data_9O0Y
# 
_entry.id   9O0Y 
# 
_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   9O0Y         pdb_00009o0y 10.2210/pdb9o0y/pdb 
WWPDB D_1000294681 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-21 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9O0Y 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-03 
_pdbx_database_status.SG_entry                        Y 
_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                 1 
_pdbx_contact_author.email              l.halabelian@utoronto.ca 
_pdbx_contact_author.name_first         Levon 
_pdbx_contact_author.name_last          Halabelian 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4361-3619 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dehghani-Tafti, S.'                   1 ? 
'Dong, A.'                             2 ? 
'Li, Y.'                               3 ? 
'Ackloo, S.'                           4 ? 
'Arrowsmith, C.H.'                     5 ? 
'Edwards, A.M.'                        6 ? 
'Halabelian, L.'                       7 ? 
'Structural Genomics Consortium (SGC)' 8 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Co-crystal structure of human TREX1 in complex with an inhibitor' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Dehghani-Tafti, S.'                   1 ? 
primary 'Dong, A.'                             2 ? 
primary 'Li, Y.'                               3 ? 
primary 'Ackloo, S.'                           4 ? 
primary 'Arrowsmith, C.H.'                     5 ? 
primary 'Edwards, A.M.'                        6 ? 
primary 'Halabelian, L.'                       7 ? 
primary 'Structural Genomics Consortium (SGC)' 8 ? 
# 
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 'Three-prime repair exonuclease 1'                                              25169.863 3   3.1.11.2 ? ? ? 
2 non-polymer syn 'N-[(2,3-dichlorophenyl)methyl]-3,5-difluoro-N-[(pyridin-3-yl)methyl]benzamide' 407.241   3   ?        ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                                                                 24.305    3   ?        ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                                  62.068    4   ?        ? ? ? 
5 non-polymer syn 'UNKNOWN ATOM OR ION'                                                           ?         6   ?        ? ? ? 
6 water       nat water                                                                           18.015    499 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;3'-5' exonuclease TREX1,Deoxyribonuclease III,DNase III
;
# 
_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       
;ALPHGHMQTLIFFDMEATGLPSSRPEVTELCLLAVHRCALESPPTSQGPPPTVPPPPRVVDKLSLCVAPGKACSPAASEI
TGLSTAVLAAHGRQCFDDNLANLLLAFLRRQPQPWCLVAHNGDRYDFPLLQAELAMLGLTSALDGAFCVDSITALKALER
ASSPSEHGPRKSYSLGSIYTRLYGQSPPDSHTAEGDVLALLSICQWRPQALLRWVDAHARPFGTIRPMYGVTAS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ALPHGHMQTLIFFDMEATGLPSSRPEVTELCLLAVHRCALESPPTSQGPPPTVPPPPRVVDKLSLCVAPGKACSPAASEI
TGLSTAVLAAHGRQCFDDNLANLLLAFLRRQPQPWCLVAHNGDRYDFPLLQAELAMLGLTSALDGAFCVDSITALKALER
ASSPSEHGPRKSYSLGSIYTRLYGQSPPDSHTAEGDVLALLSICQWRPQALLRWVDAHARPFGTIRPMYGVTAS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'N-[(2,3-dichlorophenyl)methyl]-3,5-difluoro-N-[(pyridin-3-yl)methyl]benzamide' A1B7T 
3 'MAGNESIUM ION'                                                                 MG    
4 1,2-ETHANEDIOL                                                                  EDO   
5 'UNKNOWN ATOM OR ION'                                                           UNX   
6 water                                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   LEU n 
1 3   PRO n 
1 4   HIS n 
1 5   GLY n 
1 6   HIS n 
1 7   MET n 
1 8   GLN n 
1 9   THR n 
1 10  LEU n 
1 11  ILE n 
1 12  PHE n 
1 13  PHE n 
1 14  ASP n 
1 15  MET n 
1 16  GLU n 
1 17  ALA n 
1 18  THR n 
1 19  GLY n 
1 20  LEU n 
1 21  PRO n 
1 22  SER n 
1 23  SER n 
1 24  ARG n 
1 25  PRO n 
1 26  GLU n 
1 27  VAL n 
1 28  THR n 
1 29  GLU n 
1 30  LEU n 
1 31  CYS n 
1 32  LEU n 
1 33  LEU n 
1 34  ALA n 
1 35  VAL n 
1 36  HIS n 
1 37  ARG n 
1 38  CYS n 
1 39  ALA n 
1 40  LEU n 
1 41  GLU n 
1 42  SER n 
1 43  PRO n 
1 44  PRO n 
1 45  THR n 
1 46  SER n 
1 47  GLN n 
1 48  GLY n 
1 49  PRO n 
1 50  PRO n 
1 51  PRO n 
1 52  THR n 
1 53  VAL n 
1 54  PRO n 
1 55  PRO n 
1 56  PRO n 
1 57  PRO n 
1 58  ARG n 
1 59  VAL n 
1 60  VAL n 
1 61  ASP n 
1 62  LYS n 
1 63  LEU n 
1 64  SER n 
1 65  LEU n 
1 66  CYS n 
1 67  VAL n 
1 68  ALA n 
1 69  PRO n 
1 70  GLY n 
1 71  LYS n 
1 72  ALA n 
1 73  CYS n 
1 74  SER n 
1 75  PRO n 
1 76  ALA n 
1 77  ALA n 
1 78  SER n 
1 79  GLU n 
1 80  ILE n 
1 81  THR n 
1 82  GLY n 
1 83  LEU n 
1 84  SER n 
1 85  THR n 
1 86  ALA n 
1 87  VAL n 
1 88  LEU n 
1 89  ALA n 
1 90  ALA n 
1 91  HIS n 
1 92  GLY n 
1 93  ARG n 
1 94  GLN n 
1 95  CYS n 
1 96  PHE n 
1 97  ASP n 
1 98  ASP n 
1 99  ASN n 
1 100 LEU n 
1 101 ALA n 
1 102 ASN n 
1 103 LEU n 
1 104 LEU n 
1 105 LEU n 
1 106 ALA n 
1 107 PHE n 
1 108 LEU n 
1 109 ARG n 
1 110 ARG n 
1 111 GLN n 
1 112 PRO n 
1 113 GLN n 
1 114 PRO n 
1 115 TRP n 
1 116 CYS n 
1 117 LEU n 
1 118 VAL n 
1 119 ALA n 
1 120 HIS n 
1 121 ASN n 
1 122 GLY n 
1 123 ASP n 
1 124 ARG n 
1 125 TYR n 
1 126 ASP n 
1 127 PHE n 
1 128 PRO n 
1 129 LEU n 
1 130 LEU n 
1 131 GLN n 
1 132 ALA n 
1 133 GLU n 
1 134 LEU n 
1 135 ALA n 
1 136 MET n 
1 137 LEU n 
1 138 GLY n 
1 139 LEU n 
1 140 THR n 
1 141 SER n 
1 142 ALA n 
1 143 LEU n 
1 144 ASP n 
1 145 GLY n 
1 146 ALA n 
1 147 PHE n 
1 148 CYS n 
1 149 VAL n 
1 150 ASP n 
1 151 SER n 
1 152 ILE n 
1 153 THR n 
1 154 ALA n 
1 155 LEU n 
1 156 LYS n 
1 157 ALA n 
1 158 LEU n 
1 159 GLU n 
1 160 ARG n 
1 161 ALA n 
1 162 SER n 
1 163 SER n 
1 164 PRO n 
1 165 SER n 
1 166 GLU n 
1 167 HIS n 
1 168 GLY n 
1 169 PRO n 
1 170 ARG n 
1 171 LYS n 
1 172 SER n 
1 173 TYR n 
1 174 SER n 
1 175 LEU n 
1 176 GLY n 
1 177 SER n 
1 178 ILE n 
1 179 TYR n 
1 180 THR n 
1 181 ARG n 
1 182 LEU n 
1 183 TYR n 
1 184 GLY n 
1 185 GLN n 
1 186 SER n 
1 187 PRO n 
1 188 PRO n 
1 189 ASP n 
1 190 SER n 
1 191 HIS n 
1 192 THR n 
1 193 ALA n 
1 194 GLU n 
1 195 GLY n 
1 196 ASP n 
1 197 VAL n 
1 198 LEU n 
1 199 ALA n 
1 200 LEU n 
1 201 LEU n 
1 202 SER n 
1 203 ILE n 
1 204 CYS n 
1 205 GLN n 
1 206 TRP n 
1 207 ARG n 
1 208 PRO n 
1 209 GLN n 
1 210 ALA n 
1 211 LEU n 
1 212 LEU n 
1 213 ARG n 
1 214 TRP n 
1 215 VAL n 
1 216 ASP n 
1 217 ALA n 
1 218 HIS n 
1 219 ALA n 
1 220 ARG n 
1 221 PRO n 
1 222 PHE n 
1 223 GLY n 
1 224 THR n 
1 225 ILE n 
1 226 ARG n 
1 227 PRO n 
1 228 MET n 
1 229 TYR n 
1 230 GLY n 
1 231 VAL n 
1 232 THR n 
1 233 ALA n 
1 234 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   234 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 TREX1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1B7T non-polymer         . 'N-[(2,3-dichlorophenyl)methyl]-3,5-difluoro-N-[(pyridin-3-yl)methyl]benzamide' ?                 
'C20 H14 Cl2 F2 N2 O' 407.241 
ALA   'L-peptide linking' y ALANINE                                                                         ?                 
'C3 H7 N O2'          89.093  
ARG   'L-peptide linking' y ARGININE                                                                        ?                 
'C6 H15 N4 O2 1'      175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                      ?                 
'C4 H8 N2 O3'         132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                 ?                 
'C4 H7 N O4'          133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                        ?                 
'C3 H7 N O2 S'        121.158 
EDO   non-polymer         . 1,2-ETHANEDIOL                                                                  'ETHYLENE GLYCOL' 
'C2 H6 O2'            62.068  
GLN   'L-peptide linking' y GLUTAMINE                                                                       ?                 
'C5 H10 N2 O3'        146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                 ?                 
'C5 H9 N O4'          147.129 
GLY   'peptide linking'   y GLYCINE                                                                         ?                 
'C2 H5 N O2'          75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                       ?                 
'C6 H10 N3 O2 1'      156.162 
HOH   non-polymer         . WATER                                                                           ?                 
'H2 O'                18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                      ?                 
'C6 H13 N O2'         131.173 
LEU   'L-peptide linking' y LEUCINE                                                                         ?                 
'C6 H13 N O2'         131.173 
LYS   'L-peptide linking' y LYSINE                                                                          ?                 
'C6 H15 N2 O2 1'      147.195 
MET   'L-peptide linking' y METHIONINE                                                                      ?                 
'C5 H11 N O2 S'       149.211 
MG    non-polymer         . 'MAGNESIUM ION'                                                                 ?                 
'Mg 2'                24.305  
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 
UNX   non-polymer         . 'UNKNOWN ATOM OR ION'                                                           ?                 ? ? 
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   ALA 1   5   5   ALA ALA A . n 
A 1 2   LEU 2   6   6   LEU LEU A . n 
A 1 3   PRO 3   7   7   PRO PRO A . n 
A 1 4   HIS 4   8   8   HIS HIS A . n 
A 1 5   GLY 5   9   9   GLY GLY A . n 
A 1 6   HIS 6   10  10  HIS HIS A . n 
A 1 7   MET 7   11  11  MET MET A . n 
A 1 8   GLN 8   12  12  GLN GLN A . n 
A 1 9   THR 9   13  13  THR THR A . n 
A 1 10  LEU 10  14  14  LEU LEU A . n 
A 1 11  ILE 11  15  15  ILE ILE A . n 
A 1 12  PHE 12  16  16  PHE PHE A . n 
A 1 13  PHE 13  17  17  PHE PHE A . n 
A 1 14  ASP 14  18  18  ASP ASP A . n 
A 1 15  MET 15  19  19  MET MET A . n 
A 1 16  GLU 16  20  20  GLU GLU A . n 
A 1 17  ALA 17  21  21  ALA ALA A . n 
A 1 18  THR 18  22  22  THR THR A . n 
A 1 19  GLY 19  23  23  GLY GLY A . n 
A 1 20  LEU 20  24  24  LEU LEU A . n 
A 1 21  PRO 21  25  25  PRO PRO A . n 
A 1 22  SER 22  26  26  SER SER A . n 
A 1 23  SER 23  27  27  SER SER A . n 
A 1 24  ARG 24  28  28  ARG ARG A . n 
A 1 25  PRO 25  29  29  PRO PRO A . n 
A 1 26  GLU 26  30  30  GLU GLU A . n 
A 1 27  VAL 27  31  31  VAL VAL A . n 
A 1 28  THR 28  32  32  THR THR A . n 
A 1 29  GLU 29  33  33  GLU GLU A . n 
A 1 30  LEU 30  34  34  LEU LEU A . n 
A 1 31  CYS 31  35  35  CYS CYS A . n 
A 1 32  LEU 32  36  36  LEU LEU A . n 
A 1 33  LEU 33  37  37  LEU LEU A . n 
A 1 34  ALA 34  38  38  ALA ALA A . n 
A 1 35  VAL 35  39  39  VAL VAL A . n 
A 1 36  HIS 36  40  40  HIS HIS A . n 
A 1 37  ARG 37  41  41  ARG ARG A . n 
A 1 38  CYS 38  42  42  CYS CYS A . n 
A 1 39  ALA 39  43  43  ALA ALA A . n 
A 1 40  LEU 40  44  44  LEU LEU A . n 
A 1 41  GLU 41  45  45  GLU GLU A . n 
A 1 42  SER 42  46  46  SER SER A . n 
A 1 43  PRO 43  47  47  PRO PRO A . n 
A 1 44  PRO 44  48  48  PRO PRO A . n 
A 1 45  THR 45  49  ?   ?   ?   A . n 
A 1 46  SER 46  50  ?   ?   ?   A . n 
A 1 47  GLN 47  51  ?   ?   ?   A . n 
A 1 48  GLY 48  52  ?   ?   ?   A . n 
A 1 49  PRO 49  53  ?   ?   ?   A . n 
A 1 50  PRO 50  54  54  PRO PRO A . n 
A 1 51  PRO 51  55  55  PRO PRO A . n 
A 1 52  THR 52  56  56  THR THR A . n 
A 1 53  VAL 53  57  57  VAL VAL A . n 
A 1 54  PRO 54  58  58  PRO PRO A . n 
A 1 55  PRO 55  59  59  PRO PRO A . n 
A 1 56  PRO 56  60  60  PRO PRO A . n 
A 1 57  PRO 57  61  61  PRO PRO A . n 
A 1 58  ARG 58  62  62  ARG ARG A . n 
A 1 59  VAL 59  63  63  VAL VAL A . n 
A 1 60  VAL 60  64  64  VAL VAL A . n 
A 1 61  ASP 61  65  65  ASP ASP A . n 
A 1 62  LYS 62  66  66  LYS LYS A . n 
A 1 63  LEU 63  67  67  LEU LEU A . n 
A 1 64  SER 64  68  68  SER SER A . n 
A 1 65  LEU 65  69  69  LEU LEU A . n 
A 1 66  CYS 66  70  70  CYS CYS A . n 
A 1 67  VAL 67  71  71  VAL VAL A . n 
A 1 68  ALA 68  72  72  ALA ALA A . n 
A 1 69  PRO 69  73  73  PRO PRO A . n 
A 1 70  GLY 70  74  74  GLY GLY A . n 
A 1 71  LYS 71  75  75  LYS LYS A . n 
A 1 72  ALA 72  76  76  ALA ALA A . n 
A 1 73  CYS 73  77  77  CYS CYS A . n 
A 1 74  SER 74  78  78  SER SER A . n 
A 1 75  PRO 75  79  79  PRO PRO A . n 
A 1 76  ALA 76  80  80  ALA ALA A . n 
A 1 77  ALA 77  81  81  ALA ALA A . n 
A 1 78  SER 78  82  82  SER SER A . n 
A 1 79  GLU 79  83  83  GLU GLU A . n 
A 1 80  ILE 80  84  84  ILE ILE A . n 
A 1 81  THR 81  85  85  THR THR A . n 
A 1 82  GLY 82  86  86  GLY GLY A . n 
A 1 83  LEU 83  87  87  LEU LEU A . n 
A 1 84  SER 84  88  88  SER SER A . n 
A 1 85  THR 85  89  89  THR THR A . n 
A 1 86  ALA 86  90  90  ALA ALA A . n 
A 1 87  VAL 87  91  91  VAL VAL A . n 
A 1 88  LEU 88  92  92  LEU LEU A . n 
A 1 89  ALA 89  93  93  ALA ALA A . n 
A 1 90  ALA 90  94  94  ALA ALA A . n 
A 1 91  HIS 91  95  95  HIS HIS A . n 
A 1 92  GLY 92  96  96  GLY GLY A . n 
A 1 93  ARG 93  97  97  ARG ARG A . n 
A 1 94  GLN 94  98  98  GLN GLN A . n 
A 1 95  CYS 95  99  99  CYS CYS A . n 
A 1 96  PHE 96  100 100 PHE PHE A . n 
A 1 97  ASP 97  101 101 ASP ASP A . n 
A 1 98  ASP 98  102 102 ASP ASP A . n 
A 1 99  ASN 99  103 103 ASN ASN A . n 
A 1 100 LEU 100 104 104 LEU LEU A . n 
A 1 101 ALA 101 105 105 ALA ALA A . n 
A 1 102 ASN 102 106 106 ASN ASN A . n 
A 1 103 LEU 103 107 107 LEU LEU A . n 
A 1 104 LEU 104 108 108 LEU LEU A . n 
A 1 105 LEU 105 109 109 LEU LEU A . n 
A 1 106 ALA 106 110 110 ALA ALA A . n 
A 1 107 PHE 107 111 111 PHE PHE A . n 
A 1 108 LEU 108 112 112 LEU LEU A . n 
A 1 109 ARG 109 113 113 ARG ARG A . n 
A 1 110 ARG 110 114 114 ARG ARG A . n 
A 1 111 GLN 111 115 115 GLN GLN A . n 
A 1 112 PRO 112 116 116 PRO PRO A . n 
A 1 113 GLN 113 117 117 GLN GLN A . n 
A 1 114 PRO 114 118 118 PRO PRO A . n 
A 1 115 TRP 115 119 119 TRP TRP A . n 
A 1 116 CYS 116 120 120 CYS CYS A . n 
A 1 117 LEU 117 121 121 LEU LEU A . n 
A 1 118 VAL 118 122 122 VAL VAL A . n 
A 1 119 ALA 119 123 123 ALA ALA A . n 
A 1 120 HIS 120 124 124 HIS HIS A . n 
A 1 121 ASN 121 125 125 ASN ASN A . n 
A 1 122 GLY 122 126 126 GLY GLY A . n 
A 1 123 ASP 123 127 127 ASP ASP A . n 
A 1 124 ARG 124 128 128 ARG ARG A . n 
A 1 125 TYR 125 129 129 TYR TYR A . n 
A 1 126 ASP 126 130 130 ASP ASP A . n 
A 1 127 PHE 127 131 131 PHE PHE A . n 
A 1 128 PRO 128 132 132 PRO PRO A . n 
A 1 129 LEU 129 133 133 LEU LEU A . n 
A 1 130 LEU 130 134 134 LEU LEU A . n 
A 1 131 GLN 131 135 135 GLN GLN A . n 
A 1 132 ALA 132 136 136 ALA ALA A . n 
A 1 133 GLU 133 137 137 GLU GLU A . n 
A 1 134 LEU 134 138 138 LEU LEU A . n 
A 1 135 ALA 135 139 139 ALA ALA A . n 
A 1 136 MET 136 140 140 MET MET A . n 
A 1 137 LEU 137 141 141 LEU LEU A . n 
A 1 138 GLY 138 142 142 GLY GLY A . n 
A 1 139 LEU 139 143 143 LEU LEU A . n 
A 1 140 THR 140 144 144 THR THR A . n 
A 1 141 SER 141 145 145 SER SER A . n 
A 1 142 ALA 142 146 146 ALA ALA A . n 
A 1 143 LEU 143 147 147 LEU LEU A . n 
A 1 144 ASP 144 148 148 ASP ASP A . n 
A 1 145 GLY 145 149 149 GLY GLY A . n 
A 1 146 ALA 146 150 150 ALA ALA A . n 
A 1 147 PHE 147 151 151 PHE PHE A . n 
A 1 148 CYS 148 152 152 CYS CYS A . n 
A 1 149 VAL 149 153 153 VAL VAL A . n 
A 1 150 ASP 150 154 154 ASP ASP A . n 
A 1 151 SER 151 155 155 SER SER A . n 
A 1 152 ILE 152 156 156 ILE ILE A . n 
A 1 153 THR 153 157 157 THR THR A . n 
A 1 154 ALA 154 158 158 ALA ALA A . n 
A 1 155 LEU 155 159 159 LEU LEU A . n 
A 1 156 LYS 156 160 160 LYS LYS A . n 
A 1 157 ALA 157 161 161 ALA ALA A . n 
A 1 158 LEU 158 162 162 LEU LEU A . n 
A 1 159 GLU 159 163 163 GLU GLU A . n 
A 1 160 ARG 160 164 164 ARG ARG A . n 
A 1 161 ALA 161 165 165 ALA ALA A . n 
A 1 162 SER 162 166 166 SER SER A . n 
A 1 163 SER 163 167 167 SER SER A . n 
A 1 164 PRO 164 168 ?   ?   ?   A . n 
A 1 165 SER 165 169 ?   ?   ?   A . n 
A 1 166 GLU 166 170 ?   ?   ?   A . n 
A 1 167 HIS 167 171 ?   ?   ?   A . n 
A 1 168 GLY 168 172 ?   ?   ?   A . n 
A 1 169 PRO 169 173 ?   ?   ?   A . n 
A 1 170 ARG 170 174 ?   ?   ?   A . n 
A 1 171 LYS 171 175 175 LYS LYS A . n 
A 1 172 SER 172 176 176 SER SER A . n 
A 1 173 TYR 173 177 177 TYR TYR A . n 
A 1 174 SER 174 178 178 SER SER A . n 
A 1 175 LEU 175 179 179 LEU LEU A . n 
A 1 176 GLY 176 180 180 GLY GLY A . n 
A 1 177 SER 177 181 181 SER SER A . n 
A 1 178 ILE 178 182 182 ILE ILE A . n 
A 1 179 TYR 179 183 183 TYR TYR A . n 
A 1 180 THR 180 184 184 THR THR A . n 
A 1 181 ARG 181 185 185 ARG ARG A . n 
A 1 182 LEU 182 186 186 LEU LEU A . n 
A 1 183 TYR 183 187 187 TYR TYR A . n 
A 1 184 GLY 184 188 188 GLY GLY A . n 
A 1 185 GLN 185 189 189 GLN GLN A . n 
A 1 186 SER 186 190 190 SER SER A . n 
A 1 187 PRO 187 191 191 PRO PRO A . n 
A 1 188 PRO 188 192 192 PRO PRO A . n 
A 1 189 ASP 189 193 193 ASP ASP A . n 
A 1 190 SER 190 194 194 SER SER A . n 
A 1 191 HIS 191 195 195 HIS HIS A . n 
A 1 192 THR 192 196 196 THR THR A . n 
A 1 193 ALA 193 197 197 ALA ALA A . n 
A 1 194 GLU 194 198 198 GLU GLU A . n 
A 1 195 GLY 195 199 199 GLY GLY A . n 
A 1 196 ASP 196 200 200 ASP ASP A . n 
A 1 197 VAL 197 201 201 VAL VAL A . n 
A 1 198 LEU 198 202 202 LEU LEU A . n 
A 1 199 ALA 199 203 203 ALA ALA A . n 
A 1 200 LEU 200 204 204 LEU LEU A . n 
A 1 201 LEU 201 205 205 LEU LEU A . n 
A 1 202 SER 202 206 206 SER SER A . n 
A 1 203 ILE 203 207 207 ILE ILE A . n 
A 1 204 CYS 204 208 208 CYS CYS A . n 
A 1 205 GLN 205 209 209 GLN GLN A . n 
A 1 206 TRP 206 210 210 TRP TRP A . n 
A 1 207 ARG 207 211 211 ARG ARG A . n 
A 1 208 PRO 208 212 212 PRO PRO A . n 
A 1 209 GLN 209 213 213 GLN GLN A . n 
A 1 210 ALA 210 214 214 ALA ALA A . n 
A 1 211 LEU 211 215 215 LEU LEU A . n 
A 1 212 LEU 212 216 216 LEU LEU A . n 
A 1 213 ARG 213 217 217 ARG ARG A . n 
A 1 214 TRP 214 218 218 TRP TRP A . n 
A 1 215 VAL 215 219 219 VAL VAL A . n 
A 1 216 ASP 216 220 220 ASP ASP A . n 
A 1 217 ALA 217 221 221 ALA ALA A . n 
A 1 218 HIS 218 222 222 HIS HIS A . n 
A 1 219 ALA 219 223 223 ALA ALA A . n 
A 1 220 ARG 220 224 224 ARG ARG A . n 
A 1 221 PRO 221 225 225 PRO PRO A . n 
A 1 222 PHE 222 226 226 PHE PHE A . n 
A 1 223 GLY 223 227 227 GLY GLY A . n 
A 1 224 THR 224 228 228 THR THR A . n 
A 1 225 ILE 225 229 229 ILE ILE A . n 
A 1 226 ARG 226 230 230 ARG ARG A . n 
A 1 227 PRO 227 231 231 PRO PRO A . n 
A 1 228 MET 228 232 232 MET MET A . n 
A 1 229 TYR 229 233 233 TYR TYR A . n 
A 1 230 GLY 230 234 234 GLY GLY A . n 
A 1 231 VAL 231 235 ?   ?   ?   A . n 
A 1 232 THR 232 236 ?   ?   ?   A . n 
A 1 233 ALA 233 237 ?   ?   ?   A . n 
A 1 234 SER 234 238 ?   ?   ?   A . n 
B 1 1   ALA 1   5   5   ALA ALA B . n 
B 1 2   LEU 2   6   6   LEU LEU B . n 
B 1 3   PRO 3   7   7   PRO PRO B . n 
B 1 4   HIS 4   8   8   HIS HIS B . n 
B 1 5   GLY 5   9   9   GLY GLY B . n 
B 1 6   HIS 6   10  10  HIS HIS B . n 
B 1 7   MET 7   11  11  MET MET B . n 
B 1 8   GLN 8   12  12  GLN GLN B . n 
B 1 9   THR 9   13  13  THR THR B . n 
B 1 10  LEU 10  14  14  LEU LEU B . n 
B 1 11  ILE 11  15  15  ILE ILE B . n 
B 1 12  PHE 12  16  16  PHE PHE B . n 
B 1 13  PHE 13  17  17  PHE PHE B . n 
B 1 14  ASP 14  18  18  ASP ASP B . n 
B 1 15  MET 15  19  19  MET MET B . n 
B 1 16  GLU 16  20  20  GLU GLU B . n 
B 1 17  ALA 17  21  21  ALA ALA B . n 
B 1 18  THR 18  22  22  THR THR B . n 
B 1 19  GLY 19  23  23  GLY GLY B . n 
B 1 20  LEU 20  24  24  LEU LEU B . n 
B 1 21  PRO 21  25  25  PRO PRO B . n 
B 1 22  SER 22  26  26  SER SER B . n 
B 1 23  SER 23  27  27  SER SER B . n 
B 1 24  ARG 24  28  28  ARG ARG B . n 
B 1 25  PRO 25  29  29  PRO PRO B . n 
B 1 26  GLU 26  30  30  GLU GLU B . n 
B 1 27  VAL 27  31  31  VAL VAL B . n 
B 1 28  THR 28  32  32  THR THR B . n 
B 1 29  GLU 29  33  33  GLU GLU B . n 
B 1 30  LEU 30  34  34  LEU LEU B . n 
B 1 31  CYS 31  35  35  CYS CYS B . n 
B 1 32  LEU 32  36  36  LEU LEU B . n 
B 1 33  LEU 33  37  37  LEU LEU B . n 
B 1 34  ALA 34  38  38  ALA ALA B . n 
B 1 35  VAL 35  39  39  VAL VAL B . n 
B 1 36  HIS 36  40  40  HIS HIS B . n 
B 1 37  ARG 37  41  41  ARG ARG B . n 
B 1 38  CYS 38  42  42  CYS CYS B . n 
B 1 39  ALA 39  43  43  ALA ALA B . n 
B 1 40  LEU 40  44  44  LEU LEU B . n 
B 1 41  GLU 41  45  45  GLU GLU B . n 
B 1 42  SER 42  46  46  SER SER B . n 
B 1 43  PRO 43  47  47  PRO PRO B . n 
B 1 44  PRO 44  48  48  PRO PRO B . n 
B 1 45  THR 45  49  ?   ?   ?   B . n 
B 1 46  SER 46  50  ?   ?   ?   B . n 
B 1 47  GLN 47  51  ?   ?   ?   B . n 
B 1 48  GLY 48  52  ?   ?   ?   B . n 
B 1 49  PRO 49  53  ?   ?   ?   B . n 
B 1 50  PRO 50  54  ?   ?   ?   B . n 
B 1 51  PRO 51  55  55  PRO PRO B . n 
B 1 52  THR 52  56  56  THR THR B . n 
B 1 53  VAL 53  57  57  VAL VAL B . n 
B 1 54  PRO 54  58  58  PRO PRO B . n 
B 1 55  PRO 55  59  59  PRO PRO B . n 
B 1 56  PRO 56  60  60  PRO PRO B . n 
B 1 57  PRO 57  61  61  PRO PRO B . n 
B 1 58  ARG 58  62  62  ARG ARG B . n 
B 1 59  VAL 59  63  63  VAL VAL B . n 
B 1 60  VAL 60  64  64  VAL VAL B . n 
B 1 61  ASP 61  65  65  ASP ASP B . n 
B 1 62  LYS 62  66  66  LYS LYS B . n 
B 1 63  LEU 63  67  67  LEU LEU B . n 
B 1 64  SER 64  68  68  SER SER B . n 
B 1 65  LEU 65  69  69  LEU LEU B . n 
B 1 66  CYS 66  70  70  CYS CYS B . n 
B 1 67  VAL 67  71  71  VAL VAL B . n 
B 1 68  ALA 68  72  72  ALA ALA B . n 
B 1 69  PRO 69  73  73  PRO PRO B . n 
B 1 70  GLY 70  74  74  GLY GLY B . n 
B 1 71  LYS 71  75  75  LYS LYS B . n 
B 1 72  ALA 72  76  76  ALA ALA B . n 
B 1 73  CYS 73  77  77  CYS CYS B . n 
B 1 74  SER 74  78  78  SER SER B . n 
B 1 75  PRO 75  79  79  PRO PRO B . n 
B 1 76  ALA 76  80  80  ALA ALA B . n 
B 1 77  ALA 77  81  81  ALA ALA B . n 
B 1 78  SER 78  82  82  SER SER B . n 
B 1 79  GLU 79  83  83  GLU GLU B . n 
B 1 80  ILE 80  84  84  ILE ILE B . n 
B 1 81  THR 81  85  85  THR THR B . n 
B 1 82  GLY 82  86  86  GLY GLY B . n 
B 1 83  LEU 83  87  87  LEU LEU B . n 
B 1 84  SER 84  88  88  SER SER B . n 
B 1 85  THR 85  89  89  THR THR B . n 
B 1 86  ALA 86  90  90  ALA ALA B . n 
B 1 87  VAL 87  91  91  VAL VAL B . n 
B 1 88  LEU 88  92  92  LEU LEU B . n 
B 1 89  ALA 89  93  93  ALA ALA B . n 
B 1 90  ALA 90  94  94  ALA ALA B . n 
B 1 91  HIS 91  95  95  HIS HIS B . n 
B 1 92  GLY 92  96  96  GLY GLY B . n 
B 1 93  ARG 93  97  97  ARG ARG B . n 
B 1 94  GLN 94  98  98  GLN GLN B . n 
B 1 95  CYS 95  99  99  CYS CYS B . n 
B 1 96  PHE 96  100 100 PHE PHE B . n 
B 1 97  ASP 97  101 101 ASP ASP B . n 
B 1 98  ASP 98  102 102 ASP ASP B . n 
B 1 99  ASN 99  103 103 ASN ASN B . n 
B 1 100 LEU 100 104 104 LEU LEU B . n 
B 1 101 ALA 101 105 105 ALA ALA B . n 
B 1 102 ASN 102 106 106 ASN ASN B . n 
B 1 103 LEU 103 107 107 LEU LEU B . n 
B 1 104 LEU 104 108 108 LEU LEU B . n 
B 1 105 LEU 105 109 109 LEU LEU B . n 
B 1 106 ALA 106 110 110 ALA ALA B . n 
B 1 107 PHE 107 111 111 PHE PHE B . n 
B 1 108 LEU 108 112 112 LEU LEU B . n 
B 1 109 ARG 109 113 113 ARG ARG B . n 
B 1 110 ARG 110 114 114 ARG ARG B . n 
B 1 111 GLN 111 115 115 GLN GLN B . n 
B 1 112 PRO 112 116 116 PRO PRO B . n 
B 1 113 GLN 113 117 117 GLN GLN B . n 
B 1 114 PRO 114 118 118 PRO PRO B . n 
B 1 115 TRP 115 119 119 TRP TRP B . n 
B 1 116 CYS 116 120 120 CYS CYS B . n 
B 1 117 LEU 117 121 121 LEU LEU B . n 
B 1 118 VAL 118 122 122 VAL VAL B . n 
B 1 119 ALA 119 123 123 ALA ALA B . n 
B 1 120 HIS 120 124 124 HIS HIS B . n 
B 1 121 ASN 121 125 125 ASN ASN B . n 
B 1 122 GLY 122 126 126 GLY GLY B . n 
B 1 123 ASP 123 127 127 ASP ASP B . n 
B 1 124 ARG 124 128 128 ARG ARG B . n 
B 1 125 TYR 125 129 129 TYR TYR B . n 
B 1 126 ASP 126 130 130 ASP ASP B . n 
B 1 127 PHE 127 131 131 PHE PHE B . n 
B 1 128 PRO 128 132 132 PRO PRO B . n 
B 1 129 LEU 129 133 133 LEU LEU B . n 
B 1 130 LEU 130 134 134 LEU LEU B . n 
B 1 131 GLN 131 135 135 GLN GLN B . n 
B 1 132 ALA 132 136 136 ALA ALA B . n 
B 1 133 GLU 133 137 137 GLU GLU B . n 
B 1 134 LEU 134 138 138 LEU LEU B . n 
B 1 135 ALA 135 139 139 ALA ALA B . n 
B 1 136 MET 136 140 140 MET MET B . n 
B 1 137 LEU 137 141 141 LEU LEU B . n 
B 1 138 GLY 138 142 142 GLY GLY B . n 
B 1 139 LEU 139 143 143 LEU LEU B . n 
B 1 140 THR 140 144 144 THR THR B . n 
B 1 141 SER 141 145 145 SER SER B . n 
B 1 142 ALA 142 146 146 ALA ALA B . n 
B 1 143 LEU 143 147 147 LEU LEU B . n 
B 1 144 ASP 144 148 148 ASP ASP B . n 
B 1 145 GLY 145 149 149 GLY GLY B . n 
B 1 146 ALA 146 150 150 ALA ALA B . n 
B 1 147 PHE 147 151 151 PHE PHE B . n 
B 1 148 CYS 148 152 152 CYS CYS B . n 
B 1 149 VAL 149 153 153 VAL VAL B . n 
B 1 150 ASP 150 154 154 ASP ASP B . n 
B 1 151 SER 151 155 155 SER SER B . n 
B 1 152 ILE 152 156 156 ILE ILE B . n 
B 1 153 THR 153 157 157 THR THR B . n 
B 1 154 ALA 154 158 158 ALA ALA B . n 
B 1 155 LEU 155 159 159 LEU LEU B . n 
B 1 156 LYS 156 160 160 LYS LYS B . n 
B 1 157 ALA 157 161 161 ALA ALA B . n 
B 1 158 LEU 158 162 162 LEU LEU B . n 
B 1 159 GLU 159 163 163 GLU GLU B . n 
B 1 160 ARG 160 164 164 ARG ARG B . n 
B 1 161 ALA 161 165 165 ALA ALA B . n 
B 1 162 SER 162 166 ?   ?   ?   B . n 
B 1 163 SER 163 167 ?   ?   ?   B . n 
B 1 164 PRO 164 168 ?   ?   ?   B . n 
B 1 165 SER 165 169 ?   ?   ?   B . n 
B 1 166 GLU 166 170 ?   ?   ?   B . n 
B 1 167 HIS 167 171 ?   ?   ?   B . n 
B 1 168 GLY 168 172 ?   ?   ?   B . n 
B 1 169 PRO 169 173 ?   ?   ?   B . n 
B 1 170 ARG 170 174 ?   ?   ?   B . n 
B 1 171 LYS 171 175 175 LYS LYS B . n 
B 1 172 SER 172 176 176 SER SER B . n 
B 1 173 TYR 173 177 177 TYR TYR B . n 
B 1 174 SER 174 178 178 SER SER B . n 
B 1 175 LEU 175 179 179 LEU LEU B . n 
B 1 176 GLY 176 180 180 GLY GLY B . n 
B 1 177 SER 177 181 181 SER SER B . n 
B 1 178 ILE 178 182 182 ILE ILE B . n 
B 1 179 TYR 179 183 183 TYR TYR B . n 
B 1 180 THR 180 184 184 THR THR B . n 
B 1 181 ARG 181 185 185 ARG ARG B . n 
B 1 182 LEU 182 186 186 LEU LEU B . n 
B 1 183 TYR 183 187 187 TYR TYR B . n 
B 1 184 GLY 184 188 188 GLY GLY B . n 
B 1 185 GLN 185 189 189 GLN GLN B . n 
B 1 186 SER 186 190 190 SER SER B . n 
B 1 187 PRO 187 191 191 PRO PRO B . n 
B 1 188 PRO 188 192 192 PRO PRO B . n 
B 1 189 ASP 189 193 193 ASP ASP B . n 
B 1 190 SER 190 194 194 SER SER B . n 
B 1 191 HIS 191 195 195 HIS HIS B . n 
B 1 192 THR 192 196 196 THR THR B . n 
B 1 193 ALA 193 197 197 ALA ALA B . n 
B 1 194 GLU 194 198 198 GLU GLU B . n 
B 1 195 GLY 195 199 199 GLY GLY B . n 
B 1 196 ASP 196 200 200 ASP ASP B . n 
B 1 197 VAL 197 201 201 VAL VAL B . n 
B 1 198 LEU 198 202 202 LEU LEU B . n 
B 1 199 ALA 199 203 203 ALA ALA B . n 
B 1 200 LEU 200 204 204 LEU LEU B . n 
B 1 201 LEU 201 205 205 LEU LEU B . n 
B 1 202 SER 202 206 206 SER SER B . n 
B 1 203 ILE 203 207 207 ILE ILE B . n 
B 1 204 CYS 204 208 208 CYS CYS B . n 
B 1 205 GLN 205 209 209 GLN GLN B . n 
B 1 206 TRP 206 210 210 TRP TRP B . n 
B 1 207 ARG 207 211 211 ARG ARG B . n 
B 1 208 PRO 208 212 212 PRO PRO B . n 
B 1 209 GLN 209 213 213 GLN GLN B . n 
B 1 210 ALA 210 214 214 ALA ALA B . n 
B 1 211 LEU 211 215 215 LEU LEU B . n 
B 1 212 LEU 212 216 216 LEU LEU B . n 
B 1 213 ARG 213 217 217 ARG ARG B . n 
B 1 214 TRP 214 218 218 TRP TRP B . n 
B 1 215 VAL 215 219 219 VAL VAL B . n 
B 1 216 ASP 216 220 220 ASP ASP B . n 
B 1 217 ALA 217 221 221 ALA ALA B . n 
B 1 218 HIS 218 222 222 HIS HIS B . n 
B 1 219 ALA 219 223 223 ALA ALA B . n 
B 1 220 ARG 220 224 224 ARG ARG B . n 
B 1 221 PRO 221 225 225 PRO PRO B . n 
B 1 222 PHE 222 226 226 PHE PHE B . n 
B 1 223 GLY 223 227 227 GLY GLY B . n 
B 1 224 THR 224 228 228 THR THR B . n 
B 1 225 ILE 225 229 229 ILE ILE B . n 
B 1 226 ARG 226 230 230 ARG ARG B . n 
B 1 227 PRO 227 231 231 PRO PRO B . n 
B 1 228 MET 228 232 232 MET MET B . n 
B 1 229 TYR 229 233 233 TYR TYR B . n 
B 1 230 GLY 230 234 234 GLY GLY B . n 
B 1 231 VAL 231 235 235 VAL VAL B . n 
B 1 232 THR 232 236 236 THR THR B . n 
B 1 233 ALA 233 237 ?   ?   ?   B . n 
B 1 234 SER 234 238 ?   ?   ?   B . n 
C 1 1   ALA 1   5   ?   ?   ?   C . n 
C 1 2   LEU 2   6   6   LEU LEU C . n 
C 1 3   PRO 3   7   7   PRO PRO C . n 
C 1 4   HIS 4   8   8   HIS HIS C . n 
C 1 5   GLY 5   9   9   GLY GLY C . n 
C 1 6   HIS 6   10  10  HIS HIS C . n 
C 1 7   MET 7   11  11  MET MET C . n 
C 1 8   GLN 8   12  12  GLN GLN C . n 
C 1 9   THR 9   13  13  THR THR C . n 
C 1 10  LEU 10  14  14  LEU LEU C . n 
C 1 11  ILE 11  15  15  ILE ILE C . n 
C 1 12  PHE 12  16  16  PHE PHE C . n 
C 1 13  PHE 13  17  17  PHE PHE C . n 
C 1 14  ASP 14  18  18  ASP ASP C . n 
C 1 15  MET 15  19  19  MET MET C . n 
C 1 16  GLU 16  20  20  GLU GLU C . n 
C 1 17  ALA 17  21  21  ALA ALA C . n 
C 1 18  THR 18  22  22  THR THR C . n 
C 1 19  GLY 19  23  23  GLY GLY C . n 
C 1 20  LEU 20  24  24  LEU LEU C . n 
C 1 21  PRO 21  25  25  PRO PRO C . n 
C 1 22  SER 22  26  26  SER SER C . n 
C 1 23  SER 23  27  27  SER SER C . n 
C 1 24  ARG 24  28  28  ARG ARG C . n 
C 1 25  PRO 25  29  29  PRO PRO C . n 
C 1 26  GLU 26  30  30  GLU GLU C . n 
C 1 27  VAL 27  31  31  VAL VAL C . n 
C 1 28  THR 28  32  32  THR THR C . n 
C 1 29  GLU 29  33  33  GLU GLU C . n 
C 1 30  LEU 30  34  34  LEU LEU C . n 
C 1 31  CYS 31  35  35  CYS CYS C . n 
C 1 32  LEU 32  36  36  LEU LEU C . n 
C 1 33  LEU 33  37  37  LEU LEU C . n 
C 1 34  ALA 34  38  38  ALA ALA C . n 
C 1 35  VAL 35  39  39  VAL VAL C . n 
C 1 36  HIS 36  40  40  HIS HIS C . n 
C 1 37  ARG 37  41  41  ARG ARG C . n 
C 1 38  CYS 38  42  42  CYS CYS C . n 
C 1 39  ALA 39  43  43  ALA ALA C . n 
C 1 40  LEU 40  44  44  LEU LEU C . n 
C 1 41  GLU 41  45  45  GLU GLU C . n 
C 1 42  SER 42  46  46  SER SER C . n 
C 1 43  PRO 43  47  47  PRO PRO C . n 
C 1 44  PRO 44  48  48  PRO PRO C . n 
C 1 45  THR 45  49  ?   ?   ?   C . n 
C 1 46  SER 46  50  ?   ?   ?   C . n 
C 1 47  GLN 47  51  ?   ?   ?   C . n 
C 1 48  GLY 48  52  ?   ?   ?   C . n 
C 1 49  PRO 49  53  ?   ?   ?   C . n 
C 1 50  PRO 50  54  ?   ?   ?   C . n 
C 1 51  PRO 51  55  ?   ?   ?   C . n 
C 1 52  THR 52  56  56  THR THR C . n 
C 1 53  VAL 53  57  57  VAL VAL C . n 
C 1 54  PRO 54  58  58  PRO PRO C . n 
C 1 55  PRO 55  59  59  PRO PRO C . n 
C 1 56  PRO 56  60  60  PRO PRO C . n 
C 1 57  PRO 57  61  61  PRO PRO C . n 
C 1 58  ARG 58  62  62  ARG ARG C . n 
C 1 59  VAL 59  63  63  VAL VAL C . n 
C 1 60  VAL 60  64  64  VAL VAL C . n 
C 1 61  ASP 61  65  65  ASP ASP C . n 
C 1 62  LYS 62  66  66  LYS LYS C . n 
C 1 63  LEU 63  67  67  LEU LEU C . n 
C 1 64  SER 64  68  68  SER SER C . n 
C 1 65  LEU 65  69  69  LEU LEU C . n 
C 1 66  CYS 66  70  70  CYS CYS C . n 
C 1 67  VAL 67  71  71  VAL VAL C . n 
C 1 68  ALA 68  72  72  ALA ALA C . n 
C 1 69  PRO 69  73  73  PRO PRO C . n 
C 1 70  GLY 70  74  74  GLY GLY C . n 
C 1 71  LYS 71  75  75  LYS LYS C . n 
C 1 72  ALA 72  76  76  ALA ALA C . n 
C 1 73  CYS 73  77  77  CYS CYS C . n 
C 1 74  SER 74  78  78  SER SER C . n 
C 1 75  PRO 75  79  79  PRO PRO C . n 
C 1 76  ALA 76  80  80  ALA ALA C . n 
C 1 77  ALA 77  81  81  ALA ALA C . n 
C 1 78  SER 78  82  82  SER SER C . n 
C 1 79  GLU 79  83  83  GLU GLU C . n 
C 1 80  ILE 80  84  84  ILE ILE C . n 
C 1 81  THR 81  85  85  THR THR C . n 
C 1 82  GLY 82  86  86  GLY GLY C . n 
C 1 83  LEU 83  87  87  LEU LEU C . n 
C 1 84  SER 84  88  88  SER SER C . n 
C 1 85  THR 85  89  89  THR THR C . n 
C 1 86  ALA 86  90  90  ALA ALA C . n 
C 1 87  VAL 87  91  91  VAL VAL C . n 
C 1 88  LEU 88  92  92  LEU LEU C . n 
C 1 89  ALA 89  93  93  ALA ALA C . n 
C 1 90  ALA 90  94  94  ALA ALA C . n 
C 1 91  HIS 91  95  95  HIS HIS C . n 
C 1 92  GLY 92  96  96  GLY GLY C . n 
C 1 93  ARG 93  97  97  ARG ARG C . n 
C 1 94  GLN 94  98  98  GLN GLN C . n 
C 1 95  CYS 95  99  99  CYS CYS C . n 
C 1 96  PHE 96  100 100 PHE PHE C . n 
C 1 97  ASP 97  101 101 ASP ASP C . n 
C 1 98  ASP 98  102 102 ASP ASP C . n 
C 1 99  ASN 99  103 103 ASN ASN C . n 
C 1 100 LEU 100 104 104 LEU LEU C . n 
C 1 101 ALA 101 105 105 ALA ALA C . n 
C 1 102 ASN 102 106 106 ASN ASN C . n 
C 1 103 LEU 103 107 107 LEU LEU C . n 
C 1 104 LEU 104 108 108 LEU LEU C . n 
C 1 105 LEU 105 109 109 LEU LEU C . n 
C 1 106 ALA 106 110 110 ALA ALA C . n 
C 1 107 PHE 107 111 111 PHE PHE C . n 
C 1 108 LEU 108 112 112 LEU LEU C . n 
C 1 109 ARG 109 113 113 ARG ARG C . n 
C 1 110 ARG 110 114 114 ARG ARG C . n 
C 1 111 GLN 111 115 115 GLN GLN C . n 
C 1 112 PRO 112 116 116 PRO PRO C . n 
C 1 113 GLN 113 117 117 GLN GLN C . n 
C 1 114 PRO 114 118 118 PRO PRO C . n 
C 1 115 TRP 115 119 119 TRP TRP C . n 
C 1 116 CYS 116 120 120 CYS CYS C . n 
C 1 117 LEU 117 121 121 LEU LEU C . n 
C 1 118 VAL 118 122 122 VAL VAL C . n 
C 1 119 ALA 119 123 123 ALA ALA C . n 
C 1 120 HIS 120 124 124 HIS HIS C . n 
C 1 121 ASN 121 125 125 ASN ASN C . n 
C 1 122 GLY 122 126 126 GLY GLY C . n 
C 1 123 ASP 123 127 127 ASP ASP C . n 
C 1 124 ARG 124 128 128 ARG ARG C . n 
C 1 125 TYR 125 129 129 TYR TYR C . n 
C 1 126 ASP 126 130 130 ASP ASP C . n 
C 1 127 PHE 127 131 131 PHE PHE C . n 
C 1 128 PRO 128 132 132 PRO PRO C . n 
C 1 129 LEU 129 133 133 LEU LEU C . n 
C 1 130 LEU 130 134 134 LEU LEU C . n 
C 1 131 GLN 131 135 135 GLN GLN C . n 
C 1 132 ALA 132 136 136 ALA ALA C . n 
C 1 133 GLU 133 137 137 GLU GLU C . n 
C 1 134 LEU 134 138 138 LEU LEU C . n 
C 1 135 ALA 135 139 139 ALA ALA C . n 
C 1 136 MET 136 140 140 MET MET C . n 
C 1 137 LEU 137 141 141 LEU LEU C . n 
C 1 138 GLY 138 142 142 GLY GLY C . n 
C 1 139 LEU 139 143 143 LEU LEU C . n 
C 1 140 THR 140 144 144 THR THR C . n 
C 1 141 SER 141 145 145 SER SER C . n 
C 1 142 ALA 142 146 146 ALA ALA C . n 
C 1 143 LEU 143 147 147 LEU LEU C . n 
C 1 144 ASP 144 148 148 ASP ASP C . n 
C 1 145 GLY 145 149 149 GLY GLY C . n 
C 1 146 ALA 146 150 150 ALA ALA C . n 
C 1 147 PHE 147 151 151 PHE PHE C . n 
C 1 148 CYS 148 152 152 CYS CYS C . n 
C 1 149 VAL 149 153 153 VAL VAL C . n 
C 1 150 ASP 150 154 154 ASP ASP C . n 
C 1 151 SER 151 155 155 SER SER C . n 
C 1 152 ILE 152 156 156 ILE ILE C . n 
C 1 153 THR 153 157 157 THR THR C . n 
C 1 154 ALA 154 158 158 ALA ALA C . n 
C 1 155 LEU 155 159 159 LEU LEU C . n 
C 1 156 LYS 156 160 160 LYS LYS C . n 
C 1 157 ALA 157 161 161 ALA ALA C . n 
C 1 158 LEU 158 162 162 LEU LEU C . n 
C 1 159 GLU 159 163 163 GLU GLU C . n 
C 1 160 ARG 160 164 ?   ?   ?   C . n 
C 1 161 ALA 161 165 ?   ?   ?   C . n 
C 1 162 SER 162 166 ?   ?   ?   C . n 
C 1 163 SER 163 167 ?   ?   ?   C . n 
C 1 164 PRO 164 168 ?   ?   ?   C . n 
C 1 165 SER 165 169 ?   ?   ?   C . n 
C 1 166 GLU 166 170 ?   ?   ?   C . n 
C 1 167 HIS 167 171 ?   ?   ?   C . n 
C 1 168 GLY 168 172 ?   ?   ?   C . n 
C 1 169 PRO 169 173 ?   ?   ?   C . n 
C 1 170 ARG 170 174 ?   ?   ?   C . n 
C 1 171 LYS 171 175 175 LYS LYS C . n 
C 1 172 SER 172 176 176 SER SER C . n 
C 1 173 TYR 173 177 177 TYR TYR C . n 
C 1 174 SER 174 178 178 SER SER C . n 
C 1 175 LEU 175 179 179 LEU LEU C . n 
C 1 176 GLY 176 180 180 GLY GLY C . n 
C 1 177 SER 177 181 181 SER SER C . n 
C 1 178 ILE 178 182 182 ILE ILE C . n 
C 1 179 TYR 179 183 183 TYR TYR C . n 
C 1 180 THR 180 184 184 THR THR C . n 
C 1 181 ARG 181 185 185 ARG ARG C . n 
C 1 182 LEU 182 186 186 LEU LEU C . n 
C 1 183 TYR 183 187 187 TYR TYR C . n 
C 1 184 GLY 184 188 188 GLY GLY C . n 
C 1 185 GLN 185 189 189 GLN GLN C . n 
C 1 186 SER 186 190 190 SER SER C . n 
C 1 187 PRO 187 191 191 PRO PRO C . n 
C 1 188 PRO 188 192 192 PRO PRO C . n 
C 1 189 ASP 189 193 193 ASP ASP C . n 
C 1 190 SER 190 194 194 SER SER C . n 
C 1 191 HIS 191 195 195 HIS HIS C . n 
C 1 192 THR 192 196 196 THR THR C . n 
C 1 193 ALA 193 197 197 ALA ALA C . n 
C 1 194 GLU 194 198 198 GLU GLU C . n 
C 1 195 GLY 195 199 199 GLY GLY C . n 
C 1 196 ASP 196 200 200 ASP ASP C . n 
C 1 197 VAL 197 201 201 VAL VAL C . n 
C 1 198 LEU 198 202 202 LEU LEU C . n 
C 1 199 ALA 199 203 203 ALA ALA C . n 
C 1 200 LEU 200 204 204 LEU LEU C . n 
C 1 201 LEU 201 205 205 LEU LEU C . n 
C 1 202 SER 202 206 206 SER SER C . n 
C 1 203 ILE 203 207 207 ILE ILE C . n 
C 1 204 CYS 204 208 208 CYS CYS C . n 
C 1 205 GLN 205 209 209 GLN GLN C . n 
C 1 206 TRP 206 210 210 TRP TRP C . n 
C 1 207 ARG 207 211 211 ARG ARG C . n 
C 1 208 PRO 208 212 212 PRO PRO C . n 
C 1 209 GLN 209 213 213 GLN GLN C . n 
C 1 210 ALA 210 214 214 ALA ALA C . n 
C 1 211 LEU 211 215 215 LEU LEU C . n 
C 1 212 LEU 212 216 216 LEU LEU C . n 
C 1 213 ARG 213 217 217 ARG ARG C . n 
C 1 214 TRP 214 218 218 TRP TRP C . n 
C 1 215 VAL 215 219 219 VAL VAL C . n 
C 1 216 ASP 216 220 220 ASP ASP C . n 
C 1 217 ALA 217 221 221 ALA ALA C . n 
C 1 218 HIS 218 222 222 HIS HIS C . n 
C 1 219 ALA 219 223 223 ALA ALA C . n 
C 1 220 ARG 220 224 224 ARG ARG C . n 
C 1 221 PRO 221 225 225 PRO PRO C . n 
C 1 222 PHE 222 226 226 PHE PHE C . n 
C 1 223 GLY 223 227 227 GLY GLY C . n 
C 1 224 THR 224 228 228 THR THR C . n 
C 1 225 ILE 225 229 229 ILE ILE C . n 
C 1 226 ARG 226 230 230 ARG ARG C . n 
C 1 227 PRO 227 231 231 PRO PRO C . n 
C 1 228 MET 228 232 232 MET MET C . n 
C 1 229 TYR 229 233 233 TYR TYR C . n 
C 1 230 GLY 230 234 234 GLY GLY C . n 
C 1 231 VAL 231 235 235 VAL VAL C . n 
C 1 232 THR 232 236 ?   ?   ?   C . n 
C 1 233 ALA 233 237 ?   ?   ?   C . n 
C 1 234 SER 234 238 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B7T 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B7T 
_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 
D 2 A1B7T 1   301 301  A1B7T LIG A . 
