data_9E3T
# 
_entry.id   9E3T 
# 
_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   9E3T         pdb_00009e3t 10.2210/pdb9e3t/pdb 
WWPDB D_1000289396 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-14 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9E3T 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tumer@sebs.rutgers.edu 
_pdbx_contact_author.name_first         Nilgun 
_pdbx_contact_author.name_last          Tumer 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1693-2940 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Rudolph, M.J.' 1 0000-0002-5893-9817 
'Tumer, N.'     2 0000-0002-1693-2940 
# 
_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                108310 
_citation.page_last                 108310 
_citation.title                     
'Binding of small molecules at the P-stalk site of ricin A subunit trigger conformational changes that extend into the active site.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2025.108310 
_citation.pdbx_database_id_PubMed   39955060 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'McLaughlin, J.E.' 1  ? 
primary 'Rudolph, M.J.'    2  ? 
primary 'Dutta, A.'        3  ? 
primary 'Li, X.P.'         4  ? 
primary 'Tsymbal, A.M.'    5  ? 
primary 'Chen, Y.'         6  ? 
primary 'Bhattacharya, S.' 7  ? 
primary 'Algava, B.'       8  ? 
primary 'Goger, M.'        9  ? 
primary 'Roberge, J.Y.'    10 ? 
primary 'Tumer, N.E.'      11 ? 
# 
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 'Ricin A chain'                                              30340.205 2   3.2.2.22 ? 'residues 40-294' 
'Ricin toxin catalytic subunit, N-linked glycosidase' 
2 non-polymer syn '(5M)-5-(2-ethyl-6-methylphenyl)thiophene-2-carboxylic acid' 246.325   2   ?        ? ?                 ? 
3 non-polymer syn 'CHLORIDE ION'                                               35.453    1   ?        ? ?                 ? 
4 water       nat water                                                        18.015    541 ?        ? ?                 ? 
# 
_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       
;SNAMIFPKQYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVRHEIPVLPNRVGLPINQRFILVELSNHAELSVTLALDV
TNAYVVGYRAGNSAYFFHPDNQEDAEAITHLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEEAISALYYYST
GGTQLPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRN
GSKFSVYDVSILIPIIALMVYRCAPPPSSQF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SNAMIFPKQYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVRHEIPVLPNRVGLPINQRFILVELSNHAELSVTLALDV
TNAYVVGYRAGNSAYFFHPDNQEDAEAITHLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEEAISALYYYST
GGTQLPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRN
GSKFSVYDVSILIPIIALMVYRCAPPPSSQF
;
_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 '(5M)-5-(2-ethyl-6-methylphenyl)thiophene-2-carboxylic acid' A1BH4 
3 'CHLORIDE ION'                                               CL    
4 water                                                        HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ASN n 
1 3   ALA n 
1 4   MET n 
1 5   ILE n 
1 6   PHE n 
1 7   PRO n 
1 8   LYS n 
1 9   GLN n 
1 10  TYR n 
1 11  PRO n 
1 12  ILE n 
1 13  ILE n 
1 14  ASN n 
1 15  PHE n 
1 16  THR n 
1 17  THR n 
1 18  ALA n 
1 19  GLY n 
1 20  ALA n 
1 21  THR n 
1 22  VAL n 
1 23  GLN n 
1 24  SER n 
1 25  TYR n 
1 26  THR n 
1 27  ASN n 
1 28  PHE n 
1 29  ILE n 
1 30  ARG n 
1 31  ALA n 
1 32  VAL n 
1 33  ARG n 
1 34  GLY n 
1 35  ARG n 
1 36  LEU n 
1 37  THR n 
1 38  THR n 
1 39  GLY n 
1 40  ALA n 
1 41  ASP n 
1 42  VAL n 
1 43  ARG n 
1 44  HIS n 
1 45  GLU n 
1 46  ILE n 
1 47  PRO n 
1 48  VAL n 
1 49  LEU n 
1 50  PRO n 
1 51  ASN n 
1 52  ARG n 
1 53  VAL n 
1 54  GLY n 
1 55  LEU n 
1 56  PRO n 
1 57  ILE n 
1 58  ASN n 
1 59  GLN n 
1 60  ARG n 
1 61  PHE n 
1 62  ILE n 
1 63  LEU n 
1 64  VAL n 
1 65  GLU n 
1 66  LEU n 
1 67  SER n 
1 68  ASN n 
1 69  HIS n 
1 70  ALA n 
1 71  GLU n 
1 72  LEU n 
1 73  SER n 
1 74  VAL n 
1 75  THR n 
1 76  LEU n 
1 77  ALA n 
1 78  LEU n 
1 79  ASP n 
1 80  VAL n 
1 81  THR n 
1 82  ASN n 
1 83  ALA n 
1 84  TYR n 
1 85  VAL n 
1 86  VAL n 
1 87  GLY n 
1 88  TYR n 
1 89  ARG n 
1 90  ALA n 
1 91  GLY n 
1 92  ASN n 
1 93  SER n 
1 94  ALA n 
1 95  TYR n 
1 96  PHE n 
1 97  PHE n 
1 98  HIS n 
1 99  PRO n 
1 100 ASP n 
1 101 ASN n 
1 102 GLN n 
1 103 GLU n 
1 104 ASP n 
1 105 ALA n 
1 106 GLU n 
1 107 ALA n 
1 108 ILE n 
1 109 THR n 
1 110 HIS n 
1 111 LEU n 
1 112 PHE n 
1 113 THR n 
1 114 ASP n 
1 115 VAL n 
1 116 GLN n 
1 117 ASN n 
1 118 ARG n 
1 119 TYR n 
1 120 THR n 
1 121 PHE n 
1 122 ALA n 
1 123 PHE n 
1 124 GLY n 
1 125 GLY n 
1 126 ASN n 
1 127 TYR n 
1 128 ASP n 
1 129 ARG n 
1 130 LEU n 
1 131 GLU n 
1 132 GLN n 
1 133 LEU n 
1 134 ALA n 
1 135 GLY n 
1 136 ASN n 
1 137 LEU n 
1 138 ARG n 
1 139 GLU n 
1 140 ASN n 
1 141 ILE n 
1 142 GLU n 
1 143 LEU n 
1 144 GLY n 
1 145 ASN n 
1 146 GLY n 
1 147 PRO n 
1 148 LEU n 
1 149 GLU n 
1 150 GLU n 
1 151 ALA n 
1 152 ILE n 
1 153 SER n 
1 154 ALA n 
1 155 LEU n 
1 156 TYR n 
1 157 TYR n 
1 158 TYR n 
1 159 SER n 
1 160 THR n 
1 161 GLY n 
1 162 GLY n 
1 163 THR n 
1 164 GLN n 
1 165 LEU n 
1 166 PRO n 
1 167 THR n 
1 168 LEU n 
1 169 ALA n 
1 170 ARG n 
1 171 SER n 
1 172 PHE n 
1 173 ILE n 
1 174 ILE n 
1 175 CYS n 
1 176 ILE n 
1 177 GLN n 
1 178 MET n 
1 179 ILE n 
1 180 SER n 
1 181 GLU n 
1 182 ALA n 
1 183 ALA n 
1 184 ARG n 
1 185 PHE n 
1 186 GLN n 
1 187 TYR n 
1 188 ILE n 
1 189 GLU n 
1 190 GLY n 
1 191 GLU n 
1 192 MET n 
1 193 ARG n 
1 194 THR n 
1 195 ARG n 
1 196 ILE n 
1 197 ARG n 
1 198 TYR n 
1 199 ASN n 
1 200 ARG n 
1 201 ARG n 
1 202 SER n 
1 203 ALA n 
1 204 PRO n 
1 205 ASP n 
1 206 PRO n 
1 207 SER n 
1 208 VAL n 
1 209 ILE n 
1 210 THR n 
1 211 LEU n 
1 212 GLU n 
1 213 ASN n 
1 214 SER n 
1 215 TRP n 
1 216 GLY n 
1 217 ARG n 
1 218 LEU n 
1 219 SER n 
1 220 THR n 
1 221 ALA n 
1 222 ILE n 
1 223 GLN n 
1 224 GLU n 
1 225 SER n 
1 226 ASN n 
1 227 GLN n 
1 228 GLY n 
1 229 ALA n 
1 230 PHE n 
1 231 ALA n 
1 232 SER n 
1 233 PRO n 
1 234 ILE n 
1 235 GLN n 
1 236 LEU n 
1 237 GLN n 
1 238 ARG n 
1 239 ARG n 
1 240 ASN n 
1 241 GLY n 
1 242 SER n 
1 243 LYS n 
1 244 PHE n 
1 245 SER n 
1 246 VAL n 
1 247 TYR n 
1 248 ASP n 
1 249 VAL n 
1 250 SER n 
1 251 ILE n 
1 252 LEU n 
1 253 ILE n 
1 254 PRO n 
1 255 ILE n 
1 256 ILE n 
1 257 ALA n 
1 258 LEU n 
1 259 MET n 
1 260 VAL n 
1 261 TYR n 
1 262 ARG n 
1 263 CYS n 
1 264 ALA n 
1 265 PRO n 
1 266 PRO n 
1 267 PRO n 
1 268 SER n 
1 269 SER n 
1 270 GLN n 
1 271 PHE 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                   271 
_entity_src_gen.gene_src_common_name               'castor bean' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Ricinus communis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3988 
_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 B' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     37762 
_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 
A1BH4 non-polymer         . '(5M)-5-(2-ethyl-6-methylphenyl)thiophene-2-carboxylic acid' ? 'C14 H14 O2 S'   246.325 
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 
CL    non-polymer         . 'CHLORIDE ION'                                               ? 'Cl -1'          35.453  
CYS   'L-peptide linking' y CYSTEINE                                                     ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                    ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                              ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                      ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                    ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                        ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                   ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                      ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                       ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                   ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                      ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                       ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                    ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                   ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                     ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                       ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   -3  ?   ?   ?   A . n 
A 1 2   ASN 2   -2  ?   ?   ?   A . n 
A 1 3   ALA 3   -1  ?   ?   ?   A . n 
A 1 4   MET 4   0   ?   ?   ?   A . n 
A 1 5   ILE 5   1   ?   ?   ?   A . n 
A 1 6   PHE 6   2   ?   ?   ?   A . n 
A 1 7   PRO 7   3   3   PRO PRO A . n 
A 1 8   LYS 8   4   4   LYS LYS A . n 
A 1 9   GLN 9   5   5   GLN GLN A . n 
A 1 10  TYR 10  6   6   TYR TYR A . n 
A 1 11  PRO 11  7   7   PRO PRO A . n 
A 1 12  ILE 12  8   8   ILE ILE A . n 
A 1 13  ILE 13  9   9   ILE ILE A . n 
A 1 14  ASN 14  10  10  ASN ASN A . n 
A 1 15  PHE 15  11  11  PHE PHE A . n 
A 1 16  THR 16  12  12  THR THR A . n 
A 1 17  THR 17  13  13  THR THR A . n 
A 1 18  ALA 18  14  14  ALA ALA A . n 
A 1 19  GLY 19  15  15  GLY GLY A . n 
A 1 20  ALA 20  16  16  ALA ALA A . n 
A 1 21  THR 21  17  17  THR THR A . n 
A 1 22  VAL 22  18  18  VAL VAL A . n 
A 1 23  GLN 23  19  19  GLN GLN A . n 
A 1 24  SER 24  20  20  SER SER A . n 
A 1 25  TYR 25  21  21  TYR TYR A . n 
A 1 26  THR 26  22  22  THR THR A . n 
A 1 27  ASN 27  23  23  ASN ASN A . n 
A 1 28  PHE 28  24  24  PHE PHE A . n 
A 1 29  ILE 29  25  25  ILE ILE A . n 
A 1 30  ARG 30  26  26  ARG ARG A . n 
A 1 31  ALA 31  27  27  ALA ALA A . n 
A 1 32  VAL 32  28  28  VAL VAL A . n 
A 1 33  ARG 33  29  29  ARG ARG A . n 
A 1 34  GLY 34  30  30  GLY GLY A . n 
A 1 35  ARG 35  31  31  ARG ARG A . n 
A 1 36  LEU 36  32  32  LEU LEU A . n 
A 1 37  THR 37  33  33  THR THR A . n 
A 1 38  THR 38  34  34  THR THR A . n 
A 1 39  GLY 39  35  35  GLY GLY A . n 
A 1 40  ALA 40  36  36  ALA ALA A . n 
A 1 41  ASP 41  37  37  ASP ASP A . n 
A 1 42  VAL 42  38  38  VAL VAL A . n 
A 1 43  ARG 43  39  39  ARG ARG A . n 
A 1 44  HIS 44  40  40  HIS HIS A . n 
A 1 45  GLU 45  41  41  GLU GLU A . n 
A 1 46  ILE 46  42  42  ILE ILE A . n 
A 1 47  PRO 47  43  43  PRO PRO A . n 
A 1 48  VAL 48  44  44  VAL VAL A . n 
A 1 49  LEU 49  45  45  LEU LEU A . n 
A 1 50  PRO 50  46  46  PRO PRO A . n 
A 1 51  ASN 51  47  47  ASN ASN A . n 
A 1 52  ARG 52  48  48  ARG ARG A . n 
A 1 53  VAL 53  49  49  VAL VAL A . n 
A 1 54  GLY 54  50  50  GLY GLY A . n 
A 1 55  LEU 55  51  51  LEU LEU A . n 
A 1 56  PRO 56  52  52  PRO PRO A . n 
A 1 57  ILE 57  53  53  ILE ILE A . n 
A 1 58  ASN 58  54  54  ASN ASN A . n 
A 1 59  GLN 59  55  55  GLN GLN A . n 
A 1 60  ARG 60  56  56  ARG ARG A . n 
A 1 61  PHE 61  57  57  PHE PHE A . n 
A 1 62  ILE 62  58  58  ILE ILE A . n 
A 1 63  LEU 63  59  59  LEU LEU A . n 
A 1 64  VAL 64  60  60  VAL VAL A . n 
A 1 65  GLU 65  61  61  GLU GLU A . n 
A 1 66  LEU 66  62  62  LEU LEU A . n 
A 1 67  SER 67  63  63  SER SER A . n 
A 1 68  ASN 68  64  64  ASN ASN A . n 
A 1 69  HIS 69  65  65  HIS HIS A . n 
A 1 70  ALA 70  66  66  ALA ALA A . n 
A 1 71  GLU 71  67  67  GLU GLU A . n 
A 1 72  LEU 72  68  68  LEU LEU A . n 
A 1 73  SER 73  69  69  SER SER A . n 
A 1 74  VAL 74  70  70  VAL VAL A . n 
A 1 75  THR 75  71  71  THR THR A . n 
A 1 76  LEU 76  72  72  LEU LEU A . n 
A 1 77  ALA 77  73  73  ALA ALA A . n 
A 1 78  LEU 78  74  74  LEU LEU A . n 
A 1 79  ASP 79  75  75  ASP ASP A . n 
A 1 80  VAL 80  76  76  VAL VAL A . n 
A 1 81  THR 81  77  77  THR THR A . n 
A 1 82  ASN 82  78  78  ASN ASN A . n 
A 1 83  ALA 83  79  79  ALA ALA A . n 
A 1 84  TYR 84  80  80  TYR TYR A . n 
A 1 85  VAL 85  81  81  VAL VAL A . n 
A 1 86  VAL 86  82  82  VAL VAL A . n 
A 1 87  GLY 87  83  83  GLY GLY A . n 
A 1 88  TYR 88  84  84  TYR TYR A . n 
A 1 89  ARG 89  85  85  ARG ARG A . n 
A 1 90  ALA 90  86  86  ALA ALA A . n 
A 1 91  GLY 91  87  87  GLY GLY A . n 
A 1 92  ASN 92  88  88  ASN ASN A . n 
A 1 93  SER 93  89  89  SER SER A . n 
A 1 94  ALA 94  90  90  ALA ALA A . n 
A 1 95  TYR 95  91  91  TYR TYR A . n 
A 1 96  PHE 96  92  92  PHE PHE A . n 
A 1 97  PHE 97  93  93  PHE PHE A . n 
A 1 98  HIS 98  94  94  HIS HIS A . n 
A 1 99  PRO 99  95  95  PRO PRO A . n 
A 1 100 ASP 100 96  96  ASP ASP A . n 
A 1 101 ASN 101 97  97  ASN ASN A . n 
A 1 102 GLN 102 98  98  GLN GLN A . n 
A 1 103 GLU 103 99  99  GLU GLU A . n 
A 1 104 ASP 104 100 100 ASP ASP A . n 
A 1 105 ALA 105 101 101 ALA ALA A . n 
A 1 106 GLU 106 102 102 GLU GLU A . n 
A 1 107 ALA 107 103 103 ALA ALA A . n 
A 1 108 ILE 108 104 104 ILE ILE A . n 
A 1 109 THR 109 105 105 THR THR A . n 
A 1 110 HIS 110 106 106 HIS HIS A . n 
A 1 111 LEU 111 107 107 LEU LEU A . n 
A 1 112 PHE 112 108 108 PHE PHE A . n 
A 1 113 THR 113 109 109 THR THR A . n 
A 1 114 ASP 114 110 110 ASP ASP A . n 
A 1 115 VAL 115 111 111 VAL VAL A . n 
A 1 116 GLN 116 112 112 GLN GLN A . n 
A 1 117 ASN 117 113 113 ASN ASN A . n 
A 1 118 ARG 118 114 114 ARG ARG A . n 
A 1 119 TYR 119 115 115 TYR TYR A . n 
A 1 120 THR 120 116 116 THR THR A . n 
A 1 121 PHE 121 117 117 PHE PHE A . n 
A 1 122 ALA 122 118 118 ALA ALA A . n 
A 1 123 PHE 123 119 119 PHE PHE A . n 
A 1 124 GLY 124 120 120 GLY GLY A . n 
A 1 125 GLY 125 121 121 GLY GLY A . n 
A 1 126 ASN 126 122 122 ASN ASN A . n 
A 1 127 TYR 127 123 123 TYR TYR A . n 
A 1 128 ASP 128 124 124 ASP ASP A . n 
A 1 129 ARG 129 125 125 ARG ARG A . n 
A 1 130 LEU 130 126 126 LEU LEU A . n 
A 1 131 GLU 131 127 127 GLU GLU A . n 
A 1 132 GLN 132 128 128 GLN GLN A . n 
A 1 133 LEU 133 129 129 LEU LEU A . n 
A 1 134 ALA 134 130 130 ALA ALA A . n 
A 1 135 GLY 135 131 131 GLY GLY A . n 
A 1 136 ASN 136 132 132 ASN ASN A . n 
A 1 137 LEU 137 133 133 LEU LEU A . n 
A 1 138 ARG 138 134 134 ARG ARG A . n 
A 1 139 GLU 139 135 135 GLU GLU A . n 
A 1 140 ASN 140 136 136 ASN ASN A . n 
A 1 141 ILE 141 137 137 ILE ILE A . n 
A 1 142 GLU 142 138 138 GLU GLU A . n 
A 1 143 LEU 143 139 139 LEU LEU A . n 
A 1 144 GLY 144 140 140 GLY GLY A . n 
A 1 145 ASN 145 141 141 ASN ASN A . n 
A 1 146 GLY 146 142 142 GLY GLY A . n 
A 1 147 PRO 147 143 143 PRO PRO A . n 
A 1 148 LEU 148 144 144 LEU LEU A . n 
A 1 149 GLU 149 145 145 GLU GLU A . n 
A 1 150 GLU 150 146 146 GLU GLU A . n 
A 1 151 ALA 151 147 147 ALA ALA A . n 
A 1 152 ILE 152 148 148 ILE ILE A . n 
A 1 153 SER 153 149 149 SER SER A . n 
A 1 154 ALA 154 150 150 ALA ALA A . n 
A 1 155 LEU 155 151 151 LEU LEU A . n 
A 1 156 TYR 156 152 152 TYR TYR A . n 
A 1 157 TYR 157 153 153 TYR TYR A . n 
A 1 158 TYR 158 154 154 TYR TYR A . n 
A 1 159 SER 159 155 155 SER SER A . n 
A 1 160 THR 160 156 156 THR THR A . n 
A 1 161 GLY 161 157 157 GLY GLY A . n 
A 1 162 GLY 162 158 158 GLY GLY A . n 
A 1 163 THR 163 159 159 THR THR A . n 
A 1 164 GLN 164 160 160 GLN GLN A . n 
A 1 165 LEU 165 161 161 LEU LEU A . n 
A 1 166 PRO 166 162 162 PRO PRO A . n 
A 1 167 THR 167 163 163 THR THR A . n 
A 1 168 LEU 168 164 164 LEU LEU A . n 
A 1 169 ALA 169 165 165 ALA ALA A . n 
A 1 170 ARG 170 166 166 ARG ARG A . n 
A 1 171 SER 171 167 167 SER SER A . n 
A 1 172 PHE 172 168 168 PHE PHE A . n 
A 1 173 ILE 173 169 169 ILE ILE A . n 
A 1 174 ILE 174 170 170 ILE ILE A . n 
A 1 175 CYS 175 171 171 CYS CYS A . n 
A 1 176 ILE 176 172 172 ILE ILE A . n 
A 1 177 GLN 177 173 173 GLN GLN A . n 
A 1 178 MET 178 174 174 MET MET A . n 
A 1 179 ILE 179 175 175 ILE ILE A . n 
A 1 180 SER 180 176 176 SER SER A . n 
A 1 181 GLU 181 177 177 GLU GLU A . n 
A 1 182 ALA 182 178 178 ALA ALA A . n 
A 1 183 ALA 183 179 179 ALA ALA A . n 
A 1 184 ARG 184 180 180 ARG ARG A . n 
A 1 185 PHE 185 181 181 PHE PHE A . n 
A 1 186 GLN 186 182 182 GLN GLN A . n 
A 1 187 TYR 187 183 183 TYR TYR A . n 
A 1 188 ILE 188 184 184 ILE ILE A . n 
A 1 189 GLU 189 185 185 GLU GLU A . n 
A 1 190 GLY 190 186 186 GLY GLY A . n 
A 1 191 GLU 191 187 187 GLU GLU A . n 
A 1 192 MET 192 188 188 MET MET A . n 
A 1 193 ARG 193 189 189 ARG ARG A . n 
A 1 194 THR 194 190 190 THR THR A . n 
A 1 195 ARG 195 191 191 ARG ARG A . n 
A 1 196 ILE 196 192 192 ILE ILE A . n 
A 1 197 ARG 197 193 193 ARG ARG A . n 
A 1 198 TYR 198 194 194 TYR TYR A . n 
A 1 199 ASN 199 195 195 ASN ASN A . n 
A 1 200 ARG 200 196 196 ARG ARG A . n 
A 1 201 ARG 201 197 197 ARG ARG A . n 
A 1 202 SER 202 198 198 SER SER A . n 
A 1 203 ALA 203 199 199 ALA ALA A . n 
A 1 204 PRO 204 200 200 PRO PRO A . n 
A 1 205 ASP 205 201 201 ASP ASP A . n 
A 1 206 PRO 206 202 202 PRO PRO A . n 
A 1 207 SER 207 203 203 SER SER A . n 
A 1 208 VAL 208 204 204 VAL VAL A . n 
A 1 209 ILE 209 205 205 ILE ILE A . n 
A 1 210 THR 210 206 206 THR THR A . n 
A 1 211 LEU 211 207 207 LEU LEU A . n 
A 1 212 GLU 212 208 208 GLU GLU A . n 
A 1 213 ASN 213 209 209 ASN ASN A . n 
A 1 214 SER 214 210 210 SER SER A . n 
A 1 215 TRP 215 211 211 TRP TRP A . n 
A 1 216 GLY 216 212 212 GLY GLY A . n 
A 1 217 ARG 217 213 213 ARG ARG A . n 
A 1 218 LEU 218 214 214 LEU LEU A . n 
A 1 219 SER 219 215 215 SER SER A . n 
A 1 220 THR 220 216 216 THR THR A . n 
A 1 221 ALA 221 217 217 ALA ALA A . n 
A 1 222 ILE 222 218 218 ILE ILE A . n 
A 1 223 GLN 223 219 219 GLN GLN A . n 
A 1 224 GLU 224 220 220 GLU GLU A . n 
A 1 225 SER 225 221 221 SER SER A . n 
A 1 226 ASN 226 222 222 ASN ASN A . n 
A 1 227 GLN 227 223 223 GLN GLN A . n 
A 1 228 GLY 228 224 224 GLY GLY A . n 
A 1 229 ALA 229 225 225 ALA ALA A . n 
A 1 230 PHE 230 226 226 PHE PHE A . n 
A 1 231 ALA 231 227 227 ALA ALA A . n 
A 1 232 SER 232 228 228 SER SER A . n 
A 1 233 PRO 233 229 229 PRO PRO A . n 
A 1 234 ILE 234 230 230 ILE ILE A . n 
A 1 235 GLN 235 231 231 GLN GLN A . n 
A 1 236 LEU 236 232 232 LEU LEU A . n 
A 1 237 GLN 237 233 233 GLN GLN A . n 
A 1 238 ARG 238 234 234 ARG ARG A . n 
A 1 239 ARG 239 235 235 ARG ARG A . n 
A 1 240 ASN 240 236 236 ASN ASN A . n 
A 1 241 GLY 241 237 237 GLY GLY A . n 
A 1 242 SER 242 238 238 SER SER A . n 
A 1 243 LYS 243 239 239 LYS LYS A . n 
A 1 244 PHE 244 240 240 PHE PHE A . n 
A 1 245 SER 245 241 241 SER SER A . n 
A 1 246 VAL 246 242 242 VAL VAL A . n 
A 1 247 TYR 247 243 243 TYR TYR A . n 
A 1 248 ASP 248 244 244 ASP ASP A . n 
A 1 249 VAL 249 245 245 VAL VAL A . n 
A 1 250 SER 250 246 246 SER SER A . n 
A 1 251 ILE 251 247 247 ILE ILE A . n 
A 1 252 LEU 252 248 248 LEU LEU A . n 
A 1 253 ILE 253 249 249 ILE ILE A . n 
A 1 254 PRO 254 250 250 PRO PRO A . n 
A 1 255 ILE 255 251 251 ILE ILE A . n 
A 1 256 ILE 256 252 252 ILE ILE A . n 
A 1 257 ALA 257 253 253 ALA ALA A . n 
A 1 258 LEU 258 254 254 LEU LEU A . n 
A 1 259 MET 259 255 255 MET MET A . n 
A 1 260 VAL 260 256 256 VAL VAL A . n 
A 1 261 TYR 261 257 257 TYR TYR A . n 
A 1 262 ARG 262 258 258 ARG ARG A . n 
A 1 263 CYS 263 259 259 CYS CYS A . n 
A 1 264 ALA 264 260 260 ALA ALA A . n 
A 1 265 PRO 265 261 261 PRO PRO A . n 
A 1 266 PRO 266 262 ?   ?   ?   A . n 
A 1 267 PRO 267 263 ?   ?   ?   A . n 
A 1 268 SER 268 264 ?   ?   ?   A . n 
A 1 269 SER 269 265 ?   ?   ?   A . n 
A 1 270 GLN 270 266 ?   ?   ?   A . n 
A 1 271 PHE 271 267 ?   ?   ?   A . n 
B 1 1   SER 1   -3  ?   ?   ?   B . n 
B 1 2   ASN 2   -2  ?   ?   ?   B . n 
B 1 3   ALA 3   -1  ?   ?   ?   B . n 
B 1 4   MET 4   0   ?   ?   ?   B . n 
B 1 5   ILE 5   1   ?   ?   ?   B . n 
B 1 6   PHE 6   2   ?   ?   ?   B . n 
B 1 7   PRO 7   3   ?   ?   ?   B . n 
B 1 8   LYS 8   4   4   LYS LYS B . n 
B 1 9   GLN 9   5   5   GLN GLN B . n 
B 1 10  TYR 10  6   6   TYR TYR B . n 
B 1 11  PRO 11  7   7   PRO PRO B . n 
B 1 12  ILE 12  8   8   ILE ILE B . n 
B 1 13  ILE 13  9   9   ILE ILE B . n 
B 1 14  ASN 14  10  10  ASN ASN B . n 
B 1 15  PHE 15  11  11  PHE PHE B . n 
B 1 16  THR 16  12  12  THR THR B . n 
B 1 17  THR 17  13  13  THR THR B . n 
B 1 18  ALA 18  14  14  ALA ALA B . n 
B 1 19  GLY 19  15  15  GLY GLY B . n 
B 1 20  ALA 20  16  16  ALA ALA B . n 
B 1 21  THR 21  17  17  THR THR B . n 
B 1 22  VAL 22  18  18  VAL VAL B . n 
B 1 23  GLN 23  19  19  GLN GLN B . n 
B 1 24  SER 24  20  20  SER SER B . n 
B 1 25  TYR 25  21  21  TYR TYR B . n 
B 1 26  THR 26  22  22  THR THR B . n 
B 1 27  ASN 27  23  23  ASN ASN B . n 
B 1 28  PHE 28  24  24  PHE PHE B . n 
B 1 29  ILE 29  25  25  ILE ILE B . n 
B 1 30  ARG 30  26  26  ARG ARG B . n 
B 1 31  ALA 31  27  27  ALA ALA B . n 
B 1 32  VAL 32  28  28  VAL VAL B . n 
B 1 33  ARG 33  29  29  ARG ARG B . n 
B 1 34  GLY 34  30  30  GLY GLY B . n 
B 1 35  ARG 35  31  31  ARG ARG B . n 
B 1 36  LEU 36  32  32  LEU LEU B . n 
B 1 37  THR 37  33  33  THR THR B . n 
B 1 38  THR 38  34  34  THR THR B . n 
B 1 39  GLY 39  35  35  GLY GLY B . n 
B 1 40  ALA 40  36  36  ALA ALA B . n 
B 1 41  ASP 41  37  37  ASP ASP B . n 
B 1 42  VAL 42  38  38  VAL VAL B . n 
B 1 43  ARG 43  39  39  ARG ARG B . n 
B 1 44  HIS 44  40  40  HIS HIS B . n 
B 1 45  GLU 45  41  41  GLU GLU B . n 
B 1 46  ILE 46  42  42  ILE ILE B . n 
B 1 47  PRO 47  43  43  PRO PRO B . n 
B 1 48  VAL 48  44  44  VAL VAL B . n 
B 1 49  LEU 49  45  45  LEU LEU B . n 
B 1 50  PRO 50  46  46  PRO PRO B . n 
B 1 51  ASN 51  47  47  ASN ASN B . n 
B 1 52  ARG 52  48  48  ARG ARG B . n 
B 1 53  VAL 53  49  49  VAL VAL B . n 
B 1 54  GLY 54  50  50  GLY GLY B . n 
B 1 55  LEU 55  51  51  LEU LEU B . n 
B 1 56  PRO 56  52  52  PRO PRO B . n 
B 1 57  ILE 57  53  53  ILE ILE B . n 
B 1 58  ASN 58  54  54  ASN ASN B . n 
B 1 59  GLN 59  55  55  GLN GLN B . n 
B 1 60  ARG 60  56  56  ARG ARG B . n 
B 1 61  PHE 61  57  57  PHE PHE B . n 
B 1 62  ILE 62  58  58  ILE ILE B . n 
B 1 63  LEU 63  59  59  LEU LEU B . n 
B 1 64  VAL 64  60  60  VAL VAL B . n 
B 1 65  GLU 65  61  61  GLU GLU B . n 
B 1 66  LEU 66  62  62  LEU LEU B . n 
B 1 67  SER 67  63  63  SER SER B . n 
B 1 68  ASN 68  64  64  ASN ASN B . n 
B 1 69  HIS 69  65  65  HIS HIS B . n 
B 1 70  ALA 70  66  66  ALA ALA B . n 
B 1 71  GLU 71  67  67  GLU GLU B . n 
B 1 72  LEU 72  68  68  LEU LEU B . n 
B 1 73  SER 73  69  69  SER SER B . n 
B 1 74  VAL 74  70  70  VAL VAL B . n 
B 1 75  THR 75  71  71  THR THR B . n 
B 1 76  LEU 76  72  72  LEU LEU B . n 
B 1 77  ALA 77  73  73  ALA ALA B . n 
B 1 78  LEU 78  74  74  LEU LEU B . n 
B 1 79  ASP 79  75  75  ASP ASP B . n 
B 1 80  VAL 80  76  76  VAL VAL B . n 
B 1 81  THR 81  77  77  THR THR B . n 
B 1 82  ASN 82  78  78  ASN ASN B . n 
B 1 83  ALA 83  79  79  ALA ALA B . n 
B 1 84  TYR 84  80  80  TYR TYR B . n 
B 1 85  VAL 85  81  81  VAL VAL B . n 
B 1 86  VAL 86  82  82  VAL VAL B . n 
B 1 87  GLY 87  83  83  GLY GLY B . n 
B 1 88  TYR 88  84  84  TYR TYR B . n 
B 1 89  ARG 89  85  85  ARG ARG B . n 
B 1 90  ALA 90  86  86  ALA ALA B . n 
B 1 91  GLY 91  87  87  GLY GLY B . n 
B 1 92  ASN 92  88  88  ASN ASN B . n 
B 1 93  SER 93  89  89  SER SER B . n 
B 1 94  ALA 94  90  90  ALA ALA B . n 
B 1 95  TYR 95  91  91  TYR TYR B . n 
B 1 96  PHE 96  92  92  PHE PHE B . n 
B 1 97  PHE 97  93  93  PHE PHE B . n 
B 1 98  HIS 98  94  94  HIS HIS B . n 
B 1 99  PRO 99  95  95  PRO PRO B . n 
B 1 100 ASP 100 96  96  ASP ASP B . n 
B 1 101 ASN 101 97  97  ASN ASN B . n 
B 1 102 GLN 102 98  98  GLN GLN B . n 
B 1 103 GLU 103 99  99  GLU GLU B . n 
B 1 104 ASP 104 100 100 ASP ASP B . n 
B 1 105 ALA 105 101 101 ALA ALA B . n 
B 1 106 GLU 106 102 102 GLU GLU B . n 
B 1 107 ALA 107 103 103 ALA ALA B . n 
B 1 108 ILE 108 104 104 ILE ILE B . n 
B 1 109 THR 109 105 105 THR THR B . n 
B 1 110 HIS 110 106 106 HIS HIS B . n 
B 1 111 LEU 111 107 107 LEU LEU B . n 
B 1 112 PHE 112 108 108 PHE PHE B . n 
B 1 113 THR 113 109 109 THR THR B . n 
B 1 114 ASP 114 110 110 ASP ASP B . n 
B 1 115 VAL 115 111 111 VAL VAL B . n 
B 1 116 GLN 116 112 112 GLN GLN B . n 
B 1 117 ASN 117 113 113 ASN ASN B . n 
B 1 118 ARG 118 114 114 ARG ARG B . n 
B 1 119 TYR 119 115 115 TYR TYR B . n 
B 1 120 THR 120 116 116 THR THR B . n 
B 1 121 PHE 121 117 117 PHE PHE B . n 
B 1 122 ALA 122 118 118 ALA ALA B . n 
B 1 123 PHE 123 119 119 PHE PHE B . n 
B 1 124 GLY 124 120 120 GLY GLY B . n 
B 1 125 GLY 125 121 121 GLY GLY B . n 
B 1 126 ASN 126 122 122 ASN ASN B . n 
B 1 127 TYR 127 123 123 TYR TYR B . n 
B 1 128 ASP 128 124 124 ASP ASP B . n 
B 1 129 ARG 129 125 125 ARG ARG B . n 
B 1 130 LEU 130 126 126 LEU LEU B . n 
B 1 131 GLU 131 127 127 GLU GLU B . n 
B 1 132 GLN 132 128 128 GLN GLN B . n 
B 1 133 LEU 133 129 129 LEU LEU B . n 
B 1 134 ALA 134 130 130 ALA ALA B . n 
B 1 135 GLY 135 131 131 GLY GLY B . n 
B 1 136 ASN 136 132 132 ASN ASN B . n 
B 1 137 LEU 137 133 133 LEU LEU B . n 
B 1 138 ARG 138 134 134 ARG ARG B . n 
B 1 139 GLU 139 135 135 GLU GLU B . n 
B 1 140 ASN 140 136 136 ASN ASN B . n 
B 1 141 ILE 141 137 137 ILE ILE B . n 
B 1 142 GLU 142 138 138 GLU GLU B . n 
B 1 143 LEU 143 139 139 LEU LEU B . n 
B 1 144 GLY 144 140 140 GLY GLY B . n 
B 1 145 ASN 145 141 141 ASN ASN B . n 
B 1 146 GLY 146 142 142 GLY GLY B . n 
B 1 147 PRO 147 143 143 PRO PRO B . n 
B 1 148 LEU 148 144 144 LEU LEU B . n 
B 1 149 GLU 149 145 145 GLU GLU B . n 
B 1 150 GLU 150 146 146 GLU GLU B . n 
B 1 151 ALA 151 147 147 ALA ALA B . n 
B 1 152 ILE 152 148 148 ILE ILE B . n 
B 1 153 SER 153 149 149 SER SER B . n 
B 1 154 ALA 154 150 150 ALA ALA B . n 
B 1 155 LEU 155 151 151 LEU LEU B . n 
B 1 156 TYR 156 152 152 TYR TYR B . n 
B 1 157 TYR 157 153 153 TYR TYR B . n 
B 1 158 TYR 158 154 154 TYR TYR B . n 
B 1 159 SER 159 155 155 SER SER B . n 
B 1 160 THR 160 156 156 THR THR B . n 
B 1 161 GLY 161 157 157 GLY GLY B . n 
B 1 162 GLY 162 158 158 GLY GLY B . n 
B 1 163 THR 163 159 159 THR THR B . n 
B 1 164 GLN 164 160 160 GLN GLN B . n 
B 1 165 LEU 165 161 161 LEU LEU B . n 
B 1 166 PRO 166 162 162 PRO PRO B . n 
B 1 167 THR 167 163 163 THR THR B . n 
B 1 168 LEU 168 164 164 LEU LEU B . n 
B 1 169 ALA 169 165 165 ALA ALA B . n 
B 1 170 ARG 170 166 166 ARG ARG B . n 
B 1 171 SER 171 167 167 SER SER B . n 
B 1 172 PHE 172 168 168 PHE PHE B . n 
B 1 173 ILE 173 169 169 ILE ILE B . n 
B 1 174 ILE 174 170 170 ILE ILE B . n 
B 1 175 CYS 175 171 171 CYS CYS B . n 
B 1 176 ILE 176 172 172 ILE ILE B . n 
B 1 177 GLN 177 173 173 GLN GLN B . n 
B 1 178 MET 178 174 174 MET MET B . n 
B 1 179 ILE 179 175 175 ILE ILE B . n 
B 1 180 SER 180 176 176 SER SER B . n 
B 1 181 GLU 181 177 177 GLU GLU B . n 
B 1 182 ALA 182 178 178 ALA ALA B . n 
B 1 183 ALA 183 179 179 ALA ALA B . n 
B 1 184 ARG 184 180 180 ARG ARG B . n 
B 1 185 PHE 185 181 181 PHE PHE B . n 
B 1 186 GLN 186 182 182 GLN GLN B . n 
B 1 187 TYR 187 183 183 TYR TYR B . n 
B 1 188 ILE 188 184 184 ILE ILE B . n 
B 1 189 GLU 189 185 185 GLU GLU B . n 
B 1 190 GLY 190 186 186 GLY GLY B . n 
B 1 191 GLU 191 187 187 GLU GLU B . n 
B 1 192 MET 192 188 188 MET MET B . n 
B 1 193 ARG 193 189 189 ARG ARG B . n 
B 1 194 THR 194 190 190 THR THR B . n 
B 1 195 ARG 195 191 191 ARG ARG B . n 
B 1 196 ILE 196 192 192 ILE ILE B . n 
B 1 197 ARG 197 193 193 ARG ARG B . n 
B 1 198 TYR 198 194 194 TYR TYR B . n 
B 1 199 ASN 199 195 195 ASN ASN B . n 
B 1 200 ARG 200 196 196 ARG ARG B . n 
B 1 201 ARG 201 197 197 ARG ARG B . n 
B 1 202 SER 202 198 198 SER SER B . n 
B 1 203 ALA 203 199 199 ALA ALA B . n 
B 1 204 PRO 204 200 200 PRO PRO B . n 
B 1 205 ASP 205 201 201 ASP ASP B . n 
B 1 206 PRO 206 202 202 PRO PRO B . n 
B 1 207 SER 207 203 203 SER SER B . n 
B 1 208 VAL 208 204 204 VAL VAL B . n 
B 1 209 ILE 209 205 205 ILE ILE B . n 
B 1 210 THR 210 206 206 THR THR B . n 
B 1 211 LEU 211 207 207 LEU LEU B . n 
B 1 212 GLU 212 208 208 GLU GLU B . n 
B 1 213 ASN 213 209 209 ASN ASN B . n 
B 1 214 SER 214 210 210 SER SER B . n 
B 1 215 TRP 215 211 211 TRP TRP B . n 
B 1 216 GLY 216 212 212 GLY GLY B . n 
B 1 217 ARG 217 213 213 ARG ARG B . n 
B 1 218 LEU 218 214 214 LEU LEU B . n 
B 1 219 SER 219 215 215 SER SER B . n 
B 1 220 THR 220 216 216 THR THR B . n 
B 1 221 ALA 221 217 217 ALA ALA B . n 
B 1 222 ILE 222 218 218 ILE ILE B . n 
B 1 223 GLN 223 219 219 GLN GLN B . n 
B 1 224 GLU 224 220 220 GLU GLU B . n 
B 1 225 SER 225 221 221 SER SER B . n 
B 1 226 ASN 226 222 222 ASN ASN B . n 
B 1 227 GLN 227 223 223 GLN GLN B . n 
B 1 228 GLY 228 224 224 GLY GLY B . n 
B 1 229 ALA 229 225 225 ALA ALA B . n 
B 1 230 PHE 230 226 226 PHE PHE B . n 
B 1 231 ALA 231 227 227 ALA ALA B . n 
B 1 232 SER 232 228 228 SER SER B . n 
B 1 233 PRO 233 229 229 PRO PRO B . n 
B 1 234 ILE 234 230 230 ILE ILE B . n 
B 1 235 GLN 235 231 231 GLN GLN B . n 
B 1 236 LEU 236 232 232 LEU LEU B . n 
B 1 237 GLN 237 233 233 GLN GLN B . n 
B 1 238 ARG 238 234 234 ARG ARG B . n 
B 1 239 ARG 239 235 235 ARG ARG B . n 
B 1 240 ASN 240 236 236 ASN ASN B . n 
B 1 241 GLY 241 237 237 GLY GLY B . n 
B 1 242 SER 242 238 238 SER SER B . n 
B 1 243 LYS 243 239 239 LYS LYS B . n 
B 1 244 PHE 244 240 240 PHE PHE B . n 
B 1 245 SER 245 241 241 SER SER B . n 
B 1 246 VAL 246 242 242 VAL VAL B . n 
B 1 247 TYR 247 243 243 TYR TYR B . n 
B 1 248 ASP 248 244 244 ASP ASP B . n 
B 1 249 VAL 249 245 245 VAL VAL B . n 
B 1 250 SER 250 246 246 SER SER B . n 
B 1 251 ILE 251 247 247 ILE ILE B . n 
B 1 252 LEU 252 248 248 LEU LEU B . n 
B 1 253 ILE 253 249 249 ILE ILE B . n 
B 1 254 PRO 254 250 250 PRO PRO B . n 
B 1 255 ILE 255 251 251 ILE ILE B . n 
B 1 256 ILE 256 252 252 ILE ILE B . n 
B 1 257 ALA 257 253 253 ALA ALA B . n 
B 1 258 LEU 258 254 254 LEU LEU B . n 
B 1 259 MET 259 255 255 MET MET B . n 
B 1 260 VAL 260 256 256 VAL VAL B . n 
B 1 261 TYR 261 257 257 TYR TYR B . n 
B 1 262 ARG 262 258 258 ARG ARG B . n 
B 1 263 CYS 263 259 259 CYS CYS B . n 
B 1 264 ALA 264 260 260 ALA ALA B . n 
B 1 265 PRO 265 261 261 PRO PRO B . n 
B 1 266 PRO 266 262 262 PRO PRO B . n 
B 1 267 PRO 267 263 263 PRO PRO B . n 
B 1 268 SER 268 264 ?   ?   ?   B . n 
B 1 269 SER 269 265 ?   ?   ?   B . n 
B 1 270 GLN 270 266 ?   ?   ?   B . n 
B 1 271 PHE 271 267 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BH4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BH4 
_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 A1BH4 1   301 1   A1BH4 LIG A . 
D 3 CL    1   302 1   CL    CL  A . 
E 2 A1BH4 1   301 2   A1BH4 LIG B . 
F 4 HOH   1   401 512 HOH   HOH A . 
F 4 HOH   2   402 177 HOH   HOH A . 
F 4 HOH   3   403 530 HOH   HOH A . 
F 4 HOH   4   404 285 HOH   HOH A . 
F 4 HOH   5   405 403 HOH   HOH A . 
F 4 HOH   6   406 410 HOH   HOH A . 
F 4 HOH   7   407 145 HOH   HOH A . 
F 4 HOH   8   408 198 HOH   HOH A . 
F 4 HOH   9   409 508 HOH   HOH A . 
F 4 HOH   10  410 172 HOH   HOH A . 
F 4 HOH   11  411 74  HOH   HOH A . 
F 4 HOH   12  412 329 HOH   HOH A . 
F 4 HOH   13  413 276 HOH   HOH A . 
F 4 HOH   14  414 475 HOH   HOH A . 
F 4 HOH   15  415 56  HOH   HOH A . 
F 4 HOH   16  416 518 HOH   HOH A . 
F 4 HOH   17  417 113 HOH   HOH A . 
F 4 HOH   18  418 101 HOH   HOH A . 
F 4 HOH   19  419 450 HOH   HOH A . 
F 4 HOH   20  420 347 HOH   HOH A . 
F 4 HOH   21  421 202 HOH   HOH A . 
F 4 HOH   22  422 125 HOH   HOH A . 
F 4 HOH   23  423 100 HOH   HOH A . 
F 4 HOH   24  424 104 HOH   HOH A . 
F 4 HOH   25  425 158 HOH   HOH A . 
F 4 HOH   26  426 282 HOH   HOH A . 
F 4 HOH   27  427 477 HOH   HOH A . 
F 4 HOH   28  428 68  HOH   HOH A . 
F 4 HOH   29  429 182 HOH   HOH A . 
F 4 HOH   30  430 75  HOH   HOH A . 
F 4 HOH   31  431 171 HOH   HOH A . 
F 4 HOH   32  432 73  HOH   HOH A . 
F 4 HOH   33  433 15  HOH   HOH A . 
F 4 HOH   34  434 371 HOH   HOH A . 
F 4 HOH   35  435 7   HOH   HOH A . 
F 4 HOH   36  436 3   HOH   HOH A . 
F 4 HOH   37  437 509 HOH   HOH A . 
F 4 HOH   38  438 123 HOH   HOH A . 
F 4 HOH   39  439 33  HOH   HOH A . 
F 4 HOH   40  440 13  HOH   HOH A . 
F 4 HOH   41  441 150 HOH   HOH A . 
F 4 HOH   42  442 181 HOH   HOH A . 
F 4 HOH   43  443 539 HOH   HOH A . 
F 4 HOH   44  444 12  HOH   HOH A . 
F 4 HOH   45  445 1   HOH   HOH A . 
F 4 HOH   46  446 8   HOH   HOH A . 
F 4 HOH   47  447 11  HOH   HOH A . 
F 4 HOH   48  448 274 HOH   HOH A . 
F 4 HOH   49  449 38  HOH   HOH A . 
F 4 HOH   50  450 132 HOH   HOH A . 
F 4 HOH   51  451 103 HOH   HOH A . 
F 4 HOH   52  452 62  HOH   HOH A . 
F 4 HOH   53  453 279 HOH   HOH A . 
F 4 HOH   54  454 10  HOH   HOH A . 
F 4 HOH   55  455 117 HOH   HOH A . 
F 4 HOH   56  456 205 HOH   HOH A . 
F 4 HOH   57  457 270 HOH   HOH A . 
F 4 HOH   58  458 221 HOH   HOH A . 
F 4 HOH   59  459 176 HOH   HOH A . 
F 4 HOH   60  460 46  HOH   HOH A . 
F 4 HOH   61  461 261 HOH   HOH A . 
F 4 HOH   62  462 18  HOH   HOH A . 
F 4 HOH   63  463 321 HOH   HOH A . 
F 4 HOH   64  464 29  HOH   HOH A . 
F 4 HOH   65  465 149 HOH   HOH A . 
F 4 HOH   66  466 324 HOH   HOH A . 
F 4 HOH   67  467 226 HOH   HOH A . 
F 4 HOH   68  468 421 HOH   HOH A . 
F 4 HOH   69  469 537 HOH   HOH A . 
F 4 HOH   70  470 34  HOH   HOH A . 
F 4 HOH   71  471 187 HOH   HOH A . 
F 4 HOH   72  472 115 HOH   HOH A . 
F 4 HOH   73  473 58  HOH   HOH A . 
F 4 HOH   74  474 234 HOH   HOH A . 
F 4 HOH   75  475 143 HOH   HOH A . 
F 4 HOH   76  476 448 HOH   HOH A . 
F 4 HOH   77  477 157 HOH   HOH A . 
F 4 HOH   78  478 91  HOH   HOH A . 
F 4 HOH   79  479 309 HOH   HOH A . 
F 4 HOH   80  480 32  HOH   HOH A . 
F 4 HOH   81  481 36  HOH   HOH A . 
F 4 HOH   82  482 299 HOH   HOH A . 
F 4 HOH   83  483 372 HOH   HOH A . 
F 4 HOH   84  484 114 HOH   HOH A . 
F 4 HOH   85  485 458 HOH   HOH A . 
F 4 HOH   86  486 184 HOH   HOH A . 
F 4 HOH   87  487 102 HOH   HOH A . 
F 4 HOH   88  488 454 HOH   HOH A . 
F 4 HOH   89  489 9   HOH   HOH A . 
F 4 HOH   90  490 374 HOH   HOH A . 
F 4 HOH   91  491 264 HOH   HOH A . 
F 4 HOH   92  492 84  HOH   HOH A . 
F 4 HOH   93  493 59  HOH   HOH A . 
F 4 HOH   94  494 82  HOH   HOH A . 
F 4 HOH   95  495 48  HOH   HOH A . 
F 4 HOH   96  496 175 HOH   HOH A . 
F 4 HOH   97  497 21  HOH   HOH A . 
F 4 HOH   98  498 31  HOH   HOH A . 
F 4 HOH   99  499 161 HOH   HOH A . 
F 4 HOH   100 500 121 HOH   HOH A . 
F 4 HOH   101 501 311 HOH   HOH A . 
F 4 HOH   102 502 407 HOH   HOH A . 
F 4 HOH   103 503 76  HOH   HOH A . 
F 4 HOH   104 504 214 HOH   HOH A . 
F 4 HOH   105 505 377 HOH   HOH A . 
F 4 HOH   106 506 35  HOH   HOH A . 
F 4 HOH   107 507 44  HOH   HOH A . 
F 4 HOH   108 508 72  HOH   HOH A . 
F 4 HOH   109 509 50  HOH   HOH A . 
F 4 HOH   110 510 99  HOH   HOH A . 
F 4 HOH   111 511 337 HOH   HOH A . 
F 4 HOH   112 512 247 HOH   HOH A . 
F 4 HOH   113 513 400 HOH   HOH A . 
F 4 HOH   114 514 63  HOH   HOH A . 
F 4 HOH   115 515 498 HOH   HOH A . 
F 4 HOH   116 516 406 HOH   HOH A . 
F 4 HOH   117 517 93  HOH   HOH A . 
F 4 HOH   118 518 70  HOH   HOH A . 
F 4 HOH   119 519 254 HOH   HOH A . 
F 4 HOH   120 520 168 HOH   HOH A . 
F 4 HOH   121 521 191 HOH   HOH A . 
F 4 HOH   122 522 201 HOH   HOH A . 
F 4 HOH   123 523 301 HOH   HOH A . 
F 4 HOH   124 524 24  HOH   HOH A . 
F 4 HOH   125 525 89  HOH   HOH A . 
F 4 HOH   126 526 83  HOH   HOH A . 
F 4 HOH   127 527 144 HOH   HOH A . 
F 4 HOH   128 528 367 HOH   HOH A . 
F 4 HOH   129 529 500 HOH   HOH A . 
F 4 HOH   130 530 243 HOH   HOH A . 
F 4 HOH   131 531 525 HOH   HOH A . 
F 4 HOH   132 532 241 HOH   HOH A . 
F 4 HOH   133 533 440 HOH   HOH A . 
F 4 HOH   134 534 49  HOH   HOH A . 
F 4 HOH   135 535 378 HOH   HOH A . 
F 4 HOH   136 536 27  HOH   HOH A . 
F 4 HOH   137 537 362 HOH   HOH A . 
F 4 HOH   138 538 425 HOH   HOH A . 
F 4 HOH   139 539 14  HOH   HOH A . 
F 4 HOH   140 540 312 HOH   HOH A . 
F 4 HOH   141 541 283 HOH   HOH A . 
F 4 HOH   142 542 472 HOH   HOH A . 
F 4 HOH   143 543 471 HOH   HOH A . 
F 4 HOH   144 544 260 HOH   HOH A . 
F 4 HOH   145 545 66  HOH   HOH A . 
F 4 HOH   146 546 64  HOH   HOH A . 
F 4 HOH   147 547 517 HOH   HOH A . 
F 4 HOH   148 548 124 HOH   HOH A . 
F 4 HOH   149 549 199 HOH   HOH A . 
F 4 HOH   150 550 193 HOH   HOH A . 
F 4 HOH   151 551 77  HOH   HOH A . 
F 4 HOH   152 552 431 HOH   HOH A . 
F 4 HOH   153 553 485 HOH   HOH A . 
F 4 HOH   154 554 248 HOH   HOH A . 
F 4 HOH   155 555 396 HOH   HOH A . 
F 4 HOH   156 556 540 HOH   HOH A . 
F 4 HOH   157 557 345 HOH   HOH A . 
F 4 HOH   158 558 273 HOH   HOH A . 
F 4 HOH   159 559 141 HOH   HOH A . 
F 4 HOH   160 560 43  HOH   HOH A . 
F 4 HOH   161 561 110 HOH   HOH A . 
F 4 HOH   162 562 225 HOH   HOH A . 
F 4 HOH   163 563 533 HOH   HOH A . 
F 4 HOH   164 564 253 HOH   HOH A . 
F 4 HOH   165 565 60  HOH   HOH A . 
F 4 HOH   166 566 313 HOH   HOH A . 
F 4 HOH   167 567 480 HOH   HOH A . 
F 4 HOH   168 568 192 HOH   HOH A . 
F 4 HOH   169 569 484 HOH   HOH A . 
F 4 HOH   170 570 456 HOH   HOH A . 
F 4 HOH   171 571 37  HOH   HOH A . 
F 4 HOH   172 572 488 HOH   HOH A . 
F 4 HOH   173 573 111 HOH   HOH A . 
F 4 HOH   174 574 288 HOH   HOH A . 
F 4 HOH   175 575 352 HOH   HOH A . 
F 4 HOH   176 576 522 HOH   HOH A . 
F 4 HOH   177 577 287 HOH   HOH A . 
F 4 HOH   178 578 503 HOH   HOH A . 
F 4 HOH   179 579 52  HOH   HOH A . 
F 4 HOH   180 580 153 HOH   HOH A . 
F 4 HOH   181 581 354 HOH   HOH A . 
F 4 HOH   182 582 186 HOH   HOH A . 
F 4 HOH   183 583 441 HOH   HOH A . 
F 4 HOH   184 584 531 HOH   HOH A . 
F 4 HOH   185 585 160 HOH   HOH A . 
F 4 HOH   186 586 318 HOH   HOH A . 
F 4 HOH   187 587 457 HOH   HOH A . 
F 4 HOH   188 588 116 HOH   HOH A . 
F 4 HOH   189 589 413 HOH   HOH A . 
F 4 HOH   190 590 417 HOH   HOH A . 
F 4 HOH   191 591 252 HOH   HOH A . 
F 4 HOH   192 592 368 HOH   HOH A . 
F 4 HOH   193 593 118 HOH   HOH A . 
F 4 HOH   194 594 269 HOH   HOH A . 
F 4 HOH   195 595 316 HOH   HOH A . 
F 4 HOH   196 596 355 HOH   HOH A . 
F 4 HOH   197 597 535 HOH   HOH A . 
F 4 HOH   198 598 229 HOH   HOH A . 
F 4 HOH   199 599 353 HOH   HOH A . 
F 4 HOH   200 600 122 HOH   HOH A . 
F 4 HOH   201 601 390 HOH   HOH A . 
F 4 HOH   202 602 350 HOH   HOH A . 
F 4 HOH   203 603 256 HOH   HOH A . 
F 4 HOH   204 604 504 HOH   HOH A . 
F 4 HOH   205 605 190 HOH   HOH A . 
F 4 HOH   206 606 366 HOH   HOH A . 
F 4 HOH   207 607 230 HOH   HOH A . 
F 4 HOH   208 608 105 HOH   HOH A . 
F 4 HOH   209 609 293 HOH   HOH A . 
F 4 HOH   210 610 510 HOH   HOH A . 
F 4 HOH   211 611 351 HOH   HOH A . 
F 4 HOH   212 612 126 HOH   HOH A . 
F 4 HOH   213 613 251 HOH   HOH A . 
F 4 HOH   214 614 507 HOH   HOH A . 
F 4 HOH   215 615 244 HOH   HOH A . 
F 4 HOH   216 616 451 HOH   HOH A . 
F 4 HOH   217 617 462 HOH   HOH A . 
F 4 HOH   218 618 131 HOH   HOH A . 
F 4 HOH   219 619 439 HOH   HOH A . 
F 4 HOH   220 620 468 HOH   HOH A . 
F 4 HOH   221 621 148 HOH   HOH A . 
F 4 HOH   222 622 348 HOH   HOH A . 
F 4 HOH   223 623 266 HOH   HOH A . 
F 4 HOH   224 624 452 HOH   HOH A . 
F 4 HOH   225 625 470 HOH   HOH A . 
F 4 HOH   226 626 268 HOH   HOH A . 
F 4 HOH   227 627 280 HOH   HOH A . 
F 4 HOH   228 628 183 HOH   HOH A . 
F 4 HOH   229 629 524 HOH   HOH A . 
F 4 HOH   230 630 376 HOH   HOH A . 
F 4 HOH   231 631 319 HOH   HOH A . 
F 4 HOH   232 632 333 HOH   HOH A . 
F 4 HOH   233 633 416 HOH   HOH A . 
F 4 HOH   234 634 492 HOH   HOH A . 
F 4 HOH   235 635 481 HOH   HOH A . 
F 4 HOH   236 636 482 HOH   HOH A . 
G 4 HOH   1   401 514 HOH   HOH B . 
G 4 HOH   2   402 490 HOH   HOH B . 
G 4 HOH   3   403 258 HOH   HOH B . 
G 4 HOH   4   404 218 HOH   HOH B . 
G 4 HOH   5   405 152 HOH   HOH B . 
G 4 HOH   6   406 398 HOH   HOH B . 
G 4 HOH   7   407 467 HOH   HOH B . 
G 4 HOH   8   408 106 HOH   HOH B . 
G 4 HOH   9   409 164 HOH   HOH B . 
G 4 HOH   10  410 358 HOH   HOH B . 
G 4 HOH   11  411 529 HOH   HOH B . 
G 4 HOH   12  412 339 HOH   HOH B . 
G 4 HOH   13  413 185 HOH   HOH B . 
G 4 HOH   14  414 433 HOH   HOH B . 
G 4 HOH   15  415 399 HOH   HOH B . 
G 4 HOH   16  416 136 HOH   HOH B . 
G 4 HOH   17  417 430 HOH   HOH B . 
G 4 HOH   18  418 139 HOH   HOH B . 
G 4 HOH   19  419 325 HOH   HOH B . 
G 4 HOH   20  420 412 HOH   HOH B . 
G 4 HOH   21  421 386 HOH   HOH B . 
G 4 HOH   22  422 86  HOH   HOH B . 
G 4 HOH   23  423 39  HOH   HOH B . 
G 4 HOH   24  424 128 HOH   HOH B . 
G 4 HOH   25  425 250 HOH   HOH B . 
G 4 HOH   26  426 432 HOH   HOH B . 
G 4 HOH   27  427 151 HOH   HOH B . 
G 4 HOH   28  428 206 HOH   HOH B . 
G 4 HOH   29  429 322 HOH   HOH B . 
G 4 HOH   30  430 427 HOH   HOH B . 
G 4 HOH   31  431 69  HOH   HOH B . 
G 4 HOH   32  432 169 HOH   HOH B . 
G 4 HOH   33  433 174 HOH   HOH B . 
G 4 HOH   34  434 292 HOH   HOH B . 
G 4 HOH   35  435 306 HOH   HOH B . 
G 4 HOH   36  436 277 HOH   HOH B . 
G 4 HOH   37  437 112 HOH   HOH B . 
G 4 HOH   38  438 523 HOH   HOH B . 
G 4 HOH   39  439 212 HOH   HOH B . 
G 4 HOH   40  440 437 HOH   HOH B . 
G 4 HOH   41  441 328 HOH   HOH B . 
G 4 HOH   42  442 96  HOH   HOH B . 
G 4 HOH   43  443 527 HOH   HOH B . 
G 4 HOH   44  444 98  HOH   HOH B . 
G 4 HOH   45  445 162 HOH   HOH B . 
G 4 HOH   46  446 109 HOH   HOH B . 
G 4 HOH   47  447 408 HOH   HOH B . 
G 4 HOH   48  448 208 HOH   HOH B . 
G 4 HOH   49  449 54  HOH   HOH B . 
G 4 HOH   50  450 92  HOH   HOH B . 
G 4 HOH   51  451 154 HOH   HOH B . 
G 4 HOH   52  452 389 HOH   HOH B . 
G 4 HOH   53  453 207 HOH   HOH B . 
G 4 HOH   54  454 133 HOH   HOH B . 
G 4 HOH   55  455 438 HOH   HOH B . 
G 4 HOH   56  456 119 HOH   HOH B . 
G 4 HOH   57  457 19  HOH   HOH B . 
G 4 HOH   58  458 2   HOH   HOH B . 
G 4 HOH   59  459 379 HOH   HOH B . 
G 4 HOH   60  460 423 HOH   HOH B . 
G 4 HOH   61  461 42  HOH   HOH B . 
G 4 HOH   62  462 88  HOH   HOH B . 
G 4 HOH   63  463 4   HOH   HOH B . 
G 4 HOH   64  464 165 HOH   HOH B . 
G 4 HOH   65  465 26  HOH   HOH B . 
G 4 HOH   66  466 137 HOH   HOH B . 
G 4 HOH   67  467 81  HOH   HOH B . 
G 4 HOH   68  468 334 HOH   HOH B . 
G 4 HOH   69  469 363 HOH   HOH B . 
G 4 HOH   70  470 16  HOH   HOH B . 
G 4 HOH   71  471 483 HOH   HOH B . 
G 4 HOH   72  472 289 HOH   HOH B . 
G 4 HOH   73  473 67  HOH   HOH B . 
G 4 HOH   74  474 310 HOH   HOH B . 
G 4 HOH   75  475 20  HOH   HOH B . 
G 4 HOH   76  476 302 HOH   HOH B . 
G 4 HOH   77  477 22  HOH   HOH B . 
G 4 HOH   78  478 196 HOH   HOH B . 
G 4 HOH   79  479 235 HOH   HOH B . 
G 4 HOH   80  480 340 HOH   HOH B . 
G 4 HOH   81  481 239 HOH   HOH B . 
G 4 HOH   82  482 341 HOH   HOH B . 
G 4 HOH   83  483 265 HOH   HOH B . 
G 4 HOH   84  484 532 HOH   HOH B . 
G 4 HOH   85  485 479 HOH   HOH B . 
G 4 HOH   86  486 155 HOH   HOH B . 
G 4 HOH   87  487 204 HOH   HOH B . 
G 4 HOH   88  488 541 HOH   HOH B . 
G 4 HOH   89  489 5   HOH   HOH B . 
G 4 HOH   90  490 373 HOH   HOH B . 
G 4 HOH   91  491 188 HOH   HOH B . 
G 4 HOH   92  492 51  HOH   HOH B . 
G 4 HOH   93  493 304 HOH   HOH B . 
G 4 HOH   94  494 55  HOH   HOH B . 
G 4 HOH   95  495 28  HOH   HOH B . 
G 4 HOH   96  496 53  HOH   HOH B . 
G 4 HOH   97  497 203 HOH   HOH B . 
G 4 HOH   98  498 30  HOH   HOH B . 
G 4 HOH   99  499 231 HOH   HOH B . 
G 4 HOH   100 500 65  HOH   HOH B . 
G 4 HOH   101 501 135 HOH   HOH B . 
G 4 HOH   102 502 25  HOH   HOH B . 
G 4 HOH   103 503 47  HOH   HOH B . 
G 4 HOH   104 504 453 HOH   HOH B . 
G 4 HOH   105 505 95  HOH   HOH B . 
G 4 HOH   106 506 146 HOH   HOH B . 
G 4 HOH   107 507 291 HOH   HOH B . 
G 4 HOH   108 508 365 HOH   HOH B . 
G 4 HOH   109 509 401 HOH   HOH B . 
G 4 HOH   110 510 255 HOH   HOH B . 
G 4 HOH   111 511 107 HOH   HOH B . 
G 4 HOH   112 512 237 HOH   HOH B . 
G 4 HOH   113 513 249 HOH   HOH B . 
G 4 HOH   114 514 381 HOH   HOH B . 
G 4 HOH   115 515 40  HOH   HOH B . 
G 4 HOH   116 516 189 HOH   HOH B . 
G 4 HOH   117 517 194 HOH   HOH B . 
G 4 HOH   118 518 224 HOH   HOH B . 
G 4 HOH   119 519 392 HOH   HOH B . 
G 4 HOH   120 520 331 HOH   HOH B . 
G 4 HOH   121 521 307 HOH   HOH B . 
G 4 HOH   122 522 23  HOH   HOH B . 
G 4 HOH   123 523 326 HOH   HOH B . 
G 4 HOH   124 524 526 HOH   HOH B . 
G 4 HOH   125 525 200 HOH   HOH B . 
G 4 HOH   126 526 216 HOH   HOH B . 
G 4 HOH   127 527 97  HOH   HOH B . 
G 4 HOH   128 528 515 HOH   HOH B . 
G 4 HOH   129 529 469 HOH   HOH B . 
G 4 HOH   130 530 497 HOH   HOH B . 
G 4 HOH   131 531 464 HOH   HOH B . 
G 4 HOH   132 532 519 HOH   HOH B . 
G 4 HOH   133 533 85  HOH   HOH B . 
G 4 HOH   134 534 179 HOH   HOH B . 
G 4 HOH   135 535 215 HOH   HOH B . 
G 4 HOH   136 536 45  HOH   HOH B . 
G 4 HOH   137 537 138 HOH   HOH B . 
G 4 HOH   138 538 140 HOH   HOH B . 
G 4 HOH   139 539 159 HOH   HOH B . 
G 4 HOH   140 540 142 HOH   HOH B . 
G 4 HOH   141 541 134 HOH   HOH B . 
G 4 HOH   142 542 6   HOH   HOH B . 
G 4 HOH   143 543 259 HOH   HOH B . 
G 4 HOH   144 544 411 HOH   HOH B . 
G 4 HOH   145 545 330 HOH   HOH B . 
G 4 HOH   146 546 223 HOH   HOH B . 
G 4 HOH   147 547 79  HOH   HOH B . 
G 4 HOH   148 548 80  HOH   HOH B . 
G 4 HOH   149 549 419 HOH   HOH B . 
G 4 HOH   150 550 238 HOH   HOH B . 
G 4 HOH   151 551 108 HOH   HOH B . 
G 4 HOH   152 552 385 HOH   HOH B . 
G 4 HOH   153 553 245 HOH   HOH B . 
G 4 HOH   154 554 346 HOH   HOH B . 
G 4 HOH   155 555 359 HOH   HOH B . 
G 4 HOH   156 556 478 HOH   HOH B . 
G 4 HOH   157 557 227 HOH   HOH B . 
G 4 HOH   158 558 284 HOH   HOH B . 
G 4 HOH   159 559 384 HOH   HOH B . 
G 4 HOH   160 560 286 HOH   HOH B . 
G 4 HOH   161 561 491 HOH   HOH B . 
G 4 HOH   162 562 486 HOH   HOH B . 
G 4 HOH   163 563 506 HOH   HOH B . 
G 4 HOH   164 564 120 HOH   HOH B . 
G 4 HOH   165 565 336 HOH   HOH B . 
G 4 HOH   166 566 493 HOH   HOH B . 
G 4 HOH   167 567 61  HOH   HOH B . 
G 4 HOH   168 568 383 HOH   HOH B . 
G 4 HOH   169 569 446 HOH   HOH B . 
G 4 HOH   170 570 528 HOH   HOH B . 
G 4 HOH   171 571 170 HOH   HOH B . 
G 4 HOH   172 572 94  HOH   HOH B . 
G 4 HOH   173 573 405 HOH   HOH B . 
G 4 HOH   174 574 41  HOH   HOH B . 
G 4 HOH   175 575 404 HOH   HOH B . 
G 4 HOH   176 576 463 HOH   HOH B . 
G 4 HOH   177 577 211 HOH   HOH B . 
G 4 HOH   178 578 297 HOH   HOH B . 
G 4 HOH   179 579 443 HOH   HOH B . 
G 4 HOH   180 580 147 HOH   HOH B . 
G 4 HOH   181 581 220 HOH   HOH B . 
G 4 HOH   182 582 267 HOH   HOH B . 
G 4 HOH   183 583 278 HOH   HOH B . 
G 4 HOH   184 584 233 HOH   HOH B . 
G 4 HOH   185 585 300 HOH   HOH B . 
G 4 HOH   186 586 263 HOH   HOH B . 
G 4 HOH   187 587 57  HOH   HOH B . 
G 4 HOH   188 588 257 HOH   HOH B . 
G 4 HOH   189 589 127 HOH   HOH B . 
G 4 HOH   190 590 236 HOH   HOH B . 
G 4 HOH   191 591 87  HOH   HOH B . 
G 4 HOH   192 592 271 HOH   HOH B . 
G 4 HOH   193 593 180 HOH   HOH B . 
G 4 HOH   194 594 521 HOH   HOH B . 
G 4 HOH   195 595 459 HOH   HOH B . 
G 4 HOH   196 596 332 HOH   HOH B . 
G 4 HOH   197 597 296 HOH   HOH B . 
G 4 HOH   198 598 501 HOH   HOH B . 
G 4 HOH   199 599 272 HOH   HOH B . 
G 4 HOH   200 600 71  HOH   HOH B . 
G 4 HOH   201 601 487 HOH   HOH B . 
G 4 HOH   202 602 442 HOH   HOH B . 
G 4 HOH   203 603 163 HOH   HOH B . 
G 4 HOH   204 604 460 HOH   HOH B . 
G 4 HOH   205 605 495 HOH   HOH B . 
G 4 HOH   206 606 513 HOH   HOH B . 
G 4 HOH   207 607 308 HOH   HOH B . 
G 4 HOH   208 608 402 HOH   HOH B . 
G 4 HOH   209 609 380 HOH   HOH B . 
G 4 HOH   210 610 397 HOH   HOH B . 
G 4 HOH   211 611 343 HOH   HOH B . 
G 4 HOH   212 612 356 HOH   HOH B . 
G 4 HOH   213 613 246 HOH   HOH B . 
G 4 HOH   214 614 435 HOH   HOH B . 
G 4 HOH   215 615 305 HOH   HOH B . 
G 4 HOH   216 616 240 HOH   HOH B . 
G 4 HOH   217 617 298 HOH   HOH B . 
G 4 HOH   218 618 17  HOH   HOH B . 
G 4 HOH   219 619 213 HOH   HOH B . 
G 4 HOH   220 620 466 HOH   HOH B . 
G 4 HOH   221 621 418 HOH   HOH B . 
G 4 HOH   222 622 129 HOH   HOH B . 
G 4 HOH   223 623 338 HOH   HOH B . 
G 4 HOH   224 624 536 HOH   HOH B . 
G 4 HOH   225 625 335 HOH   HOH B . 
G 4 HOH   226 626 393 HOH   HOH B . 
G 4 HOH   227 627 209 HOH   HOH B . 
G 4 HOH   228 628 516 HOH   HOH B . 
G 4 HOH   229 629 382 HOH   HOH B . 
G 4 HOH   230 630 436 HOH   HOH B . 
G 4 HOH   231 631 395 HOH   HOH B . 
G 4 HOH   232 632 409 HOH   HOH B . 
G 4 HOH   233 633 447 HOH   HOH B . 
G 4 HOH   234 634 496 HOH   HOH B . 
G 4 HOH   235 635 349 HOH   HOH B . 
G 4 HOH   236 636 317 HOH   HOH B . 
G 4 HOH   237 637 538 HOH   HOH B . 
G 4 HOH   238 638 166 HOH   HOH B . 
G 4 HOH   239 639 303 HOH   HOH B . 
G 4 HOH   240 640 294 HOH   HOH B . 
G 4 HOH   241 641 295 HOH   HOH B . 
G 4 HOH   242 642 387 HOH   HOH B . 
G 4 HOH   243 643 494 HOH   HOH B . 
G 4 HOH   244 644 449 HOH   HOH B . 
G 4 HOH   245 645 357 HOH   HOH B . 
G 4 HOH   246 646 210 HOH   HOH B . 
G 4 HOH   247 647 195 HOH   HOH B . 
G 4 HOH   248 648 489 HOH   HOH B . 
G 4 HOH   249 649 444 HOH   HOH B . 
G 4 HOH   250 650 281 HOH   HOH B . 
G 4 HOH   251 651 217 HOH   HOH B . 
G 4 HOH   252 652 420 HOH   HOH B . 
G 4 HOH   253 653 290 HOH   HOH B . 
G 4 HOH   254 654 511 HOH   HOH B . 
G 4 HOH   255 655 173 HOH   HOH B . 
G 4 HOH   256 656 167 HOH   HOH B . 
G 4 HOH   257 657 178 HOH   HOH B . 
G 4 HOH   258 658 499 HOH   HOH B . 
G 4 HOH   259 659 361 HOH   HOH B . 
G 4 HOH   260 660 197 HOH   HOH B . 
G 4 HOH   261 661 434 HOH   HOH B . 
G 4 HOH   262 662 242 HOH   HOH B . 
G 4 HOH   263 663 78  HOH   HOH B . 
G 4 HOH   264 664 445 HOH   HOH B . 
G 4 HOH   265 665 90  HOH   HOH B . 
G 4 HOH   266 666 465 HOH   HOH B . 
G 4 HOH   267 667 476 HOH   HOH B . 
G 4 HOH   268 668 424 HOH   HOH B . 
G 4 HOH   269 669 426 HOH   HOH B . 
G 4 HOH   270 670 232 HOH   HOH B . 
G 4 HOH   271 671 429 HOH   HOH B . 
G 4 HOH   272 672 320 HOH   HOH B . 
G 4 HOH   273 673 323 HOH   HOH B . 
G 4 HOH   274 674 262 HOH   HOH B . 
G 4 HOH   275 675 414 HOH   HOH B . 
G 4 HOH   276 676 222 HOH   HOH B . 
G 4 HOH   277 677 275 HOH   HOH B . 
G 4 HOH   278 678 415 HOH   HOH B . 
G 4 HOH   279 679 156 HOH   HOH B . 
G 4 HOH   280 680 473 HOH   HOH B . 
G 4 HOH   281 681 327 HOH   HOH B . 
G 4 HOH   282 682 422 HOH   HOH B . 
G 4 HOH   283 683 474 HOH   HOH B . 
G 4 HOH   284 684 520 HOH   HOH B . 
G 4 HOH   285 685 502 HOH   HOH B . 
G 4 HOH   286 686 375 HOH   HOH B . 
G 4 HOH   287 687 391 HOH   HOH B . 
G 4 HOH   288 688 370 HOH   HOH B . 
G 4 HOH   289 689 130 HOH   HOH B . 
G 4 HOH   290 690 428 HOH   HOH B . 
G 4 HOH   291 691 315 HOH   HOH B . 
G 4 HOH   292 692 364 HOH   HOH B . 
G 4 HOH   293 693 342 HOH   HOH B . 
G 4 HOH   294 694 461 HOH   HOH B . 
G 4 HOH   295 695 394 HOH   HOH B . 
G 4 HOH   296 696 228 HOH   HOH B . 
G 4 HOH   297 697 219 HOH   HOH B . 
G 4 HOH   298 698 505 HOH   HOH B . 
G 4 HOH   299 699 314 HOH   HOH B . 
G 4 HOH   300 700 534 HOH   HOH B . 
G 4 HOH   301 701 344 HOH   HOH B . 
G 4 HOH   302 702 388 HOH   HOH B . 
G 4 HOH   303 703 455 HOH   HOH B . 
G 4 HOH   304 704 360 HOH   HOH B . 
G 4 HOH   305 705 369 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.240 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9E3T 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     38.858 
_cell.length_a_esd                 ? 
_cell.length_b                     57.467 
_cell.length_b_esd                 ? 
_cell.length_c                     124.908 
_cell.length_c_esd                 ? 
_cell.volume                       278162.753 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9E3T 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9E3T 
_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             2.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.34 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM Hepes pH 6.5 and 20% PEG 6000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-10-26 
_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   0.979 
_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                        'APS BEAMLINE 24-ID-E' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          15.29 
_reflns.entry_id                                       9E3T 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               50.0 
_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                                     85134 
_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                           95.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          1.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.90 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.16 
_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                                    1.80 
_reflns_shell.d_res_low                                     1.83 
_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                             4320 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.45 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               20.02 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9E3T 
_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                            1.80 
_refine.ls_d_res_low                             42.24 
_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                     47723 
_refine.ls_number_reflns_R_free                  2393 
_refine.ls_number_reflns_R_work                  45330 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.99 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1943 
_refine.ls_R_factor_R_free                       0.2336 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1923 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.37 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 22.4623 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2154 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        42.24 
_refine_hist.number_atoms_solvent             541 
_refine_hist.number_atoms_total               4679 
_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        4103 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         35 
_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' ? 0.0036  ? 4236 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5905  ? 5766 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0433  ? 639  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0063  ? 761  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.3884 ? 1549 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.80 1.84  . . 105 2160 76.34 . . . . 0.2537 . . . . . . . . . . . 0.3003 
'X-RAY DIFFRACTION' 1.84 1.88  . . 132 2656 94.13 . . . . 0.2456 . . . . . . . . . . . 0.3171 
'X-RAY DIFFRACTION' 1.88 1.92  . . 138 2486 88.14 . . . . 0.2332 . . . . . . . . . . . 0.3071 
'X-RAY DIFFRACTION' 1.92 1.97  . . 143 2513 89.25 . . . . 0.2211 . . . . . . . . . . . 0.2858 
'X-RAY DIFFRACTION' 1.97 2.03  . . 142 2781 98.55 . . . . 0.2018 . . . . . . . . . . . 0.2552 
'X-RAY DIFFRACTION' 2.03 2.09  . . 131 2762 98.33 . . . . 0.2017 . . . . . . . . . . . 0.2532 
'X-RAY DIFFRACTION' 2.09 2.15  . . 159 2794 97.98 . . . . 0.1930 . . . . . . . . . . . 0.2296 
'X-RAY DIFFRACTION' 2.15 2.23  . . 120 2764 97.80 . . . . 0.1903 . . . . . . . . . . . 0.2361 
'X-RAY DIFFRACTION' 2.23 2.32  . . 144 2781 98.29 . . . . 0.1884 . . . . . . . . . . . 0.2620 
'X-RAY DIFFRACTION' 2.32 2.42  . . 137 2767 97.03 . . . . 0.1977 . . . . . . . . . . . 0.2437 
'X-RAY DIFFRACTION' 2.42 2.55  . . 146 2715 96.36 . . . . 0.2033 . . . . . . . . . . . 0.2600 
'X-RAY DIFFRACTION' 2.55 2.71  . . 159 2537 91.02 . . . . 0.1951 . . . . . . . . . . . 0.2237 
'X-RAY DIFFRACTION' 2.71 2.92  . . 140 2565 90.50 . . . . 0.1952 . . . . . . . . . . . 0.2335 
'X-RAY DIFFRACTION' 2.92 3.22  . . 149 2794 97.68 . . . . 0.1842 . . . . . . . . . . . 0.2151 
'X-RAY DIFFRACTION' 3.22 3.68  . . 142 2772 97.36 . . . . 0.1785 . . . . . . . . . . . 0.1981 
'X-RAY DIFFRACTION' 3.68 4.64  . . 145 2733 94.98 . . . . 0.1583 . . . . . . . . . . . 0.1846 
'X-RAY DIFFRACTION' 4.64 42.24 . . 161 2750 93.99 . . . . 0.1944 . . . . . . . . . . . 0.2366 
# 
_struct.entry_id                     9E3T 
_struct.title                        'RTA-RUNT-165 complex' 
_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        9E3T 
_struct_keywords.text            'N-linked glycosidase, TOXIN, HYDROLASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   TOXIN,HYDROLASE/INHIBITOR 
# 
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 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    RICI_RICCO 
_struct_ref.pdbx_db_accession          P02879 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;IFPKQYPIINFTTAGATVQSYTNFIRAVRGRLTTGADVRHEIPVLPNRVGLPINQRFILVELSNHAELSVTLALDVTNAY
VVGYRAGNSAYFFHPDNQEDAEAITHLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEEAISALYYYSTGGTQ
LPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVITLENSWGRLSTAIQESNQGAFASPIQLQRRNGSKF
SVYDVSILIPIIALMVYRCAPPPSSQF
;
_struct_ref.pdbx_align_begin           36 
# 
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 9E3T A 5 ? 271 ? P02879 36 ? 302 ? 1 267 
2 1 9E3T B 5 ? 271 ? P02879 36 ? 302 ? 1 267 
# 
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 9E3T SER A 1 ? UNP P02879 ? ? 'expression tag' -3 1 
1 9E3T ASN A 2 ? UNP P02879 ? ? 'expression tag' -2 2 
1 9E3T ALA A 3 ? UNP P02879 ? ? 'expression tag' -1 3 
1 9E3T MET A 4 ? UNP P02879 ? ? 'expression tag' 0  4 
2 9E3T SER B 1 ? UNP P02879 ? ? 'expression tag' -3 5 
2 9E3T ASN B 2 ? UNP P02879 ? ? 'expression tag' -2 6 
2 9E3T ALA B 3 ? UNP P02879 ? ? 'expression tag' -1 7 
2 9E3T MET B 4 ? UNP P02879 ? ? 'expression tag' 0  8 
# 
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,F 
2 1 B,E,G   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 21  ? THR A 37  ? THR A 17  THR A 33  1 ? 17 
HELX_P HELX_P2  AA2 PRO A 56  ? GLN A 59  ? PRO A 52  GLN A 55  5 ? 4  
HELX_P HELX_P3  AA3 ASN A 101 ? THR A 109 ? ASN A 97  THR A 105 1 ? 9  
HELX_P HELX_P4  AA4 ASN A 126 ? GLY A 135 ? ASN A 122 GLY A 131 1 ? 10 
HELX_P HELX_P5  AA5 LEU A 137 ? ILE A 141 ? LEU A 133 ILE A 137 5 ? 5  
HELX_P HELX_P6  AA6 GLY A 144 ? TYR A 158 ? GLY A 140 TYR A 154 1 ? 15 
HELX_P HELX_P7  AA7 SER A 159 ? GLY A 161 ? SER A 155 GLY A 157 5 ? 3  
HELX_P HELX_P8  AA8 GLN A 164 ? PHE A 185 ? GLN A 160 PHE A 181 1 ? 22 
HELX_P HELX_P9  AA9 PHE A 185 ? ASN A 199 ? PHE A 181 ASN A 195 1 ? 15 
HELX_P HELX_P10 AB1 ASP A 205 ? SER A 225 ? ASP A 201 SER A 221 1 ? 21 
HELX_P HELX_P11 AB2 SER A 250 ? ILE A 253 ? SER A 246 ILE A 249 5 ? 4  
HELX_P HELX_P12 AB3 THR B 21  ? THR B 37  ? THR B 17  THR B 33  1 ? 17 
HELX_P HELX_P13 AB4 PRO B 56  ? GLN B 59  ? PRO B 52  GLN B 55  5 ? 4  
HELX_P HELX_P14 AB5 ASN B 101 ? ILE B 108 ? ASN B 97  ILE B 104 1 ? 8  
HELX_P HELX_P15 AB6 THR B 109 ? LEU B 111 ? THR B 105 LEU B 107 5 ? 3  
HELX_P HELX_P16 AB7 ASN B 126 ? GLY B 135 ? ASN B 122 GLY B 131 1 ? 10 
HELX_P HELX_P17 AB8 LEU B 137 ? ILE B 141 ? LEU B 133 ILE B 137 5 ? 5  
HELX_P HELX_P18 AB9 GLY B 144 ? TYR B 158 ? GLY B 140 TYR B 154 1 ? 15 
HELX_P HELX_P19 AC1 SER B 159 ? GLY B 161 ? SER B 155 GLY B 157 5 ? 3  
HELX_P HELX_P20 AC2 GLN B 164 ? PHE B 185 ? GLN B 160 PHE B 181 1 ? 22 
HELX_P HELX_P21 AC3 PHE B 185 ? TYR B 198 ? PHE B 181 TYR B 194 1 ? 14 
HELX_P HELX_P22 AC4 ASP B 205 ? GLU B 224 ? ASP B 201 GLU B 220 1 ? 20 
HELX_P HELX_P23 AC5 SER B 250 ? LEU B 252 ? SER B 246 LEU B 248 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 6 ? 
AA5 ? 2 ? 
AA6 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? parallel      
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 12  ? THR A 16  ? ILE A 8   THR A 12  
AA1 2 PHE A 61  ? SER A 67  ? PHE A 57  SER A 63  
AA1 3 SER A 73  ? ASP A 79  ? SER A 69  ASP A 75  
AA1 4 VAL A 85  ? ALA A 90  ? VAL A 81  ALA A 86  
AA1 5 SER A 93  ? PHE A 96  ? SER A 89  PHE A 92  
AA1 6 ASN A 117 ? THR A 120 ? ASN A 113 THR A 116 
AA2 1 VAL A 42  ? ARG A 43  ? VAL A 38  ARG A 39  
AA2 2 ILE A 46  ? PRO A 47  ? ILE A 42  PRO A 43  
AA3 1 ALA A 229 ? GLN A 237 ? ALA A 225 GLN A 233 
AA3 2 LYS A 243 ? ASP A 248 ? LYS A 239 ASP A 244 
AA4 1 ILE B 12  ? THR B 16  ? ILE B 8   THR B 12  
AA4 2 PHE B 61  ? SER B 67  ? PHE B 57  SER B 63  
AA4 3 SER B 73  ? ASP B 79  ? SER B 69  ASP B 75  
AA4 4 VAL B 85  ? ALA B 90  ? VAL B 81  ALA B 86  
AA4 5 SER B 93  ? PHE B 96  ? SER B 89  PHE B 92  
AA4 6 ASN B 117 ? THR B 120 ? ASN B 113 THR B 116 
AA5 1 VAL B 42  ? ARG B 43  ? VAL B 38  ARG B 39  
AA5 2 ILE B 46  ? PRO B 47  ? ILE B 42  PRO B 43  
AA6 1 ALA B 229 ? GLN B 237 ? ALA B 225 GLN B 233 
AA6 2 LYS B 243 ? ASP B 248 ? LYS B 239 ASP B 244 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N PHE A 15  ? N PHE A 11  O GLU A 65  ? O GLU A 61  
AA1 2 3 N VAL A 64  ? N VAL A 60  O LEU A 76  ? O LEU A 72  
AA1 3 4 N ALA A 77  ? N ALA A 73  O GLY A 87  ? O GLY A 83  
AA1 4 5 N TYR A 88  ? N TYR A 84  O TYR A 95  ? O TYR A 91  
AA1 5 6 N ALA A 94  ? N ALA A 90  O TYR A 119 ? O TYR A 115 
AA2 1 2 N ARG A 43  ? N ARG A 39  O ILE A 46  ? O ILE A 42  
AA3 1 2 N LEU A 236 ? N LEU A 232 O PHE A 244 ? O PHE A 240 
AA4 1 2 N PHE B 15  ? N PHE B 11  O GLU B 65  ? O GLU B 61  
AA4 2 3 N VAL B 64  ? N VAL B 60  O LEU B 76  ? O LEU B 72  
AA4 3 4 N ALA B 77  ? N ALA B 73  O GLY B 87  ? O GLY B 83  
AA4 4 5 N ALA B 90  ? N ALA B 86  O SER B 93  ? O SER B 89  
AA4 5 6 N ALA B 94  ? N ALA B 90  O TYR B 119 ? O TYR B 115 
AA5 1 2 N ARG B 43  ? N ARG B 39  O ILE B 46  ? O ILE B 42  
AA6 1 2 N PHE B 230 ? N PHE B 226 O TYR B 247 ? O TYR B 243 
# 
_pdbx_entry_details.entry_id                   9E3T 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 533 ? ? O A HOH 553 ? ? 1.82 
2  1 OE1 A GLN 223 ? ? O A HOH 401 ? ? 1.87 
3  1 O   B HOH 611 ? ? O B HOH 617 ? ? 1.88 
4  1 O   A HOH 626 ? ? O A HOH 628 ? ? 1.92 
5  1 O   A HOH 529 ? ? O A HOH 619 ? ? 1.92 
6  1 O   B HOH 452 ? ? O B HOH 642 ? ? 1.92 
7  1 O   A HOH 416 ? ? O A HOH 602 ? ? 1.95 
8  1 O   B HOH 537 ? ? O B HOH 564 ? ? 1.96 
9  1 O   A HOH 408 ? ? O A HOH 429 ? ? 1.97 
10 1 O   A HOH 451 ? ? O A HOH 461 ? ? 1.99 
11 1 O   B HOH 569 ? ? O B HOH 667 ? ? 2.01 
12 1 OE1 A GLU 138 ? ? O A HOH 402 ? ? 2.03 
13 1 O   A HOH 546 ? ? O A HOH 555 ? ? 2.03 
14 1 O   B HOH 552 ? ? O B HOH 604 ? ? 2.04 
15 1 O   A HOH 482 ? ? O A HOH 601 ? ? 2.04 
16 1 O   B HOH 562 ? ? O B HOH 664 ? ? 2.04 
17 1 O   A HOH 542 ? ? O A HOH 617 ? ? 2.06 
18 1 O   B HOH 704 ? ? O B HOH 705 ? ? 2.08 
19 1 O   B HOH 647 ? ? O B HOH 665 ? ? 2.09 
20 1 O   B HOH 519 ? ? O B HOH 584 ? ? 2.10 
21 1 O   B HOH 623 ? ? O B HOH 653 ? ? 2.11 
22 1 O   B HOH 417 ? ? O B HOH 633 ? ? 2.12 
23 1 O   B HOH 573 ? ? O B HOH 631 ? ? 2.13 
24 1 O   B HOH 514 ? ? O B HOH 579 ? ? 2.13 
25 1 O   B HOH 590 ? ? O B HOH 675 ? ? 2.14 
26 1 OE1 B GLU 99  ? ? O B HOH 401 ? ? 2.17 
27 1 NH1 A ARG 196 ? ? O A HOH 403 ? ? 2.17 
28 1 O   A HOH 590 ? ? O A HOH 630 ? ? 2.17 
29 1 OH  A TYR 243 ? ? O A HOH 404 ? ? 2.18 
30 1 O   B HOH 643 ? ? O B HOH 680 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O   A HOH 491 ? ? 1_555 O   B HOH 531 ? ? 1_565 2.00 
2 1 O   B HOH 629 ? ? 1_555 O   B HOH 653 ? ? 1_655 2.03 
3 1 O   B HOH 509 ? ? 1_555 O   B HOH 606 ? ? 1_455 2.03 
4 1 NH2 B ARG 31  ? ? 1_555 OE1 B GLU 135 ? ? 1_455 2.08 
5 1 O   A HOH 622 ? ? 1_555 O   B HOH 692 ? ? 1_565 2.16 
6 1 O   A HOH 453 ? ? 1_555 O   A HOH 602 ? ? 2_656 2.19 
# 
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 ILE A 175 ? ? -121.00 -65.79 
2 1 ILE B 175 ? ? -121.18 -64.08 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 6.10128100066 -8.13607325764   47.8934393265 0.140540688812  ? -0.0480612310676  ? 
-0.00217729843037 ? 0.120174849138  ? -0.0236753761014   ? 0.153478182944  ? 1.68545941852  ? -0.0292776902109 ? 0.201598228589    
? 1.82537737725  ? 0.0819873851054 ? 1.26767305921 ? 0.0224919575698  ? 0.0892816302201  ? -0.0796894529961 ? 0.120346610681   ? 
-0.0581478156532 ? 0.089177572149    ? 0.178521897694    ? -0.0554997018072 ? 0.0342230264168   ? 
2  'X-RAY DIFFRACTION' ? refined 6.66892615964 0.603002669937   43.2417731059 0.127013356998  ? -0.0120169046247  ? 
-0.0220773092744  ? 0.126792216478  ? -0.000457574710839 ? 0.137146978954  ? 1.56294469317  ? -0.385253558933  ? -0.363438699605   
? 0.958799477589 ? 0.0514820848405 ? 2.10444487476 ? 0.0543593054319  ? 0.197740729397   ? 0.027522233873   ? -0.128003198541  ? 
0.0393210429434  ? 0.0587580419103   ? -0.0875142282406  ? -0.388615581912  ? -0.128613738348   ? 
3  'X-RAY DIFFRACTION' ? refined 10.3196560567 10.4462499333    53.0206059117 0.0953669508887 ? 0.0212763602003   ? 
0.0218744354475   ? 0.0847824121886 ? -0.0031886448351   ? 0.117494249985  ? 1.07993925957  ? 0.448217345613   ? 1.47980602377     
? 1.94902269402  ? 0.663263854493  ? 2.27413982687 ? -0.0147347934825 ? 0.0100855274933  ? 0.196145568163   ? -0.0634197608802 ? 
0.0469802671028  ? 0.187365434675    ? -0.211064247628   ? -0.158750362975  ? -0.0381832997122  ? 
4  'X-RAY DIFFRACTION' ? refined 22.5306287678 -1.12333777158   57.0287203281 0.0944399593166 ? -0.00234094523461 ? 
-0.0230808312109  ? 0.130800638551  ? 0.0109292534831    ? 0.0996533187588 ? 2.01794091427  ? 0.00841026045042 ? -0.707588319327   
? 2.45904023127  ? 0.342841240814  ? 1.64090275254 ? 0.0367563703238  ? -0.140300256915  ? 0.00866295408627 ? 0.303771508287   ? 
0.0157928250272  ? -0.142655351505   ? 0.00088639806709  ? 0.100111998767   ? -0.0688009543147  ? 
5  'X-RAY DIFFRACTION' ? refined 20.8947597029 -8.88572846188   48.1128419439 0.120160152522  ? -0.0124219259937  ? 
-0.00734490673628 ? 0.102539975928  ? 0.0049316582328    ? 0.0985480203795 ? 0.967740550911 ? -0.0376871051947 ? -0.120155982726   
? 1.31881526649  ? 0.272349996923  ? 1.83419092404 ? 0.00961592951583 ? -0.0217328696057 ? -0.071978362246  ? 0.0229488351042  ? 
-0.0113446357854 ? -0.00966017415551 ? 0.347770705044    ? 0.0110862365992  ? 0.000772691821073 ? 
6  'X-RAY DIFFRACTION' ? refined 25.060606566  -2.98786117267   29.5208271149 0.155092295998  ? -0.0213355028     ? 
0.0147810118624   ? 0.129930228294  ? -0.00115533961944  ? 0.0998763570246 ? 1.49822767333  ? -0.716541438457  ? 0.888727173975    
? 1.17514354852  ? 0.066948950417  ? 2.3067885863  ? 0.0486640840073  ? 0.0697526395661  ? 0.0825965813405  ? -0.242299989802  ? 
-0.0381429115517 ? -0.0835443414684  ? -0.251001843622   ? 0.240222696599   ? -0.0104294129452  ? 
7  'X-RAY DIFFRACTION' ? refined 13.3406537224 -0.0150295851423 30.2528899805 0.239064698135  ? -0.0102593783608  ? 
-0.00469485525093 ? 0.165327736165  ? -0.000227874465126 ? 0.0815501147604 ? 2.11403420504  ? -0.0441463794552 ? -0.00615737855591 
? 2.57365739628  ? -0.395627180222 ? 2.32550988677 ? 0.013356375764   ? 0.242366270488   ? -0.0142438249266 ? -0.606925528282  ? 
0.138299889072   ? 0.217755680242    ? -0.134253674336   ? -0.224485004857  ? -0.182520315511   ? 
8  'X-RAY DIFFRACTION' ? refined 10.4857433133 -21.79758323     14.4764221002 0.0925519877204 ? 0.0303118181731   ? 
0.00662241991865  ? 0.0707665295638 ? -0.00740700314203  ? 0.109824875358  ? 1.09864005619  ? 0.230558706254   ? -0.0988388803996  
? 1.13914495486  ? -0.410344975023 ? 1.62565429146 ? 0.0155359543304  ? -0.0208654827841 ? 0.0130547040556  ? 0.0610589936079  ? 
-0.0329996098611 ? 0.120331006292    ? -0.273594012387   ? -0.136482168548  ? 0.000685194431007 ? 
9  'X-RAY DIFFRACTION' ? refined 11.1538806147 -30.8620036127   19.1612410647 0.0939495598101 ? 0.0197251000749   ? 
0.0166170084615   ? 0.111656934724  ? -0.00566929317817  ? 0.108920259599  ? 1.45811029228  ? 0.214653455884   ? 0.131448496092    
? 1.2621128005   ? 0.0420423671753 ? 1.81287589925 ? 0.026523743621   ? -0.220468696474  ? 0.0216525553832  ? 0.0838714603057  ? 
-0.0275427063483 ? 0.0561680741907   ? 0.100903668721    ? -0.223984646671  ? -0.0206730619449  ? 
10 'X-RAY DIFFRACTION' ? refined 14.9083649033 -40.8871673208   9.56051723614 0.0941266121835 ? 0.00663729998549  ? 
-0.00858625640695 ? 0.0867163894754 ? -0.00302998325481  ? 0.0961662879311 ? 1.04704720992  ? -0.260958125687  ? -1.27728135408    
? 1.86010919748  ? 0.888815972224  ? 2.01934301609 ? 0.00371772074639 ? -0.0641408402628 ? -0.102651225057  ? 0.130793434966   ? 
0.0487868673985  ? 0.0167351915671   ? 0.212754521482    ? -0.0323546228341 ? -0.0129848362625  ? 
11 'X-RAY DIFFRACTION' ? refined 26.9072880308 -29.2100991871   5.36888596187 0.0771861391616 ? 0.016089560261    ? 
0.0221406077208   ? 0.108456848545  ? -4.66607840478e-05 ? 0.0871683110911 ? 1.67271812971  ? -0.162849147747  ? 0.928090334877    
? 2.66537363679  ? 0.154995901052  ? 2.01518759564 ? 0.00167243619136 ? 0.0717950538105  ? -0.0675993881413 ? -0.0631427344406 ? 
0.0703457947666  ? -0.217620276847   ? -0.00690961456965 ? 0.0903154630508  ? -0.0514788222925  ? 
12 'X-RAY DIFFRACTION' ? refined 25.4398290385 -23.9100349828   18.4067120187 0.114493485098  ? 0.0119499943886   ? 
-0.0106912910734  ? 0.112282661274  ? 0.0107543612837    ? 0.0863221332506 ? 0.344095630984 ? 0.111858812627   ? -0.0633238925668  
? 0.806756365039 ? 0.294287174154  ? 2.05662683562 ? 0.0466622285778  ? -0.0714478947548 ? -0.0284808246446 ? 0.106720079844   ? 
-0.0311640829503 ? -0.043593165505   ? -0.0294920115842  ? 0.0449822721416  ? -0.0146225299679  ? 
13 'X-RAY DIFFRACTION' ? refined 26.3683869621 -26.5614857333   34.8847747992 0.254340462428  ? -0.0103079175779  ? 
-0.0250213895371  ? 0.196660336883  ? 0.00869973640429   ? 0.127380339723  ? 1.12785487198  ? 0.542533385079   ? 0.153715828281    
? 1.02268070732  ? 0.220177137823  ? 1.047426514   ? 0.0867255237309  ? -0.283535416197  ? -0.091982767823  ? 0.28522945065    ? 
-0.0623141081469 ? -0.105559946544   ? 0.230433557197    ? 0.182557172847   ? -0.0190522306557  ? 
# 
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 1   A 3   ? A 30  A 32  ? ? 
;chain 'A' and (resid 3 through 32 )
;
2  'X-RAY DIFFRACTION' 2  A 31  A 33  ? A 73  A 75  ? ? 
;chain 'A' and (resid 33 through 75 )
;
3  'X-RAY DIFFRACTION' 3  A 74  A 76  ? A 120 A 122 ? ? 
;chain 'A' and (resid 76 through 122 )
;
4  'X-RAY DIFFRACTION' 4  A 121 A 123 ? A 158 A 160 ? ? 
;chain 'A' and (resid 123 through 160 )
;
5  'X-RAY DIFFRACTION' 5  A 159 A 161 ? A 199 A 201 ? ? 
;chain 'A' and (resid 161 through 201 )
;
6  'X-RAY DIFFRACTION' 6  A 200 A 202 ? A 246 A 248 ? ? 
;chain 'A' and (resid 202 through 248 )
;
7  'X-RAY DIFFRACTION' 7  A 247 A 249 ? A 259 A 261 ? ? 
;chain 'A' and (resid 249 through 261 )
;
8  'X-RAY DIFFRACTION' 8  B 1   B 4   ? B 29  B 32  ? ? 
;chain 'B' and (resid 4 through 32 )
;
9  'X-RAY DIFFRACTION' 9  B 30  B 33  ? B 72  B 75  ? ? 
;chain 'B' and (resid 33 through 75 )
;
10 'X-RAY DIFFRACTION' 10 B 73  B 76  ? B 119 B 122 ? ? 
;chain 'B' and (resid 76 through 122 )
;
11 'X-RAY DIFFRACTION' 11 B 120 B 123 ? B 157 B 160 ? ? 
;chain 'B' and (resid 123 through 160 )
;
12 'X-RAY DIFFRACTION' 12 B 158 B 161 ? B 217 B 220 ? ? 
;chain 'B' and (resid 161 through 220 )
;
13 'X-RAY DIFFRACTION' 13 B 218 B 221 ? B 260 B 263 ? ? 
;chain 'B' and (resid 221 through 263 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 636 ? 7.12 . 
2 1 O ? B HOH 700 ? 6.00 . 
3 1 O ? B HOH 701 ? 6.04 . 
4 1 O ? B HOH 702 ? 6.06 . 
5 1 O ? B HOH 703 ? 7.00 . 
6 1 O ? B HOH 704 ? 8.22 . 
7 1 O ? B HOH 705 ? 8.76 . 
# 
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 SER -3  ? A SER 1   
2  1 Y 1 A ASN -2  ? A ASN 2   
3  1 Y 1 A ALA -1  ? A ALA 3   
4  1 Y 1 A MET 0   ? A MET 4   
5  1 Y 1 A ILE 1   ? A ILE 5   
6  1 Y 1 A PHE 2   ? A PHE 6   
7  1 Y 1 A PRO 262 ? A PRO 266 
8  1 Y 1 A PRO 263 ? A PRO 267 
9  1 Y 1 A SER 264 ? A SER 268 
10 1 Y 1 A SER 265 ? A SER 269 
11 1 Y 1 A GLN 266 ? A GLN 270 
12 1 Y 1 A PHE 267 ? A PHE 271 
13 1 Y 1 B SER -3  ? B SER 1   
14 1 Y 1 B ASN -2  ? B ASN 2   
15 1 Y 1 B ALA -1  ? B ALA 3   
16 1 Y 1 B MET 0   ? B MET 4   
17 1 Y 1 B ILE 1   ? B ILE 5   
18 1 Y 1 B PHE 2   ? B PHE 6   
19 1 Y 1 B PRO 3   ? B PRO 7   
20 1 Y 1 B SER 264 ? B SER 268 
21 1 Y 1 B SER 265 ? B SER 269 
22 1 Y 1 B GLN 266 ? B GLN 270 
23 1 Y 1 B PHE 267 ? B PHE 271 
# 
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 
A1BH4 C10  C  Y N 1   
A1BH4 C13  C  Y N 2   
A1BH4 C15  C  N N 3   
A1BH4 C01  C  N N 4   
A1BH4 C02  C  N N 5   
A1BH4 C03  C  Y N 6   
A1BH4 C04  C  Y N 7   
A1BH4 C05  C  Y N 8   
A1BH4 C06  C  Y N 9   
A1BH4 C07  C  Y N 10  
A1BH4 C08  C  N N 11  
A1BH4 C09  C  Y N 12  
A1BH4 C11  C  Y N 13  
A1BH4 C12  C  Y N 14  
A1BH4 O16  O  N N 15  
A1BH4 O17  O  N N 16  
A1BH4 S14  S  Y N 17  
A1BH4 H3   H  N N 18  
A1BH4 H2   H  N N 19  
A1BH4 H1   H  N N 20  
A1BH4 H5   H  N N 21  
A1BH4 H4   H  N N 22  
A1BH4 H6   H  N N 23  
A1BH4 H7   H  N N 24  
A1BH4 H8   H  N N 25  
A1BH4 H9   H  N N 26  
A1BH4 H11  H  N N 27  
A1BH4 H10  H  N N 28  
A1BH4 H12  H  N N 29  
A1BH4 H13  H  N N 30  
A1BH4 H14  H  N N 31  
ALA   N    N  N N 32  
ALA   CA   C  N S 33  
ALA   C    C  N N 34  
ALA   O    O  N N 35  
ALA   CB   C  N N 36  
ALA   OXT  O  N N 37  
ALA   H    H  N N 38  
ALA   H2   H  N N 39  
ALA   HA   H  N N 40  
ALA   HB1  H  N N 41  
ALA   HB2  H  N N 42  
ALA   HB3  H  N N 43  
ALA   HXT  H  N N 44  
ARG   N    N  N N 45  
ARG   CA   C  N S 46  
ARG   C    C  N N 47  
ARG   O    O  N N 48  
ARG   CB   C  N N 49  
ARG   CG   C  N N 50  
ARG   CD   C  N N 51  
ARG   NE   N  N N 52  
ARG   CZ   C  N N 53  
ARG   NH1  N  N N 54  
ARG   NH2  N  N N 55  
ARG   OXT  O  N N 56  
ARG   H    H  N N 57  
ARG   H2   H  N N 58  
ARG   HA   H  N N 59  
ARG   HB2  H  N N 60  
ARG   HB3  H  N N 61  
ARG   HG2  H  N N 62  
ARG   HG3  H  N N 63  
ARG   HD2  H  N N 64  
ARG   HD3  H  N N 65  
ARG   HE   H  N N 66  
ARG   HH11 H  N N 67  
ARG   HH12 H  N N 68  
ARG   HH21 H  N N 69  
ARG   HH22 H  N N 70  
ARG   HXT  H  N N 71  
ASN   N    N  N N 72  
ASN   CA   C  N S 73  
ASN   C    C  N N 74  
ASN   O    O  N N 75  
ASN   CB   C  N N 76  
ASN   CG   C  N N 77  
ASN   OD1  O  N N 78  
ASN   ND2  N  N N 79  
ASN   OXT  O  N N 80  
ASN   H    H  N N 81  
ASN   H2   H  N N 82  
ASN   HA   H  N N 83  
ASN   HB2  H  N N 84  
ASN   HB3  H  N N 85  
ASN   HD21 H  N N 86  
ASN   HD22 H  N N 87  
ASN   HXT  H  N N 88  
ASP   N    N  N N 89  
ASP   CA   C  N S 90  
ASP   C    C  N N 91  
ASP   O    O  N N 92  
ASP   CB   C  N N 93  
ASP   CG   C  N N 94  
ASP   OD1  O  N N 95  
ASP   OD2  O  N N 96  
ASP   OXT  O  N N 97  
ASP   H    H  N N 98  
ASP   H2   H  N N 99  
ASP   HA   H  N N 100 
ASP   HB2  H  N N 101 
ASP   HB3  H  N N 102 
ASP   HD2  H  N N 103 
ASP   HXT  H  N N 104 
CL    CL   CL N N 105 
CYS   N    N  N N 106 
CYS   CA   C  N R 107 
CYS   C    C  N N 108 
CYS   O    O  N N 109 
CYS   CB   C  N N 110 
CYS   SG   S  N N 111 
CYS   OXT  O  N N 112 
CYS   H    H  N N 113 
CYS   H2   H  N N 114 
CYS   HA   H  N N 115 
CYS   HB2  H  N N 116 
CYS   HB3  H  N N 117 
CYS   HG   H  N N 118 
CYS   HXT  H  N N 119 
GLN   N    N  N N 120 
GLN   CA   C  N S 121 
GLN   C    C  N N 122 
GLN   O    O  N N 123 
GLN   CB   C  N N 124 
GLN   CG   C  N N 125 
GLN   CD   C  N N 126 
GLN   OE1  O  N N 127 
GLN   NE2  N  N N 128 
GLN   OXT  O  N N 129 
GLN   H    H  N N 130 
GLN   H2   H  N N 131 
GLN   HA   H  N N 132 
GLN   HB2  H  N N 133 
GLN   HB3  H  N N 134 
GLN   HG2  H  N N 135 
GLN   HG3  H  N N 136 
GLN   HE21 H  N N 137 
GLN   HE22 H  N N 138 
GLN   HXT  H  N N 139 
GLU   N    N  N N 140 
GLU   CA   C  N S 141 
GLU   C    C  N N 142 
GLU   O    O  N N 143 
GLU   CB   C  N N 144 
GLU   CG   C  N N 145 
GLU   CD   C  N N 146 
GLU   OE1  O  N N 147 
GLU   OE2  O  N N 148 
GLU   OXT  O  N N 149 
GLU   H    H  N N 150 
GLU   H2   H  N N 151 
GLU   HA   H  N N 152 
GLU   HB2  H  N N 153 
GLU   HB3  H  N N 154 
GLU   HG2  H  N N 155 
GLU   HG3  H  N N 156 
GLU   HE2  H  N N 157 
GLU   HXT  H  N N 158 
GLY   N    N  N N 159 
GLY   CA   C  N N 160 
GLY   C    C  N N 161 
GLY   O    O  N N 162 
GLY   OXT  O  N N 163 
GLY   H    H  N N 164 
GLY   H2   H  N N 165 
GLY   HA2  H  N N 166 
GLY   HA3  H  N N 167 
GLY   HXT  H  N N 168 
HIS   N    N  N N 169 
HIS   CA   C  N S 170 
HIS   C    C  N N 171 
HIS   O    O  N N 172 
HIS   CB   C  N N 173 
HIS   CG   C  Y N 174 
HIS   ND1  N  Y N 175 
HIS   CD2  C  Y N 176 
HIS   CE1  C  Y N 177 
HIS   NE2  N  Y N 178 
HIS   OXT  O  N N 179 
HIS   H    H  N N 180 
HIS   H2   H  N N 181 
HIS   HA   H  N N 182 
HIS   HB2  H  N N 183 
HIS   HB3  H  N N 184 
HIS   HD1  H  N N 185 
HIS   HD2  H  N N 186 
HIS   HE1  H  N N 187 
HIS   HE2  H  N N 188 
HIS   HXT  H  N N 189 
HOH   O    O  N N 190 
HOH   H1   H  N N 191 
HOH   H2   H  N N 192 
ILE   N    N  N N 193 
ILE   CA   C  N S 194 
ILE   C    C  N N 195 
ILE   O    O  N N 196 
ILE   CB   C  N S 197 
ILE   CG1  C  N N 198 
ILE   CG2  C  N N 199 
ILE   CD1  C  N N 200 
ILE   OXT  O  N N 201 
ILE   H    H  N N 202 
ILE   H2   H  N N 203 
ILE   HA   H  N N 204 
ILE   HB   H  N N 205 
ILE   HG12 H  N N 206 
ILE   HG13 H  N N 207 
ILE   HG21 H  N N 208 
ILE   HG22 H  N N 209 
ILE   HG23 H  N N 210 
ILE   HD11 H  N N 211 
ILE   HD12 H  N N 212 
ILE   HD13 H  N N 213 
ILE   HXT  H  N N 214 
LEU   N    N  N N 215 
LEU   CA   C  N S 216 
LEU   C    C  N N 217 
LEU   O    O  N N 218 
LEU   CB   C  N N 219 
LEU   CG   C  N N 220 
LEU   CD1  C  N N 221 
LEU   CD2  C  N N 222 
LEU   OXT  O  N N 223 
LEU   H    H  N N 224 
LEU   H2   H  N N 225 
LEU   HA   H  N N 226 
LEU   HB2  H  N N 227 
LEU   HB3  H  N N 228 
LEU   HG   H  N N 229 
LEU   HD11 H  N N 230 
LEU   HD12 H  N N 231 
LEU   HD13 H  N N 232 
LEU   HD21 H  N N 233 
LEU   HD22 H  N N 234 
LEU   HD23 H  N N 235 
LEU   HXT  H  N N 236 
LYS   N    N  N N 237 
LYS   CA   C  N S 238 
LYS   C    C  N N 239 
LYS   O    O  N N 240 
LYS   CB   C  N N 241 
LYS   CG   C  N N 242 
LYS   CD   C  N N 243 
LYS   CE   C  N N 244 
LYS   NZ   N  N N 245 
LYS   OXT  O  N N 246 
LYS   H    H  N N 247 
LYS   H2   H  N N 248 
LYS   HA   H  N N 249 
LYS   HB2  H  N N 250 
LYS   HB3  H  N N 251 
LYS   HG2  H  N N 252 
LYS   HG3  H  N N 253 
LYS   HD2  H  N N 254 
LYS   HD3  H  N N 255 
LYS   HE2  H  N N 256 
LYS   HE3  H  N N 257 
LYS   HZ1  H  N N 258 
LYS   HZ2  H  N N 259 
LYS   HZ3  H  N N 260 
LYS   HXT  H  N N 261 
MET   N    N  N N 262 
MET   CA   C  N S 263 
MET   C    C  N N 264 
MET   O    O  N N 265 
MET   CB   C  N N 266 
MET   CG   C  N N 267 
MET   SD   S  N N 268 
MET   CE   C  N N 269 
MET   OXT  O  N N 270 
MET   H    H  N N 271 
MET   H2   H  N N 272 
MET   HA   H  N N 273 
MET   HB2  H  N N 274 
MET   HB3  H  N N 275 
MET   HG2  H  N N 276 
MET   HG3  H  N N 277 
MET   HE1  H  N N 278 
MET   HE2  H  N N 279 
MET   HE3  H  N N 280 
MET   HXT  H  N N 281 
PHE   N    N  N N 282 
PHE   CA   C  N S 283 
PHE   C    C  N N 284 
PHE   O    O  N N 285 
PHE   CB   C  N N 286 
PHE   CG   C  Y N 287 
PHE   CD1  C  Y N 288 
PHE   CD2  C  Y N 289 
PHE   CE1  C  Y N 290 
PHE   CE2  C  Y N 291 
PHE   CZ   C  Y N 292 
PHE   OXT  O  N N 293 
PHE   H    H  N N 294 
PHE   H2   H  N N 295 
PHE   HA   H  N N 296 
PHE   HB2  H  N N 297 
PHE   HB3  H  N N 298 
PHE   HD1  H  N N 299 
PHE   HD2  H  N N 300 
PHE   HE1  H  N N 301 
PHE   HE2  H  N N 302 
PHE   HZ   H  N N 303 
PHE   HXT  H  N N 304 
PRO   N    N  N N 305 
PRO   CA   C  N S 306 
PRO   C    C  N N 307 
PRO   O    O  N N 308 
PRO   CB   C  N N 309 
PRO   CG   C  N N 310 
PRO   CD   C  N N 311 
PRO   OXT  O  N N 312 
PRO   H    H  N N 313 
PRO   HA   H  N N 314 
PRO   HB2  H  N N 315 
PRO   HB3  H  N N 316 
PRO   HG2  H  N N 317 
PRO   HG3  H  N N 318 
PRO   HD2  H  N N 319 
PRO   HD3  H  N N 320 
PRO   HXT  H  N N 321 
SER   N    N  N N 322 
SER   CA   C  N S 323 
SER   C    C  N N 324 
SER   O    O  N N 325 
SER   CB   C  N N 326 
SER   OG   O  N N 327 
SER   OXT  O  N N 328 
SER   H    H  N N 329 
SER   H2   H  N N 330 
SER   HA   H  N N 331 
SER   HB2  H  N N 332 
SER   HB3  H  N N 333 
SER   HG   H  N N 334 
SER   HXT  H  N N 335 
THR   N    N  N N 336 
THR   CA   C  N S 337 
THR   C    C  N N 338 
THR   O    O  N N 339 
THR   CB   C  N R 340 
THR   OG1  O  N N 341 
THR   CG2  C  N N 342 
THR   OXT  O  N N 343 
THR   H    H  N N 344 
THR   H2   H  N N 345 
THR   HA   H  N N 346 
THR   HB   H  N N 347 
THR   HG1  H  N N 348 
THR   HG21 H  N N 349 
THR   HG22 H  N N 350 
THR   HG23 H  N N 351 
THR   HXT  H  N N 352 
TRP   N    N  N N 353 
TRP   CA   C  N S 354 
TRP   C    C  N N 355 
TRP   O    O  N N 356 
TRP   CB   C  N N 357 
TRP   CG   C  Y N 358 
TRP   CD1  C  Y N 359 
TRP   CD2  C  Y N 360 
TRP   NE1  N  Y N 361 
TRP   CE2  C  Y N 362 
TRP   CE3  C  Y N 363 
TRP   CZ2  C  Y N 364 
TRP   CZ3  C  Y N 365 
TRP   CH2  C  Y N 366 
TRP   OXT  O  N N 367 
TRP   H    H  N N 368 
TRP   H2   H  N N 369 
TRP   HA   H  N N 370 
TRP   HB2  H  N N 371 
TRP   HB3  H  N N 372 
TRP   HD1  H  N N 373 
TRP   HE1  H  N N 374 
TRP   HE3  H  N N 375 
TRP   HZ2  H  N N 376 
TRP   HZ3  H  N N 377 
TRP   HH2  H  N N 378 
TRP   HXT  H  N N 379 
TYR   N    N  N N 380 
TYR   CA   C  N S 381 
TYR   C    C  N N 382 
TYR   O    O  N N 383 
TYR   CB   C  N N 384 
TYR   CG   C  Y N 385 
TYR   CD1  C  Y N 386 
TYR   CD2  C  Y N 387 
TYR   CE1  C  Y N 388 
TYR   CE2  C  Y N 389 
TYR   CZ   C  Y N 390 
TYR   OH   O  N N 391 
TYR   OXT  O  N N 392 
TYR   H    H  N N 393 
TYR   H2   H  N N 394 
TYR   HA   H  N N 395 
TYR   HB2  H  N N 396 
TYR   HB3  H  N N 397 
TYR   HD1  H  N N 398 
TYR   HD2  H  N N 399 
TYR   HE1  H  N N 400 
TYR   HE2  H  N N 401 
TYR   HH   H  N N 402 
TYR   HXT  H  N N 403 
VAL   N    N  N N 404 
VAL   CA   C  N S 405 
VAL   C    C  N N 406 
VAL   O    O  N N 407 
VAL   CB   C  N N 408 
VAL   CG1  C  N N 409 
VAL   CG2  C  N N 410 
VAL   OXT  O  N N 411 
VAL   H    H  N N 412 
VAL   H2   H  N N 413 
VAL   HA   H  N N 414 
VAL   HB   H  N N 415 
VAL   HG11 H  N N 416 
VAL   HG12 H  N N 417 
VAL   HG13 H  N N 418 
VAL   HG21 H  N N 419 
VAL   HG22 H  N N 420 
VAL   HG23 H  N N 421 
VAL   HXT  H  N N 422 
# 
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 
A1BH4 C02 C01  sing N N 1   
A1BH4 C03 C02  sing N N 2   
A1BH4 C04 C03  doub Y N 3   
A1BH4 C05 C04  sing Y N 4   
A1BH4 C06 C05  doub Y N 5   
A1BH4 C07 C06  sing Y N 6   
A1BH4 C08 C07  sing N N 7   
A1BH4 C09 C07  doub Y N 8   
A1BH4 C10 C09  sing N N 9   
A1BH4 C11 C10  doub Y N 10  
A1BH4 C12 C11  sing Y N 11  
A1BH4 C13 C12  doub Y N 12  
A1BH4 S14 C13  sing Y N 13  
A1BH4 C15 C13  sing N N 14  
A1BH4 O16 C15  sing N N 15  
A1BH4 O17 C15  doub N N 16  
A1BH4 C03 C09  sing Y N 17  
A1BH4 C10 S14  sing Y N 18  
A1BH4 C01 H3   sing N N 19  
A1BH4 C01 H2   sing N N 20  
A1BH4 C01 H1   sing N N 21  
A1BH4 C02 H5   sing N N 22  
A1BH4 C02 H4   sing N N 23  
A1BH4 C04 H6   sing N N 24  
A1BH4 C05 H7   sing N N 25  
A1BH4 C06 H8   sing N N 26  
A1BH4 C08 H9   sing N N 27  
A1BH4 C08 H11  sing N N 28  
A1BH4 C08 H10  sing N N 29  
A1BH4 C11 H12  sing N N 30  
A1BH4 C12 H13  sing N N 31  
A1BH4 O16 H14  sing N N 32  
ALA   N   CA   sing N N 33  
ALA   N   H    sing N N 34  
ALA   N   H2   sing N N 35  
ALA   CA  C    sing N N 36  
ALA   CA  CB   sing N N 37  
ALA   CA  HA   sing N N 38  
ALA   C   O    doub N N 39  
ALA   C   OXT  sing N N 40  
ALA   CB  HB1  sing N N 41  
ALA   CB  HB2  sing N N 42  
ALA   CB  HB3  sing N N 43  
ALA   OXT HXT  sing N N 44  
ARG   N   CA   sing N N 45  
ARG   N   H    sing N N 46  
ARG   N   H2   sing N N 47  
ARG   CA  C    sing N N 48  
ARG   CA  CB   sing N N 49  
ARG   CA  HA   sing N N 50  
ARG   C   O    doub N N 51  
ARG   C   OXT  sing N N 52  
ARG   CB  CG   sing N N 53  
ARG   CB  HB2  sing N N 54  
ARG   CB  HB3  sing N N 55  
ARG   CG  CD   sing N N 56  
ARG   CG  HG2  sing N N 57  
ARG   CG  HG3  sing N N 58  
ARG   CD  NE   sing N N 59  
ARG   CD  HD2  sing N N 60  
ARG   CD  HD3  sing N N 61  
ARG   NE  CZ   sing N N 62  
ARG   NE  HE   sing N N 63  
ARG   CZ  NH1  sing N N 64  
ARG   CZ  NH2  doub N N 65  
ARG   NH1 HH11 sing N N 66  
ARG   NH1 HH12 sing N N 67  
ARG   NH2 HH21 sing N N 68  
ARG   NH2 HH22 sing N N 69  
ARG   OXT HXT  sing N N 70  
ASN   N   CA   sing N N 71  
ASN   N   H    sing N N 72  
ASN   N   H2   sing N N 73  
ASN   CA  C    sing N N 74  
ASN   CA  CB   sing N N 75  
ASN   CA  HA   sing N N 76  
ASN   C   O    doub N N 77  
ASN   C   OXT  sing N N 78  
ASN   CB  CG   sing N N 79  
ASN   CB  HB2  sing N N 80  
ASN   CB  HB3  sing N N 81  
ASN   CG  OD1  doub N N 82  
ASN   CG  ND2  sing N N 83  
ASN   ND2 HD21 sing N N 84  
ASN   ND2 HD22 sing N N 85  
ASN   OXT HXT  sing N N 86  
ASP   N   CA   sing N N 87  
ASP   N   H    sing N N 88  
ASP   N   H2   sing N N 89  
ASP   CA  C    sing N N 90  
ASP   CA  CB   sing N N 91  
ASP   CA  HA   sing N N 92  
ASP   C   O    doub N N 93  
ASP   C   OXT  sing N N 94  
ASP   CB  CG   sing N N 95  
ASP   CB  HB2  sing N N 96  
ASP   CB  HB3  sing N N 97  
ASP   CG  OD1  doub N N 98  
ASP   CG  OD2  sing N N 99  
ASP   OD2 HD2  sing N N 100 
ASP   OXT HXT  sing N N 101 
CYS   N   CA   sing N N 102 
CYS   N   H    sing N N 103 
CYS   N   H2   sing N N 104 
CYS   CA  C    sing N N 105 
CYS   CA  CB   sing N N 106 
CYS   CA  HA   sing N N 107 
CYS   C   O    doub N N 108 
CYS   C   OXT  sing N N 109 
CYS   CB  SG   sing N N 110 
CYS   CB  HB2  sing N N 111 
CYS   CB  HB3  sing N N 112 
CYS   SG  HG   sing N N 113 
CYS   OXT HXT  sing N N 114 
GLN   N   CA   sing N N 115 
GLN   N   H    sing N N 116 
GLN   N   H2   sing N N 117 
GLN   CA  C    sing N N 118 
GLN   CA  CB   sing N N 119 
GLN   CA  HA   sing N N 120 
GLN   C   O    doub N N 121 
GLN   C   OXT  sing N N 122 
GLN   CB  CG   sing N N 123 
GLN   CB  HB2  sing N N 124 
GLN   CB  HB3  sing N N 125 
GLN   CG  CD   sing N N 126 
GLN   CG  HG2  sing N N 127 
GLN   CG  HG3  sing N N 128 
GLN   CD  OE1  doub N N 129 
GLN   CD  NE2  sing N N 130 
GLN   NE2 HE21 sing N N 131 
GLN   NE2 HE22 sing N N 132 
GLN   OXT HXT  sing N N 133 
GLU   N   CA   sing N N 134 
GLU   N   H    sing N N 135 
GLU   N   H2   sing N N 136 
GLU   CA  C    sing N N 137 
GLU   CA  CB   sing N N 138 
GLU   CA  HA   sing N N 139 
GLU   C   O    doub N N 140 
GLU   C   OXT  sing N N 141 
GLU   CB  CG   sing N N 142 
GLU   CB  HB2  sing N N 143 
GLU   CB  HB3  sing N N 144 
GLU   CG  CD   sing N N 145 
GLU   CG  HG2  sing N N 146 
GLU   CG  HG3  sing N N 147 
GLU   CD  OE1  doub N N 148 
GLU   CD  OE2  sing N N 149 
GLU   OE2 HE2  sing N N 150 
GLU   OXT HXT  sing N N 151 
GLY   N   CA   sing N N 152 
GLY   N   H    sing N N 153 
GLY   N   H2   sing N N 154 
GLY   CA  C    sing N N 155 
GLY   CA  HA2  sing N N 156 
GLY   CA  HA3  sing N N 157 
GLY   C   O    doub N N 158 
GLY   C   OXT  sing N N 159 
GLY   OXT HXT  sing N N 160 
HIS   N   CA   sing N N 161 
HIS   N   H    sing N N 162 
HIS   N   H2   sing N N 163 
HIS   CA  C    sing N N 164 
HIS   CA  CB   sing N N 165 
HIS   CA  HA   sing N N 166 
HIS   C   O    doub N N 167 
HIS   C   OXT  sing N N 168 
HIS   CB  CG   sing N N 169 
HIS   CB  HB2  sing N N 170 
HIS   CB  HB3  sing N N 171 
HIS   CG  ND1  sing Y N 172 
HIS   CG  CD2  doub Y N 173 
HIS   ND1 CE1  doub Y N 174 
HIS   ND1 HD1  sing N N 175 
HIS   CD2 NE2  sing Y N 176 
HIS   CD2 HD2  sing N N 177 
HIS   CE1 NE2  sing Y N 178 
HIS   CE1 HE1  sing N N 179 
HIS   NE2 HE2  sing N N 180 
HIS   OXT HXT  sing N N 181 
HOH   O   H1   sing N N 182 
HOH   O   H2   sing N N 183 
ILE   N   CA   sing N N 184 
ILE   N   H    sing N N 185 
ILE   N   H2   sing N N 186 
ILE   CA  C    sing N N 187 
ILE   CA  CB   sing N N 188 
ILE   CA  HA   sing N N 189 
ILE   C   O    doub N N 190 
ILE   C   OXT  sing N N 191 
ILE   CB  CG1  sing N N 192 
ILE   CB  CG2  sing N N 193 
ILE   CB  HB   sing N N 194 
ILE   CG1 CD1  sing N N 195 
ILE   CG1 HG12 sing N N 196 
ILE   CG1 HG13 sing N N 197 
ILE   CG2 HG21 sing N N 198 
ILE   CG2 HG22 sing N N 199 
ILE   CG2 HG23 sing N N 200 
ILE   CD1 HD11 sing N N 201 
ILE   CD1 HD12 sing N N 202 
ILE   CD1 HD13 sing N N 203 
ILE   OXT HXT  sing N N 204 
LEU   N   CA   sing N N 205 
LEU   N   H    sing N N 206 
LEU   N   H2   sing N N 207 
LEU   CA  C    sing N N 208 
LEU   CA  CB   sing N N 209 
LEU   CA  HA   sing N N 210 
LEU   C   O    doub N N 211 
LEU   C   OXT  sing N N 212 
LEU   CB  CG   sing N N 213 
LEU   CB  HB2  sing N N 214 
LEU   CB  HB3  sing N N 215 
LEU   CG  CD1  sing N N 216 
LEU   CG  CD2  sing N N 217 
LEU   CG  HG   sing N N 218 
LEU   CD1 HD11 sing N N 219 
LEU   CD1 HD12 sing N N 220 
LEU   CD1 HD13 sing N N 221 
LEU   CD2 HD21 sing N N 222 
LEU   CD2 HD22 sing N N 223 
LEU   CD2 HD23 sing N N 224 
LEU   OXT HXT  sing N N 225 
LYS   N   CA   sing N N 226 
LYS   N   H    sing N N 227 
LYS   N   H2   sing N N 228 
LYS   CA  C    sing N N 229 
LYS   CA  CB   sing N N 230 
LYS   CA  HA   sing N N 231 
LYS   C   O    doub N N 232 
LYS   C   OXT  sing N N 233 
LYS   CB  CG   sing N N 234 
LYS   CB  HB2  sing N N 235 
LYS   CB  HB3  sing N N 236 
LYS   CG  CD   sing N N 237 
LYS   CG  HG2  sing N N 238 
LYS   CG  HG3  sing N N 239 
LYS   CD  CE   sing N N 240 
LYS   CD  HD2  sing N N 241 
LYS   CD  HD3  sing N N 242 
LYS   CE  NZ   sing N N 243 
LYS   CE  HE2  sing N N 244 
LYS   CE  HE3  sing N N 245 
LYS   NZ  HZ1  sing N N 246 
LYS   NZ  HZ2  sing N N 247 
LYS   NZ  HZ3  sing N N 248 
LYS   OXT HXT  sing N N 249 
MET   N   CA   sing N N 250 
MET   N   H    sing N N 251 
MET   N   H2   sing N N 252 
MET   CA  C    sing N N 253 
MET   CA  CB   sing N N 254 
MET   CA  HA   sing N N 255 
MET   C   O    doub N N 256 
MET   C   OXT  sing N N 257 
MET   CB  CG   sing N N 258 
MET   CB  HB2  sing N N 259 
MET   CB  HB3  sing N N 260 
MET   CG  SD   sing N N 261 
MET   CG  HG2  sing N N 262 
MET   CG  HG3  sing N N 263 
MET   SD  CE   sing N N 264 
MET   CE  HE1  sing N N 265 
MET   CE  HE2  sing N N 266 
MET   CE  HE3  sing N N 267 
MET   OXT HXT  sing N N 268 
PHE   N   CA   sing N N 269 
PHE   N   H    sing N N 270 
PHE   N   H2   sing N N 271 
PHE   CA  C    sing N N 272 
PHE   CA  CB   sing N N 273 
PHE   CA  HA   sing N N 274 
PHE   C   O    doub N N 275 
PHE   C   OXT  sing N N 276 
PHE   CB  CG   sing N N 277 
PHE   CB  HB2  sing N N 278 
PHE   CB  HB3  sing N N 279 
PHE   CG  CD1  doub Y N 280 
PHE   CG  CD2  sing Y N 281 
PHE   CD1 CE1  sing Y N 282 
PHE   CD1 HD1  sing N N 283 
PHE   CD2 CE2  doub Y N 284 
PHE   CD2 HD2  sing N N 285 
PHE   CE1 CZ   doub Y N 286 
PHE   CE1 HE1  sing N N 287 
PHE   CE2 CZ   sing Y N 288 
PHE   CE2 HE2  sing N N 289 
PHE   CZ  HZ   sing N N 290 
PHE   OXT HXT  sing N N 291 
PRO   N   CA   sing N N 292 
PRO   N   CD   sing N N 293 
PRO   N   H    sing N N 294 
PRO   CA  C    sing N N 295 
PRO   CA  CB   sing N N 296 
PRO   CA  HA   sing N N 297 
PRO   C   O    doub N N 298 
PRO   C   OXT  sing N N 299 
PRO   CB  CG   sing N N 300 
PRO   CB  HB2  sing N N 301 
PRO   CB  HB3  sing N N 302 
PRO   CG  CD   sing N N 303 
PRO   CG  HG2  sing N N 304 
PRO   CG  HG3  sing N N 305 
PRO   CD  HD2  sing N N 306 
PRO   CD  HD3  sing N N 307 
PRO   OXT HXT  sing N N 308 
SER   N   CA   sing N N 309 
SER   N   H    sing N N 310 
SER   N   H2   sing N N 311 
SER   CA  C    sing N N 312 
SER   CA  CB   sing N N 313 
SER   CA  HA   sing N N 314 
SER   C   O    doub N N 315 
SER   C   OXT  sing N N 316 
SER   CB  OG   sing N N 317 
SER   CB  HB2  sing N N 318 
SER   CB  HB3  sing N N 319 
SER   OG  HG   sing N N 320 
SER   OXT HXT  sing N N 321 
THR   N   CA   sing N N 322 
THR   N   H    sing N N 323 
THR   N   H2   sing N N 324 
THR   CA  C    sing N N 325 
THR   CA  CB   sing N N 326 
THR   CA  HA   sing N N 327 
THR   C   O    doub N N 328 
THR   C   OXT  sing N N 329 
THR   CB  OG1  sing N N 330 
THR   CB  CG2  sing N N 331 
THR   CB  HB   sing N N 332 
THR   OG1 HG1  sing N N 333 
THR   CG2 HG21 sing N N 334 
THR   CG2 HG22 sing N N 335 
THR   CG2 HG23 sing N N 336 
THR   OXT HXT  sing N N 337 
TRP   N   CA   sing N N 338 
TRP   N   H    sing N N 339 
TRP   N   H2   sing N N 340 
TRP   CA  C    sing N N 341 
TRP   CA  CB   sing N N 342 
TRP   CA  HA   sing N N 343 
TRP   C   O    doub N N 344 
TRP   C   OXT  sing N N 345 
TRP   CB  CG   sing N N 346 
TRP   CB  HB2  sing N N 347 
TRP   CB  HB3  sing N N 348 
TRP   CG  CD1  doub Y N 349 
TRP   CG  CD2  sing Y N 350 
TRP   CD1 NE1  sing Y N 351 
TRP   CD1 HD1  sing N N 352 
TRP   CD2 CE2  doub Y N 353 
TRP   CD2 CE3  sing Y N 354 
TRP   NE1 CE2  sing Y N 355 
TRP   NE1 HE1  sing N N 356 
TRP   CE2 CZ2  sing Y N 357 
TRP   CE3 CZ3  doub Y N 358 
TRP   CE3 HE3  sing N N 359 
TRP   CZ2 CH2  doub Y N 360 
TRP   CZ2 HZ2  sing N N 361 
TRP   CZ3 CH2  sing Y N 362 
TRP   CZ3 HZ3  sing N N 363 
TRP   CH2 HH2  sing N N 364 
TRP   OXT HXT  sing N N 365 
TYR   N   CA   sing N N 366 
TYR   N   H    sing N N 367 
TYR   N   H2   sing N N 368 
TYR   CA  C    sing N N 369 
TYR   CA  CB   sing N N 370 
TYR   CA  HA   sing N N 371 
TYR   C   O    doub N N 372 
TYR   C   OXT  sing N N 373 
TYR   CB  CG   sing N N 374 
TYR   CB  HB2  sing N N 375 
TYR   CB  HB3  sing N N 376 
TYR   CG  CD1  doub Y N 377 
TYR   CG  CD2  sing Y N 378 
TYR   CD1 CE1  sing Y N 379 
TYR   CD1 HD1  sing N N 380 
TYR   CD2 CE2  doub Y N 381 
TYR   CD2 HD2  sing N N 382 
TYR   CE1 CZ   doub Y N 383 
TYR   CE1 HE1  sing N N 384 
TYR   CE2 CZ   sing Y N 385 
TYR   CE2 HE2  sing N N 386 
TYR   CZ  OH   sing N N 387 
TYR   OH  HH   sing N N 388 
TYR   OXT HXT  sing N N 389 
VAL   N   CA   sing N N 390 
VAL   N   H    sing N N 391 
VAL   N   H2   sing N N 392 
VAL   CA  C    sing N N 393 
VAL   CA  CB   sing N N 394 
VAL   CA  HA   sing N N 395 
VAL   C   O    doub N N 396 
VAL   C   OXT  sing N N 397 
VAL   CB  CG1  sing N N 398 
VAL   CB  CG2  sing N N 399 
VAL   CB  HB   sing N N 400 
VAL   CG1 HG11 sing N N 401 
VAL   CG1 HG12 sing N N 402 
VAL   CG1 HG13 sing N N 403 
VAL   CG2 HG21 sing N N 404 
VAL   CG2 HG22 sing N N 405 
VAL   CG2 HG23 sing N N 406 
VAL   OXT HXT  sing N N 407 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           AI072425 
_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   1RTC 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9E3T 
_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]   0.025735 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001908 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017401 
_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]   0.008028 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . PRO   A 1 7   ? -5.01891 10.53704  54.96318  1.000 41.16193 ? 3   PRO   A N   1 
ATOM   2    C  CA  . PRO   A 1 7   ? -3.86587 9.68615   54.65466  1.000 34.63848 ? 3   PRO   A CA  1 
ATOM   3    C  C   . PRO   A 1 7   ? -4.08346 8.83443   53.41098  1.000 29.90425 ? 3   PRO   A C   1 
ATOM   4    O  O   . PRO   A 1 7   ? -4.84505 7.86809   53.45744  1.000 24.72858 ? 3   PRO   A O   1 
ATOM   5    C  CB  . PRO   A 1 7   ? -3.73984 8.80666   55.90214  1.000 34.14025 ? 3   PRO   A CB  1 
ATOM   6    C  CG  . PRO   A 1 7   ? -5.11809 8.82978   56.55153  1.000 41.30258 ? 3   PRO   A CG  1 
ATOM   7    C  CD  . PRO   A 1 7   ? -5.97534 9.85147   55.84478  1.000 21.87152 ? 3   PRO   A CD  1 
ATOM   8    N  N   . LYS   A 1 8   ? -3.41780 9.19451   52.31523  1.000 24.29497 ? 4   LYS   A N   1 
ATOM   9    C  CA  . LYS   A 1 8   ? -3.59875 8.47097   51.06545  1.000 21.69294 ? 4   LYS   A CA  1 
ATOM   10   C  C   . LYS   A 1 8   ? -3.15554 7.02087   51.21411  1.000 20.22007 ? 4   LYS   A C   1 
ATOM   11   O  O   . LYS   A 1 8   ? -2.14797 6.72192   51.86172  1.000 21.31569 ? 4   LYS   A O   1 
ATOM   12   C  CB  . LYS   A 1 8   ? -2.82326 9.15592   49.94252  1.000 22.03264 ? 4   LYS   A CB  1 
ATOM   13   C  CG  . LYS   A 1 8   ? -3.40684 10.50793  49.55295  1.000 29.66401 ? 4   LYS   A CG  1 
ATOM   14   C  CD  . LYS   A 1 8   ? -2.77786 11.05649  48.28384  1.000 27.08759 ? 4   LYS   A CD  1 
ATOM   15   C  CE  . LYS   A 1 8   ? -3.54451 12.27172  47.78965  1.000 25.38801 ? 4   LYS   A CE  1 
ATOM   16   N  NZ  . LYS   A 1 8   ? -3.61885 13.31719  48.83968  1.000 33.83110 ? 4   LYS   A NZ  1 
ATOM   17   N  N   . GLN   A 1 9   ? -3.92394 6.11904   50.61241  1.000 16.41131 ? 5   GLN   A N   1 
ATOM   18   C  CA  . GLN   A 1 9   ? -3.68280 4.68503   50.70409  1.000 15.71115 ? 5   GLN   A CA  1 
ATOM   19   C  C   . GLN   A 1 9   ? -2.95283 4.20828   49.45453  1.000 17.23026 ? 5   GLN   A C   1 
ATOM   20   O  O   . GLN   A 1 9   ? -3.42957 4.41354   48.33234  1.000 17.30421 ? 5   GLN   A O   1 
ATOM   21   C  CB  . GLN   A 1 9   ? -4.99859 3.93154   50.88120  1.000 16.35044 ? 5   GLN   A CB  1 
ATOM   22   C  CG  . GLN   A 1 9   ? -5.69253 4.25554   52.18164  1.000 17.27893 ? 5   GLN   A CG  1 
ATOM   23   C  CD  . GLN   A 1 9   ? -4.79614 3.99083   53.37049  1.000 24.35127 ? 5   GLN   A CD  1 
ATOM   24   O  OE1 . GLN   A 1 9   ? -4.37876 2.85705   53.60345  1.000 36.32554 ? 5   GLN   A OE1 1 
ATOM   25   N  NE2 . GLN   A 1 9   ? -4.47390 5.04069   54.11647  1.000 40.51067 ? 5   GLN   A NE2 1 
ATOM   26   N  N   . TYR   A 1 10  ? -1.80138 3.57752   49.65300  1.000 14.18146 ? 6   TYR   A N   1 
ATOM   27   C  CA  . TYR   A 1 10  ? -1.01075 3.02679   48.56891  1.000 13.40346 ? 6   TYR   A CA  1 
ATOM   28   C  C   . TYR   A 1 10  ? -0.93400 1.50821   48.68713  1.000 12.99453 ? 6   TYR   A C   1 
ATOM   29   O  O   . TYR   A 1 10  ? -1.06220 0.96292   49.78780  1.000 13.07324 ? 6   TYR   A O   1 
ATOM   30   C  CB  . TYR   A 1 10  ? 0.39976  3.62662   48.57400  1.000 12.95361 ? 6   TYR   A CB  1 
ATOM   31   C  CG  . TYR   A 1 10  ? 0.41063  5.11175   48.29267  1.000 13.45410 ? 6   TYR   A CG  1 
ATOM   32   C  CD1 . TYR   A 1 10  ? 0.17369  5.59507   47.01052  1.000 13.90350 ? 6   TYR   A CD1 1 
ATOM   33   C  CD2 . TYR   A 1 10  ? 0.65290  6.03240   49.30679  1.000 13.82330 ? 6   TYR   A CD2 1 
ATOM   34   C  CE1 . TYR   A 1 10  ? 0.17829  6.94831   46.74551  1.000 14.33046 ? 6   TYR   A CE1 1 
ATOM   35   C  CE2 . TYR   A 1 10  ? 0.66087  7.39224   49.04952  1.000 14.41129 ? 6   TYR   A CE2 1 
ATOM   36   C  CZ  . TYR   A 1 10  ? 0.42479  7.84297   47.76583  1.000 16.85134 ? 6   TYR   A CZ  1 
ATOM   37   O  OH  . TYR   A 1 10  ? 0.42975  9.19265   47.50040  1.000 16.08669 ? 6   TYR   A OH  1 
ATOM   38   N  N   . PRO   A 1 11  ? -0.74271 0.79771   47.57379  1.000 12.70451 ? 7   PRO   A N   1 
ATOM   39   C  CA  . PRO   A 1 11  ? -0.67651 -0.66780  47.63980  1.000 13.72014 ? 7   PRO   A CA  1 
ATOM   40   C  C   . PRO   A 1 11  ? 0.45814  -1.12612  48.54138  1.000 18.18327 ? 7   PRO   A C   1 
ATOM   41   O  O   . PRO   A 1 11  ? 1.49581  -0.47014  48.64816  1.000 11.63679 ? 7   PRO   A O   1 
ATOM   42   C  CB  . PRO   A 1 11  ? -0.42898 -1.08194  46.18391  1.000 17.04847 ? 7   PRO   A CB  1 
ATOM   43   C  CG  . PRO   A 1 11  ? -0.88231 0.08127   45.36789  1.000 15.08909 ? 7   PRO   A CG  1 
ATOM   44   C  CD  . PRO   A 1 11  ? -0.61960 1.29863   46.19348  1.000 12.77123 ? 7   PRO   A CD  1 
ATOM   45   N  N   . ILE   A 1 12  ? 0.25458  -2.26935  49.19597  1.000 16.06908 ? 8   ILE   A N   1 
ATOM   46   C  CA  . ILE   A 1 12  ? 1.22746  -2.79762  50.14388  1.000 14.51097 ? 8   ILE   A CA  1 
ATOM   47   C  C   . ILE   A 1 12  ? 1.54327  -4.24559  49.78861  1.000 11.62278 ? 8   ILE   A C   1 
ATOM   48   O  O   . ILE   A 1 12  ? 0.63713  -5.03287  49.49536  1.000 13.64699 ? 8   ILE   A O   1 
ATOM   49   C  CB  . ILE   A 1 12  ? 0.73010  -2.67933  51.59902  1.000 24.72923 ? 8   ILE   A CB  1 
ATOM   50   C  CG1 . ILE   A 1 12  ? 1.74952  -3.28667  52.56443  1.000 21.93073 ? 8   ILE   A CG1 1 
ATOM   51   C  CG2 . ILE   A 1 12  ? -0.63205 -3.32519  51.76437  1.000 22.86077 ? 8   ILE   A CG2 1 
ATOM   52   C  CD1 . ILE   A 1 12  ? 1.48651  -2.95230  54.01792  1.000 49.08817 ? 8   ILE   A CD1 1 
ATOM   53   N  N   . ILE   A 1 13  ? 2.83074  -4.58480  49.79312  1.000 14.97997 ? 9   ILE   A N   1 
ATOM   54   C  CA  . ILE   A 1 13  ? 3.30860  -5.94351  49.56090  1.000 14.78405 ? 9   ILE   A CA  1 
ATOM   55   C  C   . ILE   A 1 13  ? 4.08300  -6.38313  50.79449  1.000 14.31009 ? 9   ILE   A C   1 
ATOM   56   O  O   . ILE   A 1 13  ? 4.97726  -5.66551  51.25263  1.000 14.13935 ? 9   ILE   A O   1 
ATOM   57   C  CB  . ILE   A 1 13  ? 4.19896  -6.03832  48.30809  1.000 14.99105 ? 9   ILE   A CB  1 
ATOM   58   C  CG1 . ILE   A 1 13  ? 3.48158  -5.47216  47.07741  1.000 16.40424 ? 9   ILE   A CG1 1 
ATOM   59   C  CG2 . ILE   A 1 13  ? 4.61438  -7.48311  48.06655  1.000 15.31224 ? 9   ILE   A CG2 1 
ATOM   60   C  CD1 . ILE   A 1 13  ? 3.74660  -4.00026  46.83759  1.000 24.03987 ? 9   ILE   A CD1 1 
ATOM   61   N  N   . ASN   A 1 14  ? 3.75163  -7.56005  51.31865  1.000 15.46632 ? 10  ASN   A N   1 
ATOM   62   C  CA  . ASN   A 1 14  ? 4.34901  -8.07052  52.54841  1.000 12.15630 ? 10  ASN   A CA  1 
ATOM   63   C  C   . ASN   A 1 14  ? 5.42278  -9.10818  52.24570  1.000 19.09850 ? 10  ASN   A C   1 
ATOM   64   O  O   . ASN   A 1 14  ? 5.23817  -9.97860  51.39096  1.000 16.21448 ? 10  ASN   A O   1 
ATOM   65   C  CB  . ASN   A 1 14  ? 3.28423  -8.69574  53.45328  1.000 14.03531 ? 10  ASN   A CB  1 
ATOM   66   C  CG  . ASN   A 1 14  ? 2.33774  -7.67079  54.03814  1.000 33.19916 ? 10  ASN   A CG  1 
ATOM   67   O  OD1 . ASN   A 1 14  ? 2.61125  -7.08103  55.08462  1.000 31.11904 ? 10  ASN   A OD1 1 
ATOM   68   N  ND2 . ASN   A 1 14  ? 1.21083  -7.45738  53.36881  1.000 30.13236 ? 10  ASN   A ND2 1 
ATOM   69   N  N   . PHE   A 1 15  ? 6.54807  -9.00943  52.95017  1.000 15.25474 ? 11  PHE   A N   1 
ATOM   70   C  CA  . PHE   A 1 15  ? 7.55239  -10.06386 52.95724  1.000 16.88633 ? 11  PHE   A CA  1 
ATOM   71   C  C   . PHE   A 1 15  ? 8.02742  -10.27605 54.38239  1.000 13.24764 ? 11  PHE   A C   1 
ATOM   72   O  O   . PHE   A 1 15  ? 8.14443  -9.31764  55.15047  1.000 12.69819 ? 11  PHE   A O   1 
ATOM   73   C  CB  . PHE   A 1 15  ? 8.76720  -9.74271  52.07429  1.000 15.31973 ? 11  PHE   A CB  1 
ATOM   74   C  CG  . PHE   A 1 15  ? 9.78117  -10.85187 52.03250  1.000 13.21770 ? 11  PHE   A CG  1 
ATOM   75   C  CD1 . PHE   A 1 15  ? 9.51204  -12.02252 51.33587  1.000 19.29682 ? 11  PHE   A CD1 1 
ATOM   76   C  CD2 . PHE   A 1 15  ? 10.98523 -10.74381 52.71140  1.000 17.53755 ? 11  PHE   A CD2 1 
ATOM   77   C  CE1 . PHE   A 1 15  ? 10.42747 -13.05437 51.29681  1.000 13.41939 ? 11  PHE   A CE1 1 
ATOM   78   C  CE2 . PHE   A 1 15  ? 11.90929 -11.77505 52.67856  1.000 19.97927 ? 11  PHE   A CE2 1 
ATOM   79   C  CZ  . PHE   A 1 15  ? 11.62766 -12.93580 51.96879  1.000 13.13229 ? 11  PHE   A CZ  1 
ATOM   80   N  N   . THR   A 1 16  ? 8.30915  -11.52886 54.72962  1.000 13.53412 ? 12  THR   A N   1 
ATOM   81   C  CA  . THR   A 1 16  ? 8.85202  -11.85418 56.04031  1.000 14.97572 ? 12  THR   A CA  1 
ATOM   82   C  C   . THR   A 1 16  ? 10.06854 -12.75445 55.88348  1.000 14.32718 ? 12  THR   A C   1 
ATOM   83   O  O   . THR   A 1 16  ? 10.09622 -13.63409 55.01637  1.000 16.88580 ? 12  THR   A O   1 
ATOM   84   C  CB  . THR   A 1 16  ? 7.80273  -12.53361 56.93927  1.000 18.39944 ? 12  THR   A CB  1 
ATOM   85   O  OG1 . THR   A 1 16  ? 8.38938  -12.83447 58.20909  1.000 19.71573 ? 12  THR   A OG1 1 
ATOM   86   C  CG2 . THR   A 1 16  ? 7.28153  -13.81629 56.30401  1.000 16.98028 ? 12  THR   A CG2 1 
ATOM   87   N  N   . THR   A 1 17  ? 11.08720 -12.51214 56.70907  1.000 14.68390 ? 13  THR   A N   1 
ATOM   88   C  CA  . THR   A 1 17  ? 12.24589 -13.39211 56.72761  1.000 19.61640 ? 13  THR   A CA  1 
ATOM   89   C  C   . THR   A 1 17  ? 11.99946 -14.65992 57.52945  1.000 16.31136 ? 13  THR   A C   1 
ATOM   90   O  O   . THR   A 1 17  ? 12.82483 -15.57734 57.47371  1.000 16.92358 ? 13  THR   A O   1 
ATOM   91   C  CB  . THR   A 1 17  ? 13.46638 -12.66392 57.29259  1.000 18.73915 ? 13  THR   A CB  1 
ATOM   92   O  OG1 . THR   A 1 17  ? 13.22722 -12.31148 58.66149  1.000 17.59670 ? 13  THR   A OG1 1 
ATOM   93   C  CG2 . THR   A 1 17  ? 13.76110 -11.40819 56.47452  1.000 19.08619 ? 13  THR   A CG2 1 
ATOM   94   N  N   . ALA   A 1 18  ? 10.89032 -14.72866 58.26293  1.000 16.66333 ? 14  ALA   A N   1 
ATOM   95   C  CA  . ALA   A 1 18  ? 10.56793 -15.89808 59.07072  1.000 18.91612 ? 14  ALA   A CA  1 
ATOM   96   C  C   . ALA   A 1 18  ? 10.10116 -17.01951 58.15506  1.000 27.13355 ? 14  ALA   A C   1 
ATOM   97   O  O   . ALA   A 1 18  ? 9.00134  -16.95855 57.59618  1.000 25.20851 ? 14  ALA   A O   1 
ATOM   98   C  CB  . ALA   A 1 18  ? 9.50128  -15.54986 60.10475  1.000 21.04163 ? 14  ALA   A CB  1 
ATOM   99   N  N   . GLY   A 1 19  ? 10.93797 -18.03982 57.99510  1.000 22.71369 ? 15  GLY   A N   1 
ATOM   100  C  CA  . GLY   A 1 19  ? 10.61906 -19.12862 57.09453  1.000 27.39916 ? 15  GLY   A CA  1 
ATOM   101  C  C   . GLY   A 1 19  ? 10.74371 -18.78187 55.62826  1.000 28.48989 ? 15  GLY   A C   1 
ATOM   102  O  O   . GLY   A 1 19  ? 10.05922 -19.38767 54.79655  1.000 25.46535 ? 15  GLY   A O   1 
ATOM   103  N  N   . ALA   A 1 20  ? 11.60634 -17.82555 55.28516  1.000 19.65095 ? 16  ALA   A N   1 
ATOM   104  C  CA  . ALA   A 1 20  ? 11.75042 -17.41346 53.89395  1.000 19.57999 ? 16  ALA   A CA  1 
ATOM   105  C  C   . ALA   A 1 20  ? 12.29152 -18.55341 53.03750  1.000 24.56568 ? 16  ALA   A C   1 
ATOM   106  O  O   . ALA   A 1 20  ? 13.18446 -19.29959 53.44971  1.000 19.74472 ? 16  ALA   A O   1 
ATOM   107  C  CB  . ALA   A 1 20  ? 12.67296 -16.19850 53.79346  1.000 19.22935 ? 16  ALA   A CB  1 
ATOM   108  N  N   . THR   A 1 21  ? 11.73668 -18.69000 51.83643  1.000 18.65076 ? 17  THR   A N   1 
ATOM   109  C  CA  . THR   A 1 21  ? 12.16657 -19.70286 50.88579  1.000 18.72770 ? 17  THR   A CA  1 
ATOM   110  C  C   . THR   A 1 21  ? 12.43704 -19.04586 49.54062  1.000 16.54134 ? 17  THR   A C   1 
ATOM   111  O  O   . THR   A 1 21  ? 12.14310 -17.86672 49.32166  1.000 15.61439 ? 17  THR   A O   1 
ATOM   112  C  CB  . THR   A 1 21  ? 11.12081 -20.81668 50.71315  1.000 22.01912 ? 17  THR   A CB  1 
ATOM   113  O  OG1 . THR   A 1 21  ? 9.89533  -20.25206 50.22871  1.000 18.11694 ? 17  THR   A OG1 1 
ATOM   114  C  CG2 . THR   A 1 21  ? 10.86846 -21.54748 52.03136  1.000 18.85029 ? 17  THR   A CG2 1 
ATOM   115  N  N   . VAL   A 1 22  ? 13.00506 -19.83536 48.62899  1.000 20.17711 ? 18  VAL   A N   1 
ATOM   116  C  CA  . VAL   A 1 22  ? 13.19969 -19.36615 47.26078  1.000 21.05372 ? 18  VAL   A CA  1 
ATOM   117  C  C   . VAL   A 1 22  ? 11.85980 -19.00413 46.62831  1.000 20.15612 ? 18  VAL   A C   1 
ATOM   118  O  O   . VAL   A 1 22  ? 11.74490 -18.00545 45.90450  1.000 18.66306 ? 18  VAL   A O   1 
ATOM   119  C  CB  . VAL   A 1 22  ? 13.95403 -20.43301 46.44490  1.000 30.67872 ? 18  VAL   A CB  1 
ATOM   120  C  CG1 . VAL   A 1 22  ? 13.79090 -20.18993 44.97030  1.000 31.75368 ? 18  VAL   A CG1 1 
ATOM   121  C  CG2 . VAL   A 1 22  ? 15.42903 -20.43804 46.82061  1.000 26.43104 ? 18  VAL   A CG2 1 
ATOM   122  N  N   . GLN   A 1 23  ? 10.81976 -19.79289 46.91163  1.000 16.78172 ? 19  GLN   A N   1 
ATOM   123  C  CA  . GLN   A 1 23  ? 9.50083  -19.50864 46.35448  1.000 18.90560 ? 19  GLN   A CA  1 
ATOM   124  C  C   . GLN   A 1 23  ? 8.90181  -18.24350 46.95956  1.000 15.52054 ? 19  GLN   A C   1 
ATOM   125  O  O   . GLN   A 1 23  ? 8.38550  -17.38352 46.23551  1.000 14.95755 ? 19  GLN   A O   1 
ATOM   126  C  CB  . GLN   A 1 23  ? 8.56830  -20.69918 46.57250  1.000 19.70690 ? 19  GLN   A CB  1 
ATOM   127  C  CG  . GLN   A 1 23  ? 8.96668  -21.94830 45.81203  1.000 44.81636 ? 19  GLN   A CG  1 
ATOM   128  C  CD  . GLN   A 1 23  ? 8.06941  -23.12907 46.13206  1.000 69.72557 ? 19  GLN   A CD  1 
ATOM   129  O  OE1 . GLN   A 1 23  ? 7.47408  -23.19765 47.20782  1.000 69.58203 ? 19  GLN   A OE1 1 
ATOM   130  N  NE2 . GLN   A 1 23  ? 7.96132  -24.06223 45.19289  1.000 69.05393 ? 19  GLN   A NE2 1 
ATOM   131  N  N   . SER   A 1 24  ? 8.95785  -18.10937 48.28790  1.000 17.49552 ? 20  SER   A N   1 
ATOM   132  C  CA  . SER   A 1 24  ? 8.34720  -16.94477 48.92412  1.000 14.70895 ? 20  SER   A CA  1 
ATOM   133  C  C   . SER   A 1 24  ? 9.07117  -15.65857 48.53943  1.000 15.22081 ? 20  SER   A C   1 
ATOM   134  O  O   . SER   A 1 24  ? 8.43884  -14.60468 48.39570  1.000 14.28603 ? 20  SER   A O   1 
ATOM   135  C  CB  . SER   A 1 24  ? 8.32102  -17.11516 50.44583  1.000 15.23816 ? 20  SER   A CB  1 
ATOM   136  O  OG  . SER   A 1 24  ? 9.58518  -16.83210 51.01889  1.000 15.59486 ? 20  SER   A OG  1 
ATOM   137  N  N   . TYR   A 1 25  ? 10.39373 -15.71830 48.36460  1.000 13.94994 ? 21  TYR   A N   1 
ATOM   138  C  CA  . TYR   A 1 25  ? 11.11134 -14.52627 47.92390  1.000 13.32605 ? 21  TYR   A CA  1 
ATOM   139  C  C   . TYR   A 1 25  ? 10.79842 -14.20838 46.46691  1.000 15.66970 ? 21  TYR   A C   1 
ATOM   140  O  O   . TYR   A 1 25  ? 10.66888 -13.03905 46.09572  1.000 12.58780 ? 21  TYR   A O   1 
ATOM   141  C  CB  . TYR   A 1 25  ? 12.61496 -14.70016 48.12138  1.000 13.64989 ? 21  TYR   A CB  1 
ATOM   142  C  CG  . TYR   A 1 25  ? 13.41978 -13.50893 47.64610  1.000 13.19497 ? 21  TYR   A CG  1 
ATOM   143  C  CD1 . TYR   A 1 25  ? 13.54347 -12.36770 48.43450  1.000 12.71216 ? 21  TYR   A CD1 1 
ATOM   144  C  CD2 . TYR   A 1 25  ? 14.04714 -13.51968 46.40452  1.000 13.40156 ? 21  TYR   A CD2 1 
ATOM   145  C  CE1 . TYR   A 1 25  ? 14.27740 -11.27129 47.99895  1.000 14.11295 ? 21  TYR   A CE1 1 
ATOM   146  C  CE2 . TYR   A 1 25  ? 14.78572 -12.43008 45.96340  1.000 13.14786 ? 21  TYR   A CE2 1 
ATOM   147  C  CZ  . TYR   A 1 25  ? 14.89388 -11.31006 46.76439  1.000 16.27149 ? 21  TYR   A CZ  1 
ATOM   148  O  OH  . TYR   A 1 25  ? 15.62137 -10.22560 46.32901  1.000 15.03061 ? 21  TYR   A OH  1 
ATOM   149  N  N   . THR   A 1 26  ? 10.66766 -15.23761 45.62936  1.000 13.76672 ? 22  THR   A N   1 
ATOM   150  C  CA  . THR   A 1 26  ? 10.31504 -15.01364 44.23221  1.000 16.50689 ? 22  THR   A CA  1 
ATOM   151  C  C   . THR   A 1 26  ? 8.92326  -14.40561 44.10558  1.000 15.66036 ? 22  THR   A C   1 
ATOM   152  O  O   . THR   A 1 26  ? 8.72204  -13.44511 43.35325  1.000 16.02942 ? 22  THR   A O   1 
ATOM   153  C  CB  . THR   A 1 26  ? 10.40806 -16.32531 43.45512  1.000 23.09891 ? 22  THR   A CB  1 
ATOM   154  O  OG1 . THR   A 1 26  ? 11.77978 -16.73054 43.38294  1.000 30.75020 ? 22  THR   A OG1 1 
ATOM   155  C  CG2 . THR   A 1 26  ? 9.85575  -16.15722 42.04761  1.000 24.73402 ? 22  THR   A CG2 1 
ATOM   156  N  N   . ASN   A 1 27  ? 7.94624  -14.95240 44.83729  1.000 14.45264 ? 23  ASN   A N   1 
ATOM   157  C  CA  . ASN   A 1 27  ? 6.59652  -14.39649 44.79077  1.000 15.70616 ? 23  ASN   A CA  1 
ATOM   158  C  C   . ASN   A 1 27  ? 6.59045  -12.94171 45.23370  1.000 15.92183 ? 23  ASN   A C   1 
ATOM   159  O  O   . ASN   A 1 27  ? 5.83565  -12.11943 44.69803  1.000 12.43610 ? 23  ASN   A O   1 
ATOM   160  C  CB  . ASN   A 1 27  ? 5.65091  -15.21181 45.66973  1.000 14.91347 ? 23  ASN   A CB  1 
ATOM   161  C  CG  . ASN   A 1 27  ? 5.46144  -16.62449 45.16969  1.000 19.75546 ? 23  ASN   A CG  1 
ATOM   162  O  OD1 . ASN   A 1 27  ? 5.79833  -16.94017 44.03358  1.000 25.29551 ? 23  ASN   A OD1 1 
ATOM   163  N  ND2 . ASN   A 1 27  ? 4.91478  -17.48409 46.01981  1.000 22.13943 ? 23  ASN   A ND2 1 
ATOM   164  N  N   . PHE   A 1 28  ? 7.42541  -12.61167 46.21782  1.000 12.33039 ? 24  PHE   A N   1 
ATOM   165  C  CA  . PHE   A 1 28  ? 7.49356  -11.24617 46.72318  1.000 11.73462 ? 24  PHE   A CA  1 
ATOM   166  C  C   . PHE   A 1 28  ? 7.97797  -10.27850 45.64729  1.000 11.43933 ? 24  PHE   A C   1 
ATOM   167  O  O   . PHE   A 1 28  ? 7.33709  -9.25410  45.38392  1.000 12.48147 ? 24  PHE   A O   1 
ATOM   168  C  CB  . PHE   A 1 28  ? 8.40458  -11.21451 47.94905  1.000 11.67943 ? 24  PHE   A CB  1 
ATOM   169  C  CG  . PHE   A 1 28  ? 8.79544  -9.84094  48.38147  1.000 18.57296 ? 24  PHE   A CG  1 
ATOM   170  C  CD1 . PHE   A 1 28  ? 7.83472  -8.91874  48.75262  1.000 17.03534 ? 24  PHE   A CD1 1 
ATOM   171  C  CD2 . PHE   A 1 28  ? 10.12978 -9.47884  48.44617  1.000 13.40073 ? 24  PHE   A CD2 1 
ATOM   172  C  CE1 . PHE   A 1 28  ? 8.19772  -7.65365  49.15814  1.000 15.75699 ? 24  PHE   A CE1 1 
ATOM   173  C  CE2 . PHE   A 1 28  ? 10.49887 -8.21022  48.85329  1.000 15.89042 ? 24  PHE   A CE2 1 
ATOM   174  C  CZ  . PHE   A 1 28  ? 9.53433  -7.30187  49.20688  1.000 17.41716 ? 24  PHE   A CZ  1 
ATOM   175  N  N   . ILE   A 1 29  ? 9.10823  -10.59067 45.00841  1.000 12.62088 ? 25  ILE   A N   1 
ATOM   176  C  CA  . ILE   A 1 29  ? 9.67540  -9.67977  44.01482  1.000 11.51265 ? 25  ILE   A CA  1 
ATOM   177  C  C   . ILE   A 1 29  ? 8.75406  -9.55858  42.80556  1.000 11.72425 ? 25  ILE   A C   1 
ATOM   178  O  O   . ILE   A 1 29  ? 8.60269  -8.47363  42.22697  1.000 11.59164 ? 25  ILE   A O   1 
ATOM   179  C  CB  . ILE   A 1 29  ? 11.08908 -10.14171 43.61491  1.000 12.51681 ? 25  ILE   A CB  1 
ATOM   180  C  CG1 . ILE   A 1 29  ? 12.03976 -10.05308 44.81061  1.000 11.84881 ? 25  ILE   A CG1 1 
ATOM   181  C  CG2 . ILE   A 1 29  ? 11.62046 -9.32443  42.44229  1.000 12.00482 ? 25  ILE   A CG2 1 
ATOM   182  C  CD1 . ILE   A 1 29  ? 12.19691 -8.64512  45.36314  1.000 16.20705 ? 25  ILE   A CD1 1 
ATOM   183  N  N   . ARG   A 1 30  ? 8.11710  -10.66100 42.40432  1.000 16.97878 ? 26  ARG   A N   1 
ATOM   184  C  CA  . ARG   A 1 30  ? 7.16842  -10.58447 41.29846  1.000 14.38515 ? 26  ARG   A CA  1 
ATOM   185  C  C   . ARG   A 1 30  ? 5.98345  -9.69435  41.65081  1.000 14.84218 ? 26  ARG   A C   1 
ATOM   186  O  O   . ARG   A 1 30  ? 5.46510  -8.97008  40.79478  1.000 18.88269 ? 26  ARG   A O   1 
ATOM   187  C  CB  . ARG   A 1 30  ? 6.70172  -11.98444 40.91187  1.000 14.84063 ? 26  ARG   A CB  1 
ATOM   188  C  CG  . ARG   A 1 30  ? 7.82203  -12.83406 40.34912  1.000 22.68240 ? 26  ARG   A CG  1 
ATOM   189  C  CD  . ARG   A 1 30  ? 7.32124  -14.17161 39.85765  1.000 29.65238 ? 26  ARG   A CD  1 
ATOM   190  N  NE  . ARG   A 1 30  ? 8.41372  -14.97541 39.32715  1.000 35.38391 ? 26  ARG   A NE  1 
ATOM   191  C  CZ  . ARG   A 1 30  ? 8.27361  -16.20395 38.85258  1.000 38.28722 ? 26  ARG   A CZ  1 
ATOM   192  N  NH1 . ARG   A 1 30  ? 7.09276  -16.79808 38.81618  1.000 39.45931 ? 26  ARG   A NH1 1 
ATOM   193  N  NH2 . ARG   A 1 30  ? 9.34552  -16.85273 38.40640  1.000 41.36496 ? 26  ARG   A NH2 1 
ATOM   194  N  N   . ALA   A 1 31  ? 5.55490  -9.71661  42.91432  1.000 17.46291 ? 27  ALA   A N   1 
ATOM   195  C  CA  . ALA   A 1 31  ? 4.45257  -8.85637  43.32929  1.000 14.86722 ? 27  ALA   A CA  1 
ATOM   196  C  C   . ALA   A 1 31  ? 4.86836  -7.38989  43.34233  1.000 15.02892 ? 27  ALA   A C   1 
ATOM   197  O  O   . ALA   A 1 31  ? 4.06372  -6.51122  43.01170  1.000 15.27057 ? 27  ALA   A O   1 
ATOM   198  C  CB  . ALA   A 1 31  ? 3.93941  -9.28385  44.70345  1.000 12.59262 ? 27  ALA   A CB  1 
ATOM   199  N  N   . VAL   A 1 32  ? 6.11710  -7.10517  43.72537  1.000 11.05564 ? 28  VAL   A N   1 
ATOM   200  C  CA  . VAL   A 1 32  ? 6.60331  -5.72853  43.70390  1.000 13.84628 ? 28  VAL   A CA  1 
ATOM   201  C  C   . VAL   A 1 32  ? 6.68644  -5.21280  42.27065  1.000 18.42595 ? 28  VAL   A C   1 
ATOM   202  O  O   . VAL   A 1 32  ? 6.27450  -4.08402  41.97928  1.000 17.23693 ? 28  VAL   A O   1 
ATOM   203  C  CB  . VAL   A 1 32  ? 7.95889  -5.62304  44.42516  1.000 11.12664 ? 28  VAL   A CB  1 
ATOM   204  C  CG1 . VAL   A 1 32  ? 8.55025  -4.22635  44.25362  1.000 12.91424 ? 28  VAL   A CG1 1 
ATOM   205  C  CG2 . VAL   A 1 32  ? 7.79534  -5.93511  45.90909  1.000 12.22000 ? 28  VAL   A CG2 1 
ATOM   206  N  N   . ARG   A 1 33  ? 7.22051  -6.02350  41.35368  1.000 14.26734 ? 29  ARG   A N   1 
ATOM   207  C  CA  . ARG   A 1 33  ? 7.24251  -5.61861  39.95194  1.000 15.77029 ? 29  ARG   A CA  1 
ATOM   208  C  C   . ARG   A 1 33  ? 5.84026  -5.31258  39.44575  1.000 19.46332 ? 29  ARG   A C   1 
ATOM   209  O  O   . ARG   A 1 33  ? 5.63763  -4.34261  38.70591  1.000 18.45164 ? 29  ARG   A O   1 
ATOM   210  C  CB  . ARG   A 1 33  ? 7.88213  -6.70540  39.08938  1.000 17.48981 ? 29  ARG   A CB  1 
ATOM   211  C  CG  . ARG   A 1 33  ? 9.32770  -6.97951  39.40691  1.000 15.42726 ? 29  ARG   A CG  1 
ATOM   212  C  CD  . ARG   A 1 33  ? 9.96301  -7.84079  38.33474  1.000 15.28926 ? 29  ARG   A CD  1 
ATOM   213  N  NE  . ARG   A 1 33  ? 11.34592 -8.15302  38.66955  1.000 15.93404 ? 29  ARG   A NE  1 
ATOM   214  C  CZ  . ARG   A 1 33  ? 11.82680 -9.37946  38.80576  1.000 16.77891 ? 29  ARG   A CZ  1 
ATOM   215  N  NH1 . ARG   A 1 33  ? 11.07461 -10.44560 38.58016  1.000 13.81934 ? 29  ARG   A NH1 1 
ATOM   216  N  NH2 . ARG   A 1 33  ? 13.09565 -9.53992  39.17187  1.000 13.63297 ? 29  ARG   A NH2 1 
ATOM   217  N  N   . GLY   A 1 34  ? 4.85851  -6.12833  39.83815  1.000 14.16973 ? 30  GLY   A N   1 
ATOM   218  C  CA  . GLY   A 1 34  ? 3.50497  -5.97089  39.33527  1.000 24.93236 ? 30  GLY   A CA  1 
ATOM   219  C  C   . GLY   A 1 34  ? 2.80103  -4.72460  39.82336  1.000 25.84561 ? 30  GLY   A C   1 
ATOM   220  O  O   . GLY   A 1 34  ? 1.86548  -4.25621  39.16777  1.000 22.58972 ? 30  GLY   A O   1 
ATOM   221  N  N   . ARG   A 1 35  ? 3.21325  -4.18307  40.96445  1.000 24.55851 ? 31  ARG   A N   1 
ATOM   222  C  CA  . ARG   A 1 35  ? 2.64315  -2.92624  41.42219  1.000 17.62288 ? 31  ARG   A CA  1 
ATOM   223  C  C   . ARG   A 1 35  ? 3.44637  -1.72246  40.95352  1.000 19.62937 ? 31  ARG   A C   1 
ATOM   224  O  O   . ARG   A 1 35  ? 2.91502  -0.60687  40.93835  1.000 18.26653 ? 31  ARG   A O   1 
ATOM   225  C  CB  . ARG   A 1 35  ? 2.53582  -2.90558  42.95106  1.000 21.15895 ? 31  ARG   A CB  1 
ATOM   226  C  CG  . ARG   A 1 35  ? 1.93360  -4.16201  43.57545  1.000 20.21225 ? 31  ARG   A CG  1 
ATOM   227  C  CD  . ARG   A 1 35  ? 0.69273  -4.64324  42.83943  1.000 34.02756 ? 31  ARG   A CD  1 
ATOM   228  N  NE  . ARG   A 1 35  ? -0.35180 -3.62941  42.77198  1.000 31.95252 ? 31  ARG   A NE  1 
ATOM   229  C  CZ  . ARG   A 1 35  ? -1.37419 -3.55380  43.61216  1.000 31.34134 ? 31  ARG   A CZ  1 
ATOM   230  N  NH1 . ARG   A 1 35  ? -1.51078 -4.40845  44.61266  1.000 33.41639 ? 31  ARG   A NH1 1 
ATOM   231  N  NH2 . ARG   A 1 35  ? -2.28436 -2.60001  43.44139  1.000 33.64770 ? 31  ARG   A NH2 1 
ATOM   232  N  N   . LEU   A 1 36  ? 4.70993  -1.92468  40.57018  1.000 14.04562 ? 32  LEU   A N   1 
ATOM   233  C  CA  . LEU   A 1 36  ? 5.53735  -0.81225  40.11821  1.000 19.66894 ? 32  LEU   A CA  1 
ATOM   234  C  C   . LEU   A 1 36  ? 5.14967  -0.36993  38.71726  1.000 18.88158 ? 32  LEU   A C   1 
ATOM   235  O  O   . LEU   A 1 36  ? 5.17321  0.82640   38.40896  1.000 16.66237 ? 32  LEU   A O   1 
ATOM   236  C  CB  . LEU   A 1 36  ? 7.01231  -1.20474  40.15323  1.000 14.86092 ? 32  LEU   A CB  1 
ATOM   237  C  CG  . LEU   A 1 36  ? 7.68550  -1.17957  41.52284  1.000 14.98346 ? 32  LEU   A CG  1 
ATOM   238  C  CD1 . LEU   A 1 36  ? 9.07825  -1.77614  41.42248  1.000 16.18797 ? 32  LEU   A CD1 1 
ATOM   239  C  CD2 . LEU   A 1 36  ? 7.74391  0.24562   42.04880  1.000 11.32139 ? 32  LEU   A CD2 1 
ATOM   240  N  N   . THR   A 1 37  ? 4.80569  -1.31933  37.85634  1.000 20.67369 ? 33  THR   A N   1 
ATOM   241  C  CA  . THR   A 1 37  ? 4.47091  -1.05103  36.47050  1.000 25.83646 ? 33  THR   A CA  1 
ATOM   242  C  C   . THR   A 1 37  ? 3.09060  -1.60956  36.16430  1.000 29.96247 ? 33  THR   A C   1 
ATOM   243  O  O   . THR   A 1 37  ? 2.52937  -2.40416  36.92162  1.000 32.76753 ? 33  THR   A O   1 
ATOM   244  C  CB  . THR   A 1 37  ? 5.50391  -1.66999  35.52030  1.000 32.65205 ? 33  THR   A CB  1 
ATOM   245  O  OG1 . THR   A 1 37  ? 5.14647  -1.37193  34.16438  1.000 45.90793 ? 33  THR   A OG1 1 
ATOM   246  C  CG2 . THR   A 1 37  ? 5.54948  -3.18214  35.70004  1.000 38.33852 ? 33  THR   A CG2 1 
ATOM   247  N  N   . THR   A 1 38  ? 2.54278  -1.17657  35.03552  1.000 33.14828 ? 34  THR   A N   1 
