND1   . HIS   B 1 59  ? 12.68   43.291 42.863 1   43.55 ? 40  HIS   B ND1   1 
ATOM   2289 C CD2   . HIS   B 1 59  ? 14.725  43.129 42.026 1   41.52 ? 40  HIS   B CD2   1 
ATOM   2290 C CE1   . HIS   B 1 59  ? 12.86   42.064 42.401 1   44.67 ? 40  HIS   B CE1   1 
ATOM   2291 N NE2   . HIS   B 1 59  ? 14.067  41.921 41.87  1   43.78 ? 40  HIS   B NE2   1 
ATOM   2292 N N     . LEU   B 1 60  ? 16.97   45.727 44.412 1   21.88 ? 41  LEU   B N     1 
ATOM   2293 C CA    . LEU   B 1 60  ? 18.372  45.33  44.491 1   20.84 ? 41  LEU   B CA    1 
ATOM   2294 C C     . LEU   B 1 60  ? 18.672  44.699 45.867 1   18.66 ? 41  LEU   B C     1 
ATOM   2295 O O     . LEU   B 1 60  ? 19.292  43.644 45.906 1   19.78 ? 41  LEU   B O     1 
ATOM   2296 C CB    . LEU   B 1 60  ? 19.279  46.565 44.301 1   21.38 ? 41  LEU   B CB    1 
ATOM   2297 C CG    . LEU   B 1 60  ? 19.184  47.178 42.923 1   24.54 ? 41  LEU   B CG    1 
ATOM   2298 C CD1   . LEU   B 1 60  ? 19.992  48.486 42.847 1   24.01 ? 41  LEU   B CD1   1 
ATOM   2299 C CD2   . LEU   B 1 60  ? 19.764  46.222 41.888 1   29.14 ? 41  LEU   B CD2   1 
ATOM   2300 N N     . LEU   B 1 61  ? 18.164  45.329 46.957 1   19.45 ? 42  LEU   B N     1 
ATOM   2301 C CA    . LEU   B 1 61  ? 18.413  44.79  48.285 1   19.44 ? 42  LEU   B CA    1 
ATOM   2302 C C     . LEU   B 1 61  ? 17.792  43.405 48.476 1   19.61 ? 42  LEU   B C     1 
ATOM   2303 O O     . LEU   B 1 61  ? 18.41   42.529 49.044 1   19.2  ? 42  LEU   B O     1 
ATOM   2304 C CB    . LEU   B 1 61  ? 17.93   45.741 49.352 1   19.5  ? 42  LEU   B CB    1 
ATOM   2305 C CG    . LEU   B 1 61  ? 18.708  47.084 49.393 1   20.35 ? 42  LEU   B CG    1 
ATOM   2306 C CD1   . LEU   B 1 61  ? 17.991  48.104 50.282 1   22.92 ? 42  LEU   B CD1   1 
ATOM   2307 C CD2   . LEU   B 1 61  ? 20.131  46.826 49.871 1   19.99 ? 42  LEU   B CD2   1 
ATOM   2308 N N     . LYS   B 1 62  ? 16.574  43.207 47.957 1   20.08 ? 43  LYS   B N     1 
ATOM   2309 C CA    . LYS   B 1 62  ? 15.955  41.867 48.081 1   20.82 ? 43  LYS   B CA    1 
ATOM   2310 C C     . LYS   B 1 62  ? 16.713  40.808 47.31  1   21.34 ? 43  LYS   B C     1 
ATOM   2311 O O     . LYS   B 1 62  ? 16.91   39.711 47.797 1   22.29 ? 43  LYS   B O     1 
ATOM   2312 C CB    . LYS   B 1 62  ? 14.502  41.887 47.646 1   22.6  ? 43  LYS   B CB    1 
ATOM   2313 C CG    . LYS   B 1 62  ? 13.669  42.713 48.556 1   24.35 ? 43  LYS   B CG    1 
ATOM   2314 C CD    . LYS   B 1 62  ? 12.249  42.7   48.018 1   29.15 ? 43  LYS   B CD    1 
ATOM   2315 C CE    . LYS   B 1 62  ? 11.698  44.065 47.792 1   35.58 ? 43  LYS   B CE    1 
ATOM   2316 N NZ    . LYS   B 1 62  ? 10.284  44.009 47.35  1   37.2  ? 43  LYS   B NZ    1 
ATOM   2317 N N     . ASN   B 1 63  ? 17.204  41.173 46.094 1   21.66 ? 44  ASN   B N     1 
ATOM   2318 C CA    . ASN   B 1 63  ? 17.996  40.208 45.337 1   22.35 ? 44  ASN   B CA    1 
ATOM   2319 C C     . ASN   B 1 63  ? 19.325  39.898 45.973 1   20.81 ? 44  ASN   B C     1 
ATOM   2320 O O     . ASN   B 1 63  ? 19.757  38.768 45.971 1   21.85 ? 44  ASN   B O     1 
ATOM   2321 C CB    . ASN   B 1 63  ? 18.212  40.686 43.916 1   27.06 ? 44  ASN   B CB    1 
ATOM   2322 C CG    . ASN   B 1 63  ? 17.1    40.309 43     1   35.71 ? 44  ASN   B CG    1 
ATOM   2323 O OD1   . ASN   B 1 63  ? 16.111  39.657 43.383 1   38.17 ? 44  ASN   B OD1   1 
ATOM   2324 N ND2   . ASN   B 1 63  ? 17.232  40.681 41.743 1   37.53 ? 44  ASN   B ND2   1 
ATOM   2325 N N     . LEU   B 1 64  ? 19.999  40.925 46.536 1   19.67 ? 45  LEU   B N     1 
ATOM   2326 C CA    . LEU   B 1 64  ? 21.259  40.699 47.224 1   19.4  ? 45  LEU   B CA    1 
ATOM   2327 C C     . LEU   B 1 64  ? 21.053  39.797 48.442 1   19.41 ? 45  LEU   B C     1 
ATOM   2328 O O     . LEU   B 1 64  ? 21.866  38.938 48.698 1   21.31 ? 45  LEU   B O     1 
ATOM   2329 C CB    . LEU   B 1 64  ? 21.924  42.017 47.627 1   19.54 ? 45  LEU   B CB    1 
ATOM   2330 C CG    . LEU   B 1 64  ? 22.371  42.843 46.428 1   20.04 ? 45  LEU   B CG    1 
ATOM   2331 C CD1   . LEU   B 1 64  ? 22.478  44.325 46.821 1   21.2  ? 45  LEU   B CD1   1 
ATOM   2332 C CD2   . LEU   B 1 64  ? 23.73   42.333 45.901 1   20.8  ? 45  LEU   B CD2   1 
ATOM   2333 N N     . PHE   B 1 65  ? 19.926  40.001 49.17  1   20.67 ? 46  PHE   B N     1 
ATOM   2334 C CA    . PHE   B 1 65  ? 19.635  39.149 50.33  1   23.59 ? 46  PHE   B CA    1 
ATOM   2335 C C     . PHE   B 1 65  ? 19.383  37.713 49.827 1   22.34 ? 46  PHE   B C     1 
ATOM   2336 O O     . PHE   B 1 65  ? 19.965  36.801 50.363 1   23.1  ? 46  PHE   B O     1 
ATOM   2337 C CB    . PHE   B 1 65  ? 18.43   39.716 51.055 1   25.87 ? 46  PHE   B CB    1 
ATOM   2338 C CG    . PHE   B 1 65  ? 17.911  38.8   52.127 1   30.03 ? 46  PHE   B CG    1 
ATOM   2339 C CD1   . PHE   B 1 65  ? 18.715  38.423 53.184 1   32.79 ? 46  PHE   B CD1   1 
ATOM   2340 C CD2   . PHE   B 1 65  ? 16.669  38.231 52.015 1   32.88 ? 46  PHE   B CD2   1 
ATOM   2341 C CE1   . PHE   B 1 65  ? 18.244  37.536 54.154 1   34.89 ? 46  PHE   B CE1   1 
ATOM   2342 C CE2   . PHE   B 1 65  ? 16.208  37.361 52.977 1   34.88 ? 46  PHE   B CE2   1 
ATOM   2343 C CZ    . PHE   B 1 65  ? 17.017  36.987 54.014 1   34.76 ? 46  PHE   B CZ    1 
ATOM   2344 N N     . LYS   B 1 66  ? 18.658  37.555 48.689 1   20.83 ? 47  LYS   B N     1 
ATOM   2345 C CA    . LYS   B 1 66  ? 18.434  36.193 48.115 1   23.02 ? 47  LYS   B CA    1 
ATOM   2346 C C     . LYS   B 1 66  ? 19.728  35.478 47.72  1   23.35 ? 47  LYS   B C     1 
ATOM   2347 O O     . LYS   B 1 66  ? 19.863  34.255 47.864 1   24.88 ? 47  LYS   B O     1 
ATOM   2348 C CB    . LYS   B 1 66  ? 17.526  36.252 46.889 1   24.26 ? 47  LYS   B CB    1 
ATOM   2349 C CG    . LYS   B 1 66  ? 16.889  34.914 46.555 1   30.35 ? 47  LYS   B CG    1 
ATOM   2350 C CD    . LYS   B 1 66  ? 15.813  35.074 45.508 1   34.03 ? 47  LYS   B CD    1 
ATOM   2351 C CE    . LYS   B 1 66  ? 16.381  34.933 44.115 1   39.47 ? 47  LYS   B CE    1 
ATOM   2352 N NZ    . LYS   B 1 66  ? 15.326  35.204 43.075 1   41.61 ? 47  LYS   B NZ    1 
ATOM   2353 N N     . ILE   B 1 67  ? 20.685  36.238 47.176 1   22.14 ? 48  ILE   B N     1 
ATOM   2354 C CA    . ILE   B 1 67  ? 21.95   35.629 46.756 1   21.68 ? 48  ILE   B CA    1 
ATOM   2355 C C     . ILE   B 1 67  ? 22.887  35.321 47.929 1   23.13 ? 48  ILE   B C     1 
ATOM   2356 O O     . ILE   B 1 67  ? 23.565  34.28  47.952 1   25.03 ? 48  ILE   B O     1 
ATOM   2357 C CB    . ILE   B 1 67  ? 22.599  36.625 45.762 1   21.7  ? 48  ILE   B CB    1 
ATOM   2358 C CG1   . ILE   B 1 67  ? 21.789  36.752 44.497 1   21.25 ? 48  ILE   B CG1   1 
ATOM   2359 C CG2   . ILE   B 1 67  ? 24.052  36.289 45.465 1   21.96 ? 48  ILE   B CG2   1 
ATOM   2360 C CD1   . ILE   B 1 67  ? 22.174  37.956 43.65  1   21.49 ? 48  ILE   B CD1   1 
ATOM   2361 N N     . PHE   B 1 68  ? 22.971  36.248 48.904 1   22.92 ? 49  PHE   B N     1 
ATOM   2362 C CA    . PHE   B 1 68  ? 23.976  36.111 49.984 1   25.02 ? 49  PHE   B CA    1 
ATOM   2363 C C     . PHE   B 1 68  ? 23.495  35.508 51.278 1   29.9  ? 49  PHE   B C     1 
ATOM   2364 O O     . PHE   B 1 68  ? 24.271  34.819 51.947 1   31.27 ? 49  PHE   B O     1 
ATOM   2365 C CB    . PHE   B 1 68  ? 24.648  37.45  50.315 1   23.9  ? 49  PHE   B CB    1 
ATOM   2366 C CG    . PHE   B 1 68  ? 25.464  37.954 49.164 1   21.95 ? 49  PHE   B CG    1 
ATOM   2367 C CD1   . PHE   B 1 68  ? 26.577  37.275 48.744 1   20.89 ? 49  PHE   B CD1   1 
ATOM   2368 C CD2   . PHE   B 1 68  ? 25.15   39.149 48.54  1   22.01 ? 49  PHE   B CD2   1 
ATOM   2369 C CE1   . PHE   B 1 68  ? 27.313  37.72  47.67  1   20.14 ? 49  PHE   B CE1   1 
ATOM   2370 C CE2   . PHE   B 1 68  ? 25.899  39.607 47.483 1   22.73 ? 49  PHE   B CE2   1 
ATOM   2371 C CZ    . PHE   B 1 68  ? 26.971  38.881 47.029 1   20.22 ? 49  PHE   B CZ    1 
ATOM   2372 N N     . CYS   B 1 69  ? 22.285  35.852 51.687 1   33.58 ? 50  CYS   B N     1 
ATOM   2373 C CA    . CYS   B 1 69  ? 21.823  35.373 52.973 1   36.53 ? 50  CYS   B CA    1 
ATOM   2374 C C     . CYS   B 1 69  ? 20.928  34.18  52.768 1   41.04 ? 50  CYS   B C     1 
ATOM   2375 O O     . CYS   B 1 69  ? 21.31   33.089 53.211 1   43.64 ? 50  CYS   B O     1 
ATOM   2376 C CB    . CYS   B 1 69  ? 21.225  36.494 53.817 1   36.58 ? 50  CYS   B CB    1 
ATOM   2377 S SG    . CYS   B 1 69  ? 22.387  37.867 54.176 1   37.03 ? 50  CYS   B SG    1 
ATOM   2378 N N     . LEU   B 1 70  ? 19.892  34.291 51.92  1   42.41 ? 51  LEU   B N     1 
ATOM   2379 C CA    . LEU   B 1 70  ? 19.084  33.123 51.567 1   44.19 ? 51  LEU   B CA    1 
ATOM   2380 C C     . LEU   B 1 70  ? 19.949  32.017 50.897 1   46.79 ? 51  LEU   B C     1 
ATOM   2381 O O     . LEU   B 1 70  ? 21.197  32.111 50.865 1   48.33 ? 51  LEU   B O     1 
ATOM   2382 C CB    . LEU   B 1 70  ? 17.946  33.493 50.623 1   44.81 ? 51  LEU   B CB    1 
ATOM   2383 C CG    . LEU   B 1 70  ? 16.818  34.363 51.164 1   47.1  ? 51  LEU   B CG    1 
ATOM   2384 C CD1   . LEU   B 1 70  ? 15.733  34.538 50.131 1   48.37 ? 51  LEU   B CD1   1 
ATOM   2385 C CD2   . LEU   B 1 70  ? 16.233  33.806 52.45  1   48.5  ? 51  LEU   B CD2   1 
ATOM   2386 N N     . GLY   B 1 72  ? 23.648  30.618 50.411 1   37.19 ? 53  GLY   B N     1 
ATOM   2387 C CA    . GLY   B 1 72  ? 23.971  30.829 49.011 1   36.02 ? 53  GLY   B CA    1 
ATOM   2388 C C     . GLY   B 1 72  ? 25.442  31.12  48.813 1   34.87 ? 53  GLY   B C     1 
ATOM   2389 O O     . GLY   B 1 72  ? 26.3    30.338 49.232 1   35.97 ? 53  GLY   B O     1 
ATOM   2390 N N     . VAL   B 1 73  ? 25.75   32.282 48.247 1   30.96 ? 54  VAL   B N     1 
ATOM   2391 C CA    . VAL   B 1 73  ? 27.148  32.672 48.008 1   29.14 ? 54  VAL   B CA    1 
ATOM   2392 C C     . VAL   B 1 73  ? 27.805  33.154 49.299 1   28.35 ? 54  VAL   B C     1 
ATOM   2393 O O     . VAL   B 1 73  ? 27.285  34.043 49.987 1   28.29 ? 54  VAL   B O     1 
ATOM   2394 C CB    . VAL   B 1 73  ? 27.229  33.737 46.892 1   28.52 ? 54  VAL   B CB    1 
ATOM   2395 C CG1   . VAL   B 1 73  ? 28.68   34.046 46.543 1   28.84 ? 54  VAL   B CG1   1 
ATOM   2396 C CG2   . VAL   B 1 73  ? 26.462  33.301 45.65  1   28.92 ? 54  VAL   B CG2   1 
ATOM   2397 N N     . LYS   B 1 74  ? 28.934  32.549 49.642 1   27.64 ? 55  LYS   B N     1 
ATOM   2398 C CA    . LYS   B 1 74  ? 29.664  32.853 50.874 1   28.44 ? 55  LYS   B CA    1 
ATOM   2399 C C     . LYS   B 1 74  ? 31.174  32.588 50.679 1   27.67 ? 55  LYS   B C     1 
ATOM   2400 O O     . LYS   B 1 74  ? 31.589  32.015 49.643 1   29.46 ? 55  LYS   B O     1 
ATOM   2401 C CB    . LYS   B 1 74  ? 29.125  31.934 51.976 1   32.41 ? 55  LYS   B CB    1 
ATOM   2402 C CG    . LYS   B 1 74  ? 29.392  30.462 51.648 1   37.02 ? 55  LYS   B CG    1 
ATOM   2403 C CD    . LYS   B 1 74  ? 28.647  29.496 52.541 1   44.61 ? 55  LYS   B CD    1 
ATOM   2404 C CE    . LYS   B 1 74  ? 28.246  28.278 51.72  1   50.47 ? 55  LYS   B CE    1 
ATOM   2405 N NZ    . LYS   B 1 74  ? 27.144  27.489 52.347 1   53.97 ? 55  LYS   B NZ    1 
ATOM   2406 N N     . GLY   B 1 75  ? 31.966  33.006 51.658 1   25.4  ? 56  GLY   B N     1 
ATOM   2407 C CA    . GLY   B 1 75  ? 33.383  32.744 51.587 1   24.89 ? 56  GLY   B CA    1 
ATOM   2408 C C     . GLY   B 1 75  ? 34.249  33.644 52.404 1   24.81 ? 56  GLY   B C     1 
ATOM   2409 O O     . GLY   B 1 75  ? 33.766  34.37  53.282 1   26.39 ? 56  GLY   B O     1 
ATOM   2410 N N     . ASP   B 1 76  ? 35.518  33.565 52.149 1   22.84 ? 57  ASP   B N     1 
ATOM   2411 C CA    . ASP   B 1 76  ? 36.49   34.33  52.883 1   23.87 ? 57  ASP   B CA    1 
ATOM   2412 C C     . ASP   B 1 76  ? 36.619  35.723 52.292 1   21.88 ? 57  ASP   B C     1 
ATOM   2413 O O     . ASP   B 1 76  ? 36.927  36.656 53.047 1   25.05 ? 57  ASP   B O     1 
ATOM   2414 C CB    . ASP   B 1 76  ? 37.868  33.66  52.814 1   28.24 ? 57  ASP   B CB    1 
ATOM   2415 C CG    . ASP   B 1 76  ? 38.002  32.416 53.666 1   37.14 ? 57  ASP   B CG    1 
ATOM   2416 O OD1   . ASP   B 1 76  ? 37.11   32.188 54.539 1   36.73 ? 57  ASP   B OD1   1 
ATOM   2417 O OD2   . ASP   B 1 76  ? 38.985  31.668 53.458 1   42.29 ? 57  ASP   B OD2   1 
ATOM   2418 N N     . LEU   B 1 77  ? 36.462  35.867 50.939 1   18.26 ? 58  LEU   B N     1 
ATOM   2419 C CA    . LEU   B 1 77  ? 36.713  37.168 50.352 1   17.37 ? 58  LEU   B CA    1 
ATOM   2420 C C     . LEU   B 1 77  ? 35.74   37.474 49.213 1   15.55 ? 58  LEU   B C     1 
ATOM   2421 O O     . LEU   B 1 77  ? 35.575  36.706 48.255 1   15.95 ? 58  LEU   B O     1 
ATOM   2422 C CB    . LEU   B 1 77  ? 38.159  37.157 49.78  1   17.9  ? 58  LEU   B CB    1 
ATOM   2423 C CG    . LEU   B 1 77  ? 38.546  38.419 48.989 1   19.82 ? 58  LEU   B CG    1 
ATOM   2424 C CD1   . LEU   B 1 77  ? 38.59   39.652 49.889 1   22.09 ? 58  LEU   B CD1   1 
ATOM   2425 C CD2   . LEU   B 1 77  ? 39.957  38.311 48.383 1   20.75 ? 58  LEU   B CD2   1 
ATOM   2426 N N     . LEU   B 1 78  ? 35.165  38.665 49.276 1   14.83 ? 59  LEU   B N     1 
ATOM   2427 C CA    . LEU   B 1 78  ? 34.316  39.234 48.207 1   14.69 ? 59  LEU   B CA    1 
ATOM   2428 C C     . LEU   B 1 78  ? 34.999  40.532 47.777 1   14.92 ? 59  LEU   B C     1 
ATOM   2429 O O     . LEU   B 1 78  ? 35.408  41.313 48.64  1   15.5  ? 59  LEU   B O     1 
ATOM   2430 C CB    . LEU   B 1 78  ? 32.911  39.523 48.723 1   16.53 ? 59  LEU   B CB    1 
ATOM   2431 C CG    . LEU   B 1 78  ? 31.972  40.2   47.657 1   16.48 ? 59  LEU   B CG    1 
ATOM   2432 C CD1   . LEU   B 1 78  ? 30.524  39.69  47.817 1   19.12 ? 59  LEU   B CD1   1 
ATOM   2433 C CD2   . LEU   B 1 78  ? 31.988  41.703 47.78  1   17.2  ? 59  LEU   B CD2   1 
ATOM   2434 N N     . ILE   B 1 79  ? 35.104  40.761 46.481 1   14.29 ? 60  ILE   B N     1 
ATOM   2435 C CA    . ILE   B 1 79  ? 35.596  42.036 45.941 1   14.89 ? 60  ILE   B CA    1 
ATOM   2436 C C     . ILE   B 1 79  ? 34.429  42.709 45.255 1   15.79 ? 60  ILE   B C     1 
ATOM   2437 O O     . ILE   B 1 79  ? 33.804  42.109 44.373 1   15.11 ? 60  ILE   B O     1 
ATOM   2438 C CB    . ILE   B 1 79  ? 36.734  41.819 44.908 1   14.95 ? 60  ILE   B CB    1 
ATOM   2439 C CG1   . ILE   B 1 79  ? 37.959  41.148 45.58  1   17.86 ? 60  ILE   B CG1   1 
ATOM   2440 C CG2   . ILE   B 1 79  ? 37.156  43.226 44.385 1   16.23 ? 60  ILE   B CG2   1 
ATOM   2441 C CD1   . ILE   B 1 79  ? 39.031  40.7   44.542 1   18.96 ? 60  ILE   B CD1   1 
ATOM   2442 N N     . ASP   B 1 80  ? 34.111  43.952 45.646 1   14.42 ? 61  ASP   B N     1 
ATOM   2443 C CA    . ASP   B 1 80  ? 33.041  44.753 45.037 1   13.57 ? 61  ASP   B CA    1 
ATOM   2444 C C     . ASP   B 1 80  ? 33.715  45.695 44.066 1   14.69 ? 61  ASP   B C     1 
ATOM   2445 O O     . ASP   B 1 80  ? 34.663  46.44  44.437 1   15.92 ? 61  ASP   B O     1 
ATOM   2446 C CB    . ASP   B 1 80  ? 32.31   45.546 46.125 1   15.93 ? 61  ASP   B CB    1 
ATOM   2447 C CG    . ASP   B 1 80  ? 31.144  46.335 45.526 1   18.98 ? 61  ASP   B CG    1 
ATOM   2448 O OD1   . ASP   B 1 80  ? 30.478  45.814 44.59  1   18.34 ? 61  ASP   B OD1   1 
ATOM   2449 O OD2   . ASP   B 1 80  ? 30.907  47.463 45.969 1   18.67 ? 61  ASP   B OD2   1 
ATOM   2450 N N     . ILE   B 1 81  ? 33.314  45.652 42.81  1   13.62 ? 62  ILE   B N     1 
ATOM   2451 C CA    . ILE   B 1 81  ? 33.938  46.373 41.691 1   15.23 ? 62  ILE   B CA    1 
ATOM   2452 C C     . ILE   B 1 81  ? 33.088  47.555 41.3   1   14.33 ? 62  ILE   B C     1 
ATOM   2453 O O     . ILE   B 1 81  ? 31.893  47.405 41.017 1   15.46 ? 62  ILE   B O     1 
ATOM   2454 C CB    . ILE   B 1 81  ? 34.076  45.395 40.508 1   15.93 ? 62  ILE   B CB    1 
ATOM   2455 C CG1   . ILE   B 1 81  ? 35.063  44.27  40.869 1   17.8  ? 62  ILE   B CG1   1 
ATOM   2456 C CG2   . ILE   B 1 81  ? 34.463  46.111 39.181 1   16.48 ? 62  ILE   B CG2   1 
ATOM   2457 C CD1   . ILE   B 1 81  ? 36.508  44.661 40.89  1   18.96 ? 62  ILE   B CD1   1 
ATOM   2458 N N     . GLY   B 1 82  ? 33.696  48.737 41.283 1   13.49 ? 63  GLY   B N     1 
ATOM   2459 C CA    . GLY   B 1 82  ? 32.93   49.923 40.91  1   13.88 ? 63  GLY   B CA    1 
ATOM   2460 C C     . GLY   B 1 82  ? 31.897  50.276 41.952 1   13.34 ? 63  GLY   B C     1 
ATOM   2461 O O     . GLY   B 1 82  ? 30.776  50.67  41.611 1   14.08 ? 63  GLY   B O     1 
ATOM   2462 N N     . SER   B 1 83  ? 32.272  50.188 43.215 1   13.7  ? 64  SER   B N     1 
ATOM   2463 C CA    . SER   B 1 83  ? 31.461  50.449 44.392 1   14.69 ? 64  SER   B CA    1 
ATOM   2464 C C     . SER   B 1 83  ? 30.888  51.874 44.393 1   15.7  ? 64  SER   B C     1 
ATOM   2465 O O     . SER   B 1 83  ? 29.905  52.162 45.072 1   15.99 ? 64  SER   B O     1 
ATOM   2466 C CB    . SER   B 1 83  ? 32.284  50.3   45.679 1   16.88 ? 64  SER   B CB    1 
ATOM   2467 O OG    . SER   B 1 83  ? 33.033  49.091 45.738 1   18.19 ? 64  SER   B OG    1 
ATOM   2468 N N     . GLY   B 1 84  ? 31.592  52.802 43.743 1   16.11 ? 65  GLY   B N     1 
ATOM   2469 C CA    . GLY   B 1 84  ? 31.223  54.213 43.873 1   16.37 ? 65  GLY   B CA    1 
ATOM   2470 C C     . GLY   B 1 84  ? 31.326  54.598 45.35  1   15.87 ? 65  GLY   B C     1 
ATOM   2471 O O     . GLY   B 1 84  ? 32.141  54.047 46.102 1   16.74 ? 65  GLY   B O     1 
ATOM   2472 N N     . PRO   B 1 85  ? 30.424  55.486 45.761 1   15.79 ? 66  PRO   B N     1 
ATOM   2473 C CA    . PRO   B 1 85  ? 30.397  55.886 47.181 1   15.7  ? 66  PRO   B CA    1 
ATOM   2474 C C     . PRO   B 1 85  ? 29.34   55.1   47.956 1   17.22 ? 66  PRO   B C     1 
ATOM   2475 O O     . PRO   B 1 85  ? 28.916  55.579 48.997 1   18.54 ? 66  PRO   B O     1 
ATOM   2476 C CB    . PRO   B 1 85  ? 29.962  57.353 47.071 1   15.88 ? 66  PRO   B CB    1 
ATOM   2477 C CG    . PRO   B 1 85  ? 28.962  57.335 45.899 1   17.43 ? 66  PRO   B CG    1 
ATOM   2478 C CD    . PRO   B 1 85  ? 29.482  56.251 44.929 1   16.11 ? 66  PRO   B CD    1 
ATOM   2479 N N     . THR   B 1 86  ? 28.873  53.94  47.46  1   16.1  ? 67  THR   B N     1 
ATOM   2480 C CA    . THR   B 1 86  ? 27.748  53.261 48.088 1   16.97 ? 67  THR   B CA    1 
ATOM   2481 C C     . THR   B 1 86  ? 28.173  52.033 48.862 1   16.12 ? 67  THR   B C     1 
ATOM   2482 O O     . THR   B 1 86  ? 29.13   51.334 48.514 1   15.99 ? 67  THR   B O     1 
ATOM   2483 C CB    . THR   B 1 86  ? 26.628  52.891 47.069 1   17.71 ? 67  THR   B CB    1 
ATOM   2484 O OG1   . THR   B 1 86  ? 27.085  51.833 46.222 1   17.73 ? 67  THR   B OG1   1 
ATOM   2485 C CG2   . THR   B 1 86  ? 26.244  54.08  46.167 1   19.29 ? 67  THR   B CG2   1 
ATOM   2486 N N     . ILE   B 1 87  ? 27.374  51.722 49.9   1   16.15 ? 68  ILE   B N     1 
ATOM   2487 C CA    . ILE   B 1 87  ? 27.616  50.527 50.698 1   16.26 ? 68  ILE   B CA    1 
ATOM   2488 C C     . ILE   B 1 87  ? 26.366  49.614 50.709 1   16.58 ? 68  ILE   B C     1 
ATOM   2489 O O     . ILE   B 1 87  ? 26.447  48.544 51.287 1   17.37 ? 68  ILE   B O     1 
ATOM   2490 C CB    . ILE   B 1 87  ? 28.071  50.867 52.134 1   19.36 ? 68  ILE   B CB    1 
ATOM   2491 C CG1   . ILE   B 1 87  ? 27.019  51.683 52.883 1   21.64 ? 68  ILE   B CG1   1 
ATOM   2492 C CG2   . ILE   B 1 87  ? 29.437  51.594 52.124 1   21.13 ? 68  ILE   B CG2   1 
ATOM   2493 C CD1   . ILE   B 1 87  ? 26.031  50.976 53.569 1   23.7  ? 68  ILE   B CD1   1 
ATOM   2494 N N     . TYR   B 1 88  ? 25.227  50.03  50.129 1   15.97 ? 69  TYR   B N     1 
ATOM   2495 C CA    . TYR   B 1 88  ? 24.005  49.218 50.175 1   16.65 ? 69  TYR   B CA    1 
ATOM   2496 C C     . TYR   B 1 88  ? 24.212  47.808 49.663 1   16.27 ? 69  TYR   B C     1 
ATOM   2497 O O     . TYR   B 1 88  ? 23.584  46.859 50.154 1   17.49 ? 69  TYR   B O     1 
ATOM   2498 C CB    . TYR   B 1 88  ? 22.849  49.919 49.422 1   17.67 ? 69  TYR   B CB    1 
ATOM   2499 C CG    . TYR   B 1 88  ? 22.921  49.765 47.925 1   17.29 ? 69  TYR   B CG    1 
ATOM   2500 C CD1   . TYR   B 1 88  ? 22.381  48.653 47.292 1   16.93 ? 69  TYR   B CD1   1 
ATOM   2501 C CD2   . TYR   B 1 88  ? 23.618  50.676 47.152 1   16.39 ? 69  TYR   B CD2   1 
ATOM   2502 C CE1   . TYR   B 1 88  ? 22.52   48.463 45.924 1   16.47 ? 69  TYR   B CE1   1 
ATOM   2503 C CE2   . TYR   B 1 88  ? 23.774  50.49  45.775 1   16.06 ? 69  TYR   B CE2   1 
ATOM   2504 C CZ    . TYR   B 1 88  ? 23.223  49.376 45.166 1   15.16 ? 69  TYR   B CZ    1 
ATOM   2505 O OH    . TYR   B 1 88  ? 23.363  49.148 43.819 1   16.02 ? 69  TYR   B OH    1 
ATOM   2506 N N     . GLN   B 1 89  ? 25.089  47.68  48.657 1   15.2  ? 70  GLN   B N     1 
ATOM   2507 C CA    . GLN   B 1 89  ? 25.29   46.397 47.987 1   16.09 ? 70  GLN   B CA    1 
ATOM   2508 C C     . GLN   B 1 89  ? 26.114  45.439 48.786 1   15.65 ? 70  GLN   B C     1 
ATOM   2509 O O     . GLN   B 1 89  ? 26.294  44.294 48.39  1   15.6  ? 70  GLN   B O     1 
ATOM   2510 C CB    . GLN   B 1 89  ? 25.906  46.597 46.551 1   16.64 ? 70  GLN   B CB    1 
ATOM   2511 C CG    . GLN   B 1 89  ? 27.372  47.087 46.528 1   16.44 ? 70  GLN   B CG    1 
ATOM   2512 C CD    . GLN   B 1 89  ? 27.555  48.595 46.69  1   17.14 ? 70  GLN   B CD    1 
ATOM   2513 O OE1   . GLN   B 1 89  ? 26.717  49.334 47.186 1   17.67 ? 70  GLN   B OE1   1 
ATOM   2514 N NE2   . GLN   B 1 89  ? 28.714  49.126 46.263 1   18.97 ? 70  GLN   B NE2   1 
ATOM   2515 N N     . LEU   B 1 90  ? 26.581  45.875 49.992 1   16.52 ? 71  LEU   B N     1 
ATOM   2516 C CA    . LEU   B 1 90  ? 27.433  45.07  50.883 1   16.9  ? 71  LEU   B CA    1 
ATOM   2517 C C     . LEU   B 1 90  ? 26.722  44.639 52.145 1   18.1  ? 71  LEU   B C     1 
ATOM   2518 O O     . LEU   B 1 90  ? 27.298  43.897 52.932 1   19.77 ? 71  LEU   B O     1 
ATOM   2519 C CB    . LEU   B 1 90  ? 28.651  45.895 51.306 1   17.55 ? 71  LEU   B CB    1 
ATOM   2520 C CG    . LEU   B 1 90  ? 29.384  46.616 50.129 1   18.27 ? 71  LEU   B CG    1 
ATOM   2521 C CD1   . LEU   B 1 90  ? 30.467  47.558 50.66  1   20.39 ? 71  LEU   B CD1   1 
ATOM   2522 C CD2   . LEU   B 1 90  ? 29.937  45.592 49.129 1   18.26 ? 71  LEU   B CD2   1 
ATOM   2523 N N     . LEU   B 1 91  ? 25.494  45.143 52.404 1   17.03 ? 72  LEU   B N     1 
ATOM   2524 C CA    . LEU   B 1 91  ? 24.87   44.919 53.706 1   18.11 ? 72  LEU   B CA    1 
ATOM   2525 C C     . LEU   B 1 91  ? 24.475  43.479 53.937 1   19.99 ? 72  LEU   B C     1 
ATOM   2526 O O     . LEU   B 1 91  ? 24.724  43.003 55.038 1   22.32 ? 72  LEU   B O     1 
ATOM   2527 C CB    . LEU   B 1 91  ? 23.709  45.875 53.881 1   19.25 ? 72  LEU   B CB    1 
ATOM   2528 C CG    . LEU   B 1 91  ? 24.15   47.312 54.082 1   20.1  ? 72  LEU   B CG    1 
ATOM   2529 C CD1   . LEU   B 1 91  ? 22.981  48.239 53.908 1   20.48 ? 72  LEU   B CD1   1 
ATOM   2530 C CD2   . LEU   B 1 91  ? 24.769  47.541 55.493 1   21.99 ? 72  LEU   B CD2   1 
ATOM   2531 N N     . SER   B 1 92  ? 23.956  42.756 52.948 1   18.46 ? 73  SER   B N     1 
ATOM   2532 C CA    . SER   B 1 92  ? 23.685  41.323 53.147 1   19.57 ? 73  SER   B CA    1 
ATOM   2533 C C     . SER   B 1 92  ? 25.003  40.542 53.001 1   20.12 ? 73  SER   B C     1 
ATOM   2534 O O     . SER   B 1 92  ? 25.211  39.548 53.713 1   21.45 ? 73  SER   B O     1 
ATOM   2535 C CB    . SER   B 1 92  ? 22.623  40.836 52.17  1   19.62 ? 73  SER   B CB    1 
ATOM   2536 O OG    . SER   B 1 92  ? 21.334  41.311 52.538 1   21.04 ? 73  SER   B OG    1 
ATOM   2537 N N     . ALA   B 1 93  ? 25.879  40.964 52.063 1   19.15 ? 74  ALA   B N     1 
ATOM   2538 C CA    . ALA   B 1 93  ? 27.149  40.273 51.855 1   18.75 ? 74  ALA   B CA    1 
ATOM   2539 C C     . ALA   B 1 93  ? 28.013  40.182 53.086 1   19.36 ? 74  ALA   B C     1 
ATOM   2540 O O     . ALA   B 1 93  ? 28.697  39.167 53.242 1   20.12 ? 74  ALA   B O     1 
ATOM   2541 C CB    . ALA   B 1 93  ? 27.933  40.966 50.731 1   19.36 ? 74  ALA   B CB    1 
ATOM   2542 N N     . CYS   B 1 94  ? 27.993  41.192 53.976 1   19.39 ? 75  CYS   B N     1 
ATOM   2543 C CA    . CYS   B 1 94  ? 28.872  41.141 55.17  1   20.17 ? 75  CYS   B CA    1 
ATOM   2544 C C     . CYS   B 1 94  ? 28.465  40.024 56.148 1   22.28 ? 75  CYS   B C     1 
ATOM   2545 O O     . CYS   B 1 94  ? 29.254  39.691 57.037 1   22.98 ? 75  CYS   B O     1 
ATOM   2546 C CB    . CYS   B 1 94  ? 29.006  42.486 55.87  1   21.6  ? 75  CYS   B CB    1 
ATOM   2547 S SG    . CYS   B 1 94  ? 27.534  42.957 56.78  1   22.86 ? 75  CYS   B SG    1 
ATOM   2548 N N     . GLU   B 1 95  ? 27.276  39.435 55.979 1   21.6  ? 76  GLU   B N     1 
ATOM   2549 C CA    . GLU   B 1 95  ? 26.91   38.3   56.833 1   22.32 ? 76  GLU   B CA    1 
ATOM   2550 C C     . GLU   B 1 95  ? 27.589  37.011 56.354 1   23.89 ? 76  GLU   B C     1 
ATOM   2551 O O     . GLU   B 1 95  ? 27.667  36.04  57.117 1   25.68 ? 76  GLU   B O     1 
ATOM   2552 C CB    . GLU   B 1 95  ? 25.391  38.089 56.82  1   23.21 ? 76  GLU   B CB    1 
ATOM   2553 C CG    . GLU   B 1 95  ? 24.62   39.29  57.337 1   26.01 ? 76  GLU   B CG    1 
ATOM   2554 C CD    . GLU   B 1 95  ? 24.947  39.652 58.774 1   29.89 ? 76  GLU   B CD    1 
ATOM   2555 O OE1   . GLU   B 1 95  ? 25.257  38.727 59.566 1   36.46 ? 76  GLU   B OE1   1 
ATOM   2556 O OE2   . GLU   B 1 95  ? 24.861  40.853 59.117 1   29.28 ? 76  GLU   B OE2   1 
ATOM   2557 N N     . SER   B 1 96  ? 28      36.954 55.074 1   22.57 ? 77  SER   B N     1 
ATOM   2558 C CA    . SER   B 1 96  ? 28.516  35.739 54.438 1   23.93 ? 77  SER   B CA    1 
ATOM   2559 C C     . SER   B 1 96  ? 29.958  35.763 54.044 1   23.33 ? 77  SER   B C     1 
ATOM   2560 O O     . SER   B 1 96  ? 30.476  34.714 53.628 1   24.38 ? 77  SER   B O     1 
ATOM   2561 C CB    . SER   B 1 96  ? 27.696  35.445 53.184 1   25.9  ? 77  SER   B CB    1 
ATOM   2562 O OG    . SER   B 1 96  ? 26.339  35.309 53.568 1   30.16 ? 77  SER   B OG    1 
ATOM   2563 N N     . PHE   B 1 97  ? 30.624  36.909 54.154 1   21.25 ? 78  PHE   B N     1 
ATOM   2564 C CA    . PHE   B 1 97  ? 32.04   36.995 53.789 1   20.91 ? 78  PHE   B CA    1 
ATOM   2565 C C     . PHE   B 1 97  ? 32.851  37.538 54.938 1   22.41 ? 78  PHE   B C     1 
ATOM   2566 O O     . PHE   B 1 97  ? 32.506  38.595 55.48  1   24.83 ? 78  PHE   B O     1 
ATOM   2567 C CB    . PHE   B 1 97  ? 32.209  37.905 52.529 1   20.01 ? 78  PHE   B CB    1 
ATOM   2568 C CG    . PHE   B 1 97  ? 31.747  37.185 51.288 1   18.68 ? 78  PHE   B CG    1 
ATOM   2569 C CD1   . PHE   B 1 97  ? 30.428  37.233 50.886 1   21.1  ? 78  PHE   B CD1   1 
ATOM   2570 C CD2   . PHE   B 1 97  ? 32.625  36.378 50.562 1   19.87 ? 78  PHE   B CD2   1 
ATOM   2571 C CE1   . PHE   B 1 97  ? 29.995  36.532 49.777 1   22.49 ? 78  PHE   B CE1   1 
ATOM   2572 C CE2   . PHE   B 1 97  ? 32.184  35.696 49.442 1   21.36 ? 78  PHE   B CE2   1 
ATOM   2573 C CZ    . PHE   B 1 97  ? 30.873  35.756 49.072 1   22.69 ? 78  PHE   B CZ    1 
ATOM   2574 N N     . LYS   B 1 98  ? 33.974  36.914 55.229 1   23.12 ? 79  LYS   B N     1 
ATOM   2575 C CA    . LYS   B 1 98  ? 34.84   37.368 56.31  1   24.04 ? 79  LYS   B CA    1 
ATOM   2576 C C     . LYS   B 1 98  ? 35.466  38.725 55.953 1   23.28 ? 79  LYS   B C     1 
ATOM   2577 O O     . LYS   B 1 98  ? 35.614  39.584 56.825 1   23.54 ? 79  LYS   B O     1 
ATOM   2578 C CB    . LYS   B 1 98  ? 35.915  36.296 56.587 1   27.87 ? 79  LYS   B CB    1 
ATOM   2579 C CG    . LYS   B 1 98  ? 37.142  36.753 57.369 1   37.05 ? 79  LYS   B CG    1 
ATOM   2580 C CD    . LYS   B 1 98  ? 38.03   35.553 57.7   1   45.55 ? 79  LYS   B CD    1 
ATOM   2581 C CE    . LYS   B 1 98  ? 39.462  35.973 57.919 1   52.61 ? 79  LYS   B CE    1 
ATOM   2582 N NZ    . LYS   B 1 98  ? 39.938  36.828 56.8   1   56.94 ? 79  LYS   B NZ    1 
ATOM   2583 N N     . GLU   B 1 99  ? 35.875  38.885 54.698 1   20.74 ? 80  GLU   B N     1 
ATOM   2584 C CA    . GLU   B 1 99  ? 36.501  40.13  54.254 1   19.3  ? 80  GLU   B CA    1 
ATOM   2585 C C     . GLU   B 1 99  ? 35.844  40.591 52.968 1   17.91 ? 80  GLU   B C     1 
ATOM   2586 O O     . GLU   B 1 99  ? 35.505  39.781 52.099 1   16.99 ? 80  GLU   B O     1 
ATOM   2587 C CB    . GLU   B 1 99  ? 38.021  39.973 53.996 1   21.54 ? 80  GLU   B CB    1 
ATOM   2588 C CG    . GLU   B 1 99  ? 38.702  41.248 53.504 1   28.1  ? 80  GLU   B CG    1 
ATOM   2589 C CD    . GLU   B 1 99  ? 40.211  41.271 53.285 1   36.86 ? 80  GLU   B CD    1 
ATOM   2590 O OE1   . GLU   B 1 99  ? 40.883  40.274 53.621 1   41.02 ? 80  GLU   B OE1   1 
ATOM   2591 O OE2   . GLU   B 1 99  ? 40.729  42.332 52.861 1   35.57 ? 80  GLU   B OE2   1 
ATOM   2592 N N     . ILE   B 1 100 ? 35.637  41.899 52.859 1   17.22 ? 81  ILE   B N     1 
ATOM   2593 C CA    . ILE   B 1 100 ? 35.11   42.521 51.645 1   16.61 ? 81  ILE   B CA    1 
ATOM   2594 C C     . ILE   B 1 100 ? 36.104  43.626 51.235 1   18.3  ? 81  ILE   B C     1 
ATOM   2595 O O     . ILE   B 1 100 ? 36.592  44.386 52.095 1   20.01 ? 81  ILE   B O     1 
ATOM   2596 C CB    . ILE   B 1 100 ? 33.729  43.187 51.925 1   17.37 ? 81  ILE   B CB    1 
ATOM   2597 C CG1   . ILE   B 1 100 ? 32.689  42.103 52.234 1   18    ? 81  ILE   B CG1   1 
ATOM   2598 C CG2   . ILE   B 1 100 ? 33.273  44.05  50.719 1   18.15 ? 81  ILE   B CG2   1 
ATOM   2599 C CD1   . ILE   B 1 100 ? 31.291  42.64  52.623 1   19.95 ? 81  ILE   B CD1   1 
ATOM   2600 N N     . VAL   B 1 101 ? 36.505  43.653 49.962 1   16.29 ? 82  VAL   B N     1 
ATOM   2601 C CA    . VAL   B 1 101 ? 37.384  44.706 49.433 1   16.19 ? 82  VAL   B CA    1 
ATOM   2602 C C     . VAL   B 1 101 ? 36.485  45.57  48.544 1   16.66 ? 82  VAL   B C     1 
ATOM   2603 O O     . VAL   B 1 101 ? 35.709  45.034 47.746 1   16.77 ? 82  VAL   B O     1 
ATOM   2604 C CB    . VAL   B 1 101 ? 38.512  44.078 48.606 1   17.15 ? 82  VAL   B CB    1 
ATOM   2605 C CG1   . VAL   B 1 101 ? 39.287  45.149 47.836 1   18.63 ? 82  VAL   B CG1   1 
ATOM   2606 C CG2   . VAL   B 1 101 ? 39.455  43.322 49.547 1   18.5  ? 82  VAL   B CG2   1 
ATOM   2607 N N     . VAL   B 1 102 ? 36.504  46.894 48.742 1   15.52 ? 83  VAL   B N     1 
ATOM   2608 C CA    . VAL   B 1 102 ? 35.701  47.804 47.94  1   15.52 ? 83  VAL   B CA    1 
ATOM   2609 C C     . VAL   B 1 102 ? 36.621  48.558 47.001 1   15.03 ? 83  VAL   B C     1 
ATOM   2610 O O     . VAL   B 1 102 ? 37.774  48.85  47.333 1   15.34 ? 83  VAL   B O     1 
ATOM   2611 C CB    . VAL   B 1 102 ? 34.859  48.758 48.777 1   16.67 ? 83  VAL   B CB    1 
ATOM   2612 C CG1   . VAL   B 1 102 ? 33.85   47.966 49.613 1   18.25 ? 83  VAL   B CG1   1 
ATOM   2613 C CG2   . VAL   B 1 102 ? 35.733  49.663 49.656 1   19.21 ? 83  VAL   B CG2   1 
ATOM   2614 N N     . THR   B 1 103 ? 36.148  48.814 45.781 1   15.36 ? 84  THR   B N     1 
ATOM   2615 C CA    . THR   B 1 103 ? 37.01   49.397 44.752 1   15.24 ? 84  THR   B CA    1 
ATOM   2616 C C     . THR   B 1 103 ? 36.288  50.339 43.864 1   15.82 ? 84  THR   B C     1 
ATOM   2617 O O     . THR   B 1 103 ? 35.081  50.15  43.639 1   16.86 ? 84  THR   B O     1 
ATOM   2618 C CB    . THR   B 1 103 ? 37.63   48.289 43.864 1   16.36 ? 84  THR   B CB    1 
ATOM   2619 O OG1   . THR   B 1 103 ? 36.621  47.762 42.968 1   16.83 ? 84  THR   B OG1   1 
ATOM   2620 C CG2   . THR   B 1 103 ? 38.249  47.149 44.649 1   16.81 ? 84  THR   B CG2   1 
ATOM   2621 N N     . ASP   B 1 104 ? 36.991  51.289 43.239 1   15.3  ? 85  ASP   B N     1 
ATOM   2622 C CA    . ASP   B 1 104 ? 36.326  52.183 42.276 1   15.59 ? 85  ASP   B CA    1 
ATOM   2623 C C     . ASP   B 1 104 ? 37.384  52.904 41.463 1   15.05 ? 85  ASP   B C     1 
ATOM   2624 O O     . ASP   B 1 104 ? 38.539  53.041 41.926 1   15.57 ? 85  ASP   B O     1 
ATOM   2625 C CB    . ASP   B 1 104 ? 35.463  53.244 42.985 1   15.95 ? 85  ASP   B CB    1 
ATOM   2626 C CG    . ASP   B 1 104 ? 34.449  53.828 41.997 1   15.77 ? 85  ASP   B CG    1 
ATOM   2627 O OD1   . ASP   B 1 104 ? 33.528  53.113 41.614 1   14.3  ? 85  ASP   B OD1   1 
ATOM   2628 O OD2   . ASP   B 1 104 ? 34.55   55.022 41.65  1   15.11 ? 85  ASP   B OD2   1 
ATOM   2629 N N     . TYR   B 1 105 ? 37.002  53.418 40.28  1   15.28 ? 86  TYR   B N     1 
ATOM   2630 C CA    . TYR   B 1 105 ? 37.936  54.24  39.509 1   14.99 ? 86  TYR   B CA    1 
ATOM   2631 C C     . TYR   B 1 105 ? 38.113  55.629 40.128 1   15.58 ? 86  TYR   B C     1 
ATOM   2632 O O     . TYR   B 1 105 ? 39.179  56.217 39.956 1   17.33 ? 86  TYR   B O     1 
ATOM   2633 C CB    . TYR   B 1 105 ? 37.397  54.379 38.067 1   15.6  ? 86  TYR   B CB    1 
ATOM   2634 C CG    . TYR   B 1 105 ? 38.439  54.994 37.166 1   19.01 ? 86  TYR   B CG    1 
ATOM   2635 C CD1   . TYR   B 1 105 ? 39.585  54.294 36.826 1   20.29 ? 86  TYR   B CD1   1 
ATOM   2636 C CD2   . TYR   B 1 105 ? 38.313  56.292 36.713 1   20.19 ? 86  TYR   B CD2   1 
ATOM   2637 C CE1   . TYR   B 1 105 ? 40.573  54.863 36.024 1   21.5  ? 86  TYR   B CE1   1 
ATOM   2638 C CE2   . TYR   B 1 105 ? 39.284  56.865 35.899 1   21.4  ? 86  TYR   B CE2   1 
ATOM   2639 C CZ    . TYR   B 1 105 ? 40.417  56.152 35.573 1   21.86 ? 86  TYR   B CZ    1 
ATOM   2640 O OH    . TYR   B 1 105 ? 41.414  56.698 34.769 1   24.63 ? 86  TYR   B OH    1 
ATOM   2641 N N     . SER   B 1 106 ? 37.069  56.166 40.764 1   16.16 ? 87  SER   B N     1 
ATOM   2642 C CA    . SER   B 1 106 ? 37.129  57.548 41.263 1   15.95 ? 87  SER   B CA    1 
ATOM   2643 C C     . SER   B 1 106 ? 37.677  57.602 42.689 1   16.27 ? 87  SER   B C     1 
ATOM   2644 O O     . SER   B 1 106 ? 37.086  57.087 43.622 1   16.51 ? 87  SER   B O     1 
ATOM   2645 C CB    . SER   B 1 106 ? 35.735  58.171 41.188 1   18.69 ? 87  SER   B CB    1 
ATOM   2646 O OG    . SER   B 1 106 ? 35.681  59.31  42.059 1   21.69 ? 87  SER   B OG    1 
ATOM   2647 N N     . ASP   B 1 107 ? 38.755  58.389 42.88  1   17.94 ? 88  ASP   B N     1 
ATOM   2648 C CA    . ASP   B 1 107 ? 39.319  58.584 44.227 1   18.37 ? 88  ASP   B CA    1 
ATOM   2649 C C     . ASP   B 1 107 ? 38.332  59.39  45.066 1   18.35 ? 88  ASP   B C     1 
ATOM   2650 O O     . ASP   B 1 107 ? 38.239  59.119 46.274 1   19.8  ? 88  ASP   B O     1 
ATOM   2651 C CB    . ASP   B 1 107 ? 40.662  59.354 44.147 1   21.65 ? 88  ASP   B CB    1 
ATOM   2652 C CG    . ASP   B 1 107 ? 41.62   58.691 43.19  1   33.4  ? 88  ASP   B CG    1 
ATOM   2653 O OD1   . ASP   B 1 107 ? 42.284  57.726 43.599 1   37.47 ? 88  ASP   B OD1   1 
ATOM   2654 O OD2   . ASP   B 1 107 ? 41.649  59.096 41.997 1   39.7  ? 88  ASP   B OD2   1 
ATOM   2655 N N     . GLN   B 1 108 ? 37.53   60.323 44.466 1   17.61 ? 89  GLN   B N     1 
ATOM   2656 C CA    . GLN   B 1 108 ? 36.531  61.053 45.257 1   18.69 ? 89  GLN   B CA    1 
ATOM   2657 C C     . GLN   B 1 108 ? 35.49   60.077 45.843 1   17.6  ? 89  GLN   B C     1 
ATOM   2658 O O     . GLN   B 1 108 ? 35.064  60.215 46.986 1   18.44 ? 89  GLN   B O     1 
ATOM   2659 C CB    . GLN   B 1 108 ? 35.756  62.074 44.366 1   21.63 ? 89  GLN   B CB    1 
ATOM   2660 C CG    . GLN   B 1 108 ? 36.46   63.353 43.949 1   27.84 ? 89  GLN   B CG    1 
ATOM   2661 C CD    . GLN   B 1 108 ? 35.402  64.312 43.389 1   33.66 ? 89  GLN   B CD    1 
ATOM   2662 O OE1   . GLN   B 1 108 ? 35.127  64.386 42.161 1   38.53 ? 89  GLN   B OE1   1 
ATOM   2663 N NE2   . GLN   B 1 108 ? 34.743  65.036 44.28  1   30.68 ? 89  GLN   B NE2   1 
ATOM   2664 N N     . ASN   B 1 109 ? 35.106  59.044 45.055 1   16.14 ? 90  ASN   B N     1 
ATOM   2665 C CA    . ASN   B 1 109 ? 34.153  58.093 45.542 1   16.62 ? 90  ASN   B CA    1 
ATOM   2666 C C     . ASN   B 1 109 ? 34.739  57.257 46.685 1   17.03 ? 90  ASN   B C     1 
ATOM   2667 O O     . ASN   B 1 109 ? 34.055  57.003 47.691 1   18.33 ? 90  ASN   B O     1 
ATOM   2668 C CB    . ASN   B 1 109 ? 33.742  57.157 44.419 1   17.82 ? 90  ASN   B CB    1 
ATOM   2669 C CG    . ASN   B 1 109 ? 32.673  57.759 43.58  1   19.29 ? 90  ASN   B CG    1 
ATOM   2670 O OD1   . ASN   B 1 109 ? 31.886  58.605 44.049 1   22.28 ? 90  ASN   B OD1   1 
ATOM   2671 N ND2   . ASN   B 1 109 ? 32.527  57.265 42.326 1   17.86 ? 90  ASN   B ND2   1 
ATOM   2672 N N     . LEU   B 1 110 ? 35.994  56.845 46.542 1   17.59 ? 91  LEU   B N     1 
ATOM   2673 C CA    . LEU   B 1 110 ? 36.639  56.056 47.611 1   19.32 ? 91  LEU   B CA    1 
ATOM   2674 C C     . LEU   B 1 110 ? 36.755  56.876 48.902 1   18.93 ? 91  LEU   B C     1 
ATOM   2675 O O     . LEU   B 1 110 ? 36.572  56.343 50.003 1   19.95 ? 91  LEU   B O     1 
ATOM   2676 C CB    . LEU   B 1 110 ? 38.033  55.585 47.197 1   21.44 ? 91  LEU   B CB    1 
ATOM   2677 C CG    . LEU   B 1 110 ? 38.005  54.61  45.993 1   26.6  ? 91  LEU   B CG    1 
ATOM   2678 C CD1   . LEU   B 1 110 ? 39.398  54.223 45.635 1   29.12 ? 91  LEU   B CD1   1 
ATOM   2679 C CD2   . LEU   B 1 110 ? 37.115  53.411 46.273 1   28.13 ? 91  LEU   B CD2   1 
ATOM   2680 N N     . GLN   B 1 111 ? 37.024  58.176 48.758 1   18.39 ? 92  GLN   B N     1 
ATOM   2681 C CA    . GLN   B 1 111 ? 37.106  59.012 49.962 1   19.35 ? 92  GLN   B CA    1 
ATOM   2682 C C     . GLN   B 1 111 ? 35.744  59.121 50.637 1   18.14 ? 92  GLN   B C     1 
ATOM   2683 O O     . GLN   B 1 111 ? 35.663  59.108 51.873 1   19.62 ? 92  GLN   B O     1 
ATOM   2684 C CB    . GLN   B 1 111 ? 37.643  60.398 49.593 1   22.57 ? 92  GLN   B CB    1 
ATOM   2685 C CG    . GLN   B 1 111 ? 39.095  60.349 49.188 1   29.37 ? 92  GLN   B CG    1 
ATOM   2686 C CD    . GLN   B 1 111 ? 39.664  61.715 48.885 1   41.49 ? 92  GLN   B CD    1 
ATOM   2687 O OE1   . GLN   B 1 111 ? 39.445  62.688 49.629 1   45.44 ? 92  GLN   B OE1   1 
ATOM   2688 N NE2   . GLN   B 1 111 ? 40.441  61.804 47.812 1   43.03 ? 92  GLN   B NE2   1 
ATOM   2689 N N     . GLU   B 1 112 ? 34.655  59.175 49.86  1   18.22 ? 93  GLU   B N     1 
ATOM   2690 C CA    . GLU   B 1 112 ? 33.299  59.242 50.412 1   20.13 ? 93  GLU   B CA    1 
ATOM   2691 C C     . GLU   B 1 112 ? 32.956  57.919 51.138 1   21.45 ? 93  GLU   B C     1 
ATOM   2692 O O     . GLU   B 1 112 ? 32.45   57.945 52.275 1   21.84 ? 93  GLU   B O     1 
ATOM   2693 C CB    . GLU   B 1 112 ? 32.299  59.643 49.307 1   22.62 ? 93  GLU   B CB    1 
ATOM   2694 C CG    . GLU   B 1 112 ? 30.863  59.841 49.768 1   22.72 ? 93  GLU   B CG    1 
ATOM   2695 C CD    . GLU   B 1 112 ? 30.616  61.032 50.673 1   25.11 ? 93  GLU   B CD    1 
ATOM   2696 O OE1   . GLU   B 1 112 ? 31.334  62.052 50.56  1   28.46 ? 93  GLU   B OE1   1 
ATOM   2697 O OE2   . GLU   B 1 112 ? 29.662  60.947 51.478 1   28.71 ? 93  GLU   B OE2   1 
ATOM   2698 N N     . LEU   B 1 113 ? 33.387  56.782 50.558 1   20.61 ? 94  LEU   B N     1 
ATOM   2699 C CA    . LEU   B 1 113 ? 33.241  55.465 51.207 1   22.53 ? 94  LEU   B CA    1 
ATOM   2700 C C     . LEU   B 1 113 ? 33.993  55.448 52.524 1   22.36 ? 94  LEU   B C     1 
ATOM   2701 O O     . LEU   B 1 113 ? 33.458  55.011 53.552 1   22.46 ? 94  LEU   B O     1 
ATOM   2702 C CB    . LEU   B 1 113 ? 33.913  54.369 50.343 1   23.5  ? 94  LEU   B CB    1 
ATOM   2703 C CG    . LEU   B 1 113 ? 33.16   53.841 49.193 1   25.25 ? 94  LEU   B CG    1 
ATOM   2704 C CD1   . LEU   B 1 113 ? 34.029  52.795 48.452 1   26.12 ? 94  LEU   B CD1   1 
ATOM   2705 C CD2   . LEU   B 1 113 ? 31.89   53.179 49.669 1   25.07 ? 94  LEU   B CD2   1 
ATOM   2706 N N     . GLU   B 1 114 ? 35.223  55.928 52.498 1   21.59 ? 95  GLU   B N     1 
ATOM   2707 C CA    . GLU   B 1 114 ? 36.066  55.92  53.682 1   23.76 ? 95  GLU   B CA    1 
ATOM   2708 C C     . GLU   B 1 114 ? 35.509  56.766 54.788 1   23.1  ? 95  GLU   B C     1 
ATOM   2709 O O     . GLU   B 1 114 ? 35.616  56.368 55.954 1   23.94 ? 95  GLU   B O     1 
ATOM   2710 C CB    . GLU   B 1 114 ? 37.504  56.28  53.36  1   27.77 ? 95  GLU   B CB    1 
ATOM   2711 C CG    . GLU   B 1 114 ? 38.114  55.124 52.6   1   36.93 ? 95  GLU   B CG    1 
ATOM   2712 C CD    . GLU   B 1 114 ? 39.609  55.15  52.395 1   49.03 ? 95  GLU   B CD    1 
ATOM   2713 O OE1   . GLU   B 1 114 ? 40.071  55.897 51.502 1   51.94 ? 95  GLU   B OE1   1 
ATOM   2714 O OE2   . GLU   B 1 114 ? 40.312  54.376 53.086 1   51.78 ? 95  GLU   B OE2   1 
ATOM   2715 N N     . LYS   B 1 115 ? 34.821  57.877 54.459 1   21.67 ? 96  LYS   B N     1 
ATOM   2716 C CA    . LYS   B 1 115 ? 34.182  58.701 55.502 1   22.43 ? 96  LYS   B CA    1 
ATOM   2717 C C     . LYS   B 1 115 ? 33.135  57.862 56.246 1   22.14 ? 96  LYS   B C     1 
ATOM   2718 O O     . LYS   B 1 115 ? 33.035  57.929 57.47  1   24.37 ? 96  LYS   B O     1 
ATOM   2719 C CB    . LYS   B 1 115 ? 33.494  59.91  54.876 1   24.73 ? 96  LYS   B CB    1 
ATOM   2720 C CG    . LYS   B 1 115 ? 34.501  60.992 54.458 1   28.32 ? 96  LYS   B CG    1 
ATOM   2721 C CD    . LYS   B 1 115 ? 33.763  62.221 53.93  1   34.05 ? 96  LYS   B CD    1 
ATOM   2722 C CE    . LYS   B 1 115 ? 34.766  63.334 53.701 1   42.18 ? 96  LYS   B CE    1 
ATOM   2723 N NZ    . LYS   B 1 115 ? 34.464  64.144 52.483 1   48.57 ? 96  LYS   B NZ    1 
ATOM   2724 N N     . TRP   B 1 116 ? 32.382  57.004 55.507 1   21.1  ? 97  TRP   B N     1 
ATOM   2725 C CA    . TRP   B 1 116 ? 31.4    56.165 56.158 1   20.77 ? 97  TRP   B CA    1 
ATOM   2726 C C     . TRP   B 1 116 ? 32.06   55.053 56.945 1   20.36 ? 97  TRP   B C     1 
ATOM   2727 O O     . TRP   B 1 116 ? 31.666  54.783 58.098 1   20.72 ? 97  TRP   B O     1 
ATOM   2728 C CB    . TRP   B 1 116 ? 30.395  55.577 55.154 1   21.39 ? 97  TRP   B CB    1 
ATOM   2729 C CG    . TRP   B 1 116 ? 29.278  54.908 55.876 1   21.35 ? 97  TRP   B CG    1 
ATOM   2730 C CD1   . TRP   B 1 116 ? 28.167  55.504 56.393 1   22.58 ? 97  TRP   B CD1   1 
ATOM   2731 C CD2   . TRP   B 1 116 ? 29.194  53.513 56.249 1   21.09 ? 97  TRP   B CD2   1 
ATOM   2732 N NE1   . TRP   B 1 116 ? 27.384  54.571 57.037 1   23.68 ? 97  TRP   B NE1   1 
ATOM   2733 C CE2   . TRP   B 1 116 ? 27.982  53.342 56.947 1   22.6  ? 97  TRP   B CE2   1 
ATOM   2734 C CE3   . TRP   B 1 116 ? 30.005  52.395 56.021 1   22.56 ? 97  TRP   B CE3   1 
ATOM   2735 C CZ2   . TRP   B 1 116 ? 27.584  52.106 57.462 1   24.51 ? 97  TRP   B CZ2   1 
ATOM   2736 C CZ3   . TRP   B 1 116 ? 29.608  51.18  56.549 1   23.89 ? 97  TRP   B CZ3   1 
ATOM   2737 C CH2   . TRP   B 1 116 ? 28.421  51.055 57.272 1   23.69 ? 97  TRP   B CH2   1 
ATOM   2738 N N     . LEU   B 1 117 ? 33.064  54.397 56.361 1   20.2  ? 98  LEU   B N     1 
ATOM   2739 C CA    . LEU   B 1 117 ? 33.743  53.299 57.045 1   21.46 ? 98  LEU   B CA    1 
ATOM   2740 C C     . LEU   B 1 117 ? 34.366  53.756 58.362 1   22.62 ? 98  LEU   B C     1 
ATOM   2741 O O     . LEU   B 1 117 ? 34.279  53.054 59.359 1   24.28 ? 98  LEU   B O     1 
ATOM   2742 C CB    . LEU   B 1 117 ? 34.809  52.705 56.15  1   21.28 ? 98  LEU   B CB    1 
ATOM   2743 C CG    . LEU   B 1 117 ? 34.245  51.988 54.921 1   21.42 ? 98  LEU   B CG    1 
ATOM   2744 C CD1   . LEU   B 1 117 ? 35.391  51.653 53.967 1   22    ? 98  LEU   B CD1   1 
ATOM   2745 C CD2   . LEU   B 1 117 ? 33.453  50.713 55.319 1   22.21 ? 98  LEU   B CD2   1 
ATOM   2746 N N     . LYS   B 1 118 ? 34.943  54.961 58.371 1   22.47 ? 99  LYS   B N     1 
ATOM   2747 C CA    . LYS   B 1 118 ? 35.542  55.521 59.6   1   24.32 ? 99  LYS   B CA    1 
ATOM   2748 C C     . LYS   B 1 118 ? 34.555  56.268 60.478 1   26.16 ? 99  LYS   B C     1 
ATOM   2749 O O     . LYS   B 1 118 ? 34.987  56.832 61.496 1   27.26 ? 99  LYS   B O     1 
ATOM   2750 C CB    . LYS   B 1 118 ? 36.716  56.471 59.226 1   26.26 ? 99  LYS   B CB    1 
ATOM   2751 C CG    . LYS   B 1 118 ? 37.84   55.729 58.517 1   31.31 ? 99  LYS   B CG    1 
ATOM   2752 C CD    . LYS   B 1 118 ? 38.998  56.629 58.103 1   36.44 ? 99  LYS   B CD    1 
ATOM   2753 C CE    . LYS   B 1 118 ? 39.95   55.88  57.215 1   41.2  ? 99  LYS   B CE    1 
ATOM   2754 N NZ    . LYS   B 1 118 ? 40.992  56.777 56.633 1   45.96 ? 99  LYS   B NZ    1 
ATOM   2755 N N     . ALA   B 1 119 ? 33.272  56.325 60.13  1   25.48 ? 100 ALA   B N     1 
ATOM   2756 C CA    . ALA   B 1 119 ? 32.249  57.047 60.901 1   26.66 ? 100 ALA   B CA    1 
ATOM   2757 C C     . ALA   B 1 119 ? 32.613  58.518 61.062 1   28.2  ? 100 ALA   B C     1 
ATOM   2758 O O     . ALA   B 1 119 ? 32.346  59.113 62.11  1   29.58 ? 100 ALA   B O     1 
ATOM   2759 C CB    . ALA   B 1 119 ? 31.989  56.388 62.268 1   26.68 ? 100 ALA   B CB    1 
ATOM   2760 N N     . ALA   B 1 120 ? 33.141  59.122 60.001 1   27.2  ? 101 ALA   B N     1 
ATOM   2761 C CA    . ALA   B 1 120 ? 33.466  60.555 60.008 1   27.13 ? 101 ALA   B CA    1 
ATOM   2762 C C     . ALA   B 1 120 ? 32.173  61.367 60.027 1   28.37 ? 101 ALA   B C     1 
ATOM   2763 O O     . ALA   B 1 120 ? 31.133  60.923 59.58  1   28.51 ? 101 ALA   B O     1 
ATOM   2764 C CB    . ALA   B 1 120 ? 34.305  60.915 58.786 1   27.21 ? 101 ALA   B CB    1 
ATOM   2765 N N     . PRO   B 1 121 ? 32.201  62.596 60.588 1   30.93 ? 102 PRO   B N     1 
ATOM   2766 C CA    . PRO   B 1 121 ? 30.951  63.364 60.718 1   31.78 ? 102 PRO   B CA    1 
ATOM   2767 C C     . PRO   B 1 121 ? 30.217  63.673 59.412 1   32.3  ? 102 PRO   B C     1 
ATOM   2768 O O     . PRO   B 1 121 ? 28.983  63.708 59.411 1   34.06 ? 102 PRO   B O     1 
ATOM   2769 C CB    . PRO   B 1 121 ? 31.37   64.644 61.471 1   32.3  ? 102 PRO   B CB    1 
ATOM   2770 C CG    . PRO   B 1 121 ? 32.704  64.344 62.051 1   32.4  ? 102 PRO   B CG    1 
ATOM   2771 C CD    . PRO   B 1 121 ? 33.35   63.266 61.212 1   31.61 ? 102 PRO   B CD    1 
ATOM   2772 N N     . ALA   B 1 122 ? 30.941  63.855 58.311 1   31.05 ? 103 ALA   B N     1 
ATOM   2773 C CA    . ALA   B 1 122 ? 30.278  64.181 57.052 1   31.49 ? 103 ALA   B CA    1 
ATOM   2774 C C     . ALA   B 1 122 ? 29.845  62.95  56.265 1   30.52 ? 103 ALA   B C     1 
ATOM   2775 O O     . ALA   B 1 122 ? 29.512  63.099 55.084 1   31.02 ? 103 ALA   B O     1 
ATOM   2776 C CB    . ALA   B 1 122 ? 31.148  65.073 56.201 1   31.91 ? 103 ALA   B CB    1 
ATOM   2777 N N     . ALA   B 1 123 ? 29.898  61.747 56.871 1   29.64 ? 104 ALA   B N     1 
ATOM   2778 C CA    . ALA   B 1 123 ? 29.52   60.516 56.184 1   29.37 ? 104 ALA   B CA    1 
ATOM   2779 C C     . ALA   B 1 123 ? 28.053  60.545 55.827 1   27.35 ? 104 ALA   B C     1 
ATOM   2780 O O     . ALA   B 1 123 ? 27.238  61.18  56.514 1   27.88 ? 104 ALA   B O     1 
ATOM   2781 C CB    . ALA   B 1 123 ? 29.785  59.318 57.085 1   30.14 ? 104 ALA   B CB    1 
ATOM   2782 N N     . PHE   B 1 124 ? 27.682  59.834 54.738 1   25.34 ? 105 PHE   B N     1 
ATOM   2783 C CA    . PHE   B 1 124 ? 26.274  59.764 54.336 1   22.94 ? 105 PHE   B CA    1 
ATOM   2784 C C     . PHE   B 1 124 ? 25.461  58.969 55.336 1   24.8  ? 105 PHE   B C     1 
ATOM   2785 O O     . PHE   B 1 124 ? 25.963  58.023 55.942 1   24.63 ? 105 PHE   B O     1 
ATOM   2786 C CB    . PHE   B 1 124 ? 26.19   59.066 52.954 1   21.52 ? 105 PHE   B CB    1 
ATOM   2787 C CG    . PHE   B 1 124 ? 24.807  59.05  52.343 1   20.84 ? 105 PHE   B CG    1 
ATOM   2788 C CD1   . PHE   B 1 124 ? 24.238  60.206 51.839 1   22.07 ? 105 PHE   B CD1   1 
ATOM   2789 C CD2   . PHE   B 1 124 ? 24.122  57.856 52.173 1   21.56 ? 105 PHE   B CD2   1 
ATOM   2790 C CE1   . PHE   B 1 124 ? 22.967  60.175 51.248 1   22.61 ? 105 PHE   B CE1   1 
ATOM   2791 C CE2   . PHE   B 1 124 ? 22.861  57.827 51.572 1   22.37 ? 105 PHE   B CE2   1 
ATOM   2792 C CZ    . PHE   B 1 124 ? 22.302  58.982 51.09  1   22.54 ? 105 PHE   B CZ    1 
ATOM   2793 N N     . ASP   B 1 125 ? 24.186  59.308 55.472 1   24.43 ? 106 ASP   B N     1 
ATOM   2794 C CA    . ASP   B 1 125 ? 23.312  58.583 56.401 1   24.38 ? 106 ASP   B CA    1 
ATOM   2795 C C     . ASP   B 1 125 ? 22.645  57.422 55.68  1   24.19 ? 106 ASP   B C     1 
ATOM   2796 O O     . ASP   B 1 125 ? 21.644  57.592 54.99  1   25.21 ? 106 ASP   B O     1 
ATOM   2797 C CB    . ASP   B 1 125 ? 22.243  59.525 56.98  1   26.6  ? 106 ASP   B CB    1 
ATOM   2798 C CG    . ASP   B 1 125 ? 21.296  58.85  57.956 1   31.75 ? 106 ASP   B CG    1 
ATOM   2799 O OD1   . ASP   B 1 125 ? 21.568  57.673 58.348 1   28.25 ? 106 ASP   B OD1   1 
ATOM   2800 O OD2   . ASP   B 1 125 ? 20.314  59.525 58.399 1   37.38 ? 106 ASP   B OD2   1 
ATOM   2801 N N     . TRP   B 1 126 ? 23.198  56.213 55.884 1   22.34 ? 107 TRP   B N     1 
ATOM   2802 C CA    . TRP   B 1 126 ? 22.624  54.993 55.298 1   21.65 ? 107 TRP   B CA    1 
ATOM   2803 C C     . TRP   B 1 126 ? 21.599  54.34  56.222 1   21.32 ? 107 TRP   B C     1 
ATOM   2804 O O     . TRP   B 1 126 ? 21.065  53.281 55.871 1   21.74 ? 107 TRP   B O     1 
ATOM   2805 C CB    . TRP   B 1 126 ? 23.758  53.986 55.044 1   20.12 ? 107 TRP   B CB    1 
ATOM   2806 C CG    . TRP   B 1 126 ? 24.596  54.33  53.854 1   19.27 ? 107 TRP   B CG    1 
ATOM   2807 C CD1   . TRP   B 1 126 ? 25.852  54.886 53.835 1   18.73 ? 107 TRP   B CD1   1 
ATOM   2808 C CD2   . TRP   B 1 126 ? 24.22   54.121 52.483 1   18.57 ? 107 TRP   B CD2   1 
ATOM   2809 N NE1   . TRP   B 1 126 ? 26.251  55.098 52.52  1   18.8  ? 107 TRP   B NE1   1 
ATOM   2810 C CE2   . TRP   B 1 126 ? 25.268  54.629 51.68  1   19.06 ? 107 TRP   B CE2   1 
ATOM   2811 C CE3   . TRP   B 1 126 ? 23.059  53.662 51.858 1   17.66 ? 107 TRP   B CE3   1 
ATOM   2812 C CZ2   . TRP   B 1 126 ? 25.196  54.65  50.286 1   18.66 ? 107 TRP   B CZ2   1 
ATOM   2813 C CZ3   . TRP   B 1 126 ? 23.003  53.637 50.475 1   18.37 ? 107 TRP   B CZ3   1 
ATOM   2814 C CH2   . TRP   B 1 126 ? 24.077  54.119 49.707 1   17.82 ? 107 TRP   B CH2   1 
ATOM   2815 N N     . SER   B 1 127 ? 21.282  54.942 57.405 1   22.31 ? 108 SER   B N     1 
ATOM   2816 C CA    . SER   B 1 127 ? 20.41   54.253 58.379 1   24.57 ? 108 SER   B CA    1 
ATOM   2817 C C     . SER   B 1 127 ? 19.047  53.77  57.835 1   24.55 ? 108 SER   B C     1 
ATOM   2818 O O     . SER   B 1 127 ? 18.676  52.651 58.215 1   26.14 ? 108 SER   B O     1 
ATOM   2819 C CB    . SER   B 1 127 ? 20.222  55.055 59.671 1   29.67 ? 108 SER   B CB    1 
ATOM   2820 O OG    . SER   B 1 127 ? 19.622  56.307 59.445 1   33.77 ? 108 SER   B OG    1 
ATOM   2821 N N     . PRO   B 1 128 ? 18.314  54.477 56.936 1   26.35 ? 109 PRO   B N     1 
ATOM   2822 C CA    . PRO   B 1 128 ? 17.039  53.907 56.439 1   26.91 ? 109 PRO   B CA    1 
ATOM   2823 C C     . PRO   B 1 128 ? 17.249  52.628 55.626 1   25.44 ? 109 PRO   B C     1 
ATOM   2824 O O     . PRO   B 1 128 ? 16.454  51.714 55.677 1   26.87 ? 109 PRO   B O     1 
ATOM   2825 C CB    . PRO   B 1 128 ? 16.457  55.006 55.55  1   29.36 ? 109 PRO   B CB    1 
ATOM   2826 C CG    . PRO   B 1 128 ? 17.275  56.217 55.805 1   29.5  ? 109 PRO   B CG    1 
ATOM   2827 C CD    . PRO   B 1 128 ? 18.571  55.812 56.369 1   27.03 ? 109 PRO   B CD    1 
ATOM   2828 N N     . VAL   B 1 129 ? 18.372  52.567 54.865 1   22.15 ? 110 VAL   B N     1 
ATOM   2829 C CA    . VAL   B 1 129 ? 18.685  51.391 54.068 1   21.23 ? 110 VAL   B CA    1 
ATOM   2830 C C     . VAL   B 1 129 ? 19.112  50.261 54.997 1   19.94 ? 110 VAL   B C     1 
ATOM   2831 O O     . VAL   B 1 129 ? 18.685  49.109 54.816 1   20.28 ? 110 VAL   B O     1 
ATOM   2832 C CB    . VAL   B 1 129 ? 19.797  51.751 53.072 1   22.15 ? 110 VAL   B CB    1 
ATOM   2833 C CG1   . VAL   B 1 129 ? 20.3    50.487 52.358 1   22.4  ? 110 VAL   B CG1   1 
ATOM   2834 C CG2   . VAL   B 1 129 ? 19.278  52.78  52.069 1   23.56 ? 110 VAL   B CG2   1 
ATOM   2835 N N     . VAL   B 1 130 ? 19.971  50.572 55.988 1   21.07 ? 111 VAL   B N     1 
ATOM   2836 C CA    . VAL   B 1 130 ? 20.42   49.541 56.946 1   22.21 ? 111 VAL   B CA    1 
ATOM   2837 C C     . VAL   B 1 130 ? 19.22   48.914 57.69  1   22.66 ? 111 VAL   B C     1 
ATOM   2838 O O     . VAL   B 1 130 ? 19.142  47.691 57.817 1   22.81 ? 111 VAL   B O     1 
ATOM   2839 C CB    . VAL   B 1 130 ? 21.423  50.152 57.942 1   23.33 ? 111 VAL   B CB    1 
ATOM   2840 C CG1   . VAL   B 1 130 ? 21.769  49.155 59.026 1   26.63 ? 111 VAL   B CG1   1 
ATOM   2841 C CG2   . VAL   B 1 130 ? 22.695  50.626 57.216 1   21.94 ? 111 VAL   B CG2   1 
ATOM   2842 N N     . THR   B 1 131 ? 18.281  49.766 58.114 1   23.8  ? 112 THR   B N     1 
ATOM   2843 C CA    . THR   B 1 131 ? 17.089  49.28  58.806 1   24.78 ? 112 THR   B CA    1 
ATOM   2844 C C     . THR   B 1 131 ? 16.266  48.349 57.909 1   24.7  ? 112 THR   B C     1 
ATOM   2845 O O     . THR   B 1 131 ? 15.834  47.285 58.347 1   26.08 ? 112 THR   B O     1 
ATOM   2846 C CB    . THR   B 1 131 ? 16.238  50.476 59.256 1   27.76 ? 112 THR   B CB    1 
ATOM   2847 O OG1   . THR   B 1 131 ? 16.994  51.193 60.236 1   30.55 ? 112 THR   B OG1   1 
ATOM   2848 C CG2   . THR   B 1 131 ? 14.899  50.051 59.868 1   29.71 ? 112 THR   B CG2   1 
ATOM   2849 N N     . TYR   B 1 132 ? 16.133  48.731 56.61  1   23.18 ? 113 TYR   B N     1 
ATOM   2850 C CA    . TYR   B 1 132 ? 15.39   47.913 55.667 1   23.51 ? 113 TYR   B CA    1 
ATOM   2851 C C     . TYR   B 1 132 ? 16.037  46.521 55.49  1   23.03 ? 113 TYR   B C     1 
ATOM   2852 O O     . TYR   B 1 132 ? 15.332  45.499 55.501 1   23.86 ? 113 TYR   B O     1 
ATOM   2853 C CB    . TYR   B 1 132 ? 15.255  48.66  54.343 1   25.08 ? 113 TYR   B CB    1 
ATOM   2854 C CG    . TYR   B 1 132 ? 14.409  47.937 53.326 1   26.77 ? 113 TYR   B CG    1 
ATOM   2855 C CD1   . TYR   B 1 132 ? 13.023  48.007 53.363 1   29.32 ? 113 TYR   B CD1   1 
ATOM   2856 C CD2   . TYR   B 1 132 ? 14.991  47.206 52.309 1   27.9  ? 113 TYR   B CD2   1 
ATOM   2857 C CE1   . TYR   B 1 132 ? 12.247  47.309 52.446 1   31.93 ? 113 TYR   B CE1   1 
ATOM   2858 C CE2   . TYR   B 1 132 ? 14.223  46.555 51.355 1   29.42 ? 113 TYR   B CE2   1 
ATOM   2859 C CZ    . TYR   B 1 132 ? 12.852  46.66  51.387 1   32.02 ? 113 TYR   B CZ    1 
ATOM   2860 O OH    . TYR   B 1 132 ? 12.098  46.003 50.443 1   34.7  ? 113 TYR   B OH    1 
ATOM   2861 N N     . VAL   B 1 133 ? 17.381  46.458 55.405 1   22.82 ? 114 VAL   B N     1 
ATOM   2862 C CA    . VAL   B 1 133 ? 18.068  45.177 55.299 1   21.98 ? 114 VAL   B CA    1 
ATOM   2863 C C     . VAL   B 1 133 ? 17.915  44.355 56.598 1   23.35 ? 114 VAL   B C     1 
ATOM   2864 O O     . VAL   B 1 133 ? 17.721  43.152 56.549 1   24.08 ? 114 VAL   B O     1 
ATOM   2865 C CB    . VAL   B 1 133 ? 19.542  45.348 54.907 1   20.58 ? 114 VAL   B CB    1 
ATOM   2866 C CG1   . VAL   B 1 133 ? 20.271  44.006 54.933 1   21.86 ? 114 VAL   B CG1   1 
ATOM   2867 C CG2   . VAL   B 1 133 ? 19.658  45.998 53.522 1   20.53 ? 114 VAL   B CG2   1 
ATOM   2868 N N     . CYS   B 1 134 ? 17.988  45.023 57.758 1   23.97 ? 115 CYS   B N     1 
ATOM   2869 C CA    . CYS   B 1 134 ? 17.782  44.303 59.039 1   24.32 ? 115 CYS   B CA    1 
ATOM   2870 C C     . CYS   B 1 134 ? 16.384  43.637 59.072 1   25.6  ? 115 CYS   B C     1 
ATOM   2871 O O     . CYS   B 1 134 ? 16.243  42.507 59.533 1   26.45 ? 115 CYS   B O     1 
ATOM   2872 C CB    . CYS   B 1 134 ? 17.964  45.264 60.204 1   24.25 ? 115 CYS   B CB    1 
ATOM   2873 S SG    . CYS   B 1 134 ? 19.686  45.7   60.516 1   26.58 ? 115 CYS   B SG    1 
ATOM   2874 N N     . ASP   B 1 135 ? 15.385  44.35  58.536 1   26.56 ? 116 ASP   B N     1 
ATOM   2875 C CA    . ASP   B 1 135 ? 14.02   43.829 58.43  1   26.15 ? 116 ASP   B CA    1 
ATOM   2876 C C     . ASP   B 1 135 ? 13.96   42.606 57.503 1   27.03 ? 116 ASP   B C     1 
ATOM   2877 O O     . ASP   B 1 135 ? 13.327  41.606 57.849 1   27.86 ? 116 ASP   B O     1 
ATOM   2878 C CB    . ASP   B 1 135 ? 13.07   44.924 57.898 1   28.93 ? 116 ASP   B CB    1 
ATOM   2879 C CG    . ASP   B 1 135 ? 12.766  46.045 58.862 1   34.99 ? 116 ASP   B CG    1 
ATOM   2880 O OD1   . ASP   B 1 135 ? 13.135  45.923 60.053 1   37.23 ? 116 ASP   B OD1   1 
ATOM   2881 O OD2   . ASP   B 1 135 ? 12.127  47.033 58.437 1   36.71 ? 116 ASP   B OD2   1 
ATOM   2882 N N     . LEU   B 1 136 ? 14.57   42.694 56.306 1   25.83 ? 117 LEU   B N     1 
ATOM   2883 C CA    . LEU   B 1 136 ? 14.584  41.587 55.329 1   26.8  ? 117 LEU   B CA    1 
ATOM   2884 C C     . LEU   B 1 136 ? 15.16   40.306 55.942 1   27.9  ? 117 LEU   B C     1 
ATOM   2885 O O     . LEU   B 1 136 ? 14.674  39.19  55.703 1   28.14 ? 117 LEU   B O     1 
ATOM   2886 C CB    . LEU   B 1 136 ? 15.49   41.947 54.109 1   26.05 ? 117 LEU   B CB    1 
ATOM   2887 C CG    . LEU   B 1 136 ? 15.109  43.11  53.231 1   26.47 ? 117 LEU   B CG    1 
ATOM   2888 C CD1   . LEU   B 1 136 ? 16.132  43.266 52.067 1   27.71 ? 117 LEU   B CD1   1 
ATOM   2889 C CD2   . LEU   B 1 136 ? 13.725  42.9   52.651 1   26.25 ? 117 LEU   B CD2   1 
ATOM   2890 N N     . GLU   B 1 137 ? 16.255  40.475 56.676 1   26.84 ? 118 GLU   B N     1 
ATOM   2891 C CA    . GLU   B 1 137 ? 17.031  39.392 57.263 1   27.42 ? 118 GLU   B CA    1 
ATOM   2892 C C     . GLU   B 1 137 ? 16.43   38.79  58.546 1   28.84 ? 118 GLU   B C     1 
ATOM   2893 O O     . GLU   B 1 137 ? 17.012  37.866 59.105 1   31.3  ? 118 GLU   B O     1 
ATOM   2894 C CB    . GLU   B 1 137 ? 18.474  39.868 57.495 1   26.7  ? 118 GLU   B CB    1 
ATOM   2895 C CG    . GLU   B 1 137 ? 19.164  40.185 56.175 1   25.71 ? 118 GLU   B CG    1 
ATOM   2896 C CD    . GLU   B 1 137 ? 20.622  40.563 56.286 1   28.47 ? 118 GLU   B CD    1 
ATOM   2897 O OE1   . GLU   B 1 137 ? 21.09   40.784 57.425 1   27.76 ? 118 GLU   B OE1   1 
ATOM   2898 O OE2   . GLU   B 1 137 ? 21.29   40.68  55.228 1   27    ? 118 GLU   B OE2   1 
ATOM   2899 N N     . GLY   B 1 138 ? 15.254  39.254 58.964 1   27.84 ? 119 GLY   B N     1 
ATOM   2900 C CA    . GLY   B 1 138 ? 14.542  38.643 60.074 1   29.35 ? 119 GLY   B CA    1 
ATOM   2901 C C     . GLY   B 1 138 ? 14.562  39.379 61.388 1   29.76 ? 119 GLY   B C     1 
ATOM   2902 O O     . GLY   B 1 138 ? 14.151  38.825 62.417 1   29.72 ? 119 GLY   B O     1 
ATOM   2903 N N     . ASN   B 1 139 ? 15.074  40.617 61.378 1   29.45 ? 120 ASN   B N     1 
ATOM   2904 C CA    . ASN   B 1 139 ? 15.218  41.422 62.609 1   29.23 ? 120 ASN   B CA    1 
ATOM   2905 C C     . ASN   B 1 139 ? 16.054  40.696 63.654 1   30.52 ? 120 ASN   B C     1 
ATOM   2906 O O     . ASN   B 1 139 ? 15.75   40.733 64.863 1   32.62 ? 120 ASN   B O     1 
ATOM   2907 C CB    . ASN   B 1 139 ? 13.87   41.898 63.156 1   30.76 ? 120 ASN   B CB    1 
ATOM   2908 C CG    . ASN   B 1 139 ? 13.243  42.909 62.236 1   33.17 ? 120 ASN   B CG    1 
ATOM   2909 O OD1   . ASN   B 1 139 ? 13.72   44.053 62.114 1   34.8  ? 120 ASN   B OD1   1 
ATOM   2910 N ND2   . ASN   B 1 139 ? 12.197  42.482 61.53  1   30.97 ? 120 ASN   B ND2   1 
ATOM   2911 N N     . ARG   B 1 140 ? 17.083  39.974 63.172 1   29.48 ? 121 ARG   B N     1 
ATOM   2912 C CA    . ARG   B 1 140 ? 18.005  39.279 64.063 1   30.13 ? 121 ARG   B CA    1 
ATOM   2913 C C     . ARG   B 1 140 ? 18.839  40.331 64.819 1   30.19 ? 121 ARG   B C     1 
ATOM   2914 O O     . ARG   B 1 140 ? 19.232  40.092 65.954 1   32.72 ? 121 ARG   B O     1 
ATOM   2915 C CB    . ARG   B 1 140 ? 18.937  38.364 63.252 1   31.05 ? 121 ARG   B CB    1 
ATOM   2916 C CG    . ARG   B 1 140 ? 18.206  37.326 62.379 1   33.72 ? 121 ARG   B CG    1 
ATOM   2917 C CD    . ARG   B 1 140 ? 19.247  36.428 61.736 1   37.3  ? 121 ARG   B CD    1 
ATOM   2918 N NE    . ARG   B 1 140 ? 18.671  35.474 60.785 1   41.76 ? 121 ARG   B NE    1 
ATOM   2919 C CZ    . ARG   B 1 140 ? 18.294  34.237 61.097 1   42.8  ? 121 ARG   B CZ    1 
ATOM   2920 N NH1   . ARG   B 1 140 ? 18.395  33.799 62.349 1   40.64 ? 121 ARG   B NH1   1 
ATOM   2921 N NH2   . ARG   B 1 140 ? 17.815  33.426 60.159 1   43.17 ? 121 ARG   B NH2   1 
ATOM   2922 N N     . VAL   B 1 141 ? 19.201  41.447 64.146 1   28.6  ? 122 VAL   B N     1 
ATOM   2923 C CA    . VAL   B 1 141 ? 20.008  42.522 64.715 1   28.91 ? 122 VAL   B CA    1 
ATOM   2924 C C     . VAL   B 1 141 ? 19.374  43.893 64.388 1   28.6  ? 122 VAL   B C     1 
ATOM   2925 O O     . VAL   B 1 141 ? 18.506  43.999 63.493 1   29.05 ? 122 VAL   B O     1 
ATOM   2926 C CB    . VAL   B 1 141 ? 21.475  42.467 64.184 1   29.79 ? 122 VAL   B CB    1 
ATOM   2927 C CG1   . VAL   B 1 141 ? 22.127  41.122 64.463 1   30.82 ? 122 VAL   B CG1   1 
ATOM   2928 C CG2   . VAL   B 1 141 ? 21.54   42.807 62.676 1   30.06 ? 122 VAL   B CG2   1 
ATOM   2929 N N     . LYS   B 1 142 ? 19.824  44.944 65.086 1   26.93 ? 123 LYS   B N     1 
ATOM   2930 C CA    . LYS   B 1 142 ? 19.424  46.304 64.8   1   26.84 ? 123 LYS   B CA    1 
ATOM   2931 C C     . LYS   B 1 142 ? 20.533  47     63.982 1   26.69 ? 123 LYS   B C     1 
ATOM   2932 O O     . LYS   B 1 142 ? 21.643  46.488 63.86  1   26.69 ? 123 LYS   B O     1 
ATOM   2933 C CB    . LYS   B 1 142 ? 19.118  47.066 66.085 1   28.15 ? 123 LYS   B CB    1 
ATOM   2934 C CG    . LYS   B 1 142 ? 17.959  46.454 66.849 1   31.05 ? 123 LYS   B CG    1 
ATOM   2935 C CD    . LYS   B 1 142 ? 17.651  47.244 68.107 1   34.58 ? 123 LYS   B CD    1 
ATOM   2936 C CE    . LYS   B 1 142 ? 16.583  46.551 68.904 1   40.35 ? 123 LYS   B CE    1 
ATOM   2937 N NZ    . LYS   B 1 142 ? 15.325  46.501 68.12  1   44.81 ? 123 LYS   B NZ    1 
ATOM   2938 N N     . GLY   B 1 143 ? 20.224  48.185 63.493 1   26.85 ? 124 GLY   B N     1 
ATOM   2939 C CA    . GLY   B 1 143 ? 21.104  48.962 62.636 1   27.21 ? 124 GLY   B CA    1 
ATOM   2940 C C     . GLY   B 1 143 ? 22.545  49.087 63.064 1   27.69 ? 124 GLY   B C     1 
ATOM   2941 O O     . GLY   B 1 143 ? 23.432  48.765 62.271 1   27.36 ? 124 GLY   B O     1 
ATOM   2942 N N     . PRO   B 1 144 ? 22.826  49.585 64.281 1   27.16 ? 125 PRO   B N     1 
ATOM   2943 C CA    . PRO   B 1 144 ? 24.24   49.768 64.68  1   27.39 ? 125 PRO   B CA    1 
ATOM   2944 C C     . PRO   B 1 144 ? 25.094  48.491 64.622 1   26.84 ? 125 PRO   B C     1 
ATOM   2945 O O     . PRO   B 1 144 ? 26.266  48.539 64.205 1   27.11 ? 125 PRO   B O     1 
ATOM   2946 C CB    . PRO   B 1 144 ? 24.136  50.351 66.098 1   29.4  ? 125 PRO   B CB    1 
ATOM   2947 C CG    . PRO   B 1 144 ? 22.777  51.015 66.145 1   30.11 ? 125 PRO   B CG    1 
ATOM   2948 C CD    . PRO   B 1 144 ? 21.894  50.099 65.318 1   28.03 ? 125 PRO   B CD    1 
ATOM   2949 N N     . GLU   B 1 145 ? 24.525  47.345 65.015 1   26.58 ? 126 GLU   B N     1 
ATOM   2950 C CA    . GLU   B 1 145 ? 25.24   46.072 64.964 1   25.11 ? 126 GLU   B CA    1 
ATOM   2951 C C     . GLU   B 1 145 ? 25.539  45.68  63.503 1   25.29 ? 126 GLU   B C     1 
ATOM   2952 O O     . GLU   B 1 145 ? 26.629  45.208 63.181 1   25.26 ? 126 GLU   B O     1 
ATOM   2953 C CB    . GLU   B 1 145 ? 24.443  44.966 65.673 1   26.77 ? 126 GLU   B CB    1 
ATOM   2954 C CG    . GLU   B 1 145 ? 25.146  43.629 65.619 1   29.32 ? 126 GLU   B CG    1 
ATOM   2955 C CD    . GLU   B 1 145 ? 24.577  42.542 66.516 1   36.19 ? 126 GLU   B CD    1 
ATOM   2956 O OE1   . GLU   B 1 145 ? 23.581  42.804 67.235 1   35.82 ? 126 GLU   B OE1   1 
ATOM   2957 O OE2   . GLU   B 1 145 ? 25.133  41.418 66.481 1   36.64 ? 126 GLU   B OE2   1 
ATOM   2958 N N     . LYS   B 1 146 ? 24.543  45.847 62.624 1   24.98 ? 127 LYS   B N     1 
ATOM   2959 C CA    . LYS   B 1 146 ? 24.745  45.571 61.187 1   23.7  ? 127 LYS   B CA    1 
ATOM   2960 C C     . LYS   B 1 146 ? 25.877  46.454 60.591 1   23.07 ? 127 LYS   B C     1 
ATOM   2961 O O     . LYS   B 1 146 ? 26.752  45.958 59.881 1   22.54 ? 127 LYS   B O     1 
ATOM   2962 C CB    . LYS   B 1 146 ? 23.41   45.776 60.432 1   24.54 ? 127 LYS   B CB    1 
ATOM   2963 C CG    . LYS   B 1 146 ? 23.518  45.929 58.91  1   29.02 ? 127 LYS   B CG    1 
ATOM   2964 C CD    . LYS   B 1 146 ? 22.901  44.776 58.174 1   36.06 ? 127 LYS   B CD    1 
ATOM   2965 C CE    . LYS   B 1 146 ? 23.91   43.705 57.991 1   35.9  ? 127 LYS   B CE    1 
ATOM   2966 N NZ    . LYS   B 1 146 ? 23.268  42.411 57.537 1   28.98 ? 127 LYS   B NZ    1 
ATOM   2967 N N     . GLU   B 1 147 ? 25.848  47.758 60.886 1   22.98 ? 128 GLU   B N     1 
ATOM   2968 C CA    . GLU   B 1 147 ? 26.883  48.663 60.366 1   21.77 ? 128 GLU   B CA    1 
ATOM   2969 C C     . GLU   B 1 147 ? 28.249  48.289 60.87  1   21.9  ? 128 GLU   B C     1 
ATOM   2970 O O     . GLU   B 1 147 ? 29.213  48.343 60.105 1   22.41 ? 128 GLU   B O     1 
ATOM   2971 C CB    . GLU   B 1 147 ? 26.621  50.106 60.753 1   24.58 ? 128 GLU   B CB    1 
ATOM   2972 C CG    . GLU   B 1 147 ? 25.389  50.687 60.089 1   27.8  ? 128 GLU   B CG    1 
ATOM   2973 C CD    . GLU   B 1 147 ? 25.289  52.196 60.257 1   33.16 ? 128 GLU   B CD    1 
ATOM   2974 O OE1   . GLU   B 1 147 ? 26.105  52.795 61.004 1   34.47 ? 128 GLU   B OE1   1 
ATOM   2975 O OE2   . GLU   B 1 147 ? 24.359  52.777 59.66  1   33.71 ? 128 GLU   B OE2   1 
ATOM   2976 N N     . GLU   B 1 148 ? 28.35   47.925 62.167 1   21.64 ? 129 GLU   B N     1 
ATOM   2977 C CA    . GLU   B 1 148 ? 29.643  47.539 62.706 1   22.75 ? 129 GLU   B CA    1 
ATOM   2978 C C     . GLU   B 1 148 ? 30.145  46.266 62.023 1   22.46 ? 129 GLU   B C     1 
ATOM   2979 O O     . GLU   B 1 148 ? 31.344  46.181 61.731 1   23.32 ? 129 GLU   B O     1 
ATOM   2980 C CB    . GLU   B 1 148 ? 29.578  47.38  64.232 1   25.39 ? 129 GLU   B CB    1 
ATOM   2981 C CG    . GLU   B 1 148 ? 30.88   46.923 64.87  1   26.09 ? 129 GLU   B CG    1 
ATOM   2982 C CD    . GLU   B 1 148 ? 32.062  47.869 64.8   1   29.45 ? 129 GLU   B CD    1 
ATOM   2983 O OE1   . GLU   B 1 148 ? 31.909  49.02  64.326 1   29.64 ? 129 GLU   B OE1   1 
ATOM   2984 O OE2   . GLU   B 1 148 ? 33.162  47.442 65.216 1   32.21 ? 129 GLU   B OE2   1 
ATOM   2985 N N     . LYS   B 1 149 ? 29.253  45.311 61.726 1   23.07 ? 130 LYS   B N     1 
ATOM   2986 C CA    . LYS   B 1 149 ? 29.666  44.09  61.017 1   23.16 ? 130 LYS   B CA    1 
ATOM   2987 C C     . LYS   B 1 149 ? 30.253  44.411 59.629 1   22.06 ? 130 LYS   B C     1 
ATOM   2988 O O     . LYS   B 1 149 ? 31.307  43.887 59.24  1   22.11 ? 130 LYS   B O     1 
ATOM   2989 C CB    . LYS   B 1 149 ? 28.492  43.127 60.877 1   26.19 ? 130 LYS   B CB    1 
ATOM   2990 C CG    . LYS   B 1 149 ? 28.992  41.764 60.4   1   31.43 ? 130 LYS   B CG    1 
ATOM   2991 C CD    . LYS   B 1 149 ? 27.973  40.698 60.62  1   36.31 ? 130 LYS   B CD    1 
ATOM   2992 C CE    . LYS   B 1 149 ? 28.632  39.381 60.937 1   41.2  ? 130 LYS   B CE    1 
ATOM   2993 N NZ    . LYS   B 1 149 ? 27.595  38.339 61.142 1   42.24 ? 130 LYS   B NZ    1 
ATOM   2994 N N     . LEU   B 1 150 ? 29.631  45.378 58.935 1   20.46 ? 131 LEU   B N     1 
ATOM   2995 C CA    . LEU   B 1 150 ? 30.15   45.773 57.629 1   19.58 ? 131 LEU   B CA    1 
ATOM   2996 C C     . LEU   B 1 150 ? 31.478  46.494 57.769 1   19.37 ? 131 LEU   B C     1 
ATOM   2997 O O     . LEU   B 1 150 ? 32.42   46.181 57.043 1   19.46 ? 131 LEU   B O     1 
ATOM   2998 C CB    . LEU   B 1 150 ? 29.137  46.631 56.881 1   19.92 ? 131 LEU   B CB    1 
ATOM   2999 C CG    . LEU   B 1 150 ? 29.634  47.152 55.531 1   19.96 ? 131 LEU   B CG    1 
ATOM   3000 C CD1   . LEU   B 1 150 ? 30.081  46.013 54.584 1   20.23 ? 131 LEU   B CD1   1 
ATOM   3001 C CD2   . LEU   B 1 150 ? 28.558  47.972 54.839 1   20.85 ? 131 LEU   B CD2   1 
ATOM   3002 N N     . ARG   B 1 151 ? 31.602  47.439 58.737 1   20.1  ? 132 ARG   B N     1 
ATOM   3003 C CA    . ARG   B 1 151 ? 32.866  48.148 58.938 1   20.62 ? 132 ARG   B CA    1 
ATOM   3004 C C     . ARG   B 1 151 ? 33.993  47.188 59.258 1   21.87 ? 132 ARG   B C     1 
ATOM   3005 O O     . ARG   B 1 151 ? 35.116  47.385 58.776 1   22.37 ? 132 ARG   B O     1 
ATOM   3006 C CB    . ARG   B 1 151 ? 32.714  49.192 60.042 1   22.02 ? 132 ARG   B CB    1 
ATOM   3007 C CG    . ARG   B 1 151 ? 31.86   50.368 59.579 1   22.89 ? 132 ARG   B CG    1 
ATOM   3008 C CD    . ARG   B 1 151 ? 31.765  51.442 60.661 1   25.2  ? 132 ARG   B CD    1 
ATOM   3009 N NE    . ARG   B 1 151 ? 31.15   52.645 60.11  1   24.79 ? 132 ARG   B NE    1 
ATOM   3010 C CZ    . ARG   B 1 151 ? 29.948  53.1   60.45  1   23.89 ? 132 ARG   B CZ    1 
ATOM   3011 N NH1   . ARG   B 1 151 ? 29.244  52.495 61.405 1   25.33 ? 132 ARG   B NH1   1 
ATOM   3012 N NH2   . ARG   B 1 151 ? 29.449  54.175 59.856 1   24.42 ? 132 ARG   B NH2   1 
ATOM   3013 N N     . GLN   B 1 152 ? 33.715  46.14  60.058 1   21.29 ? 133 GLN   B N     1 
ATOM   3014 C CA    . GLN   B 1 152 ? 34.765  45.167 60.371 1   21.71 ? 133 GLN   B CA    1 
ATOM   3015 C C     . GLN   B 1 152 ? 35.148  44.315 59.174 1   23.91 ? 133 GLN   B C     1 
ATOM   3016 O O     . GLN   B 1 152 ? 36.285  43.849 59.1   1   25.43 ? 133 GLN   B O     1 
ATOM   3017 C CB    . GLN   B 1 152 ? 34.377  44.283 61.557 1   22.06 ? 133 GLN   B CB    1 
ATOM   3018 C CG    . GLN   B 1 152 ? 34.237  45.034 62.876 1   26.3  ? 133 GLN   B CG    1 
ATOM   3019 C CD    . GLN   B 1 152 ? 35.587  45.526 63.343 1   29.73 ? 133 GLN   B CD    1 
ATOM   3020 O OE1   . GLN   B 1 152 ? 36.633  44.886 63.11  1   30.66 ? 133 GLN   B OE1   1 
ATOM   3021 N NE2   . GLN   B 1 152 ? 35.581  46.662 64.048 1   29.77 ? 133 GLN   B NE2   1 
ATOM   3022 N N     . ALA   B 1 153 ? 34.233  44.126 58.235 1   22.85 ? 134 ALA   B N     1 
ATOM   3023 C CA    . ALA   B 1 153 ? 34.506  43.287 57.064 1   21.01 ? 134 ALA   B CA    1 
ATOM   3024 C C     . ALA   B 1 153 ? 35.365  43.971 56.026 1   20.47 ? 134 ALA   B C     1 
ATOM   3025 O O     . ALA   B 1 153 ? 36.143  43.307 55.349 1   21.15 ? 134 ALA   B O     1 
ATOM   3026 C CB    . ALA   B 1 153 ? 33.195  42.834 56.418 1   21.22 ? 134 ALA   B CB    1 
ATOM   3027 N N     . VAL   B 1 154 ? 35.29   45.306 55.927 1   21.09 ? 135 VAL   B N     1 
ATOM   3028 C CA    . VAL   B 1 154 ? 36.02   46.023 54.906 1   22    ? 135 VAL   B CA    1 
ATOM   3029 C C     . VAL   B 1 154 ? 37.412  46.417 55.369 1   25.41 ? 135 VAL   B C     1 
ATOM   3030 O O     . VAL   B 1 154 ? 37.53   47.251 56.257 1   26.17 ? 135 VAL   B O     1 
ATOM   3031 C CB    . VAL   B 1 154 ? 35.195  47.245 54.429 1   20.17 ? 135 VAL   B CB    1 
ATOM   3032 C CG1   . VAL   B 1 154 ? 35.932  47.973 53.315 1   20.26 ? 135 VAL   B CG1   1 
ATOM   3033 C CG2   . VAL   B 1 154 ? 33.798  46.834 53.942 1   21.29 ? 135 VAL   B CG2   1 
ATOM   3034 N N     . LYS   B 1 155 ? 38.496  45.825 54.815 1   27.63 ? 136 LYS   B N     1 
ATOM   3035 C CA    . LYS   B 1 155 ? 39.861  46.192 55.243 1   29.15 ? 136 LYS   B CA    1 
ATOM   3036 C C     . LYS   B 1 155 ? 40.634  46.998 54.198 1   28.2  ? 136 LYS   B C     1 
ATOM   3037 O O     . LYS   B 1 155 ? 41.572  47.735 54.532 1   31.12 ? 136 LYS   B O     1 
ATOM   3038 C CB    . LYS   B 1 155 ? 40.692  44.954 55.634 1   32.58 ? 136 LYS   B CB    1 
ATOM   3039 C CG    . LYS   B 1 155 ? 39.963  43.995 56.553 1   39.75 ? 136 LYS   B CG    1 
ATOM   3040 C CD    . LYS   B 1 155 ? 39.862  44.556 57.959 1   45.54 ? 136 LYS   B CD    1 
ATOM   3041 C CE    . LYS   B 1 155 ? 39.611  43.444 58.96  1   50.11 ? 136 LYS   B CE    1 
ATOM   3042 N NZ    . LYS   B 1 155 ? 38.596  42.466 58.481 1   53.64 ? 136 LYS   B NZ    1 
ATOM   3043 N N     . GLN   B 1 156 ? 40.243  46.876 52.901 1   23.72 ? 137 GLN   B N     1 
ATOM   3044 C CA    . GLN   B 1 156 ? 40.945  47.582 51.837 1   20.81 ? 137 GLN   B CA    1 
ATOM   3045 C C     . GLN   B 1 156 ? 39.977  48.305 50.919 1   18.74 ? 137 GLN   B C     1 
ATOM   3046 O O     . GLN   B 1 156 ? 38.875  47.796 50.635 1   18.33 ? 137 GLN   B O     1 
ATOM   3047 C CB    . GLN   B 1 156 ? 41.771  46.606 51.012 1   22.28 ? 137 GLN   B CB    1 