E 3 MG    1   302 302  MG    MG  A . 
F 4 EDO   1   303 303  EDO   EDO A . 
G 5 UNX   1   304 1001 UNX   UNX A . 
H 5 UNX   1   305 1002 UNX   UNX A . 
I 2 A1B7T 1   301 301  A1B7T LIG B . 
J 3 MG    1   302 302  MG    MG  B . 
K 4 EDO   1   303 303  EDO   EDO B . 
L 5 UNX   1   304 1004 UNX   UNX B . 
M 5 UNX   1   305 1005 UNX   UNX B . 
N 2 A1B7T 1   301 301  A1B7T LIG C . 
O 3 MG    1   302 302  MG    MG  C . 
P 4 EDO   1   303 303  EDO   EDO C . 
Q 4 EDO   1   304 304  EDO   EDO C . 
R 5 UNX   1   305 1003 UNX   UNX C . 
S 5 UNX   1   306 1006 UNX   UNX C . 
T 6 HOH   1   401 279  HOH   HOH A . 
T 6 HOH   2   402 191  HOH   HOH A . 
T 6 HOH   3   403 311  HOH   HOH A . 
T 6 HOH   4   404 117  HOH   HOH A . 
T 6 HOH   5   405 127  HOH   HOH A . 
T 6 HOH   6   406 326  HOH   HOH A . 
T 6 HOH   7   407 22   HOH   HOH A . 
T 6 HOH   8   408 154  HOH   HOH A . 
T 6 HOH   9   409 301  HOH   HOH A . 
T 6 HOH   10  410 125  HOH   HOH A . 
T 6 HOH   11  411 451  HOH   HOH A . 
T 6 HOH   12  412 345  HOH   HOH A . 
T 6 HOH   13  413 452  HOH   HOH A . 
T 6 HOH   14  414 356  HOH   HOH A . 
T 6 HOH   15  415 196  HOH   HOH A . 
T 6 HOH   16  416 388  HOH   HOH A . 
T 6 HOH   17  417 231  HOH   HOH A . 
T 6 HOH   18  418 350  HOH   HOH A . 
T 6 HOH   19  419 336  HOH   HOH A . 
T 6 HOH   20  420 49   HOH   HOH A . 
T 6 HOH   21  421 479  HOH   HOH A . 
T 6 HOH   22  422 450  HOH   HOH A . 
T 6 HOH   23  423 306  HOH   HOH A . 
T 6 HOH   24  424 57   HOH   HOH A . 
T 6 HOH   25  425 54   HOH   HOH A . 
T 6 HOH   26  426 121  HOH   HOH A . 
T 6 HOH   27  427 66   HOH   HOH A . 
T 6 HOH   28  428 42   HOH   HOH A . 
T 6 HOH   29  429 471  HOH   HOH A . 
T 6 HOH   30  430 374  HOH   HOH A . 
T 6 HOH   31  431 53   HOH   HOH A . 
T 6 HOH   32  432 498  HOH   HOH A . 
T 6 HOH   33  433 123  HOH   HOH A . 
T 6 HOH   34  434 76   HOH   HOH A . 
T 6 HOH   35  435 503  HOH   HOH A . 
T 6 HOH   36  436 208  HOH   HOH A . 
T 6 HOH   37  437 177  HOH   HOH A . 
T 6 HOH   38  438 375  HOH   HOH A . 
T 6 HOH   39  439 187  HOH   HOH A . 
T 6 HOH   40  440 183  HOH   HOH A . 
T 6 HOH   41  441 237  HOH   HOH A . 
T 6 HOH   42  442 268  HOH   HOH A . 
T 6 HOH   43  443 391  HOH   HOH A . 
T 6 HOH   44  444 97   HOH   HOH A . 
T 6 HOH   45  445 192  HOH   HOH A . 
T 6 HOH   46  446 352  HOH   HOH A . 
T 6 HOH   47  447 81   HOH   HOH A . 
T 6 HOH   48  448 310  HOH   HOH A . 
T 6 HOH   49  449 473  HOH   HOH A . 
T 6 HOH   50  450 60   HOH   HOH A . 
T 6 HOH   51  451 282  HOH   HOH A . 
T 6 HOH   52  452 334  HOH   HOH A . 
T 6 HOH   53  453 172  HOH   HOH A . 
T 6 HOH   54  454 158  HOH   HOH A . 
T 6 HOH   55  455 1    HOH   HOH A . 
T 6 HOH   56  456 533  HOH   HOH A . 
T 6 HOH   57  457 151  HOH   HOH A . 
T 6 HOH   58  458 5    HOH   HOH A . 
T 6 HOH   59  459 139  HOH   HOH A . 
T 6 HOH   60  460 92   HOH   HOH A . 
T 6 HOH   61  461 55   HOH   HOH A . 
T 6 HOH   62  462 51   HOH   HOH A . 
T 6 HOH   63  463 293  HOH   HOH A . 
T 6 HOH   64  464 40   HOH   HOH A . 
T 6 HOH   65  465 430  HOH   HOH A . 
T 6 HOH   66  466 300  HOH   HOH A . 
T 6 HOH   67  467 253  HOH   HOH A . 
T 6 HOH   68  468 38   HOH   HOH A . 
T 6 HOH   69  469 169  HOH   HOH A . 
T 6 HOH   70  470 328  HOH   HOH A . 
T 6 HOH   71  471 236  HOH   HOH A . 
T 6 HOH   72  472 83   HOH   HOH A . 
T 6 HOH   73  473 115  HOH   HOH A . 
T 6 HOH   74  474 360  HOH   HOH A . 
T 6 HOH   75  475 516  HOH   HOH A . 
T 6 HOH   76  476 536  HOH   HOH A . 
T 6 HOH   77  477 8    HOH   HOH A . 
T 6 HOH   78  478 126  HOH   HOH A . 
T 6 HOH   79  479 232  HOH   HOH A . 
T 6 HOH   80  480 58   HOH   HOH A . 
T 6 HOH   81  481 2    HOH   HOH A . 
T 6 HOH   82  482 56   HOH   HOH A . 
T 6 HOH   83  483 80   HOH   HOH A . 
T 6 HOH   84  484 302  HOH   HOH A . 
T 6 HOH   85  485 205  HOH   HOH A . 
T 6 HOH   86  486 295  HOH   HOH A . 
T 6 HOH   87  487 318  HOH   HOH A . 
T 6 HOH   88  488 219  HOH   HOH A . 
T 6 HOH   89  489 214  HOH   HOH A . 
T 6 HOH   90  490 48   HOH   HOH A . 
T 6 HOH   91  491 256  HOH   HOH A . 
T 6 HOH   92  492 323  HOH   HOH A . 
T 6 HOH   93  493 304  HOH   HOH A . 
T 6 HOH   94  494 453  HOH   HOH A . 
T 6 HOH   95  495 166  HOH   HOH A . 
T 6 HOH   96  496 382  HOH   HOH A . 
T 6 HOH   97  497 31   HOH   HOH A . 
T 6 HOH   98  498 16   HOH   HOH A . 
T 6 HOH   99  499 141  HOH   HOH A . 
T 6 HOH   100 500 24   HOH   HOH A . 
T 6 HOH   101 501 540  HOH   HOH A . 
T 6 HOH   102 502 227  HOH   HOH A . 
T 6 HOH   103 503 270  HOH   HOH A . 
T 6 HOH   104 504 225  HOH   HOH A . 
T 6 HOH   105 505 50   HOH   HOH A . 
T 6 HOH   106 506 64   HOH   HOH A . 
T 6 HOH   107 507 361  HOH   HOH A . 
T 6 HOH   108 508 69   HOH   HOH A . 
T 6 HOH   109 509 412  HOH   HOH A . 
T 6 HOH   110 510 70   HOH   HOH A . 
T 6 HOH   111 511 181  HOH   HOH A . 
T 6 HOH   112 512 251  HOH   HOH A . 
T 6 HOH   113 513 37   HOH   HOH A . 
T 6 HOH   114 514 101  HOH   HOH A . 
T 6 HOH   115 515 257  HOH   HOH A . 
T 6 HOH   116 516 62   HOH   HOH A . 
T 6 HOH   117 517 28   HOH   HOH A . 
T 6 HOH   118 518 528  HOH   HOH A . 
T 6 HOH   119 519 197  HOH   HOH A . 
T 6 HOH   120 520 428  HOH   HOH A . 
T 6 HOH   121 521 486  HOH   HOH A . 
T 6 HOH   122 522 340  HOH   HOH A . 
T 6 HOH   123 523 373  HOH   HOH A . 
T 6 HOH   124 524 444  HOH   HOH A . 
T 6 HOH   125 525 288  HOH   HOH A . 
T 6 HOH   126 526 517  HOH   HOH A . 
T 6 HOH   127 527 4    HOH   HOH A . 
T 6 HOH   128 528 320  HOH   HOH A . 
T 6 HOH   129 529 383  HOH   HOH A . 
T 6 HOH   130 530 190  HOH   HOH A . 
T 6 HOH   131 531 372  HOH   HOH A . 
T 6 HOH   132 532 247  HOH   HOH A . 
T 6 HOH   133 533 419  HOH   HOH A . 
T 6 HOH   134 534 487  HOH   HOH A . 
T 6 HOH   135 535 193  HOH   HOH A . 
T 6 HOH   136 536 210  HOH   HOH A . 
T 6 HOH   137 537 525  HOH   HOH A . 
T 6 HOH   138 538 400  HOH   HOH A . 
T 6 HOH   139 539 495  HOH   HOH A . 
T 6 HOH   140 540 342  HOH   HOH A . 
T 6 HOH   141 541 529  HOH   HOH A . 
T 6 HOH   142 542 413  HOH   HOH A . 
T 6 HOH   143 543 494  HOH   HOH A . 
T 6 HOH   144 544 417  HOH   HOH A . 
T 6 HOH   145 545 515  HOH   HOH A . 
T 6 HOH   146 546 325  HOH   HOH A . 
T 6 HOH   147 547 332  HOH   HOH A . 
T 6 HOH   148 548 524  HOH   HOH A . 
T 6 HOH   149 549 124  HOH   HOH A . 
T 6 HOH   150 550 316  HOH   HOH A . 
T 6 HOH   151 551 518  HOH   HOH A . 
T 6 HOH   152 552 422  HOH   HOH A . 
T 6 HOH   153 553 59   HOH   HOH A . 
T 6 HOH   154 554 511  HOH   HOH A . 
T 6 HOH   155 555 386  HOH   HOH A . 
T 6 HOH   156 556 202  HOH   HOH A . 
T 6 HOH   157 557 445  HOH   HOH A . 
T 6 HOH   158 558 331  HOH   HOH A . 
T 6 HOH   159 559 133  HOH   HOH A . 
T 6 HOH   160 560 249  HOH   HOH A . 
T 6 HOH   161 561 496  HOH   HOH A . 
T 6 HOH   162 562 502  HOH   HOH A . 
T 6 HOH   163 563 189  HOH   HOH A . 
T 6 HOH   164 564 174  HOH   HOH A . 
T 6 HOH   165 565 102  HOH   HOH A . 
T 6 HOH   166 566 514  HOH   HOH A . 
T 6 HOH   167 567 142  HOH   HOH A . 
T 6 HOH   168 568 488  HOH   HOH A . 
T 6 HOH   169 569 531  HOH   HOH A . 
T 6 HOH   170 570 535  HOH   HOH A . 
T 6 HOH   171 571 364  HOH   HOH A . 
T 6 HOH   172 572 384  HOH   HOH A . 
T 6 HOH   173 573 199  HOH   HOH A . 
T 6 HOH   174 574 160  HOH   HOH A . 
T 6 HOH   175 575 431  HOH   HOH A . 
T 6 HOH   176 576 500  HOH   HOH A . 
T 6 HOH   177 577 171  HOH   HOH A . 
T 6 HOH   178 578 138  HOH   HOH A . 
T 6 HOH   179 579 429  HOH   HOH A . 
T 6 HOH   180 580 489  HOH   HOH A . 
U 6 HOH   1   401 347  HOH   HOH B . 
U 6 HOH   2   402 261  HOH   HOH B . 
U 6 HOH   3   403 175  HOH   HOH B . 
U 6 HOH   4   404 381  HOH   HOH B . 
U 6 HOH   5   405 6    HOH   HOH B . 
U 6 HOH   6   406 298  HOH   HOH B . 
U 6 HOH   7   407 113  HOH   HOH B . 
U 6 HOH   8   408 398  HOH   HOH B . 
U 6 HOH   9   409 33   HOH   HOH B . 
U 6 HOH   10  410 91   HOH   HOH B . 
U 6 HOH   11  411 321  HOH   HOH B . 
U 6 HOH   12  412 25   HOH   HOH B . 
U 6 HOH   13  413 507  HOH   HOH B . 
U 6 HOH   14  414 94   HOH   HOH B . 
U 6 HOH   15  415 104  HOH   HOH B . 
U 6 HOH   16  416 506  HOH   HOH B . 
U 6 HOH   17  417 454  HOH   HOH B . 
U 6 HOH   18  418 243  HOH   HOH B . 
U 6 HOH   19  419 271  HOH   HOH B . 
U 6 HOH   20  420 392  HOH   HOH B . 
U 6 HOH   21  421 150  HOH   HOH B . 
U 6 HOH   22  422 276  HOH   HOH B . 
U 6 HOH   23  423 456  HOH   HOH B . 
U 6 HOH   24  424 45   HOH   HOH B . 
U 6 HOH   25  425 504  HOH   HOH B . 
U 6 HOH   26  426 509  HOH   HOH B . 
U 6 HOH   27  427 296  HOH   HOH B . 
U 6 HOH   28  428 278  HOH   HOH B . 
U 6 HOH   29  429 307  HOH   HOH B . 
U 6 HOH   30  430 380  HOH   HOH B . 
U 6 HOH   31  431 280  HOH   HOH B . 
U 6 HOH   32  432 186  HOH   HOH B . 
U 6 HOH   33  433 211  HOH   HOH B . 
U 6 HOH   34  434 281  HOH   HOH B . 
U 6 HOH   35  435 217  HOH   HOH B . 
U 6 HOH   36  436 472  HOH   HOH B . 
U 6 HOH   37  437 170  HOH   HOH B . 
U 6 HOH   38  438 455  HOH   HOH B . 
U 6 HOH   39  439 67   HOH   HOH B . 
U 6 HOH   40  440 176  HOH   HOH B . 
U 6 HOH   41  441 167  HOH   HOH B . 
U 6 HOH   42  442 23   HOH   HOH B . 
U 6 HOH   43  443 106  HOH   HOH B . 
U 6 HOH   44  444 252  HOH   HOH B . 
U 6 HOH   45  445 365  HOH   HOH B . 
U 6 HOH   46  446 294  HOH   HOH B . 
U 6 HOH   47  447 114  HOH   HOH B . 
U 6 HOH   48  448 421  HOH   HOH B . 
U 6 HOH   49  449 341  HOH   HOH B . 
U 6 HOH   50  450 35   HOH   HOH B . 
U 6 HOH   51  451 322  HOH   HOH B . 
U 6 HOH   52  452 44   HOH   HOH B . 
U 6 HOH   53  453 135  HOH   HOH B . 
U 6 HOH   54  454 152  HOH   HOH B . 
U 6 HOH   55  455 254  HOH   HOH B . 
U 6 HOH   56  456 14   HOH   HOH B . 
U 6 HOH   57  457 95   HOH   HOH B . 
U 6 HOH   58  458 513  HOH   HOH B . 
U 6 HOH   59  459 407  HOH   HOH B . 
U 6 HOH   60  460 389  HOH   HOH B . 
U 6 HOH   61  461 538  HOH   HOH B . 
U 6 HOH   62  462 283  HOH   HOH B . 
U 6 HOH   63  463 9    HOH   HOH B . 
U 6 HOH   64  464 10   HOH   HOH B . 
U 6 HOH   65  465 520  HOH   HOH B . 
U 6 HOH   66  466 207  HOH   HOH B . 
U 6 HOH   67  467 408  HOH   HOH B . 
U 6 HOH   68  468 303  HOH   HOH B . 
U 6 HOH   69  469 327  HOH   HOH B . 
U 6 HOH   70  470 146  HOH   HOH B . 
U 6 HOH   71  471 99   HOH   HOH B . 
U 6 HOH   72  472 29   HOH   HOH B . 
U 6 HOH   73  473 385  HOH   HOH B . 
U 6 HOH   74  474 79   HOH   HOH B . 
U 6 HOH   75  475 47   HOH   HOH B . 
U 6 HOH   76  476 216  HOH   HOH B . 
U 6 HOH   77  477 368  HOH   HOH B . 
U 6 HOH   78  478 30   HOH   HOH B . 
U 6 HOH   79  479 403  HOH   HOH B . 
U 6 HOH   80  480 136  HOH   HOH B . 
U 6 HOH   81  481 32   HOH   HOH B . 
U 6 HOH   82  482 312  HOH   HOH B . 
U 6 HOH   83  483 299  HOH   HOH B . 
U 6 HOH   84  484 464  HOH   HOH B . 
U 6 HOH   85  485 259  HOH   HOH B . 
U 6 HOH   86  486 206  HOH   HOH B . 
U 6 HOH   87  487 86   HOH   HOH B . 
U 6 HOH   88  488 120  HOH   HOH B . 
U 6 HOH   89  489 258  HOH   HOH B . 
U 6 HOH   90  490 188  HOH   HOH B . 
U 6 HOH   91  491 510  HOH   HOH B . 
U 6 HOH   92  492 234  HOH   HOH B . 
U 6 HOH   93  493 224  HOH   HOH B . 
U 6 HOH   94  494 26   HOH   HOH B . 
U 6 HOH   95  495 260  HOH   HOH B . 
U 6 HOH   96  496 218  HOH   HOH B . 
U 6 HOH   97  497 20   HOH   HOH B . 
U 6 HOH   98  498 315  HOH   HOH B . 
U 6 HOH   99  499 457  HOH   HOH B . 
U 6 HOH   100 500 462  HOH   HOH B . 
U 6 HOH   101 501 89   HOH   HOH B . 
U 6 HOH   102 502 87   HOH   HOH B . 
U 6 HOH   103 503 72   HOH   HOH B . 
U 6 HOH   104 504 194  HOH   HOH B . 
U 6 HOH   105 505 349  HOH   HOH B . 
U 6 HOH   106 506 75   HOH   HOH B . 
U 6 HOH   107 507 149  HOH   HOH B . 
U 6 HOH   108 508 314  HOH   HOH B . 
U 6 HOH   109 509 351  HOH   HOH B . 
U 6 HOH   110 510 90   HOH   HOH B . 
U 6 HOH   111 511 12   HOH   HOH B . 
U 6 HOH   112 512 378  HOH   HOH B . 
U 6 HOH   113 513 212  HOH   HOH B . 
U 6 HOH   114 514 244  HOH   HOH B . 
U 6 HOH   115 515 394  HOH   HOH B . 
U 6 HOH   116 516 539  HOH   HOH B . 
U 6 HOH   117 517 68   HOH   HOH B . 
U 6 HOH   118 518 132  HOH   HOH B . 
U 6 HOH   119 519 379  HOH   HOH B . 
U 6 HOH   120 520 246  HOH   HOH B . 
U 6 HOH   121 521 523  HOH   HOH B . 
U 6 HOH   122 522 432  HOH   HOH B . 
U 6 HOH   123 523 103  HOH   HOH B . 
U 6 HOH   124 524 248  HOH   HOH B . 
U 6 HOH   125 525 107  HOH   HOH B . 
U 6 HOH   126 526 402  HOH   HOH B . 
U 6 HOH   127 527 401  HOH   HOH B . 
U 6 HOH   128 528 19   HOH   HOH B . 
U 6 HOH   129 529 34   HOH   HOH B . 
U 6 HOH   130 530 335  HOH   HOH B . 
U 6 HOH   131 531 116  HOH   HOH B . 
U 6 HOH   132 532 411  HOH   HOH B . 
U 6 HOH   133 533 338  HOH   HOH B . 
U 6 HOH   134 534 370  HOH   HOH B . 
U 6 HOH   135 535 393  HOH   HOH B . 
U 6 HOH   136 536 161  HOH   HOH B . 
U 6 HOH   137 537 476  HOH   HOH B . 
U 6 HOH   138 538 178  HOH   HOH B . 
U 6 HOH   139 539 508  HOH   HOH B . 
U 6 HOH   140 540 319  HOH   HOH B . 
U 6 HOH   141 541 420  HOH   HOH B . 
U 6 HOH   142 542 77   HOH   HOH B . 
U 6 HOH   143 543 483  HOH   HOH B . 
U 6 HOH   144 544 512  HOH   HOH B . 
U 6 HOH   145 545 465  HOH   HOH B . 
U 6 HOH   146 546 522  HOH   HOH B . 
U 6 HOH   147 547 526  HOH   HOH B . 
U 6 HOH   148 548 313  HOH   HOH B . 
U 6 HOH   149 549 484  HOH   HOH B . 
U 6 HOH   150 550 410  HOH   HOH B . 
U 6 HOH   151 551 490  HOH   HOH B . 
U 6 HOH   152 552 128  HOH   HOH B . 
U 6 HOH   153 553 200  HOH   HOH B . 
U 6 HOH   154 554 148  HOH   HOH B . 
U 6 HOH   155 555 426  HOH   HOH B . 
U 6 HOH   156 556 61   HOH   HOH B . 
U 6 HOH   157 557 357  HOH   HOH B . 
U 6 HOH   158 558 537  HOH   HOH B . 
U 6 HOH   159 559 286  HOH   HOH B . 
U 6 HOH   160 560 359  HOH   HOH B . 
U 6 HOH   161 561 348  HOH   HOH B . 
V 6 HOH   1   401 505  HOH   HOH C . 
V 6 HOH   2   402 346  HOH   HOH C . 
V 6 HOH   3   403 329  HOH   HOH C . 
V 6 HOH   4   404 501  HOH   HOH C . 
V 6 HOH   5   405 290  HOH   HOH C . 
V 6 HOH   6   406 180  HOH   HOH C . 
V 6 HOH   7   407 242  HOH   HOH C . 
V 6 HOH   8   408 111  HOH   HOH C . 
V 6 HOH   9   409 131  HOH   HOH C . 
V 6 HOH   10  410 63   HOH   HOH C . 
V 6 HOH   11  411 265  HOH   HOH C . 
V 6 HOH   12  412 250  HOH   HOH C . 
V 6 HOH   13  413 333  HOH   HOH C . 
V 6 HOH   14  414 309  HOH   HOH C . 
V 6 HOH   15  415 46   HOH   HOH C . 
V 6 HOH   16  416 532  HOH   HOH C . 
V 6 HOH   17  417 140  HOH   HOH C . 
V 6 HOH   18  418 289  HOH   HOH C . 
V 6 HOH   19  419 52   HOH   HOH C . 
V 6 HOH   20  420 478  HOH   HOH C . 
V 6 HOH   21  421 277  HOH   HOH C . 
V 6 HOH   22  422 446  HOH   HOH C . 
V 6 HOH   23  423 448  HOH   HOH C . 
V 6 HOH   24  424 84   HOH   HOH C . 
V 6 HOH   25  425 110  HOH   HOH C . 
V 6 HOH   26  426 530  HOH   HOH C . 
V 6 HOH   27  427 173  HOH   HOH C . 
V 6 HOH   28  428 449  HOH   HOH C . 
V 6 HOH   29  429 362  HOH   HOH C . 
V 6 HOH   30  430 153  HOH   HOH C . 
V 6 HOH   31  431 130  HOH   HOH C . 
V 6 HOH   32  432 220  HOH   HOH C . 
V 6 HOH   33  433 369  HOH   HOH C . 
V 6 HOH   34  434 98   HOH   HOH C . 
V 6 HOH   35  435 143  HOH   HOH C . 
V 6 HOH   36  436 238  HOH   HOH C . 
V 6 HOH   37  437 162  HOH   HOH C . 
V 6 HOH   38  438 308  HOH   HOH C . 
V 6 HOH   39  439 469  HOH   HOH C . 
V 6 HOH   40  440 221  HOH   HOH C . 
V 6 HOH   41  441 164  HOH   HOH C . 
V 6 HOH   42  442 156  HOH   HOH C . 
V 6 HOH   43  443 165  HOH   HOH C . 
V 6 HOH   44  444 73   HOH   HOH C . 
V 6 HOH   45  445 467  HOH   HOH C . 
V 6 HOH   46  446 155  HOH   HOH C . 
V 6 HOH   47  447 222  HOH   HOH C . 
V 6 HOH   48  448 108  HOH   HOH C . 
V 6 HOH   49  449 157  HOH   HOH C . 
V 6 HOH   50  450 15   HOH   HOH C . 
V 6 HOH   51  451 145  HOH   HOH C . 
V 6 HOH   52  452 226  HOH   HOH C . 
V 6 HOH   53  453 240  HOH   HOH C . 
V 6 HOH   54  454 358  HOH   HOH C . 
V 6 HOH   55  455 11   HOH   HOH C . 
V 6 HOH   56  456 399  HOH   HOH C . 
V 6 HOH   57  457 129  HOH   HOH C . 
V 6 HOH   58  458 17   HOH   HOH C . 
V 6 HOH   59  459 272  HOH   HOH C . 
V 6 HOH   60  460 65   HOH   HOH C . 
V 6 HOH   61  461 88   HOH   HOH C . 
V 6 HOH   62  462 21   HOH   HOH C . 
V 6 HOH   63  463 184  HOH   HOH C . 
V 6 HOH   64  464 3    HOH   HOH C . 
V 6 HOH   65  465 27   HOH   HOH C . 
V 6 HOH   66  466 273  HOH   HOH C . 
V 6 HOH   67  467 7    HOH   HOH C . 
V 6 HOH   68  468 275  HOH   HOH C . 
V 6 HOH   69  469 118  HOH   HOH C . 
V 6 HOH   70  470 387  HOH   HOH C . 
V 6 HOH   71  471 390  HOH   HOH C . 
V 6 HOH   72  472 137  HOH   HOH C . 
V 6 HOH   73  473 292  HOH   HOH C . 
V 6 HOH   74  474 223  HOH   HOH C . 
V 6 HOH   75  475 371  HOH   HOH C . 
V 6 HOH   76  476 264  HOH   HOH C . 
V 6 HOH   77  477 354  HOH   HOH C . 
V 6 HOH   78  478 266  HOH   HOH C . 
V 6 HOH   79  479 477  HOH   HOH C . 
V 6 HOH   80  480 78   HOH   HOH C . 
V 6 HOH   81  481 119  HOH   HOH C . 
V 6 HOH   82  482 416  HOH   HOH C . 
V 6 HOH   83  483 235  HOH   HOH C . 
V 6 HOH   84  484 343  HOH   HOH C . 
V 6 HOH   85  485 82   HOH   HOH C . 
V 6 HOH   86  486 245  HOH   HOH C . 
V 6 HOH   87  487 418  HOH   HOH C . 
V 6 HOH   88  488 274  HOH   HOH C . 
V 6 HOH   89  489 122  HOH   HOH C . 
V 6 HOH   90  490 96   HOH   HOH C . 
V 6 HOH   91  491 239  HOH   HOH C . 
V 6 HOH   92  492 255  HOH   HOH C . 
V 6 HOH   93  493 36   HOH   HOH C . 
V 6 HOH   94  494 43   HOH   HOH C . 
V 6 HOH   95  495 305  HOH   HOH C . 
V 6 HOH   96  496 241  HOH   HOH C . 
V 6 HOH   97  497 112  HOH   HOH C . 
V 6 HOH   98  498 485  HOH   HOH C . 
V 6 HOH   99  499 284  HOH   HOH C . 
V 6 HOH   100 500 475  HOH   HOH C . 
V 6 HOH   101 501 18   HOH   HOH C . 
V 6 HOH   102 502 71   HOH   HOH C . 
V 6 HOH   103 503 215  HOH   HOH C . 
V 6 HOH   104 504 291  HOH   HOH C . 
V 6 HOH   105 505 203  HOH   HOH C . 
V 6 HOH   106 506 447  HOH   HOH C . 
V 6 HOH   107 507 85   HOH   HOH C . 
V 6 HOH   108 508 147  HOH   HOH C . 
V 6 HOH   109 509 229  HOH   HOH C . 
V 6 HOH   110 510 105  HOH   HOH C . 
V 6 HOH   111 511 39   HOH   HOH C . 
V 6 HOH   112 512 228  HOH   HOH C . 
V 6 HOH   113 513 159  HOH   HOH C . 
V 6 HOH   114 514 263  HOH   HOH C . 
V 6 HOH   115 515 109  HOH   HOH C . 
V 6 HOH   116 516 492  HOH   HOH C . 
V 6 HOH   117 517 93   HOH   HOH C . 
V 6 HOH   118 518 230  HOH   HOH C . 
V 6 HOH   119 519 337  HOH   HOH C . 
V 6 HOH   120 520 74   HOH   HOH C . 
V 6 HOH   121 521 480  HOH   HOH C . 
V 6 HOH   122 522 209  HOH   HOH C . 
V 6 HOH   123 523 13   HOH   HOH C . 
V 6 HOH   124 524 163  HOH   HOH C . 
V 6 HOH   125 525 297  HOH   HOH C . 
V 6 HOH   126 526 466  HOH   HOH C . 
V 6 HOH   127 527 434  HOH   HOH C . 
V 6 HOH   128 528 443  HOH   HOH C . 
V 6 HOH   129 529 527  HOH   HOH C . 
V 6 HOH   130 530 435  HOH   HOH C . 
V 6 HOH   131 531 481  HOH   HOH C . 
V 6 HOH   132 532 491  HOH   HOH C . 
V 6 HOH   133 533 144  HOH   HOH C . 
V 6 HOH   134 534 414  HOH   HOH C . 
V 6 HOH   135 535 519  HOH   HOH C . 
V 6 HOH   136 536 482  HOH   HOH C . 
V 6 HOH   137 537 493  HOH   HOH C . 
V 6 HOH   138 538 100  HOH   HOH C . 
V 6 HOH   139 539 134  HOH   HOH C . 
V 6 HOH   140 540 324  HOH   HOH C . 
V 6 HOH   141 541 441  HOH   HOH C . 
V 6 HOH   142 542 404  HOH   HOH C . 
V 6 HOH   143 543 442  HOH   HOH C . 
V 6 HOH   144 544 439  HOH   HOH C . 
V 6 HOH   145 545 423  HOH   HOH C . 
V 6 HOH   146 546 201  HOH   HOH C . 
V 6 HOH   147 547 353  HOH   HOH C . 
V 6 HOH   148 548 233  HOH   HOH C . 
V 6 HOH   149 549 267  HOH   HOH C . 