ATOM   248  C  CA  . THR   A 1 38  ? 1.33119  -1.79059  34.51715  1.000 37.36566 ? 34  THR   A CA  1 
ATOM   249  C  C   . THR   A 1 38  ? 1.63558  -2.94672  33.57883  1.000 34.10244 ? 34  THR   A C   1 
ATOM   250  O  O   . THR   A 1 38  ? 0.82692  -3.87229  33.46116  1.000 36.50224 ? 34  THR   A O   1 
ATOM   251  C  CB  . THR   A 1 38  ? 0.48232  -0.75411  33.77668  1.000 41.17717 ? 34  THR   A CB  1 
ATOM   252  O  OG1 . THR   A 1 38  ? 1.11030  -0.42975  32.53022  1.000 37.96702 ? 34  THR   A OG1 1 
ATOM   253  C  CG2 . THR   A 1 38  ? 0.34128  0.51174   34.61151  1.000 49.48383 ? 34  THR   A CG2 1 
ATOM   254  N  N   . GLY   A 1 39  ? 2.79201  -2.92543  32.92364  1.000 35.43976 ? 35  GLY   A N   1 
ATOM   255  C  CA  . GLY   A 1 39  ? 3.06015  -3.85127  31.84852  1.000 43.05927 ? 35  GLY   A CA  1 
ATOM   256  C  C   . GLY   A 1 39  ? 2.52162  -3.41933  30.50393  1.000 37.32133 ? 35  GLY   A C   1 
ATOM   257  O  O   . GLY   A 1 39  ? 2.67708  -4.16173  29.52617  1.000 39.38275 ? 35  GLY   A O   1 
ATOM   258  N  N   . ALA   A 1 40  ? 1.89172  -2.24439  30.42127  1.000 37.61970 ? 36  ALA   A N   1 
ATOM   259  C  CA  . ALA   A 1 40  ? 1.36412  -1.75335  29.15449  1.000 44.42898 ? 36  ALA   A CA  1 
ATOM   260  C  C   . ALA   A 1 40  ? 2.42685  -1.08168  28.29656  1.000 36.11229 ? 36  ALA   A C   1 
ATOM   261  O  O   . ALA   A 1 40  ? 2.26281  -1.01225  27.07446  1.000 39.53547 ? 36  ALA   A O   1 
ATOM   262  C  CB  . ALA   A 1 40  ? 0.21153  -0.77758  29.40283  1.000 35.93214 ? 36  ALA   A CB  1 
ATOM   263  N  N   . ASP   A 1 41  ? 3.50175  -0.58629  28.90064  1.000 25.43934 ? 37  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 41  ? 4.61758  0.00940   28.17167  1.000 29.45130 ? 37  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 41  ? 5.78476  -0.96707  28.24985  1.000 24.45801 ? 37  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 41  ? 6.44035  -1.07631  29.28764  1.000 23.18579 ? 37  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 41  ? 4.98960  1.37028   28.75309  1.000 22.47175 ? 37  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 41  ? 6.05234  2.08901   27.93587  1.000 26.86556 ? 37  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 41  ? 6.43047  1.58740   26.85157  1.000 28.89807 ? 37  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 41  ? 6.50521  3.16507   28.37835  1.000 28.02472 ? 37  ASP   A OD2 1 
ATOM   271  N  N   . VAL   A 1 42  ? 6.03132  -1.69016  27.15997  1.000 24.73307 ? 38  VAL   A N   1 
ATOM   272  C  CA  . VAL   A 1 42  ? 7.17979  -2.58124  27.06244  1.000 24.87887 ? 38  VAL   A CA  1 
ATOM   273  C  C   . VAL   A 1 42  ? 7.96686  -2.20856  25.81359  1.000 27.17987 ? 38  VAL   A C   1 
ATOM   274  O  O   . VAL   A 1 42  ? 7.38286  -1.98591  24.74621  1.000 27.78954 ? 38  VAL   A O   1 
ATOM   275  C  CB  . VAL   A 1 42  ? 6.76599  -4.06924  27.03987  1.000 27.96311 ? 38  VAL   A CB  1 
ATOM   276  C  CG1 . VAL   A 1 42  ? 5.96881  -4.42215  28.28679  1.000 28.03877 ? 38  VAL   A CG1 1 
ATOM   277  C  CG2 . VAL   A 1 42  ? 5.96702  -4.41290  25.78661  1.000 42.12204 ? 38  VAL   A CG2 1 
ATOM   278  N  N   . ARG   A 1 43  ? 9.28529  -2.09794  25.95708  1.000 20.17843 ? 39  ARG   A N   1 
ATOM   279  C  CA  . ARG   A 1 43  ? 10.18960 -1.93339  24.82570  1.000 20.96446 ? 39  ARG   A CA  1 
ATOM   280  C  C   . ARG   A 1 43  ? 11.12486 -3.12991  24.80666  1.000 25.42996 ? 39  ARG   A C   1 
ATOM   281  O  O   . ARG   A 1 43  ? 11.79716 -3.40716  25.80714  1.000 20.83604 ? 39  ARG   A O   1 
ATOM   282  C  CB  . ARG   A 1 43  ? 10.99881 -0.63777  24.91557  1.000 23.73167 ? 39  ARG   A CB  1 
ATOM   283  C  CG  . ARG   A 1 43  ? 10.35594 0.46652   25.71505  1.000 25.42816 ? 39  ARG   A CG  1 
ATOM   284  C  CD  . ARG   A 1 43  ? 9.29776  1.22025   24.94159  1.000 23.90212 ? 39  ARG   A CD  1 
ATOM   285  N  NE  . ARG   A 1 43  ? 8.68144  2.23533   25.78803  1.000 21.43204 ? 39  ARG   A NE  1 
ATOM   286  C  CZ  . ARG   A 1 43  ? 9.18496  3.44352   26.00313  1.000 29.83117 ? 39  ARG   A CZ  1 
ATOM   287  N  NH1 . ARG   A 1 43  ? 10.30214 3.84262   25.41647  1.000 27.20710 ? 39  ARG   A NH1 1 
ATOM   288  N  NH2 . ARG   A 1 43  ? 8.55132  4.27259   26.82851  1.000 26.08813 ? 39  ARG   A NH2 1 
ATOM   289  N  N   . HIS   A 1 44  ? 11.15974 -3.83663  23.67630  1.000 22.10209 ? 40  HIS   A N   1 
ATOM   290  C  CA  . HIS   A 1 44  ? 12.03997 -4.99074  23.50087  1.000 24.81413 ? 40  HIS   A CA  1 
ATOM   291  C  C   . HIS   A 1 44  ? 11.81854 -6.02598  24.60051  1.000 24.10432 ? 40  HIS   A C   1 
ATOM   292  O  O   . HIS   A 1 44  ? 12.76579 -6.62907  25.10946  1.000 32.35650 ? 40  HIS   A O   1 
ATOM   293  C  CB  . HIS   A 1 44  ? 13.50450 -4.55280  23.43759  1.000 22.23045 ? 40  HIS   A CB  1 
ATOM   294  C  CG  . HIS   A 1 44  ? 13.79696 -3.61485  22.30869  1.000 25.75043 ? 40  HIS   A CG  1 
ATOM   295  N  ND1 . HIS   A 1 44  ? 13.98084 -4.04720  21.01295  1.000 31.61384 ? 40  HIS   A ND1 1 
ATOM   296  C  CD2 . HIS   A 1 44  ? 13.91678 -2.26654  22.27584  1.000 24.83631 ? 40  HIS   A CD2 1 
ATOM   297  C  CE1 . HIS   A 1 44  ? 14.21110 -3.00681  20.23221  1.000 25.07878 ? 40  HIS   A CE1 1 
ATOM   298  N  NE2 . HIS   A 1 44  ? 14.17818 -1.91436  20.97354  1.000 28.76923 ? 40  HIS   A NE2 1 
ATOM   299  N  N   . GLU   A 1 45  ? 10.54881 -6.21933  24.96911  1.000 21.25120 ? 41  GLU   A N   1 
ATOM   300  C  CA  . GLU   A 1 45  ? 10.06139 -7.18937  25.95042  1.000 20.74275 ? 41  GLU   A CA  1 
ATOM   301  C  C   . GLU   A 1 45  ? 10.37317 -6.79479  27.38543  1.000 25.10294 ? 41  GLU   A C   1 
ATOM   302  O  O   . GLU   A 1 45  ? 10.18229 -7.61383  28.29175  1.000 26.69532 ? 41  GLU   A O   1 
ATOM   303  C  CB  . GLU   A 1 45  ? 10.60889 -8.60268  25.70497  1.000 21.27598 ? 41  GLU   A CB  1 
ATOM   304  C  CG  . GLU   A 1 45  ? 10.59563 -9.06316  24.24726  1.000 32.73615 ? 41  GLU   A CG  1 
ATOM   305  C  CD  . GLU   A 1 45  ? 9.31226  -9.76307  23.85415  1.000 48.05457 ? 41  GLU   A CD  1 
ATOM   306  O  OE1 . GLU   A 1 45  ? 8.25178  -9.44698  24.43495  1.000 54.43527 ? 41  GLU   A OE1 1 
ATOM   307  O  OE2 . GLU   A 1 45  ? 9.36800  -10.63599 22.96113  1.000 52.30280 ? 41  GLU   A OE2 1 
ATOM   308  N  N   . ILE   A 1 46  ? 10.83497 -5.57381  27.62269  1.000 20.89088 ? 42  ILE   A N   1 
ATOM   309  C  CA  . ILE   A 1 46  ? 11.25451 -5.11583  28.94380  1.000 19.19209 ? 42  ILE   A CA  1 
ATOM   310  C  C   . ILE   A 1 46  ? 10.26687 -4.05398  29.41680  1.000 21.94163 ? 42  ILE   A C   1 
ATOM   311  O  O   . ILE   A 1 46  ? 10.10513 -3.02536  28.74581  1.000 18.12908 ? 42  ILE   A O   1 
ATOM   312  C  CB  . ILE   A 1 46  ? 12.68745 -4.56199  28.92159  1.000 21.19674 ? 42  ILE   A CB  1 
ATOM   313  C  CG1 . ILE   A 1 46  ? 13.65100 -5.60847  28.35996  1.000 22.73842 ? 42  ILE   A CG1 1 
ATOM   314  C  CG2 . ILE   A 1 46  ? 13.10970 -4.12906  30.32461  1.000 16.88599 ? 42  ILE   A CG2 1 
ATOM   315  C  CD1 . ILE   A 1 46  ? 15.01308 -5.05181  27.99674  1.000 17.06958 ? 42  ILE   A CD1 1 
ATOM   316  N  N   . PRO   A 1 47  ? 9.59191  -4.25495  30.54795  1.000 18.73519 ? 43  PRO   A N   1 
ATOM   317  C  CA  . PRO   A 1 47  ? 8.63300  -3.25256  31.02735  1.000 16.95102 ? 43  PRO   A CA  1 
ATOM   318  C  C   . PRO   A 1 47  ? 9.30908  -1.93902  31.39280  1.000 16.86384 ? 43  PRO   A C   1 
ATOM   319  O  O   . PRO   A 1 47  ? 10.43491 -1.91163  31.89729  1.000 14.67605 ? 43  PRO   A O   1 
ATOM   320  C  CB  . PRO   A 1 47  ? 8.01441  -3.91818  32.26451  1.000 18.31849 ? 43  PRO   A CB  1 
ATOM   321  C  CG  . PRO   A 1 47  ? 8.23218  -5.38088  32.05798  1.000 15.78815 ? 43  PRO   A CG  1 
ATOM   322  C  CD  . PRO   A 1 47  ? 9.54909  -5.48923  31.34803  1.000 21.71172 ? 43  PRO   A CD  1 
ATOM   323  N  N   . VAL   A 1 48  ? 8.59835  -0.84358  31.13927  1.000 15.91191 ? 44  VAL   A N   1 
ATOM   324  C  CA  . VAL   A 1 48  ? 9.05035  0.49866   31.48763  1.000 15.58447 ? 44  VAL   A CA  1 
ATOM   325  C  C   . VAL   A 1 48  ? 8.20024  1.02203   32.63732  1.000 15.12724 ? 44  VAL   A C   1 
ATOM   326  O  O   . VAL   A 1 48  ? 6.97593  0.85046   32.64827  1.000 15.61638 ? 44  VAL   A O   1 
ATOM   327  C  CB  . VAL   A 1 48  ? 8.96888  1.44828   30.27727  1.000 20.66452 ? 44  VAL   A CB  1 
ATOM   328  C  CG1 . VAL   A 1 48  ? 9.54688  2.81444   30.62729  1.000 16.71559 ? 44  VAL   A CG1 1 
ATOM   329  C  CG2 . VAL   A 1 48  ? 9.68932  0.84617   29.09643  1.000 17.33649 ? 44  VAL   A CG2 1 
ATOM   330  N  N   . LEU   A 1 49  ? 8.85151  1.67166   33.59713  1.000 14.32312 ? 45  LEU   A N   1 
ATOM   331  C  CA  . LEU   A 1 49  ? 8.14669  2.29874   34.70050  1.000 13.98445 ? 45  LEU   A CA  1 
ATOM   332  C  C   . LEU   A 1 49  ? 7.36278  3.51831   34.20675  1.000 14.92610 ? 45  LEU   A C   1 
ATOM   333  O  O   . LEU   A 1 49  ? 7.64784  4.05954   33.13597  1.000 15.70844 ? 45  LEU   A O   1 
ATOM   334  C  CB  . LEU   A 1 49  ? 9.14557  2.69206   35.78742  1.000 13.06282 ? 45  LEU   A CB  1 
ATOM   335  C  CG  . LEU   A 1 49  ? 9.94487  1.49992   36.32866  1.000 14.67059 ? 45  LEU   A CG  1 
ATOM   336  C  CD1 . LEU   A 1 49  ? 11.12386 1.94080   37.19802  1.000 12.06124 ? 45  LEU   A CD1 1 
ATOM   337  C  CD2 . LEU   A 1 49  ? 9.02716  0.56789   37.10440  1.000 11.96638 ? 45  LEU   A CD2 1 
ATOM   338  N  N   . PRO   A 1 50  ? 6.35186  3.95505   34.96011  1.000 15.00362 ? 46  PRO   A N   1 
ATOM   339  C  CA  . PRO   A 1 50  ? 5.54841  5.09795   34.51184  1.000 16.06164 ? 46  PRO   A CA  1 
ATOM   340  C  C   . PRO   A 1 50  ? 6.37095  6.37335   34.42954  1.000 16.87834 ? 46  PRO   A C   1 
ATOM   341  O  O   . PRO   A 1 50  ? 7.31468  6.58784   35.19635  1.000 15.46969 ? 46  PRO   A O   1 
ATOM   342  C  CB  . PRO   A 1 50  ? 4.45771  5.21305   35.58455  1.000 22.55764 ? 46  PRO   A CB  1 
ATOM   343  C  CG  . PRO   A 1 50  ? 4.41342  3.87262   36.24050  1.000 25.01627 ? 46  PRO   A CG  1 
ATOM   344  C  CD  . PRO   A 1 50  ? 5.80945  3.34657   36.18907  1.000 16.17681 ? 46  PRO   A CD  1 
ATOM   345  N  N   . ASN   A 1 51  ? 5.99009  7.22211   33.47963  1.000 17.47993 ? 47  ASN   A N   1 
ATOM   346  C  CA  . ASN   A 1 51  ? 6.58054  8.54594   33.34988  1.000 22.65148 ? 47  ASN   A CA  1 
ATOM   347  C  C   . ASN   A 1 51  ? 6.22698  9.39842   34.56479  1.000 23.65041 ? 47  ASN   A C   1 
ATOM   348  O  O   . ASN   A 1 51  ? 5.05408  9.53463   34.92871  1.000 18.24213 ? 47  ASN   A O   1 
ATOM   349  C  CB  . ASN   A 1 51  ? 6.08796  9.20265   32.05872  1.000 21.69591 ? 47  ASN   A CB  1 
ATOM   350  C  CG  . ASN   A 1 51  ? 6.73857  10.55485  31.78431  1.000 20.40131 ? 47  ASN   A CG  1 
ATOM   351  O  OD1 . ASN   A 1 51  ? 7.60690  11.01341  32.52586  1.000 22.89813 ? 47  ASN   A OD1 1 
ATOM   352  N  ND2 . ASN   A 1 51  ? 6.32360  11.19041  30.69469  1.000 23.48665 ? 47  ASN   A ND2 1 
ATOM   353  N  N   . ARG   A 1 52  ? 7.25512  9.96397   35.19784  1.000 22.31582 ? 48  ARG   A N   1 
ATOM   354  C  CA  . ARG   A 1 52  ? 7.04592  10.84276  36.34375  1.000 20.26910 ? 48  ARG   A CA  1 
ATOM   355  C  C   . ARG   A 1 52  ? 6.21810  12.07139  35.97284  1.000 21.33248 ? 48  ARG   A C   1 
ATOM   356  O  O   . ARG   A 1 52  ? 5.49682  12.61453  36.81871  1.000 21.30063 ? 48  ARG   A O   1 
ATOM   357  C  CB  . ARG   A 1 52  ? 8.41154  11.23579  36.91676  1.000 26.77089 ? 48  ARG   A CB  1 
ATOM   358  C  CG  . ARG   A 1 52  ? 8.45454  12.48454  37.77045  1.000 35.38937 ? 48  ARG   A CG  1 
ATOM   359  C  CD  . ARG   A 1 52  ? 9.84770  13.09968  37.72101  1.000 40.84895 ? 48  ARG   A CD  1 
ATOM   360  N  NE  . ARG   A 1 52  ? 9.95841  14.27962  38.56903  1.000 52.40799 ? 48  ARG   A NE  1 
ATOM   361  C  CZ  . ARG   A 1 52  ? 10.42232 14.26486  39.81031  1.000 38.93231 ? 48  ARG   A CZ  1 
ATOM   362  N  NH1 . ARG   A 1 52  ? 10.84592 13.14605  40.37579  1.000 42.02117 ? 48  ARG   A NH1 1 
ATOM   363  N  NH2 . ARG   A 1 52  ? 10.46086 15.40053  40.50165  1.000 40.03381 ? 48  ARG   A NH2 1 
ATOM   364  N  N   . VAL   A 1 53  ? 6.27680  12.50187  34.71648  1.000 19.96997 ? 49  VAL   A N   1 
ATOM   365  C  CA  . VAL   A 1 53  ? 5.58258  13.71093  34.28122  1.000 23.79528 ? 49  VAL   A CA  1 
ATOM   366  C  C   . VAL   A 1 53  ? 4.09443  13.40853  34.14101  1.000 29.18771 ? 49  VAL   A C   1 
ATOM   367  O  O   . VAL   A 1 53  ? 3.70004  12.51987  33.37831  1.000 32.06294 ? 49  VAL   A O   1 
ATOM   368  C  CB  . VAL   A 1 53  ? 6.16997  14.23570  32.96246  1.000 31.83437 ? 49  VAL   A CB  1 
ATOM   369  C  CG1 . VAL   A 1 53  ? 5.43604  15.49497  32.49978  1.000 25.47258 ? 49  VAL   A CG1 1 
ATOM   370  C  CG2 . VAL   A 1 53  ? 7.66131  14.49926  33.11999  1.000 28.75373 ? 49  VAL   A CG2 1 
ATOM   371  N  N   . GLY   A 1 54  ? 3.26623  14.14495  34.88274  1.000 22.94828 ? 50  GLY   A N   1 
ATOM   372  C  CA  . GLY   A 1 54  ? 1.82785  13.96544  34.83529  1.000 29.19616 ? 50  GLY   A CA  1 
ATOM   373  C  C   . GLY   A 1 54  ? 1.28195  12.83234  35.67653  1.000 27.18233 ? 50  GLY   A C   1 
ATOM   374  O  O   . GLY   A 1 54  ? 0.08464  12.53841  35.58785  1.000 30.26800 ? 50  GLY   A O   1 
ATOM   375  N  N   . LEU   A 1 55  ? 2.11013  12.19192  36.49131  1.000 23.66022 ? 51  LEU   A N   1 
ATOM   376  C  CA  . LEU   A 1 55  ? 1.66148  11.05026  37.27715  1.000 23.59644 ? 51  LEU   A CA  1 
ATOM   377  C  C   . LEU   A 1 55  ? 0.91032  11.53172  38.51353  1.000 24.42374 ? 51  LEU   A C   1 
ATOM   378  O  O   . LEU   A 1 55  ? 1.46121  12.31936  39.29042  1.000 19.64971 ? 51  LEU   A O   1 
ATOM   379  C  CB  . LEU   A 1 55  ? 2.84940  10.18690  37.68223  1.000 23.49259 ? 51  LEU   A CB  1 
ATOM   380  C  CG  . LEU   A 1 55  ? 2.53169  8.87952   38.40889  1.000 18.48131 ? 51  LEU   A CG  1 
ATOM   381  C  CD1 . LEU   A 1 55  ? 1.68132  7.96829   37.53556  1.000 27.51346 ? 51  LEU   A CD1 1 
ATOM   382  C  CD2 . LEU   A 1 55  ? 3.81156  8.18482   38.81877  1.000 20.23272 ? 51  LEU   A CD2 1 
ATOM   383  N  N   . PRO   A 1 56  ? -0.33202 11.10115  38.72808  1.000 25.15971 ? 52  PRO   A N   1 
ATOM   384  C  CA  . PRO   A 1 56  ? -1.07253 11.54485  39.91396  1.000 20.49636 ? 52  PRO   A CA  1 
ATOM   385  C  C   . PRO   A 1 56  ? -0.43360 11.04491  41.20154  1.000 19.09558 ? 52  PRO   A C   1 
ATOM   386  O  O   . PRO   A 1 56  ? 0.13033  9.94966   41.26337  1.000 17.96759 ? 52  PRO   A O   1 
ATOM   387  C  CB  . PRO   A 1 56  ? -2.46421 10.93496  39.71189  1.000 21.26577 ? 52  PRO   A CB  1 
ATOM   388  C  CG  . PRO   A 1 56  ? -2.56636 10.70602  38.23170  1.000 22.39744 ? 52  PRO   A CG  1 
ATOM   389  C  CD  . PRO   A 1 56  ? -1.17869 10.32650  37.80608  1.000 21.88028 ? 52  PRO   A CD  1 
ATOM   390  N  N   . ILE   A 1 57  ? -0.54163 11.87253  42.24447  1.000 19.32290 ? 53  ILE   A N   1 
ATOM   391  C  CA  . ILE   A 1 57  ? 0.07791  11.55187  43.52674  1.000 18.20419 ? 53  ILE   A CA  1 
ATOM   392  C  C   . ILE   A 1 57  ? -0.47382 10.25034  44.09604  1.000 19.30252 ? 53  ILE   A C   1 
ATOM   393  O  O   . ILE   A 1 57  ? 0.24976  9.49958   44.76158  1.000 16.37828 ? 53  ILE   A O   1 
ATOM   394  C  CB  . ILE   A 1 57  ? -0.10415 12.73022  44.50615  1.000 18.88973 ? 53  ILE   A CB  1 
ATOM   395  C  CG1 . ILE   A 1 57  ? 0.60589  12.44668  45.83059  1.000 17.95723 ? 53  ILE   A CG1 1 
ATOM   396  C  CG2 . ILE   A 1 57  ? -1.58769 13.04081  44.72084  1.000 20.10110 ? 53  ILE   A CG2 1 
ATOM   397  C  CD1 . ILE   A 1 57  ? 2.08380  12.17945  45.67776  1.000 16.99381 ? 53  ILE   A CD1 1 
ATOM   398  N  N   . ASN   A 1 58  ? -1.74828 9.94830   43.83723  1.000 22.21001 ? 54  ASN   A N   1 
ATOM   399  C  CA  . ASN   A 1 58  ? -2.34515 8.73199   44.37898  1.000 17.95767 ? 54  ASN   A CA  1 
ATOM   400  C  C   . ASN   A 1 58  ? -1.77420 7.46288   43.75925  1.000 25.59040 ? 54  ASN   A C   1 
ATOM   401  O  O   . ASN   A 1 58  ? -1.98567 6.37700   44.31032  1.000 21.36141 ? 54  ASN   A O   1 
ATOM   402  C  CB  . ASN   A 1 58  ? -3.86241 8.76760   44.19478  1.000 23.04367 ? 54  ASN   A CB  1 
ATOM   403  C  CG  . ASN   A 1 58  ? -4.27343 9.45943   42.91461  1.000 34.90738 ? 54  ASN   A CG  1 
ATOM   404  O  OD1 . ASN   A 1 58  ? -4.12098 8.91158   41.82207  1.000 49.22044 ? 54  ASN   A OD1 1 
ATOM   405  N  ND2 . ASN   A 1 58  ? -4.79885 10.67426  43.04084  1.000 43.85206 ? 54  ASN   A ND2 1 
ATOM   406  N  N   . GLN   A 1 59  ? -1.05228 7.56973   42.64458  1.000 22.40400 ? 55  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 59  ? -0.41941 6.42425   42.00516  1.000 17.77900 ? 55  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 59  ? 1.10067  6.46490   42.11113  1.000 15.58050 ? 55  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 59  ? 1.77968  5.64974   41.48028  1.000 19.90179 ? 55  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 59  ? -0.84447 6.34894   40.53584  1.000 18.69639 ? 55  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 59  ? -2.35207 6.33521   40.33644  1.000 24.23124 ? 55  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 59  ? -2.75138 6.49624   38.88131  1.000 42.39356 ? 55  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 59  ? -1.90225 6.51011   37.98933  1.000 36.35532 ? 55  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 59  ? -4.05112 6.62517   38.63510  1.000 38.22782 ? 55  GLN   A NE2 1 
ATOM   415  N  N   . ARG   A 1 60  ? 1.64868  7.37858   42.91214  1.000 14.93992 ? 56  ARG   A N   1 
ATOM   416  C  CA  . ARG   A 1 60  ? 3.08182  7.64947   42.87511  1.000 14.25056 ? 56  ARG   A CA  1 
ATOM   417  C  C   . ARG   A 1 60  ? 3.90751  6.63319   43.66165  1.000 13.08442 ? 56  ARG   A C   1 
ATOM   418  O  O   . ARG   A 1 60  ? 5.09313  6.44923   43.36443  1.000 12.52593 ? 56  ARG   A O   1 
ATOM   419  C  CB  . ARG   A 1 60  ? 3.34677  9.06266   43.40319  1.000 14.69861 ? 56  ARG   A CB  1 
ATOM   420  C  CG  . ARG   A 1 60  ? 4.81298  9.45697   43.43656  1.000 16.68040 ? 56  ARG   A CG  1 
ATOM   421  C  CD  . ARG   A 1 60  ? 5.42605  9.39679   42.05062  1.000 14.37627 ? 56  ARG   A CD  1 
ATOM   422  N  NE  . ARG   A 1 60  ? 6.84135  9.74400   42.07339  1.000 19.56710 ? 56  ARG   A NE  1 
ATOM   423  C  CZ  . ARG   A 1 60  ? 7.30470  10.98421  42.13913  1.000 21.07644 ? 56  ARG   A CZ  1 
ATOM   424  N  NH1 . ARG   A 1 60  ? 6.48940  12.02530  42.18053  1.000 23.34064 ? 56  ARG   A NH1 1 
ATOM   425  N  NH2 . ARG   A 1 60  ? 8.61955  11.18498  42.16529  1.000 30.43964 ? 56  ARG   A NH2 1 
ATOM   426  N  N   . PHE   A 1 61  ? 3.32683  5.96593   44.65716  1.000 12.82226 ? 57  PHE   A N   1 
ATOM   427  C  CA  . PHE   A 1 61  ? 4.11460  5.15066   45.57287  1.000 11.88534 ? 57  PHE   A CA  1 
ATOM   428  C  C   . PHE   A 1 61  ? 3.49383  3.77492   45.76803  1.000 11.73058 ? 57  PHE   A C   1 
ATOM   429  O  O   . PHE   A 1 61  ? 2.29834  3.56625   45.55192  1.000 12.39839 ? 57  PHE   A O   1 
ATOM   430  C  CB  . PHE   A 1 61  ? 4.26092  5.81887   46.95148  1.000 11.79521 ? 57  PHE   A CB  1 
ATOM   431  C  CG  . PHE   A 1 61  ? 4.91527  7.16967   46.91063  1.000 12.09334 ? 57  PHE   A CG  1 
ATOM   432  C  CD1 . PHE   A 1 61  ? 6.27169  7.28895   46.64746  1.000 11.64983 ? 57  PHE   A CD1 1 
ATOM   433  C  CD2 . PHE   A 1 61  ? 4.18052  8.31595   47.15902  1.000 12.96626 ? 57  PHE   A CD2 1 
ATOM   434  C  CE1 . PHE   A 1 61  ? 6.87842  8.52709   46.62010  1.000 12.10018 ? 57  PHE   A CE1 1 
ATOM   435  C  CE2 . PHE   A 1 61  ? 4.78475  9.56441   47.13255  1.000 13.42530 ? 57  PHE   A CE2 1 
ATOM   436  C  CZ  . PHE   A 1 61  ? 6.13572  9.66703   46.86424  1.000 13.00220 ? 57  PHE   A CZ  1 
ATOM   437  N  N   . ILE   A 1 62  ? 4.33983  2.83324   46.18972  1.000 10.97794 ? 58  ILE   A N   1 
ATOM   438  C  CA  . ILE   A 1 62  ? 3.90079  1.55737   46.73714  1.000 10.86859 ? 58  ILE   A CA  1 
ATOM   439  C  C   . ILE   A 1 62  ? 4.63688  1.34756   48.05250  1.000 11.76255 ? 58  ILE   A C   1 
ATOM   440  O  O   . ILE   A 1 62  ? 5.64891  1.99224   48.33335  1.000 16.25735 ? 58  ILE   A O   1 
ATOM   441  C  CB  . ILE   A 1 62  ? 4.14157  0.36362   45.78750  1.000 12.55585 ? 58  ILE   A CB  1 
ATOM   442  C  CG1 . ILE   A 1 62  ? 5.63664  0.09053   45.62232  1.000 12.08338 ? 58  ILE   A CG1 1 
ATOM   443  C  CG2 . ILE   A 1 62  ? 3.45164  0.59854   44.44583  1.000 11.51209 ? 58  ILE   A CG2 1 
ATOM   444  C  CD1 . ILE   A 1 62  ? 5.92733  -1.21486  44.88825  1.000 15.26174 ? 58  ILE   A CD1 1 
ATOM   445  N  N   . LEU   A 1 63  ? 4.11170  0.44087   48.86917  1.000 10.36042 ? 59  LEU   A N   1 
ATOM   446  C  CA  . LEU   A 1 63  ? 4.67223  0.18083   50.18600  1.000 9.99233  ? 59  LEU   A CA  1 
ATOM   447  C  C   . LEU   A 1 63  ? 5.06316  -1.28430  50.30511  1.000 12.06995 ? 59  LEU   A C   1 
ATOM   448  O  O   . LEU   A 1 63  ? 4.34358  -2.17244  49.83575  1.000 12.26624 ? 59  LEU   A O   1 
ATOM   449  C  CB  . LEU   A 1 63  ? 3.67847  0.55010   51.29545  1.000 10.49489 ? 59  LEU   A CB  1 
ATOM   450  C  CG  . LEU   A 1 63  ? 3.06989  1.94968   51.18149  1.000 17.11901 ? 59  LEU   A CG  1 
ATOM   451  C  CD1 . LEU   A 1 63  ? 1.96755  2.14639   52.22334  1.000 16.83203 ? 59  LEU   A CD1 1 
ATOM   452  C  CD2 . LEU   A 1 63  ? 4.14155  3.03257   51.30700  1.000 14.66269 ? 59  LEU   A CD2 1 
ATOM   453  N  N   . VAL   A 1 64  ? 6.20841  -1.52738  50.93307  1.000 9.75156  ? 60  VAL   A N   1 
ATOM   454  C  CA  . VAL   A 1 64  ? 6.70088  -2.87328  51.19472  1.000 13.15255 ? 60  VAL   A CA  1 
ATOM   455  C  C   . VAL   A 1 64  ? 6.79677  -3.03626  52.70380  1.000 11.61663 ? 60  VAL   A C   1 
ATOM   456  O  O   . VAL   A 1 64  ? 7.55956  -2.31984  53.36214  1.000 9.57372  ? 60  VAL   A O   1 
ATOM   457  C  CB  . VAL   A 1 64  ? 8.05829  -3.12628  50.51992  1.000 10.61770 ? 60  VAL   A CB  1 
ATOM   458  C  CG1 . VAL   A 1 64  ? 8.70361  -4.36762  51.08371  1.000 16.87681 ? 60  VAL   A CG1 1 
ATOM   459  C  CG2 . VAL   A 1 64  ? 7.87771  -3.26762  49.00610  1.000 17.91921 ? 60  VAL   A CG2 1 
ATOM   460  N  N   . GLU   A 1 65  ? 6.00821  -3.94849  53.25451  1.000 10.67978 ? 61  GLU   A N   1 
ATOM   461  C  CA  . GLU   A 1 65  ? 6.02969  -4.21447  54.68655  1.000 15.80127 ? 61  GLU   A CA  1 
ATOM   462  C  C   . GLU   A 1 65  ? 6.93730  -5.40672  54.94972  1.000 16.02915 ? 61  GLU   A C   1 
ATOM   463  O  O   . GLU   A 1 65  ? 6.67848  -6.51105  54.45649  1.000 18.49616 ? 61  GLU   A O   1 
ATOM   464  C  CB  . GLU   A 1 65  ? 4.63061  -4.48014  55.23640  1.000 15.58250 ? 61  GLU   A CB  1 
ATOM   465  C  CG  . GLU   A 1 65  ? 4.66202  -4.90382  56.69763  1.000 30.26063 ? 61  GLU   A CG  1 
ATOM   466  C  CD  . GLU   A 1 65  ? 3.48910  -4.37817  57.49218  1.000 42.52585 ? 61  GLU   A CD  1 
ATOM   467  O  OE1 . GLU   A 1 65  ? 2.34543  -4.79971  57.21870  1.000 43.44212 ? 61  GLU   A OE1 1 
ATOM   468  O  OE2 . GLU   A 1 65  ? 3.71367  -3.53675  58.38894  1.000 46.20753 ? 61  GLU   A OE2 1 
ATOM   469  N  N   . LEU   A 1 66  ? 7.99328  -5.18003  55.72385  1.000 12.38257 ? 62  LEU   A N   1 
ATOM   470  C  CA  . LEU   A 1 66  ? 8.97855  -6.20038  56.04317  1.000 13.19845 ? 62  LEU   A CA  1 
ATOM   471  C  C   . LEU   A 1 66  ? 8.81499  -6.62736  57.49399  1.000 14.72364 ? 62  LEU   A C   1 
ATOM   472  O  O   . LEU   A 1 66  ? 8.71250  -5.78074  58.38413  1.000 15.50627 ? 62  LEU   A O   1 
ATOM   473  C  CB  . LEU   A 1 66  ? 10.39593 -5.67798  55.81006  1.000 16.37461 ? 62  LEU   A CB  1 
ATOM   474  C  CG  . LEU   A 1 66  ? 10.74171 -5.22557  54.39266  1.000 13.36254 ? 62  LEU   A CG  1 
ATOM   475  C  CD1 . LEU   A 1 66  ? 12.18999 -4.76520  54.34037  1.000 8.44107  ? 62  LEU   A CD1 1 
ATOM   476  C  CD2 . LEU   A 1 66  ? 10.49335 -6.35043  53.39808  1.000 9.87581  ? 62  LEU   A CD2 1 
ATOM   477  N  N   . SER   A 1 67  ? 8.79202  -7.93483  57.72802  1.000 13.20887 ? 63  SER   A N   1 
ATOM   478  C  CA  . SER   A 1 67  ? 8.72485  -8.48339  59.07473  1.000 13.95042 ? 63  SER   A CA  1 
ATOM   479  C  C   . SER   A 1 67  ? 9.84462  -9.49746  59.24758  1.000 14.38360 ? 63  SER   A C   1 
ATOM   480  O  O   . SER   A 1 67  ? 10.31678 -10.08772 58.27210  1.000 13.89520 ? 63  SER   A O   1 
ATOM   481  C  CB  . SER   A 1 67  ? 7.36735  -9.14670  59.34998  1.000 18.97037 ? 63  SER   A CB  1 
ATOM   482  O  OG  . SER   A 1 67  ? 6.30131  -8.24812  59.10176  1.000 34.76929 ? 63  SER   A OG  1 
ATOM   483  N  N   . ASN   A 1 68  ? 10.28035 -9.69075  60.49369  1.000 13.11355 ? 64  ASN   A N   1 
ATOM   484  C  CA  . ASN   A 1 68  ? 11.33828 -10.66496 60.74165  1.000 15.20941 ? 64  ASN   A CA  1 
ATOM   485  C  C   . ASN   A 1 68  ? 10.95090 -11.65547 61.83586  1.000 13.85599 ? 64  ASN   A C   1 
ATOM   486  O  O   . ASN   A 1 68  ? 9.80513  -11.65309 62.29787  1.000 14.30586 ? 64  ASN   A O   1 
ATOM   487  C  CB  . ASN   A 1 68  ? 12.65899 -9.95588  61.07627  1.000 19.00233 ? 64  ASN   A CB  1 
ATOM   488  C  CG  . ASN   A 1 68  ? 12.61678 -9.17680  62.38655  1.000 14.33901 ? 64  ASN   A CG  1 
ATOM   489  O  OD1 . ASN   A 1 68  ? 11.63261 -9.20331  63.12691  1.000 15.43676 ? 64  ASN   A OD1 1 
ATOM   490  N  ND2 . ASN   A 1 68  ? 13.70748 -8.47896  62.67777  1.000 13.42645 ? 64  ASN   A ND2 1 
ATOM   491  N  N   . HIS   A 1 69  ? 11.89717 -12.51663 62.23663  1.000 14.45711 ? 65  HIS   A N   1 
ATOM   492  C  CA  . HIS   A 1 69  ? 11.60871 -13.55281 63.22818  1.000 15.72601 ? 65  HIS   A CA  1 
ATOM   493  C  C   . HIS   A 1 69  ? 11.19928 -12.95932 64.56668  1.000 18.55766 ? 65  HIS   A C   1 
ATOM   494  O  O   . HIS   A 1 69  ? 10.38032 -13.54939 65.28251  1.000 17.72949 ? 65  HIS   A O   1 
ATOM   495  C  CB  . HIS   A 1 69  ? 12.82448 -14.45780 63.43918  1.000 16.52403 ? 65  HIS   A CB  1 
ATOM   496  C  CG  . HIS   A 1 69  ? 13.05298 -15.44914 62.34279  1.000 16.53697 ? 65  HIS   A CG  1 
ATOM   497  N  ND1 . HIS   A 1 69  ? 13.66702 -15.11834 61.15567  1.000 19.88686 ? 65  HIS   A ND1 1 
ATOM   498  C  CD2 . HIS   A 1 69  ? 12.77871 -16.77248 62.26811  1.000 19.51835 ? 65  HIS   A CD2 1 
ATOM   499  C  CE1 . HIS   A 1 69  ? 13.75123 -16.19202 60.39155  1.000 23.30752 ? 65  HIS   A CE1 1 
ATOM   500  N  NE2 . HIS   A 1 69  ? 13.21866 -17.20919 61.04302  1.000 22.45296 ? 65  HIS   A NE2 1 
ATOM   501  N  N   . ALA   A 1 70  ? 11.77196 -11.81066 64.93315  1.000 18.85177 ? 66  ALA   A N   1 
ATOM   502  C  CA  . ALA   A 1 70  ? 11.38658 -11.11086 66.15236  1.000 15.95933 ? 66  ALA   A CA  1 
ATOM   503  C  C   . ALA   A 1 70  ? 10.03550 -10.42599 66.03301  1.000 16.37005 ? 66  ALA   A C   1 
ATOM   504  O  O   . ALA   A 1 70  ? 9.64116  -9.71616  66.96459  1.000 17.67104 ? 66  ALA   A O   1 
ATOM   505  C  CB  . ALA   A 1 70  ? 12.45235 -10.07844 66.52597  1.000 19.08154 ? 66  ALA   A CB  1 
ATOM   506  N  N   . GLU   A 1 71  ? 9.33685  -10.60503 64.90956  1.000 16.77614 ? 67  GLU   A N   1 
ATOM   507  C  CA  . GLU   A 1 71  ? 8.02046  -10.01289 64.67458  1.000 19.14647 ? 67  GLU   A CA  1 
ATOM   508  C  C   . GLU   A 1 71  ? 8.05687  -8.48762  64.74497  1.000 20.11639 ? 67  GLU   A C   1 
ATOM   509  O  O   . GLU   A 1 71  ? 7.06545  -7.84583  65.09855  1.000 22.27145 ? 67  GLU   A O   1 
ATOM   510  C  CB  . GLU   A 1 71  ? 6.97511  -10.58181 65.63932  1.000 18.43465 ? 67  GLU   A CB  1 
ATOM   511  C  CG  . GLU   A 1 71  ? 6.64280  -12.04569 65.35554  1.000 30.29678 ? 67  GLU   A CG  1 
ATOM   512  C  CD  . GLU   A 1 71  ? 5.74756  -12.66822 66.40943  1.000 51.47522 ? 67  GLU   A CD  1 
ATOM   513  O  OE1 . GLU   A 1 71  ? 4.90364  -11.94232 66.97634  1.000 41.78022 ? 67  GLU   A OE1 1 
ATOM   514  O  OE2 . GLU   A 1 71  ? 5.89628  -13.88303 66.67680  1.000 45.50375 ? 67  GLU   A OE2 1 
ATOM   515  N  N   . LEU   A 1 72  ? 9.19873  -7.89613  64.41057  1.000 13.68512 ? 68  LEU   A N   1 
ATOM   516  C  CA  . LEU   A 1 72  ? 9.28238  -6.45985  64.19486  1.000 13.39819 ? 68  LEU   A CA  1 
ATOM   517  C  C   . LEU   A 1 72  ? 8.93780  -6.16314  62.74273  1.000 15.54740 ? 68  LEU   A C   1 
ATOM   518  O  O   . LEU   A 1 72  ? 9.28499  -6.93197  61.84189  1.000 14.91997 ? 68  LEU   A O   1 
ATOM   519  C  CB  . LEU   A 1 72  ? 10.68015 -5.93628  64.52556  1.000 13.94109 ? 68  LEU   A CB  1 
ATOM   520  C  CG  . LEU   A 1 72  ? 11.18476 -6.30177  65.92320  1.000 16.53698 ? 68  LEU   A CG  1 
ATOM   521  C  CD1 . LEU   A 1 72  ? 12.57153 -5.73479  66.16015  1.000 25.87450 ? 68  LEU   A CD1 1 
ATOM   522  C  CD2 . LEU   A 1 72  ? 10.21364 -5.80912  66.98044  1.000 19.60011 ? 68  LEU   A CD2 1 
ATOM   523  N  N   . SER   A 1 73  ? 8.24430  -5.05343  62.51993  1.000 14.23048 ? 69  SER   A N   1 
ATOM   524  C  CA  . SER   A 1 73  ? 7.80145  -4.67834  61.18448  1.000 17.86764 ? 69  SER   A CA  1 
ATOM   525  C  C   . SER   A 1 73  ? 8.21235  -3.24658  60.88533  1.000 13.83783 ? 69  SER   A C   1 
ATOM   526  O  O   . SER   A 1 73  ? 8.10913  -2.37250  61.74748  1.000 12.78973 ? 69  SER   A O   1 
ATOM   527  C  CB  . SER   A 1 73  ? 6.28102  -4.81720  61.04184  1.000 24.03946 ? 69  SER   A CB  1 
ATOM   528  O  OG  . SER   A 1 73  ? 5.87390  -6.15970  61.23625  1.000 37.98989 ? 69  SER   A OG  1 
ATOM   529  N  N   . VAL   A 1 74  ? 8.69724  -3.01918  59.66635  1.000 11.77803 ? 70  VAL   A N   1 
ATOM   530  C  CA  . VAL   A 1 74  ? 8.90510  -1.67981  59.13352  1.000 9.96078  ? 70  VAL   A CA  1 
ATOM   531  C  C   . VAL   A 1 74  ? 8.27313  -1.64013  57.75088  1.000 11.25163 ? 70  VAL   A C   1 
ATOM   532  O  O   . VAL   A 1 74  ? 8.12378  -2.67234  57.08903  1.000 12.00701 ? 70  VAL   A O   1 
ATOM   533  C  CB  . VAL   A 1 74  ? 10.40025 -1.27934  59.06648  1.000 12.54841 ? 70  VAL   A CB  1 
ATOM   534  C  CG1 . VAL   A 1 74  ? 11.05264 -1.38491  60.44156  1.000 13.22601 ? 70  VAL   A CG1 1 
ATOM   535  C  CG2 . VAL   A 1 74  ? 11.14379 -2.12809  58.06116  1.000 12.25972 ? 70  VAL   A CG2 1 
ATOM   536  N  N   . THR   A 1 75  ? 7.87386  -0.44530  57.32335  1.000 9.95836  ? 71  THR   A N   1 
ATOM   537  C  CA  . THR   A 1 75  ? 7.20996  -0.27017  56.03717  1.000 9.53199  ? 71  THR   A CA  1 
ATOM   538  C  C   . THR   A 1 75  ? 8.04140  0.66989   55.18051  1.000 10.03694 ? 71  THR   A C   1 
ATOM   539  O  O   . THR   A 1 75  ? 8.19775  1.84604   55.51974  1.000 9.37731  ? 71  THR   A O   1 
ATOM   540  C  CB  . THR   A 1 75  ? 5.78803  0.27377   56.20250  1.000 15.44647 ? 71  THR   A CB  1 
ATOM   541  O  OG1 . THR   A 1 75  ? 4.99175  -0.66404  56.94067  1.000 17.05364 ? 71  THR   A OG1 1 
ATOM   542  C  CG2 . THR   A 1 75  ? 5.14883  0.47726   54.83960  1.000 12.95756 ? 71  THR   A CG2 1 
ATOM   543  N  N   . LEU   A 1 76  ? 8.56895  0.15087   54.07481  1.000 8.80487  ? 72  LEU   A N   1 
ATOM   544  C  CA  . LEU   A 1 76  ? 9.34271  0.95288   53.13893  1.000 13.96796 ? 72  LEU   A CA  1 
ATOM   545  C  C   . LEU   A 1 76  ? 8.41829  1.54113   52.08167  1.000 10.69214 ? 72  LEU   A C   1 
ATOM   546  O  O   . LEU   A 1 76  ? 7.46420  0.88846   51.64814  1.000 9.44074  ? 72  LEU   A O   1 
ATOM   547  C  CB  . LEU   A 1 76  ? 10.42747 0.10514   52.47087  1.000 9.83895  ? 72  LEU   A CB  1 
ATOM   548  C  CG  . LEU   A 1 76  ? 11.78261 -0.10763  53.15296  1.000 13.03626 ? 72  LEU   A CG  1 
ATOM   549  C  CD1 . LEU   A 1 76  ? 11.65556 -0.39213  54.63881  1.000 18.47513 ? 72  LEU   A CD1 1 
ATOM   550  C  CD2 . LEU   A 1 76  ? 12.50605 -1.25204  52.45331  1.000 27.71433 ? 72  LEU   A CD2 1 
ATOM   551  N  N   . ALA   A 1 77  ? 8.69906  2.77857   51.67550  1.000 8.95148  ? 73  ALA   A N   1 
ATOM   552  C  CA  . ALA   A 1 77  ? 7.98175  3.42965   50.58439  1.000 9.28054  ? 73  ALA   A CA  1 
ATOM   553  C  C   . ALA   A 1 77  ? 8.86781  3.47139   49.34715  1.000 9.21872  ? 73  ALA   A C   1 
ATOM   554  O  O   . ALA   A 1 77  ? 10.02386 3.89993   49.42342  1.000 11.13506 ? 73  ALA   A O   1 
ATOM   555  C  CB  . ALA   A 1 77  ? 7.55007  4.84582   50.96996  1.000 12.33132 ? 73  ALA   A CB  1 
ATOM   556  N  N   . LEU   A 1 78  ? 8.32402  3.02927   48.21443  1.000 11.01080 ? 74  LEU   A N   1 
ATOM   557  C  CA  . LEU   A 1 78  ? 9.03686  2.99129   46.94553  1.000 9.43181  ? 74  LEU   A CA  1 
ATOM   558  C  C   . LEU   A 1 78  ? 8.36758  3.91297   45.93991  1.000 10.41483 ? 74  LEU   A C   1 
ATOM   559  O  O   . LEU   A 1 78  ? 7.14033  3.92494   45.80927  1.000 12.69400 ? 74  LEU   A O   1 
ATOM   560  C  CB  . LEU   A 1 78  ? 9.09405  1.57019   46.35994  1.000 8.88645  ? 74  LEU   A CB  1 
ATOM   561  C  CG  . LEU   A 1 78  ? 10.22721 0.65314   46.81958  1.000 14.97629 ? 74  LEU   A CG  1 
ATOM   562  C  CD1 . LEU   A 1 78  ? 10.12825 0.37392   48.30381  1.000 18.92915 ? 74  LEU   A CD1 1 
ATOM   563  C  CD2 . LEU   A 1 78  ? 10.21491 -0.65199  46.02471  1.000 11.85631 ? 74  LEU   A CD2 1 
ATOM   564  N  N   . ASP   A 1 79  ? 9.19144  4.67950   45.23528  1.000 9.92353  ? 75  ASP   A N   1 
ATOM   565  C  CA  . ASP   A 1 79  ? 8.73337  5.52548   44.14303  1.000 12.51435 ? 75  ASP   A CA  1 
ATOM   566  C  C   . ASP   A 1 79  ? 8.53967  4.65774   42.90474  1.000 10.77353 ? 75  ASP   A C   1 
ATOM   567  O  O   . ASP   A 1 79  ? 9.45681  3.93965   42.49752  1.000 11.74869 ? 75  ASP   A O   1 
ATOM   568  C  CB  . ASP   A 1 79  ? 9.76855  6.62281   43.89088  1.000 13.01866 ? 75  ASP   A CB  1 
ATOM   569  C  CG  . ASP   A 1 79  ? 9.28671  7.69220   42.93703  1.000 15.30733 ? 75  ASP   A CG  1 
ATOM   570  O  OD1 . ASP   A 1 79  ? 8.56618  7.36932   41.97345  1.000 17.38388 ? 75  ASP   A OD1 1 
ATOM   571  O  OD2 . ASP   A 1 79  ? 9.65187  8.86664   43.15148  1.000 25.43228 ? 75  ASP   A OD2 1 
ATOM   572  N  N   . VAL   A 1 80  ? 7.34418  4.70657   42.31111  1.000 10.25860 ? 76  VAL   A N   1 
ATOM   573  C  CA  . VAL   A 1 80  ? 7.07095  3.85520   41.15641  1.000 10.24581 ? 76  VAL   A CA  1 
ATOM   574  C  C   . VAL   A 1 80  ? 7.80047  4.31105   39.90240  1.000 14.10726 ? 76  VAL   A C   1 
ATOM   575  O  O   . VAL   A 1 80  ? 7.88623  3.54244   38.93711  1.000 13.17341 ? 76  VAL   A O   1 
ATOM   576  C  CB  . VAL   A 1 80  ? 5.55934  3.77291   40.85608  1.000 11.17492 ? 76  VAL   A CB  1 
ATOM   577  C  CG1 . VAL   A 1 80  ? 4.80026  3.26572   42.08054  1.000 10.41259 ? 76  VAL   A CG1 1 
ATOM   578  C  CG2 . VAL   A 1 80  ? 5.02401  5.13150   40.39761  1.000 17.10123 ? 76  VAL   A CG2 1 
ATOM   579  N  N   . THR   A 1 81  ? 8.34108  5.53120   39.89306  1.000 11.10529 ? 77  THR   A N   1 
ATOM   580  C  CA  . THR   A 1 81  ? 9.00689  6.04134   38.70166  1.000 11.97093 ? 77  THR   A CA  1 
ATOM   581  C  C   . THR   A 1 81  ? 10.44075 5.54903   38.56578  1.000 12.27716 ? 77  THR   A C   1 
ATOM   582  O  O   . THR   A 1 81  ? 11.00326 5.63217   37.46828  1.000 13.84705 ? 77  THR   A O   1 
ATOM   583  C  CB  . THR   A 1 81  ? 8.98993  7.57017   38.69340  1.000 15.12508 ? 77  THR   A CB  1 
ATOM   584  O  OG1 . THR   A 1 81  ? 9.70171  8.06926   39.83582  1.000 15.33191 ? 77  THR   A OG1 1 
ATOM   585  C  CG2 . THR   A 1 81  ? 7.56038  8.07655   38.71890  1.000 17.75764 ? 77  THR   A CG2 1 
ATOM   586  N  N   . ASN   A 1 82  ? 11.04206 5.03314   39.64183  1.000 11.55389 ? 78  ASN   A N   1 
ATOM   587  C  CA  . ASN   A 1 82  ? 12.39061 4.48471   39.55694  1.000 12.08910 ? 78  ASN   A CA  1 
ATOM   588  C  C   . ASN   A 1 82  ? 12.59347 3.26427   40.45081  1.000 18.17198 ? 78  ASN   A C   1 
ATOM   589  O  O   . ASN   A 1 82  ? 13.72979 2.78418   40.55953  1.000 16.39342 ? 78  ASN   A O   1 
ATOM   590  C  CB  . ASN   A 1 82  ? 13.43519 5.55285   39.90900  1.000 14.64187 ? 78  ASN   A CB  1 
ATOM   591  C  CG  . ASN   A 1 82  ? 13.25424 6.11605   41.30976  1.000 23.29634 ? 78  ASN   A CG  1 
ATOM   592  O  OD1 . ASN   A 1 82  ? 12.52713 5.56203   42.13210  1.000 15.78036 ? 78  ASN   A OD1 1 
ATOM   593  N  ND2 . ASN   A 1 82  ? 13.92359 7.22720   41.58511  1.000 30.07264 ? 78  ASN   A ND2 1 
ATOM   594  N  N   . ALA   A 1 83  ? 11.54132 2.77015   41.10711  1.000 9.94171  ? 79  ALA   A N   1 
ATOM   595  C  CA  . ALA   A 1 83  ? 11.56964 1.56354   41.93940  1.000 12.35280 ? 79  ALA   A CA  1 
ATOM   596  C  C   . ALA   A 1 83  ? 12.44341 1.71042   43.18179  1.000 19.64327 ? 79  ALA   A C   1 
ATOM   597  O  O   . ALA   A 1 83  ? 12.79146 0.70869   43.81359  1.000 21.47306 ? 79  ALA   A O   1 
ATOM   598  C  CB  . ALA   A 1 83  ? 12.01874 0.33731   41.13402  1.000 19.24032 ? 79  ALA   A CB  1 
ATOM   599  N  N   . TYR   A 1 84  ? 12.79292 2.93068   43.57049  1.000 16.03479 ? 80  TYR   A N   1 
ATOM   600  C  CA  . TYR   A 1 84  ? 13.75070 3.14857   44.64483  1.000 22.67558 ? 80  TYR   A CA  1 
ATOM   601  C  C   . TYR   A 1 84  ? 13.05047 3.56087   45.93694  1.000 10.51412 ? 80  TYR   A C   1 
ATOM   602  O  O   . TYR   A 1 84  ? 12.00931 4.22448   45.92428  1.000 11.21061 ? 80  TYR   A O   1 
ATOM   603  C  CB  . TYR   A 1 84  ? 14.77171 4.21341   44.24260  1.000 21.20805 ? 80  TYR   A CB  1 
ATOM   604  C  CG  . TYR   A 1 84  ? 16.16866 4.00994   44.79890  1.000 15.01861 ? 80  TYR   A CG  1 
ATOM   605  C  CD1 . TYR   A 1 84  ? 17.08158 3.17989   44.15770  1.000 23.13987 ? 80  TYR   A CD1 1 
ATOM   606  C  CD2 . TYR   A 1 84  ? 16.58456 4.68052   45.94237  1.000 16.20756 ? 80  TYR   A CD2 1 
ATOM   607  C  CE1 . TYR   A 1 84  ? 18.36490 3.00582   44.65146  1.000 20.32729 ? 80  TYR   A CE1 1 
ATOM   608  C  CE2 . TYR   A 1 84  ? 17.86184 4.51054   46.44606  1.000 25.85490 ? 80  TYR   A CE2 1 
ATOM   609  C  CZ  . TYR   A 1 84  ? 18.74792 3.67248   45.79618  1.000 22.51410 ? 80  TYR   A CZ  1 
ATOM   610  O  OH  . TYR   A 1 84  ? 20.02215 3.50948   46.29491  1.000 18.96903 ? 80  TYR   A OH  1 
ATOM   611  N  N   . VAL   A 1 85  ? 13.64530 3.15675   47.05957  1.000 13.06506 ? 81  VAL   A N   1 
ATOM   612  C  CA  . VAL   A 1 85  ? 13.12678 3.52064   48.37111  1.000 7.44788  ? 81  VAL   A CA  1 
ATOM   613  C  C   . VAL   A 1 85  ? 13.30918 5.01625   48.59472  1.000 6.89680  ? 81  VAL   A C   1 
ATOM   614  O  O   . VAL   A 1 85  ? 14.39533 5.56242   48.36501  1.000 12.49922 ? 81  VAL   A O   1 
ATOM   615  C  CB  . VAL   A 1 85  ? 13.83903 2.71072   49.46746  1.000 11.86983 ? 81  VAL   A CB  1 
ATOM   616  C  CG1 . VAL   A 1 85  ? 13.34289 3.11892   50.84693  1.000 6.29170  ? 81  VAL   A CG1 1 
ATOM   617  C  CG2 . VAL   A 1 85  ? 13.65025 1.21882   49.24456  1.000 10.48152 ? 81  VAL   A CG2 1 
ATOM   618  N  N   . VAL   A 1 86  ? 12.25051 5.68252   49.06291  1.000 8.14224  ? 82  VAL   A N   1 
ATOM   619  C  CA  . VAL   A 1 86  ? 12.31032 7.09776   49.42690  1.000 7.02972  ? 82  VAL   A CA  1 
ATOM   620  C  C   . VAL   A 1 86  ? 12.28716 7.32468   50.93376  1.000 6.75238  ? 82  VAL   A C   1 
ATOM   621  O  O   . VAL   A 1 86  ? 12.57493 8.45014   51.37968  1.000 9.51820  ? 82  VAL   A O   1 
ATOM   622  C  CB  . VAL   A 1 86  ? 11.16722 7.90329   48.77155  1.000 10.19358 ? 82  VAL   A CB  1 
ATOM   623  C  CG1 . VAL   A 1 86  ? 11.19950 7.77262   47.24255  1.000 9.61248  ? 82  VAL   A CG1 1 
ATOM   624  C  CG2 . VAL   A 1 86  ? 9.82049  7.46925   49.32919  1.000 8.62705  ? 82  VAL   A CG2 1 
ATOM   625  N  N   . GLY   A 1 87  ? 11.93591 6.31917   51.72273  1.000 6.49161  ? 83  GLY   A N   1 
ATOM   626  C  CA  . GLY   A 1 87  ? 11.78179 6.49166   53.15361  1.000 10.37668 ? 83  GLY   A CA  1 
ATOM   627  C  C   . GLY   A 1 87  ? 11.10196 5.27646   53.74551  1.000 16.45379 ? 83  GLY   A C   1 
ATOM   628  O  O   . GLY   A 1 87  ? 10.76401 4.32312   53.04039  1.000 10.00305 ? 83  GLY   A O   1 
ATOM   629  N  N   . TYR   A 1 88  ? 10.90951 5.31945   55.06346  1.000 9.10220  ? 84  TYR   A N   1 
ATOM   630  C  CA  . TYR   A 1 88  ? 10.28608 4.19099   55.73606  1.000 7.44713  ? 84  TYR   A CA  1 
ATOM   631  C  C   . TYR   A 1 88  ? 9.60714  4.64292   57.01345  1.000 8.36340  ? 84  TYR   A C   1 
ATOM   632  O  O   . TYR   A 1 88  ? 9.87527  5.72307   57.54530  1.000 7.26616  ? 84  TYR   A O   1 
ATOM   633  C  CB  . TYR   A 1 88  ? 11.29299 3.07458   56.05460  1.000 6.80565  ? 84  TYR   A CB  1 
ATOM   634  C  CG  . TYR   A 1 88  ? 12.13734 3.26842   57.29508  1.000 8.03060  ? 84  TYR   A CG  1 
ATOM   635  C  CD1 . TYR   A 1 88  ? 13.28230 4.05108   57.26639  1.000 8.77303  ? 84  TYR   A CD1 1 
ATOM   636  C  CD2 . TYR   A 1 88  ? 11.81153 2.62551   58.49051  1.000 6.85602  ? 84  TYR   A CD2 1 
ATOM   637  C  CE1 . TYR   A 1 88  ? 14.07005 4.21483   58.40209  1.000 11.12366 ? 84  TYR   A CE1 1 
ATOM   638  C  CE2 . TYR   A 1 88  ? 12.59109 2.77685   59.62303  1.000 6.91928  ? 84  TYR   A CE2 1 
ATOM   639  C  CZ  . TYR   A 1 88  ? 13.72106 3.56760   59.57284  1.000 8.92135  ? 84  TYR   A CZ  1 
ATOM   640  O  OH  . TYR   A 1 88  ? 14.49691 3.71442   60.69647  1.000 11.73016 ? 84  TYR   A OH  1 
ATOM   641  N  N   . ARG   A 1 89  ? 8.73694  3.77254   57.50986  1.000 7.72036  ? 85  ARG   A N   1 
ATOM   642  C  CA  . ARG   A 1 89  ? 7.99548  4.00481   58.73600  1.000 10.77623 ? 85  ARG   A CA  1 
ATOM   643  C  C   . ARG   A 1 89  ? 8.28508  2.89069   59.72769  1.000 10.88093 ? 85  ARG   A C   1 
ATOM   644  O  O   . ARG   A 1 89  ? 8.28484  1.71069   59.36633  1.000 9.99051  ? 85  ARG   A O   1 
ATOM   645  C  CB  . ARG   A 1 89  ? 6.50242  4.07087   58.44311  1.000 11.82129 ? 85  ARG   A CB  1 
ATOM   646  C  CG  . ARG   A 1 89  ? 5.62642  4.25842   59.65763  1.000 11.20235 ? 85  ARG   A CG  1 
ATOM   647  C  CD  . ARG   A 1 89  ? 4.19156  4.16913   59.22794  1.000 21.15008 ? 85  ARG   A CD  1 
ATOM   648  N  NE  . ARG   A 1 89  ? 3.85450  2.83314   58.75267  1.000 35.68264 ? 85  ARG   A NE  1 
ATOM   649  C  CZ  . ARG   A 1 89  ? 2.74842  2.52960   58.08564  1.000 45.64508 ? 85  ARG   A CZ  1 
ATOM   650  N  NH1 . ARG   A 1 89  ? 1.85201  3.45277   57.77656  1.000 36.81362 ? 85  ARG   A NH1 1 
ATOM   651  N  NH2 . ARG   A 1 89  ? 2.53639  1.26743   57.71842  1.000 34.24589 ? 85  ARG   A NH2 1 
ATOM   652  N  N   . ALA   A 1 90  ? 8.52563  3.26472   60.98075  1.000 9.06878  ? 86  ALA   A N   1 
ATOM   653  C  CA  . ALA   A 1 90  ? 8.64830  2.28613   62.05581  1.000 12.55927 ? 86  ALA   A CA  1 
ATOM   654  C  C   . ALA   A 1 90  ? 7.93539  2.84122   63.27748  1.000 14.92652 ? 86  ALA   A C   1 
ATOM   655  O  O   . ALA   A 1 90  ? 8.30830  3.90612   63.77554  1.000 11.81057 ? 86  ALA   A O   1 
ATOM   656  C  CB  . ALA   A 1 90  ? 10.11429 1.97580   62.37301  1.000 12.50115 ? 86  ALA   A CB  1 
ATOM   657  N  N   . GLY   A 1 91  ? 6.90459  2.13583   63.73824  1.000 16.77698 ? 87  GLY   A N   1 
ATOM   658  C  CA  . GLY   A 1 91  ? 6.15280  2.60420   64.88961  1.000 14.71688 ? 87  GLY   A CA  1 
ATOM   659  C  C   . GLY   A 1 91  ? 5.59269  3.99199   64.65549  1.000 16.76681 ? 87  GLY   A C   1 
ATOM   660  O  O   . GLY   A 1 91  ? 4.92069  4.26118   63.65357  1.000 16.11563 ? 87  GLY   A O   1 
ATOM   661  N  N   . ASN   A 1 92  ? 5.90078  4.89979   65.57486  1.000 13.51253 ? 88  ASN   A N   1 
ATOM   662  C  CA  . ASN   A 1 92  ? 5.35021  6.24382   65.55938  1.000 14.01279 ? 88  ASN   A CA  1 
ATOM   663  C  C   . ASN   A 1 92  ? 6.23117  7.24705   64.81834  1.000 16.98679 ? 88  ASN   A C   1 
ATOM   664  O  O   . ASN   A 1 92  ? 5.98688  8.45332   64.92546  1.000 13.26020 ? 88  ASN   A O   1 
ATOM   665  C  CB  . ASN   A 1 92  ? 5.11676  6.71888   66.99520  1.000 15.32232 ? 88  ASN   A CB  1 
ATOM   666  C  CG  . ASN   A 1 92  ? 4.02353  7.76012   67.09560  1.000 25.05209 ? 88  ASN   A CG  1 
ATOM   667  O  OD1 . ASN   A 1 92  ? 3.15188  7.85473   66.22818  1.000 27.36103 ? 88  ASN   A OD1 1 
ATOM   668  N  ND2 . ASN   A 1 92  ? 4.05969  8.54785   68.16247  1.000 24.97917 ? 88  ASN   A ND2 1 
ATOM   669  N  N   . SER   A 1 93  ? 7.22835  6.78745   64.05430  1.000 12.05530 ? 89  SER   A N   1 
ATOM   670  C  CA  . SER   A 1 93  ? 8.13121  7.68490   63.34089  1.000 11.54236 ? 89  SER   A CA  1 
ATOM   671  C  C   . SER   A 1 93  ? 8.26802  7.27254   61.88186  1.000 13.41793 ? 89  SER   A C   1 
ATOM   672  O  O   . SER   A 1 93  ? 8.18009  6.08903   61.53863  1.000 14.09974 ? 89  SER   A O   1 
ATOM   673  C  CB  . SER   A 1 93  ? 9.52225  7.72027   63.98524  1.000 12.89197 ? 89  SER   A CB  1 
ATOM   674  O  OG  . SER   A 1 93  ? 9.45138  8.18536   65.32330  1.000 14.34363 ? 89  SER   A OG  1 
ATOM   675  N  N   . ALA   A 1 94  ? 8.49819  8.26975   61.02718  1.000 9.35732  ? 90  ALA   A N   1 
ATOM   676  C  CA  . ALA   A 1 94  ? 8.77713  8.06343   59.60974  1.000 8.65714  ? 90  ALA   A CA  1 
ATOM   677  C  C   . ALA   A 1 94  ? 10.01294 8.86059   59.22273  1.000 9.51307  ? 90  ALA   A C   1 
ATOM   678  O  O   . ALA   A 1 94  ? 10.18071 10.00688  59.65184  1.000 11.31055 ? 90  ALA   A O   1 
ATOM   679  C  CB  . ALA   A 1 94  ? 7.59896  8.48352   58.72882  1.000 12.13584 ? 90  ALA   A CB  1 
ATOM   680  N  N   . TYR   A 1 95  ? 10.86846 8.25325   58.40264  1.000 7.38240  ? 91  TYR   A N   1 
ATOM   681  C  CA  . TYR   A 1 95  ? 12.12695 8.85416   57.98307  1.000 7.30740  ? 91  TYR   A CA  1 
ATOM   682  C  C   . TYR   A 1 95  ? 12.19770 8.88041   56.46658  1.000 8.87146  ? 91  TYR   A C   1 
ATOM   683  O  O   . TYR   A 1 95  ? 11.86411 7.89045   55.81038  1.000 10.52612 ? 91  TYR   A O   1 
ATOM   684  C  CB  . TYR   A 1 95  ? 13.31583 8.08055   58.53753  1.000 9.31413  ? 91  TYR   A CB  1 
ATOM   685  C  CG  . TYR   A 1 95  ? 13.31465 8.01544   60.03894  1.000 12.31499 ? 91  TYR   A CG  1 
ATOM   686  C  CD1 . TYR   A 1 95  ? 12.64066 7.00194   60.70836  1.000 11.88061 ? 91  TYR   A CD1 1 
ATOM   687  C  CD2 . TYR   A 1 95  ? 13.97592 8.97393   60.79005  1.000 15.10929 ? 91  TYR   A CD2 1 
ATOM   688  C  CE1 . TYR   A 1 95  ? 12.63170 6.94272   62.08759  1.000 8.82525  ? 91  TYR   A CE1 1 
ATOM   689  C  CE2 . TYR   A 1 95  ? 13.97849 8.91834   62.17136  1.000 13.92081 ? 91  TYR   A CE2 1 
ATOM   690  C  CZ  . TYR   A 1 95  ? 13.30045 7.90330   62.81254  1.000 15.98747 ? 91  TYR   A CZ  1 
ATOM   691  O  OH  . TYR   A 1 95  ? 13.29442 7.84906   64.18883  1.000 17.20888 ? 91  TYR   A OH  1 
ATOM   692  N  N   . PHE   A 1 96  ? 12.65925 10.00388  55.91684  1.000 6.98330  ? 92  PHE   A N   1 
ATOM   693  C  CA  . PHE   A 1 96  ? 12.70899 10.20770  54.47583  1.000 7.60978  ? 92  PHE   A CA  1 
ATOM   694  C  C   . PHE   A 1 96  ? 14.10133 10.63818  54.04424  1.000 11.06236 ? 92  PHE   A C   1 
ATOM   695  O  O   . PHE   A 1 96  ? 14.74301 11.45589  54.71022  1.000 8.31681  ? 92  PHE   A O   1 
ATOM   696  C  CB  . PHE   A 1 96  ? 11.69557 11.26267  54.04256  1.000 9.66157  ? 92  PHE   A CB  1 
ATOM   697  C  CG  . PHE   A 1 96  ? 10.27214 10.87621  54.31058  1.000 13.01823 ? 92  PHE   A CG  1 
ATOM   698  C  CD1 . PHE   A 1 96  ? 9.56157  10.12595  53.38636  1.000 7.96182  ? 92  PHE   A CD1 1 
ATOM   699  C  CD2 . PHE   A 1 96  ? 9.64194  11.26418  55.48063  1.000 13.88082 ? 92  PHE   A CD2 1 
ATOM   700  C  CE1 . PHE   A 1 96  ? 8.24575  9.77145   53.62930  1.000 12.52566 ? 92  PHE   A CE1 1 
ATOM   701  C  CE2 . PHE   A 1 96  ? 8.32707  10.90842  55.73042  1.000 13.01580 ? 92  PHE   A CE2 1 
ATOM   702  C  CZ  . PHE   A 1 96  ? 7.63087  10.16037  54.80212  1.000 11.16439 ? 92  PHE   A CZ  1 
ATOM   703  N  N   . PHE   A 1 97  ? 14.56342 10.08617  52.92596  1.000 9.85296  ? 93  PHE   A N   1 
ATOM   704  C  CA  . PHE   A 1 97  ? 15.77555 10.59299  52.30309  1.000 7.31142  ? 93  PHE   A CA  1 
ATOM   705  C  C   . PHE   A 1 97  ? 15.55958 12.02190  51.82053  1.000 11.62939 ? 93  PHE   A C   1 
ATOM   706  O  O   . PHE   A 1 97  ? 14.44261 12.42814  51.48672  1.000 12.10794 ? 93  PHE   A O   1 
ATOM   707  C  CB  . PHE   A 1 97  ? 16.18918 9.70396   51.12802  1.000 12.51985 ? 93  PHE   A CB  1 
ATOM   708  C  CG  . PHE   A 1 97  ? 16.64998 8.33382   51.53598  1.000 12.93619 ? 93  PHE   A CG  1 
ATOM   709  C  CD1 . PHE   A 1 97  ? 17.62034 8.17617   52.51233  1.000 12.87814 ? 93  PHE   A CD1 1 
ATOM   710  C  CD2 . PHE   A 1 97  ? 16.10820 7.20276   50.94635  1.000 9.61246  ? 93  PHE   A CD2 1 
ATOM   711  C  CE1 . PHE   A 1 97  ? 18.04558 6.91367   52.88919  1.000 12.09303 ? 93  PHE   A CE1 1 
ATOM   712  C  CE2 . PHE   A 1 97  ? 16.53004 5.93919   51.31959  1.000 15.45898 ? 93  PHE   A CE2 1 
ATOM   713  C  CZ  . PHE   A 1 97  ? 17.49777 5.79546   52.29399  1.000 13.54062 ? 93  PHE   A CZ  1 
ATOM   714  N  N   . HIS   A 1 98  ? 16.64048 12.78656  51.79087  1.000 15.49100 ? 94  HIS   A N   1 
ATOM   715  C  CA  . HIS   A 1 98  ? 16.57095 14.15729  51.31092  1.000 11.32595 ? 94  HIS   A CA  1 
ATOM   716  C  C   . HIS   A 1 98  ? 16.09566 14.16262  49.86273  1.000 14.92940 ? 94  HIS   A C   1 
ATOM   717  O  O   . HIS   A 1 98  ? 16.73880 13.53547  49.00824  1.000 14.81065 ? 94  HIS   A O   1 
ATOM   718  C  CB  . HIS   A 1 98  ? 17.92650 14.83967  51.42262  1.000 9.82957  ? 94  HIS   A CB  1 
ATOM   719  C  CG  . HIS   A 1 98  ? 17.88059 16.31102  51.15317  1.000 19.84976 ? 94  HIS   A CG  1 
ATOM   720  N  ND1 . HIS   A 1 98  ? 18.10051 16.84720  49.90230  1.000 28.51717 ? 94  HIS   A ND1 1 
ATOM   721  C  CD2 . HIS   A 1 98  ? 17.63356 17.35934  51.97422  1.000 25.90180 ? 94  HIS   A CD2 1 
ATOM   722  C  CE1 . HIS   A 1 98  ? 17.99545 18.16312  49.96552  1.000 22.69669 ? 94  HIS   A CE1 1 
ATOM   723  N  NE2 . HIS   A 1 98  ? 17.71231 18.49950  51.21117  1.000 26.05202 ? 94  HIS   A NE2 1 
ATOM   724  N  N   . PRO   A 1 99  ? 14.98809 14.82956  49.54697  1.000 13.22875 ? 95  PRO   A N   1 
ATOM   725  C  CA  . PRO   A 1 99  ? 14.46911 14.78787  48.17527  1.000 21.00908 ? 95  PRO   A CA  1 
ATOM   726  C  C   . PRO   A 1 99  ? 15.36820 15.53919  47.20886  1.000 14.76394 ? 95  PRO   A C   1 
ATOM   727  O  O   . PRO   A 1 99  ? 15.98169 16.55418  47.54840  1.000 19.81199 ? 95  PRO   A O   1 
ATOM   728  C  CB  . PRO   A 1 99  ? 13.09654 15.46094  48.29367  1.000 20.75605 ? 95  PRO   A CB  1 
ATOM   729  C  CG  . PRO   A 1 99  ? 13.21829 16.34628  49.48945  1.000 28.33877 ? 95  PRO   A CG  1 
ATOM   730  C  CD  . PRO   A 1 99  ? 14.13055 15.62267  50.44295  1.000 18.04729 ? 95  PRO   A CD  1 
ATOM   731  N  N   . ASP   A 1 100 ? 15.43271 15.02414  45.97872  1.000 25.06874 ? 96  ASP   A N   1 
ATOM   732  C  CA  . ASP   A 1 100 ? 16.27104 15.63495  44.95352  1.000 29.11083 ? 96  ASP   A CA  1 
ATOM   733  C  C   . ASP   A 1 100 ? 15.69929 16.94697  44.43072  1.000 26.00947 ? 96  ASP   A C   1 
ATOM   734  O  O   . ASP   A 1 100 ? 16.44364 17.73925  43.84305  1.000 29.25133 ? 96  ASP   A O   1 
ATOM   735  C  CB  . ASP   A 1 100 ? 16.47432 14.65738  43.79257  1.000 33.70884 ? 96  ASP   A CB  1 
ATOM   736  C  CG  . ASP   A 1 100 ? 17.25525 13.41907  44.19951  1.000 53.84324 ? 96  ASP   A CG  1 
ATOM   737  O  OD1 . ASP   A 1 100 ? 18.26663 13.55997  44.91986  1.000 50.88522 ? 96  ASP   A OD1 1 
ATOM   738  O  OD2 . ASP   A 1 100 ? 16.85553 12.30353  43.80434  1.000 62.33394 ? 96  ASP   A OD2 1 
ATOM   739  N  N   . ASN   A 1 101 ? 14.40807 17.19958  44.62935  1.000 18.71247 ? 97  ASN   A N   1 
ATOM   740  C  CA  . ASN   A 1 101 ? 13.78096 18.39920  44.08864  1.000 18.09847 ? 97  ASN   A CA  1 
ATOM   741  C  C   . ASN   A 1 101 ? 12.52170 18.71038  44.88077  1.000 21.01538 ? 97  ASN   A C   1 
ATOM   742  O  O   . ASN   A 1 101 ? 12.05585 17.90907  45.69396  1.000 19.32217 ? 97  ASN   A O   1 
ATOM   743  C  CB  . ASN   A 1 101 ? 13.45158 18.24178  42.60160  1.000 18.75346 ? 97  ASN   A CB  1 
ATOM   744  C  CG  . ASN   A 1 101 ? 12.78485 16.92302  42.29207  1.000 25.13213 ? 97  ASN   A CG  1 
ATOM   745  O  OD1 . ASN   A 1 101 ? 11.60590 16.72241  42.58704  1.000 21.62213 ? 97  ASN   A OD1 1 
ATOM   746  N  ND2 . ASN   A 1 101 ? 13.53772 16.01147  41.68508  1.000 23.38334 ? 97  ASN   A ND2 1 
ATOM   747  N  N   . GLN   A 1 102 ? 11.96671 19.89081  44.60769  1.000 19.24765 ? 98  GLN   A N   1 
ATOM   748  C  CA  . GLN   A 1 102 ? 10.80969 20.37218  45.35077  1.000 26.55524 ? 98  GLN   A CA  1 
ATOM   749  C  C   . GLN   A 1 102 ? 9.54216  19.62254  44.96608  1.000 23.19914 ? 98  GLN   A C   1 
ATOM   750  O  O   . GLN   A 1 102 ? 8.62839  19.49269  45.78946  1.000 22.09133 ? 98  GLN   A O   1 
ATOM   751  C  CB  . GLN   A 1 102 ? 10.64462 21.87760  45.12556  1.000 31.36773 ? 98  GLN   A CB  1 
ATOM   752  C  CG  . GLN   A 1 102 ? 9.47100  22.51272  45.85228  1.000 33.26563 ? 98  GLN   A CG  1 
ATOM   753  C  CD  . GLN   A 1 102 ? 9.54363  22.34637  47.35725  1.000 30.81972 ? 98  GLN   A CD  1 
ATOM   754  O  OE1 . GLN   A 1 102 ? 10.62647 22.29760  47.94050  1.000 32.02808 ? 98  GLN   A OE1 1 
ATOM   755  N  NE2 . GLN   A 1 102 ? 8.38371  22.25653  47.99510  1.000 33.09853 ? 98  GLN   A NE2 1 
ATOM   756  N  N   . GLU   A 1 103 ? 9.46366  19.12117  43.73094  1.000 27.72786 ? 99  GLU   A N   1 
ATOM   757  C  CA  . GLU   A 1 103 ? 8.32710  18.28436  43.36028  1.000 28.24762 ? 99  GLU   A CA  1 
ATOM   758  C  C   . GLU   A 1 103 ? 8.30596  17.00296  44.18713  1.000 24.27837 ? 99  GLU   A C   1 
ATOM   759  O  O   . GLU   A 1 103 ? 7.24688  16.57652  44.66102  1.000 15.84660 ? 99  GLU   A O   1 
ATOM   760  C  CB  . GLU   A 1 103 ? 8.36726  17.96752  41.86465  1.000 28.99213 ? 99  GLU   A CB  1 
ATOM   761  C  CG  . GLU   A 1 103 ? 7.02867  17.51567  41.29597  1.000 41.75003 ? 99  GLU   A CG  1 
ATOM   762  C  CD  . GLU   A 1 103 ? 7.12525  17.02847  39.85986  1.000 56.26317 ? 99  GLU   A CD  1 
ATOM   763  O  OE1 . GLU   A 1 103 ? 7.66578  17.76888  39.00900  1.000 50.77488 ? 99  GLU   A OE1 1 
ATOM   764  O  OE2 . GLU   A 1 103 ? 6.66389  15.89804  39.58612  1.000 45.08452 ? 99  GLU   A OE2 1 
ATOM   765  N  N   . ASP   A 1 104 ? 9.47350  16.39028  44.39501  1.000 17.49903 ? 100 ASP   A N   1 
ATOM   766  C  CA  . ASP   A 1 104 ? 9.54098  15.19641  45.23044  1.000 18.35487 ? 100 ASP   A CA  1 
ATOM   767  C  C   . ASP   A 1 104 ? 9.33147  15.52698  46.70347  1.000 19.71780 ? 100 ASP   A C   1 
ATOM   768  O  O   . ASP   A 1 104 ? 8.77322  14.71064  47.44548  1.000 14.83322 ? 100 ASP   A O   1 
ATOM   769  C  CB  . ASP   A 1 104 ? 10.88187 14.48851  45.02966  1.000 16.83877 ? 100 ASP   A CB  1 
ATOM   770  C  CG  . ASP   A 1 104 ? 11.00587 13.84539  43.65711  1.000 39.97082 ? 100 ASP   A CG  1 
ATOM   771  O  OD1 . ASP   A 1 104 ? 9.99848  13.81773  42.91530  1.000 29.44406 ? 100 ASP   A OD1 1 
ATOM   772  O  OD2 . ASP   A 1 104 ? 12.11389 13.36969  43.32011  1.000 30.74199 ? 100 ASP   A OD2 1 
ATOM   773  N  N   . ALA   A 1 105 ? 9.77632  16.70654  47.14596  1.000 19.91099 ? 101 ALA   A N   1 
ATOM   774  C  CA  . ALA   A 1 105 ? 9.56302  17.10231  48.53487  1.000 21.39289 ? 101 ALA   A CA  1 
ATOM   775  C  C   . ALA   A 1 105 ? 8.07698  17.21464  48.85234  1.000 23.93907 ? 101 ALA   A C   1 
ATOM   776  O  O   . ALA   A 1 105 ? 7.63394  16.82605  49.94027  1.000 21.77697 ? 101 ALA   A O   1 
ATOM   777  C  CB  . ALA   A 1 105 ? 10.27502 18.42511  48.81999  1.000 24.86363 ? 101 ALA   A CB  1 
ATOM   778  N  N   . GLU   A 1 106 ? 7.29169  17.74438  47.91243  1.000 15.15073 ? 102 GLU   A N   1 
ATOM   779  C  CA  . GLU   A 1 106 ? 5.84664  17.82616  48.10714  1.000 17.34073 ? 102 GLU   A CA  1 
ATOM   780  C  C   . GLU   A 1 106 ? 5.19347  16.45245  48.00938  1.000 17.70745 ? 102 GLU   A C   1 
ATOM   781  O  O   . GLU   A 1 106 ? 4.21216  16.17508  48.70810  1.000 20.15775 ? 102 GLU   A O   1 
ATOM   782  C  CB  . GLU   A 1 106 ? 5.23506  18.78224  47.08371  1.000 21.67275 ? 102 GLU   A CB  1 
ATOM   783  C  CG  . GLU   A 1 106 ? 5.42677  20.25075  47.42041  1.000 26.47598 ? 102 GLU   A CG  1 
ATOM   784  C  CD  . GLU   A 1 106 ? 5.31993  21.14468  46.20435  1.000 50.46848 ? 102 GLU   A CD  1 
ATOM   785  O  OE1 . GLU   A 1 106 ? 5.41266  20.62241  45.07271  1.000 61.12145 ? 102 GLU   A OE1 1 
ATOM   786  O  OE2 . GLU   A 1 106 ? 5.15111  22.37001  46.37606  1.000 40.33021 ? 102 GLU   A OE2 1 
ATOM   787  N  N   . ALA   A 1 107 ? 5.71908  15.58152  47.14589  1.000 15.66408 ? 103 ALA   A N   1 
ATOM   788  C  CA  . ALA   A 1 107 ? 5.11926  14.26151  46.97638  1.000 20.38907 ? 103 ALA   A CA  1 
ATOM   789  C  C   . ALA   A 1 107 ? 5.20910  13.43734  48.25658  1.000 16.17627 ? 103 ALA   A C   1 
ATOM   790  O  O   . ALA   A 1 107 ? 4.24849  12.75525  48.63137  1.000 17.08957 ? 103 ALA   A O   1 
ATOM   791  C  CB  . ALA   A 1 107 ? 5.78988  13.52417  45.81654  1.000 18.29172 ? 103 ALA   A CB  1 
ATOM   792  N  N   . ILE   A 1 108 ? 6.35475  13.48399  48.94391  1.000 12.98320 ? 104 ILE   A N   1 
ATOM   793  C  CA  . ILE   A 1 108 ? 6.53829  12.63753  50.12267  1.000 17.89779 ? 104 ILE   A CA  1 
ATOM   794  C  C   . ILE   A 1 108 ? 5.76842  13.12480  51.33929  1.000 16.25708 ? 104 ILE   A C   1 
ATOM   795  O  O   . ILE   A 1 108 ? 5.63431  12.36905  52.30831  1.000 15.16581 ? 104 ILE   A O   1 
ATOM   796  C  CB  . ILE   A 1 108 ? 8.02340  12.49427  50.51023  1.000 18.23446 ? 104 ILE   A CB  1 
ATOM   797  C  CG1 . ILE   A 1 108 ? 8.61877  13.85253  50.89471  1.000 17.50329 ? 104 ILE   A CG1 1 
ATOM   798  C  CG2 . ILE   A 1 108 ? 8.81139  11.84166  49.37778  1.000 15.85914 ? 104 ILE   A CG2 1 
ATOM   799  C  CD1 . ILE   A 1 108 ? 10.01094 13.75939  51.48867  1.000 20.17847 ? 104 ILE   A CD1 1 
ATOM   800  N  N   . THR   A 1 109 ? 5.24326  14.35371  51.32577  1.000 18.03089 ? 105 THR   A N   1 
ATOM   801  C  CA  . THR   A 1 109 ? 4.38691  14.77252  52.43066  1.000 17.64296 ? 105 THR   A CA  1 
ATOM   802  C  C   . THR   A 1 109 ? 3.09103  13.97642  52.47298  1.000 22.82646 ? 105 THR   A C   1 
ATOM   803  O  O   . THR   A 1 109 ? 2.39261  14.00618  53.49096  1.000 19.10383 ? 105 THR   A O   1 
ATOM   804  C  CB  . THR   A 1 109 ? 4.06548  16.27157  52.35519  1.000 14.65937 ? 105 THR   A CB  1 
ATOM   805  O  OG1 . THR   A 1 109 ? 3.25176  16.54470  51.20724  1.000 16.61330 ? 105 THR   A OG1 1 
ATOM   806  C  CG2 . THR   A 1 109 ? 5.34651  17.09305  52.27827  1.000 28.10469 ? 105 THR   A CG2 1 
ATOM   807  N  N   . HIS   A 1 110 ? 2.75628  13.26844  51.39716  1.000 18.94947 ? 106 HIS   A N   1 
ATOM   808  C  CA  . HIS   A 1 110 ? 1.56746  12.42891  51.35554  1.000 18.69838 ? 106 HIS   A CA  1 
ATOM   809  C  C   . HIS   A 1 110 ? 1.82323  11.01987  51.87125  1.000 19.08435 ? 106 HIS   A C   1 
ATOM   810  O  O   . HIS   A 1 110 ? 0.89906  10.19920  51.87940  1.000 20.49548 ? 106 HIS   A O   1 
ATOM   811  C  CB  . HIS   A 1 110 ? 1.02285  12.36622  49.92691  1.000 15.08321 ? 106 HIS   A CB  1 
ATOM   812  C  CG  . HIS   A 1 110 ? 0.64004  13.70305  49.37602  1.000 20.02971 ? 106 HIS   A CG  1 
ATOM   813  N  ND1 . HIS   A 1 110 ? -0.66511 14.14218  49.33007  1.000 32.47275 ? 106 HIS   A ND1 1 
ATOM   814  C  CD2 . HIS   A 1 110 ? 1.39360  14.70794  48.86948  1.000 23.09288 ? 106 HIS   A CD2 1 
ATOM   815  C  CE1 . HIS   A 1 110 ? -0.70056 15.35609  48.80953  1.000 30.32861 ? 106 HIS   A CE1 1 
ATOM   816  N  NE2 . HIS   A 1 110 ? 0.53582  15.72375  48.52532  1.000 20.14988 ? 106 HIS   A NE2 1 
ATOM   817  N  N   . LEU   A 1 111 ? 3.04347  10.72150  52.30031  1.000 13.05774 ? 107 LEU   A N   1 
ATOM   818  C  CA  . LEU   A 1 111 ? 3.39640  9.40231   52.80266  1.000 15.15030 ? 107 LEU   A CA  1 
ATOM   819  C  C   . LEU   A 1 111 ? 3.37865  9.39582   54.32328  1.000 14.87610 ? 107 LEU   A C   1 
ATOM   820  O  O   . LEU   A 1 111 ? 3.89075  10.31940  54.96263  1.000 14.47336 ? 107 LEU   A O   1 
ATOM   821  C  CB  . LEU   A 1 111 ? 4.77978  8.97762   52.30478  1.000 11.29560 ? 107 LEU   A CB  1 
ATOM   822  C  CG  . LEU   A 1 111 ? 4.89605  8.46187   50.86883  1.000 10.52789 ? 107 LEU   A CG  1 
ATOM   823  C  CD1 . LEU   A 1 111 ? 6.36129  8.38258   50.46249  1.000 8.94196  ? 107 LEU   A CD1 1 
ATOM   824  C  CD2 . LEU   A 1 111 ? 4.23585  7.09402   50.74227  1.000 11.74437 ? 107 LEU   A CD2 1 
ATOM   825  N  N   . PHE   A 1 112 ? 2.78194  8.34740   54.89554  1.000 16.87070 ? 108 PHE   A N   1 
ATOM   826  C  CA  . PHE   A 1 112 ? 2.85243  8.09432   56.33277  1.000 13.98161 ? 108 PHE   A CA  1 
ATOM   827  C  C   . PHE   A 1 112 ? 2.33076  9.28396   57.13496  1.000 21.21434 ? 108 PHE   A C   1 
ATOM   828  O  O   . PHE   A 1 112 ? 2.91037  9.67130   58.14929  1.000 19.18223 ? 108 PHE   A O   1 
ATOM   829  C  CB  . PHE   A 1 112 ? 4.28293  7.74693   56.75256  1.000 10.78403 ? 108 PHE   A CB  1 
ATOM   830  C  CG  . PHE   A 1 112 ? 4.86654  6.56469   56.02350  1.000 11.11930 ? 108 PHE   A CG  1 
ATOM   831  C  CD1 . PHE   A 1 112 ? 4.12365  5.40971   55.83721  1.000 10.24481 ? 108 PHE   A CD1 1 
ATOM   832  C  CD2 . PHE   A 1 112 ? 6.15861  6.61372   55.52600  1.000 10.58328 ? 108 PHE   A CD2 1 
ATOM   833  C  CE1 . PHE   A 1 112 ? 4.66515  4.31710   55.16659  1.000 9.57718  ? 108 PHE   A CE1 1 
ATOM   834  C  CE2 . PHE   A 1 112 ? 6.70807  5.53277   54.85569  1.000 12.45285 ? 108 PHE   A CE2 1 
ATOM   835  C  CZ  . PHE   A 1 112 ? 5.95962  4.37963   54.67510  1.000 10.96660 ? 108 PHE   A CZ  1 
ATOM   836  N  N   . THR   A 1 113 ? 1.22609  9.87060   56.67925  1.000 14.17087 ? 109 THR   A N   1 
ATOM   837  C  CA  . THR   A 1 113 ? 0.78618  11.14640  57.22870  1.000 25.21417 ? 109 THR   A CA  1 
ATOM   838  C  C   . THR   A 1 113 ? 0.14711  11.02391  58.60306  1.000 30.27573 ? 109 THR   A C   1 
ATOM   839  O  O   . THR   A 1 113 ? -0.02068 12.04486  59.27755  1.000 38.85306 ? 109 THR   A O   1 
ATOM   840  C  CB  . THR   A 1 113 ? -0.19545 11.81532  56.26999  1.000 26.96940 ? 109 THR   A CB  1 
ATOM   841  O  OG1 . THR   A 1 113 ? -1.39864 11.04448  56.20725  1.000 40.63806 ? 109 THR   A OG1 1 
ATOM   842  C  CG2 . THR   A 1 113 ? 0.40866  11.90612  54.88237  1.000 39.57377 ? 109 THR   A CG2 1 
ATOM   843  N  N   . ASP   A 1 114 ? -0.21049 9.81683   59.03275  1.000 26.57215 ? 110 ASP   A N   1 
ATOM   844  C  CA  . ASP   A 1 114 ? -0.75953 9.60360   60.36307  1.000 32.11873 ? 110 ASP   A CA  1 
ATOM   845  C  C   . ASP   A 1 114 ? 0.32291  9.33249   61.39733  1.000 34.29888 ? 110 ASP   A C   1 
ATOM   846  O  O   . ASP   A 1 114 ? 0.00366  9.03165   62.55319  1.000 34.04969 ? 110 ASP   A O   1 
ATOM   847  C  CB  . ASP   A 1 114 ? -1.76429 8.44952   60.34533  1.000 34.81089 ? 110 ASP   A CB  1 
ATOM   848  C  CG  . ASP   A 1 114 ? -1.12782 7.13005   59.96512  1.000 40.93275 ? 110 ASP   A CG  1 
ATOM   849  O  OD1 . ASP   A 1 114 ? -0.19564 7.13781   59.13301  1.000 33.56792 ? 110 ASP   A OD1 1 
ATOM   850  O  OD2 . ASP   A 1 114 ? -1.55934 6.08549   60.49857  1.000 52.95455 ? 110 ASP   A OD2 1 
ATOM   851  N  N   . VAL   A 1 115 ? 1.58715  9.42868   61.00681  1.000 27.83192 ? 111 VAL   A N   1 
ATOM   852  C  CA  . VAL   A 1 115 ? 2.69665  9.24967   61.93075  1.000 28.40604 ? 111 VAL   A CA  1 
ATOM   853  C  C   . VAL   A 1 115 ? 2.87177  10.52874  62.73979  1.000 21.01634 ? 111 VAL   A C   1 
ATOM   854  O  O   . VAL   A 1 115 ? 2.68048  11.63882  62.22711  1.000 19.28752 ? 111 VAL   A O   1 
ATOM   855  C  CB  . VAL   A 1 115 ? 3.97319  8.86885   61.15415  1.000 26.84224 ? 111 VAL   A CB  1 
ATOM   856  C  CG1 . VAL   A 1 115 ? 4.76018  10.09749  60.71213  1.000 31.18039 ? 111 VAL   A CG1 1 
ATOM   857  C  CG2 . VAL   A 1 115 ? 4.82932  7.95689   61.96611  1.000 30.12600 ? 111 VAL   A CG2 1 
ATOM   858  N  N   . GLN   A 1 116 ? 3.20588  10.38150  64.02510  1.000 15.84444 ? 112 GLN   A N   1 
ATOM   859  C  CA  . GLN   A 1 116 ? 3.36185  11.56150  64.87280  1.000 17.56753 ? 112 GLN   A CA  1 
ATOM   860  C  C   . GLN   A 1 116 ? 4.66096  12.30740  64.59561  1.000 15.37931 ? 112 GLN   A C   1 
ATOM   861  O  O   . GLN   A 1 116 ? 4.69184  13.54001  64.68936  1.000 21.86477 ? 112 GLN   A O   1 
ATOM   862  C  CB  . GLN   A 1 116 ? 3.29976  11.17721  66.35158  1.000 19.60189 ? 112 GLN   A CB  1 
ATOM   863  C  CG  . GLN   A 1 116 ? 1.90637  11.22285  66.95957  1.000 19.79613 ? 112 GLN   A CG  1 
ATOM   864  C  CD  . GLN   A 1 116 ? 1.93080  11.28868  68.47938  1.000 24.78879 ? 112 GLN   A CD  1 
ATOM   865  O  OE1 . GLN   A 1 116 ? 2.77561  10.67141  69.12868  1.000 22.44745 ? 112 GLN   A OE1 1 
ATOM   866  N  NE2 . GLN   A 1 116 ? 1.00708  12.05047  69.05137  1.000 29.01379 ? 112 GLN   A NE2 1 
ATOM   867  N  N   . ASN   A 1 117 ? 5.73012  11.59439  64.25257  1.000 13.90023 ? 113 ASN   A N   1 
ATOM   868  C  CA  . ASN   A 1 117 ? 7.05752  12.17893  64.09184  1.000 13.22963 ? 113 ASN   A CA  1 
ATOM   869  C  C   . ASN   A 1 117 ? 7.54289  11.95953  62.66465  1.000 14.96708 ? 113 ASN   A C   1 
ATOM   870  O  O   . ASN   A 1 117 ? 7.68218  10.81313  62.22637  1.000 20.19659 ? 113 ASN   A O   1 
ATOM   871  C  CB  . ASN   A 1 117 ? 8.03533  11.55906  65.08790  1.000 12.43723 ? 113 ASN   A CB  1 
ATOM   872  C  CG  . ASN   A 1 117 ? 7.53226  11.63420  66.51215  1.000 16.88500 ? 113 ASN   A CG  1 
ATOM   873  O  OD1 . ASN   A 1 117 ? 7.14148  12.70422  66.98737  1.000 16.61850 ? 113 ASN   A OD1 1 
ATOM   874  N  ND2 . ASN   A 1 117 ? 7.52183  10.49538  67.19992  1.000 20.84817 ? 113 ASN   A ND2 1 
ATOM   875  N  N   . ARG   A 1 118 ? 7.80552  13.05374  61.94950  1.000 13.11272 ? 114 ARG   A N   1 
ATOM   876  C  CA  . ARG   A 1 118 ? 8.33167  13.01671  60.58903  1.000 15.02322 ? 114 ARG   A CA  1 
ATOM   877  C  C   . ARG   A 1 118 ? 9.73620  13.60207  60.57352  1.000 14.35292 ? 114 ARG   A C   1 
ATOM   878  O  O   . ARG   A 1 118 ? 9.95749  14.70584  61.08910  1.000 14.39130 ? 114 ARG   A O   1 
ATOM   879  C  CB  . ARG   A 1 118 ? 7.44959  13.81057  59.61943  1.000 19.81570 ? 114 ARG   A CB  1 
ATOM   880  C  CG  . ARG   A 1 118 ? 5.98403  13.44423  59.62201  1.000 30.94595 ? 114 ARG   A CG  1 
ATOM   881  C  CD  . ARG   A 1 118 ? 5.20169  14.29798  58.62660  1.000 23.61492 ? 114 ARG   A CD  1 
ATOM   882  N  NE  . ARG   A 1 118 ? 5.52715  13.97599  57.24137  1.000 22.87509 ? 114 ARG   A NE  1 
ATOM   883  C  CZ  . ARG   A 1 118 ? 5.05673  12.91478  56.59970  1.000 22.24209 ? 114 ARG   A CZ  1 
ATOM   884  N  NH1 . ARG   A 1 118 ? 4.26125  12.04302  57.19934  1.000 18.28911 ? 114 ARG   A NH1 1 
ATOM   885  N  NH2 . ARG   A 1 118 ? 5.38845  12.72528  55.32558  1.000 14.60870 ? 114 ARG   A NH2 1 
ATOM   886  N  N   . TYR   A 1 119 ? 10.66548 12.88782  59.94494  1.000 13.29291 ? 115 TYR   A N   1 
ATOM   887  C  CA  . TYR   A 1 119 ? 12.05882 13.29921  59.85933  1.000 9.22298  ? 115 TYR   A CA  1 
ATOM   888  C  C   . TYR   A 1 119 ? 12.55159 13.16162  58.42847  1.000 11.93671 ? 115 TYR   A C   1 
ATOM   889  O  O   . TYR   A 1 119 ? 12.27268 12.16015  57.76150  1.000 14.29441 ? 115 TYR   A O   1 
ATOM   890  C  CB  . TYR   A 1 119 ? 12.94659 12.45466  60.77826  1.000 8.34230  ? 115 TYR   A CB  1 
ATOM   891  C  CG  . TYR   A 1 119 ? 12.52046 12.45263  62.23028  1.000 10.80303 ? 115 TYR   A CG  1 
ATOM   892  C  CD1 . TYR   A 1 119 ? 12.78330 13.53819  63.05370  1.000 16.62156 ? 115 TYR   A CD1 1 
ATOM   893  C  CD2 . TYR   A 1 119 ? 11.86312 11.35834  62.77809  1.000 14.23045 ? 115 TYR   A CD2 1 
ATOM   894  C  CE1 . TYR   A 1 119 ? 12.40072 13.53601  64.37996  1.000 20.76717 ? 115 TYR   A CE1 1 
ATOM   895  C  CE2 . TYR   A 1 119 ? 11.48106 11.34347  64.10613  1.000 12.83470 ? 115 TYR   A CE2 1 
ATOM   896  C  CZ  . TYR   A 1 119 ? 11.74920 12.43592  64.90243  1.000 23.08728 ? 115 TYR   A CZ  1 
ATOM   897  O  OH  . TYR   A 1 119 ? 11.36754 12.43060  66.22644  1.000 21.46585 ? 115 TYR   A OH  1 
ATOM   898  N  N   . THR   A 1 120 ? 13.30347 14.15555  57.96581  1.000 9.57422  ? 116 THR   A N   1 
ATOM   899  C  CA  . THR   A 1 120 ? 13.97539 14.08125  56.67646  1.000 8.36270  ? 116 THR   A CA  1 
ATOM   900  C  C   . THR   A 1 120 ? 15.47644 14.18970  56.89632  1.000 13.22441 ? 116 THR   A C   1 
ATOM   901  O  O   . THR   A 1 120 ? 15.94301 15.11808  57.56535  1.000 13.53784 ? 116 THR   A O   1 
ATOM   902  C  CB  . THR   A 1 120 ? 13.48807 15.17965  55.73005  1.000 13.88107 ? 116 THR   A CB  1 
ATOM   903  O  OG1 . THR   A 1 120 ? 12.07881 15.02877  55.52179  1.000 17.00611 ? 116 THR   A OG1 1 
ATOM   904  C  CG2 . THR   A 1 120 ? 14.20794 15.08195  54.38436  1.000 10.35812 ? 116 THR   A CG2 1 
ATOM   905  N  N   . PHE   A 1 121 ? 16.22149 13.23078  56.35426  1.000 11.81679 ? 117 PHE   A N   1 
ATOM   906  C  CA  . PHE   A 1 121 ? 17.67120 13.23388  56.47230  1.000 12.21021 ? 117 PHE   A CA  1 
ATOM   907  C  C   . PHE   A 1 121 ? 18.28116 14.30314  55.57136  1.000 12.01582 ? 117 PHE   A C   1 
ATOM   908  O  O   . PHE   A 1 121 ? 17.65663 14.78976  54.62385  1.000 16.32469 ? 117 PHE   A O   1 
ATOM   909  C  CB  . PHE   A 1 121 ? 18.25639 11.87103  56.08680  1.000 13.01830 ? 117 PHE   A CB  1 
ATOM   910  C  CG  . PHE   A 1 121 ? 17.88502 10.74835  57.01447  1.000 10.85424 ? 117 PHE   A CG  1 
ATOM   911  C  CD1 . PHE   A 1 121 ? 18.22802 10.79122  58.35850  1.000 13.92472 ? 117 PHE   A CD1 1 
ATOM   912  C  CD2 . PHE   A 1 121 ? 17.22620 9.62713   56.53172  1.000 9.37903  ? 117 PHE   A CD2 1 
ATOM   913  C  CE1 . PHE   A 1 121 ? 17.90105 9.74750   59.20298  1.000 19.05961 ? 117 PHE   A CE1 1 
ATOM   914  C  CE2 . PHE   A 1 121 ? 16.89526 8.57727   57.37451  1.000 17.88180 ? 117 PHE   A CE2 1 
ATOM   915  C  CZ  . PHE   A 1 121 ? 17.23248 8.64012   58.71458  1.000 13.98991 ? 117 PHE   A CZ  1 
ATOM   916  N  N   . ALA   A 1 122 ? 19.53660 14.64943  55.86376  1.000 12.62105 ? 118 ALA   A N   1 
ATOM   917  C  CA  . ALA   A 1 122 ? 20.28173 15.55994  55.00342  1.000 17.86569 ? 118 ALA   A CA  1 
ATOM   918  C  C   . ALA   A 1 122 ? 20.89658 14.85482  53.80085  1.000 22.79108 ? 118 ALA   A C   1 
ATOM   919  O  O   . ALA   A 1 122 ? 21.29669 15.52669  52.84110  1.000 20.20340 ? 118 ALA   A O   1 
ATOM   920  C  CB  . ALA   A 1 122 ? 21.37867 16.26325  55.80389  1.000 26.57524 ? 118 ALA   A CB  1 
ATOM   921  N  N   . PHE   A 1 123 ? 20.97276 13.52705  53.83194  1.000 14.82896 ? 119 PHE   A N   1 
ATOM   922  C  CA  . PHE   A 1 123 ? 21.56074 12.73370  52.76502  1.000 16.44080 ? 119 PHE   A CA  1 
ATOM   923  C  C   . PHE   A 1 123 ? 20.47266 12.06434  51.93403  1.000 17.37212 ? 119 PHE   A C   1 
ATOM   924  O  O   . PHE   A 1 123 ? 19.37803 11.77012  52.42331  1.000 10.11980 ? 119 PHE   A O   1 
ATOM   925  C  CB  . PHE   A 1 123 ? 22.51642 11.67313  53.32893  1.000 13.45998 ? 119 PHE   A CB  1 
ATOM   926  C  CG  . PHE   A 1 123 ? 21.92098 10.82261  54.42521  1.000 15.23955 ? 119 PHE   A CG  1 
ATOM   927  C  CD1 . PHE   A 1 123 ? 21.22243 9.66585   54.12397  1.000 10.53221 ? 119 PHE   A CD1 1 
ATOM   928  C  CD2 . PHE   A 1 123 ? 22.07846 11.17437  55.76030  1.000 21.06093 ? 119 PHE   A CD2 1 
ATOM   929  C  CE1 . PHE   A 1 123 ? 20.67981 8.87909   55.13172  1.000 18.83633 ? 119 PHE   A CE1 1 
ATOM   930  C  CE2 . PHE   A 1 123 ? 21.54164 10.39331  56.76971  1.000 14.85635 ? 119 PHE   A CE2 1 
ATOM   931  C  CZ  . PHE   A 1 123 ? 20.84229 9.24558   56.45643  1.000 16.44081 ? 119 PHE   A CZ  1 
ATOM   932  N  N   . GLY   A 1 124 ? 20.78570 11.83950  50.65827  1.000 17.47419 ? 120 GLY   A N   1 
ATOM   933  C  CA  . GLY   A 1 124 ? 19.89687 11.12832  49.76843  1.000 21.97887 ? 120 GLY   A CA  1 
ATOM   934  C  C   . GLY   A 1 124 ? 20.10531 9.62716   49.84560  1.000 19.01186 ? 120 GLY   A C   1 
ATOM   935  O  O   . GLY   A 1 124 ? 20.97980 9.12055   50.54873  1.000 23.20488 ? 120 GLY   A O   1 
ATOM   936  N  N   . GLY   A 1 125 ? 19.27410 8.90840   49.09981  1.000 15.02015 ? 121 GLY   A N   1 
ATOM   937  C  CA  . GLY   A 1 125 ? 19.31010 7.46308   49.10139  1.000 14.10915 ? 121 GLY   A CA  1 
ATOM   938  C  C   . GLY   A 1 125 ? 20.35210 6.82994   48.21091  1.000 22.34830 ? 121 GLY   A C   1 
ATOM   939  O  O   . GLY   A 1 125 ? 20.37024 5.60399   48.08280  1.000 21.63015 ? 121 GLY   A O   1 
ATOM   940  N  N   . ASN   A 1 126 ? 21.22813 7.61902   47.59304  1.000 19.49698 ? 122 ASN   A N   1 
ATOM   941  C  CA  . ASN   A 1 126 ? 22.18609 7.06657   46.64616  1.000 15.10687 ? 122 ASN   A CA  1 
ATOM   942  C  C   . ASN   A 1 126 ? 23.28975 6.29458   47.36644  1.000 17.75336 ? 122 ASN   A C   1 
ATOM   943  O  O   . ASN   A 1 126 ? 23.66716 6.60966   48.49932  1.000 17.46446 ? 122 ASN   A O   1 
ATOM   944  C  CB  . ASN   A 1 126 ? 22.78875 8.17895   45.78756  1.000 19.34383 ? 122 ASN   A CB  1 
ATOM   945  C  CG  . ASN   A 1 126 ? 23.55639 9.19559   46.60349  1.000 34.46260 ? 122 ASN   A CG  1 
ATOM   946  O  OD1 . ASN   A 1 126 ? 24.78327 9.13460   46.69519  1.000 35.45604 ? 122 ASN   A OD1 1 
ATOM   947  N  ND2 . ASN   A 1 126 ? 22.83701 10.14034  47.20420  1.000 34.70561 ? 122 ASN   A ND2 1 
ATOM   948  N  N   . TYR   A 1 127 ? 23.80396 5.26569   46.68473  1.000 18.86622 ? 123 TYR   A N   1 
ATOM   949  C  CA  . TYR   A 1 127 ? 24.82043 4.39433   47.26808  1.000 13.07482 ? 123 TYR   A CA  1 
ATOM   950  C  C   . TYR   A 1 127 ? 26.06935 5.15450   47.68245  1.000 13.75221 ? 123 TYR   A C   1 
ATOM   951  O  O   . TYR   A 1 127 ? 26.72528 4.77060   48.65707  1.000 13.79797 ? 123 TYR   A O   1 
ATOM   952  C  CB  . TYR   A 1 127 ? 25.21286 3.30286   46.27595  1.000 10.47191 ? 123 TYR   A CB  1 
ATOM   953  C  CG  . TYR   A 1 127 ? 24.14849 2.26790   46.04622  1.000 26.35568 ? 123 TYR   A CG  1 
ATOM   954  C  CD1 . TYR   A 1 127 ? 23.43779 1.72694   47.11057  1.000 20.26507 ? 123 TYR   A CD1 1 
ATOM   955  C  CD2 . TYR   A 1 127 ? 23.85193 1.82927   44.76441  1.000 22.22610 ? 123 TYR   A CD2 1 
ATOM   956  C  CE1 . TYR   A 1 127 ? 22.46558 0.77625   46.90065  1.000 19.78160 ? 123 TYR   A CE1 1 
ATOM   957  C  CE2 . TYR   A 1 127 ? 22.88437 0.88249   44.54636  1.000 14.96411 ? 123 TYR   A CE2 1 
ATOM   958  C  CZ  . TYR   A 1 127 ? 22.19473 0.36196   45.61229  1.000 15.61470 ? 123 TYR   A CZ  1 
ATOM   959  O  OH  . TYR   A 1 127 ? 21.22653 -0.58219  45.39540  1.000 20.46198 ? 123 TYR   A OH  1 
ATOM   960  N  N   . ASP   A 1 128 ? 26.43691 6.20287   46.94037  1.000 16.36593 ? 124 ASP   A N   1 
ATOM   961  C  CA  . ASP   A 1 128 ? 27.68335 6.90744   47.22483  1.000 20.00498 ? 124 ASP   A CA  1 
ATOM   962  C  C   . ASP   A 1 128 ? 27.72431 7.39469   48.66848  1.000 20.09570 ? 124 ASP   A C   1 
ATOM   963  O  O   . ASP   A 1 128 ? 28.68391 7.12455   49.40007  1.000 16.96872 ? 124 ASP   A O   1 
ATOM   964  C  CB  . ASP   A 1 128 ? 27.86459 8.07208   46.25418  1.000 18.66054 ? 124 ASP   A CB  1 
ATOM   965  C  CG  . ASP   A 1 128 ? 28.12985 7.61044   44.83455  1.000 44.10449 ? 124 ASP   A CG  1 
ATOM   966  O  OD1 . ASP   A 1 128 ? 28.01514 6.39410   44.57030  1.000 40.00479 ? 124 ASP   A OD1 1 
ATOM   967  O  OD2 . ASP   A 1 128 ? 28.45944 8.46270   43.98277  1.000 54.13789 ? 124 ASP   A OD2 1 
ATOM   968  N  N   . ARG   A 1 129 ? 26.67772 8.09238   49.10676  1.000 18.87280 ? 125 ARG   A N   1 
ATOM   969  C  CA  . ARG   A 1 129 ? 26.68306 8.61764   50.46573  1.000 18.73379 ? 125 ARG   A CA  1 
ATOM   970  C  C   . ARG   A 1 129 ? 26.34845 7.54920   51.49752  1.000 14.78345 ? 125 ARG   A C   1 
ATOM   971  O  O   . ARG   A 1 129 ? 26.88570 7.58855   52.60894  1.000 11.90494 ? 125 ARG   A O   1 
ATOM   972  C  CB  . ARG   A 1 129 ? 25.71387 9.79484   50.58968  1.000 20.63753 ? 125 ARG   A CB  1 
ATOM   973  C  CG  . ARG   A 1 129 ? 25.77970 10.50815  51.94177  1.000 25.88931 ? 125 ARG   A CG  1 
ATOM   974  C  CD  . ARG   A 1 129 ? 27.21741 10.87095  52.32470  1.000 31.06141 ? 125 ARG   A CD  1 
ATOM   975  N  NE  . ARG   A 1 129 ? 27.28751 11.61748  53.57715  1.000 44.19596 ? 125 ARG   A NE  1 
ATOM   976  C  CZ  . ARG   A 1 129 ? 28.40562 11.86436  54.24863  1.000 36.50118 ? 125 ARG   A CZ  1 
ATOM   977  N  NH1 . ARG   A 1 129 ? 29.57965 11.42169  53.82807  1.000 32.21500 ? 125 ARG   A NH1 1 
ATOM   978  N  NH2 . ARG   A 1 129 ? 28.34406 12.57153  55.37303  1.000 35.28746 ? 125 ARG   A NH2 1 
ATOM   979  N  N   . LEU   A 1 130 ? 25.48005 6.58960   51.16138  1.000 11.48446 ? 126 LEU   A N   1 
ATOM   980  C  CA  . LEU   A 1 130 ? 25.15640 5.54094   52.12617  1.000 13.42087 ? 126 LEU   A CA  1 
ATOM   981  C  C   . LEU   A 1 130 ? 26.38698 4.71102   52.46694  1.000 12.04048 ? 126 LEU   A C   1 
ATOM   982  O  O   . LEU   A 1 130 ? 26.60796 4.36575   53.63495  1.000 9.90104  ? 126 LEU   A O   1 
ATOM   983  C  CB  . LEU   A 1 130 ? 24.03932 4.64296   51.59453  1.000 9.33372  ? 126 LEU   A CB  1 
ATOM   984  C  CG  . LEU   A 1 130 ? 22.64547 5.26161   51.47754  1.000 15.66327 ? 126 LEU   A CG  1 
ATOM   985  C  CD1 . LEU   A 1 130 ? 21.67247 4.24846   50.88265  1.000 17.11352 ? 126 LEU   A CD1 1 
ATOM   986  C  CD2 . LEU   A 1 130 ? 22.16325 5.76684   52.83724  1.000 17.92392 ? 126 LEU   A CD2 1 
ATOM   987  N  N   . GLU   A 1 131 ? 27.19804 4.37792   51.45734  1.000 11.80497 ? 127 GLU   A N   1 
ATOM   988  C  CA  . GLU   A 1 131 ? 28.44715 3.66566   51.71325  1.000 11.60379 ? 127 GLU   A CA  1 
ATOM   989  C  C   . GLU   A 1 131 ? 29.36603 4.46926   52.62599  1.000 11.25698 ? 127 GLU   A C   1 
ATOM   990  O  O   . GLU   A 1 131 ? 30.04543 3.90430   53.49130  1.000 11.65767 ? 127 GLU   A O   1 
ATOM   991  C  CB  . GLU   A 1 131 ? 29.15000 3.34904   50.39257  1.000 10.62029 ? 127 GLU   A CB  1 
ATOM   992  C  CG  . GLU   A 1 131 ? 28.48741 2.24612   49.57301  1.000 9.98793  ? 127 GLU   A CG  1 
ATOM   993  C  CD  . GLU   A 1 131 ? 29.05435 2.14814   48.16061  1.000 19.78189 ? 127 GLU   A CD  1 
ATOM   994  O  OE1 . GLU   A 1 131 ? 29.54465 3.17606   47.64077  1.000 11.93700 ? 127 GLU   A OE1 1 
ATOM   995  O  OE2 . GLU   A 1 131 ? 29.02041 1.04501   47.56850  1.000 17.74224 ? 127 GLU   A OE2 1 
ATOM   996  N  N   . GLN   A 1 132 ? 29.41112 5.78876   52.43801  1.000 12.98783 ? 128 GLN   A N   1 
ATOM   997  C  CA  . GLN   A 1 132 ? 30.23217 6.62629   53.30485  1.000 12.88975 ? 128 GLN   A CA  1 
ATOM   998  C  C   . GLN   A 1 132 ? 29.71229 6.62143   54.73861  1.000 16.27173 ? 128 GLN   A C   1 
ATOM   999  O  O   . GLN   A 1 132 ? 30.49957 6.52264   55.68823  1.000 13.92853 ? 128 GLN   A O   1 
ATOM   1000 C  CB  . GLN   A 1 132 ? 30.29329 8.04443   52.74040  1.000 14.47440 ? 128 GLN   A CB  1 
ATOM   1001 C  CG  . GLN   A 1 132 ? 31.14141 8.12333   51.48308  1.000 17.31780 ? 128 GLN   A CG  1 
ATOM   1002 C  CD  . GLN   A 1 132 ? 30.98731 9.42995   50.74091  1.000 23.92183 ? 128 GLN   A CD  1 
ATOM   1003 O  OE1 . GLN   A 1 132 ? 30.33281 10.35740  51.21748  1.000 29.69965 ? 128 GLN   A OE1 1 
ATOM   1004 N  NE2 . GLN   A 1 132 ? 31.58791 9.50879   49.55872  1.000 20.44614 ? 128 GLN   A NE2 1 
ATOM   1005 N  N   . LEU   A 1 133 ? 28.39158 6.71101   54.91920  1.000 12.97812 ? 129 LEU   A N   1 
ATOM   1006 C  CA  . LEU   A 1 133 ? 27.83273 6.65666   56.26720  1.000 12.17997 ? 129 LEU   A CA  1 
ATOM   1007 C  C   . LEU   A 1 133 ? 28.00970 5.27533   56.88214  1.000 13.03063 ? 129 LEU   A C   1 
ATOM   1008 O  O   . LEU   A 1 133 ? 28.24555 5.15165   58.08938  1.000 18.45019 ? 129 LEU   A O   1 
ATOM   1009 C  CB  . LEU   A 1 133 ? 26.35536 7.04631   56.23829  1.000 14.73203 ? 129 LEU   A CB  1 
ATOM   1010 C  CG  . LEU   A 1 133 ? 26.04099 8.48853   55.83632  1.000 24.40743 ? 129 LEU   A CG  1 
ATOM   1011 C  CD1 . LEU   A 1 133 ? 24.57245 8.63902   55.44978  1.000 23.03450 ? 129 LEU   A CD1 1 
ATOM   1012 C  CD2 . LEU   A 1 133 ? 26.39463 9.43571   56.97143  1.000 18.59551 ? 129 LEU   A CD2 1 
ATOM   1013 N  N   . ALA   A 1 134 ? 27.90391 4.22265   56.06839  1.000 12.74469 ? 130 ALA   A N   1 
ATOM   1014 C  CA  . ALA   A 1 134 ? 28.05376 2.86470   56.57601  1.000 12.05101 ? 130 ALA   A CA  1 
ATOM   1015 C  C   . ALA   A 1 134 ? 29.49970 2.51486   56.89492  1.000 15.20639 ? 130 ALA   A C   1 
ATOM   1016 O  O   . ALA   A 1 134 ? 29.74029 1.59568   57.68356  1.000 15.69207 ? 130 ALA   A O   1 
ATOM   1017 C  CB  . ALA   A 1 134 ? 27.49076 1.85669   55.56832  1.000 10.16820 ? 130 ALA   A CB  1 
ATOM   1018 N  N   . GLY   A 1 135 ? 30.46163 3.23235   56.32087  1.000 15.44895 ? 131 GLY   A N   1 
ATOM   1019 C  CA  . GLY   A 1 135 ? 31.84913 2.86160   56.49001  1.000 13.71828 ? 131 GLY   A CA  1 
ATOM   1020 C  C   . GLY   A 1 135 ? 32.27071 1.65277   55.68767  1.000 14.76042 ? 131 GLY   A C   1 
ATOM   1021 O  O   . GLY   A 1 135 ? 33.29555 1.04391   55.99983  1.000 15.17481 ? 131 GLY   A O   1 
ATOM   1022 N  N   . ASN   A 1 136 ? 31.50961 1.28700   54.65532  1.000 15.07384 ? 132 ASN   A N   1 
ATOM   1023 C  CA  . ASN   A 1 136 ? 31.82673 0.12409   53.83695  1.000 15.86923 ? 132 ASN   A CA  1 
ATOM   1024 C  C   . ASN   A 1 136 ? 31.18363 0.27118   52.46716  1.000 13.27833 ? 132 ASN   A C   1 
ATOM   1025 O  O   . ASN   A 1 136 ? 30.05833 0.76491   52.35387  1.000 10.73512 ? 132 ASN   A O   1 
ATOM   1026 C  CB  . ASN   A 1 136 ? 31.34293 -1.17833  54.48455  1.000 18.14410 ? 132 ASN   A CB  1 
ATOM   1027 C  CG  . ASN   A 1 136 ? 32.37857 -1.79533  55.39585  1.000 23.93161 ? 132 ASN   A CG  1 
ATOM   1028 O  OD1 . ASN   A 1 136 ? 32.08228 -2.16038  56.53380  1.000 32.90886 ? 132 ASN   A OD1 1 
ATOM   1029 N  ND2 . ASN   A 1 136 ? 33.60488 -1.91446  54.90104  1.000 21.34182 ? 132 ASN   A ND2 1 
ATOM   1030 N  N   . LEU   A 1 137 ? 31.90158 -0.17915  51.43965  1.000 13.43057 ? 133 LEU   A N   1 
ATOM   1031 C  CA  . LEU   A 1 137 ? 31.34035 -0.28829  50.10110  1.000 13.17721 ? 133 LEU   A CA  1 
ATOM   1032 C  C   . LEU   A 1 137 ? 30.36654 -1.46174  50.01574  1.000 16.25622 ? 133 LEU   A C   1 
ATOM   1033 O  O   . LEU   A 1 137 ? 30.39617 -2.38727  50.82996  1.000 13.23701 ? 133 LEU   A O   1 
ATOM   1034 C  CB  . LEU   A 1 137 ? 32.45172 -0.47060  49.06781  1.000 12.43496 ? 133 LEU   A CB  1 
ATOM   1035 C  CG  . LEU   A 1 137 ? 33.39767 0.71096   48.86488  1.000 13.12103 ? 133 LEU   A CG  1 
ATOM   1036 C  CD1 . LEU   A 1 137 ? 34.56746 0.30425   47.98862  1.000 22.85019 ? 133 LEU   A CD1 1 
ATOM   1037 C  CD2 . LEU   A 1 137 ? 32.64479 1.88287   48.25163  1.000 18.97092 ? 133 LEU   A CD2 1 
ATOM   1038 N  N   . ARG   A 1 138 ? 29.50291 -1.41734  48.99220  1.000 10.61169 ? 134 ARG   A N   1 
ATOM   1039 C  CA  . ARG   A 1 138 ? 28.56756 -2.51269  48.74063  1.000 11.69684 ? 134 ARG   A CA  1 
ATOM   1040 C  C   . ARG   A 1 138 ? 29.27732 -3.85570  48.63366  1.000 11.94600 ? 134 ARG   A C   1 
ATOM   1041 O  O   . ARG   A 1 138 ? 28.73532 -4.88584  49.05208  1.000 13.67398 ? 134 ARG   A O   1 
ATOM   1042 C  CB  . ARG   A 1 138 ? 27.77672 -2.24977  47.45639  1.000 14.28876 ? 134 ARG   A CB  1 
ATOM   1043 C  CG  . ARG   A 1 138 ? 26.53666 -1.39249  47.61933  1.000 13.22846 ? 134 ARG   A CG  1 
ATOM   1044 C  CD  . ARG   A 1 138 ? 26.00164 -0.99138  46.24397  1.000 12.23830 ? 134 ARG   A CD  1 
ATOM   1045 N  NE  . ARG   A 1 138 ? 26.84294 0.02724   45.63068  1.000 9.69776  ? 134 ARG   A NE  1 
ATOM   1046 C  CZ  . ARG   A 1 138 ? 26.85500 0.30603   44.33391  1.000 14.56219 ? 134 ARG   A CZ  1 
ATOM   1047 N  NH1 . ARG   A 1 138 ? 26.10299 -0.36511  43.47556  1.000 11.60581 ? 134 ARG   A NH1 1 
ATOM   1048 N  NH2 . ARG   A 1 138 ? 27.64332 1.27992   43.88734  1.000 15.89893 ? 134 ARG   A NH2 1 
ATOM   1049 N  N   . GLU   A 1 139 ? 30.48648 -3.87246  48.06536  1.000 10.89326 ? 135 GLU   A N   1 
ATOM   1050 C  CA  . GLU   A 1 139 ? 31.18353 -5.14099  47.88374  1.000 11.56245 ? 135 GLU   A CA  1 
ATOM   1051 C  C   . GLU   A 1 139 ? 31.67306 -5.74508  49.19425  1.000 11.93180 ? 135 GLU   A C   1 
ATOM   1052 O  O   . GLU   A 1 139 ? 32.19360 -6.86398  49.18074  1.000 12.93842 ? 135 GLU   A O   1 
ATOM   1053 C  CB  . GLU   A 1 139 ? 32.36141 -4.97088  46.92046  1.000 12.56874 ? 135 GLU   A CB  1 
ATOM   1054 C  CG  . GLU   A 1 139 ? 33.41563 -3.97755  47.36753  1.000 19.90667 ? 135 GLU   A CG  1 
ATOM   1055 C  CD  . GLU   A 1 139 ? 34.23189 -3.45548  46.20020  1.000 35.61007 ? 135 GLU   A CD  1 
ATOM   1056 O  OE1 . GLU   A 1 139 ? 33.62218 -3.10756  45.16377  1.000 37.11786 ? 135 GLU   A OE1 1 
ATOM   1057 O  OE2 . GLU   A 1 139 ? 35.47658 -3.40561  46.31119  1.000 27.30444 ? 135 GLU   A OE2 1 
ATOM   1058 N  N   . ASN   A 1 140 ? 31.52497 -5.04408  50.31866  1.000 11.69296 ? 136 ASN   A N   1 
ATOM   1059 C  CA  . ASN   A 1 140 ? 31.92014 -5.57842  51.61759  1.000 12.23344 ? 136 ASN   A CA  1 
ATOM   1060 C  C   . ASN   A 1 140 ? 30.74622 -5.65239  52.58755  1.000 17.78931 ? 136 ASN   A C   1 
ATOM   1061 O  O   . ASN   A 1 140 ? 30.95360 -5.75882  53.79980  1.000 14.36738 ? 136 ASN   A O   1 
ATOM   1062 C  CB  . ASN   A 1 140 ? 33.05217 -4.74214  52.21439  1.000 14.84061 ? 136 ASN   A CB  1 
ATOM   1063 C  CG  . ASN   A 1 140 ? 34.28054 -4.70626  51.32292  1.000 15.79842 ? 136 ASN   A CG  1 
ATOM   1064 O  OD1 . ASN   A 1 140 ? 34.64574 -3.65756  50.79109  1.000 21.72026 ? 136 ASN   A OD1 1 
ATOM   1065 N  ND2 . ASN   A 1 140 ? 34.92494 -5.85364  51.15737  1.000 14.85888 ? 136 ASN   A ND2 1 
ATOM   1066 N  N   . ILE   A 1 141 ? 29.51786 -5.59530  52.08138  1.000 10.61930 ? 137 ILE   A N   1 
ATOM   1067 C  CA  . ILE   A 1 141 ? 28.31282 -5.67803  52.90024  1.000 10.50470 ? 137 ILE   A CA  1 
ATOM   1068 C  C   . ILE   A 1 141 ? 27.54370 -6.91098  52.44860  1.000 14.83428 ? 137 ILE   A C   1 
ATOM   1069 O  O   . ILE   A 1 141 ? 27.04525 -6.96066  51.31778  1.000 10.23549 ? 137 ILE   A O   1 
ATOM   1070 C  CB  . ILE   A 1 141 ? 27.45421 -4.41271  52.78561  1.000 11.52122 ? 137 ILE   A CB  1 
ATOM   1071 C  CG1 . ILE   A 1 141 ? 28.19306 -3.21713  53.39023  1.000 9.69814  ? 137 ILE   A CG1 1 
ATOM   1072 C  CG2 . ILE   A 1 141 ? 26.10318 -4.61572  53.45577  1.000 11.50730 ? 137 ILE   A CG2 1 
ATOM   1073 C  CD1 . ILE   A 1 141 ? 27.55452 -1.88502  53.05996  1.000 10.64196 ? 137 ILE   A CD1 1 
ATOM   1074 N  N   . GLU   A 1 142 ? 27.44899 -7.90834  53.32281  1.000 10.38549 ? 138 GLU   A N   1 
ATOM   1075 C  CA  . GLU   A 1 142 ? 26.84711 -9.17524  52.93780  1.000 10.52534 ? 138 GLU   A CA  1 
ATOM   1076 C  C   . GLU   A 1 142 ? 25.33296 -9.05005  52.79093  1.000 10.27402 ? 138 GLU   A C   1 
ATOM   1077 O  O   . GLU   A 1 142 ? 24.67178 -8.29078  53.50327  1.000 9.42025  ? 138 GLU   A O   1 
ATOM   1078 C  CB  . GLU   A 1 142 ? 27.18735 -10.25390 53.96462  1.000 13.69737 ? 138 GLU   A CB  1 
ATOM   1079 C  CG  . GLU   A 1 142 ? 28.65600 -10.65100 53.96719  1.000 12.46729 ? 138 GLU   A CG  1 
ATOM   1080 C  CD  . GLU   A 1 142 ? 29.08495 -11.24397 55.28466  1.000 31.72451 ? 138 GLU   A CD  1 
ATOM   1081 O  OE1 . GLU   A 1 142 ? 28.58285 -10.77969 56.32934  1.000 38.19393 ? 138 GLU   A OE1 1 
ATOM   1082 O  OE2 . GLU   A 1 142 ? 29.91867 -12.17287 55.27725  1.000 33.75566 ? 138 GLU   A OE2 1 
ATOM   1083 N  N   . LEU   A 1 143 ? 24.78344 -9.82514  51.85995  1.000 9.85273  ? 139 LEU   A N   1 
ATOM   1084 C  CA  . LEU   A 1 143 ? 23.35319 -9.86230  51.59129  1.000 9.46630  ? 139 LEU   A CA  1 
ATOM   1085 C  C   . LEU   A 1 143 ? 22.81040 -11.26421 51.83708  1.000 11.47879 ? 139 LEU   A C   1 
ATOM   1086 O  O   . LEU   A 1 143 ? 23.54662 -12.25470 51.80678  1.000 13.72396 ? 139 LEU   A O   1 
ATOM   1087 C  CB  . LEU   A 1 143 ? 23.06011 -9.43059  50.14848  1.000 9.18044  ? 139 LEU   A CB  1 
ATOM   1088 C  CG  . LEU   A 1 143 ? 23.60262 -8.05379  49.78084  1.000 8.75254  ? 139 LEU   A CG  1 
ATOM   1089 C  CD1 . LEU   A 1 143 ? 23.45368 -7.81216  48.27885  1.000 10.83169 ? 139 LEU   A CD1 1 
ATOM   1090 C  CD2 . LEU   A 1 143 ? 22.87149 -6.97965  50.58322  1.000 8.22440  ? 139 LEU   A CD2 1 
ATOM   1091 N  N   . GLY   A 1 144 ? 21.50436 -11.33818 52.07216  1.000 11.44919 ? 140 GLY   A N   1 
ATOM   1092 C  CA  . GLY   A 1 144 ? 20.84294 -12.60756 52.31262  1.000 13.94130 ? 140 GLY   A CA  1 
ATOM   1093 C  C   . GLY   A 1 144 ? 19.76114 -12.48410 53.36310  1.000 15.81607 ? 140 GLY   A C   1 
ATOM   1094 O  O   . GLY   A 1 144 ? 19.47312 -11.38309 53.83358  1.000 12.05669 ? 140 GLY   A O   1 
ATOM   1095 N  N   . ASN   A 1 145 ? 19.16055 -13.61230 53.74433  1.000 14.05103 ? 141 ASN   A N   1 
ATOM   1096 C  CA  . ASN   A 1 145 ? 18.05425 -13.56945 54.69513  1.000 12.74558 ? 141 ASN   A CA  1 
ATOM   1097 C  C   . ASN   A 1 145 ? 18.52763 -13.11367 56.06858  1.000 11.93167 ? 141 ASN   A C   1 
ATOM   1098 O  O   . ASN   A 1 145 ? 17.82105 -12.36921 56.75786  1.000 11.74182 ? 141 ASN   A O   1 
ATOM   1099 C  CB  . ASN   A 1 145 ? 17.38477 -14.93599 54.78284  1.000 18.35360 ? 141 ASN   A CB  1 
ATOM   1100 C  CG  . ASN   A 1 145 ? 15.99242 -14.86705 55.37144  1.000 20.06474 ? 141 ASN   A CG  1 
ATOM   1101 O  OD1 . ASN   A 1 145 ? 15.11779 -14.18827 54.83150  1.000 13.46677 ? 141 ASN   A OD1 1 
ATOM   1102 N  ND2 . ASN   A 1 145 ? 15.77343 -15.57358 56.47573  1.000 16.90098 ? 141 ASN   A ND2 1 
ATOM   1103 N  N   . GLY   A 1 146 ? 19.70527 -13.56820 56.49066  1.000 16.11807 ? 142 GLY   A N   1 
ATOM   1104 C  CA  . GLY   A 1 146 ? 20.28351 -13.16245 57.75047  1.000 15.87026 ? 142 GLY   A CA  1 
ATOM   1105 C  C   . GLY   A 1 146 ? 20.50134 -11.66186 57.82994  1.000 12.85273 ? 142 GLY   A C   1 
ATOM   1106 O  O   . GLY   A 1 146 ? 20.07439 -11.00181 58.78196  1.000 17.90491 ? 142 GLY   A O   1 
ATOM   1107 N  N   . PRO   A 1 147 ? 21.19626 -11.09712 56.83597  1.000 11.36887 ? 143 PRO   A N   1 
ATOM   1108 C  CA  . PRO   A 1 147 ? 21.34059 -9.63180  56.79299  1.000 14.03528 ? 143 PRO   A CA  1 
ATOM   1109 C  C   . PRO   A 1 147 ? 20.02052 -8.88049  56.76294  1.000 9.79562  ? 143 PRO   A C   1 
ATOM   1110 O  O   . PRO   A 1 147 ? 19.89244 -7.84758  57.42918  1.000 9.63917  ? 143 PRO   A O   1 
ATOM   1111 C  CB  . PRO   A 1 147 ? 22.14838 -9.41057  55.50759  1.000 12.92575 ? 143 PRO   A CB  1 
ATOM   1112 C  CG  . PRO   A 1 147 ? 22.98844 -10.62452 55.40828  1.000 12.62646 ? 143 PRO   A CG  1 
ATOM   1113 C  CD  . PRO   A 1 147 ? 22.13671 -11.76344 55.91639  1.000 14.33751 ? 143 PRO   A CD  1 
ATOM   1114 N  N   . LEU   A 1 148 ? 19.03466 -9.35863  56.00065  1.000 10.24022 ? 144 LEU   A N   1 
ATOM   1115 C  CA  . LEU   A 1 148 ? 17.75248 -8.66172  55.94298  1.000 9.45718  ? 144 LEU   A CA  1 
ATOM   1116 C  C   . LEU   A 1 148 ? 17.05719 -8.68259  57.30050  1.000 10.03949 ? 144 LEU   A C   1 
ATOM   1117 O  O   . LEU   A 1 148 ? 16.49228 -7.66976  57.73193  1.000 10.83163 ? 144 LEU   A O   1 
ATOM   1118 C  CB  . LEU   A 1 148 ? 16.86894 -9.28529  54.86197  1.000 10.90159 ? 144 LEU   A CB  1 
ATOM   1119 C  CG  . LEU   A 1 148 ? 15.58015 -8.56895  54.43951  1.000 13.59512 ? 144 LEU   A CG  1 
ATOM   1120 C  CD1 . LEU   A 1 148 ? 15.81169 -7.08235  54.22287  1.000 8.78982  ? 144 LEU   A CD1 1 
ATOM   1121 C  CD2 . LEU   A 1 148 ? 15.01721 -9.19817  53.17068  1.000 10.78012 ? 144 LEU   A CD2 1 
ATOM   1122 N  N   . GLU   A 1 149 ? 17.10379 -9.82686  57.99042  1.000 10.87449 ? 145 GLU   A N   1 
ATOM   1123 C  CA  . GLU   A 1 149 ? 16.57084 -9.92771  59.34783  1.000 11.68772 ? 145 GLU   A CA  1 
ATOM   1124 C  C   . GLU   A 1 149 ? 17.18832 -8.87657  60.26302  1.000 11.63669 ? 145 GLU   A C   1 
ATOM   1125 O  O   . GLU   A 1 149 ? 16.48477 -8.19397  61.01716  1.000 13.10140 ? 145 GLU   A O   1 
ATOM   1126 C  CB  . GLU   A 1 149 ? 16.83464 -11.33182 59.89759  1.000 12.76461 ? 145 GLU   A CB  1 
ATOM   1127 C  CG  . GLU   A 1 149 ? 16.59829 -11.48215 61.38618  1.000 18.06293 ? 145 GLU   A CG  1 
ATOM   1128 C  CD  . GLU   A 1 149 ? 15.22302 -12.02711 61.68836  1.000 17.66764 ? 145 GLU   A CD  1 
ATOM   1129 O  OE1 . GLU   A 1 149 ? 14.53314 -12.44328 60.73396  1.000 23.15040 ? 145 GLU   A OE1 1 
ATOM   1130 O  OE2 . GLU   A 1 149 ? 14.82898 -12.03312 62.87154  1.000 21.59430 ? 145 GLU   A OE2 1 
ATOM   1131 N  N   . GLU   A 1 150 ? 18.51495 -8.74548  60.21761  1.000 11.78415 ? 146 GLU   A N   1 
ATOM   1132 C  CA  . GLU   A 1 150 ? 19.19203 -7.74252  61.03354  1.000 12.82599 ? 146 GLU   A CA  1 
ATOM   1133 C  C   . GLU   A 1 150 ? 18.86602 -6.33081  60.55737  1.000 11.99986 ? 146 GLU   A C   1 
ATOM   1134 O  O   . GLU   A 1 150 ? 18.71320 -5.41209  61.37417  1.000 11.31769 ? 146 GLU   A O   1 
ATOM   1135 C  CB  . GLU   A 1 150 ? 20.69874 -7.99403  61.00526  1.000 12.08832 ? 146 GLU   A CB  1 
ATOM   1136 C  CG  . GLU   A 1 150 ? 21.08587 -9.39539  61.46921  1.000 14.72736 ? 146 GLU   A CG  1 
ATOM   1137 C  CD  . GLU   A 1 150 ? 22.44141 -9.84044  60.93829  1.000 28.72406 ? 146 GLU   A CD  1 
ATOM   1138 O  OE1 . GLU   A 1 150 ? 23.21602 -8.98526  60.46031  1.000 25.95116 ? 146 GLU   A OE1 1 
ATOM   1139 O  OE2 . GLU   A 1 150 ? 22.72968 -11.05281 60.99397  1.000 28.92644 ? 146 GLU   A OE2 1 
ATOM   1140 N  N   . ALA   A 1 151 ? 18.75347 -6.14024  59.24011  1.000 9.92131  ? 147 ALA   A N   1 
ATOM   1141 C  CA  . ALA   A 1 151 ? 18.43777 -4.81902  58.70515  1.000 11.11886 ? 147 ALA   A CA  1 
ATOM   1142 C  C   . ALA   A 1 151 ? 17.06647 -4.34482  59.16814  1.000 13.93463 ? 147 ALA   A C   1 
ATOM   1143 O  O   . ALA   A 1 151 ? 16.87651 -3.15636  59.46054  1.000 13.17387 ? 147 ALA   A O   1 
ATOM   1144 C  CB  . ALA   A 1 151 ? 18.50735 -4.83703  57.17681  1.000 12.04610 ? 147 ALA   A CB  1 
ATOM   1145 N  N   . ILE   A 1 152 ? 16.09614 -5.25858  59.23208  1.000 9.90763  ? 148 ILE   A N   1 
ATOM   1146 C  CA  . ILE   A 1 152 ? 14.75418 -4.89719  59.67587  1.000 12.40665 ? 148 ILE   A CA  1 
ATOM   1147 C  C   . ILE   A 1 152 ? 14.77866 -4.44217  61.12910  1.000 12.50864 ? 148 ILE   A C   1 
ATOM   1148 O  O   . ILE   A 1 152 ? 14.15110 -3.43767  61.49159  1.000 11.29612 ? 148 ILE   A O   1 
ATOM   1149 C  CB  . ILE   A 1 152 ? 13.79198 -6.08066  59.45943  1.000 13.65673 ? 148 ILE   A CB  1 
ATOM   1150 C  CG1 . ILE   A 1 152 ? 13.45683 -6.22495  57.96453  1.000 10.29741 ? 148 ILE   A CG1 1 
ATOM   1151 C  CG2 . ILE   A 1 152 ? 12.53120 -5.92326  60.31200  1.000 11.95509 ? 148 ILE   A CG2 1 
ATOM   1152 C  CD1 . ILE   A 1 152 ? 12.96729 -7.61371  57.56982  1.000 10.79703 ? 148 ILE   A CD1 1 
ATOM   1153 N  N   . SER   A 1 153 ? 15.50276 -5.17188  61.98355  1.000 11.67283 ? 149 SER   A N   1 
ATOM   1154 C  CA  . SER   A 1 153 ? 15.60353 -4.78297  63.38763  1.000 12.62031 ? 149 SER   A CA  1 
ATOM   1155 C  C   . SER   A 1 153 ? 16.28385 -3.42782  63.54087  1.000 12.37762 ? 149 SER   A C   1 
ATOM   1156 O  O   . SER   A 1 153 ? 15.86613 -2.60393  64.36464  1.000 13.00635 ? 149 SER   A O   1 
ATOM   1157 C  CB  . SER   A 1 153 ? 16.36389 -5.85017  64.17821  1.000 15.91003 ? 149 SER   A CB  1 
ATOM   1158 O  OG  . SER   A 1 153 ? 15.62645 -7.05584  64.25514  1.000 14.86034 ? 149 SER   A OG  1 
ATOM   1159 N  N   . ALA   A 1 154 ? 17.34316 -3.18417  62.76688  1.000 13.60944 ? 150 ALA   A N   1 
ATOM   1160 C  CA  . ALA   A 1 154 ? 18.05349 -1.91142  62.86280  1.000 18.51538 ? 150 ALA   A CA  1 
ATOM   1161 C  C   . ALA   A 1 154 ? 17.14582 -0.74613  62.48664  1.000 14.68470 ? 150 ALA   A C   1 
ATOM   1162 O  O   . ALA   A 1 154 ? 17.08150 0.26161   63.20152  1.000 11.83614 ? 150 ALA   A O   1 
ATOM   1163 C  CB  . ALA   A 1 154 ? 19.29761 -1.93681  61.97561  1.000 15.79117 ? 150 ALA   A CB  1 
ATOM   1164 N  N   . LEU   A 1 155 ? 16.43485 -0.86865  61.36155  1.000 10.55250 ? 151 LEU   A N   1 
ATOM   1165 C  CA  . LEU   A 1 155 ? 15.48906 0.16969   60.96159  1.000 11.52855 ? 151 LEU   A CA  1 
ATOM   1166 C  C   . LEU   A 1 155 ? 14.43129 0.39339   62.03231  1.000 11.41918 ? 151 LEU   A C   1 
ATOM   1167 O  O   . LEU   A 1 155 ? 14.04666 1.53643   62.30661  1.000 12.00563 ? 151 LEU   A O   1 
ATOM   1168 C  CB  . LEU   A 1 155 ? 14.82675 -0.20045  59.63193  1.000 12.85032 ? 151 LEU   A CB  1 
ATOM   1169 C  CG  . LEU   A 1 155 ? 15.38010 0.43145   58.35227  1.000 18.64679 ? 151 LEU   A CG  1 
ATOM   1170 C  CD1 . LEU   A 1 155 ? 16.85748 0.16943   58.22443  1.000 22.25029 ? 151 LEU   A CD1 1 
ATOM   1171 C  CD2 . LEU   A 1 155 ? 14.64371 -0.08409  57.12214  1.000 21.83756 ? 151 LEU   A CD2 1 
ATOM   1172 N  N   . TYR   A 1 156 ? 13.94763 -0.68498  62.64872  1.000 11.93304 ? 152 TYR   A N   1 
ATOM   1173 C  CA  . TYR   A 1 156 ? 12.90584 -0.54491  63.66025  1.000 15.60501 ? 152 TYR   A CA  1 
ATOM   1174 C  C   . TYR   A 1 156 ? 13.40749 0.24260   64.86612  1.000 17.98216 ? 152 TYR   A C   1 
ATOM   1175 O  O   . TYR   A 1 156 ? 12.73142 1.15767   65.34965  1.000 14.66757 ? 152 TYR   A O   1 
ATOM   1176 C  CB  . TYR   A 1 156 ? 12.39656 -1.92023  64.09391  1.000 13.57097 ? 152 TYR   A CB  1 
ATOM   1177 C  CG  . TYR   A 1 156 ? 11.24932 -1.83213  65.07047  1.000 14.83077 ? 152 TYR   A CG  1 
ATOM   1178 C  CD1 . TYR   A 1 156 ? 11.47337 -1.85583  66.44305  1.000 15.99184 ? 152 TYR   A CD1 1 
ATOM   1179 C  CD2 . TYR   A 1 156 ? 9.94162  -1.69466  64.62161  1.000 17.40669 ? 152 TYR   A CD2 1 
ATOM   1180 C  CE1 . TYR   A 1 156 ? 10.42619 -1.75764  67.33717  1.000 23.40429 ? 152 TYR   A CE1 1 
ATOM   1181 C  CE2 . TYR   A 1 156 ? 8.88828  -1.59878  65.51045  1.000 20.44618 ? 152 TYR   A CE2 1 
ATOM   1182 C  CZ  . TYR   A 1 156 ? 9.13672  -1.63127  66.86556  1.000 27.91821 ? 152 TYR   A CZ  1 
ATOM   1183 O  OH  . TYR   A 1 156 ? 8.09053  -1.53592  67.75331  1.000 34.87110 ? 152 TYR   A OH  1 
ATOM   1184 N  N   . TYR   A 1 157 ? 14.59096 -0.10046  65.36917  1.000 15.56896 ? 153 TYR   A N   1 
ATOM   1185 C  CA  . TYR   A 1 157 ? 15.08212 0.50722   66.60031  1.000 15.10320 ? 153 TYR   A CA  1 
ATOM   1186 C  C   . TYR   A 1 157 ? 15.74599 1.86284   66.38329  1.000 17.90266 ? 153 TYR   A C   1 
ATOM   1187 O  O   . TYR   A 1 157 ? 16.14228 2.50126   67.36482  1.000 16.07741 ? 153 TYR   A O   1 
ATOM   1188 C  CB  . TYR   A 1 157 ? 16.04173 -0.45185  67.31001  1.000 15.70000 ? 153 TYR   A CB  1 
ATOM   1189 C  CG  . TYR   A 1 157 ? 15.31723 -1.61861  67.95517  1.000 16.53397 ? 153 TYR   A CG  1 
ATOM   1190 C  CD1 . TYR   A 1 157 ? 14.33371 -1.39828  68.90951  1.000 19.31938 ? 153 TYR   A CD1 1 
ATOM   1191 C  CD2 . TYR   A 1 157 ? 15.60884 -2.93015  67.60654  1.000 16.26905 ? 153 TYR   A CD2 1 
ATOM   1192 C  CE1 . TYR   A 1 157 ? 13.65932 -2.44996  69.50304  1.000 22.38071 ? 153 TYR   A CE1 1 
ATOM   1193 C  CE2 . TYR   A 1 157 ? 14.94110 -3.99048  68.19485  1.000 20.66197 ? 153 TYR   A CE2 1 
ATOM   1194 C  CZ  . TYR   A 1 157 ? 13.96696 -3.74251  69.14180  1.000 20.46072 ? 153 TYR   A CZ  1 
ATOM   1195 O  OH  . TYR   A 1 157 ? 13.29456 -4.78301  69.73402  1.000 25.59543 ? 153 TYR   A OH  1 
ATOM   1196 N  N   . TYR   A 1 158 ? 15.86708 2.33266   65.13917  1.000 13.80503 ? 154 TYR   A N   1 
ATOM   1197 C  CA  . TYR   A 1 158 ? 16.28891 3.71621   64.94666  1.000 13.87429 ? 154 TYR   A CA  1 
ATOM   1198 C  C   . TYR   A 1 158 ? 15.25523 4.68971   65.49977  1.000 18.78748 ? 154 TYR   A C   1 
ATOM   1199 O  O   . TYR   A 1 158 ? 15.61012 5.80103   65.90866  1.000 24.01261 ? 154 TYR   A O   1 
ATOM   1200 C  CB  . TYR   A 1 158 ? 16.55652 4.00977   63.46646  1.000 13.83923 ? 154 TYR   A CB  1 
ATOM   1201 C  CG  . TYR   A 1 158 ? 17.25004 5.33944   63.26630  1.000 21.73129 ? 154 TYR   A CG  1 
ATOM   1202 C  CD1 . TYR   A 1 158 ? 18.60032 5.48929   63.56536  1.000 21.89022 ? 154 TYR   A CD1 1 
ATOM   1203 C  CD2 . TYR   A 1 158 ? 16.55455 6.45115   62.80915  1.000 19.47042 ? 154 TYR   A CD2 1 
ATOM   1204 C  CE1 . TYR   A 1 158 ? 19.23930 6.70501   63.40846  1.000 16.89778 ? 154 TYR   A CE1 1 
ATOM   1205 C  CE2 . TYR   A 1 158 ? 17.18818 7.67391   62.64879  1.000 15.18119 ? 154 TYR   A CE2 1 
ATOM   1206 C  CZ  . TYR   A 1 158 ? 18.53049 7.79269   62.94901  1.000 18.81256 ? 154 TYR   A CZ  1 
ATOM   1207 O  OH  . TYR   A 1 158 ? 19.17071 9.00108   62.78867  1.000 24.43896 ? 154 TYR   A OH  1 
ATOM   1208 N  N   . SER   A 1 159 ? 13.98344 4.27837   65.54854  1.000 18.50304 ? 155 SER   A N   1 
ATOM   1209 C  CA  . SER   A 1 159 ? 12.91986 5.17911   65.98106  1.000 25.28546 ? 155 SER   A CA  1 
ATOM   1210 C  C   . SER   A 1 159 ? 13.09476 5.61336   67.42776  1.000 26.17219 ? 155 SER   A C   1 
ATOM   1211 O  O   . SER   A 1 159 ? 12.65815 6.70776   67.79664  1.000 27.12430 ? 155 SER   A O   1 
ATOM   1212 C  CB  . SER   A 1 159 ? 11.55400 4.51659   65.78674  1.000 27.89895 ? 155 SER   A CB  1 
ATOM   1213 O  OG  . SER   A 1 159 ? 11.54595 3.20285   66.32373  1.000 28.90137 ? 155 SER   A OG  1 
ATOM   1214 N  N   . THR   A 1 160 ? 13.72756 4.78218   68.26074  1.000 32.47725 ? 156 THR   A N   1 
ATOM   1215 C  CA  . THR   A 1 160 ? 13.93903 5.10909   69.66940  1.000 34.75644 ? 156 THR   A CA  1 
ATOM   1216 C  C   . THR   A 1 160 ? 15.41652 5.21827   70.04415  1.000 30.08058 ? 156 THR   A C   1 
ATOM   1217 O  O   . THR   A 1 160 ? 15.76905 5.07582   71.22184  1.000 33.94998 ? 156 THR   A O   1 
ATOM   1218 C  CB  . THR   A 1 160 ? 13.24824 4.07796   70.55921  1.000 39.28419 ? 156 THR   A CB  1 
ATOM   1219 O  OG1 . THR   A 1 160 ? 13.55281 2.75110   70.09299  1.000 29.62030 ? 156 THR   A OG1 1 
ATOM   1220 C  CG2 . THR   A 1 160 ? 11.73213 4.31431   70.56283  1.000 27.09476 ? 156 THR   A CG2 1 
ATOM   1221 N  N   . GLY   A 1 161 ? 16.28465 5.46788   69.06819  1.000 23.71574 ? 157 GLY   A N   1 
ATOM   1222 C  CA  . GLY   A 1 161 ? 17.67770 5.74783   69.32839  1.000 22.49766 ? 157 GLY   A CA  1 
ATOM   1223 C  C   . GLY   A 1 161 ? 18.56040 4.55032   69.60234  1.000 28.31566 ? 157 GLY   A C   1 
ATOM   1224 O  O   . GLY   A 1 161 ? 19.71928 4.73806   69.98393  1.000 28.17239 ? 157 GLY   A O   1 
ATOM   1225 N  N   . GLY   A 1 162 ? 18.07118 3.32687   69.41684  1.000 21.80935 ? 158 GLY   A N   1 
ATOM   1226 C  CA  . GLY   A 1 162 ? 18.92984 2.18565   69.69147  1.000 20.42118 ? 158 GLY   A CA  1 
ATOM   1227 C  C   . GLY   A 1 162 ? 19.79332 1.72061   68.53678  1.000 23.35692 ? 158 GLY   A C   1 
ATOM   1228 O  O   . GLY   A 1 162 ? 20.53912 0.74708   68.68777  1.000 38.38207 ? 158 GLY   A O   1 
ATOM   1229 N  N   . THR   A 1 163 ? 19.70711 2.38248   67.38582  1.000 17.86516 ? 159 THR   A N   1 
ATOM   1230 C  CA  . THR   A 1 163 ? 20.52254 2.06330   66.21917  1.000 14.96784 ? 159 THR   A CA  1 
ATOM   1231 C  C   . THR   A 1 163 ? 21.38949 3.26721   65.87501  1.000 15.93889 ? 159 THR   A C   1 
ATOM   1232 O  O   . THR   A 1 163 ? 20.87558 4.37936   65.72752  1.000 15.03897 ? 159 THR   A O   1 
ATOM   1233 C  CB  . THR   A 1 163 ? 19.65183 1.68985   65.01603  1.000 14.35655 ? 159 THR   A CB  1 
ATOM   1234 O  OG1 . THR   A 1 163 ? 18.87573 0.52323   65.31557  1.000 16.65139 ? 159 THR   A OG1 1 
ATOM   1235 C  CG2 . THR   A 1 163 ? 20.52143 1.41705   63.80169  1.000 14.49932 ? 159 THR   A CG2 1 
ATOM   1236 N  N   . GLN   A 1 164 ? 22.69583 3.04191   65.74537  1.000 15.22729 ? 160 GLN   A N   1 
ATOM   1237 C  CA  . GLN   A 1 164 ? 23.62190 4.08396   65.32341  1.000 15.38407 ? 160 GLN   A CA  1 
ATOM   1238 C  C   . GLN   A 1 164 ? 23.51538 4.31143   63.81718  1.000 14.00356 ? 160 GLN   A C   1 
ATOM   1239 O  O   . GLN   A 1 164 ? 23.11218 3.42835   63.05947  1.000 13.60933 ? 160 GLN   A O   1 
ATOM   1240 C  CB  . GLN   A 1 164 ? 25.05752 3.70447   65.68739  1.000 19.81045 ? 160 GLN   A CB  1 
ATOM   1241 C  CG  . GLN   A 1 164 ? 25.31758 3.57448   67.18116  1.000 22.27458 ? 160 GLN   A CG  1 
ATOM   1242 C  CD  . GLN   A 1 164 ? 25.60721 4.90742   67.83368  1.000 32.04618 ? 160 GLN   A CD  1 
ATOM   1243 O  OE1 . GLN   A 1 164 ? 26.75215 5.36277   67.86102  1.000 48.55800 ? 160 GLN   A OE1 1 
ATOM   1244 N  NE2 . GLN   A 1 164 ? 24.56905 5.54484   68.36333  1.000 33.24401 ? 160 GLN   A NE2 1 
ATOM   1245 N  N   . LEU   A 1 165 ? 23.90860 5.51196   63.38554  1.000 11.90407 ? 161 LEU   A N   1 
ATOM   1246 C  CA  . LEU   A 1 165 ? 23.76744 5.87314   61.97565  1.000 11.66044 ? 161 LEU   A CA  1 
ATOM   1247 C  C   . LEU   A 1 165 ? 24.53173 4.95235   61.02311  1.000 15.80142 ? 161 LEU   A C   1 
ATOM   1248 O  O   . LEU   A 1 165 ? 23.95399 4.57284   59.98639  1.000 12.54770 ? 161 LEU   A O   1 
ATOM   1249 C  CB  . LEU   A 1 165 ? 24.18187 7.33560   61.77277  1.000 12.91385 ? 161 LEU   A CB  1 
ATOM   1250 C  CG  . LEU   A 1 165 ? 23.96552 7.92461   60.37318  1.000 16.13650 ? 161 LEU   A CG  1 
ATOM   1251 C  CD1 . LEU   A 1 165 ? 22.49304 7.88523   59.99727  1.000 20.12823 ? 161 LEU   A CD1 1 
ATOM   1252 C  CD2 . LEU   A 1 165 ? 24.50165 9.34611   60.28812  1.000 21.54202 ? 161 LEU   A CD2 1 
ATOM   1253 N  N   . PRO   A 1 166 ? 25.79473 4.57247   61.27501  1.000 17.66153 ? 162 PRO   A N   1 
ATOM   1254 C  CA  . PRO   A 1 166 ? 26.45343 3.64196   60.33997  1.000 13.83259 ? 162 PRO   A CA  1 
ATOM   1255 C  C   . PRO   A 1 166 ? 25.70225 2.33478   60.17509  1.000 16.66997 ? 162 PRO   A C   1 
ATOM   1256 O  O   . PRO   A 1 166 ? 25.63980 1.79846   59.06358  1.000 14.39092 ? 162 PRO   A O   1 
ATOM   1257 C  CB  . PRO   A 1 166 ? 27.83598 3.43066   60.97150  1.000 15.30064 ? 162 PRO   A CB  1 
ATOM   1258 C  CG  . PRO   A 1 166 ? 28.07153 4.65476   61.76823  1.000 17.44798 ? 162 PRO   A CG  1 
ATOM   1259 C  CD  . PRO   A 1 166 ? 26.72756 5.02394   62.32445  1.000 16.73769 ? 162 PRO   A CD  1 
ATOM   1260 N  N   . THR   A 1 167 ? 25.11852 1.80867   61.25433  1.000 14.16616 ? 163 THR   A N   1 
ATOM   1261 C  CA  . THR   A 1 167 ? 24.32909 0.58705   61.13792  1.000 11.39995 ? 163 THR   A CA  1 
ATOM   1262 C  C   . THR   A 1 167 ? 23.03276 0.83757   60.37620  1.000 14.31907 ? 163 THR   A C   1 
ATOM   1263 O  O   . THR   A 1 167 ? 22.58010 -0.02959  59.62147  1.000 11.45096 ? 163 THR   A O   1 
ATOM   1264 C  CB  . THR   A 1 167 ? 24.05433 0.01271   62.53198  1.000 16.85298 ? 163 THR   A CB  1 
ATOM   1265 O  OG1 . THR   A 1 167 ? 25.29534 -0.36390  63.13950  1.000 21.10488 ? 163 THR   A OG1 1 
ATOM   1266 C  CG2 . THR   A 1 167 ? 23.14766 -1.20857  62.46716  1.000 14.49851 ? 163 THR   A CG2 1 
ATOM   1267 N  N   . LEU   A 1 168 ? 22.43689 2.02073   60.53625  1.000 10.98703 ? 164 LEU   A N   1 
ATOM   1268 C  CA  . LEU   A 1 168 ? 21.24494 2.35268   59.76448  1.000 12.49013 ? 164 LEU   A CA  1 
ATOM   1269 C  C   . LEU   A 1 168 ? 21.56289 2.40403   58.27464  1.000 11.64955 ? 164 LEU   A C   1 
ATOM   1270 O  O   . LEU   A 1 168 ? 20.83511 1.83481   57.45134  1.000 8.44494  ? 164 LEU   A O   1 
ATOM   1271 C  CB  . LEU   A 1 168 ? 20.66388 3.68711   60.24059  1.000 12.86826 ? 164 LEU   A CB  1 
ATOM   1272 C  CG  . LEU   A 1 168 ? 19.35275 4.12005   59.57932  1.000 10.57418 ? 164 LEU   A CG  1 
ATOM   1273 C  CD1 . LEU   A 1 168 ? 18.19810 3.20896   59.98600  1.000 14.91921 ? 164 LEU   A CD1 1 
ATOM   1274 C  CD2 . LEU   A 1 168 ? 19.02988 5.57344   59.89553  1.000 18.35894 ? 164 LEU   A CD2 1 
ATOM   1275 N  N   . ALA   A 1 169 ? 22.66139 3.07651   57.91578  1.000 11.64140 ? 165 ALA   A N   1 
ATOM   1276 C  CA  . ALA   A 1 169 ? 23.04108 3.20708   56.51132  1.000 10.01265 ? 165 ALA   A CA  1 
ATOM   1277 C  C   . ALA   A 1 169 ? 23.29638 1.84885   55.87803  1.000 12.33659 ? 165 ALA   A C   1 
ATOM   1278 O  O   . ALA   A 1 169 ? 22.88719 1.59595   54.73769  1.000 11.16973 ? 165 ALA   A O   1 
ATOM   1279 C  CB  . ALA   A 1 169 ? 24.28650 4.08327   56.38542  1.000 14.20279 ? 165 ALA   A CB  1 
ATOM   1280 N  N   . ARG   A 1 170 ? 23.98841 0.96475   56.59467  1.000 8.50808  ? 166 ARG   A N   1 
ATOM   1281 C  CA  . ARG   A 1 170 ? 24.24001 -0.36486  56.05252  1.000 9.40428  ? 166 ARG   A CA  1 
ATOM   1282 C  C   . ARG   A 1 170 ? 22.93779 -1.12993  55.87431  1.000 9.04909  ? 166 ARG   A C   1 
ATOM   1283 O  O   . ARG   A 1 170 ? 22.77798 -1.88695  54.90898  1.000 13.03545 ? 166 ARG   A O   1 
ATOM   1284 C  CB  . ARG   A 1 170 ? 25.20133 -1.14091  56.95886  1.000 13.56839 ? 166 ARG   A CB  1 
ATOM   1285 C  CG  . ARG   A 1 170 ? 25.22176 -2.64664  56.67610  1.000 21.36425 ? 166 ARG   A CG  1 
ATOM   1286 C  CD  . ARG   A 1 170 ? 26.20692 -3.37346  57.46420  1.000 34.35129 ? 166 ARG   A CD  1 
ATOM   1287 N  NE  . ARG   A 1 170 ? 25.94685 -3.29864  58.89070  1.000 36.79145 ? 166 ARG   A NE  1 
ATOM   1288 C  CZ  . ARG   A 1 170 ? 26.66568 -2.53809  59.69257  1.000 34.07828 ? 166 ARG   A CZ  1 
ATOM   1289 N  NH1 . ARG   A 1 170 ? 27.60462 -1.73847  59.21283  1.000 33.86279 ? 166 ARG   A NH1 1 
ATOM   1290 N  NH2 . ARG   A 1 170 ? 26.47057 -2.61360  61.00035  1.000 31.28430 ? 166 ARG   A NH2 1 
ATOM   1291 N  N   . SER   A 1 171 ? 21.99533 -0.94957  56.80090  1.000 8.43648  ? 167 SER   A N   1 
ATOM   1292 C  CA  . SER   A 1 171 ? 20.70141 -1.61236  56.67418  1.000 9.67093  ? 167 SER   A CA  1 
ATOM   1293 C  C   . SER   A 1 171 ? 19.92769 -1.09487  55.46528  1.000 9.80879  ? 167 SER   A C   1 
ATOM   1294 O  O   . SER   A 1 171 ? 19.22401 -1.86319  54.80061  1.000 9.54596  ? 167 SER   A O   1 
ATOM   1295 C  CB  . SER   A 1 171 ? 19.90129 -1.42510  57.95717  1.000 16.49818 ? 167 SER   A CB  1 
ATOM   1296 O  OG  . SER   A 1 171 ? 20.61339 -1.95434  59.05968  1.000 14.67835 ? 167 SER   A OG  1 
ATOM   1297 N  N   . PHE   A 1 172 ? 20.04888 0.20192   55.16046  1.000 8.01411  ? 168 PHE   A N   1 
ATOM   1298 C  CA  . PHE   A 1 172 ? 19.45183 0.73246   53.93590  1.000 7.44068  ? 168 PHE   A CA  1 
ATOM   1299 C  C   . PHE   A 1 172 ? 20.05546 0.07969   52.69992  1.000 7.52069  ? 168 PHE   A C   1 
ATOM   1300 O  O   . PHE   A 1 172 ? 19.34515 -0.21547  51.73344  1.000 11.77978 ? 168 PHE   A O   1 
ATOM   1301 C  CB  . PHE   A 1 172 ? 19.64380 2.25000   53.85512  1.000 8.21090  ? 168 PHE   A CB  1 
ATOM   1302 C  CG  . PHE   A 1 172 ? 18.72347 3.03612   54.73811  1.000 9.13289  ? 168 PHE   A CG  1 
ATOM   1303 C  CD1 . PHE   A 1 172 ? 17.41474 2.63939   54.93161  1.000 12.79946 ? 168 PHE   A CD1 1 
ATOM   1304 C  CD2 . PHE   A 1 172 ? 19.17216 4.18953   55.36890  1.000 8.83924  ? 168 PHE   A CD2 1 
ATOM   1305 C  CE1 . PHE   A 1 172 ? 16.56751 3.37307   55.74592  1.000 15.25881 ? 168 PHE   A CE1 1 
ATOM   1306 C  CE2 . PHE   A 1 172 ? 18.33239 4.92350   56.18344  1.000 16.00326 ? 168 PHE   A CE2 1 
ATOM   1307 C  CZ  . PHE   A 1 172 ? 17.02768 4.51410   56.37033  1.000 15.91288 ? 168 PHE   A CZ  1 
ATOM   1308 N  N   . ILE   A 1 173 ? 21.37269 -0.12387  52.70016  1.000 9.35948  ? 169 ILE   A N   1 
ATOM   1309 C  CA  . ILE   A 1 173 ? 22.03971 -0.70819  51.53932  1.000 7.51027  ? 169 ILE   A CA  1 
ATOM   1310 C  C   . ILE   A 1 173 ? 21.55904 -2.13662  51.31307  1.000 9.72419  ? 169 ILE   A C   1 
ATOM   1311 O  O   . ILE   A 1 173 ? 21.33072 -2.55937  50.17153  1.000 10.42315 ? 169 ILE   A O   1 
ATOM   1312 C  CB  . ILE   A 1 173 ? 23.56754 -0.63450  51.72254  1.000 7.32291  ? 169 ILE   A CB  1 
ATOM   1313 C  CG1 . ILE   A 1 173 ? 24.06175 0.80635   51.58592  1.000 7.77076  ? 169 ILE   A CG1 1 
ATOM   1314 C  CG2 . ILE   A 1 173 ? 24.30286 -1.55816  50.75725  1.000 8.02858  ? 169 ILE   A CG2 1 
ATOM   1315 C  CD1 . ILE   A 1 173 ? 25.53679 0.94091   51.87791  1.000 7.78202  ? 169 ILE   A CD1 1 
ATOM   1316 N  N   . ILE   A 1 174 ? 21.38237 -2.89427  52.39764  1.000 7.80470  ? 170 ILE   A N   1 
ATOM   1317 C  CA  . ILE   A 1 174 ? 20.86554 -4.25885  52.30040  1.000 7.55954  ? 170 ILE   A CA  1 
ATOM   1318 C  C   . ILE   A 1 174 ? 19.44769 -4.25608  51.74202  1.000 12.97496 ? 170 ILE   A C   1 
ATOM   1319 O  O   . ILE   A 1 174 ? 19.12140 -5.01938  50.82320  1.000 9.69914  ? 170 ILE   A O   1 
ATOM   1320 C  CB  . ILE   A 1 174 ? 20.91843 -4.94978  53.67709  1.000 7.98630  ? 170 ILE   A CB  1 
ATOM   1321 C  CG1 . ILE   A 1 174 ? 22.36507 -5.08271  54.16718  1.000 8.23647  ? 170 ILE   A CG1 1 
ATOM   1322 C  CG2 . ILE   A 1 174 ? 20.23698 -6.31338  53.60842  1.000 10.60861 ? 170 ILE   A CG2 1 
ATOM   1323 C  CD1 . ILE   A 1 174 ? 22.48610 -5.42849  55.64938  1.000 10.79600 ? 170 ILE   A CD1 1 
ATOM   1324 N  N   . CYS   A 1 175 ? 18.57941 -3.39956  52.29422  1.000 10.08774 ? 171 CYS   A N   1 
ATOM   1325 C  CA  . CYS   A 1 175 ? 17.17990 -3.38963  51.87351  1.000 10.41875 ? 171 CYS   A CA  1 
ATOM   1326 C  C   . CYS   A 1 175 ? 17.03036 -2.95839  50.42186  1.000 14.50382 ? 171 CYS   A C   1 
ATOM   1327 O  O   . CYS   A 1 175 ? 16.25764 -3.56130  49.66535  1.000 13.60204 ? 171 CYS   A O   1 
ATOM   1328 C  CB  . CYS   A 1 175 ? 16.35965 -2.47406  52.77993  1.000 14.03967 ? 171 CYS   A CB  1 
ATOM   1329 S  SG  . CYS   A 1 175 ? 16.02981 -3.16785  54.39916  1.000 20.64034 ? 171 CYS   A SG  1 
ATOM   1330 N  N   . ILE   A 1 176 ? 17.75262 -1.91470  50.01515  1.000 11.83473 ? 172 ILE   A N   1 
ATOM   1331 C  CA  . ILE   A 1 176 ? 17.61666 -1.41741  48.65009  1.000 11.00898 ? 172 ILE   A CA  1 
ATOM   1332 C  C   . ILE   A 1 176 ? 18.02522 -2.49015  47.64855  1.000 11.71328 ? 172 ILE   A C   1 
ATOM   1333 O  O   . ILE   A 1 176 ? 17.36479 -2.68622  46.61980  1.000 13.46711 ? 172 ILE   A O   1 
ATOM   1334 C  CB  . ILE   A 1 176 ? 18.43176 -0.12252  48.47425  1.000 13.80789 ? 172 ILE   A CB  1 
ATOM   1335 C  CG1 . ILE   A 1 176 ? 17.81998 1.00226   49.32068  1.000 16.62653 ? 172 ILE   A CG1 1 
ATOM   1336 C  CG2 . ILE   A 1 176 ? 18.48918 0.28255   47.00987  1.000 11.06549 ? 172 ILE   A CG2 1 
ATOM   1337 C  CD1 . ILE   A 1 176 ? 18.66012 2.26445   49.35614  1.000 19.37906 ? 172 ILE   A CD1 1 
ATOM   1338 N  N   . GLN   A 1 177 ? 19.10139 -3.21922  47.94197  1.000 9.66521  ? 173 GLN   A N   1 
ATOM   1339 C  CA  . GLN   A 1 177 ? 19.58533 -4.21379  46.99190  1.000 12.19824 ? 173 GLN   A CA  1 
ATOM   1340 C  C   . GLN   A 1 177 ? 18.66967 -5.42926  46.93172  1.000 10.69471 ? 173 GLN   A C   1 
ATOM   1341 O  O   . GLN   A 1 177 ? 18.44237 -5.98383  45.85065  1.000 15.20487 ? 173 GLN   A O   1 
ATOM   1342 C  CB  . GLN   A 1 177 ? 21.00671 -4.63306  47.34729  1.000 7.35650  ? 173 GLN   A CB  1 
ATOM   1343 C  CG  . GLN   A 1 177 ? 22.03405 -3.54956  47.11219  1.000 10.49641 ? 173 GLN   A CG  1 
ATOM   1344 C  CD  . GLN   A 1 177 ? 23.43818 -4.04126  47.35530  1.000 9.85010  ? 173 GLN   A CD  1 
ATOM   1345 O  OE1 . GLN   A 1 177 ? 24.08144 -4.57419  46.45631  1.000 13.17240 ? 173 GLN   A OE1 1 
ATOM   1346 N  NE2 . GLN   A 1 177 ? 23.91975 -3.87368  48.58065  1.000 11.34261 ? 173 GLN   A NE2 1 
ATOM   1347 N  N   . MET   A 1 178 ? 18.14254 -5.86928  48.07541  1.000 10.51679 ? 174 MET   A N   1 
ATOM   1348 C  CA  . MET   A 1 178 ? 17.32587 -7.07687  48.07080  1.000 9.40518  ? 174 MET   A CA  1 
ATOM   1349 C  C   . MET   A 1 178 ? 15.88559 -6.81354  47.66147  1.000 10.21534 ? 174 MET   A C   1 
ATOM   1350 O  O   . MET   A 1 178 ? 15.13341 -7.77190  47.46015  1.000 11.43547 ? 174 MET   A O   1 
ATOM   1351 C  CB  . MET   A 1 178 ? 17.37899 -7.74987  49.44792  1.000 8.36080  ? 174 MET   A CB  1 
ATOM   1352 C  CG  . MET   A 1 178 ? 18.77311 -8.25827  49.78719  1.000 8.40311  ? 174 MET   A CG  1 
ATOM   1353 S  SD  . MET   A 1 178 ? 18.88192 -9.13384  51.36112  1.000 11.93687 ? 174 MET   A SD  1 
ATOM   1354 C  CE  . MET   A 1 178 ? 17.87178 -10.56915 51.00695  1.000 20.47978 ? 174 MET   A CE  1 
ATOM   1355 N  N   . ILE   A 1 179 ? 15.49190 -5.55036  47.50119  1.000 8.03975  ? 175 ILE   A N   1 
ATOM   1356 C  CA  . ILE   A 1 179 ? 14.12725 -5.23210  47.09938  1.000 9.49500  ? 175 ILE   A CA  1 
ATOM   1357 C  C   . ILE   A 1 179 ? 14.13345 -4.44282  45.79411  1.000 10.51091 ? 175 ILE   A C   1 
ATOM   1358 O  O   . ILE   A 1 179 ? 13.66954 -4.93540  44.75978  1.000 12.63089 ? 175 ILE   A O   1 
ATOM   1359 C  CB  . ILE   A 1 179 ? 13.39102 -4.46866  48.21284  1.000 14.22574 ? 175 ILE   A CB  1 
ATOM   1360 C  CG1 . ILE   A 1 179 ? 13.38904 -5.29979  49.50277  1.000 18.46372 ? 175 ILE   A CG1 1 
ATOM   1361 C  CG2 . ILE   A 1 179 ? 11.97257 -4.14169  47.77082  1.000 13.46960 ? 175 ILE   A CG2 1 
ATOM   1362 C  CD1 . ILE   A 1 179 ? 12.91051 -4.54178  50.71842  1.000 21.11154 ? 175 ILE   A CD1 1 
ATOM   1363 N  N   . SER   A 1 180 ? 14.67470 -3.22176  45.82641  1.000 9.23247  ? 176 SER   A N   1 
ATOM   1364 C  CA  . SER   A 1 180 ? 14.64428 -2.36493  44.64307  1.000 7.95826  ? 176 SER   A CA  1 
ATOM   1365 C  C   . SER   A 1 180 ? 15.47263 -2.95071  43.50469  1.000 10.76995 ? 176 SER   A C   1 
ATOM   1366 O  O   . SER   A 1 180 ? 14.99063 -3.07221  42.37093  1.000 9.09878  ? 176 SER   A O   1 
ATOM   1367 C  CB  . SER   A 1 180 ? 15.14227 -0.96473  44.99936  1.000 7.70129  ? 176 SER   A CB  1 
ATOM   1368 O  OG  . SER   A 1 180 ? 14.25801 -0.32582  45.90559  1.000 17.04445 ? 176 SER   A OG  1 
ATOM   1369 N  N   . GLU   A 1 181 ? 16.72893 -3.31118  43.77904  1.000 9.62142  ? 177 GLU   A N   1 
ATOM   1370 C  CA  . GLU   A 1 181 ? 17.57478 -3.81227  42.69960  1.000 8.37442  ? 177 GLU   A CA  1 
ATOM   1371 C  C   . GLU   A 1 181 ? 17.14316 -5.20004  42.23480  1.000 12.66498 ? 177 GLU   A C   1 
ATOM   1372 O  O   . GLU   A 1 181 ? 17.27676 -5.52102  41.04810  1.000 8.44437  ? 177 GLU   A O   1 
ATOM   1373 C  CB  . GLU   A 1 181 ? 19.03957 -3.81952  43.12962  1.000 9.57427  ? 177 GLU   A CB  1 
ATOM   1374 C  CG  . GLU   A 1 181 ? 19.57224 -2.46066  43.57460  1.000 10.77309 ? 177 GLU   A CG  1 
ATOM   1375 C  CD  . GLU   A 1 181 ? 19.78148 -1.47694  42.43283  1.000 20.00252 ? 177 GLU   A CD  1 
ATOM   1376 O  OE1 . GLU   A 1 181 ? 19.46255 -1.80945  41.26522  1.000 17.11128 ? 177 GLU   A OE1 1 
ATOM   1377 O  OE2 . GLU   A 1 181 ? 20.27751 -0.35918  42.70748  1.000 19.71366 ? 177 GLU   A OE2 1 
ATOM   1378 N  N   . ALA   A 1 182 ? 16.61905 -6.03432  43.13428  1.000 11.34525 ? 178 ALA   A N   1 
ATOM   1379 C  CA  . ALA   A 1 182 ? 16.08599 -7.31767  42.68335  1.000 10.14226 ? 178 ALA   A CA  1 
ATOM   1380 C  C   . ALA   A 1 182 ? 14.82931 -7.12929  41.84308  1.000 14.41365 ? 178 ALA   A C   1 
ATOM   1381 O  O   . ALA   A 1 182 ? 14.57968 -7.90792  40.91317  1.000 11.85901 ? 178 ALA   A O   1 
ATOM   1382 C  CB  . ALA   A 1 182 ? 15.80595 -8.22913  43.87754  1.000 10.89879 ? 178 ALA   A CB  1 
ATOM   1383 N  N   . ALA   A 1 183 ? 14.03037 -6.10283  42.13957  1.000 11.23429 ? 179 ALA   A N   1 
ATOM   1384 C  CA  . ALA   A 1 183 ? 12.88888 -5.81620  41.27856  1.000 14.25532 ? 179 ALA   A CA  1 
ATOM   1385 C  C   . ALA   A 1 183 ? 13.34956 -5.34313  39.90536  1.000 13.32987 ? 179 ALA   A C   1 
ATOM   1386 O  O   . ALA   A 1 183 ? 12.74374 -5.69254  38.88547  1.000 11.50237 ? 179 ALA   A O   1 
ATOM   1387 C  CB  . ALA   A 1 183 ? 11.98135 -4.77856  41.93751  1.000 13.14261 ? 179 ALA   A CB  1 
ATOM   1388 N  N   . ARG   A 1 184 ? 14.44393 -4.57758  39.86041  1.000 11.72674 ? 180 ARG   A N   1 
ATOM   1389 C  CA  . ARG   A 1 184 ? 14.92605 -4.02656  38.59706  1.000 10.66259 ? 180 ARG   A CA  1 
ATOM   1390 C  C   . ARG   A 1 184 ? 15.57881 -5.08104  37.70858  1.000 9.75052  ? 180 ARG   A C   1 
ATOM   1391 O  O   . ARG   A 1 184 ? 15.54612 -4.95073  36.47621  1.000 10.21842 ? 180 ARG   A O   1 
ATOM   1392 C  CB  . ARG   A 1 184 ? 15.92478 -2.90056  38.86505  1.000 9.36012  ? 180 ARG   A CB  1 
ATOM   1393 C  CG  . ARG   A 1 184 ? 15.33923 -1.61531  39.42486  1.000 10.26716 ? 180 ARG   A CG  1 
ATOM   1394 C  CD  . ARG   A 1 184 ? 16.47602 -0.74552  39.93182  1.000 10.80524 ? 180 ARG   A CD  1 
ATOM   1395 N  NE  . ARG   A 1 184 ? 16.07033 0.61219   40.27193  1.000 13.60601 ? 180 ARG   A NE  1 
ATOM   1396 C  CZ  . ARG   A 1 184 ? 16.91071 1.54912   40.68963  1.000 20.59726 ? 180 ARG   A CZ  1 
ATOM   1397 N  NH1 . ARG   A 1 184 ? 18.20053 1.29647   40.85152  1.000 18.26093 ? 180 ARG   A NH1 1 
ATOM   1398 N  NH2 . ARG   A 1 184 ? 16.44867 2.76996   40.94619  1.000 20.09507 ? 180 ARG   A NH2 1 
ATOM   1399 N  N   . PHE   A 1 185 ? 16.19250 -6.11038  38.29924  1.000 10.04049 ? 181 PHE   A N   1 
ATOM   1400 C  CA  . PHE   A 1 185 ? 17.01480 -7.07309  37.56731  1.000 10.68651 ? 181 PHE   A CA  1 
ATOM   1401 C  C   . PHE   A 1 185 ? 16.63723 -8.49353  37.96743  1.000 11.61141 ? 181 PHE   A C   1 
ATOM   1402 O  O   . PHE   A 1 185 ? 16.76609 -8.85995  39.14066  1.000 16.42225 ? 181 PHE   A O   1 
ATOM   1403 C  CB  . PHE   A 1 185 ? 18.50855 -6.86612  37.85431  1.000 9.57378  ? 181 PHE   A CB  1 
ATOM   1404 C  CG  . PHE   A 1 185 ? 19.06968 -5.56693  37.36028  1.000 9.75770  ? 181 PHE   A CG  1 