ATOM   3048 C CG    . GLN   B 1 156 ? 42.704  45.743 51.882 1   25.15 ? 137 GLN   B CG    1 
ATOM   3049 C CD    . GLN   B 1 156 ? 43.507  44.764 51.088 1   31.64 ? 137 GLN   B CD    1 
ATOM   3050 O OE1   . GLN   B 1 156 ? 44.336  45.163 50.282 1   32.65 ? 137 GLN   B OE1   1 
ATOM   3051 N NE2   . GLN   B 1 156 ? 43.222  43.47  51.288 1   34.54 ? 137 GLN   B NE2   1 
ATOM   3052 N N     . VAL   B 1 157 ? 40.342  49.526 50.53  1   18.28 ? 138 VAL   B N     1 
ATOM   3053 C CA    . VAL   B 1 157 ? 39.572  50.414 49.675 1   18.5  ? 138 VAL   B CA    1 
ATOM   3054 C C     . VAL   B 1 157 ? 40.547  50.783 48.578 1   19.58 ? 138 VAL   B C     1 
ATOM   3055 O O     . VAL   B 1 157 ? 41.522  51.503 48.83  1   21.24 ? 138 VAL   B O     1 
ATOM   3056 C CB    . VAL   B 1 157 ? 39.174  51.642 50.512 1   20.39 ? 138 VAL   B CB    1 
ATOM   3057 C CG1   . VAL   B 1 157 ? 38.459  52.657 49.63  1   22.88 ? 138 VAL   B CG1   1 
ATOM   3058 C CG2   . VAL   B 1 157 ? 38.289  51.2   51.696 1   20.42 ? 138 VAL   B CG2   1 
ATOM   3059 N N     . LEU   B 1 158 ? 40.335  50.266 47.373 1   18.34 ? 139 LEU   B N     1 
ATOM   3060 C CA    . LEU   B 1 158 ? 41.323  50.307 46.296 1   17.67 ? 139 LEU   B CA    1 
ATOM   3061 C C     . LEU   B 1 158 ? 40.856  50.924 45.012 1   17.02 ? 139 LEU   B C     1 
ATOM   3062 O O     . LEU   B 1 158 ? 39.715  50.754 44.598 1   16.43 ? 139 LEU   B O     1 
ATOM   3063 C CB    . LEU   B 1 158 ? 41.738  48.854 45.965 1   18.7  ? 139 LEU   B CB    1 
ATOM   3064 C CG    . LEU   B 1 158 ? 42.303  48.035 47.154 1   21.64 ? 139 LEU   B CG    1 
ATOM   3065 C CD1   . LEU   B 1 158 ? 42.608  46.647 46.761 1   21.97 ? 139 LEU   B CD1   1 
ATOM   3066 C CD2   . LEU   B 1 158 ? 43.581  48.673 47.684 1   22.28 ? 139 LEU   B CD2   1 
ATOM   3067 N N     . LYS   B 1 159 ? 41.78   51.54  44.305 1   17.23 ? 140 LYS   B N     1 
ATOM   3068 C CA    . LYS   B 1 159 ? 41.557  52.001 42.951 1   16.86 ? 140 LYS   B CA    1 
ATOM   3069 C C     . LYS   B 1 159 ? 41.404  50.794 42.021 1   17.7  ? 140 LYS   B C     1 
ATOM   3070 O O     . LYS   B 1 159 ? 42.139  49.781 42.102 1   19.36 ? 140 LYS   B O     1 
ATOM   3071 C CB    . LYS   B 1 159 ? 42.796  52.813 42.524 1   18.79 ? 140 LYS   B CB    1 
ATOM   3072 C CG    . LYS   B 1 159 ? 42.774  53.25  41.074 1   25.94 ? 140 LYS   B CG    1 
ATOM   3073 C CD    . LYS   B 1 159 ? 41.918  54.478 41.001 1   32.18 ? 140 LYS   B CD    1 
ATOM   3074 C CE    . LYS   B 1 159 ? 42.481  55.546 40.084 1   35    ? 140 LYS   B CE    1 
ATOM   3075 N NZ    . LYS   B 1 159 ? 41.661  55.774 38.862 1   32.68 ? 140 LYS   B NZ    1 
ATOM   3076 N N     A CYS   B 1 160 ? 40.423  50.866 41.124 0.5 17.18 ? 141 CYS   B N     1 
ATOM   3077 N N     B CYS   B 1 160 ? 40.433  50.916 41.129 0.5 17.73 ? 141 CYS   B N     1 
ATOM   3078 C CA    A CYS   B 1 160 ? 40.304  49.847 40.098 0.5 16.74 ? 141 CYS   B CA    1 
ATOM   3079 C CA    B CYS   B 1 160 ? 40.137  49.875 40.19  0.5 17.6  ? 141 CYS   B CA    1 
ATOM   3080 C C     A CYS   B 1 160 ? 39.965  50.451 38.762 0.5 15.45 ? 141 CYS   B C     1 
ATOM   3081 C C     B CYS   B 1 160 ? 39.829  50.412 38.784 0.5 15.71 ? 141 CYS   B C     1 
ATOM   3082 O O     A CYS   B 1 160 ? 39.447  51.579 38.679 0.5 16.62 ? 141 CYS   B O     1 
ATOM   3083 O O     B CYS   B 1 160 ? 39.098  51.401 38.68  0.5 16.54 ? 141 CYS   B O     1 
ATOM   3084 C CB    A CYS   B 1 160 ? 39.301  48.772 40.488 0.5 17.94 ? 141 CYS   B CB    1 
ATOM   3085 C CB    B CYS   B 1 160 ? 38.948  49.102 40.736 0.5 19.66 ? 141 CYS   B CB    1 
ATOM   3086 S SG    A CYS   B 1 160 ? 37.58   49.301 40.323 0.5 17.21 ? 141 CYS   B SG    1 
ATOM   3087 S SG    B CYS   B 1 160 ? 38.209  47.977 39.549 0.5 20.78 ? 141 CYS   B SG    1 
ATOM   3088 N N     . ASP   B 1 161 ? 40.265  49.707 37.71  1   15.24 ? 142 ASP   B N     1 
ATOM   3089 C CA    . ASP   B 1 161 ? 39.869  50.098 36.367 1   14.49 ? 142 ASP   B CA    1 
ATOM   3090 C C     . ASP   B 1 161 ? 39.509  48.813 35.657 1   14.75 ? 142 ASP   B C     1 
ATOM   3091 O O     . ASP   B 1 161 ? 40.395  48.012 35.303 1   15    ? 142 ASP   B O     1 
ATOM   3092 C CB    . ASP   B 1 161 ? 41.001  50.85  35.637 1   15.51 ? 142 ASP   B CB    1 
ATOM   3093 C CG    . ASP   B 1 161 ? 40.639  51.269 34.232 1   16.97 ? 142 ASP   B CG    1 
ATOM   3094 O OD1   . ASP   B 1 161 ? 39.545  50.876 33.734 1   16.74 ? 142 ASP   B OD1   1 
ATOM   3095 O OD2   . ASP   B 1 161 ? 41.451  51.986 33.615 1   19.85 ? 142 ASP   B OD2   1 
ATOM   3096 N N     . VAL   B 1 162 ? 38.208  48.583 35.446 1   15.01 ? 143 VAL   B N     1 
ATOM   3097 C CA    . VAL   B 1 162 ? 37.744  47.311 34.869 1   15.24 ? 143 VAL   B CA    1 
ATOM   3098 C C     . VAL   B 1 162 ? 38.233  47.089 33.45  1   16.26 ? 143 VAL   B C     1 
ATOM   3099 O O     . VAL   B 1 162 ? 38.118  45.971 32.954 1   16.44 ? 143 VAL   B O     1 
ATOM   3100 C CB    . VAL   B 1 162 ? 36.204  47.188 34.923 1   15.93 ? 143 VAL   B CB    1 
ATOM   3101 C CG1   . VAL   B 1 162 ? 35.706  47.344 36.343 1   16.84 ? 143 VAL   B CG1   1 
ATOM   3102 C CG2   . VAL   B 1 162 ? 35.512  48.169 33.949 1   16.87 ? 143 VAL   B CG2   1 
ATOM   3103 N N     . THR   B 1 163 ? 38.703  48.161 32.765 1   15.95 ? 144 THR   B N     1 
ATOM   3104 C CA    . THR   B 1 163 ? 39.099  47.982 31.36  1   17.23 ? 144 THR   B CA    1 
ATOM   3105 C C     . THR   B 1 163 ? 40.537  47.45  31.264 1   18.7  ? 144 THR   B C     1 
ATOM   3106 O O     . THR   B 1 163 ? 41.001  47.206 30.122 1   20.79 ? 144 THR   B O     1 
ATOM   3107 C CB    . THR   B 1 163 ? 38.967  49.321 30.6   1   19.16 ? 144 THR   B CB    1 
ATOM   3108 O OG1   . THR   B 1 163 ? 39.978  50.227 31.071 1   19.94 ? 144 THR   B OG1   1 
ATOM   3109 C CG2   . THR   B 1 163 ? 37.572  49.913 30.662 1   20.73 ? 144 THR   B CG2   1 
ATOM   3110 N N     . GLN   B 1 164 ? 41.259  47.318 32.39  1   17.68 ? 145 GLN   B N     1 
ATOM   3111 C CA    . GLN   B 1 164 ? 42.639  46.854 32.372 1   19.13 ? 145 GLN   B CA    1 
ATOM   3112 C C     . GLN   B 1 164 ? 42.746  45.396 32.694 1   19.51 ? 145 GLN   B C     1 
ATOM   3113 O O     . GLN   B 1 164 ? 42.034  44.872 33.571 1   18.88 ? 145 GLN   B O     1 
ATOM   3114 C CB    . GLN   B 1 164 ? 43.466  47.673 33.356 1   21.03 ? 145 GLN   B CB    1 
ATOM   3115 C CG    . GLN   B 1 164 ? 43.436  49.186 33.092 1   23.08 ? 145 GLN   B CG    1 
ATOM   3116 C CD    . GLN   B 1 164 ? 43.836  49.503 31.671 1   26.43 ? 145 GLN   B CD    1 
ATOM   3117 O OE1   . GLN   B 1 164 ? 43.008  49.899 30.844 1   28.08 ? 145 GLN   B OE1   1 
ATOM   3118 N NE2   . GLN   B 1 164 ? 45.084  49.2   31.365 1   25.18 ? 145 GLN   B NE2   1 
ATOM   3119 N N     . SER   B 1 165 ? 43.753  44.752 32.085 1   19.64 ? 146 SER   B N     1 
ATOM   3120 C CA    . SER   B 1 165 ? 43.978  43.319 32.334 1   20.7  ? 146 SER   B CA    1 
ATOM   3121 C C     . SER   B 1 165 ? 44.162  42.996 33.837 1   21.81 ? 146 SER   B C     1 
ATOM   3122 O O     . SER   B 1 165 ? 43.762  41.927 34.297 1   23.69 ? 146 SER   B O     1 
ATOM   3123 C CB    . SER   B 1 165 ? 45.25   42.844 31.603 1   24.74 ? 146 SER   B CB    1 
ATOM   3124 O OG    . SER   B 1 165 ? 45.078  43.046 30.214 1   29.34 ? 146 SER   B OG    1 
ATOM   3125 N N     . GLN   B 1 166 ? 44.825  43.92  34.583 1   22.62 ? 147 GLN   B N     1 
ATOM   3126 C CA    . GLN   B 1 166 ? 44.977  43.838 36.033 1   21.72 ? 147 GLN   B CA    1 
ATOM   3127 C C     . GLN   B 1 166 ? 44.116  45.014 36.557 1   20.81 ? 147 GLN   B C     1 
ATOM   3128 O O     . GLN   B 1 166 ? 44.622  46.131 36.689 1   21.02 ? 147 GLN   B O     1 
ATOM   3129 C CB    . GLN   B 1 166 ? 46.441  44.091 36.483 1   26.5  ? 147 GLN   B CB    1 
ATOM   3130 C CG    . GLN   B 1 166 ? 47.373  42.867 36.419 1   33.67 ? 147 GLN   B CG    1 
ATOM   3131 C CD    . GLN   B 1 166 ? 47.788  42.564 35.017 1   43.2  ? 147 GLN   B CD    1 
ATOM   3132 O OE1   . GLN   B 1 166 ? 47.569  41.46  34.489 1   45.81 ? 147 GLN   B OE1   1 
ATOM   3133 N NE2   . GLN   B 1 166 ? 48.408  43.542 34.381 1   45.02 ? 147 GLN   B NE2   1 
ATOM   3134 N N     . PRO   B 1 167 ? 42.825  44.805 36.859 1   19.44 ? 148 PRO   B N     1 
ATOM   3135 C CA    . PRO   B 1 167 ? 41.991  45.955 37.29  1   18.52 ? 148 PRO   B CA    1 
ATOM   3136 C C     . PRO   B 1 167 ? 42.497  46.644 38.538 1   19.67 ? 148 PRO   B C     1 
ATOM   3137 O O     . PRO   B 1 167 ? 42.215  47.831 38.721 1   19.19 ? 148 PRO   B O     1 
ATOM   3138 C CB    . PRO   B 1 167 ? 40.595  45.33  37.553 1   19.36 ? 148 PRO   B CB    1 
ATOM   3139 C CG    . PRO   B 1 167 ? 40.561  44.13  36.658 1   21.71 ? 148 PRO   B CG    1 
ATOM   3140 C CD    . PRO   B 1 167 ? 42.011  43.573 36.732 1   19.82 ? 148 PRO   B CD    1 
ATOM   3141 N N     . LEU   B 1 168 ? 43.2    45.918 39.406 1   19.75 ? 149 LEU   B N     1 
ATOM   3142 C CA    . LEU   B 1 168 ? 43.695  46.516 40.647 1   21.27 ? 149 LEU   B CA    1 
ATOM   3143 C C     . LEU   B 1 168 ? 45.145  46.971 40.524 1   21.76 ? 149 LEU   B C     1 
ATOM   3144 O O     . LEU   B 1 168 ? 45.754  47.298 41.558 1   23.45 ? 149 LEU   B O     1 
ATOM   3145 C CB    . LEU   B 1 168 ? 43.538  45.555 41.814 1   22.78 ? 149 LEU   B CB    1 
ATOM   3146 C CG    . LEU   B 1 168 ? 42.121  44.981 41.966 1   23.33 ? 149 LEU   B CG    1 
ATOM   3147 C CD1   . LEU   B 1 168 ? 42.072  44.021 43.143 1   24.76 ? 149 LEU   B CD1   1 
ATOM   3148 C CD2   . LEU   B 1 168 ? 41.076  46.043 42.106 1   22.86 ? 149 LEU   B CD2   1 
ATOM   3149 N N     . GLY   B 1 169 ? 45.64   47.105 39.293 1   22.72 ? 150 GLY   B N     1 
ATOM   3150 C CA    . GLY   B 1 169 ? 46.987  47.608 39.021 1   25.54 ? 150 GLY   B CA    1 
ATOM   3151 C C     . GLY   B 1 169 ? 48.088  46.782 39.637 1   27.45 ? 150 GLY   B C     1 
ATOM   3152 O O     . GLY   B 1 169 ? 48.162  45.564 39.438 1   27.28 ? 150 GLY   B O     1 
ATOM   3153 N N     . ALA   B 1 170 ? 48.949  47.428 40.413 1   28.23 ? 151 ALA   B N     1 
ATOM   3154 C CA    . ALA   B 1 170 ? 50.065  46.711 41.038 1   29.8  ? 151 ALA   B CA    1 
ATOM   3155 C C     . ALA   B 1 170 ? 49.674  45.95  42.29  1   30.55 ? 151 ALA   B C     1 
ATOM   3156 O O     . ALA   B 1 170 ? 50.435  45.095 42.737 1   31.45 ? 151 ALA   B O     1 
ATOM   3157 C CB    . ALA   B 1 170 ? 51.22   47.656 41.341 1   29.87 ? 151 ALA   B CB    1 
ATOM   3158 N N     . VAL   B 1 171 ? 48.462  46.212 42.855 1   29.04 ? 152 VAL   B N     1 
ATOM   3159 C CA    . VAL   B 1 171 ? 48.079  45.596 44.101 1   29.97 ? 152 VAL   B CA    1 
ATOM   3160 C C     . VAL   B 1 171 ? 47.69   44.146 43.958 1   31.33 ? 152 VAL   B C     1 
ATOM   3161 O O     . VAL   B 1 171 ? 46.694  43.831 43.277 1   32.23 ? 152 VAL   B O     1 
ATOM   3162 C CB    . VAL   B 1 171 ? 46.935  46.407 44.786 1   30.49 ? 152 VAL   B CB    1 
ATOM   3163 C CG1   . VAL   B 1 171 ? 46.504  45.765 46.092 1   31.6  ? 152 VAL   B CG1   1 
ATOM   3164 C CG2   . VAL   B 1 171 ? 47.344  47.848 45.016 1   31.11 ? 152 VAL   B CG2   1 
ATOM   3165 N N     . PRO   B 1 172 ? 48.364  43.261 44.7   1   31.34 ? 153 PRO   B N     1 
ATOM   3166 C CA    . PRO   B 1 172 ? 47.97   41.862 44.669 1   32.6  ? 153 PRO   B CA    1 
ATOM   3167 C C     . PRO   B 1 172 ? 46.909  41.584 45.723 1   31.62 ? 153 PRO   B C     1 
ATOM   3168 O O     . PRO   B 1 172 ? 46.908  42.165 46.824 1   35.26 ? 153 PRO   B O     1 
ATOM   3169 C CB    . PRO   B 1 172 ? 49.26   41.133 44.981 1   33.41 ? 153 PRO   B CB    1 
ATOM   3170 C CG    . PRO   B 1 172 ? 50.002  42.08  45.934 1   33.18 ? 153 PRO   B CG    1 
ATOM   3171 C CD    . PRO   B 1 172 ? 49.569  43.48  45.538 1   31.05 ? 153 PRO   B CD    1 
ATOM   3172 N N     . LEU   B 1 173 ? 46.006  40.701 45.389 1   27.06 ? 154 LEU   B N     1 
ATOM   3173 C CA    . LEU   B 1 173 ? 45.009  40.236 46.337 1   25.46 ? 154 LEU   B CA    1 
ATOM   3174 C C     . LEU   B 1 173 ? 44.899  38.746 46.136 1   23.52 ? 154 LEU   B C     1 
ATOM   3175 O O     . LEU   B 1 173 ? 45.009  38.274 44.984 1   23.11 ? 154 LEU   B O     1 
ATOM   3176 C CB    . LEU   B 1 173 ? 43.612  40.828 46     1   25.56 ? 154 LEU   B CB    1 
ATOM   3177 C CG    . LEU   B 1 173 ? 43.273  42.211 46.426 1   28.03 ? 154 LEU   B CG    1 
ATOM   3178 C CD1   . LEU   B 1 173 ? 41.769  42.447 46.174 1   26.23 ? 154 LEU   B CD1   1 
ATOM   3179 C CD2   . LEU   B 1 173 ? 43.492  42.386 47.911 1   29.38 ? 154 LEU   B CD2   1 
ATOM   3180 N N     . PRO   B 1 174 ? 44.513  38.005 47.169 1   23.71 ? 155 PRO   B N     1 
ATOM   3181 C CA    . PRO   B 1 174 ? 44.209  36.592 46.972 1   24.29 ? 155 PRO   B CA    1 
ATOM   3182 C C     . PRO   B 1 174 ? 43.021  36.464 46.006 1   22.21 ? 155 PRO   B C     1 
ATOM   3183 O O     . PRO   B 1 174 ? 42.164  37.38  45.967 1   21.8  ? 155 PRO   B O     1 
ATOM   3184 C CB    . PRO   B 1 174 ? 43.723  36.131 48.362 1   26.01 ? 155 PRO   B CB    1 
ATOM   3185 C CG    . PRO   B 1 174 ? 44.209  37.137 49.312 1   27.77 ? 155 PRO   B CG    1 
ATOM   3186 C CD    . PRO   B 1 174 ? 44.287  38.427 48.564 1   25.19 ? 155 PRO   B CD    1 
ATOM   3187 N N     . PRO   B 1 175 ? 42.903  35.34  45.28  1   22.23 ? 156 PRO   B N     1 
ATOM   3188 C CA    . PRO   B 1 175 ? 41.736  35.119 44.415 1   22.68 ? 156 PRO   B CA    1 
ATOM   3189 C C     . PRO   B 1 175 ? 40.471  35.131 45.289 1   21.19 ? 156 PRO   B C     1 
ATOM   3190 O O     . PRO   B 1 175 ? 40.45   34.559 46.391 1   22.55 ? 156 PRO   B O     1 
ATOM   3191 C CB    . PRO   B 1 175 ? 41.983  33.728 43.818 1   24.56 ? 156 PRO   B CB    1 
ATOM   3192 C CG    . PRO   B 1 175 ? 43.518  33.548 43.889 1   26.11 ? 156 PRO   B CG    1 
ATOM   3193 C CD    . PRO   B 1 175 ? 43.843  34.196 45.24  1   23.48 ? 156 PRO   B CD    1 
ATOM   3194 N N     . ALA   B 1 176 ? 39.457  35.85  44.84  1   18.22 ? 157 ALA   B N     1 
ATOM   3195 C CA    . ALA   B 1 176 ? 38.243  35.984 45.613 1   17.72 ? 157 ALA   B CA    1 
ATOM   3196 C C     . ALA   B 1 176 ? 37.292  34.826 45.452 1   15.99 ? 157 ALA   B C     1 
ATOM   3197 O O     . ALA   B 1 176 ? 37.282  34.127 44.417 1   17.14 ? 157 ALA   B O     1 
ATOM   3198 C CB    . ALA   B 1 176 ? 37.545  37.296 45.204 1   18.02 ? 157 ALA   B CB    1 
ATOM   3199 N N     . ASP   B 1 177 ? 36.426  34.653 46.447 1   15.15 ? 158 ASP   B N     1 
ATOM   3200 C CA    . ASP   B 1 177 ? 35.343  33.68  46.332 1   17.12 ? 158 ASP   B CA    1 
ATOM   3201 C C     . ASP   B 1 177 ? 34.154  34.273 45.522 1   17.62 ? 158 ASP   B C     1 
ATOM   3202 O O     . ASP   B 1 177 ? 33.35   33.519 44.984 1   17.99 ? 158 ASP   B O     1 
ATOM   3203 C CB    . ASP   B 1 177 ? 34.878  33.287 47.733 1   18.75 ? 158 ASP   B CB    1 
ATOM   3204 C CG    . ASP   B 1 177 ? 36.038  32.698 48.493 1   22.89 ? 158 ASP   B CG    1 
ATOM   3205 O OD1   . ASP   B 1 177 ? 36.451  31.587 48.145 1   25.97 ? 158 ASP   B OD1   1 
ATOM   3206 O OD2   . ASP   B 1 177 ? 36.614  33.403 49.349 1   22.11 ? 158 ASP   B OD2   1 
ATOM   3207 N N     . CYS   B 1 178 ? 34.008  35.604 45.531 1   15.94 ? 159 CYS   B N     1 
ATOM   3208 C CA    . CYS   B 1 178 ? 32.944  36.257 44.787 1   15.26 ? 159 CYS   B CA    1 
ATOM   3209 C C     . CYS   B 1 178 ? 33.444  37.632 44.316 1   14.55 ? 159 CYS   B C     1 
ATOM   3210 O O     . CYS   B 1 178 ? 34.134  38.32  45.068 1   15.1  ? 159 CYS   B O     1 
ATOM   3211 C CB    . CYS   B 1 178 ? 31.737  36.432 45.695 1   16.03 ? 159 CYS   B CB    1 
ATOM   3212 S SG    . CYS   B 1 178 ? 30.31   37.298 44.939 1   17.67 ? 159 CYS   B SG    1 
ATOM   3213 N N     . VAL   B 1 179 ? 33.06   37.995 43.103 1   13.97 ? 160 VAL   B N     1 
ATOM   3214 C CA    . VAL   B 1 179 ? 33.239  39.347 42.577 1   13.57 ? 160 VAL   B CA    1 
ATOM   3215 C C     . VAL   B 1 179 ? 31.841  39.905 42.321 1   13.65 ? 160 VAL   B C     1 
ATOM   3216 O O     . VAL   B 1 179 ? 31.035  39.224 41.667 1   14.9  ? 160 VAL   B O     1 
ATOM   3217 C CB    . VAL   B 1 179 ? 34.083  39.378 41.308 1   15.36 ? 160 VAL   B CB    1 
ATOM   3218 C CG1   . VAL   B 1 179 ? 33.968  40.745 40.612 1   16.94 ? 160 VAL   B CG1   1 
ATOM   3219 C CG2   . VAL   B 1 179 ? 35.554  39.107 41.686 1   16.44 ? 160 VAL   B CG2   1 
ATOM   3220 N N     . LEU   B 1 180 ? 31.533  41.032 42.92  1   13.31 ? 161 LEU   B N     1 
ATOM   3221 C CA    . LEU   B 1 180 ? 30.216  41.688 42.808 1   13.78 ? 161 LEU   B CA    1 
ATOM   3222 C C     . LEU   B 1 180 ? 30.386  43.007 42.105 1   13.89 ? 161 LEU   B C     1 
ATOM   3223 O O     . LEU   B 1 180 ? 31.377  43.72  42.315 1   14.82 ? 161 LEU   B O     1 
ATOM   3224 C CB    . LEU   B 1 180 ? 29.783  42.013 44.236 1   14    ? 161 LEU   B CB    1 
ATOM   3225 C CG    . LEU   B 1 180 ? 28.506  42.851 44.42  1   14.37 ? 161 LEU   B CG    1 
ATOM   3226 C CD1   . LEU   B 1 180 ? 27.27   42.106 43.871 1   15.31 ? 161 LEU   B CD1   1 
ATOM   3227 C CD2   . LEU   B 1 180 ? 28.302  43.187 45.89  1   16.1  ? 161 LEU   B CD2   1 
ATOM   3228 N N     . SER   B 1 181 ? 29.42   43.355 41.24  1   13.3  ? 162 SER   B N     1 
ATOM   3229 C CA    . SER   B 1 181 ? 29.471  44.69  40.606 1   13.59 ? 162 SER   B CA    1 
ATOM   3230 C C     . SER   B 1 181 ? 28.091  45.156 40.332 1   13.98 ? 162 SER   B C     1 
ATOM   3231 O O     . SER   B 1 181 ? 27.362  44.508 39.574 1   14.28 ? 162 SER   B O     1 
ATOM   3232 C CB    . SER   B 1 181 ? 30.297  44.682 39.328 1   15.7  ? 162 SER   B CB    1 
ATOM   3233 O OG    . SER   B 1 181 ? 30.525  46.016 38.863 1   16.01 ? 162 SER   B OG    1 
ATOM   3234 N N     . THR   B 1 182 ? 27.68   46.268 40.982 1   14.04 ? 163 THR   B N     1 
ATOM   3235 C CA    . THR   B 1 182 ? 26.339  46.802 40.825 1   13.18 ? 163 THR   B CA    1 
ATOM   3236 C C     . THR   B 1 182 ? 26.412  48.139 40.078 1   12.86 ? 163 THR   B C     1 
ATOM   3237 O O     . THR   B 1 182 ? 27.146  49.059 40.458 1   13.66 ? 163 THR   B O     1 
ATOM   3238 C CB    . THR   B 1 182 ? 25.611  46.945 42.165 1   14.98 ? 163 THR   B CB    1 
ATOM   3239 O OG1   . THR   B 1 182 ? 26.355  47.782 43.06  1   16.07 ? 163 THR   B OG1   1 
ATOM   3240 C CG2   . THR   B 1 182 ? 25.424  45.586 42.838 1   15.61 ? 163 THR   B CG2   1 
ATOM   3241 N N     . LEU   B 1 183 ? 25.685  48.212 38.965 1   13.02 ? 164 LEU   B N     1 
ATOM   3242 C CA    . LEU   B 1 183 ? 25.49   49.491 38.243 1   14.01 ? 164 LEU   B CA    1 
ATOM   3243 C C     . LEU   B 1 183 ? 26.811  50.109 37.791 1   13.52 ? 164 LEU   B C     1 
ATOM   3244 O O     . LEU   B 1 183 ? 26.895  51.334 37.639 1   15.06 ? 164 LEU   B O     1 
ATOM   3245 C CB    . LEU   B 1 183 ? 24.658  50.47  39.082 1   14.2  ? 164 LEU   B CB    1 
ATOM   3246 C CG    . LEU   B 1 183 ? 23.177  50.034 39.245 1   15.46 ? 164 LEU   B CG    1 
ATOM   3247 C CD1   . LEU   B 1 183 ? 22.546  50.761 40.43  1   17.85 ? 164 LEU   B CD1   1 
ATOM   3248 C CD2   . LEU   B 1 183 ? 22.415  50.334 37.966 1   14.98 ? 164 LEU   B CD2   1 
ATOM   3249 N N     . CYS   B 1 184 ? 27.82   49.297 37.492 1   13.11 ? 165 CYS   B N     1 
ATOM   3250 C CA    . CYS   B 1 184 ? 29.12   49.757 37.045 1   13.51 ? 165 CYS   B CA    1 
ATOM   3251 C C     . CYS   B 1 184 ? 29.417  49.479 35.603 1   13.84 ? 165 CYS   B C     1 
ATOM   3252 O O     . CYS   B 1 184 ? 29.899  50.359 34.875 1   13.75 ? 165 CYS   B O     1 
ATOM   3253 C CB    . CYS   B 1 184 ? 30.19   49.18  37.957 1   14.21 ? 165 CYS   B CB    1 
ATOM   3254 S SG    . CYS   B 1 184 ? 31.914  49.443 37.372 1   15.23 ? 165 CYS   B SG    1 
ATOM   3255 N N     . LEU   B 1 185 ? 29.28   48.206 35.185 1   13.29 ? 166 LEU   B N     1 
ATOM   3256 C CA    . LEU   B 1 185 ? 29.82   47.828 33.871 1   14.15 ? 166 LEU   B CA    1 
ATOM   3257 C C     . LEU   B 1 185 ? 29.171  48.524 32.712 1   14.2  ? 166 LEU   B C     1 
ATOM   3258 O O     . LEU   B 1 185 ? 29.899  48.847 31.771 1   15.78 ? 166 LEU   B O     1 
ATOM   3259 C CB    . LEU   B 1 185 ? 29.831  46.312 33.713 1   14.37 ? 166 LEU   B CB    1 
ATOM   3260 C CG    . LEU   B 1 185 ? 30.625  45.576 34.756 1   16.07 ? 166 LEU   B CG    1 
ATOM   3261 C CD1   . LEU   B 1 185 ? 30.483  44.037 34.427 1   17.98 ? 166 LEU   B CD1   1 
ATOM   3262 C CD2   . LEU   B 1 185 ? 32.122  45.978 34.758 1   16.73 ? 166 LEU   B CD2   1 
ATOM   3263 N N     . ASP   B 1 186 ? 27.862  48.809 32.755 1   14.78 ? 167 ASP   B N     1 
ATOM   3264 C CA    . ASP   B 1 186 ? 27.256  49.55  31.628 1   17.23 ? 167 ASP   B CA    1 
ATOM   3265 C C     . ASP   B 1 186 ? 27.861  50.968 31.523 1   16.66 ? 167 ASP   B C     1 
ATOM   3266 O O     . ASP   B 1 186 ? 28.015  51.488 30.415 1   18.31 ? 167 ASP   B O     1 
ATOM   3267 C CB    . ASP   B 1 186 ? 25.745  49.795 31.884 1   19.45 ? 167 ASP   B CB    1 
ATOM   3268 C CG    . ASP   B 1 186 ? 24.764  48.689 31.796 1   27.73 ? 167 ASP   B CG    1 
ATOM   3269 O OD1   . ASP   B 1 186 ? 25.131  47.653 31.273 1   29.4  ? 167 ASP   B OD1   1 
ATOM   3270 O OD2   . ASP   B 1 186 ? 23.572  48.919 32.21  1   27.55 ? 167 ASP   B OD2   1 
ATOM   3271 N N     . ALA   B 1 187 ? 28.161  51.573 32.659 1   14.28 ? 168 ALA   B N     1 
ATOM   3272 C CA    . ALA   B 1 187 ? 28.71   52.948 32.661 1   14.48 ? 168 ALA   B CA    1 
ATOM   3273 C C     . ALA   B 1 187 ? 30.169  52.907 32.201 1   16.15 ? 168 ALA   B C     1 
ATOM   3274 O O     . ALA   B 1 187 ? 30.664  53.862 31.585 1   19.38 ? 168 ALA   B O     1 
ATOM   3275 C CB    . ALA   B 1 187 ? 28.62   53.466 34.073 1   14.64 ? 168 ALA   B CB    1 
ATOM   3276 N N     . ALA   B 1 188 ? 30.91   51.829 32.507 1   13.85 ? 169 ALA   B N     1 
ATOM   3277 C CA    . ALA   B 1 188 ? 32.369  51.799 32.257 1   15.12 ? 169 ALA   B CA    1 
ATOM   3278 C C     . ALA   B 1 188 ? 32.761  51.35  30.885 1   16.87 ? 169 ALA   B C     1 
ATOM   3279 O O     . ALA   B 1 188 ? 33.962  51.482 30.529 1   16.51 ? 169 ALA   B O     1 
ATOM   3280 C CB    . ALA   B 1 188 ? 32.996  50.828 33.271 1   15.42 ? 169 ALA   B CB    1 
ATOM   3281 N N     . CYS   B 1 189 ? 31.854  50.752 30.123 1   16.69 ? 170 CYS   B N     1 
ATOM   3282 C CA    . CYS   B 1 189 ? 32.272  50.11  28.873 1   17.52 ? 170 CYS   B CA    1 
ATOM   3283 C C     . CYS   B 1 189 ? 31.667  50.76  27.695 1   19.63 ? 170 CYS   B C     1 
ATOM   3284 O O     . CYS   B 1 189 ? 30.449  50.839 27.602 1   19.58 ? 170 CYS   B O     1 
ATOM   3285 C CB    . CYS   B 1 189 ? 31.908  48.619 28.928 1   18.1  ? 170 CYS   B CB    1 
ATOM   3286 S SG    . CYS   B 1 189 ? 32.647  47.716 30.277 1   18    ? 170 CYS   B SG    1 
ATOM   3287 N N     . PRO   B 1 190 ? 32.458  51.223 26.732 1   21.57 ? 171 PRO   B N     1 
ATOM   3288 C CA    . PRO   B 1 190 ? 31.854  51.984 25.615 1   23.23 ? 171 PRO   B CA    1 
ATOM   3289 C C     . PRO   B 1 190 ? 31.21   51.127 24.54  1   24.38 ? 171 PRO   B C     1 
ATOM   3290 O O     . PRO   B 1 190 ? 30.434  51.654 23.745 1   27.17 ? 171 PRO   B O     1 
ATOM   3291 C CB    . PRO   B 1 190 ? 33.039  52.793 25.055 1   25.34 ? 171 PRO   B CB    1 
ATOM   3292 C CG    . PRO   B 1 190 ? 34.015  52.858 26.222 1   26.85 ? 171 PRO   B CG    1 
ATOM   3293 C CD    . PRO   B 1 190 ? 33.911  51.429 26.802 1   23.25 ? 171 PRO   B CD    1 
ATOM   3294 N N     . ASP   B 1 191 ? 31.511  49.823 24.485 1   22.78 ? 172 ASP   B N     1 
ATOM   3295 C CA    . ASP   B 1 191 ? 30.966  48.934 23.477 1   23.6  ? 172 ASP   B CA    1 
ATOM   3296 C C     . ASP   B 1 191 ? 30.965  47.489 23.959 1   21.4  ? 172 ASP   B C     1 
ATOM   3297 O O     . ASP   B 1 191 ? 31.515  47.202 25.02  1   20.3  ? 172 ASP   B O     1 
ATOM   3298 C CB    . ASP   B 1 191 ? 31.736  49.082 22.14  1   25.92 ? 172 ASP   B CB    1 
ATOM   3299 C CG    . ASP   B 1 191 ? 33.226  48.938 22.307 1   32.43 ? 172 ASP   B CG    1 
ATOM   3300 O OD1   . ASP   B 1 191 ? 33.654  48.067 23.092 1   29.78 ? 172 ASP   B OD1   1 
ATOM   3301 O OD2   . ASP   B 1 191 ? 33.973  49.711 21.668 1   38.24 ? 172 ASP   B OD2   1 
ATOM   3302 N N     . LEU   B 1 192 ? 30.275  46.606 23.257 1   22.49 ? 173 LEU   B N     1 
ATOM   3303 C CA    . LEU   B 1 192 ? 30.143  45.235 23.665 1   21.69 ? 173 LEU   B CA    1 
ATOM   3304 C C     . LEU   B 1 192 ? 31.472  44.462 23.74  1   22.26 ? 173 LEU   B C     1 
ATOM   3305 O O     . LEU   B 1 192 ? 31.683  43.754 24.746 1   20.87 ? 173 LEU   B O     1 
ATOM   3306 C CB    . LEU   B 1 192 ? 29.112  44.505 22.788 1   22.43 ? 173 LEU   B CB    1 
ATOM   3307 C CG    . LEU   B 1 192 ? 28.733  43.146 23.171 1   25.67 ? 173 LEU   B CG    1 
ATOM   3308 C CD1   . LEU   B 1 192 ? 28.206  43.103 24.613 1   24.71 ? 173 LEU   B CD1   1 
ATOM   3309 C CD2   . LEU   B 1 192 ? 27.657  42.628 22.159 1   28.41 ? 173 LEU   B CD2   1 
ATOM   3310 N N     . PRO   B 1 193 ? 32.432  44.635 22.816 1   23.12 ? 174 PRO   B N     1 
ATOM   3311 C CA    . PRO   B 1 193 ? 33.735  43.958 23.003 1   22.28 ? 174 PRO   B CA    1 
ATOM   3312 C C     . PRO   B 1 193 ? 34.442  44.425 24.27  1   21.12 ? 174 PRO   B C     1 
ATOM   3313 O O     . PRO   B 1 193 ? 35.026  43.573 24.96  1   20.23 ? 174 PRO   B O     1 
ATOM   3314 C CB    . PRO   B 1 193 ? 34.515  44.309 21.726 1   24.14 ? 174 PRO   B CB    1 
ATOM   3315 C CG    . PRO   B 1 193 ? 33.408  44.575 20.695 1   25.98 ? 174 PRO   B CG    1 
ATOM   3316 C CD    . PRO   B 1 193 ? 32.397  45.358 21.53  1   25.37 ? 174 PRO   B CD    1 
ATOM   3317 N N     . THR   B 1 194 ? 34.335  45.703 24.651 1   19.93 ? 175 THR   B N     1 
ATOM   3318 C CA    . THR   B 1 194 ? 34.964  46.166 25.892 1   19.74 ? 175 THR   B CA    1 
ATOM   3319 C C     . THR   B 1 194 ? 34.235  45.546 27.089 1   16.79 ? 175 THR   B C     1 
ATOM   3320 O O     . THR   B 1 194 ? 34.873  45.208 28.102 1   16.85 ? 175 THR   B O     1 
ATOM   3321 C CB    . THR   B 1 194 ? 34.957  47.694 26.023 1   22.63 ? 175 THR   B CB    1 
ATOM   3322 O OG1   . THR   B 1 194 ? 35.674  48.217 24.902 1   27.5  ? 175 THR   B OG1   1 
ATOM   3323 C CG2   . THR   B 1 194 ? 35.632  48.154 27.34  1   23.36 ? 175 THR   B CG2   1 
ATOM   3324 N N     . TYR   B 1 195 ? 32.899  45.413 26.998 1   16.09 ? 176 TYR   B N     1 
ATOM   3325 C CA    . TYR   B 1 195 ? 32.127  44.808 28.096 1   15.14 ? 176 TYR   B CA    1 
ATOM   3326 C C     . TYR   B 1 195 ? 32.565  43.34  28.315 1   16.36 ? 176 TYR   B C     1 
ATOM   3327 O O     . TYR   B 1 195 ? 32.836  42.936 29.446 1   15.6  ? 176 TYR   B O     1 
ATOM   3328 C CB    . TYR   B 1 195 ? 30.658  44.89  27.698 1   16.02 ? 176 TYR   B CB    1 
ATOM   3329 C CG    . TYR   B 1 195 ? 29.724  44.45  28.781 1   15.57 ? 176 TYR   B CG    1 
ATOM   3330 C CD1   . TYR   B 1 195 ? 29.305  45.332 29.75  1   17.33 ? 176 TYR   B CD1   1 
ATOM   3331 C CD2   . TYR   B 1 195 ? 29.209  43.157 28.803 1   17.85 ? 176 TYR   B CD2   1 
ATOM   3332 C CE1   . TYR   B 1 195 ? 28.433  44.948 30.755 1   17.1  ? 176 TYR   B CE1   1 
ATOM   3333 C CE2   . TYR   B 1 195 ? 28.329  42.75  29.798 1   17.41 ? 176 TYR   B CE2   1 
ATOM   3334 C CZ    . TYR   B 1 195 ? 27.932  43.652 30.763 1   17.25 ? 176 TYR   B CZ    1 
ATOM   3335 O OH    . TYR   B 1 195 ? 27.044  43.261 31.728 1   19.39 ? 176 TYR   B OH    1 
ATOM   3336 N N     . CYS   B 1 196 ? 32.736  42.576 27.202 1   16.6  ? 177 CYS   B N     1 
ATOM   3337 C CA    . CYS   B 1 196 ? 33.214  41.212 27.345 1   17.24 ? 177 CYS   B CA    1 
ATOM   3338 C C     . CYS   B 1 196 ? 34.65   41.206 27.941 1   17.02 ? 177 CYS   B C     1 
ATOM   3339 O O     . CYS   B 1 196 ? 34.948  40.416 28.859 1   17.46 ? 177 CYS   B O     1 
ATOM   3340 C CB    . CYS   B 1 196 ? 33.176  40.497 26.002 1   18.64 ? 177 CYS   B CB    1 
ATOM   3341 S SG    . CYS   B 1 196 ? 33.626  38.767 26.153 1   22.31 ? 177 CYS   B SG    1 
ATOM   3342 N N     . ARG   B 1 197 ? 35.536  42.123 27.491 1   17.41 ? 178 ARG   B N     1 
ATOM   3343 C CA    . ARG   B 1 197 ? 36.88   42.157 28.059 1   17.84 ? 178 ARG   B CA    1 
ATOM   3344 C C     . ARG   B 1 197 ? 36.827  42.486 29.548 1   16.62 ? 178 ARG   B C     1 
ATOM   3345 O O     . ARG   B 1 197 ? 37.561  41.881 30.347 1   17.31 ? 178 ARG   B O     1 
ATOM   3346 C CB    . ARG   B 1 197 ? 37.742  43.194 27.344 1   23.32 ? 178 ARG   B CB    1 
ATOM   3347 C CG    . ARG   B 1 197 ? 38.074  42.816 25.94  1   30.1  ? 178 ARG   B CG    1 
ATOM   3348 C CD    . ARG   B 1 197 ? 39.26   43.623 25.432 1   35.56 ? 178 ARG   B CD    1 
ATOM   3349 N NE    . ARG   B 1 197 ? 39.033  45.063 25.542 1   36.77 ? 178 ARG   B NE    1 
ATOM   3350 C CZ    . ARG   B 1 197 ? 38.403  45.797 24.62  1   38.61 ? 178 ARG   B CZ    1 
ATOM   3351 N NH1   . ARG   B 1 197 ? 38.265  47.107 24.789 1   38.46 ? 178 ARG   B NH1   1 
ATOM   3352 N NH2   . ARG   B 1 197 ? 37.925  45.226 23.513 1   39.56 ? 178 ARG   B NH2   1 
ATOM   3353 N N     . ALA   B 1 198 ? 35.959  43.426 29.936 1   15.05 ? 179 ALA   B N     1 
ATOM   3354 C CA    . ALA   B 1 198 ? 35.863  43.797 31.348 1   15.34 ? 179 ALA   B CA    1 
ATOM   3355 C C     . ALA   B 1 198 ? 35.428  42.559 32.191 1   15.26 ? 179 ALA   B C     1 
ATOM   3356 O O     . ALA   B 1 198 ? 35.96   42.359 33.272 1   15.56 ? 179 ALA   B O     1 
ATOM   3357 C CB    . ALA   B 1 198 ? 34.867  44.934 31.52  1   15.53 ? 179 ALA   B CB    1 
ATOM   3358 N N     . LEU   B 1 199 ? 34.503  41.743 31.651 1   15.12 ? 180 LEU   B N     1 
ATOM   3359 C CA    . LEU   B 1 199 ? 34.093  40.524 32.396 1   15.38 ? 180 LEU   B CA    1 
ATOM   3360 C C     . LEU   B 1 199 ? 35.278  39.556 32.527 1   15.54 ? 180 LEU   B C     1 
ATOM   3361 O O     . LEU   B 1 199 ? 35.481  38.971 33.612 1   16.08 ? 180 LEU   B O     1 
ATOM   3362 C CB    . LEU   B 1 199 ? 32.958  39.838 31.636 1   15.66 ? 180 LEU   B CB    1 
ATOM   3363 C CG    . LEU   B 1 199 ? 31.636  40.595 31.695 1   16.09 ? 180 LEU   B CG    1 
ATOM   3364 C CD1   . LEU   B 1 199 ? 30.636  39.976 30.766 1   19.58 ? 180 LEU   B CD1   1 
ATOM   3365 C CD2   . LEU   B 1 199 ? 31.067  40.614 33.099 1   17.8  ? 180 LEU   B CD2   1 
ATOM   3366 N N     . ARG   B 1 200 ? 36.123  39.449 31.49  1   15.78 ? 181 ARG   B N     1 
ATOM   3367 C CA    . ARG   B 1 200 ? 37.342  38.631 31.628 1   16.47 ? 181 ARG   B CA    1 
ATOM   3368 C C     . ARG   B 1 200 ? 38.272  39.234 32.69  1   17.23 ? 181 ARG   B C     1 
ATOM   3369 O O     . ARG   B 1 200 ? 38.891  38.505 33.494 1   17.7  ? 181 ARG   B O     1 
ATOM   3370 C CB    . ARG   B 1 200 ? 38.086  38.526 30.299 1   17.85 ? 181 ARG   B CB    1 
ATOM   3371 C CG    . ARG   B 1 200 ? 37.294  37.88  29.196 1   19.12 ? 181 ARG   B CG    1 
ATOM   3372 C CD    . ARG   B 1 200 ? 38.22   37.583 28.022 1   21.01 ? 181 ARG   B CD    1 
ATOM   3373 N NE    . ARG   B 1 200 ? 37.527  37.424 26.738 1   26.89 ? 181 ARG   B NE    1 
ATOM   3374 C CZ    . ARG   B 1 200 ? 37.202  36.267 26.186 1   33.15 ? 181 ARG   B CZ    1 
ATOM   3375 N NH1   . ARG   B 1 200 ? 37.495  35.129 26.796 1   34.31 ? 181 ARG   B NH1   1 
ATOM   3376 N NH2   . ARG   B 1 200 ? 36.618  36.236 24.997 1   33.76 ? 181 ARG   B NH2   1 
ATOM   3377 N N     . ASN   B 1 201 ? 38.399  40.577 32.676 1   16.37 ? 182 ASN   B N     1 
ATOM   3378 C CA    . ASN   B 1 201 ? 39.306  41.211 33.634 1   16.64 ? 182 ASN   B CA    1 
ATOM   3379 C C     . ASN   B 1 201 ? 38.837  41.017 35.072 1   17.25 ? 182 ASN   B C     1 
ATOM   3380 O O     . ASN   B 1 201 ? 39.65   40.763 35.97  1   18.35 ? 182 ASN   B O     1 
ATOM   3381 C CB    . ASN   B 1 201 ? 39.44   42.696 33.299 1   17.35 ? 182 ASN   B CB    1 
ATOM   3382 C CG    . ASN   B 1 201 ? 40.045  42.924 31.924 1   17.32 ? 182 ASN   B CG    1 
ATOM   3383 O OD1   . ASN   B 1 201 ? 40.776  42.08  31.368 1   19.85 ? 182 ASN   B OD1   1 
ATOM   3384 N ND2   . ASN   B 1 201 ? 39.777  44.102 31.364 1   16.7  ? 182 ASN   B ND2   1 
ATOM   3385 N N     . LEU   B 1 202 ? 37.528  41.067 35.303 1   15.28 ? 183 LEU   B N     1 
ATOM   3386 C CA    . LEU   B 1 202 ? 36.991  40.774 36.644 1   16.41 ? 183 LEU   B CA    1 
ATOM   3387 C C     . LEU   B 1 202 ? 37.279  39.306 36.996 1   17.25 ? 183 LEU   B C     1 
ATOM   3388 O O     . LEU   B 1 202 ? 37.588  39.012 38.135 1   17.02 ? 183 LEU   B O     1 
ATOM   3389 C CB    . LEU   B 1 202 ? 35.494  41.024 36.705 1   16.86 ? 183 LEU   B CB    1 
ATOM   3390 C CG    . LEU   B 1 202 ? 35.057  42.443 37.104 1   18.81 ? 183 LEU   B CG    1 
ATOM   3391 C CD1   . LEU   B 1 202 ? 35.771  43.561 36.347 1   21.78 ? 183 LEU   B CD1   1 
ATOM   3392 C CD2   . LEU   B 1 202 ? 33.557  42.579 37.024 1   18.63 ? 183 LEU   B CD2   1 
ATOM   3393 N N     . GLY   B 1 203 ? 37.197  38.424 36.011 1   17.26 ? 184 GLY   B N     1 
ATOM   3394 C CA    . GLY   B 1 203 ? 37.473  36.996 36.237 1   17    ? 184 GLY   B CA    1 
ATOM   3395 C C     . GLY   B 1 203 ? 38.872  36.74  36.718 1   18.15 ? 184 GLY   B C     1 
ATOM   3396 O O     . GLY   B 1 203 ? 39.1    35.776 37.474 1   18.58 ? 184 GLY   B O     1 
ATOM   3397 N N     . SER   B 1 204 ? 39.827  37.623 36.329 1   17.64 ? 185 SER   B N     1 
ATOM   3398 C CA    . SER   B 1 204 ? 41.21   37.412 36.78  1   19.07 ? 185 SER   B CA    1 
ATOM   3399 C C     . SER   B 1 204 ? 41.317  37.565 38.317 1   17.95 ? 185 SER   B C     1 
ATOM   3400 O O     . SER   B 1 204 ? 42.328  37.172 38.908 1   20.05 ? 185 SER   B O     1 
ATOM   3401 C CB    . SER   B 1 204 ? 42.151  38.403 36.087 1   19.98 ? 185 SER   B CB    1 
ATOM   3402 O OG    . SER   B 1 204 ? 42.062  39.723 36.614 1   20.45 ? 185 SER   B OG    1 
ATOM   3403 N N     . LEU   B 1 205 ? 40.312  38.199 38.964 1   17.05 ? 186 LEU   B N     1 
ATOM   3404 C CA    . LEU   B 1 205 ? 40.337  38.381 40.42  1   16.82 ? 186 LEU   B CA    1 
ATOM   3405 C C     . LEU   B 1 205 ? 39.638  37.266 41.163 1   17.25 ? 186 LEU   B C     1 
ATOM   3406 O O     . LEU   B 1 205 ? 39.597  37.322 42.395 1   18.75 ? 186 LEU   B O     1 
ATOM   3407 C CB    . LEU   B 1 205 ? 39.554  39.69  40.731 1   18.05 ? 186 LEU   B CB    1 
ATOM   3408 C CG    . LEU   B 1 205 ? 40.13   40.913 40.041 1   19.12 ? 186 LEU   B CG    1 
ATOM   3409 C CD1   . LEU   B 1 205 ? 39.232  42.142 40.337 1   20.34 ? 186 LEU   B CD1   1 
ATOM   3410 C CD2   . LEU   B 1 205 ? 41.562  41.21  40.492 1   22.39 ? 186 LEU   B CD2   1 
ATOM   3411 N N     . LEU   B 1 206 ? 39.056  36.297 40.437 1   16.76 ? 187 LEU   B N     1 
ATOM   3412 C CA    . LEU   B 1 206 ? 38.15   35.323 41.017 1   17.51 ? 187 LEU   B CA    1 
ATOM   3413 C C     . LEU   B 1 206 ? 38.782  33.918 40.939 1   19.15 ? 187 LEU   B C     1 
ATOM   3414 O O     . LEU   B 1 206 ? 39.413  33.554 39.94  1   20.41 ? 187 LEU   B O     1 
ATOM   3415 C CB    . LEU   B 1 206 ? 36.907  35.281 40.085 1   20.63 ? 187 LEU   B CB    1 
ATOM   3416 C CG    . LEU   B 1 206 ? 35.551  35.479 40.565 1   25.27 ? 187 LEU   B CG    1 
ATOM   3417 C CD1   . LEU   B 1 206 ? 34.543  35.104 39.485 1   21    ? 187 LEU   B CD1   1 
ATOM   3418 C CD2   . LEU   B 1 206 ? 35.226  34.946 41.969 1   21.69 ? 187 LEU   B CD2   1 
ATOM   3419 N N     . LYS   B 1 207 ? 38.564  33.123 41.972 1   18.86 ? 188 LYS   B N     1 
ATOM   3420 C CA    . LYS   B 1 207 ? 39.002  31.73  41.961 1   19.46 ? 188 LYS   B CA    1 
ATOM   3421 C C     . LYS   B 1 207 ? 38.237  30.959 40.889 1   20.53 ? 188 LYS   B C     1 
ATOM   3422 O O     . LYS   B 1 207 ? 37.118  31.267 40.559 1   19.75 ? 188 LYS   B O     1 
ATOM   3423 C CB    . LYS   B 1 207 ? 38.817  31.083 43.375 1   22.32 ? 188 LYS   B CB    1 
ATOM   3424 C CG    . LYS   B 1 207 ? 37.394  30.865 43.792 1   28.79 ? 188 LYS   B CG    1 
ATOM   3425 C CD    . LYS   B 1 207 ? 37.245  30.29  45.193 1   32.61 ? 188 LYS   B CD    1 
ATOM   3426 C CE    . LYS   B 1 207 ? 35.766  30.061 45.496 1   36.5  ? 188 LYS   B CE    1 
ATOM   3427 N NZ    . LYS   B 1 207 ? 35.571  29.488 46.852 1   39.76 ? 188 LYS   B NZ    1 
ATOM   3428 N N     . PRO   B 1 208 ? 38.82   29.814 40.455 1   21.94 ? 189 PRO   B N     1 
ATOM   3429 C CA    . PRO   B 1 208 ? 38.068  28.899 39.594 1   22.01 ? 189 PRO   B CA    1 
ATOM   3430 C C     . PRO   B 1 208 ? 36.829  28.416 40.366 1   21.67 ? 189 PRO   B C     1 
ATOM   3431 O O     . PRO   B 1 208 ? 36.906  28.134 41.589 1   21.34 ? 189 PRO   B O     1 
ATOM   3432 C CB    . PRO   B 1 208 ? 39.042  27.722 39.362 1   24.64 ? 189 PRO   B CB    1 
ATOM   3433 C CG    . PRO   B 1 208 ? 40.327  28.211 39.675 1   24.98 ? 189 PRO   B CG    1 
ATOM   3434 C CD    . PRO   B 1 208 ? 40.164  29.284 40.753 1   23.6  ? 189 PRO   B CD    1 
ATOM   3435 N N     . GLY   B 1 209 ? 35.685  28.45  39.702 1   21.11 ? 190 GLY   B N     1 
ATOM   3436 C CA    . GLY   B 1 209 ? 34.447  28.088 40.36  1   22.26 ? 190 GLY   B CA    1 
ATOM   3437 C C     . GLY   B 1 209 ? 33.849  29.177 41.242 1   22.07 ? 190 GLY   B C     1 
ATOM   3438 O O     . GLY   B 1 209 ? 32.823  28.967 41.865 1   24.11 ? 190 GLY   B O     1 
ATOM   3439 N N     . GLY   B 1 210 ? 34.51   30.327 41.339 1   19.39 ? 191 GLY   B N     1 
ATOM   3440 C CA    . GLY   B 1 210 ? 34.025  31.452 42.127 1   18.46 ? 191 GLY   B CA    1 
ATOM   3441 C C     . GLY   B 1 210 ? 32.819  32.087 41.484 1   18.29 ? 191 GLY   B C     1 
ATOM   3442 O O     . GLY   B 1 210 ? 32.575  31.919 40.286 1   18.76 ? 191 GLY   B O     1 
ATOM   3443 N N     . PHE   B 1 211 ? 32.131  32.893 42.261 1   17.19 ? 192 PHE   B N     1 
ATOM   3444 C CA    . PHE   B 1 211 ? 30.881  33.489 41.796 1   17.24 ? 192 PHE   B CA    1 
ATOM   3445 C C     . PHE   B 1 211 ? 31.038  34.911 41.318 1   15.83 ? 192 PHE   B C     1 
ATOM   3446 O O     . PHE   B 1 211 ? 31.727  35.707 41.941 1   17.24 ? 192 PHE   B O     1 
ATOM   3447 C CB    . PHE   B 1 211 ? 29.853  33.49  42.931 1   20.24 ? 192 PHE   B CB    1 
ATOM   3448 C CG    . PHE   B 1 211 ? 29.276  32.121 43.226 1   24.42 ? 192 PHE   B CG    1 
ATOM   3449 C CD1   . PHE   B 1 211 ? 28.199  31.64  42.506 1   27.3  ? 192 PHE   B CD1   1 
ATOM   3450 C CD2   . PHE   B 1 211 ? 29.789  31.349 44.245 1   26.03 ? 192 PHE   B CD2   1 
ATOM   3451 C CE1   . PHE   B 1 211 ? 27.628  30.408 42.819 1   28.19 ? 192 PHE   B CE1   1 
ATOM   3452 C CE2   . PHE   B 1 211 ? 29.217  30.118 44.562 1   27.98 ? 192 PHE   B CE2   1 
ATOM   3453 C CZ    . PHE   B 1 211 ? 28.165  29.651 43.834 1   28.52 ? 192 PHE   B CZ    1 
ATOM   3454 N N     . LEU   B 1 212 ? 30.391  35.211 40.214 1   15.03 ? 193 LEU   B N     1 
ATOM   3455 C CA    . LEU   B 1 212 ? 30.319  36.577 39.656 1   14.63 ? 193 LEU   B CA    1 
ATOM   3456 C C     . LEU   B 1 212 ? 28.86   37.017 39.806 1   14.7  ? 193 LEU   B C     1 
ATOM   3457 O O     . LEU   B 1 212 ? 27.94   36.32  39.351 1   15.62 ? 193 LEU   B O     1 
ATOM   3458 C CB    . LEU   B 1 212 ? 30.653  36.541 38.191 1   15.29 ? 193 LEU   B CB    1 
ATOM   3459 C CG    . LEU   B 1 212 ? 30.604  37.9   37.487 1   17.17 ? 193 LEU   B CG    1 
ATOM   3460 C CD1   . LEU   B 1 212 ? 31.822  38.677 37.874 1   21.15 ? 193 LEU   B CD1   1 
ATOM   3461 C CD2   . LEU   B 1 212 ? 30.554  37.701 35.964 1   19.01 ? 193 LEU   B CD2   1 
ATOM   3462 N N     . VAL   B 1 213 ? 28.648  38.146 40.485 1   14.01 ? 194 VAL   B N     1 
ATOM   3463 C CA    . VAL   B 1 213 ? 27.298  38.688 40.723 1   13.81 ? 194 VAL   B CA    1 
ATOM   3464 C C     . VAL   B 1 213 ? 27.228  40.051 40.108 1   13.8  ? 194 VAL   B C     1 
ATOM   3465 O O     . VAL   B 1 213 ? 28.015  40.939 40.502 1   14.25 ? 194 VAL   B O     1 
ATOM   3466 C CB    . VAL   B 1 213 ? 26.969  38.731 42.224 1   14.69 ? 194 VAL   B CB    1 
ATOM   3467 C CG1   . VAL   B 1 213 ? 25.583  39.297 42.452 1   15.42 ? 194 VAL   B CG1   1 
ATOM   3468 C CG2   . VAL   B 1 213 ? 27.012  37.321 42.813 1   16.4  ? 194 VAL   B CG2   1 
ATOM   3469 N N     . ILE   B 1 214 ? 26.373  40.235 39.098 1   13.34 ? 195 ILE   B N     1 
ATOM   3470 C CA    . ILE   B 1 214 ? 26.265  41.518 38.395 1   13.31 ? 195 ILE   B CA    1 
ATOM   3471 C C     . ILE   B 1 214 ? 24.83   41.946 38.484 1   13.84 ? 195 ILE   B C     1 
ATOM   3472 O O     . ILE   B 1 214 ? 23.918  41.167 38.2   1   14.24 ? 195 ILE   B O     1 
ATOM   3473 C CB    . ILE   B 1 214 ? 26.7    41.426 36.923 1   14.57 ? 195 ILE   B CB    1 
ATOM   3474 C CG1   . ILE   B 1 214 ? 28.12   40.821 36.74  1   17.54 ? 195 ILE   B CG1   1 
ATOM   3475 C CG2   . ILE   B 1 214 ? 26.598  42.8   36.227 1   16.75 ? 195 ILE   B CG2   1 
ATOM   3476 C CD1   . ILE   B 1 214 ? 29.367  41.567 37.277 1   21.15 ? 195 ILE   B CD1   1 
ATOM   3477 N N     . MET   B 1 215 ? 24.58   43.221 38.749 1   13.65 ? 196 MET   B N     1 
ATOM   3478 C CA    . MET   B 1 215 ? 23.245  43.806 38.677 1   13.57 ? 196 MET   B CA    1 
ATOM   3479 C C     . MET   B 1 215 ? 23.407  45.113 37.933 1   14.07 ? 196 MET   B C     1 
ATOM   3480 O O     . MET   B 1 215 ? 24.376  45.86  38.234 1   15.16 ? 196 MET   B O     1 
ATOM   3481 C CB    . MET   B 1 215 ? 22.632  44.051 40.054 1   16.93 ? 196 MET   B CB    1 
ATOM   3482 C CG    . MET   B 1 215 ? 22.541  42.784 40.843 1   19.74 ? 196 MET   B CG    1 
ATOM   3483 S SD    . MET   B 1 215 ? 21.727  43.029 42.449 1   23.53 ? 196 MET   B SD    1 
ATOM   3484 C CE    . MET   B 1 215 ? 21.84   41.367 43.074 1   25.55 ? 196 MET   B CE    1 
ATOM   3485 N N     . ASP   B 1 216 ? 22.581  45.387 36.949 1   13.57 ? 197 ASP   B N     1 
ATOM   3486 C CA    . ASP   B 1 216 ? 22.782  46.646 36.169 1   13.52 ? 197 ASP   B CA    1 
ATOM   3487 C C     . ASP   B 1 216 ? 21.539  46.943 35.369 1   13.96 ? 197 ASP   B C     1 
ATOM   3488 O O     . ASP   B 1 216 ? 20.562  46.192 35.369 1   15.17 ? 197 ASP   B O     1 
ATOM   3489 C CB    . ASP   B 1 216 ? 23.981  46.504 35.212 1   14.1  ? 197 ASP   B CB    1 
ATOM   3490 C CG    . ASP   B 1 216 ? 24.848  47.694 35.031 1   15.82 ? 197 ASP   B CG    1 
ATOM   3491 O OD1   . ASP   B 1 216 ? 24.347  48.811 35.163 1   15.67 ? 197 ASP   B OD1   1 
ATOM   3492 O OD2   . ASP   B 1 216 ? 26.029  47.498 34.664 1   17.61 ? 197 ASP   B OD2   1 
ATOM   3493 N N     . ALA   B 1 217 ? 21.543  48.126 34.762 1   14.79 ? 198 ALA   B N     1 
ATOM   3494 C CA    . ALA   B 1 217 ? 20.415  48.56  33.963 1   15.01 ? 198 ALA   B CA    1 
ATOM   3495 C C     . ALA   B 1 217 ? 20.395  47.865 32.608 1   15.88 ? 198 ALA   B C     1 
ATOM   3496 O O     . ALA   B 1 217 ? 21.428  47.535 32.013 1   17.29 ? 198 ALA   B O     1 
ATOM   3497 C CB    . ALA   B 1 217 ? 20.553  50.082 33.746 1   16.32 ? 198 ALA   B CB    1 
ATOM   3498 N N     . LEU   B 1 218 ? 19.172  47.668 32.082 1   15.18 ? 199 LEU   B N     1 
ATOM   3499 C CA    . LEU   B 1 218 ? 19.025  47.166 30.712 1   15.65 ? 199 LEU   B CA    1 
ATOM   3500 C C     . LEU   B 1 218 ? 18.674  48.322 29.78  1   16.14 ? 199 LEU   B C     1 
ATOM   3501 O O     . LEU   B 1 218 ? 17.853  49.165 30.148 1   16.27 ? 199 LEU   B O     1 
ATOM   3502 C CB    . LEU   B 1 218 ? 17.871  46.096 30.634 1   15.6  ? 199 LEU   B CB    1 
ATOM   3503 C CG    . LEU   B 1 218 ? 18.207  44.777 31.318 1   16.89 ? 199 LEU   B CG    1 
ATOM   3504 C CD1   . LEU   B 1 218 ? 16.891  43.982 31.578 1   18.38 ? 199 LEU   B CD1   1 
ATOM   3505 C CD2   . LEU   B 1 218 ? 19.154  43.972 30.476 1   19.54 ? 199 LEU   B CD2   1 
ATOM   3506 N N     . LYS   B 1 219 ? 19.27   48.338 28.592 1   16.16 ? 200 LYS   B N     1 
ATOM   3507 C CA    . LYS   B 1 219 ? 18.925  49.236 27.505 1   17.64 ? 200 LYS   B CA    1 
ATOM   3508 C C     . LYS   B 1 219 ? 19.011  50.69  27.872 1   18.18 ? 200 LYS   B C     1 
ATOM   3509 O O     . LYS   B 1 219 ? 18.279  51.502 27.321 1   20.36 ? 200 LYS   B O     1 
ATOM   3510 C CB    . LYS   B 1 219 ? 17.548  48.896 26.923 1   19.3  ? 200 LYS   B CB    1 
ATOM   3511 C CG    . LYS   B 1 219 ? 17.532  47.458 26.368 1   22.48 ? 200 LYS   B CG    1 
ATOM   3512 C CD    . LYS   B 1 219 ? 16.194  47.113 25.736 1   30.22 ? 200 LYS   B CD    1 
ATOM   3513 C CE    . LYS   B 1 219 ? 16.282  45.758 25.095 1   38.27 ? 200 LYS   B CE    1 
ATOM   3514 N NZ    . LYS   B 1 219 ? 14.96   45.291 24.575 1   43.43 ? 200 LYS   B NZ    1 
ATOM   3515 N N     . SER   B 1 220 ? 19.927  51.059 28.745 1   16.37 ? 201 SER   B N     1 
ATOM   3516 C CA    . SER   B 1 220 ? 20.128  52.479 29.123 1   16.96 ? 201 SER   B CA    1 
ATOM   3517 C C     . SER   B 1 220 ? 21.282  53.028 28.311 1   15.69 ? 201 SER   B C     1 
ATOM   3518 O O     . SER   B 1 220 ? 22.36   52.415 28.273 1   16.22 ? 201 SER   B O     1 
ATOM   3519 C CB    . SER   B 1 220 ? 20.444  52.546 30.617 1   22.19 ? 201 SER   B CB    1 
ATOM   3520 O OG    . SER   B 1 220 ? 20.689  53.863 31.073 1   31.15 ? 201 SER   B OG    1 
ATOM   3521 N N     . SER   B 1 221 ? 21.092  54.198 27.691 1   16.26 ? 202 SER   B N     1 
ATOM   3522 C CA    . SER   B 1 221 ? 22.191  54.846 26.992 1   16.47 ? 202 SER   B CA    1 
ATOM   3523 C C     . SER   B 1 221 ? 22.737  56.054 27.745 1   15.89 ? 202 SER   B C     1 
ATOM   3524 O O     . SER   B 1 221 ? 23.786  56.587 27.341 1   17.5  ? 202 SER   B O     1 
ATOM   3525 C CB    . SER   B 1 221 ? 21.837  55.191 25.55  1   18.41 ? 202 SER   B CB    1 
ATOM   3526 O OG    . SER   B 1 221 ? 20.829  56.181 25.541 1   21.17 ? 202 SER   B OG    1 
ATOM   3527 N N     . TYR   B 1 222 ? 22.128  56.447 28.853 1   14.93 ? 203 TYR   B N     1 
ATOM   3528 C CA    . TYR   B 1 222 ? 22.692  57.465 29.721 1   16.16 ? 203 TYR   B CA    1 
ATOM   3529 C C     . TYR   B 1 222 ? 22.076  57.407 31.093 1   16.17 ? 203 TYR   B C     1 
ATOM   3530 O O     . TYR   B 1 222 ? 20.977  56.803 31.289 1   16.78 ? 203 TYR   B O     1 
ATOM   3531 C CB    . TYR   B 1 222 ? 22.542  58.887 29.119 1   16.91 ? 203 TYR   B CB    1 
ATOM   3532 C CG    . TYR   B 1 222 ? 21.104  59.335 29.109 1   18.98 ? 203 TYR   B CG    1 
ATOM   3533 C CD1   . TYR   B 1 222 ? 20.537  59.97  30.216 1   20.15 ? 203 TYR   B CD1   1 
ATOM   3534 C CD2   . TYR   B 1 222 ? 20.305  59.16  27.986 1   20.25 ? 203 TYR   B CD2   1 
ATOM   3535 C CE1   . TYR   B 1 222 ? 19.219  60.432 30.194 1   22.85 ? 203 TYR   B CE1   1 
ATOM   3536 C CE2   . TYR   B 1 222 ? 18.981  59.586 27.971 1   22.85 ? 203 TYR   B CE2   1 
ATOM   3537 C CZ    . TYR   B 1 222 ? 18.422  60.137 29.106 1   24.59 ? 203 TYR   B CZ    1 
ATOM   3538 O OH    . TYR   B 1 222 ? 17.129  60.607 29.055 1   27.46 ? 203 TYR   B OH    1 
ATOM   3539 N N     . TYR   B 1 223 ? 22.698  58.036 32.067 1   15.92 ? 204 TYR   B N     1 
ATOM   3540 C CA    . TYR   B 1 223 ? 22.09   58.306 33.356 1   15.83 ? 204 TYR   B CA    1 
ATOM   3541 C C     . TYR   B 1 223 ? 22.56   59.694 33.79  1   15.7  ? 204 TYR   B C     1 
ATOM   3542 O O     . TYR   B 1 223 ? 23.632  60.191 33.356 1   16.31 ? 204 TYR   B O     1 
ATOM   3543 C CB    . TYR   B 1 223 ? 22.352  57.215 34.405 1   15.74 ? 204 TYR   B CB    1 
ATOM   3544 C CG    . TYR   B 1 223 ? 23.788  57.09  34.856 1   14.91 ? 204 TYR   B CG    1 
ATOM   3545 C CD1   . TYR   B 1 223 ? 24.757  56.549 34.023 1   13.65 ? 204 TYR   B CD1   1 
ATOM   3546 C CD2   . TYR   B 1 223 ? 24.168  57.498 36.12  1   15.08 ? 204 TYR   B CD2   1 
ATOM   3547 C CE1   . TYR   B 1 223 ? 26.086  56.415 34.452 1   14.02 ? 204 TYR   B CE1   1 
ATOM   3548 C CE2   . TYR   B 1 223 ? 25.488  57.387 36.556 1   15.98 ? 204 TYR   B CE2   1 
ATOM   3549 C CZ    . TYR   B 1 223 ? 26.441  56.815 35.73  1   15.43 ? 204 TYR   B CZ    1 
ATOM   3550 O OH    . TYR   B 1 223 ? 27.744  56.741 36.188 1   16    ? 204 TYR   B OH    1 
ATOM   3551 N N     . MET   B 1 224 ? 21.784  60.309 34.667 1   16.67 ? 205 MET   B N     1 
ATOM   3552 C CA    . MET   B 1 224 ? 22.016  61.68  35.087 1   16.4  ? 205 MET   B CA    1 
ATOM   3553 C C     . MET   B 1 224 ? 22.343  61.79  36.555 1   16.06 ? 205 MET   B C     1 
ATOM   3554 O O     . MET   B 1 224 ? 21.79   61.028 37.377 1   17.07 ? 205 MET   B O     1 
ATOM   3555 C CB    . MET   B 1 224 ? 20.718  62.496 34.889 1   17.56 ? 205 MET   B CB    1 
ATOM   3556 C CG    . MET   B 1 224 ? 20.231  62.568 33.458 1   18.61 ? 205 MET   B CG    1 
ATOM   3557 S SD    . MET   B 1 224 ? 21.351  63.195 32.222 1   19.12 ? 205 MET   B SD    1 
ATOM   3558 C CE    . MET   B 1 224 ? 21.499  64.901 32.793 1   19.06 ? 205 MET   B CE    1 
ATOM   3559 N N     . ILE   B 1 225 ? 23.23   62.739 36.925 1   16.36 ? 206 ILE   B N     1 
ATOM   3560 C CA    . ILE   B 1 225 ? 23.399  63.084 38.317 1   17.44 ? 206 ILE   B CA    1 
ATOM   3561 C C     . ILE   B 1 225 ? 23.133  64.589 38.329 1   18.99 ? 206 ILE   B C     1 
ATOM   3562 O O     . ILE   B 1 225 ? 23.995  65.374 37.936 1   18.83 ? 206 ILE   B O     1 
ATOM   3563 C CB    . ILE   B 1 225 ? 24.8    62.766 38.855 1   18.17 ? 206 ILE   B CB    1 
ATOM   3564 C CG1   . ILE   B 1 225 ? 25.107  61.286 38.636 1   17.57 ? 206 ILE   B CG1   1 
ATOM   3565 C CG2   . ILE   B 1 225 ? 24.854  63.113 40.361 1   21.05 ? 206 ILE   B CG2   1 
ATOM   3566 C CD1   . ILE   B 1 225 ? 26.575  60.931 39.14  1   19.63 ? 206 ILE   B CD1   1 
ATOM   3567 N N     . GLY   B 1 226 ? 21.887  64.948 38.561 1   19.96 ? 207 GLY   B N     1 
ATOM   3568 C CA    . GLY   B 1 226 ? 21.471  66.34  38.418 1   20.86 ? 207 GLY   B CA    1 
ATOM   3569 C C     . GLY   B 1 226 ? 21.518  66.669 36.933 1   20.76 ? 207 GLY   B C     1 
ATOM   3570 O O     . GLY   B 1 226 ? 20.968  65.919 36.125 1   21.55 ? 207 GLY   B O     1 
ATOM   3571 N N     . GLU   B 1 227 ? 22.152  67.787 36.567 1   21.14 ? 208 GLU   B N     1 
ATOM   3572 C CA    . GLU   B 1 227 ? 22.275  68.152 35.163 1   21.12 ? 208 GLU   B CA    1 
ATOM   3573 C C     . GLU   B 1 227 ? 23.485  67.493 34.487 1   19.51 ? 208 GLU   B C     1 
ATOM   3574 O O     . GLU   B 1 227 ? 23.615  67.652 33.269 1   19.55 ? 208 GLU   B O     1 
ATOM   3575 C CB    . GLU   B 1 227 ? 22.428  69.668 35.07  1   23.02 ? 208 GLU   B CB    1 
ATOM   3576 C CG    . GLU   B 1 227 ? 21.147  70.398 35.458 1   25.92 ? 208 GLU   B CG    1 
ATOM   3577 C CD    . GLU   B 1 227 ? 21.278  71.883 35.209 1   33.05 ? 208 GLU   B CD    1 
ATOM   3578 O OE1   . GLU   B 1 227 ? 21.252  72.281 34.022 1   36.25 ? 208 GLU   B OE1   1 
ATOM   3579 O OE2   . GLU   B 1 227 ? 21.465  72.639 36.189 1   35.15 ? 208 GLU   B OE2   1 
ATOM   3580 N N     . GLN   B 1 228 ? 24.323  66.715 35.22  1   18.86 ? 209 GLN   B N     1 
ATOM   3581 C CA    . GLN   B 1 228 ? 25.468  66.05  34.585 1   18.15 ? 209 GLN   B CA    1 
ATOM   3582 C C     . GLN   B 1 228 ? 25.052  64.732 33.958 1   16.97 ? 209 GLN   B C     1 
ATOM   3583 O O     . GLN   B 1 228 ? 24.526  63.85  34.648 1   17.24 ? 209 GLN   B O     1 
ATOM   3584 C CB    . GLN   B 1 228 ? 26.553  65.77  35.632 1   18.22 ? 209 GLN   B CB    1 
ATOM   3585 C CG    . GLN   B 1 228 ? 27.802  65.078 35.07  1   17.13 ? 209 GLN   B CG    1 
ATOM   3586 C CD    . GLN   B 1 228 ? 28.558  65.934 34.094 1   17.99 ? 209 GLN   B CD    1 
ATOM   3587 O OE1   . GLN   B 1 228 ? 28.688  65.596 32.881 1   20.67 ? 209 GLN   B OE1   1 
ATOM   3588 N NE2   . GLN   B 1 228 ? 29.078  66.963 34.6   1   15.99 ? 209 GLN   B NE2   1 
ATOM   3589 N N     . LYS   B 1 229 ? 25.286  64.606 32.659 1   16.4  ? 210 LYS   B N     1 
ATOM   3590 C CA    . LYS   B 1 229 ? 25.004  63.371 31.923 1   16.19 ? 210 LYS   B CA    1 
ATOM   3591 C C     . LYS   B 1 229 ? 26.233  62.477 31.903 1   15.85 ? 210 LYS   B C     1 
ATOM   3592 O O     . LYS   B 1 229 ? 27.347  62.965 31.699 1   16.53 ? 210 LYS   B O     1 
ATOM   3593 C CB    . LYS   B 1 229 ? 24.601  63.698 30.47  1   17.44 ? 210 LYS   B CB    1 
ATOM   3594 C CG    . LYS   B 1 229 ? 24.175  62.482 29.608 1   18.07 ? 210 LYS   B CG    1 
ATOM   3595 C CD    . LYS   B 1 229 ? 23.602  63.019 28.302 1   24.32 ? 210 LYS   B CD    1 
ATOM   3596 C CE    . LYS   B 1 229 ? 23.076  62.042 27.315 1   28.6  ? 210 LYS   B CE    1 
ATOM   3597 N NZ    . LYS   B 1 229 ? 22.257  62.756 26.256 1   28.42 ? 210 LYS   B NZ    1 
ATOM   3598 N N     . PHE   B 1 230 ? 26      61.166 32.026 1   15.08 ? 211 PHE   B N     1 
ATOM   3599 C CA    . PHE   B 1 230 ? 27.033  60.164 31.863 1   15.89 ? 211 PHE   B CA    1 
ATOM   3600 C C     . PHE   B 1 230 ? 26.494  59.133 30.878 1   14.85 ? 211 PHE   B C     1 
ATOM   3601 O O     . PHE   B 1 230 ? 25.309  58.752 30.946 1   16.01 ? 211 PHE   B O     1 
ATOM   3602 C CB    . PHE   B 1 230 ? 27.295  59.405 33.175 1   16.05 ? 211 PHE   B CB    1 
ATOM   3603 C CG    . PHE   B 1 230 ? 28.045  60.237 34.186 1   16.38 ? 211 PHE   B CG    1 
ATOM   3604 C CD1   . PHE   B 1 230 ? 29.425  60.258 34.197 1   17.51 ? 211 PHE   B CD1   1 
ATOM   3605 C CD2   . PHE   B 1 230 ? 27.36   61.038 35.085 1   19.41 ? 211 PHE   B CD2   1 
ATOM   3606 C CE1   . PHE   B 1 230 ? 30.104  61.144 35.066 1   20.52 ? 211 PHE   B CE1   1 
ATOM   3607 C CE2   . PHE   B 1 230 ? 28.045  61.857 35.965 1   20.74 ? 211 PHE   B CE2   1 
ATOM   3608 C CZ    . PHE   B 1 230 ? 29.391  61.881 35.95  1   19.9  ? 211 PHE   B CZ    1 
ATOM   3609 N N     . SER   B 1 231 ? 27.335  58.646 29.987 1   15.31 ? 212 SER   B N     1 
ATOM   3610 C CA    . SER   B 1 231 ? 26.951  57.605 29.037 1   15.48 ? 212 SER   B CA    1 
ATOM   3611 C C     . SER   B 1 231 ? 26.743  56.278 29.727 1   15.17 ? 212 SER   B C     1 
ATOM   3612 O O     . SER   B 1 231 ? 27.288  56.005 30.794 1   14.8  ? 212 SER   B O     1 
ATOM   3613 C CB    . SER   B 1 231 ? 28.052  57.408 28.001 1   17.76 ? 212 SER   B CB    1 
ATOM   3614 O OG    . SER   B 1 231 ? 28.308  58.609 27.308 1   24.06 ? 212 SER   B OG    1 
ATOM   3615 N N     . SER   B 1 232 ? 25.931  55.425 29.061 1   14.46 ? 213 SER   B N     1 
ATOM   3616 C CA    . SER   B 1 232 ? 25.788  54.029 29.495 1   14.99 ? 213 SER   B CA    1 
ATOM   3617 C C     . SER   B 1 232 ? 25.716  53.189 28.214 1   15.84 ? 213 SER   B C     1 
ATOM   3618 O O     . SER   B 1 232 ? 25.22   53.634 27.173 1   15.56 ? 213 SER   B O     1 
ATOM   3619 C CB    . SER   B 1 232 ? 24.503  53.871 30.305 1   17.82 ? 213 SER   B CB    1 
ATOM   3620 O OG    . SER   B 1 232 ? 24.238  52.502 30.613 1   20.65 ? 213 SER   B OG    1 
ATOM   3621 N N     . LEU   B 1 233 ? 26.182  51.935 28.318 1   15.27 ? 214 LEU   B N     1 
ATOM   3622 C CA    . LEU   B 1 233 ? 26.084  51.006 27.172 1   16.28 ? 214 LEU   B CA    1 
ATOM   3623 C C     . LEU   B 1 233 ? 24.712  50.366 27.178 1   15.96 ? 214 LEU   B C     1 
ATOM   3624 O O     . LEU   B 1 233 ? 24.348  49.687 28.172 1   16.26 ? 214 LEU   B O     1 
ATOM   3625 C CB    . LEU   B 1 233 ? 27.162  49.927 27.351 1   16.69 ? 214 LEU   B CB    1 
ATOM   3626 C CG    . LEU   B 1 233 ? 27.265  48.912 26.202 1   19.19 ? 214 LEU   B CG    1 
ATOM   3627 C CD1   . LEU   B 1 233 ? 27.642  49.557 24.85  1   20.64 ? 214 LEU   B CD1   1 
ATOM   3628 C CD2   . LEU   B 1 233 ? 28.302  47.785 26.595 1   19.06 ? 214 LEU   B CD2   1 
ATOM   3629 N N     . PRO   B 1 234 ? 23.908  50.534 26.122 1   16.86 ? 215 PRO   B N     1 
ATOM   3630 C CA    . PRO   B 1 234 ? 22.515  50.067 26.196 1   18.73 ? 215 PRO   B CA    1 
ATOM   3631 C C     . PRO   B 1 234 ? 22.298  48.584 25.84  1   21.68 ? 215 PRO   B C     1 
ATOM   3632 O O     . PRO   B 1 234 ? 21.529  48.299 24.903 1   26.79 ? 215 PRO   B O     1 
ATOM   3633 C CB    . PRO   B 1 234 ? 21.8    51.003 25.215 1   18.74 ? 215 PRO   B CB    1 
ATOM   3634 C CG    . PRO   B 1 234 ? 22.812  51.278 24.188 1   18.31 ? 215 PRO   B CG    1 
ATOM   3635 C CD    . PRO   B 1 234 ? 24.137  51.392 24.929 1   16.99 ? 215 PRO   B CD    1 
ATOM   3636 N N     . LEU   B 1 235 ? 22.692  47.708 26.707 1   19.34 ? 216 LEU   B N     1 
ATOM   3637 C CA    . LEU   B 1 235 ? 22.556  46.259 26.443 1   18.47 ? 216 LEU   B CA    1 
ATOM   3638 C C     . LEU   B 1 235 ? 21.265  45.68  26.834 1   18.68 ? 216 LEU   B C     1 
ATOM   3639 O O     . LEU   B 1 235 ? 20.701  45.978 27.886 1   19.67 ? 216 LEU   B O     1 
ATOM   3640 C CB    . LEU   B 1 235 ? 23.649  45.502 27.209 1   19.3  ? 216 LEU   B CB    1 
ATOM   3641 C CG    . LEU   B 1 235 ? 25.12   45.825 26.863 1   20.72 ? 216 LEU   B CG    1 
ATOM   3642 C CD1   . LEU   B 1 235 ? 26.083  44.879 27.582 1   24.29 ? 216 LEU   B CD1   1 
ATOM   3643 C CD2   . LEU   B 1 235 ? 25.374  45.796 25.33  1   22.34 ? 216 LEU   B CD2   1 
ATOM   3644 N N     . GLY   B 1 236 ? 20.813  44.744 26.015 1   17.95 ? 217 GLY   B N     1 
ATOM   3645 C CA    . GLY   B 1 236 ? 19.656  43.924 26.336 1   18.95 ? 217 GLY   B CA    1 
ATOM   3646 C C     . GLY   B 1 236 ? 20.088  42.626 27.016 1   18.4  ? 217 GLY   B C     1 
ATOM   3647 O O     . GLY   B 1 236 ? 21.29   42.291 27.074 1   18.05 ? 217 GLY   B O     1 
ATOM   3648 N N     . ARG   B 1 237 ? 19.134  41.884 27.569 1   18.38 ? 218 ARG   B N     1 
ATOM   3649 C CA    . ARG   B 1 237 ? 19.437  40.698 28.33  1   18.93 ? 218 ARG   B CA    1 
ATOM   3650 C C     . ARG   B 1 237 ? 20.211  39.662 27.506 1   17.62 ? 218 ARG   B C     1 
ATOM   3651 O O     . ARG   B 1 237 ? 21.082  38.97  28.049 1   18.22 ? 218 ARG   B O     1 
ATOM   3652 C CB    . ARG   B 1 237 ? 18.19   40.1   28.998 1   22.11 ? 218 ARG   B CB    1 
ATOM   3653 C CG    . ARG   B 1 237 ? 17.188  39.611 28.025 1   28.24 ? 218 ARG   B CG    1 
ATOM   3654 C CD    . ARG   B 1 237 ? 16.171  38.668 28.671 1   36.13 ? 218 ARG   B CD    1 
ATOM   3655 N NE    . ARG   B 1 237 ? 16.826  37.48  29.234 1   41.4  ? 218 ARG   B NE    1 
ATOM   3656 C CZ    . ARG   B 1 237 ? 16.268  36.692 30.136 1   39.83 ? 218 ARG   B CZ    1 
ATOM   3657 N NH1   . ARG   B 1 237 ? 15.057  36.965 30.601 1   43.95 ? 218 ARG   B NH1   1 
ATOM   3658 N NH2   . ARG   B 1 237 ? 16.936  35.646 30.621 1   36.62 ? 218 ARG   B NH2   1 
ATOM   3659 N N     . GLU   B 1 238 ? 19.899  39.534 26.214 1   18.83 ? 219 GLU   B N     1 
ATOM   3660 C CA    . GLU   B 1 238 ? 20.575  38.504 25.404 1   18.91 ? 219 GLU   B CA    1 
ATOM   3661 C C     . GLU   B 1 238 ? 22.053  38.819 25.283 1   18.13 ? 219 GLU   B C     1 
ATOM   3662 O O     . GLU   B 1 238 ? 22.901  37.919 25.39  1   18.03 ? 219 GLU   B O     1 
ATOM   3663 C CB    . GLU   B 1 238 ? 19.903  38.409 24.028 1   21.94 ? 219 GLU   B CB    1 
ATOM   3664 C CG    . GLU   B 1 238 ? 18.445  37.918 24.094 1   26.3  ? 219 GLU   B CG    1 
ATOM   3665 C CD    . GLU   B 1 238 ? 17.379  38.954 24.461 1   39.4  ? 219 GLU   B CD    1 
ATOM   3666 O OE1   . GLU   B 1 238 ? 17.686  40.163 24.64  1   38.35 ? 219 GLU   B OE1   1 
ATOM   3667 O OE2   . GLU   B 1 238 ? 16.2    38.529 24.541 1   46.64 ? 219 GLU   B OE2   1 
ATOM   3668 N N     . ALA   B 1 239 ? 22.375  40.092 25.031 1   17.88 ? 220 ALA   B N     1 
ATOM   3669 C CA    . ALA   B 1 239 ? 23.795  40.46  24.884 1   17.79 ? 220 ALA   B CA    1 
ATOM   3670 C C     . ALA   B 1 239 ? 24.548  40.317 26.196 1   16.55 ? 220 ALA   B C     1 
ATOM   3671 O O     . ALA   B 1 239 ? 25.745  39.925 26.178 1   15.69 ? 220 ALA   B O     1 
ATOM   3672 C CB    . ALA   B 1 239 ? 23.908  41.875 24.388 1   19.2  ? 220 ALA   B CB    1 
ATOM   3673 N N     . VAL   B 1 240 ? 23.926  40.615 27.345 1   15.58 ? 221 VAL   B N     1 
ATOM   3674 C CA    . VAL   B 1 240 ? 24.591  40.441 28.631 1   15.93 ? 221 VAL   B CA    1 
ATOM   3675 C C     . VAL   B 1 240 ? 24.916  38.951 28.859 1   16.6  ? 221 VAL   B C     1 
ATOM   3676 O O     . VAL   B 1 240 ? 26.067  38.594 29.137 1   15.97 ? 221 VAL   B O     1 
ATOM   3677 C CB    . VAL   B 1 240 ? 23.731  40.96  29.801 1   16.55 ? 221 VAL   B CB    1 
ATOM   3678 C CG1   . VAL   B 1 240 ? 24.343  40.6   31.147 1   16.28 ? 221 VAL   B CG1   1 
ATOM   3679 C CG2   . VAL   B 1 240 ? 23.492  42.464 29.695 1   17.44 ? 221 VAL   B CG2   1 
ATOM   3680 N N     . GLU   B 1 241 ? 23.92   38.089 28.62  1   16.17 ? 222 GLU   B N     1 
ATOM   3681 C CA    . GLU   B 1 241 ? 24.163  36.653 28.858 1   17.23 ? 222 GLU   B CA    1 
ATOM   3682 C C     . GLU   B 1 241 ? 25.207  36.137 27.883 1   17.06 ? 222 GLU   B C     1 
ATOM   3683 O O     . GLU   B 1 241 ? 26.103  35.341 28.309 1   19.25 ? 222 GLU   B O     1 
ATOM   3684 C CB    . GLU   B 1 241 ? 22.861  35.923 28.572 1   21.5  ? 222 GLU   B CB    1 
ATOM   3685 C CG    . GLU   B 1 241 ? 21.807  36.046 29.625 1   30.99 ? 222 GLU   B CG    1 
ATOM   3686 C CD    . GLU   B 1 241 ? 20.437  35.63  29.104 1   42.77 ? 222 GLU   B CD    1 
ATOM   3687 O OE1   . GLU   B 1 241 ? 20.316  34.515 28.544 1   42.12 ? 222 GLU   B OE1   1 
ATOM   3688 O OE2   . GLU   B 1 241 ? 19.498  36.453 29.205 1   45.68 ? 222 GLU   B OE2   1 
ATOM   3689 N N     . ALA   B 1 242 ? 25.158  36.558 26.608 1   17.09 ? 223 ALA   B N     1 
ATOM   3690 C CA    . ALA   B 1 242 ? 26.155  36.084 25.641 1   18.41 ? 223 ALA   B CA    1 
ATOM   3691 C C     . ALA   B 1 242 ? 27.553  36.551 26.048 1   17.63 ? 223 ALA   B C     1 
ATOM   3692 O O     . ALA   B 1 242 ? 28.514  35.77  25.922 1   18.1  ? 223 ALA   B O     1 
ATOM   3693 C CB    . ALA   B 1 242 ? 25.837  36.58  24.252 1   20.61 ? 223 ALA   B CB    1 
ATOM   3694 N N     . ALA   B 1 243 ? 27.699  37.775 26.564 1   16.1  ? 224 ALA   B N     1 
ATOM   3695 C CA    . ALA   B 1 243 ? 29.041  38.277 26.904 1   16.27 ? 224 ALA   B CA    1 
ATOM   3696 C C     . ALA   B 1 243 ? 29.595  37.503 28.116 1   16.52 ? 224 ALA   B C     1 
ATOM   3697 O O     . ALA   B 1 243 ? 30.798  37.191 28.171 1   16.25 ? 224 ALA   B O     1 
ATOM   3698 C CB    . ALA   B 1 243 ? 28.938  39.762 27.259 1   16.74 ? 224 ALA   B CB    1 
ATOM   3699 N N     . VAL   B 1 244 ? 28.741  37.128 29.072 1   16.46 ? 225 VAL   B N     1 
ATOM   3700 C CA    . VAL   B 1 244 ? 29.169  36.364 30.244 1   15.85 ? 225 VAL   B CA    1 
ATOM   3701 C C     . VAL   B 1 244 ? 29.643  34.977 29.811 1   16.24 ? 225 VAL   B C     1 
ATOM   3702 O O     . VAL   B 1 244 ? 30.682  34.54  30.293 1   16.99 ? 225 VAL   B O     1 
ATOM   3703 C CB    . VAL   B 1 244 ? 28.007  36.309 31.256 1   17.92 ? 225 VAL   B CB    1 
ATOM   3704 C CG1   . VAL   B 1 244 ? 28.332  35.372 32.393 1   19.17 ? 225 VAL   B CG1   1 
ATOM   3705 C CG2   . VAL   B 1 244 ? 27.757  37.723 31.826 1   17.93 ? 225 VAL   B CG2   1 
ATOM   3706 N N     . LYS   B 1 245 ? 28.915  34.341 28.906 1   16.21 ? 226 LYS   B N     1 
ATOM   3707 C CA    . LYS   B 1 245 ? 29.365  33.003 28.414 1   16.96 ? 226 LYS   B CA    1 
ATOM   3708 C C     . LYS   B 1 245 ? 30.659  33.166 27.601 1   17.12 ? 226 LYS   B C     1 
ATOM   3709 O O     . LYS   B 1 245 ? 31.553  32.28  27.67  1   18.39 ? 226 LYS   B O     1 
ATOM   3710 C CB    . LYS   B 1 245 ? 28.276  32.348 27.567 1   19.99 ? 226 LYS   B CB    1 
ATOM   3711 C CG    . LYS   B 1 245 ? 27.051  31.975 28.411 1   23.27 ? 226 LYS   B CG    1 
ATOM   3712 C CD    . LYS   B 1 245 ? 25.952  31.419 27.526 1   29.15 ? 226 LYS   B CD    1 
ATOM   3713 C CE    . LYS   B 1 245 ? 24.618  31.504 28.221 1   38.32 ? 226 LYS   B CE    1 
ATOM   3714 N NZ    . LYS   B 1 245 ? 24.322  30.266 29.01  1   41.15 ? 226 LYS   B NZ    1 
ATOM   3715 N N     . GLU   B 1 246 ? 30.761  34.212 26.798 1   17.29 ? 227 GLU   B N     1 
ATOM   3716 C CA    . GLU   B 1 246 ? 31.976  34.418 25.99  1   18.05 ? 227 GLU   B CA    1 
ATOM   3717 C C     . GLU   B 1 246 ? 33.18   34.67  26.88  1   17.14 ? 227 GLU   B C     1 
ATOM   3718 O O     . GLU   B 1 246 ? 34.282  34.181 26.568 1   17.91 ? 227 GLU   B O     1 
ATOM   3719 C CB    . GLU   B 1 246 ? 31.729  35.586 25.026 1   18.56 ? 227 GLU   B CB    1 
ATOM   3720 C CG    . GLU   B 1 246 ? 32.868  35.883 24.061 1   22.28 ? 227 GLU   B CG    1 
ATOM   3721 C CD    . GLU   B 1 246 ? 32.584  37.073 23.158 1   29.16 ? 227 GLU   B CD    1 
ATOM   3722 O OE1   . GLU   B 1 246 ? 31.418  37.543 23.142 1   31.23 ? 227 GLU   B OE1   1 
ATOM   3723 O OE2   . GLU   B 1 246 ? 33.516  37.546 22.465 1   31.6  ? 227 GLU   B OE2   1 
ATOM   3724 N N     . ALA   B 1 247 ? 32.989  35.321 28.058 1   16.65 ? 228 ALA   B N     1 
ATOM   3725 C CA    . ALA   B 1 247 ? 34.069  35.64  28.976 1   17.12 ? 228 ALA   B CA    1 
ATOM   3726 C C     . ALA   B 1 247 ? 34.494  34.469 29.857 1   18.19 ? 228 ALA   B C     1 
ATOM   3727 O O     . ALA   B 1 247 ? 35.364  34.666 30.704 1   18.75 ? 228 ALA   B O     1 
ATOM   3728 C CB    . ALA   B 1 247 ? 33.716  36.886 29.834 1   17.85 ? 228 ALA   B CB    1 
ATOM   3729 N N     . GLY   B 1 248 ? 33.849  33.311 29.712 1   18.2  ? 229 GLY   B N     1 
ATOM   3730 C CA    . GLY   B 1 248 ? 34.3    32.111 30.411 1   19.51 ? 229 GLY   B CA    1 
ATOM   3731 C C     . GLY   B 1 248 ? 33.603  31.811 31.71  1   18.06 ? 229 GLY   B C     1 
ATOM   3732 O O     . GLY   B 1 248 ? 34.209  31.203 32.613 1   18.67 ? 229 GLY   B O     1 
ATOM   3733 N N     . TYR   B 1 249 ? 32.293  32.149 31.775 1   17.34 ? 230 TYR   B N     1 
ATOM   3734 C CA    . TYR   B 1 249 ? 31.531  31.819 32.961 1   16.75 ? 230 TYR   B CA    1 
ATOM   3735 C C     . TYR   B 1 249 ? 30.352  30.92  32.553 1   17.24 ? 230 TYR   B C     1 
ATOM   3736 O O     . TYR   B 1 249 ? 29.976  30.887 31.388 1   19.39 ? 230 TYR   B O     1 
ATOM   3737 C CB    . TYR   B 1 249 ? 30.918  33.09  33.596 1   15.66 ? 230 TYR   B CB    1 
ATOM   3738 C CG    . TYR   B 1 249 ? 31.963  34.082 34.034 1   14.59 ? 230 TYR   B CG    1 
ATOM   3739 C CD1   . TYR   B 1 249 ? 32.392  35.087 33.171 1   15.26 ? 230 TYR   B CD1   1 
ATOM   3740 C CD2   . TYR   B 1 249 ? 32.368  34.147 35.36  1   14.82 ? 230 TYR   B CD2   1 
ATOM   3741 C CE1   . TYR   B 1 249 ? 33.301  36.054 33.589 1   15.45 ? 230 TYR   B CE1   1 
ATOM   3742 C CE2   . TYR   B 1 249 ? 33.261  35.112 35.791 1   15.59 ? 230 TYR   B CE2   1 
ATOM   3743 C CZ    . TYR   B 1 249 ? 33.731  36.054 34.892 1   16.28 ? 230 TYR   B CZ    1 
ATOM   3744 O OH    . TYR   B 1 249 ? 34.582  37.055 35.346 1   17.11 ? 230 TYR   B OH    1 
ATOM   3745 N N     . THR   B 1 250 ? 29.776  30.248 33.502 1   16.11 ? 231 THR   B N     1 
ATOM   3746 C CA    . THR   B 1 250 ? 28.487  29.559 33.311 1   17.58 ? 231 THR   B CA    1 
ATOM   3747 C C     . THR   B 1 250 ? 27.41   30.281 34.085 1   18.42 ? 231 THR   B C     1 
ATOM   3748 O O     . THR   B 1 250 ? 27.655  30.691 35.221 1   22.39 ? 231 THR   B O     1 
ATOM   3749 C CB    . THR   B 1 250 ? 28.55   28.108 33.798 1   21.59 ? 231 THR   B CB    1 
ATOM   3750 O OG1   . THR   B 1 250 ? 28.879  28.075 35.192 1   23.51 ? 231 THR   B OG1   1 
ATOM   3751 C CG2   . THR   B 1 250 ? 29.592  27.331 33.091 1   23.59 ? 231 THR   B CG2   1 
ATOM   3752 N N     . ILE   B 1 251 ? 26.25   30.492 33.486 1   18.06 ? 232 ILE   B N     1 
ATOM   3753 C CA    . ILE   B 1 251 ? 25.181  31.238 34.143 1   18.79 ? 232 ILE   B CA    1 
ATOM   3754 C C     . ILE   B 1 251 ? 24.41   30.336 35.09  1   17.52 ? 232 ILE   B C     1 
ATOM   3755 O O     . ILE   B 1 251 ? 24.013  29.25  34.668 1   19.73 ? 232 ILE   B O     1 
ATOM   3756 C CB    . ILE   B 1 251 ? 24.318  31.898 33.04  1   21.23 ? 232 ILE   B CB    1 
ATOM   3757 C CG1   . ILE   B 1 251 ? 25.173  32.968 32.287 1   27.08 ? 232 ILE   B CG1   1 
ATOM   3758 C CG2   . ILE   B 1 251 ? 23.025  32.554 33.693 1   22.21 ? 232 ILE   B CG2   1 
ATOM   3759 C CD1   . ILE   B 1 251 ? 24.467  33.754 31.219 1   31.79 ? 232 ILE   B CD1   1 
ATOM   3760 N N     . GLU   B 1 252 ? 24.25   30.737 36.366 1   17.16 ? 233 GLU   B N     1 
ATOM   3761 C CA    . GLU   B 1 252 ? 23.497  29.998 37.4   1   17.21 ? 233 GLU   B CA    1 
ATOM   3762 C C     . GLU   B 1 252 ? 22.053  30.527 37.385 1   16.66 ? 233 GLU   B C     1 
ATOM   3763 O O     . GLU   B 1 252 ? 21.096  29.75  37.405 1   17.36 ? 233 GLU   B O     1 
ATOM   3764 C CB    . GLU   B 1 252 ? 24.106  30.205 38.803 1   20.12 ? 233 GLU   B CB    1 
ATOM   3765 C CG    . GLU   B 1 252 ? 25.532  29.692 39.036 1   24.09 ? 233 GLU   B CG    1 
ATOM   3766 C CD    . GLU   B 1 252 ? 25.442  28.292 39.63  1   37.15 ? 233 GLU   B CD    1 
ATOM   3767 O OE1   . GLU   B 1 252 ? 25.582  27.336 38.839 1   39.75 ? 233 GLU   B OE1   1 
ATOM   3768 O OE2   . GLU   B 1 252 ? 25.115  28.139 40.833 1   40.55 ? 233 GLU   B OE2   1 
ATOM   3769 N N     . TRP   B 1 253 ? 21.894  31.826 37.48  1   15.6  ? 234 TRP   B N     1 
ATOM   3770 C CA    . TRP   B 1 253 ? 20.586  32.391 37.266 1   19.69 ? 234 TRP   B CA    1 
ATOM   3771 C C     . TRP   B 1 253 ? 20.614  33.726 36.732 1   15.41 ? 234 TRP   B C     1 
ATOM   3772 O O     . TRP   B 1 253 ? 21.632  34.424 36.8   1   14.84 ? 234 TRP   B O     1 
ATOM   3773 C CB    . TRP   B 1 253 ? 19.656  32.288 38.371 1   24.94 ? 234 TRP   B CB    1 
ATOM   3774 C CG    . TRP   B 1 253 ? 20.138  32.888 39.611 1   25.71 ? 234 TRP   B CG    1 
ATOM   3775 C CD1   . TRP   B 1 253 ? 19.867  34.139 40.095 1   30.08 ? 234 TRP   B CD1   1 
ATOM   3776 C CD2   . TRP   B 1 253 ? 20.425  32.09  40.721 1   26.6  ? 234 TRP   B CD2   1 
ATOM   3777 N NE1   . TRP   B 1 253 ? 20.154  34.174 41.453 1   31.1  ? 234 TRP   B NE1   1 
ATOM   3778 C CE2   . TRP   B 1 253 ? 20.372  32.895 41.866 1   30.35 ? 234 TRP   B CE2   1 
ATOM   3779 C CE3   . TRP   B 1 253 ? 20.548  30.696 40.886 1   28.76 ? 234 TRP   B CE3   1 
ATOM   3780 C CZ2   . TRP   B 1 253 ? 20.647  32.388 43.131 1   35.15 ? 234 TRP   B CZ2   1 
ATOM   3781 C CZ3   . TRP   B 1 253 ? 20.727  30.206 42.135 1   32.57 ? 234 TRP   B CZ3   1 
ATOM   3782 C CH2   . TRP   B 1 253 ? 20.837  31.055 43.237 1   35.04 ? 234 TRP   B CH2   1 
ATOM   3783 N N     . PHE   B 1 254 ? 19.472  34.127 36.167 1   14.56 ? 235 PHE   B N     1 
ATOM   3784 C CA    . PHE   B 1 254 ? 19.379  35.388 35.491 1   14.7  ? 235 PHE   B CA    1 
ATOM   3785 C C     . PHE   B 1 254 ? 17.958  35.913 35.663 1   14.22 ? 235 PHE   B C     1 
ATOM   3786 O O     . PHE   B 1 254 ? 16.998  35.217 35.329 1   14.86 ? 235 PHE   B O     1 
ATOM   3787 C CB    . PHE   B 1 254 ? 19.696  35.225 33.984 1   16.05 ? 235 PHE   B CB    1 
ATOM   3788 C CG    . PHE   B 1 254 ? 19.985  36.545 33.294 1   17.05 ? 235 PHE   B CG    1 
ATOM   3789 C CD1   . PHE   B 1 254 ? 18.965  37.436 32.991 1   17.49 ? 235 PHE   B CD1   1 
ATOM   3790 C CD2   . PHE   B 1 254 ? 21.283  36.913 32.985 1   19.36 ? 235 PHE   B CD2   1 
ATOM   3791 C CE1   . PHE   B 1 254 ? 19.262  38.685 32.456 1   19.85 ? 235 PHE   B CE1   1 
ATOM   3792 C CE2   . PHE   B 1 254 ? 21.548  38.125 32.351 1   20.31 ? 235 PHE   B CE2   1 
ATOM   3793 C CZ    . PHE   B 1 254 ? 20.544  38.998 32.136 1   19.84 ? 235 PHE   B CZ    1 
ATOM   3794 N N     . GLU   B 1 255 ? 17.809  37.101 36.218 1   14.58 ? 236 GLU   B N     1 
ATOM   3795 C CA    . GLU   B 1 255 ? 16.489  37.687 36.446 1   15.09 ? 236 GLU   B CA    1 
ATOM   3796 C C     . GLU   B 1 255 ? 16.371  39.012 35.769 1   14.53 ? 236 GLU   B C     1 
ATOM   3797 O O     . GLU   B 1 255 ? 17.315  39.802 35.854 1   15.6  ? 236 GLU   B O     1 
ATOM   3798 C CB    . GLU   B 1 255 ? 16.265  37.832 37.953 1   15.93 ? 236 GLU   B CB    1 
ATOM   3799 C CG    . GLU   B 1 255 ? 14.899  38.409 38.336 1   19.73 ? 236 GLU   B CG    1 
ATOM   3800 C CD    . GLU   B 1 255 ? 14.637  38.353 39.808 1   30.77 ? 236 GLU   B CD    1 
ATOM   3801 O OE1   . GLU   B 1 255 ? 15.185  37.426 40.458 1   33.87 ? 236 GLU   B OE1   1 
ATOM   3802 O OE2   . GLU   B 1 255 ? 13.791  39.132 40.306 1   33.81 ? 236 GLU   B OE2   1 
ATOM   3803 N N     . VAL   B 1 256 ? 15.236  39.314 35.201 1   14.93 ? 237 VAL   B N     1 
ATOM   3804 C CA    . VAL   B 1 256 ? 14.916  40.643 34.658 1   15.83 ? 237 VAL   B CA    1 
ATOM   3805 C C     . VAL   B 1 256 ? 13.788  41.185 35.445 1   16.64 ? 237 VAL   B C     1 
ATOM   3806 O O     . VAL   B 1 256 ? 12.785  40.509 35.666 1   16.78 ? 237 VAL   B O     1 