V 6 HOH   150 550 534  HOH   HOH C . 
V 6 HOH   151 551 425  HOH   HOH C . 
V 6 HOH   152 552 317  HOH   HOH C . 
V 6 HOH   153 553 521  HOH   HOH C . 
V 6 HOH   154 554 499  HOH   HOH C . 
V 6 HOH   155 555 437  HOH   HOH C . 
V 6 HOH   156 556 436  HOH   HOH C . 
V 6 HOH   157 557 440  HOH   HOH C . 
V 6 HOH   158 558 438  HOH   HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ILE 84  ? CD1 ? A ILE 80  CD1 
2  1 Y 1 A ARG 164 ? CG  ? A ARG 160 CG  
3  1 Y 1 A ARG 164 ? CD  ? A ARG 160 CD  
4  1 Y 1 A ARG 164 ? NE  ? A ARG 160 NE  
5  1 Y 1 A ARG 164 ? CZ  ? A ARG 160 CZ  
6  1 Y 1 A ARG 164 ? NH1 ? A ARG 160 NH1 
7  1 Y 1 A ARG 164 ? NH2 ? A ARG 160 NH2 
8  1 Y 1 A SER 166 ? OG  ? A SER 162 OG  
9  1 Y 1 A SER 167 ? OG  ? A SER 163 OG  
10 1 Y 1 A SER 190 ? OG  ? A SER 186 OG  
11 1 Y 1 A SER 194 ? OG  ? A SER 190 OG  
12 1 Y 1 A ARG 211 ? NE  ? A ARG 207 NE  
13 1 Y 1 A ARG 211 ? CZ  ? A ARG 207 CZ  
14 1 Y 1 A ARG 211 ? NH1 ? A ARG 207 NH1 
15 1 Y 1 A ARG 211 ? NH2 ? A ARG 207 NH2 
16 1 Y 1 A ARG 230 ? NE  ? A ARG 226 NE  
17 1 Y 1 A ARG 230 ? CZ  ? A ARG 226 CZ  
18 1 Y 1 A ARG 230 ? NH1 ? A ARG 226 NH1 
19 1 Y 1 A ARG 230 ? NH2 ? A ARG 226 NH2 
20 1 Y 1 B ILE 84  ? CD1 ? B ILE 80  CD1 
21 1 Y 1 B LYS 160 ? CD  ? B LYS 156 CD  
22 1 Y 1 B LYS 160 ? CE  ? B LYS 156 CE  
23 1 Y 1 B LYS 160 ? NZ  ? B LYS 156 NZ  
24 1 Y 1 B GLU 163 ? CG  ? B GLU 159 CG  
25 1 Y 1 B GLU 163 ? CD  ? B GLU 159 CD  
26 1 Y 1 B GLU 163 ? OE1 ? B GLU 159 OE1 
27 1 Y 1 B GLU 163 ? OE2 ? B GLU 159 OE2 
28 1 Y 1 B ARG 164 ? CG  ? B ARG 160 CG  
29 1 Y 1 B ARG 164 ? CD  ? B ARG 160 CD  
30 1 Y 1 B ARG 164 ? NE  ? B ARG 160 NE  
31 1 Y 1 B ARG 164 ? CZ  ? B ARG 160 CZ  
32 1 Y 1 B ARG 164 ? NH1 ? B ARG 160 NH1 
33 1 Y 1 B ARG 164 ? NH2 ? B ARG 160 NH2 
34 1 Y 1 B GLN 189 ? CG  ? B GLN 185 CG  
35 1 Y 1 B GLN 189 ? CD  ? B GLN 185 CD  
36 1 Y 1 B GLN 189 ? OE1 ? B GLN 185 OE1 
37 1 Y 1 B GLN 189 ? NE2 ? B GLN 185 NE2 
38 1 Y 1 B SER 194 ? OG  ? B SER 190 OG  
39 1 Y 1 B ARG 211 ? NE  ? B ARG 207 NE  
40 1 Y 1 B ARG 211 ? CZ  ? B ARG 207 CZ  
41 1 Y 1 B ARG 211 ? NH1 ? B ARG 207 NH1 
42 1 Y 1 B ARG 211 ? NH2 ? B ARG 207 NH2 
43 1 Y 1 B ARG 230 ? NE  ? B ARG 226 NE  
44 1 Y 1 B ARG 230 ? CZ  ? B ARG 226 CZ  
45 1 Y 1 B ARG 230 ? NH1 ? B ARG 226 NH1 
46 1 Y 1 B ARG 230 ? NH2 ? B ARG 226 NH2 
47 1 Y 1 C THR 56  ? OG1 ? C THR 52  OG1 
48 1 Y 1 C THR 56  ? CG2 ? C THR 52  CG2 
49 1 Y 1 C THR 144 ? OG1 ? C THR 140 OG1 
50 1 Y 1 C THR 144 ? CG2 ? C THR 140 CG2 
51 1 Y 1 C GLU 163 ? CG  ? C GLU 159 CG  
52 1 Y 1 C GLU 163 ? CD  ? C GLU 159 CD  
53 1 Y 1 C GLU 163 ? OE1 ? C GLU 159 OE1 
54 1 Y 1 C GLU 163 ? OE2 ? C GLU 159 OE2 
55 1 Y 1 C LYS 175 ? CE  ? C LYS 171 CE  
56 1 Y 1 C LYS 175 ? NZ  ? C LYS 171 NZ  
57 1 Y 1 C GLN 189 ? CG  ? C GLN 185 CG  
58 1 Y 1 C GLN 189 ? CD  ? C GLN 185 CD  
59 1 Y 1 C GLN 189 ? OE1 ? C GLN 185 OE1 
60 1 Y 1 C GLN 189 ? NE2 ? C GLN 185 NE2 
61 1 Y 1 C SER 190 ? OG  ? C SER 186 OG  
62 1 Y 1 C ARG 211 ? NE  ? C ARG 207 NE  
63 1 Y 1 C ARG 211 ? CZ  ? C ARG 207 CZ  
64 1 Y 1 C ARG 211 ? NH1 ? C ARG 207 NH1 
65 1 Y 1 C ARG 211 ? NH2 ? C ARG 207 NH2 
66 1 Y 1 C ARG 230 ? NE  ? C ARG 226 NE  
67 1 Y 1 C ARG 230 ? CZ  ? C ARG 226 CZ  
68 1 Y 1 C ARG 230 ? NH1 ? C ARG 226 NH1 
69 1 Y 1 C ARG 230 ? NH2 ? C ARG 226 NH2 
70 1 Y 1 C VAL 235 ? CG1 ? C VAL 231 CG1 
71 1 Y 1 C VAL 235 ? CG2 ? C VAL 231 CG2 
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0425 ? 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .        ? 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .        ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        ? 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9O0Y 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.422 
_cell.length_a_esd                 ? 
_cell.length_b                     153.254 
_cell.length_b_esd                 ? 
_cell.length_c                     140.513 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_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                         9O0Y 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9O0Y 
_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             2.76 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.43 
_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              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20% PEG 600, 0.15M KSCN, 0.1M Tris 7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 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         2023-02-11 
_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   0.97918 
_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        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-E 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9O0Y 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.50 
_reflns.d_resolution_low                               50.00 
_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                                     133196 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.978 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.089 
_reflns.pdbx_Rpim_I_all                                0.026 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1481276 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   1.000 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.085 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_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 
_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 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_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 
1.50 1.53  ? ? ? ? ? ? 6589 ? ? ? ? ? ? ? ? ? ? ? 9.3  0.721 ? ? 1.026 0.328 ? 1  1 0.755 0.928 ? 99.9  ? 0.971 ? ? ? ? ? ? ? ? ? 
1.53 1.55  ? ? ? ? ? ? 6606 ? ? ? ? ? ? ? ? ? ? ? 10.6 0.725 ? ? 0.866 0.264 ? 2  1 0.854 0.960 ? 100.0 ? 0.824 ? ? ? ? ? ? ? ? ? 
1.55 1.58  ? ? ? ? ? ? 6602 ? ? ? ? ? ? ? ? ? ? ? 11.4 0.730 ? ? 0.741 0.219 ? 3  1 0.906 0.975 ? 100.0 ? 0.707 ? ? ? ? ? ? ? ? ? 
1.58 1.62  ? ? ? ? ? ? 6610 ? ? ? ? ? ? ? ? ? ? ? 11.4 0.742 ? ? 0.677 0.200 ? 4  1 0.910 0.976 ? 100.0 ? 0.646 ? ? ? ? ? ? ? ? ? 
1.62 1.65  ? ? ? ? ? ? 6630 ? ? ? ? ? ? ? ? ? ? ? 11.3 0.752 ? ? 0.581 0.173 ? 5  1 0.928 0.981 ? 100.0 ? 0.554 ? ? ? ? ? ? ? ? ? 
1.65 1.69  ? ? ? ? ? ? 6585 ? ? ? ? ? ? ? ? ? ? ? 11.2 0.768 ? ? 0.495 0.148 ? 6  1 0.948 0.987 ? 100.0 ? 0.472 ? ? ? ? ? ? ? ? ? 
1.69 1.73  ? ? ? ? ? ? 6597 ? ? ? ? ? ? ? ? ? ? ? 11.0 0.791 ? ? 0.403 0.121 ? 7  1 0.961 0.990 ? 100.0 ? 0.384 ? ? ? ? ? ? ? ? ? 
1.73 1.78  ? ? ? ? ? ? 6623 ? ? ? ? ? ? ? ? ? ? ? 10.3 0.812 ? ? 0.321 0.099 ? 8  1 0.972 0.993 ? 100.0 ? 0.304 ? ? ? ? ? ? ? ? ? 
1.78 1.83  ? ? ? ? ? ? 6635 ? ? ? ? ? ? ? ? ? ? ? 10.5 0.851 ? ? 0.254 0.078 ? 9  1 0.980 0.995 ? 99.9  ? 0.241 ? ? ? ? ? ? ? ? ? 
1.83 1.89  ? ? ? ? ? ? 6612 ? ? ? ? ? ? ? ? ? ? ? 11.8 0.871 ? ? 0.209 0.061 ? 10 1 0.989 0.997 ? 100.0 ? 0.200 ? ? ? ? ? ? ? ? ? 
1.89 1.96  ? ? ? ? ? ? 6629 ? ? ? ? ? ? ? ? ? ? ? 11.8 0.918 ? ? 0.171 0.050 ? 11 1 0.993 0.998 ? 100.0 ? 0.163 ? ? ? ? ? ? ? ? ? 
1.96 2.04  ? ? ? ? ? ? 6649 ? ? ? ? ? ? ? ? ? ? ? 11.7 0.936 ? ? 0.144 0.042 ? 12 1 0.995 0.999 ? 100.0 ? 0.138 ? ? ? ? ? ? ? ? ? 
2.04 2.13  ? ? ? ? ? ? 6645 ? ? ? ? ? ? ? ? ? ? ? 11.5 0.993 ? ? 0.118 0.035 ? 13 1 0.995 0.999 ? 100.0 ? 0.112 ? ? ? ? ? ? ? ? ? 
2.13 2.24  ? ? ? ? ? ? 6640 ? ? ? ? ? ? ? ? ? ? ? 11.4 1.038 ? ? 0.095 0.028 ? 14 1 0.997 0.999 ? 100.0 ? 0.091 ? ? ? ? ? ? ? ? ? 
2.24 2.38  ? ? ? ? ? ? 6676 ? ? ? ? ? ? ? ? ? ? ? 11.1 1.093 ? ? 0.085 0.026 ? 15 1 0.997 0.999 ? 99.9  ? 0.081 ? ? ? ? ? ? ? ? ? 
2.38 2.56  ? ? ? ? ? ? 6667 ? ? ? ? ? ? ? ? ? ? ? 9.9  1.147 ? ? 0.077 0.024 ? 16 1 0.997 0.999 ? 99.9  ? 0.073 ? ? ? ? ? ? ? ? ? 
2.56 2.82  ? ? ? ? ? ? 6694 ? ? ? ? ? ? ? ? ? ? ? 12.0 1.227 ? ? 0.070 0.020 ? 17 1 0.998 0.999 ? 100.0 ? 0.067 ? ? ? ? ? ? ? ? ? 
2.82 3.23  ? ? ? ? ? ? 6747 ? ? ? ? ? ? ? ? ? ? ? 12.0 1.356 ? ? 0.062 0.018 ? 18 1 0.998 1.000 ? 100.0 ? 0.059 ? ? ? ? ? ? ? ? ? 
3.23 4.07  ? ? ? ? ? ? 6765 ? ? ? ? ? ? ? ? ? ? ? 11.5 1.453 ? ? 0.055 0.016 ? 19 1 0.998 1.000 ? 99.9  ? 0.053 ? ? ? ? ? ? ? ? ? 
4.07 50.00 ? ? ? ? ? ? 6995 ? ? ? ? ? ? ? ? ? ? ? 10.8 1.501 ? ? 0.054 0.016 ? 20 1 0.998 0.999 ? 99.9  ? 0.051 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.73 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.47 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.27 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               19.601 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.973 
_refine.correlation_coeff_Fo_to_Fc_free          0.966 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9O0Y 
_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                            1.50 
_refine.ls_d_res_low                             49.32 
_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                     130475 
_refine.ls_number_reflns_R_free                  2663 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.78 
_refine.ls_percent_reflns_R_free                 2.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.14340 
_refine.ls_R_factor_R_free                       0.16790 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.14291 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.058 
_refine.pdbx_overall_ESU_R_Free                  0.053 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_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                             1.967 
_refine.overall_SU_ML                            0.033 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        49.32 
_refine_hist.number_atoms_solvent             499 
_refine_hist.number_atoms_total               5448 
_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        4843 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         106 
_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_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005  0.012  5298  ? r_bond_refined_d             ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  4961  ? r_bond_other_d               ? ? ? 
'X-RAY DIFFRACTION' ? 1.256  1.814  7276  ? r_angle_refined_deg          ? ? ? 
'X-RAY DIFFRACTION' ? 0.464  1.726  11453 ? r_angle_other_deg            ? ? ? 
'X-RAY DIFFRACTION' ? 5.821  5.000  688   ? r_dihedral_angle_1_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 6.225  5.000  32    ? r_dihedral_angle_2_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 12.459 10.000 762   ? r_dihedral_angle_3_deg       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 0.067  0.200  826   ? r_chiral_restr               ? ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  6456  ? r_gen_planes_refined         ? ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  1144  ? r_gen_planes_other           ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? ? 
'X-RAY DIFFRACTION' ? 3.689  2.054  2704  ? r_mcbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 3.685  2.054  2704  ? r_mcbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? 6.015  3.667  3408  ? r_mcangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 6.015  3.668  3409  ? r_mcangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 3.837  2.199  2594  ? r_scbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 3.836  2.199  2595  ? r_scbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 6.091  3.990  3869  ? r_scangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 12.481 23.34  5930  ? r_long_range_B_refined       ? ? ? 
'X-RAY DIFFRACTION' ? 11.194 21.21  5765  ? r_long_range_B_other         ? ? ? 
'X-RAY DIFFRACTION' ? 2.062  3.000  10259 ? r_rigid_bond_restr           ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? ? 
# 
_refine_ls_shell.pdbx_refine_id                      'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                          1.50 
_refine_ls_shell.d_res_low                           1.538 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                191 
_refine_ls_shell.number_reflns_R_work                9335 
_refine_ls_shell.percent_reflns_obs                  97.74 
_refine_ls_shell.percent_reflns_R_free               ? 
_refine_ls_shell.R_factor_all                        ? 
_refine_ls_shell.R_factor_obs                        ? 
_refine_ls_shell.R_factor_R_free_error               ? 
_refine_ls_shell.R_factor_R_work                     0.241 
_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.correlation_coeff_Fo_to_Fc          ? 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free     ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work   ? 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free   ? 
_refine_ls_shell.pdbx_total_number_of_bins_used      ? 
_refine_ls_shell.pdbx_phase_error                    ? 
_refine_ls_shell.pdbx_fsc_work                       ? 
_refine_ls_shell.pdbx_fsc_free                       ? 
_refine_ls_shell.R_factor_R_free                     0.271 
# 
_struct.entry_id                     9O0Y 
_struct.title                        'Co-crystal structure of human TREX1 in complex with an inhibitor' 
_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        9O0Y 
_struct_keywords.text            
'TREX1, SGC, TRANSPORT PROTEIN, Structural Genomics, PSI-Biology, Structural Genomics Consortium, HYDROLASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   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 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
I N N 2 ? 
J N N 3 ? 
K N N 4 ? 
L N N 5 ? 
M N N 5 ? 
N N N 2 ? 
O N N 3 ? 
P N N 4 ? 
Q N N 4 ? 
R N N 5 ? 
S N N 5 ? 
T N N 6 ? 
U N N 6 ? 
V N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    TREX1_HUMAN 
_struct_ref.pdbx_db_accession          Q9NSU2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ALPPGPMQTLIFFDMEATGLPFSQPKVTELCLLAVHRCALESPPTSQGPPPTVPPPPRVVDKLSLCVAPGKACSPAASEI
TGLSTAVLAAHGRQCFDDNLANLLLAFLRRQPQPWCLVAHNGDRYDFPLLQAELAMLGLTSALDGAFCVDSITALKALER
ASSPSEHGPRKSYSLGSIYTRLYGQSPPDSHTAEGDVLALLSICQWRPQALLRWVDAHARPFGTIRPMYGVTAS
;
_struct_ref.pdbx_align_begin           5 
# 
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 9O0Y A 1 ? 234 ? Q9NSU2 5 ? 238 ? 5 238 
2 1 9O0Y B 1 ? 234 ? Q9NSU2 5 ? 238 ? 5 238 
3 1 9O0Y C 1 ? 234 ? Q9NSU2 5 ? 238 ? 5 238 
# 
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 9O0Y HIS A 4  ? UNP Q9NSU2 PRO 8  conflict 8  1  
1 9O0Y HIS A 6  ? UNP Q9NSU2 PRO 10 conflict 10 2  
1 9O0Y SER A 22 ? UNP Q9NSU2 PHE 26 conflict 26 3  
1 9O0Y ARG A 24 ? UNP Q9NSU2 GLN 28 conflict 28 4  
1 9O0Y GLU A 26 ? UNP Q9NSU2 LYS 30 conflict 30 5  
2 9O0Y HIS B 4  ? UNP Q9NSU2 PRO 8  conflict 8  6  
2 9O0Y HIS B 6  ? UNP Q9NSU2 PRO 10 conflict 10 7  
2 9O0Y SER B 22 ? UNP Q9NSU2 PHE 26 conflict 26 8  
2 9O0Y ARG B 24 ? UNP Q9NSU2 GLN 28 conflict 28 9  
2 9O0Y GLU B 26 ? UNP Q9NSU2 LYS 30 conflict 30 10 
3 9O0Y HIS C 4  ? UNP Q9NSU2 PRO 8  conflict 8  11 
3 9O0Y HIS C 6  ? UNP Q9NSU2 PRO 10 conflict 10 12 
3 9O0Y SER C 22 ? UNP Q9NSU2 PHE 26 conflict 26 13 
3 9O0Y ARG C 24 ? UNP Q9NSU2 GLN 28 conflict 28 14 
3 9O0Y GLU C 26 ? UNP Q9NSU2 LYS 30 conflict 30 15 
# 
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_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4150  ? 
1 MORE         -11   ? 
1 'SSA (A^2)'  17050 ? 
2 'ABSA (A^2)' 3840  ? 
2 MORE         -15   ? 
2 'SSA (A^2)'  16760 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1,2 A,D,E,F,G,H,T                 
2 1   B,C,I,J,K,L,M,N,O,P,Q,R,S,U,V 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z   1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 4_555 x,-y,-z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 LEU A 20  ? ARG A 24  ? LEU A 24  ARG A 28  5 ? 5  
HELX_P HELX_P2  AA2 ARG A 37  ? SER A 42  ? ARG A 41  SER A 46  1 ? 6  
HELX_P HELX_P3  AA3 SER A 74  ? GLY A 82  ? SER A 78  GLY A 86  1 ? 9  
HELX_P HELX_P4  AA4 SER A 84  ? HIS A 91  ? SER A 88  HIS A 95  1 ? 8  
HELX_P HELX_P5  AA5 ASP A 97  ? ARG A 109 ? ASP A 101 ARG A 113 1 ? 13 
HELX_P HELX_P6  AA6 TYR A 125 ? LEU A 137 ? TYR A 129 LEU A 141 1 ? 13 
HELX_P HELX_P7  AA7 SER A 151 ? SER A 163 ? SER A 155 SER A 167 1 ? 13 
HELX_P HELX_P8  AA8 SER A 174 ? GLY A 184 ? SER A 178 GLY A 188 1 ? 11 
HELX_P HELX_P9  AA9 THR A 192 ? GLN A 205 ? THR A 196 GLN A 209 1 ? 14 
HELX_P HELX_P10 AB1 ARG A 207 ? ALA A 219 ? ARG A 211 ALA A 223 1 ? 13 
HELX_P HELX_P11 AB2 GLY A 223 ? ILE A 225 ? GLY A 227 ILE A 229 5 ? 3  
HELX_P HELX_P12 AB3 LEU B 20  ? ARG B 24  ? LEU B 24  ARG B 28  5 ? 5  
HELX_P HELX_P13 AB4 ARG B 37  ? SER B 42  ? ARG B 41  SER B 46  1 ? 6  
HELX_P HELX_P14 AB5 SER B 74  ? GLY B 82  ? SER B 78  GLY B 86  1 ? 9  
HELX_P HELX_P15 AB6 SER B 84  ? HIS B 91  ? SER B 88  HIS B 95  1 ? 8  
HELX_P HELX_P16 AB7 ASP B 97  ? ARG B 110 ? ASP B 101 ARG B 114 1 ? 14 
HELX_P HELX_P17 AB8 TYR B 125 ? LEU B 137 ? TYR B 129 LEU B 141 1 ? 13 
HELX_P HELX_P18 AB9 SER B 151 ? ALA B 161 ? SER B 155 ALA B 165 1 ? 11 
HELX_P HELX_P19 AC1 SER B 174 ? GLY B 184 ? SER B 178 GLY B 188 1 ? 11 
HELX_P HELX_P20 AC2 THR B 192 ? GLN B 205 ? THR B 196 GLN B 209 1 ? 14 
HELX_P HELX_P21 AC3 ARG B 207 ? ALA B 219 ? ARG B 211 ALA B 223 1 ? 13 
HELX_P HELX_P22 AC4 GLY B 223 ? ILE B 225 ? GLY B 227 ILE B 229 5 ? 3  
HELX_P HELX_P23 AC5 LEU C 20  ? ARG C 24  ? LEU C 24  ARG C 28  5 ? 5  
HELX_P HELX_P24 AC6 ARG C 37  ? SER C 42  ? ARG C 41  SER C 46  1 ? 6  
HELX_P HELX_P25 AC7 SER C 74  ? GLY C 82  ? SER C 78  GLY C 86  1 ? 9  
HELX_P HELX_P26 AC8 SER C 84  ? HIS C 91  ? SER C 88  HIS C 95  1 ? 8  
HELX_P HELX_P27 AC9 ASP C 97  ? ARG C 110 ? ASP C 101 ARG C 114 1 ? 14 
HELX_P HELX_P28 AD1 TYR C 125 ? LEU C 137 ? TYR C 129 LEU C 141 1 ? 13 
HELX_P HELX_P29 AD2 SER C 151 ? GLU C 159 ? SER C 155 GLU C 163 1 ? 9  
HELX_P HELX_P30 AD3 SER C 174 ? GLY C 184 ? SER C 178 GLY C 188 1 ? 11 
HELX_P HELX_P31 AD4 THR C 192 ? GLN C 205 ? THR C 196 GLN C 209 1 ? 14 
HELX_P HELX_P32 AD5 ARG C 207 ? ALA C 219 ? ARG C 211 ALA C 223 1 ? 13 
HELX_P HELX_P33 AD6 GLY C 223 ? ILE C 225 ? GLY C 227 ILE C 229 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP   14 OD1 ? ? ? 1_555 E MG  . MG ? ? A ASP   18  A MG  302 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc2  metalc ? ? D A1B7T .  N16 ? ? ? 1_555 E MG  . MG ? ? A A1B7T 301 A MG  302 1_555 ? ? ? ? ? ? ? 2.204 ? ? 
metalc3  metalc ? ? E MG    .  MG  ? ? ? 1_555 T HOH . O  ? ? A MG    302 A HOH 411 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc4  metalc ? ? E MG    .  MG  ? ? ? 1_555 T HOH . O  ? ? A MG    302 A HOH 413 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc5  metalc ? ? E MG    .  MG  ? ? ? 1_555 T HOH . O  ? ? A MG    302 A HOH 422 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc6  metalc ? ? E MG    .  MG  ? ? ? 1_555 T HOH . O  ? ? A MG    302 A HOH 494 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
metalc7  metalc ? ? B ASP   14 OD1 ? ? ? 1_555 J MG  . MG ? ? B ASP   18  B MG  302 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc8  metalc ? ? I A1B7T .  N16 ? ? ? 1_555 J MG  . MG ? ? B A1B7T 301 B MG  302 1_555 ? ? ? ? ? ? ? 2.227 ? ? 
metalc9  metalc ? ? J MG    .  MG  ? ? ? 1_555 U HOH . O  ? ? B MG    302 B HOH 417 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc10 metalc ? ? J MG    .  MG  ? ? ? 1_555 U HOH . O  ? ? B MG    302 B HOH 423 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc11 metalc ? ? J MG    .  MG  ? ? ? 1_555 U HOH . O  ? ? B MG    302 B HOH 438 1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc12 metalc ? ? J MG    .  MG  ? ? ? 1_555 U HOH . O  ? ? B MG    302 B HOH 499 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
metalc13 metalc ? ? C ASP   14 OD1 ? ? ? 1_555 O MG  . MG ? ? C ASP   18  C MG  302 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc14 metalc ? ? N A1B7T .  N16 ? ? ? 1_555 O MG  . MG ? ? C A1B7T 301 C MG  302 1_555 ? ? ? ? ? ? ? 2.213 ? ? 
metalc15 metalc ? ? O MG    .  MG  ? ? ? 1_555 V HOH . O  ? ? C MG    302 C HOH 422 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc16 metalc ? ? O MG    .  MG  ? ? ? 1_555 V HOH . O  ? ? C MG    302 C HOH 423 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
metalc17 metalc ? ? O MG    .  MG  ? ? ? 1_555 V HOH . O  ? ? C MG    302 C HOH 428 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc18 metalc ? ? O MG    .  MG  ? ? ? 1_555 V HOH . O  ? ? C MG    302 C HOH 506 1_555 ? ? ? ? ? ? ? 2.105 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP   14 ? A ASP   18  ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 N16 ? D A1B7T . ? A A1B7T 301 ? 1_555 173.7 ? 
2  OD1 ? A ASP   14 ? A ASP   18  ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   411 ? 1_555 87.7  ? 
3  N16 ? D A1B7T .  ? A A1B7T 301 ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   411 ? 1_555 91.3  ? 
4  OD1 ? A ASP   14 ? A ASP   18  ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   413 ? 1_555 85.8  ? 
5  N16 ? D A1B7T .  ? A A1B7T 301 ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   413 ? 1_555 88.0  ? 
6  O   ? T HOH   .  ? A HOH   411 ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   413 ? 1_555 90.9  ? 
7  OD1 ? A ASP   14 ? A ASP   18  ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   422 ? 1_555 88.0  ? 
8  N16 ? D A1B7T .  ? A A1B7T 301 ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   422 ? 1_555 98.2  ? 
9  O   ? T HOH   .  ? A HOH   411 ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   422 ? 1_555 85.7  ? 
10 O   ? T HOH   .  ? A HOH   413 ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   422 ? 1_555 173.0 ? 
11 OD1 ? A ASP   14 ? A ASP   18  ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   494 ? 1_555 88.2  ? 
12 N16 ? D A1B7T .  ? A A1B7T 301 ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   494 ? 1_555 93.1  ? 
13 O   ? T HOH   .  ? A HOH   411 ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   494 ? 1_555 174.6 ? 
14 O   ? T HOH   .  ? A HOH   413 ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   494 ? 1_555 92.3  ? 
15 O   ? T HOH   .  ? A HOH   422 ? 1_555 MG ? E MG . ? A MG 302 ? 1_555 O   ? T HOH   . ? A HOH   494 ? 1_555 90.7  ? 
16 OD1 ? B ASP   14 ? B ASP   18  ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 N16 ? I A1B7T . ? B A1B7T 301 ? 1_555 175.3 ? 
17 OD1 ? B ASP   14 ? B ASP   18  ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   417 ? 1_555 86.9  ? 
18 N16 ? I A1B7T .  ? B A1B7T 301 ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   417 ? 1_555 97.2  ? 
19 OD1 ? B ASP   14 ? B ASP   18  ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   423 ? 1_555 87.4  ? 
20 N16 ? I A1B7T .  ? B A1B7T 301 ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   423 ? 1_555 88.3  ? 
21 O   ? U HOH   .  ? B HOH   417 ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   423 ? 1_555 172.2 ? 
22 OD1 ? B ASP   14 ? B ASP   18  ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   438 ? 1_555 88.8  ? 
23 N16 ? I A1B7T .  ? B A1B7T 301 ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   438 ? 1_555 89.4  ? 
24 O   ? U HOH   .  ? B HOH   417 ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   438 ? 1_555 85.3  ? 
25 O   ? U HOH   .  ? B HOH   423 ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   438 ? 1_555 89.3  ? 
26 OD1 ? B ASP   14 ? B ASP   18  ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   499 ? 1_555 88.4  ? 
27 N16 ? I A1B7T .  ? B A1B7T 301 ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   499 ? 1_555 93.7  ? 
28 O   ? U HOH   .  ? B HOH   417 ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   499 ? 1_555 91.5  ? 
29 O   ? U HOH   .  ? B HOH   423 ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   499 ? 1_555 93.7  ? 
30 O   ? U HOH   .  ? B HOH   438 ? 1_555 MG ? J MG . ? B MG 302 ? 1_555 O   ? U HOH   . ? B HOH   499 ? 1_555 175.8 ? 
31 OD1 ? C ASP   14 ? C ASP   18  ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 N16 ? N A1B7T . ? C A1B7T 301 ? 1_555 175.4 ? 
32 OD1 ? C ASP   14 ? C ASP   18  ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   422 ? 1_555 86.8  ? 
33 N16 ? N A1B7T .  ? C A1B7T 301 ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   422 ? 1_555 89.1  ? 
34 OD1 ? C ASP   14 ? C ASP   18  ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   423 ? 1_555 88.2  ? 
35 N16 ? N A1B7T .  ? C A1B7T 301 ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   423 ? 1_555 95.8  ? 
36 O   ? V HOH   .  ? C HOH   422 ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   423 ? 1_555 174.7 ? 
37 OD1 ? C ASP   14 ? C ASP   18  ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   428 ? 1_555 87.5  ? 
38 N16 ? N A1B7T .  ? C A1B7T 301 ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   428 ? 1_555 90.5  ? 
39 O   ? V HOH   .  ? C HOH   422 ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   428 ? 1_555 90.8  ? 
40 O   ? V HOH   .  ? C HOH   423 ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   428 ? 1_555 87.2  ? 
41 OD1 ? C ASP   14 ? C ASP   18  ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   506 ? 1_555 88.3  ? 
42 N16 ? N A1B7T .  ? C A1B7T 301 ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   506 ? 1_555 93.8  ? 
43 O   ? V HOH   .  ? C HOH   422 ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   506 ? 1_555 91.3  ? 
44 O   ? V HOH   .  ? C HOH   423 ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   506 ? 1_555 90.5  ? 
45 O   ? V HOH   .  ? C HOH   428 ? 1_555 MG ? O MG . ? C MG 302 ? 1_555 O   ? V HOH   . ? C HOH   506 ? 1_555 175.3 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLN 113 A . ? GLN 117 A PRO 114 A ? PRO 118 A 1 -2.49 
2 GLN 113 B . ? GLN 117 B PRO 114 B ? PRO 118 B 1 -1.66 
3 GLN 113 C . ? GLN 117 C PRO 114 C ? PRO 118 C 1 -3.75 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6  ? 
AA2 ? 12 ? 
# 
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  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? parallel      
AA1 4  5  ? parallel      
AA1 5  6  ? anti-parallel 
AA2 1  2  ? anti-parallel 
AA2 2  3  ? parallel      
AA2 3  4  ? parallel      
AA2 4  5  ? anti-parallel 
AA2 5  6  ? anti-parallel 
AA2 6  7  ? anti-parallel 
AA2 7  8  ? anti-parallel 
AA2 8  9  ? anti-parallel 
AA2 9  10 ? parallel      
AA2 10 11 ? parallel      
AA2 11 12 ? 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  ASP A 61  ? CYS A 66  ? ASP A 65  CYS A 70  
AA1 2  VAL A 27  ? HIS A 36  ? VAL A 31  HIS A 40  
AA1 3  THR A 9   ? ALA A 17  ? THR A 13  ALA A 21  
AA1 4  TRP A 115 ? ALA A 119 ? TRP A 119 ALA A 123 
AA1 5  PHE A 147 ? ASP A 150 ? PHE A 151 ASP A 154 
AA1 6  ARG A 220 ? PRO A 221 ? ARG A 224 PRO A 225 
AA2 1  ARG B 220 ? PRO B 221 ? ARG B 224 PRO B 225 
AA2 2  PHE B 147 ? ASP B 150 ? PHE B 151 ASP B 154 
AA2 3  TRP B 115 ? ALA B 119 ? TRP B 119 ALA B 123 
AA2 4  THR B 9   ? ALA B 17  ? THR B 13  ALA B 21  
AA2 5  VAL B 27  ? HIS B 36  ? VAL B 31  HIS B 40  
AA2 6  ASP B 61  ? CYS B 66  ? ASP B 65  CYS B 70  
AA2 7  ASP C 61  ? CYS C 66  ? ASP C 65  CYS C 70  
AA2 8  VAL C 27  ? HIS C 36  ? VAL C 31  HIS C 40  
AA2 9  THR C 9   ? ALA C 17  ? THR C 13  ALA C 21  
AA2 10 TRP C 115 ? ALA C 119 ? TRP C 119 ALA C 123 
AA2 11 PHE C 147 ? ASP C 150 ? PHE C 151 ASP C 154 
AA2 12 ARG C 220 ? PRO C 221 ? ARG C 224 PRO C 225 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  O ASP A 61  ? O ASP A 65  N ALA A 34  ? N ALA A 38  
AA1 2  3  O VAL A 35  ? O VAL A 39  N LEU A 10  ? N LEU A 14  
AA1 3  4  N ILE A 11  ? N ILE A 15  O CYS A 116 ? O CYS A 120 
AA1 4  5  N LEU A 117 ? N LEU A 121 O PHE A 147 ? O PHE A 151 
AA1 5  6  N CYS A 148 ? N CYS A 152 O ARG A 220 ? O ARG A 224 
AA2 1  2  O ARG B 220 ? O ARG B 224 N CYS B 148 ? N CYS B 152 
AA2 2  3  O PHE B 147 ? O PHE B 151 N LEU B 117 ? N LEU B 121 
AA2 3  4  O CYS B 116 ? O CYS B 120 N ILE B 11  ? N ILE B 15  
AA2 4  5  N LEU B 10  ? N LEU B 14  O VAL B 35  ? O VAL B 39  
AA2 5  6  N ALA B 34  ? N ALA B 38  O ASP B 61  ? O ASP B 65  
AA2 6  7  N SER B 64  ? N SER B 68  O LYS C 62  ? O LYS C 66  
AA2 7  8  O ASP C 61  ? O ASP C 65  N ALA C 34  ? N ALA C 38  
AA2 8  9  O VAL C 35  ? O VAL C 39  N LEU C 10  ? N LEU C 14  
AA2 9  10 N ILE C 11  ? N ILE C 15  O CYS C 116 ? O CYS C 120 
AA2 10 11 N LEU C 117 ? N LEU C 121 O PHE C 147 ? O PHE C 151 
AA2 11 12 N CYS C 148 ? N CYS C 152 O ARG C 220 ? O ARG C 224 
# 
_pdbx_entry_details.entry_id                   9O0Y 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OE1 
_pdbx_validate_close_contact.auth_asym_id_1   C 
_pdbx_validate_close_contact.auth_comp_id_1   GLU 
_pdbx_validate_close_contact.auth_seq_id_1    83 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   C 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.14 
# 
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 TYR A 129 ? ? -109.07 -77.41 
2 1 SER A 145 ? ? 85.99   1.61   
3 1 HIS B 8   ? ? -147.77 39.05  
4 1 TYR B 129 ? ? -111.96 -77.64 
5 1 TYR C 129 ? ? -110.20 -77.34 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          PSI:Biology 
_pdbx_SG_project.full_name_of_center   'Structural Genomics Consortium' 
_pdbx_SG_project.initial_of_center     SGC 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     500 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   U 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 580 ? 9.17 . 
2 1 O ? B HOH 561 ? 5.87 . 