ATOM   1405 C  CD1 . PHE   A 1 185 ? 19.48337 -5.42752  36.04336  1.000 12.31486 ? 181 PHE   A CD1 1 
ATOM   1406 C  CD2 . PHE   A 1 185 ? 19.23968 -4.49885  38.22766  1.000 8.83536  ? 181 PHE   A CD2 1 
ATOM   1407 C  CE1 . PHE   A 1 185 ? 20.02495 -4.23660  35.59190  1.000 11.77657 ? 181 PHE   A CE1 1 
ATOM   1408 C  CE2 . PHE   A 1 185 ? 19.78057 -3.30688  37.78407  1.000 9.98949  ? 181 PHE   A CE2 1 
ATOM   1409 C  CZ  . PHE   A 1 185 ? 20.17254 -3.17245  36.46360  1.000 11.84573 ? 181 PHE   A CZ  1 
ATOM   1410 N  N   . GLN   A 1 186 ? 16.22034 -9.31175  36.99457  1.000 10.97695 ? 182 GLN   A N   1 
ATOM   1411 C  CA  . GLN   A 1 186 ? 16.07761 -10.73774 37.28178  1.000 11.46523 ? 182 GLN   A CA  1 
ATOM   1412 C  C   . GLN   A 1 186 ? 17.40292 -11.34974 37.70640  1.000 11.30450 ? 182 GLN   A C   1 
ATOM   1413 O  O   . GLN   A 1 186 ? 17.42537 -12.29346 38.50146  1.000 11.49539 ? 182 GLN   A O   1 
ATOM   1414 C  CB  . GLN   A 1 186 ? 15.54435 -11.49847 36.06813  1.000 12.39778 ? 182 GLN   A CB  1 
ATOM   1415 C  CG  . GLN   A 1 186 ? 14.22427 -11.01832 35.52628  1.000 16.84472 ? 182 GLN   A CG  1 
ATOM   1416 C  CD  . GLN   A 1 186 ? 14.41935 -10.19323 34.28788  1.000 23.81737 ? 182 GLN   A CD  1 
ATOM   1417 O  OE1 . GLN   A 1 186 ? 15.24577 -9.28551  34.27034  1.000 27.77038 ? 182 GLN   A OE1 1 
ATOM   1418 N  NE2 . GLN   A 1 186 ? 13.68392 -10.51699 33.23184  1.000 31.43373 ? 182 GLN   A NE2 1 
ATOM   1419 N  N   . TYR   A 1 187 ? 18.51525 -10.83786 37.17744  1.000 11.66940 ? 183 TYR   A N   1 
ATOM   1420 C  CA  . TYR   A 1 187 ? 19.82016 -11.39101 37.52472  1.000 11.09901 ? 183 TYR   A CA  1 
ATOM   1421 C  C   . TYR   A 1 187 ? 20.09721 -11.24160 39.01452  1.000 13.15360 ? 183 TYR   A C   1 
ATOM   1422 O  O   . TYR   A 1 187 ? 20.56271 -12.18487 39.66620  1.000 11.86094 ? 183 TYR   A O   1 
ATOM   1423 C  CB  . TYR   A 1 187 ? 20.90592 -10.70872 36.69102  1.000 11.06434 ? 183 TYR   A CB  1 
ATOM   1424 C  CG  . TYR   A 1 187 ? 22.30793 -11.21565 36.95009  1.000 12.98072 ? 183 TYR   A CG  1 
ATOM   1425 C  CD1 . TYR   A 1 187 ? 22.78150 -12.35562 36.31878  1.000 12.50961 ? 183 TYR   A CD1 1 
ATOM   1426 C  CD2 . TYR   A 1 187 ? 23.15911 -10.54695 37.82492  1.000 15.81631 ? 183 TYR   A CD2 1 
ATOM   1427 C  CE1 . TYR   A 1 187 ? 24.06772 -12.81704 36.54610  1.000 17.88867 ? 183 TYR   A CE1 1 
ATOM   1428 C  CE2 . TYR   A 1 187 ? 24.44423 -10.99915 38.06071  1.000 19.41367 ? 183 TYR   A CE2 1 
ATOM   1429 C  CZ  . TYR   A 1 187 ? 24.89298 -12.13530 37.41985  1.000 15.58426 ? 183 TYR   A CZ  1 
ATOM   1430 O  OH  . TYR   A 1 187 ? 26.17097 -12.58627 37.65333  1.000 18.52460 ? 183 TYR   A OH  1 
ATOM   1431 N  N   . ILE   A 1 188 ? 19.78334 -10.07186 39.57686  1.000 9.91422  ? 184 ILE   A N   1 
ATOM   1432 C  CA  . ILE   A 1 188 ? 19.99030 -9.84782  41.00394  1.000 9.46789  ? 184 ILE   A CA  1 
ATOM   1433 C  C   . ILE   A 1 188 ? 18.96086 -10.61691 41.82613  1.000 9.69196  ? 184 ILE   A C   1 
ATOM   1434 O  O   . ILE   A 1 188 ? 19.27450 -11.13796 42.90399  1.000 11.14127 ? 184 ILE   A O   1 
ATOM   1435 C  CB  . ILE   A 1 188 ? 19.96100 -8.33863  41.30669  1.000 9.17034  ? 184 ILE   A CB  1 
ATOM   1436 C  CG1 . ILE   A 1 188 ? 21.07267 -7.63547  40.52460  1.000 8.79521  ? 184 ILE   A CG1 1 
ATOM   1437 C  CG2 . ILE   A 1 188 ? 20.09864 -8.07896  42.80226  1.000 10.47366 ? 184 ILE   A CG2 1 
ATOM   1438 C  CD1 . ILE   A 1 188 ? 21.21808 -6.15888  40.83814  1.000 8.99194  ? 184 ILE   A CD1 1 
ATOM   1439 N  N   . GLU   A 1 189 ? 17.71498 -10.69023 41.34397  1.000 12.10442 ? 185 GLU   A N   1 
ATOM   1440 C  CA  . GLU   A 1 189 ? 16.74139 -11.58264 41.96839  1.000 16.54212 ? 185 GLU   A CA  1 
ATOM   1441 C  C   . GLU   A 1 189 ? 17.29984 -12.99708 42.08044  1.000 11.04018 ? 185 GLU   A C   1 
ATOM   1442 O  O   . GLU   A 1 189 ? 17.18665 -13.64174 43.13137  1.000 12.52960 ? 185 GLU   A O   1 
ATOM   1443 C  CB  . GLU   A 1 189 ? 15.43508 -11.58562 41.17067  1.000 10.90791 ? 185 GLU   A CB  1 
ATOM   1444 C  CG  . GLU   A 1 189 ? 14.36609 -12.51830 41.73292  1.000 11.58289 ? 185 GLU   A CG  1 
ATOM   1445 C  CD  . GLU   A 1 189 ? 13.28760 -12.87944 40.71713  1.000 20.92102 ? 185 GLU   A CD  1 
ATOM   1446 O  OE1 . GLU   A 1 189 ? 13.23469 -12.25522 39.63318  1.000 20.80881 ? 185 GLU   A OE1 1 
ATOM   1447 O  OE2 . GLU   A 1 189 ? 12.49496 -13.80335 40.99983  1.000 24.37616 ? 185 GLU   A OE2 1 
ATOM   1448 N  N   . GLY   A 1 190 ? 17.92596 -13.48785 41.00753  1.000 14.04415 ? 186 GLY   A N   1 
ATOM   1449 C  CA  . GLY   A 1 190 ? 18.53783 -14.80455 41.05066  1.000 12.10225 ? 186 GLY   A CA  1 
ATOM   1450 C  C   . GLY   A 1 190 ? 19.70683 -14.89036 42.01177  1.000 12.60754 ? 186 GLY   A C   1 
ATOM   1451 O  O   . GLY   A 1 190 ? 19.93815 -15.94179 42.61332  1.000 14.97816 ? 186 GLY   A O   1 
ATOM   1452 N  N   . GLU   A 1 191 ? 20.45883 -13.79546 42.16706  1.000 11.35234 ? 187 GLU   A N   1 
ATOM   1453 C  CA  . GLU   A 1 191 ? 21.56159 -13.76933 43.12865  1.000 14.09262 ? 187 GLU   A CA  1 
ATOM   1454 C  C   . GLU   A 1 191 ? 21.06315 -13.91083 44.56340  1.000 17.64308 ? 187 GLU   A C   1 
ATOM   1455 O  O   . GLU   A 1 191 ? 21.70684 -14.57357 45.38828  1.000 12.96577 ? 187 GLU   A O   1 
ATOM   1456 C  CB  . GLU   A 1 191 ? 22.36136 -12.47367 42.97447  1.000 15.82312 ? 187 GLU   A CB  1 
ATOM   1457 C  CG  . GLU   A 1 191 ? 23.21290 -12.40378 41.71824  1.000 21.94508 ? 187 GLU   A CG  1 
ATOM   1458 C  CD  . GLU   A 1 191 ? 24.51886 -13.16633 41.84998  1.000 35.37660 ? 187 GLU   A CD  1 
ATOM   1459 O  OE1 . GLU   A 1 191 ? 24.85374 -13.59058 42.97719  1.000 25.90046 ? 187 GLU   A OE1 1 
ATOM   1460 O  OE2 . GLU   A 1 191 ? 25.21481 -13.33504 40.82819  1.000 32.20372 ? 187 GLU   A OE2 1 
ATOM   1461 N  N   . MET   A 1 192 ? 19.93186 -13.28330 44.89368  1.000 14.28624 ? 188 MET   A N   1 
ATOM   1462 C  CA  . MET   A 1 192 ? 19.38014 -13.47143 46.23224  1.000 12.47483 ? 188 MET   A CA  1 
ATOM   1463 C  C   . MET   A 1 192 ? 18.80459 -14.86983 46.39716  1.000 11.59079 ? 188 MET   A C   1 
ATOM   1464 O  O   . MET   A 1 192 ? 18.83380 -15.42657 47.50313  1.000 12.19487 ? 188 MET   A O   1 
ATOM   1465 C  CB  . MET   A 1 192 ? 18.30926 -12.42261 46.52921  1.000 16.73860 ? 188 MET   A CB  1 
ATOM   1466 C  CG  . MET   A 1 192 ? 18.79726 -10.99487 46.41938  1.000 24.63044 ? 188 MET   A CG  1 
ATOM   1467 S  SD  . MET   A 1 192 ? 20.27152 -10.67056 47.41108  1.000 18.87516 ? 188 MET   A SD  1 
ATOM   1468 C  CE  . MET   A 1 192 ? 21.07024 -9.48569  46.33063  1.000 28.41239 ? 188 MET   A CE  1 
ATOM   1469 N  N   . ARG   A 1 193 ? 18.28136 -15.45005 45.31457  1.000 12.05008 ? 189 ARG   A N   1 
ATOM   1470 C  CA  . ARG   A 1 193 ? 17.79669 -16.82482 45.37209  1.000 17.23567 ? 189 ARG   A CA  1 
ATOM   1471 C  C   . ARG   A 1 193 ? 18.92470 -17.79755 45.69253  1.000 13.66989 ? 189 ARG   A C   1 
ATOM   1472 O  O   . ARG   A 1 193 ? 18.73082 -18.74779 46.45925  1.000 15.40488 ? 189 ARG   A O   1 
ATOM   1473 C  CB  . ARG   A 1 193 ? 17.11281 -17.20269 44.05578  1.000 21.53489 ? 189 ARG   A CB  1 
ATOM   1474 C  CG  . ARG   A 1 193 ? 15.74876 -16.54228 43.85615  1.000 26.40798 ? 189 ARG   A CG  1 
ATOM   1475 C  CD  . ARG   A 1 193 ? 15.28531 -16.61710 42.40558  1.000 24.90097 ? 189 ARG   A CD  1 
ATOM   1476 N  NE  . ARG   A 1 193 ? 15.24048 -17.98880 41.91439  1.000 22.76716 ? 189 ARG   A NE  1 
ATOM   1477 C  CZ  . ARG   A 1 193 ? 14.16371 -18.76142 41.94845  1.000 40.55371 ? 189 ARG   A CZ  1 
ATOM   1478 N  NH1 . ARG   A 1 193 ? 13.01774 -18.32731 42.44588  1.000 32.38449 ? 189 ARG   A NH1 1 
ATOM   1479 N  NH2 . ARG   A 1 193 ? 14.23861 -20.00171 41.47293  1.000 41.32459 ? 189 ARG   A NH2 1 
ATOM   1480 N  N   A THR   A 1 194 ? 20.10909 -17.58074 45.11210  0.945 15.50388 ? 190 THR   A N   1 
ATOM   1481 N  N   B THR   A 1 194 ? 20.11766 -17.57260 45.13343  0.055 15.59948 ? 190 THR   A N   1 
ATOM   1482 C  CA  A THR   A 1 194 ? 21.23199 -18.46689 45.39898  0.945 16.02141 ? 190 THR   A CA  1 
ATOM   1483 C  CA  B THR   A 1 194 ? 21.21749 -18.49639 45.39734  0.055 16.10088 ? 190 THR   A CA  1 
ATOM   1484 C  C   A THR   A 1 194 ? 21.61822 -18.39780 46.86819  0.945 14.89730 ? 190 THR   A C   1 
ATOM   1485 C  C   B THR   A 1 194 ? 21.72075 -18.37627 46.83263  0.055 15.06789 ? 190 THR   A C   1 
ATOM   1486 O  O   A THR   A 1 194 ? 21.94443 -19.42108 47.48212  0.945 15.00330 ? 190 THR   A O   1 
ATOM   1487 O  O   B THR   A 1 194 ? 22.23252 -19.35471 47.38848  0.055 15.09927 ? 190 THR   A O   1 
ATOM   1488 C  CB  A THR   A 1 194 ? 22.43354 -18.12407 44.51666  0.945 20.98358 ? 190 THR   A CB  1 
ATOM   1489 C  CB  B THR   A 1 194 ? 22.36081 -18.28167 44.39837  0.055 20.37361 ? 190 THR   A CB  1 
ATOM   1490 O  OG1 A THR   A 1 194 ? 22.92565 -16.82230 44.85346  0.945 32.50079 ? 190 THR   A OG1 1 
ATOM   1491 O  OG1 B THR   A 1 194 ? 23.18001 -19.45562 44.35155  0.055 19.71478 ? 190 THR   A OG1 1 
ATOM   1492 C  CG2 A THR   A 1 194 ? 22.03644 -18.15029 43.05055  0.945 14.05010 ? 190 THR   A CG2 1 
ATOM   1493 C  CG2 B THR   A 1 194 ? 23.23244 -17.11153 44.79782  0.055 24.90887 ? 190 THR   A CG2 1 
ATOM   1494 N  N   . ARG   A 1 195 ? 21.57446 -17.20158 47.45423  1.000 15.05935 ? 191 ARG   A N   1 
ATOM   1495 C  CA  . ARG   A 1 195 ? 21.93004 -17.06977 48.86196  1.000 17.52094 ? 191 ARG   A CA  1 
ATOM   1496 C  C   . ARG   A 1 195 ? 20.92999 -17.80698 49.74556  1.000 16.98585 ? 191 ARG   A C   1 
ATOM   1497 O  O   . ARG   A 1 195 ? 21.31126 -18.42238 50.75000  1.000 15.86173 ? 191 ARG   A O   1 
ATOM   1498 C  CB  . ARG   A 1 195 ? 22.02853 -15.58946 49.23523  1.000 12.61412 ? 191 ARG   A CB  1 
ATOM   1499 C  CG  . ARG   A 1 195 ? 23.29203 -14.92926 48.69921  1.000 12.95128 ? 191 ARG   A CG  1 
ATOM   1500 C  CD  . ARG   A 1 195 ? 23.19145 -13.40964 48.64065  1.000 15.70245 ? 191 ARG   A CD  1 
ATOM   1501 N  NE  . ARG   A 1 195 ? 24.47228 -12.81493 48.27483  1.000 18.16502 ? 191 ARG   A NE  1 
ATOM   1502 C  CZ  . ARG   A 1 195 ? 24.95089 -12.74983 47.03853  1.000 30.49446 ? 191 ARG   A CZ  1 
ATOM   1503 N  NH1 . ARG   A 1 195 ? 24.26868 -13.21899 46.00397  1.000 22.12266 ? 191 ARG   A NH1 1 
ATOM   1504 N  NH2 . ARG   A 1 195 ? 26.14560 -12.20037 46.83395  1.000 25.22897 ? 191 ARG   A NH2 1 
ATOM   1505 N  N   . ILE   A 1 196 ? 19.65027 -17.77932 49.36977  1.000 13.80985 ? 192 ILE   A N   1 
ATOM   1506 C  CA  . ILE   A 1 196 ? 18.63437 -18.51247 50.11800  1.000 18.64954 ? 192 ILE   A CA  1 
ATOM   1507 C  C   . ILE   A 1 196 ? 18.77182 -20.01381 49.88409  1.000 24.61660 ? 192 ILE   A C   1 
ATOM   1508 O  O   . ILE   A 1 196 ? 18.56323 -20.81767 50.80020  1.000 20.95615 ? 192 ILE   A O   1 
ATOM   1509 C  CB  . ILE   A 1 196 ? 17.23447 -17.99462 49.74088  1.000 15.94912 ? 192 ILE   A CB  1 
ATOM   1510 C  CG1 . ILE   A 1 196 ? 17.09287 -16.52369 50.13754  1.000 20.66560 ? 192 ILE   A CG1 1 
ATOM   1511 C  CG2 . ILE   A 1 196 ? 16.14947 -18.82895 50.41147  1.000 27.52977 ? 192 ILE   A CG2 1 
ATOM   1512 C  CD1 . ILE   A 1 196 ? 16.05546 -15.76955 49.33484  1.000 29.74686 ? 192 ILE   A CD1 1 
ATOM   1513 N  N   . ARG   A 1 197 ? 19.13654 -20.41551 48.66058  1.000 15.99798 ? 193 ARG   A N   1 
ATOM   1514 C  CA  . ARG   A 1 197 ? 19.32020 -21.83434 48.36191  1.000 17.28438 ? 193 ARG   A CA  1 
ATOM   1515 C  C   . ARG   A 1 197 ? 20.44795 -22.43695 49.19079  1.000 17.93442 ? 193 ARG   A C   1 
ATOM   1516 O  O   . ARG   A 1 197 ? 20.33342 -23.56606 49.68232  1.000 19.70227 ? 193 ARG   A O   1 
ATOM   1517 C  CB  . ARG   A 1 197 ? 19.60027 -22.02616 46.86778  1.000 18.89304 ? 193 ARG   A CB  1 
ATOM   1518 C  CG  . ARG   A 1 197 ? 18.50208 -22.75290 46.10656  1.000 34.64666 ? 193 ARG   A CG  1 
ATOM   1519 C  CD  . ARG   A 1 197 ? 18.98511 -23.26149 44.74479  1.000 25.77107 ? 193 ARG   A CD  1 
ATOM   1520 N  NE  . ARG   A 1 197 ? 19.76707 -22.26857 44.01474  1.000 28.69149 ? 193 ARG   A NE  1 
ATOM   1521 C  CZ  . ARG   A 1 197 ? 21.04444 -22.41268 43.68218  1.000 25.16465 ? 193 ARG   A CZ  1 
ATOM   1522 N  NH1 . ARG   A 1 197 ? 21.71838 -23.50981 43.98241  1.000 21.78943 ? 193 ARG   A NH1 1 
ATOM   1523 N  NH2 . ARG   A 1 197 ? 21.65661 -21.43741 43.01659  1.000 25.43309 ? 193 ARG   A NH2 1 
ATOM   1524 N  N   . TYR   A 1 198 ? 21.54697 -21.70279 49.35260  1.000 17.25599 ? 194 TYR   A N   1 
ATOM   1525 C  CA  . TYR   A 1 198 ? 22.68442 -22.16186 50.13755  1.000 17.91730 ? 194 TYR   A CA  1 
ATOM   1526 C  C   . TYR   A 1 198 ? 22.54631 -21.85096 51.62287  1.000 17.89812 ? 194 TYR   A C   1 
ATOM   1527 O  O   . TYR   A 1 198 ? 23.35757 -22.34018 52.41657  1.000 18.67953 ? 194 TYR   A O   1 
ATOM   1528 C  CB  . TYR   A 1 198 ? 23.98222 -21.52897 49.61639  1.000 17.39274 ? 194 TYR   A CB  1 
ATOM   1529 C  CG  . TYR   A 1 198 ? 24.58500 -22.21884 48.41240  1.000 19.86721 ? 194 TYR   A CG  1 
ATOM   1530 C  CD1 . TYR   A 1 198 ? 24.19303 -21.88439 47.12443  1.000 19.02407 ? 194 TYR   A CD1 1 
ATOM   1531 C  CD2 . TYR   A 1 198 ? 25.55492 -23.20009 48.56664  1.000 23.74467 ? 194 TYR   A CD2 1 
ATOM   1532 C  CE1 . TYR   A 1 198 ? 24.74976 -22.51353 46.02055  1.000 23.14178 ? 194 TYR   A CE1 1 
ATOM   1533 C  CE2 . TYR   A 1 198 ? 26.11301 -23.83359 47.47461  1.000 24.21075 ? 194 TYR   A CE2 1 
ATOM   1534 C  CZ  . TYR   A 1 198 ? 25.70894 -23.48715 46.20527  1.000 21.77683 ? 194 TYR   A CZ  1 
ATOM   1535 O  OH  . TYR   A 1 198 ? 26.26745 -24.12013 45.11983  1.000 23.92405 ? 194 TYR   A OH  1 
ATOM   1536 N  N   . ASN   A 1 199 ? 21.54603 -21.06000 52.01090  1.000 17.14815 ? 195 ASN   A N   1 
ATOM   1537 C  CA  . ASN   A 1 199 ? 21.42493 -20.55513 53.37755  1.000 21.17561 ? 195 ASN   A CA  1 
ATOM   1538 C  C   . ASN   A 1 199 ? 22.72811 -19.88622 53.82031  1.000 25.10569 ? 195 ASN   A C   1 
ATOM   1539 O  O   . ASN   A 1 199 ? 23.22087 -20.08814 54.93373  1.000 17.25647 ? 195 ASN   A O   1 
ATOM   1540 C  CB  . ASN   A 1 199 ? 21.01208 -21.67087 54.34320  1.000 18.37546 ? 195 ASN   A CB  1 
ATOM   1541 C  CG  . ASN   A 1 199 ? 20.65269 -21.14447 55.72336  1.000 20.48201 ? 195 ASN   A CG  1 
ATOM   1542 O  OD1 . ASN   A 1 199 ? 20.18340 -20.01637 55.86296  1.000 22.50758 ? 195 ASN   A OD1 1 
ATOM   1543 N  ND2 . ASN   A 1 199 ? 20.89046 -21.95349 56.74975  1.000 19.54507 ? 195 ASN   A ND2 1 
ATOM   1544 N  N   . ARG   A 1 200 ? 23.29130 -19.07553 52.91905  1.000 15.74980 ? 196 ARG   A N   1 
ATOM   1545 C  CA  . ARG   A 1 200 ? 24.56554 -18.40491 53.14017  1.000 15.46506 ? 196 ARG   A CA  1 
ATOM   1546 C  C   . ARG   A 1 200 ? 24.43180 -16.92439 52.82250  1.000 19.20113 ? 196 ARG   A C   1 
ATOM   1547 O  O   . ARG   A 1 200 ? 23.75739 -16.54708 51.85963  1.000 37.83445 ? 196 ARG   A O   1 
ATOM   1548 C  CB  . ARG   A 1 200 ? 25.68429 -19.00528 52.27509  1.000 25.63300 ? 196 ARG   A CB  1 
ATOM   1549 C  CG  . ARG   A 1 200 ? 25.95997 -20.48567 52.48939  1.000 31.56769 ? 196 ARG   A CG  1 
ATOM   1550 C  CD  . ARG   A 1 200 ? 27.38200 -20.80225 52.04091  1.000 38.25001 ? 196 ARG   A CD  1 
ATOM   1551 N  NE  . ARG   A 1 200 ? 27.57864 -22.18151 51.59331  1.000 58.82950 ? 196 ARG   A NE  1 
ATOM   1552 C  CZ  . ARG   A 1 200 ? 28.74856 -22.67571 51.20900  1.000 56.37797 ? 196 ARG   A CZ  1 
ATOM   1553 N  NH1 . ARG   A 1 200 ? 29.84692 -21.93593 51.21629  1.000 63.83555 ? 196 ARG   A NH1 1 
ATOM   1554 N  NH2 . ARG   A 1 200 ? 28.81910 -23.94121 50.81179  1.000 59.54155 ? 196 ARG   A NH2 1 
ATOM   1555 N  N   . ARG   A 1 201 ? 25.07955 -16.09314 53.63251  1.000 13.90881 ? 197 ARG   A N   1 
ATOM   1556 C  CA  . ARG   A 1 201 ? 25.18512 -14.66729 53.36940  1.000 16.07328 ? 197 ARG   A CA  1 
ATOM   1557 C  C   . ARG   A 1 201 ? 26.51596 -14.38175 52.68625  1.000 18.33410 ? 197 ARG   A C   1 
ATOM   1558 O  O   . ARG   A 1 201 ? 27.52664 -15.02660 52.98191  1.000 14.79423 ? 197 ARG   A O   1 
ATOM   1559 C  CB  . ARG   A 1 201 ? 25.07295 -13.85349 54.66303  1.000 17.99657 ? 197 ARG   A CB  1 
ATOM   1560 C  CG  . ARG   A 1 201 ? 26.26998 -13.99191 55.58976  1.000 20.32571 ? 197 ARG   A CG  1 
ATOM   1561 C  CD  . ARG   A 1 201 ? 26.28817 -12.87742 56.61969  1.000 33.08457 ? 197 ARG   A CD  1 
ATOM   1562 N  NE  . ARG   A 1 201 ? 25.23641 -13.04477 57.61021  1.000 28.86944 ? 197 ARG   A NE  1 
ATOM   1563 C  CZ  . ARG   A 1 201 ? 24.77925 -12.07824 58.39332  1.000 24.31770 ? 197 ARG   A CZ  1 
ATOM   1564 N  NH1 . ARG   A 1 201 ? 25.24134 -10.84106 58.30890  1.000 30.27196 ? 197 ARG   A NH1 1 
ATOM   1565 N  NH2 . ARG   A 1 201 ? 23.82946 -12.36009 59.27949  1.000 20.05826 ? 197 ARG   A NH2 1 
ATOM   1566 N  N   . SER   A 1 202 ? 26.50539 -13.42747 51.75686  1.000 14.20608 ? 198 SER   A N   1 
ATOM   1567 C  CA  . SER   A 1 202 ? 27.71868 -13.04710 51.04612  1.000 12.68244 ? 198 SER   A CA  1 
ATOM   1568 C  C   . SER   A 1 202 ? 27.50250 -11.69670 50.37620  1.000 11.17831 ? 198 SER   A C   1 
ATOM   1569 O  O   . SER   A 1 202 ? 26.37322 -11.32241 50.05329  1.000 10.57287 ? 198 SER   A O   1 
ATOM   1570 C  CB  . SER   A 1 202 ? 28.11619 -14.09507 50.00179  1.000 23.17261 ? 198 SER   A CB  1 
ATOM   1571 O  OG  . SER   A 1 202 ? 27.18889 -14.10918 48.93477  1.000 20.01203 ? 198 SER   A OG  1 
ATOM   1572 N  N   . ALA   A 1 203 ? 28.60170 -10.97583 50.17781  1.000 11.21018 ? 199 ALA   A N   1 
ATOM   1573 C  CA  . ALA   A 1 203 ? 28.54941 -9.68851  49.50776  1.000 10.52077 ? 199 ALA   A CA  1 
ATOM   1574 C  C   . ALA   A 1 203 ? 28.32329 -9.88017  48.00800  1.000 11.59392 ? 199 ALA   A C   1 
ATOM   1575 O  O   . ALA   A 1 203 ? 28.68790 -10.91571 47.44684  1.000 10.96946 ? 199 ALA   A O   1 
ATOM   1576 C  CB  . ALA   A 1 203 ? 29.84440 -8.92034  49.74655  1.000 14.69875 ? 199 ALA   A CB  1 
ATOM   1577 N  N   . PRO   A 1 204 ? 27.71710 -8.90007  47.33610  1.000 11.33235 ? 200 PRO   A N   1 
ATOM   1578 C  CA  . PRO   A 1 204 ? 27.51918 -9.02294  45.88646  1.000 11.66583 ? 200 PRO   A CA  1 
ATOM   1579 C  C   . PRO   A 1 204 ? 28.83865 -8.89246  45.14020  1.000 13.80522 ? 200 PRO   A C   1 
ATOM   1580 O  O   . PRO   A 1 204 ? 29.70542 -8.09847  45.51388  1.000 14.48253 ? 200 PRO   A O   1 
ATOM   1581 C  CB  . PRO   A 1 204 ? 26.57157 -7.86306  45.56227  1.000 14.97848 ? 200 PRO   A CB  1 
ATOM   1582 C  CG  . PRO   A 1 204 ? 26.87780 -6.84799  46.59920  1.000 14.71115 ? 200 PRO   A CG  1 
ATOM   1583 C  CD  . PRO   A 1 204 ? 27.17380 -7.63365  47.85694  1.000 10.40689 ? 200 PRO   A CD  1 
ATOM   1584 N  N   . ASP   A 1 205 ? 28.98830 -9.68555  44.08171  1.000 12.57148 ? 201 ASP   A N   1 
ATOM   1585 C  CA  . ASP   A 1 205 ? 30.21659 -9.71495  43.29485  1.000 12.46033 ? 201 ASP   A CA  1 
ATOM   1586 C  C   . ASP   A 1 205 ? 30.18398 -8.61936  42.23074  1.000 11.00805 ? 201 ASP   A C   1 
ATOM   1587 O  O   . ASP   A 1 205 ? 29.17048 -7.93660  42.06346  1.000 13.00389 ? 201 ASP   A O   1 
ATOM   1588 C  CB  . ASP   A 1 205 ? 30.41723 -11.12578 42.71926  1.000 19.18806 ? 201 ASP   A CB  1 
ATOM   1589 C  CG  . ASP   A 1 205 ? 29.38850 -11.51449 41.66569  1.000 27.05357 ? 201 ASP   A CG  1 
ATOM   1590 O  OD1 . ASP   A 1 205 ? 28.69894 -10.64013 41.10262  1.000 23.07714 ? 201 ASP   A OD1 1 
ATOM   1591 O  OD2 . ASP   A 1 205 ? 29.28403 -12.73207 41.38942  1.000 28.92592 ? 201 ASP   A OD2 1 
ATOM   1592 N  N   . PRO   A 1 206 ? 31.29332 -8.39069  41.50674  1.000 11.64631 ? 202 PRO   A N   1 
ATOM   1593 C  CA  . PRO   A 1 206 ? 31.34360 -7.21650  40.61354  1.000 15.23901 ? 202 PRO   A CA  1 
ATOM   1594 C  C   . PRO   A 1 206 ? 30.28945 -7.19666  39.51745  1.000 17.31694 ? 202 PRO   A C   1 
ATOM   1595 O  O   . PRO   A 1 206 ? 29.94699 -6.10943  39.03270  1.000 15.16421 ? 202 PRO   A O   1 
ATOM   1596 C  CB  . PRO   A 1 206 ? 32.75799 -7.29084  40.01847  1.000 18.53536 ? 202 PRO   A CB  1 
ATOM   1597 C  CG  . PRO   A 1 206 ? 33.54834 -8.02662  41.01394  1.000 17.41867 ? 202 PRO   A CG  1 
ATOM   1598 C  CD  . PRO   A 1 206 ? 32.61715 -9.03987  41.60460  1.000 12.95446 ? 202 PRO   A CD  1 
ATOM   1599 N  N   . SER   A 1 207 ? 29.77588 -8.35364  39.09448  1.000 9.72821  ? 203 SER   A N   1 
ATOM   1600 C  CA  . SER   A 1 207 ? 28.73365 -8.35589  38.07204  1.000 12.11865 ? 203 SER   A CA  1 
ATOM   1601 C  C   . SER   A 1 207 ? 27.46162 -7.70170  38.59083  1.000 11.67037 ? 203 SER   A C   1 
ATOM   1602 O  O   . SER   A 1 207 ? 26.77083 -6.98961  37.85182  1.000 11.13521 ? 203 SER   A O   1 
ATOM   1603 C  CB  . SER   A 1 207 ? 28.45078 -9.78619  37.60673  1.000 13.17714 ? 203 SER   A CB  1 
ATOM   1604 O  OG  . SER   A 1 207 ? 27.81747 -10.54135 38.62661  1.000 12.01387 ? 203 SER   A OG  1 
ATOM   1605 N  N   . VAL   A 1 208 ? 27.14554 -7.92380  39.86439  1.000 13.46405 ? 204 VAL   A N   1 
ATOM   1606 C  CA  . VAL   A 1 208 ? 25.96207 -7.31702  40.46217  1.000 11.27564 ? 204 VAL   A CA  1 
ATOM   1607 C  C   . VAL   A 1 208 ? 26.15847 -5.81655  40.62831  1.000 10.78417 ? 204 VAL   A C   1 
ATOM   1608 O  O   . VAL   A 1 208 ? 25.27987 -5.01561  40.28720  1.000 10.43635 ? 204 VAL   A O   1 
ATOM   1609 C  CB  . VAL   A 1 208 ? 25.64695 -7.99533  41.80706  1.000 9.18718  ? 204 VAL   A CB  1 
ATOM   1610 C  CG1 . VAL   A 1 208 ? 24.50731 -7.27171  42.52979  1.000 12.17342 ? 204 VAL   A CG1 1 
ATOM   1611 C  CG2 . VAL   A 1 208 ? 25.32460 -9.46006  41.58811  1.000 15.23151 ? 204 VAL   A CG2 1 
ATOM   1612 N  N   . ILE   A 1 209 ? 27.31368 -5.41565  41.16200  1.000 9.81658  ? 205 ILE   A N   1 
ATOM   1613 C  CA  . ILE   A 1 209 ? 27.54896 -4.00767  41.46535  1.000 9.95633  ? 205 ILE   A CA  1 
ATOM   1614 C  C   . ILE   A 1 209 ? 27.50974 -3.16840  40.19244  1.000 10.85169 ? 205 ILE   A C   1 
ATOM   1615 O  O   . ILE   A 1 209 ? 26.92131 -2.07834  40.16547  1.000 11.16924 ? 205 ILE   A O   1 
ATOM   1616 C  CB  . ILE   A 1 209 ? 28.87905 -3.85464  42.22558  1.000 11.02963 ? 205 ILE   A CB  1 
ATOM   1617 C  CG1 . ILE   A 1 209 ? 28.74590 -4.48269  43.61581  1.000 13.90368 ? 205 ILE   A CG1 1 
ATOM   1618 C  CG2 . ILE   A 1 209 ? 29.28369 -2.38540  42.33709  1.000 14.72245 ? 205 ILE   A CG2 1 
ATOM   1619 C  CD1 . ILE   A 1 209 ? 30.05915 -4.79194  44.26425  1.000 26.50065 ? 205 ILE   A CD1 1 
ATOM   1620 N  N   . THR   A 1 210 ? 28.10591 -3.67273  39.10874  1.000 9.88792  ? 206 THR   A N   1 
ATOM   1621 C  CA  . THR   A 1 210 ? 28.13502 -2.90665  37.86706  1.000 10.07039 ? 206 THR   A CA  1 
ATOM   1622 C  C   . THR   A 1 210 ? 26.75623 -2.83555  37.21719  1.000 13.53146 ? 206 THR   A C   1 
ATOM   1623 O  O   . THR   A 1 210 ? 26.40566 -1.80762  36.62256  1.000 11.59329 ? 206 THR   A O   1 
ATOM   1624 C  CB  . THR   A 1 210 ? 29.18131 -3.49966  36.91561  1.000 14.51927 ? 206 THR   A CB  1 
ATOM   1625 O  OG1 . THR   A 1 210 ? 30.49158 -3.12028  37.35857  1.000 14.99441 ? 206 THR   A OG1 1 
ATOM   1626 C  CG2 . THR   A 1 210 ? 28.98773 -3.01311  35.48035  1.000 14.46874 ? 206 THR   A CG2 1 
ATOM   1627 N  N   . LEU   A 1 211 ? 25.95375 -3.89859  37.32306  1.000 13.39407 ? 207 LEU   A N   1 
ATOM   1628 C  CA  . LEU   A 1 211 ? 24.57906 -3.81089  36.83733  1.000 13.42736 ? 207 LEU   A CA  1 
ATOM   1629 C  C   . LEU   A 1 211 ? 23.80670 -2.74214  37.59642  1.000 9.09952  ? 207 LEU   A C   1 
ATOM   1630 O  O   . LEU   A 1 211 ? 23.07876 -1.94388  36.99425  1.000 11.64310 ? 207 LEU   A O   1 
ATOM   1631 C  CB  . LEU   A 1 211 ? 23.87079 -5.15580  36.96489  1.000 10.03323 ? 207 LEU   A CB  1 
ATOM   1632 C  CG  . LEU   A 1 211 ? 24.01677 -6.21402  35.87991  1.000 15.59463 ? 207 LEU   A CG  1 
ATOM   1633 C  CD1 . LEU   A 1 211 ? 23.22136 -7.45038  36.29173  1.000 13.88673 ? 207 LEU   A CD1 1 
ATOM   1634 C  CD2 . LEU   A 1 211 ? 23.54418 -5.70571  34.52220  1.000 11.73694 ? 207 LEU   A CD2 1 
ATOM   1635 N  N   . GLU   A 1 212 ? 23.94353 -2.72213  38.92504  1.000 9.25946  ? 208 GLU   A N   1 
ATOM   1636 C  CA  . GLU   A 1 212 ? 23.31817 -1.67177  39.72283  1.000 10.27104 ? 208 GLU   A CA  1 
ATOM   1637 C  C   . GLU   A 1 212 ? 23.76265 -0.29570  39.24797  1.000 12.02090 ? 208 GLU   A C   1 
ATOM   1638 O  O   . GLU   A 1 212 ? 22.93565 0.59529   39.02744  1.000 12.65412 ? 208 GLU   A O   1 
ATOM   1639 C  CB  . GLU   A 1 212 ? 23.65180 -1.86573  41.20422  1.000 12.77527 ? 208 GLU   A CB  1 
ATOM   1640 C  CG  . GLU   A 1 212 ? 23.07278 -3.14092  41.80357  1.000 9.66873  ? 208 GLU   A CG  1 
ATOM   1641 C  CD  . GLU   A 1 212 ? 23.51835 -3.38484  43.23979  1.000 16.00485 ? 208 GLU   A CD  1 
ATOM   1642 O  OE1 . GLU   A 1 212 ? 24.29770 -2.56845  43.77680  1.000 15.79241 ? 208 GLU   A OE1 1 
ATOM   1643 O  OE2 . GLU   A 1 212 ? 23.09306 -4.40333  43.83090  1.000 14.60160 ? 208 GLU   A OE2 1 
ATOM   1644 N  N   . ASN   A 1 213 ? 25.07204 -0.11209  39.06517  1.000 10.45283 ? 209 ASN   A N   1 
ATOM   1645 C  CA  . ASN   A 1 213 ? 25.59692 1.18264   38.64621  1.000 12.35887 ? 209 ASN   A CA  1 
ATOM   1646 C  C   . ASN   A 1 213 ? 25.12832 1.58019   37.25130  1.000 16.84394 ? 209 ASN   A C   1 
ATOM   1647 O  O   . ASN   A 1 213 ? 25.13274 2.77275   36.92565  1.000 13.61477 ? 209 ASN   A O   1 
ATOM   1648 C  CB  . ASN   A 1 213 ? 27.12650 1.17008   38.67411  1.000 11.62554 ? 209 ASN   A CB  1 
ATOM   1649 C  CG  . ASN   A 1 213 ? 27.69532 1.04269   40.08408  1.000 13.14333 ? 209 ASN   A CG  1 
ATOM   1650 O  OD1 . ASN   A 1 213 ? 26.98835 1.21833   41.07557  1.000 12.40267 ? 209 ASN   A OD1 1 
ATOM   1651 N  ND2 . ASN   A 1 213 ? 28.98889 0.74812   40.17021  1.000 13.08453 ? 209 ASN   A ND2 1 
ATOM   1652 N  N   . SER   A 1 214 ? 24.72236 0.61594   36.42932  1.000 11.07481 ? 210 SER   A N   1 
ATOM   1653 C  CA  . SER   A 1 214 ? 24.44086 0.84735   35.01852  1.000 10.95008 ? 210 SER   A CA  1 
ATOM   1654 C  C   . SER   A 1 214 ? 22.95483 0.91007   34.69013  1.000 14.46906 ? 210 SER   A C   1 
ATOM   1655 O  O   . SER   A 1 214 ? 22.60699 1.07329   33.51655  1.000 15.37212 ? 210 SER   A O   1 
ATOM   1656 C  CB  . SER   A 1 214 ? 25.09176 -0.25065  34.17118  1.000 14.60302 ? 210 SER   A CB  1 
ATOM   1657 O  OG  . SER   A 1 214 ? 26.48910 -0.30766  34.38814  1.000 20.09665 ? 210 SER   A OG  1 
ATOM   1658 N  N   . TRP   A 1 215 ? 22.07136 0.78358   35.68372  1.000 10.23558 ? 211 TRP   A N   1 
ATOM   1659 C  CA  . TRP   A 1 215 ? 20.64302 0.67136   35.38903  1.000 10.54673 ? 211 TRP   A CA  1 
ATOM   1660 C  C   . TRP   A 1 215 ? 20.13588 1.87221   34.59714  1.000 11.80971 ? 211 TRP   A C   1 
ATOM   1661 O  O   . TRP   A 1 215 ? 19.39640 1.71026   33.61843  1.000 11.16375 ? 211 TRP   A O   1 
ATOM   1662 C  CB  . TRP   A 1 215 ? 19.85323 0.50647   36.68543  1.000 10.12362 ? 211 TRP   A CB  1 
ATOM   1663 C  CG  . TRP   A 1 215 ? 18.37690 0.30951   36.48935  1.000 10.16031 ? 211 TRP   A CG  1 
ATOM   1664 C  CD1 . TRP   A 1 215 ? 17.75246 -0.78974  35.96261  1.000 11.23023 ? 211 TRP   A CD1 1 
ATOM   1665 C  CD2 . TRP   A 1 215 ? 17.33788 1.22793   36.84598  1.000 10.78119 ? 211 TRP   A CD2 1 
ATOM   1666 N  NE1 . TRP   A 1 215 ? 16.38881 -0.60333  35.96417  1.000 13.95675 ? 211 TRP   A NE1 1 
ATOM   1667 C  CE2 . TRP   A 1 215 ? 16.11098 0.62691   36.50363  1.000 10.74550 ? 211 TRP   A CE2 1 
ATOM   1668 C  CE3 . TRP   A 1 215 ? 17.32714 2.50286   37.42133  1.000 15.77443 ? 211 TRP   A CE3 1 
ATOM   1669 C  CZ2 . TRP   A 1 215 ? 14.88554 1.26083   36.71190  1.000 11.40657 ? 211 TRP   A CZ2 1 
ATOM   1670 C  CZ3 . TRP   A 1 215 ? 16.10796 3.12936   37.62937  1.000 15.21169 ? 211 TRP   A CZ3 1 
ATOM   1671 C  CH2 . TRP   A 1 215 ? 14.90683 2.50729   37.27601  1.000 12.09444 ? 211 TRP   A CH2 1 
ATOM   1672 N  N   . GLY   A 1 216 ? 20.54102 3.08212   34.99007  1.000 11.41497 ? 212 GLY   A N   1 
ATOM   1673 C  CA  . GLY   A 1 216 ? 20.11459 4.26808   34.26325  1.000 12.17925 ? 212 GLY   A CA  1 
ATOM   1674 C  C   . GLY   A 1 216 ? 20.67342 4.33916   32.85243  1.000 15.86296 ? 212 GLY   A C   1 
ATOM   1675 O  O   . GLY   A 1 216 ? 19.95713 4.69286   31.91143  1.000 14.70657 ? 212 GLY   A O   1 
ATOM   1676 N  N   . ARG   A 1 217 ? 21.96046 4.01470   32.68500  1.000 17.67969 ? 213 ARG   A N   1 
ATOM   1677 C  CA  . ARG   A 1 217 ? 22.55298 3.99805   31.34870  1.000 17.23261 ? 213 ARG   A CA  1 
ATOM   1678 C  C   . ARG   A 1 217 ? 21.92144 2.91955   30.47687  1.000 12.32411 ? 213 ARG   A C   1 
ATOM   1679 O  O   . ARG   A 1 217 ? 21.72421 3.12117   29.27044  1.000 15.07972 ? 213 ARG   A O   1 
ATOM   1680 C  CB  . ARG   A 1 217 ? 24.06345 3.77503   31.43693  1.000 18.44785 ? 213 ARG   A CB  1 
ATOM   1681 C  CG  . ARG   A 1 217 ? 24.80142 4.73776   32.34840  1.000 34.14289 ? 213 ARG   A CG  1 
ATOM   1682 C  CD  . ARG   A 1 217 ? 26.24783 4.29683   32.53985  1.000 41.66176 ? 213 ARG   A CD  1 
ATOM   1683 N  NE  . ARG   A 1 217 ? 26.77071 4.68952   33.84307  1.000 45.78706 ? 213 ARG   A NE  1 
ATOM   1684 C  CZ  . ARG   A 1 217 ? 27.30614 5.87254   34.10916  1.000 45.42184 ? 213 ARG   A CZ  1 
ATOM   1685 N  NH1 . ARG   A 1 217 ? 27.40522 6.81071   33.18116  1.000 54.21821 ? 213 ARG   A NH1 1 
ATOM   1686 N  NH2 . ARG   A 1 217 ? 27.75011 6.12221   35.33764  1.000 47.24504 ? 213 ARG   A NH2 1 
ATOM   1687 N  N   . LEU   A 1 218 ? 21.61873 1.75681   31.06448  1.000 12.67434 ? 214 LEU   A N   1 
ATOM   1688 C  CA  . LEU   A 1 218 ? 21.00570 0.67816   30.29533  1.000 17.84492 ? 214 LEU   A CA  1 
ATOM   1689 C  C   . LEU   A 1 218 ? 19.60335 1.05607   29.83804  1.000 17.34972 ? 214 LEU   A C   1 
ATOM   1690 O  O   . LEU   A 1 218 ? 19.21550 0.75412   28.70302  1.000 15.18407 ? 214 LEU   A O   1 
ATOM   1691 C  CB  . LEU   A 1 218 ? 20.96908 -0.61259  31.11632  1.000 17.05361 ? 214 LEU   A CB  1 
ATOM   1692 C  CG  . LEU   A 1 218 ? 22.30463 -1.30286  31.40858  1.000 10.76619 ? 214 LEU   A CG  1 
ATOM   1693 C  CD1 . LEU   A 1 218 ? 22.12505 -2.37371  32.48159  1.000 13.52743 ? 214 LEU   A CD1 1 
ATOM   1694 C  CD2 . LEU   A 1 218 ? 22.88978 -1.90126  30.14703  1.000 18.93516 ? 214 LEU   A CD2 1 
ATOM   1695 N  N   . SER   A 1 219 ? 18.82661 1.71218   30.70739  1.000 11.25062 ? 215 SER   A N   1 
ATOM   1696 C  CA  . SER   A 1 219 ? 17.49562 2.15913   30.30795  1.000 13.66514 ? 215 SER   A CA  1 
ATOM   1697 C  C   . SER   A 1 219 ? 17.57452 3.13110   29.13850  1.000 13.05005 ? 215 SER   A C   1 
ATOM   1698 O  O   . SER   A 1 219 ? 16.77758 3.04818   28.19577  1.000 12.23830 ? 215 SER   A O   1 
ATOM   1699 C  CB  . SER   A 1 219 ? 16.77682 2.81133   31.48743  1.000 13.54983 ? 215 SER   A CB  1 
ATOM   1700 O  OG  . SER   A 1 219 ? 16.58099 1.89790   32.55026  1.000 13.24177 ? 215 SER   A OG  1 
ATOM   1701 N  N   . THR   A 1 220 ? 18.53634 4.05603   29.18359  1.000 12.86769 ? 216 THR   A N   1 
ATOM   1702 C  CA  . THR   A 1 220 ? 18.70256 5.02177   28.10147  1.000 17.96327 ? 216 THR   A CA  1 
ATOM   1703 C  C   . THR   A 1 220 ? 19.12583 4.33173   26.80840  1.000 16.95502 ? 216 THR   A C   1 
ATOM   1704 O  O   . THR   A 1 220 ? 18.54863 4.58032   25.74188  1.000 13.94950 ? 216 THR   A O   1 
ATOM   1705 C  CB  . THR   A 1 220 ? 19.72819 6.08452   28.50589  1.000 14.84933 ? 216 THR   A CB  1 
ATOM   1706 O  OG1 . THR   A 1 220 ? 19.25113 6.81459   29.64549  1.000 17.34904 ? 216 THR   A OG1 1 
ATOM   1707 C  CG2 . THR   A 1 220 ? 19.98273 7.05099   27.35857  1.000 15.57111 ? 216 THR   A CG2 1 
ATOM   1708 N  N   . ALA   A 1 221 ? 20.13137 3.45449   26.88738  1.000 13.12255 ? 217 ALA   A N   1 
ATOM   1709 C  CA  . ALA   A 1 221 ? 20.65429 2.80478   25.68772  1.000 18.30455 ? 217 ALA   A CA  1 
ATOM   1710 C  C   . ALA   A 1 221 ? 19.58558 1.97221   24.99377  1.000 15.00017 ? 217 ALA   A C   1 
ATOM   1711 O  O   . ALA   A 1 221 ? 19.50804 1.94694   23.76000  1.000 13.21728 ? 217 ALA   A O   1 
ATOM   1712 C  CB  . ALA   A 1 221 ? 21.85440 1.92989   26.04419  1.000 12.64255 ? 217 ALA   A CB  1 
ATOM   1713 N  N   . ILE   A 1 222 ? 18.75572 1.28079   25.77131  1.000 14.91200 ? 218 ILE   A N   1 
ATOM   1714 C  CA  . ILE   A 1 222 ? 17.70990 0.44901   25.18967  1.000 14.41804 ? 218 ILE   A CA  1 
ATOM   1715 C  C   . ILE   A 1 222 ? 16.63245 1.31584   24.54862  1.000 12.45462 ? 218 ILE   A C   1 
ATOM   1716 O  O   . ILE   A 1 222 ? 16.23915 1.09256   23.39788  1.000 16.93941 ? 218 ILE   A O   1 
ATOM   1717 C  CB  . ILE   A 1 222 ? 17.13189 -0.49660  26.25844  1.000 11.16223 ? 218 ILE   A CB  1 
ATOM   1718 C  CG1 . ILE   A 1 222 ? 18.18120 -1.54162  26.64711  1.000 10.52141 ? 218 ILE   A CG1 1 
ATOM   1719 C  CG2 . ILE   A 1 222 ? 15.84693 -1.14644  25.76991  1.000 12.01892 ? 218 ILE   A CG2 1 
ATOM   1720 C  CD1 . ILE   A 1 222 ? 17.83966 -2.33088  27.89943  1.000 11.72363 ? 218 ILE   A CD1 1 
ATOM   1721 N  N   . GLN   A 1 223 ? 16.15680 2.33578   25.26858  1.000 12.92767 ? 219 GLN   A N   1 
ATOM   1722 C  CA  . GLN   A 1 223 ? 15.05272 3.13916   24.75549  1.000 13.47242 ? 219 GLN   A CA  1 
ATOM   1723 C  C   . GLN   A 1 223 ? 15.47493 4.06866   23.62573  1.000 16.70904 ? 219 GLN   A C   1 
ATOM   1724 O  O   . GLN   A 1 223 ? 14.61194 4.52601   22.87047  1.000 26.11995 ? 219 GLN   A O   1 
ATOM   1725 C  CB  . GLN   A 1 223 ? 14.40755 3.93174   25.89510  1.000 15.31168 ? 219 GLN   A CB  1 
ATOM   1726 C  CG  . GLN   A 1 223 ? 13.60040 3.03729   26.83671  1.000 16.43531 ? 219 GLN   A CG  1 
ATOM   1727 C  CD  . GLN   A 1 223 ? 13.15061 3.74657   28.08983  1.000 14.77032 ? 219 GLN   A CD  1 
ATOM   1728 O  OE1 . GLN   A 1 223 ? 12.40680 4.72669   28.03026  1.000 21.22623 ? 219 GLN   A OE1 1 
ATOM   1729 N  NE2 . GLN   A 1 223 ? 13.60098 3.25266   29.24263  1.000 12.70432 ? 219 GLN   A NE2 1 
ATOM   1730 N  N   . GLU   A 1 224 ? 16.77013 4.34678   23.47652  1.000 14.62264 ? 220 GLU   A N   1 
ATOM   1731 C  CA  . GLU   A 1 224 ? 17.24273 5.14863   22.35455  1.000 19.52357 ? 220 GLU   A CA  1 
ATOM   1732 C  C   . GLU   A 1 224 ? 17.68482 4.30691   21.16461  1.000 18.38227 ? 220 GLU   A C   1 
ATOM   1733 O  O   . GLU   A 1 224 ? 17.99779 4.87151   20.11002  1.000 16.80554 ? 220 GLU   A O   1 
ATOM   1734 C  CB  . GLU   A 1 224 ? 18.40772 6.04780   22.78739  1.000 18.24162 ? 220 GLU   A CB  1 
ATOM   1735 C  CG  . GLU   A 1 224 ? 18.02241 7.12909   23.77559  1.000 20.19397 ? 220 GLU   A CG  1 
ATOM   1736 C  CD  . GLU   A 1 224 ? 19.13707 8.13298   24.01290  1.000 34.24977 ? 220 GLU   A CD  1 
ATOM   1737 O  OE1 . GLU   A 1 224 ? 20.21830 7.98575   23.40281  1.000 40.86866 ? 220 GLU   A OE1 1 
ATOM   1738 O  OE2 . GLU   A 1 224 ? 18.92919 9.07227   24.81022  1.000 39.69428 ? 220 GLU   A OE2 1 
ATOM   1739 N  N   . SER   A 1 225 ? 17.69731 2.98384   21.30383  1.000 14.85970 ? 221 SER   A N   1 
ATOM   1740 C  CA  . SER   A 1 225 ? 18.34433 2.11889   20.32777  1.000 17.04104 ? 221 SER   A CA  1 
ATOM   1741 C  C   . SER   A 1 225 ? 17.60314 2.10985   18.99628  1.000 17.68854 ? 221 SER   A C   1 
ATOM   1742 O  O   . SER   A 1 225 ? 16.39310 2.33972   18.92374  1.000 18.20926 ? 221 SER   A O   1 
ATOM   1743 C  CB  . SER   A 1 225 ? 18.43802 0.69153   20.86528  1.000 19.27585 ? 221 SER   A CB  1 
ATOM   1744 O  OG  . SER   A 1 225 ? 17.14977 0.11246   20.98532  1.000 16.08632 ? 221 SER   A OG  1 
ATOM   1745 N  N   . ASN   A 1 226 ? 18.35546 1.83320   17.93428  1.000 16.35790 ? 222 ASN   A N   1 
ATOM   1746 C  CA  . ASN   A 1 226 ? 17.81069 1.65829   16.58930  1.000 22.75506 ? 222 ASN   A CA  1 
ATOM   1747 C  C   . ASN   A 1 226 ? 17.47306 0.18033   16.42952  1.000 21.79956 ? 222 ASN   A C   1 
ATOM   1748 O  O   . ASN   A 1 226 ? 18.34930 -0.63984  16.15085  1.000 21.17570 ? 222 ASN   A O   1 
ATOM   1749 C  CB  . ASN   A 1 226 ? 18.81812 2.13216   15.54582  1.000 26.17811 ? 222 ASN   A CB  1 
ATOM   1750 C  CG  . ASN   A 1 226 ? 18.29174 2.04292   14.11507  1.000 35.97939 ? 222 ASN   A CG  1 
ATOM   1751 O  OD1 . ASN   A 1 226 ? 17.21564 1.49905   13.85399  1.000 29.53197 ? 222 ASN   A OD1 1 
ATOM   1752 N  ND2 . ASN   A 1 226 ? 19.06980 2.57054   13.17686  1.000 34.06860 ? 222 ASN   A ND2 1 
ATOM   1753 N  N   . GLN   A 1 227 ? 16.19569 -0.15696  16.61564  1.000 21.00896 ? 223 GLN   A N   1 
ATOM   1754 C  CA  . GLN   A 1 227 ? 15.71359 -1.53669  16.53294  1.000 24.97341 ? 223 GLN   A CA  1 
ATOM   1755 C  C   . GLN   A 1 227 ? 16.53956 -2.47102  17.41300  1.000 27.58376 ? 223 GLN   A C   1 
ATOM   1756 O  O   . GLN   A 1 227 ? 16.88550 -3.58685  17.02079  1.000 23.72965 ? 223 GLN   A O   1 
ATOM   1757 C  CB  . GLN   A 1 227 ? 15.69017 -2.03036  15.08387  1.000 29.13568 ? 223 GLN   A CB  1 
ATOM   1758 C  CG  . GLN   A 1 227 ? 14.48454 -1.55457  14.28687  1.000 42.23431 ? 223 GLN   A CG  1 
ATOM   1759 C  CD  . GLN   A 1 227 ? 14.40709 -2.17915  12.90215  1.000 46.15406 ? 223 GLN   A CD  1 
ATOM   1760 O  OE1 . GLN   A 1 227 ? 15.39253 -2.70396  12.38656  1.000 53.91385 ? 223 GLN   A OE1 1 
ATOM   1761 N  NE2 . GLN   A 1 227 ? 13.22746 -2.12788  12.29838  1.000 48.45973 ? 223 GLN   A NE2 1 
ATOM   1762 N  N   . GLY   A 1 228 ? 16.86159 -2.00549  18.61831  1.000 22.61850 ? 224 GLY   A N   1 
ATOM   1763 C  CA  . GLY   A 1 228 ? 17.59594 -2.79014  19.58246  1.000 23.75046 ? 224 GLY   A CA  1 
ATOM   1764 C  C   . GLY   A 1 228 ? 19.09867 -2.60578  19.55940  1.000 17.93122 ? 224 GLY   A C   1 
ATOM   1765 O  O   . GLY   A 1 228 ? 19.76303 -2.95027  20.54134  1.000 18.79641 ? 224 GLY   A O   1 
ATOM   1766 N  N   . ALA   A 1 229 ? 19.65486 -2.06985  18.47754  1.000 18.25589 ? 225 ALA   A N   1 
ATOM   1767 C  CA  . ALA   A 1 229 ? 21.09636 -1.91230  18.35350  1.000 17.95776 ? 225 ALA   A CA  1 
ATOM   1768 C  C   . ALA   A 1 229 ? 21.53319 -0.60815  19.00579  1.000 19.25419 ? 225 ALA   A C   1 
ATOM   1769 O  O   . ALA   A 1 229 ? 20.93129 0.44351   18.76931  1.000 18.19957 ? 225 ALA   A O   1 
ATOM   1770 C  CB  . ALA   A 1 229 ? 21.51643 -1.93877  16.88351  1.000 17.90347 ? 225 ALA   A CB  1 
ATOM   1771 N  N   . PHE   A 1 230 ? 22.58313 -0.68077  19.81755  1.000 18.14820 ? 226 PHE   A N   1 
ATOM   1772 C  CA  . PHE   A 1 230 ? 23.07820 0.49018   20.52457  1.000 20.74754 ? 226 PHE   A CA  1 
ATOM   1773 C  C   . PHE   A 1 230 ? 23.97528 1.32512   19.62258  1.000 18.92662 ? 226 PHE   A C   1 
ATOM   1774 O  O   . PHE   A 1 230 ? 24.70415 0.80125   18.77529  1.000 22.75146 ? 226 PHE   A O   1 
ATOM   1775 C  CB  . PHE   A 1 230 ? 23.86424 0.08636   21.77538  1.000 19.70924 ? 226 PHE   A CB  1 
ATOM   1776 C  CG  . PHE   A 1 230 ? 23.03328 -0.57893  22.83892  1.000 21.94876 ? 226 PHE   A CG  1 
ATOM   1777 C  CD1 . PHE   A 1 230 ? 21.64910 -0.53583  22.79400  1.000 19.57444 ? 226 PHE   A CD1 1 
ATOM   1778 C  CD2 . PHE   A 1 230 ? 23.64320 -1.23088  23.89889  1.000 17.02663 ? 226 PHE   A CD2 1 
ATOM   1779 C  CE1 . PHE   A 1 230 ? 20.89063 -1.14093  23.77639  1.000 15.59283 ? 226 PHE   A CE1 1 
ATOM   1780 C  CE2 . PHE   A 1 230 ? 22.89078 -1.83829  24.88577  1.000 16.64185 ? 226 PHE   A CE2 1 
ATOM   1781 C  CZ  . PHE   A 1 230 ? 21.51213 -1.79360  24.82588  1.000 19.10509 ? 226 PHE   A CZ  1 
ATOM   1782 N  N   . ALA   A 1 231 ? 23.92102 2.64361   19.82079  1.000 32.83363 ? 227 ALA   A N   1 
ATOM   1783 C  CA  . ALA   A 1 231 ? 24.85576 3.52989   19.13663  1.000 40.84264 ? 227 ALA   A CA  1 
ATOM   1784 C  C   . ALA   A 1 231 ? 26.27885 3.29631   19.62747  1.000 33.12974 ? 227 ALA   A C   1 
ATOM   1785 O  O   . ALA   A 1 231 ? 27.21641 3.19735   18.82785  1.000 41.98245 ? 227 ALA   A O   1 
ATOM   1786 C  CB  . ALA   A 1 231 ? 24.44428 4.98829   19.34222  1.000 41.42120 ? 227 ALA   A CB  1 
ATOM   1787 N  N   . SER   A 1 232 ? 26.45620 3.20178   20.93963  1.000 28.54253 ? 228 SER   A N   1 
ATOM   1788 C  CA  . SER   A 1 232 ? 27.74743 2.94668   21.55110  1.000 39.12613 ? 228 SER   A CA  1 
ATOM   1789 C  C   . SER   A 1 232 ? 27.62714 1.78817   22.52812  1.000 31.27268 ? 228 SER   A C   1 
ATOM   1790 O  O   . SER   A 1 232 ? 26.58320 1.61280   23.16375  1.000 38.52640 ? 228 SER   A O   1 
ATOM   1791 C  CB  . SER   A 1 232 ? 28.27058 4.19286   22.28075  1.000 36.71326 ? 228 SER   A CB  1 
ATOM   1792 O  OG  . SER   A 1 232 ? 27.24926 4.79264   23.05902  1.000 44.07152 ? 228 SER   A OG  1 
ATOM   1793 N  N   . PRO   A 1 233 ? 28.67191 0.97561   22.65851  1.000 32.29420 ? 229 PRO   A N   1 
ATOM   1794 C  CA  . PRO   A 1 233 ? 28.60203 -0.17111  23.56765  1.000 29.56117 ? 229 PRO   A CA  1 
ATOM   1795 C  C   . PRO   A 1 233 ? 28.60883 0.27656   25.01953  1.000 22.90998 ? 229 PRO   A C   1 
ATOM   1796 O  O   . PRO   A 1 233 ? 29.07327 1.36370   25.36468  1.000 22.35505 ? 229 PRO   A O   1 
ATOM   1797 C  CB  . PRO   A 1 233 ? 29.86461 -0.97744  23.23421  1.000 30.00647 ? 229 PRO   A CB  1 
ATOM   1798 C  CG  . PRO   A 1 233 ? 30.41377 -0.36902  21.96542  1.000 37.46027 ? 229 PRO   A CG  1 
ATOM   1799 C  CD  . PRO   A 1 233 ? 29.96967 1.05270   21.97136  1.000 37.51100 ? 229 PRO   A CD  1 
ATOM   1800 N  N   . ILE   A 1 234 ? 28.06752 -0.58664  25.87415  1.000 25.00505 ? 230 ILE   A N   1 
ATOM   1801 C  CA  . ILE   A 1 234 ? 28.10119 -0.40760  27.32043  1.000 23.45392 ? 230 ILE   A CA  1 
ATOM   1802 C  C   . ILE   A 1 234 ? 29.00495 -1.48655  27.89585  1.000 28.08251 ? 230 ILE   A C   1 
ATOM   1803 O  O   . ILE   A 1 234 ? 28.84899 -2.67072  27.57176  1.000 25.69469 ? 230 ILE   A O   1 
ATOM   1804 C  CB  . ILE   A 1 234 ? 26.69355 -0.47494  27.94334  1.000 21.22263 ? 230 ILE   A CB  1 
ATOM   1805 C  CG1 . ILE   A 1 234 ? 25.93056 0.83464   27.73098  1.000 36.61821 ? 230 ILE   A CG1 1 
ATOM   1806 C  CG2 . ILE   A 1 234 ? 26.77631 -0.78180  29.43137  1.000 33.30482 ? 230 ILE   A CG2 1 
ATOM   1807 C  CD1 . ILE   A 1 234 ? 25.30676 0.97465   26.36821  1.000 41.41023 ? 230 ILE   A CD1 1 
ATOM   1808 N  N   . GLN   A 1 235 ? 29.96225 -1.07886  28.72627  1.000 26.79422 ? 231 GLN   A N   1 
ATOM   1809 C  CA  . GLN   A 1 235 ? 30.82862 -2.03379  29.40112  1.000 24.54310 ? 231 GLN   A CA  1 
ATOM   1810 C  C   . GLN   A 1 235 ? 30.15809 -2.53421  30.67334  1.000 22.98520 ? 231 GLN   A C   1 
ATOM   1811 O  O   . GLN   A 1 235 ? 29.68228 -1.73951  31.48903  1.000 17.42699 ? 231 GLN   A O   1 
ATOM   1812 C  CB  . GLN   A 1 235 ? 32.17669 -1.39930  29.74916  1.000 29.74386 ? 231 GLN   A CB  1 
ATOM   1813 C  CG  . GLN   A 1 235 ? 33.19041 -1.32365  28.62461  1.000 35.55973 ? 231 GLN   A CG  1 
ATOM   1814 C  CD  . GLN   A 1 235 ? 34.57548 -0.97738  29.14680  1.000 47.25034 ? 231 GLN   A CD  1 
ATOM   1815 O  OE1 . GLN   A 1 235 ? 34.72173 -0.51031  30.27777  1.000 47.65660 ? 231 GLN   A OE1 1 
ATOM   1816 N  NE2 . GLN   A 1 235 ? 35.59850 -1.21962  28.33423  1.000 46.49280 ? 231 GLN   A NE2 1 
ATOM   1817 N  N   . LEU   A 1 236 ? 30.11991 -3.84750  30.83632  1.000 13.62963 ? 232 LEU   A N   1 
ATOM   1818 C  CA  . LEU   A 1 236 ? 29.67487 -4.49384  32.06141  1.000 13.93549 ? 232 LEU   A CA  1 
ATOM   1819 C  C   . LEU   A 1 236 ? 30.81821 -5.33705  32.61885  1.000 19.24989 ? 232 LEU   A C   1 
ATOM   1820 O  O   . LEU   A 1 236 ? 31.89902 -5.41958  32.02801  1.000 16.87355 ? 232 LEU   A O   1 
ATOM   1821 C  CB  . LEU   A 1 236 ? 28.42740 -5.34284  31.80897  1.000 13.08000 ? 232 LEU   A CB  1 
ATOM   1822 C  CG  . LEU   A 1 236 ? 27.15618 -4.58576  31.42321  1.000 23.22386 ? 232 LEU   A CG  1 
ATOM   1823 C  CD1 . LEU   A 1 236 ? 26.01613 -5.55517  31.18076  1.000 17.46022 ? 232 LEU   A CD1 1 
ATOM   1824 C  CD2 . LEU   A 1 236 ? 26.78116 -3.58000  32.50016  1.000 22.17703 ? 232 LEU   A CD2 1 
ATOM   1825 N  N   . GLN   A 1 237 ? 30.57592 -5.96178  33.77226  1.000 11.69245 ? 233 GLN   A N   1 
ATOM   1826 C  CA  . GLN   A 1 237 ? 31.57926 -6.76287  34.46125  1.000 12.22511 ? 233 GLN   A CA  1 
ATOM   1827 C  C   . GLN   A 1 237 ? 31.12455 -8.20984  34.58518  1.000 13.63932 ? 233 GLN   A C   1 
ATOM   1828 O  O   . GLN   A 1 237 ? 29.94353 -8.48167  34.82363  1.000 11.05754 ? 233 GLN   A O   1 
ATOM   1829 C  CB  . GLN   A 1 237 ? 31.87276 -6.21424  35.86215  1.000 16.32817 ? 233 GLN   A CB  1 
ATOM   1830 C  CG  . GLN   A 1 237 ? 33.10165 -5.34395  35.93621  1.000 21.38646 ? 233 GLN   A CG  1 
ATOM   1831 C  CD  . GLN   A 1 237 ? 33.44777 -4.94516  37.35136  1.000 17.66011 ? 233 GLN   A CD  1 
ATOM   1832 O  OE1 . GLN   A 1 237 ? 32.60045 -4.45538  38.09685  1.000 27.17735 ? 233 GLN   A OE1 1 
ATOM   1833 N  NE2 . GLN   A 1 237 ? 34.69883 -5.16134  37.73363  1.000 26.08141 ? 233 GLN   A NE2 1 
ATOM   1834 N  N   . ARG   A 1 238 ? 32.07279 -9.13294  34.42648  1.000 13.81372 ? 234 ARG   A N   1 
ATOM   1835 C  CA  . ARG   A 1 238 ? 31.85334 -10.53899 34.73263  1.000 12.52016 ? 234 ARG   A CA  1 
ATOM   1836 C  C   . ARG   A 1 238 ? 31.97436 -10.76221 36.24005  1.000 15.98279 ? 234 ARG   A C   1 
ATOM   1837 O  O   . ARG   A 1 238 ? 32.31043 -9.85043  36.99956  1.000 18.18161 ? 234 ARG   A O   1 
ATOM   1838 C  CB  . ARG   A 1 238 ? 32.84667 -11.40814 33.96577  1.000 14.57452 ? 234 ARG   A CB  1 
ATOM   1839 C  CG  . ARG   A 1 238 ? 32.80501 -11.21029 32.45904  1.000 19.12801 ? 234 ARG   A CG  1 
ATOM   1840 C  CD  . ARG   A 1 238 ? 33.52549 -12.33804 31.72677  1.000 16.51637 ? 234 ARG   A CD  1 
ATOM   1841 N  NE  . ARG   A 1 238 ? 33.40369 -12.19847 30.28071  1.000 21.04889 ? 234 ARG   A NE  1 
ATOM   1842 C  CZ  . ARG   A 1 238 ? 32.34024 -12.57267 29.58311  1.000 25.81286 ? 234 ARG   A CZ  1 
ATOM   1843 N  NH1 . ARG   A 1 238 ? 31.30019 -13.14889 30.16479  1.000 19.12149 ? 234 ARG   A NH1 1 
ATOM   1844 N  NH2 . ARG   A 1 238 ? 32.31628 -12.35927 28.26891  1.000 27.27596 ? 234 ARG   A NH2 1 
ATOM   1845 N  N   . ARG   A 1 239 ? 31.70059 -11.99452 36.68954  1.000 13.78011 ? 235 ARG   A N   1 
ATOM   1846 C  CA  . ARG   A 1 239 ? 31.83932 -12.29752 38.11358  1.000 16.60817 ? 235 ARG   A CA  1 
ATOM   1847 C  C   . ARG   A 1 239 ? 33.28382 -12.17461 38.58104  1.000 20.20982 ? 235 ARG   A C   1 
ATOM   1848 O  O   . ARG   A 1 239 ? 33.52834 -11.82912 39.74371  1.000 16.56472 ? 235 ARG   A O   1 
ATOM   1849 C  CB  . ARG   A 1 239 ? 31.31259 -13.70057 38.42444  1.000 16.43246 ? 235 ARG   A CB  1 
ATOM   1850 C  CG  . ARG   A 1 239 ? 29.81456 -13.88603 38.20958  1.000 21.43735 ? 235 ARG   A CG  1 
ATOM   1851 C  CD  . ARG   A 1 239 ? 29.36454 -15.25655 38.70690  1.000 19.92853 ? 235 ARG   A CD  1 
ATOM   1852 N  NE  . ARG   A 1 239 ? 27.98747 -15.55979 38.33606  1.000 26.24573 ? 235 ARG   A NE  1 
ATOM   1853 C  CZ  . ARG   A 1 239 ? 26.92566 -15.25267 39.06827  1.000 34.79341 ? 235 ARG   A CZ  1 
ATOM   1854 N  NH1 . ARG   A 1 239 ? 27.04273 -14.61791 40.22376  1.000 37.15329 ? 235 ARG   A NH1 1 
ATOM   1855 N  NH2 . ARG   A 1 239 ? 25.71567 -15.59097 38.63018  1.000 32.49725 ? 235 ARG   A NH2 1 
ATOM   1856 N  N   . ASN   A 1 240 ? 34.25205 -12.45096 37.70680  1.000 17.60718 ? 236 ASN   A N   1 
ATOM   1857 C  CA  . ASN   A 1 240 ? 35.66034 -12.33459 38.06633  1.000 19.92239 ? 236 ASN   A CA  1 
ATOM   1858 C  C   . ASN   A 1 240 ? 36.20804 -10.92542 37.86713  1.000 14.78319 ? 236 ASN   A C   1 
ATOM   1859 O  O   . ASN   A 1 240 ? 37.42349 -10.73074 37.94783  1.000 19.05736 ? 236 ASN   A O   1 
ATOM   1860 C  CB  . ASN   A 1 240 ? 36.51055 -13.34797 37.27863  1.000 18.86992 ? 236 ASN   A CB  1 
ATOM   1861 C  CG  . ASN   A 1 240 ? 36.56458 -13.05934 35.77644  1.000 28.99548 ? 236 ASN   A CG  1 
ATOM   1862 O  OD1 . ASN   A 1 240 ? 36.15319 -11.99734 35.30630  1.000 26.81703 ? 236 ASN   A OD1 1 
ATOM   1863 N  ND2 . ASN   A 1 240 ? 37.08570 -14.01905 35.01756  1.000 15.40276 ? 236 ASN   A ND2 1 
ATOM   1864 N  N   . GLY   A 1 241 ? 35.34840 -9.95150  37.57987  1.000 19.33360 ? 237 GLY   A N   1 
ATOM   1865 C  CA  . GLY   A 1 241 ? 35.76002 -8.56964  37.47166  1.000 22.80438 ? 237 GLY   A CA  1 
ATOM   1866 C  C   . GLY   A 1 241 ? 36.20105 -8.12025  36.09497  1.000 28.88396 ? 237 GLY   A C   1 
ATOM   1867 O  O   . GLY   A 1 241 ? 36.41659 -6.91713  35.89705  1.000 23.40192 ? 237 GLY   A O   1 
ATOM   1868 N  N   . SER   A 1 242 ? 36.34981 -9.03396  35.13994  1.000 17.33075 ? 238 SER   A N   1 
ATOM   1869 C  CA  . SER   A 1 242 ? 36.76250 -8.63218  33.80517  1.000 22.84305 ? 238 SER   A CA  1 
ATOM   1870 C  C   . SER   A 1 242 ? 35.61785 -7.92219  33.08555  1.000 19.46344 ? 238 SER   A C   1 
ATOM   1871 O  O   . SER   A 1 242 ? 34.43789 -8.09355  33.40759  1.000 25.43631 ? 238 SER   A O   1 
ATOM   1872 C  CB  . SER   A 1 242 ? 37.23394 -9.84359  32.99769  1.000 16.92965 ? 238 SER   A CB  1 
ATOM   1873 O  OG  . SER   A 1 242 ? 36.21260 -10.81766 32.91022  1.000 22.27661 ? 238 SER   A OG  1 
ATOM   1874 N  N   . LYS   A 1 243 ? 35.98308 -7.11156  32.09998  1.000 24.57949 ? 239 LYS   A N   1 
ATOM   1875 C  CA  . LYS   A 1 243 ? 35.03649 -6.28140  31.37143  1.000 21.72837 ? 239 LYS   A CA  1 
ATOM   1876 C  C   . LYS   A 1 243 ? 34.66162 -6.91981  30.03860  1.000 23.30867 ? 239 LYS   A C   1 
ATOM   1877 O  O   . LYS   A 1 243 ? 35.47171 -7.59731  29.40137  1.000 21.42904 ? 239 LYS   A O   1 
ATOM   1878 C  CB  . LYS   A 1 243 ? 35.61958 -4.88528  31.12953  1.000 25.14467 ? 239 LYS   A CB  1 
ATOM   1879 C  CG  . LYS   A 1 243 ? 35.04135 -3.79494  32.02118  1.000 37.05880 ? 239 LYS   A CG  1 
ATOM   1880 C  CD  . LYS   A 1 243 ? 35.24400 -4.09660  33.49396  1.000 28.45427 ? 239 LYS   A CD  1 
ATOM   1881 C  CE  . LYS   A 1 243 ? 36.70019 -3.98137  33.89113  1.000 47.83545 ? 239 LYS   A CE  1 
ATOM   1882 N  NZ  . LYS   A 1 243 ? 36.93913 -4.27720  35.33461  1.000 33.12303 ? 239 LYS   A NZ  1 
ATOM   1883 N  N   . PHE   A 1 244 ? 33.41536 -6.69772  29.62550  1.000 17.49239 ? 240 PHE   A N   1 
ATOM   1884 C  CA  . PHE   A 1 244 ? 32.97424 -7.05451  28.28374  1.000 22.91598 ? 240 PHE   A CA  1 
ATOM   1885 C  C   . PHE   A 1 244 ? 31.96196 -6.02026  27.81013  1.000 17.15471 ? 240 PHE   A C   1 
ATOM   1886 O  O   . PHE   A 1 244 ? 31.34290 -5.31600  28.61030  1.000 17.12856 ? 240 PHE   A O   1 
ATOM   1887 C  CB  . PHE   A 1 244 ? 32.37958 -8.46965  28.22771  1.000 15.65496 ? 240 PHE   A CB  1 
ATOM   1888 C  CG  . PHE   A 1 244 ? 31.05154 -8.60394  28.91250  1.000 14.19447 ? 240 PHE   A CG  1 
ATOM   1889 C  CD1 . PHE   A 1 244 ? 30.97329 -8.68592  30.29313  1.000 18.76788 ? 240 PHE   A CD1 1 
ATOM   1890 C  CD2 . PHE   A 1 244 ? 29.88184 -8.65993  28.17427  1.000 15.15173 ? 240 PHE   A CD2 1 
ATOM   1891 C  CE1 . PHE   A 1 244 ? 29.75054 -8.81391  30.92483  1.000 24.33536 ? 240 PHE   A CE1 1 
ATOM   1892 C  CE2 . PHE   A 1 244 ? 28.65464 -8.78526  28.79924  1.000 20.18993 ? 240 PHE   A CE2 1 
ATOM   1893 C  CZ  . PHE   A 1 244 ? 28.58888 -8.86204  30.17647  1.000 21.64693 ? 240 PHE   A CZ  1 
ATOM   1894 N  N   . SER   A 1 245 ? 31.80289 -5.93544  26.49294  1.000 20.68396 ? 241 SER   A N   1 
ATOM   1895 C  CA  . SER   A 1 245 ? 30.96231 -4.92207  25.87234  1.000 23.35385 ? 241 SER   A CA  1 
ATOM   1896 C  C   . SER   A 1 245 ? 29.63654 -5.51760  25.41528  1.000 19.82817 ? 241 SER   A C   1 
ATOM   1897 O  O   . SER   A 1 245 ? 29.59161 -6.62813  24.87839  1.000 18.31304 ? 241 SER   A O   1 
ATOM   1898 C  CB  . SER   A 1 245 ? 31.67884 -4.27695  24.68374  1.000 33.77577 ? 241 SER   A CB  1 
ATOM   1899 O  OG  . SER   A 1 245 ? 32.77209 -3.48498  25.11202  1.000 36.30715 ? 241 SER   A OG  1 
ATOM   1900 N  N   . VAL   A 1 246 ? 28.56087 -4.76519  25.63314  1.000 16.11836 ? 242 VAL   A N   1 
ATOM   1901 C  CA  . VAL   A 1 246 ? 27.21956 -5.11308  25.17694  1.000 21.80456 ? 242 VAL   A CA  1 
ATOM   1902 C  C   . VAL   A 1 246 ? 26.84140 -4.15048  24.06061  1.000 16.56873 ? 242 VAL   A C   1 
ATOM   1903 O  O   . VAL   A 1 246 ? 26.94001 -2.92924  24.23162  1.000 14.29391 ? 242 VAL   A O   1 
ATOM   1904 C  CB  . VAL   A 1 246 ? 26.19783 -5.04794  26.32483  1.000 18.52801 ? 242 VAL   A CB  1 
ATOM   1905 C  CG1 . VAL   A 1 246 ? 24.78655 -5.28608  25.79213  1.000 19.49271 ? 242 VAL   A CG1 1 
ATOM   1906 C  CG2 . VAL   A 1 246 ? 26.54912 -6.05626  27.40966  1.000 30.85424 ? 242 VAL   A CG2 1 
ATOM   1907 N  N   . TYR   A 1 247 ? 26.40537 -4.69684  22.91887  1.000 15.44244 ? 243 TYR   A N   1 
ATOM   1908 C  CA  . TYR   A 1 247 ? 26.17770 -3.90138  21.71836  1.000 17.99676 ? 243 TYR   A CA  1 
ATOM   1909 C  C   . TYR   A 1 247 ? 24.71504 -3.77573  21.31414  1.000 24.14682 ? 243 TYR   A C   1 
ATOM   1910 O  O   . TYR   A 1 247 ? 24.40590 -2.95889  20.43794  1.000 19.09038 ? 243 TYR   A O   1 
ATOM   1911 C  CB  . TYR   A 1 247 ? 26.96521 -4.48292  20.53369  1.000 22.02370 ? 243 TYR   A CB  1 
ATOM   1912 C  CG  . TYR   A 1 247 ? 28.45933 -4.48657  20.74879  1.000 22.94205 ? 243 TYR   A CG  1 
ATOM   1913 C  CD1 . TYR   A 1 247 ? 29.06981 -5.48271  21.49862  1.000 26.09587 ? 243 TYR   A CD1 1 
ATOM   1914 C  CD2 . TYR   A 1 247 ? 29.25777 -3.49327  20.20508  1.000 28.46553 ? 243 TYR   A CD2 1 
ATOM   1915 C  CE1 . TYR   A 1 247 ? 30.43408 -5.48646  21.70327  1.000 35.33431 ? 243 TYR   A CE1 1 
ATOM   1916 C  CE2 . TYR   A 1 247 ? 30.62269 -3.49337  20.39936  1.000 37.36783 ? 243 TYR   A CE2 1 
ATOM   1917 C  CZ  . TYR   A 1 247 ? 31.20441 -4.48767  21.14968  1.000 29.54684 ? 243 TYR   A CZ  1 
ATOM   1918 O  OH  . TYR   A 1 247 ? 32.56550 -4.47745  21.33834  1.000 45.69076 ? 243 TYR   A OH  1 
ATOM   1919 N  N   . ASP   A 1 248 ? 23.81475 -4.56230  21.89757  1.000 17.24412 ? 244 ASP   A N   1 
ATOM   1920 C  CA  . ASP   A 1 248 ? 22.39697 -4.42782  21.58877  1.000 13.90956 ? 244 ASP   A CA  1 
ATOM   1921 C  C   . ASP   A 1 248 ? 21.58687 -5.04097  22.72297  1.000 11.60290 ? 244 ASP   A C   1 
ATOM   1922 O  O   . ASP   A 1 248 ? 22.13457 -5.62068  23.66161  1.000 17.82832 ? 244 ASP   A O   1 
ATOM   1923 C  CB  . ASP   A 1 248 ? 22.04707 -5.05680  20.23142  1.000 19.61660 ? 244 ASP   A CB  1 
ATOM   1924 C  CG  . ASP   A 1 248 ? 22.49374 -6.49769  20.11529  1.000 17.59526 ? 244 ASP   A CG  1 
ATOM   1925 O  OD1 . ASP   A 1 248 ? 21.83235 -7.37978  20.70462  1.000 18.89577 ? 244 ASP   A OD1 1 
ATOM   1926 O  OD2 . ASP   A 1 248 ? 23.50051 -6.74659  19.41797  1.000 22.71167 ? 244 ASP   A OD2 1 
ATOM   1927 N  N   . VAL   A 1 249 ? 20.26265 -4.89450  22.62245  1.000 13.97160 ? 245 VAL   A N   1 
ATOM   1928 C  CA  . VAL   A 1 249 ? 19.37175 -5.19555  23.73818  1.000 14.92242 ? 245 VAL   A CA  1 
ATOM   1929 C  C   . VAL   A 1 249 ? 19.21135 -6.69393  24.00287  1.000 19.68029 ? 245 VAL   A C   1 
ATOM   1930 O  O   . VAL   A 1 249 ? 18.85732 -7.08102  25.12314  1.000 12.40893 ? 245 VAL   A O   1 
ATOM   1931 C  CB  . VAL   A 1 249 ? 17.99858 -4.54037  23.48028  1.000 14.95576 ? 245 VAL   A CB  1 
ATOM   1932 C  CG1 . VAL   A 1 249 ? 17.30147 -5.19866  22.30166  1.000 16.89593 ? 245 VAL   A CG1 1 
ATOM   1933 C  CG2 . VAL   A 1 249 ? 17.11871 -4.58466  24.72134  1.000 17.94032 ? 245 VAL   A CG2 1 
ATOM   1934 N  N   . SER   A 1 250 ? 19.48330 -7.55296  23.01677  1.000 15.57267 ? 246 SER   A N   1 
ATOM   1935 C  CA  . SER   A 1 250 ? 19.03041 -8.94168  23.09124  1.000 15.10447 ? 246 SER   A CA  1 
ATOM   1936 C  C   . SER   A 1 250 ? 19.59990 -9.66587  24.30769  1.000 16.22279 ? 246 SER   A C   1 
ATOM   1937 O  O   . SER   A 1 250 ? 18.86498 -10.33812 25.03956  1.000 18.54844 ? 246 SER   A O   1 
ATOM   1938 C  CB  . SER   A 1 250 ? 19.39670 -9.67925  21.80478  1.000 16.29030 ? 246 SER   A CB  1 
ATOM   1939 O  OG  . SER   A 1 250 ? 18.75083 -9.07892  20.69680  1.000 20.43280 ? 246 SER   A OG  1 
ATOM   1940 N  N   . ILE   A 1 251 ? 20.90854 -9.53644  24.54245  1.000 13.56084 ? 247 ILE   A N   1 
ATOM   1941 C  CA  . ILE   A 1 251 ? 21.56237 -10.22473 25.65395  1.000 18.81821 ? 247 ILE   A CA  1 
ATOM   1942 C  C   . ILE   A 1 251 ? 21.00910 -9.80613  27.01046  1.000 19.77484 ? 247 ILE   A C   1 
ATOM   1943 O  O   . ILE   A 1 251 ? 21.20522 -10.51607 28.00631  1.000 17.89773 ? 247 ILE   A O   1 
ATOM   1944 C  CB  . ILE   A 1 251 ? 23.08695 -9.97646  25.58538  1.000 29.36137 ? 247 ILE   A CB  1 
ATOM   1945 C  CG1 . ILE   A 1 251 ? 23.86085 -11.09339 26.27598  1.000 27.17594 ? 247 ILE   A CG1 1 
ATOM   1946 C  CG2 . ILE   A 1 251 ? 23.44751 -8.65064  26.22661  1.000 26.22395 ? 247 ILE   A CG2 1 
ATOM   1947 C  CD1 . ILE   A 1 251 ? 25.36072 -10.93410 26.15006  1.000 29.43511 ? 247 ILE   A CD1 1 
ATOM   1948 N  N   . LEU   A 1 252 ? 20.31448 -8.67241  27.07932  1.000 14.12132 ? 248 LEU   A N   1 
ATOM   1949 C  CA  . LEU   A 1 252 ? 19.87468 -8.09526  28.34885  1.000 12.76881 ? 248 LEU   A CA  1 
ATOM   1950 C  C   . LEU   A 1 252 ? 18.45070 -8.47267  28.72848  1.000 12.27434 ? 248 LEU   A C   1 
ATOM   1951 O  O   . LEU   A 1 252 ? 18.06252 -8.26277  29.87937  1.000 19.03961 ? 248 LEU   A O   1 
ATOM   1952 C  CB  . LEU   A 1 252 ? 19.98713 -6.56717  28.29379  1.000 9.97892  ? 248 LEU   A CB  1 
ATOM   1953 C  CG  . LEU   A 1 252 ? 21.39480 -6.00352  28.11043  1.000 17.44889 ? 248 LEU   A CG  1 
ATOM   1954 C  CD1 . LEU   A 1 252 ? 21.33347 -4.53419  27.72443  1.000 15.68664 ? 248 LEU   A CD1 1 
ATOM   1955 C  CD2 . LEU   A 1 252 ? 22.20223 -6.19949  29.38337  1.000 20.92967 ? 248 LEU   A CD2 1 
ATOM   1956 N  N   . ILE   A 1 253 ? 17.67240 -9.01714  27.79932  1.000 17.17854 ? 249 ILE   A N   1 
ATOM   1957 C  CA  . ILE   A 1 253 ? 16.26191 -9.32185  28.04085  1.000 16.01526 ? 249 ILE   A CA  1 
ATOM   1958 C  C   . ILE   A 1 253 ? 16.07404 -10.23391 29.25310  1.000 25.38209 ? 249 ILE   A C   1 
ATOM   1959 O  O   . ILE   A 1 253 ? 15.17639 -9.97390  30.06526  1.000 21.90917 ? 249 ILE   A O   1 
ATOM   1960 C  CB  . ILE   A 1 253 ? 15.60384 -9.90957  26.78366  1.000 17.82525 ? 249 ILE   A CB  1 
ATOM   1961 C  CG1 . ILE   A 1 253 ? 15.59697 -8.85930  25.66710  1.000 22.61572 ? 249 ILE   A CG1 1 
ATOM   1962 C  CG2 . ILE   A 1 253 ? 14.18530 -10.37676 27.07855  1.000 18.21109 ? 249 ILE   A CG2 1 
ATOM   1963 C  CD1 . ILE   A 1 253 ? 14.86120 -9.27976  24.41284  1.000 33.12120 ? 249 ILE   A CD1 1 
ATOM   1964 N  N   . PRO   A 1 254 ? 16.86848 -11.29225 29.44626  1.000 16.32879 ? 250 PRO   A N   1 
ATOM   1965 C  CA  . PRO   A 1 254 ? 16.70748 -12.09993 30.66282  1.000 16.72903 ? 250 PRO   A CA  1 
ATOM   1966 C  C   . PRO   A 1 254 ? 17.31077 -11.47138 31.90925  1.000 16.58550 ? 250 PRO   A C   1 
ATOM   1967 O  O   . PRO   A 1 254 ? 17.14819 -12.03367 32.99599  1.000 15.75619 ? 250 PRO   A O   1 
ATOM   1968 C  CB  . PRO   A 1 254 ? 17.43485 -13.41363 30.31494  1.000 18.05050 ? 250 PRO   A CB  1 
ATOM   1969 C  CG  . PRO   A 1 254 ? 17.76815 -13.33326 28.86523  1.000 23.84389 ? 250 PRO   A CG  1 
ATOM   1970 C  CD  . PRO   A 1 254 ? 17.88005 -11.88898 28.55456  1.000 21.37428 ? 250 PRO   A CD  1 
ATOM   1971 N  N   . ILE   A 1 255 ? 17.97906 -10.32898 31.78498  1.000 15.28258 ? 251 ILE   A N   1 
ATOM   1972 C  CA  . ILE   A 1 255 ? 18.80080 -9.76609  32.85263  1.000 12.07981 ? 251 ILE   A CA  1 
ATOM   1973 C  C   . ILE   A 1 255 ? 18.11964 -8.58555  33.52947  1.000 13.35514 ? 251 ILE   A C   1 
ATOM   1974 O  O   . ILE   A 1 255 ? 18.12260 -8.47758  34.75555  1.000 10.83046 ? 251 ILE   A O   1 
ATOM   1975 C  CB  . ILE   A 1 255 ? 20.18536 -9.36089  32.29736  1.000 12.92821 ? 251 ILE   A CB  1 
ATOM   1976 C  CG1 . ILE   A 1 255 ? 20.90271 -10.57641 31.71307  1.000 19.49304 ? 251 ILE   A CG1 1 
ATOM   1977 C  CG2 . ILE   A 1 255 ? 21.02492 -8.67403  33.38486  1.000 16.21379 ? 251 ILE   A CG2 1 
ATOM   1978 C  CD1 . ILE   A 1 255 ? 21.09860 -11.70545 32.69992  1.000 22.99379 ? 251 ILE   A CD1 1 
ATOM   1979 N  N   . ILE   A 1 256 ? 17.55116 -7.67358  32.74650  1.000 11.16359 ? 252 ILE   A N   1 
ATOM   1980 C  CA  . ILE   A 1 256 ? 16.89349 -6.48867  33.28214  1.000 15.82388 ? 252 ILE   A CA  1 
ATOM   1981 C  C   . ILE   A 1 256 ? 15.38448 -6.67209  33.18019  1.000 15.63258 ? 252 ILE   A C   1 
ATOM   1982 O  O   . ILE   A 1 256 ? 14.86908 -7.17819  32.17348  1.000 17.18925 ? 252 ILE   A O   1 
ATOM   1983 C  CB  . ILE   A 1 256 ? 17.37110 -5.21605  32.55489  1.000 12.33885 ? 252 ILE   A CB  1 
ATOM   1984 C  CG1 . ILE   A 1 256 ? 16.72714 -3.97198  33.16845  1.000 13.87798 ? 252 ILE   A CG1 1 
ATOM   1985 C  CG2 . ILE   A 1 256 ? 17.10912 -5.30759  31.05842  1.000 18.41079 ? 252 ILE   A CG2 1 
ATOM   1986 C  CD1 . ILE   A 1 256 ? 17.38551 -2.66399  32.75495  1.000 18.16775 ? 252 ILE   A CD1 1 
ATOM   1987 N  N   . ALA   A 1 257 ? 14.67335 -6.29106  34.24408  1.000 15.29176 ? 253 ALA   A N   1 
ATOM   1988 C  CA  . ALA   A 1 257 ? 13.23832 -6.51359  34.34502  1.000 11.18218 ? 253 ALA   A CA  1 
ATOM   1989 C  C   . ALA   A 1 257 ? 12.41166 -5.23668  34.34783  1.000 14.09984 ? 253 ALA   A C   1 
ATOM   1990 O  O   . ALA   A 1 257 ? 11.21216 -5.30153  34.06549  1.000 17.53252 ? 253 ALA   A O   1 
ATOM   1991 C  CB  . ALA   A 1 257 ? 12.91215 -7.30776  35.61980  1.000 16.44851 ? 253 ALA   A CB  1 
ATOM   1992 N  N   . LEU   A 1 258 ? 13.01067 -4.09423  34.67726  1.000 10.24032 ? 254 LEU   A N   1 
ATOM   1993 C  CA  . LEU   A 1 258 ? 12.31895 -2.81437  34.72481  1.000 16.64645 ? 254 LEU   A CA  1 
ATOM   1994 C  C   . LEU   A 1 258 ? 13.25137 -1.74228  34.18524  1.000 12.39719 ? 254 LEU   A C   1 
ATOM   1995 O  O   . LEU   A 1 258 ? 14.47094 -1.83686  34.33534  1.000 14.21461 ? 254 LEU   A O   1 
ATOM   1996 C  CB  . LEU   A 1 258 ? 11.89184 -2.43999  36.15668  1.000 16.42126 ? 254 LEU   A CB  1 
ATOM   1997 C  CG  . LEU   A 1 258 ? 10.99442 -3.37463  36.96653  1.000 16.04525 ? 254 LEU   A CG  1 
ATOM   1998 C  CD1 . LEU   A 1 258 ? 10.88164 -2.86497  38.39828  1.000 18.15263 ? 254 LEU   A CD1 1 
ATOM   1999 C  CD2 . LEU   A 1 258 ? 9.61711  -3.49631  36.34220  1.000 23.33357 ? 254 LEU   A CD2 1 
ATOM   2000 N  N   . MET   A 1 259 ? 12.67300 -0.72044  33.55553  1.000 12.23784 ? 255 MET   A N   1 
ATOM   2001 C  CA  . MET   A 1 259 ? 13.43733 0.42006   33.07164  1.000 10.91249 ? 255 MET   A CA  1 
ATOM   2002 C  C   . MET   A 1 259 ? 12.75266 1.71737   33.46339  1.000 11.25663 ? 255 MET   A C   1 
ATOM   2003 O  O   . MET   A 1 259 ? 11.52424 1.82418   33.40534  1.000 11.92798 ? 255 MET   A O   1 
ATOM   2004 C  CB  . MET   A 1 259 ? 13.60415 0.39463   31.54635  1.000 11.98257 ? 255 MET   A CB  1 
ATOM   2005 C  CG  . MET   A 1 259 ? 14.50407 -0.70599  31.02744  1.000 11.72520 ? 255 MET   A CG  1 
ATOM   2006 S  SD  . MET   A 1 259 ? 14.74136 -0.53246  29.24984  1.000 18.23150 ? 255 MET   A SD  1 
ATOM   2007 C  CE  . MET   A 1 259 ? 13.04239 -0.47061  28.68960  1.000 22.26993 ? 255 MET   A CE  1 
ATOM   2008 N  N   . VAL   A 1 260 ? 13.55723 2.70664   33.85035  1.000 11.00923 ? 256 VAL   A N   1 
ATOM   2009 C  CA  . VAL   A 1 260 ? 13.03117 4.04619   34.07108  1.000 11.62001 ? 256 VAL   A CA  1 
ATOM   2010 C  C   . VAL   A 1 260 ? 12.64126 4.65190   32.72764  1.000 13.42983 ? 256 VAL   A C   1 
ATOM   2011 O  O   . VAL   A 1 260 ? 13.31201 4.43858   31.70934  1.000 14.84854 ? 256 VAL   A O   1 
ATOM   2012 C  CB  . VAL   A 1 260 ? 14.06064 4.91183   34.82184  1.000 11.28985 ? 256 VAL   A CB  1 
ATOM   2013 C  CG1 . VAL   A 1 260 ? 15.40163 4.94631   34.08844  1.000 11.34844 ? 256 VAL   A CG1 1 
ATOM   2014 C  CG2 . VAL   A 1 260 ? 13.53162 6.31988   35.04115  1.000 13.21695 ? 256 VAL   A CG2 1 
ATOM   2015 N  N   . TYR   A 1 261 ? 11.53004 5.38470   32.71324  1.000 13.67182 ? 257 TYR   A N   1 
ATOM   2016 C  CA  . TYR   A 1 261 ? 11.02905 5.99721   31.48618  1.000 15.01989 ? 257 TYR   A CA  1 
ATOM   2017 C  C   . TYR   A 1 261 ? 12.00323 7.04992   30.96561  1.000 15.44686 ? 257 TYR   A C   1 
ATOM   2018 O  O   . TYR   A 1 261 ? 12.31315 8.01894   31.66208  1.000 17.59615 ? 257 TYR   A O   1 
ATOM   2019 C  CB  . TYR   A 1 261 ? 9.65984  6.61617   31.76026  1.000 16.06828 ? 257 TYR   A CB  1 
ATOM   2020 C  CG  . TYR   A 1 261 ? 8.93795  7.19182   30.56163  1.000 17.73712 ? 257 TYR   A CG  1 
ATOM   2021 C  CD1 . TYR   A 1 261 ? 9.19934  8.48443   30.12163  1.000 18.72524 ? 257 TYR   A CD1 1 
ATOM   2022 C  CD2 . TYR   A 1 261 ? 7.96077  6.45963   29.89800  1.000 18.56072 ? 257 TYR   A CD2 1 
ATOM   2023 C  CE1 . TYR   A 1 261 ? 8.53171  9.02013   29.03907  1.000 20.45617 ? 257 TYR   A CE1 1 
ATOM   2024 C  CE2 . TYR   A 1 261 ? 7.28405  6.99025   28.81163  1.000 20.31953 ? 257 TYR   A CE2 1 
ATOM   2025 C  CZ  . TYR   A 1 261 ? 7.57536  8.27163   28.39006  1.000 22.08080 ? 257 TYR   A CZ  1 
ATOM   2026 O  OH  . TYR   A 1 261 ? 6.90832  8.81078   27.31703  1.000 24.34004 ? 257 TYR   A OH  1 
ATOM   2027 N  N   . ARG   A 1 262 ? 12.46730 6.87440   29.72670  1.000 16.01709 ? 258 ARG   A N   1 
ATOM   2028 C  CA  . ARG   A 1 262 ? 13.34965 7.84388   29.09097  1.000 21.53514 ? 258 ARG   A CA  1 
ATOM   2029 C  C   . ARG   A 1 262 ? 12.70153 8.60134   27.94477  1.000 21.97728 ? 258 ARG   A C   1 
ATOM   2030 O  O   . ARG   A 1 262 ? 13.05111 9.76097   27.71412  1.000 23.72626 ? 258 ARG   A O   1 
ATOM   2031 C  CB  . ARG   A 1 262 ? 14.61717 7.15717   28.56722  1.000 16.30822 ? 258 ARG   A CB  1 
ATOM   2032 C  CG  . ARG   A 1 262 ? 15.50176 6.56715   29.64771  1.000 14.83337 ? 258 ARG   A CG  1 
ATOM   2033 C  CD  . ARG   A 1 262 ? 15.82777 7.59012   30.72714  1.000 18.88959 ? 258 ARG   A CD  1 
ATOM   2034 N  NE  . ARG   A 1 262 ? 17.07877 7.26507   31.39936  1.000 23.58668 ? 258 ARG   A NE  1 
ATOM   2035 C  CZ  . ARG   A 1 262 ? 17.39110 7.63892   32.63204  1.000 22.57781 ? 258 ARG   A CZ  1 
ATOM   2036 N  NH1 . ARG   A 1 262 ? 16.55488 8.34863   33.37214  1.000 18.06998 ? 258 ARG   A NH1 1 
ATOM   2037 N  NH2 . ARG   A 1 262 ? 18.56609 7.27760   33.14003  1.000 23.25606 ? 258 ARG   A NH2 1 
ATOM   2038 N  N   . CYS   A 1 263 ? 11.77317 7.97999   27.22537  1.000 21.56738 ? 259 CYS   A N   1 
ATOM   2039 C  CA  . CYS   A 1 263 ? 11.10504 8.62312   26.10167  1.000 21.14881 ? 259 CYS   A CA  1 
ATOM   2040 C  C   . CYS   A 1 263 ? 9.83520  7.84147   25.78875  1.000 28.24971 ? 259 CYS   A C   1 
ATOM   2041 O  O   . CYS   A 1 263 ? 9.56638  6.78890   26.37575  1.000 25.19113 ? 259 CYS   A O   1 
ATOM   2042 C  CB  . CYS   A 1 263 ? 12.02684 8.69996   24.88190  1.000 30.36867 ? 259 CYS   A CB  1 
ATOM   2043 S  SG  . CYS   A 1 263 ? 12.56954 7.07917   24.28428  1.000 28.30054 ? 259 CYS   A SG  1 
ATOM   2044 N  N   . ALA   A 1 264 ? 9.05784  8.36653   24.84811  1.000 29.02238 ? 260 ALA   A N   1 
ATOM   2045 C  CA  . ALA   A 1 264 ? 7.82930  7.71178   24.43952  1.000 31.18062 ? 260 ALA   A CA  1 
ATOM   2046 C  C   . ALA   A 1 264 ? 8.13999  6.41768   23.68728  1.000 25.22189 ? 260 ALA   A C   1 
ATOM   2047 O  O   . ALA   A 1 264 ? 9.19832  6.28873   23.06451  1.000 27.86964 ? 260 ALA   A O   1 
ATOM   2048 C  CB  . ALA   A 1 264 ? 7.00058  8.64295   23.55666  1.000 37.42138 ? 260 ALA   A CB  1 
ATOM   2049 N  N   . PRO   A 1 265 ? 7.22968  5.43337   23.73262  1.000 29.77241 ? 261 PRO   A N   1 
ATOM   2050 C  CA  . PRO   A 1 265 ? 7.42199  4.19549   22.96812  1.000 34.22640 ? 261 PRO   A CA  1 
ATOM   2051 C  C   . PRO   A 1 265 ? 7.25448  4.40916   21.46548  1.000 41.17890 ? 261 PRO   A C   1 
ATOM   2052 O  O   . PRO   A 1 265 ? 8.09253  3.94164   20.69342  1.000 46.07518 ? 261 PRO   A O   1 
ATOM   2053 C  CB  . PRO   A 1 265 ? 6.32633  3.27718   23.51177  1.000 27.99216 ? 261 PRO   A CB  1 
ATOM   2054 C  CG  . PRO   A 1 265 ? 5.25552  4.21241   23.95918  1.000 43.60890 ? 261 PRO   A CG  1 
ATOM   2055 C  CD  . PRO   A 1 265 ? 5.97826  5.41213   24.51008  1.000 33.16498 ? 261 PRO   A CD  1 
ATOM   2056 N  N   . LYS   B 1 8   ? 0.97956  -39.58484 10.23042  1.000 31.03383 ? 4   LYS   B N   1 
ATOM   2057 C  CA  . LYS   B 1 8   ? 0.77947  -38.79230 11.43461  1.000 32.46023 ? 4   LYS   B CA  1 
ATOM   2058 C  C   . LYS   B 1 8   ? 1.18248  -37.33874 11.20748  1.000 18.84189 ? 4   LYS   B C   1 
ATOM   2059 O  O   . LYS   B 1 8   ? 2.09901  -37.04418 10.43812  1.000 25.23702 ? 4   LYS   B O   1 
ATOM   2060 C  CB  . LYS   B 1 8   ? 1.56122  -39.39264 12.60550  1.000 26.37733 ? 4   LYS   B CB  1 
ATOM   2061 C  CG  . LYS   B 1 8   ? 0.94286  -40.68060 13.14533  1.000 37.97169 ? 4   LYS   B CG  1 
ATOM   2062 C  CD  . LYS   B 1 8   ? 1.73312  -41.25393 14.31544  1.000 29.74193 ? 4   LYS   B CD  1 
ATOM   2063 C  CE  . LYS   B 1 8   ? 1.13539  -42.57807 14.77673  1.000 28.96705 ? 4   LYS   B CE  1 
ATOM   2064 N  NZ  . LYS   B 1 8   ? 1.04026  -43.56501 13.66015  1.000 28.60896 ? 4   LYS   B NZ  1 
ATOM   2065 N  N   . GLN   B 1 9   ? 0.48309  -36.43425 11.88231  1.000 18.94386 ? 5   GLN   B N   1 
ATOM   2066 C  CA  . GLN   B 1 9   ? 0.67601  -34.99703 11.72967  1.000 13.59522 ? 5   GLN   B CA  1 
ATOM   2067 C  C   . GLN   B 1 9   ? 1.37481  -34.45656 12.97191  1.000 15.87914 ? 5   GLN   B C   1 
ATOM   2068 O  O   . GLN   B 1 9   ? 0.76372  -34.35403 14.04122  1.000 20.93117 ? 5   GLN   B O   1 
ATOM   2069 C  CB  . GLN   B 1 9   ? -0.66251 -34.29945 11.50394  1.000 13.99045 ? 5   GLN   B CB  1 
ATOM   2070 C  CG  . GLN   B 1 9   ? -1.23293 -34.51218 10.11799  1.000 20.98743 ? 5   GLN   B CG  1 
ATOM   2071 C  CD  . GLN   B 1 9   ? -0.37766 -33.87772 9.04285   1.000 20.58179 ? 5   GLN   B CD  1 
ATOM   2072 O  OE1 . GLN   B 1 9   ? 0.14705  -32.77934 9.21907   1.000 30.21020 ? 5   GLN   B OE1 1 
ATOM   2073 N  NE2 . GLN   B 1 9   ? -0.22341 -34.57223 7.92384   1.000 27.17977 ? 5   GLN   B NE2 1 
ATOM   2074 N  N   . TYR   B 1 10  ? 2.64606  -34.09876 12.82504  1.000 10.87770 ? 6   TYR   B N   1 
ATOM   2075 C  CA  . TYR   B 1 10  ? 3.43694  -33.53167 13.90252  1.000 9.57816  ? 6   TYR   B CA  1 
ATOM   2076 C  C   . TYR   B 1 10  ? 3.49047  -32.01100 13.78749  1.000 14.52528 ? 6   TYR   B C   1 
ATOM   2077 O  O   . TYR   B 1 10  ? 3.35262  -31.46317 12.68730  1.000 11.08547 ? 6   TYR   B O   1 
ATOM   2078 C  CB  . TYR   B 1 10  ? 4.85483  -34.11009 13.87447  1.000 10.15219 ? 6   TYR   B CB  1 
ATOM   2079 C  CG  . TYR   B 1 10  ? 4.90211  -35.58349 14.22550  1.000 9.44052  ? 6   TYR   B CG  1 
ATOM   2080 C  CD1 . TYR   B 1 10  ? 4.78109  -36.00184 15.54125  1.000 12.84179 ? 6   TYR   B CD1 1 
ATOM   2081 C  CD2 . TYR   B 1 10  ? 5.06052  -36.55505 13.24001  1.000 11.88911 ? 6   TYR   B CD2 1 
ATOM   2082 C  CE1 . TYR   B 1 10  ? 4.82021  -37.34618 15.87585  1.000 17.25400 ? 6   TYR   B CE1 1 
ATOM   2083 C  CE2 . TYR   B 1 10  ? 5.10256  -37.90731 13.56615  1.000 16.40289 ? 6   TYR   B CE2 1 
ATOM   2084 C  CZ  . TYR   B 1 10  ? 4.98374  -38.29318 14.88898  1.000 20.50382 ? 6   TYR   B CZ  1 
ATOM   2085 O  OH  . TYR   B 1 10  ? 5.01987  -39.62970 15.23533  1.000 21.28415 ? 6   TYR   B OH  1 
ATOM   2086 N  N   . PRO   B 1 11  ? 3.66440  -31.30292 14.90851  1.000 13.09088 ? 7   PRO   B N   1 
ATOM   2087 C  CA  . PRO   B 1 11  ? 3.74579  -29.83794 14.84850  1.000 10.08736 ? 7   PRO   B CA  1 
ATOM   2088 C  C   . PRO   B 1 11  ? 4.87089  -29.38821 13.93168  1.000 10.71967 ? 7   PRO   B C   1 
ATOM   2089 O  O   . PRO   B 1 11  ? 5.95662  -29.97552 13.91492  1.000 12.23873 ? 7   PRO   B O   1 
ATOM   2090 C  CB  . PRO   B 1 11  ? 4.01673  -29.43244 16.30140  1.000 15.45165 ? 7   PRO   B CB  1 
ATOM   2091 C  CG  . PRO   B 1 11  ? 3.54690  -30.58734 17.12288  1.000 19.32217 ? 7   PRO   B CG  1 
ATOM   2092 C  CD  . PRO   B 1 11  ? 3.79761  -31.80871 16.28720  1.000 15.63787 ? 7   PRO   B CD  1 
ATOM   2093 N  N   . ILE   B 1 12  ? 4.60445  -28.33073 13.16768  1.000 10.55395 ? 8   ILE   B N   1 
ATOM   2094 C  CA  . ILE   B 1 12  ? 5.55738  -27.81135 12.19732  1.000 9.33412  ? 8   ILE   B CA  1 
ATOM   2095 C  C   . ILE   B 1 12  ? 5.82202  -26.33972 12.49001  1.000 11.75768 ? 8   ILE   B C   1 
ATOM   2096 O  O   . ILE   B 1 12  ? 4.89713  -25.57291 12.78296  1.000 14.88620 ? 8   ILE   B O   1 
ATOM   2097 C  CB  . ILE   B 1 12  ? 5.06153  -28.02378 10.74986  1.000 16.06245 ? 8   ILE   B CB  1 
ATOM   2098 C  CG1 . ILE   B 1 12  ? 6.09983  -27.52329 9.74238   1.000 16.53440 ? 8   ILE   B CG1 1 
ATOM   2099 C  CG2 . ILE   B 1 12  ? 3.70841  -27.36290 10.52697  1.000 25.93135 ? 8   ILE   B CG2 1 
ATOM   2100 C  CD1 . ILE   B 1 12  ? 6.02447  -28.22594 8.39826   1.000 29.51012 ? 8   ILE   B CD1 1 
ATOM   2101 N  N   . ILE   B 1 13  ? 7.09877  -25.96136 12.44162  1.000 13.48783 ? 9   ILE   B N   1 
ATOM   2102 C  CA  . ILE   B 1 13  ? 7.54800  -24.58737 12.63914  1.000 13.17224 ? 9   ILE   B CA  1 
ATOM   2103 C  C   . ILE   B 1 13  ? 8.34366  -24.17812 11.40782  1.000 10.80237 ? 9   ILE   B C   1 
ATOM   2104 O  O   . ILE   B 1 13  ? 9.23481  -24.91387 10.97091  1.000 11.58642 ? 9   ILE   B O   1 
ATOM   2105 C  CB  . ILE   B 1 13  ? 8.40808  -24.43571 13.90857  1.000 8.35646  ? 9   ILE   B CB  1 
ATOM   2106 C  CG1 . ILE   B 1 13  ? 7.67596  -24.97676 15.14557  1.000 11.90631 ? 9   ILE   B CG1 1 
ATOM   2107 C  CG2 . ILE   B 1 13  ? 8.80128  -22.98192 14.10942  1.000 13.78138 ? 9   ILE   B CG2 1 
ATOM   2108 C  CD1 . ILE   B 1 13  ? 8.03177  -26.40121 15.48098  1.000 14.97245 ? 9   ILE   B CD1 1 
ATOM   2109 N  N   . ASN   B 1 14  ? 8.03604  -23.00439 10.86498  1.000 12.45326 ? 10  ASN   B N   1 
ATOM   2110 C  CA  . ASN   B 1 14  ? 8.61387  -22.53511 9.61148   1.000 16.47652 ? 10  ASN   B CA  1 
ATOM   2111 C  C   . ASN   B 1 14  ? 9.64695  -21.44198 9.85453   1.000 14.39232 ? 10  ASN   B C   1 
ATOM   2112 O  O   . ASN   B 1 14  ? 9.45093  -20.56530 10.70060  1.000 13.06153 ? 10  ASN   B O   1 
ATOM   2113 C  CB  . ASN   B 1 14  ? 7.52410  -22.00514 8.68033   1.000 14.61093 ? 10  ASN   B CB  1 
ATOM   2114 C  CG  . ASN   B 1 14  ? 6.62821  -23.10493 8.15101   1.000 20.93718 ? 10  ASN   B CG  1 
ATOM   2115 O  OD1 . ASN   B 1 14  ? 5.67603  -23.51770 8.81080   1.000 32.84877 ? 10  ASN   B OD1 1 
ATOM   2116 N  ND2 . ASN   B 1 14  ? 6.92986  -23.58556 6.95298   1.000 31.33438 ? 10  ASN   B ND2 1 
ATOM   2117 N  N   . PHE   B 1 15  ? 10.74925 -21.50232 9.10839   1.000 7.30795  ? 11  PHE   B N   1 
ATOM   2118 C  CA  . PHE   B 1 15  ? 11.74182 -20.43603 9.08956   1.000 12.39504 ? 11  PHE   B CA  1 
ATOM   2119 C  C   . PHE   B 1 15  ? 12.25610 -20.27445 7.66846   1.000 12.12876 ? 11  PHE   B C   1 
ATOM   2120 O  O   . PHE   B 1 15  ? 12.39500 -21.25929 6.93728   1.000 9.23345  ? 11  PHE   B O   1 
ATOM   2121 C  CB  . PHE   B 1 15  ? 12.91629 -20.72010 10.03107  1.000 8.34676  ? 11  PHE   B CB  1 
ATOM   2122 C  CG  . PHE   B 1 15  ? 13.93557 -19.61113 10.08415  1.000 13.57518 ? 11  PHE   B CG  1 
ATOM   2123 C  CD1 . PHE   B 1 15  ? 13.62531 -18.39313 10.67707  1.000 11.34845 ? 11  PHE   B CD1 1 
ATOM   2124 C  CD2 . PHE   B 1 15  ? 15.20164 -19.78581 9.55132   1.000 13.63569 ? 11  PHE   B CD2 1 
ATOM   2125 C  CE1 . PHE   B 1 15  ? 14.55754 -17.37149 10.73792  1.000 7.95896  ? 11  PHE   B CE1 1 
ATOM   2126 C  CE2 . PHE   B 1 15  ? 16.13786 -18.76803 9.60404   1.000 12.20968 ? 11  PHE   B CE2 1 
ATOM   2127 C  CZ  . PHE   B 1 15  ? 15.81683 -17.55720 10.20263  1.000 9.44194  ? 11  PHE   B CZ  1 
ATOM   2128 N  N   . THR   B 1 16  ? 12.52786 -19.03725 7.27399   1.000 10.46406 ? 12  THR   B N   1 
ATOM   2129 C  CA  . THR   B 1 16  ? 13.13550 -18.78205 5.97638   1.000 8.13472  ? 12  THR   B CA  1 
ATOM   2130 C  C   . THR   B 1 16  ? 14.32960 -17.85414 6.13473   1.000 12.67580 ? 12  THR   B C   1 
ATOM   2131 O  O   . THR   B 1 16  ? 14.31174 -16.93510 6.95826   1.000 11.47308 ? 12  THR   B O   1 
ATOM   2132 C  CB  . THR   B 1 16  ? 12.12831 -18.18459 4.97459   1.000 11.27086 ? 12  THR   B CB  1 
ATOM   2133 O  OG1 . THR   B 1 16  ? 12.76252 -18.03927 3.70040   1.000 14.65379 ? 12  THR   B OG1 1 
ATOM   2134 C  CG2 . THR   B 1 16  ? 11.61770 -16.82241 5.43459   1.000 13.89157 ? 12  THR   B CG2 1 
ATOM   2135 N  N   . THR   B 1 17  ? 15.37854 -18.11571 5.35453   1.000 14.05450 ? 13  THR   B N   1 
ATOM   2136 C  CA  . THR   B 1 17  ? 16.51736 -17.20967 5.29478   1.000 8.59437  ? 13  THR   B CA  1 
ATOM   2137 C  C   . THR   B 1 17  ? 16.25092 -15.99851 4.41297   1.000 9.43789  ? 13  THR   B C   1 
ATOM   2138 O  O   . THR   B 1 17  ? 17.06518 -15.06834 4.39856   1.000 12.94965 ? 13  THR   B O   1 
ATOM   2139 C  CB  . THR   B 1 17  ? 17.75740 -17.95585 4.79181   1.000 18.33610 ? 13  THR   B CB  1 
ATOM   2140 O  OG1 . THR   B 1 17  ? 17.54165 -18.39509 3.44588   1.000 16.81720 ? 13  THR   B OG1 1 
ATOM   2141 C  CG2 . THR   B 1 17  ? 18.03290 -19.17322 5.66616   1.000 13.22972 ? 13  THR   B CG2 1 
ATOM   2142 N  N   . ALA   B 1 18  ? 15.13502 -15.98402 3.68816   1.000 12.78742 ? 14  ALA   B N   1 
ATOM   2143 C  CA  . ALA   B 1 18  ? 14.79048 -14.86558 2.81720   1.000 14.99281 ? 14  ALA   B CA  1 
ATOM   2144 C  C   . ALA   B 1 18  ? 14.18889 -13.76145 3.67339   1.000 15.62996 ? 14  ALA   B C   1 
ATOM   2145 O  O   . ALA   B 1 18  ? 13.05001 -13.87622 4.13975   1.000 16.03426 ? 14  ALA   B O   1 
ATOM   2146 C  CB  . ALA   B 1 18  ? 13.82362 -15.31213 1.72259   1.000 14.65011 ? 14  ALA   B CB  1 
ATOM   2147 N  N   . GLY   B 1 19  ? 14.95571 -12.69823 3.89634   1.000 15.54137 ? 15  GLY   B N   1 
ATOM   2148 C  CA  . GLY   B 1 19  ? 14.49536 -11.63095 4.75597   1.000 22.38521 ? 15  GLY   B CA  1 
ATOM   2149 C  C   . GLY   B 1 19  ? 14.64825 -11.90141 6.23161   1.000 19.83954 ? 15  GLY   B C   1 
ATOM   2150 O  O   . GLY   B 1 19  ? 13.96441 -11.26134 7.03582   1.000 21.74825 ? 15  GLY   B O   1 
ATOM   2151 N  N   . ALA   B 1 20  ? 15.52814 -12.82883 6.61120   1.000 16.98019 ? 16  ALA   B N   1 
ATOM   2152 C  CA  . ALA   B 1 20  ? 15.71063 -13.18149 8.01384   1.000 12.71793 ? 16  ALA   B CA  1 
ATOM   2153 C  C   . ALA   B 1 20  ? 16.13552 -11.96573 8.82552   1.000 15.44116 ? 16  ALA   B C   1 
ATOM   2154 O  O   . ALA   B 1 20  ? 16.94269 -11.14724 8.37848   1.000 17.72244 ? 16  ALA   B O   1 
ATOM   2155 C  CB  . ALA   B 1 20  ? 16.75378 -14.29349 8.15246   1.000 13.75511 ? 16  ALA   B CB  1 
ATOM   2156 N  N   . THR   B 1 21  ? 15.57264 -11.84472 10.02389  1.000 14.72443 ? 17  THR   B N   1 
ATOM   2157 C  CA  . THR   B 1 21  ? 15.87499 -10.73848 10.91889  1.000 14.57788 ? 17  THR   B CA  1 
ATOM   2158 C  C   . THR   B 1 21  ? 16.10083 -11.28177 12.32011  1.000 13.25425 ? 17  THR   B C   1 
ATOM   2159 O  O   . THR   B 1 21  ? 15.86270 -12.45927 12.59804  1.000 10.71368 ? 17  THR   B O   1 
ATOM   2160 C  CB  . THR   B 1 21  ? 14.74026 -9.70792  10.96456  1.000 19.26133 ? 17  THR   B CB  1 
ATOM   2161 O  OG1 . THR   B 1 21  ? 13.57023 -10.32411 11.52275  1.000 13.69392 ? 17  THR   B OG1 1 
ATOM   2162 C  CG2 . THR   B 1 21  ? 14.42263 -9.17696  9.57381   1.000 21.83298 ? 17  THR   B CG2 1 
ATOM   2163 N  N   . VAL   B 1 22  ? 16.54436 -10.39735 13.21987  1.000 11.98602 ? 18  VAL   B N   1 
ATOM   2164 C  CA  . VAL   B 1 22  ? 16.60512 -10.76824 14.63072  1.000 11.92265 ? 18  VAL   B CA  1 
ATOM   2165 C  C   . VAL   B 1 22  ? 15.23965 -11.23531 15.11022  1.000 16.60254 ? 18  VAL   B C   1 
ATOM   2166 O  O   . VAL   B 1 22  ? 15.12067 -12.26006 15.79454  1.000 14.35007 ? 18  VAL   B O   1 
ATOM   2167 C  CB  . VAL   B 1 22  ? 17.11850 -9.59218  15.48182  1.000 18.22584 ? 18  VAL   B CB  1 
ATOM   2168 C  CG1 . VAL   B 1 22  ? 16.95653 -9.91122  16.96438  1.000 16.61498 ? 18  VAL   B CG1 1 
ATOM   2169 C  CG2 . VAL   B 1 22  ? 18.55972 -9.30441  15.16273  1.000 15.12927 ? 18  VAL   B CG2 1 
ATOM   2170 N  N   . GLN   B 1 23  ? 14.18443 -10.50126 14.74683  1.000 12.27032 ? 19  GLN   B N   1 
ATOM   2171 C  CA  . GLN   B 1 23  ? 12.85727 -10.84556 15.24479  1.000 13.44294 ? 19  GLN   B CA  1 
ATOM   2172 C  C   . GLN   B 1 23  ? 12.38711 -12.19351 14.70704  1.000 14.50656 ? 19  GLN   B C   1 
ATOM   2173 O  O   . GLN   B 1 23  ? 11.83587 -13.00406 15.45916  1.000 12.09689 ? 19  GLN   B O   1 
ATOM   2174 C  CB  . GLN   B 1 23  ? 11.85389 -9.74986  14.89104  1.000 20.24185 ? 19  GLN   B CB  1 
ATOM   2175 C  CG  . GLN   B 1 23  ? 10.47605 -9.97585  15.50415  1.000 18.81219 ? 19  GLN   B CG  1 
ATOM   2176 C  CD  . GLN   B 1 23  ? 10.48582 -9.87181  17.01897  1.000 36.97896 ? 19  GLN   B CD  1 
ATOM   2177 O  OE1 . GLN   B 1 23  ? 10.97321 -8.89023  17.58236  1.000 38.35138 ? 19  GLN   B OE1 1 
ATOM   2178 N  NE2 . GLN   B 1 23  ? 9.95393  -10.89166 17.68702  1.000 36.04059 ? 19  GLN   B NE2 1 
ATOM   2179 N  N   . SER   B 1 24  ? 12.59403 -12.45801 13.41186  1.000 10.95317 ? 20  SER   B N   1 
ATOM   2180 C  CA  . SER   B 1 24  ? 12.09461 -13.70725 12.84310  1.000 10.21255 ? 20  SER   B CA  1 
ATOM   2181 C  C   . SER   B 1 24  ? 12.88398 -14.91283 13.34234  1.000 10.56564 ? 20  SER   B C   1 
ATOM   2182 O  O   . SER   B 1 24  ? 12.31143 -15.99689 13.51405  1.000 11.17398 ? 20  SER   B O   1 
ATOM   2183 C  CB  . SER   B 1 24  ? 12.11220 -13.65062 11.31197  1.000 12.85837 ? 20  SER   B CB  1 
ATOM   2184 O  OG  . SER   B 1 24  ? 13.41018 -13.86963 10.78960  1.000 14.48116 ? 20  SER   B OG  1 
ATOM   2185 N  N   . TYR   B 1 25  ? 14.18865 -14.75422 13.58195  1.000 10.12876 ? 21  TYR   B N   1 
ATOM   2186 C  CA  . TYR   B 1 25  ? 14.95933 -15.86362 14.13317  1.000 11.00166 ? 21  TYR   B CA  1 
ATOM   2187 C  C   . TYR   B 1 25  ? 14.59704 -16.10774 15.59384  1.000 12.25950 ? 21  TYR   B C   1 
ATOM   2188 O  O   . TYR   B 1 25  ? 14.52004 -17.26252 16.03367  1.000 8.39085  ? 21  TYR   B O   1 
ATOM   2189 C  CB  . TYR   B 1 25  ? 16.46008 -15.60519 13.97803  1.000 10.25824 ? 21  TYR   B CB  1 
ATOM   2190 C  CG  . TYR   B 1 25  ? 17.32263 -16.75493 14.46778  1.000 11.18686 ? 21  TYR   B CG  1 
ATOM   2191 C  CD1 . TYR   B 1 25  ? 17.41717 -17.94243 13.74783  1.000 11.51520 ? 21  TYR   B CD1 1 
ATOM   2192 C  CD2 . TYR   B 1 25  ? 18.03987 -16.64944 15.65141  1.000 12.19446 ? 21  TYR   B CD2 1 
ATOM   2193 C  CE1 . TYR   B 1 25  ? 18.20216 -18.99751 14.20532  1.000 11.18227 ? 21  TYR   B CE1 1 
ATOM   2194 C  CE2 . TYR   B 1 25  ? 18.82412 -17.68465 16.10755  1.000 14.45688 ? 21  TYR   B CE2 1 
ATOM   2195 C  CZ  . TYR   B 1 25  ? 18.90228 -18.85598 15.38613  1.000 12.35319 ? 21  TYR   B CZ  1 
ATOM   2196 O  OH  . TYR   B 1 25  ? 19.69210 -19.87487 15.86674  1.000 10.75460 ? 21  TYR   B OH  1 
ATOM   2197 N  N   . THR   B 1 26  ? 14.35989 -15.03310 16.35569  1.000 9.68303  ? 22  THR   B N   1 
ATOM   2198 C  CA  . THR   B 1 26  ? 13.92497 -15.17819 17.74134  1.000 9.85267  ? 22  THR   B CA  1 
ATOM   2199 C  C   . THR   B 1 26  ? 12.57880 -15.88577 17.82171  1.000 10.62220 ? 22  THR   B C   1 
ATOM   2200 O  O   . THR   B 1 26  ? 12.40227 -16.82105 18.61178  1.000 14.10183 ? 22  THR   B O   1 
ATOM   2201 C  CB  . THR   B 1 26  ? 13.83119 -13.81092 18.42123  1.000 15.31478 ? 22  THR   B CB  1 
ATOM   2202 O  OG1 . THR   B 1 26  ? 15.11381 -13.17042 18.42000  1.000 17.10323 ? 22  THR   B OG1 1 
ATOM   2203 C  CG2 . THR   B 1 26  ? 13.34919 -13.97570 19.85027  1.000 15.20415 ? 22  THR   B CG2 1 
ATOM   2204 N  N   . ASN   B 1 27  ? 11.60742 -15.43294 17.02084  1.000 14.86883 ? 23  ASN   B N   1 
ATOM   2205 C  CA  . ASN   B 1 27  ? 10.29499 -16.07109 17.00374  1.000 12.20583 ? 23  ASN   B CA  1 
ATOM   2206 C  C   . ASN   B 1 27  ? 10.41280 -17.54729 16.66437  1.000 10.95957 ? 23  ASN   B C   1 
ATOM   2207 O  O   . ASN   B 1 27  ? 9.68059  -18.37955 17.20930  1.000 11.80978 ? 23  ASN   B O   1 
ATOM   2208 C  CB  . ASN   B 1 27  ? 9.37853  -15.37064 15.99875  1.000 15.93995 ? 23  ASN   B CB  1 
ATOM   2209 C  CG  . ASN   B 1 27  ? 9.04678  -13.95039 16.40190  1.000 23.63468 ? 23  ASN   B CG  1 
ATOM   2210 O  OD1 . ASN   B 1 27  ? 9.11992  -13.59655 17.57764  1.000 23.09119 ? 23  ASN   B OD1 1 
ATOM   2211 N  ND2 . ASN   B 1 27  ? 8.67654  -13.12464 15.42351  1.000 26.24530 ? 23  ASN   B ND2 1 
ATOM   2212 N  N   . PHE   B 1 28  ? 11.34714 -17.88493 15.77780  1.000 10.86996 ? 24  PHE   B N   1 
ATOM   2213 C  CA  . PHE   B 1 28  ? 11.51285 -19.26000 15.32560  1.000 7.86166  ? 24  PHE   B CA  1 
ATOM   2214 C  C   . PHE   B 1 28  ? 12.03119 -20.16043 16.44202  1.000 10.25770 ? 24  PHE   B C   1 
ATOM   2215 O  O   . PHE   B 1 28  ? 11.45469 -21.22184 16.70746  1.000 8.36000  ? 24  PHE   B O   1 
ATOM   2216 C  CB  . PHE   B 1 28  ? 12.45654 -19.28191 14.12970  1.000 7.56166  ? 24  PHE   B CB  1 
ATOM   2217 C  CG  . PHE   B 1 28  ? 12.96315 -20.63755 13.77853  1.000 10.80265 ? 24  PHE   B CG  1 
ATOM   2218 C  CD1 . PHE   B 1 28  ? 12.08587 -21.65339 13.43469  1.000 12.35741 ? 24  PHE   B CD1 1 
ATOM   2219 C  CD2 . PHE   B 1 28  ? 14.32517 -20.89203 13.75498  1.000 16.55877 ? 24  PHE   B CD2 1 
ATOM   2220 C  CE1 . PHE   B 1 28  ? 12.55780 -22.90057 13.09345  1.000 9.33637  ? 24  PHE   B CE1 1 
ATOM   2221 C  CE2 . PHE   B 1 28  ? 14.80246 -22.14334 13.41195  1.000 16.06385 ? 24  PHE   B CE2 1 
ATOM   2222 C  CZ  . PHE   B 1 28  ? 13.91754 -23.14627 13.08260  1.000 15.93986 ? 24  PHE   B CZ  1 
ATOM   2223 N  N   . ILE   B 1 29  ? 13.12051 -19.75725 17.10714  1.000 8.59022  ? 25  ILE   B N   1 
ATOM   2224 C  CA  . ILE   B 1 29  ? 13.70960 -20.61138 18.13995  1.000 9.20405  ? 25  ILE   B CA  1 
ATOM   2225 C  C   . ILE   B 1 29  ? 12.78183 -20.71846 19.34414  1.000 14.13138 ? 25  ILE   B C   1 
ATOM   2226 O  O   . ILE   B 1 29  ? 12.67833 -21.78054 19.97254  1.000 8.89619  ? 25  ILE   B O   1 
ATOM   2227 C  CB  . ILE   B 1 29  ? 15.10708 -20.10338 18.54412  1.000 9.25931  ? 25  ILE   B CB  1 
ATOM   2228 C  CG1 . ILE   B 1 29  ? 16.07987 -20.20825 17.37314  1.000 7.42812  ? 25  ILE   B CG1 1 
ATOM   2229 C  CG2 . ILE   B 1 29  ? 15.65821 -20.91607 19.72133  1.000 7.75556  ? 25  ILE   B CG2 1 
ATOM   2230 C  CD1 . ILE   B 1 29  ? 16.24325 -21.62951 16.83688  1.000 8.95564  ? 25  ILE   B CD1 1 
ATOM   2231 N  N   . ARG   B 1 30  ? 12.09163 -19.62670 19.68634  1.000 10.82128 ? 26  ARG   B N   1 
ATOM   2232 C  CA  . ARG   B 1 30  ? 11.11392 -19.68171 20.76802  1.000 8.97709  ? 26  ARG   B CA  1 
ATOM   2233 C  C   . ARG   B 1 30  ? 9.97393  -20.63745 20.44018  1.000 9.56102  ? 26  ARG   B C   1 
ATOM   2234 O  O   . ARG   B 1 30  ? 9.47524  -21.34032 21.32475  1.000 12.57867 ? 26  ARG   B O   1 
ATOM   2235 C  CB  . ARG   B 1 30  ? 10.57634 -18.28145 21.06090  1.000 13.05569 ? 26  ARG   B CB  1 
ATOM   2236 C  CG  . ARG   B 1 30  ? 11.61750 -17.36013 21.66807  1.000 16.83622 ? 26  ARG   B CG  1 
ATOM   2237 C  CD  . ARG   B 1 30  ? 10.99515 -16.10718 22.25432  1.000 20.90034 ? 26  ARG   B CD  1 
ATOM   2238 N  NE  . ARG   B 1 30  ? 12.01012 -15.21953 22.80776  1.000 20.64131 ? 26  ARG   B NE  1 
ATOM   2239 C  CZ  . ARG   B 1 30  ? 11.78481 -13.96800 23.18094  1.000 30.53341 ? 26  ARG   B CZ  1 
ATOM   2240 N  NH1 . ARG   B 1 30  ? 10.58424 -13.42224 23.07647  1.000 28.41278 ? 26  ARG   B NH1 1 
ATOM   2241 N  NH2 . ARG   B 1 30  ? 12.79059 -13.24452 23.66556  1.000 28.83973 ? 26  ARG   B NH2 1 
ATOM   2242 N  N   . ALA   B 1 31  ? 9.53862  -20.67193 19.17580  1.000 9.54299  ? 27  ALA   B N   1 
ATOM   2243 C  CA  . ALA   B 1 31  ? 8.49807  -21.62144 18.78340  1.000 16.55583 ? 27  ALA   B CA  1 
ATOM   2244 C  C   . ALA   B 1 31  ? 8.99856  -23.05991 18.87081  1.000 11.75255 ? 27  ALA   B C   1 
ATOM   2245 O  O   . ALA   B 1 31  ? 8.27104  -23.95270 19.32368  1.000 14.29226 ? 27  ALA   B O   1 
ATOM   2246 C  CB  . ALA   B 1 31  ? 8.00349  -21.31175 17.36958  1.000 10.91944 ? 27  ALA   B CB  1 
ATOM   2247 N  N   . VAL   B 1 32  ? 10.23781 -23.30364 18.44380  1.000 13.57581 ? 28  VAL   B N   1 
ATOM   2248 C  CA  . VAL   B 1 32  ? 10.81496 -24.64153 18.55552  1.000 9.04905  ? 28  VAL   B CA  1 
ATOM   2249 C  C   . VAL   B 1 32  ? 10.85808 -25.07622 20.01577  1.000 9.80425  ? 28  VAL   B C   1 
ATOM   2250 O  O   . VAL   B 1 32  ? 10.41177 -26.17388 20.37091  1.000 12.36122 ? 28  VAL   B O   1 
ATOM   2251 C  CB  . VAL   B 1 32  ? 12.21187 -24.67493 17.91183  1.000 6.70383  ? 28  VAL   B CB  1 
ATOM   2252 C  CG1 . VAL   B 1 32  ? 12.92423 -25.97667 18.24423  1.000 15.43872 ? 28  VAL   B CG1 1 
ATOM   2253 C  CG2 . VAL   B 1 32  ? 12.10180 -24.49445 16.39621  1.000 9.40220  ? 28  VAL   B CG2 1 
ATOM   2254 N  N   . ARG   B 1 33  ? 11.37733 -24.20971 20.88830  1.000 9.63011  ? 29  ARG   B N   1 
ATOM   2255 C  CA  . ARG   B 1 33  ? 11.43053 -24.53901 22.31042  1.000 15.15806 ? 29  ARG   B CA  1 
ATOM   2256 C  C   . ARG   B 1 33  ? 10.04180 -24.83117 22.86607  1.000 12.47958 ? 29  ARG   B C   1 
ATOM   2257 O  O   . ARG   B 1 33  ? 9.86474  -25.77118 23.64944  1.000 14.57247 ? 29  ARG   B O   1 
ATOM   2258 C  CB  . ARG   B 1 33  ? 12.08282 -23.40011 23.09109  1.000 21.69100 ? 29  ARG   B CB  1 
ATOM   2259 C  CG  . ARG   B 1 33  ? 13.52020 -23.10666 22.70541  1.000 8.81845  ? 29  ARG   B CG  1 
ATOM   2260 C  CD  . ARG   B 1 33  ? 14.15104 -22.15797 23.71107  1.000 10.31232 ? 29  ARG   B CD  1 
ATOM   2261 N  NE  . ARG   B 1 33  ? 15.55281 -21.89594 23.41304  1.000 12.81930 ? 29  ARG   B NE  1 
ATOM   2262 C  CZ  . ARG   B 1 33  ? 16.08692 -20.68712 23.31652  1.000 13.87372 ? 29  ARG   B CZ  1 
ATOM   2263 N  NH1 . ARG   B 1 33  ? 15.37234 -19.59555 23.54286  1.000 12.57423 ? 29  ARG   B NH1 1 
ATOM   2264 N  NH2 . ARG   B 1 33  ? 17.37293 -20.57062 22.99545  1.000 10.11649 ? 29  ARG   B NH2 1 
ATOM   2265 N  N   . GLY   B 1 34  ? 9.04321  -24.03428 22.47344  1.000 11.99001 ? 30  GLY   B N   1 
ATOM   2266 C  CA  . GLY   B 1 34  ? 7.68349  -24.26091 22.93139  1.000 16.08730 ? 30  GLY   B CA  1 
ATOM   2267 C  C   . GLY   B 1 34  ? 7.08997  -25.56792 22.45389  1.000 20.37530 ? 30  GLY   B C   1 
ATOM   2268 O  O   . GLY   B 1 34  ? 6.15735  -26.08507 23.08151  1.000 19.35341 ? 30  GLY   B O   1 
ATOM   2269 N  N   . ARG   B 1 35  ? 7.60813  -26.11585 21.35543  1.000 16.77861 ? 31  ARG   B N   1 
ATOM   2270 C  CA  . ARG   B 1 35  ? 7.14773  -27.39721 20.84289  1.000 15.92003 ? 31  ARG   B CA  1 
ATOM   2271 C  C   . ARG   B 1 35  ? 7.93659  -28.57436 21.38932  1.000 11.31180 ? 31  ARG   B C   1 
ATOM   2272 O  O   . ARG   B 1 35  ? 7.42507  -29.70123 21.38959  1.000 11.85737 ? 31  ARG   B O   1 
ATOM   2273 C  CB  . ARG   B 1 35  ? 7.22277  -27.40127 19.31594  1.000 19.85817 ? 31  ARG   B CB  1 
ATOM   2274 C  CG  . ARG   B 1 35  ? 6.26530  -26.43081 18.69211  1.000 19.65064 ? 31  ARG   B CG  1 
ATOM   2275 C  CD  . ARG   B 1 35  ? 4.93498  -26.63648 19.33456  1.000 23.79864 ? 31  ARG   B CD  1 
ATOM   2276 N  NE  . ARG   B 1 35  ? 3.84174  -26.09569 18.54990  1.000 39.08249 ? 31  ARG   B NE  1 
ATOM   2277 C  CZ  . ARG   B 1 35  ? 2.59043  -26.50613 18.66924  1.000 34.18600 ? 31  ARG   B CZ  1 
ATOM   2278 N  NH1 . ARG   B 1 35  ? 2.26336  -27.49157 19.48704  1.000 36.82895 ? 31  ARG   B NH1 1 
ATOM   2279 N  NH2 . ARG   B 1 35  ? 1.64505  -25.90833 17.95983  1.000 46.75562 ? 31  ARG   B NH2 1 
ATOM   2280 N  N   . LEU   B 1 36  ? 9.17013  -28.33986 21.83565  1.000 14.58692 ? 32  LEU   B N   1 
ATOM   2281 C  CA  . LEU   B 1 36  ? 9.97493  -29.40280 22.41973  1.000 16.53043 ? 32  LEU   B CA  1 
ATOM   2282 C  C   . LEU   B 1 36  ? 9.51141  -29.73935 23.82747  1.000 17.89393 ? 32  LEU   B C   1 
ATOM   2283 O  O   . LEU   B 1 36  ? 9.46659  -30.91665 24.19918  1.000 16.86892 ? 32  LEU   B O   1 
ATOM   2284 C  CB  . LEU   B 1 36  ? 11.44706 -28.99971 22.43364  1.000 15.33534 ? 32  LEU   B CB  1 
ATOM   2285 C  CG  . LEU   B 1 36  ? 12.12421 -28.90451 21.06587  1.000 12.54286 ? 32  LEU   B CG  1 
ATOM   2286 C  CD1 . LEU   B 1 36  ? 13.50996 -28.29183 21.19777  1.000 11.17066 ? 32  LEU   B CD1 1 
ATOM   2287 C  CD2 . LEU   B 1 36  ? 12.20428 -30.28279 20.43151  1.000 19.44613 ? 32  LEU   B CD2 1 
ATOM   2288 N  N   . THR   B 1 37  ? 9.16277  -28.72262 24.61417  1.000 16.47655 ? 33  THR   B N   1 
ATOM   2289 C  CA  . THR   B 1 37  ? 8.77331  -28.88115 26.00794  1.000 32.20897 ? 33  THR   B CA  1 
ATOM   2290 C  C   . THR   B 1 37  ? 7.38833  -28.29699 26.24543  1.000 23.04797 ? 33  THR   B C   1 
ATOM   2291 O  O   . THR   B 1 37  ? 7.00078  -27.30180 25.62588  1.000 26.47723 ? 33  THR   B O   1 
ATOM   2292 C  CB  . THR   B 1 37  ? 9.76121  -28.18310 26.95811  1.000 33.70010 ? 33  THR   B CB  1 
ATOM   2293 O  OG1 . THR   B 1 37  ? 10.11461 -26.89800 26.42631  1.000 47.12787 ? 33  THR   B OG1 1 
ATOM   2294 C  CG2 . THR   B 1 37  ? 11.00773 -29.01442 27.15219  1.000 36.81249 ? 33  THR   B CG2 1 
ATOM   2295 N  N   . THR   B 1 38  ? 6.64851  -28.92002 27.16435  1.000 22.15832 ? 34  THR   B N   1 
ATOM   2296 C  CA  . THR   B 1 38  ? 5.42030  -28.31512 27.66155  1.000 39.20756 ? 34  THR   B CA  1 
ATOM   2297 C  C   . THR   B 1 38  ? 5.68994  -27.28029 28.74384  1.000 35.98239 ? 34  THR   B C   1 
ATOM   2298 O  O   . THR   B 1 38  ? 4.84281  -26.41217 28.98217  1.000 32.21297 ? 34  THR   B O   1 
ATOM   2299 C  CB  . THR   B 1 38  ? 4.47370  -29.38607 28.21465  1.000 30.88790 ? 34  THR   B CB  1 
ATOM   2300 O  OG1 . THR   B 1 38  ? 5.11666  -30.08985 29.28589  1.000 35.38291 ? 34  THR   B OG1 1 
ATOM   2301 C  CG2 . THR   B 1 38  ? 4.08219  -30.37009 27.12078  1.000 37.12016 ? 34  THR   B CG2 1 
ATOM   2302 N  N   . GLY   B 1 39  ? 6.85128  -27.34456 29.38976  1.000 32.52502 ? 35  GLY   B N   1 
ATOM   2303 C  CA  . GLY   B 1 39  ? 7.15809  -26.47773 30.50359  1.000 44.54755 ? 35  GLY   B CA  1 
ATOM   2304 C  C   . GLY   B 1 39  ? 6.73244  -27.00979 31.85180  1.000 35.17231 ? 35  GLY   B C   1 
ATOM   2305 O  O   . GLY   B 1 39  ? 6.90869  -26.31181 32.85892  1.000 39.74333 ? 35  GLY   B O   1 
ATOM   2306 N  N   . ALA   B 1 40  ? 6.17851  -28.22354 31.90681  1.000 30.38950 ? 36  ALA   B N   1 
ATOM   2307 C  CA  . ALA   B 1 40  ? 5.71212  -28.77926 33.17193  1.000 34.01601 ? 36  ALA   B CA  1 
ATOM   2308 C  C   . ALA   B 1 40  ? 6.86238  -29.23561 34.06066  1.000 36.17902 ? 36  ALA   B C   1 
ATOM   2309 O  O   . ALA   B 1 40  ? 6.75456  -29.16215 35.28907  1.000 35.07169 ? 36  ALA   B O   1 
ATOM   2310 C  CB  . ALA   B 1 40  ? 4.75914  -29.94518 32.91193  1.000 36.87381 ? 36  ALA   B CB  1 
ATOM   2311 N  N   . ASP   B 1 41  ? 7.95772  -29.70689 33.46669  1.000 26.67415 ? 37  ASP   B N   1 
ATOM   2312 C  CA  . ASP   B 1 41  ? 9.11295  -30.20273 34.20588  1.000 21.82628 ? 37  ASP   B CA  1 
ATOM   2313 C  C   . ASP   B 1 41  ? 10.20593 -29.13947 34.16526  1.000 22.57861 ? 37  ASP   B C   1 
ATOM   2314 O  O   . ASP   B 1 41  ? 10.80261 -28.89554 33.11350  1.000 25.43399 ? 37  ASP   B O   1 
ATOM   2315 C  CB  . ASP   B 1 41  ? 9.60200  -31.52257 33.61319  1.000 19.73846 ? 37  ASP   B CB  1 
ATOM   2316 C  CG  . ASP   B 1 41  ? 10.62563 -32.21774 34.49404  1.000 30.33238 ? 37  ASP   B CG  1 
ATOM   2317 O  OD1 . ASP   B 1 41  ? 10.94672 -31.68139 35.57661  1.000 26.12706 ? 37  ASP   B OD1 1 
ATOM   2318 O  OD2 . ASP   B 1 41  ? 11.10552 -33.30545 34.10514  1.000 23.24266 ? 37  ASP   B OD2 1 
ATOM   2319 N  N   . VAL   B 1 42  ? 10.46453 -28.50695 35.30837  1.000 19.78677 ? 38  VAL   B N   1 
ATOM   2320 C  CA  . VAL   B 1 42  ? 11.45177 -27.43817 35.42360  1.000 18.52502 ? 38  VAL   B CA  1 
ATOM   2321 C  C   . VAL   B 1 42  ? 12.28707 -27.68710 36.67263  1.000 24.33017 ? 38  VAL   B C   1 
ATOM   2322 O  O   . VAL   B 1 42  ? 11.73622 -27.91435 37.75550  1.000 23.44953 ? 38  VAL   B O   1 
ATOM   2323 C  CB  . VAL   B 1 42  ? 10.78309 -26.04994 35.48845  1.000 18.97849 ? 38  VAL   B CB  1 
ATOM   2324 C  CG1 . VAL   B 1 42  ? 11.80651 -24.98010 35.79762  1.000 22.67381 ? 38  VAL   B CG1 1 
ATOM   2325 C  CG2 . VAL   B 1 42  ? 10.06601 -25.73057 34.18179  1.000 23.84711 ? 38  VAL   B CG2 1 
ATOM   2326 N  N   . ARG   B 1 43  ? 13.61122 -27.65137 36.52494  1.000 19.10651 ? 39  ARG   B N   1 
ATOM   2327 C  CA  . ARG   B 1 43  ? 14.52928 -27.77393 37.65261  1.000 20.54609 ? 39  ARG   B CA  1 
ATOM   2328 C  C   . ARG   B 1 43  ? 15.42657 -26.54634 37.67693  1.000 20.17221 ? 39  ARG   B C   1 
ATOM   2329 O  O   . ARG   B 1 43  ? 16.11601 -26.26145 36.69238  1.000 19.42974 ? 39  ARG   B O   1 
ATOM   2330 C  CB  . ARG   B 1 43  ? 15.38055 -29.04226 37.55691  1.000 22.08144 ? 39  ARG   B CB  1 
ATOM   2331 C  CG  . ARG   B 1 43  ? 14.75504 -30.18258 36.78099  1.000 20.66184 ? 39  ARG   B CG  1 
ATOM   2332 C  CD  . ARG   B 1 43  ? 13.87218 -31.07584 37.63322  1.000 20.28236 ? 39  ARG   B CD  1 
ATOM   2333 N  NE  . ARG   B 1 43  ? 13.28173 -32.13173 36.81696  1.000 27.23765 ? 39  ARG   B NE  1 
ATOM   2334 C  CZ  . ARG   B 1 43  ? 13.83138 -33.32066 36.60286  1.000 24.64881 ? 39  ARG   B CZ  1 
ATOM   2335 N  NH1 . ARG   B 1 43  ? 14.95611 -33.68058 37.19903  1.000 20.13507 ? 39  ARG   B NH1 1 
ATOM   2336 N  NH2 . ARG   B 1 43  ? 13.23996 -34.16805 35.76322  1.000 19.01644 ? 39  ARG   B NH2 1 
ATOM   2337 N  N   . HIS   B 1 44  ? 15.42394 -25.82885 38.79817  1.000 21.50917 ? 40  HIS   B N   1 
ATOM   2338 C  CA  . HIS   B 1 44  ? 16.27537 -24.65311 38.96197  1.000 21.84613 ? 40  HIS   B CA  1 
ATOM   2339 C  C   . HIS   B 1 44  ? 16.06084 -23.66125 37.82327  1.000 23.44075 ? 40  HIS   B C   1 
ATOM   2340 O  O   . HIS   B 1 44  ? 17.00566 -23.05794 37.30761  1.000 24.79891 ? 40  HIS   B O   1 
ATOM   2341 C  CB  . HIS   B 1 44  ? 17.74553 -25.06099 39.06881  1.000 21.83592 ? 40  HIS   B CB  1 
ATOM   2342 C  CG  . HIS   B 1 44  ? 18.00873 -26.06778 40.14480  1.000 29.56285 ? 40  HIS   B CG  1 
ATOM   2343 N  ND1 . HIS   B 1 44  ? 17.84957 -25.78249 41.48327  1.000 33.31294 ? 40  HIS   B ND1 1 
ATOM   2344 C  CD2 . HIS   B 1 44  ? 18.41088 -27.35880 40.08031  1.000 27.63869 ? 40  HIS   B CD2 1 
ATOM   2345 C  CE1 . HIS   B 1 44  ? 18.14552 -26.85351 42.19758  1.000 40.02000 ? 40  HIS   B CE1 1 
ATOM   2346 N  NE2 . HIS   B 1 44  ? 18.48696 -27.82449 41.36994  1.000 31.68668 ? 40  HIS   B NE2 1 
ATOM   2347 N  N   . GLU   B 1 45  ? 14.79918 -23.52466 37.40965  1.000 20.58713 ? 41  GLU   B N   1 
ATOM   2348 C  CA  . GLU   B 1 45  ? 14.32280 -22.60272 36.37834  1.000 22.08880 ? 41  GLU   B CA  1 
ATOM   2349 C  C   . GLU   B 1 45  ? 14.69947 -23.03056 34.96202  1.000 25.07668 ? 41  GLU   B C   1 
ATOM   2350 O  O   . GLU   B 1 45  ? 14.55870 -22.23236 34.02759  1.000 20.66272 ? 41  GLU   B O   1 
ATOM   2351 C  CB  . GLU   B 1 45  ? 14.80573 -21.16855 36.63482  1.000 27.97865 ? 41  GLU   B CB  1 
ATOM   2352 C  CG  . GLU   B 1 45  ? 14.49547 -20.66886 38.04301  1.000 29.56589 ? 41  GLU   B CG  1 
ATOM   2353 C  CD  . GLU   B 1 45  ? 14.82580 -19.20334 38.23736  1.000 44.55618 ? 41  GLU   B CD  1 
ATOM   2354 O  OE1 . GLU   B 1 45  ? 15.83770 -18.73611 37.67447  1.000 45.95911 ? 41  GLU   B OE1 1 
ATOM   2355 O  OE2 . GLU   B 1 45  ? 14.06708 -18.51490 38.95087  1.000 55.99410 ? 41  GLU   B OE2 1 
ATOM   2356 N  N   . ILE   B 1 46  ? 15.13599 -24.26789 34.76552  1.000 17.68677 ? 42  ILE   B N   1 
ATOM   2357 C  CA  . ILE   B 1 46  ? 15.57768 -24.75522 33.46169  1.000 16.32842 ? 42  ILE   B CA  1 
ATOM   2358 C  C   . ILE   B 1 46  ? 14.61545 -25.84848 33.00836  1.000 20.10711 ? 42  ILE   B C   1 
ATOM   2359 O  O   . ILE   B 1 46  ? 14.48015 -26.86876 33.69832  1.000 16.30869 ? 42  ILE   B O   1 
ATOM   2360 C  CB  . ILE   B 1 46  ? 17.02127 -25.27828 33.51454  1.000 16.64921 ? 42  ILE   B CB  1 
ATOM   2361 C  CG1 . ILE   B 1 46  ? 17.94141 -24.21408 34.11667  1.000 17.68352 ? 42  ILE   B CG1 1 
ATOM   2362 C  CG2 . ILE   B 1 46  ? 17.49310 -25.66434 32.11980  1.000 22.09968 ? 42  ILE   B CG2 1 
ATOM   2363 C  CD1 . ILE   B 1 46  ? 19.37455 -24.66008 34.27870  1.000 20.72208 ? 42  ILE   B CD1 1 
ATOM   2364 N  N   . PRO   B 1 47  ? 13.93574 -25.68583 31.87199  1.000 18.01669 ? 43  PRO   B N   1 
ATOM   2365 C  CA  . PRO   B 1 47  ? 12.98734 -26.71122 31.42072  1.000 16.69856 ? 43  PRO   B CA  1 
ATOM   2366 C  C   . PRO   B 1 47  ? 13.67869 -28.01531 31.05258  1.000 16.46053 ? 43  PRO   B C   1 
ATOM   2367 O  O   . PRO   B 1 47  ? 14.80972 -28.03365 30.56080  1.000 14.88865 ? 43  PRO   B O   1 
ATOM   2368 C  CB  . PRO   B 1 47  ? 12.33228 -26.07073 30.18873  1.000 22.91626 ? 43  PRO   B CB  1 
ATOM   2369 C  CG  . PRO   B 1 47  ? 12.53407 -24.59652 30.37514  1.000 17.93870 ? 43  PRO   B CG  1 
ATOM   2370 C  CD  . PRO   B 1 47  ? 13.86836 -24.46927 31.04458  1.000 16.99928 ? 43  PRO   B CD  1 
ATOM   2371 N  N   . VAL   B 1 48  ? 12.97070 -29.11767 31.28925  1.000 15.73162 ? 44  VAL   B N   1 
ATOM   2372 C  CA  . VAL   B 1 48  ? 13.44625 -30.45691 30.96173  1.000 14.06529 ? 44  VAL   B CA  1 
ATOM   2373 C  C   . VAL   B 1 48  ? 12.61114 -31.01721 29.81940  1.000 13.39385 ? 44  VAL   B C   1 
ATOM   2374 O  O   . VAL   B 1 48  ? 11.37918 -30.90454 29.82065  1.000 15.55948 ? 44  VAL   B O   1 
ATOM   2375 C  CB  . VAL   B 1 48  ? 13.38748 -31.39564 32.18029  1.000 15.15659 ? 44  VAL   B CB  1 
ATOM   2376 C  CG1 . VAL   B 1 48  ? 13.91664 -32.77181 31.81016  1.000 14.97657 ? 44  VAL   B CG1 1 
ATOM   2377 C  CG2 . VAL   B 1 48  ? 14.18318 -30.81041 33.32075  1.000 22.25090 ? 44  VAL   B CG2 1 
ATOM   2378 N  N   . LEU   B 1 49  ? 13.28808 -31.63042 28.85118  1.000 12.63660 ? 45  LEU   B N   1 
ATOM   2379 C  CA  . LEU   B 1 49  ? 12.62253 -32.27063 27.73048  1.000 12.09399 ? 45  LEU   B CA  1 
ATOM   2380 C  C   . LEU   B 1 49  ? 11.82024 -33.47835 28.21140  1.000 14.31051 ? 45  LEU   B C   1 
ATOM   2381 O  O   . LEU   B 1 49  ? 12.07071 -34.00662 29.29694  1.000 13.63732 ? 45  LEU   B O   1 
ATOM   2382 C  CB  . LEU   B 1 49  ? 13.65678 -32.69537 26.68886  1.000 13.40827 ? 45  LEU   B CB  1 
ATOM   2383 C  CG  . LEU   B 1 49  ? 14.41408 -31.54690 26.01320  1.000 13.75922 ? 45  LEU   B CG  1 
ATOM   2384 C  CD1 . LEU   B 1 49  ? 15.53562 -32.08267 25.12092  1.000 10.24860 ? 45  LEU   B CD1 1 
ATOM   2385 C  CD2 . LEU   B 1 49  ? 13.46391 -30.67005 25.20706  1.000 11.41049 ? 45  LEU   B CD2 1 
ATOM   2386 N  N   . PRO   B 1 50  ? 10.84060 -33.92908 27.42314  1.000 12.64902 ? 46  PRO   B N   1 
ATOM   2387 C  CA  . PRO   B 1 50  ? 10.02871 -35.07333 27.84988  1.000 13.47529 ? 46  PRO   B CA  1 
ATOM   2388 C  C   . PRO   B 1 50  ? 10.86402 -36.33130 28.03685  1.000 13.76973 ? 46  PRO   B C   1 
ATOM   2389 O  O   . PRO   B 1 50  ? 11.86412 -36.55448 27.34769  1.000 15.79976 ? 46  PRO   B O   1 
ATOM   2390 C  CB  . PRO   B 1 50  ? 9.02131  -35.23971 26.70640  1.000 23.77121 ? 46  PRO   B CB  1 
ATOM   2391 C  CG  . PRO   B 1 50  ? 8.92748  -33.88644 26.09425  1.000 24.55016 ? 46  PRO   B CG  1 
ATOM   2392 C  CD  . PRO   B 1 50  ? 10.30910 -33.31079 26.19528  1.000 15.34807 ? 46  PRO   B CD  1 
ATOM   2393 N  N   . ASN   B 1 51  ? 10.43000 -37.15244 28.99108  1.000 14.86969 ? 47  ASN   B N   1 
ATOM   2394 C  CA  . ASN   B 1 51  ? 11.03965 -38.45168 29.24596  1.000 15.76592 ? 47  ASN   B CA  1 
ATOM   2395 C  C   . ASN   B 1 51  ? 10.68799 -39.41509 28.11605  1.000 17.28950 ? 47  ASN   B C   1 
ATOM   2396 O  O   . ASN   B 1 51  ? 9.50891  -39.66421 27.84344  1.000 15.54413 ? 47  ASN   B O   1 
ATOM   2397 C  CB  . ASN   B 1 51  ? 10.55668 -38.98373 30.59352  1.000 19.49121 ? 47  ASN   B CB  1 
ATOM   2398 C  CG  . ASN   B 1 51  ? 11.17822 -40.32322 30.97004  1.000 18.96846 ? 47  ASN   B CG  1 
ATOM   2399 O  OD1 . ASN   B 1 51  ? 12.05503 -40.84547 30.28105  1.000 19.27957 ? 47  ASN   B OD1 1 
ATOM   2400 N  ND2 . ASN   B 1 51  ? 10.72874 -40.87544 32.08787  1.000 23.57167 ? 47  ASN   B ND2 1 
ATOM   2401 N  N   . ARG   B 1 52  ? 11.72059 -39.95537 27.46638  1.000 14.85577 ? 48  ARG   B N   1 
ATOM   2402 C  CA  . ARG   B 1 52  ? 11.53576 -40.84966 26.32656  1.000 14.97406 ? 48  ARG   B CA  1 
ATOM   2403 C  C   . ARG   B 1 52  ? 10.77658 -42.11863 26.70966  1.000 23.99507 ? 48  ARG   B C   1 
ATOM   2404 O  O   . ARG   B 1 52  ? 10.11017 -42.72413 25.86040  1.000 19.80150 ? 48  ARG   B O   1 
ATOM   2405 C  CB  . ARG   B 1 52  ? 12.91257 -41.19489 25.74849  1.000 20.29827 ? 48  ARG   B CB  1 
ATOM   2406 C  CG  . ARG   B 1 52  ? 12.95652 -41.90059 24.40372  1.000 31.55836 ? 48  ARG   B CG  1 
ATOM   2407 C  CD  . ARG   B 1 52  ? 14.31332 -42.59918 24.24862  1.000 38.83827 ? 48  ARG   B CD  1 
ATOM   2408 N  NE  . ARG   B 1 52  ? 14.99927 -42.29455 22.99699  1.000 48.18489 ? 48  ARG   B NE  1 
ATOM   2409 C  CZ  . ARG   B 1 52  ? 15.89635 -41.32835 22.84279  1.000 51.74593 ? 48  ARG   B CZ  1 
ATOM   2410 N  NH1 . ARG   B 1 52  ? 16.21127 -40.51042 23.83496  1.000 40.01364 ? 48  ARG   B NH1 1 
ATOM   2411 N  NH2 . ARG   B 1 52  ? 16.49342 -41.17925 21.66242  1.000 48.92934 ? 48  ARG   B NH2 1 
ATOM   2412 N  N   . VAL   B 1 53  ? 10.84646 -42.52252 27.97667  1.000 20.20417 ? 49  VAL   B N   1 
ATOM   2413 C  CA  . VAL   B 1 53  ? 10.34099 -43.82250 28.41398  1.000 19.56546 ? 49  VAL   B CA  1 
ATOM   2414 C  C   . VAL   B 1 53  ? 8.81464  -43.77898 28.44755  1.000 27.80385 ? 49  VAL   B C   1 
ATOM   2415 O  O   . VAL   B 1 53  ? 8.22052  -43.07067 29.26474  1.000 28.36141 ? 49  VAL   B O   1 
ATOM   2416 C  CB  . VAL   B 1 53  ? 10.91732 -44.21425 29.77853  1.000 25.02484 ? 49  VAL   B CB  1 
ATOM   2417 C  CG1 . VAL   B 1 53  ? 10.39726 -45.57635 30.19705  1.000 25.57363 ? 49  VAL   B CG1 1 
ATOM   2418 C  CG2 . VAL   B 1 53  ? 12.43846 -44.21116 29.72422  1.000 24.13240 ? 49  VAL   B CG2 1 
ATOM   2419 N  N   . GLY   B 1 54  ? 8.17767  -44.54711 27.56318  1.000 33.76408 ? 50  GLY   B N   1 
ATOM   2420 C  CA  . GLY   B 1 54  ? 6.73275  -44.59355 27.47386  1.000 36.55059 ? 50  GLY   B CA  1 
ATOM   2421 C  C   . GLY   B 1 54  ? 6.08896  -43.43114 26.74903  1.000 33.71177 ? 50  GLY   B C   1 
ATOM   2422 O  O   . GLY   B 1 54  ? 4.85422  -43.36175 26.70178  1.000 32.62494 ? 50  GLY   B O   1 
ATOM   2423 N  N   . LEU   B 1 55  ? 6.87258  -42.52150 26.19104  1.000 19.13920 ? 51  LEU   B N   1 
ATOM   2424 C  CA  . LEU   B 1 55  ? 6.32024  -41.36381 25.49187  1.000 24.57091 ? 51  LEU   B CA  1 
ATOM   2425 C  C   . LEU   B 1 55  ? 5.59096  -41.82264 24.23706  1.000 24.50404 ? 51  LEU   B C   1 
ATOM   2426 O  O   . LEU   B 1 55  ? 6.18377  -42.53375 23.41596  1.000 23.47632 ? 51  LEU   B O   1 
ATOM   2427 C  CB  . LEU   B 1 55  ? 7.43538  -40.38408 25.13414  1.000 17.91431 ? 51  LEU   B CB  1 
ATOM   2428 C  CG  . LEU   B 1 55  ? 7.04185  -39.08035 24.42880  1.000 20.17705 ? 51  LEU   B CG  1 
ATOM   2429 C  CD1 . LEU   B 1 55  ? 6.25370  -38.17063 25.36365  1.000 22.31883 ? 51  LEU   B CD1 1 
ATOM   2430 C  CD2 . LEU   B 1 55  ? 8.27355  -38.36709 23.87854  1.000 17.92228 ? 51  LEU   B CD2 1 
ATOM   2431 N  N   . PRO   B 1 56  ? 4.31856  -41.47002 24.05629  1.000 26.67734 ? 52  PRO   B N   1 
ATOM   2432 C  CA  . PRO   B 1 56  ? 3.59271  -41.91946 22.86144  1.000 19.92486 ? 52  PRO   B CA  1 
ATOM   2433 C  C   . PRO   B 1 56  ? 4.23715  -41.40993 21.58224  1.000 20.84419 ? 52  PRO   B C   1 
ATOM   2434 O  O   . PRO   B 1 56  ? 4.75710  -40.29194 21.52339  1.000 14.57316 ? 52  PRO   B O   1 
ATOM   2435 C  CB  . PRO   B 1 56  ? 2.18941  -41.33544 23.05882  1.000 25.40196 ? 52  PRO   B CB  1 
ATOM   2436 C  CG  . PRO   B 1 56  ? 2.05967  -41.19713 24.54944  1.000 25.37333 ? 52  PRO   B CG  1 
ATOM   2437 C  CD  . PRO   B 1 56  ? 3.43050  -40.79958 25.02206  1.000 21.60212 ? 52  PRO   B CD  1 
ATOM   2438 N  N   . ILE   B 1 57  ? 4.18831  -42.25613 20.54870  1.000 20.33477 ? 53  ILE   B N   1 
ATOM   2439 C  CA  . ILE   B 1 57  ? 4.83114  -41.95130 19.27441  1.000 17.84832 ? 53  ILE   B CA  1 
ATOM   2440 C  C   . ILE   B 1 57  ? 4.26102  -40.68006 18.65540  1.000 16.08576 ? 53  ILE   B C   1 
ATOM   2441 O  O   . ILE   B 1 57  ? 4.97450  -39.94279 17.96516  1.000 13.42439 ? 53  ILE   B O   1 
ATOM   2442 C  CB  . ILE   B 1 57  ? 4.69650  -43.16440 18.32839  1.000 19.48478 ? 53  ILE   B CB  1 
ATOM   2443 C  CG1 . ILE   B 1 57  ? 5.37835  -42.89596 16.98518  1.000 21.36273 ? 53  ILE   B CG1 1 
ATOM   2444 C  CG2 . ILE   B 1 57  ? 3.23174  -43.55497 18.14945  1.000 23.04370 ? 53  ILE   B CG2 1 
ATOM   2445 C  CD1 . ILE   B 1 57  ? 6.88403  -42.79216 17.07943  1.000 25.16667 ? 53  ILE   B CD1 1 
ATOM   2446 N  N   . ASN   B 1 58  ? 2.98070  -40.39130 18.89510  1.000 21.46552 ? 54  ASN   B N   1 
ATOM   2447 C  CA  . ASN   B 1 58  ? 2.36716  -39.19735 18.32181  1.000 22.88565 ? 54  ASN   B CA  1 
ATOM   2448 C  C   . ASN   B 1 58  ? 2.87475  -37.90719 18.95341  1.000 19.30711 ? 54  ASN   B C   1 
ATOM   2449 O  O   . ASN   B 1 58  ? 2.56182  -36.82520 18.44425  1.000 21.08309 ? 54  ASN   B O   1 
ATOM   2450 C  CB  . ASN   B 1 58  ? 0.84535  -39.28128 18.45525  1.000 31.19856 ? 54  ASN   B CB  1 
ATOM   2451 C  CG  . ASN   B 1 58  ? 0.41336  -39.90745 19.76443  1.000 35.64966 ? 54  ASN   B CG  1 
ATOM   2452 O  OD1 . ASN   B 1 58  ? 0.57168  -41.11273 19.96872  1.000 58.01809 ? 54  ASN   B OD1 1 
ATOM   2453 N  ND2 . ASN   B 1 58  ? -0.13552 -39.09425 20.66124  1.000 54.90289 ? 54  ASN   B ND2 1 
ATOM   2454 N  N   . GLN   B 1 59  ? 3.64492  -37.99162 20.03764  1.000 13.54849 ? 55  GLN   B N   1 
ATOM   2455 C  CA  . GLN   B 1 59  ? 4.23662  -36.82471 20.67729  1.000 15.98016 ? 55  GLN   B CA  1 
ATOM   2456 C  C   . GLN   B 1 59  ? 5.75692  -36.81720 20.57245  1.000 14.04659 ? 55  GLN   B C   1 
ATOM   2457 O  O   . GLN   B 1 59  ? 6.41256  -36.01412 21.24300  1.000 14.99411 ? 55  GLN   B O   1 
ATOM   2458 C  CB  . GLN   B 1 59  ? 3.81775  -36.76401 22.14585  1.000 15.60107 ? 55  GLN   B CB  1 
ATOM   2459 C  CG  . GLN   B 1 59  ? 2.31690  -36.90526 22.36593  1.000 25.91257 ? 55  GLN   B CG  1 
ATOM   2460 C  CD  . GLN   B 1 59  ? 1.96573  -37.20864 23.81607  1.000 29.93464 ? 55  GLN   B CD  1 
ATOM   2461 O  OE1 . GLN   B 1 59  ? 2.63375  -36.74358 24.74076  1.000 28.79405 ? 55  GLN   B OE1 1 
ATOM   2462 N  NE2 . GLN   B 1 59  ? 0.91844  -38.00096 24.01786  1.000 36.36298 ? 55  GLN   B NE2 1 
ATOM   2463 N  N   . ARG   B 1 60  ? 6.33197  -37.67490 19.72904  1.000 13.51290 ? 56  ARG   B N   1 
ATOM   2464 C  CA  . ARG   B 1 60  ? 7.77026  -37.91251 19.77128  1.000 12.00662 ? 56  ARG   B CA  1 
ATOM   2465 C  C   . ARG   B 1 60  ? 8.56992  -36.91967 18.93032  1.000 11.68429 ? 56  ARG   B C   1 
ATOM   2466 O  O   . ARG   B 1 60  ? 9.75359  -36.68937 19.21903  1.000 9.99019  ? 56  ARG   B O   1 
ATOM   2467 C  CB  . ARG   B 1 60  ? 8.06373  -39.34719 19.31740  1.000 11.77059 ? 56  ARG   B CB  1 
ATOM   2468 C  CG  . ARG   B 1 60  ? 9.53367  -39.72189 19.27951  1.000 11.44850 ? 56  ARG   B CG  1 
ATOM   2469 C  CD  . ARG   B 1 60  ? 10.14157 -39.75119 20.67085  1.000 19.38708 ? 56  ARG   B CD  1 
ATOM   2470 N  NE  . ARG   B 1 60  ? 11.56535 -40.06187 20.62696  1.000 20.35101 ? 56  ARG   B NE  1 
ATOM   2471 C  CZ  . ARG   B 1 60  ? 12.06510 -41.29010 20.63047  1.000 26.62306 ? 56  ARG   B CZ  1 
ATOM   2472 N  NH1 . ARG   B 1 60  ? 11.28201 -42.35487 20.69414  1.000 29.66850 ? 56  ARG   B NH1 1 
ATOM   2473 N  NH2 . ARG   B 1 60  ? 13.38341 -41.45414 20.56599  1.000 31.46872 ? 56  ARG   B NH2 1 
ATOM   2474 N  N   . PHE   B 1 61  ? 7.96704  -36.32327 17.89973  1.000 10.61952 ? 57  PHE   B N   1 
ATOM   2475 C  CA  . PHE   B 1 61  ? 8.71554  -35.52366 16.93882  1.000 10.06348 ? 57  PHE   B CA  1 
ATOM   2476 C  C   . PHE   B 1 61  ? 8.06180  -34.16590 16.71381  1.000 9.22621  ? 57  PHE   B C   1 
ATOM   2477 O  O   . PHE   B 1 61  ? 6.85877  -33.98707 16.91769  1.000 10.02885 ? 57  PHE   B O   1 
ATOM   2478 C  CB  . PHE   B 1 61  ? 8.83458  -36.24155 15.58320  1.000 9.36361  ? 57  PHE   B CB  1 
ATOM   2479 C  CG  . PHE   B 1 61  ? 9.49938  -37.57918 15.66112  1.000 9.72502  ? 57  PHE   B CG  1 
ATOM   2480 C  CD1 . PHE   B 1 61  ? 10.86818 -37.67729 15.85397  1.000 9.35785  ? 57  PHE   B CD1 1 
ATOM   2481 C  CD2 . PHE   B 1 61  ? 8.75716  -38.73987 15.52789  1.000 13.01784 ? 57  PHE   B CD2 1 
ATOM   2482 C  CE1 . PHE   B 1 61  ? 11.48322 -38.90733 15.92874  1.000 13.42506 ? 57  PHE   B CE1 1 
ATOM   2483 C  CE2 . PHE   B 1 61  ? 9.36627  -39.97933 15.59657  1.000 15.01776 ? 57  PHE   B CE2 1 
ATOM   2484 C  CZ  . PHE   B 1 61  ? 10.73290 -40.06329 15.79714  1.000 11.43622 ? 57  PHE   B CZ  1 
ATOM   2485 N  N   . ILE   B 1 62  ? 8.88304  -33.20378 16.27952  1.000 8.64273  ? 58  ILE   B N   1 
ATOM   2486 C  CA  . ILE   B 1 62  ? 8.40431  -31.96526 15.68020  1.000 8.54217  ? 58  ILE   B CA  1 
ATOM   2487 C  C   . ILE   B 1 62  ? 9.12206  -31.77952 14.35163  1.000 9.47026  ? 58  ILE   B C   1 
ATOM   2488 O  O   . ILE   B 1 62  ? 10.17072 -32.37619 14.09498  1.000 11.46057 ? 58  ILE   B O   1 
ATOM   2489 C  CB  . ILE   B 1 62  ? 8.61245  -30.71694 16.57429  1.000 8.49172  ? 58  ILE   B CB  1 
ATOM   2490 C  CG1 . ILE   B 1 62  ? 10.10421 -30.43291 16.78295  1.000 10.60602 ? 58  ILE   B CG1 1 
ATOM   2491 C  CG2 . ILE   B 1 62  ? 7.86401  -30.85529 17.89611  1.000 9.06365  ? 58  ILE   B CG2 1 
ATOM   2492 C  CD1 . ILE   B 1 62  ? 10.37021 -29.15465 17.57601  1.000 12.65631 ? 58  ILE   B CD1 1 
ATOM   2493 N  N   . LEU   B 1 63  ? 8.54623  -30.92695 13.50685  1.000 9.74903  ? 59  LEU   B N   1 
ATOM   2494 C  CA  . LEU   B 1 63  ? 9.06499  -30.67207 12.17187  1.000 11.63858 ? 59  LEU   B CA  1 
ATOM   2495 C  C   . LEU   B 1 63  ? 9.47450  -29.21442 12.03860  1.000 7.83822  ? 59  LEU   B C   1 
ATOM   2496 O  O   . LEU   B 1 63  ? 8.77498  -28.31691 12.51528  1.000 10.93210 ? 59  LEU   B O   1 
ATOM   2497 C  CB  . LEU   B 1 63  ? 8.02790  -30.99803 11.09898  1.000 10.02612 ? 59  LEU   B CB  1 
ATOM   2498 C  CG  . LEU   B 1 63  ? 7.41571  -32.39304 11.17904  1.000 14.40161 ? 59  LEU   B CG  1 
ATOM   2499 C  CD1 . LEU   B 1 63  ? 6.35938  -32.55720 10.09493  1.000 10.87535 ? 59  LEU   B CD1 1 
ATOM   2500 C  CD2 . LEU   B 1 63  ? 8.49559  -33.45628 11.06966  1.000 9.22467  ? 59  LEU   B CD2 1 
ATOM   2501 N  N   . VAL   B 1 64  ? 10.60136 -28.98829 11.37223  1.000 7.53310  ? 60  VAL   B N   1 
ATOM   2502 C  CA  . VAL   B 1 64  ? 11.09814 -27.64825 11.08305  1.000 10.05807 ? 60  VAL   B CA  1 
ATOM   2503 C  C   . VAL   B 1 64  ? 11.23752 -27.53012 9.57138   1.000 9.83653  ? 60  VAL   B C   1 
ATOM   2504 O  O   . VAL   B 1 64  ? 12.07975 -28.20252 8.96626   1.000 8.18397  ? 60  VAL   B O   1 
ATOM   2505 C  CB  . VAL   B 1 64  ? 12.42893 -27.36579 11.78955  1.000 13.24587 ? 60  VAL   B CB  1 
ATOM   2506 C  CG1 . VAL   B 1 64  ? 13.08865 -26.13997 11.19915  1.000 16.86812 ? 60  VAL   B CG1 1 
ATOM   2507 C  CG2 . VAL   B 1 64  ? 12.19033 -27.16655 13.27850  1.000 16.98387 ? 60  VAL   B CG2 1 
ATOM   2508 N  N   . GLU   B 1 65  ? 10.42140 -26.67343 8.96231   1.000 12.95203 ? 61  GLU   B N   1 
ATOM   2509 C  CA  . GLU   B 1 65  ? 10.44477 -26.45422 7.52124   1.000 11.24284 ? 61  GLU   B CA  1 
ATOM   2510 C  C   . GLU   B 1 65  ? 11.30235 -25.23195 7.22217   1.000 10.20903 ? 61  GLU   B C   1 
ATOM   2511 O  O   . GLU   B 1 65  ? 10.99759 -24.12533 7.68180   1.000 12.02617 ? 61  GLU   B O   1 
ATOM   2512 C  CB  . GLU   B 1 65  ? 9.02958  -26.27336 6.97318   1.000 17.55416 ? 61  GLU   B CB  1 
ATOM   2513 C  CG  . GLU   B 1 65  ? 8.97717  -25.72470 5.55169   1.000 25.55823 ? 61  GLU   B CG  1 
ATOM   2514 C  CD  . GLU   B 1 65  ? 7.79390  -26.25350 4.76716   1.000 42.40565 ? 61  GLU   B CD  1 
ATOM   2515 O  OE1 . GLU   B 1 65  ? 7.74686  -27.47707 4.51752   1.000 56.49920 ? 61  GLU   B OE1 1 
ATOM   2516 O  OE2 . GLU   B 1 65  ? 6.90776  -25.45042 4.40424   1.000 48.60387 ? 61  GLU   B OE2 1 
ATOM   2517 N  N   . LEU   B 1 66  ? 12.37549 -25.43701 6.46679   1.000 9.42656  ? 62  LEU   B N   1 
ATOM   2518 C  CA  . LEU   B 1 66  ? 13.31731 -24.38279 6.12222   1.000 9.12559  ? 62  LEU   B CA  1 
ATOM   2519 C  C   . LEU   B 1 66  ? 13.15838 -24.02534 4.65208   1.000 11.74057 ? 62  LEU   B C   1 
ATOM   2520 O  O   . LEU   B 1 66  ? 13.09510 -24.91523 3.80014   1.000 11.88047 ? 62  LEU   B O   1 
ATOM   2521 C  CB  . LEU   B 1 66  ? 14.75271 -24.82835 6.39719   1.000 8.24478  ? 62  LEU   B CB  1 
ATOM   2522 C  CG  . LEU   B 1 66  ? 15.05597 -25.20473 7.84443   1.000 10.14589 ? 62  LEU   B CG  1 
ATOM   2523 C  CD1 . LEU   B 1 66  ? 16.50187 -25.64886 7.96950   1.000 10.10598 ? 62  LEU   B CD1 1 
ATOM   2524 C  CD2 . LEU   B 1 66  ? 14.75893 -24.01283 8.75887   1.000 11.13908 ? 62  LEU   B CD2 1 
ATOM   2525 N  N   . SER   B 1 67  ? 13.09403 -22.72800 4.36237   1.000 11.39444 ? 63  SER   B N   1 
ATOM   2526 C  CA  . SER   B 1 67  ? 13.04618 -22.21992 2.99841   1.000 12.52261 ? 63  SER   B CA  1 
ATOM   2527 C  C   . SER   B 1 67  ? 14.12141 -21.15189 2.83347   1.000 14.96028 ? 63  SER   B C   1 
ATOM   2528 O  O   . SER   B 1 67  ? 14.59748 -20.57536 3.81219   1.000 11.36842 ? 63  SER   B O   1 
ATOM   2529 C  CB  . SER   B 1 67  ? 11.66359 -21.64087 2.66830   1.000 16.20648 ? 63  SER   B CB  1 
ATOM   2530 O  OG  . SER   B 1 67  ? 10.63779 -22.56460 2.99619   1.000 23.75785 ? 63  SER   B OG  1 
ATOM   2531 N  N   . ASN   B 1 68  ? 14.50645 -20.88091 1.58754   1.000 11.52704 ? 64  ASN   B N   1 
ATOM   2532 C  CA  . ASN   B 1 68  ? 15.58930 -19.93143 1.33723   1.000 12.37629 ? 64  ASN   B CA  1 
ATOM   2533 C  C   . ASN   B 1 68  ? 15.20714 -19.02741 0.16447   1.000 15.88782 ? 64  ASN   B C   1 
ATOM   2534 O  O   . ASN   B 1 68  ? 14.08378 -19.08559 -0.34664  1.000 13.51670 ? 64  ASN   B O   1 
ATOM   2535 C  CB  . ASN   B 1 68  ? 16.91575 -20.67636 1.12535   1.000 11.78491 ? 64  ASN   B CB  1 
ATOM   2536 C  CG  . ASN   B 1 68  ? 16.91225 -21.57270 -0.10125  1.000 12.13066 ? 64  ASN   B CG  1 
ATOM   2537 O  OD1 . ASN   B 1 68  ? 15.97482 -21.57055 -0.90136  1.000 12.54174 ? 64  ASN   B OD1 1 
ATOM   2538 N  ND2 . ASN   B 1 68  ? 17.98180 -22.34125 -0.25789  1.000 14.68463 ? 64  ASN   B ND2 1 
ATOM   2539 N  N   . HIS   B 1 69  ? 16.15343 -18.16797 -0.24677  1.000 14.64365 ? 65  HIS   B N   1 
ATOM   2540 C  CA  . HIS   B 1 69  ? 15.89510 -17.21582 -1.32860  1.000 17.92753 ? 65  HIS   B CA  1 
ATOM   2541 C  C   . HIS   B 1 69  ? 15.58392 -17.91827 -2.64060  1.000 20.75270 ? 65  HIS   B C   1 
ATOM   2542 O  O   . HIS   B 1 69  ? 14.79625 -17.40742 -3.44536  1.000 19.56108 ? 65  HIS   B O   1 
ATOM   2543 C  CB  . HIS   B 1 69  ? 17.09265 -16.28635 -1.54192  1.000 19.38070 ? 65  HIS   B CB  1 
ATOM   2544 C  CG  . HIS   B 1 69  ? 17.21302 -15.19220 -0.52848  1.000 16.00426 ? 65  HIS   B CG  1 
ATOM   2545 N  ND1 . HIS   B 1 69  ? 17.94861 -15.32896 0.62857   1.000 27.07841 ? 65  HIS   B ND1 1 
ATOM   2546 C  CD2 . HIS   B 1 69  ? 16.71070 -13.93550 -0.50884  1.000 21.01136 ? 65  HIS   B CD2 1 
ATOM   2547 C  CE1 . HIS   B 1 69  ? 17.89066 -14.20503 1.31974   1.000 24.37610 ? 65  HIS   B CE1 1 
ATOM   2548 N  NE2 . HIS   B 1 69  ? 17.14451 -13.34382 0.65257   1.000 19.96231 ? 65  HIS   B NE2 1 
ATOM   2549 N  N   . ALA   B 1 70  ? 16.21325 -19.06621 -2.89185  1.000 15.04246 ? 66  ALA   B N   1 
ATOM   2550 C  CA  . ALA   B 1 70  ? 15.91187 -19.83552 -4.09281  1.000 15.51390 ? 66  ALA   B CA  1 
ATOM   2551 C  C   . ALA   B 1 70  ? 14.53256 -20.47358 -4.03995  1.000 20.68913 ? 66  ALA   B C   1 
ATOM   2552 O  O   . ALA   B 1 70  ? 14.13859 -21.13234 -5.00794  1.000 17.27753 ? 66  ALA   B O   1 
ATOM   2553 C  CB  . ALA   B 1 70  ? 16.98031 -20.90840 -4.30645  1.000 18.08174 ? 66  ALA   B CB  1 
ATOM   2554 N  N   . GLU   B 1 71  ? 13.81226 -20.29387 -2.92962  1.000 14.57813 ? 67  GLU   B N   1 
ATOM   2555 C  CA  . GLU   B 1 71  ? 12.45614 -20.80594 -2.73141  1.000 14.39934 ? 67  GLU   B CA  1 
ATOM   2556 C  C   . GLU   B 1 71  ? 12.41747 -22.32908 -2.77796  1.000 20.61606 ? 67  GLU   B C   1 
ATOM   2557 O  O   . GLU   B 1 71  ? 11.41863 -22.92961 -3.18323  1.000 18.70963 ? 67  GLU   B O   1 
ATOM   2558 C  CB  . GLU   B 1 71  ? 11.47014 -20.18912 -3.72667  1.000 19.75014 ? 67  GLU   B CB  1 
ATOM   2559 C  CG  . GLU   B 1 71  ? 11.21302 -18.70059 -3.44838  1.000 21.66267 ? 67  GLU   B CG  1 
ATOM   2560 C  CD  . GLU   B 1 71  ? 10.26597 -18.05377 -4.44351  1.000 45.04080 ? 67  GLU   B CD  1 
ATOM   2561 O  OE1 . GLU   B 1 71  ? 9.61438  -18.78708 -5.21774  1.000 32.03802 ? 67  GLU   B OE1 1 
ATOM   2562 O  OE2 . GLU   B 1 71  ? 10.17866 -16.80523 -4.45352  1.000 46.51658 ? 67  GLU   B OE2 1 