ATOM   3807 C CB    . VAL   B 1 256 ? 14.572  40.58  33.164 1   19.9  ? 237 VAL   B CB    1 
ATOM   3808 C CG1   . VAL   B 1 256 ? 14.003  41.916 32.638 1   22.82 ? 237 VAL   B CG1   1 
ATOM   3809 C CG2   . VAL   B 1 256 ? 15.83   40.172 32.392 1   22.03 ? 237 VAL   B CG2   1 
ATOM   3810 N N     . ILE   B 1 257 ? 13.937  42.464 35.896 1   18.05 ? 238 ILE   B N     1 
ATOM   3811 C CA    . ILE   B 1 257 ? 12.874  43.167 36.574 1   20.6  ? 238 ILE   B CA    1 
ATOM   3812 C C     . ILE   B 1 257 ? 12.403  44.265 35.639 1   19.89 ? 238 ILE   B C     1 
ATOM   3813 O O     . ILE   B 1 257 ? 13.227  44.932 34.972 1   19.47 ? 238 ILE   B O     1 
ATOM   3814 C CB    . ILE   B 1 257 ? 13.144  43.704 37.982 1   28.66 ? 238 ILE   B CB    1 
ATOM   3815 C CG1   . ILE   B 1 257 ? 14.044  44.939 37.964 1   32.3  ? 238 ILE   B CG1   1 
ATOM   3816 C CG2   . ILE   B 1 257 ? 13.675  42.603 38.919 1   31.49 ? 238 ILE   B CG2   1 
ATOM   3817 C CD1   . ILE   B 1 257 ? 14.169  45.743 39.323 1   35.78 ? 238 ILE   B CD1   1 
ATOM   3818 N N     A SER   B 1 258 ? 11.101  44.506 35.601 0.5 20.23 ? 239 SER   B N     1 
ATOM   3819 N N     B SER   B 1 258 ? 11.119  44.534 35.653 0.5 20.29 ? 239 SER   B N     1 
ATOM   3820 C CA    A SER   B 1 258 ? 10.586  45.512 34.677 0.5 20.55 ? 239 SER   B CA    1 
ATOM   3821 C CA    B SER   B 1 258 ? 10.546  45.508 34.734 0.5 20.78 ? 239 SER   B CA    1 
ATOM   3822 C C     A SER   B 1 258 ? 10.793  46.955 35.123 0.5 21.26 ? 239 SER   B C     1 
ATOM   3823 C C     B SER   B 1 258 ? 10.655  46.978 35.157 0.5 21.59 ? 239 SER   B C     1 
ATOM   3824 O O     A SER   B 1 258 ? 10.951  47.83  34.269 0.5 23.21 ? 239 SER   B O     1 
ATOM   3825 O O     B SER   B 1 258 ? 10.577  47.89  34.32  0.5 24    ? 239 SER   B O     1 
ATOM   3826 C CB    A SER   B 1 258 ? 9.109   45.274 34.394 0.5 22.47 ? 239 SER   B CB    1 
ATOM   3827 C CB    B SER   B 1 258 ? 9.094   45.146 34.475 0.5 22.92 ? 239 SER   B CB    1 
ATOM   3828 O OG    A SER   B 1 258 ? 8.351   45.353 35.584 0.5 23.29 ? 239 SER   B OG    1 
ATOM   3829 O OG    B SER   B 1 258 ? 9.068   43.804 34.012 0.5 24.9  ? 239 SER   B OG    1 
ATOM   3830 N N     . GLN   B 1 259 ? 10.83   47.191 36.457 1   21.1  ? 240 GLN   B N     1 
ATOM   3831 C CA    . GLN   B 1 259 ? 10.893  48.578 37.006 1   20.57 ? 240 GLN   B CA    1 
ATOM   3832 C C     . GLN   B 1 259 ? 12.05   49.347 36.425 1   20.85 ? 240 GLN   B C     1 
ATOM   3833 O O     . GLN   B 1 259 ? 13.177  48.873 36.431 1   21.33 ? 240 GLN   B O     1 
ATOM   3834 C CB    . GLN   B 1 259 ? 11.103  48.506 38.521 1   22.19 ? 240 GLN   B CB    1 
ATOM   3835 C CG    . GLN   B 1 259 ? 11.189  49.888 39.221 1   25.07 ? 240 GLN   B CG    1 
ATOM   3836 C CD    . GLN   B 1 259 ? 9.917   50.648 39.188 1   32.56 ? 240 GLN   B CD    1 
ATOM   3837 O OE1   . GLN   B 1 259 ? 8.911   50.206 39.763 1   33.35 ? 240 GLN   B OE1   1 
ATOM   3838 N NE2   . GLN   B 1 259 ? 9.939   51.838 38.554 1   31.85 ? 240 GLN   B NE2   1 
ATOM   3839 N N     . SER   B 1 260 ? 11.804  50.568 35.951 1   19.82 ? 241 SER   B N     1 
ATOM   3840 C CA    . SER   B 1 260 ? 12.822  51.446 35.386 1   20.56 ? 241 SER   B CA    1 
ATOM   3841 C C     . SER   B 1 260 ? 13.014  52.651 36.284 1   19.96 ? 241 SER   B C     1 
ATOM   3842 O O     . SER   B 1 260 ? 12.177  52.962 37.13  1   20.85 ? 241 SER   B O     1 
ATOM   3843 C CB    . SER   B 1 260 ? 12.446  51.892 33.975 1   21.87 ? 241 SER   B CB    1 
ATOM   3844 O OG    . SER   B 1 260 ? 12.35   50.758 33.11  1   21.96 ? 241 SER   B OG    1 
ATOM   3845 N N     . TYR   B 1 261 ? 14.15   53.398 36.099 1   18.95 ? 242 TYR   B N     1 
ATOM   3846 C CA    . TYR   B 1 261 ? 14.364  54.633 36.854 1   19.25 ? 242 TYR   B CA    1 
ATOM   3847 C C     . TYR   B 1 261 ? 13.372  55.645 36.352 1   20.42 ? 242 TYR   B C     1 
ATOM   3848 O O     . TYR   B 1 261 ? 12.807  55.513 35.258 1   21.17 ? 242 TYR   B O     1 
ATOM   3849 C CB    . TYR   B 1 261 ? 15.82   55.103 36.599 1   18.57 ? 242 TYR   B CB    1 
ATOM   3850 C CG    . TYR   B 1 261 ? 16.812  54.273 37.361 1   17.63 ? 242 TYR   B CG    1 
ATOM   3851 C CD1   . TYR   B 1 261 ? 17.079  54.53  38.707 1   16.68 ? 242 TYR   B CD1   1 
ATOM   3852 C CD2   . TYR   B 1 261 ? 17.484  53.217 36.748 1   17.7  ? 242 TYR   B CD2   1 
ATOM   3853 C CE1   . TYR   B 1 261 ? 17.989  53.762 39.417 1   17.46 ? 242 TYR   B CE1   1 
ATOM   3854 C CE2   . TYR   B 1 261 ? 18.352  52.42  37.46  1   18.52 ? 242 TYR   B CE2   1 
ATOM   3855 C CZ    . TYR   B 1 261 ? 18.605  52.692 38.79  1   17.71 ? 242 TYR   B CZ    1 
ATOM   3856 O OH    . TYR   B 1 261 ? 19.53   51.924 39.45  1   18.48 ? 242 TYR   B OH    1 
ATOM   3857 N N     . SER   B 1 262 ? 13.315  56.785 37.066 1   20.48 ? 243 SER   B N     1 
ATOM   3858 C CA    . SER   B 1 262 ? 12.516  57.91  36.599 1   21.9  ? 243 SER   B CA    1 
ATOM   3859 C C     . SER   B 1 262 ? 13.06   58.382 35.226 1   22.2  ? 243 SER   B C     1 
ATOM   3860 O O     . SER   B 1 262 ? 14.293  58.383 35.038 1   19.62 ? 243 SER   B O     1 
ATOM   3861 C CB    . SER   B 1 262 ? 12.575  59.035 37.627 1   25.61 ? 243 SER   B CB    1 
ATOM   3862 O OG    . SER   B 1 262 ? 12.062  58.664 38.909 1   28.34 ? 243 SER   B OG    1 
ATOM   3863 N N     . SER   B 1 263 ? 12.218  58.725 34.243 1   26.75 ? 244 SER   B N     1 
ATOM   3864 C CA    . SER   B 1 263 ? 12.704  59.073 32.902 1   28.21 ? 244 SER   B CA    1 
ATOM   3865 C C     . SER   B 1 263 ? 13.63   60.313 32.859 1   27.88 ? 244 SER   B C     1 
ATOM   3866 O O     . SER   B 1 263 ? 14.379  60.484 31.893 1   28.89 ? 244 SER   B O     1 
ATOM   3867 C CB    . SER   B 1 263 ? 11.542  59.202 31.927 1   31.26 ? 244 SER   B CB    1 
ATOM   3868 O OG    . SER   B 1 263 ? 10.814  60.356 32.304 1   32.23 ? 244 SER   B OG    1 
ATOM   3869 N N     . THR   B 1 264 ? 13.626  61.119 33.881 1   26.73 ? 245 THR   B N     1 
ATOM   3870 C CA    . THR   B 1 264 ? 14.513  62.276 33.967 1   27.85 ? 245 THR   B CA    1 
ATOM   3871 C C     . THR   B 1 264 ? 15.901  61.895 34.562 1   27.95 ? 245 THR   B C     1 
ATOM   3872 O O     . THR   B 1 264 ? 16.824  62.734 34.614 1   30.27 ? 245 THR   B O     1 
ATOM   3873 C CB    . THR   B 1 264 ? 13.821  63.353 34.803 1   30.13 ? 245 THR   B CB    1 
ATOM   3874 O OG1   . THR   B 1 264 ? 13.495  62.77  36.062 1   32.6  ? 245 THR   B OG1   1 
ATOM   3875 C CG2   . THR   B 1 264 ? 12.525  63.883 34.126 1   31.51 ? 245 THR   B CG2   1 
ATOM   3876 N N     . MET   B 1 265 ? 16.044  60.634 35.055 1   23.75 ? 246 MET   B N     1 
ATOM   3877 C CA    . MET   B 1 265 ? 17.305  60.133 35.64  1   23.3  ? 246 MET   B CA    1 
ATOM   3878 C C     . MET   B 1 265 ? 18.031  59.206 34.653 1   21.93 ? 246 MET   B C     1 
ATOM   3879 O O     . MET   B 1 265 ? 19.263  59.231 34.575 1   21.09 ? 246 MET   B O     1 
ATOM   3880 C CB    . MET   B 1 265 ? 17.142  59.313 36.919 1   27.89 ? 246 MET   B CB    1 
ATOM   3881 C CG    . MET   B 1 265 ? 15.909  59.547 37.657 1   35.84 ? 246 MET   B CG    1 
ATOM   3882 S SD    . MET   B 1 265 ? 16.066  60.729 39.01  1   37.58 ? 246 MET   B SD    1 
ATOM   3883 C CE    . MET   B 1 265 ? 17.893  60.548 39.51  1   24.15 ? 246 MET   B CE    1 
ATOM   3884 N N     . ALA   B 1 266 ? 17.318  58.294 33.992 1   21.46 ? 247 ALA   B N     1 
ATOM   3885 C CA    . ALA   B 1 266 ? 17.954  57.348 33.058 1   21.36 ? 247 ALA   B CA    1 
ATOM   3886 C C     . ALA   B 1 266 ? 16.943  56.778 32.113 1   22.71 ? 247 ALA   B C     1 
ATOM   3887 O O     . ALA   B 1 266 ? 15.751  56.73  32.483 1   28.74 ? 247 ALA   B O     1 
ATOM   3888 C CB    . ALA   B 1 266 ? 18.627  56.201 33.817 1   21.65 ? 247 ALA   B CB    1 
ATOM   3889 N N     . ASN   B 1 267 ? 17.335  56.347 30.931 1   18.6  ? 248 ASN   B N     1 
ATOM   3890 C CA    . ASN   B 1 267 ? 16.374  55.871 29.945 1   17.92 ? 248 ASN   B CA    1 
ATOM   3891 C C     . ASN   B 1 267 ? 16.387  54.319 29.841 1   19.22 ? 248 ASN   B C     1 
ATOM   3892 O O     . ASN   B 1 267 ? 16.238  53.796 28.731 1   22.2  ? 248 ASN   B O     1 
ATOM   3893 C CB    . ASN   B 1 267 ? 16.639  56.495 28.579 1   20.52 ? 248 ASN   B CB    1 
ATOM   3894 C CG    . ASN   B 1 267 ? 17.981  56.163 27.99  1   19.54 ? 248 ASN   B CG    1 
ATOM   3895 O OD1   . ASN   B 1 267 ? 18.907  55.651 28.715 1   18.28 ? 248 ASN   B OD1   1 
ATOM   3896 N ND2   . ASN   B 1 267 ? 18.173  56.408 26.675 1   21.3  ? 248 ASN   B ND2   1 
ATOM   3897 N N     . ASN   B 1 268 ? 16.47   53.632 30.983 1   17.73 ? 249 ASN   B N     1 
ATOM   3898 C CA    . ASN   B 1 268 ? 16.538  52.16  30.942 1   16.9  ? 249 ASN   B CA    1 
ATOM   3899 C C     . ASN   B 1 268 ? 15.192  51.543 30.722 1   19.02 ? 249 ASN   B C     1 
ATOM   3900 O O     . ASN   B 1 268 ? 14.142  52.177 30.912 1   20.12 ? 249 ASN   B O     1 
ATOM   3901 C CB    . ASN   B 1 268 ? 17.17   51.617 32.215 1   17.45 ? 249 ASN   B CB    1 
ATOM   3902 C CG    . ASN   B 1 268 ? 16.359  51.828 33.476 1   18.42 ? 249 ASN   B CG    1 
ATOM   3903 O OD1   . ASN   B 1 268 ? 15.909  52.958 33.747 1   18.17 ? 249 ASN   B OD1   1 
ATOM   3904 N ND2   . ASN   B 1 268 ? 16.234  50.832 34.342 1   18.77 ? 249 ASN   B ND2   1 
ATOM   3905 N N     . GLU   B 1 269 ? 15.22   50.245 30.38  1   18.06 ? 250 GLU   B N     1 
ATOM   3906 C CA    . GLU   B 1 269 ? 14.029  49.394 30.289 1   19.1  ? 250 GLU   B CA    1 
ATOM   3907 C C     . GLU   B 1 269 ? 14.28   48.242 31.27  1   18.19 ? 250 GLU   B C     1 
ATOM   3908 O O     . GLU   B 1 269 ? 14.675  47.121 30.869 1   19.15 ? 250 GLU   B O     1 
ATOM   3909 C CB    . GLU   B 1 269 ? 13.838  48.814 28.881 1   22.63 ? 250 GLU   B CB    1 
ATOM   3910 C CG    . GLU   B 1 269 ? 13.552  49.924 27.9   1   29.96 ? 250 GLU   B CG    1 
ATOM   3911 C CD    . GLU   B 1 269 ? 13.389  49.485 26.461 1   48.04 ? 250 GLU   B CD    1 
ATOM   3912 O OE1   . GLU   B 1 269 ? 14.021  50.109 25.579 1   54.78 ? 250 GLU   B OE1   1 
ATOM   3913 O OE2   . GLU   B 1 269 ? 12.628  48.521 26.207 1   53.33 ? 250 GLU   B OE2   1 
ATOM   3914 N N     . GLY   B 1 270 ? 14.107  48.499 32.547 1   17.72 ? 251 GLY   B N     1 
ATOM   3915 C CA    . GLY   B 1 270 ? 14.306  47.513 33.602 1   17.83 ? 251 GLY   B CA    1 
ATOM   3916 C C     . GLY   B 1 270 ? 15.773  47.299 33.968 1   15.65 ? 251 GLY   B C     1 
ATOM   3917 O O     . GLY   B 1 270 ? 16.688  48.061 33.587 1   15.92 ? 251 GLY   B O     1 
ATOM   3918 N N     . LEU   B 1 271 ? 15.995  46.265 34.76  1   15.44 ? 252 LEU   B N     1 
ATOM   3919 C CA    . LEU   B 1 271 ? 17.316  45.936 35.27  1   16.38 ? 252 LEU   B CA    1 
ATOM   3920 C C     . LEU   B 1 271 ? 17.44   44.444 35.263 1   15.3  ? 252 LEU   B C     1 
ATOM   3921 O O     . LEU   B 1 271 ? 16.448  43.705 35.194 1   16.29 ? 252 LEU   B O     1 
ATOM   3922 C CB    . LEU   B 1 271 ? 17.463  46.4   36.71  1   19.48 ? 252 LEU   B CB    1 
ATOM   3923 C CG    . LEU   B 1 271 ? 17.754  47.94  36.876 1   23.51 ? 252 LEU   B CG    1 
ATOM   3924 C CD1   . LEU   B 1 271 ? 16.478  48.635 37.149 1   25.75 ? 252 LEU   B CD1   1 
ATOM   3925 C CD2   . LEU   B 1 271 ? 18.677  48.201 38.074 1   24.28 ? 252 LEU   B CD2   1 
ATOM   3926 N N     . PHE   B 1 272 ? 18.659  43.976 35.309 1   14.47 ? 253 PHE   B N     1 
ATOM   3927 C CA    . PHE   B 1 272 ? 18.914  42.54  35.412 1   14.03 ? 253 PHE   B CA    1 
ATOM   3928 C C     . PHE   B 1 272 ? 19.761  42.265 36.647 1   13.27 ? 253 PHE   B C     1 
ATOM   3929 O O     . PHE   B 1 272 ? 20.496  43.133 37.139 1   13.82 ? 253 PHE   B O     1 
ATOM   3930 C CB    . PHE   B 1 272 ? 19.599  41.942 34.187 1   15.19 ? 253 PHE   B CB    1 
ATOM   3931 C CG    . PHE   B 1 272 ? 21.05   42.351 34.052 1   14.86 ? 253 PHE   B CG    1 
ATOM   3932 C CD1   . PHE   B 1 272 ? 22.06   41.587 34.605 1   14.64 ? 253 PHE   B CD1   1 
ATOM   3933 C CD2   . PHE   B 1 272 ? 21.406  43.459 33.316 1   15.61 ? 253 PHE   B CD2   1 
ATOM   3934 C CE1   . PHE   B 1 272 ? 23.406  41.962 34.476 1   15.03 ? 253 PHE   B CE1   1 
ATOM   3935 C CE2   . PHE   B 1 272 ? 22.749  43.824 33.18  1   14.78 ? 253 PHE   B CE2   1 
ATOM   3936 C CZ    . PHE   B 1 272 ? 23.739  43.093 33.803 1   14.16 ? 253 PHE   B CZ    1 
ATOM   3937 N N     . SER   B 1 273 ? 19.696  41.002 37.105 1   14.22 ? 254 SER   B N     1 
ATOM   3938 C CA    . SER   B 1 273 ? 20.568  40.493 38.146 1   14.73 ? 254 SER   B CA    1 
ATOM   3939 C C     . SER   B 1 273 ? 21.028  39.145 37.647 1   14.52 ? 254 SER   B C     1 
ATOM   3940 O O     . SER   B 1 273 ? 20.178  38.333 37.242 1   14.78 ? 254 SER   B O     1 
ATOM   3941 C CB    . SER   B 1 273 ? 19.797  40.347 39.451 1   21.22 ? 254 SER   B CB    1 
ATOM   3942 O OG    . SER   B 1 273 ? 20.491  39.688 40.495 1   28.75 ? 254 SER   B OG    1 
ATOM   3943 N N     . LEU   B 1 274 ? 22.286  38.846 37.786 1   14.1  ? 255 LEU   B N     1 
ATOM   3944 C CA    . LEU   B 1 274 ? 22.756  37.53  37.431 1   15.96 ? 255 LEU   B CA    1 
ATOM   3945 C C     . LEU   B 1 274 ? 23.771  37.016 38.367 1   14.88 ? 255 LEU   B C     1 
ATOM   3946 O O     . LEU   B 1 274 ? 24.519  37.775 38.985 1   13.97 ? 255 LEU   B O     1 
ATOM   3947 C CB    . LEU   B 1 274 ? 23.208  37.438 36.006 1   18.83 ? 255 LEU   B CB    1 
ATOM   3948 C CG    . LEU   B 1 274 ? 24.474  38.157 35.72  1   17.89 ? 255 LEU   B CG    1 
ATOM   3949 C CD1   . LEU   B 1 274 ? 25.721  37.269 35.925 1   20.65 ? 255 LEU   B CD1   1 
ATOM   3950 C CD2   . LEU   B 1 274 ? 24.569  38.575 34.226 1   20.11 ? 255 LEU   B CD2   1 
ATOM   3951 N N     . VAL   B 1 275 ? 23.784  35.691 38.468 1   14.69 ? 256 VAL   B N     1 
ATOM   3952 C CA    . VAL   B 1 275 ? 24.787  34.972 39.203 1   15.11 ? 256 VAL   B CA    1 
ATOM   3953 C C     . VAL   B 1 275 ? 25.428  33.985 38.241 1   15.79 ? 256 VAL   B C     1 
ATOM   3954 O O     . VAL   B 1 275 ? 24.723  33.197 37.615 1   15.93 ? 256 VAL   B O     1 
ATOM   3955 C CB    . VAL   B 1 275 ? 24.205  34.245 40.443 1   17.92 ? 256 VAL   B CB    1 
ATOM   3956 C CG1   . VAL   B 1 275 ? 25.283  33.473 41.197 1   19.71 ? 256 VAL   B CG1   1 
ATOM   3957 C CG2   . VAL   B 1 275 ? 23.454  35.215 41.37  1   20.01 ? 256 VAL   B CG2   1 
ATOM   3958 N N     . ALA   B 1 276 ? 26.75   34.022 38.1   1   16.44 ? 257 ALA   B N     1 
ATOM   3959 C CA    . ALA   B 1 276 ? 27.494  33.133 37.239 1   16.31 ? 257 ALA   B CA    1 
ATOM   3960 C C     . ALA   B 1 276 ? 28.677  32.547 38.004 1   17.04 ? 257 ALA   B C     1 
ATOM   3961 O O     . ALA   B 1 276 ? 29.032  33.051 39.067 1   17.26 ? 257 ALA   B O     1 
ATOM   3962 C CB    . ALA   B 1 276 ? 27.943  33.849 35.986 1   18.41 ? 257 ALA   B CB    1 
ATOM   3963 N N     . ARG   B 1 277 ? 29.281  31.473 37.491 1   17.16 ? 258 ARG   B N     1 
ATOM   3964 C CA    . ARG   B 1 277 ? 30.456  30.881 38.096 1   17.68 ? 258 ARG   B CA    1 
ATOM   3965 C C     . ARG   B 1 277 ? 31.555  30.844 37.063 1   16.96 ? 258 ARG   B C     1 
ATOM   3966 O O     . ARG   B 1 277 ? 31.326  30.54  35.871 1   17.61 ? 258 ARG   B O     1 
ATOM   3967 C CB    . ARG   B 1 277 ? 30.177  29.428 38.534 1   22.41 ? 258 ARG   B CB    1 
ATOM   3968 C CG    . ARG   B 1 277 ? 29.316  29.359 39.759 1   29.51 ? 258 ARG   B CG    1 
ATOM   3969 C CD    . ARG   B 1 277 ? 29.309  27.911 40.23  1   34.23 ? 258 ARG   B CD    1 
ATOM   3970 N NE    . ARG   B 1 277 ? 30.376  27.639 41.193 1   37.55 ? 258 ARG   B NE    1 
ATOM   3971 C CZ    . ARG   B 1 277 ? 30.387  26.584 42.003 1   40.35 ? 258 ARG   B CZ    1 
ATOM   3972 N NH1   . ARG   B 1 277 ? 29.406  25.685 41.95  1   37.93 ? 258 ARG   B NH1   1 
ATOM   3973 N NH2   . ARG   B 1 277 ? 31.386  26.407 42.858 1   40.61 ? 258 ARG   B NH2   1 
ATOM   3974 N N     . LYS   B 1 278 ? 32.787  31.141 37.505 1   17.5  ? 259 LYS   B N     1 
ATOM   3975 C CA    . LYS   B 1 278 ? 33.913  31.117 36.588 1   17.78 ? 259 LYS   B CA    1 
ATOM   3976 C C     . LYS   B 1 278 ? 34.288  29.673 36.251 1   21.43 ? 259 LYS   B C     1 
ATOM   3977 O O     . LYS   B 1 278 ? 34.351  28.872 37.17  1   23.25 ? 259 LYS   B O     1 
ATOM   3978 C CB    . LYS   B 1 278 ? 35.089  31.783 37.269 1   18.46 ? 259 LYS   B CB    1 
ATOM   3979 C CG    . LYS   B 1 278 ? 36.255  31.995 36.329 1   21.05 ? 259 LYS   B CG    1 
ATOM   3980 C CD    . LYS   B 1 278 ? 37.446  32.458 37.171 1   23.77 ? 259 LYS   B CD    1 
ATOM   3981 C CE    . LYS   B 1 278 ? 38.667  32.582 36.334 1   27.74 ? 259 LYS   B CE    1 
ATOM   3982 N NZ    . LYS   B 1 278 ? 39.797  33.14  37.095 1   21.66 ? 259 LYS   B NZ    1 
ATOM   3983 N N     . LEU   B 1 279 ? 34.56   29.383 34.982 1   21.13 ? 260 LEU   B N     1 
ATOM   3984 C CA    . LEU   B 1 279 ? 35.089  28.029 34.678 1   25.9  ? 260 LEU   B CA    1 
ATOM   3985 C C     . LEU   B 1 279 ? 36.567  28.046 35.155 1   30.97 ? 260 LEU   B C     1 
ATOM   3986 O O     . LEU   B 1 279 ? 37.305  29.027 34.87  1   34.25 ? 260 LEU   B O     1 
ATOM   3987 C CB    . LEU   B 1 279 ? 35.089  27.815 33.196 1   26.53 ? 260 LEU   B CB    1 
ATOM   3988 C CG    . LEU   B 1 279 ? 33.762  27.675 32.57  1   29.44 ? 260 LEU   B CG    1 
ATOM   3989 C CD1   . LEU   B 1 279 ? 33.888  27.821 31.055 1   32.33 ? 260 LEU   B CD1   1 
ATOM   3990 C CD2   . LEU   B 1 279 ? 33.181  26.31  32.93  1   30.21 ? 260 LEU   B CD2   1 
HETATM 3991 C C1    . A1IPO C 2 .   ? 7.781   18.831 33.971 1   19.71 ? 301 A1IPO A C1    1 
HETATM 3992 C C3    . A1IPO C 2 .   ? 7.831   18.203 36.24  1   15.3  ? 301 A1IPO A C3    1 
HETATM 3993 N N6    . A1IPO C 2 .   ? 6.656   17.925 38.706 1   15.07 ? 301 A1IPO A N6    1 
HETATM 3994 C C7    . A1IPO C 2 .   ? 7.961   17.679 38.548 1   14.95 ? 301 A1IPO A C7    1 
HETATM 3995 C C8    . A1IPO C 2 .   ? 8.669   17.33  39.809 1   16.75 ? 301 A1IPO A C8    1 
HETATM 3996 C C9    . A1IPO C 2 .   ? 8.585   17.783 37.334 1   15.74 ? 301 A1IPO A C9    1 
HETATM 3997 C C10   . A1IPO C 2 .   ? 10.048  17.477 37.18  1   18.09 ? 301 A1IPO A C10   1 
HETATM 3998 O O2    . A1IPO C 2 .   ? 8.515   18.317 35.055 1   18.07 ? 301 A1IPO A O2    1 
HETATM 3999 C C4    . A1IPO C 2 .   ? 6.481   18.432 36.344 1   14.62 ? 301 A1IPO A C4    1 
HETATM 4000 C C5    . A1IPO C 2 .   ? 5.935   18.238 37.604 1   14.76 ? 301 A1IPO A C5    1 
HETATM 4001 N N     . SAH   D 3 .   ? 2.453   21.64  42.61  1   16.5  ? 302 SAH   A N     1 
HETATM 4002 C CA    . SAH   D 3 .   ? 3.163   20.378 42.966 1   15.52 ? 302 SAH   A CA    1 
HETATM 4003 C CB    . SAH   D 3 .   ? 2.74    19.238 42.036 1   15.99 ? 302 SAH   A CB    1 
HETATM 4004 C CG    . SAH   D 3 .   ? 3.126   19.384 40.569 1   15.45 ? 302 SAH   A CG    1 
HETATM 4005 S SD    . SAH   D 3 .   ? 2.981   17.803 39.67  1   15.49 ? 302 SAH   A SD    1 
HETATM 4006 C C     . SAH   D 3 .   ? 4.683   20.612 42.976 1   15.5  ? 302 SAH   A C     1 
HETATM 4007 O O     . SAH   D 3 .   ? 5.094   21.8   42.993 1   15.35 ? 302 SAH   A O     1 
HETATM 4008 O OXT   . SAH   D 3 .   ? 5.427   19.588 42.976 1   15.32 ? 302 SAH   A OXT   1 
HETATM 4009 C "C5'" . SAH   D 3 .   ? 1.691   18.198 38.435 1   14.86 ? 302 SAH   A "C5'" 1 
HETATM 4010 C "C4'" . SAH   D 3 .   ? 0.31    18.331 39.045 1   14.75 ? 302 SAH   A "C4'" 1 
HETATM 4011 O "O4'" . SAH   D 3 .   ? -0.538  18.772 37.96  1   14.63 ? 302 SAH   A "O4'" 1 
HETATM 4012 C "C3'" . SAH   D 3 .   ? -0.288  16.996 39.546 1   15.12 ? 302 SAH   A "C3'" 1 
HETATM 4013 O "O3'" . SAH   D 3 .   ? -0.669  17.124 40.901 1   16.06 ? 302 SAH   A "O3'" 1 
HETATM 4014 C "C2'" . SAH   D 3 .   ? -1.438  16.743 38.575 1   15.08 ? 302 SAH   A "C2'" 1 
HETATM 4015 O "O2'" . SAH   D 3 .   ? -2.538  16.048 39.148 1   16.76 ? 302 SAH   A "O2'" 1 
HETATM 4016 C "C1'" . SAH   D 3 .   ? -1.798  18.175 38.184 1   14.58 ? 302 SAH   A "C1'" 1 
HETATM 4017 N N9    . SAH   D 3 .   ? -2.603  18.276 36.973 1   14.35 ? 302 SAH   A N9    1 
HETATM 4018 C C8    . SAH   D 3 .   ? -2.462  17.607 35.79  1   15.12 ? 302 SAH   A C8    1 
HETATM 4019 N N7    . SAH   D 3 .   ? -3.325  17.957 34.871 1   17.1  ? 302 SAH   A N7    1 
HETATM 4020 C C5    . SAH   D 3 .   ? -4.086  18.933 35.494 1   15.54 ? 302 SAH   A C5    1 
HETATM 4021 C C6    . SAH   D 3 .   ? -5.153  19.734 35.046 1   15.8  ? 302 SAH   A C6    1 
HETATM 4022 N N6    . SAH   D 3 .   ? -5.668  19.638 33.806 1   16.93 ? 302 SAH   A N6    1 
HETATM 4023 N N1    . SAH   D 3 .   ? -5.641  20.655 35.9   1   15.81 ? 302 SAH   A N1    1 
HETATM 4024 C C2    . SAH   D 3 .   ? -5.143  20.732 37.136 1   15.36 ? 302 SAH   A C2    1 
HETATM 4025 N N3    . SAH   D 3 .   ? -4.144  20.015 37.679 1   16.39 ? 302 SAH   A N3    1 
HETATM 4026 C C4    . SAH   D 3 .   ? -3.653  19.139 36.792 1   15.4  ? 302 SAH   A C4    1 
HETATM 4027 C C1    . A1IPO E 2 .   ? 23.176  53.162 33.752 1   17.67 ? 301 A1IPO B C1    1 
HETATM 4028 C C3    . A1IPO E 2 .   ? 23.108  53.885 36     1   15.59 ? 301 A1IPO B C3    1 
HETATM 4029 N N6    . A1IPO E 2 .   ? 24.234  54.244 38.492 1   14.82 ? 301 A1IPO B N6    1 
HETATM 4030 C C7    . A1IPO E 2 .   ? 22.926  54.509 38.291 1   15.58 ? 301 A1IPO B C7    1 
HETATM 4031 C C8    . A1IPO E 2 .   ? 22.189  54.933 39.498 1   17.04 ? 301 A1IPO B C8    1 
HETATM 4032 C C9    . A1IPO E 2 .   ? 22.339  54.361 37.053 1   16    ? 301 A1IPO B C9    1 
HETATM 4033 C C10   . A1IPO E 2 .   ? 20.879  54.724 36.855 1   18.13 ? 301 A1IPO B C10   1 
HETATM 4034 O O2    . A1IPO E 2 .   ? 22.443  53.722 34.808 1   16.93 ? 301 A1IPO B O2    1 
HETATM 4035 C C4    . A1IPO E 2 .   ? 24.458  53.616 36.162 1   14.98 ? 301 A1IPO B C4    1 
HETATM 4036 C C5    . A1IPO E 2 .   ? 24.972  53.815 37.433 1   15.03 ? 301 A1IPO B C5    1 
HETATM 4037 N N     . SAH   F 3 .   ? 28.155  50.452 42.604 1   14.97 ? 302 SAH   B N     1 
HETATM 4038 C CA    . SAH   F 3 .   ? 27.509  51.765 42.904 1   13.93 ? 302 SAH   B CA    1 
HETATM 4039 C CB    . SAH   F 3 .   ? 28.021  52.851 41.956 1   14.89 ? 302 SAH   B CB    1 
HETATM 4040 C CG    . SAH   F 3 .   ? 27.669  52.69  40.485 1   14.45 ? 302 SAH   B CG    1 
HETATM 4041 S SD    . SAH   F 3 .   ? 27.907  54.264 39.552 1   14.41 ? 302 SAH   B SD    1 
HETATM 4042 C C     . SAH   F 3 .   ? 25.982  51.606 42.85  1   14.43 ? 302 SAH   B C     1 
HETATM 4043 O O     . SAH   F 3 .   ? 25.513  50.438 42.9   1   14.89 ? 302 SAH   B O     1 
HETATM 4044 O OXT   . SAH   F 3 .   ? 25.299  52.667 42.828 1   15.27 ? 302 SAH   B OXT   1 
HETATM 4045 C "C5'" . SAH   F 3 .   ? 29.207  53.789 38.366 1   14.36 ? 302 SAH   B "C5'" 1 
HETATM 4046 C "C4'" . SAH   F 3 .   ? 30.55   53.589 39.04  1   13.42 ? 302 SAH   B "C4'" 1 
HETATM 4047 O "O4'" . SAH   F 3 .   ? 31.41   53.091 37.998 1   12.94 ? 302 SAH   B "O4'" 1 
HETATM 4048 C "C3'" . SAH   F 3 .   ? 31.177  54.903 39.539 1   14.18 ? 302 SAH   B "C3'" 1 
HETATM 4049 O "O3'" . SAH   F 3 .   ? 31.521  54.787 40.917 1   14.47 ? 302 SAH   B "O3'" 1 
HETATM 4050 C "C2'" . SAH   F 3 .   ? 32.399  55.064 38.615 1   14.23 ? 302 SAH   B "C2'" 1 
HETATM 4051 O "O2'" . SAH   F 3 .   ? 33.502  55.754 39.217 1   15.58 ? 302 SAH   B "O2'" 1 
HETATM 4052 C "C1'" . SAH   F 3 .   ? 32.694  53.617 38.279 1   13.65 ? 302 SAH   B "C1'" 1 
HETATM 4053 N N9    . SAH   F 3 .   ? 33.545  53.442 37.111 1   13.7  ? 302 SAH   B N9    1 
HETATM 4054 C C8    . SAH   F 3 .   ? 33.441  54.071 35.899 1   13.97 ? 302 SAH   B C8    1 
HETATM 4055 N N7    . SAH   F 3 .   ? 34.327  53.677 35.014 1   14.56 ? 302 SAH   B N7    1 
HETATM 4056 C C5    . SAH   F 3 .   ? 35.065  52.719 35.693 1   12.87 ? 302 SAH   B C5    1 
HETATM 4057 C C6    . SAH   F 3 .   ? 36.155  51.909 35.313 1   13.29 ? 302 SAH   B C6    1 
HETATM 4058 N N6    . SAH   F 3 .   ? 36.76   51.966 34.089 1   14.93 ? 302 SAH   B N6    1 
HETATM 4059 N N1    . SAH   F 3 .   ? 36.623  51.035 36.218 1   14.46 ? 302 SAH   B N1    1 
HETATM 4060 C C2    . SAH   F 3 .   ? 36.082  50.999 37.441 1   14.8  ? 302 SAH   B C2    1 
HETATM 4061 N N3    . SAH   F 3 .   ? 35.075  51.739 37.925 1   14.21 ? 302 SAH   B N3    1 
HETATM 4062 C C4    . SAH   F 3 .   ? 34.596  52.565 36.989 1   13.28 ? 302 SAH   B C4    1 
HETATM 4063 O O     . HOH   G 4 .   ? 8.329   25.933 30.552 1   40.82 ? 401 HOH   A O     1 
HETATM 4064 O O     . HOH   G 4 .   ? 11.639  23.219 23.752 1   49.51 ? 402 HOH   A O     1 
HETATM 4065 O O     . HOH   G 4 .   ? 4.524   41.965 30.473 1   21.34 ? 403 HOH   A O     1 
HETATM 4066 O O     . HOH   G 4 .   ? -2.618  19.132 20.714 1   49.04 ? 404 HOH   A O     1 
HETATM 4067 O O     . HOH   G 4 .   ? 20.729  22.392 32.915 1   34.36 ? 405 HOH   A O     1 
HETATM 4068 O O     . HOH   G 4 .   ? -2.721  9.272  50.545 1   45.63 ? 406 HOH   A O     1 
HETATM 4069 O O     . HOH   G 4 .   ? 14.693  36.666 64.029 1   31.39 ? 407 HOH   A O     1 
HETATM 4070 O O     . HOH   G 4 .   ? 7.093   39.332 43.733 1   27.3  ? 408 HOH   A O     1 
HETATM 4071 O O     . HOH   G 4 .   ? 7.928   3.679  41.849 1   30.9  ? 409 HOH   A O     1 
HETATM 4072 O O     . HOH   G 4 .   ? -3.534  10.385 41.402 1   24.91 ? 410 HOH   A O     1 
HETATM 4073 O O     . HOH   G 4 .   ? 22.339  24.354 41.816 1   33.72 ? 411 HOH   A O     1 
HETATM 4074 O O     . HOH   G 4 .   ? -9.893  37.901 47.506 1   31.8  ? 412 HOH   A O     1 
HETATM 4075 O O     . HOH   G 4 .   ? -10.329 12.341 33.629 1   32.69 ? 413 HOH   A O     1 
HETATM 4076 O O     . HOH   G 4 .   ? 15.078  10.05  31.904 1   37.85 ? 414 HOH   A O     1 
HETATM 4077 O O     . HOH   G 4 .   ? 8.878   39.478 28.883 1   37.41 ? 415 HOH   A O     1 
HETATM 4078 O O     . HOH   G 4 .   ? -22.31  25.009 42.383 1   34.93 ? 416 HOH   A O     1 
HETATM 4079 O O     . HOH   G 4 .   ? -5.978  22.615 57.091 1   45.35 ? 417 HOH   A O     1 
HETATM 4080 O O     . HOH   G 4 .   ? 8.358   32.959 59.931 1   41.6  ? 418 HOH   A O     1 
HETATM 4081 O O     . HOH   G 4 .   ? -2.624  32.597 57.216 1   37.77 ? 419 HOH   A O     1 
HETATM 4082 O O     . HOH   G 4 .   ? -9.152  27.423 51.758 1   43.27 ? 420 HOH   A O     1 
HETATM 4083 O O     . HOH   G 4 .   ? -12.598 18.556 33.624 1   26.44 ? 421 HOH   A O     1 
HETATM 4084 O O     . HOH   G 4 .   ? 0.629   17.519 22.434 1   33.99 ? 422 HOH   A O     1 
HETATM 4085 O O     . HOH   G 4 .   ? 15.366  20.073 26.296 1   44.08 ? 423 HOH   A O     1 
HETATM 4086 O O     . HOH   G 4 .   ? -16.197 27.748 39.419 1   32.11 ? 424 HOH   A O     1 
HETATM 4087 O O     . HOH   G 4 .   ? -13.896 22.341 42.275 1   31.14 ? 425 HOH   A O     1 
HETATM 4088 O O     . HOH   G 4 .   ? 17.061  12.724 43.721 1   39.44 ? 426 HOH   A O     1 
HETATM 4089 O O     . HOH   G 4 .   ? 1.377   15.235 31.75  1   16.55 ? 427 HOH   A O     1 
HETATM 4090 O O     . HOH   G 4 .   ? 10.393  0.722  32.741 1   40.16 ? 428 HOH   A O     1 
HETATM 4091 O O     . HOH   G 4 .   ? -10.65  16.237 48.943 1   67.45 ? 429 HOH   A O     1 
HETATM 4092 O O     . HOH   G 4 .   ? -9.119  41.318 48.565 1   44.33 ? 430 HOH   A O     1 
HETATM 4093 O O     . HOH   G 4 .   ? -0.942  41.616 28.32  1   23.23 ? 431 HOH   A O     1 
HETATM 4094 O O     . HOH   G 4 .   ? 13.238  28.321 63.791 1   40.39 ? 432 HOH   A O     1 
HETATM 4095 O O     . HOH   G 4 .   ? -15.215 24.033 49.808 1   40.31 ? 433 HOH   A O     1 
HETATM 4096 O O     . HOH   G 4 .   ? 14.911  29.694 25.297 1   41.05 ? 434 HOH   A O     1 
HETATM 4097 O O     . HOH   G 4 .   ? 5.114   45.053 33.811 1   26.4  ? 435 HOH   A O     1 
HETATM 4098 O O     . HOH   G 4 .   ? -14.247 24.608 29.403 1   23.5  ? 436 HOH   A O     1 
HETATM 4099 O O     . HOH   G 4 .   ? 8.933   22.777 29.611 1   20.65 ? 437 HOH   A O     1 
HETATM 4100 O O     . HOH   G 4 .   ? 1.104   13.543 53.078 1   26.29 ? 438 HOH   A O     1 
HETATM 4101 O O     . HOH   G 4 .   ? -13.058 35.522 39.867 1   35.19 ? 439 HOH   A O     1 
HETATM 4102 O O     . HOH   G 4 .   ? 12.604  6.183  45.433 1   47.02 ? 440 HOH   A O     1 
HETATM 4103 O O     . HOH   G 4 .   ? -4.877  34.623 20.664 1   33.91 ? 441 HOH   A O     1 
HETATM 4104 O O     . HOH   G 4 .   ? -4.859  18.416 31.164 1   21.12 ? 442 HOH   A O     1 
HETATM 4105 O O     . HOH   G 4 .   ? 18.896  15.782 49.232 1   57.95 ? 443 HOH   A O     1 
HETATM 4106 O O     . HOH   G 4 .   ? -12.063 37.775 38.568 1   45.08 ? 444 HOH   A O     1 
HETATM 4107 O O     . HOH   G 4 .   ? 4.17    44.77  42.833 1   38.58 ? 445 HOH   A O     1 
HETATM 4108 O O     . HOH   G 4 .   ? 1.918   34.8   22.444 1   34.91 ? 446 HOH   A O     1 
HETATM 4109 O O     . HOH   G 4 .   ? 4.789   26.443 32.778 1   22.46 ? 447 HOH   A O     1 
HETATM 4110 O O     . HOH   G 4 .   ? -6.957  6.053  33.868 1   39.08 ? 448 HOH   A O     1 
HETATM 4111 O O     . HOH   G 4 .   ? 4.934   29.907 49.865 1   22.02 ? 449 HOH   A O     1 
HETATM 4112 O O     . HOH   G 4 .   ? 1.515   9.237  31.055 1   18.4  ? 450 HOH   A O     1 
HETATM 4113 O O     . HOH   G 4 .   ? 16.636  14.452 46.915 1   49.13 ? 451 HOH   A O     1 
HETATM 4114 O O     . HOH   G 4 .   ? 10.431  21.41  61.235 1   45.14 ? 452 HOH   A O     1 
HETATM 4115 O O     . HOH   G 4 .   ? 17.564  36.166 40.733 1   34.75 ? 453 HOH   A O     1 
HETATM 4116 O O     . HOH   G 4 .   ? 6.941   -1.886 37.208 1   44.65 ? 454 HOH   A O     1 
HETATM 4117 O O     . HOH   G 4 .   ? 6.058   40.391 55.172 1   56.1  ? 455 HOH   A O     1 
HETATM 4118 O O     . HOH   G 4 .   ? -13.663 30.579 36.768 1   26.28 ? 456 HOH   A O     1 
HETATM 4119 O O     . HOH   G 4 .   ? 19.179  28.658 45.261 1   30.18 ? 457 HOH   A O     1 
HETATM 4120 O O     . HOH   G 4 .   ? 7.534   13.147 25.875 1   42.25 ? 458 HOH   A O     1 
HETATM 4121 O O     . HOH   G 4 .   ? 9.879   44.304 52.191 1   45.52 ? 459 HOH   A O     1 
HETATM 4122 O O     . HOH   G 4 .   ? 1.701   4.354  37.737 1   25.49 ? 460 HOH   A O     1 
HETATM 4123 O O     . HOH   G 4 .   ? 10.552  19.784 42.297 1   21.99 ? 461 HOH   A O     1 
HETATM 4124 O O     . HOH   G 4 .   ? -8.574  35.758 32.325 1   24.23 ? 462 HOH   A O     1 
HETATM 4125 O O     . HOH   G 4 .   ? 7.828   5.142  46.908 1   37.74 ? 463 HOH   A O     1 
HETATM 4126 O O     . HOH   G 4 .   ? -1.95   8.518  29.075 1   21.56 ? 464 HOH   A O     1 
HETATM 4127 O O     . HOH   G 4 .   ? 7.051   28.339 50.741 1   21.04 ? 465 HOH   A O     1 
HETATM 4128 O O     . HOH   G 4 .   ? 3.214   7.759  39.573 1   18.61 ? 466 HOH   A O     1 
HETATM 4129 O O     . HOH   G 4 .   ? 12.492  18.58  43.763 1   19.88 ? 467 HOH   A O     1 
HETATM 4130 O O     . HOH   G 4 .   ? 8.664   36.464 24.612 1   24.91 ? 468 HOH   A O     1 
HETATM 4131 O O     . HOH   G 4 .   ? 12.845  18.978 25.359 1   50.29 ? 469 HOH   A O     1 
HETATM 4132 O O     . HOH   G 4 .   ? -19.341 28.582 31.157 1   34.58 ? 470 HOH   A O     1 
HETATM 4133 O O     . HOH   G 4 .   ? -2.954  31.076 21.571 1   27.58 ? 471 HOH   A O     1 
HETATM 4134 O O     . HOH   G 4 .   ? 19.867  24.46  31.91  1   33.11 ? 472 HOH   A O     1 
HETATM 4135 O O     . HOH   G 4 .   ? -8.707  11.849 29.901 1   33.15 ? 473 HOH   A O     1 
HETATM 4136 O O     . HOH   G 4 .   ? 5.168   5.873  40.27  1   23.15 ? 474 HOH   A O     1 
HETATM 4137 O O     . HOH   G 4 .   ? 19.491  26.023 45.224 1   32.7  ? 475 HOH   A O     1 
HETATM 4138 O O     . HOH   G 4 .   ? 0.908   24.435 42.573 1   17.8  ? 476 HOH   A O     1 
HETATM 4139 O O     . HOH   G 4 .   ? -2.554  7.431  47.021 1   38.78 ? 477 HOH   A O     1 
HETATM 4140 O O     . HOH   G 4 .   ? -11.077 40.67  36.352 1   42.91 ? 478 HOH   A O     1 
HETATM 4141 O O     . HOH   G 4 .   ? -4.854  29.829 22.982 1   25.15 ? 479 HOH   A O     1 
HETATM 4142 O O     . HOH   G 4 .   ? -3.919  9.314  48.317 1   26.41 ? 480 HOH   A O     1 
HETATM 4143 O O     . HOH   G 4 .   ? 9.044   -3.106 34.411 1   33.87 ? 481 HOH   A O     1 
HETATM 4144 O O     . HOH   G 4 .   ? -4.954  37.639 23.221 1   21.9  ? 482 HOH   A O     1 
HETATM 4145 O O     . HOH   G 4 .   ? -11.248 40.435 49.929 1   47.39 ? 483 HOH   A O     1 
HETATM 4146 O O     . HOH   G 4 .   ? -6.161  20.771 24.964 1   31.89 ? 484 HOH   A O     1 
HETATM 4147 O O     . HOH   G 4 .   ? 2.527   45.265 37.3   1   33.21 ? 485 HOH   A O     1 
HETATM 4148 O O     . HOH   G 4 .   ? 2.093   22.005 64.833 1   40.08 ? 486 HOH   A O     1 
HETATM 4149 O O     . HOH   G 4 .   ? -8.882  22.179 55.54  1   60.97 ? 487 HOH   A O     1 
HETATM 4150 O O     . HOH   G 4 .   ? 21.099  14.726 41.656 1   28    ? 488 HOH   A O     1 
HETATM 4151 O O     . HOH   G 4 .   ? 15.173  10.942 44.133 1   31.77 ? 489 HOH   A O     1 
HETATM 4152 O O     . HOH   G 4 .   ? 4.297   10.814 22.041 1   31.33 ? 490 HOH   A O     1 
HETATM 4153 O O     . HOH   G 4 .   ? 21.046  26.785 48.266 1   54.98 ? 491 HOH   A O     1 
HETATM 4154 O O     . HOH   G 4 .   ? -11.747 32.804 42.462 1   28.42 ? 492 HOH   A O     1 
HETATM 4155 O O     . HOH   G 4 .   ? -6.887  11.734 53.38  1   37.82 ? 493 HOH   A O     1 
HETATM 4156 O O     . HOH   G 4 .   ? 9.906   3.59   32.351 1   27.02 ? 494 HOH   A O     1 
HETATM 4157 O O     . HOH   G 4 .   ? 15.886  26.725 29.02  1   25.27 ? 495 HOH   A O     1 
HETATM 4158 O O     . HOH   G 4 .   ? 12.889  6.813  36.108 1   40.83 ? 496 HOH   A O     1 
HETATM 4159 O O     . HOH   G 4 .   ? -8.205  24.18  27.081 1   35.26 ? 497 HOH   A O     1 
HETATM 4160 O O     . HOH   G 4 .   ? 9.186   0.416  39.707 1   40.83 ? 498 HOH   A O     1 
HETATM 4161 O O     . HOH   G 4 .   ? 9.523   29.483 51.19  1   21.85 ? 499 HOH   A O     1 
HETATM 4162 O O     . HOH   G 4 .   ? -16.79  27.579 48.037 1   45.3  ? 500 HOH   A O     1 
HETATM 4163 O O     . HOH   G 4 .   ? 3.453   17.275 60.93  1   44.47 ? 501 HOH   A O     1 
HETATM 4164 O O     . HOH   G 4 .   ? 7.762   2.66   39.229 1   26.74 ? 502 HOH   A O     1 
HETATM 4165 O O     . HOH   G 4 .   ? 9.396   45.12  38.453 1   27.78 ? 503 HOH   A O     1 
HETATM 4166 O O     . HOH   G 4 .   ? -2.964  43.229 43.689 1   39.13 ? 504 HOH   A O     1 
HETATM 4167 O O     . HOH   G 4 .   ? 17.873  26.272 27.212 1   33.23 ? 505 HOH   A O     1 
HETATM 4168 O O     . HOH   G 4 .   ? 5.277   16.9   24.918 1   26.74 ? 506 HOH   A O     1 
HETATM 4169 O O     . HOH   G 4 .   ? -6.333  31.9   24.101 1   31.37 ? 507 HOH   A O     1 
HETATM 4170 O O     . HOH   G 4 .   ? 10.327  3.349  42.481 1   44.36 ? 508 HOH   A O     1 
HETATM 4171 O O     . HOH   G 4 .   ? 5.596   17.628 58.472 1   32.7  ? 509 HOH   A O     1 
HETATM 4172 O O     . HOH   G 4 .   ? 3.99    14.564 58.9   1   39.6  ? 510 HOH   A O     1 
HETATM 4173 O O     . HOH   G 4 .   ? 10.8    16.528 53.164 1   34.41 ? 511 HOH   A O     1 
HETATM 4174 O O     . HOH   G 4 .   ? -17.759 21     39.442 1   34.81 ? 512 HOH   A O     1 
HETATM 4175 O O     . HOH   G 4 .   ? 13.472  30.334 38.691 1   26.49 ? 513 HOH   A O     1 
HETATM 4176 O O     . HOH   G 4 .   ? 16.495  25.657 62.579 1   50.65 ? 514 HOH   A O     1 
HETATM 4177 O O     . HOH   G 4 .   ? 17.148  18.535 27.547 1   34.63 ? 515 HOH   A O     1 
HETATM 4178 O O     . HOH   G 4 .   ? -6.341  37.328 32.274 1   24.48 ? 516 HOH   A O     1 
HETATM 4179 O O     . HOH   G 4 .   ? -11.886 31.446 31.659 1   38.22 ? 517 HOH   A O     1 
HETATM 4180 O O     . HOH   G 4 .   ? 1.912   16.076 51.865 1   21.97 ? 518 HOH   A O     1 
HETATM 4181 O O     . HOH   G 4 .   ? -1.207  5.466  43.975 1   44.26 ? 519 HOH   A O     1 
HETATM 4182 O O     . HOH   G 4 .   ? 11.295  9.267  39.322 1   30.91 ? 520 HOH   A O     1 
HETATM 4183 O O     . HOH   G 4 .   ? -3.677  16.409 32.508 1   22.23 ? 521 HOH   A O     1 
HETATM 4184 O O     . HOH   G 4 .   ? 3.554   31.851 23.547 1   27.15 ? 522 HOH   A O     1 
HETATM 4185 O O     . HOH   G 4 .   ? 20.636  18.532 51.327 1   62.47 ? 523 HOH   A O     1 
HETATM 4186 O O     . HOH   G 4 .   ? -7.523  37.024 28.539 1   30.46 ? 524 HOH   A O     1 
HETATM 4187 O O     . HOH   G 4 .   ? -0.134  21.61  63.676 1   38.76 ? 525 HOH   A O     1 
HETATM 4188 O O     . HOH   G 4 .   ? 10.514  38.432 64.753 1   45.62 ? 526 HOH   A O     1 
HETATM 4189 O O     . HOH   G 4 .   ? -3.83   15.409 27.223 1   38.11 ? 527 HOH   A O     1 
HETATM 4190 O O     . HOH   G 4 .   ? 10.108  11.435 25.474 1   48.23 ? 528 HOH   A O     1 
HETATM 4191 O O     . HOH   G 4 .   ? 4.654   20.978 34.958 1   17.28 ? 529 HOH   A O     1 
HETATM 4192 O O     . HOH   G 4 .   ? 22.884  17.629 48.365 1   58.35 ? 530 HOH   A O     1 
HETATM 4193 O O     . HOH   G 4 .   ? -6.744  14.34  28.216 1   40.01 ? 531 HOH   A O     1 
HETATM 4194 O O     . HOH   G 4 .   ? -13.843 28.027 38.243 1   25.55 ? 532 HOH   A O     1 
HETATM 4195 O O     . HOH   G 4 .   ? 2.386   23.67  20.855 1   35.23 ? 533 HOH   A O     1 
HETATM 4196 O O     . HOH   G 4 .   ? 18.822  26.502 23.757 1   45.97 ? 534 HOH   A O     1 
HETATM 4197 O O     . HOH   G 4 .   ? 10.838  32.133 61.007 1   32.01 ? 535 HOH   A O     1 
HETATM 4198 O O     . HOH   G 4 .   ? 20.879  17.534 36.214 1   35.12 ? 536 HOH   A O     1 
HETATM 4199 O O     . HOH   G 4 .   ? 21.676  13.567 36.184 1   47.36 ? 537 HOH   A O     1 
HETATM 4200 O O     . HOH   G 4 .   ? -9.963  9.782  41.354 1   47.59 ? 538 HOH   A O     1 
HETATM 4201 O O     . HOH   G 4 .   ? 21.772  21.006 35.947 1   32.02 ? 539 HOH   A O     1 
HETATM 4202 O O     . HOH   G 4 .   ? 17.294  24.239 23.472 1   57.53 ? 540 HOH   A O     1 
HETATM 4203 O O     . HOH   G 4 .   ? 19.74   31.536 33.812 1   28.86 ? 541 HOH   A O     1 
HETATM 4204 O O     . HOH   G 4 .   ? -9.501  23.955 22.81  1   46.63 ? 542 HOH   A O     1 
HETATM 4205 O O     . HOH   G 4 .   ? -11.075 27.645 28.059 1   38.97 ? 543 HOH   A O     1 
HETATM 4206 O O     . HOH   G 4 .   ? 11.443  13.681 54.191 1   41.77 ? 544 HOH   A O     1 
HETATM 4207 O O     . HOH   G 4 .   ? -13.286 22.292 35.672 1   42.38 ? 545 HOH   A O     1 
HETATM 4208 O O     . HOH   G 4 .   ? 14.306  16.69  47.636 1   28.52 ? 546 HOH   A O     1 
HETATM 4209 O O     . HOH   G 4 .   ? 23.516  25.491 37.867 1   37.21 ? 547 HOH   A O     1 
HETATM 4210 O O     . HOH   G 4 .   ? 17.042  13.151 30.891 1   43    ? 548 HOH   A O     1 
HETATM 4211 O O     . HOH   G 4 .   ? -7.477  10.485 41.823 1   30.67 ? 549 HOH   A O     1 
HETATM 4212 O O     . HOH   G 4 .   ? -15.195 34.976 41.473 1   52.17 ? 550 HOH   A O     1 
HETATM 4213 O O     . HOH   G 4 .   ? -4.475  42.072 48.661 1   59.64 ? 551 HOH   A O     1 
HETATM 4214 O O     . HOH   G 4 .   ? -1.546  15.615 30.8   1   26.41 ? 552 HOH   A O     1 
HETATM 4215 O O     . HOH   G 4 .   ? 19.666  20.008 30.519 1   36.91 ? 553 HOH   A O     1 
HETATM 4216 O O     . HOH   G 4 .   ? -15.598 25.268 31.838 1   23.37 ? 554 HOH   A O     1 
HETATM 4217 O O     . HOH   G 4 .   ? -13.018 21.125 38.078 1   40.77 ? 555 HOH   A O     1 
HETATM 4218 O O     . HOH   G 4 .   ? 0.248   7.077  47.334 1   38.88 ? 556 HOH   A O     1 
HETATM 4219 O O     . HOH   G 4 .   ? 4.689   37.9   55.449 1   47.93 ? 557 HOH   A O     1 
HETATM 4220 O O     . HOH   G 4 .   ? 20.97   26.794 51.175 1   48.87 ? 558 HOH   A O     1 
HETATM 4221 O O     . HOH   G 4 .   ? -3.35   41.232 45.216 1   37.34 ? 559 HOH   A O     1 
HETATM 4222 O O     . HOH   G 4 .   ? 10.507  29.869 23.628 1   22.51 ? 560 HOH   A O     1 
HETATM 4223 O O     . HOH   G 4 .   ? 9.332   27.317 23.24  1   25.04 ? 561 HOH   A O     1 
HETATM 4224 O O     . HOH   G 4 .   ? -6.654  40.072 31.543 1   26.66 ? 562 HOH   A O     1 
HETATM 4225 O O     . HOH   G 4 .   ? -10.543 37.18  33.534 1   27.79 ? 563 HOH   A O     1 
HETATM 4226 O O     . HOH   G 4 .   ? 5.297   4.868  31.633 1   20.54 ? 564 HOH   A O     1 
HETATM 4227 O O     . HOH   G 4 .   ? 14.461  28.878 27.944 1   24.02 ? 565 HOH   A O     1 
HETATM 4228 O O     . HOH   G 4 .   ? -3.404  30.947 59.137 1   33.46 ? 566 HOH   A O     1 
HETATM 4229 O O     . HOH   G 4 .   ? -14.055 19.838 48.773 1   62.77 ? 567 HOH   A O     1 
HETATM 4230 O O     . HOH   G 4 .   ? 7.885   10.78  55.1   1   33.32 ? 568 HOH   A O     1 
HETATM 4231 O O     . HOH   G 4 .   ? 2.879   25.649 36.912 1   18.1  ? 569 HOH   A O     1 
HETATM 4232 O O     . HOH   G 4 .   ? 23.041  18.698 39.59  1   36.56 ? 570 HOH   A O     1 
HETATM 4233 O O     . HOH   G 4 .   ? 6.469   43.886 51.764 1   44.94 ? 571 HOH   A O     1 
HETATM 4234 O O     . HOH   G 4 .   ? 19.102  8.436  33.245 1   40.29 ? 572 HOH   A O     1 
HETATM 4235 O O     . HOH   G 4 .   ? 17.248  34.883 57.343 1   49.67 ? 573 HOH   A O     1 
HETATM 4236 O O     . HOH   G 4 .   ? 3.733   18.782 23.831 1   34.7  ? 574 HOH   A O     1 
HETATM 4237 O O     . HOH   G 4 .   ? 12.187  8.412  27.625 1   42.71 ? 575 HOH   A O     1 
HETATM 4238 O O     . HOH   G 4 .   ? -16.331 31.541 41.384 1   51.57 ? 576 HOH   A O     1 
HETATM 4239 O O     . HOH   G 4 .   ? 5.401   41.578 43.396 1   42.21 ? 577 HOH   A O     1 
HETATM 4240 O O     . HOH   G 4 .   ? -2.675  13.387 23.386 1   32.39 ? 578 HOH   A O     1 
HETATM 4241 O O     . HOH   G 4 .   ? -13.856 35.919 35.913 1   49.34 ? 579 HOH   A O     1 
HETATM 4242 O O     . HOH   G 4 .   ? -0.978  5.463  41.287 1   39.35 ? 580 HOH   A O     1 
HETATM 4243 O O     . HOH   G 4 .   ? -9.552  19.324 27.64  1   42.22 ? 581 HOH   A O     1 
HETATM 4244 O O     . HOH   G 4 .   ? 14.121  13.763 46.737 1   37.66 ? 582 HOH   A O     1 
HETATM 4245 O O     . HOH   G 4 .   ? 12.182  23.915 63.074 1   66.54 ? 583 HOH   A O     1 
HETATM 4246 O O     . HOH   G 4 .   ? -6.972  41.306 50.203 1   36.95 ? 584 HOH   A O     1 
HETATM 4247 O O     . HOH   G 4 .   ? 0.516   29.325 64.288 1   38.85 ? 585 HOH   A O     1 
HETATM 4248 O O     . HOH   G 4 .   ? -6.798  28.719 21.628 1   39.1  ? 586 HOH   A O     1 
HETATM 4249 O O     . HOH   G 4 .   ? 3.651   4.011  46.93  1   61.4  ? 587 HOH   A O     1 
HETATM 4250 O O     . HOH   G 4 .   ? 4.356   43.233 45.194 1   43.46 ? 588 HOH   A O     1 
HETATM 4251 O O     . HOH   G 4 .   ? 1.569   14.518 60.039 1   48.39 ? 589 HOH   A O     1 
HETATM 4252 O O     . HOH   G 4 .   ? -14.286 20.485 44.099 1   32.94 ? 590 HOH   A O     1 
HETATM 4253 O O     . HOH   G 4 .   ? -12.053 20.913 52.102 1   50.86 ? 591 HOH   A O     1 
HETATM 4254 O O     . HOH   G 4 .   ? -9.755  42.518 34.874 1   44.87 ? 592 HOH   A O     1 
HETATM 4255 O O     . HOH   G 4 .   ? -9.398  12.883 52.111 1   52.94 ? 593 HOH   A O     1 
HETATM 4256 O O     . HOH   G 4 .   ? 11.6    39.022 30.866 1   38.19 ? 594 HOH   A O     1 
HETATM 4257 O O     . HOH   G 4 .   ? -15.264 30.774 50.039 1   49.05 ? 595 HOH   A O     1 
HETATM 4258 O O     . HOH   G 4 .   ? -2.691  7.592  59.721 1   70    ? 596 HOH   A O     1 
HETATM 4259 O O     . HOH   G 4 .   ? 21.276  14.727 48.979 1   52.6  ? 597 HOH   A O     1 
HETATM 4260 O O     . HOH   G 4 .   ? 22.397  15.088 52.362 1   49.81 ? 598 HOH   A O     1 
HETATM 4261 O O     . HOH   G 4 .   ? 14.187  7.134  33.541 1   48.64 ? 599 HOH   A O     1 
HETATM 4262 O O     . HOH   G 4 .   ? -13.607 21.978 50.689 1   57.89 ? 600 HOH   A O     1 
HETATM 4263 O O     . HOH   G 4 .   ? 7.799   32.973 21.584 1   32.46 ? 601 HOH   A O     1 
HETATM 4264 O O     . HOH   G 4 .   ? -6.666  3.326  34.333 1   27.25 ? 602 HOH   A O     1 
HETATM 4265 O O     . HOH   G 4 .   ? -15.103 20.314 39.633 1   38.82 ? 603 HOH   A O     1 
HETATM 4266 O O     . HOH   G 4 .   ? -7.300  39.710 28.791 1   22.08 ? 604 HOH   A O     1 
HETATM 4267 O O     . HOH   G 4 .   ? -5.345  17.599 28.581 1   32.65 ? 605 HOH   A O     1 
HETATM 4268 O O     . HOH   G 4 .   ? 9.653   31.025 21.17  1   31.11 ? 606 HOH   A O     1 
HETATM 4269 O O     . HOH   G 4 .   ? 5.225   2.385  37.959 1   27.3  ? 607 HOH   A O     1 
HETATM 4270 O O     . HOH   G 4 .   ? -9.354  43.892 47.961 1   42.49 ? 608 HOH   A O     1 
HETATM 4271 O O     . HOH   G 4 .   ? 16.808  36.182 65.897 1   45.83 ? 609 HOH   A O     1 
HETATM 4272 O O     . HOH   G 4 .   ? 11.607  7.545  30.029 1   56.53 ? 610 HOH   A O     1 
HETATM 4273 O O     . HOH   G 4 .   ? -9.514  14.593 28.293 1   42.34 ? 611 HOH   A O     1 
HETATM 4274 O O     . HOH   G 4 .   ? 3.515   3.843  39.411 1   27.56 ? 612 HOH   A O     1 
HETATM 4275 O O     . HOH   G 4 .   ? 21.254  21.989 30.148 1   28.63 ? 613 HOH   A O     1 
HETATM 4276 O O     . HOH   G 4 .   ? 5.222   31.922 21.398 1   28.83 ? 614 HOH   A O     1 
HETATM 4277 O O     . HOH   G 4 .   ? -6.753  2.365  37.467 1   35.76 ? 615 HOH   A O     1 
HETATM 4278 O O     . HOH   G 4 .   ? -12.984 36.127 33.137 1   44.82 ? 616 HOH   A O     1 
HETATM 4279 O O     . HOH   G 4 .   ? 9.982   5.455  29.939 1   32.11 ? 617 HOH   A O     1 
HETATM 4280 O O     . HOH   G 4 .   ? -15.969 20.649 46.27  1   39.59 ? 618 HOH   A O     1 
HETATM 4281 O O     . HOH   H 4 .   ? 10.793  47.329 27.217 1   30.85 ? 401 HOH   B O     1 
HETATM 4282 O O     . HOH   H 4 .   ? 36.071  27.648 43.802 1   45.05 ? 402 HOH   B O     1 
HETATM 4283 O O     . HOH   H 4 .   ? 22.667  46.106 30.497 1   38.13 ? 403 HOH   B O     1 
HETATM 4284 O O     . HOH   H 4 .   ? 9.57    53.347 47.326 1   55.11 ? 404 HOH   B O     1 
HETATM 4285 O O     . HOH   H 4 .   ? 26.617  27.971 36.678 1   40.57 ? 405 HOH   B O     1 
HETATM 4286 O O     . HOH   H 4 .   ? 12.651  50.947 23.677 1   39.45 ? 406 HOH   B O     1 
HETATM 4287 O O     . HOH   H 4 .   ? 33.944  62.764 50.477 1   43.51 ? 407 HOH   B O     1 
HETATM 4288 O O     . HOH   H 4 .   ? 39.034  44.515 52.575 1   29.36 ? 408 HOH   B O     1 
HETATM 4289 O O     . HOH   H 4 .   ? 52.871  44.434 42.825 1   35.08 ? 409 HOH   B O     1 
HETATM 4290 O O     . HOH   H 4 .   ? 14.305  36.945 56.805 1   32.69 ? 410 HOH   B O     1 
HETATM 4291 O O     . HOH   H 4 .   ? 23.378  68.54  41.077 1   33.06 ? 411 HOH   B O     1 
HETATM 4292 O O     . HOH   H 4 .   ? 37.754  42.93  61.941 1   38.24 ? 412 HOH   B O     1 
HETATM 4293 O O     . HOH   H 4 .   ? 21.892  74.674 33.425 1   34.82 ? 413 HOH   B O     1 
HETATM 4294 O O     . HOH   H 4 .   ? 41.844  59.047 33.840 1   28.35 ? 414 HOH   B O     1 
HETATM 4295 O O     . HOH   H 4 .   ? 43.709  55.566 34.58  1   30.62 ? 415 HOH   B O     1 
HETATM 4296 O O     . HOH   H 4 .   ? 35.664  34.261 23.665 1   30.87 ? 416 HOH   B O     1 
HETATM 4297 O O     . HOH   H 4 .   ? 20.74   31.863 47.535 1   55.29 ? 417 HOH   B O     1 
HETATM 4298 O O     . HOH   H 4 .   ? 15.778  51.878 26.208 1   43.38 ? 418 HOH   B O     1 
HETATM 4299 O O     . HOH   H 4 .   ? 16.286  62.297 30.81  1   33.29 ? 419 HOH   B O     1 
HETATM 4300 O O     . HOH   H 4 .   ? 35.449  58.783 25.233 1   35.91 ? 420 HOH   B O     1 
HETATM 4301 O O     . HOH   H 4 .   ? 42.775  35.878 41.1   1   32.05 ? 421 HOH   B O     1 
HETATM 4302 O O     . HOH   H 4 .   ? 39.435  33.89  48.677 1   31.15 ? 422 HOH   B O     1 
HETATM 4303 O O     . HOH   H 4 .   ? 43.877  48.893 54.262 1   45.49 ? 423 HOH   B O     1 
HETATM 4304 O O     . HOH   H 4 .   ? 34.651  61.561 41.274 1   23.52 ? 424 HOH   B O     1 
HETATM 4305 O O     . HOH   H 4 .   ? 32.556  66.267 43.605 1   40.61 ? 425 HOH   B O     1 
HETATM 4306 O O     . HOH   H 4 .   ? 13.343  55.763 32.713 1   42.05 ? 426 HOH   B O     1 
HETATM 4307 O O     . HOH   H 4 .   ? 25.41   32.479 51.782 1   44.04 ? 427 HOH   B O     1 
HETATM 4308 O O     . HOH   H 4 .   ? 6.935   46.422 37.496 1   40.91 ? 428 HOH   B O     1 
HETATM 4309 O O     . HOH   H 4 .   ? 20.807  40.452 60.009 1   37.1  ? 429 HOH   B O     1 
HETATM 4310 O O     . HOH   H 4 .   ? 15.153  35.959 33.029 1   28.68 ? 430 HOH   B O     1 
HETATM 4311 O O     . HOH   H 4 .   ? 18.66   66.335 34.921 1   54.46 ? 431 HOH   B O     1 
HETATM 4312 O O     . HOH   H 4 .   ? 30.917  29.845 29.156 1   22.18 ? 432 HOH   B O     1 
HETATM 4313 O O     . HOH   H 4 .   ? 20.645  70.948 31.829 1   43.18 ? 433 HOH   B O     1 
HETATM 4314 O O     . HOH   H 4 .   ? 29.708  56.661 31.682 1   16.21 ? 434 HOH   B O     1 
HETATM 4315 O O     . HOH   H 4 .   ? 13.131  45.985 26.752 1   47.97 ? 435 HOH   B O     1 
HETATM 4316 O O     . HOH   H 4 .   ? 31.752  39.752 57.907 1   28.13 ? 436 HOH   B O     1 
HETATM 4317 O O     . HOH   H 4 .   ? 16.022  44.881 63.737 1   30.64 ? 437 HOH   B O     1 
HETATM 4318 O O     . HOH   H 4 .   ? 26.002  45.404 32.886 1   23.5  ? 438 HOH   B O     1 
HETATM 4319 O O     . HOH   H 4 .   ? 30.354  30.599 47.774 1   53.23 ? 439 HOH   B O     1 
HETATM 4320 O O     . HOH   H 4 .   ? 29.608  67.444 37.153 1   23.02 ? 440 HOH   B O     1 
HETATM 4321 O O     . HOH   H 4 .   ? 27.732  50.675 64.774 1   30.98 ? 441 HOH   B O     1 
HETATM 4322 O O     . HOH   H 4 .   ? 46.834  43.509 40.463 1   30.17 ? 442 HOH   B O     1 
HETATM 4323 O O     . HOH   H 4 .   ? 16.025  61.709 43.254 1   32.56 ? 443 HOH   B O     1 
HETATM 4324 O O     . HOH   H 4 .   ? 28.047  62.641 52.745 1   39.44 ? 444 HOH   B O     1 
HETATM 4325 O O     . HOH   H 4 .   ? 18.149  42.475 23.395 1   44.62 ? 445 HOH   B O     1 
HETATM 4326 O O     . HOH   H 4 .   ? 28.337  36.182 59.76  1   47.19 ? 446 HOH   B O     1 
HETATM 4327 O O     . HOH   H 4 .   ? 40.831  30.692 37.346 1   37.63 ? 447 HOH   B O     1 
HETATM 4328 O O     . HOH   H 4 .   ? 29.716  62.548 30.387 1   18.99 ? 448 HOH   B O     1 
HETATM 4329 O O     . HOH   H 4 .   ? 45.793  46.692 30.765 1   28.64 ? 449 HOH   B O     1 
HETATM 4330 O O     . HOH   H 4 .   ? 20.105  52.724 41.938 1   20.04 ? 450 HOH   B O     1 
HETATM 4331 O O     . HOH   H 4 .   ? 22.091  52.75  61.087 1   47.55 ? 451 HOH   B O     1 
HETATM 4332 O O     . HOH   H 4 .   ? 21.568  44.57  67.353 1   32.12 ? 452 HOH   B O     1 
HETATM 4333 O O     . HOH   H 4 .   ? 35.116  40.068 59.415 1   32.96 ? 453 HOH   B O     1 
HETATM 4334 O O     . HOH   H 4 .   ? 15.575  59.145 53.871 1   43.03 ? 454 HOH   B O     1 
HETATM 4335 O O     . HOH   H 4 .   ? 44.461  49.153 43.295 1   23.58 ? 455 HOH   B O     1 
HETATM 4336 O O     . HOH   H 4 .   ? 14.072  53.338 27.207 1   35.65 ? 456 HOH   B O     1 
HETATM 4337 O O     . HOH   H 4 .   ? 38.356  65.538 33.452 1   31.13 ? 457 HOH   B O     1 
HETATM 4338 O O     . HOH   H 4 .   ? 24.769  63.465 50.037 1   39.82 ? 458 HOH   B O     1 
HETATM 4339 O O     . HOH   H 4 .   ? 22.071  49.143 29.517 1   24.18 ? 459 HOH   B O     1 
HETATM 4340 O O     . HOH   H 4 .   ? 30.558  54.062 22.53  1   37.84 ? 460 HOH   B O     1 
HETATM 4341 O O     . HOH   H 4 .   ? 43.742  52.849 34.756 1   24.84 ? 461 HOH   B O     1 
HETATM 4342 O O     . HOH   H 4 .   ? 33.44   52.066 20.457 1   44.07 ? 462 HOH   B O     1 
HETATM 4343 O O     . HOH   H 4 .   ? 12.976  54.595 30.608 1   43.58 ? 463 HOH   B O     1 
HETATM 4344 O O     . HOH   H 4 .   ? 44.165  40.721 37.989 1   24.17 ? 464 HOH   B O     1 
HETATM 4345 O O     . HOH   H 4 .   ? 36.152  49.505 57.456 1   27.26 ? 465 HOH   B O     1 
HETATM 4346 O O     . HOH   H 4 .   ? 19.151  59.234 60.824 1   47.73 ? 466 HOH   B O     1 
HETATM 4347 O O     . HOH   H 4 .   ? 41.678  54.771 49.631 1   62.05 ? 467 HOH   B O     1 
HETATM 4348 O O     . HOH   H 4 .   ? 24.852  34.488 55.682 1   46.57 ? 468 HOH   B O     1 
HETATM 4349 O O     . HOH   H 4 .   ? 45.656  39.685 35.243 1   38.13 ? 469 HOH   B O     1 
HETATM 4350 O O     . HOH   H 4 .   ? 26.213  52.85  63.719 1   47.18 ? 470 HOH   B O     1 
HETATM 4351 O O     . HOH   H 4 .   ? 31.128  63.828 52.607 1   44.85 ? 471 HOH   B O     1 
HETATM 4352 O O     . HOH   H 4 .   ? 21.474  71.77  38.769 1   48.84 ? 472 HOH   B O     1 
HETATM 4353 O O     . HOH   H 4 .   ? 33.963  40.197 22.036 1   28.02 ? 473 HOH   B O     1 
HETATM 4354 O O     . HOH   H 4 .   ? 32.417  55.91  30.887 1   23.23 ? 474 HOH   B O     1 
HETATM 4355 O O     . HOH   H 4 .   ? 30.084  50.95  63.71  1   26.58 ? 475 HOH   B O     1 
HETATM 4356 O O     . HOH   H 4 .   ? 39.108  35.814 33.111 1   23.24 ? 476 HOH   B O     1 
HETATM 4357 O O     . HOH   H 4 .   ? 24.771  41.59  61.741 1   41.13 ? 477 HOH   B O     1 
HETATM 4358 O O     . HOH   H 4 .   ? 24.836  36.047 59.915 1   49.59 ? 478 HOH   B O     1 
HETATM 4359 O O     . HOH   H 4 .   ? 12.818  37.8   42.488 1   39.08 ? 479 HOH   B O     1 
HETATM 4360 O O     . HOH   H 4 .   ? 21.454  68.285 31.716 1   29.22 ? 480 HOH   B O     1 
HETATM 4361 O O     . HOH   H 4 .   ? 10.264  44.107 60.477 1   43.99 ? 481 HOH   B O     1 
HETATM 4362 O O     . HOH   H 4 .   ? 14.519  58.13  46.761 1   57.67 ? 482 HOH   B O     1 
HETATM 4363 O O     . HOH   H 4 .   ? 27.432  25.339 39.185 1   36.14 ? 483 HOH   B O     1 
HETATM 4364 O O     . HOH   H 4 .   ? 22.242  35.31  24.851 1   28.73 ? 484 HOH   B O     1 
HETATM 4365 O O     . HOH   H 4 .   ? 28.75   36.9   23.166 1   36.41 ? 485 HOH   B O     1 
HETATM 4366 O O     . HOH   H 4 .   ? 33.541  64.775 46.734 1   39.84 ? 486 HOH   B O     1 
HETATM 4367 O O     . HOH   H 4 .   ? 35.997  53.079 31.449 1   16.05 ? 487 HOH   B O     1 
HETATM 4368 O O     . HOH   H 4 .   ? 41.734  38.737 43.618 1   21.79 ? 488 HOH   B O     1 
HETATM 4369 O O     . HOH   H 4 .   ? 29.747  58.626 52.947 1   22.06 ? 489 HOH   B O     1 
HETATM 4370 O O     . HOH   H 4 .   ? 33.506  63.116 28.809 1   24.95 ? 490 HOH   B O     1 
HETATM 4371 O O     . HOH   H 4 .   ? 22.844  44.252 50.624 1   18.7  ? 491 HOH   B O     1 
HETATM 4372 O O     . HOH   H 4 .   ? 13.965  60.13  42.871 1   36.43 ? 492 HOH   B O     1 
HETATM 4373 O O     . HOH   H 4 .   ? 24.826  42.486 49.857 1   17.18 ? 493 HOH   B O     1 
HETATM 4374 O O     . HOH   H 4 .   ? 18.141  54.081 43.315 1   21.31 ? 494 HOH   B O     1 
HETATM 4375 O O     . HOH   H 4 .   ? 24.833  58.847 26.161 1   37.57 ? 495 HOH   B O     1 
HETATM 4376 O O     . HOH   H 4 .   ? 37.306  50.433 25.122 1   37.88 ? 496 HOH   B O     1 
HETATM 4377 O O     . HOH   H 4 .   ? 42.173  33.504 39.871 1   42.07 ? 497 HOH   B O     1 
HETATM 4378 O O     . HOH   H 4 .   ? 8.692   48.031 41.451 1   41.48 ? 498 HOH   B O     1 
HETATM 4379 O O     . HOH   H 4 .   ? 39.528  36.728 53.983 1   34.09 ? 499 HOH   B O     1 
HETATM 4380 O O     . HOH   H 4 .   ? 19.001  58.897 53.695 1   44.29 ? 500 HOH   B O     1 
HETATM 4381 O O     . HOH   H 4 .   ? 28.009  64.232 39.186 1   18.92 ? 501 HOH   B O     1 
HETATM 4382 O O     . HOH   H 4 .   ? 37.73   60.221 53.343 1   36.93 ? 502 HOH   B O     1 
HETATM 4383 O O     . HOH   H 4 .   ? 20.295  43.351 50.978 1   18.56 ? 503 HOH   B O     1 
HETATM 4384 O O     . HOH   H 4 .   ? 25.863  54.895 24.791 1   26.55 ? 504 HOH   B O     1 
HETATM 4385 O O     . HOH   H 4 .   ? 19.558  51.783 61.108 1   36.27 ? 505 HOH   B O     1 
HETATM 4386 O O     . HOH   H 4 .   ? 32.552  41.482 59.841 1   24.46 ? 506 HOH   B O     1 
HETATM 4387 O O     . HOH   H 4 .   ? 10.907  47.301 31.539 1   33.21 ? 507 HOH   B O     1 
HETATM 4388 O O     . HOH   H 4 .   ? 9.8     58.325 40.493 1   35.7  ? 508 HOH   B O     1 
HETATM 4389 O O     . HOH   H 4 .   ? 34.893  62.708 48.21  1   25    ? 509 HOH   B O     1 
HETATM 4390 O O     . HOH   H 4 .   ? 27.322  41.259 64.769 1   47.16 ? 510 HOH   B O     1 
HETATM 4391 O O     . HOH   H 4 .   ? 35.91   41.28  23.651 1   26.7  ? 511 HOH   B O     1 
HETATM 4392 O O     . HOH   H 4 .   ? 43.382  57.567 37.606 1   42.01 ? 512 HOH   B O     1 
HETATM 4393 O O     . HOH   H 4 .   ? 26.142  66.253 39.683 1   22.84 ? 513 HOH   B O     1 
HETATM 4394 O O     . HOH   H 4 .   ? 42.529  40.028 32.669 1   34.25 ? 514 HOH   B O     1 
HETATM 4395 O O     . HOH   H 4 .   ? 15.01   45.457 28.65  1   26.53 ? 515 HOH   B O     1 
HETATM 4396 O O     . HOH   H 4 .   ? 37.321  39.578 24.961 1   34.41 ? 516 HOH   B O     1 
HETATM 4397 O O     . HOH   H 4 .   ? 9.37    46.475 50.864 1   50.26 ? 517 HOH   B O     1 
HETATM 4398 O O     . HOH   H 4 .   ? 24.863  55.132 58.226 1   27.62 ? 518 HOH   B O     1 
HETATM 4399 O O     . HOH   H 4 .   ? 36.991  31.532 32.706 1   26.17 ? 519 HOH   B O     1 
HETATM 4400 O O     . HOH   H 4 .   ? 18.205  64.304 36.482 1   41.32 ? 520 HOH   B O     1 
HETATM 4401 O O     . HOH   H 4 .   ? 30.086  39.922 23.796 1   34.72 ? 521 HOH   B O     1 
HETATM 4402 O O     . HOH   H 4 .   ? 23.137  67.213 46.353 1   39.4  ? 522 HOH   B O     1 
HETATM 4403 O O     . HOH   H 4 .   ? 27.004  55.452 60.877 1   37.72 ? 523 HOH   B O     1 
HETATM 4404 O O     . HOH   H 4 .   ? 26.031  29.142 30.939 1   26.91 ? 524 HOH   B O     1 
HETATM 4405 O O     . HOH   H 4 .   ? 42.242  39.585 51.256 1   38.96 ? 525 HOH   B O     1 
HETATM 4406 O O     . HOH   H 4 .   ? 29.554  47.673 42.691 1   15.6  ? 526 HOH   B O     1 
HETATM 4407 O O     . HOH   H 4 .   ? 7.572   43.261 31.687 1   34.65 ? 527 HOH   B O     1 
HETATM 4408 O O     . HOH   H 4 .   ? 39.357  45.568 62.874 1   37.11 ? 528 HOH   B O     1 
HETATM 4409 O O     . HOH   H 4 .   ? 35.797  31.935 27.355 1   18.86 ? 529 HOH   B O     1 
HETATM 4410 O O     . HOH   H 4 .   ? 38.61   29.878 51.303 1   58.48 ? 530 HOH   B O     1 
HETATM 4411 O O     . HOH   H 4 .   ? 30.776  65.048 46.838 1   39.42 ? 531 HOH   B O     1 
HETATM 4412 O O     . HOH   H 4 .   ? 28.488  43.716 64.704 1   32.62 ? 532 HOH   B O     1 
HETATM 4413 O O     . HOH   H 4 .   ? 34.832  52.614 62.098 1   54.17 ? 533 HOH   B O     1 
HETATM 4414 O O     . HOH   H 4 .   ? 48.606  50.136 41.161 1   32.28 ? 534 HOH   B O     1 
HETATM 4415 O O     . HOH   H 4 .   ? 15.107  44.363 66.273 1   52.56 ? 535 HOH   B O     1 
HETATM 4416 O O     . HOH   H 4 .   ? 41.155  61.834 41.455 1   41.56 ? 536 HOH   B O     1 
HETATM 4417 O O     . HOH   H 4 .   ? 28.705  47.357 21.018 1   32.88 ? 537 HOH   B O     1 
HETATM 4418 O O     . HOH   H 4 .   ? 36.722  34.355 33.179 1   24.07 ? 538 HOH   B O     1 
HETATM 4419 O O     . HOH   H 4 .   ? 27.317  39.637 23.828 1   26.11 ? 539 HOH   B O     1 
HETATM 4420 O O     . HOH   H 4 .   ? 39.011  27.348 43.331 1   30.74 ? 540 HOH   B O     1 
HETATM 4421 O O     . HOH   H 4 .   ? 18.953  34.763 64.965 1   42.67 ? 541 HOH   B O     1 
HETATM 4422 O O     . HOH   H 4 .   ? 37.841  47.066 59.528 1   38.31 ? 542 HOH   B O     1 
HETATM 4423 O O     . HOH   H 4 .   ? 32.487  28.522 44.657 1   41.02 ? 543 HOH   B O     1 
HETATM 4424 O O     . HOH   H 4 .   ? 18.421  41.148 60.947 1   27.33 ? 544 HOH   B O     1 
HETATM 4425 O O     . HOH   H 4 .   ? 28.989  68.883 41.248 1   43.63 ? 545 HOH   B O     1 
HETATM 4426 O O     . HOH   H 4 .   ? 28.773  56.221 51.777 1   19.74 ? 546 HOH   B O     1 
HETATM 4427 O O     . HOH   H 4 .   ? 26.184  50.971 34.804 1   16.12 ? 547 HOH   B O     1 
HETATM 4428 O O     . HOH   H 4 .   ? 20.986  27.202 38.703 1   18.77 ? 548 HOH   B O     1 
HETATM 4429 O O     . HOH   H 4 .   ? 23.073  32.029 46.244 1   39.47 ? 549 HOH   B O     1 
HETATM 4430 O O     . HOH   H 4 .   ? 16.982  65.21  33.168 1   43.58 ? 550 HOH   B O     1 
HETATM 4431 O O     . HOH   H 4 .   ? 44.269  52.345 48.824 1   45.89 ? 551 HOH   B O     1 
HETATM 4432 O O     . HOH   H 4 .   ? 29.448  59.527 61.442 1   53.71 ? 552 HOH   B O     1 
HETATM 4433 O O     . HOH   H 4 .   ? 42.53   50.781 51.906 1   34.27 ? 553 HOH   B O     1 
HETATM 4434 O O     . HOH   H 4 .   ? 19.937  62.799 38.681 1   27.65 ? 554 HOH   B O     1 
HETATM 4435 O O     . HOH   H 4 .   ? 40.187  52.426 28.917 1   31.33 ? 555 HOH   B O     1 
HETATM 4436 O O     . HOH   H 4 .   ? 23.374  69.44  38.584 1   26.51 ? 556 HOH   B O     1 
HETATM 4437 O O     . HOH   H 4 .   ? 36.275  50.992 59.603 1   35.99 ? 557 HOH   B O     1 
HETATM 4438 O O     . HOH   H 4 .   ? 22.89   29.08  52.727 1   46    ? 558 HOH   B O     1 
HETATM 4439 O O     . HOH   H 4 .   ? 40.985  44.743 28.624 1   35.15 ? 559 HOH   B O     1 
HETATM 4440 O O     . HOH   H 4 .   ? 38.065  42.587 22.356 1   41.04 ? 560 HOH   B O     1 
HETATM 4441 O O     . HOH   H 4 .   ? 21.773  30.688 30.298 1   39.02 ? 561 HOH   B O     1 
HETATM 4442 O O     . HOH   H 4 .   ? 32.337  63.789 48.483 1   41.42 ? 562 HOH   B O     1 
HETATM 4443 O O     . HOH   H 4 .   ? 21.869  60.333 24.732 1   38.99 ? 563 HOH   B O     1 
HETATM 4444 O O     . HOH   H 4 .   ? 16.271  62.425 46.138 1   48.64 ? 564 HOH   B O     1 
HETATM 4445 O O     . HOH   H 4 .   ? 32.69   30.86  45.93  1   30.6  ? 565 HOH   B O     1 
HETATM 4446 O O     . HOH   H 4 .   ? 9.166   51.763 35.69  1   37.78 ? 566 HOH   B O     1 
HETATM 4447 O O     . HOH   H 4 .   ? 33.506  29.858 49.271 1   46.34 ? 567 HOH   B O     1 
HETATM 4448 O O     . HOH   H 4 .   ? 40.539  59.006 30.252 1   31.7  ? 568 HOH   B O     1 
HETATM 4449 O O     . HOH   H 4 .   ? 17.64   49.407 62.932 1   38.67 ? 569 HOH   B O     1 
HETATM 4450 O O     . HOH   H 4 .   ? 32.133  33.204 55.49  1   39.57 ? 570 HOH   B O     1 
HETATM 4451 O O     . HOH   H 4 .   ? 23.233  61.943 54.671 1   31.32 ? 571 HOH   B O     1 
HETATM 4452 O O     . HOH   H 4 .   ? 16.245  58.052 25.229 1   31.66 ? 572 HOH   B O     1 
HETATM 4453 O O     . HOH   H 4 .   ? 26.518  57.938 58.805 1   39.6  ? 573 HOH   B O     1 
HETATM 4454 O O     . HOH   H 4 .   ? 9.437   50.408 33.377 1   38.77 ? 574 HOH   B O     1 
HETATM 4455 O O     . HOH   H 4 .   ? 19.977  36.886 39.845 1   26.44 ? 575 HOH   B O     1 
HETATM 4456 O O     . HOH   H 4 .   ? 38.412  61.293 41.727 1   27.16 ? 576 HOH   B O     1 
HETATM 4457 O O     . HOH   H 4 .   ? 34.304  50.265 63.202 1   37.18 ? 577 HOH   B O     1 
HETATM 4458 O O     . HOH   H 4 .   ? 34.693  55.135 32.495 1   17.03 ? 578 HOH   B O     1 
HETATM 4459 O O     . HOH   H 4 .   ? 44.357  43.218 39.319 1   22.16 ? 579 HOH   B O     1 
HETATM 4460 O O     . HOH   H 4 .   ? 43.316  51.060 28.161 1   42.31 ? 580 HOH   B O     1 
HETATM 4461 O O     . HOH   H 4 .   ? 16.498  43.201 27.677 1   22.82 ? 581 HOH   B O     1 
HETATM 4462 O O     . HOH   H 4 .   ? 16.423  55.992 47.139 1   28.43 ? 582 HOH   B O     1 
HETATM 4463 O O     . HOH   H 4 .   ? 10.552  40.969 33.778 1   29.28 ? 583 HOH   B O     1 
HETATM 4464 O O     . HOH   H 4 .   ? 27.79   46.363 37.088 1   17.24 ? 584 HOH   B O     1 
HETATM 4465 O O     . HOH   H 4 .   ? 9.957   54.71  35.428 1   36.23 ? 585 HOH   B O     1 
HETATM 4466 O O     . HOH   H 4 .   ? 21.783  44.485 23.224 1   24.94 ? 586 HOH   B O     1 
HETATM 4467 O O     . HOH   H 4 .   ? 39.611  47.281 27.493 1   31.74 ? 587 HOH   B O     1 
HETATM 4468 O O     . HOH   H 4 .   ? 34.107  58.62  23.211 1   44.72 ? 588 HOH   B O     1 
HETATM 4469 O O     . HOH   H 4 .   ? 40.866  34.408 34.622 1   26.65 ? 589 HOH   B O     1 
HETATM 4470 O O     . HOH   H 4 .   ? 38.324  34.655 29.625 1   38.5  ? 590 HOH   B O     1 
HETATM 4471 O O     . HOH   H 4 .   ? 19.985  68.929 41.288 1   52.15 ? 591 HOH   B O     1 
HETATM 4472 O O     . HOH   H 4 .   ? 43.929  50.279 38.95  1   32.66 ? 592 HOH   B O     1 
HETATM 4473 O O     . HOH   H 4 .   ? 44.188  52.499 45.814 1   29.06 ? 593 HOH   B O     1 
HETATM 4474 O O     . HOH   H 4 .   ? 37.971  56.172 28.669 1   22.73 ? 594 HOH   B O     1 
HETATM 4475 O O     . HOH   H 4 .   ? 45.155  47.919 51.207 1   48.24 ? 595 HOH   B O     1 
HETATM 4476 O O     . HOH   H 4 .   ? 20.016  56.02  52.984 1   30.72 ? 596 HOH   B O     1 
HETATM 4477 O O     . HOH   H 4 .   ? 20.468  41.947 23.591 1   22.41 ? 597 HOH   B O     1 
HETATM 4478 O O     . HOH   H 4 .   ? 32.065  37.327 19.81  1   51.02 ? 598 HOH   B O     1 
HETATM 4479 O O     . HOH   H 4 .   ? 46.721  45.933 33.299 1   34.94 ? 599 HOH   B O     1 
HETATM 4480 O O     . HOH   H 4 .   ? 17.042  59.218 46.486 1   48.22 ? 600 HOH   B O     1 
HETATM 4481 O O     . HOH   H 4 .   ? 15.668  42.32  25.436 1   50.22 ? 601 HOH   B O     1 
HETATM 4482 O O     . HOH   H 4 .   ? 39.181  49.729 55.549 1   39.97 ? 602 HOH   B O     1 
HETATM 4483 O O     . HOH   H 4 .   ? 46.734  39.673 32.147 1   51.22 ? 603 HOH   B O     1 
HETATM 4484 O O     . HOH   H 4 .   ? 33.931  64.386 57.914 1   42.4  ? 604 HOH   B O     1 
HETATM 4485 O O     . HOH   H 4 .   ? 18.445  53.208 24.766 1   56.29 ? 605 HOH   B O     1 
HETATM 4486 O O     . HOH   H 4 .   ? 22.564  47.349 67.435 1   33.14 ? 606 HOH   B O     1 
HETATM 4487 O O     . HOH   H 4 .   ? 18.602  66.238 45.397 1   56.02 ? 607 HOH   B O     1 
HETATM 4488 O O     . HOH   H 4 .   ? 36.015  30.542 51.089 1   44.05 ? 608 HOH   B O     1 
HETATM 4489 O O     . HOH   H 4 .   ? 22.853  39.228 61.553 1   50.24 ? 609 HOH   B O     1 
HETATM 4490 O O     . HOH   H 4 .   ? 18.657  33.055 31.181 1   36.87 ? 610 HOH   B O     1 
HETATM 4491 O O     . HOH   H 4 .   ? 10.88   57.899 48.036 1   63.39 ? 611 HOH   B O     1 
HETATM 4492 O O     . HOH   H 4 .   ? 44.791  40.701 51.457 1   40.69 ? 612 HOH   B O     1 
HETATM 4493 O O     . HOH   H 4 .   ? 44.386  49.319 36.576 1   41.32 ? 613 HOH   B O     1 
HETATM 4494 O O     . HOH   H 4 .   ? 7.691   44.432 45.505 1   41.72 ? 614 HOH   B O     1 
HETATM 4495 O O     . HOH   H 4 .   ? 34.481  25.829 43.737 1   49.48 ? 615 HOH   B O     1 
HETATM 4496 O O     . HOH   H 4 .   ? 26.692  57.782 24.586 1   49.72 ? 616 HOH   B O     1 
HETATM 4497 O O     . HOH   H 4 .   ? 28.746  57.38  59.91  1   51.71 ? 617 HOH   B O     1 
HETATM 4498 O O     . HOH   H 4 .   ? 25.127  26.144 33.931 1   49.13 ? 618 HOH   B O     1 
HETATM 4499 O O     . HOH   H 4 .   ? 15.089  54.46  25.589 1   40.78 ? 619 HOH   B O     1 
HETATM 4500 O O     . HOH   H 4 .   ? 31.553  41.353 21.864 1   32.93 ? 620 HOH   B O     1 
HETATM 4501 O O     . HOH   H 4 .   ? 45.914  50.958 40.901 1   38.17 ? 621 HOH   B O     1 
HETATM 4502 O O     . HOH   H 4 .   ? 37.779  32.053 29.608 1   28.64 ? 622 HOH   B O     1 
HETATM 4503 O O     . HOH   H 4 .   ? 38.777  52.124 55.699 1   51.28 ? 623 HOH   B O     1 
HETATM 4504 O O     . HOH   H 4 .   ? 37.972  68.325 33.636 1   27.64 ? 624 HOH   B O     1 
HETATM 4505 O O     . HOH   H 4 .   ? 31.178  43.123 64.248 1   33.51 ? 625 HOH   B O     1 
HETATM 4506 O O     . HOH   H 4 .   ? 21.511  40.57  21.288 1   32.22 ? 626 HOH   B O     1 
HETATM 4507 O O     . HOH   H 4 .   ? 44.732  50.252 50.642 1   58.92 ? 627 HOH   B O     1 
HETATM 4508 O O     . HOH   H 4 .   ? 18.864  68.541 38.548 1   47.46 ? 628 HOH   B O     1 
HETATM 4509 O O     . HOH   H 4 .   ? 28.446  49.805 67.42  1   48.53 ? 629 HOH   B O     1 
HETATM 4510 O O     . HOH   H 4 .   ? 15.706  47.417 63.415 1   52.83 ? 630 HOH   B O     1 
HETATM 4511 O O     . HOH   H 4 .   ? 19.908  46.031 21.858 1   39.27 ? 631 HOH   B O     1 
HETATM 4512 O O     . HOH   H 4 .   ? 41.837  57.554 47.72  1   70.05 ? 632 HOH   B O     1 
HETATM 4513 O O     . HOH   H 4 .   ? 41.531  36.644 51.712 1   38.72 ? 633 HOH   B O     1 
HETATM 4514 O O     . HOH   H 4 .   ? 37.495  53.482 29.127 1   23.64 ? 634 HOH   B O     1 
HETATM 4515 O O     . HOH   H 4 .   ? 38.912  26.843 45.862 1   48.04 ? 635 HOH   B O     1 
HETATM 4516 O O     . HOH   H 4 .   ? 10.521  43.289 54.736 1   48.12 ? 636 HOH   B O     1 
HETATM 4517 O O     . HOH   H 4 .   ? 19.681  64.315 29.583 1   34.87 ? 637 HOH   B O     1 
HETATM 4518 O O     . HOH   H 4 .   ? 37.192  51.847 27.115 1   30.14 ? 638 HOH   B O     1 
HETATM 4519 O O     . HOH   H 4 .   ? 32.505  41.18  62.673 1   34.16 ? 639 HOH   B O     1 
HETATM 4520 O O     . HOH   H 4 .   ? 27.678  68.277 38.843 1   26.69 ? 640 HOH   B O     1 
HETATM 4521 O O     . HOH   H 4 .   ? 25.717  39.681 21.582 1   29.2  ? 641 HOH   B O     1 
HETATM 4522 O O     . HOH   H 4 .   ? 26.017  46.687 21.476 1   35.21 ? 642 HOH   B O     1 
HETATM 4523 O O     . HOH   H 4 .   ? 21.44   66.444 29.322 1   31.42 ? 643 HOH   B O     1 
HETATM 4524 O O     . HOH   H 4 .   ? 20.972  48.98  68.804 1   37.47 ? 644 HOH   B O     1 
HETATM 4525 O O     . HOH   H 4 .   ? 24.208  44.535 22.022 1   42.34 ? 645 HOH   B O     1 
HETATM 4526 O O     . HOH   H 4 .   ? 24.501  42.098 20.649 1   41.24 ? 646 HOH   B O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLY   A 23  ? 0.4973 0.3017 0.3229 -0.0517 -0.0522 -0.0134 4   GLY   A N   
2    C CA  . GLY   A 23  ? 0.4747 0.2837 0.3064 -0.0454 -0.0364 -0.0181 4   GLY   A CA  
3    C C   . GLY   A 23  ? 0.4327 0.2654 0.2938 -0.0371 -0.0328 -0.0161 4   GLY   A C   
4    O O   . GLY   A 23  ? 0.4593 0.2964 0.3268 -0.0321 -0.0211 -0.0189 4   GLY   A O   
5    N N   . PHE   A 24  ? 0.3504 0.1978 0.2302 -0.0358 -0.0426 -0.0115 5   PHE   A N   
6    C CA  . PHE   A 24  ? 0.3298 0.1982 0.2351 -0.0292 -0.0401 -0.0097 5   PHE   A CA  
7    C C   . PHE   A 24  ? 0.3167 0.1947 0.2387 -0.0276 -0.0438 -0.0086 5   PHE   A C   
8    O O   . PHE   A 24  ? 0.3298 0.2027 0.2497 -0.032  -0.0528 -0.0072 5   PHE   A O   
9    C CB  . PHE   A 24  ? 0.3139 0.1893 0.2259 -0.0301 -0.0472 -0.0056 5   PHE   A CB  
10   C CG  . PHE   A 24  ? 0.3008 0.1929 0.2311 -0.0243 -0.0417 -0.0049 5   PHE   A CG  
11   C CD1 . PHE   A 24  ? 0.2995 0.1907 0.2246 -0.0225 -0.0339 -0.0061 5   PHE   A CD1 
12   C CD2 . PHE   A 24  ? 0.2959 0.2036 0.2478 -0.0213 -0.0439 -0.0033 5   PHE   A CD2 
13   C CE1 . PHE   A 24  ? 0.2801 0.1861 0.2217 -0.0178 -0.0301 -0.0052 5   PHE   A CE1 
14   C CE2 . PHE   A 24  ? 0.2911 0.2122 0.257  -0.017  -0.0393 -0.0029 5   PHE   A CE2 
15   C CZ  . PHE   A 24  ? 0.2647 0.1849 0.2255 -0.0152 -0.033  -0.0038 5   PHE   A CZ  
16   N N   . THR   A 25  ? 0.2914 0.1829 0.2301 -0.0222 -0.038  -0.0088 6   THR   A N   
17   C CA  . THR   A 25  ? 0.2896 0.1905 0.2435 -0.021  -0.0403 -0.0075 6   THR   A CA  
18   C C   . THR   A 25  ? 0.3115 0.2172 0.2746 -0.0242 -0.0499 -0.0045 6   THR   A C   
19   O O   . THR   A 25  ? 0.3112 0.2234 0.2813 -0.024  -0.0528 -0.0025 6   THR   A O   
20   C CB  . THR   A 25  ? 0.2714 0.1865 0.2404 -0.0159 -0.0343 -0.0069 6   THR   A CB  
21   O OG1 . THR   A 25  ? 0.2738 0.1849 0.2385 -0.0129 -0.0264 -0.0092 6   THR   A OG1 
22   C CG2 . THR   A 25  ? 0.2706 0.1951 0.2535 -0.0154 -0.0359 -0.0053 6   THR   A CG2 
23   N N   . SER   A 26  ? 0.326  0.2283 0.2908 -0.0271 -0.0549 -0.004  7   SER   A N   
24   C CA  . SER   A 26  ? 0.317  0.2249 0.2952 -0.0301 -0.0639 -0.001  7   SER   A CA  
25   C C   . SER   A 26  ? 0.2955 0.2205 0.2954 -0.0267 -0.0598 0.0001  7   SER   A C   
26   O O   . SER   A 26  ? 0.2844 0.2141 0.2866 -0.0238 -0.0526 -0.0011 7   SER   A O   
27   C CB  . SER   A 26  ? 0.3268 0.2265 0.3021 -0.0344 -0.0696 -0.0009 7   SER   A CB  
28   O OG  . SER   A 26  ? 0.3438 0.2464 0.3232 -0.0322 -0.0634 -0.0023 7   SER   A OG  
29   N N   . LYS   A 27  ? 0.3032 0.2363 0.3188 -0.0276 -0.0644 0.0023  8   LYS   A N   
30   C CA  . LYS   A 27  ? 0.3035 0.2509 0.3376 -0.0251 -0.0589 0.0023  8   LYS   A CA  
31   C C   . LYS   A 27  ? 0.286  0.2368 0.3267 -0.0258 -0.0552 0.0019  8   LYS   A C   
32   O O   . LYS   A 27  ? 0.2728 0.231  0.3183 -0.0237 -0.0479 0.001   8   LYS   A O   
33   C CB  . LYS   A 27  ? 0.3759 0.3313 0.4285 -0.0256 -0.0629 0.0041  8   LYS   A CB  
34   C CG  . LYS   A 27  ? 0.408  0.3652 0.4772 -0.0292 -0.07   0.0063  8   LYS   A CG  
35   C CD  . LYS   A 27  ? 0.3984 0.3631 0.488  -0.0289 -0.0737 0.0081  8   LYS   A CD  
36   C CE  . LYS   A 27  ? 0.3993 0.3581 0.4802 -0.0289 -0.0802 0.01    8   LYS   A CE  
37   N NZ  . LYS   A 27  ? 0.3657 0.329  0.4693 -0.0301 -0.0883 0.0133  8   LYS   A NZ  
38   N N   . ASP   A 28  ? 0.2849 0.2293 0.3246 -0.0293 -0.0608 0.0027  9   ASP   A N   
39   C CA  . ASP   A 28  ? 0.2762 0.2227 0.322  -0.0306 -0.0578 0.0027  9   ASP   A CA  
40   C C   . ASP   A 28  ? 0.2816 0.2253 0.3154 -0.028  -0.0508 0.0013  9   ASP   A C   
41   O O   . ASP   A 28  ? 0.292  0.2391 0.3305 -0.0285 -0.0465 0.0017  9   ASP   A O   