# 
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 THR 49  ? A THR 45  
2  1 Y 1 A SER 50  ? A SER 46  
3  1 Y 1 A GLN 51  ? A GLN 47  
4  1 Y 1 A GLY 52  ? A GLY 48  
5  1 Y 1 A PRO 53  ? A PRO 49  
6  1 Y 1 A PRO 168 ? A PRO 164 
7  1 Y 1 A SER 169 ? A SER 165 
8  1 Y 1 A GLU 170 ? A GLU 166 
9  1 Y 1 A HIS 171 ? A HIS 167 
10 1 Y 1 A GLY 172 ? A GLY 168 
11 1 Y 1 A PRO 173 ? A PRO 169 
12 1 Y 1 A ARG 174 ? A ARG 170 
13 1 Y 1 A VAL 235 ? A VAL 231 
14 1 Y 1 A THR 236 ? A THR 232 
15 1 Y 1 A ALA 237 ? A ALA 233 
16 1 Y 1 A SER 238 ? A SER 234 
17 1 Y 1 B THR 49  ? B THR 45  
18 1 Y 1 B SER 50  ? B SER 46  
19 1 Y 1 B GLN 51  ? B GLN 47  
20 1 Y 1 B GLY 52  ? B GLY 48  
21 1 Y 1 B PRO 53  ? B PRO 49  
22 1 Y 1 B PRO 54  ? B PRO 50  
23 1 Y 1 B SER 166 ? B SER 162 
24 1 Y 1 B SER 167 ? B SER 163 
25 1 Y 1 B PRO 168 ? B PRO 164 
26 1 Y 1 B SER 169 ? B SER 165 
27 1 Y 1 B GLU 170 ? B GLU 166 
28 1 Y 1 B HIS 171 ? B HIS 167 
29 1 Y 1 B GLY 172 ? B GLY 168 
30 1 Y 1 B PRO 173 ? B PRO 169 
31 1 Y 1 B ARG 174 ? B ARG 170 
32 1 Y 1 B ALA 237 ? B ALA 233 
33 1 Y 1 B SER 238 ? B SER 234 
34 1 Y 1 C ALA 5   ? C ALA 1   
35 1 Y 1 C THR 49  ? C THR 45  
36 1 Y 1 C SER 50  ? C SER 46  
37 1 Y 1 C GLN 51  ? C GLN 47  
38 1 Y 1 C GLY 52  ? C GLY 48  
39 1 Y 1 C PRO 53  ? C PRO 49  
40 1 Y 1 C PRO 54  ? C PRO 50  
41 1 Y 1 C PRO 55  ? C PRO 51  
42 1 Y 1 C ARG 164 ? C ARG 160 
43 1 Y 1 C ALA 165 ? C ALA 161 
44 1 Y 1 C SER 166 ? C SER 162 
45 1 Y 1 C SER 167 ? C SER 163 
46 1 Y 1 C PRO 168 ? C PRO 164 
47 1 Y 1 C SER 169 ? C SER 165 
48 1 Y 1 C GLU 170 ? C GLU 166 
49 1 Y 1 C HIS 171 ? C HIS 167 
50 1 Y 1 C GLY 172 ? C GLY 168 
51 1 Y 1 C PRO 173 ? C PRO 169 
52 1 Y 1 C ARG 174 ? C ARG 170 
53 1 Y 1 C THR 236 ? C THR 232 
54 1 Y 1 C ALA 237 ? C ALA 233 
55 1 Y 1 C SER 238 ? C SER 234 
# 
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 
A1B7T C4   C  Y N 1   
A1B7T C5   C  Y N 2   
A1B7T C6   C  Y N 3   
A1B7T C7   C  Y N 4   
A1B7T C8   C  N N 5   
A1B7T C13  C  Y N 6   
A1B7T C15  C  Y N 7   
A1B7T C17  C  Y N 8   
A1B7T C20  C  Y N 9   
A1B7T C21  C  Y N 10  
A1B7T C22  C  Y N 11  
A1B7T C24  C  Y N 12  
A1B7T F1   F  N N 13  
A1B7T C2   C  Y N 14  
A1B7T C3   C  Y N 15  
A1B7T O9   O  N N 16  
A1B7T N10  N  N N 17  
A1B7T C11  C  N N 18  
A1B7T C12  C  Y N 19  
A1B7T C14  C  Y N 20  
A1B7T N16  N  Y N 21  
A1B7T C18  C  N N 22  
A1B7T C19  C  Y N 23  
A1B7T C23  C  Y N 24  
A1B7T CL25 CL N N 25  
A1B7T CL26 CL N N 26  
A1B7T F27  F  N N 27  
A1B7T H1   H  N N 28  
A1B7T H2   H  N N 29  
A1B7T H3   H  N N 30  
A1B7T H4   H  N N 31  
A1B7T H5   H  N N 32  
A1B7T H6   H  N N 33  
A1B7T H7   H  N N 34  
A1B7T H8   H  N N 35  
A1B7T H9   H  N N 36  
A1B7T H10  H  N N 37  
A1B7T H11  H  N N 38  
A1B7T H12  H  N N 39  
A1B7T H13  H  N N 40  
A1B7T H14  H  N N 41  
ALA   N    N  N N 42  
ALA   CA   C  N S 43  
ALA   C    C  N N 44  
ALA   O    O  N N 45  
ALA   CB   C  N N 46  
ALA   OXT  O  N N 47  
ALA   H    H  N N 48  
ALA   H2   H  N N 49  
ALA   HA   H  N N 50  
ALA   HB1  H  N N 51  
ALA   HB2  H  N N 52  
ALA   HB3  H  N N 53  
ALA   HXT  H  N N 54  
ARG   N    N  N N 55  
ARG   CA   C  N S 56  
ARG   C    C  N N 57  
ARG   O    O  N N 58  
ARG   CB   C  N N 59  
ARG   CG   C  N N 60  
ARG   CD   C  N N 61  
ARG   NE   N  N N 62  
ARG   CZ   C  N N 63  
ARG   NH1  N  N N 64  
ARG   NH2  N  N N 65  
ARG   OXT  O  N N 66  
ARG   H    H  N N 67  
ARG   H2   H  N N 68  
ARG   HA   H  N N 69  
ARG   HB2  H  N N 70  
ARG   HB3  H  N N 71  
ARG   HG2  H  N N 72  
ARG   HG3  H  N N 73  
ARG   HD2  H  N N 74  
ARG   HD3  H  N N 75  
ARG   HE   H  N N 76  
ARG   HH11 H  N N 77  
ARG   HH12 H  N N 78  
ARG   HH21 H  N N 79  
ARG   HH22 H  N N 80  
ARG   HXT  H  N N 81  
ASN   N    N  N N 82  
ASN   CA   C  N S 83  
ASN   C    C  N N 84  
ASN   O    O  N N 85  
ASN   CB   C  N N 86  
ASN   CG   C  N N 87  
ASN   OD1  O  N N 88  
ASN   ND2  N  N N 89  
ASN   OXT  O  N N 90  
ASN   H    H  N N 91  
ASN   H2   H  N N 92  
ASN   HA   H  N N 93  
ASN   HB2  H  N N 94  
ASN   HB3  H  N N 95  
ASN   HD21 H  N N 96  
ASN   HD22 H  N N 97  
ASN   HXT  H  N N 98  
ASP   N    N  N N 99  
ASP   CA   C  N S 100 
ASP   C    C  N N 101 
ASP   O    O  N N 102 
ASP   CB   C  N N 103 
ASP   CG   C  N N 104 
ASP   OD1  O  N N 105 
ASP   OD2  O  N N 106 
ASP   OXT  O  N N 107 
ASP   H    H  N N 108 
ASP   H2   H  N N 109 
ASP   HA   H  N N 110 
ASP   HB2  H  N N 111 
ASP   HB3  H  N N 112 
ASP   HD2  H  N N 113 
ASP   HXT  H  N N 114 
CYS   N    N  N N 115 
CYS   CA   C  N R 116 
CYS   C    C  N N 117 
CYS   O    O  N N 118 
CYS   CB   C  N N 119 
CYS   SG   S  N N 120 
CYS   OXT  O  N N 121 
CYS   H    H  N N 122 
CYS   H2   H  N N 123 
CYS   HA   H  N N 124 
CYS   HB2  H  N N 125 
CYS   HB3  H  N N 126 
CYS   HG   H  N N 127 
CYS   HXT  H  N N 128 
EDO   C1   C  N N 129 
EDO   O1   O  N N 130 
EDO   C2   C  N N 131 
EDO   O2   O  N N 132 
EDO   H11  H  N N 133 
EDO   H12  H  N N 134 
EDO   HO1  H  N N 135 
EDO   H21  H  N N 136 
EDO   H22  H  N N 137 
EDO   HO2  H  N N 138 
GLN   N    N  N N 139 
GLN   CA   C  N S 140 
GLN   C    C  N N 141 
GLN   O    O  N N 142 
GLN   CB   C  N N 143 
GLN   CG   C  N N 144 
GLN   CD   C  N N 145 
GLN   OE1  O  N N 146 
GLN   NE2  N  N N 147 
GLN   OXT  O  N N 148 
GLN   H    H  N N 149 
GLN   H2   H  N N 150 
GLN   HA   H  N N 151 
GLN   HB2  H  N N 152 
GLN   HB3  H  N N 153 
GLN   HG2  H  N N 154 
GLN   HG3  H  N N 155 
GLN   HE21 H  N N 156 
GLN   HE22 H  N N 157 
GLN   HXT  H  N N 158 
GLU   N    N  N N 159 
GLU   CA   C  N S 160 
GLU   C    C  N N 161 
GLU   O    O  N N 162 
GLU   CB   C  N N 163 
GLU   CG   C  N N 164 
GLU   CD   C  N N 165 
GLU   OE1  O  N N 166 
GLU   OE2  O  N N 167 
GLU   OXT  O  N N 168 
GLU   H    H  N N 169 
GLU   H2   H  N N 170 
GLU   HA   H  N N 171 
GLU   HB2  H  N N 172 
GLU   HB3  H  N N 173 
GLU   HG2  H  N N 174 
GLU   HG3  H  N N 175 
GLU   HE2  H  N N 176 
GLU   HXT  H  N N 177 
GLY   N    N  N N 178 
GLY   CA   C  N N 179 
GLY   C    C  N N 180 
GLY   O    O  N N 181 
GLY   OXT  O  N N 182 
GLY   H    H  N N 183 
GLY   H2   H  N N 184 
GLY   HA2  H  N N 185 
GLY   HA3  H  N N 186 
GLY   HXT  H  N N 187 
HIS   N    N  N N 188 
HIS   CA   C  N S 189 
HIS   C    C  N N 190 
HIS   O    O  N N 191 
HIS   CB   C  N N 192 
HIS   CG   C  Y N 193 
HIS   ND1  N  Y N 194 
HIS   CD2  C  Y N 195 
HIS   CE1  C  Y N 196 
HIS   NE2  N  Y N 197 
HIS   OXT  O  N N 198 
HIS   H    H  N N 199 
HIS   H2   H  N N 200 
HIS   HA   H  N N 201 
HIS   HB2  H  N N 202 
HIS   HB3  H  N N 203 
HIS   HD1  H  N N 204 
HIS   HD2  H  N N 205 
HIS   HE1  H  N N 206 
HIS   HE2  H  N N 207 
HIS   HXT  H  N N 208 
HOH   O    O  N N 209 
HOH   H1   H  N N 210 
HOH   H2   H  N N 211 
ILE   N    N  N N 212 
ILE   CA   C  N S 213 
ILE   C    C  N N 214 
ILE   O    O  N N 215 
ILE   CB   C  N S 216 
ILE   CG1  C  N N 217 
ILE   CG2  C  N N 218 
ILE   CD1  C  N N 219 
ILE   OXT  O  N N 220 
ILE   H    H  N N 221 
ILE   H2   H  N N 222 
ILE   HA   H  N N 223 
ILE   HB   H  N N 224 
ILE   HG12 H  N N 225 
ILE   HG13 H  N N 226 
ILE   HG21 H  N N 227 
ILE   HG22 H  N N 228 
ILE   HG23 H  N N 229 
ILE   HD11 H  N N 230 
ILE   HD12 H  N N 231 
ILE   HD13 H  N N 232 
ILE   HXT  H  N N 233 
LEU   N    N  N N 234 
LEU   CA   C  N S 235 
LEU   C    C  N N 236 
LEU   O    O  N N 237 
LEU   CB   C  N N 238 
LEU   CG   C  N N 239 
LEU   CD1  C  N N 240 
LEU   CD2  C  N N 241 
LEU   OXT  O  N N 242 
LEU   H    H  N N 243 
LEU   H2   H  N N 244 
LEU   HA   H  N N 245 
LEU   HB2  H  N N 246 
LEU   HB3  H  N N 247 
LEU   HG   H  N N 248 
LEU   HD11 H  N N 249 
LEU   HD12 H  N N 250 
LEU   HD13 H  N N 251 
LEU   HD21 H  N N 252 
LEU   HD22 H  N N 253 
LEU   HD23 H  N N 254 
LEU   HXT  H  N N 255 
LYS   N    N  N N 256 
LYS   CA   C  N S 257 
LYS   C    C  N N 258 
LYS   O    O  N N 259 
LYS   CB   C  N N 260 
LYS   CG   C  N N 261 
LYS   CD   C  N N 262 
LYS   CE   C  N N 263 
LYS   NZ   N  N N 264 
LYS   OXT  O  N N 265 
LYS   H    H  N N 266 
LYS   H2   H  N N 267 
LYS   HA   H  N N 268 
LYS   HB2  H  N N 269 
LYS   HB3  H  N N 270 
LYS   HG2  H  N N 271 
LYS   HG3  H  N N 272 
LYS   HD2  H  N N 273 
LYS   HD3  H  N N 274 
LYS   HE2  H  N N 275 
LYS   HE3  H  N N 276 
LYS   HZ1  H  N N 277 
LYS   HZ2  H  N N 278 
LYS   HZ3  H  N N 279 
LYS   HXT  H  N N 280 
MET   N    N  N N 281 
MET   CA   C  N S 282 
MET   C    C  N N 283 
MET   O    O  N N 284 
MET   CB   C  N N 285 
MET   CG   C  N N 286 
MET   SD   S  N N 287 
MET   CE   C  N N 288 
MET   OXT  O  N N 289 
MET   H    H  N N 290 
MET   H2   H  N N 291 
MET   HA   H  N N 292 
MET   HB2  H  N N 293 
MET   HB3  H  N N 294 
MET   HG2  H  N N 295 
MET   HG3  H  N N 296 
MET   HE1  H  N N 297 
MET   HE2  H  N N 298 
MET   HE3  H  N N 299 
MET   HXT  H  N N 300 
MG    MG   MG N N 301 
PHE   N    N  N N 302 
PHE   CA   C  N S 303 
PHE   C    C  N N 304 
PHE   O    O  N N 305 
PHE   CB   C  N N 306 
PHE   CG   C  Y N 307 
PHE   CD1  C  Y N 308 
PHE   CD2  C  Y N 309 
PHE   CE1  C  Y N 310 
PHE   CE2  C  Y N 311 
PHE   CZ   C  Y N 312 
PHE   OXT  O  N N 313 
PHE   H    H  N N 314 
PHE   H2   H  N N 315 
PHE   HA   H  N N 316 
PHE   HB2  H  N N 317 
PHE   HB3  H  N N 318 
PHE   HD1  H  N N 319 
PHE   HD2  H  N N 320 
PHE   HE1  H  N N 321 
PHE   HE2  H  N N 322 
PHE   HZ   H  N N 323 
PHE   HXT  H  N N 324 
PRO   N    N  N N 325 
PRO   CA   C  N S 326 
PRO   C    C  N N 327 
PRO   O    O  N N 328 
PRO   CB   C  N N 329 
PRO   CG   C  N N 330 
PRO   CD   C  N N 331 
PRO   OXT  O  N N 332 
PRO   H    H  N N 333 
PRO   HA   H  N N 334 
PRO   HB2  H  N N 335 
PRO   HB3  H  N N 336 
PRO   HG2  H  N N 337 
PRO   HG3  H  N N 338 
PRO   HD2  H  N N 339 
PRO   HD3  H  N N 340 
PRO   HXT  H  N N 341 
SER   N    N  N N 342 
SER   CA   C  N S 343 
SER   C    C  N N 344 
SER   O    O  N N 345 
SER   CB   C  N N 346 
SER   OG   O  N N 347 
SER   OXT  O  N N 348 
SER   H    H  N N 349 
SER   H2   H  N N 350 
SER   HA   H  N N 351 
SER   HB2  H  N N 352 
SER   HB3  H  N N 353 
SER   HG   H  N N 354 
SER   HXT  H  N N 355 
THR   N    N  N N 356 
THR   CA   C  N S 357 
THR   C    C  N N 358 
THR   O    O  N N 359 
THR   CB   C  N R 360 
THR   OG1  O  N N 361 
THR   CG2  C  N N 362 
THR   OXT  O  N N 363 
THR   H    H  N N 364 
THR   H2   H  N N 365 
THR   HA   H  N N 366 
THR   HB   H  N N 367 
THR   HG1  H  N N 368 
THR   HG21 H  N N 369 
THR   HG22 H  N N 370 
THR   HG23 H  N N 371 
THR   HXT  H  N N 372 
TRP   N    N  N N 373 
TRP   CA   C  N S 374 
TRP   C    C  N N 375 
TRP   O    O  N N 376 
TRP   CB   C  N N 377 
TRP   CG   C  Y N 378 
TRP   CD1  C  Y N 379 
TRP   CD2  C  Y N 380 
TRP   NE1  N  Y N 381 
TRP   CE2  C  Y N 382 
TRP   CE3  C  Y N 383 
TRP   CZ2  C  Y N 384 
TRP   CZ3  C  Y N 385 
TRP   CH2  C  Y N 386 
TRP   OXT  O  N N 387 
TRP   H    H  N N 388 
TRP   H2   H  N N 389 
TRP   HA   H  N N 390 
TRP   HB2  H  N N 391 
TRP   HB3  H  N N 392 
TRP   HD1  H  N N 393 
TRP   HE1  H  N N 394 
TRP   HE3  H  N N 395 
TRP   HZ2  H  N N 396 
TRP   HZ3  H  N N 397 
TRP   HH2  H  N N 398 
TRP   HXT  H  N N 399 
TYR   N    N  N N 400 
TYR   CA   C  N S 401 
TYR   C    C  N N 402 
TYR   O    O  N N 403 
TYR   CB   C  N N 404 
TYR   CG   C  Y N 405 
TYR   CD1  C  Y N 406 
TYR   CD2  C  Y N 407 
TYR   CE1  C  Y N 408 
TYR   CE2  C  Y N 409 
TYR   CZ   C  Y N 410 
TYR   OH   O  N N 411 
TYR   OXT  O  N N 412 
TYR   H    H  N N 413 
TYR   H2   H  N N 414 
TYR   HA   H  N N 415 
TYR   HB2  H  N N 416 
TYR   HB3  H  N N 417 
TYR   HD1  H  N N 418 
TYR   HD2  H  N N 419 
TYR   HE1  H  N N 420 
TYR   HE2  H  N N 421 
TYR   HH   H  N N 422 
TYR   HXT  H  N N 423 
VAL   N    N  N N 424 
VAL   CA   C  N S 425 
VAL   C    C  N N 426 
VAL   O    O  N N 427 
VAL   CB   C  N N 428 
VAL   CG1  C  N N 429 
VAL   CG2  C  N N 430 
VAL   OXT  O  N N 431 
VAL   H    H  N N 432 
VAL   H2   H  N N 433 
VAL   HA   H  N N 434 
VAL   HB   H  N N 435 
VAL   HG11 H  N N 436 
VAL   HG12 H  N N 437 
VAL   HG13 H  N N 438 
VAL   HG21 H  N N 439 
VAL   HG22 H  N N 440 
VAL   HG23 H  N N 441 
VAL   HXT  H  N N 442 
# 
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 
A1B7T CL25 C24  sing N N 1   
A1B7T O9   C8   doub N N 2   
A1B7T CL26 C23  sing N N 3   
A1B7T C24  C23  doub Y N 4   
A1B7T C24  C19  sing Y N 5   
A1B7T C23  C22  sing Y N 6   
A1B7T C18  C19  sing N N 7   
A1B7T C18  N10  sing N N 8   
A1B7T C19  C20  doub Y N 9   
A1B7T C8   N10  sing N N 10  
A1B7T C8   C6   sing N N 11  
A1B7T C22  C21  doub Y N 12  
A1B7T N10  C11  sing N N 13  
A1B7T C20  C21  sing Y N 14  
A1B7T C6   C5   doub Y N 15  
A1B7T C6   C7   sing Y N 16  
A1B7T C5   C4   sing Y N 17  
A1B7T C7   C2   doub Y N 18  
A1B7T C4   F27  sing N N 19  
A1B7T C4   C3   doub Y N 20  
A1B7T C2   C3   sing Y N 21  
A1B7T C2   F1   sing N N 22  
A1B7T C11  C12  sing N N 23  
A1B7T C17  C12  doub Y N 24  
A1B7T C17  N16  sing Y N 25  
A1B7T C12  C13  sing Y N 26  
A1B7T N16  C15  doub Y N 27  
A1B7T C13  C14  doub Y N 28  
A1B7T C15  C14  sing Y N 29  
A1B7T C5   H1   sing N N 30  
A1B7T C7   H2   sing N N 31  
A1B7T C13  H3   sing N N 32  
A1B7T C15  H4   sing N N 33  
A1B7T C17  H5   sing N N 34  
A1B7T C20  H6   sing N N 35  
A1B7T C21  H7   sing N N 36  
A1B7T C22  H8   sing N N 37  
A1B7T C3   H9   sing N N 38  
A1B7T C11  H10  sing N N 39  
A1B7T C11  H11  sing N N 40  
A1B7T C14  H12  sing N N 41  
A1B7T C18  H13  sing N N 42  
A1B7T C18  H14  sing N N 43  
ALA   N    CA   sing N N 44  
ALA   N    H    sing N N 45  
ALA   N    H2   sing N N 46  
ALA   CA   C    sing N N 47  
ALA   CA   CB   sing N N 48  
ALA   CA   HA   sing N N 49  
ALA   C    O    doub N N 50  
ALA   C    OXT  sing N N 51  
ALA   CB   HB1  sing N N 52  
ALA   CB   HB2  sing N N 53  
ALA   CB   HB3  sing N N 54  
ALA   OXT  HXT  sing N N 55  
ARG   N    CA   sing N N 56  
ARG   N    H    sing N N 57  
ARG   N    H2   sing N N 58  
ARG   CA   C    sing N N 59  
ARG   CA   CB   sing N N 60  
ARG   CA   HA   sing N N 61  
ARG   C    O    doub N N 62  
ARG   C    OXT  sing N N 63  
ARG   CB   CG   sing N N 64  
ARG   CB   HB2  sing N N 65  
ARG   CB   HB3  sing N N 66  
ARG   CG   CD   sing N N 67  
ARG   CG   HG2  sing N N 68  
ARG   CG   HG3  sing N N 69  
ARG   CD   NE   sing N N 70  
ARG   CD   HD2  sing N N 71  
ARG   CD   HD3  sing N N 72  
ARG   NE   CZ   sing N N 73  
ARG   NE   HE   sing N N 74  
ARG   CZ   NH1  sing N N 75  
ARG   CZ   NH2  doub N N 76  
ARG   NH1  HH11 sing N N 77  
ARG   NH1  HH12 sing N N 78  
ARG   NH2  HH21 sing N N 79  
ARG   NH2  HH22 sing N N 80  
ARG   OXT  HXT  sing N N 81  
ASN   N    CA   sing N N 82  
ASN   N    H    sing N N 83  
ASN   N    H2   sing N N 84  
ASN   CA   C    sing N N 85  
ASN   CA   CB   sing N N 86  
ASN   CA   HA   sing N N 87  
ASN   C    O    doub N N 88  
ASN   C    OXT  sing N N 89  
ASN   CB   CG   sing N N 90  
ASN   CB   HB2  sing N N 91  
ASN   CB   HB3  sing N N 92  
ASN   CG   OD1  doub N N 93  
ASN   CG   ND2  sing N N 94  
ASN   ND2  HD21 sing N N 95  
ASN   ND2  HD22 sing N N 96  
ASN   OXT  HXT  sing N N 97  
ASP   N    CA   sing N N 98  
ASP   N    H    sing N N 99  
ASP   N    H2   sing N N 100 
ASP   CA   C    sing N N 101 
ASP   CA   CB   sing N N 102 
ASP   CA   HA   sing N N 103 
ASP   C    O    doub N N 104 
ASP   C    OXT  sing N N 105 
ASP   CB   CG   sing N N 106 
ASP   CB   HB2  sing N N 107 
ASP   CB   HB3  sing N N 108 
ASP   CG   OD1  doub N N 109 
ASP   CG   OD2  sing N N 110 
ASP   OD2  HD2  sing N N 111 
ASP   OXT  HXT  sing N N 112 
CYS   N    CA   sing N N 113 
CYS   N    H    sing N N 114 
CYS   N    H2   sing N N 115 
CYS   CA   C    sing N N 116 
CYS   CA   CB   sing N N 117 
CYS   CA   HA   sing N N 118 
CYS   C    O    doub N N 119 
CYS   C    OXT  sing N N 120 
CYS   CB   SG   sing N N 121 
CYS   CB   HB2  sing N N 122 
CYS   CB   HB3  sing N N 123 
CYS   SG   HG   sing N N 124 
CYS   OXT  HXT  sing N N 125 
EDO   C1   O1   sing N N 126 
EDO   C1   C2   sing N N 127 
EDO   C1   H11  sing N N 128 
EDO   C1   H12  sing N N 129 
EDO   O1   HO1  sing N N 130 
EDO   C2   O2   sing N N 131 
EDO   C2   H21  sing N N 132 
EDO   C2   H22  sing N N 133 
EDO   O2   HO2  sing N N 134 
GLN   N    CA   sing N N 135 
GLN   N    H    sing N N 136 
GLN   N    H2   sing N N 137 
GLN   CA   C    sing N N 138 
GLN   CA   CB   sing N N 139 
GLN   CA   HA   sing N N 140 
GLN   C    O    doub N N 141 
GLN   C    OXT  sing N N 142 
GLN   CB   CG   sing N N 143 
GLN   CB   HB2  sing N N 144 
GLN   CB   HB3  sing N N 145 
GLN   CG   CD   sing N N 146 
GLN   CG   HG2  sing N N 147 
GLN   CG   HG3  sing N N 148 
GLN   CD   OE1  doub N N 149 
GLN   CD   NE2  sing N N 150 
GLN   NE2  HE21 sing N N 151 
GLN   NE2  HE22 sing N N 152 
GLN   OXT  HXT  sing N N 153 
GLU   N    CA   sing N N 154 
GLU   N    H    sing N N 155 
GLU   N    H2   sing N N 156 
GLU   CA   C    sing N N 157 
GLU   CA   CB   sing N N 158 
GLU   CA   HA   sing N N 159 
GLU   C    O    doub N N 160 
GLU   C    OXT  sing N N 161 
GLU   CB   CG   sing N N 162 
GLU   CB   HB2  sing N N 163 
GLU   CB   HB3  sing N N 164 
GLU   CG   CD   sing N N 165 
GLU   CG   HG2  sing N N 166 
GLU   CG   HG3  sing N N 167 
GLU   CD   OE1  doub N N 168 
GLU   CD   OE2  sing N N 169 
GLU   OE2  HE2  sing N N 170 
GLU   OXT  HXT  sing N N 171 
GLY   N    CA   sing N N 172 
GLY   N    H    sing N N 173 
GLY   N    H2   sing N N 174 
GLY   CA   C    sing N N 175 
GLY   CA   HA2  sing N N 176 
GLY   CA   HA3  sing N N 177 
GLY   C    O    doub N N 178 
GLY   C    OXT  sing N N 179 
GLY   OXT  HXT  sing N N 180 
HIS   N    CA   sing N N 181 
HIS   N    H    sing N N 182 
HIS   N    H2   sing N N 183 
HIS   CA   C    sing N N 184 
HIS   CA   CB   sing N N 185 
HIS   CA   HA   sing N N 186 
HIS   C    O    doub N N 187 
HIS   C    OXT  sing N N 188 
HIS   CB   CG   sing N N 189 
HIS   CB   HB2  sing N N 190 
HIS   CB   HB3  sing N N 191 
HIS   CG   ND1  sing Y N 192 
HIS   CG   CD2  doub Y N 193 
HIS   ND1  CE1  doub Y N 194 
HIS   ND1  HD1  sing N N 195 
HIS   CD2  NE2  sing Y N 196 
HIS   CD2  HD2  sing N N 197 
HIS   CE1  NE2  sing Y N 198 
HIS   CE1  HE1  sing N N 199 
HIS   NE2  HE2  sing N N 200 
HIS   OXT  HXT  sing N N 201 
HOH   O    H1   sing N N 202 
HOH   O    H2   sing N N 203 
ILE   N    CA   sing N N 204 
ILE   N    H    sing N N 205 
ILE   N    H2   sing N N 206 
ILE   CA   C    sing N N 207 
ILE   CA   CB   sing N N 208 
ILE   CA   HA   sing N N 209 
ILE   C    O    doub N N 210 
ILE   C    OXT  sing N N 211 
ILE   CB   CG1  sing N N 212 
ILE   CB   CG2  sing N N 213 
ILE   CB   HB   sing N N 214 
ILE   CG1  CD1  sing N N 215 
ILE   CG1  HG12 sing N N 216 
ILE   CG1  HG13 sing N N 217 
ILE   CG2  HG21 sing N N 218 
ILE   CG2  HG22 sing N N 219 
ILE   CG2  HG23 sing N N 220 
ILE   CD1  HD11 sing N N 221 
ILE   CD1  HD12 sing N N 222 
ILE   CD1  HD13 sing N N 223 
ILE   OXT  HXT  sing N N 224 
LEU   N    CA   sing N N 225 
LEU   N    H    sing N N 226 
LEU   N    H2   sing N N 227 
LEU   CA   C    sing N N 228 
LEU   CA   CB   sing N N 229 
LEU   CA   HA   sing N N 230 
LEU   C    O    doub N N 231 
LEU   C    OXT  sing N N 232 
LEU   CB   CG   sing N N 233 
LEU   CB   HB2  sing N N 234 
LEU   CB   HB3  sing N N 235 
LEU   CG   CD1  sing N N 236 
LEU   CG   CD2  sing N N 237 
LEU   CG   HG   sing N N 238 
LEU   CD1  HD11 sing N N 239 
LEU   CD1  HD12 sing N N 240 
LEU   CD1  HD13 sing N N 241 
LEU   CD2  HD21 sing N N 242 
LEU   CD2  HD22 sing N N 243 
LEU   CD2  HD23 sing N N 244 
LEU   OXT  HXT  sing N N 245 
LYS   N    CA   sing N N 246 
LYS   N    H    sing N N 247 
LYS   N    H2   sing N N 248 
LYS   CA   C    sing N N 249 
LYS   CA   CB   sing N N 250 
LYS   CA   HA   sing N N 251 
LYS   C    O    doub N N 252 
LYS   C    OXT  sing N N 253 
LYS   CB   CG   sing N N 254 
LYS   CB   HB2  sing N N 255 
LYS   CB   HB3  sing N N 256 
LYS   CG   CD   sing N N 257 
LYS   CG   HG2  sing N N 258 
LYS   CG   HG3  sing N N 259 
LYS   CD   CE   sing N N 260 
LYS   CD   HD2  sing N N 261 
LYS   CD   HD3  sing N N 262 
LYS   CE   NZ   sing N N 263 
LYS   CE   HE2  sing N N 264 
LYS   CE   HE3  sing N N 265 
LYS   NZ   HZ1  sing N N 266 
LYS   NZ   HZ2  sing N N 267 
LYS   NZ   HZ3  sing N N 268 
LYS   OXT  HXT  sing N N 269 
MET   N    CA   sing N N 270 
MET   N    H    sing N N 271 
MET   N    H2   sing N N 272 
MET   CA   C    sing N N 273 
MET   CA   CB   sing N N 274 
MET   CA   HA   sing N N 275 
MET   C    O    doub N N 276 
MET   C    OXT  sing N N 277 
MET   CB   CG   sing N N 278 
MET   CB   HB2  sing N N 279 
MET   CB   HB3  sing N N 280 
MET   CG   SD   sing N N 281 
MET   CG   HG2  sing N N 282 
MET   CG   HG3  sing N N 283 
MET   SD   CE   sing N N 284 
MET   CE   HE1  sing N N 285 
MET   CE   HE2  sing N N 286 
MET   CE   HE3  sing N N 287 
MET   OXT  HXT  sing N N 288 
PHE   N    CA   sing N N 289 
PHE   N    H    sing N N 290 
PHE   N    H2   sing N N 291 
PHE   CA   C    sing N N 292 
PHE   CA   CB   sing N N 293 
PHE   CA   HA   sing N N 294 
PHE   C    O    doub N N 295 
PHE   C    OXT  sing N N 296 
PHE   CB   CG   sing N N 297 
PHE   CB   HB2  sing N N 298 
PHE   CB   HB3  sing N N 299 
PHE   CG   CD1  doub Y N 300 
PHE   CG   CD2  sing Y N 301 
PHE   CD1  CE1  sing Y N 302 
PHE   CD1  HD1  sing N N 303 
PHE   CD2  CE2  doub Y N 304 
PHE   CD2  HD2  sing N N 305 
PHE   CE1  CZ   doub Y N 306 
PHE   CE1  HE1  sing N N 307 
PHE   CE2  CZ   sing Y N 308 
PHE   CE2  HE2  sing N N 309 
PHE   CZ   HZ   sing N N 310 
PHE   OXT  HXT  sing N N 311 
PRO   N    CA   sing N N 312 
PRO   N    CD   sing N N 313 
PRO   N    H    sing N N 314 
PRO   CA   C    sing N N 315 
PRO   CA   CB   sing N N 316 
PRO   CA   HA   sing N N 317 
PRO   C    O    doub N N 318 
PRO   C    OXT  sing N N 319 
PRO   CB   CG   sing N N 320 
PRO   CB   HB2  sing N N 321 
PRO   CB   HB3  sing N N 322 
PRO   CG   CD   sing N N 323 
PRO   CG   HG2  sing N N 324 
PRO   CG   HG3  sing N N 325 
PRO   CD   HD2  sing N N 326 
PRO   CD   HD3  sing N N 327 
PRO   OXT  HXT  sing N N 328 
SER   N    CA   sing N N 329 
SER   N    H    sing N N 330 
SER   N    H2   sing N N 331 
SER   CA   C    sing N N 332 
SER   CA   CB   sing N N 333 
SER   CA   HA   sing N N 334 
SER   C    O    doub N N 335 
SER   C    OXT  sing N N 336 
SER   CB   OG   sing N N 337 
SER   CB   HB2  sing N N 338 
SER   CB   HB3  sing N N 339 
SER   OG   HG   sing N N 340 
SER   OXT  HXT  sing N N 341 
THR   N    CA   sing N N 342 
THR   N    H    sing N N 343 
THR   N    H2   sing N N 344 
THR   CA   C    sing N N 345 
THR   CA   CB   sing N N 346 
THR   CA   HA   sing N N 347 
THR   C    O    doub N N 348 
THR   C    OXT  sing N N 349 
THR   CB   OG1  sing N N 350 
THR   CB   CG2  sing N N 351 
THR   CB   HB   sing N N 352 
THR   OG1  HG1  sing N N 353 
THR   CG2  HG21 sing N N 354 
THR   CG2  HG22 sing N N 355 
THR   CG2  HG23 sing N N 356 
THR   OXT  HXT  sing N N 357 
TRP   N    CA   sing N N 358 
TRP   N    H    sing N N 359 
TRP   N    H2   sing N N 360 
TRP   CA   C    sing N N 361 
TRP   CA   CB   sing N N 362 
TRP   CA   HA   sing N N 363 
TRP   C    O    doub N N 364 
TRP   C    OXT  sing N N 365 
TRP   CB   CG   sing N N 366 
TRP   CB   HB2  sing N N 367 
TRP   CB   HB3  sing N N 368 
TRP   CG   CD1  doub Y N 369 
TRP   CG   CD2  sing Y N 370 
TRP   CD1  NE1  sing Y N 371 
TRP   CD1  HD1  sing N N 372 
TRP   CD2  CE2  doub Y N 373 
TRP   CD2  CE3  sing Y N 374 
TRP   NE1  CE2  sing Y N 375 
TRP   NE1  HE1  sing N N 376 
TRP   CE2  CZ2  sing Y N 377 
TRP   CE3  CZ3  doub Y N 378 
TRP   CE3  HE3  sing N N 379 
TRP   CZ2  CH2  doub Y N 380 
TRP   CZ2  HZ2  sing N N 381 
TRP   CZ3  CH2  sing Y N 382 
TRP   CZ3  HZ3  sing N N 383 
TRP   CH2  HH2  sing N N 384 
TRP   OXT  HXT  sing N N 385 
TYR   N    CA   sing N N 386 
TYR   N    H    sing N N 387 
TYR   N    H2   sing N N 388 
TYR   CA   C    sing N N 389 
TYR   CA   CB   sing N N 390 
TYR   CA   HA   sing N N 391 
TYR   C    O    doub N N 392 
TYR   C    OXT  sing N N 393 
TYR   CB   CG   sing N N 394 
TYR   CB   HB2  sing N N 395 
TYR   CB   HB3  sing N N 396 
TYR   CG   CD1  doub Y N 397 
TYR   CG   CD2  sing Y N 398 
TYR   CD1  CE1  sing Y N 399 
TYR   CD1  HD1  sing N N 400 
TYR   CD2  CE2  doub Y N 401 
TYR   CD2  HD2  sing N N 402 
TYR   CE1  CZ   doub Y N 403 
TYR   CE1  HE1  sing N N 404 
TYR   CE2  CZ   sing Y N 405 
TYR   CE2  HE2  sing N N 406 
TYR   CZ   OH   sing N N 407 
TYR   OH   HH   sing N N 408 
TYR   OXT  HXT  sing N N 409 
VAL   N    CA   sing N N 410 
VAL   N    H    sing N N 411 
VAL   N    H2   sing N N 412 
VAL   CA   C    sing N N 413 
VAL   CA   CB   sing N N 414 
VAL   CA   HA   sing N N 415 
VAL   C    O    doub N N 416 
VAL   C    OXT  sing N N 417 
VAL   CB   CG1  sing N N 418 
VAL   CB   CG2  sing N N 419 
VAL   CB   HB   sing N N 420 
VAL   CG1  HG11 sing N N 421 
VAL   CG1  HG12 sing N N 422 
VAL   CG1  HG13 sing N N 423 
VAL   CG2  HG21 sing N N 424 
VAL   CG2  HG22 sing N N 425 
VAL   CG2  HG23 sing N N 426 
VAL   OXT  HXT  sing N N 427 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                Canada 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7TQO 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9O0Y 
_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]   0.012916 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006525 
_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]   0.007117 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
MG 
N  
O  
S  
X  
# 
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    . ALA   A 1 1   ? 31.629  -3.773  34.559  1.00 34.58 ? 5   ALA   A N    1 
ATOM   2    C  CA   . ALA   A 1 1   ? 30.416  -4.247  33.847  1.00 32.68 ? 5   ALA   A CA   1 
ATOM   3    C  C    . ALA   A 1 1   ? 30.397  -3.674  32.435  1.00 30.22 ? 5   ALA   A C    1 
ATOM   4    O  O    . ALA   A 1 1   ? 30.792  -2.530  32.220  1.00 32.45 ? 5   ALA   A O    1 
ATOM   5    C  CB   . ALA   A 1 1   ? 29.164  -3.857  34.602  1.00 34.72 ? 5   ALA   A CB   1 
ATOM   6    N  N    . LEU   A 1 2   ? 29.921  -4.480  31.485  1.00 26.88 ? 6   LEU   A N    1 
ATOM   7    C  CA   . LEU   A 1 2   ? 29.805  -4.043  30.106  1.00 25.40 ? 6   LEU   A CA   1 
ATOM   8    C  C    . LEU   A 1 2   ? 28.419  -3.452  29.885  1.00 26.15 ? 6   LEU   A C    1 
ATOM   9    O  O    . LEU   A 1 2   ? 27.426  -4.174  29.962  1.00 27.61 ? 6   LEU   A O    1 
ATOM   10   C  CB   . LEU   A 1 2   ? 30.037  -5.240  29.190  1.00 24.80 ? 6   LEU   A CB   1 
ATOM   11   C  CG   . LEU   A 1 2   ? 31.392  -5.934  29.325  1.00 24.90 ? 6   LEU   A CG   1 
ATOM   12   C  CD1  . LEU   A 1 2   ? 31.465  -6.993  28.256  1.00 26.10 ? 6   LEU   A CD1  1 
ATOM   13   C  CD2  . LEU   A 1 2   ? 32.573  -4.992  29.217  1.00 25.14 ? 6   LEU   A CD2  1 
ATOM   14   N  N    . PRO   A 1 3   ? 28.314  -2.140  29.570  1.00 26.01 ? 7   PRO   A N    1 
ATOM   15   C  CA   . PRO   A 1 3   ? 27.013  -1.472  29.509  1.00 26.38 ? 7   PRO   A CA   1 
ATOM   16   C  C    . PRO   A 1 3   ? 26.088  -2.005  28.415  1.00 25.67 ? 7   PRO   A C    1 
ATOM   17   O  O    . PRO   A 1 3   ? 24.866  -1.948  28.559  1.00 27.38 ? 7   PRO   A O    1 
ATOM   18   C  CB   . PRO   A 1 3   ? 27.395  0.007   29.292  1.00 26.54 ? 7   PRO   A CB   1 
ATOM   19   C  CG   . PRO   A 1 3   ? 28.754  -0.043  28.629  1.00 27.18 ? 7   PRO   A CG   1 
ATOM   20   C  CD   . PRO   A 1 3   ? 29.439  -1.243  29.262  1.00 26.02 ? 7   PRO   A CD   1 
ATOM   21   N  N    . HIS   A 1 4   ? 26.680  -2.533  27.334  1.00 24.53 ? 8   HIS   A N    1 
ATOM   22   C  CA   . HIS   A 1 4   ? 25.918  -2.966  26.173  1.00 23.67 ? 8   HIS   A CA   1 
ATOM   23   C  C    . HIS   A 1 4   ? 26.404  -4.322  25.660  1.00 22.55 ? 8   HIS   A C    1 
ATOM   24   O  O    . HIS   A 1 4   ? 26.152  -4.659  24.508  1.00 23.54 ? 8   HIS   A O    1 
ATOM   25   C  CB   . HIS   A 1 4   ? 25.964  -1.877  25.099  1.00 25.08 ? 8   HIS   A CB   1 
ATOM   26   C  CG   . HIS   A 1 4   ? 25.462  -0.570  25.603  1.00 26.01 ? 8   HIS   A CG   1 
ATOM   27   N  ND1  . HIS   A 1 4   ? 24.121  -0.349  25.839  1.00 27.02 ? 8   HIS   A ND1  1 
ATOM   28   C  CD2  . HIS   A 1 4   ? 26.096  0.562   25.962  1.00 26.90 ? 8   HIS   A CD2  1 
ATOM   29   C  CE1  . HIS   A 1 4   ? 23.960  0.884   26.304  1.00 27.67 ? 8   HIS   A CE1  1 
ATOM   30   N  NE2  . HIS   A 1 4   ? 25.146  1.450   26.398  1.00 27.01 ? 8   HIS   A NE2  1 
ATOM   31   N  N    . GLY   A 1 5   ? 27.047  -5.114  26.528  1.00 20.92 ? 9   GLY   A N    1 
ATOM   32   C  CA   . GLY   A 1 5   ? 27.611  -6.399  26.137  1.00 19.59 ? 9   GLY   A CA   1 