ATOM   2563 N  N   . LEU   B 1 72  ? 13.51174 -22.95081 -2.35605  1.000 14.27173 ? 68  LEU   B N   1 
ATOM   2564 C  CA  . LEU   B 1 72  ? 13.54420 -24.37197 -2.05419  1.000 12.46622 ? 68  LEU   B CA  1 
ATOM   2565 C  C   . LEU   B 1 72  ? 13.20018 -24.58267 -0.58618  1.000 16.42984 ? 68  LEU   B C   1 
ATOM   2566 O  O   . LEU   B 1 72  ? 13.50544 -23.74274 0.26484   1.000 13.09540 ? 68  LEU   B O   1 
ATOM   2567 C  CB  . LEU   B 1 72  ? 14.92325 -24.95357 -2.35634  1.000 13.12312 ? 68  LEU   B CB  1 
ATOM   2568 C  CG  . LEU   B 1 72  ? 15.40448 -24.74332 -3.79242  1.000 18.73688 ? 68  LEU   B CG  1 
ATOM   2569 C  CD1 . LEU   B 1 72  ? 16.85494 -25.17575 -3.95029  1.000 15.72924 ? 68  LEU   B CD1 1 
ATOM   2570 C  CD2 . LEU   B 1 72  ? 14.49807 -25.49435 -4.75379  1.000 23.53392 ? 68  LEU   B CD2 1 
ATOM   2571 N  N   . SER   B 1 73  ? 12.55659 -25.71215 -0.29463  1.000 15.98512 ? 69  SER   B N   1 
ATOM   2572 C  CA  . SER   B 1 73  ? 12.14634 -26.04439 1.06240   1.000 12.91217 ? 69  SER   B CA  1 
ATOM   2573 C  C   . SER   B 1 73  ? 12.59382 -27.45292 1.41839   1.000 14.82585 ? 69  SER   B C   1 
ATOM   2574 O  O   . SER   B 1 73  ? 12.52752 -28.36392 0.58946   1.000 11.83827 ? 69  SER   B O   1 
ATOM   2575 C  CB  . SER   B 1 73  ? 10.62248 -25.93169 1.23704   1.000 15.24190 ? 69  SER   B CB  1 
ATOM   2576 O  OG  . SER   B 1 73  ? 10.20348 -24.57860 1.17582   1.000 30.89417 ? 69  SER   B OG  1 
ATOM   2577 N  N   . VAL   B 1 74  ? 13.04846 -27.62621 2.65723   1.000 9.66444  ? 70  VAL   B N   1 
ATOM   2578 C  CA  . VAL   B 1 74  ? 13.32531 -28.94180 3.21669   1.000 8.95790  ? 70  VAL   B CA  1 
ATOM   2579 C  C   . VAL   B 1 74  ? 12.69385 -28.98343 4.60008   1.000 10.17822 ? 70  VAL   B C   1 
ATOM   2580 O  O   . VAL   B 1 74  ? 12.52872 -27.94904 5.25280   1.000 9.67987  ? 70  VAL   B O   1 
ATOM   2581 C  CB  . VAL   B 1 74  ? 14.84167 -29.25823 3.29428   1.000 12.99918 ? 70  VAL   B CB  1 
ATOM   2582 C  CG1 . VAL   B 1 74  ? 15.45756 -29.31082 1.90140   1.000 10.52039 ? 70  VAL   B CG1 1 
ATOM   2583 C  CG2 . VAL   B 1 74  ? 15.56381 -28.23773 4.16160   1.000 9.07233  ? 70  VAL   B CG2 1 
ATOM   2584 N  N   . THR   B 1 75  ? 12.32155 -30.18105 5.04555   1.000 8.41093  ? 71  THR   B N   1 
ATOM   2585 C  CA  . THR   B 1 75  ? 11.69394 -30.34513 6.35354   1.000 9.03813  ? 71  THR   B CA  1 
ATOM   2586 C  C   . THR   B 1 75  ? 12.55117 -31.24795 7.22445   1.000 7.80243  ? 71  THR   B C   1 
ATOM   2587 O  O   . THR   B 1 75  ? 12.72433 -32.43140 6.91799   1.000 8.75462  ? 71  THR   B O   1 
ATOM   2588 C  CB  . THR   B 1 75  ? 10.27823 -30.91195 6.24008   1.000 10.29793 ? 71  THR   B CB  1 
ATOM   2589 O  OG1 . THR   B 1 75  ? 9.47286  -30.02376 5.45896   1.000 17.36655 ? 71  THR   B OG1 1 
ATOM   2590 C  CG2 . THR   B 1 75  ? 9.65700  -31.02692 7.62602   1.000 8.36944  ? 71  THR   B CG2 1 
ATOM   2591 N  N   . LEU   B 1 76  ? 13.06809 -30.68778 8.31479   1.000 10.97125 ? 72  LEU   B N   1 
ATOM   2592 C  CA  . LEU   B 1 76  ? 13.83274 -31.43430 9.29985   1.000 12.07226 ? 72  LEU   B CA  1 
ATOM   2593 C  C   . LEU   B 1 76  ? 12.88151 -32.02333 10.32688  1.000 14.79166 ? 72  LEU   B C   1 
ATOM   2594 O  O   . LEU   B 1 76  ? 11.88286 -31.39539 10.68349  1.000 7.73817  ? 72  LEU   B O   1 
ATOM   2595 C  CB  . LEU   B 1 76  ? 14.84708 -30.52627 9.99634   1.000 8.05156  ? 72  LEU   B CB  1 
ATOM   2596 C  CG  . LEU   B 1 76  ? 16.26711 -30.39603 9.44036   1.000 16.41349 ? 72  LEU   B CG  1 
ATOM   2597 C  CD1 . LEU   B 1 76  ? 16.27368 -30.33439 7.93659   1.000 10.89726 ? 72  LEU   B CD1 1 
ATOM   2598 C  CD2 . LEU   B 1 76  ? 16.92589 -29.15250 10.02107  1.000 23.97423 ? 72  LEU   B CD2 1 
ATOM   2599 N  N   . ALA   B 1 77  ? 13.18516 -33.23726 10.78657  1.000 8.30656  ? 73  ALA   B N   1 
ATOM   2600 C  CA  . ALA   B 1 77  ? 12.44988 -33.86748 11.87455  1.000 9.85850  ? 73  ALA   B CA  1 
ATOM   2601 C  C   . ALA   B 1 77  ? 13.32391 -33.86894 13.11888  1.000 12.62211 ? 73  ALA   B C   1 
ATOM   2602 O  O   . ALA   B 1 77  ? 14.48276 -34.29173 13.06394  1.000 8.60625  ? 73  ALA   B O   1 
ATOM   2603 C  CB  . ALA   B 1 77  ? 12.03529 -35.29725 11.51717  1.000 14.15218 ? 73  ALA   B CB  1 
ATOM   2604 N  N   . LEU   B 1 78  ? 12.77149 -33.39068 14.22868  1.000 9.00397  ? 74  LEU   B N   1 
ATOM   2605 C  CA  . LEU   B 1 78  ? 13.48768 -33.29340 15.49299  1.000 9.33224  ? 74  LEU   B CA  1 
ATOM   2606 C  C   . LEU   B 1 78  ? 12.86740 -34.22906 16.51967  1.000 12.45323 ? 74  LEU   B C   1 
ATOM   2607 O  O   . LEU   B 1 78  ? 11.64133 -34.31744 16.63010  1.000 9.91470  ? 74  LEU   B O   1 
ATOM   2608 C  CB  . LEU   B 1 78  ? 13.47080 -31.85859 16.03903  1.000 10.02961 ? 74  LEU   B CB  1 
ATOM   2609 C  CG  . LEU   B 1 78  ? 14.60031 -30.90730 15.62572  1.000 11.24301 ? 74  LEU   B CG  1 
ATOM   2610 C  CD1 . LEU   B 1 78  ? 14.67754 -30.76359 14.12001  1.000 17.78664 ? 74  LEU   B CD1 1 
ATOM   2611 C  CD2 . LEU   B 1 78  ? 14.40623 -29.54555 16.28922  1.000 13.01017 ? 74  LEU   B CD2 1 
ATOM   2612 N  N   . ASP   B 1 79  ? 13.72720 -34.90944 17.27472  1.000 8.09439  ? 75  ASP   B N   1 
ATOM   2613 C  CA  . ASP   B 1 79  ? 13.30557 -35.77693 18.36934  1.000 10.54094 ? 75  ASP   B CA  1 
ATOM   2614 C  C   . ASP   B 1 79  ? 13.12098 -34.91302 19.61221  1.000 14.35171 ? 75  ASP   B C   1 
ATOM   2615 O  O   . ASP   B 1 79  ? 14.06268 -34.24745 20.04735  1.000 11.58675 ? 75  ASP   B O   1 
ATOM   2616 C  CB  . ASP   B 1 79  ? 14.36117 -36.86282 18.58802  1.000 11.47873 ? 75  ASP   B CB  1 
ATOM   2617 C  CG  . ASP   B 1 79  ? 13.94967 -37.91756 19.60828  1.000 22.89445 ? 75  ASP   B CG  1 
ATOM   2618 O  OD1 . ASP   B 1 79  ? 13.10423 -37.64465 20.48467  1.000 15.63639 ? 75  ASP   B OD1 1 
ATOM   2619 O  OD2 . ASP   B 1 79  ? 14.49752 -39.03787 19.53187  1.000 22.30572 ? 75  ASP   B OD2 1 
ATOM   2620 N  N   . VAL   B 1 80  ? 11.90738 -34.89878 20.17286  1.000 12.65433 ? 76  VAL   B N   1 
ATOM   2621 C  CA  . VAL   B 1 80  ? 11.63508 -33.98417 21.27781  1.000 11.20988 ? 76  VAL   B CA  1 
ATOM   2622 C  C   . VAL   B 1 80  ? 12.39709 -34.36565 22.53870  1.000 11.06362 ? 76  VAL   B C   1 
ATOM   2623 O  O   . VAL   B 1 80  ? 12.58442 -33.51807 23.41956  1.000 11.55631 ? 76  VAL   B O   1 
ATOM   2624 C  CB  . VAL   B 1 80  ? 10.12603 -33.90436 21.58355  1.000 10.40152 ? 76  VAL   B CB  1 
ATOM   2625 C  CG1 . VAL   B 1 80  ? 9.35563  -33.43003 20.35849  1.000 9.80885  ? 76  VAL   B CG1 1 
ATOM   2626 C  CG2 . VAL   B 1 80  ? 9.60479  -35.25150 22.08220  1.000 14.75378 ? 76  VAL   B CG2 1 
ATOM   2627 N  N   . THR   B 1 81  ? 12.85484 -35.61490 22.65210  1.000 15.01154 ? 77  THR   B N   1 
ATOM   2628 C  CA  . THR   B 1 81  ? 13.51908 -36.04572 23.87676  1.000 12.50422 ? 77  THR   B CA  1 
ATOM   2629 C  C   . THR   B 1 81  ? 14.95098 -35.53951 23.98800  1.000 12.79151 ? 77  THR   B C   1 
ATOM   2630 O  O   . THR   B 1 81  ? 15.47299 -35.45552 25.10490  1.000 13.83130 ? 77  THR   B O   1 
ATOM   2631 C  CB  . THR   B 1 81  ? 13.51036 -37.57223 23.98519  1.000 13.04308 ? 77  THR   B CB  1 
ATOM   2632 O  OG1 . THR   B 1 81  ? 14.25338 -38.13719 22.89874  1.000 17.15156 ? 77  THR   B OG1 1 
ATOM   2633 C  CG2 . THR   B 1 81  ? 12.08250 -38.09621 23.95138  1.000 13.01506 ? 77  THR   B CG2 1 
ATOM   2634 N  N   . ASN   B 1 82  ? 15.59883 -35.20447 22.86812  1.000 12.05921 ? 78  ASN   B N   1 
ATOM   2635 C  CA  . ASN   B 1 82  ? 16.93513 -34.62310 22.91356  1.000 13.02693 ? 78  ASN   B CA  1 
ATOM   2636 C  C   . ASN   B 1 82  ? 17.10596 -33.43902 21.96315  1.000 14.05871 ? 78  ASN   B C   1 
ATOM   2637 O  O   . ASN   B 1 82  ? 18.23008 -32.93176 21.83139  1.000 13.53226 ? 78  ASN   B O   1 
ATOM   2638 C  CB  . ASN   B 1 82  ? 17.99939 -35.68498 22.61432  1.000 12.84156 ? 78  ASN   B CB  1 
ATOM   2639 C  CG  . ASN   B 1 82  ? 17.76042 -36.40225 21.30116  1.000 20.79277 ? 78  ASN   B CG  1 
ATOM   2640 O  OD1 . ASN   B 1 82  ? 16.92826 -35.98807 20.49238  1.000 15.40879 ? 78  ASN   B OD1 1 
ATOM   2641 N  ND2 . ASN   B 1 82  ? 18.49758 -37.48552 21.07927  1.000 26.87683 ? 78  ASN   B ND2 1 
ATOM   2642 N  N   . ALA   B 1 83  ? 16.03610 -32.98996 21.30058  1.000 13.92220 ? 79  ALA   B N   1 
ATOM   2643 C  CA  . ALA   B 1 83  ? 16.02857 -31.81973 20.41364  1.000 12.94589 ? 79  ALA   B CA  1 
ATOM   2644 C  C   . ALA   B 1 83  ? 16.94760 -31.98095 19.20936  1.000 19.89972 ? 79  ALA   B C   1 
ATOM   2645 O  O   . ALA   B 1 83  ? 17.28118 -30.99621 18.54140  1.000 24.60401 ? 79  ALA   B O   1 
ATOM   2646 C  CB  . ALA   B 1 83  ? 16.38811 -30.53613 21.16984  1.000 17.46843 ? 79  ALA   B CB  1 
ATOM   2647 N  N   . TYR   B 1 84  ? 17.35308 -33.19974 18.89021  1.000 17.21572 ? 80  TYR   B N   1 
ATOM   2648 C  CA  . TYR   B 1 84  ? 18.30335 -33.40975 17.81223  1.000 18.43994 ? 80  TYR   B CA  1 
ATOM   2649 C  C   . TYR   B 1 84  ? 17.59825 -33.84427 16.53483  1.000 12.83591 ? 80  TYR   B C   1 
ATOM   2650 O  O   . TYR   B 1 84  ? 16.51691 -34.44057 16.56195  1.000 10.27144 ? 80  TYR   B O   1 
ATOM   2651 C  CB  . TYR   B 1 84  ? 19.34760 -34.44742 18.20963  1.000 19.76213 ? 80  TYR   B CB  1 
ATOM   2652 C  CG  . TYR   B 1 84  ? 20.70871 -34.21894 17.59101  1.000 18.15497 ? 80  TYR   B CG  1 
ATOM   2653 C  CD1 . TYR   B 1 84  ? 21.61996 -33.34964 18.17448  1.000 22.55629 ? 80  TYR   B CD1 1 
ATOM   2654 C  CD2 . TYR   B 1 84  ? 21.08488 -34.88378 16.43065  1.000 21.05647 ? 80  TYR   B CD2 1 
ATOM   2655 C  CE1 . TYR   B 1 84  ? 22.87292 -33.14710 17.61822  1.000 21.85738 ? 80  TYR   B CE1 1 
ATOM   2656 C  CE2 . TYR   B 1 84  ? 22.33069 -34.68810 15.86696  1.000 18.17051 ? 80  TYR   B CE2 1 
ATOM   2657 C  CZ  . TYR   B 1 84  ? 23.22336 -33.82242 16.46432  1.000 17.94300 ? 80  TYR   B CZ  1 
ATOM   2658 O  OH  . TYR   B 1 84  ? 24.46615 -33.62709 15.90203  1.000 25.15511 ? 80  TYR   B OH  1 
ATOM   2659 N  N   . VAL   B 1 85  ? 18.24025 -33.53583 15.40965  1.000 13.85935 ? 81  VAL   B N   1 
ATOM   2660 C  CA  . VAL   B 1 85  ? 17.71530 -33.89673 14.10113  1.000 9.21688  ? 81  VAL   B CA  1 
ATOM   2661 C  C   . VAL   B 1 85  ? 17.89958 -35.38969 13.87426  1.000 12.32273 ? 81  VAL   B C   1 
ATOM   2662 O  O   . VAL   B 1 85  ? 18.99703 -35.92859 14.06469  1.000 15.59538 ? 81  VAL   B O   1 
ATOM   2663 C  CB  . VAL   B 1 85  ? 18.42402 -33.08845 13.00566  1.000 9.30500  ? 81  VAL   B CB  1 
ATOM   2664 C  CG1 . VAL   B 1 85  ? 17.92286 -33.51626 11.62626  1.000 7.97319  ? 81  VAL   B CG1 1 
ATOM   2665 C  CG2 . VAL   B 1 85  ? 18.23097 -31.59599 13.23358  1.000 11.82789 ? 81  VAL   B CG2 1 
ATOM   2666 N  N   . VAL   B 1 86  ? 16.82898 -36.06383 13.45206  1.000 8.33658  ? 82  VAL   B N   1 
ATOM   2667 C  CA  . VAL   B 1 86  ? 16.89202 -37.48441 13.11815  1.000 10.93748 ? 82  VAL   B CA  1 
ATOM   2668 C  C   . VAL   B 1 86  ? 16.81058 -37.74446 11.62048  1.000 12.57895 ? 82  VAL   B C   1 
ATOM   2669 O  O   . VAL   B 1 86  ? 17.11083 -38.86932 11.18633  1.000 9.97276  ? 82  VAL   B O   1 
ATOM   2670 C  CB  . VAL   B 1 86  ? 15.79749 -38.28751 13.85290  1.000 16.10342 ? 82  VAL   B CB  1 
ATOM   2671 C  CG1 . VAL   B 1 86  ? 15.95865 -38.14300 15.36568  1.000 13.47437 ? 82  VAL   B CG1 1 
ATOM   2672 C  CG2 . VAL   B 1 86  ? 14.40804 -37.84817 13.40622  1.000 9.25745  ? 82  VAL   B CG2 1 
ATOM   2673 N  N   . GLY   B 1 87  ? 16.43402 -36.75677 10.82112  1.000 6.77117  ? 83  GLY   B N   1 
ATOM   2674 C  CA  . GLY   B 1 87  ? 16.29353 -36.96065 9.39343   1.000 8.77204  ? 83  GLY   B CA  1 
ATOM   2675 C  C   . GLY   B 1 87  ? 15.64090 -35.75105 8.76426   1.000 8.03149  ? 83  GLY   B C   1 
ATOM   2676 O  O   . GLY   B 1 87  ? 15.33022 -34.76879 9.44023   1.000 9.18902  ? 83  GLY   B O   1 
ATOM   2677 N  N   . TYR   B 1 88  ? 15.43463 -35.83607 7.44801   1.000 6.30526  ? 84  TYR   B N   1 
ATOM   2678 C  CA  . TYR   B 1 88  ? 14.79302 -34.72679 6.74877   1.000 6.37544  ? 84  TYR   B CA  1 
ATOM   2679 C  C   . TYR   B 1 88  ? 14.12692 -35.21991 5.47579   1.000 7.09204  ? 84  TYR   B C   1 
ATOM   2680 O  O   . TYR   B 1 88  ? 14.43480 -36.30158 4.97030   1.000 6.66511  ? 84  TYR   B O   1 
ATOM   2681 C  CB  . TYR   B 1 88  ? 15.78479 -33.60562 6.42140   1.000 6.43217  ? 84  TYR   B CB  1 
ATOM   2682 C  CG  . TYR   B 1 88  ? 16.64139 -33.81537 5.19423   1.000 11.71231 ? 84  TYR   B CG  1 
ATOM   2683 C  CD1 . TYR   B 1 88  ? 17.76968 -34.62037 5.23772   1.000 6.43501  ? 84  TYR   B CD1 1 
ATOM   2684 C  CD2 . TYR   B 1 88  ? 16.33633 -33.17758 3.99430   1.000 12.19665 ? 84  TYR   B CD2 1 
ATOM   2685 C  CE1 . TYR   B 1 88  ? 18.56477 -34.79933 4.12106   1.000 8.96991  ? 84  TYR   B CE1 1 
ATOM   2686 C  CE2 . TYR   B 1 88  ? 17.12549 -33.35107 2.87072   1.000 9.25452  ? 84  TYR   B CE2 1 
ATOM   2687 C  CZ  . TYR   B 1 88  ? 18.23848 -34.15734 2.94095   1.000 8.40675  ? 84  TYR   B CZ  1 
ATOM   2688 O  OH  . TYR   B 1 88  ? 19.02560 -34.32718 1.83097   1.000 10.82191 ? 84  TYR   B OH  1 
ATOM   2689 N  N   . ARG   B 1 89  ? 13.20787 -34.39385 4.96561   1.000 7.97585  ? 85  ARG   B N   1 
ATOM   2690 C  CA  . ARG   B 1 89  ? 12.49230 -34.65168 3.72526   1.000 7.22308  ? 85  ARG   B CA  1 
ATOM   2691 C  C   . ARG   B 1 89  ? 12.82439 -33.56910 2.71098   1.000 7.74537  ? 85  ARG   B C   1 
ATOM   2692 O  O   . ARG   B 1 89  ? 12.80579 -32.37558 3.03388   1.000 7.65953  ? 85  ARG   B O   1 
ATOM   2693 C  CB  . ARG   B 1 89  ? 10.97694 -34.70530 3.94297   1.000 7.67190  ? 85  ARG   B CB  1 
ATOM   2694 C  CG  . ARG   B 1 89  ? 10.17208 -34.84272 2.64414   1.000 13.65455 ? 85  ARG   B CG  1 
ATOM   2695 C  CD  . ARG   B 1 89  ? 8.67126  -34.84765 2.90105   1.000 17.86208 ? 85  ARG   B CD  1 
ATOM   2696 N  NE  . ARG   B 1 89  ? 7.93081  -34.33594 1.75432   1.000 38.54250 ? 85  ARG   B NE  1 
ATOM   2697 C  CZ  . ARG   B 1 89  ? 7.25169  -35.08463 0.89586   1.000 46.26779 ? 85  ARG   B CZ  1 
ATOM   2698 N  NH1 . ARG   B 1 89  ? 7.16691  -36.39687 1.03765   1.000 46.32711 ? 85  ARG   B NH1 1 
ATOM   2699 N  NH2 . ARG   B 1 89  ? 6.63873  -34.50030 -0.13027  1.000 44.09035 ? 85  ARG   B NH2 1 
ATOM   2700 N  N   . ALA   B 1 90  ? 13.12049 -33.99133 1.48573   1.000 8.58771  ? 86  ALA   B N   1 
ATOM   2701 C  CA  . ALA   B 1 90  ? 13.31087 -33.08867 0.35643   1.000 10.95722 ? 86  ALA   B CA  1 
ATOM   2702 C  C   . ALA   B 1 90  ? 12.56032 -33.66705 -0.83259  1.000 11.33197 ? 86  ALA   B C   1 
ATOM   2703 O  O   . ALA   B 1 90  ? 12.91182 -34.74579 -1.31914  1.000 11.44146 ? 86  ALA   B O   1 
ATOM   2704 C  CB  . ALA   B 1 90  ? 14.79318 -32.91455 0.02366   1.000 14.19472 ? 86  ALA   B CB  1 
ATOM   2705 N  N   . GLY   B 1 91  ? 11.52842 -32.96182 -1.29080  1.000 17.24418 ? 87  GLY   B N   1 
ATOM   2706 C  CA  . GLY   B 1 91  ? 10.78453 -33.43835 -2.44650  1.000 21.43203 ? 87  GLY   B CA  1 
ATOM   2707 C  C   . GLY   B 1 91  ? 10.17472 -34.80001 -2.17194  1.000 17.37844 ? 87  GLY   B C   1 
ATOM   2708 O  O   . GLY   B 1 91  ? 9.46444  -34.99918 -1.18060  1.000 20.84982 ? 87  GLY   B O   1 
ATOM   2709 N  N   . ASN   B 1 92  ? 10.47326 -35.76297 -3.04557  1.000 15.73692 ? 88  ASN   B N   1 
ATOM   2710 C  CA  . ASN   B 1 92  ? 9.92288  -37.10922 -2.95800  1.000 15.40597 ? 88  ASN   B CA  1 
ATOM   2711 C  C   . ASN   B 1 92  ? 10.82858 -38.08577 -2.21005  1.000 15.35836 ? 88  ASN   B C   1 
ATOM   2712 O  O   . ASN   B 1 92  ? 10.64815 -39.30082 -2.34887  1.000 12.48847 ? 88  ASN   B O   1 
ATOM   2713 C  CB  . ASN   B 1 92  ? 9.63887  -37.65771 -4.35947  1.000 14.71021 ? 88  ASN   B CB  1 
ATOM   2714 C  CG  . ASN   B 1 92  ? 8.36983  -37.09528 -4.96675  1.000 20.35646 ? 88  ASN   B CG  1 
ATOM   2715 O  OD1 . ASN   B 1 92  ? 7.36381  -36.91762 -4.28343  1.000 26.50095 ? 88  ASN   B OD1 1 
ATOM   2716 N  ND2 . ASN   B 1 92  ? 8.41008  -36.82216 -6.26529  1.000 23.68783 ? 88  ASN   B ND2 1 
ATOM   2717 N  N   . SER   B 1 93  ? 11.79033 -37.59852 -1.42456  1.000 13.03247 ? 89  SER   B N   1 
ATOM   2718 C  CA  . SER   B 1 93  ? 12.68107 -38.48752 -0.69045  1.000 8.40083  ? 89  SER   B CA  1 
ATOM   2719 C  C   . SER   B 1 93  ? 12.85021 -38.00933 0.74312   1.000 13.37444 ? 89  SER   B C   1 
ATOM   2720 O  O   . SER   B 1 93  ? 12.87113 -36.80463 1.00819   1.000 13.10288 ? 89  SER   B O   1 
ATOM   2721 C  CB  . SER   B 1 93  ? 14.06116 -38.59092 -1.35526  1.000 8.26255  ? 89  SER   B CB  1 
ATOM   2722 O  OG  . SER   B 1 93  ? 13.96241 -39.11660 -2.66980  1.000 12.41427 ? 89  SER   B OG  1 
ATOM   2723 N  N   . ALA   B 1 94  ? 12.96949 -38.96478 1.66378   1.000 9.01743  ? 90  ALA   B N   1 
ATOM   2724 C  CA  . ALA   B 1 94  ? 13.34295 -38.68721 3.04416   1.000 7.38849  ? 90  ALA   B CA  1 
ATOM   2725 C  C   . ALA   B 1 94  ? 14.58479 -39.49293 3.39721   1.000 9.43284  ? 90  ALA   B C   1 
ATOM   2726 O  O   . ALA   B 1 94  ? 14.71703 -40.65466 2.99691   1.000 9.88096  ? 90  ALA   B O   1 
ATOM   2727 C  CB  . ALA   B 1 94  ? 12.20663 -39.01420 4.01741   1.000 8.67211  ? 90  ALA   B CB  1 
ATOM   2728 N  N   . TYR   B 1 95  ? 15.48975 -38.86611 4.14424   1.000 6.59994  ? 91  TYR   B N   1 
ATOM   2729 C  CA  . TYR   B 1 95  ? 16.74914 -39.46220 4.56201   1.000 6.78800  ? 91  TYR   B CA  1 
ATOM   2730 C  C   . TYR   B 1 95  ? 16.83232 -39.44145 6.07972   1.000 10.89882 ? 91  TYR   B C   1 
ATOM   2731 O  O   . TYR   B 1 95  ? 16.49218 -38.43637 6.70642   1.000 10.32450 ? 91  TYR   B O   1 
ATOM   2732 C  CB  . TYR   B 1 95  ? 17.93541 -38.70201 3.96903   1.000 6.54014  ? 91  TYR   B CB  1 
ATOM   2733 C  CG  . TYR   B 1 95  ? 17.91596 -38.66245 2.46305   1.000 10.12865 ? 91  TYR   B CG  1 
ATOM   2734 C  CD1 . TYR   B 1 95  ? 17.20161 -37.68554 1.78032   1.000 12.54697 ? 91  TYR   B CD1 1 
ATOM   2735 C  CD2 . TYR   B 1 95  ? 18.59897 -39.61324 1.72397   1.000 11.50366 ? 91  TYR   B CD2 1 
ATOM   2736 C  CE1 . TYR   B 1 95  ? 17.17752 -37.66072 0.39921   1.000 9.89479  ? 91  TYR   B CE1 1 
ATOM   2737 C  CE2 . TYR   B 1 95  ? 18.58454 -39.59037 0.35156   1.000 10.85667 ? 91  TYR   B CE2 1 
ATOM   2738 C  CZ  . TYR   B 1 95  ? 17.87187 -38.61865 -0.30578  1.000 13.89060 ? 91  TYR   B CZ  1 
ATOM   2739 O  OH  . TYR   B 1 95  ? 17.86029 -38.60683 -1.68468  1.000 20.21528 ? 91  TYR   B OH  1 
ATOM   2740 N  N   . PHE   B 1 96  ? 17.29558 -40.54408 6.66647   1.000 6.81674  ? 92  PHE   B N   1 
ATOM   2741 C  CA  . PHE   B 1 96  ? 17.36678 -40.68403 8.11670   1.000 7.03352  ? 92  PHE   B CA  1 
ATOM   2742 C  C   . PHE   B 1 96  ? 18.76055 -41.11691 8.55482   1.000 8.96065  ? 92  PHE   B C   1 
ATOM   2743 O  O   . PHE   B 1 96  ? 19.39460 -41.94802 7.90102   1.000 10.01634 ? 92  PHE   B O   1 
ATOM   2744 C  CB  . PHE   B 1 96  ? 16.33763 -41.70110 8.62220   1.000 10.34886 ? 92  PHE   B CB  1 
ATOM   2745 C  CG  . PHE   B 1 96  ? 14.91708 -41.31464 8.33265   1.000 10.26667 ? 92  PHE   B CG  1 
ATOM   2746 C  CD1 . PHE   B 1 96  ? 14.17441 -40.60715 9.26507   1.000 11.38735 ? 92  PHE   B CD1 1 
ATOM   2747 C  CD2 . PHE   B 1 96  ? 14.32605 -41.65039 7.12593   1.000 12.33561 ? 92  PHE   B CD2 1 
ATOM   2748 C  CE1 . PHE   B 1 96  ? 12.86331 -40.24758 9.00025   1.000 14.59017 ? 92  PHE   B CE1 1 
ATOM   2749 C  CE2 . PHE   B 1 96  ? 13.01764 -41.29521 6.85250   1.000 11.92890 ? 92  PHE   B CE2 1 
ATOM   2750 C  CZ  . PHE   B 1 96  ? 12.28660 -40.58971 7.78863   1.000 14.94703 ? 92  PHE   B CZ  1 
ATOM   2751 N  N   . PHE   B 1 97  ? 19.23168 -40.55578 9.67013   1.000 10.23113 ? 93  PHE   B N   1 
ATOM   2752 C  CA  . PHE   B 1 97  ? 20.46095 -41.04967 10.27334  1.000 8.26536  ? 93  PHE   B CA  1 
ATOM   2753 C  C   . PHE   B 1 97  ? 20.25078 -42.47568 10.76891  1.000 9.19181  ? 93  PHE   B C   1 
ATOM   2754 O  O   . PHE   B 1 97  ? 19.12816 -42.89395 11.06260  1.000 11.40143 ? 93  PHE   B O   1 
ATOM   2755 C  CB  . PHE   B 1 97  ? 20.90242 -40.15349 11.43450  1.000 8.58477  ? 93  PHE   B CB  1 
ATOM   2756 C  CG  . PHE   B 1 97  ? 21.30286 -38.76159 11.02086  1.000 13.15138 ? 93  PHE   B CG  1 
ATOM   2757 C  CD1 . PHE   B 1 97  ? 22.29999 -38.55858 10.08027  1.000 9.34033  ? 93  PHE   B CD1 1 
ATOM   2758 C  CD2 . PHE   B 1 97  ? 20.69892 -37.65704 11.59652  1.000 11.27187 ? 93  PHE   B CD2 1 
ATOM   2759 C  CE1 . PHE   B 1 97  ? 22.67474 -37.28061 9.71268   1.000 17.24328 ? 93  PHE   B CE1 1 
ATOM   2760 C  CE2 . PHE   B 1 97  ? 21.06930 -36.37491 11.23185  1.000 15.56571 ? 93  PHE   B CE2 1 
ATOM   2761 C  CZ  . PHE   B 1 97  ? 22.05743 -36.18666 10.28990  1.000 16.15927 ? 93  PHE   B CZ  1 
ATOM   2762 N  N   . HIS   B 1 98  ? 21.33552 -43.22789 10.85254  1.000 11.27587 ? 94  HIS   B N   1 
ATOM   2763 C  CA  . HIS   B 1 98  ? 21.23432 -44.60258 11.32058  1.000 12.68834 ? 94  HIS   B CA  1 
ATOM   2764 C  C   . HIS   B 1 98  ? 20.73272 -44.61331 12.76105  1.000 17.45732 ? 94  HIS   B C   1 
ATOM   2765 O  O   . HIS   B 1 98  ? 21.36080 -43.99167 13.62970  1.000 11.17972 ? 94  HIS   B O   1 
ATOM   2766 C  CB  . HIS   B 1 98  ? 22.58005 -45.30857 11.22505  1.000 11.12412 ? 94  HIS   B CB  1 
ATOM   2767 C  CG  . HIS   B 1 98  ? 22.52549 -46.75855 11.59522  1.000 19.04381 ? 94  HIS   B CG  1 
ATOM   2768 N  ND1 . HIS   B 1 98  ? 22.85213 -47.21967 12.85312  1.000 24.91608 ? 94  HIS   B ND1 1 
ATOM   2769 C  CD2 . HIS   B 1 98  ? 22.18110 -47.85007 10.87256  1.000 24.58121 ? 94  HIS   B CD2 1 
ATOM   2770 C  CE1 . HIS   B 1 98  ? 22.71232 -48.53291 12.88831  1.000 24.54917 ? 94  HIS   B CE1 1 
ATOM   2771 N  NE2 . HIS   B 1 98  ? 22.30646 -48.94003 11.69897  1.000 23.89398 ? 94  HIS   B NE2 1 
ATOM   2772 N  N   . PRO   B 1 99  ? 19.61655 -45.27661 13.05632  1.000 19.42065 ? 95  PRO   B N   1 
ATOM   2773 C  CA  . PRO   B 1 99  ? 19.11275 -45.27835 14.43464  1.000 18.31288 ? 95  PRO   B CA  1 
ATOM   2774 C  C   . PRO   B 1 99  ? 20.01522 -46.09072 15.35075  1.000 25.18874 ? 95  PRO   B C   1 
ATOM   2775 O  O   . PRO   B 1 99  ? 20.55262 -47.13048 14.96238  1.000 19.83979 ? 95  PRO   B O   1 
ATOM   2776 C  CB  . PRO   B 1 99  ? 17.71893 -45.90572 14.30713  1.000 19.83916 ? 95  PRO   B CB  1 
ATOM   2777 C  CG  . PRO   B 1 99  ? 17.75472 -46.67601 13.02524  1.000 18.37283 ? 95  PRO   B CG  1 
ATOM   2778 C  CD  . PRO   B 1 99  ? 18.69773 -45.94680 12.12103  1.000 14.56927 ? 95  PRO   B CD  1 
ATOM   2779 N  N   . ASP   B 1 100 ? 20.18213 -45.59400 16.58063  1.000 24.31044 ? 96  ASP   B N   1 
ATOM   2780 C  CA  . ASP   B 1 100 ? 21.07663 -46.22978 17.54238  1.000 30.74791 ? 96  ASP   B CA  1 
ATOM   2781 C  C   . ASP   B 1 100 ? 20.50653 -47.52127 18.10665  1.000 32.55571 ? 96  ASP   B C   1 
ATOM   2782 O  O   . ASP   B 1 100 ? 21.26280 -48.34112 18.63555  1.000 34.11259 ? 96  ASP   B O   1 
ATOM   2783 C  CB  . ASP   B 1 100 ? 21.37573 -45.27644 18.70417  1.000 39.35565 ? 96  ASP   B CB  1 
ATOM   2784 C  CG  . ASP   B 1 100 ? 21.80515 -43.89518 18.24125  1.000 50.64181 ? 96  ASP   B CG  1 
ATOM   2785 O  OD1 . ASP   B 1 100 ? 22.56761 -43.79925 17.25734  1.000 58.24880 ? 96  ASP   B OD1 1 
ATOM   2786 O  OD2 . ASP   B 1 100 ? 21.37729 -42.90120 18.86719  1.000 61.63931 ? 96  ASP   B OD2 1 
ATOM   2787 N  N   . ASN   B 1 101 ? 19.19723 -47.71279 18.02813  1.000 23.42680 ? 97  ASN   B N   1 
ATOM   2788 C  CA  . ASN   B 1 101 ? 18.55865 -48.83271 18.69864  1.000 25.27605 ? 97  ASN   B CA  1 
ATOM   2789 C  C   . ASN   B 1 101 ? 17.21037 -49.06848 18.03985  1.000 19.64339 ? 97  ASN   B C   1 
ATOM   2790 O  O   . ASN   B 1 101 ? 16.79207 -48.32540 17.15263  1.000 20.69921 ? 97  ASN   B O   1 
ATOM   2791 C  CB  . ASN   B 1 101 ? 18.43323 -48.56757 20.19946  1.000 26.51575 ? 97  ASN   B CB  1 
ATOM   2792 C  CG  . ASN   B 1 101 ? 17.91037 -47.18122 20.50022  1.000 31.59831 ? 97  ASN   B CG  1 
ATOM   2793 O  OD1 . ASN   B 1 101 ? 16.86802 -46.77333 19.99008  1.000 33.04692 ? 97  ASN   B OD1 1 
ATOM   2794 N  ND2 . ASN   B 1 101 ? 18.64698 -46.43723 21.31720  1.000 37.83514 ? 97  ASN   B ND2 1 
ATOM   2795 N  N   . GLN   B 1 102 ? 16.52744 -50.11459 18.48883  1.000 24.89492 ? 98  GLN   B N   1 
ATOM   2796 C  CA  . GLN   B 1 102 ? 15.43112 -50.64287 17.68550  1.000 20.35368 ? 98  GLN   B CA  1 
ATOM   2797 C  C   . GLN   B 1 102 ? 14.13079 -49.86760 17.88100  1.000 21.59498 ? 98  GLN   B C   1 
ATOM   2798 O  O   . GLN   B 1 102 ? 13.32754 -49.76745 16.94710  1.000 18.08820 ? 98  GLN   B O   1 
ATOM   2799 C  CB  . GLN   B 1 102 ? 15.23929 -52.12982 17.98598  1.000 33.52273 ? 98  GLN   B CB  1 
ATOM   2800 C  CG  . GLN   B 1 102 ? 14.22429 -52.83412 17.05550  1.000 34.59995 ? 98  GLN   B CG  1 
ATOM   2801 C  CD  . GLN   B 1 102 ? 14.58666 -52.68602 15.59048  1.000 42.03209 ? 98  GLN   B CD  1 
ATOM   2802 O  OE1 . GLN   B 1 102 ? 15.63008 -53.18021 15.15619  1.000 41.10174 ? 98  GLN   B OE1 1 
ATOM   2803 N  NE2 . GLN   B 1 102 ? 13.75160 -51.97958 14.82962  1.000 34.93696 ? 98  GLN   B NE2 1 
ATOM   2804 N  N   . GLU   B 1 103 ? 13.91777 -49.28898 19.06129  1.000 18.24912 ? 99  GLU   B N   1 
ATOM   2805 C  CA  . GLU   B 1 103 ? 12.75629 -48.43110 19.26777  1.000 23.43761 ? 99  GLU   B CA  1 
ATOM   2806 C  C   . GLU   B 1 103 ? 12.86868 -47.14845 18.45199  1.000 19.54952 ? 99  GLU   B C   1 
ATOM   2807 O  O   . GLU   B 1 103 ? 11.86397 -46.65176 17.93137  1.000 18.72232 ? 99  GLU   B O   1 
ATOM   2808 C  CB  . GLU   B 1 103 ? 12.59331 -48.11908 20.75574  1.000 31.09965 ? 99  GLU   B CB  1 
ATOM   2809 C  CG  . GLU   B 1 103 ? 13.87229 -47.64358 21.43783  1.000 35.38094 ? 99  GLU   B CG  1 
ATOM   2810 C  CD  . GLU   B 1 103 ? 14.88268 -48.76774 21.62479  1.000 39.40944 ? 99  GLU   B CD  1 
ATOM   2811 O  OE1 . GLU   B 1 103 ? 15.02415 -49.27053 22.75782  1.000 52.48174 ? 99  GLU   B OE1 1 
ATOM   2812 O  OE2 . GLU   B 1 103 ? 15.50682 -49.17815 20.62675  1.000 52.82092 ? 99  GLU   B OE2 1 
ATOM   2813 N  N   . ASP   B 1 104 ? 14.08116 -46.59525 18.33158  1.000 15.28181 ? 100 ASP   B N   1 
ATOM   2814 C  CA  . ASP   B 1 104 ? 14.28355 -45.44749 17.45017  1.000 18.97644 ? 100 ASP   B CA  1 
ATOM   2815 C  C   . ASP   B 1 104 ? 14.07459 -45.83138 15.99285  1.000 17.37326 ? 100 ASP   B C   1 
ATOM   2816 O  O   . ASP   B 1 104 ? 13.54486 -45.03639 15.20800  1.000 13.36617 ? 100 ASP   B O   1 
ATOM   2817 C  CB  . ASP   B 1 104 ? 15.68277 -44.86183 17.63605  1.000 16.57574 ? 100 ASP   B CB  1 
ATOM   2818 C  CG  . ASP   B 1 104 ? 15.80316 -44.02084 18.88922  1.000 37.98188 ? 100 ASP   B CG  1 
ATOM   2819 O  OD1 . ASP   B 1 104 ? 14.77406 -43.79990 19.56154  1.000 37.78088 ? 100 ASP   B OD1 1 
ATOM   2820 O  OD2 . ASP   B 1 104 ? 16.93051 -43.58240 19.20016  1.000 37.79461 ? 100 ASP   B OD2 1 
ATOM   2821 N  N   . ALA   B 1 105 ? 14.50811 -47.03525 15.60774  1.000 12.45033 ? 101 ALA   B N   1 
ATOM   2822 C  CA  . ALA   B 1 105 ? 14.26894 -47.50111 14.24671  1.000 14.56919 ? 101 ALA   B CA  1 
ATOM   2823 C  C   . ALA   B 1 105 ? 12.77771 -47.61455 13.96932  1.000 21.24950 ? 101 ALA   B C   1 
ATOM   2824 O  O   . ALA   B 1 105 ? 12.30543 -47.22642 12.89339  1.000 19.63634 ? 101 ALA   B O   1 
ATOM   2825 C  CB  . ALA   B 1 105 ? 14.96188 -48.84435 14.01742  1.000 19.38484 ? 101 ALA   B CB  1 
ATOM   2826 N  N   . GLU   B 1 106 ? 12.01974 -48.13887 14.93612  1.000 15.51194 ? 102 GLU   B N   1 
ATOM   2827 C  CA  . GLU   B 1 106 ? 10.56947 -48.20481 14.79480  1.000 23.43232 ? 102 GLU   B CA  1 
ATOM   2828 C  C   . GLU   B 1 106 ? 9.95129  -46.80981 14.78133  1.000 24.13698 ? 102 GLU   B C   1 
ATOM   2829 O  O   . GLU   B 1 106 ? 9.01191  -46.54888 14.02021  1.000 20.98860 ? 102 GLU   B O   1 
ATOM   2830 C  CB  . GLU   B 1 106 ? 9.97922  -49.05043 15.92523  1.000 20.88030 ? 102 GLU   B CB  1 
ATOM   2831 C  CG  . GLU   B 1 106 ? 8.57752  -49.58166 15.66431  1.000 35.94128 ? 102 GLU   B CG  1 
ATOM   2832 C  CD  . GLU   B 1 106 ? 7.50030  -48.52775 15.83414  1.000 41.99443 ? 102 GLU   B CD  1 
ATOM   2833 O  OE1 . GLU   B 1 106 ? 7.61561  -47.69772 16.76193  1.000 42.74314 ? 102 GLU   B OE1 1 
ATOM   2834 O  OE2 . GLU   B 1 106 ? 6.53995  -48.52874 15.03378  1.000 46.25833 ? 102 GLU   B OE2 1 
ATOM   2835 N  N   . ALA   B 1 107 ? 10.47344 -45.89685 15.60430  1.000 16.66027 ? 103 ALA   B N   1 
ATOM   2836 C  CA  . ALA   B 1 107 ? 9.85349  -44.58225 15.73931  1.000 22.01379 ? 103 ALA   B CA  1 
ATOM   2837 C  C   . ALA   B 1 107 ? 9.91316  -43.79386 14.43612  1.000 15.83564 ? 103 ALA   B C   1 
ATOM   2838 O  O   . ALA   B 1 107 ? 8.91620  -43.18509 14.02965  1.000 14.70878 ? 103 ALA   B O   1 
ATOM   2839 C  CB  . ALA   B 1 107 ? 10.51640 -43.79874 16.87267  1.000 17.04409 ? 103 ALA   B CB  1 
ATOM   2840 N  N   . ILE   B 1 108 ? 11.06197 -43.80085 13.75465  1.000 13.66122 ? 104 ILE   B N   1 
ATOM   2841 C  CA  . ILE   B 1 108 ? 11.20409 -42.97334 12.56170  1.000 9.23728  ? 104 ILE   B CA  1 
ATOM   2842 C  C   . ILE   B 1 108 ? 10.40561 -43.50096 11.38111  1.000 15.38611 ? 104 ILE   B C   1 
ATOM   2843 O  O   . ILE   B 1 108 ? 10.28035 -42.79760 10.37257  1.000 12.59351 ? 104 ILE   B O   1 
ATOM   2844 C  CB  . ILE   B 1 108 ? 12.68376 -42.81639 12.14957  1.000 11.89976 ? 104 ILE   B CB  1 
ATOM   2845 C  CG1 . ILE   B 1 108 ? 13.29300 -44.16531 11.76327  1.000 14.44614 ? 104 ILE   B CG1 1 
ATOM   2846 C  CG2 . ILE   B 1 108 ? 13.48512 -42.16011 13.27011  1.000 20.98720 ? 104 ILE   B CG2 1 
ATOM   2847 C  CD1 . ILE   B 1 108 ? 14.72571 -44.05759 11.26482  1.000 13.30749 ? 104 ILE   B CD1 1 
ATOM   2848 N  N   . THR   B 1 109 ? 9.85593  -44.71573 11.47330  1.000 14.76074 ? 105 THR   B N   1 
ATOM   2849 C  CA  . THR   B 1 109 ? 8.95179  -45.17480 10.42506  1.000 15.50754 ? 105 THR   B CA  1 
ATOM   2850 C  C   . THR   B 1 109 ? 7.63032  -44.42180 10.43424  1.000 17.28004 ? 105 THR   B C   1 
ATOM   2851 O  O   . THR   B 1 109 ? 6.86609  -44.53978 9.47082   1.000 19.83515 ? 105 THR   B O   1 
ATOM   2852 C  CB  . THR   B 1 109 ? 8.68297  -46.67780 10.54880  1.000 19.29646 ? 105 THR   B CB  1 
ATOM   2853 O  OG1 . THR   B 1 109 ? 7.94271  -46.94032 11.74613  1.000 18.50871 ? 105 THR   B OG1 1 
ATOM   2854 C  CG2 . THR   B 1 109 ? 9.98785  -47.45386 10.58565  1.000 18.92484 ? 105 THR   B CG2 1 
ATOM   2855 N  N   . HIS   B 1 110 ? 7.34838  -43.65689 11.48890  1.000 13.44183 ? 106 HIS   B N   1 
ATOM   2856 C  CA  . HIS   B 1 110 ? 6.14135  -42.84893 11.58216  1.000 15.73936 ? 106 HIS   B CA  1 
ATOM   2857 C  C   . HIS   B 1 110 ? 6.33025  -41.44858 11.01509  1.000 18.36150 ? 106 HIS   B C   1 
ATOM   2858 O  O   . HIS   B 1 110 ? 5.40019  -40.63941 11.08216  1.000 15.77698 ? 106 HIS   B O   1 
ATOM   2859 C  CB  . HIS   B 1 110 ? 5.68179  -42.74313 13.04145  1.000 16.68694 ? 106 HIS   B CB  1 
ATOM   2860 C  CG  . HIS   B 1 110 ? 5.33252  -44.05680 13.66890  1.000 22.88335 ? 106 HIS   B CG  1 
ATOM   2861 N  ND1 . HIS   B 1 110 ? 4.03311  -44.43119 13.93486  1.000 27.57707 ? 106 HIS   B ND1 1 
ATOM   2862 C  CD2 . HIS   B 1 110 ? 6.11302  -45.07802 14.09593  1.000 23.19314 ? 106 HIS   B CD2 1 
ATOM   2863 C  CE1 . HIS   B 1 110 ? 4.02756  -45.62850 14.49469  1.000 29.43487 ? 106 HIS   B CE1 1 
ATOM   2864 N  NE2 . HIS   B 1 110 ? 5.27697  -46.04373 14.60309  1.000 27.41847 ? 106 HIS   B NE2 1 
ATOM   2865 N  N   . LEU   B 1 111 ? 7.50729  -41.14690 10.47457  1.000 11.62787 ? 107 LEU   B N   1 
ATOM   2866 C  CA  . LEU   B 1 111 ? 7.82788  -39.83800 9.92507   1.000 10.65197 ? 107 LEU   B CA  1 
ATOM   2867 C  C   . LEU   B 1 111 ? 7.78678  -39.87953 8.40625   1.000 13.92219 ? 107 LEU   B C   1 
ATOM   2868 O  O   . LEU   B 1 111 ? 8.24991  -40.84484 7.79126   1.000 12.70662 ? 107 LEU   B O   1 
ATOM   2869 C  CB  . LEU   B 1 111 ? 9.21362  -39.38352 10.37722  1.000 11.08201 ? 107 LEU   B CB  1 
ATOM   2870 C  CG  . LEU   B 1 111 ? 9.34742  -38.90120 11.81984  1.000 8.22516  ? 107 LEU   B CG  1 
ATOM   2871 C  CD1 . LEU   B 1 111 ? 10.80753 -38.84031 12.19088  1.000 7.80810  ? 107 LEU   B CD1 1 
ATOM   2872 C  CD2 . LEU   B 1 111 ? 8.70658  -37.53427 11.94696  1.000 11.87249 ? 107 LEU   B CD2 1 
ATOM   2873 N  N   . PHE   B 1 112 ? 7.23681  -38.82052 7.81097   1.000 13.65172 ? 108 PHE   B N   1 
ATOM   2874 C  CA  . PHE   B 1 112 ? 7.19707  -38.66067 6.35958   1.000 15.10594 ? 108 PHE   B CA  1 
ATOM   2875 C  C   . PHE   B 1 112 ? 6.64297  -39.92150 5.69172   1.000 17.47638 ? 108 PHE   B C   1 
ATOM   2876 O  O   . PHE   B 1 112 ? 7.21504  -40.45424 4.74164   1.000 17.61902 ? 108 PHE   B O   1 
ATOM   2877 C  CB  . PHE   B 1 112 ? 8.58891  -38.31404 5.81267   1.000 8.44559  ? 108 PHE   B CB  1 
ATOM   2878 C  CG  . PHE   B 1 112 ? 9.26597  -37.16043 6.52281   1.000 14.58807 ? 108 PHE   B CG  1 
ATOM   2879 C  CD1 . PHE   B 1 112 ? 8.60026  -35.96322 6.73853   1.000 10.17759 ? 108 PHE   B CD1 1 
ATOM   2880 C  CD2 . PHE   B 1 112 ? 10.57439 -37.28067 6.97164   1.000 7.70908  ? 108 PHE   B CD2 1 
ATOM   2881 C  CE1 . PHE   B 1 112 ? 9.22634  -34.90517 7.39284   1.000 11.75420 ? 108 PHE   B CE1 1 
ATOM   2882 C  CE2 . PHE   B 1 112 ? 11.20898 -36.22343 7.62877   1.000 10.01676 ? 108 PHE   B CE2 1 
ATOM   2883 C  CZ  . PHE   B 1 112 ? 10.53162 -35.03560 7.83572   1.000 7.29893  ? 108 PHE   B CZ  1 
ATOM   2884 N  N   . THR   B 1 113 ? 5.51240  -40.40971 6.21048   1.000 14.34593 ? 109 THR   B N   1 
ATOM   2885 C  CA  . THR   B 1 113 ? 5.03457  -41.73363 5.82453   1.000 15.24158 ? 109 THR   B CA  1 
ATOM   2886 C  C   . THR   B 1 113 ? 4.50655  -41.77642 4.39914   1.000 20.64191 ? 109 THR   B C   1 
ATOM   2887 O  O   . THR   B 1 113 ? 4.38048  -42.86783 3.83275   1.000 22.66358 ? 109 THR   B O   1 
ATOM   2888 C  CB  . THR   B 1 113 ? 3.94686  -42.21330 6.78657   1.000 19.43154 ? 109 THR   B CB  1 
ATOM   2889 O  OG1 . THR   B 1 113 ? 2.83275  -41.31125 6.74675   1.000 23.79872 ? 109 THR   B OG1 1 
ATOM   2890 C  CG2 . THR   B 1 113 ? 4.49055  -42.28571 8.20657   1.000 21.69771 ? 109 THR   B CG2 1 
ATOM   2891 N  N   . ASP   B 1 114 ? 4.19996  -40.62624 3.80874   1.000 19.12760 ? 110 ASP   B N   1 
ATOM   2892 C  CA  . ASP   B 1 114 ? 3.69873  -40.57161 2.44466   1.000 28.61039 ? 110 ASP   B CA  1 
ATOM   2893 C  C   . ASP   B 1 114 ? 4.79861  -40.34322 1.41932   1.000 28.61667 ? 110 ASP   B C   1 
ATOM   2894 O  O   . ASP   B 1 114 ? 4.50374  -40.28964 0.22062   1.000 26.80016 ? 110 ASP   B O   1 
ATOM   2895 C  CB  . ASP   B 1 114 ? 2.64257  -39.47097 2.31466   1.000 28.95914 ? 110 ASP   B CB  1 
ATOM   2896 C  CG  . ASP   B 1 114 ? 3.13946  -38.12659 2.81070   1.000 30.85873 ? 110 ASP   B CG  1 
ATOM   2897 O  OD1 . ASP   B 1 114 ? 4.19299  -38.08725 3.48184   1.000 27.68248 ? 110 ASP   B OD1 1 
ATOM   2898 O  OD2 . ASP   B 1 114 ? 2.47635  -37.10792 2.52801   1.000 47.76206 ? 110 ASP   B OD2 1 
ATOM   2899 N  N   . VAL   B 1 115 ? 6.05332  -40.21391 1.85363   1.000 23.23533 ? 111 VAL   B N   1 
ATOM   2900 C  CA  . VAL   B 1 115 ? 7.13294  -39.93513 0.91807   1.000 17.51279 ? 111 VAL   B CA  1 
ATOM   2901 C  C   . VAL   B 1 115 ? 7.37661  -41.15998 0.04319   1.000 14.61322 ? 111 VAL   B C   1 
ATOM   2902 O  O   . VAL   B 1 115 ? 7.24338  -42.30872 0.48985   1.000 11.50425 ? 111 VAL   B O   1 
ATOM   2903 C  CB  . VAL   B 1 115 ? 8.40185  -39.49883 1.67357   1.000 15.69765 ? 111 VAL   B CB  1 
ATOM   2904 C  CG1 . VAL   B 1 115 ? 9.11070  -40.68168 2.31482   1.000 15.07517 ? 111 VAL   B CG1 1 
ATOM   2905 C  CG2 . VAL   B 1 115 ? 9.33591  -38.75566 0.74488   1.000 15.52561 ? 111 VAL   B CG2 1 
ATOM   2906 N  N   . GLN   B 1 116 ? 7.70890  -40.91907 -1.22673  1.000 13.01849 ? 112 GLN   B N   1 
ATOM   2907 C  CA  . GLN   B 1 116 ? 7.83783  -42.02597 -2.16986  1.000 12.17462 ? 112 GLN   B CA  1 
ATOM   2908 C  C   . GLN   B 1 116 ? 9.09350  -42.85366 -1.91917  1.000 11.58569 ? 112 GLN   B C   1 
ATOM   2909 O  O   . GLN   B 1 116 ? 9.07156  -44.07399 -2.11979  1.000 14.30157 ? 112 GLN   B O   1 
ATOM   2910 C  CB  . GLN   B 1 116 ? 7.81446  -41.49704 -3.60561  1.000 16.54249 ? 112 GLN   B CB  1 
ATOM   2911 C  CG  . GLN   B 1 116 ? 6.42470  -41.05026 -4.05580  1.000 14.26303 ? 112 GLN   B CG  1 
ATOM   2912 C  CD  . GLN   B 1 116 ? 6.40885  -40.44911 -5.44741  1.000 21.39743 ? 112 GLN   B CD  1 
ATOM   2913 O  OE1 . GLN   B 1 116 ? 7.44264  -40.34006 -6.10475  1.000 22.76212 ? 112 GLN   B OE1 1 
ATOM   2914 N  NE2 . GLN   B 1 116 ? 5.22637  -40.05603 -5.90358  1.000 31.50859 ? 112 GLN   B NE2 1 
ATOM   2915 N  N   . ASN   B 1 117 ? 10.18693 -42.22907 -1.47938  1.000 11.62568 ? 113 ASN   B N   1 
ATOM   2916 C  CA  . ASN   B 1 117 ? 11.43876 -42.94078 -1.23836  1.000 9.85952  ? 113 ASN   B CA  1 
ATOM   2917 C  C   . ASN   B 1 117 ? 11.94839 -42.65339 0.16255   1.000 13.49375 ? 113 ASN   B C   1 
ATOM   2918 O  O   . ASN   B 1 117 ? 12.02633 -41.49168 0.56992   1.000 13.53385 ? 113 ASN   B O   1 
ATOM   2919 C  CB  . ASN   B 1 117 ? 12.50844 -42.54823 -2.24941  1.000 10.08083 ? 113 ASN   B CB  1 
ATOM   2920 C  CG  . ASN   B 1 117 ? 11.98523 -42.53052 -3.65504  1.000 16.41843 ? 113 ASN   B CG  1 
ATOM   2921 O  OD1 . ASN   B 1 117 ? 11.72810 -43.57814 -4.24673  1.000 14.32839 ? 113 ASN   B OD1 1 
ATOM   2922 N  ND2 . ASN   B 1 117 ? 11.80512 -41.33552 -4.19912  1.000 11.17246 ? 113 ASN   B ND2 1 
ATOM   2923 N  N   . ARG   B 1 118 ? 12.32379 -43.70918 0.88118   1.000 14.22194 ? 114 ARG   B N   1 
ATOM   2924 C  CA  . ARG   B 1 118 ? 12.89616 -43.59478 2.21491   1.000 11.43017 ? 114 ARG   B CA  1 
ATOM   2925 C  C   . ARG   B 1 118 ? 14.30691 -44.16279 2.19970   1.000 8.91990  ? 114 ARG   B C   1 
ATOM   2926 O  O   . ARG   B 1 118 ? 14.52809 -45.26817 1.69357   1.000 15.46730 ? 114 ARG   B O   1 
ATOM   2927 C  CB  . ARG   B 1 118 ? 12.04208 -44.33148 3.24694   1.000 17.81476 ? 114 ARG   B CB  1 
ATOM   2928 C  CG  . ARG   B 1 118 ? 10.56237 -44.01071 3.17643   1.000 15.71560 ? 114 ARG   B CG  1 
ATOM   2929 C  CD  . ARG   B 1 118 ? 9.78085  -44.85005 4.17207   1.000 15.15865 ? 114 ARG   B CD  1 
ATOM   2930 N  NE  . ARG   B 1 118 ? 10.14169 -44.52657 5.54612   1.000 18.90354 ? 114 ARG   B NE  1 
ATOM   2931 C  CZ  . ARG   B 1 118 ? 9.66690  -43.48403 6.21401   1.000 13.75547 ? 114 ARG   B CZ  1 
ATOM   2932 N  NH1 . ARG   B 1 118 ? 8.82677  -42.62850 5.65396   1.000 18.60722 ? 114 ARG   B NH1 1 
ATOM   2933 N  NH2 . ARG   B 1 118 ? 10.04625 -43.29335 7.47250   1.000 14.01419 ? 114 ARG   B NH2 1 
ATOM   2934 N  N   . TYR   B 1 119 ? 15.25518 -43.41005 2.75140   1.000 8.06595  ? 115 TYR   B N   1 
ATOM   2935 C  CA  . TYR   B 1 119 ? 16.64563 -43.83437 2.83470   1.000 9.35062  ? 115 TYR   B CA  1 
ATOM   2936 C  C   . TYR   B 1 119 ? 17.13376 -43.73006 4.26949   1.000 12.44141 ? 115 TYR   B C   1 
ATOM   2937 O  O   . TYR   B 1 119 ? 16.80140 -42.77515 4.97890   1.000 11.18921 ? 115 TYR   B O   1 
ATOM   2938 C  CB  . TYR   B 1 119 ? 17.54754 -42.98836 1.93409   1.000 8.73022  ? 115 TYR   B CB  1 
ATOM   2939 C  CG  . TYR   B 1 119 ? 17.17963 -43.03591 0.47321   1.000 8.81003  ? 115 TYR   B CG  1 
ATOM   2940 C  CD1 . TYR   B 1 119 ? 17.58341 -44.09409 -0.32712  1.000 10.47148 ? 115 TYR   B CD1 1 
ATOM   2941 C  CD2 . TYR   B 1 119 ? 16.43718 -42.01276 -0.11042  1.000 10.53583 ? 115 TYR   B CD2 1 
ATOM   2942 C  CE1 . TYR   B 1 119 ? 17.24749 -44.13883 -1.67026  1.000 16.39745 ? 115 TYR   B CE1 1 
ATOM   2943 C  CE2 . TYR   B 1 119 ? 16.10306 -42.04435 -1.44862  1.000 12.73182 ? 115 TYR   B CE2 1 
ATOM   2944 C  CZ  . TYR   B 1 119 ? 16.50940 -43.11200 -2.22432  1.000 16.81449 ? 115 TYR   B CZ  1 
ATOM   2945 O  OH  . TYR   B 1 119 ? 16.17978 -43.15914 -3.55855  1.000 17.43895 ? 115 TYR   B OH  1 
ATOM   2946 N  N   . THR   B 1 120 ? 17.93016 -44.71127 4.69011   1.000 9.44961  ? 116 THR   B N   1 
ATOM   2947 C  CA  . THR   B 1 120 ? 18.60006 -44.67555 5.98411   1.000 10.24357 ? 116 THR   B CA  1 
ATOM   2948 C  C   . THR   B 1 120 ? 20.10227 -44.73025 5.75633   1.000 12.89671 ? 116 THR   B C   1 
ATOM   2949 O  O   . THR   B 1 120 ? 20.61614 -45.71576 5.21597   1.000 15.62681 ? 116 THR   B O   1 
ATOM   2950 C  CB  . THR   B 1 120 ? 18.15661 -45.82811 6.88355   1.000 15.84354 ? 116 THR   B CB  1 
ATOM   2951 O  OG1 . THR   B 1 120 ? 16.73023 -45.81378 7.01369   1.000 16.87761 ? 116 THR   B OG1 1 
ATOM   2952 C  CG2 . THR   B 1 120 ? 18.79284 -45.68695 8.26993   1.000 11.78556 ? 116 THR   B CG2 1 
ATOM   2953 N  N   . PHE   B 1 121 ? 20.79709 -43.66800 6.15327   1.000 11.65387 ? 117 PHE   B N   1 
ATOM   2954 C  CA  . PHE   B 1 121 ? 22.25055 -43.65918 6.11265   1.000 9.94702  ? 117 PHE   B CA  1 
ATOM   2955 C  C   . PHE   B 1 121 ? 22.81930 -44.74484 7.02774   1.000 16.05741 ? 117 PHE   B C   1 
ATOM   2956 O  O   . PHE   B 1 121 ? 22.17259 -45.20462 7.97303   1.000 14.77763 ? 117 PHE   B O   1 
ATOM   2957 C  CB  . PHE   B 1 121 ? 22.78676 -42.29264 6.54088   1.000 13.41184 ? 117 PHE   B CB  1 
ATOM   2958 C  CG  . PHE   B 1 121 ? 22.41624 -41.16573 5.61520   1.000 10.51347 ? 117 PHE   B CG  1 
ATOM   2959 C  CD1 . PHE   B 1 121 ? 22.64066 -41.26163 4.25027   1.000 18.40252 ? 117 PHE   B CD1 1 
ATOM   2960 C  CD2 . PHE   B 1 121 ? 21.85776 -39.99763 6.11808   1.000 16.81687 ? 117 PHE   B CD2 1 
ATOM   2961 C  CE1 . PHE   B 1 121 ? 22.30786 -40.21478 3.40310   1.000 16.02956 ? 117 PHE   B CE1 1 
ATOM   2962 C  CE2 . PHE   B 1 121 ? 21.52238 -38.94769 5.27993   1.000 11.84632 ? 117 PHE   B CE2 1 
ATOM   2963 C  CZ  . PHE   B 1 121 ? 21.74823 -39.05758 3.91468   1.000 13.08917 ? 117 PHE   B CZ  1 
ATOM   2964 N  N   . ALA   B 1 122 ? 24.05299 -45.15637 6.73478   1.000 17.62586 ? 118 ALA   B N   1 
ATOM   2965 C  CA  . ALA   B 1 122 ? 24.76746 -46.07942 7.60834   1.000 15.48856 ? 118 ALA   B CA  1 
ATOM   2966 C  C   . ALA   B 1 122 ? 25.41301 -45.37694 8.79217   1.000 14.81833 ? 118 ALA   B C   1 
ATOM   2967 O  O   . ALA   B 1 122 ? 25.86526 -46.05109 9.72528   1.000 18.45169 ? 118 ALA   B O   1 
ATOM   2968 C  CB  . ALA   B 1 122 ? 25.84045 -46.83540 6.81875   1.000 19.56135 ? 118 ALA   B CB  1 
ATOM   2969 N  N   . PHE   B 1 123 ? 25.46864 -44.05075 8.77259   1.000 18.36198 ? 119 PHE   B N   1 
ATOM   2970 C  CA  . PHE   B 1 123 ? 26.10009 -43.27167 9.82271   1.000 16.26830 ? 119 PHE   B CA  1 
ATOM   2971 C  C   . PHE   B 1 123 ? 25.05159 -42.55651 10.66178  1.000 15.55533 ? 119 PHE   B C   1 
ATOM   2972 O  O   . PHE   B 1 123 ? 23.95078 -42.25323 10.19016  1.000 12.93189 ? 119 PHE   B O   1 
ATOM   2973 C  CB  . PHE   B 1 123 ? 27.08572 -42.24982 9.23705   1.000 21.10856 ? 119 PHE   B CB  1 
ATOM   2974 C  CG  . PHE   B 1 123 ? 26.49827 -41.37542 8.15448   1.000 14.93535 ? 119 PHE   B CG  1 
ATOM   2975 C  CD1 . PHE   B 1 123 ? 25.86454 -40.18593 8.47094   1.000 13.49829 ? 119 PHE   B CD1 1 
ATOM   2976 C  CD2 . PHE   B 1 123 ? 26.60006 -41.73999 6.81964   1.000 18.30902 ? 119 PHE   B CD2 1 
ATOM   2977 C  CE1 . PHE   B 1 123 ? 25.33034 -39.37752 7.47701   1.000 17.38331 ? 119 PHE   B CE1 1 
ATOM   2978 C  CE2 . PHE   B 1 123 ? 26.07266 -40.94083 5.82262   1.000 11.58686 ? 119 PHE   B CE2 1 
ATOM   2979 C  CZ  . PHE   B 1 123 ? 25.43668 -39.75813 6.14906   1.000 17.96343 ? 119 PHE   B CZ  1 
ATOM   2980 N  N   . GLY   B 1 124 ? 25.40838 -42.29769 11.92129  1.000 20.47185 ? 120 GLY   B N   1 
ATOM   2981 C  CA  . GLY   B 1 124 ? 24.57790 -41.49595 12.79244  1.000 18.33302 ? 120 GLY   B CA  1 
ATOM   2982 C  C   . GLY   B 1 124 ? 24.87244 -40.00764 12.65646  1.000 18.49447 ? 120 GLY   B C   1 
ATOM   2983 O  O   . GLY   B 1 124 ? 25.82962 -39.59311 12.00363  1.000 20.64124 ? 120 GLY   B O   1 
ATOM   2984 N  N   . GLY   B 1 125 ? 24.03135 -39.20338 13.30225  1.000 16.30594 ? 121 GLY   B N   1 
ATOM   2985 C  CA  . GLY   B 1 125 ? 24.11884 -37.75981 13.17606  1.000 15.55429 ? 121 GLY   B CA  1 
ATOM   2986 C  C   . GLY   B 1 125 ? 24.96134 -37.06299 14.22445  1.000 18.70519 ? 121 GLY   B C   1 
ATOM   2987 O  O   . GLY   B 1 125 ? 24.75475 -35.87699 14.49600  1.000 16.80221 ? 121 GLY   B O   1 
ATOM   2988 N  N   . ASN   B 1 126 ? 25.91244 -37.77582 14.82250  1.000 16.45844 ? 122 ASN   B N   1 
ATOM   2989 C  CA  . ASN   B 1 126 ? 26.79705 -37.15940 15.79694  1.000 17.60156 ? 122 ASN   B CA  1 
ATOM   2990 C  C   . ASN   B 1 126 ? 27.88791 -36.35317 15.09601  1.000 15.96881 ? 122 ASN   B C   1 
ATOM   2991 O  O   . ASN   B 1 126 ? 28.24421 -36.60917 13.94297  1.000 13.83189 ? 122 ASN   B O   1 
ATOM   2992 C  CB  . ASN   B 1 126 ? 27.42117 -38.21914 16.70322  1.000 26.84340 ? 122 ASN   B CB  1 
ATOM   2993 C  CG  . ASN   B 1 126 ? 28.22927 -39.23635 15.93421  1.000 27.30455 ? 122 ASN   B CG  1 
ATOM   2994 O  OD1 . ASN   B 1 126 ? 29.44854 -39.10866 15.80328  1.000 24.06572 ? 122 ASN   B OD1 1 
ATOM   2995 N  ND2 . ASN   B 1 126 ? 27.55332 -40.25605 15.41290  1.000 34.44108 ? 122 ASN   B ND2 1 
ATOM   2996 N  N   . TYR   B 1 127 ? 28.42088 -35.36498 15.82033  1.000 16.64188 ? 123 TYR   B N   1 
ATOM   2997 C  CA  . TYR   B 1 127 ? 29.38940 -34.44290 15.23207  1.000 18.19647 ? 123 TYR   B CA  1 
ATOM   2998 C  C   . TYR   B 1 127 ? 30.65075 -35.15909 14.77318  1.000 15.36155 ? 123 TYR   B C   1 
ATOM   2999 O  O   . TYR   B 1 127 ? 31.22336 -34.81089 13.73280  1.000 15.89937 ? 123 TYR   B O   1 
ATOM   3000 C  CB  . TYR   B 1 127 ? 29.75780 -33.35705 16.23814  1.000 15.10464 ? 123 TYR   B CB  1 
ATOM   3001 C  CG  . TYR   B 1 127 ? 28.69213 -32.31715 16.43390  1.000 14.23751 ? 123 TYR   B CG  1 
ATOM   3002 C  CD1 . TYR   B 1 127 ? 27.93871 -31.85342 15.36358  1.000 17.78485 ? 123 TYR   B CD1 1 
ATOM   3003 C  CD2 . TYR   B 1 127 ? 28.43865 -31.79380 17.69170  1.000 20.47081 ? 123 TYR   B CD2 1 
ATOM   3004 C  CE1 . TYR   B 1 127 ? 26.96368 -30.89264 15.54526  1.000 20.09567 ? 123 TYR   B CE1 1 
ATOM   3005 C  CE2 . TYR   B 1 127 ? 27.46968 -30.83628 17.88134  1.000 19.23454 ? 123 TYR   B CE2 1 
ATOM   3006 C  CZ  . TYR   B 1 127 ? 26.73510 -30.39017 16.80939  1.000 14.97785 ? 123 TYR   B CZ  1 
ATOM   3007 O  OH  . TYR   B 1 127 ? 25.76692 -29.43388 17.01000  1.000 18.23241 ? 123 TYR   B OH  1 
ATOM   3008 N  N   . ASP   B 1 128 ? 31.11517 -36.13826 15.55266  1.000 13.27079 ? 124 ASP   B N   1 
ATOM   3009 C  CA  . ASP   B 1 128 ? 32.35088 -36.83597 15.21307  1.000 19.19892 ? 124 ASP   B CA  1 
ATOM   3010 C  C   . ASP   B 1 128 ? 32.27218 -37.45568 13.82355  1.000 18.61883 ? 124 ASP   B C   1 
ATOM   3011 O  O   . ASP   B 1 128 ? 33.22046 -37.35377 13.03637  1.000 20.43789 ? 124 ASP   B O   1 
ATOM   3012 C  CB  . ASP   B 1 128 ? 32.65478 -37.90961 16.25816  1.000 19.80999 ? 124 ASP   B CB  1 
ATOM   3013 C  CG  . ASP   B 1 128 ? 32.93719 -37.32724 17.63906  1.000 36.34254 ? 124 ASP   B CG  1 
ATOM   3014 O  OD1 . ASP   B 1 128 ? 33.33208 -36.14469 17.72682  1.000 27.29941 ? 124 ASP   B OD1 1 
ATOM   3015 O  OD2 . ASP   B 1 128 ? 32.77160 -38.05859 18.63903  1.000 41.98095 ? 124 ASP   B OD2 1 
ATOM   3016 N  N   . ARG   B 1 129 ? 31.14821 -38.09882 13.50160  1.000 13.55018 ? 125 ARG   B N   1 
ATOM   3017 C  CA  . ARG   B 1 129 ? 31.00885 -38.71590 12.18526  1.000 13.02889 ? 125 ARG   B CA  1 
ATOM   3018 C  C   . ARG   B 1 129 ? 30.76846 -37.67066 11.10389  1.000 15.01754 ? 125 ARG   B C   1 
ATOM   3019 O  O   . ARG   B 1 129 ? 31.36274 -37.74147 10.02025  1.000 12.40223 ? 125 ARG   B O   1 
ATOM   3020 C  CB  . ARG   B 1 129 ? 29.86706 -39.72934 12.19648  1.000 19.95035 ? 125 ARG   B CB  1 
ATOM   3021 C  CG  . ARG   B 1 129 ? 30.09830 -40.92666 11.28994  1.000 34.00709 ? 125 ARG   B CG  1 
ATOM   3022 C  CD  . ARG   B 1 129 ? 30.65703 -42.09347 12.08775  1.000 44.25537 ? 125 ARG   B CD  1 
ATOM   3023 N  NE  . ARG   B 1 129 ? 29.85641 -42.34299 13.28142  1.000 58.59689 ? 125 ARG   B NE  1 
ATOM   3024 C  CZ  . ARG   B 1 129 ? 28.71692 -43.02103 13.28865  1.000 34.51342 ? 125 ARG   B CZ  1 
ATOM   3025 N  NH1 . ARG   B 1 129 ? 28.22533 -43.55424 12.18440  1.000 36.70978 ? 125 ARG   B NH1 1 
ATOM   3026 N  NH2 . ARG   B 1 129 ? 28.05222 -43.16266 14.43157  1.000 43.46845 ? 125 ARG   B NH2 1 
ATOM   3027 N  N   . LEU   B 1 130 ? 29.89926 -36.69453 11.37452  1.000 15.52086 ? 126 LEU   B N   1 
ATOM   3028 C  CA  . LEU   B 1 130 ? 29.60269 -35.67913 10.36719  1.000 11.27556 ? 126 LEU   B CA  1 
ATOM   3029 C  C   . LEU   B 1 130 ? 30.84493 -34.87108 10.01395  1.000 10.04867 ? 126 LEU   B C   1 
ATOM   3030 O  O   . LEU   B 1 130 ? 31.06607 -34.54202 8.84160   1.000 10.59786 ? 126 LEU   B O   1 
ATOM   3031 C  CB  . LEU   B 1 130 ? 28.48477 -34.76117 10.85574  1.000 10.63027 ? 126 LEU   B CB  1 
ATOM   3032 C  CG  . LEU   B 1 130 ? 27.09595 -35.39014 10.99531  1.000 9.17978  ? 126 LEU   B CG  1 
ATOM   3033 C  CD1 . LEU   B 1 130 ? 26.08953 -34.34439 11.45565  1.000 15.19492 ? 126 LEU   B CD1 1 
ATOM   3034 C  CD2 . LEU   B 1 130 ? 26.66093 -36.02882 9.67763   1.000 12.08572 ? 126 LEU   B CD2 1 
ATOM   3035 N  N   . GLU   B 1 131 ? 31.66235 -34.53482 11.01498  1.000 10.52690 ? 127 GLU   B N   1 
ATOM   3036 C  CA  . GLU   B 1 131 ? 32.90595 -33.81757 10.74590  1.000 15.45928 ? 127 GLU   B CA  1 
ATOM   3037 C  C   . GLU   B 1 131 ? 33.82978 -34.63836 9.85554   1.000 15.10470 ? 127 GLU   B C   1 
ATOM   3038 O  O   . GLU   B 1 131 ? 34.46238 -34.09885 8.94010   1.000 11.98494 ? 127 GLU   B O   1 
ATOM   3039 C  CB  . GLU   B 1 131 ? 33.60737 -33.45779 12.05771  1.000 12.76462 ? 127 GLU   B CB  1 
ATOM   3040 C  CG  . GLU   B 1 131 ? 33.01052 -32.24997 12.79988  1.000 11.97953 ? 127 GLU   B CG  1 
ATOM   3041 C  CD  . GLU   B 1 131 ? 33.54693 -32.11020 14.21720  1.000 19.28967 ? 127 GLU   B CD  1 
ATOM   3042 O  OE1 . GLU   B 1 131 ? 34.03662 -33.11827 14.77111  1.000 15.05513 ? 127 GLU   B OE1 1 
ATOM   3043 O  OE2 . GLU   B 1 131 ? 33.48856 -30.99432 14.77936  1.000 17.56722 ? 127 GLU   B OE2 1 
ATOM   3044 N  N   . GLN   B 1 132 ? 33.92593 -35.94555 10.11369  1.000 12.38637 ? 128 GLN   B N   1 
ATOM   3045 C  CA  . GLN   B 1 132 ? 34.74875 -36.80500 9.26925   1.000 13.34339 ? 128 GLN   B CA  1 
ATOM   3046 C  C   . GLN   B 1 132 ? 34.22015 -36.84208 7.84219   1.000 14.90218 ? 128 GLN   B C   1 
ATOM   3047 O  O   . GLN   B 1 132 ? 34.99998 -36.79960 6.88417   1.000 17.05848 ? 128 GLN   B O   1 
ATOM   3048 C  CB  . GLN   B 1 132 ? 34.81370 -38.21700 9.85548   1.000 18.06190 ? 128 GLN   B CB  1 
ATOM   3049 C  CG  . GLN   B 1 132 ? 35.55446 -38.29315 11.17893  1.000 26.36480 ? 128 GLN   B CG  1 
ATOM   3050 C  CD  . GLN   B 1 132 ? 35.55223 -39.68402 11.78702  1.000 30.64075 ? 128 GLN   B CD  1 
ATOM   3051 O  OE1 . GLN   B 1 132 ? 35.07962 -40.64310 11.17808  1.000 32.79922 ? 128 GLN   B OE1 1 
ATOM   3052 N  NE2 . GLN   B 1 132 ? 36.08579 -39.79776 12.99931  1.000 34.83679 ? 128 GLN   B NE2 1 
ATOM   3053 N  N   . LEU   B 1 133 ? 32.89615 -36.91837 7.67941   1.000 12.52268 ? 129 LEU   B N   1 
ATOM   3054 C  CA  . LEU   B 1 133 ? 32.32154 -36.94078 6.33869   1.000 15.07237 ? 129 LEU   B CA  1 
ATOM   3055 C  C   . LEU   B 1 133 ? 32.49387 -35.59784 5.64308   1.000 12.57604 ? 129 LEU   B C   1 
ATOM   3056 O  O   . LEU   B 1 133 ? 32.73802 -35.54610 4.43167   1.000 15.58445 ? 129 LEU   B O   1 
ATOM   3057 C  CB  . LEU   B 1 133 ? 30.84408 -37.31944 6.40747   1.000 13.12534 ? 129 LEU   B CB  1 
ATOM   3058 C  CG  . LEU   B 1 133 ? 30.50861 -38.72564 6.89776   1.000 22.85950 ? 129 LEU   B CG  1 
ATOM   3059 C  CD1 . LEU   B 1 133 ? 29.01066 -38.85105 7.12931   1.000 18.15627 ? 129 LEU   B CD1 1 
ATOM   3060 C  CD2 . LEU   B 1 133 ? 30.98897 -39.76386 5.89600   1.000 20.77848 ? 129 LEU   B CD2 1 
ATOM   3061 N  N   . ALA   B 1 134 ? 32.37449 -34.49936 6.39213   1.000 10.73484 ? 130 ALA   B N   1 
ATOM   3062 C  CA  . ALA   B 1 134 ? 32.51579 -33.17389 5.80335   1.000 12.39829 ? 130 ALA   B CA  1 
ATOM   3063 C  C   . ALA   B 1 134 ? 33.96561 -32.81074 5.51136   1.000 15.30653 ? 130 ALA   B C   1 
ATOM   3064 O  O   . ALA   B 1 134 ? 34.21528 -31.89237 4.72083   1.000 16.29756 ? 130 ALA   B O   1 
ATOM   3065 C  CB  . ALA   B 1 134 ? 31.89642 -32.12198 6.72470   1.000 10.89032 ? 130 ALA   B CB  1 
ATOM   3066 N  N   . GLY   B 1 135 ? 34.92304 -33.51043 6.11535   1.000 16.84245 ? 131 GLY   B N   1 
ATOM   3067 C  CA  . GLY   B 1 135 ? 36.31106 -33.12452 5.97014   1.000 13.59382 ? 131 GLY   B CA  1 
ATOM   3068 C  C   . GLY   B 1 135 ? 36.68406 -31.84657 6.68769   1.000 16.64841 ? 131 GLY   B C   1 
ATOM   3069 O  O   . GLY   B 1 135 ? 37.65668 -31.19464 6.30162   1.000 14.49862 ? 131 GLY   B O   1 
ATOM   3070 N  N   . ASN   B 1 136 ? 35.93919 -31.46934 7.72647   1.000 13.77291 ? 132 ASN   B N   1 
ATOM   3071 C  CA  . ASN   B 1 136 ? 36.22753 -30.26618 8.49705   1.000 16.00512 ? 132 ASN   B CA  1 
ATOM   3072 C  C   . ASN   B 1 136 ? 35.57106 -30.36754 9.86587   1.000 12.10481 ? 132 ASN   B C   1 
ATOM   3073 O  O   . ASN   B 1 136 ? 34.47964 -30.92725 10.00504  1.000 11.94525 ? 132 ASN   B O   1 
ATOM   3074 C  CB  . ASN   B 1 136 ? 35.72547 -29.00295 7.78902   1.000 19.42733 ? 132 ASN   B CB  1 
ATOM   3075 C  CG  . ASN   B 1 136 ? 36.77745 -28.36602 6.91363   1.000 24.98728 ? 132 ASN   B CG  1 
ATOM   3076 O  OD1 . ASN   B 1 136 ? 37.91800 -28.16840 7.33403   1.000 33.04329 ? 132 ASN   B OD1 1 
ATOM   3077 N  ND2 . ASN   B 1 136 ? 36.40071 -28.04054 5.68633   1.000 30.11484 ? 132 ASN   B ND2 1 
ATOM   3078 N  N   . LEU   B 1 137 ? 36.23543 -29.78975 10.86386  1.000 17.27060 ? 133 LEU   B N   1 
ATOM   3079 C  CA  . LEU   B 1 137 ? 35.67277 -29.64399 12.19765  1.000 18.02193 ? 133 LEU   B CA  1 
ATOM   3080 C  C   . LEU   B 1 137 ? 34.71805 -28.45116 12.25609  1.000 15.53091 ? 133 LEU   B C   1 
ATOM   3081 O  O   . LEU   B 1 137 ? 34.78997 -27.52446 11.44486  1.000 15.33377 ? 133 LEU   B O   1 
ATOM   3082 C  CB  . LEU   B 1 137 ? 36.78256 -29.45403 13.23517  1.000 15.32468 ? 133 LEU   B CB  1 
ATOM   3083 C  CG  . LEU   B 1 137 ? 37.87282 -30.51806 13.36082  1.000 24.55520 ? 133 LEU   B CG  1 
ATOM   3084 C  CD1 . LEU   B 1 137 ? 38.95964 -30.03330 14.31314  1.000 22.83383 ? 133 LEU   B CD1 1 
ATOM   3085 C  CD2 . LEU   B 1 137 ? 37.28297 -31.83113 13.84236  1.000 19.84290 ? 133 LEU   B CD2 1 
ATOM   3086 N  N   . ARG   B 1 138 ? 33.83039 -28.47528 13.25744  1.000 15.26534 ? 134 ARG   B N   1 
ATOM   3087 C  CA  . ARG   B 1 138 ? 32.87462 -27.38181 13.45041  1.000 13.35039 ? 134 ARG   B CA  1 
ATOM   3088 C  C   . ARG   B 1 138 ? 33.56429 -26.02354 13.51786  1.000 13.32772 ? 134 ARG   B C   1 
ATOM   3089 O  O   . ARG   B 1 138 ? 33.03716 -25.02686 13.01139  1.000 15.42771 ? 134 ARG   B O   1 
ATOM   3090 C  CB  . ARG   B 1 138 ? 32.06028 -27.61049 14.72532  1.000 11.95435 ? 134 ARG   B CB  1 
ATOM   3091 C  CG  . ARG   B 1 138 ? 30.94855 -28.63456 14.60828  1.000 11.78909 ? 134 ARG   B CG  1 
ATOM   3092 C  CD  . ARG   B 1 138 ? 30.43556 -29.01590 15.99292  1.000 15.54001 ? 134 ARG   B CD  1 
ATOM   3093 N  NE  . ARG   B 1 138 ? 31.35597 -29.91219 16.68335  1.000 15.01237 ? 134 ARG   B NE  1 
ATOM   3094 C  CZ  . ARG   B 1 138 ? 31.35721 -30.12394 17.99236  1.000 21.47108 ? 134 ARG   B CZ  1 
ATOM   3095 N  NH1 . ARG   B 1 138 ? 30.53158 -29.47741 18.79782  1.000 15.14114 ? 134 ARG   B NH1 1 
ATOM   3096 N  NH2 . ARG   B 1 138 ? 32.20908 -31.00756 18.50642  1.000 20.65177 ? 134 ARG   B NH2 1 
ATOM   3097 N  N   . GLU   B 1 139 ? 34.74741 -25.96148 14.13589  1.000 12.65880 ? 135 GLU   B N   1 
ATOM   3098 C  CA  . GLU   B 1 139 ? 35.46269 -24.69408 14.25032  1.000 15.01789 ? 135 GLU   B CA  1 
ATOM   3099 C  C   . GLU   B 1 139 ? 36.00485 -24.18874 12.92036  1.000 17.06676 ? 135 GLU   B C   1 
ATOM   3100 O  O   . GLU   B 1 139 ? 36.52936 -23.07101 12.87318  1.000 15.02029 ? 135 GLU   B O   1 
ATOM   3101 C  CB  . GLU   B 1 139 ? 36.61219 -24.83025 15.23857  1.000 18.11984 ? 135 GLU   B CB  1 
ATOM   3102 C  CG  . GLU   B 1 139 ? 37.45643 -26.03739 14.96983  1.000 29.16392 ? 135 GLU   B CG  1 
ATOM   3103 C  CD  . GLU   B 1 139 ? 38.28040 -26.41375 16.16005  1.000 53.62549 ? 135 GLU   B CD  1 
ATOM   3104 O  OE1 . GLU   B 1 139 ? 39.49184 -26.11086 16.15443  1.000 50.15140 ? 135 GLU   B OE1 1 
ATOM   3105 O  OE2 . GLU   B 1 139 ? 37.71399 -26.99362 17.11165  1.000 47.91313 ? 135 GLU   B OE2 1 
ATOM   3106 N  N   . ASN   B 1 140 ? 35.90649 -24.97679 11.85046  1.000 17.40033 ? 136 ASN   B N   1 
ATOM   3107 C  CA  . ASN   B 1 140 ? 36.30194 -24.52677 10.52053  1.000 18.61954 ? 136 ASN   B CA  1 
ATOM   3108 C  C   . ASN   B 1 140 ? 35.11842 -24.47801 9.56006   1.000 21.10264 ? 136 ASN   B C   1 
ATOM   3109 O  O   . ASN   B 1 140 ? 35.31392 -24.48577 8.34147   1.000 21.53832 ? 136 ASN   B O   1 
ATOM   3110 C  CB  . ASN   B 1 140 ? 37.41200 -25.41849 9.96015   1.000 14.01347 ? 136 ASN   B CB  1 
ATOM   3111 C  CG  . ASN   B 1 140 ? 38.65780 -25.41574 10.83199  1.000 17.40126 ? 136 ASN   B CG  1 
ATOM   3112 O  OD1 . ASN   B 1 140 ? 39.07748 -26.45651 11.34183  1.000 24.27825 ? 136 ASN   B OD1 1 
ATOM   3113 N  ND2 . ASN   B 1 140 ? 39.24919 -24.23929 11.01541  1.000 23.60301 ? 136 ASN   B ND2 1 
ATOM   3114 N  N   . ILE   B 1 141 ? 33.89540 -24.42122 10.08312  1.000 14.17971 ? 137 ILE   B N   1 
ATOM   3115 C  CA  . ILE   B 1 141 ? 32.67822 -24.37269 9.27554   1.000 10.22160 ? 137 ILE   B CA  1 
ATOM   3116 C  C   . ILE   B 1 141 ? 31.90209 -23.13465 9.70172   1.000 15.79192 ? 137 ILE   B C   1 
ATOM   3117 O  O   . ILE   B 1 141 ? 31.44160 -23.04614 10.84671  1.000 10.94949 ? 137 ILE   B O   1 
ATOM   3118 C  CB  . ILE   B 1 141 ? 31.83142 -25.64351 9.43659   1.000 14.96207 ? 137 ILE   B CB  1 
ATOM   3119 C  CG1 . ILE   B 1 141 ? 32.56118 -26.84324 8.82067   1.000 17.35202 ? 137 ILE   B CG1 1 
ATOM   3120 C  CG2 . ILE   B 1 141 ? 30.45361 -25.44939 8.81497   1.000 12.82994 ? 137 ILE   B CG2 1 
ATOM   3121 C  CD1 . ILE   B 1 141 ? 32.01216 -28.20936 9.23102   1.000 12.11890 ? 137 ILE   B CD1 1 
ATOM   3122 N  N   . GLU   B 1 142 ? 31.75818 -22.17826 8.78994   1.000 13.62202 ? 138 GLU   B N   1 
ATOM   3123 C  CA  . GLU   B 1 142 ? 31.13666 -20.90549 9.12874   1.000 10.42703 ? 138 GLU   B CA  1 
ATOM   3124 C  C   . GLU   B 1 142 ? 29.63079 -21.06479 9.31638   1.000 9.60712  ? 138 GLU   B C   1 
ATOM   3125 O  O   . GLU   B 1 142 ? 28.98093 -21.89141 8.66829   1.000 10.97383 ? 138 GLU   B O   1 
ATOM   3126 C  CB  . GLU   B 1 142 ? 31.42453 -19.87024 8.03573   1.000 11.76511 ? 138 GLU   B CB  1 
ATOM   3127 C  CG  . GLU   B 1 142 ? 32.91315 -19.63183 7.80955   1.000 18.63052 ? 138 GLU   B CG  1 
ATOM   3128 C  CD  . GLU   B 1 142 ? 33.21710 -18.94801 6.48651   1.000 34.14021 ? 138 GLU   B CD  1 
ATOM   3129 O  OE1 . GLU   B 1 142 ? 32.33803 -18.92860 5.59826   1.000 35.48326 ? 138 GLU   B OE1 1 
ATOM   3130 O  OE2 . GLU   B 1 142 ? 34.34426 -18.43434 6.33130   1.000 47.56729 ? 138 GLU   B OE2 1 
ATOM   3131 N  N   . LEU   B 1 143 ? 29.08204 -20.26920 10.22764  1.000 9.84223  ? 139 LEU   B N   1 
ATOM   3132 C  CA  . LEU   B 1 143 ? 27.65035 -20.19818 10.47438  1.000 9.43023  ? 139 LEU   B CA  1 
ATOM   3133 C  C   . LEU   B 1 143 ? 27.15203 -18.78587 10.18308  1.000 9.95697  ? 139 LEU   B C   1 
ATOM   3134 O  O   . LEU   B 1 143 ? 27.93087 -17.83033 10.11544  1.000 10.72248 ? 139 LEU   B O   1 
ATOM   3135 C  CB  . LEU   B 1 143 ? 27.31416 -20.59106 11.91942  1.000 9.52688  ? 139 LEU   B CB  1 
ATOM   3136 C  CG  . LEU   B 1 143 ? 27.85756 -21.96235 12.32779  1.000 9.99694  ? 139 LEU   B CG  1 
ATOM   3137 C  CD1 . LEU   B 1 143 ? 27.61480 -22.24900 13.80857  1.000 9.65273  ? 139 LEU   B CD1 1 
ATOM   3138 C  CD2 . LEU   B 1 143 ? 27.24121 -23.05398 11.44332  1.000 8.46864  ? 139 LEU   B CD2 1 
ATOM   3139 N  N   . GLY   B 1 144 ? 25.83565 -18.66484 10.02195  1.000 9.71897  ? 140 GLY   B N   1 
ATOM   3140 C  CA  . GLY   B 1 144 ? 25.20684 -17.40581 9.67099   1.000 10.30995 ? 140 GLY   B CA  1 
ATOM   3141 C  C   . GLY   B 1 144 ? 24.05060 -17.62748 8.71771   1.000 11.65049 ? 140 GLY   B C   1 
ATOM   3142 O  O   . GLY   B 1 144 ? 23.75380 -18.77500 8.36808   1.000 9.21704  ? 140 GLY   B O   1 
ATOM   3143 N  N   . ASN   B 1 145 ? 23.38541 -16.55045 8.28733   1.000 10.56114 ? 141 ASN   B N   1 
ATOM   3144 C  CA  . ASN   B 1 145 ? 22.27502 -16.71204 7.35422   1.000 10.41142 ? 141 ASN   B CA  1 
ATOM   3145 C  C   . ASN   B 1 145 ? 22.75329 -17.22195 6.00009   1.000 10.80908 ? 141 ASN   B C   1 
ATOM   3146 O  O   . ASN   B 1 145 ? 22.03190 -17.97297 5.33330   1.000 9.65963  ? 141 ASN   B O   1 
ATOM   3147 C  CB  . ASN   B 1 145 ? 21.52004 -15.39420 7.18940   1.000 13.98005 ? 141 ASN   B CB  1 
ATOM   3148 C  CG  . ASN   B 1 145 ? 20.13388 -15.58649 6.59963   1.000 17.89424 ? 141 ASN   B CG  1 
ATOM   3149 O  OD1 . ASN   B 1 145 ? 19.30415 -16.29878 7.16412   1.000 16.63398 ? 141 ASN   B OD1 1 
ATOM   3150 N  ND2 . ASN   B 1 145 ? 19.87299 -14.94305 5.46320   1.000 15.86266 ? 141 ASN   B ND2 1 
ATOM   3151 N  N   . GLY   B 1 146 ? 23.96121 -16.83763 5.58759   1.000 10.65129 ? 142 GLY   B N   1 
ATOM   3152 C  CA  . GLY   B 1 146 ? 24.52595 -17.26737 4.32828   1.000 11.21507 ? 142 GLY   B CA  1 
ATOM   3153 C  C   . GLY   B 1 146 ? 24.78370 -18.75956 4.27577   1.000 14.10278 ? 142 GLY   B C   1 
ATOM   3154 O  O   . GLY   B 1 146 ? 24.32079 -19.45821 3.36802   1.000 12.59907 ? 142 GLY   B O   1 
ATOM   3155 N  N   . PRO   B 1 147 ? 25.55273 -19.27694 5.24157   1.000 12.10714 ? 143 PRO   B N   1 
ATOM   3156 C  CA  . PRO   B 1 147 ? 25.71270 -20.73700 5.33969   1.000 8.93635  ? 143 PRO   B CA  1 
ATOM   3157 C  C   . PRO   B 1 147 ? 24.39841 -21.49757 5.41663   1.000 10.39124 ? 143 PRO   B C   1 
ATOM   3158 O  O   . PRO   B 1 147 ? 24.29200 -22.58778 4.83881   1.000 12.02821 ? 143 PRO   B O   1 
ATOM   3159 C  CB  . PRO   B 1 147 ? 26.54345 -20.89799 6.61944   1.000 10.26289 ? 143 PRO   B CB  1 
ATOM   3160 C  CG  . PRO   B 1 147 ? 27.39211 -19.66429 6.64630   1.000 10.37707 ? 143 PRO   B CG  1 
ATOM   3161 C  CD  . PRO   B 1 147 ? 26.50169 -18.56163 6.11716   1.000 11.61193 ? 143 PRO   B CD  1 
ATOM   3162 N  N   . LEU   B 1 148 ? 23.38929 -20.95785 6.10779   1.000 8.07784  ? 144 LEU   B N   1 
ATOM   3163 C  CA  . LEU   B 1 148 ? 22.11860 -21.66959 6.20881   1.000 10.80276 ? 144 LEU   B CA  1 
ATOM   3164 C  C   . LEU   B 1 148 ? 21.40354 -21.70782 4.86332   1.000 11.52947 ? 144 LEU   B C   1 
ATOM   3165 O  O   . LEU   B 1 148 ? 20.87618 -22.75383 4.46487   1.000 10.98195 ? 144 LEU   B O   1 
ATOM   3166 C  CB  . LEU   B 1 148 ? 21.23281 -21.03107 7.27817   1.000 9.02683  ? 144 LEU   B CB  1 
ATOM   3167 C  CG  . LEU   B 1 148 ? 19.96943 -21.83322 7.62262   1.000 9.17809  ? 144 LEU   B CG  1 
ATOM   3168 C  CD1 . LEU   B 1 148 ? 20.32999 -23.26381 8.03834   1.000 10.95240 ? 144 LEU   B CD1 1 
ATOM   3169 C  CD2 . LEU   B 1 148 ? 19.14628 -21.14901 8.70397   1.000 16.38877 ? 144 LEU   B CD2 1 
ATOM   3170 N  N   . GLU   B 1 149 ? 21.38008 -20.57695 4.15460   1.000 8.48860  ? 145 GLU   B N   1 
ATOM   3171 C  CA  . GLU   B 1 149 ? 20.84184 -20.53420 2.79578   1.000 8.82165  ? 145 GLU   B CA  1 
ATOM   3172 C  C   . GLU   B 1 149 ? 21.45716 -21.62110 1.91580   1.000 10.39128 ? 145 GLU   B C   1 
ATOM   3173 O  O   . GLU   B 1 149 ? 20.74762 -22.34250 1.20246   1.000 14.89641 ? 145 GLU   B O   1 
ATOM   3174 C  CB  . GLU   B 1 149 ? 21.09407 -19.14937 2.19407   1.000 9.63161  ? 145 GLU   B CB  1 
ATOM   3175 C  CG  . GLU   B 1 149 ? 20.92655 -19.07730 0.67916   1.000 10.79230 ? 145 GLU   B CG  1 
ATOM   3176 C  CD  . GLU   B 1 149 ? 19.52170 -18.68561 0.26683   1.000 17.52195 ? 145 GLU   B CD  1 
ATOM   3177 O  OE1 . GLU   B 1 149 ? 18.79841 -18.11124 1.11004   1.000 15.80537 ? 145 GLU   B OE1 1 
ATOM   3178 O  OE2 . GLU   B 1 149 ? 19.14045 -18.94930 -0.89914  1.000 17.30581 ? 145 GLU   B OE2 1 
ATOM   3179 N  N   . GLU   B 1 150 ? 22.78563 -21.74825 1.95706   1.000 12.76967 ? 146 GLU   B N   1 
ATOM   3180 C  CA  . GLU   B 1 150 ? 23.48320 -22.71528 1.11559   1.000 12.39941 ? 146 GLU   B CA  1 
ATOM   3181 C  C   . GLU   B 1 150 ? 23.25422 -24.14716 1.58481   1.000 10.49386 ? 146 GLU   B C   1 
ATOM   3182 O  O   . GLU   B 1 150 ? 23.20496 -25.06951 0.76042   1.000 10.11139 ? 146 GLU   B O   1 
ATOM   3183 C  CB  . GLU   B 1 150 ? 24.97834 -22.39346 1.09678   1.000 11.65117 ? 146 GLU   B CB  1 
ATOM   3184 C  CG  . GLU   B 1 150 ? 25.29114 -21.00095 0.54759   1.000 20.80540 ? 146 GLU   B CG  1 
ATOM   3185 C  CD  . GLU   B 1 150 ? 26.55456 -20.39778 1.14121   1.000 25.75723 ? 146 GLU   B CD  1 
ATOM   3186 O  OE1 . GLU   B 1 150 ? 27.32109 -21.13434 1.79482   1.000 25.88303 ? 146 GLU   B OE1 1 
ATOM   3187 O  OE2 . GLU   B 1 150 ? 26.77516 -19.18148 0.96358   1.000 25.60786 ? 146 GLU   B OE2 1 
ATOM   3188 N  N   . ALA   B 1 151 ? 23.12620 -24.35121 2.89597   1.000 9.90123  ? 147 ALA   B N   1 
ATOM   3189 C  CA  . ALA   B 1 151 ? 22.84899 -25.68216 3.42102   1.000 7.39595  ? 147 ALA   B CA  1 
ATOM   3190 C  C   . ALA   B 1 151 ? 21.47336 -26.16588 2.98928   1.000 10.30759 ? 147 ALA   B C   1 
ATOM   3191 O  O   . ALA   B 1 151 ? 21.29253 -27.35312 2.68676   1.000 7.38450  ? 147 ALA   B O   1 
ATOM   3192 C  CB  . ALA   B 1 151 ? 22.95799 -25.67660 4.94651   1.000 8.65061  ? 147 ALA   B CB  1 
ATOM   3193 N  N   . ILE   B 1 152 ? 20.49300 -25.25923 2.95707   1.000 7.99470  ? 148 ILE   B N   1 
ATOM   3194 C  CA  . ILE   B 1 152 ? 19.14466 -25.63389 2.54569   1.000 9.21142  ? 148 ILE   B CA  1 
ATOM   3195 C  C   . ILE   B 1 152 ? 19.14999 -26.12142 1.10306   1.000 10.45656 ? 148 ILE   B C   1 
ATOM   3196 O  O   . ILE   B 1 152 ? 18.57012 -27.16721 0.78480   1.000 8.14857  ? 148 ILE   B O   1 
ATOM   3197 C  CB  . ILE   B 1 152 ? 18.17787 -24.45228 2.76159   1.000 8.11747  ? 148 ILE   B CB  1 
ATOM   3198 C  CG1 . ILE   B 1 152 ? 18.00113 -24.19074 4.26162   1.000 13.71253 ? 148 ILE   B CG1 1 
ATOM   3199 C  CG2 . ILE   B 1 152 ? 16.82374 -24.71570 2.11259   1.000 9.64807  ? 148 ILE   B CG2 1 
ATOM   3200 C  CD1 . ILE   B 1 152 ? 17.32890 -22.86849 4.58970   1.000 13.82741 ? 148 ILE   B CD1 1 
ATOM   3201 N  N   . SER   B 1 153 ? 19.82925 -25.39212 0.21143   1.000 10.00356 ? 149 SER   B N   1 
ATOM   3202 C  CA  . SER   B 1 153 ? 19.90573 -25.83167 -1.18006  1.000 9.93918  ? 149 SER   B CA  1 
ATOM   3203 C  C   . SER   B 1 153 ? 20.65025 -27.15726 -1.30078  1.000 10.97706 ? 149 SER   B C   1 
ATOM   3204 O  O   . SER   B 1 153 ? 20.25856 -28.02796 -2.08901  1.000 9.05594  ? 149 SER   B O   1 
ATOM   3205 C  CB  . SER   B 1 153 ? 20.57474 -24.76001 -2.04231  1.000 14.44831 ? 149 SER   B CB  1 
ATOM   3206 O  OG  . SER   B 1 153 ? 19.66680 -23.72255 -2.36896  1.000 12.68691 ? 149 SER   B OG  1 
ATOM   3207 N  N   . ALA   B 1 154 ? 21.71843 -27.33636 -0.51940  1.000 8.70827  ? 150 ALA   B N   1 
ATOM   3208 C  CA  . ALA   B 1 154 ? 22.47748 -28.58261 -0.58858  1.000 10.67242 ? 150 ALA   B CA  1 
ATOM   3209 C  C   . ALA   B 1 154 ? 21.62705 -29.76578 -0.14389  1.000 12.40375 ? 150 ALA   B C   1 
ATOM   3210 O  O   . ALA   B 1 154 ? 21.61985 -30.81581 -0.79603  1.000 10.99638 ? 150 ALA   B O   1 
ATOM   3211 C  CB  . ALA   B 1 154 ? 23.74612 -28.47956 0.25537   1.000 15.41438 ? 150 ALA   B CB  1 
ATOM   3212 N  N   . LEU   B 1 155 ? 20.89852 -29.61298 0.96807   1.000 9.23695  ? 151 LEU   B N   1 
ATOM   3213 C  CA  . LEU   B 1 155 ? 20.00214 -30.67718 1.41296   1.000 12.22438 ? 151 LEU   B CA  1 
ATOM   3214 C  C   . LEU   B 1 155 ? 18.95331 -30.99018 0.35580   1.000 8.54761  ? 151 LEU   B C   1 
ATOM   3215 O  O   . LEU   B 1 155 ? 18.60602 -32.15770 0.13990   1.000 10.36365 ? 151 LEU   B O   1 
ATOM   3216 C  CB  . LEU   B 1 155 ? 19.32205 -30.29350 2.73072   1.000 8.90703  ? 151 LEU   B CB  1 
ATOM   3217 C  CG  . LEU   B 1 155 ? 19.84907 -30.99166 3.98826   1.000 14.84763 ? 151 LEU   B CG  1 
ATOM   3218 C  CD1 . LEU   B 1 155 ? 21.32054 -30.71233 4.16137   1.000 20.18875 ? 151 LEU   B CD1 1 
ATOM   3219 C  CD2 . LEU   B 1 155 ? 19.07779 -30.56856 5.22901   1.000 13.19900 ? 151 LEU   B CD2 1 
ATOM   3220 N  N   . TYR   B 1 156 ? 18.44090 -29.96218 -0.31718  1.000 8.78150  ? 152 TYR   B N   1 
ATOM   3221 C  CA  . TYR   B 1 156 ? 17.38824 -30.18992 -1.30006  1.000 12.01176 ? 152 TYR   B CA  1 
ATOM   3222 C  C   . TYR   B 1 156 ? 17.90513 -30.97271 -2.50312  1.000 12.54863 ? 152 TYR   B C   1 
ATOM   3223 O  O   . TYR   B 1 156 ? 17.23736 -31.89944 -2.97726  1.000 13.57429 ? 152 TYR   B O   1 
ATOM   3224 C  CB  . TYR   B 1 156 ? 16.77723 -28.86291 -1.74975  1.000 11.37755 ? 152 TYR   B CB  1 
ATOM   3225 C  CG  . TYR   B 1 156 ? 15.62131 -29.06088 -2.70893  1.000 16.78719 ? 152 TYR   B CG  1 
ATOM   3226 C  CD1 . TYR   B 1 156 ? 14.32984 -29.25280 -2.23346  1.000 16.02209 ? 152 TYR   B CD1 1 
ATOM   3227 C  CD2 . TYR   B 1 156 ? 15.82460 -29.08491 -4.08496  1.000 17.08825 ? 152 TYR   B CD2 1 
ATOM   3228 C  CE1 . TYR   B 1 156 ? 13.27092 -29.44827 -3.09677  1.000 17.22250 ? 152 TYR   B CE1 1 
ATOM   3229 C  CE2 . TYR   B 1 156 ? 14.77388 -29.28815 -4.95508  1.000 17.00714 ? 152 TYR   B CE2 1 
ATOM   3230 C  CZ  . TYR   B 1 156 ? 13.49748 -29.46439 -4.45598  1.000 18.85254 ? 152 TYR   B CZ  1 
ATOM   3231 O  OH  . TYR   B 1 156 ? 12.44099 -29.66086 -5.31873  1.000 27.30174 ? 152 TYR   B OH  1 
ATOM   3232 N  N   . TYR   B 1 157 ? 19.08358 -30.62098 -3.01592  1.000 10.14106 ? 153 TYR   B N   1 
ATOM   3233 C  CA  . TYR   B 1 157 ? 19.55899 -31.24887 -4.24347  1.000 14.54196 ? 153 TYR   B CA  1 
ATOM   3234 C  C   . TYR   B 1 157 ? 20.23270 -32.59315 -4.01154  1.000 11.88373 ? 153 TYR   B C   1 
ATOM   3235 O  O   . TYR   B 1 157 ? 20.59803 -33.25400 -4.98812  1.000 16.88999 ? 153 TYR   B O   1 
ATOM   3236 C  CB  . TYR   B 1 157 ? 20.51212 -30.31950 -4.99335  1.000 11.02678 ? 153 TYR   B CB  1 
ATOM   3237 C  CG  . TYR   B 1 157 ? 19.79101 -29.18249 -5.67544  1.000 11.65951 ? 153 TYR   B CG  1 
ATOM   3238 C  CD1 . TYR   B 1 157 ? 18.92195 -29.42180 -6.73806  1.000 14.10926 ? 153 TYR   B CD1 1 
ATOM   3239 C  CD2 . TYR   B 1 157 ? 19.97088 -27.87162 -5.25836  1.000 11.16117 ? 153 TYR   B CD2 1 
ATOM   3240 C  CE1 . TYR   B 1 157 ? 18.25559 -28.38099 -7.36406  1.000 21.32118 ? 153 TYR   B CE1 1 
ATOM   3241 C  CE2 . TYR   B 1 157 ? 19.31443 -26.82627 -5.88346  1.000 15.57691 ? 153 TYR   B CE2 1 
ATOM   3242 C  CZ  . TYR   B 1 157 ? 18.45557 -27.08762 -6.92870  1.000 17.07461 ? 153 TYR   B CZ  1 
ATOM   3243 O  OH  . TYR   B 1 157 ? 17.80012 -26.04677 -7.54111  1.000 23.43827 ? 153 TYR   B OH  1 
ATOM   3244 N  N   . TYR   B 1 158 ? 20.40595 -33.02114 -2.76068  1.000 10.07649 ? 154 TYR   B N   1 
ATOM   3245 C  CA  . TYR   B 1 158 ? 20.85858 -34.39061 -2.53985  1.000 10.67668 ? 154 TYR   B CA  1 
ATOM   3246 C  C   . TYR   B 1 158 ? 19.83639 -35.39234 -3.06103  1.000 14.10235 ? 154 TYR   B C   1 
ATOM   3247 O  O   . TYR   B 1 158 ? 20.20075 -36.50096 -3.46815  1.000 15.67865 ? 154 TYR   B O   1 
ATOM   3248 C  CB  . TYR   B 1 158 ? 21.13589 -34.62765 -1.05541  1.000 12.33676 ? 154 TYR   B CB  1 
ATOM   3249 C  CG  . TYR   B 1 158 ? 21.82973 -35.93976 -0.77789  1.000 18.26241 ? 154 TYR   B CG  1 
ATOM   3250 C  CD1 . TYR   B 1 158 ? 23.18204 -36.10252 -1.05499  1.000 16.01849 ? 154 TYR   B CD1 1 
ATOM   3251 C  CD2 . TYR   B 1 158 ? 21.13630 -37.01620 -0.24323  1.000 17.22058 ? 154 TYR   B CD2 1 
ATOM   3252 C  CE1 . TYR   B 1 158 ? 23.82186 -37.29835 -0.80800  1.000 19.90687 ? 154 TYR   B CE1 1 
ATOM   3253 C  CE2 . TYR   B 1 158 ? 21.77045 -38.22124 0.00682   1.000 19.33343 ? 154 TYR   B CE2 1 
ATOM   3254 C  CZ  . TYR   B 1 158 ? 23.11160 -38.35407 -0.27608  1.000 25.25732 ? 154 TYR   B CZ  1 
ATOM   3255 O  OH  . TYR   B 1 158 ? 23.74849 -39.54661 -0.02918  1.000 28.50855 ? 154 TYR   B OH  1 
ATOM   3256 N  N   . SER   B 1 159 ? 18.55709 -35.01104 -3.08014  1.000 13.85987 ? 155 SER   B N   1 
ATOM   3257 C  CA  . SER   B 1 159 ? 17.50751 -35.92243 -3.51204  1.000 14.72354 ? 155 SER   B CA  1 
ATOM   3258 C  C   . SER   B 1 159 ? 17.62893 -36.29861 -4.98325  1.000 21.44105 ? 155 SER   B C   1 
ATOM   3259 O  O   . SER   B 1 159 ? 17.04395 -37.30585 -5.40037  1.000 18.45016 ? 155 SER   B O   1 
ATOM   3260 C  CB  . SER   B 1 159 ? 16.13850 -35.30199 -3.24127  1.000 23.93956 ? 155 SER   B CB  1 
ATOM   3261 O  OG  . SER   B 1 159 ? 16.01679 -34.05288 -3.90140  1.000 25.40776 ? 155 SER   B OG  1 
ATOM   3262 N  N   . THR   B 1 160 ? 18.37049 -35.51925 -5.77735  1.000 14.86246 ? 156 THR   B N   1 
ATOM   3263 C  CA  . THR   B 1 160 ? 18.61556 -35.84302 -7.17990  1.000 17.44242 ? 156 THR   B CA  1 
ATOM   3264 C  C   . THR   B 1 160 ? 20.10274 -36.03992 -7.47091  1.000 28.75564 ? 156 THR   B C   1 
ATOM   3265 O  O   . THR   B 1 160 ? 20.52517 -35.95952 -8.63076  1.000 22.60361 ? 156 THR   B O   1 
ATOM   3266 C  CB  . THR   B 1 160 ? 18.02848 -34.76124 -8.09143  1.000 20.03929 ? 156 THR   B CB  1 
ATOM   3267 O  OG1 . THR   B 1 160 ? 18.50180 -33.47245 -7.68368  1.000 22.35988 ? 156 THR   B OG1 1 
ATOM   3268 C  CG2 . THR   B 1 160 ? 16.50420 -34.78014 -8.02663  1.000 24.65820 ? 156 THR   B CG2 1 
ATOM   3269 N  N   . GLY   B 1 161 ? 20.90478 -36.31189 -6.44336  1.000 20.21622 ? 157 GLY   B N   1 
ATOM   3270 C  CA  . GLY   B 1 161 ? 22.31604 -36.57861 -6.62637  1.000 20.84533 ? 157 GLY   B CA  1 
ATOM   3271 C  C   . GLY   B 1 161 ? 23.17357 -35.37177 -6.93223  1.000 24.80833 ? 157 GLY   B C   1 
ATOM   3272 O  O   . GLY   B 1 161 ? 24.36144 -35.53968 -7.23584  1.000 24.25478 ? 157 GLY   B O   1 
ATOM   3273 N  N   . GLY   B 1 162 ? 22.61860 -34.16389 -6.86118  1.000 23.02934 ? 158 GLY   B N   1 
ATOM   3274 C  CA  . GLY   B 1 162 ? 23.32751 -32.93959 -7.17040  1.000 19.36314 ? 158 GLY   B CA  1 
ATOM   3275 C  C   . GLY   B 1 162 ? 24.17423 -32.38233 -6.04908  1.000 26.99822 ? 158 GLY   B C   1 
ATOM   3276 O  O   . GLY   B 1 162 ? 24.77304 -31.31375 -6.21172  1.000 26.63687 ? 158 GLY   B O   1 
ATOM   3277 N  N   . THR   B 1 163 ? 24.23675 -33.06957 -4.91126  1.000 18.54216 ? 159 THR   B N   1 
ATOM   3278 C  CA  . THR   B 1 163 ? 25.05840 -32.66812 -3.77667  1.000 19.82376 ? 159 THR   B CA  1 
ATOM   3279 C  C   . THR   B 1 163 ? 25.95052 -33.83998 -3.39630  1.000 13.76876 ? 159 THR   B C   1 
ATOM   3280 O  O   . THR   B 1 163 ? 25.46632 -34.96726 -3.25695  1.000 15.33543 ? 159 THR   B O   1 
ATOM   3281 C  CB  . THR   B 1 163 ? 24.18631 -32.24845 -2.58313  1.000 13.90493 ? 159 THR   B CB  1 
ATOM   3282 O  OG1 . THR   B 1 163 ? 23.38588 -31.11424 -2.94136  1.000 17.52043 ? 159 THR   B OG1 1 
ATOM   3283 C  CG2 . THR   B 1 163 ? 25.04043 -31.90876 -1.36292  1.000 10.06808 ? 159 THR   B CG2 1 
ATOM   3284 N  N   . GLN   B 1 164 ? 27.24500 -33.57748 -3.23934  1.000 13.30780 ? 160 GLN   B N   1 
ATOM   3285 C  CA  . GLN   B 1 164 ? 28.16756 -34.60416 -2.78488  1.000 18.60929 ? 160 GLN   B CA  1 
ATOM   3286 C  C   . GLN   B 1 164 ? 28.04473 -34.80427 -1.27731  1.000 15.69277 ? 160 GLN   B C   1 
ATOM   3287 O  O   . GLN   B 1 164 ? 27.59155 -33.92296 -0.53878  1.000 12.31055 ? 160 GLN   B O   1 
ATOM   3288 C  CB  . GLN   B 1 164 ? 29.60381 -34.23872 -3.14434  1.000 15.72094 ? 160 GLN   B CB  1 
ATOM   3289 C  CG  . GLN   B 1 164 ? 29.77631 -33.81516 -4.58806  1.000 30.50138 ? 160 GLN   B CG  1 
ATOM   3290 C  CD  . GLN   B 1 164 ? 31.12390 -34.20806 -5.14445  1.000 41.49461 ? 160 GLN   B CD  1 
ATOM   3291 O  OE1 . GLN   B 1 164 ? 31.29862 -35.31922 -5.64314  1.000 55.88247 ? 160 GLN   B OE1 1 
ATOM   3292 N  NE2 . GLN   B 1 164 ? 32.08916 -33.29981 -5.06021  1.000 53.32638 ? 160 GLN   B NE2 1 
ATOM   3293 N  N   . LEU   B 1 165 ? 28.46602 -35.98583 -0.82456  1.000 13.72034 ? 161 LEU   B N   1 
ATOM   3294 C  CA  . LEU   B 1 165 ? 28.30976 -36.33153 0.58688   1.000 12.63581 ? 161 LEU   B CA  1 
ATOM   3295 C  C   . LEU   B 1 165 ? 29.01997 -35.35633 1.51702   1.000 12.75819 ? 161 LEU   B C   1 
ATOM   3296 O  O   . LEU   B 1 165 ? 28.40142 -34.92896 2.50754   1.000 12.97584 ? 161 LEU   B O   1 
ATOM   3297 C  CB  . LEU   B 1 165 ? 28.77280 -37.77422 0.82051   1.000 20.15088 ? 161 LEU   B CB  1 
ATOM   3298 C  CG  . LEU   B 1 165 ? 28.55870 -38.33522 2.22730   1.000 23.41598 ? 161 LEU   B CG  1 
ATOM   3299 C  CD1 . LEU   B 1 165 ? 27.09115 -38.23739 2.63065   1.000 17.55798 ? 161 LEU   B CD1 1 
ATOM   3300 C  CD2 . LEU   B 1 165 ? 29.04690 -39.77160 2.30275   1.000 25.31556 ? 161 LEU   B CD2 1 
ATOM   3301 N  N   . PRO   B 1 166 ? 30.28253 -34.96440 1.28614   1.000 12.55266 ? 162 PRO   B N   1 
ATOM   3302 C  CA  . PRO   B 1 166 ? 30.90360 -34.00235 2.21425   1.000 17.43108 ? 162 PRO   B CA  1 
ATOM   3303 C  C   . PRO   B 1 166 ? 30.13385 -32.70030 2.33130   1.000 14.94577 ? 162 PRO   B C   1 
ATOM   3304 O  O   . PRO   B 1 166 ? 30.03128 -32.14632 3.43231   1.000 13.76614 ? 162 PRO   B O   1 
ATOM   3305 C  CB  . PRO   B 1 166 ? 32.30160 -33.79673 1.61552   1.000 15.35288 ? 162 PRO   B CB  1 
ATOM   3306 C  CG  . PRO   B 1 166 ? 32.58120 -35.07765 0.90315   1.000 15.65386 ? 162 PRO   B CG  1 
ATOM   3307 C  CD  . PRO   B 1 166 ? 31.26169 -35.47126 0.30380   1.000 23.26856 ? 162 PRO   B CD  1 
ATOM   3308 N  N   . THR   B 1 167 ? 29.57084 -32.20604 1.22516   1.000 9.51357  ? 163 THR   B N   1 
ATOM   3309 C  CA  . THR   B 1 167 ? 28.76588 -30.98868 1.27605   1.000 10.41873 ? 163 THR   B CA  1 
ATOM   3310 C  C   . THR   B 1 167 ? 27.47524 -31.20475 2.06023   1.000 12.58625 ? 163 THR   B C   1 
ATOM   3311 O  O   . THR   B 1 167 ? 27.02917 -30.30997 2.78898   1.000 10.58915 ? 163 THR   B O   1 
ATOM   3312 C  CB  . THR   B 1 167 ? 28.45772 -30.51251 -0.14229  1.000 17.47502 ? 163 THR   B CB  1 
ATOM   3313 O  OG1 . THR   B 1 167 ? 29.68584 -30.30794 -0.85108  1.000 24.01848 ? 163 THR   B OG1 1 
ATOM   3314 C  CG2 . THR   B 1 167 ? 27.67003 -29.21779 -0.11702  1.000 12.30418 ? 163 THR   B CG2 1 
ATOM   3315 N  N   . LEU   B 1 168 ? 26.85801 -32.38270 1.91910   1.000 8.92393  ? 164 LEU   B N   1 
ATOM   3316 C  CA  . LEU   B 1 168 ? 25.67738 -32.70178 2.71614   1.000 8.79293  ? 164 LEU   B CA  1 
ATOM   3317 C  C   . LEU   B 1 168 ? 26.01566 -32.73684 4.20219   1.000 10.12636 ? 164 LEU   B C   1 
ATOM   3318 O  O   . LEU   B 1 168 ? 25.27665 -32.19319 5.02995   1.000 9.32570  ? 164 LEU   B O   1 
ATOM   3319 C  CB  . LEU   B 1 168 ? 25.09091 -34.04250 2.27368   1.000 13.92760 ? 164 LEU   B CB  1 
ATOM   3320 C  CG  . LEU   B 1 168 ? 23.80783 -34.48540 2.98665   1.000 11.89173 ? 164 LEU   B CG  1 
ATOM   3321 C  CD1 . LEU   B 1 168 ? 22.59392 -33.75083 2.42173   1.000 12.79786 ? 164 LEU   B CD1 1 
ATOM   3322 C  CD2 . LEU   B 1 168 ? 23.62170 -35.99211 2.88098   1.000 13.73251 ? 164 LEU   B CD2 1 
ATOM   3323 N  N   . ALA   B 1 169 ? 27.12915 -33.37979 4.55694   1.000 9.04958  ? 165 ALA   B N   1 
ATOM   3324 C  CA  . ALA   B 1 169 ? 27.51548 -33.47193 5.96221   1.000 9.09898  ? 165 ALA   B CA  1 
ATOM   3325 C  C   . ALA   B 1 169 ? 27.79513 -32.09351 6.54771   1.000 12.09338 ? 165 ALA   B C   1 
ATOM   3326 O  O   . ALA   B 1 169 ? 27.40982 -31.80289 7.68641   1.000 13.50920 ? 165 ALA   B O   1 
ATOM   3327 C  CB  . ALA   B 1 169 ? 28.73766 -34.37392 6.10766   1.000 11.67844 ? 165 ALA   B CB  1 
ATOM   3328 N  N   . ARG   B 1 170 ? 28.47398 -31.23492 5.78725   1.000 8.69316  ? 166 ARG   B N   1 
ATOM   3329 C  CA  . ARG   B 1 170 ? 28.67810 -29.86203 6.23485   1.000 12.73030 ? 166 ARG   B CA  1 
ATOM   3330 C  C   . ARG   B 1 170 ? 27.34988 -29.13336 6.39985   1.000 9.25934  ? 166 ARG   B C   1 
ATOM   3331 O  O   . ARG   B 1 170 ? 27.17252 -28.35615 7.34472   1.000 9.49743  ? 166 ARG   B O   1 
ATOM   3332 C  CB  . ARG   B 1 170 ? 29.58290 -29.11619 5.25470   1.000 16.30390 ? 166 ARG   B CB  1 
ATOM   3333 C  CG  . ARG   B 1 170 ? 29.84916 -27.68267 5.66968   1.000 20.04265 ? 166 ARG   B CG  1 
ATOM   3334 C  CD  . ARG   B 1 170 ? 31.03715 -27.08756 4.93942   1.000 28.97757 ? 166 ARG   B CD  1 
ATOM   3335 N  NE  . ARG   B 1 170 ? 30.83371 -27.00664 3.49685   1.000 32.92104 ? 166 ARG   B NE  1 
ATOM   3336 C  CZ  . ARG   B 1 170 ? 31.36651 -27.84394 2.61664   1.000 32.31887 ? 166 ARG   B CZ  1 
ATOM   3337 N  NH1 . ARG   B 1 170 ? 32.12981 -28.85473 2.99843   1.000 30.82395 ? 166 ARG   B NH1 1 
ATOM   3338 N  NH2 . ARG   B 1 170 ? 31.13182 -27.65770 1.32090   1.000 34.62960 ? 166 ARG   B NH2 1 
ATOM   3339 N  N   . SER   B 1 171 ? 26.39798 -29.37829 5.49720   1.000 7.99830  ? 167 SER   B N   1 
ATOM   3340 C  CA  . SER   B 1 171 ? 25.09739 -28.72846 5.61549   1.000 7.86925  ? 167 SER   B CA  1 
ATOM   3341 C  C   . SER   B 1 171 ? 24.34852 -29.21102 6.85701   1.000 9.07764  ? 167 SER   B C   1 
ATOM   3342 O  O   . SER   B 1 171 ? 23.69826 -28.41509 7.54488   1.000 12.71671 ? 167 SER   B O   1 
ATOM   3343 C  CB  . SER   B 1 171 ? 24.28762 -28.96249 4.34275   1.000 12.90955 ? 167 SER   B CB  1 
ATOM   3344 O  OG  . SER   B 1 171 ? 24.98770 -28.47486 3.20756   1.000 8.07717  ? 167 SER   B OG  1 
ATOM   3345 N  N   . PHE   B 1 172 ? 24.45046 -30.50417 7.17943   1.000 8.07771  ? 168 PHE   B N   1 
ATOM   3346 C  CA  . PHE   B 1 172 ? 23.88348 -30.99782 8.43337   1.000 10.61728 ? 168 PHE   B CA  1 
ATOM   3347 C  C   . PHE   B 1 172 ? 24.48742 -30.29095 9.64044   1.000 13.65988 ? 168 PHE   B C   1 
ATOM   3348 O  O   . PHE   B 1 172 ? 23.76439 -29.90886 10.56898  1.000 10.21029 ? 168 PHE   B O   1 
ATOM   3349 C  CB  . PHE   B 1 172 ? 24.09257 -32.50555 8.55108   1.000 8.46738  ? 168 PHE   B CB  1 
ATOM   3350 C  CG  . PHE   B 1 172 ? 23.14282 -33.30869 7.72136   1.000 13.12366 ? 168 PHE   B CG  1 
ATOM   3351 C  CD1 . PHE   B 1 172 ? 21.80744 -32.95759 7.64627   1.000 18.88933 ? 168 PHE   B CD1 1 
ATOM   3352 C  CD2 . PHE   B 1 172 ? 23.58333 -34.41700 7.01647   1.000 14.88485 ? 168 PHE   B CD2 1 
ATOM   3353 C  CE1 . PHE   B 1 172 ? 20.93158 -33.69410 6.89090   1.000 15.54474 ? 168 PHE   B CE1 1 
ATOM   3354 C  CE2 . PHE   B 1 172 ? 22.70786 -35.15849 6.26055   1.000 15.91518 ? 168 PHE   B CE2 1 
ATOM   3355 C  CZ  . PHE   B 1 172 ? 21.38203 -34.79532 6.19491   1.000 18.00109 ? 168 PHE   B CZ  1 
ATOM   3356 N  N   . ILE   B 1 173 ? 25.81187 -30.11379 9.65232   1.000 11.58936 ? 169 ILE   B N   1 
ATOM   3357 C  CA  . ILE   B 1 173 ? 26.46585 -29.47744 10.79588  1.000 10.68845 ? 169 ILE   B CA  1 
ATOM   3358 C  C   . ILE   B 1 173 ? 25.97446 -28.04305 10.96371  1.000 7.76310  ? 169 ILE   B C   1 
ATOM   3359 O  O   . ILE   B 1 173 ? 25.80467 -27.55484 12.08831  1.000 10.65896 ? 169 ILE   B O   1 
ATOM   3360 C  CB  . ILE   B 1 173 ? 27.99686 -29.54232 10.63173  1.000 10.57283 ? 169 ILE   B CB  1 
ATOM   3361 C  CG1 . ILE   B 1 173 ? 28.48493 -30.98693 10.77039  1.000 9.04211  ? 169 ILE   B CG1 1 
ATOM   3362 C  CG2 . ILE   B 1 173 ? 28.69536 -28.64902 11.64507  1.000 13.41420 ? 169 ILE   B CG2 1 
ATOM   3363 C  CD1 . ILE   B 1 173 ? 29.93128 -31.17392 10.34661  1.000 9.10348  ? 169 ILE   B CD1 1 
ATOM   3364 N  N   . ILE   B 1 174 ? 25.72701 -27.35370 9.84993   1.000 7.62599  ? 170 ILE   B N   1 
ATOM   3365 C  CA  . ILE   B 1 174 ? 25.21310 -25.98751 9.90167   1.000 8.22512  ? 170 ILE   B CA  1 
ATOM   3366 C  C   . ILE   B 1 174 ? 23.79762 -25.97152 10.46714  1.000 9.14371  ? 170 ILE   B C   1 
ATOM   3367 O  O   . ILE   B 1 174 ? 23.47117 -25.16921 11.35114  1.000 9.34014  ? 170 ILE   B O   1 
ATOM   3368 C  CB  . ILE   B 1 174 ? 25.26283 -25.34681 8.49967   1.000 9.88298  ? 170 ILE   B CB  1 
ATOM   3369 C  CG1 . ILE   B 1 174 ? 26.70717 -25.13489 8.04858   1.000 8.39031  ? 170 ILE   B CG1 1 
ATOM   3370 C  CG2 . ILE   B 1 174 ? 24.49808 -24.03067 8.48002   1.000 14.39732 ? 170 ILE   B CG2 1 
ATOM   3371 C  CD1 . ILE   B 1 174 ? 26.85099 -24.86829 6.54515   1.000 12.02825 ? 170 ILE   B CD1 1 
ATOM   3372 N  N   . CYS   B 1 175 ? 22.93451 -26.85762 9.96487   1.000 10.15463 ? 171 CYS   B N   1 
ATOM   3373 C  CA  . CYS   B 1 175 ? 21.54251 -26.86908 10.41169  1.000 12.88355 ? 171 CYS   B CA  1 
ATOM   3374 C  C   . CYS   B 1 175 ? 21.42722 -27.26952 11.87665  1.000 15.05538 ? 171 CYS   B C   1 
ATOM   3375 O  O   . CYS   B 1 175 ? 20.64919 -26.67153 12.63195  1.000 14.69818 ? 171 CYS   B O   1 
ATOM   3376 C  CB  . CYS   B 1 175 ? 20.71901 -27.81136 9.53652   1.000 17.70233 ? 171 CYS   B CB  1 
ATOM   3377 S  SG  . CYS   B 1 175 ? 20.44578 -27.20634 7.85558   1.000 18.68311 ? 171 CYS   B SG  1 
ATOM   3378 N  N   . ILE   B 1 176 ? 22.19310 -28.27768 12.29679  1.000 9.48472  ? 172 ILE   B N   1 
ATOM   3379 C  CA  . ILE   B 1 176 ? 22.08259 -28.77482 13.66435  1.000 11.94325 ? 172 ILE   B CA  1 
ATOM   3380 C  C   . ILE   B 1 176 ? 22.44372 -27.68388 14.66317  1.000 11.69131 ? 172 ILE   B C   1 
ATOM   3381 O  O   . ILE   B 1 176 ? 21.74785 -27.48914 15.66656  1.000 12.18509 ? 172 ILE   B O   1 
ATOM   3382 C  CB  . ILE   B 1 176 ? 22.95240 -30.03162 13.84288  1.000 9.21281  ? 172 ILE   B CB  1 
ATOM   3383 C  CG1 . ILE   B 1 176 ? 22.33936 -31.20096 13.06331  1.000 13.79878 ? 172 ILE   B CG1 1 
ATOM   3384 C  CG2 . ILE   B 1 176 ? 23.10164 -30.37770 15.32000  1.000 11.43399 ? 172 ILE   B CG2 1 
ATOM   3385 C  CD1 . ILE   B 1 176 ? 23.26095 -32.39160 12.91017  1.000 12.11419 ? 172 ILE   B CD1 1 
ATOM   3386 N  N   . GLN   B 1 177 ? 23.51212 -26.93058 14.39248  1.000 8.62568  ? 173 GLN   B N   1 
ATOM   3387 C  CA  . GLN   B 1 177 ? 23.91204 -25.88249 15.33035  1.000 11.09012 ? 173 GLN   B CA  1 
ATOM   3388 C  C   . GLN   B 1 177 ? 22.91753 -24.72680 15.34567  1.000 9.81465  ? 173 GLN   B C   1 
ATOM   3389 O  O   . GLN   B 1 177 ? 22.57200 -24.21542 16.41727  1.000 10.66286 ? 173 GLN   B O   1 
ATOM   3390 C  CB  . GLN   B 1 177 ? 25.31637 -25.38176 14.99439  1.000 10.40059 ? 173 GLN   B CB  1 
ATOM   3391 C  CG  . GLN   B 1 177 ? 26.38382 -26.45130 15.14242  1.000 9.75664  ? 173 GLN   B CG  1 
ATOM   3392 C  CD  . GLN   B 1 177 ? 27.77621 -25.92356 14.86160  1.000 12.10807 ? 173 GLN   B CD  1 
ATOM   3393 O  OE1 . GLN   B 1 177 ? 28.46404 -25.45856 15.76327  1.000 11.63508 ? 173 GLN   B OE1 1 
ATOM   3394 N  NE2 . GLN   B 1 177 ? 28.19482 -25.98801 13.60173  1.000 11.73282 ? 173 GLN   B NE2 1 
ATOM   3395 N  N   . MET   B 1 178 ? 22.44384 -24.29478 14.17473  1.000 7.68091  ? 174 MET   B N   1 
ATOM   3396 C  CA  . MET   B 1 178 ? 21.60028 -23.10947 14.12682  1.000 7.81684  ? 174 MET   B CA  1 
ATOM   3397 C  C   . MET   B 1 178 ? 20.15736 -23.38273 14.53568  1.000 11.40338 ? 174 MET   B C   1 
ATOM   3398 O  O   . MET   B 1 178 ? 19.38838 -22.42782 14.68232  1.000 10.20717 ? 174 MET   B O   1 
ATOM   3399 C  CB  . MET   B 1 178 ? 21.63536 -22.49171 12.72356  1.000 10.46252 ? 174 MET   B CB  1 
ATOM   3400 C  CG  . MET   B 1 178 ? 23.03661 -22.09342 12.27048  1.000 13.88158 ? 174 MET   B CG  1 
ATOM   3401 S  SD  . MET   B 1 178 ? 23.08035 -21.06516 10.78339  1.000 13.30368 ? 174 MET   B SD  1 
ATOM   3402 C  CE  . MET   B 1 178 ? 22.26811 -19.57517 11.35587  1.000 14.96342 ? 174 MET   B CE  1 
ATOM   3403 N  N   . ILE   B 1 179 ? 19.77589 -24.64709 14.72710  1.000 10.14896 ? 175 ILE   B N   1 
ATOM   3404 C  CA  . ILE   B 1 179 ? 18.41808 -25.00427 15.13132  1.000 8.65131  ? 175 ILE   B CA  1 
ATOM   3405 C  C   . ILE   B 1 179 ? 18.45502 -25.77085 16.45002  1.000 11.12628 ? 175 ILE   B C   1 
ATOM   3406 O  O   . ILE   B 1 179 ? 17.93628 -25.29881 17.46747  1.000 15.21958 ? 175 ILE   B O   1 
ATOM   3407 C  CB  . ILE   B 1 179 ? 17.71152 -25.83181 14.04069  1.000 11.85796 ? 175 ILE   B CB  1 
ATOM   3408 C  CG1 . ILE   B 1 179 ? 17.64254 -25.04871 12.72737  1.000 14.17822 ? 175 ILE   B CG1 1 
ATOM   3409 C  CG2 . ILE   B 1 179 ? 16.30844 -26.23784 14.49567  1.000 8.96985  ? 175 ILE   B CG2 1 
ATOM   3410 C  CD1 . ILE   B 1 179 ? 17.15177 -25.87206 11.56460  1.000 15.57589 ? 175 ILE   B CD1 1 
ATOM   3411 N  N   . SER   B 1 180 ? 19.07187 -26.95859 16.44451  1.000 8.49324  ? 176 SER   B N   1 
ATOM   3412 C  CA  . SER   B 1 180 ? 19.07536 -27.79566 17.64290  1.000 12.26310 ? 176 SER   B CA  1 
ATOM   3413 C  C   . SER   B 1 180 ? 19.88717 -27.16165 18.76719  1.000 10.39354 ? 176 SER   B C   1 
ATOM   3414 O  O   . SER   B 1 180 ? 19.39905 -27.02444 19.89586  1.000 10.70268 ? 176 SER   B O   1 
ATOM   3415 C  CB  . SER   B 1 180 ? 19.61442 -29.18932 17.31873  1.000 15.14248 ? 176 SER   B CB  1 
ATOM   3416 O  OG  . SER   B 1 180 ? 18.75771 -29.88084 16.42327  1.000 18.25888 ? 176 SER   B OG  1 
ATOM   3417 N  N   . GLU   B 1 181 ? 21.13982 -26.79189 18.49101  1.000 11.29177 ? 177 GLU   B N   1 
ATOM   3418 C  CA  . GLU   B 1 181 ? 21.97317 -26.22559 19.54898  1.000 9.28197  ? 177 GLU   B CA  1 
ATOM   3419 C  C   . GLU   B 1 181 ? 21.44777 -24.86761 20.00560  1.000 14.78109 ? 177 GLU   B C   1 
ATOM   3420 O  O   . GLU   B 1 181 ? 21.48685 -24.55110 21.20237  1.000 8.80726  ? 177 GLU   B O   1 
ATOM   3421 C  CB  . GLU   B 1 181 ? 23.42569 -26.11624 19.08058  1.000 11.59722 ? 177 GLU   B CB  1 
ATOM   3422 C  CG  . GLU   B 1 181 ? 24.06073 -27.44006 18.67834  1.000 11.26478 ? 177 GLU   B CG  1 
ATOM   3423 C  CD  . GLU   B 1 181 ? 24.32206 -28.38508 19.84865  1.000 22.18679 ? 177 GLU   B CD  1 
ATOM   3424 O  OE1 . GLU   B 1 181 ? 23.97713 -28.04980 21.00462  1.000 19.19834 ? 177 GLU   B OE1 1 
ATOM   3425 O  OE2 . GLU   B 1 181 ? 24.88298 -29.47692 19.60490  1.000 24.98556 ? 177 GLU   B OE2 1 
ATOM   3426 N  N   . ALA   B 1 182 ? 20.94555 -24.05625 19.06967  1.000 11.68584 ? 178 ALA   B N   1 
ATOM   3427 C  CA  . ALA   B 1 182 ? 20.34395 -22.77623 19.43735  1.000 8.62576  ? 178 ALA   B CA  1 
ATOM   3428 C  C   . ALA   B 1 182 ? 19.13099 -22.96864 20.33943  1.000 11.92467 ? 178 ALA   B C   1 
ATOM   3429 O  O   . ALA   B 1 182 ? 18.92563 -22.20017 21.28855  1.000 14.01911 ? 178 ALA   B O   1 
ATOM   3430 C  CB  . ALA   B 1 182 ? 19.95514 -22.00021 18.17882  1.000 9.78225  ? 178 ALA   B CB  1 
ATOM   3431 N  N   . ALA   B 1 183 ? 18.31361 -23.98971 20.06328  1.000 10.14838 ? 179 ALA   B N   1 
ATOM   3432 C  CA  . ALA   B 1 183 ? 17.19032 -24.28864 20.94629  1.000 10.85909 ? 179 ALA   B CA  1 
ATOM   3433 C  C   . ALA   B 1 183 ? 17.67163 -24.70000 22.33209  1.000 9.76229  ? 179 ALA   B C   1 
ATOM   3434 O  O   . ALA   B 1 183 ? 17.07489 -24.31252 23.34575  1.000 11.43227 ? 179 ALA   B O   1 
ATOM   3435 C  CB  . ALA   B 1 183 ? 16.31763 -25.38368 20.33540  1.000 10.94826 ? 179 ALA   B CB  1 
ATOM   3436 N  N   . ARG   B 1 184 ? 18.76556 -25.46733 22.39704  1.000 9.54892  ? 180 ARG   B N   1 
ATOM   3437 C  CA  . ARG   B 1 184 ? 19.25860 -25.97449 23.67893  1.000 9.80954  ? 180 ARG   B CA  1 
ATOM   3438 C  C   . ARG   B 1 184 ? 19.88004 -24.88363 24.54796  1.000 10.00654 ? 180 ARG   B C   1 
ATOM   3439 O  O   . ARG   B 1 184 ? 19.80796 -24.96444 25.78297  1.000 11.50961 ? 180 ARG   B O   1 
ATOM   3440 C  CB  . ARG   B 1 184 ? 20.29454 -27.07089 23.44631  1.000 9.69781  ? 180 ARG   B CB  1 
ATOM   3441 C  CG  . ARG   B 1 184 ? 19.77211 -28.35549 22.84443  1.000 10.06506 ? 180 ARG   B CG  1 
ATOM   3442 C  CD  . ARG   B 1 184 ? 20.95434 -29.22930 22.44678  1.000 11.33051 ? 180 ARG   B CD  1 
ATOM   3443 N  NE  . ARG   B 1 184 ? 20.56415 -30.59192 22.11148  1.000 13.02338 ? 180 ARG   B NE  1 
ATOM   3444 C  CZ  . ARG   B 1 184 ? 21.41650 -31.53892 21.74336  1.000 24.90386 ? 180 ARG   B CZ  1 
ATOM   3445 N  NH1 . ARG   B 1 184 ? 22.71029 -31.29248 21.62108  1.000 22.68334 ? 180 ARG   B NH1 1 
ATOM   3446 N  NH2 . ARG   B 1 184 ? 20.96035 -32.76578 21.49947  1.000 18.46626 ? 180 ARG   B NH2 1 
ATOM   3447 N  N   . PHE   B 1 185 ? 20.52351 -23.88681 23.93958  1.000 10.09734 ? 181 PHE   B N   1 
ATOM   3448 C  CA  . PHE   B 1 185 ? 21.27897 -22.86976 24.66882  1.000 10.58826 ? 181 PHE   B CA  1 
ATOM   3449 C  C   . PHE   B 1 185 ? 20.85066 -21.48278 24.21149  1.000 9.65366  ? 181 PHE   B C   1 
ATOM   3450 O  O   . PHE   B 1 185 ? 20.95699 -21.16566 23.02194  1.000 11.77311 ? 181 PHE   B O   1 
ATOM   3451 C  CB  . PHE   B 1 185 ? 22.78946 -23.01762 24.44207  1.000 10.39098 ? 181 PHE   B CB  1 
ATOM   3452 C  CG  . PHE   B 1 185 ? 23.37635 -24.30789 24.94004  1.000 11.14218 ? 181 PHE   B CG  1 
ATOM   3453 C  CD1 . PHE   B 1 185 ? 23.84581 -24.41568 26.24260  1.000 11.78431 ? 181 PHE   B CD1 1 
ATOM   3454 C  CD2 . PHE   B 1 185 ? 23.50737 -25.39454 24.09422  1.000 9.75470  ? 181 PHE   B CD2 1 
ATOM   3455 C  CE1 . PHE   B 1 185 ? 24.40702 -25.59471 26.69466  1.000 11.39431 ? 181 PHE   B CE1 1 
ATOM   3456 C  CE2 . PHE   B 1 185 ? 24.06791 -26.58118 24.54144  1.000 9.78811  ? 181 PHE   B CE2 1 
ATOM   3457 C  CZ  . PHE   B 1 185 ? 24.51886 -26.68179 25.83580  1.000 11.03400 ? 181 PHE   B CZ  1 
ATOM   3458 N  N   . GLN   B 1 186 ? 20.40610 -20.64086 25.15346  1.000 12.80914 ? 182 GLN   B N   1 
ATOM   3459 C  CA  . GLN   B 1 186 ? 20.22732 -19.22715 24.82288  1.000 14.42568 ? 182 GLN   B CA  1 
ATOM   3460 C  C   . GLN   B 1 186 ? 21.53709 -18.59844 24.37796  1.000 9.99076  ? 182 GLN   B C   1 
ATOM   3461 O  O   . GLN   B 1 186 ? 21.53470 -17.67899 23.55264  1.000 13.81949 ? 182 GLN   B O   1 
ATOM   3462 C  CB  . GLN   B 1 186 ? 19.67623 -18.43788 26.01357  1.000 14.63102 ? 182 GLN   B CB  1 
ATOM   3463 C  CG  . GLN   B 1 186 ? 18.36992 -18.93710 26.58303  1.000 19.60293 ? 182 GLN   B CG  1 
ATOM   3464 C  CD  . GLN   B 1 186 ? 18.58761 -19.77849 27.81338  1.000 24.70752 ? 182 GLN   B CD  1 
ATOM   3465 O  OE1 . GLN   B 1 186 ? 19.52761 -20.56659 27.86887  1.000 21.19060 ? 182 GLN   B OE1 1 
ATOM   3466 N  NE2 . GLN   B 1 186 ? 17.73457 -19.60404 28.81867  1.000 24.49029 ? 182 GLN   B NE2 1 
ATOM   3467 N  N   . TYR   B 1 187 ? 22.66169 -19.07316 24.91908  1.000 9.96076  ? 183 TYR   B N   1 
ATOM   3468 C  CA  . TYR   B 1 187 ? 23.96119 -18.53868 24.52457  1.000 10.91859 ? 183 TYR   B CA  1 
ATOM   3469 C  C   . TYR   B 1 187 ? 24.20050 -18.71992 23.03228  1.000 14.82627 ? 183 TYR   B C   1 
ATOM   3470 O  O   . TYR   B 1 187 ? 24.62989 -17.78749 22.34206  1.000 10.85809 ? 183 TYR   B O   1 
ATOM   3471 C  CB  . TYR   B 1 187 ? 25.07735 -19.21033 25.32282  1.000 10.06402 ? 183 TYR   B CB  1 
ATOM   3472 C  CG  . TYR   B 1 187 ? 26.44448 -18.62127 25.04252  1.000 14.72887 ? 183 TYR   B CG  1 
ATOM   3473 C  CD1 . TYR   B 1 187 ? 26.85357 -17.44088 25.65559  1.000 13.87820 ? 183 TYR   B CD1 1 
ATOM   3474 C  CD2 . TYR   B 1 187 ? 27.32075 -19.23552 24.15732  1.000 14.42272 ? 183 TYR   B CD2 1 
ATOM   3475 C  CE1 . TYR   B 1 187 ? 28.10192 -16.89465 25.39860  1.000 14.33941 ? 183 TYR   B CE1 1 
ATOM   3476 C  CE2 . TYR   B 1 187 ? 28.57243 -18.69795 23.89475  1.000 16.15383 ? 183 TYR   B CE2 1 
ATOM   3477 C  CZ  . TYR   B 1 187 ? 28.95432 -17.52580 24.51314  1.000 21.38093 ? 183 TYR   B CZ  1 
ATOM   3478 O  OH  . TYR   B 1 187 ? 30.19765 -16.99254 24.25448  1.000 17.21948 ? 183 TYR   B OH  1 
ATOM   3479 N  N   . ILE   B 1 188 ? 23.93797 -19.92453 22.51888  1.000 13.72777 ? 184 ILE   B N   1 
ATOM   3480 C  CA  . ILE   B 1 188 ? 24.14518 -20.19716 21.09972  1.000 8.96437  ? 184 ILE   B CA  1 
ATOM   3481 C  C   . ILE   B 1 188 ? 23.07098 -19.51831 20.25296  1.000 14.15048 ? 184 ILE   B C   1 
ATOM   3482 O  O   . ILE   B 1 188 ? 23.34788 -19.07027 19.13067  1.000 13.01620 ? 184 ILE   B O   1 
ATOM   3483 C  CB  . ILE   B 1 188 ? 24.19929 -21.72091 20.87005  1.000 11.99193 ? 184 ILE   B CB  1 
ATOM   3484 C  CG1 . ILE   B 1 188 ? 25.37740 -22.32457 21.64369  1.000 14.91003 ? 184 ILE   B CG1 1 
ATOM   3485 C  CG2 . ILE   B 1 188 ? 24.28730 -22.06001 19.38027  1.000 10.64053 ? 184 ILE   B CG2 1 
ATOM   3486 C  CD1 . ILE   B 1 188 ? 25.44328 -23.84105 21.60388  1.000 11.27555 ? 184 ILE   B CD1 1 
ATOM   3487 N  N   . GLU   B 1 189 ? 21.83454 -19.43295 20.75948  1.000 9.04228  ? 185 GLU   B N   1 
ATOM   3488 C  CA  . GLU   B 1 189 ? 20.81327 -18.63658 20.08102  1.000 11.66691 ? 185 GLU   B CA  1 
ATOM   3489 C  C   . GLU   B 1 189 ? 21.28619 -17.20182 19.88344  1.000 18.87054 ? 185 GLU   B C   1 
ATOM   3490 O  O   . GLU   B 1 189 ? 21.11678 -16.62424 18.80150  1.000 10.76568 ? 185 GLU   B O   1 
ATOM   3491 C  CB  . GLU   B 1 189 ? 19.50450 -18.65418 20.87312  1.000 15.19530 ? 185 GLU   B CB  1 
ATOM   3492 C  CG  . GLU   B 1 189 ? 18.38638 -17.80570 20.24700  1.000 10.66732 ? 185 GLU   B CG  1 
ATOM   3493 C  CD  . GLU   B 1 189 ? 17.26364 -17.47051 21.22044  1.000 16.06250 ? 185 GLU   B CD  1 
ATOM   3494 O  OE1 . GLU   B 1 189 ? 17.35917 -17.84491 22.41200  1.000 21.96538 ? 185 GLU   B OE1 1 
ATOM   3495 O  OE2 . GLU   B 1 189 ? 16.28125 -16.82394 20.79135  1.000 21.64823 ? 185 GLU   B OE2 1 
ATOM   3496 N  N   . GLY   B 1 190 ? 21.89546 -16.61561 20.91839  1.000 14.71844 ? 186 GLY   B N   1 
ATOM   3497 C  CA  . GLY   B 1 190 ? 22.38688 -15.25166 20.81169  1.000 13.69739 ? 186 GLY   B CA  1 
ATOM   3498 C  C   . GLY   B 1 190 ? 23.55488 -15.10978 19.85861  1.000 10.94887 ? 186 GLY   B C   1 
ATOM   3499 O  O   . GLY   B 1 190 ? 23.68588 -14.08575 19.18372  1.000 12.57118 ? 186 GLY   B O   1 
ATOM   3500 N  N   . GLU   B 1 191 ? 24.41836 -16.12576 19.79144  1.000 10.98088 ? 187 GLU   B N   1 
ATOM   3501 C  CA  . GLU   B 1 191 ? 25.50882 -16.11302 18.81948  1.000 13.64280 ? 187 GLU   B CA  1 
ATOM   3502 C  C   . GLU   B 1 191 ? 24.98062 -16.13308 17.38956  1.000 15.02427 ? 187 GLU   B C   1 
ATOM   3503 O  O   . GLU   B 1 191 ? 25.56061 -15.50410 16.49491  1.000 12.38910 ? 187 GLU   B O   1 
ATOM   3504 C  CB  . GLU   B 1 191 ? 26.43893 -17.30398 19.05751  1.000 21.80198 ? 187 GLU   B CB  1 
ATOM   3505 C  CG  . GLU   B 1 191 ? 27.50495 -17.07990 20.12103  1.000 24.25135 ? 187 GLU   B CG  1 
ATOM   3506 C  CD  . GLU   B 1 191 ? 28.81885 -16.60407 19.53104  1.000 34.88486 ? 187 GLU   B CD  1 
ATOM   3507 O  OE1 . GLU   B 1 191 ? 28.79143 -15.76937 18.60277  1.000 50.29975 ? 187 GLU   B OE1 1 
ATOM   3508 O  OE2 . GLU   B 1 191 ? 29.88069 -17.07729 19.98652  1.000 48.16025 ? 187 GLU   B OE2 1 
ATOM   3509 N  N   . MET   B 1 192 ? 23.89527 -16.86789 17.14338  1.000 11.58894 ? 188 MET   B N   1 
ATOM   3510 C  CA  . MET   B 1 192 ? 23.31310 -16.84999 15.80523  1.000 10.97501 ? 188 MET   B CA  1 
ATOM   3511 C  C   . MET   B 1 192 ? 22.54254 -15.55899 15.56283  1.000 13.67404 ? 188 MET   B C   1 
ATOM   3512 O  O   . MET   B 1 192 ? 22.58175 -15.00553 14.45736  1.000 9.79992  ? 188 MET   B O   1 
ATOM   3513 C  CB  . MET   B 1 192 ? 22.40218 -18.06065 15.60329  1.000 12.18492 ? 188 MET   B CB  1 
ATOM   3514 C  CG  . MET   B 1 192 ? 23.08899 -19.41241 15.82488  1.000 12.98948 ? 188 MET   B CG  1 
ATOM   3515 S  SD  . MET   B 1 192 ? 24.53844 -19.66961 14.77363  1.000 16.47226 ? 188 MET   B SD  1 
ATOM   3516 C  CE  . MET   B 1 192 ? 25.87656 -19.43986 15.94397  1.000 20.60537 ? 188 MET   B CE  1 
ATOM   3517 N  N   . ARG   B 1 193 ? 21.83009 -15.07866 16.58523  1.000 13.88185 ? 189 ARG   B N   1 
ATOM   3518 C  CA  . ARG   B 1 193 ? 21.14696 -13.79194 16.49439  1.000 14.45371 ? 189 ARG   B CA  1 
ATOM   3519 C  C   . ARG   B 1 193 ? 22.10218 -12.68132 16.08764  1.000 16.42536 ? 189 ARG   B C   1 
ATOM   3520 O  O   . ARG   B 1 193 ? 21.76763 -11.83599 15.25053  1.000 15.91710 ? 189 ARG   B O   1 
ATOM   3521 C  CB  . ARG   B 1 193 ? 20.50492 -13.44067 17.83650  1.000 13.48412 ? 189 ARG   B CB  1 
ATOM   3522 C  CG  . ARG   B 1 193 ? 19.00998 -13.61460 17.91393  1.000 27.00120 ? 189 ARG   B CG  1 
ATOM   3523 C  CD  . ARG   B 1 193 ? 18.45804 -12.76033 19.04836  1.000 26.33896 ? 189 ARG   B CD  1 
ATOM   3524 N  NE  . ARG   B 1 193 ? 19.42598 -12.60446 20.13174  1.000 25.41381 ? 189 ARG   B NE  1 
ATOM   3525 C  CZ  . ARG   B 1 193 ? 19.38804 -13.27432 21.27606  1.000 22.03046 ? 189 ARG   B CZ  1 
ATOM   3526 N  NH1 . ARG   B 1 193 ? 18.42486 -14.14189 21.53557  1.000 19.64101 ? 189 ARG   B NH1 1 
ATOM   3527 N  NH2 . ARG   B 1 193 ? 20.33677 -13.06142 22.18654  1.000 23.36315 ? 189 ARG   B NH2 1 
ATOM   3528 N  N   . THR   B 1 194 ? 23.29442 -12.65919 16.68396  1.000 13.20886 ? 190 THR   B N   1 
ATOM   3529 C  CA  . THR   B 1 194 ? 24.22730 -11.56611 16.43126  1.000 17.32178 ? 190 THR   B CA  1 
ATOM   3530 C  C   . THR   B 1 194 ? 24.78137 -11.62180 15.01167  1.000 11.28360 ? 190 THR   B C   1 
ATOM   3531 O  O   . THR   B 1 194 ? 24.92440 -10.58336 14.35471  1.000 15.20355 ? 190 THR   B O   1 
ATOM   3532 C  CB  . THR   B 1 194 ? 25.35353 -11.60236 17.46335  1.000 15.82009 ? 190 THR   B CB  1 
ATOM   3533 O  OG1 . THR   B 1 194 ? 24.79974 -11.37161 18.76511  1.000 24.30622 ? 190 THR   B OG1 1 
ATOM   3534 C  CG2 . THR   B 1 194 ? 26.38156 -10.52761 17.17039  1.000 28.43862 ? 190 THR   B CG2 1 
ATOM   3535 N  N   . ARG   B 1 195 ? 25.09982 -12.82228 14.52445  1.000 14.69932 ? 191 ARG   B N   1 
ATOM   3536 C  CA  . ARG   B 1 195 ? 25.49048 -12.97619 13.12521  1.000 11.98862 ? 191 ARG   B CA  1 
ATOM   3537 C  C   . ARG   B 1 195 ? 24.41081 -12.44577 12.18794  1.000 10.42433 ? 191 ARG   B C   1 
ATOM   3538 O  O   . ARG   B 1 195 ? 24.71384 -11.80734 11.17047  1.000 15.05356 ? 191 ARG   B O   1 
ATOM   3539 C  CB  . ARG   B 1 195 ? 25.78400 -14.44786 12.82741  1.000 14.03796 ? 191 ARG   B CB  1 
ATOM   3540 C  CG  . ARG   B 1 195 ? 27.15240 -14.92207 13.29811  1.000 14.69118 ? 191 ARG   B CG  1 
ATOM   3541 C  CD  . ARG   B 1 195 ? 27.21403 -16.43910 13.37795  1.000 24.97828 ? 191 ARG   B CD  1 
ATOM   3542 N  NE  . ARG   B 1 195 ? 28.54272 -16.91273 13.74563  1.000 19.41270 ? 191 ARG   B NE  1 
ATOM   3543 C  CZ  . ARG   B 1 195 ? 28.99782 -16.98329 14.98964  1.000 26.72614 ? 191 ARG   B CZ  1 
ATOM   3544 N  NH1 . ARG   B 1 195 ? 28.25529 -16.61146 16.02069  1.000 22.96544 ? 191 ARG   B NH1 1 
ATOM   3545 N  NH2 . ARG   B 1 195 ? 30.23001 -17.43707 15.20469  1.000 26.36189 ? 191 ARG   B NH2 1 
ATOM   3546 N  N   . ILE   B 1 196 ? 23.14318 -12.70448 12.51433  1.000 14.16818 ? 192 ILE   B N   1 
ATOM   3547 C  CA  . ILE   B 1 196 ? 22.04376 -12.24103 11.67611  1.000 17.87084 ? 192 ILE   B CA  1 
ATOM   3548 C  C   . ILE   B 1 196 ? 21.88920 -10.72961 11.78190  1.000 14.13053 ? 192 ILE   B C   1 
ATOM   3549 O  O   . ILE   B 1 196 ? 21.66546 -10.04417 10.77619  1.000 13.96137 ? 192 ILE   B O   1 
ATOM   3550 C  CB  . ILE   B 1 196 ? 20.74709 -12.97991 12.05831  1.000 14.44615 ? 192 ILE   B CB  1 
ATOM   3551 C  CG1 . ILE   B 1 196 ? 20.85517 -14.46424 11.68887  1.000 26.72889 ? 192 ILE   B CG1 1 
ATOM   3552 C  CG2 . ILE   B 1 196 ? 19.53996 -12.34109 11.39091  1.000 13.63713 ? 192 ILE   B CG2 1 
ATOM   3553 C  CD1 . ILE   B 1 196 ? 19.74995 -15.33043 12.27096  1.000 18.35300 ? 192 ILE   B CD1 1 
ATOM   3554 N  N   . ARG   B 1 197 ? 22.01644 -10.18179 12.99569  1.000 15.17604 ? 193 ARG   B N   1 
ATOM   3555 C  CA  . ARG   B 1 197 ? 21.79906 -8.74950  13.18543  1.000 16.09908 ? 193 ARG   B CA  1 
ATOM   3556 C  C   . ARG   B 1 197 ? 22.79596 -7.91586  12.38995  1.000 13.42027 ? 193 ARG   B C   1 
ATOM   3557 O  O   . ARG   B 1 197 ? 22.43447 -6.87611  11.82787  1.000 18.00703 ? 193 ARG   B O   1 
ATOM   3558 C  CB  . ARG   B 1 197 ? 21.88478 -8.38579  14.66855  1.000 13.87486 ? 193 ARG   B CB  1 
ATOM   3559 C  CG  . ARG   B 1 197 ? 21.53658 -6.92961  14.94566  1.000 15.64030 ? 193 ARG   B CG  1 
ATOM   3560 C  CD  . ARG   B 1 197 ? 21.75498 -6.55085  16.40743  1.000 14.06402 ? 193 ARG   B CD  1 
ATOM   3561 N  NE  . ARG   B 1 197 ? 20.71583 -7.06293  17.29517  1.000 17.13913 ? 193 ARG   B NE  1 
ATOM   3562 C  CZ  . ARG   B 1 197 ? 19.54352 -6.47492  17.50336  1.000 20.21238 ? 193 ARG   B CZ  1 
ATOM   3563 N  NH1 . ARG   B 1 197 ? 19.19254 -5.37728  16.85320  1.000 20.29035 ? 193 ARG   B NH1 1 
ATOM   3564 N  NH2 . ARG   B 1 197 ? 18.70168 -7.00110  18.38890  1.000 24.25359 ? 193 ARG   B NH2 1 
ATOM   3565 N  N   . TYR   B 1 198 ? 24.05723 -8.34359  12.34347  1.000 13.04788 ? 194 TYR   B N   1 
ATOM   3566 C  CA  . TYR   B 1 198 ? 25.12176 -7.55805  11.73120  1.000 19.58046 ? 194 TYR   B CA  1 
ATOM   3567 C  C   . TYR   B 1 198 ? 25.60450 -8.14643  10.41121  1.000 14.31745 ? 194 TYR   B C   1 
ATOM   3568 O  O   . TYR   B 1 198 ? 26.64438 -7.71659  9.89768   1.000 13.56646 ? 194 TYR   B O   1 
ATOM   3569 C  CB  . TYR   B 1 198 ? 26.29090 -7.40972  12.70849  1.000 15.46873 ? 194 TYR   B CB  1 
ATOM   3570 C  CG  . TYR   B 1 198 ? 25.90118 -6.70914  13.99196  1.000 14.04513 ? 194 TYR   B CG  1 
ATOM   3571 C  CD1 . TYR   B 1 198 ? 25.63266 -5.34486  14.00502  1.000 20.70546 ? 194 TYR   B CD1 1 
ATOM   3572 C  CD2 . TYR   B 1 198 ? 25.78848 -7.40955  15.18620  1.000 17.01299 ? 194 TYR   B CD2 1 
ATOM   3573 C  CE1 . TYR   B 1 198 ? 25.26828 -4.69770  15.17334  1.000 18.70607 ? 194 TYR   B CE1 1 
ATOM   3574 C  CE2 . TYR   B 1 198 ? 25.42268 -6.76994  16.35911  1.000 17.40247 ? 194 TYR   B CE2 1 
ATOM   3575 C  CZ  . TYR   B 1 198 ? 25.16407 -5.41322  16.34604  1.000 19.23508 ? 194 TYR   B CZ  1 
ATOM   3576 O  OH  . TYR   B 1 198 ? 24.80263 -4.76251  17.50758  1.000 17.86666 ? 194 TYR   B OH  1 
ATOM   3577 N  N   . ASN   B 1 199 ? 24.87896 -9.11719  9.85918   1.000 12.31903 ? 195 ASN   B N   1 
ATOM   3578 C  CA  . ASN   B 1 199 ? 25.20458 -9.74096  8.57689   1.000 13.01931 ? 195 ASN   B CA  1 
ATOM   3579 C  C   . ASN   B 1 199 ? 26.62891 -10.29915 8.58038   1.000 17.96829 ? 195 ASN   B C   1 
ATOM   3580 O  O   . ASN   B 1 199 ? 27.47366 -9.95468  7.74808   1.000 17.04177 ? 195 ASN   B O   1 
ATOM   3581 C  CB  . ASN   B 1 199 ? 25.00430 -8.75728  7.41884   1.000 15.89885 ? 195 ASN   B CB  1 
ATOM   3582 C  CG  . ASN   B 1 199 ? 25.09091 -9.43969  6.06790   1.000 15.01026 ? 195 ASN   B CG  1 
ATOM   3583 O  OD1 . ASN   B 1 199 ? 24.93134 -10.65976 5.97172   1.000 17.11188 ? 195 ASN   B OD1 1 
ATOM   3584 N  ND2 . ASN   B 1 199 ? 25.35422 -8.66489  5.02188   1.000 15.32559 ? 195 ASN   B ND2 1 
ATOM   3585 N  N   . ARG   B 1 200 ? 26.88631 -11.17442 9.54398   1.000 11.38290 ? 196 ARG   B N   1 
ATOM   3586 C  CA  . ARG   B 1 200 ? 28.19396 -11.79085 9.69034   1.000 11.18205 ? 196 ARG   B CA  1 
ATOM   3587 C  C   . ARG   B 1 200 ? 28.15100 -13.24551 9.24656   1.000 17.38475 ? 196 ARG   B C   1 
ATOM   3588 O  O   . ARG   B 1 200 ? 27.08738 -13.84027 9.04318   1.000 22.42279 ? 196 ARG   B O   1 
ATOM   3589 C  CB  . ARG   B 1 200 ? 28.68467 -11.68879 11.13723  1.000 13.83183 ? 196 ARG   B CB  1 
ATOM   3590 C  CG  . ARG   B 1 200 ? 28.95794 -10.26335 11.57067  1.000 16.95716 ? 196 ARG   B CG  1 
ATOM   3591 C  CD  . ARG   B 1 200 ? 29.22398 -10.16937 13.06126  1.000 18.82071 ? 196 ARG   B CD  1 
ATOM   3592 N  NE  . ARG   B 1 200 ? 29.44114 -8.78881  13.47456  1.000 19.57922 ? 196 ARG   B NE  1 
ATOM   3593 C  CZ  . ARG   B 1 200 ? 29.43390 -8.37683  14.73543  1.000 25.87284 ? 196 ARG   B CZ  1 
ATOM   3594 N  NH1 . ARG   B 1 200 ? 29.22814 -9.21811  15.73591  1.000 27.28124 ? 196 ARG   B NH1 1 
ATOM   3595 N  NH2 . ARG   B 1 200 ? 29.63474 -7.08808  14.99836  1.000 31.07578 ? 196 ARG   B NH2 1 
ATOM   3596 N  N   . ARG   B 1 201 ? 29.34569 -13.80420 9.09627   1.000 15.14675 ? 197 ARG   B N   1 
ATOM   3597 C  CA  . ARG   B 1 201 ? 29.53023 -15.18890 8.68210   1.000 13.60562 ? 197 ARG   B CA  1 
ATOM   3598 C  C   . ARG   B 1 201 ? 30.82565 -15.63994 9.33842   1.000 20.39808 ? 197 ARG   B C   1 
ATOM   3599 O  O   . ARG   B 1 201 ? 31.89045 -15.09420 9.03031   1.000 17.12114 ? 197 ARG   B O   1 
ATOM   3600 C  CB  . ARG   B 1 201 ? 29.59812 -15.29845 7.15926   1.000 18.38194 ? 197 ARG   B CB  1 
ATOM   3601 C  CG  . ARG   B 1 201 ? 29.88078 -16.68322 6.60979   1.000 19.71436 ? 197 ARG   B CG  1 
ATOM   3602 C  CD  . ARG   B 1 201 ? 30.09111 -16.63791 5.09471   1.000 14.02840 ? 197 ARG   B CD  1 
ATOM   3603 N  NE  . ARG   B 1 201 ? 30.17913 -17.97751 4.52184   1.000 14.87487 ? 197 ARG   B NE  1 
ATOM   3604 C  CZ  . ARG   B 1 201 ? 29.29376 -18.50168 3.68526   1.000 18.95951 ? 197 ARG   B CZ  1 
ATOM   3605 N  NH1 . ARG   B 1 201 ? 28.26255 -17.80118 3.23848   1.000 15.28065 ? 197 ARG   B NH1 1 
ATOM   3606 N  NH2 . ARG   B 1 201 ? 29.45249 -19.75829 3.27701   1.000 17.15774 ? 197 ARG   B NH2 1 
ATOM   3607 N  N   . SER   B 1 202 ? 30.73635 -16.58908 10.26934  1.000 12.43017 ? 198 SER   B N   1 
ATOM   3608 C  CA  . SER   B 1 202 ? 31.91205 -16.96913 11.04399  1.000 14.76703 ? 198 SER   B CA  1 
ATOM   3609 C  C   . SER   B 1 202 ? 31.68181 -18.30965 11.72348  1.000 11.78516 ? 198 SER   B C   1 
ATOM   3610 O  O   . SER   B 1 202 ? 30.55151 -18.65917 12.07557  1.000 14.16492 ? 198 SER   B O   1 
ATOM   3611 C  CB  . SER   B 1 202 ? 32.25434 -15.90454 12.09369  1.000 18.63963 ? 198 SER   B CB  1 
ATOM   3612 O  OG  . SER   B 1 202 ? 31.20624 -15.76771 13.03993  1.000 20.29749 ? 198 SER   B OG  1 
ATOM   3613 N  N   . ALA   B 1 203 ? 32.77542 -19.04176 11.91907  1.000 10.29009 ? 199 ALA   B N   1 
ATOM   3614 C  CA  . ALA   B 1 203 ? 32.71446 -20.31911 12.60600  1.000 16.25351 ? 199 ALA   B CA  1 
ATOM   3615 C  C   . ALA   B 1 203 ? 32.53642 -20.10288 14.10926  1.000 17.22025 ? 199 ALA   B C   1 
ATOM   3616 O  O   . ALA   B 1 203 ? 32.93055 -19.06384 14.64492  1.000 13.78937 ? 199 ALA   B O   1 
ATOM   3617 C  CB  . ALA   B 1 203 ? 33.98428 -21.12418 12.33882  1.000 16.93368 ? 199 ALA   B CB  1 
ATOM   3618 N  N   . PRO   B 1 204 ? 31.93435 -21.06233 14.81196  1.000 10.92663 ? 200 PRO   B N   1 
ATOM   3619 C  CA  . PRO   B 1 204 ? 31.76052 -20.90525 16.26405  1.000 14.34366 ? 200 PRO   B CA  1 
ATOM   3620 C  C   . PRO   B 1 204 ? 33.09586 -20.93009 16.98970  1.000 16.80669 ? 200 PRO   B C   1 
ATOM   3621 O  O   . PRO   B 1 204 ? 34.01147 -21.66484 16.61507  1.000 13.07435 ? 200 PRO   B O   1 
ATOM   3622 C  CB  . PRO   B 1 204 ? 30.89606 -22.11105 16.64726  1.000 14.85125 ? 200 PRO   B CB  1 
ATOM   3623 C  CG  . PRO   B 1 204 ? 31.22682 -23.13726 15.59936  1.000 12.23686 ? 200 PRO   B CG  1 
ATOM   3624 C  CD  . PRO   B 1 204 ? 31.38029 -22.33906 14.33010  1.000 13.59159 ? 200 PRO   B CD  1 
ATOM   3625 N  N   . ASP   B 1 205 ? 33.19822 -20.12076 18.04003  1.000 16.49762 ? 201 ASP   B N   1 
ATOM   3626 C  CA  . ASP   B 1 205 ? 34.41704 -20.04596 18.83581  1.000 16.11071 ? 201 ASP   B CA  1 
ATOM   3627 C  C   . ASP   B 1 205 ? 34.43405 -21.17410 19.86456  1.000 15.05341 ? 201 ASP   B C   1 
ATOM   3628 O  O   . ASP   B 1 205 ? 33.46940 -21.93380 19.97825  1.000 15.06725 ? 201 ASP   B O   1 
ATOM   3629 C  CB  . ASP   B 1 205 ? 34.52804 -18.65899 19.47693  1.000 17.49904 ? 201 ASP   B CB  1 
ATOM   3630 C  CG  . ASP   B 1 205 ? 33.38210 -18.33581 20.41165  1.000 29.14962 ? 201 ASP   B CG  1 
ATOM   3631 O  OD1 . ASP   B 1 205 ? 33.13303 -19.10723 21.36026  1.000 33.87143 ? 201 ASP   B OD1 1 
ATOM   3632 O  OD2 . ASP   B 1 205 ? 32.74856 -17.27632 20.21616  1.000 44.11033 ? 201 ASP   B OD2 1 
ATOM   3633 N  N   . PRO   B 1 206 ? 35.53502 -21.33119 20.61608  1.000 16.85495 ? 202 PRO   B N   1 
ATOM   3634 C  CA  . PRO   B 1 206 ? 35.59439 -22.43719 21.58760  1.000 14.39562 ? 202 PRO   B CA  1 
ATOM   3635 C  C   . PRO   B 1 206 ? 34.51490 -22.39548 22.65650  1.000 18.93846 ? 202 PRO   B C   1 
ATOM   3636 O  O   . PRO   B 1 206 ? 34.17581 -23.45035 23.20660  1.000 15.14049 ? 202 PRO   B O   1 
ATOM   3637 C  CB  . PRO   B 1 206 ? 36.99067 -22.28385 22.20516  1.000 22.58490 ? 202 PRO   B CB  1 
ATOM   3638 C  CG  . PRO   B 1 206 ? 37.78474 -21.60533 21.16976  1.000 14.29379 ? 202 PRO   B CG  1 
ATOM   3639 C  CD  . PRO   B 1 206 ? 36.84929 -20.67079 20.47722  1.000 18.28923 ? 202 PRO   B CD  1 
ATOM   3640 N  N   . SER   B 1 207 ? 33.97320 -21.21969 22.98808  1.000 15.11949 ? 203 SER   B N   1 
ATOM   3641 C  CA  . SER   B 1 207 ? 32.92414 -21.17985 24.00396  1.000 16.29349 ? 203 SER   B CA  1 
ATOM   3642 C  C   . SER   B 1 207 ? 31.67422 -21.90112 23.52014  1.000 20.84582 ? 203 SER   B C   1 
ATOM   3643 O  O   . SER   B 1 207 ? 31.01899 -22.60842 24.29396  1.000 19.38646 ? 203 SER   B O   1 
ATOM   3644 C  CB  . SER   B 1 207 ? 32.59399 -19.73586 24.38235  1.000 15.93396 ? 203 SER   B CB  1 
ATOM   3645 O  OG  . SER   B 1 207 ? 31.98864 -19.05689 23.29642  1.000 16.81471 ? 203 SER   B OG  1 
ATOM   3646 N  N   . VAL   B 1 208 ? 31.34079 -21.74680 22.23739  1.000 14.63649 ? 204 VAL   B N   1 
ATOM   3647 C  CA  . VAL   B 1 208 ? 30.16131 -22.40637 21.68614  1.000 9.79711  ? 204 VAL   B CA  1 
ATOM   3648 C  C   . VAL   B 1 208 ? 30.39558 -23.90408 21.55088  1.000 11.27556 ? 204 VAL   B C   1 
ATOM   3649 O  O   . VAL   B 1 208 ? 29.53132 -24.71411 21.90546  1.000 11.68473 ? 204 VAL   B O   1 
ATOM   3650 C  CB  . VAL   B 1 208 ? 29.78089 -21.77397 20.33585  1.000 12.48562 ? 204 VAL   B CB  1 
ATOM   3651 C  CG1 . VAL   B 1 208 ? 28.74703 -22.64018 19.61272  1.000 9.83154  ? 204 VAL   B CG1 1 
ATOM   3652 C  CG2 . VAL   B 1 208 ? 29.25385 -20.36269 20.54659  1.000 14.85326 ? 204 VAL   B CG2 1 
ATOM   3653 N  N   . ILE   B 1 209 ? 31.56446 -24.29734 21.03825  1.000 10.12259 ? 205 ILE   B N   1 
ATOM   3654 C  CA  . ILE   B 1 209 ? 31.81507 -25.70800 20.76038  1.000 11.31320 ? 205 ILE   B CA  1 
ATOM   3655 C  C   . ILE   B 1 209 ? 31.84729 -26.52073 22.05043  1.000 14.19032 ? 205 ILE   B C   1 
ATOM   3656 O  O   . ILE   B 1 209 ? 31.37974 -27.66684 22.08918  1.000 13.42612 ? 205 ILE   B O   1 
ATOM   3657 C  CB  . ILE   B 1 209 ? 33.11537 -25.85976 19.95143  1.000 17.51221 ? 205 ILE   B CB  1 
ATOM   3658 C  CG1 . ILE   B 1 209 ? 32.93618 -25.21715 18.57246  1.000 16.34562 ? 205 ILE   B CG1 1 
ATOM   3659 C  CG2 . ILE   B 1 209 ? 33.50492 -27.32591 19.81526  1.000 21.14245 ? 205 ILE   B CG2 1 
ATOM   3660 C  CD1 . ILE   B 1 209 ? 34.10030 -25.42202 17.66143  1.000 29.46642 ? 205 ILE   B CD1 1 
ATOM   3661 N  N   . THR   B 1 210 ? 32.38629 -25.94651 23.12763  1.000 12.44460 ? 206 THR   B N   1 
ATOM   3662 C  CA  . THR   B 1 210 ? 32.46937 -26.69859 24.37560  1.000 14.17097 ? 206 THR   B CA  1 
ATOM   3663 C  C   . THR   B 1 210 ? 31.10369 -26.80551 25.04413  1.000 15.00455 ? 206 THR   B C   1 
ATOM   3664 O  O   . THR   B 1 210 ? 30.77987 -27.84329 25.63148  1.000 14.99546 ? 206 THR   B O   1 
ATOM   3665 C  CB  . THR   B 1 210 ? 33.50772 -26.06845 25.30569  1.000 19.51391 ? 206 THR   B CB  1 
ATOM   3666 O  OG1 . THR   B 1 210 ? 34.81469 -26.29720 24.76342  1.000 19.86950 ? 206 THR   B OG1 1 
ATOM   3667 C  CG2 . THR   B 1 210 ? 33.44596 -26.67865 26.70858  1.000 12.71891 ? 206 THR   B CG2 1 
ATOM   3668 N  N   . LEU   B 1 211 ? 30.27332 -25.76251 24.94015  1.000 10.86319 ? 207 LEU   B N   1 
ATOM   3669 C  CA  . LEU   B 1 211 ? 28.89435 -25.88807 25.40394  1.000 10.85792 ? 207 LEU   B CA  1 
ATOM   3670 C  C   . LEU   B 1 211 ? 28.18087 -27.01068 24.66613  1.000 12.61914 ? 207 LEU   B C   1 
ATOM   3671 O  O   . LEU   B 1 211 ? 27.48879 -27.83223 25.27933  1.000 13.40661 ? 207 LEU   B O   1 
ATOM   3672 C  CB  . LEU   B 1 211 ? 28.13880 -24.57151 25.22039  1.000 13.30947 ? 207 LEU   B CB  1 
ATOM   3673 C  CG  . LEU   B 1 211 ? 28.24665 -23.47353 26.27935  1.000 13.70084 ? 207 LEU   B CG  1 
ATOM   3674 C  CD1 . LEU   B 1 211 ? 27.49212 -22.24337 25.80369  1.000 15.82692 ? 207 LEU   B CD1 1 
ATOM   3675 C  CD2 . LEU   B 1 211 ? 27.69446 -23.93856 27.62505  1.000 10.85606 ? 207 LEU   B CD2 1 
ATOM   3676 N  N   . GLU   B 1 212 ? 28.34126 -27.06109 23.34017  1.000 10.23526 ? 208 GLU   B N   1 
ATOM   3677 C  CA  . GLU   B 1 212 ? 27.74745 -28.14188 22.55994  1.000 15.47328 ? 208 GLU   B CA  1 
ATOM   3678 C  C   . GLU   B 1 212 ? 28.21486 -29.50137 23.06364  1.000 16.30906 ? 208 GLU   B C   1 
ATOM   3679 O  O   . GLU   B 1 212 ? 27.40963 -30.42287 23.24084  1.000 14.20527 ? 208 GLU   B O   1 
ATOM   3680 C  CB  . GLU   B 1 212 ? 28.09255 -27.96757 21.07657  1.000 13.24065 ? 208 GLU   B CB  1 
ATOM   3681 C  CG  . GLU   B 1 212 ? 27.40404 -26.78642 20.40978  1.000 9.05180  ? 208 GLU   B CG  1 
ATOM   3682 C  CD  . GLU   B 1 212 ? 27.89009 -26.54811 18.98811  1.000 17.40877 ? 208 GLU   B CD  1 
ATOM   3683 O  OE1 . GLU   B 1 212 ? 28.75617 -27.31321 18.50960  1.000 17.11277 ? 208 GLU   B OE1 1 
ATOM   3684 O  OE2 . GLU   B 1 212 ? 27.40929 -25.59248 18.34780  1.000 14.65111 ? 208 GLU   B OE2 1 
ATOM   3685 N  N   . ASN   B 1 213 ? 29.51725 -29.63813 23.32126  1.000 11.32187 ? 209 ASN   B N   1 
ATOM   3686 C  CA  . ASN   B 1 213 ? 30.06293 -30.91695 23.75526  1.000 11.44527 ? 209 ASN   B CA  1 
ATOM   3687 C  C   . ASN   B 1 213 ? 29.59629 -31.31477 25.14842  1.000 11.86584 ? 209 ASN   B C   1 
ATOM   3688 O  O   . ASN   B 1 213 ? 29.60076 -32.50717 25.46721  1.000 15.98948 ? 209 ASN   B O   1 
ATOM   3689 C  CB  . ASN   B 1 213 ? 31.59241 -30.88079 23.72876  1.000 13.38905 ? 209 ASN   B CB  1 
ATOM   3690 C  CG  . ASN   B 1 213 ? 32.15264 -30.76059 22.32569  1.000 17.06544 ? 209 ASN   B CG  1 
ATOM   3691 O  OD1 . ASN   B 1 213 ? 31.45686 -31.00988 21.34089  1.000 14.62400 ? 209 ASN   B OD1 1 
ATOM   3692 N  ND2 . ASN   B 1 213 ? 33.42498 -30.39163 22.22876  1.000 18.94289 ? 209 ASN   B ND2 1 
ATOM   3693 N  N   . SER   B 1 214 ? 29.19241 -30.35534 25.97963  1.000 14.07179 ? 210 SER   B N   1 
ATOM   3694 C  CA  . SER   B 1 214 ? 28.89789 -30.61710 27.38380  1.000 12.22620 ? 210 SER   B CA  1 
ATOM   3695 C  C   . SER   B 1 214 ? 27.40650 -30.67904 27.69661  1.000 16.65766 ? 210 SER   B C   1 
ATOM   3696 O  O   . SER   B 1 214 ? 27.04747 -30.81131 28.87171  1.000 14.89111 ? 210 SER   B O   1 
ATOM   3697 C  CB  . SER   B 1 214 ? 29.55536 -29.54635 28.26136  1.000 16.19139 ? 210 SER   B CB  1 
ATOM   3698 O  OG  . SER   B 1 214 ? 30.92755 -29.38739 27.93557  1.000 18.28081 ? 210 SER   B OG  1 
ATOM   3699 N  N   . TRP   B 1 215 ? 26.53365 -30.59116 26.68359  1.000 11.77007 ? 211 TRP   B N   1 
ATOM   3700 C  CA  . TRP   B 1 215 ? 25.09633 -30.50419 26.94237  1.000 16.37726 ? 211 TRP   B CA  1 
ATOM   3701 C  C   . TRP   B 1 215 ? 24.59378 -31.70507 27.73744  1.000 14.04122 ? 211 TRP   B C   1 
ATOM   3702 O  O   . TRP   B 1 215 ? 23.81727 -31.54877 28.68961  1.000 14.22167 ? 211 TRP   B O   1 
ATOM   3703 C  CB  . TRP   B 1 215 ? 24.32872 -30.37740 25.62489  1.000 12.86993 ? 211 TRP   B CB  1 
ATOM   3704 C  CG  . TRP   B 1 215 ? 22.84747 -30.19725 25.81730  1.000 13.70893 ? 211 TRP   B CG  1 
ATOM   3705 C  CD1 . TRP   B 1 215 ? 22.22147 -29.11559 26.35937  1.000 12.20089 ? 211 TRP   B CD1 1 
ATOM   3706 C  CD2 . TRP   B 1 215 ? 21.81300 -31.12930 25.47688  1.000 11.48335 ? 211 TRP   B CD2 1 
ATOM   3707 N  NE1 . TRP   B 1 215 ? 20.86351 -29.31099 26.37388  1.000 12.53251 ? 211 TRP   B NE1 1 
ATOM   3708 C  CE2 . TRP   B 1 215 ? 20.58532 -30.53842 25.83649  1.000 11.08944 ? 211 TRP   B CE2 1 
ATOM   3709 C  CE3 . TRP   B 1 215 ? 21.80588 -32.40353 24.89990  1.000 16.81429 ? 211 TRP   B CE3 1 
ATOM   3710 C  CZ2 . TRP   B 1 215 ? 19.36228 -31.17310 25.63679  1.000 11.39221 ? 211 TRP   B CZ2 1 
ATOM   3711 C  CZ3 . TRP   B 1 215 ? 20.58739 -33.03755 24.70340  1.000 16.93206 ? 211 TRP   B CZ3 1 
ATOM   3712 C  CH2 . TRP   B 1 215 ? 19.38181 -32.41801 25.06935  1.000 14.00408 ? 211 TRP   B CH2 1 
ATOM   3713 N  N   . GLY   B 1 216 ? 25.02314 -32.91107 27.36320  1.000 12.75301 ? 212 GLY   B N   1 
ATOM   3714 C  CA  . GLY   B 1 216 ? 24.63425 -34.08504 28.12410  1.000 20.40706 ? 212 GLY   B CA  1 
ATOM   3715 C  C   . GLY   B 1 216 ? 25.17107 -34.06506 29.54350  1.000 17.53981 ? 212 GLY   B C   1 
ATOM   3716 O  O   . GLY   B 1 216 ? 24.45057 -34.38179 30.49274  1.000 16.11087 ? 212 GLY   B O   1 
ATOM   3717 N  N   . ARG   B 1 217 ? 26.44533 -33.69224 29.70560  1.000 18.99261 ? 213 ARG   B N   1 
ATOM   3718 C  CA  . ARG   B 1 217 ? 27.05433 -33.65722 31.03364  1.000 16.28781 ? 213 ARG   B CA  1 
ATOM   3719 C  C   . ARG   B 1 217 ? 26.44164 -32.56601 31.90019  1.000 21.68295 ? 213 ARG   B C   1 
ATOM   3720 O  O   . ARG   B 1 217 ? 26.28909 -32.74534 33.11407  1.000 15.69943 ? 213 ARG   B O   1 