42   C CB  . ASP   A 28  ? 0.329  0.2675 0.3747 -0.0352 -0.066  0.0038  9   ASP   A CB  
43   C CG  . ASP   A 28  ? 0.4169 0.3406 0.4404 -0.0361 -0.0688 0.0024  9   ASP   A CG  
44   O OD1 . ASP   A 28  ? 0.5047 0.4232 0.5207 -0.0358 -0.0652 0.0012  9   ASP   A OD1 
45   O OD2 . ASP   A 28  ? 0.4611 0.3776 0.4741 -0.037  -0.0737 0.0024  9   ASP   A OD2 
46   N N   . THR   A 29  ? 0.2671 0.2041 0.286  -0.0255 -0.0492 -0.0001 10  THR   A N   
47   C CA  . THR   A 29  ? 0.2679 0.2029 0.2795 -0.0225 -0.0431 -0.001  10  THR   A CA  
48   C C   . THR   A 29  ? 0.2546 0.2003 0.2743 -0.0204 -0.0376 -0.0002 10  THR   A C   
49   O O   . THR   A 29  ? 0.2468 0.1925 0.265  -0.0195 -0.0342 0.0005  10  THR   A O   
50   C CB  . THR   A 29  ? 0.2974 0.224  0.2951 -0.0203 -0.0415 -0.0029 10  THR   A CB  
51   O OG1 . THR   A 29  ? 0.3438 0.2581 0.3308 -0.0236 -0.0465 -0.004  10  THR   A OG1 
52   C CG2 . THR   A 29  ? 0.2918 0.2155 0.2855 -0.0171 -0.0357 -0.0037 10  THR   A CG2 
53   N N   . TYR   A 30  ? 0.2349 0.1889 0.2623 -0.0199 -0.037  -0.0002 11  TYR   A N   
54   C CA  . TYR   A 30  ? 0.2268 0.1894 0.2598 -0.0189 -0.0317 0       11  TYR   A CA  
55   C C   . TYR   A 30  ? 0.2541 0.2202 0.2943 -0.0221 -0.0293 0.0008  11  TYR   A C   
56   O O   . TYR   A 30  ? 0.2793 0.2481 0.3177 -0.0223 -0.0248 0.0013  11  TYR   A O   
57   C CB  . TYR   A 30  ? 0.2174 0.1866 0.2568 -0.0178 -0.0311 -0.0008 11  TYR   A CB  
58   C CG  . TYR   A 30  ? 0.2047 0.1717 0.2357 -0.0146 -0.0305 -0.0014 11  TYR   A CG  
59   C CD1 . TYR   A 30  ? 0.1966 0.1665 0.2248 -0.0124 -0.0263 -0.0014 11  TYR   A CD1 
60   C CD2 . TYR   A 30  ? 0.2029 0.1637 0.2276 -0.0143 -0.0344 -0.0016 11  TYR   A CD2 
61   C CE1 . TYR   A 30  ? 0.2035 0.1714 0.226  -0.0095 -0.0253 -0.0018 11  TYR   A CE1 
62   C CE2 . TYR   A 30  ? 0.2107 0.1687 0.2273 -0.0118 -0.0324 -0.0024 11  TYR   A CE2 
63   C CZ  . TYR   A 30  ? 0.2092 0.1715 0.2263 -0.0091 -0.0275 -0.0025 11  TYR   A CZ  
64   O OH  . TYR   A 30  ? 0.2097 0.1699 0.2216 -0.0067 -0.0249 -0.0032 11  TYR   A OH  
65   N N   . LEU   A 31  ? 0.2652 0.2304 0.3131 -0.0252 -0.0324 0.0012  12  LEU   A N   
66   C CA  . LEU   A 31  ? 0.2854 0.2538 0.3411 -0.0287 -0.0287 0.0019  12  LEU   A CA  
67   C C   . LEU   A 31  ? 0.2887 0.2509 0.3347 -0.0297 -0.0278 0.0034  12  LEU   A C   
68   O O   . LEU   A 31  ? 0.3035 0.2672 0.3491 -0.0319 -0.023  0.0043  12  LEU   A O   
69   C CB  . LEU   A 31  ? 0.3035 0.2729 0.3731 -0.0318 -0.0328 0.0023  12  LEU   A CB  
70   C CG  . LEU   A 31  ? 0.3446 0.3194 0.4271 -0.0313 -0.0356 0.0017  12  LEU   A CG  
71   C CD1 . LEU   A 31  ? 0.3702 0.345  0.4679 -0.0346 -0.042  0.0031  12  LEU   A CD1 
72   C CD2 . LEU   A 31  ? 0.3628 0.3464 0.4552 -0.0309 -0.0276 0.0001  12  LEU   A CD2 
73   N N   . SER   A 32  ? 0.2849 0.2391 0.3222 -0.028  -0.0318 0.0036  13  SER   A N   
74   C CA  . SER   A 32  ? 0.2912 0.238  0.3217 -0.0288 -0.0322 0.005   13  SER   A CA  
75   C C   . SER   A 32  ? 0.3113 0.254  0.3327 -0.0253 -0.031  0.0057  13  SER   A C   
76   O O   . SER   A 32  ? 0.3622 0.3014 0.3807 -0.0261 -0.0302 0.008   13  SER   A O   
77   C CB  . SER   A 32  ? 0.3198 0.2587 0.3489 -0.0302 -0.0378 0.0043  13  SER   A CB  
78   O OG  . SER   A 32  ? 0.3201 0.2549 0.3431 -0.0281 -0.041  0.0024  13  SER   A OG  
79   N N   . HIS   A 33  ? 0.2511 0.1937 0.2689 -0.0216 -0.0311 0.0041  14  HIS   A N   
80   C CA  . HIS   A 33  ? 0.2496 0.1875 0.262  -0.0179 -0.0299 0.0044  14  HIS   A CA  
81   C C   . HIS   A 33  ? 0.2434 0.1876 0.2568 -0.0152 -0.0276 0.0051  14  HIS   A C   
82   O O   . HIS   A 33  ? 0.2442 0.1858 0.2565 -0.012  -0.0268 0.0057  14  HIS   A O   
83   C CB  . HIS   A 33  ? 0.2685 0.1982 0.2749 -0.0161 -0.0309 0.0016  14  HIS   A CB  
84   C CG  . HIS   A 33  ? 0.2965 0.2166 0.2994 -0.0186 -0.0335 0.001   14  HIS   A CG  
85   N ND1 . HIS   A 33  ? 0.3065 0.2269 0.312  -0.0228 -0.0374 0.0011  14  HIS   A ND1 
86   C CD2 . HIS   A 33  ? 0.3278 0.2382 0.3267 -0.0176 -0.0327 0.0005  14  HIS   A CD2 
87   C CE1 . HIS   A 33  ? 0.3291 0.2397 0.3306 -0.0246 -0.0393 0.0007  14  HIS   A CE1 
88   N NE2 . HIS   A 33  ? 0.3441 0.248  0.341  -0.0215 -0.0363 0.0001  14  HIS   A NE2 
89   N N   . PHE   A 34  ? 0.242  0.1944 0.2588 -0.0165 -0.0263 0.0047  15  PHE   A N   
90   C CA  . PHE   A 34  ? 0.2369 0.1947 0.2539 -0.0149 -0.0245 0.0053  15  PHE   A CA  
91   C C   . PHE   A 34  ? 0.2429 0.2014 0.2582 -0.0181 -0.0238 0.0081  15  PHE   A C   
92   O O   . PHE   A 34  ? 0.2376 0.1987 0.254  -0.022  -0.0218 0.0078  15  PHE   A O   
93   C CB  . PHE   A 34  ? 0.2169 0.1815 0.2378 -0.0149 -0.0232 0.0031  15  PHE   A CB  
94   C CG  . PHE   A 34  ? 0.2088 0.1783 0.2295 -0.0133 -0.0215 0.0032  15  PHE   A CG  
95   C CD1 . PHE   A 34  ? 0.2241 0.1964 0.2433 -0.016  -0.0199 0.0044  15  PHE   A CD1 
96   C CD2 . PHE   A 34  ? 0.2084 0.1788 0.2294 -0.01   -0.0214 0.0019  15  PHE   A CD2 
97   C CE1 . PHE   A 34  ? 0.2317 0.2078 0.2501 -0.0153 -0.019  0.0042  15  PHE   A CE1 
98   C CE2 . PHE   A 34  ? 0.2091 0.1844 0.2313 -0.009  -0.0202 0.0019  15  PHE   A CE2 
99   C CZ  . PHE   A 34  ? 0.21   0.1881 0.2311 -0.0116 -0.0194 0.0031  15  PHE   A CZ  
100  N N   . ASN   A 35  ? 0.2359 0.1911 0.2488 -0.0169 -0.0256 0.011   16  ASN   A N   
101  C CA  . ASN   A 35  ? 0.2528 0.2058 0.2611 -0.0207 -0.0267 0.0148  16  ASN   A CA  
102  C C   . ASN   A 35  ? 0.2543 0.2118 0.2596 -0.0222 -0.026  0.0153  16  ASN   A C   
103  O O   . ASN   A 35  ? 0.2518 0.2105 0.2589 -0.0192 -0.0282 0.0163  16  ASN   A O   
104  C CB  . ASN   A 35  ? 0.2739 0.2203 0.283  -0.0187 -0.0306 0.0184  16  ASN   A CB  
105  C CG  . ASN   A 35  ? 0.3144 0.2567 0.3177 -0.0232 -0.0334 0.0235  16  ASN   A CG  
106  O OD1 . ASN   A 35  ? 0.3307 0.2748 0.3275 -0.0272 -0.0333 0.0249  16  ASN   A OD1 
107  N ND2 . ASN   A 35  ? 0.371  0.3061 0.3753 -0.0231 -0.0363 0.0265  16  ASN   A ND2 
108  N N   . PRO   A 36  ? 0.2486 0.2083 0.2498 -0.0271 -0.0224 0.0142  17  PRO   A N   
109  C CA  . PRO   A 36  ? 0.272  0.2349 0.269  -0.0287 -0.0211 0.0135  17  PRO   A CA  
110  C C   . PRO   A 36  ? 0.2792 0.2381 0.2689 -0.0304 -0.0262 0.018   17  PRO   A C   
111  O O   . PRO   A 36  ? 0.2674 0.2291 0.2579 -0.0288 -0.028  0.018   17  PRO   A O   
112  C CB  . PRO   A 36  ? 0.2983 0.2621 0.292  -0.0343 -0.0148 0.011   17  PRO   A CB  
113  C CG  . PRO   A 36  ? 0.2962 0.2585 0.2942 -0.0354 -0.0133 0.0108  17  PRO   A CG  
114  C CD  . PRO   A 36  ? 0.2706 0.2302 0.2727 -0.031  -0.0184 0.0126  17  PRO   A CD  
115  N N   . ARG   A 37  ? 0.2892 0.2411 0.2722 -0.0342 -0.0292 0.0225  18  ARG   A N   
116  C CA  . ARG   A 37  ? 0.3078 0.2547 0.284  -0.0366 -0.0359 0.0279  18  ARG   A CA  
117  C C   . ARG   A 37  ? 0.296  0.2445 0.2842 -0.0299 -0.0416 0.0301  18  ARG   A C   
118  O O   . ARG   A 37  ? 0.3018 0.2509 0.2906 -0.0298 -0.0466 0.0328  18  ARG   A O   
119  C CB  . ARG   A 37  ? 0.3678 0.3054 0.3339 -0.0425 -0.0387 0.033   18  ARG   A CB  
120  C CG  . ARG   A 37  ? 0.4464 0.3774 0.404  -0.0463 -0.0476 0.0397  18  ARG   A CG  
121  C CD  . ARG   A 37  ? 0.5219 0.4543 0.4713 -0.0495 -0.0485 0.0387  18  ARG   A CD  
122  N NE  . ARG   A 37  ? 0.6033 0.5325 0.5369 -0.057  -0.0409 0.0353  18  ARG   A NE  
123  C CZ  . ARG   A 37  ? 0.6559 0.5748 0.5695 -0.0663 -0.0428 0.0388  18  ARG   A CZ  
124  N NH1 . ARG   A 37  ? 0.6603 0.5758 0.5605 -0.0732 -0.0332 0.0347  18  ARG   A NH1 
125  N NH2 . ARG   A 37  ? 0.6598 0.571  0.5668 -0.0692 -0.0542 0.0465  18  ARG   A NH2 
126  N N   . ASP   A 38  ? 0.2699 0.219  0.2682 -0.0245 -0.0403 0.0286  19  ASP   A N   
127  C CA  . ASP   A 38  ? 0.2698 0.2197 0.2805 -0.0182 -0.0432 0.0297  19  ASP   A CA  
128  C C   . ASP   A 38  ? 0.2601 0.2174 0.276  -0.0149 -0.0406 0.0261  19  ASP   A C   
129  O O   . ASP   A 38  ? 0.2585 0.2175 0.2821 -0.0124 -0.044  0.0283  19  ASP   A O   
130  C CB  . ASP   A 38  ? 0.303  0.2499 0.3201 -0.0143 -0.0408 0.0277  19  ASP   A CB  
131  C CG  . ASP   A 38  ? 0.372  0.3164 0.4016 -0.009  -0.043  0.0296  19  ASP   A CG  
132  O OD1 . ASP   A 38  ? 0.3995 0.343  0.4341 -0.0093 -0.0492 0.0349  19  ASP   A OD1 
133  O OD2 . ASP   A 38  ? 0.379  0.3213 0.4137 -0.005  -0.0389 0.026   19  ASP   A OD2 
134  N N   . TYR   A 39  ? 0.2438 0.2054 0.2564 -0.0153 -0.0351 0.0211  20  TYR   A N   
135  C CA  . TYR   A 39  ? 0.2106 0.1786 0.2271 -0.0129 -0.0328 0.018   20  TYR   A CA  
136  C C   . TYR   A 39  ? 0.2286 0.1979 0.2417 -0.0159 -0.0367 0.0206  20  TYR   A C   
137  O O   . TYR   A 39  ? 0.2246 0.1972 0.2451 -0.0131 -0.0384 0.0211  20  TYR   A O   
138  C CB  . TYR   A 39  ? 0.2049 0.1762 0.2183 -0.0142 -0.0275 0.0132  20  TYR   A CB  
139  C CG  . TYR   A 39  ? 0.2002 0.1772 0.2174 -0.0119 -0.0252 0.0101  20  TYR   A CG  
140  C CD1 . TYR   A 39  ? 0.1951 0.173  0.2185 -0.0071 -0.0241 0.0087  20  TYR   A CD1 
141  C CD2 . TYR   A 39  ? 0.208  0.1883 0.2215 -0.015  -0.0235 0.0085  20  TYR   A CD2 
142  C CE1 . TYR   A 39  ? 0.1938 0.1762 0.2199 -0.0054 -0.022  0.0062  20  TYR   A CE1 
143  C CE2 . TYR   A 39  ? 0.1945 0.1796 0.2122 -0.0129 -0.0214 0.0056  20  TYR   A CE2 
144  C CZ  . TYR   A 39  ? 0.1946 0.1808 0.2185 -0.0082 -0.0211 0.0049  20  TYR   A CZ  
145  O OH  . TYR   A 39  ? 0.1861 0.1763 0.2132 -0.0067 -0.0193 0.0027  20  TYR   A OH  
146  N N   . LEU   A 40  ? 0.2471 0.213  0.2484 -0.0223 -0.0378 0.0221  21  LEU   A N   
147  C CA  . LEU   A 40  ? 0.2633 0.228  0.2574 -0.0267 -0.042  0.0245  21  LEU   A CA  
148  C C   . LEU   A 40  ? 0.2746 0.2365 0.2745 -0.0258 -0.0511 0.0309  21  LEU   A C   
149  O O   . LEU   A 40  ? 0.2783 0.2428 0.2825 -0.0255 -0.0552 0.0323  21  LEU   A O   
150  C CB  . LEU   A 40  ? 0.2864 0.2453 0.2638 -0.0347 -0.0403 0.0247  21  LEU   A CB  
151  C CG  . LEU   A 40  ? 0.2905 0.2526 0.2652 -0.0361 -0.0308 0.0182  21  LEU   A CG  
152  C CD1 . LEU   A 40  ? 0.3389 0.2941 0.298  -0.0444 -0.0272 0.0182  21  LEU   A CD1 
153  C CD2 . LEU   A 40  ? 0.3026 0.2705 0.2809 -0.0344 -0.0283 0.0142  21  LEU   A CD2 
154  N N   . GLU   A 41  ? 0.273  0.23   0.276  -0.025  -0.0544 0.0348  22  GLU   A N   
155  C CA  . GLU   A 41  ? 0.2931 0.2476 0.3061 -0.0235 -0.0634 0.0413  22  GLU   A CA  
156  C C   . GLU   A 41  ? 0.2933 0.2543 0.3259 -0.0162 -0.0624 0.04    22  GLU   A C   
157  O O   . GLU   A 41  ? 0.3124 0.2745 0.3546 -0.0157 -0.0694 0.0443  22  GLU   A O   
158  C CB  . GLU   A 41  ? 0.3367 0.2845 0.3513 -0.0233 -0.0659 0.0451  22  GLU   A CB  
159  C CG  . GLU   A 41  ? 0.4365 0.376  0.4319 -0.0318 -0.069  0.0486  22  GLU   A CG  
160  C CD  . GLU   A 41  ? 0.5505 0.4848 0.5371 -0.0381 -0.0792 0.055   22  GLU   A CD  
161  O OE1 . GLU   A 41  ? 0.559  0.4887 0.5251 -0.046  -0.0781 0.0544  22  GLU   A OE1 
162  O OE2 . GLU   A 41  ? 0.582  0.5165 0.5824 -0.0354 -0.088  0.0603  22  GLU   A OE2 
163  N N   . LYS   A 42  ? 0.2765 0.2412 0.3151 -0.0109 -0.054  0.0343  23  LYS   A N   
164  C CA  . LYS   A 42  ? 0.2626 0.2317 0.3179 -0.0045 -0.051  0.0325  23  LYS   A CA  
165  C C   . LYS   A 42  ? 0.2439 0.2197 0.3015 -0.0043 -0.05   0.0305  23  LYS   A C   
166  O O   . LYS   A 42  ? 0.27   0.2491 0.3425 -0.0011 -0.0513 0.0319  23  LYS   A O   
167  C CB  . LYS   A 42  ? 0.2871 0.2555 0.3437 -0.0003 -0.0424 0.027   23  LYS   A CB  
168  C CG  . LYS   A 42  ? 0.3992 0.3619 0.4657 0.0032  -0.0423 0.0286  23  LYS   A CG  
169  C CD  . LYS   A 42  ? 0.4723 0.4287 0.5302 0.0004  -0.0441 0.0301  23  LYS   A CD  
170  C CE  . LYS   A 42  ? 0.4628 0.4134 0.534  0.0041  -0.0454 0.0326  23  LYS   A CE  
171  N NZ  . LYS   A 42  ? 0.4646 0.4097 0.5322 0.0001  -0.0533 0.0389  23  LYS   A NZ  
172  N N   . TYR   A 43  ? 0.2356 0.2132 0.2798 -0.0077 -0.0469 0.0269  24  TYR   A N   
173  C CA  . TYR   A 43  ? 0.2201 0.2034 0.2662 -0.0073 -0.045  0.0243  24  TYR   A CA  
174  C C   . TYR   A 43  ? 0.2266 0.2099 0.2635 -0.0131 -0.05   0.0259  24  TYR   A C   
175  O O   . TYR   A 43  ? 0.2333 0.221  0.2748 -0.0127 -0.0501 0.0247  24  TYR   A O   
176  C CB  . TYR   A 43  ? 0.2068 0.1925 0.2477 -0.0059 -0.0366 0.0181  24  TYR   A CB  
177  C CG  . TYR   A 43  ? 0.1971 0.1822 0.2456 -0.0005 -0.0315 0.0158  24  TYR   A CG  
178  C CD1 . TYR   A 43  ? 0.2021 0.1901 0.2607 0.0033  -0.0284 0.0146  24  TYR   A CD1 
179  C CD2 . TYR   A 43  ? 0.2046 0.185  0.2489 -0.0001 -0.0294 0.0147  24  TYR   A CD2 
180  C CE1 . TYR   A 43  ? 0.1964 0.1817 0.2587 0.0071  -0.0226 0.0119  24  TYR   A CE1 
181  C CE2 . TYR   A 43  ? 0.1993 0.177  0.2474 0.0037  -0.0247 0.0122  24  TYR   A CE2 
182  C CZ  . TYR   A 43  ? 0.2034 0.183  0.2594 0.0072  -0.0209 0.0106  24  TYR   A CZ  
183  O OH  . TYR   A 43  ? 0.214  0.1886 0.2707 0.01    -0.0151 0.0076  24  TYR   A OH  
184  N N   . TYR   A 44  ? 0.2468 0.2241 0.2691 -0.0192 -0.0534 0.028   25  TYR   A N   
185  C CA  . TYR   A 44  ? 0.2778 0.2528 0.2864 -0.026  -0.0559 0.0279  25  TYR   A CA  
186  C C   . TYR   A 44  ? 0.3214 0.2886 0.3205 -0.0325 -0.0662 0.0344  25  TYR   A C   
187  O O   . TYR   A 44  ? 0.3334 0.2953 0.3149 -0.0399 -0.0673 0.0339  25  TYR   A O   
188  C CB  . TYR   A 44  ? 0.2638 0.2378 0.2591 -0.0291 -0.0474 0.0222  25  TYR   A CB  
189  C CG  . TYR   A 44  ? 0.227  0.2081 0.2312 -0.0238 -0.0396 0.0164  25  TYR   A CG  
190  C CD1 . TYR   A 44  ? 0.2413 0.2266 0.2487 -0.0233 -0.0387 0.014   25  TYR   A CD1 
191  C CD2 . TYR   A 44  ? 0.2327 0.2156 0.2424 -0.0196 -0.0345 0.0141  25  TYR   A CD2 
192  C CE1 . TYR   A 44  ? 0.231  0.2219 0.2469 -0.0186 -0.033  0.0099  25  TYR   A CE1 
193  C CE2 . TYR   A 44  ? 0.2151 0.203  0.2318 -0.0155 -0.0293 0.0099  25  TYR   A CE2 
194  C CZ  . TYR   A 44  ? 0.221  0.2128 0.2407 -0.0149 -0.0286 0.0081  25  TYR   A CZ  
195  O OH  . TYR   A 44  ? 0.2127 0.2085 0.2388 -0.0113 -0.0243 0.0048  25  TYR   A OH  
196  N N   . LYS   A 45  ? 0.3524 0.318  0.3626 -0.0303 -0.0735 0.0405  26  LYS   A N   
197  C CA  . LYS   A 45  ? 0.4128 0.37   0.4151 -0.0368 -0.0856 0.0482  26  LYS   A CA  
198  C C   . LYS   A 45  ? 0.4479 0.4046 0.4481 -0.0412 -0.0938 0.0507  26  LYS   A C   
199  O O   . LYS   A 45  ? 0.4765 0.4237 0.4581 -0.0501 -0.1019 0.0547  26  LYS   A O   
200  C CB  . LYS   A 45  ? 0.4529 0.409  0.4725 -0.0324 -0.0918 0.0543  26  LYS   A CB  
201  C CG  . LYS   A 45  ? 0.5393 0.4846 0.5479 -0.0393 -0.1033 0.0626  26  LYS   A CG  
202  C CD  . LYS   A 45  ? 0.6235 0.5672 0.6487 -0.0344 -0.1065 0.0672  26  LYS   A CD  
203  C CE  . LYS   A 45  ? 0.7078 0.6396 0.7212 -0.0417 -0.1185 0.0761  26  LYS   A CE  
204  N NZ  . LYS   A 45  ? 0.7687 0.6923 0.7524 -0.0498 -0.114  0.0741  26  LYS   A NZ  
205  N N   . PHE   A 46  ? 0.4355 0.4011 0.4529 -0.0358 -0.0918 0.0483  27  PHE   A N   
206  C CA  . PHE   A 46  ? 0.4586 0.425  0.4764 -0.0394 -0.0986 0.0497  27  PHE   A CA  
207  C C   . PHE   A 46  ? 0.4986 0.4584 0.518  -0.0446 -0.1149 0.0592  27  PHE   A C   
208  O O   . PHE   A 46  ? 0.5194 0.4718 0.521  -0.0533 -0.1226 0.0613  27  PHE   A O   
209  C CB  . PHE   A 46  ? 0.4809 0.4436 0.4749 -0.046  -0.0931 0.0437  27  PHE   A CB  
210  C CG  . PHE   A 46  ? 0.4963 0.463  0.4935 -0.0468 -0.0938 0.0411  27  PHE   A CG  
211  C CD1 . PHE   A 46  ? 0.4955 0.473  0.514  -0.039  -0.0882 0.0381  27  PHE   A CD1 
212  C CD2 . PHE   A 46  ? 0.5242 0.4828 0.5012 -0.0562 -0.0989 0.041   27  PHE   A CD2 
213  C CE1 . PHE   A 46  ? 0.5032 0.484  0.5241 -0.04   -0.088  0.0353  27  PHE   A CE1 
214  C CE2 . PHE   A 46  ? 0.5256 0.4874 0.505  -0.0571 -0.0987 0.0378  27  PHE   A CE2 
215  C CZ  . PHE   A 46  ? 0.5143 0.4877 0.5167 -0.0488 -0.0935 0.0352  27  PHE   A CZ  
216  N N   . GLY   A 47  ? 0.5023 0.4635 0.5419 -0.0398 -0.1202 0.0649  28  GLY   A N   
217  C CA  . GLY   A 47  ? 0.53   0.4853 0.5762 -0.044  -0.1371 0.0751  28  GLY   A CA  
218  C C   . GLY   A 47  ? 0.5531 0.5135 0.6172 -0.044  -0.146  0.0783  28  GLY   A C   
219  O O   . GLY   A 47  ? 0.5654 0.5344 0.6375 -0.0403 -0.1379 0.0724  28  GLY   A O   
220  N N   . SER   A 51  ? 0.3053 0.3151 0.4867 -0.0019 -0.0922 0.0559  32  SER   A N   
221  C CA  . SER   A 51  ? 0.2843 0.2946 0.4678 0.0045  -0.0775 0.0499  32  SER   A CA  
222  C C   . SER   A 51  ? 0.2491 0.263  0.4216 0.0055  -0.0658 0.0423  32  SER   A C   
223  O O   . SER   A 51  ? 0.2526 0.2671 0.4099 0.001   -0.0686 0.041   32  SER   A O   
224  C CB  . SER   A 51  ? 0.3097 0.3127 0.473  0.0032  -0.077  0.0492  32  SER   A CB  
225  O OG  . SER   A 51  ? 0.3141 0.3143 0.4489 -0.0023 -0.0772 0.0463  32  SER   A OG  
226  N N   . ALA   A 52  ? 0.2296 0.2441 0.4068 0.0109  -0.0529 0.0371  33  ALA   A N   
227  C CA  . ALA   A 52  ? 0.2197 0.2356 0.3842 0.0114  -0.0424 0.0305  33  ALA   A CA  
228  C C   . ALA   A 52  ? 0.2198 0.2322 0.3566 0.0073  -0.0437 0.0279  33  ALA   A C   
229  O O   . ALA   A 52  ? 0.2228 0.2373 0.3496 0.0051  -0.0421 0.0251  33  ALA   A O   
230  C CB  . ALA   A 52  ? 0.2268 0.2405 0.396  0.0165  -0.0295 0.0259  33  ALA   A CB  
231  N N   . GLU   A 53  ? 0.2179 0.225  0.3439 0.0062  -0.0463 0.029   34  GLU   A N   
232  C CA  . GLU   A 53  ? 0.2149 0.2187 0.3174 0.0021  -0.0465 0.0265  34  GLU   A CA  
233  C C   . GLU   A 53  ? 0.2139 0.2179 0.3062 -0.0039 -0.0538 0.0281  34  GLU   A C   
234  O O   . GLU   A 53  ? 0.2313 0.2354 0.3095 -0.0064 -0.0504 0.024   34  GLU   A O   
235  C CB  . GLU   A 53  ? 0.2276 0.2253 0.3224 0.0013  -0.0489 0.0284  34  GLU   A CB  
236  C CG  . GLU   A 53  ? 0.2558 0.251  0.3536 0.006   -0.0407 0.0253  34  GLU   A CG  
237  C CD  . GLU   A 53  ? 0.263  0.2598 0.3814 0.0113  -0.0361 0.0252  34  GLU   A CD  
238  O OE1 . GLU   A 53  ? 0.2677 0.2654 0.4035 0.0123  -0.042  0.0302  34  GLU   A OE1 
239  O OE2 . GLU   A 53  ? 0.261  0.2576 0.3788 0.0141  -0.0266 0.0203  34  GLU   A OE2 
240  N N   . SER   A 54  ? 0.2307 0.2342 0.3307 -0.0066 -0.0644 0.0341  35  SER   A N   
241  C CA  . SER   A 54  ? 0.2507 0.2522 0.3382 -0.0135 -0.0719 0.0355  35  SER   A CA  
242  C C   . SER   A 54  ? 0.2255 0.2325 0.319  -0.0132 -0.0694 0.0328  35  SER   A C   
243  O O   . SER   A 54  ? 0.2579 0.263  0.336  -0.018  -0.0699 0.0301  35  SER   A O   
244  C CB  . SER   A 54  ? 0.2947 0.2922 0.3865 -0.0176 -0.0858 0.0435  35  SER   A CB  
245  O OG  . SER   A 54  ? 0.3608 0.3516 0.4424 -0.0192 -0.088  0.0459  35  SER   A OG  
246  N N   . GLN   A 55  ? 0.2202 0.2334 0.3356 -0.0077 -0.0657 0.0329  36  GLN   A N   
247  C CA  . GLN   A 55  ? 0.2268 0.2452 0.3484 -0.0075 -0.0627 0.0304  36  GLN   A CA  
248  C C   . GLN   A 55  ? 0.2144 0.2325 0.3206 -0.007  -0.0529 0.0237  36  GLN   A C   
249  O O   . GLN   A 55  ? 0.2273 0.246  0.3264 -0.0101 -0.053  0.0213  36  GLN   A O   
250  C CB  . GLN   A 55  ? 0.2417 0.266  0.3899 -0.002  -0.0585 0.0316  36  GLN   A CB  
251  C CG  . GLN   A 55  ? 0.2862 0.3123 0.4563 -0.0024 -0.0692 0.0388  36  GLN   A CG  
252  C CD  . GLN   A 55  ? 0.3526 0.3784 0.5192 -0.0089 -0.0809 0.042   36  GLN   A CD  
253  O OE1 . GLN   A 55  ? 0.3931 0.4131 0.547  -0.0146 -0.092  0.0459  36  GLN   A OE1 
254  N NE2 . GLN   A 55  ? 0.3784 0.4092 0.5532 -0.009  -0.0784 0.0402  36  GLN   A NE2 
255  N N   . ILE   A 56  ? 0.2003 0.2169 0.3021 -0.0034 -0.0453 0.0208  37  ILE   A N   
256  C CA  . ILE   A 56  ? 0.1943 0.2101 0.2832 -0.0031 -0.0377 0.0154  37  ILE   A CA  
257  C C   . ILE   A 56  ? 0.1987 0.2109 0.2698 -0.0084 -0.0404 0.0138  37  ILE   A C   
258  O O   . ILE   A 56  ? 0.2048 0.2178 0.2701 -0.01   -0.0375 0.0102  37  ILE   A O   
259  C CB  . ILE   A 56  ? 0.1961 0.2097 0.2842 0.001   -0.0309 0.0135  37  ILE   A CB  
260  C CG1 . ILE   A 56  ? 0.205  0.2208 0.3085 0.0056  -0.025  0.0134  37  ILE   A CG1 
261  C CG2 . ILE   A 56  ? 0.2069 0.2186 0.2809 0.0003  -0.026  0.0091  37  ILE   A CG2 
262  C CD1 . ILE   A 56  ? 0.1994 0.211  0.3027 0.0091  -0.0191 0.012   37  ILE   A CD1 
263  N N   . LEU   A 57  ? 0.2135 0.2212 0.2764 -0.0115 -0.0456 0.0164  38  LEU   A N   
264  C CA  . LEU   A 57  ? 0.2312 0.234  0.2758 -0.0176 -0.0469 0.0147  38  LEU   A CA  
265  C C   . LEU   A 57  ? 0.233  0.2352 0.273  -0.0226 -0.0506 0.0139  38  LEU   A C   
266  O O   . LEU   A 57  ? 0.2444 0.2448 0.2739 -0.0254 -0.0461 0.0092  38  LEU   A O   
267  C CB  . LEU   A 57  ? 0.2514 0.2483 0.2876 -0.021  -0.0524 0.0186  38  LEU   A CB  
268  C CG  . LEU   A 57  ? 0.2924 0.2824 0.3079 -0.0283 -0.0529 0.017   38  LEU   A CG  
269  C CD1 . LEU   A 57  ? 0.2951 0.2858 0.3037 -0.0279 -0.0425 0.0102  38  LEU   A CD1 
270  C CD2 . LEU   A 57  ? 0.3196 0.3031 0.3271 -0.0313 -0.0578 0.0215  38  LEU   A CD2 
271  N N   . LYS   A 58  ? 0.2383 0.2417 0.2878 -0.0236 -0.0586 0.0184  39  LYS   A N   
272  C CA  . LYS   A 58  ? 0.2438 0.246  0.2894 -0.0286 -0.0632 0.0179  39  LYS   A CA  
273  C C   . LYS   A 58  ? 0.2429 0.2495 0.2927 -0.0261 -0.0554 0.0127  39  LYS   A C   
274  O O   . LYS   A 58  ? 0.2524 0.2557 0.2909 -0.0305 -0.054  0.0088  39  LYS   A O   
275  C CB  . LYS   A 58  ? 0.282  0.2862 0.3426 -0.0294 -0.0738 0.0243  39  LYS   A CB  
276  C CG  . LYS   A 58  ? 0.3468 0.3446 0.4012 -0.0338 -0.0845 0.0305  39  LYS   A CG  
277  C CD  . LYS   A 58  ? 0.4231 0.4237 0.4976 -0.0339 -0.096  0.0376  39  LYS   A CD  
278  C CE  . LYS   A 58  ? 0.5242 0.5212 0.6033 -0.0344 -0.105  0.0447  39  LYS   A CE  
279  N NZ  . LYS   A 58  ? 0.5821 0.5831 0.6866 -0.0337 -0.1161 0.0518  39  LYS   A NZ  
280  N N   . HIS   A 59  ? 0.2291 0.2421 0.2943 -0.0192 -0.0497 0.0123  40  HIS   A N   
281  C CA  . HIS   A 59  ? 0.2307 0.2469 0.2993 -0.0171 -0.043  0.0082  40  HIS   A CA  
282  C C   . HIS   A 59  ? 0.2151 0.2285 0.2709 -0.0179 -0.0365 0.0029  40  HIS   A C   
283  O O   . HIS   A 59  ? 0.2276 0.2402 0.2797 -0.02   -0.0343 -0.0006 40  HIS   A O   
284  C CB  . HIS   A 59  ? 0.2325 0.2539 0.3169 -0.011  -0.0379 0.0089  40  HIS   A CB  
285  C CG  . HIS   A 59  ? 0.2489 0.2727 0.3369 -0.0103 -0.0335 0.0062  40  HIS   A CG  
286  N ND1 . HIS   A 59  ? 0.2738 0.3002 0.3709 -0.0122 -0.0371 0.0076  40  HIS   A ND1 
287  C CD2 . HIS   A 59  ? 0.2728 0.2957 0.3552 -0.0091 -0.0272 0.0023  40  HIS   A CD2 
288  C CE1 . HIS   A 59  ? 0.2947 0.3217 0.3914 -0.0116 -0.032  0.0045  40  HIS   A CE1 
289  N NE2 . HIS   A 59  ? 0.2987 0.3235 0.387  -0.0097 -0.0264 0.0016  40  HIS   A NE2 
290  N N   . LEU   A 60  ? 0.2146 0.2261 0.2646 -0.0164 -0.0336 0.0024  41  LEU   A N   
291  C CA  . LEU   A 60  ? 0.2242 0.2334 0.2653 -0.0173 -0.0278 -0.0021 41  LEU   A CA  
292  C C   . LEU   A 60  ? 0.2167 0.2208 0.2452 -0.0238 -0.0284 -0.0049 41  LEU   A C   
293  O O   . LEU   A 60  ? 0.2192 0.2227 0.246  -0.0248 -0.0234 -0.0095 41  LEU   A O   
294  C CB  . LEU   A 60  ? 0.2465 0.2542 0.2841 -0.0158 -0.0262 -0.0013 41  LEU   A CB  
295  C CG  . LEU   A 60  ? 0.2759 0.2863 0.3229 -0.01   -0.0243 0.0003  41  LEU   A CG  
296  C CD1 . LEU   A 60  ? 0.29   0.2977 0.3326 -0.0092 -0.0236 0.001   41  LEU   A CD1 
297  C CD2 . LEU   A 60  ? 0.3219 0.334  0.3726 -0.0073 -0.0193 -0.0026 41  LEU   A CD2 
298  N N   . LEU   A 61  ? 0.2353 0.2349 0.2549 -0.0288 -0.0348 -0.002  42  LEU   A N   
299  C CA  . LEU   A 61  ? 0.2377 0.2297 0.2409 -0.0365 -0.0351 -0.0049 42  LEU   A CA  
300  C C   . LEU   A 61  ? 0.2223 0.214  0.2265 -0.0388 -0.0356 -0.0076 42  LEU   A C   
301  O O   . LEU   A 61  ? 0.2552 0.242  0.2499 -0.0427 -0.0302 -0.0131 42  LEU   A O   
302  C CB  . LEU   A 61  ? 0.2552 0.2407 0.2466 -0.0422 -0.0435 -0.0001 42  LEU   A CB  
303  C CG  . LEU   A 61  ? 0.2827 0.2661 0.2692 -0.0416 -0.0423 0.0018  42  LEU   A CG  
304  C CD1 . LEU   A 61  ? 0.3075 0.2849 0.2862 -0.0464 -0.0531 0.0084  42  LEU   A CD1 
305  C CD2 . LEU   A 61  ? 0.291  0.2698 0.2653 -0.0448 -0.0329 -0.0039 42  LEU   A CD2 
306  N N   . LYS   A 62  ? 0.2292 0.2261 0.2464 -0.0361 -0.0408 -0.0041 43  LYS   A N   
307  C CA  . LYS   A 62  ? 0.2359 0.2327 0.2556 -0.0382 -0.0416 -0.0063 43  LYS   A CA  
308  C C   . LYS   A 62  ? 0.2394 0.2388 0.2645 -0.0346 -0.0321 -0.0118 43  LYS   A C   
309  O O   . LYS   A 62  ? 0.2511 0.2463 0.2705 -0.038  -0.0289 -0.0166 43  LYS   A O   
310  C CB  . LYS   A 62  ? 0.2487 0.2514 0.2847 -0.0358 -0.0484 -0.0013 43  LYS   A CB  
311  C CG  . LYS   A 62  ? 0.2848 0.2842 0.3176 -0.0405 -0.0598 0.0044  43  LYS   A CG  
312  C CD  . LYS   A 62  ? 0.373  0.3791 0.4265 -0.0378 -0.066  0.0095  43  LYS   A CD  
313  C CE  . LYS   A 62  ? 0.4533 0.4619 0.5173 -0.0355 -0.072  0.0159  43  LYS   A CE  
314  N NZ  . LYS   A 62  ? 0.5057 0.5211 0.5936 -0.0331 -0.0772 0.0206  43  LYS   A NZ  
315  N N   . ASN   A 63  ? 0.2267 0.2318 0.2621 -0.0279 -0.0277 -0.0111 44  ASN   A N   
316  C CA  . ASN   A 63  ? 0.2161 0.2228 0.2571 -0.0248 -0.0206 -0.015  44  ASN   A CA  
317  C C   . ASN   A 63  ? 0.231  0.233  0.2634 -0.0275 -0.0147 -0.0202 44  ASN   A C   
318  O O   . ASN   A 63  ? 0.2366 0.2371 0.2715 -0.0281 -0.01   -0.0246 44  ASN   A O   
319  C CB  . ASN   A 63  ? 0.2391 0.2508 0.2901 -0.0183 -0.0187 -0.0124 44  ASN   A CB  
320  C CG  . ASN   A 63  ? 0.2577 0.2736 0.3196 -0.0154 -0.0204 -0.0094 44  ASN   A CG  
321  O OD1 . ASN   A 63  ? 0.3093 0.3257 0.3743 -0.0177 -0.0235 -0.0089 44  ASN   A OD1 
322  N ND2 . ASN   A 63  ? 0.2602 0.2783 0.3278 -0.0109 -0.018  -0.0076 44  ASN   A ND2 
323  N N   . LEU   A 64  ? 0.2227 0.2218 0.2461 -0.0294 -0.0141 -0.0199 45  LEU   A N   
324  C CA  . LEU   A 64  ? 0.2379 0.2324 0.2544 -0.0324 -0.0069 -0.0251 45  LEU   A CA  
325  C C   . LEU   A 64  ? 0.2577 0.2445 0.2627 -0.0393 -0.0049 -0.0298 45  LEU   A C   
326  O O   . LEU   A 64  ? 0.2647 0.2486 0.2705 -0.0406 0.0031  -0.0357 45  LEU   A O   
327  C CB  . LEU   A 64  ? 0.2411 0.2336 0.2499 -0.0338 -0.0066 -0.0235 45  LEU   A CB  
328  C CG  . LEU   A 64  ? 0.2374 0.236  0.2572 -0.0272 -0.0073 -0.0201 45  LEU   A CG  
329  C CD1 . LEU   A 64  ? 0.262  0.2585 0.2741 -0.0286 -0.0103 -0.0166 45  LEU   A CD1 
330  C CD2 . LEU   A 64  ? 0.2458 0.2465 0.2752 -0.0244 -0.0006 -0.0235 45  LEU   A CD2 
331  N N   . PHE   A 65  ? 0.2674 0.2504 0.2622 -0.044  -0.0123 -0.0271 46  PHE   A N   
332  C CA  . PHE   A 65  ? 0.2866 0.2605 0.2674 -0.0517 -0.012  -0.0313 46  PHE   A CA  
333  C C   . PHE   A 65  ? 0.284  0.2601 0.2758 -0.0496 -0.0089 -0.0349 46  PHE   A C   
334  O O   . PHE   A 65  ? 0.2846 0.2545 0.2717 -0.0528 -0.0012 -0.0418 46  PHE   A O   
335  C CB  . PHE   A 65  ? 0.3106 0.2804 0.2805 -0.057  -0.0235 -0.026  46  PHE   A CB  
336  C CG  . PHE   A 65  ? 0.3638 0.3238 0.3194 -0.0652 -0.0251 -0.0298 46  PHE   A CG  
337  C CD1 . PHE   A 65  ? 0.4077 0.3562 0.3445 -0.0723 -0.0171 -0.0366 46  PHE   A CD1 
338  C CD2 . PHE   A 65  ? 0.3982 0.3603 0.3605 -0.0656 -0.033  -0.0273 46  PHE   A CD2 
339  C CE1 . PHE   A 65  ? 0.4505 0.3881 0.3721 -0.0805 -0.0178 -0.0409 46  PHE   A CE1 
340  C CE2 . PHE   A 65  ? 0.4299 0.382  0.3782 -0.0737 -0.035  -0.031  46  PHE   A CE2 
341  C CZ  . PHE   A 65  ? 0.4383 0.3777 0.3655 -0.0811 -0.0273 -0.038  46  PHE   A CZ  
342  N N   . LYS   A 66  ? 0.255  0.2393 0.2624 -0.0439 -0.0133 -0.031  47  LYS   A N   
343  C CA  . LYS   A 66  ? 0.2676 0.2537 0.2858 -0.0418 -0.0108 -0.0336 47  LYS   A CA  
344  C C   . LYS   A 66  ? 0.2707 0.2569 0.2965 -0.0388 -0.001  -0.0388 47  LYS   A C   
345  O O   . LYS   A 66  ? 0.2913 0.2727 0.3173 -0.0412 0.004   -0.0444 47  LYS   A O   
346  C CB  . LYS   A 66  ? 0.2608 0.2552 0.2939 -0.0365 -0.016  -0.0281 47  LYS   A CB  
347  C CG  . LYS   A 66  ? 0.309  0.3046 0.3528 -0.0345 -0.0131 -0.0306 47  LYS   A CG  
348  C CD  . LYS   A 66  ? 0.3241 0.3259 0.3802 -0.0312 -0.0175 -0.0256 47  LYS   A CD  
349  C CE  . LYS   A 66  ? 0.3587 0.3608 0.4248 -0.0291 -0.0138 -0.0278 47  LYS   A CE  
350  N NZ  . LYS   A 66  ? 0.3952 0.3987 0.4679 -0.0243 -0.0083 -0.0287 47  LYS   A NZ  
351  N N   . ILE   A 67  ? 0.2402 0.2312 0.273  -0.034  0.0014  -0.037  48  ILE   A N   
352  C CA  . ILE   A 67  ? 0.2289 0.2208 0.2727 -0.031  0.0089  -0.0408 48  ILE   A CA  
353  C C   . ILE   A 67  ? 0.2578 0.2424 0.2947 -0.0359 0.0176  -0.0479 48  ILE   A C   
354  O O   . ILE   A 67  ? 0.2681 0.2505 0.3141 -0.0356 0.024   -0.053  48  ILE   A O   
355  C CB  . ILE   A 67  ? 0.2368 0.2346 0.2878 -0.0258 0.0076  -0.0365 48  ILE   A CB  
356  C CG1 . ILE   A 67  ? 0.2367 0.2402 0.2952 -0.0211 0.0013  -0.0307 48  ILE   A CG1 
357  C CG2 . ILE   A 67  ? 0.2532 0.252  0.3166 -0.0232 0.0137  -0.0394 48  ILE   A CG2 
358  C CD1 . ILE   A 67  ? 0.2566 0.2639 0.317  -0.0172 -0.001  -0.0262 48  ILE   A CD1 
359  N N   . PHE   A 68  ? 0.26   0.2398 0.2814 -0.0407 0.0189  -0.0486 49  PHE   A N   
360  C CA  . PHE   A 68  ? 0.3057 0.2778 0.3202 -0.0456 0.0296  -0.0557 49  PHE   A CA  
361  C C   . PHE   A 68  ? 0.3461 0.3071 0.3434 -0.0536 0.0326  -0.0612 49  PHE   A C   
362  O O   . PHE   A 68  ? 0.3868 0.3409 0.3832 -0.0569 0.0437  -0.0689 49  PHE   A O   
363  C CB  . PHE   A 68  ? 0.3072 0.2784 0.313  -0.0474 0.0311  -0.054  49  PHE   A CB  
364  C CG  . PHE   A 68  ? 0.288  0.2689 0.3116 -0.04   0.0297  -0.0499 49  PHE   A CG  
365  C CD1 . PHE   A 68  ? 0.2807 0.2658 0.3246 -0.0355 0.0352  -0.0524 49  PHE   A CD1 
366  C CD2 . PHE   A 68  ? 0.298  0.2828 0.318  -0.0379 0.0224  -0.0434 49  PHE   A CD2 
367  C CE1 . PHE   A 68  ? 0.28   0.2724 0.3384 -0.0297 0.0323  -0.0483 49  PHE   A CE1 
368  C CE2 . PHE   A 68  ? 0.3052 0.2973 0.3394 -0.0318 0.0208  -0.04   49  PHE   A CE2 
369  C CZ  . PHE   A 68  ? 0.2957 0.2912 0.3479 -0.0281 0.0253  -0.0423 49  PHE   A CZ  
370  N N   . CYS   A 69  ? 0.3275 0.2858 0.3118 -0.0572 0.023   -0.0577 50  CYS   A N   
371  C CA  . CYS   A 69  ? 0.3573 0.3031 0.3222 -0.0661 0.0244  -0.0627 50  CYS   A CA  
372  C C   . CYS   A 69  ? 0.364  0.3099 0.3364 -0.0654 0.0217  -0.0643 50  CYS   A C   
373  O O   . CYS   A 69  ? 0.398  0.3331 0.3596 -0.0717 0.0273  -0.0713 50  CYS   A O   
374  C CB  . CYS   A 69  ? 0.3831 0.3224 0.3249 -0.0731 0.0154  -0.0583 50  CYS   A CB  
375  S SG  . CYS   A 69  ? 0.5076 0.4444 0.4378 -0.0753 0.0192  -0.0566 50  CYS   A SG  
376  N N   . LEU   A 70  ? 0.3513 0.3077 0.3399 -0.0589 0.0135  -0.0581 51  LEU   A N   
377  C CA  . LEU   A 70  ? 0.341  0.2974 0.3368 -0.0587 0.0107  -0.0591 51  LEU   A CA  
378  C C   . LEU   A 70  ? 0.3492 0.3104 0.3663 -0.0522 0.0173  -0.0617 51  LEU   A C   
379  O O   . LEU   A 70  ? 0.356  0.3122 0.3761 -0.054  0.0208  -0.0666 51  LEU   A O   
380  C CB  . LEU   A 70  ? 0.3354 0.2986 0.3355 -0.0569 -0.0017 -0.051  51  LEU   A CB  
381  C CG  . LEU   A 70  ? 0.347  0.3057 0.3295 -0.0631 -0.0105 -0.047  51  LEU   A CG  
382  C CD1 . LEU   A 70  ? 0.3541 0.3204 0.3465 -0.0608 -0.0221 -0.0393 51  LEU   A CD1 
383  C CD2 . LEU   A 70  ? 0.3735 0.3166 0.3314 -0.0742 -0.0097 -0.0529 51  LEU   A CD2 
384  N N   . ASP   A 71  ? 0.3501 0.3206 0.3823 -0.0449 0.0177  -0.0578 52  ASP   A N   
385  C CA  . ASP   A 71  ? 0.363  0.3377 0.4158 -0.0389 0.0219  -0.0588 52  ASP   A CA  
386  C C   . ASP   A 71  ? 0.429  0.3982 0.4838 -0.0406 0.0337  -0.0663 52  ASP   A C   
387  O O   . ASP   A 71  ? 0.4719 0.4348 0.5107 -0.0461 0.0382  -0.0698 52  ASP   A O   
388  C CB  . ASP   A 71  ? 0.334  0.319  0.3993 -0.0317 0.0165  -0.0512 52  ASP   A CB  
389  C CG  . ASP   A 71  ? 0.3546 0.3442 0.4183 -0.0305 0.0073  -0.0446 52  ASP   A CG  
390  O OD1 . ASP   A 71  ? 0.3515 0.3381 0.4109 -0.034  0.0044  -0.0453 52  ASP   A OD1 
391  O OD2 . ASP   A 71  ? 0.3684 0.3643 0.4362 -0.0263 0.0036  -0.0389 52  ASP   A OD2 
392  N N   . GLY   A 72  ? 0.4395 0.4104 0.5141 -0.0364 0.0388  -0.0687 53  GLY   A N   
393  C CA  . GLY   A 72  ? 0.4328 0.3992 0.5148 -0.0374 0.0509  -0.076  53  GLY   A CA  
394  C C   . GLY   A 72  ? 0.411  0.3829 0.5022 -0.0342 0.0536  -0.0742 53  GLY   A C   
395  O O   . GLY   A 72  ? 0.4175 0.3886 0.5253 -0.0328 0.0626  -0.0788 53  GLY   A O   
396  N N   . VAL   A 73  ? 0.3811 0.3582 0.4633 -0.0332 0.0465  -0.0678 54  VAL   A N   
397  C CA  . VAL   A 73  ? 0.3492 0.3312 0.4407 -0.0302 0.0484  -0.0658 54  VAL   A CA  
398  C C   . VAL   A 73  ? 0.3559 0.3314 0.4362 -0.036  0.0587  -0.0719 54  VAL   A C   
399  O O   . VAL   A 73  ? 0.3651 0.3373 0.4239 -0.0406 0.0568  -0.0706 54  VAL   A O   
400  C CB  . VAL   A 73  ? 0.338  0.3274 0.4268 -0.0264 0.0376  -0.0571 54  VAL   A CB  
401  C CG1 . VAL   A 73  ? 0.3301 0.3242 0.431  -0.0233 0.039   -0.0552 54  VAL   A CG1 
402  C CG2 . VAL   A 73  ? 0.3406 0.3343 0.4383 -0.0219 0.0294  -0.0519 54  VAL   A CG2 
403  N N   . LYS   A 74  ? 0.3403 0.3136 0.4365 -0.036  0.0701  -0.0783 55  LYS   A N   
404  C CA  . LYS   A 74  ? 0.342  0.3076 0.4291 -0.0421 0.0831  -0.0855 55  LYS   A CA  
405  C C   . LYS   A 74  ? 0.3279 0.2973 0.4436 -0.0386 0.0926  -0.0887 55  LYS   A C   
406  O O   . LYS   A 74  ? 0.3197 0.2966 0.4619 -0.0319 0.088   -0.0855 55  LYS   A O   
407  C CB  . LYS   A 74  ? 0.3696 0.3229 0.4412 -0.0489 0.0909  -0.0937 55  LYS   A CB  
408  C CG  . LYS   A 74  ? 0.4087 0.3621 0.5037 -0.0452 0.0953  -0.0979 55  LYS   A CG  
409  C CD  . LYS   A 74  ? 0.476  0.4165 0.5555 -0.0519 0.1024  -0.1062 55  LYS   A CD  
410  C CE  . LYS   A 74  ? 0.5151 0.4581 0.6122 -0.0471 0.0976  -0.1054 55  LYS   A CE  
411  N NZ  . LYS   A 74  ? 0.5163 0.4468 0.6096 -0.0522 0.1087  -0.1156 55  LYS   A NZ  
412  N N   . GLY   A 75  ? 0.3394 0.3031 0.4504 -0.0437 0.1056  -0.0949 56  GLY   A N   
413  C CA  . GLY   A 75  ? 0.3502 0.3174 0.4911 -0.041  0.1161  -0.0985 56  GLY   A CA  
414  C C   . GLY   A 75  ? 0.363  0.3269 0.4984 -0.0459 0.1277  -0.1022 56  GLY   A C   
415  O O   . GLY   A 75  ? 0.387  0.3429 0.4912 -0.053  0.1298  -0.1032 56  GLY   A O   
416  N N   . ASP   A 76  ? 0.3379 0.3074 0.5047 -0.0425 0.1348  -0.1037 57  ASP   A N   
417  C CA  . ASP   A 76  ? 0.3431 0.3106 0.5109 -0.0467 0.1472  -0.1072 57  ASP   A CA  
418  C C   . ASP   A 76  ? 0.334  0.3093 0.4974 -0.0449 0.1361  -0.0984 57  ASP   A C   
419  O O   . ASP   A 76  ? 0.3616 0.3324 0.509  -0.0506 0.143   -0.0998 57  ASP   A O   
420  C CB  . ASP   A 76  ? 0.3645 0.3362 0.5738 -0.0434 0.1593  -0.1122 57  ASP   A CB  
421  C CG  . ASP   A 76  ? 0.483  0.4446 0.6978 -0.0468 0.1766  -0.1236 57  ASP   A CG  
422  O OD1 . ASP   A 76  ? 0.5217 0.4709 0.703  -0.0537 0.1816  -0.1288 57  ASP   A OD1 
423  O OD2 . ASP   A 76  ? 0.5217 0.4872 0.775  -0.0428 0.1848  -0.1272 57  ASP   A OD2 
424  N N   . LEU   A 77  ? 0.3122 0.2978 0.4885 -0.0375 0.1192  -0.0894 58  LEU   A N   
425  C CA  . LEU   A 77  ? 0.2789 0.271  0.4532 -0.0357 0.1095  -0.0817 58  LEU   A CA  
426  C C   . LEU   A 77  ? 0.2458 0.2428 0.4105 -0.0311 0.0909  -0.0729 58  LEU   A C   
427  O O   . LEU   A 77  ? 0.2299 0.2312 0.4102 -0.0258 0.0831  -0.0699 58  LEU   A O   
428  C CB  . LEU   A 77  ? 0.2748 0.2752 0.4869 -0.0315 0.1113  -0.0806 58  LEU   A CB  
429  C CG  . LEU   A 77  ? 0.2843 0.2916 0.4996 -0.0294 0.1009  -0.0728 58  LEU   A CG  
430  C CD1 . LEU   A 77  ? 0.3196 0.322  0.5111 -0.0358 0.1076  -0.0741 58  LEU   A CD1 
431  C CD2 . LEU   A 77  ? 0.3034 0.3186 0.5588 -0.0254 0.1006  -0.0713 58  LEU   A CD2 
432  N N   . LEU   A 78  ? 0.2371 0.2331 0.3776 -0.0333 0.0846  -0.0684 59  LEU   A N   
433  C CA  . LEU   A 78  ? 0.2307 0.2311 0.3629 -0.0292 0.069   -0.0602 59  LEU   A CA  
434  C C   . LEU   A 78  ? 0.2281 0.2323 0.3629 -0.0285 0.0652  -0.0557 59  LEU   A C   
435  O O   . LEU   A 78  ? 0.2468 0.2474 0.3718 -0.0334 0.0724  -0.0578 59  LEU   A O   
436  C CB  . LEU   A 78  ? 0.2351 0.2297 0.3364 -0.0328 0.065   -0.0593 59  LEU   A CB  
437  C CG  . LEU   A 78  ? 0.2444 0.2432 0.3372 -0.0289 0.0504  -0.0511 59  LEU   A CG  
438  C CD1 . LEU   A 78  ? 0.2725 0.268  0.3491 -0.03   0.0456  -0.0505 59  LEU   A CD1 
439  C CD2 . LEU   A 78  ? 0.286  0.2841 0.3654 -0.0308 0.0475  -0.0474 59  LEU   A CD2 
440  N N   . ILE   A 79  ? 0.2104 0.2208 0.357  -0.0232 0.0537  -0.0494 60  ILE   A N   
441  C CA  . ILE   A 79  ? 0.2098 0.223  0.3566 -0.0225 0.0481  -0.0445 60  ILE   A CA  
442  C C   . ILE   A 79  ? 0.2066 0.2191 0.3329 -0.0209 0.037   -0.0389 60  ILE   A C   
443  O O   . ILE   A 79  ? 0.1917 0.2055 0.3192 -0.0174 0.0296  -0.0362 60  ILE   A O   
444  C CB  . ILE   A 79  ? 0.2242 0.2432 0.3989 -0.0187 0.043   -0.0416 60  ILE   A CB  
445  C CG1 . ILE   A 79  ? 0.2444 0.2649 0.4452 -0.0198 0.0545  -0.0471 60  ILE   A CG1 
446  C CG2 . ILE   A 79  ? 0.2302 0.2507 0.4018 -0.0187 0.0364  -0.0367 60  ILE   A CG2 
447  C CD1 . ILE   A 79  ? 0.2563 0.2827 0.4899 -0.0156 0.0472  -0.0434 60  ILE   A CD1 
448  N N   . ASP   A 80  ? 0.1997 0.2096 0.3085 -0.0236 0.0363  -0.0371 61  ASP   A N   
449  C CA  . ASP   A 80  ? 0.2017 0.2109 0.2943 -0.0219 0.0268  -0.0319 61  ASP   A CA  
450  C C   . ASP   A 80  ? 0.2063 0.2179 0.3058 -0.0197 0.0207  -0.0277 61  ASP   A C   
451  O O   . ASP   A 80  ? 0.2188 0.2305 0.323  -0.022  0.0244  -0.0283 61  ASP   A O   
452  C CB  . ASP   A 80  ? 0.2158 0.2197 0.286  -0.0266 0.0289  -0.0322 61  ASP   A CB  
453  C CG  . ASP   A 80  ? 0.2911 0.2945 0.3486 -0.0245 0.0195  -0.0268 61  ASP   A CG  
454  O OD1 . ASP   A 80  ? 0.27   0.2759 0.3312 -0.0203 0.0137  -0.0247 61  ASP   A OD1 
455  O OD2 . ASP   A 80  ? 0.2882 0.2885 0.3334 -0.027  0.0183  -0.0247 61  ASP   A OD2 
456  N N   . ILE   A 81  ? 0.1951 0.208  0.2961 -0.0158 0.0119  -0.0238 62  ILE   A N   
457  C CA  . ILE   A 81  ? 0.1997 0.2132 0.3063 -0.0139 0.0048  -0.0199 62  ILE   A CA  
458  C C   . ILE   A 81  ? 0.1905 0.2009 0.2803 -0.0134 0       -0.0166 62  ILE   A C   
459  O O   . ILE   A 81  ? 0.2011 0.2103 0.2806 -0.0119 -0.0024 -0.0155 62  ILE   A O   
460  C CB  . ILE   A 81  ? 0.2165 0.2311 0.3345 -0.0108 -0.0015 -0.0178 62  ILE   A CB  
461  C CG1 . ILE   A 81  ? 0.2251 0.2429 0.3654 -0.0108 0.0026  -0.0206 62  ILE   A CG1 
462  C CG2 . ILE   A 81  ? 0.214  0.2264 0.3314 -0.0097 -0.0107 -0.0133 62  ILE   A CG2 
463  C CD1 . ILE   A 81  ? 0.2468 0.267  0.4053 -0.012  0.0036  -0.0206 62  ILE   A CD1 
464  N N   . GLY   A 82  ? 0.1805 0.1897 0.2688 -0.0148 -0.0009 -0.0152 63  GLY   A N   
465  C CA  . GLY   A 82  ? 0.177  0.1826 0.2508 -0.0142 -0.005  -0.0124 63  GLY   A CA  
466  C C   . GLY   A 82  ? 0.1828 0.1866 0.243  -0.0159 -0.002  -0.0127 63  GLY   A C   
467  O O   . GLY   A 82  ? 0.1854 0.1872 0.2362 -0.0141 -0.0055 -0.0106 63  GLY   A O   
468  N N   . SER   A 83  ? 0.1768 0.1804 0.2359 -0.0198 0.0045  -0.0153 64  SER   A N   
469  C CA  . SER   A 83  ? 0.1985 0.1987 0.243  -0.023  0.0067  -0.0155 64  SER   A CA  
470  C C   . SER   A 83  ? 0.2157 0.2122 0.2496 -0.0234 0.0023  -0.0115 64  SER   A C   
471  O O   . SER   A 83  ? 0.2275 0.2209 0.2497 -0.0252 0.0006  -0.0099 64  SER   A O   
472  C CB  . SER   A 83  ? 0.231  0.2293 0.2747 -0.0285 0.0155  -0.0191 64  SER   A CB  
473  O OG  . SER   A 83  ? 0.2473 0.2487 0.3047 -0.0283 0.0214  -0.0235 64  SER   A OG  
474  N N   . GLY   A 84  ? 0.2039 0.2    0.2421 -0.0225 0.0002  -0.0099 65  GLY   A N   
475  C CA  . GLY   A 84  ? 0.217  0.2087 0.2461 -0.0232 -0.0031 -0.0064 65  GLY   A CA  
476  C C   . GLY   A 84  ? 0.2213 0.2089 0.2399 -0.029  0.0008  -0.0064 65  GLY   A C   
477  O O   . GLY   A 84  ? 0.2309 0.2188 0.2511 -0.0328 0.0077  -0.0096 65  GLY   A O   
478  N N   . PRO   A 85  ? 0.2204 0.2036 0.2282 -0.03   -0.0036 -0.0026 66  PRO   A N   
479  C CA  . PRO   A 85  ? 0.2333 0.2105 0.2275 -0.0365 -0.0016 -0.0016 66  PRO   A CA  
480  C C   . PRO   A 85  ? 0.26   0.2352 0.2445 -0.0388 -0.003  -0.0017 66  PRO   A C   
481  O O   . PRO   A 85  ? 0.2807 0.2489 0.2506 -0.0442 -0.0049 0.001   66  PRO   A O   
482  C CB  . PRO   A 85  ? 0.2414 0.214  0.2308 -0.0362 -0.0077 0.0036  66  PRO   A CB  
483  C CG  . PRO   A 85  ? 0.2403 0.2162 0.2375 -0.0293 -0.0136 0.005   66  PRO   A CG  
484  C CD  . PRO   A 85  ? 0.2177 0.1999 0.2259 -0.0256 -0.0104 0.0009  66  PRO   A CD  
485  N N   . THR   A 86  ? 0.2328 0.2131 0.2244 -0.0351 -0.0032 -0.004  67  THR   A N   
486  C CA  . THR   A 86  ? 0.2393 0.2176 0.2226 -0.0372 -0.0058 -0.0037 67  THR   A CA  
487  C C   . THR   A 86  ? 0.2556 0.2326 0.2345 -0.0416 0.0015  -0.009  67  THR   A C   
488  O O   . THR   A 86  ? 0.2728 0.2536 0.2621 -0.0402 0.0083  -0.0134 67  THR   A O   
489  C CB  . THR   A 86  ? 0.2489 0.2322 0.2413 -0.031  -0.0116 -0.002  67  THR   A CB  
490  O OG1 . THR   A 86  ? 0.2405 0.2297 0.2443 -0.0272 -0.0076 -0.0059 67  THR   A OG1 
491  C CG2 . THR   A 86  ? 0.2472 0.2312 0.2454 -0.0264 -0.0167 0.0021  67  THR   A CG2 
492  N N   . ILE   A 87  ? 0.2688 0.2398 0.2331 -0.0468 -0.0007 -0.0084 68  ILE   A N   
493  C CA  . ILE   A 87  ? 0.2778 0.2456 0.2355 -0.0515 0.0063  -0.014  68  ILE   A CA  
494  C C   . ILE   A 87  ? 0.2751 0.2435 0.2313 -0.0509 0.0009  -0.0137 68  ILE   A C   
495  O O   . ILE   A 87  ? 0.2827 0.2483 0.234  -0.0544 0.0062  -0.0186 68  ILE   A O   
496  C CB  . ILE   A 87  ? 0.3156 0.2721 0.2524 -0.0614 0.0118  -0.0154 68  ILE   A CB  
497  C CG1 . ILE   A 87  ? 0.3657 0.314  0.2844 -0.0663 0.0015  -0.009  68  ILE   A CG1 
498  C CG2 . ILE   A 87  ? 0.3309 0.2875 0.272  -0.0624 0.0194  -0.0166 68  ILE   A CG2 
499  C CD1 . ILE   A 87  ? 0.4147 0.3571 0.3199 -0.0711 -0.0033 -0.0089 68  ILE   A CD1 
500  N N   . TYR   A 88  ? 0.2641 0.2359 0.2253 -0.0467 -0.0091 -0.0084 69  TYR   A N   
501  C CA  . TYR   A 88  ? 0.2762 0.2488 0.2376 -0.0466 -0.0145 -0.0077 69  TYR   A CA  
502  C C   . TYR   A 88  ? 0.2611 0.2388 0.2328 -0.0435 -0.0086 -0.0132 69  TYR   A C   
503  O O   . TYR   A 88  ? 0.2703 0.2456 0.2371 -0.0465 -0.0092 -0.0153 69  TYR   A O   
504  C CB  . TYR   A 88  ? 0.2666 0.2437 0.2378 -0.0414 -0.0242 -0.0014 69  TYR   A CB  
505  C CG  . TYR   A 88  ? 0.2451 0.2311 0.2348 -0.0329 -0.0221 -0.0021 69  TYR   A CG  
506  C CD1 . TYR   A 88  ? 0.233  0.224  0.2322 -0.0295 -0.0216 -0.004  69  TYR   A CD1 
507  C CD2 . TYR   A 88  ? 0.2482 0.2362 0.244  -0.029  -0.0206 -0.0011 69  TYR   A CD2 
508  C CE1 . TYR   A 88  ? 0.2204 0.2174 0.2329 -0.0229 -0.0195 -0.0045 69  TYR   A CE1 
509  C CE2 . TYR   A 88  ? 0.2295 0.2232 0.2383 -0.0226 -0.0187 -0.002  69  TYR   A CE2 
510  C CZ  . TYR   A 88  ? 0.217  0.2149 0.2334 -0.0197 -0.0183 -0.0035 69  TYR   A CZ  
511  O OH  . TYR   A 88  ? 0.2075 0.2092 0.2338 -0.0144 -0.0167 -0.004  69  TYR   A OH  
512  N N   . GLN   A 89  ? 0.2399 0.224  0.2261 -0.0378 -0.0039 -0.0151 70  GLN   A N   
513  C CA  . GLN   A 89  ? 0.2451 0.2341 0.2434 -0.0343 0.0001  -0.019  70  GLN   A CA  
514  C C   . GLN   A 89  ? 0.2504 0.2356 0.2456 -0.0387 0.0093  -0.0255 70  GLN   A C   
515  O O   . GLN   A 89  ? 0.2464 0.2347 0.2522 -0.0363 0.0127  -0.0289 70  GLN   A O   
516  C CB  . GLN   A 89  ? 0.2304 0.2262 0.2445 -0.0274 0.0003  -0.0179 70  GLN   A CB  
517  C CG  . GLN   A 89  ? 0.2374 0.2332 0.2558 -0.0277 0.0057  -0.0197 70  GLN   A CG  
518  C CD  . GLN   A 89  ? 0.2562 0.2494 0.2678 -0.029  0.0034  -0.0162 70  GLN   A CD  
519  O OE1 . GLN   A 89  ? 0.2463 0.2359 0.2474 -0.0312 -0.0015 -0.0128 70  GLN   A OE1 
520  N NE2 . GLN   A 89  ? 0.2865 0.2813 0.3055 -0.0279 0.0061  -0.0167 70  GLN   A NE2 
521  N N   . LEU   A 90  ? 0.2567 0.2342 0.2372 -0.0456 0.0138  -0.0274 71  LEU   A N   
522  C CA  . LEU   A 90  ? 0.277  0.249  0.2532 -0.0508 0.025   -0.0344 71  LEU   A CA  
523  C C   . LEU   A 90  ? 0.3159 0.2772 0.2703 -0.0592 0.0256  -0.0368 71  LEU   A C   
524  O O   . LEU   A 90  ? 0.331  0.2861 0.2801 -0.0641 0.0361  -0.0436 71  LEU   A O   
525  C CB  . LEU   A 90  ? 0.2782 0.2477 0.2525 -0.0537 0.0322  -0.0355 71  LEU   A CB  
526  C CG  . LEU   A 90  ? 0.2932 0.2714 0.2859 -0.0468 0.0301  -0.0324 71  LEU   A CG  
527  C CD1 . LEU   A 90  ? 0.3259 0.3008 0.3151 -0.0508 0.0364  -0.0329 71  LEU   A CD1 
528  C CD2 . LEU   A 90  ? 0.2999 0.286  0.3153 -0.0407 0.0325  -0.035  71  LEU   A CD2 
529  N N   . LEU   A 91  ? 0.3019 0.26   0.2438 -0.0614 0.0148  -0.0314 72  LEU   A N   
530  C CA  . LEU   A 91  ? 0.3349 0.2807 0.2527 -0.071  0.0131  -0.0324 72  LEU   A CA  
531  C C   . LEU   A 91  ? 0.359  0.3022 0.276  -0.0728 0.0163  -0.038  72  LEU   A C   
532  O O   . LEU   A 91  ? 0.3757 0.3071 0.2743 -0.0813 0.0234  -0.0436 72  LEU   A O   
533  C CB  . LEU   A 91  ? 0.3455 0.2894 0.2543 -0.0725 -0.0011 -0.0241 72  LEU   A CB  
534  C CG  . LEU   A 91  ? 0.3673 0.3082 0.2688 -0.0743 -0.0032 -0.0193 72  LEU   A CG  
535  C CD1 . LEU   A 91  ? 0.3635 0.3055 0.2654 -0.0729 -0.0177 -0.0106 72  LEU   A CD1 
536  C CD2 . LEU   A 91  ? 0.3877 0.3138 0.2627 -0.0855 0.0034  -0.0223 72  LEU   A CD2 
537  N N   . SER   A 92  ? 0.3221 0.2748 0.2579 -0.0656 0.0128  -0.0374 73  SER   A N   
538  C CA  . SER   A 92  ? 0.3251 0.2753 0.2622 -0.0671 0.0169  -0.0432 73  SER   A CA  
539  C C   . SER   A 92  ? 0.3383 0.29   0.2882 -0.0649 0.0307  -0.0507 73  SER   A C   
540  O O   . SER   A 92  ? 0.3437 0.2878 0.2875 -0.0696 0.0389  -0.0577 73  SER   A O   
541  C CB  . SER   A 92  ? 0.3182 0.2768 0.2696 -0.0611 0.0079  -0.0394 73  SER   A CB  
542  O OG  . SER   A 92  ? 0.3485 0.3042 0.2893 -0.0646 -0.0041 -0.0336 73  SER   A OG  
543  N N   . ALA   A 93  ? 0.3148 0.2757 0.2834 -0.058  0.0332  -0.0492 74  ALA   A N   
544  C CA  . ALA   A 93  ? 0.3271 0.2906 0.3129 -0.0553 0.0447  -0.0551 74  ALA   A CA  
545  C C   . ALA   A 93  ? 0.3615 0.3146 0.3352 -0.0632 0.0581  -0.0623 74  ALA   A C   
546  O O   . ALA   A 93  ? 0.3641 0.3158 0.3493 -0.0631 0.0689  -0.0693 74  ALA   A O   
547  C CB  . ALA   A 93  ? 0.3134 0.2872 0.3184 -0.0481 0.0428  -0.051  74  ALA   A CB  
548  N N   . CYS   A 94  ? 0.3677 0.3126 0.319  -0.0702 0.0582  -0.0608 75  CYS   A N   
549  C CA  . CYS   A 94  ? 0.3846 0.3182 0.3227 -0.0784 0.0726  -0.068  75  CYS   A CA  
550  C C   . CYS   A 94  ? 0.4128 0.3339 0.3346 -0.0859 0.0794  -0.0755 75  CYS   A C   
551  O O   . CYS   A 94  ? 0.4467 0.3581 0.3612 -0.0922 0.0945  -0.0835 75  CYS   A O   
552  C CB  . CYS   A 94  ? 0.3982 0.3248 0.3149 -0.0848 0.0709  -0.064  75  CYS   A CB  
553  S SG  . CYS   A 94  ? 0.4476 0.3616 0.3291 -0.0937 0.0579  -0.059  75  CYS   A SG  
554  N N   . GLU   A 95  ? 0.4011 0.322  0.3182 -0.0853 0.0692  -0.0734 76  GLU   A N   
555  C CA  . GLU   A 95  ? 0.422  0.3311 0.3252 -0.092  0.0748  -0.0808 76  GLU   A CA  
556  C C   . GLU   A 95  ? 0.4322 0.3465 0.3617 -0.0863 0.0853  -0.0878 76  GLU   A C   
557  O O   . GLU   A 95  ? 0.4617 0.365  0.383  -0.0919 0.0953  -0.0963 76  GLU   A O   
558  C CB  . GLU   A 95  ? 0.4375 0.3453 0.3295 -0.0934 0.0593  -0.0757 76  GLU   A CB  
559  C CG  . GLU   A 95  ? 0.4831 0.385  0.3513 -0.0993 0.0469  -0.0681 76  GLU   A CG  
560  C CD  . GLU   A 95  ? 0.5842 0.4673 0.4187 -0.1122 0.0538  -0.0721 76  GLU   A CD  
561  O OE1 . GLU   A 95  ? 0.6345 0.5054 0.4568 -0.119  0.0659  -0.0814 76  GLU   A OE1 
562  O OE2 . GLU   A 95  ? 0.607  0.4865 0.4267 -0.116  0.0474  -0.0659 76  GLU   A OE2 
563  N N   . SER   A 96  ? 0.3995 0.3292 0.3601 -0.0755 0.0823  -0.0841 77  SER   A N   
564  C CA  . SER   A 96  ? 0.3926 0.328  0.3805 -0.0694 0.0883  -0.0885 77  SER   A CA  
565  C C   . SER   A 96  ? 0.3881 0.3299 0.4021 -0.0647 0.0986  -0.0912 77  SER   A C   
566  O O   . SER   A 96  ? 0.3757 0.3211 0.4139 -0.0602 0.1042  -0.0951 77  SER   A O   
567  C CB  . SER   A 96  ? 0.3978 0.3444 0.4005 -0.0613 0.0743  -0.0815 77  SER   A CB  
568  O OG  . SER   A 96  ? 0.4201 0.361  0.4024 -0.0657 0.0653  -0.0795 77  SER   A OG  
569  N N   . PHE   A 97  ? 0.3715 0.3154 0.3836 -0.0655 0.1003  -0.0886 78  PHE   A N   
570  C CA  . PHE   A 97  ? 0.3688 0.3195 0.4079 -0.0614 0.1092  -0.0905 78  PHE   A CA  
571  C C   . PHE   A 97  ? 0.4131 0.3544 0.4398 -0.0693 0.124   -0.0962 78  PHE   A C   
572  O O   . PHE   A 97  ? 0.4395 0.3751 0.4405 -0.075  0.1208  -0.0931 78  PHE   A O   
573  C CB  . PHE   A 97  ? 0.3411 0.3049 0.3952 -0.0537 0.0967  -0.0811 78  PHE   A CB  
574  C CG  . PHE   A 97  ? 0.3077 0.2804 0.3799 -0.0457 0.0858  -0.0767 78  PHE   A CG  
575  C CD1 . PHE   A 97  ? 0.3185 0.2919 0.3768 -0.0446 0.0734  -0.0715 78  PHE   A CD1 
576  C CD2 . PHE   A 97  ? 0.3029 0.282  0.4062 -0.0399 0.0886  -0.078  78  PHE   A CD2 
577  C CE1 . PHE   A 97  ? 0.3245 0.3047 0.3976 -0.0382 0.0649  -0.0678 78  PHE   A CE1 
578  C CE2 . PHE   A 97  ? 0.3077 0.2932 0.4249 -0.0335 0.0784  -0.0735 78  PHE   A CE2 
579  C CZ  . PHE   A 97  ? 0.3149 0.3005 0.4157 -0.0329 0.0674  -0.0688 78  PHE   A CZ  
580  N N   . LYS   A 98  ? 0.4082 0.3484 0.4554 -0.0695 0.14    -0.104  79  LYS   A N   
581  C CA  . LYS   A 98  ? 0.4335 0.3646 0.4718 -0.0772 0.1567  -0.1101 79  LYS   A CA  
582  C C   . LYS   A 98  ? 0.4262 0.3649 0.4698 -0.0756 0.1526  -0.1036 79  LYS   A C   
583  O O   . LYS   A 98  ? 0.4595 0.3894 0.4799 -0.0834 0.1586  -0.1043 79  LYS   A O   
584  C CB  . LYS   A 98  ? 0.4641 0.3942 0.5307 -0.0764 0.1751  -0.1199 79  LYS   A CB  
585  C CG  . LYS   A 98  ? 0.5535 0.4791 0.6262 -0.0816 0.194   -0.126  79  LYS   A CG  
586  C CD  . LYS   A 98  ? 0.6448 0.5673 0.7441 -0.0812 0.2128  -0.1367 79  LYS   A CD  
587  C CE  . LYS   A 98  ? 0.7212 0.6391 0.8286 -0.0867 0.2335  -0.1433 79  LYS   A CE  
588  N NZ  . LYS   A 98  ? 0.7801 0.683  0.8415 -0.0985 0.2386  -0.1444 79  LYS   A NZ  
589  N N   . GLU   A 99  ? 0.3774 0.3311 0.4503 -0.066  0.1423  -0.097  80  GLU   A N   
590  C CA  . GLU   A 99  ? 0.3553 0.316  0.4345 -0.0642 0.1376  -0.0908 80  GLU   A CA  
591  C C   . GLU   A 99  ? 0.3426 0.3134 0.4253 -0.0567 0.1175  -0.081  80  GLU   A C   
592  O O   . GLU   A 99  ? 0.3282 0.3052 0.4268 -0.0503 0.1101  -0.0793 80  GLU   A O   
593  C CB  . GLU   A 99  ? 0.3414 0.3094 0.4578 -0.061  0.1479  -0.0937 80  GLU   A CB  
594  C CG  . GLU   A 99  ? 0.4184 0.3927 0.5415 -0.0601 0.1437  -0.0878 80  GLU   A CG  
595  C CD  . GLU   A 99  ? 0.4815 0.4642 0.6445 -0.0568 0.1514  -0.0895 80  GLU   A CD  
596  O OE1 . GLU   A 99  ? 0.4775 0.4656 0.6478 -0.0562 0.1474  -0.0846 80  GLU   A OE1 
597  O OE2 . GLU   A 99  ? 0.5274 0.5119 0.7169 -0.0545 0.1602  -0.0951 80  GLU   A OE2 
598  N N   . ILE   A 100 ? 0.3165 0.2878 0.3843 -0.0578 0.1096  -0.0747 81  ILE   A N   
599  C CA  . ILE   A 100 ? 0.3128 0.2926 0.3835 -0.0513 0.0926  -0.0659 81  ILE   A CA  
600  C C   . ILE   A 100 ? 0.2986 0.2837 0.3816 -0.05   0.092   -0.0623 81  ILE   A C   
601  O O   . ILE   A 100 ? 0.3323 0.3116 0.4034 -0.0561 0.0997  -0.0637 81  ILE   A O   
602  C CB  . ILE   A 100 ? 0.3299 0.3041 0.3697 -0.0543 0.0828  -0.0614 81  ILE   A CB  
603  C CG1 . ILE   A 100 ? 0.3449 0.3144 0.3741 -0.0556 0.0816  -0.0642 81  ILE   A CG1 
604  C CG2 . ILE   A 100 ? 0.3304 0.3125 0.3737 -0.048  0.0675  -0.0527 81  ILE   A CG2 
605  C CD1 . ILE   A 100 ? 0.3602 0.324  0.3615 -0.0591 0.0713  -0.0597 81  ILE   A CD1 
606  N N   . VAL   A 101 ? 0.2646 0.2596 0.3713 -0.0429 0.0833  -0.0579 82  VAL   A N   
607  C CA  . VAL   A 101 ? 0.2622 0.2622 0.3812 -0.0414 0.0803  -0.0539 82  VAL   A CA  
608  C C   . VAL   A 101 ? 0.2473 0.249  0.3524 -0.0382 0.0651  -0.0464 82  VAL   A C   
609  O O   . VAL   A 101 ? 0.247  0.2515 0.3538 -0.0335 0.0562  -0.0438 82  VAL   A O   
610  C CB  . VAL   A 101 ? 0.272  0.2802 0.427  -0.0365 0.0802  -0.0541 82  VAL   A CB  
611  C CG1 . VAL   A 101 ? 0.2808 0.2941 0.4474 -0.0348 0.0734  -0.0488 82  VAL   A CG1 
612  C CG2 . VAL   A 101 ? 0.2795 0.286  0.4518 -0.0396 0.0971  -0.062  82  VAL   A CG2 
613  N N   . VAL   A 102 ? 0.2368 0.236  0.3285 -0.0409 0.0631  -0.0431 83  VAL   A N   
614  C CA  . VAL   A 102 ? 0.2587 0.2588 0.3391 -0.0379 0.0501  -0.0365 83  VAL   A CA  
615  C C   . VAL   A 102 ? 0.2415 0.2465 0.3381 -0.0351 0.0452  -0.033  83  VAL   A C   
616  O O   . VAL   A 102 ? 0.2384 0.2443 0.3475 -0.0377 0.0523  -0.0349 83  VAL   A O   
617  C CB  . VAL   A 102 ? 0.286  0.2785 0.3389 -0.0427 0.0489  -0.0344 83  VAL   A CB  
618  C CG1 . VAL   A 102 ? 0.2933 0.2802 0.3293 -0.0458 0.0509  -0.0371 83  VAL   A CG1 
619  C CG2 . VAL   A 102 ? 0.3157 0.3038 0.364  -0.0488 0.0571  -0.0355 83  VAL   A CG2 
620  N N   . THR   A 103 ? 0.2261 0.2339 0.3241 -0.0301 0.0337  -0.0284 84  THR   A N   
621  C CA  . THR   A 103 ? 0.2209 0.2321 0.3335 -0.0278 0.0276  -0.0252 84  THR   A CA  
622  C C   . THR   A 103 ? 0.2216 0.2307 0.3212 -0.0253 0.0171  -0.0202 84  THR   A C   
623  O O   . THR   A 103 ? 0.2186 0.2261 0.3053 -0.0233 0.013   -0.019  84  THR   A O   
624  C CB  . THR   A 103 ? 0.2309 0.2472 0.3666 -0.024  0.0242  -0.0253 84  THR   A CB  
625  O OG1 . THR   A 103 ? 0.2455 0.2613 0.3736 -0.0202 0.016   -0.0229 84  THR   A OG1 
626  C CG2 . THR   A 103 ? 0.2373 0.2556 0.3896 -0.0252 0.0346  -0.0307 84  THR   A CG2 
627  N N   . ASP   A 104 ? 0.2141 0.2234 0.3191 -0.0253 0.0126  -0.0174 85  ASP   A N   
628  C CA  . ASP   A 104 ? 0.2099 0.2159 0.3033 -0.0231 0.0036  -0.0134 85  ASP   A CA  
629  C C   . ASP   A 104 ? 0.2006 0.2067 0.3046 -0.0234 -0.0016 -0.0113 85  ASP   A C   
630  O O   . ASP   A 104 ? 0.1994 0.2079 0.3176 -0.0261 0.0028  -0.0124 85  ASP   A O   
631  C CB  . ASP   A 104 ? 0.2177 0.219  0.2915 -0.025  0.0046  -0.0122 85  ASP   A CB  
632  C CG  . ASP   A 104 ? 0.2101 0.2083 0.2734 -0.0216 -0.0033 -0.009  85  ASP   A CG  
633  O OD1 . ASP   A 104 ? 0.2014 0.2002 0.2612 -0.0188 -0.0053 -0.009  85  ASP   A OD1 
634  O OD2 . ASP   A 104 ? 0.2139 0.2085 0.2726 -0.0219 -0.0065 -0.0068 85  ASP   A OD2 
635  N N   . TYR   A 105 ? 0.2005 0.2031 0.2976 -0.0212 -0.0102 -0.0083 86  TYR   A N   
636  C CA  . TYR   A 105 ? 0.2087 0.2092 0.312  -0.0224 -0.0163 -0.0061 86  TYR   A CA  
637  C C   . TYR   A 105 ? 0.2095 0.2072 0.3062 -0.0252 -0.0135 -0.0056 86  TYR   A C   
638  O O   . TYR   A 105 ? 0.2235 0.2212 0.3306 -0.0276 -0.0154 -0.0046 86  TYR   A O   
639  C CB  . TYR   A 105 ? 0.2107 0.2056 0.3042 -0.0202 -0.0254 -0.0038 86  TYR   A CB  
640  C CG  . TYR   A 105 ? 0.2216 0.2132 0.3217 -0.0221 -0.0331 -0.0016 86  TYR   A CG  
641  C CD1 . TYR   A 105 ? 0.2459 0.2411 0.3657 -0.0231 -0.0374 -0.0007 86  TYR   A CD1 
642  C CD2 . TYR   A 105 ? 0.2499 0.2348 0.3383 -0.0233 -0.0364 -0.0005 86  TYR   A CD2 
643  C CE1 . TYR   A 105 ? 0.2661 0.258  0.3931 -0.0257 -0.0459 0.0018  86  TYR   A CE1 
644  C CE2 . TYR   A 105 ? 0.2726 0.2536 0.3663 -0.0259 -0.044  0.0014  86  TYR   A CE2 
645  C CZ  . TYR   A 105 ? 0.2816 0.2662 0.3943 -0.0273 -0.0492 0.0027  86  TYR   A CZ  
646  O OH  . TYR   A 105 ? 0.3149 0.2955 0.4345 -0.0305 -0.0584 0.0051  86  TYR   A OH  
647  N N   . SER   A 106 ? 0.217  0.2116 0.2973 -0.0253 -0.0105 -0.0055 87  SER   A N   
648  C CA  . SER   A 106 ? 0.2166 0.207  0.2887 -0.0279 -0.0093 -0.004  87  SER   A CA  
649  C C   . SER   A 106 ? 0.229  0.2209 0.3032 -0.0324 -0.0004 -0.0055 87  SER   A C   
650  O O   . SER   A 106 ? 0.2358 0.2278 0.3021 -0.0334 0.0049  -0.0069 87  SER   A O   
651  C CB  . SER   A 106 ? 0.237  0.2224 0.2919 -0.0258 -0.0118 -0.0024 87  SER   A CB  
652  O OG  . SER   A 106 ? 0.2865 0.2677 0.3334 -0.0288 -0.0098 -0.0007 87  SER   A OG  
653  N N   . ASP   A 107 ? 0.2463 0.2378 0.3284 -0.0359 0.0013  -0.0049 88  ASP   A N   
654  C CA  . ASP   A 107 ? 0.259  0.2501 0.3408 -0.0411 0.0112  -0.0063 88  ASP   A CA  
655  C C   . ASP   A 107 ? 0.2517 0.2359 0.3115 -0.0433 0.0118  -0.0042 88  ASP   A C   
656  O O   . ASP   A 107 ? 0.284  0.2662 0.3356 -0.0474 0.0195  -0.0057 88  ASP   A O   
657  C CB  . ASP   A 107 ? 0.3179 0.3099 0.4143 -0.0445 0.0124  -0.0056 88  ASP   A CB  
658  C CG  . ASP   A 107 ? 0.4546 0.4527 0.5744 -0.0425 0.0083  -0.0062 88  ASP   A CG  
659  O OD1 . ASP   A 107 ? 0.4877 0.4914 0.6245 -0.0432 0.0149  -0.0091 88  ASP   A OD1 
660  O OD2 . ASP   A 107 ? 0.5196 0.5158 0.6403 -0.0403 -0.002  -0.0038 88  ASP   A OD2 
661  N N   . GLN   A 108 ? 0.2468 0.2263 0.2963 -0.0408 0.0039  -0.0009 89  GLN   A N   
662  C CA  . GLN   A 108 ? 0.2742 0.2472 0.3056 -0.0425 0.003   0.002   89  GLN   A CA  
663  C C   . GLN   A 108 ? 0.2723 0.246  0.2946 -0.0417 0.0042  0.001   89  GLN   A C   
664  O O   . GLN   A 108 ? 0.2837 0.2527 0.2925 -0.0461 0.0069  0.0021  89  GLN   A O   
665  C CB  . GLN   A 108 ? 0.3265 0.295  0.3527 -0.0388 -0.0055 0.0052  89  GLN   A CB  
666  C CG  . GLN   A 108 ? 0.4017 0.3657 0.43   -0.0406 -0.0078 0.0072  89  GLN   A CG  
667  C CD  . GLN   A 108 ? 0.4696 0.4274 0.4897 -0.0371 -0.0144 0.01    89  GLN   A CD  
668  O OE1 . GLN   A 108 ? 0.4878 0.4449 0.5108 -0.0329 -0.0187 0.0091  89  GLN   A OE1 
669  N NE2 . GLN   A 108 ? 0.4634 0.4158 0.4731 -0.0392 -0.0151 0.0135  89  GLN   A NE2 
670  N N   . ASN   A 109 ? 0.2502 0.2288 0.2791 -0.0369 0.0019  -0.0009 90  ASN   A N   
671  C CA  . ASN   A 109 ? 0.2628 0.2424 0.2847 -0.0363 0.0029  -0.002  90  ASN   A CA  
672  C C   . ASN   A 109 ? 0.2757 0.2557 0.2966 -0.0413 0.0121  -0.0055 90  ASN   A C   
673  O O   . ASN   A 109 ? 0.3012 0.2771 0.3082 -0.0447 0.0138  -0.0054 90  ASN   A O   
674  C CB  . ASN   A 109 ? 0.2557 0.2403 0.286  -0.0306 -0.0005 -0.0034 90  ASN   A CB  
675  C CG  . ASN   A 109 ? 0.2828 0.2649 0.3082 -0.0263 -0.0075 -0.0007 90  ASN   A CG  
676  O OD1 . ASN   A 109 ? 0.3227 0.3004 0.3387 -0.0271 -0.01   0.0023  90  ASN   A OD1 
677  N ND2 . ASN   A 109 ? 0.2628 0.2471 0.2944 -0.0219 -0.0107 -0.0014 90  ASN   A ND2 
678  N N   . LEU   A 110 ? 0.2724 0.2568 0.3085 -0.0422 0.0179  -0.0087 91  LEU   A N   
679  C CA  . LEU   A 110 ? 0.2994 0.2837 0.3369 -0.0471 0.0288  -0.013  91  LEU   A CA  
680  C C   . LEU   A 110 ? 0.3247 0.3008 0.3457 -0.0545 0.0344  -0.012  91  LEU   A C   
681  O O   . LEU   A 110 ? 0.3504 0.3219 0.3594 -0.0596 0.0415  -0.0146 91  LEU   A O   
682  C CB  . LEU   A 110 ? 0.3105 0.3012 0.372  -0.0464 0.0339  -0.0161 91  LEU   A CB  
683  C CG  . LEU   A 110 ? 0.3621 0.3596 0.4402 -0.04   0.0282  -0.0168 91  LEU   A CG  
684  C CD1 . LEU   A 110 ? 0.3706 0.3739 0.4751 -0.0399 0.0317  -0.0187 91  LEU   A CD1 
685  C CD2 . LEU   A 110 ? 0.3844 0.3823 0.4567 -0.0385 0.0295  -0.0191 91  LEU   A CD2 
686  N N   . GLN   A 111 ? 0.3128 0.2859 0.3314 -0.0558 0.031   -0.0082 92  GLN   A N   
687  C CA  . GLN   A 111 ? 0.3194 0.2834 0.3205 -0.0635 0.0353  -0.0063 92  GLN   A CA  
688  C C   . GLN   A 111 ? 0.3367 0.2932 0.3147 -0.0655 0.0298  -0.0031 92  GLN   A C   
689  O O   . GLN   A 111 ? 0.3692 0.3174 0.3292 -0.0731 0.0352  -0.0034 92  GLN   A O   
690  C CB  . GLN   A 111 ? 0.3482 0.3103 0.3529 -0.0641 0.0318  -0.0024 92  GLN   A CB  
691  C CG  . GLN   A 111 ? 0.4329 0.4013 0.4601 -0.0643 0.038   -0.0054 92  GLN   A CG  
692  C CD  . GLN   A 111 ? 0.5559 0.522  0.5867 -0.0658 0.0349  -0.0018 92  GLN   A CD  
693  O OE1 . GLN   A 111 ? 0.6191 0.5768 0.6335 -0.0702 0.0341  0.0019  92  GLN   A OE1 
694  N NE2 . GLN   A 111 ? 0.5732 0.5458 0.6253 -0.0625 0.0322  -0.0025 92  GLN   A NE2 
695  N N   . GLU   A 112 ? 0.3287 0.2876 0.3072 -0.0593 0.0192  -0.0001 93  GLU   A N   
696  C CA  . GLU   A 112 ? 0.3418 0.2949 0.3034 -0.0605 0.0126  0.0033  93  GLU   A CA  
697  C C   . GLU   A 112 ? 0.3706 0.323  0.3246 -0.0634 0.0176  -0.0008 93  GLU   A C   
698  O O   . GLU   A 112 ? 0.3728 0.3162 0.3068 -0.0701 0.0173  0.0008  93  GLU   A O   
699  C CB  . GLU   A 112 ? 0.3453 0.302  0.3139 -0.0527 0.0019  0.0068  93  GLU   A CB  
700  C CG  . GLU   A 112 ? 0.371  0.3226 0.3273 -0.0534 -0.0063 0.0114  93  GLU   A CG  
701  C CD  . GLU   A 112 ? 0.4113 0.3528 0.353  -0.059  -0.0111 0.0174  93  GLU   A CD  
702  O OE1 . GLU   A 112 ? 0.4406 0.3796 0.3844 -0.0598 -0.0105 0.0192  93  GLU   A OE1 
703  O OE2 . GLU   A 112 ? 0.4313 0.3668 0.3597 -0.0628 -0.0166 0.0209  93  GLU   A OE2 
704  N N   . LEU   A 113 ? 0.3708 0.3312 0.34   -0.0595 0.0225  -0.0061 94  LEU   A N   
705  C CA  . LEU   A 113 ? 0.409  0.3687 0.3738 -0.062  0.0288  -0.011  94  LEU   A CA  
706  C C   . LEU   A 113 ? 0.4088 0.3599 0.3598 -0.0715 0.0401  -0.0141 94  LEU   A C   
707  O O   . LEU   A 113 ? 0.4122 0.3548 0.3436 -0.0777 0.0421  -0.0153 94  LEU   A O   
708  C CB  . LEU   A 113 ? 0.426  0.3954 0.4134 -0.0566 0.0335  -0.016  94  LEU   A CB  
709  C CG  . LEU   A 113 ? 0.4602 0.4366 0.4581 -0.0489 0.0258  -0.0151 94  LEU   A CG  
710  C CD1 . LEU   A 113 ? 0.4612 0.4454 0.4809 -0.045  0.0305  -0.0195 94  LEU   A CD1 
711  C CD2 . LEU   A 113 ? 0.4661 0.4396 0.4515 -0.0498 0.0226  -0.0151 94  LEU   A CD2 
712  N N   . GLU   A 114 ? 0.3979 0.3503 0.359  -0.0732 0.0477  -0.0156 95  GLU   A N   
713  C CA  . GLU   A 114 ? 0.4159 0.3603 0.3666 -0.0824 0.061   -0.0192 95  GLU   A CA  
714  C C   . GLU   A 114 ? 0.4231 0.3538 0.3439 -0.0909 0.0583  -0.0148 95  GLU   A C   
715  O O   . GLU   A 114 ? 0.4431 0.3636 0.3449 -0.0996 0.0673  -0.0181 95  GLU   A O   
716  C CB  . GLU   A 114 ? 0.4533 0.4033 0.4253 -0.0819 0.0693  -0.0214 95  GLU   A CB  
717  C CG  . GLU   A 114 ? 0.542  0.503  0.5416 -0.0757 0.0736  -0.0266 95  GLU   A CG  
718  C CD  . GLU   A 114 ? 0.6573 0.6242 0.6823 -0.0759 0.0833  -0.0298 95  GLU   A CD  
719  O OE1 . GLU   A 114 ? 0.6843 0.6569 0.7241 -0.0721 0.0765  -0.0261 95  GLU   A OE1 
720  O OE2 . GLU   A 114 ? 0.6852 0.6508 0.7167 -0.0799 0.0976  -0.0362 95  GLU   A OE2 
721  N N   . LYS   A 115 ? 0.4197 0.3489 0.3348 -0.0888 0.0455  -0.0073 96  LYS   A N   
722  C CA  . LYS   A 115 ? 0.4356 0.3509 0.3225 -0.0969 0.0402  -0.0016 96  LYS   A CA  
723  C C   . LYS   A 115 ? 0.4405 0.3487 0.3079 -0.1011 0.0372  -0.0023 96  LYS   A C   
724  O O   . LYS   A 115 ? 0.4739 0.3679 0.3142 -0.1118 0.0404  -0.0019 96  LYS   A O   
725  C CB  . LYS   A 115 ? 0.4412 0.3573 0.3307 -0.0922 0.0257  0.0065  96  LYS   A CB  
726  C CG  . LYS   A 115 ? 0.5029 0.4204 0.4025 -0.0917 0.0279  0.0084  96  LYS   A CG  
727  C CD  . LYS   A 115 ? 0.5901 0.5061 0.4903 -0.0878 0.0142  0.0162  96  LYS   A CD  
728  C CE  . LYS   A 115 ? 0.6684 0.5836 0.5756 -0.0889 0.0171  0.0179  96  LYS   A CE  
729  N NZ  . LYS   A 115 ? 0.7068 0.6263 0.6276 -0.081  0.0067  0.0219  96  LYS   A NZ  
730  N N   . TRP   A 116 ? 0.4169 0.3339 0.2966 -0.0935 0.0315  -0.0038 97  TRP   A N   
731  C CA  . TRP   A 116 ? 0.4232 0.3341 0.2865 -0.0973 0.0282  -0.0047 97  TRP   A CA  
732  C C   . TRP   A 116 ? 0.4372 0.3431 0.2925 -0.1037 0.0433  -0.0133 97  TRP   A C   
733  O O   . TRP   A 116 ? 0.4453 0.3376 0.2737 -0.1133 0.0446  -0.014  97  TRP   A O   
734  C CB  . TRP   A 116 ? 0.4057 0.3274 0.2853 -0.0878 0.0185  -0.0037 97  TRP   A CB  
735  C CG  . TRP   A 116 ? 0.4168 0.3312 0.2787 -0.0926 0.0128  -0.0032 97  TRP   A CG  
736  C CD1 . TRP   A 116 ? 0.4447 0.3512 0.2911 -0.0964 -0.0003 0.0041  97  TRP   A CD1 
737  C CD2 . TRP   A 116 ? 0.4227 0.3357 0.2804 -0.0949 0.0198  -0.0101 97  TRP   A CD2 
738  N NE1 . TRP   A 116 ? 0.4639 0.3643 0.2963 -0.1012 -0.0028 0.0024  97  TRP   A NE1 
739  C CE2 . TRP   A 116 ? 0.4527 0.357  0.2913 -0.1003 0.0098  -0.0066 97  TRP   A CE2 
740  C CE3 . TRP   A 116 ? 0.4293 0.3479 0.3    -0.0927 0.0327  -0.0186 97  TRP   A CE3 
741  C CZ2 . TRP   A 116 ? 0.47   0.3697 0.2989 -0.1043 0.013   -0.0119 97  TRP   A CZ2 
742  C CZ3 . TRP   A 116 ? 0.4454 0.3593 0.3072 -0.0964 0.0369  -0.024  97  TRP   A CZ3 
743  C CH2 . TRP   A 116 ? 0.4646 0.3691 0.3049 -0.1022 0.0272  -0.0208 97  TRP   A CH2 
744  N N   . LEU   A 117 ? 0.43   0.3455 0.3081 -0.0989 0.0546  -0.0198 98  LEU   A N   
745  C CA  . LEU   A 117 ? 0.45   0.3616 0.3258 -0.104  0.0703  -0.0287 98  LEU   A CA  
746  C C   . LEU   A 117 ? 0.4805 0.3766 0.3313 -0.1165 0.0818  -0.0306 98  LEU   A C   
747  O O   . LEU   A 117 ? 0.5083 0.3931 0.3395 -0.1247 0.0908  -0.036  98  LEU   A O   
748  C CB  . LEU   A 117 ? 0.4436 0.3685 0.3526 -0.0965 0.0793  -0.0341 98  LEU   A CB  
749  C CG  . LEU   A 117 ? 0.4351 0.3732 0.3664 -0.0855 0.0704  -0.0336 98  LEU   A CG  
750  C CD1 . LEU   A 117 ? 0.4425 0.3929 0.4066 -0.0787 0.076   -0.0366 98  LEU   A CD1 
751  C CD2 . LEU   A 117 ? 0.4489 0.3837 0.3718 -0.0868 0.0711  -0.0377 98  LEU   A CD2 
752  N N   . LYS   A 118 ? 0.4881 0.3825 0.3379 -0.1185 0.0814  -0.0259 99  LYS   A N   
753  C CA  . LYS   A 118 ? 0.5257 0.4045 0.3504 -0.131  0.0921  -0.0267 99  LYS   A CA  
754  C C   . LYS   A 118 ? 0.5628 0.425  0.3506 -0.1401 0.0808  -0.0196 99  LYS   A C   
755  O O   . LYS   A 118 ? 0.5674 0.414  0.3293 -0.1518 0.0881  -0.0191 99  LYS   A O   
756  C CB  . LYS   A 118 ? 0.559  0.4427 0.4001 -0.1299 0.0978  -0.0251 99  LYS   A CB  
757  C CG  . LYS   A 118 ? 0.6464 0.544  0.5228 -0.1234 0.1101  -0.0323 99  LYS   A CG  
758  C CD  . LYS   A 118 ? 0.7477 0.652  0.6448 -0.1216 0.1139  -0.0304 99  LYS   A CD  
759  C CE  . LYS   A 118 ? 0.8124 0.732  0.7484 -0.1137 0.1214  -0.0362 99  LYS   A CE  
760  N NZ  . LYS   A 118 ? 0.8542 0.7818 0.8138 -0.1109 0.1218  -0.0337 99  LYS   A NZ  
761  N N   . ALA   A 119 ? 0.5708 0.4352 0.3555 -0.1358 0.0636  -0.0142 100 ALA   A N   
762  C CA  . ALA   A 119 ? 0.6116 0.4619 0.3664 -0.1432 0.0491  -0.0062 100 ALA   A CA  
763  C C   . ALA   A 119 ? 0.6413 0.484  0.3854 -0.1477 0.0436  0.002   100 ALA   A C   
764  O O   . ALA   A 119 ? 0.6714 0.4957 0.3824 -0.1598 0.0413  0.0061  100 ALA   A O   
765  C CB  . ALA   A 119 ? 0.6327 0.4651 0.3536 -0.1559 0.0549  -0.0104 100 ALA   A CB  
766  N N   . ALA   A 120 ? 0.628  0.4839 0.3991 -0.1383 0.0414  0.0046  101 ALA   A N   
767  C CA  . ALA   A 120 ? 0.6482 0.4986 0.414  -0.1409 0.0357  0.0123  101 ALA   A CA  
768  C C   . ALA   A 120 ? 0.6718 0.5177 0.429  -0.1399 0.0147  0.0226  101 ALA   A C   
769  O O   . ALA   A 120 ? 0.659  0.5143 0.4306 -0.1316 0.0045  0.0238  101 ALA   A O   
770  C CB  . ALA   A 120 ? 0.6382 0.5041 0.4368 -0.1309 0.0389  0.0113  101 ALA   A CB  
771  N N   . PRO   A 121 ? 0.6992 0.5299 0.433  -0.149  0.0079  0.0306  102 PRO   A N   
772  C CA  . PRO   A 121 ? 0.702  0.5282 0.4312 -0.148  -0.0131 0.0412  102 PRO   A CA  
773  C C   . PRO   A 121 ? 0.6714 0.514  0.4346 -0.1335 -0.0233 0.0446  102 PRO   A C   
774  O O   . PRO   A 121 ? 0.6798 0.5238 0.4477 -0.1297 -0.0382 0.0501  102 PRO   A O   
775  C CB  . PRO   A 121 ? 0.7315 0.5401 0.4358 -0.1591 -0.0161 0.0489  102 PRO   A CB  
776  C CG  . PRO   A 121 ? 0.7528 0.5517 0.4364 -0.1698 0.0033  0.0415  102 PRO   A CG  
777  C CD  . PRO   A 121 ? 0.7091 0.5257 0.4212 -0.1606 0.0188  0.0306  102 PRO   A CD  
778  N N   . ALA   A 122 ? 0.6298 0.4844 0.4167 -0.1257 -0.0151 0.0408  103 ALA   A N   
779  C CA  . ALA   A 122 ? 0.5865 0.4551 0.4034 -0.1126 -0.0227 0.0427  103 ALA   A CA  
780  C C   . ALA   A 122 ? 0.5411 0.4245 0.3785 -0.1028 -0.0213 0.0365  103 ALA   A C   
781  O O   . ALA   A 122 ? 0.5449 0.439  0.4053 -0.0925 -0.0259 0.0371  103 ALA   A O   
782  C CB  . ALA   A 122 ? 0.5831 0.4566 0.4145 -0.1093 -0.0155 0.0413  103 ALA   A CB  
783  N N   . ALA   A 123 ? 0.5156 0.3984 0.3439 -0.1065 -0.0138 0.0304  104 ALA   A N   
784  C CA  . ALA   A 123 ? 0.4945 0.3899 0.3403 -0.0983 -0.0122 0.0247  104 ALA   A CA  
785  C C   . ALA   A 123 ? 0.4757 0.3738 0.3278 -0.0932 -0.027  0.0302  104 ALA   A C   
786  O O   . ALA   A 123 ? 0.4939 0.382  0.3315 -0.0985 -0.0381 0.0374  104 ALA   A O   
787  C CB  . ALA   A 123 ? 0.5139 0.4051 0.3457 -0.1048 -0.0018 0.0177  104 ALA   A CB  
788  N N   . PHE   A 124 ? 0.4236 0.3349 0.2976 -0.0833 -0.0272 0.0268  105 PHE   A N   
789  C CA  . PHE   A 124 ? 0.4083 0.3233 0.2913 -0.0782 -0.0393 0.0311  105 PHE   A CA  
790  C C   . PHE   A 124 ? 0.4277 0.3352 0.2927 -0.0856 -0.0441 0.0318  105 PHE   A C   
791  O O   . PHE   A 124 ? 0.4491 0.3531 0.3012 -0.091  -0.035  0.0257  105 PHE   A O   
792  C CB  . PHE   A 124 ? 0.3704 0.2998 0.2777 -0.0675 -0.0357 0.0262  105 PHE   A CB  
793  C CG  . PHE   A 124 ? 0.3571 0.2917 0.2779 -0.0612 -0.0459 0.03    105 PHE   A CG  
794  C CD1 . PHE   A 124 ? 0.3556 0.2902 0.2872 -0.0569 -0.054  0.036   105 PHE   A CD1 
795  C CD2 . PHE   A 124 ? 0.3707 0.3102 0.2956 -0.0594 -0.0463 0.0271  105 PHE   A CD2 
796  C CE1 . PHE   A 124 ? 0.3483 0.2879 0.2954 -0.0511 -0.0617 0.039   105 PHE   A CE1 
797  C CE2 . PHE   A 124 ? 0.3608 0.3057 0.3006 -0.0536 -0.0544 0.0304  105 PHE   A CE2 
798  C CZ  . PHE   A 124 ? 0.3352 0.2805 0.2869 -0.0493 -0.0615 0.0361  105 PHE   A CZ  
799  N N   . ASP   A 125 ? 0.4405 0.3454 0.3065 -0.0854 -0.0582 0.039   106 ASP   A N   
800  C CA  . ASP   A 125 ? 0.4523 0.3497 0.3024 -0.0925 -0.0653 0.0406  106 ASP   A CA  
801  C C   . ASP   A 125 ? 0.4289 0.3375 0.2955 -0.0857 -0.0646 0.0362  106 ASP   A C   
802  O O   . ASP   A 125 ? 0.4382 0.3543 0.3245 -0.0788 -0.0733 0.0402  106 ASP   A O   
803  C CB  . ASP   A 125 ? 0.497  0.3856 0.3417 -0.0965 -0.0827 0.0515  106 ASP   A CB  
804  C CG  . ASP   A 125 ? 0.5631 0.4423 0.3903 -0.105  -0.0928 0.0545  106 ASP   A CG  
805  O OD1 . ASP   A 125 ? 0.5492 0.4267 0.3638 -0.1092 -0.085  0.0474  106 ASP   A OD1 
806  O OD2 . ASP   A 125 ? 0.6317 0.5048 0.4583 -0.1079 -0.1091 0.064   106 ASP   A OD2 
807  N N   . TRP   A 126 ? 0.4105 0.3197 0.2697 -0.0882 -0.0539 0.0281  107 TRP   A N   
808  C CA  . TRP   A 126 ? 0.3957 0.314  0.2681 -0.083  -0.0528 0.0237  107 TRP   A CA  
809  C C   . TRP   A 126 ? 0.4242 0.334  0.2807 -0.0907 -0.0617 0.0257  107 TRP   A C   
810  O O   . TRP   A 126 ? 0.4092 0.3252 0.2747 -0.0877 -0.0612 0.0222  107 TRP   A O   
811  C CB  . TRP   A 126 ? 0.3675 0.2902 0.2416 -0.0817 -0.0369 0.0139  107 TRP   A CB  
812  C CG  . TRP   A 126 ? 0.3338 0.2677 0.2293 -0.0725 -0.0299 0.0116  107 TRP   A CG  
813  C CD1 . TRP   A 126 ? 0.3304 0.2633 0.2249 -0.0734 -0.0213 0.0094  107 TRP   A CD1 
814  C CD2 . TRP   A 126 ? 0.3091 0.2556 0.229  -0.062  -0.0314 0.0112  107 TRP   A CD2 
815  N NE1 . TRP   A 126 ? 0.3213 0.2653 0.238  -0.064  -0.0191 0.0084  107 TRP   A NE1 
816  C CE2 . TRP   A 126 ? 0.3002 0.252  0.2312 -0.0572 -0.0246 0.0092  107 TRP   A CE2 
817  C CE3 . TRP   A 126 ? 0.3051 0.2581 0.238  -0.0567 -0.0382 0.0131  107 TRP   A CE3 
818  C CZ2 . TRP   A 126 ? 0.2868 0.2485 0.2382 -0.0479 -0.0247 0.0087  107 TRP   A CZ2 
819  C CZ3 . TRP   A 126 ? 0.2896 0.253  0.2436 -0.0472 -0.0365 0.0122  107 TRP   A CZ3 
820  C CH2 . TRP   A 126 ? 0.2817 0.2486 0.2432 -0.0433 -0.03   0.0099  107 TRP   A CH2 
821  N N   . SER   A 127 ? 0.4528 0.3476 0.2852 -0.1013 -0.0706 0.0316  108 SER   A N   
822  C CA  . SER   A 127 ? 0.4807 0.3649 0.2938 -0.1105 -0.0792 0.0331  108 SER   A CA  
823  C C   . SER   A 127 ? 0.4734 0.3663 0.3067 -0.1051 -0.0909 0.0364  108 SER   A C   
824  O O   . SER   A 127 ? 0.4812 0.3715 0.3065 -0.109  -0.0905 0.0323  108 SER   A O   
825  C CB  . SER   A 127 ? 0.5285 0.3939 0.3119 -0.1231 -0.0895 0.0404  108 SER   A CB  
826  O OG  . SER   A 127 ? 0.5791 0.4462 0.3758 -0.1197 -0.1037 0.0508  108 SER   A OG  
827  N N   . PRO   A 128 ? 0.4768 0.3804 0.3376 -0.096  -0.0995 0.0427  109 PRO   A N   
828  C CA  . PRO   A 128 ? 0.461  0.373  0.3423 -0.0913 -0.1084 0.045   109 PRO   A CA  
829  C C   . PRO   A 128 ? 0.4383 0.3616 0.3324 -0.0848 -0.0965 0.036   109 PRO   A C   
830  O O   . PRO   A 128 ? 0.4485 0.3738 0.3471 -0.0855 -0.1007 0.0353  109 PRO   A O   
831  C CB  . PRO   A 128 ? 0.4666 0.3874 0.3758 -0.0824 -0.1157 0.0521  109 PRO   A CB  
832  C CG  . PRO   A 128 ? 0.4884 0.4026 0.3878 -0.0842 -0.1143 0.055   109 PRO   A CG  
833  C CD  . PRO   A 128 ? 0.4784 0.3861 0.3534 -0.0899 -0.1009 0.0475  109 PRO   A CD  
834  N N   . VAL   A 129 ? 0.4158 0.346  0.3163 -0.0786 -0.082  0.0295  110 VAL   A N   
835  C CA  . VAL   A 129 ? 0.3862 0.3261 0.2989 -0.0726 -0.0712 0.0217  110 VAL   A CA  