ATOM   33   C  C    . GLY   A 1 5   ? 28.833  -6.229  25.234  1.00 18.10 ? 9   GLY   A C    1 
ATOM   34   O  O    . GLY   A 1 5   ? 29.344  -5.124  25.050  1.00 19.48 ? 9   GLY   A O    1 
ATOM   35   N  N    . HIS   A 1 6   ? 29.307  -7.339  24.669  1.00 16.07 ? 10  HIS   A N    1 
ATOM   36   C  CA   . HIS   A 1 6   ? 30.494  -7.295  23.830  1.00 14.88 ? 10  HIS   A CA   1 
ATOM   37   C  C    . HIS   A 1 6   ? 30.130  -6.810  22.427  1.00 14.36 ? 10  HIS   A C    1 
ATOM   38   O  O    . HIS   A 1 6   ? 29.194  -7.303  21.813  1.00 14.59 ? 10  HIS   A O    1 
ATOM   39   C  CB   . HIS   A 1 6   ? 31.153  -8.675  23.771  1.00 15.61 ? 10  HIS   A CB   1 
ATOM   40   C  CG   . HIS   A 1 6   ? 31.792  -9.094  25.054  1.00 16.13 ? 10  HIS   A CG   1 
ATOM   41   N  ND1  . HIS   A 1 6   ? 33.012  -8.581  25.444  1.00 17.06 ? 10  HIS   A ND1  1 
ATOM   42   C  CD2  . HIS   A 1 6   ? 31.424  -9.960  26.022  1.00 17.14 ? 10  HIS   A CD2  1 
ATOM   43   C  CE1  . HIS   A 1 6   ? 33.363  -9.130  26.603  1.00 17.75 ? 10  HIS   A CE1  1 
ATOM   44   N  NE2  . HIS   A 1 6   ? 32.414  -9.971  26.975  1.00 17.36 ? 10  HIS   A NE2  1 
ATOM   45   N  N    . MET   A 1 7   ? 30.914  -5.864  21.909  1.00 13.32 ? 11  MET   A N    1 
ATOM   46   C  CA   . MET   A 1 7   ? 30.755  -5.409  20.537  1.00 13.36 ? 11  MET   A CA   1 
ATOM   47   C  C    . MET   A 1 7   ? 31.218  -6.515  19.584  1.00 12.72 ? 11  MET   A C    1 
ATOM   48   O  O    . MET   A 1 7   ? 32.301  -7.071  19.755  1.00 13.48 ? 11  MET   A O    1 
ATOM   49   C  CB   . MET   A 1 7   ? 31.582  -4.141  20.309  1.00 13.53 ? 11  MET   A CB   1 
ATOM   50   C  CG   . MET   A 1 7   ? 31.187  -2.939  21.160  1.00 14.00 ? 11  MET   A CG   1 
ATOM   51   S  SD   . MET   A 1 7   ? 29.506  -2.356  20.902  1.00 15.21 ? 11  MET   A SD   1 
ATOM   52   C  CE   . MET   A 1 7   ? 28.633  -2.844  22.395  1.00 16.42 ? 11  MET   A CE   1 
ATOM   53   N  N    . GLN   A 1 8   ? 30.415  -6.833  18.561  1.00 12.28 ? 12  GLN   A N    1 
ATOM   54   C  CA   . GLN   A 1 8   ? 30.755  -7.914  17.642  1.00 12.23 ? 12  GLN   A CA   1 
ATOM   55   C  C    . GLN   A 1 8   ? 31.534  -7.405  16.429  1.00 12.28 ? 12  GLN   A C    1 
ATOM   56   O  O    . GLN   A 1 8   ? 32.351  -8.142  15.879  1.00 12.83 ? 12  GLN   A O    1 
ATOM   57   C  CB   . GLN   A 1 8   ? 29.511  -8.671  17.183  1.00 12.83 ? 12  GLN   A CB   1 
ATOM   58   C  CG   . GLN   A 1 8   ? 28.780  -9.345  18.332  1.00 13.14 ? 12  GLN   A CG   1 
ATOM   59   C  CD   . GLN   A 1 8   ? 29.708  -10.228 19.137  1.00 12.99 ? 12  GLN   A CD   1 
ATOM   60   O  OE1  . GLN   A 1 8   ? 30.160  -11.271 18.651  1.00 13.92 ? 12  GLN   A OE1  1 
ATOM   61   N  NE2  . GLN   A 1 8   ? 30.010  -9.827  20.364  1.00 12.68 ? 12  GLN   A NE2  1 
ATOM   62   N  N    . THR   A 1 9   ? 31.247  -6.174  15.998  1.00 12.55 ? 13  THR   A N    1 
ATOM   63   C  CA   . THR   A 1 9   ? 31.953  -5.565  14.880  1.00 12.87 ? 13  THR   A CA   1 
ATOM   64   C  C    . THR   A 1 9   ? 32.454  -4.192  15.315  1.00 12.86 ? 13  THR   A C    1 
ATOM   65   O  O    . THR   A 1 9   ? 31.687  -3.401  15.861  1.00 13.79 ? 13  THR   A O    1 
ATOM   66   C  CB   . THR   A 1 9   ? 31.059  -5.421  13.650  1.00 13.93 ? 13  THR   A CB   1 
ATOM   67   O  OG1  . THR   A 1 9   ? 30.423  -6.660  13.347  1.00 14.30 ? 13  THR   A OG1  1 
ATOM   68   C  CG2  . THR   A 1 9   ? 31.873  -4.981  12.446  1.00 15.35 ? 13  THR   A CG2  1 
ATOM   69   N  N    . LEU   A 1 10  ? 33.733  -3.926  15.057  1.00 12.31 ? 14  LEU   A N    1 
ATOM   70   C  CA   . LEU   A 1 10  ? 34.284  -2.586  15.176  1.00 12.87 ? 14  LEU   A CA   1 
ATOM   71   C  C    . LEU   A 1 10  ? 34.335  -2.004  13.773  1.00 12.27 ? 14  LEU   A C    1 
ATOM   72   O  O    . LEU   A 1 10  ? 34.914  -2.611  12.871  1.00 12.76 ? 14  LEU   A O    1 
ATOM   73   C  CB   . LEU   A 1 10  ? 35.654  -2.598  15.846  1.00 15.19 ? 14  LEU   A CB   1 
ATOM   74   C  CG   . LEU   A 1 10  ? 35.625  -2.530  17.386  1.00 18.30 ? 14  LEU   A CG   1 
ATOM   75   C  CD1  . LEU   A 1 10  ? 34.777  -3.583  18.037  1.00 20.65 ? 14  LEU   A CD1  1 
ATOM   76   C  CD2  . LEU   A 1 10  ? 37.053  -2.525  17.929  1.00 19.57 ? 14  LEU   A CD2  1 
ATOM   77   N  N    . ILE   A 1 11  ? 33.674  -0.860  13.590  1.00 11.89 ? 15  ILE   A N    1 
ATOM   78   C  CA   . ILE   A 1 11  ? 33.670  -0.192  12.300  1.00 11.97 ? 15  ILE   A CA   1 
ATOM   79   C  C    . ILE   A 1 11  ? 34.566  1.031   12.427  1.00 11.68 ? 15  ILE   A C    1 
ATOM   80   O  O    . ILE   A 1 11  ? 34.149  2.054   12.975  1.00 12.42 ? 15  ILE   A O    1 
ATOM   81   C  CB   . ILE   A 1 11  ? 32.258  0.178   11.815  1.00 14.11 ? 15  ILE   A CB   1 
ATOM   82   C  CG1  . ILE   A 1 11  ? 31.317  -1.033  11.804  1.00 16.94 ? 15  ILE   A CG1  1 
ATOM   83   C  CG2  . ILE   A 1 11  ? 32.348  0.820   10.433  1.00 14.62 ? 15  ILE   A CG2  1 
ATOM   84   C  CD1  . ILE   A 1 11  ? 30.472  -1.147  13.049  1.00 19.61 ? 15  ILE   A CD1  1 
ATOM   85   N  N    . PHE   A 1 12  ? 35.811  0.881   11.973  1.00 11.30 ? 16  PHE   A N    1 
ATOM   86   C  CA   . PHE   A 1 12  ? 36.740  1.991   11.933  1.00 11.69 ? 16  PHE   A CA   1 
ATOM   87   C  C    . PHE   A 1 12  ? 36.199  2.982   10.912  1.00 11.64 ? 16  PHE   A C    1 
ATOM   88   O  O    . PHE   A 1 12  ? 35.828  2.599   9.802   1.00 12.49 ? 16  PHE   A O    1 
ATOM   89   C  CB   . PHE   A 1 12  ? 38.156  1.496   11.634  1.00 12.10 ? 16  PHE   A CB   1 
ATOM   90   C  CG   . PHE   A 1 12  ? 38.673  0.604   12.750  1.00 13.15 ? 16  PHE   A CG   1 
ATOM   91   C  CD1  . PHE   A 1 12  ? 39.306  1.151   13.857  1.00 13.78 ? 16  PHE   A CD1  1 
ATOM   92   C  CD2  . PHE   A 1 12  ? 38.460  -0.766  12.728  1.00 13.32 ? 16  PHE   A CD2  1 
ATOM   93   C  CE1  . PHE   A 1 12  ? 39.721  0.341   14.905  1.00 14.61 ? 16  PHE   A CE1  1 
ATOM   94   C  CE2  . PHE   A 1 12  ? 38.877  -1.564  13.775  1.00 14.10 ? 16  PHE   A CE2  1 
ATOM   95   C  CZ   . PHE   A 1 12  ? 39.510  -1.009  14.858  1.00 14.15 ? 16  PHE   A CZ   1 
ATOM   96   N  N    . PHE   A 1 13  ? 36.156  4.258   11.300  1.00 11.41 ? 17  PHE   A N    1 
ATOM   97   C  CA   . PHE   A 1 13  ? 35.373  5.251   10.585  1.00 11.03 ? 17  PHE   A CA   1 
ATOM   98   C  C    . PHE   A 1 13  ? 36.149  6.551   10.512  1.00 11.15 ? 17  PHE   A C    1 
ATOM   99   O  O    . PHE   A 1 13  ? 36.678  7.019   11.514  1.00 11.77 ? 17  PHE   A O    1 
ATOM   100  C  CB   . PHE   A 1 13  ? 34.059  5.435   11.344  1.00 11.56 ? 17  PHE   A CB   1 
ATOM   101  C  CG   . PHE   A 1 13  ? 33.095  6.485   10.817  1.00 11.93 ? 17  PHE   A CG   1 
ATOM   102  C  CD1  . PHE   A 1 13  ? 32.759  6.558   9.471   1.00 12.59 ? 17  PHE   A CD1  1 
ATOM   103  C  CD2  . PHE   A 1 13  ? 32.514  7.405   11.683  1.00 12.80 ? 17  PHE   A CD2  1 
ATOM   104  C  CE1  . PHE   A 1 13  ? 31.874  7.526   9.017   1.00 12.89 ? 17  PHE   A CE1  1 
ATOM   105  C  CE2  . PHE   A 1 13  ? 31.618  8.355   11.211  1.00 13.20 ? 17  PHE   A CE2  1 
ATOM   106  C  CZ   . PHE   A 1 13  ? 31.304  8.411   9.883   1.00 12.91 ? 17  PHE   A CZ   1 
ATOM   107  N  N    . ASP   A 1 14  ? 36.174  7.136   9.321   1.00 10.56 ? 18  ASP   A N    1 
ATOM   108  C  CA   . ASP   A 1 14  ? 36.755  8.450   9.149   1.00 10.98 ? 18  ASP   A CA   1 
ATOM   109  C  C    . ASP   A 1 14  ? 36.045  9.179   8.021   1.00 10.66 ? 18  ASP   A C    1 
ATOM   110  O  O    . ASP   A 1 14  ? 35.739  8.588   6.992   1.00 11.52 ? 18  ASP   A O    1 
ATOM   111  C  CB   . ASP   A 1 14  ? 38.242  8.399   8.857   1.00 11.80 ? 18  ASP   A CB   1 
ATOM   112  C  CG   . ASP   A 1 14  ? 38.932  9.745   9.001   1.00 13.35 ? 18  ASP   A CG   1 
ATOM   113  O  OD1  . ASP   A 1 14  ? 39.075  10.213  10.157  1.00 14.24 ? 18  ASP   A OD1  1 
ATOM   114  O  OD2  . ASP   A 1 14  ? 39.258  10.344  7.958   1.00 14.67 ? 18  ASP   A OD2  1 
ATOM   115  N  N    . MET   A 1 15  ? 35.830  10.474  8.224   1.00 10.83 ? 19  MET   A N    1 
ATOM   116  C  CA   . MET   A 1 15  ? 35.306  11.333  7.180   1.00 10.93 ? 19  MET   A CA   1 
ATOM   117  C  C    . MET   A 1 15  ? 36.236  12.515  6.941   1.00 10.95 ? 19  MET   A C    1 
ATOM   118  O  O    . MET   A 1 15  ? 36.985  12.944  7.817   1.00 11.44 ? 19  MET   A O    1 
ATOM   119  C  CB   . MET   A 1 15  ? 33.920  11.865  7.545   1.00 11.65 ? 19  MET   A CB   1 
ATOM   120  C  CG   . MET   A 1 15  ? 32.938  10.727  7.782   1.00 12.30 ? 19  MET   A CG   1 
ATOM   121  S  SD   . MET   A 1 15  ? 31.201  11.148  7.551   1.00 13.89 ? 19  MET   A SD   1 
ATOM   122  C  CE   . MET   A 1 15  ? 30.983  12.320  8.892   1.00 13.96 ? 19  MET   A CE   1 
ATOM   123  N  N    A GLU   A 1 16  ? 36.177  13.030  5.706   0.50 10.80 ? 20  GLU   A N    1 
ATOM   124  N  N    B GLU   A 1 16  ? 36.127  13.062  5.732   0.50 10.69 ? 20  GLU   A N    1 
ATOM   125  C  CA   A GLU   A 1 16  ? 36.738  14.322  5.344   0.50 11.28 ? 20  GLU   A CA   1 
ATOM   126  C  CA   B GLU   A 1 16  ? 36.718  14.344  5.407   0.50 11.08 ? 20  GLU   A CA   1 
ATOM   127  C  C    A GLU   A 1 16  ? 35.562  15.283  5.177   0.50 10.89 ? 20  GLU   A C    1 
ATOM   128  C  C    B GLU   A 1 16  ? 35.570  15.298  5.116   0.50 10.84 ? 20  GLU   A C    1 
ATOM   129  O  O    A GLU   A 1 16  ? 34.449  14.857  4.873   0.50 10.65 ? 20  GLU   A O    1 
ATOM   130  O  O    B GLU   A 1 16  ? 34.498  14.884  4.681   0.50 10.72 ? 20  GLU   A O    1 
ATOM   131  C  CB   A GLU   A 1 16  ? 37.531  14.278  4.034   0.50 12.31 ? 20  GLU   A CB   1 
ATOM   132  C  CB   B GLU   A 1 16  ? 37.702  14.185  4.252   0.50 12.01 ? 20  GLU   A CB   1 
ATOM   133  C  CG   A GLU   A 1 16  ? 38.663  13.250  3.974   0.50 13.67 ? 20  GLU   A CG   1 
ATOM   134  C  CG   B GLU   A 1 16  ? 38.897  13.329  4.653   0.50 12.97 ? 20  GLU   A CG   1 
ATOM   135  C  CD   A GLU   A 1 16  ? 39.899  13.488  4.829   0.50 15.72 ? 20  GLU   A CD   1 
ATOM   136  C  CD   B GLU   A 1 16  ? 39.983  13.204  3.610   0.50 14.28 ? 20  GLU   A CD   1 
ATOM   137  O  OE1  A GLU   A 1 16  ? 39.953  14.537  5.495   0.50 17.62 ? 20  GLU   A OE1  1 
ATOM   138  O  OE1  B GLU   A 1 16  ? 39.698  13.515  2.445   0.50 16.58 ? 20  GLU   A OE1  1 
ATOM   139  O  OE2  A GLU   A 1 16  ? 40.804  12.609  4.860   0.50 17.92 ? 20  GLU   A OE2  1 
ATOM   140  O  OE2  B GLU   A 1 16  ? 41.120  12.834  3.961   0.50 16.04 ? 20  GLU   A OE2  1 
ATOM   141  N  N    . ALA   A 1 17  ? 35.810  16.577  5.378   1.00 10.93 ? 21  ALA   A N    1 
ATOM   142  C  CA   . ALA   A 1 17  ? 34.771  17.585  5.274   1.00 10.82 ? 21  ALA   A CA   1 
ATOM   143  C  C    . ALA   A 1 17  ? 35.340  18.879  4.690   1.00 11.11 ? 21  ALA   A C    1 
ATOM   144  O  O    . ALA   A 1 17  ? 36.546  19.016  4.480   1.00 12.05 ? 21  ALA   A O    1 
ATOM   145  C  CB   . ALA   A 1 17  ? 34.160  17.814  6.640   1.00 11.25 ? 21  ALA   A CB   1 
ATOM   146  N  N    . THR   A 1 18  ? 34.437  19.827  4.440   1.00 10.83 ? 22  THR   A N    1 
ATOM   147  C  CA   . THR   A 1 18  ? 34.775  21.097  3.816   1.00 10.89 ? 22  THR   A CA   1 
ATOM   148  C  C    . THR   A 1 18  ? 35.581  22.009  4.743   1.00 11.38 ? 22  THR   A C    1 
ATOM   149  O  O    . THR   A 1 18  ? 36.162  22.980  4.274   1.00 12.39 ? 22  THR   A O    1 
ATOM   150  C  CB   . THR   A 1 18  ? 33.497  21.808  3.374   1.00 11.12 ? 22  THR   A CB   1 
ATOM   151  O  OG1  . THR   A 1 18  ? 32.596  21.903  4.474   1.00 11.32 ? 22  THR   A OG1  1 
ATOM   152  C  CG2  . THR   A 1 18  ? 32.808  21.093  2.232   1.00 11.53 ? 22  THR   A CG2  1 
ATOM   153  N  N    . GLY   A 1 19  ? 35.544  21.753  6.050   1.00 11.08 ? 23  GLY   A N    1 
ATOM   154  C  CA   . GLY   A 1 19  ? 36.162  22.618  7.039   1.00 11.13 ? 23  GLY   A CA   1 
ATOM   155  C  C    . GLY   A 1 19  ? 35.997  22.010  8.423   1.00 11.21 ? 23  GLY   A C    1 
ATOM   156  O  O    . GLY   A 1 19  ? 35.478  20.911  8.547   1.00 10.95 ? 23  GLY   A O    1 
ATOM   157  N  N    . LEU   A 1 20  ? 36.412  22.745  9.451   1.00 12.27 ? 24  LEU   A N    1 
ATOM   158  C  CA   . LEU   A 1 20  ? 36.281  22.306  10.826  1.00 12.29 ? 24  LEU   A CA   1 
ATOM   159  C  C    . LEU   A 1 20  ? 34.881  22.621  11.349  1.00 12.62 ? 24  LEU   A C    1 
ATOM   160  O  O    . LEU   A 1 20  ? 34.108  23.348  10.722  1.00 12.68 ? 24  LEU   A O    1 
ATOM   161  C  CB   . LEU   A 1 20  ? 37.366  22.967  11.663  1.00 12.68 ? 24  LEU   A CB   1 
ATOM   162  C  CG   . LEU   A 1 20  ? 38.803  22.646  11.253  1.00 13.77 ? 24  LEU   A CG   1 
ATOM   163  C  CD1  . LEU   A 1 20  ? 39.771  23.429  12.123  1.00 14.83 ? 24  LEU   A CD1  1 
ATOM   164  C  CD2  . LEU   A 1 20  ? 39.092  21.158  11.307  1.00 15.05 ? 24  LEU   A CD2  1 
ATOM   165  N  N    . PRO   A 1 21  ? 34.485  22.042  12.504  1.00 12.67 ? 25  PRO   A N    1 
ATOM   166  C  CA   . PRO   A 1 21  ? 33.107  22.193  12.982  1.00 12.71 ? 25  PRO   A CA   1 
ATOM   167  C  C    . PRO   A 1 21  ? 32.552  23.616  13.038  1.00 13.26 ? 25  PRO   A C    1 
ATOM   168  O  O    . PRO   A 1 21  ? 31.378  23.825  12.724  1.00 14.22 ? 25  PRO   A O    1 
ATOM   169  C  CB   . PRO   A 1 21  ? 33.179  21.526  14.348  1.00 13.09 ? 25  PRO   A CB   1 
ATOM   170  C  CG   . PRO   A 1 21  ? 34.186  20.419  14.135  1.00 13.17 ? 25  PRO   A CG   1 
ATOM   171  C  CD   . PRO   A 1 21  ? 35.277  21.096  13.314  1.00 13.39 ? 25  PRO   A CD   1 
ATOM   172  N  N    . SER   A 1 22  ? 33.397  24.588  13.417  1.00 13.99 ? 26  SER   A N    1 
ATOM   173  C  CA   . SER   A 1 22  ? 32.960  25.974  13.539  1.00 14.62 ? 26  SER   A CA   1 
ATOM   174  C  C    . SER   A 1 22  ? 32.542  26.612  12.211  1.00 13.79 ? 26  SER   A C    1 
ATOM   175  O  O    . SER   A 1 22  ? 31.958  27.694  12.226  1.00 14.46 ? 26  SER   A O    1 
ATOM   176  C  CB   . SER   A 1 22  ? 34.024  26.811  14.217  1.00 16.12 ? 26  SER   A CB   1 
ATOM   177  O  OG   . SER   A 1 22  ? 34.189  26.376  15.558  1.00 20.55 ? 26  SER   A OG   1 
ATOM   178  N  N    . SER   A 1 23  ? 32.847  25.967  11.082  1.00 13.00 ? 27  SER   A N    1 
ATOM   179  C  CA   . SER   A 1 23  ? 32.454  26.435  9.756   1.00 12.84 ? 27  SER   A CA   1 
ATOM   180  C  C    . SER   A 1 23  ? 31.130  25.832  9.273   1.00 12.34 ? 27  SER   A C    1 
ATOM   181  O  O    . SER   A 1 23  ? 30.739  26.101  8.139   1.00 13.35 ? 27  SER   A O    1 
ATOM   182  C  CB   . SER   A 1 23  ? 33.530  26.115  8.752   1.00 12.96 ? 27  SER   A CB   1 
ATOM   183  O  OG   . SER   A 1 23  ? 33.607  24.718  8.479   1.00 12.93 ? 27  SER   A OG   1 
ATOM   184  N  N    . ARG   A 1 24  ? 30.458  25.011  10.090  1.00 12.23 ? 28  ARG   A N    1 
ATOM   185  C  CA   . ARG   A 1 24  ? 29.241  24.307  9.690   1.00 12.33 ? 28  ARG   A CA   1 
ATOM   186  C  C    . ARG   A 1 24  ? 29.522  23.484  8.433   1.00 11.59 ? 28  ARG   A C    1 
ATOM   187  O  O    . ARG   A 1 24  ? 28.951  23.693  7.358   1.00 12.30 ? 28  ARG   A O    1 
ATOM   188  C  CB   . ARG   A 1 24  ? 28.061  25.268  9.505   1.00 13.15 ? 28  ARG   A CB   1 
ATOM   189  C  CG   . ARG   A 1 24  ? 26.745  24.524  9.322   1.00 14.99 ? 28  ARG   A CG   1 
ATOM   190  C  CD   . ARG   A 1 24  ? 25.781  25.276  8.419   1.00 16.89 ? 28  ARG   A CD   1 
ATOM   191  N  NE   . ARG   A 1 24  ? 24.679  24.455  7.909   1.00 19.04 ? 28  ARG   A NE   1 
ATOM   192  C  CZ   . ARG   A 1 24  ? 24.752  23.566  6.912   1.00 19.88 ? 28  ARG   A CZ   1 
ATOM   193  N  NH1  . ARG   A 1 24  ? 25.912  23.270  6.326   1.00 20.15 ? 28  ARG   A NH1  1 
ATOM   194  N  NH2  . ARG   A 1 24  ? 23.650  22.951  6.519   1.00 21.25 ? 28  ARG   A NH2  1 
ATOM   195  N  N    . PRO   A 1 25  ? 30.462  22.529  8.522   1.00 11.27 ? 29  PRO   A N    1 
ATOM   196  C  CA   . PRO   A 1 25  ? 30.987  21.855  7.333   1.00 11.26 ? 29  PRO   A CA   1 
ATOM   197  C  C    . PRO   A 1 25  ? 30.074  20.741  6.846   1.00 11.31 ? 29  PRO   A C    1 
ATOM   198  O  O    . PRO   A 1 25  ? 29.162  20.314  7.553   1.00 11.19 ? 29  PRO   A O    1 
ATOM   199  C  CB   . PRO   A 1 25  ? 32.307  21.297  7.843   1.00 11.46 ? 29  PRO   A CB   1 
ATOM   200  C  CG   . PRO   A 1 25  ? 31.983  20.926  9.266   1.00 11.38 ? 29  PRO   A CG   1 
ATOM   201  C  CD   . PRO   A 1 25  ? 31.105  22.073  9.760   1.00 11.23 ? 29  PRO   A CD   1 
ATOM   202  N  N    . GLU   A 1 26  ? 30.369  20.279  5.631   1.00 11.11 ? 30  GLU   A N    1 
ATOM   203  C  CA   . GLU   A 1 26  ? 29.681  19.155  5.025   1.00 11.35 ? 30  GLU   A CA   1 
ATOM   204  C  C    . GLU   A 1 26  ? 30.684  18.090  4.598   1.00 11.28 ? 30  GLU   A C    1 
ATOM   205  O  O    . GLU   A 1 26  ? 31.837  18.381  4.319   1.00 11.08 ? 30  GLU   A O    1 
ATOM   206  C  CB   . GLU   A 1 26  ? 28.846  19.658  3.855   1.00 12.89 ? 30  GLU   A CB   1 
ATOM   207  C  CG   . GLU   A 1 26  ? 27.774  20.622  4.338   1.00 14.18 ? 30  GLU   A CG   1 
ATOM   208  C  CD   . GLU   A 1 26  ? 26.674  20.961  3.357   1.00 16.47 ? 30  GLU   A CD   1 
ATOM   209  O  OE1  . GLU   A 1 26  ? 26.558  20.307  2.296   1.00 18.04 ? 30  GLU   A OE1  1 
ATOM   210  O  OE2  . GLU   A 1 26  ? 25.901  21.878  3.723   1.00 19.08 ? 30  GLU   A OE2  1 
ATOM   211  N  N    . VAL   A 1 27  ? 30.211  16.844  4.571   1.00 10.94 ? 31  VAL   A N    1 
ATOM   212  C  CA   . VAL   A 1 27  ? 31.036  15.701  4.210   1.00 10.78 ? 31  VAL   A CA   1 
ATOM   213  C  C    . VAL   A 1 27  ? 31.497  15.775  2.756   1.00 10.55 ? 31  VAL   A C    1 
ATOM   214  O  O    . VAL   A 1 27  ? 30.692  16.020  1.863   1.00 11.45 ? 31  VAL   A O    1 
ATOM   215  C  CB   . VAL   A 1 27  ? 30.271  14.395  4.487   1.00 11.25 ? 31  VAL   A CB   1 
ATOM   216  C  CG1  . VAL   A 1 27  ? 31.030  13.172  3.991   1.00 11.72 ? 31  VAL   A CG1  1 
ATOM   217  C  CG2  . VAL   A 1 27  ? 29.958  14.237  5.969   1.00 11.61 ? 31  VAL   A CG2  1 
ATOM   218  N  N    . THR   A 1 28  ? 32.787  15.470  2.538   1.00 10.30 ? 32  THR   A N    1 
ATOM   219  C  CA   . THR   A 1 28  ? 33.361  15.285  1.206   1.00 10.56 ? 32  THR   A CA   1 
ATOM   220  C  C    . THR   A 1 28  ? 33.807  13.847  0.968   1.00 10.48 ? 32  THR   A C    1 
ATOM   221  O  O    . THR   A 1 28  ? 33.932  13.447  -0.176  1.00 10.83 ? 32  THR   A O    1 
ATOM   222  C  CB   . THR   A 1 28  ? 34.543  16.236  1.004   1.00 11.19 ? 32  THR   A CB   1 
ATOM   223  O  OG1  . THR   A 1 28  ? 35.467  15.960  2.051   1.00 11.64 ? 32  THR   A OG1  1 
ATOM   224  C  CG2  . THR   A 1 28  ? 34.136  17.690  1.085   1.00 11.91 ? 32  THR   A CG2  1 
ATOM   225  N  N    . GLU   A 1 29  ? 34.071  13.080  2.021   1.00 10.42 ? 33  GLU   A N    1 
ATOM   226  C  CA   . GLU   A 1 29  ? 34.510  11.703  1.848   1.00 11.01 ? 33  GLU   A CA   1 
ATOM   227  C  C    . GLU   A 1 29  ? 34.210  10.945  3.131   1.00 10.70 ? 33  GLU   A C    1 
ATOM   228  O  O    . GLU   A 1 29  ? 34.286  11.510  4.219   1.00 10.71 ? 33  GLU   A O    1 
ATOM   229  C  CB   . GLU   A 1 29  ? 36.010  11.607  1.538   1.00 12.48 ? 33  GLU   A CB   1 
ATOM   230  C  CG   . GLU   A 1 29  ? 36.472  10.250  1.007   1.00 14.08 ? 33  GLU   A CG   1 
ATOM   231  C  CD   . GLU   A 1 29  ? 37.961  10.158  0.687   1.00 16.04 ? 33  GLU   A CD   1 
ATOM   232  O  OE1  . GLU   A 1 29  ? 38.781  10.779  1.407   1.00 17.79 ? 33  GLU   A OE1  1 
ATOM   233  O  OE2  . GLU   A 1 29  ? 38.318  9.424   -0.263  1.00 18.20 ? 33  GLU   A OE2  1 
ATOM   234  N  N    . LEU   A 1 30  ? 33.894  9.660   2.998   1.00 11.14 ? 34  LEU   A N    1 
ATOM   235  C  CA   . LEU   A 1 30  ? 33.722  8.823   4.170   1.00 11.54 ? 34  LEU   A CA   1 
ATOM   236  C  C    . LEU   A 1 30  ? 34.317  7.452   3.888   1.00 11.22 ? 34  LEU   A C    1 
ATOM   237  O  O    . LEU   A 1 30  ? 34.314  6.983   2.750   1.00 12.62 ? 34  LEU   A O    1 
ATOM   238  C  CB   . LEU   A 1 30  ? 32.256  8.755   4.580   1.00 13.20 ? 34  LEU   A CB   1 
ATOM   239  C  CG   . LEU   A 1 30  ? 31.287  8.130   3.580   1.00 14.69 ? 34  LEU   A CG   1 
ATOM   240  C  CD1  . LEU   A 1 30  ? 31.192  6.619   3.710   1.00 15.57 ? 34  LEU   A CD1  1 
ATOM   241  C  CD2  . LEU   A 1 30  ? 29.925  8.780   3.751   1.00 16.50 ? 34  LEU   A CD2  1 
ATOM   242  N  N    . CYS   A 1 31  ? 34.838  6.832   4.944   1.00 10.84 ? 35  CYS   A N    1 
ATOM   243  C  CA   . CYS   A 1 31  ? 35.317  5.465   4.872   1.00 11.06 ? 35  CYS   A CA   1 
ATOM   244  C  C    . CYS   A 1 31  ? 34.895  4.704   6.123   1.00 10.89 ? 35  CYS   A C    1 
ATOM   245  O  O    . CYS   A 1 31  ? 35.088  5.185   7.243   1.00 10.93 ? 35  CYS   A O    1 
ATOM   246  C  CB   . CYS   A 1 31  ? 36.832  5.395   4.704   1.00 12.07 ? 35  CYS   A CB   1 
ATOM   247  S  SG   . CYS   A 1 31  ? 37.464  3.698   4.602   1.00 16.39 ? 35  CYS   A SG   1 
ATOM   248  N  N    . LEU   A 1 32  ? 34.290  3.534   5.895   1.00 11.01 ? 36  LEU   A N    1 
ATOM   249  C  CA   . LEU   A 1 32  ? 33.989  2.556   6.927   1.00 11.16 ? 36  LEU   A CA   1 
ATOM   250  C  C    . LEU   A 1 32  ? 34.797  1.296   6.645   1.00 11.13 ? 36  LEU   A C    1 
ATOM   251  O  O    . LEU   A 1 32  ? 34.780  0.794   5.517   1.00 11.53 ? 36  LEU   A O    1 
ATOM   252  C  CB   . LEU   A 1 32  ? 32.502  2.199   6.926   1.00 12.07 ? 36  LEU   A CB   1 
ATOM   253  C  CG   . LEU   A 1 32  ? 31.519  3.259   7.438   1.00 13.87 ? 36  LEU   A CG   1 
ATOM   254  C  CD1  . LEU   A 1 32  ? 31.458  4.505   6.624   1.00 15.58 ? 36  LEU   A CD1  1 
ATOM   255  C  CD2  . LEU   A 1 32  ? 30.134  2.637   7.521   1.00 15.64 ? 36  LEU   A CD2  1 
ATOM   256  N  N    A LEU   A 1 33  ? 35.468  0.790   7.683   0.50 11.04 ? 37  LEU   A N    1 
ATOM   257  N  N    B LEU   A 1 33  ? 35.468  0.766   7.676   0.50 10.94 ? 37  LEU   A N    1 
ATOM   258  C  CA   A LEU   A 1 33  ? 36.163  -0.480  7.620   0.50 11.55 ? 37  LEU   A CA   1 
ATOM   259  C  CA   B LEU   A 1 33  ? 36.175  -0.502  7.579   0.50 11.41 ? 37  LEU   A CA   1 
ATOM   260  C  C    A LEU   A 1 33  ? 35.659  -1.333  8.775   0.50 11.06 ? 37  LEU   A C    1 
ATOM   261  C  C    B LEU   A 1 33  ? 35.727  -1.373  8.749   0.50 11.01 ? 37  LEU   A C    1 
ATOM   262  O  O    A LEU   A 1 33  ? 35.927  -1.023  9.937   0.50 11.05 ? 37  LEU   A O    1 
ATOM   263  O  O    B LEU   A 1 33  ? 36.113  -1.124  9.893   0.50 11.14 ? 37  LEU   A O    1 
ATOM   264  C  CB   A LEU   A 1 33  ? 37.672  -0.275  7.708   0.50 12.60 ? 37  LEU   A CB   1 
ATOM   265  C  CB   B LEU   A 1 33  ? 37.690  -0.286  7.573   0.50 12.24 ? 37  LEU   A CB   1 
ATOM   266  C  CG   A LEU   A 1 33  ? 38.512  -1.544  7.569   0.50 13.83 ? 37  LEU   A CG   1 
ATOM   267  C  CG   B LEU   A 1 33  ? 38.552  -1.474  7.129   0.50 13.22 ? 37  LEU   A CG   1 
ATOM   268  C  CD1  A LEU   A 1 33  ? 38.418  -2.096  6.156   0.50 14.15 ? 37  LEU   A CD1  1 
ATOM   269  C  CD1  B LEU   A 1 33  ? 39.933  -1.012  6.708   0.50 13.28 ? 37  LEU   A CD1  1 
ATOM   270  C  CD2  A LEU   A 1 33  ? 39.946  -1.268  7.959   0.50 14.70 ? 37  LEU   A CD2  1 
ATOM   271  C  CD2  B LEU   A 1 33  ? 38.679  -2.524  8.212   0.50 13.88 ? 37  LEU   A CD2  1 
ATOM   272  N  N    . ALA   A 1 34  ? 34.898  -2.379  8.441   1.00 10.95 ? 38  ALA   A N    1 
ATOM   273  C  CA   . ALA   A 1 34  ? 34.266  -3.227  9.438   1.00 11.31 ? 38  ALA   A CA   1 
ATOM   274  C  C    . ALA   A 1 34  ? 35.135  -4.454  9.689   1.00 11.89 ? 38  ALA   A C    1 
ATOM   275  O  O    . ALA   A 1 34  ? 35.438  -5.203  8.758   1.00 12.49 ? 38  ALA   A O    1 
ATOM   276  C  CB   . ALA   A 1 34  ? 32.885  -3.630  8.981   1.00 12.44 ? 38  ALA   A CB   1 
ATOM   277  N  N    . VAL   A 1 35  ? 35.500  -4.633  10.963  1.00 12.34 ? 39  VAL   A N    1 
ATOM   278  C  CA   . VAL   A 1 35  ? 36.362  -5.699  11.447  1.00 13.38 ? 39  VAL   A CA   1 
ATOM   279  C  C    . VAL   A 1 35  ? 35.612  -6.468  12.530  1.00 12.81 ? 39  VAL   A C    1 
ATOM   280  O  O    . VAL   A 1 35  ? 35.164  -5.887  13.514  1.00 13.06 ? 39  VAL   A O    1 
ATOM   281  C  CB   . VAL   A 1 35  ? 37.655  -5.069  12.017  1.00 15.19 ? 39  VAL   A CB   1 
ATOM   282  C  CG1  . VAL   A 1 35  ? 38.597  -6.112  12.579  1.00 17.25 ? 39  VAL   A CG1  1 
ATOM   283  C  CG2  . VAL   A 1 35  ? 38.385  -4.205  11.000  1.00 16.28 ? 39  VAL   A CG2  1 
ATOM   284  N  N    . HIS   A 1 36  ? 35.472  -7.782  12.366  1.00 12.03 ? 40  HIS   A N    1 
ATOM   285  C  CA   . HIS   A 1 36  ? 34.884  -8.603  13.415  1.00 12.50 ? 40  HIS   A CA   1 
ATOM   286  C  C    . HIS   A 1 36  ? 35.796  -8.596  14.636  1.00 12.51 ? 40  HIS   A C    1 
ATOM   287  O  O    . HIS   A 1 36  ? 37.014  -8.546  14.510  1.00 12.46 ? 40  HIS   A O    1 
ATOM   288  C  CB   . HIS   A 1 36  ? 34.683  -10.037 12.919  1.00 13.31 ? 40  HIS   A CB   1 
ATOM   289  C  CG   . HIS   A 1 36  ? 33.838  -10.852 13.820  1.00 14.47 ? 40  HIS   A CG   1 
ATOM   290  N  ND1  . HIS   A 1 36  ? 34.333  -11.519 14.919  1.00 16.06 ? 40  HIS   A ND1  1 
ATOM   291  C  CD2  . HIS   A 1 36  ? 32.522  -11.064 13.812  1.00 16.41 ? 40  HIS   A CD2  1 
ATOM   292  C  CE1  . HIS   A 1 36  ? 33.332  -12.150 15.524  1.00 17.12 ? 40  HIS   A CE1  1 
ATOM   293  N  NE2  . HIS   A 1 36  ? 32.221  -11.882 14.870  1.00 17.08 ? 40  HIS   A NE2  1 
ATOM   294  N  N    . ARG   A 1 37  ? 35.201  -8.675  15.826  1.00 12.39 ? 41  ARG   A N    1 
ATOM   295  C  CA   . ARG   A 1 37  ? 35.978  -8.625  17.056  1.00 12.93 ? 41  ARG   A CA   1 
ATOM   296  C  C    . ARG   A 1 37  ? 37.068  -9.695  17.108  1.00 13.82 ? 41  ARG   A C    1 
ATOM   297  O  O    . ARG   A 1 37  ? 38.093  -9.470  17.741  1.00 14.84 ? 41  ARG   A O    1 
ATOM   298  C  CB   . ARG   A 1 37  ? 35.087  -8.720  18.293  1.00 13.41 ? 41  ARG   A CB   1 
ATOM   299  C  CG   . ARG   A 1 37  ? 34.336  -10.034 18.453  1.00 13.84 ? 41  ARG   A CG   1 
ATOM   300  C  CD   . ARG   A 1 37  ? 33.603  -10.110 19.774  1.00 14.07 ? 41  ARG   A CD   1 
ATOM   301  N  NE   . ARG   A 1 37  ? 34.498  -10.186 20.933  1.00 14.30 ? 41  ARG   A NE   1 
ATOM   302  C  CZ   . ARG   A 1 37  ? 34.643  -9.263  21.886  1.00 14.22 ? 41  ARG   A CZ   1 
ATOM   303  N  NH1  . ARG   A 1 37  ? 34.069  -8.063  21.785  1.00 14.20 ? 41  ARG   A NH1  1 
ATOM   304  N  NH2  . ARG   A 1 37  ? 35.396  -9.539  22.939  1.00 15.32 ? 41  ARG   A NH2  1 
ATOM   305  N  N    . CYS   A 1 38  ? 36.858  -10.849 16.455  1.00 14.06 ? 42  CYS   A N    1 
ATOM   306  C  CA   . CYS   A 1 38  ? 37.824  -11.928 16.521  1.00 16.22 ? 42  CYS   A CA   1 
ATOM   307  C  C    . CYS   A 1 38  ? 39.193  -11.515 15.979  1.00 16.78 ? 42  CYS   A C    1 
ATOM   308  O  O    . CYS   A 1 38  ? 40.204  -12.067 16.404  1.00 18.24 ? 42  CYS   A O    1 
ATOM   309  C  CB   . CYS   A 1 38  ? 37.290  -13.191 15.858  1.00 17.01 ? 42  CYS   A CB   1 
ATOM   310  S  SG   . CYS   A 1 38  ? 37.171  -13.125 14.058  1.00 20.90 ? 42  CYS   A SG   1 
ATOM   311  N  N    . ALA   A 1 39  ? 39.236  -10.532 15.068  1.00 16.64 ? 43  ALA   A N    1 
ATOM   312  C  CA   . ALA   A 1 39  ? 40.498  -10.088 14.499  1.00 17.89 ? 43  ALA   A CA   1 
ATOM   313  C  C    . ALA   A 1 39  ? 41.376  -9.414  15.550  1.00 18.52 ? 43  ALA   A C    1 
ATOM   314  O  O    . ALA   A 1 39  ? 42.596  -9.408  15.391  1.00 20.38 ? 43  ALA   A O    1 
ATOM   315  C  CB   . ALA   A 1 39  ? 40.258  -9.164  13.333  1.00 18.42 ? 43  ALA   A CB   1 
ATOM   316  N  N    . LEU   A 1 40  ? 40.749  -8.860  16.604  1.00 18.37 ? 44  LEU   A N    1 
ATOM   317  C  CA   . LEU   A 1 40  ? 41.454  -8.186  17.686  1.00 19.55 ? 44  LEU   A CA   1 
ATOM   318  C  C    . LEU   A 1 40  ? 41.546  -9.093  18.912  1.00 19.11 ? 44  LEU   A C    1 
ATOM   319  O  O    . LEU   A 1 40  ? 42.527  -9.030  19.640  1.00 20.12 ? 44  LEU   A O    1 
ATOM   320  C  CB   . LEU   A 1 40  ? 40.760  -6.875  18.053  1.00 21.41 ? 44  LEU   A CB   1 
ATOM   321  C  CG   . LEU   A 1 40  ? 40.604  -5.859  16.918  1.00 24.51 ? 44  LEU   A CG   1 
ATOM   322  C  CD1  . LEU   A 1 40  ? 39.743  -4.698  17.373  1.00 27.21 ? 44  LEU   A CD1  1 
ATOM   323  C  CD2  . LEU   A 1 40  ? 41.956  -5.396  16.468  1.00 26.62 ? 44  LEU   A CD2  1 
ATOM   324  N  N    . GLU   A 1 41  ? 40.505  -9.893  19.158  1.00 18.37 ? 45  GLU   A N    1 
ATOM   325  C  CA   . GLU   A 1 41  ? 40.418  -10.733 20.342  1.00 19.46 ? 45  GLU   A CA   1 
ATOM   326  C  C    . GLU   A 1 41  ? 41.361  -11.928 20.227  1.00 20.62 ? 45  GLU   A C    1 
ATOM   327  O  O    . GLU   A 1 41  ? 41.925  -12.373 21.230  1.00 22.35 ? 45  GLU   A O    1 
ATOM   328  C  CB   . GLU   A 1 41  ? 38.972  -11.206 20.476  1.00 19.55 ? 45  GLU   A CB   1 
ATOM   329  C  CG   . GLU   A 1 41  ? 38.648  -11.824 21.827  1.00 20.21 ? 45  GLU   A CG   1 
ATOM   330  C  CD   . GLU   A 1 41  ? 37.175  -12.148 21.953  1.00 20.76 ? 45  GLU   A CD   1 
ATOM   331  O  OE1  . GLU   A 1 41  ? 36.712  -12.224 23.099  1.00 23.17 ? 45  GLU   A OE1  1 