ATOM   3721 C  CB  . ARG   B 1 217 ? 28.56458 -33.45228 30.91669  1.000 22.14956 ? 213 ARG   B CB  1 
ATOM   3722 C  CG  . ARG   B 1 217 ? 29.35014 -34.72252 30.65604  1.000 34.98928 ? 213 ARG   B CG  1 
ATOM   3723 C  CD  . ARG   B 1 217 ? 30.83652 -34.43577 30.49172  1.000 41.12121 ? 213 ARG   B CD  1 
ATOM   3724 N  NE  . ARG   B 1 217 ? 31.13463 -33.80042 29.21280  1.000 45.01767 ? 213 ARG   B NE  1 
ATOM   3725 C  CZ  . ARG   B 1 217 ? 32.35273 -33.68681 28.70039  1.000 48.69955 ? 213 ARG   B CZ  1 
ATOM   3726 N  NH1 . ARG   B 1 217 ? 33.41583 -34.15469 29.33479  1.000 61.04037 ? 213 ARG   B NH1 1 
ATOM   3727 N  NH2 . ARG   B 1 217 ? 32.50784 -33.09434 27.51976  1.000 29.52225 ? 213 ARG   B NH2 1 
ATOM   3728 N  N   . LEU   B 1 218 ? 26.10605 -31.41801 31.30186  1.000 14.00509 ? 214 LEU   B N   1 
ATOM   3729 C  CA  . LEU   B 1 218 ? 25.45795 -30.35826 32.06890  1.000 19.16815 ? 214 LEU   B CA  1 
ATOM   3730 C  C   . LEU   B 1 218 ? 24.06351 -30.77629 32.51231  1.000 15.10453 ? 214 LEU   B C   1 
ATOM   3731 O  O   . LEU   B 1 218 ? 23.64657 -30.47239 33.63567  1.000 16.54756 ? 214 LEU   B O   1 
ATOM   3732 C  CB  . LEU   B 1 218 ? 25.38573 -29.07216 31.24718  1.000 12.67886 ? 214 LEU   B CB  1 
ATOM   3733 C  CG  . LEU   B 1 218 ? 26.69119 -28.31469 31.01916  1.000 15.63553 ? 214 LEU   B CG  1 
ATOM   3734 C  CD1 . LEU   B 1 218 ? 26.48330 -27.25136 29.94626  1.000 18.63256 ? 214 LEU   B CD1 1 
ATOM   3735 C  CD2 . LEU   B 1 218 ? 27.18469 -27.69641 32.32335  1.000 18.16428 ? 214 LEU   B CD2 1 
ATOM   3736 N  N   . SER   B 1 219 ? 23.31909 -31.45277 31.63529  1.000 13.45276 ? 215 SER   B N   1 
ATOM   3737 C  CA  . SER   B 1 219 ? 21.99517 -31.93541 32.01260  1.000 13.81794 ? 215 SER   B CA  1 
ATOM   3738 C  C   . SER   B 1 219 ? 22.08841 -32.87748 33.20410  1.000 17.49436 ? 215 SER   B C   1 
ATOM   3739 O  O   . SER   B 1 219 ? 21.31750 -32.76490 34.16480  1.000 15.19354 ? 215 SER   B O   1 
ATOM   3740 C  CB  . SER   B 1 219 ? 21.33182 -32.63057 30.82148  1.000 15.29996 ? 215 SER   B CB  1 
ATOM   3741 O  OG  . SER   B 1 219 ? 21.21411 -31.74757 29.71162  1.000 14.31417 ? 215 SER   B OG  1 
ATOM   3742 N  N   . THR   B 1 220 ? 23.04928 -33.80303 33.16388  1.000 15.08719 ? 216 THR   B N   1 
ATOM   3743 C  CA  . THR   B 1 220 ? 23.22222 -34.75565 34.25688  1.000 16.07158 ? 216 THR   B CA  1 
ATOM   3744 C  C   . THR   B 1 220 ? 23.63957 -34.05239 35.54552  1.000 21.30201 ? 216 THR   B C   1 
ATOM   3745 O  O   . THR   B 1 220 ? 23.09836 -34.33279 36.62225  1.000 21.40003 ? 216 THR   B O   1 
ATOM   3746 C  CB  . THR   B 1 220 ? 24.25261 -35.81606 33.86294  1.000 16.90723 ? 216 THR   B CB  1 
ATOM   3747 O  OG1 . THR   B 1 220 ? 23.75675 -36.58230 32.75703  1.000 17.37408 ? 216 THR   B OG1 1 
ATOM   3748 C  CG2 . THR   B 1 220 ? 24.54327 -36.75444 35.03624  1.000 25.95935 ? 216 THR   B CG2 1 
ATOM   3749 N  N   . ALA   B 1 221 ? 24.60689 -33.13426 35.45455  1.000 16.00355 ? 217 ALA   B N   1 
ATOM   3750 C  CA  . ALA   B 1 221 ? 25.11050 -32.46735 36.65134  1.000 18.37754 ? 217 ALA   B CA  1 
ATOM   3751 C  C   . ALA   B 1 221 ? 24.02292 -31.64738 37.33274  1.000 17.19958 ? 217 ALA   B C   1 
ATOM   3752 O  O   . ALA   B 1 221 ? 23.90776 -31.65823 38.56321  1.000 18.08437 ? 217 ALA   B O   1 
ATOM   3753 C  CB  . ALA   B 1 221 ? 26.30626 -31.58152 36.30016  1.000 16.77719 ? 217 ALA   B CB  1 
ATOM   3754 N  N   . ILE   B 1 222 ? 23.20950 -30.93597 36.55141  1.000 15.65681 ? 218 ILE   B N   1 
ATOM   3755 C  CA  . ILE   B 1 222 ? 22.16155 -30.10470 37.13841  1.000 18.03664 ? 218 ILE   B CA  1 
ATOM   3756 C  C   . ILE   B 1 222 ? 21.07814 -30.96896 37.77606  1.000 20.61153 ? 218 ILE   B C   1 
ATOM   3757 O  O   . ILE   B 1 222 ? 20.59306 -30.67175 38.87531  1.000 19.83101 ? 218 ILE   B O   1 
ATOM   3758 C  CB  . ILE   B 1 222 ? 21.58244 -29.15313 36.07485  1.000 19.36741 ? 218 ILE   B CB  1 
ATOM   3759 C  CG1 . ILE   B 1 222 ? 22.63380 -28.13008 35.65277  1.000 14.37195 ? 218 ILE   B CG1 1 
ATOM   3760 C  CG2 . ILE   B 1 222 ? 20.33828 -28.44676 36.59960  1.000 15.45484 ? 218 ILE   B CG2 1 
ATOM   3761 C  CD1 . ILE   B 1 222 ? 22.27059 -27.37325 34.38705  1.000 13.60278 ? 218 ILE   B CD1 1 
ATOM   3762 N  N   . GLN   B 1 223 ? 20.69260 -32.06153 37.11538  1.000 16.49467 ? 219 GLN   B N   1 
ATOM   3763 C  CA  . GLN   B 1 223 ? 19.56746 -32.84455 37.61370  1.000 17.23117 ? 219 GLN   B CA  1 
ATOM   3764 C  C   . GLN   B 1 223 ? 19.94235 -33.70487 38.81388  1.000 18.23986 ? 219 GLN   B C   1 
ATOM   3765 O  O   . GLN   B 1 223 ? 19.07827 -33.99153 39.64855  1.000 21.50644 ? 219 GLN   B O   1 
ATOM   3766 C  CB  . GLN   B 1 223 ? 18.98436 -33.70005 36.48799  1.000 17.08699 ? 219 GLN   B CB  1 
ATOM   3767 C  CG  . GLN   B 1 223 ? 18.26407 -32.86073 35.43054  1.000 16.31257 ? 219 GLN   B CG  1 
ATOM   3768 C  CD  . GLN   B 1 223 ? 17.81409 -33.67494 34.23278  1.000 23.68442 ? 219 GLN   B CD  1 
ATOM   3769 O  OE1 . GLN   B 1 223 ? 17.24509 -34.75592 34.37804  1.000 20.76691 ? 219 GLN   B OE1 1 
ATOM   3770 N  NE2 . GLN   B 1 223 ? 18.07272 -33.15878 33.03919  1.000 15.30227 ? 219 GLN   B NE2 1 
ATOM   3771 N  N   . GLU   B 1 224 ? 21.20788 -34.10584 38.93103  1.000 18.36666 ? 220 GLU   B N   1 
ATOM   3772 C  CA  . GLU   B 1 224 ? 21.68240 -34.87884 40.07415  1.000 19.40755 ? 220 GLU   B CA  1 
ATOM   3773 C  C   . GLU   B 1 224 ? 22.25108 -34.00877 41.18773  1.000 21.92966 ? 220 GLU   B C   1 
ATOM   3774 O  O   . GLU   B 1 224 ? 22.71953 -34.54722 42.19814  1.000 21.75738 ? 220 GLU   B O   1 
ATOM   3775 C  CB  . GLU   B 1 224 ? 22.75418 -35.87791 39.63031  1.000 19.64621 ? 220 GLU   B CB  1 
ATOM   3776 C  CG  . GLU   B 1 224 ? 22.27683 -36.94020 38.65962  1.000 25.80427 ? 220 GLU   B CG  1 
ATOM   3777 C  CD  . GLU   B 1 224 ? 23.35876 -37.96021 38.35496  1.000 38.49324 ? 220 GLU   B CD  1 
ATOM   3778 O  OE1 . GLU   B 1 224 ? 24.50599 -37.75987 38.80688  1.000 40.74718 ? 220 GLU   B OE1 1 
ATOM   3779 O  OE2 . GLU   B 1 224 ? 23.06542 -38.96095 37.66723  1.000 32.09360 ? 220 GLU   B OE2 1 
ATOM   3780 N  N   . SER   B 1 225 ? 22.22145 -32.69027 41.02747  1.000 20.71553 ? 221 SER   B N   1 
ATOM   3781 C  CA  . SER   B 1 225 ? 22.90288 -31.79076 41.94439  1.000 21.11141 ? 221 SER   B CA  1 
ATOM   3782 C  C   . SER   B 1 225 ? 22.25653 -31.80873 43.32540  1.000 35.36522 ? 221 SER   B C   1 
ATOM   3783 O  O   . SER   B 1 225 ? 21.10465 -32.21213 43.50410  1.000 27.30914 ? 221 SER   B O   1 
ATOM   3784 C  CB  . SER   B 1 225 ? 22.89036 -30.36255 41.39891  1.000 28.10810 ? 221 SER   B CB  1 
ATOM   3785 O  OG  . SER   B 1 225 ? 21.56964 -29.84469 41.37098  1.000 25.16200 ? 221 SER   B OG  1 
ATOM   3786 N  N   . ASN   B 1 226 ? 23.02578 -31.34827 44.30954  1.000 25.71992 ? 222 ASN   B N   1 
ATOM   3787 C  CA  . ASN   B 1 226 ? 22.53914 -31.14954 45.67071  1.000 33.45512 ? 222 ASN   B CA  1 
ATOM   3788 C  C   . ASN   B 1 226 ? 21.97630 -29.73617 45.74862  1.000 32.67734 ? 222 ASN   B C   1 
ATOM   3789 O  O   . ASN   B 1 226 ? 22.67561 -28.78312 46.09597  1.000 31.08996 ? 222 ASN   B O   1 
ATOM   3790 C  CB  . ASN   B 1 226 ? 23.65630 -31.37563 46.68051  1.000 25.18510 ? 222 ASN   B CB  1 
ATOM   3791 C  CG  . ASN   B 1 226 ? 23.15114 -31.42712 48.10724  1.000 49.94668 ? 222 ASN   B CG  1 
ATOM   3792 O  OD1 . ASN   B 1 226 ? 22.04225 -30.98308 48.39814  1.000 44.33279 ? 222 ASN   B OD1 1 
ATOM   3793 N  ND2 . ASN   B 1 226 ? 23.97082 -31.95805 49.00895  1.000 58.40122 ? 222 ASN   B ND2 1 
ATOM   3794 N  N   . GLN   B 1 227 ? 20.69295 -29.60010 45.40560  1.000 26.87012 ? 223 GLN   B N   1 
ATOM   3795 C  CA  . GLN   B 1 227 ? 19.99782 -28.30588 45.40334  1.000 29.81645 ? 223 GLN   B CA  1 
ATOM   3796 C  C   . GLN   B 1 227 ? 20.75046 -27.27405 44.56291  1.000 28.26140 ? 223 GLN   B C   1 
ATOM   3797 O  O   . GLN   B 1 227 ? 20.91159 -26.11392 44.95229  1.000 27.48012 ? 223 GLN   B O   1 
ATOM   3798 C  CB  . GLN   B 1 227 ? 19.78088 -27.79912 46.83106  1.000 42.64259 ? 223 GLN   B CB  1 
ATOM   3799 C  CG  . GLN   B 1 227 ? 18.66696 -26.76543 46.96985  1.000 49.40541 ? 223 GLN   B CG  1 
ATOM   3800 C  CD  . GLN   B 1 227 ? 17.28282 -27.37051 46.83077  1.000 53.15289 ? 223 GLN   B CD  1 
ATOM   3801 O  OE1 . GLN   B 1 227 ? 16.70856 -27.39836 45.74092  1.000 49.94772 ? 223 GLN   B OE1 1 
ATOM   3802 N  NE2 . GLN   B 1 227 ? 16.73848 -27.85729 47.93945  1.000 39.18249 ? 223 GLN   B NE2 1 
ATOM   3803 N  N   . GLY   B 1 228 ? 21.21705 -27.70222 43.39207  1.000 27.18118 ? 224 GLY   B N   1 
ATOM   3804 C  CA  . GLY   B 1 228 ? 21.91561 -26.83888 42.47105  1.000 22.24063 ? 224 GLY   B CA  1 
ATOM   3805 C  C   . GLY   B 1 228 ? 23.42602 -26.93649 42.52755  1.000 19.75745 ? 224 GLY   B C   1 
ATOM   3806 O  O   . GLY   B 1 228 ? 24.08921 -26.58226 41.54857  1.000 20.68718 ? 224 GLY   B O   1 
ATOM   3807 N  N   . ALA   B 1 229 ? 23.98584 -27.39727 43.64296  1.000 20.90462 ? 225 ALA   B N   1 
ATOM   3808 C  CA  . ALA   B 1 229 ? 25.43012 -27.53308 43.76743  1.000 21.33784 ? 225 ALA   B CA  1 
ATOM   3809 C  C   . ALA   B 1 229 ? 25.89811 -28.80874 43.07657  1.000 24.21474 ? 225 ALA   B C   1 
ATOM   3810 O  O   . ALA   B 1 229 ? 25.40931 -29.90316 43.37691  1.000 28.06829 ? 225 ALA   B O   1 
ATOM   3811 C  CB  . ALA   B 1 229 ? 25.83852 -27.54488 45.24111  1.000 22.70063 ? 225 ALA   B CB  1 
ATOM   3812 N  N   . PHE   B 1 230 ? 26.84644 -28.66523 42.15363  1.000 20.81642 ? 226 PHE   B N   1 
ATOM   3813 C  CA  . PHE   B 1 230 ? 27.34995 -29.81122 41.40739  1.000 29.10734 ? 226 PHE   B CA  1 
ATOM   3814 C  C   . PHE   B 1 230 ? 28.14904 -30.73691 42.31375  1.000 26.33399 ? 226 PHE   B C   1 
ATOM   3815 O  O   . PHE   B 1 230 ? 28.89176 -30.28354 43.18754  1.000 26.12321 ? 226 PHE   B O   1 
ATOM   3816 C  CB  . PHE   B 1 230 ? 28.23865 -29.35502 40.25114  1.000 21.02049 ? 226 PHE   B CB  1 
ATOM   3817 C  CG  . PHE   B 1 230 ? 27.49485 -28.69795 39.12523  1.000 22.28484 ? 226 PHE   B CG  1 
ATOM   3818 C  CD1 . PHE   B 1 230 ? 26.11079 -28.63515 39.12248  1.000 22.27523 ? 226 PHE   B CD1 1 
ATOM   3819 C  CD2 . PHE   B 1 230 ? 28.18716 -28.15685 38.05633  1.000 21.29837 ? 226 PHE   B CD2 1 
ATOM   3820 C  CE1 . PHE   B 1 230 ? 25.43448 -28.03041 38.08133  1.000 19.30221 ? 226 PHE   B CE1 1 
ATOM   3821 C  CE2 . PHE   B 1 230 ? 27.51531 -27.55397 37.01443  1.000 18.54918 ? 226 PHE   B CE2 1 
ATOM   3822 C  CZ  . PHE   B 1 230 ? 26.13757 -27.49382 37.02676  1.000 20.10676 ? 226 PHE   B CZ  1 
ATOM   3823 N  N   . ALA   B 1 231 ? 28.00267 -32.04654 42.08992  1.000 30.48468 ? 227 ALA   B N   1 
ATOM   3824 C  CA  . ALA   B 1 231 ? 28.82481 -33.01306 42.81195  1.000 38.34895 ? 227 ALA   B CA  1 
ATOM   3825 C  C   . ALA   B 1 231 ? 30.26935 -32.97099 42.32841  1.000 45.53721 ? 227 ALA   B C   1 
ATOM   3826 O  O   . ALA   B 1 231 ? 31.20395 -33.11263 43.12611  1.000 41.02494 ? 227 ALA   B O   1 
ATOM   3827 C  CB  . ALA   B 1 231 ? 28.24449 -34.41787 42.65621  1.000 28.37429 ? 227 ALA   B CB  1 
ATOM   3828 N  N   . SER   B 1 232 ? 30.46762 -32.78099 41.02514  1.000 25.55575 ? 228 SER   B N   1 
ATOM   3829 C  CA  . SER   B 1 232 ? 31.77017 -32.58689 40.41221  1.000 39.36097 ? 228 SER   B CA  1 
ATOM   3830 C  C   . SER   B 1 232 ? 31.73297 -31.33748 39.54405  1.000 27.89131 ? 228 SER   B C   1 
ATOM   3831 O  O   . SER   B 1 232 ? 30.70653 -31.04792 38.91855  1.000 32.19737 ? 228 SER   B O   1 
ATOM   3832 C  CB  . SER   B 1 232 ? 32.17522 -33.79660 39.55550  1.000 43.19803 ? 228 SER   B CB  1 
ATOM   3833 O  OG  . SER   B 1 232 ? 32.58003 -34.88754 40.36336  1.000 52.22014 ? 228 SER   B OG  1 
ATOM   3834 N  N   . PRO   B 1 233 ? 32.82174 -30.57561 39.49237  1.000 28.47261 ? 229 PRO   B N   1 
ATOM   3835 C  CA  . PRO   B 1 233 ? 32.84538 -29.38326 38.63973  1.000 27.18188 ? 229 PRO   B CA  1 
ATOM   3836 C  C   . PRO   B 1 233 ? 32.91139 -29.75027 37.16478  1.000 32.51814 ? 229 PRO   B C   1 
ATOM   3837 O  O   . PRO   B 1 233 ? 33.36115 -30.83216 36.77915  1.000 31.63477 ? 229 PRO   B O   1 
ATOM   3838 C  CB  . PRO   B 1 233 ? 34.11326 -28.64933 39.08735  1.000 30.39214 ? 229 PRO   B CB  1 
ATOM   3839 C  CG  . PRO   B 1 233 ? 34.98051 -29.71239 39.67168  1.000 23.59218 ? 229 PRO   B CG  1 
ATOM   3840 C  CD  . PRO   B 1 233 ? 34.05010 -30.71475 40.29321  1.000 32.88801 ? 229 PRO   B CD  1 
ATOM   3841 N  N   . ILE   B 1 234 ? 32.44604 -28.81925 36.33402  1.000 27.77259 ? 230 ILE   B N   1 
ATOM   3842 C  CA  . ILE   B 1 234 ? 32.42504 -28.98302 34.88543  1.000 24.36944 ? 230 ILE   B CA  1 
ATOM   3843 C  C   . ILE   B 1 234 ? 33.30697 -27.90789 34.26817  1.000 29.21252 ? 230 ILE   B C   1 
ATOM   3844 O  O   . ILE   B 1 234 ? 33.15243 -26.72025 34.57485  1.000 29.20874 ? 230 ILE   B O   1 
ATOM   3845 C  CB  . ILE   B 1 234 ? 30.99432 -28.90451 34.32215  1.000 24.94267 ? 230 ILE   B CB  1 
ATOM   3846 C  CG1 . ILE   B 1 234 ? 30.11670 -30.00750 34.92275  1.000 32.54241 ? 230 ILE   B CG1 1 
ATOM   3847 C  CG2 . ILE   B 1 234 ? 31.01245 -29.00610 32.80154  1.000 33.16838 ? 230 ILE   B CG2 1 
ATOM   3848 C  CD1 . ILE   B 1 234 ? 30.54692 -31.41317 34.55200  1.000 35.15877 ? 230 ILE   B CD1 1 
ATOM   3849 N  N   . GLN   B 1 235 ? 34.22821 -28.32352 33.40401  1.000 18.57009 ? 231 GLN   B N   1 
ATOM   3850 C  CA  . GLN   B 1 235 ? 35.12027 -27.39862 32.71678  1.000 29.46937 ? 231 GLN   B CA  1 
ATOM   3851 C  C   . GLN   B 1 235 ? 34.44828 -26.85591 31.46199  1.000 23.55418 ? 231 GLN   B C   1 
ATOM   3852 O  O   . GLN   B 1 235 ? 34.00613 -27.62942 30.60823  1.000 25.28384 ? 231 GLN   B O   1 
ATOM   3853 C  CB  . GLN   B 1 235 ? 36.42949 -28.09785 32.34634  1.000 31.76424 ? 231 GLN   B CB  1 
ATOM   3854 C  CG  . GLN   B 1 235 ? 37.10006 -28.77565 33.51314  1.000 35.13072 ? 231 GLN   B CG  1 
ATOM   3855 C  CD  . GLN   B 1 235 ? 37.25511 -27.84376 34.68962  1.000 40.93689 ? 231 GLN   B CD  1 
ATOM   3856 O  OE1 . GLN   B 1 235 ? 37.77103 -26.73440 34.55090  1.000 47.60054 ? 231 GLN   B OE1 1 
ATOM   3857 N  NE2 . GLN   B 1 235 ? 36.79587 -28.28032 35.85603  1.000 48.75369 ? 231 GLN   B NE2 1 
ATOM   3858 N  N   . LEU   B 1 236 ? 34.37069 -25.53289 31.35530  1.000 19.96012 ? 232 LEU   B N   1 
ATOM   3859 C  CA  . LEU   B 1 236 ? 33.88115 -24.86129 30.15770  1.000 19.01823 ? 232 LEU   B CA  1 
ATOM   3860 C  C   . LEU   B 1 236 ? 34.95823 -23.91429 29.63521  1.000 18.42185 ? 232 LEU   B C   1 
ATOM   3861 O  O   . LEU   B 1 236 ? 35.95885 -23.65401 30.30611  1.000 23.22229 ? 232 LEU   B O   1 
ATOM   3862 C  CB  . LEU   B 1 236 ? 32.57291 -24.10868 30.43880  1.000 14.87832 ? 232 LEU   B CB  1 
ATOM   3863 C  CG  . LEU   B 1 236 ? 31.37777 -24.97469 30.84913  1.000 17.93599 ? 232 LEU   B CG  1 
ATOM   3864 C  CD1 . LEU   B 1 236 ? 30.14293 -24.11788 31.11299  1.000 16.71130 ? 232 LEU   B CD1 1 
ATOM   3865 C  CD2 . LEU   B 1 236 ? 31.08241 -26.03254 29.79456  1.000 19.87272 ? 232 LEU   B CD2 1 
ATOM   3866 N  N   . GLN   B 1 237 ? 34.75437 -23.39917 28.42002  1.000 19.08323 ? 233 GLN   B N   1 
ATOM   3867 C  CA  . GLN   B 1 237 ? 35.73415 -22.54745 27.75551  1.000 17.30135 ? 233 GLN   B CA  1 
ATOM   3868 C  C   . GLN   B 1 237 ? 35.19204 -21.14110 27.52246  1.000 19.44402 ? 233 GLN   B C   1 
ATOM   3869 O  O   . GLN   B 1 237 ? 34.00317 -20.94874 27.25124  1.000 14.03569 ? 233 GLN   B O   1 
ATOM   3870 C  CB  . GLN   B 1 237 ? 36.17461 -23.13887 26.40396  1.000 16.85971 ? 233 GLN   B CB  1 
ATOM   3871 C  CG  . GLN   B 1 237 ? 37.33871 -24.10560 26.49807  1.000 22.64821 ? 233 GLN   B CG  1 
ATOM   3872 C  CD  . GLN   B 1 237 ? 37.90285 -24.47861 25.13757  1.000 20.67403 ? 233 GLN   B CD  1 
ATOM   3873 O  OE1 . GLN   B 1 237 ? 39.09260 -24.30645 24.87768  1.000 31.94945 ? 233 GLN   B OE1 1 
ATOM   3874 N  NE2 . GLN   B 1 237 ? 37.04924 -24.99077 24.26449  1.000 28.28027 ? 233 GLN   B NE2 1 
ATOM   3875 N  N   . ARG   B 1 238 ? 36.09013 -20.16007 27.62218  1.000 15.09411 ? 234 ARG   B N   1 
ATOM   3876 C  CA  . ARG   B 1 238 ? 35.79895 -18.78219 27.25491  1.000 14.71141 ? 234 ARG   B CA  1 
ATOM   3877 C  C   . ARG   B 1 238 ? 35.99308 -18.60118 25.75027  1.000 14.52716 ? 234 ARG   B C   1 
ATOM   3878 O  O   . ARG   B 1 238 ? 36.38269 -19.52639 25.03568  1.000 15.95829 ? 234 ARG   B O   1 
ATOM   3879 C  CB  . ARG   B 1 238 ? 36.68483 -17.82336 28.05019  1.000 18.19545 ? 234 ARG   B CB  1 
ATOM   3880 C  CG  . ARG   B 1 238 ? 36.52514 -17.94394 29.56801  1.000 16.87079 ? 234 ARG   B CG  1 
ATOM   3881 C  CD  . ARG   B 1 238 ? 37.30679 -16.87090 30.31647  1.000 18.96911 ? 234 ARG   B CD  1 
ATOM   3882 N  NE  . ARG   B 1 238 ? 37.09999 -16.97255 31.75739  1.000 19.84323 ? 234 ARG   B NE  1 
ATOM   3883 C  CZ  . ARG   B 1 238 ? 36.04930 -16.48106 32.40058  1.000 23.49738 ? 234 ARG   B CZ  1 
ATOM   3884 N  NH1 . ARG   B 1 238 ? 35.10153 -15.81107 31.76643  1.000 16.38100 ? 234 ARG   B NH1 1 
ATOM   3885 N  NH2 . ARG   B 1 238 ? 35.94605 -16.66764 33.71406  1.000 22.04291 ? 234 ARG   B NH2 1 
ATOM   3886 N  N   . ARG   B 1 239 ? 35.71359 -17.39529 25.24756  1.000 16.16745 ? 235 ARG   B N   1 
ATOM   3887 C  CA  . ARG   B 1 239 ? 35.86566 -17.16487 23.81181  1.000 15.60768 ? 235 ARG   B CA  1 
ATOM   3888 C  C   . ARG   B 1 239 ? 37.32018 -17.29542 23.37071  1.000 18.56123 ? 235 ARG   B C   1 
ATOM   3889 O  O   . ARG   B 1 239 ? 37.58890 -17.70333 22.23458  1.000 18.44301 ? 235 ARG   B O   1 
ATOM   3890 C  CB  . ARG   B 1 239 ? 35.31856 -15.78865 23.42554  1.000 23.07545 ? 235 ARG   B CB  1 
ATOM   3891 C  CG  . ARG   B 1 239 ? 33.79966 -15.65968 23.48278  1.000 21.10614 ? 235 ARG   B CG  1 
ATOM   3892 C  CD  . ARG   B 1 239 ? 33.35147 -14.30969 22.92895  1.000 29.42606 ? 235 ARG   B CD  1 
ATOM   3893 N  NE  . ARG   B 1 239 ? 31.93753 -14.04391 23.16914  1.000 22.34691 ? 235 ARG   B NE  1 
ATOM   3894 C  CZ  . ARG   B 1 239 ? 30.95940 -14.38069 22.33963  1.000 30.94073 ? 235 ARG   B CZ  1 
ATOM   3895 N  NH1 . ARG   B 1 239 ? 31.20450 -15.00413 21.19849  1.000 36.60277 ? 235 ARG   B NH1 1 
ATOM   3896 N  NH2 . ARG   B 1 239 ? 29.70382 -14.08588 22.66350  1.000 33.69597 ? 235 ARG   B NH2 1 
ATOM   3897 N  N   . ASN   B 1 240 ? 38.26793 -16.96705 24.24633  1.000 22.21061 ? 236 ASN   B N   1 
ATOM   3898 C  CA  . ASN   B 1 240 ? 39.68574 -17.04824 23.91878  1.000 22.96441 ? 236 ASN   B CA  1 
ATOM   3899 C  C   . ASN   B 1 240 ? 40.27247 -18.43434 24.15981  1.000 26.25188 ? 236 ASN   B C   1 
ATOM   3900 O  O   . ASN   B 1 240 ? 41.49074 -18.60727 24.04922  1.000 26.82983 ? 236 ASN   B O   1 
ATOM   3901 C  CB  . ASN   B 1 240 ? 40.47955 -15.99714 24.70692  1.000 19.35399 ? 236 ASN   B CB  1 
ATOM   3902 C  CG  . ASN   B 1 240 ? 40.51211 -16.26586 26.20779  1.000 31.99025 ? 236 ASN   B CG  1 
ATOM   3903 O  OD1 . ASN   B 1 240 ? 39.95767 -17.24925 26.70280  1.000 27.63629 ? 236 ASN   B OD1 1 
ATOM   3904 N  ND2 . ASN   B 1 240 ? 41.18185 -15.38251 26.93995  1.000 33.49076 ? 236 ASN   B ND2 1 
ATOM   3905 N  N   . GLY   B 1 241 ? 39.44077 -19.41776 24.49636  1.000 19.21387 ? 237 GLY   B N   1 
ATOM   3906 C  CA  . GLY   B 1 241 ? 39.89971 -20.77319 24.68929  1.000 20.22168 ? 237 GLY   B CA  1 
ATOM   3907 C  C   . GLY   B 1 241 ? 40.36477 -21.11696 26.08921  1.000 26.87732 ? 237 GLY   B C   1 
ATOM   3908 O  O   . GLY   B 1 241 ? 40.60493 -22.29881 26.36671  1.000 28.01292 ? 237 GLY   B O   1 
ATOM   3909 N  N   . SER   B 1 242 ? 40.50819 -20.13914 26.98104  1.000 25.23660 ? 238 SER   B N   1 
ATOM   3910 C  CA  . SER   B 1 242 ? 40.89517 -20.45965 28.34839  1.000 18.82150 ? 238 SER   B CA  1 
ATOM   3911 C  C   . SER   B 1 242 ? 39.74127 -21.14915 29.07199  1.000 25.59391 ? 238 SER   B C   1 
ATOM   3912 O  O   . SER   B 1 242 ? 38.56815 -20.96578 28.73653  1.000 24.04759 ? 238 SER   B O   1 
ATOM   3913 C  CB  . SER   B 1 242 ? 41.33316 -19.19939 29.10267  1.000 28.37145 ? 238 SER   B CB  1 
ATOM   3914 O  OG  . SER   B 1 242 ? 40.31088 -18.21755 29.14207  1.000 26.82138 ? 238 SER   B OG  1 
ATOM   3915 N  N   . LYS   B 1 243 ? 40.08628 -21.95895 30.06810  1.000 20.77720 ? 239 LYS   B N   1 
ATOM   3916 C  CA  . LYS   B 1 243 ? 39.12381 -22.80323 30.75855  1.000 26.67854 ? 239 LYS   B CA  1 
ATOM   3917 C  C   . LYS   B 1 243 ? 38.69904 -22.17669 32.08160  1.000 33.62483 ? 239 LYS   B C   1 
ATOM   3918 O  O   . LYS   B 1 243 ? 39.44823 -21.41709 32.70145  1.000 22.34194 ? 239 LYS   B O   1 
ATOM   3919 C  CB  . LYS   B 1 243 ? 39.71406 -24.19215 31.01668  1.000 24.22507 ? 239 LYS   B CB  1 
ATOM   3920 C  CG  . LYS   B 1 243 ? 40.65238 -24.69981 29.91937  1.000 42.32717 ? 239 LYS   B CG  1 
ATOM   3921 C  CD  . LYS   B 1 243 ? 39.89403 -25.16691 28.68763  1.000 37.03094 ? 239 LYS   B CD  1 
ATOM   3922 C  CE  . LYS   B 1 243 ? 40.83102 -25.75453 27.63569  1.000 38.50324 ? 239 LYS   B CE  1 
ATOM   3923 N  NZ  . LYS   B 1 243 ? 41.78102 -24.74464 27.08320  1.000 37.08553 ? 239 LYS   B NZ  1 
ATOM   3924 N  N   . PHE   B 1 244 ? 37.48251 -22.50508 32.51289  1.000 23.27905 ? 240 PHE   B N   1 
ATOM   3925 C  CA  . PHE   B 1 244 ? 37.04253 -22.14070 33.85249  1.000 23.95168 ? 240 PHE   B CA  1 
ATOM   3926 C  C   . PHE   B 1 244 ? 36.09789 -23.21588 34.37101  1.000 22.18643 ? 240 PHE   B C   1 
ATOM   3927 O  O   . PHE   B 1 244 ? 35.48036 -23.94865 33.59432  1.000 20.49741 ? 240 PHE   B O   1 
ATOM   3928 C  CB  . PHE   B 1 244 ? 36.38542 -20.75084 33.88523  1.000 25.33645 ? 240 PHE   B CB  1 
ATOM   3929 C  CG  . PHE   B 1 244 ? 35.04740 -20.68077 33.20813  1.000 21.82663 ? 240 PHE   B CG  1 
ATOM   3930 C  CD1 . PHE   B 1 244 ? 33.87937 -20.76864 33.94905  1.000 20.89618 ? 240 PHE   B CD1 1 
ATOM   3931 C  CD2 . PHE   B 1 244 ? 34.95340 -20.49706 31.83523  1.000 19.72042 ? 240 PHE   B CD2 1 
ATOM   3932 C  CE1 . PHE   B 1 244 ? 32.64042 -20.69134 33.33481  1.000 21.03175 ? 240 PHE   B CE1 1 
ATOM   3933 C  CE2 . PHE   B 1 244 ? 33.71719 -20.42074 31.21371  1.000 18.69718 ? 240 PHE   B CE2 1 
ATOM   3934 C  CZ  . PHE   B 1 244 ? 32.55722 -20.51945 31.96371  1.000 14.74561 ? 240 PHE   B CZ  1 
ATOM   3935 N  N   . SER   B 1 245 ? 36.01031 -23.31772 35.69323  1.000 25.22079 ? 241 SER   B N   1 
ATOM   3936 C  CA  . SER   B 1 245 ? 35.24641 -24.37018 36.34761  1.000 24.60777 ? 241 SER   B CA  1 
ATOM   3937 C  C   . SER   B 1 245 ? 33.88934 -23.84877 36.79711  1.000 28.07602 ? 241 SER   B C   1 
ATOM   3938 O  O   . SER   B 1 245 ? 33.76215 -22.70219 37.23573  1.000 19.04191 ? 241 SER   B O   1 
ATOM   3939 C  CB  . SER   B 1 245 ? 36.00867 -24.93646 37.54705  1.000 24.13049 ? 241 SER   B CB  1 
ATOM   3940 O  OG  . SER   B 1 245 ? 37.09848 -25.72987 37.11242  1.000 35.76622 ? 241 SER   B OG  1 
ATOM   3941 N  N   . VAL   B 1 246 ? 32.87880 -24.70421 36.68494  1.000 23.58976 ? 242 VAL   B N   1 
ATOM   3942 C  CA  . VAL   B 1 246 ? 31.51097 -24.38227 37.06521  1.000 17.53932 ? 242 VAL   B CA  1 
ATOM   3943 C  C   . VAL   B 1 246 ? 31.09064 -25.33066 38.17703  1.000 22.88986 ? 242 VAL   B C   1 
ATOM   3944 O  O   . VAL   B 1 246 ? 31.18556 -26.55450 38.02234  1.000 18.65216 ? 242 VAL   B O   1 
ATOM   3945 C  CB  . VAL   B 1 246 ? 30.55189 -24.49032 35.86816  1.000 25.41997 ? 242 VAL   B CB  1 
ATOM   3946 C  CG1 . VAL   B 1 246 ? 29.12933 -24.39498 36.35169  1.000 17.22889 ? 242 VAL   B CG1 1 
ATOM   3947 C  CG2 . VAL   B 1 246 ? 30.85538 -23.40564 34.83863  1.000 21.10551 ? 242 VAL   B CG2 1 
ATOM   3948 N  N   . TYR   B 1 247 ? 30.62590 -24.76481 39.29517  1.000 23.47870 ? 243 TYR   B N   1 
ATOM   3949 C  CA  . TYR   B 1 247 ? 30.24575 -25.54658 40.46274  1.000 19.55918 ? 243 TYR   B CA  1 
ATOM   3950 C  C   . TYR   B 1 247 ? 28.76612 -25.46789 40.81696  1.000 23.20824 ? 243 TYR   B C   1 
ATOM   3951 O  O   . TYR   B 1 247 ? 28.31396 -26.24817 41.66129  1.000 19.99653 ? 243 TYR   B O   1 
ATOM   3952 C  CB  . TYR   B 1 247 ? 31.06212 -25.10950 41.69046  1.000 20.61900 ? 243 TYR   B CB  1 
ATOM   3953 C  CG  . TYR   B 1 247 ? 32.53619 -25.44127 41.61729  1.000 28.59462 ? 243 TYR   B CG  1 
ATOM   3954 C  CD1 . TYR   B 1 247 ? 33.02343 -26.63641 42.12978  1.000 31.98692 ? 243 TYR   B CD1 1 
ATOM   3955 C  CD2 . TYR   B 1 247 ? 33.44310 -24.55445 41.05146  1.000 29.64324 ? 243 TYR   B CD2 1 
ATOM   3956 C  CE1 . TYR   B 1 247 ? 34.36907 -26.94252 42.07458  1.000 31.48143 ? 243 TYR   B CE1 1 
ATOM   3957 C  CE2 . TYR   B 1 247 ? 34.79401 -24.85520 40.99066  1.000 31.51411 ? 243 TYR   B CE2 1 
ATOM   3958 C  CZ  . TYR   B 1 247 ? 35.24862 -26.05203 41.50284  1.000 36.28083 ? 243 TYR   B CZ  1 
ATOM   3959 O  OH  . TYR   B 1 247 ? 36.58867 -26.36039 41.44804  1.000 48.31773 ? 243 TYR   B OH  1 
ATOM   3960 N  N   . ASP   B 1 248 ? 27.99786 -24.56788 40.20717  1.000 20.12598 ? 244 ASP   B N   1 
ATOM   3961 C  CA  . ASP   B 1 248 ? 26.62690 -24.35379 40.64549  1.000 23.03111 ? 244 ASP   B CA  1 
ATOM   3962 C  C   . ASP   B 1 248 ? 25.74357 -24.04600 39.44825  1.000 20.31995 ? 244 ASP   B C   1 
ATOM   3963 O  O   . ASP   B 1 248 ? 26.20765 -23.51427 38.43951  1.000 20.82221 ? 244 ASP   B O   1 
ATOM   3964 C  CB  . ASP   B 1 248 ? 26.54484 -23.21662 41.66740  1.000 18.72313 ? 244 ASP   B CB  1 
ATOM   3965 C  CG  . ASP   B 1 248 ? 25.13697 -23.00069 42.18396  1.000 29.18847 ? 244 ASP   B CG  1 
ATOM   3966 O  OD1 . ASP   B 1 248 ? 24.65024 -23.84735 42.96094  1.000 26.52121 ? 244 ASP   B OD1 1 
ATOM   3967 O  OD2 . ASP   B 1 248 ? 24.51194 -21.99137 41.79935  1.000 25.11054 ? 244 ASP   B OD2 1 
ATOM   3968 N  N   . VAL   B 1 249 ? 24.45394 -24.36633 39.58102  1.000 17.06685 ? 245 VAL   B N   1 
ATOM   3969 C  CA  . VAL   B 1 249 ? 23.52335 -24.20162 38.46978  1.000 17.98131 ? 245 VAL   B CA  1 
ATOM   3970 C  C   . VAL   B 1 249 ? 23.31335 -22.73510 38.09797  1.000 15.93176 ? 245 VAL   B C   1 
ATOM   3971 O  O   . VAL   B 1 249 ? 22.98812 -22.43615 36.94190  1.000 15.69885 ? 245 VAL   B O   1 
ATOM   3972 C  CB  . VAL   B 1 249 ? 22.18418 -24.88318 38.81453  1.000 17.80442 ? 245 VAL   B CB  1 
ATOM   3973 C  CG1 . VAL   B 1 249 ? 21.52340 -24.20395 40.01680  1.000 16.98187 ? 245 VAL   B CG1 1 
ATOM   3974 C  CG2 . VAL   B 1 249 ? 21.24914 -24.90159 37.60770  1.000 16.85856 ? 245 VAL   B CG2 1 
ATOM   3975 N  N   . SER   B 1 250 ? 23.52370 -21.80669 39.03929  1.000 17.32950 ? 246 SER   B N   1 
ATOM   3976 C  CA  . SER   B 1 250 ? 23.15286 -20.40943 38.81568  1.000 19.00821 ? 246 SER   B CA  1 
ATOM   3977 C  C   . SER   B 1 250 ? 23.92423 -19.77481 37.66459  1.000 17.73212 ? 246 SER   B C   1 
ATOM   3978 O  O   . SER   B 1 250 ? 23.40603 -18.87132 36.99826  1.000 19.19326 ? 246 SER   B O   1 
ATOM   3979 C  CB  . SER   B 1 250 ? 23.36954 -19.59453 40.09047  1.000 20.69184 ? 246 SER   B CB  1 
ATOM   3980 O  OG  . SER   B 1 250 ? 24.73815 -19.57344 40.45607  1.000 25.17971 ? 246 SER   B OG  1 
ATOM   3981 N  N   . ILE   B 1 251 ? 25.16240 -20.20749 37.42019  1.000 15.20237 ? 247 ILE   B N   1 
ATOM   3982 C  CA  . ILE   B 1 251 ? 25.91612 -19.60741 36.32683  1.000 21.47266 ? 247 ILE   B CA  1 
ATOM   3983 C  C   . ILE   B 1 251 ? 25.38452 -20.07241 34.97338  1.000 13.89052 ? 247 ILE   B C   1 
ATOM   3984 O  O   . ILE   B 1 251 ? 25.61974 -19.40918 33.95660  1.000 21.26184 ? 247 ILE   B O   1 
ATOM   3985 C  CB  . ILE   B 1 251 ? 27.42542 -19.88962 36.50709  1.000 27.82783 ? 247 ILE   B CB  1 
ATOM   3986 C  CG1 . ILE   B 1 251 ? 28.22565 -19.61326 35.23066  1.000 22.63743 ? 247 ILE   B CG1 1 
ATOM   3987 C  CG2 . ILE   B 1 251 ? 27.65511 -21.28645 36.97774  1.000 28.08301 ? 247 ILE   B CG2 1 
ATOM   3988 C  CD1 . ILE   B 1 251 ? 29.71369 -19.81034 35.39062  1.000 40.24283 ? 247 ILE   B CD1 1 
ATOM   3989 N  N   . LEU   B 1 252 ? 24.61589 -21.16011 34.93718  1.000 14.75165 ? 248 LEU   B N   1 
ATOM   3990 C  CA  . LEU   B 1 252 ? 24.09172 -21.67155 33.67315  1.000 17.29525 ? 248 LEU   B CA  1 
ATOM   3991 C  C   . LEU   B 1 252 ? 22.69062 -21.18622 33.34679  1.000 15.01247 ? 248 LEU   B C   1 
ATOM   3992 O  O   . LEU   B 1 252 ? 22.24061 -21.37208 32.21126  1.000 14.34708 ? 248 LEU   B O   1 
ATOM   3993 C  CB  . LEU   B 1 252 ? 24.05385 -23.20596 33.66922  1.000 15.11285 ? 248 LEU   B CB  1 
ATOM   3994 C  CG  . LEU   B 1 252 ? 25.35048 -24.00851 33.62696  1.000 18.12253 ? 248 LEU   B CG  1 
ATOM   3995 C  CD1 . LEU   B 1 252 ? 26.26432 -23.52104 32.51230  1.000 23.48967 ? 248 LEU   B CD1 1 
ATOM   3996 C  CD2 . LEU   B 1 252 ? 26.03431 -23.94917 34.96173  1.000 33.18438 ? 248 LEU   B CD2 1 
ATOM   3997 N  N   . ILE   B 1 253 ? 21.97722 -20.61286 34.31316  1.000 19.58429 ? 249 ILE   B N   1 
ATOM   3998 C  CA  . ILE   B 1 253 ? 20.56685 -20.26930 34.08768  1.000 29.89094 ? 249 ILE   B CA  1 
ATOM   3999 C  C   . ILE   B 1 253 ? 20.38416 -19.35589 32.88009  1.000 31.76262 ? 249 ILE   B C   1 
ATOM   4000 O  O   . ILE   B 1 253 ? 19.47493 -19.60980 32.07420  1.000 25.51579 ? 249 ILE   B O   1 
ATOM   4001 C  CB  . ILE   B 1 253 ? 19.94705 -19.69251 35.37094  1.000 21.44450 ? 249 ILE   B CB  1 
ATOM   4002 C  CG1 . ILE   B 1 253 ? 19.83885 -20.78485 36.44154  1.000 20.86651 ? 249 ILE   B CG1 1 
ATOM   4003 C  CG2 . ILE   B 1 253 ? 18.58982 -19.07877 35.07356  1.000 33.82186 ? 249 ILE   B CG2 1 
ATOM   4004 C  CD1 . ILE   B 1 253 ? 19.17994 -20.31640 37.72481  1.000 33.15932 ? 249 ILE   B CD1 1 
ATOM   4005 N  N   . PRO   B 1 254 ? 21.18497 -18.30539 32.67097  1.000 21.03361 ? 250 PRO   B N   1 
ATOM   4006 C  CA  . PRO   B 1 254 ? 21.05294 -17.51288 31.44237  1.000 20.38981 ? 250 PRO   B CA  1 
ATOM   4007 C  C   . PRO   B 1 254 ? 21.62711 -18.18009 30.19970  1.000 22.43166 ? 250 PRO   B C   1 
ATOM   4008 O  O   . PRO   B 1 254 ? 21.58888 -17.57244 29.12774  1.000 17.53092 ? 250 PRO   B O   1 
ATOM   4009 C  CB  . PRO   B 1 254 ? 21.83026 -16.22507 31.77429  1.000 21.53641 ? 250 PRO   B CB  1 
ATOM   4010 C  CG  . PRO   B 1 254 ? 21.99968 -16.21994 33.25892  1.000 30.07917 ? 250 PRO   B CG  1 
ATOM   4011 C  CD  . PRO   B 1 254 ? 22.09311 -17.65538 33.63563  1.000 22.89147 ? 250 PRO   B CD  1 
ATOM   4012 N  N   . ILE   B 1 255 ? 22.13189 -19.41158 30.29749  1.000 14.76544 ? 251 ILE   B N   1 
ATOM   4013 C  CA  . ILE   B 1 255 ? 22.98052 -20.00558 29.27291  1.000 14.03060 ? 251 ILE   B CA  1 
ATOM   4014 C  C   . ILE   B 1 255 ? 22.31857 -21.21451 28.62065  1.000 15.49049 ? 251 ILE   B C   1 
ATOM   4015 O  O   . ILE   B 1 255 ? 22.28801 -21.33041 27.39022  1.000 11.06812 ? 251 ILE   B O   1 
ATOM   4016 C  CB  . ILE   B 1 255 ? 24.36523 -20.38024 29.84642  1.000 14.81151 ? 251 ILE   B CB  1 
ATOM   4017 C  CG1 . ILE   B 1 255 ? 25.03915 -19.14468 30.44005  1.000 19.56742 ? 251 ILE   B CG1 1 
ATOM   4018 C  CG2 . ILE   B 1 255 ? 25.24105 -20.99938 28.77986  1.000 21.94798 ? 251 ILE   B CG2 1 
ATOM   4019 C  CD1 . ILE   B 1 255 ? 25.31893 -18.04176 29.43879  1.000 14.93488 ? 251 ILE   B CD1 1 
ATOM   4020 N  N   . ILE   B 1 256 ? 21.80073 -22.13743 29.42724  1.000 14.01617 ? 252 ILE   B N   1 
ATOM   4021 C  CA  . ILE   B 1 256 ? 21.20077 -23.36832 28.92248  1.000 13.88617 ? 252 ILE   B CA  1 
ATOM   4022 C  C   . ILE   B 1 256 ? 19.68521 -23.25179 29.02397  1.000 15.15068 ? 252 ILE   B C   1 
ATOM   4023 O  O   . ILE   B 1 256 ? 19.15115 -22.79796 30.04509  1.000 21.24741 ? 252 ILE   B O   1 
ATOM   4024 C  CB  . ILE   B 1 256 ? 21.73281 -24.60230 29.67525  1.000 12.88951 ? 252 ILE   B CB  1 
ATOM   4025 C  CG1 . ILE   B 1 256 ? 21.18567 -25.88988 29.04772  1.000 12.20437 ? 252 ILE   B CG1 1 
ATOM   4026 C  CG2 . ILE   B 1 256 ? 21.41727 -24.52609 31.15711  1.000 13.78292 ? 252 ILE   B CG2 1 
ATOM   4027 C  CD1 . ILE   B 1 256 ? 22.00038 -27.12593 29.38039  1.000 17.43715 ? 252 ILE   B CD1 1 
ATOM   4028 N  N   . ALA   B 1 257 ? 18.99031 -23.62530 27.94753  1.000 11.95602 ? 253 ALA   B N   1 
ATOM   4029 C  CA  . ALA   B 1 257 ? 17.55228 -23.42060 27.84671  1.000 13.21634 ? 253 ALA   B CA  1 
ATOM   4030 C  C   . ALA   B 1 257 ? 16.73957 -24.69647 27.97011  1.000 12.88378 ? 253 ALA   B C   1 
ATOM   4031 O  O   . ALA   B 1 257 ? 15.55761 -24.62134 28.31338  1.000 19.46032 ? 253 ALA   B O   1 
ATOM   4032 C  CB  . ALA   B 1 257 ? 17.19971 -22.74929 26.50962  1.000 16.36195 ? 253 ALA   B CB  1 
ATOM   4033 N  N   . LEU   B 1 258 ? 17.33321 -25.85104 27.68382  1.000 13.12298 ? 254 LEU   B N   1 
ATOM   4034 C  CA  . LEU   B 1 258 ? 16.63927 -27.12928 27.70631  1.000 17.06650 ? 254 LEU   B CA  1 
ATOM   4035 C  C   . LEU   B 1 258 ? 17.62814 -28.19430 28.15260  1.000 11.66263 ? 254 LEU   B C   1 
ATOM   4036 O  O   . LEU   B 1 258 ? 18.82265 -28.11193 27.85229  1.000 16.52241 ? 254 LEU   B O   1 
ATOM   4037 C  CB  . LEU   B 1 258 ? 16.06886 -27.49918 26.32651  1.000 19.35506 ? 254 LEU   B CB  1 
ATOM   4038 C  CG  . LEU   B 1 258 ? 15.06665 -26.56959 25.64437  1.000 16.92443 ? 254 LEU   B CG  1 
ATOM   4039 C  CD1 . LEU   B 1 258 ? 14.95422 -26.91303 24.17475  1.000 16.66373 ? 254 LEU   B CD1 1 
ATOM   4040 C  CD2 . LEU   B 1 258 ? 13.70783 -26.65375 26.31139  1.000 29.04636 ? 254 LEU   B CD2 1 
ATOM   4041 N  N   . MET   B 1 259 ? 17.12387 -29.19719 28.86421  1.000 13.14313 ? 255 MET   B N   1 
ATOM   4042 C  CA  . MET   B 1 259 ? 17.93288 -30.32658 29.29959  1.000 12.68583 ? 255 MET   B CA  1 
ATOM   4043 C  C   . MET   B 1 259 ? 17.26884 -31.63086 28.88694  1.000 17.56809 ? 255 MET   B C   1 
ATOM   4044 O  O   . MET   B 1 259 ? 16.04333 -31.76263 28.95921  1.000 15.49314 ? 255 MET   B O   1 
ATOM   4045 C  CB  . MET   B 1 259 ? 18.13090 -30.32643 30.82291  1.000 15.09826 ? 255 MET   B CB  1 
ATOM   4046 C  CG  . MET   B 1 259 ? 18.85306 -29.10880 31.36314  1.000 13.14849 ? 255 MET   B CG  1 
ATOM   4047 S  SD  . MET   B 1 259 ? 19.11013 -29.22380 33.14916  1.000 18.59048 ? 255 MET   B SD  1 
ATOM   4048 C  CE  . MET   B 1 259 ? 17.42894 -29.08981 33.74939  1.000 20.19389 ? 255 MET   B CE  1 
ATOM   4049 N  N   . VAL   B 1 260 ? 18.08375 -32.60081 28.46963  1.000 14.25786 ? 256 VAL   B N   1 
ATOM   4050 C  CA  . VAL   B 1 260 ? 17.58005 -33.95416 28.27656  1.000 16.20725 ? 256 VAL   B CA  1 
ATOM   4051 C  C   . VAL   B 1 260 ? 17.21664 -34.53941 29.63481  1.000 18.21844 ? 256 VAL   B C   1 
ATOM   4052 O  O   . VAL   B 1 260 ? 17.87054 -34.25671 30.64770  1.000 16.89227 ? 256 VAL   B O   1 
ATOM   4053 C  CB  . VAL   B 1 260 ? 18.61858 -34.82246 27.53949  1.000 14.35542 ? 256 VAL   B CB  1 
ATOM   4054 C  CG1 . VAL   B 1 260 ? 19.90201 -34.95133 28.35166  1.000 18.01880 ? 256 VAL   B CG1 1 
ATOM   4055 C  CG2 . VAL   B 1 260 ? 18.04998 -36.19964 27.20330  1.000 14.53118 ? 256 VAL   B CG2 1 
ATOM   4056 N  N   . TYR   B 1 261 ? 16.14371 -35.32674 29.67030  1.000 14.85900 ? 257 TYR   B N   1 
ATOM   4057 C  CA  . TYR   B 1 261 ? 15.70086 -35.95616 30.90836  1.000 16.05751 ? 257 TYR   B CA  1 
ATOM   4058 C  C   . TYR   B 1 261 ? 16.72961 -36.98625 31.36240  1.000 25.32031 ? 257 TYR   B C   1 
ATOM   4059 O  O   . TYR   B 1 261 ? 17.07096 -37.90557 30.61158  1.000 16.69598 ? 257 TYR   B O   1 
ATOM   4060 C  CB  . TYR   B 1 261 ? 14.33564 -36.60941 30.70032  1.000 18.02845 ? 257 TYR   B CB  1 
ATOM   4061 C  CG  . TYR   B 1 261 ? 13.69574 -37.18560 31.95040  1.000 17.65358 ? 257 TYR   B CG  1 
ATOM   4062 C  CD1 . TYR   B 1 261 ? 13.91484 -38.50551 32.32348  1.000 17.82004 ? 257 TYR   B CD1 1 
ATOM   4063 C  CD2 . TYR   B 1 261 ? 12.85129 -36.41686 32.73788  1.000 16.94260 ? 257 TYR   B CD2 1 
ATOM   4064 C  CE1 . TYR   B 1 261 ? 13.32277 -39.03686 33.45572  1.000 23.81983 ? 257 TYR   B CE1 1 
ATOM   4065 C  CE2 . TYR   B 1 261 ? 12.25354 -36.93877 33.86765  1.000 17.88420 ? 257 TYR   B CE2 1 
ATOM   4066 C  CZ  . TYR   B 1 261 ? 12.49335 -38.24915 34.22282  1.000 18.79014 ? 257 TYR   B CZ  1 
ATOM   4067 O  OH  . TYR   B 1 261 ? 11.89927 -38.77058 35.34904  1.000 23.76428 ? 257 TYR   B OH  1 
ATOM   4068 N  N   . ARG   B 1 262 ? 17.22615 -36.83000 32.58740  1.000 17.00902 ? 258 ARG   B N   1 
ATOM   4069 C  CA  . ARG   B 1 262 ? 18.17752 -37.76104 33.18161  1.000 20.86766 ? 258 ARG   B CA  1 
ATOM   4070 C  C   . ARG   B 1 262 ? 17.60247 -38.54704 34.34453  1.000 19.00715 ? 258 ARG   B C   1 
ATOM   4071 O  O   . ARG   B 1 262 ? 17.87126 -39.74306 34.46292  1.000 19.88608 ? 258 ARG   B O   1 
ATOM   4072 C  CB  . ARG   B 1 262 ? 19.42473 -37.01549 33.66711  1.000 25.69214 ? 258 ARG   B CB  1 
ATOM   4073 C  CG  . ARG   B 1 262 ? 20.29056 -36.45889 32.56014  1.000 23.14494 ? 258 ARG   B CG  1 
ATOM   4074 C  CD  . ARG   B 1 262 ? 20.68517 -37.53987 31.57655  1.000 30.88151 ? 258 ARG   B CD  1 
ATOM   4075 N  NE  . ARG   B 1 262 ? 21.87026 -37.15336 30.82354  1.000 30.07613 ? 258 ARG   B NE  1 
ATOM   4076 C  CZ  . ARG   B 1 262 ? 22.16669 -37.60143 29.61402  1.000 29.88544 ? 258 ARG   B CZ  1 
ATOM   4077 N  NH1 . ARG   B 1 262 ? 21.36912 -38.44243 28.97570  1.000 30.97469 ? 258 ARG   B NH1 1 
ATOM   4078 N  NH2 . ARG   B 1 262 ? 23.28477 -37.18569 29.02584  1.000 19.66193 ? 258 ARG   B NH2 1 
ATOM   4079 N  N   . CYS   B 1 263 ? 16.82299 -37.89857 35.20646  1.000 23.85149 ? 259 CYS   B N   1 
ATOM   4080 C  CA  . CYS   B 1 263 ? 16.28024 -38.53458 36.39948  1.000 26.31820 ? 259 CYS   B CA  1 
ATOM   4081 C  C   . CYS   B 1 263 ? 15.10229 -37.70933 36.89617  1.000 22.27168 ? 259 CYS   B C   1 
ATOM   4082 O  O   . CYS   B 1 263 ? 14.85666 -36.59435 36.42947  1.000 21.13174 ? 259 CYS   B O   1 
ATOM   4083 C  CB  . CYS   B 1 263 ? 17.34382 -38.66491 37.49417  1.000 23.68754 ? 259 CYS   B CB  1 
ATOM   4084 S  SG  . CYS   B 1 263 ? 18.03130 -37.07254 38.03352  1.000 26.59438 ? 259 CYS   B SG  1 
ATOM   4085 N  N   . ALA   B 1 264 ? 14.37961 -38.26999 37.85970  1.000 24.91817 ? 260 ALA   B N   1 
ATOM   4086 C  CA  . ALA   B 1 264 ? 13.31316 -37.53450 38.51481  1.000 26.71563 ? 260 ALA   B CA  1 
ATOM   4087 C  C   . ALA   B 1 264 ? 13.89976 -36.52061 39.49290  1.000 23.89343 ? 260 ALA   B C   1 
ATOM   4088 O  O   . ALA   B 1 264 ? 15.04683 -36.65634 39.92685  1.000 32.74370 ? 260 ALA   B O   1 
ATOM   4089 C  CB  . ALA   B 1 264 ? 12.37810 -38.49619 39.24063  1.000 24.90618 ? 260 ALA   B CB  1 
ATOM   4090 N  N   . PRO   B 1 265 ? 13.14750 -35.47497 39.82601  1.000 28.19617 ? 261 PRO   B N   1 
ATOM   4091 C  CA  . PRO   B 1 265 ? 13.64028 -34.47145 40.78449  1.000 27.54169 ? 261 PRO   B CA  1 
ATOM   4092 C  C   . PRO   B 1 265 ? 14.02489 -35.10985 42.10689  1.000 32.18772 ? 261 PRO   B C   1 
ATOM   4093 O  O   . PRO   B 1 265 ? 13.32277 -36.00242 42.60716  1.000 23.49727 ? 261 PRO   B O   1 
ATOM   4094 C  CB  . PRO   B 1 265 ? 12.44690 -33.51586 40.95206  1.000 28.97184 ? 261 PRO   B CB  1 
ATOM   4095 C  CG  . PRO   B 1 265 ? 11.35910 -34.02199 40.01943  1.000 43.38447 ? 261 PRO   B CG  1 
ATOM   4096 C  CD  . PRO   B 1 265 ? 11.98448 -34.98603 39.07130  1.000 31.10466 ? 261 PRO   B CD  1 
ATOM   4097 N  N   . PRO   B 1 266 ? 15.12864 -34.67049 42.70569  1.000 25.89029 ? 262 PRO   B N   1 
ATOM   4098 C  CA  . PRO   B 1 266 ? 15.62756 -35.30147 43.93258  1.000 31.30633 ? 262 PRO   B CA  1 
ATOM   4099 C  C   . PRO   B 1 266 ? 14.67500 -35.08281 45.09329  1.000 31.93015 ? 262 PRO   B C   1 
ATOM   4100 O  O   . PRO   B 1 266 ? 13.77932 -34.22712 45.02293  1.000 35.26997 ? 262 PRO   B O   1 
ATOM   4101 C  CB  . PRO   B 1 266 ? 16.96926 -34.58715 44.17617  1.000 40.91200 ? 262 PRO   B CB  1 
ATOM   4102 C  CG  . PRO   B 1 266 ? 17.31499 -33.93763 42.87877  1.000 44.36970 ? 262 PRO   B CG  1 
ATOM   4103 C  CD  . PRO   B 1 266 ? 16.01094 -33.58705 42.24516  1.000 40.95561 ? 262 PRO   B CD  1 
ATOM   4104 N  N   . PRO   B 1 267 ? 14.83492 -35.84316 46.18876  1.000 31.14837 ? 263 PRO   B N   1 
ATOM   4105 C  CA  . PRO   B 1 267 ? 14.02558 -35.66600 47.40035  1.000 33.81366 ? 263 PRO   B CA  1 
ATOM   4106 C  C   . PRO   B 1 267 ? 14.27302 -34.31936 48.07865  1.000 39.37536 ? 263 PRO   B C   1 
ATOM   4107 O  O   . PRO   B 1 267 ? 13.40999 -33.44334 48.01719  1.000 35.40025 ? 263 PRO   B O   1 
ATOM   4108 C  CB  . PRO   B 1 267 ? 14.48564 -36.81820 48.30389  1.000 34.03527 ? 263 PRO   B CB  1 
ATOM   4109 C  CG  . PRO   B 1 267 ? 15.09874 -37.81456 47.37937  1.000 30.51125 ? 263 PRO   B CG  1 
ATOM   4110 C  CD  . PRO   B 1 267 ? 15.73710 -37.00290 46.30054  1.000 29.62819 ? 263 PRO   B CD  1 
HETATM 4111 C  C10 . A1BH4 C 2 .   ? 26.88846 -11.69597 32.77505  1.000 15.44280 ? 301 A1BH4 A C10 1 
HETATM 4112 C  C13 . A1BH4 C 2 .   ? 28.92589 -12.95522 33.70851  1.000 22.91339 ? 301 A1BH4 A C13 1 
HETATM 4113 C  C15 . A1BH4 C 2 .   ? 30.25091 -13.67380 33.92663  1.000 20.16477 ? 301 A1BH4 A C15 1 
HETATM 4114 C  C01 . A1BH4 C 2 .   ? 25.90280 -8.83501  34.42336  1.000 31.81166 ? 301 A1BH4 A C01 1 
HETATM 4115 C  C02 . A1BH4 C 2 .   ? 26.59892 -8.84675  33.06968  1.000 15.68767 ? 301 A1BH4 A C02 1 
HETATM 4116 C  C03 . A1BH4 C 2 .   ? 25.75626 -9.57778  32.03519  1.000 26.41306 ? 301 A1BH4 A C03 1 
HETATM 4117 C  C04 . A1BH4 C 2 .   ? 24.85689 -8.87430  31.25168  1.000 21.15797 ? 301 A1BH4 A C04 1 
HETATM 4118 C  C05 . A1BH4 C 2 .   ? 24.09125 -9.54663  30.31305  1.000 18.40186 ? 301 A1BH4 A C05 1 
HETATM 4119 C  C06 . A1BH4 C 2 .   ? 24.22382 -10.91832 30.17084  1.000 20.13354 ? 301 A1BH4 A C06 1 
HETATM 4120 C  C07 . A1BH4 C 2 .   ? 25.12105 -11.62148 30.95596  1.000 21.62575 ? 301 A1BH4 A C07 1 
HETATM 4121 C  C08 . A1BH4 C 2 .   ? 25.25012 -13.13186 30.78501  1.000 24.11742 ? 301 A1BH4 A C08 1 
HETATM 4122 C  C09 . A1BH4 C 2 .   ? 25.88200 -10.94923 31.90260  1.000 15.82346 ? 301 A1BH4 A C09 1 
HETATM 4123 C  C11 . A1BH4 C 2 .   ? 26.78191 -12.01576 34.14104  1.000 16.87581 ? 301 A1BH4 A C11 1 
HETATM 4124 C  C12 . A1BH4 C 2 .   ? 27.91912 -12.71226 34.65325  1.000 13.86143 ? 301 A1BH4 A C12 1 
HETATM 4125 O  O16 . A1BH4 C 2 .   ? 31.01214 -13.86684 32.94588  1.000 19.90299 ? 301 A1BH4 A O16 1 
HETATM 4126 O  O17 . A1BH4 C 2 .   ? 30.57915 -14.07020 35.07269  1.000 19.58398 ? 301 A1BH4 A O17 1 
HETATM 4127 S  S14 . A1BH4 C 2 .   ? 28.38239 -12.28748 32.25679  1.000 19.75406 ? 301 A1BH4 A S14 1 
HETATM 4128 CL CL  . CL    D 3 .   ? -1.75908 11.51504  52.31929  1.000 42.10088 ? 302 CL    A CL  1 
HETATM 4129 C  C10 . A1BH4 E 2 .   ? 31.03458 -17.49506 29.00515  1.000 18.24497 ? 301 A1BH4 B C10 1 
HETATM 4130 C  C13 . A1BH4 E 2 .   ? 33.02287 -16.13440 28.11936  1.000 20.34850 ? 301 A1BH4 B C13 1 
HETATM 4131 C  C15 . A1BH4 E 2 .   ? 34.31681 -15.35561 27.93795  1.000 25.51559 ? 301 A1BH4 B C15 1 
HETATM 4132 C  C01 . A1BH4 E 2 .   ? 30.24106 -20.65974 27.43614  1.000 21.90302 ? 301 A1BH4 B C01 1 
HETATM 4133 C  C02 . A1BH4 E 2 .   ? 30.96133 -20.35084 28.74040  1.000 18.06457 ? 301 A1BH4 B C02 1 
HETATM 4134 C  C03 . A1BH4 E 2 .   ? 30.03146 -19.66792 29.73190  1.000 14.00730 ? 301 A1BH4 B C03 1 
HETATM 4135 C  C04 . A1BH4 E 2 .   ? 29.15444 -20.42362 30.48577  1.000 20.81711 ? 301 A1BH4 B C04 1 
HETATM 4136 C  C05 . A1BH4 E 2 .   ? 28.31274 -19.79478 31.38839  1.000 19.76312 ? 301 A1BH4 B C05 1 
HETATM 4137 C  C06 . A1BH4 E 2 .   ? 28.33586 -18.41688 31.52058  1.000 17.35115 ? 301 A1BH4 B C06 1 
HETATM 4138 C  C07 . A1BH4 E 2 .   ? 29.20579 -17.65908 30.75667  1.000 17.04737 ? 301 A1BH4 B C07 1 
HETATM 4139 C  C08 . A1BH4 E 2 .   ? 29.22906 -16.14083 30.90950  1.000 19.81764 ? 301 A1BH4 B C08 1 
HETATM 4140 C  C09 . A1BH4 E 2 .   ? 30.04723 -18.28691 29.85355  1.000 17.66363 ? 301 A1BH4 B C09 1 
HETATM 4141 C  C11 . A1BH4 E 2 .   ? 30.95339 -17.21198 27.63317  1.000 16.74934 ? 301 A1BH4 B C11 1 
HETATM 4142 C  C12 . A1BH4 E 2 .   ? 32.06634 -16.45552 27.14567  1.000 17.28419 ? 301 A1BH4 B C12 1 
HETATM 4143 O  O16 . A1BH4 E 2 .   ? 34.95472 -14.98617 28.95920  1.000 21.67830 ? 301 A1BH4 B O16 1 
HETATM 4144 O  O17 . A1BH4 E 2 .   ? 34.75512 -15.12256 26.78212  1.000 16.18116 ? 301 A1BH4 B O17 1 
HETATM 4145 S  S14 . A1BH4 E 2 .   ? 32.46770 -16.79681 29.57002  1.000 15.90410 ? 301 A1BH4 B S14 1 
HETATM 4146 O  O   . HOH   F 4 .   ? 17.14563 -2.13586  12.08262  1.000 31.64858 ? 401 HOH   A O   1 
HETATM 4147 O  O   . HOH   F 4 .   ? 28.34419 -10.05313 58.20767  1.000 40.46549 ? 402 HOH   A O   1 
HETATM 4148 O  O   . HOH   F 4 .   ? 31.48582 -22.76046 52.36988  1.000 42.28271 ? 403 HOH   A O   1 
HETATM 4149 O  O   . HOH   F 4 .   ? 33.60575 -6.20754  22.15400  1.000 36.30671 ? 404 HOH   A O   1 
HETATM 4150 O  O   . HOH   F 4 .   ? 26.87214 5.26467   43.03076  1.000 37.37575 ? 405 HOH   A O   1 
HETATM 4151 O  O   . HOH   F 4 .   ? 7.13413  21.65387  44.06393  1.000 42.82291 ? 406 HOH   A O   1 
HETATM 4152 O  O   . HOH   F 4 .   ? 29.73927 12.13501  49.94012  1.000 32.16352 ? 407 HOH   A O   1 
HETATM 4153 O  O   . HOH   F 4 .   ? 1.55192  4.45972   59.88770  1.000 34.16447 ? 408 HOH   A O   1 
HETATM 4154 O  O   . HOH   F 4 .   ? 20.95572 1.65187   41.59157  1.000 26.46929 ? 409 HOH   A O   1 
HETATM 4155 O  O   . HOH   F 4 .   ? 29.36783 -1.47214  57.60667  1.000 31.51614 ? 410 HOH   A O   1 
HETATM 4156 O  O   . HOH   F 4 .   ? 18.53800 -19.10427 57.36152  1.000 21.83958 ? 411 HOH   A O   1 
HETATM 4157 O  O   . HOH   F 4 .   ? 10.24873 -11.12545 20.76816  1.000 37.30174 ? 412 HOH   A O   1 
HETATM 4158 O  O   . HOH   F 4 .   ? 10.77121 -14.45685 38.98325  1.000 41.65055 ? 413 HOH   A O   1 
HETATM 4159 O  O   . HOH   F 4 .   ? 13.18682 -13.93371 37.86283  1.000 37.11439 ? 414 HOH   A O   1 
HETATM 4160 O  O   . HOH   F 4 .   ? 3.00387  12.85868  60.12771  1.000 25.94282 ? 415 HOH   A O   1 
HETATM 4161 O  O   . HOH   F 4 .   ? 16.752   -9.259    64.190    1.000 36.86047 ? 416 HOH   A O   1 
HETATM 4162 O  O   . HOH   F 4 .   ? 29.30401 3.64894   45.20703  1.000 25.26569 ? 417 HOH   A O   1 
HETATM 4163 O  O   . HOH   F 4 .   ? 30.03063 -13.20034 27.74529  1.000 29.08540 ? 418 HOH   A O   1 
HETATM 4164 O  O   . HOH   F 4 .   ? 5.46131  -24.17407 45.12772  1.000 43.37952 ? 419 HOH   A O   1 
HETATM 4165 O  O   . HOH   F 4 .   ? 4.23180  2.76099   61.76173  1.000 51.43559 ? 420 HOH   A O   1 
HETATM 4166 O  O   . HOH   F 4 .   ? 28.15164 -16.36344 35.96253  1.000 33.50376 ? 421 HOH   A O   1 
HETATM 4167 O  O   . HOH   F 4 .   ? 21.17107 -13.00379 61.38346  1.000 24.06395 ? 422 HOH   A O   1 
HETATM 4168 O  O   . HOH   F 4 .   ? -2.36062 0.75177   51.95409  1.000 22.44887 ? 423 HOH   A O   1 
HETATM 4169 O  O   . HOH   F 4 .   ? 12.40928 11.44399  41.69884  1.000 31.96734 ? 424 HOH   A O   1 
HETATM 4170 O  O   . HOH   F 4 .   ? 27.79564 0.58212   32.40077  1.000 30.41741 ? 425 HOH   A O   1 
HETATM 4171 O  O   . HOH   F 4 .   ? 32.39445 -3.94259  40.58391  1.000 30.92626 ? 426 HOH   A O   1 
HETATM 4172 O  O   . HOH   F 4 .   ? 27.69085 -0.57129  62.24956  1.000 33.34363 ? 427 HOH   A O   1 
HETATM 4173 O  O   . HOH   F 4 .   ? 15.56596 -12.06352 65.33258  1.000 20.97831 ? 428 HOH   A O   1 
HETATM 4174 O  O   . HOH   F 4 .   ? -0.27676 3.86217   60.31730  1.000 33.96871 ? 429 HOH   A O   1 
HETATM 4175 O  O   . HOH   F 4 .   ? 21.55385 9.29043   63.71911  1.000 25.11917 ? 430 HOH   A O   1 
HETATM 4176 O  O   . HOH   F 4 .   ? 7.63682  -12.35479 61.09235  1.000 28.54414 ? 431 HOH   A O   1 
HETATM 4177 O  O   . HOH   F 4 .   ? 22.72769 -8.75156  22.69632  1.000 23.59845 ? 432 HOH   A O   1 
HETATM 4178 O  O   . HOH   F 4 .   ? 31.01293 -16.59483 35.39239  1.000 18.82101 ? 433 HOH   A O   1 
HETATM 4179 O  O   . HOH   F 4 .   ? -1.47552 -1.32967  41.33396  1.000 38.09517 ? 434 HOH   A O   1 
HETATM 4180 O  O   . HOH   F 4 .   ? 7.90747  13.45951  69.34391  1.000 12.46710 ? 435 HOH   A O   1 
HETATM 4181 O  O   . HOH   F 4 .   ? 9.88742  6.31476   35.00691  1.000 12.08992 ? 436 HOH   A O   1 
HETATM 4182 O  O   . HOH   F 4 .   ? 4.78231  -11.48737 49.32694  1.000 22.98667 ? 437 HOH   A O   1 
HETATM 4183 O  O   . HOH   F 4 .   ? -3.89725 6.34799   46.65660  1.000 20.25304 ? 438 HOH   A O   1 
HETATM 4184 O  O   . HOH   F 4 .   ? 8.59794  -15.43462 65.53520  1.000 27.52263 ? 439 HOH   A O   1 
HETATM 4185 O  O   . HOH   F 4 .   ? 6.29207  -13.97675 49.73800  1.000 15.02928 ? 440 HOH   A O   1 
HETATM 4186 O  O   . HOH   F 4 .   ? 33.13471 -4.50188  43.00830  1.000 28.28240 ? 441 HOH   A O   1 
HETATM 4187 O  O   . HOH   F 4 .   ? -0.05914 7.87759   52.94621  1.000 30.03690 ? 442 HOH   A O   1 
HETATM 4188 O  O   . HOH   F 4 .   ? 21.68481 5.89101   22.82158  1.000 33.18624 ? 443 HOH   A O   1 
HETATM 4189 O  O   . HOH   F 4 .   ? 21.23070 3.06901   22.12955  1.000 17.36004 ? 444 HOH   A O   1 
HETATM 4190 O  O   . HOH   F 4 .   ? 26.06007 -4.96486  49.66351  1.000 12.47353 ? 445 HOH   A O   1 
HETATM 4191 O  O   . HOH   F 4 .   ? 34.35131 -1.41327  52.14414  1.000 14.33401 ? 446 HOH   A O   1 
HETATM 4192 O  O   . HOH   F 4 .   ? 23.60029 4.07553   35.22006  1.000 15.78642 ? 447 HOH   A O   1 
HETATM 4193 O  O   . HOH   F 4 .   ? 7.86291  14.40190  41.40205  1.000 37.35173 ? 448 HOH   A O   1 
HETATM 4194 O  O   . HOH   F 4 .   ? 0.57627  3.26324   43.56199  1.000 16.99193 ? 449 HOH   A O   1 
HETATM 4195 O  O   . HOH   F 4 .   ? 16.84330 11.18787  47.78220  1.000 27.02538 ? 450 HOH   A O   1 
HETATM 4196 O  O   . HOH   F 4 .   ? 12.96990 -8.42450  30.80373  1.000 25.59286 ? 451 HOH   A O   1 
HETATM 4197 O  O   . HOH   F 4 .   ? 19.84942 -1.54121  66.67140  1.000 20.84660 ? 452 HOH   A O   1 
HETATM 4198 O  O   . HOH   F 4 .   ? 10.15928 17.04200  59.83412  1.000 27.14996 ? 453 HOH   A O   1 
HETATM 4199 O  O   . HOH   F 4 .   ? 30.48299 0.66142   45.37777  1.000 16.88795 ? 454 HOH   A O   1 
HETATM 4200 O  O   . HOH   F 4 .   ? 4.51873  -1.10510  31.58397  1.000 24.01834 ? 455 HOH   A O   1 
HETATM 4201 O  O   . HOH   F 4 .   ? 4.26097  1.08073   33.58977  1.000 34.35768 ? 456 HOH   A O   1 
HETATM 4202 O  O   . HOH   F 4 .   ? 14.22221 -19.21355 59.58403  1.000 30.26932 ? 457 HOH   A O   1 
HETATM 4203 O  O   . HOH   F 4 .   ? 3.74951  -12.88679 43.20554  1.000 23.32156 ? 458 HOH   A O   1 
HETATM 4204 O  O   . HOH   F 4 .   ? 13.92184 12.89753  45.25131  1.000 31.88645 ? 459 HOH   A O   1 
HETATM 4205 O  O   . HOH   F 4 .   ? 36.65862 -3.72379  48.71990  1.000 21.23340 ? 460 HOH   A O   1 
HETATM 4206 O  O   . HOH   F 4 .   ? 10.99940 -8.65089  30.65724  1.000 30.70791 ? 461 HOH   A O   1 
HETATM 4207 O  O   . HOH   F 4 .   ? 12.71441 10.78132  49.99358  1.000 15.88799 ? 462 HOH   A O   1 
HETATM 4208 O  O   . HOH   F 4 .   ? 2.28412  0.49977   60.31458  1.000 40.62093 ? 463 HOH   A O   1 
HETATM 4209 O  O   . HOH   F 4 .   ? 30.83656 5.48999   48.30939  1.000 15.83405 ? 464 HOH   A O   1 
HETATM 4210 O  O   . HOH   F 4 .   ? 1.12703  3.41145   40.05391  1.000 29.56350 ? 465 HOH   A O   1 
HETATM 4211 O  O   . HOH   F 4 .   ? 9.42787  15.15939  56.18725  1.000 29.62154 ? 466 HOH   A O   1 
HETATM 4212 O  O   . HOH   F 4 .   ? 34.10302 -10.73423 26.98239  1.000 34.14147 ? 467 HOH   A O   1 
HETATM 4213 O  O   . HOH   F 4 .   ? 19.488   5.045     17.811    1.000 30.02875 ? 468 HOH   A O   1 
HETATM 4214 O  O   . HOH   F 4 .   ? 11.62061 10.00741  39.48925  1.000 41.71225 ? 469 HOH   A O   1 
HETATM 4215 O  O   . HOH   F 4 .   ? 32.48242 -16.14381 33.40949  1.000 20.23647 ? 470 HOH   A O   1 
HETATM 4216 O  O   . HOH   F 4 .   ? 5.37280  -8.50111  56.52529  1.000 21.84065 ? 471 HOH   A O   1 
HETATM 4217 O  O   . HOH   F 4 .   ? 4.84354  16.68194  43.32670  1.000 22.40373 ? 472 HOH   A O   1 
HETATM 4218 O  O   . HOH   F 4 .   ? 27.14528 -11.94459 44.28050  1.000 18.73811 ? 473 HOH   A O   1 
HETATM 4219 O  O   . HOH   F 4 .   ? 16.00148 -9.17141  20.85215  1.000 27.68795 ? 474 HOH   A O   1 
HETATM 4220 O  O   . HOH   F 4 .   ? 14.05399 -22.28421 49.33235  1.000 20.77780 ? 475 HOH   A O   1 
HETATM 4221 O  O   . HOH   F 4 .   ? 19.65216 -1.53101  13.88804  1.000 31.02854 ? 476 HOH   A O   1 
HETATM 4222 O  O   . HOH   F 4 .   ? 10.62373 -9.50598  69.53815  1.000 31.91886 ? 477 HOH   A O   1 
HETATM 4223 O  O   . HOH   F 4 .   ? -1.77214 3.62091   44.04667  1.000 18.63083 ? 478 HOH   A O   1 
HETATM 4224 O  O   . HOH   F 4 .   ? 21.56940 7.98394   30.63576  1.000 34.30627 ? 479 HOH   A O   1 
HETATM 4225 O  O   . HOH   F 4 .   ? 8.75100  -15.31527 53.25198  1.000 16.30423 ? 480 HOH   A O   1 
HETATM 4226 O  O   . HOH   F 4 .   ? 20.12550 -5.10368  63.76056  1.000 20.06327 ? 481 HOH   A O   1 
HETATM 4227 O  O   . HOH   F 4 .   ? 9.47149  -3.20491  21.54315  1.000 34.08912 ? 482 HOH   A O   1 
HETATM 4228 O  O   . HOH   F 4 .   ? 4.05106  6.28044   31.69394  1.000 28.00844 ? 483 HOH   A O   1 
HETATM 4229 O  O   . HOH   F 4 .   ? 21.71042 -9.51534  18.89855  1.000 24.65236 ? 484 HOH   A O   1 
HETATM 4230 O  O   . HOH   F 4 .   ? 12.94766 11.86073  25.85368  1.000 32.20715 ? 485 HOH   A O   1 
HETATM 4231 O  O   . HOH   F 4 .   ? 2.83285  15.52439  55.81419  1.000 24.74994 ? 486 HOH   A O   1 
HETATM 4232 O  O   . HOH   F 4 .   ? 30.00962 1.64308   29.43281  1.000 30.79767 ? 487 HOH   A O   1 
HETATM 4233 O  O   . HOH   F 4 .   ? 17.64488 9.13157   46.81650  1.000 50.42825 ? 488 HOH   A O   1 
HETATM 4234 O  O   . HOH   F 4 .   ? 27.88624 -6.45722  35.32150  1.000 13.78988 ? 489 HOH   A O   1 
HETATM 4235 O  O   . HOH   F 4 .   ? 20.99127 18.30427  52.49156  1.000 28.63068 ? 490 HOH   A O   1 
HETATM 4236 O  O   . HOH   F 4 .   ? 16.08246 16.17325  40.48625  1.000 32.30410 ? 491 HOH   A O   1 
HETATM 4237 O  O   . HOH   F 4 .   ? 31.20035 -1.93621  46.14652  1.000 21.54574 ? 492 HOH   A O   1 
HETATM 4238 O  O   . HOH   F 4 .   ? 6.32716  -0.25486  62.30861  1.000 21.54548 ? 493 HOH   A O   1 
HETATM 4239 O  O   . HOH   F 4 .   ? -0.76378 4.30877   52.38349  1.000 17.14902 ? 494 HOH   A O   1 
HETATM 4240 O  O   . HOH   F 4 .   ? 5.70755  3.81781   31.02172  1.000 17.55852 ? 495 HOH   A O   1 
HETATM 4241 O  O   . HOH   F 4 .   ? 30.38573 -0.01142  37.81668  1.000 27.93669 ? 496 HOH   A O   1 
HETATM 4242 O  O   . HOH   F 4 .   ? 20.31305 -16.09972 52.99963  1.000 17.46719 ? 497 HOH   A O   1 
HETATM 4243 O  O   . HOH   F 4 .   ? 7.37262  4.25488   67.92389  1.000 18.82465 ? 498 HOH   A O   1 
HETATM 4244 O  O   . HOH   F 4 .   ? 15.31788 7.87369   46.98164  1.000 25.74020 ? 499 HOH   A O   1 
HETATM 4245 O  O   . HOH   F 4 .   ? 3.83041  -15.68722 65.91105  1.000 38.74733 ? 500 HOH   A O   1 
HETATM 4246 O  O   . HOH   F 4 .   ? 26.05601 -15.97223 43.97754  1.000 37.39488 ? 501 HOH   A O   1 
HETATM 4247 O  O   . HOH   F 4 .   ? 0.137    -6.332    38.236    1.000 36.07569 ? 502 HOH   A O   1 
HETATM 4248 O  O   . HOH   F 4 .   ? 30.95101 -12.22481 51.22015  1.000 24.67887 ? 503 HOH   A O   1 
HETATM 4249 O  O   . HOH   F 4 .   ? 25.32133 3.52464   41.34612  1.000 27.39511 ? 504 HOH   A O   1 
HETATM 4250 O  O   . HOH   F 4 .   ? 19.70481 -1.98055  68.90827  1.000 37.67177 ? 505 HOH   A O   1 
HETATM 4251 O  O   . HOH   F 4 .   ? 22.31262 4.60656   44.33304  1.000 23.56099 ? 506 HOH   A O   1 
HETATM 4252 O  O   . HOH   F 4 .   ? 15.70799 -7.48736  67.08403  1.000 24.60338 ? 507 HOH   A O   1 
HETATM 4253 O  O   . HOH   F 4 .   ? 23.39381 5.12512   28.08888  1.000 16.02758 ? 508 HOH   A O   1 
HETATM 4254 O  O   . HOH   F 4 .   ? 8.78686  16.97063  52.55987  1.000 22.02589 ? 509 HOH   A O   1 
HETATM 4255 O  O   . HOH   F 4 .   ? 2.55404  8.72776   33.77997  1.000 21.43217 ? 510 HOH   A O   1 
HETATM 4256 O  O   . HOH   F 4 .   ? 1.16574  1.47558   55.20738  1.000 32.89583 ? 511 HOH   A O   1 
HETATM 4257 O  O   . HOH   F 4 .   ? 10.01897 9.19984   35.02251  1.000 21.43892 ? 512 HOH   A O   1 
HETATM 4258 O  O   . HOH   F 4 .   ? 25.22553 6.51477   43.89063  1.000 27.11473 ? 513 HOH   A O   1 
HETATM 4259 O  O   . HOH   F 4 .   ? 0.56618  4.13711   55.29401  1.000 31.77752 ? 514 HOH   A O   1 
HETATM 4260 O  O   . HOH   F 4 .   ? 28.84781 -15.37315 46.94825  1.000 42.61763 ? 515 HOH   A O   1 
HETATM 4261 O  O   . HOH   F 4 .   ? 24.06993 2.84232   23.85016  1.000 35.95846 ? 516 HOH   A O   1 
HETATM 4262 O  O   . HOH   F 4 .   ? 15.72662 -18.31683 54.39551  1.000 30.94006 ? 517 HOH   A O   1 
HETATM 4263 O  O   . HOH   F 4 .   ? 32.98163 7.18756   48.56117  1.000 16.32638 ? 518 HOH   A O   1 
HETATM 4264 O  O   . HOH   F 4 .   ? 38.17421 -7.44508  28.40059  1.000 36.13639 ? 519 HOH   A O   1 
HETATM 4265 O  O   . HOH   F 4 .   ? 27.72872 -8.78399  24.36689  1.000 34.25573 ? 520 HOH   A O   1 
HETATM 4266 O  O   . HOH   F 4 .   ? 17.09774 -12.62883 24.91875  1.000 23.63500 ? 521 HOH   A O   1 
HETATM 4267 O  O   . HOH   F 4 .   ? 1.64922  6.12446   53.42025  1.000 20.08719 ? 522 HOH   A O   1 
HETATM 4268 O  O   . HOH   F 4 .   ? 25.87140 -8.37080  19.86914  1.000 27.29265 ? 523 HOH   A O   1 
HETATM 4269 O  O   . HOH   F 4 .   ? 30.78812 0.92619   42.44954  1.000 17.40265 ? 524 HOH   A O   1 
HETATM 4270 O  O   . HOH   F 4 .   ? 0.82736  1.20976   41.84156  1.000 31.30790 ? 525 HOH   A O   1 
HETATM 4271 O  O   . HOH   F 4 .   ? 35.88472 -11.39538 41.41138  1.000 26.76003 ? 526 HOH   A O   1 
HETATM 4272 O  O   . HOH   F 4 .   ? 20.98451 7.19046   66.51821  1.000 32.32232 ? 527 HOH   A O   1 
HETATM 4273 O  O   . HOH   F 4 .   ? 27.10896 1.66354   64.22215  1.000 33.68246 ? 528 HOH   A O   1 
HETATM 4274 O  O   . HOH   F 4 .   ? -2.91268 13.53475  56.51518  1.000 39.47686 ? 529 HOH   A O   1 
HETATM 4275 O  O   . HOH   F 4 .   ? 14.15970 9.97486   32.83095  1.000 22.74977 ? 530 HOH   A O   1 
HETATM 4276 O  O   . HOH   F 4 .   ? 16.63480 17.52661  54.90400  1.000 39.02858 ? 531 HOH   A O   1 
HETATM 4277 O  O   . HOH   F 4 .   ? 8.62722  -10.84275 37.00995  1.000 23.81147 ? 532 HOH   A O   1 
HETATM 4278 O  O   . HOH   F 4 .   ? 10.35941 11.47059  33.46414  1.000 30.56702 ? 533 HOH   A O   1 
HETATM 4279 O  O   . HOH   F 4 .   ? 21.53970 -14.82042 38.74980  1.000 21.69546 ? 534 HOH   A O   1 
HETATM 4280 O  O   . HOH   F 4 .   ? 4.37248  16.21071  36.68570  1.000 35.49854 ? 535 HOH   A O   1 
HETATM 4281 O  O   . HOH   F 4 .   ? 23.95466 0.37389   65.96966  1.000 13.74193 ? 536 HOH   A O   1 
HETATM 4282 O  O   . HOH   F 4 .   ? 29.092   -13.505   57.786    1.000 43.12167 ? 537 HOH   A O   1 
HETATM 4283 O  O   . HOH   F 4 .   ? 29.12086 -24.88305 44.90571  1.000 32.30390 ? 538 HOH   A O   1 
HETATM 4284 O  O   . HOH   F 4 .   ? 33.96041 -14.64561 35.73713  1.000 16.21802 ? 539 HOH   A O   1 
HETATM 4285 O  O   . HOH   F 4 .   ? 8.28469  -5.34707  23.24522  1.000 27.08144 ? 540 HOH   A O   1 
HETATM 4286 O  O   . HOH   F 4 .   ? 5.65036  -8.97283  62.18875  1.000 32.63069 ? 541 HOH   A O   1 
HETATM 4287 O  O   . HOH   F 4 .   ? 28.84222 1.03938   35.64127  1.000 37.05634 ? 542 HOH   A O   1 
HETATM 4288 O  O   . HOH   F 4 .   ? 25.85889 -8.91650  61.86045  1.000 33.97953 ? 543 HOH   A O   1 
HETATM 4289 O  O   . HOH   F 4 .   ? 17.40931 -21.08349 53.54793  1.000 29.99365 ? 544 HOH   A O   1 
HETATM 4290 O  O   . HOH   F 4 .   ? 11.96709 3.01472   23.06626  1.000 23.09274 ? 545 HOH   A O   1 
HETATM 4291 O  O   . HOH   F 4 .   ? 31.45361 -0.30738  33.44492  1.000 32.88671 ? 546 HOH   A O   1 
HETATM 4292 O  O   . HOH   F 4 .   ? 8.74170  -1.81070  70.67130  1.000 39.05643 ? 547 HOH   A O   1 
HETATM 4293 O  O   . HOH   F 4 .   ? 21.46539 3.81706   37.76782  1.000 20.58133 ? 548 HOH   A O   1 
HETATM 4294 O  O   . HOH   F 4 .   ? 37.90428 -13.51573 32.14159  1.000 23.30435 ? 549 HOH   A O   1 
HETATM 4295 O  O   . HOH   F 4 .   ? 5.04121  0.43977   24.41136  1.000 31.80849 ? 550 HOH   A O   1 
HETATM 4296 O  O   . HOH   F 4 .   ? 12.61605 9.47355   43.46990  1.000 37.20152 ? 551 HOH   A O   1 
HETATM 4297 O  O   . HOH   F 4 .   ? 16.59766 10.44488  26.21087  1.000 42.83483 ? 552 HOH   A O   1 
HETATM 4298 O  O   . HOH   F 4 .   ? 11.86709 10.45620  33.43594  1.000 33.00221 ? 553 HOH   A O   1 
HETATM 4299 O  O   . HOH   F 4 .   ? 4.19021  -1.76286  24.73049  1.000 36.72409 ? 554 HOH   A O   1 
HETATM 4300 O  O   . HOH   F 4 .   ? 29.88491 0.90780   33.00252  1.000 42.20025 ? 555 HOH   A O   1 
HETATM 4301 O  O   . HOH   F 4 .   ? 17.98019 17.73562  41.20035  1.000 36.64924 ? 556 HOH   A O   1 
HETATM 4302 O  O   . HOH   F 4 .   ? 0.97959  2.04029   30.72644  1.000 38.98567 ? 557 HOH   A O   1 
HETATM 4303 O  O   . HOH   F 4 .   ? 2.22152  15.25083  64.10243  1.000 30.84951 ? 558 HOH   A O   1 
HETATM 4304 O  O   . HOH   F 4 .   ? 4.89398  -0.61111  60.00101  1.000 36.47204 ? 559 HOH   A O   1 
HETATM 4305 O  O   . HOH   F 4 .   ? 25.32306 -7.86275  56.46972  1.000 19.05902 ? 560 HOH   A O   1 
HETATM 4306 O  O   . HOH   F 4 .   ? 39.01646 -6.72231  31.82405  1.000 29.65609 ? 561 HOH   A O   1 
HETATM 4307 O  O   . HOH   F 4 .   ? 23.95130 -6.65959  58.58699  1.000 34.05854 ? 562 HOH   A O   1 
HETATM 4308 O  O   . HOH   F 4 .   ? 20.69245 -25.65008 51.91648  1.000 33.32472 ? 563 HOH   A O   1 
HETATM 4309 O  O   . HOH   F 4 .   ? 3.37720  12.10074  41.69410  1.000 29.24759 ? 564 HOH   A O   1 
HETATM 4310 O  O   . HOH   F 4 .   ? 1.48575  -9.24317  50.07893  1.000 20.68070 ? 565 HOH   A O   1 
HETATM 4311 O  O   . HOH   F 4 .   ? 35.44750 -4.10457  23.70898  1.000 45.54416 ? 566 HOH   A O   1 
HETATM 4312 O  O   . HOH   F 4 .   ? 5.48377  2.60522   19.69800  1.000 34.14812 ? 567 HOH   A O   1 
HETATM 4313 O  O   . HOH   F 4 .   ? 7.15154  -17.05060 55.08992  1.000 28.46932 ? 568 HOH   A O   1 
HETATM 4314 O  O   . HOH   F 4 .   ? 23.45990 12.90594  49.44729  1.000 31.91361 ? 569 HOH   A O   1 
HETATM 4315 O  O   . HOH   F 4 .   ? 31.56221 0.77732   31.50287  1.000 40.98818 ? 570 HOH   A O   1 
HETATM 4316 O  O   . HOH   F 4 .   ? 25.79938 -7.77883  22.70961  1.000 15.09379 ? 571 HOH   A O   1 
HETATM 4317 O  O   . HOH   F 4 .   ? 6.36958  -4.24464  64.94302  1.000 25.51784 ? 572 HOH   A O   1 
HETATM 4318 O  O   . HOH   F 4 .   ? 18.48358 -18.19025 53.90902  1.000 20.13178 ? 573 HOH   A O   1 
HETATM 4319 O  O   . HOH   F 4 .   ? 34.04622 -8.65497  52.37658  1.000 35.75535 ? 574 HOH   A O   1 
HETATM 4320 O  O   . HOH   F 4 .   ? 1.33857  18.50567  47.18208  1.000 32.46651 ? 575 HOH   A O   1 
HETATM 4321 O  O   . HOH   F 4 .   ? 13.27742 1.05056   17.07948  1.000 33.21599 ? 576 HOH   A O   1 
HETATM 4322 O  O   . HOH   F 4 .   ? 7.68744  14.86014  54.58173  1.000 26.83311 ? 577 HOH   A O   1 
HETATM 4323 O  O   . HOH   F 4 .   ? 31.853   -12.830   57.827    1.000 39.49164 ? 578 HOH   A O   1 
HETATM 4324 O  O   . HOH   F 4 .   ? 6.75705  -13.69115 52.79885  1.000 18.24750 ? 579 HOH   A O   1 
HETATM 4325 O  O   . HOH   F 4 .   ? 28.33773 -7.38374  56.48802  1.000 23.40871 ? 580 HOH   A O   1 
HETATM 4326 O  O   . HOH   F 4 .   ? 14.92674 -6.25903  16.37877  1.000 34.75963 ? 581 HOH   A O   1 
HETATM 4327 O  O   . HOH   F 4 .   ? 21.89963 7.72133   33.69602  1.000 27.88136 ? 582 HOH   A O   1 
HETATM 4328 O  O   . HOH   F 4 .   ? -3.72100 2.79692   45.32621  1.000 30.45753 ? 583 HOH   A O   1 
HETATM 4329 O  O   . HOH   F 4 .   ? -5.18496 12.20667  51.78350  1.000 42.77316 ? 584 HOH   A O   1 
HETATM 4330 O  O   . HOH   F 4 .   ? 18.91238 -3.92495  65.82858  1.000 19.94778 ? 585 HOH   A O   1 
HETATM 4331 O  O   . HOH   F 4 .   ? 17.73175 -5.17288  13.29183  1.000 35.51295 ? 586 HOH   A O   1 
HETATM 4332 O  O   . HOH   F 4 .   ? 29.48606 3.83344   31.76841  1.000 43.16457 ? 587 HOH   A O   1 
HETATM 4333 O  O   . HOH   F 4 .   ? 28.92772 -14.18438 44.61743  1.000 35.11958 ? 588 HOH   A O   1 
HETATM 4334 O  O   . HOH   F 4 .   ? -0.74640 15.16924  55.12800  1.000 39.71643 ? 589 HOH   A O   1 
HETATM 4335 O  O   . HOH   F 4 .   ? 22.46754 9.20487   26.13747  1.000 42.16127 ? 590 HOH   A O   1 
HETATM 4336 O  O   . HOH   F 4 .   ? 34.34637 -16.19653 37.73805  1.000 28.63336 ? 591 HOH   A O   1 
HETATM 4337 O  O   . HOH   F 4 .   ? 26.25843 -17.06872 46.57859  1.000 34.70236 ? 592 HOH   A O   1 
HETATM 4338 O  O   . HOH   F 4 .   ? 2.47937  -12.39208 52.24206  1.000 31.21433 ? 593 HOH   A O   1 
HETATM 4339 O  O   . HOH   F 4 .   ? 37.33451 -9.31829  41.46253  1.000 35.03217 ? 594 HOH   A O   1 
HETATM 4340 O  O   . HOH   F 4 .   ? 10.02873 -9.71472  32.60970  1.000 40.51259 ? 595 HOH   A O   1 
HETATM 4341 O  O   . HOH   F 4 .   ? -6.06656 5.34847   45.74398  1.000 52.00377 ? 596 HOH   A O   1 
HETATM 4342 O  O   . HOH   F 4 .   ? 23.14838 -4.48159  61.28031  1.000 35.04693 ? 597 HOH   A O   1 
HETATM 4343 O  O   . HOH   F 4 .   ? 4.06088  -15.70527 49.38030  1.000 27.62099 ? 598 HOH   A O   1 
HETATM 4344 O  O   . HOH   F 4 .   ? 38.62260 -7.65867  40.16256  1.000 34.08091 ? 599 HOH   A O   1 
HETATM 4345 O  O   . HOH   F 4 .   ? 22.45887 -1.71778  66.21913  1.000 30.04755 ? 600 HOH   A O   1 
HETATM 4346 O  O   . HOH   F 4 .   ? 9.79993  -1.31008  20.85602  1.000 36.08713 ? 601 HOH   A O   1 
HETATM 4347 O  O   . HOH   F 4 .   ? 18.649   -9.719    64.245    1.000 26.97587 ? 602 HOH   A O   1 
HETATM 4348 O  O   . HOH   F 4 .   ? 19.68973 -7.15457  64.88599  1.000 25.06717 ? 603 HOH   A O   1 
HETATM 4349 O  O   . HOH   F 4 .   ? 19.43009 -2.96583  12.13445  1.000 41.60901 ? 604 HOH   A O   1 
HETATM 4350 O  O   . HOH   F 4 .   ? 24.91799 -0.89600  15.03827  1.000 40.25868 ? 605 HOH   A O   1 
HETATM 4351 O  O   . HOH   F 4 .   ? 0.87710  -11.56051 53.67189  1.000 33.98333 ? 606 HOH   A O   1 
HETATM 4352 O  O   . HOH   F 4 .   ? 22.75724 3.51070   41.96224  1.000 21.74000 ? 607 HOH   A O   1 
HETATM 4353 O  O   . HOH   F 4 .   ? 4.42182  -13.18849 53.88122  1.000 28.36893 ? 608 HOH   A O   1 
HETATM 4354 O  O   . HOH   F 4 .   ? -5.38091 10.84136  59.11695  1.000 42.70573 ? 609 HOH   A O   1 
HETATM 4355 O  O   . HOH   F 4 .   ? 32.604   14.246    53.148    1.000 37.56186 ? 610 HOH   A O   1 
HETATM 4356 O  O   . HOH   F 4 .   ? 12.64289 11.10541  46.82359  1.000 33.45547 ? 611 HOH   A O   1 
HETATM 4357 O  O   . HOH   F 4 .   ? 23.38682 7.53412   29.26632  1.000 28.02565 ? 612 HOH   A O   1 
HETATM 4358 O  O   . HOH   F 4 .   ? 22.86615 6.90321   35.64649  1.000 37.48645 ? 613 HOH   A O   1 
HETATM 4359 O  O   . HOH   F 4 .   ? 2.85748  -11.61760 47.69198  1.000 35.61100 ? 614 HOH   A O   1 
HETATM 4360 O  O   . HOH   F 4 .   ? 28.02654 14.49643  50.48662  1.000 53.12577 ? 615 HOH   A O   1 
HETATM 4361 O  O   . HOH   F 4 .   ? 1.89954  5.99266   32.96117  1.000 38.21727 ? 616 HOH   A O   1 
HETATM 4362 O  O   . HOH   F 4 .   ? 30.86563 0.72567   35.45379  1.000 38.61465 ? 617 HOH   A O   1 
HETATM 4363 O  O   . HOH   F 4 .   ? 4.35755  -11.05010 56.39819  1.000 22.31595 ? 618 HOH   A O   1 
HETATM 4364 O  O   . HOH   F 4 .   ? -4.56702 14.16896  57.25353  1.000 39.16147 ? 619 HOH   A O   1 
HETATM 4365 O  O   . HOH   F 4 .   ? 34.36241 -11.96943 43.99067  1.000 34.05208 ? 620 HOH   A O   1 
HETATM 4366 O  O   . HOH   F 4 .   ? -2.84786 14.63375  54.23405  1.000 47.50171 ? 621 HOH   A O   1 
HETATM 4367 O  O   . HOH   F 4 .   ? 8.965    23.174    42.192    1.000 40.68472 ? 622 HOH   A O   1 
HETATM 4368 O  O   . HOH   F 4 .   ? -4.44563 13.18286  59.56034  1.000 41.90020 ? 623 HOH   A O   1 
HETATM 4369 O  O   . HOH   F 4 .   ? 28.20375 3.57410   29.27961  1.000 40.90015 ? 624 HOH   A O   1 
HETATM 4370 O  O   . HOH   F 4 .   ? 3.62980  -12.01578 58.85742  1.000 34.08466 ? 625 HOH   A O   1 
HETATM 4371 O  O   . HOH   F 4 .   ? 28.76535 8.93502   60.76029  1.000 35.86859 ? 626 HOH   A O   1 
HETATM 4372 O  O   . HOH   F 4 .   ? 33.09861 1.48893   44.49467  1.000 35.31601 ? 627 HOH   A O   1 
HETATM 4373 O  O   . HOH   F 4 .   ? 28.94426 10.34549  59.47459  1.000 32.77933 ? 628 HOH   A O   1 
HETATM 4374 O  O   . HOH   F 4 .   ? 22.35762 -4.12578  64.14621  1.000 31.28559 ? 629 HOH   A O   1 
HETATM 4375 O  O   . HOH   F 4 .   ? 22.45802 10.24371  28.04124  1.000 33.54523 ? 630 HOH   A O   1 
HETATM 4376 O  O   . HOH   F 4 .   ? 30.95528 -15.25495 45.38590  1.000 42.73294 ? 631 HOH   A O   1 
HETATM 4377 O  O   . HOH   F 4 .   ? 25.03125 -13.87262 27.11000  1.000 37.70413 ? 632 HOH   A O   1 
HETATM 4378 O  O   . HOH   F 4 .   ? 31.78698 2.84769   33.52825  1.000 37.98361 ? 633 HOH   A O   1 
HETATM 4379 O  O   . HOH   F 4 .   ? 4.56356  2.15950   16.98411  1.000 46.03853 ? 634 HOH   A O   1 
HETATM 4380 O  O   . HOH   F 4 .   ? 6.42533  1.14672   16.29248  1.000 43.98257 ? 635 HOH   A O   1 
HETATM 4381 O  O   . HOH   F 4 .   ? -2.19408 -12.99528 56.26583  1.000 47.02547 ? 636 HOH   A O   1 
HETATM 4382 O  O   . HOH   G 4 .   ? 15.65580 -47.52490 23.87198  1.000 46.26151 ? 401 HOH   B O   1 
HETATM 4383 O  O   . HOH   G 4 .   ? 30.09906 -25.70572 1.39546   1.000 35.38603 ? 402 HOH   B O   1 
HETATM 4384 O  O   . HOH   G 4 .   ? 35.37814 -24.32084 6.13405   1.000 31.47274 ? 403 HOH   B O   1 
HETATM 4385 O  O   . HOH   G 4 .   ? 34.06406 -33.88914 16.87596  1.000 28.29177 ? 404 HOH   B O   1 
HETATM 4386 O  O   . HOH   G 4 .   ? 9.58687  -13.96253 19.74042  1.000 30.78605 ? 405 HOH   B O   1 
HETATM 4387 O  O   . HOH   G 4 .   ? 0.93742  -38.63440 8.15958   1.000 32.55395 ? 406 HOH   B O   1 
HETATM 4388 O  O   . HOH   G 4 .   ? 39.78271 -27.04987 33.50135  1.000 39.17626 ? 407 HOH   B O   1 
HETATM 4389 O  O   . HOH   G 4 .   ? 33.62102 -29.08524 4.72769   1.000 28.80200 ? 408 HOH   B O   1 
HETATM 4390 O  O   . HOH   G 4 .   ? 6.73274  -29.34956 5.37777   1.000 33.00794 ? 409 HOH   B O   1 
HETATM 4391 O  O   . HOH   G 4 .   ? 17.66313 -52.21669 15.68182  1.000 43.17401 ? 410 HOH   B O   1 
HETATM 4392 O  O   . HOH   G 4 .   ? 25.31375 -30.06719 49.02960  1.000 46.60422 ? 411 HOH   B O   1 
HETATM 4393 O  O   . HOH   G 4 .   ? 10.33775 -36.06497 -7.33050  1.000 37.63615 ? 412 HOH   B O   1 
HETATM 4394 O  O   . HOH   G 4 .   ? 33.23289 -29.40660 29.28662  1.000 29.67068 ? 413 HOH   B O   1 
HETATM 4395 O  O   . HOH   G 4 .   ? 1.20249  -23.74686 17.08967  1.000 40.58795 ? 414 HOH   B O   1 
HETATM 4396 O  O   . HOH   G 4 .   ? 0.49270  -41.26030 8.61022   1.000 44.17231 ? 415 HOH   B O   1 
HETATM 4397 O  O   . HOH   G 4 .   ? 18.84899 -43.52313 17.74798  1.000 39.10593 ? 416 HOH   B O   1 
HETATM 4398 O  O   . HOH   G 4 .   ? 39.15484 -24.95732 35.41977  1.000 43.21687 ? 417 HOH   B O   1 
HETATM 4399 O  O   . HOH   G 4 .   ? 25.58616 -31.20798 21.15841  1.000 23.05399 ? 418 HOH   B O   1 
HETATM 4400 O  O   . HOH   G 4 .   ? 2.08935  -41.77211 10.35403  1.000 33.53741 ? 419 HOH   B O   1 
HETATM 4401 O  O   . HOH   G 4 .   ? 3.89964  -24.15261 17.03843  1.000 38.91579 ? 420 HOH   B O   1 
HETATM 4402 O  O   . HOH   G 4 .   ? 11.69472 -31.65827 48.18300  1.000 30.99899 ? 421 HOH   B O   1 
HETATM 4403 O  O   . HOH   G 4 .   ? 9.910    -40.544   -6.359    1.000 18.48997 ? 422 HOH   B O   1 
HETATM 4404 O  O   . HOH   G 4 .   ? 36.72759 -13.26286 29.26469  1.000 28.75103 ? 423 HOH   B O   1 
HETATM 4405 O  O   . HOH   G 4 .   ? 13.60788 -15.42221 -4.38469  1.000 28.61279 ? 424 HOH   B O   1 
HETATM 4406 O  O   . HOH   G 4 .   ? 28.97259 -13.30194 18.94843  1.000 31.37795 ? 425 HOH   B O   1 
HETATM 4407 O  O   . HOH   G 4 .   ? 17.55478 -21.18792 31.76953  1.000 32.51293 ? 426 HOH   B O   1 
HETATM 4408 O  O   . HOH   G 4 .   ? 25.11045 -17.31317 0.78306   1.000 31.41017 ? 427 HOH   B O   1 
HETATM 4409 O  O   . HOH   G 4 .   ? 17.98359 -23.60956 -6.85518  1.000 17.73166 ? 428 HOH   B O   1 
HETATM 4410 O  O   . HOH   G 4 .   ? 3.27668  -41.70586 -1.49840  1.000 40.18209 ? 429 HOH   B O   1 
HETATM 4411 O  O   . HOH   G 4 .   ? 37.31243 -37.81410 6.58255   1.000 36.89504 ? 430 HOH   B O   1 
HETATM 4412 O  O   . HOH   G 4 .   ? 16.84428 -32.82622 39.29498  1.000 21.72905 ? 431 HOH   B O   1 
HETATM 4413 O  O   . HOH   G 4 .   ? 30.96954 -13.27182 13.48781  1.000 30.78208 ? 432 HOH   B O   1 
HETATM 4414 O  O   . HOH   G 4 .   ? 18.61768 -15.82901 23.43674  1.000 21.90347 ? 433 HOH   B O   1 
HETATM 4415 O  O   . HOH   G 4 .   ? 31.39502 -17.75728 18.04396  1.000 24.12963 ? 434 HOH   B O   1 
HETATM 4416 O  O   . HOH   G 4 .   ? 20.891   -46.979   22.418    1.000 34.40109 ? 435 HOH   B O   1 
HETATM 4417 O  O   . HOH   G 4 .   ? 15.05140 -41.68846 -5.32869  1.000 27.83529 ? 436 HOH   B O   1 
HETATM 4418 O  O   . HOH   G 4 .   ? 35.55066 -28.01867 16.19369  1.000 23.69946 ? 437 HOH   B O   1 
HETATM 4419 O  O   . HOH   G 4 .   ? 25.84915 -37.11440 29.06825  1.000 39.49455 ? 438 HOH   B O   1 
HETATM 4420 O  O   . HOH   G 4 .   ? 6.93951  -45.89781 7.29028   1.000 26.32228 ? 439 HOH   B O   1 
HETATM 4421 O  O   . HOH   G 4 .   ? 28.26447 -17.74754 -0.56822  1.000 28.28763 ? 440 HOH   B O   1 
HETATM 4422 O  O   . HOH   G 4 .   ? 15.23864 -20.94612 31.89863  1.000 27.65958 ? 441 HOH   B O   1 
HETATM 4423 O  O   . HOH   G 4 .   ? 4.67653  -38.52707 9.78775   1.000 28.88104 ? 442 HOH   B O   1 
HETATM 4424 O  O   . HOH   G 4 .   ? 43.78038 -25.35891 25.56424  1.000 37.94829 ? 443 HOH   B O   1 
HETATM 4425 O  O   . HOH   G 4 .   ? 24.89139 -2.17340  17.59778  1.000 24.86776 ? 444 HOH   B O   1 
HETATM 4426 O  O   . HOH   G 4 .   ? 9.47893  -20.72374 23.84334  1.000 23.52499 ? 445 HOH   B O   1 
HETATM 4427 O  O   . HOH   G 4 .   ? 5.59004  -33.98511 22.63330  1.000 29.95828 ? 446 HOH   B O   1 
HETATM 4428 O  O   . HOH   G 4 .   ? 43.50645 -19.66320 25.29896  1.000 33.95863 ? 447 HOH   B O   1 
HETATM 4429 O  O   . HOH   G 4 .   ? 20.21267 -5.53157  11.85528  1.000 22.03900 ? 448 HOH   B O   1 
HETATM 4430 O  O   . HOH   G 4 .   ? 7.07866  -43.47784 2.80674   1.000 19.98605 ? 449 HOH   B O   1 
HETATM 4431 O  O   . HOH   G 4 .   ? 13.19819 -47.15132 10.45020  1.000 26.34928 ? 450 HOH   B O   1 
HETATM 4432 O  O   . HOH   G 4 .   ? 25.79331 -37.50025 -3.78337  1.000 24.88819 ? 451 HOH   B O   1 
HETATM 4433 O  O   . HOH   G 4 .   ? 32.55120 -20.78721 3.77961   1.000 38.13149 ? 452 HOH   B O   1 
HETATM 4434 O  O   . HOH   G 4 .   ? 16.92035 -39.70484 18.82221  1.000 26.13059 ? 453 HOH   B O   1 
HETATM 4435 O  O   . HOH   G 4 .   ? 14.62578 -47.50911 3.03341   1.000 31.04441 ? 454 HOH   B O   1 
HETATM 4436 O  O   . HOH   G 4 .   ? 9.13905  -19.18842 12.90119  1.000 18.83961 ? 455 HOH   B O   1 
HETATM 4437 O  O   . HOH   G 4 .   ? 6.83249  -38.29718 -2.12461  1.000 23.05982 ? 456 HOH   B O   1 
HETATM 4438 O  O   . HOH   G 4 .   ? 35.46728 -36.18715 13.71337  1.000 24.54094 ? 457 HOH   B O   1 
HETATM 4439 O  O   . HOH   G 4 .   ? 14.46871 -36.25453 27.42410  1.000 10.26858 ? 458 HOH   B O   1 
HETATM 4440 O  O   . HOH   G 4 .   ? 30.74290 -39.40843 19.62945  1.000 38.59260 ? 459 HOH   B O   1 
HETATM 4441 O  O   . HOH   G 4 .   ? 3.77794  -45.05343 5.17511   1.000 34.48428 ? 460 HOH   B O   1 
HETATM 4442 O  O   . HOH   G 4 .   ? 38.86237 -28.72559 10.02008  1.000 15.49140 ? 461 HOH   B O   1 
HETATM 4443 O  O   . HOH   G 4 .   ? 14.70175 -16.02597 22.74791  1.000 22.19185 ? 462 HOH   B O   1 
HETATM 4444 O  O   . HOH   G 4 .   ? 30.44852 -24.93350 12.48843  1.000 13.18001 ? 463 HOH   B O   1 
HETATM 4445 O  O   . HOH   G 4 .   ? 19.90370 -37.09822 -10.94464 1.000 26.69195 ? 464 HOH   B O   1 
HETATM 4446 O  O   . HOH   G 4 .   ? 16.36714 -39.47853 -3.73316  1.000 18.99385 ? 465 HOH   B O   1 
HETATM 4447 O  O   . HOH   G 4 .   ? 25.58378 -32.97512 40.14710  1.000 21.32694 ? 466 HOH   B O   1 
HETATM 4448 O  O   . HOH   G 4 .   ? 9.73934  -29.32891 2.90926   1.000 20.34880 ? 467 HOH   B O   1 
HETATM 4449 O  O   . HOH   G 4 .   ? 10.92292 -41.08830 36.21250  1.000 31.29595 ? 468 HOH   B O   1 
HETATM 4450 O  O   . HOH   G 4 .   ? 23.66251 -44.76149 14.72647  1.000 40.89367 ? 469 HOH   B O   1 
HETATM 4451 O  O   . HOH   G 4 .   ? 5.12282  -33.78627 18.92993  1.000 17.45759 ? 470 HOH   B O   1 
HETATM 4452 O  O   . HOH   G 4 .   ? 18.82815 -39.68463 29.68238  1.000 28.61247 ? 471 HOH   B O   1 
HETATM 4453 O  O   . HOH   G 4 .   ? 6.59069  -32.05184 28.22777  1.000 35.75271 ? 472 HOH   B O   1 
HETATM 4454 O  O   . HOH   G 4 .   ? 34.90655 -30.22993 16.91981  1.000 21.85760 ? 473 HOH   B O   1 
HETATM 4455 O  O   . HOH   G 4 .   ? 21.69615 -16.90513 37.62411  1.000 32.97321 ? 474 HOH   B O   1 
HETATM 4456 O  O   . HOH   G 4 .   ? 12.83332 -43.94978 -6.65966  1.000 15.52746 ? 475 HOH   B O   1 
HETATM 4457 O  O   . HOH   G 4 .   ? 10.12651 -29.56022 -3.95075  1.000 32.84044 ? 476 HOH   B O   1 
HETATM 4458 O  O   . HOH   G 4 .   ? 24.26129 -25.17026 -1.71280  1.000 14.41656 ? 477 HOH   B O   1 
HETATM 4459 O  O   . HOH   G 4 .   ? 12.58478 -23.92282 38.90319  1.000 24.74571 ? 478 HOH   B O   1 
HETATM 4460 O  O   . HOH   G 4 .   ? 14.65023 -41.54920 30.58783  1.000 30.21606 ? 479 HOH   B O   1 
HETATM 4461 O  O   . HOH   G 4 .   ? 9.29011  -46.57820 18.77712  1.000 29.79654 ? 480 HOH   B O   1 
HETATM 4462 O  O   . HOH   G 4 .   ? 6.83263  -45.52483 -1.60195  1.000 23.46683 ? 481 HOH   B O   1 
HETATM 4463 O  O   . HOH   G 4 .   ? 18.66077 -30.38300 42.30530  1.000 32.30513 ? 482 HOH   B O   1 
HETATM 4464 O  O   . HOH   G 4 .   ? 15.44005 -13.15219 23.01316  1.000 22.60873 ? 483 HOH   B O   1 
HETATM 4465 O  O   . HOH   G 4 .   ? 29.53130 -27.75396 43.99898  1.000 31.94361 ? 484 HOH   B O   1 
HETATM 4466 O  O   . HOH   G 4 .   ? 9.97477  -22.10906 5.60782   1.000 18.87823 ? 485 HOH   B O   1 
HETATM 4467 O  O   . HOH   G 4 .   ? 34.23067 -12.65539 25.72650  1.000 34.19494 ? 486 HOH   B O   1 
HETATM 4468 O  O   . HOH   G 4 .   ? 9.82919  -37.33055 36.41889  1.000 28.47831 ? 487 HOH   B O   1 
HETATM 4469 O  O   . HOH   G 4 .   ? 38.00306 -21.05454 11.74413  1.000 45.35731 ? 488 HOH   B O   1 
HETATM 4470 O  O   . HOH   G 4 .   ? 12.78703 -15.21227 8.44854   1.000 14.18719 ? 489 HOH   B O   1 
HETATM 4471 O  O   . HOH   G 4 .   ? 34.95459 -29.56135 24.35497  1.000 25.99464 ? 490 HOH   B O   1 
HETATM 4472 O  O   . HOH   G 4 .   ? 1.67376  -30.80278 10.60732  1.000 25.33817 ? 491 HOH   B O   1 
HETATM 4473 O  O   . HOH   G 4 .   ? 37.43018 -14.94112 26.14266  1.000 17.35447 ? 492 HOH   B O   1 
HETATM 4474 O  O   . HOH   G 4 .   ? 37.85276 -21.84268 37.11928  1.000 32.32394 ? 493 HOH   B O   1 
HETATM 4475 O  O   . HOH   G 4 .   ? 34.30211 -30.96907 32.62117  1.000 35.97604 ? 494 HOH   B O   1 
HETATM 4476 O  O   . HOH   G 4 .   ? 19.86805 -22.96973 -5.01990  1.000 22.27784 ? 495 HOH   B O   1 
HETATM 4477 O  O   . HOH   G 4 .   ? 27.81160 -33.72904 27.18544  1.000 17.91607 ? 496 HOH   B O   1 
HETATM 4478 O  O   . HOH   G 4 .   ? 17.377   -7.836    12.593    1.000 20.77189 ? 497 HOH   B O   1 
HETATM 4479 O  O   . HOH   G 4 .   ? 10.22707 -16.95434 11.95084  1.000 15.90913 ? 498 HOH   B O   1 
HETATM 4480 O  O   . HOH   G 4 .   ? 26.12675 -29.63704 -7.96164  1.000 36.99390 ? 499 HOH   B O   1 
HETATM 4481 O  O   . HOH   G 4 .   ? 10.43901 -34.19741 31.56157  1.000 22.15427 ? 500 HOH   B O   1 
HETATM 4482 O  O   . HOH   G 4 .   ? 30.15680 -33.42522 20.90874  1.000 23.86811 ? 501 HOH   B O   1 
HETATM 4483 O  O   . HOH   G 4 .   ? 24.24034 -14.04854 9.15551   1.000 14.84413 ? 502 HOH   B O   1 
HETATM 4484 O  O   . HOH   G 4 .   ? 17.33217 -41.29575 12.53109  1.000 14.61827 ? 503 HOH   B O   1 
HETATM 4485 O  O   . HOH   G 4 .   ? 7.27968  -40.17533 29.43225  1.000 46.18457 ? 504 HOH   B O   1 
HETATM 4486 O  O   . HOH   G 4 .   ? 19.92560 -38.23663 15.31882  1.000 21.79290 ? 505 HOH   B O   1 
HETATM 4487 O  O   . HOH   G 4 .   ? 2.45535  -34.04053 18.48621  1.000 21.31978 ? 506 HOH   B O   1 
HETATM 4488 O  O   . HOH   G 4 .   ? 37.32937 -37.51887 14.02166  1.000 35.03807 ? 507 HOH   B O   1 
HETATM 4489 O  O   . HOH   G 4 .   ? 24.32386 -33.54641 21.99411  1.000 42.48014 ? 508 HOH   B O   1 
HETATM 4490 O  O   . HOH   G 4 .   ? 0.35918  -43.84644 10.96021  1.000 38.74680 ? 509 HOH   B O   1 
HETATM 4491 O  O   . HOH   G 4 .   ? 28.69319 -32.91097 38.36212  1.000 28.40937 ? 510 HOH   B O   1 
HETATM 4492 O  O   . HOH   G 4 .   ? 24.12302 -28.75024 -4.25268  1.000 17.97380 ? 511 HOH   B O   1 
HETATM 4493 O  O   . HOH   G 4 .   ? 36.60368 -18.26961 4.67938   1.000 36.12761 ? 512 HOH   B O   1 
HETATM 4494 O  O   . HOH   G 4 .   ? 27.74211 -34.67131 34.54261  1.000 24.18671 ? 513 HOH   B O   1 
HETATM 4495 O  O   . HOH   G 4 .   ? 14.35232 -39.00412 27.65477  1.000 21.97826 ? 514 HOH   B O   1 
HETATM 4496 O  O   . HOH   G 4 .   ? 18.853   -47.202   3.616     1.000 16.80710 ? 515 HOH   B O   1 
HETATM 4497 O  O   . HOH   G 4 .   ? 8.92964  -14.34014 -4.96623  1.000 31.99628 ? 516 HOH   B O   1 
HETATM 4498 O  O   . HOH   G 4 .   ? 22.28779 -38.34848 -3.83967  1.000 28.47896 ? 517 HOH   B O   1 
HETATM 4499 O  O   . HOH   G 4 .   ? 28.55701 -22.44914 -0.36212  1.000 34.51158 ? 518 HOH   B O   1 
HETATM 4500 O  O   . HOH   G 4 .   ? 32.97267 -14.62991 6.47354   1.000 27.97266 ? 519 HOH   B O   1 
HETATM 4501 O  O   . HOH   G 4 .   ? 8.01905  -42.18344 21.30971  1.000 27.42145 ? 520 HOH   B O   1 
HETATM 4502 O  O   . HOH   G 4 .   ? 14.37969 -41.02954 38.41850  1.000 33.32514 ? 521 HOH   B O   1 
HETATM 4503 O  O   . HOH   G 4 .   ? 2.24187  -26.81392 13.43667  1.000 19.77327 ? 522 HOH   B O   1 
HETATM 4504 O  O   . HOH   G 4 .   ? 10.74179 -36.73435 41.73661  1.000 29.29356 ? 523 HOH   B O   1 
HETATM 4505 O  O   . HOH   G 4 .   ? 16.01297 -47.19158 9.37109   1.000 28.84349 ? 524 HOH   B O   1 
HETATM 4506 O  O   . HOH   G 4 .   ? 7.33587  -40.48601 -8.92416  1.000 22.06947 ? 525 HOH   B O   1 
HETATM 4507 O  O   . HOH   G 4 .   ? 26.23086 -37.46473 -6.33632  1.000 29.59304 ? 526 HOH   B O   1 
HETATM 4508 O  O   . HOH   G 4 .   ? 8.41970  -28.53444 37.49820  1.000 22.20615 ? 527 HOH   B O   1 
HETATM 4509 O  O   . HOH   G 4 .   ? 19.13361 -37.95147 18.35205  1.000 35.57304 ? 528 HOH   B O   1 
HETATM 4510 O  O   . HOH   G 4 .   ? 10.22633 -6.24337  16.87211  1.000 37.66954 ? 529 HOH   B O   1 
HETATM 4511 O  O   . HOH   G 4 .   ? 23.30402 -39.31169 33.40121  1.000 35.37931 ? 530 HOH   B O   1 
HETATM 4512 O  O   . HOH   G 4 .   ? 15.332   -39.435   40.458    1.000 46.41624 ? 531 HOH   B O   1 
HETATM 4513 O  O   . HOH   G 4 .   ? 22.60682 -35.07489 21.23360  1.000 36.44827 ? 532 HOH   B O   1 
HETATM 4514 O  O   . HOH   G 4 .   ? 7.61729  -17.63928 19.02985  1.000 25.38071 ? 533 HOH   B O   1 
HETATM 4515 O  O   . HOH   G 4 .   ? 15.30985 -19.28830 27.34460  1.000 32.27818 ? 534 HOH   B O   1 
HETATM 4516 O  O   . HOH   G 4 .   ? 15.96743 -6.23073  18.69642  1.000 26.47524 ? 535 HOH   B O   1 
HETATM 4517 O  O   . HOH   G 4 .   ? 26.45588 -16.67674 33.89268  1.000 26.71137 ? 536 HOH   B O   1 
HETATM 4518 O  O   . HOH   G 4 .   ? 21.66802 -41.35141 14.69030  1.000 24.82226 ? 537 HOH   B O   1 
HETATM 4519 O  O   . HOH   G 4 .   ? 3.57709  -34.66099 9.86643   1.000 27.58988 ? 538 HOH   B O   1 
HETATM 4520 O  O   . HOH   G 4 .   ? 30.45620 -21.92455 39.64837  1.000 23.33661 ? 539 HOH   B O   1 
HETATM 4521 O  O   . HOH   G 4 .   ? 39.54761 -18.34652 32.34785  1.000 31.35891 ? 540 HOH   B O   1 
HETATM 4522 O  O   . HOH   G 4 .   ? 29.08339 -38.27156 -2.44540  1.000 27.92697 ? 541 HOH   B O   1 
HETATM 4523 O  O   . HOH   G 4 .   ? 32.21860 -23.28190 26.81623  1.000 11.07012 ? 542 HOH   B O   1 
HETATM 4524 O  O   . HOH   G 4 .   ? 34.67927 -14.48213 9.38585   1.000 36.37665 ? 543 HOH   B O   1 
HETATM 4525 O  O   . HOH   G 4 .   ? 30.44143 -34.73562 23.83503  1.000 26.30121 ? 544 HOH   B O   1 
HETATM 4526 O  O   . HOH   G 4 .   ? 6.75979  -31.73804 23.61930  1.000 32.42175 ? 545 HOH   B O   1 
HETATM 4527 O  O   . HOH   G 4 .   ? 17.94069 -11.92148 3.03630   1.000 32.38598 ? 546 HOH   B O   1 
HETATM 4528 O  O   . HOH   G 4 .   ? 5.11851  -31.16287 20.43119  1.000 26.25791 ? 547 HOH   B O   1 
HETATM 4529 O  O   . HOH   G 4 .   ? 26.70155 -6.11487  5.31931   1.000 18.87065 ? 548 HOH   B O   1 
HETATM 4530 O  O   . HOH   G 4 .   ? 29.08389 -37.03755 -4.89846  1.000 37.38800 ? 549 HOH   B O   1 
HETATM 4531 O  O   . HOH   G 4 .   ? 32.72752 -15.58909 17.85386  1.000 35.50614 ? 550 HOH   B O   1 
HETATM 4532 O  O   . HOH   G 4 .   ? 35.27760 -18.15399 10.72908  1.000 15.66393 ? 551 HOH   B O   1 
HETATM 4533 O  O   . HOH   G 4 .   ? 28.21440 -23.15073 3.69285   1.000 26.14306 ? 552 HOH   B O   1 
HETATM 4534 O  O   . HOH   G 4 .   ? 21.57814 -14.70084 24.24975  1.000 25.68740 ? 553 HOH   B O   1 
HETATM 4535 O  O   . HOH   G 4 .   ? 4.52280  -28.42380 23.69905  1.000 27.76196 ? 554 HOH   B O   1 
HETATM 4536 O  O   . HOH   G 4 .   ? 21.253   -47.903   7.319     1.000 27.44945 ? 555 HOH   B O   1 
HETATM 4537 O  O   . HOH   G 4 .   ? 10.58846 -30.54746 0.40906   1.000 19.60951 ? 556 HOH   B O   1 
HETATM 4538 O  O   . HOH   G 4 .   ? 5.51010  -23.40267 20.12585  1.000 26.74389 ? 557 HOH   B O   1 
HETATM 4539 O  O   . HOH   G 4 .   ? 9.89308  -30.84619 38.17835  1.000 28.72199 ? 558 HOH   B O   1 
HETATM 4540 O  O   . HOH   G 4 .   ? 33.471   -18.679   2.906     1.000 38.01691 ? 559 HOH   B O   1 
HETATM 4541 O  O   . HOH   G 4 .   ? 39.44669 -25.19646 22.10597  1.000 29.46328 ? 560 HOH   B O   1 
HETATM 4542 O  O   . HOH   G 4 .   ? 19.383   -45.327   23.930    1.000 46.55145 ? 561 HOH   B O   1 
HETATM 4543 O  O   . HOH   G 4 .   ? 13.97954 -22.15008 28.41663  1.000 31.93552 ? 562 HOH   B O   1 
HETATM 4544 O  O   . HOH   G 4 .   ? 41.42203 -14.93066 29.83367  1.000 45.06808 ? 563 HOH   B O   1 
HETATM 4545 O  O   . HOH   G 4 .   ? 22.06425 -39.59173 15.45261  1.000 32.17272 ? 564 HOH   B O   1 
HETATM 4546 O  O   . HOH   G 4 .   ? 24.86074 -41.02881 16.32594  1.000 30.05041 ? 565 HOH   B O   1 
HETATM 4547 O  O   . HOH   G 4 .   ? 36.60656 -22.42279 17.79358  1.000 33.99741 ? 566 HOH   B O   1 
HETATM 4548 O  O   . HOH   G 4 .   ? 22.67675 -11.13851 20.80146  1.000 29.97325 ? 567 HOH   B O   1 
HETATM 4549 O  O   . HOH   G 4 .   ? 29.80888 -22.65934 5.94026   1.000 20.56048 ? 568 HOH   B O   1 
HETATM 4550 O  O   . HOH   G 4 .   ? 7.60611  -34.12623 -3.34309  1.000 34.13661 ? 569 HOH   B O   1 
HETATM 4551 O  O   . HOH   G 4 .   ? 24.34346 -27.76155 48.32154  1.000 36.75988 ? 570 HOH   B O   1 
HETATM 4552 O  O   . HOH   G 4 .   ? 32.73238 -22.53467 6.01335   1.000 32.98652 ? 571 HOH   B O   1 
HETATM 4553 O  O   . HOH   G 4 .   ? 24.67866 -15.08473 23.55790  1.000 22.54142 ? 572 HOH   B O   1 
HETATM 4554 O  O   . HOH   G 4 .   ? 8.64256  -31.46447 28.79670  1.000 32.28165 ? 573 HOH   B O   1 
HETATM 4555 O  O   . HOH   G 4 .   ? 28.32909 -30.82263 -3.60671  1.000 17.74875 ? 574 HOH   B O   1 
HETATM 4556 O  O   . HOH   G 4 .   ? 13.13681 -23.57033 26.91345  1.000 26.20324 ? 575 HOH   B O   1 
HETATM 4557 O  O   . HOH   G 4 .   ? 8.11199  -9.13123  19.25648  1.000 36.44916 ? 576 HOH   B O   1 
HETATM 4558 O  O   . HOH   G 4 .   ? 5.80193  -21.31252 11.91889  1.000 22.55397 ? 577 HOH   B O   1 
HETATM 4559 O  O   . HOH   G 4 .   ? 13.76515 -26.73310 41.12811  1.000 31.64154 ? 578 HOH   B O   1 
HETATM 4560 O  O   . HOH   G 4 .   ? 15.97971 -39.92673 28.68126  1.000 45.08384 ? 579 HOH   B O   1 
HETATM 4561 O  O   . HOH   G 4 .   ? 14.35656 -7.57089  14.10866  1.000 22.53849 ? 580 HOH   B O   1 
HETATM 4562 O  O   . HOH   G 4 .   ? 15.90201 -21.63027 -7.39486  1.000 34.45098 ? 581 HOH   B O   1 
HETATM 4563 O  O   . HOH   G 4 .   ? 31.85157 -20.44511 37.82910  1.000 29.22792 ? 582 HOH   B O   1 
HETATM 4564 O  O   . HOH   G 4 .   ? 2.92755  -45.21368 2.60432   1.000 42.75100 ? 583 HOH   B O   1 
HETATM 4565 O  O   . HOH   G 4 .   ? 33.86308 -15.78307 4.95779   1.000 33.86545 ? 584 HOH   B O   1 
HETATM 4566 O  O   . HOH   G 4 .   ? 7.69539  -36.53112 30.13206  1.000 29.43609 ? 585 HOH   B O   1 
HETATM 4567 O  O   . HOH   G 4 .   ? 42.27604 -24.27136 24.13366  1.000 35.28433 ? 586 HOH   B O   1 
HETATM 4568 O  O   . HOH   G 4 .   ? 35.33937 -30.72543 19.89856  1.000 23.21924 ? 587 HOH   B O   1 
HETATM 4569 O  O   . HOH   G 4 .   ? 19.83430 -4.25058  14.09718  1.000 29.71272 ? 588 HOH   B O   1 
HETATM 4570 O  O   . HOH   G 4 .   ? 26.40378 -39.60046 -1.52334  1.000 26.55411 ? 589 HOH   B O   1 
HETATM 4571 O  O   . HOH   G 4 .   ? 35.60383 -29.55729 28.85456  1.000 33.14367 ? 590 HOH   B O   1 
HETATM 4572 O  O   . HOH   G 4 .   ? 5.99292  -36.42360 9.28002   1.000 13.62316 ? 591 HOH   B O   1 
HETATM 4573 O  O   . HOH   G 4 .   ? 40.11241 -18.74640 20.80480  1.000 31.20654 ? 592 HOH   B O   1 
HETATM 4574 O  O   . HOH   G 4 .   ? 26.36607 -33.99392 24.80044  1.000 32.56336 ? 593 HOH   B O   1 
HETATM 4575 O  O   . HOH   G 4 .   ? 9.48073  -33.80203 37.29548  1.000 36.30037 ? 594 HOH   B O   1 
HETATM 4576 O  O   . HOH   G 4 .   ? 2.93084  -40.84378 -3.97724  1.000 39.91039 ? 595 HOH   B O   1 
HETATM 4577 O  O   . HOH   G 4 .   ? 38.51032 -17.64547 35.20005  1.000 40.19497 ? 596 HOH   B O   1 
HETATM 4578 O  O   . HOH   G 4 .   ? 29.24964 -12.33461 15.55340  1.000 28.54071 ? 597 HOH   B O   1 
HETATM 4579 O  O   . HOH   G 4 .   ? 38.66332 -21.48164 9.66657   1.000 31.70778 ? 598 HOH   B O   1 
HETATM 4580 O  O   . HOH   G 4 .   ? 10.64596 -26.62832 -2.62126  1.000 26.76031 ? 599 HOH   B O   1 
HETATM 4581 O  O   . HOH   G 4 .   ? 26.38909 -34.69713 18.18039  1.000 21.21509 ? 600 HOH   B O   1 
HETATM 4582 O  O   . HOH   G 4 .   ? 26.24685 -37.72399 31.16030  1.000 31.49140 ? 601 HOH   B O   1 
HETATM 4583 O  O   . HOH   G 4 .   ? 11.61795 -43.52027 33.63318  1.000 30.16959 ? 602 HOH   B O   1 
HETATM 4584 O  O   . HOH   G 4 .   ? 12.24061 -45.50278 8.18569   1.000 22.74153 ? 603 HOH   B O   1 
HETATM 4585 O  O   . HOH   G 4 .   ? 30.18341 -22.89025 3.23833   1.000 38.11099 ? 604 HOH   B O   1 
HETATM 4586 O  O   . HOH   G 4 .   ? 0.83107  -32.84285 16.89314  1.000 31.57703 ? 605 HOH   B O   1 
HETATM 4587 O  O   . HOH   G 4 .   ? 37.498   -42.768   10.841    1.000 43.42058 ? 606 HOH   B O   1 
HETATM 4588 O  O   . HOH   G 4 .   ? 35.23854 -15.70157 18.83114  1.000 38.93445 ? 607 HOH   B O   1 
HETATM 4589 O  O   . HOH   G 4 .   ? 10.72595 -26.89234 -5.16395  1.000 34.40229 ? 608 HOH   B O   1 
HETATM 4590 O  O   . HOH   G 4 .   ? 19.01424 -40.45573 19.70793  1.000 39.89706 ? 609 HOH   B O   1 
HETATM 4591 O  O   . HOH   G 4 .   ? 34.30031 -30.47677 26.71377  1.000 36.51937 ? 610 HOH   B O   1 
HETATM 4592 O  O   . HOH   G 4 .   ? 9.81929  -21.71974 -0.45231  1.000 31.38132 ? 611 HOH   B O   1 
HETATM 4593 O  O   . HOH   G 4 .   ? 11.98490 -47.17601 6.31459   1.000 34.22832 ? 612 HOH   B O   1 
HETATM 4594 O  O   . HOH   G 4 .   ? 18.10844 -11.17251 5.27088   1.000 30.24963 ? 613 HOH   B O   1 
HETATM 4595 O  O   . HOH   G 4 .   ? 8.54306  -35.01655 35.45875  1.000 45.43605 ? 614 HOH   B O   1 
HETATM 4596 O  O   . HOH   G 4 .   ? 34.02399 -33.43782 20.92185  1.000 35.53081 ? 615 HOH   B O   1 
HETATM 4597 O  O   . HOH   G 4 .   ? 12.32542 -19.33294 24.96349  1.000 31.81598 ? 616 HOH   B O   1 
HETATM 4598 O  O   . HOH   G 4 .   ? 9.05258  -20.54828 0.80272   1.000 36.31063 ? 617 HOH   B O   1 
HETATM 4599 O  O   . HOH   G 4 .   ? 10.75830 -17.04628 9.38638   1.000 15.53402 ? 618 HOH   B O   1 
HETATM 4600 O  O   . HOH   G 4 .   ? 8.37185  -14.72067 12.43476  1.000 23.95204 ? 619 HOH   B O   1 
HETATM 4601 O  O   . HOH   G 4 .   ? 16.357   -48.266   4.678     1.000 42.97444 ? 620 HOH   B O   1 
HETATM 4602 O  O   . HOH   G 4 .   ? 2.861    -24.610   21.460    1.000 35.60572 ? 621 HOH   B O   1 
HETATM 4603 O  O   . HOH   G 4 .   ? 5.69423  -20.68625 5.62122   1.000 32.07010 ? 622 HOH   B O   1 
HETATM 4604 O  O   . HOH   G 4 .   ? 0.364    -38.988   6.011     1.000 28.21744 ? 623 HOH   B O   1 
HETATM 4605 O  O   . HOH   G 4 .   ? 35.19213 -36.11753 20.65733  1.000 39.11022 ? 624 HOH   B O   1 
HETATM 4606 O  O   . HOH   G 4 .   ? 27.60809 -25.77756 3.00267   1.000 27.55715 ? 625 HOH   B O   1 
HETATM 4607 O  O   . HOH   G 4 .   ? 24.55719 -16.12102 35.17386  1.000 32.33174 ? 626 HOH   B O   1 
HETATM 4608 O  O   . HOH   G 4 .   ? 6.81989  -18.34748 9.93095   1.000 29.70103 ? 627 HOH   B O   1 
HETATM 4609 O  O   . HOH   G 4 .   ? 12.03366 -52.32102 19.00873  1.000 36.44553 ? 628 HOH   B O   1 
HETATM 4610 O  O   . HOH   G 4 .   ? 37.02246 -41.48475 8.33337   1.000 27.05003 ? 629 HOH   B O   1 
HETATM 4611 O  O   . HOH   G 4 .   ? 33.35963 -25.16936 5.18874   1.000 31.94495 ? 630 HOH   B O   1 
HETATM 4612 O  O   . HOH   G 4 .   ? 8.18552  -32.20790 30.74113  1.000 30.78071 ? 631 HOH   B O   1 
HETATM 4613 O  O   . HOH   G 4 .   ? 33.20190 -33.88719 22.95211  1.000 35.82782 ? 632 HOH   B O   1 
HETATM 4614 O  O   . HOH   G 4 .   ? 40.71723 -23.52421 35.29912  1.000 48.05242 ? 633 HOH   B O   1 
HETATM 4615 O  O   . HOH   G 4 .   ? -0.364   -38.768   3.942     1.000 46.04676 ? 634 HOH   B O   1 
HETATM 4616 O  O   . HOH   G 4 .   ? 10.52070 -23.34410 26.76561  1.000 31.79121 ? 635 HOH   B O   1 
HETATM 4617 O  O   . HOH   G 4 .   ? 40.23876 -15.30738 32.37175  1.000 38.75691 ? 636 HOH   B O   1 
HETATM 4618 O  O   . HOH   G 4 .   ? 43.72542 -21.85875 24.55603  1.000 40.92380 ? 637 HOH   B O   1 
HETATM 4619 O  O   . HOH   G 4 .   ? 23.21024 -26.65108 -3.76791  1.000 15.71899 ? 638 HOH   B O   1 
HETATM 4620 O  O   . HOH   G 4 .   ? 3.47244  -32.72492 7.71945   1.000 34.55325 ? 639 HOH   B O   1 
HETATM 4621 O  O   . HOH   G 4 .   ? 6.73741  -32.77025 4.84506   1.000 34.39743 ? 640 HOH   B O   1 
HETATM 4622 O  O   . HOH   G 4 .   ? 27.96649 -25.84387 0.83405   1.000 31.45826 ? 641 HOH   B O   1 
HETATM 4623 O  O   . HOH   G 4 .   ? 32.26429 -21.93763 2.26561   1.000 35.46067 ? 642 HOH   B O   1 
HETATM 4624 O  O   . HOH   G 4 .   ? 8.08600  -45.78446 1.57012   1.000 33.95574 ? 643 HOH   B O   1 
HETATM 4625 O  O   . HOH   G 4 .   ? 0.26070  -46.53579 11.48228  1.000 38.25021 ? 644 HOH   B O   1 
HETATM 4626 O  O   . HOH   G 4 .   ? 30.81455 -21.50051 0.21426   1.000 43.13736 ? 645 HOH   B O   1 
HETATM 4627 O  O   . HOH   G 4 .   ? 9.70898  -29.17007 -1.79816  1.000 26.72387 ? 646 HOH   B O   1 
HETATM 4628 O  O   . HOH   G 4 .   ? 36.28273 -39.14099 4.20182   1.000 31.59308 ? 647 HOH   B O   1 
HETATM 4629 O  O   . HOH   G 4 .   ? 39.526   -27.303   3.669     1.000 47.42685 ? 648 HOH   B O   1 
HETATM 4630 O  O   . HOH   G 4 .   ? 7.14422  -15.57194 20.19023  1.000 43.40545 ? 649 HOH   B O   1 
HETATM 4631 O  O   . HOH   G 4 .   ? 36.26435 -32.07806 30.96037  1.000 43.00155 ? 650 HOH   B O   1 
HETATM 4632 O  O   . HOH   G 4 .   ? 8.81458  -17.95842 7.78684   1.000 24.17062 ? 651 HOH   B O   1 
HETATM 4633 O  O   . HOH   G 4 .   ? 39.82917 -22.91621 37.34621  1.000 44.31628 ? 652 HOH   B O   1 
HETATM 4634 O  O   . HOH   G 4 .   ? -1.011   -40.334   6.880     1.000 28.56969 ? 653 HOH   B O   1 
HETATM 4635 O  O   . HOH   G 4 .   ? 38.74842 -13.95043 21.63730  1.000 30.25973 ? 654 HOH   B O   1 
HETATM 4636 O  O   . HOH   G 4 .   ? 27.17930 -33.41420 20.62658  1.000 21.55041 ? 655 HOH   B O   1 
HETATM 4637 O  O   . HOH   G 4 .   ? 12.86863 -14.36881 -1.73547  1.000 36.13775 ? 656 HOH   B O   1 
HETATM 4638 O  O   . HOH   G 4 .   ? 26.85728 -28.72191 -4.00865  1.000 27.48751 ? 657 HOH   B O   1 
HETATM 4639 O  O   . HOH   G 4 .   ? 41.89957 -18.34131 33.52676  1.000 50.47545 ? 658 HOH   B O   1 
HETATM 4640 O  O   . HOH   G 4 .   ? 37.96523 -12.91780 24.53640  1.000 31.64125 ? 659 HOH   B O   1 
HETATM 4641 O  O   . HOH   G 4 .   ? 8.67241  -19.79253 5.86221   1.000 30.44841 ? 660 HOH   B O   1 
HETATM 4642 O  O   . HOH   G 4 .   ? 1.284    -42.890   0.443     1.000 37.78281 ? 661 HOH   B O   1 
HETATM 4643 O  O   . HOH   G 4 .   ? 18.415   -49.239   5.029     1.000 25.72958 ? 662 HOH   B O   1 
HETATM 4644 O  O   . HOH   G 4 .   ? 22.34175 -24.61842 -5.42682  1.000 22.20594 ? 663 HOH   B O   1 
HETATM 4645 O  O   . HOH   G 4 .   ? 13.53625 -20.61276 27.14328  1.000 31.48424 ? 664 HOH   B O   1 
HETATM 4646 O  O   . HOH   G 4 .   ? 34.27029 -39.49495 3.77812   1.000 28.97697 ? 665 HOH   B O   1 
HETATM 4647 O  O   . HOH   G 4 .   ? 13.22565 -49.76851 9.68658   1.000 45.31398 ? 666 HOH   B O   1 
HETATM 4648 O  O   . HOH   G 4 .   ? 8.07344  -32.78500 -4.77066  1.000 38.19811 ? 667 HOH   B O   1 
HETATM 4649 O  O   . HOH   G 4 .   ? 7.84317  -45.08579 20.52353  1.000 34.09435 ? 668 HOH   B O   1 
HETATM 4650 O  O   . HOH   G 4 .   ? 36.08588 -33.63547 21.87658  1.000 41.39815 ? 669 HOH   B O   1 
HETATM 4651 O  O   . HOH   G 4 .   ? 19.05998 -40.62219 14.71140  1.000 26.30308 ? 670 HOH   B O   1 
HETATM 4652 O  O   . HOH   G 4 .   ? 43.01336 -18.92464 20.10209  1.000 36.04669 ? 671 HOH   B O   1 
HETATM 4653 O  O   . HOH   G 4 .   ? 23.65457 -36.64750 24.80663  1.000 37.16989 ? 672 HOH   B O   1 
HETATM 4654 O  O   . HOH   G 4 .   ? 21.04930 -37.08482 24.52125  1.000 33.53409 ? 673 HOH   B O   1 
HETATM 4655 O  O   . HOH   G 4 .   ? 18.80264 -14.82398 25.84760  1.000 24.19975 ? 674 HOH   B O   1 
HETATM 4656 O  O   . HOH   G 4 .   ? 37.51562 -30.07912 29.66207  1.000 43.31256 ? 675 HOH   B O   1 
HETATM 4657 O  O   . HOH   G 4 .   ? 4.17060  -44.15926 -2.11155  1.000 32.96288 ? 676 HOH   B O   1 
HETATM 4658 O  O   . HOH   G 4 .   ? 8.36311  -18.75581 3.32040   1.000 30.84125 ? 677 HOH   B O   1 
HETATM 4659 O  O   . HOH   G 4 .   ? 6.76033  -38.83155 31.25005  1.000 39.23458 ? 678 HOH   B O   1 
HETATM 4660 O  O   . HOH   G 4 .   ? 4.95315  -35.02723 7.09307   1.000 30.92146 ? 679 HOH   B O   1 
HETATM 4661 O  O   . HOH   G 4 .   ? 6.60122  -46.67544 2.91655   1.000 35.79303 ? 680 HOH   B O   1 
HETATM 4662 O  O   . HOH   G 4 .   ? 28.16352 -37.41025 33.19954  1.000 31.50917 ? 681 HOH   B O   1 
HETATM 4663 O  O   . HOH   G 4 .   ? 41.995   -30.124   7.067     1.000 39.58014 ? 682 HOH   B O   1 
HETATM 4664 O  O   . HOH   G 4 .   ? 4.61499  -21.34689 18.64536  1.000 36.59564 ? 683 HOH   B O   1 
HETATM 4665 O  O   . HOH   G 4 .   ? 37.837   -31.467   17.890    1.000 32.70937 ? 684 HOH   B O   1 
HETATM 4666 O  O   . HOH   G 4 .   ? 14.08973 -43.39340 33.91850  1.000 42.74010 ? 685 HOH   B O   1 
HETATM 4667 O  O   . HOH   G 4 .   ? 24.26526 -22.88528 -3.13796  1.000 35.24195 ? 686 HOH   B O   1 
HETATM 4668 O  O   . HOH   G 4 .   ? 19.436   -49.545   7.483     1.000 33.63686 ? 687 HOH   B O   1 
HETATM 4669 O  O   . HOH   G 4 .   ? 9.18396  -22.85492 28.56477  1.000 37.89265 ? 688 HOH   B O   1 
HETATM 4670 O  O   . HOH   G 4 .   ? 32.52585 -18.12528 37.31478  1.000 30.22571 ? 689 HOH   B O   1 
HETATM 4671 O  O   . HOH   G 4 .   ? 5.70522  -32.53962 7.06688   1.000 41.94061 ? 690 HOH   B O   1 
HETATM 4672 O  O   . HOH   G 4 .   ? 31.97391 -39.18474 -1.69397  1.000 35.52598 ? 691 HOH   B O   1 
HETATM 4673 O  O   . HOH   G 4 .   ? 9.77146  -32.44359 42.96959  1.000 40.93624 ? 692 HOH   B O   1 
HETATM 4674 O  O   . HOH   G 4 .   ? 5.48794  -35.90436 28.60083  1.000 35.72343 ? 693 HOH   B O   1 
HETATM 4675 O  O   . HOH   G 4 .   ? 38.782   -25.001   2.694     1.000 40.45978 ? 694 HOH   B O   1 
HETATM 4676 O  O   . HOH   G 4 .   ? 2.22315  -25.39892 3.01800   1.000 34.17533 ? 695 HOH   B O   1 
HETATM 4677 O  O   . HOH   G 4 .   ? 27.19669 -13.55108 26.90668  1.000 35.09423 ? 696 HOH   B O   1 
HETATM 4678 O  O   . HOH   G 4 .   ? 32.85502 -42.93593 7.23860   1.000 34.72894 ? 697 HOH   B O   1 
HETATM 4679 O  O   . HOH   G 4 .   ? 39.159   -29.358   1.482     1.000 44.35213 ? 698 HOH   B O   1 
HETATM 4680 O  O   . HOH   G 4 .   ? 4.24121  -31.97622 5.04106   1.000 29.75423 ? 699 HOH   B O   1 
HETATM 4681 O  O   . HOH   G 4 .   ? 0.21181  -32.07281 0.18362   1.000 43.33254 ? 700 HOH   B O   1 
HETATM 4682 O  O   . HOH   G 4 .   ? 34.69278 -42.97724 5.61665   1.000 45.55866 ? 701 HOH   B O   1 
HETATM 4683 O  O   . HOH   G 4 .   ? 2.58063  -25.08085 0.17680   1.000 51.87321 ? 702 HOH   B O   1 
HETATM 4684 O  O   . HOH   G 4 .   ? 4.32985  -37.98576 32.32679  1.000 41.72299 ? 703 HOH   B O   1 
HETATM 4685 O  O   . HOH   G 4 .   ? 37.66550 -42.92674 2.08957   1.000 31.78747 ? 704 HOH   B O   1 
HETATM 4686 O  O   . HOH   G 4 .   ? 35.81279 -43.62317 1.44407   1.000 36.77805 ? 705 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   . PRO A 7   ? 0.46681 0.45984 0.63732 0.01220  0.04383  -0.08587 3   PRO A N   
2    C CA  . PRO A 7   ? 0.39246 0.38104 0.54260 0.00335  0.03764  -0.07747 3   PRO A CA  
3    C C   . PRO A 7   ? 0.32445 0.32832 0.48346 0.00024  0.03231  -0.06701 3   PRO A C   
4    O O   . PRO A 7   ? 0.25319 0.27102 0.41537 -0.00262 0.03877  -0.06785 3   PRO A O   
5    C CB  . PRO A 7   ? 0.39477 0.38072 0.52168 -0.00226 0.04789  -0.08387 3   PRO A CB  
6    C CG  . PRO A 7   ? 0.47771 0.47498 0.61662 0.00200  0.06124  -0.09295 3   PRO A CG  
7    C CD  . PRO A 7   ? 0.21896 0.22352 0.38853 0.01138  0.05826  -0.09392 3   PRO A CD  
8    N N   . LYS A 8   ? 0.25327 0.25416 0.41567 0.00038  0.02087  -0.05747 4   LYS A N   
9    C CA  . LYS A 8   ? 0.21368 0.22820 0.38236 -0.00190 0.01500  -0.04828 4   LYS A CA  
10   C C   . LYS A 8   ? 0.19983 0.21775 0.35069 -0.01029 0.01798  -0.04692 4   LYS A C   
11   O O   . LYS A 8   ? 0.22409 0.23058 0.35523 -0.01468 0.01897  -0.04772 4   LYS A O   
12   C CB  . LYS A 8   ? 0.21918 0.22799 0.38997 -0.00065 0.00342  -0.03799 4   LYS A CB  
13   C CG  . LYS A 8   ? 0.30990 0.31605 0.50115 0.00802  -0.00118 -0.03677 4   LYS A CG  
14   C CD  . LYS A 8   ? 0.27784 0.28041 0.47095 0.00850  -0.01235 -0.02401 4   LYS A CD  
15   C CE  . LYS A 8   ? 0.24953 0.25065 0.46445 0.01771  -0.01780 -0.02114 4   LYS A CE  
16   N NZ  . LYS A 8   ? 0.35940 0.34549 0.58054 0.02265  -0.01376 -0.03035 4   LYS A NZ  
17   N N   . GLN A 9   ? 0.14378 0.17708 0.30270 -0.01237 0.01860  -0.04504 5   GLN A N   
18   C CA  . GLN A 9   ? 0.13852 0.17477 0.28366 -0.02005 0.02154  -0.04416 5   GLN A CA  
19   C C   . GLN A 9   ? 0.15895 0.19703 0.29869 -0.02250 0.01197  -0.03577 5   GLN A C   
20   O O   . GLN A 9   ? 0.15224 0.20037 0.30488 -0.01980 0.00526  -0.03152 5   GLN A O   
21   C CB  . GLN A 9   ? 0.13729 0.18860 0.29535 -0.02197 0.02885  -0.04841 5   GLN A CB  
22   C CG  . GLN A 9   ? 0.14820 0.19902 0.30929 -0.02024 0.04099  -0.05699 5   GLN A CG  
23   C CD  . GLN A 9   ? 0.25195 0.28662 0.38666 -0.02409 0.04671  -0.05965 5   GLN A CD  
24   O OE1 . GLN A 9   ? 0.40993 0.44144 0.52884 -0.03096 0.04861  -0.05727 5   GLN A OE1 
25   N NE2 . GLN A 9   ? 0.46211 0.48547 0.59164 -0.01946 0.04841  -0.06466 5   GLN A NE2 
26   N N   . TYR A 10  ? 0.12988 0.15868 0.25028 -0.02712 0.01128  -0.03362 6   TYR A N   
27   C CA  . TYR A 10  ? 0.12181 0.15221 0.23525 -0.02935 0.00422  -0.02695 6   TYR A CA  
28   C C   . TYR A 10  ? 0.11966 0.15145 0.22262 -0.03522 0.00725  -0.02834 6   TYR A C   
29   O O   . TYR A 10  ? 0.12490 0.15147 0.22035 -0.03831 0.01441  -0.03260 6   TYR A O   
30   C CB  . TYR A 10  ? 0.12339 0.14237 0.22642 -0.02909 0.00007  -0.02274 6   TYR A CB  
31   C CG  . TYR A 10  ? 0.12726 0.14282 0.24111 -0.02414 -0.00409 -0.01993 6   TYR A CG  
32   C CD1 . TYR A 10  ? 0.12738 0.15000 0.25089 -0.02116 -0.01067 -0.01291 6   TYR A CD1 
33   C CD2 . TYR A 10  ? 0.13596 0.13990 0.24936 -0.02244 -0.00194 -0.02425 6   TYR A CD2 
34   C CE1 . TYR A 10  ? 0.13118 0.14862 0.26469 -0.01667 -0.01482 -0.00900 6   TYR A CE1 
35   C CE2 . TYR A 10  ? 0.14159 0.14000 0.26597 -0.01802 -0.00610 -0.02187 6   TYR A CE2 
36   C CZ  . TYR A 10  ? 0.16684 0.17164 0.30180 -0.01517 -0.01245 -0.01358 6   TYR A CZ  
37   O OH  . TYR A 10  ? 0.15598 0.15331 0.30193 -0.01080 -0.01693 -0.00987 6   TYR A OH  
38   N N   . PRO A 11  ? 0.11455 0.15230 0.21586 -0.03679 0.00203  -0.02488 7   PRO A N   
39   C CA  . PRO A 11  ? 0.13059 0.16764 0.22307 -0.04211 0.00432  -0.02679 7   PRO A CA  
40   C C   . PRO A 11  ? 0.19739 0.22088 0.27261 -0.04430 0.00706  -0.02661 7   PRO A C   
41   O O   . PRO A 11  ? 0.11866 0.13566 0.18783 -0.04214 0.00430  -0.02386 7   PRO A O   
42   C CB  . PRO A 11  ? 0.17069 0.21460 0.26247 -0.04182 -0.00305 -0.02355 7   PRO A CB  
43   C CG  . PRO A 11  ? 0.13915 0.19128 0.24289 -0.03692 -0.00853 -0.02006 7   PRO A CG  
44   C CD  . PRO A 11  ? 0.11139 0.15602 0.21784 -0.03366 -0.00613 -0.01923 7   PRO A CD  
45   N N   . ILE A 12  ? 0.17443 0.19357 0.24255 -0.04889 0.01198  -0.02911 8   ILE A N   
46   C CA  . ILE A 12  ? 0.16478 0.17056 0.21601 -0.05069 0.01393  -0.02847 8   ILE A CA  
47   C C   . ILE A 12  ? 0.13173 0.13403 0.17585 -0.05405 0.01282  -0.02776 8   ILE A C   
48   O O   . ILE A 12  ? 0.15380 0.16066 0.20407 -0.05768 0.01489  -0.02982 8   ILE A O   
49   C CB  . ILE A 12  ? 0.29819 0.29763 0.34379 -0.05254 0.02194  -0.03154 8   ILE A CB  
50   C CG1 . ILE A 12  ? 0.27417 0.25920 0.29990 -0.05427 0.02225  -0.02996 8   ILE A CG1 
51   C CG2 . ILE A 12  ? 0.26927 0.27566 0.32368 -0.05669 0.02898  -0.03427 8   ILE A CG2 
52   C CD1 . ILE A 12  ? 0.62425 0.60161 0.63927 -0.05522 0.02904  -0.03268 8   ILE A CD1 
53   N N   . ILE A 13  ? 0.18057 0.17497 0.21363 -0.05271 0.00916  -0.02524 9   ILE A N   
54   C CA  . ILE A 13  ? 0.18259 0.17089 0.20825 -0.05449 0.00789  -0.02492 9   ILE A CA  
55   C C   . ILE A 13  ? 0.18608 0.16032 0.19732 -0.05513 0.00911  -0.02309 9   ILE A C   
56   O O   . ILE A 13  ? 0.18655 0.15771 0.19297 -0.05231 0.00643  -0.02142 9   ILE A O   
57   C CB  . ILE A 13  ? 0.18320 0.17639 0.21000 -0.05096 0.00204  -0.02372 9   ILE A CB  
58   C CG1 . ILE A 13  ? 0.19289 0.19968 0.23072 -0.04987 -0.00034 -0.02445 9   ILE A CG1 
59   C CG2 . ILE A 13  ? 0.19180 0.17784 0.21215 -0.05193 0.00116  -0.02502 9   ILE A CG2 
60   C CD1 . ILE A 13  ? 0.28584 0.29850 0.32906 -0.04634 -0.00246 -0.02107 9   ILE A CD1 
61   N N   . ASN A 14  ? 0.20594 0.17125 0.21046 -0.05910 0.01236  -0.02302 10  ASN A N   
62   C CA  . ASN A 14  ? 0.17417 0.12482 0.16290 -0.05996 0.01326  -0.02014 10  ASN A CA  
63   C C   . ASN A 14  ? 0.26680 0.20900 0.24986 -0.05766 0.00788  -0.01802 10  ASN A C   
64   O O   . ASN A 14  ? 0.22834 0.17107 0.21666 -0.05843 0.00707  -0.01968 10  ASN A O   
65   C CB  . ASN A 14  ? 0.20180 0.14612 0.18536 -0.06612 0.02128  -0.01979 10  ASN A CB  
66   C CG  . ASN A 14  ? 0.44078 0.39240 0.42824 -0.06737 0.02796  -0.02229 10  ASN A CG  
67   O OD1 . ASN A 14  ? 0.42027 0.36615 0.39597 -0.06631 0.02983  -0.02195 10  ASN A OD1 
68   N ND2 . ASN A 14  ? 0.39202 0.35654 0.39633 -0.06924 0.03121  -0.02548 10  ASN A ND2 
69   N N   . PHE A 15  ? 0.22401 0.15853 0.19707 -0.05447 0.00368  -0.01505 11  PHE A N   
70   C CA  . PHE A 15  ? 0.24987 0.17452 0.21721 -0.05164 -0.00120 -0.01254 11  PHE A CA  
71   C C   . PHE A 15  ? 0.21395 0.12468 0.16472 -0.05184 -0.00284 -0.00816 11  PHE A C   
72   O O   . PHE A 15  ? 0.20864 0.12043 0.15340 -0.05181 -0.00322 -0.00806 11  PHE A O   
73   C CB  . PHE A 15  ? 0.22441 0.15757 0.20009 -0.04552 -0.00730 -0.01309 11  PHE A CB  
74   C CG  . PHE A 15  ? 0.20159 0.12610 0.17452 -0.04135 -0.01191 -0.01144 11  PHE A CG  
75   C CD1 . PHE A 15  ? 0.27939 0.19906 0.25474 -0.04135 -0.01076 -0.01370 11  PHE A CD1 
76   C CD2 . PHE A 15  ? 0.25891 0.17966 0.22778 -0.03721 -0.01805 -0.00818 11  PHE A CD2 
77   C CE1 . PHE A 15  ? 0.20846 0.11891 0.18250 -0.03648 -0.01489 -0.01283 11  PHE A CE1 
78   C CE2 . PHE A 15  ? 0.29237 0.20571 0.26104 -0.03223 -0.02273 -0.00663 11  PHE A CE2 
79   C CZ  . PHE A 15  ? 0.20668 0.11432 0.17796 -0.03148 -0.02077 -0.00899 11  PHE A CZ  
80   N N   . THR A 16  ? 0.22502 0.12165 0.16756 -0.05183 -0.00447 -0.00465 12  THR A N   
81   C CA  . THR A 16  ? 0.25410 0.13611 0.17879 -0.05132 -0.00772 0.00090  12  THR A CA  
82   C C   . THR A 16  ? 0.24846 0.12255 0.17335 -0.04525 -0.01608 0.00388  12  THR A C   
83   O O   . THR A 16  ? 0.27847 0.15086 0.21225 -0.04372 -0.01610 0.00231  12  THR A O   
84   C CB  . THR A 16  ? 0.30638 0.17541 0.21730 -0.05819 -0.00024 0.00459  12  THR A CB  
85   O OG1 . THR A 16  ? 0.33494 0.18902 0.22515 -0.05729 -0.00416 0.01098  12  THR A OG1 
86   C CG2 . THR A 16  ? 0.28864 0.15051 0.20602 -0.06119 0.00250  0.00510  12  THR A CG2 
87   N N   . THR A 17  ? 0.25738 0.12714 0.17340 -0.04133 -0.02374 0.00738  13  THR A N   
88   C CA  . THR A 17  ? 0.32221 0.18414 0.23899 -0.03477 -0.03240 0.01091  13  THR A CA  
89   C C   . THR A 17  ? 0.29297 0.13293 0.19386 -0.03632 -0.03269 0.01775  13  THR A C   
90   O O   . THR A 17  ? 0.30314 0.13396 0.20592 -0.03043 -0.03951 0.02089  13  THR A O   
91   C CB  . THR A 17  ? 0.30972 0.17673 0.22555 -0.02995 -0.04218 0.01223  13  THR A CB  
92   O OG1 . THR A 17  ? 0.30567 0.16294 0.19998 -0.03338 -0.04350 0.01577  13  THR A OG1 
93   C CG2 . THR A 17  ? 0.30157 0.18909 0.23452 -0.02919 -0.04174 0.00653  13  THR A CG2 
94   N N   . ALA A 18  ? 0.30517 0.13654 0.19141 -0.04393 -0.02504 0.02046  14  ALA A N   
95   C CA  . ALA A 18  ? 0.34654 0.15601 0.21618 -0.04697 -0.02393 0.02856  14  ALA A CA  
96   C C   . ALA A 18  ? 0.44865 0.25171 0.33058 -0.04856 -0.02031 0.02716  14  ALA A C   
97   O O   . ALA A 18  ? 0.41937 0.22885 0.30958 -0.05506 -0.01144 0.02274  14  ALA A O   
98   C CB  . ALA A 18  ? 0.38124 0.18599 0.23225 -0.05529 -0.01489 0.03160  14  ALA A CB  
99   N N   . GLY A 19  ? 0.39613 0.18657 0.28031 -0.04232 -0.02783 0.03026  15  GLY A N   
100  C CA  . GLY A 19  ? 0.45417 0.23668 0.35019 -0.04282 -0.02569 0.02739  15  GLY A CA  
101  C C   . GLY A 19  ? 0.45463 0.25582 0.37204 -0.03934 -0.02487 0.01648  15  GLY A C   
102  O O   . GLY A 19  ? 0.41396 0.21319 0.34041 -0.04281 -0.02055 0.01138  15  GLY A O   
103  N N   . ALA A 20  ? 0.33413 0.15317 0.25934 -0.03299 -0.02909 0.01290  16  ALA A N   
104  C CA  . ALA A 20  ? 0.32109 0.15867 0.26419 -0.02990 -0.02752 0.00373  16  ALA A CA  
105  C C   . ALA A 20  ? 0.38348 0.21374 0.33617 -0.02346 -0.03028 -0.00031 16  ALA A C   
106  O O   . ALA A 20  ? 0.32713 0.14482 0.27825 -0.01664 -0.03680 0.00364  16  ALA A O   
107  C CB  . ALA A 20  ? 0.30823 0.16467 0.25772 -0.02488 -0.03140 0.00247  16  ALA A CB  
108  N N   . THR A 21  ? 0.30277 0.14064 0.26524 -0.02517 -0.02576 -0.00869 17  THR A N   
109  C CA  . THR A 21  ? 0.30278 0.13489 0.27389 -0.01908 -0.02735 -0.01523 17  THR A CA  
110  C C   . THR A 21  ? 0.26381 0.11838 0.24630 -0.01533 -0.02509 -0.02413 17  THR A C   
111  O O   . THR A 21  ? 0.24557 0.11810 0.22960 -0.01859 -0.02237 -0.02442 17  THR A O   
112  C CB  . THR A 21  ? 0.35125 0.16528 0.32010 -0.02587 -0.02443 -0.01760 17  THR A CB  
113  O OG1 . THR A 21  ? 0.29720 0.12303 0.26814 -0.03498 -0.01857 -0.02183 17  THR A OG1 
114  C CG2 . THR A 21  ? 0.32325 0.11319 0.27979 -0.03010 -0.02578 -0.00719 17  THR A CG2 
115  N N   . VAL A 22  ? 0.30815 0.16059 0.29789 -0.00813 -0.02602 -0.03136 18  VAL A N   
116  C CA  . VAL A 22  ? 0.31008 0.18226 0.30761 -0.00482 -0.02279 -0.04019 18  VAL A CA  
117  C C   . VAL A 22  ? 0.29738 0.17610 0.29236 -0.01402 -0.01863 -0.04461 18  VAL A C   
118  O O   . VAL A 22  ? 0.27097 0.16960 0.26854 -0.01477 -0.01617 -0.04678 18  VAL A O   
119  C CB  . VAL A 22  ? 0.43198 0.29799 0.43567 0.00465  -0.02363 -0.04851 18  VAL A CB  
120  C CG1 . VAL A 22  ? 0.43939 0.32129 0.44581 0.00581  -0.01916 -0.05899 18  VAL A CG1 
121  C CG2 . VAL A 22  ? 0.37431 0.24406 0.38589 0.01548  -0.02733 -0.04497 18  VAL A CG2 
122  N N   . GLN A 23  ? 0.26149 0.12376 0.25238 -0.02143 -0.01818 -0.04525 19  GLN A N   
123  C CA  . GLN A 23  ? 0.28587 0.15525 0.27721 -0.03042 -0.01526 -0.04957 19  GLN A CA  
124  C C   . GLN A 23  ? 0.23907 0.12146 0.22918 -0.03636 -0.01280 -0.04290 19  GLN A C   
125  O O   . GLN A 23  ? 0.22499 0.12481 0.21852 -0.03854 -0.01124 -0.04592 19  GLN A O   
126  C CB  . GLN A 23  ? 0.30325 0.15204 0.29349 -0.03776 -0.01533 -0.05160 19  GLN A CB  
127  C CG  . GLN A 23  ? 0.62527 0.46000 0.61755 -0.03264 -0.01791 -0.06074 19  GLN A CG  
128  C CD  . GLN A 23  ? 0.94845 0.76004 0.94077 -0.04102 -0.01846 -0.06170 19  GLN A CD  
129  O OE1 . GLN A 23  ? 0.95085 0.75272 0.94023 -0.04881 -0.01668 -0.05246 19  GLN A OE1 
130  N NE2 . GLN A 23  ? 0.94201 0.74440 0.93733 -0.03987 -0.02053 -0.07315 19  GLN A NE2 
131  N N   . SER A 24  ? 0.26897 0.14243 0.25335 -0.03859 -0.01268 -0.03393 20  SER A N   
132  C CA  . SER A 24  ? 0.23077 0.11482 0.21328 -0.04390 -0.00973 -0.02899 20  SER A CA  
133  C C   . SER A 24  ? 0.22958 0.13291 0.21584 -0.03862 -0.01074 -0.02875 20  SER A C   
134  O O   . SER A 24  ? 0.21234 0.12910 0.20137 -0.04208 -0.00839 -0.02864 20  SER A O   
135  C CB  . SER A 24  ? 0.24581 0.11516 0.21801 -0.04695 -0.00920 -0.02011 20  SER A CB  
136  O OG  . SER A 24  ? 0.25211 0.12031 0.22012 -0.03964 -0.01385 -0.01548 20  SER A OG  
137  N N   . TYR A 25  ? 0.21227 0.11737 0.20039 -0.03029 -0.01415 -0.02845 21  TYR A N   
138  C CA  . TYR A 25  ? 0.19627 0.12005 0.19001 -0.02633 -0.01458 -0.02788 21  TYR A CA  
139  C C   . TYR A 25  ? 0.21923 0.15781 0.21834 -0.02590 -0.01220 -0.03412 21  TYR A C   
140  O O   . TYR A 25  ? 0.17418 0.12765 0.17644 -0.02704 -0.01099 -0.03269 21  TYR A O   
141  C CB  . TYR A 25  ? 0.19915 0.12307 0.19641 -0.01799 -0.01852 -0.02585 21  TYR A CB  
142  C CG  . TYR A 25  ? 0.18410 0.12770 0.18954 -0.01489 -0.01846 -0.02483 21  TYR A CG  
143  C CD1 . TYR A 25  ? 0.17638 0.12512 0.18151 -0.01761 -0.02010 -0.01951 21  TYR A CD1 
144  C CD2 . TYR A 25  ? 0.17986 0.13639 0.19294 -0.00969 -0.01629 -0.02934 21  TYR A CD2 
145  C CE1 . TYR A 25  ? 0.18556 0.15094 0.19973 -0.01587 -0.02019 -0.01811 21  TYR A CE1 
146  C CE2 . TYR A 25  ? 0.16797 0.14246 0.18913 -0.00792 -0.01525 -0.02711 21  TYR A CE2 
147  C CZ  . TYR A 25  ? 0.20575 0.18414 0.22835 -0.01139 -0.01750 -0.02119 21  TYR A CZ  
148  O OH  . TYR A 25  ? 0.18140 0.17622 0.21347 -0.01069 -0.01664 -0.01855 21  TYR A OH  
149  N N   . THR A 26  ? 0.19681 0.13034 0.19593 -0.02423 -0.01196 -0.04109 22  THR A N   
150  C CA  . THR A 26  ? 0.22665 0.17323 0.22731 -0.02397 -0.01042 -0.04760 22  THR A CA  
151  C C   . THR A 26  ? 0.21389 0.16649 0.21465 -0.03186 -0.00968 -0.04748 22  THR A C   
152  O O   . THR A 26  ? 0.21279 0.18104 0.21522 -0.03191 -0.00921 -0.04727 22  THR A O   
153  C CB  . THR A 26  ? 0.31377 0.25110 0.31278 -0.02078 -0.01094 -0.05668 22  THR A CB  
154  O OG1 . THR A 26  ? 0.41017 0.34639 0.41181 -0.01158 -0.01101 -0.05752 22  THR A OG1 
155  C CG2 . THR A 26  ? 0.33116 0.28049 0.32813 -0.02164 -0.01024 -0.06424 22  THR A CG2 
156  N N   . ASN A 27  ? 0.20284 0.14350 0.20279 -0.03854 -0.00946 -0.04703 23  ASN A N   
157  C CA  . ASN A 27  ? 0.21506 0.16313 0.21857 -0.04578 -0.00841 -0.04709 23  ASN A CA  
158  C C   . ASN A 27  ? 0.21311 0.17299 0.21886 -0.04573 -0.00711 -0.04076 23  ASN A C   
159  O O   . ASN A 27  ? 0.16311 0.13581 0.17359 -0.04776 -0.00721 -0.04124 23  ASN A O   
160  C CB  . ASN A 27  ? 0.20964 0.14352 0.21349 -0.05338 -0.00676 -0.04643 23  ASN A CB  
161  C CG  . ASN A 27  ? 0.27538 0.19625 0.27899 -0.05501 -0.00859 -0.05330 23  ASN A CG  
162  O OD1 . ASN A 27  ? 0.34446 0.26909 0.34756 -0.05088 -0.01117 -0.06056 23  ASN A OD1 
163  N ND2 . ASN A 27  ? 0.31109 0.21573 0.31437 -0.06130 -0.00694 -0.05116 23  ASN A ND2 
164  N N   . PHE A 28  ? 0.17031 0.12522 0.17296 -0.04319 -0.00675 -0.03505 24  PHE A N   
165  C CA  . PHE A 28  ? 0.15932 0.12278 0.16376 -0.04322 -0.00604 -0.03004 24  PHE A CA  
166  C C   . PHE A 28  ? 0.14879 0.12801 0.15784 -0.03934 -0.00720 -0.02983 24  PHE A C   
167  O O   . PHE A 28  ? 0.15728 0.14628 0.17068 -0.04108 -0.00683 -0.02842 24  PHE A O   
168  C CB  . PHE A 28  ? 0.16363 0.11757 0.16256 -0.04121 -0.00705 -0.02511 24  PHE A CB  
169  C CG  . PHE A 28  ? 0.24774 0.20943 0.24851 -0.04025 -0.00770 -0.02129 24  PHE A CG  
170  C CD1 . PHE A 28  ? 0.22632 0.19211 0.22883 -0.04410 -0.00519 -0.02069 24  PHE A CD1 
171  C CD2 . PHE A 28  ? 0.18070 0.14537 0.18310 -0.03549 -0.01095 -0.01878 24  PHE A CD2 
172  C CE1 . PHE A 28  ? 0.20791 0.17848 0.21231 -0.04311 -0.00619 -0.01812 24  PHE A CE1 
173  C CE2 . PHE A 28  ? 0.20935 0.17988 0.21454 -0.03555 -0.01226 -0.01576 24  PHE A CE2 
174  C CZ  . PHE A 28  ? 0.22803 0.20031 0.23343 -0.03932 -0.01002 -0.01565 24  PHE A CZ  
175  N N   . ILE A 29  ? 0.16302 0.14487 0.17164 -0.03387 -0.00821 -0.03083 25  ILE A N   
176  C CA  . ILE A 29  ? 0.14285 0.13970 0.15488 -0.03068 -0.00800 -0.02923 25  ILE A CA  
177  C C   . ILE A 29  ? 0.14285 0.14856 0.15406 -0.03222 -0.00812 -0.03263 25  ILE A C   
178  O O   . ILE A 29  ? 0.13664 0.15363 0.15015 -0.03224 -0.00834 -0.02905 25  ILE A O   
179  C CB  . ILE A 29  ? 0.15453 0.15364 0.16741 -0.02442 -0.00756 -0.03004 25  ILE A CB  
180  C CG1 . ILE A 29  ? 0.14715 0.14023 0.16282 -0.02269 -0.00939 -0.02568 25  ILE A CG1 
181  C CG2 . ILE A 29  ? 0.14179 0.15719 0.15715 -0.02190 -0.00556 -0.02829 25  ILE A CG2 
182  C CD1 . ILE A 29  ? 0.19890 0.19801 0.21888 -0.02505 -0.01033 -0.01965 25  ILE A CD1 
183  N N   . ARG A 30  ? 0.21238 0.21242 0.22031 -0.03369 -0.00886 -0.03938 26  ARG A N   
184  C CA  . ARG A 30  ? 0.17707 0.18558 0.18392 -0.03561 -0.01079 -0.04333 26  ARG A CA  
185  C C   . ARG A 30  ? 0.17900 0.19264 0.19229 -0.04026 -0.01193 -0.03997 26  ARG A C   
186  O O   . ARG A 30  ? 0.22597 0.25106 0.24043 -0.04014 -0.01429 -0.03895 26  ARG A O   
187  C CB  . ARG A 30  ? 0.18690 0.18667 0.19030 -0.03722 -0.01230 -0.05231 26  ARG A CB  
188  C CG  . ARG A 30  ? 0.28951 0.28530 0.28701 -0.03115 -0.01111 -0.05732 26  ARG A CG  
189  C CD  . ARG A 30  ? 0.38230 0.36814 0.37622 -0.03264 -0.01326 -0.06756 26  ARG A CD  
190  N NE  . ARG A 30  ? 0.45803 0.43948 0.44692 -0.02556 -0.01157 -0.07347 26  ARG A NE  
191  C CZ  . ARG A 30  ? 0.49969 0.47025 0.48480 -0.02490 -0.01312 -0.08373 26  ARG A CZ  
192  N NH1 . ARG A 30  ? 0.51668 0.47976 0.50283 -0.03193 -0.01692 -0.08902 26  ARG A NH1 
193  N NH2 . ARG A 30  ? 0.54090 0.50815 0.52263 -0.01701 -0.01075 -0.08932 26  ARG A NH2 
194  N N   . ALA A 31  ? 0.21362 0.21905 0.23083 -0.04385 -0.01013 -0.03798 27  ALA A N   
195  C CA  . ALA A 31  ? 0.17634 0.18728 0.20127 -0.04736 -0.00987 -0.03559 27  ALA A CA  
196  C C   . ALA A 31  ? 0.17491 0.19352 0.20260 -0.04430 -0.00999 -0.02926 27  ALA A C   
197  O O   . ALA A 31  ? 0.17283 0.20021 0.20717 -0.04471 -0.01157 -0.02759 27  ALA A O   
198  C CB  . ALA A 31  ? 0.15060 0.15081 0.17705 -0.05189 -0.00622 -0.03535 27  ALA A CB  
199  N N   . VAL A 32  ? 0.12689 0.14206 0.15111 -0.04126 -0.00892 -0.02563 28  VAL A N   
200  C CA  . VAL A 32  ? 0.15900 0.18018 0.18691 -0.03925 -0.00937 -0.01966 28  VAL A CA  
201  C C   . VAL A 32  ? 0.21315 0.24608 0.24088 -0.03696 -0.01134 -0.01742 28  VAL A C   
202  O O   . VAL A 32  ? 0.19443 0.23337 0.22713 -0.03673 -0.01288 -0.01295 28  VAL A O   
203  C CB  . VAL A 32  ? 0.12696 0.14277 0.15303 -0.03735 -0.00867 -0.01681 28  VAL A CB  
204  C CG1 . VAL A 32  ? 0.14570 0.16782 0.17716 -0.03620 -0.00950 -0.01081 28  VAL A CG1 
205  C CG2 . VAL A 32  ? 0.14566 0.14952 0.16913 -0.03961 -0.00763 -0.01780 28  VAL A CG2 
206  N N   . ARG A 33  ? 0.16180 0.19744 0.18285 -0.03489 -0.01121 -0.02037 29  ARG A N   
207  C CA  . ARG A 33  ? 0.17852 0.22522 0.19546 -0.03289 -0.01261 -0.01844 29  ARG A CA  
208  C C   . ARG A 33  ? 0.22279 0.27479 0.24194 -0.03474 -0.01695 -0.01927 29  ARG A C   
209  O O   . ARG A 33  ? 0.20724 0.26730 0.22654 -0.03350 -0.01936 -0.01356 29  ARG A O   
210  C CB  . ARG A 33  ? 0.20298 0.25093 0.21063 -0.03019 -0.01118 -0.02409 29  ARG A CB  
211  C CG  . ARG A 33  ? 0.17738 0.22338 0.18541 -0.02703 -0.00711 -0.02314 29  ARG A CG  
212  C CD  . ARG A 33  ? 0.17710 0.22726 0.17657 -0.02301 -0.00466 -0.02871 29  ARG A CD  
213  N NE  . ARG A 33  ? 0.18411 0.23391 0.18740 -0.01916 -0.00065 -0.02829 29  ARG A NE  
214  C CZ  . ARG A 33  ? 0.19760 0.24039 0.19954 -0.01576 0.00050  -0.03547 29  ARG A CZ  
215  N NH1 . ARG A 33  ? 0.16502 0.19934 0.16071 -0.01632 -0.00164 -0.04404 29  ARG A NH1 