836  C C   . VAL   A 129 ? 0.4021 0.3334 0.2932 -0.0807 -0.0646 0.015   110 VAL   A C   
837  O O   . VAL   A 129 ? 0.3951 0.3301 0.2918 -0.0796 -0.0629 0.0111  110 VAL   A O   
838  C CB  . VAL   A 129 ? 0.3658 0.3138 0.2909 -0.0647 -0.0598 0.018   110 VAL   A CB  
839  C CG1 . VAL   A 129 ? 0.361  0.3167 0.2956 -0.0599 -0.0489 0.0102  110 VAL   A CG1 
840  C CG2 . VAL   A 129 ? 0.3671 0.3224 0.3131 -0.0566 -0.0653 0.0237  110 VAL   A CG2 
841  N N   . VAL   A 130 ? 0.4168 0.3358 0.283  -0.0894 -0.0596 0.0131  111 VAL   A N   
842  C CA  . VAL   A 130 ? 0.4406 0.3492 0.2845 -0.0981 -0.0515 0.0059  111 VAL   A CA  
843  C C   . VAL   A 130 ? 0.46   0.3605 0.2912 -0.1054 -0.063  0.0082  111 VAL   A C   
844  O O   . VAL   A 130 ? 0.4697 0.3692 0.2981 -0.1072 -0.0579 0.0018  111 VAL   A O   
845  C CB  . VAL   A 130 ? 0.4651 0.36   0.2826 -0.1074 -0.0448 0.0046  111 VAL   A CB  
846  C CG1 . VAL   A 130 ? 0.4939 0.3747 0.2848 -0.1182 -0.0363 -0.003  111 VAL   A CG1 
847  C CG2 . VAL   A 130 ? 0.4523 0.3552 0.2834 -0.1009 -0.0327 0.0015  111 VAL   A CG2 
848  N N   . THR   A 131 ? 0.4702 0.3655 0.2969 -0.1093 -0.0792 0.0176  112 THR   A N   
849  C CA  . THR   A 131 ? 0.4842 0.3715 0.3006 -0.1167 -0.0933 0.0216  112 THR   A CA  
850  C C   . THR   A 131 ? 0.4744 0.3756 0.3178 -0.1084 -0.0948 0.0199  112 THR   A C   
851  O O   . THR   A 131 ? 0.4956 0.3919 0.3301 -0.1136 -0.0961 0.0164  112 THR   A O   
852  C CB  . THR   A 131 ? 0.5268 0.408  0.3403 -0.1208 -0.1119 0.0334  112 THR   A CB  
853  O OG1 . THR   A 131 ? 0.5553 0.4208 0.3388 -0.1304 -0.11   0.0346  112 THR   A OG1 
854  C CG2 . THR   A 131 ? 0.5553 0.4298 0.3636 -0.1278 -0.1291 0.0388  112 THR   A CG2 
855  N N   . TYR   A 132 ? 0.4409 0.3586 0.3159 -0.0959 -0.0934 0.0219  113 TYR   A N   
856  C CA  . TYR   A 132 ? 0.4261 0.357  0.3271 -0.0879 -0.0934 0.0206  113 TYR   A CA  
857  C C   . TYR   A 132 ? 0.4065 0.3385 0.3038 -0.0874 -0.0799 0.0105  113 TYR   A C   
858  O O   . TYR   A 132 ? 0.4109 0.3438 0.3116 -0.0887 -0.0827 0.0087  113 TYR   A O   
859  C CB  . TYR   A 132 ? 0.4208 0.3662 0.3516 -0.0758 -0.0922 0.0239  113 TYR   A CB  
860  C CG  . TYR   A 132 ? 0.4113 0.3692 0.3689 -0.0682 -0.0931 0.024   113 TYR   A CG  
861  C CD1 . TYR   A 132 ? 0.4187 0.3851 0.3871 -0.0614 -0.0807 0.0172  113 TYR   A CD1 
862  C CD2 . TYR   A 132 ? 0.4168 0.3776 0.3903 -0.0679 -0.1064 0.0313  113 TYR   A CD2 
863  C CE1 . TYR   A 132 ? 0.4187 0.3952 0.4096 -0.0552 -0.0808 0.0174  113 TYR   A CE1 
864  C CE2 . TYR   A 132 ? 0.4184 0.3905 0.4174 -0.0611 -0.1057 0.0312  113 TYR   A CE2 
865  C CZ  . TYR   A 132 ? 0.4243 0.4036 0.43   -0.0552 -0.0926 0.0241  113 TYR   A CZ  
866  O OH  . TYR   A 132 ? 0.4274 0.4167 0.4562 -0.0493 -0.0912 0.0241  113 TYR   A OH  
867  N N   . VAL   A 133 ? 0.3736 0.3049 0.2642 -0.0862 -0.0655 0.0038  114 VAL   A N   
868  C CA  . VAL   A 133 ? 0.3706 0.3022 0.2596 -0.0859 -0.0525 -0.0056 114 VAL   A CA  
869  C C   . VAL   A 133 ? 0.4103 0.3265 0.2723 -0.0978 -0.0531 -0.0097 114 VAL   A C   
870  O O   . VAL   A 133 ? 0.4063 0.3231 0.2714 -0.0979 -0.0493 -0.0151 114 VAL   A O   
871  C CB  . VAL   A 133 ? 0.3748 0.3093 0.2662 -0.0821 -0.038  -0.011  114 VAL   A CB  
872  C CG1 . VAL   A 133 ? 0.3895 0.323  0.2805 -0.0826 -0.0249 -0.0207 114 VAL   A CG1 
873  C CG2 . VAL   A 133 ? 0.3634 0.3123 0.2809 -0.0706 -0.0379 -0.0076 114 VAL   A CG2 
874  N N   . CYS   A 134 ? 0.44   0.3413 0.2746 -0.1083 -0.0578 -0.0072 115 CYS   A N   
875  C CA  . CYS   A 134 ? 0.477  0.3607 0.2814 -0.1212 -0.059  -0.0109 115 CYS   A CA  
876  C C   . CYS   A 134 ? 0.4856 0.3698 0.2952 -0.1231 -0.0729 -0.0074 115 CYS   A C   
877  O O   . CYS   A 134 ? 0.5006 0.3776 0.2995 -0.1284 -0.0695 -0.0136 115 CYS   A O   
878  C CB  . CYS   A 134 ? 0.5099 0.3766 0.2829 -0.1327 -0.0637 -0.007  115 CYS   A CB  
879  S SG  . CYS   A 134 ? 0.5525 0.4138 0.3124 -0.1345 -0.0438 -0.014  115 CYS   A SG  
880  N N   . ASP   A 135 ? 0.4748 0.368  0.3036 -0.1182 -0.0876 0.0024  116 ASP   A N   
881  C CA  . ASP   A 135 ? 0.4798 0.3765 0.3211 -0.1185 -0.1013 0.0068  116 ASP   A CA  
882  C C   . ASP   A 135 ? 0.489  0.3978 0.3523 -0.1105 -0.0925 0.0006  116 ASP   A C   
883  O O   . ASP   A 135 ? 0.52   0.424  0.3784 -0.1154 -0.096  -0.0019 116 ASP   A O   
884  C CB  . ASP   A 135 ? 0.4844 0.3907 0.3488 -0.1129 -0.1156 0.0179  116 ASP   A CB  
885  C CG  . ASP   A 135 ? 0.5935 0.4873 0.4396 -0.1216 -0.1299 0.0265  116 ASP   A CG  
886  O OD1 . ASP   A 135 ? 0.6038 0.4793 0.4142 -0.134  -0.1302 0.0243  116 ASP   A OD1 
887  O OD2 . ASP   A 135 ? 0.6499 0.5514 0.5169 -0.1165 -0.1406 0.0355  116 ASP   A OD2 
888  N N   . LEU   A 136 ? 0.4693 0.3927 0.356  -0.0986 -0.0815 -0.0017 117 LEU   A N   
889  C CA  . LEU   A 136 ? 0.4657 0.4    0.373  -0.091  -0.0735 -0.0067 117 LEU   A CA  
890  C C   . LEU   A 136 ? 0.4635 0.3884 0.3545 -0.0967 -0.0635 -0.0163 117 LEU   A C   
891  O O   . LEU   A 136 ? 0.4541 0.3815 0.3538 -0.0958 -0.0634 -0.0192 117 LEU   A O   
892  C CB  . LEU   A 136 ? 0.4627 0.4097 0.3897 -0.0796 -0.0626 -0.0082 117 LEU   A CB  
893  C CG  . LEU   A 136 ? 0.4871 0.4445 0.4337 -0.0721 -0.0685 -0.0005 117 LEU   A CG  
894  C CD1 . LEU   A 136 ? 0.4799 0.4468 0.4406 -0.0626 -0.0566 -0.0035 117 LEU   A CD1 
895  C CD2 . LEU   A 136 ? 0.4976 0.4632 0.4655 -0.0685 -0.078  0.0049  117 LEU   A CD2 
896  N N   . GLU   A 137 ? 0.4708 0.3848 0.3395 -0.1022 -0.0538 -0.0218 118 GLU   A N   
897  C CA  . GLU   A 137 ? 0.4878 0.392  0.3417 -0.1074 -0.0408 -0.0321 118 GLU   A CA  
898  C C   . GLU   A 137 ? 0.5315 0.4181 0.3576 -0.1204 -0.0467 -0.0345 118 GLU   A C   
899  O O   . GLU   A 137 ? 0.5723 0.4486 0.3845 -0.1256 -0.0354 -0.0438 118 GLU   A O   
900  C CB  . GLU   A 137 ? 0.5026 0.4027 0.347  -0.1079 -0.0266 -0.0371 118 GLU   A CB  
901  C CG  . GLU   A 137 ? 0.5004 0.4172 0.3732 -0.0953 -0.0198 -0.0364 118 GLU   A CG  
902  C CD  . GLU   A 137 ? 0.5134 0.4285 0.3831 -0.0948 -0.0056 -0.0414 118 GLU   A CD  
903  O OE1 . GLU   A 137 ? 0.5388 0.4393 0.3828 -0.1046 -0.0004 -0.0449 118 GLU   A OE1 
904  O OE2 . GLU   A 137 ? 0.4481 0.3756 0.3405 -0.0853 0       -0.0415 118 GLU   A OE2 
905  N N   . GLY   A 138 ? 0.5243 0.4073 0.3444 -0.1256 -0.0643 -0.0263 119 GLY   A N   
906  C CA  . GLY   A 138 ? 0.5483 0.4146 0.3431 -0.1383 -0.0729 -0.0274 119 GLY   A CA  
907  C C   . GLY   A 138 ? 0.5796 0.4257 0.3371 -0.1519 -0.0791 -0.0252 119 GLY   A C   
908  O O   . GLY   A 138 ? 0.6026 0.431  0.3324 -0.1645 -0.0845 -0.0275 119 GLY   A O   
909  N N   . ASN   A 139 ? 0.5831 0.4305 0.3377 -0.1505 -0.0789 -0.0205 120 ASN   A N   
910  C CA  . ASN   A 139 ? 0.6217 0.4492 0.3396 -0.1636 -0.0839 -0.0177 120 ASN   A CA  
911  C C   . ASN   A 139 ? 0.6622 0.4695 0.3452 -0.175  -0.069  -0.029  120 ASN   A C   
912  O O   . ASN   A 139 ? 0.6937 0.4792 0.3397 -0.1899 -0.0759 -0.0283 120 ASN   A O   
913  C CB  . ASN   A 139 ? 0.6474 0.4675 0.3564 -0.1715 -0.1083 -0.0067 120 ASN   A CB  
914  C CG  . ASN   A 139 ? 0.6667 0.5046 0.4086 -0.1608 -0.1205 0.0045  120 ASN   A CG  
915  O OD1 . ASN   A 139 ? 0.6841 0.5239 0.4266 -0.1584 -0.1204 0.0092  120 ASN   A OD1 
916  N ND2 . ASN   A 139 ? 0.6483 0.4996 0.4194 -0.1542 -0.13   0.0084  120 ASN   A ND2 
917  N N   . ARG   A 140 ? 0.6605 0.4743 0.3561 -0.1683 -0.0486 -0.0396 121 ARG   A N   
918  C CA  . ARG   A 140 ? 0.682  0.4782 0.3502 -0.1776 -0.0307 -0.0516 121 ARG   A CA  
919  C C   . ARG   A 140 ? 0.7121 0.4963 0.3553 -0.1846 -0.0233 -0.0515 121 ARG   A C   
920  O O   . ARG   A 140 ? 0.7501 0.5118 0.3566 -0.1982 -0.0146 -0.0582 121 ARG   A O   
921  C CB  . ARG   A 140 ? 0.6796 0.4879 0.3743 -0.1672 -0.0114 -0.0617 121 ARG   A CB  
922  C CG  . ARG   A 140 ? 0.6763 0.4993 0.401  -0.1581 -0.0172 -0.0613 121 ARG   A CG  
923  C CD  . ARG   A 140 ? 0.6809 0.5125 0.428  -0.1494 0.002   -0.0711 121 ARG   A CD  
924  N NE  . ARG   A 140 ? 0.6801 0.526  0.4567 -0.1402 -0.0021 -0.0706 121 ARG   A NE  
925  C CZ  . ARG   A 140 ? 0.7028 0.5412 0.4751 -0.1442 -0.0007 -0.0766 121 ARG   A CZ  
926  N NH1 . ARG   A 140 ? 0.7162 0.5324 0.4547 -0.1577 0.0042  -0.0839 121 ARG   A NH1 
927  N NH2 . ARG   A 140 ? 0.6885 0.5404 0.4888 -0.1355 -0.0042 -0.0754 121 ARG   A NH2 
928  N N   . VAL   A 141 ? 0.6955 0.4939 0.3582 -0.1757 -0.0249 -0.0447 122 VAL   A N   
929  C CA  . VAL   A 141 ? 0.7074 0.4969 0.3511 -0.1811 -0.0188 -0.0432 122 VAL   A CA  
930  C C   . VAL   A 141 ? 0.6997 0.4957 0.3501 -0.1783 -0.0377 -0.0294 122 VAL   A C   
931  O O   . VAL   A 141 ? 0.6921 0.504  0.3704 -0.169  -0.0514 -0.0221 122 VAL   A O   
932  C CB  . VAL   A 141 ? 0.7052 0.505  0.3682 -0.1727 0.0034  -0.0511 122 VAL   A CB  
933  C CG1 . VAL   A 141 ? 0.7127 0.5073 0.375  -0.1742 0.0224  -0.0647 122 VAL   A CG1 
934  C CG2 . VAL   A 141 ? 0.6932 0.5191 0.3995 -0.1558 -0.0003 -0.0458 122 VAL   A CG2 
935  N N   . LYS   A 142 ? 0.6969 0.48   0.3222 -0.1867 -0.0375 -0.0258 123 LYS   A N   
936  C CA  . LYS   A 142 ? 0.6915 0.4793 0.3232 -0.1842 -0.0534 -0.0132 123 LYS   A CA  
937  C C   . LYS   A 142 ? 0.6691 0.4717 0.3243 -0.1734 -0.0411 -0.014  123 LYS   A C   
938  O O   . LYS   A 142 ? 0.6603 0.4658 0.3207 -0.1707 -0.0209 -0.0239 123 LYS   A O   
939  C CB  . LYS   A 142 ? 0.743  0.5056 0.331  -0.2012 -0.0637 -0.0074 123 LYS   A CB  
940  C CG  . LYS   A 142 ? 0.8253 0.5717 0.3884 -0.213  -0.0782 -0.0058 123 LYS   A CG  
941  C CD  . LYS   A 142 ? 0.9243 0.6443 0.4423 -0.2305 -0.0898 0.0011  123 LYS   A CD  
942  C CE  . LYS   A 142 ? 1.0115 0.7116 0.4988 -0.2446 -0.103  0.0015  123 LYS   A CE  
943  N NZ  . LYS   A 142 ? 1.0308 0.7459 0.549  -0.237  -0.123  0.0087  123 LYS   A NZ  
944  N N   . GLY   A 143 ? 0.66   0.4709 0.3294 -0.1679 -0.0535 -0.0035 124 GLY   A N   
945  C CA  . GLY   A 143 ? 0.661  0.486  0.3537 -0.1576 -0.0454 -0.0026 124 GLY   A CA  
946  C C   . GLY   A 143 ? 0.6842 0.5022 0.3633 -0.1617 -0.0252 -0.0103 124 GLY   A C   
947  O O   . GLY   A 143 ? 0.6698 0.5017 0.3734 -0.1522 -0.011  -0.0166 124 GLY   A O   
948  N N   . PRO   A 144 ? 0.7049 0.5011 0.3456 -0.1764 -0.0233 -0.0098 125 PRO   A N   
949  C CA  . PRO   A 144 ? 0.7133 0.5031 0.3432 -0.1805 -0.0027 -0.0169 125 PRO   A CA  
950  C C   . PRO   A 144 ? 0.6951 0.4878 0.3331 -0.1784 0.0189  -0.0307 125 PRO   A C   
951  O O   . PRO   A 144 ? 0.6879 0.4889 0.343  -0.1731 0.0351  -0.036  125 PRO   A O   
952  C CB  . PRO   A 144 ? 0.7544 0.517  0.3366 -0.1985 -0.0064 -0.0136 125 PRO   A CB  
953  C CG  . PRO   A 144 ? 0.7669 0.5269 0.3446 -0.2002 -0.033  -0.0006 125 PRO   A CG  
954  C CD  . PRO   A 144 ? 0.7263 0.5026 0.3328 -0.1899 -0.0407 -0.0015 125 PRO   A CD  
955  N N   . GLU   A 145 ? 0.6803 0.4664 0.3084 -0.1825 0.0189  -0.0361 126 GLU   A N   
956  C CA  . GLU   A 145 ? 0.6646 0.4525 0.3018 -0.1806 0.0386  -0.0492 126 GLU   A CA  
957  C C   . GLU   A 145 ? 0.6303 0.4448 0.3155 -0.1629 0.0411  -0.0502 126 GLU   A C   
958  O O   . GLU   A 145 ? 0.6267 0.4479 0.3299 -0.1581 0.0589  -0.0583 126 GLU   A O   
959  C CB  . GLU   A 145 ? 0.7032 0.4773 0.3186 -0.1891 0.0357  -0.054  126 GLU   A CB  
960  C CG  . GLU   A 145 ? 0.7382 0.5138 0.3651 -0.1867 0.056   -0.0675 126 GLU   A CG  
961  C CD  . GLU   A 145 ? 0.8384 0.596  0.4384 -0.1973 0.0572  -0.0744 126 GLU   A CD  
962  O OE1 . GLU   A 145 ? 0.8563 0.5991 0.4258 -0.2078 0.0409  -0.0683 126 GLU   A OE1 
963  O OE2 . GLU   A 145 ? 0.8564 0.6145 0.4668 -0.1953 0.0739  -0.0857 126 GLU   A OE2 
964  N N   . LYS   A 146 ? 0.588  0.4164 0.2935 -0.1539 0.0234  -0.042  127 LYS   A N   
965  C CA  . LYS   A 146 ? 0.5568 0.4086 0.3043 -0.1381 0.0241  -0.0418 127 LYS   A CA  
966  C C   . LYS   A 146 ? 0.5425 0.4038 0.3073 -0.1318 0.0322  -0.0409 127 LYS   A C   
967  O O   . LYS   A 146 ? 0.5284 0.4006 0.3175 -0.1243 0.0446  -0.0468 127 LYS   A O   
968  C CB  . LYS   A 146 ? 0.5497 0.4118 0.3117 -0.1314 0.0038  -0.0324 127 LYS   A CB  
969  C CG  . LYS   A 146 ? 0.5665 0.4506 0.367  -0.1162 0.0023  -0.0299 127 LYS   A CG  
970  C CD  . LYS   A 146 ? 0.616  0.5096 0.4355 -0.1096 0.0004  -0.0326 127 LYS   A CD  
971  C CE  . LYS   A 146 ? 0.6302 0.5266 0.4607 -0.1069 0.0175  -0.0427 127 LYS   A CE  
972  N NZ  . LYS   A 146 ? 0.5897 0.4907 0.4322 -0.1033 0.0163  -0.0461 127 LYS   A NZ  
973  N N   . GLU   A 147 ? 0.5507 0.4073 0.3033 -0.1353 0.0249  -0.0333 128 GLU   A N   
974  C CA  . GLU   A 147 ? 0.5437 0.4078 0.3106 -0.1305 0.0317  -0.032  128 GLU   A CA  
975  C C   . GLU   A 147 ? 0.5542 0.4126 0.3173 -0.1351 0.053   -0.0415 128 GLU   A C   
976  O O   . GLU   A 147 ? 0.5405 0.4113 0.3298 -0.1272 0.0619  -0.0441 128 GLU   A O   
977  C CB  . GLU   A 147 ? 0.5605 0.417  0.3107 -0.1355 0.0205  -0.0224 128 GLU   A CB  
978  C CG  . GLU   A 147 ? 0.5857 0.4506 0.3482 -0.1289 0.0003  -0.0123 128 GLU   A CG  
979  C CD  . GLU   A 147 ? 0.6482 0.5087 0.4031 -0.1312 -0.01   -0.0026 128 GLU   A CD  
980  O OE1 . GLU   A 147 ? 0.6608 0.5097 0.396  -0.1394 -0.0025 -0.0031 128 GLU   A OE1 
981  O OE2 . GLU   A 147 ? 0.648  0.5162 0.4178 -0.1247 -0.0252 0.0055  128 GLU   A OE2 
982  N N   . GLU   A 148 ? 0.5815 0.4202 0.3118 -0.1484 0.0616  -0.0469 129 GLU   A N   
983  C CA  . GLU   A 148 ? 0.5949 0.4272 0.3223 -0.1534 0.0843  -0.0569 129 GLU   A CA  
984  C C   . GLU   A 148 ? 0.5762 0.4209 0.3347 -0.1445 0.0959  -0.0657 129 GLU   A C   
985  O O   . GLU   A 148 ? 0.5899 0.4416 0.3696 -0.1408 0.1106  -0.0708 129 GLU   A O   
986  C CB  . GLU   A 148 ? 0.6373 0.4436 0.3203 -0.1704 0.0922  -0.0615 129 GLU   A CB  
987  C CG  . GLU   A 148 ? 0.7529 0.5508 0.4325 -0.1764 0.1182  -0.0729 129 GLU   A CG  
988  C CD  . GLU   A 148 ? 0.8503 0.6522 0.5403 -0.1758 0.1287  -0.0719 129 GLU   A CD  
989  O OE1 . GLU   A 148 ? 0.8391 0.6474 0.5331 -0.1723 0.1154  -0.0618 129 GLU   A OE1 
990  O OE2 . GLU   A 148 ? 0.8939 0.6919 0.5891 -0.1791 0.151   -0.0816 129 GLU   A OE2 
991  N N   . LYS   A 149 ? 0.5544 0.4027 0.3184 -0.1409 0.0884  -0.0667 130 LYS   A N   
992  C CA  . LYS   A 149 ? 0.5484 0.4083 0.3425 -0.1323 0.0973  -0.074  130 LYS   A CA  
993  C C   . LYS   A 149 ? 0.5134 0.3949 0.3473 -0.1184 0.0947  -0.0702 130 LYS   A C   
994  O O   . LYS   A 149 ? 0.5037 0.3926 0.3627 -0.1135 0.1078  -0.0763 130 LYS   A O   
995  C CB  . LYS   A 149 ? 0.5846 0.4443 0.3764 -0.131  0.0873  -0.0742 130 LYS   A CB  
996  C CG  . LYS   A 149 ? 0.6449 0.5113 0.4616 -0.125  0.0992  -0.0831 130 LYS   A CG  
997  C CD  . LYS   A 149 ? 0.7392 0.5994 0.5459 -0.1277 0.0939  -0.0858 130 LYS   A CD  
998  C CE  . LYS   A 149 ? 0.8042 0.6592 0.6182 -0.1292 0.1118  -0.0979 130 LYS   A CE  
999  N NZ  . LYS   A 149 ? 0.8494 0.6987 0.6549 -0.1313 0.1056  -0.1003 130 LYS   A NZ  
1000 N N   . LEU   A 150 ? 0.4755 0.3653 0.3139 -0.113  0.0783  -0.0602 131 LEU   A N   
1001 C CA  . LEU   A 150 ? 0.4451 0.3525 0.316  -0.1013 0.0752  -0.0565 131 LEU   A CA  
1002 C C   . LEU   A 150 ? 0.4566 0.3644 0.3339 -0.1028 0.0867  -0.0581 131 LEU   A C   
1003 O O   . LEU   A 150 ? 0.4431 0.362  0.3494 -0.0958 0.0937  -0.0609 131 LEU   A O   
1004 C CB  . LEU   A 150 ? 0.4269 0.3415 0.3001 -0.0959 0.0564  -0.0463 131 LEU   A CB  
1005 C CG  . LEU   A 150 ? 0.3905 0.321  0.293  -0.0848 0.0528  -0.0424 131 LEU   A CG  
1006 C CD1 . LEU   A 150 ? 0.3927 0.3346 0.3241 -0.0764 0.0582  -0.0472 131 LEU   A CD1 
1007 C CD2 . LEU   A 150 ? 0.4053 0.3409 0.3088 -0.0801 0.0361  -0.0334 131 LEU   A CD2 
1008 N N   . ARG   A 151 ? 0.4739 0.3688 0.3245 -0.1124 0.0887  -0.0562 132 ARG   A N   
1009 C CA  . ARG   A 151 ? 0.4959 0.3901 0.3514 -0.1149 0.1003  -0.0576 132 ARG   A CA  
1010 C C   . ARG   A 151 ? 0.5084 0.4018 0.3777 -0.1164 0.121   -0.0682 132 ARG   A C   
1011 O O   . ARG   A 151 ? 0.5085 0.4114 0.404  -0.1117 0.1286  -0.0696 132 ARG   A O   
1012 C CB  . ARG   A 151 ? 0.514  0.3917 0.3342 -0.1265 0.099   -0.0536 132 ARG   A CB  
1013 C CG  . ARG   A 151 ? 0.5284 0.4092 0.3438 -0.1234 0.0792  -0.0422 132 ARG   A CG  
1014 C CD  . ARG   A 151 ? 0.565  0.4291 0.347  -0.1351 0.0768  -0.0373 132 ARG   A CD  
1015 N NE  . ARG   A 151 ? 0.5604 0.4294 0.3456 -0.1305 0.0593  -0.0265 132 ARG   A NE  
1016 C CZ  . ARG   A 151 ? 0.5828 0.444  0.3485 -0.1342 0.0432  -0.0189 132 ARG   A CZ  
1017 N NH1 . ARG   A 151 ? 0.5931 0.4399 0.3311 -0.1438 0.0413  -0.0204 132 ARG   A NH1 
1018 N NH2 . ARG   A 151 ? 0.5723 0.439  0.3463 -0.129  0.0286  -0.0096 132 ARG   A NH2 
1019 N N   . GLN   A 152 ? 0.5316 0.4141 0.3859 -0.1226 0.1296  -0.0758 133 GLN   A N   
1020 C CA  . GLN   A 152 ? 0.5488 0.43   0.4188 -0.1237 0.1504  -0.0867 133 GLN   A CA  
1021 C C   . GLN   A 152 ? 0.5215 0.4207 0.4339 -0.1111 0.1497  -0.0884 133 GLN   A C   
1022 O O   . GLN   A 152 ? 0.5237 0.4274 0.4618 -0.109  0.1645  -0.0946 133 GLN   A O   
1023 C CB  . GLN   A 152 ? 0.6148 0.4774 0.4555 -0.1345 0.1607  -0.0951 133 GLN   A CB  
1024 C CG  . GLN   A 152 ? 0.7215 0.5628 0.5183 -0.1493 0.1653  -0.0949 133 GLN   A CG  
1025 C CD  . GLN   A 152 ? 0.8138 0.6514 0.6149 -0.1542 0.1844  -0.0992 133 GLN   A CD  
1026 O OE1 . GLN   A 152 ? 0.8345 0.6786 0.6649 -0.1504 0.2013  -0.1071 133 GLN   A OE1 
1027 N NE2 . GLN   A 152 ? 0.8423 0.6691 0.6157 -0.1628 0.1821  -0.0938 133 GLN   A NE2 
1028 N N   . ALA   A 153 ? 0.4871 0.3963 0.4083 -0.1028 0.1324  -0.0824 134 ALA   A N   
1029 C CA  . ALA   A 153 ? 0.4706 0.3951 0.4287 -0.0916 0.13    -0.0831 134 ALA   A CA  
1030 C C   . ALA   A 153 ? 0.446  0.3847 0.4332 -0.0837 0.1264  -0.0783 134 ALA   A C   
1031 O O   . ALA   A 153 ? 0.4274 0.3758 0.447  -0.0772 0.1307  -0.0808 134 ALA   A O   
1032 C CB  . ALA   A 153 ? 0.4618 0.3906 0.4171 -0.0865 0.114   -0.0785 134 ALA   A CB  
1033 N N   . VAL   A 154 ? 0.4546 0.3937 0.4307 -0.0847 0.1182  -0.0712 135 VAL   A N   
1034 C CA  . VAL   A 154 ? 0.4559 0.4072 0.4569 -0.0778 0.1133  -0.0662 135 VAL   A CA  
1035 C C   . VAL   A 154 ? 0.4845 0.4344 0.4963 -0.0819 0.1284  -0.0702 135 VAL   A C   
1036 O O   . VAL   A 154 ? 0.4962 0.4368 0.486  -0.0897 0.1327  -0.0693 135 VAL   A O   
1037 C CB  . VAL   A 154 ? 0.4498 0.4028 0.4372 -0.0758 0.0967  -0.0568 135 VAL   A CB  
1038 C CG1 . VAL   A 154 ? 0.4441 0.4085 0.4559 -0.069  0.0913  -0.0522 135 VAL   A CG1 
1039 C CG2 . VAL   A 154 ? 0.4404 0.3949 0.4196 -0.072  0.0832  -0.0532 135 VAL   A CG2 
1040 N N   . LYS   A 155 ? 0.4901 0.4489 0.5366 -0.0771 0.136   -0.074  136 LYS   A N   
1041 C CA  . LYS   A 155 ? 0.499  0.458  0.5617 -0.0806 0.151   -0.0778 136 LYS   A CA  
1042 C C   . LYS   A 155 ? 0.4656 0.4371 0.5559 -0.0744 0.143   -0.0718 136 LYS   A C   
1043 O O   . LYS   A 155 ? 0.4867 0.4579 0.585  -0.0781 0.1518  -0.0725 136 LYS   A O   
1044 C CB  . LYS   A 155 ? 0.5486 0.5065 0.6326 -0.0816 0.169   -0.0876 136 LYS   A CB  
1045 C CG  . LYS   A 155 ? 0.6495 0.5967 0.7122 -0.0855 0.1743  -0.0939 136 LYS   A CG  
1046 C CD  . LYS   A 155 ? 0.7395 0.6692 0.7712 -0.098  0.1916  -0.1008 136 LYS   A CD  
1047 C CE  . LYS   A 155 ? 0.8019 0.7214 0.825  -0.1018 0.203   -0.1101 136 LYS   A CE  
1048 N NZ  . LYS   A 155 ? 0.8346 0.7579 0.8541 -0.0959 0.187   -0.1069 136 LYS   A NZ  
1049 N N   . GLN   A 156 ? 0.4097 0.3914 0.5144 -0.0655 0.1266  -0.0661 137 GLN   A N   
1050 C CA  . GLN   A 156 ? 0.349  0.3409 0.4778 -0.0601 0.1176  -0.0605 137 GLN   A CA  
1051 C C   . GLN   A 156 ? 0.3287 0.3228 0.4428 -0.0558 0.0989  -0.0523 137 GLN   A C   
1052 O O   . GLN   A 156 ? 0.3343 0.3275 0.4362 -0.053  0.0909  -0.051  137 GLN   A O   
1053 C CB  . GLN   A 156 ? 0.3428 0.3446 0.5103 -0.0537 0.1174  -0.062  137 GLN   A CB  
1054 C CG  . GLN   A 156 ? 0.3633 0.3634 0.5506 -0.057  0.1371  -0.0709 137 GLN   A CG  
1055 C CD  . GLN   A 156 ? 0.4083 0.4184 0.6377 -0.0505 0.1355  -0.0714 137 GLN   A CD  
1056 O OE1 . GLN   A 156 ? 0.3964 0.4148 0.6521 -0.0472 0.1286  -0.0669 137 GLN   A OE1 
1057 N NE2 . GLN   A 156 ? 0.4195 0.4282 0.6562 -0.0488 0.1406  -0.0764 137 GLN   A NE2 
1058 N N   . VAL   A 157 ? 0.3091 0.3051 0.4242 -0.0558 0.0932  -0.0474 138 VAL   A N   
1059 C CA  . VAL   A 157 ? 0.3079 0.3048 0.4107 -0.0523 0.0774  -0.0401 138 VAL   A CA  
1060 C C   . VAL   A 157 ? 0.3017 0.3068 0.4311 -0.0481 0.071   -0.037  138 VAL   A C   
1061 O O   . VAL   A 157 ? 0.3213 0.327  0.461  -0.0512 0.0765  -0.037  138 VAL   A O   
1062 C CB  . VAL   A 157 ? 0.3351 0.3232 0.4099 -0.0585 0.0782  -0.0377 138 VAL   A CB  
1063 C CG1 . VAL   A 157 ? 0.3544 0.3433 0.4199 -0.0547 0.0632  -0.0306 138 VAL   A CG1 
1064 C CG2 . VAL   A 157 ? 0.3644 0.3428 0.4124 -0.0641 0.084   -0.0408 138 VAL   A CG2 
1065 N N   . LEU   A 158 ? 0.2797 0.2905 0.4216 -0.0416 0.0599  -0.0343 139 LEU   A N   
1066 C CA  . LEU   A 158 ? 0.2498 0.2672 0.4182 -0.0381 0.0531  -0.0317 139 LEU   A CA  
1067 C C   . LEU   A 158 ? 0.24   0.2579 0.4022 -0.0342 0.0376  -0.0257 139 LEU   A C   
1068 O O   . LEU   A 158 ? 0.2357 0.2511 0.3805 -0.0316 0.0312  -0.024  139 LEU   A O   
1069 C CB  . LEU   A 158 ? 0.2478 0.2705 0.4416 -0.0348 0.0549  -0.0344 139 LEU   A CB  
1070 C CG  . LEU   A 158 ? 0.2802 0.3024 0.4848 -0.038  0.0716  -0.0416 139 LEU   A CG  
1071 C CD1 . LEU   A 158 ? 0.2694 0.2962 0.4992 -0.0338 0.0713  -0.0435 139 LEU   A CD1 
1072 C CD2 . LEU   A 158 ? 0.2779 0.3016 0.4998 -0.0421 0.0816  -0.0434 139 LEU   A CD2 
1073 N N   . LYS   A 159 ? 0.2305 0.2513 0.4093 -0.0336 0.0315  -0.0227 140 LYS   A N   
1074 C CA  . LYS   A 159 ? 0.239  0.259  0.4146 -0.0305 0.0171  -0.0176 140 LYS   A CA  
1075 C C   . LYS   A 159 ? 0.2469 0.2693 0.4325 -0.0263 0.0098  -0.0167 140 LYS   A C   
1076 O O   . LYS   A 159 ? 0.2499 0.277  0.4592 -0.0256 0.0133  -0.0186 140 LYS   A O   
1077 C CB  . LYS   A 159 ? 0.2744 0.2964 0.4682 -0.0324 0.0132  -0.0152 140 LYS   A CB  
1078 C CG  . LYS   A 159 ? 0.3701 0.3897 0.5617 -0.0304 -0.0021 -0.0102 140 LYS   A CG  
1079 C CD  . LYS   A 159 ? 0.4856 0.4986 0.65   -0.031  -0.0051 -0.0085 140 LYS   A CD  
1080 C CE  . LYS   A 159 ? 0.5507 0.5603 0.7165 -0.0324 -0.0143 -0.005  140 LYS   A CE  
1081 N NZ  . LYS   A 159 ? 0.5797 0.5832 0.7235 -0.0337 -0.0133 -0.0043 140 LYS   A NZ  
1082 N N   A CYS   A 160 ? 0.2284 0.2472 0.397  -0.0236 0.0002  -0.0137 141 CYS   A N   
1083 N N   B CYS   A 160 ? 0.2343 0.2531 0.4028 -0.0237 0.0002  -0.0136 141 CYS   A N   
1084 C CA  A CYS   A 160 ? 0.2173 0.2367 0.3925 -0.0204 -0.0078 -0.0119 141 CYS   A CA  
1085 C CA  B CYS   A 160 ? 0.2285 0.2476 0.4013 -0.0204 -0.0073 -0.0121 141 CYS   A CA  
1086 C C   A CYS   A 160 ? 0.2023 0.2163 0.3644 -0.0194 -0.0202 -0.0074 141 CYS   A C   
1087 C C   B CYS   A 160 ? 0.2079 0.2218 0.369  -0.0193 -0.02   -0.0075 141 CYS   A C   
1088 O O   A CYS   A 160 ? 0.2131 0.2226 0.3562 -0.0201 -0.0212 -0.0065 141 CYS   A O   
1089 O O   B CYS   A 160 ? 0.2184 0.2277 0.3599 -0.0198 -0.021  -0.0066 141 CYS   A O   
1090 C CB  A CYS   A 160 ? 0.2265 0.2461 0.3931 -0.0185 -0.0028 -0.0146 141 CYS   A CB  
1091 C CB  B CYS   A 160 ? 0.2508 0.2693 0.4097 -0.0188 -0.0019 -0.0147 141 CYS   A CB  
1092 S SG  A CYS   A 160 ? 0.2173 0.2314 0.3514 -0.0174 -0.0049 -0.0135 141 CYS   A SG  
1093 S SG  B CYS   A 160 ? 0.2624 0.2795 0.419  -0.015  -0.0109 -0.0123 141 CYS   A SG  
1094 N N   . ASP   A 161 ? 0.1901 0.2034 0.3618 -0.0182 -0.0296 -0.0045 142 ASP   A N   
1095 C CA  . ASP   A 161 ? 0.1785 0.1844 0.3348 -0.0181 -0.0408 -0.0006 142 ASP   A CA  
1096 C C   . ASP   A 161 ? 0.1864 0.1912 0.3446 -0.0161 -0.0457 0.0009  142 ASP   A C   
1097 O O   . ASP   A 161 ? 0.2003 0.2072 0.3793 -0.0164 -0.0513 0.003   142 ASP   A O   
1098 C CB  . ASP   A 161 ? 0.1908 0.1937 0.3557 -0.0209 -0.0506 0.0029  142 ASP   A CB  
1099 C CG  . ASP   A 161 ? 0.2012 0.1938 0.3461 -0.022  -0.0615 0.0062  142 ASP   A CG  
1100 O OD1 . ASP   A 161 ? 0.2137 0.2019 0.3411 -0.0202 -0.0617 0.0062  142 ASP   A OD1 
1101 O OD2 . ASP   A 161 ? 0.2214 0.2095 0.3685 -0.025  -0.0702 0.0089  142 ASP   A OD2 
1102 N N   . VAL   A 162 ? 0.1734 0.1749 0.3116 -0.0143 -0.0437 0.0002  143 VAL   A N   
1103 C CA  . VAL   A 162 ? 0.184  0.1843 0.3227 -0.0127 -0.0472 0.0015  143 VAL   A CA  
1104 C C   . VAL   A 162 ? 0.2079 0.2011 0.3459 -0.0144 -0.0602 0.0066  143 VAL   A C   
1105 O O   . VAL   A 162 ? 0.2014 0.1932 0.3438 -0.0137 -0.0645 0.0086  143 VAL   A O   
1106 C CB  . VAL   A 162 ? 0.1904 0.1885 0.3085 -0.0108 -0.0422 -0.0001 143 VAL   A CB  
1107 C CG1 . VAL   A 162 ? 0.1984 0.2021 0.3156 -0.01   -0.0314 -0.0043 143 VAL   A CG1 
1108 C CG2 . VAL   A 162 ? 0.2054 0.1952 0.3008 -0.0115 -0.046  0.0016  143 VAL   A CG2 
1109 N N   . THR   A 163 ? 0.2049 0.1917 0.3338 -0.0171 -0.0669 0.0088  144 THR   A N   
1110 C CA  . THR   A 163 ? 0.2292 0.2064 0.3525 -0.0201 -0.0804 0.0138  144 THR   A CA  
1111 C C   . THR   A 163 ? 0.2375 0.2179 0.3888 -0.0218 -0.0896 0.0174  144 THR   A C   
1112 O O   . THR   A 163 ? 0.2591 0.231  0.4075 -0.0249 -0.1029 0.0226  144 THR   A O   
1113 C CB  . THR   A 163 ? 0.2598 0.2267 0.3604 -0.0231 -0.0847 0.0145  144 THR   A CB  
1114 O OG1 . THR   A 163 ? 0.2766 0.2469 0.3894 -0.0247 -0.0853 0.0141  144 THR   A OG1 
1115 C CG2 . THR   A 163 ? 0.2639 0.2279 0.3413 -0.0212 -0.0753 0.011   144 THR   A CG2 
1116 N N   . GLN   A 164 ? 0.2104 0.2018 0.3882 -0.0202 -0.0828 0.015   145 GLN   A N   
1117 C CA  . GLN   A 164 ? 0.2111 0.2066 0.4207 -0.0215 -0.0906 0.0182  145 GLN   A CA  
1118 C C   . GLN   A 164 ? 0.2174 0.2187 0.4489 -0.0187 -0.0882 0.018   145 GLN   A C   
1119 O O   . GLN   A 164 ? 0.2177 0.224  0.4475 -0.0156 -0.0758 0.0132  145 GLN   A O   
1120 C CB  . GLN   A 164 ? 0.2199 0.2233 0.4478 -0.022  -0.0832 0.0153  145 GLN   A CB  
1121 C CG  . GLN   A 164 ? 0.2613 0.2589 0.4691 -0.0249 -0.0853 0.0155  145 GLN   A CG  
1122 C CD  . GLN   A 164 ? 0.2956 0.2822 0.4939 -0.029  -0.1022 0.0212  145 GLN   A CD  
1123 O OE1 . GLN   A 164 ? 0.3057 0.2924 0.5258 -0.0311 -0.114  0.0259  145 GLN   A OE1 
1124 N NE2 . GLN   A 164 ? 0.3871 0.363  0.5532 -0.0306 -0.1047 0.0212  145 GLN   A NE2 
1125 N N   . SER   A 165 ? 0.22   0.2206 0.4752 -0.02   -0.1007 0.0234  146 SER   A N   
1126 C CA  . SER   A 165 ? 0.2276 0.2331 0.5085 -0.0174 -0.1002 0.024   146 SER   A CA  
1127 C C   . SER   A 165 ? 0.233  0.2502 0.5373 -0.0143 -0.0829 0.017   146 SER   A C   
1128 O O   . SER   A 165 ? 0.2364 0.2568 0.5495 -0.0113 -0.0757 0.0142  146 SER   A O   
1129 C CB  . SER   A 165 ? 0.2692 0.2725 0.5766 -0.0197 -0.1175 0.0316  146 SER   A CB  
1130 O OG  . SER   A 165 ? 0.3175 0.3074 0.5983 -0.0236 -0.1332 0.038   146 SER   A OG  
1131 N N   . GLN   A 166 ? 0.231  0.2534 0.5444 -0.0154 -0.0762 0.0141  147 GLN   A N   
1132 C CA  . GLN   A 166 ? 0.2284 0.2594 0.557  -0.0139 -0.0582 0.007   147 GLN   A CA  
1133 C C   . GLN   A 166 ? 0.2325 0.2614 0.5287 -0.0149 -0.0491 0.0029  147 GLN   A C   
1134 O O   . GLN   A 166 ? 0.2451 0.2742 0.5397 -0.0174 -0.0493 0.0033  147 GLN   A O   
1135 C CB  . GLN   A 166 ? 0.2489 0.2868 0.6159 -0.0151 -0.0572 0.0072  147 GLN   A CB  
1136 C CG  . GLN   A 166 ? 0.2661 0.3072 0.671  -0.0135 -0.0644 0.0107  147 GLN   A CG  
1137 C CD  . GLN   A 166 ? 0.3005 0.3349 0.7062 -0.0153 -0.0873 0.0202  147 GLN   A CD  
1138 O OE1 . GLN   A 166 ? 0.3593 0.3893 0.764  -0.014  -0.0959 0.0239  147 GLN   A OE1 
1139 N NE2 . GLN   A 166 ? 0.2795 0.3116 0.6852 -0.0189 -0.0979 0.0244  147 GLN   A NE2 
1140 N N   . PRO   A 167 ? 0.2067 0.2334 0.4775 -0.0133 -0.0417 -0.0005 148 PRO   A N   
1141 C CA  . PRO   A 167 ? 0.2166 0.2406 0.4581 -0.0144 -0.0354 -0.003  148 PRO   A CA  
1142 C C   . PRO   A 167 ? 0.2291 0.2576 0.4774 -0.0162 -0.0229 -0.0075 148 PRO   A C   
1143 O O   . PRO   A 167 ? 0.2396 0.2655 0.4702 -0.0181 -0.0219 -0.0074 148 PRO   A O   
1144 C CB  . PRO   A 167 ? 0.2166 0.2387 0.4378 -0.0122 -0.0301 -0.0055 148 PRO   A CB  
1145 C CG  . PRO   A 167 ? 0.2311 0.2515 0.461  -0.0105 -0.0389 -0.0021 148 PRO   A CG  
1146 C CD  . PRO   A 167 ? 0.2047 0.2302 0.4715 -0.0107 -0.041  -0.0011 148 PRO   A CD  
1147 N N   . LEU   A 168 ? 0.2288 0.263  0.5022 -0.0162 -0.013  -0.0113 149 LEU   A N   
1148 C CA  . LEU   A 168 ? 0.2338 0.271  0.5131 -0.0189 0.0007  -0.016  149 LEU   A CA  
1149 C C   . LEU   A 168 ? 0.228  0.2695 0.5363 -0.0208 -0.0016 -0.014  149 LEU   A C   
1150 O O   . LEU   A 168 ? 0.2393 0.2837 0.5585 -0.0233 0.0111  -0.0181 149 LEU   A O   
1151 C CB  . LEU   A 168 ? 0.2387 0.2779 0.5246 -0.0188 0.0161  -0.0228 149 LEU   A CB  
1152 C CG  . LEU   A 168 ? 0.2664 0.3016 0.5261 -0.0172 0.0178  -0.0247 149 LEU   A CG  
1153 C CD1 . LEU   A 168 ? 0.2948 0.3305 0.5612 -0.0179 0.0325  -0.0316 149 LEU   A CD1 
1154 C CD2 . LEU   A 168 ? 0.2819 0.3123 0.5072 -0.0187 0.0169  -0.0238 149 LEU   A CD2 
1155 N N   . GLY   A 169 ? 0.245  0.2857 0.5637 -0.0204 -0.0177 -0.0077 150 GLY   A N   
1156 C CA  . GLY   A 169 ? 0.2436 0.2878 0.5904 -0.0226 -0.0235 -0.0046 150 GLY   A CA  
1157 C C   . GLY   A 169 ? 0.2547 0.3069 0.6433 -0.0222 -0.0143 -0.0075 150 GLY   A C   
1158 O O   . GLY   A 169 ? 0.271  0.3253 0.678  -0.0195 -0.015  -0.0077 150 GLY   A O   
1159 N N   . ALA   A 170 ? 0.2596 0.316  0.6653 -0.0252 -0.005  -0.0097 151 ALA   A N   
1160 C CA  . ALA   A 170 ? 0.2529 0.3169 0.701  -0.0253 0.006   -0.0131 151 ALA   A CA  
1161 C C   . ALA   A 170 ? 0.2666 0.331  0.7114 -0.0251 0.0276  -0.0218 151 ALA   A C   
1162 O O   . ALA   A 170 ? 0.2729 0.3425 0.7529 -0.0248 0.0386  -0.0257 151 ALA   A O   
1163 C CB  . ALA   A 170 ? 0.2606 0.3287 0.7307 -0.0291 0.0078  -0.012  151 ALA   A CB  
1164 N N   . VAL   A 171 ? 0.2546 0.3128 0.6582 -0.0255 0.0335  -0.0251 152 VAL   A N   
1165 C CA  . VAL   A 171 ? 0.2594 0.316  0.6559 -0.0267 0.0534  -0.0334 152 VAL   A CA  
1166 C C   . VAL   A 171 ? 0.2593 0.3161 0.6659 -0.0229 0.0544  -0.0357 152 VAL   A C   
1167 O O   . VAL   A 171 ? 0.2768 0.3304 0.663  -0.0202 0.0433  -0.0326 152 VAL   A O   
1168 C CB  . VAL   A 171 ? 0.295  0.3442 0.6455 -0.0296 0.0588  -0.0356 152 VAL   A CB  
1169 C CG1 . VAL   A 171 ? 0.3115 0.3569 0.6513 -0.0319 0.0778  -0.0439 152 VAL   A CG1 
1170 C CG2 . VAL   A 171 ? 0.3064 0.3546 0.6479 -0.0336 0.0591  -0.0335 152 VAL   A CG2 
1171 N N   . PRO   A 172 ? 0.2356 0.2953 0.6714 -0.0231 0.0696  -0.0419 153 PRO   A N   
1172 C CA  . PRO   A 172 ? 0.2426 0.3019 0.6893 -0.0195 0.0715  -0.0446 153 PRO   A CA  
1173 C C   . PRO   A 172 ? 0.2736 0.3257 0.6873 -0.0214 0.0849  -0.0518 153 PRO   A C   
1174 O O   . PRO   A 172 ? 0.3019 0.35   0.698  -0.0262 0.0998  -0.0574 153 PRO   A O   
1175 C CB  . PRO   A 172 ? 0.2454 0.3106 0.7419 -0.0192 0.0829  -0.0485 153 PRO   A CB  
1176 C CG  . PRO   A 172 ? 0.2419 0.3075 0.7384 -0.0244 0.0983  -0.0528 153 PRO   A CG  
1177 C CD  . PRO   A 172 ? 0.2256 0.2891 0.6901 -0.0265 0.0855  -0.0465 153 PRO   A CD  
1178 N N   . LEU   A 173 ? 0.2578 0.3074 0.6619 -0.0181 0.0787  -0.0512 154 LEU   A N   
1179 C CA  . LEU   A 173 ? 0.2563 0.2991 0.633  -0.0198 0.0898  -0.0579 154 LEU   A CA  
1180 C C   . LEU   A 173 ? 0.2461 0.2892 0.6431 -0.0159 0.09    -0.0599 154 LEU   A C   
1181 O O   . LEU   A 173 ? 0.2587 0.3057 0.6756 -0.0116 0.0751  -0.0534 154 LEU   A O   
1182 C CB  . LEU   A 173 ? 0.2841 0.3222 0.6169 -0.02   0.0788  -0.0538 154 LEU   A CB  
1183 C CG  . LEU   A 173 ? 0.3104 0.3452 0.6128 -0.0244 0.0808  -0.0532 154 LEU   A CG  
1184 C CD1 . LEU   A 173 ? 0.3187 0.3487 0.5832 -0.0239 0.0714  -0.0502 154 LEU   A CD1 
1185 C CD2 . LEU   A 173 ? 0.3306 0.3602 0.6243 -0.0303 0.1007  -0.0613 154 LEU   A CD2 
1186 N N   . PRO   A 174 ? 0.2542 0.2916 0.6427 -0.0179 0.1055  -0.0685 155 PRO   A N   
1187 C CA  . PRO   A 174 ? 0.2579 0.2943 0.6613 -0.0143 0.1049  -0.0704 155 PRO   A CA  
1188 C C   . PRO   A 174 ? 0.2495 0.2847 0.6286 -0.0113 0.0865  -0.0632 155 PRO   A C   
1189 O O   . PRO   A 174 ? 0.2563 0.2892 0.6008 -0.0132 0.0802  -0.0601 155 PRO   A O   
1190 C CB  . PRO   A 174 ? 0.2773 0.3049 0.6609 -0.0188 0.1245  -0.0811 155 PRO   A CB  
1191 C CG  . PRO   A 174 ? 0.3025 0.3275 0.6745 -0.0248 0.1381  -0.0854 155 PRO   A CG  
1192 C CD  . PRO   A 174 ? 0.2766 0.3066 0.6382 -0.0243 0.1233  -0.0766 155 PRO   A CD  
1193 N N   . PRO   A 175 ? 0.2341 0.2702 0.6304 -0.007  0.078   -0.0604 156 PRO   A N   
1194 C CA  . PRO   A 175 ? 0.2324 0.266  0.6036 -0.005  0.0631  -0.0545 156 PRO   A CA  
1195 C C   . PRO   A 175 ? 0.2508 0.2778 0.584  -0.0083 0.0713  -0.06   156 PRO   A C   
1196 O O   . PRO   A 175 ? 0.2788 0.3014 0.6121 -0.0108 0.0864  -0.0685 156 PRO   A O   
1197 C CB  . PRO   A 175 ? 0.2361 0.2704 0.6363 -0.0009 0.0579  -0.0528 156 PRO   A CB  
1198 C CG  . PRO   A 175 ? 0.2306 0.2702 0.6781 0.0003  0.064   -0.0544 156 PRO   A CG  
1199 C CD  . PRO   A 175 ? 0.222  0.2601 0.6604 -0.0042 0.0835  -0.0633 156 PRO   A CD  
1200 N N   . ALA   A 176 ? 0.2155 0.2412 0.5163 -0.009  0.0614  -0.0551 157 ALA   A N   
1201 C CA  . ALA   A 176 ? 0.2121 0.2319 0.4783 -0.0124 0.0669  -0.059  157 ALA   A CA  
1202 C C   . ALA   A 176 ? 0.1902 0.2066 0.45   -0.011  0.0644  -0.0599 157 ALA   A C   
1203 O O   . ALA   A 176 ? 0.1947 0.2132 0.4691 -0.0069 0.0542  -0.055  157 ALA   A O   
1204 C CB  . ALA   A 176 ? 0.2234 0.2434 0.4616 -0.0134 0.0576  -0.0534 157 ALA   A CB  
1205 N N   . ASP   A 177 ? 0.2024 0.2126 0.4392 -0.0149 0.0727  -0.0657 158 ASP   A N   
1206 C CA  . ASP   A 177 ? 0.2157 0.2221 0.4417 -0.0144 0.0698  -0.0664 158 ASP   A CA  
1207 C C   . ASP   A 177 ? 0.2126 0.2203 0.4157 -0.0131 0.0558  -0.0589 158 ASP   A C   
1208 O O   . ASP   A 177 ? 0.2202 0.2271 0.4208 -0.0113 0.0496  -0.0567 158 ASP   A O   
1209 C CB  . ASP   A 177 ? 0.2662 0.2643 0.4753 -0.0201 0.0835  -0.0755 158 ASP   A CB  
1210 C CG  . ASP   A 177 ? 0.3507 0.3467 0.5837 -0.0214 0.0993  -0.0837 158 ASP   A CG  
1211 O OD1 . ASP   A 177 ? 0.3824 0.3791 0.6417 -0.0179 0.1009  -0.0854 158 ASP   A OD1 
1212 O OD2 . ASP   A 177 ? 0.3347 0.3283 0.5625 -0.0256 0.1099  -0.0878 158 ASP   A OD2 
1213 N N   . CYS   A 178 ? 0.2012 0.2102 0.3871 -0.0146 0.0523  -0.0556 159 CYS   A N   
1214 C CA  . CYS   A 178 ? 0.1966 0.2066 0.3627 -0.0135 0.041   -0.0492 159 CYS   A CA  
1215 C C   . CYS   A 178 ? 0.1968 0.2098 0.3604 -0.013  0.0363  -0.0447 159 CYS   A C   
1216 O O   . CYS   A 178 ? 0.1991 0.2117 0.3627 -0.0158 0.0433  -0.0475 159 CYS   A O   
1217 C CB  . CYS   A 178 ? 0.1862 0.1911 0.3259 -0.0177 0.0438  -0.0519 159 CYS   A CB  
1218 S SG  . CYS   A 178 ? 0.2358 0.2422 0.3548 -0.0163 0.0315  -0.0445 159 CYS   A SG  
1219 N N   . VAL   A 179 ? 0.1672 0.1822 0.3268 -0.0101 0.025   -0.038  160 VAL   A N   
1220 C CA  . VAL   A 179 ? 0.1755 0.1919 0.3277 -0.0098 0.0193  -0.0335 160 VAL   A CA  
1221 C C   . VAL   A 179 ? 0.1762 0.1909 0.3052 -0.0099 0.0143  -0.0306 160 VAL   A C   
1222 O O   . VAL   A 179 ? 0.1794 0.1935 0.3061 -0.008  0.0095  -0.0284 160 VAL   A O   
1223 C CB  . VAL   A 179 ? 0.1901 0.2088 0.3586 -0.0069 0.0107  -0.0284 160 VAL   A CB  
1224 C CG1 . VAL   A 179 ? 0.2001 0.2182 0.3551 -0.0069 0.0038  -0.0237 160 VAL   A CG1 
1225 C CG2 . VAL   A 179 ? 0.1801 0.2015 0.3748 -0.0072 0.0156  -0.0308 160 VAL   A CG2 
1226 N N   . LEU   A 180 ? 0.1788 0.1923 0.2928 -0.0122 0.0156  -0.0305 161 LEU   A N   
1227 C CA  . LEU   A 180 ? 0.1735 0.1855 0.2686 -0.0123 0.0112  -0.0277 161 LEU   A CA  
1228 C C   . LEU   A 180 ? 0.1682 0.1806 0.259  -0.0111 0.006   -0.0234 161 LEU   A C   
1229 O O   . LEU   A 180 ? 0.1812 0.1938 0.2758 -0.0123 0.008   -0.0239 161 LEU   A O   
1230 C CB  . LEU   A 180 ? 0.1859 0.1946 0.2666 -0.017  0.0168  -0.031  161 LEU   A CB  
1231 C CG  . LEU   A 180 ? 0.1946 0.2015 0.2579 -0.018  0.0121  -0.0278 161 LEU   A CG  
1232 C CD1 . LEU   A 180 ? 0.2096 0.2175 0.2713 -0.0158 0.0072  -0.0258 161 LEU   A CD1 
1233 C CD2 . LEU   A 180 ? 0.2353 0.2373 0.2843 -0.0238 0.0166  -0.0304 161 LEU   A CD2 
1234 N N   . SER   A 181 ? 0.1613 0.173  0.2439 -0.009  0.0001  -0.0197 162 SER   A N   
1235 C CA  . SER   A 181 ? 0.1572 0.1676 0.2334 -0.0082 -0.0038 -0.0164 162 SER   A CA  
1236 C C   . SER   A 181 ? 0.159  0.1681 0.2236 -0.0072 -0.0064 -0.014  162 SER   A C   
1237 O O   . SER   A 181 ? 0.1764 0.1854 0.2411 -0.0053 -0.0085 -0.0127 162 SER   A O   
1238 C CB  . SER   A 181 ? 0.1821 0.1919 0.2661 -0.0063 -0.0088 -0.0138 162 SER   A CB  
1239 O OG  . SER   A 181 ? 0.1894 0.1969 0.2671 -0.0065 -0.0116 -0.0116 162 SER   A OG  
1240 N N   . THR   A 182 ? 0.1633 0.1712 0.2192 -0.0086 -0.0062 -0.0132 163 THR   A N   
1241 C CA  . THR   A 182 ? 0.1624 0.1694 0.211  -0.0075 -0.0088 -0.0108 163 THR   A CA  
1242 C C   . THR   A 182 ? 0.1615 0.166  0.2067 -0.006  -0.0111 -0.0083 163 THR   A C   
1243 O O   . THR   A 182 ? 0.1716 0.1747 0.2149 -0.0075 -0.0107 -0.0082 163 THR   A O   
1244 C CB  . THR   A 182 ? 0.1998 0.2063 0.2415 -0.0106 -0.0081 -0.0112 163 THR   A CB  
1245 O OG1 . THR   A 182 ? 0.2001 0.2043 0.2366 -0.0139 -0.0064 -0.0117 163 THR   A OG1 
1246 C CG2 . THR   A 182 ? 0.1887 0.1959 0.2316 -0.0126 -0.0056 -0.0142 163 THR   A CG2 
1247 N N   . LEU   A 183 ? 0.1589 0.1619 0.2032 -0.0034 -0.0126 -0.0066 164 LEU   A N   
1248 C CA  . LEU   A 183 ? 0.1632 0.1624 0.2034 -0.002  -0.0138 -0.0049 164 LEU   A CA  
1249 C C   . LEU   A 183 ? 0.1597 0.1561 0.1992 -0.0028 -0.015  -0.0051 164 LEU   A C   
1250 O O   . LEU   A 183 ? 0.1793 0.1723 0.215  -0.0028 -0.0158 -0.0042 164 LEU   A O   
1251 C CB  . LEU   A 183 ? 0.1579 0.157  0.1958 -0.0023 -0.0143 -0.0033 164 LEU   A CB  
1252 C CG  . LEU   A 183 ? 0.1749 0.1761 0.2157 -0.0011 -0.0145 -0.0022 164 LEU   A CG  
1253 C CD1 . LEU   A 183 ? 0.2035 0.2051 0.2434 -0.0028 -0.0171 -0.0001 164 LEU   A CD1 
1254 C CD2 . LEU   A 183 ? 0.1906 0.1892 0.2331 0.002   -0.0129 -0.0015 164 LEU   A CD2 
1255 N N   . CYS   A 184 ? 0.1449 0.1422 0.1895 -0.0035 -0.0159 -0.0059 165 CYS   A N   
1256 C CA  . CYS   A 184 ? 0.1563 0.1514 0.2032 -0.0047 -0.0183 -0.0057 165 CYS   A CA  
1257 C C   . CYS   A 184 ? 0.1706 0.1607 0.2154 -0.0044 -0.0224 -0.0044 165 CYS   A C   
1258 O O   . CYS   A 184 ? 0.1763 0.1608 0.2158 -0.0052 -0.0252 -0.0034 165 CYS   A O   
1259 C CB  . CYS   A 184 ? 0.1665 0.1662 0.2239 -0.0065 -0.0166 -0.0074 165 CYS   A CB  
1260 S SG  . CYS   A 184 ? 0.1958 0.1945 0.2628 -0.008  -0.0203 -0.0067 165 CYS   A SG  
1261 N N   . LEU   A 185 ? 0.1597 0.1503 0.2074 -0.0039 -0.0233 -0.0041 166 LEU   A N   
1262 C CA  . LEU   A 185 ? 0.1849 0.1695 0.23   -0.0049 -0.0286 -0.0021 166 LEU   A CA  
1263 C C   . LEU   A 185 ? 0.1909 0.1667 0.2211 -0.0052 -0.0291 -0.0012 166 LEU   A C   
1264 O O   . LEU   A 185 ? 0.2095 0.1779 0.2338 -0.0074 -0.0343 0.0002  166 LEU   A O   
1265 C CB  . LEU   A 185 ? 0.1971 0.1836 0.2491 -0.0046 -0.0298 -0.0015 166 LEU   A CB  
1266 C CG  . LEU   A 185 ? 0.2101 0.2039 0.2785 -0.0044 -0.0286 -0.003  166 LEU   A CG  
1267 C CD1 . LEU   A 185 ? 0.211  0.205  0.2859 -0.004  -0.0302 -0.0021 166 LEU   A CD1 
1268 C CD2 . LEU   A 185 ? 0.2274 0.2217 0.3065 -0.006  -0.0324 -0.0023 166 LEU   A CD2 
1269 N N   . ASP   A 186 ? 0.2042 0.1796 0.2283 -0.0035 -0.024  -0.0021 167 ASP   A N   
1270 C CA  . ASP   A 186 ? 0.2056 0.1713 0.216  -0.004  -0.0225 -0.0021 167 ASP   A CA  
1271 C C   . ASP   A 186 ? 0.2128 0.174  0.2187 -0.005  -0.0239 -0.0026 167 ASP   A C   
1272 O O   . ASP   A 186 ? 0.2481 0.1987 0.2417 -0.007  -0.0251 -0.0027 167 ASP   A O   
1273 C CB  . ASP   A 186 ? 0.2577 0.2254 0.268  -0.0016 -0.0159 -0.0032 167 ASP   A CB  
1274 C CG  . ASP   A 186 ? 0.3191 0.2896 0.332  -0.0007 -0.0129 -0.0029 167 ASP   A CG  
1275 O OD1 . ASP   A 186 ? 0.337  0.3053 0.3481 -0.0021 -0.0154 -0.0019 167 ASP   A OD1 
1276 O OD2 . ASP   A 186 ? 0.3077 0.2816 0.3248 0.0014  -0.0082 -0.0035 167 ASP   A OD2 
1277 N N   . ALA   A 187 ? 0.1972 0.165  0.2114 -0.0042 -0.0235 -0.003  168 ALA   A N   
1278 C CA  . ALA   A 187 ? 0.2047 0.1684 0.2157 -0.0052 -0.0249 -0.0033 168 ALA   A CA  
1279 C C   . ALA   A 187 ? 0.215  0.1758 0.2272 -0.0083 -0.0315 -0.0022 168 ALA   A C   
1280 O O   . ALA   A 187 ? 0.2227 0.1764 0.2285 -0.0102 -0.0343 -0.0022 168 ALA   A O   
1281 C CB  . ALA   A 187 ? 0.1976 0.1687 0.2164 -0.0042 -0.0227 -0.0034 168 ALA   A CB  
1282 N N   . ALA   A 188 ? 0.1975 0.1643 0.2206 -0.0088 -0.0344 -0.0013 169 ALA   A N   
1283 C CA  . ALA   A 188 ? 0.2231 0.1893 0.2536 -0.0114 -0.0411 0.0002  169 ALA   A CA  
1284 C C   . ALA   A 188 ? 0.2282 0.1852 0.251  -0.0141 -0.0484 0.0024  169 ALA   A C   
1285 O O   . ALA   A 188 ? 0.2587 0.2132 0.2866 -0.0169 -0.0559 0.0042  169 ALA   A O   
1286 C CB  . ALA   A 188 ? 0.2186 0.1952 0.2674 -0.0107 -0.0399 -0.0001 169 ALA   A CB  
1287 N N   . CYS   A 189 ? 0.2206 0.1725 0.2328 -0.0139 -0.0474 0.0027  170 CYS   A N   
1288 C CA  . CYS   A 189 ? 0.2376 0.18   0.2414 -0.0173 -0.0551 0.0055  170 CYS   A CA  
1289 C C   . CYS   A 189 ? 0.2604 0.1883 0.2405 -0.0199 -0.0542 0.0049  170 CYS   A C   
1290 O O   . CYS   A 189 ? 0.2705 0.1967 0.2421 -0.0181 -0.0462 0.0029  170 CYS   A O   
1291 C CB  . CYS   A 189 ? 0.2417 0.1882 0.2516 -0.0159 -0.0545 0.0068  170 CYS   A CB  
1292 S SG  . CYS   A 189 ? 0.2349 0.1967 0.2729 -0.0132 -0.0541 0.0066  170 CYS   A SG  
1293 N N   . PRO   A 190 ? 0.2936 0.2099 0.2626 -0.0246 -0.0619 0.0063  171 PRO   A N   
1294 C CA  . PRO   A 190 ? 0.3237 0.2239 0.2672 -0.0278 -0.0593 0.0045  171 PRO   A CA  
1295 C C   . PRO   A 190 ? 0.3577 0.2465 0.283  -0.0309 -0.059  0.0056  171 PRO   A C   
1296 O O   . PRO   A 190 ? 0.3897 0.2662 0.2947 -0.0328 -0.0523 0.0029  171 PRO   A O   
1297 C CB  . PRO   A 190 ? 0.3484 0.2395 0.286  -0.0327 -0.0689 0.0058  171 PRO   A CB  
1298 C CG  . PRO   A 190 ? 0.3538 0.2592 0.3169 -0.0305 -0.0729 0.0071  171 PRO   A CG  
1299 C CD  . PRO   A 190 ? 0.3104 0.2281 0.2908 -0.0271 -0.0719 0.0088  171 PRO   A CD  
1300 N N   . ASP   A 191 ? 0.3348 0.2268 0.2675 -0.0316 -0.065  0.0094  172 ASP   A N   
1301 C CA  . ASP   A 191 ? 0.3508 0.2313 0.2658 -0.0351 -0.0653 0.0112  172 ASP   A CA  
1302 C C   . ASP   A 191 ? 0.3356 0.2265 0.2674 -0.0326 -0.0675 0.0141  172 ASP   A C   
1303 O O   . ASP   A 191 ? 0.3137 0.2192 0.2701 -0.0288 -0.0695 0.0146  172 ASP   A O   
1304 C CB  . ASP   A 191 ? 0.411  0.2723 0.3039 -0.0433 -0.0767 0.0144  172 ASP   A CB  
1305 C CG  . ASP   A 191 ? 0.4706 0.3355 0.3793 -0.0452 -0.0916 0.0189  172 ASP   A CG  
1306 O OD1 . ASP   A 191 ? 0.424  0.3026 0.3575 -0.0417 -0.0949 0.0213  172 ASP   A OD1 
1307 O OD2 . ASP   A 191 ? 0.5373 0.3912 0.4348 -0.0504 -0.0996 0.0198  172 ASP   A OD2 
1308 N N   . LEU   A 192 ? 0.3506 0.2333 0.2689 -0.035  -0.0658 0.0157  173 LEU   A N   
1309 C CA  . LEU   A 192 ? 0.3519 0.2428 0.2844 -0.0328 -0.0669 0.0183  173 LEU   A CA  
1310 C C   . LEU   A 192 ? 0.3543 0.2481 0.3032 -0.0342 -0.0811 0.0236  173 LEU   A C   
1311 O O   . LEU   A 192 ? 0.3232 0.2312 0.2966 -0.0297 -0.0804 0.0236  173 LEU   A O   
1312 C CB  . LEU   A 192 ? 0.3823 0.262  0.295  -0.0359 -0.0619 0.0191  173 LEU   A CB  
1313 C CG  . LEU   A 192 ? 0.3905 0.2783 0.3169 -0.0335 -0.0613 0.0213  173 LEU   A CG  
1314 C CD1 . LEU   A 192 ? 0.3689 0.2759 0.3192 -0.0262 -0.0528 0.0174  173 LEU   A CD1 
1315 C CD2 . LEU   A 192 ? 0.44   0.3155 0.3452 -0.0374 -0.0553 0.0221  173 LEU   A CD2 
1316 N N   . PRO   A 193 ? 0.3778 0.2588 0.3161 -0.0403 -0.0938 0.0277  174 PRO   A N   
1317 C CA  . PRO   A 193 ? 0.3634 0.2491 0.3237 -0.0409 -0.1074 0.0329  174 PRO   A CA  
1318 C C   . PRO   A 193 ? 0.3258 0.2292 0.3158 -0.0354 -0.1052 0.0302  174 PRO   A C   
1319 O O   . PRO   A 193 ? 0.3165 0.2305 0.3324 -0.0325 -0.1079 0.0318  174 PRO   A O   
1320 C CB  . PRO   A 193 ? 0.4039 0.2709 0.344  -0.0492 -0.1216 0.0378  174 PRO   A CB  
1321 C CG  . PRO   A 193 ? 0.4357 0.2856 0.3394 -0.0539 -0.1149 0.036   174 PRO   A CG  
1322 C CD  . PRO   A 193 ? 0.3981 0.2588 0.3047 -0.0475 -0.0973 0.0283  174 PRO   A CD  
1323 N N   . THR   A 194 ? 0.3069 0.2128 0.2932 -0.0341 -0.0989 0.0258  175 THR   A N   
1324 C CA  . THR   A 194 ? 0.2797 0.2013 0.2918 -0.0296 -0.0955 0.0232  175 THR   A CA  
1325 C C   . THR   A 194 ? 0.2617 0.1973 0.2883 -0.0237 -0.0841 0.0197  175 THR   A C   
1326 O O   . THR   A 194 ? 0.2543 0.2019 0.3055 -0.0208 -0.0831 0.0189  175 THR   A O   
1327 C CB  . THR   A 194 ? 0.3108 0.2307 0.3138 -0.0299 -0.0913 0.0197  175 THR   A CB  
1328 O OG1 . THR   A 194 ? 0.3467 0.2525 0.3359 -0.0362 -0.1028 0.0228  175 THR   A OG1 
1329 C CG2 . THR   A 194 ? 0.3046 0.2392 0.3319 -0.0262 -0.0873 0.0173  175 THR   A CG2 
1330 N N   . TYR   A 195 ? 0.2509 0.1844 0.2626 -0.0223 -0.0752 0.0173  176 TYR   A N   
1331 C CA  . TYR   A 195 ? 0.2215 0.1669 0.245  -0.0175 -0.0657 0.0144  176 TYR   A CA  
1332 C C   . TYR   A 195 ? 0.223  0.1729 0.2642 -0.0167 -0.0702 0.017   176 TYR   A C   
1333 O O   . TYR   A 195 ? 0.2185 0.1801 0.2801 -0.0134 -0.0661 0.0147  176 TYR   A O   
1334 C CB  . TYR   A 195 ? 0.227  0.1672 0.2315 -0.0171 -0.0574 0.0125  176 TYR   A CB  
1335 C CG  . TYR   A 195 ? 0.2179 0.1695 0.2327 -0.0127 -0.0481 0.0094  176 TYR   A CG  
1336 C CD1 . TYR   A 195 ? 0.2306 0.1899 0.2498 -0.0099 -0.0413 0.0059  176 TYR   A CD1 
1337 C CD2 . TYR   A 195 ? 0.2257 0.1794 0.2454 -0.012  -0.0471 0.0105  176 TYR   A CD2 
1338 C CE1 . TYR   A 195 ? 0.2386 0.2067 0.2654 -0.0068 -0.0343 0.0035  176 TYR   A CE1 
1339 C CE2 . TYR   A 195 ? 0.2191 0.1823 0.2472 -0.0087 -0.0395 0.0077  176 TYR   A CE2 
1340 C CZ  . TYR   A 195 ? 0.2288 0.199  0.2602 -0.0063 -0.0335 0.0043  176 TYR   A CZ  
1341 O OH  . TYR   A 195 ? 0.2383 0.2162 0.276  -0.004  -0.0274 0.0021  176 TYR   A OH  
1342 N N   . CYS   A 196 ? 0.248  0.1876 0.281  -0.0203 -0.0787 0.0218  177 CYS   A N   
1343 C CA  . CYS   A 196 ? 0.2462 0.1893 0.2973 -0.0196 -0.0839 0.0248  177 CYS   A CA  
1344 C C   . CYS   A 196 ? 0.2438 0.1943 0.3222 -0.0187 -0.0901 0.0259  177 CYS   A C   
1345 O O   . CYS   A 196 ? 0.231  0.1917 0.3333 -0.0154 -0.0869 0.0243  177 CYS   A O   
1346 C CB  . CYS   A 196 ? 0.2684 0.1974 0.304  -0.0243 -0.0928 0.0306  177 CYS   A CB  
1347 S SG  . CYS   A 196 ? 0.3323 0.2643 0.3913 -0.0234 -0.1    0.0352  177 CYS   A SG  
1348 N N   . ARG   A 197 ? 0.2517 0.1975 0.328  -0.0217 -0.0979 0.0279  178 ARG   A N   
1349 C CA  . ARG   A 197 ? 0.2417 0.1954 0.3465 -0.021  -0.1028 0.0288  178 ARG   A CA  
1350 C C   . ARG   A 197 ? 0.2149 0.1827 0.3356 -0.0164 -0.0899 0.0224  178 ARG   A C   
1351 O O   . ARG   A 197 ? 0.2082 0.185  0.3564 -0.0143 -0.0884 0.0214  178 ARG   A O   
1352 C CB  . ARG   A 197 ? 0.2939 0.2401 0.3927 -0.0254 -0.1131 0.0318  178 ARG   A CB  
1353 C CG  . ARG   A 197 ? 0.4193 0.3505 0.5049 -0.0312 -0.1285 0.0389  178 ARG   A CG  
1354 C CD  . ARG   A 197 ? 0.4726 0.3989 0.5631 -0.0356 -0.1409 0.0424  178 ARG   A CD  
1355 N NE  . ARG   A 197 ? 0.5197 0.4452 0.5952 -0.036  -0.1344 0.0379  178 ARG   A NE  
1356 C CZ  . ARG   A 197 ? 0.5628 0.4743 0.6048 -0.04   -0.1346 0.0372  178 ARG   A CZ  
1357 N NH1 . ARG   A 197 ? 0.5797 0.4909 0.6121 -0.04   -0.1287 0.0331  178 ARG   A NH1 
1358 N NH2 . ARG   A 197 ? 0.5861 0.4826 0.6038 -0.0445 -0.1404 0.0407  178 ARG   A NH2 
1359 N N   . ALA   A 198 ? 0.1928 0.1619 0.2965 -0.0153 -0.0801 0.0179  179 ALA   A N   
1360 C CA  . ALA   A 198 ? 0.1868 0.167  0.3017 -0.0121 -0.0688 0.0124  179 ALA   A CA  
1361 C C   . ALA   A 198 ? 0.1974 0.1846 0.3245 -0.0092 -0.0619 0.0099  179 ALA   A C   
1362 O O   . ALA   A 198 ? 0.187  0.1825 0.3328 -0.0077 -0.0558 0.0066  179 ALA   A O   
1363 C CB  . ALA   A 198 ? 0.2056 0.1843 0.2992 -0.0117 -0.0615 0.0093  179 ALA   A CB  
1364 N N   . LEU   A 199 ? 0.1858 0.1687 0.3025 -0.0089 -0.0626 0.0114  180 LEU   A N   
1365 C CA  . LEU   A 199 ? 0.1853 0.1737 0.3135 -0.0066 -0.0569 0.0091  180 LEU   A CA  
1366 C C   . LEU   A 199 ? 0.1954 0.1871 0.3518 -0.0061 -0.0615 0.0106  180 LEU   A C   
1367 O O   . LEU   A 199 ? 0.1935 0.1924 0.3671 -0.0041 -0.0538 0.0065  180 LEU   A O   
1368 C CB  . LEU   A 199 ? 0.1976 0.1799 0.3094 -0.0069 -0.0576 0.011   180 LEU   A CB  
1369 C CG  . LEU   A 199 ? 0.2107 0.1921 0.3014 -0.0065 -0.0503 0.0084  180 LEU   A CG  
1370 C CD1 . LEU   A 199 ? 0.2395 0.2139 0.3152 -0.0075 -0.0511 0.0108  180 LEU   A CD1 
1371 C CD2 . LEU   A 199 ? 0.2229 0.2133 0.3196 -0.0041 -0.0404 0.0031  180 LEU   A CD2 
1372 N N   . ARG   A 200 ? 0.1925 0.1782 0.354  -0.0084 -0.0739 0.0165  181 ARG   A N   
1373 C CA  . ARG   A 200 ? 0.2001 0.1892 0.393  -0.0078 -0.0796 0.0188  181 ARG   A CA  
1374 C C   . ARG   A 200 ? 0.2073 0.2054 0.421  -0.0068 -0.0733 0.0147  181 ARG   A C   
1375 O O   . ARG   A 200 ? 0.2081 0.2129 0.4489 -0.0048 -0.0681 0.012   181 ARG   A O   
1376 C CB  . ARG   A 200 ? 0.2206 0.2007 0.4143 -0.0113 -0.0962 0.0269  181 ARG   A CB  
1377 C CG  . ARG   A 200 ? 0.2641 0.2329 0.4364 -0.0136 -0.1034 0.0318  181 ARG   A CG  
1378 C CD  . ARG   A 200 ? 0.3025 0.2621 0.4804 -0.0177 -0.1211 0.0403  181 ARG   A CD  
1379 N NE  . ARG   A 200 ? 0.3416 0.2867 0.4887 -0.0221 -0.1285 0.0452  181 ARG   A NE  
1380 C CZ  . ARG   A 200 ? 0.33   0.2683 0.4755 -0.0234 -0.1344 0.05    181 ARG   A CZ  
1381 N NH1 . ARG   A 200 ? 0.2693 0.2149 0.4436 -0.0198 -0.1334 0.05    181 ARG   A NH1 
1382 N NH2 . ARG   A 200 ? 0.3665 0.2897 0.4813 -0.0286 -0.1409 0.0546  181 ARG   A NH2 
1383 N N   . ASN   A 201 ? 0.1892 0.1868 0.3904 -0.0084 -0.0727 0.0139  182 ASN   A N   
1384 C CA  . ASN   A 201 ? 0.1854 0.1905 0.4047 -0.0082 -0.0666 0.0105  182 ASN   A CA  
1385 C C   . ASN   A 201 ? 0.1937 0.2059 0.4159 -0.0061 -0.0507 0.0031  182 ASN   A C   
1386 O O   . ASN   A 201 ? 0.2035 0.222  0.4499 -0.0056 -0.044  -0.0001 182 ASN   A O   
1387 C CB  . ASN   A 201 ? 0.1994 0.2012 0.4023 -0.0107 -0.0696 0.0114  182 ASN   A CB  
1388 C CG  . ASN   A 201 ? 0.2251 0.218  0.423  -0.014  -0.0854 0.0182  182 ASN   A CG  
1389 O OD1 . ASN   A 201 ? 0.2335 0.2247 0.4491 -0.0148 -0.0958 0.0231  182 ASN   A OD1 
1390 N ND2 . ASN   A 201 ? 0.2331 0.2194 0.4074 -0.0164 -0.0882 0.019   182 ASN   A ND2 
1391 N N   . LEU   A 202 ? 0.1788 0.1894 0.3771 -0.0054 -0.0445 0.0004  183 LEU   A N   
1392 C CA  . LEU   A 202 ? 0.1891 0.2044 0.3876 -0.0044 -0.0312 -0.006  183 LEU   A CA  
1393 C C   . LEU   A 202 ? 0.1865 0.2043 0.4072 -0.0028 -0.0282 -0.0078 183 LEU   A C   
1394 O O   . LEU   A 202 ? 0.1841 0.2059 0.4166 -0.0027 -0.0174 -0.0134 183 LEU   A O   
1395 C CB  . LEU   A 202 ? 0.1998 0.2124 0.3706 -0.0041 -0.0278 -0.0072 183 LEU   A CB  
1396 C CG  . LEU   A 202 ? 0.2293 0.2416 0.3814 -0.0053 -0.0241 -0.0087 183 LEU   A CG  
1397 C CD1 . LEU   A 202 ? 0.2733 0.2829 0.4238 -0.0066 -0.0311 -0.0052 183 LEU   A CD1 
1398 C CD2 . LEU   A 202 ? 0.2311 0.2407 0.3613 -0.0046 -0.0227 -0.0088 183 LEU   A CD2 
1399 N N   . GLY   A 203 ? 0.1786 0.1927 0.4032 -0.002  -0.0375 -0.0031 184 GLY   A N   
1400 C CA  . GLY   A 203 ? 0.1734 0.1889 0.42   -0.0003 -0.036  -0.0041 184 GLY   A CA  
1401 C C   . GLY   A 203 ? 0.1812 0.2017 0.4623 0.0002  -0.0341 -0.0053 184 GLY   A C   
1402 O O   . GLY   A 203 ? 0.1871 0.2103 0.4875 0.0016  -0.0256 -0.0099 184 GLY   A O   
1403 N N   . SER   A 204 ? 0.1912 0.2127 0.4809 -0.0011 -0.0407 -0.0019 185 SER   A N   
1404 C CA  . SER   A 204 ? 0.1789 0.206  0.5058 -0.0007 -0.0385 -0.0029 185 SER   A CA  
1405 C C   . SER   A 204 ? 0.1913 0.2236 0.5239 -0.0009 -0.0197 -0.0121 185 SER   A C   
1406 O O   . SER   A 204 ? 0.2081 0.245  0.5723 -0.0004 -0.0132 -0.015  185 SER   A O   
1407 C CB  . SER   A 204 ? 0.1653 0.1922 0.4981 -0.0028 -0.0495 0.0025  185 SER   A CB  
1408 O OG  . SER   A 204 ? 0.1996 0.228  0.5155 -0.0046 -0.0424 -0.0007 185 SER   A OG  
1409 N N   . LEU   A 205 ? 0.1757 0.2065 0.4787 -0.0021 -0.0112 -0.0164 186 LEU   A N   
1410 C CA  . LEU   A 205 ? 0.1684 0.2015 0.4699 -0.0037 0.0058  -0.0246 186 LEU   A CA  
1411 C C   . LEU   A 205 ? 0.1931 0.2244 0.4925 -0.0031 0.0159  -0.0306 186 LEU   A C   
1412 O O   . LEU   A 205 ? 0.2129 0.2439 0.5083 -0.0053 0.0302  -0.0378 186 LEU   A O   
1413 C CB  . LEU   A 205 ? 0.1804 0.2114 0.4485 -0.006  0.0082  -0.0253 186 LEU   A CB  
1414 C CG  . LEU   A 205 ? 0.2149 0.2462 0.4803 -0.0071 -0.0007 -0.0203 186 LEU   A CG  
1415 C CD1 . LEU   A 205 ? 0.2363 0.2648 0.4696 -0.0089 0.0014  -0.0208 186 LEU   A CD1 
1416 C CD2 . LEU   A 205 ? 0.2168 0.2528 0.5106 -0.0084 0.0038  -0.0216 186 LEU   A CD2 
1417 N N   . LEU   A 206 ? 0.183  0.2119 0.4806 -0.0009 0.0084  -0.0276 187 LEU   A N   
1418 C CA  . LEU   A 206 ? 0.1921 0.2182 0.482  -0.0006 0.0152  -0.0321 187 LEU   A CA  
1419 C C   . LEU   A 206 ? 0.2055 0.2322 0.5283 0.0018  0.0163  -0.0332 187 LEU   A C   
1420 O O   . LEU   A 206 ? 0.2183 0.2458 0.5605 0.0038  0.0043  -0.0266 187 LEU   A O   
1421 C CB  . LEU   A 206 ? 0.2175 0.2401 0.4823 0.0001  0.0046  -0.0268 187 LEU   A CB  
1422 C CG  . LEU   A 206 ? 0.2814 0.3014 0.5161 -0.0014 0.0091  -0.0296 187 LEU   A CG  
1423 C CD1 . LEU   A 206 ? 0.2427 0.2597 0.4631 -0.0001 -0.0011 -0.024  187 LEU   A CD1 
1424 C CD2 . LEU   A 206 ? 0.2535 0.2721 0.4863 -0.0033 0.0227  -0.038  187 LEU   A CD2 
1425 N N   . LYS   A 207 ? 0.1972 0.2223 0.5233 0.0011  0.0294  -0.0409 188 LYS   A N   
1426 C CA  . LYS   A 207 ? 0.208  0.2327 0.5653 0.0035  0.0324  -0.0431 188 LYS   A CA  
1427 C C   . LYS   A 207 ? 0.2148 0.2364 0.5669 0.0057  0.0195  -0.0368 188 LYS   A C   
1428 O O   . LYS   A 207 ? 0.2114 0.2303 0.5329 0.0046  0.0152  -0.0348 188 LYS   A O   
1429 C CB  . LYS   A 207 ? 0.2289 0.2502 0.584  0.0013  0.051   -0.0541 188 LYS   A CB  
1430 C CG  . LYS   A 207 ? 0.2544 0.2703 0.5773 -0.0006 0.0526  -0.0566 188 LYS   A CG  
1431 C CD  . LYS   A 207 ? 0.2792 0.2897 0.5985 -0.0038 0.0702  -0.0676 188 LYS   A CD  
1432 C CE  . LYS   A 207 ? 0.3397 0.3447 0.6334 -0.0053 0.0687  -0.069  188 LYS   A CE  
1433 N NZ  . LYS   A 207 ? 0.4008 0.3982 0.6825 -0.0101 0.0849  -0.0797 188 LYS   A NZ  
1434 N N   . PRO   A 208 ? 0.2358 0.2571 0.6188 0.0085  0.0144  -0.0341 189 PRO   A N   
1435 C CA  . PRO   A 208 ? 0.2374 0.2542 0.6135 0.0098  0.0035  -0.0285 189 PRO   A CA  
1436 C C   . PRO   A 208 ? 0.2268 0.2398 0.578  0.0083  0.0127  -0.0348 189 PRO   A C   
1437 O O   . PRO   A 208 ? 0.2201 0.2322 0.5747 0.0071  0.0278  -0.0443 189 PRO   A O   
1438 C CB  . PRO   A 208 ? 0.2423 0.2591 0.6602 0.0127  0.001   -0.0271 189 PRO   A CB  
1439 C CG  . PRO   A 208 ? 0.2581 0.2802 0.7057 0.0132  0.007   -0.0297 189 PRO   A CG  
1440 C CD  . PRO   A 208 ? 0.2436 0.2682 0.6697 0.0103  0.0186  -0.0359 189 PRO   A CD  
1441 N N   . GLY   A 209 ? 0.2352 0.2453 0.5604 0.0077  0.0044  -0.0301 190 GLY   A N   
1442 C CA  . GLY   A 209 ? 0.2286 0.2355 0.531  0.006   0.0113  -0.0351 190 GLY   A CA  
1443 C C   . GLY   A 209 ? 0.2166 0.2244 0.4917 0.0029  0.0192  -0.04   190 GLY   A C   
1444 O O   . GLY   A 209 ? 0.2216 0.2266 0.4777 0.0008  0.0241  -0.044  190 GLY   A O   
1445 N N   . GLY   A 210 ? 0.1935 0.2049 0.468  0.0023  0.02    -0.0396 191 GLY   A N   
1446 C CA  . GLY   A 210 ? 0.2084 0.22   0.4582 -0.0008 0.0265  -0.0432 191 GLY   A CA  
1447 C C   . GLY   A 210 ? 0.197  0.208  0.4184 -0.0014 0.0184  -0.0383 191 GLY   A C   
1448 O O   . GLY   A 210 ? 0.1968 0.2073 0.4168 0.0004  0.0078  -0.0315 191 GLY   A O   
1449 N N   . PHE   A 211 ? 0.1802 0.1903 0.3795 -0.0043 0.0236  -0.0415 192 PHE   A N   
1450 C CA  . PHE   A 211 ? 0.1874 0.1972 0.3624 -0.0049 0.0171  -0.0374 192 PHE   A CA  
1451 C C   . PHE   A 211 ? 0.1786 0.1906 0.3443 -0.0046 0.0121  -0.033  192 PHE   A C   
1452 O O   . PHE   A 211 ? 0.1986 0.2119 0.3659 -0.0058 0.0164  -0.035  192 PHE   A O   
1453 C CB  . PHE   A 211 ? 0.2085 0.2154 0.3644 -0.0085 0.0233  -0.0424 192 PHE   A CB  
1454 C CG  . PHE   A 211 ? 0.2468 0.2502 0.4061 -0.0093 0.0263  -0.046  192 PHE   A CG  
1455 C CD1 . PHE   A 211 ? 0.2683 0.2712 0.4215 -0.0083 0.0198  -0.0422 192 PHE   A CD1 
1456 C CD2 . PHE   A 211 ? 0.2848 0.2846 0.4527 -0.0114 0.0366  -0.0536 192 PHE   A CD2 
1457 C CE1 . PHE   A 211 ? 0.2977 0.297  0.454  -0.0093 0.0224  -0.0455 192 PHE   A CE1 
1458 C CE2 . PHE   A 211 ? 0.2993 0.2947 0.4689 -0.0125 0.0396  -0.0575 192 PHE   A CE2 
1459 C CZ  . PHE   A 211 ? 0.3001 0.2956 0.464  -0.0115 0.0319  -0.0532 192 PHE   A CZ  
1460 N N   . LEU   A 212 ? 0.1619 0.1735 0.3174 -0.0032 0.0036  -0.0271 193 LEU   A N   
1461 C CA  . LEU   A 212 ? 0.1584 0.1707 0.3018 -0.003  -0.0012 -0.023  193 LEU   A CA  
1462 C C   . LEU   A 212 ? 0.1561 0.1677 0.2795 -0.004  -0.0012 -0.0226 193 LEU   A C   
1463 O O   . LEU   A 212 ? 0.1577 0.1681 0.2776 -0.0035 -0.0034 -0.0211 193 LEU   A O   
1464 C CB  . LEU   A 212 ? 0.1636 0.1742 0.3107 -0.0012 -0.0106 -0.0167 193 LEU   A CB  
1465 C CG  . LEU   A 212 ? 0.1997 0.2092 0.3342 -0.0014 -0.0152 -0.0131 193 LEU   A CG  
1466 C CD1 . LEU   A 212 ? 0.2245 0.2362 0.3686 -0.002  -0.014  -0.0142 193 LEU   A CD1 
1467 C CD2 . LEU   A 212 ? 0.2137 0.2184 0.3438 -0.001  -0.024  -0.0071 193 LEU   A CD2 
1468 N N   . VAL   A 213 ? 0.1516 0.1638 0.2636 -0.0056 0.0011  -0.0237 194 VAL   A N   
1469 C CA  . VAL   A 213 ? 0.1567 0.1685 0.2529 -0.0065 0.0002  -0.0227 194 VAL   A CA  
1470 C C   . VAL   A 213 ? 0.1587 0.1704 0.2469 -0.0055 -0.0035 -0.0189 194 VAL   A C   
1471 O O   . VAL   A 213 ? 0.16   0.172  0.2479 -0.0064 -0.002  -0.0197 194 VAL   A O   
1472 C CB  . VAL   A 213 ? 0.1681 0.1787 0.2565 -0.0101 0.0056  -0.027  194 VAL   A CB  
1473 C CG1 . VAL   A 213 ? 0.1929 0.2032 0.2678 -0.0112 0.0026  -0.0249 194 VAL   A CG1 
1474 C CG2 . VAL   A 213 ? 0.1996 0.2085 0.2947 -0.0117 0.0106  -0.0319 194 VAL   A CG2 
1475 N N   . ILE   A 214 ? 0.1528 0.1636 0.2353 -0.0039 -0.0074 -0.0152 195 ILE   A N   
1476 C CA  . ILE   A 214 ? 0.148  0.1574 0.2229 -0.003  -0.0101 -0.0123 195 ILE   A CA  
1477 C C   . ILE   A 214 ? 0.1567 0.1663 0.2235 -0.0027 -0.01   -0.011  195 ILE   A C   
1478 O O   . ILE   A 214 ? 0.1532 0.1632 0.2208 -0.0023 -0.0099 -0.0105 195 ILE   A O   
1479 C CB  . ILE   A 214 ? 0.1673 0.1733 0.2431 -0.0017 -0.0143 -0.0091 195 ILE   A CB  
1480 C CG1 . ILE   A 214 ? 0.2044 0.2102 0.2925 -0.0019 -0.0165 -0.0091 195 ILE   A CG1 
1481 C CG2 . ILE   A 214 ? 0.1911 0.1939 0.2572 -0.0013 -0.0161 -0.0069 195 ILE   A CG2 
1482 C CD1 . ILE   A 214 ? 0.2318 0.2393 0.326  -0.0027 -0.0157 -0.0105 195 ILE   A CD1 
1483 N N   . MET   A 215 ? 0.1441 0.1535 0.2048 -0.0029 -0.0101 -0.0102 196 MET   A N   
1484 C CA  . MET   A 215 ? 0.1462 0.1558 0.2026 -0.0021 -0.0106 -0.0084 196 MET   A CA  
1485 C C   . MET   A 215 ? 0.1592 0.1659 0.2112 -0.0008 -0.0113 -0.0066 196 MET   A C   
1486 O O   . MET   A 215 ? 0.1709 0.1768 0.2214 -0.0016 -0.0118 -0.0071 196 MET   A O   
1487 C CB  . MET   A 215 ? 0.1842 0.1954 0.2383 -0.0044 -0.0108 -0.009  196 MET   A CB  
1488 C CG  . MET   A 215 ? 0.208  0.2203 0.2642 -0.0066 -0.0097 -0.0116 196 MET   A CG  
1489 S SD  . MET   A 215 ? 0.2684 0.2796 0.3171 -0.0112 -0.011  -0.0125 196 MET   A SD  
1490 C CE  . MET   A 215 ? 0.2869 0.2973 0.3376 -0.0138 -0.0081 -0.0169 196 MET   A CE  
1491 N N   . ASP   A 216 ? 0.146  0.1504 0.1962 0.0009  -0.0107 -0.0049 197 ASP   A N   
1492 C CA  . ASP   A 216 ? 0.1527 0.1525 0.1976 0.0019  -0.0105 -0.004  197 ASP   A CA  
1493 C C   . ASP   A 216 ? 0.1543 0.1518 0.1986 0.0035  -0.0075 -0.003  197 ASP   A C   
1494 O O   . ASP   A 216 ? 0.159  0.1589 0.2079 0.0038  -0.0059 -0.0027 197 ASP   A O   
1495 C CB  . ASP   A 216 ? 0.1716 0.1669 0.2127 0.0012  -0.0123 -0.004  197 ASP   A CB  
1496 C CG  . ASP   A 216 ? 0.2031 0.1948 0.2398 0.0007  -0.0138 -0.004  197 ASP   A CG  
1497 O OD1 . ASP   A 216 ? 0.194  0.1845 0.2283 0.0015  -0.0125 -0.0037 197 ASP   A OD1 
1498 O OD2 . ASP   A 216 ? 0.2342 0.2238 0.2711 -0.0005 -0.0169 -0.0038 197 ASP   A OD2 
1499 N N   . ALA   A 217 ? 0.17   0.1627 0.2098 0.0043  -0.0062 -0.0029 198 ALA   A N   
1500 C CA  . ALA   A 217 ? 0.1616 0.1509 0.2019 0.0058  -0.0016 -0.0027 198 ALA   A CA  
1501 C C   . ALA   A 217 ? 0.1873 0.17   0.22   0.0048  0.0017  -0.0031 198 ALA   A C   
1502 O O   . ALA   A 217 ? 0.225  0.203  0.2492 0.0029  -0.0011 -0.0031 198 ALA   A O   
1503 C CB  . ALA   A 217 ? 0.1844 0.1691 0.2218 0.0067  -0.0005 -0.003  198 ALA   A CB  
1504 N N   . LEU   A 218 ? 0.1842 0.1661 0.2205 0.0057  0.0075  -0.0032 199 LEU   A N   
1505 C CA  . LEU   A 218 ? 0.2028 0.1761 0.229  0.0039  0.0121  -0.0037 199 LEU   A CA  
1506 C C   . LEU   A 218 ? 0.2111 0.1755 0.2309 0.0041  0.019   -0.0055 199 LEU   A C   
1507 O O   . LEU   A 218 ? 0.2014 0.1689 0.2318 0.0067  0.0223  -0.006  199 LEU   A O   
1508 C CB  . LEU   A 218 ? 0.1962 0.1737 0.231  0.0041  0.016   -0.003  199 LEU   A CB  
1509 C CG  . LEU   A 218 ? 0.2003 0.184  0.2393 0.0033  0.0104  -0.0017 199 LEU   A CG  
1510 C CD1 . LEU   A 218 ? 0.1941 0.1836 0.2453 0.0038  0.0138  -0.0011 199 LEU   A CD1 
1511 C CD2 . LEU   A 218 ? 0.2213 0.1978 0.2482 0.0006  0.0078  -0.001  199 LEU   A CD2 
1512 N N   . LYS   A 219 ? 0.2219 0.1742 0.224  0.001   0.0203  -0.0063 200 LYS   A N   
1513 C CA  . LYS   A 219 ? 0.2448 0.1849 0.2357 -0.0002 0.0284  -0.0089 200 LYS   A CA  
1514 C C   . LYS   A 219 ? 0.2652 0.2048 0.26   0.002   0.029   -0.0105 200 LYS   A C   
1515 O O   . LYS   A 219 ? 0.3056 0.239  0.3008 0.0028  0.038   -0.013  200 LYS   A O   
1516 C CB  . LYS   A 219 ? 0.2761 0.2148 0.2722 0.0001  0.0393  -0.01   200 LYS   A CB  
1517 C CG  . LYS   A 219 ? 0.2972 0.2331 0.2855 -0.0032 0.0392  -0.0083 200 LYS   A CG  
1518 C CD  . LYS   A 219 ? 0.4131 0.346  0.4049 -0.0037 0.0513  -0.0096 200 LYS   A CD  
1519 C CE  . LYS   A 219 ? 0.4988 0.4278 0.4809 -0.0076 0.0504  -0.0074 200 LYS   A CE  
1520 N NZ  . LYS   A 219 ? 0.5498 0.4746 0.534  -0.009  0.0634  -0.0087 200 LYS   A NZ  
1521 N N   . SER   A 220 ? 0.2436 0.189  0.2419 0.0028  0.0205  -0.0092 201 SER   A N   
1522 C CA  . SER   A 220 ? 0.2372 0.1816 0.2384 0.0045  0.0201  -0.0101 201 SER   A CA  
1523 C C   . SER   A 220 ? 0.2551 0.1878 0.2383 0.0011  0.0172  -0.0113 201 SER   A C   
1524 O O   . SER   A 220 ? 0.2478 0.1803 0.2242 -0.0014 0.0097  -0.0098 201 SER   A O   
1525 C CB  . SER   A 220 ? 0.3022 0.2588 0.3163 0.0064  0.0126  -0.0077 201 SER   A CB  
1526 O OG  . SER   A 220 ? 0.3959 0.3515 0.4126 0.0076  0.0112  -0.0079 201 SER   A OG  
1527 N N   . SER   A 221 ? 0.2594 0.182  0.2361 0.0009  0.0228  -0.0142 202 SER   A N   
1528 C CA  . SER   A 221 ? 0.2799 0.1904 0.2391 -0.0028 0.0193  -0.0154 202 SER   A CA  
1529 C C   . SER   A 221 ? 0.2588 0.172  0.2247 -0.0011 0.0153  -0.0153 202 SER   A C   
1530 O O   . SER   A 221 ? 0.2744 0.1797 0.2285 -0.0042 0.0104  -0.0157 202 SER   A O   
1531 C CB  . SER   A 221 ? 0.327  0.22   0.2675 -0.0062 0.028   -0.0193 202 SER   A CB  
1532 O OG  . SER   A 221 ? 0.3606 0.2519 0.3106 -0.0028 0.038   -0.0223 202 SER   A OG  
1533 N N   . TYR   A 222 ? 0.2417 0.1657 0.2259 0.0031  0.0158  -0.014  203 TYR   A N   
1534 C CA  . TYR   A 222 ? 0.2484 0.1758 0.239  0.0042  0.0108  -0.0128 203 TYR   A CA  
1535 C C   . TYR   A 222 ? 0.2309 0.1715 0.2397 0.0075  0.0087  -0.0098 203 TYR   A C   
1536 O O   . TYR   A 222 ? 0.2224 0.1687 0.241  0.0096  0.0121  -0.0092 203 TYR   A O   
1537 C CB  . TYR   A 222 ? 0.2655 0.1814 0.252  0.0045  0.016   -0.0157 203 TYR   A CB  
1538 C CG  . TYR   A 222 ? 0.2811 0.1976 0.2812 0.0085  0.0248  -0.0169 203 TYR   A CG  
1539 C CD1 . TYR   A 222 ? 0.2764 0.2014 0.2953 0.0121  0.0228  -0.0142 203 TYR   A CD1 
1540 C CD2 . TYR   A 222 ? 0.3121 0.2202 0.3072 0.0081  0.0351  -0.0205 203 TYR   A CD2 
1541 C CE1 . TYR   A 222 ? 0.3011 0.2272 0.3365 0.0159  0.0297  -0.0146 203 TYR   A CE1 
1542 C CE2 . TYR   A 222 ? 0.3376 0.2469 0.3492 0.0119  0.0441  -0.0217 203 TYR   A CE2 
1543 C CZ  . TYR   A 222 ? 0.3472 0.2667 0.381  0.0161  0.0407  -0.0184 203 TYR   A CZ  
1544 O OH  . TYR   A 222 ? 0.3965 0.3175 0.4505 0.0199  0.0487  -0.0191 203 TYR   A OH  
1545 N N   . TYR   A 223 ? 0.2132 0.1577 0.2261 0.0074  0.003   -0.0079 204 TYR   A N   
1546 C CA  . TYR   A 223 ? 0.2074 0.1605 0.234  0.0095  0.0004  -0.0048 204 TYR   A CA  
1547 C C   . TYR   A 223 ? 0.2077 0.1569 0.2348 0.0093  -0.0022 -0.0039 204 TYR   A C   
1548 O O   . TYR   A 223 ? 0.2194 0.1622 0.2365 0.007   -0.0037 -0.0053 204 TYR   A O   
1549 C CB  . TYR   A 223 ? 0.2089 0.1724 0.239  0.0084  -0.0045 -0.0025 204 TYR   A CB  
1550 C CG  . TYR   A 223 ? 0.1884 0.1532 0.2121 0.0053  -0.0094 -0.0022 204 TYR   A CG  
1551 C CD1 . TYR   A 223 ? 0.1913 0.1525 0.2064 0.0033  -0.0102 -0.0039 204 TYR   A CD1 
1552 C CD2 . TYR   A 223 ? 0.1961 0.1652 0.223  0.0041  -0.0132 0       204 TYR   A CD2 
1553 C CE1 . TYR   A 223 ? 0.1922 0.1553 0.2059 0.0007  -0.0145 -0.0035 204 TYR   A CE1 
1554 C CE2 . TYR   A 223 ? 0.2057 0.1761 0.229  0.0011  -0.016  -0.0001 204 TYR   A CE2 
1555 C CZ  . TYR   A 223 ? 0.1956 0.1639 0.2142 -0.0002 -0.0165 -0.0019 204 TYR   A CZ  
1556 O OH  . TYR   A 223 ? 0.213  0.1831 0.2321 -0.003  -0.0192 -0.0018 204 TYR   A OH  
1557 N N   . MET   A 224 ? 0.2043 0.1571 0.2433 0.0113  -0.0037 -0.001  205 MET   A N   
1558 C CA  . MET   A 224 ? 0.2105 0.1589 0.2519 0.0114  -0.0061 0.0006  205 MET   A CA  
1559 C C   . MET   A 224 ? 0.2153 0.1697 0.2592 0.0095  -0.0131 0.005   205 MET   A C   
1560 O O   . MET   A 224 ? 0.2248 0.1866 0.2739 0.0093  -0.0158 0.0074  205 MET   A O   
1561 C CB  . MET   A 224 ? 0.2208 0.1662 0.2759 0.0152  -0.0021 0.0009  205 MET   A CB  
1562 C CG  . MET   A 224 ? 0.2465 0.1841 0.2998 0.0169  0.0075  -0.004  205 MET   A CG  
1563 S SD  . MET   A 224 ? 0.268  0.1914 0.3017 0.0141  0.0108  -0.0091 205 MET   A SD  
1564 C CE  . MET   A 224 ? 0.2861 0.2046 0.3275 0.0152  0.0077  -0.0071 205 MET   A CE  
1565 N N   . ILE   A 225 ? 0.2125 0.1627 0.252  0.0075  -0.0161 0.0061  206 ILE   A N   
1566 C CA  . ILE   A 225 ? 0.2198 0.1729 0.2606 0.0051  -0.022  0.0106  206 ILE   A CA  
1567 C C   . ILE   A 225 ? 0.2305 0.1763 0.2764 0.0064  -0.023  0.0126  206 ILE   A C   
1568 O O   . ILE   A 225 ? 0.2417 0.1814 0.2815 0.005   -0.0226 0.0112  206 ILE   A O   
1569 C CB  . ILE   A 225 ? 0.2181 0.1733 0.249  0.0006  -0.024  0.0104  206 ILE   A CB  
1570 C CG1 . ILE   A 225 ? 0.2321 0.1934 0.2601 0       -0.0221 0.0078  206 ILE   A CG1 
1571 C CG2 . ILE   A 225 ? 0.2519 0.2086 0.2816 -0.0028 -0.0288 0.015   206 ILE   A CG2 
1572 C CD1 . ILE   A 225 ? 0.2454 0.209  0.2675 -0.0042 -0.0228 0.0069  206 ILE   A CD1 
1573 N N   . GLY   A 226 ? 0.2417 0.1877 0.3008 0.0094  -0.024  0.0153  207 GLY   A N   
1574 C CA  . GLY   A 226 ? 0.259  0.1977 0.3268 0.0116  -0.0243 0.0169  207 GLY   A CA  
1575 C C   . GLY   A 226 ? 0.2669 0.198  0.3325 0.0139  -0.0161 0.0108  207 GLY   A C   
1576 O O   . GLY   A 226 ? 0.2726 0.2049 0.3399 0.016   -0.0099 0.0071  207 GLY   A O   
1577 N N   . GLU   A 227 ? 0.2705 0.1927 0.3308 0.013   -0.0156 0.0095  208 GLU   A N   
1578 C CA  . GLU   A 227 ? 0.26   0.1727 0.3151 0.0141  -0.0079 0.0032  208 GLU   A CA  
1579 C C   . GLU   A 227 ? 0.2648 0.1763 0.3019 0.0105  -0.0071 -0.0006 208 GLU   A C   
1580 O O   . GLU   A 227 ? 0.2731 0.1754 0.3017 0.0102  -0.0015 -0.0058 208 GLU   A O   
1581 C CB  . GLU   A 227 ? 0.2706 0.1727 0.3274 0.0143  -0.008  0.0031  208 GLU   A CB  
1582 C CG  . GLU   A 227 ? 0.3156 0.2165 0.3927 0.0183  -0.0086 0.0068  208 GLU   A CG  
1583 C CD  . GLU   A 227 ? 0.4011 0.2903 0.4796 0.0184  -0.0081 0.0061  208 GLU   A CD  
1584 O OE1 . GLU   A 227 ? 0.4115 0.2904 0.4858 0.0194  0.0002  -0.0004 208 GLU   A OE1 
1585 O OE2 . GLU   A 227 ? 0.3996 0.2887 0.4811 0.0168  -0.0158 0.0118  208 GLU   A OE2 
1586 N N   . GLN   A 228 ? 0.2331 0.1529 0.2646 0.0074  -0.0125 0.0018  209 GLN   A N   
1587 C CA  . GLN   A 228 ? 0.2362 0.1553 0.2548 0.0041  -0.0128 -0.0011 209 GLN   A CA  
1588 C C   . GLN   A 228 ? 0.2285 0.1513 0.2445 0.0051  -0.0093 -0.0035 209 GLN   A C   
1589 O O   . GLN   A 228 ? 0.2247 0.1568 0.2469 0.0061  -0.0103 -0.0014 209 GLN   A O   
1590 C CB  . GLN   A 228 ? 0.2328 0.1589 0.2494 0.0004  -0.0185 0.0019  209 GLN   A CB  
1591 C CG  . GLN   A 228 ? 0.2411 0.1669 0.2486 -0.0028 -0.0198 -0.0006 209 GLN   A CG  
1592 C CD  . GLN   A 228 ? 0.2742 0.1892 0.274  -0.005  -0.0204 -0.0031 209 GLN   A CD  
1593 O OE1 . GLN   A 228 ? 0.2991 0.2075 0.2901 -0.006  -0.0192 -0.0064 209 GLN   A OE1 
1594 N NE2 . GLN   A 228 ? 0.2389 0.1507 0.2405 -0.0066 -0.0227 -0.0013 209 GLN   A NE2 
1595 N N   . LYS   A 229 ? 0.2328 0.1471 0.2383 0.004   -0.0058 -0.0078 210 LYS   A N   
1596 C CA  . LYS   A 229 ? 0.2374 0.1528 0.2374 0.0039  -0.0027 -0.0099 210 LYS   A CA  
1597 C C   . LYS   A 229 ? 0.2415 0.1606 0.2341 0.0003  -0.0084 -0.0092 210 LYS   A C   
1598 O O   . LYS   A 229 ? 0.2542 0.1692 0.2408 -0.0029 -0.0128 -0.0092 210 LYS   A O   
1599 C CB  . LYS   A 229 ? 0.266  0.1675 0.2553 0.0035  0.0044  -0.0148 210 LYS   A CB  
1600 C CG  . LYS   A 229 ? 0.3114 0.2122 0.2941 0.003   0.0089  -0.0168 210 LYS   A CG  
1601 C CD  . LYS   A 229 ? 0.354  0.2397 0.3266 0.0025  0.0182  -0.0219 210 LYS   A CD  
1602 C CE  . LYS   A 229 ? 0.3887 0.2704 0.3528 0.0014  0.0249  -0.0243 210 LYS   A CE  
1603 N NZ  . LYS   A 229 ? 0.4245 0.291  0.3811 0.001   0.0367  -0.0298 210 LYS   A NZ  
1604 N N   . PHE   A 230 ? 0.2266 0.1531 0.2211 0.0008  -0.0082 -0.0085 211 PHE   A N   
1605 C CA  . PHE   A 230 ? 0.2371 0.1667 0.2267 -0.0022 -0.013  -0.008  211 PHE   A CA  
1606 C C   . PHE   A 230 ? 0.2356 0.1617 0.2181 -0.0023 -0.0098 -0.0097 211 PHE   A C   
1607 O O   . PHE   A 230 ? 0.2376 0.1667 0.2252 0.0005  -0.0046 -0.01   211 PHE   A O   
1608 C CB  . PHE   A 230 ? 0.2228 0.1654 0.2228 -0.0019 -0.0161 -0.0053 211 PHE   A CB  
1609 C CG  . PHE   A 230 ? 0.2204 0.1657 0.2249 -0.0032 -0.0191 -0.0035 211 PHE   A CG  
1610 C CD1 . PHE   A 230 ? 0.2428 0.1881 0.2466 -0.0065 -0.0232 -0.0032 211 PHE   A CD1 
1611 C CD2 . PHE   A 230 ? 0.2449 0.1919 0.255  -0.0015 -0.0181 -0.0016 211 PHE   A CD2 
1612 C CE1 . PHE   A 230 ? 0.2626 0.2092 0.27   -0.0082 -0.0249 -0.0016 211 PHE   A CE1 
1613 C CE2 . PHE   A 230 ? 0.2567 0.2044 0.2687 -0.0036 -0.0207 0.0004  211 PHE   A CE2 
1614 C CZ  . PHE   A 230 ? 0.2592 0.2066 0.2694 -0.0069 -0.0234 0.0001  211 PHE   A CZ  
1615 N N   . SER   A 231 ? 0.2397 0.1597 0.2114 -0.0059 -0.0135 -0.0102 212 SER   A N   
1616 C CA  . SER   A 231 ? 0.2441 0.1594 0.2067 -0.0071 -0.0116 -0.011  212 SER   A CA  
1617 C C   . SER   A 231 ? 0.2431 0.1711 0.2165 -0.0054 -0.0129 -0.0088 212 SER   A C   
1618 O O   . SER   A 231 ? 0.2234 0.1616 0.2077 -0.0049 -0.0169 -0.0069 212 SER   A O   
1619 C CB  . SER   A 231 ? 0.2556 0.1609 0.204  -0.0124 -0.0183 -0.0107 212 SER   A CB  
1620 O OG  . SER   A 231 ? 0.3142 0.2063 0.2505 -0.0149 -0.0178 -0.013  212 SER   A OG  
1621 N N   . SER   A 232 ? 0.2376 0.1631 0.2063 -0.0053 -0.0087 -0.0094 213 SER   A N   
1622 C CA  . SER   A 232 ? 0.2216 0.1565 0.198  -0.0045 -0.0104 -0.0075 213 SER   A CA  
1623 C C   . SER   A 232 ? 0.2428 0.1681 0.2054 -0.0076 -0.01   -0.0076 213 SER   A C   
1624 O O   . SER   A 232 ? 0.2608 0.1739 0.2096 -0.0093 -0.0047 -0.0097 213 SER   A O   
1625 C CB  . SER   A 232 ? 0.234  0.1779 0.2228 -0.0005 -0.0047 -0.0075 213 SER   A CB  
1626 O OG  . SER   A 232 ? 0.2639 0.2152 0.2586 -0.0001 -0.0055 -0.0062 213 SER   A OG  
1627 N N   . LEU   A 233 ? 0.234  0.1642 0.2004 -0.0085 -0.015  -0.0053 214 LEU   A N   
1628 C CA  . LEU   A 233 ? 0.2511 0.1723 0.2047 -0.0118 -0.0158 -0.0043 214 LEU   A CA  
1629 C C   . LEU   A 233 ? 0.2558 0.1803 0.2128 -0.0096 -0.0074 -0.0051 214 LEU   A C   