ATOM   332  O  OE2  . GLU   A 1 41  ? 36.507  -12.349 20.918  1.00 21.28 ? 45  GLU   A OE2  1 
ATOM   333  N  N    . SER   A 1 42  ? 41.502  -12.439 18.996  1.00 22.55 ? 46  SER   A N    1 
ATOM   334  C  CA   . SER   A 1 42  ? 42.220  -13.666 18.689  1.00 24.99 ? 46  SER   A CA   1 
ATOM   335  C  C    . SER   A 1 42  ? 43.067  -13.435 17.441  1.00 27.56 ? 46  SER   A C    1 
ATOM   336  O  O    . SER   A 1 42  ? 42.833  -14.053 16.407  1.00 28.07 ? 46  SER   A O    1 
ATOM   337  C  CB   . SER   A 1 42  ? 41.260  -14.816 18.476  1.00 26.16 ? 46  SER   A CB   1 
ATOM   338  O  OG   . SER   A 1 42  ? 40.406  -15.008 19.597  1.00 26.98 ? 46  SER   A OG   1 
ATOM   339  N  N    . PRO   A 1 43  ? 44.045  -12.505 17.478  1.00 31.33 ? 47  PRO   A N    1 
ATOM   340  C  CA   . PRO   A 1 43  ? 44.807  -12.167 16.274  1.00 33.35 ? 47  PRO   A CA   1 
ATOM   341  C  C    . PRO   A 1 43  ? 45.631  -13.374 15.829  1.00 37.15 ? 47  PRO   A C    1 
ATOM   342  O  O    . PRO   A 1 43  ? 46.131  -14.114 16.677  1.00 36.81 ? 47  PRO   A O    1 
ATOM   343  C  CB   . PRO   A 1 43  ? 45.659  -10.963 16.694  1.00 33.72 ? 47  PRO   A CB   1 
ATOM   344  C  CG   . PRO   A 1 43  ? 45.748  -11.057 18.195  1.00 34.27 ? 47  PRO   A CG   1 
ATOM   345  C  CD   . PRO   A 1 43  ? 44.474  -11.750 18.665  1.00 32.87 ? 47  PRO   A CD   1 
ATOM   346  N  N    . PRO   A 1 44  ? 45.732  -13.663 14.506  1.00 42.47 ? 48  PRO   A N    1 
ATOM   347  C  CA   . PRO   A 1 44  ? 46.553  -14.778 14.020  1.00 46.87 ? 48  PRO   A CA   1 
ATOM   348  C  C    . PRO   A 1 44  ? 48.041  -14.606 14.323  1.00 50.16 ? 48  PRO   A C    1 
ATOM   349  O  O    . PRO   A 1 44  ? 48.444  -13.467 14.648  1.00 51.64 ? 48  PRO   A O    1 
ATOM   350  C  CB   . PRO   A 1 44  ? 46.277  -14.818 12.499  1.00 48.38 ? 48  PRO   A CB   1 
ATOM   351  C  CG   . PRO   A 1 44  ? 44.990  -14.042 12.322  1.00 47.66 ? 48  PRO   A CG   1 
ATOM   352  C  CD   . PRO   A 1 44  ? 45.015  -12.981 13.414  1.00 46.08 ? 48  PRO   A CD   1 
ATOM   353  N  N    . PRO   A 1 50  ? 56.905  -11.406 11.606  1.00 72.66 ? 54  PRO   A N    1 
ATOM   354  C  CA   . PRO   A 1 50  ? 57.075  -10.503 12.736  1.00 68.86 ? 54  PRO   A CA   1 
ATOM   355  C  C    . PRO   A 1 50  ? 57.329  -9.056  12.314  1.00 63.82 ? 54  PRO   A C    1 
ATOM   356  O  O    . PRO   A 1 50  ? 58.335  -8.462  12.689  1.00 63.66 ? 54  PRO   A O    1 
ATOM   357  C  CB   . PRO   A 1 50  ? 58.286  -11.159 13.420  1.00 69.98 ? 54  PRO   A CB   1 
ATOM   358  C  CG   . PRO   A 1 50  ? 59.156  -11.603 12.263  1.00 72.20 ? 54  PRO   A CG   1 
ATOM   359  C  CD   . PRO   A 1 50  ? 58.207  -11.791 11.086  1.00 71.81 ? 54  PRO   A CD   1 
ATOM   360  N  N    . PRO   A 1 51  ? 56.413  -8.431  11.538  1.00 59.65 ? 55  PRO   A N    1 
ATOM   361  C  CA   . PRO   A 1 51  ? 56.672  -7.111  10.957  1.00 57.00 ? 55  PRO   A CA   1 
ATOM   362  C  C    . PRO   A 1 51  ? 56.590  -5.963  11.961  1.00 53.38 ? 55  PRO   A C    1 
ATOM   363  O  O    . PRO   A 1 51  ? 56.083  -6.132  13.068  1.00 53.58 ? 55  PRO   A O    1 
ATOM   364  C  CB   . PRO   A 1 51  ? 55.581  -7.018  9.874   1.00 58.55 ? 55  PRO   A CB   1 
ATOM   365  C  CG   . PRO   A 1 51  ? 54.422  -7.802  10.452  1.00 58.37 ? 55  PRO   A CG   1 
ATOM   366  C  CD   . PRO   A 1 51  ? 55.077  -8.953  11.199  1.00 59.03 ? 55  PRO   A CD   1 
ATOM   367  N  N    . THR   A 1 52  ? 57.097  -4.793  11.552  1.00 49.34 ? 56  THR   A N    1 
ATOM   368  C  CA   . THR   A 1 52  ? 57.029  -3.592  12.368  1.00 48.14 ? 56  THR   A CA   1 
ATOM   369  C  C    . THR   A 1 52  ? 55.563  -3.256  12.626  1.00 42.82 ? 56  THR   A C    1 
ATOM   370  O  O    . THR   A 1 52  ? 55.142  -3.152  13.776  1.00 44.49 ? 56  THR   A O    1 
ATOM   371  C  CB   . THR   A 1 52  ? 57.755  -2.439  11.673  1.00 51.02 ? 56  THR   A CB   1 
ATOM   372  O  OG1  . THR   A 1 52  ? 59.088  -2.883  11.429  1.00 54.18 ? 56  THR   A OG1  1 
ATOM   373  C  CG2  . THR   A 1 52  ? 57.784  -1.179  12.519  1.00 51.54 ? 56  THR   A CG2  1 
ATOM   374  N  N    . VAL   A 1 53  ? 54.795  -3.111  11.539  1.00 36.95 ? 57  VAL   A N    1 
ATOM   375  C  CA   . VAL   A 1 53  ? 53.390  -2.756  11.620  1.00 33.96 ? 57  VAL   A CA   1 
ATOM   376  C  C    . VAL   A 1 53  ? 52.566  -4.016  11.377  1.00 32.02 ? 57  VAL   A C    1 
ATOM   377  O  O    . VAL   A 1 53  ? 52.816  -4.727  10.413  1.00 32.51 ? 57  VAL   A O    1 
ATOM   378  C  CB   . VAL   A 1 53  ? 53.022  -1.654  10.609  1.00 33.89 ? 57  VAL   A CB   1 
ATOM   379  C  CG1  . VAL   A 1 53  ? 51.588  -1.178  10.797  1.00 33.43 ? 57  VAL   A CG1  1 
ATOM   380  C  CG2  . VAL   A 1 53  ? 53.986  -0.476  10.679  1.00 35.11 ? 57  VAL   A CG2  1 
ATOM   381  N  N    . PRO   A 1 54  ? 51.565  -4.327  12.235  1.00 31.26 ? 58  PRO   A N    1 
ATOM   382  C  CA   . PRO   A 1 54  ? 50.680  -5.466  12.000  1.00 30.34 ? 58  PRO   A CA   1 
ATOM   383  C  C    . PRO   A 1 54  ? 50.011  -5.366  10.634  1.00 29.88 ? 58  PRO   A C    1 
ATOM   384  O  O    . PRO   A 1 54  ? 49.608  -4.279  10.227  1.00 28.13 ? 58  PRO   A O    1 
ATOM   385  C  CB   . PRO   A 1 54  ? 49.643  -5.397  13.134  1.00 32.78 ? 58  PRO   A CB   1 
ATOM   386  C  CG   . PRO   A 1 54  ? 50.268  -4.523  14.194  1.00 33.53 ? 58  PRO   A CG   1 
ATOM   387  C  CD   . PRO   A 1 54  ? 51.258  -3.616  13.485  1.00 32.33 ? 58  PRO   A CD   1 
ATOM   388  N  N    . PRO   A 1 55  ? 49.853  -6.483  9.889   1.00 30.57 ? 59  PRO   A N    1 
ATOM   389  C  CA   . PRO   A 1 55  ? 49.063  -6.461  8.662   1.00 29.59 ? 59  PRO   A CA   1 
ATOM   390  C  C    . PRO   A 1 55  ? 47.598  -6.278  9.040   1.00 26.18 ? 59  PRO   A C    1 
ATOM   391  O  O    . PRO   A 1 55  ? 47.173  -6.708  10.109  1.00 24.85 ? 59  PRO   A O    1 
ATOM   392  C  CB   . PRO   A 1 55  ? 49.340  -7.830  8.029   1.00 31.26 ? 59  PRO   A CB   1 
ATOM   393  C  CG   . PRO   A 1 55  ? 49.646  -8.717  9.217   1.00 32.34 ? 59  PRO   A CG   1 
ATOM   394  C  CD   . PRO   A 1 55  ? 50.401  -7.818  10.187  1.00 32.26 ? 59  PRO   A CD   1 
ATOM   395  N  N    . PRO   A 1 56  ? 46.770  -5.663  8.175   1.00 24.28 ? 60  PRO   A N    1 
ATOM   396  C  CA   . PRO   A 1 56  ? 45.335  -5.632  8.425   1.00 22.19 ? 60  PRO   A CA   1 
ATOM   397  C  C    . PRO   A 1 56  ? 44.773  -7.051  8.375   1.00 18.73 ? 60  PRO   A C    1 
ATOM   398  O  O    . PRO   A 1 56  ? 45.358  -7.950  7.759   1.00 18.59 ? 60  PRO   A O    1 
ATOM   399  C  CB   . PRO   A 1 56  ? 44.768  -4.743  7.320   1.00 24.50 ? 60  PRO   A CB   1 
ATOM   400  C  CG   . PRO   A 1 56  ? 45.812  -4.804  6.220   1.00 26.95 ? 60  PRO   A CG   1 
ATOM   401  C  CD   . PRO   A 1 56  ? 47.146  -5.039  6.897   1.00 26.41 ? 60  PRO   A CD   1 
ATOM   402  N  N    . PRO   A 1 57  ? 43.611  -7.304  9.012   1.00 16.86 ? 61  PRO   A N    1 
ATOM   403  C  CA   . PRO   A 1 57  ? 42.959  -8.606  8.900   1.00 16.51 ? 61  PRO   A CA   1 
ATOM   404  C  C    . PRO   A 1 57  ? 42.608  -8.910  7.447   1.00 16.20 ? 61  PRO   A C    1 
ATOM   405  O  O    . PRO   A 1 57  ? 42.255  -8.018  6.680   1.00 16.63 ? 61  PRO   A O    1 
ATOM   406  C  CB   . PRO   A 1 57  ? 41.700  -8.483  9.772   1.00 17.44 ? 61  PRO   A CB   1 
ATOM   407  C  CG   . PRO   A 1 57  ? 41.937  -7.249  10.604  1.00 17.84 ? 61  PRO   A CG   1 
ATOM   408  C  CD   . PRO   A 1 57  ? 42.805  -6.341  9.773   1.00 17.37 ? 61  PRO   A CD   1 
ATOM   409  N  N    . ARG   A 1 58  ? 42.671  -10.189 7.081   1.00 15.49 ? 62  ARG   A N    1 
ATOM   410  C  CA   . ARG   A 1 58  ? 42.289  -10.622 5.747   1.00 15.64 ? 62  ARG   A CA   1 
ATOM   411  C  C    . ARG   A 1 58  ? 40.806  -10.359 5.494   1.00 14.75 ? 62  ARG   A C    1 
ATOM   412  O  O    . ARG   A 1 58  ? 40.423  -9.920  4.412   1.00 14.70 ? 62  ARG   A O    1 
ATOM   413  C  CB   . ARG   A 1 58  ? 42.552  -12.118 5.564   1.00 16.22 ? 62  ARG   A CB   1 
ATOM   414  C  CG   . ARG   A 1 58  ? 41.993  -12.699 4.273   1.00 16.49 ? 62  ARG   A CG   1 
ATOM   415  C  CD   . ARG   A 1 58  ? 42.636  -12.077 3.056   1.00 16.87 ? 62  ARG   A CD   1 
ATOM   416  N  NE   . ARG   A 1 58  ? 42.039  -12.581 1.814   1.00 16.12 ? 62  ARG   A NE   1 
ATOM   417  C  CZ   . ARG   A 1 58  ? 41.058  -11.980 1.142   1.00 14.77 ? 62  ARG   A CZ   1 
ATOM   418  N  NH1  . ARG   A 1 58  ? 40.404  -10.965 1.671   1.00 14.61 ? 62  ARG   A NH1  1 
ATOM   419  N  NH2  . ARG   A 1 58  ? 40.724  -12.388 -0.067  1.00 14.42 ? 62  ARG   A NH2  1 
ATOM   420  N  N    . VAL   A 1 59  ? 39.969  -10.684 6.480   1.00 14.00 ? 63  VAL   A N    1 
ATOM   421  C  CA   . VAL   A 1 59  ? 38.529  -10.569 6.316   1.00 14.03 ? 63  VAL   A CA   1 
ATOM   422  C  C    . VAL   A 1 59  ? 38.081  -9.226  6.880   1.00 14.13 ? 63  VAL   A C    1 
ATOM   423  O  O    . VAL   A 1 59  ? 38.024  -9.033  8.092   1.00 16.17 ? 63  VAL   A O    1 
ATOM   424  C  CB   . VAL   A 1 59  ? 37.780  -11.735 6.980   1.00 14.82 ? 63  VAL   A CB   1 
ATOM   425  C  CG1  . VAL   A 1 59  ? 36.272  -11.587 6.799   1.00 15.05 ? 63  VAL   A CG1  1 
ATOM   426  C  CG2  . VAL   A 1 59  ? 38.261  -13.078 6.458   1.00 15.89 ? 63  VAL   A CG2  1 
ATOM   427  N  N    . VAL   A 1 60  ? 37.794  -8.293  5.974   1.00 13.78 ? 64  VAL   A N    1 
ATOM   428  C  CA   . VAL   A 1 60  ? 37.276  -6.986  6.333   1.00 14.26 ? 64  VAL   A CA   1 
ATOM   429  C  C    . VAL   A 1 60  ? 36.263  -6.599  5.266   1.00 13.52 ? 64  VAL   A C    1 
ATOM   430  O  O    . VAL   A 1 60  ? 36.309  -7.118  4.150   1.00 15.09 ? 64  VAL   A O    1 
ATOM   431  C  CB   . VAL   A 1 60  ? 38.353  -5.893  6.466   1.00 16.73 ? 64  VAL   A CB   1 
ATOM   432  C  CG1  . VAL   A 1 60  ? 39.392  -6.235  7.520   1.00 18.06 ? 64  VAL   A CG1  1 
ATOM   433  C  CG2  . VAL   A 1 60  ? 39.018  -5.581  5.134   1.00 18.38 ? 64  VAL   A CG2  1 
ATOM   434  N  N    . ASP   A 1 61  ? 35.346  -5.712  5.643   1.00 12.10 ? 65  ASP   A N    1 
ATOM   435  C  CA   . ASP   A 1 61  ? 34.472  -5.041  4.699   1.00 11.53 ? 65  ASP   A CA   1 
ATOM   436  C  C    . ASP   A 1 61  ? 34.866  -3.569  4.665   1.00 11.65 ? 65  ASP   A C    1 
ATOM   437  O  O    . ASP   A 1 61  ? 35.110  -2.978  5.709   1.00 12.16 ? 65  ASP   A O    1 
ATOM   438  C  CB   . ASP   A 1 61  ? 33.012  -5.156  5.103   1.00 12.32 ? 65  ASP   A CB   1 
ATOM   439  C  CG   . ASP   A 1 61  ? 32.306  -6.473  4.837   1.00 13.68 ? 65  ASP   A CG   1 
ATOM   440  O  OD1  . ASP   A 1 61  ? 32.957  -7.440  4.332   1.00 14.59 ? 65  ASP   A OD1  1 
ATOM   441  O  OD2  . ASP   A 1 61  ? 31.082  -6.508  5.122   1.00 15.13 ? 65  ASP   A OD2  1 
ATOM   442  N  N    . LYS   A 1 62  ? 34.886  -2.976  3.470   1.00 11.22 ? 66  LYS   A N    1 
ATOM   443  C  CA   . LYS   A 1 62  ? 35.336  -1.604  3.317   1.00 11.96 ? 66  LYS   A CA   1 
ATOM   444  C  C    . LYS   A 1 62  ? 34.365  -0.863  2.401   1.00 11.77 ? 66  LYS   A C    1 
ATOM   445  O  O    . LYS   A 1 62  ? 33.952  -1.374  1.365   1.00 12.53 ? 66  LYS   A O    1 
ATOM   446  C  CB   . LYS   A 1 62  ? 36.768  -1.592  2.773   1.00 15.26 ? 66  LYS   A CB   1 
ATOM   447  C  CG   . LYS   A 1 62  ? 37.442  -0.239  2.705   1.00 18.38 ? 66  LYS   A CG   1 
ATOM   448  C  CD   . LYS   A 1 62  ? 38.786  -0.307  1.983   1.00 21.13 ? 66  LYS   A CD   1 
ATOM   449  C  CE   . LYS   A 1 62  ? 39.767  -1.266  2.562   1.00 22.69 ? 66  LYS   A CE   1 
ATOM   450  N  NZ   . LYS   A 1 62  ? 41.079  -1.121  1.919   1.00 22.57 ? 66  LYS   A NZ   1 
ATOM   451  N  N    . LEU   A 1 63  ? 34.044  0.365   2.786   1.00 11.74 ? 67  LEU   A N    1 
ATOM   452  C  CA   . LEU   A 1 63  ? 33.267  1.268   1.961   1.00 12.11 ? 67  LEU   A CA   1 
ATOM   453  C  C    . LEU   A 1 63  ? 33.964  2.620   2.009   1.00 12.24 ? 67  LEU   A C    1 
ATOM   454  O  O    . LEU   A 1 63  ? 34.161  3.159   3.097   1.00 13.89 ? 67  LEU   A O    1 
ATOM   455  C  CB   . LEU   A 1 63  ? 31.850  1.365   2.513   1.00 13.31 ? 67  LEU   A CB   1 
ATOM   456  C  CG   . LEU   A 1 63  ? 30.934  2.367   1.813   1.00 14.34 ? 67  LEU   A CG   1 
ATOM   457  C  CD1  . LEU   A 1 63  ? 30.686  1.969   0.361   1.00 14.23 ? 67  LEU   A CD1  1 
ATOM   458  C  CD2  . LEU   A 1 63  ? 29.630  2.547   2.591   1.00 16.62 ? 67  LEU   A CD2  1 
ATOM   459  N  N    . SER   A 1 64  ? 34.341  3.148   0.842   1.00 12.12 ? 68  SER   A N    1 
ATOM   460  C  CA   . SER   A 1 64  ? 34.924  4.474   0.752   1.00 12.90 ? 68  SER   A CA   1 
ATOM   461  C  C    . SER   A 1 64  ? 34.173  5.227   -0.340  1.00 12.76 ? 68  SER   A C    1 
ATOM   462  O  O    . SER   A 1 64  ? 34.101  4.745   -1.468  1.00 13.59 ? 68  SER   A O    1 
ATOM   463  C  CB   . SER   A 1 64  ? 36.412  4.390   0.482   1.00 16.07 ? 68  SER   A CB   1 
ATOM   464  O  OG   . SER   A 1 64  ? 37.024  5.668   0.507   1.00 20.45 ? 68  SER   A OG   1 
ATOM   465  N  N    . LEU   A 1 65  ? 33.599  6.382   0.010   1.00 12.30 ? 69  LEU   A N    1 
ATOM   466  C  CA   . LEU   A 1 65  ? 32.764  7.139   -0.910  1.00 12.71 ? 69  LEU   A CA   1 
ATOM   467  C  C    . LEU   A 1 65  ? 33.151  8.610   -0.851  1.00 12.03 ? 69  LEU   A C    1 
ATOM   468  O  O    . LEU   A 1 65  ? 33.318  9.155   0.240   1.00 11.95 ? 69  LEU   A O    1 
ATOM   469  C  CB   . LEU   A 1 65  ? 31.283  7.002   -0.557  1.00 14.37 ? 69  LEU   A CB   1 
ATOM   470  C  CG   . LEU   A 1 65  ? 30.674  5.608   -0.596  1.00 16.29 ? 69  LEU   A CG   1 
ATOM   471  C  CD1  . LEU   A 1 65  ? 29.290  5.686   -0.013  1.00 17.40 ? 69  LEU   A CD1  1 
ATOM   472  C  CD2  . LEU   A 1 65  ? 30.635  5.047   -1.993  1.00 17.22 ? 69  LEU   A CD2  1 
ATOM   473  N  N    . CYS   A 1 66  ? 33.228  9.246   -2.027  1.00 11.48 ? 70  CYS   A N    1 
ATOM   474  C  CA   . CYS   A 1 66  ? 33.328  10.691  -2.099  1.00 11.73 ? 70  CYS   A CA   1 
ATOM   475  C  C    . CYS   A 1 66  ? 31.931  11.275  -2.273  1.00 11.78 ? 70  CYS   A C    1 
ATOM   476  O  O    . CYS   A 1 66  ? 31.039  10.651  -2.848  1.00 12.48 ? 70  CYS   A O    1 
ATOM   477  C  CB   . CYS   A 1 66  ? 34.265  11.131  -3.214  1.00 12.81 ? 70  CYS   A CB   1 
ATOM   478  S  SG   . CYS   A 1 66  ? 35.992  10.670  -2.942  1.00 15.72 ? 70  CYS   A SG   1 
ATOM   479  N  N    . VAL   A 1 67  ? 31.761  12.484  -1.743  1.00 11.69 ? 71  VAL   A N    1 
ATOM   480  C  CA   . VAL   A 1 67  ? 30.466  13.119  -1.622  1.00 12.28 ? 71  VAL   A CA   1 
ATOM   481  C  C    . VAL   A 1 67  ? 30.611  14.559  -2.087  1.00 12.72 ? 71  VAL   A C    1 
ATOM   482  O  O    . VAL   A 1 67  ? 31.553  15.234  -1.689  1.00 13.04 ? 71  VAL   A O    1 
ATOM   483  C  CB   . VAL   A 1 67  ? 29.981  13.076  -0.161  1.00 13.04 ? 71  VAL   A CB   1 
ATOM   484  C  CG1  . VAL   A 1 67  ? 28.618  13.743  -0.024  1.00 14.22 ? 71  VAL   A CG1  1 
ATOM   485  C  CG2  . VAL   A 1 67  ? 29.963  11.658  0.397   1.00 13.07 ? 71  VAL   A CG2  1 
ATOM   486  N  N    . ALA   A 1 68  ? 29.645  15.027  -2.879  1.00 13.59 ? 72  ALA   A N    1 
ATOM   487  C  CA   . ALA   A 1 68  ? 29.622  16.419  -3.299  1.00 14.16 ? 72  ALA   A CA   1 
ATOM   488  C  C    . ALA   A 1 68  ? 28.976  17.254  -2.200  1.00 13.69 ? 72  ALA   A C    1 
ATOM   489  O  O    . ALA   A 1 68  ? 27.792  17.101  -1.932  1.00 15.14 ? 72  ALA   A O    1 
ATOM   490  C  CB   . ALA   A 1 68  ? 28.865  16.561  -4.608  1.00 15.82 ? 72  ALA   A CB   1 
ATOM   491  N  N    . PRO   A 1 69  ? 29.717  18.148  -1.518  1.00 12.67 ? 73  PRO   A N    1 
ATOM   492  C  CA   . PRO   A 1 69  ? 29.126  18.966  -0.466  1.00 12.92 ? 73  PRO   A CA   1 
ATOM   493  C  C    . PRO   A 1 69  ? 28.370  20.136  -1.080  1.00 12.70 ? 73  PRO   A C    1 
ATOM   494  O  O    . PRO   A 1 69  ? 28.577  20.488  -2.242  1.00 13.57 ? 73  PRO   A O    1 
ATOM   495  C  CB   . PRO   A 1 69  ? 30.364  19.425  0.300   1.00 12.90 ? 73  PRO   A CB   1 
ATOM   496  C  CG   . PRO   A 1 69  ? 31.386  19.620  -0.786  1.00 13.25 ? 73  PRO   A CG   1 
ATOM   497  C  CD   . PRO   A 1 69  ? 31.142  18.441  -1.716  1.00 13.08 ? 73  PRO   A CD   1 
ATOM   498  N  N    . GLY   A 1 70  ? 27.553  20.787  -0.257  1.00 13.05 ? 74  GLY   A N    1 
ATOM   499  C  CA   . GLY   A 1 70  ? 26.753  21.914  -0.710  1.00 12.91 ? 74  GLY   A CA   1 
ATOM   500  C  C    . GLY   A 1 70  ? 27.484  23.255  -0.646  1.00 12.62 ? 74  GLY   A C    1 
ATOM   501  O  O    . GLY   A 1 70  ? 26.866  24.291  -0.829  1.00 13.19 ? 74  GLY   A O    1 
ATOM   502  N  N    . LYS   A 1 71  ? 28.787  23.241  -0.365  1.00 12.50 ? 75  LYS   A N    1 
ATOM   503  C  CA   . LYS   A 1 71  ? 29.563  24.465  -0.236  1.00 12.72 ? 75  LYS   A CA   1 
ATOM   504  C  C    . LYS   A 1 71  ? 30.997  24.171  -0.642  1.00 12.61 ? 75  LYS   A C    1 
ATOM   505  O  O    . LYS   A 1 71  ? 31.386  23.012  -0.772  1.00 12.42 ? 75  LYS   A O    1 
ATOM   506  C  CB   . LYS   A 1 71  ? 29.508  24.992  1.205   1.00 13.23 ? 75  LYS   A CB   1 
ATOM   507  C  CG   . LYS   A 1 71  ? 30.190  24.088  2.234   1.00 14.29 ? 75  LYS   A CG   1 
ATOM   508  C  CD   . LYS   A 1 71  ? 30.043  24.547  3.681   1.00 16.12 ? 75  LYS   A CD   1 
ATOM   509  C  CE   . LYS   A 1 71  ? 30.717  25.869  3.900   1.00 18.35 ? 75  LYS   A CE   1 
ATOM   510  N  NZ   . LYS   A 1 71  ? 30.902  26.216  5.306   1.00 19.64 ? 75  LYS   A NZ   1 
ATOM   511  N  N    . ALA   A 1 72  ? 31.781  25.228  -0.822  1.00 13.10 ? 76  ALA   A N    1 
ATOM   512  C  CA   . ALA   A 1 72  ? 33.186  25.095  -1.152  1.00 13.39 ? 76  ALA   A CA   1 
ATOM   513  C  C    . ALA   A 1 72  ? 33.955  24.519  0.033   1.00 13.61 ? 76  ALA   A C    1 
ATOM   514  O  O    . ALA   A 1 72  ? 33.677  24.822  1.198   1.00 14.53 ? 76  ALA   A O    1 
ATOM   515  C  CB   . ALA   A 1 72  ? 33.757  26.447  -1.545  1.00 14.44 ? 76  ALA   A CB   1 
ATOM   516  N  N    . CYS   A 1 73  ? 34.967  23.721  -0.292  1.00 12.92 ? 77  CYS   A N    1 
ATOM   517  C  CA   . CYS   A 1 73  ? 35.989  23.341  0.663   1.00 13.14 ? 77  CYS   A CA   1 
ATOM   518  C  C    . CYS   A 1 73  ? 36.874  24.552  0.900   1.00 14.05 ? 77  CYS   A C    1 
ATOM   519  O  O    . CYS   A 1 73  ? 37.171  25.295  -0.036  1.00 15.54 ? 77  CYS   A O    1 
ATOM   520  C  CB   . CYS   A 1 73  ? 36.881  22.228  0.123   1.00 13.18 ? 77  CYS   A CB   1 
ATOM   521  S  SG   . CYS   A 1 73  ? 36.008  20.683  -0.195  1.00 14.10 ? 77  CYS   A SG   1 
ATOM   522  N  N    . SER   A 1 74  ? 37.332  24.726  2.136   1.00 13.92 ? 78  SER   A N    1 
ATOM   523  C  CA   . SER   A 1 74  ? 38.293  25.781  2.394   1.00 15.70 ? 78  SER   A CA   1 
ATOM   524  C  C    . SER   A 1 74  ? 39.638  25.409  1.775   1.00 15.79 ? 78  SER   A C    1 
ATOM   525  O  O    . SER   A 1 74  ? 39.947  24.236  1.556   1.00 15.82 ? 78  SER   A O    1 
ATOM   526  C  CB   . SER   A 1 74  ? 38.455  26.042  3.845   1.00 16.87 ? 78  SER   A CB   1 
ATOM   527  O  OG   . SER   A 1 74  ? 39.071  24.933  4.466   1.00 16.74 ? 78  SER   A OG   1 
ATOM   528  N  N    . PRO   A 1 75  ? 40.492  26.404  1.471   1.00 16.91 ? 79  PRO   A N    1 
ATOM   529  C  CA   . PRO   A 1 75  ? 41.863  26.128  1.053   1.00 17.56 ? 79  PRO   A CA   1 
ATOM   530  C  C    . PRO   A 1 75  ? 42.595  25.176  1.996   1.00 15.93 ? 79  PRO   A C    1 
ATOM   531  O  O    . PRO   A 1 75  ? 43.291  24.274  1.543   1.00 17.17 ? 79  PRO   A O    1 
ATOM   532  C  CB   . PRO   A 1 75  ? 42.466  27.536  1.018   1.00 18.52 ? 79  PRO   A CB   1 
ATOM   533  C  CG   . PRO   A 1 75  ? 41.310  28.415  0.630   1.00 18.93 ? 79  PRO   A CG   1 
ATOM   534  C  CD   . PRO   A 1 75  ? 40.139  27.832  1.388   1.00 18.02 ? 79  PRO   A CD   1 
ATOM   535  N  N    . ALA   A 1 76  ? 42.417  25.352  3.311   1.00 16.52 ? 80  ALA   A N    1 
ATOM   536  C  CA   . ALA   A 1 76  ? 43.070  24.493  4.284   1.00 16.75 ? 80  ALA   A CA   1 
ATOM   537  C  C    . ALA   A 1 76  ? 42.564  23.060  4.155   1.00 16.51 ? 80  ALA   A C    1 
ATOM   538  O  O    . ALA   A 1 76  ? 43.347  22.117  4.201   1.00 18.15 ? 80  ALA   A O    1 
ATOM   539  C  CB   . ALA   A 1 76  ? 42.868  25.013  5.693   1.00 17.11 ? 80  ALA   A CB   1 
ATOM   540  N  N    . ALA   A 1 77  ? 41.252  22.900  3.968   1.00 15.76 ? 81  ALA   A N    1 
ATOM   541  C  CA   . ALA   A 1 77  ? 40.691  21.570  3.820   1.00 15.64 ? 81  ALA   A CA   1 
ATOM   542  C  C    . ALA   A 1 77  ? 41.247  20.917  2.557   1.00 15.23 ? 81  ALA   A C    1 
ATOM   543  O  O    . ALA   A 1 77  ? 41.587  19.742  2.552   1.00 16.60 ? 81  ALA   A O    1 
ATOM   544  C  CB   . ALA   A 1 77  ? 39.179  21.634  3.784   1.00 15.73 ? 81  ALA   A CB   1 
ATOM   545  N  N    . SER   A 1 78  ? 41.314  21.671  1.459   1.00 14.86 ? 82  SER   A N    1 
ATOM   546  C  CA   . SER   A 1 78  ? 41.772  21.117  0.195   1.00 14.86 ? 82  SER   A CA   1 
ATOM   547  C  C    . SER   A 1 78  ? 43.240  20.703  0.271   1.00 15.45 ? 82  SER   A C    1 
ATOM   548  O  O    . SER   A 1 78  ? 43.632  19.706  -0.329  1.00 16.84 ? 82  SER   A O    1 
ATOM   549  C  CB   . SER   A 1 78  ? 41.524  22.083  -0.929  1.00 14.82 ? 82  SER   A CB   1 
ATOM   550  O  OG   . SER   A 1 78  ? 40.138  22.179  -1.216  1.00 16.00 ? 82  SER   A OG   1 
ATOM   551  N  N    . GLU   A 1 79  ? 44.056  21.464  1.004   1.00 16.39 ? 83  GLU   A N    1 
ATOM   552  C  CA   . GLU   A 1 79  ? 45.466  21.137  1.147   1.00 19.07 ? 83  GLU   A CA   1 
ATOM   553  C  C    . GLU   A 1 79  ? 45.680  19.833  1.910   1.00 20.43 ? 83  GLU   A C    1 
ATOM   554  O  O    . GLU   A 1 79  ? 46.619  19.101  1.599   1.00 23.29 ? 83  GLU   A O    1 
ATOM   555  C  CB   . GLU   A 1 79  ? 46.228  22.278  1.820   1.00 21.66 ? 83  GLU   A CB   1 
ATOM   556  C  CG   . GLU   A 1 79  ? 46.460  23.437  0.865   1.00 25.69 ? 83  GLU   A CG   1 
ATOM   557  C  CD   . GLU   A 1 79  ? 47.057  24.670  1.509   1.00 28.95 ? 83  GLU   A CD   1 
ATOM   558  O  OE1  . GLU   A 1 79  ? 47.103  24.749  2.750   1.00 32.90 ? 83  GLU   A OE1  1 
ATOM   559  O  OE2  . GLU   A 1 79  ? 47.453  25.568  0.747   1.00 34.73 ? 83  GLU   A OE2  1 
ATOM   560  N  N    A ILE   A 1 80  ? 44.831  19.560  2.909   0.50 19.96 ? 84  ILE   A N    1 
ATOM   561  N  N    B ILE   A 1 80  ? 44.843  19.562  2.917   0.50 20.15 ? 84  ILE   A N    1 
ATOM   562  C  CA   A ILE   A 1 80  ? 45.022  18.399  3.763   0.50 21.83 ? 84  ILE   A CA   1 
ATOM   563  C  CA   B ILE   A 1 80  ? 45.031  18.389  3.754   0.50 22.16 ? 84  ILE   A CA   1 
ATOM   564  C  C    A ILE   A 1 80  ? 44.309  17.176  3.187   0.50 22.01 ? 84  ILE   A C    1 
ATOM   565  C  C    B ILE   A 1 80  ? 44.337  17.173  3.144   0.50 22.15 ? 84  ILE   A C    1 
ATOM   566  O  O    A ILE   A 1 80  ? 44.769  16.063  3.421   0.50 23.74 ? 84  ILE   A O    1 
ATOM   567  O  O    B ILE   A 1 80  ? 44.844  16.066  3.298   0.50 23.96 ? 84  ILE   A O    1 
ATOM   568  C  CB   A ILE   A 1 80  ? 44.608  18.691  5.220   0.50 23.60 ? 84  ILE   A CB   1 
ATOM   569  C  CB   B ILE   A 1 80  ? 44.580  18.665  5.201   0.50 24.30 ? 84  ILE   A CB   1 
ATOM   570  C  CG1  A ILE   A 1 80  ? 45.025  17.553  6.150   0.50 24.75 ? 84  ILE   A CG1  1 
ATOM   571  C  CG1  B ILE   A 1 80  ? 43.140  19.149  5.271   0.50 25.53 ? 84  ILE   A CG1  1 
ATOM   572  C  CG2  A ILE   A 1 80  ? 43.117  18.994  5.343   0.50 24.70 ? 84  ILE   A CG2  1 
ATOM   573  C  CG2  B ILE   A 1 80  ? 45.531  19.648  5.878   0.50 25.58 ? 84  ILE   A CG2  1 
ATOM   574  N  N    . THR   A 1 81  ? 43.204  17.366  2.447   1.00 21.07 ? 85  THR   A N    1 
ATOM   575  C  CA   . THR   A 1 81  ? 42.381  16.240  1.998   1.00 20.88 ? 85  THR   A CA   1 
ATOM   576  C  C    . THR   A 1 81  ? 42.625  15.910  0.524   1.00 20.17 ? 85  THR   A C    1 
ATOM   577  O  O    . THR   A 1 81  ? 42.244  14.828  0.085   1.00 22.77 ? 85  THR   A O    1 
ATOM   578  C  CB   . THR   A 1 81  ? 40.887  16.488  2.238   1.00 20.49 ? 85  THR   A CB   1 
ATOM   579  O  OG1  . THR   A 1 81  ? 40.439  17.524  1.360   1.00 19.56 ? 85  THR   A OG1  1 
ATOM   580  C  CG2  . THR   A 1 81  ? 40.563  16.840  3.681   1.00 21.46 ? 85  THR   A CG2  1 
ATOM   581  N  N    . GLY   A 1 82  ? 43.179  16.864  -0.244  1.00 19.76 ? 86  GLY   A N    1 
ATOM   582  C  CA   . GLY   A 1 82  ? 43.341  16.755  -1.686  1.00 19.23 ? 86  GLY   A CA   1 
ATOM   583  C  C    . GLY   A 1 82  ? 42.020  16.771  -2.466  1.00 17.80 ? 86  GLY   A C    1 
ATOM   584  O  O    . GLY   A 1 82  ? 41.984  16.378  -3.626  1.00 20.65 ? 86  GLY   A O    1 
ATOM   585  N  N    . LEU   A 1 83  ? 40.941  17.253  -1.852  1.00 15.88 ? 87  LEU   A N    1 
ATOM   586  C  CA   . LEU   A 1 83  ? 39.636  17.340  -2.488  1.00 14.68 ? 87  LEU   A CA   1 
ATOM   587  C  C    . LEU   A 1 83  ? 39.245  18.809  -2.595  1.00 14.22 ? 87  LEU   A C    1 
ATOM   588  O  O    . LEU   A 1 83  ? 39.649  19.633  -1.779  1.00 15.32 ? 87  LEU   A O    1 
ATOM   589  C  CB   . LEU   A 1 83  ? 38.568  16.578  -1.703  1.00 15.29 ? 87  LEU   A CB   1 
ATOM   590  C  CG   . LEU   A 1 83  ? 38.809  15.080  -1.497  1.00 15.29 ? 87  LEU   A CG   1 
ATOM   591  C  CD1  . LEU   A 1 83  ? 37.757  14.512  -0.542  1.00 16.04 ? 87  LEU   A CD1  1 
ATOM   592  C  CD2  . LEU   A 1 83  ? 38.799  14.337  -2.813  1.00 15.96 ? 87  LEU   A CD2  1 
ATOM   593  N  N    . SER   A 1 84  ? 38.434  19.112  -3.608  1.00 13.45 ? 88  SER   A N    1 
ATOM   594  C  CA   . SER   A 1 84  ? 37.730  20.378  -3.693  1.00 12.89 ? 88  SER   A CA   1 
ATOM   595  C  C    . SER   A 1 84  ? 36.331  20.086  -4.208  1.00 12.61 ? 88  SER   A C    1 
ATOM   596  O  O    . SER   A 1 84  ? 36.117  19.072  -4.867  1.00 12.64 ? 88  SER   A O    1 
ATOM   597  C  CB   . SER   A 1 84  ? 38.437  21.394  -4.588  1.00 14.14 ? 88  SER   A CB   1 
ATOM   598  O  OG   . SER   A 1 84  ? 38.341  21.016  -5.954  1.00 15.57 ? 88  SER   A OG   1 
ATOM   599  N  N    . THR   A 1 85  ? 35.400  21.012  -3.958  1.00 12.58 ? 89  THR   A N    1 
ATOM   600  C  CA   . THR   A 1 85  ? 34.018  20.803  -4.368  1.00 12.73 ? 89  THR   A CA   1 
ATOM   601  C  C    . THR   A 1 85  ? 33.935  20.720  -5.892  1.00 12.85 ? 89  THR   A C    1 
ATOM   602  O  O    . THR   A 1 85  ? 33.234  19.859  -6.428  1.00 13.30 ? 89  THR   A O    1 
ATOM   603  C  CB   . THR   A 1 85  ? 33.138  21.899  -3.765  1.00 13.25 ? 89  THR   A CB   1 
ATOM   604  O  OG1  . THR   A 1 85  ? 33.359  21.787  -2.355  1.00 13.55 ? 89  THR   A OG1  1 
ATOM   605  C  CG2  . THR   A 1 85  ? 31.670  21.722  -4.110  1.00 13.59 ? 89  THR   A CG2  1 
ATOM   606  N  N    . ALA   A 1 86  ? 34.695  21.573  -6.593  1.00 13.19 ? 90  ALA   A N    1 
ATOM   607  C  CA   . ALA   A 1 86  ? 34.668  21.570  -8.047  1.00 13.92 ? 90  ALA   A CA   1 
ATOM   608  C  C    . ALA   A 1 86  ? 35.182  20.248  -8.612  1.00 14.29 ? 90  ALA   A C    1 
ATOM   609  O  O    . ALA   A 1 86  ? 34.632  19.738  -9.581  1.00 14.97 ? 90  ALA   A O    1 
ATOM   610  C  CB   . ALA   A 1 86  ? 35.478  22.728  -8.578  1.00 14.37 ? 90  ALA   A CB   1 
ATOM   611  N  N    . VAL   A 1 87  ? 36.253  19.707  -8.026  1.00 14.20 ? 91  VAL   A N    1 
ATOM   612  C  CA   . VAL   A 1 87  ? 36.823  18.460  -8.507  1.00 15.11 ? 91  VAL   A CA   1 
ATOM   613  C  C    . VAL   A 1 87  ? 35.884  17.294  -8.195  1.00 13.77 ? 91  VAL   A C    1 
ATOM   614  O  O    . VAL   A 1 87  ? 35.704  16.415  -9.027  1.00 13.79 ? 91  VAL   A O    1 
ATOM   615  C  CB   . VAL   A 1 87  ? 38.245  18.236  -7.968  1.00 17.95 ? 91  VAL   A CB   1 
ATOM   616  C  CG1  . VAL   A 1 87  ? 38.735  16.823  -8.244  1.00 19.68 ? 91  VAL   A CG1  1 
ATOM   617  C  CG2  . VAL   A 1 87  ? 39.209  19.253  -8.562  1.00 19.34 ? 91  VAL   A CG2  1 
ATOM   618  N  N    . LEU   A 1 88  ? 35.269  17.286  -7.009  1.00 12.31 ? 92  LEU   A N    1 
ATOM   619  C  CA   . LEU   A 1 88  ? 34.265  16.275  -6.713  1.00 12.32 ? 92  LEU   A CA   1 
ATOM   620  C  C    . LEU   A 1 88  ? 33.151  16.311  -7.757  1.00 12.92 ? 92  LEU   A C    1 
ATOM   621  O  O    . LEU   A 1 88  ? 32.720  15.267  -8.246  1.00 13.09 ? 92  LEU   A O    1 
ATOM   622  C  CB   . LEU   A 1 88  ? 33.745  16.505  -5.300  1.00 12.19 ? 92  LEU   A CB   1 
ATOM   623  C  CG   . LEU   A 1 88  ? 34.738  16.139  -4.193  1.00 12.45 ? 92  LEU   A CG   1 
ATOM   624  C  CD1  . LEU   A 1 88  ? 34.405  16.822  -2.886  1.00 12.53 ? 92  LEU   A CD1  1 
ATOM   625  C  CD2  . LEU   A 1 88  ? 34.791  14.642  -3.998  1.00 12.98 ? 92  LEU   A CD2  1 
ATOM   626  N  N    . ALA   A 1 89  ? 32.701  17.522  -8.107  1.00 13.26 ? 93  ALA   A N    1 
ATOM   627  C  CA   . ALA   A 1 89  ? 31.667  17.679  -9.121  1.00 14.47 ? 93  ALA   A CA   1 
ATOM   628  C  C    . ALA   A 1 89  ? 32.129  17.164  -10.483 1.00 14.81 ? 93  ALA   A C    1 
ATOM   629  O  O    . ALA   A 1 89  ? 31.350  16.521  -11.182 1.00 15.51 ? 93  ALA   A O    1 
ATOM   630  C  CB   . ALA   A 1 89  ? 31.237  19.119  -9.197  1.00 15.77 ? 93  ALA   A CB   1 