216  N NH2 . ARG A 33  ? 0.15510 0.19924 0.16365 -0.01165 0.00332  -0.03411 29  ARG A NH2 
217  N N   . GLY A 34  ? 0.15621 0.20395 0.17822 -0.03785 -0.01830 -0.02576 30  GLY A N   
218  C CA  . GLY A 34  ? 0.28850 0.34329 0.31553 -0.03977 -0.02316 -0.02765 30  GLY A CA  
219  C C   . GLY A 34  ? 0.29492 0.35355 0.33355 -0.03978 -0.02415 -0.02205 30  GLY A C   
220  O O   . GLY A 34  ? 0.24902 0.31653 0.29276 -0.03935 -0.02934 -0.02111 30  GLY A O   
221  N N   . ARG A 35  ? 0.27940 0.33128 0.32243 -0.03982 -0.01993 -0.01891 31  ARG A N   
222  C CA  . ARG A 35  ? 0.18728 0.24135 0.24096 -0.03886 -0.02044 -0.01451 31  ARG A CA  
223  C C   . ARG A 35  ? 0.21256 0.26838 0.26489 -0.03562 -0.02168 -0.00621 31  ARG A C   
224  O O   . ARG A 35  ? 0.19161 0.24986 0.25258 -0.03387 -0.02398 -0.00187 31  ARG A O   
225  C CB  . ARG A 35  ? 0.23354 0.27868 0.29172 -0.04088 -0.01530 -0.01658 31  ARG A CB  
226  C CG  . ARG A 35  ? 0.22308 0.26390 0.28099 -0.04516 -0.01229 -0.02311 31  ARG A CG  
227  C CD  . ARG A 35  ? 0.39244 0.44256 0.45789 -0.04730 -0.01575 -0.02719 31  ARG A CD  
228  N NE  . ARG A 35  ? 0.35829 0.41790 0.43786 -0.04572 -0.01777 -0.02561 31  ARG A NE  
229  C CZ  . ARG A 35  ? 0.34570 0.40747 0.43766 -0.04790 -0.01396 -0.02844 31  ARG A CZ  
230  N NH1 . ARG A 35  ? 0.37501 0.42950 0.46517 -0.05262 -0.00749 -0.03203 31  ARG A NH1 
231  N NH2 . ARG A 35  ? 0.36669 0.43831 0.47346 -0.04504 -0.01635 -0.02726 31  ARG A NH2 
232  N N   . LEU A 36  ? 0.14527 0.19993 0.18847 -0.03480 -0.01993 -0.00378 32  LEU A N   
233  C CA  . LEU A 36  ? 0.21584 0.27255 0.25893 -0.03303 -0.02010 0.00494  32  LEU A CA  
234  C C   . LEU A 36  ? 0.20422 0.27007 0.24312 -0.03114 -0.02435 0.01014  32  LEU A C   
235  O O   . LEU A 36  ? 0.17446 0.24130 0.21734 -0.02991 -0.02633 0.01861  32  LEU A O   
236  C CB  . LEU A 36  ? 0.15744 0.21254 0.19467 -0.03299 -0.01612 0.00583  32  LEU A CB  
237  C CG  . LEU A 36  ? 0.16049 0.20659 0.20222 -0.03429 -0.01371 0.00436  32  LEU A CG  
238  C CD1 . LEU A 36  ? 0.17667 0.22385 0.21454 -0.03346 -0.01090 0.00435  32  LEU A CD1 
239  C CD2 . LEU A 36  ? 0.11233 0.15497 0.16287 -0.03486 -0.01485 0.00996  32  LEU A CD2 
240  N N   . THR A 37  ? 0.24890 0.30068 0.23592 -0.02068 -0.04041 -0.00674 33  THR A N   
241  C CA  . THR A 37  ? 0.31349 0.37805 0.29012 -0.01606 -0.04351 -0.00537 33  THR A CA  
242  C C   . THR A 37  ? 0.35487 0.44756 0.33600 -0.02023 -0.05161 -0.00789 33  THR A C   
243  O O   . THR A 37  ? 0.38451 0.48395 0.37656 -0.02942 -0.05425 -0.01196 33  THR A O   
244  C CB  . THR A 37  ? 0.40738 0.45978 0.37347 -0.02013 -0.04254 -0.01161 33  THR A CB  
245  O OG1 . THR A 37  ? 0.57463 0.64096 0.52870 -0.01473 -0.04555 -0.00991 33  THR A OG1 
246  C CG2 . THR A 37  ? 0.47900 0.52874 0.44894 -0.03307 -0.04626 -0.02237 33  THR A CG2 
247  N N   . THR A 38  ? 0.39216 0.50255 0.36478 -0.01352 -0.05545 -0.00509 34  THR A N   
248  C CA  . THR A 38  ? 0.43450 0.57481 0.41041 -0.01865 -0.06435 -0.00941 34  THR A CA  
249  C C   . THR A 38  ? 0.39603 0.53564 0.36406 -0.02940 -0.06896 -0.02080 34  THR A C   
250  O O   . THR A 38  ? 0.41857 0.57575 0.39259 -0.04036 -0.07592 -0.02862 34  THR A O   
251  C CB  . THR A 38  ? 0.47666 0.64076 0.44712 -0.00466 -0.06739 -0.00075 34  THR A CB  
252  O OG1 . THR A 38  ? 0.44384 0.60202 0.39671 0.00177  -0.06663 0.00065  34  THR A OG1 
253  C CG2 . THR A 38  ? 0.58231 0.74070 0.55715 0.00843  -0.06133 0.01059  34  THR A CG2 
254  N N   . GLY A 39  ? 0.42402 0.54354 0.37899 -0.02700 -0.06480 -0.02246 35  GLY A N   
255  C CA  . GLY A 39  ? 0.52394 0.64423 0.46788 -0.03377 -0.06885 -0.03295 35  GLY A CA  
256  C C   . GLY A 39  ? 0.44808 0.59124 0.37872 -0.02612 -0.07419 -0.03130 35  GLY A C   
257  O O   . GLY A 39  ? 0.47685 0.62317 0.39634 -0.03113 -0.07822 -0.04094 35  GLY A O   
258  N N   . ALA A 40  ? 0.44674 0.60562 0.37701 -0.01318 -0.07432 -0.01947 36  ALA A N   
259  C CA  . ALA A 40  ? 0.52999 0.71181 0.44631 -0.00343 -0.07937 -0.01591 36  ALA A CA  
260  C C   . ALA A 40  ? 0.43667 0.60117 0.33427 0.00680  -0.07228 -0.00975 36  ALA A C   
261  O O   . ALA A 40  ? 0.48039 0.65969 0.36209 0.01234  -0.07614 -0.00992 36  ALA A O   
262  C CB  . ALA A 40  ? 0.41196 0.61824 0.33506 0.00816  -0.08220 -0.00481 36  ALA A CB  
263  N N   . ASP A 41  ? 0.31075 0.44600 0.20983 0.00906  -0.06198 -0.00435 37  ASP A N   
264  C CA  . ASP A 41  ? 0.37262 0.49012 0.25628 0.01641  -0.05367 0.00141  37  ASP A CA  
265  C C   . ASP A 41  ? 0.31626 0.41328 0.19975 0.00571  -0.04982 -0.00955 37  ASP A C   
266  O O   . ASP A 41  ? 0.30273 0.38021 0.19801 0.00067  -0.04460 -0.01059 37  ASP A O   
267  C CB  . ASP A 41  ? 0.28908 0.38967 0.17508 0.02663  -0.04446 0.01558  37  ASP A CB  
268  C CG  . ASP A 41  ? 0.35543 0.43961 0.22572 0.03377  -0.03517 0.02327  37  ASP A CG  
269  O OD1 . ASP A 41  ? 0.38424 0.47336 0.24040 0.03285  -0.03602 0.01861  37  ASP A OD1 
270  O OD2 . ASP A 41  ? 0.37562 0.44178 0.24742 0.03996  -0.02659 0.03380  37  ASP A OD2 
271  N N   . VAL A 42  ? 0.32255 0.42504 0.19215 0.00312  -0.05264 -0.01810 38  VAL A N   
272  C CA  . VAL A 42  ? 0.33168 0.41527 0.19833 -0.00422 -0.04829 -0.02824 38  VAL A CA  
273  C C   . VAL A 42  ? 0.36815 0.44977 0.21479 0.00371  -0.04264 -0.02510 38  VAL A C   
274  O O   . VAL A 42  ? 0.37455 0.47514 0.20619 0.01001  -0.04719 -0.02322 38  VAL A O   
275  C CB  . VAL A 42  ? 0.36821 0.45673 0.23753 -0.01691 -0.05656 -0.04483 38  VAL A CB  
276  C CG1 . VAL A 42  ? 0.36175 0.45274 0.25086 -0.02527 -0.06099 -0.04640 38  VAL A CG1 
277  C CG2 . VAL A 42  ? 0.54432 0.65715 0.39898 -0.01639 -0.06552 -0.05127 38  VAL A CG2 
278  N N   . ARG A 43  ? 0.28646 0.34722 0.13300 0.00392  -0.03251 -0.02379 39  ARG A N   
279  C CA  . ARG A 43  ? 0.30327 0.36121 0.13208 0.00957  -0.02562 -0.02237 39  ARG A CA  
280  C C   . ARG A 43  ? 0.36379 0.40971 0.19272 0.00234  -0.02348 -0.03642 39  ARG A C   
281  O O   . ARG A 43  ? 0.30605 0.33584 0.14978 -0.00276 -0.01950 -0.03876 39  ARG A O   
282  C CB  . ARG A 43  ? 0.34257 0.38800 0.17112 0.01686  -0.01381 -0.00720 39  ARG A CB  
283  C CG  . ARG A 43  ? 0.36119 0.40503 0.19994 0.02112  -0.01358 0.00522  39  ARG A CG  
284  C CD  . ARG A 43  ? 0.34024 0.40184 0.16609 0.03172  -0.01793 0.01510  39  ARG A CD  
285  N NE  . ARG A 43  ? 0.30660 0.36486 0.14285 0.03681  -0.01731 0.02615  39  ARG A NE  
286  C CZ  . ARG A 43  ? 0.41874 0.46011 0.25460 0.04296  -0.00738 0.03930  39  ARG A CZ  
287  N NH1 . ARG A 43  ? 0.39306 0.42111 0.21958 0.04421  0.00317  0.04444  39  ARG A NH1 
288  N NH2 . ARG A 43  ? 0.36955 0.40702 0.21466 0.04768  -0.00753 0.04720  39  ARG A NH2 
289  N N   . HIS A 44  ? 0.32468 0.37874 0.13636 0.00286  -0.02624 -0.04596 40  HIS A N   
290  C CA  . HIS A 44  ? 0.36405 0.40625 0.17253 -0.00187 -0.02377 -0.06000 40  HIS A CA  
291  C C   . HIS A 44  ? 0.35329 0.38424 0.17832 -0.01247 -0.02895 -0.07054 40  HIS A C   
292  O O   . HIS A 44  ? 0.46131 0.47506 0.29303 -0.01502 -0.02374 -0.07602 40  HIS A O   
293  C CB  . HIS A 44  ? 0.33575 0.36508 0.14382 0.00296  -0.01049 -0.05416 40  HIS A CB  
294  C CG  . HIS A 44  ? 0.38316 0.42163 0.17361 0.01256  -0.00380 -0.04350 40  HIS A CG  
295  N ND1 . HIS A 44  ? 0.46171 0.50922 0.23026 0.01690  -0.00335 -0.05002 40  HIS A ND1 
296  C CD2 . HIS A 44  ? 0.37156 0.41035 0.16176 0.01883  0.00311  -0.02645 40  HIS A CD2 
297  C CE1 . HIS A 44  ? 0.38106 0.43530 0.13652 0.02569  0.00380  -0.03643 40  HIS A CE1 
298  N NE2 . HIS A 44  ? 0.42560 0.47348 0.19402 0.02677  0.00802  -0.02174 40  HIS A NE2 
299  N N   . GLU A 45  ? 0.31126 0.35321 0.14298 -0.01818 -0.03896 -0.07257 41  GLU A N   
300  C CA  . GLU A 45  ? 0.30250 0.33687 0.14877 -0.02932 -0.04474 -0.08144 41  GLU A CA  
301  C C   . GLU A 45  ? 0.35548 0.37686 0.22145 -0.03052 -0.04016 -0.07311 41  GLU A C   
302  O O   . GLU A 45  ? 0.37503 0.38663 0.25264 -0.03888 -0.04284 -0.07911 41  GLU A O   
303  C CB  . GLU A 45  ? 0.31633 0.33547 0.15659 -0.03548 -0.04500 -0.09793 41  GLU A CB  
304  C CG  . GLU A 45  ? 0.46603 0.49159 0.28620 -0.03257 -0.04731 -0.10630 41  GLU A CG  
305  C CD  . GLU A 45  ? 0.65685 0.69019 0.47881 -0.03915 -0.05782 -0.11144 41  GLU A CD  
306  O OE1 . GLU A 45  ? 0.72914 0.77533 0.56382 -0.04339 -0.06372 -0.10631 41  GLU A OE1 
307  O OE2 . GLU A 45  ? 0.71650 0.74364 0.52713 -0.04012 -0.05986 -0.12092 41  GLU A OE2 
308  N N   . ILE A 46  ? 0.30139 0.32173 0.17064 -0.02275 -0.03324 -0.05966 42  ILE A N   
309  C CA  . ILE A 46  ? 0.27830 0.28634 0.16457 -0.02334 -0.02851 -0.05263 42  ILE A CA  
310  C C   . ILE A 46  ? 0.30702 0.32645 0.20022 -0.02021 -0.03114 -0.04140 42  ILE A C   
311  O O   . ILE A 46  ? 0.25877 0.28673 0.14332 -0.01202 -0.02900 -0.03199 42  ILE A O   
312  C CB  . ILE A 46  ? 0.30786 0.30373 0.19379 -0.01803 -0.01770 -0.04760 42  ILE A CB  
313  C CG1 . ILE A 46  ? 0.33276 0.32020 0.21100 -0.01898 -0.01470 -0.05873 42  ILE A CG1 
314  C CG2 . ILE A 46  ? 0.25109 0.23584 0.15466 -0.01951 -0.01403 -0.04215 42  ILE A CG2 
315  C CD1 . ILE A 46  ? 0.26353 0.24595 0.13909 -0.01313 -0.00384 -0.05400 42  ILE A CD1 
316  N N   . PRO A 47  ? 0.26151 0.28110 0.16924 -0.02550 -0.03513 -0.04148 43  PRO A N   
317  C CA  . PRO A 47  ? 0.23282 0.26403 0.14722 -0.02119 -0.03717 -0.03128 43  PRO A CA  
318  C C   . PRO A 47  ? 0.23452 0.25528 0.15095 -0.01323 -0.02869 -0.01970 43  PRO A C   
319  O O   . PRO A 47  ? 0.21077 0.21492 0.13194 -0.01450 -0.02211 -0.02017 43  PRO A O   
320  C CB  . PRO A 47  ? 0.24518 0.27576 0.17507 -0.02954 -0.04135 -0.03516 43  PRO A CB  
321  C CG  . PRO A 47  ? 0.21609 0.24003 0.14376 -0.03906 -0.04445 -0.04818 43  PRO A CG  
322  C CD  . PRO A 47  ? 0.29915 0.30967 0.21613 -0.03533 -0.03825 -0.05112 43  PRO A CD  
323  N N   . VAL A 48  ? 0.22024 0.25111 0.13323 -0.00493 -0.02896 -0.00946 44  VAL A N   
324  C CA  . VAL A 48  ? 0.21954 0.23884 0.13377 0.00252  -0.02105 0.00194  44  VAL A CA  
325  C C   . VAL A 48  ? 0.20877 0.23066 0.13533 0.00429  -0.02315 0.00644  44  VAL A C   
326  O O   . VAL A 48  ? 0.20800 0.24852 0.13683 0.00533  -0.03035 0.00639  44  VAL A O   
327  C CB  . VAL A 48  ? 0.28750 0.31198 0.18567 0.01283  -0.01795 0.01177  44  VAL A CB  
328  C CG1 . VAL A 48  ? 0.24296 0.25020 0.14195 0.01901  -0.00835 0.02326  44  VAL A CG1 
329  C CG2 . VAL A 48  ? 0.24955 0.27511 0.13405 0.01145  -0.01631 0.00659  44  VAL A CG2 
330  N N   . LEU A 49  ? 0.20160 0.20644 0.13618 0.00466  -0.01681 0.00984  45  LEU A N   
331  C CA  . LEU A 49  ? 0.19396 0.19904 0.13834 0.00783  -0.01741 0.01413  45  LEU A CA  
332  C C   . LEU A 49  ? 0.20641 0.21753 0.14319 0.02017  -0.01637 0.02538  45  LEU A C   
333  O O   . LEU A 49  ? 0.22131 0.23032 0.14522 0.02611  -0.01296 0.03146  45  LEU A O   
334  C CB  . LEU A 49  ? 0.18622 0.17095 0.13916 0.00496  -0.01101 0.01350  45  LEU A CB  
335  C CG  . LEU A 49  ? 0.20595 0.18533 0.16614 -0.00507 -0.01205 0.00347  45  LEU A CG  
336  C CD1 . LEU A 49  ? 0.17635 0.13840 0.14352 -0.00722 -0.00576 0.00276  45  LEU A CD1 
337  C CD2 . LEU A 49  ? 0.16533 0.15546 0.13388 -0.01002 -0.01899 -0.00159 45  LEU A CD2 
338  N N   . PRO A 50  ? 0.20236 0.22156 0.14615 0.02522  -0.01890 0.02885  46  PRO A N   
339  C CA  . PRO A 50  ? 0.21619 0.24151 0.15257 0.03914  -0.01801 0.03992  46  PRO A CA  
340  C C   . PRO A 50  ? 0.23751 0.23714 0.16665 0.04578  -0.00801 0.04847  46  PRO A C   
341  O O   . PRO A 50  ? 0.22462 0.20350 0.15966 0.04007  -0.00223 0.04566  46  PRO A O   
342  C CB  . PRO A 50  ? 0.29057 0.32785 0.23867 0.04223  -0.02157 0.04014  46  PRO A CB  
343  C CG  . PRO A 50  ? 0.31509 0.36073 0.27468 0.02870  -0.02671 0.02921  46  PRO A CG  
344  C CD  . PRO A 50  ? 0.21032 0.23608 0.16824 0.01934  -0.02284 0.02314  46  PRO A CD  
345  N N   . ASN A 51  ? 0.24880 0.25052 0.16484 0.05780  -0.00608 0.05913  47  ASN A N   
346  C CA  . ASN A 51  ? 0.32556 0.30165 0.23343 0.06523  0.00404  0.06929  47  ASN A CA  
347  C C   . ASN A 51  ? 0.33996 0.30283 0.25581 0.07043  0.00710  0.07140  47  ASN A C   
348  O O   . ASN A 51  ? 0.26509 0.24363 0.18440 0.07900  0.00227  0.07344  47  ASN A O   
349  C CB  . ASN A 51  ? 0.31698 0.29984 0.20752 0.07876  0.00487  0.08151  47  ASN A CB  
350  C CG  . ASN A 51  ? 0.31402 0.26726 0.19388 0.08596  0.01663  0.09353  47  ASN A CG  
351  O OD1 . ASN A 51  ? 0.35201 0.27984 0.23817 0.07938  0.02411  0.09164  47  ASN A OD1 
352  N ND2 . ASN A 51  ? 0.35753 0.31418 0.22068 0.09921  0.01832  0.10605  47  ASN A ND2 
353  N N   . ARG A 52  ? 0.33116 0.26652 0.25022 0.06503  0.01517  0.07014  48  ARG A N   
354  C CA  . ARG A 52  ? 0.30883 0.22784 0.23346 0.06956  0.01887  0.07082  48  ARG A CA  
355  C C   . ARG A 52  ? 0.32822 0.24043 0.24189 0.08716  0.02240  0.08353  48  ARG A C   
356  O O   . ARG A 52  ? 0.32732 0.23717 0.24483 0.09546  0.02236  0.08419  48  ARG A O   
357  C CB  . ARG A 52  ? 0.39900 0.29034 0.32783 0.05919  0.02672  0.06645  48  ARG A CB  
358  C CG  . ARG A 52  ? 0.51674 0.38217 0.44572 0.06424  0.03344  0.06873  48  ARG A CG  
359  C CD  . ARG A 52  ? 0.59533 0.43318 0.52356 0.05481  0.04279  0.06829  48  ARG A CD  
360  N NE  . ARG A 52  ? 0.75035 0.56182 0.67910 0.05718  0.04895  0.06804  48  ARG A NE  
361  C CZ  . ARG A 52  ? 0.57756 0.38401 0.51769 0.04837  0.04786  0.05647  48  ARG A CZ  
362  N NH1 . ARG A 52  ? 0.60879 0.42863 0.55920 0.03860  0.04268  0.04696  48  ARG A NH1 
363  N NH2 . ARG A 52  ? 0.59563 0.38820 0.53727 0.04867  0.05057  0.05310  48  ARG A NH2 
364  N N   . VAL A 53  ? 0.31663 0.22640 0.21574 0.09433  0.02558  0.09403  49  VAL A N   
365  C CA  . VAL A 53  ? 0.37251 0.27267 0.25893 0.11259  0.02991  0.10792  49  VAL A CA  
366  C C   . VAL A 53  ? 0.42877 0.36315 0.31707 0.12415  0.02034  0.10924  49  VAL A C   
367  O O   . VAL A 53  ? 0.45644 0.41942 0.34238 0.12350  0.01237  0.10860  49  VAL A O   
368  C CB  . VAL A 53  ? 0.48206 0.37258 0.35492 0.11324  0.03626  0.11603  49  VAL A CB  
369  C CG1 . VAL A 53  ? 0.40549 0.29129 0.27106 0.12692  0.03989  0.12427  49  VAL A CG1 
370  C CG2 . VAL A 53  ? 0.45232 0.31360 0.32660 0.09960  0.04583  0.11360  49  VAL A CG2 
371  N N   . GLY A 54  ? 0.34820 0.28172 0.24200 0.13291  0.02114  0.10902  50  GLY A N   
372  C CA  . GLY A 54  ? 0.41480 0.38167 0.31284 0.14331  0.01345  0.10971  50  GLY A CA  
373  C C   . GLY A 54  ? 0.37563 0.36934 0.28784 0.13822  0.00450  0.10172  50  GLY A C   
374  O O   . GLY A 54  ? 0.40184 0.42825 0.31995 0.14386  -0.00235 0.10110  50  GLY A O   
375  N N   . LEU A 55  ? 0.33185 0.31447 0.25266 0.12368  0.00499  0.09252  51  LEU A N   
376  C CA  . LEU A 55  ? 0.31745 0.32508 0.25403 0.11314  -0.00254 0.08165  51  LEU A CA  
377  C C   . LEU A 55  ? 0.32459 0.33382 0.26958 0.12126  -0.00121 0.08075  51  LEU A C   
378  O O   . LEU A 55  ? 0.27447 0.25409 0.21804 0.12284  0.00617  0.07992  51  LEU A O   
379  C CB  . LEU A 55  ? 0.31823 0.31327 0.26111 0.09361  -0.00190 0.07085  51  LEU A CB  
380  C CG  . LEU A 55  ? 0.24267 0.25958 0.19995 0.08114  -0.00899 0.06025  51  LEU A CG  
381  C CD1 . LEU A 55  ? 0.34537 0.39634 0.30368 0.07952  -0.01799 0.05963  51  LEU A CD1 
382  C CD2 . LEU A 55  ? 0.26916 0.26903 0.23056 0.06503  -0.00714 0.05122  51  LEU A CD2 
383  N N   . PRO A 56  ? 0.31949 0.36319 0.27328 0.12631  -0.00784 0.08041  52  PRO A N   
384  C CA  . PRO A 56  ? 0.25643 0.30417 0.21816 0.13493  -0.00584 0.07962  52  PRO A CA  
385  C C   . PRO A 56  ? 0.23981 0.27475 0.21098 0.12081  -0.00388 0.06891  52  PRO A C   
386  O O   . PRO A 56  ? 0.22213 0.26128 0.19927 0.10377  -0.00746 0.06131  52  PRO A O   
387  C CB  . PRO A 56  ? 0.24779 0.34101 0.21920 0.13807  -0.01386 0.07997  52  PRO A CB  
388  C CG  . PRO A 56  ? 0.26031 0.36700 0.22369 0.13774  -0.01849 0.08374  52  PRO A CG  
389  C CD  . PRO A 56  ? 0.26457 0.34643 0.22035 0.12625  -0.01705 0.08157  52  PRO A CD  
390  N N   . ILE A 57  ? 0.24795 0.26689 0.21934 0.12926  0.00191  0.06834  53  ILE A N   
391  C CA  . ILE A 57  ? 0.23596 0.24171 0.21401 0.11813  0.00410  0.05854  53  ILE A CA  
392  C C   . ILE A 57  ? 0.23479 0.27200 0.22661 0.10735  -0.00219 0.05263  53  ILE A C   
393  O O   . ILE A 57  ? 0.19839 0.22873 0.19517 0.09296  -0.00274 0.04480  53  ILE A O   
394  C CB  . ILE A 57  ? 0.25268 0.23822 0.22683 0.13126  0.01112  0.05859  53  ILE A CB  
395  C CG1 . ILE A 57  ? 0.24377 0.21567 0.22285 0.12007  0.01302  0.04787  53  ILE A CG1 
396  C CG2 . ILE A 57  ? 0.25767 0.27057 0.23551 0.14656  0.01009  0.06309  53  ILE A CG2 
397  C CD1 . ILE A 57  ? 0.24034 0.18810 0.21725 0.10429  0.01405  0.04240  53  ILE A CD1 
398  N N   . ASN A 58  ? 0.25766 0.33018 0.25604 0.11384  -0.00688 0.05658  54  ASN A N   
399  C CA  . ASN A 58  ? 0.18921 0.29166 0.20144 0.10253  -0.01197 0.05162  54  ASN A CA  
400  C C   . ASN A 58  ? 0.28353 0.39036 0.29843 0.08397  -0.01752 0.04668  54  ASN A C   
401  O O   . ASN A 58  ? 0.22154 0.34348 0.24662 0.07142  -0.02051 0.04155  54  ASN A O   
402  C CB  . ASN A 58  ? 0.23784 0.37978 0.25793 0.11340  -0.01548 0.05696  54  ASN A CB  
403  C CG  . ASN A 58  ? 0.38848 0.53763 0.40021 0.12737  -0.01752 0.06548  54  ASN A CG  
404  O OD1 . ASN A 58  ? 0.56767 0.72567 0.57681 0.12044  -0.02302 0.06586  54  ASN A OD1 
405  N ND2 . ASN A 58  ? 0.50728 0.64687 0.51202 0.14241  -0.01156 0.06956  54  ASN A ND2 
406  N N   . GLN A 59  ? 0.25108 0.34383 0.25634 0.08224  -0.01827 0.04826  55  GLN A N   
407  C CA  . GLN A 59  ? 0.19206 0.28571 0.19775 0.06618  -0.02275 0.04286  55  GLN A CA  
408  C C   . GLN A 59  ? 0.17773 0.23716 0.17710 0.05845  -0.01830 0.03879  55  GLN A C   
409  O O   . GLN A 59  ? 0.23416 0.29033 0.23169 0.04744  -0.02081 0.03473  55  GLN A O   
410  C CB  . GLN A 59  ? 0.19985 0.31097 0.19956 0.06972  -0.02793 0.04702  55  GLN A CB  
411  C CG  . GLN A 59  ? 0.25472 0.40437 0.26159 0.07780  -0.03327 0.05096  55  GLN A CG  
412  C CD  . GLN A 59  ? 0.48191 0.64851 0.48034 0.08480  -0.03838 0.05601  55  GLN A CD  
413  O OE1 . GLN A 59  ? 0.41503 0.56462 0.40169 0.08235  -0.03779 0.05629  55  GLN A OE1 
414  N NE2 . GLN A 59  ? 0.41526 0.61767 0.41955 0.09413  -0.04336 0.06018  55  GLN A NE2 
415  N N   . ARG A 60  ? 0.17872 0.21374 0.17519 0.06379  -0.01180 0.03898  56  ARG A N   
416  C CA  . ARG A 60  ? 0.18213 0.18659 0.17274 0.05788  -0.00724 0.03604  56  ARG A CA  
417  C C   . ARG A 60  ? 0.16684 0.16607 0.16424 0.04339  -0.00843 0.02722  56  ARG A C   
418  O O   . ARG A 60  ? 0.16622 0.14888 0.16083 0.03584  -0.00675 0.02398  56  ARG A O   
419  C CB  . ARG A 60  ? 0.19798 0.17771 0.18279 0.06825  0.00000  0.03872  56  ARG A CB  
420  C CG  . ARG A 60  ? 0.23463 0.18400 0.21516 0.06116  0.00518  0.03530  56  ARG A CG  
421  C CD  . ARG A 60  ? 0.20952 0.15387 0.18285 0.05819  0.00583  0.03935  56  ARG A CD  
422  N NE  . ARG A 60  ? 0.28450 0.20318 0.25578 0.05036  0.01132  0.03618  56  ARG A NE  
423  C CZ  . ARG A 60  ? 0.31415 0.20716 0.27949 0.05488  0.01862  0.03922  56  ARG A CZ  
424  N NH1 . ARG A 60  ? 0.34718 0.23334 0.30632 0.06880  0.02172  0.04587  56  ARG A NH1 
425  N NH2 . ARG A 60  ? 0.43899 0.31264 0.40494 0.04519  0.02319  0.03538  56  ARG A NH2 
426  N N   . PHE A 61  ? 0.15586 0.16943 0.16190 0.03990  -0.01084 0.02388  57  PHE A N   
427  C CA  . PHE A 61  ? 0.14500 0.15080 0.15578 0.02894  -0.01104 0.01688  57  PHE A CA  
428  C C   . PHE A 61  ? 0.13348 0.16015 0.15208 0.01988  -0.01603 0.01473  57  PHE A C   
429  O O   . PHE A 61  ? 0.13272 0.18269 0.15568 0.02216  -0.01890 0.01787  57  PHE A O   
430  C CB  . PHE A 61  ? 0.14722 0.14214 0.15880 0.03345  -0.00702 0.01449  57  PHE A CB  
431  C CG  . PHE A 61  ? 0.16150 0.13221 0.16578 0.04043  -0.00162 0.01503  57  PHE A CG  
432  C CD1 . PHE A 61  ? 0.16355 0.11400 0.16509 0.03357  0.00043  0.01151  57  PHE A CD1 
433  C CD2 . PHE A 61  ? 0.17474 0.14263 0.17529 0.05368  0.00190  0.01884  57  PHE A CD2 
434  C CE1 . PHE A 61  ? 0.17887 0.10625 0.17463 0.03785  0.00596  0.01177  57  PHE A CE1 
435  C CE2 . PHE A 61  ? 0.19181 0.13336 0.18493 0.05925  0.00753  0.01905  57  PHE A CE2 
436  C CZ  . PHE A 61  ? 0.19399 0.11502 0.18501 0.05030  0.00960  0.01545  57  PHE A CZ  
437  N N   . ILE A 62  ? 0.12618 0.14413 0.14680 0.00941  -0.01679 0.00940  58  ILE A N   
438  C CA  . ILE A 62  ? 0.11836 0.14880 0.14579 0.00037  -0.01972 0.00730  58  ILE A CA  
439  C C   . ILE A 62  ? 0.13357 0.15143 0.16192 -0.00199 -0.01729 0.00406  58  ILE A C   
440  O O   . ILE A 62  ? 0.19770 0.19795 0.22206 0.00071  -0.01467 0.00164  58  ILE A O   
441  C CB  . ILE A 62  ? 0.13913 0.17153 0.16641 -0.01011 -0.02376 0.00424  58  ILE A CB  
442  C CG1 . ILE A 62  ? 0.14198 0.15250 0.16463 -0.01412 -0.02237 -0.00018 58  ILE A CG1 
443  C CG2 . ILE A 62  ? 0.12204 0.16859 0.14677 -0.00735 -0.02691 0.00671  58  ILE A CG2 
444  C CD1 . ILE A 62  ? 0.18275 0.19251 0.20462 -0.02388 -0.02565 -0.00439 58  ILE A CD1 
445  N N   . LEU A 63  ? 0.11067 0.13872 0.14426 -0.00736 -0.01812 0.00419  59  LEU A N   
446  C CA  . LEU A 63  ? 0.10899 0.12839 0.14228 -0.00843 -0.01608 0.00225  59  LEU A CA  
447  C C   . LEU A 63  ? 0.13601 0.15176 0.17083 -0.01901 -0.01798 0.00067  59  LEU A C   
448  O O   . LEU A 63  ? 0.13367 0.15998 0.17240 -0.02627 -0.02010 0.00191  59  LEU A O   
449  C CB  . LEU A 63  ? 0.10983 0.14305 0.14588 -0.00274 -0.01355 0.00530  59  LEU A CB  
450  C CG  . LEU A 63  ? 0.19270 0.23061 0.22714 0.00940  -0.01128 0.00733  59  LEU A CG  
451  C CD1 . LEU A 63  ? 0.18203 0.23758 0.21994 0.01520  -0.00853 0.01028  59  LEU A CD1 
452  C CD2 . LEU A 63  ? 0.17146 0.18685 0.19880 0.01529  -0.00896 0.00356  59  LEU A CD2 
453  N N   . VAL A 64  ? 0.11274 0.11337 0.14440 -0.01971 -0.01725 -0.00233 60  VAL A N   
454  C CA  . VAL A 64  ? 0.15818 0.15186 0.18970 -0.02717 -0.01833 -0.00320 60  VAL A CA  
455  C C   . VAL A 64  ? 0.13927 0.13258 0.16952 -0.02474 -0.01634 -0.00156 60  VAL A C   
456  O O   . VAL A 64  ? 0.11660 0.10354 0.14362 -0.01875 -0.01552 -0.00417 60  VAL A O   
457  C CB  . VAL A 64  ? 0.13234 0.11040 0.16068 -0.02864 -0.01945 -0.00777 60  VAL A CB  
458  C CG1 . VAL A 64  ? 0.21518 0.18390 0.24217 -0.03263 -0.01984 -0.00836 60  VAL A CG1 
459  C CG2 . VAL A 64  ? 0.22447 0.20394 0.25244 -0.03215 -0.02130 -0.00909 60  VAL A CG2 
460  N N   . GLU A 65  ? 0.12416 0.12499 0.15663 -0.02973 -0.01542 0.00269  61  GLU A N   
461  C CA  . GLU A 65  ? 0.18974 0.19119 0.21944 -0.02733 -0.01299 0.00566  61  GLU A CA  
462  C C   . GLU A 65  ? 0.19884 0.18544 0.22476 -0.03130 -0.01369 0.00586  61  GLU A C   
463  O O   . GLU A 65  ? 0.23098 0.21329 0.25850 -0.03959 -0.01400 0.00756  61  GLU A O   
464  C CB  . GLU A 65  ? 0.17968 0.19869 0.21369 -0.02992 -0.01015 0.01165  61  GLU A CB  
465  C CG  . GLU A 65  ? 0.36702 0.38625 0.39649 -0.02789 -0.00688 0.01589  61  GLU A CG  
466  C CD  . GLU A 65  ? 0.51495 0.55408 0.54675 -0.02386 -0.00288 0.02009  61  GLU A CD  
467  O OE1 . GLU A 65  ? 0.51892 0.57330 0.55839 -0.03036 -0.00125 0.02438  61  GLU A OE1 
468  O OE2 . GLU A 65  ? 0.56297 0.60357 0.58913 -0.01423 -0.00132 0.01846  61  GLU A OE2 
469  N N   . LEU A 66  ? 0.15697 0.13582 0.17770 -0.02510 -0.01403 0.00376  62  LEU A N   
470  C CA  . LEU A 66  ? 0.17307 0.13886 0.18955 -0.02564 -0.01490 0.00420  62  LEU A CA  
471  C C   . LEU A 66  ? 0.19331 0.16173 0.20439 -0.02240 -0.01264 0.00988  62  LEU A C   
472  O O   . LEU A 66  ? 0.20117 0.17843 0.20957 -0.01595 -0.01186 0.00926  62  LEU A O   
473  C CB  . LEU A 66  ? 0.21617 0.17457 0.23142 -0.02059 -0.01751 -0.00236 62  LEU A CB  
474  C CG  . LEU A 66  ? 0.17788 0.13283 0.19701 -0.02298 -0.01885 -0.00740 62  LEU A CG  
475  C CD1 . LEU A 66  ? 0.11734 0.06704 0.13633 -0.01876 -0.02041 -0.01315 62  LEU A CD1 
476  C CD2 . LEU A 66  ? 0.13571 0.08388 0.15565 -0.03011 -0.01920 -0.00643 62  LEU A CD2 
477  N N   . SER A 67  ? 0.17804 0.13755 0.18629 -0.02655 -0.01122 0.01540  63  SER A N   
478  C CA  . SER A 67  ? 0.18971 0.14943 0.19091 -0.02311 -0.00850 0.02248  63  SER A CA  
479  C C   . SER A 67  ? 0.20285 0.14583 0.19783 -0.02025 -0.00975 0.02402  63  SER A C   
480  O O   . SER A 67  ? 0.20020 0.13050 0.19725 -0.02388 -0.01125 0.02114  63  SER A O   
481  C CB  . SER A 67  ? 0.25066 0.21623 0.25390 -0.03106 -0.00363 0.03073  63  SER A CB  
482  O OG  . SER A 67  ? 0.44237 0.42603 0.45267 -0.03277 -0.00260 0.02939  63  SER A OG  
483  N N   . ASN A 68  ? 0.18937 0.13304 0.17584 -0.01248 -0.00912 0.02849  64  ASN A N   
484  C CA  . ASN A 68  ? 0.22300 0.15211 0.20279 -0.00739 -0.01031 0.03118  64  ASN A CA  
485  C C   . ASN A 68  ? 0.21094 0.13435 0.18117 -0.00588 -0.00581 0.04306  64  ASN A C   
486  O O   . ASN A 68  ? 0.21411 0.14514 0.18431 -0.01089 -0.00121 0.04909  64  ASN A O   
487  C CB  . ASN A 68  ? 0.26958 0.20476 0.24767 0.00293  -0.01544 0.02419  64  ASN A CB  
488  C CG  . ASN A 68  ? 0.20745 0.15798 0.17939 0.01036  -0.01603 0.02445  64  ASN A CG  
489  O OD1 . ASN A 68  ? 0.22074 0.17740 0.18839 0.00941  -0.01199 0.03088  64  ASN A OD1 
490  N ND2 . ASN A 68  ? 0.19357 0.15146 0.16512 0.01753  -0.02100 0.01681  64  ASN A ND2 
491  N N   . HIS A 69  ? 0.22560 0.13605 0.18765 0.00149  -0.00660 0.04716  65  HIS A N   
492  C CA  . HIS A 69  ? 0.24847 0.14951 0.19954 0.00375  -0.00167 0.06009  65  HIS A CA  
493  C C   . HIS A 69  ? 0.28071 0.19981 0.22458 0.00977  -0.00000 0.06481  65  HIS A C   
494  O O   . HIS A 69  ? 0.27294 0.19012 0.21057 0.00704  0.00632  0.07601  65  HIS A O   
495  C CB  . HIS A 69  ? 0.26676 0.15182 0.20926 0.01406  -0.00348 0.06348  65  HIS A CB  
496  C CG  . HIS A 69  ? 0.27399 0.13518 0.21916 0.00871  -0.00241 0.06252  65  HIS A CG  
497  N ND1 . HIS A 69  ? 0.31384 0.17404 0.26773 0.00729  -0.00662 0.05122  65  HIS A ND1 
498  C CD2 . HIS A 69  ? 0.32216 0.15820 0.26125 0.00477  0.00279  0.07117  65  HIS A CD2 
499  C CE1 . HIS A 69  ? 0.36544 0.20202 0.31812 0.00331  -0.00437 0.05216  65  HIS A CE1 
500  N NE2 . HIS A 69  ? 0.36298 0.18329 0.30684 0.00140  0.00124  0.06384  65  HIS A NE2 
501  N N   . ALA A 70  ? 0.27867 0.21491 0.22270 0.01767  -0.00517 0.05625  66  ALA A N   
502  C CA  . ALA A 70  ? 0.23855 0.19276 0.17508 0.02374  -0.00406 0.05802  66  ALA A CA  
503  C C   . ALA A 70  ? 0.23753 0.20384 0.18062 0.01585  0.00029  0.05732  66  ALA A C   
504  O O   . ALA A 70  ? 0.25062 0.23276 0.18804 0.02114  0.00167  0.05717  66  ALA A O   
505  C CB  . ALA A 70  ? 0.27422 0.24159 0.20920 0.03346  -0.01136 0.04699  66  ALA A CB  
506  N N   . GLU A 71  ? 0.24072 0.20142 0.19527 0.00426  0.00220  0.05630  67  GLU A N   
507  C CA  . GLU A 71  ? 0.26347 0.23791 0.22610 -0.00296 0.00599  0.05596  67  GLU A CA  
508  C C   . GLU A 71  ? 0.26964 0.25985 0.23484 0.00302  0.00276  0.04555  67  GLU A C   
509  O O   . GLU A 71  ? 0.29133 0.29672 0.25817 0.00313  0.00638  0.04623  67  GLU A O   
510  C CB  . GLU A 71  ? 0.25403 0.23515 0.21125 -0.00532 0.01387  0.06831  67  GLU A CB  
511  C CG  . GLU A 71  ? 0.41003 0.37351 0.36760 -0.01544 0.01857  0.07853  67  GLU A CG  
512  C CD  . GLU A 71  ? 0.67879 0.64726 0.62978 -0.01785 0.02734  0.09227  67  GLU A CD  
513  O OE1 . GLU A 71  ? 0.54822 0.53866 0.50058 -0.01642 0.03086  0.09312  67  GLU A OE1 
514  O OE2 . GLU A 71  ? 0.61176 0.56150 0.55567 -0.02066 0.03134  0.10259  67  GLU A OE2 
515  N N   . LEU A 72  ? 0.18930 0.17567 0.15501 0.00805  -0.00354 0.03582  68  LEU A N   
516  C CA  . LEU A 72  ? 0.18125 0.17682 0.15100 0.01119  -0.00639 0.02500  68  LEU A CA  
517  C C   . LEU A 72  ? 0.20567 0.19747 0.18759 0.00328  -0.00710 0.02080  68  LEU A C   
518  O O   . LEU A 72  ? 0.20020 0.18027 0.18642 -0.00249 -0.00841 0.02162  68  LEU A O   
519  C CB  . LEU A 72  ? 0.18995 0.18429 0.15546 0.01864  -0.01246 0.01634  68  LEU A CB  
520  C CG  . LEU A 72  ? 0.22556 0.22492 0.17785 0.02761  -0.01332 0.02001  68  LEU A CG  
521  C CD1 . LEU A 72  ? 0.34356 0.34549 0.29407 0.03379  -0.02037 0.00983  68  LEU A CD1 
522  C CD2 . LEU A 72  ? 0.26247 0.27523 0.20702 0.03172  -0.00890 0.02270  68  LEU A CD2 
523  N N   . SER A 73  ? 0.18429 0.18583 0.17057 0.00403  -0.00607 0.01640  69  SER A N   
524  C CA  . SER A 73  ? 0.22730 0.22788 0.22371 -0.00185 -0.00661 0.01344  69  SER A CA  
525  C C   . SER A 73  ? 0.17575 0.17661 0.17342 0.00317  -0.00892 0.00396  69  SER A C   
526  O O   . SER A 73  ? 0.16211 0.16925 0.15460 0.01020  -0.00798 0.00057  69  SER A O   
527  C CB  . SER A 73  ? 0.29939 0.31267 0.30133 -0.00645 -0.00207 0.01970  69  SER A CB  
528  O OG  . SER A 73  ? 0.47683 0.48794 0.47867 -0.01359 0.00073  0.02842  69  SER A OG  
529  N N   . VAL A 74  ? 0.15039 0.14312 0.15400 -0.00052 -0.01147 -0.00039 70  VAL A N   
530  C CA  . VAL A 74  ? 0.12727 0.11808 0.13311 0.00240  -0.01231 -0.00757 70  VAL A CA  
531  C C   . VAL A 74  ? 0.14124 0.13209 0.15418 -0.00251 -0.01189 -0.00577 70  VAL A C   
532  O O   . VAL A 74  ? 0.15029 0.13944 0.16648 -0.00919 -0.01254 -0.00207 70  VAL A O   
533  C CB  . VAL A 74  ? 0.16354 0.14481 0.16843 0.00348  -0.01584 -0.01541 70  VAL A CB  
534  C CG1 . VAL A 74  ? 0.17352 0.15789 0.17112 0.00856  -0.01749 -0.01766 70  VAL A CG1 
535  C CG2 . VAL A 74  ? 0.16112 0.13435 0.17035 -0.00214 -0.01792 -0.01486 70  VAL A CG2 
536  N N   . THR A 75  ? 0.12389 0.11626 0.13823 0.00132  -0.01077 -0.00848 71  THR A N   
537  C CA  . THR A 75  ? 0.11583 0.11080 0.13554 -0.00126 -0.01064 -0.00632 71  THR A CA  
538  C C   . THR A 75  ? 0.12630 0.10928 0.14578 0.00004  -0.01147 -0.01149 71  THR A C   
539  O O   . THR A 75  ? 0.12049 0.09873 0.13707 0.00593  -0.00993 -0.01533 71  THR A O   
540  C CB  . THR A 75  ? 0.18514 0.19500 0.20676 0.00351  -0.00775 -0.00245 71  THR A CB  
541  O OG1 . THR A 75  ? 0.20070 0.22343 0.22383 0.00058  -0.00609 0.00316  71  THR A OG1 
542  C CG2 . THR A 75  ? 0.15026 0.16509 0.17698 0.00196  -0.00858 -0.00023 71  THR A CG2 
543  N N   . LEU A 76  ? 0.11179 0.08899 0.13377 -0.00564 -0.01332 -0.01168 72  LEU A N   
544  C CA  . LEU A 76  ? 0.18065 0.14750 0.20257 -0.00540 -0.01316 -0.01518 72  LEU A CA  
545  C C   . LEU A 76  ? 0.13749 0.10862 0.16014 -0.00320 -0.01205 -0.01152 72  LEU A C   
546  O O   . LEU A 76  ? 0.11700 0.09957 0.14213 -0.00552 -0.01316 -0.00732 72  LEU A O   
547  C CB  . LEU A 76  ? 0.13018 0.09014 0.15351 -0.01131 -0.01510 -0.01723 72  LEU A CB  
548  C CG  . LEU A 76  ? 0.17271 0.12669 0.19592 -0.01182 -0.01630 -0.02214 72  LEU A CG  
549  C CD1 . LEU A 76  ? 0.24085 0.19972 0.26140 -0.00880 -0.01706 -0.02205 72  LEU A CD1 
550  C CD2 . LEU A 76  ? 0.35928 0.30974 0.38400 -0.01630 -0.01787 -0.02234 72  LEU A CD2 
551  N N   . ALA A 77  ? 0.11921 0.08134 0.13957 0.00118  -0.00983 -0.01301 73  ALA A N   
552  C CA  . ALA A 77  ? 0.12306 0.08721 0.14235 0.00502  -0.00862 -0.00873 73  ALA A CA  
553  C C   . ALA A 77  ? 0.12588 0.08041 0.14398 0.00108  -0.00846 -0.00928 73  ALA A C   
554  O O   . ALA A 77  ? 0.15463 0.09629 0.17217 -0.00094 -0.00680 -0.01337 73  ALA A O   
555  C CB  . ALA A 77  ? 0.16477 0.12331 0.18046 0.01448  -0.00501 -0.00841 73  ALA A CB  
556  N N   . LEU A 78  ? 0.14600 0.10855 0.16381 -0.00027 -0.01012 -0.00551 74  LEU A N   
557  C CA  . LEU A 78  ? 0.12907 0.08510 0.14419 -0.00326 -0.00970 -0.00545 74  LEU A CA  
558  C C   . LEU A 78  ? 0.14264 0.10016 0.15292 0.00346  -0.00805 0.00027  74  LEU A C   
559  O O   . LEU A 78  ? 0.16662 0.13843 0.17726 0.00797  -0.00992 0.00430  74  LEU A O   
560  C CB  . LEU A 78  ? 0.11938 0.08245 0.13582 -0.01056 -0.01338 -0.00692 74  LEU A CB  
561  C CG  . LEU A 78  ? 0.19812 0.15406 0.21684 -0.01648 -0.01407 -0.01206 74  LEU A CG  
562  C CD1 . LEU A 78  ? 0.24663 0.20405 0.26854 -0.01626 -0.01473 -0.01331 74  LEU A CD1 
563  C CD2 . LEU A 78  ? 0.15776 0.11705 0.17568 -0.02237 -0.01691 -0.01356 74  LEU A CD2 
564  N N   . ASP A 79  ? 0.14244 0.08622 0.14839 0.00431  -0.00429 0.00110  75  ASP A N   
565  C CA  . ASP A 79  ? 0.17796 0.12041 0.17712 0.01110  -0.00204 0.00778  75  ASP A CA  
566  C C   . ASP A 79  ? 0.15288 0.10726 0.14920 0.00801  -0.00548 0.00919  75  ASP A C   
567  O O   . ASP A 79  ? 0.16631 0.11730 0.16279 0.00090  -0.00572 0.00522  75  ASP A O   
568  C CB  . ASP A 79  ? 0.19268 0.11401 0.18796 0.01160  0.00433  0.00850  75  ASP A CB  
569  C CG  . ASP A 79  ? 0.22659 0.14189 0.21312 0.02049  0.00812  0.01704  75  ASP A CG  
570  O OD1 . ASP A 79  ? 0.24981 0.17872 0.23198 0.02418  0.00532  0.02199  75  ASP A OD1 
571  O OD2 . ASP A 79  ? 0.36226 0.25839 0.34566 0.02378  0.01396  0.01870  75  ASP A OD2 
572  N N   . VAL A 80  ? 0.14875 0.12606 0.11497 0.01146  -0.04012 0.02662  76  VAL A N   
573  C CA  . VAL A 80  ? 0.15514 0.12583 0.10833 0.01119  -0.05000 0.02782  76  VAL A CA  
574  C C   . VAL A 80  ? 0.21580 0.17545 0.14477 0.00818  -0.04816 0.02784  76  VAL A C   
575  O O   . VAL A 80  ? 0.21081 0.16532 0.12439 0.00798  -0.05415 0.02624  76  VAL A O   
576  C CB  . VAL A 80  ? 0.16423 0.13281 0.12756 0.01330  -0.06217 0.03481  76  VAL A CB  
577  C CG1 . VAL A 80  ? 0.14172 0.12526 0.12866 0.01374  -0.06256 0.03474  76  VAL A CG1 
578  C CG2 . VAL A 80  ? 0.24268 0.20162 0.20547 0.01496  -0.06446 0.04049  76  VAL A CG2 
579  N N   . THR A 81  ? 0.18119 0.13636 0.10440 0.00487  -0.04028 0.02954  77  THR A N   
580  C CA  . THR A 81  ? 0.20430 0.14880 0.10175 -0.00129 -0.03788 0.03095  77  THR A CA  
581  C C   . THR A 81  ? 0.20747 0.16365 0.09536 -0.00487 -0.02698 0.02147  77  THR A C   
582  O O   . THR A 81  ? 0.23626 0.18848 0.10139 -0.01048 -0.02428 0.02060  77  THR A O   
583  C CB  . THR A 81  ? 0.25012 0.18205 0.14251 -0.00548 -0.03597 0.03760  77  THR A CB  
584  O OG1 . THR A 81  ? 0.24522 0.18667 0.15066 -0.00621 -0.02546 0.03377  77  THR A OG1 
585  C CG2 . THR A 81  ? 0.28371 0.20460 0.18640 0.00026  -0.04868 0.04482  77  THR A CG2 
586  N N   . ASN A 82  ? 0.18788 0.15892 0.09220 -0.00183 -0.02110 0.01365  78  ASN A N   
587  C CA  . ASN A 82  ? 0.19164 0.17637 0.09132 -0.00302 -0.01269 0.00235  78  ASN A CA  
588  C C   . ASN A 82  ? 0.26042 0.25501 0.17502 0.00412  -0.01616 -0.00657 78  ASN A C   
589  O O   . ASN A 82  ? 0.23354 0.24048 0.14885 0.00542  -0.01092 -0.01793 78  ASN A O   
590  C CB  . ASN A 82  ? 0.22160 0.21277 0.12195 -0.01012 0.00009  0.00101  78  ASN A CB  
591  C CG  . ASN A 82  ? 0.32455 0.31595 0.24465 -0.00815 0.00181  0.00324  78  ASN A CG  
592  O OD1 . ASN A 82  ? 0.22456 0.21608 0.15895 -0.00172 -0.00418 0.00355  78  ASN A OD1 
593  N ND2 . ASN A 82  ? 0.41075 0.40185 0.33002 -0.01479 0.00996  0.00482  78  ASN A ND2 
594  N N   . ALA A 83  ? 0.15385 0.14358 0.08031 0.00808  -0.02541 -0.00204 79  ALA A N   
595  C CA  . ALA A 83  ? 0.17990 0.17338 0.11607 0.01262  -0.03184 -0.00814 79  ALA A CA  
596  C C   . ALA A 83  ? 0.26541 0.26730 0.21365 0.01281  -0.02463 -0.01438 79  ALA A C   
597  O O   . ALA A 83  ? 0.28682 0.28999 0.23907 0.01619  -0.03033 -0.02149 79  ALA A O   
598  C CB  . ALA A 83  ? 0.27142 0.26434 0.19529 0.01690  -0.03934 -0.01724 79  ALA A CB  
599  N N   . TYR A 84  ? 0.21725 0.22197 0.17003 0.00914  -0.01423 -0.01175 80  TYR A N   
600  C CA  . TYR A 84  ? 0.29575 0.30762 0.25820 0.00891  -0.00761 -0.01824 80  TYR A CA  
601  C C   . TYR A 84  ? 0.13902 0.14704 0.11343 0.00876  -0.00740 -0.01260 80  TYR A C   
602  O O   . TYR A 84  ? 0.14859 0.15175 0.12562 0.00806  -0.00779 -0.00380 80  TYR A O   
603  C CB  . TYR A 84  ? 0.27644 0.29453 0.23484 0.00362  0.00375  -0.02024 80  TYR A CB  
604  C CG  . TYR A 84  ? 0.19129 0.22225 0.15709 0.00403  0.00899  -0.03212 80  TYR A CG  
605  C CD1 . TYR A 84  ? 0.29102 0.33436 0.25383 0.00692  0.00880  -0.04423 80  TYR A CD1 
606  C CD2 . TYR A 84  ? 0.20271 0.23408 0.17902 0.00222  0.01352  -0.03233 80  TYR A CD2 
607  C CE1 . TYR A 84  ? 0.24713 0.30501 0.22020 0.00838  0.01257  -0.05671 80  TYR A CE1 
608  C CE2 . TYR A 84  ? 0.31820 0.36134 0.30282 0.00265  0.01675  -0.04344 80  TYR A CE2 
609  C CZ  . TYR A 84  ? 0.27120 0.32864 0.25560 0.00586  0.01612  -0.05580 80  TYR A CZ  
610  O OH  . TYR A 84  ? 0.21801 0.28763 0.21509 0.00687  0.01729  -0.06561 80  TYR A OH  
611  N N   . VAL A 85  ? 0.16822 0.17869 0.14951 0.00993  -0.00731 -0.01883 81  VAL A N   
612  C CA  . VAL A 85  ? 0.09522 0.10274 0.08502 0.00913  -0.00574 -0.01510 81  VAL A CA  
613  C C   . VAL A 85  ? 0.08750 0.09434 0.08020 0.00718  0.00362  -0.01196 81  VAL A C   
614  O O   . VAL A 85  ? 0.15819 0.16788 0.14884 0.00496  0.00927  -0.01615 81  VAL A O   
615  C CB  . VAL A 85  ? 0.15088 0.15734 0.14278 0.01005  -0.00951 -0.02278 81  VAL A CB  
616  C CG1 . VAL A 85  ? 0.07976 0.08261 0.07669 0.00805  -0.00673 -0.01919 81  VAL A CG1 
617  C CG2 . VAL A 85  ? 0.13653 0.13878 0.12294 0.01188  -0.02197 -0.02577 81  VAL A CG2 
618  N N   . VAL A 86  ? 0.10256 0.10623 0.10057 0.00789  0.00464  -0.00529 82  VAL A N   
619  C CA  . VAL A 86  ? 0.08923 0.08846 0.08941 0.00763  0.01079  -0.00297 82  VAL A CA  
620  C C   . VAL A 86  ? 0.08369 0.08243 0.09044 0.00890  0.01397  -0.00557 82  VAL A C   
621  O O   . VAL A 86  ? 0.12035 0.11363 0.12766 0.00915  0.01833  -0.00568 82  VAL A O   
622  C CB  . VAL A 86  ? 0.13070 0.12510 0.13151 0.00970  0.00840  0.00457  82  VAL A CB  
623  C CG1 . VAL A 86  ? 0.12809 0.11915 0.11799 0.00741  0.00457  0.00791  82  VAL A CG1 
624  C CG2 . VAL A 86  ? 0.10523 0.10568 0.11687 0.01333  0.00505  0.00687  82  VAL A CG2 
625  N N   . GLY A 87  ? 0.07847 0.08054 0.08764 0.00887  0.01111  -0.00729 83  GLY A N   
626  C CA  . GLY A 87  ? 0.12715 0.12810 0.13901 0.00888  0.01431  -0.00920 83  GLY A CA  
627  C C   . GLY A 87  ? 0.20323 0.20749 0.21445 0.00601  0.00982  -0.00830 83  GLY A C   
628  O O   . GLY A 87  ? 0.12141 0.12762 0.13104 0.00453  0.00309  -0.00617 83  GLY A O   
629  N N   . TYR A 88  ? 0.11076 0.11409 0.12099 0.00415  0.01304  -0.00972 84  TYR A N   
630  C CA  . TYR A 88  ? 0.09066 0.09556 0.09674 -0.00183 0.00894  -0.00787 84  TYR A CA  
631  C C   . TYR A 88  ? 0.10049 0.11005 0.10723 -0.00394 0.01655  -0.00790 84  TYR A C   
632  O O   . TYR A 88  ? 0.08680 0.09434 0.09495 0.00041  0.02338  -0.01123 84  TYR A O   
633  C CB  . TYR A 88  ? 0.09039 0.08324 0.08495 -0.00524 -0.00013 -0.01188 84  TYR A CB  
634  C CG  . TYR A 88  ? 0.11187 0.09441 0.09885 -0.00642 0.00101  -0.01699 84  TYR A CG  
635  C CD1 . TYR A 88  ? 0.12178 0.10046 0.11109 -0.00182 0.00364  -0.02261 84  TYR A CD1 
636  C CD2 . TYR A 88  ? 0.10306 0.07862 0.07882 -0.01363 -0.00159 -0.01588 84  TYR A CD2 
637  C CE1 . TYR A 88  ? 0.15735 0.12534 0.13996 -0.00281 0.00293  -0.02748 84  TYR A CE1 
638  C CE2 . TYR A 88  ? 0.11134 0.07427 0.07730 -0.01491 -0.00222 -0.02047 84  TYR A CE2 
639  C CZ  . TYR A 88  ? 0.13655 0.09556 0.10686 -0.00872 -0.00048 -0.02655 84  TYR A CZ  
640  O OH  . TYR A 88  ? 0.17974 0.12521 0.14074 -0.00987 -0.00266 -0.03125 84  TYR A OH  
641  N N   . ARG A 89  ? 0.09119 0.10674 0.09541 -0.01156 0.01495  -0.00440 85  ARG A N   
642  C CA  . ARG A 89  ? 0.12750 0.15135 0.13059 -0.01596 0.02320  -0.00472 85  ARG A CA  
643  C C   . ARG A 89  ? 0.13894 0.15102 0.12347 -0.02733 0.01780  -0.00377 85  ARG A C   
644  O O   . ARG A 89  ? 0.13219 0.13764 0.10976 -0.03400 0.00699  0.00001  85  ARG A O   
645  C CB  . ARG A 89  ? 0.12816 0.17463 0.14637 -0.01712 0.02760  -0.00102 85  ARG A CB  
646  C CG  . ARG A 89  ? 0.11483 0.17676 0.13404 -0.02237 0.03799  -0.00261 85  ARG A CG  
647  C CD  . ARG A 89  ? 0.22577 0.31401 0.26382 -0.02401 0.04075  0.00031  85  ARG A CD  
648  N NE  . ARG A 89  ? 0.41123 0.49911 0.44544 -0.03557 0.03100  0.00783  85  ARG A NE  
649  C CZ  . ARG A 89  ? 0.52563 0.63263 0.57604 -0.03816 0.02879  0.01194  85  ARG A CZ  
650  N NH1 . ARG A 89  ? 0.39865 0.52803 0.47207 -0.02903 0.03520  0.00866  85  ARG A NH1 
651  N NH2 . ARG A 89  ? 0.38516 0.48738 0.42865 -0.04975 0.01809  0.01903  85  ARG A NH2 
652  N N   . ALA A 90  ? 0.12128 0.12787 0.09542 -0.02967 0.02375  -0.00721 86  ALA A N   
653  C CA  . ALA A 90  ? 0.17693 0.17057 0.12969 -0.04232 0.01872  -0.00547 86  ALA A CA  
654  C C   . ALA A 90  ? 0.20502 0.20932 0.15281 -0.04699 0.03191  -0.00700 86  ALA A C   
655  O O   . ALA A 90  ? 0.16590 0.16830 0.11455 -0.03883 0.03944  -0.01308 86  ALA A O   
656  C CB  . ALA A 90  ? 0.18988 0.15714 0.12797 -0.04061 0.00798  -0.00984 86  ALA A CB  
657  N N   . GLY A 91  ? 0.22624 0.24259 0.16862 -0.06051 0.03477  -0.00188 87  GLY A N   
658  C CA  . GLY A 91  ? 0.19673 0.22821 0.13423 -0.06614 0.04921  -0.00435 87  GLY A CA  
659  C C   . GLY A 91  ? 0.20700 0.26184 0.16822 -0.05124 0.06250  -0.01119 87  GLY A C   
660  O O   . GLY A 91  ? 0.18464 0.25828 0.16941 -0.04433 0.06339  -0.01025 87  GLY A O   
661  N N   . ASN A 92  ? 0.16973 0.22024 0.12344 -0.04538 0.07086  -0.01860 88  ASN A N   
662  C CA  . ASN A 92  ? 0.16372 0.23212 0.13659 -0.03023 0.08097  -0.02621 88  ASN A CA  
663  C C   . ASN A 92  ? 0.20352 0.25700 0.18491 -0.01464 0.07646  -0.03014 88  ASN A C   
664  O O   . ASN A 92  ? 0.15125 0.20984 0.14273 -0.00138 0.08061  -0.03612 88  ASN A O   
665  C CB  . ASN A 92  ? 0.18431 0.25302 0.14485 -0.02997 0.08803  -0.03101 88  ASN A CB  
666  C CG  . ASN A 92  ? 0.29269 0.38553 0.27365 -0.01686 0.09617  -0.03643 88  ASN A CG  
667  O OD1 . ASN A 92  ? 0.30756 0.42045 0.31158 -0.01210 0.09669  -0.03516 88  ASN A OD1 
668  N ND2 . ASN A 92  ? 0.29607 0.38538 0.26764 -0.01069 0.10154  -0.04287 88  ASN A ND2 
669  N N   . SER A 93  ? 0.14888 0.18248 0.12668 -0.01514 0.06441  -0.02554 89  SER A N   
670  C CA  . SER A 93  ? 0.14479 0.16458 0.12919 -0.00333 0.05966  -0.02793 89  SER A CA  
671  C C   . SER A 93  ? 0.16436 0.18520 0.16025 -0.00200 0.05134  -0.02239 89  SER A C   
672  O O   . SER A 93  ? 0.17394 0.19541 0.16638 -0.01052 0.04511  -0.01716 89  SER A O   
673  C CB  . SER A 93  ? 0.17652 0.17013 0.14319 -0.00469 0.05421  -0.03061 89  SER A CB  
674  O OG  . SER A 93  ? 0.20091 0.19000 0.15408 -0.00526 0.06109  -0.03608 89  SER A OG  
675  N N   . ALA A 94  ? 0.10999 0.12859 0.11695 0.00828  0.05032  -0.02360 90  ALA A N   
676  C CA  . ALA A 94  ? 0.09928 0.11611 0.11355 0.00985  0.04306  -0.01908 90  ALA A CA  
677  C C   . ALA A 94  ? 0.11678 0.11701 0.12767 0.01429  0.04008  -0.02110 90  ALA A C   
678  O O   . ALA A 94  ? 0.14183 0.13549 0.15242 0.02017  0.04335  -0.02492 90  ALA A O   
679  C CB  . ALA A 94  ? 0.13233 0.16521 0.16357 0.01567  0.04396  -0.01684 90  ALA A CB  
680  N N   . TYR A 95  ? 0.09259 0.08692 0.10098 0.01113  0.03364  -0.01908 91  TYR A N   
681  C CA  . TYR A 95  ? 0.09615 0.07923 0.10226 0.01243  0.03149  -0.02109 91  TYR A CA  
682  C C   . TYR A 95  ? 0.11316 0.09970 0.12422 0.01302  0.02847  -0.01724 91  TYR A C   
683  O O   . TYR A 95  ? 0.13154 0.12472 0.14369 0.01084  0.02465  -0.01465 91  TYR A O   
684  C CB  . TYR A 95  ? 0.12714 0.10176 0.12500 0.00784  0.02696  -0.02509 91  TYR A CB  
685  C CG  . TYR A 95  ? 0.17084 0.13787 0.15921 0.00594  0.02845  -0.02840 91  TYR A CG  
686  C CD1 . TYR A 95  ? 0.16702 0.13634 0.14805 0.00060  0.02736  -0.02687 91  TYR A CD1 
687  C CD2 . TYR A 95  ? 0.21124 0.16726 0.19558 0.00817  0.03039  -0.03259 91  TYR A CD2 
688  C CE1 . TYR A 95  ? 0.13538 0.09638 0.10356 -0.00288 0.02906  -0.02946 91  TYR A CE1 
689  C CE2 . TYR A 95  ? 0.20292 0.15039 0.17562 0.00631  0.03117  -0.03567 91  TYR A CE2 
690  C CZ  . TYR A 95  ? 0.23134 0.18112 0.19498 0.00063  0.03124  -0.03431 91  TYR A CZ  
691  O OH  . TYR A 95  ? 0.25545 0.19507 0.20334 -0.00289 0.03261  -0.03718 91  TYR A OH  
692  N N   . PHE A 96  ? 0.09133 0.07124 0.10276 0.01491  0.02930  -0.01664 92  PHE A N   
693  C CA  . PHE A 96  ? 0.09881 0.07954 0.11079 0.01403  0.02695  -0.01234 92  PHE A CA  
694  C C   . PHE A 96  ? 0.14596 0.12110 0.15326 0.00920  0.02732  -0.01399 92  PHE A C   
695  O O   . PHE A 96  ? 0.11464 0.08129 0.12007 0.00839  0.02884  -0.01639 92  PHE A O   
696  C CB  . PHE A 96  ? 0.12484 0.10216 0.14010 0.01931  0.02619  -0.00840 92  PHE A CB  
697  C CG  . PHE A 96  ? 0.16059 0.14921 0.18483 0.02406  0.02620  -0.00766 92  PHE A CG  
698  C CD1 . PHE A 96  ? 0.09240 0.08955 0.12057 0.02328  0.02228  -0.00345 92  PHE A CD1 
699  C CD2 . PHE A 96  ? 0.16871 0.16100 0.19769 0.02882  0.03027  -0.01176 92  PHE A CD2 
700  C CE1 . PHE A 96  ? 0.14212 0.15267 0.18113 0.02624  0.02213  -0.00280 92  PHE A CE1 
701  C CE2 . PHE A 96  ? 0.14894 0.15707 0.18853 0.03192  0.03177  -0.01200 92  PHE A CE2 
702  C CZ  . PHE A 96  ? 0.12016 0.13812 0.16592 0.03014  0.02753  -0.00722 92  PHE A CZ  
703  N N   . PHE A 97  ? 0.12927 0.11041 0.13469 0.00554  0.02603  -0.01319 93  PHE A N   
704  C CA  . PHE A 97  ? 0.09840 0.07912 0.10028 -0.00065 0.02807  -0.01440 93  PHE A CA  
705  C C   . PHE A 97  ? 0.15920 0.12756 0.15510 -0.00299 0.02826  -0.00811 93  PHE A C   
706  O O   . PHE A 97  ? 0.16783 0.12985 0.16237 0.00130  0.02525  -0.00290 93  PHE A O   
707  C CB  . PHE A 97  ? 0.16131 0.15326 0.16113 -0.00352 0.02761  -0.01586 93  PHE A CB  
708  C CG  . PHE A 97  ? 0.16208 0.16304 0.16640 -0.00102 0.02468  -0.02367 93  PHE A CG  
709  C CD1 . PHE A 97  ? 0.15948 0.16131 0.16852 -0.00124 0.02429  -0.03107 93  PHE A CD1 
710  C CD2 . PHE A 97  ? 0.11893 0.12464 0.12166 0.00176  0.02002  -0.02375 93  PHE A CD2 
711  C CE1 . PHE A 97  ? 0.14721 0.15339 0.15888 0.00179  0.01844  -0.03870 93  PHE A CE1 
712  C CE2 . PHE A 97  ? 0.19107 0.20061 0.19569 0.00440  0.01432  -0.03112 93  PHE A CE2 
713  C CZ  . PHE A 97  ? 0.16547 0.17466 0.17435 0.00469  0.01309  -0.03873 93  PHE A CZ  
714  N N   . HIS A 98  ? 0.21064 0.17483 0.20312 -0.01017 0.03031  -0.00883 94  HIS A N   
715  C CA  . HIS A 98  ? 0.16639 0.11447 0.14947 -0.01480 0.02830  -0.00214 94  HIS A CA  
716  C C   . HIS A 98  ? 0.21560 0.16236 0.18929 -0.01831 0.02641  0.00460  94  HIS A C   
717  O O   . HIS A 98  ? 0.21086 0.17036 0.18152 -0.02486 0.03011  0.00339  94  HIS A O   
718  C CB  . HIS A 98  ? 0.14900 0.09508 0.12940 -0.02541 0.03072  -0.00344 94  HIS A CB  
719  C CG  . HIS A 98  ? 0.28730 0.21129 0.25561 -0.03132 0.02627  0.00390  94  HIS A CG  
720  N ND1 . HIS A 98  ? 0.40360 0.32172 0.35820 -0.04274 0.02552  0.01133  94  HIS A ND1 
721  C CD2 . HIS A 98  ? 0.37171 0.27536 0.33708 -0.02762 0.02089  0.00482  94  HIS A CD2 
722  C CE1 . HIS A 98  ? 0.34204 0.23508 0.28525 -0.04658 0.01857  0.01737  94  HIS A CE1 
723  N NE2 . HIS A 98  ? 0.38518 0.26916 0.33552 -0.03655 0.01535  0.01296  94  HIS A NE2 
724  N N   . PRO A 99  ? 0.20071 0.13255 0.16937 -0.01348 0.02004  0.01063  95  PRO A N   
725  C CA  . PRO A 99  ? 0.30418 0.23188 0.26219 -0.01643 0.01616  0.01724  95  PRO A CA  
726  C C   . PRO A 99  ? 0.23413 0.15246 0.17438 -0.03116 0.01690  0.02279  95  PRO A C   
727  O O   . PRO A 99  ? 0.30417 0.20989 0.23871 -0.03792 0.01612  0.02467  95  PRO A O   
728  C CB  . PRO A 99  ? 0.30547 0.21802 0.26515 -0.00618 0.00706  0.02076  95  PRO A CB  
729  C CG  . PRO A 99  ? 0.40337 0.30589 0.36748 -0.00187 0.00633  0.01740  95  PRO A CG  
730  C CD  . PRO A 99  ? 0.26473 0.18330 0.23768 -0.00377 0.01516  0.01028  95  PRO A CD  
731  N N   . ASP A 100 ? 0.36620 0.29034 0.29595 -0.03725 0.01816  0.02561  96  ASP A N   
732  C CA  . ASP A 100 ? 0.42599 0.34421 0.33588 -0.05381 0.02056  0.03109  96  ASP A CA  
733  C C   . ASP A 100 ? 0.40392 0.28997 0.29435 -0.05859 0.00955  0.04190  96  ASP A C   
734  O O   . ASP A 100 ? 0.45489 0.33001 0.32652 -0.07493 0.01015  0.04795  96  ASP A O   
735  C CB  . ASP A 100 ? 0.48160 0.41562 0.38356 -0.05824 0.02545  0.02969  96  ASP A CB  
736  C CG  . ASP A 100 ? 0.72112 0.68494 0.63973 -0.05463 0.03454  0.01779  96  ASP A CG  
737  O OD1 . ASP A 100 ? 0.67663 0.65149 0.60528 -0.05857 0.04054  0.01201  96  ASP A OD1 
738  O OD2 . ASP A 100 ? 0.82416 0.79862 0.74562 -0.04747 0.03386  0.01390  96  ASP A OD2 
739  N N   . ASN A 101 ? 0.31528 0.18604 0.20967 -0.04533 -0.00133 0.04410  97  ASN A N   
740  C CA  . ASN A 101 ? 0.32467 0.16222 0.20077 -0.04729 -0.01537 0.05314  97  ASN A CA  
741  C C   . ASN A 101 ? 0.35929 0.18795 0.25124 -0.02830 -0.02543 0.04999  97  ASN A C   
742  O O   . ASN A 101 ? 0.32321 0.17305 0.23790 -0.01586 -0.02028 0.04229  97  ASN A O   
743  C CB  . ASN A 101 ? 0.34349 0.17127 0.19779 -0.05482 -0.02052 0.06081  97  ASN A CB  
744  C CG  . ASN A 101 ? 0.41331 0.26182 0.27977 -0.04486 -0.01797 0.05649  97  ASN A CG  
745  O OD1 . ASN A 101 ? 0.36451 0.21181 0.24522 -0.03000 -0.02600 0.05487  97  ASN A OD1 
746  N ND2 . ASN A 101 ? 0.38620 0.25477 0.24750 -0.05313 -0.00723 0.05390  97  ASN A ND2 
747  N N   . GLN A 102 ? 0.35198 0.14876 0.23058 -0.02674 -0.04062 0.05571  98  GLN A N   
748  C CA  . GLN A 102 ? 0.44222 0.23048 0.33628 -0.00777 -0.05122 0.05081  98  GLN A CA  
749  C C   . GLN A 102 ? 0.39101 0.19154 0.29891 0.00492  -0.05573 0.04891  98  GLN A C   
750  O O   . GLN A 102 ? 0.36520 0.17787 0.29630 0.02123  -0.05705 0.04121  98  GLN A O   
751  C CB  . GLN A 102 ? 0.51515 0.27927 0.39741 -0.00862 -0.06493 0.05239  98  GLN A CB  
752  C CG  . GLN A 102 ? 0.53455 0.29542 0.43397 0.01110  -0.07520 0.04440  98  GLN A CG  
753  C CD  . GLN A 102 ? 0.49262 0.26663 0.41175 0.02196  -0.06678 0.03532  98  GLN A CD  
754  O OE1 . GLN A 102 ? 0.50917 0.28359 0.42416 0.01340  -0.05794 0.03544  98  GLN A OE1 
755  N NE2 . GLN A 102 ? 0.50977 0.29701 0.45081 0.04015  -0.06890 0.02650  98  GLN A NE2 
756  N N   . GLU A 103 ? 0.45362 0.25237 0.34755 -0.00290 -0.05795 0.05543  99  GLU A N   
757  C CA  . GLU A 103 ? 0.45102 0.26328 0.35898 0.00776  -0.06214 0.05371  99  GLU A CA  
758  C C   . GLU A 103 ? 0.38025 0.22900 0.31322 0.01332  -0.04775 0.04570  99  GLU A C   
759  O O   . GLU A 103 ? 0.26095 0.12480 0.21635 0.02617  -0.04998 0.04072  99  GLU A O   
760  C CB  . GLU A 103 ? 0.47026 0.27485 0.35646 -0.00295 -0.06618 0.06101  99  GLU A CB  
761  C CG  . GLU A 103 ? 0.62608 0.43632 0.52391 0.00765  -0.07624 0.05975  99  GLU A CG  
762  C CD  . GLU A 103 ? 0.81845 0.62407 0.69522 -0.00273 -0.07831 0.06507  99  GLU A CD  
763  O OE1 . GLU A 103 ? 0.76350 0.55066 0.61506 -0.01514 -0.08123 0.06953  99  GLU A OE1 
764  O OE2 . GLU A 103 ? 0.66905 0.48981 0.55415 0.00115  -0.07723 0.06422  99  GLU A OE2 
765  N N   . ASP A 104 ? 0.29069 0.15397 0.22022 0.00326  -0.03373 0.04401  100 ASP A N   
766  C CA  . ASP A 104 ? 0.28506 0.17759 0.23474 0.00774  -0.02258 0.03660  100 ASP A CA  
767  C C   . ASP A 104 ? 0.29400 0.19333 0.26186 0.01701  -0.01906 0.02965  100 ASP A C   
768  O O   . ASP A 104 ? 0.21924 0.13888 0.20547 0.02413  -0.01466 0.02433  100 ASP A O   
769  C CB  . ASP A 104 ? 0.26462 0.16925 0.20593 -0.00396 -0.01105 0.03507  100 ASP A CB  
770  C CG  . ASP A 104 ? 0.56262 0.46780 0.48829 -0.01115 -0.01222 0.03907  100 ASP A CG  
771  O OD1 . ASP A 104 ? 0.43360 0.32961 0.35553 -0.00698 -0.02242 0.04359  100 ASP A OD1 
772  O OD2 . ASP A 104 ? 0.44504 0.36054 0.36248 -0.02046 -0.00330 0.03672  100 ASP A OD2 
773  N N   . ALA A 105 ? 0.30469 0.18624 0.26560 0.01601  -0.02129 0.02972  101 ALA A N   
774  C CA  . ALA A 105 ? 0.31736 0.20284 0.29263 0.02564  -0.01868 0.02229  101 ALA A CA  
775  C C   . ALA A 105 ? 0.34175 0.23329 0.33454 0.04112  -0.02529 0.01807  101 ALA A C   
776  O O   . ALA A 105 ? 0.30228 0.21273 0.31241 0.04892  -0.01863 0.01061  101 ALA A O   
777  C CB  . ALA A 105 ? 0.37408 0.23466 0.33597 0.02179  -0.02293 0.02355  101 ALA A CB  
778  N N   . GLU A 106 ? 0.23695 0.11340 0.22531 0.04522  -0.03870 0.02233  102 GLU A N   
779  C CA  . GLU A 106 ? 0.25472 0.14068 0.26348 0.06058  -0.04611 0.01712  102 GLU A CA  
780  C C   . GLU A 106 ? 0.24402 0.15951 0.26927 0.06093  -0.04019 0.01633  102 GLU A C   
781  O O   . GLU A 106 ? 0.26005 0.19753 0.30833 0.07089  -0.03811 0.00944  102 GLU A O   
782  C CB  . GLU A 106 ? 0.32155 0.18166 0.32025 0.06429  -0.06427 0.02152  102 GLU A CB  
783  C CG  . GLU A 106 ? 0.39256 0.23171 0.38169 0.06603  -0.07068 0.01885  102 GLU A CG  
784  C CD  . GLU A 106 ? 0.71221 0.52472 0.68064 0.05984  -0.08563 0.02543  102 GLU A CD  
785  O OE1 . GLU A 106 ? 0.85290 0.66065 0.80879 0.05079  -0.08825 0.03335  102 GLU A OE1 
786  O OE2 . GLU A 106 ? 0.59120 0.38694 0.55422 0.06359  -0.09530 0.02223  102 GLU A OE2 
787  N N   . ALA A 107 ? 0.22168 0.13852 0.23496 0.04964  -0.03769 0.02288  103 ALA A N   
788  C CA  . ALA A 107 ? 0.26952 0.20971 0.29546 0.04921  -0.03486 0.02284  103 ALA A CA  
789  C C   . ALA A 107 ? 0.20299 0.16800 0.24363 0.04924  -0.02197 0.01656  103 ALA A C   
790  O O   . ALA A 107 ? 0.20123 0.18772 0.26038 0.05321  -0.02093 0.01384  103 ALA A O   
791  C CB  . ALA A 107 ? 0.25136 0.18532 0.25833 0.03790  -0.03525 0.02960  103 ALA A CB  
792  N N   . ILE A 108 ? 0.16651 0.12844 0.19835 0.04367  -0.01280 0.01446  104 ILE A N   
793  C CA  . ILE A 108 ? 0.21951 0.20025 0.26027 0.04210  -0.00233 0.00931  104 ILE A CA  
794  C C   . ILE A 108 ? 0.18991 0.18159 0.24620 0.05123  0.00130  0.00218  104 ILE A C   
795  O O   . ILE A 108 ? 0.16797 0.17681 0.23146 0.04932  0.00929  -0.00152 104 ILE A O   
796  C CB  . ILE A 108 ? 0.23035 0.20453 0.25794 0.03395  0.00478  0.00823  104 ILE A CB  
797  C CG1 . ILE A 108 ? 0.22948 0.18585 0.24972 0.03555  0.00454  0.00672  104 ILE A CG1 
798  C CG2 . ILE A 108 ? 0.20589 0.17631 0.22038 0.02524  0.00346  0.01263  104 ILE A CG2 
799  C CD1 . ILE A 108 ? 0.26718 0.22041 0.27911 0.02814  0.01141  0.00432  104 ILE A CD1 
800  N N   . THR A 109 ? 0.21436 0.19605 0.27468 0.06108  -0.00500 -0.00047 105 THR A N   
801  C CA  . THR A 109 ? 0.19889 0.19535 0.27612 0.07177  -0.00135 -0.00957 105 THR A CA  
802  C C   . THR A 109 ? 0.24762 0.27320 0.34648 0.07466  -0.00023 -0.01158 105 THR A C   
803  O O   . THR A 109 ? 0.18834 0.23506 0.30245 0.08037  0.00675  -0.01969 105 THR A O   
804  C CB  . THR A 109 ? 0.16713 0.14520 0.24466 0.08401  -0.01110 -0.01372 105 THR A CB  
805  O OG1 . THR A 109 ? 0.19212 0.16434 0.27476 0.08927  -0.02461 -0.01027 105 THR A OG1 
806  C CG2 . THR A 109 ? 0.35510 0.30278 0.40997 0.07856  -0.01349 -0.01037 105 THR A CG2 
807  N N   . HIS A 110 ? 0.19733 0.22533 0.29734 0.07005  -0.00676 -0.00467 106 HIS A N   
808  C CA  . HIS A 110 ? 0.17822 0.23356 0.29868 0.07032  -0.00703 -0.00526 106 HIS A CA  
809  C C   . HIS A 110 ? 0.17892 0.24941 0.29679 0.05780  0.00187  -0.00264 106 HIS A C   
810  O O   . HIS A 110 ? 0.18440 0.27723 0.31711 0.05458  0.00174  -0.00181 106 HIS A O   
811  C CB  . HIS A 110 ? 0.13459 0.18207 0.25643 0.07170  -0.02110 0.00097  106 HIS A CB  
812  C CG  . HIS A 110 ? 0.20265 0.23237 0.32602 0.08383  -0.03348 -0.00117 106 HIS A CG  
813  N ND1 . HIS A 110 ? 0.34978 0.39309 0.49095 0.09262  -0.03890 -0.00602 106 HIS A ND1 
814  C CD2 . HIS A 110 ? 0.25912 0.25637 0.36193 0.08501  -0.04056 0.00175  106 HIS A CD2 
815  C CE1 . HIS A 110 ? 0.33445 0.35285 0.46506 0.09881  -0.04934 -0.00629 106 HIS A CE1 
816  N NE2 . HIS A 110 ? 0.22293 0.21268 0.33000 0.09400  -0.05094 -0.00119 106 HIS A NE2 
817  N N   . LEU A 111 ? 0.11285 0.17090 0.21239 0.05035  0.00797  -0.00143 107 LEU A N   
818  C CA  . LEU A 111 ? 0.13860 0.20483 0.23222 0.03905  0.01328  0.00065  107 LEU A CA  
819  C C   . LEU A 111 ? 0.13061 0.20841 0.22621 0.03761  0.02429  -0.00547 107 LEU A C   
820  O O   . LEU A 111 ? 0.13035 0.19872 0.22086 0.04299  0.02861  -0.01058 107 LEU A O   
821  C CB  . LEU A 111 ? 0.10341 0.14949 0.17628 0.03241  0.01141  0.00433  107 LEU A CB  
822  C CG  . LEU A 111 ? 0.09879 0.13650 0.16473 0.02963  0.00228  0.01042  107 LEU A CG  
823  C CD1 . LEU A 111 ? 0.09053 0.11150 0.13773 0.02526  0.00294  0.01084  107 LEU A CD1 
824  C CD2 . LEU A 111 ? 0.10821 0.15887 0.17915 0.02335  -0.00147 0.01353  107 LEU A CD2 
825  N N   . PHE A 112 ? 0.14785 0.24451 0.24865 0.02918  0.02808  -0.00454 108 PHE A N   
826  C CA  . PHE A 112 ? 0.10992 0.21525 0.20607 0.02366  0.03840  -0.00878 108 PHE A CA  
827  C C   . PHE A 112 ? 0.19422 0.31063 0.30120 0.03438  0.04626  -0.01806 108 PHE A C   
828  O O   . PHE A 112 ? 0.17463 0.28366 0.27055 0.03491  0.05312  -0.02302 108 PHE A O   
829  C CB  . PHE A 112 ? 0.08461 0.16706 0.15808 0.01777  0.03858  -0.00787 108 PHE A CB  
830  C CG  . PHE A 112 ? 0.09601 0.16766 0.15881 0.00939  0.03009  -0.00148 108 PHE A CG  
831  C CD1 . PHE A 112 ? 0.08004 0.16306 0.14615 0.00056  0.02598  0.00344  108 PHE A CD1 
832  C CD2 . PHE A 112 ? 0.10040 0.15145 0.15026 0.01035  0.02577  -0.00126 108 PHE A CD2 
833  C CE1 . PHE A 112 ? 0.07953 0.14997 0.13439 -0.00558 0.01624  0.00804  108 PHE A CE1 
834  C CE2 . PHE A 112 ? 0.12984 0.17263 0.17068 0.00479  0.01778  0.00208  108 PHE A CE2 
835  C CZ  . PHE A 112 ? 0.10782 0.15857 0.15028 -0.00237 0.01227  0.00651  108 PHE A CZ  
836  N N   . THR A 113 ? 0.09206 0.22557 0.22080 0.04400  0.04397  -0.02144 109 THR A N   
837  C CA  . THR A 113 ? 0.22997 0.36382 0.36423 0.05642  0.04688  -0.02915 109 THR A CA  
838  C C   . THR A 113 ? 0.28820 0.43930 0.42284 0.05235  0.05848  -0.03359 109 THR A C   
839  O O   . THR A 113 ? 0.39852 0.54581 0.53191 0.06144  0.06170  -0.04031 109 THR A O   
840  C CB  . THR A 113 ? 0.24447 0.38343 0.39681 0.06727  0.03746  -0.02976 109 THR A CB  
841  O OG1 . THR A 113 ? 0.40200 0.56941 0.57265 0.06192  0.03891  -0.02828 109 THR A OG1 
842  C CG2 . THR A 113 ? 0.41212 0.53079 0.56071 0.07004  0.02482  -0.02441 109 THR A CG2 
843  N N   . ASP A 114 ? 0.23559 0.40380 0.37023 0.03832  0.06395  -0.03001 110 ASP A N   
844  C CA  . ASP A 114 ? 0.30219 0.48494 0.43323 0.03202  0.07498  -0.03343 110 ASP A CA  
845  C C   . ASP A 114 ? 0.34423 0.50988 0.44909 0.02452  0.08029  -0.03336 110 ASP A C   
846  O O   . ASP A 114 ? 0.34098 0.51529 0.43747 0.01715  0.08876  -0.03520 110 ASP A O   
847  C CB  . ASP A 114 ? 0.32440 0.53204 0.46622 0.01862  0.07696  -0.02884 110 ASP A CB  
848  C CG  . ASP A 114 ? 0.40883 0.60849 0.53794 0.00315  0.07204  -0.01977 110 ASP A CG  
849  O OD1 . ASP A 114 ? 0.32323 0.50558 0.44662 0.00626  0.06443  -0.01699 110 ASP A OD1 
850  O OD2 . ASP A 114 ? 0.55955 0.76945 0.68304 -0.01249 0.07495  -0.01543 110 ASP A OD2 
851  N N   . VAL A 115 ? 0.27477 0.41637 0.36634 0.02591  0.07499  -0.03161 111 VAL A N   
852  C CA  . VAL A 115 ? 0.29634 0.41913 0.36383 0.02000  0.07793  -0.03245 111 VAL A CA  
853  C C   . VAL A 115 ? 0.20813 0.32080 0.26959 0.03184  0.08120  -0.03973 111 VAL A C   
854  O O   . VAL A 115 ? 0.18439 0.29247 0.25598 0.04534  0.07744  -0.04304 111 VAL A O   
855  C CB  . VAL A 115 ? 0.28675 0.38811 0.34502 0.01687  0.07076  -0.02899 111 VAL A CB  
856  C CG1 . VAL A 115 ? 0.34907 0.42931 0.40633 0.02981  0.06612  -0.03222 111 VAL A CG1 
857  C CG2 . VAL A 115 ? 0.34153 0.42705 0.37607 0.00388  0.07038  -0.02597 111 VAL A CG2 
858  N N   . GLN A 116 ? 0.15046 0.25780 0.19375 0.02622  0.08708  -0.04217 112 GLN A N   
859  C CA  . GLN A 116 ? 0.17808 0.27547 0.21393 0.03714  0.08985  -0.04932 112 GLN A CA  
860  C C   . GLN A 116 ? 0.16354 0.23234 0.18847 0.04391  0.08174  -0.05023 112 GLN A C   
861  O O   . GLN A 116 ? 0.24922 0.30703 0.27451 0.05610  0.08001  -0.05468 112 GLN A O   
862  C CB  . GLN A 116 ? 0.20871 0.30907 0.22700 0.02891  0.09802  -0.05181 112 GLN A CB  
863  C CG  . GLN A 116 ? 0.19847 0.32603 0.22767 0.02889  0.10783  -0.05564 112 GLN A CG  
864  C CD  . GLN A 116 ? 0.26874 0.39492 0.27820 0.02517  0.11602  -0.06027 112 GLN A CD  
865  O OE1 . GLN A 116 ? 0.25197 0.36245 0.23848 0.01459  0.11463  -0.05746 112 GLN A OE1 
866  N NE2 . GLN A 116 ? 0.31420 0.45603 0.33217 0.03382  0.12395  -0.06821 112 GLN A NE2 
867  N N   . ASN A 117 ? 0.15262 0.20724 0.16828 0.03500  0.07662  -0.04627 113 ASN A N   
868  C CA  . ASN A 117 ? 0.15620 0.18429 0.16217 0.03768  0.06892  -0.04712 113 ASN A CA  
869  C C   . ASN A 117 ? 0.17768 0.19874 0.19226 0.03663  0.06255  -0.04162 113 ASN A C   
870  O O   . ASN A 117 ? 0.24287 0.26687 0.25763 0.02757  0.06326  -0.03698 113 ASN A O   
871  C CB  . ASN A 117 ? 0.15834 0.17028 0.14393 0.02767  0.06929  -0.04728 113 ASN A CB  
872  C CG  . ASN A 117 ? 0.21634 0.23481 0.19040 0.02656  0.07621  -0.05197 113 ASN A CG  
873  O OD1 . ASN A 117 ? 0.21155 0.23294 0.18694 0.03762  0.07755  -0.05770 113 ASN A OD1 
874  N ND2 . ASN A 117 ? 0.27092 0.29012 0.23110 0.01295  0.08008  -0.04952 113 ASN A ND2 
875  N N   . ARG A 118 ? 0.15615 0.16640 0.17568 0.04532  0.05604  -0.04223 114 ARG A N   
876  C CA  . ARG A 118 ? 0.18183 0.18267 0.20631 0.04431  0.05043  -0.03649 114 ARG A CA  
877  C C   . ARG A 118 ? 0.18497 0.16240 0.19798 0.04212  0.04479  -0.03577 114 ARG A C   
878  O O   . ARG A 118 ? 0.19044 0.15729 0.19908 0.04712  0.04153  -0.03986 114 ARG A O   
879  C CB  . ARG A 118 ? 0.23616 0.24194 0.27481 0.05419  0.04660  -0.03642 114 ARG A CB  
880  C CG  . ARG A 118 ? 0.36321 0.39547 0.41712 0.05789  0.05049  -0.03789 114 ARG A CG  
881  C CD  . ARG A 118 ? 0.26585 0.29814 0.33327 0.06863  0.04394  -0.03739 114 ARG A CD  
882  N NE  . ARG A 118 ? 0.25812 0.28277 0.32826 0.06517  0.03646  -0.03032 114 ARG A NE  
883  C CZ  . ARG A 118 ? 0.24300 0.28218 0.31992 0.05879  0.03553  -0.02466 114 ARG A CZ  
884  N NH1 . ARG A 118 ? 0.18178 0.24534 0.26778 0.05473  0.04216  -0.02626 114 ARG A NH1 
885  N NH2 . ARG A 118 ? 0.15124 0.17970 0.22412 0.05537  0.02750  -0.01712 114 ARG A NH2 
886  N N   . TYR A 119 ? 0.17474 0.14586 0.18447 0.03471  0.04299  -0.03137 115 TYR A N   
887  C CA  . TYR A 119 ? 0.13126 0.08601 0.13316 0.03064  0.03813  -0.03077 115 TYR A CA  
888  C C   . TYR A 119 ? 0.16517 0.11793 0.17045 0.02727  0.03560  -0.02577 115 TYR A C   
889  O O   . TYR A 119 ? 0.18985 0.15424 0.19903 0.02408  0.03503  -0.02249 115 TYR A O   
890  C CB  . TYR A 119 ? 0.12386 0.07602 0.11708 0.02364  0.03695  -0.03253 115 TYR A CB  
891  C CG  . TYR A 119 ? 0.15732 0.10998 0.14316 0.02475  0.03960  -0.03666 115 TYR A CG  
892  C CD1 . TYR A 119 ? 0.23554 0.17937 0.21663 0.02852  0.03715  -0.04023 115 TYR A CD1 
893  C CD2 . TYR A 119 ? 0.19927 0.16023 0.18120 0.02094  0.04497  -0.03742 115 TYR A CD2 
894  C CE1 . TYR A 119 ? 0.29058 0.23497 0.26350 0.02954  0.04035  -0.04481 115 TYR A CE1 
895  C CE2 . TYR A 119 ? 0.18492 0.14592 0.15682 0.02016  0.04908  -0.04126 115 TYR A CE2 
896  C CZ  . TYR A 119 ? 0.31885 0.27199 0.28637 0.02516  0.04694  -0.04511 115 TYR A CZ  
897  O OH  . TYR A 119 ? 0.30199 0.25549 0.25812 0.02459  0.05147  -0.04953 115 TYR A OH  
898  N N   . THR A 120 ? 0.14099 0.08002 0.14277 0.02613  0.03226  -0.02442 116 THR A N   
899  C CA  . THR A 120 ? 0.12577 0.06484 0.12713 0.01948  0.02960  -0.01938 116 THR A CA  
900  C C   . THR A 120 ? 0.19067 0.12373 0.18807 0.01198  0.02910  -0.02164 116 THR A C   
901  O O   . THR A 120 ? 0.20076 0.11991 0.19371 0.01212  0.02758  -0.02374 116 THR A O   
902  C CB  . THR A 120 ? 0.19966 0.12862 0.19914 0.02176  0.02527  -0.01433 116 THR A CB  
903  O OG1 . THR A 120 ? 0.23410 0.17127 0.24079 0.02980  0.02452  -0.01354 116 THR A OG1 
904  C CG2 . THR A 120 ? 0.15648 0.08561 0.15147 0.01245  0.02372  -0.00870 116 THR A CG2 
905  N N   . PHE A 121 ? 0.16826 0.11249 0.16824 0.00610  0.02957  -0.02227 117 PHE A N   
906  C CA  . PHE A 121 ? 0.17291 0.11739 0.17363 -0.00072 0.02904  -0.02606 117 PHE A CA  
907  C C   . PHE A 121 ? 0.17324 0.11242 0.17088 -0.00824 0.02899  -0.02168 117 PHE A C   
908  O O   . PHE A 121 ? 0.23055 0.16605 0.22366 -0.00890 0.02847  -0.01525 117 PHE A O   
909  C CB  . PHE A 121 ? 0.17613 0.13635 0.18215 -0.00294 0.02864  -0.03015 117 PHE A CB  
910  C CG  . PHE A 121 ? 0.14848 0.10979 0.15415 0.00143  0.02605  -0.03407 117 PHE A CG  
911  C CD1 . PHE A 121 ? 0.19110 0.14512 0.19286 0.00247  0.02226  -0.03634 117 PHE A CD1 
912  C CD2 . PHE A 121 ? 0.12669 0.09669 0.13298 0.00319  0.02452  -0.03283 117 PHE A CD2 
913  C CE1 . PHE A 121 ? 0.25772 0.21218 0.25428 0.00425  0.01741  -0.03634 117 PHE A CE1 
914  C CE2 . PHE A 121 ? 0.23607 0.20434 0.23902 0.00461  0.02065  -0.03521 117 PHE A CE2 
915  C CZ  . PHE A 121 ? 0.19143 0.15169 0.18843 0.00457  0.01701  -0.03612 117 PHE A CZ  
916  N N   . ALA A 122 ? 0.18060 0.11894 0.18001 -0.01523 0.02860  -0.02498 118 ALA A N   
917  C CA  . ALA A 122 ? 0.24891 0.18503 0.24487 -0.02638 0.02911  -0.02058 118 ALA A CA  
918  C C   . ALA A 122 ? 0.30278 0.26038 0.30280 -0.03380 0.03371  -0.02130 118 ALA A C   
919  O O   . ALA A 122 ? 0.27200 0.22981 0.26582 -0.04472 0.03567  -0.01603 118 ALA A O   
920  C CB  . ALA A 122 ? 0.36122 0.28970 0.35882 -0.03245 0.02668  -0.02382 118 ALA A CB  
921  N N   . PHE A 123 ? 0.19364 0.16792 0.20187 -0.02851 0.03482  -0.02793 119 PHE A N   
922  C CA  . PHE A 123 ? 0.20532 0.20136 0.21799 -0.03274 0.03864  -0.03159 119 PHE A CA  
923  C C   . PHE A 123 ? 0.21850 0.21623 0.22533 -0.02738 0.03850  -0.02757 119 PHE A C   
924  O O   . PHE A 123 ? 0.13031 0.11875 0.13545 -0.01887 0.03509  -0.02509 119 PHE A O   
925  C CB  . PHE A 123 ? 0.15771 0.16982 0.18389 -0.02937 0.03692  -0.04381 119 PHE A CB  
926  C CG  . PHE A 123 ? 0.18302 0.18613 0.20989 -0.01867 0.03064  -0.04715 119 PHE A CG  
927  C CD1 . PHE A 123 ? 0.12256 0.12977 0.14784 -0.01209 0.02806  -0.04811 119 PHE A CD1 
928  C CD2 . PHE A 123 ? 0.26141 0.25059 0.28822 -0.01662 0.02671  -0.04903 119 PHE A CD2 
929  C CE1 . PHE A 123 ? 0.23155 0.22945 0.25469 -0.00539 0.02194  -0.04995 119 PHE A CE1 
930  C CE2 . PHE A 123 ? 0.18694 0.16704 0.21050 -0.00927 0.02141  -0.05145 119 PHE A CE2 
931  C CZ  . PHE A 123 ? 0.20607 0.19138 0.22723 -0.00447 0.01866  -0.05005 119 PHE A CZ  
932  N N   . GLY A 124 ? 0.21658 0.22736 0.22000 -0.03330 0.04246  -0.02718 120 GLY A N   
933  C CA  . GLY A 124 ? 0.27499 0.28786 0.27225 -0.02888 0.04135  -0.02429 120 GLY A CA  
934  C C   . GLY A 124 ? 0.22980 0.25738 0.23519 -0.02139 0.03895  -0.03405 120 GLY A C   
935  O O   . GLY A 124 ? 0.27640 0.31287 0.29241 -0.01922 0.03763  -0.04371 120 GLY A O   
936  N N   . GLY A 125 ? 0.18115 0.20890 0.18065 -0.01713 0.03631  -0.03160 121 GLY A N   
937  C CA  . GLY A 125 ? 0.16522 0.20175 0.16911 -0.00970 0.03118  -0.03981 121 GLY A CA  
938  C C   . GLY A 125 ? 0.26220 0.31878 0.26815 -0.01082 0.03394  -0.05023 121 GLY A C   
939  O O   . GLY A 125 ? 0.25069 0.31257 0.25859 -0.00335 0.02770  -0.05802 121 GLY A O   
940  N N   . ASN A 126 ? 0.22244 0.29081 0.22755 -0.02029 0.04275  -0.05127 122 ASN A N   
941  C CA  . ASN A 126 ? 0.15912 0.24845 0.16642 -0.02165 0.04558  -0.06026 122 ASN A CA  
942  C C   . ASN A 126 ? 0.18302 0.28355 0.20797 -0.01548 0.03906  -0.07204 122 ASN A C   
943  O O   . ASN A 126 ? 0.17734 0.27433 0.21190 -0.01537 0.03709  -0.07410 122 ASN A O   
944  C CB  . ASN A 126 ? 0.21283 0.30945 0.21269 -0.03585 0.05540  -0.05539 122 ASN A CB  
945  C CG  . ASN A 126 ? 0.40117 0.49866 0.40959 -0.04404 0.05901  -0.05475 122 ASN A CG  
946  O OD1 . ASN A 126 ? 0.40414 0.51851 0.42453 -0.04652 0.06004  -0.06321 122 ASN A OD1 
947  N ND2 . ASN A 126 ? 0.41303 0.49038 0.41524 -0.04782 0.05927  -0.04455 122 ASN A ND2 
948  N N   . TYR A 127 ? 0.21166 0.25824 0.24693 -0.00117 0.02523  0.03400  123 TYR A N   
949  C CA  . TYR A 127 ? 0.13205 0.18599 0.17875 -0.00566 0.02217  0.02594  123 TYR A CA  
950  C C   . TYR A 127 ? 0.13727 0.18784 0.19741 -0.01197 0.02665  0.02264  123 TYR A C   
951  O O   . TYR A 127 ? 0.13255 0.18809 0.20362 -0.01508 0.02096  0.01583  123 TYR A O   
952  C CB  . TYR A 127 ? 0.09656 0.15968 0.14165 -0.00508 0.02331  0.02439  123 TYR A CB  
953  C CG  . TYR A 127 ? 0.29890 0.36761 0.33488 -0.00110 0.01724  0.02375  123 TYR A CG  
954  C CD1 . TYR A 127 ? 0.22087 0.29044 0.25867 -0.00007 0.00993  0.02108  123 TYR A CD1 
955  C CD2 . TYR A 127 ? 0.24893 0.32174 0.27381 0.00079  0.01938  0.02517  123 TYR A CD2 
956  C CE1 . TYR A 127 ? 0.21482 0.28949 0.24730 0.00206  0.00566  0.01974  123 TYR A CE1 
957  C CE2 . TYR A 127 ? 0.15703 0.23590 0.17564 0.00291  0.01343  0.02270  123 TYR A CE2 
958  C CZ  . TYR A 127 ? 0.16303 0.24296 0.18729 0.00321  0.00695  0.01995  123 TYR A CZ  
959  O OH  . TYR A 127 ? 0.22355 0.30949 0.24442 0.00390  0.00225  0.01680  123 TYR A OH  
960  N N   . ASP A 128 ? 0.17316 0.21566 0.23301 -0.01414 0.03663  0.02742  124 ASP A N   
961  C CA  . ASP A 128 ? 0.21450 0.25495 0.29064 -0.02194 0.04239  0.02318  124 ASP A CA  
962  C C   . ASP A 128 ? 0.21440 0.25111 0.29804 -0.02556 0.03608  0.01645  124 ASP A C   
963  O O   . ASP A 128 ? 0.16689 0.21227 0.26557 -0.03072 0.03111  0.00821  124 ASP A O   
964  C CB  . ASP A 128 ? 0.20305 0.23071 0.27526 -0.02384 0.05594  0.03089  124 ASP A CB  
965  C CG  . ASP A 128 ? 0.52681 0.55848 0.59048 -0.02205 0.06363  0.03618  124 ASP A CG  
966  O OD1 . ASP A 128 ? 0.47204 0.51580 0.53216 -0.01879 0.05801  0.03323  124 ASP A OD1 
967  O OD2 . ASP A 128 ? 0.65887 0.68000 0.71812 -0.02419 0.07627  0.04311  124 ASP A OD2 
968  N N   . ARG A 129 ? 0.20644 0.23108 0.27956 -0.02244 0.03574  0.01937  125 ARG A N   
969  C CA  . ARG A 129 ? 0.20539 0.22431 0.28210 -0.02629 0.03135  0.01182  125 ARG A CA  
970  C C   . ARG A 129 ? 0.15383 0.18182 0.22605 -0.02391 0.01933  0.00675  125 ARG A C   
971  O O   . ARG A 129 ? 0.11532 0.14497 0.19204 -0.02860 0.01305  -0.00147 125 ARG A O   
972  C CB  . ARG A 129 ? 0.23828 0.23923 0.30662 -0.02348 0.03759  0.01598  125 ARG A CB  
973  C CG  . ARG A 129 ? 0.30705 0.29885 0.37777 -0.02868 0.03583  0.00642  125 ARG A CG  
974  C CD  . ARG A 129 ? 0.36622 0.36098 0.45298 -0.03980 0.03573  -0.00311 125 ARG A CD  
975  N NE  . ARG A 129 ? 0.53565 0.52103 0.62257 -0.04583 0.03366  -0.01386 125 ARG A NE  
976  C CZ  . ARG A 129 ? 0.43221 0.42268 0.53199 -0.05601 0.02941  -0.02536 125 ARG A CZ  
977  N NH1 . ARG A 129 ? 0.36683 0.37315 0.48404 -0.06091 0.02702  -0.02734 125 ARG A NH1 
978  N NH2 . ARG A 129 ? 0.42146 0.40190 0.51740 -0.06149 0.02746  -0.03607 125 ARG A NH2 
979  N N   . LEU A 130 ? 0.11341 0.14687 0.17608 -0.01714 0.01596  0.01137  126 LEU A N   
980  C CA  . LEU A 130 ? 0.13758 0.17694 0.19542 -0.01526 0.00655  0.00778  126 LEU A CA  
981  C C   . LEU A 130 ? 0.11281 0.16334 0.18133 -0.01821 -0.00028 0.00265  126 LEU A C   
982  O O   . LEU A 130 ? 0.08586 0.13785 0.15248 -0.01927 -0.00854 -0.00201 126 LEU A O   
983  C CB  . LEU A 130 ? 0.08742 0.13071 0.13651 -0.00893 0.00557  0.01296  126 LEU A CB  
984  C CG  . LEU A 130 ? 0.17257 0.20902 0.21355 -0.00434 0.00933  0.01762  126 LEU A CG  
985  C CD1 . LEU A 130 ? 0.18960 0.23444 0.22620 0.00038  0.00685  0.02095  126 LEU A CD1 
986  C CD2 . LEU A 130 ? 0.20557 0.23339 0.24207 -0.00525 0.00878  0.01342  126 LEU A CD2 
987  N N   . GLU A 131 ? 0.10352 0.16213 0.18289 -0.01887 0.00322  0.00370  127 GLU A N   
988  C CA  . GLU A 131 ? 0.09172 0.16259 0.18658 -0.02071 -0.00236 -0.00125 127 GLU A CA  
989  C C   . GLU A 131 ? 0.08288 0.15542 0.18941 -0.02739 -0.00643 -0.00831 127 GLU A C   
990  O O   . GLU A 131 ? 0.08250 0.16420 0.19624 -0.02758 -0.01702 -0.01299 127 GLU A O   
991  C CB  . GLU A 131 ? 0.07312 0.15147 0.17893 -0.02073 0.00555  0.00026  127 GLU A CB  
992  C CG  . GLU A 131 ? 0.06784 0.14786 0.16379 -0.01481 0.00690  0.00400  127 GLU A CG  
993  C CD  . GLU A 131 ? 0.18885 0.27307 0.28970 -0.01537 0.01731  0.00512  127 GLU A CD  
994  O OE1 . GLU A 131 ? 0.08893 0.17020 0.19442 -0.01979 0.02616  0.00646  127 GLU A OE1 
995  O OE2 . GLU A 131 ? 0.16195 0.25096 0.26121 -0.01182 0.01786  0.00433  127 GLU A OE2 
996  N N   . GLN A 132 ? 0.10707 0.17059 0.21582 -0.03292 0.00149  -0.00928 128 GLN A N   
997  C CA  . GLN A 132 ? 0.10179 0.16593 0.22203 -0.04104 -0.00198 -0.01806 128 GLN A CA  
998  C C   . GLN A 132 ? 0.15125 0.21031 0.25669 -0.04063 -0.01237 -0.02277 128 GLN A C   
999  O O   . GLN A 132 ? 0.11648 0.18411 0.22863 -0.04445 -0.02314 -0.03059 128 GLN A O   
1000 C CB  . GLN A 132 ? 0.12460 0.17592 0.24944 -0.04729 0.01111  -0.01768 128 GLN A CB  
1001 C CG  . GLN A 132 ? 0.15318 0.21046 0.29436 -0.05015 0.02187  -0.01465 128 GLN A CG  
1002 C CD  . GLN A 132 ? 0.24296 0.28306 0.38290 -0.05431 0.03717  -0.01010 128 GLN A CD  
1003 O OE1 . GLN A 132 ? 0.32474 0.34841 0.45530 -0.05537 0.03947  -0.01038 128 GLN A OE1 
1004 N NE2 . GLN A 132 ? 0.19534 0.23756 0.34396 -0.05627 0.04897  -0.00546 128 GLN A NE2 
1005 N N   . LEU A 133 ? 0.12058 0.16681 0.20572 -0.03586 -0.00945 -0.01828 129 LEU A N   
1006 C CA  . LEU A 133 ? 0.11805 0.15827 0.18646 -0.03534 -0.01681 -0.02253 129 LEU A CA  
1007 C C   . LEU A 133 ? 0.12720 0.17773 0.19018 -0.03079 -0.02871 -0.02137 129 LEU A C   
1008 O O   . LEU A 133 ? 0.19873 0.24970 0.25260 -0.03233 -0.03853 -0.02663 129 LEU A O   
1009 C CB  . LEU A 133 ? 0.16068 0.18638 0.21269 -0.03081 -0.00876 -0.01782 129 LEU A CB  
1010 C CG  . LEU A 133 ? 0.28710 0.29842 0.34185 -0.03348 0.00280  -0.01814 129 LEU A CG  
1011 C CD1 . LEU A 133 ? 0.27621 0.27852 0.32047 -0.02577 0.01024  -0.01044 129 LEU A CD1 
1012 C CD2 . LEU A 133 ? 0.21743 0.21946 0.26966 -0.04100 0.00149  -0.02951 129 LEU A CD2 
1013 N N   . ALA A 134 ? 0.11993 0.17744 0.18687 -0.02504 -0.02783 -0.01449 130 ALA A N   
1014 C CA  . ALA A 134 ? 0.11027 0.17446 0.17315 -0.01994 -0.03742 -0.01219 130 ALA A CA  
1015 C C   . ALA A 134 ? 0.13961 0.21835 0.21981 -0.02121 -0.04783 -0.01651 130 ALA A C   
1016 O O   . ALA A 134 ? 0.14629 0.22883 0.22110 -0.01691 -0.05859 -0.01516 130 ALA A O   
1017 C CB  . ALA A 134 ? 0.08581 0.15147 0.14907 -0.01415 -0.03222 -0.00516 130 ALA A CB  
1018 N N   . GLY A 135 ? 0.13272 0.21979 0.23448 -0.02676 -0.04468 -0.02122 131 GLY A N   
1019 C CA  . GLY A 135 ? 0.09721 0.20215 0.22188 -0.02759 -0.05388 -0.02563 131 GLY A CA  
1020 C C   . GLY A 135 ? 0.10241 0.21746 0.24096 -0.02063 -0.05280 -0.02076 131 GLY A C   
1021 O O   . GLY A 135 ? 0.10060 0.22647 0.24951 -0.01762 -0.05962 -0.02123 131 GLY A O   
1022 N N   . ASN A 136 ? 0.11123 0.21884 0.24266 -0.01737 -0.04156 -0.01495 132 ASN A N   
1023 C CA  . ASN A 136 ? 0.11543 0.22995 0.25758 -0.01127 -0.03871 -0.01188 132 ASN A CA  
1024 C C   . ASN A 136 ? 0.08669 0.19467 0.22316 -0.01181 -0.02420 -0.00873 132 ASN A C   
1025 O O   . ASN A 136 ? 0.06481 0.16080 0.18228 -0.01275 -0.01982 -0.00561 132 ASN A O   
1026 C CB  . ASN A 136 ? 0.15000 0.25998 0.27941 -0.00332 -0.04681 -0.00721 132 ASN A CB  
1027 C CG  . ASN A 136 ? 0.21811 0.33638 0.35480 0.00079  -0.05843 -0.00771 132 ASN A CG  
1028 O OD1 . ASN A 136 ? 0.33869 0.45176 0.45994 0.00388  -0.06861 -0.00507 132 ASN A OD1 
1029 N ND2 . ASN A 136 ? 0.17464 0.30454 0.33172 0.00110  -0.05572 -0.01022 132 ASN A ND2 
1030 N N   . LEU A 137 ? 0.08030 0.19690 0.23309 -0.01064 -0.01704 -0.00968 133 LEU A N   
1031 C CA  . LEU A 137 ? 0.08188 0.19307 0.22572 -0.01006 -0.00462 -0.00687 133 LEU A CA  
1032 C C   . LEU A 137 ? 0.12831 0.23289 0.25647 -0.00411 -0.00677 -0.00397 133 LEU A C   
1033 O O   . LEU A 137 ? 0.08969 0.19445 0.21881 0.00035  -0.01547 -0.00368 133 LEU A O   
1034 C CB  . LEU A 137 ? 0.06207 0.18389 0.22651 -0.01094 0.00507  -0.00998 133 LEU A CB  
1035 C CG  . LEU A 137 ? 0.06500 0.19069 0.24285 -0.01821 0.01141  -0.01243 133 LEU A CG  
1036 C CD1 . LEU A 137 ? 0.18136 0.31417 0.37267 -0.01756 0.01991  -0.01489 133 LEU A CD1 
1037 C CD2 . LEU A 137 ? 0.14750 0.26187 0.31144 -0.02320 0.02139  -0.00841 133 LEU A CD2 
1038 N N   . ARG A 138 ? 0.06370 0.16219 0.17730 -0.00428 0.00129  -0.00168 134 ARG A N   
1039 C CA  . ARG A 138 ? 0.08322 0.17678 0.18443 -0.00048 0.00043  -0.00082 134 ARG A CA  
1040 C C   . ARG A 138 ? 0.08075 0.17843 0.19471 0.00378  -0.00004 -0.00418 134 ARG A C   
1041 O O   . ARG A 138 ? 0.10631 0.19830 0.21494 0.00712  -0.00422 -0.00362 134 ARG A O   
1042 C CB  . ARG A 138 ? 0.12178 0.21248 0.20865 -0.00164 0.00848  0.00052  134 ARG A CB  
1043 C CG  . ARG A 138 ? 0.11571 0.20012 0.18680 -0.00254 0.00683  0.00514  134 ARG A CG  
1044 C CD  . ARG A 138 ? 0.10750 0.19149 0.16601 -0.00270 0.01366  0.00752  134 ARG A CD  
1045 N NE  . ARG A 138 ? 0.07426 0.15802 0.13619 -0.00523 0.02182  0.00962  134 ARG A NE  
1046 C CZ  . ARG A 138 ? 0.13953 0.22270 0.19107 -0.00545 0.02999  0.01192  134 ARG A CZ  
1047 N NH1 . ARG A 138 ? 0.10651 0.19111 0.14335 -0.00332 0.02955  0.01114  134 ARG A NH1 
1048 N NH2 . ARG A 138 ? 0.15611 0.23682 0.21116 -0.00845 0.03905  0.01480  134 ARG A NH2 
1049 N N   . GLU A 139 ? 0.05829 0.16499 0.19061 0.00383  0.00560  -0.00770 135 GLU A N   
1050 C CA  . GLU A 139 ? 0.06063 0.17097 0.20771 0.00914  0.00677  -0.01128 135 GLU A CA  
1051 C C   . GLU A 139 ? 0.06060 0.17301 0.21974 0.01442  -0.00531 -0.00954 135 GLU A C   
1052 O O   . GLU A 139 ? 0.06877 0.18214 0.24069 0.02065  -0.00549 -0.01104 135 GLU A O   
1053 C CB  . GLU A 139 ? 0.06362 0.18436 0.22957 0.00812  0.01775  -0.01595 135 GLU A CB  
1054 C CG  . GLU A 139 ? 0.14932 0.27800 0.32904 0.00462  0.01559  -0.01558 135 GLU A CG  
1055 C CD  . GLU A 139 ? 0.34483 0.47747 0.53073 0.00064  0.02955  -0.01816 135 GLU A CD  
1056 O OE1 . GLU A 139 ? 0.37000 0.49827 0.54204 -0.00238 0.04041  -0.01765 135 GLU A OE1 
1057 O OE2 . GLU A 139 ? 0.23121 0.37140 0.43483 0.00062  0.02990  -0.02046 135 GLU A OE2 
1058 N N   . ASN A 140 ? 0.05933 0.17147 0.21349 0.01264  -0.01527 -0.00636 136 ASN A N   
1059 C CA  . ASN A 140 ? 0.06445 0.17728 0.22309 0.01783  -0.02815 -0.00363 136 ASN A CA  
1060 C C   . ASN A 140 ? 0.14736 0.24694 0.28160 0.01773  -0.03472 0.00140  136 ASN A C   
1061 O O   . ASN A 140 ? 0.10537 0.20417 0.23635 0.02049  -0.04596 0.00446  136 ASN A O   
1062 C CB  . ASN A 140 ? 0.09115 0.21374 0.25898 0.01506  -0.03354 -0.00546 136 ASN A CB  
1063 C CG  . ASN A 140 ? 0.09304 0.22610 0.28113 0.01446  -0.02535 -0.00971 136 ASN A CG  
1064 O OD1 . ASN A 140 ? 0.16462 0.30254 0.35811 0.00771  -0.01870 -0.01260 136 ASN A OD1 
1065 N ND2 . ASN A 140 ? 0.07642 0.21180 0.27635 0.02165  -0.02495 -0.00988 136 ASN A ND2 
1066 N N   . ILE A 141 ? 0.06583 0.15554 0.18212 0.01457  -0.02778 0.00224  137 ILE A N   
1067 C CA  . ILE A 141 ? 0.07549 0.15316 0.17048 0.01379  -0.03091 0.00637  137 ILE A CA  
1068 C C   . ILE A 141 ? 0.13523 0.20371 0.22469 0.01586  -0.02582 0.00709  137 ILE A C   
1069 O O   . ILE A 141 ? 0.07719 0.14636 0.16535 0.01323  -0.01791 0.00370  137 ILE A O   
1070 C CB  . ILE A 141 ? 0.09311 0.16899 0.17565 0.00789  -0.02742 0.00608  137 ILE A CB  
1071 C CG1 . ILE A 141 ? 0.06644 0.14805 0.15399 0.00483  -0.03215 0.00432  137 ILE A CG1 
1072 C CG2 . ILE A 141 ? 0.10288 0.16767 0.16667 0.00730  -0.02765 0.00941  137 ILE A CG2 
1073 C CD1 . ILE A 141 ? 0.08189 0.16068 0.16178 -0.00034 -0.02635 0.00368  137 ILE A CD1 
1074 N N   . GLU A 142 ? 0.08340 0.14252 0.16868 0.02027  -0.03035 0.01140  138 GLU A N   
1075 C CA  . GLU A 142 ? 0.08937 0.13784 0.17270 0.02168  -0.02467 0.01137  138 GLU A CA  
1076 C C   . GLU A 142 ? 0.09335 0.13544 0.16158 0.01568  -0.01954 0.01093  138 GLU A C   
1077 O O   . GLU A 142 ? 0.08699 0.12770 0.14324 0.01291  -0.02164 0.01374  138 GLU A O   
1078 C CB  . GLU A 142 ? 0.13344 0.17087 0.21613 0.02851  -0.03008 0.01786  138 GLU A CB  
1079 C CG  . GLU A 142 ? 0.10858 0.15365 0.21148 0.03642  -0.03519 0.01810  138 GLU A CG  
1080 C CD  . GLU A 142 ? 0.35640 0.39393 0.45506 0.04423  -0.04551 0.02709  138 GLU A CD  
1081 O OE1 . GLU A 142 ? 0.44658 0.47900 0.52562 0.04219  -0.05130 0.03207  138 GLU A OE1 
1082 O OE2 . GLU A 142 ? 0.37749 0.41363 0.49145 0.05299  -0.04758 0.02940  138 GLU A OE2 
1083 N N   . LEU A 143 ? 0.08837 0.12730 0.15869 0.01361  -0.01261 0.00635  139 LEU A N   
1084 C CA  . LEU A 143 ? 0.08745 0.12363 0.14860 0.00774  -0.00834 0.00443  139 LEU A CA  
1085 C C   . LEU A 143 ? 0.11771 0.13975 0.17868 0.00713  -0.00435 0.00445  139 LEU A C   
1086 O O   . LEU A 143 ? 0.14620 0.16034 0.21491 0.01154  -0.00317 0.00435  139 LEU A O   
1087 C CB  . LEU A 143 ? 0.07976 0.12662 0.14243 0.00408  -0.00442 -0.00254 139 LEU A CB  
1088 C CG  . LEU A 143 ? 0.07067 0.12857 0.13332 0.00438  -0.00600 -0.00170 139 LEU A CG  
1089 C CD1 . LEU A 143 ? 0.09489 0.16072 0.15594 0.00199  -0.00142 -0.00722 139 LEU A CD1 
1090 C CD2 . LEU A 143 ? 0.06665 0.12507 0.12076 0.00278  -0.00904 0.00305  139 LEU A CD2 
1091 N N   . GLY A 144 ? 0.12076 0.13934 0.17491 0.00162  -0.00132 0.00444  140 GLY A N   
1092 C CA  . GLY A 144 ? 0.15687 0.16114 0.21169 -0.00116 0.00434  0.00403  140 GLY A CA  
1093 C C   . GLY A 144 ? 0.18585 0.18369 0.23140 -0.00487 0.00663  0.00945  140 GLY A C   
1094 O O   . GLY A 144 ? 0.13806 0.14340 0.17664 -0.00504 0.00382  0.01232  140 GLY A O   
1095 N N   . ASN A 145 ? 0.16851 0.15106 0.21430 -0.00812 0.01333  0.01058  141 ASN A N   
1096 C CA  . ASN A 145 ? 0.15673 0.13280 0.19475 -0.01284 0.01852  0.01517  141 ASN A CA  
1097 C C   . ASN A 145 ? 0.15478 0.12234 0.17623 -0.00717 0.01500  0.02612  141 ASN A C   
1098 O O   . ASN A 145 ? 0.15455 0.12470 0.16689 -0.00966 0.01688  0.02852  141 ASN A O   
1099 C CB  . ASN A 145 ? 0.23168 0.19110 0.27457 -0.01848 0.02823  0.01410  141 ASN A CB  
1100 C CG  . ASN A 145 ? 0.25407 0.21263 0.29567 -0.02652 0.03633  0.01483  141 ASN A CG  
1101 O OD1 . ASN A 145 ? 0.16156 0.13866 0.21145 -0.03173 0.03611  0.00788  141 ASN A OD1 
1102 N ND2 . ASN A 145 ? 0.22443 0.16157 0.25616 -0.02713 0.04402  0.02374  141 ASN A ND2 
1103 N N   . GLY A 146 ? 0.21239 0.17016 0.22986 0.00070  0.00977  0.03233  142 GLY A N   
1104 C CA  . GLY A 146 ? 0.21702 0.16852 0.21746 0.00658  0.00353  0.04196  142 GLY A CA  
1105 C C   . GLY A 146 ? 0.17446 0.14283 0.17105 0.00671  -0.00337 0.03918  142 GLY A C   
1106 O O   . GLY A 146 ? 0.24457 0.21039 0.22535 0.00539  -0.00307 0.04256  142 GLY A O   
1107 N N   . PRO A 147 ? 0.14582 0.12998 0.15617 0.00810  -0.00843 0.03274  143 PRO A N   
1108 C CA  . PRO A 147 ? 0.17543 0.17377 0.18408 0.00713  -0.01299 0.02966  143 PRO A CA  
1109 C C   . PRO A 147 ? 0.12156 0.12421 0.12642 0.00116  -0.00669 0.02684  143 PRO A C   
1110 O O   . PRO A 147 ? 0.12218 0.12667 0.11740 0.00082  -0.00819 0.02758  143 PRO A O   
1111 C CB  . PRO A 147 ? 0.15127 0.16303 0.17682 0.00844  -0.01545 0.02346  143 PRO A CB  
1112 C CG  . PRO A 147 ? 0.14733 0.15177 0.18064 0.01363  -0.01668 0.02534  143 PRO A CG  
1113 C CD  . PRO A 147 ? 0.17721 0.16420 0.20335 0.01205  -0.01027 0.02943  143 PRO A CD  
1114 N N   . LEU A 148 ? 0.12340 0.12854 0.13714 -0.00347 0.00013  0.02274  144 LEU A N   
1115 C CA  . LEU A 148 ? 0.11074 0.12316 0.12543 -0.00808 0.00535  0.02009  144 LEU A CA  
1116 C C   . LEU A 148 ? 0.12660 0.12738 0.12747 -0.00971 0.01123  0.02514  144 LEU A C   
1117 O O   . LEU A 148 ? 0.13679 0.14178 0.13299 -0.01046 0.01351  0.02455  144 LEU A O   
1118 C CB  . LEU A 148 ? 0.12186 0.14162 0.15073 -0.01302 0.00965  0.01385  144 LEU A CB  
1119 C CG  . LEU A 148 ? 0.14858 0.18252 0.18545 -0.01665 0.01253  0.00984  144 LEU A CG  
1120 C CD1 . LEU A 148 ? 0.08503 0.12911 0.11983 -0.01267 0.00800  0.01039  144 LEU A CD1 
1121 C CD2 . LEU A 148 ? 0.10475 0.14925 0.15559 -0.02099 0.01253  0.00220  144 LEU A CD2 
1122 N N   . GLU A 149 ? 0.14521 0.12959 0.13838 -0.00992 0.01488  0.03044  145 GLU A N   
1123 C CA  . GLU A 149 ? 0.16634 0.13643 0.14130 -0.01118 0.02151  0.03674  145 GLU A CA  
1124 C C   . GLU A 149 ? 0.17210 0.14122 0.12882 -0.00719 0.01527  0.03926  145 GLU A C   
1125 O O   . GLU A 149 ? 0.19504 0.16216 0.14060 -0.00939 0.02125  0.03909  145 GLU A O   
1126 C CB  . GLU A 149 ? 0.18955 0.13918 0.15627 -0.01012 0.02476  0.04433  145 GLU A CB  
1127 C CG  . GLU A 149 ? 0.27143 0.20271 0.21217 -0.00966 0.03017  0.05347  145 GLU A CG  
1128 C CD  . GLU A 149 ? 0.26873 0.19168 0.21088 -0.01760 0.04639  0.05403  145 GLU A CD  
1129 O OE1 . GLU A 149 ? 0.32757 0.25903 0.29301 -0.02338 0.05161  0.04714  145 GLU A OE1 
1130 O OE2 . GLU A 149 ? 0.33060 0.23923 0.25066 -0.01858 0.05417  0.06071  145 GLU A OE2 
1131 N N   . GLU A 150 ? 0.17401 0.14496 0.12877 -0.00168 0.00364  0.04053  146 GLU A N   
1132 C CA  . GLU A 150 ? 0.19195 0.16380 0.13158 0.00094  -0.00397 0.04085  146 GLU A CA  
1133 C C   . GLU A 150 ? 0.17430 0.15963 0.12202 -0.00155 -0.00308 0.03326  146 GLU A C   
1134 O O   . GLU A 150 ? 0.17127 0.15387 0.10488 -0.00244 -0.00229 0.03169  146 GLU A O   
1135 C CB  . GLU A 150 ? 0.18106 0.15523 0.12302 0.00698  -0.01710 0.04305  146 GLU A CB  
1136 C CG  . GLU A 150 ? 0.22167 0.18114 0.15676 0.01169  -0.01866 0.05201  146 GLU A CG  
1137 C CD  . GLU A 150 ? 0.39155 0.35772 0.34212 0.01834  -0.02930 0.05257  146 GLU A CD  
1138 O OE1 . GLU A 150 ? 0.34711 0.32917 0.30975 0.01888  -0.03658 0.04655  146 GLU A OE1 
1139 O OE2 . GLU A 150 ? 0.39733 0.35220 0.34954 0.02308  -0.02913 0.05903  146 GLU A OE2 
1140 N N   . ALA A 151 ? 0.13661 0.13497 0.10539 -0.00241 -0.00275 0.02861  147 ALA A N   
1141 C CA  . ALA A 151 ? 0.14557 0.15486 0.12203 -0.00351 -0.00167 0.02339  147 ALA A CA  
1142 C C   . ALA A 151 ? 0.18300 0.19060 0.15585 -0.00613 0.00836  0.02231  147 ALA A C   
1143 O O   . ALA A 151 ? 0.17408 0.18290 0.14357 -0.00590 0.01005  0.01947  147 ALA A O   
1144 C CB  . ALA A 151 ? 0.14655 0.16872 0.14243 -0.00338 -0.00293 0.02023  147 ALA A CB  
1145 N N   . ILE A 152 ? 0.13202 0.13667 0.10775 -0.00885 0.01616  0.02390  148 ILE A N   
1146 C CA  . ILE A 152 ? 0.16321 0.16837 0.13982 -0.01152 0.02720  0.02249  148 ILE A CA  
1147 C C   . ILE A 152 ? 0.17701 0.16851 0.12975 -0.01145 0.03147  0.02415  148 ILE A C   
1148 O O   . ILE A 152 ? 0.16159 0.15459 0.11302 -0.01148 0.03779  0.02066  148 ILE A O   
1149 C CB  . ILE A 152 ? 0.17551 0.18073 0.16265 -0.01599 0.03517  0.02316  148 ILE A CB  
1150 C CG1 . ILE A 152 ? 0.11918 0.14171 0.13036 -0.01691 0.03154  0.01844  148 ILE A CG1 
1151 C CG2 . ILE A 152 ? 0.15573 0.15784 0.14067 -0.01936 0.04881  0.02293  148 ILE A CG2 
1152 C CD1 . ILE A 152 ? 0.12239 0.14370 0.14415 -0.02216 0.03559  0.01736  148 ILE A CD1 
1153 N N   . SER A 153 ? 0.17788 0.15528 0.11036 -0.01079 0.02807  0.02943  149 SER A N   
1154 C CA  . SER A 153 ? 0.20383 0.16759 0.10810 -0.01074 0.03058  0.03091  149 SER A CA  
1155 C C   . SER A 153 ? 0.20112 0.16890 0.10027 -0.00911 0.02331  0.02498  149 SER A C   
1156 O O   . SER A 153 ? 0.21595 0.17764 0.10059 -0.01038 0.02978  0.02118  149 SER A O   
1157 C CB  . SER A 153 ? 0.25769 0.20646 0.14036 -0.00881 0.02524  0.03918  149 SER A CB  
1158 O OG  . SER A 153 ? 0.24712 0.18669 0.13082 -0.01130 0.03541  0.04502  149 SER A OG  
1159 N N   . ALA A 154 ? 0.20959 0.18662 0.12089 -0.00691 0.01122  0.02337  150 ALA A N   
1160 C CA  . ALA A 154 ? 0.27126 0.25157 0.18067 -0.00676 0.00496  0.01722  150 ALA A CA  
1161 C C   . ALA A 154 ? 0.21762 0.20221 0.13813 -0.00765 0.01431  0.01167  150 ALA A C   
1162 O O   . ALA A 154 ? 0.18757 0.16575 0.09640 -0.00878 0.01744  0.00629  150 ALA A O   
1163 C CB  . ALA A 154 ? 0.22807 0.21875 0.15318 -0.00496 -0.00714 0.01680  150 ALA A CB  
1164 N N   . LEU A 155 ? 0.15424 0.14945 0.09726 -0.00673 0.01849  0.01263  151 LEU A N   
1165 C CA  . LEU A 155 ? 0.16065 0.16100 0.11638 -0.00562 0.02664  0.00915  151 LEU A CA  
1166 C C   . LEU A 155 ? 0.16577 0.15771 0.11040 -0.00674 0.03936  0.00715  151 LEU A C   
1167 O O   . LEU A 155 ? 0.17412 0.16312 0.11892 -0.00554 0.04565  0.00234  151 LEU A O   
1168 C CB  . LEU A 155 ? 0.16463 0.17943 0.14420 -0.00410 0.02719  0.01127  151 LEU A CB  
1169 C CG  . LEU A 155 ? 0.23011 0.25444 0.22395 -0.00153 0.02041  0.01122  151 LEU A CG  
1170 C CD1 . LEU A 155 ? 0.27830 0.30051 0.26660 -0.00250 0.01071  0.01160  151 LEU A CD1 
1171 C CD2 . LEU A 155 ? 0.25970 0.29825 0.27177 -0.00031 0.02005  0.01299  151 LEU A CD2 
1172 N N   . TYR A 156 ? 0.17726 0.16377 0.11237 -0.00906 0.04490  0.01072  152 TYR A N   
1173 C CA  . TYR A 156 ? 0.23001 0.20843 0.15449 -0.01075 0.05965  0.00899  152 TYR A CA  
1174 C C   . TYR A 156 ? 0.27454 0.23817 0.17053 -0.01144 0.06059  0.00451  152 TYR A C   
1175 O O   . TYR A 156 ? 0.23467 0.19428 0.12835 -0.01113 0.07162  -0.00131 152 TYR A O   
1176 C CB  . TYR A 156 ? 0.20827 0.18114 0.12623 -0.01412 0.06641  0.01471  152 TYR A CB  
1177 C CG  . TYR A 156 ? 0.22962 0.19502 0.13886 -0.01663 0.08449  0.01316  152 TYR A CG  
1178 C CD1 . TYR A 156 ? 0.26239 0.20899 0.13624 -0.01834 0.08988  0.01395  152 TYR A CD1 
1179 C CD2 . TYR A 156 ? 0.24890 0.22712 0.18535 -0.01711 0.09628  0.01052  152 TYR A CD2 
1180 C CE1 . TYR A 156 ? 0.36167 0.30090 0.22668 -0.02080 0.10814  0.01204  152 TYR A CE1 
1181 C CE2 . TYR A 156 ? 0.29073 0.26353 0.22259 -0.01947 0.11478  0.00843  152 TYR A CE2 
1182 C CZ  . TYR A 156 ? 0.40322 0.35673 0.30081 -0.02104 0.11896  0.00899  152 TYR A CZ  
1183 O OH  . TYR A 156 ? 0.49266 0.44264 0.38965 -0.02242 0.13198  0.00632  152 TYR A OH  
1184 N N   . TYR A 157 ? 0.25366 0.20959 0.12830 -0.01218 0.04884  0.00639  153 TYR A N   
1185 C CA  . TYR A 157 ? 0.26258 0.20496 0.10631 -0.01378 0.04787  0.00142  153 TYR A CA  
1186 C C   . TYR A 157 ? 0.29549 0.24012 0.14461 -0.01383 0.04167  -0.00748 153 TYR A C   
1187 O O   . TYR A 157 ? 0.28395 0.21796 0.10896 -0.01623 0.04067  -0.01436 153 TYR A O   
1188 C CB  . TYR A 157 ? 0.28140 0.21574 0.09938 -0.01392 0.03640  0.00760  153 TYR A CB  
1189 C CG  . TYR A 157 ? 0.30100 0.22452 0.10269 -0.01474 0.04664  0.01601  153 TYR A CG  
1190 C CD1 . TYR A 157 ? 0.34666 0.25849 0.12890 -0.01729 0.06356  0.01384  153 TYR A CD1 
1191 C CD2 . TYR A 157 ? 0.29610 0.21958 0.10247 -0.01323 0.04127  0.02587  153 TYR A CD2 
1192 C CE1 . TYR A 157 ? 0.39123 0.29473 0.16440 -0.01850 0.07343  0.02156  153 TYR A CE1 
1193 C CE2 . TYR A 157 ? 0.36079 0.27153 0.15275 -0.01468 0.05233  0.03407  153 TYR A CE2 
1194 C CZ  . TYR A 157 ? 0.36618 0.26809 0.14314 -0.01754 0.06812  0.03193  153 TYR A CZ  
1195 O OH  . TYR A 157 ? 0.43536 0.32910 0.20805 -0.01909 0.07772  0.03897  153 TYR A OH  
1196 N N   . TYR A 158 ? 0.22972 0.18657 0.10824 -0.01179 0.03817  -0.00785 154 TYR A N   
1197 C CA  . TYR A 158 ? 0.22892 0.18447 0.11377 -0.01227 0.03685  -0.01591 154 TYR A CA  
1198 C C   . TYR A 158 ? 0.29535 0.24177 0.17673 -0.01180 0.05262  -0.02275 154 TYR A C   
1199 O O   . TYR A 158 ? 0.36687 0.30432 0.24118 -0.01372 0.05381  -0.03174 154 TYR A O   
1200 C CB  . TYR A 158 ? 0.21427 0.18260 0.12896 -0.00968 0.03194  -0.01302 154 TYR A CB  
1201 C CG  . TYR A 158 ? 0.31369 0.27825 0.23375 -0.01117 0.02967  -0.01996 154 TYR A CG  
1202 C CD1 . TYR A 158 ? 0.31861 0.28222 0.23090 -0.01547 0.01785  -0.02421 154 TYR A CD1 
1203 C CD2 . TYR A 158 ? 0.28125 0.24291 0.21562 -0.00829 0.03964  -0.02234 154 TYR A CD2 
1204 C CE1 . TYR A 158 ? 0.25454 0.21394 0.17356 -0.01859 0.01706  -0.03161 154 TYR A CE1 
1205 C CE2 . TYR A 158 ? 0.22769 0.18231 0.16682 -0.01023 0.03935  -0.02841 154 TYR A CE2 
1206 C CZ  . TYR A 158 ? 0.27666 0.22991 0.20822 -0.01626 0.02857  -0.03352 154 TYR A CZ  
1207 O OH  . TYR A 158 ? 0.34807 0.29392 0.28658 -0.01986 0.02936  -0.04047 154 TYR A OH  
1208 N N   . SER A 159 ? 0.28898 0.23742 0.17664 -0.00966 0.06557  -0.01955 155 SER A N   
1209 C CA  . SER A 159 ? 0.37609 0.31821 0.26643 -0.00785 0.08224  -0.02589 155 SER A CA  
1210 C C   . SER A 159 ? 0.40483 0.32870 0.26089 -0.01191 0.08838  -0.03480 155 SER A C   
1211 O O   . SER A 159 ? 0.41999 0.33492 0.27568 -0.01105 0.09965  -0.04372 155 SER A O   
1212 C CB  . SER A 159 ? 0.40076 0.35186 0.30741 -0.00551 0.09463  -0.02096 155 SER A CB  
1213 O OG  . SER A 159 ? 0.41982 0.36862 0.30968 -0.00927 0.09441  -0.01531 155 SER A OG  
1214 N N   . THR A 160 ? 0.49693 0.41420 0.32285 -0.01587 0.08115  -0.03264 156 THR A N   
1215 C CA  . THR A 160 ? 0.54443 0.44447 0.33169 -0.01996 0.08505  -0.04087 156 THR A CA  
1216 C C   . THR A 160 ? 0.49291 0.39010 0.25991 -0.02364 0.06564  -0.04462 156 THR A C   
1217 O O   . THR A 160 ? 0.55632 0.44379 0.28984 -0.02653 0.06214  -0.04772 156 THR A O   
1218 C CB  . THR A 160 ? 0.60957 0.50481 0.37824 -0.02057 0.09319  -0.03409 156 THR A CB  
1219 O OG1 . THR A 160 ? 0.48471 0.38597 0.25476 -0.02007 0.08496  -0.02199 156 THR A OG1 
1220 C CG2 . THR A 160 ? 0.44702 0.34528 0.23718 -0.01823 0.11283  -0.03483 156 THR A CG2 
1221 N N   . GLY A 161 ? 0.40051 0.30901 0.19157 -0.02311 0.05193  -0.04375 157 GLY A N   
1222 C CA  . GLY A 161 ? 0.38838 0.29757 0.16886 -0.02709 0.03436  -0.04934 157 GLY A CA  
1223 C C   . GLY A 161 ? 0.46497 0.37981 0.23108 -0.02665 0.01767  -0.04090 157 GLY A C   
1224 O O   . GLY A 161 ? 0.46579 0.38296 0.22167 -0.02973 0.00187  -0.04607 157 GLY A O   
1225 N N   . GLY A 162 ? 0.38145 0.29879 0.14841 -0.02284 0.02037  -0.02835 158 GLY A N   
1226 C CA  . GLY A 162 ? 0.36731 0.28750 0.12110 -0.02106 0.00502  -0.01945 158 GLY A CA  
1227 C C   . GLY A 162 ? 0.38879 0.32517 0.17350 -0.01836 -0.00818 -0.01381 158 GLY A C   
1228 O O   . GLY A 162 ? 0.58016 0.51961 0.35858 -0.01552 -0.02082 -0.00611 158 GLY A O   
1229 N N   . THR A 163 ? 0.30524 0.25115 0.12241 -0.01851 -0.00482 -0.01695 159 THR A N   
1230 C CA  . THR A 163 ? 0.25402 0.21477 0.09991 -0.01656 -0.01493 -0.01296 159 THR A CA  
1231 C C   . THR A 163 ? 0.25980 0.22610 0.11970 -0.02039 -0.02092 -0.02276 159 THR A C   
1232 O O   . THR A 163 ? 0.24833 0.20930 0.11379 -0.02263 -0.01091 -0.02967 159 THR A O   
1233 C CB  . THR A 163 ? 0.23570 0.20290 0.10688 -0.01358 -0.00518 -0.00672 159 THR A CB  
1234 O OG1 . THR A 163 ? 0.26966 0.23190 0.13111 -0.01158 0.00091  0.00144  159 THR A OG1 
1235 C CG2 . THR A 163 ? 0.22417 0.20530 0.12143 -0.01198 -0.01424 -0.00385 159 THR A CG2 
1236 N N   . GLN A 164 ? 0.24474 0.22141 0.11242 -0.02102 -0.03634 -0.02325 160 GLN A N   
1237 C CA  . GLN A 164 ? 0.23830 0.22203 0.12419 -0.02584 -0.04163 -0.03225 160 GLN A CA  
1238 C C   . GLN A 164 ? 0.20783 0.19918 0.12506 -0.02435 -0.03472 -0.02850 160 GLN A C   
1239 O O   . GLN A 164 ? 0.19800 0.19430 0.12479 -0.01946 -0.03190 -0.01929 160 GLN A O   
1240 C CB  . GLN A 164 ? 0.28986 0.28542 0.17742 -0.02692 -0.06050 -0.03415 160 GLN A CB  
1241 C CG  . GLN A 164 ? 0.33427 0.32375 0.18832 -0.02835 -0.07076 -0.03831 160 GLN A CG  
1242 C CD  . GLN A 164 ? 0.46262 0.44707 0.30792 -0.03693 -0.07185 -0.05410 160 GLN A CD  
1243 O OE1 . GLN A 164 ? 0.66354 0.65954 0.52190 -0.04193 -0.08447 -0.06246 160 GLN A OE1 
1244 N NE2 . GLN A 164 ? 0.49022 0.45757 0.31532 -0.03911 -0.05783 -0.05931 160 GLN A NE2 
1245 N N   . LEU A 165 ? 0.13066 0.19250 0.12914 -0.02830 -0.01897 -0.04835 161 LEU A N   
1246 C CA  . LEU A 165 ? 0.12263 0.18391 0.13650 -0.02858 -0.01566 -0.04560 161 LEU A CA  
1247 C C   . LEU A 165 ? 0.17080 0.23768 0.19190 -0.02660 -0.01880 -0.03941 161 LEU A C   
1248 O O   . LEU A 165 ? 0.12865 0.19321 0.15490 -0.02502 -0.01510 -0.03437 161 LEU A O   
1249 C CB  . LEU A 165 ? 0.13631 0.19542 0.15894 -0.03264 -0.01526 -0.05199 161 LEU A CB  
1250 C CG  . LEU A 165 ? 0.17404 0.22941 0.20967 -0.03306 -0.01119 -0.04920 161 LEU A CG  
1251 C CD1 . LEU A 165 ? 0.22682 0.27654 0.26142 -0.02939 -0.00508 -0.04630 161 LEU A CD1 
1252 C CD2 . LEU A 165 ? 0.24217 0.29250 0.28383 -0.03803 -0.01090 -0.05529 161 LEU A CD2 
1253 N N   . PRO A 166 ? 0.19132 0.26621 0.21353 -0.02609 -0.02552 -0.03988 162 PRO A N   
1254 C CA  . PRO A 166 ? 0.13883 0.21890 0.16785 -0.02274 -0.02745 -0.03424 162 PRO A CA  
1255 C C   . PRO A 166 ? 0.18002 0.25367 0.19969 -0.01844 -0.02553 -0.02753 162 PRO A C   
1256 O O   . PRO A 166 ? 0.14958 0.22223 0.17498 -0.01661 -0.02345 -0.02309 162 PRO A O   
1257 C CB  . PRO A 166 ? 0.15330 0.24463 0.18343 -0.02164 -0.03563 -0.03684 162 PRO A CB  
1258 C CG  . PRO A 166 ? 0.17974 0.27294 0.21026 -0.02727 -0.03738 -0.04487 162 PRO A CG  
1259 C CD  . PRO A 166 ? 0.17863 0.25969 0.19763 -0.02828 -0.03192 -0.04618 162 PRO A CD  
1260 N N   . THR A 167 ? 0.15526 0.22352 0.15946 -0.01746 -0.02576 -0.02685 163 THR A N   
1261 C CA  . THR A 167 ? 0.12617 0.18638 0.12060 -0.01521 -0.02302 -0.02057 163 THR A CA  
1262 C C   . THR A 167 ? 0.16279 0.21886 0.16241 -0.01789 -0.01565 -0.01945 163 THR A C   
1263 O O   . THR A 167 ? 0.12787 0.17986 0.12735 -0.01706 -0.01359 -0.01464 163 THR A O   
1264 C CB  . THR A 167 ? 0.20350 0.25824 0.17859 -0.01448 -0.02436 -0.01981 163 THR A CB  
1265 O OG1 . THR A 167 ? 0.25764 0.31672 0.22752 -0.01042 -0.03273 -0.01991 163 THR A OG1 
1266 C CG2 . THR A 167 ? 0.18086 0.22522 0.14480 -0.01413 -0.02028 -0.01334 163 THR A CG2 
1267 N N   . LEU A 168 ? 0.11866 0.17576 0.12304 -0.02071 -0.01206 -0.02422 164 LEU A N   
1268 C CA  . LEU A 168 ? 0.13592 0.19138 0.14727 -0.02183 -0.00610 -0.02342 164 LEU A CA  
1269 C C   . LEU A 168 ? 0.12081 0.17759 0.14423 -0.02093 -0.00653 -0.02064 164 LEU A C   
1270 O O   . LEU A 168 ? 0.08014 0.13527 0.10546 -0.02063 -0.00419 -0.01690 164 LEU A O   
1271 C CB  . LEU A 168 ? 0.13979 0.19527 0.15387 -0.02320 -0.00265 -0.02947 164 LEU A CB  
1272 C CG  . LEU A 168 ? 0.10824 0.16363 0.12990 -0.02270 0.00305  -0.02917 164 LEU A CG  
1273 C CD1 . LEU A 168 ? 0.16510 0.22150 0.18026 -0.02354 0.00726  -0.02673 164 LEU A CD1 
1274 C CD2 . LEU A 168 ? 0.20611 0.25973 0.23172 -0.02225 0.00569  -0.03545 164 LEU A CD2 
1275 N N   . ALA A 169 ? 0.11703 0.17714 0.14815 -0.02116 -0.00937 -0.02269 165 ALA A N   
1276 C CA  . ALA A 169 ? 0.09271 0.15386 0.13387 -0.02072 -0.00886 -0.02009 165 ALA A CA  
1277 C C   . ALA A 169 ? 0.12314 0.18402 0.16157 -0.01798 -0.01023 -0.01505 165 ALA A C   
1278 O O   . ALA A 169 ? 0.10801 0.16675 0.14964 -0.01739 -0.00816 -0.01198 165 ALA A O   
1279 C CB  . ALA A 169 ? 0.14152 0.20729 0.19083 -0.02276 -0.01101 -0.02333 165 ALA A CB  
1280 N N   . ARG A 170 ? 0.07663 0.13865 0.10799 -0.01573 -0.01408 -0.01428 166 ARG A N   
1281 C CA  . ARG A 170 ? 0.09045 0.14934 0.11753 -0.01215 -0.01528 -0.00978 166 ARG A CA  
1282 C C   . ARG A 170 ? 0.09131 0.14173 0.11078 -0.01341 -0.01195 -0.00665 166 ARG A C   
1283 O O   . ARG A 170 ? 0.14330 0.18959 0.16240 -0.01234 -0.01108 -0.00370 166 ARG A O   
1284 C CB  . ARG A 170 ? 0.14519 0.20552 0.16482 -0.00810 -0.02062 -0.00930 166 ARG A CB  
1285 C CG  . ARG A 170 ? 0.24985 0.30172 0.26017 -0.00362 -0.02150 -0.00441 166 ARG A CG  
1286 C CD  . ARG A 170 ? 0.41648 0.46906 0.41965 0.00221  -0.02730 -0.00338 166 ARG A CD  
1287 N NE  . ARG A 170 ? 0.45220 0.50228 0.44343 0.00110  -0.02950 -0.00402 166 ARG A NE  
1288 C CZ  . ARG A 170 ? 0.41357 0.47359 0.40765 0.00107  -0.03391 -0.00815 166 ARG A CZ  
1289 N NH1 . ARG A 170 ? 0.40112 0.47445 0.41106 0.00076  -0.03590 -0.01204 166 ARG A NH1 
1290 N NH2 . ARG A 170 ? 0.38410 0.44053 0.36403 0.00086  -0.03634 -0.00850 166 ARG A NH2 
1291 N N   . SER A 171 ? 0.08628 0.13461 0.09966 -0.01620 -0.00976 -0.00777 167 SER A N   
1292 C CA  . SER A 171 ? 0.10533 0.14840 0.11372 -0.01892 -0.00594 -0.00541 167 SER A CA  
1293 C C   . SER A 171 ? 0.10249 0.14857 0.12163 -0.02035 -0.00333 -0.00561 167 SER A C   
1294 O O   . SER A 171 ? 0.10069 0.14359 0.11842 -0.02195 -0.00206 -0.00323 167 SER A O   
1295 C CB  . SER A 171 ? 0.19446 0.23716 0.19524 -0.02174 -0.00307 -0.00711 167 SER A CB  
1296 O OG  . SER A 171 ? 0.17700 0.21570 0.16501 -0.02004 -0.00616 -0.00628 167 SER A OG  
1297 N N   . PHE A 172 ? 0.07479 0.12600 0.10372 -0.01987 -0.00290 -0.00844 168 PHE A N   
1298 C CA  . PHE A 172 ? 0.06408 0.11694 0.10169 -0.01977 -0.00146 -0.00781 168 PHE A CA  
1299 C C   . PHE A 172 ? 0.06576 0.11623 0.10376 -0.01831 -0.00316 -0.00476 168 PHE A C   
1300 O O   . PHE A 172 ? 0.11959 0.16921 0.15878 -0.01879 -0.00261 -0.00306 168 PHE A O   
1301 C CB  . PHE A 172 ? 0.07049 0.12548 0.11601 -0.01904 -0.00074 -0.01075 168 PHE A CB  
1302 C CG  . PHE A 172 ? 0.08136 0.13792 0.12773 -0.01945 0.00198  -0.01433 168 PHE A CG  
1303 C CD1 . PHE A 172 ? 0.12695 0.18648 0.17290 -0.02017 0.00465  -0.01410 168 PHE A CD1 
1304 C CD2 . PHE A 172 ? 0.07746 0.13292 0.12547 -0.01938 0.00224  -0.01855 168 PHE A CD2 
1305 C CE1 . PHE A 172 ? 0.15653 0.21911 0.20412 -0.01971 0.00808  -0.01793 168 PHE A CE1 
1306 C CE2 . PHE A 172 ? 0.16814 0.22396 0.21596 -0.01888 0.00529  -0.02262 168 PHE A CE2 
1307 C CZ  . PHE A 172 ? 0.16560 0.22556 0.21346 -0.01847 0.00849  -0.02226 168 PHE A CZ  
1308 N N   . ILE A 173 ? 0.08923 0.13978 0.12660 -0.01628 -0.00529 -0.00457 169 ILE A N   
1309 C CA  . ILE A 173 ? 0.06619 0.11519 0.10397 -0.01410 -0.00593 -0.00236 169 ILE A CA  
1310 C C   . ILE A 173 ? 0.09962 0.14149 0.12837 -0.01387 -0.00628 -0.00005 169 ILE A C   
1311 O O   . ILE A 173 ? 0.10981 0.14859 0.13763 -0.01365 -0.00581 0.00125  169 ILE A O   
1312 C CB  . ILE A 173 ? 0.06122 0.11485 0.10217 -0.01158 -0.00778 -0.00334 169 ILE A CB  
1313 C CG1 . ILE A 173 ? 0.06175 0.12109 0.11241 -0.01368 -0.00669 -0.00566 169 ILE A CG1 
1314 C CG2 . ILE A 173 ? 0.07115 0.12331 0.11059 -0.00796 -0.00795 -0.00144 169 ILE A CG2 
1315 C CD1 . ILE A 173 ? 0.05740 0.12469 0.11359 -0.01275 -0.00861 -0.00757 169 ILE A CD1 
1316 N N   . ILE A 174 ? 0.07951 0.11715 0.09988 -0.01438 -0.00702 0.00043  170 ILE A N   
1317 C CA  . ILE A 174 ? 0.08314 0.11087 0.09322 -0.01547 -0.00680 0.00273  170 ILE A CA  
1318 C C   . ILE A 174 ? 0.15095 0.17900 0.16304 -0.02059 -0.00459 0.00258  170 ILE A C   
1319 O O   . ILE A 174 ? 0.11241 0.13493 0.12119 -0.02179 -0.00477 0.00342  170 ILE A O   
1320 C CB  . ILE A 174 ? 0.09430 0.11591 0.09324 -0.01556 -0.00748 0.00397  170 ILE A CB  
1321 C CG1 . ILE A 174 ? 0.09783 0.12037 0.09475 -0.00926 -0.01128 0.00416  170 ILE A CG1 
1322 C CG2 . ILE A 174 ? 0.13581 0.14433 0.12294 -0.01845 -0.00626 0.00661  170 ILE A CG2 
1323 C CD1 . ILE A 174 ? 0.13534 0.15385 0.12101 -0.00857 -0.01300 0.00522  170 ILE A CD1 
1324 N N   . CYS A 175 ? 0.11007 0.14538 0.12784 -0.02341 -0.00269 0.00094  171 CYS A N   
1325 C CA  . CYS A 175 ? 0.11158 0.15081 0.13347 -0.02775 -0.00095 0.00039  171 CYS A CA  
1326 C C   . CYS A 175 ? 0.15998 0.20249 0.18861 -0.02625 -0.00256 0.00037  171 CYS A C   
1327 O O   . CYS A 175 ? 0.14902 0.19094 0.17685 -0.02924 -0.00323 0.00057  171 CYS A O   
1328 C CB  . CYS A 175 ? 0.15259 0.20046 0.18039 -0.02925 0.00182  -0.00189 171 CYS A CB  
1329 S SG  . CYS A 175 ? 0.24102 0.28512 0.25810 -0.03321 0.00509  -0.00164 171 CYS A SG  
1330 N N   . ILE A 176 ? 0.12331 0.16875 0.15760 -0.02224 -0.00324 0.00010  172 ILE A N   
1331 C CA  . ILE A 176 ? 0.11095 0.15805 0.14929 -0.02057 -0.00442 0.00087  172 ILE A CA  
1332 C C   . ILE A 176 ? 0.12464 0.16490 0.15551 -0.02043 -0.00576 0.00212  172 ILE A C   
1333 O O   . ILE A 176 ? 0.14708 0.18752 0.17709 -0.02147 -0.00725 0.00233  172 ILE A O   
1334 C CB  . ILE A 176 ? 0.14405 0.19277 0.18782 -0.01733 -0.00387 0.00086  172 ILE A CB  
1335 C CG1 . ILE A 176 ? 0.17603 0.22941 0.22629 -0.01718 -0.00254 -0.00115 172 ILE A CG1 
1336 C CG2 . ILE A 176 ? 0.10960 0.15705 0.15379 -0.01547 -0.00464 0.00280  172 ILE A CG2 
1337 C CD1 . ILE A 176 ? 0.20999 0.26206 0.26427 -0.01540 -0.00168 -0.00180 172 ILE A CD1 
1338 N N   . GLN A 177 ? 0.10272 0.13691 0.12760 -0.01860 -0.00560 0.00255  173 GLN A N   
1339 C CA  . GLN A 177 ? 0.13991 0.16642 0.15715 -0.01712 -0.00623 0.00306  173 GLN A CA  
1340 C C   . GLN A 177 ? 0.12603 0.14501 0.13531 -0.02148 -0.00699 0.00267  173 GLN A C   
1341 O O   . GLN A 177 ? 0.18645 0.20063 0.19064 -0.02231 -0.00802 0.00206  173 GLN A O   
1342 C CB  . GLN A 177 ? 0.08056 0.10394 0.09501 -0.01243 -0.00590 0.00332  173 GLN A CB  
1343 C CG  . GLN A 177 ? 0.11488 0.14626 0.13768 -0.00946 -0.00483 0.00317  173 GLN A CG  
1344 C CD  . GLN A 177 ? 0.10668 0.13857 0.12901 -0.00455 -0.00487 0.00284  173 GLN A CD  
1345 O OE1 . GLN A 177 ? 0.15052 0.17996 0.17001 -0.00113 -0.00373 0.00276  173 GLN A OE1 
1346 N NE2 . GLN A 177 ? 0.12336 0.15928 0.14833 -0.00364 -0.00636 0.00229  173 GLN A NE2 
1347 N N   . MET A 178 ? 0.12519 0.14226 0.13215 -0.02505 -0.00622 0.00282  174 MET A N   
1348 C CA  . MET A 178 ? 0.11679 0.12504 0.11552 -0.03080 -0.00613 0.00258  174 MET A CA  
1349 C C   . MET A 178 ? 0.12181 0.13903 0.12729 -0.03704 -0.00658 0.00098  174 MET A C   
1350 O O   . MET A 178 ? 0.14086 0.15252 0.14112 -0.04344 -0.00676 0.00003  174 MET A O   
1351 C CB  . MET A 178 ? 0.10863 0.10928 0.09976 -0.03266 -0.00442 0.00410  174 MET A CB  
1352 C CG  . MET A 178 ? 0.11506 0.10607 0.09815 -0.02559 -0.00537 0.00572  174 MET A CG  
1353 S SD  . MET A 178 ? 0.16821 0.14715 0.13818 -0.02645 -0.00444 0.00861  174 MET A SD  
1354 C CE  . MET A 178 ? 0.28620 0.24803 0.24391 -0.03480 -0.00276 0.00911  174 MET A CE  
1355 N N   . ILE A 179 ? 0.08589 0.11665 0.10294 -0.03522 -0.00701 0.00047  175 ILE A N   
1356 C CA  . ILE A 179 ? 0.09778 0.13984 0.12315 -0.03930 -0.00824 -0.00115 175 ILE A CA  
1357 C C   . ILE A 179 ? 0.10762 0.15479 0.13695 -0.03495 -0.01158 -0.00105 175 ILE A C   
1358 O O   . ILE A 179 ? 0.13575 0.18226 0.16190 -0.03724 -0.01472 -0.00209 175 ILE A O   
1359 C CB  . ILE A 179 ? 0.15059 0.20426 0.18567 -0.04042 -0.00549 -0.00191 175 ILE A CB  
1360 C CG1 . ILE A 179 ? 0.20883 0.25593 0.23677 -0.04517 -0.00171 -0.00143 175 ILE A CG1 
1361 C CG2 . ILE A 179 ? 0.13244 0.20082 0.17852 -0.04341 -0.00696 -0.00395 175 ILE A CG2 
1362 C CD1 . ILE A 179 ? 0.23704 0.29365 0.27145 -0.04536 0.00205  -0.00238 175 ILE A CD1 
1363 N N   . SER A 180 ? 0.08842 0.13928 0.12309 -0.02904 -0.01100 0.00023  176 SER A N   
1364 C CA  . SER A 180 ? 0.07057 0.12446 0.10735 -0.02481 -0.01364 0.00134  176 SER A CA  
1365 C C   . SER A 180 ? 0.11294 0.15723 0.13903 -0.02350 -0.01468 0.00217  176 SER A C   
1366 O O   . SER A 180 ? 0.09277 0.13769 0.11525 -0.02369 -0.01806 0.00198  176 SER A O   
1367 C CB  . SER A 180 ? 0.06455 0.12061 0.10745 -0.01977 -0.01182 0.00269  176 SER A CB  
1368 O OG  . SER A 180 ? 0.17681 0.24171 0.22909 -0.01985 -0.01084 0.00122  176 SER A OG  
1369 N N   . GLU A 181 ? 0.10284 0.13910 0.12364 -0.02163 -0.01194 0.00275  177 GLU A N   
1370 C CA  . GLU A 181 ? 0.09284 0.12115 0.10420 -0.01933 -0.01176 0.00304  177 GLU A CA  
1371 C C   . GLU A 181 ? 0.15303 0.17355 0.15462 -0.02301 -0.01360 0.00077  177 GLU A C   
1372 O O   . GLU A 181 ? 0.10398 0.11968 0.09719 -0.02208 -0.01483 0.00003  177 GLU A O   
1373 C CB  . GLU A 181 ? 0.10941 0.13420 0.12017 -0.01561 -0.00833 0.00372  177 GLU A CB  
1374 C CG  . GLU A 181 ? 0.11934 0.15071 0.13927 -0.01348 -0.00644 0.00518  177 GLU A CG  
1375 C CD  . GLU A 181 ? 0.23602 0.26820 0.25578 -0.01149 -0.00565 0.00726  177 GLU A CD  
1376 O OE1 . GLU A 181 ? 0.20310 0.23195 0.21511 -0.01119 -0.00703 0.00769  177 GLU A OE1 
1377 O OE2 . GLU A 181 ? 0.22934 0.26429 0.25540 -0.01060 -0.00360 0.00848  177 GLU A OE2 
1378 N N   . ALA A 182 ? 0.13743 0.15521 0.13842 -0.02772 -0.01350 -0.00051 178 ALA A N   
1379 C CA  . ALA A 182 ? 0.12842 0.13710 0.11984 -0.03290 -0.01521 -0.00301 178 ALA A CA  
1380 C C   . ALA A 182 ? 0.17869 0.19590 0.17307 -0.03732 -0.01954 -0.00485 178 ALA A C   
1381 O O   . ALA A 182 ? 0.15168 0.16216 0.13675 -0.04023 -0.02213 -0.00745 178 ALA A O   
1382 C CB  . ALA A 182 ? 0.14106 0.14305 0.12999 -0.03792 -0.01339 -0.00325 178 ALA A CB  
1383 N N   . ALA A 183 ? 0.12922 0.16141 0.13622 -0.03735 -0.02079 -0.00397 179 ALA A N   
1384 C CA  . ALA A 183 ? 0.16252 0.20543 0.17369 -0.03954 -0.02600 -0.00551 179 ALA A CA  
1385 C C   . ALA A 183 ? 0.15426 0.19437 0.15784 -0.03399 -0.02875 -0.00433 179 ALA A C   
1386 O O   . ALA A 183 ? 0.13255 0.17386 0.13063 -0.03630 -0.03375 -0.00647 179 ALA A O   
1387 C CB  . ALA A 183 ? 0.13755 0.19730 0.16451 -0.03867 -0.02641 -0.00482 179 ALA A CB  
1388 N N   . ARG A 184 ? 0.13574 0.17187 0.13796 -0.02736 -0.02538 -0.00111 180 ARG A N   
1389 C CA  . ARG A 184 ? 0.12600 0.15898 0.12015 -0.02246 -0.02651 0.00086  180 ARG A CA  
1390 C C   . ARG A 184 ? 0.12378 0.14434 0.10235 -0.02304 -0.02585 -0.00136 180 ARG A C   
1391 O O   . ARG A 184 ? 0.13372 0.15210 0.10243 -0.02124 -0.02836 -0.00122 180 ARG A O   
1392 C CB  . ARG A 184 ? 0.10844 0.14077 0.10643 -0.01692 -0.02196 0.00474  180 ARG A CB  
1393 C CG  . ARG A 184 ? 0.11279 0.15434 0.12297 -0.01462 -0.02274 0.00698  180 ARG A CG  
1394 C CD  . ARG A 184 ? 0.11966 0.15782 0.13307 -0.01152 -0.01739 0.00947  180 ARG A CD  
1395 N NE  . ARG A 184 ? 0.15082 0.19341 0.17273 -0.00850 -0.01762 0.01164  180 ARG A NE  
1396 C CZ  . ARG A 184 ? 0.23939 0.27867 0.26454 -0.00676 -0.01352 0.01344  180 ARG A CZ  
1397 N NH1 . ARG A 184 ? 0.21204 0.24695 0.23484 -0.00783 -0.00913 0.01331  180 ARG A NH1 
1398 N NH2 . ARG A 184 ? 0.23057 0.27114 0.26181 -0.00380 -0.01392 0.01501  180 ARG A NH2 
1399 N N   . PHE A 185 ? 0.13183 0.14311 0.10655 -0.02469 -0.02245 -0.00338 181 PHE A N   
1400 C CA  . PHE A 185 ? 0.14935 0.14719 0.10950 -0.02316 -0.02044 -0.00572 181 PHE A CA  
1401 C C   . PHE A 185 ? 0.16656 0.15402 0.12061 -0.02878 -0.02131 -0.00970 181 PHE A C   
1402 O O   . PHE A 185 ? 0.22667 0.21173 0.18557 -0.03014 -0.01906 -0.00906 181 PHE A O   
1403 C CB  . PHE A 185 ? 0.13624 0.13065 0.09687 -0.01685 -0.01423 -0.00374 181 PHE A CB  
1404 C CG  . PHE A 185 ? 0.13507 0.13635 0.09933 -0.01256 -0.01192 -0.00001 181 PHE A CG  
1405 C CD1 . PHE A 185 ? 0.17248 0.16998 0.12544 -0.00990 -0.01060 0.00026  181 PHE A CD1 
1406 C CD2 . PHE A 185 ? 0.11619 0.12594 0.09358 -0.01158 -0.01038 0.00311  181 PHE A CD2 
1407 C CE1 . PHE A 185 ? 0.16366 0.16539 0.11841 -0.00693 -0.00750 0.00436  181 PHE A CE1 
1408 C CE2 . PHE A 185 ? 0.12885 0.14214 0.10857 -0.00872 -0.00773 0.00656  181 PHE A CE2 
1409 C CZ  . PHE A 185 ? 0.15753 0.16660 0.12595 -0.00665 -0.00607 0.00760  181 PHE A CZ  
1410 N N   . GLN A 186 ? 0.16540 0.14475 0.10692 -0.03220 -0.02442 -0.01382 182 GLN A N   
1411 C CA  . GLN A 186 ? 0.17968 0.14383 0.11212 -0.03738 -0.02417 -0.01784 182 GLN A CA  
1412 C C   . GLN A 186 ? 0.18438 0.13469 0.11045 -0.03082 -0.01849 -0.01731 182 GLN A C   
1413 O O   . GLN A 186 ? 0.19200 0.13031 0.11447 -0.03328 -0.01717 -0.01811 182 GLN A O   
1414 C CB  . GLN A 186 ? 0.19910 0.15481 0.11714 -0.04194 -0.02837 -0.02333 182 GLN A CB  
1415 C CG  . GLN A 186 ? 0.24870 0.21912 0.17220 -0.04804 -0.03554 -0.02468 182 GLN A CG  
1416 C CD  . GLN A 186 ? 0.33709 0.31327 0.25459 -0.04219 -0.03801 -0.02356 182 GLN A CD  
1417 O OE1 . GLN A 186 ? 0.38495 0.36476 0.30544 -0.03435 -0.03409 -0.01885 182 GLN A OE1 
1418 N NE2 . GLN A 186 ? 0.43682 0.41300 0.34452 -0.04645 -0.04449 -0.02792 182 GLN A NE2 
1419 N N   . TYR A 187 ? 0.18901 0.14093 0.11344 -0.02233 -0.01499 -0.01584 183 TYR A N   
1420 C CA  . TYR A 187 ? 0.18624 0.12862 0.10686 -0.01483 -0.00990 -0.01581 183 TYR A CA  
1421 C C   . TYR A 187 ? 0.20719 0.15354 0.13905 -0.01376 -0.00862 -0.01231 183 TYR A C   
1422 O O   . TYR A 187 ? 0.19683 0.13057 0.12327 -0.01129 -0.00720 -0.01280 183 TYR A O   
1423 C CB  . TYR A 187 ? 0.18395 0.13233 0.10411 -0.00709 -0.00574 -0.01486 183 TYR A CB  
1424 C CG  . TYR A 187 ? 0.21042 0.15345 0.12934 0.00170  -0.00039 -0.01542 183 TYR A CG  
1425 C CD1 . TYR A 187 ? 0.21473 0.14177 0.11881 0.00593  0.00178  -0.02000 183 TYR A CD1 
1426 C CD2 . TYR A 187 ? 0.23778 0.19244 0.17074 0.00617  0.00221  -0.01190 183 TYR A CD2 
1427 C CE1 . TYR A 187 ? 0.28381 0.20772 0.18816 0.01563  0.00655  -0.02075 183 TYR A CE1 
1428 C CE2 . TYR A 187 ? 0.28351 0.23668 0.21744 0.01482  0.00627  -0.01271 183 TYR A CE2 
1429 C CZ  . TYR A 187 ? 0.24452 0.18290 0.16471 0.02014  0.00849  -0.01696 183 TYR A CZ  
1430 O OH  . TYR A 187 ? 0.28094 0.21946 0.20345 0.03032  0.01240  -0.01797 183 TYR A OH  
1431 N N   . ILE A 188 ? 0.15610 0.11850 0.10210 -0.01530 -0.00939 -0.00884 184 ILE A N   
1432 C CA  . ILE A 188 ? 0.14583 0.11262 0.10128 -0.01475 -0.00847 -0.00603 184 ILE A CA  
1433 C C   . ILE A 188 ? 0.15189 0.11165 0.10471 -0.02233 -0.01037 -0.00653 184 ILE A C   
1434 O O   . ILE A 188 ? 0.17307 0.12600 0.12425 -0.02137 -0.00916 -0.00503 184 ILE A O   
1435 C CB  . ILE A 188 ? 0.13148 0.11564 0.10131 -0.01422 -0.00829 -0.00307 184 ILE A CB  
1436 C CG1 . ILE A 188 ? 0.12448 0.11375 0.09595 -0.00804 -0.00524 -0.00223 184 ILE A CG1 
1437 C CG2 . ILE A 188 ? 0.14371 0.13237 0.12187 -0.01428 -0.00770 -0.00104 184 ILE A CG2 
1438 C CD1 . ILE A 188 ? 0.11828 0.12097 0.10240 -0.00768 -0.00435 0.00067  184 ILE A CD1 
1439 N N   . GLU A 189 ? 0.18184 0.14391 0.13416 -0.03024 -0.01337 -0.00851 185 GLU A N   
1440 C CA  . GLU A 189 ? 0.24176 0.19621 0.19056 -0.03918 -0.01426 -0.00973 185 GLU A CA  
1441 C C   . GLU A 189 ? 0.18519 0.11611 0.11818 -0.03819 -0.01261 -0.01108 185 GLU A C   
1442 O O   . GLU A 189 ? 0.20857 0.12966 0.13783 -0.04109 -0.01108 -0.00935 185 GLU A O   
1443 C CB  . GLU A 189 ? 0.16770 0.12880 0.11795 -0.04772 -0.01831 -0.01298 185 GLU A CB  
1444 C CG  . GLU A 189 ? 0.17903 0.13404 0.12703 -0.05919 -0.01870 -0.01491 185 GLU A CG  
1445 C CD  . GLU A 189 ? 0.29703 0.25489 0.24299 -0.06788 -0.02344 -0.01985 185 GLU A CD  
1446 O OE1 . GLU A 189 ? 0.29211 0.25923 0.23930 -0.06442 -0.02718 -0.02117 185 GLU A OE1 
1447 O OE2 . GLU A 189 ? 0.34449 0.29490 0.28679 -0.07867 -0.02355 -0.02242 185 GLU A OE2 
1448 N N   . GLY A 190 ? 0.23037 0.15069 0.15255 -0.03345 -0.01253 -0.01404 186 GLY A N   
1449 C CA  . GLY A 190 ? 0.21903 0.11530 0.12550 -0.03037 -0.01075 -0.01572 186 GLY A CA  
1450 C C   . GLY A 190 ? 0.22635 0.11891 0.13376 -0.02054 -0.00809 -0.01199 186 GLY A C   
1451 O O   . GLY A 190 ? 0.26667 0.13954 0.16289 -0.01926 -0.00718 -0.01134 186 GLY A O   
1452 N N   . GLU A 191 ? 0.20015 0.11090 0.12029 -0.01359 -0.00716 -0.00950 187 GLU A N   
1453 C CA  . GLU A 191 ? 0.23346 0.14508 0.15692 -0.00467 -0.00579 -0.00638 187 GLU A CA  
1454 C C   . GLU A 191 ? 0.27905 0.18812 0.20319 -0.00921 -0.00662 -0.00281 187 GLU A C   
1455 O O   . GLU A 191 ? 0.22589 0.12356 0.14319 -0.00348 -0.00648 -0.00058 187 GLU A O   
1456 C CB  . GLU A 191 ? 0.24322 0.17652 0.18147 0.00100  -0.00471 -0.00516 187 GLU A CB  
1457 C CG  . GLU A 191 ? 0.32073 0.25593 0.25716 0.00764  -0.00221 -0.00785 187 GLU A CG  
1458 C CD  . GLU A 191 ? 0.49473 0.42250 0.42692 0.01895  -0.00014 -0.00865 187 GLU A CD  
1459 O OE1 . GLU A 191 ? 0.37634 0.29944 0.30832 0.02254  -0.00156 -0.00634 187 GLU A OE1 
1460 O OE2 . GLU A 191 ? 0.45591 0.38303 0.38465 0.02488  0.00294  -0.01158 187 GLU A OE2 
1461 N N   . MET A 192 ? 0.23034 0.15028 0.16220 -0.01875 -0.00737 -0.00210 188 MET A N   
1462 C CA  . MET A 192 ? 0.20874 0.12574 0.13951 -0.02396 -0.00695 0.00094  188 MET A CA  
1463 C C   . MET A 192 ? 0.21092 0.10400 0.12548 -0.03036 -0.00625 0.00068  188 MET A C   
1464 O O   . MET A 192 ? 0.22517 0.10656 0.13162 -0.03101 -0.00518 0.00414  188 MET A O   
1465 C CB  . MET A 192 ? 0.25184 0.18806 0.19609 -0.03180 -0.00702 0.00111  188 MET A CB  
1466 C CG  . MET A 192 ? 0.34014 0.29670 0.29901 -0.02640 -0.00745 0.00151  188 MET A CG  
1467 S SD  . MET A 192 ? 0.26571 0.22484 0.22662 -0.01623 -0.00720 0.00414  188 MET A SD  
1468 C CE  . MET A 192 ? 0.37725 0.35212 0.35017 -0.01056 -0.00708 0.00265  188 MET A CE  
1469 N N   . ARG A 193 ? 0.22178 0.10607 0.13000 -0.03555 -0.00688 -0.00338 189 ARG A N   
1470 C CA  . ARG A 193 ? 0.30163 0.16013 0.19312 -0.04244 -0.00605 -0.00442 189 ARG A CA  
1471 C C   . ARG A 193 ? 0.26956 0.10419 0.14565 -0.03191 -0.00517 -0.00256 189 ARG A C   
1472 O O   . ARG A 193 ? 0.30337 0.11622 0.16572 -0.03524 -0.00385 0.00008  189 ARG A O   
1473 C CB  . ARG A 193 ? 0.35877 0.21320 0.24626 -0.04963 -0.00770 -0.01033 189 ARG A CB  
1474 C CG  . ARG A 193 ? 0.40936 0.28410 0.30992 -0.06180 -0.00938 -0.01218 189 ARG A CG  
1475 C CD  . ARG A 193 ? 0.39014 0.26710 0.28888 -0.06570 -0.01278 -0.01816 189 ARG A CD  
1476 N NE  . ARG A 193 ? 0.37861 0.22794 0.25850 -0.07019 -0.01271 -0.02226 189 ARG A NE  
1477 C CZ  . ARG A 193 ? 0.60867 0.44872 0.48347 -0.08460 -0.01325 -0.02522 189 ARG A CZ  
1478 N NH1 . ARG A 193 ? 0.49449 0.35302 0.38295 -0.09577 -0.01365 -0.02456 189 ARG A NH1 
1479 N NH2 . ARG A 193 ? 0.63419 0.44586 0.49009 -0.08809 -0.01303 -0.02935 189 ARG A NH2 
1480 N N   A THR A 194 ? 0.29093 0.12923 0.16892 -0.01888 -0.00563 -0.00374 190 THR A N   
1481 N N   B THR A 194 ? 0.29206 0.13050 0.17015 -0.01879 -0.00563 -0.00365 190 THR A N   
1482 C CA  A THR A 194 ? 0.30822 0.12677 0.17375 -0.00667 -0.00518 -0.00231 190 THR A CA  
1483 C CA  B THR A 194 ? 0.30959 0.12747 0.17470 -0.00682 -0.00516 -0.00234 190 THR A CA  
1484 C C   A THR A 194 ? 0.29392 0.11263 0.15949 -0.00238 -0.00577 0.00387  190 THR A C   
1485 C C   B THR A 194 ? 0.29571 0.11508 0.16172 -0.00124 -0.00583 0.00377  190 THR A C   
1486 O O   A THR A 194 ? 0.30862 0.10315 0.15828 0.00210  -0.00577 0.00674  190 THR A O   
1487 O O   B THR A 194 ? 0.30861 0.10534 0.15976 0.00546  -0.00605 0.00644  190 THR A O   
1488 C CB  A THR A 194 ? 0.36589 0.19423 0.23716 0.00644  -0.00484 -0.00514 190 THR A CB  
1489 C CB  B THR A 194 ? 0.36012 0.18496 0.22902 0.00578  -0.00472 -0.00574 190 THR A CB  
1490 O OG1 A THR A 194 ? 0.49606 0.35280 0.38602 0.01026  -0.00537 -0.00299 190 THR A OG1 
1491 O OG1 B THR A 194 ? 0.36521 0.16527 0.21859 0.01636  -0.00400 -0.00643 190 THR A OG1 
1492 C CG2 A THR A 194 ? 0.27904 0.10700 0.14779 0.00216  -0.00418 -0.01113 190 THR A CG2 
1493 C CG2 B THR A 194 ? 0.40273 0.25432 0.28937 0.01380  -0.00517 -0.00328 190 THR A CG2 
1494 N N   . ARG A 195 ? 0.28213 0.12630 0.16376 -0.00352 -0.00647 0.00597  191 ARG A N   
1495 C CA  . ARG A 195 ? 0.31317 0.15872 0.19383 0.00020  -0.00751 0.01123  191 ARG A CA  
1496 C C   . ARG A 195 ? 0.31727 0.14413 0.18398 -0.01034 -0.00583 0.01468  191 ARG A C   
1497 O O   . ARG A 195 ? 0.31265 0.12376 0.16627 -0.00570 -0.00642 0.01949  191 ARG A O   
1498 C CB  . ARG A 195 ? 0.23450 0.11021 0.13456 -0.00001 -0.00832 0.01152  191 ARG A CB  
1499 C CG  . ARG A 195 ? 0.22924 0.12144 0.14140 0.01143  -0.00963 0.00959  191 ARG A CG  
1500 C CD  . ARG A 195 ? 0.24865 0.16816 0.17981 0.00820  -0.00955 0.00847  191 ARG A CD  
1501 N NE  . ARG A 195 ? 0.27113 0.20565 0.21340 0.01792  -0.01017 0.00708  191 ARG A NE  
1502 C CZ  . ARG A 195 ? 0.42484 0.36302 0.37079 0.02160  -0.00837 0.00401  191 ARG A CZ  
1503 N NH1 . ARG A 195 ? 0.32483 0.25239 0.26334 0.01696  -0.00671 0.00167  191 ARG A NH1 
1504 N NH2 . ARG A 195 ? 0.34932 0.30285 0.30642 0.02959  -0.00808 0.00296  191 ARG A NH2 
1505 N N   . ILE A 196 ? 0.27581 0.10423 0.14467 -0.02460 -0.00371 0.01238  192 ILE A N   
1506 C CA  . ILE A 196 ? 0.34677 0.15844 0.20339 -0.03679 -0.00086 0.01511  192 ILE A CA  
1507 C C   . ILE A 196 ? 0.44174 0.21758 0.27600 -0.03656 -0.00010 0.01551  192 ILE A C   
1508 O O   . ILE A 196 ? 0.40839 0.16185 0.22600 -0.04005 0.00190  0.02036  192 ILE A O   
1509 C CB  . ILE A 196 ? 0.30295 0.13121 0.17183 -0.05202 0.00096  0.01171  192 ILE A CB  
1510 C CG1 . ILE A 196 ? 0.34546 0.20547 0.23427 -0.05101 0.00060  0.01189  192 ILE A CG1 
1511 C CG2 . ILE A 196 ? 0.45891 0.27084 0.31626 -0.06651 0.00498  0.01378  192 ILE A CG2 
1512 C CD1 . ILE A 196 ? 0.44785 0.32936 0.35303 -0.05969 0.00041  0.00736  192 ILE A CD1 
1513 N N   . ARG A 197 ? 0.33601 0.10402 0.16782 -0.03224 -0.00131 0.01047  193 ARG A N   
1514 C CA  . ARG A 197 ? 0.37179 0.10350 0.18144 -0.03087 -0.00052 0.00980  193 ARG A CA  