1630 O O   . LEU   A 233 ? 0.2557 0.1927 0.2281 -0.0065 -0.0071 -0.0042 214 LEU   A O   
1631 C CB  . LEU   A 233 ? 0.258  0.1837 0.218  -0.0133 -0.0251 -0.001  214 LEU   A CB  
1632 C CG  . LEU   A 233 ? 0.2983 0.2143 0.2461 -0.0173 -0.0288 0.0014  214 LEU   A CG  
1633 C CD1 . LEU   A 233 ? 0.3373 0.2355 0.2623 -0.023  -0.032  0.0015  214 LEU   A CD1 
1634 C CD2 . LEU   A 233 ? 0.2945 0.2174 0.2555 -0.0178 -0.0384 0.005   214 LEU   A CD2 
1635 N N   . PRO   A 234 ? 0.2849 0.1979 0.2279 -0.0115 0       -0.0068 215 PRO   A N   
1636 C CA  . PRO   A 234 ? 0.2922 0.2092 0.242  -0.0091 0.0092  -0.0078 215 PRO   A CA  
1637 C C   . PRO   A 234 ? 0.3323 0.2495 0.28   -0.011  0.0084  -0.0055 215 PRO   A C   
1638 O O   . PRO   A 234 ? 0.412  0.3202 0.349  -0.0133 0.0159  -0.0065 215 PRO   A O   
1639 C CB  . PRO   A 234 ? 0.3195 0.2229 0.256  -0.0107 0.0193  -0.0114 215 PRO   A CB  
1640 C CG  . PRO   A 234 ? 0.3455 0.2335 0.2593 -0.0164 0.0142  -0.0115 215 PRO   A CG  
1641 C CD  . PRO   A 234 ? 0.3132 0.209  0.2351 -0.0157 0.0021  -0.009  215 PRO   A CD  
1642 N N   . LEU   A 235 ? 0.2901 0.2186 0.251  -0.0093 0.002   -0.0032 216 LEU   A N   
1643 C CA  . LEU   A 235 ? 0.278  0.2068 0.2386 -0.0109 0.0003  -0.0007 216 LEU   A CA  
1644 C C   . LEU   A 235 ? 0.2642 0.2006 0.2361 -0.0085 0.0076  -0.0013 216 LEU   A C   
1645 O O   . LEU   A 235 ? 0.2632 0.2108 0.2509 -0.0046 0.0098  -0.0024 216 LEU   A O   
1646 C CB  . LEU   A 235 ? 0.2874 0.2246 0.2593 -0.0103 -0.0096 0.0017  216 LEU   A CB  
1647 C CG  . LEU   A 235 ? 0.3251 0.2565 0.2908 -0.013  -0.019  0.0033  216 LEU   A CG  
1648 C CD1 . LEU   A 235 ? 0.351  0.291  0.3319 -0.0122 -0.027  0.0055  216 LEU   A CD1 
1649 C CD2 . LEU   A 235 ? 0.3499 0.2639 0.2928 -0.0187 -0.0215 0.005   216 LEU   A CD2 
1650 N N   . GLY   A 236 ? 0.2729 0.2028 0.2367 -0.0113 0.0105  0       217 GLY   A N   
1651 C CA  . GLY   A 236 ? 0.2658 0.2032 0.2418 -0.0096 0.016   0.0002  217 GLY   A CA  
1652 C C   . GLY   A 236 ? 0.2521 0.1978 0.2385 -0.009  0.0085  0.0027  217 GLY   A C   
1653 O O   . GLY   A 236 ? 0.247  0.1912 0.231  -0.0102 -0.0004 0.0045  217 GLY   A O   
1654 N N   . ARG   A 237 ? 0.2369 0.1908 0.2363 -0.0073 0.012   0.0027  218 ARG   A N   
1655 C CA  . ARG   A 237 ? 0.2294 0.191  0.2398 -0.0067 0.0061  0.0042  218 ARG   A CA  
1656 C C   . ARG   A 237 ? 0.2376 0.1906 0.2384 -0.0102 0.0007  0.0073  218 ARG   A C   
1657 O O   . ARG   A 237 ? 0.2355 0.1923 0.2438 -0.0097 -0.0066 0.0085  218 ARG   A O   
1658 C CB  . ARG   A 237 ? 0.2547 0.2252 0.2796 -0.005  0.0105  0.0036  218 ARG   A CB  
1659 C CG  . ARG   A 237 ? 0.3095 0.274  0.3296 -0.0073 0.0179  0.0045  218 ARG   A CG  
1660 C CD  . ARG   A 237 ? 0.3802 0.3536 0.4163 -0.0063 0.0202  0.0048  218 ARG   A CD  
1661 N NE  . ARG   A 237 ? 0.4607 0.4277 0.4922 -0.0093 0.0263  0.0063  218 ARG   A NE  
1662 C CZ  . ARG   A 237 ? 0.5265 0.488  0.5514 -0.0122 0.0229  0.0089  218 ARG   A CZ  
1663 N NH1 . ARG   A 237 ? 0.5373 0.4992 0.5615 -0.012  0.0135  0.0101  218 ARG   A NH1 
1664 N NH2 . ARG   A 237 ? 0.5379 0.4927 0.5576 -0.0155 0.0293  0.0105  218 ARG   A NH2 
1665 N N   . GLU   A 238 ? 0.2412 0.1817 0.2256 -0.0141 0.0043  0.0088  219 GLU   A N   
1666 C CA  . GLU   A 238 ? 0.2588 0.1895 0.2328 -0.0183 -0.0023 0.0129  219 GLU   A CA  
1667 C C   . GLU   A 238 ? 0.2737 0.2001 0.2428 -0.0194 -0.0129 0.0147  219 GLU   A C   
1668 O O   . GLU   A 238 ? 0.2781 0.2048 0.2533 -0.0201 -0.0218 0.0178  219 GLU   A O   
1669 C CB  . GLU   A 238 ? 0.3185 0.2342 0.2717 -0.0235 0.0044  0.0142  219 GLU   A CB  
1670 C CG  . GLU   A 238 ? 0.3753 0.2952 0.3361 -0.0228 0.0154  0.0128  219 GLU   A CG  
1671 C CD  . GLU   A 238 ? 0.4884 0.4146 0.4575 -0.0195 0.0261  0.0085  219 GLU   A CD  
1672 O OE1 . GLU   A 238 ? 0.4463 0.3732 0.4142 -0.0176 0.0261  0.0061  219 GLU   A OE1 
1673 O OE2 . GLU   A 238 ? 0.6079 0.5381 0.5863 -0.0191 0.0345  0.0078  219 GLU   A OE2 
1674 N N   . ALA   A 239 ? 0.254  0.1761 0.2138 -0.0198 -0.0123 0.0128  220 ALA   A N   
1675 C CA  . ALA   A 239 ? 0.2661 0.184  0.2222 -0.0213 -0.0228 0.0146  220 ALA   A CA  
1676 C C   . ALA   A 239 ? 0.2482 0.1806 0.2272 -0.0169 -0.0278 0.0138  220 ALA   A C   
1677 O O   . ALA   A 239 ? 0.2503 0.1818 0.2347 -0.0179 -0.0375 0.0166  220 ALA   A O   
1678 C CB  . ALA   A 239 ? 0.2909 0.2011 0.2325 -0.0228 -0.0202 0.0123  220 ALA   A CB  
1679 N N   . VAL   A 240 ? 0.219  0.1641 0.212  -0.0125 -0.0216 0.0102  221 VAL   A N   
1680 C CA  . VAL   A 240 ? 0.199  0.1561 0.211  -0.0092 -0.0249 0.0089  221 VAL   A CA  
1681 C C   . VAL   A 240 ? 0.1995 0.1592 0.2227 -0.0093 -0.029  0.0109  221 VAL   A C   
1682 O O   . VAL   A 240 ? 0.2141 0.1758 0.2478 -0.0091 -0.0356 0.012   221 VAL   A O   
1683 C CB  . VAL   A 240 ? 0.1994 0.1672 0.2206 -0.0058 -0.018  0.0052  221 VAL   A CB  
1684 C CG1 . VAL   A 240 ? 0.2016 0.1796 0.239  -0.0037 -0.0201 0.0035  221 VAL   A CG1 
1685 C CG2 . VAL   A 240 ? 0.2189 0.1844 0.2323 -0.0052 -0.0146 0.0035  221 VAL   A CG2 
1686 N N   . GLU   A 241 ? 0.2016 0.1606 0.2237 -0.0098 -0.0251 0.0115  222 GLU   A N   
1687 C CA  . GLU   A 241 ? 0.2133 0.1737 0.2459 -0.0099 -0.0287 0.0134  222 GLU   A CA  
1688 C C   . GLU   A 241 ? 0.2287 0.1793 0.257  -0.0131 -0.0383 0.0183  222 GLU   A C   
1689 O O   . GLU   A 241 ? 0.2349 0.1888 0.2789 -0.0121 -0.0442 0.0195  222 GLU   A O   
1690 C CB  . GLU   A 241 ? 0.2349 0.1941 0.2641 -0.0108 -0.0229 0.0138  222 GLU   A CB  
1691 C CG  . GLU   A 241 ? 0.3316 0.3012 0.3705 -0.008  -0.016  0.01    222 GLU   A CG  
1692 C CD  . GLU   A 241 ? 0.474  0.4415 0.5087 -0.0094 -0.0095 0.0107  222 GLU   A CD  
1693 O OE1 . GLU   A 241 ? 0.4779 0.4404 0.5114 -0.0115 -0.0109 0.0135  222 GLU   A OE1 
1694 O OE2 . GLU   A 241 ? 0.4728 0.4431 0.5064 -0.0084 -0.0029 0.0088  222 GLU   A OE2 
1695 N N   . ALA   A 242 ? 0.2343 0.1724 0.2424 -0.0171 -0.0402 0.0212  223 ALA   A N   
1696 C CA  . ALA   A 242 ? 0.2428 0.1695 0.2444 -0.0212 -0.0514 0.0269  223 ALA   A CA  
1697 C C   . ALA   A 242 ? 0.2454 0.1762 0.2599 -0.02   -0.0595 0.0272  223 ALA   A C   
1698 O O   . ALA   A 242 ? 0.2627 0.1916 0.2886 -0.0209 -0.0695 0.0313  223 ALA   A O   
1699 C CB  . ALA   A 242 ? 0.2753 0.1854 0.2483 -0.027  -0.0515 0.0294  223 ALA   A CB  
1700 N N   . ALA   A 243 ? 0.2307 0.167  0.2457 -0.0179 -0.0558 0.0232  224 ALA   A N   
1701 C CA  . ALA   A 243 ? 0.2257 0.1654 0.2528 -0.0173 -0.0629 0.0236  224 ALA   A CA  
1702 C C   . ALA   A 243 ? 0.2201 0.1722 0.2747 -0.0134 -0.0626 0.0218  224 ALA   A C   
1703 O O   . ALA   A 243 ? 0.2212 0.1743 0.2917 -0.0136 -0.0707 0.0242  224 ALA   A O   
1704 C CB  . ALA   A 243 ? 0.2277 0.1698 0.2479 -0.0162 -0.0578 0.0197  224 ALA   A CB  
1705 N N   . VAL   A 244 ? 0.2095 0.1704 0.271  -0.0103 -0.0536 0.0177  225 VAL   A N   
1706 C CA  . VAL   A 244 ? 0.1994 0.1701 0.284  -0.0073 -0.0516 0.0149  225 VAL   A CA  
1707 C C   . VAL   A 244 ? 0.202  0.1689 0.298  -0.0081 -0.0584 0.019   225 VAL   A C   
1708 O O   . VAL   A 244 ? 0.2004 0.1714 0.3177 -0.0068 -0.0617 0.0189  225 VAL   A O   
1709 C CB  . VAL   A 244 ? 0.2052 0.1833 0.2896 -0.0051 -0.0414 0.0099  225 VAL   A CB  
1710 C CG1 . VAL   A 244 ? 0.2019 0.1871 0.3057 -0.0031 -0.0385 0.0068  225 VAL   A CG1 
1711 C CG2 . VAL   A 244 ? 0.1998 0.1822 0.2773 -0.0041 -0.036  0.0064  225 VAL   A CG2 
1712 N N   . LYS   A 245 ? 0.2116 0.1702 0.2945 -0.0105 -0.0603 0.0227  226 LYS   A N   
1713 C CA  . LYS   A 245 ? 0.2212 0.1746 0.3142 -0.0118 -0.0684 0.0278  226 LYS   A CA  
1714 C C   . LYS   A 245 ? 0.2356 0.1819 0.332  -0.0144 -0.0813 0.0336  226 LYS   A C   
1715 O O   . LYS   A 245 ? 0.2393 0.1862 0.3575 -0.0137 -0.0887 0.0365  226 LYS   A O   
1716 C CB  . LYS   A 245 ? 0.2453 0.1899 0.3205 -0.0147 -0.0674 0.031   226 LYS   A CB  
1717 C CG  . LYS   A 245 ? 0.2529 0.2051 0.3309 -0.0122 -0.0566 0.026   226 LYS   A CG  
1718 C CD  . LYS   A 245 ? 0.4094 0.3534 0.4702 -0.0153 -0.054  0.0289  226 LYS   A CD  
1719 C CE  . LYS   A 245 ? 0.5274 0.4793 0.5881 -0.0133 -0.0429 0.0239  226 LYS   A CE  
1720 N NZ  . LYS   A 245 ? 0.5838 0.5428 0.663  -0.011  -0.0407 0.0213  226 LYS   A NZ  
1721 N N   . GLU   A 246 ? 0.2325 0.1708 0.3085 -0.0178 -0.0851 0.0356  227 GLU   A N   
1722 C CA  . GLU   A 246 ? 0.2519 0.1824 0.3298 -0.0212 -0.0989 0.0415  227 GLU   A CA  
1723 C C   . GLU   A 246 ? 0.2258 0.1674 0.3331 -0.0177 -0.1008 0.0394  227 GLU   A C   
1724 O O   . GLU   A 246 ? 0.2433 0.1826 0.3689 -0.0188 -0.1127 0.0447  227 GLU   A O   
1725 C CB  . GLU   A 246 ? 0.2809 0.2004 0.329  -0.0257 -0.1006 0.0426  227 GLU   A CB  
1726 C CG  . GLU   A 246 ? 0.3109 0.2191 0.3545 -0.0309 -0.1163 0.0492  227 GLU   A CG  
1727 C CD  . GLU   A 246 ? 0.3987 0.2947 0.4109 -0.0359 -0.1168 0.0491  227 GLU   A CD  
1728 O OE1 . GLU   A 246 ? 0.4108 0.2996 0.4206 -0.0398 -0.1287 0.0529  227 GLU   A OE1 
1729 O OE2 . GLU   A 246 ? 0.3937 0.2875 0.3857 -0.0358 -0.105  0.0448  227 GLU   A OE2 
1730 N N   . ALA   A 247 ? 0.2119 0.1652 0.326  -0.0138 -0.0893 0.0321  228 ALA   A N   
1731 C CA  . ALA   A 247 ? 0.2058 0.1688 0.3452 -0.0112 -0.0886 0.0293  228 ALA   A CA  
1732 C C   . ALA   A 247 ? 0.2202 0.1914 0.3894 -0.0078 -0.0853 0.0272  228 ALA   A C   
1733 O O   . ALA   A 247 ? 0.2282 0.2073 0.4206 -0.0057 -0.0828 0.0242  228 ALA   A O   
1734 C CB  . ALA   A 247 ? 0.2122 0.1822 0.3438 -0.0096 -0.0782 0.023   228 ALA   A CB  
1735 N N   . GLY   A 248 ? 0.1973 0.1658 0.366  -0.0074 -0.0845 0.0282  229 GLY   A N   
1736 C CA  . GLY   A 248 ? 0.2064 0.18   0.4034 -0.0046 -0.0828 0.0268  229 GLY   A CA  
1737 C C   . GLY   A 248 ? 0.1928 0.1746 0.3938 -0.0016 -0.0684 0.0186  229 GLY   A C   
1738 O O   . GLY   A 248 ? 0.1932 0.1809 0.4187 0.0007  -0.0635 0.0146  229 GLY   A O   
1739 N N   . TYR   A 249 ? 0.1859 0.1672 0.3632 -0.0021 -0.0617 0.0161  230 TYR   A N   
1740 C CA  . TYR   A 249 ? 0.1632 0.1507 0.3415 -0.0003 -0.0498 0.009   230 TYR   A CA  
1741 C C   . TYR   A 249 ? 0.1714 0.1547 0.3389 -0.001  -0.0491 0.0105  230 TYR   A C   
1742 O O   . TYR   A 249 ? 0.2034 0.1789 0.3579 -0.0032 -0.0562 0.0166  230 TYR   A O   
1743 C CB  . TYR   A 249 ? 0.17   0.162  0.3318 -0.0003 -0.0421 0.0044  230 TYR   A CB  
1744 C CG  . TYR   A 249 ? 0.161  0.1569 0.3307 0       -0.0415 0.0027  230 TYR   A CG  
1745 C CD1 . TYR   A 249 ? 0.1754 0.1676 0.3366 -0.0015 -0.0488 0.007   230 TYR   A CD1 
1746 C CD2 . TYR   A 249 ? 0.1498 0.1521 0.3328 0.0011  -0.0328 -0.0036 230 TYR   A CD2 
1747 C CE1 . TYR   A 249 ? 0.1811 0.177  0.3494 -0.0015 -0.0482 0.0054  230 TYR   A CE1 
1748 C CE2 . TYR   A 249 ? 0.1679 0.1737 0.3579 0.0009  -0.0312 -0.0052 230 TYR   A CE2 
1749 C CZ  . TYR   A 249 ? 0.1681 0.1712 0.351  -0.0002 -0.0391 -0.0006 230 TYR   A CZ  
1750 O OH  . TYR   A 249 ? 0.1737 0.1802 0.3638 -0.0007 -0.0377 -0.002  230 TYR   A OH  
1751 N N   . THR   A 250 ? 0.1693 0.1569 0.3416 0.0002  -0.0407 0.0049  231 THR   A N   
1752 C CA  . THR   A 250 ? 0.1747 0.1598 0.3375 -0.0007 -0.0385 0.0053  231 THR   A CA  
1753 C C   . THR   A 250 ? 0.1924 0.1825 0.3428 -0.0007 -0.0298 -0.0001 231 THR   A C   
1754 O O   . THR   A 250 ? 0.1862 0.1813 0.3432 0       -0.0236 -0.0061 231 THR   A O   
1755 C CB  . THR   A 250 ? 0.2129 0.1968 0.3953 0.0003  -0.0385 0.0044  231 THR   A CB  
1756 O OG1 . THR   A 250 ? 0.2448 0.225  0.4173 -0.0011 -0.0382 0.0063  231 THR   A OG1 
1757 C CG2 . THR   A 250 ? 0.2093 0.199  0.4068 0.0018  -0.0296 -0.0037 231 THR   A CG2 
1758 N N   . ILE   A 251 ? 0.1774 0.1655 0.3106 -0.002  -0.0292 0.0019  232 ILE   A N   
1759 C CA  . ILE   A 251 ? 0.1737 0.1665 0.2963 -0.0021 -0.0228 -0.002  232 ILE   A CA  
1760 C C   . ILE   A 251 ? 0.1782 0.1731 0.3039 -0.0027 -0.0183 -0.0054 232 ILE   A C   
1761 O O   . ILE   A 251 ? 0.195  0.1864 0.3223 -0.0035 -0.0199 -0.0029 232 ILE   A O   
1762 C CB  . ILE   A 251 ? 0.1901 0.1798 0.2955 -0.0032 -0.0239 0.002   232 ILE   A CB  
1763 C CG1 . ILE   A 251 ? 0.2147 0.2017 0.315  -0.0032 -0.0281 0.0043  232 ILE   A CG1 
1764 C CG2 . ILE   A 251 ? 0.2054 0.1998 0.303  -0.0032 -0.0181 -0.0009 232 ILE   A CG2 
1765 C CD1 . ILE   A 251 ? 0.2627 0.2432 0.3446 -0.0049 -0.029  0.0082  232 ILE   A CD1 
1766 N N   . GLU   A 252 ? 0.1741 0.1734 0.3004 -0.003  -0.0132 -0.0111 233 GLU   A N   
1767 C CA  . GLU   A 252 ? 0.1777 0.1778 0.305  -0.0045 -0.0095 -0.0149 233 GLU   A CA  
1768 C C   . GLU   A 252 ? 0.1804 0.1826 0.2964 -0.0057 -0.009  -0.0136 233 GLU   A C   
1769 O O   . GLU   A 252 ? 0.1837 0.1853 0.3007 -0.007  -0.0088 -0.0133 233 GLU   A O   
1770 C CB  . GLU   A 252 ? 0.2073 0.2088 0.3386 -0.0055 -0.0046 -0.0215 233 GLU   A CB  
1771 C CG  . GLU   A 252 ? 0.2586 0.2579 0.4066 -0.0041 -0.0038 -0.0232 233 GLU   A CG  
1772 C CD  . GLU   A 252 ? 0.3407 0.3391 0.4953 -0.0056 0.0035  -0.031  233 GLU   A CD  
1773 O OE1 . GLU   A 252 ? 0.3329 0.3296 0.5047 -0.0043 0.0053  -0.0328 233 GLU   A OE1 
1774 O OE2 . GLU   A 252 ? 0.3995 0.398  0.5423 -0.0084 0.0075  -0.0351 233 GLU   A OE2 
1775 N N   . TRP   A 253 ? 0.1624 0.167  0.2698 -0.0053 -0.0089 -0.0128 234 TRP   A N   
1776 C CA  . TRP   A 253 ? 0.1643 0.171  0.2646 -0.0059 -0.0086 -0.0109 234 TRP   A CA  
1777 C C   . TRP   A 253 ? 0.1527 0.1601 0.2457 -0.0046 -0.009  -0.0087 234 TRP   A C   
1778 O O   . TRP   A 253 ? 0.1471 0.1542 0.2391 -0.0038 -0.0096 -0.0096 234 TRP   A O   
1779 C CB  . TRP   A 253 ? 0.2022 0.2115 0.3019 -0.0082 -0.0076 -0.0142 234 TRP   A CB  
1780 C CG  . TRP   A 253 ? 0.2121 0.2222 0.3075 -0.0094 -0.0066 -0.0178 234 TRP   A CG  
1781 C CD1 . TRP   A 253 ? 0.2368 0.2448 0.3337 -0.0112 -0.0041 -0.0228 234 TRP   A CD1 
1782 C CD2 . TRP   A 253 ? 0.2306 0.2428 0.3188 -0.0096 -0.0074 -0.017  234 TRP   A CD2 
1783 N NE1 . TRP   A 253 ? 0.251  0.2592 0.3405 -0.0128 -0.003  -0.025  234 TRP   A NE1 
1784 C CE2 . TRP   A 253 ? 0.2453 0.2562 0.3293 -0.0119 -0.0057 -0.0211 234 TRP   A CE2 
1785 C CE3 . TRP   A 253 ? 0.2396 0.254  0.3249 -0.0081 -0.0087 -0.0132 234 TRP   A CE3 
1786 C CZ2 . TRP   A 253 ? 0.2705 0.282  0.3466 -0.0129 -0.0064 -0.0209 234 TRP   A CZ2 
1787 C CZ3 . TRP   A 253 ? 0.2613 0.2766 0.3408 -0.0084 -0.0095 -0.0132 234 TRP   A CZ3 
1788 C CH2 . TRP   A 253 ? 0.2623 0.2762 0.3369 -0.0109 -0.0089 -0.0166 234 TRP   A CH2 
1789 N N   . PHE   A 254 ? 0.1428 0.1506 0.2319 -0.0045 -0.0082 -0.006  235 PHE   A N   
1790 C CA  . PHE   A 254 ? 0.15   0.157  0.2323 -0.0033 -0.0076 -0.0041 235 PHE   A CA  
1791 C C   . PHE   A 254 ? 0.1538 0.1641 0.2371 -0.0034 -0.0055 -0.0033 235 PHE   A C   
1792 O O   . PHE   A 254 ? 0.1528 0.1632 0.2399 -0.0041 -0.0038 -0.0019 235 PHE   A O   
1793 C CB  . PHE   A 254 ? 0.1614 0.1621 0.2382 -0.0032 -0.0079 -0.0008 235 PHE   A CB  
1794 C CG  . PHE   A 254 ? 0.1715 0.1688 0.239  -0.0026 -0.0076 0.0004  235 PHE   A CG  
1795 C CD1 . PHE   A 254 ? 0.1925 0.1905 0.2567 -0.002  -0.0038 0.0007  235 PHE   A CD1 
1796 C CD2 . PHE   A 254 ? 0.2132 0.2064 0.2771 -0.0026 -0.0113 0.0012  235 PHE   A CD2 
1797 C CE1 . PHE   A 254 ? 0.2105 0.2041 0.2658 -0.0016 -0.003  0.0012  235 PHE   A CE1 
1798 C CE2 . PHE   A 254 ? 0.2379 0.227  0.2923 -0.0026 -0.0114 0.0021  235 PHE   A CE2 
1799 C CZ  . PHE   A 254 ? 0.2205 0.2095 0.2699 -0.0021 -0.007  0.0018  235 PHE   A CZ  
1800 N N   . GLU   A 255 ? 0.1404 0.1534 0.222  -0.0027 -0.0059 -0.0039 236 GLU   A N   
1801 C CA  . GLU   A 255 ? 0.1385 0.155  0.2247 -0.0026 -0.005  -0.0026 236 GLU   A CA  
1802 C C   . GLU   A 255 ? 0.1454 0.1604 0.2282 -0.0007 -0.0027 -0.0013 236 GLU   A C   
1803 O O   . GLU   A 255 ? 0.1599 0.1729 0.2363 0       -0.0039 -0.0021 236 GLU   A O   
1804 C CB  . GLU   A 255 ? 0.158  0.178  0.2461 -0.0043 -0.0088 -0.004  236 GLU   A CB  
1805 C CG  . GLU   A 255 ? 0.1774 0.2013 0.2731 -0.0047 -0.0104 -0.0019 236 GLU   A CG  
1806 C CD  . GLU   A 255 ? 0.216  0.2408 0.3091 -0.007  -0.0157 -0.0023 236 GLU   A CD  
1807 O OE1 . GLU   A 255 ? 0.2837 0.3103 0.3814 -0.0097 -0.02   -0.0016 236 GLU   A OE1 
1808 O OE2 . GLU   A 255 ? 0.2387 0.262  0.3248 -0.0063 -0.016  -0.0028 236 GLU   A OE2 
1809 N N   . VAL   A 256 ? 0.1332 0.1487 0.2212 0.0001  0.001   0.0003  237 VAL   A N   
1810 C CA  . VAL   A 256 ? 0.1384 0.1522 0.2257 0.0019  0.0043  0.0009  237 VAL   A CA  
1811 C C   . VAL   A 256 ? 0.1519 0.1716 0.2521 0.0025  0.003   0.0022  237 VAL   A C   
1812 O O   . VAL   A 256 ? 0.1618 0.1854 0.2731 0.0015  0.0029  0.0033  237 VAL   A O   
1813 C CB  . VAL   A 256 ? 0.1784 0.1859 0.261  0.002   0.0114  0.0014  237 VAL   A CB  
1814 C CG1 . VAL   A 256 ? 0.2349 0.2403 0.3188 0.0038  0.0166  0.0013  237 VAL   A CG1 
1815 C CG2 . VAL   A 256 ? 0.2099 0.2104 0.2784 0.0008  0.0102  0.0012  237 VAL   A CG2 
1816 N N   . ILE   A 257 ? 0.1497 0.1699 0.2504 0.0038  0.0011  0.0026  238 ILE   A N   
1817 C CA  . ILE   A 257 ? 0.1563 0.181  0.2712 0.0046  -0.0009 0.0047  238 ILE   A CA  
1818 C C   . ILE   A 257 ? 0.1601 0.1819 0.279  0.0073  0.0058  0.0048  238 ILE   A C   
1819 O O   . ILE   A 257 ? 0.1812 0.1972 0.2881 0.0081  0.0088  0.0032  238 ILE   A O   
1820 C CB  . ILE   A 257 ? 0.1838 0.2107 0.2978 0.0031  -0.0095 0.0059  238 ILE   A CB  
1821 C CG1 . ILE   A 257 ? 0.2099 0.233  0.3137 0.0041  -0.0098 0.0052  238 ILE   A CG1 
1822 C CG2 . ILE   A 257 ? 0.2142 0.242  0.3219 -0.0005 -0.0146 0.0047  238 ILE   A CG2 
1823 C CD1 . ILE   A 257 ? 0.2252 0.249  0.3271 0.0021  -0.0176 0.0069  238 ILE   A CD1 
1824 N N   A SER   A 258 ? 0.1412 0.1665 0.278  0.0086  0.0083  0.0066  239 SER   A N   
1825 N N   B SER   A 258 ? 0.1504 0.1759 0.2872 0.0086  0.008   0.0066  239 SER   A N   
1826 C CA  A SER   A 258 ? 0.138  0.1599 0.281  0.0112  0.0168  0.0059  239 SER   A CA  
1827 C CA  B SER   A 258 ? 0.1602 0.1825 0.304  0.0112  0.0164  0.0061  239 SER   A CA  
1828 C C   A SER   A 258 ? 0.1598 0.1813 0.306  0.0131  0.013   0.007   239 SER   A C   
1829 C C   B SER   A 258 ? 0.1733 0.1953 0.3215 0.0132  0.013   0.0072  239 SER   A C   
1830 O O   A SER   A 258 ? 0.1658 0.1816 0.3092 0.015   0.0198  0.0052  239 SER   A O   
1831 O O   B SER   A 258 ? 0.1827 0.1998 0.3317 0.0154  0.0202  0.0057  239 SER   A O   
1832 C CB  A SER   A 258 ? 0.1373 0.1631 0.302  0.0121  0.0229  0.007   239 SER   A CB  
1833 C CB  B SER   A 258 ? 0.1833 0.2097 0.3484 0.0118  0.0222  0.0072  239 SER   A CB  
1834 O OG  A SER   A 258 ? 0.1357 0.1695 0.3182 0.0117  0.0139  0.0106  239 SER   A OG  
1835 O OG  B SER   A 258 ? 0.2415 0.2669 0.4005 0.0096  0.0259  0.0063  239 SER   A OG  
1836 N N   . GLN   A 259 ? 0.1568 0.1828 0.3072 0.0121  0.0023  0.0098  240 GLN   A N   
1837 C CA  . GLN   A 259 ? 0.1555 0.1807 0.3099 0.0134  -0.0025 0.0118  240 GLN   A CA  
1838 C C   . GLN   A 259 ? 0.1647 0.1829 0.3017 0.0142  0.001   0.0091  240 GLN   A C   
1839 O O   . GLN   A 259 ? 0.1813 0.197  0.3005 0.0124  -0.0002 0.0071  240 GLN   A O   
1840 C CB  . GLN   A 259 ? 0.1904 0.2185 0.3419 0.0102  -0.0148 0.0149  240 GLN   A CB  
1841 C CG  . GLN   A 259 ? 0.2222 0.2484 0.3749 0.0103  -0.0215 0.0179  240 GLN   A CG  
1842 C CD  . GLN   A 259 ? 0.2412 0.2702 0.4188 0.0128  -0.0228 0.0216  240 GLN   A CD  
1843 O OE1 . GLN   A 259 ? 0.2723 0.3062 0.4662 0.0116  -0.0287 0.0252  240 GLN   A OE1 
1844 N NE2 . GLN   A 259 ? 0.2493 0.2746 0.4323 0.0163  -0.0178 0.0212  240 GLN   A NE2 
1845 N N   . SER   A 260 ? 0.1712 0.1861 0.3155 0.017   0.0051  0.0091  241 SER   A N   
1846 C CA  . SER   A 260 ? 0.1847 0.1921 0.3137 0.0176  0.0081  0.0065  241 SER   A CA  
1847 C C   . SER   A 260 ? 0.1917 0.1989 0.3241 0.0181  0.0009  0.0093  241 SER   A C   
1848 O O   . SER   A 260 ? 0.1959 0.2076 0.3442 0.0184  -0.0053 0.0134  241 SER   A O   
1849 C CB  . SER   A 260 ? 0.2111 0.2118 0.3416 0.0197  0.0202  0.0032  241 SER   A CB  
1850 O OG  . SER   A 260 ? 0.2458 0.2449 0.3696 0.0183  0.0268  0.001   241 SER   A OG  
1851 N N   . TYR   A 261 ? 0.1822 0.1834 0.2991 0.0176  0.0009  0.0076  242 TYR   A N   
1852 C CA  . TYR   A 261 ? 0.197  0.1968 0.3161 0.0178  -0.0054 0.0104  242 TYR   A CA  
1853 C C   . TYR   A 261 ? 0.2151 0.2127 0.3526 0.0215  -0.0009 0.0112  242 TYR   A C   
1854 O O   . TYR   A 261 ? 0.2146 0.2097 0.3581 0.0237  0.0093  0.008   242 TYR   A O   
1855 C CB  . TYR   A 261 ? 0.1845 0.1781 0.284  0.0165  -0.0048 0.0079  242 TYR   A CB  
1856 C CG  . TYR   A 261 ? 0.1664 0.1627 0.2524 0.0129  -0.01   0.0078  242 TYR   A CG  
1857 C CD1 . TYR   A 261 ? 0.1692 0.1674 0.2528 0.0102  -0.0179 0.0108  242 TYR   A CD1 
1858 C CD2 . TYR   A 261 ? 0.1787 0.1746 0.2544 0.0117  -0.0067 0.0047  242 TYR   A CD2 
1859 C CE1 . TYR   A 261 ? 0.1811 0.1809 0.2531 0.0066  -0.0207 0.0099  242 TYR   A CE1 
1860 C CE2 . TYR   A 261 ? 0.1846 0.1831 0.2518 0.0089  -0.0105 0.0044  242 TYR   A CE2 
1861 C CZ  . TYR   A 261 ? 0.1755 0.176  0.241  0.0064  -0.0166 0.0065  242 TYR   A CZ  
1862 O OH  . TYR   A 261 ? 0.1975 0.1994 0.2545 0.0034  -0.0181 0.005   242 TYR   A OH  
1863 N N   . SER   A 262 ? 0.2306 0.2274 0.3749 0.0219  -0.0076 0.0149  243 SER   A N   
1864 C CA  . SER   A 262 ? 0.2379 0.2318 0.4015 0.0257  -0.004  0.0157  243 SER   A CA  
1865 C C   . SER   A 262 ? 0.2524 0.2372 0.4061 0.0274  0.0076  0.0098  243 SER   A C   
1866 O O   . SER   A 262 ? 0.2213 0.2014 0.3528 0.0252  0.0079  0.0071  243 SER   A O   
1867 C CB  . SER   A 262 ? 0.261  0.254  0.4301 0.0251  -0.0148 0.0213  243 SER   A CB  
1868 O OG  . SER   A 262 ? 0.277  0.2759 0.4521 0.0223  -0.0267 0.0272  243 SER   A OG  
1869 N N   . SER   A 263 ? 0.2869 0.2683 0.4574 0.0309  0.017   0.0077  244 SER   A N   
1870 C CA  . SER   A 263 ? 0.3218 0.2924 0.481  0.0317  0.029   0.0015  244 SER   A CA  
1871 C C   . SER   A 263 ? 0.3189 0.2814 0.4636 0.0309  0.0262  0.0005  244 SER   A C   
1872 O O   . SER   A 263 ? 0.3558 0.3092 0.4813 0.0293  0.0327  -0.0045 244 SER   A O   
1873 C CB  . SER   A 263 ? 0.339  0.3067 0.5215 0.0355  0.0406  -0.0009 244 SER   A CB  
1874 O OG  . SER   A 263 ? 0.382  0.3508 0.5865 0.0385  0.0353  0.0032  244 SER   A OG  
1875 N N   . THR   A 264 ? 0.307  0.2724 0.4589 0.031   0.0155  0.0058  245 THR   A N   
1876 C CA  . THR   A 264 ? 0.3229 0.2814 0.4625 0.0299  0.0114  0.006   245 THR   A CA  
1877 C C   . THR   A 264 ? 0.3127 0.2723 0.4283 0.0255  0.0054  0.006   245 THR   A C   
1878 O O   . THR   A 264 ? 0.3227 0.2768 0.426  0.0238  0.0028  0.0056  245 THR   A O   
1879 C CB  . THR   A 264 ? 0.368  0.3288 0.5251 0.0311  0.0017  0.0126  245 THR   A CB  
1880 O OG1 . THR   A 264 ? 0.4058 0.3759 0.5651 0.0287  -0.0087 0.0181  245 THR   A OG1 
1881 C CG2 . THR   A 264 ? 0.3763 0.336  0.5624 0.0359  0.007   0.0132  245 THR   A CG2 
1882 N N   . MET   A 265 ? 0.2611 0.2279 0.371  0.0236  0.0034  0.0063  246 MET   A N   
1883 C CA  . MET   A 265 ? 0.2535 0.2219 0.3448 0.0198  -0.0017 0.0062  246 MET   A CA  
1884 C C   . MET   A 265 ? 0.2544 0.2195 0.3308 0.0185  0.0043  0.0015  246 MET   A C   
1885 O O   . MET   A 265 ? 0.2438 0.2057 0.3052 0.016   0.0024  0       246 MET   A O   
1886 C CB  . MET   A 265 ? 0.2944 0.2718 0.3882 0.0177  -0.0097 0.0103  246 MET   A CB  
1887 C CG  . MET   A 265 ? 0.4155 0.3972 0.5281 0.0189  -0.0152 0.0153  246 MET   A CG  
1888 S SD  . MET   A 265 ? 0.4877 0.4666 0.6043 0.0177  -0.025  0.0213  246 MET   A SD  
1889 C CE  . MET   A 265 ? 0.2803 0.2561 0.3706 0.013   -0.0265 0.0192  246 MET   A CE  
1890 N N   . ALA   A 266 ? 0.2403 0.2071 0.3211 0.0196  0.0103  -0.0003 247 ALA   A N   
1891 C CA  . ALA   A 266 ? 0.2522 0.2154 0.3174 0.0175  0.0145  -0.0038 247 ALA   A CA  
1892 C C   . ALA   A 266 ? 0.277  0.2387 0.3476 0.0187  0.0236  -0.006  247 ALA   A C   
1893 O O   . ALA   A 266 ? 0.3138 0.2809 0.4035 0.0212  0.0253  -0.0043 247 ALA   A O   
1894 C CB  . ALA   A 266 ? 0.2502 0.2205 0.3086 0.0149  0.0076  -0.0021 247 ALA   A CB  
1895 N N   . ASN   A 267 ? 0.2484 0.2018 0.3029 0.0165  0.0293  -0.0096 248 ASN   A N   
1896 C CA  . ASN   A 267 ? 0.2454 0.1952 0.302  0.0167  0.0397  -0.0121 248 ASN   A CA  
1897 C C   . ASN   A 267 ? 0.2665 0.2208 0.3177 0.0146  0.0382  -0.0111 248 ASN   A C   
1898 O O   . ASN   A 267 ? 0.3037 0.2504 0.344  0.0125  0.0454  -0.0135 248 ASN   A O   
1899 C CB  . ASN   A 267 ? 0.2738 0.208  0.314  0.0148  0.0488  -0.0169 248 ASN   A CB  
1900 C CG  . ASN   A 267 ? 0.3216 0.2475 0.3363 0.0103  0.0444  -0.0179 248 ASN   A CG  
1901 O OD1 . ASN   A 267 ? 0.2973 0.2295 0.3087 0.0092  0.0341  -0.0151 248 ASN   A OD1 
1902 N ND2 . ASN   A 267 ? 0.3466 0.2569 0.3422 0.0069  0.052   -0.022  248 ASN   A ND2 
1903 N N   . ASN   A 268 ? 0.2166 0.1821 0.2753 0.0149  0.0294  -0.0076 249 ASN   A N   
1904 C CA  . ASN   A 268 ? 0.2052 0.1745 0.2596 0.0129  0.0277  -0.0068 249 ASN   A CA  
1905 C C   . ASN   A 268 ? 0.2118 0.1847 0.2799 0.014   0.0344  -0.0067 249 ASN   A C   
1906 O O   . ASN   A 268 ? 0.2255 0.2013 0.3112 0.0167  0.0384  -0.0063 249 ASN   A O   
1907 C CB  . ASN   A 268 ? 0.2216 0.2    0.2781 0.0123  0.0175  -0.0042 249 ASN   A CB  
1908 C CG  . ASN   A 268 ? 0.2002 0.1877 0.2741 0.0141  0.0132  -0.0013 249 ASN   A CG  
1909 O OD1 . ASN   A 268 ? 0.1964 0.1835 0.2797 0.0161  0.0134  -0.0004 249 ASN   A OD1 
1910 N ND2 . ASN   A 268 ? 0.1857 0.1807 0.2636 0.0129  0.008   0.0004  249 ASN   A ND2 
1911 N N   . GLU   A 269 ? 0.1985 0.1722 0.2608 0.0119  0.0349  -0.0064 250 GLU   A N   
1912 C CA  . GLU   A 269 ? 0.2122 0.1907 0.2873 0.0122  0.0397  -0.0057 250 GLU   A CA  
1913 C C   . GLU   A 269 ? 0.2093 0.1967 0.2869 0.0112  0.0306  -0.0032 250 GLU   A C   
1914 O O   . GLU   A 269 ? 0.2145 0.2002 0.2828 0.0089  0.0302  -0.0032 250 GLU   A O   
1915 C CB  . GLU   A 269 ? 0.239  0.2077 0.302  0.0096  0.0497  -0.0079 250 GLU   A CB  
1916 C CG  . GLU   A 269 ? 0.2919 0.2498 0.3508 0.0099  0.0604  -0.0114 250 GLU   A CG  
1917 C CD  . GLU   A 269 ? 0.4305 0.3757 0.4733 0.0062  0.0716  -0.0142 250 GLU   A CD  
1918 O OE1 . GLU   A 269 ? 0.4796 0.411  0.5024 0.0037  0.0756  -0.0171 250 GLU   A OE1 
1919 O OE2 . GLU   A 269 ? 0.4474 0.3953 0.4966 0.0051  0.0765  -0.0134 250 GLU   A OE2 
1920 N N   . GLY   A 270 ? 0.1731 0.1687 0.2621 0.0126  0.0233  -0.0011 251 GLY   A N   
1921 C CA  . GLY   A 270 ? 0.1822 0.1852 0.2734 0.0112  0.0152  0.0007  251 GLY   A CA  
1922 C C   . GLY   A 270 ? 0.1605 0.1619 0.2371 0.0094  0.0095  0       251 GLY   A C   
1923 O O   . GLY   A 270 ? 0.1682 0.1641 0.2344 0.0094  0.0093  -0.0011 251 GLY   A O   
1924 N N   . LEU   A 271 ? 0.16   0.1663 0.2372 0.0078  0.0046  0.0005  252 LEU   A N   
1925 C CA  . LEU   A 271 ? 0.1511 0.157  0.2189 0.0062  -0.0001 -0.0004 252 LEU   A CA  
1926 C C   . LEU   A 271 ? 0.1474 0.1549 0.215  0.0047  -0.0007 -0.0008 252 LEU   A C   
1927 O O   . LEU   A 271 ? 0.1629 0.1734 0.2384 0.0045  0.0006  -0.0001 252 LEU   A O   
1928 C CB  . LEU   A 271 ? 0.1673 0.1774 0.2375 0.0053  -0.0058 0.0004  252 LEU   A CB  
1929 C CG  . LEU   A 271 ? 0.196  0.2036 0.2643 0.0063  -0.0067 0.0011  252 LEU   A CG  
1930 C CD1 . LEU   A 271 ? 0.2192 0.2291 0.2999 0.0078  -0.0072 0.0035  252 LEU   A CD1 
1931 C CD2 . LEU   A 271 ? 0.2128 0.2213 0.2755 0.0039  -0.0116 0.001   252 LEU   A CD2 
1932 N N   . PHE   A 272 ? 0.1499 0.1556 0.2107 0.0035  -0.003  -0.0018 253 PHE   A N   
1933 C CA  . PHE   A 272 ? 0.1455 0.1526 0.2078 0.0022  -0.0042 -0.0024 253 PHE   A CA  
1934 C C   . PHE   A 272 ? 0.1465 0.1565 0.2095 0.0009  -0.0076 -0.004  253 PHE   A C   
1935 O O   . PHE   A 272 ? 0.1523 0.1617 0.2119 0.0007  -0.0089 -0.0046 253 PHE   A O   
1936 C CB  . PHE   A 272 ? 0.1536 0.1546 0.2094 0.0017  -0.0035 -0.0019 253 PHE   A CB  
1937 C CG  . PHE   A 272 ? 0.1608 0.1586 0.2112 0.0013  -0.0067 -0.0023 253 PHE   A CG  
1938 C CD1 . PHE   A 272 ? 0.1681 0.1679 0.2227 0.0005  -0.0098 -0.0032 253 PHE   A CD1 
1939 C CD2 . PHE   A 272 ? 0.1717 0.1641 0.214  0.0014  -0.0063 -0.0019 253 PHE   A CD2 
1940 C CE1 . PHE   A 272 ? 0.1759 0.1737 0.2292 0.0001  -0.0128 -0.0033 253 PHE   A CE1 
1941 C CE2 . PHE   A 272 ? 0.1811 0.1707 0.2199 0.0007  -0.0102 -0.0019 253 PHE   A CE2 
1942 C CZ  . PHE   A 272 ? 0.1687 0.1618 0.2144 0.0001  -0.0135 -0.0024 253 PHE   A CZ  
1943 N N   . SER   A 273 ? 0.1466 0.1584 0.2135 -0.0004 -0.0082 -0.0051 254 SER   A N   
1944 C CA  . SER   A 273 ? 0.1536 0.1665 0.2212 -0.0021 -0.0094 -0.0077 254 SER   A CA  
1945 C C   . SER   A 273 ? 0.1422 0.1539 0.2139 -0.0022 -0.009  -0.0083 254 SER   A C   
1946 O O   . SER   A 273 ? 0.1432 0.1549 0.2175 -0.0022 -0.0085 -0.0071 254 SER   A O   
1947 C CB  . SER   A 273 ? 0.1944 0.2098 0.2626 -0.0045 -0.0105 -0.0089 254 SER   A CB  
1948 O OG  . SER   A 273 ? 0.2252 0.2412 0.2904 -0.0047 -0.0122 -0.0074 254 SER   A OG  
1949 N N   . LEU   A 274 ? 0.1372 0.148  0.2113 -0.0026 -0.0093 -0.0101 255 LEU   A N   
1950 C CA  . LEU   A 274 ? 0.1548 0.1642 0.2356 -0.0026 -0.0096 -0.0105 255 LEU   A CA  
1951 C C   . LEU   A 274 ? 0.1506 0.1607 0.2377 -0.0036 -0.008  -0.0143 255 LEU   A C   
1952 O O   . LEU   A 274 ? 0.1508 0.1616 0.2369 -0.0041 -0.0069 -0.0159 255 LEU   A O   
1953 C CB  . LEU   A 274 ? 0.1717 0.177  0.2516 -0.0016 -0.0121 -0.0071 255 LEU   A CB  
1954 C CG  . LEU   A 274 ? 0.1735 0.177  0.2531 -0.0012 -0.0145 -0.0065 255 LEU   A CG  
1955 C CD1 . LEU   A 274 ? 0.1949 0.1986 0.2871 -0.0012 -0.016  -0.0077 255 LEU   A CD1 
1956 C CD2 . LEU   A 274 ? 0.1983 0.1956 0.2697 -0.0012 -0.0176 -0.0025 255 LEU   A CD2 
1957 N N   . VAL   A 275 ? 0.1475 0.1568 0.2424 -0.004  -0.0073 -0.0158 256 VAL   A N   
1958 C CA  . VAL   A 275 ? 0.1533 0.1623 0.2578 -0.0047 -0.0045 -0.0198 256 VAL   A CA  
1959 C C   . VAL   A 275 ? 0.1515 0.1583 0.2671 -0.0031 -0.0074 -0.0175 256 VAL   A C   
1960 O O   . VAL   A 275 ? 0.1527 0.1578 0.2681 -0.003  -0.0093 -0.0151 256 VAL   A O   
1961 C CB  . VAL   A 275 ? 0.1999 0.2083 0.303  -0.0074 -0.0003 -0.0248 256 VAL   A CB  
1962 C CG1 . VAL   A 275 ? 0.2239 0.2306 0.3387 -0.008  0.0045  -0.0297 256 VAL   A CG1 
1963 C CG2 . VAL   A 275 ? 0.2252 0.2342 0.3158 -0.0099 0.001   -0.0262 256 VAL   A CG2 
1964 N N   . ALA   A 276 ? 0.1647 0.1714 0.2909 -0.0022 -0.008  -0.0177 257 ALA   A N   
1965 C CA  . ALA   A 276 ? 0.1734 0.1776 0.3127 -0.0009 -0.0123 -0.0148 257 ALA   A CA  
1966 C C   . ALA   A 276 ? 0.1602 0.1656 0.3184 -0.0005 -0.0087 -0.0189 257 ALA   A C   
1967 O O   . ALA   A 276 ? 0.1651 0.1726 0.3236 -0.0015 -0.0026 -0.0235 257 ALA   A O   
1968 C CB  . ALA   A 276 ? 0.1859 0.1876 0.3208 -0.0004 -0.0195 -0.0089 257 ALA   A CB  
1969 N N   . ARG   A 277 ? 0.164  0.1671 0.3385 0.0007  -0.0122 -0.0169 258 ARG   A N   
1970 C CA  . ARG   A 277 ? 0.1609 0.1651 0.3587 0.0016  -0.009  -0.0201 258 ARG   A CA  
1971 C C   . ARG   A 277 ? 0.1531 0.1563 0.365  0.003   -0.0184 -0.0138 258 ARG   A C   
1972 O O   . ARG   A 277 ? 0.1728 0.1719 0.3792 0.0029  -0.0274 -0.0072 258 ARG   A O   
1973 C CB  . ARG   A 277 ? 0.1897 0.1916 0.4    0.0019  -0.005  -0.0237 258 ARG   A CB  
1974 C CG  . ARG   A 277 ? 0.254  0.2558 0.4521 -0.0005 0.0045  -0.0309 258 ARG   A CG  
1975 C CD  . ARG   A 277 ? 0.3418 0.3403 0.5541 -0.0005 0.0095  -0.0356 258 ARG   A CD  
1976 N NE  . ARG   A 277 ? 0.4427 0.4412 0.673  -0.0005 0.0184  -0.0422 258 ARG   A NE  
1977 C CZ  . ARG   A 277 ? 0.5164 0.5112 0.7569 -0.0014 0.0271  -0.0492 258 ARG   A CZ  
1978 N NH1 . ARG   A 277 ? 0.5249 0.5158 0.7596 -0.0024 0.0265  -0.0501 258 ARG   A NH1 
1979 N NH2 . ARG   A 277 ? 0.548  0.5425 0.8054 -0.0016 0.0368  -0.0556 258 ARG   A NH2 
1980 N N   . LYS   A 278 ? 0.17   0.1761 0.3997 0.0036  -0.0164 -0.0156 259 LYS   A N   
1981 C CA  . LYS   A 278 ? 0.1673 0.1725 0.4139 0.0045  -0.0265 -0.0094 259 LYS   A CA  
1982 C C   . LYS   A 278 ? 0.1945 0.197  0.4642 0.0059  -0.0309 -0.007  259 LYS   A C   
1983 O O   . LYS   A 278 ? 0.2147 0.2185 0.4997 0.0069  -0.0222 -0.0129 259 LYS   A O   
1984 C CB  . LYS   A 278 ? 0.1868 0.1968 0.4502 0.0047  -0.0216 -0.0128 259 LYS   A CB  
1985 C CG  . LYS   A 278 ? 0.2019 0.2117 0.4816 0.0049  -0.033  -0.006  259 LYS   A CG  
1986 C CD  . LYS   A 278 ? 0.2489 0.2645 0.5519 0.0052  -0.0261 -0.0103 259 LYS   A CD  
1987 C CE  . LYS   A 278 ? 0.2638 0.2796 0.5892 0.0055  -0.0379 -0.0037 259 LYS   A CE  
1988 N NZ  . LYS   A 278 ? 0.2047 0.2266 0.553  0.0055  -0.0303 -0.0078 259 LYS   A NZ  
1989 N N   . LEU   A 279 ? 0.2074 0.2049 0.4775 0.0055  -0.0442 0.0016  260 LEU   A N   
1990 C CA  . LEU   A 279 ? 0.2314 0.2254 0.526  0.0067  -0.0507 0.0054  260 LEU   A CA  
1991 C C   . LEU   A 279 ? 0.2684 0.2659 0.5971 0.0082  -0.0537 0.0064  260 LEU   A C   
1992 O O   . LEU   A 279 ? 0.2837 0.2829 0.6123 0.0072  -0.0586 0.009   260 LEU   A O   
1993 C CB  . LEU   A 279 ? 0.264  0.2495 0.5427 0.0045  -0.0646 0.0151  260 LEU   A CB  
1994 C CG  . LEU   A 279 ? 0.3212 0.3031 0.5679 0.0028  -0.0615 0.0149  260 LEU   A CG  
1995 C CD1 . LEU   A 279 ? 0.3544 0.3268 0.5852 -0.0002 -0.0736 0.0239  260 LEU   A CD1 
1996 C CD2 . LEU   A 279 ? 0.3295 0.3123 0.5811 0.004   -0.0533 0.01    260 LEU   A CD2 
1997 N N   . PHE   B 24  ? 0.3296 0.2934 0.2968 -0.0278 -0.0023 0.0179  5   PHE   B N   
1998 C CA  . PHE   B 24  ? 0.3051 0.2749 0.2838 -0.0244 -0.0011 0.0143  5   PHE   B CA  
1999 C C   . PHE   B 24  ? 0.2742 0.2473 0.2577 -0.0269 0.0024  0.014   5   PHE   B C   
2000 O O   . PHE   B 24  ? 0.2734 0.2496 0.2526 -0.0311 0.0057  0.0151  5   PHE   B O   
2001 C CB  . PHE   B 24  ? 0.3119 0.2897 0.2912 -0.0219 0.0015  0.0109  5   PHE   B CB  
2002 C CG  . PHE   B 24  ? 0.3224 0.3027 0.3117 -0.0176 0.0002  0.0082  5   PHE   B CG  
2003 C CD1 . PHE   B 24  ? 0.3268 0.3034 0.3175 -0.0146 -0.0043 0.008   5   PHE   B CD1 
2004 C CD2 . PHE   B 24  ? 0.3358 0.3228 0.3327 -0.017  0.0033  0.0061  5   PHE   B CD2 
2005 C CE1 . PHE   B 24  ? 0.3197 0.2995 0.3195 -0.0113 -0.005  0.0058  5   PHE   B CE1 
2006 C CE2 . PHE   B 24  ? 0.3346 0.324  0.3394 -0.0137 0.0025  0.004   5   PHE   B CE2 
2007 C CZ  . PHE   B 24  ? 0.3043 0.2901 0.311  -0.0109 -0.0015 0.004   5   PHE   B CZ  
2008 N N   . THR   B 25  ? 0.2466 0.2196 0.2388 -0.0247 0.0018  0.0123  6   THR   B N   
2009 C CA  . THR   B 25  ? 0.2285 0.2033 0.2244 -0.0272 0.0043  0.0116  6   THR   B CA  
2010 C C   . THR   B 25  ? 0.2364 0.2218 0.233  -0.0289 0.0087  0.0099  6   THR   B C   
2011 O O   . THR   B 25  ? 0.24   0.2322 0.24   -0.0258 0.0099  0.0074  6   THR   B O   
2012 C CB  . THR   B 25  ? 0.2234 0.1978 0.2279 -0.0235 0.0035  0.0091  6   THR   B CB  
2013 O OG1 . THR   B 25  ? 0.2238 0.1895 0.2297 -0.0213 -0.0004 0.0104  6   THR   B OG1 
2014 C CG2 . THR   B 25  ? 0.2345 0.2102 0.2418 -0.0258 0.0057  0.0076  6   THR   B CG2 
2015 N N   . SER   B 26  ? 0.2579 0.2448 0.2519 -0.0341 0.0108  0.0115  7   SER   B N   
2016 C CA  . SER   B 26  ? 0.2709 0.269  0.2671 -0.036  0.0149  0.0103  7   SER   B CA  
2017 C C   . SER   B 26  ? 0.256  0.2589 0.2601 -0.0345 0.0154  0.0074  7   SER   B C   
2018 O O   . SER   B 26  ? 0.2508 0.2473 0.257  -0.0343 0.0134  0.007   7   SER   B O   
2019 C CB  . SER   B 26  ? 0.3116 0.3102 0.3038 -0.0426 0.0168  0.0133  7   SER   B CB  
2020 O OG  . SER   B 26  ? 0.3557 0.3459 0.3481 -0.0456 0.0145  0.0145  7   SER   B OG  
2021 N N   . LYS   B 27  ? 0.2324 0.2461 0.2408 -0.0334 0.0179  0.0055  8   LYS   B N   
2022 C CA  . LYS   B 27  ? 0.2305 0.2482 0.2455 -0.032  0.0177  0.0031  8   LYS   B CA  
2023 C C   . LYS   B 27  ? 0.2466 0.2626 0.2623 -0.0367 0.0173  0.0036  8   LYS   B C   
2024 O O   . LYS   B 27  ? 0.2498 0.2632 0.268  -0.0358 0.0161  0.0019  8   LYS   B O   
2025 C CB  . LYS   B 27  ? 0.2479 0.2771 0.2677 -0.0292 0.0196  0.0011  8   LYS   B CB  
2026 C CG  . LYS   B 27  ? 0.2736 0.3126 0.2946 -0.0325 0.0227  0.002   8   LYS   B CG  
2027 C CD  . LYS   B 27  ? 0.2758 0.3249 0.3015 -0.0282 0.0244  -0.0002 8   LYS   B CD  
2028 C CE  . LYS   B 27  ? 0.3319 0.3922 0.36   -0.0305 0.0281  0.0004  8   LYS   B CE  
2029 N NZ  . LYS   B 27  ? 0.3441 0.4118 0.3754 -0.025  0.0298  -0.0021 8   LYS   B NZ  
2030 N N   . ASP   B 28  ? 0.2484 0.2648 0.2614 -0.0423 0.0184  0.0061  9   ASP   B N   
2031 C CA  . ASP   B 28  ? 0.2482 0.2611 0.2613 -0.0475 0.0173  0.0066  9   ASP   B CA  
2032 C C   . ASP   B 28  ? 0.2478 0.2472 0.2581 -0.0465 0.0145  0.0061  9   ASP   B C   
2033 O O   . ASP   B 28  ? 0.2663 0.2619 0.2772 -0.0486 0.0133  0.0048  9   ASP   B O   
2034 C CB  . ASP   B 28  ? 0.2715 0.2867 0.2821 -0.0541 0.0187  0.0099  9   ASP   B CB  
2035 C CG  . ASP   B 28  ? 0.3813 0.3869 0.3845 -0.0552 0.0181  0.0129  9   ASP   B CG  
2036 O OD1 . ASP   B 28  ? 0.4294 0.4236 0.429  -0.0581 0.0155  0.0144  9   ASP   B OD1 
2037 O OD2 . ASP   B 28  ? 0.4256 0.4339 0.4261 -0.0527 0.0196  0.0135  9   ASP   B OD2 
2038 N N   . THR   B 29  ? 0.2409 0.2328 0.2484 -0.0429 0.0132  0.0068  10  THR   B N   
2039 C CA  . THR   B 29  ? 0.2352 0.2153 0.2417 -0.0409 0.0107  0.0062  10  THR   B CA  
2040 C C   . THR   B 29  ? 0.2204 0.2016 0.2314 -0.0372 0.0108  0.0025  10  THR   B C   
2041 O O   . THR   B 29  ? 0.2427 0.2158 0.2534 -0.0366 0.0098  0.001   10  THR   B O   
2042 C CB  . THR   B 29  ? 0.2889 0.263  0.2932 -0.0375 0.0088  0.0079  10  THR   B CB  
2043 O OG1 . THR   B 29  ? 0.3447 0.3179 0.3431 -0.0415 0.0089  0.0116  10  THR   B OG1 
2044 C CG2 . THR   B 29  ? 0.2831 0.2455 0.2878 -0.035  0.0061  0.0076  10  THR   B CG2 
2045 N N   . TYR   B 30  ? 0.2033 0.194  0.2181 -0.0343 0.0122  0.001   11  TYR   B N   
2046 C CA  . TYR   B 30  ? 0.2098 0.2022 0.228  -0.0315 0.0126  -0.002  11  TYR   B CA  
2047 C C   . TYR   B 30  ? 0.2394 0.2323 0.2568 -0.0354 0.0126  -0.0035 11  TYR   B C   
2048 O O   . TYR   B 30  ? 0.2765 0.2659 0.2938 -0.0339 0.0126  -0.0059 11  TYR   B O   
2049 C CB  . TYR   B 30  ? 0.1941 0.1954 0.216  -0.0279 0.0135  -0.0028 11  TYR   B CB  
2050 C CG  . TYR   B 30  ? 0.1645 0.1628 0.1876 -0.0234 0.0126  -0.0025 11  TYR   B CG  
2051 C CD1 . TYR   B 30  ? 0.1692 0.1678 0.1904 -0.0228 0.012   -0.0006 11  TYR   B CD1 
2052 C CD2 . TYR   B 30  ? 0.1638 0.1587 0.1896 -0.0201 0.0124  -0.0039 11  TYR   B CD2 
2053 C CE1 . TYR   B 30  ? 0.1831 0.1781 0.2052 -0.0192 0.0103  -0.0001 11  TYR   B CE1 
2054 C CE2 . TYR   B 30  ? 0.1643 0.1574 0.1926 -0.0164 0.0113  -0.0034 11  TYR   B CE2 
2055 C CZ  . TYR   B 30  ? 0.1758 0.1685 0.2023 -0.0161 0.0097  -0.0014 11  TYR   B CZ  
2056 O OH  . TYR   B 30  ? 0.194  0.1843 0.223  -0.0128 0.0078  -0.0008 11  TYR   B OH  
2057 N N   . LEU   B 31  ? 0.2245 0.222  0.2412 -0.0404 0.0128  -0.002  12  LEU   B N   
2058 C CA  . LEU   B 31  ? 0.2454 0.2436 0.2616 -0.0447 0.012   -0.0032 12  LEU   B CA  
2059 C C   . LEU   B 31  ? 0.2748 0.2599 0.2863 -0.0471 0.0105  -0.0041 12  LEU   B C   
2060 O O   . LEU   B 31  ? 0.2924 0.2739 0.302  -0.048  0.0097  -0.0068 12  LEU   B O   
2061 C CB  . LEU   B 31  ? 0.2586 0.266  0.2768 -0.05   0.0123  -0.0011 12  LEU   B CB  
2062 C CG  . LEU   B 31  ? 0.2851 0.3054 0.3083 -0.0475 0.0141  -0.0005 12  LEU   B CG  
2063 C CD1 . LEU   B 31  ? 0.3041 0.3338 0.33   -0.0526 0.0152  0.0017  12  LEU   B CD1 
2064 C CD2 . LEU   B 31  ? 0.3035 0.3293 0.33   -0.0443 0.0135  -0.0028 12  LEU   B CD2 
2065 N N   . SER   B 32  ? 0.2747 0.2519 0.2836 -0.0477 0.0099  -0.002  13  SER   B N   
2066 C CA  . SER   B 32  ? 0.2868 0.2506 0.2912 -0.0503 0.008   -0.0022 13  SER   B CA  
2067 C C   . SER   B 32  ? 0.2898 0.2428 0.2934 -0.0449 0.0075  -0.0038 13  SER   B C   
2068 O O   . SER   B 32  ? 0.3414 0.2839 0.342  -0.0452 0.0064  -0.0061 13  SER   B O   
2069 C CB  . SER   B 32  ? 0.2825 0.2442 0.2843 -0.0553 0.0072  0.0021  13  SER   B CB  
2070 O OG  . SER   B 32  ? 0.2807 0.246  0.283  -0.053  0.0081  0.0048  13  SER   B OG  
2071 N N   . HIS   B 33  ? 0.2388 0.1942 0.2453 -0.0397 0.008   -0.0028 14  HIS   B N   
2072 C CA  . HIS   B 33  ? 0.2304 0.1766 0.2377 -0.0349 0.0071  -0.0034 14  HIS   B CA  
2073 C C   . HIS   B 33  ? 0.2358 0.1856 0.248  -0.0286 0.0088  -0.0062 14  HIS   B C   
2074 O O   . HIS   B 33  ? 0.2506 0.1943 0.2653 -0.0241 0.0083  -0.0068 14  HIS   B O   
2075 C CB  . HIS   B 33  ? 0.2145 0.1582 0.221  -0.0346 0.0053  0.0007  14  HIS   B CB  
2076 C CG  . HIS   B 33  ? 0.2408 0.1766 0.2417 -0.0405 0.0033  0.0037  14  HIS   B CG  
2077 N ND1 . HIS   B 33  ? 0.259  0.2004 0.2573 -0.0471 0.0042  0.0055  14  HIS   B ND1 
2078 C CD2 . HIS   B 33  ? 0.281  0.2033 0.2789 -0.0406 0.0005  0.0052  14  HIS   B CD2 
2079 C CE1 . HIS   B 33  ? 0.2829 0.2141 0.2764 -0.0517 0.002   0.0081  14  HIS   B CE1 
2080 N NE2 . HIS   B 33  ? 0.3057 0.2246 0.2984 -0.0479 -0.0005 0.0082  14  HIS   B NE2 
2081 N N   . PHE   B 34  ? 0.2285 0.189  0.243  -0.0281 0.0106  -0.0072 15  PHE   B N   
2082 C CA  . PHE   B 34  ? 0.2104 0.1744 0.2291 -0.023  0.0124  -0.0095 15  PHE   B CA  
2083 C C   . PHE   B 34  ? 0.2322 0.1928 0.2482 -0.0234 0.014   -0.0133 15  PHE   B C   
2084 O O   . PHE   B 34  ? 0.2268 0.1913 0.24   -0.027  0.0142  -0.0142 15  PHE   B O   
2085 C CB  . PHE   B 34  ? 0.1944 0.17   0.2158 -0.0224 0.0132  -0.0086 15  PHE   B CB  
2086 C CG  . PHE   B 34  ? 0.1832 0.1629 0.2092 -0.0179 0.0147  -0.0099 15  PHE   B CG  
2087 C CD1 . PHE   B 34  ? 0.1926 0.1734 0.2179 -0.0174 0.0167  -0.0126 15  PHE   B CD1 
2088 C CD2 . PHE   B 34  ? 0.1768 0.1588 0.207  -0.0147 0.0139  -0.0082 15  PHE   B CD2 
2089 C CE1 . PHE   B 34  ? 0.19   0.1751 0.2193 -0.0139 0.0184  -0.0131 15  PHE   B CE1 
2090 C CE2 . PHE   B 34  ? 0.1924 0.1789 0.2272 -0.0114 0.0151  -0.0089 15  PHE   B CE2 
2091 C CZ  . PHE   B 34  ? 0.1854 0.1734 0.2199 -0.0111 0.0175  -0.0112 15  PHE   B CZ  
2092 N N   . ASN   B 35  ? 0.2304 0.1832 0.2471 -0.0199 0.0148  -0.0155 16  ASN   B N   
2093 C CA  . ASN   B 35  ? 0.2416 0.1891 0.2543 -0.02   0.0166  -0.0197 16  ASN   B CA  
2094 C C   . ASN   B 35  ? 0.2343 0.189  0.2495 -0.0168 0.0198  -0.0215 16  ASN   B C   
2095 O O   . ASN   B 35  ? 0.2364 0.1922 0.2571 -0.012  0.0214  -0.0216 16  ASN   B O   
2096 C CB  . ASN   B 35  ? 0.2553 0.1908 0.2679 -0.0169 0.0164  -0.0214 16  ASN   B CB  
2097 C CG  . ASN   B 35  ? 0.316  0.2442 0.3234 -0.0165 0.0186  -0.0264 16  ASN   B CG  
2098 O OD1 . ASN   B 35  ? 0.3101 0.2428 0.3157 -0.0157 0.0215  -0.0291 16  ASN   B OD1 
2099 N ND2 . ASN   B 35  ? 0.3623 0.2776 0.366  -0.0169 0.017   -0.028  16  ASN   B ND2 
2100 N N   . PRO   B 36  ? 0.2336 0.1935 0.2449 -0.0196 0.0204  -0.0225 17  PRO   B N   
2101 C CA  . PRO   B 36  ? 0.2386 0.2057 0.2519 -0.017  0.0231  -0.0233 17  PRO   B CA  
2102 C C   . PRO   B 36  ? 0.2522 0.2151 0.2653 -0.0131 0.027   -0.0267 17  PRO   B C   
2103 O O   . PRO   B 36  ? 0.2323 0.2004 0.2509 -0.0096 0.0294  -0.0261 17  PRO   B O   
2104 C CB  . PRO   B 36  ? 0.2617 0.233  0.2694 -0.0212 0.0222  -0.0236 17  PRO   B CB  
2105 C CG  . PRO   B 36  ? 0.2732 0.2411 0.2774 -0.026  0.0192  -0.0232 17  PRO   B CG  
2106 C CD  . PRO   B 36  ? 0.246  0.2069 0.2522 -0.0255 0.0181  -0.0221 17  PRO   B CD  
2107 N N   . ARG   B 37  ? 0.2648 0.2178 0.2717 -0.0137 0.0277  -0.0303 18  ARG   B N   
2108 C CA  . ARG   B 37  ? 0.2861 0.235  0.2923 -0.0095 0.0321  -0.0343 18  ARG   B CA  
2109 C C   . ARG   B 37  ? 0.2679 0.2162 0.2839 -0.004  0.0331  -0.0334 18  ARG   B C   
2110 O O   . ARG   B 37  ? 0.2764 0.2283 0.2973 0.0003  0.0372  -0.0347 18  ARG   B O   
2111 C CB  . ARG   B 37  ? 0.3424 0.2793 0.3392 -0.0112 0.0321  -0.0388 18  ARG   B CB  
2112 C CG  . ARG   B 37  ? 0.4413 0.3782 0.4278 -0.0166 0.0311  -0.0404 18  ARG   B CG  
2113 C CD  . ARG   B 37  ? 0.5739 0.4972 0.551  -0.019  0.0297  -0.0446 18  ARG   B CD  
2114 N NE  . ARG   B 37  ? 0.6965 0.6164 0.6626 -0.0207 0.0317  -0.049  18  ARG   B NE  
2115 C CZ  . ARG   B 37  ? 0.7796 0.6875 0.7354 -0.0234 0.0303  -0.0533 18  ARG   B CZ  
2116 N NH1 . ARG   B 37  ? 0.7875 0.6925 0.7322 -0.0251 0.0319  -0.0572 18  ARG   B NH1 
2117 N NH2 . ARG   B 37  ? 0.7997 0.6977 0.7554 -0.025  0.027   -0.0535 18  ARG   B NH2 
2118 N N   . ASP   B 38  ? 0.2522 0.1961 0.2712 -0.0041 0.0293  -0.031  19  ASP   B N   
2119 C CA  . ASP   B 38  ? 0.252  0.1951 0.2804 0.001   0.0291  -0.0298 19  ASP   B CA  
2120 C C   . ASP   B 38  ? 0.2371 0.1916 0.274  0.0027  0.0293  -0.0263 19  ASP   B C   
2121 O O   . ASP   B 38  ? 0.245  0.2027 0.2902 0.0073  0.0313  -0.0264 19  ASP   B O   
2122 C CB  . ASP   B 38  ? 0.2792 0.2144 0.307  -0.0004 0.0243  -0.0273 19  ASP   B CB  
2123 C CG  . ASP   B 38  ? 0.3875 0.3171 0.4225 0.005   0.0235  -0.0271 19  ASP   B CG  
2124 O OD1 . ASP   B 38  ? 0.4098 0.3385 0.4489 0.0101  0.0274  -0.0307 19  ASP   B OD1 
2125 O OD2 . ASP   B 38  ? 0.4062 0.3322 0.4427 0.0043  0.0192  -0.0236 19  ASP   B OD2 
2126 N N   . TYR   B 39  ? 0.2144 0.1755 0.2493 -0.0012 0.0272  -0.0234 20  TYR   B N   
2127 C CA  . TYR   B 39  ? 0.2083 0.1794 0.2502 0.0001  0.0271  -0.0205 20  TYR   B CA  
2128 C C   . TYR   B 39  ? 0.2109 0.1875 0.2557 0.0024  0.0317  -0.0223 20  TYR   B C   
2129 O O   . TYR   B 39  ? 0.2062 0.1879 0.2598 0.0054  0.0326  -0.0209 20  TYR   B O   
2130 C CB  . TYR   B 39  ? 0.1963 0.1723 0.2339 -0.0042 0.0247  -0.0183 20  TYR   B CB  
2131 C CG  . TYR   B 39  ? 0.1825 0.1668 0.2257 -0.0033 0.0239  -0.0155 20  TYR   B CG  
2132 C CD1 . TYR   B 39  ? 0.1689 0.1538 0.2177 -0.0016 0.021   -0.0129 20  TYR   B CD1 
2133 C CD2 . TYR   B 39  ? 0.1835 0.1742 0.2258 -0.0043 0.0254  -0.0154 20  TYR   B CD2 
2134 C CE1 . TYR   B 39  ? 0.1732 0.1646 0.2262 -0.0011 0.0196  -0.0106 20  TYR   B CE1 
2135 C CE2 . TYR   B 39  ? 0.1604 0.1575 0.2072 -0.0038 0.024   -0.0129 20  TYR   B CE2 
2136 C CZ  . TYR   B 39  ? 0.1678 0.165  0.2198 -0.0022 0.0212  -0.0107 20  TYR   B CZ  
2137 O OH  . TYR   B 39  ? 0.1743 0.1765 0.23   -0.0018 0.0196  -0.0086 20  TYR   B OH  
2138 N N   . LEU   B 40  ? 0.2236 0.1991 0.2605 0.0003  0.0346  -0.0251 21  LEU   B N   
2139 C CA  . LEU   B 40  ? 0.2323 0.2126 0.2699 0.0018  0.0396  -0.0267 21  LEU   B CA  
2140 C C   . LEU   B 40  ? 0.2404 0.2189 0.2843 0.0069  0.0436  -0.0292 21  LEU   B C   
2141 O O   . LEU   B 40  ? 0.2607 0.2464 0.3125 0.0094  0.0466  -0.0282 21  LEU   B O   
2142 C CB  . LEU   B 40  ? 0.2489 0.2266 0.2748 -0.0016 0.0411  -0.0293 21  LEU   B CB  
2143 C CG  . LEU   B 40  ? 0.2456 0.2275 0.267  -0.0061 0.0374  -0.0266 21  LEU   B CG  
2144 C CD1 . LEU   B 40  ? 0.2919 0.2707 0.3018 -0.0097 0.0379  -0.0291 21  LEU   B CD1 
2145 C CD2 . LEU   B 40  ? 0.2749 0.2661 0.3026 -0.0056 0.0374  -0.023  21  LEU   B CD2 
2146 N N   . GLU   B 41  ? 0.243  0.2119 0.2844 0.0085  0.0433  -0.032  22  GLU   B N   
2147 C CA  . GLU   B 41  ? 0.2642 0.2308 0.3125 0.0142  0.0469  -0.0347 22  GLU   B CA  
2148 C C   . GLU   B 41  ? 0.2679 0.2404 0.3305 0.0179  0.045   -0.0312 22  GLU   B C   
2149 O O   . GLU   B 41  ? 0.2911 0.2688 0.3631 0.0223  0.0491  -0.0321 22  GLU   B O   
2150 C CB  . GLU   B 41  ? 0.3092 0.2627 0.3521 0.0153  0.0456  -0.0382 22  GLU   B CB  
2151 C CG  . GLU   B 41  ? 0.3873 0.3341 0.4168 0.0128  0.0483  -0.0429 22  GLU   B CG  
2152 C CD  . GLU   B 41  ? 0.4971 0.4474 0.5255 0.0156  0.0558  -0.0468 22  GLU   B CD  
2153 O OE1 . GLU   B 41  ? 0.5147 0.4667 0.5332 0.0119  0.0578  -0.048  22  GLU   B OE1 
2154 O OE2 . GLU   B 41  ? 0.5403 0.4922 0.5781 0.0215  0.0596  -0.0483 22  GLU   B OE2 
2155 N N   . LYS   B 42  ? 0.2485 0.2203 0.313  0.0161  0.0389  -0.0273 23  LYS   B N   
2156 C CA  . LYS   B 42  ? 0.2492 0.2251 0.3258 0.0192  0.036   -0.0239 23  LYS   B CA  
2157 C C   . LYS   B 42  ? 0.2418 0.2295 0.3259 0.0188  0.0368  -0.0211 23  LYS   B C   
2158 O O   . LYS   B 42  ? 0.2649 0.2579 0.3611 0.0222  0.0369  -0.0197 23  LYS   B O   
2159 C CB  . LYS   B 42  ? 0.2766 0.2473 0.3506 0.0169  0.0292  -0.0206 23  LYS   B CB  
2160 C CG  . LYS   B 42  ? 0.4108 0.3713 0.4862 0.0199  0.0267  -0.0212 23  LYS   B CG  
2161 C CD  . LYS   B 42  ? 0.477  0.4268 0.5415 0.0175  0.0266  -0.0239 23  LYS   B CD  
2162 C CE  . LYS   B 42  ? 0.5037 0.4432 0.5717 0.0219  0.0248  -0.0249 23  LYS   B CE  
2163 N NZ  . LYS   B 42  ? 0.5157 0.4461 0.577  0.0229  0.0284  -0.0303 23  LYS   B NZ  
2164 N N   . TYR   B 43  ? 0.2177 0.2092 0.2951 0.0144  0.0368  -0.02   24  TYR   B N   
2165 C CA  . TYR   B 43  ? 0.2077 0.2086 0.2912 0.0134  0.0365  -0.0169 24  TYR   B CA  
2166 C C   . TYR   B 43  ? 0.2144 0.2214 0.2964 0.0122  0.0418  -0.0177 24  TYR   B C   
2167 O O   . TYR   B 43  ? 0.222  0.2366 0.3114 0.0119  0.042   -0.0151 24  TYR   B O   
2168 C CB  . TYR   B 43  ? 0.1961 0.1967 0.2742 0.0096  0.0311  -0.014  24  TYR   B CB  
2169 C CG  . TYR   B 43  ? 0.1982 0.1947 0.2788 0.0104  0.0255  -0.0119 24  TYR   B CG  
2170 C CD1 . TYR   B 43  ? 0.1951 0.1955 0.2853 0.0121  0.0224  -0.009  24  TYR   B CD1 
2171 C CD2 . TYR   B 43  ? 0.1993 0.1879 0.2723 0.009   0.0232  -0.0124 24  TYR   B CD2 
2172 C CE1 . TYR   B 43  ? 0.1971 0.1932 0.2883 0.0127  0.0169  -0.0069 24  TYR   B CE1 
2173 C CE2 . TYR   B 43  ? 0.2009 0.1854 0.275  0.0093  0.0182  -0.01   24  TYR   B CE2 
2174 C CZ  . TYR   B 43  ? 0.2026 0.1905 0.2853 0.0113  0.015   -0.0073 24  TYR   B CZ  
2175 O OH  . TYR   B 43  ? 0.2134 0.1969 0.296  0.0114  0.0096  -0.0047 24  TYR   B OH  
2176 N N   . TYR   B 44  ? 0.2109 0.2143 0.283  0.011   0.0457  -0.0211 25  TYR   B N   
2177 C CA  . TYR   B 44  ? 0.232  0.2403 0.2995 0.0087  0.0499  -0.0212 25  TYR   B CA  
2178 C C   . TYR   B 44  ? 0.2741 0.2814 0.3381 0.0104  0.057   -0.0253 25  TYR   B C   
2179 O O   . TYR   B 44  ? 0.2765 0.2857 0.3329 0.0079  0.0604  -0.0259 25  TYR   B O   
2180 C CB  . TYR   B 44  ? 0.2259 0.2321 0.2821 0.004   0.0467  -0.0204 25  TYR   B CB  
2181 C CG  . TYR   B 44  ? 0.2047 0.2137 0.2646 0.0025  0.041   -0.0164 25  TYR   B CG  
2182 C CD1 . TYR   B 44  ? 0.2021 0.2177 0.2676 0.0019  0.0406  -0.0132 25  TYR   B CD1 
2183 C CD2 . TYR   B 44  ? 0.1899 0.1946 0.2477 0.0019  0.0362  -0.0159 25  TYR   B CD2 
2184 C CE1 . TYR   B 44  ? 0.2067 0.2239 0.2757 0.0011  0.0354  -0.0101 25  TYR   B CE1 
2185 C CE2 . TYR   B 44  ? 0.1887 0.1957 0.2495 0.0011  0.0316  -0.0127 25  TYR   B CE2 
2186 C CZ  . TYR   B 44  ? 0.1841 0.197  0.2504 0.0009  0.0311  -0.0101 25  TYR   B CZ  
2187 O OH  . TYR   B 44  ? 0.1903 0.2044 0.2587 0.0003  0.0265  -0.0076 25  TYR   B OH  
2188 N N   . LYS   B 45  ? 0.2849 0.2892 0.3545 0.015   0.0594  -0.0282 26  LYS   B N   
2189 C CA  . LYS   B 45  ? 0.3361 0.3392 0.4027 0.0176  0.0669  -0.0329 26  LYS   B CA  
2190 C C   . LYS   B 45  ? 0.3542 0.3682 0.428  0.0181  0.0728  -0.0315 26  LYS   B C   
2191 O O   . LYS   B 45  ? 0.3767 0.3914 0.4431 0.0176  0.0793  -0.0343 26  LYS   B O   
2192 C CB  . LYS   B 45  ? 0.3967 0.3938 0.4692 0.0232  0.0674  -0.0362 26  LYS   B CB  
2193 C CG  . LYS   B 45  ? 0.4908 0.4818 0.5557 0.0258  0.074   -0.0425 26  LYS   B CG  
2194 C CD  . LYS   B 45  ? 0.5804 0.5616 0.648  0.0306  0.0726  -0.0458 26  LYS   B CD  
2195 C CE  . LYS   B 45  ? 0.6504 0.6235 0.7081 0.033   0.0787  -0.0528 26  LYS   B CE  
2196 N NZ  . LYS   B 45  ? 0.7029 0.6617 0.7565 0.0352  0.0752  -0.0561 26  LYS   B NZ  
2197 N N   . PHE   B 46  ? 0.35   0.3725 0.4374 0.0186  0.0706  -0.0271 27  PHE   B N   
2198 C CA  . PHE   B 46  ? 0.3535 0.3873 0.4491 0.0179  0.0753  -0.0246 27  PHE   B CA  
2199 C C   . PHE   B 46  ? 0.3787 0.4163 0.4787 0.022   0.0844  -0.0284 27  PHE   B C   
2200 O O   . PHE   B 46  ? 0.3898 0.4324 0.4856 0.0201  0.0909  -0.0287 27  PHE   B O   
2201 C CB  . PHE   B 46  ? 0.3496 0.3847 0.4343 0.012   0.0751  -0.0221 27  PHE   B CB  
2202 C CG  . PHE   B 46  ? 0.3411 0.3862 0.434  0.0094  0.0758  -0.0172 27  PHE   B CG  
2203 C CD1 . PHE   B 46  ? 0.3477 0.3972 0.4533 0.0095  0.0703  -0.0132 27  PHE   B CD1 
2204 C CD2 . PHE   B 46  ? 0.3472 0.3962 0.4336 0.006   0.0811  -0.0162 27  PHE   B CD2 
2205 C CE1 . PHE   B 46  ? 0.354  0.4114 0.4663 0.0063  0.0701  -0.0086 27  PHE   B CE1 
2206 C CE2 . PHE   B 46  ? 0.3594 0.4164 0.4526 0.0028  0.0811  -0.0111 27  PHE   B CE2 
2207 C CZ  . PHE   B 46  ? 0.3595 0.4206 0.466  0.0029  0.0755  -0.0075 27  PHE   B CZ  
2208 N N   . GLY   B 47  ? 0.3855 0.4202 0.4932 0.0278  0.0849  -0.0315 28  GLY   B N   
2209 C CA  . GLY   B 47  ? 0.3979 0.4362 0.5118 0.0331  0.0936  -0.0357 28  GLY   B CA  
2210 C C   . GLY   B 47  ? 0.414  0.4673 0.5463 0.0346  0.0975  -0.0325 28  GLY   B C   
2211 O O   . GLY   B 47  ? 0.4017 0.4619 0.5411 0.031   0.0931  -0.0269 28  GLY   B O   
2212 N N   . HIS   B 50  ? 0.4333 0.521  0.6446 0.0426  0.08    -0.0166 31  HIS   B N   
2213 C CA  . HIS   B 50  ? 0.4212 0.5143 0.6399 0.0379  0.0723  -0.0105 31  HIS   B CA  
2214 C C   . HIS   B 50  ? 0.4121 0.4949 0.6273 0.038   0.0609  -0.0087 31  HIS   B C   
2215 O O   . HIS   B 50  ? 0.4344 0.5215 0.6626 0.0384  0.0541  -0.005  31  HIS   B O   
2216 C CB  . HIS   B 50  ? 0.431  0.54   0.6732 0.0397  0.0741  -0.0076 31  HIS   B CB  
2217 C CG  . HIS   B 50  ? 0.4744 0.5947 0.7224 0.0407  0.0862  -0.0095 31  HIS   B CG  
2218 N ND1 . HIS   B 50  ? 0.4984 0.6268 0.7623 0.0479  0.0924  -0.0124 31  HIS   B ND1 
2219 C CD2 . HIS   B 50  ? 0.4902 0.6146 0.7296 0.0356  0.0931  -0.009  31  HIS   B CD2 
2220 C CE1 . HIS   B 50  ? 0.4969 0.6348 0.7614 0.0467  0.1034  -0.0136 31  HIS   B CE1 
2221 N NE2 . HIS   B 50  ? 0.4988 0.6343 0.7482 0.0391  0.1041  -0.0114 31  HIS   B NE2 
2222 N N   . SER   B 51  ? 0.3705 0.4401 0.5675 0.0367  0.0587  -0.011  32  SER   B N   
2223 C CA  . SER   B 51  ? 0.3276 0.3873 0.5198 0.0366  0.0491  -0.0095 32  SER   B CA  
2224 C C   . SER   B 51  ? 0.2883 0.3481 0.4761 0.0307  0.0424  -0.0052 32  SER   B C   
2225 O O   . SER   B 51  ? 0.2588 0.3225 0.4419 0.0262  0.045   -0.0041 32  SER   B O   
2226 C CB  . SER   B 51  ? 0.3387 0.3849 0.5138 0.037   0.0496  -0.0134 32  SER   B CB  
2227 O OG  . SER   B 51  ? 0.3362 0.3804 0.4964 0.0316  0.0518  -0.0138 32  SER   B OG  
2228 N N   . ALA   B 52  ? 0.269  0.3229 0.4564 0.0305  0.0334  -0.0029 33  ALA   B N   
2229 C CA  . ALA   B 52  ? 0.2465 0.2988 0.4279 0.0254  0.0269  0.0005  33  ALA   B CA  
2230 C C   . ALA   B 52  ? 0.2273 0.2735 0.3908 0.0215  0.0291  -0.0012 33  ALA   B C   
2231 O O   . ALA   B 52  ? 0.23   0.2785 0.3899 0.0174  0.0283  0.0007  33  ALA   B O   
2232 C CB  . ALA   B 52  ? 0.2593 0.3048 0.4404 0.0263  0.0179  0.0024  33  ALA   B CB  
2233 N N   . GLU   B 53  ? 0.2287 0.2668 0.3817 0.023   0.0316  -0.0046 34  GLU   B N   
2234 C CA  . GLU   B 53  ? 0.2291 0.2619 0.3658 0.0194  0.0334  -0.0062 34  GLU   B CA  
2235 C C   . GLU   B 53  ? 0.236  0.275  0.371  0.017   0.0396  -0.0066 34  GLU   B C   
2236 O O   . GLU   B 53  ? 0.2392 0.2776 0.3659 0.013   0.0384  -0.0053 34  GLU   B O   
2237 C CB  . GLU   B 53  ? 0.244  0.2679 0.3717 0.0213  0.0354  -0.01   34  GLU   B CB  
2238 C CG  . GLU   B 53  ? 0.2658 0.2812 0.3903 0.022   0.0288  -0.0091 34  GLU   B CG  
2239 C CD  . GLU   B 53  ? 0.2887 0.3057 0.4261 0.0253  0.0242  -0.0068 34  GLU   B CD  
2240 O OE1 . GLU   B 53  ? 0.2924 0.3125 0.4405 0.0298  0.0273  -0.0082 34  GLU   B OE1 
2241 O OE2 . GLU   B 53  ? 0.2686 0.2839 0.4055 0.0237  0.0174  -0.0037 34  GLU   B OE2 
2242 N N   . SER   B 54  ? 0.2447 0.2901 0.3878 0.0195  0.0463  -0.0081 35  SER   B N   
2243 C CA  . SER   B 54  ? 0.2494 0.3009 0.3901 0.0168  0.0526  -0.0079 35  SER   B CA  
2244 C C   . SER   B 54  ? 0.2458 0.3051 0.3945 0.0134  0.0502  -0.0033 35  SER   B C   
2245 O O   . SER   B 54  ? 0.2473 0.3079 0.3893 0.0093  0.0517  -0.0019 35  SER   B O   
2246 C CB  . SER   B 54  ? 0.2677 0.3237 0.4135 0.0204  0.0613  -0.0112 35  SER   B CB  
2247 O OG  . SER   B 54  ? 0.3625 0.409  0.4973 0.0226  0.0631  -0.0158 35  SER   B OG  
2248 N N   . GLN   B 55  ? 0.2331 0.2968 0.3957 0.0147  0.0456  -0.0007 36  GLN   B N   
2249 C CA  . GLN   B 55  ? 0.2287 0.2989 0.3989 0.0109  0.0422  0.0038  36  GLN   B CA  
2250 C C   . GLN   B 55  ? 0.225  0.2879 0.383  0.007   0.0361  0.0053  36  GLN   B C   
2251 O O   . GLN   B 55  ? 0.2333 0.2984 0.3896 0.0029  0.0358  0.0078  36  GLN   B O   
2252 C CB  . GLN   B 55  ? 0.2589 0.3342 0.4458 0.013   0.0372  0.0061  36  GLN   B CB  
2253 C CG  . GLN   B 55  ? 0.3228 0.4081 0.5254 0.017   0.0435  0.0052  36  GLN   B CG  
2254 C CD  . GLN   B 55  ? 0.4176 0.5128 0.6245 0.0139  0.0508  0.0066  36  GLN   B CD  
2255 O OE1 . GLN   B 55  ? 0.4685 0.5647 0.6696 0.0149  0.0594  0.0037  36  GLN   B OE1 
2256 N NE2 . GLN   B 55  ? 0.443  0.5447 0.6584 0.0096  0.0474  0.0111  36  GLN   B NE2 
2257 N N   . ILE   B 56  ? 0.2273 0.2814 0.377  0.0083  0.0313  0.0038  37  ILE   B N   
2258 C CA  . ILE   B 56  ? 0.2227 0.2705 0.3611 0.0052  0.0262  0.0046  37  ILE   B CA  
2259 C C   . ILE   B 56  ? 0.2175 0.2634 0.3441 0.0029  0.0304  0.0034  37  ILE   B C   
2260 O O   . ILE   B 56  ? 0.2226 0.268  0.345  -0.0002 0.0282  0.0054  37  ILE   B O   
2261 C CB  . ILE   B 56  ? 0.2438 0.2838 0.3767 0.0071  0.0212  0.0034  37  ILE   B CB  
2262 C CG1 . ILE   B 56  ? 0.2511 0.2925 0.3942 0.0082  0.0151  0.0057  37  ILE   B CG1 
2263 C CG2 . ILE   B 56  ? 0.2529 0.2869 0.3726 0.0046  0.0181  0.0032  37  ILE   B CG2 
2264 C CD1 . ILE   B 56  ? 0.2684 0.3028 0.4079 0.0105  0.011   0.0049  37  ILE   B CD1 
2265 N N   . LEU   B 57  ? 0.212  0.2567 0.3336 0.0045  0.0361  0.0003  38  LEU   B N   
2266 C CA  . LEU   B 57  ? 0.2098 0.2528 0.3196 0.0021  0.0399  -0.0007 38  LEU   B CA  
2267 C C   . LEU   B 57  ? 0.213  0.2622 0.3255 -0.0012 0.0427  0.0022  38  LEU   B C   
2268 O O   . LEU   B 57  ? 0.2199 0.2671 0.3249 -0.0043 0.0409  0.0039  38  LEU   B O   
2269 C CB  . LEU   B 57  ? 0.2133 0.2534 0.3172 0.0042  0.0453  -0.0048 38  LEU   B CB  
2270 C CG  . LEU   B 57  ? 0.2392 0.2773 0.3303 0.0015  0.049   -0.0061 38  LEU   B CG  
2271 C CD1 . LEU   B 57  ? 0.227  0.2605 0.3082 -0.0014 0.0436  -0.0048 38  LEU   B CD1 
2272 C CD2 . LEU   B 57  ? 0.2704 0.3038 0.355  0.0036  0.053   -0.0106 38  LEU   B CD2 
2273 N N   . LYS   B 58  ? 0.2266 0.2836 0.3512 -0.0004 0.0465  0.0033  39  LYS   B N   
2274 C CA  . LYS   B 58  ? 0.2224 0.2857 0.3505 -0.0042 0.0492  0.0068  39  LYS   B CA  
2275 C C   . LYS   B 58  ? 0.2194 0.2812 0.3486 -0.0074 0.0421  0.0106  39  LYS   B C   
2276 O O   . LYS   B 58  ? 0.2115 0.2725 0.3348 -0.0112 0.0422  0.013   39  LYS   B O   
2277 C CB  . LYS   B 58  ? 0.2414 0.3148 0.3847 -0.0027 0.0544  0.0075  39  LYS   B CB  
2278 C CG  . LYS   B 58  ? 0.3064 0.3814 0.4475 0.0005  0.0628  0.0034  39  LYS   B CG  
2279 C CD  . LYS   B 58  ? 0.354  0.4404 0.5127 0.0028  0.068   0.004   39  LYS   B CD  
2280 C CE  . LYS   B 58  ? 0.4343 0.5203 0.594  0.0084  0.074   -0.0011 39  LYS   B CE  
2281 N NZ  . LYS   B 58  ? 0.4779 0.5756 0.6566 0.0117  0.0787  -0.0008 39  LYS   B NZ  
2282 N N   . HIS   B 59  ? 0.2204 0.2807 0.3562 -0.006  0.0356  0.0111  40  HIS   B N   
2283 C CA  . HIS   B 59  ? 0.2442 0.3017 0.3798 -0.0089 0.0286  0.014   40  HIS   B CA  
2284 C C   . HIS   B 59  ? 0.242  0.2914 0.3632 -0.01   0.0258  0.0133  40  HIS   B C   
2285 O O   . HIS   B 59  ? 0.2577 0.3055 0.376  -0.0131 0.0235  0.0158  40  HIS   B O   
2286 C CB  . HIS   B 59  ? 0.3001 0.3569 0.4439 -0.0075 0.0219  0.0147  40  HIS   B CB  
2287 C CG  . HIS   B 59  ? 0.4261 0.4817 0.572  -0.0113 0.0161  0.018   40  HIS   B CG  
2288 N ND1 . HIS   B 59  ? 0.4781 0.5409 0.6357 -0.0143 0.0166  0.0215  40  HIS   B ND1 
2289 C CD2 . HIS   B 59  ? 0.4642 0.5122 0.6013 -0.0126 0.0105  0.0182  40  HIS   B CD2 
2290 C CE1 . HIS   B 59  ? 0.4946 0.5528 0.6498 -0.0176 0.0107  0.0237  40  HIS   B CE1 
2291 N NE2 . HIS   B 59  ? 0.4905 0.5395 0.6333 -0.0164 0.0069  0.0216  40  HIS   B NE2 
2292 N N   . LEU   B 60  ? 0.2247 0.2693 0.3375 -0.0075 0.026   0.01    41  LEU   B N   
2293 C CA  . LEU   B 60  ? 0.2175 0.2561 0.3181 -0.0083 0.0238  0.0092  41  LEU   B CA  
2294 C C   . LEU   B 60  ? 0.1918 0.2313 0.2861 -0.0111 0.0274  0.0105  41  LEU   B C   
2295 O O   . LEU   B 60  ? 0.2086 0.2449 0.298  -0.0129 0.024   0.0123  41  LEU   B O   
2296 C CB  . LEU   B 60  ? 0.2279 0.2627 0.3217 -0.0058 0.0245  0.0056  41  LEU   B CB  
2297 C CG  . LEU   B 60  ? 0.2675 0.3    0.3648 -0.0034 0.0204  0.0047  41  LEU   B CG  
2298 C CD1 . LEU   B 60  ? 0.2643 0.2929 0.3551 -0.0016 0.0217  0.0016  41  LEU   B CD1 
2299 C CD2 . LEU   B 60  ? 0.328  0.3567 0.4224 -0.0042 0.0142  0.0058  41  LEU   B CD2 
2300 N N   . LEU   B 61  ? 0.2002 0.2437 0.2949 -0.0111 0.0342  0.0097  42  LEU   B N   
2301 C CA  . LEU   B 61  ? 0.2025 0.2464 0.2896 -0.0141 0.0377  0.0111  42  LEU   B CA  
2302 C C   . LEU   B 61  ? 0.2025 0.2488 0.2939 -0.0178 0.0364  0.0158  42  LEU   B C   
2303 O O   . LEU   B 61  ? 0.2009 0.2439 0.2846 -0.0204 0.0348  0.018   42  LEU   B O   
2304 C CB  . LEU   B 61  ? 0.2025 0.25   0.2884 -0.0134 0.0456  0.0089  42  LEU   B CB  
2305 C CG  . LEU   B 61  ? 0.2171 0.2603 0.2959 -0.0105 0.0468  0.0042  42  LEU   B CG  
2306 C CD1 . LEU   B 61  ? 0.2484 0.2945 0.3277 -0.0089 0.0546  0.0013  42  LEU   B CD1 
2307 C CD2 . LEU   B 61  ? 0.2189 0.2565 0.2843 -0.0122 0.0443  0.0038  42  LEU   B CD2 
2308 N N   . LYS   B 62  ? 0.2025 0.254  0.3066 -0.0182 0.0363  0.0177  43  LYS   B N   
2309 C CA  . LYS   B 62  ? 0.2097 0.263  0.3185 -0.0225 0.0344  0.0225  43  LYS   B CA  
2310 C C   . LYS   B 62  ? 0.2201 0.2659 0.3248 -0.0234 0.0263  0.0239  43  LYS   B C   
2311 O O   . LYS   B 62  ? 0.2346 0.2774 0.3351 -0.0268 0.0246  0.0271  43  LYS   B O   
2312 C CB  . LYS   B 62  ? 0.2244 0.2855 0.3489 -0.023  0.0354  0.0242  43  LYS   B CB  
2313 C CG  . LYS   B 62  ? 0.2419 0.3116 0.3716 -0.0223 0.0442  0.0233  43  LYS   B CG  
2314 C CD  . LYS   B 62  ? 0.2939 0.3725 0.4413 -0.0225 0.0444  0.0253  43  LYS   B CD  
2315 C CE  . LYS   B 62  ? 0.371  0.4544 0.5265 -0.0173 0.048   0.0217  43  LYS   B CE  
2316 N NZ  . LYS   B 62  ? 0.3818 0.4754 0.5562 -0.0175 0.0481  0.024   43  LYS   B NZ  
2317 N N   . ASN   B 63  ? 0.2254 0.2672 0.3302 -0.0201 0.0214  0.0212  44  ASN   B N   
2318 C CA  . ASN   B 63  ? 0.2383 0.2727 0.3383 -0.0203 0.0143  0.0216  44  ASN   B CA  
2319 C C   . ASN   B 63  ? 0.2244 0.2538 0.3125 -0.0201 0.0139  0.0211  44  ASN   B C   
2320 O O   . ASN   B 63  ? 0.2404 0.2648 0.325  -0.0215 0.0098  0.0231  44  ASN   B O   
2321 C CB  . ASN   B 63  ? 0.2983 0.3299 0.4    -0.017  0.0099  0.0188  44  ASN   B CB  
2322 C CG  . ASN   B 63  ? 0.4038 0.437  0.5158 -0.018  0.006   0.0204  44  ASN   B CG  
2323 O OD1 . ASN   B 63  ? 0.4313 0.4683 0.5508 -0.0214 0.0065  0.0238  44  ASN   B OD1 
2324 N ND2 . ASN   B 63  ? 0.4278 0.4579 0.5402 -0.0156 0.0017  0.0183  44  ASN   B ND2 
2325 N N   . LEU   B 64  ? 0.2116 0.242  0.2936 -0.0183 0.0179  0.0183  45  LEU   B N   
2326 C CA  . LEU   B 64  ? 0.2131 0.2397 0.2844 -0.0183 0.0172  0.018   45  LEU   B CA  
2327 C C   . LEU   B 64  ? 0.2145 0.241  0.2822 -0.0222 0.0187  0.022   45  LEU   B C   
2328 O O   . LEU   B 64  ? 0.2421 0.2638 0.3037 -0.0229 0.015   0.0236  45  LEU   B O   
2329 C CB  . LEU   B 64  ? 0.2163 0.244  0.2821 -0.0164 0.0209  0.0144  45  LEU   B CB  
2330 C CG  . LEU   B 64  ? 0.2225 0.2491 0.29   -0.0131 0.0187  0.0111  45  LEU   B CG  
2331 C CD1 . LEU   B 64  ? 0.2374 0.2655 0.3025 -0.0119 0.0233  0.0079  45  LEU   B CD1 
2332 C CD2 . LEU   B 64  ? 0.2353 0.2578 0.2974 -0.0119 0.0139  0.0103  45  LEU   B CD2 
2333 N N   . PHE   B 65  ? 0.2272 0.2591 0.299  -0.0246 0.0242  0.0237  46  PHE   B N   
2334 C CA  . PHE   B 65  ? 0.2655 0.2974 0.3333 -0.029  0.0262  0.028   46  PHE   B CA  
2335 C C   . PHE   B 65  ? 0.2498 0.2777 0.3214 -0.0315 0.0202  0.0321  46  PHE   B C   
2336 O O   . PHE   B 65  ? 0.2635 0.2861 0.3281 -0.0334 0.0173  0.0349  46  PHE   B O   
2337 C CB  . PHE   B 65  ? 0.2903 0.3299 0.3628 -0.0308 0.0341  0.0286  46  PHE   B CB  
2338 C CG  . PHE   B 65  ? 0.3435 0.3842 0.4133 -0.0361 0.0366  0.0338  46  PHE   B CG  
2339 C CD1 . PHE   B 65  ? 0.3844 0.4204 0.4411 -0.0383 0.0366  0.0355  46  PHE   B CD1 
2340 C CD2 . PHE   B 65  ? 0.3743 0.4201 0.4547 -0.0394 0.0381  0.0374  46  PHE   B CD2 
2341 C CE1 . PHE   B 65  ? 0.4121 0.4482 0.4652 -0.0436 0.0385  0.0409  46  PHE   B CE1 
2342 C CE2 . PHE   B 65  ? 0.4004 0.447  0.478  -0.0449 0.0405  0.0427  46  PHE   B CE2 
2343 C CZ  . PHE   B 65  ? 0.4053 0.4465 0.4688 -0.047  0.0404  0.0445  46  PHE   B CZ  
2344 N N   . LYS   B 66  ? 0.2269 0.2559 0.3088 -0.0308 0.0173  0.0318  47  LYS   B N   
2345 C CA  . LYS   B 66  ? 0.2553 0.279  0.3403 -0.0331 0.0108  0.0351  47  LYS   B CA  
2346 C C   . LYS   B 66  ? 0.2652 0.2796 0.3422 -0.0309 0.0044  0.0342  47  LYS   B C   
2347 O O   . LYS   B 66  ? 0.2876 0.2957 0.3622 -0.0333 0       0.0375  47  LYS   B O   
2348 C CB  . LYS   B 66  ? 0.2665 0.2923 0.3628 -0.0326 0.008   0.0343  47  LYS   B CB  
2349 C CG  . LYS   B 66  ? 0.3434 0.3652 0.4444 -0.0367 0.0026  0.0383  47  LYS   B CG  
2350 C CD  . LYS   B 66  ? 0.3849 0.4105 0.4978 -0.0371 0.0004  0.0381  47  LYS   B CD  
2351 C CE  . LYS   B 66  ? 0.4569 0.4752 0.5678 -0.0336 -0.0067 0.0347  47  LYS   B CE  
2352 N NZ  . LYS   B 66  ? 0.479  0.5011 0.6008 -0.0339 -0.0093 0.0343  47  LYS   B NZ  
2353 N N   . ILE   B 67  ? 0.2514 0.2649 0.3248 -0.0263 0.0037  0.0297  48  ILE   B N   
2354 C CA  . ILE   B 67  ? 0.2501 0.2565 0.3173 -0.0235 -0.0017 0.0284  48  ILE   B CA  
2355 C C   . ILE   B 67  ? 0.2721 0.2762 0.3304 -0.0242 -0.0015 0.0301  48  ILE   B C   
2356 O O   . ILE   B 67  ? 0.2997 0.2972 0.3543 -0.0237 -0.0065 0.0317  48  ILE   B O   
2357 C CB  . ILE   B 67  ? 0.2498 0.2576 0.317  -0.0189 -0.0018 0.0233  48  ILE   B CB  
2358 C CG1 . ILE   B 67  ? 0.2416 0.2497 0.3161 -0.0181 -0.0037 0.0219  48  ILE   B CG1 
2359 C CG2 . ILE   B 67  ? 0.2566 0.2599 0.3177 -0.0155 -0.0054 0.0212  48  ILE   B CG2 
2360 C CD1 . ILE   B 67  ? 0.2439 0.2544 0.3184 -0.0146 -0.0025 0.0176  48  ILE   B CD1 
2361 N N   . PHE   B 68  ? 0.2691 0.2782 0.3234 -0.025  0.0041  0.0296  49  PHE   B N   
2362 C CA  . PHE   B 68  ? 0.2997 0.3066 0.3443 -0.0254 0.0037  0.0308  49  PHE   B CA  
2363 C C   . PHE   B 68  ? 0.3634 0.3694 0.4032 -0.0303 0.0055  0.0359  49  PHE   B C   
2364 O O   . PHE   B 68  ? 0.3848 0.3858 0.4174 -0.031  0.002   0.0385  49  PHE   B O   
2365 C CB  . PHE   B 68  ? 0.2856 0.2966 0.3259 -0.0235 0.0073  0.027   49  PHE   B CB  
2366 C CG  . PHE   B 68  ? 0.2601 0.2711 0.3029 -0.0191 0.0048  0.0227  49  PHE   B CG  
2367 C CD1 . PHE   B 68  ? 0.2485 0.2557 0.2896 -0.0165 -0.0006 0.0224  49  PHE   B CD1 
2368 C CD2 . PHE   B 68  ? 0.2582 0.2732 0.3049 -0.0175 0.0081  0.0191  49  PHE   B CD2 
2369 C CE1 . PHE   B 68  ? 0.2379 0.246  0.2814 -0.0127 -0.0021 0.0186  49  PHE   B CE1 
2370 C CE2 . PHE   B 68  ? 0.2669 0.2818 0.315  -0.014  0.0061  0.0157  49  PHE   B CE2 
2371 C CZ  . PHE   B 68  ? 0.2366 0.2485 0.2831 -0.0118 0.0013  0.0154  49  PHE   B CZ  
2372 N N   . CYS   B 69  ? 0.4071 0.4183 0.4504 -0.0334 0.0113  0.0372  50  CYS   B N   
2373 C CA  . CYS   B 69  ? 0.4463 0.4575 0.484  -0.0385 0.0143  0.042   50  CYS   B CA  
2374 C C   . CYS   B 69  ? 0.5024 0.5112 0.5459 -0.0423 0.0118  0.0469  50  CYS   B C   
2375 O O   . CYS   B 69  ? 0.5394 0.5411 0.5775 -0.0445 0.007   0.051   50  CYS   B O   
2376 C CB  . CYS   B 69  ? 0.4453 0.4637 0.4808 -0.0398 0.0229  0.0405  50  CYS   B CB  
2377 S SG  . CYS   B 69  ? 0.4538 0.4728 0.4805 -0.0361 0.0249  0.0348  50  CYS   B SG  
2378 N N   . LEU   B 70  ? 0.5144 0.5276 0.5695 -0.0426 0.013   0.0462  51  LEU   B N   
2379 C CA  . LEU   B 70  ? 0.5357 0.546  0.5972 -0.0464 0.0093  0.0506  51  LEU   B CA  
2380 C C   . LEU   B 70  ? 0.5733 0.5725 0.6319 -0.0447 0.0001  0.0512  51  LEU   B C   
2381 O O   . LEU   B 70  ? 0.5966 0.5915 0.6481 -0.0407 -0.0028 0.0487  51  LEU   B O   
2382 C CB  . LEU   B 70  ? 0.5369 0.5536 0.6118 -0.0463 0.0106  0.0492  51  LEU   B CB  
2383 C CG  . LEU   B 70  ? 0.5599 0.588  0.6415 -0.0482 0.0193  0.0493  51  LEU   B CG  
2384 C CD1 . LEU   B 70  ? 0.5694 0.6031 0.6655 -0.048  0.0185  0.0486  51  LEU   B CD1 
2385 C CD2 . LEU   B 70  ? 0.578  0.6085 0.6564 -0.0545 0.0238  0.0551  51  LEU   B CD2 
2386 N N   . GLY   B 72  ? 0.4646 0.4425 0.506  -0.0336 -0.0164 0.0476  53  GLY   B N   
2387 C CA  . GLY   B 72  ? 0.4483 0.4253 0.4948 -0.0286 -0.0191 0.0424  53  GLY   B CA  
2388 C C   . GLY   B 72  ? 0.4354 0.4117 0.4778 -0.0228 -0.0212 0.0387  53  GLY   B C   
2389 O O   . GLY   B 72  ? 0.4529 0.4232 0.4908 -0.0215 -0.0257 0.0405  53  GLY   B O   
2390 N N   . VAL   B 73  ? 0.383  0.3659 0.4274 -0.0197 -0.0178 0.0338  54  VAL   B N   
2391 C CA  . VAL   B 73  ? 0.3604 0.3445 0.4024 -0.0147 -0.0192 0.0303  54  VAL   B CA  
2392 C C   . VAL   B 73  ? 0.3514 0.3387 0.387  -0.016  -0.0174 0.0319  54  VAL   B C   
2393 O O   . VAL   B 73  ? 0.3496 0.342  0.3831 -0.019  -0.0121 0.0322  54  VAL   B O   
2394 C CB  . VAL   B 73  ? 0.3495 0.3388 0.3954 -0.0116 -0.0166 0.0249  54  VAL   B CB  
2395 C CG1 . VAL   B 73  ? 0.3535 0.3444 0.3979 -0.0068 -0.018  0.0215  54  VAL   B CG1 
2396 C CG2 . VAL   B 73  ? 0.354  0.3399 0.405  -0.011  -0.0187 0.0236  54  VAL   B CG2 
2397 N N   . LYS   B 74  ? 0.3448 0.3285 0.3769 -0.0136 -0.022  0.0328  55  LYS   B N   
2398 C CA  . LYS   B 74  ? 0.3565 0.3421 0.3819 -0.0149 -0.022  0.0348  55  LYS   B CA  
2399 C C   . LYS   B 74  ? 0.3468 0.332  0.3726 -0.0099 -0.027  0.0332  55  LYS   B C   
2400 O O   . LYS   B 74  ? 0.3685 0.3512 0.3994 -0.0053 -0.0301 0.0309  55  LYS   B O   
2401 C CB  . LYS   B 74  ? 0.4106 0.3904 0.4304 -0.0196 -0.0236 0.041   55  LYS   B CB  
2402 C CG  . LYS   B 74  ? 0.4717 0.4421 0.4929 -0.0178 -0.0307 0.0437  55  LYS   B CG  
2403 C CD  . LYS   B 74  ? 0.5717 0.5352 0.5881 -0.0232 -0.0324 0.0503  55  LYS   B CD  
2404 C CE  . LYS   B 74  ? 0.6474 0.6019 0.6684 -0.0224 -0.0374 0.0515  55  LYS   B CE  
2405 N NZ  . LYS   B 74  ? 0.6943 0.6433 0.7129 -0.0291 -0.0375 0.0577  55  LYS   B NZ  
2406 N N   . GLY   B 75  ? 0.3189 0.3069 0.3394 -0.0107 -0.0276 0.0343  56  GLY   B N   
2407 C CA  . GLY   B 75  ? 0.3114 0.3004 0.3337 -0.0062 -0.0325 0.0334  56  GLY   B CA  
2408 C C   . GLY   B 75  ? 0.3098 0.3047 0.328  -0.0073 -0.0323 0.033   56  GLY   B C   
2409 O O   . GLY   B 75  ? 0.3315 0.328  0.343  -0.0119 -0.0286 0.034   56  GLY   B O   
2410 N N   . ASP   B 76  ? 0.2825 0.2806 0.3048 -0.003  -0.0361 0.0315  57  ASP   B N   
2411 C CA  . ASP   B 76  ? 0.2944 0.2984 0.3141 -0.004  -0.0373 0.0313  57  ASP   B CA  
2412 C C   . ASP   B 76  ? 0.2656 0.2775 0.2881 -0.0042 -0.032  0.0263  57  ASP   B C   
2413 O O   . ASP   B 76  ? 0.3063 0.3216 0.3238 -0.0074 -0.0309 0.026   57  ASP   B O   
2414 C CB  . ASP   B 76  ? 0.3474 0.353  0.3725 0.001   -0.0441 0.0319  57  ASP   B CB  
2415 C CG  . ASP   B 76  ? 0.4642 0.4618 0.4851 0.0009  -0.0508 0.0375  57  ASP   B CG  
2416 O OD1 . ASP   B 76  ? 0.4641 0.4556 0.4759 -0.0043 -0.05   0.0415  57  ASP   B OD1 
2417 O OD2 . ASP   B 76  ? 0.5275 0.525  0.5543 0.006   -0.0566 0.0381  57  ASP   B OD2 
2418 N N   . LEU   B 77  ? 0.2167 0.2307 0.2465 -0.0009 -0.0292 0.0225  58  LEU   B N   
2419 C CA  . LEU   B 77  ? 0.2022 0.2232 0.2346 -0.0012 -0.0249 0.0184  58  LEU   B CA  
2420 C C   . LEU   B 77  ? 0.1785 0.1984 0.2138 -0.0006 -0.0203 0.0156  58  LEU   B C   
2421 O O   . LEU   B 77  ? 0.183  0.2003 0.2227 0.0028  -0.0213 0.0147  58  LEU   B O   
2422 C CB  . LEU   B 77  ? 0.2042 0.2319 0.2439 0.003   -0.0277 0.0164  58  LEU   B CB  
2423 C CG  . LEU   B 77  ? 0.2249 0.26   0.2681 0.0028  -0.0236 0.0124  58  LEU   B CG  