ATOM   631  N  N    . ALA   A 1 90  ? 33.385  17.443  -10.857 1.00 15.05 ? 94  ALA   A N    1 
ATOM   632  C  CA   . ALA   A 1 90  ? 33.927  16.983  -12.134 1.00 15.80 ? 94  ALA   A CA   1 
ATOM   633  C  C    . ALA   A 1 90  ? 33.933  15.458  -12.237 1.00 15.35 ? 94  ALA   A C    1 
ATOM   634  O  O    . ALA   A 1 90  ? 33.848  14.907  -13.333 1.00 17.13 ? 94  ALA   A O    1 
ATOM   635  C  CB   . ALA   A 1 90  ? 35.322  17.543  -12.357 1.00 17.20 ? 94  ALA   A CB   1 
ATOM   636  N  N    . HIS   A 1 91  ? 34.016  14.773  -11.092 1.00 14.07 ? 95  HIS   A N    1 
ATOM   637  C  CA   . HIS   A 1 91  ? 33.969  13.318  -11.040 1.00 14.29 ? 95  HIS   A CA   1 
ATOM   638  C  C    . HIS   A 1 91  ? 32.551  12.792  -10.824 1.00 14.14 ? 95  HIS   A C    1 
ATOM   639  O  O    . HIS   A 1 91  ? 32.371  11.614  -10.508 1.00 15.08 ? 95  HIS   A O    1 
ATOM   640  C  CB   . HIS   A 1 91  ? 34.904  12.789  -9.952  1.00 15.05 ? 95  HIS   A CB   1 
ATOM   641  C  CG   . HIS   A 1 91  ? 36.345  12.927  -10.281 1.00 15.97 ? 95  HIS   A CG   1 
ATOM   642  N  ND1  . HIS   A 1 91  ? 37.013  14.127  -10.202 1.00 18.37 ? 95  HIS   A ND1  1 
ATOM   643  C  CD2  . HIS   A 1 91  ? 37.255  12.030  -10.689 1.00 16.98 ? 95  HIS   A CD2  1 
ATOM   644  C  CE1  . HIS   A 1 91  ? 38.282  13.946  -10.539 1.00 18.74 ? 95  HIS   A CE1  1 
ATOM   645  N  NE2  . HIS   A 1 91  ? 38.456  12.682  -10.821 1.00 18.64 ? 95  HIS   A NE2  1 
ATOM   646  N  N    . GLY   A 1 92  ? 31.550  13.658  -10.989 1.00 13.84 ? 96  GLY   A N    1 
ATOM   647  C  CA   . GLY   A 1 92  ? 30.156  13.250  -10.973 1.00 14.43 ? 96  GLY   A CA   1 
ATOM   648  C  C    . GLY   A 1 92  ? 29.660  12.833  -9.591  1.00 14.52 ? 96  GLY   A C    1 
ATOM   649  O  O    . GLY   A 1 92  ? 28.681  12.098  -9.485  1.00 16.40 ? 96  GLY   A O    1 
ATOM   650  N  N    . ARG   A 1 93  ? 30.296  13.333  -8.529  1.00 13.96 ? 97  ARG   A N    1 
ATOM   651  C  CA   . ARG   A 1 93  ? 29.893  12.918  -7.194  1.00 14.38 ? 97  ARG   A CA   1 
ATOM   652  C  C    . ARG   A 1 93  ? 28.534  13.522  -6.839  1.00 14.87 ? 97  ARG   A C    1 
ATOM   653  O  O    . ARG   A 1 93  ? 28.209  14.645  -7.225  1.00 16.57 ? 97  ARG   A O    1 
ATOM   654  C  CB   . ARG   A 1 93  ? 30.950  13.278  -6.150  1.00 14.13 ? 97  ARG   A CB   1 
ATOM   655  C  CG   . ARG   A 1 93  ? 32.307  12.609  -6.320  1.00 14.33 ? 97  ARG   A CG   1 
ATOM   656  C  CD   . ARG   A 1 93  ? 32.242  11.096  -6.409  1.00 14.70 ? 97  ARG   A CD   1 
ATOM   657  N  NE   . ARG   A 1 93  ? 31.957  10.637  -7.771  1.00 14.81 ? 97  ARG   A NE   1 
ATOM   658  C  CZ   . ARG   A 1 93  ? 31.560  9.416   -8.109  1.00 15.86 ? 97  ARG   A CZ   1 
ATOM   659  N  NH1  . ARG   A 1 93  ? 31.378  8.503   -7.182  1.00 16.19 ? 97  ARG   A NH1  1 
ATOM   660  N  NH2  . ARG   A 1 93  ? 31.356  9.105   -9.374  1.00 16.31 ? 97  ARG   A NH2  1 
ATOM   661  N  N    . GLN   A 1 94  ? 27.740  12.743  -6.103  1.00 15.33 ? 98  GLN   A N    1 
ATOM   662  C  CA   . GLN   A 1 94  ? 26.416  13.158  -5.676  1.00 15.81 ? 98  GLN   A CA   1 
ATOM   663  C  C    . GLN   A 1 94  ? 26.446  13.616  -4.222  1.00 15.24 ? 98  GLN   A C    1 
ATOM   664  O  O    . GLN   A 1 94  ? 27.364  13.300  -3.468  1.00 14.54 ? 98  GLN   A O    1 
ATOM   665  C  CB   . GLN   A 1 94  ? 25.414  12.015  -5.810  1.00 17.96 ? 98  GLN   A CB   1 
ATOM   666  C  CG   . GLN   A 1 94  ? 25.264  11.524  -7.238  1.00 20.37 ? 98  GLN   A CG   1 
ATOM   667  C  CD   . GLN   A 1 94  ? 24.445  10.260  -7.335  1.00 23.22 ? 98  GLN   A CD   1 
ATOM   668  O  OE1  . GLN   A 1 94  ? 23.784  9.821   -6.381  1.00 27.20 ? 98  GLN   A OE1  1 
ATOM   669  N  NE2  . GLN   A 1 94  ? 24.529  9.647   -8.501  1.00 24.20 ? 98  GLN   A NE2  1 
ATOM   670  N  N    . CYS   A 1 95  ? 25.405  14.355  -3.844  1.00 16.35 ? 99  CYS   A N    1 
ATOM   671  C  CA   . CYS   A 1 95  ? 25.309  14.900  -2.504  1.00 17.31 ? 99  CYS   A CA   1 
ATOM   672  C  C    . CYS   A 1 95  ? 24.978  13.808  -1.487  1.00 16.46 ? 99  CYS   A C    1 
ATOM   673  O  O    . CYS   A 1 95  ? 24.706  12.652  -1.826  1.00 16.15 ? 99  CYS   A O    1 
ATOM   674  C  CB   . CYS   A 1 95  ? 24.285  16.022  -2.455  1.00 19.72 ? 99  CYS   A CB   1 
ATOM   675  S  SG   . CYS   A 1 95  ? 22.597  15.440  -2.726  1.00 25.12 ? 99  CYS   A SG   1 
ATOM   676  N  N    . PHE   A 1 96  ? 25.022  14.204  -0.212  1.00 15.88 ? 100 PHE   A N    1 
ATOM   677  C  CA   . PHE   A 1 96  ? 24.613  13.343  0.879   1.00 16.20 ? 100 PHE   A CA   1 
ATOM   678  C  C    . PHE   A 1 96  ? 23.094  13.268  0.845   1.00 17.41 ? 100 PHE   A C    1 
ATOM   679  O  O    . PHE   A 1 96  ? 22.432  14.248  1.181   1.00 21.29 ? 100 PHE   A O    1 
ATOM   680  C  CB   . PHE   A 1 96  ? 25.162  13.899  2.198   1.00 16.23 ? 100 PHE   A CB   1 
ATOM   681  C  CG   . PHE   A 1 96  ? 25.299  12.858  3.294   1.00 16.15 ? 100 PHE   A CG   1 
ATOM   682  C  CD1  . PHE   A 1 96  ? 24.188  12.172  3.775   1.00 17.77 ? 100 PHE   A CD1  1 
ATOM   683  C  CD2  . PHE   A 1 96  ? 26.544  12.551  3.833   1.00 16.90 ? 100 PHE   A CD2  1 
ATOM   684  C  CE1  . PHE   A 1 96  ? 24.324  11.216  4.774   1.00 18.25 ? 100 PHE   A CE1  1 
ATOM   685  C  CE2  . PHE   A 1 96  ? 26.670  11.591  4.824   1.00 17.43 ? 100 PHE   A CE2  1 
ATOM   686  C  CZ   . PHE   A 1 96  ? 25.563  10.926  5.288   1.00 18.28 ? 100 PHE   A CZ   1 
ATOM   687  N  N    . ASP   A 1 97  ? 22.553  12.131  0.402   1.00 16.36 ? 101 ASP   A N    1 
ATOM   688  C  CA   . ASP   A 1 97  ? 21.122  12.011  0.178   1.00 17.93 ? 101 ASP   A CA   1 
ATOM   689  C  C    . ASP   A 1 97  ? 20.576  10.715  0.782   1.00 17.90 ? 101 ASP   A C    1 
ATOM   690  O  O    . ASP   A 1 97  ? 21.298  9.946   1.408   1.00 16.38 ? 101 ASP   A O    1 
ATOM   691  C  CB   . ASP   A 1 97  ? 20.830  12.140  -1.308  1.00 19.61 ? 101 ASP   A CB   1 
ATOM   692  C  CG   . ASP   A 1 97  ? 21.464  11.070  -2.182  1.00 21.33 ? 101 ASP   A CG   1 
ATOM   693  O  OD1  . ASP   A 1 97  ? 22.057  10.129  -1.617  1.00 20.59 ? 101 ASP   A OD1  1 
ATOM   694  O  OD2  . ASP   A 1 97  ? 21.353  11.185  -3.423  1.00 25.77 ? 101 ASP   A OD2  1 
ATOM   695  N  N    . ASP   A 1 98  ? 19.277  10.476  0.563   1.00 18.85 ? 102 ASP   A N    1 
ATOM   696  C  CA   . ASP   A 1 98  ? 18.601  9.298   1.086   1.00 20.51 ? 102 ASP   A CA   1 
ATOM   697  C  C    . ASP   A 1 98  ? 19.277  8.014   0.623   1.00 19.78 ? 102 ASP   A C    1 
ATOM   698  O  O    . ASP   A 1 98  ? 19.466  7.098   1.423   1.00 20.20 ? 102 ASP   A O    1 
ATOM   699  C  CB   . ASP   A 1 98  ? 17.143  9.263   0.654   1.00 23.44 ? 102 ASP   A CB   1 
ATOM   700  C  CG   . ASP   A 1 98  ? 16.235  10.242  1.377   1.00 28.46 ? 102 ASP   A CG   1 
ATOM   701  O  OD1  . ASP   A 1 98  ? 16.735  10.931  2.290   1.00 32.04 ? 102 ASP   A OD1  1 
ATOM   702  O  OD2  . ASP   A 1 98  ? 15.039  10.315  1.003   1.00 35.31 ? 102 ASP   A OD2  1 
ATOM   703  N  N    . ASN   A 1 99  ? 19.626  7.943   -0.665  1.00 18.82 ? 103 ASN   A N    1 
ATOM   704  C  CA   . ASN   A 1 99  ? 20.284  6.760   -1.201  1.00 19.66 ? 103 ASN   A CA   1 
ATOM   705  C  C    . ASN   A 1 99  ? 21.579  6.478   -0.435  1.00 17.92 ? 103 ASN   A C    1 
ATOM   706  O  O    . ASN   A 1 99  ? 21.886  5.323   -0.134  1.00 18.01 ? 103 ASN   A O    1 
ATOM   707  C  CB   . ASN   A 1 99  ? 20.541  6.880   -2.702  1.00 20.21 ? 103 ASN   A CB   1 
ATOM   708  C  CG   . ASN   A 1 99  ? 21.229  5.652   -3.262  1.00 21.23 ? 103 ASN   A CG   1 
ATOM   709  O  OD1  . ASN   A 1 99  ? 20.653  4.555   -3.254  1.00 22.76 ? 103 ASN   A OD1  1 
ATOM   710  N  ND2  . ASN   A 1 99  ? 22.453  5.803   -3.749  1.00 20.97 ? 103 ASN   A ND2  1 
ATOM   711  N  N    . LEU   A 1 100 ? 22.348  7.525   -0.114  1.00 16.70 ? 104 LEU   A N    1 
ATOM   712  C  CA   . LEU   A 1 100 ? 23.588  7.328   0.621   1.00 15.81 ? 104 LEU   A CA   1 
ATOM   713  C  C    . LEU   A 1 100 ? 23.295  6.789   2.019   1.00 15.30 ? 104 LEU   A C    1 
ATOM   714  O  O    . LEU   A 1 100 ? 23.962  5.866   2.490   1.00 15.11 ? 104 LEU   A O    1 
ATOM   715  C  CB   . LEU   A 1 100 ? 24.416  8.611   0.685   1.00 15.56 ? 104 LEU   A CB   1 
ATOM   716  C  CG   . LEU   A 1 100 ? 25.759  8.497   1.415   1.00 16.28 ? 104 LEU   A CG   1 
ATOM   717  C  CD1  . LEU   A 1 100 ? 26.602  7.385   0.863   1.00 17.90 ? 104 LEU   A CD1  1 
ATOM   718  C  CD2  . LEU   A 1 100 ? 26.512  9.814   1.348   1.00 17.30 ? 104 LEU   A CD2  1 
ATOM   719  N  N    . ALA   A 1 101 ? 22.305  7.369   2.698   1.00 16.08 ? 105 ALA   A N    1 
ATOM   720  C  CA   . ALA   A 1 101 ? 21.961  6.889   4.030   1.00 16.81 ? 105 ALA   A CA   1 
ATOM   721  C  C    . ALA   A 1 101 ? 21.557  5.413   3.977   1.00 17.97 ? 105 ALA   A C    1 
ATOM   722  O  O    . ALA   A 1 101 ? 21.951  4.621   4.836   1.00 18.83 ? 105 ALA   A O    1 
ATOM   723  C  CB   . ALA   A 1 101 ? 20.860  7.750   4.613   1.00 17.60 ? 105 ALA   A CB   1 
ATOM   724  N  N    . ASN   A 1 102 ? 20.774  5.045   2.957   1.00 18.80 ? 106 ASN   A N    1 
ATOM   725  C  CA   . ASN   A 1 102 ? 20.331  3.666   2.788   1.00 19.36 ? 106 ASN   A CA   1 
ATOM   726  C  C    . ASN   A 1 102 ? 21.519  2.740   2.531   1.00 17.86 ? 106 ASN   A C    1 
ATOM   727  O  O    . ASN   A 1 102 ? 21.551  1.623   3.044   1.00 18.55 ? 106 ASN   A O    1 
ATOM   728  C  CB   . ASN   A 1 102 ? 19.323  3.530   1.652   1.00 21.82 ? 106 ASN   A CB   1 
ATOM   729  C  CG   . ASN   A 1 102 ? 17.993  4.173   1.969   1.00 25.41 ? 106 ASN   A CG   1 
ATOM   730  O  OD1  . ASN   A 1 102 ? 17.610  4.296   3.137   1.00 28.51 ? 106 ASN   A OD1  1 
ATOM   731  N  ND2  . ASN   A 1 102 ? 17.264  4.563   0.934   1.00 28.41 ? 106 ASN   A ND2  1 
ATOM   732  N  N    A LEU   A 1 103 ? 22.481  3.197   1.717   0.50 16.89 ? 107 LEU   A N    1 
ATOM   733  N  N    B LEU   A 1 103 ? 22.470  3.216   1.722   0.50 16.72 ? 107 LEU   A N    1 
ATOM   734  C  CA   A LEU   A 1 103 ? 23.685  2.429   1.428   0.50 16.37 ? 107 LEU   A CA   1 
ATOM   735  C  CA   B LEU   A 1 103 ? 23.687  2.486   1.409   0.50 16.01 ? 107 LEU   A CA   1 
ATOM   736  C  C    A LEU   A 1 103 ? 24.464  2.185   2.719   0.50 15.48 ? 107 LEU   A C    1 
ATOM   737  C  C    B LEU   A 1 103 ? 24.480  2.208   2.687   0.50 15.36 ? 107 LEU   A C    1 
ATOM   738  O  O    A LEU   A 1 103 ? 24.864  1.055   2.995   0.50 15.04 ? 107 LEU   A O    1 
ATOM   739  O  O    B LEU   A 1 103 ? 24.903  1.077   2.923   0.50 15.22 ? 107 LEU   A O    1 
ATOM   740  C  CB   A LEU   A 1 103 ? 24.535  3.137   0.370   0.50 16.17 ? 107 LEU   A CB   1 
ATOM   741  C  CB   B LEU   A 1 103 ? 24.455  3.335   0.396   0.50 15.53 ? 107 LEU   A CB   1 
ATOM   742  C  CG   A LEU   A 1 103 ? 25.947  2.583   0.134   0.50 16.25 ? 107 LEU   A CG   1 
ATOM   743  C  CG   B LEU   A 1 103 ? 25.680  2.695   -0.260  0.50 15.25 ? 107 LEU   A CG   1 
ATOM   744  C  CD1  A LEU   A 1 103 ? 25.962  1.112   -0.269  0.50 16.46 ? 107 LEU   A CD1  1 
ATOM   745  C  CD1  B LEU   A 1 103 ? 26.167  3.571   -1.410  0.50 15.32 ? 107 LEU   A CD1  1 
ATOM   746  C  CD2  A LEU   A 1 103 ? 26.660  3.422   -0.920  0.50 16.60 ? 107 LEU   A CD2  1 
ATOM   747  C  CD2  B LEU   A 1 103 ? 26.785  2.486   0.748   0.50 15.26 ? 107 LEU   A CD2  1 
ATOM   748  N  N    . LEU   A 1 104 ? 24.656  3.237   3.526   1.00 15.28 ? 108 LEU   A N    1 
ATOM   749  C  CA   . LEU   A 1 104 ? 25.355  3.081   4.799   1.00 15.44 ? 108 LEU   A CA   1 
ATOM   750  C  C    . LEU   A 1 104 ? 24.660  2.036   5.672   1.00 15.34 ? 108 LEU   A C    1 
ATOM   751  O  O    . LEU   A 1 104 ? 25.327  1.192   6.274   1.00 14.80 ? 108 LEU   A O    1 
ATOM   752  C  CB   . LEU   A 1 104 ? 25.470  4.399   5.564   1.00 16.15 ? 108 LEU   A CB   1 
ATOM   753  C  CG   . LEU   A 1 104 ? 26.293  5.495   4.891   1.00 17.59 ? 108 LEU   A CG   1 
ATOM   754  C  CD1  . LEU   A 1 104 ? 26.168  6.774   5.689   1.00 18.64 ? 108 LEU   A CD1  1 
ATOM   755  C  CD2  . LEU   A 1 104 ? 27.746  5.107   4.744   1.00 17.92 ? 108 LEU   A CD2  1 
ATOM   756  N  N    . LEU   A 1 105 ? 23.327  2.116   5.775   1.00 16.23 ? 109 LEU   A N    1 
ATOM   757  C  CA   . LEU   A 1 105 ? 22.598  1.189   6.631   1.00 17.70 ? 109 LEU   A CA   1 
ATOM   758  C  C    . LEU   A 1 105 ? 22.705  -0.239  6.086   1.00 16.69 ? 109 LEU   A C    1 
ATOM   759  O  O    . LEU   A 1 105 ? 22.848  -1.175  6.868   1.00 16.18 ? 109 LEU   A O    1 
ATOM   760  C  CB   . LEU   A 1 105 ? 21.140  1.592   6.845   1.00 20.73 ? 109 LEU   A CB   1 
ATOM   761  C  CG   . LEU   A 1 105 ? 20.366  0.786   7.901   1.00 24.16 ? 109 LEU   A CG   1 
ATOM   762  C  CD1  . LEU   A 1 105 ? 21.074  0.658   9.255   1.00 25.86 ? 109 LEU   A CD1  1 
ATOM   763  C  CD2  . LEU   A 1 105 ? 19.002  1.421   8.102   1.00 26.70 ? 109 LEU   A CD2  1 
ATOM   764  N  N    . ALA   A 1 106 ? 22.657  -0.409  4.755   1.00 15.50 ? 110 ALA   A N    1 
ATOM   765  C  CA   . ALA   A 1 106 ? 22.767  -1.732  4.151   1.00 15.03 ? 110 ALA   A CA   1 
ATOM   766  C  C    . ALA   A 1 106 ? 24.146  -2.324  4.434   1.00 14.11 ? 110 ALA   A C    1 
ATOM   767  O  O    . ALA   A 1 106 ? 24.272  -3.522  4.681   1.00 14.47 ? 110 ALA   A O    1 
ATOM   768  C  CB   . ALA   A 1 106 ? 22.502  -1.676  2.669   1.00 15.15 ? 110 ALA   A CB   1 
ATOM   769  N  N    . PHE   A 1 107 ? 25.182  -1.480  4.387   1.00 13.54 ? 111 PHE   A N    1 
ATOM   770  C  CA   . PHE   A 1 107 ? 26.529  -1.919  4.707   1.00 12.53 ? 111 PHE   A CA   1 
ATOM   771  C  C    . PHE   A 1 107 ? 26.615  -2.359  6.174   1.00 12.73 ? 111 PHE   A C    1 
ATOM   772  O  O    . PHE   A 1 107 ? 27.188  -3.403  6.483   1.00 12.87 ? 111 PHE   A O    1 
ATOM   773  C  CB   . PHE   A 1 107 ? 27.500  -0.775  4.404   1.00 12.86 ? 111 PHE   A CB   1 
ATOM   774  C  CG   . PHE   A 1 107 ? 28.952  -1.070  4.744   1.00 12.83 ? 111 PHE   A CG   1 
ATOM   775  C  CD1  . PHE   A 1 107 ? 29.801  -1.642  3.809   1.00 12.92 ? 111 PHE   A CD1  1 
ATOM   776  C  CD2  . PHE   A 1 107 ? 29.465  -0.774  6.001   1.00 13.18 ? 111 PHE   A CD2  1 
ATOM   777  C  CE1  . PHE   A 1 107 ? 31.124  -1.909  4.128   1.00 12.83 ? 111 PHE   A CE1  1 
ATOM   778  C  CE2  . PHE   A 1 107 ? 30.782  -1.054  6.317   1.00 13.44 ? 111 PHE   A CE2  1 
ATOM   779  C  CZ   . PHE   A 1 107 ? 31.609  -1.614  5.379   1.00 13.12 ? 111 PHE   A CZ   1 
ATOM   780  N  N    . LEU   A 1 108 ? 26.053  -1.562  7.086   1.00 13.72 ? 112 LEU   A N    1 
ATOM   781  C  CA   . LEU   A 1 108 ? 26.090  -1.915  8.499   1.00 14.28 ? 112 LEU   A CA   1 
ATOM   782  C  C    . LEU   A 1 108 ? 25.310  -3.202  8.752   1.00 14.19 ? 112 LEU   A C    1 
ATOM   783  O  O    . LEU   A 1 108 ? 25.715  -4.016  9.578   1.00 14.59 ? 112 LEU   A O    1 
ATOM   784  C  CB   . LEU   A 1 108 ? 25.566  -0.784  9.382   1.00 15.94 ? 112 LEU   A CB   1 
ATOM   785  C  CG   . LEU   A 1 108 ? 26.456  0.458   9.428   1.00 17.54 ? 112 LEU   A CG   1 
ATOM   786  C  CD1  . LEU   A 1 108 ? 25.727  1.621   10.061  1.00 19.68 ? 112 LEU   A CD1  1 
ATOM   787  C  CD2  . LEU   A 1 108 ? 27.773  0.163   10.149  1.00 19.28 ? 112 LEU   A CD2  1 
ATOM   788  N  N    . ARG   A 1 109 ? 24.217  -3.402  8.011   1.00 14.30 ? 113 ARG   A N    1 
ATOM   789  C  CA   . ARG   A 1 109 ? 23.389  -4.588  8.182   1.00 15.66 ? 113 ARG   A CA   1 
ATOM   790  C  C    . ARG   A 1 109 ? 24.110  -5.874  7.781   1.00 15.18 ? 113 ARG   A C    1 
ATOM   791  O  O    . ARG   A 1 109 ? 23.645  -6.961  8.133   1.00 17.82 ? 113 ARG   A O    1 
ATOM   792  C  CB   . ARG   A 1 109 ? 22.036  -4.447  7.482   1.00 17.85 ? 113 ARG   A CB   1 
ATOM   793  C  CG   . ARG   A 1 109 ? 21.065  -3.593  8.286   1.00 21.44 ? 113 ARG   A CG   1 
ATOM   794  C  CD   . ARG   A 1 109 ? 19.618  -3.704  7.811   1.00 25.91 ? 113 ARG   A CD   1 
ATOM   795  N  NE   . ARG   A 1 109 ? 19.519  -3.470  6.370   1.00 29.52 ? 113 ARG   A NE   1 
ATOM   796  C  CZ   . ARG   A 1 109 ? 19.036  -2.390  5.754   1.00 31.95 ? 113 ARG   A CZ   1 
ATOM   797  N  NH1  . ARG   A 1 109 ? 19.220  -2.256  4.452   1.00 31.52 ? 113 ARG   A NH1  1 
ATOM   798  N  NH2  . ARG   A 1 109 ? 18.412  -1.434  6.425   1.00 36.05 ? 113 ARG   A NH2  1 
ATOM   799  N  N    . ARG   A 1 110 ? 25.231  -5.769  7.066   1.00 14.11 ? 114 ARG   A N    1 
ATOM   800  C  CA   . ARG   A 1 110 ? 26.055  -6.931  6.767   1.00 14.82 ? 114 ARG   A CA   1 
ATOM   801  C  C    . ARG   A 1 110 ? 26.965  -7.310  7.931   1.00 14.09 ? 114 ARG   A C    1 
ATOM   802  O  O    . ARG   A 1 110 ? 27.642  -8.335  7.862   1.00 15.18 ? 114 ARG   A O    1 
ATOM   803  C  CB   . ARG   A 1 110 ? 26.860  -6.723  5.481   1.00 15.58 ? 114 ARG   A CB   1 
ATOM   804  C  CG   . ARG   A 1 110 ? 25.874  -6.777  4.325   1.00 17.80 ? 114 ARG   A CG   1 
ATOM   805  C  CD   . ARG   A 1 110 ? 26.396  -7.209  3.015   1.00 17.64 ? 114 ARG   A CD   1 
ATOM   806  N  NE   . ARG   A 1 110 ? 27.228  -8.410  3.066   1.00 15.32 ? 114 ARG   A NE   1 
ATOM   807  C  CZ   . ARG   A 1 110 ? 26.863  -9.657  2.811   1.00 14.79 ? 114 ARG   A CZ   1 
ATOM   808  N  NH1  . ARG   A 1 110 ? 25.600  -9.986  2.677   1.00 15.37 ? 114 ARG   A NH1  1 
ATOM   809  N  NH2  . ARG   A 1 110 ? 27.792  -10.582 2.670   1.00 14.11 ? 114 ARG   A NH2  1 
ATOM   810  N  N    . GLN   A 1 111 ? 26.975  -6.507  9.000   1.00 13.77 ? 115 GLN   A N    1 
ATOM   811  C  CA   . GLN   A 1 111 ? 27.881  -6.742  10.112  1.00 13.95 ? 115 GLN   A CA   1 
ATOM   812  C  C    . GLN   A 1 111 ? 27.103  -7.264  11.315  1.00 14.44 ? 115 GLN   A C    1 
ATOM   813  O  O    . GLN   A 1 111 ? 26.033  -6.760  11.622  1.00 16.12 ? 115 GLN   A O    1 
ATOM   814  C  CB   . GLN   A 1 111 ? 28.580  -5.457  10.542  1.00 14.12 ? 115 GLN   A CB   1 
ATOM   815  C  CG   . GLN   A 1 111 ? 29.061  -4.577  9.393   1.00 13.47 ? 115 GLN   A CG   1 
ATOM   816  C  CD   . GLN   A 1 111 ? 29.892  -5.309  8.365   1.00 13.22 ? 115 GLN   A CD   1 
ATOM   817  O  OE1  . GLN   A 1 111 ? 30.706  -6.193  8.675   1.00 13.71 ? 115 GLN   A OE1  1 
ATOM   818  N  NE2  . GLN   A 1 111 ? 29.717  -4.905  7.117   1.00 13.12 ? 115 GLN   A NE2  1 
ATOM   819  N  N    . PRO   A 1 112 ? 27.638  -8.234  12.075  1.00 14.68 ? 116 PRO   A N    1 
ATOM   820  C  CA   . PRO   A 1 112 ? 26.976  -8.660  13.308  1.00 14.61 ? 116 PRO   A CA   1 
ATOM   821  C  C    . PRO   A 1 112 ? 26.919  -7.541  14.336  1.00 14.38 ? 116 PRO   A C    1 
ATOM   822  O  O    . PRO   A 1 112 ? 27.874  -6.783  14.498  1.00 14.35 ? 116 PRO   A O    1 
ATOM   823  C  CB   . PRO   A 1 112 ? 27.767  -9.829  13.851  1.00 16.08 ? 116 PRO   A CB   1 
ATOM   824  C  CG   . PRO   A 1 112 ? 29.022  -9.850  13.050  1.00 17.15 ? 116 PRO   A CG   1 
ATOM   825  C  CD   . PRO   A 1 112 ? 28.853  -9.008  11.787  1.00 15.61 ? 116 PRO   A CD   1 
ATOM   826  N  N    . GLN   A 1 113 ? 25.800  -7.510  15.053  1.00 15.21 ? 117 GLN   A N    1 
ATOM   827  C  CA   . GLN   A 1 113 ? 25.566  -6.526  16.092  1.00 15.18 ? 117 GLN   A CA   1 
ATOM   828  C  C    . GLN   A 1 113 ? 25.921  -7.125  17.447  1.00 15.09 ? 117 GLN   A C    1 
ATOM   829  O  O    . GLN   A 1 113 ? 25.819  -8.342  17.640  1.00 15.49 ? 117 GLN   A O    1 
ATOM   830  C  CB   . GLN   A 1 113 ? 24.092  -6.133  16.109  1.00 17.23 ? 117 GLN   A CB   1 
ATOM   831  C  CG   . GLN   A 1 113 ? 23.689  -5.257  14.935  1.00 19.99 ? 117 GLN   A CG   1 
ATOM   832  C  CD   . GLN   A 1 113 ? 22.327  -4.635  15.116  1.00 24.36 ? 117 GLN   A CD   1 
ATOM   833  O  OE1  . GLN   A 1 113 ? 22.197  -3.481  15.535  1.00 28.68 ? 117 GLN   A OE1  1 
ATOM   834  N  NE2  . GLN   A 1 113 ? 21.298  -5.425  14.873  1.00 28.62 ? 117 GLN   A NE2  1 
ATOM   835  N  N    . PRO   A 1 114 ? 26.258  -6.300  18.458  1.00 15.54 ? 118 PRO   A N    1 
ATOM   836  C  CA   . PRO   A 1 114 ? 26.357  -4.841  18.322  1.00 14.98 ? 118 PRO   A CA   1 
ATOM   837  C  C    . PRO   A 1 114 ? 27.513  -4.331  17.465  1.00 14.28 ? 118 PRO   A C    1 
ATOM   838  O  O    . PRO   A 1 114 ? 28.592  -4.910  17.480  1.00 15.09 ? 118 PRO   A O    1 
ATOM   839  C  CB   . PRO   A 1 114 ? 26.518  -4.347  19.767  1.00 16.36 ? 118 PRO   A CB   1 
ATOM   840  C  CG   . PRO   A 1 114 ? 26.092  -5.495  20.627  1.00 16.34 ? 118 PRO   A CG   1 
ATOM   841  C  CD   . PRO   A 1 114 ? 26.398  -6.744  19.851  1.00 16.12 ? 118 PRO   A CD   1 
ATOM   842  N  N    . TRP   A 1 115 ? 27.235  -3.227  16.760  1.00 13.86 ? 119 TRP   A N    1 
ATOM   843  C  CA   . TRP   A 1 115 ? 28.187  -2.464  15.970  1.00 15.08 ? 119 TRP   A CA   1 
ATOM   844  C  C    . TRP   A 1 115 ? 28.785  -1.350  16.820  1.00 13.75 ? 119 TRP   A C    1 
ATOM   845  O  O    . TRP   A 1 115 ? 28.022  -0.638  17.464  1.00 14.17 ? 119 TRP   A O    1 
ATOM   846  C  CB   . TRP   A 1 115 ? 27.467  -1.755  14.802  1.00 16.48 ? 119 TRP   A CB   1 
ATOM   847  C  CG   . TRP   A 1 115 ? 26.577  -2.561  13.895  1.00 16.60 ? 119 TRP   A CG   1 
ATOM   848  C  CD1  . TRP   A 1 115 ? 26.786  -3.812  13.414  1.00 16.82 ? 119 TRP   A CD1  1 
ATOM   849  C  CD2  . TRP   A 1 115 ? 25.320  -2.117  13.331  1.00 17.53 ? 119 TRP   A CD2  1 
ATOM   850  N  NE1  . TRP   A 1 115 ? 25.757  -4.177  12.593  1.00 18.20 ? 119 TRP   A NE1  1 
ATOM   851  C  CE2  . TRP   A 1 115 ? 24.833  -3.168  12.527  1.00 18.76 ? 119 TRP   A CE2  1 
ATOM   852  C  CE3  . TRP   A 1 115 ? 24.552  -0.951  13.443  1.00 19.71 ? 119 TRP   A CE3  1 
ATOM   853  C  CZ2  . TRP   A 1 115 ? 23.624  -3.084  11.834  1.00 19.30 ? 119 TRP   A CZ2  1 
ATOM   854  C  CZ3  . TRP   A 1 115 ? 23.351  -0.874  12.764  1.00 20.28 ? 119 TRP   A CZ3  1 
ATOM   855  C  CH2  . TRP   A 1 115 ? 22.903  -1.918  11.957  1.00 19.96 ? 119 TRP   A CH2  1 
ATOM   856  N  N    . CYS   A 1 116 ? 30.096  -1.102  16.701  1.00 12.65 ? 120 CYS   A N    1 
ATOM   857  C  CA   . CYS   A 1 116 ? 30.698  0.054   17.347  1.00 13.14 ? 120 CYS   A CA   1 
ATOM   858  C  C    . CYS   A 1 116 ? 31.558  0.832   16.357  1.00 12.71 ? 120 CYS   A C    1 
ATOM   859  O  O    . CYS   A 1 116 ? 32.573  0.319   15.902  1.00 12.32 ? 120 CYS   A O    1 
ATOM   860  C  CB   . CYS   A 1 116 ? 31.528  -0.353  18.557  1.00 14.31 ? 120 CYS   A CB   1 
ATOM   861  S  SG   . CYS   A 1 116 ? 32.044  1.052   19.571  1.00 16.47 ? 120 CYS   A SG   1 
ATOM   862  N  N    . LEU   A 1 117 ? 31.147  2.072   16.061  1.00 12.71 ? 121 LEU   A N    1 
ATOM   863  C  CA   . LEU   A 1 117 ? 31.962  2.981   15.268  1.00 12.76 ? 121 LEU   A CA   1 
ATOM   864  C  C    . LEU   A 1 117 ? 33.165  3.422   16.100  1.00 12.60 ? 121 LEU   A C    1 
ATOM   865  O  O    . LEU   A 1 117 ? 33.025  3.747   17.278  1.00 14.19 ? 121 LEU   A O    1 
ATOM   866  C  CB   . LEU   A 1 117 ? 31.158  4.211   14.855  1.00 14.03 ? 121 LEU   A CB   1 
ATOM   867  C  CG   . LEU   A 1 117 ? 29.951  3.955   13.958  1.00 16.22 ? 121 LEU   A CG   1 
ATOM   868  C  CD1  . LEU   A 1 117 ? 29.094  5.208   13.909  1.00 17.59 ? 121 LEU   A CD1  1 
ATOM   869  C  CD2  . LEU   A 1 117 ? 30.406  3.571   12.569  1.00 16.92 ? 121 LEU   A CD2  1 
ATOM   870  N  N    . VAL   A 1 118 ? 34.339  3.453   15.475  1.00 12.32 ? 122 VAL   A N    1 
ATOM   871  C  CA   . VAL   A 1 118 ? 35.571  3.864   16.131  1.00 12.08 ? 122 VAL   A CA   1 
ATOM   872  C  C    . VAL   A 1 118 ? 36.212  4.939   15.264  1.00 11.94 ? 122 VAL   A C    1 
ATOM   873  O  O    . VAL   A 1 118 ? 36.565  4.660   14.129  1.00 11.75 ? 122 VAL   A O    1 
ATOM   874  C  CB   . VAL   A 1 118 ? 36.536  2.679   16.335  1.00 13.01 ? 122 VAL   A CB   1 
ATOM   875  C  CG1  . VAL   A 1 118 ? 37.830  3.120   16.998  1.00 13.48 ? 122 VAL   A CG1  1 
ATOM   876  C  CG2  . VAL   A 1 118 ? 35.870  1.551   17.104  1.00 13.42 ? 122 VAL   A CG2  1 
ATOM   877  N  N    . ALA   A 1 119 ? 36.343  6.158   15.796  1.00 11.63 ? 123 ALA   A N    1 
ATOM   878  C  CA   . ALA   A 1 119 ? 36.912  7.265   15.043  1.00 12.00 ? 123 ALA   A CA   1 
ATOM   879  C  C    . ALA   A 1 119 ? 37.816  8.105   15.935  1.00 12.16 ? 123 ALA   A C    1 
ATOM   880  O  O    . ALA   A 1 119 ? 37.544  8.291   17.124  1.00 12.71 ? 123 ALA   A O    1 
ATOM   881  C  CB   . ALA   A 1 119 ? 35.813  8.106   14.430  1.00 12.10 ? 123 ALA   A CB   1 
ATOM   882  N  N    . HIS   A 1 120 ? 38.883  8.639   15.340  1.00 12.77 ? 124 HIS   A N    1 
ATOM   883  C  CA   . HIS   A 1 120 ? 39.893  9.369   16.085  1.00 13.81 ? 124 HIS   A CA   1 
ATOM   884  C  C    . HIS   A 1 120 ? 39.481  10.837  16.236  1.00 13.61 ? 124 HIS   A C    1 
ATOM   885  O  O    . HIS   A 1 120 ? 39.362  11.560  15.258  1.00 14.05 ? 124 HIS   A O    1 
ATOM   886  C  CB   . HIS   A 1 120 ? 41.242  9.211   15.387  1.00 15.20 ? 124 HIS   A CB   1 
ATOM   887  C  CG   . HIS   A 1 120 ? 42.372  9.431   16.331  1.00 17.18 ? 124 HIS   A CG   1 
ATOM   888  N  ND1  . HIS   A 1 120 ? 42.695  8.529   17.320  1.00 18.99 ? 124 HIS   A ND1  1 
ATOM   889  C  CD2  . HIS   A 1 120 ? 43.224  10.452  16.461  1.00 18.63 ? 124 HIS   A CD2  1 
ATOM   890  C  CE1  . HIS   A 1 120 ? 43.741  8.989   17.995  1.00 19.59 ? 124 HIS   A CE1  1 
ATOM   891  N  NE2  . HIS   A 1 120 ? 44.070  10.167  17.498  1.00 19.83 ? 124 HIS   A NE2  1 
ATOM   892  N  N    . ASN   A 1 121 ? 39.275  11.288  17.478  1.00 13.70 ? 125 ASN   A N    1 
ATOM   893  C  CA   . ASN   A 1 121 ? 38.584  12.549  17.721  1.00 14.29 ? 125 ASN   A CA   1 
ATOM   894  C  C    . ASN   A 1 121 ? 37.186  12.486  17.106  1.00 13.44 ? 125 ASN   A C    1 
ATOM   895  O  O    . ASN   A 1 121 ? 36.626  13.500  16.700  1.00 13.23 ? 125 ASN   A O    1 
ATOM   896  C  CB   . ASN   A 1 121 ? 39.367  13.769  17.229  1.00 15.81 ? 125 ASN   A CB   1 
ATOM   897  C  CG   . ASN   A 1 121 ? 39.875  14.647  18.347  1.00 18.21 ? 125 ASN   A CG   1 
ATOM   898  O  OD1  . ASN   A 1 121 ? 39.247  14.755  19.405  1.00 20.13 ? 125 ASN   A OD1  1 
ATOM   899  N  ND2  . ASN   A 1 121 ? 41.028  15.259  18.137  1.00 20.93 ? 125 ASN   A ND2  1 
ATOM   900  N  N    . GLY   A 1 122 ? 36.577  11.296  17.117  1.00 13.02 ? 126 GLY   A N    1 
ATOM   901  C  CA   . GLY   A 1 122 ? 35.241  11.130  16.583  1.00 12.89 ? 126 GLY   A CA   1 
ATOM   902  C  C    . GLY   A 1 122 ? 34.195  11.991  17.292  1.00 12.77 ? 126 GLY   A C    1 
ATOM   903  O  O    . GLY   A 1 122 ? 33.209  12.371  16.677  1.00 12.55 ? 126 GLY   A O    1 
ATOM   904  N  N    . ASP   A 1 123 ? 34.363  12.254  18.591  1.00 13.68 ? 127 ASP   A N    1 
ATOM   905  C  CA   . ASP   A 1 123 ? 33.379  13.035  19.321  1.00 14.85 ? 127 ASP   A CA   1 
ATOM   906  C  C    . ASP   A 1 123 ? 33.358  14.484  18.837  1.00 14.99 ? 127 ASP   A C    1 
ATOM   907  O  O    . ASP   A 1 123 ? 32.332  15.149  18.942  1.00 15.97 ? 127 ASP   A O    1 
ATOM   908  C  CB   . ASP   A 1 123 ? 33.638  12.992  20.817  1.00 16.14 ? 127 ASP   A CB   1 
ATOM   909  C  CG   . ASP   A 1 123 ? 33.356  11.661  21.487  1.00 18.40 ? 127 ASP   A CG   1 
ATOM   910  O  OD1  . ASP   A 1 123 ? 32.866  10.753  20.796  1.00 20.43 ? 127 ASP   A OD1  1 
ATOM   911  O  OD2  . ASP   A 1 123 ? 33.590  11.569  22.708  1.00 22.15 ? 127 ASP   A OD2  1 
ATOM   912  N  N    . ARG   A 1 124 ? 34.489  14.964  18.317  1.00 14.86 ? 128 ARG   A N    1 
ATOM   913  C  CA   . ARG   A 1 124 ? 34.591  16.324  17.803  1.00 14.91 ? 128 ARG   A CA   1 
ATOM   914  C  C    . ARG   A 1 124 ? 34.222  16.410  16.319  1.00 14.33 ? 128 ARG   A C    1 
ATOM   915  O  O    . ARG   A 1 124 ? 33.602  17.392  15.898  1.00 14.25 ? 128 ARG   A O    1 
ATOM   916  C  CB   . ARG   A 1 124 ? 36.030  16.809  17.986  1.00 16.24 ? 128 ARG   A CB   1 
ATOM   917  C  CG   . ARG   A 1 124 ? 36.228  18.250  17.554  1.00 17.62 ? 128 ARG   A CG   1 
ATOM   918  C  CD   . ARG   A 1 124 ? 37.682  18.615  17.648  1.00 19.73 ? 128 ARG   A CD   1 
ATOM   919  N  NE   . ARG   A 1 124 ? 38.159  18.657  19.033  1.00 21.59 ? 128 ARG   A NE   1 
ATOM   920  C  CZ   . ARG   A 1 124 ? 39.415  18.939  19.331  1.00 24.05 ? 128 ARG   A CZ   1 
ATOM   921  N  NH1  . ARG   A 1 124 ? 39.779  19.030  20.594  1.00 26.28 ? 128 ARG   A NH1  1 
ATOM   922  N  NH2  . ARG   A 1 124 ? 40.288  19.159  18.356  1.00 24.04 ? 128 ARG   A NH2  1 
ATOM   923  N  N    . TYR   A 1 125 ? 34.658  15.421  15.523  1.00 13.32 ? 129 TYR   A N    1 
ATOM   924  C  CA   . TYR   A 1 125 ? 34.554  15.505  14.071  1.00 12.90 ? 129 TYR   A CA   1 
ATOM   925  C  C    . TYR   A 1 125 ? 33.500  14.543  13.518  1.00 11.84 ? 129 TYR   A C    1 
ATOM   926  O  O    . TYR   A 1 125 ? 32.410  14.958  13.138  1.00 12.30 ? 129 TYR   A O    1 
ATOM   927  C  CB   . TYR   A 1 125 ? 35.941  15.250  13.483  1.00 13.10 ? 129 TYR   A CB   1 
ATOM   928  C  CG   . TYR   A 1 125 ? 37.025  16.232  13.902  1.00 13.67 ? 129 TYR   A CG   1 
ATOM   929  C  CD1  . TYR   A 1 125 ? 36.820  17.604  13.872  1.00 14.26 ? 129 TYR   A CD1  1 