1515 C C   . ARG A 197 ? 0.39102 0.10360 0.18680 -0.01578 -0.00163 0.01540  193 ARG A C   
1516 O O   . ARG A 197 ? 0.42638 0.11618 0.20604 -0.01681 -0.00024 0.01785  193 ARG A O   
1517 C CB  . ARG A 197 ? 0.39276 0.12230 0.20279 -0.02723 -0.00153 0.00245  193 ARG A CB  
1518 C CG  . ARG A 197 ? 0.59999 0.31479 0.40164 -0.04244 -0.00041 -0.00280 193 ARG A CG  
1519 C CD  . ARG A 197 ? 0.49313 0.19797 0.28809 -0.03599 -0.00126 -0.00974 193 ARG A CD  
1520 N NE  . ARG A 197 ? 0.51794 0.24588 0.32633 -0.02504 -0.00272 -0.01228 193 ARG A NE  
1521 C CZ  . ARG A 197 ? 0.47555 0.19954 0.28104 -0.00817 -0.00241 -0.01306 193 ARG A CZ  
1522 N NH1 . ARG A 197 ? 0.44860 0.14278 0.23651 0.00135  -0.00149 -0.01191 193 ARG A NH1 
1523 N NH2 . ARG A 197 ? 0.46516 0.21553 0.28566 -0.00053 -0.00272 -0.01505 193 ARG A NH2 
1524 N N   . TYR A 198 ? 0.37179 0.10448 0.17938 -0.00110 -0.00440 0.01645  194 TYR A N   
1525 C CA  . TYR A 198 ? 0.38753 0.10803 0.18521 0.01488  -0.00690 0.02141  194 TYR A CA  
1526 C C   . TYR A 198 ? 0.38678 0.11142 0.18184 0.01308  -0.00781 0.02854  194 TYR A C   
1527 O O   . TYR A 198 ? 0.40411 0.11726 0.18836 0.02511  -0.01056 0.03331  194 TYR A O   
1528 C CB  . TYR A 198 ? 0.36822 0.11121 0.18141 0.03113  -0.00961 0.01851  194 TYR A CB  
1529 C CG  . TYR A 198 ? 0.40583 0.13546 0.21358 0.04018  -0.00868 0.01304  194 TYR A CG  
1530 C CD1 . TYR A 198 ? 0.38926 0.12862 0.20494 0.03370  -0.00650 0.00629  194 TYR A CD1 
1531 C CD2 . TYR A 198 ? 0.46628 0.17503 0.26088 0.05584  -0.01001 0.01439  194 TYR A CD2 
1532 C CE1 . TYR A 198 ? 0.44789 0.17462 0.25677 0.04207  -0.00506 0.00073  194 TYR A CE1 
1533 C CE2 . TYR A 198 ? 0.47549 0.17706 0.26735 0.06385  -0.00827 0.00848  194 TYR A CE2 
1534 C CZ  . TYR A 198 ? 0.44216 0.14724 0.23803 0.05774  -0.00561 0.00171  194 TYR A CZ  
1535 O OH  . TYR A 198 ? 0.47289 0.17138 0.26474 0.06555  -0.00340 -0.00434 194 TYR A OH  
1536 N N   . ASN A 199 ? 0.36786 0.11065 0.17304 -0.00099 -0.00565 0.02881  195 ASN A N   
1537 C CA  . ASN A 199 ? 0.41602 0.16784 0.22072 -0.00262 -0.00600 0.03437  195 ASN A CA  
1538 C C   . ASN A 199 ? 0.45650 0.22693 0.27047 0.01355  -0.01128 0.03554  195 ASN A C   
1539 O O   . ASN A 199 ? 0.36310 0.12652 0.16605 0.02058  -0.01403 0.04113  195 ASN A O   
1540 C CB  . ASN A 199 ? 0.39860 0.12033 0.17926 -0.00717 -0.00369 0.04039  195 ASN A CB  
1541 C CG  . ASN A 199 ? 0.42269 0.15407 0.20147 -0.01187 -0.00265 0.04548  195 ASN A CG  
1542 O OD1 . ASN A 199 ? 0.43486 0.19144 0.22889 -0.01846 -0.00150 0.04389  195 ASN A OD1 
1543 N ND2 . ASN A 199 ? 0.42115 0.13727 0.18421 -0.00775 -0.00294 0.05007  195 ASN A ND2 
1544 N N   . ARG A 200 ? 0.32313 0.11798 0.15731 0.01900  -0.01281 0.03010  196 ARG A N   
1545 C CA  . ARG A 200 ? 0.30847 0.12411 0.15503 0.03296  -0.01742 0.02975  196 ARG A CA  
1546 C C   . ARG A 200 ? 0.33653 0.18595 0.20708 0.02779  -0.01691 0.02568  196 ARG A C   
1547 O O   . ARG A 200 ? 0.56714 0.42377 0.44663 0.01942  -0.01383 0.02166  196 ARG A O   
1548 C CB  . ARG A 200 ? 0.43938 0.24881 0.28575 0.04756  -0.01916 0.02715  196 ARG A CB  
1549 C CG  . ARG A 200 ? 0.53452 0.30816 0.35676 0.05571  -0.01998 0.03072  196 ARG A CG  
1550 C CD  . ARG A 200 ? 0.61675 0.39343 0.44314 0.07502  -0.02316 0.02871  196 ARG A CD  
1551 N NE  . ARG A 200 ? 0.89338 0.63961 0.70226 0.08159  -0.02179 0.02812  196 ARG A NE  
1552 C CZ  . ARG A 200 ? 0.85987 0.60962 0.67261 0.09707  -0.02321 0.02541  196 ARG A CZ  
1553 N NH1 . ARG A 200 ? 0.93853 0.71692 0.77001 0.10890  -0.02647 0.02386  196 ARG A NH1 
1554 N NH2 . ARG A 200 ? 0.91284 0.63829 0.71118 0.10010  -0.02108 0.02393  196 ARG A NH2 
1555 N N   . ARG A 201 ? 0.25994 0.12880 0.13973 0.03293  -0.02037 0.02667  197 ARG A N   
1556 C CA  . ARG A 201 ? 0.27000 0.16889 0.17182 0.02997  -0.02029 0.02279  197 ARG A CA  
1557 C C   . ARG A 201 ? 0.28919 0.20308 0.20434 0.04164  -0.02262 0.01967  197 ARG A C   
1558 O O   . ARG A 201 ? 0.24788 0.15645 0.15778 0.05404  -0.02630 0.02118  197 ARG A O   
1559 C CB  . ARG A 201 ? 0.28943 0.20082 0.19354 0.02705  -0.02225 0.02459  197 ARG A CB  
1560 C CG  . ARG A 201 ? 0.31919 0.23355 0.21955 0.03917  -0.02849 0.02689  197 ARG A CG  
1561 C CD  . ARG A 201 ? 0.47228 0.40526 0.37952 0.03588  -0.03073 0.02622  197 ARG A CD  
1562 N NE  . ARG A 201 ? 0.42802 0.34887 0.32002 0.02725  -0.02823 0.02970  197 ARG A NE  
1563 C CZ  . ARG A 201 ? 0.36482 0.29842 0.26073 0.02067  -0.02740 0.02836  197 ARG A CZ  
1564 N NH1 . ARG A 201 ? 0.42630 0.38343 0.34047 0.02096  -0.02921 0.02359  197 ARG A NH1 
1565 N NH2 . ARG A 201 ? 0.32002 0.24158 0.20052 0.01325  -0.02401 0.03167  197 ARG A NH2 
1566 N N   . SER A 202 ? 0.22498 0.15763 0.15715 0.03787  -0.02021 0.01548  198 SER A N   
1567 C CA  . SER A 202 ? 0.19545 0.14469 0.14173 0.04680  -0.02077 0.01230  198 SER A CA  
1568 C C   . SER A 202 ? 0.16363 0.13382 0.12728 0.03931  -0.01795 0.00911  198 SER A C   
1569 O O   . SER A 202 ? 0.15691 0.12479 0.12002 0.02915  -0.01531 0.00881  198 SER A O   
1570 C CB  . SER A 202 ? 0.33554 0.27036 0.27456 0.05428  -0.01877 0.01072  198 SER A CB  
1571 O OG  . SER A 202 ? 0.29866 0.22651 0.23520 0.04546  -0.01448 0.00850  198 SER A OG  
1572 N N   . ALA A 203 ? 0.15206 0.14270 0.13118 0.04453  -0.01859 0.00683  199 ALA A N   
1573 C CA  . ALA A 203 ? 0.13235 0.14065 0.12674 0.03807  -0.01552 0.00431  199 ALA A CA  
1574 C C   . ALA A 203 ? 0.14798 0.15140 0.14113 0.03696  -0.01070 0.00254  199 ALA A C   
1575 O O   . ALA A 203 ? 0.14653 0.13874 0.13153 0.04388  -0.00973 0.00184  199 ALA A O   
1576 C CB  . ALA A 203 ? 0.17225 0.20313 0.18310 0.04273  -0.01711 0.00225  199 ALA A CB  
1577 N N   . PRO A 204 ? 0.14017 0.15061 0.13980 0.02890  -0.00783 0.00172  200 PRO A N   
1578 C CA  . PRO A 204 ? 0.14673 0.15305 0.14347 0.02796  -0.00379 0.00017  200 PRO A CA  
1579 C C   . PRO A 204 ? 0.16709 0.18517 0.17227 0.03506  -0.00054 -0.00196 200 PRO A C   
1580 O O   . PRO A 204 ? 0.16513 0.20087 0.18427 0.03623  -0.00051 -0.00245 200 PRO A O   
1581 C CB  . PRO A 204 ? 0.18494 0.19728 0.18689 0.01850  -0.00268 0.00068  200 PRO A CB  
1582 C CG  . PRO A 204 ? 0.17328 0.19903 0.18664 0.01663  -0.00437 0.00122  200 PRO A CG  
1583 C CD  . PRO A 204 ? 0.12204 0.14304 0.13033 0.02103  -0.00829 0.00212  200 PRO A CD  
1584 N N   . ASP A 205 ? 0.15746 0.16609 0.15411 0.03931  0.00254  -0.00376 201 ASP A N   
1585 C CA  . ASP A 205 ? 0.15032 0.16950 0.15361 0.04680  0.00700  -0.00627 201 ASP A CA  
1586 C C   . ASP A 205 ? 0.12641 0.15609 0.13576 0.04060  0.01214  -0.00660 201 ASP A C   
1587 O O   . ASP A 205 ? 0.15351 0.18010 0.16047 0.03193  0.01135  -0.00484 201 ASP A O   
1588 C CB  . ASP A 205 ? 0.24589 0.24799 0.23518 0.05533  0.00835  -0.00854 201 ASP A CB  
1589 C CG  . ASP A 205 ? 0.35640 0.34124 0.33027 0.04979  0.01018  -0.00977 201 ASP A CG  
1590 O OD1 . ASP A 205 ? 0.30398 0.29347 0.27937 0.04108  0.01128  -0.00898 201 ASP A OD1 
1591 O OD2 . ASP A 205 ? 0.39137 0.35698 0.35071 0.05462  0.01013  -0.01178 201 ASP A OD2 
1592 N N   . PRO A 206 ? 0.09467 0.21913 0.12871 -0.00514 -0.00312 -0.01867 202 PRO A N   
1593 C CA  . PRO A 206 ? 0.14201 0.26103 0.17597 -0.01369 0.00072  -0.02107 202 PRO A CA  
1594 C C   . PRO A 206 ? 0.17599 0.27834 0.20364 -0.01479 0.00320  -0.01689 202 PRO A C   
1595 O O   . PRO A 206 ? 0.15318 0.24609 0.17690 -0.02069 0.00525  -0.01752 202 PRO A O   
1596 C CB  . PRO A 206 ? 0.17595 0.31014 0.21817 -0.01617 0.00283  -0.02501 202 PRO A CB  
1597 C CG  . PRO A 206 ? 0.15475 0.30474 0.20234 -0.00961 -0.00131 -0.02768 202 PRO A CG  
1598 C CD  . PRO A 206 ? 0.10369 0.24403 0.14449 -0.00130 -0.00471 -0.02240 202 PRO A CD  
1599 N N   . SER A 207 ? 0.08224 0.17917 0.10821 -0.00920 0.00196  -0.01293 203 SER A N   
1600 C CA  . SER A 207 ? 0.11943 0.20115 0.13988 -0.00985 0.00287  -0.00977 203 SER A CA  
1601 C C   . SER A 207 ? 0.11762 0.19152 0.13428 -0.01105 0.00213  -0.00723 203 SER A C   
1602 O O   . SER A 207 ? 0.11615 0.17912 0.12782 -0.01345 0.00343  -0.00702 203 SER A O   
1603 C CB  . SER A 207 ? 0.13471 0.21120 0.15476 -0.00379 -0.00049 -0.00682 203 SER A CB  
1604 O OG  . SER A 207 ? 0.11972 0.19571 0.14105 -0.00092 -0.00448 -0.00203 203 SER A OG  
1605 N N   . VAL A 208 ? 0.13765 0.21822 0.15570 -0.00824 0.00004  -0.00535 204 VAL A N   
1606 C CA  . VAL A 208 ? 0.11190 0.19004 0.12649 -0.00746 -0.00018 -0.00337 204 VAL A CA  
1607 C C   . VAL A 208 ? 0.10811 0.18332 0.11832 -0.01026 0.00057  -0.00927 204 VAL A C   
1608 O O   . VAL A 208 ? 0.10868 0.17435 0.11351 -0.01035 0.00071  -0.00971 204 VAL A O   
1609 C CB  . VAL A 208 ? 0.08147 0.17017 0.09744 -0.00302 -0.00183 0.00102  204 VAL A CB  
1610 C CG1 . VAL A 208 ? 0.11957 0.21125 0.13172 -0.00062 -0.00113 0.00225  204 VAL A CG1 
1611 C CG2 . VAL A 208 ? 0.15765 0.24412 0.17696 -0.00173 -0.00385 0.00818  204 VAL A CG2 
1612 N N   . ILE A 209 ? 0.09269 0.17521 0.10509 -0.01236 -0.00010 -0.01422 205 ILE A N   
1613 C CA  . ILE A 209 ? 0.09743 0.17509 0.10578 -0.01582 -0.00148 -0.02016 205 ILE A CA  
1614 C C   . ILE A 209 ? 0.11519 0.17759 0.11954 -0.02230 0.00044  -0.02065 205 ILE A C   
1615 O O   . ILE A 209 ? 0.12621 0.17546 0.12271 -0.02286 -0.00132 -0.02285 205 ILE A O   
1616 C CB  . ILE A 209 ? 0.10513 0.19499 0.11896 -0.01811 -0.00372 -0.02544 205 ILE A CB  
1617 C CG1 . ILE A 209 ? 0.13751 0.23979 0.15098 -0.00998 -0.00644 -0.02501 205 ILE A CG1 
1618 C CG2 . ILE A 209 ? 0.15563 0.23725 0.16651 -0.02452 -0.00653 -0.03187 205 ILE A CG2 
1619 C CD1 . ILE A 209 ? 0.28997 0.40700 0.30994 -0.00992 -0.00908 -0.02909 205 ILE A CD1 
1620 N N   . THR A 210 ? 0.10150 0.16478 0.10941 -0.02598 0.00378  -0.01847 206 THR A N   
1621 C CA  . THR A 210 ? 0.11013 0.15993 0.11257 -0.03205 0.00637  -0.01764 206 THR A CA  
1622 C C   . THR A 210 ? 0.16178 0.19667 0.15569 -0.02773 0.00596  -0.01462 206 THR A C   
1623 O O   . THR A 210 ? 0.14547 0.16444 0.13059 -0.03058 0.00574  -0.01483 206 THR A O   
1624 C CB  . THR A 210 ? 0.16169 0.22058 0.16940 -0.03543 0.01070  -0.01629 206 THR A CB  
1625 O OG1 . THR A 210 ? 0.16047 0.23288 0.17637 -0.04195 0.01115  -0.01961 206 THR A OG1 
1626 C CG2 . THR A 210 ? 0.16822 0.21376 0.16777 -0.03920 0.01433  -0.01327 206 THR A CG2 
1627 N N   . LEU A 211 ? 0.15778 0.19698 0.15415 -0.02117 0.00506  -0.01160 207 LEU A N   
1628 C CA  . LEU A 211 ? 0.16357 0.19226 0.15435 -0.01716 0.00363  -0.00932 207 LEU A CA  
1629 C C   . LEU A 211 ? 0.11225 0.13610 0.09738 -0.01433 0.00113  -0.01191 207 LEU A C   
1630 O O   . LEU A 211 ? 0.15194 0.16186 0.12858 -0.01290 -0.00016 -0.01258 207 LEU A O   
1631 C CB  . LEU A 211 ? 0.11608 0.15206 0.11308 -0.01258 0.00213  -0.00513 207 LEU A CB  
1632 C CG  . LEU A 211 ? 0.18707 0.21991 0.18554 -0.01210 0.00187  -0.00305 207 LEU A CG  
1633 C CD1 . LEU A 211 ? 0.16159 0.19929 0.16675 -0.00902 -0.00165 0.00143  207 LEU A CD1 
1634 C CD2 . LEU A 211 ? 0.14584 0.16434 0.13577 -0.01215 0.00203  -0.00348 207 LEU A CD2 
1635 N N   . GLU A 212 ? 0.10949 0.14459 0.09774 -0.01183 -0.00019 -0.01388 208 GLU A N   
1636 C CA  . GLU A 212 ? 0.12586 0.15733 0.10706 -0.00708 -0.00319 -0.01803 208 GLU A CA  
1637 C C   . GLU A 212 ? 0.15751 0.16978 0.12945 -0.01173 -0.00534 -0.02270 208 GLU A C   
1638 O O   . GLU A 212 ? 0.17348 0.17174 0.13558 -0.00757 -0.00820 -0.02481 208 GLU A O   
1639 C CB  . GLU A 212 ? 0.15139 0.19834 0.13567 -0.00345 -0.00440 -0.02017 208 GLU A CB  
1640 C CG  . GLU A 212 ? 0.10396 0.16821 0.09520 0.00111  -0.00254 -0.01382 208 GLU A CG  
1641 C CD  . GLU A 212 ? 0.17888 0.25821 0.17102 0.00504  -0.00342 -0.01494 208 GLU A CD  
1642 O OE1 . GLU A 212 ? 0.17827 0.25532 0.16645 0.00463  -0.00626 -0.02202 208 GLU A OE1 
1643 O OE2 . GLU A 212 ? 0.15520 0.24802 0.15158 0.00822  -0.00185 -0.00839 208 GLU A OE2 
1644 N N   . ASN A 213 ? 0.13687 0.14830 0.11199 -0.02061 -0.00439 -0.02395 209 ASN A N   
1645 C CA  . ASN A 213 ? 0.16973 0.16257 0.13728 -0.02799 -0.00667 -0.02681 209 ASN A CA  
1646 C C   . ASN A 213 ? 0.23570 0.21003 0.19426 -0.03010 -0.00502 -0.02285 209 ASN A C   
1647 O O   . ASN A 213 ? 0.20544 0.15854 0.15332 -0.03379 -0.00824 -0.02425 209 ASN A O   
1648 C CB  . ASN A 213 ? 0.15469 0.15597 0.13106 -0.03875 -0.00512 -0.02755 209 ASN A CB  
1649 C CG  . ASN A 213 ? 0.16667 0.18302 0.14970 -0.03679 -0.00875 -0.03298 209 ASN A CG  
1650 O OD1 . ASN A 213 ? 0.15872 0.17570 0.13683 -0.02787 -0.01278 -0.03669 209 ASN A OD1 
1651 N ND2 . ASN A 213 ? 0.15764 0.18800 0.15151 -0.04428 -0.00741 -0.03370 209 ASN A ND2 
1652 N N   . SER A 214 ? 0.15985 0.13982 0.12113 -0.02746 -0.00114 -0.01808 210 SER A N   
1653 C CA  . SER A 214 ? 0.16628 0.13104 0.11873 -0.02912 0.00069  -0.01424 210 SER A CA  
1654 C C   . SER A 214 ? 0.21628 0.17223 0.16125 -0.01945 -0.00242 -0.01401 210 SER A C   
1655 O O   . SER A 214 ? 0.23497 0.17790 0.17121 -0.01899 -0.00193 -0.01124 210 SER A O   
1656 C CB  . SER A 214 ? 0.20644 0.18287 0.16553 -0.03188 0.00610  -0.01033 210 SER A CB  
1657 O OG  . SER A 214 ? 0.26947 0.25760 0.23651 -0.04005 0.00929  -0.01070 210 SER A OG  
1658 N N   . TRP A 215 ? 0.15866 0.12345 0.10680 -0.01126 -0.00551 -0.01671 211 TRP A N   
1659 C CA  . TRP A 215 ? 0.16395 0.12763 0.10915 -0.00206 -0.00804 -0.01621 211 TRP A CA  
1660 C C   . TRP A 215 ? 0.19356 0.13262 0.12254 0.00078  -0.01175 -0.01771 211 TRP A C   
1661 O O   . TRP A 215 ? 0.18892 0.12182 0.11343 0.00467  -0.01271 -0.01565 211 TRP A O   
1662 C CB  . TRP A 215 ? 0.15105 0.13150 0.10210 0.00598  -0.00986 -0.01850 211 TRP A CB  
1663 C CG  . TRP A 215 ? 0.14913 0.13569 0.10123 0.01492  -0.01197 -0.01761 211 TRP A CG  
1664 C CD1 . TRP A 215 ? 0.15588 0.15326 0.11755 0.01492  -0.01112 -0.01291 211 TRP A CD1 
1665 C CD2 . TRP A 215 ? 0.16051 0.14436 0.10476 0.02552  -0.01617 -0.02208 211 TRP A CD2 
1666 N NE1 . TRP A 215 ? 0.18807 0.19192 0.15030 0.02351  -0.01414 -0.01367 211 TRP A NE1 
1667 C CE2 . TRP A 215 ? 0.15331 0.15026 0.10471 0.03107  -0.01685 -0.01941 211 TRP A CE2 
1668 C CE3 . TRP A 215 ? 0.23214 0.20344 0.16378 0.03151  -0.02040 -0.02877 211 TRP A CE3 
1669 C CZ2 . TRP A 215 ? 0.16145 0.16307 0.10888 0.04298  -0.02059 -0.02304 211 TRP A CZ2 
1670 C CZ3 . TRP A 215 ? 0.22660 0.19943 0.15195 0.04473  -0.02467 -0.03297 211 TRP A CZ3 
1671 C CH2 . TRP A 215 ? 0.17866 0.16844 0.11244 0.05062  -0.02422 -0.03001 211 TRP A CH2 
1672 N N   . GLY A 216 ? 0.19726 0.12011 0.11635 -0.00098 -0.01497 -0.02143 212 GLY A N   
1673 C CA  . GLY A 216 ? 0.22220 0.11706 0.12349 0.00169  -0.01965 -0.02234 212 GLY A CA  
1674 C C   . GLY A 216 ? 0.27641 0.15614 0.17017 -0.00656 -0.01635 -0.01620 212 GLY A C   
1675 O O   . GLY A 216 ? 0.27117 0.13508 0.15253 -0.00129 -0.01876 -0.01457 212 GLY A O   
1676 N N   . ARG A 217 ? 0.29505 0.18110 0.19560 -0.01867 -0.01075 -0.01273 213 ARG A N   
1677 C CA  . ARG A 217 ? 0.29464 0.17171 0.18841 -0.02601 -0.00599 -0.00619 213 ARG A CA  
1678 C C   . ARG A 217 ? 0.22856 0.11542 0.12429 -0.01910 -0.00377 -0.00400 213 ARG A C   
1679 O O   . ARG A 217 ? 0.27240 0.14532 0.15524 -0.01801 -0.00314 -0.00019 213 ARG A O   
1680 C CB  . ARG A 217 ? 0.30267 0.19191 0.20635 -0.03922 0.00009  -0.00351 213 ARG A CB  
1681 C CG  . ARG A 217 ? 0.50336 0.38555 0.40837 -0.04782 -0.00316 -0.00630 213 ARG A CG  
1682 C CD  . ARG A 217 ? 0.58682 0.48952 0.50662 -0.05971 0.00265  -0.00457 213 ARG A CD  
1683 N NE  . ARG A 217 ? 0.63460 0.54237 0.56273 -0.06358 -0.00194 -0.01048 213 ARG A NE  
1684 C CZ  . ARG A 217 ? 0.63743 0.52763 0.56076 -0.07344 -0.00667 -0.01142 213 ARG A CZ  
1685 N NH1 . ARG A 217 ? 0.76161 0.62683 0.67160 -0.08157 -0.00694 -0.00551 213 ARG A NH1 
1686 N NH2 . ARG A 217 ? 0.65585 0.55224 0.58701 -0.07529 -0.01205 -0.01827 213 ARG A NH2 
1687 N N   . LEU A 218 ? 0.22034 0.12996 0.13127 -0.01462 -0.00325 -0.00611 214 LEU A N   
1688 C CA  . LEU A 218 ? 0.28224 0.19960 0.19618 -0.00883 -0.00315 -0.00473 214 LEU A CA  
1689 C C   . LEU A 218 ? 0.28281 0.18880 0.18760 0.00098  -0.00912 -0.00611 214 LEU A C   
1690 O O   . LEU A 218 ? 0.25987 0.15950 0.15756 0.00461  -0.01016 -0.00450 214 LEU A O   
1691 C CB  . LEU A 218 ? 0.25830 0.19937 0.19029 -0.00751 -0.00261 -0.00581 214 LEU A CB  
1692 C CG  . LEU A 218 ? 0.17081 0.12579 0.11247 -0.01439 0.00242  -0.00488 214 LEU A CG  
1693 C CD1 . LEU A 218 ? 0.19436 0.16847 0.15115 -0.01204 0.00126  -0.00569 214 LEU A CD1 
1694 C CD2 . LEU A 218 ? 0.27589 0.23006 0.21350 -0.01543 0.00578  -0.00253 214 LEU A CD2 
1695 N N   . SER A 219 ? 0.20612 0.11081 0.11054 0.00673  -0.01360 -0.00980 215 SER A N   
1696 C CA  . SER A 219 ? 0.24236 0.13846 0.13839 0.01750  -0.01976 -0.01193 215 SER A CA  
1697 C C   . SER A 219 ? 0.25127 0.11886 0.12571 0.01803  -0.02158 -0.00986 215 SER A C   
1698 O O   . SER A 219 ? 0.24574 0.10677 0.11249 0.02523  -0.02515 -0.00957 215 SER A O   
1699 C CB  . SER A 219 ? 0.23887 0.13953 0.13643 0.02502  -0.02387 -0.01698 215 SER A CB  
1700 O OG  . SER A 219 ? 0.21958 0.14792 0.13563 0.02534  -0.02179 -0.01749 215 SER A OG  
1701 N N   . THR A 220 ? 0.25815 0.10830 0.12246 0.00994  -0.01968 -0.00794 216 THR A N   
1702 C CA  . THR A 220 ? 0.33971 0.16069 0.18212 0.00842  -0.02092 -0.00382 216 THR A CA  
1703 C C   . THR A 220 ? 0.32760 0.15050 0.16611 0.00517  -0.01562 0.00187  216 THR A C   
1704 O O   . THR A 220 ? 0.29992 0.10755 0.12254 0.01169  -0.01851 0.00384  216 THR A O   
1705 C CB  . THR A 220 ? 0.30846 0.11192 0.14382 -0.00264 -0.02011 -0.00187 216 THR A CB  
1706 O OG1 . THR A 220 ? 0.34223 0.13986 0.17710 0.00316  -0.02702 -0.00871 216 THR A OG1 
1707 C CG2 . THR A 220 ? 0.33572 0.10793 0.14799 -0.00672 -0.02069 0.00492  216 THR A CG2 
1708 N N   . ALA A 221 ? 0.26828 0.11034 0.11998 -0.00326 -0.00840 0.00392  217 ALA A N   
1709 C CA  . ALA A 221 ? 0.33438 0.17989 0.18122 -0.00504 -0.00308 0.00844  217 ALA A CA  
1710 C C   . ALA A 221 ? 0.29145 0.14111 0.13738 0.00669  -0.00783 0.00564  217 ALA A C   
1711 O O   . ALA A 221 ? 0.27721 0.11689 0.10810 0.01048  -0.00760 0.00843  217 ALA A O   
1712 C CB  . ALA A 221 ? 0.24960 0.11822 0.11254 -0.01332 0.00424  0.00919  217 ALA A CB  
1713 N N   . ILE A 222 ? 0.27988 0.14493 0.14178 0.01220  -0.01246 0.00046  218 ILE A N   
1714 C CA  . ILE A 222 ? 0.27085 0.14152 0.13545 0.02149  -0.01830 -0.00237 218 ILE A CA  
1715 C C   . ILE A 222 ? 0.25759 0.10987 0.10575 0.03102  -0.02525 -0.00346 218 ILE A C   
1716 O O   . ILE A 222 ? 0.32070 0.16534 0.15758 0.03729  -0.02850 -0.00333 218 ILE A O   
1717 C CB  . ILE A 222 ? 0.21436 0.10776 0.10199 0.02243  -0.02099 -0.00581 218 ILE A CB  
1718 C CG1 . ILE A 222 ? 0.19667 0.10556 0.09754 0.01516  -0.01557 -0.00465 218 ILE A CG1 
1719 C CG2 . ILE A 222 ? 0.22199 0.12050 0.11418 0.03082  -0.02894 -0.00866 218 ILE A CG2 
1720 C CD1 . ILE A 222 ? 0.19827 0.12725 0.11992 0.01386  -0.01689 -0.00592 218 ILE A CD1 
1721 N N   . GLN A 223 ? 0.26742 0.11149 0.11229 0.03369  -0.02842 -0.00522 219 GLN A N   
1722 C CA  . GLN A 223 ? 0.28478 0.11254 0.11458 0.04515  -0.03638 -0.00738 219 GLN A CA  
1723 C C   . GLN A 223 ? 0.34486 0.14269 0.14731 0.04501  -0.03588 -0.00222 219 GLN A C   
1724 O O   . GLN A 223 ? 0.47415 0.25722 0.26108 0.05572  -0.04280 -0.00330 219 GLN A O   
1725 C CB  . GLN A 223 ? 0.30666 0.13516 0.13996 0.05048  -0.04065 -0.01189 219 GLN A CB  
1726 C CG  . GLN A 223 ? 0.30219 0.16215 0.16013 0.05402  -0.04226 -0.01618 219 GLN A CG  
1727 C CD  . GLN A 223 ? 0.27788 0.14361 0.13971 0.05932  -0.04445 -0.02056 219 GLN A CD  
1728 O OE1 . GLN A 223 ? 0.36847 0.22086 0.21717 0.07036  -0.05093 -0.02428 219 GLN A OE1 
1729 N NE2 . GLN A 223 ? 0.23959 0.12510 0.11801 0.05299  -0.03959 -0.02062 219 GLN A NE2 
1730 N N   . GLU A 224 ? 0.32317 0.11297 0.11946 0.03311  -0.02795 0.00392  220 GLU A N   
1731 C CA  . GLU A 224 ? 0.40254 0.16614 0.17313 0.03092  -0.02597 0.01123  220 GLU A CA  
1732 C C   . GLU A 224 ? 0.38758 0.15817 0.15269 0.03086  -0.02095 0.01491  220 GLU A C   
1733 O O   . GLU A 224 ? 0.38167 0.13310 0.12376 0.03058  -0.01875 0.02178  220 GLU A O   
1734 C CB  . GLU A 224 ? 0.39207 0.14286 0.15817 0.01671  -0.02029 0.01716  220 GLU A CB  
1735 C CG  . GLU A 224 ? 0.42313 0.15757 0.18658 0.01811  -0.02710 0.01346  220 GLU A CG  
1736 C CD  . GLU A 224 ? 0.61022 0.32535 0.36576 0.00333  -0.02388 0.01975  220 GLU A CD  
1737 O OE1 . GLU A 224 ? 0.69367 0.41167 0.44748 -0.00892 -0.01508 0.02800  220 GLU A OE1 
1738 O OE2 . GLU A 224 ? 0.68637 0.38420 0.43763 0.00411  -0.03064 0.01620  220 GLU A OE2 
1739 N N   . SER A 225 ? 0.32814 0.12435 0.11211 0.03192  -0.01971 0.01059  221 SER A N   
1740 C CA  . SER A 225 ? 0.35424 0.15899 0.13425 0.03170  -0.01456 0.01282  221 SER A CA  
1741 C C   . SER A 225 ? 0.37389 0.16518 0.13302 0.04387  -0.02034 0.01256  221 SER A C   
1742 O O   . SER A 225 ? 0.38418 0.16770 0.13999 0.05390  -0.03010 0.00811  221 SER A O   
1743 C CB  . SER A 225 ? 0.36562 0.19690 0.16987 0.03139  -0.01453 0.00714  221 SER A CB  
1744 O OG  . SER A 225 ? 0.32035 0.15703 0.13382 0.04060  -0.02452 0.00053  221 SER A OG  
1745 N N   . ASN A 226 ? 0.36200 0.15271 0.10681 0.04386  -0.01427 0.01705  222 ASN A N   
1746 C CA  . ASN A 226 ? 0.45213 0.23412 0.17833 0.05594  -0.01894 0.01594  222 ASN A CA  
1747 C C   . ASN A 226 ? 0.43029 0.22972 0.16827 0.06354  -0.02465 0.00747  222 ASN A C   
1748 O O   . ASN A 226 ? 0.41689 0.22986 0.15783 0.06190  -0.01876 0.00730  222 ASN A O   
1749 C CB  . ASN A 226 ? 0.50221 0.28002 0.21242 0.05173  -0.00874 0.02437  222 ASN A CB  
1750 C CG  . ASN A 226 ? 0.63307 0.40503 0.32895 0.06385  -0.01261 0.02246  222 ASN A CG  
1751 O OD1 . ASN A 226 ? 0.55017 0.32228 0.24964 0.07527  -0.02305 0.01382  222 ASN A OD1 
1752 N ND2 . ASN A 226 ? 0.61516 0.38359 0.29570 0.06082  -0.00417 0.03088  222 ASN A ND2 
1753 N N   . GLN A 227 ? 0.41658 0.21734 0.16432 0.07152  -0.03654 -0.00013 223 GLN A N   
1754 C CA  . GLN A 227 ? 0.45684 0.27237 0.21967 0.07693  -0.04450 -0.00852 223 GLN A CA  
1755 C C   . GLN A 227 ? 0.47574 0.31082 0.26150 0.06767  -0.03879 -0.00952 223 GLN A C   
1756 O O   . GLN A 227 ? 0.42307 0.26638 0.21216 0.07070  -0.04040 -0.01357 223 GLN A O   
1757 C CB  . GLN A 227 ? 0.51425 0.32685 0.26593 0.08639  -0.04662 -0.01137 223 GLN A CB  
1758 C CG  . GLN A 227 ? 0.68614 0.48751 0.43106 0.09644  -0.05528 -0.01494 223 GLN A CG  
1759 C CD  . GLN A 227 ? 0.73951 0.53905 0.47509 0.10669  -0.05871 -0.01893 223 GLN A CD  
1760 O OE1 . GLN A 227 ? 0.83827 0.64276 0.56745 0.10686  -0.05250 -0.01723 223 GLN A OE1 
1761 N NE2 . GLN A 227 ? 0.77081 0.56461 0.50583 0.11605  -0.06876 -0.02489 223 GLN A NE2 
1762 N N   . GLY A 228 ? 0.40599 0.24722 0.20620 0.05751  -0.03307 -0.00637 224 GLY A N   
1763 C CA  . GLY A 228 ? 0.40717 0.26642 0.22882 0.04917  -0.02826 -0.00702 224 GLY A CA  
1764 C C   . GLY A 228 ? 0.33352 0.19735 0.15044 0.04171  -0.01603 -0.00177 224 GLY A C   
1765 O O   . GLY A 228 ? 0.33401 0.21190 0.16826 0.03394  -0.01145 -0.00157 224 GLY A O   
1766 N N   . ALA A 229 ? 0.34841 0.20257 0.14265 0.04381  -0.01052 0.00293  225 ALA A N   
1767 C CA  . ALA A 229 ? 0.34285 0.20581 0.13365 0.03631  0.00179  0.00869  225 ALA A CA  
1768 C C   . ALA A 229 ? 0.36186 0.21748 0.15223 0.02409  0.00813  0.01600  225 ALA A C   
1769 O O   . ALA A 229 ? 0.36027 0.19520 0.13604 0.02476  0.00522  0.01949  225 ALA A O   
1770 C CB  . ALA A 229 ? 0.35172 0.21051 0.11801 0.04373  0.00579  0.01164  225 ALA A CB  
1771 N N   . PHE A 230 ? 0.33751 0.20883 0.14321 0.01354  0.01556  0.01774  226 PHE A N   
1772 C CA  . PHE A 230 ? 0.37194 0.23679 0.17958 0.00080  0.02014  0.02353  226 PHE A CA  
1773 C C   . PHE A 230 ? 0.35714 0.21531 0.14667 -0.00633 0.02942  0.03369  226 PHE A C   
1774 O O   . PHE A 230 ? 0.40313 0.27469 0.18664 -0.00417 0.03646  0.03615  226 PHE A O   
1775 C CB  . PHE A 230 ? 0.34384 0.22934 0.17568 -0.00783 0.02344  0.02100  226 PHE A CB  
1776 C CG  . PHE A 230 ? 0.36426 0.25596 0.21373 -0.00333 0.01543  0.01342  226 PHE A CG  
1777 C CD1 . PHE A 230 ? 0.33950 0.21904 0.18519 0.00528  0.00628  0.00990  226 PHE A CD1 
1778 C CD2 . PHE A 230 ? 0.28856 0.19989 0.15849 -0.00784 0.01722  0.01046  226 PHE A CD2 
1779 C CE1 . PHE A 230 ? 0.28025 0.16900 0.14321 0.00812  0.00009  0.00454  226 PHE A CE1 
1780 C CE2 . PHE A 230 ? 0.27666 0.19414 0.16152 -0.00442 0.01071  0.00535  226 PHE A CE2 
1781 C CZ  . PHE A 230 ? 0.31230 0.21941 0.19420 0.00293  0.00264  0.00287  226 PHE A CZ  
1782 N N   . ALA A 231 ? 0.54336 0.38055 0.32362 -0.01477 0.02917  0.03989  227 ALA A N   
1783 C CA  . ALA A 231 ? 0.65194 0.48229 0.41760 -0.02584 0.03827  0.05171  227 ALA A CA  
1784 C C   . ALA A 231 ? 0.53906 0.39638 0.32335 -0.03912 0.04820  0.05439  227 ALA A C   
1785 O O   . ALA A 231 ? 0.64823 0.51997 0.42694 -0.04330 0.05848  0.06156  227 ALA A O   
1786 C CB  . ALA A 231 ? 0.67478 0.47232 0.42672 -0.03244 0.03341  0.05728  227 ALA A CB  
1787 N N   . SER A 232 ? 0.47048 0.33712 0.27688 -0.04502 0.04527  0.04858  228 SER A N   
1788 C CA  . SER A 232 ? 0.58882 0.48243 0.41536 -0.05649 0.05267  0.04928  228 SER A CA  
1789 C C   . SER A 232 ? 0.47526 0.38942 0.32353 -0.04936 0.04855  0.03832  228 SER A C   
1790 O O   . SER A 232 ? 0.56954 0.47333 0.42096 -0.04188 0.03950  0.03165  228 SER A O   
1791 C CB  . SER A 232 ? 0.56074 0.44260 0.39160 -0.07384 0.05251  0.05440  228 SER A CB  
1792 O OG  . SER A 232 ? 0.66328 0.51993 0.49130 -0.07051 0.04149  0.04923  228 SER A OG  
1793 N N   . PRO A 233 ? 0.47328 0.41741 0.33634 -0.05102 0.05500  0.03673  229 PRO A N   
1794 C CA  . PRO A 233 ? 0.42667 0.38813 0.30839 -0.04388 0.05061  0.02726  229 PRO A CA  
1795 C C   . PRO A 233 ? 0.33775 0.29803 0.23470 -0.05177 0.04600  0.02409  229 PRO A C   
1796 O O   . PRO A 233 ? 0.33284 0.28616 0.23039 -0.06460 0.04745  0.02836  229 PRO A O   
1797 C CB  . PRO A 233 ? 0.41891 0.41166 0.30954 -0.04348 0.05901  0.02717  229 PRO A CB  
1798 C CG  . PRO A 233 ? 0.51849 0.51179 0.39304 -0.04789 0.06837  0.03657  229 PRO A CG  
1799 C CD  . PRO A 233 ? 0.53237 0.49739 0.39548 -0.05886 0.06663  0.04390  229 PRO A CD  
1800 N N   . ILE A 234 ? 0.35846 0.32470 0.26691 -0.04382 0.03972  0.01663  230 ILE A N   
1801 C CA  . ILE A 234 ? 0.33266 0.30282 0.25566 -0.04827 0.03551  0.01261  230 ILE A CA  
1802 C C   . ILE A 234 ? 0.37626 0.37421 0.31653 -0.04682 0.03772  0.00871  230 ILE A C   
1803 O O   . ILE A 234 ? 0.34270 0.34915 0.28443 -0.03664 0.03675  0.00579  230 ILE A O   
1804 C CB  . ILE A 234 ? 0.30962 0.26555 0.23119 -0.04010 0.02674  0.00839  230 ILE A CB  
1805 C CG1 . ILE A 234 ? 0.51864 0.44764 0.42505 -0.04198 0.02318  0.01084  230 ILE A CG1 
1806 C CG2 . ILE A 234 ? 0.45326 0.42135 0.39082 -0.04068 0.02330  0.00357  230 ILE A CG2 
1807 C CD1 . ILE A 234 ? 0.59075 0.50384 0.47881 -0.03616 0.02329  0.01447  230 ILE A CD1 
1808 N N   . GLN A 235 ? 0.35152 0.36238 0.30416 -0.05654 0.03957  0.00826  231 GLN A N   
1809 C CA  . GLN A 235 ? 0.30874 0.34598 0.27781 -0.05433 0.04047  0.00397  231 GLN A CA  
1810 C C   . GLN A 235 ? 0.28705 0.32269 0.26359 -0.04839 0.03290  -0.00123 231 GLN A C   
1811 O O   . GLN A 235 ? 0.22070 0.24468 0.19677 -0.05216 0.02865  -0.00223 231 GLN A O   
1812 C CB  . GLN A 235 ? 0.36488 0.41980 0.34545 -0.06732 0.04507  0.00539  231 GLN A CB  
1813 C CG  . GLN A 235 ? 0.43332 0.50481 0.41298 -0.07245 0.05465  0.01067  231 GLN A CG  
1814 C CD  . GLN A 235 ? 0.56687 0.66432 0.56411 -0.08457 0.05837  0.01087  231 GLN A CD  
1815 O OE1 . GLN A 235 ? 0.56919 0.66534 0.57621 -0.09123 0.05289  0.00755  231 GLN A OE1 
1816 N NE2 . GLN A 235 ? 0.54723 0.67045 0.54884 -0.08673 0.06737  0.01425  231 GLN A NE2 
1817 N N   . LEU A 236 ? 0.16301 0.20971 0.14514 -0.03862 0.03095  -0.00430 232 LEU A N   
1818 C CA  . LEU A 236 ? 0.16327 0.21280 0.15342 -0.03359 0.02492  -0.00755 232 LEU A CA  
1819 C C   . LEU A 236 ? 0.21873 0.29149 0.22119 -0.03141 0.02562  -0.01062 232 LEU A C   
1820 O O   . LEU A 236 ? 0.18233 0.27071 0.18808 -0.03314 0.03079  -0.01085 232 LEU A O   
1821 C CB  . LEU A 236 ? 0.15812 0.19580 0.14306 -0.02427 0.02001  -0.00730 232 LEU A CB  
1822 C CG  . LEU A 236 ? 0.29691 0.31414 0.27135 -0.02430 0.01770  -0.00531 232 LEU A CG  
1823 C CD1 . LEU A 236 ? 0.22655 0.23714 0.19972 -0.01607 0.01228  -0.00530 232 LEU A CD1 
1824 C CD2 . LEU A 236 ? 0.28487 0.29713 0.26063 -0.02862 0.01554  -0.00599 232 LEU A CD2 
1825 N N   . GLN A 237 ? 0.11964 0.19611 0.12851 -0.02694 0.02047  -0.01265 233 GLN A N   
1826 C CA  . GLN A 237 ? 0.11630 0.21268 0.13553 -0.02332 0.01943  -0.01578 233 GLN A CA  
1827 C C   . GLN A 237 ? 0.13548 0.22891 0.15384 -0.01236 0.01440  -0.01585 233 GLN A C   
1828 O O   . GLN A 237 ? 0.10896 0.18792 0.12326 -0.01010 0.01040  -0.01324 233 GLN A O   
1829 C CB  . GLN A 237 ? 0.16349 0.26694 0.18996 -0.02770 0.01675  -0.01793 233 GLN A CB  
1830 C CG  . GLN A 237 ? 0.21983 0.33842 0.25434 -0.03715 0.01994  -0.02020 233 GLN A CG  
1831 C CD  . GLN A 237 ? 0.16782 0.29389 0.20930 -0.03963 0.01527  -0.02400 233 GLN A CD  
1832 O OE1 . GLN A 237 ? 0.29460 0.40733 0.33069 -0.03947 0.01144  -0.02419 233 GLN A OE1 
1833 N NE2 . GLN A 237 ? 0.26287 0.41204 0.31607 -0.04066 0.01517  -0.02769 233 GLN A NE2 
1834 N N   . ARG A 238 ? 0.13160 0.23916 0.15410 -0.00565 0.01410  -0.01875 234 ARG A N   
1835 C CA  . ARG A 238 ? 0.11676 0.22037 0.13858 0.00471  0.00754  -0.01918 234 ARG A CA  
1836 C C   . ARG A 238 ? 0.15655 0.26623 0.18450 0.00522  0.00350  -0.01880 234 ARG A C   
1837 O O   . ARG A 238 ? 0.17974 0.29844 0.21264 -0.00127 0.00548  -0.01975 234 ARG A O   
1838 C CB  . ARG A 238 ? 0.13901 0.25414 0.16061 0.01408  0.00778  -0.02352 234 ARG A CB  
1839 C CG  . ARG A 238 ? 0.20053 0.31222 0.21403 0.01531  0.01228  -0.02407 234 ARG A CG  
1840 C CD  . ARG A 238 ? 0.16600 0.28547 0.17607 0.02892  0.01024  -0.02919 234 ARG A CD  
1841 N NE  . ARG A 238 ? 0.22813 0.34384 0.22780 0.03194  0.01417  -0.02985 234 ARG A NE  
1842 C CZ  . ARG A 238 ? 0.29979 0.39244 0.28854 0.03574  0.00925  -0.02920 234 ARG A CZ  
1843 N NH1 . ARG A 238 ? 0.22183 0.29430 0.21040 0.03591  0.00048  -0.02729 234 ARG A NH1 
1844 N NH2 . ARG A 238 ? 0.32246 0.41354 0.30036 0.03918  0.01314  -0.03011 234 ARG A NH2 
1845 N N   . ARG A 239 ? 0.13132 0.23456 0.15771 0.01321  -0.00302 -0.01727 235 ARG A N   
1846 C CA  . ARG A 239 ? 0.16412 0.27298 0.19394 0.01497  -0.00684 -0.01583 235 ARG A CA  
1847 C C   . ARG A 239 ? 0.19980 0.33121 0.23686 0.01742  -0.00604 -0.02154 235 ARG A C   
1848 O O   . ARG A 239 ? 0.14959 0.28965 0.19014 0.01586  -0.00740 -0.02195 235 ARG A O   
1849 C CB  . ARG A 239 ? 0.16783 0.26318 0.19335 0.02238  -0.01437 -0.01157 235 ARG A CB  
1850 C CG  . ARG A 239 ? 0.23895 0.31509 0.26048 0.01846  -0.01637 -0.00494 235 ARG A CG  
1851 C CD  . ARG A 239 ? 0.22501 0.28831 0.24387 0.02315  -0.02447 0.00087  235 ARG A CD  
1852 N NE  . ARG A 239 ? 0.31099 0.35773 0.32850 0.01854  -0.02727 0.00705  235 ARG A NE  
1853 C CZ  . ARG A 239 ? 0.41846 0.46520 0.43833 0.01208  -0.02593 0.01434  235 ARG A CZ  
1854 N NH1 . ARG A 239 ? 0.44334 0.50358 0.46474 0.01046  -0.02197 0.01607  235 ARG A NH1 
1855 N NH2 . ARG A 239 ? 0.39311 0.42767 0.41397 0.00779  -0.02900 0.01954  235 ARG A NH2 
1856 N N   . ASN A 240 ? 0.16207 0.30533 0.20159 0.02198  -0.00410 -0.02638 236 ASN A N   
1857 C CA  . ASN A 240 ? 0.17949 0.34902 0.22846 0.02425  -0.00317 -0.03217 236 ASN A CA  
1858 C C   . ASN A 240 ? 0.10650 0.29145 0.16374 0.01181  0.00385  -0.03404 236 ASN A C   
1859 O O   . ASN A 240 ? 0.14870 0.35899 0.21640 0.01143  0.00554  -0.03876 236 ASN A O   
1860 C CB  . ASN A 240 ? 0.16293 0.34253 0.21151 0.03673  -0.00454 -0.03693 236 ASN A CB  
1861 C CG  . ASN A 240 ? 0.29159 0.47284 0.33727 0.03538  0.00207  -0.03791 236 ASN A CG  
1862 O OD1 . ASN A 240 ? 0.26537 0.44285 0.31071 0.02381  0.00834  -0.03490 236 ASN A OD1 
1863 N ND2 . ASN A 240 ? 0.11907 0.30531 0.16085 0.04865  0.00015  -0.04233 236 ASN A ND2 
1864 N N   . GLY A 241 ? 0.17047 0.34064 0.22348 0.00160  0.00732  -0.03033 237 GLY A N   
1865 C CA  . GLY A 241 ? 0.20979 0.38804 0.26863 -0.01137 0.01225  -0.03107 237 GLY A CA  
1866 C C   . GLY A 241 ? 0.28451 0.46925 0.34369 -0.01661 0.01986  -0.03011 237 GLY A C   
1867 O O   . GLY A 241 ? 0.21350 0.39993 0.27573 -0.02935 0.02391  -0.02874 237 GLY A O   
1868 N N   . SER A 242 ? 0.13867 0.32624 0.19358 -0.00700 0.02150  -0.03059 238 SER A N   
1869 C CA  . SER A 242 ? 0.20636 0.40210 0.25947 -0.01053 0.02955  -0.02914 238 SER A CA  
1870 C C   . SER A 242 ? 0.17649 0.34592 0.21711 -0.01691 0.03185  -0.02377 238 SER A C   
1871 O O   . SER A 242 ? 0.26249 0.40852 0.29545 -0.01459 0.02675  -0.02211 238 SER A O   
1872 C CB  . SER A 242 ? 0.12906 0.33539 0.17879 0.00450  0.02974  -0.03262 238 SER A CB  
1873 O OG  . SER A 242 ? 0.20901 0.39028 0.24712 0.01495  0.02280  -0.03251 238 SER A OG  
1874 N N   . LYS A 243 ? 0.24008 0.41502 0.27881 -0.02501 0.03967  -0.02055 239 LYS A N   
1875 C CA  . LYS A 243 ? 0.21622 0.36711 0.24225 -0.03147 0.04198  -0.01520 239 LYS A CA  
1876 C C   . LYS A 243 ? 0.24291 0.38699 0.25572 -0.02156 0.04428  -0.01432 239 LYS A C   
1877 O O   . LYS A 243 ? 0.21220 0.37594 0.22607 -0.01359 0.04782  -0.01676 239 LYS A O   
1878 C CB  . LYS A 243 ? 0.25646 0.41290 0.28602 -0.04791 0.04833  -0.01071 239 LYS A CB  
1879 C CG  . LYS A 243 ? 0.41380 0.55102 0.44324 -0.05848 0.04368  -0.00967 239 LYS A CG  
1880 C CD  . LYS A 243 ? 0.29837 0.44372 0.33904 -0.05631 0.03682  -0.01532 239 LYS A CD  
1881 C CE  . LYS A 243 ? 0.52789 0.70402 0.58561 -0.06263 0.03884  -0.01807 239 LYS A CE  
1882 N NZ  . LYS A 243 ? 0.33566 0.52002 0.40284 -0.05926 0.03136  -0.02406 239 LYS A NZ  
1883 N N   . PHE A 244 ? 0.18261 0.29953 0.18250 -0.02085 0.04154  -0.01162 240 PHE A N   
1884 C CA  . PHE A 244 ? 0.25934 0.36676 0.24460 -0.01297 0.04312  -0.01066 240 PHE A CA  
1885 C C   . PHE A 244 ? 0.19862 0.28149 0.17170 -0.01976 0.04351  -0.00548 240 PHE A C   
1886 O O   . PHE A 244 ? 0.20197 0.27159 0.17725 -0.02680 0.04009  -0.00413 240 PHE A O   
1887 C CB  . PHE A 244 ? 0.17163 0.27019 0.15300 0.00183  0.03484  -0.01556 240 PHE A CB  
1888 C CG  . PHE A 244 ? 0.16099 0.23682 0.14152 0.00146  0.02654  -0.01483 240 PHE A CG  
1889 C CD1 . PHE A 244 ? 0.21449 0.29264 0.20596 -0.00181 0.02262  -0.01518 240 PHE A CD1 
1890 C CD2 . PHE A 244 ? 0.18406 0.23865 0.15298 0.00491  0.02266  -0.01374 240 PHE A CD2 
1891 C CE1 . PHE A 244 ? 0.29065 0.35221 0.28178 -0.00203 0.01623  -0.01356 240 PHE A CE1 
1892 C CE2 . PHE A 244 ? 0.25271 0.29122 0.22319 0.00415  0.01553  -0.01269 240 PHE A CE2 
1893 C CZ  . PHE A 244 ? 0.26592 0.30889 0.24767 0.00051  0.01293  -0.01216 240 PHE A CZ  
1894 N N   . SER A 245 ? 0.25002 0.32714 0.20873 -0.01596 0.04727  -0.00305 241 SER A N   
1895 C CA  . SER A 245 ? 0.29612 0.35052 0.24071 -0.02115 0.04798  0.00227  241 SER A CA  
1896 C C   . SER A 245 ? 0.26224 0.29536 0.19578 -0.01031 0.04000  -0.00031 241 SER A C   
1897 O O   . SER A 245 ? 0.24325 0.27933 0.17324 0.00155  0.03687  -0.00472 241 SER A O   
1898 C CB  . SER A 245 ? 0.42905 0.49105 0.36323 -0.02546 0.05797  0.00838  241 SER A CB  
1899 O OG  . SER A 245 ? 0.45153 0.53086 0.39712 -0.03952 0.06485  0.01248  241 SER A OG  
1900 N N   . VAL A 246 ? 0.22408 0.23595 0.15240 -0.01406 0.03580  0.00186  242 VAL A N   
1901 C CA  . VAL A 246 ? 0.30555 0.29836 0.22456 -0.00565 0.02808  0.00006  242 VAL A CA  
1902 C C   . VAL A 246 ? 0.25087 0.22768 0.15099 -0.00651 0.03076  0.00476  242 VAL A C   
1903 O O   . VAL A 246 ? 0.22593 0.19476 0.12240 -0.01606 0.03413  0.00972  242 VAL A O   
1904 C CB  . VAL A 246 ? 0.26382 0.24816 0.19200 -0.00725 0.02079  -0.00138 242 VAL A CB  
1905 C CG1 . VAL A 246 ? 0.28419 0.25192 0.20452 0.00008  0.01303  -0.00268 242 VAL A CG1 
1906 C CG2 . VAL A 246 ? 0.40968 0.40851 0.35413 -0.00592 0.01805  -0.00468 242 VAL A CG2 
1907 N N   . TYR A 247 ? 0.24332 0.21341 0.13001 0.00394  0.02821  0.00306  243 TYR A N   
1908 C CA  . TYR A 247 ? 0.28719 0.24370 0.15291 0.00518  0.03126  0.00787  243 TYR A CA  
1909 C C   . TYR A 247 ? 0.37596 0.31038 0.23112 0.01223  0.02188  0.00605  243 TYR A C   
1910 O O   . TYR A 247 ? 0.32310 0.24267 0.15958 0.01324  0.02321  0.01047  243 TYR A O   
1911 C CB  . TYR A 247 ? 0.33801 0.30653 0.19226 0.01312  0.03693  0.00766  243 TYR A CB  
1912 C CG  . TYR A 247 ? 0.33787 0.33229 0.20153 0.00668  0.04749  0.01020  243 TYR A CG  
1913 C CD1 . TYR A 247 ? 0.36571 0.37919 0.24663 0.00955  0.04611  0.00416  243 TYR A CD1 
1914 C CD2 . TYR A 247 ? 0.40849 0.40894 0.26413 -0.00258 0.05845  0.01913  243 TYR A CD2 
1915 C CE1 . TYR A 247 ? 0.47050 0.51066 0.36138 0.00465  0.05513  0.00569  243 TYR A CE1 
1916 C CE2 . TYR A 247 ? 0.50814 0.53651 0.37516 -0.00941 0.06811  0.02164  243 TYR A CE2 
1917 C CZ  . TYR A 247 ? 0.39610 0.44537 0.28118 -0.00516 0.06629  0.01428  243 TYR A CZ  
1918 O OH  . TYR A 247 ? 0.58622 0.66611 0.48371 -0.01105 0.07540  0.01611  243 TYR A OH  
1919 N N   . ASP A 248 ? 0.28536 0.21805 0.15178 0.01702  0.01235  0.00027  244 ASP A N   
1920 C CA  . ASP A 248 ? 0.25079 0.16688 0.11083 0.02295  0.00306  -0.00169 244 ASP A CA  
1921 C C   . ASP A 248 ? 0.21353 0.13414 0.09318 0.02212  -0.00461 -0.00537 244 ASP A C   
1922 O O   . ASP A 248 ? 0.28274 0.21669 0.17797 0.01800  -0.00299 -0.00620 244 ASP A O   
1923 C CB  . ASP A 248 ? 0.33057 0.23981 0.17497 0.03484  -0.00180 -0.00511 244 ASP A CB  
1924 C CG  . ASP A 248 ? 0.29895 0.21932 0.15027 0.04128  -0.00498 -0.01114 244 ASP A CG  
1925 O OD1 . ASP A 248 ? 0.31056 0.23129 0.17610 0.04264  -0.01413 -0.01561 244 ASP A OD1 
1926 O OD2 . ASP A 248 ? 0.36414 0.29282 0.20598 0.04532  0.00140  -0.01115 244 ASP A OD2 
1927 N N   . VAL A 249 ? 0.24723 0.15791 0.12572 0.02632  -0.01294 -0.00706 245 VAL A N   
1928 C CA  . VAL A 249 ? 0.25111 0.16808 0.14779 0.02420  -0.01875 -0.00852 245 VAL A CA  
1929 C C   . VAL A 249 ? 0.30363 0.22940 0.21473 0.02580  -0.02503 -0.01174 245 VAL A C   
1930 O O   . VAL A 249 ? 0.20268 0.13801 0.13079 0.02147  -0.02698 -0.01087 245 VAL A O   
1931 C CB  . VAL A 249 ? 0.25653 0.16360 0.14812 0.02893  -0.02563 -0.00938 245 VAL A CB  
1932 C CG1 . VAL A 249 ? 0.28602 0.18600 0.16994 0.03765  -0.03430 -0.01327 245 VAL A CG1 
1933 C CG2 . VAL A 249 ? 0.28463 0.20242 0.19460 0.02639  -0.02921 -0.00968 245 VAL A CG2 
1934 N N   . SER A 250 ? 0.25544 0.17728 0.15897 0.03221  -0.02863 -0.01524 246 SER A N   
1935 C CA  . SER A 250 ? 0.24546 0.16845 0.16000 0.03473  -0.03859 -0.01900 246 SER A CA  
1936 C C   . SER A 250 ? 0.25020 0.18466 0.18153 0.02880  -0.03673 -0.01724 246 SER A C   
1937 O O   . SER A 250 ? 0.27356 0.21115 0.22005 0.02528  -0.04330 -0.01618 246 SER A O   
1938 C CB  . SER A 250 ? 0.26798 0.18286 0.16812 0.04445  -0.04309 -0.02441 246 SER A CB  
1939 O OG  . SER A 250 ? 0.32961 0.23337 0.21338 0.05089  -0.04625 -0.02598 246 SER A OG  
1940 N N   . ILE A 251 ? 0.21476 0.15673 0.14376 0.02740  -0.02785 -0.01633 247 ILE A N   
1941 C CA  . ILE A 251 ? 0.27319 0.22589 0.21593 0.02352  -0.02646 -0.01520 247 ILE A CA  
1942 C C   . ILE A 251 ? 0.27815 0.23831 0.23489 0.01561  -0.02513 -0.01068 247 ILE A C   
1943 O O   . ILE A 251 ? 0.24796 0.21545 0.21662 0.01272  -0.02642 -0.00892 247 ILE A O   
1944 C CB  . ILE A 251 ? 0.40505 0.36772 0.34283 0.02387  -0.01677 -0.01553 247 ILE A CB  
1945 C CG1 . ILE A 251 ? 0.37136 0.34246 0.31874 0.02548  -0.01866 -0.01717 247 ILE A CG1 
1946 C CG2 . ILE A 251 ? 0.36255 0.33188 0.30195 0.01557  -0.00756 -0.01133 247 ILE A CG2 
1947 C CD1 . ILE A 251 ? 0.39632 0.38144 0.34064 0.02716  -0.00987 -0.01848 247 ILE A CD1 
1948 N N   . LEU A 252 ? 0.20813 0.16627 0.16215 0.01333  -0.02298 -0.00886 248 LEU A N   
1949 C CA  . LEU A 252 ? 0.18472 0.15142 0.14901 0.00800  -0.02072 -0.00562 248 LEU A CA  
1950 C C   . LEU A 252 ? 0.17388 0.14354 0.14894 0.00776  -0.02791 -0.00408 248 LEU A C   
1951 O O   . LEU A 252 ? 0.25255 0.23324 0.23763 0.00442  -0.02625 -0.00106 248 LEU A O   
1952 C CB  . LEU A 252 ? 0.15419 0.11650 0.10847 0.00664  -0.01487 -0.00516 248 LEU A CB  
1953 C CG  . LEU A 252 ? 0.25119 0.21384 0.19794 0.00343  -0.00680 -0.00491 248 LEU A CG  
1954 C CD1 . LEU A 252 ? 0.23705 0.18825 0.17072 0.00174  -0.00349 -0.00370 248 LEU A CD1 
1955 C CD2 . LEU A 252 ? 0.28673 0.26321 0.24530 -0.00146 -0.00327 -0.00421 248 LEU A CD2 
1956 N N   . ILE A 253 ? 0.32162 0.18853 0.14256 -0.02891 0.01693  -0.06632 249 ILE A N   
1957 C CA  . ILE A 253 ? 0.30827 0.17163 0.12861 -0.03681 -0.00077 -0.06469 249 ILE A CA  
1958 C C   . ILE A 253 ? 0.41569 0.28440 0.26432 -0.03877 -0.00340 -0.06313 249 ILE A C   
1959 O O   . ILE A 253 ? 0.35772 0.24555 0.22918 -0.04100 -0.01201 -0.05245 249 ILE A O   
1960 C CB  . ILE A 253 ? 0.34264 0.19161 0.14303 -0.04116 -0.01287 -0.07019 249 ILE A CB  
1961 C CG1 . ILE A 253 ? 0.41128 0.25989 0.18813 -0.03904 -0.01211 -0.06710 249 ILE A CG1 
1962 C CG2 . ILE A 253 ? 0.34444 0.19430 0.15320 -0.05085 -0.03334 -0.06752 249 ILE A CG2 
1963 C CD1 . ILE A 253 ? 0.55600 0.39223 0.31023 -0.04359 -0.02527 -0.07178 249 ILE A CD1 
1964 N N   . PRO A 254 ? 0.30265 0.16029 0.15748 -0.03595 0.00427  -0.07023 250 PRO A N   
1965 C CA  . PRO A 254 ? 0.29349 0.16097 0.18116 -0.03594 0.00188  -0.06367 250 PRO A CA  
1966 C C   . PRO A 254 ? 0.27532 0.16765 0.18721 -0.02934 0.01149  -0.05425 250 PRO A C   
1967 O O   . PRO A 254 ? 0.25310 0.15563 0.18993 -0.02897 0.00949  -0.04673 250 PRO A O   
1968 C CB  . PRO A 254 ? 0.32025 0.16291 0.20268 -0.03338 0.00708  -0.07495 250 PRO A CB  
1969 C CG  . PRO A 254 ? 0.40801 0.23689 0.26106 -0.03142 0.00968  -0.08517 250 PRO A CG  
1970 C CD  . PRO A 254 ? 0.37497 0.21954 0.21762 -0.02976 0.01402  -0.07977 250 PRO A CD  
1971 N N   . ILE A 255 ? 0.25856 0.15970 0.16241 -0.02510 0.02116  -0.05419 251 ILE A N   
1972 C CA  . ILE A 255 ? 0.20484 0.12607 0.12807 -0.01944 0.03075  -0.04863 251 ILE A CA  
1973 C C   . ILE A 255 ? 0.21229 0.15243 0.14271 -0.02057 0.02687  -0.03915 251 ILE A C   
1974 O O   . ILE A 255 ? 0.16765 0.12529 0.11856 -0.01839 0.02734  -0.03203 251 ILE A O   
1975 C CB  . ILE A 255 ? 0.22015 0.13798 0.13308 -0.01474 0.04582  -0.05601 251 ILE A CB  
1976 C CG1 . ILE A 255 ? 0.31079 0.21083 0.21902 -0.01087 0.05193  -0.06599 251 ILE A CG1 
1977 C CG2 . ILE A 255 ? 0.24725 0.18771 0.18109 -0.01094 0.05332  -0.05058 251 ILE A CG2 
1978 C CD1 . ILE A 255 ? 0.34540 0.24875 0.27950 -0.00681 0.04980  -0.06274 251 ILE A CD1 
1979 N N   . ILE A 256 ? 0.19217 0.12784 0.10416 -0.02300 0.02335  -0.03896 252 ILE A N   
1980 C CA  . ILE A 256 ? 0.24462 0.19467 0.16195 -0.02219 0.02049  -0.03079 252 ILE A CA  
1981 C C   . ILE A 256 ? 0.23956 0.19334 0.16107 -0.02568 0.00620  -0.02501 252 ILE A C   
1982 O O   . ILE A 256 ? 0.26845 0.20887 0.17580 -0.03024 -0.00254 -0.02866 252 ILE A O   
1983 C CB  . ILE A 256 ? 0.20974 0.15261 0.10648 -0.02124 0.02723  -0.03247 252 ILE A CB  
1984 C CG1 . ILE A 256 ? 0.22350 0.17753 0.12626 -0.01890 0.02492  -0.02468 252 ILE A CG1 
1985 C CG2 . ILE A 256 ? 0.30297 0.22593 0.17063 -0.02429 0.02318  -0.03703 252 ILE A CG2 
1986 C CD1 . ILE A 256 ? 0.28561 0.23181 0.17287 -0.01819 0.03349  -0.02516 252 ILE A CD1 
1987 N N   . ALA A 257 ? 0.22206 0.19527 0.16369 -0.02372 0.00376  -0.01624 253 ALA A N   
1988 C CA  . ALA A 257 ? 0.16230 0.14605 0.11653 -0.02670 -0.00826 -0.00905 253 ALA A CA  
1989 C C   . ALA A 257 ? 0.19570 0.18991 0.15012 -0.02232 -0.01127 -0.00268 253 ALA A C   
1990 O O   . ALA A 257 ? 0.23379 0.23623 0.19614 -0.02443 -0.02265 0.00274  253 ALA A O   
1991 C CB  . ALA A 257 ? 0.21471 0.21465 0.19561 -0.02760 -0.00779 -0.00232 253 ALA A CB  
1992 N N   . LEU A 258 ? 0.14900 0.14316 0.09692 -0.01630 -0.00187 -0.00306 254 LEU A N   
1993 C CA  . LEU A 258 ? 0.22852 0.22821 0.17576 -0.01026 -0.00316 0.00246  254 LEU A CA  
1994 C C   . LEU A 258 ? 0.18794 0.17040 0.11270 -0.00809 0.00468  -0.00173 254 LEU A C   
1995 O O   . LEU A 258 ? 0.21496 0.19089 0.13425 -0.01000 0.01428  -0.00775 254 LEU A O   
1996 C CB  . LEU A 258 ? 0.21178 0.23175 0.18041 -0.00445 0.00190  0.00789  254 LEU A CB  
1997 C CG  . LEU A 258 ? 0.19166 0.23246 0.18553 -0.00632 -0.00198 0.01449  254 LEU A CG  
1998 C CD1 . LEU A 258 ? 0.20864 0.26594 0.21514 0.00048  0.00719  0.01812  254 LEU A CD1 
1999 C CD2 . LEU A 258 ? 0.27731 0.32763 0.28163 -0.00781 -0.01450 0.02101  254 LEU A CD2 
2000 N N   . MET A 259 ? 0.19188 0.16770 0.10541 -0.00417 0.00046  0.00257  255 MET A N   
2001 C CA  . MET A 259 ? 0.18805 0.14585 0.08073 -0.00259 0.00806  0.00103  255 MET A CA  
2002 C C   . MET A 259 ? 0.19071 0.14965 0.08734 0.00598  0.00780  0.00736  255 MET A C   
2003 O O   . MET A 259 ? 0.19248 0.16161 0.09912 0.01126  -0.00184 0.01428  255 MET A O   
2004 C CB  . MET A 259 ? 0.21754 0.15584 0.08190 -0.00655 0.00390  0.00016  255 MET A CB  
2005 C CG  . MET A 259 ? 0.22010 0.15101 0.07440 -0.01353 0.00798  -0.00835 255 MET A CG  
2006 S SD  . MET A 259 ? 0.32433 0.23020 0.13818 -0.01706 0.00602  -0.00983 255 MET A SD  
2007 C CE  . MET A 259 ? 0.37465 0.28489 0.18661 -0.01488 -0.01550 -0.00149 255 MET A CE  
2008 N N   . VAL A 260 ? 0.19336 0.14157 0.08337 0.00739  0.01831  0.00477  256 VAL A N   
2009 C CA  . VAL A 260 ? 0.20406 0.14490 0.09255 0.01590  0.01913  0.00951  256 VAL A CA  
2010 C C   . VAL A 260 ? 0.24010 0.16273 0.10744 0.01764  0.01238  0.01632  256 VAL A C   
2011 O O   . VAL A 260 ? 0.26999 0.17823 0.11596 0.01054  0.01336  0.01494  256 VAL A O   
2012 C CB  . VAL A 260 ? 0.20435 0.13486 0.08976 0.01465  0.03122  0.00362  256 VAL A CB  
2013 C CG1 . VAL A 260 ? 0.21610 0.13073 0.08436 0.00468  0.03836  -0.00059 256 VAL A CG1 
2014 C CG2 . VAL A 260 ? 0.23442 0.15151 0.11625 0.02384  0.03258  0.00725  256 VAL A CG2 
2015 N N   . TYR A 261 ? 0.24085 0.16491 0.11371 0.02802  0.00557  0.02431  257 TYR A N   
2016 C CA  . TYR A 261 ? 0.26970 0.17776 0.12323 0.03160  -0.00330 0.03314  257 TYR A CA  
2017 C C   . TYR A 261 ? 0.29405 0.17137 0.12150 0.02891  0.00611  0.03361  257 TYR A C   
2018 O O   . TYR A 261 ? 0.32377 0.19038 0.15443 0.03273  0.01501  0.03218  257 TYR A O   
2019 C CB  . TYR A 261 ? 0.27355 0.19246 0.14451 0.04560  -0.01162 0.04214  257 TYR A CB  
2020 C CG  . TYR A 261 ? 0.30370 0.21100 0.15922 0.05160  -0.02445 0.05360  257 TYR A CG  
2021 C CD1 . TYR A 261 ? 0.33260 0.21105 0.16782 0.05733  -0.02062 0.05949  257 TYR A CD1 
2022 C CD2 . TYR A 261 ? 0.30617 0.23108 0.16798 0.05139  -0.04157 0.05931  257 TYR A CD2 
2023 C CE1 . TYR A 261 ? 0.36346 0.23063 0.18314 0.06388  -0.03327 0.07188  257 TYR A CE1 
2024 C CE2 . TYR A 261 ? 0.33639 0.25234 0.18332 0.05729  -0.05566 0.07058  257 TYR A CE2 
2025 C CZ  . TYR A 261 ? 0.37555 0.26263 0.20079 0.06428  -0.05131 0.07743  257 TYR A CZ  
2026 O OH  . TYR A 261 ? 0.41294 0.29012 0.22175 0.07109  -0.06604 0.09045  257 TYR A OH  
2027 N N   . ARG A 262 ? 0.31547 0.17734 0.11577 0.02185  0.00440  0.03564  258 ARG A N   
2028 C CA  . ARG A 262 ? 0.40372 0.23656 0.17795 0.01796  0.01386  0.03856  258 ARG A CA  
2029 C C   . ARG A 262 ? 0.42399 0.23726 0.17378 0.02380  0.00449  0.05173  258 ARG A C   
2030 O O   . ARG A 262 ? 0.45955 0.24740 0.19454 0.02524  0.01102  0.05795  258 ARG A O   
2031 C CB  . ARG A 262 ? 0.34414 0.17256 0.10293 0.00501  0.02392  0.03123  258 ARG A CB  
2032 C CG  . ARG A 262 ? 0.31275 0.15705 0.09380 -0.00076 0.03430  0.01965  258 ARG A CG  
2033 C CD  . ARG A 262 ? 0.36108 0.20076 0.15587 0.00120  0.04221  0.01785  258 ARG A CD  
2034 N NE  . ARG A 262 ? 0.41424 0.26186 0.22009 -0.00779 0.05357  0.00814  258 ARG A NE  
2035 C CZ  . ARG A 262 ? 0.39347 0.24738 0.21700 -0.00765 0.05787  0.00231  258 ARG A CZ  
2036 N NH1 . ARG A 262 ? 0.33455 0.18628 0.16574 0.00161  0.05398  0.00392  258 ARG A NH1 
2037 N NH2 . ARG A 262 ? 0.39558 0.25894 0.22910 -0.01638 0.06603  -0.00565 258 ARG A NH2 
2038 N N   . CYS A 263 ? 0.41698 0.24056 0.16192 0.02661  -0.01154 0.05661  259 CYS A N   
2039 C CA  . CYS A 263 ? 0.42111 0.23359 0.14887 0.03178  -0.02299 0.06841  259 CYS A CA  
2040 C C   . CYS A 263 ? 0.50038 0.33517 0.23782 0.03613  -0.04359 0.07217  259 CYS A C   
2041 O O   . CYS A 263 ? 0.44836 0.30458 0.20420 0.03347  -0.04775 0.06525  259 CYS A O   
2042 C CB  . CYS A 263 ? 0.55098 0.34933 0.25356 0.02127  -0.01599 0.06669  259 CYS A CB  
2043 S SG  . CYS A 263 ? 0.52246 0.33457 0.21826 0.00926  -0.01577 0.05379  259 CYS A SG  
2044 N N   . ALA A 264 ? 0.51305 0.34630 0.24337 0.04141  -0.05631 0.08277  260 ALA A N   
2045 C CA  . ALA A 264 ? 0.52861 0.38548 0.27064 0.04415  -0.07717 0.08699  260 ALA A CA  
2046 C C   . ALA A 264 ? 0.45630 0.31874 0.18328 0.03066  -0.08146 0.07686  260 ALA A C   
2047 O O   . ALA A 264 ? 0.50359 0.34932 0.20600 0.02193  -0.06964 0.07026  260 ALA A O   
2048 C CB  . ALA A 264 ? 0.61015 0.46436 0.34734 0.05284  -0.08892 0.10132  260 ALA A CB  
2049 N N   . PRO A 265 ? 0.50023 0.38661 0.24438 0.02882  -0.09767 0.07487  261 PRO A N   
2050 C CA  . PRO A 265 ? 0.56081 0.44915 0.29048 0.01648  -0.10298 0.06420  261 PRO A CA  
2051 C C   . PRO A 265 ? 0.66170 0.54033 0.36258 0.01483  -0.11097 0.06785  261 PRO A C   
2052 O O   . PRO A 265 ? 0.73759 0.60128 0.41177 0.00656  -0.10320 0.05911  261 PRO A O   
2053 C CB  . PRO A 265 ? 0.46155 0.37877 0.22325 0.01535  -0.11951 0.06324  261 PRO A CB  
2054 C CG  . PRO A 265 ? 0.64475 0.57889 0.43330 0.02920  -0.12800 0.07738  261 PRO A CG  
2055 C CD  . PRO A 265 ? 0.52161 0.43542 0.30308 0.03795  -0.11090 0.08187  261 PRO A CD  
2056 N N   . LYS B 8   ? 0.31796 0.38737 0.47382 -0.05440 -0.01169 -0.02387 4   LYS B N   
2057 C CA  . LYS B 8   ? 0.33041 0.41176 0.49117 -0.04766 -0.00724 -0.01678 4   LYS B CA  
2058 C C   . LYS B 8   ? 0.15672 0.24413 0.31506 -0.03704 -0.00756 -0.01748 4   LYS B C   
2059 O O   . LYS B 8   ? 0.24515 0.32075 0.39299 -0.03309 -0.00882 -0.02161 4   LYS B O   
2060 C CB  . LYS B 8   ? 0.25831 0.32649 0.41742 -0.04706 -0.00101 -0.01247 4   LYS B CB  
2061 C CG  . LYS B 8   ? 0.40517 0.47047 0.56711 -0.05660 0.00006  -0.00929 4   LYS B CG  
2062 C CD  . LYS B 8   ? 0.30601 0.35848 0.46557 -0.05527 0.00559  -0.00404 4   LYS B CD  
2063 C CE  . LYS B 8   ? 0.29723 0.34495 0.45844 -0.06512 0.00633  -0.00088 4   LYS B CE  
2064 N NZ  . LYS B 8   ? 0.29800 0.33288 0.45613 -0.07302 0.00228  -0.00689 4   LYS B NZ  
2065 N N   . GLN B 9   ? 0.15174 0.25454 0.31350 -0.03137 -0.00576 -0.01262 5   GLN B N   
2066 C CA  . GLN B 9   ? 0.08352 0.19133 0.24171 -0.02090 -0.00594 -0.01252 5   GLN B CA  
2067 C C   . GLN B 9   ? 0.11620 0.21764 0.26949 -0.01448 0.00057  -0.00882 5   GLN B C   
2068 O O   . GLN B 9   ? 0.17673 0.28618 0.33238 -0.01356 0.00468  -0.00436 5   GLN B O   
2069 C CB  . GLN B 9   ? 0.07973 0.20808 0.24376 -0.01818 -0.00866 -0.00998 5   GLN B CB  
2070 C CG  . GLN B 9   ? 0.16515 0.30070 0.33158 -0.02306 -0.01676 -0.01346 5   GLN B CG  
2071 C CD  . GLN B 9   ? 0.16644 0.29236 0.32322 -0.01840 -0.02069 -0.01836 5   GLN B CD  
2072 O OE1 . GLN B 9   ? 0.29229 0.41373 0.44183 -0.00872 -0.01840 -0.01688 5   GLN B OE1 
2073 N NE2 . GLN B 9   ? 0.25419 0.37337 0.40515 -0.02548 -0.02596 -0.02356 5   GLN B NE2 
2074 N N   . TYR B 10  ? 0.06124 0.14777 0.20430 -0.01033 0.00136  -0.01057 6   TYR B N   
2075 C CA  . TYR B 10  ? 0.04925 0.12889 0.18579 -0.00518 0.00620  -0.00746 6   TYR B CA  
2076 C C   . TYR B 10  ? 0.11382 0.19497 0.24310 0.00374  0.00601  -0.00774 6   TYR B C   
2077 O O   . TYR B 10  ? 0.07078 0.15314 0.19727 0.00638  0.00177  -0.01037 6   TYR B O   
2078 C CB  . TYR B 10  ? 0.06472 0.12717 0.19385 -0.00662 0.00702  -0.00811 6   TYR B CB  
2079 C CG  . TYR B 10  ? 0.05536 0.11273 0.19061 -0.01405 0.00837  -0.00673 6   TYR B CG  
2080 C CD1 . TYR B 10  ? 0.09657 0.15573 0.23563 -0.01618 0.01241  -0.00124 6   TYR B CD1 
2081 C CD2 . TYR B 10  ? 0.08888 0.13816 0.22470 -0.01903 0.00581  -0.01090 6   TYR B CD2 
2082 C CE1 . TYR B 10  ? 0.15284 0.20569 0.29705 -0.02297 0.01361  0.00103  6   TYR B CE1 
2083 C CE2 . TYR B 10  ? 0.14707 0.18851 0.28766 -0.02564 0.00729  -0.00963 6   TYR B CE2 
2084 C CZ  . TYR B 10  ? 0.19687 0.24007 0.34211 -0.02753 0.01106  -0.00317 6   TYR B CZ  
2085 O OH  . TYR B 10  ? 0.20884 0.24250 0.35736 -0.03381 0.01243  -0.00086 6   TYR B OH  
2086 N N   . PRO B 11  ? 0.09747 0.17750 0.22242 0.00825  0.01047  -0.00502 7   PRO B N   
2087 C CA  . PRO B 11  ? 0.06307 0.14074 0.17946 0.01659  0.01069  -0.00563 7   PRO B CA  
2088 C C   . PRO B 11  ? 0.07908 0.14353 0.18470 0.01787  0.00735  -0.00798 7   PRO B C   
2089 O O   . PRO B 11  ? 0.10283 0.15756 0.20462 0.01411  0.00737  -0.00820 7   PRO B O   
2090 C CB  . PRO B 11  ? 0.13419 0.20817 0.24473 0.01867  0.01631  -0.00316 7   PRO B CB  
2091 C CG  . PRO B 11  ? 0.17754 0.25925 0.29737 0.01257  0.01931  -0.00024 7   PRO B CG  
2092 C CD  . PRO B 11  ? 0.12959 0.20902 0.25556 0.00554  0.01547  -0.00127 7   PRO B CD  
2093 N N   . ILE B 12  ? 0.07835 0.14311 0.17955 0.02357  0.00477  -0.00906 8   ILE B N   
2094 C CA  . ILE B 12  ? 0.07009 0.12372 0.16084 0.02459  0.00174  -0.01069 8   ILE B CA  
2095 C C   . ILE B 12  ? 0.10710 0.15250 0.18714 0.03125  0.00297  -0.00970 8   ILE B C   
2096 O O   . ILE B 12  ? 0.14444 0.19505 0.22612 0.03741  0.00411  -0.00877 8   ILE B O   
2097 C CB  . ILE B 12  ? 0.15256 0.21193 0.24581 0.02361  -0.00365 -0.01275 8   ILE B CB  
2098 C CG1 . ILE B 12  ? 0.16637 0.21430 0.24756 0.02421  -0.00591 -0.01407 8   ILE B CG1 
2099 C CG2 . ILE B 12  ? 0.27107 0.34360 0.37060 0.02898  -0.00579 -0.01132 8   ILE B CG2 
2100 C CD1 . ILE B 12  ? 0.32999 0.38018 0.41108 0.02009  -0.01018 -0.01716 8   ILE B CD1 
2101 N N   . ILE B 13  ? 0.13693 0.16924 0.20630 0.02990  0.00306  -0.00975 9   ILE B N   
2102 C CA  . ILE B 13  ? 0.14086 0.16172 0.19791 0.03413  0.00369  -0.00906 9   ILE B CA  
2103 C C   . ILE B 13  ? 0.11591 0.12929 0.16524 0.03324  0.00031  -0.00929 9   ILE B C   
2104 O O   . ILE B 13  ? 0.12608 0.13828 0.17586 0.02816  -0.00025 -0.00984 9   ILE B O   
2105 C CB  . ILE B 13  ? 0.08490 0.09739 0.13522 0.03150  0.00695  -0.00819 9   ILE B CB  
2106 C CG1 . ILE B 13  ? 0.12508 0.14542 0.18188 0.03143  0.01082  -0.00758 9   ILE B CG1 
2107 C CG2 . ILE B 13  ? 0.16290 0.16160 0.19913 0.03476  0.00730  -0.00818 9   ILE B CG2 
2108 C CD1 . ILE B 13  ? 0.15924 0.18519 0.22446 0.02499  0.01126  -0.00633 9   ILE B CD1 
2109 N N   . ASN B 14  ? 0.14103 0.14904 0.18309 0.03858  -0.00140 -0.00848 10  ASN B N   
2110 C CA  . ASN B 14  ? 0.19672 0.19855 0.23076 0.03802  -0.00464 -0.00784 10  ASN B CA  
2111 C C   . ASN B 14  ? 0.18007 0.16603 0.20074 0.03729  -0.00362 -0.00630 10  ASN B C   
2112 O O   . ASN B 14  ? 0.16787 0.14555 0.18286 0.04067  -0.00172 -0.00590 10  ASN B O   
2113 C CB  . ASN B 14  ? 0.17104 0.17812 0.20599 0.04402  -0.00833 -0.00674 10  ASN B CB  
2114 C CG  . ASN B 14  ? 0.24169 0.26507 0.28876 0.04237  -0.01097 -0.00823 10  ASN B CG  
2115 O OD1 . ASN B 14  ? 0.38526 0.41957 0.44327 0.04393  -0.00981 -0.00843 10  ASN B OD1 
2116 N ND2 . ASN B 14  ? 0.37369 0.39870 0.41817 0.03853  -0.01437 -0.00941 10  ASN B ND2 
2117 N N   . PHE B 15  ? 0.09358 0.07520 0.10890 0.03247  -0.00457 -0.00562 11  PHE B N   
2118 C CA  . PHE B 15  ? 0.16679 0.13451 0.16966 0.03030  -0.00440 -0.00344 11  PHE B CA  
2119 C C   . PHE B 15  ? 0.16567 0.13215 0.16301 0.02848  -0.00643 -0.00192 11  PHE B C   
2120 O O   . PHE B 15  ? 0.12412 0.09979 0.12692 0.02628  -0.00667 -0.00343 11  PHE B O   
2121 C CB  . PHE B 15  ? 0.11644 0.08168 0.11902 0.02385  -0.00222 -0.00314 11  PHE B CB  
2122 C CG  . PHE B 15  ? 0.19123 0.14307 0.18150 0.01986  -0.00257 -0.00075 11  PHE B CG  
2123 C CD1 . PHE B 15  ? 0.17138 0.10893 0.15088 0.02222  -0.00257 -0.00061 11  PHE B CD1 
2124 C CD2 . PHE B 15  ? 0.19180 0.14503 0.18126 0.01356  -0.00251 0.00132  11  PHE B CD2 
2125 C CE1 . PHE B 15  ? 0.13727 0.06062 0.10452 0.01707  -0.00326 0.00142  11  PHE B CE1 
2126 C CE2 . PHE B 15  ? 0.18089 0.12310 0.15992 0.00841  -0.00308 0.00406  11  PHE B CE2 
2127 C CZ  . PHE B 15  ? 0.15497 0.08139 0.12239 0.00949  -0.00383 0.00405  11  PHE B CZ  
2128 N N   . THR B 16  ? 0.15276 0.10672 0.13810 0.02924  -0.00754 0.00100  12  THR B N   
2129 C CA  . THR B 16  ? 0.12640 0.07825 0.10443 0.02660  -0.00886 0.00340  12  THR B CA  
2130 C C   . THR B 16  ? 0.19167 0.13066 0.15929 0.02102  -0.00774 0.00659  12  THR B C   
2131 O O   . THR B 16  ? 0.18279 0.10914 0.14399 0.02151  -0.00761 0.00739  12  THR B O   
2132 C CB  . THR B 16  ? 0.16820 0.11882 0.14123 0.03283  -0.01255 0.00544  12  THR B CB  
2133 O OG1 . THR B 16  ? 0.21425 0.16363 0.17890 0.02941  -0.01354 0.00791  12  THR B OG1 
2134 C CG2 . THR B 16  ? 0.20891 0.14490 0.17401 0.03852  -0.01331 0.00816  12  THR B CG2 
2135 N N   . THR B 17  ? 0.20861 0.15098 0.17442 0.01527  -0.00659 0.00820  13  THR B N   
2136 C CA  . THR B 17  ? 0.14595 0.07824 0.10236 0.00878  -0.00581 0.01225  13  THR B CA  
2137 C C   . THR B 17  ? 0.16560 0.08474 0.10825 0.01046  -0.00798 0.01646  13  THR B C   
2138 O O   . THR B 17  ? 0.21713 0.12460 0.15030 0.00473  -0.00771 0.02035  13  THR B O   
2139 C CB  . THR B 17  ? 0.26407 0.20731 0.22531 0.00245  -0.00282 0.01308  13  THR B CB  
2140 O OG1 . THR B 17  ? 0.24329 0.19299 0.20270 0.00449  -0.00246 0.01268  13  THR B OG1 
2141 C CG2 . THR B 17  ? 0.19076 0.14594 0.16597 0.00174  -0.00083 0.00988  13  THR B CG2 
2142 N N   . ALA B 18  ? 0.20785 0.12872 0.14929 0.01770  -0.01055 0.01638  14  ALA B N   
2143 C CA  . ALA B 18  ? 0.24412 0.15287 0.17267 0.02053  -0.01323 0.02146  14  ALA B CA  
2144 C C   . ALA B 18  ? 0.25971 0.15136 0.18279 0.02560  -0.01427 0.02245  14  ALA B C   
2145 O O   . ALA B 18  ? 0.26180 0.15639 0.19104 0.03391  -0.01529 0.02007  14  ALA B O   
2146 C CB  . ALA B 18  ? 0.23594 0.15500 0.16570 0.02629  -0.01641 0.02151  14  ALA B CB  
2147 N N   . GLY B 19  ? 0.26849 0.14208 0.17993 0.02041  -0.01361 0.02580  15  GLY B N   
2148 C CA  . GLY B 19  ? 0.36435 0.21797 0.26821 0.02464  -0.01381 0.02575  15  GLY B CA  
2149 C C   . GLY B 19  ? 0.33071 0.18372 0.23938 0.02257  -0.01148 0.02036  15  GLY B C   
2150 O O   . GLY B 19  ? 0.36073 0.20056 0.26504 0.02866  -0.01083 0.01834  15  GLY B O   
2151 N N   . ALA B 20  ? 0.28711 0.15393 0.20413 0.01460  -0.00999 0.01820  16  ALA B N   
2152 C CA  . ALA B 20  ? 0.23120 0.09943 0.15260 0.01203  -0.00839 0.01385  16  ALA B CA  
2153 C C   . ALA B 20  ? 0.27837 0.12321 0.18511 0.00745  -0.00845 0.01394  16  ALA B C   
2154 O O   . ALA B 20  ? 0.31499 0.14717 0.21121 0.00023  -0.00950 0.01790  16  ALA B O   
2155 C CB  . ALA B 20  ? 0.23479 0.12090 0.16694 0.00390  -0.00735 0.01341  16  ALA B CB  
2156 N N   . THR B 21  ? 0.27200 0.11041 0.17705 0.01120  -0.00708 0.00941  17  THR B N   
2157 C CA  . THR B 21  ? 0.28131 0.09992 0.17267 0.00694  -0.00670 0.00755  17  THR B CA  
2158 C C   . THR B 21  ? 0.26314 0.08479 0.15567 0.00297  -0.00564 0.00306  17  THR B C   
2159 O O   . THR B 21  ? 0.22008 0.06100 0.12599 0.00515  -0.00474 0.00162  17  THR B O   
2160 C CB  . THR B 21  ? 0.34590 0.15390 0.23204 0.01727  -0.00517 0.00605  17  THR B CB  
2161 O OG1 . THR B 21  ? 0.26885 0.08722 0.16424 0.02748  -0.00275 0.00242  17  THR B OG1 
2162 C CG2 . THR B 21  ? 0.37976 0.18508 0.26471 0.02183  -0.00681 0.01122  17  THR B CG2 
2163 N N   . VAL B 22  ? 0.25534 0.06398 0.13609 -0.00317 -0.00572 0.00078  18  VAL B N   
2164 C CA  . VAL B 22  ? 0.25511 0.06438 0.13352 -0.00611 -0.00477 -0.00371 18  VAL B CA  
2165 C C   . VAL B 22  ? 0.31066 0.12529 0.19487 0.00654  -0.00094 -0.00759 18  VAL B C   
2166 O O   . VAL B 22  ? 0.27603 0.10202 0.16718 0.00663  0.00011  -0.00952 18  VAL B O   
2167 C CB  . VAL B 22  ? 0.34609 0.13829 0.20812 -0.01332 -0.00544 -0.00602 18  VAL B CB  
2168 C CG1 . VAL B 22  ? 0.32768 0.11905 0.18457 -0.01462 -0.00403 -0.01109 18  VAL B CG1 
2169 C CG2 . VAL B 22  ? 0.30772 0.10017 0.16696 -0.02738 -0.00949 -0.00199 18  VAL B CG2 
2170 N N   . GLN B 23  ? 0.25786 0.06725 0.14110 0.01714  0.00125  -0.00807 19  GLN B N   
2171 C CA  . GLN B 23  ? 0.26754 0.08514 0.15809 0.02868  0.00524  -0.01114 19  GLN B CA  
2172 C C   . GLN B 23  ? 0.26813 0.10699 0.17606 0.03346  0.00506  -0.00967 19  GLN B C   
2173 O O   . GLN B 23  ? 0.23158 0.08138 0.14667 0.03690  0.00780  -0.01232 19  GLN B O   
2174 C CB  . GLN B 23  ? 0.35721 0.16672 0.24517 0.03853  0.00716  -0.01084 19  GLN B CB  
2175 C CG  . GLN B 23  ? 0.33315 0.15233 0.22930 0.04968  0.01172  -0.01366 19  GLN B CG  
2176 C CD  . GLN B 23  ? 0.56872 0.38087 0.45544 0.04767  0.01557  -0.01900 19  GLN B CD  
2177 O OE1 . GLN B 23  ? 0.59793 0.39076 0.46849 0.04313  0.01595  -0.02122 19  GLN B OE1 
2178 N NE2 . GLN B 23  ? 0.54862 0.37621 0.44455 0.05056  0.01846  -0.02102 19  GLN B NE2 
2179 N N   . SER B 24  ? 0.21910 0.06386 0.13320 0.03351  0.00203  -0.00546 20  SER B N   
2180 C CA  . SER B 24  ? 0.19637 0.06393 0.12773 0.03738  0.00153  -0.00439 20  SER B CA  
2181 C C   . SER B 24  ? 0.19236 0.07614 0.13294 0.02853  0.00121  -0.00490 20  SER B C   
2182 O O   . SER B 24  ? 0.18953 0.09126 0.14377 0.03131  0.00237  -0.00585 20  SER B O   
2183 C CB  . SER B 24  ? 0.22751 0.09907 0.16198 0.03879  -0.00171 -0.00002 20  SER B CB  
2184 O OG  . SER B 24  ? 0.24797 0.12131 0.18093 0.02815  -0.00382 0.00252  20  SER B OG  
2185 N N   . TYR B 25  ? 0.19090 0.06905 0.12490 0.01780  -0.00050 -0.00370 21  TYR B N   
2186 C CA  . TYR B 25  ? 0.19371 0.08731 0.13699 0.01048  -0.00093 -0.00327 21  TYR B CA  
2187 C C   . TYR B 25  ? 0.21028 0.10401 0.15151 0.01085  0.00130  -0.00651 21  TYR B C   
2188 O O   . TYR B 25  ? 0.15197 0.06193 0.10491 0.01030  0.00209  -0.00630 21  TYR B O   
2189 C CB  . TYR B 25  ? 0.18685 0.07743 0.12549 -0.00092 -0.00365 -0.00012 21  TYR B CB  
2190 C CG  . TYR B 25  ? 0.18899 0.09705 0.13901 -0.00738 -0.00438 0.00160  21  TYR B CG  
2191 C CD1 . TYR B 25  ? 0.18187 0.10809 0.14757 -0.00554 -0.00376 0.00325  21  TYR B CD1 
2192 C CD2 . TYR B 25  ? 0.20449 0.11004 0.14880 -0.01514 -0.00585 0.00166  21  TYR B CD2 
2193 C CE1 . TYR B 25  ? 0.16920 0.10996 0.14571 -0.01006 -0.00406 0.00533  21  TYR B CE1 
2194 C CE2 . TYR B 25  ? 0.22395 0.14603 0.17931 -0.02016 -0.00700 0.00444  21  TYR B CE2 
2195 C CZ  . TYR B 25  ? 0.18602 0.12534 0.15801 -0.01700 -0.00584 0.00648  21  TYR B CZ  
2196 O OH  . TYR B 25  ? 0.15707 0.11133 0.14022 -0.02083 -0.00669 0.00975  21  TYR B OH  
2197 N N   . THR B 26  ? 0.18938 0.06389 0.11464 0.01182  0.00268  -0.00954 22  THR B N   
2198 C CA  . THR B 26  ? 0.19353 0.06686 0.11397 0.01281  0.00569  -0.01318 22  THR B CA  
2199 C C   . THR B 26  ? 0.19446 0.08175 0.12739 0.02318  0.00968  -0.01443 22  THR B C   
2200 O O   . THR B 26  ? 0.23178 0.13221 0.17181 0.02198  0.01135  -0.01463 22  THR B O   
2201 C CB  . THR B 26  ? 0.27865 0.12580 0.17744 0.01310  0.00729  -0.01729 22  THR B CB  
2202 O OG1 . THR B 26  ? 0.30950 0.14390 0.19645 0.00125  0.00299  -0.01600 22  THR B OG1 
2203 C CG2 . THR B 26  ? 0.27984 0.12600 0.17185 0.01441  0.01125  -0.02159 22  THR B CG2 
2204 N N   . ASN B 27  ? 0.24798 0.13310 0.18387 0.03313  0.01103  -0.01459 23  ASN B N   
2205 C CA  . ASN B 27  ? 0.20438 0.10532 0.15406 0.04244  0.01425  -0.01508 23  ASN B CA  
2206 C C   . ASN B 27  ? 0.17514 0.09871 0.14256 0.03849  0.01244  -0.01263 23  ASN B C   
2207 O O   . ASN B 27  ? 0.17787 0.11542 0.15543 0.04082  0.01522  -0.01310 23  ASN B O   
2208 C CB  . ASN B 27  ? 0.25211 0.14966 0.20388 0.05290  0.01419  -0.01409 23  ASN B CB  
2209 C CG  . ASN B 27  ? 0.35959 0.24007 0.29835 0.05640  0.01633  -0.01583 23  ASN B CG  
2210 O OD1 . ASN B 27  ? 0.35947 0.23037 0.28752 0.05499  0.01978  -0.01937 23  ASN B OD1 
2211 N ND2 . ASN B 27  ? 0.39393 0.27036 0.33292 0.06081  0.01430  -0.01322 23  ASN B ND2 
2212 N N   . PHE B 28  ? 0.17192 0.09840 0.14269 0.03233  0.00831  -0.01000 24  PHE B N   
2213 C CA  . PHE B 28  ? 0.12258 0.06731 0.10882 0.02922  0.00694  -0.00823 24  PHE B CA  
2214 C C   . PHE B 28  ? 0.14950 0.10115 0.13910 0.02317  0.00798  -0.00773 24  PHE B C   
2215 O O   . PHE B 28  ? 0.11709 0.08211 0.11845 0.02423  0.00954  -0.00745 24  PHE B O   
2216 C CB  . PHE B 28  ? 0.11880 0.06305 0.10546 0.02484  0.00346  -0.00593 24  PHE B CB  
2217 C CG  . PHE B 28  ? 0.15078 0.10955 0.15012 0.02062  0.00270  -0.00466 24  PHE B CG  
2218 C CD1 . PHE B 28  ? 0.16190 0.13376 0.17387 0.02392  0.00326  -0.00557 24  PHE B CD1 
2219 C CD2 . PHE B 28  ? 0.22369 0.18286 0.22261 0.01335  0.00149  -0.00243 24  PHE B CD2 
2220 C CE1 . PHE B 28  ? 0.11695 0.09872 0.13907 0.02027  0.00297  -0.00497 24  PHE B CE1 
2221 C CE2 . PHE B 28  ? 0.20947 0.18070 0.22019 0.01100  0.00161  -0.00131 24  PHE B CE2 
2222 C CZ  . PHE B 28  ? 0.20113 0.18198 0.22253 0.01459  0.00251  -0.00293 24  PHE B CZ  
2223 N N   . ILE B 29  ? 0.13475 0.07760 0.11404 0.01619  0.00670  -0.00703 25  ILE B N   
2224 C CA  . ILE B 29  ? 0.13906 0.08936 0.12130 0.01020  0.00661  -0.00528 25  ILE B CA  
2225 C C   . ILE B 29  ? 0.20216 0.15340 0.18136 0.01335  0.01058  -0.00728 25  ILE B C   
2226 O O   . ILE B 29  ? 0.12935 0.09196 0.11670 0.01158  0.01165  -0.00532 25  ILE B O   
2227 C CB  . ILE B 29  ? 0.14566 0.08833 0.11783 0.00124  0.00325  -0.00343 25  ILE B CB  
2228 C CG1 . ILE B 29  ? 0.11922 0.06551 0.09751 -0.00222 0.00036  -0.00048 25  ILE B CG1 
2229 C CG2 . ILE B 29  ? 0.12324 0.07403 0.09740 -0.00445 0.00246  -0.00080 25  ILE B CG2 
2230 C CD1 . ILE B 29  ? 0.12716 0.09008 0.12302 -0.00136 0.00063  0.00200  25  ILE B CD1 
2231 N N   . ARG B 30  ? 0.16842 0.10723 0.13551 0.01838  0.01338  -0.01095 26  ARG B N   
2232 C CA  . ARG B 30  ? 0.14545 0.08604 0.10960 0.02269  0.01863  -0.01323 26  ARG B CA  
2233 C C   . ARG B 30  ? 0.14097 0.09929 0.12302 0.02844  0.02131  -0.01212 26  ARG B C   
2234 O O   . ARG B 30  ? 0.17472 0.14240 0.16081 0.02813  0.02475  -0.01142 26  ARG B O   
2235 C CB  . ARG B 30  ? 0.20849 0.13105 0.15651 0.02870  0.02199  -0.01782 26  ARG B CB  
2236 C CG  . ARG B 30  ? 0.26970 0.17281 0.19719 0.02129  0.01975  -0.01976 26  ARG B CG  
2237 C CD  . ARG B 30  ? 0.33394 0.21700 0.24318 0.02733  0.02457  -0.02539 26  ARG B CD  
2238 N NE  . ARG B 30  ? 0.34465 0.20702 0.23260 0.01857  0.02177  -0.02782 26  ARG B NE  
2239 C CZ  . ARG B 30  ? 0.48462 0.32285 0.35266 0.02156  0.02469  -0.03321 26  ARG B CZ  
2240 N NH1 . ARG B 30  ? 0.45862 0.29316 0.32777 0.03410  0.03062  -0.03575 26  ARG B NH1 
2241 N NH2 . ARG B 30  ? 0.47584 0.29549 0.32444 0.01119  0.02109  -0.03533 26  ARG B NH2 
2242 N N   . ALA B 31  ? 0.13566 0.09900 0.12793 0.03291  0.01955  -0.01166 27  ALA B N   
2243 C CA  . ALA B 31  ? 0.21282 0.19378 0.22245 0.03649  0.02085  -0.01055 27  ALA B CA  
2244 C C   . ALA B 31  ? 0.14457 0.13683 0.16514 0.02938  0.01917  -0.00764 27  ALA B C   
2245 O O   . ALA B 31  ? 0.16937 0.17372 0.19996 0.02929  0.02177  -0.00647 27  ALA B O   
2246 C CB  . ALA B 31  ? 0.13846 0.12185 0.15459 0.04174  0.01808  -0.01060 27  ALA B CB  
2247 N N   . VAL B 32  ? 0.16942 0.15778 0.18861 0.02356  0.01521  -0.00605 28  VAL B N   
2248 C CA  . VAL B 32  ? 0.10595 0.10286 0.13501 0.01799  0.01401  -0.00299 28  VAL B CA  
2249 C C   . VAL B 32  ? 0.11580 0.11481 0.14191 0.01477  0.01645  -0.00087 28  VAL B C   
2250 O O   . VAL B 32  ? 0.14166 0.15026 0.17775 0.01348  0.01810  0.00137  28  VAL B O   
2251 C CB  . VAL B 32  ? 0.07812 0.07083 0.10577 0.01349  0.01021  -0.00138 28  VAL B CB  
2252 C CG1 . VAL B 32  ? 0.18335 0.18319 0.22006 0.00890  0.00958  0.00237  28  VAL B CG1 
2253 C CG2 . VAL B 32  ? 0.11108 0.10379 0.14237 0.01621  0.00835  -0.00303 28  VAL B CG2 
2254 N N   . ARG B 33  ? 0.12188 0.11110 0.13292 0.01281  0.01659  -0.00146 29  ARG B N   
2255 C CA  . ARG B 33  ? 0.19339 0.18407 0.19847 0.00933  0.01863  0.00054  29  ARG B CA  
2256 C C   . ARG B 33  ? 0.15555 0.15389 0.16473 0.01372  0.02443  -0.00036 29  ARG B C   
2257 O O   . ARG B 33  ? 0.17790 0.18425 0.19153 0.01072  0.02627  0.00318  29  ARG B O   
2258 C CB  . ARG B 33  ? 0.28722 0.26440 0.27253 0.00632  0.01772  -0.00140 29  ARG B CB  
2259 C CG  . ARG B 33  ? 0.12724 0.09902 0.10880 0.00015  0.01184  0.00050  29  ARG B CG  
2260 C CD  . ARG B 33  ? 0.15688 0.11652 0.11842 -0.00534 0.01031  -0.00094 29  ARG B CD  
2261 N NE  . ARG B 33  ? 0.19020 0.14735 0.14952 -0.01268 0.00428  0.00175  29  ARG B NE  
2262 C CZ  . ARG B 33  ? 0.21303 0.15604 0.15808 -0.01633 0.00195  -0.00097 29  ARG B CZ  
2263 N NH1 . ARG B 33  ? 0.20687 0.13414 0.13675 -0.01270 0.00521  -0.00688 29  ARG B NH1 
2264 N NH2 . ARG B 33  ? 0.16454 0.10904 0.11080 -0.02380 -0.00350 0.00257  29  ARG B NH2 
2265 N N   . GLY B 34  ? 0.15014 0.14691 0.15852 0.02099  0.02752  -0.00435 30  GLY B N   
2266 C CA  . GLY B 34  ? 0.19654 0.20355 0.21115 0.02581  0.03353  -0.00482 30  GLY B CA  
2267 C C   . GLY B 34  ? 0.23900 0.26198 0.27318 0.02427  0.03324  -0.00162 30  GLY B C   
2268 O O   . GLY B 34  ? 0.22027 0.25422 0.26085 0.02485  0.03802  -0.00010 30  GLY B O   
2269 N N   . ARG B 35  ? 0.19012 0.21415 0.23323 0.02183  0.02807  -0.00072 31  ARG B N   
2270 C CA  . ARG B 35  ? 0.16980 0.20558 0.22950 0.01915  0.02722  0.00151  31  ARG B CA  
2271 C C   . ARG B 35  ? 0.11047 0.14639 0.17294 0.01219  0.02613  0.00597  31  ARG B C   
2272 O O   . ARG B 35  ? 0.11076 0.15484 0.18493 0.00920  0.02703  0.00844  31  ARG B O   
2273 C CB  . ARG B 35  ? 0.21747 0.25322 0.28383 0.02054  0.02269  -0.00060 31  ARG B CB  
2274 C CG  . ARG B 35  ? 0.21378 0.25222 0.28064 0.02774  0.02313  -0.00347 31  ARG B CG  
2275 C CD  . ARG B 35  ? 0.25916 0.31084 0.33425 0.03030  0.02796  -0.00262 31  ARG B CD  
2276 N NE  . ARG B 35  ? 0.44732 0.50777 0.52987 0.03695  0.02755  -0.00400 31  ARG B NE  
2277 C CZ  . ARG B 35  ? 0.37513 0.45265 0.47113 0.03833  0.03012  -0.00265 31  ARG B CZ  
2278 N NH1 . ARG B 35  ? 0.40327 0.48977 0.50629 0.03283  0.03352  -0.00002 31  ARG B NH1 
2279 N NH2 . ARG B 35  ? 0.53010 0.61533 0.63108 0.04427  0.02829  -0.00374 31  ARG B NH2 
2280 N N   . LEU B 36  ? 0.15826 0.18534 0.21063 0.00937  0.02389  0.00753  32  LEU B N   
2281 C CA  . LEU B 36  ? 0.18175 0.20945 0.23687 0.00388  0.02253  0.01295  32  LEU B CA  
2282 C C   . LEU B 36  ? 0.19904 0.23080 0.25004 0.00153  0.02644  0.01660  32  LEU B C   
2283 O O   . LEU B 36  ? 0.18195 0.21821 0.24078 -0.00211 0.02699  0.02163  32  LEU B O   
2284 C CB  . LEU B 36  ? 0.17185 0.19188 0.21895 0.00158  0.01830  0.01429  32  LEU B CB  
2285 C CG  . LEU B 36  ? 0.13577 0.15295 0.18785 0.00275  0.01490  0.01224  32  LEU B CG  
2286 C CD1 . LEU B 36  ? 0.12304 0.13466 0.16674 0.00003  0.01134  0.01386  32  LEU B CD1 
2287 C CD2 . LEU B 36  ? 0.21705 0.23838 0.28343 0.00182  0.01447  0.01428  32  LEU B CD2 
2288 N N   . THR B 37  ? 0.18470 0.25412 0.18722 0.02017  0.03053  -0.02307 33  THR B N   
2289 C CA  . THR B 37  ? 0.38322 0.46458 0.37599 0.01669  0.03463  -0.02442 33  THR B CA  
2290 C C   . THR B 37  ? 0.25873 0.35849 0.25849 0.01887  0.04127  -0.03048 33  THR B C   
2291 O O   . THR B 37  ? 0.29786 0.39916 0.30899 0.02624  0.04175  -0.03667 33  THR B O   
2292 C CB  . THR B 37  ? 0.40638 0.48373 0.39034 0.01917  0.03270  -0.02978 33  THR B CB  
2293 O OG1 . THR B 37  ? 0.57580 0.64665 0.56820 0.02642  0.03113  -0.03765 33  THR B OG1 
2294 C CG2 . THR B 37  ? 0.45252 0.51839 0.42779 0.01570  0.02676  -0.02252 33  THR B CG2 
2295 N N   . THR B 38  ? 0.24492 0.35909 0.23791 0.01263  0.04654  -0.02828 34  THR B N   
2296 C CA  . THR B 38  ? 0.45183 0.58721 0.45067 0.01515  0.05418  -0.03535 34  THR B CA  
2297 C C   . THR B 38  ? 0.41243 0.55112 0.40361 0.02057  0.05721  -0.04563 34  THR B C   
2298 O O   . THR B 38  ? 0.35956 0.50634 0.35805 0.02600  0.06099  -0.05275 34  THR B O   
2299 C CB  . THR B 38  ? 0.34229 0.49411 0.33720 0.00503  0.05984  -0.02896 34  THR B CB  
2300 O OG1 . THR B 38  ? 0.40722 0.55414 0.38303 -0.00204 0.05965  -0.02360 34  THR B OG1 
2301 C CG2 . THR B 38  ? 0.41960 0.56816 0.42264 -0.00110 0.05683  -0.02029 34  THR B CG2 
2302 N N   . GLY B 39  ? 0.37742 0.50401 0.35438 0.01864  0.05309  -0.04492 35  GLY B N   
2303 C CA  . GLY B 39  ? 0.53228 0.66153 0.49879 0.02180  0.05522  -0.05477 35  GLY B CA  
2304 C C   . GLY B 39  ? 0.41434 0.55670 0.36535 0.01496  0.06047  -0.05310 35  GLY B C   
2305 O O   . GLY B 39  ? 0.47558 0.61737 0.41712 0.01662  0.06126  -0.06036 35  GLY B O   
2306 N N   . ALA B 40  ? 0.35187 0.50306 0.29974 0.00638  0.06335  -0.04278 36  ALA B N   
2307 C CA  . ALA B 40  ? 0.39947 0.55998 0.33300 -0.00122 0.06774  -0.03895 36  ALA B CA  
2308 C C   . ALA B 40  ? 0.43694 0.58943 0.34827 -0.00589 0.06303  -0.03445 36  ALA B C   
2309 O O   . ALA B 40  ? 0.42603 0.58305 0.32348 -0.00870 0.06527  -0.03589 36  ALA B O   
2310 C CB  . ALA B 40  ? 0.43123 0.60087 0.36894 -0.01017 0.07148  -0.02842 36  ALA B CB  
2311 N N   . ASP B 41  ? 0.32233 0.45852 0.23264 -0.00615 0.05439  -0.02772 37  ASP B N   
2312 C CA  . ASP B 41  ? 0.27019 0.39620 0.16290 -0.00954 0.04707  -0.02143 37  ASP B CA  
2313 C C   . ASP B 41  ? 0.28215 0.39897 0.17677 -0.00233 0.04050  -0.03093 37  ASP B C   
2314 O O   . ASP B 41  ? 0.31767 0.42223 0.22648 0.00232  0.03520  -0.03122 37  ASP B O   
2315 C CB  . ASP B 41  ? 0.24845 0.35999 0.14153 -0.01412 0.04076  -0.00658 37  ASP B CB  
2316 C CG  . ASP B 41  ? 0.39160 0.49507 0.26582 -0.01768 0.03351  0.00222  37  ASP B CG  
2317 O OD1 . ASP B 41  ? 0.34085 0.45123 0.20064 -0.01763 0.03305  -0.00307 37  ASP B OD1 
2318 O OD2 . ASP B 41  ? 0.30660 0.39650 0.18001 -0.02015 0.02790  0.01424  37  ASP B OD2 
2319 N N   . VAL B 42  ? 0.24971 0.37273 0.12937 -0.00229 0.04103  -0.03887 38  VAL B N   
2320 C CA  . VAL B 42  ? 0.23623 0.35161 0.11603 0.00272  0.03497  -0.04922 38  VAL B CA  
2321 C C   . VAL B 42  ? 0.31670 0.43351 0.17423 -0.00195 0.02919  -0.04721 38  VAL B C   
2322 O O   . VAL B 42  ? 0.30765 0.43414 0.14918 -0.00636 0.03394  -0.04660 38  VAL B O   
2323 C CB  . VAL B 42  ? 0.23807 0.35908 0.12394 0.00909  0.04179  -0.06586 38  VAL B CB  
2324 C CG1 . VAL B 42  ? 0.28916 0.40067 0.17168 0.01197  0.03537  -0.07661 38  VAL B CG1 
2325 C CG2 . VAL B 42  ? 0.29289 0.41166 0.20154 0.01490  0.04541  -0.06718 38  VAL B CG2 
2326 N N   . ARG B 43  ? 0.25366 0.35991 0.11240 -0.00107 0.01840  -0.04509 39  ARG B N   
2327 C CA  . ARG B 43  ? 0.27766 0.38593 0.11707 -0.00474 0.01067  -0.04387 39  ARG B CA  
2328 C C   . ARG B 43  ? 0.27300 0.37676 0.11669 -0.00174 0.00473  -0.05696 39  ARG B C   
2329 O O   . ARG B 43  ? 0.26083 0.35489 0.12252 0.00155  -0.00014 -0.05706 39  ARG B O   
2330 C CB  . ARG B 43  ? 0.30016 0.40181 0.13703 -0.00711 0.00154  -0.02722 39  ARG B CB  
2331 C CG  . ARG B 43  ? 0.28121 0.37784 0.12601 -0.00826 0.00532  -0.01438 39  ARG B CG  
2332 C CD  . ARG B 43  ? 0.28009 0.38418 0.10637 -0.01526 0.01108  -0.00555 39  ARG B CD  
2333 N NE  . ARG B 43  ? 0.36744 0.46486 0.20261 -0.01746 0.01424  0.00585  39  ARG B NE  
2334 C CZ  . ARG B 43  ? 0.33942 0.42465 0.17247 -0.01900 0.00762  0.02028  39  ARG B CZ  
2335 N NH1 . ARG B 43  ? 0.28747 0.36775 0.10982 -0.01813 -0.00267 0.02671  39  ARG B NH1 
2336 N NH2 . ARG B 43  ? 0.26761 0.34517 0.10976 -0.02116 0.01094  0.02813  39  ARG B NH2 
2337 N N   . HIS B 44  ? 0.29342 0.40352 0.12031 -0.00364 0.00533  -0.06788 40  HIS B N   
2338 C CA  . HIS B 44  ? 0.29893 0.40297 0.12815 -0.00261 -0.00079 -0.08063 40  HIS B CA  
2339 C C   . HIS B 44  ? 0.31510 0.41035 0.16519 0.00317  0.00289  -0.09058 40  HIS B C   
2340 O O   . HIS B 44  ? 0.33161 0.41764 0.19300 0.00370  -0.00411 -0.09421 40  HIS B O   
2341 C CB  . HIS B 44  ? 0.29979 0.40284 0.12703 -0.00550 -0.01469 -0.07397 40  HIS B CB  
2342 C CG  . HIS B 44  ? 0.40215 0.51213 0.20897 -0.01020 -0.01977 -0.06251 40  HIS B CG  
2343 N ND1 . HIS B 44  ? 0.45513 0.56714 0.24347 -0.01369 -0.01895 -0.06651 40  HIS B ND1 
2344 C CD2 . HIS B 44  ? 0.37841 0.48961 0.18212 -0.01131 -0.02568 -0.04572 40  HIS B CD2 
2345 C CE1 . HIS B 44  ? 0.54388 0.65904 0.31766 -0.01701 -0.02431 -0.05291 40  HIS B CE1 
2346 N NE2 . HIS B 44  ? 0.43565 0.54981 0.21849 -0.01554 -0.02860 -0.03991 40  HIS B NE2 
2347 N N   . GLU B 45  ? 0.27587 0.37241 0.13393 0.00721  0.01370  -0.09236 41  GLU B N   
2348 C CA  . GLU B 45  ? 0.29132 0.37916 0.16880 0.01376  0.01830  -0.10002 41  GLU B CA  
2349 C C   . GLU B 45  ? 0.32540 0.40497 0.22242 0.01569  0.01486  -0.09036 41  GLU B C   
2350 O O   . GLU B 45  ? 0.26748 0.33755 0.18005 0.02054  0.01637  -0.09544 41  GLU B O   
2351 C CB  . GLU B 45  ? 0.36942 0.44517 0.24847 0.01508  0.01549  -0.11330 41  GLU B CB  
2352 C CG  . GLU B 45  ? 0.39438 0.47260 0.25639 0.01299  0.01818  -0.12046 41  GLU B CG  
2353 C CD  . GLU B 45  ? 0.58857 0.65248 0.45188 0.01456  0.01651  -0.13384 41  GLU B CD  
2354 O OE1 . GLU B 45  ? 0.60716 0.66090 0.47817 0.01297  0.00897  -0.13640 41  GLU B OE1 
2355 O OE2 . GLU B 45  ? 0.73616 0.79863 0.59274 0.01714  0.02291  -0.14170 41  GLU B OE2 
2356 N N   . ILE B 46  ? 0.23140 0.31254 0.12807 0.01229  0.01045  -0.07575 42  ILE B N   
2357 C CA  . ILE B 46  ? 0.21129 0.28370 0.12542 0.01391  0.00712  -0.06619 42  ILE B CA  
2358 C C   . ILE B 46  ? 0.25692 0.33337 0.17369 0.01363  0.01268  -0.05563 42  ILE B C   
2359 O O   . ILE B 46  ? 0.21101 0.29363 0.11502 0.00927  0.01251  -0.04710 42  ILE B O   
2360 C CB  . ILE B 46  ? 0.21650 0.28584 0.13026 0.01107  -0.00338 -0.05887 42  ILE B CB  
2361 C CG1 . ILE B 46  ? 0.23127 0.29944 0.14118 0.00929  -0.00942 -0.06982 42  ILE B CG1 
2362 C CG2 . ILE B 46  ? 0.28226 0.34294 0.21448 0.01355  -0.00548 -0.05115 42  ILE B CG2 
2363 C CD1 . ILE B 46  ? 0.26900 0.33853 0.17982 0.00643  -0.02037 -0.06349 42  ILE B CD1 
2364 N N   . PRO B 47  ? 0.22652 0.29929 0.15874 0.01744  0.01713  -0.05544 43  PRO B N   
2365 C CA  . PRO B 47  ? 0.20734 0.28460 0.14253 0.01591  0.02189  -0.04623 43  PRO B CA  
2366 C C   . PRO B 47  ? 0.20675 0.27740 0.14128 0.01260  0.01628  -0.03272 43  PRO B C   
2367 O O   . PRO B 47  ? 0.18791 0.24956 0.12823 0.01408  0.00960  -0.03039 43  PRO B O   
2368 C CB  . PRO B 47  ? 0.28144 0.35505 0.23423 0.02134  0.02545  -0.05010 43  PRO B CB  
2369 C CG  . PRO B 47  ? 0.21888 0.28878 0.17393 0.02608  0.02556  -0.06320 43  PRO B CG  
2370 C CD  . PRO B 47  ? 0.21164 0.27660 0.15765 0.02292  0.01829  -0.06444 43  PRO B CD  
2371 N N   . VAL B 48  ? 0.19822 0.27340 0.12611 0.00806  0.01945  -0.02393 44  VAL B N   
2372 C CA  . VAL B 48  ? 0.18058 0.24714 0.10670 0.00513  0.01493  -0.01093 44  VAL B CA  
2373 C C   . VAL B 48  ? 0.16943 0.23267 0.10680 0.00446  0.01878  -0.00666 44  VAL B C   
2374 O O   . VAL B 48  ? 0.19283 0.26606 0.13230 0.00249  0.02576  -0.00906 44  VAL B O   
2375 C CB  . VAL B 48  ? 0.19945 0.27010 0.10634 -0.00104 0.01421  -0.00255 44  VAL B CB  
2376 C CG1 . VAL B 48  ? 0.20185 0.25988 0.10731 -0.00288 0.00889  0.01098  44  VAL B CG1 
2377 C CG2 . VAL B 48  ? 0.29195 0.36729 0.18619 -0.00072 0.00965  -0.00734 44  VAL B CG2 
2378 N N   . LEU B 49  ? 0.16164 0.21211 0.10638 0.00607  0.01417  -0.00078 45  LEU B N   
2379 C CA  . LEU B 49  ? 0.15364 0.19892 0.10696 0.00474  0.01651  0.00332  45  LEU B CA  
2380 C C   . LEU B 49  ? 0.18450 0.23120 0.12804 -0.00313 0.01919  0.01215  45  LEU B C   
2381 O O   . LEU B 49  ? 0.18047 0.22784 0.10984 -0.00680 0.01772  0.01770  45  LEU B O   
2382 C CB  . LEU B 49  ? 0.17269 0.20339 0.13338 0.00838  0.01118  0.00689  45  LEU B CB  
2383 C CG  . LEU B 49  ? 0.17402 0.20300 0.14577 0.01458  0.00931  -0.00068 45  LEU B CG  
2384 C CD1 . LEU B 49  ? 0.13147 0.14866 0.10926 0.01772  0.00486  0.00344  45  LEU B CD1 
2385 C CD2 . LEU B 49  ? 0.13962 0.17279 0.12114 0.01643  0.01396  -0.00719 45  LEU B CD2 
2386 N N   . PRO B 50  ? 0.16103 0.20827 0.11131 -0.00665 0.02278  0.01398  46  PRO B N   
2387 C CA  . PRO B 50  ? 0.17398 0.22233 0.11569 -0.01606 0.02562  0.02248  46  PRO B CA  
2388 C C   . PRO B 50  ? 0.18725 0.21747 0.11847 -0.01854 0.01995  0.03333  46  PRO B C   
2389 O O   . PRO B 50  ? 0.21631 0.23218 0.15183 -0.01294 0.01444  0.03441  46  PRO B O   
2390 C CB  . PRO B 50  ? 0.29948 0.35019 0.25353 -0.01867 0.02857  0.02120  46  PRO B CB  
2391 C CG  . PRO B 50  ? 0.30230 0.36107 0.26942 -0.01046 0.02961  0.01075  46  PRO B CG  
2392 C CD  . PRO B 50  ? 0.18947 0.23877 0.15492 -0.00312 0.02460  0.00801  46  PRO B CD  
2393 N N   . ASN B 51  ? 0.20547 0.23674 0.12277 -0.02682 0.02168  0.04163  47  ASN B N   
2394 C CA  . ASN B 51  ? 0.22696 0.23931 0.13276 -0.02987 0.01643  0.05362  47  ASN B CA  
2395 C C   . ASN B 51  ? 0.24939 0.24620 0.16133 -0.03355 0.01599  0.05753  47  ASN B C   
2396 O O   . ASN B 51  ? 0.22410 0.22746 0.13905 -0.04194 0.02119  0.05766  47  ASN B O   
2397 C CB  . ASN B 51  ? 0.27829 0.29632 0.16597 -0.03889 0.01906  0.06195  47  ASN B CB  
2398 C CG  . ASN B 51  ? 0.28348 0.27999 0.15724 -0.04182 0.01294  0.07592  47  ASN B CG  
2399 O OD1 . ASN B 51  ? 0.29220 0.26986 0.17047 -0.03564 0.00654  0.07859  47  ASN B OD1 
2400 N ND2 . ASN B 51  ? 0.34672 0.34594 0.20296 -0.05090 0.01514  0.08507  47  ASN B ND2 
2401 N N   . ARG B 52  ? 0.22441 0.20158 0.13846 -0.02729 0.00976  0.06011  48  ARG B N   
2402 C CA  . ARG B 52  ? 0.23017 0.18989 0.14889 -0.02949 0.00886  0.06206  48  ARG B CA  
2403 C C   . ARG B 52  ? 0.35199 0.30055 0.25917 -0.04158 0.01008  0.07233  48  ARG B C   
2404 O O   . ARG B 52  ? 0.30042 0.24056 0.21139 -0.04785 0.01145  0.07224  48  ARG B O   
2405 C CB  . ARG B 52  ? 0.30266 0.24429 0.22429 -0.01917 0.00249  0.06270  48  ARG B CB  
2406 C CG  . ARG B 52  ? 0.44931 0.37295 0.37681 -0.01820 0.00165  0.06121  48  ARG B CG  
2407 C CD  . ARG B 52  ? 0.54853 0.45262 0.47452 -0.00879 -0.00432 0.06511  48  ARG B CD  
2408 N NE  . ARG B 52  ? 0.66425 0.56448 0.60208 -0.00007 -0.00468 0.05728  48  ARG B NE  
2409 C CZ  . ARG B 52  ? 0.70241 0.61407 0.64963 0.00889  -0.00563 0.05156  48  ARG B CZ  
2410 N NH1 . ARG B 52  ? 0.54873 0.47617 0.49543 0.01052  -0.00689 0.05151  48  ARG B NH1 
2411 N NH2 . ARG B 52  ? 0.66510 0.57225 0.62174 0.01559  -0.00513 0.04551  48  ARG B NH2 
2412 N N   . VAL B 53  ? 0.30905 0.25732 0.20130 -0.04593 0.00944  0.08134  49  VAL B N   
2413 C CA  . VAL B 53  ? 0.31062 0.24340 0.18939 -0.05742 0.00957  0.09349  49  VAL B CA  
2414 C C   . VAL B 53  ? 0.40865 0.35812 0.28965 -0.07106 0.01761  0.09236  49  VAL B C   
2415 O O   . VAL B 53  ? 0.40834 0.38190 0.28736 -0.07447 0.02320  0.09020  49  VAL B O   
2416 C CB  . VAL B 53  ? 0.38740 0.31543 0.24800 -0.05773 0.00603  0.10451  49  VAL B CB  
2417 C CG1 . VAL B 53  ? 0.40292 0.31482 0.25394 -0.06708 0.00656  0.11463  49  VAL B CG1 
2418 C CG2 . VAL B 53  ? 0.37997 0.29545 0.24150 -0.04346 -0.00264 0.10516  49  VAL B CG2 
2419 N N   . GLY B 54  ? 0.48663 0.42421 0.37205 -0.07898 0.01824  0.09328  50  GLY B N   
2420 C CA  . GLY B 54  ? 0.51471 0.46907 0.40498 -0.09267 0.02502  0.09230  50  GLY B CA  
2421 C C   . GLY B 54  ? 0.46396 0.44417 0.37276 -0.08872 0.02890  0.07937  50  GLY B C   
2422 O O   . GLY B 54  ? 0.44157 0.44088 0.35715 -0.09894 0.03452  0.07784  50  GLY B O   
2423 N N   . LEU B 55  ? 0.27588 0.25782 0.19351 -0.07449 0.02599  0.07061  51  LEU B N   
2424 C CA  . LEU B 55  ? 0.33182 0.33565 0.26612 -0.06952 0.02888  0.05920  51  LEU B CA  
2425 C C   . LEU B 55  ? 0.32913 0.32905 0.27287 -0.07565 0.02805  0.05672  51  LEU B C   
2426 O O   . LEU B 55  ? 0.32502 0.30067 0.26630 -0.07415 0.02304  0.05784  51  LEU B O   
2427 C CB  . LEU B 55  ? 0.24639 0.24813 0.18614 -0.05413 0.02532  0.05191  51  LEU B CB  
2428 C CG  . LEU B 55  ? 0.26361 0.28396 0.21907 -0.04710 0.02737  0.04086  51  LEU B CG  
2429 C CD1 . LEU B 55  ? 0.28095 0.32813 0.23893 -0.04783 0.03366  0.03694  51  LEU B CD1 
2430 C CD2 . LEU B 55  ? 0.23673 0.24800 0.19624 -0.03412 0.02305  0.03559  51  LEU B CD2 
2431 N N   . PRO B 56  ? 0.34521 0.36877 0.29964 -0.08252 0.03259  0.05307  52  PRO B N   
2432 C CA  . PRO B 56  ? 0.25743 0.27901 0.22061 -0.08937 0.03065  0.05067  52  PRO B CA  
2433 C C   . PRO B 56  ? 0.26985 0.28204 0.24009 -0.07788 0.02567  0.04311  52  PRO B C   
2434 O O   . PRO B 56  ? 0.18590 0.20614 0.16168 -0.06540 0.02566  0.03733  52  PRO B O   
2435 C CB  . PRO B 56  ? 0.31100 0.36695 0.28721 -0.09561 0.03647  0.04727  52  PRO B CB  
2436 C CG  . PRO B 56  ? 0.30896 0.37797 0.27714 -0.09844 0.04274  0.05176  52  PRO B CG  
2437 C CD  . PRO B 56  ? 0.26973 0.32335 0.22770 -0.08580 0.03987  0.05172  52  PRO B CD  
2438 N N   . ILE B 57  ? 0.26982 0.26406 0.23875 -0.08311 0.02160  0.04312  53  ILE B N   
2439 C CA  . ILE B 57  ? 0.24096 0.22377 0.21343 -0.07365 0.01721  0.03661  53  ILE B CA  
2440 C C   . ILE B 57  ? 0.20557 0.21305 0.19257 -0.06746 0.01783  0.02899  53  ILE B C   
2441 O O   . ILE B 57  ? 0.17217 0.17583 0.16207 -0.05608 0.01573  0.02406  53  ILE B O   
2442 C CB  . ILE B 57  ? 0.27113 0.23135 0.23785 -0.08239 0.01334  0.03721  53  ILE B CB  
2443 C CG1 . ILE B 57  ? 0.29836 0.24685 0.26648 -0.07292 0.00955  0.03013  53  ILE B CG1 
2444 C CG2 . ILE B 57  ? 0.30911 0.28466 0.28178 -0.09787 0.01417  0.03765  53  ILE B CG2 
2445 C CD1 . ILE B 57  ? 0.35436 0.28516 0.31670 -0.05977 0.00868  0.03025  53  ILE B CD1 
2446 N N   . ASN B 58  ? 0.26182 0.29523 0.25855 -0.07456 0.02077  0.02830  54  ASN B N   
2447 C CA  . ASN B 58  ? 0.26703 0.32398 0.27854 -0.06766 0.02072  0.02166  54  ASN B CA  
2448 C C   . ASN B 58  ? 0.21718 0.28416 0.23224 -0.05433 0.02359  0.01831  54  ASN B C   
2449 O O   . ASN B 58  ? 0.23122 0.31246 0.25738 -0.04612 0.02298  0.01287  54  ASN B O   
2450 C CB  . ASN B 58  ? 0.35931 0.44374 0.38235 -0.07831 0.02313  0.02181  54  ASN B CB  
2451 C CG  . ASN B 58  ? 0.41494 0.50656 0.43303 -0.08910 0.02901  0.02797  54  ASN B CG  
2452 O OD1 . ASN B 58  ? 0.70845 0.78097 0.71500 -0.10013 0.02826  0.03422  54  ASN B OD1 
2453 N ND2 . ASN B 58  ? 0.64732 0.76558 0.67316 -0.08594 0.03513  0.02628  54  ASN B ND2 
2454 N N   . GLN B 59  ? 0.15015 0.20912 0.15551 -0.05215 0.02607  0.02146  55  GLN B N   
2455 C CA  . GLN B 59  ? 0.17833 0.24388 0.18496 -0.04062 0.02812  0.01762  55  GLN B CA  
2456 C C   . GLN B 59  ? 0.16430 0.20697 0.16243 -0.03270 0.02462  0.01817  55  GLN B C   
2457 O O   . GLN B 59  ? 0.17595 0.22104 0.17272 -0.02506 0.02565  0.01581  55  GLN B O   
2458 C CB  . GLN B 59  ? 0.16973 0.25056 0.17249 -0.04456 0.03408  0.01969  55  GLN B CB  
2459 C CG  . GLN B 59  ? 0.28890 0.39504 0.30061 -0.05379 0.03885  0.01986  55  GLN B CG  
2460 C CD  . GLN B 59  ? 0.33869 0.45641 0.34228 -0.06101 0.04545  0.02399  55  GLN B CD  
2461 O OE1 . GLN B 59  ? 0.32768 0.44370 0.32267 -0.05517 0.04733  0.02315  55  GLN B OE1 
2462 N NE2 . GLN B 59  ? 0.41538 0.54533 0.42092 -0.07471 0.04892  0.02860  55  GLN B NE2 
2463 N N   . ARG B 60  ? 0.16631 0.18778 0.15933 -0.03429 0.02056  0.02048  56  ARG B N   
2464 C CA  . ARG B 60  ? 0.15657 0.15775 0.14188 -0.02777 0.01786  0.02213  56  ARG B CA  
2465 C C   . ARG B 60  ? 0.15123 0.15012 0.14260 -0.01687 0.01607  0.01640  56  ARG B C   
2466 O O   . ARG B 60  ? 0.13341 0.12414 0.12203 -0.01010 0.01488  0.01648  56  ARG B O   
2467 C CB  . ARG B 60  ? 0.16410 0.14234 0.14079 -0.03358 0.01507  0.02687  56  ARG B CB  
2468 C CG  . ARG B 60  ? 0.16888 0.12671 0.13940 -0.02585 0.01221  0.02856  56  ARG B CG  
2469 C CD  . ARG B 60  ? 0.27143 0.22979 0.23540 -0.02391 0.01228  0.03367  56  ARG B CD  
2470 N NE  . ARG B 60  ? 0.29011 0.23227 0.25087 -0.01548 0.00881  0.03526  56  ARG B NE  
2471 C CZ  . ARG B 60  ? 0.37927 0.30016 0.33213 -0.01631 0.00609  0.04086  56  ARG B CZ  
2472 N NH1 . ARG B 60  ? 0.42379 0.33406 0.36942 -0.02647 0.00628  0.04582  56  ARG B NH1 
2473 N NH2 . ARG B 60  ? 0.44427 0.35421 0.39718 -0.00672 0.00304  0.04147  56  ARG B NH2 
2474 N N   . PHE B 61  ? 0.13250 0.13897 0.13202 -0.01543 0.01555  0.01200  57  PHE B N   
2475 C CA  . PHE B 61  ? 0.12602 0.12719 0.12916 -0.00681 0.01380  0.00802  57  PHE B CA  
2476 C C   . PHE B 61  ? 0.10655 0.12433 0.11967 -0.00194 0.01459  0.00362  57  PHE B C   
2477 O O   . PHE B 61  ? 0.10928 0.14337 0.12840 -0.00528 0.01585  0.00288  57  PHE B O   
2478 C CB  . PHE B 61  ? 0.12283 0.11025 0.12269 -0.00886 0.01118  0.00765  57  PHE B CB  
2479 C CG  . PHE B 61  ? 0.13714 0.10489 0.12748 -0.01207 0.01026  0.01102  57  PHE B CG  
2480 C CD1 . PHE B 61  ? 0.13755 0.09327 0.12474 -0.00518 0.01003  0.01179  57  PHE B CD1 
2481 C CD2 . PHE B 61  ? 0.18274 0.14384 0.16804 -0.02190 0.00934  0.01336  57  PHE B CD2 
2482 C CE1 . PHE B 61  ? 0.19787 0.13494 0.17728 -0.00629 0.00887  0.01495  57  PHE B CE1 
2483 C CE2 . PHE B 61  ? 0.21837 0.15789 0.19434 -0.02415 0.00824  0.01646  57  PHE B CE2 
2484 C CZ  . PHE B 61  ? 0.17805 0.10530 0.15118 -0.01543 0.00798  0.01729  57  PHE B CZ  
2485 N N   . ILE B 62  ? 0.09981 0.11325 0.11533 0.00616  0.01385  0.00088  58  ILE B N   
2486 C CA  . ILE B 62  ? 0.09288 0.11516 0.11653 0.01166  0.01330  -0.00253 58  ILE B CA  
2487 C C   . ILE B 62  ? 0.10943 0.11938 0.13101 0.01486  0.01099  -0.00263 58  ILE B C   
2488 O O   . ILE B 62  ? 0.14115 0.13765 0.15666 0.01473  0.01093  -0.00145 58  ILE B O   
2489 C CB  . ILE B 62  ? 0.08846 0.11763 0.11655 0.01809  0.01531  -0.00602 58  ILE B CB  
2490 C CG1 . ILE B 62  ? 0.12073 0.13743 0.14482 0.02167  0.01497  -0.00636 58  ILE B CG1 
2491 C CG2 . ILE B 62  ? 0.09084 0.13400 0.11954 0.01511  0.01859  -0.00672 58  ILE B CG2 
2492 C CD1 . ILE B 62  ? 0.14412 0.16512 0.17164 0.02700  0.01618  -0.01081 58  ILE B CD1 
2493 N N   . LEU B 63  ? 0.10945 0.12485 0.13612 0.01823  0.00922  -0.00386 59  LEU B N   
2494 C CA  . LEU B 63  ? 0.13783 0.14331 0.16108 0.02054  0.00720  -0.00333 59  LEU B CA  
2495 C C   . LEU B 63  ? 0.08860 0.09311 0.11611 0.02782  0.00732  -0.00431 59  LEU B C   
2496 O O   . LEU B 63  ? 0.12216 0.13622 0.15699 0.03174  0.00720  -0.00591 59  LEU B O   
2497 C CB  . LEU B 63  ? 0.11586 0.12637 0.13872 0.01718  0.00362  -0.00260 59  LEU B CB  
2498 C CG  . LEU B 63  ? 0.17209 0.18372 0.19139 0.00823  0.00289  -0.00205 59  LEU B CG  
2499 C CD1 . LEU B 63  ? 0.12479 0.14371 0.14471 0.00452  -0.00173 -0.00206 59  LEU B CD1 
2500 C CD2 . LEU B 63  ? 0.11586 0.10954 0.12509 0.00556  0.00434  -0.00169 59  LEU B CD2 
2501 N N   . VAL B 64  ? 0.09018 0.08281 0.11323 0.02950  0.00786  -0.00349 60  VAL B N   
2502 C CA  . VAL B 64  ? 0.12270 0.11113 0.14833 0.03461  0.00792  -0.00346 60  VAL B CA  
2503 C C   . VAL B 64  ? 0.12411 0.10579 0.14384 0.03449  0.00635  -0.00067 60  VAL B C   
2504 O O   . VAL B 64  ? 0.10798 0.08203 0.12094 0.03201  0.00806  -0.00008 60  VAL B O   
2505 C CB  . VAL B 64  ? 0.16491 0.14729 0.19108 0.03543  0.01058  -0.00471 60  VAL B CB  
2506 C CG1 . VAL B 64  ? 0.21289 0.18795 0.24008 0.03821  0.01077  -0.00386 60  VAL B CG1 
2507 C CG2 . VAL B 64  ? 0.20838 0.19800 0.23893 0.03622  0.01140  -0.00775 60  VAL B CG2 
2508 N N   . GLU B 65  ? 0.16187 0.14656 0.18369 0.03771  0.00315  0.00104  61  GLU B N   
2509 C CA  . GLU B 65  ? 0.14462 0.12355 0.15901 0.03761  0.00086  0.00461  61  GLU B CA  
2510 C C   . GLU B 65  ? 0.13511 0.10400 0.14878 0.04077  0.00223  0.00703  61  GLU B C   
2511 O O   . GLU B 65  ? 0.15601 0.12462 0.17631 0.04551  0.00101  0.00709  61  GLU B O   
2512 C CB  . GLU B 65  ? 0.22058 0.20917 0.23722 0.03919  -0.00476 0.00631  61  GLU B CB  
2513 C CG  . GLU B 65  ? 0.32658 0.30945 0.33507 0.04046  -0.00841 0.01110  61  GLU B CG  
2514 C CD  . GLU B 65  ? 0.53740 0.53028 0.54353 0.03837  -0.01450 0.01222  61  GLU B CD  
2515 O OE1 . GLU B 65  ? 0.71754 0.71161 0.71756 0.03178  -0.01427 0.00981  61  GLU B OE1 
2516 O OE2 . GLU B 65  ? 0.61225 0.61157 0.62290 0.04338  -0.02000 0.01538  61  GLU B OE2 
2517 N N   . LEU B 66  ? 0.13067 0.09107 0.13642 0.03791  0.00516  0.00868  62  LEU B N   
2518 C CA  . LEU B 66  ? 0.13037 0.08146 0.13490 0.03857  0.00737  0.01159  62  LEU B CA  
2519 C C   . LEU B 66  ? 0.16880 0.11450 0.16279 0.03800  0.00550  0.01716  62  LEU B C   
2520 O O   . LEU B 66  ? 0.17328 0.12020 0.15792 0.03504  0.00559  0.01726  62  LEU B O   
2521 C CB  . LEU B 66  ? 0.12004 0.06849 0.12474 0.03538  0.01297  0.00964  62  LEU B CB  
2522 C CG  . LEU B 66  ? 0.13959 0.09303 0.15287 0.03570  0.01412  0.00502  62  LEU B CG  
2523 C CD1 . LEU B 66  ? 0.13907 0.09153 0.15339 0.03340  0.01860  0.00392  62  LEU B CD1 
2524 C CD2 . LEU B 66  ? 0.14978 0.10274 0.17071 0.03862  0.01239  0.00372  62  LEU B CD2 
2525 N N   . SER B 67  ? 0.16675 0.10520 0.16099 0.04068  0.00361  0.02176  63  SER B N   
2526 C CA  . SER B 67  ? 0.18720 0.11869 0.16991 0.04000  0.00169  0.02878  63  SER B CA  
2527 C C   . SER B 67  ? 0.22256 0.14194 0.20392 0.03800  0.00544  0.03291  63  SER B C   
2528 O O   . SER B 67  ? 0.17491 0.09110 0.16594 0.03852  0.00732  0.03021  63  SER B O   
2529 C CB  . SER B 67  ? 0.23283 0.16659 0.21635 0.04565  -0.00625 0.03252  63  SER B CB  
2530 O OG  . SER B 67  ? 0.32235 0.26986 0.31048 0.04652  -0.00957 0.02820  63  SER B OG  
2531 N N   . ASN B 68  ? 0.18559 0.09830 0.15409 0.03478  0.00655  0.03949  64  ASN B N   
2532 C CA  . ASN B 68  ? 0.20070 0.10244 0.16710 0.03073  0.01101  0.04427  64  ASN B CA  
2533 C C   . ASN B 68  ? 0.25306 0.14387 0.20674 0.03098  0.00724  0.05452  64  ASN B C   
2534 O O   . ASN B 68  ? 0.22414 0.11697 0.17246 0.03546  0.00029  0.05742  64  ASN B O   
2535 C CB  . ASN B 68  ? 0.19233 0.09895 0.15649 0.02434  0.01957  0.04155  64  ASN B CB  
2536 C CG  . ASN B 68  ? 0.20041 0.11108 0.14942 0.02197  0.02161  0.04268  64  ASN B CG  
2537 O OD1 . ASN B 68  ? 0.20969 0.11893 0.14791 0.02371  0.01614  0.04653  64  ASN B OD1 
2538 N ND2 . ASN B 68  ? 0.23117 0.14746 0.17931 0.01827  0.02937  0.03884  64  ASN B ND2 
2539 N N   . HIS B 69  ? 0.24259 0.12215 0.19166 0.02568  0.01148  0.06062  65  HIS B N   
2540 C CA  . HIS B 69  ? 0.29312 0.15939 0.22865 0.02514  0.00810  0.07207  65  HIS B CA  
2541 C C   . HIS B 69  ? 0.33305 0.20496 0.25050 0.02342  0.00723  0.07604  65  HIS B C   
2542 O O   . HIS B 69  ? 0.32377 0.18927 0.23020 0.02636  0.00026  0.08442  65  HIS B O   
2543 C CB  . HIS B 69  ? 0.31652 0.17028 0.24958 0.01721  0.01426  0.07804  65  HIS B CB  
2544 C CG  . HIS B 69  ? 0.27366 0.11478 0.21965 0.01857  0.01250  0.07707  65  HIS B CG  
2545 N ND1 . HIS B 69  ? 0.40722 0.25361 0.36803 0.01602  0.01670  0.06821  65  HIS B ND1 
2546 C CD2 . HIS B 69  ? 0.34081 0.16863 0.28889 0.02099  0.00531  0.08136  65  HIS B CD2 
2547 C CE1 . HIS B 69  ? 0.37456 0.20842 0.34320 0.01684  0.01302  0.06745  65  HIS B CE1 
2548 N NE2 . HIS B 69  ? 0.32436 0.14778 0.28633 0.01976  0.00575  0.07447  65  HIS B NE2 
2549 N N   . ALA B 70  ? 0.25832 0.14147 0.17176 0.01896  0.01392  0.07011  66  ALA B N   
2550 C CA  . ALA B 70  ? 0.26864 0.15704 0.16377 0.01714  0.01334  0.07153  66  ALA B CA  
2551 C C   . ALA B 70  ? 0.33139 0.22759 0.22711 0.02294  0.00406  0.06800  66  ALA B C   
2552 O O   . ALA B 70  ? 0.29183 0.19251 0.17213 0.02125  0.00182  0.06829  66  ALA B O   
2553 C CB  . ALA B 70  ? 0.29932 0.19651 0.19119 0.01190  0.02358  0.06450  66  ALA B CB  
2554 N N   . GLU B 71  ? 0.24733 0.14623 0.16035 0.02904  -0.00103 0.06423  67  GLU B N   
2555 C CA  . GLU B 71  ? 0.24019 0.14910 0.15782 0.03424  -0.00959 0.06098  67  GLU B CA  
2556 C C   . GLU B 71  ? 0.31616 0.23627 0.23088 0.03073  -0.00730 0.05217  67  GLU B C   
2557 O O   . GLU B 71  ? 0.29085 0.21892 0.20111 0.03131  -0.01395 0.05081  67  GLU B O   
2558 C CB  . GLU B 71  ? 0.31244 0.21889 0.21909 0.03761  -0.01924 0.07023  67  GLU B CB  
2559 C CG  . GLU B 71  ? 0.33849 0.23268 0.25191 0.04386  -0.02360 0.07818  67  GLU B CG  
2560 C CD  . GLU B 71  ? 0.63924 0.53014 0.54196 0.04852  -0.03406 0.08872  67  GLU B CD  
2561 O OE1 . GLU B 71  ? 0.47432 0.37609 0.36689 0.04732  -0.03941 0.08874  67  GLU B OE1 
2562 O OE2 . GLU B 71  ? 0.66174 0.53912 0.56656 0.05302  -0.03737 0.09678  67  GLU B OE2 
2563 N N   . LEU B 72  ? 0.23470 0.15510 0.15246 0.02707  0.00170  0.04616  68  LEU B N   
2564 C CA  . LEU B 72  ? 0.20881 0.13683 0.12802 0.02517  0.00421  0.03696  68  LEU B CA  
2565 C C   . LEU B 72  ? 0.25084 0.18438 0.18904 0.02843  0.00307  0.03155  68  LEU B C   
2566 O O   . LEU B 72  ? 0.20563 0.13643 0.15551 0.03098  0.00429  0.03270  68  LEU B O   
2567 C CB  . LEU B 72  ? 0.21978 0.14568 0.13315 0.02106  0.01439  0.03348  68  LEU B CB  
2568 C CG  . LEU B 72  ? 0.29900 0.22056 0.19236 0.01710  0.01778  0.03839  68  LEU B CG  
2569 C CD1 . LEU B 72  ? 0.26123 0.18336 0.15305 0.01403  0.02933  0.03466  68  LEU B CD1 
2570 C CD2 . LEU B 72  ? 0.36439 0.28835 0.24144 0.01569  0.01210  0.03674  68  LEU B CD2 
2571 N N   . SER B 73  ? 0.24218 0.18295 0.18224 0.02759  0.00075  0.02555  69  SER B N   
2572 C CA  . SER B 73  ? 0.19593 0.14304 0.15163 0.02960  -0.00010 0.02086  69  SER B CA  
2573 C C   . SER B 73  ? 0.22015 0.16802 0.17514 0.02629  0.00410  0.01400  69  SER B C   
2574 O O   . SER B 73  ? 0.18680 0.13306 0.12994 0.02280  0.00408  0.01147  69  SER B O   
2575 C CB  . SER B 73  ? 0.22028 0.17693 0.18191 0.03200  -0.00843 0.02163  69  SER B CB  
2576 O OG  . SER B 73  ? 0.41754 0.37279 0.38351 0.03743  -0.01244 0.02754  69  SER B OG  
2577 N N   . VAL B 74  ? 0.15041 0.09961 0.11719 0.02755  0.00729  0.01094  70  VAL B N   
2578 C CA  . VAL B 74  ? 0.14107 0.09027 0.10902 0.02551  0.00988  0.00549  70  VAL B CA  
2579 C C   . VAL B 74  ? 0.15007 0.10604 0.13062 0.02668  0.00765  0.00414  70  VAL B C   
2580 O O   . VAL B 74  ? 0.13972 0.09902 0.12905 0.02993  0.00668  0.00594  70  VAL B O   
2581 C CB  . VAL B 74  ? 0.19403 0.13806 0.16182 0.02597  0.01718  0.00353  70  VAL B CB  
2582 C CG1 . VAL B 74  ? 0.16869 0.10787 0.12316 0.02447  0.02088  0.00409  70  VAL B CG1 
2583 C CG2 . VAL B 74  ? 0.13997 0.08558 0.11915 0.02838  0.01936  0.00547  70  VAL B CG2 
2584 N N   . THR B 75  ? 0.12733 0.08447 0.10777 0.02370  0.00707  0.00083  71  THR B N   
2585 C CA  . THR B 75  ? 0.12952 0.09394 0.11995 0.02355  0.00572  -0.00005 71  THR B CA  
2586 C C   . THR B 75  ? 0.11511 0.07457 0.10678 0.02289  0.00940  -0.00216 71  THR B C   
2587 O O   . THR B 75  ? 0.13175 0.08425 0.11664 0.01999  0.01014  -0.00414 71  THR B O   
2588 C CB  . THR B 75  ? 0.14286 0.11513 0.13328 0.01941  0.00090  -0.00059 71  THR B CB  
2589 O OG1 . THR B 75  ? 0.23015 0.20886 0.22084 0.02131  -0.00363 0.00196  71  THR B OG1 
2590 C CG2 . THR B 75  ? 0.11188 0.09354 0.11257 0.01879  0.00091  -0.00116 71  THR B CG2 
2591 N N   . LEU B 76  ? 0.15159 0.11387 0.15139 0.02579  0.01112  -0.00184 72  LEU B N   
2592 C CA  . LEU B 76  ? 0.16576 0.12534 0.16759 0.02589  0.01327  -0.00279 72  LEU B CA  
2593 C C   . LEU B 76  ? 0.19766 0.16269 0.20166 0.02278  0.01137  -0.00267 72  LEU B C   
2594 O O   . LEU B 76  ? 0.10349 0.07824 0.11228 0.02254  0.00966  -0.00248 72  LEU B O   
2595 C CB  . LEU B 76  ? 0.11193 0.07336 0.12063 0.02946  0.01520  -0.00263 72  LEU B CB  
2596 C CG  . LEU B 76  ? 0.21937 0.17622 0.22804 0.03141  0.01865  -0.00272 72  LEU B CG  
2597 C CD1 . LEU B 76  ? 0.15353 0.10584 0.15468 0.03069  0.02008  -0.00226 72  LEU B CD1 
2598 C CD2 . LEU B 76  ? 0.31130 0.27191 0.32771 0.03299  0.01924  -0.00246 72  LEU B CD2 
2599 N N   . ALA B 77  ? 0.11879 0.07754 0.11929 0.02058  0.01193  -0.00255 73  ALA B N   
2600 C CA  . ALA B 77  ? 0.13689 0.09956 0.13812 0.01657  0.01089  -0.00123 73  ALA B CA  
2601 C C   . ALA B 77  ? 0.17109 0.13374 0.17475 0.01927  0.01196  0.00002  73  ALA B C   
2602 O O   . ALA B 77  ? 0.12337 0.07790 0.12572 0.02238  0.01279  0.00028  73  ALA B O   
2603 C CB  . ALA B 77  ? 0.19692 0.15013 0.19066 0.01076  0.00983  -0.00094 73  ALA B CB  
2604 N N   . LEU B 78  ? 0.12064 0.09360 0.12788 0.01841  0.01186  0.00047  74  LEU B N   
2605 C CA  . LEU B 78  ? 0.12391 0.09878 0.13190 0.02029  0.01209  0.00142  74  LEU B CA  
2606 C C   . LEU B 78  ? 0.16460 0.14082 0.16774 0.01510  0.01181  0.00462  74  LEU B C   
2607 O O   . LEU B 78  ? 0.12980 0.11370 0.13322 0.01031  0.01243  0.00479  74  LEU B O   
2608 C CB  . LEU B 78  ? 0.12744 0.11230 0.14134 0.02353  0.01264  -0.00152 74  LEU B CB  
2609 C CG  . LEU B 78  ? 0.14233 0.12436 0.16049 0.02807  0.01278  -0.00347 74  LEU B CG  
2610 C CD1 . LEU B 78  ? 0.22713 0.20337 0.24531 0.02897  0.01336  -0.00347 74  LEU B CD1 
2611 C CD2 . LEU B 78  ? 0.16080 0.15005 0.18348 0.03013  0.01296  -0.00692 74  LEU B CD2 
2612 N N   . ASP B 79  ? 0.11290 0.08265 0.11200 0.01598  0.01078  0.00769  75  ASP B N   
2613 C CA  . ASP B 79  ? 0.14626 0.11554 0.13871 0.01098  0.01031  0.01229  75  ASP B CA  
2614 C C   . ASP B 79  ? 0.18968 0.17285 0.18277 0.01125  0.01116  0.01123  75  ASP B C   
2615 O O   . ASP B 79  ? 0.15325 0.13862 0.14837 0.01608  0.00995  0.00947  75  ASP B O   
2616 C CB  . ASP B 79  ? 0.16470 0.11951 0.15193 0.01318  0.00793  0.01669  75  ASP B CB  
2617 C CG  . ASP B 79  ? 0.31402 0.26380 0.29206 0.00741  0.00689  0.02330  75  ASP B CG  
2618 O OD1 . ASP B 79  ? 0.21910 0.18034 0.19467 0.00226  0.00845  0.02448  75  ASP B OD1 
2619 O OD2 . ASP B 79  ? 0.31367 0.24730 0.28654 0.00828  0.00475  0.02751  75  ASP B OD2 
2620 N N   . VAL B 80  ? 0.18642 0.16739 0.12700 -0.00612 0.02932  0.00140  76  VAL B N   
2621 C CA  . VAL B 80  ? 0.17235 0.14987 0.10371 -0.00944 0.03681  -0.00084 76  VAL B CA  
2622 C C   . VAL B 80  ? 0.18072 0.15085 0.08880 -0.00709 0.03119  -0.00238 76  VAL B C   
2623 O O   . VAL B 80  ? 0.18988 0.16016 0.08905 -0.00958 0.03462  -0.00715 76  VAL B O   
2624 C CB  . VAL B 80  ? 0.16360 0.13447 0.09714 -0.01392 0.04853  0.00374  76  VAL B CB  
2625 C CG1 . VAL B 80  ? 0.14472 0.12666 0.10131 -0.01410 0.05256  0.00463  76  VAL B CG1 
2626 C CG2 . VAL B 80  ? 0.22768 0.18444 0.14846 -0.01461 0.04899  0.00926  76  VAL B CG2 
2627 N N   . THR B 81  ? 0.23694 0.20005 0.13337 -0.00156 0.02273  0.00135  77  THR B N   
2628 C CA  . THR B 81  ? 0.21655 0.17142 0.08713 0.00355  0.01658  0.00122  77  THR B CA  
2629 C C   . THR B 81  ? 0.21404 0.18584 0.08614 0.00772  0.00548  -0.00799 77  THR B C   
2630 O O   . THR B 81  ? 0.23410 0.20498 0.08645 0.01087  0.00062  -0.01117 77  THR B O   
2631 C CB  . THR B 81  ? 0.23413 0.17247 0.08898 0.00999  0.01272  0.00920  77  THR B CB  
2632 O OG1 . THR B 81  ? 0.27849 0.22583 0.14736 0.01486  0.00399  0.00853  77  THR B OG1 
2633 C CG2 . THR B 81  ? 0.23949 0.16145 0.09357 0.00372  0.02555  0.01595  77  THR B CG2 
2634 N N   . ASN B 82  ? 0.19194 0.17966 0.08660 0.00761  0.00171  -0.01328 78  ASN B N   
2635 C CA  . ASN B 82  ? 0.19589 0.20223 0.09684 0.00935  -0.00645 -0.02458 78  ASN B CA  
2636 C C   . ASN B 82  ? 0.19703 0.21558 0.12156 0.00236  0.00056  -0.03234 78  ASN B C   
2637 O O   . ASN B 82  ? 0.18192 0.21643 0.11582 0.00188  -0.00386 -0.04347 78  ASN B O   
2638 C CB  . ASN B 82  ? 0.19152 0.20408 0.09232 0.01948  -0.02010 -0.02464 78  ASN B CB  
2639 C CG  . ASN B 82  ? 0.28884 0.29726 0.20394 0.02066  -0.01914 -0.01869 78  ASN B CG  
2640 O OD1 . ASN B 82  ? 0.21734 0.22293 0.14519 0.01406  -0.00995 -0.01629 78  ASN B OD1 
2641 N ND2 . ASN B 82  ? 0.36686 0.37520 0.27914 0.02993  -0.02881 -0.01657 78  ASN B ND2 
2642 N N   . ALA B 83  ? 0.19454 0.20599 0.12845 -0.00249 0.01182  -0.02726 79  ALA B N   
2643 C CA  . ALA B 83  ? 0.17450 0.19168 0.12570 -0.00743 0.02095  -0.03236 79  ALA B CA  
2644 C C   . ALA B 83  ? 0.25434 0.28087 0.22089 -0.00505 0.01612  -0.03648 79  ALA B C   
2645 O O   . ALA B 83  ? 0.30879 0.33925 0.28680 -0.00872 0.02361  -0.04289 79  ALA B O   
2646 C CB  . ALA B 83  ? 0.23128 0.25256 0.17988 -0.01370 0.02813  -0.04268 79  ALA B CB  
2647 N N   . TYR B 84  ? 0.22020 0.24777 0.18615 0.00102  0.00556  -0.03286 80  TYR B N   
2648 C CA  . TYR B 84  ? 0.22818 0.26431 0.20814 0.00333  0.00126  -0.03752 80  TYR B CA  
2649 C C   . TYR B 84  ? 0.15728 0.18600 0.14443 0.00427  0.00412  -0.02966 80  TYR B C   
2650 O O   . TYR B 84  ? 0.12981 0.14926 0.11119 0.00476  0.00512  -0.02057 80  TYR B O   
2651 C CB  . TYR B 84  ? 0.24385 0.28725 0.21976 0.01065  -0.01218 -0.03987 80  TYR B CB  
2652 C CG  . TYR B 84  ? 0.21273 0.27222 0.20485 0.01137  -0.01582 -0.05130 80  TYR B CG  
2653 C CD1 . TYR B 84  ? 0.26132 0.33679 0.25893 0.00776  -0.01611 -0.06508 80  TYR B CD1 
2654 C CD2 . TYR B 84  ? 0.24610 0.30528 0.24867 0.01475  -0.01805 -0.04965 80  TYR B CD2 
2655 C CE1 . TYR B 84  ? 0.24101 0.33314 0.25634 0.00727  -0.01814 -0.07749 80  TYR B CE1 
2656 C CE2 . TYR B 84  ? 0.19944 0.27300 0.21796 0.01498  -0.01983 -0.06080 80  TYR B CE2 
2657 C CZ  . TYR B 84  ? 0.18836 0.27907 0.21432 0.01115  -0.01970 -0.07496 80  TYR B CZ  
2658 O OH  . TYR B 84  ? 0.26806 0.37492 0.31279 0.01023  -0.02014 -0.08793 80  TYR B OH  
2659 N N   . VAL B 85  ? 0.16450 0.19787 0.16422 0.00396  0.00593  -0.03447 81  VAL B N   
2660 C CA  . VAL B 85  ? 0.10583 0.13339 0.11098 0.00525  0.00777  -0.02859 81  VAL B CA  
2661 C C   . VAL B 85  ? 0.14675 0.17194 0.14951 0.00987  -0.00175 -0.02415 81  VAL B C   
2662 O O   . VAL B 85  ? 0.18584 0.21672 0.19000 0.01360  -0.00889 -0.02874 81  VAL B O   
2663 C CB  . VAL B 85  ? 0.10280 0.13255 0.11820 0.00371  0.01414  -0.03535 81  VAL B CB  
2664 C CG1 . VAL B 85  ? 0.08734 0.11067 0.10494 0.00605  0.01478  -0.02937 81  VAL B CG1 
2665 C CG2 . VAL B 85  ? 0.13544 0.16306 0.15091 -0.00078 0.02634  -0.03958 81  VAL B CG2 
2666 N N   . VAL B 86  ? 0.09981 0.11719 0.09975 0.00978  -0.00127 -0.01604 82  VAL B N   
2667 C CA  . VAL B 86  ? 0.13568 0.14724 0.13266 0.01278  -0.00736 -0.01209 82  VAL B CA  
2668 C C   . VAL B 86  ? 0.15417 0.16482 0.15895 0.01230  -0.00652 -0.01190 82  VAL B C   
2669 O O   . VAL B 86  ? 0.12320 0.12890 0.12682 0.01440  -0.01066 -0.01064 82  VAL B O   
2670 C CB  . VAL B 86  ? 0.20795 0.20963 0.19428 0.01152  -0.00661 -0.00480 82  VAL B CB  
2671 C CG1 . VAL B 86  ? 0.17959 0.17894 0.15344 0.01301  -0.00761 -0.00454 82  VAL B CG1 
2672 C CG2 . VAL B 86  ? 0.11925 0.12167 0.11082 0.00656  0.00000  -0.00171 82  VAL B CG2 
2673 N N   . GLY B 87  ? 0.07778 0.09125 0.08824 0.01037  -0.00081 -0.01299 83  GLY B N   
2674 C CA  . GLY B 87  ? 0.10249 0.11422 0.11659 0.01072  -0.00029 -0.01258 83  GLY B CA  
2675 C C   . GLY B 87  ? 0.09221 0.10524 0.10771 0.01080  0.00649  -0.01176 83  GLY B C   
2676 O O   . GLY B 87  ? 0.10660 0.12107 0.12147 0.01025  0.01177  -0.01165 83  GLY B O   
2677 N N   . TYR B 88  ? 0.07097 0.08212 0.08648 0.01235  0.00668  -0.01102 84  TYR B N   
2678 C CA  . TYR B 88  ? 0.07274 0.08333 0.08616 0.01537  0.01267  -0.00899 84  TYR B CA  
2679 C C   . TYR B 88  ? 0.08230 0.09380 0.09337 0.01764  0.00889  -0.00662 84  TYR B C   
2680 O O   . TYR B 88  ? 0.07733 0.08747 0.08844 0.01565  0.00369  -0.00823 84  TYR B O   
2681 C CB  . TYR B 88  ? 0.07629 0.08017 0.08792 0.01654  0.02137  -0.01354 84  TYR B CB  
2682 C CG  . TYR B 88  ? 0.14616 0.14323 0.15562 0.01757  0.02264  -0.01696 84  TYR B CG  
2683 C CD1 . TYR B 88  ? 0.07727 0.07518 0.09206 0.01505  0.01907  -0.02242 84  TYR B CD1 
2684 C CD2 . TYR B 88  ? 0.15796 0.14674 0.15872 0.02215  0.02812  -0.01467 84  TYR B CD2 
2685 C CE1 . TYR B 88  ? 0.11207 0.10309 0.12565 0.01553  0.02180  -0.02619 84  TYR B CE1 
2686 C CE2 . TYR B 88  ? 0.12521 0.10499 0.12143 0.02274  0.03083  -0.01794 84  TYR B CE2 
2687 C CZ  . TYR B 88  ? 0.11157 0.09261 0.11523 0.01866  0.02820  -0.02407 84  TYR B CZ  
2688 O OH  . TYR B 88  ? 0.14654 0.11812 0.14652 0.01880  0.03231  -0.02790 84  TYR B OH  
2689 N N   . ARG B 89  ? 0.09361 0.10758 0.10186 0.02257  0.01168  -0.00312 85  ARG B N   
2690 C CA  . ARG B 89  ? 0.08409 0.10180 0.08855 0.02654  0.00730  -0.00143 85  ARG B CA  
2691 C C   . ARG B 89  ? 0.09796 0.10526 0.09106 0.03412  0.01396  -0.00020 85  ARG B C   
2692 O O   . ARG B 89  ? 0.09990 0.10146 0.08966 0.03823  0.02264  0.00186  85  ARG B O   
2693 C CB  . ARG B 89  ? 0.08276 0.11534 0.09340 0.02806  0.00335  0.00153  85  ARG B CB  
2694 C CG  . ARG B 89  ? 0.15678 0.19803 0.16399 0.03357  -0.00264 0.00198  85  ARG B CG  
2695 C CD  . ARG B 89  ? 0.20000 0.26103 0.21764 0.03524  -0.00671 0.00295  85  ARG B CD  
2696 N NE  . ARG B 89  ? 0.46056 0.53100 0.47288 0.04589  -0.01098 0.00457  85  ARG B NE  
2697 C CZ  . ARG B 89  ? 0.55251 0.63816 0.56730 0.04549  -0.02047 0.00066  85  ARG B CZ  
2698 N NH1 . ARG B 89  ? 0.54844 0.64004 0.57175 0.03363  -0.02491 -0.00538 85  ARG B NH1 
2699 N NH2 . ARG B 89  ? 0.52452 0.61899 0.53172 0.05765  -0.02519 0.00248  85  ARG B NH2 
2700 N N   . ALA B 90  ? 0.11297 0.11523 0.09809 0.03588  0.01131  -0.00151 86  ALA B N   
2701 C CA  . ALA B 90  ? 0.15243 0.14191 0.12198 0.04418  0.01769  0.00045  86  ALA B CA  
2702 C C   . ALA B 90  ? 0.15761 0.15358 0.11937 0.04864  0.00865  0.00152  86  ALA B C   
2703 O O   . ALA B 90  ? 0.15864 0.15507 0.12101 0.04296  0.00318  -0.00259 86  ALA B O   
2704 C CB  . ALA B 90  ? 0.20084 0.17303 0.16546 0.04089  0.02662  -0.00432 86  ALA B CB  
2705 N N   . GLY B 91  ? 0.23305 0.23476 0.18739 0.05926  0.00698  0.00648  87  GLY B N   
2706 C CA  . GLY B 91  ? 0.28567 0.29689 0.23176 0.06465  -0.00305 0.00635  87  GLY B CA  
2707 C C   . GLY B 91  ? 0.22206 0.25394 0.18430 0.05476  -0.01441 0.00101  87  GLY B C   
2708 O O   . GLY B 91  ? 0.25549 0.30253 0.23418 0.05063  -0.01681 0.00073  87  GLY B O   
2709 N N   . ASN B 92  ? 0.20374 0.23384 0.16035 0.05003  -0.01960 -0.00384 88  ASN B N   
2710 C CA  . ASN B 92  ? 0.19007 0.23613 0.15915 0.03975  -0.02830 -0.01015 88  ASN B CA  
2711 C C   . ASN B 92  ? 0.18990 0.22589 0.16776 0.02769  -0.02459 -0.01340 88  ASN B C   
2712 O O   . ASN B 92  ? 0.15034 0.19097 0.13320 0.01887  -0.02888 -0.01890 88  ASN B O   
2713 C CB  . ASN B 92  ? 0.18390 0.23423 0.14079 0.04117  -0.03599 -0.01466 88  ASN B CB  
2714 C CG  . ASN B 92  ? 0.24962 0.32083 0.20300 0.05225  -0.04474 -0.01365 88  ASN B CG  
2715 O OD1 . ASN B 92  ? 0.31512 0.40729 0.28450 0.05329  -0.04830 -0.01347 88  ASN B OD1 
2716 N ND2 . ASN B 92  ? 0.30077 0.36668 0.23257 0.06139  -0.04827 -0.01326 88  ASN B ND2 
2717 N N   . SER B 93  ? 0.16439 0.18701 0.14378 0.02751  -0.01655 -0.01072 89  SER B N   
2718 C CA  . SER B 93  ? 0.10591 0.12062 0.09267 0.01905  -0.01433 -0.01338 89  SER B CA  
2719 C C   . SER B 93  ? 0.16565 0.18109 0.16142 0.01829  -0.01029 -0.01060 89  SER B C   
2720 O O   . SER B 93  ? 0.16340 0.17734 0.15711 0.02388  -0.00529 -0.00746 89  SER B O   
2721 C CB  . SER B 93  ? 0.11266 0.10997 0.09131 0.01913  -0.00931 -0.01584 89  SER B CB  
2722 O OG  . SER B 93  ? 0.16984 0.16395 0.13790 0.01898  -0.01233 -0.01886 89  SER B OG  
2723 N N   . ALA B 94  ? 0.10780 0.12352 0.11130 0.01161  -0.01162 -0.01185 90  ALA B N   
2724 C CA  . ALA B 94  ? 0.08598 0.10003 0.09472 0.01077  -0.00845 -0.00996 90  ALA B CA  
2725 C C   . ALA B 94  ? 0.11515 0.11915 0.12411 0.00856  -0.00809 -0.01233 90  ALA B C   
2726 O O   . ALA B 94  ? 0.12280 0.12207 0.13057 0.00528  -0.01042 -0.01432 90  ALA B O   
2727 C CB  . ALA B 94  ? 0.09697 0.12017 0.11236 0.00695  -0.00987 -0.00817 90  ALA B CB  
2728 N N   . TYR B 95  ? 0.07945 0.08105 0.09027 0.01069  -0.00495 -0.01283 91  TYR B N   
2729 C CA  . TYR B 95  ? 0.08286 0.07921 0.09584 0.01100  -0.00557 -0.01577 91  TYR B CA  
2730 C C   . TYR B 95  ? 0.13337 0.13267 0.14806 0.01126  -0.00682 -0.01423 91  TYR B C   
2731 O O   . TYR B 95  ? 0.12423 0.12840 0.13965 0.01141  -0.00413 -0.01329 91  TYR B O   
2732 C CB  . TYR B 95  ? 0.08007 0.07365 0.09477 0.01330  -0.00077 -0.02066 91  TYR B CB  
2733 C CG  . TYR B 95  ? 0.12962 0.11673 0.13849 0.01373  0.00175  -0.02187 91  TYR B CG  
2734 C CD1 . TYR B 95  ? 0.16281 0.14925 0.16466 0.01600  0.00511  -0.01952 91  TYR B CD1 
2735 C CD2 . TYR B 95  ? 0.14946 0.12983 0.15780 0.01294  0.00104  -0.02505 91  TYR B CD2 
2736 C CE1 . TYR B 95  ? 0.13483 0.11392 0.12720 0.01772  0.00689  -0.02023 91  TYR B CE1 
2737 C CE2 . TYR B 95  ? 0.14641 0.11937 0.14673 0.01307  0.00368  -0.02649 91  TYR B CE2 
2738 C CZ  . TYR B 95  ? 0.18805 0.16035 0.17937 0.01556  0.00616  -0.02402 91  TYR B CZ  
2739 O OH  . TYR B 95  ? 0.27509 0.23857 0.25444 0.01694  0.00832  -0.02511 91  TYR B OH  
2740 N N   . PHE B 96  ? 0.08372 0.07834 0.09694 0.01210  -0.01028 -0.01382 92  PHE B N   
2741 C CA  . PHE B 96  ? 0.08739 0.08233 0.09752 0.01376  -0.01223 -0.01165 92  PHE B CA  
2742 C C   . PHE B 96  ? 0.11144 0.10627 0.12275 0.01951  -0.01594 -0.01482 92  PHE B C   
2743 O O   . PHE B 96  ? 0.12609 0.11576 0.13872 0.02184  -0.01713 -0.01631 92  PHE B O   
2744 C CB  . PHE B 96  ? 0.13435 0.12146 0.13740 0.01087  -0.01228 -0.00656 92  PHE B CB  
2745 C CG  . PHE B 96  ? 0.13089 0.12294 0.13626 0.00538  -0.00935 -0.00493 92  PHE B CG  
2746 C CD1 . PHE B 96  ? 0.14368 0.14025 0.14873 0.00406  -0.00686 -0.00263 92  PHE B CD1 
2747 C CD2 . PHE B 96  ? 0.15555 0.14929 0.16385 0.00199  -0.00932 -0.00648 92  PHE B CD2 
2748 C CE1 . PHE B 96  ? 0.18018 0.18408 0.19010 0.00024  -0.00427 -0.00173 92  PHE B CE1 
2749 C CE2 . PHE B 96  ? 0.14597 0.14883 0.15845 -0.00168 -0.00818 -0.00611 92  PHE B CE2 
2750 C CZ  . PHE B 96  ? 0.18161 0.19022 0.19609 -0.00213 -0.00559 -0.00366 92  PHE B CZ  
2751 N N   . PHE B 97  ? 0.12531 0.12704 0.13639 0.02220  -0.01794 -0.01651 93  PHE B N   
2752 C CA  . PHE B 97  ? 0.09896 0.10425 0.11084 0.02944  -0.02368 -0.01966 93  PHE B CA  
2753 C C   . PHE B 97  ? 0.11939 0.11096 0.11889 0.03436  -0.02681 -0.01286 93  PHE B C   
2754 O O   . PHE B 97  ? 0.15431 0.13495 0.14395 0.03063  -0.02383 -0.00662 93  PHE B O   
2755 C CB  . PHE B 97  ? 0.09881 0.11611 0.11127 0.03086  -0.02608 -0.02386 93  PHE B CB  
2756 C CG  . PHE B 97  ? 0.14896 0.17751 0.17323 0.02586  -0.02077 -0.03219 93  PHE B CG  
2757 C CD1 . PHE B 97  ? 0.09461 0.12878 0.13150 0.02581  -0.01853 -0.03995 93  PHE B CD1 
2758 C CD2 . PHE B 97  ? 0.12506 0.15628 0.14693 0.02102  -0.01612 -0.03263 93  PHE B CD2 
2759 C CE1 . PHE B 97  ? 0.18962 0.23019 0.23536 0.02051  -0.01080 -0.04802 93  PHE B CE1 
2760 C CE2 . PHE B 97  ? 0.17446 0.21195 0.20501 0.01635  -0.00872 -0.04030 93  PHE B CE2 
2761 C CZ  . PHE B 97  ? 0.17690 0.21826 0.21882 0.01586  -0.00561 -0.04804 93  PHE B CZ  
2762 N N   . HIS B 98  ? 0.14561 0.13701 0.14581 0.04301  -0.03158 -0.01448 94  HIS B N   
2763 C CA  . HIS B 98  ? 0.17409 0.14833 0.15968 0.04968  -0.03294 -0.00739 94  HIS B CA  
2764 C C   . HIS B 98  ? 0.24182 0.21055 0.21092 0.05253  -0.03469 -0.00184 94  HIS B C   
2765 O O   . HIS B 98  ? 0.15791 0.13986 0.12700 0.05771  -0.04072 -0.00521 94  HIS B O   
2766 C CB  . HIS B 98  ? 0.15214 0.12880 0.14172 0.06134  -0.03818 -0.01007 94  HIS B CB  
2767 C CG  . HIS B 98  ? 0.26547 0.22017 0.23794 0.06989  -0.03767 -0.00201 94  HIS B CG  
2768 N ND1 . HIS B 98  ? 0.34692 0.29638 0.30340 0.08215  -0.04315 0.00297  94  HIS B ND1 
2769 C CD2 . HIS B 98  ? 0.34431 0.27868 0.31098 0.06817  -0.03117 0.00180  94  HIS B CD2 
2770 C CE1 . HIS B 98  ? 0.35592 0.28036 0.29648 0.08843  -0.03903 0.01047  94  HIS B CE1 
2771 N NE2 . HIS B 98  ? 0.34845 0.26354 0.29587 0.07924  -0.03125 0.00933  94  HIS B NE2 
2772 N N   . PRO B 99  ? 0.27777 0.22757 0.23256 0.04850  -0.02883 0.00545  95  PRO B N   
2773 C CA  . PRO B 99  ? 0.27255 0.21393 0.20933 0.05072  -0.02848 0.01078  95  PRO B CA  
2774 C C   . PRO B 99  ? 0.36824 0.30073 0.28809 0.06596  -0.03468 0.01468  95  PRO B C   
2775 O O   . PRO B 99  ? 0.30550 0.22663 0.22169 0.07369  -0.03499 0.01708  95  PRO B O   
2776 C CB  . PRO B 99  ? 0.30096 0.22333 0.22951 0.04132  -0.01823 0.01601  95  PRO B CB  
2777 C CG  . PRO B 99  ? 0.28162 0.19815 0.21831 0.03823  -0.01517 0.01446  95  PRO B CG  
2778 C CD  . PRO B 99  ? 0.22044 0.15722 0.17591 0.03985  -0.02115 0.00746  95  PRO B CD  
2779 N N   . ASP B 100 ? 0.35930 0.29684 0.26755 0.07115  -0.03965 0.01522  96  ASP B N   
2780 C CA  . ASP B 100 ? 0.44849 0.38116 0.33863 0.08806  -0.04790 0.01855  96  ASP B CA  
2781 C C   . ASP B 100 ? 0.49262 0.39054 0.35381 0.09391  -0.04083 0.02998  96  ASP B C   
2782 O O   . ASP B 100 ? 0.51711 0.41034 0.36867 0.10482  -0.04323 0.03190  96  ASP B O   
2783 C CB  . ASP B 100 ? 0.55415 0.50302 0.43817 0.09110  -0.05549 0.01465  96  ASP B CB  
2784 C CG  . ASP B 100 ? 0.67782 0.65756 0.58877 0.08250  -0.05869 0.00246  96  ASP B CG  
2785 O OD1 . ASP B 100 ? 0.76205 0.75639 0.69476 0.08260  -0.06104 -0.00426 96  ASP B OD1 
2786 O OD2 . ASP B 100 ? 0.81520 0.80237 0.72444 0.07533  -0.05718 -0.00061 96  ASP B OD2 
2787 N N   . ASN B 101 ? 0.38540 0.26462 0.24009 0.08140  -0.02838 0.03416  97  ASN B N   
2788 C CA  . ASN B 101 ? 0.42950 0.27453 0.25635 0.08384  -0.01820 0.04334  97  ASN B CA  
2789 C C   . ASN B 101 ? 0.36084 0.19225 0.19326 0.06681  -0.00399 0.04372  97  ASN B C   
2790 O O   . ASN B 101 ? 0.35888 0.21086 0.21673 0.05445  -0.00385 0.03693  97  ASN B O   
2791 C CB  . ASN B 101 ? 0.45312 0.29467 0.25969 0.08778  -0.01895 0.04573  97  ASN B CB  
2792 C CG  . ASN B 101 ? 0.51072 0.36761 0.32226 0.07961  -0.02124 0.04253  97  ASN B CG  
2793 O OD1 . ASN B 101 ? 0.52354 0.38270 0.34939 0.06396  -0.01213 0.04018  97  ASN B OD1 
2794 N ND2 . ASN B 101 ? 0.58362 0.45994 0.39400 0.08608  -0.03168 0.03812  97  ASN B ND2 
2795 N N   . GLN B 102 ? 0.44497 0.24493 0.25599 0.06522  0.00872  0.04981  98  GLN B N   
2796 C CA  . GLN B 102 ? 0.38969 0.17599 0.20766 0.04984  0.02256  0.04838  98  GLN B CA  
2797 C C   . GLN B 102 ? 0.39904 0.19457 0.22690 0.03375  0.02968  0.04477  98  GLN B C   
2798 O O   . GLN B 102 ? 0.34405 0.15020 0.19302 0.01963  0.03478  0.03865  98  GLN B O   
2799 C CB  . GLN B 102 ? 0.57172 0.32995 0.37204 0.05116  0.03494  0.05131  98  GLN B CB  
2800 C CG  . GLN B 102 ? 0.58603 0.33284 0.39577 0.03464  0.04931  0.04700  98  GLN B CG  
2801 C CD  . GLN B 102 ? 0.66854 0.42843 0.50006 0.03089  0.04385  0.04213  98  GLN B CD  
2802 O OE1 . GLN B 102 ? 0.65660 0.41651 0.48857 0.04150  0.03813  0.04279  98  GLN B OE1 
2803 N NE2 . GLN B 102 ? 0.56377 0.34490 0.41877 0.01563  0.04416  0.03464  98  GLN B NE2 
2804 N N   . GLU B 103 ? 0.36212 0.15560 0.17567 0.03625  0.02960  0.04785  99  GLU B N   
2805 C CA  . GLU B 103 ? 0.42008 0.22508 0.24536 0.02236  0.03596  0.04406  99  GLU B CA  
2806 C C   . GLU B 103 ? 0.34802 0.19034 0.20443 0.01770  0.02594  0.03662  99  GLU B C   
2807 O O   . GLU B 103 ? 0.32662 0.18231 0.20243 0.00531  0.03111  0.03188  99  GLU B O   
2808 C CB  . GLU B 103 ? 0.53010 0.32162 0.32993 0.02691  0.03888  0.04913  99  GLU B CB  
2809 C CG  . GLU B 103 ? 0.58550 0.38606 0.37276 0.04312  0.02363  0.05120  99  GLU B CG  
2810 C CD  . GLU B 103 ? 0.64491 0.43375 0.41872 0.05775  0.01882  0.05414  99  GLU B CD  
2811 O OE1 . GLU B 103 ? 0.82286 0.59670 0.57450 0.06553  0.02094  0.05719  99  GLU B OE1 
2812 O OE2 . GLU B 103 ? 0.80904 0.60311 0.59481 0.06139  0.01396  0.05304  99  GLU B OE2 