2424 C CD1 . LEU   B 77  ? 0.2548 0.2923 0.2923 -0.0022 -0.0219 0.0123  58  LEU   B CD1 
2425 C CD2 . LEU   B 77  ? 0.2313 0.2742 0.283  0.007   -0.0257 0.0107  58  LEU   B CD2 
2426 N N   . LEU   B 78  ? 0.1696 0.1917 0.2024 -0.0037 -0.0155 0.0139  59  LEU   B N   
2427 C CA  . LEU   B 78  ? 0.1667 0.1889 0.2024 -0.0034 -0.0112 0.0112  59  LEU   B CA  
2428 C C   . LEU   B 78  ? 0.1673 0.1953 0.2044 -0.0035 -0.0088 0.008   59  LEU   B C   
2429 O O   . LEU   B 78  ? 0.1752 0.2055 0.2083 -0.0063 -0.0084 0.008   59  LEU   B O   
2430 C CB  . LEU   B 78  ? 0.1922 0.2113 0.2244 -0.0069 -0.0076 0.0124  59  LEU   B CB  
2431 C CG  . LEU   B 78  ? 0.1903 0.2098 0.2262 -0.0065 -0.0037 0.0099  59  LEU   B CG  
2432 C CD1 . LEU   B 78  ? 0.2246 0.2405 0.2612 -0.0083 -0.0023 0.0121  59  LEU   B CD1 
2433 C CD2 . LEU   B 78  ? 0.1989 0.2216 0.233  -0.0082 0.0001  0.0075  59  LEU   B CD2 
2434 N N   . ILE   B 79  ? 0.1571 0.187  0.1988 -0.0011 -0.0075 0.0054  60  ILE   B N   
2435 C CA  . ILE   B 79  ? 0.1628 0.1974 0.2055 -0.0019 -0.0049 0.0028  60  ILE   B CA  
2436 C C   . ILE   B 79  ? 0.1752 0.2071 0.2176 -0.0028 -0.0012 0.0015  60  ILE   B C   
2437 O O   . ILE   B 79  ? 0.1668 0.1959 0.2115 -0.0008 -0.0014 0.0013  60  ILE   B O   
2438 C CB  . ILE   B 79  ? 0.1601 0.1998 0.2082 0.0015  -0.0059 0.0011  60  ILE   B CB  
2439 C CG1 . ILE   B 79  ? 0.1949 0.2385 0.2453 0.0031  -0.0099 0.0024  60  ILE   B CG1 
2440 C CG2 . ILE   B 79  ? 0.1747 0.2189 0.2231 -0.0005 -0.0028 -0.001  60  ILE   B CG2 
2441 C CD1 . ILE   B 79  ? 0.2047 0.2538 0.2618 0.0076  -0.0105 0.0006  60  ILE   B CD1 
2442 N N   . ASP   B 80  ? 0.1588 0.1909 0.1984 -0.0057 0.0016  0.0006  61  ASP   B N   
2443 C CA  . ASP   B 80  ? 0.1487 0.1784 0.1887 -0.0063 0.0048  -0.0006 61  ASP   B CA  
2444 C C   . ASP   B 80  ? 0.1616 0.1939 0.2028 -0.0061 0.0058  -0.0026 61  ASP   B C   
2445 O O   . ASP   B 80  ? 0.1765 0.2119 0.2164 -0.0079 0.0058  -0.0033 61  ASP   B O   
2446 C CB  . ASP   B 80  ? 0.1806 0.2083 0.2165 -0.0091 0.0076  -0.0006 61  ASP   B CB  
2447 C CG  . ASP   B 80  ? 0.2193 0.2447 0.2571 -0.0089 0.0106  -0.0017 61  ASP   B CG  
2448 O OD1 . ASP   B 80  ? 0.2101 0.2345 0.252  -0.0071 0.01    -0.0013 61  ASP   B OD1 
2449 O OD2 . ASP   B 80  ? 0.2166 0.2409 0.2518 -0.0105 0.0132  -0.0031 61  ASP   B OD2 
2450 N N   . ILE   B 81  ? 0.1476 0.1787 0.1912 -0.0044 0.0062  -0.0033 62  ILE   B N   
2451 C CA  . ILE   B 81  ? 0.167  0.2003 0.2113 -0.0042 0.0071  -0.0048 62  ILE   B CA  
2452 C C   . ILE   B 81  ? 0.1571 0.187  0.2002 -0.0057 0.0091  -0.0053 62  ILE   B C   
2453 O O   . ILE   B 81  ? 0.1723 0.1985 0.2164 -0.0048 0.0093  -0.0049 62  ILE   B O   
2454 C CB  . ILE   B 81  ? 0.1752 0.2085 0.2214 -0.001  0.0058  -0.0052 62  ILE   B CB  
2455 C CG1 . ILE   B 81  ? 0.1972 0.2339 0.2453 0.0013  0.0036  -0.005  62  ILE   B CG1 
2456 C CG2 . ILE   B 81  ? 0.1821 0.2166 0.2276 -0.0009 0.0073  -0.0065 62  ILE   B CG2 
2457 C CD1 . ILE   B 81  ? 0.2089 0.2526 0.2588 0.001   0.004   -0.0056 62  ILE   B CD1 
2458 N N   . GLY   B 82  ? 0.1468 0.1778 0.1881 -0.008  0.0104  -0.006  63  GLY   B N   
2459 C CA  . GLY   B 82  ? 0.1535 0.1801 0.1936 -0.0092 0.0119  -0.0065 63  GLY   B CA  
2460 C C   . GLY   B 82  ? 0.1481 0.1712 0.1875 -0.0096 0.0132  -0.0067 63  GLY   B C   
2461 O O   . GLY   B 82  ? 0.1582 0.1777 0.199  -0.0087 0.014   -0.0067 63  GLY   B O   
2462 N N   . SER   B 83  ? 0.1531 0.1773 0.1901 -0.0111 0.0134  -0.0069 64  SER   B N   
2463 C CA  . SER   B 83  ? 0.1673 0.1888 0.2021 -0.0118 0.0153  -0.0073 64  SER   B CA  
2464 C C   . SER   B 83  ? 0.1822 0.1991 0.2154 -0.0125 0.0175  -0.009  64  SER   B C   
2465 O O   . SER   B 83  ? 0.1868 0.2011 0.2196 -0.0119 0.02    -0.0098 64  SER   B O   
2466 C CB  . SER   B 83  ? 0.196  0.2191 0.2262 -0.0139 0.0146  -0.0074 64  SER   B CB  
2467 O OG  . SER   B 83  ? 0.2108 0.2379 0.2424 -0.0131 0.0119  -0.0058 64  SER   B OG  
2468 N N   . GLY   B 84  ? 0.1881 0.2039 0.2202 -0.0139 0.0169  -0.0097 65  GLY   B N   
2469 C CA  . GLY   B 84  ? 0.1941 0.2041 0.2238 -0.0149 0.0184  -0.0114 65  GLY   B CA  
2470 C C   . GLY   B 84  ? 0.1903 0.1982 0.2146 -0.0166 0.0197  -0.0133 65  GLY   B C   
2471 O O   . GLY   B 84  ? 0.2012 0.2124 0.2226 -0.0184 0.0185  -0.0129 65  GLY   B O   
2472 N N   . PRO   B 85  ? 0.1916 0.1939 0.2144 -0.0158 0.0223  -0.0153 66  PRO   B N   
2473 C CA  . PRO   B 85  ? 0.1937 0.1929 0.2098 -0.0171 0.0242  -0.0177 66  PRO   B CA  
2474 C C   . PRO   B 85  ? 0.212  0.2132 0.229  -0.015  0.0273  -0.0175 66  PRO   B C   
2475 O O   . PRO   B 85  ? 0.2316 0.2294 0.2435 -0.0152 0.0303  -0.0199 66  PRO   B O   
2476 C CB  . PRO   B 85  ? 0.1992 0.1905 0.2136 -0.0168 0.0256  -0.0203 66  PRO   B CB  
2477 C CG  . PRO   B 85  ? 0.2161 0.2075 0.2385 -0.0132 0.0259  -0.0189 66  PRO   B CG  
2478 C CD  . PRO   B 85  ? 0.1959 0.1938 0.2225 -0.0135 0.0231  -0.0156 66  PRO   B CD  
2479 N N   . THR   B 86  ? 0.1941 0.2003 0.2173 -0.0133 0.0268  -0.0148 67  THR   B N   
2480 C CA  . THR   B 86  ? 0.2038 0.212  0.2291 -0.0117 0.0299  -0.0142 67  THR   B CA  
2481 C C   . THR   B 86  ? 0.1928 0.2046 0.2149 -0.0134 0.0288  -0.0121 67  THR   B C   
2482 O O   . THR   B 86  ? 0.1904 0.2046 0.2126 -0.0143 0.025   -0.0103 67  THR   B O   
2483 C CB  . THR   B 86  ? 0.2092 0.2194 0.2442 -0.0088 0.0301  -0.0125 67  THR   B CB  
2484 O OG1 . THR   B 86  ? 0.2073 0.2208 0.2454 -0.0089 0.0263  -0.0099 67  THR   B OG1 
2485 C CG2 . THR   B 86  ? 0.2295 0.2357 0.2678 -0.007  0.03    -0.0139 67  THR   B CG2 
2486 N N   . ILE   B 87  ? 0.1939 0.206  0.2136 -0.0135 0.0324  -0.0121 68  ILE   B N   
2487 C CA  . ILE   B 87  ? 0.1957 0.2103 0.2118 -0.0153 0.0315  -0.0094 68  ILE   B CA  
2488 C C   . ILE   B 87  ? 0.1966 0.2144 0.2188 -0.0143 0.034   -0.0069 68  ILE   B C   
2489 O O   . ILE   B 87  ? 0.207  0.2262 0.2269 -0.0159 0.033   -0.0041 68  ILE   B O   
2490 C CB  . ILE   B 87  ? 0.2398 0.2516 0.2443 -0.018  0.0329  -0.011  68  ILE   B CB  
2491 C CG1 . ILE   B 87  ? 0.2704 0.2798 0.2718 -0.0173 0.0392  -0.0139 68  ILE   B CG1 
2492 C CG2 . ILE   B 87  ? 0.2648 0.2742 0.264  -0.0199 0.0292  -0.0127 68  ILE   B CG2 
2493 C CD1 . ILE   B 87  ? 0.2957 0.3078 0.2971 -0.0175 0.0434  -0.0122 68  ILE   B CD1 
2494 N N   . TYR   B 88  ? 0.186  0.2047 0.2161 -0.0119 0.0367  -0.0076 69  TYR   B N   
2495 C CA  . TYR   B 88  ? 0.1909 0.2136 0.228  -0.0115 0.039   -0.0051 69  TYR   B CA  
2496 C C   . TYR   B 88  ? 0.1844 0.2089 0.2248 -0.0124 0.0345  -0.0013 69  TYR   B C   
2497 O O   . TYR   B 88  ? 0.1986 0.2254 0.2405 -0.0139 0.0356  0.0016  69  TYR   B O   
2498 C CB  . TYR   B 88  ? 0.2    0.2241 0.2471 -0.0085 0.0413  -0.0063 69  TYR   B CB  
2499 C CG  . TYR   B 88  ? 0.1929 0.2169 0.2471 -0.007  0.0363  -0.0052 69  TYR   B CG  
2500 C CD1 . TYR   B 88  ? 0.185  0.212  0.2463 -0.0071 0.0337  -0.002  69  TYR   B CD1 
2501 C CD2 . TYR   B 88  ? 0.1833 0.2036 0.2359 -0.0059 0.0339  -0.0072 69  TYR   B CD2 
2502 C CE1 . TYR   B 88  ? 0.178  0.204  0.2438 -0.0059 0.0289  -0.0013 69  TYR   B CE1 
2503 C CE2 . TYR   B 88  ? 0.1778 0.1976 0.2349 -0.0048 0.0295  -0.0061 69  TYR   B CE2 
2504 C CZ  . TYR   B 88  ? 0.1633 0.1859 0.2267 -0.0047 0.027   -0.0033 69  TYR   B CZ  
2505 O OH  . TYR   B 88  ? 0.1736 0.195  0.2399 -0.0038 0.0226  -0.0025 69  TYR   B OH  
2506 N N   . GLN   B 89  ? 0.1709 0.1941 0.2123 -0.0116 0.0296  -0.0013 70  GLN   B N   
2507 C CA  . GLN   B 89  ? 0.1809 0.2047 0.2258 -0.0115 0.0251  0.0016  70  GLN   B CA  
2508 C C   . GLN   B 89  ? 0.1777 0.2008 0.2163 -0.0134 0.0229  0.0036  70  GLN   B C   
2509 O O   . GLN   B 89  ? 0.1764 0.199  0.2171 -0.0132 0.0191  0.006   70  GLN   B O   
2510 C CB  . GLN   B 89  ? 0.1872 0.21   0.2351 -0.0095 0.0212  0.0005  70  GLN   B CB  
2511 C CG  . GLN   B 89  ? 0.1869 0.2087 0.2289 -0.0098 0.0194  -0.0012 70  GLN   B CG  
2512 C CD  . GLN   B 89  ? 0.1973 0.2176 0.2364 -0.01   0.0219  -0.0041 70  GLN   B CD  
2513 O OE1 . GLN   B 89  ? 0.2042 0.2236 0.2435 -0.0099 0.0256  -0.0054 70  GLN   B OE1 
2514 N NE2 . GLN   B 89  ? 0.2214 0.2413 0.2579 -0.0104 0.0198  -0.0053 70  GLN   B NE2 
2515 N N   . LEU   B 90  ? 0.1918 0.2141 0.222  -0.0153 0.0249  0.0028  71  LEU   B N   
2516 C CA  . LEU   B 90  ? 0.1992 0.2205 0.2223 -0.0172 0.0222  0.005   71  LEU   B CA  
2517 C C   . LEU   B 90  ? 0.2162 0.2372 0.2341 -0.0199 0.0255  0.0072  71  LEU   B C   
2518 O O   . LEU   B 90  ? 0.2401 0.2596 0.2516 -0.0219 0.023   0.0097  71  LEU   B O   
2519 C CB  . LEU   B 90  ? 0.2101 0.2304 0.2263 -0.018  0.0209  0.0026  71  LEU   B CB  
2520 C CG  . LEU   B 90  ? 0.2175 0.2386 0.2379 -0.016  0.0188  0.0002  71  LEU   B CG  
2521 C CD1 . LEU   B 90  ? 0.2469 0.2671 0.2607 -0.0177 0.018   -0.002  71  LEU   B CD1 
2522 C CD2 . LEU   B 90  ? 0.2152 0.2376 0.241  -0.0141 0.0143  0.0019  71  LEU   B CD2 
2523 N N   . LEU   B 91  ? 0.2013 0.224  0.2217 -0.0201 0.0313  0.0064  72  LEU   B N   
2524 C CA  . LEU   B 91  ? 0.217  0.2401 0.231  -0.0229 0.0358  0.008   72  LEU   B CA  
2525 C C   . LEU   B 91  ? 0.2401 0.2636 0.2556 -0.0252 0.0341  0.0132  72  LEU   B C   
2526 O O   . LEU   B 91  ? 0.2735 0.2951 0.2796 -0.0281 0.0343  0.0156  72  LEU   B O   
2527 C CB  . LEU   B 91  ? 0.2295 0.2551 0.2469 -0.0219 0.0429  0.0052  72  LEU   B CB  
2528 C CG  . LEU   B 91  ? 0.2429 0.266  0.2549 -0.0205 0.045   0.0001  72  LEU   B CG  
2529 C CD1 . LEU   B 91  ? 0.2447 0.27   0.2633 -0.018  0.0511  -0.0028 72  LEU   B CD1 
2530 C CD2 . LEU   B 91  ? 0.2729 0.2925 0.2699 -0.0233 0.0464  -0.0008 72  LEU   B CD2 
2531 N N   . SER   B 92  ? 0.217  0.2418 0.2426 -0.0242 0.0316  0.0151  73  SER   B N   
2532 C CA  . SER   B 92  ? 0.2312 0.2547 0.2576 -0.0267 0.0289  0.0202  73  SER   B CA  
2533 C C   . SER   B 92  ? 0.2412 0.2601 0.2632 -0.0261 0.0217  0.0216  73  SER   B C   
2534 O O   . SER   B 92  ? 0.2608 0.2767 0.2774 -0.0286 0.0192  0.0257  73  SER   B O   
2535 C CB  . SER   B 92  ? 0.227  0.2529 0.2656 -0.0262 0.0285  0.0217  73  SER   B CB  
2536 O OG  . SER   B 92  ? 0.2416 0.2727 0.285  -0.0274 0.0352  0.0217  73  SER   B OG  
2537 N N   . ALA   B 93  ? 0.2282 0.2466 0.2526 -0.0227 0.0182  0.0185  74  ALA   B N   
2538 C CA  . ALA   B 93  ? 0.225  0.2405 0.2471 -0.0214 0.0119  0.0194  74  ALA   B CA  
2539 C C   . ALA   B 93  ? 0.2366 0.2504 0.2484 -0.0234 0.0104  0.0208  74  ALA   B C   
2540 O O   . ALA   B 93  ? 0.2478 0.2586 0.2579 -0.0232 0.005   0.0237  74  ALA   B O   
2541 C CB  . ALA   B 93  ? 0.2309 0.2478 0.2571 -0.0178 0.01    0.0154  74  ALA   B CB  
2542 N N   . CYS   B 94  ? 0.239  0.2539 0.2437 -0.0252 0.0145  0.0189  75  CYS   B N   
2543 C CA  . CYS   B 94  ? 0.2534 0.2661 0.2469 -0.0274 0.0123  0.0203  75  CYS   B CA  
2544 C C   . CYS   B 94  ? 0.2833 0.2928 0.2706 -0.0308 0.0116  0.0257  75  CYS   B C   
2545 O O   . CYS   B 94  ? 0.296  0.3027 0.2744 -0.0326 0.0078  0.0279  75  CYS   B O   
2546 C CB  . CYS   B 94  ? 0.2738 0.2871 0.2597 -0.0287 0.0163  0.0165  75  CYS   B CB  
2547 S SG  . CYS   B 94  ? 0.2913 0.3051 0.2722 -0.0314 0.0252  0.0162  75  CYS   B SG  
2548 N N   . GLU   B 95  ? 0.2729 0.2828 0.265  -0.0321 0.0145  0.0281  76  GLU   B N   
2549 C CA  . GLU   B 95  ? 0.285  0.2914 0.2716 -0.0358 0.0134  0.034   76  GLU   B CA  
2550 C C   . GLU   B 95  ? 0.3053 0.3072 0.2951 -0.0344 0.0053  0.0374  76  GLU   B C   
2551 O O   . GLU   B 95  ? 0.3317 0.3289 0.3153 -0.0372 0.0022  0.0426  76  GLU   B O   
2552 C CB  . GLU   B 95  ? 0.2936 0.3027 0.2854 -0.0382 0.0194  0.0358  76  GLU   B CB  
2553 C CG  . GLU   B 95  ? 0.3284 0.3421 0.3179 -0.0391 0.028   0.0324  76  GLU   B CG  
2554 C CD  . GLU   B 95  ? 0.3833 0.3951 0.3575 -0.0422 0.0307  0.0328  76  GLU   B CD  
2555 O OE1 . GLU   B 95  ? 0.4708 0.4783 0.4363 -0.0455 0.0273  0.0378  76  GLU   B OE1 
2556 O OE2 . GLU   B 95  ? 0.3762 0.39   0.3463 -0.0415 0.0359  0.0282  76  GLU   B OE2 
2557 N N   . SER   B 96  ? 0.2852 0.2879 0.2846 -0.03   0.002   0.0347  77  SER   B N   
2558 C CA  . SER   B 96  ? 0.3024 0.3005 0.3062 -0.0277 -0.005  0.0369  77  SER   B CA  
2559 C C   . SER   B 96  ? 0.2945 0.2926 0.2992 -0.0236 -0.0104 0.0347  77  SER   B C   
2560 O O   . SER   B 96  ? 0.3083 0.3022 0.316  -0.0211 -0.0163 0.0364  77  SER   B O   
2561 C CB  . SER   B 96  ? 0.3238 0.3222 0.338  -0.026  -0.0045 0.0356  77  SER   B CB  
2562 O OG  . SER   B 96  ? 0.3772 0.3764 0.3923 -0.0302 0.0001  0.0383  77  SER   B OG  
2563 N N   . PHE   B 97  ? 0.2674 0.27   0.2701 -0.0227 -0.0087 0.031   78  PHE   B N   
2564 C CA  . PHE   B 97  ? 0.2617 0.2661 0.2666 -0.0191 -0.0135 0.0291  78  PHE   B CA  
2565 C C   . PHE   B 97  ? 0.2832 0.2887 0.2794 -0.0213 -0.0149 0.0296  78  PHE   B C   
2566 O O   . PHE   B 97  ? 0.3152 0.3226 0.3058 -0.024  -0.0101 0.0276  78  PHE   B O   
2567 C CB  . PHE   B 97  ? 0.2461 0.2555 0.2588 -0.0159 -0.011  0.0238  78  PHE   B CB  
2568 C CG  . PHE   B 97  ? 0.2271 0.2347 0.2478 -0.0129 -0.0119 0.0233  78  PHE   B CG  
2569 C CD1 . PHE   B 97  ? 0.2572 0.2639 0.2807 -0.0144 -0.0082 0.0233  78  PHE   B CD1 
2570 C CD2 . PHE   B 97  ? 0.2411 0.2474 0.2665 -0.0087 -0.0169 0.0229  78  PHE   B CD2 
2571 C CE1 . PHE   B 97  ? 0.2735 0.2777 0.3034 -0.0122 -0.0099 0.0229  78  PHE   B CE1 
2572 C CE2 . PHE   B 97  ? 0.2591 0.2624 0.2902 -0.0062 -0.0179 0.022   78  PHE   B CE2 
2573 C CZ  . PHE   B 97  ? 0.2758 0.2777 0.3087 -0.0082 -0.0148 0.0221  78  PHE   B CZ  
2574 N N   . LYS   B 98  ? 0.2928 0.2973 0.2883 -0.0197 -0.0215 0.0317  79  LYS   B N   
2575 C CA  . LYS   B 98  ? 0.3069 0.3123 0.2943 -0.0219 -0.0243 0.0325  79  LYS   B CA  
2576 C C   . LYS   B 98  ? 0.2943 0.3061 0.284  -0.0214 -0.0222 0.0274  79  LYS   B C   
2577 O O   . LYS   B 98  ? 0.3004 0.3124 0.2815 -0.0248 -0.021  0.0265  79  LYS   B O   
2578 C CB  . LYS   B 98  ? 0.3556 0.359  0.3442 -0.0196 -0.0328 0.0361  79  LYS   B CB  
2579 C CG  . LYS   B 98  ? 0.4724 0.4788 0.4567 -0.0205 -0.0377 0.0364  79  LYS   B CG  
2580 C CD  . LYS   B 98  ? 0.5803 0.5841 0.5664 -0.018  -0.0466 0.0408  79  LYS   B CD  
2581 C CE  . LYS   B 98  ? 0.667  0.677  0.6551 -0.0171 -0.0518 0.0399  79  LYS   B CE  
2582 N NZ  . LYS   B 98  ? 0.7151 0.7336 0.7149 -0.0137 -0.049  0.0345  79  LYS   B NZ  
2583 N N   . GLU   B 99  ? 0.2572 0.2733 0.2576 -0.0173 -0.0221 0.0243  80  GLU   B N   
2584 C CA  . GLU   B 99  ? 0.2361 0.2579 0.2393 -0.0171 -0.0203 0.02    80  GLU   B CA  
2585 C C   . GLU   B 99  ? 0.2156 0.2391 0.2259 -0.0151 -0.0153 0.0166  80  GLU   B C   
2586 O O   . GLU   B 99  ? 0.2023 0.2246 0.2188 -0.012  -0.0156 0.017   80  GLU   B O   
2587 C CB  . GLU   B 99  ? 0.2605 0.2878 0.2699 -0.0145 -0.0261 0.0198  80  GLU   B CB  
2588 C CG  . GLU   B 99  ? 0.3404 0.3742 0.3533 -0.0151 -0.0243 0.0159  80  GLU   B CG  
2589 C CD  . GLU   B 99  ? 0.4463 0.4877 0.4666 -0.0133 -0.0291 0.0156  80  GLU   B CD  
2590 O OE1 . GLU   B 99  ? 0.4976 0.5398 0.5211 -0.0108 -0.0347 0.0184  80  GLU   B OE1 
2591 O OE2 . GLU   B 99  ? 0.4272 0.4737 0.4505 -0.0146 -0.0273 0.0127  80  GLU   B OE2 
2592 N N   . ILE   B 100 ? 0.2067 0.2321 0.2155 -0.0169 -0.011  0.0132  81  ILE   B N   
2593 C CA  . ILE   B 100 ? 0.1964 0.2234 0.2113 -0.0151 -0.0068 0.0101  81  ILE   B CA  
2594 C C   . ILE   B 100 ? 0.2154 0.2472 0.2326 -0.0154 -0.007  0.0071  81  ILE   B C   
2595 O O   . ILE   B 100 ? 0.2389 0.271  0.2503 -0.0186 -0.0076 0.0065  81  ILE   B O   
2596 C CB  . ILE   B 100 ? 0.2084 0.2322 0.2193 -0.0173 -0.001  0.0091  81  ILE   B CB  
2597 C CG1 . ILE   B 100 ? 0.2178 0.2381 0.228  -0.0176 -0.0004 0.0123  81  ILE   B CG1 
2598 C CG2 . ILE   B 100 ? 0.2158 0.241  0.2326 -0.0157 0.0026  0.0058  81  ILE   B CG2 
2599 C CD1 . ILE   B 100 ? 0.2441 0.2626 0.2514 -0.0197 0.0057  0.0118  81  ILE   B CD1 
2600 N N   . VAL   B 101 ? 0.1861 0.2215 0.2113 -0.0125 -0.0069 0.0055  82  VAL   B N   
2601 C CA  . VAL   B 101 ? 0.1823 0.2226 0.2104 -0.0132 -0.0064 0.0031  82  VAL   B CA  
2602 C C   . VAL   B 101 ? 0.1885 0.2268 0.2175 -0.0133 -0.0016 0.0008  82  VAL   B C   
2603 O O   . VAL   B 101 ? 0.1896 0.226  0.2218 -0.0108 -0.0002 0.0009  82  VAL   B O   
2604 C CB  . VAL   B 101 ? 0.1896 0.2362 0.226  -0.0099 -0.0093 0.0032  82  VAL   B CB  
2605 C CG1 . VAL   B 101 ? 0.2052 0.2573 0.2454 -0.0109 -0.0077 0.001   82  VAL   B CG1 
2606 C CG2 . VAL   B 101 ? 0.2059 0.2548 0.2422 -0.0096 -0.0147 0.0057  82  VAL   B CG2 
2607 N N   . VAL   B 102 ? 0.1755 0.213  0.2011 -0.0162 0.0005  -0.0012 83  VAL   B N   
2608 C CA  . VAL   B 102 ? 0.1762 0.211  0.2026 -0.0161 0.0044  -0.0032 83  VAL   B CA  
2609 C C   . VAL   B 102 ? 0.1673 0.2062 0.1976 -0.0167 0.0042  -0.0045 83  VAL   B C   
2610 O O   . VAL   B 102 ? 0.1698 0.2128 0.2003 -0.0187 0.0019  -0.0044 83  VAL   B O   
2611 C CB  . VAL   B 102 ? 0.1946 0.2242 0.2144 -0.0186 0.0074  -0.0046 83  VAL   B CB  
2612 C CG1 . VAL   B 102 ? 0.2167 0.2434 0.2333 -0.0182 0.0086  -0.0031 83  VAL   B CG1 
2613 C CG2 . VAL   B 102 ? 0.2289 0.2582 0.2429 -0.0223 0.006   -0.0059 83  VAL   B CG2 
2614 N N   . THR   B 103 ? 0.1707 0.2087 0.2041 -0.015  0.0063  -0.0052 84  THR   B N   
2615 C CA  . THR   B 103 ? 0.1668 0.2088 0.2036 -0.0156 0.0065  -0.0059 84  THR   B CA  
2616 C C   . THR   B 103 ? 0.1757 0.2136 0.2119 -0.016  0.0091  -0.0068 84  THR   B C   
2617 O O   . THR   B 103 ? 0.1905 0.2239 0.2263 -0.0141 0.0104  -0.0069 84  THR   B O   
2618 C CB  . THR   B 103 ? 0.1773 0.2247 0.2198 -0.0121 0.0053  -0.0052 84  THR   B CB  
2619 O OG1 . THR   B 103 ? 0.1841 0.2278 0.2274 -0.0092 0.0065  -0.0053 84  THR   B OG1 
2620 C CG2 . THR   B 103 ? 0.1812 0.232  0.2255 -0.0106 0.0021  -0.0039 84  THR   B CG2 
2621 N N   . ASP   B 104 ? 0.1684 0.208  0.205  -0.0183 0.0096  -0.0073 85  ASP   B N   
2622 C CA  . ASP   B 104 ? 0.1739 0.2088 0.2095 -0.0186 0.0115  -0.0077 85  ASP   B CA  
2623 C C   . ASP   B 104 ? 0.1656 0.2041 0.2022 -0.0213 0.0118  -0.0073 85  ASP   B C   
2624 O O   . ASP   B 104 ? 0.1698 0.2139 0.2078 -0.0239 0.0106  -0.0071 85  ASP   B O   
2625 C CB  . ASP   B 104 ? 0.1826 0.2098 0.2138 -0.0203 0.0126  -0.0089 85  ASP   B CB  
2626 C CG  . ASP   B 104 ? 0.182  0.2038 0.2135 -0.019  0.014   -0.0088 85  ASP   B CG  
2627 O OD1 . ASP   B 104 ? 0.1629 0.1838 0.1965 -0.0158 0.0142  -0.0084 85  ASP   B OD1 
2628 O OD2 . ASP   B 104 ? 0.1757 0.1934 0.205  -0.0213 0.0143  -0.0091 85  ASP   B OD2 
2629 N N   . TYR   B 105 ? 0.1698 0.2053 0.2057 -0.0212 0.0131  -0.007  86  TYR   B N   
2630 C CA  . TYR   B 105 ? 0.1652 0.2034 0.2011 -0.0246 0.0138  -0.0061 86  TYR   B CA  
2631 C C   . TYR   B 105 ? 0.1753 0.2088 0.208  -0.0294 0.0133  -0.0064 86  TYR   B C   
2632 O O   . TYR   B 105 ? 0.1958 0.2333 0.2294 -0.0334 0.0131  -0.0056 86  TYR   B O   
2633 C CB  . TYR   B 105 ? 0.1743 0.2095 0.2088 -0.0234 0.015   -0.0053 86  TYR   B CB  
2634 C CG  . TYR   B 105 ? 0.2163 0.2556 0.2505 -0.0269 0.0162  -0.004  86  TYR   B CG  
2635 C CD1 . TYR   B 105 ? 0.2276 0.2773 0.2659 -0.0265 0.0173  -0.0039 86  TYR   B CD1 
2636 C CD2 . TYR   B 105 ? 0.2344 0.2677 0.2648 -0.0307 0.0164  -0.0028 86  TYR   B CD2 
2637 C CE1 . TYR   B 105 ? 0.2411 0.296  0.2798 -0.0301 0.0192  -0.0025 86  TYR   B CE1 
2638 C CE2 . TYR   B 105 ? 0.2486 0.2859 0.2785 -0.0347 0.0178  -0.0011 86  TYR   B CE2 
2639 C CZ  . TYR   B 105 ? 0.2492 0.298  0.2835 -0.0346 0.0195  -0.001  86  TYR   B CZ  
2640 O OH  . TYR   B 105 ? 0.2823 0.3366 0.3168 -0.0388 0.0217  0.0009  86  TYR   B OH  
2641 N N   . SER   B 106 ? 0.1866 0.2115 0.2158 -0.0289 0.0132  -0.0076 87  SER   B N   
2642 C CA  . SER   B 106 ? 0.1876 0.2056 0.2127 -0.0329 0.0127  -0.0084 87  SER   B CA  
2643 C C   . SER   B 106 ? 0.1919 0.211  0.2152 -0.0352 0.0113  -0.0098 87  SER   B C   
2644 O O   . SER   B 106 ? 0.1961 0.2137 0.2177 -0.0329 0.0114  -0.0111 87  SER   B O   
2645 C CB  . SER   B 106 ? 0.2266 0.2345 0.2492 -0.0306 0.0136  -0.0093 87  SER   B CB  
2646 O OG  . SER   B 106 ? 0.2687 0.2689 0.2867 -0.0333 0.0131  -0.0111 87  SER   B OG  
2647 N N   . ASP   B 107 ? 0.213  0.2334 0.2353 -0.0404 0.0098  -0.0096 88  ASP   B N   
2648 C CA  . ASP   B 107 ? 0.2194 0.2397 0.2388 -0.0435 0.0076  -0.011  88  ASP   B CA  
2649 C C   . ASP   B 107 ? 0.2256 0.234  0.2377 -0.0433 0.0081  -0.0138 88  ASP   B C   
2650 O O   . ASP   B 107 ? 0.2457 0.2529 0.2538 -0.0431 0.0074  -0.0155 88  ASP   B O   
2651 C CB  . ASP   B 107 ? 0.2594 0.2833 0.28   -0.0499 0.0054  -0.01   88  ASP   B CB  
2652 C CG  . ASP   B 107 ? 0.4014 0.4378 0.4299 -0.0499 0.0058  -0.0074 88  ASP   B CG  
2653 O OD1 . ASP   B 107 ? 0.4483 0.494  0.4813 -0.0486 0.0045  -0.0069 88  ASP   B OD1 
2654 O OD2 . ASP   B 107 ? 0.4806 0.5171 0.5105 -0.0508 0.0077  -0.0058 88  ASP   B OD2 
2655 N N   . GLN   B 108 ? 0.2199 0.2192 0.23   -0.0426 0.0095  -0.0143 89  GLN   B N   
2656 C CA  . GLN   B 108 ? 0.2393 0.2275 0.2434 -0.0413 0.0106  -0.0175 89  GLN   B CA  
2657 C C   . GLN   B 108 ? 0.2248 0.2145 0.2295 -0.0361 0.0129  -0.0185 89  GLN   B C   
2658 O O   . GLN   B 108 ? 0.2388 0.224  0.2381 -0.0356 0.0139  -0.0212 89  GLN   B O   
2659 C CB  . GLN   B 108 ? 0.2797 0.2586 0.2835 -0.0403 0.0115  -0.0174 89  GLN   B CB  
2660 C CG  . GLN   B 108 ? 0.3614 0.3339 0.3624 -0.0457 0.0094  -0.0168 89  GLN   B CG  
2661 C CD  . GLN   B 108 ? 0.4396 0.4005 0.4391 -0.0432 0.0101  -0.0173 89  GLN   B CD  
2662 O OE1 . GLN   B 108 ? 0.5003 0.461  0.5028 -0.0423 0.0101  -0.0144 89  GLN   B OE1 
2663 N NE2 . GLN   B 108 ? 0.4067 0.3575 0.4014 -0.0418 0.0107  -0.021  89  GLN   B NE2 
2664 N N   . ASN   B 109 ? 0.2021 0.1982 0.2128 -0.0324 0.0139  -0.0163 90  ASN   B N   
2665 C CA  . ASN   B 109 ? 0.2072 0.205  0.2191 -0.0282 0.0158  -0.0167 90  ASN   B CA  
2666 C C   . ASN   B 109 ? 0.2116 0.2143 0.221  -0.0294 0.0148  -0.0168 90  ASN   B C   
2667 O O   . ASN   B 109 ? 0.2302 0.2305 0.2358 -0.028  0.0164  -0.0183 90  ASN   B O   
2668 C CB  . ASN   B 109 ? 0.2186 0.2215 0.237  -0.0248 0.0161  -0.0143 90  ASN   B CB  
2669 C CG  . ASN   B 109 ? 0.2385 0.2357 0.2589 -0.0224 0.0172  -0.0142 90  ASN   B CG  
2670 O OD1 . ASN   B 109 ? 0.2795 0.2694 0.2977 -0.0215 0.0187  -0.0163 90  ASN   B OD1 
2671 N ND2 . ASN   B 109 ? 0.218  0.2181 0.2425 -0.0208 0.0166  -0.012  90  ASN   B ND2 
2672 N N   . LEU   B 110 ? 0.2157 0.2254 0.2271 -0.0318 0.012   -0.0152 91  LEU   B N   
2673 C CA  . LEU   B 110 ? 0.2369 0.2512 0.2462 -0.0329 0.01    -0.0149 91  LEU   B CA  
2674 C C   . LEU   B 110 ? 0.237  0.2449 0.2374 -0.0363 0.0093  -0.0174 91  LEU   B C   
2675 O O   . LEU   B 110 ? 0.2517 0.2592 0.2471 -0.0361 0.0091  -0.0179 91  LEU   B O   
2676 C CB  . LEU   B 110 ? 0.2588 0.2824 0.2734 -0.0348 0.0069  -0.0128 91  LEU   B CB  
2677 C CG  . LEU   B 110 ? 0.3195 0.3496 0.3418 -0.031  0.0077  -0.0107 91  LEU   B CG  
2678 C CD1 . LEU   B 110 ? 0.3463 0.386  0.374  -0.0324 0.0053  -0.0091 91  LEU   B CD1 
2679 C CD2 . LEU   B 110 ? 0.3387 0.3686 0.3615 -0.0268 0.0086  -0.0101 91  LEU   B CD2 
2680 N N   . GLN   B 111 ? 0.2332 0.2351 0.2306 -0.0396 0.0087  -0.0191 92  GLN   B N   
2681 C CA  . GLN   B 111 ? 0.2511 0.2453 0.2389 -0.0428 0.0079  -0.0222 92  GLN   B CA  
2682 C C   . GLN   B 111 ? 0.2401 0.2269 0.2223 -0.0393 0.0121  -0.025  92  GLN   B C   
2683 O O   . GLN   B 111 ? 0.2628 0.2461 0.2365 -0.0404 0.0122  -0.027  92  GLN   B O   
2684 C CB  . GLN   B 111 ? 0.2946 0.2826 0.2805 -0.0471 0.0062  -0.0234 92  GLN   B CB  
2685 C CG  . GLN   B 111 ? 0.3762 0.3725 0.3671 -0.0517 0.0023  -0.0208 92  GLN   B CG  
2686 C CD  . GLN   B 111 ? 0.5326 0.5226 0.5214 -0.057  0.0004  -0.0215 92  GLN   B CD  
2687 O OE1 . GLN   B 111 ? 0.5892 0.5681 0.5694 -0.0592 -0.0002 -0.0248 92  GLN   B OE1 
2688 N NE2 . GLN   B 111 ? 0.5473 0.544  0.5435 -0.0593 -0.0006 -0.0185 92  GLN   B NE2 
2689 N N   . GLU   B 112 ? 0.24   0.225  0.2271 -0.035  0.0155  -0.0249 93  GLU   B N   
2690 C CA  . GLU   B 112 ? 0.2668 0.2468 0.2512 -0.0313 0.02    -0.0273 93  GLU   B CA  
2691 C C   . GLU   B 112 ? 0.2817 0.2677 0.2655 -0.0296 0.0213  -0.0258 93  GLU   B C   
2692 O O   . GLU   B 112 ? 0.2903 0.2728 0.2668 -0.0295 0.0239  -0.0281 93  GLU   B O   
2693 C CB  . GLU   B 112 ? 0.2968 0.2744 0.2882 -0.0273 0.0223  -0.027  93  GLU   B CB  
2694 C CG  . GLU   B 112 ? 0.2996 0.2729 0.2906 -0.023  0.0272  -0.0295 93  GLU   B CG  
2695 C CD  . GLU   B 112 ? 0.3362 0.2992 0.3186 -0.0234 0.0291  -0.0344 93  GLU   B CD  
2696 O OE1 . GLU   B 112 ? 0.3823 0.3384 0.3606 -0.0265 0.0264  -0.0358 93  GLU   B OE1 
2697 O OE2 . GLU   B 112 ? 0.3832 0.3448 0.363  -0.0206 0.0336  -0.0368 93  GLU   B OE2 
2698 N N   . LEU   B 113 ? 0.266  0.2605 0.2565 -0.029  0.0192  -0.0221 94  LEU   B N   
2699 C CA  . LEU   B 113 ? 0.2887 0.2884 0.2788 -0.0281 0.0192  -0.02   94  LEU   B CA  
2700 C C   . LEU   B 113 ? 0.2903 0.2886 0.2706 -0.0318 0.017   -0.0208 94  LEU   B C   
2701 O O   . LEU   B 113 ? 0.2942 0.2911 0.2681 -0.0316 0.019   -0.0211 94  LEU   B O   
2702 C CB  . LEU   B 113 ? 0.2956 0.3035 0.2938 -0.0273 0.0161  -0.0163 94  LEU   B CB  
2703 C CG  . LEU   B 113 ? 0.3142 0.3246 0.3207 -0.0236 0.0176  -0.0147 94  LEU   B CG  
2704 C CD1 . LEU   B 113 ? 0.3207 0.3383 0.3333 -0.0229 0.0142  -0.0119 94  LEU   B CD1 
2705 C CD2 . LEU   B 113 ? 0.3121 0.3219 0.3188 -0.0212 0.0208  -0.0143 94  LEU   B CD2 
2706 N N   . GLU   B 114 ? 0.2807 0.2798 0.2598 -0.0354 0.0127  -0.0209 95  GLU   B N   
2707 C CA  . GLU   B 114 ? 0.3114 0.3096 0.2817 -0.0394 0.0091  -0.0214 95  GLU   B CA  
2708 C C   . GLU   B 114 ? 0.3103 0.2989 0.2683 -0.0408 0.0117  -0.0254 95  GLU   B C   
2709 O O   . GLU   B 114 ? 0.3246 0.3119 0.2733 -0.0426 0.0107  -0.0256 95  GLU   B O   
2710 C CB  . GLU   B 114 ? 0.3599 0.3619 0.3332 -0.0432 0.0037  -0.0204 95  GLU   B CB  
2711 C CG  . GLU   B 114 ? 0.469  0.4815 0.4529 -0.0413 0.0014  -0.0164 95  GLU   B CG  
2712 C CD  . GLU   B 114 ? 0.6181 0.6378 0.6069 -0.0446 -0.0038 -0.0148 95  GLU   B CD  
2713 O OE1 . GLU   B 114 ? 0.6528 0.674  0.6468 -0.0462 -0.0039 -0.015  95  GLU   B OE1 
2714 O OE2 . GLU   B 114 ? 0.6515 0.676  0.6398 -0.0454 -0.008  -0.0128 95  GLU   B OE2 
2715 N N   . LYS   B 115 ? 0.295  0.2764 0.2522 -0.0396 0.0152  -0.0288 96  LYS   B N   
2716 C CA  . LYS   B 115 ? 0.3117 0.2833 0.2571 -0.04   0.0186  -0.0336 96  LYS   B CA  
2717 C C   . LYS   B 115 ? 0.3088 0.2818 0.2507 -0.0371 0.0234  -0.0333 96  LYS   B C   
2718 O O   . LYS   B 115 ? 0.3426 0.3111 0.2723 -0.0389 0.0246  -0.0355 96  LYS   B O   
2719 C CB  . LYS   B 115 ? 0.3426 0.3067 0.2901 -0.0378 0.0217  -0.0369 96  LYS   B CB  
2720 C CG  . LYS   B 115 ? 0.39   0.3494 0.3367 -0.0419 0.0171  -0.0379 96  LYS   B CG  
2721 C CD  . LYS   B 115 ? 0.4655 0.4154 0.413  -0.0397 0.0199  -0.0412 96  LYS   B CD  
2722 C CE  . LYS   B 115 ? 0.5715 0.515  0.5161 -0.0448 0.0152  -0.0422 96  LYS   B CE  
2723 N NZ  . LYS   B 115 ? 0.6516 0.5907 0.6031 -0.0432 0.0156  -0.0418 96  LYS   B NZ  
2724 N N   . TRP   B 116 ? 0.2899 0.2694 0.2424 -0.0332 0.026   -0.0302 97  TRP   B N   
2725 C CA  . TRP   B 116 ? 0.2856 0.2674 0.2361 -0.0312 0.0305  -0.0292 97  TRP   B CA  
2726 C C   . TRP   B 116 ? 0.2809 0.2665 0.226  -0.034  0.027   -0.0258 97  TRP   B C   
2727 O O   . TRP   B 116 ? 0.2897 0.273  0.2244 -0.0351 0.0296  -0.0264 97  TRP   B O   
2728 C CB  . TRP   B 116 ? 0.2873 0.2746 0.2509 -0.0268 0.0336  -0.0269 97  TRP   B CB  
2729 C CG  . TRP   B 116 ? 0.2868 0.2758 0.2485 -0.0253 0.039   -0.0262 97  TRP   B CG  
2730 C CD1 . TRP   B 116 ? 0.3044 0.2902 0.2634 -0.0231 0.0456  -0.0296 97  TRP   B CD1 
2731 C CD2 . TRP   B 116 ? 0.2816 0.2762 0.2435 -0.0262 0.0383  -0.0218 97  TRP   B CD2 
2732 N NE1 . TRP   B 116 ? 0.3172 0.3072 0.2752 -0.0229 0.0496  -0.0274 97  TRP   B NE1 
2733 C CE2 . TRP   B 116 ? 0.3014 0.2962 0.261  -0.025  0.045   -0.0224 97  TRP   B CE2 
2734 C CE3 . TRP   B 116 ? 0.2978 0.297  0.2624 -0.0276 0.0328  -0.0173 97  TRP   B CE3 
2735 C CZ2 . TRP   B 116 ? 0.3245 0.3236 0.2833 -0.026  0.046   -0.0183 97  TRP   B CZ2 
2736 C CZ3 . TRP   B 116 ? 0.314  0.3162 0.2774 -0.0281 0.0334  -0.0136 97  TRP   B CZ3 
2737 C CH2 . TRP   B 116 ? 0.3127 0.3146 0.2728 -0.0278 0.0399  -0.0139 97  TRP   B CH2 
2738 N N   . LEU   B 117 ? 0.2749 0.2663 0.2263 -0.0351 0.0212  -0.0223 98  LEU   B N   
2739 C CA  . LEU   B 117 ? 0.2909 0.286  0.2385 -0.0371 0.0169  -0.0186 98  LEU   B CA  
2740 C C   . LEU   B 117 ? 0.3124 0.302  0.2451 -0.0415 0.0144  -0.0205 98  LEU   B C   
2741 O O   . LEU   B 117 ? 0.3365 0.3255 0.2606 -0.043  0.014   -0.0187 98  LEU   B O   
2742 C CB  . LEU   B 117 ? 0.2829 0.2849 0.2408 -0.0369 0.0111  -0.0153 98  LEU   B CB  
2743 C CG  . LEU   B 117 ? 0.2787 0.2858 0.2493 -0.0328 0.0128  -0.013  98  LEU   B CG  
2744 C CD1 . LEU   B 117 ? 0.281  0.2943 0.2607 -0.0325 0.0078  -0.011  98  LEU   B CD1 
2745 C CD2 . LEU   B 117 ? 0.2882 0.2969 0.2588 -0.0313 0.0145  -0.0098 98  LEU   B CD2 
2746 N N   . LYS   B 118 ? 0.3133 0.2981 0.2422 -0.0439 0.0126  -0.0242 99  LYS   B N   
2747 C CA  . LYS   B 118 ? 0.344  0.3223 0.2577 -0.0485 0.0097  -0.0267 99  LYS   B CA  
2748 C C   . LYS   B 118 ? 0.3746 0.3437 0.2755 -0.0482 0.016   -0.0316 99  LYS   B C   
2749 O O   . LYS   B 118 ? 0.3957 0.3577 0.2822 -0.052  0.0139  -0.0345 99  LYS   B O   
2750 C CB  . LYS   B 118 ? 0.3683 0.3454 0.2838 -0.052  0.004   -0.0282 99  LYS   B CB  
2751 C CG  . LYS   B 118 ? 0.425  0.4122 0.3524 -0.0526 -0.0023 -0.0235 99  LYS   B CG  
2752 C CD  . LYS   B 118 ? 0.4886 0.4765 0.4195 -0.0565 -0.0074 -0.0245 99  LYS   B CD  
2753 C CE  . LYS   B 118 ? 0.5401 0.5398 0.4855 -0.0559 -0.0115 -0.0201 99  LYS   B CE  
2754 N NZ  . LYS   B 118 ? 0.5977 0.5996 0.5487 -0.0596 -0.0153 -0.0206 99  LYS   B NZ  
2755 N N   . ALA   B 119 ? 0.3647 0.3335 0.2701 -0.0438 0.0235  -0.0329 100 ALA   B N   
2756 C CA  . ALA   B 119 ? 0.3856 0.3468 0.2808 -0.0425 0.0307  -0.038  100 ALA   B CA  
2757 C C   . ALA   B 119 ? 0.411  0.362  0.2986 -0.0442 0.0296  -0.0439 100 ALA   B C   
2758 O O   . ALA   B 119 ? 0.4362 0.3788 0.3089 -0.0454 0.0324  -0.0486 100 ALA   B O   
2759 C CB  . ALA   B 119 ? 0.3911 0.3508 0.2718 -0.0446 0.0327  -0.0374 100 ALA   B CB  
2760 N N   . ALA   B 120 ? 0.3949 0.3463 0.2925 -0.0442 0.0262  -0.0438 101 ALA   B N   
2761 C CA  . ALA   B 120 ? 0.3993 0.3404 0.2912 -0.0459 0.0248  -0.049  101 ALA   B CA  
2762 C C   . ALA   B 120 ? 0.4179 0.3517 0.3085 -0.0411 0.0327  -0.0541 101 ALA   B C   
2763 O O   . ALA   B 120 ? 0.4149 0.3539 0.3146 -0.0362 0.0382  -0.0528 101 ALA   B O   
2764 C CB  . ALA   B 120 ? 0.3953 0.3395 0.2992 -0.0473 0.0195  -0.0467 101 ALA   B CB  
2765 N N   . PRO   B 121 ? 0.4583 0.3795 0.3373 -0.0422 0.0333  -0.0603 102 PRO   B N   
2766 C CA  . PRO   B 121 ? 0.4719 0.3861 0.3495 -0.0368 0.0412  -0.0657 102 PRO   B CA  
2767 C C   . PRO   B 121 ? 0.4721 0.3888 0.3663 -0.0315 0.0436  -0.0646 102 PRO   B C   
2768 O O   . PRO   B 121 ? 0.4928 0.4101 0.3912 -0.0259 0.0508  -0.0666 102 PRO   B O   
2769 C CB  . PRO   B 121 ? 0.4889 0.3877 0.3506 -0.0396 0.0395  -0.0726 102 PRO   B CB  
2770 C CG  . PRO   B 121 ? 0.4932 0.3922 0.3457 -0.047  0.0315  -0.0706 102 PRO   B CG  
2771 C CD  . PRO   B 121 ? 0.4738 0.3869 0.3403 -0.0485 0.0267  -0.0627 102 PRO   B CD  
2772 N N   . ALA   B 122 ? 0.4524 0.3711 0.3562 -0.0334 0.0378  -0.0613 103 ALA   B N   
2773 C CA  . ALA   B 122 ? 0.4528 0.3729 0.3709 -0.0288 0.0394  -0.06   103 ALA   B CA  
2774 C C   . ALA   B 122 ? 0.4313 0.3649 0.3632 -0.0261 0.0406  -0.0542 103 ALA   B C   
2775 O O   . ALA   B 122 ? 0.433  0.3688 0.3769 -0.0233 0.0402  -0.052  103 ALA   B O   
2776 C CB  . ALA   B 122 ? 0.4589 0.3735 0.3799 -0.032  0.0333  -0.0594 103 ALA   B CB  
2777 N N   . ALA   B 123 ? 0.4181 0.36   0.3479 -0.0272 0.0413  -0.0513 104 ALA   B N   
2778 C CA  . ALA   B 123 ? 0.4068 0.3604 0.3487 -0.0251 0.0419  -0.0459 104 ALA   B CA  
2779 C C   . ALA   B 123 ? 0.3777 0.3331 0.3283 -0.0192 0.0483  -0.0467 104 ALA   B C   
2780 O O   . ALA   B 123 ? 0.3879 0.3379 0.3334 -0.0165 0.054   -0.0513 104 ALA   B O   
2781 C CB  . ALA   B 123 ? 0.4166 0.3762 0.3525 -0.0276 0.0415  -0.0432 104 ALA   B CB  
2782 N N   . PHE   B 124 ? 0.3449 0.3085 0.3093 -0.017  0.0475  -0.0422 105 PHE   B N   
2783 C CA  . PHE   B 124 ? 0.3101 0.277  0.2847 -0.0116 0.0527  -0.0422 105 PHE   B CA  
2784 C C   . PHE   B 124 ? 0.3328 0.3049 0.3048 -0.0108 0.0586  -0.0421 105 PHE   B C   
2785 O O   . PHE   B 124 ? 0.3312 0.3071 0.2975 -0.0142 0.0572  -0.0395 105 PHE   B O   
2786 C CB  . PHE   B 124 ? 0.285  0.2593 0.2733 -0.0104 0.0493  -0.0371 105 PHE   B CB  
2787 C CG  . PHE   B 124 ? 0.2712 0.2491 0.2717 -0.0053 0.053   -0.0366 105 PHE   B CG  
2788 C CD1 . PHE   B 124 ? 0.2873 0.2592 0.2922 -0.0016 0.054   -0.0393 105 PHE   B CD1 
2789 C CD2 . PHE   B 124 ? 0.2745 0.2616 0.283  -0.0043 0.0544  -0.0329 105 PHE   B CD2 
2790 C CE1 . PHE   B 124 ? 0.2886 0.2646 0.306  0.0033  0.0566  -0.0385 105 PHE   B CE1 
2791 C CE2 . PHE   B 124 ? 0.2792 0.2705 0.3002 0       0.0571  -0.032  105 PHE   B CE2 
2792 C CZ  . PHE   B 124 ? 0.2815 0.2676 0.3072 0.0039  0.0579  -0.0348 105 PHE   B CZ  
2793 N N   . ASP   B 125 ? 0.3261 0.2988 0.3033 -0.0062 0.065   -0.0445 106 ASP   B N   
2794 C CA  . ASP   B 125 ? 0.324  0.3026 0.2998 -0.0055 0.0717  -0.0442 106 ASP   B CA  
2795 C C   . ASP   B 125 ? 0.3133 0.3028 0.3031 -0.0045 0.0715  -0.0386 106 ASP   B C   
2796 O O   . ASP   B 125 ? 0.3206 0.3138 0.3234 -0.0003 0.0737  -0.0383 106 ASP   B O   
2797 C CB  . ASP   B 125 ? 0.3536 0.3286 0.3286 -0.0008 0.0796  -0.0499 106 ASP   B CB  
2798 C CG  . ASP   B 125 ? 0.4169 0.3988 0.3908 -0.0001 0.0876  -0.0498 106 ASP   B CG  
2799 O OD1 . ASP   B 125 ? 0.3717 0.3594 0.3421 -0.0042 0.0867  -0.0453 106 ASP   B OD1 
2800 O OD2 . ASP   B 125 ? 0.4876 0.469  0.4636 0.0044  0.0951  -0.0542 106 ASP   B OD2 
2801 N N   . TRP   B 126 ? 0.2892 0.2834 0.2761 -0.0084 0.0685  -0.0341 107 TRP   B N   
2802 C CA  . TRP   B 126 ? 0.2736 0.2769 0.2721 -0.0082 0.0679  -0.0286 107 TRP   B CA  
2803 C C   . TRP   B 126 ? 0.2675 0.2766 0.2659 -0.0084 0.0749  -0.0276 107 TRP   B C   
2804 O O   . TRP   B 126 ? 0.2675 0.2839 0.2748 -0.009  0.0746  -0.0229 107 TRP   B O   
2805 C CB  . TRP   B 126 ? 0.2547 0.2593 0.2504 -0.0121 0.0609  -0.0243 107 TRP   B CB  
2806 C CG  . TRP   B 126 ? 0.2431 0.2455 0.2434 -0.0118 0.0544  -0.0238 107 TRP   B CG  
2807 C CD1 . TRP   B 126 ? 0.2405 0.2377 0.2333 -0.014  0.0499  -0.0253 107 TRP   B CD1 
2808 C CD2 . TRP   B 126 ? 0.2288 0.2346 0.2421 -0.0094 0.0518  -0.0215 107 TRP   B CD2 
2809 N NE1 . TRP   B 126 ? 0.2387 0.2361 0.2394 -0.0131 0.0454  -0.0241 107 TRP   B NE1 
2810 C CE2 . TRP   B 126 ? 0.2365 0.2387 0.2489 -0.0101 0.0464  -0.0219 107 TRP   B CE2 
2811 C CE3 . TRP   B 126 ? 0.2114 0.2227 0.2369 -0.0068 0.0535  -0.0194 107 TRP   B CE3 
2812 C CZ2 . TRP   B 126 ? 0.2279 0.2312 0.2497 -0.0084 0.0431  -0.0202 107 TRP   B CZ2 
2813 C CZ3 . TRP   B 126 ? 0.2169 0.2291 0.2519 -0.0051 0.0493  -0.0177 107 TRP   B CZ3 
2814 C CH2 . TRP   B 126 ? 0.2122 0.2202 0.2445 -0.0058 0.0443  -0.0182 107 TRP   B CH2 
2815 N N   . SER   B 127 ? 0.2846 0.2905 0.2727 -0.0082 0.0816  -0.0319 108 SER   B N   
2816 C CA  . SER   B 127 ? 0.312  0.3238 0.2978 -0.0093 0.0888  -0.0304 108 SER   B CA  
2817 C C   . SER   B 127 ? 0.3024 0.3244 0.3058 -0.0066 0.0929  -0.0277 108 SER   B C   
2818 O O   . SER   B 127 ? 0.3202 0.3485 0.3246 -0.0096 0.0945  -0.023  108 SER   B O   
2819 C CB  . SER   B 127 ? 0.383  0.3897 0.3547 -0.0089 0.096   -0.0362 108 SER   B CB  
2820 O OG  . SER   B 127 ? 0.4341 0.4379 0.4112 -0.0034 0.1003  -0.0418 108 SER   B OG  
2821 N N   . PRO   B 128 ? 0.3199 0.3439 0.3375 -0.0015 0.0937  -0.0295 109 PRO   B N   
2822 C CA  . PRO   B 128 ? 0.3176 0.3523 0.3527 0.0004  0.0967  -0.0262 109 PRO   B CA  
2823 C C   . PRO   B 128 ? 0.295  0.3342 0.3374 -0.0029 0.0899  -0.0196 109 PRO   B C   
2824 O O   . PRO   B 128 ? 0.3076 0.355  0.3582 -0.0044 0.0921  -0.0155 109 PRO   B O   
2825 C CB  . PRO   B 128 ? 0.3447 0.3787 0.3922 0.0064  0.0968  -0.0295 109 PRO   B CB  
2826 C CG  . PRO   B 128 ? 0.3544 0.3768 0.3898 0.0078  0.0957  -0.0351 109 PRO   B CG  
2827 C CD  . PRO   B 128 ? 0.3306 0.3471 0.3493 0.0025  0.0918  -0.0344 109 PRO   B CD  
2828 N N   . VAL   B 129 ? 0.2565 0.2898 0.2954 -0.004  0.0814  -0.0186 110 VAL   B N   
2829 C CA  . VAL   B 129 ? 0.2422 0.2781 0.2865 -0.0065 0.0747  -0.0132 110 VAL   B CA  
2830 C C   . VAL   B 129 ? 0.2289 0.2655 0.2634 -0.0115 0.0747  -0.0097 110 VAL   B C   
2831 O O   . VAL   B 129 ? 0.2294 0.2709 0.2701 -0.0137 0.0734  -0.0048 110 VAL   B O   
2832 C CB  . VAL   B 129 ? 0.2565 0.2862 0.2991 -0.006  0.0669  -0.0139 110 VAL   B CB  
2833 C CG1 . VAL   B 129 ? 0.2581 0.2894 0.3035 -0.0085 0.0601  -0.009  110 VAL   B CG1 
2834 C CG2 . VAL   B 129 ? 0.2713 0.3    0.324  -0.0014 0.0664  -0.0163 110 VAL   B CG2 
2835 N N   . VAL   B 130 ? 0.2504 0.2811 0.269  -0.0136 0.0754  -0.0119 111 VAL   B N   
2836 C CA  . VAL   B 130 ? 0.2687 0.299  0.2763 -0.0184 0.0748  -0.0083 111 VAL   B CA  
2837 C C   . VAL   B 130 ? 0.2712 0.3083 0.2815 -0.0201 0.0822  -0.0057 111 VAL   B C   
2838 O O   . VAL   B 130 ? 0.272  0.3118 0.283  -0.0236 0.0802  -0.0002 111 VAL   B O   
2839 C CB  . VAL   B 130 ? 0.2913 0.3142 0.2812 -0.0201 0.0747  -0.0117 111 VAL   B CB  
2840 C CG1 . VAL   B 130 ? 0.3372 0.3594 0.315  -0.025  0.0744  -0.0078 111 VAL   B CG1 
2841 C CG2 . VAL   B 130 ? 0.2761 0.2934 0.2642 -0.0195 0.067   -0.0133 111 VAL   B CG2 
2842 N N   . THR   B 131 ? 0.2838 0.3239 0.2966 -0.0173 0.0905  -0.0095 112 THR   B N   
2843 C CA  . THR   B 131 ? 0.2922 0.3404 0.3089 -0.0188 0.0987  -0.0073 112 THR   B CA  
2844 C C   . THR   B 131 ? 0.2826 0.339  0.317  -0.0193 0.0965  -0.0021 112 THR   B C   
2845 O O   . THR   B 131 ? 0.2984 0.3593 0.3334 -0.0235 0.0981  0.0031  112 THR   B O   
2846 C CB  . THR   B 131 ? 0.3286 0.3791 0.3471 -0.0144 0.1081  -0.0133 112 THR   B CB  
2847 O OG1 . THR   B 131 ? 0.3732 0.415  0.3727 -0.0149 0.11    -0.018  112 THR   B OG1 
2848 C CG2 . THR   B 131 ? 0.3475 0.4085 0.3728 -0.0154 0.1176  -0.0112 112 THR   B CG2 
2849 N N   . TYR   B 132 ? 0.2585 0.3156 0.3065 -0.0154 0.0919  -0.0031 113 TYR   B N   
2850 C CA  . TYR   B 132 ? 0.255  0.3188 0.3194 -0.0159 0.0886  0.0015  113 TYR   B CA  
2851 C C   . TYR   B 132 ? 0.2511 0.3122 0.3115 -0.0207 0.0815  0.0072  113 TYR   B C   
2852 O O   . TYR   B 132 ? 0.2574 0.324  0.325  -0.024  0.0818  0.0122  113 TYR   B O   
2853 C CB  . TYR   B 132 ? 0.2712 0.3344 0.3475 -0.011  0.0843  -0.0009 113 TYR   B CB  
2854 C CG  . TYR   B 132 ? 0.2846 0.3545 0.3779 -0.0112 0.0807  0.0033  113 TYR   B CG  
2855 C CD1 . TYR   B 132 ? 0.3086 0.3887 0.4167 -0.01   0.0862  0.0041  113 TYR   B CD1 
2856 C CD2 . TYR   B 132 ? 0.2997 0.3658 0.3944 -0.0126 0.0716  0.0062  113 TYR   B CD2 
2857 C CE1 . TYR   B 132 ? 0.3343 0.4206 0.4582 -0.0109 0.082   0.0082  113 TYR   B CE1 
2858 C CE2 . TYR   B 132 ? 0.3125 0.3836 0.4217 -0.0131 0.0677  0.0096  113 TYR   B CE2 
2859 C CZ  . TYR   B 132 ? 0.3373 0.4182 0.4612 -0.0122 0.0724  0.0106  113 TYR   B CZ  
2860 O OH  . TYR   B 132 ? 0.3649 0.4506 0.5031 -0.0133 0.0676  0.0142  113 TYR   B OH  
2861 N N   . VAL   B 133 ? 0.2551 0.3078 0.304  -0.0213 0.0752  0.0065  114 VAL   B N   
2862 C CA  . VAL   B 133 ? 0.247  0.2964 0.2917 -0.0251 0.0685  0.0114  114 VAL   B CA  
2863 C C   . VAL   B 133 ? 0.2674 0.3175 0.3024 -0.0302 0.0723  0.0153  114 VAL   B C   
2864 O O   . VAL   B 133 ? 0.2755 0.3263 0.3131 -0.0337 0.0693  0.0206  114 VAL   B O   
2865 C CB  . VAL   B 133 ? 0.2347 0.2763 0.271  -0.024  0.0613  0.0096  114 VAL   B CB  
2866 C CG1 . VAL   B 133 ? 0.2536 0.2917 0.2852 -0.0273 0.0548  0.0144  114 VAL   B CG1 
2867 C CG2 . VAL   B 133 ? 0.2311 0.2721 0.2769 -0.0199 0.0574  0.0069  114 VAL   B CG2 
2868 N N   . CYS   B 134 ? 0.2795 0.3286 0.3028 -0.0307 0.0787  0.0125  115 CYS   B N   
2869 C CA  . CYS   B 134 ? 0.2874 0.337  0.2999 -0.0358 0.083   0.0163  115 CYS   B CA  
2870 C C   . CYS   B 134 ? 0.2964 0.3553 0.3211 -0.0382 0.0884  0.0205  115 CYS   B C   
2871 O O   . CYS   B 134 ? 0.3082 0.3672 0.3298 -0.0433 0.0874  0.0265  115 CYS   B O   
2872 C CB  . CYS   B 134 ? 0.2922 0.3393 0.29   -0.0355 0.0896  0.0117  115 CYS   B CB  
2873 S SG  . CYS   B 134 ? 0.3311 0.3672 0.3115 -0.0356 0.0824  0.0088  115 CYS   B SG  
2874 N N   . ASP   B 135 ? 0.3012 0.3676 0.3405 -0.0344 0.0931  0.0176  116 ASP   B N   
2875 C CA  . ASP   B 135 ? 0.2875 0.3644 0.3418 -0.0362 0.0978  0.0214  116 ASP   B CA  
2876 C C   . ASP   B 135 ? 0.2955 0.3721 0.3595 -0.039  0.0894  0.0271  116 ASP   B C   
2877 O O   . ASP   B 135 ? 0.3035 0.3842 0.3707 -0.0442 0.0908  0.0328  116 ASP   B O   
2878 C CB  . ASP   B 135 ? 0.315  0.3996 0.3845 -0.0306 0.103   0.0168  116 ASP   B CB  
2879 C CG  . ASP   B 135 ? 0.3933 0.4799 0.4563 -0.0277 0.1131  0.0112  116 ASP   B CG  
2880 O OD1 . ASP   B 135 ? 0.4286 0.5115 0.4745 -0.0308 0.1174  0.0111  116 ASP   B OD1 
2881 O OD2 . ASP   B 135 ? 0.4096 0.5009 0.4842 -0.0221 0.1168  0.0069  116 ASP   B OD2 
2882 N N   . LEU   B 136 ? 0.2804 0.3521 0.3491 -0.0358 0.0808  0.0255  117 LEU   B N   
2883 C CA  . LEU   B 136 ? 0.2905 0.3604 0.3673 -0.0378 0.0723  0.0299  117 LEU   B CA  
2884 C C   . LEU   B 136 ? 0.31   0.374  0.376  -0.0433 0.0685  0.0354  117 LEU   B C   
2885 O O   . LEU   B 136 ? 0.3107 0.3755 0.3831 -0.0473 0.0653  0.0407  117 LEU   B O   
2886 C CB  . LEU   B 136 ? 0.283  0.3463 0.3607 -0.0334 0.064   0.0266  117 LEU   B CB  
2887 C CG  . LEU   B 136 ? 0.2838 0.3504 0.3717 -0.0279 0.0648  0.0219  117 LEU   B CG  
2888 C CD1 . LEU   B 136 ? 0.3025 0.3616 0.3887 -0.0249 0.0562  0.0197  117 LEU   B CD1 
2889 C CD2 . LEU   B 136 ? 0.2719 0.3475 0.3778 -0.0282 0.0661  0.0242  117 LEU   B CD2 
2890 N N   . GLU   B 137 ? 0.3045 0.3614 0.3541 -0.0434 0.0677  0.034   118 GLU   B N   
2891 C CA  . GLU   B 137 ? 0.3183 0.3678 0.3558 -0.0476 0.0629  0.0387  118 GLU   B CA  
2892 C C   . GLU   B 137 ? 0.3378 0.3897 0.3681 -0.0537 0.069   0.0437  118 GLU   B C   
2893 O O   . GLU   B 137 ? 0.3749 0.4202 0.3944 -0.0575 0.0649  0.0482  118 GLU   B O   
2894 C CB  . GLU   B 137 ? 0.3162 0.358  0.3401 -0.0451 0.0589  0.0353  118 GLU   B CB  
2895 C CG  . GLU   B 137 ? 0.3024 0.3413 0.333  -0.0402 0.052   0.0318  118 GLU   B CG  
2896 C CD  . GLU   B 137 ? 0.3433 0.3756 0.3628 -0.0382 0.0474  0.029   118 GLU   B CD  
2897 O OE1 . GLU   B 137 ? 0.3395 0.3695 0.3458 -0.0401 0.0496  0.0289  118 GLU   B OE1 
2898 O OE2 . GLU   B 137 ? 0.324  0.354  0.3481 -0.0347 0.0416  0.0268  118 GLU   B OE2 
2899 N N   . GLY   B 138 ? 0.3198 0.3813 0.3568 -0.0545 0.0784  0.0432  119 GLY   B N   
2900 C CA  . GLY   B 138 ? 0.3392 0.4047 0.3713 -0.0607 0.085   0.0484  119 GLY   B CA  
2901 C C   . GLY   B 138 ? 0.3489 0.4154 0.3664 -0.0614 0.094   0.0459  119 GLY   B C   
2902 O O   . GLY   B 138 ? 0.3504 0.4187 0.36   -0.0671 0.0994  0.0505  119 GLY   B O   
2903 N N   . ASN   B 139 ? 0.3471 0.4118 0.3598 -0.0559 0.0958  0.0386  120 ASN   B N   
2904 C CA  . ASN   B 139 ? 0.3501 0.4138 0.3468 -0.056  0.1037  0.035   120 ASN   B CA  
2905 C C   . ASN   B 139 ? 0.3762 0.4313 0.3523 -0.0613 0.1007  0.0392  120 ASN   B C   
2906 O O   . ASN   B 139 ? 0.4067 0.4629 0.3699 -0.065  0.1084  0.0402  120 ASN   B O   
2907 C CB  . ASN   B 139 ? 0.3634 0.4385 0.3667 -0.0562 0.1165  0.0338  120 ASN   B CB  
2908 C CG  . ASN   B 139 ? 0.3859 0.4678 0.4067 -0.0494 0.1191  0.028   120 ASN   B CG  
2909 O OD1 . ASN   B 139 ? 0.4092 0.4872 0.4258 -0.0441 0.1196  0.0211  120 ASN   B OD1 
2910 N ND2 . ASN   B 139 ? 0.3482 0.4395 0.389  -0.0498 0.1197  0.0312  120 ASN   B ND2 
2911 N N   . ARG   B 140 ? 0.3666 0.4135 0.3401 -0.0619 0.0895  0.0422  121 ARG   B N   
2912 C CA  . ARG   B 140 ? 0.384  0.4219 0.3389 -0.0663 0.0846  0.0463  121 ARG   B CA  
2913 C C   . ARG   B 140 ? 0.392  0.4248 0.3301 -0.0644 0.0861  0.0406  121 ARG   B C   
2914 O O   . ARG   B 140 ? 0.4319 0.4595 0.3518 -0.0685 0.0865  0.043   121 ARG   B O   
2915 C CB  . ARG   B 140 ? 0.3968 0.4276 0.3552 -0.0658 0.0721  0.0498  121 ARG   B CB  
2916 C CG  . ARG   B 140 ? 0.4241 0.4579 0.3991 -0.0672 0.0691  0.0545  121 ARG   B CG  
2917 C CD  . ARG   B 140 ? 0.4724 0.4973 0.4474 -0.0664 0.057   0.0573  121 ARG   B CD  
2918 N NE  . ARG   B 140 ? 0.5238 0.5496 0.5134 -0.0674 0.0529  0.0611  121 ARG   B NE  
2919 C CZ  . ARG   B 140 ? 0.5384 0.561  0.527  -0.0731 0.0506  0.0685  121 ARG   B CZ  
2920 N NH1 . ARG   B 140 ? 0.5173 0.5362 0.4908 -0.0784 0.0524  0.0734  121 ARG   B NH1 
2921 N NH2 . ARG   B 140 ? 0.5386 0.5611 0.5405 -0.0738 0.0461  0.0712  121 ARG   B NH2 
2922 N N   . VAL   B 141 ? 0.37   0.403  0.3136 -0.0584 0.0853  0.0333  122 VAL   B N   
2923 C CA  . VAL   B 141 ? 0.3805 0.4081 0.3099 -0.0564 0.0857  0.0273  122 VAL   B CA  
2924 C C   . VAL   B 141 ? 0.3725 0.4049 0.3094 -0.0513 0.0933  0.0196  122 VAL   B C   
2925 O O   . VAL   B 141 ? 0.3697 0.4093 0.3248 -0.0483 0.0959  0.019   122 VAL   B O   
2926 C CB  . VAL   B 141 ? 0.3949 0.4151 0.3218 -0.0546 0.074   0.0267  122 VAL   B CB  
2927 C CG1 . VAL   B 141 ? 0.4117 0.4269 0.3326 -0.0587 0.0658  0.0341  122 VAL   B CG1 
2928 C CG2 . VAL   B 141 ? 0.3913 0.4144 0.3365 -0.0492 0.0701  0.0236  122 VAL   B CG2 
2929 N N   . LYS   B 142 ? 0.3576 0.3852 0.2806 -0.0501 0.0962  0.0137  123 LYS   B N   
2930 C CA  . LYS   B 142 ? 0.3541 0.3835 0.2823 -0.0447 0.102   0.0059  123 LYS   B CA  
2931 C C   . LYS   B 142 ? 0.3535 0.3769 0.2835 -0.0412 0.0934  0.0018  123 LYS   B C   
2932 O O   . LYS   B 142 ? 0.3571 0.3754 0.2817 -0.0432 0.0843  0.0046  123 LYS   B O   
2933 C CB  . LYS   B 142 ? 0.3767 0.4042 0.2885 -0.0455 0.1114  0.0013  123 LYS   B CB  
2934 C CG  . LYS   B 142 ? 0.4113 0.4461 0.3222 -0.0489 0.1212  0.0051  123 LYS   B CG  
2935 C CD  . LYS   B 142 ? 0.4629 0.4953 0.3558 -0.0495 0.1311  0       123 LYS   B CD  
2936 C CE  . LYS   B 142 ? 0.5341 0.5742 0.4249 -0.0536 0.141   0.0044  123 LYS   B CE  
2937 N NZ  . LYS   B 142 ? 0.5783 0.6311 0.4933 -0.0504 0.1472  0.0049  123 LYS   B NZ  
2938 N N   . GLY   B 143 ? 0.353  0.377  0.2901 -0.0362 0.0968  -0.0045 124 GLY   B N   
2939 C CA  . GLY   B 143 ? 0.3581 0.3773 0.2985 -0.0329 0.0901  -0.0084 124 GLY   B CA  
2940 C C   . GLY   B 143 ? 0.372  0.3827 0.2974 -0.0355 0.0826  -0.0091 124 GLY   B C   
2941 O O   . GLY   B 143 ? 0.3664 0.3759 0.2972 -0.0353 0.0739  -0.0071 124 GLY   B O   
2942 N N   . PRO   B 144 ? 0.3734 0.3784 0.2801 -0.0378 0.0856  -0.0122 125 PRO   B N   
2943 C CA  . PRO   B 144 ? 0.3837 0.3807 0.2765 -0.0405 0.0775  -0.0129 125 PRO   B CA  
2944 C C   . PRO   B 144 ? 0.3769 0.3741 0.2689 -0.0439 0.0685  -0.0058 125 PRO   B C   
2945 O O   . PRO   B 144 ? 0.3811 0.3754 0.2735 -0.0441 0.0598  -0.0056 125 PRO   B O   
2946 C CB  . PRO   B 144 ? 0.418  0.4092 0.29   -0.0429 0.0834  -0.0168 125 PRO   B CB  
2947 C CG  . PRO   B 144 ? 0.4238 0.4189 0.3016 -0.0391 0.0949  -0.0213 125 PRO   B CG  
2948 C CD  . PRO   B 144 ? 0.3875 0.3927 0.2847 -0.0378 0.0966  -0.0158 125 PRO   B CD  
2949 N N   . GLU   B 145 ? 0.3726 0.3732 0.2642 -0.0466 0.0704  0.0002  126 GLU   B N   
2950 C CA  . GLU   B 145 ? 0.3543 0.3542 0.2456 -0.0495 0.062   0.0072  126 GLU   B CA  
2951 C C   . GLU   B 145 ? 0.349  0.3525 0.2592 -0.0461 0.0557  0.0088  126 GLU   B C   
2952 O O   . GLU   B 145 ? 0.3492 0.3507 0.2601 -0.0464 0.0468  0.0112  126 GLU   B O   
2953 C CB  . GLU   B 145 ? 0.3761 0.378  0.2629 -0.0534 0.0659  0.0134  126 GLU   B CB  
2954 C CG  . GLU   B 145 ? 0.4092 0.4091 0.2957 -0.0561 0.0568  0.0207  126 GLU   B CG  
2955 C CD  . GLU   B 145 ? 0.4991 0.4986 0.3774 -0.0612 0.0592  0.0276  126 GLU   B CD  
2956 O OE1 . GLU   B 145 ? 0.4955 0.4975 0.3681 -0.0631 0.0691  0.0268  126 GLU   B OE1 
2957 O OE2 . GLU   B 145 ? 0.5059 0.5024 0.3837 -0.0632 0.0512  0.0339  126 GLU   B OE2 
2958 N N   . LYS   B 146 ? 0.3381 0.3473 0.2636 -0.0429 0.0605  0.0076  127 LYS   B N   
2959 C CA  . LYS   B 146 ? 0.3154 0.3275 0.2577 -0.0395 0.0552  0.0085  127 LYS   B CA  
2960 C C   . LYS   B 146 ? 0.3082 0.3172 0.2511 -0.0372 0.0497  0.0042  127 LYS   B C   
2961 O O   . LYS   B 146 ? 0.2998 0.3087 0.248  -0.0364 0.0422  0.0062  127 LYS   B O   
2962 C CB  . LYS   B 146 ? 0.319  0.3373 0.2763 -0.0367 0.0615  0.0074  127 LYS   B CB  
2963 C CG  . LYS   B 146 ? 0.3697 0.3902 0.3428 -0.0327 0.0572  0.0064  127 LYS   B CG  
2964 C CD  . LYS   B 146 ? 0.4534 0.4779 0.4387 -0.033  0.0554  0.0113  127 LYS   B CD  
2965 C CE  . LYS   B 146 ? 0.4534 0.4744 0.4364 -0.0343 0.0468  0.0153  127 LYS   B CE  
2966 N NZ  . LYS   B 146 ? 0.3622 0.3852 0.3539 -0.0357 0.0449  0.0207  127 LYS   B NZ  
2967 N N   . GLU   B 147 ? 0.3098 0.3163 0.2472 -0.0361 0.0537  -0.0017 128 GLU   B N   
2968 C CA  . GLU   B 147 ? 0.2955 0.2988 0.233  -0.0347 0.0487  -0.0056 128 GLU   B CA  
2969 C C   . GLU   B 147 ? 0.3014 0.3015 0.2293 -0.0377 0.0409  -0.0035 128 GLU   B C   
2970 O O   . GLU   B 147 ? 0.3057 0.3064 0.2395 -0.0368 0.0345  -0.0035 128 GLU   B O   
2971 C CB  . GLU   B 147 ? 0.3345 0.3338 0.2657 -0.0335 0.054   -0.0122 128 GLU   B CB  
2972 C CG  . GLU   B 147 ? 0.3702 0.3727 0.3132 -0.0294 0.0607  -0.0149 128 GLU   B CG  
2973 C CD  . GLU   B 147 ? 0.4414 0.4387 0.3798 -0.0273 0.0645  -0.0218 128 GLU   B CD  
2974 O OE1 . GLU   B 147 ? 0.4649 0.4554 0.3894 -0.0297 0.0624  -0.0248 128 GLU   B OE1 
2975 O OE2 . GLU   B 147 ? 0.4443 0.4436 0.3929 -0.0234 0.0693  -0.0242 128 GLU   B OE2 
2976 N N   . GLU   B 148 ? 0.3042 0.301  0.217  -0.0415 0.0413  -0.0018 129 GLU   B N   
2977 C CA  . GLU   B 148 ? 0.3223 0.3161 0.226  -0.0445 0.0331  0.0006  129 GLU   B CA  
2978 C C   . GLU   B 148 ? 0.3141 0.3113 0.228  -0.0437 0.0262  0.0063  129 GLU   B C   
2979 O O   . GLU   B 148 ? 0.3242 0.3217 0.2401 -0.0436 0.0186  0.007   129 GLU   B O   
2980 C CB  . GLU   B 148 ? 0.3638 0.3527 0.2482 -0.0489 0.0347  0.0017  129 GLU   B CB  
2981 C CG  . GLU   B 148 ? 0.3771 0.3628 0.2516 -0.0522 0.0253  0.0048  129 GLU   B CG  
2982 C CD  . GLU   B 148 ? 0.4213 0.4046 0.2932 -0.0527 0.0194  0.0008  129 GLU   B CD  
2983 O OE1 . GLU   B 148 ? 0.4228 0.4053 0.2981 -0.0509 0.0229  -0.0049 129 GLU   B OE1 
2984 O OE2 . GLU   B 148 ? 0.4582 0.4404 0.3253 -0.055  0.0108  0.0038  129 GLU   B OE2 
2985 N N   . LYS   B 149 ? 0.3185 0.3186 0.2396 -0.043  0.0288  0.0102  130 LYS   B N   
2986 C CA  . LYS   B 149 ? 0.3157 0.3178 0.2465 -0.0418 0.0224  0.0152  130 LYS   B CA  
2987 C C   . LYS   B 149 ? 0.2961 0.3014 0.2408 -0.0378 0.0189  0.0128  130 LYS   B C   
2988 O O   . LYS   B 149 ? 0.2952 0.3012 0.2436 -0.0368 0.0117  0.0146  130 LYS   B O   
2989 C CB  . LYS   B 149 ? 0.3516 0.3555 0.2881 -0.0421 0.0262  0.0192  130 LYS   B CB  
2990 C CG  . LYS   B 149 ? 0.416  0.4195 0.3588 -0.0415 0.0189  0.0245  130 LYS   B CG  
2991 C CD  . LYS   B 149 ? 0.4776 0.4807 0.4214 -0.0437 0.0213  0.0297  130 LYS   B CD  
2992 C CE  . LYS   B 149 ? 0.542  0.5408 0.4826 -0.0451 0.0135  0.0357  130 LYS   B CE  
2993 N NZ  . LYS   B 149 ? 0.5551 0.5529 0.4969 -0.0479 0.0158  0.0411  130 LYS   B NZ  
2994 N N   . LEU   B 150 ? 0.273  0.2802 0.2244 -0.0355 0.0241  0.0084  131 LEU   B N   
2995 C CA  . LEU   B 150 ? 0.2571 0.2669 0.22   -0.0322 0.0213  0.0061  131 LEU   B CA  
2996 C C   . LEU   B 150 ? 0.2563 0.265  0.2147 -0.0331 0.0166  0.0038  131 LEU   B C   
2997 O O   . LEU   B 150 ? 0.2543 0.2656 0.2195 -0.0316 0.0111  0.0047  131 LEU   B O   
2998 C CB  . LEU   B 150 ? 0.2584 0.2696 0.2289 -0.0297 0.0273  0.0026  131 LEU   B CB  
2999 C CG  . LEU   B 150 ? 0.2549 0.268  0.2356 -0.0268 0.0247  0.0004  131 LEU   B CG  
3000 C CD1 . LEU   B 150 ? 0.2544 0.2702 0.244  -0.025  0.0195  0.0037  131 LEU   B CD1 
3001 C CD2 . LEU   B 150 ? 0.2635 0.2773 0.2512 -0.0244 0.0301  -0.0025 131 LEU   B CD2 
3002 N N   . ARG   B 151 ? 0.2707 0.2757 0.2172 -0.0357 0.0185  0.0007  132 ARG   B N   
3003 C CA  . ARG   B 151 ? 0.2793 0.283  0.2212 -0.0374 0.0135  -0.0014 132 ARG   B CA  
3004 C C   . ARG   B 151 ? 0.295  0.3003 0.2357 -0.0387 0.0055  0.0029  132 ARG   B C   
3005 O O   . ARG   B 151 ? 0.2986 0.3069 0.2446 -0.0384 0.0001  0.0025  132 ARG   B O   
3006 C CB  . ARG   B 151 ? 0.3038 0.3016 0.2312 -0.0403 0.0166  -0.0053 132 ARG   B CB  
3007 C CG  . ARG   B 151 ? 0.3145 0.3104 0.2449 -0.0382 0.0233  -0.0104 132 ARG   B CG  
3008 C CD  . ARG   B 151 ? 0.3511 0.34   0.2665 -0.0407 0.0264  -0.0152 132 ARG   B CD  
3009 N NE  . ARG   B 151 ? 0.3453 0.3317 0.2649 -0.0381 0.0314  -0.0203 132 ARG   B NE  
3010 C CZ  . ARG   B 151 ? 0.3356 0.3196 0.2525 -0.0363 0.0394  -0.0233 132 ARG   B CZ  
3011 N NH1 . ARG   B 151 ? 0.3565 0.3406 0.2654 -0.0373 0.0439  -0.0219 132 ARG   B NH1 
3012 N NH2 . ARG   B 151 ? 0.3413 0.3229 0.2634 -0.0334 0.043   -0.0276 132 ARG   B NH2 
3013 N N   . GLN   B 152 ? 0.2903 0.294  0.2246 -0.0401 0.0045  0.0071  133 GLN   B N   
3014 C CA  . GLN   B 152 ? 0.2955 0.3001 0.2292 -0.0408 -0.0037 0.0116  133 GLN   B CA  
3015 C C   . GLN   B 152 ? 0.3167 0.3261 0.2655 -0.0368 -0.0073 0.0138  133 GLN   B C   
3016 O O   . GLN   B 152 ? 0.334  0.346  0.2864 -0.0361 -0.0143 0.0158  133 GLN   B O   
3017 C CB  . GLN   B 152 ? 0.3053 0.3056 0.2271 -0.0437 -0.0043 0.0161  133 GLN   B CB  
3018 C CG  . GLN   B 152 ? 0.3668 0.3618 0.2707 -0.0481 -0.002  0.0141  133 GLN   B CG  
3019 C CD  . GLN   B 152 ? 0.4125 0.4067 0.3106 -0.0503 -0.0095 0.0131  133 GLN   B CD  
3020 O OE1 . GLN   B 152 ? 0.4212 0.4185 0.3254 -0.0495 -0.0176 0.0164  133 GLN   B OE1 
3021 N NE2 . GLN   B 152 ? 0.4183 0.4083 0.3046 -0.0532 -0.007  0.0086  133 GLN   B NE2 
3022 N N   . ALA   B 153 ? 0.2997 0.3106 0.2577 -0.034  -0.0026 0.0132  134 ALA   B N   
3023 C CA  . ALA   B 153 ? 0.271  0.2854 0.2421 -0.03   -0.0056 0.0149  134 ALA   B CA  
3024 C C   . ALA   B 153 ? 0.2596 0.2787 0.2396 -0.0278 -0.0072 0.0117  134 ALA   B C   
3025 O O   . ALA   B 153 ? 0.2643 0.2868 0.2526 -0.025  -0.0116 0.013   134 ALA   B O   
3026 C CB  . ALA   B 153 ? 0.2718 0.2855 0.2488 -0.0284 -0.0007 0.0155  134 ALA   B CB  
3027 N N   . VAL   B 154 ? 0.2681 0.2872 0.2462 -0.029  -0.0037 0.0075  135 VAL   B N   
3028 C CA  . VAL   B 154 ? 0.2755 0.2988 0.2617 -0.0276 -0.0045 0.0048  135 VAL   B CA  
3029 C C   . VAL   B 154 ? 0.3184 0.3444 0.3026 -0.0298 -0.01   0.0047  135 VAL   B C   
3030 O O   . VAL   B 154 ? 0.3322 0.3551 0.307  -0.0335 -0.0099 0.003   135 VAL   B O   
3031 C CB  . VAL   B 154 ? 0.2529 0.2742 0.2394 -0.0277 0.0015  0.0009  135 VAL   B CB  
3032 C CG1 . VAL   B 154 ? 0.2501 0.2753 0.2445 -0.0267 0.0006  -0.0012 135 VAL   B CG1 
3033 C CG2 . VAL   B 154 ? 0.2662 0.2861 0.2565 -0.0254 0.0063  0.0013  135 VAL   B CG2 
3034 N N   . LYS   B 155 ? 0.3416 0.3736 0.3346 -0.0278 -0.015  0.0063  136 LYS   B N   
3035 C CA  . LYS   B 155 ? 0.3594 0.3957 0.3526 -0.03   -0.0206 0.0064  136 LYS   B CA  
3036 C C   . LYS   B 155 ? 0.3421 0.3847 0.3446 -0.0297 -0.0203 0.0041  136 LYS   B C   
3037 O O   . LYS   B 155 ? 0.3783 0.4239 0.3802 -0.033  -0.0235 0.0033  136 LYS   B O   
3038 C CB  . LYS   B 155 ? 0.4006 0.4402 0.397  -0.0283 -0.0274 0.0104  136 LYS   B CB  
3039 C CG  . LYS   B 155 ? 0.4969 0.5299 0.4834 -0.0293 -0.0287 0.0137  136 LYS   B CG  
3040 C CD  . LYS   B 155 ? 0.5771 0.6047 0.5487 -0.0346 -0.0286 0.0129  136 LYS   B CD  
3041 C CE  . LYS   B 155 ? 0.6404 0.6623 0.6012 -0.0362 -0.0313 0.017   136 LYS   B CE  
3042 N NZ  . LYS   B 155 ? 0.6844 0.7044 0.6493 -0.033  -0.0292 0.0198  136 LYS   B NZ  
3043 N N   . GLN   B 156 ? 0.2819 0.3266 0.2928 -0.0262 -0.0165 0.0031  137 GLN   B N   
3044 C CA  . GLN   B 156 ? 0.2403 0.291  0.2595 -0.0261 -0.0156 0.0013  137 GLN   B CA  
3045 C C   . GLN   B 156 ? 0.2152 0.2622 0.2347 -0.0254 -0.0097 -0.0011 137 GLN   B C   
3046 O O   . GLN   B 156 ? 0.2115 0.2545 0.2305 -0.0229 -0.0067 -0.0009 137 GLN   B O   
3047 C CB  . GLN   B 156 ? 0.2524 0.3111 0.2829 -0.0219 -0.018  0.0028  137 GLN   B CB  
3048 C CG  . GLN   B 156 ? 0.2872 0.3495 0.319  -0.0214 -0.0246 0.0057  137 GLN   B CG  
3049 C CD  . GLN   B 156 ? 0.3629 0.4329 0.4065 -0.0164 -0.0267 0.0068  137 GLN   B CD  
3050 O OE1 . GLN   B 156 ? 0.37   0.4482 0.4223 -0.0159 -0.026  0.0056  137 GLN   B OE1 
3051 N NE2 . GLN   B 156 ? 0.4005 0.4674 0.4443 -0.0126 -0.029  0.009   137 GLN   B NE2 
3052 N N   . VAL   B 157 ? 0.2088 0.2567 0.2289 -0.0282 -0.0085 -0.0032 138 VAL   B N   
3053 C CA  . VAL   B 157 ? 0.213  0.257  0.2331 -0.0282 -0.0038 -0.0053 138 VAL   B CA  
3054 C C   . VAL   B 157 ? 0.2215 0.2726 0.2498 -0.0285 -0.0041 -0.0053 138 VAL   B C   
3055 O O   . VAL   B 157 ? 0.2413 0.2957 0.27   -0.0324 -0.0064 -0.0056 138 VAL   B O   
3056 C CB  . VAL   B 157 ? 0.2425 0.2791 0.2532 -0.0321 -0.0025 -0.0076 138 VAL   B CB  
3057 C CG1 . VAL   B 157 ? 0.2753 0.3074 0.2866 -0.032  0.0016  -0.0097 138 VAL   B CG1 
3058 C CG2 . VAL   B 157 ? 0.2476 0.2784 0.2498 -0.0319 -0.0016 -0.0076 138 VAL   B CG2 
3059 N N   . LEU   B 158 ? 0.2029 0.2566 0.2373 -0.0248 -0.002  -0.005  139 LEU   B N   
3060 C CA  . LEU   B 158 ? 0.189  0.2509 0.2314 -0.0244 -0.0019 -0.0047 139 LEU   B CA  
3061 C C   . LEU   B 158 ? 0.1812 0.2411 0.2245 -0.024  0.002   -0.0056 139 LEU   B C   
3062 O O   . LEU   B 158 ? 0.1764 0.2303 0.2174 -0.0216 0.0042  -0.0061 139 LEU   B O   
3063 C CB  . LEU   B 158 ? 0.1979 0.2658 0.2468 -0.0194 -0.0034 -0.0034 139 LEU   B CB  
3064 C CG  . LEU   B 158 ? 0.2343 0.3046 0.2834 -0.019  -0.0081 -0.0018 139 LEU   B CG  
3065 C CD1 . LEU   B 158 ? 0.2348 0.3093 0.2905 -0.0136 -0.0096 -0.0007 139 LEU   B CD1 
3066 C CD2 . LEU   B 158 ? 0.2392 0.3165 0.291  -0.0231 -0.0115 -0.0013 139 LEU   B CD2 
3067 N N   . LYS   B 159 ? 0.1804 0.2463 0.2279 -0.0263 0.0025  -0.0054 140 LYS   B N   
3068 C CA  . LYS   B 159 ? 0.1756 0.2409 0.2241 -0.026  0.0059  -0.0057 140 LYS   B CA  
3069 C C   . LYS   B 159 ? 0.1839 0.2523 0.2363 -0.0205 0.0072  -0.0056 140 LYS   B C   
3070 O O   . LYS   B 159 ? 0.2007 0.2762 0.2585 -0.0176 0.0057  -0.0052 140 LYS   B O   
3071 C CB  . LYS   B 159 ? 0.1962 0.2689 0.2487 -0.0304 0.006   -0.005  140 LYS   B CB  
3072 C CG  . LYS   B 159 ? 0.2861 0.3599 0.3396 -0.0305 0.0096  -0.0046 140 LYS   B CG  
3073 C CD  . LYS   B 159 ? 0.3711 0.4342 0.4176 -0.0335 0.0105  -0.0049 140 LYS   B CD  
3074 C CE  . LYS   B 159 ? 0.4063 0.4706 0.4529 -0.0382 0.0121  -0.0036 140 LYS   B CE  
3075 N NZ  . LYS   B 159 ? 0.3805 0.4382 0.4231 -0.0369 0.0146  -0.0033 140 LYS   B NZ  
3076 N N   A CYS   B 160 ? 0.1803 0.2428 0.2298 -0.0188 0.0095  -0.006  141 CYS   B N   
3077 N N   B CYS   B 160 ? 0.1873 0.2497 0.2367 -0.019  0.0095  -0.006  141 CYS   B N   
3078 C CA  A CYS   B 160 ? 0.1733 0.2376 0.2252 -0.0142 0.0106  -0.0064 141 CYS   B CA  
3079 C CA  B CYS   B 160 ? 0.1848 0.2479 0.236  -0.0143 0.0105  -0.0064 141 CYS   B CA  
3080 C C   A CYS   B 160 ? 0.1586 0.2204 0.208  -0.0148 0.0133  -0.0065 141 CYS   B C   
3081 C C   B CYS   B 160 ? 0.1623 0.2232 0.2113 -0.0146 0.0132  -0.0065 141 CYS   B C   
3082 O O   A CYS   B 160 ? 0.1768 0.2327 0.2221 -0.018  0.014   -0.0061 141 CYS   B O   
3083 O O   B CYS   B 160 ? 0.1765 0.2307 0.2213 -0.0171 0.0138  -0.0063 141 CYS   B O   
3084 C CB  A CYS   B 160 ? 0.1906 0.2496 0.2412 -0.0104 0.0092  -0.0065 141 CYS   B CB  
3085 C CB  B CYS   B 160 ? 0.214  0.2702 0.2627 -0.0115 0.0093  -0.0065 141 CYS   B CB  
3086 S SG  A CYS   B 160 ? 0.1869 0.235  0.232  -0.0107 0.0103  -0.0067 141 CYS   B SG  
3087 S SG  B CYS   B 160 ? 0.2291 0.2824 0.2781 -0.0065 0.0098  -0.0071 141 CYS   B SG  
3088 N N   . ASP   B 161 ? 0.1542 0.2196 0.2053 -0.0116 0.0148  -0.007  142 ASP   B N   
3089 C CA  . ASP   B 161 ? 0.1471 0.2092 0.1942 -0.0118 0.017   -0.0071 142 ASP   B CA  
3090 C C   . ASP   B 161 ? 0.151  0.2119 0.1977 -0.0065 0.017   -0.0084 142 ASP   B C   
3091 O O   . ASP   B 161 ? 0.1506 0.2184 0.2009 -0.0036 0.018   -0.0095 142 ASP   B O   
3092 C CB  . ASP   B 161 ? 0.1572 0.2265 0.2055 -0.0151 0.0198  -0.0064 142 ASP   B CB  
3093 C CG  . ASP   B 161 ? 0.1789 0.2444 0.2214 -0.0158 0.0221  -0.006  142 ASP   B CG  
3094 O OD1 . ASP   B 161 ? 0.1801 0.2378 0.2183 -0.0131 0.0212  -0.0065 142 ASP   B OD1 
3095 O OD2 . ASP   B 161 ? 0.2139 0.2843 0.2562 -0.0193 0.0247  -0.0049 142 ASP   B OD2 
3096 N N   . VAL   B 162 ? 0.1585 0.2106 0.2014 -0.0051 0.0156  -0.0086 143 VAL   B N   
3097 C CA  . VAL   B 162 ? 0.1626 0.2118 0.2047 -0.0005 0.0146  -0.0099 143 VAL   B CA  
3098 C C   . VAL   B 162 ? 0.1758 0.227  0.215  0.001   0.0169  -0.0112 143 VAL   B C   
3099 O O   . VAL   B 162 ? 0.179  0.2285 0.2173 0.0051  0.0162  -0.013  143 VAL   B O   
3100 C CB  . VAL   B 162 ? 0.1753 0.2153 0.2147 -0.0002 0.0123  -0.0094 143 VAL   B CB  
3101 C CG1 . VAL   B 162 ? 0.1865 0.225  0.2283 -0.0015 0.0109  -0.0083 143 VAL   B CG1 
3102 C CG2 . VAL   B 162 ? 0.1905 0.2254 0.225  -0.0023 0.0128  -0.0086 143 VAL   B CG2 
3103 N N   . THR   B 163 ? 0.172  0.2256 0.2085 -0.0024 0.0196  -0.0103 144 THR   B N   
3104 C CA  . THR   B 163 ? 0.1892 0.2442 0.2211 -0.0013 0.0224  -0.0115 144 THR   B CA  
3105 C C   . THR   B 163 ? 0.2024 0.2687 0.2396 0.0007  0.0256  -0.013  144 THR   B C   
3106 O O   . THR   B 163 ? 0.2292 0.2979 0.2628 0.0022  0.0288  -0.0144 144 THR   B O   
3107 C CB  . THR   B 163 ? 0.2165 0.2688 0.2426 -0.0061 0.024   -0.0094 144 THR   B CB  
3108 O OG1 . THR   B 163 ? 0.2225 0.2823 0.2527 -0.0102 0.026   -0.0079 144 THR   B OG1 
3109 C CG2 . THR   B 163 ? 0.2413 0.283  0.2635 -0.0077 0.0207  -0.0078 144 THR   B CG2 
3110 N N   . GLN   B 164 ? 0.1844 0.2577 0.2297 0.0008  0.0247  -0.0126 145 GLN   B N   
3111 C CA  . GLN   B 164 ? 0.1964 0.2817 0.2488 0.0029  0.0273  -0.0137 145 GLN   B CA  
3112 C C   . GLN   B 164 ? 0.1998 0.2854 0.2562 0.0093  0.0253  -0.0159 145 GLN   B C   
3113 O O   . GLN   B 164 ? 0.1937 0.273  0.2506 0.0106  0.0212  -0.0155 145 GLN   B O   
3114 C CB  . GLN   B 164 ? 0.2155 0.3088 0.2747 -0.0014 0.0269  -0.0116 145 GLN   B CB  
3115 C CG  . GLN   B 164 ? 0.2432 0.3353 0.2985 -0.0083 0.0284  -0.0092 145 GLN   B CG  
3116 C CD  . GLN   B 164 ? 0.2859 0.3811 0.3371 -0.0093 0.0332  -0.0093 145 GLN   B CD  
3117 O OE1 . GLN   B 164 ? 0.3127 0.3991 0.355  -0.0105 0.0336  -0.0089 145 GLN   B OE1 
3118 N NE2 . GLN   B 164 ? 0.2638 0.3715 0.3216 -0.0082 0.0368  -0.01   145 GLN   B NE2 
3119 N N   . SER   B 165 ? 0.1973 0.2912 0.2576 0.0134  0.0285  -0.0182 146 SER   B N   
3120 C CA  . SER   B 165 ? 0.2093 0.3032 0.274  0.0202  0.0266  -0.0206 146 SER   B CA  
3121 C C   . SER   B 165 ? 0.2202 0.316  0.2925 0.0205  0.0219  -0.0188 146 SER   B C   
3122 O O   . SER   B 165 ? 0.2459 0.3357 0.3186 0.0247  0.0182  -0.0195 146 SER   B O   
3123 C CB  . SER   B 165 ? 0.2547 0.3601 0.3251 0.0245  0.0313  -0.0232 146 SER   B CB  
3124 O OG  . SER   B 165 ? 0.3167 0.4196 0.3784 0.0245  0.0358  -0.0251 146 SER   B OG  
3125 N N   . GLN   B 166 ? 0.226  0.3299 0.3037 0.0159  0.0218  -0.0163 147 GLN   B N   
3126 C CA  . GLN   B 166 ? 0.2124 0.3176 0.2952 0.0148  0.0171  -0.0142 147 GLN   B CA  
3127 C C   . GLN   B 166 ? 0.2054 0.3037 0.2818 0.0081  0.016   -0.012  147 GLN   B C   
3128 O O   . GLN   B 166 ? 0.2057 0.3093 0.2835 0.003   0.0173  -0.0106 147 GLN   B O   
3129 C CB  . GLN   B 166 ? 0.2644 0.3844 0.358  0.014   0.0176  -0.0133 147 GLN   B CB  
3130 C CG  . GLN   B 166 ? 0.3496 0.4773 0.4523 0.0212  0.0171  -0.0151 147 GLN   B CG  
3131 C CD  . GLN   B 166 ? 0.4685 0.601  0.5718 0.0252  0.0229  -0.0182 147 GLN   B CD  
3132 O OE1 . GLN   B 166 ? 0.5037 0.6313 0.6054 0.0318  0.0232  -0.0211 147 GLN   B OE1 
3133 N NE2 . GLN   B 166 ? 0.488  0.6295 0.5929 0.0211  0.0278  -0.0177 147 GLN   B NE2 
3134 N N   . PRO   B 167 ? 0.194  0.2807 0.2639 0.0081  0.0137  -0.0117 148 PRO   B N   
3135 C CA  . PRO   B 167 ? 0.1862 0.2667 0.2508 0.0026  0.0133  -0.0101 148 PRO   B CA  
3136 C C   . PRO   B 167 ? 0.1986 0.2829 0.2658 -0.0015 0.0113  -0.0084 148 PRO   B C   
3137 O O   . PRO   B 167 ? 0.1946 0.2762 0.2584 -0.0064 0.0119  -0.0075 148 PRO   B O   
3138 C CB  . PRO   B 167 ? 0.2021 0.2715 0.2618 0.0044  0.011   -0.0101 148 PRO   B CB  
3139 C CG  . PRO   B 167 ? 0.2324 0.3002 0.2921 0.0098  0.0112  -0.0121 148 PRO   B CG  
3140 C CD  . PRO   B 167 ? 0.2025 0.2809 0.2698 0.0129  0.0116  -0.0129 148 PRO   B CD  
3141 N N   . LEU   B 168 ? 0.1961 0.2855 0.2688 0.0005  0.0083  -0.0079 149 LEU   B N   
3142 C CA  . LEU   B 168 ? 0.2138 0.3063 0.2881 -0.0035 0.0056  -0.0063 149 LEU   B CA  
3143 C C   . LEU   B 168 ? 0.213  0.3183 0.2953 -0.0055 0.0062  -0.0058 149 LEU   B C   
3144 O O   . LEU   B 168 ? 0.2324 0.3415 0.3172 -0.0086 0.0029  -0.0045 149 LEU   B O   
3145 C CB  . LEU   B 168 ? 0.2337 0.3235 0.3084 -0.0013 0.0011  -0.0053 149 LEU   B CB  
3146 C CG  . LEU   B 168 ? 0.2467 0.3249 0.3147 0.0004  0.0006  -0.0053 149 LEU   B CG  
3147 C CD1 . LEU   B 168 ? 0.2657 0.3416 0.3337 0.0021  -0.0038 -0.0036 149 LEU   B CD1 
3148 C CD2 . LEU   B 168 ? 0.2456 0.3166 0.3066 -0.0038 0.0023  -0.0052 149 LEU   B CD2 
3149 N N   . GLY   B 169 ? 0.2223 0.3335 0.3075 -0.0046 0.0104  -0.0068 150 GLY   B N   
3150 C CA  . GLY   B 169 ? 0.2508 0.3754 0.3443 -0.007  0.0121  -0.0062 150 GLY   B CA  
3151 C C   . GLY   B 169 ? 0.2678 0.4031 0.372  -0.0037 0.0091  -0.0058 150 GLY   B C   
3152 O O   . GLY   B 169 ? 0.2643 0.4005 0.3719 0.0031  0.0086  -0.0071 150 GLY   B O   
3153 N N   . ALA   B 170 ? 0.2733 0.4164 0.383  -0.0083 0.0064  -0.0041 151 ALA   B N   
3154 C CA  . ALA   B 170 ? 0.2856 0.44   0.4068 -0.0055 0.0027  -0.0032 151 ALA   B CA  
3155 C C   . ALA   B 170 ? 0.2983 0.4457 0.4167 -0.0034 -0.0036 -0.0023 151 ALA   B C   
3156 O O   . ALA   B 170 ? 0.3044 0.459  0.4315 0.0007  -0.0072 -0.0016 151 ALA   B O   
3157 C CB  . ALA   B 170 ? 0.2796 0.4464 0.409  -0.0116 0.0017  -0.0014 151 ALA   B CB  
3158 N N   . VAL   B 171 ? 0.2879 0.4213 0.3943 -0.0057 -0.0049 -0.0021 152 VAL   B N   
3159 C CA  . VAL   B 171 ? 0.3032 0.4298 0.4056 -0.0048 -0.0105 -0.0008 152 VAL   B CA  
3160 C C   . VAL   B 171 ? 0.3217 0.444  0.4247 0.0025  -0.0115 -0.0012 152 VAL   B C   
3161 O O   . VAL   B 171 ? 0.3378 0.4517 0.4351 0.0049  -0.0084 -0.0027 152 VAL   B O   
3162 C CB  . VAL   B 171 ? 0.3182 0.4323 0.4079 -0.01   -0.0107 -0.0006 152 VAL   B CB  
3163 C CG1 . VAL   B 171 ? 0.3365 0.4436 0.4206 -0.0095 -0.0158 0.0009  152 VAL   B CG1 
3164 C CG2 . VAL   B 171 ? 0.3257 0.4422 0.414  -0.0172 -0.0105 -0.0004 152 VAL   B CG2 
3165 N N   . PRO   B 172 ? 0.3184 0.4448 0.4274 0.0057  -0.0168 0.0003  153 PRO   B N   
3166 C CA  . PRO   B 172 ? 0.3364 0.4569 0.4453 0.0124  -0.0187 0.0002  153 PRO   B CA  
3167 C C   . PRO   B 172 ? 0.3319 0.4394 0.43   0.0105  -0.0222 0.0021  153 PRO   B C   
3168 O O   . PRO   B 172 ? 0.3801 0.4861 0.4734 0.0054  -0.0254 0.0041  153 PRO   B O   
3169 C CB  . PRO   B 172 ? 0.339  0.4703 0.4602 0.0167  -0.0232 0.0014  153 PRO   B CB  
3170 C CG  . PRO   B 172 ? 0.3331 0.4714 0.4562 0.0102  -0.0268 0.0036  153 PRO   B CG  
3171 C CD  . PRO   B 172 ? 0.3087 0.4455 0.4256 0.0035  -0.0218 0.0024  153 PRO   B CD  
3172 N N   . LEU   B 173 ? 0.2786 0.3769 0.3725 0.0142  -0.0214 0.0016  154 LEU   B N   
3173 C CA  . LEU   B 173 ? 0.2652 0.352  0.35   0.0128  -0.0244 0.0037  154 LEU   B CA  
3174 C C   . LEU   B 173 ? 0.2415 0.3235 0.3288 0.0192  -0.027  0.0041  154 LEU   B C   
3175 O O   . LEU   B 173 ? 0.2344 0.3176 0.3261 0.0241  -0.0242 0.0014  154 LEU   B O   
3176 C CB  . LEU   B 173 ? 0.2726 0.3504 0.3482 0.0095  -0.0198 0.0026  154 LEU   B CB  
3177 C CG  . LEU   B 173 ? 0.306  0.3833 0.3757 0.0031  -0.0176 0.0025  154 LEU   B CG  
3178 C CD1 . LEU   B 173 ? 0.2891 0.3566 0.3509 0.0016  -0.014  0.0018  154 LEU   B CD1 
3179 C CD2 . LEU   B 173 ? 0.325  0.4012 0.3902 -0.0006 -0.0221 0.005   154 LEU   B CD2 
3180 N N   . PRO   B 174 ? 0.248  0.3224 0.3304 0.0189  -0.0319 0.0073  155 PRO   B N   
3181 C CA  . PRO   B 174 ? 0.2576 0.3245 0.3407 0.0243  -0.0346 0.0079  155 PRO   B CA  
3182 C C   . PRO   B 174 ? 0.2355 0.2945 0.3139 0.0247  -0.03   0.0056  155 PRO   B C   
3183 O O   . PRO   B 174 ? 0.2331 0.2899 0.3055 0.0198  -0.0261 0.0051  155 PRO   B O   
3184 C CB  . PRO   B 174 ? 0.2848 0.3435 0.3602 0.0213  -0.0397 0.0124  155 PRO   B CB  
3185 C CG  . PRO   B 174 ? 0.306  0.3703 0.3789 0.0159  -0.0409 0.0138  155 PRO   B CG  
3186 C CD  . PRO   B 174 ? 0.2705 0.3416 0.3452 0.0133  -0.0351 0.0104  155 PRO   B CD  
3187 N N   . PRO   B 175 ? 0.2366 0.2905 0.3175 0.0304  -0.0308 0.0042  156 PRO   B N   
3188 C CA  . PRO   B 175 ? 0.2467 0.2921 0.3227 0.0304  -0.0277 0.0023  156 PRO   B CA  
3189 C C   . PRO   B 175 ? 0.2337 0.2701 0.3012 0.0251  -0.0287 0.0056  156 PRO   B C   
3190 O O   . PRO   B 175 ? 0.2531 0.2855 0.3182 0.024   -0.0331 0.0094  156 PRO   B O   
3191 C CB  . PRO   B 175 ? 0.2711 0.3113 0.3507 0.0374  -0.0304 0.0008  156 PRO   B CB  
3192 C CG  . PRO   B 175 ? 0.2841 0.3347 0.3733 0.0423  -0.0323 0.0002  156 PRO   B CG  
3193 C CD  . PRO   B 175 ? 0.2496 0.3046 0.3378 0.0372  -0.0352 0.0042  156 PRO   B CD  
3194 N N   . ALA   B 176 ? 0.1983 0.2324 0.2615 0.0215  -0.0243 0.0045  157 ALA   B N   
3195 C CA  . ALA   B 176 ? 0.1963 0.224  0.2529 0.0165  -0.0241 0.0072  157 ALA   B CA  
3196 C C   . ALA   B 176 ? 0.1785 0.1959 0.233  0.0174  -0.0262 0.0086  157 ALA   B C   
3197 O O   . ALA   B 176 ? 0.1935 0.2075 0.2504 0.0215  -0.0268 0.0062  157 ALA   B O   
3198 C CB  . ALA   B 176 ? 0.2002 0.2302 0.2542 0.0126  -0.0187 0.0054  157 ALA   B CB  
3199 N N   . ASP   B 177 ? 0.1713 0.1836 0.2207 0.0132  -0.0271 0.0123  158 ASP   B N   
3200 C CA  . ASP   B 177 ? 0.2    0.2028 0.2474 0.0124  -0.0287 0.0141  158 ASP   B CA  
3201 C C   . ASP   B 177 ? 0.2068 0.2089 0.2539 0.0101  -0.0244 0.0122  158 ASP   B C   
3202 O O   . ASP   B 177 ? 0.2136 0.2089 0.261  0.0103  -0.0257 0.0124  158 ASP   B O   
3203 C CB  . ASP   B 177 ? 0.2239 0.2225 0.266  0.0082  -0.0308 0.0193  158 ASP   B CB  
3204 C CG  . ASP   B 177 ? 0.2763 0.275  0.3185 0.0105  -0.036  0.0215  158 ASP   B CG  
3205 O OD1 . ASP   B 177 ? 0.316  0.3096 0.3611 0.0149  -0.0405 0.0217  158 ASP   B OD1 
3206 O OD2 . ASP   B 177 ? 0.2653 0.2695 0.3052 0.0084  -0.0359 0.0225  158 ASP   B OD2 
3207 N N   . CYS   B 178 ? 0.1836 0.1919 0.2301 0.0076  -0.0199 0.0107  159 CYS   B N   
3208 C CA  . CYS   B 178 ? 0.1749 0.183  0.2218 0.0058  -0.0162 0.0091  159 CYS   B CA  
3209 C C   . CYS   B 178 ? 0.1633 0.1786 0.211  0.0058  -0.0125 0.0061  159 CYS   B C   
3210 O O   . CYS   B 178 ? 0.1691 0.1892 0.2155 0.0045  -0.0116 0.0064  159 CYS   B O   
3211 C CB  . CYS   B 178 ? 0.1862 0.1924 0.2305 0.001   -0.0144 0.0122  159 CYS   B CB  
3212 S SG  . CYS   B 178 ? 0.2059 0.2129 0.2525 -0.0012 -0.0102 0.0108  159 CYS   B SG  
3213 N N   . VAL   B 179 ? 0.1555 0.1706 0.2047 0.0069  -0.0107 0.0035  160 VAL   B N   
3214 C CA  . VAL   B 179 ? 0.1488 0.1689 0.1981 0.006   -0.007  0.0012  160 VAL   B CA  
3215 C C   . VAL   B 179 ? 0.1506 0.1683 0.1997 0.0035  -0.0049 0.0015  160 VAL   B C   
3216 O O   . VAL   B 179 ? 0.1677 0.1808 0.2178 0.0042  -0.0065 0.0017  160 VAL   B O   