2813 N N   . ASP B 104 ? 0.28667 0.14597 0.14800 0.02797  0.01231  0.03506  100 ASP B N   
2814 C CA  . ASP B 104 ? 0.31421 0.20399 0.20282 0.02381  0.00519  0.02797  100 ASP B CA  
2815 C C   . ASP B 104 ? 0.28574 0.18133 0.19304 0.01748  0.00654  0.02428  100 ASP B C   
2816 O O   . ASP B 104 ? 0.22217 0.13632 0.14937 0.00976  0.00656  0.01952  100 ASP B O   
2817 C CB  . ASP B 104 ? 0.27804 0.18344 0.16832 0.03488  -0.00757 0.02529  100 ASP B CB  
2818 C CG  . ASP B 104 ? 0.55138 0.46154 0.43022 0.03781  -0.01032 0.02514  100 ASP B CG  
2819 O OD1 . ASP B 104 ? 0.55469 0.45574 0.42507 0.03104  -0.00173 0.02763  100 ASP B OD1 
2820 O OD2 . ASP B 104 ? 0.54432 0.46831 0.42339 0.04633  -0.02066 0.02143  100 ASP B OD2 
2821 N N   . ALA B 105 ? 0.23150 0.11059 0.13097 0.02164  0.00776  0.02644  101 ALA B N   
2822 C CA  . ALA B 105 ? 0.25239 0.13447 0.16671 0.01461  0.01008  0.02227  101 ALA B CA  
2823 C C   . ALA B 105 ? 0.33472 0.21627 0.25639 0.00012  0.02013  0.01957  101 ALA B C   
2824 O O   . ALA B 105 ? 0.30203 0.20123 0.24283 -0.00738 0.01881  0.01381  101 ALA B O   
2825 C CB  . ALA B 105 ? 0.32485 0.18503 0.22665 0.02155  0.01199  0.02523  101 ALA B CB  
2826 N N   . GLU B 106 ? 0.27371 0.13564 0.18003 -0.00358 0.03049  0.02308  102 GLU B N   
2827 C CA  . GLU B 106 ? 0.36992 0.23433 0.28607 -0.01809 0.04101  0.01878  102 GLU B CA  
2828 C C   . GLU B 106 ? 0.36359 0.25556 0.29794 -0.02188 0.03716  0.01556  102 GLU B C   
2829 O O   . GLU B 106 ? 0.31137 0.22080 0.26530 -0.03120 0.03904  0.00946  102 GLU B O   
2830 C CB  . GLU B 106 ? 0.35514 0.18924 0.24897 -0.02108 0.05524  0.02306  102 GLU B CB  
2831 C CG  . GLU B 106 ? 0.54361 0.37470 0.44729 -0.03769 0.06955  0.01656  102 GLU B CG  
2832 C CD  . GLU B 106 ? 0.60570 0.46129 0.52860 -0.04587 0.07084  0.01196  102 GLU B CD  
2833 O OE1 . GLU B 106 ? 0.61701 0.47442 0.53261 -0.04019 0.06863  0.01648  102 GLU B OE1 
2834 O OE2 . GLU B 106 ? 0.64603 0.52004 0.59153 -0.05753 0.07393  0.00326  102 GLU B OE2 
2835 N N   . ALA B 107 ? 0.26946 0.16616 0.19740 -0.01415 0.03176  0.01906  103 ALA B N   
2836 C CA  . ALA B 107 ? 0.32559 0.24326 0.26758 -0.01739 0.03101  0.01669  103 ALA B CA  
2837 C C   . ALA B 107 ? 0.23147 0.17441 0.19580 -0.01784 0.02353  0.01184  103 ALA B C   
2838 O O   . ALA B 107 ? 0.20636 0.16575 0.18676 -0.02353 0.02592  0.00847  103 ALA B O   
2839 C CB  . ALA B 107 ? 0.26771 0.18352 0.19637 -0.00959 0.02737  0.02024  103 ALA B CB  
2840 N N   . ILE B 108 ? 0.20272 0.14861 0.16773 -0.01110 0.01501  0.01136  104 ILE B N   
2841 C CA  . ILE B 108 ? 0.13449 0.10028 0.11620 -0.01055 0.00928  0.00739  104 ILE B CA  
2842 C C   . ILE B 108 ? 0.20630 0.17882 0.19949 -0.01747 0.01053  0.00322  104 ILE B C   
2843 O O   . ILE B 108 ? 0.16160 0.15035 0.16655 -0.01679 0.00641  0.00030  104 ILE B O   
2844 C CB  . ILE B 108 ? 0.16850 0.13516 0.14848 -0.00240 0.00163  0.00674  104 ILE B CB  
2845 C CG1 . ILE B 108 ? 0.20801 0.16007 0.18081 -0.00050 0.00073  0.00726  104 ILE B CG1 
2846 C CG2 . ILE B 108 ? 0.28650 0.25278 0.25814 0.00394  -0.00101 0.00823  104 ILE B CG2 
2847 C CD1 . ILE B 108 ? 0.19188 0.14712 0.16662 0.00740  -0.00611 0.00541  104 ILE B CD1 
2848 N N   . THR B 109 ? 0.20414 0.16385 0.19285 -0.02416 0.01675  0.00228  105 THR B N   
2849 C CA  . THR B 109 ? 0.20602 0.17580 0.20740 -0.03282 0.01834  -0.00410 105 THR B CA  
2850 C C   . THR B 109 ? 0.21631 0.20693 0.23333 -0.03798 0.02049  -0.00750 105 THR B C   
2851 O O   . THR B 109 ? 0.23864 0.24571 0.26929 -0.04336 0.01887  -0.01399 105 THR B O   
2852 C CB  . THR B 109 ? 0.26359 0.21299 0.25660 -0.04051 0.02698  -0.00598 105 THR B CB  
2853 O OG1 . THR B 109 ? 0.25979 0.19732 0.24613 -0.04546 0.03736  -0.00414 105 THR B OG1 
2854 C CG2 . THR B 109 ? 0.27156 0.19909 0.24840 -0.03307 0.02542  -0.00172 105 THR B CG2 
2855 N N   . HIS B 110 ? 0.16798 0.15933 0.18342 -0.03594 0.02386  -0.00387 106 HIS B N   
2856 C CA  . HIS B 110 ? 0.18526 0.19644 0.21633 -0.03894 0.02660  -0.00654 106 HIS B CA  
2857 C C   . HIS B 110 ? 0.20985 0.23897 0.24883 -0.03024 0.01943  -0.00517 106 HIS B C   
2858 O O   . HIS B 110 ? 0.16752 0.21309 0.21884 -0.02976 0.02136  -0.00630 106 HIS B O   
2859 C CB  . HIS B 110 ? 0.20339 0.20327 0.22737 -0.04169 0.03636  -0.00350 106 HIS B CB  
2860 C CG  . HIS B 110 ? 0.29230 0.27098 0.30618 -0.05039 0.04682  -0.00455 106 HIS B CG  
2861 N ND1 . HIS B 110 ? 0.34652 0.32977 0.37151 -0.06134 0.05755  -0.01029 106 HIS B ND1 
2862 C CD2 . HIS B 110 ? 0.31238 0.26358 0.30528 -0.04926 0.04963  -0.00072 106 HIS B CD2 
2863 C CE1 . HIS B 110 ? 0.38396 0.34067 0.39377 -0.06779 0.06804  -0.01004 106 HIS B CE1 
2864 N NE2 . HIS B 110 ? 0.37229 0.30827 0.36121 -0.05963 0.06319  -0.00348 106 HIS B NE2 
2865 N N   . LEU B 111 ? 0.12832 0.15326 0.16023 -0.02313 0.01272  -0.00298 107 LEU B N   
2866 C CA  . LEU B 111 ? 0.11110 0.14695 0.14667 -0.01504 0.00856  -0.00163 107 LEU B CA  
2867 C C   . LEU B 111 ? 0.14697 0.19378 0.18823 -0.01295 0.00221  -0.00486 107 LEU B C   
2868 O O   . LEU B 111 ? 0.13507 0.17523 0.17250 -0.01581 -0.00061 -0.00728 107 LEU B O   
2869 C CB  . LEU B 111 ? 0.12443 0.14816 0.14848 -0.00943 0.00723  0.00135  107 LEU B CB  
2870 C CG  . LEU B 111 ? 0.09314 0.10949 0.10988 -0.00906 0.01202  0.00412  107 LEU B CG  
2871 C CD1 . LEU B 111 ? 0.09452 0.10140 0.10076 -0.00467 0.00859  0.00449  107 LEU B CD1 
2872 C CD2 . LEU B 111 ? 0.13336 0.16046 0.15728 -0.00650 0.01605  0.00476  107 LEU B CD2 
2873 N N   . PHE B 112 ? 0.13614 0.19811 0.18446 -0.00702 0.00049  -0.00460 108 PHE B N   
2874 C CA  . PHE B 112 ? 0.15093 0.22255 0.20048 -0.00243 -0.00587 -0.00673 108 PHE B CA  
2875 C C   . PHE B 112 ? 0.17681 0.25551 0.23171 -0.01034 -0.00952 -0.01317 108 PHE B C   
2876 O O   . PHE B 112 ? 0.18220 0.25617 0.23107 -0.01073 -0.01368 -0.01556 108 PHE B O   
2877 C CB  . PHE B 112 ? 0.07516 0.13294 0.11279 0.00296  -0.00721 -0.00475 108 PHE B CB  
2878 C CG  . PHE B 112 ? 0.15729 0.20696 0.19004 0.00811  -0.00204 -0.00086 108 PHE B CG  
2879 C CD1 . PHE B 112 ? 0.09800 0.15477 0.13393 0.01374  0.00186  0.00188  108 PHE B CD1 
2880 C CD2 . PHE B 112 ? 0.07712 0.11298 0.10282 0.00736  -0.00070 -0.00096 108 PHE B CD2 
2881 C CE1 . PHE B 112 ? 0.12268 0.17040 0.15353 0.01687  0.00839  0.00408  108 PHE B CE1 
2882 C CE2 . PHE B 112 ? 0.10913 0.13982 0.13165 0.01036  0.00433  0.00014  108 PHE B CE2 
2883 C CZ  . PHE B 112 ? 0.07249 0.10789 0.09694 0.01429  0.00956  0.00246  108 PHE B CZ  
2884 N N   . THR B 113 ? 0.12962 0.21917 0.19629 -0.01782 -0.00648 -0.01710 109 THR B N   
2885 C CA  . THR B 113 ? 0.13823 0.23087 0.21001 -0.02872 -0.00658 -0.02491 109 THR B CA  
2886 C C   . THR B 113 ? 0.19754 0.31102 0.27574 -0.02737 -0.01519 -0.03152 109 THR B C   
2887 O O   . THR B 113 ? 0.22269 0.33649 0.30193 -0.03639 -0.01607 -0.03900 109 THR B O   
2888 C CB  . THR B 113 ? 0.18555 0.28370 0.26906 -0.03853 0.00142  -0.02891 109 THR B CB  
2889 O OG1 . THR B 113 ? 0.22668 0.35102 0.32654 -0.03444 -0.00015 -0.03080 109 THR B OG1 
2890 C CG2 . THR B 113 ? 0.22601 0.30024 0.29816 -0.03964 0.00999  -0.02225 109 THR B CG2 
2891 N N   . ASP B 114 ? 0.17228 0.30170 0.25279 -0.01589 -0.02108 -0.02907 110 ASP B N   
2892 C CA  . ASP B 114 ? 0.28479 0.43449 0.36778 -0.01173 -0.03070 -0.03458 110 ASP B CA  
2893 C C   . ASP B 114 ? 0.29606 0.43097 0.36027 -0.00434 -0.03501 -0.03102 110 ASP B C   
2894 O O   . ASP B 114 ? 0.26985 0.41773 0.33070 0.00023  -0.04314 -0.03487 110 ASP B O   
2895 C CB  . ASP B 114 ? 0.27676 0.45249 0.37107 -0.00089 -0.03478 -0.03368 110 ASP B CB  
2896 C CG  . ASP B 114 ? 0.30799 0.47103 0.39348 0.01155  -0.03034 -0.02264 110 ASP B CG  
2897 O OD1 . ASP B 114 ? 0.27981 0.41756 0.35444 0.00930  -0.02378 -0.01727 110 ASP B OD1 
2898 O OD2 . ASP B 114 ? 0.51554 0.69427 0.60493 0.02392  -0.03314 -0.01992 110 ASP B OD2 
2899 N N   . VAL B 115 ? 0.24064 0.34970 0.29250 -0.00304 -0.02966 -0.02462 111 VAL B N   
2900 C CA  . VAL B 115 ? 0.17839 0.27290 0.21412 0.00339  -0.03150 -0.02204 111 VAL B CA  
2901 C C   . VAL B 115 ? 0.14435 0.23516 0.17572 -0.00464 -0.03468 -0.02915 111 VAL B C   
2902 O O   . VAL B 115 ? 0.10415 0.19155 0.14141 -0.01612 -0.03182 -0.03392 111 VAL B O   
2903 C CB  . VAL B 115 ? 0.16547 0.23752 0.19346 0.00571  -0.02458 -0.01575 111 VAL B CB  
2904 C CG1 . VAL B 115 ? 0.16272 0.21977 0.19030 -0.00362 -0.02126 -0.01749 111 VAL B CG1 
2905 C CG2 . VAL B 115 ? 0.17189 0.23223 0.18578 0.01431  -0.02414 -0.01306 111 VAL B CG2 
2906 N N   . GLN B 116 ? 0.12878 0.21805 0.14781 0.00140  -0.03930 -0.03000 112 GLN B N   
2907 C CA  . GLN B 116 ? 0.12056 0.20762 0.13440 -0.00624 -0.04236 -0.03779 112 GLN B CA  
2908 C C   . GLN B 116 ? 0.12377 0.18498 0.13145 -0.01236 -0.03561 -0.03723 112 GLN B C   
2909 O O   . GLN B 116 ? 0.15931 0.21613 0.16795 -0.02264 -0.03440 -0.04382 112 GLN B O   
2910 C CB  . GLN B 116 ? 0.17928 0.27081 0.17845 0.00288  -0.04908 -0.03869 112 GLN B CB  
2911 C CG  . GLN B 116 ? 0.13806 0.26013 0.14374 0.00863  -0.05860 -0.04216 112 GLN B CG  
2912 C CD  . GLN B 116 ? 0.23403 0.35863 0.22034 0.02081  -0.06583 -0.04154 112 GLN B CD  
2913 O OE1 . GLN B 116 ? 0.26549 0.36671 0.23266 0.02392  -0.06216 -0.03857 112 GLN B OE1 
2914 N NE2 . GLN B 116 ? 0.35284 0.50049 0.34385 0.02746  -0.07311 -0.04299 112 GLN B NE2 
2915 N N   . ASN B 117 ? 0.13166 0.17630 0.13377 -0.00620 -0.03065 -0.03033 113 ASN B N   
2916 C CA  . ASN B 117 ? 0.11768 0.14115 0.11579 -0.00950 -0.02526 -0.03003 113 ASN B CA  
2917 C C   . ASN B 117 ? 0.16403 0.18094 0.16773 -0.00787 -0.02076 -0.02457 113 ASN B C   
2918 O O   . ASN B 117 ? 0.16317 0.18342 0.16764 -0.00122 -0.01973 -0.02009 113 ASN B O   
2919 C CB  . ASN B 117 ? 0.12898 0.13941 0.11463 -0.00383 -0.02365 -0.02971 113 ASN B CB  
2920 C CG  . ASN B 117 ? 0.21062 0.22721 0.18599 -0.00260 -0.02865 -0.03388 113 ASN B CG  
2921 O OD1 . ASN B 117 ? 0.18454 0.20170 0.15818 -0.01023 -0.03070 -0.04054 113 ASN B OD1 
2922 N ND2 . ASN B 117 ? 0.14587 0.16613 0.11250 0.00739  -0.03019 -0.03020 113 ASN B ND2 
2923 N N   . ARG B 118 ? 0.17629 0.18230 0.18178 -0.01334 -0.01757 -0.02509 114 ARG B N   
2924 C CA  . ARG B 118 ? 0.14268 0.14141 0.15021 -0.01094 -0.01442 -0.02034 114 ARG B CA  
2925 C C   . ARG B 118 ? 0.11768 0.10045 0.12078 -0.00832 -0.01229 -0.02039 114 ARG B C   
2926 O O   . ARG B 118 ? 0.20512 0.17785 0.20472 -0.01214 -0.01083 -0.02347 114 ARG B O   
2927 C CB  . ARG B 118 ? 0.22233 0.22101 0.23354 -0.01738 -0.01196 -0.01986 114 ARG B CB  
2928 C CG  . ARG B 118 ? 0.18689 0.20395 0.20628 -0.02164 -0.01343 -0.02225 114 ARG B CG  
2929 C CD  . ARG B 118 ? 0.17970 0.19357 0.20269 -0.02990 -0.00808 -0.02321 114 ARG B CD  
2930 N NE  . ARG B 118 ? 0.23122 0.23615 0.25088 -0.02617 -0.00460 -0.01680 114 ARG B NE  
2931 C CZ  . ARG B 118 ? 0.16094 0.17628 0.18543 -0.02304 -0.00447 -0.01375 114 ARG B CZ  
2932 N NH1 . ARG B 118 ? 0.21286 0.24775 0.24638 -0.02152 -0.00751 -0.01552 114 ARG B NH1 
2933 N NH2 . ARG B 118 ? 0.16931 0.17490 0.18827 -0.02047 -0.00119 -0.00884 114 ARG B NH2 
2934 N N   . TYR B 119 ? 0.10691 0.08835 0.11121 -0.00196 -0.01163 -0.01800 115 TYR B N   
2935 C CA  . TYR B 119 ? 0.12670 0.09804 0.13053 0.00200  -0.01037 -0.01907 115 TYR B CA  
2936 C C   . TYR B 119 ? 0.16522 0.13662 0.17088 0.00621  -0.01109 -0.01600 115 TYR B C   
2937 O O   . TYR B 119 ? 0.14584 0.12567 0.15363 0.00715  -0.01145 -0.01412 115 TYR B O   
2938 C CB  . TYR B 119 ? 0.11835 0.09028 0.12307 0.00560  -0.00855 -0.02225 115 TYR B CB  
2939 C CG  . TYR B 119 ? 0.12221 0.09181 0.12072 0.00309  -0.00792 -0.02501 115 TYR B CG  
2940 C CD1 . TYR B 119 ? 0.14798 0.10719 0.14270 0.00053  -0.00658 -0.02849 115 TYR B CD1 
2941 C CD2 . TYR B 119 ? 0.14296 0.11985 0.13751 0.00433  -0.00847 -0.02406 115 TYR B CD2 
2942 C CE1 . TYR B 119 ? 0.22654 0.18343 0.21306 -0.00196 -0.00636 -0.03173 115 TYR B CE1 
2943 C CE2 . TYR B 119 ? 0.17441 0.14937 0.15998 0.00373  -0.00908 -0.02644 115 TYR B CE2 
2944 C CZ  . TYR B 119 ? 0.23075 0.19608 0.21204 -0.00002 -0.00830 -0.03065 115 TYR B CZ  
2945 O OH  . TYR B 119 ? 0.24315 0.20630 0.21315 -0.00090 -0.00924 -0.03373 115 TYR B OH  
2946 N N   . THR B 120 ? 0.13136 0.09285 0.13483 0.00963  -0.01124 -0.01556 116 THR B N   
2947 C CA  . THR B 120 ? 0.14139 0.10344 0.14438 0.01617  -0.01357 -0.01324 116 THR B CA  
2948 C C   . THR B 120 ? 0.17249 0.13599 0.18154 0.02315  -0.01495 -0.01736 116 THR B C   
2949 O O   . THR B 120 ? 0.21082 0.16429 0.21864 0.02527  -0.01363 -0.01832 116 THR B O   
2950 C CB  . THR B 120 ? 0.22025 0.16880 0.21293 0.01674  -0.01260 -0.00818 116 THR B CB  
2951 O OG1 . THR B 120 ? 0.23422 0.18278 0.22427 0.00852  -0.00968 -0.00634 116 THR B OG1 
2952 C CG2 . THR B 120 ? 0.16990 0.11961 0.15829 0.02517  -0.01628 -0.00524 116 THR B CG2 
2953 N N   . PHE B 121 ? 0.14986 0.12629 0.16664 0.02613  -0.01656 -0.02088 117 PHE B N   
2954 C CA  . PHE B 121 ? 0.12298 0.10568 0.14929 0.03252  -0.01801 -0.02680 117 PHE B CA  
2955 C C   . PHE B 121 ? 0.20325 0.18160 0.22526 0.04190  -0.02307 -0.02383 117 PHE B C   
2956 O O   . PHE B 121 ? 0.19341 0.16453 0.20354 0.04363  -0.02512 -0.01724 117 PHE B O   
2957 C CB  . PHE B 121 ? 0.15835 0.15712 0.19412 0.03217  -0.01792 -0.03275 117 PHE B CB  
2958 C CG  . PHE B 121 ? 0.12066 0.12019 0.15861 0.02533  -0.01099 -0.03550 117 PHE B CG  
2959 C CD1 . PHE B 121 ? 0.22272 0.21498 0.26152 0.02309  -0.00578 -0.03823 117 PHE B CD1 
2960 C CD2 . PHE B 121 ? 0.19891 0.20428 0.23577 0.02209  -0.00880 -0.03508 117 PHE B CD2 
2961 C CE1 . PHE B 121 ? 0.19427 0.18414 0.23064 0.01888  0.00105  -0.03971 117 PHE B CE1 
2962 C CE2 . PHE B 121 ? 0.13703 0.14004 0.17304 0.01806  -0.00139 -0.03650 117 PHE B CE2 
2963 C CZ  . PHE B 121 ? 0.15595 0.15072 0.19066 0.01703  0.00334  -0.03846 117 PHE B CZ  
2964 N N   . ALA B 122 ? 0.21897 0.20078 0.24995 0.04892  -0.02427 -0.02872 118 ALA B N   
2965 C CA  . ALA B 122 ? 0.19359 0.17380 0.22111 0.06142  -0.03003 -0.02625 118 ALA B CA  
2966 C C   . ALA B 122 ? 0.17673 0.17682 0.20948 0.06804  -0.03782 -0.02994 118 ALA B C   
2967 O O   . ALA B 122 ? 0.22517 0.22504 0.25087 0.08016  -0.04452 -0.02669 118 ALA B O   
2968 C CB  . ALA B 122 ? 0.24287 0.22072 0.27965 0.06785  -0.02833 -0.03049 118 ALA B CB  
2969 N N   . PHE B 123 ? 0.21276 0.22893 0.25598 0.06082  -0.03666 -0.03690 119 PHE B N   
2970 C CA  . PHE B 123 ? 0.17707 0.21418 0.22688 0.06451  -0.04302 -0.04324 119 PHE B CA  
2971 C C   . PHE B 123 ? 0.17271 0.20785 0.21047 0.05848  -0.04274 -0.03869 119 PHE B C   
2972 O O   . PHE B 123 ? 0.14527 0.16905 0.17703 0.04944  -0.03616 -0.03387 119 PHE B O   
2973 C CB  . PHE B 123 ? 0.22439 0.28108 0.29657 0.05981  -0.03939 -0.05713 119 PHE B CB  
2974 C CG  . PHE B 123 ? 0.14815 0.19698 0.22235 0.04725  -0.02819 -0.05858 119 PHE B CG  
2975 C CD1 . PHE B 123 ? 0.13002 0.18152 0.20133 0.03929  -0.02413 -0.05943 119 PHE B CD1 
2976 C CD2 . PHE B 123 ? 0.19367 0.23121 0.27078 0.04456  -0.02136 -0.05898 119 PHE B CD2 
2977 C CE1 . PHE B 123 ? 0.18247 0.22508 0.25294 0.03056  -0.01380 -0.05968 119 PHE B CE1 
2978 C CE2 . PHE B 123 ? 0.11201 0.14113 0.18711 0.03523  -0.01175 -0.05966 119 PHE B CE2 
2979 C CZ  . PHE B 123 ? 0.19319 0.22470 0.26464 0.02907  -0.00814 -0.05957 119 PHE B CZ  
2980 N N   . GLY B 124 ? 0.23203 0.27950 0.26631 0.06425  -0.05027 -0.04078 120 GLY B N   
2981 C CA  . GLY B 124 ? 0.20825 0.25583 0.23249 0.05842  -0.04931 -0.03853 120 GLY B CA  
2982 C C   . GLY B 124 ? 0.19980 0.26417 0.23873 0.04923  -0.04459 -0.04969 120 GLY B C   
2983 O O   . GLY B 124 ? 0.21654 0.29405 0.27368 0.04762  -0.04243 -0.06033 120 GLY B O   
2984 N N   . GLY B 125 ? 0.17572 0.23777 0.20606 0.04286  -0.04125 -0.04757 121 GLY B N   
2985 C CA  . GLY B 125 ? 0.15946 0.23143 0.20010 0.03339  -0.03365 -0.05677 121 GLY B CA  
2986 C C   . GLY B 125 ? 0.19068 0.28340 0.23663 0.03363  -0.03831 -0.06846 121 GLY B C   
2987 O O   . GLY B 125 ? 0.16463 0.26120 0.21258 0.02504  -0.03108 -0.07440 121 GLY B O   
2988 N N   . ASN B 126 ? 0.15694 0.26356 0.20485 0.04384  -0.05019 -0.07247 122 ASN B N   
2989 C CA  . ASN B 126 ? 0.16275 0.29042 0.21562 0.04409  -0.05463 -0.08435 122 ASN B CA  
2990 C C   . ASN B 126 ? 0.12946 0.27171 0.20557 0.03703  -0.04654 -0.09948 122 ASN B C   
2991 O O   . ASN B 126 ? 0.09963 0.23849 0.18743 0.03618  -0.04197 -0.10113 122 ASN B O   
2992 C CB  . ASN B 126 ? 0.28283 0.41268 0.32442 0.05772  -0.06615 -0.07993 122 ASN B CB  
2993 C CG  . ASN B 126 ? 0.28618 0.41515 0.33612 0.06573  -0.06872 -0.07898 122 ASN B CG  
2994 O OD1 . ASN B 126 ? 0.23460 0.38008 0.29970 0.06696  -0.06959 -0.09001 122 ASN B OD1 
2995 N ND2 . ASN B 126 ? 0.38653 0.49562 0.42646 0.07073  -0.06907 -0.06639 122 ASN B ND2 
2996 N N   . TYR B 127 ? 0.23503 0.19951 0.19778 0.03183  -0.04461 0.03006  123 TYR B N   
2997 C CA  . TYR B 127 ? 0.24466 0.22088 0.22584 0.03522  -0.04499 0.01999  123 TYR B CA  
2998 C C   . TYR B 127 ? 0.20135 0.17796 0.20436 0.04019  -0.05397 0.01410  123 TYR B C   
2999 O O   . TYR B 127 ? 0.19674 0.18663 0.22074 0.04119  -0.04907 0.00644  123 TYR B O   
3000 C CB  . TYR B 127 ? 0.20972 0.18463 0.17955 0.03715  -0.04967 0.01820  123 TYR B CB  
3001 C CG  . TYR B 127 ? 0.20256 0.18146 0.15694 0.03472  -0.03924 0.01950  123 TYR B CG  
3002 C CD1 . TYR B 127 ? 0.24093 0.23090 0.20391 0.03176  -0.02725 0.01800  123 TYR B CD1 
3003 C CD2 . TYR B 127 ? 0.29235 0.26309 0.22236 0.03660  -0.04212 0.02151  123 TYR B CD2 
3004 C CE1 . TYR B 127 ? 0.27285 0.26664 0.22406 0.03131  -0.01903 0.01838  123 TYR B CE1 
3005 C CE2 . TYR B 127 ? 0.27964 0.25463 0.19656 0.03649  -0.03235 0.02103  123 TYR B CE2 
3006 C CZ  . TYR B 127 ? 0.21760 0.20458 0.14691 0.03414  -0.02114 0.01943  123 TYR B CZ  
3007 O OH  . TYR B 127 ? 0.26104 0.25230 0.17940 0.03574  -0.01271 0.01824  123 TYR B OH  
3008 N N   . ASP B 128 ? 0.18131 0.14359 0.17933 0.04383  -0.06705 0.01758  124 ASP B N   
3009 C CA  . ASP B 128 ? 0.24847 0.21157 0.26944 0.05085  -0.07724 0.01094  124 ASP B CA  
3010 C C   . ASP B 128 ? 0.23321 0.20292 0.27130 0.05171  -0.06934 0.00567  124 ASP B C   
3011 O O   . ASP B 128 ? 0.24343 0.22696 0.30616 0.05646  -0.06788 -0.00389 124 ASP B O   
3012 C CB  . ASP B 128 ? 0.26705 0.20977 0.27588 0.05394  -0.09240 0.01673  124 ASP B CB  
3013 C CG  . ASP B 128 ? 0.48469 0.42104 0.47512 0.05303  -0.09963 0.01961  124 ASP B CG  
3014 O OD1 . ASP B 128 ? 0.36450 0.31215 0.36060 0.05355  -0.09916 0.01437  124 ASP B OD1 
3015 O OD2 . ASP B 128 ? 0.56878 0.48777 0.53854 0.05154  -0.10605 0.02680  124 ASP B OD2 
3016 N N   . ARG B 129 ? 0.17632 0.13686 0.20166 0.04695  -0.06404 0.01149  125 ARG B N   
3017 C CA  . ARG B 129 ? 0.16477 0.12809 0.20218 0.04799  -0.05833 0.00570  125 ARG B CA  
3018 C C   . ARG B 129 ? 0.18154 0.16345 0.22561 0.04485  -0.04362 0.00021  125 ARG B C   
3019 O O   . ARG B 129 ? 0.14002 0.13149 0.19973 0.04874  -0.03882 -0.00881 125 ARG B O   
3020 C CB  . ARG B 129 ? 0.26303 0.20925 0.28575 0.04257  -0.05966 0.01385  125 ARG B CB  
3021 C CG  . ARG B 129 ? 0.44088 0.37739 0.47384 0.04724  -0.06438 0.00769  125 ARG B CG  
3022 C CD  . ARG B 129 ? 0.57847 0.49331 0.60973 0.05261  -0.08118 0.01095  125 ARG B CD  
3023 N NE  . ARG B 129 ? 0.77299 0.67187 0.78156 0.04452  -0.08593 0.02594  125 ARG B NE  
3024 C CZ  . ARG B 129 ? 0.47659 0.36203 0.47273 0.03534  -0.08502 0.03530  125 ARG B CZ  
3025 N NH1 . ARG B 129 ? 0.50271 0.38594 0.50616 0.03341  -0.08225 0.03069  125 ARG B NH1 
3026 N NH2 . ARG B 129 ? 0.60054 0.47497 0.57608 0.02737  -0.08673 0.04954  125 ARG B NH2 
3027 N N   . LEU B 130 ? 0.19071 0.17721 0.22180 0.03840  -0.03625 0.00548  126 LEU B N   
3028 C CA  . LEU B 130 ? 0.13110 0.13146 0.16586 0.03539  -0.02418 0.00158  126 LEU B CA  
3029 C C   . LEU B 130 ? 0.10526 0.11940 0.15715 0.03829  -0.02210 -0.00599 126 LEU B C   
3030 O O   . LEU B 130 ? 0.10600 0.13023 0.16644 0.03781  -0.01322 -0.01133 126 LEU B O   
3031 C CB  . LEU B 130 ? 0.12771 0.12937 0.14682 0.02989  -0.01874 0.00805  126 LEU B CB  
3032 C CG  . LEU B 130 ? 0.11573 0.11050 0.12256 0.02506  -0.01696 0.01571  126 LEU B CG  
3033 C CD1 . LEU B 130 ? 0.19355 0.19453 0.18926 0.02177  -0.01015 0.02006  126 LEU B CD1 
3034 C CD2 . LEU B 130 ? 0.15060 0.14514 0.16346 0.02357  -0.01401 0.01260  126 LEU B CD2 
3035 N N   . GLU B 131 ? 0.10958 0.12424 0.16615 0.04057  -0.03043 -0.00611 127 GLU B N   
3036 C CA  . GLU B 131 ? 0.16005 0.18946 0.23788 0.04199  -0.02986 -0.01287 127 GLU B CA  
3037 C C   . GLU B 131 ? 0.14515 0.18358 0.24518 0.04784  -0.02837 -0.02077 127 GLU B C   
3038 O O   . GLU B 131 ? 0.09481 0.14961 0.21095 0.04681  -0.01893 -0.02631 127 GLU B O   
3039 C CB  . GLU B 131 ? 0.12642 0.15275 0.20583 0.04377  -0.04277 -0.01204 127 GLU B CB  
3040 C CG  . GLU B 131 ? 0.12412 0.14584 0.18522 0.03894  -0.04246 -0.00800 127 GLU B CG  
3041 C CD  . GLU B 131 ? 0.22188 0.23469 0.27636 0.04169  -0.05759 -0.00710 127 GLU B CD  
3042 O OE1 . GLU B 131 ? 0.16992 0.17549 0.22661 0.04693  -0.06898 -0.00644 127 GLU B OE1 
3043 O OE2 . GLU B 131 ? 0.20369 0.21455 0.24923 0.03917  -0.05955 -0.00741 127 GLU B OE2 
3044 N N   . GLN B 132 ? 0.11425 0.14157 0.21480 0.05422  -0.03732 -0.02139 128 GLN B N   
3045 C CA  . GLN B 132 ? 0.11732 0.15161 0.23806 0.06217  -0.03628 -0.03061 128 GLN B CA  
3046 C C   . GLN B 132 ? 0.13723 0.17586 0.25312 0.06028  -0.02186 -0.03444 128 GLN B C   
3047 O O   . GLN B 132 ? 0.15430 0.20810 0.28574 0.06348  -0.01288 -0.04265 128 GLN B O   
3048 C CB  . GLN B 132 ? 0.18496 0.20025 0.30106 0.06827  -0.04991 -0.02941 128 GLN B CB  
3049 C CG  . GLN B 132 ? 0.29164 0.30142 0.40869 0.06933  -0.06375 -0.02620 128 GLN B CG  
3050 C CD  . GLN B 132 ? 0.35630 0.34431 0.46360 0.07305  -0.07660 -0.02335 128 GLN B CD  
3051 O OE1 . GLN B 132 ? 0.38882 0.36598 0.49142 0.07500  -0.07585 -0.02447 128 GLN B OE1 
3052 N NE2 . GLN B 132 ? 0.41360 0.39343 0.51661 0.07361  -0.08926 -0.01984 128 GLN B NE2 
3053 N N   . LEU B 133 ? 0.11904 0.14478 0.21198 0.05451  -0.01928 -0.02822 129 LEU B N   
3054 C CA  . LEU B 133 ? 0.15338 0.18063 0.23867 0.05265  -0.00828 -0.03170 129 LEU B CA  
3055 C C   . LEU B 133 ? 0.11583 0.15922 0.20278 0.04730  0.00466  -0.03235 129 LEU B C   
3056 O O   . LEU B 133 ? 0.15093 0.20200 0.23921 0.04839  0.01503  -0.03838 129 LEU B O   
3057 C CB  . LEU B 133 ? 0.14117 0.15221 0.20532 0.04711  -0.01090 -0.02443 129 LEU B CB  
3058 C CG  . LEU B 133 ? 0.27235 0.26399 0.33222 0.04979  -0.02290 -0.02228 129 LEU B CG  
3059 C CD1 . LEU B 133 ? 0.22215 0.20287 0.26483 0.04112  -0.02403 -0.01275 129 LEU B CD1 
3060 C CD2 . LEU B 133 ? 0.24548 0.23204 0.31197 0.05785  -0.02393 -0.03303 129 LEU B CD2 
3061 N N   . ALA B 134 ? 0.09219 0.13885 0.17684 0.04153  0.00393  -0.02616 130 ALA B N   
3062 C CA  . ALA B 134 ? 0.10933 0.16718 0.19457 0.03547  0.01419  -0.02545 130 ALA B CA  
3063 C C   . ALA B 134 ? 0.13181 0.20816 0.24160 0.03659  0.01909  -0.03125 130 ALA B C   
3064 O O   . ALA B 134 ? 0.14049 0.22672 0.25202 0.03098  0.03001  -0.03104 130 ALA B O   
3065 C CB  . ALA B 134 ? 0.09557 0.14818 0.17003 0.02992  0.01036  -0.01810 130 ALA B CB  
3066 N N   . GLY B 135 ? 0.14286 0.22445 0.27263 0.04336  0.01105  -0.03591 131 GLY B N   
3067 C CA  . GLY B 135 ? 0.08651 0.18768 0.24231 0.04332  0.01443  -0.04029 131 GLY B CA  
3068 C C   . GLY B 135 ? 0.11912 0.22772 0.28572 0.03618  0.01104  -0.03676 131 GLY B C   
3069 O O   . GLY B 135 ? 0.08149 0.20525 0.26415 0.03119  0.01719  -0.03753 131 GLY B O   
3070 N N   . ASN B 136 ? 0.09423 0.18653 0.24255 0.03369  0.00080  -0.03050 132 ASN B N   
3071 C CA  . ASN B 136 ? 0.12122 0.21407 0.27283 0.02735  -0.00512 -0.02748 132 ASN B CA  
3072 C C   . ASN B 136 ? 0.08473 0.15885 0.21634 0.02979  -0.01911 -0.02338 132 ASN B C   
3073 O O   . ASN B 136 ? 0.09483 0.15527 0.20377 0.03189  -0.01889 -0.01961 132 ASN B O   
3074 C CB  . ASN B 136 ? 0.16852 0.26073 0.30889 0.01792  0.00565  -0.02331 132 ASN B CB  
3075 C CG  . ASN B 136 ? 0.22445 0.33631 0.38865 0.01151  0.01598  -0.02536 132 ASN B CG  
3076 O OD1 . ASN B 136 ? 0.31268 0.43837 0.50444 0.01023  0.01072  -0.02838 132 ASN B OD1 
3077 N ND2 . ASN B 136 ? 0.29226 0.40587 0.44610 0.00692  0.03057  -0.02325 132 ASN B ND2 
3078 N N   . LEU B 137 ? 0.14751 0.22146 0.28723 0.02880  -0.03101 -0.02402 133 LEU B N   
3079 C CA  . LEU B 137 ? 0.17080 0.22657 0.28739 0.03054  -0.04338 -0.02048 133 LEU B CA  
3080 C C   . LEU B 137 ? 0.14969 0.19615 0.24426 0.02494  -0.03825 -0.01691 133 LEU B C   
3081 O O   . LEU B 137 ? 0.14276 0.19576 0.24409 0.01860  -0.02965 -0.01712 133 LEU B O   
3082 C CB  . LEU B 137 ? 0.13123 0.18833 0.26271 0.03239  -0.06027 -0.02377 133 LEU B CB  
3083 C CG  . LEU B 137 ? 0.23628 0.30294 0.39376 0.03956  -0.06961 -0.02826 133 LEU B CG  
3084 C CD1 . LEU B 137 ? 0.21077 0.27732 0.37949 0.03831  -0.08456 -0.03098 133 LEU B CD1 
3085 C CD2 . LEU B 137 ? 0.18860 0.23895 0.32639 0.04722  -0.07543 -0.02492 133 LEU B CD2 
3086 N N   . ARG B 138 ? 0.16070 0.19118 0.22813 0.02773  -0.04379 -0.01351 134 ARG B N   
3087 C CA  . ARG B 138 ? 0.14649 0.16788 0.19288 0.02517  -0.03994 -0.01157 134 ARG B CA  
3088 C C   . ARG B 138 ? 0.14297 0.16467 0.19876 0.02021  -0.04458 -0.01500 134 ARG B C   
3089 O O   . ARG B 138 ? 0.17279 0.19126 0.22213 0.01632  -0.03811 -0.01416 134 ARG B O   
3090 C CB  . ARG B 138 ? 0.14315 0.14987 0.16119 0.02995  -0.04588 -0.00875 134 ARG B CB  
3091 C CG  . ARG B 138 ? 0.14642 0.15090 0.15061 0.03184  -0.03832 -0.00314 134 ARG B CG  
3092 C CD  . ARG B 138 ? 0.20680 0.19843 0.18522 0.03562  -0.04459 0.00066  134 ARG B CD  
3093 N NE  . ARG B 138 ? 0.20096 0.18693 0.18251 0.03862  -0.05759 0.00110  134 ARG B NE  
3094 C CZ  . ARG B 138 ? 0.29480 0.26711 0.25390 0.04192  -0.06754 0.00365  134 ARG B CZ  
3095 N NH1 . ARG B 138 ? 0.22645 0.19079 0.15806 0.04299  -0.06462 0.00498  134 ARG B NH1 
3096 N NH2 . ARG B 138 ? 0.28523 0.25115 0.24829 0.04505  -0.08097 0.00458  134 ARG B NH2 
3097 N N   . GLU B 139 ? 0.12818 0.15258 0.20021 0.02001  -0.05734 -0.01874 135 GLU B N   
3098 C CA  . GLU B 139 ? 0.15436 0.17821 0.23804 0.01371  -0.06398 -0.02191 135 GLU B CA  
3099 C C   . GLU B 139 ? 0.16671 0.20599 0.27576 0.00488  -0.05269 -0.02117 135 GLU B C   
3100 O O   . GLU B 139 ? 0.13776 0.17581 0.25713 -0.00279 -0.05664 -0.02214 135 GLU B O   
3101 C CB  . GLU B 139 ? 0.18880 0.21313 0.28654 0.01533  -0.08235 -0.02624 135 GLU B CB  
3102 C CG  . GLU B 139 ? 0.31456 0.35529 0.43825 0.01874  -0.08363 -0.02729 135 GLU B CG  
3103 C CD  . GLU B 139 ? 0.62431 0.66035 0.75286 0.02382  -0.10457 -0.03065 135 GLU B CD  
3104 O OE1 . GLU B 139 ? 0.56607 0.61426 0.72520 0.02006  -0.11208 -0.03455 135 GLU B OE1 
3105 O OE2 . GLU B 139 ? 0.56739 0.58633 0.66676 0.03085  -0.11228 -0.02857 135 GLU B OE2 
3106 N N   . ASN B 140 ? 0.16370 0.21598 0.28146 0.00531  -0.03910 -0.01938 136 ASN B N   
3107 C CA  . ASN B 140 ? 0.16889 0.23469 0.30388 -0.00284 -0.02567 -0.01787 136 ASN B CA  
3108 C C   . ASN B 140 ? 0.20972 0.26921 0.32288 -0.00309 -0.01206 -0.01359 136 ASN B C   
3109 O O   . ASN B 140 ? 0.20906 0.27900 0.33031 -0.00760 0.00077  -0.01201 136 ASN B O   
3110 C CB  . ASN B 140 ? 0.09228 0.18128 0.25889 -0.00186 -0.02105 -0.02119 136 ASN B CB  
3111 C CG  . ASN B 140 ? 0.12290 0.22120 0.31707 -0.00176 -0.03589 -0.02570 136 ASN B CG  
3112 O OD1 . ASN B 140 ? 0.20518 0.30828 0.40900 0.00672  -0.04399 -0.02929 136 ASN B OD1 
3113 N ND2 . ASN B 140 ? 0.19680 0.29601 0.40400 -0.01132 -0.04137 -0.02543 136 ASN B ND2 
3114 N N   . ILE B 141 ? 0.13656 0.17997 0.22223 0.00185  -0.01468 -0.01183 137 ILE B N   
3115 C CA  . ILE B 141 ? 0.09471 0.13233 0.16133 0.00248  -0.00466 -0.00814 137 ILE B CA  
3116 C C   . ILE B 141 ? 0.17674 0.19821 0.22507 0.00187  -0.00888 -0.00682 137 ILE B C   
3117 O O   . ILE B 141 ? 0.12315 0.13494 0.15794 0.00744  -0.01700 -0.00863 137 ILE B O   
3118 C CB  . ILE B 141 ? 0.15885 0.19567 0.21397 0.00984  -0.00304 -0.00758 137 ILE B CB  
3119 C CG1 . ILE B 141 ? 0.17911 0.22891 0.25129 0.01142  0.00110  -0.00991 137 ILE B CG1 
3120 C CG2 . ILE B 141 ? 0.14028 0.17054 0.17666 0.01051  0.00386  -0.00411 137 ILE B CG2 
3121 C CD1 . ILE B 141 ? 0.11664 0.16269 0.18113 0.01815  -0.00186 -0.00965 137 ILE B CD1 
3122 N N   . GLU B 142 ? 0.15137 0.16865 0.19756 -0.00425 -0.00350 -0.00380 138 GLU B N   
3123 C CA  . GLU B 142 ? 0.12177 0.12156 0.15285 -0.00429 -0.00910 -0.00333 138 GLU B CA  
3124 C C   . GLU B 142 ? 0.12079 0.11357 0.13067 0.00441  -0.00741 -0.00295 138 GLU B C   
3125 O O   . GLU B 142 ? 0.13674 0.13666 0.14356 0.00663  0.00013  -0.00069 138 GLU B O   
3126 C CB  . GLU B 142 ? 0.13936 0.13418 0.17348 -0.01392 -0.00468 0.00125  138 GLU B CB  
3127 C CG  . GLU B 142 ? 0.21464 0.21974 0.27350 -0.02452 -0.00447 0.00183  138 GLU B CG  
3128 C CD  . GLU B 142 ? 0.41026 0.41513 0.47178 -0.03562 0.00504  0.00869  138 GLU B CD  
3129 O OE1 . GLU B 142 ? 0.43533 0.43389 0.47897 -0.03404 0.01210  0.01274  138 GLU B OE1 
3130 O OE2 . GLU B 142 ? 0.57155 0.58270 0.65309 -0.04652 0.00517  0.01052  138 GLU B OE2 
3131 N N   . LEU B 143 ? 0.13277 0.11209 0.12909 0.00957  -0.01483 -0.00590 139 LEU B N   
3132 C CA  . LEU B 143 ? 0.13478 0.10948 0.11404 0.01828  -0.01285 -0.00634 139 LEU B CA  
3133 C C   . LEU B 143 ? 0.14987 0.10834 0.12010 0.01923  -0.01651 -0.00682 139 LEU B C   
3134 O O   . LEU B 143 ? 0.16216 0.10917 0.13608 0.01318  -0.02281 -0.00725 139 LEU B O   
3135 C CB  . LEU B 143 ? 0.13994 0.11378 0.10826 0.02637  -0.01701 -0.01045 139 LEU B CB  
3136 C CG  . LEU B 143 ? 0.13989 0.12499 0.11496 0.02564  -0.01632 -0.00924 139 LEU B CG  
3137 C CD1 . LEU B 143 ? 0.14229 0.12276 0.10170 0.03255  -0.02141 -0.01199 139 LEU B CD1 
3138 C CD2 . LEU B 143 ? 0.11497 0.11201 0.09478 0.02486  -0.00676 -0.00457 139 LEU B CD2 
3139 N N   . GLY B 144 ? 0.15068 0.10797 0.11062 0.02682  -0.01351 -0.00668 140 GLY B N   
3140 C CA  . GLY B 144 ? 0.16632 0.10766 0.11775 0.03010  -0.01781 -0.00728 140 GLY B CA  
3141 C C   . GLY B 144 ? 0.18214 0.12894 0.13159 0.03357  -0.01248 -0.00351 140 GLY B C   
3142 O O   . GLY B 144 ? 0.14429 0.10704 0.09888 0.03266  -0.00552 -0.00085 140 GLY B O   
3143 N N   . ASN B 145 ? 0.17562 0.10781 0.11785 0.03781  -0.01745 -0.00350 141 ASN B N   
3144 C CA  . ASN B 145 ? 0.17257 0.10926 0.11376 0.04164  -0.01509 -0.00010 141 ASN B CA  
3145 C C   . ASN B 145 ? 0.17602 0.11556 0.11912 0.03105  -0.01064 0.00742  141 ASN B C   
3146 O O   . ASN B 145 ? 0.15753 0.10767 0.10182 0.03245  -0.00705 0.00969  141 ASN B O   
3147 C CB  . ASN B 145 ? 0.22671 0.14467 0.15980 0.04964  -0.02370 -0.00194 141 ASN B CB  
3148 C CG  . ASN B 145 ? 0.27289 0.19922 0.20779 0.05797  -0.02337 -0.00108 141 ASN B CG  
3149 O OD1 . ASN B 145 ? 0.24810 0.19383 0.19008 0.06514  -0.01828 -0.00447 141 ASN B OD1 
3150 N ND2 . ASN B 145 ? 0.25414 0.16568 0.18289 0.05652  -0.02943 0.00406  141 ASN B ND2 
3151 N N   . GLY B 146 ? 0.17674 0.10764 0.12032 0.02032  -0.01063 0.01097  142 GLY B N   
3152 C CA  . GLY B 146 ? 0.18284 0.11706 0.12623 0.01042  -0.00423 0.01751  142 GLY B CA  
3153 C C   . GLY B 146 ? 0.20940 0.16476 0.16168 0.00912  0.00415  0.01625  142 GLY B C   
3154 O O   . GLY B 146 ? 0.18970 0.15082 0.13818 0.00904  0.00812  0.01848  142 GLY B O   
3155 N N   . PRO B 147 ? 0.17724 0.14222 0.14055 0.00835  0.00530  0.01236  143 PRO B N   
3156 C CA  . PRO B 147 ? 0.12862 0.11085 0.10007 0.00899  0.01104  0.01070  143 PRO B CA  
3157 C C   . PRO B 147 ? 0.14596 0.13490 0.11395 0.01627  0.01146  0.00996  143 PRO B C   
3158 O O   . PRO B 147 ? 0.16298 0.16064 0.13340 0.01505  0.01562  0.01062  143 PRO B O   
3159 C CB  . PRO B 147 ? 0.14103 0.12721 0.12170 0.00938  0.00786  0.00661  143 PRO B CB  
3160 C CG  . PRO B 147 ? 0.14568 0.12030 0.12830 0.00323  0.00345  0.00727  143 PRO B CG  
3161 C CD  . PRO B 147 ? 0.17124 0.12969 0.14027 0.00517  0.00014  0.00991  143 PRO B CD  
3162 N N   . LEU B 148 ? 0.11922 0.10486 0.08284 0.02384  0.00726  0.00814  144 LEU B N   
3163 C CA  . LEU B 148 ? 0.14985 0.14578 0.11482 0.02959  0.00854  0.00797  144 LEU B CA  
3164 C C   . LEU B 148 ? 0.16072 0.15502 0.12233 0.02874  0.00771  0.01112  144 LEU B C   
3165 O O   . LEU B 148 ? 0.14931 0.15315 0.11480 0.02811  0.00947  0.01194  144 LEU B O   
3166 C CB  . LEU B 148 ? 0.12802 0.12405 0.09091 0.03874  0.00607  0.00449  144 LEU B CB  
3167 C CG  . LEU B 148 ? 0.12265 0.13460 0.09148 0.04363  0.00949  0.00466  144 LEU B CG  
3168 C CD1 . LEU B 148 ? 0.14001 0.16242 0.11371 0.03873  0.01403  0.00658  144 LEU B CD1 
3169 C CD2 . LEU B 148 ? 0.21370 0.22845 0.18054 0.05365  0.00964  0.00033  144 LEU B CD2 
3170 N N   . GLU B 149 ? 0.12988 0.10979 0.08286 0.02841  0.00351  0.01315  145 GLU B N   
3171 C CA  . GLU B 149 ? 0.13864 0.11292 0.08362 0.02712  0.00106  0.01685  145 GLU B CA  
3172 C C   . GLU B 149 ? 0.15743 0.13689 0.10051 0.02011  0.00680  0.01825  145 GLU B C   
3173 O O   . GLU B 149 ? 0.21388 0.19721 0.15491 0.02096  0.00526  0.01850  145 GLU B O   
3174 C CB  . GLU B 149 ? 0.15995 0.11353 0.09248 0.02537  -0.00404 0.02049  145 GLU B CB  
3175 C CG  . GLU B 149 ? 0.18297 0.12629 0.10080 0.02140  -0.00591 0.02598  145 GLU B CG  
3176 C CD  . GLU B 149 ? 0.27115 0.20938 0.18522 0.02988  -0.01600 0.02641  145 GLU B CD  
3177 O OE1 . GLU B 149 ? 0.24613 0.18572 0.16868 0.03888  -0.02111 0.02281  145 GLU B OE1 
3178 O OE2 . GLU B 149 ? 0.27394 0.20706 0.17654 0.02833  -0.01928 0.02969  145 GLU B OE2 
3179 N N   . GLU B 150 ? 0.18683 0.16671 0.13165 0.01366  0.01281  0.01830  146 GLU B N   
3180 C CA  . GLU B 150 ? 0.18087 0.16606 0.12419 0.00859  0.01945  0.01809  146 GLU B CA  
3181 C C   . GLU B 150 ? 0.14898 0.14715 0.10259 0.01131  0.02061  0.01413  146 GLU B C   
3182 O O   . GLU B 150 ? 0.14482 0.14483 0.09453 0.01036  0.02241  0.01280  146 GLU B O   
3183 C CB  . GLU B 150 ? 0.16985 0.15551 0.11733 0.00159  0.02600  0.01878  146 GLU B CB  
3184 C CG  . GLU B 150 ? 0.29430 0.26502 0.23119 -0.00396 0.02519  0.02447  146 GLU B CG  
3185 C CD  . GLU B 150 ? 0.35266 0.32461 0.30139 -0.01049 0.02768  0.02491  146 GLU B CD  
3186 O OE1 . GLU B 150 ? 0.34420 0.33022 0.30901 -0.01062 0.03091  0.02054  146 GLU B OE1 
3187 O OE2 . GLU B 150 ? 0.35755 0.31522 0.30020 -0.01567 0.02485  0.02976  146 GLU B OE2 
3188 N N   . ALA B 151 ? 0.13562 0.14056 0.10002 0.01455  0.01908  0.01231  147 ALA B N   
3189 C CA  . ALA B 151 ? 0.09800 0.11241 0.07060 0.01609  0.01933  0.01044  147 ALA B CA  
3190 C C   . ALA B 151 ? 0.13439 0.15124 0.10601 0.01809  0.01557  0.01144  147 ALA B C   
3191 O O   . ALA B 151 ? 0.09536 0.11537 0.06984 0.01668  0.01508  0.01042  147 ALA B O   
3192 C CB  . ALA B 151 ? 0.11009 0.12896 0.08964 0.01872  0.01847  0.00969  147 ALA B CB  
3193 N N   . ILE B 152 ? 0.10645 0.12155 0.07576 0.02163  0.01162  0.01298  148 ILE B N   
3194 C CA  . ILE B 152 ? 0.11897 0.13915 0.09187 0.02362  0.00669  0.01376  148 ILE B CA  
3195 C C   . ILE B 152 ? 0.14041 0.15339 0.10350 0.02049  0.00372  0.01352  148 ILE B C   
3196 O O   . ILE B 152 ? 0.10829 0.12543 0.07589 0.01903  0.00044  0.01260  148 ILE B O   
3197 C CB  . ILE B 152 ? 0.10467 0.12484 0.07891 0.02992  0.00232  0.01438  148 ILE B CB  
3198 C CG1 . ILE B 152 ? 0.16976 0.19884 0.15241 0.03432  0.00602  0.01303  148 ILE B CG1 
3199 C CG2 . ILE B 152 ? 0.11995 0.14620 0.10043 0.03208  -0.00461 0.01501  148 ILE B CG2 
3200 C CD1 . ILE B 152 ? 0.17217 0.19871 0.15449 0.04259  0.00265  0.01142  148 ILE B CD1 
3201 N N   . SER B 153 ? 0.14377 0.14462 0.09170 0.01881  0.00478  0.01446  149 SER B N   
3202 C CA  . SER B 153 ? 0.15075 0.14321 0.08368 0.01632  0.00317  0.01385  149 SER B CA  
3203 C C   . SER B 153 ? 0.16194 0.15811 0.09702 0.01381  0.00822  0.00963  149 SER B C   
3204 O O   . SER B 153 ? 0.14076 0.13363 0.06970 0.01352  0.00407  0.00688  149 SER B O   
3205 C CB  . SER B 153 ? 0.21878 0.19745 0.13274 0.01387  0.00564  0.01714  149 SER B CB  
3206 O OG  . SER B 153 ? 0.20206 0.17142 0.10857 0.01704  -0.00316 0.02084  149 SER B OG  
3207 N N   . ALA B 154 ? 0.12834 0.13015 0.07239 0.01272  0.01549  0.00833  150 ALA B N   
3208 C CA  . ALA B 154 ? 0.15091 0.15566 0.09893 0.01215  0.01921  0.00360  150 ALA B CA  
3209 C C   . ALA B 154 ? 0.16854 0.17653 0.12622 0.01294  0.01281  0.00238  150 ALA B C   
3210 O O   . ALA B 154 ? 0.15354 0.15698 0.10729 0.01288  0.01038  -0.00178 150 ALA B O   
3211 C CB  . ALA B 154 ? 0.20518 0.21626 0.16423 0.01161  0.02582  0.00267  150 ALA B CB  
3212 N N   . LEU B 155 ? 0.12204 0.13722 0.09171 0.01340  0.01023  0.00595  151 LEU B N   
3213 C CA  . LEU B 155 ? 0.15505 0.17442 0.13501 0.01198  0.00507  0.00691  151 LEU B CA  
3214 C C   . LEU B 155 ? 0.11101 0.12673 0.08703 0.01081  -0.00292 0.00606  151 LEU B C   
3215 O O   . LEU B 155 ? 0.13366 0.14666 0.11345 0.00821  -0.00825 0.00437  151 LEU B O   
3216 C CB  . LEU B 155 ? 0.10572 0.13559 0.09711 0.01260  0.00608  0.01149  151 LEU B CB  
3217 C CG  . LEU B 155 ? 0.17783 0.21048 0.17584 0.01163  0.00898  0.01310  151 LEU B CG  
3218 C CD1 . LEU B 155 ? 0.24843 0.27651 0.24215 0.01344  0.01283  0.01017  151 LEU B CD1 
3219 C CD2 . LEU B 155 ? 0.15143 0.19428 0.15580 0.01258  0.01138  0.01750  151 LEU B CD2 
3220 N N   . TYR B 156 ? 0.11737 0.13091 0.08538 0.01266  -0.00572 0.00719  152 TYR B N   
3221 C CA  . TYR B 156 ? 0.16072 0.17054 0.12514 0.01211  -0.01598 0.00639  152 TYR B CA  
3222 C C   . TYR B 156 ? 0.17796 0.17400 0.12484 0.01112  -0.01850 0.00090  152 TYR B C   
3223 O O   . TYR B 156 ? 0.19166 0.18400 0.14010 0.00914  -0.02773 -0.00174 152 TYR B O   
3224 C CB  . TYR B 156 ? 0.15543 0.16342 0.11345 0.01561  -0.02017 0.00900  152 TYR B CB  
3225 C CG  . TYR B 156 ? 0.22558 0.23046 0.18179 0.01577  -0.03347 0.00825  152 TYR B CG  
3226 C CD1 . TYR B 156 ? 0.20328 0.22281 0.18268 0.01571  -0.04053 0.00996  152 TYR B CD1 
3227 C CD2 . TYR B 156 ? 0.24319 0.23136 0.17473 0.01580  -0.03908 0.00571  152 TYR B CD2 
3228 C CE1 . TYR B 156 ? 0.21816 0.23641 0.19981 0.01554  -0.05473 0.00893  152 TYR B CE1 
3229 C CE2 . TYR B 156 ? 0.24474 0.22829 0.17316 0.01615  -0.05382 0.00452  152 TYR B CE2 
3230 C CZ  . TYR B 156 ? 0.25402 0.25295 0.20934 0.01595  -0.06260 0.00603  152 TYR B CZ  
3231 O OH  . TYR B 156 ? 0.36185 0.35769 0.31781 0.01606  -0.07931 0.00456  152 TYR B OH  
3232 N N   . TYR B 157 ? 0.15545 0.14405 0.08581 0.01236  -0.01034 -0.00132 153 TYR B N   
3233 C CA  . TYR B 157 ? 0.22215 0.19822 0.13216 0.01293  -0.01086 -0.00749 153 TYR B CA  
3234 C C   . TYR B 157 ? 0.18672 0.16191 0.10290 0.01342  -0.00852 -0.01376 153 TYR B C   
3235 O O   . TYR B 157 ? 0.25918 0.22363 0.15893 0.01540  -0.00923 -0.02091 153 TYR B O   
3236 C CB  . TYR B 157 ? 0.18661 0.15661 0.07574 0.01354  -0.00136 -0.00684 153 TYR B CB  
3237 C CG  . TYR B 157 ? 0.20252 0.16442 0.07606 0.01346  -0.00752 -0.00155 153 TYR B CG  
3238 C CD1 . TYR B 157 ? 0.24319 0.19336 0.09954 0.01440  -0.01950 -0.00339 153 TYR B CD1 
3239 C CD2 . TYR B 157 ? 0.19507 0.15862 0.07038 0.01284  -0.00351 0.00502  153 TYR B CD2 
3240 C CE1 . TYR B 157 ? 0.34262 0.28348 0.18402 0.01523  -0.02742 0.00182  153 TYR B CE1 
3241 C CE2 . TYR B 157 ? 0.25951 0.21244 0.11990 0.01360  -0.01092 0.01012  153 TYR B CE2 
3242 C CZ  . TYR B 157 ? 0.28772 0.22967 0.13137 0.01507  -0.02295 0.00880  153 TYR B CZ  
3243 O OH  . TYR B 157 ? 0.37748 0.30721 0.20586 0.01669  -0.03242 0.01423  153 TYR B OH  
3244 N N   . TYR B 158 ? 0.15384 0.13807 0.09095 0.01246  -0.00643 -0.01166 154 TYR B N   
3245 C CA  . TYR B 158 ? 0.16092 0.14065 0.10410 0.01321  -0.00813 -0.01696 154 TYR B CA  
3246 C C   . TYR B 158 ? 0.20797 0.17795 0.14991 0.01082  -0.02131 -0.01968 154 TYR B C   
3247 O O   . TYR B 158 ? 0.23340 0.19189 0.17042 0.01267  -0.02510 -0.02701 154 TYR B O   
3248 C CB  . TYR B 158 ? 0.17240 0.16100 0.13534 0.01207  -0.00544 -0.01238 154 TYR B CB  
3249 C CG  . TYR B 158 ? 0.24803 0.22963 0.21622 0.01401  -0.00735 -0.01730 154 TYR B CG  
3250 C CD1 . TYR B 158 ? 0.22100 0.20165 0.18598 0.01964  -0.00027 -0.02415 154 TYR B CD1 
3251 C CD2 . TYR B 158 ? 0.23351 0.20950 0.21130 0.01019  -0.01651 -0.01488 154 TYR B CD2 
3252 C CE1 . TYR B 158 ? 0.27061 0.24406 0.24170 0.02341  -0.00347 -0.02960 154 TYR B CE1 
3253 C CE2 . TYR B 158 ? 0.26257 0.22809 0.24392 0.01246  -0.02028 -0.01905 154 TYR B CE2 
3254 C CZ  . TYR B 158 ? 0.33930 0.30316 0.31721 0.02007  -0.01432 -0.02697 154 TYR B CZ  
3255 O OH  . TYR B 158 ? 0.38254 0.33533 0.36532 0.02428  -0.01941 -0.03204 154 TYR B OH  
3256 N N   . SER B 159 ? 0.20161 0.17580 0.14920 0.00711  -0.02937 -0.01461 155 SER B N   
3257 C CA  . SER B 159 ? 0.21366 0.18076 0.16501 0.00313  -0.04361 -0.01643 155 SER B CA  
3258 C C   . SER B 159 ? 0.31312 0.26220 0.23934 0.00620  -0.05061 -0.02571 155 SER B C   
3259 O O   . SER B 159 ? 0.27884 0.21682 0.20536 0.00353  -0.06356 -0.03010 155 SER B O   
3260 C CB  . SER B 159 ? 0.32103 0.30094 0.28763 -0.00072 -0.05014 -0.00934 155 SER B CB  
3261 O OG  . SER B 159 ? 0.34398 0.32446 0.29694 0.00327  -0.04922 -0.00857 155 SER B OG  
3262 N N   . THR B 160 ? 0.23893 0.18375 0.14203 0.01118  -0.04250 -0.02866 156 THR B N   
3263 C CA  . THR B 160 ? 0.28744 0.21457 0.16072 0.01500  -0.04632 -0.03783 156 THR B CA  
3264 C C   . THR B 160 ? 0.43630 0.36046 0.29582 0.02085  -0.03165 -0.04491 156 THR B C   
3265 O O   . THR B 160 ? 0.37169 0.28487 0.20227 0.02493  -0.02848 -0.05149 156 THR B O   
3266 C CB  . THR B 160 ? 0.32854 0.25139 0.18147 0.01528  -0.05078 -0.03461 156 THR B CB  
3267 O OG1 . THR B 160 ? 0.35384 0.28750 0.20824 0.01554  -0.03831 -0.02690 156 THR B OG1 
3268 C CG2 . THR B 160 ? 0.38133 0.30658 0.24899 0.01107  -0.06849 -0.03064 156 THR B CG2 
3269 N N   . GLY B 161 ? 0.31801 0.25243 0.19768 0.02167  -0.02272 -0.04388 157 GLY B N   
3270 C CA  . GLY B 161 ? 0.32745 0.26296 0.20161 0.02784  -0.00969 -0.05122 157 GLY B CA  
3271 C C   . GLY B 161 ? 0.37758 0.32297 0.24205 0.02849  0.00613  -0.04806 157 GLY B C   
3272 O O   . GLY B 161 ? 0.37057 0.31988 0.23111 0.03333  0.01849  -0.05452 157 GLY B O   
3273 N N   . GLY B 162 ? 0.35441 0.30411 0.21650 0.02374  0.00597  -0.03836 158 GLY B N   
3274 C CA  . GLY B 162 ? 0.30945 0.26494 0.16133 0.02232  0.01896  -0.03351 158 GLY B CA  
3275 C C   . GLY B 162 ? 0.39281 0.36444 0.26856 0.02059  0.02885  -0.02861 158 GLY B C   
3276 O O   . GLY B 162 ? 0.38829 0.36469 0.25910 0.01773  0.03875  -0.02363 158 GLY B O   
3277 N N   . THR B 163 ? 0.27528 0.25367 0.17556 0.02160  0.02530  -0.02938 159 THR B N   
3278 C CA  . THR B 163 ? 0.27976 0.27169 0.20177 0.02077  0.03202  -0.02588 159 THR B CA  
3279 C C   . THR B 163 ? 0.19734 0.19262 0.13318 0.02596  0.03375  -0.03370 159 THR B C   
3280 O O   . THR B 163 ? 0.21918 0.20599 0.15751 0.02822  0.02438  -0.03753 159 THR B O   
3281 C CB  . THR B 163 ? 0.19873 0.19436 0.13523 0.01759  0.02445  -0.01787 159 THR B CB  
3282 O OG1 . THR B 163 ? 0.24915 0.24174 0.17480 0.01472  0.02212  -0.01169 159 THR B OG1 
3283 C CG2 . THR B 163 ? 0.14014 0.14679 0.09561 0.01738  0.02926  -0.01535 159 THR B CG2 
3284 N N   . GLN B 164 ? 0.18407 0.19121 0.13035 0.02769  0.04462  -0.03595 160 GLN B N   
3285 C CA  . GLN B 164 ? 0.24391 0.25589 0.20727 0.03409  0.04518  -0.04345 160 GLN B CA  
3286 C C   . GLN B 164 ? 0.19957 0.21379 0.18289 0.03306  0.03659  -0.03815 160 GLN B C   
3287 O O   . GLN B 164 ? 0.15464 0.17201 0.14110 0.02775  0.03474  -0.02954 160 GLN B O   
3288 C CB  . GLN B 164 ? 0.19927 0.22688 0.17117 0.03643  0.05971  -0.04794 160 GLN B CB  
3289 C CG  . GLN B 164 ? 0.39438 0.42135 0.34318 0.03571  0.07150  -0.05076 160 GLN B CG  
3290 C CD  . GLN B 164 ? 0.52817 0.56384 0.48459 0.04165  0.08197  -0.05548 160 GLN B CD  
3291 O OE1 . GLN B 164 ? 0.71446 0.74191 0.66691 0.04815  0.08182  -0.06546 160 GLN B OE1 
3292 N NE2 . GLN B 164 ? 0.66743 0.72149 0.63724 0.03822  0.08975  -0.04910 160 GLN B NE2 
3293 N N   . LEU B 165 ? 0.20969 0.14999 0.16162 0.04659  0.00696  -0.00936 161 LEU B N   
3294 C CA  . LEU B 165 ? 0.19610 0.13458 0.14943 0.04709  0.00394  -0.00682 161 LEU B CA  
3295 C C   . LEU B 165 ? 0.18839 0.14246 0.15390 0.04884  0.00337  -0.00507 161 LEU B C   
3296 O O   . LEU B 165 ? 0.18936 0.14611 0.15755 0.04490  0.00089  -0.00272 161 LEU B O   
3297 C CB  . LEU B 165 ? 0.29950 0.22285 0.24329 0.05346  0.00372  -0.00745 161 LEU B CB  
3298 C CG  . LEU B 165 ? 0.34435 0.26054 0.28481 0.05389  0.00049  -0.00463 161 LEU B CG  
3299 C CD1 . LEU B 165 ? 0.27278 0.18489 0.20945 0.04342  -0.00137 -0.00314 161 LEU B CD1 
3300 C CD2 . LEU B 165 ? 0.37913 0.27628 0.30646 0.06129  0.00034  -0.00530 161 LEU B CD2 
3301 N N   . PRO B 166 ? 0.17954 0.14495 0.15245 0.05386  0.00570  -0.00638 162 PRO B N   
3302 C CA  . PRO B 166 ? 0.23269 0.21321 0.21640 0.05358  0.00483  -0.00497 162 PRO B CA  
3303 C C   . PRO B 166 ? 0.19869 0.18409 0.18508 0.04582  0.00441  -0.00355 162 PRO B C   
3304 O O   . PRO B 166 ? 0.18064 0.17112 0.17128 0.04390  0.00223  -0.00159 162 PRO B O   
3305 C CB  . PRO B 166 ? 0.19986 0.19312 0.19036 0.05835  0.00835  -0.00763 162 PRO B CB  
3306 C CG  . PRO B 166 ? 0.20957 0.19248 0.19273 0.06537  0.00984  -0.00985 162 PRO B CG  
3307 C CD  . PRO B 166 ? 0.31550 0.28139 0.28720 0.06014  0.00927  -0.00950 162 PRO B CD  
3308 N N   . THR B 167 ? 0.13206 0.11481 0.11460 0.04197  0.00624  -0.00454 163 THR B N   
3309 C CA  . THR B 167 ? 0.14264 0.12775 0.12547 0.03637  0.00546  -0.00321 163 THR B CA  
3310 C C   . THR B 167 ? 0.17245 0.15276 0.15301 0.03375  0.00198  -0.00144 163 THR B C   
3311 O O   . THR B 167 ? 0.14481 0.12942 0.12811 0.03128  0.00067  0.00005  163 THR B O   
3312 C CB  . THR B 167 ? 0.23499 0.21685 0.21213 0.03415  0.00762  -0.00458 163 THR B CB  
3313 O OG1 . THR B 167 ? 0.31556 0.30263 0.29441 0.03562  0.01176  -0.00647 163 THR B OG1 
3314 C CG2 . THR B 167 ? 0.16973 0.15244 0.14534 0.03025  0.00647  -0.00316 163 THR B CG2 
3315 N N   . LEU B 168 ? 0.13108 0.10224 0.10574 0.03374  0.00083  -0.00188 164 LEU B N   
3316 C CA  . LEU B 168 ? 0.13119 0.09922 0.10368 0.02997  -0.00181 -0.00057 164 LEU B CA  
3317 C C   . LEU B 168 ? 0.14607 0.11646 0.12223 0.03104  -0.00320 0.00151  164 LEU B C   
3318 O O   . LEU B 168 ? 0.13395 0.10825 0.11214 0.02782  -0.00451 0.00282  164 LEU B O   
3319 C CB  . LEU B 168 ? 0.20319 0.15933 0.16667 0.02827  -0.00228 -0.00175 164 LEU B CB  
3320 C CG  . LEU B 168 ? 0.17943 0.13283 0.13956 0.02223  -0.00432 -0.00098 164 LEU B CG  
3321 C CD1 . LEU B 168 ? 0.18762 0.14910 0.14955 0.01765  -0.00535 -0.00190 164 LEU B CD1 
3322 C CD2 . LEU B 168 ? 0.21167 0.14953 0.16058 0.02040  -0.00436 -0.00181 164 LEU B CD2 
3323 N N   . ALA B 169 ? 0.13296 0.10139 0.10950 0.03619  -0.00306 0.00165  165 ALA B N   
3324 C CA  . ALA B 169 ? 0.13230 0.10244 0.11098 0.03784  -0.00508 0.00370  165 ALA B CA  
3325 C C   . ALA B 169 ? 0.16341 0.14594 0.15014 0.03618  -0.00520 0.00446  165 ALA B C   
3326 O O   . ALA B 169 ? 0.18078 0.16455 0.16796 0.03399  -0.00689 0.00617  165 ALA B O   
3327 C CB  . ALA B 169 ? 0.16626 0.13355 0.14391 0.04552  -0.00546 0.00341  165 ALA B CB  
3328 N N   . ARG B 170 ? 0.11612 0.10656 0.10762 0.03656  -0.00309 0.00305  166 ARG B N   
3329 C CA  . ARG B 170 ? 0.16287 0.16182 0.15900 0.03359  -0.00281 0.00351  166 ARG B CA  
3330 C C   . ARG B 170 ? 0.12081 0.11700 0.11400 0.02945  -0.00338 0.00433  166 ARG B C   
3331 O O   . ARG B 170 ? 0.12249 0.12152 0.11685 0.02756  -0.00425 0.00534  166 ARG B O   
3332 C CB  . ARG B 170 ? 0.20503 0.21044 0.20401 0.03318  0.00026  0.00169  166 ARG B CB  
3333 C CG  . ARG B 170 ? 0.24985 0.26098 0.25070 0.02888  0.00092  0.00196  166 ARG B CG  
3334 C CD  . ARG B 170 ? 0.35946 0.37840 0.36315 0.02724  0.00427  0.00003  166 ARG B CD  
3335 N NE  . ARG B 170 ? 0.41273 0.42660 0.41151 0.02665  0.00727  -0.00119 166 ARG B NE  
3336 C CZ  . ARG B 170 ? 0.40435 0.41963 0.40399 0.02996  0.00934  -0.00297 166 ARG B CZ  
3337 N NH1 . ARG B 170 ? 0.38155 0.40285 0.38677 0.03524  0.00864  -0.00378 166 ARG B NH1 
3338 N NH2 . ARG B 170 ? 0.43750 0.44721 0.43105 0.02863  0.01208  -0.00403 166 ARG B NH2 
3339 N N   . SER B 171 ? 0.10781 0.09916 0.09693 0.02842  -0.00303 0.00362  167 SER B N   
3340 C CA  . SER B 171 ? 0.10666 0.09831 0.09402 0.02588  -0.00393 0.00396  167 SER B CA  
3341 C C   . SER B 171 ? 0.12200 0.11356 0.10935 0.02414  -0.00557 0.00512  167 SER B C   
3342 O O   . SER B 171 ? 0.16663 0.16176 0.15479 0.02295  -0.00596 0.00559  167 SER B O   
3343 C CB  . SER B 171 ? 0.17275 0.16157 0.15618 0.02531  -0.00387 0.00262  167 SER B CB  
3344 O OG  . SER B 171 ? 0.11249 0.10021 0.09420 0.02653  -0.00198 0.00167  167 SER B OG  
3345 N N   . PHE B 172 ? 0.11195 0.09811 0.09685 0.02407  -0.00624 0.00553  168 PHE B N   
3346 C CA  . PHE B 172 ? 0.14545 0.12968 0.12828 0.02159  -0.00734 0.00690  168 PHE B CA  
3347 C C   . PHE B 172 ? 0.18171 0.16994 0.16737 0.02260  -0.00799 0.00832  168 PHE B C   
3348 O O   . PHE B 172 ? 0.13743 0.12791 0.12261 0.02005  -0.00815 0.00895  168 PHE B O   
3349 C CB  . PHE B 172 ? 0.12396 0.09748 0.10028 0.02177  -0.00792 0.00739  168 PHE B CB  
3350 C CG  . PHE B 172 ? 0.18665 0.15449 0.15750 0.01787  -0.00745 0.00596  168 PHE B CG  
3351 C CD1 . PHE B 172 ? 0.25715 0.23142 0.22914 0.01263  -0.00732 0.00501  168 PHE B CD1 
3352 C CD2 . PHE B 172 ? 0.21489 0.17159 0.17908 0.01957  -0.00721 0.00518  168 PHE B CD2 
3353 C CE1 . PHE B 172 ? 0.21735 0.18859 0.18468 0.00792  -0.00727 0.00328  168 PHE B CE1 
3354 C CE2 . PHE B 172 ? 0.23221 0.18263 0.18986 0.01475  -0.00687 0.00354  168 PHE B CE2 
3355 C CZ  . PHE B 172 ? 0.25530 0.21377 0.21488 0.00830  -0.00705 0.00258  168 PHE B CZ  
3356 N N   . ILE B 173 ? 0.15381 0.14414 0.14239 0.02602  -0.00827 0.00847  169 ILE B N   
3357 C CA  . ILE B 173 ? 0.14013 0.13500 0.13098 0.02622  -0.00940 0.00950  169 ILE B CA  
3358 C C   . ILE B 173 ? 0.10131 0.10039 0.09326 0.02358  -0.00835 0.00901  169 ILE B C   
3359 O O   . ILE B 173 ? 0.13804 0.13811 0.12885 0.02203  -0.00903 0.00978  169 ILE B O   
3360 C CB  . ILE B 173 ? 0.13555 0.13551 0.13066 0.02995  -0.00995 0.00904  169 ILE B CB  
3361 C CG1 . ILE B 173 ? 0.11903 0.11329 0.11124 0.03470  -0.01164 0.00974  169 ILE B CG1 
3362 C CG2 . ILE B 173 ? 0.16818 0.17531 0.16619 0.02870  -0.01120 0.00943  169 ILE B CG2 
3363 C CD1 . ILE B 173 ? 0.11551 0.11729 0.11309 0.04014  -0.01182 0.00848  169 ILE B CD1 
3364 N N   . ILE B 174 ? 0.09921 0.09903 0.09151 0.02346  -0.00670 0.00771  170 ILE B N   
3365 C CA  . ILE B 174 ? 0.10720 0.10762 0.09769 0.02232  -0.00580 0.00726  170 ILE B CA  
3366 C C   . ILE B 174 ? 0.11933 0.12002 0.10807 0.02178  -0.00609 0.00735  170 ILE B C   
3367 O O   . ILE B 174 ? 0.12222 0.12345 0.10920 0.02136  -0.00588 0.00743  170 ILE B O   
3368 C CB  . ILE B 174 ? 0.12936 0.12806 0.11808 0.02301  -0.00427 0.00613  170 ILE B CB  
3369 C CG1 . ILE B 174 ? 0.10928 0.10979 0.09973 0.02222  -0.00295 0.00559  170 ILE B CG1 
3370 C CG2 . ILE B 174 ? 0.18911 0.18500 0.17293 0.02340  -0.00376 0.00582  170 ILE B CG2 
3371 C CD1 . ILE B 174 ? 0.15717 0.15501 0.14484 0.02242  -0.00094 0.00452  170 ILE B CD1 
3372 N N   . CYS B 175 ? 0.13198 0.13299 0.12086 0.02138  -0.00632 0.00696  171 CYS B N   
3373 C CA  . CYS B 175 ? 0.16530 0.17033 0.15388 0.02007  -0.00621 0.00640  171 CYS B CA  
3374 C C   . CYS B 175 ? 0.19322 0.19815 0.18067 0.01755  -0.00616 0.00749  171 CYS B C   
3375 O O   . CYS B 175 ? 0.18745 0.19650 0.17451 0.01718  -0.00529 0.00698  171 CYS B O   
3376 C CB  . CYS B 175 ? 0.22580 0.23227 0.21453 0.01836  -0.00655 0.00537  171 CYS B CB  
3377 S SG  . CYS B 175 ? 0.23791 0.24564 0.22633 0.02139  -0.00702 0.00385  171 CYS B SG  
3378 N N   . ILE B 176 ? 0.12498 0.12464 0.11076 0.01646  -0.00706 0.00894  172 ILE B N   
3379 C CA  . ILE B 176 ? 0.15815 0.15533 0.14030 0.01392  -0.00731 0.01034  172 ILE B CA  
3380 C C   . ILE B 176 ? 0.15433 0.15360 0.13628 0.01471  -0.00734 0.01066  172 ILE B C   
3381 O O   . ILE B 176 ? 0.16099 0.16165 0.14033 0.01257  -0.00633 0.01069  172 ILE B O   
3382 C CB  . ILE B 176 ? 0.12769 0.11641 0.10595 0.01447  -0.00898 0.01205  172 ILE B CB  
3383 C CG1 . ILE B 176 ? 0.18871 0.17204 0.16354 0.01213  -0.00845 0.01153  172 ILE B CG1 
3384 C CG2 . ILE B 176 ? 0.15918 0.14349 0.13177 0.01289  -0.00994 0.01402  172 ILE B CG2 
3385 C CD1 . ILE B 176 ? 0.17283 0.14516 0.14229 0.01476  -0.00996 0.01274  172 ILE B CD1 
3386 N N   . GLN B 177 ? 0.11473 0.11435 0.09866 0.01703  -0.00811 0.01055  173 GLN B N   
3387 C CA  . GLN B 177 ? 0.14638 0.14655 0.12844 0.01656  -0.00825 0.01052  173 GLN B CA  
3388 C C   . GLN B 177 ? 0.13040 0.13184 0.11067 0.01708  -0.00617 0.00895  173 GLN B C   
3389 O O   . GLN B 177 ? 0.14256 0.14348 0.11910 0.01618  -0.00547 0.00874  173 GLN B O   
3390 C CB  . GLN B 177 ? 0.13657 0.13781 0.12080 0.01723  -0.00934 0.01034  173 GLN B CB  
3391 C CG  . GLN B 177 ? 0.12732 0.12961 0.11377 0.01860  -0.01177 0.01155  173 GLN B CG  
3392 C CD  . GLN B 177 ? 0.15389 0.16186 0.14430 0.01878  -0.01260 0.01071  173 GLN B CD  
3393 O OE1 . GLN B 177 ? 0.14709 0.15815 0.13684 0.01710  -0.01426 0.01077  173 GLN B OE1 
3394 N NE2 . GLN B 177 ? 0.14710 0.15735 0.14135 0.02011  -0.01126 0.00964  173 GLN B NE2 
3395 N N   . MET B 178 ? 0.10254 0.10501 0.08429 0.01932  -0.00526 0.00775  174 MET B N   
3396 C CA  . MET B 178 ? 0.10528 0.10776 0.08397 0.02195  -0.00383 0.00624  174 MET B CA  
3397 C C   . MET B 178 ? 0.14798 0.15732 0.12798 0.02262  -0.00267 0.00519  174 MET B C   
3398 O O   . MET B 178 ? 0.13314 0.14398 0.11070 0.02623  -0.00147 0.00364  174 MET B O   
3399 C CB  . MET B 178 ? 0.13990 0.13990 0.11773 0.02489  -0.00378 0.00551  174 MET B CB  
3400 C CG  . MET B 178 ? 0.18561 0.18012 0.16171 0.02308  -0.00391 0.00602  174 MET B CG  
3401 S SD  . MET B 178 ? 0.18253 0.17010 0.15284 0.02554  -0.00301 0.00529  174 MET B SD  
3402 C CE  . MET B 178 ? 0.20940 0.18933 0.16981 0.02927  -0.00212 0.00431  174 MET B CE  
3403 N N   . ILE B 179 ? 0.12980 0.14313 0.11269 0.01918  -0.00279 0.00577  175 ILE B N   
3404 C CA  . ILE B 179 ? 0.10737 0.12945 0.09190 0.01769  -0.00113 0.00441  175 ILE B CA  
3405 C C   . ILE B 179 ? 0.14043 0.16062 0.12170 0.01255  -0.00021 0.00565  175 ILE B C   
3406 O O   . ILE B 179 ? 0.19213 0.21517 0.17098 0.01223  0.00178  0.00482  175 ILE B O   
3407 C CB  . ILE B 179 ? 0.14451 0.17274 0.13329 0.01628  -0.00166 0.00350  175 ILE B CB  
3408 C CG1 . ILE B 179 ? 0.17303 0.20234 0.16334 0.02176  -0.00292 0.00243  175 ILE B CG1 
3409 C CG2 . ILE B 179 ? 0.10305 0.14341 0.09435 0.01298  0.00031  0.00159  175 ILE B CG2 
3410 C CD1 . ILE B 179 ? 0.18821 0.22205 0.18155 0.02009  -0.00412 0.00159  175 ILE B CD1 
3411 N N   . SER B 180 ? 0.10974 0.12368 0.08928 0.00900  -0.00159 0.00763  176 SER B N   
3412 C CA  . SER B 180 ? 0.16101 0.17030 0.13464 0.00418  -0.00106 0.00923  176 SER B CA  
3413 C C   . SER B 180 ? 0.14045 0.14481 0.10965 0.00540  -0.00188 0.01041  176 SER B C   
3414 O O   . SER B 180 ? 0.14568 0.15065 0.11032 0.00290  -0.00003 0.01027  176 SER B O   
3415 C CB  . SER B 180 ? 0.20163 0.20195 0.17177 0.00172  -0.00281 0.01118  176 SER B CB  
3416 O OG  . SER B 180 ? 0.23940 0.24301 0.21135 -0.00140 -0.00180 0.00982  176 SER B OG  
3417 N N   . GLU B 181 ? 0.15290 0.15312 0.12302 0.00852  -0.00452 0.01133  177 GLU B N   
3418 C CA  . GLU B 181 ? 0.13006 0.12675 0.09586 0.00862  -0.00591 0.01217  177 GLU B CA  
3419 C C   . GLU B 181 ? 0.19951 0.19858 0.16352 0.00956  -0.00363 0.01009  177 GLU B C   
3420 O O   . GLU B 181 ? 0.12675 0.12323 0.08466 0.00788  -0.00326 0.01022  177 GLU B O   
3421 C CB  . GLU B 181 ? 0.15899 0.15417 0.12748 0.01091  -0.00907 0.01295  177 GLU B CB  
3422 C CG  . GLU B 181 ? 0.15553 0.14764 0.12484 0.01199  -0.01142 0.01474  177 GLU B CG  
3423 C CD  . GLU B 181 ? 0.29858 0.28417 0.26024 0.01086  -0.01355 0.01716  177 GLU B CD  
3424 O OE1 . GLU B 181 ? 0.26314 0.24728 0.21903 0.00827  -0.01299 0.01750  177 GLU B OE1 
3425 O OE2 . GLU B 181 ? 0.33629 0.31682 0.29623 0.01306  -0.01579 0.01873  177 GLU B OE2 
3426 N N   . ALA B 182 ? 0.15797 0.16048 0.12556 0.01279  -0.00219 0.00812  178 ALA B N   
3427 C CA  . ALA B 182 ? 0.12036 0.12303 0.08435 0.01537  0.00008  0.00594  178 ALA B CA  
3428 C C   . ALA B 182 ? 0.16086 0.16910 0.12312 0.01430  0.00315  0.00476  178 ALA B C   
3429 O O   . ALA B 182 ? 0.19015 0.19614 0.14637 0.01496  0.00494  0.00353  178 ALA B O   
3430 C CB  . ALA B 182 ? 0.13370 0.13771 0.10028 0.02026  0.00058  0.00435  178 ALA B CB  
3431 N N   . ALA B 183 ? 0.13443 0.15002 0.10114 0.01193  0.00418  0.00478  179 ALA B N   
3432 C CA  . ALA B 183 ? 0.14153 0.16428 0.10679 0.00901  0.00773  0.00346  179 ALA B CA  
3433 C C   . ALA B 183 ? 0.13304 0.14812 0.08976 0.00419  0.00788  0.00532  179 ALA B C   
3434 O O   . ALA B 183 ? 0.15500 0.17233 0.10704 0.00326  0.01109  0.00389  179 ALA B O   
3435 C CB  . ALA B 183 ? 0.13786 0.16953 0.10859 0.00511  0.00871  0.00304  179 ALA B CB  
3436 N N   . ARG B 184 ? 0.13430 0.14030 0.08821 0.00187  0.00433  0.00841  180 ARG B N   
3437 C CA  . ARG B 184 ? 0.14346 0.14132 0.08794 -0.00206 0.00343  0.01062  180 ARG B CA  
3438 C C   . ARG B 184 ? 0.14926 0.14283 0.08811 -0.00039 0.00263  0.01009  180 ARG B C   
3439 O O   . ARG B 184 ? 0.17263 0.16209 0.10259 -0.00349 0.00354  0.01064  180 ARG B O   
3440 C CB  . ARG B 184 ? 0.14537 0.13502 0.08808 -0.00284 -0.00089 0.01389  180 ARG B CB  
3441 C CG  . ARG B 184 ? 0.15027 0.13873 0.09343 -0.00600 -0.00019 0.01480  180 ARG B CG  
3442 C CD  . ARG B 184 ? 0.16994 0.14921 0.11135 -0.00377 -0.00478 0.01754  180 ARG B CD  
3443 N NE  . ARG B 184 ? 0.19529 0.16760 0.13194 -0.00735 -0.00430 0.01881  180 ARG B NE  
3444 C CZ  . ARG B 184 ? 0.35035 0.31260 0.28329 -0.00484 -0.00771 0.02099  180 ARG B CZ  
3445 N NH1 . ARG B 184 ? 0.32146 0.28308 0.25733 0.00148  -0.01186 0.02194  180 ARG B NH1 
3446 N NH2 . ARG B 184 ? 0.27449 0.22720 0.19995 -0.00888 -0.00677 0.02194  180 ARG B NH2 
3447 N N   . PHE B 185 ? 0.14949 0.14253 0.09163 0.00353  0.00096  0.00903  181 PHE B N   
3448 C CA  . PHE B 185 ? 0.15982 0.14709 0.09540 0.00368  -0.00032 0.00839  181 PHE B CA  
3449 C C   . PHE B 185 ? 0.14806 0.13525 0.08348 0.00769  0.00222  0.00530  181 PHE B C   
3450 O O   . PHE B 185 ? 0.17253 0.16112 0.11368 0.01072  0.00168  0.00480  181 PHE B O   
3451 C CB  . PHE B 185 ? 0.15781 0.14220 0.09480 0.00312  -0.00546 0.01022  181 PHE B CB  
3452 C CG  . PHE B 185 ? 0.16859 0.15107 0.10370 0.00132  -0.00895 0.01335  181 PHE B CG  
3453 C CD1 . PHE B 185 ? 0.18138 0.15912 0.10725 -0.00112 -0.01122 0.01459  181 PHE B CD1 
3454 C CD2 . PHE B 185 ? 0.14869 0.13244 0.08951 0.00266  -0.01032 0.01502  181 PHE B CD2 
3455 C CE1 . PHE B 185 ? 0.17893 0.15300 0.10100 -0.00138 -0.01506 0.01774  181 PHE B CE1 
3456 C CE2 . PHE B 185 ? 0.15211 0.13108 0.08871 0.00240  -0.01373 0.01795  181 PHE B CE2 
3457 C CZ  . PHE B 185 ? 0.17269 0.14673 0.09982 0.00081  -0.01628 0.01945  181 PHE B CZ  
3458 N N   . GLN B 186 ? 0.19204 0.17566 0.11900 0.00810  0.00493  0.00323  182 GLN B N   
3459 C CA  . GLN B 186 ? 0.21565 0.19411 0.13834 0.01255  0.00669  0.00043  182 GLN B CA  
3460 C C   . GLN B 186 ? 0.16296 0.13343 0.08322 0.01075  0.00329  0.00095  182 GLN B C   
3461 O O   . GLN B 186 ? 0.21373 0.17911 0.13223 0.01400  0.00403  -0.00047 182 GLN B O   
3462 C CB  . GLN B 186 ? 0.22364 0.19705 0.13522 0.01334  0.01014  -0.00209 182 GLN B CB  
3463 C CG  . GLN B 186 ? 0.28289 0.26585 0.19608 0.01436  0.01457  -0.00335 182 GLN B CG  
3464 C CD  . GLN B 186 ? 0.34969 0.33161 0.25747 0.00765  0.01435  -0.00153 182 GLN B CD  
3465 O OE1 . GLN B 186 ? 0.30578 0.28499 0.21438 0.00322  0.01002  0.00170  182 GLN B OE1 
3466 N NE2 . GLN B 186 ? 0.34855 0.33223 0.24973 0.00743  0.01904  -0.00366 182 GLN B NE2 
3467 N N   . TYR B 187 ? 0.16317 0.13275 0.08255 0.00548  -0.00046 0.00285  183 TYR B N   
3468 C CA  . TYR B 187 ? 0.17675 0.14272 0.09539 0.00244  -0.00358 0.00290  183 TYR B CA  
3469 C C   . TYR B 187 ? 0.22178 0.19174 0.14980 0.00455  -0.00410 0.00352  183 TYR B C   
3470 O O   . TYR B 187 ? 0.17441 0.13872 0.09942 0.00404  -0.00365 0.00226  183 TYR B O   
3471 C CB  . TYR B 187 ? 0.16486 0.13396 0.08356 -0.00236 -0.00818 0.00476  183 TYR B CB  
3472 C CG  . TYR B 187 ? 0.22391 0.19311 0.14261 -0.00664 -0.01130 0.00409  183 TYR B CG  
3473 C CD1 . TYR B 187 ? 0.21968 0.18053 0.12709 -0.01121 -0.01111 0.00176  183 TYR B CD1 
3474 C CD2 . TYR B 187 ? 0.21356 0.19151 0.14293 -0.00668 -0.01403 0.00536  183 TYR B CD2 
3475 C CE1 . TYR B 187 ? 0.22508 0.18745 0.13230 -0.01707 -0.01364 0.00071  183 TYR B CE1 
3476 C CE2 . TYR B 187 ? 0.23402 0.21528 0.16448 -0.01147 -0.01631 0.00423  183 TYR B CE2 
3477 C CZ  . TYR B 187 ? 0.30627 0.28025 0.22585 -0.01732 -0.01611 0.00189  183 TYR B CZ  
3478 O OH  . TYR B 187 ? 0.25171 0.23036 0.17220 -0.02394 -0.01808 0.00038  183 TYR B OH  
3479 N N   . ILE B 188 ? 0.20198 0.18002 0.13959 0.00631  -0.00485 0.00540  184 ILE B N   
3480 C CA  . ILE B 188 ? 0.13769 0.11936 0.08356 0.00830  -0.00527 0.00588  184 ILE B CA  
3481 C C   . ILE B 188 ? 0.20435 0.18386 0.14945 0.01307  -0.00213 0.00425  184 ILE B C   
3482 O O   . ILE B 188 ? 0.19039 0.16758 0.13659 0.01437  -0.00206 0.00389  184 ILE B O   
3483 C CB  . ILE B 188 ? 0.17109 0.15960 0.12496 0.00864  -0.00710 0.00815  184 ILE B CB  
3484 C CG1 . ILE B 188 ? 0.20769 0.19763 0.16120 0.00593  -0.01105 0.00983  184 ILE B CG1 
3485 C CG2 . ILE B 188 ? 0.15037 0.14208 0.11185 0.01094  -0.00707 0.00831  184 ILE B CG2 
3486 C CD1 . ILE B 188 ? 0.15958 0.15196 0.11688 0.00720  -0.01305 0.01224  184 ILE B CD1 
3487 N N   . GLU B 189 ? 0.13990 0.12089 0.08278 0.01606  0.00047  0.00311  185 GLU B N   
3488 C CA  . GLU B 189 ? 0.17406 0.15397 0.11525 0.02224  0.00293  0.00111  185 GLU B CA  
3489 C C   . GLU B 189 ? 0.27342 0.23981 0.20376 0.02346  0.00341  -0.00027 185 GLU B C   
3490 O O   . GLU B 189 ? 0.17286 0.13476 0.10142 0.02744  0.00368  -0.00074 185 GLU B O   
3491 C CB  . GLU B 189 ? 0.21716 0.20285 0.15734 0.02530  0.00597  -0.00061 185 GLU B CB  
3492 C CG  . GLU B 189 ? 0.15983 0.14686 0.09862 0.03377  0.00810  -0.00312 185 GLU B CG  
3493 C CD  . GLU B 189 ? 0.22758 0.21958 0.16314 0.03758  0.01173  -0.00577 185 GLU B CD  
3494 O OE1 . GLU B 189 ? 0.30300 0.29563 0.23595 0.03269  0.01299  -0.00558 185 GLU B OE1 
3495 O OE2 . GLU B 189 ? 0.29725 0.29290 0.23239 0.04604  0.01333  -0.00818 185 GLU B OE2 
3496 N N   . GLY B 190 ? 0.22663 0.18484 0.14777 0.01947  0.00343  -0.00091 186 GLY B N   
3497 C CA  . GLY B 190 ? 0.22327 0.16590 0.13127 0.01876  0.00415  -0.00244 186 GLY B CA  
3498 C C   . GLY B 190 ? 0.18910 0.12868 0.09822 0.01387  0.00238  -0.00144 186 GLY B C   
3499 O O   . GLY B 190 ? 0.21727 0.14393 0.11645 0.01459  0.00355  -0.00238 186 GLY B O   
3500 N N   . GLU B 191 ? 0.18215 0.13291 0.10216 0.00906  -0.00023 0.00034  187 GLU B N   
3501 C CA  . GLU B 191 ? 0.21438 0.16621 0.13778 0.00483  -0.00135 0.00091  187 GLU B CA  
3502 C C   . GLU B 191 ? 0.23120 0.18221 0.15745 0.00986  -0.00016 0.00132  187 GLU B C   
3503 O O   . GLU B 191 ? 0.20177 0.14578 0.12318 0.00741  0.00062  0.00101  187 GLU B O   
3504 C CB  . GLU B 191 ? 0.30912 0.27489 0.24437 0.00119  -0.00446 0.00247  187 GLU B CB  
3505 C CG  . GLU B 191 ? 0.34080 0.30795 0.27269 -0.00565 -0.00674 0.00189  187 GLU B CG  
3506 C CD  . GLU B 191 ? 0.47456 0.44390 0.40700 -0.01238 -0.00733 0.00090  187 GLU B CD  
3507 O OE1 . GLU B 191 ? 0.67486 0.63511 0.60119 -0.01350 -0.00463 -0.00006 187 GLU B OE1 
3508 O OE2 . GLU B 191 ? 0.63684 0.61758 0.57546 -0.01652 -0.01049 0.00099  187 GLU B OE2 
3509 N N   . MET B 192 ? 0.18286 0.14121 0.11626 0.01604  -0.00001 0.00192  188 MET B N   
3510 C CA  . MET B 192 ? 0.17462 0.13258 0.10980 0.02106  0.00054  0.00207  188 MET B CA  
3511 C C   . MET B 192 ? 0.21757 0.16221 0.13977 0.02683  0.00227  0.00062  188 MET B C   
3512 O O   . MET B 192 ? 0.17319 0.10956 0.08960 0.02890  0.00257  0.00074  188 MET B O   
3513 C CB  . MET B 192 ? 0.18178 0.15285 0.12835 0.02467  -0.00014 0.00276  188 MET B CB  
3514 C CG  . MET B 192 ? 0.18544 0.16609 0.14201 0.02030  -0.00191 0.00435  188 MET B CG  
3515 S SD  . MET B 192 ? 0.22805 0.20928 0.18854 0.01656  -0.00297 0.00514  188 MET B SD  
3516 C CE  . MET B 192 ? 0.28088 0.26251 0.23952 0.01025  -0.00433 0.00514  188 MET B CE  
3517 N N   . ARG B 193 ? 0.22324 0.16472 0.13948 0.03011  0.00348  -0.00079 189 ARG B N   
3518 C CA  . ARG B 193 ? 0.24026 0.16699 0.14192 0.03701  0.00514  -0.00249 189 ARG B CA  
3519 C C   . ARG B 193 ? 0.27706 0.18377 0.16326 0.03249  0.00575  -0.00260 189 ARG B C   
3520 O O   . ARG B 193 ? 0.27913 0.17194 0.15370 0.03786  0.00634  -0.00284 189 ARG B O   
3521 C CB  . ARG B 193 ? 0.23012 0.15566 0.12655 0.03977  0.00688  -0.00440 189 ARG B CB  
3522 C CG  . ARG B 193 ? 0.39603 0.33241 0.29748 0.04969  0.00799  -0.00588 189 ARG B CG  
3523 C CD  . ARG B 193 ? 0.39421 0.32248 0.28408 0.05413  0.01069  -0.00851 189 ARG B CD  
3524 N NE  . ARG B 193 ? 0.38759 0.30744 0.27058 0.04501  0.01105  -0.00846 189 ARG B NE  
3525 C CZ  . ARG B 193 ? 0.33977 0.26929 0.22800 0.04072  0.01166  -0.00857 189 ARG B CZ  
3526 N NH1 . ARG B 193 ? 0.29977 0.24694 0.19956 0.04368  0.01272  -0.00883 189 ARG B NH1 
3527 N NH2 . ARG B 193 ? 0.36197 0.28310 0.24262 0.03260  0.01115  -0.00851 189 ARG B NH2 
3528 N N   . THR B 194 ? 0.23744 0.14224 0.12220 0.02229  0.00553  -0.00251 190 THR B N   
3529 C CA  . THR B 194 ? 0.30099 0.18724 0.16992 0.01550  0.00664  -0.00316 190 THR B CA  
3530 C C   . THR B 194 ? 0.22454 0.10947 0.09472 0.01293  0.00667  -0.00187 190 THR B C   
3531 O O   . THR B 194 ? 0.28636 0.15160 0.13970 0.01223  0.00827  -0.00218 190 THR B O   
3532 C CB  . THR B 194 ? 0.28100 0.17004 0.15005 0.00448  0.00595  -0.00385 190 THR B CB  
3533 O OG1 . THR B 194 ? 0.39133 0.27731 0.25489 0.00687  0.00635  -0.00524 190 THR B OG1 
3534 C CG2 . THR B 194 ? 0.45167 0.32382 0.30505 -0.00509 0.00732  -0.00492 190 THR B CG2 
3535 N N   . ARG B 195 ? 0.25552 0.15940 0.14359 0.01149  0.00517  -0.00048 191 ARG B N   
3536 C CA  . ARG B 195 ? 0.22058 0.12451 0.11042 0.01031  0.00555  0.00054  191 ARG B CA  
3537 C C   . ARG B 195 ? 0.20775 0.10012 0.08820 0.01995  0.00587  0.00091  191 ARG B C   
3538 O O   . ARG B 195 ? 0.27475 0.15353 0.14368 0.01853  0.00706  0.00135  191 ARG B O   
3539 C CB  . ARG B 195 ? 0.23263 0.15814 0.14260 0.00967  0.00387  0.00167  191 ARG B CB  
3540 C CG  . ARG B 195 ? 0.23451 0.17101 0.15267 0.00052  0.00328  0.00143  191 ARG B CG  
3541 C CD  . ARG B 195 ? 0.35256 0.30800 0.28851 0.00276  0.00111  0.00252  191 ARG B CD  
3542 N NE  . ARG B 195 ? 0.27553 0.24262 0.21944 -0.00382 0.00000  0.00220  191 ARG B NE  
3543 C CZ  . ARG B 195 ? 0.36609 0.33805 0.31133 -0.00715 -0.00189 0.00185  191 ARG B CZ  
3544 N NH1 . ARG B 195 ? 0.32302 0.28807 0.26149 -0.00532 -0.00227 0.00173  191 ARG B NH1 
3545 N NH2 . ARG B 195 ? 0.35443 0.33939 0.30781 -0.01200 -0.00350 0.00140  191 ARG B NH2 
3546 N N   . ILE B 196 ? 0.25174 0.15007 0.13652 0.02976  0.00477  0.00063  192 ILE B N   
3547 C CA  . ILE B 196 ? 0.30351 0.19458 0.18092 0.04053  0.00420  0.00067  192 ILE B CA  
3548 C C   . ILE B 196 ? 0.27277 0.13770 0.12642 0.04404  0.00566  -0.00022 192 ILE B C   
3549 O O   . ILE B 196 ? 0.28038 0.12977 0.12032 0.04880  0.00552  0.00044  192 ILE B O   
3550 C CB  . ILE B 196 ? 0.24982 0.15879 0.14028 0.04918  0.00276  -0.00001 192 ILE B CB  
3551 C CG1 . ILE B 196 ? 0.39195 0.32181 0.30182 0.04560  0.00132  0.00103  192 ILE B CG1 
3552 C CG2 . ILE B 196 ? 0.24417 0.14749 0.12648 0.06179  0.00171  -0.00066 192 ILE B CG2 
3553 C CD1 . ILE B 196 ? 0.27537 0.22372 0.19823 0.04992  0.00055  0.00020  192 ILE B CD1 
3554 N N   . ARG B 197 ? 0.29096 0.14845 0.13721 0.04182  0.00703  -0.00172 193 ARG B N   
3555 C CA  . ARG B 197 ? 0.32017 0.15007 0.14145 0.04590  0.00863  -0.00292 193 ARG B CA  
3556 C C   . ARG B 197 ? 0.30003 0.10699 0.10289 0.03747  0.01012  -0.00209 193 ARG B C   
3557 O O   . ARG B 197 ? 0.37373 0.15582 0.15464 0.04359  0.01072  -0.00198 193 ARG B O   
3558 C CB  . ARG B 197 ? 0.29502 0.12092 0.11125 0.04308  0.01007  -0.00497 193 ARG B CB  
3559 C CG  . ARG B 197 ? 0.33661 0.13225 0.12540 0.04879  0.01193  -0.00667 193 ARG B CG  
3560 C CD  . ARG B 197 ? 0.32091 0.11072 0.10274 0.04420  0.01361  -0.00899 193 ARG B CD  
3561 N NE  . ARG B 197 ? 0.35003 0.15727 0.14391 0.05331  0.01364  -0.01042 193 ARG B NE  
3562 C CZ  . ARG B 197 ? 0.39426 0.19456 0.17915 0.06768  0.01470  -0.01235 193 ARG B CZ  
3563 N NH1 . ARG B 197 ? 0.40756 0.18794 0.17544 0.07468  0.01435  -0.01101 193 ARG B NH1 
3564 N NH2 . ARG B 197 ? 0.43510 0.25419 0.23224 0.07356  0.01548  -0.01402 193 ARG B NH2 
3565 N N   . TYR B 198 ? 0.29024 0.10491 0.10062 0.02348  0.01085  -0.00163 194 TYR B N   
3566 C CA  . TYR B 198 ? 0.38501 0.18046 0.17850 0.01238  0.01317  -0.00144 194 TYR B CA  
3567 C C   . TYR B 198 ? 0.31260 0.11695 0.11445 0.00886  0.01324  0.00028  194 TYR B C   
3568 O O   . TYR B 198 ? 0.30944 0.10425 0.10177 -0.00277 0.01574  0.00025  194 TYR B O   
3569 C CB  . TYR B 198 ? 0.33233 0.12976 0.12565 -0.00223 0.01446  -0.00307 194 TYR B CB  
3570 C CG  . TYR B 198 ? 0.32272 0.10729 0.10364 -0.00015 0.01480  -0.00505 194 TYR B CG  
3571 C CD1 . TYR B 198 ? 0.42804 0.17912 0.17955 0.00185  0.01683  -0.00607 194 TYR B CD1 
3572 C CD2 . TYR B 198 ? 0.34871 0.15250 0.14521 0.00016  0.01324  -0.00592 194 TYR B CD2 
3573 C CE1 . TYR B 198 ? 0.41138 0.14929 0.15008 0.00430  0.01750  -0.00827 194 TYR B CE1 
3574 C CE2 . TYR B 198 ? 0.36177 0.15348 0.14596 0.00201  0.01393  -0.00796 194 TYR B CE2 
3575 C CZ  . TYR B 198 ? 0.40534 0.16449 0.16101 0.00421  0.01616  -0.00930 194 TYR B CZ  
3576 O OH  . TYR B 198 ? 0.39714 0.14272 0.13899 0.00647  0.01720  -0.01172 194 TYR B OH  
3577 N N   . ASN B 199 ? 0.27560 0.09813 0.09434 0.01781  0.01090  0.00145  195 ASN B N   
3578 C CA  . ASN B 199 ? 0.27926 0.10995 0.10546 0.01599  0.01086  0.00287  195 ASN B CA  
3579 C C   . ASN B 199 ? 0.33353 0.17806 0.17112 0.00210  0.01268  0.00240  195 ASN B C   
3580 O O   . ASN B 199 ? 0.32714 0.16394 0.15643 -0.00630 0.01533  0.00254  195 ASN B O   
3581 C CB  . ASN B 199 ? 0.33228 0.13690 0.13491 0.01886  0.01191  0.00400  195 ASN B CB  
3582 C CG  . ASN B 199 ? 0.31583 0.12896 0.12553 0.01933  0.01149  0.00543  195 ASN B CG  
3583 O OD1 . ASN B 199 ? 0.32683 0.16457 0.15878 0.02140  0.00971  0.00550  195 ASN B OD1 
3584 N ND2 . ASN B 199 ? 0.33410 0.12515 0.12305 0.01696  0.01332  0.00652  195 ASN B ND2 
3585 N N   . ARG B 200 ? 0.23679 0.10254 0.09317 0.00006  0.01126  0.00171  196 ARG B N   
3586 C CA  . ARG B 200 ? 0.22434 0.10687 0.09366 -0.01076 0.01208  0.00099  196 ARG B CA  
3587 C C   . ARG B 200 ? 0.28809 0.19349 0.17896 -0.00669 0.01036  0.00182  196 ARG B C   
3588 O O   . ARG B 200 ? 0.34836 0.25822 0.24539 0.00297  0.00831  0.00279  196 ARG B O   
3589 C CB  . ARG B 200 ? 0.25513 0.14312 0.12730 -0.01649 0.01126  -0.00041 196 ARG B CB  
3590 C CG  . ARG B 200 ? 0.31011 0.17463 0.15955 -0.02332 0.01339  -0.00178 196 ARG B CG  
3591 C CD  . ARG B 200 ? 0.33175 0.20062 0.18273 -0.02747 0.01201  -0.00328 196 ARG B CD  
3592 N NE  . ARG B 200 ? 0.35775 0.20155 0.18462 -0.03435 0.01416  -0.00492 196 ARG B NE  
3593 C CZ  . ARG B 200 ? 0.44129 0.28003 0.26173 -0.03686 0.01339  -0.00650 196 ARG B CZ  
3594 N NH1 . ARG B 200 ? 0.44773 0.30496 0.28388 -0.03317 0.01053  -0.00645 196 ARG B NH1 
3595 N NH2 . ARG B 200 ? 0.52419 0.33672 0.31982 -0.04357 0.01568  -0.00819 196 ARG B NH2 
3596 N N   . ARG B 201 ? 0.25127 0.17134 0.15289 -0.01448 0.01132  0.00109  197 ARG B N   
3597 C CA  . ARG B 201 ? 0.21893 0.15890 0.13912 -0.01129 0.01010  0.00151  197 ARG B CA  
3598 C C   . ARG B 201 ? 0.29530 0.25260 0.22713 -0.01864 0.00991  0.00014  197 ARG B C   
3599 O O   . ARG B 201 ? 0.25473 0.21295 0.18284 -0.02801 0.01264  -0.00136 197 ARG B O   
3600 C CB  . ARG B 201 ? 0.28149 0.21816 0.19878 -0.01074 0.01230  0.00188  197 ARG B CB  
3601 C CG  . ARG B 201 ? 0.28689 0.24145 0.22072 -0.00789 0.01171  0.00186  197 ARG B CG  
3602 C CD  . ARG B 201 ? 0.21834 0.16804 0.14664 -0.00898 0.01463  0.00179  197 ARG B CD  
3603 N NE  . ARG B 201 ? 0.21985 0.18362 0.16171 -0.00478 0.01405  0.00159  197 ARG B NE  
3604 C CZ  . ARG B 201 ? 0.27299 0.23336 0.21402 0.00172  0.01286  0.00242  197 ARG B CZ  
3605 N NH1 . ARG B 201 ? 0.23555 0.18108 0.16397 0.00561  0.01185  0.00358  197 ARG B NH1 
3606 N NH2 . ARG B 201 ? 0.24261 0.21448 0.19482 0.00471  0.01246  0.00190  197 ARG B NH2 
3607 N N   . SER B 202 ? 0.18555 0.15646 0.13028 -0.01473 0.00665  0.00054  198 SER B N   
3608 C CA  . SER B 202 ? 0.20637 0.19366 0.16105 -0.02011 0.00531  -0.00068 198 SER B CA  
3609 C C   . SER B 202 ? 0.15985 0.16005 0.12788 -0.01302 0.00156  0.00049  198 SER B C   
3610 O O   . SER B 202 ? 0.19226 0.18671 0.15923 -0.00664 0.00006  0.00198  198 SER B O   
3611 C CB  . SER B 202 ? 0.26089 0.24152 0.20581 -0.02768 0.00508  -0.00189 198 SER B CB  
3612 O OG  . SER B 202 ? 0.28678 0.25806 0.22637 -0.02245 0.00309  -0.00085 198 SER B OG  
3613 N N   . ALA B 203 ? 0.13118 0.14889 0.11091 -0.01430 0.00014  -0.00036 199 ALA B N   
3614 C CA  . ALA B 203 ? 0.20007 0.22769 0.18980 -0.00763 -0.00368 0.00088  199 ALA B CA  
3615 C C   . ALA B 203 ? 0.21393 0.23999 0.20037 -0.00883 -0.00687 0.00145  199 ALA B C   
3616 O O   . ALA B 203 ? 0.17363 0.19692 0.15338 -0.01600 -0.00651 0.00011  199 ALA B O   
3617 C CB  . ALA B 203 ? 0.19832 0.24478 0.20031 -0.00688 -0.00452 -0.00040 199 ALA B CB  
3618 N N   . PRO B 204 ? 0.13323 0.15950 0.12243 -0.00267 -0.00976 0.00333  200 PRO B N   
3619 C CA  . PRO B 204 ? 0.17860 0.20291 0.16348 -0.00390 -0.01259 0.00394  200 PRO B CA  
3620 C C   . PRO B 204 ? 0.20357 0.24175 0.19326 -0.00766 -0.01590 0.00281  200 PRO B C   
3621 O O   . PRO B 204 ? 0.14830 0.20055 0.14791 -0.00526 -0.01740 0.00235  200 PRO B O   
3622 C CB  . PRO B 204 ? 0.18523 0.20715 0.17190 0.00306  -0.01437 0.00627  200 PRO B CB  
3623 C CG  . PRO B 204 ? 0.14737 0.17539 0.14219 0.00769  -0.01416 0.00656  200 PRO B CG  
3624 C CD  . PRO B 204 ? 0.16512 0.19178 0.15952 0.00474  -0.01033 0.00490  200 PRO B CD  
3625 N N   . ASP B 205 ? 0.20321 0.23807 0.18556 -0.01317 -0.01719 0.00205  201 ASP B N   
3626 C CA  . ASP B 205 ? 0.19241 0.24134 0.17838 -0.01771 -0.02104 0.00067  201 ASP B CA  
3627 C C   . ASP B 205 ? 0.17624 0.23045 0.16528 -0.01120 -0.02632 0.00283  201 ASP B C   
3628 O O   . ASP B 205 ? 0.18018 0.22525 0.16705 -0.00482 -0.02620 0.00529  201 ASP B O   
3629 C CB  . ASP B 205 ? 0.21647 0.25750 0.19091 -0.02748 -0.02013 -0.00136 201 ASP B CB  
3630 C CG  . ASP B 205 ? 0.37365 0.39780 0.33610 -0.02590 -0.01993 -0.00017 201 ASP B CG  
3631 O OD1 . ASP B 205 ? 0.43255 0.45866 0.39576 -0.02147 -0.02340 0.00161  201 ASP B OD1 
3632 O OD2 . ASP B 205 ? 0.57223 0.58053 0.52323 -0.02901 -0.01613 -0.00115 201 ASP B OD2 
3633 N N   . PRO B 206 ? 0.19264 0.26178 0.18600 -0.01286 -0.03120 0.00192  202 PRO B N   
3634 C CA  . PRO B 206 ? 0.16026 0.23246 0.15425 -0.00566 -0.03682 0.00435  202 PRO B CA  
3635 C C   . PRO B 206 ? 0.22750 0.28301 0.20907 -0.00558 -0.03717 0.00645  202 PRO B C   
3636 O O   . PRO B 206 ? 0.18143 0.23300 0.16084 0.00099  -0.03998 0.00923  202 PRO B O   
3637 C CB  . PRO B 206 ? 0.25540 0.34767 0.25505 -0.00888 -0.04217 0.00230  202 PRO B CB  
3638 C CG  . PRO B 206 ? 0.14350 0.24843 0.15117 -0.01512 -0.03880 -0.00109 202 PRO B CG  
3639 C CD  . PRO B 206 ? 0.20318 0.28949 0.20225 -0.02059 -0.03207 -0.00142 202 PRO B CD  
3640 N N   . SER B 207 ? 0.18598 0.23060 0.15789 -0.01261 -0.03414 0.00508  203 SER B N   
3641 C CA  . SER B 207 ? 0.20950 0.23971 0.16987 -0.01206 -0.03373 0.00659  203 SER B CA  
3642 C C   . SER B 207 ? 0.27047 0.29089 0.23068 -0.00586 -0.03030 0.00878  203 SER B C   
3643 O O   . SER B 207 ? 0.25585 0.27001 0.21073 -0.00287 -0.03128 0.01097  203 SER B O   
3644 C CB  . SER B 207 ? 0.21222 0.23182 0.16138 -0.01970 -0.03068 0.00415  203 SER B CB  
3645 O OG  . SER B 207 ? 0.22646 0.23775 0.17468 -0.02019 -0.02510 0.00307  203 SER B OG  
3646 N N   . VAL B 208 ? 0.19052 0.20980 0.15580 -0.00462 -0.02629 0.00811  204 VAL B N   
3647 C CA  . VAL B 208 ? 0.13143 0.14357 0.09724 0.00036  -0.02331 0.00968  204 VAL B CA  
3648 C C   . VAL B 208 ? 0.14696 0.16325 0.11821 0.00616  -0.02613 0.01199  204 VAL B C   
3649 O O   . VAL B 208 ? 0.15590 0.16504 0.12303 0.00870  -0.02574 0.01396  204 VAL B O   
3650 C CB  . VAL B 208 ? 0.16550 0.17502 0.13387 0.00015  -0.01893 0.00822  204 VAL B CB  
3651 C CG1 . VAL B 208 ? 0.13201 0.13826 0.10328 0.00526  -0.01691 0.00959  204 VAL B CG1 
3652 C CG2 . VAL B 208 ? 0.20193 0.20168 0.16074 -0.00375 -0.01587 0.00635  204 VAL B CG2 
3653 N N   . ILE B 209 ? 0.12588 0.15331 0.10542 0.00824  -0.02873 0.01156  205 ILE B N   
3654 C CA  . ILE B 209 ? 0.13909 0.16832 0.12245 0.01530  -0.03110 0.01344  205 ILE B CA  
3655 C C   . ILE B 209 ? 0.17945 0.20428 0.15544 0.01806  -0.03566 0.01601  205 ILE B C   
3656 O O   . ILE B 209 ? 0.17407 0.19023 0.14583 0.02259  -0.03621 0.01836  205 ILE B O   
3657 C CB  . ILE B 209 ? 0.20908 0.25314 0.20317 0.01785  -0.03256 0.01178  205 ILE B CB  
3658 C CG1 . ILE B 209 ? 0.19247 0.23731 0.19128 0.01515  -0.02736 0.00973  205 ILE B CG1 
3659 C CG2 . ILE B 209 ? 0.25405 0.29902 0.25024 0.02687  -0.03569 0.01351  205 ILE B CG2 
3660 C CD1 . ILE B 209 ? 0.35042 0.40971 0.35946 0.01728  -0.02740 0.00783  205 ILE B CD1 
3661 N N   . THR B 210 ? 0.15714 0.18616 0.12954 0.01479  -0.03901 0.01561  206 THR B N   
3662 C CA  . THR B 210 ? 0.18359 0.20764 0.14721 0.01756  -0.04384 0.01824  206 THR B CA  
3663 C C   . THR B 210 ? 0.20335 0.21148 0.15528 0.01481  -0.04063 0.01995  206 THR B C   
3664 O O   . THR B 210 ? 0.20926 0.20780 0.15270 0.01786  -0.04244 0.02285  206 THR B O   
3665 C CB  . THR B 210 ? 0.24782 0.28264 0.21098 0.01469  -0.04897 0.01704  206 THR B CB  
3666 O OG1 . THR B 210 ? 0.24256 0.29508 0.21731 0.01864  -0.05264 0.01563  206 THR B OG1 
3667 C CG2 . THR B 210 ? 0.16843 0.19550 0.11932 0.01667  -0.05388 0.01988  206 THR B CG2 
3668 N N   . LEU B 211 ? 0.15250 0.15726 0.10299 0.00926  -0.03558 0.01806  207 LEU B N   
3669 C CA  . LEU B 211 ? 0.15916 0.15237 0.10102 0.00727  -0.03154 0.01898  207 LEU B CA  
3670 C C   . LEU B 211 ? 0.18276 0.17069 0.12602 0.01037  -0.02938 0.02059  207 LEU B C   
3671 O O   . LEU B 211 ? 0.19879 0.17742 0.13318 0.00985  -0.02879 0.02271  207 LEU B O   
3672 C CB  . LEU B 211 ? 0.19079 0.18276 0.13215 0.00310  -0.02644 0.01618  207 LEU B CB  
3673 C CG  . LEU B 211 ? 0.19931 0.18892 0.13234 -0.00150 -0.02664 0.01455  207 LEU B CG  
3674 C CD1 . LEU B 211 ? 0.22768 0.21385 0.15982 -0.00335 -0.02128 0.01170  207 LEU B CD1 
3675 C CD2 . LEU B 211 ? 0.16974 0.15171 0.09104 -0.00270 -0.02706 0.01627  207 LEU B CD2 
3676 N N   . GLU B 212 ? 0.14767 0.14057 0.10065 0.01271  -0.02794 0.01947  208 GLU B N   
3677 C CA  . GLU B 212 ? 0.21556 0.20312 0.16923 0.01517  -0.02622 0.02061  208 GLU B CA  
3678 C C   . GLU B 212 ? 0.23094 0.21112 0.17760 0.01923  -0.03032 0.02358  208 GLU B C   
3679 O O   . GLU B 212 ? 0.21083 0.17976 0.14914 0.01818  -0.02885 0.02534  208 GLU B O   
3680 C CB  . GLU B 212 ? 0.18150 0.17577 0.14581 0.01749  -0.02482 0.01882  208 GLU B CB  
3681 C CG  . GLU B 212 ? 0.12620 0.12335 0.09437 0.01434  -0.02050 0.01638  208 GLU B CG  
3682 C CD  . GLU B 212 ? 0.22734 0.23011 0.20400 0.01617  -0.01941 0.01480  208 GLU B CD  
3683 O OE1 . GLU B 212 ? 0.22117 0.22713 0.20191 0.01988  -0.02152 0.01524  208 GLU B OE1 
3684 O OE2 . GLU B 212 ? 0.19172 0.19507 0.16989 0.01440  -0.01635 0.01306  208 GLU B OE2 
3685 N N   . ASN B 213 ? 0.16502 0.15124 0.11392 0.02382  -0.03558 0.02405  209 ASN B N   
3686 C CA  . ASN B 213 ? 0.17171 0.15022 0.11293 0.03007  -0.04028 0.02689  209 ASN B CA  
3687 C C   . ASN B 213 ? 0.18646 0.15229 0.11210 0.02767  -0.04188 0.02971  209 ASN B C   
3688 O O   . ASN B 213 ? 0.24701 0.19925 0.16127 0.03148  -0.04421 0.03262  209 ASN B O   
3689 C CB  . ASN B 213 ? 0.18934 0.18131 0.13808 0.03658  -0.04598 0.02621  209 ASN B CB  
3690 C CG  . ASN B 213 ? 0.22751 0.23094 0.18996 0.03971  -0.04421 0.02364  209 ASN B CG  
3691 O OD1 . ASN B 213 ? 0.19793 0.19570 0.16201 0.03890  -0.03974 0.02308  209 ASN B OD1 
3692 N ND2 . ASN B 213 ? 0.24235 0.26294 0.21445 0.04288  -0.04768 0.02184  209 ASN B ND2 
3693 N N   . SER B 214 ? 0.21455 0.18260 0.13751 0.02148  -0.04045 0.02887  210 SER B N   
3694 C CA  . SER B 214 ? 0.19981 0.15724 0.10749 0.01897  -0.04213 0.03127  210 SER B CA  
3695 C C   . SER B 214 ? 0.26205 0.20944 0.16143 0.01188  -0.03571 0.03147  210 SER B C   
3696 O O   . SER B 214 ? 0.24709 0.18567 0.13303 0.00845  -0.03581 0.03313  210 SER B O   
3697 C CB  . SER B 214 ? 0.24684 0.21339 0.15497 0.01680  -0.04530 0.02994  210 SER B CB  
3698 O OG  . SER B 214 ? 0.26548 0.24573 0.18338 0.02191  -0.05085 0.02895  210 SER B OG  
3699 N N   . TRP B 215 ? 0.19684 0.14660 0.10377 0.00951  -0.03018 0.02964  211 TRP B N   
3700 C CA  . TRP B 215 ? 0.25811 0.20400 0.16016 0.00263  -0.02386 0.02887  211 TRP B CA  
3701 C C   . TRP B 215 ? 0.23953 0.16929 0.12468 -0.00057 -0.02345 0.03204  211 TRP B C   
3702 O O   . TRP B 215 ? 0.24621 0.17212 0.12202 -0.00653 -0.02012 0.03214  211 TRP B O   
3703 C CB  . TRP B 215 ? 0.20783 0.16019 0.12098 0.00170  -0.01930 0.02647  211 TRP B CB  
3704 C CG  . TRP B 215 ? 0.21871 0.17239 0.12978 -0.00475 -0.01296 0.02488  211 TRP B CG  
3705 C CD1 . TRP B 215 ? 0.19698 0.15747 0.10912 -0.00726 -0.00949 0.02253  211 TRP B CD1 
3706 C CD2 . TRP B 215 ? 0.19323 0.14245 0.10063 -0.00954 -0.00923 0.02507  211 TRP B CD2 
3707 N NE1 . TRP B 215 ? 0.20067 0.16380 0.11171 -0.01236 -0.00382 0.02111  211 TRP B NE1 
3708 C CE2 . TRP B 215 ? 0.18527 0.14235 0.09373 -0.01476 -0.00358 0.02259  211 TRP B CE2 
3709 C CE3 . TRP B 215 ? 0.26571 0.20488 0.16827 -0.01016 -0.01000 0.02678  211 TRP B CE3 
3710 C CZ2 . TRP B 215 ? 0.18926 0.14770 0.09589 -0.02140 0.00123  0.02159  211 TRP B CZ2 
3711 C CZ3 . TRP B 215 ? 0.26911 0.20641 0.16783 -0.01767 -0.00522 0.02596  211 TRP B CZ3 
3712 C CH2 . TRP B 215 ? 0.22730 0.17580 0.12898 -0.02363 0.00030  0.02330  211 TRP B CH2 
3713 N N   . GLY B 216 ? 0.22878 0.14760 0.10818 0.00320  -0.02643 0.03455  212 GLY B N   
3714 C CA  . GLY B 216 ? 0.33883 0.23807 0.19848 0.00001  -0.02634 0.03793  212 GLY B CA  
3715 C C   . GLY B 216 ? 0.30967 0.20134 0.15543 0.00091  -0.03057 0.04057  212 GLY B C   
3716 O O   . GLY B 216 ? 0.30053 0.18084 0.13076 -0.00583 -0.02774 0.04212  212 GLY B O   
3717 N N   . ARG B 217 ? 0.32397 0.22281 0.17485 0.00873  -0.03737 0.04092  213 ARG B N   
3718 C CA  . ARG B 217 ? 0.29594 0.18911 0.13381 0.01025  -0.04266 0.04329  213 ARG B CA  
3719 C C   . ARG B 217 ? 0.36264 0.26191 0.19931 0.00259  -0.03885 0.04131  213 ARG B C   
3720 O O   . ARG B 217 ? 0.29614 0.18450 0.11587 -0.00057 -0.03971 0.04344  213 ARG B O   
3721 C CB  . ARG B 217 ? 0.36366 0.26790 0.21002 0.01999  -0.05097 0.04327  213 ARG B CB  
3722 C CG  . ARG B 217 ? 0.53219 0.42568 0.37156 0.02995  -0.05673 0.04628  213 ARG B CG  
3723 C CD  . ARG B 217 ? 0.59938 0.51088 0.45215 0.03943  -0.06388 0.04495  213 ARG B CD  
3724 N NE  . ARG B 217 ? 0.63596 0.56536 0.50914 0.04099  -0.06218 0.04149  213 ARG B NE  
3725 C CZ  . ARG B 217 ? 0.67277 0.61863 0.55896 0.04914  -0.06714 0.03995  213 ARG B CZ  
3726 N NH1 . ARG B 217 ? 0.82825 0.77822 0.71279 0.05642  -0.07352 0.04098  213 ARG B NH1 
3727 N NH2 . ARG B 217 ? 0.41862 0.37997 0.32312 0.04837  -0.06363 0.03641  213 ARG B NH2 
3728 N N   . LEU B 218 ? 0.25471 0.16990 0.10753 0.00009  -0.03466 0.03721  214 LEU B N   
3729 C CA  . LEU B 218 ? 0.31938 0.23888 0.17004 -0.00612 -0.03039 0.03484  214 LEU B CA  
3730 C C   . LEU B 218 ? 0.27434 0.18517 0.11439 -0.01368 -0.02308 0.03509  214 LEU B C   
3731 O O   . LEU B 218 ? 0.29804 0.20440 0.12630 -0.01846 -0.02087 0.03505  214 LEU B O   
3732 C CB  . LEU B 218 ? 0.22611 0.16148 0.09415 -0.00599 -0.02751 0.03048  214 LEU B CB  
3733 C CG  . LEU B 218 ? 0.25700 0.20282 0.13425 -0.00185 -0.03329 0.02919  214 LEU B CG  
3734 C CD1 . LEU B 218 ? 0.28620 0.24333 0.17843 -0.00217 -0.02941 0.02536  214 LEU B CD1 
3735 C CD2 . LEU B 218 ? 0.29292 0.23733 0.15990 -0.00415 -0.03672 0.02908  214 LEU B CD2 
3736 N N   . SER B 219 ? 0.25255 0.16202 0.09657 -0.01558 -0.01896 0.03495  215 SER B N   
3737 C CA  . SER B 219 ? 0.26234 0.16584 0.09684 -0.02418 -0.01182 0.03483  215 SER B CA  
3738 C C   . SER B 219 ? 0.32339 0.20702 0.13430 -0.02756 -0.01352 0.03901  215 SER B C   
3739 O O   . SER B 219 ? 0.29924 0.17928 0.09876 -0.03484 -0.00861 0.03869  215 SER B O   
3740 C CB  . SER B 219 ? 0.27825 0.18311 0.11997 -0.02613 -0.00842 0.03408  215 SER B CB  
3741 O OG  . SER B 219 ? 0.25322 0.17549 0.11516 -0.02275 -0.00705 0.03041  215 SER B OG  
3742 N N   . THR B 220 ? 0.30029 0.17038 0.10257 -0.02168 -0.02050 0.04290  216 THR B N   
3743 C CA  . THR B 220 ? 0.32659 0.17673 0.10733 -0.02304 -0.02281 0.04657  216 THR B CA  
3744 C C   . THR B 220 ? 0.39370 0.24634 0.16933 -0.02265 -0.02531 0.04628  216 THR B C   
3745 O O   . THR B 220 ? 0.40219 0.24592 0.16499 -0.02870 -0.02201 0.04653  216 THR B O   
3746 C CB  . THR B 220 ? 0.34131 0.18097 0.12012 -0.01374 -0.02980 0.04906  216 THR B CB  
3747 O OG1 . THR B 220 ? 0.34867 0.18247 0.12900 -0.01539 -0.02671 0.04904  216 THR B OG1 
3748 C CG2 . THR B 220 ? 0.46759 0.28972 0.22903 -0.01311 -0.03241 0.05130  216 THR B CG2 
3749 N N   . ALA B 221 ? 0.31941 0.18412 0.10453 -0.01623 -0.03112 0.04546  217 ALA B N   
3750 C CA  . ALA B 221 ? 0.35040 0.21748 0.13038 -0.01606 -0.03427 0.04494  217 ALA B CA  
3751 C C   . ALA B 221 ? 0.33608 0.20587 0.11156 -0.02494 -0.02637 0.04220  217 ALA B C   
3752 O O   . ALA B 221 ? 0.35337 0.21654 0.11721 -0.02815 -0.02570 0.04239  217 ALA B O   
3753 C CB  . ALA B 221 ? 0.32126 0.20279 0.11340 -0.00932 -0.04149 0.04372  217 ALA B CB  
3754 N N   . ILE B 222 ? 0.30955 0.19010 0.09524 -0.02824 -0.02001 0.03916  218 ILE B N   
3755 C CA  . ILE B 222 ? 0.33849 0.22452 0.12230 -0.03489 -0.01186 0.03561  218 ILE B CA  
3756 C C   . ILE B 222 ? 0.37843 0.25492 0.14979 -0.04287 -0.00507 0.03642  218 ILE B C   
3757 O O   . ILE B 222 ? 0.37190 0.24667 0.13493 -0.04741 -0.00110 0.03491  218 ILE B O   
3758 C CB  . ILE B 222 ? 0.34209 0.24633 0.14745 -0.03358 -0.00670 0.03068  218 ILE B CB  
3759 C CG1 . ILE B 222 ? 0.27169 0.18513 0.08924 -0.02721 -0.01235 0.02887  218 ILE B CG1 
3760 C CG2 . ILE B 222 ? 0.29112 0.20156 0.09454 -0.03908 0.00252  0.02677  218 ILE B CG2 
3761 C CD1 . ILE B 222 ? 0.25065 0.17827 0.08792 -0.02446 -0.00893 0.02511  218 ILE B CD1 
3762 N N   . GLN B 223 ? 0.32842 0.19891 0.09939 -0.04499 -0.00351 0.03822  219 GLN B N   
3763 C CA  . GLN B 223 ? 0.34292 0.20692 0.10487 -0.05422 0.00376  0.03783  219 GLN B CA  
3764 C C   . GLN B 223 ? 0.36761 0.21318 0.11224 -0.05533 0.00049  0.04066  219 GLN B C   
3765 O O   . GLN B 223 ? 0.41370 0.25471 0.14873 -0.06352 0.00652  0.03961  219 GLN B O   
3766 C CB  . GLN B 223 ? 0.33978 0.20318 0.10627 -0.05764 0.00676  0.03814  219 GLN B CB  
3767 C CG  . GLN B 223 ? 0.31743 0.20140 0.10098 -0.05858 0.01214  0.03437  219 GLN B CG  
3768 C CD  . GLN B 223 ? 0.40775 0.29316 0.19899 -0.06098 0.01378  0.03415  219 GLN B CD  
3769 O OE1 . GLN B 223 ? 0.37857 0.25245 0.15803 -0.06915 0.01692  0.03544  219 GLN B OE1 
3770 N NE2 . GLN B 223 ? 0.28995 0.18950 0.10197 -0.05391 0.01150  0.03188  219 GLN B NE2 
3771 N N   . GLU B 224 ? 0.37371 0.20978 0.11435 -0.04704 -0.00884 0.04389  220 GLU B N   
3772 C CA  . GLU B 224 ? 0.39832 0.21708 0.12200 -0.04639 -0.01289 0.04659  220 GLU B CA  
3773 C C   . GLU B 224 ? 0.43039 0.25256 0.15028 -0.04417 -0.01628 0.04611  220 GLU B C   
3774 O O   . GLU B 224 ? 0.43737 0.24629 0.14302 -0.04304 -0.02031 0.04837  220 GLU B O   
3775 C CB  . GLU B 224 ? 0.40605 0.21339 0.12702 -0.03744 -0.02123 0.05002  220 GLU B CB  
3776 C CG  . GLU B 224 ? 0.48729 0.28569 0.20746 -0.03961 -0.01853 0.05061  220 GLU B CG  
3777 C CD  . GLU B 224 ? 0.65406 0.43924 0.36927 -0.02961 -0.02650 0.05354  220 GLU B CD  
3778 O OE1 . GLU B 224 ? 0.68179 0.46900 0.39741 -0.02042 -0.03428 0.05500  220 GLU B OE1 
3779 O OE2 . GLU B 224 ? 0.57834 0.35186 0.28921 -0.03086 -0.02490 0.05398  220 GLU B OE2 
3780 N N   . SER B 225 ? 0.39359 0.25187 0.14164 -0.04125 -0.02592 0.05491  221 SER B N   
3781 C CA  . SER B 225 ? 0.39589 0.26769 0.13855 -0.04334 -0.02946 0.05230  221 SER B CA  
3782 C C   . SER B 225 ? 0.58498 0.45459 0.30415 -0.05514 -0.02663 0.05485  221 SER B C   
3783 O O   . SER B 225 ? 0.48855 0.35011 0.19897 -0.06299 -0.01907 0.05579  221 SER B O   
3784 C CB  . SER B 225 ? 0.47305 0.36166 0.23326 -0.04304 -0.02391 0.04024  221 SER B CB  
3785 O OG  . SER B 225 ? 0.43487 0.32513 0.19605 -0.05108 -0.01272 0.03355  221 SER B OG  
3786 N N   . ASN B 226 ? 0.46350 0.34146 0.17228 -0.05703 -0.03267 0.05560  222 ASN B N   
3787 C CA  . ASN B 226 ? 0.56663 0.44765 0.25686 -0.06808 -0.02942 0.05541  222 ASN B CA  
3788 C C   . ASN B 226 ? 0.55035 0.44562 0.24562 -0.07449 -0.01960 0.04204  222 ASN B C   
3789 O O   . ASN B 226 ? 0.52542 0.43329 0.22257 -0.07435 -0.02243 0.03632  222 ASN B O   
3790 C CB  . ASN B 226 ? 0.46359 0.34836 0.14497 -0.06598 -0.04071 0.06183  222 ASN B CB  
3791 C CG  . ASN B 226 ? 0.78163 0.66871 0.44740 -0.07612 -0.03747 0.06252  222 ASN B CG  
3792 O OD1 . ASN B 226 ? 0.71027 0.60050 0.37367 -0.08496 -0.02615 0.05544  222 ASN B OD1 
3793 N ND2 . ASN B 226 ? 0.89244 0.77851 0.54804 -0.07479 -0.04751 0.07082  222 ASN B ND2 
3794 N N   . GLN B 227 ? 0.47606 0.36958 0.17530 -0.07993 -0.00799 0.03654  223 GLN B N   
3795 C CA  . GLN B 227 ? 0.50599 0.41239 0.21451 -0.08492 0.00238  0.02303  223 GLN B CA  
3796 C C   . GLN B 227 ? 0.47519 0.39248 0.20614 -0.07653 -0.00022 0.01550  223 GLN B C   
3797 O O   . GLN B 227 ? 0.46039 0.38937 0.19436 -0.07931 0.00215  0.00630  223 GLN B O   
3798 C CB  . GLN B 227 ? 0.66907 0.58440 0.36675 -0.09352 0.00570  0.01856  223 GLN B CB  
3799 C CG  . GLN B 227 ? 0.74874 0.67381 0.45464 -0.10010 0.01865  0.00531  223 GLN B CG  
3800 C CD  . GLN B 227 ? 0.79769 0.71723 0.50464 -0.10534 0.02801  0.00564  223 GLN B CD  
3801 O OE1 . GLN B 227 ? 0.75412 0.67061 0.47305 -0.10277 0.03249  0.00363  223 GLN B OE1 
3802 N NE2 . GLN B 227 ? 0.62520 0.54392 0.31963 -0.11322 0.03090  0.00809  223 GLN B NE2 
3803 N N   . GLY B 228 ? 0.45781 0.37079 0.20416 -0.06675 -0.00488 0.01918  224 GLY B N   
3804 C CA  . GLY B 228 ? 0.38514 0.30744 0.15246 -0.05934 -0.00711 0.01317  224 GLY B CA  
3805 C C   . GLY B 228 ? 0.35208 0.27849 0.12012 -0.05248 -0.01858 0.01762  224 GLY B C   
3806 O O   . GLY B 228 ? 0.35612 0.28784 0.14206 -0.04512 -0.02128 0.01518  224 GLY B O   
3807 N N   . ALA B 229 ? 0.37336 0.29828 0.12264 -0.05506 -0.02553 0.02410  225 ALA B N   
3808 C CA  . ALA B 229 ? 0.37663 0.30677 0.12734 -0.04839 -0.03741 0.02872  225 ALA B CA  
3809 C C   . ALA B 229 ? 0.41514 0.33441 0.17050 -0.03890 -0.04414 0.03838  225 ALA B C   
3810 O O   . ALA B 229 ? 0.47320 0.37803 0.21524 -0.04042 -0.04483 0.04673  225 ALA B O   
3811 C CB  . ALA B 229 ? 0.40045 0.33324 0.12883 -0.05498 -0.04336 0.03244  225 ALA B CB  
3812 N N   . PHE B 230 ? 0.36356 0.28955 0.13782 -0.02948 -0.04876 0.03686  226 PHE B N   
3813 C CA  . PHE B 230 ? 0.46917 0.38608 0.25070 -0.01955 -0.05443 0.04403  226 PHE B CA  
3814 C C   . PHE B 230 ? 0.44038 0.35184 0.20835 -0.01648 -0.06623 0.05475  226 PHE B C   
3815 O O   . PHE B 230 ? 0.43646 0.35815 0.19795 -0.01834 -0.07301 0.05533  226 PHE B O   
3816 C CB  . PHE B 230 ? 0.35520 0.28325 0.16023 -0.01097 -0.05596 0.03871  226 PHE B CB  
3817 C CG  . PHE B 230 ? 0.36589 0.29581 0.18502 -0.01231 -0.04595 0.03053  226 PHE B CG  
3818 C CD1 . PHE B 230 ? 0.37047 0.29237 0.18352 -0.01938 -0.03685 0.02845  226 PHE B CD1 
3819 C CD2 . PHE B 230 ? 0.34344 0.28367 0.18213 -0.00675 -0.04596 0.02522  226 PHE B CD2 
3820 C CE1 . PHE B 230 ? 0.32758 0.25151 0.15431 -0.02025 -0.02897 0.02161  226 PHE B CE1 
3821 C CE2 . PHE B 230 ? 0.30438 0.24564 0.15476 -0.00839 -0.03781 0.01878  226 PHE B CE2 
3822 C CZ  . PHE B 230 ? 0.32882 0.26170 0.17344 -0.01479 -0.02983 0.01721  226 PHE B CZ  
3823 N N   . ALA B 231 ? 0.49990 0.39460 0.26378 -0.01178 -0.06928 0.06342  227 ALA B N   
3824 C CA  . ALA B 231 ? 0.60527 0.49286 0.35896 -0.00691 -0.08190 0.07462  227 ALA B CA  
3825 C C   . ALA B 231 ? 0.68598 0.58557 0.45866 0.00497  -0.09112 0.07395  227 ALA B C   
3826 O O   . ALA B 231 ? 0.62876 0.53368 0.39631 0.00760  -0.10246 0.07963  227 ALA B O   
3827 C CB  . ALA B 231 ? 0.48953 0.35396 0.23461 -0.00511 -0.08243 0.08376  227 ALA B CB  
3828 N N   . SER B 232 ? 0.42384 0.32864 0.21853 0.01183  -0.08648 0.06701  228 SER B N   
3829 C CA  . SER B 232 ? 0.58687 0.50626 0.40241 0.02202  -0.09247 0.06386  228 SER B CA  
3830 C C   . SER B 232 ? 0.43102 0.36611 0.26261 0.01959  -0.08383 0.05201  228 SER B C   
3831 O O   . SER B 232 ? 0.48707 0.41674 0.31954 0.01479  -0.07344 0.04718  228 SER B O   
3832 C CB  . SER B 232 ? 0.63516 0.54369 0.46247 0.03399  -0.09587 0.06771  228 SER B CB  
3833 O OG  . SER B 232 ? 0.75706 0.65352 0.57355 0.03864  -0.10704 0.07909  228 SER B OG  
3834 N N   . PRO B 233 ? 0.42767 0.38211 0.27205 0.02234  -0.08823 0.04749  229 PRO B N   
3835 C CA  . PRO B 233 ? 0.40171 0.36999 0.26109 0.01960  -0.08058 0.03697  229 PRO B CA  
3836 C C   . PRO B 233 ? 0.46406 0.43050 0.34098 0.02669  -0.07570 0.03358  229 PRO B C   
3837 O O   . PRO B 233 ? 0.45311 0.41310 0.33577 0.03594  -0.07993 0.03779  229 PRO B O   
3838 C CB  . PRO B 233 ? 0.43298 0.42170 0.30008 0.02057  -0.08825 0.03452  229 PRO B CB  
3839 C CG  . PRO B 233 ? 0.34814 0.33506 0.21319 0.02885  -0.10045 0.04342  229 PRO B CG  
3840 C CD  . PRO B 233 ? 0.48001 0.44492 0.32466 0.02683  -0.10089 0.05215  229 PRO B CD  
3841 N N   . ILE B 234 ? 0.39943 0.37120 0.28460 0.02203  -0.06677 0.02568  230 ILE B N   
3842 C CA  . ILE B 234 ? 0.35153 0.32280 0.25160 0.02644  -0.06113 0.02154  230 ILE B CA  
3843 C C   . ILE B 234 ? 0.40084 0.39189 0.31721 0.02616  -0.06028 0.01430  230 ILE B C   
3844 O O   . ILE B 234 ? 0.39853 0.39771 0.31356 0.01848  -0.05794 0.00997  230 ILE B O   
3845 C CB  . ILE B 234 ? 0.36480 0.32329 0.25962 0.02052  -0.05151 0.01963  230 ILE B CB  
3846 C CG1 . ILE B 234 ? 0.47286 0.41201 0.35160 0.01977  -0.05192 0.02681  230 ILE B CG1 
3847 C CG2 . ILE B 234 ? 0.46405 0.42312 0.37308 0.02407  -0.04623 0.01520  230 ILE B CG2 
3848 C CD1 . ILE B 234 ? 0.50877 0.43713 0.38997 0.02925  -0.05638 0.03203  230 ILE B CD1 
3849 N N   . GLN B 235 ? 0.25841 0.25696 0.19021 0.03417  -0.06186 0.01263  231 GLN B N   
3850 C CA  . GLN B 235 ? 0.38464 0.40251 0.33255 0.03357  -0.06053 0.00591  231 GLN B CA  
3851 C C   . GLN B 235 ? 0.30878 0.32432 0.26186 0.02904  -0.05089 0.00060  231 GLN B C   
3852 O O   . GLN B 235 ? 0.33370 0.33886 0.28811 0.03254  -0.04691 0.00091  231 GLN B O   
3853 C CB  . GLN B 235 ? 0.40494 0.43383 0.36812 0.04399  -0.06596 0.00581  231 GLN B CB  
3854 C CG  . GLN B 235 ? 0.44853 0.47854 0.40774 0.04990  -0.07695 0.01224  231 GLN B CG  
3855 C CD  . GLN B 235 ? 0.52200 0.56092 0.47250 0.04239  -0.08166 0.01289  231 GLN B CD  
3856 O OE1 . GLN B 235 ? 0.59816 0.65361 0.55683 0.03733  -0.08044 0.00710  231 GLN B OE1 
3857 N NE2 . GLN B 235 ? 0.63070 0.65819 0.56353 0.04074  -0.08683 0.01978  231 GLN B NE2 
3858 N N   . LEU B 236 ? 0.25947 0.28392 0.21500 0.02103  -0.04766 -0.00409 232 LEU B N   
3859 C CA  . LEU B 236 ? 0.24567 0.26987 0.20707 0.01626  -0.03996 -0.00863 232 LEU B CA  
3860 C C   . LEU B 236 ? 0.22726 0.27047 0.20221 0.01398  -0.04003 -0.01371 232 LEU B C   
3861 O O   . LEU B 236 ? 0.28209 0.33883 0.26143 0.01498  -0.04574 -0.01424 232 LEU B O   
3862 C CB  . LEU B 236 ? 0.19994 0.21391 0.15145 0.00791  -0.03543 -0.00915 232 LEU B CB  
3863 C CG  . LEU B 236 ? 0.24894 0.24494 0.18761 0.00840  -0.03379 -0.00477 232 LEU B CG  
3864 C CD1 . LEU B 236 ? 0.23778 0.22722 0.16996 0.00022  -0.02887 -0.00666 232 LEU B CD1 
3865 C CD2 . LEU B 236 ? 0.27571 0.26234 0.21703 0.01339  -0.03090 -0.00339 232 LEU B CD2 
3866 N N   . GLN B 237 ? 0.23312 0.27762 0.21434 0.01020  -0.03390 -0.01719 233 GLN B N   
3867 C CA  . GLN B 237 ? 0.20074 0.26234 0.19429 0.00690  -0.03289 -0.02174 233 GLN B CA  
3868 C C   . GLN B 237 ? 0.22876 0.28928 0.22074 -0.00338 -0.02939 -0.02411 233 GLN B C   
3869 O O   . GLN B 237 ? 0.16714 0.21384 0.15231 -0.00685 -0.02560 -0.02309 233 GLN B O   
3870 C CB  . GLN B 237 ? 0.19053 0.25652 0.19354 0.01075  -0.02876 -0.02402 233 GLN B CB  
3871 C CG  . GLN B 237 ? 0.25686 0.33392 0.26975 0.02045  -0.03264 -0.02460 233 GLN B CG  
3872 C CD  . GLN B 237 ? 0.22550 0.31057 0.24945 0.02294  -0.02737 -0.02903 233 GLN B CD  
3873 O OE1 . GLN B 237 ? 0.35745 0.46172 0.39476 0.02441  -0.02793 -0.03291 233 GLN B OE1 
3874 N NE2 . GLN B 237 ? 0.32829 0.39954 0.34669 0.02289  -0.02199 -0.02894 233 GLN B NE2 
3875 N N   . ARG B 238 ? 0.16628 0.24162 0.16560 -0.00820 -0.03105 -0.02733 234 ARG B N   
3876 C CA  . ARG B 238 ? 0.16121 0.23636 0.16140 -0.01795 -0.02813 -0.02984 234 ARG B CA  
3877 C C   . ARG B 238 ? 0.15533 0.23404 0.16259 -0.02074 -0.02312 -0.03116 234 ARG B C   
3878 O O   . ARG B 238 ? 0.17071 0.25327 0.18236 -0.01520 -0.02140 -0.03122 234 ARG B O   
3879 C CB  . ARG B 238 ? 0.19964 0.28807 0.20363 -0.02289 -0.03227 -0.03274 234 ARG B CB  
3880 C CG  . ARG B 238 ? 0.18673 0.27244 0.18185 -0.02145 -0.03743 -0.03177 234 ARG B CG  
3881 C CD  . ARG B 238 ? 0.20837 0.30624 0.20613 -0.02800 -0.04130 -0.03546 234 ARG B CD  
3882 N NE  . ARG B 238 ? 0.22399 0.31886 0.21110 -0.02767 -0.04599 -0.03482 234 ARG B NE  
3883 C CZ  . ARG B 238 ? 0.27822 0.36004 0.25453 -0.03197 -0.04394 -0.03586 234 ARG B CZ  
3884 N NH1 . ARG B 238 ? 0.19190 0.26235 0.16815 -0.03629 -0.03807 -0.03743 234 ARG B NH1 
3885 N NH2 . ARG B 238 ? 0.26382 0.34441 0.22930 -0.03202 -0.04800 -0.03539 234 ARG B NH2 
3886 N N   . ARG B 239 ? 0.17654 0.25332 0.18443 -0.02972 -0.02074 -0.03233 235 ARG B N   
3887 C CA  . ARG B 239 ? 0.16707 0.24657 0.17938 -0.03391 -0.01626 -0.03280 235 ARG B CA  
3888 C C   . ARG B 239 ? 0.19406 0.29400 0.21719 -0.03358 -0.01592 -0.03587 235 ARG B C   
3889 O O   . ARG B 239 ? 0.18995 0.29430 0.21650 -0.03343 -0.01170 -0.03677 235 ARG B O   
3890 C CB  . ARG B 239 ? 0.26455 0.33702 0.27519 -0.04395 -0.01499 -0.03248 235 ARG B CB  
3891 C CG  . ARG B 239 ? 0.24866 0.30182 0.25145 -0.04433 -0.01414 -0.02985 235 ARG B CG  
3892 C CD  . ARG B 239 ? 0.35605 0.40254 0.35948 -0.05354 -0.01348 -0.02924 235 ARG B CD  
3893 N NE  . ARG B 239 ? 0.27347 0.30340 0.27220 -0.05349 -0.01345 -0.02758 235 ARG B NE  
3894 C CZ  . ARG B 239 ? 0.38669 0.40631 0.38261 -0.05289 -0.01164 -0.02449 235 ARG B CZ  
3895 N NH1 . ARG B 239 ? 0.45750 0.48024 0.45300 -0.05272 -0.00949 -0.02281 235 ARG B NH1 
3896 N NH2 . ARG B 239 ? 0.42659 0.43327 0.42043 -0.05269 -0.01191 -0.02360 235 ARG B NH2 
3897 N N   . ASN B 240 ? 0.23383 0.34738 0.26269 -0.03375 -0.02013 -0.03799 236 ASN B N   
3898 C CA  . ASN B 240 ? 0.23185 0.36745 0.27325 -0.03351 -0.02015 -0.04143 236 ASN B CA  
3899 C C   . ASN B 240 ? 0.26889 0.41238 0.31619 -0.02153 -0.02218 -0.04191 236 ASN B C   
3900 O O   . ASN B 240 ? 0.26527 0.42890 0.32525 -0.01946 -0.02300 -0.04523 236 ASN B O   
3901 C CB  . ASN B 240 ? 0.18035 0.32844 0.22657 -0.04009 -0.02428 -0.04375 236 ASN B CB  
3902 C CG  . ASN B 240 ? 0.34171 0.48941 0.38436 -0.03498 -0.03120 -0.04301 236 ASN B CG  
3903 O OD1 . ASN B 240 ? 0.29194 0.42984 0.32827 -0.02651 -0.03306 -0.04019 236 ASN B OD1 
3904 N ND2 . ASN B 240 ? 0.35609 0.51446 0.40195 -0.04100 -0.03520 -0.04548 236 ASN B ND2 
3905 N N   . GLY B 241 ? 0.18756 0.31572 0.22677 -0.01369 -0.02319 -0.03872 237 GLY B N   
3906 C CA  . GLY B 241 ? 0.19750 0.32927 0.24156 -0.00199 -0.02546 -0.03850 237 GLY B CA  
3907 C C   . GLY B 241 ? 0.28007 0.41653 0.32461 0.00392  -0.03377 -0.03657 237 GLY B C   
3908 O O   . GLY B 241 ? 0.29396 0.42948 0.34092 0.01434  -0.03694 -0.03497 237 GLY B O   
3909 N N   . SER B 242 ? 0.25872 0.39956 0.30060 -0.00251 -0.03781 -0.03660 238 SER B N   
3910 C CA  . SER B 242 ? 0.17686 0.32158 0.21669 0.00210  -0.04627 -0.03437 238 SER B CA  
3911 C C   . SER B 242 ? 0.27502 0.39830 0.29913 0.00599  -0.04789 -0.02921 238 SER B C   
3912 O O   . SER B 242 ? 0.26424 0.37079 0.27867 0.00225  -0.04278 -0.02815 238 SER B O   
3913 C CB  . SER B 242 ? 0.29441 0.44928 0.33429 -0.00701 -0.04981 -0.03665 238 SER B CB  
3914 O OG  . SER B 242 ? 0.28317 0.42373 0.31219 -0.01606 -0.04610 -0.03695 238 SER B OG  
3915 N N   . LYS B 243 ? 0.21443 0.33872 0.23629 0.01328  -0.05535 -0.02570 239 LYS B N   
3916 C CA  . LYS B 243 ? 0.30057 0.40544 0.30765 0.01739  -0.05724 -0.02012 239 LYS B CA  
3917 C C   . LYS B 243 ? 0.39453 0.49508 0.38798 0.01116  -0.06127 -0.01850 239 LYS B C   
3918 O O   . LYS B 243 ? 0.24590 0.36054 0.24245 0.00689  -0.06582 -0.02079 239 LYS B O   
3919 C CB  . LYS B 243 ? 0.26774 0.37351 0.27920 0.02943  -0.06331 -0.01625 239 LYS B CB  
3920 C CG  . LYS B 243 ? 0.48647 0.60526 0.51651 0.03638  -0.06118 -0.02002 239 LYS B CG  
3921 C CD  . LYS B 243 ? 0.42408 0.52985 0.45308 0.03737  -0.05237 -0.02147 239 LYS B CD  
3922 C CE  . LYS B 243 ? 0.43258 0.55123 0.47915 0.04443  -0.04965 -0.02616 239 LYS B CE  
3923 N NZ  . LYS B 243 ? 0.40239 0.54405 0.46264 0.03846  -0.04701 -0.03224 239 LYS B NZ  
3924 N N   . PHE B 244 ? 0.27497 0.35640 0.25312 0.01010  -0.05924 -0.01505 240 PHE B N   
3925 C CA  . PHE B 244 ? 0.29003 0.36656 0.25347 0.00504  -0.06275 -0.01346 240 PHE B CA  
3926 C C   . PHE B 244 ? 0.27866 0.33680 0.22753 0.00865  -0.06309 -0.00731 240 PHE B C   
3927 O O   . PHE B 244 ? 0.26101 0.30750 0.21029 0.01255  -0.05855 -0.00551 240 PHE B O   
3928 C CB  . PHE B 244 ? 0.30951 0.38390 0.26926 -0.00562 -0.05729 -0.01870 240 PHE B CB  
3929 C CG  . PHE B 244 ? 0.27193 0.33008 0.22730 -0.00797 -0.04902 -0.01903 240 PHE B CG  
3930 C CD1 . PHE B 244 ? 0.26961 0.31370 0.21065 -0.01088 -0.04681 -0.01755 240 PHE B CD1 
3931 C CD2 . PHE B 244 ? 0.24188 0.29991 0.20750 -0.00794 -0.04351 -0.02101 240 PHE B CD2 
3932 C CE1 . PHE B 244 ? 0.27643 0.30735 0.21534 -0.01298 -0.03962 -0.01808 240 PHE B CE1 
3933 C CE2 . PHE B 244 ? 0.23485 0.27875 0.19681 -0.01026 -0.03699 -0.02094 240 PHE B CE2 
3934 C CZ  . PHE B 244 ? 0.19333 0.22403 0.14290 -0.01245 -0.03522 -0.01954 240 PHE B CZ  
3935 N N   . SER B 245 ? 0.32243 0.37819 0.25766 0.00659  -0.06861 -0.00406 241 SER B N   
3936 C CA  . SER B 245 ? 0.32529 0.36462 0.24507 0.00907  -0.07010 0.00275  241 SER B CA  
3937 C C   . SER B 245 ? 0.37807 0.40519 0.28351 0.00042  -0.06332 0.00108  241 SER B C   
3938 O O   . SER B 245 ? 0.26257 0.29537 0.16556 -0.00741 -0.06137 -0.00431 241 SER B O   
3939 C CB  . SER B 245 ? 0.32028 0.36416 0.23240 0.01211  -0.08112 0.00857  241 SER B CB  
3940 O OG  . SER B 245 ? 0.46032 0.51226 0.38637 0.02242  -0.08750 0.01127  241 SER B OG  
3941 N N   . VAL B 246 ? 0.32966 0.34018 0.22647 0.00182  -0.05959 0.00522  242 VAL B N   
3942 C CA  . VAL B 246 ? 0.26088 0.26003 0.14550 -0.00563 -0.05259 0.00379  242 VAL B CA  
3943 C C   . VAL B 246 ? 0.33856 0.32675 0.20440 -0.00621 -0.05606 0.01097  242 VAL B C   
3944 O O   . VAL B 246 ? 0.28859 0.26778 0.15233 0.00026  -0.05947 0.01782  242 VAL B O   
3945 C CB  . VAL B 246 ? 0.36160 0.35131 0.25294 -0.00519 -0.04421 0.00201  242 VAL B CB  
3946 C CG1 . VAL B 246 ? 0.26566 0.24396 0.14500 -0.01177 -0.03782 0.00151  242 VAL B CG1 
3947 C CG2 . VAL B 246 ? 0.29842 0.29797 0.20552 -0.00674 -0.04063 -0.00469 242 VAL B CG2 
3948 N N   . TYR B 247 ? 0.35069 0.33901 0.20239 -0.01441 -0.05503 0.00923  243 TYR B N   
3949 C CA  . TYR B 247 ? 0.31098 0.29004 0.14215 -0.01714 -0.05822 0.01600  243 TYR B CA  
3950 C C   . TYR B 247 ? 0.36490 0.33306 0.18385 -0.02497 -0.04900 0.01426  243 TYR B C   
3951 O O   . TYR B 247 ? 0.33334 0.29188 0.13456 -0.02791 -0.05030 0.02054  243 TYR B O   
3952 C CB  . TYR B 247 ? 0.32420 0.31388 0.14535 -0.02098 -0.06607 0.01627  243 TYR B CB  
3953 C CG  . TYR B 247 ? 0.41843 0.41897 0.24906 -0.01314 -0.07724 0.02009  243 TYR B CG  
3954 C CD1 . TYR B 247 ? 0.46594 0.46087 0.28855 -0.00746 -0.08679 0.03027  243 TYR B CD1 
3955 C CD2 . TYR B 247 ? 0.42048 0.43714 0.26870 -0.01160 -0.07849 0.01361  243 TYR B CD2 
3956 C CE1 . TYR B 247 ? 0.45216 0.45825 0.28574 0.00054  -0.09742 0.03343  243 TYR B CE1 
3957 C CE2 . TYR B 247 ? 0.43659 0.46546 0.29535 -0.00455 -0.08838 0.01647  243 TYR B CE2 
3958 C CZ  . TYR B 247 ? 0.50075 0.52479 0.35296 0.00199  -0.09789 0.02615  243 TYR B CZ  
3959 O OH  . TYR B 247 ? 0.64455 0.68181 0.50949 0.00987  -0.10814 0.02873  243 TYR B OH  
3960 N N   . ASP B 248 ? 0.32235 0.29187 0.15048 -0.02859 -0.03999 0.00622  244 ASP B N   
3961 C CA  . ASP B 248 ? 0.36466 0.32714 0.18328 -0.03626 -0.03119 0.00309  244 ASP B CA  
3962 C C   . ASP B 248 ? 0.32663 0.28551 0.15993 -0.03530 -0.02306 -0.00135 244 ASP B C   
3963 O O   . ASP B 248 ? 0.32563 0.29019 0.17533 -0.03137 -0.02336 -0.00462 244 ASP B O   
3964 C CB  . ASP B 248 ? 0.30982 0.28062 0.12095 -0.04455 -0.02902 -0.00442 244 ASP B CB  
3965 C CG  . ASP B 248 ? 0.44724 0.41239 0.24940 -0.05238 -0.01922 -0.00874 244 ASP B CG  
3966 O OD1 . ASP B 248 ? 0.42179 0.37943 0.20647 -0.05607 -0.01880 -0.00314 244 ASP B OD1 
3967 O OD2 . ASP B 248 ? 0.39089 0.35914 0.20406 -0.05490 -0.01198 -0.01765 244 ASP B OD2 
3968 N N   . VAL B 249 ? 0.29047 0.24053 0.11747 -0.03964 -0.01589 -0.00136 245 VAL B N   
3969 C CA  . VAL B 249 ? 0.29889 0.24516 0.13916 -0.03886 -0.00902 -0.00455 245 VAL B CA  
3970 C C   . VAL B 249 ? 0.26561 0.22026 0.11946 -0.04120 -0.00469 -0.01412 245 VAL B C   
3971 O O   . VAL B 249 ? 0.25802 0.21200 0.12647 -0.03872 -0.00215 -0.01613 245 VAL B O   
3972 C CB  . VAL B 249 ? 0.30314 0.23967 0.13367 -0.04381 -0.00257 -0.00255 245 VAL B CB  
3973 C CG1 . VAL B 249 ? 0.29483 0.23545 0.11496 -0.05246 0.00293  -0.00831 245 VAL B CG1 
3974 C CG2 . VAL B 249 ? 0.28787 0.22039 0.13229 -0.04251 0.00306  -0.00454 245 VAL B CG2 
3975 N N   . SER B 250 ? 0.28253 0.24440 0.13152 -0.04611 -0.00431 -0.01996 246 SER B N   
3976 C CA  . SER B 250 ? 0.29803 0.26526 0.15893 -0.04902 0.00051  -0.02958 246 SER B CA  
3977 C C   . SER B 250 ? 0.27473 0.24653 0.15248 -0.04455 -0.00285 -0.03082 246 SER B C   
3978 O O   . SER B 250 ? 0.28883 0.26085 0.17958 -0.04535 0.00109  -0.03620 246 SER B O   
3979 C CB  . SER B 250 ? 0.32051 0.29403 0.17166 -0.05527 0.00101  -0.03603 246 SER B CB  
3980 O OG  . SER B 250 ? 0.37663 0.35678 0.22331 -0.05390 -0.00740 -0.03360 246 SER B OG  
3981 N N   . ILE B 251 ? 0.24120 0.21703 0.11939 -0.04007 -0.01015 -0.02597 247 ILE B N   
3982 C CA  . ILE B 251 ? 0.31362 0.29502 0.20723 -0.03695 -0.01255 -0.02741 247 ILE B CA  
3983 C C   . ILE B 251 ? 0.21639 0.19159 0.11980 -0.03311 -0.00998 -0.02450 247 ILE B C   
3984 O O   . ILE B 251 ? 0.30455 0.28262 0.22068 -0.03239 -0.00978 -0.02657 247 ILE B O   
3985 C CB  . ILE B 251 ? 0.39147 0.38163 0.28424 -0.03360 -0.02069 -0.02419 247 ILE B CB  
3986 C CG1 . ILE B 251 ? 0.31861 0.31460 0.22691 -0.02986 -0.02262 -0.02425 247 ILE B CG1 
3987 C CG2 . ILE B 251 ? 0.39989 0.38574 0.28140 -0.02958 -0.02491 -0.01633 247 ILE B CG2 
3988 C CD1 . ILE B 251 ? 0.53711 0.54436 0.44758 -0.02666 -0.03009 -0.02227 247 ILE B CD1 
3989 N N   . LEU B 252 ? 0.23239 0.19871 0.12940 -0.03168 -0.00784 -0.01987 248 LEU B N   
3990 C CA  . LEU B 252 ? 0.26398 0.22421 0.16895 -0.02868 -0.00568 -0.01733 248 LEU B CA  
3991 C C   . LEU B 252 ? 0.23476 0.19050 0.14515 -0.03232 0.00074  -0.02086 248 LEU B C   
3992 O O   . LEU B 252 ? 0.22485 0.17694 0.14334 -0.03075 0.00209  -0.01956 248 LEU B O   
3993 C CB  . LEU B 252 ? 0.24197 0.19395 0.13830 -0.02491 -0.00735 -0.01024 248 LEU B CB  
3994 C CG  . LEU B 252 ? 0.27994 0.23413 0.17451 -0.01876 -0.01409 -0.00550 248 LEU B CG  
3995 C CD1 . LEU B 252 ? 0.34047 0.30297 0.24906 -0.01539 -0.01596 -0.00772 248 LEU B CD1 
3996 C CD2 . LEU B 252 ? 0.47253 0.43162 0.35671 -0.01989 -0.01877 -0.00445 248 LEU B CD2 
3997 N N   . ILE B 253 ? 0.29382 0.25022 0.20007 -0.03715 0.00468  -0.02549 249 ILE B N   
3998 C CA  . ILE B 253 ? 0.42334 0.37637 0.33600 -0.04000 0.01096  -0.02903 249 ILE B CA  
3999 C C   . ILE B 253 ? 0.44113 0.39532 0.37039 -0.03890 0.01099  -0.03161 249 ILE B C   
4000 O O   . ILE B 253 ? 0.36116 0.31120 0.29713 -0.03850 0.01322  -0.03029 249 ILE B O   
4001 C CB  . ILE B 253 ? 0.31754 0.27302 0.22423 -0.04530 0.01573  -0.03525 249 ILE B CB  
4002 C CG1 . ILE B 253 ? 0.31738 0.26966 0.20580 -0.04765 0.01638  -0.03110 249 ILE B CG1 
4003 C CG2 . ILE B 253 ? 0.47069 0.42539 0.38899 -0.04739 0.02203  -0.04068 249 ILE B CG2 
4004 C CD1 . ILE B 253 ? 0.47484 0.43001 0.35505 -0.05405 0.02210  -0.03744 249 ILE B CD1 
4005 N N   . PRO B 254 ? 0.30127 0.26055 0.23736 -0.03894 0.00822  -0.03477 250 PRO B N   
4006 C CA  . PRO B 254 ? 0.28854 0.24735 0.23883 -0.03841 0.00743  -0.03554 250 PRO B CA  
4007 C C   . PRO B 254 ? 0.31397 0.27189 0.26645 -0.03519 0.00411  -0.02964 250 PRO B C   
4008 O O   . PRO B 254 ? 0.24877 0.20633 0.21099 -0.03554 0.00303  -0.02940 250 PRO B O   
4009 C CB  . PRO B 254 ? 0.29998 0.26387 0.25444 -0.04059 0.00549  -0.04065 250 PRO B CB  
4010 C CG  . PRO B 254 ? 0.41082 0.37771 0.35435 -0.04293 0.00675  -0.04442 250 PRO B CG  
4011 C CD  . PRO B 254 ? 0.32446 0.28983 0.25547 -0.04090 0.00607  -0.03851 250 PRO B CD  
4012 N N   . ILE B 255 ? 0.22016 0.17714 0.16372 -0.03224 0.00249  -0.02499 251 ILE B N   
4013 C CA  . ILE B 255 ? 0.20991 0.16795 0.15525 -0.02879 -0.00061 -0.02102 251 ILE B CA  
4014 C C   . ILE B 255 ? 0.23187 0.18226 0.17444 -0.02678 0.00082  -0.01691 251 ILE B C   
4015 O O   . ILE B 255 ? 0.17446 0.12356 0.12252 -0.02615 0.00053  -0.01551 251 ILE B O   
4016 C CB  . ILE B 255 ? 0.21951 0.18386 0.15940 -0.02598 -0.00469 -0.01978 251 ILE B CB  
4017 C CG1 . ILE B 255 ? 0.27607 0.24851 0.21889 -0.02899 -0.00635 -0.02430 251 ILE B CG1 
4018 C CG2 . ILE B 255 ? 0.30785 0.27461 0.25146 -0.02197 -0.00700 -0.01695 251 ILE B CG2 
4019 C CD1 . ILE B 255 ? 0.21247 0.18834 0.16665 -0.03135 -0.00668 -0.02651 251 ILE B CD1 
4020 N N   . ILE B 256 ? 0.21819 0.16310 0.15126 -0.02651 0.00233  -0.01491 252 ILE B N   
4021 C CA  . ILE B 256 ? 0.22068 0.15707 0.14986 -0.02519 0.00355  -0.01102 252 ILE B CA  
4022 C C   . ILE B 256 ? 0.23747 0.16976 0.16843 -0.02939 0.00806  -0.01240 252 ILE B C   
4023 O O   . ILE B 256 ? 0.31488 0.24891 0.24352 -0.03245 0.01075  -0.01520 252 ILE B O   
4024 C CB  . ILE B 256 ? 0.21359 0.14531 0.13085 -0.02209 0.00145  -0.00679 252 ILE B CB  
4025 C CG1 . ILE B 256 ? 0.20961 0.13081 0.12330 -0.02078 0.00251  -0.00304 252 ILE B CG1 
4026 C CG2 . ILE B 256 ? 0.22822 0.15978 0.13569 -0.02521 0.00257  -0.00709 252 ILE B CG2 
4027 C CD1 . ILE B 256 ? 0.28067 0.19606 0.18580 -0.01579 -0.00106 0.00151  252 ILE B CD1 
4028 N N   . ALA B 257 ? 0.19686 0.12483 0.13258 -0.02985 0.00902  -0.01106 253 ALA B N   
4029 C CA  . ALA B 257 ? 0.21162 0.13790 0.15264 -0.03369 0.01262  -0.01263 253 ALA B CA  
4030 C C   . ALA B 257 ? 0.21247 0.13088 0.14617 -0.03530 0.01503  -0.00963 253 ALA B C   
4031 O O   . ALA B 257 ? 0.29486 0.21340 0.23114 -0.03915 0.01885  -0.01130 253 ALA B O   
4032 C CB  . ALA B 257 ? 0.24688 0.17489 0.19991 -0.03433 0.01122  -0.01329 253 ALA B CB  
4033 N N   . LEU B 258 ? 0.22045 0.13211 0.14606 -0.03258 0.01303  -0.00562 254 LEU B N   
4034 C CA  . LEU B 258 ? 0.27614 0.17808 0.19423 -0.03436 0.01481  -0.00240 254 LEU B CA  
4035 C C   . LEU B 258 ? 0.21394 0.10877 0.12042 -0.03033 0.01204  0.00168  254 LEU B C   
4036 O O   . LEU B 258 ? 0.27412 0.17178 0.18187 -0.02526 0.00843  0.00184  254 LEU B O   
4037 C CB  . LEU B 258 ? 0.30437 0.20276 0.22827 -0.03538 0.01467  -0.00207 254 LEU B CB  
4038 C CG  . LEU B 258 ? 0.26734 0.17184 0.20387 -0.03883 0.01573  -0.00490 254 LEU B CG  
4039 C CD1 . LEU B 258 ? 0.26385 0.16550 0.20380 -0.03910 0.01365  -0.00395 254 LEU B CD1 
4040 C CD2 . LEU B 258 ? 0.42024 0.32508 0.35830 -0.04383 0.02002  -0.00601 254 LEU B CD2 
4041 N N   . MET B 259 ? 0.23931 0.12500 0.13507 -0.03272 0.01357  0.00512  255 MET B N   
4042 C CA  . MET B 259 ? 0.24044 0.11664 0.12493 -0.02885 0.01022  0.01006  255 MET B CA  
4043 C C   . MET B 259 ? 0.30883 0.17108 0.18760 -0.03073 0.01141  0.01332  255 MET B C   
4044 O O   . MET B 259 ? 0.28351 0.14347 0.16169 -0.03724 0.01558  0.01298  255 MET B O   
4045 C CB  . MET B 259 ? 0.27474 0.15110 0.14782 -0.03054 0.00969  0.01254  255 MET B CB  
4046 C CG  . MET B 259 ? 0.24450 0.13372 0.12137 -0.02922 0.00816  0.00908  255 MET B CG  
4047 S SD  . MET B 259 ? 0.31898 0.20781 0.17956 -0.03210 0.00695  0.01215  255 MET B SD  
4048 C CE  . MET B 259 ? 0.34084 0.22885 0.19759 -0.04186 0.01520  0.00986  255 MET B CE  
4049 N N   . VAL B 260 ? 0.27110 0.12423 0.14641 -0.02508 0.00782  0.01602  256 VAL B N   
4050 C CA  . VAL B 260 ? 0.30375 0.14071 0.17135 -0.02667 0.00834  0.01954  256 VAL B CA  
4051 C C   . VAL B 260 ? 0.33669 0.16525 0.19028 -0.03071 0.00861  0.02505  256 VAL B C   
4052 O O   . VAL B 260 ? 0.32058 0.15283 0.16842 -0.02883 0.00595  0.02732  256 VAL B O   
4053 C CB  . VAL B 260 ? 0.28278 0.11163 0.15103 -0.01873 0.00446  0.02019  256 VAL B CB  
4054 C CG1 . VAL B 260 ? 0.33013 0.15979 0.19472 -0.01155 -0.00083 0.02334  256 VAL B CG1 
4055 C CG2 . VAL B 260 ? 0.29348 0.10399 0.15465 -0.02065 0.00520  0.02280  256 VAL B CG2 
4056 N N   . TYR B 261 ? 0.29978 0.11760 0.14719 -0.03731 0.01184  0.02723  257 TYR B N   
4057 C CA  . TYR B 261 ? 0.32297 0.13167 0.15547 -0.04293 0.01273  0.03299  257 TYR B CA  
4058 C C   . TYR B 261 ? 0.44868 0.24304 0.27034 -0.03681 0.00637  0.03973  257 TYR B C   
4059 O O   . TYR B 261 ? 0.34329 0.12525 0.16583 -0.03218 0.00381  0.04088  257 TYR B O   
4060 C CB  . TYR B 261 ? 0.35162 0.15216 0.18122 -0.05193 0.01774  0.03357  257 TYR B CB  
4061 C CG  . TYR B 261 ? 0.35475 0.14724 0.16876 -0.06022 0.02018  0.03915  257 TYR B CG  
4062 C CD1 . TYR B 261 ? 0.36621 0.14214 0.16873 -0.05968 0.01660  0.04572  257 TYR B CD1 
4063 C CD2 . TYR B 261 ? 0.34183 0.14644 0.15548 -0.06801 0.02595  0.03659  257 TYR B CD2 
4064 C CE1 . TYR B 261 ? 0.44666 0.22015 0.23823 -0.06675 0.01816  0.04977  257 TYR B CE1 
4065 C CE2 . TYR B 261 ? 0.36026 0.15961 0.15965 -0.07639 0.02885  0.04096  257 TYR B CE2 
4066 C CZ  . TYR B 261 ? 0.37959 0.16514 0.16921 -0.07528 0.02438  0.04728  257 TYR B CZ  
4067 O OH  . TYR B 261 ? 0.44687 0.23079 0.22527 -0.08289 0.02641  0.05074  257 TYR B OH  
4068 N N   . ARG B 262 ? 0.34619 0.14218 0.15790 -0.03669 0.00352  0.04393  258 ARG B N   
4069 C CA  . ARG B 262 ? 0.40300 0.18587 0.20400 -0.03106 -0.00375 0.05152  258 ARG B CA  
4070 C C   . ARG B 262 ? 0.39043 0.15963 0.17213 -0.03892 -0.00372 0.05967  258 ARG B C   
4071 O O   . ARG B 262 ? 0.40982 0.16175 0.18401 -0.03640 -0.00830 0.06615  258 ARG B O   
4072 C CB  . ARG B 262 ? 0.45888 0.25441 0.26289 -0.02400 -0.00927 0.05107  258 ARG B CB  
4073 C CG  . ARG B 262 ? 0.41714 0.22373 0.23853 -0.01523 -0.01083 0.04470  258 ARG B CG  
4074 C CD  . ARG B 262 ? 0.51807 0.31138 0.34391 -0.00833 -0.01324 0.04534  258 ARG B CD  
4075 N NE  . ARG B 262 ? 0.49972 0.30367 0.33937 0.00123  -0.01633 0.04073  258 ARG B NE  
4076 C CZ  . ARG B 262 ? 0.49537 0.29579 0.34435 0.00650  -0.01569 0.03675  258 ARG B CZ  
4077 N NH1 . ARG B 262 ? 0.51492 0.30087 0.36111 0.00336  -0.01252 0.03657  258 ARG B NH1 
4078 N NH2 . ARG B 262 ? 0.35784 0.17017 0.21906 0.01438  -0.01791 0.03233  258 ARG B NH2 
4079 N N   . CYS B 263 ? 0.45099 0.22914 0.22611 -0.04833 0.00151  0.05871  259 CYS B N   
4080 C CA  . CYS B 263 ? 0.49005 0.26106 0.24887 -0.05660 0.00222  0.06491  259 CYS B CA  
4081 C C   . CYS B 263 ? 0.43472 0.21874 0.19276 -0.06765 0.01142  0.05972  259 CYS B C   
4082 O O   . CYS B 263 ? 0.41180 0.20980 0.18131 -0.06782 0.01599  0.05212  259 CYS B O   
4083 C CB  . CYS B 263 ? 0.46125 0.23059 0.20817 -0.05284 -0.00576 0.07164  259 CYS B CB  
4084 S SG  . CYS B 263 ? 0.49090 0.28062 0.23894 -0.05145 -0.00629 0.06673  259 CYS B SG  
4085 N N   . ALA B 264 ? 0.47206 0.25435 0.22036 -0.07589 0.01385  0.06259  260 ALA B N   
4086 C CA  . ALA B 264 ? 0.49086 0.28636 0.23786 -0.08626 0.02262  0.05736  260 ALA B CA  
4087 C C   . ALA B 264 ? 0.45401 0.26064 0.19320 -0.08701 0.02215  0.05601  260 ALA B C   
4088 O O   . ALA B 264 ? 0.57007 0.37269 0.30136 -0.08114 0.01401  0.06131  260 ALA B O   
4089 C CB  . ALA B 264 ? 0.47255 0.26272 0.21106 -0.09512 0.02540  0.06069  260 ALA B CB  
4090 N N   . PRO B 265 ? 0.50233 0.32402 0.24498 -0.09377 0.03059  0.04822  261 PRO B N   
4091 C CA  . PRO B 265 ? 0.49241 0.32596 0.22810 -0.09517 0.03088  0.04511  261 PRO B CA  
4092 C C   . PRO B 265 ? 0.55852 0.38761 0.27686 -0.09828 0.02600  0.05201  261 PRO B C   
4093 O O   . PRO B 265 ? 0.45287 0.27562 0.16429 -0.10468 0.02782  0.05582  261 PRO B O   
4094 C CB  . PRO B 265 ? 0.50263 0.35163 0.24654 -0.10321 0.04239  0.03485  261 PRO B CB  
4095 C CG  . PRO B 265 ? 0.68226 0.52795 0.43820 -0.10564 0.04729  0.03341  261 PRO B CG  
4096 C CD  . PRO B 265 ? 0.53153 0.36141 0.28889 -0.09802 0.03945  0.04047  261 PRO B CD  
4097 N N   . PRO B 266 ? 0.48000 0.31273 0.19098 -0.09431 0.01951  0.05382  262 PRO B N   
4098 C CA  . PRO B 266 ? 0.55555 0.38370 0.25025 -0.09650 0.01326  0.06147  262 PRO B CA  
4099 C C   . PRO B 266 ? 0.56365 0.40001 0.24954 -0.10838 0.02106  0.05786  262 PRO B C   
4100 O O   . PRO B 266 ? 0.59929 0.44778 0.29303 -0.11378 0.03101  0.04801  262 PRO B O   
4101 C CB  . PRO B 266 ? 0.67566 0.51046 0.36835 -0.08965 0.00538  0.06161  262 PRO B CB  
4102 C CG  . PRO B 266 ? 0.71366 0.55116 0.42103 -0.08202 0.00553  0.05661  262 PRO B CG  
4103 C CD  . PRO B 266 ? 0.66570 0.50708 0.38335 -0.08755 0.01686  0.04908  262 PRO B CD  
4104 N N   . PRO B 267 ? 0.56110 0.39131 0.23109 -0.11269 0.01683  0.06545  263 PRO B N   
4105 C CA  . PRO B 267 ? 0.59588 0.43365 0.25524 -0.12444 0.02369  0.06243  263 PRO B CA  
4106 C C   . PRO B 267 ? 0.66088 0.51567 0.31953 -0.12671 0.02688  0.05359  263 PRO B C   
4107 O O   . PRO B 267 ? 0.60348 0.47061 0.27096 -0.13151 0.03713  0.04273  263 PRO B O   
4108 C CB  . PRO B 267 ? 0.60879 0.43384 0.25056 -0.12628 0.01547  0.07447  263 PRO B CB  
4109 C CG  . PRO B 267 ? 0.56789 0.37682 0.21458 -0.11658 0.00700  0.08289  263 PRO B CG  
4110 C CD  . PRO B 267 ? 0.54975 0.36442 0.21156 -0.10672 0.00541  0.07755  263 PRO B CD  
# 