3217 C CB  . VAL   B 179 ? 0.1701 0.1927 0.2209 0.0095  -0.0067 -0.0019 160 VAL   B CB  
3218 C CG1 . VAL   B 179 ? 0.1893 0.215  0.2394 0.0078  -0.0032 -0.0035 160 VAL   B CG1 
3219 C CG2 . VAL   B 179 ? 0.1813 0.2091 0.2342 0.0118  -0.008  -0.0022 160 VAL   B CG2 
3220 N N   . LEU   B 180 ? 0.1458 0.1661 0.1938 0.0008  -0.0019 0.0017  161 LEU   B N   
3221 C CA  . LEU   B 180 ? 0.152  0.1709 0.2009 -0.0012 0.0005  0.002   161 LEU   B CA  
3222 C C   . LEU   B 180 ? 0.1527 0.1738 0.2014 -0.0013 0.0028  -0.0002 161 LEU   B C   
3223 O O   . LEU   B 180 ? 0.164  0.1883 0.2109 -0.0017 0.0039  -0.0012 161 LEU   B O   
3224 C CB  . LEU   B 180 ? 0.1551 0.1747 0.202  -0.0041 0.0026  0.0038  161 LEU   B CB  
3225 C CG  . LEU   B 180 ? 0.1592 0.179  0.2077 -0.0059 0.0061  0.0038  161 LEU   B CG  
3226 C CD1 . LEU   B 180 ? 0.1703 0.1879 0.2236 -0.0059 0.0049  0.0053  161 LEU   B CD1 
3227 C CD2 . LEU   B 180 ? 0.182  0.2028 0.2268 -0.0084 0.0089  0.0049  161 LEU   B CD2 
3228 N N   . SER   B 181 ? 0.1452 0.1643 0.1959 -0.0012 0.0032  -0.0006 162 SER   B N   
3229 C CA  . SER   B 181 ? 0.1487 0.1687 0.1988 -0.0015 0.0052  -0.0021 162 SER   B CA  
3230 C C   . SER   B 181 ? 0.1533 0.1714 0.2064 -0.0021 0.0058  -0.0015 162 SER   B C   
3231 O O   . SER   B 181 ? 0.1571 0.1728 0.2126 -0.0013 0.0035  -0.0009 162 SER   B O   
3232 C CB  . SER   B 181 ? 0.176  0.1962 0.2245 0.0001  0.0041  -0.0037 162 SER   B CB  
3233 O OG  . SER   B 181 ? 0.18   0.2011 0.2271 -0.0009 0.006   -0.0045 162 SER   B OG  
3234 N N   . THR   B 182 ? 0.1537 0.1725 0.2072 -0.0033 0.0088  -0.0018 163 THR   B N   
3235 C CA  . THR   B 182 ? 0.1417 0.1595 0.1995 -0.0032 0.0097  -0.0013 163 THR   B CA  
3236 C C   . THR   B 182 ? 0.1385 0.1546 0.1954 -0.0029 0.0103  -0.0025 163 THR   B C   
3237 O O   . THR   B 182 ? 0.1498 0.1659 0.2031 -0.0038 0.0121  -0.0038 163 THR   B O   
3238 C CB  . THR   B 182 ? 0.1634 0.1829 0.2229 -0.0043 0.013   -0.0007 163 THR   B CB  
3239 O OG1 . THR   B 182 ? 0.1787 0.1985 0.2332 -0.0053 0.0156  -0.0022 163 THR   B OG1 
3240 C CG2 . THR   B 182 ? 0.1709 0.1913 0.2311 -0.0053 0.0121  0.0014  163 THR   B CG2 
3241 N N   . LEU   B 183 ? 0.1403 0.1545 0.2    -0.0019 0.008   -0.002  164 LEU   B N   
3242 C CA  . LEU   B 183 ? 0.1538 0.1654 0.2132 -0.0016 0.008   -0.0024 164 LEU   B CA  
3243 C C   . LEU   B 183 ? 0.1501 0.1607 0.203  -0.0025 0.0083  -0.0034 164 LEU   B C   
3244 O O   . LEU   B 183 ? 0.1709 0.1791 0.2223 -0.0031 0.0091  -0.0038 164 LEU   B O   
3245 C CB  . LEU   B 183 ? 0.155  0.1665 0.2181 -0.0012 0.0109  -0.0028 164 LEU   B CB  
3246 C CG  . LEU   B 183 ? 0.1674 0.181  0.239  -0.0002 0.0107  -0.0015 164 LEU   B CG  
3247 C CD1 . LEU   B 183 ? 0.1961 0.2113 0.2709 0.0004  0.0152  -0.0024 164 LEU   B CD1 
3248 C CD2 . LEU   B 183 ? 0.1609 0.1721 0.2363 0.0011  0.0069  -0.0004 164 LEU   B CD2 
3249 N N   . CYS   B 184 ? 0.1454 0.1578 0.195  -0.0026 0.0074  -0.0038 165 CYS   B N   
3250 C CA  . CYS   B 184 ? 0.1517 0.1651 0.1965 -0.0036 0.0081  -0.0045 165 CYS   B CA  
3251 C C   . CYS   B 184 ? 0.1573 0.1694 0.1991 -0.003  0.0063  -0.0044 165 CYS   B C   
3252 O O   . CYS   B 184 ? 0.1579 0.1688 0.196  -0.0043 0.0068  -0.0043 165 CYS   B O   
3253 C CB  . CYS   B 184 ? 0.1593 0.1771 0.2034 -0.0041 0.0092  -0.0051 165 CYS   B CB  
3254 S SG  . CYS   B 184 ? 0.1721 0.1939 0.2127 -0.0052 0.0099  -0.0059 165 CYS   B SG  
3255 N N   . LEU   B 185 ? 0.1502 0.1623 0.1923 -0.0013 0.0043  -0.0047 166 LEU   B N   
3256 C CA  . LEU   B 185 ? 0.1631 0.1742 0.2004 -0.0005 0.0033  -0.0054 166 LEU   B CA  
3257 C C   . LEU   B 185 ? 0.1663 0.1727 0.2005 -0.0011 0.0015  -0.0045 166 LEU   B C   
3258 O O   . LEU   B 185 ? 0.1883 0.1944 0.2168 -0.0017 0.0022  -0.0048 166 LEU   B O   
3259 C CB  . LEU   B 185 ? 0.1659 0.1766 0.2035 0.0017  0.0013  -0.0064 166 LEU   B CB  
3260 C CG  . LEU   B 185 ? 0.1853 0.2001 0.2252 0.0026  0.0025  -0.007  166 LEU   B CG  
3261 C CD1 . LEU   B 185 ? 0.2105 0.2225 0.2502 0.0051  -0.0003 -0.0079 166 LEU   B CD1 
3262 C CD2 . LEU   B 185 ? 0.1924 0.2126 0.2306 0.0024  0.0052  -0.008  166 LEU   B CD2 
3263 N N   . ASP   B 186 ? 0.1735 0.1766 0.2114 -0.001  -0.0007 -0.0032 167 ASP   B N   
3264 C CA  . ASP   B 186 ? 0.2071 0.2055 0.2421 -0.0015 -0.0032 -0.0019 167 ASP   B CA  
3265 C C   . ASP   B 186 ? 0.2013 0.1988 0.2329 -0.0034 -0.0011 -0.0012 167 ASP   B C   
3266 O O   . ASP   B 186 ? 0.2253 0.2194 0.251  -0.0045 -0.0023 -0.0002 167 ASP   B O   
3267 C CB  . ASP   B 186 ? 0.2334 0.2299 0.2756 -0.0009 -0.0057 -0.0004 167 ASP   B CB  
3268 C CG  . ASP   B 186 ? 0.3369 0.333  0.3835 0       -0.0091 -0.0001 167 ASP   B CG  
3269 O OD1 . ASP   B 186 ? 0.3598 0.3549 0.4024 0.0004  -0.0106 -0.0011 167 ASP   B OD1 
3270 O OD2 . ASP   B 186 ? 0.3318 0.3285 0.3863 0.0004  -0.0103 0.0013  167 ASP   B OD2 
3271 N N   . ALA   B 187 ? 0.1693 0.1692 0.2041 -0.0042 0.0018  -0.0015 168 ALA   B N   
3272 C CA  . ALA   B 187 ? 0.1734 0.1715 0.2053 -0.0065 0.0034  -0.0009 168 ALA   B CA  
3273 C C   . ALA   B 187 ? 0.1954 0.1968 0.2216 -0.0084 0.0055  -0.0013 168 ALA   B C   
3274 O O   . ALA   B 187 ? 0.2385 0.2377 0.2601 -0.0109 0.006   -0.0001 168 ALA   B O   
3275 C CB  . ALA   B 187 ? 0.1736 0.1729 0.2098 -0.0067 0.0056  -0.0018 168 ALA   B CB  
3276 N N   . ALA   B 188 ? 0.164  0.171  0.1911 -0.0074 0.0069  -0.0029 169 ALA   B N   
3277 C CA  . ALA   B 188 ? 0.1793 0.1917 0.2035 -0.0088 0.0095  -0.0035 169 ALA   B CA  
3278 C C   . ALA   B 188 ? 0.2035 0.2157 0.2218 -0.0084 0.0096  -0.0036 169 ALA   B C   
3279 O O   . ALA   B 188 ? 0.1979 0.2152 0.214  -0.0098 0.0125  -0.0039 169 ALA   B O   
3280 C CB  . ALA   B 188 ? 0.1796 0.1981 0.2081 -0.0073 0.0106  -0.005  169 ALA   B CB  
3281 N N   . CYS   B 189 ? 0.2036 0.2111 0.2196 -0.0064 0.0068  -0.0037 170 CYS   B N   
3282 C CA  . CYS   B 189 ? 0.2164 0.2236 0.2256 -0.0055 0.007   -0.0047 170 CYS   B CA  
3283 C C   . CYS   B 189 ? 0.2478 0.2482 0.2499 -0.007  0.0047  -0.0029 170 CYS   B C   
3284 O O   . CYS   B 189 ? 0.2486 0.2434 0.252  -0.0064 0.0007  -0.0018 170 CYS   B O   
3285 C CB  . CYS   B 189 ? 0.2234 0.2301 0.2343 -0.0019 0.0051  -0.0069 170 CYS   B CB  
3286 S SG  . CYS   B 189 ? 0.2172 0.2309 0.2357 0.0001  0.0069  -0.0086 170 CYS   B SG  
3287 N N   . PRO   B 190 ? 0.2748 0.2757 0.2692 -0.0091 0.007   -0.0023 171 PRO   B N   
3288 C CA  . PRO   B 190 ? 0.301  0.2943 0.2872 -0.0112 0.0044  0.0003  171 PRO   B CA  
3289 C C   . PRO   B 190 ? 0.3198 0.3077 0.299  -0.0093 0.0009  -0.0007 171 PRO   B C   
3290 O O   . PRO   B 190 ? 0.3593 0.34   0.333  -0.0106 -0.003  0.0016  171 PRO   B O   
3291 C CB  . PRO   B 190 ? 0.3288 0.3251 0.3089 -0.0148 0.0086  0.0017  171 PRO   B CB  
3292 C CG  . PRO   B 190 ? 0.3422 0.3473 0.3306 -0.0153 0.0126  0.0005  171 PRO   B CG  
3293 C CD  . PRO   B 190 ? 0.2935 0.3022 0.2875 -0.0107 0.0122  -0.0028 171 PRO   B CD  
3294 N N   . ASP   B 191 ? 0.2987 0.2892 0.2777 -0.0063 0.0018  -0.0041 172 ASP   B N   
3295 C CA  . ASP   B 191 ? 0.3136 0.2982 0.285  -0.0047 -0.0016 -0.0057 172 ASP   B CA  
3296 C C   . ASP   B 191 ? 0.2836 0.2699 0.2596 -0.0009 -0.0021 -0.0092 172 ASP   B C   
3297 O O   . ASP   B 191 ? 0.2648 0.2574 0.249  0.0004  0.0007  -0.0102 172 ASP   B O   
3298 C CB  . ASP   B 191 ? 0.3479 0.3312 0.3059 -0.0061 0.0012  -0.0062 172 ASP   B CB  
3299 C CG  . ASP   B 191 ? 0.427  0.4195 0.3856 -0.0057 0.0084  -0.0081 172 ASP   B CG  
3300 O OD1 . ASP   B 191 ? 0.3891 0.387  0.3553 -0.0025 0.0101  -0.0109 172 ASP   B OD1 
3301 O OD2 . ASP   B 191 ? 0.502  0.4967 0.4542 -0.0087 0.0122  -0.0065 172 ASP   B OD2 
3302 N N   . LEU   B 192 ? 0.3013 0.281  0.272  0.0006  -0.0063 -0.0108 173 LEU   B N   
3303 C CA  . LEU   B 192 ? 0.2902 0.2693 0.2647 0.0038  -0.0078 -0.0139 173 LEU   B CA  
3304 C C   . LEU   B 192 ? 0.296  0.2804 0.2694 0.0068  -0.0026 -0.0176 173 LEU   B C   
3305 O O   . LEU   B 192 ? 0.2744 0.2623 0.2563 0.009   -0.0021 -0.0187 173 LEU   B O   
3306 C CB  . LEU   B 192 ? 0.3049 0.2746 0.2729 0.0041  -0.0142 -0.0148 173 LEU   B CB  
3307 C CG  . LEU   B 192 ? 0.3455 0.3124 0.3173 0.0065  -0.0172 -0.0172 173 LEU   B CG  
3308 C CD1 . LEU   B 192 ? 0.3271 0.2984 0.3132 0.0063  -0.0179 -0.0151 173 LEU   B CD1 
3309 C CD2 . LEU   B 192 ? 0.386  0.3429 0.3504 0.0056  -0.0244 -0.0177 173 LEU   B CD2 
3310 N N   . PRO   B 193 ? 0.3094 0.2956 0.2736 0.0069  0.0018  -0.0192 174 PRO   B N   
3311 C CA  . PRO   B 193 ? 0.2957 0.2891 0.2618 0.0102  0.0073  -0.0227 174 PRO   B CA  
3312 C C   . PRO   B 193 ? 0.2737 0.277  0.2518 0.0097  0.0106  -0.021  174 PRO   B C   
3313 O O   . PRO   B 193 ? 0.2588 0.2664 0.2434 0.0131  0.0119  -0.0232 174 PRO   B O   
3314 C CB  . PRO   B 193 ? 0.323  0.3172 0.277  0.0095  0.0119  -0.024  174 PRO   B CB  
3315 C CG  . PRO   B 193 ? 0.3537 0.337  0.2965 0.007   0.0067  -0.0226 174 PRO   B CG  
3316 C CD  . PRO   B 193 ? 0.3433 0.3254 0.2951 0.0042  0.0021  -0.0181 174 PRO   B CD  
3317 N N   . THR   B 194 ? 0.2568 0.2627 0.2378 0.0057  0.0112  -0.0172 175 THR   B N   
3318 C CA  . THR   B 194 ? 0.2482 0.2624 0.2396 0.0048  0.0137  -0.0158 175 THR   B CA  
3319 C C   . THR   B 194 ? 0.2084 0.221  0.2084 0.0064  0.0099  -0.0156 175 THR   B C   
3320 O O   . THR   B 194 ? 0.2047 0.2234 0.2122 0.0077  0.0114  -0.0161 175 THR   B O   
3321 C CB  . THR   B 194 ? 0.2843 0.2997 0.2759 -0.0001 0.0147  -0.0121 175 THR   B CB  
3322 O OG1 . THR   B 194 ? 0.3483 0.3653 0.3315 -0.0021 0.0184  -0.0118 175 THR   B OG1 
3323 C CG2 . THR   B 194 ? 0.2877 0.3109 0.2892 -0.0013 0.0167  -0.011  175 THR   B CG2 
3324 N N   . TYR   B 195 ? 0.2025 0.2072 0.2016 0.006   0.005   -0.0146 176 TYR   B N   
3325 C CA  . TYR   B 195 ? 0.1882 0.1916 0.1953 0.0069  0.0019  -0.0141 176 TYR   B CA  
3326 C C   . TYR   B 195 ? 0.2032 0.2067 0.2117 0.0108  0.0015  -0.017  176 TYR   B C   
3327 O O   . TYR   B 195 ? 0.19   0.1972 0.2056 0.0118  0.0017  -0.0167 176 TYR   B O   
3328 C CB  . TYR   B 195 ? 0.2024 0.1981 0.2081 0.0057  -0.0032 -0.0125 176 TYR   B CB  
3329 C CG  . TYR   B 195 ? 0.1941 0.1891 0.2083 0.0058  -0.0059 -0.0113 176 TYR   B CG  
3330 C CD1 . TYR   B 195 ? 0.2133 0.2112 0.2341 0.004   -0.0051 -0.0089 176 TYR   B CD1 
3331 C CD2 . TYR   B 195 ? 0.224  0.215  0.2392 0.0075  -0.0094 -0.0125 176 TYR   B CD2 
3332 C CE1 . TYR   B 195 ? 0.2078 0.2058 0.2361 0.0039  -0.0068 -0.0077 176 TYR   B CE1 
3333 C CE2 . TYR   B 195 ? 0.2159 0.2067 0.239  0.007   -0.0116 -0.0108 176 TYR   B CE2 
3334 C CZ  . TYR   B 195 ? 0.2104 0.2051 0.2399 0.0051  -0.01   -0.0084 176 TYR   B CZ  
3335 O OH  . TYR   B 195 ? 0.2349 0.23   0.2718 0.0044  -0.0114 -0.0067 176 TYR   B OH  
3336 N N   . CYS   B 196 ? 0.2103 0.2095 0.2111 0.0132  0.0009  -0.02   177 CYS   B N   
3337 C CA  . CYS   B 196 ? 0.2183 0.2166 0.2201 0.0174  0.0005  -0.0231 177 CYS   B CA  
3338 C C   . CYS   B 196 ? 0.2104 0.2186 0.2176 0.0195  0.0054  -0.0241 177 CYS   B C   
3339 O O   . CYS   B 196 ? 0.2134 0.2232 0.227  0.0219  0.0044  -0.0245 177 CYS   B O   
3340 C CB  . CYS   B 196 ? 0.2419 0.233  0.2333 0.0196  -0.0006 -0.0267 177 CYS   B CB  
3341 S SG  . CYS   B 196 ? 0.2894 0.2766 0.2816 0.0254  -0.0019 -0.031  177 CYS   B SG  
3342 N N   . ARG   B 197 ? 0.2138 0.2288 0.219  0.0181  0.0102  -0.0239 178 ARG   B N   
3343 C CA  . ARG   B 197 ? 0.2135 0.2391 0.2252 0.0196  0.0144  -0.0245 178 ARG   B CA  
3344 C C   . ARG   B 197 ? 0.1936 0.2232 0.2146 0.0178  0.0129  -0.0216 178 ARG   B C   
3345 O O   . ARG   B 197 ? 0.1985 0.2332 0.2262 0.0203  0.0131  -0.0222 178 ARG   B O   
3346 C CB  . ARG   B 197 ? 0.2817 0.3143 0.2902 0.0171  0.0196  -0.024  178 ARG   B CB  
3347 C CG  . ARG   B 197 ? 0.3713 0.4021 0.3704 0.0194  0.0225  -0.0273 178 ARG   B CG  
3348 C CD  . ARG   B 197 ? 0.4372 0.4782 0.4358 0.0175  0.029   -0.0269 178 ARG   B CD  
3349 N NE  . ARG   B 197 ? 0.4525 0.4944 0.4502 0.0112  0.0292  -0.0226 178 ARG   B NE  
3350 C CZ  . ARG   B 197 ? 0.4814 0.5166 0.4691 0.0078  0.0286  -0.0209 178 ARG   B CZ  
3351 N NH1 . ARG   B 197 ? 0.4793 0.5149 0.4671 0.0024  0.0286  -0.0169 178 ARG   B NH1 
3352 N NH2 . ARG   B 197 ? 0.4996 0.5269 0.4766 0.0096  0.0275  -0.0232 178 ARG   B NH2 
3353 N N   . ALA   B 198 ? 0.1746 0.2015 0.1957 0.0136  0.0113  -0.0186 179 ALA   B N   
3354 C CA  . ALA   B 198 ? 0.175  0.2048 0.2031 0.0117  0.0104  -0.0162 179 ALA   B CA  
3355 C C   . ALA   B 198 ? 0.1738 0.2003 0.2059 0.0144  0.0069  -0.0165 179 ALA   B C   
3356 O O   . ALA   B 198 ? 0.1743 0.2052 0.2119 0.0147  0.0068  -0.0157 179 ALA   B O   
3357 C CB  . ALA   B 198 ? 0.179  0.2051 0.206  0.0076  0.0094  -0.0136 179 ALA   B CB  
3358 N N   . LEU   B 199 ? 0.1759 0.1941 0.2046 0.0158  0.0037  -0.0174 180 LEU   B N   
3359 C CA  . LEU   B 199 ? 0.1794 0.1935 0.2114 0.0179  0.0002  -0.0173 180 LEU   B CA  
3360 C C   . LEU   B 199 ? 0.1795 0.197  0.2138 0.0224  0.0008  -0.0195 180 LEU   B C   
3361 O O   . LEU   B 199 ? 0.1844 0.2028 0.2237 0.0233  -0.0009 -0.0183 180 LEU   B O   
3362 C CB  . LEU   B 199 ? 0.1876 0.1921 0.2152 0.0182  -0.0036 -0.0181 180 LEU   B CB  
3363 C CG  . LEU   B 199 ? 0.1939 0.1954 0.2219 0.0143  -0.0053 -0.0154 180 LEU   B CG  
3364 C CD1 . LEU   B 199 ? 0.2424 0.2354 0.2662 0.0143  -0.0094 -0.0162 180 LEU   B CD1 
3365 C CD2 . LEU   B 199 ? 0.2128 0.216  0.2476 0.0123  -0.0062 -0.0125 180 LEU   B CD2 
3366 N N   . ARG   B 200 ? 0.1829 0.2028 0.2139 0.0251  0.0036  -0.0226 181 ARG   B N   
3367 C CA  . ARG   B 200 ? 0.1887 0.2134 0.2236 0.03    0.0049  -0.025  181 ARG   B CA  
3368 C C   . ARG   B 200 ? 0.1923 0.2276 0.2349 0.0288  0.0066  -0.0228 181 ARG   B C   
3369 O O   . ARG   B 200 ? 0.1953 0.2333 0.2438 0.0317  0.005   -0.0226 181 ARG   B O   
3370 C CB  . ARG   B 200 ? 0.2071 0.2338 0.2371 0.0332  0.0087  -0.0289 181 ARG   B CB  
3371 C CG  . ARG   B 200 ? 0.2299 0.2456 0.2508 0.0346  0.0067  -0.0316 181 ARG   B CG  
3372 C CD  . ARG   B 200 ? 0.2547 0.2728 0.2707 0.0388  0.0111  -0.0362 181 ARG   B CD  
3373 N NE  . ARG   B 200 ? 0.3362 0.3449 0.3404 0.0386  0.0103  -0.0386 181 ARG   B NE  
3374 C CZ  . ARG   B 200 ? 0.4208 0.4193 0.4192 0.0424  0.0075  -0.0424 181 ARG   B CZ  
3375 N NH1 . ARG   B 200 ? 0.4346 0.4305 0.4383 0.047   0.0051  -0.044  181 ARG   B NH1 
3376 N NH2 . ARG   B 200 ? 0.4353 0.4255 0.422  0.0416  0.0066  -0.0446 181 ARG   B NH2 
3377 N N   . ASN   B 201 ? 0.1796 0.2204 0.2219 0.0243  0.0095  -0.0211 182 ASN   B N   
3378 C CA  . ASN   B 201 ? 0.1776 0.2281 0.2267 0.0225  0.0108  -0.0192 182 ASN   B CA  
3379 C C   . ASN   B 201 ? 0.1849 0.2331 0.2373 0.021   0.007   -0.0165 182 ASN   B C   
3380 O O   . ASN   B 201 ? 0.1951 0.2489 0.2532 0.022   0.006   -0.0157 182 ASN   B O   
3381 C CB  . ASN   B 201 ? 0.1858 0.2405 0.2328 0.0175  0.0141  -0.0178 182 ASN   B CB  
3382 C CG  . ASN   B 201 ? 0.1855 0.2437 0.2288 0.0183  0.0183  -0.0199 182 ASN   B CG  
3383 O OD1 . ASN   B 201 ? 0.2161 0.2776 0.2606 0.0231  0.02    -0.0228 182 ASN   B OD1 
3384 N ND2 . ASN   B 201 ? 0.1794 0.237  0.218  0.0138  0.0203  -0.0185 182 ASN   B ND2 
3385 N N   . LEU   B 202 ? 0.1639 0.2038 0.2127 0.0187  0.0048  -0.0151 183 LEU   B N   
3386 C CA  . LEU   B 202 ? 0.1784 0.2157 0.2294 0.0173  0.0018  -0.0126 183 LEU   B CA  
3387 C C   . LEU   B 202 ? 0.1891 0.2237 0.2425 0.0215  -0.0014 -0.013  183 LEU   B C   
3388 O O   . LEU   B 202 ? 0.1847 0.221  0.2411 0.0213  -0.0035 -0.011  183 LEU   B O   
3389 C CB  . LEU   B 202 ? 0.1876 0.2175 0.2355 0.0144  0.0007  -0.0111 183 LEU   B CB  
3390 C CG  . LEU   B 202 ? 0.2121 0.2436 0.2592 0.0099  0.0027  -0.0096 183 LEU   B CG  
3391 C CD1 . LEU   B 202 ? 0.2484 0.2847 0.2942 0.0085  0.0058  -0.0105 183 LEU   B CD1 
3392 C CD2 . LEU   B 202 ? 0.2125 0.2374 0.258  0.0082  0.0016  -0.0085 183 LEU   B CD2 
3393 N N   . GLY   B 203 ? 0.1915 0.2213 0.2428 0.0253  -0.0021 -0.0155 184 GLY   B N   
3394 C CA  . GLY   B 203 ? 0.1891 0.2147 0.2423 0.0299  -0.0055 -0.0163 184 GLY   B CA  
3395 C C   . GLY   B 203 ? 0.1988 0.2326 0.2581 0.0333  -0.0053 -0.0167 184 GLY   B C   
3396 O O   . GLY   B 203 ? 0.2042 0.2354 0.2664 0.0358  -0.0091 -0.0155 184 GLY   B O   
3397 N N   . SER   B 204 ? 0.1881 0.2322 0.25   0.033   -0.0012 -0.0178 185 SER   B N   
3398 C CA  . SER   B 204 ? 0.2004 0.2541 0.27   0.0361  -0.0011 -0.018  185 SER   B CA  
3399 C C   . SER   B 204 ? 0.1844 0.2401 0.2573 0.0332  -0.0046 -0.014  185 SER   B C   
3400 O O   . SER   B 204 ? 0.2068 0.2687 0.2863 0.0359  -0.0065 -0.0134 185 SER   B O   
3401 C CB  . SER   B 204 ? 0.2073 0.2724 0.2796 0.0352  0.0041  -0.0194 185 SER   B CB  
3402 O OG  . SER   B 204 ? 0.2119 0.2813 0.2837 0.0288  0.0053  -0.0168 185 SER   B OG  
3403 N N   . LEU   B 205 ? 0.1761 0.2273 0.2444 0.0277  -0.0053 -0.0115 186 LEU   B N   
3404 C CA  . LEU   B 205 ? 0.1727 0.2247 0.2418 0.0246  -0.0082 -0.008  186 LEU   B CA  
3405 C C   . LEU   B 205 ? 0.1819 0.2248 0.2489 0.0255  -0.0126 -0.0058 186 LEU   B C   
3406 O O   . LEU   B 205 ? 0.2013 0.2439 0.2674 0.0228  -0.0151 -0.0027 186 LEU   B O   
3407 C CB  . LEU   B 205 ? 0.19   0.2414 0.2546 0.0184  -0.0058 -0.0068 186 LEU   B CB  
3408 C CG  . LEU   B 205 ? 0.2007 0.2594 0.2662 0.0163  -0.0017 -0.0082 186 LEU   B CG  
3409 C CD1 . LEU   B 205 ? 0.2189 0.2744 0.2795 0.0108  0       -0.0072 186 LEU   B CD1 
3410 C CD2 . LEU   B 205 ? 0.2364 0.3059 0.3083 0.0163  -0.0021 -0.0079 186 LEU   B CD2 
3411 N N   . LEU   B 206 ? 0.1789 0.2138 0.2441 0.0286  -0.0137 -0.0073 187 LEU   B N   
3412 C CA  . LEU   B 206 ? 0.1927 0.2175 0.255  0.0282  -0.0177 -0.0049 187 LEU   B CA  
3413 C C   . LEU   B 206 ? 0.2139 0.2347 0.2791 0.0342  -0.0217 -0.0056 187 LEU   B C   
3414 O O   . LEU   B 206 ? 0.2285 0.2507 0.2961 0.0393  -0.0205 -0.0094 187 LEU   B O   
3415 C CB  . LEU   B 206 ? 0.2362 0.2535 0.2942 0.0269  -0.0164 -0.0063 187 LEU   B CB  
3416 C CG  . LEU   B 206 ? 0.2979 0.3099 0.3525 0.022   -0.0167 -0.0036 187 LEU   B CG  
3417 C CD1 . LEU   B 206 ? 0.247  0.2517 0.2991 0.0222  -0.0171 -0.0053 187 LEU   B CD1 
3418 C CD2 . LEU   B 206 ? 0.2538 0.2625 0.3077 0.0195  -0.0198 0.0007  187 LEU   B CD2 
3419 N N   . LYS   B 207 ? 0.2124 0.2274 0.2769 0.0336  -0.0263 -0.002  188 LYS   B N   
3420 C CA  . LYS   B 207 ? 0.2214 0.2299 0.2881 0.0391  -0.031  -0.0022 188 LYS   B CA  
3421 C C   . LYS   B 207 ? 0.2394 0.2377 0.3029 0.0413  -0.0315 -0.005  188 LYS   B C   
3422 O O   . LYS   B 207 ? 0.2324 0.2265 0.2916 0.0372  -0.03   -0.0048 188 LYS   B O   
3423 C CB  . LYS   B 207 ? 0.26   0.263  0.325  0.0369  -0.0363 0.0032  188 LYS   B CB  
3424 C CG  . LYS   B 207 ? 0.347  0.341  0.4059 0.0313  -0.0371 0.0064  188 LYS   B CG  
3425 C CD  . LYS   B 207 ? 0.3979 0.3871 0.4541 0.0285  -0.0417 0.0121  188 LYS   B CD  
3426 C CE  . LYS   B 207 ? 0.4517 0.4327 0.5026 0.0229  -0.0416 0.0152  188 LYS   B CE  
3427 N NZ  . LYS   B 207 ? 0.4959 0.4719 0.5429 0.0195  -0.0455 0.0211  188 LYS   B NZ  
3428 N N   . PRO   B 208 ? 0.2583 0.2513 0.324  0.0479  -0.0345 -0.0073 189 PRO   B N   
3429 C CA  . PRO   B 208 ? 0.2648 0.2454 0.3262 0.0497  -0.0364 -0.0097 189 PRO   B CA  
3430 C C   . PRO   B 208 ? 0.2652 0.2356 0.3225 0.044   -0.0404 -0.0049 189 PRO   B C   
3431 O O   . PRO   B 208 ? 0.2612 0.2306 0.3192 0.042   -0.0436 0       189 PRO   B O   
3432 C CB  . PRO   B 208 ? 0.2983 0.2745 0.3633 0.058   -0.0398 -0.0123 189 PRO   B CB  
3433 C CG  . PRO   B 208 ? 0.2959 0.2852 0.368  0.0611  -0.0379 -0.0126 189 PRO   B CG  
3434 C CD  . PRO   B 208 ? 0.2755 0.2732 0.3478 0.0541  -0.0367 -0.0079 189 PRO   B CD  
3435 N N   . GLY   B 209 ? 0.2616 0.2258 0.3146 0.0407  -0.0397 -0.0057 190 GLY   B N   
3436 C CA  . GLY   B 209 ? 0.2796 0.2361 0.3299 0.0347  -0.0426 -0.0011 190 GLY   B CA  
3437 C C   . GLY   B 209 ? 0.2747 0.239  0.3249 0.028   -0.0393 0.0029  190 GLY   B C   
3438 O O   . GLY   B 209 ? 0.3025 0.2624 0.3512 0.0228  -0.0407 0.0069  190 GLY   B O   
3439 N N   . GLY   B 210 ? 0.2362 0.212  0.2883 0.0281  -0.0349 0.0017  191 GLY   B N   
3440 C CA  . GLY   B 210 ? 0.2223 0.2052 0.2738 0.0224  -0.0315 0.0045  191 GLY   B CA  
3441 C C   . GLY   B 210 ? 0.2208 0.2032 0.271  0.0187  -0.0286 0.0037  191 GLY   B C   
3442 O O   . GLY   B 210 ? 0.2281 0.207  0.2776 0.0207  -0.0288 0.0004  191 GLY   B O   
3443 N N   . PHE   B 211 ? 0.2057 0.192  0.2554 0.0136  -0.026  0.0065  192 PHE   B N   
3444 C CA  . PHE   B 211 ? 0.2063 0.1926 0.2562 0.0101  -0.0237 0.0065  192 PHE   B CA  
3445 C C   . PHE   B 211 ? 0.1856 0.1797 0.236  0.0098  -0.0191 0.0039  192 PHE   B C   
3446 O O   . PHE   B 211 ? 0.2014 0.202  0.2516 0.0094  -0.0166 0.0041  192 PHE   B O   
3447 C CB  . PHE   B 211 ? 0.2445 0.2303 0.2942 0.0047  -0.0231 0.0111  192 PHE   B CB  
3448 C CG  . PHE   B 211 ? 0.3006 0.2774 0.3499 0.0032  -0.0276 0.0143  192 PHE   B CG  
3449 C CD1 . PHE   B 211 ? 0.3383 0.3098 0.3893 0.0014  -0.0295 0.0144  192 PHE   B CD1 
3450 C CD2 . PHE   B 211 ? 0.3227 0.2963 0.3699 0.0031  -0.0304 0.0176  192 PHE   B CD2 
3451 C CE1 . PHE   B 211 ? 0.3525 0.3154 0.4032 -0.0009 -0.0338 0.0178  192 PHE   B CE1 
3452 C CE2 . PHE   B 211 ? 0.3507 0.3153 0.3971 0.001   -0.0347 0.0212  192 PHE   B CE2 
3453 C CZ  . PHE   B 211 ? 0.3587 0.318  0.407  -0.001  -0.0363 0.0212  192 PHE   B CZ  
3454 N N   . LEU   B 212 ? 0.1759 0.1686 0.2264 0.0097  -0.0184 0.0019  193 LEU   B N   
3455 C CA  . LEU   B 212 ? 0.169  0.1674 0.2195 0.009   -0.0145 0       193 LEU   B CA  
3456 C C   . LEU   B 212 ? 0.1694 0.1673 0.222  0.005   -0.0137 0.002   193 LEU   B C   
3457 O O   . LEU   B 212 ? 0.1825 0.175  0.2361 0.0041  -0.0165 0.0027  193 LEU   B O   
3458 C CB  . LEU   B 212 ? 0.1786 0.1752 0.2272 0.0121  -0.015  -0.0037 193 LEU   B CB  
3459 C CG  . LEU   B 212 ? 0.2011 0.2023 0.2488 0.0111  -0.0115 -0.0052 193 LEU   B CG  
3460 C CD1 . LEU   B 212 ? 0.249  0.2576 0.2969 0.0119  -0.0084 -0.006  193 LEU   B CD1 
3461 C CD2 . LEU   B 212 ? 0.2269 0.2242 0.2713 0.0132  -0.0127 -0.0083 193 LEU   B CD2 
3462 N N   . VAL   B 213 ? 0.1585 0.1619 0.2119 0.0027  -0.0099 0.003   194 VAL   B N   
3463 C CA  . VAL   B 213 ? 0.1547 0.159  0.2111 -0.0004 -0.0082 0.0047  194 VAL   B CA  
3464 C C   . VAL   B 213 ? 0.1532 0.161  0.21   -0.0002 -0.0055 0.0027  194 VAL   B C   
3465 O O   . VAL   B 213 ? 0.1584 0.1699 0.2131 0       -0.0027 0.0017  194 VAL   B O   
3466 C CB  . VAL   B 213 ? 0.1648 0.1715 0.2217 -0.0033 -0.006  0.0076  194 VAL   B CB  
3467 C CG1 . VAL   B 213 ? 0.172  0.1809 0.2332 -0.0059 -0.0034 0.009   194 VAL   B CG1 
3468 C CG2 . VAL   B 213 ? 0.1884 0.1906 0.2443 -0.004  -0.0093 0.0103  194 VAL   B CG2 
3469 N N   . ILE   B 214 ? 0.1473 0.1532 0.2062 -0.0002 -0.0068 0.0022  195 ILE   B N   
3470 C CA  . ILE   B 214 ? 0.1464 0.1542 0.2051 0       -0.005  0.0008  195 ILE   B CA  
3471 C C   . ILE   B 214 ? 0.151  0.1597 0.2154 -0.0017 -0.0046 0.0025  195 ILE   B C   
3472 O O   . ILE   B 214 ? 0.1555 0.162  0.2235 -0.0027 -0.0076 0.0039  195 ILE   B O   
3473 C CB  . ILE   B 214 ? 0.1647 0.1693 0.2196 0.002   -0.0073 -0.0014 195 ILE   B CB  
3474 C CG1 . ILE   B 214 ? 0.2038 0.2083 0.2544 0.0045  -0.0075 -0.0034 195 ILE   B CG1 
3475 C CG2 . ILE   B 214 ? 0.1921 0.1981 0.2461 0.0018  -0.0057 -0.0022 195 ILE   B CG2 
3476 C CD1 . ILE   B 214 ? 0.2483 0.2582 0.2973 0.0049  -0.0041 -0.0042 195 ILE   B CD1 
3477 N N   . MET   B 215 ? 0.147  0.1588 0.2128 -0.0021 -0.0014 0.0022  196 MET   B N   
3478 C CA  . MET   B 215 ? 0.1434 0.1566 0.2158 -0.0028 -0.0009 0.0034  196 MET   B CA  
3479 C C   . MET   B 215 ? 0.1504 0.1631 0.2212 -0.0017 -0.0003 0.002   196 MET   B C   
3480 O O   . MET   B 215 ? 0.1655 0.1788 0.2316 -0.0014 0.0023  0.0006  196 MET   B O   
3481 C CB  . MET   B 215 ? 0.1832 0.2005 0.2596 -0.0042 0.0032  0.0047  196 MET   B CB  
3482 C CG  . MET   B 215 ? 0.2187 0.2361 0.2954 -0.006  0.0027  0.0068  196 MET   B CG  
3483 S SD  . MET   B 215 ? 0.2638 0.2862 0.3441 -0.0081 0.0082  0.0086  196 MET   B SD  
3484 C CE  . MET   B 215 ? 0.2907 0.311  0.3693 -0.0106 0.0059  0.0116  196 MET   B CE  
3485 N N   . ASP   B 216 ? 0.1435 0.1546 0.2175 -0.0013 -0.0032 0.0025  197 ASP   B N   
3486 C CA  . ASP   B 216 ? 0.1443 0.1537 0.2158 -0.0003 -0.0032 0.0016  197 ASP   B CA  
3487 C C   . ASP   B 216 ? 0.1483 0.1566 0.2256 0       -0.0066 0.003   197 ASP   B C   
3488 O O   . ASP   B 216 ? 0.161  0.1706 0.2448 -0.0006 -0.009  0.0045  197 ASP   B O   
3489 C CB  . ASP   B 216 ? 0.1556 0.1618 0.2182 0.0001  -0.0046 0.0001  197 ASP   B CB  
3490 C CG  . ASP   B 216 ? 0.1792 0.185  0.2369 0       -0.0023 -0.0009 197 ASP   B CG  
3491 O OD1 . ASP   B 216 ? 0.1767 0.1821 0.2368 0       -0.0012 -0.0004 197 ASP   B OD1 
3492 O OD2 . ASP   B 216 ? 0.204  0.2097 0.2555 0.0001  -0.0017 -0.0021 197 ASP   B OD2 
3493 N N   . ALA   B 217 ? 0.16   0.1663 0.2358 0.0008  -0.0069 0.0028  198 ALA   B N   
3494 C CA  . ALA   B 217 ? 0.1614 0.1663 0.2426 0.0015  -0.0108 0.0044  198 ALA   B CA  
3495 C C   . ALA   B 217 ? 0.1754 0.1759 0.2518 0.0009  -0.0166 0.0048  198 ALA   B C   
3496 O O   . ALA   B 217 ? 0.1977 0.195  0.2644 0.0006  -0.017  0.0035  198 ALA   B O   
3497 C CB  . ALA   B 217 ? 0.1793 0.1819 0.2589 0.0025  -0.0097 0.0042  198 ALA   B CB  
3498 N N   . LEU   B 218 ? 0.1642 0.1647 0.2476 0.0008  -0.0214 0.0067  199 LEU   B N   
3499 C CA  . LEU   B 218 ? 0.1738 0.169  0.2517 0       -0.0278 0.0071  199 LEU   B CA  
3500 C C   . LEU   B 218 ? 0.1816 0.1734 0.2581 0.0008  -0.0311 0.0084  199 LEU   B C   
3501 O O   . LEU   B 218 ? 0.1793 0.1739 0.2651 0.002   -0.0307 0.0099  199 LEU   B O   
3502 C CB  . LEU   B 218 ? 0.1699 0.1666 0.2562 -0.0013 -0.0326 0.0086  199 LEU   B CB  
3503 C CG  . LEU   B 218 ? 0.186  0.1837 0.2719 -0.0025 -0.0311 0.0077  199 LEU   B CG  
3504 C CD1 . LEU   B 218 ? 0.2    0.201  0.2975 -0.0045 -0.0345 0.01    199 LEU   B CD1 
3505 C CD2 . LEU   B 218 ? 0.2261 0.217  0.2995 -0.0027 -0.0334 0.0055  199 LEU   B CD2 
3506 N N   . LYS   B 219 ? 0.1879 0.1734 0.2528 0.0002  -0.0341 0.008   200 LYS   B N   
3507 C CA  . LYS   B 219 ? 0.2096 0.1901 0.2706 0.0002  -0.0387 0.0098  200 LYS   B CA  
3508 C C   . LYS   B 219 ? 0.2155 0.1963 0.2789 0.0014  -0.0357 0.0108  200 LYS   B C   
3509 O O   . LYS   B 219 ? 0.243  0.2211 0.3093 0.0021  -0.0399 0.0131  200 LYS   B O   
3510 C CB  . LYS   B 219 ? 0.2282 0.2083 0.2968 -0.0002 -0.0462 0.0121  200 LYS   B CB  
3511 C CG  . LYS   B 219 ? 0.2711 0.2484 0.3346 -0.0019 -0.0503 0.0109  200 LYS   B CG  
3512 C CD  . LYS   B 219 ? 0.3672 0.3436 0.4376 -0.003  -0.0587 0.0132  200 LYS   B CD  
3513 C CE  . LYS   B 219 ? 0.4731 0.4447 0.5363 -0.005  -0.0631 0.0116  200 LYS   B CE  
3514 N NZ  . LYS   B 219 ? 0.536  0.5072 0.607  -0.0068 -0.0718 0.0139  200 LYS   B NZ  
3515 N N   . SER   B 220 ? 0.1925 0.1755 0.2541 0.0016  -0.0291 0.0091  201 SER   B N   
3516 C CA  . SER   B 220 ? 0.2001 0.1819 0.2624 0.0024  -0.0262 0.0096  201 SER   B CA  
3517 C C   . SER   B 220 ? 0.1902 0.1666 0.2391 0.0006  -0.0257 0.0097  201 SER   B C   
3518 O O   . SER   B 220 ? 0.1991 0.1766 0.2405 -0.0007 -0.0228 0.0079  201 SER   B O   
3519 C CB  . SER   B 220 ? 0.2628 0.25   0.3305 0.003   -0.0196 0.0077  201 SER   B CB  
3520 O OG  . SER   B 220 ? 0.377  0.362  0.4445 0.0037  -0.0168 0.0075  201 SER   B OG  
3521 N N   . SER   B 221 ? 0.2002 0.171  0.2465 0.0005  -0.0283 0.0119  202 SER   B N   
3522 C CA  . SER   B 221 ? 0.2087 0.1747 0.2425 -0.0018 -0.0271 0.0125  202 SER   B CA  
3523 C C   . SER   B 221 ? 0.2015 0.1663 0.2359 -0.0022 -0.0229 0.0123  202 SER   B C   
3524 O O   . SER   B 221 ? 0.2261 0.1881 0.251  -0.0048 -0.021  0.0128  202 SER   B O   
3525 C CB  . SER   B 221 ? 0.2383 0.197  0.2642 -0.0029 -0.0334 0.0155  202 SER   B CB  
3526 O OG  . SER   B 221 ? 0.272  0.2271 0.3051 -0.0011 -0.0374 0.018   202 SER   B OG  
3527 N N   . TYR   B 222 ? 0.1851 0.1524 0.2299 0.0001  -0.021  0.0114  203 TYR   B N   
3528 C CA  . TYR   B 222 ? 0.201  0.167  0.2459 -0.0003 -0.0167 0.0103  203 TYR   B CA  
3529 C C   . TYR   B 222 ? 0.196  0.1668 0.2516 0.0023  -0.0134 0.0081  203 TYR   B C   
3530 O O   . TYR   B 222 ? 0.1992 0.174  0.2641 0.0047  -0.0149 0.0082  203 TYR   B O   
3531 C CB  . TYR   B 222 ? 0.2146 0.1716 0.2562 -0.0007 -0.0197 0.0129  203 TYR   B CB  
3532 C CG  . TYR   B 222 ? 0.2381 0.193  0.2899 0.0032  -0.0237 0.0142  203 TYR   B CG  
3533 C CD1 . TYR   B 222 ? 0.2496 0.2052 0.3109 0.0063  -0.021  0.0124  203 TYR   B CD1 
3534 C CD2 . TYR   B 222 ? 0.2551 0.2073 0.3072 0.0039  -0.0304 0.0172  203 TYR   B CD2 
3535 C CE1 . TYR   B 222 ? 0.2804 0.2351 0.3526 0.0104  -0.0244 0.0136  203 TYR   B CE1 
3536 C CE2 . TYR   B 222 ? 0.2845 0.2358 0.3478 0.0076  -0.0345 0.0187  203 TYR   B CE2 
3537 C CZ  . TYR   B 222 ? 0.3022 0.2558 0.3765 0.0111  -0.0312 0.0168  203 TYR   B CZ  
3538 O OH  . TYR   B 222 ? 0.3345 0.2879 0.4209 0.0154  -0.035  0.0182  203 TYR   B OH  
3539 N N   . TYR   B 223 ? 0.1933 0.1638 0.2478 0.0017  -0.0089 0.0061  204 TYR   B N   
3540 C CA  . TYR   B 223 ? 0.1886 0.1616 0.2514 0.0043  -0.0054 0.0039  204 TYR   B CA  
3541 C C   . TYR   B 223 ? 0.1905 0.1567 0.2495 0.0037  -0.0037 0.0029  204 TYR   B C   
3542 O O   . TYR   B 223 ? 0.2026 0.1645 0.2525 0.0003  -0.0039 0.0037  204 TYR   B O   
3543 C CB  . TYR   B 223 ? 0.1841 0.165  0.249  0.0039  -0.0012 0.0016  204 TYR   B CB  
3544 C CG  . TYR   B 223 ? 0.176  0.1579 0.2326 0.0008  0.0019  0.0001  204 TYR   B CG  
3545 C CD1 . TYR   B 223 ? 0.1621 0.1448 0.2116 -0.0018 0.0007  0.0011  204 TYR   B CD1 
3546 C CD2 . TYR   B 223 ? 0.178  0.1606 0.2342 0.0004  0.0061  -0.0023 204 TYR   B CD2 
3547 C CE1 . TYR   B 223 ? 0.1679 0.153  0.2118 -0.0044 0.0035  -0.0002 204 TYR   B CE1 
3548 C CE2 . TYR   B 223 ? 0.1912 0.1753 0.2407 -0.0027 0.0082  -0.0034 204 TYR   B CE2 
3549 C CZ  . TYR   B 223 ? 0.1853 0.1714 0.2296 -0.005  0.0069  -0.0022 204 TYR   B CZ  
3550 O OH  . TYR   B 223 ? 0.1932 0.182  0.2328 -0.0078 0.0089  -0.0033 204 TYR   B OH  
3551 N N   . MET   B 224 ? 0.2007 0.166  0.2668 0.007   -0.0016 0.0011  205 MET   B N   
3552 C CA  . MET   B 224 ? 0.2009 0.1579 0.2642 0.0073  -0.0005 -0.0003 205 MET   B CA  
3553 C C   . MET   B 224 ? 0.1962 0.1551 0.259  0.0073  0.0051  -0.0043 205 MET   B C   
3554 O O   . MET   B 224 ? 0.2045 0.1707 0.2732 0.0092  0.0083  -0.006  205 MET   B O   
3555 C CB  . MET   B 224 ? 0.2142 0.1667 0.2862 0.0122  -0.0031 0.0004  205 MET   B CB  
3556 C CG  . MET   B 224 ? 0.2284 0.1775 0.3011 0.0125  -0.0097 0.0047  205 MET   B CG  
3557 S SD  . MET   B 224 ? 0.2426 0.1825 0.3015 0.0075  -0.0137 0.0081  205 MET   B SD  
3558 C CE  . MET   B 224 ? 0.2464 0.1744 0.3035 0.0084  -0.013  0.0067  205 MET   B CE  
3559 N N   . ILE   B 225 ? 0.2048 0.1568 0.26   0.0047  0.0062  -0.0057 206 ILE   B N   
3560 C CA  . ILE   B 225 ? 0.2191 0.1704 0.2729 0.0051  0.0108  -0.0099 206 ILE   B CA  
3561 C C   . ILE   B 225 ? 0.2432 0.1826 0.2959 0.0068  0.0096  -0.011  206 ILE   B C   
3562 O O   . ILE   B 225 ? 0.2463 0.1779 0.2913 0.0031  0.0074  -0.01   206 ILE   B O   
3563 C CB  . ILE   B 225 ? 0.2305 0.1841 0.2757 0       0.0126  -0.011  206 ILE   B CB  
3564 C CG1 . ILE   B 225 ? 0.219  0.183  0.2654 -0.0013 0.0128  -0.0094 206 ILE   B CG1 
3565 C CG2 . ILE   B 225 ? 0.2682 0.2205 0.3112 0.0004  0.0169  -0.0154 206 ILE   B CG2 
3566 C CD1 . ILE   B 225 ? 0.2465 0.2138 0.2856 -0.0061 0.0141  -0.0102 206 ILE   B CD1 
3567 N N   . GLY   B 226 ? 0.253  0.1912 0.3143 0.0125  0.0103  -0.0122 207 GLY   B N   
3568 C CA  . GLY   B 226 ? 0.2682 0.1945 0.33   0.0154  0.0083  -0.013  207 GLY   B CA  
3569 C C   . GLY   B 226 ? 0.269  0.1901 0.3296 0.014   0.0018  -0.0079 207 GLY   B C   
3570 O O   . GLY   B 226 ? 0.2752 0.2024 0.3413 0.0151  -0.0009 -0.0047 207 GLY   B O   
3571 N N   . GLU   B 227 ? 0.2804 0.1894 0.3333 0.0113  -0.0009 -0.0069 208 GLU   B N   
3572 C CA  . GLU   B 227 ? 0.2832 0.1862 0.3329 0.0092  -0.007  -0.0017 208 GLU   B CA  
3573 C C   . GLU   B 227 ? 0.2644 0.1719 0.3052 0.0023  -0.0076 0.0013  208 GLU   B C   
3574 O O   . GLU   B 227 ? 0.2675 0.1712 0.3043 0.0001  -0.012  0.0058  208 GLU   B O   
3575 C CB  . GLU   B 227 ? 0.3142 0.2014 0.359  0.0089  -0.0097 -0.0015 208 GLU   B CB  
3576 C CG  . GLU   B 227 ? 0.3497 0.2311 0.404  0.0167  -0.0102 -0.0039 208 GLU   B CG  
3577 C CD  . GLU   B 227 ? 0.4474 0.3115 0.4968 0.0167  -0.0141 -0.003  208 GLU   B CD  
3578 O OE1 . GLU   B 227 ? 0.4909 0.3484 0.5381 0.0153  -0.0202 0.0024  208 GLU   B OE1 
3579 O OE2 . GLU   B 227 ? 0.4777 0.3339 0.5241 0.0174  -0.0114 -0.0076 208 GLU   B OE2 
3580 N N   . GLN   B 228 ? 0.2542 0.1702 0.2921 -0.0008 -0.0032 -0.0011 209 GLN   B N   
3581 C CA  . GLN   B 228 ? 0.2457 0.1671 0.2767 -0.0065 -0.0034 0.0013  209 GLN   B CA  
3582 C C   . GLN   B 228 ? 0.2262 0.1575 0.2612 -0.0049 -0.004  0.003   209 GLN   B C   
3583 O O   . GLN   B 228 ? 0.2248 0.1642 0.2662 -0.0019 -0.0015 0.0007  209 GLN   B O   
3584 C CB  . GLN   B 228 ? 0.2462 0.1725 0.2734 -0.0101 0.0008  -0.0017 209 GLN   B CB  
3585 C CG  . GLN   B 228 ? 0.2319 0.1653 0.2536 -0.0155 0.0012  0.0004  209 GLN   B CG  
3586 C CD  . GLN   B 228 ? 0.2475 0.1739 0.262  -0.0205 -0.0014 0.004   209 GLN   B CD  
3587 O OE1 . GLN   B 228 ? 0.2819 0.2098 0.2936 -0.0219 -0.0033 0.0077  209 GLN   B OE1 
3588 N NE2 . GLN   B 228 ? 0.226  0.1448 0.2367 -0.0235 -0.0014 0.0031  209 GLN   B NE2 
3589 N N   . LYS   B 229 ? 0.2209 0.1509 0.2513 -0.0072 -0.0075 0.007   210 LYS   B N   
3590 C CA  . LYS   B 229 ? 0.2151 0.1529 0.2471 -0.0064 -0.0087 0.0085  210 LYS   B CA  
3591 C C   . LYS   B 229 ? 0.2101 0.1557 0.2366 -0.0104 -0.0057 0.0079  210 LYS   B C   
3592 O O   . LYS   B 229 ? 0.2217 0.1654 0.2411 -0.015  -0.0048 0.0089  210 LYS   B O   
3593 C CB  . LYS   B 229 ? 0.2342 0.1658 0.2626 -0.0068 -0.0143 0.013   210 LYS   B CB  
3594 C CG  . LYS   B 229 ? 0.24   0.1776 0.2689 -0.0059 -0.0167 0.0144  210 LYS   B CG  
3595 C CD  . LYS   B 229 ? 0.3231 0.2526 0.3483 -0.0059 -0.023  0.0188  210 LYS   B CD  
3596 C CE  . LYS   B 229 ? 0.3766 0.3091 0.401  -0.0052 -0.0269 0.0205  210 LYS   B CE  
3597 N NZ  . LYS   B 229 ? 0.3778 0.3013 0.4008 -0.0042 -0.0341 0.0248  210 LYS   B NZ  
3598 N N   . PHE   B 230 ? 0.1961 0.1505 0.2265 -0.0086 -0.0047 0.0068  211 PHE   B N   
3599 C CA  . PHE   B 230 ? 0.2053 0.1671 0.2315 -0.0111 -0.0025 0.0063  211 PHE   B CA  
3600 C C   . PHE   B 230 ? 0.1911 0.1556 0.2175 -0.0095 -0.0052 0.0076  211 PHE   B C   
3601 O O   . PHE   B 230 ? 0.2034 0.1684 0.2366 -0.006  -0.0074 0.0076  211 PHE   B O   
3602 C CB  . PHE   B 230 ? 0.2032 0.1726 0.2338 -0.0102 0.0014  0.003   211 PHE   B CB  
3603 C CG  . PHE   B 230 ? 0.2087 0.1763 0.2374 -0.0125 0.0041  0.0012  211 PHE   B CG  
3604 C CD1 . PHE   B 230 ? 0.2236 0.1943 0.2472 -0.0168 0.0057  0.0012  211 PHE   B CD1 
3605 C CD2 . PHE   B 230 ? 0.2475 0.2102 0.2796 -0.0105 0.0047  -0.0006 211 PHE   B CD2 
3606 C CE1 . PHE   B 230 ? 0.2634 0.2313 0.2849 -0.0196 0.0072  -0.0002 211 PHE   B CE1 
3607 C CE2 . PHE   B 230 ? 0.2666 0.2261 0.2955 -0.0129 0.0066  -0.0025 211 PHE   B CE2 
3608 C CZ  . PHE   B 230 ? 0.2568 0.2188 0.2805 -0.0177 0.0075  -0.0022 211 PHE   B CZ  
3609 N N   . SER   B 231 ? 0.1988 0.1652 0.2179 -0.012  -0.0051 0.0086  212 SER   B N   
3610 C CA  . SER   B 231 ? 0.201  0.1691 0.2182 -0.0108 -0.0076 0.0092  212 SER   B CA  
3611 C C   . SER   B 231 ? 0.1927 0.168  0.2158 -0.0084 -0.0062 0.0067  212 SER   B C   
3612 O O   . SER   B 231 ? 0.1852 0.1656 0.2114 -0.0084 -0.0026 0.0045  212 SER   B O   
3613 C CB  . SER   B 231 ? 0.233  0.2018 0.24   -0.014  -0.0066 0.0102  212 SER   B CB  
3614 O OG  . SER   B 231 ? 0.3173 0.2792 0.3177 -0.0171 -0.0078 0.0132  212 SER   B OG  
3615 N N   . SER   B 232 ? 0.1833 0.1584 0.2075 -0.0066 -0.0098 0.0071  213 SER   B N   
3616 C CA  . SER   B 232 ? 0.1868 0.1675 0.215  -0.0049 -0.0091 0.0051  213 SER   B CA  
3617 C C   . SER   B 232 ? 0.2005 0.1792 0.2223 -0.0049 -0.0125 0.0055  213 SER   B C   
3618 O O   . SER   B 232 ? 0.2002 0.1732 0.2176 -0.0055 -0.0166 0.0076  213 SER   B O   
3619 C CB  . SER   B 232 ? 0.2187 0.2008 0.2577 -0.0024 -0.0103 0.005   213 SER   B CB  
3620 O OG  . SER   B 232 ? 0.2518 0.2383 0.2946 -0.0013 -0.0106 0.0038  213 SER   B OG  
3621 N N   . LEU   B 233 ? 0.1922 0.1749 0.2131 -0.0042 -0.0112 0.0033  214 LEU   B N   
3622 C CA  . LEU   B 233 ? 0.2082 0.1881 0.2224 -0.0039 -0.0144 0.0028  214 LEU   B CA  
3623 C C   . LEU   B 233 ? 0.2024 0.1808 0.2233 -0.0025 -0.0194 0.0034  214 LEU   B C   
3624 O O   . LEU   B 233 ? 0.202  0.1845 0.2313 -0.0013 -0.0185 0.0024  214 LEU   B O   
3625 C CB  . LEU   B 233 ? 0.2129 0.1971 0.2242 -0.0032 -0.0109 -0.0001 214 LEU   B CB  
3626 C CG  . LEU   B 233 ? 0.2484 0.2293 0.2514 -0.0025 -0.0133 -0.0017 214 LEU   B CG  
3627 C CD1 . LEU   B 233 ? 0.2722 0.2486 0.2633 -0.0043 -0.0138 -0.0006 214 LEU   B CD1 
3628 C CD2 . LEU   B 233 ? 0.2454 0.2309 0.248  -0.0007 -0.0097 -0.005  214 LEU   B CD2 
3629 N N   . PRO   B 234 ? 0.2167 0.1895 0.2343 -0.0029 -0.0249 0.0052  215 PRO   B N   
3630 C CA  . PRO   B 234 ? 0.2377 0.2101 0.264  -0.0019 -0.0301 0.0063  215 PRO   B CA  
3631 C C   . PRO   B 234 ? 0.2759 0.2474 0.3005 -0.0017 -0.0332 0.0045  215 PRO   B C   
3632 O O   . PRO   B 234 ? 0.343  0.3099 0.3651 -0.0023 -0.0395 0.0056  215 PRO   B O   
3633 C CB  . PRO   B 234 ? 0.2405 0.2072 0.2642 -0.0025 -0.0355 0.0093  215 PRO   B CB  
3634 C CG  . PRO   B 234 ? 0.2416 0.2037 0.2504 -0.0043 -0.0346 0.0092  215 PRO   B CG  
3635 C CD  . PRO   B 234 ? 0.2238 0.1907 0.231  -0.0045 -0.027  0.0072  215 PRO   B CD  
3636 N N   . LEU   B 235 ? 0.2436 0.2193 0.2718 -0.001  -0.0298 0.0025  216 LEU   B N   
3637 C CA  . LEU   B 235 ? 0.2339 0.2075 0.2602 -0.0008 -0.0327 0.0007  216 LEU   B CA  
3638 C C   . LEU   B 235 ? 0.2327 0.2074 0.2696 -0.0012 -0.0369 0.0021  216 LEU   B C   
3639 O O   . LEU   B 235 ? 0.2397 0.2198 0.288  -0.001  -0.035  0.0036  216 LEU   B O   
3640 C CB  . LEU   B 235 ? 0.2436 0.2207 0.269  0.0003  -0.0275 -0.002  216 LEU   B CB  
3641 C CG  . LEU   B 235 ? 0.2645 0.2423 0.2803 0.0008  -0.0227 -0.0039 216 LEU   B CG  
3642 C CD1 . LEU   B 235 ? 0.3083 0.2896 0.3249 0.0025  -0.019  -0.0064 216 LEU   B CD1 
3643 C CD2 . LEU   B 235 ? 0.2914 0.263  0.2944 0.0004  -0.0252 -0.0048 216 LEU   B CD2 
3644 N N   . GLY   B 236 ? 0.2264 0.196  0.2594 -0.0019 -0.0426 0.0015  217 GLY   B N   
3645 C CA  . GLY   B 236 ? 0.2356 0.206  0.2784 -0.0031 -0.0472 0.0027  217 GLY   B CA  
3646 C C   . GLY   B 236 ? 0.2284 0.1989 0.2717 -0.0029 -0.0454 0.0007  217 GLY   B C   
3647 O O   . GLY   B 236 ? 0.227  0.1963 0.2623 -0.0014 -0.0414 -0.002  217 GLY   B O   
3648 N N   . ARG   B 237 ? 0.2243 0.1966 0.2775 -0.0044 -0.0482 0.0023  218 ARG   B N   
3649 C CA  . ARG   B 237 ? 0.2308 0.2029 0.2855 -0.0047 -0.0468 0.0012  218 ARG   B CA  
3650 C C   . ARG   B 237 ? 0.2212 0.1847 0.2635 -0.0037 -0.0492 -0.0024 218 ARG   B C   
3651 O O   . ARG   B 237 ? 0.23   0.1928 0.2695 -0.0022 -0.046  -0.0043 218 ARG   B O   
3652 C CB  . ARG   B 237 ? 0.2658 0.2411 0.3334 -0.0073 -0.0497 0.0042  218 ARG   B CB  
3653 C CG  . ARG   B 237 ? 0.3447 0.3152 0.4131 -0.0097 -0.0581 0.0051  218 ARG   B CG  
3654 C CD  . ARG   B 237 ? 0.44   0.4128 0.52   -0.013  -0.0611 0.0077  218 ARG   B CD  
3655 N NE  . ARG   B 237 ? 0.5094 0.4781 0.5854 -0.0132 -0.0597 0.0062  218 ARG   B NE  
3656 C CZ  . ARG   B 237 ? 0.4859 0.457  0.5706 -0.016  -0.06   0.0086  218 ARG   B CZ  
3657 N NH1 . ARG   B 237 ? 0.5308 0.5096 0.6295 -0.0188 -0.0609 0.0125  218 ARG   B NH1 
3658 N NH2 . ARG   B 237 ? 0.4484 0.4146 0.5283 -0.0159 -0.0591 0.0075  218 ARG   B NH2 
3659 N N   . GLU   B 238 ? 0.2415 0.1979 0.2759 -0.0044 -0.055  -0.0034 219 GLU   B N   
3660 C CA  . GLU   B 238 ? 0.2499 0.1972 0.2716 -0.0033 -0.0572 -0.0075 219 GLU   B CA  
3661 C C   . GLU   B 238 ? 0.2429 0.191  0.2552 0       -0.0506 -0.0106 219 GLU   B C   
3662 O O   . GLU   B 238 ? 0.2442 0.1893 0.2516 0.0023  -0.0488 -0.0137 219 GLU   B O   
3663 C CB  . GLU   B 238 ? 0.2936 0.2328 0.3073 -0.005  -0.0649 -0.008  219 GLU   B CB  
3664 C CG  . GLU   B 238 ? 0.3457 0.2841 0.3695 -0.0086 -0.0725 -0.0051 219 GLU   B CG  
3665 C CD  . GLU   B 238 ? 0.5043 0.4511 0.5415 -0.0103 -0.0735 -0.0003 219 GLU   B CD  
3666 O OE1 . GLU   B 238 ? 0.4887 0.4411 0.5273 -0.0087 -0.0687 0.0008  219 GLU   B OE1 
3667 O OE2 . GLU   B 238 ? 0.5925 0.5401 0.6395 -0.0133 -0.0795 0.0022  219 GLU   B OE2 
3668 N N   . ALA   B 239 ? 0.239  0.1911 0.2491 0.0003  -0.0472 -0.0095 220 ALA   B N   
3669 C CA  . ALA   B 239 ? 0.2399 0.1941 0.2421 0.0028  -0.0408 -0.012  220 ALA   B CA  
3670 C C   . ALA   B 239 ? 0.2195 0.1805 0.2289 0.0044  -0.035  -0.0121 220 ALA   B C   
3671 O O   . ALA   B 239 ? 0.2101 0.1717 0.2143 0.0069  -0.0311 -0.0151 220 ALA   B O   
3672 C CB  . ALA   B 239 ? 0.2581 0.2146 0.2569 0.0019  -0.039  -0.0102 220 ALA   B CB  
3673 N N   . VAL   B 240 ? 0.2014 0.168  0.2226 0.003   -0.0342 -0.009  221 VAL   B N   
3674 C CA  . VAL   B 240 ? 0.202  0.1744 0.2289 0.0041  -0.0294 -0.0089 221 VAL   B CA  
3675 C C   . VAL   B 240 ? 0.2123 0.1804 0.238  0.0055  -0.031  -0.0109 221 VAL   B C   
3676 O O   . VAL   B 240 ? 0.2048 0.1743 0.2278 0.0081  -0.0276 -0.013  221 VAL   B O   
3677 C CB  . VAL   B 240 ? 0.204  0.1823 0.2426 0.0022  -0.0284 -0.0054 221 VAL   B CB  
3678 C CG1 . VAL   B 240 ? 0.1976 0.1803 0.2406 0.0028  -0.0243 -0.0051 221 VAL   B CG1 
3679 C CG2 . VAL   B 240 ? 0.2135 0.1954 0.2539 0.0014  -0.0264 -0.0037 221 VAL   B CG2 
3680 N N   . GLU   B 241 ? 0.2083 0.1706 0.2357 0.0039  -0.0368 -0.0103 222 GLU   B N   
3681 C CA  . GLU   B 241 ? 0.224  0.1806 0.2502 0.005   -0.0391 -0.012  222 GLU   B CA  
3682 C C   . GLU   B 241 ? 0.2276 0.1784 0.2423 0.0086  -0.0387 -0.0168 222 GLU   B C   
3683 O O   . GLU   B 241 ? 0.256  0.2056 0.2697 0.0116  -0.037  -0.0188 222 GLU   B O   
3684 C CB  . GLU   B 241 ? 0.2791 0.2296 0.3082 0.0019  -0.0461 -0.0105 222 GLU   B CB  
3685 C CG  . GLU   B 241 ? 0.3932 0.3493 0.4348 -0.0016 -0.0466 -0.0059 222 GLU   B CG  
3686 C CD  . GLU   B 241 ? 0.5425 0.4946 0.588  -0.0053 -0.0537 -0.004  222 GLU   B CD  
3687 O OE1 . GLU   B 241 ? 0.5391 0.4817 0.5794 -0.0058 -0.059  -0.0059 222 GLU   B OE1 
3688 O OE2 . GLU   B 241 ? 0.5746 0.5327 0.6284 -0.0075 -0.0541 -0.001  222 GLU   B OE2 
3689 N N   . ALA   B 242 ? 0.2322 0.1792 0.2379 0.0086  -0.0401 -0.0187 223 ALA   B N   
3690 C CA  . ALA   B 242 ? 0.2546 0.1964 0.2485 0.0122  -0.0389 -0.0236 223 ALA   B CA  
3691 C C   . ALA   B 242 ? 0.2419 0.1918 0.236  0.0153  -0.0313 -0.0249 223 ALA   B C   
3692 O O   . ALA   B 242 ? 0.2499 0.1979 0.24   0.0193  -0.0294 -0.0286 223 ALA   B O   
3693 C CB  . ALA   B 242 ? 0.2876 0.2245 0.2709 0.011   -0.0412 -0.0249 223 ALA   B CB  
3694 N N   . ALA   B 243 ? 0.2179 0.1768 0.2172 0.0137  -0.0273 -0.0219 224 ALA   B N   
3695 C CA  . ALA   B 243 ? 0.2173 0.1841 0.2169 0.016   -0.0207 -0.0229 224 ALA   B CA  
3696 C C   . ALA   B 243 ? 0.2169 0.1868 0.224  0.0181  -0.0195 -0.0229 224 ALA   B C   
3697 O O   . ALA   B 243 ? 0.2127 0.1859 0.2188 0.0216  -0.016  -0.0254 224 ALA   B O   
3698 C CB  . ALA   B 243 ? 0.2195 0.1936 0.2231 0.0131  -0.0177 -0.0195 224 ALA   B CB  
3699 N N   . VAL   B 244 ? 0.214  0.1828 0.2285 0.0161  -0.0225 -0.0199 225 VAL   B N   
3700 C CA  . VAL   B 244 ? 0.2037 0.1742 0.2242 0.0175  -0.0222 -0.0192 225 VAL   B CA  
3701 C C   . VAL   B 244 ? 0.2127 0.1754 0.2288 0.0215  -0.0247 -0.0229 225 VAL   B C   
3702 O O   . VAL   B 244 ? 0.2208 0.1862 0.2386 0.0249  -0.0226 -0.0241 225 VAL   B O   
3703 C CB  . VAL   B 244 ? 0.2274 0.198  0.2556 0.0138  -0.0247 -0.015  225 VAL   B CB  
3704 C CG1 . VAL   B 244 ? 0.2419 0.212  0.2744 0.0147  -0.0254 -0.0138 225 VAL   B CG1 
3705 C CG2 . VAL   B 244 ? 0.2232 0.2021 0.256  0.0111  -0.0211 -0.0121 225 VAL   B CG2 
3706 N N   . LYS   B 245 ? 0.2175 0.1705 0.2278 0.021   -0.0294 -0.0246 226 LYS   B N   
3707 C CA  . LYS   B 245 ? 0.2319 0.1756 0.2367 0.0251  -0.032  -0.0288 226 LYS   B CA  
3708 C C   . LYS   B 245 ? 0.2353 0.1818 0.2335 0.0299  -0.027  -0.0336 226 LYS   B C   
3709 O O   . LYS   B 245 ? 0.2522 0.1966 0.2499 0.035   -0.0262 -0.0368 226 LYS   B O   
3710 C CB  . LYS   B 245 ? 0.2762 0.2082 0.2752 0.023   -0.0385 -0.0299 226 LYS   B CB  
3711 C CG  . LYS   B 245 ? 0.3158 0.2455 0.3228 0.0182  -0.0434 -0.0253 226 LYS   B CG  
3712 C CD  . LYS   B 245 ? 0.3954 0.3145 0.3977 0.0154  -0.0503 -0.026  226 LYS   B CD  
3713 C CE  . LYS   B 245 ? 0.5078 0.4288 0.5196 0.0096  -0.0539 -0.0206 226 LYS   B CE  
3714 N NZ  . LYS   B 245 ? 0.5441 0.459  0.5604 0.0084  -0.0577 -0.0188 226 LYS   B NZ  
3715 N N   . GLU   B 246 ? 0.2378 0.1885 0.2309 0.0287  -0.0239 -0.034  227 GLU   B N   
3716 C CA  . GLU   B 246 ? 0.2482 0.2026 0.235  0.0326  -0.0184 -0.0382 227 GLU   B CA  
3717 C C   . GLU   B 246 ? 0.2302 0.1958 0.2252 0.0352  -0.0131 -0.0375 227 GLU   B C   
3718 O O   . GLU   B 246 ? 0.2397 0.2075 0.2332 0.0403  -0.0098 -0.0414 227 GLU   B O   
3719 C CB  . GLU   B 246 ? 0.2564 0.2129 0.236  0.0295  -0.0164 -0.0376 227 GLU   B CB  
3720 C CG  . GLU   B 246 ? 0.3048 0.2652 0.2764 0.0324  -0.0104 -0.0414 227 GLU   B CG  
3721 C CD  . GLU   B 246 ? 0.3942 0.3557 0.3581 0.0286  -0.0089 -0.0398 227 GLU   B CD  
3722 O OE1 . GLU   B 246 ? 0.4217 0.3793 0.3856 0.0242  -0.0136 -0.0364 227 GLU   B OE1 
3723 O OE2 . GLU   B 246 ? 0.4253 0.3919 0.3833 0.0297  -0.003  -0.0417 227 GLU   B OE2 
3724 N N   . ALA   B 247 ? 0.2185 0.1913 0.2227 0.032   -0.0127 -0.0328 228 ALA   B N   
3725 C CA  . ALA   B 247 ? 0.2184 0.2017 0.2303 0.0335  -0.0087 -0.0317 228 ALA   B CA  
3726 C C   . ALA   B 247 ? 0.2307 0.2121 0.2482 0.0372  -0.011  -0.032  228 ALA   B C   
3727 O O   . ALA   B 247 ? 0.2327 0.2227 0.257  0.0384  -0.0086 -0.0308 228 ALA   B O   
3728 C CB  . ALA   B 247 ? 0.2234 0.2141 0.2409 0.0285  -0.0073 -0.0269 228 ALA   B CB  
3729 N N   . GLY   B 248 ? 0.2356 0.2056 0.2504 0.0384  -0.0161 -0.0332 229 GLY   B N   
3730 C CA  . GLY   B 248 ? 0.2521 0.2183 0.271  0.0424  -0.0188 -0.0338 229 GLY   B CA  
3731 C C   . GLY   B 248 ? 0.2324 0.1966 0.2573 0.039   -0.0227 -0.0288 229 GLY   B C   
3732 O O   . GLY   B 248 ? 0.238  0.2033 0.268  0.0415  -0.0238 -0.0276 229 GLY   B O   
3733 N N   . TYR   B 249 ? 0.2246 0.1854 0.2488 0.0334  -0.0252 -0.0258 230 TYR   B N   
3734 C CA  . TYR   B 249 ? 0.216  0.1748 0.2455 0.0298  -0.0284 -0.021  230 TYR   B CA  
3735 C C   . TYR   B 249 ? 0.2273 0.174  0.2538 0.0275  -0.0343 -0.0208 230 TYR   B C   
3736 O O   . TYR   B 249 ? 0.2583 0.1996 0.2788 0.0277  -0.0356 -0.0239 230 TYR   B O   
3737 C CB  . TYR   B 249 ? 0.1981 0.1654 0.2315 0.0245  -0.0257 -0.0169 230 TYR   B CB  
3738 C CG  . TYR   B 249 ? 0.1799 0.1585 0.2159 0.0254  -0.0206 -0.0168 230 TYR   B CG  
3739 C CD1 . TYR   B 249 ? 0.1875 0.1715 0.2207 0.0258  -0.0166 -0.019  230 TYR   B CD1 
3740 C CD2 . TYR   B 249 ? 0.1795 0.1632 0.2205 0.0247  -0.02   -0.0137 230 TYR   B CD2 
3741 C CE1 . TYR   B 249 ? 0.1856 0.1798 0.2216 0.0257  -0.0123 -0.0184 230 TYR   B CE1 
3742 C CE2 . TYR   B 249 ? 0.1851 0.1787 0.2284 0.0247  -0.0159 -0.0134 230 TYR   B CE2 
3743 C CZ  . TYR   B 249 ? 0.1927 0.1917 0.234  0.0252  -0.0121 -0.0158 230 TYR   B CZ  
3744 O OH  . TYR   B 249 ? 0.1991 0.2078 0.2431 0.0243  -0.0084 -0.0151 230 TYR   B OH  
3745 N N   . THR   B 250 ? 0.213  0.1557 0.2434 0.0249  -0.0377 -0.017  231 THR   B N   
3746 C CA  . THR   B 250 ? 0.2349 0.1681 0.2647 0.0209  -0.0432 -0.0154 231 THR   B CA  
3747 C C   . THR   B 250 ? 0.2415 0.181  0.2773 0.0147  -0.0423 -0.0101 231 THR   B C   
3748 O O   . THR   B 250 ? 0.2879 0.2346 0.3282 0.0135  -0.0394 -0.0068 231 THR   B O   
3749 C CB  . THR   B 250 ? 0.2894 0.2119 0.3191 0.022   -0.0483 -0.0146 231 THR   B CB  
3750 O OG1 . THR   B 250 ? 0.3102 0.2376 0.3453 0.0211  -0.0472 -0.0101 231 THR   B OG1 
3751 C CG2 . THR   B 250 ? 0.3188 0.2344 0.3433 0.029   -0.0492 -0.0201 231 THR   B CG2 
3752 N N   . ILE   B 251 ? 0.2376 0.175  0.2736 0.0108  -0.0447 -0.0094 232 ILE   B N   
3753 C CA  . ILE   B 251 ? 0.2421 0.1866 0.2852 0.0055  -0.0434 -0.0048 232 ILE   B CA  
3754 C C   . ILE   B 251 ? 0.2256 0.1664 0.2735 0.0014  -0.0466 -0.0002 232 ILE   B C   
3755 O O   . ILE   B 251 ? 0.2578 0.1882 0.3037 0.0004  -0.0522 -0.0006 232 ILE   B O   
3756 C CB  . ILE   B 251 ? 0.2732 0.218  0.3154 0.0036  -0.0448 -0.0058 232 ILE   B CB  
3757 C CG1 . ILE   B 251 ? 0.3472 0.2971 0.3845 0.007   -0.0404 -0.0092 232 ILE   B CG1 
3758 C CG2 . ILE   B 251 ? 0.2801 0.232  0.3316 -0.0018 -0.0441 -0.0009 232 ILE   B CG2 
3759 C CD1 . ILE   B 251 ? 0.4074 0.3577 0.4427 0.0055  -0.0417 -0.01   232 ILE   B CD1 
3760 N N   . GLU   B 252 ? 0.2169 0.165  0.27   -0.0012 -0.0431 0.004   233 GLU   B N   
3761 C CA  . GLU   B 252 ? 0.2166 0.1629 0.2742 -0.0059 -0.0449 0.0091  233 GLU   B CA  
3762 C C   . GLU   B 252 ? 0.2056 0.1572 0.2703 -0.0112 -0.0446 0.0121  233 GLU   B C   
3763 O O   . GLU   B 252 ? 0.2147 0.1618 0.283  -0.0155 -0.0487 0.0149  233 GLU   B O   
3764 C CB  . GLU   B 252 ? 0.2514 0.2033 0.3097 -0.0059 -0.0408 0.0121  233 GLU   B CB  
3765 C CG  . GLU   B 252 ? 0.3046 0.2529 0.3579 -0.0009 -0.0414 0.0101  233 GLU   B CG  
3766 C CD  . GLU   B 252 ? 0.4736 0.412  0.5259 -0.0024 -0.0464 0.0133  233 GLU   B CD  
3767 O OE1 . GLU   B 252 ? 0.511  0.4389 0.5603 -0.0001 -0.0514 0.0108  233 GLU   B OE1 
3768 O OE2 . GLU   B 252 ? 0.5155 0.4557 0.5696 -0.0063 -0.0455 0.0184  233 GLU   B OE2 
3769 N N   . TRP   B 253 ? 0.1877 0.1493 0.2555 -0.011  -0.0396 0.0119  234 TRP   B N   
3770 C CA  . TRP   B 253 ? 0.2353 0.2022 0.3106 -0.0148 -0.0395 0.0139  234 TRP   B CA  
3771 C C   . TRP   B 253 ? 0.1787 0.1522 0.2547 -0.0127 -0.0363 0.0117  234 TRP   B C   
3772 O O   . TRP   B 253 ? 0.1721 0.1484 0.2435 -0.0092 -0.0325 0.0093  234 TRP   B O   
3773 C CB  . TRP   B 253 ? 0.2975 0.2697 0.3804 -0.0196 -0.0375 0.0189  234 TRP   B CB  
3774 C CG  . TRP   B 253 ? 0.3051 0.2843 0.3876 -0.0192 -0.0311 0.0204  234 TRP   B CG  
3775 C CD1 . TRP   B 253 ? 0.3558 0.3448 0.4421 -0.0191 -0.0251 0.0206  234 TRP   B CD1 
3776 C CD2 . TRP   B 253 ? 0.3179 0.2945 0.3982 -0.0211 -0.0307 0.0235  234 TRP   B CD2 
3777 N NE1 . TRP   B 253 ? 0.3681 0.3605 0.453  -0.0204 -0.0207 0.023   234 TRP   B NE1 
3778 C CE2 . TRP   B 253 ? 0.362  0.3473 0.4438 -0.0222 -0.0243 0.0254  234 TRP   B CE2 
3779 C CE3 . TRP   B 253 ? 0.3494 0.3164 0.4269 -0.0226 -0.0358 0.0256  234 TRP   B CE3 
3780 C CZ2 . TRP   B 253 ? 0.4241 0.4087 0.5028 -0.0243 -0.0226 0.0288  234 TRP   B CZ2 
3781 C CZ3 . TRP   B 253 ? 0.3984 0.365  0.4742 -0.0249 -0.0343 0.0295  234 TRP   B CZ3 
3782 C CH2 . TRP   B 253 ? 0.4267 0.4021 0.5025 -0.0256 -0.0278 0.031   234 TRP   B CH2 
3783 N N   . PHE   B 254 ? 0.1649 0.1412 0.2471 -0.015  -0.0381 0.0128  235 PHE   B N   
3784 C CA  . PHE   B 254 ? 0.165  0.146  0.2477 -0.0131 -0.0363 0.0109  235 PHE   B CA  
3785 C C   . PHE   B 254 ? 0.1526 0.1408 0.2468 -0.0163 -0.0362 0.0141  235 PHE   B C   
3786 O O   . PHE   B 254 ? 0.1598 0.1457 0.2592 -0.0197 -0.0413 0.0161  235 PHE   B O   
3787 C CB  . PHE   B 254 ? 0.1872 0.1605 0.2623 -0.011  -0.0413 0.0073  235 PHE   B CB  
3788 C CG  . PHE   B 254 ? 0.1995 0.1764 0.272  -0.0084 -0.0389 0.0052  235 PHE   B CG  
3789 C CD1 . PHE   B 254 ? 0.2011 0.1829 0.2805 -0.0099 -0.0396 0.0069  235 PHE   B CD1 
3790 C CD2 . PHE   B 254 ? 0.2321 0.2078 0.2957 -0.0048 -0.036  0.0019  235 PHE   B CD2 
3791 C CE1 . PHE   B 254 ? 0.2312 0.2154 0.3078 -0.0077 -0.0375 0.0055  235 PHE   B CE1 
3792 C CE2 . PHE   B 254 ? 0.2442 0.2226 0.305  -0.0032 -0.034  0.0006  235 PHE   B CE2 
3793 C CZ  . PHE   B 254 ? 0.2349 0.217  0.3018 -0.0047 -0.0347 0.0025  235 PHE   B CZ  
3794 N N   . GLU   B 255 ? 0.1529 0.1496 0.2516 -0.0154 -0.0306 0.0146  236 GLU   B N   
3795 C CA  . GLU   B 255 ? 0.1526 0.1573 0.2634 -0.0176 -0.0296 0.0174  236 GLU   B CA  
3796 C C   . GLU   B 255 ? 0.1443 0.1519 0.2561 -0.0148 -0.0288 0.0157  236 GLU   B C   
3797 O O   . GLU   B 255 ? 0.16   0.1675 0.2651 -0.0118 -0.025  0.0133  236 GLU   B O   
3798 C CB  . GLU   B 255 ? 0.159  0.1711 0.2749 -0.0191 -0.0229 0.0198  236 GLU   B CB  
3799 C CG  . GLU   B 255 ? 0.1994 0.2213 0.3289 -0.0209 -0.0204 0.0225  236 GLU   B CG  
3800 C CD  . GLU   B 255 ? 0.3357 0.3643 0.4691 -0.023  -0.0137 0.0249  236 GLU   B CD  
3801 O OE1 . GLU   B 255 ? 0.3784 0.4028 0.5056 -0.025  -0.0135 0.0262  236 GLU   B OE1 
3802 O OE2 . GLU   B 255 ? 0.3681 0.4057 0.511  -0.023  -0.009  0.026   236 GLU   B OE2 
3803 N N   . VAL   B 256 ? 0.1452 0.156  0.2661 -0.0159 -0.0321 0.0173  237 VAL   B N   
3804 C CA  . VAL   B 256 ? 0.1545 0.1686 0.2785 -0.0134 -0.0317 0.0166  237 VAL   B CA  
3805 C C   . VAL   B 256 ? 0.1565 0.1808 0.2948 -0.0141 -0.0281 0.0191  237 VAL   B C   
3806 O O   . VAL   B 256 ? 0.1535 0.182  0.302  -0.0174 -0.03   0.0221  237 VAL   B O   
3807 C CB  . VAL   B 256 ? 0.2086 0.217  0.3304 -0.0135 -0.0397 0.0161  237 VAL   B CB  
3808 C CG1 . VAL   B 256 ? 0.2426 0.2546 0.3697 -0.0113 -0.0403 0.0165  237 VAL   B CG1 
3809 C CG2 . VAL   B 256 ? 0.2441 0.2427 0.3501 -0.012  -0.0417 0.0128  237 VAL   B CG2 
3810 N N   . ILE   B 257 ? 0.1725 0.2012 0.3122 -0.011  -0.0224 0.018   238 ILE   B N   
3811 C CA  . ILE   B 257 ? 0.1971 0.2354 0.3504 -0.0105 -0.0184 0.0196  238 ILE   B CA  
3812 C C   . ILE   B 257 ? 0.1865 0.225  0.3442 -0.0076 -0.0216 0.0193  238 ILE   B C   
3813 O O   . ILE   B 257 ? 0.1868 0.2187 0.3343 -0.0052 -0.0229 0.0171  238 ILE   B O   
3814 C CB  . ILE   B 257 ? 0.2974 0.3408 0.4507 -0.0094 -0.0092 0.0188  238 ILE   B CB  
3815 C CG1 . ILE   B 257 ? 0.3475 0.3875 0.4923 -0.0056 -0.006  0.0156  238 ILE   B CG1 
3816 C CG2 . ILE   B 257 ? 0.3356 0.3779 0.483  -0.0125 -0.0065 0.0196  238 ILE   B CG2 
3817 C CD1 . ILE   B 257 ? 0.3899 0.4345 0.535  -0.0041 0.0028  0.0142  238 ILE   B CD1 
3818 N N   A SER   B 258 ? 0.183  0.2293 0.3562 -0.0076 -0.023  0.0216  239 SER   B N   
3819 N N   B SER   B 258 ? 0.1838 0.2302 0.3569 -0.0076 -0.0226 0.0215  239 SER   B N   
3820 C CA  A SER   B 258 ? 0.1855 0.2316 0.3637 -0.0047 -0.0273 0.0218  239 SER   B CA  
3821 C CA  B SER   B 258 ? 0.1881 0.2347 0.3669 -0.0048 -0.027  0.0218  239 SER   B CA  
3822 C C   A SER   B 258 ? 0.1939 0.2415 0.3726 -0.0002 -0.0215 0.0199  239 SER   B C   
3823 C C   B SER   B 258 ? 0.1973 0.2457 0.3775 -0.0001 -0.0214 0.02    239 SER   B C   
3824 O O   A SER   B 258 ? 0.2213 0.2639 0.3967 0.0024  -0.0251 0.0193  239 SER   B O   
3825 O O   B SER   B 258 ? 0.2293 0.2739 0.4086 0.0026  -0.0252 0.0198  239 SER   B O   
3826 C CB  A SER   B 258 ? 0.2012 0.2554 0.3972 -0.0061 -0.0318 0.0251  239 SER   B CB  
3827 C CB  B SER   B 258 ? 0.2066 0.2613 0.4029 -0.0066 -0.0315 0.0253  239 SER   B CB  
3828 O OG  A SER   B 258 ? 0.2032 0.2689 0.4127 -0.0061 -0.0246 0.0263  239 SER   B OG  
3829 O OG  B SER   B 258 ? 0.234  0.2848 0.4272 -0.0112 -0.0376 0.0266  239 SER   B OG  
3830 N N   . GLN   B 259 ? 0.189  0.2422 0.3703 0.0006  -0.0127 0.0188  240 GLN   B N   
3831 C CA  . GLN   B 259 ? 0.1816 0.2359 0.3641 0.005   -0.0069 0.0166  240 GLN   B CA  
3832 C C   . GLN   B 259 ? 0.1933 0.2375 0.3613 0.0068  -0.0083 0.0142  240 GLN   B C   
3833 O O   . GLN   B 259 ? 0.2057 0.2442 0.3604 0.0049  -0.0079 0.013   240 GLN   B O   
3834 C CB  . GLN   B 259 ? 0.2008 0.2599 0.3824 0.0047  0.0026  0.0152  240 GLN   B CB  
3835 C CG  . GLN   B 259 ? 0.2372 0.2967 0.4187 0.0091  0.0092  0.0122  240 GLN   B CG  
3836 C CD  . GLN   B 259 ? 0.324  0.3909 0.5223 0.0128  0.01    0.0127  240 GLN   B CD  
3837 O OE1 . GLN   B 259 ? 0.3261 0.4034 0.5376 0.012   0.0132  0.0144  240 GLN   B OE1 
3838 N NE2 . GLN   B 259 ? 0.3167 0.3785 0.5151 0.017   0.0075  0.0115  240 GLN   B NE2 
3839 N N   . SER   B 260 ? 0.1802 0.2221 0.3509 0.0105  -0.0096 0.0138  241 SER   B N   
3840 C CA  . SER   B 260 ? 0.197  0.2293 0.3548 0.0118  -0.0109 0.0121  241 SER   B CA  
3841 C C   . SER   B 260 ? 0.1896 0.2215 0.3473 0.0151  -0.0042 0.0095  241 SER   B C   
3842 O O   . SER   B 260 ? 0.1948 0.2337 0.3638 0.0174  0.0005  0.0089  241 SER   B O   
3843 C CB  . SER   B 260 ? 0.2148 0.2424 0.3736 0.0128  -0.0193 0.0141  241 SER   B CB  
3844 O OG  . SER   B 260 ? 0.2171 0.2435 0.3736 0.0095  -0.0258 0.0159  241 SER   B OG  
3845 N N   . TYR   B 261 ? 0.1841 0.2075 0.3286 0.0153  -0.0037 0.0076  242 TYR   B N   
3846 C CA  . TYR   B 261 ? 0.1892 0.2101 0.3323 0.0182  0.0016  0.0049  242 TYR   B CA  
3847 C C   . TYR   B 261 ? 0.2007 0.2209 0.3543 0.0224  -0.0013 0.0058  242 TYR   B C   
3848 O O   . TYR   B 261 ? 0.2088 0.2284 0.3671 0.0225  -0.0084 0.0087  242 TYR   B O   
3849 C CB  . TYR   B 261 ? 0.1889 0.2007 0.3159 0.0164  0.0015  0.0035  242 TYR   B CB  
3850 C CG  . TYR   B 261 ? 0.1795 0.1928 0.2977 0.0132  0.0054  0.002   242 TYR   B CG  
3851 C CD1 . TYR   B 261 ? 0.1675 0.1825 0.2838 0.0134  0.0122  -0.0006 242 TYR   B CD1 
3852 C CD2 . TYR   B 261 ? 0.1828 0.1954 0.2942 0.0101  0.0021  0.0032  242 TYR   B CD2 
3853 C CE1 . TYR   B 261 ? 0.1796 0.1958 0.2878 0.0105  0.0149  -0.0015 242 TYR   B CE1 
3854 C CE2 . TYR   B 261 ? 0.195  0.209  0.2997 0.0077  0.0052  0.0022  242 TYR   B CE2 
3855 C CZ  . TYR   B 261 ? 0.1845 0.2005 0.2878 0.0078  0.0113  0.0001  242 TYR   B CZ  
3856 O OH  . TYR   B 261 ? 0.1964 0.2134 0.2924 0.0053  0.0133  -0.0006 242 TYR   B OH  
3857 N N   . SER   B 262 ? 0.2017 0.2197 0.3566 0.0259  0.0034  0.0032  243 SER   B N   
3858 C CA  . SER   B 262 ? 0.2177 0.2329 0.3815 0.0306  0.0005  0.0037  243 SER   B CA  
3859 C C   . SER   B 262 ? 0.228  0.2329 0.3827 0.0295  -0.0074 0.0061  243 SER   B C   
3860 O O   . SER   B 262 ? 0.2024 0.2007 0.3422 0.026   -0.0073 0.0055  243 SER   B O   
3861 C CB  . SER   B 262 ? 0.2657 0.278  0.4293 0.0344  0.0072  -0.0003 243 SER   B CB  
3862 O OG  . SER   B 262 ? 0.2951 0.3164 0.4654 0.0355  0.0152  -0.0027 243 SER   B OG  
3863 N N   . SER   B 263 ? 0.2832 0.2871 0.4461 0.0318  -0.0144 0.0091  244 SER   B N   
3864 C CA  . SER   B 263 ? 0.3083 0.3023 0.4612 0.03    -0.0221 0.0119  244 SER   B CA  
3865 C C   . SER   B 263 ? 0.312  0.2943 0.4529 0.0302  -0.0211 0.0106  244 SER   B C   
3866 O O   . SER   B 263 ? 0.3315 0.3058 0.4603 0.0272  -0.0257 0.0127  244 SER   B O   
3867 C CB  . SER   B 263 ? 0.3428 0.3379 0.5071 0.0325  -0.0304 0.0156  244 SER   B CB  
3868 O OG  . SER   B 263 ? 0.3516 0.346  0.5269 0.0383  -0.0291 0.0148  244 SER   B OG  
3869 N N   . THR   B 264 ? 0.2971 0.2782 0.4405 0.0332  -0.0152 0.0073  245 THR   B N   
3870 C CA  . THR   B 264 ? 0.3187 0.2883 0.4509 0.0329  -0.0141 0.0058  245 THR   B CA  
3871 C C   . THR   B 264 ? 0.325  0.2937 0.4432 0.028   -0.0089 0.0034  245 THR   B C   
3872 O O   . THR   B 264 ? 0.3609 0.3205 0.4685 0.0262  -0.0081 0.0023  245 THR   B O   
3873 C CB  . THR   B 264 ? 0.3453 0.3129 0.4866 0.0389  -0.0106 0.0029  245 THR   B CB  
3874 O OG1 . THR   B 264 ? 0.3711 0.3487 0.519  0.0401  -0.0028 -0.0006 245 THR   B OG1 
3875 C CG2 . THR   B 264 ? 0.358  0.3257 0.5137 0.0443  -0.0166 0.0057  245 THR   B CG2 
3876 N N   . MET   B 265 ? 0.2685 0.2465 0.3873 0.0256  -0.0057 0.0026  246 MET   B N   
3877 C CA  . MET   B 265 ? 0.2666 0.2451 0.3738 0.0213  -0.0014 0.0006  246 MET   B CA  
3878 C C   . MET   B 265 ? 0.2517 0.2306 0.3509 0.017   -0.0054 0.0031  246 MET   B C   
3879 O O   . MET   B 265 ? 0.2461 0.2215 0.3338 0.0135  -0.0044 0.0026  246 MET   B O   
3880 C CB  . MET   B 265 ? 0.3203 0.3078 0.4315 0.0212  0.005   -0.0019 246 MET   B CB  
3881 C CG  . MET   B 265 ? 0.4149 0.4077 0.5391 0.0258  0.0083  -0.0033 246 MET   B CG  
3882 S SD  . MET   B 265 ? 0.4393 0.4274 0.5611 0.0287  0.0154  -0.0083 246 MET   B SD  
3883 C CE  . MET   B 265 ? 0.2772 0.2601 0.3802 0.0226  0.0176  -0.0102 246 MET   B CE  
3884 N N   . ALA   B 266 ? 0.2422 0.226  0.3473 0.0171  -0.0093 0.0055  247 ALA   B N   
3885 C CA  . ALA   B 266 ? 0.2438 0.2273 0.3407 0.0135  -0.0129 0.0072  247 ALA   B CA  
3886 C C   . ALA   B 266 ? 0.2579 0.2435 0.3616 0.0142  -0.0193 0.0101  247 ALA   B C   
3887 O O   . ALA   B 266 ? 0.3279 0.3189 0.4451 0.0171  -0.0196 0.0105  247 ALA   B O   
3888 C CB  . ALA   B 266 ? 0.2464 0.2359 0.34   0.0111  -0.0086 0.0054  247 ALA   B CB  
3889 N N   . ASN   B 267 ? 0.2099 0.1917 0.3051 0.0117  -0.0243 0.012   248 ASN   B N   
3890 C CA  . ASN   B 267 ? 0.1995 0.1818 0.2997 0.012   -0.0315 0.0147  248 ASN   B CA  
3891 C C   . ASN   B 267 ? 0.2146 0.2017 0.3141 0.0097  -0.0323 0.0143  248 ASN   B C   
3892 O O   . ASN   B 267 ? 0.2549 0.239  0.3497 0.0081  -0.0385 0.016   248 ASN   B O   
3893 C CB  . ASN   B 267 ? 0.2388 0.212  0.3289 0.0109  -0.0376 0.0174  248 ASN   B CB  
3894 C CG  . ASN   B 267 ? 0.2333 0.2022 0.307  0.0072  -0.0365 0.0167  248 ASN   B CG  
3895 O OD1 . ASN   B 267 ? 0.2174 0.1898 0.2872 0.0058  -0.0305 0.014   248 ASN   B OD1 
3896 N ND2 . ASN   B 267 ? 0.2614 0.2231 0.3249 0.0054  -0.042  0.0192  248 ASN   B ND2 
3897 N N   . ASN   B 268 ? 0.1919 0.1858 0.296  0.0095  -0.0267 0.0123  249 ASN   B N   
3898 C CA  . ASN   B 268 ? 0.1806 0.1778 0.2836 0.0072  -0.0277 0.012   249 ASN   B CA  
3899 C C   . ASN   B 268 ? 0.2019 0.2036 0.3171 0.0074  -0.0325 0.0141  249 ASN   B C   
3900 O O   . ASN   B 268 ? 0.2104 0.2158 0.3381 0.0098  -0.0334 0.0155  249 ASN   B O   
3901 C CB  . ASN   B 268 ? 0.1864 0.188  0.2886 0.0065  -0.0207 0.0097  249 ASN   B CB  
3902 C CG  . ASN   B 268 ? 0.1922 0.2009 0.3068 0.0082  -0.016  0.0093  249 ASN   B CG  
3903 O OD1 . ASN   B 268 ? 0.1873 0.1958 0.3073 0.0109  -0.0144 0.0092  249 ASN   B OD1 
3904 N ND2 . ASN   B 268 ? 0.1935 0.2078 0.3118 0.0069  -0.0129 0.0089  249 ASN   B ND2 
3905 N N   . GLU   B 269 ? 0.1905 0.1925 0.3031 0.0049  -0.0353 0.0142  250 GLU   B N   
3906 C CA  . GLU   B 269 ? 0.1982 0.2052 0.3224 0.0038  -0.0398 0.0161  250 GLU   B CA  
3907 C C   . GLU   B 269 ? 0.1848 0.1962 0.3102 0.0019  -0.0353 0.0149  250 GLU   B C   
3908 O O   . GLU   B 269 ? 0.2004 0.2084 0.3188 -0.0004 -0.038  0.0144  250 GLU   B O   
3909 C CB  . GLU   B 269 ? 0.247  0.248  0.3649 0.0019  -0.0486 0.0173  250 GLU   B CB  
3910 C CG  . GLU   B 269 ? 0.3421 0.3381 0.458  0.0034  -0.0538 0.0192  250 GLU   B CG  
3911 C CD  . GLU   B 269 ? 0.5761 0.5653 0.684  0.0014  -0.0629 0.0205  250 GLU   B CD  
3912 O OE1 . GLU   B 269 ? 0.6683 0.6497 0.7632 0.0014  -0.0649 0.0206  250 GLU   B OE1 
3913 O OE2 . GLU   B 269 ? 0.6404 0.6316 0.7543 -0.0006 -0.0681 0.0215  250 GLU   B OE2 
3914 N N   . GLY   B 270 ? 0.1741 0.192  0.307  0.003   -0.0285 0.0144  251 GLY   B N   
3915 C CA  . GLY   B 270 ? 0.1738 0.1959 0.3078 0.0011  -0.0239 0.0139  251 GLY   B CA  
3916 C C   . GLY   B 270 ? 0.1523 0.1699 0.2725 0.0006  -0.02   0.0114  251 GLY   B C   
3917 O O   . GLY   B 270 ? 0.1605 0.1732 0.2711 0.0018  -0.0192 0.0098  251 GLY   B O   
3918 N N   . LEU   B 271 ? 0.149  0.1689 0.2688 -0.0013 -0.0176 0.0114  252 LEU   B N   
3919 C CA  . LEU   B 271 ? 0.1655 0.1826 0.2745 -0.0017 -0.014  0.0094  252 LEU   B CA  
3920 C C   . LEU   B 271 ? 0.1531 0.1684 0.26   -0.004  -0.0167 0.01    252 LEU   B C   
3921 O O   . LEU   B 271 ? 0.1622 0.1796 0.277  -0.0059 -0.0198 0.0121  252 LEU   B O   
3922 C CB  . LEU   B 271 ? 0.2024 0.2243 0.3135 -0.0012 -0.0067 0.0087  252 LEU   B CB  
3923 C CG  . LEU   B 271 ? 0.2543 0.2755 0.3636 0.0012  -0.0032 0.007   252 LEU   B CG  
3924 C CD1 . LEU   B 271 ? 0.2769 0.3031 0.3984 0.0029  -0.0019 0.008   252 LEU   B CD1 
3925 C CD2 . LEU   B 271 ? 0.2658 0.2877 0.3689 0.001   0.0028  0.0052  252 LEU   B CD2 
3926 N N   . PHE   B 272 ? 0.1472 0.1586 0.2438 -0.0039 -0.0157 0.0082  253 PHE   B N   
3927 C CA  . PHE   B 272 ? 0.1435 0.1522 0.2375 -0.0055 -0.018  0.0085  253 PHE   B CA  
3928 C C   . PHE   B 272 ? 0.1345 0.1448 0.2249 -0.0056 -0.0131 0.0081  253 PHE   B C   
3929 O O   . PHE   B 272 ? 0.1421 0.1541 0.2289 -0.0043 -0.0088 0.0067  253 PHE   B O   
3930 C CB  . PHE   B 272 ? 0.1637 0.1649 0.2484 -0.0048 -0.0228 0.0066  253 PHE   B CB  
3931 C CG  . PHE   B 272 ? 0.1635 0.1629 0.2382 -0.0027 -0.0198 0.004   253 PHE   B CG  
3932 C CD1 . PHE   B 272 ? 0.1627 0.161  0.2325 -0.0022 -0.0181 0.0028  253 PHE   B CD1 
3933 C CD2 . PHE   B 272 ? 0.1747 0.1732 0.2451 -0.0014 -0.0193 0.0029  253 PHE   B CD2 
3934 C CE1 . PHE   B 272 ? 0.1702 0.1682 0.2325 -0.0003 -0.0155 0.0006  253 PHE   B CE1 
3935 C CE2 . PHE   B 272 ? 0.1672 0.1649 0.2293 -0.0001 -0.0165 0.0008  253 PHE   B CE2 
3936 C CZ  . PHE   B 272 ? 0.1603 0.1586 0.2192 0.0005  -0.0143 -0.0004 253 PHE   B CZ  
3937 N N   . SER   B 273 ? 0.1468 0.1557 0.2377 -0.0074 -0.0145 0.0094  254 SER   B N   
3938 C CA  . SER   B 273 ? 0.1548 0.1637 0.2411 -0.0077 -0.0116 0.0094  254 SER   B CA  
3939 C C   . SER   B 273 ? 0.1559 0.158  0.2375 -0.0077 -0.0164 0.0091  254 SER   B C   
3940 O O   . SER   B 273 ? 0.1589 0.1583 0.2444 -0.0097 -0.0207 0.0106  254 SER   B O   
3941 C CB  . SER   B 273 ? 0.2332 0.2473 0.3258 -0.0102 -0.0079 0.0123  254 SER   B CB  
3942 O OG  . SER   B 273 ? 0.3304 0.3436 0.4184 -0.0111 -0.0061 0.0132  254 SER   B OG  
3943 N N   . LEU   B 274 ? 0.154  0.1535 0.2283 -0.0058 -0.0158 0.0073  255 LEU   B N   
3944 C CA  . LEU   B 274 ? 0.1812 0.1739 0.2514 -0.0052 -0.02   0.0067  255 LEU   B CA  
3945 C C   . LEU   B 274 ? 0.1689 0.1612 0.2354 -0.0043 -0.0184 0.007   255 LEU   B C   
3946 O O   . LEU   B 274 ? 0.1564 0.1532 0.221  -0.0033 -0.0144 0.0063  255 LEU   B O   
3947 C CB  . LEU   B 274 ? 0.2211 0.2086 0.2858 -0.0027 -0.0232 0.0035  255 LEU   B CB  
3948 C CG  . LEU   B 274 ? 0.2105 0.2    0.2693 0.0003  -0.0201 0.0006  255 LEU   B CG  
3949 C CD1 . LEU   B 274 ? 0.2479 0.2346 0.302  0.003   -0.0204 -0.001  255 LEU   B CD1 
3950 C CD2 . LEU   B 274 ? 0.2412 0.2277 0.2952 0.0018  -0.022  -0.002  255 LEU   B CD2 
3951 N N   . VAL   B 275 ? 0.1689 0.1551 0.2344 -0.0048 -0.0222 0.008   256 VAL   B N   
3952 C CA  . VAL   B 275 ? 0.1761 0.16   0.2379 -0.0034 -0.0224 0.0084  256 VAL   B CA  
3953 C C   . VAL   B 275 ? 0.189  0.1648 0.2463 -0.0002 -0.027  0.0055  256 VAL   B C   
3954 O O   . VAL   B 275 ? 0.1928 0.162  0.2505 -0.0014 -0.0314 0.0057  256 VAL   B O   
3955 C CB  . VAL   B 275 ? 0.2112 0.1944 0.2754 -0.0072 -0.0227 0.0129  256 VAL   B CB  
3956 C CG1 . VAL   B 275 ? 0.2363 0.2162 0.2962 -0.0055 -0.0239 0.0137  256 VAL   B CG1 
3957 C CG2 . VAL   B 275 ? 0.2335 0.2249 0.3019 -0.0103 -0.0175 0.0153  256 VAL   B CG2 
3958 N N   . ALA   B 276 ? 0.1984 0.1747 0.2516 0.004   -0.0259 0.0028  257 ALA   B N   
3959 C CA  . ALA   B 276 ? 0.2005 0.1699 0.2495 0.0081  -0.0291 -0.0006 257 ALA   B CA  
3960 C C   . ALA   B 276 ? 0.2101 0.1793 0.2582 0.0111  -0.0293 -0.0004 257 ALA   B C   
3961 O O   . ALA   B 276 ? 0.2102 0.1856 0.2599 0.01    -0.0266 0.0019  257 ALA   B O   
3962 C CB  . ALA   B 276 ? 0.2276 0.1988 0.2732 0.0108  -0.0275 -0.0048 257 ALA   B CB  
3963 N N   . ARG   B 277 ? 0.215  0.1768 0.2604 0.0151  -0.0327 -0.0028 258 ARG   B N   
3964 C CA  . ARG   B 277 ? 0.2216 0.1832 0.2671 0.0189  -0.0335 -0.0029 258 ARG   B CA  
3965 C C   . ARG   B 277 ? 0.2129 0.1751 0.2562 0.025   -0.0324 -0.0083 258 ARG   B C   
3966 O O   . ARG   B 277 ? 0.2243 0.1808 0.2639 0.0267  -0.0336 -0.0119 258 ARG   B O   
3967 C CB  . ARG   B 277 ? 0.2853 0.236  0.3303 0.0188  -0.0392 -0.0007 258 ARG   B CB  
3968 C CG  . ARG   B 277 ? 0.3744 0.3253 0.4214 0.0129  -0.0397 0.0052  258 ARG   B CG  
3969 C CD  . ARG   B 277 ? 0.4382 0.3781 0.4842 0.0131  -0.0455 0.0078  258 ARG   B CD  
3970 N NE  . ARG   B 277 ? 0.4798 0.4211 0.5257 0.0158  -0.0462 0.0095  258 ARG   B NE  
3971 C CZ  . ARG   B 277 ? 0.5183 0.4516 0.5632 0.015   -0.0508 0.0135  258 ARG   B CZ  
3972 N NH1 . ARG   B 277 ? 0.4914 0.4144 0.5354 0.0113  -0.0548 0.016   258 ARG   B NH1 
3973 N NH2 . ARG   B 277 ? 0.521  0.4561 0.566  0.0176  -0.0518 0.0153  258 ARG   B NH2 
3974 N N   . LYS   B 278 ? 0.2167 0.1863 0.262  0.0282  -0.03   -0.0089 259 LYS   B N   
3975 C CA  . LYS   B 278 ? 0.2195 0.1918 0.2641 0.0341  -0.0281 -0.0138 259 LYS   B CA  
3976 C C   . LYS   B 278 ? 0.2695 0.2317 0.3129 0.0394  -0.0324 -0.0162 259 LYS   B C   
3977 O O   . LYS   B 278 ? 0.2934 0.2511 0.3388 0.0396  -0.0362 -0.0132 259 LYS   B O   
3978 C CB  . LYS   B 278 ? 0.223  0.2066 0.2719 0.0355  -0.025  -0.0131 259 LYS   B CB  
3979 C CG  . LYS   B 278 ? 0.2535 0.2432 0.3031 0.0407  -0.0216 -0.0178 259 LYS   B CG  
3980 C CD  . LYS   B 278 ? 0.2822 0.283  0.3379 0.0419  -0.02   -0.0164 259 LYS   B CD  
3981 C CE  . LYS   B 278 ? 0.3292 0.3375 0.3874 0.0472  -0.0164 -0.0207 259 LYS   B CE  
3982 N NZ  . LYS   B 278 ? 0.2458 0.2663 0.3109 0.0476  -0.015  -0.0191 259 LYS   B NZ  
3983 N N   . LEU   B 279 ? 0.2684 0.2267 0.3078 0.0435  -0.0317 -0.0216 260 LEU   B N   
3984 C CA  . LEU   B 279 ? 0.3325 0.281  0.3707 0.0497  -0.0354 -0.0247 260 LEU   B CA  
3985 C C   . LEU   B 279 ? 0.3917 0.3488 0.436  0.0554  -0.0335 -0.0254 260 LEU   B C   
3986 O O   . LEU   B 279 ? 0.4282 0.3979 0.4751 0.0562  -0.0281 -0.0268 260 LEU   B O   
3987 C CB  . LEU   B 279 ? 0.3445 0.2875 0.3761 0.0531  -0.0342 -0.0308 260 LEU   B CB  
3988 C CG  . LEU   B 279 ? 0.3866 0.3199 0.4119 0.0485  -0.0373 -0.0309 260 LEU   B CG  
3989 C CD1 . LEU   B 279 ? 0.4267 0.3575 0.4441 0.0512  -0.0349 -0.037  260 LEU   B CD1 
3990 C CD2 . LEU   B 279 ? 0.4016 0.3203 0.426  0.0482  -0.0444 -0.0296 260 LEU   B CD2 
3991 C C1  . A1IPO C .   ? 0.2513 0.2239 0.2736 0.0047  -0.0064 -0.0039 301 A1IPO A C1  
3992 C C3  . A1IPO C .   ? 0.1889 0.1708 0.2214 0.0047  -0.0107 -0.0013 301 A1IPO A C3  
3993 N N6  . A1IPO C .   ? 0.1839 0.1721 0.2167 0.0002  -0.0163 0.0007  301 A1IPO A N6  
3994 C C7  . A1IPO C .   ? 0.1809 0.1688 0.2183 0.0026  -0.0158 0.0021  301 A1IPO A C7  
3995 C C8  . A1IPO C .   ? 0.202  0.1919 0.2427 0.0015  -0.0193 0.0051  301 A1IPO A C8  
3996 C C9  . A1IPO C .   ? 0.1913 0.1767 0.2302 0.0051  -0.0124 0.0009  301 A1IPO A C9  
3997 C C10 . A1IPO C .   ? 0.2181 0.2035 0.2657 0.0079  -0.0103 0.0021  301 A1IPO A C10 
3998 O O2  . A1IPO C .   ? 0.2261 0.2036 0.257  0.0062  -0.0066 -0.0025 301 A1IPO A O2  
3999 C C4  . A1IPO C .   ? 0.1815 0.1637 0.2101 0.0024  -0.0131 -0.002  301 A1IPO A C4  
4000 C C5  . A1IPO C .   ? 0.1815 0.1674 0.2118 0.0005  -0.0152 -0.0011 301 A1IPO A C5  
4027 C C1  . A1IPO E .   ? 0.2055 0.1994 0.2664 0.0012  -0.0032 0.0019  301 A1IPO B C1  
4028 C C3  . A1IPO E .   ? 0.1763 0.1737 0.2424 0.0019  0.004   -0.0007 301 A1IPO B C3  
4029 N N6  . A1IPO E .   ? 0.1669 0.1675 0.2287 0.0002  0.0122  -0.0046 301 A1IPO B N6  
4030 C C7  . A1IPO E .   ? 0.1741 0.1743 0.2434 0.0026  0.0115  -0.0039 301 A1IPO B C7  
4031 C C8  . A1IPO E .   ? 0.1906 0.1923 0.2646 0.0043  0.0157  -0.0056 301 A1IPO B C8  
4032 C C9  . A1IPO E .   ? 0.1789 0.1778 0.2513 0.0035  0.0071  -0.0018 301 A1IPO B C9  
4033 C C10 . A1IPO E .   ? 0.2025 0.2017 0.2847 0.0064  0.0057  -0.0008 301 A1IPO B C10 
4034 O O2  . A1IPO E .   ? 0.1932 0.1887 0.2613 0.0027  -0.0006 0.0012  301 A1IPO B O2  
4035 C C4  . A1IPO E .   ? 0.1707 0.169  0.2295 -0.0003 0.0055  -0.0017 301 A1IPO B C4  
4036 C C5  . A1IPO E .   ? 0.1711 0.1712 0.2287 -0.0011 0.0094  -0.0035 301 A1IPO B C5  
# 