ATOM   930  C  CD2  . TYR   A 1 125 ? 38.265  15.776  14.326  1.00 14.60 ? 129 TYR   A CD2  1 
ATOM   931  C  CE1  . TYR   A 1 125 ? 37.821  18.490  14.233  1.00 15.37 ? 129 TYR   A CE1  1 
ATOM   932  C  CE2  . TYR   A 1 125 ? 39.272  16.649  14.692  1.00 15.70 ? 129 TYR   A CE2  1 
ATOM   933  C  CZ   . TYR   A 1 125 ? 39.045  18.012  14.658  1.00 16.19 ? 129 TYR   A CZ   1 
ATOM   934  O  OH   . TYR   A 1 125 ? 40.027  18.893  15.043  1.00 19.68 ? 129 TYR   A OH   1 
ATOM   935  N  N    . ASP   A 1 126 ? 33.841  13.253  13.434  1.00 11.64 ? 130 ASP   A N    1 
ATOM   936  C  CA   . ASP   A 1 126 ? 33.101  12.322  12.595  1.00 11.59 ? 130 ASP   A CA   1 
ATOM   937  C  C    . ASP   A 1 126 ? 31.689  12.064  13.107  1.00 11.58 ? 130 ASP   A C    1 
ATOM   938  O  O    . ASP   A 1 126 ? 30.748  12.023  12.314  1.00 12.09 ? 130 ASP   A O    1 
ATOM   939  C  CB   . ASP   A 1 126 ? 33.882  11.032  12.459  1.00 11.59 ? 130 ASP   A CB   1 
ATOM   940  C  CG   . ASP   A 1 126 ? 35.350  11.280  12.157  1.00 12.08 ? 130 ASP   A CG   1 
ATOM   941  O  OD1  . ASP   A 1 126 ? 36.096  11.583  13.114  1.00 13.15 ? 130 ASP   A OD1  1 
ATOM   942  O  OD2  . ASP   A 1 126 ? 35.708  11.259  10.962  1.00 12.89 ? 130 ASP   A OD2  1 
ATOM   943  N  N    . PHE   A 1 127 ? 31.541  11.839  14.417  1.00 11.54 ? 131 PHE   A N    1 
ATOM   944  C  CA   . PHE   A 1 127 ? 30.243  11.429  14.932  1.00 12.09 ? 131 PHE   A CA   1 
ATOM   945  C  C    . PHE   A 1 127 ? 29.223  12.564  14.832  1.00 12.20 ? 131 PHE   A C    1 
ATOM   946  O  O    . PHE   A 1 127 ? 28.124  12.349  14.319  1.00 12.33 ? 131 PHE   A O    1 
ATOM   947  C  CB   . PHE   A 1 127 ? 30.353  10.887  16.354  1.00 12.52 ? 131 PHE   A CB   1 
ATOM   948  C  CG   . PHE   A 1 127 ? 31.295  9.707   16.529  1.00 12.66 ? 131 PHE   A CG   1 
ATOM   949  C  CD1  . PHE   A 1 127 ? 31.495  8.773   15.515  1.00 13.40 ? 131 PHE   A CD1  1 
ATOM   950  C  CD2  . PHE   A 1 127 ? 31.961  9.519   17.741  1.00 13.37 ? 131 PHE   A CD2  1 
ATOM   951  C  CE1  . PHE   A 1 127 ? 32.331  7.688   15.713  1.00 13.32 ? 131 PHE   A CE1  1 
ATOM   952  C  CE2  . PHE   A 1 127 ? 32.809  8.437   17.919  1.00 13.58 ? 131 PHE   A CE2  1 
ATOM   953  C  CZ   . PHE   A 1 127 ? 32.987  7.524   16.906  1.00 14.01 ? 131 PHE   A CZ   1 
ATOM   954  N  N    . PRO   A 1 128 ? 29.490  13.792  15.331  1.00 12.69 ? 132 PRO   A N    1 
ATOM   955  C  CA   . PRO   A 1 128 ? 28.493  14.861  15.215  1.00 13.09 ? 132 PRO   A CA   1 
ATOM   956  C  C    . PRO   A 1 128 ? 28.202  15.267  13.775  1.00 12.87 ? 132 PRO   A C    1 
ATOM   957  O  O    . PRO   A 1 128 ? 27.077  15.660  13.464  1.00 12.64 ? 132 PRO   A O    1 
ATOM   958  C  CB   . PRO   A 1 128 ? 29.052  16.007  16.046  1.00 13.77 ? 132 PRO   A CB   1 
ATOM   959  C  CG   . PRO   A 1 128 ? 30.503  15.701  16.188  1.00 14.20 ? 132 PRO   A CG   1 
ATOM   960  C  CD   . PRO   A 1 128 ? 30.663  14.200  16.115  1.00 13.42 ? 132 PRO   A CD   1 
ATOM   961  N  N    . LEU   A 1 129 ? 29.206  15.164  12.888  1.00 12.17 ? 133 LEU   A N    1 
ATOM   962  C  CA   . LEU   A 1 129 ? 28.956  15.513  11.498  1.00 12.16 ? 133 LEU   A CA   1 
ATOM   963  C  C    . LEU   A 1 129 ? 28.039  14.475  10.843  1.00 12.14 ? 133 LEU   A C    1 
ATOM   964  O  O    . LEU   A 1 129 ? 27.112  14.835  10.105  1.00 12.25 ? 133 LEU   A O    1 
ATOM   965  C  CB   . LEU   A 1 129 ? 30.238  15.721  10.699  1.00 11.99 ? 133 LEU   A CB   1 
ATOM   966  C  CG   . LEU   A 1 129 ? 30.005  16.118  9.234   1.00 12.27 ? 133 LEU   A CG   1 
ATOM   967  C  CD1  . LEU   A 1 129 ? 29.061  17.317  9.077   1.00 12.59 ? 133 LEU   A CD1  1 
ATOM   968  C  CD2  . LEU   A 1 129 ? 31.321  16.411  8.566   1.00 12.70 ? 133 LEU   A CD2  1 
ATOM   969  N  N    . LEU   A 1 130 ? 28.286  13.183  11.094  1.00 12.04 ? 134 LEU   A N    1 
ATOM   970  C  CA   . LEU   A 1 130 ? 27.407  12.153  10.562  1.00 12.88 ? 134 LEU   A CA   1 
ATOM   971  C  C    . LEU   A 1 130 ? 25.979  12.384  11.063  1.00 13.35 ? 134 LEU   A C    1 
ATOM   972  O  O    . LEU   A 1 130 ? 25.026  12.338  10.283  1.00 13.93 ? 134 LEU   A O    1 
ATOM   973  C  CB   . LEU   A 1 130 ? 27.919  10.752  10.889  1.00 13.66 ? 134 LEU   A CB   1 
ATOM   974  C  CG   . LEU   A 1 130 ? 27.031  9.598   10.416  1.00 14.64 ? 134 LEU   A CG   1 
ATOM   975  C  CD1  . LEU   A 1 130 ? 26.839  9.626   8.909   1.00 15.80 ? 134 LEU   A CD1  1 
ATOM   976  C  CD2  . LEU   A 1 130 ? 27.616  8.274   10.871  1.00 15.15 ? 134 LEU   A CD2  1 
ATOM   977  N  N    . GLN   A 1 131 ? 25.824  12.668  12.364  1.00 13.58 ? 135 GLN   A N    1 
ATOM   978  C  CA   . GLN   A 1 131 ? 24.500  12.930  12.910  1.00 14.93 ? 135 GLN   A CA   1 
ATOM   979  C  C    . GLN   A 1 131 ? 23.846  14.143  12.251  1.00 14.70 ? 135 GLN   A C    1 
ATOM   980  O  O    . GLN   A 1 131 ? 22.636  14.139  12.018  1.00 16.20 ? 135 GLN   A O    1 
ATOM   981  C  CB   . GLN   A 1 131 ? 24.573  13.087  14.428  1.00 16.65 ? 135 GLN   A CB   1 
ATOM   982  C  CG   . GLN   A 1 131 ? 24.798  11.774  15.162  1.00 19.11 ? 135 GLN   A CG   1 
ATOM   983  C  CD   . GLN   A 1 131 ? 23.568  10.887  15.227  1.00 21.73 ? 135 GLN   A CD   1 
ATOM   984  O  OE1  . GLN   A 1 131 ? 22.837  10.678  14.248  1.00 23.20 ? 135 GLN   A OE1  1 
ATOM   985  N  NE2  . GLN   A 1 131 ? 23.338  10.332  16.406  1.00 23.79 ? 135 GLN   A NE2  1 
ATOM   986  N  N    . ALA   A 1 132 ? 24.629  15.184  11.960  1.00 14.39 ? 136 ALA   A N    1 
ATOM   987  C  CA   . ALA   A 1 132 ? 24.087  16.377  11.320  1.00 14.20 ? 136 ALA   A CA   1 
ATOM   988  C  C    . ALA   A 1 132 ? 23.604  16.083  9.902   1.00 14.75 ? 136 ALA   A C    1 
ATOM   989  O  O    . ALA   A 1 132 ? 22.541  16.557  9.506   1.00 15.48 ? 136 ALA   A O    1 
ATOM   990  C  CB   . ALA   A 1 132 ? 25.111  17.485  11.306  1.00 13.65 ? 136 ALA   A CB   1 
ATOM   991  N  N    . GLU   A 1 133 ? 24.400  15.326  9.134   1.00 14.30 ? 137 GLU   A N    1 
ATOM   992  C  CA   . GLU   A 1 133 ? 24.013  14.996  7.766   1.00 15.10 ? 137 GLU   A CA   1 
ATOM   993  C  C    . GLU   A 1 133 ? 22.716  14.182  7.775   1.00 15.58 ? 137 GLU   A C    1 
ATOM   994  O  O    . GLU   A 1 133 ? 21.825  14.410  6.956   1.00 16.89 ? 137 GLU   A O    1 
ATOM   995  C  CB   . GLU   A 1 133 ? 25.131  14.267  7.020   1.00 15.85 ? 137 GLU   A CB   1 
ATOM   996  C  CG   . GLU   A 1 133 ? 26.363  15.124  6.734   1.00 16.09 ? 137 GLU   A CG   1 
ATOM   997  C  CD   . GLU   A 1 133 ? 26.314  16.001  5.486   1.00 16.90 ? 137 GLU   A CD   1 
ATOM   998  O  OE1  . GLU   A 1 133 ? 25.216  16.232  4.935   1.00 18.78 ? 137 GLU   A OE1  1 
ATOM   999  O  OE2  . GLU   A 1 133 ? 27.388  16.473  5.052   1.00 17.17 ? 137 GLU   A OE2  1 
ATOM   1000 N  N    . LEU   A 1 134 ? 22.593  13.234  8.708   1.00 16.32 ? 138 LEU   A N    1 
ATOM   1001 C  CA   . LEU   A 1 134 ? 21.386  12.422  8.798   1.00 17.62 ? 138 LEU   A CA   1 
ATOM   1002 C  C    . LEU   A 1 134 ? 20.186  13.285  9.192   1.00 18.80 ? 138 LEU   A C    1 
ATOM   1003 O  O    . LEU   A 1 134 ? 19.089  13.112  8.660   1.00 19.93 ? 138 LEU   A O    1 
ATOM   1004 C  CB   . LEU   A 1 134 ? 21.609  11.268  9.772   1.00 18.31 ? 138 LEU   A CB   1 
ATOM   1005 C  CG   . LEU   A 1 134 ? 22.602  10.200  9.304   1.00 19.56 ? 138 LEU   A CG   1 
ATOM   1006 C  CD1  . LEU   A 1 134 ? 22.858  9.205   10.419  1.00 20.59 ? 138 LEU   A CD1  1 
ATOM   1007 C  CD2  . LEU   A 1 134 ? 22.125  9.480   8.043   1.00 19.98 ? 138 LEU   A CD2  1 
ATOM   1008 N  N    . ALA   A 1 135 ? 20.393  14.215  10.130  1.00 18.56 ? 139 ALA   A N    1 
ATOM   1009 C  CA   . ALA   A 1 135 ? 19.312  15.078  10.583  1.00 20.37 ? 139 ALA   A CA   1 
ATOM   1010 C  C    . ALA   A 1 135 ? 18.776  15.954  9.451   1.00 21.21 ? 139 ALA   A C    1 
ATOM   1011 O  O    . ALA   A 1 135 ? 17.571  16.195  9.380   1.00 22.33 ? 139 ALA   A O    1 
ATOM   1012 C  CB   . ALA   A 1 135 ? 19.776  15.916  11.751  1.00 20.78 ? 139 ALA   A CB   1 
ATOM   1013 N  N    A MET   A 1 136 ? 19.671  16.426  8.571   0.50 21.36 ? 140 MET   A N    1 
ATOM   1014 N  N    B MET   A 1 136 ? 19.668  16.430  8.574   0.50 20.80 ? 140 MET   A N    1 
ATOM   1015 C  CA   A MET   A 1 136 ? 19.279  17.260  7.443   0.50 22.71 ? 140 MET   A CA   1 
ATOM   1016 C  CA   B MET   A 1 136 ? 19.258  17.263  7.453   0.50 21.80 ? 140 MET   A CA   1 
ATOM   1017 C  C    A MET   A 1 136 ? 18.389  16.491  6.465   0.50 23.18 ? 140 MET   A C    1 
ATOM   1018 C  C    B MET   A 1 136 ? 18.339  16.487  6.510   0.50 22.64 ? 140 MET   A C    1 
ATOM   1019 O  O    A MET   A 1 136 ? 17.651  17.109  5.700   0.50 24.40 ? 140 MET   A O    1 
ATOM   1020 O  O    B MET   A 1 136 ? 17.501  17.095  5.845   0.50 23.96 ? 140 MET   A O    1 
ATOM   1021 C  CB   A MET   A 1 136 ? 20.499  17.799  6.684   0.50 24.33 ? 140 MET   A CB   1 
ATOM   1022 C  CB   B MET   A 1 136 ? 20.467  17.819  6.690   0.50 22.44 ? 140 MET   A CB   1 
ATOM   1023 C  CG   A MET   A 1 136 ? 21.270  18.895  7.406   0.50 27.29 ? 140 MET   A CG   1 
ATOM   1024 C  CG   B MET   A 1 136 ? 21.307  18.794  7.500   0.50 24.25 ? 140 MET   A CG   1 
ATOM   1025 S  SD   A MET   A 1 136 ? 20.480  20.519  7.426   0.50 33.62 ? 140 MET   A SD   1 
ATOM   1026 S  SD   B MET   A 1 136 ? 20.404  20.211  8.161   0.50 27.69 ? 140 MET   A SD   1 
ATOM   1027 C  CE   A MET   A 1 136 ? 19.752  20.628  9.066   0.50 33.84 ? 140 MET   A CE   1 
ATOM   1028 C  CE   B MET   A 1 136 ? 19.835  20.909  6.601   0.50 27.91 ? 140 MET   A CE   1 
ATOM   1029 N  N    . LEU   A 1 137 ? 18.466  15.152  6.483   1.00 22.57 ? 141 LEU   A N    1 
ATOM   1030 C  CA   . LEU   A 1 137 ? 17.613  14.305  5.654   1.00 24.13 ? 141 LEU   A CA   1 
ATOM   1031 C  C    . LEU   A 1 137 ? 16.329  13.910  6.381   1.00 26.78 ? 141 LEU   A C    1 
ATOM   1032 O  O    . LEU   A 1 137 ? 15.519  13.167  5.822   1.00 28.74 ? 141 LEU   A O    1 
ATOM   1033 C  CB   . LEU   A 1 137 ? 18.359  13.039  5.237   1.00 23.49 ? 141 LEU   A CB   1 
ATOM   1034 C  CG   . LEU   A 1 137 ? 19.613  13.240  4.389   1.00 24.29 ? 141 LEU   A CG   1 
ATOM   1035 C  CD1  . LEU   A 1 137 ? 20.255  11.884  4.147   1.00 24.00 ? 141 LEU   A CD1  1 
ATOM   1036 C  CD2  . LEU   A 1 137 ? 19.306  13.932  3.074   1.00 25.59 ? 141 LEU   A CD2  1 
ATOM   1037 N  N    . GLY   A 1 138 ? 16.158  14.363  7.629   1.00 28.24 ? 142 GLY   A N    1 
ATOM   1038 C  CA   . GLY   A 1 138 ? 15.037  13.934  8.450   1.00 30.30 ? 142 GLY   A CA   1 
ATOM   1039 C  C    . GLY   A 1 138 ? 15.175  12.464  8.839   1.00 30.97 ? 142 GLY   A C    1 
ATOM   1040 O  O    . GLY   A 1 138 ? 14.177  11.773  9.046   1.00 36.10 ? 142 GLY   A O    1 
ATOM   1041 N  N    . LEU   A 1 139 ? 16.427  12.004  8.935   1.00 31.79 ? 143 LEU   A N    1 
ATOM   1042 C  CA   . LEU   A 1 139 ? 16.734  10.632  9.290   1.00 32.56 ? 143 LEU   A CA   1 
ATOM   1043 C  C    . LEU   A 1 139 ? 17.465  10.616  10.628  1.00 34.37 ? 143 LEU   A C    1 
ATOM   1044 O  O    . LEU   A 1 139 ? 18.354  9.795   10.841  1.00 32.73 ? 143 LEU   A O    1 
ATOM   1045 C  CB   . LEU   A 1 139 ? 17.558  9.989   8.174   1.00 32.05 ? 143 LEU   A CB   1 
ATOM   1046 C  CG   . LEU   A 1 139 ? 16.854  9.857   6.820   1.00 33.64 ? 143 LEU   A CG   1 
ATOM   1047 C  CD1  . LEU   A 1 139 ? 17.803  9.311   5.774   1.00 34.55 ? 143 LEU   A CD1  1 
ATOM   1048 C  CD2  . LEU   A 1 139 ? 15.620  8.977   6.916   1.00 34.25 ? 143 LEU   A CD2  1 
ATOM   1049 N  N    . THR   A 1 140 ? 17.090  11.536  11.527  1.00 36.96 ? 144 THR   A N    1 
ATOM   1050 C  CA   . THR   A 1 140 ? 17.576  11.464  12.894  1.00 40.14 ? 144 THR   A CA   1 
ATOM   1051 C  C    . THR   A 1 140 ? 17.240  10.064  13.393  1.00 41.04 ? 144 THR   A C    1 
ATOM   1052 O  O    . THR   A 1 140 ? 16.142  9.572   13.145  1.00 42.75 ? 144 THR   A O    1 
ATOM   1053 C  CB   . THR   A 1 140 ? 16.958  12.543  13.787  1.00 41.77 ? 144 THR   A CB   1 
ATOM   1054 O  OG1  . THR   A 1 140 ? 15.558  12.284  13.830  1.00 46.39 ? 144 THR   A OG1  1 
ATOM   1055 C  CG2  . THR   A 1 140 ? 17.202  13.953  13.280  1.00 40.71 ? 144 THR   A CG2  1 
ATOM   1056 N  N    . SER   A 1 141 ? 18.219  9.408   14.021  1.00 42.49 ? 145 SER   A N    1 
ATOM   1057 C  CA   . SER   A 1 141 ? 18.014  8.122   14.672  1.00 42.83 ? 145 SER   A CA   1 
ATOM   1058 C  C    . SER   A 1 141 ? 18.166  6.951   13.700  1.00 39.76 ? 145 SER   A C    1 
ATOM   1059 O  O    . SER   A 1 141 ? 18.004  5.803   14.110  1.00 37.57 ? 145 SER   A O    1 
ATOM   1060 C  CB   . SER   A 1 141 ? 16.678  8.049   15.379  1.00 42.85 ? 145 SER   A CB   1 
ATOM   1061 O  OG   . SER   A 1 141 ? 15.656  7.574   14.512  1.00 43.16 ? 145 SER   A OG   1 
ATOM   1062 N  N    . ALA   A 1 142 ? 18.489  7.224   12.428  1.00 36.99 ? 146 ALA   A N    1 
ATOM   1063 C  CA   . ALA   A 1 142 ? 18.607  6.154   11.445  1.00 35.82 ? 146 ALA   A CA   1 
ATOM   1064 C  C    . ALA   A 1 142 ? 19.705  5.172   11.848  1.00 35.16 ? 146 ALA   A C    1 
ATOM   1065 O  O    . ALA   A 1 142 ? 19.591  3.982   11.583  1.00 36.80 ? 146 ALA   A O    1 
ATOM   1066 C  CB   . ALA   A 1 142 ? 18.867  6.722   10.070  1.00 36.49 ? 146 ALA   A CB   1 
ATOM   1067 N  N    . LEU   A 1 143 ? 20.772  5.684   12.476  1.00 34.37 ? 147 LEU   A N    1 
ATOM   1068 C  CA   . LEU   A 1 143 ? 21.939  4.881   12.805  1.00 35.50 ? 147 LEU   A CA   1 
ATOM   1069 C  C    . LEU   A 1 143 ? 22.038  4.651   14.308  1.00 35.34 ? 147 LEU   A C    1 
ATOM   1070 O  O    . LEU   A 1 143 ? 23.107  4.302   14.796  1.00 37.25 ? 147 LEU   A O    1 
ATOM   1071 C  CB   . LEU   A 1 143 ? 23.199  5.583   12.302  1.00 36.28 ? 147 LEU   A CB   1 
ATOM   1072 C  CG   . LEU   A 1 143 ? 23.821  5.026   11.023  1.00 40.59 ? 147 LEU   A CG   1 
ATOM   1073 C  CD1  . LEU   A 1 143 ? 22.904  5.072   9.815   1.00 41.48 ? 147 LEU   A CD1  1 
ATOM   1074 C  CD2  . LEU   A 1 143 ? 25.089  5.813   10.778  1.00 41.74 ? 147 LEU   A CD2  1 
ATOM   1075 N  N    . ASP   A 1 144 ? 20.935  4.818   15.041  1.00 37.24 ? 148 ASP   A N    1 
ATOM   1076 C  CA   . ASP   A 1 144 ? 21.018  4.830   16.493  1.00 38.94 ? 148 ASP   A CA   1 
ATOM   1077 C  C    . ASP   A 1 144 ? 20.999  3.408   17.060  1.00 37.72 ? 148 ASP   A C    1 
ATOM   1078 O  O    . ASP   A 1 144 ? 21.086  3.232   18.271  1.00 38.45 ? 148 ASP   A O    1 
ATOM   1079 C  CB   . ASP   A 1 144 ? 19.997  5.785   17.089  1.00 40.69 ? 148 ASP   A CB   1 
ATOM   1080 C  CG   . ASP   A 1 144 ? 20.327  7.272   16.991  1.00 40.09 ? 148 ASP   A CG   1 
ATOM   1081 O  OD1  . ASP   A 1 144 ? 21.360  7.638   16.363  1.00 38.22 ? 148 ASP   A OD1  1 
ATOM   1082 O  OD2  . ASP   A 1 144 ? 19.548  8.066   17.554  1.00 42.15 ? 148 ASP   A OD2  1 
ATOM   1083 N  N    . GLY   A 1 145 ? 20.928  2.390   16.192  1.00 36.20 ? 149 GLY   A N    1 
ATOM   1084 C  CA   . GLY   A 1 145 ? 21.233  1.030   16.610  1.00 32.26 ? 149 GLY   A CA   1 
ATOM   1085 C  C    . GLY   A 1 145 ? 22.714  0.857   16.963  1.00 29.31 ? 149 GLY   A C    1 
ATOM   1086 O  O    . GLY   A 1 145 ? 23.100  -0.076  17.671  1.00 28.41 ? 149 GLY   A O    1 
ATOM   1087 N  N    . ALA   A 1 146 ? 23.541  1.772   16.454  1.00 25.97 ? 150 ALA   A N    1 
ATOM   1088 C  CA   . ALA   A 1 146 ? 24.980  1.681   16.603  1.00 21.11 ? 150 ALA   A CA   1 
ATOM   1089 C  C    . ALA   A 1 146 ? 25.441  2.186   17.966  1.00 18.45 ? 150 ALA   A C    1 
ATOM   1090 O  O    . ALA   A 1 146 ? 24.768  2.973   18.637  1.00 20.41 ? 150 ALA   A O    1 
ATOM   1091 C  CB   . ALA   A 1 146 ? 25.664  2.479   15.512  1.00 22.47 ? 150 ALA   A CB   1 
ATOM   1092 N  N    . PHE   A 1 147 ? 26.662  1.776   18.303  1.00 15.90 ? 151 PHE   A N    1 
ATOM   1093 C  CA   . PHE   A 1 147 ? 27.432  2.326   19.401  1.00 15.09 ? 151 PHE   A CA   1 
ATOM   1094 C  C    . PHE   A 1 147 ? 28.633  3.047   18.809  1.00 14.05 ? 151 PHE   A C    1 
ATOM   1095 O  O    . PHE   A 1 147 ? 28.907  2.925   17.608  1.00 13.70 ? 151 PHE   A O    1 
ATOM   1096 C  CB   . PHE   A 1 147 ? 27.863  1.214   20.367  1.00 15.58 ? 151 PHE   A CB   1 
ATOM   1097 C  CG   . PHE   A 1 147 ? 26.645  0.547   20.982  1.00 16.70 ? 151 PHE   A CG   1 
ATOM   1098 C  CD1  . PHE   A 1 147 ? 26.032  1.081   22.110  1.00 18.10 ? 151 PHE   A CD1  1 
ATOM   1099 C  CD2  . PHE   A 1 147 ? 26.056  -0.549  20.368  1.00 17.60 ? 151 PHE   A CD2  1 
ATOM   1100 C  CE1  . PHE   A 1 147 ? 24.888  0.493   22.627  1.00 18.59 ? 151 PHE   A CE1  1 
ATOM   1101 C  CE2  . PHE   A 1 147 ? 24.904  -1.116  20.885  1.00 17.74 ? 151 PHE   A CE2  1 
ATOM   1102 C  CZ   . PHE   A 1 147 ? 24.330  -0.596  22.014  1.00 19.07 ? 151 PHE   A CZ   1 
ATOM   1103 N  N    . CYS   A 1 148 ? 29.340  3.808   19.652  1.00 14.30 ? 152 CYS   A N    1 
ATOM   1104 C  CA   . CYS   A 1 148 ? 30.518  4.514   19.185  1.00 14.99 ? 152 CYS   A CA   1 
ATOM   1105 C  C    . CYS   A 1 148 ? 31.520  4.720   20.313  1.00 14.99 ? 152 CYS   A C    1 
ATOM   1106 O  O    . CYS   A 1 148 ? 31.154  4.759   21.495  1.00 16.02 ? 152 CYS   A O    1 
ATOM   1107 C  CB   . CYS   A 1 148 ? 30.175  5.831   18.505  1.00 16.06 ? 152 CYS   A CB   1 
ATOM   1108 S  SG   . CYS   A 1 148 ? 29.483  7.072   19.618  1.00 17.89 ? 152 CYS   A SG   1 
ATOM   1109 N  N    A VAL   A 1 149 ? 32.787  4.831   19.917  0.50 14.65 ? 153 VAL   A N    1 
ATOM   1110 N  N    B VAL   A 1 149 ? 32.792  4.837   19.904  0.50 14.48 ? 153 VAL   A N    1 
ATOM   1111 C  CA   A VAL   A 1 149 ? 33.853  5.202   20.825  0.50 15.57 ? 153 VAL   A CA   1 
ATOM   1112 C  CA   B VAL   A 1 149 ? 33.926  5.103   20.774  0.50 15.28 ? 153 VAL   A CA   1 
ATOM   1113 C  C    A VAL   A 1 149 ? 34.819  6.097   20.065  0.50 14.85 ? 153 VAL   A C    1 
ATOM   1114 C  C    B VAL   A 1 149 ? 34.860  6.071   20.056  0.50 14.70 ? 153 VAL   A C    1 
ATOM   1115 O  O    A VAL   A 1 149 ? 35.049  5.919   18.866  0.50 14.83 ? 153 VAL   A O    1 
ATOM   1116 O  O    B VAL   A 1 149 ? 35.120  5.915   18.859  0.50 14.64 ? 153 VAL   A O    1 
ATOM   1117 C  CB   A VAL   A 1 149 ? 34.604  3.998   21.421  0.50 16.79 ? 153 VAL   A CB   1 
ATOM   1118 C  CB   B VAL   A 1 149 ? 34.693  3.820   21.164  0.50 16.19 ? 153 VAL   A CB   1 
ATOM   1119 C  CG1  A VAL   A 1 149 ? 33.674  3.040   22.147  0.50 17.73 ? 153 VAL   A CG1  1 
ATOM   1120 C  CG1  B VAL   A 1 149 ? 36.169  4.092   21.450  0.50 16.51 ? 153 VAL   A CG1  1 
ATOM   1121 C  CG2  A VAL   A 1 149 ? 35.420  3.265   20.368  0.50 16.51 ? 153 VAL   A CG2  1 
ATOM   1122 C  CG2  B VAL   A 1 149 ? 34.069  3.123   22.362  0.50 16.80 ? 153 VAL   A CG2  1 
ATOM   1123 N  N    . ASP   A 1 150 ? 35.385  7.050   20.803  1.00 14.82 ? 154 ASP   A N    1 
ATOM   1124 C  CA   . ASP   A 1 150 ? 36.424  7.930   20.302  1.00 15.44 ? 154 ASP   A CA   1 
ATOM   1125 C  C    . ASP   A 1 150 ? 37.777  7.312   20.637  1.00 15.56 ? 154 ASP   A C    1 
ATOM   1126 O  O    . ASP   A 1 150 ? 38.100  7.110   21.805  1.00 16.10 ? 154 ASP   A O    1 
ATOM   1127 C  CB   . ASP   A 1 150 ? 36.275  9.310   20.921  1.00 16.51 ? 154 ASP   A CB   1 
ATOM   1128 C  CG   . ASP   A 1 150 ? 37.149  10.391  20.310  1.00 17.85 ? 154 ASP   A CG   1 
ATOM   1129 O  OD1  . ASP   A 1 150 ? 38.286  10.063  19.901  1.00 18.12 ? 154 ASP   A OD1  1 
ATOM   1130 O  OD2  . ASP   A 1 150 ? 36.688  11.557  20.282  1.00 19.72 ? 154 ASP   A OD2  1 
ATOM   1131 N  N    . SER   A 1 151 ? 38.571  6.997   19.610  1.00 15.66 ? 155 SER   A N    1 
ATOM   1132 C  CA   . SER   A 1 151 ? 39.842  6.326   19.821  1.00 16.22 ? 155 SER   A CA   1 
ATOM   1133 C  C    . SER   A 1 151 ? 40.876  7.192   20.546  1.00 17.51 ? 155 SER   A C    1 
ATOM   1134 O  O    . SER   A 1 151 ? 41.801  6.651   21.134  1.00 18.27 ? 155 SER   A O    1 
ATOM   1135 C  CB   . SER   A 1 151 ? 40.404  5.781   18.532  1.00 15.86 ? 155 SER   A CB   1 
ATOM   1136 O  OG   . SER   A 1 151 ? 40.536  6.791   17.546  1.00 15.76 ? 155 SER   A OG   1 
ATOM   1137 N  N    A ILE   A 1 152 ? 40.733  8.521   20.514  0.50 18.19 ? 156 ILE   A N    1 
ATOM   1138 N  N    B ILE   A 1 152 ? 40.767  8.527   20.505  0.50 18.63 ? 156 ILE   A N    1 
ATOM   1139 C  CA   A ILE   A 1 152 ? 41.685  9.350   21.238  0.50 18.96 ? 156 ILE   A CA   1 
ATOM   1140 C  CA   B ILE   A 1 152 ? 41.717  9.329   21.268  0.50 19.74 ? 156 ILE   A CA   1 
ATOM   1141 C  C    A ILE   A 1 152 ? 41.495  9.119   22.741  0.50 19.87 ? 156 ILE   A C    1 
ATOM   1142 C  C    B ILE   A 1 152 ? 41.505  9.071   22.759  0.50 20.31 ? 156 ILE   A C    1 
ATOM   1143 O  O    A ILE   A 1 152 ? 42.474  9.002   23.475  0.50 20.90 ? 156 ILE   A O    1 
ATOM   1144 O  O    B ILE   A 1 152 ? 42.473  8.931   23.502  0.50 21.24 ? 156 ILE   A O    1 
ATOM   1145 C  CB   A ILE   A 1 152 ? 41.594  10.827  20.809  0.50 19.58 ? 156 ILE   A CB   1 
ATOM   1146 C  CB   B ILE   A 1 152 ? 41.651  10.827  20.927  0.50 21.24 ? 156 ILE   A CB   1 
ATOM   1147 C  CG1  A ILE   A 1 152 ? 42.911  11.551  21.068  0.50 19.76 ? 156 ILE   A CG1  1 
ATOM   1148 C  CG1  B ILE   A 1 152 ? 42.180  11.076  19.534  0.50 21.84 ? 156 ILE   A CG1  1 
ATOM   1149 C  CG2  A ILE   A 1 152 ? 40.399  11.541  21.441  0.50 19.32 ? 156 ILE   A CG2  1 
ATOM   1150 C  CG2  B ILE   A 1 152 ? 42.420  11.650  21.960  0.50 21.57 ? 156 ILE   A CG2  1 
ATOM   1151 C  CD1  A ILE   A 1 152 ? 42.974  12.951  20.483  0.50 19.83 ? 156 ILE   A CD1  1 
ATOM   1152 C  CD1  B ILE   A 1 152 ? 41.926  12.473  19.011  0.50 22.57 ? 156 ILE   A CD1  1 
ATOM   1153 N  N    . THR   A 1 153 ? 40.239  8.970   23.184  1.00 19.42 ? 157 THR   A N    1 
ATOM   1154 C  CA   . THR   A 1 153 ? 39.934  8.657   24.575  1.00 20.48 ? 157 THR   A CA   1 
ATOM   1155 C  C    . THR   A 1 153 ? 40.491  7.275   24.928  1.00 20.56 ? 157 THR   A C    1 
ATOM   1156 O  O    . THR   A 1 153 ? 41.139  7.092   25.963  1.00 22.32 ? 157 THR   A O    1 
ATOM   1157 C  CB   . THR   A 1 153 ? 38.423  8.728   24.804  1.00 20.71 ? 157 THR   A CB   1 
ATOM   1158 O  OG1  . THR   A 1 153 ? 37.962  9.968   24.265  1.00 21.51 ? 157 THR   A OG1  1 
ATOM   1159 C  CG2  . THR   A 1 153 ? 38.065  8.613   26.278  1.00 21.63 ? 157 THR   A CG2  1 
ATOM   1160 N  N    . ALA   A 1 154 ? 40.238  6.292   24.061  1.00 20.29 ? 158 ALA   A N    1 
ATOM   1161 C  CA   . ALA   A 1 154 ? 40.713  4.931   24.272  1.00 20.68 ? 158 ALA   A CA   1 
ATOM   1162 C  C    . ALA   A 1 154 ? 42.234  4.892   24.390  1.00 20.97 ? 158 ALA   A C    1 
ATOM   1163 O  O    . ALA   A 1 154 ? 42.771  4.282   25.309  1.00 22.59 ? 158 ALA   A O    1 
ATOM   1164 C  CB   . ALA   A 1 154 ? 40.260  4.039   23.150  1.00 19.85 ? 158 ALA   A CB   1 
ATOM   1165 N  N    . LEU   A 1 155 ? 42.930  5.534   23.450  1.00 21.67 ? 159 LEU   A N    1 
ATOM   1166 C  CA   . LEU   A 1 155 ? 44.375  5.387   23.371  1.00 22.98 ? 159 LEU   A CA   1 
ATOM   1167 C  C    . LEU   A 1 155 ? 45.070  6.156   24.498  1.00 25.06 ? 159 LEU   A C    1 
ATOM   1168 O  O    . LEU   A 1 155 ? 46.112  5.715   24.984  1.00 25.29 ? 159 LEU   A O    1 
ATOM   1169 C  CB   . LEU   A 1 155 ? 44.831  5.789   21.970  1.00 24.50 ? 159 LEU   A CB   1 
ATOM   1170 C  CG   . LEU   A 1 155 ? 44.295  4.893   20.848  1.00 26.53 ? 159 LEU   A CG   1 
ATOM   1171 C  CD1  . LEU   A 1 155 ? 44.396  5.575   19.490  1.00 26.91 ? 159 LEU   A CD1  1 
ATOM   1172 C  CD2  . LEU   A 1 155 ? 45.012  3.562   20.840  1.00 27.57 ? 159 LEU   A CD2  1 
ATOM   1173 N  N    . LYS   A 1 156 ? 44.485  7.278   24.938  1.00 26.02 ? 160 LYS   A N    1 
ATOM   1174 C  CA   . LYS   A 1 156 ? 44.971  7.972   26.124  1.00 28.94 ? 160 LYS   A CA   1 
ATOM   1175 C  C    . LYS   A 1 156 ? 44.903  7.047   27.337  1.00 30.58 ? 160 LYS   A C    1 
ATOM   1176 O  O    . LYS   A 1 156 ? 45.870  6.943   28.089  1.00 31.64 ? 160 LYS   A O    1 
ATOM   1177 C  CB   . LYS   A 1 156 ? 44.188  9.261   26.398  1.00 31.62 ? 160 LYS   A CB   1 
ATOM   1178 C  CG   . LYS   A 1 156 ? 44.578  10.433  25.518  1.00 33.16 ? 160 LYS   A CG   1 
ATOM   1179 C  CD   . LYS   A 1 156 ? 43.846  11.727  25.857  1.00 36.10 ? 160 LYS   A CD   1 
ATOM   1180 C  CE   . LYS   A 1 156 ? 44.254  12.845  24.951  1.00 37.75 ? 160 LYS   A CE   1 
ATOM   1181 N  NZ   . LYS   A 1 156 ? 43.456  14.057  25.159  1.00 39.98 ? 160 LYS   A NZ   1 
ATOM   1182 N  N    . ALA   A 1 157 ? 43.759  6.375   27.518  1.00 31.21 ? 161 ALA   A N    1 
ATOM   1183 C  CA   . ALA   A 1 157 ? 43.569  5.473   28.645  1.00 32.66 ? 161 ALA   A CA   1 
ATOM   1184 C  C    . ALA   A 1 157 ? 44.555  4.307   28.588  1.00 32.63 ? 161 ALA   A C    1 
ATOM   1185 O  O    . ALA   A 1 157 ? 45.121  3.921   29.609  1.00 34.99 ? 161 ALA   A O    1 
ATOM   1186 C  CB   . ALA   A 1 157 ? 42.142  4.984   28.682  1.00 33.11 ? 161 ALA   A CB   1 
ATOM   1187 N  N    . LEU   A 1 158 ? 44.780  3.758   27.391  1.00 32.00 ? 162 LEU   A N    1 
ATOM   1188 C  CA   . LEU   A 1 158 ? 45.612  2.575   27.250  1.00 32.87 ? 162 LEU   A CA   1 
ATOM   1189 C  C    . LEU   A 1 158 ? 47.089  2.922   27.444  1.00 34.35 ? 162 LEU   A C    1 
ATOM   1190 O  O    . LEU   A 1 158 ? 47.822  2.149   28.057  1.00 33.32 ? 162 LEU   A O    1 
ATOM   1191 C  CB   . LEU   A 1 158 ? 45.320  1.914   25.908  1.00 34.92 ? 162 LEU   A CB   1 
ATOM   1192 C  CG   . LEU   A 1 158 ? 43.912  1.315   25.796  1.00 37.32 ? 162 LEU   A CG   1 
ATOM   1193 C  CD1  . LEU   A 1 158 ? 43.486  1.153   24.358  1.00 38.39 ? 162 LEU   A CD1  1 
ATOM   1194 C  CD2  . LEU   A 1 158 ? 43.831  -0.005  26.538  1.00 38.46 ? 162 LEU   A CD2  1 
ATOM   1195 N  N    . GLU   A 1 159 ? 47.520  4.090   26.953  1.00 35.46 ? 163 GLU   A N    1 
ATOM   1196 C  CA   . GLU   A 1 159 ? 48.901  4.519   27.130  1.00 38.97 ? 163 GLU   A CA   1 
ATOM   1197 C  C    . GLU   A 1 159 ? 49.169  4.783   28.614  1.00 40.32 ? 163 GLU   A C    1 
ATOM   1198 O  O    . GLU   A 1 159 ? 50.259  4.487   29.100  1.00 41.97 ? 163 GLU   A O    1 
ATOM   1199 C  CB   . GLU   A 1 159 ? 49.257  5.700   26.221  1.00 42.41 ? 163 GLU   A CB   1 
ATOM   1200 C  CG   . GLU   A 1 159 ? 49.631  5.275   24.799  1.00 47.07 ? 163 GLU   A CG   1 
ATOM   1201 C  CD   . GLU   A 1 159 ? 50.300  6.321   23.916  1.00 49.85 ? 163 GLU   A CD   1 
ATOM   1202 O  OE1  . GLU   A 1 159 ? 49.600  7.156   23.297  1.00 53.56 ? 163 GLU   A OE1  1 
ATOM   1203 O  OE2  . GLU   A 1 159 ? 51.548  6.295   23.841  1.00 52.82 ? 163 GLU   A OE2  1 
ATOM   1204 N  N    . ARG   A 1 160 ? 48.164  5.295   29.342  1.00 40.25 ? 164 ARG   A N    1 
ATOM   1205 C  CA   . ARG   A 1 160 ? 48.306  5.550   30.772  1.00 42.12 ? 164 ARG   A CA   1 
ATOM   1206 C  C    . ARG   A 1 160 ? 48.460  4.240   31.547  1.00 44.31 ? 164 ARG   A C    1 
ATOM   1207 O  O    . ARG   A 1 160 ? 49.236  4.171   32.497  1.00 46.04 ? 164 ARG   A O    1 
ATOM   1208 C  CB   . ARG   A 1 160 ? 47.106  6.333   31.319  1.00 43.08 ? 164 ARG   A CB   1 
ATOM   1209 N  N    . ALA   A 1 161 ? 47.706  3.208   31.151  1.00 44.66 ? 165 ALA   A N    1 
ATOM   1210 C  CA   . ALA   A 1 161 ? 47.765  1.906   31.801  1.00 45.31 ? 165 ALA   A CA   1 
ATOM   1211 C  C    . ALA   A 1 161 ? 49.119  1.234   31.563  1.00 47.10 ? 165 ALA   A C    1 
ATOM   1212 O  O    . ALA   A 1 161 ? 49.580  0.465   32.405  1.00 46.59 ? 165 ALA   A O    1 
ATOM   1213 C  CB   . ALA   A 1 161 ? 46.631  1.028   31.313  1.00 44.81 ? 165 ALA   A CB   1 
ATOM   1214 N  N    . SER   A 1 162 ? 49.738  1.516   30.409  1.00 48.61 ? 166 SER   A N    1 
ATOM   1215 C  CA   . SER   A 1 162 ? 50.987  0.882   30.013  1.00 51.56 ? 166 SER   A CA   1 
ATOM   1216 C  C    . SER   A 1 162 ? 52.174  1.534   30.722  1.00 54.18 ? 166 SER   A C    1 
ATOM   1217 O  O    . SER   A 1 162 ? 53.125  0.843   31.080  1.00 59.32 ? 166 SER   A O    1 
ATOM   1218 C  CB   . SER   A 1 162 ? 51.162  0.915   28.511  1.00 51.43 ? 166 SER   A CB   1 
ATOM   1219 N  N    . SER   A 1 163 ? 52.117  2.860   30.909  1.00 56.44 ? 167 SER   A N    1 
ATOM   1220 C  CA   . SER   A 1 163 ? 53.187  3.601   31.560  1.00 58.84 ? 167 SER   A CA   1 
ATOM   1221 C  C    . SER   A 1 163 ? 52.736  4.049   32.959  1.00 60.83 ? 167 SER   A C    1 
ATOM   1222 O  O    . SER   A 1 163 ? 52.203  5.177   33.060  1.00 63.89 ? 167 SER   A O    1 
ATOM   1223 C  CB   . SER   A 1 163 ? 53.629  4.776   30.720  1.00 59.44 ? 167 SER   A CB   1 
ATOM   1224 N  N    . LYS   A 1 171 ? 52.155  15.051  25.643  1.00 48.06 ? 175 LYS   A N    1 
ATOM   1225 C  CA   . LYS   A 1 171 ? 52.461  14.583  24.263  1.00 46.47 ? 175 LYS   A CA   1 
ATOM   1226 C  C    . LYS   A 1 171 ? 51.209  14.714  23.399  1.00 42.46 ? 175 LYS   A C    1 
ATOM   1227 O  O    . LYS   A 1 171 ? 50.102  14.824  23.923  1.00 42.21 ? 175 LYS   A O    1 
ATOM   1228 C  CB   . LYS   A 1 171 ? 52.999  13.146  24.283  1.00 49.04 ? 175 LYS   A CB   1 
ATOM   1229 C  CG   . LYS   A 1 171 ? 52.047  12.084  24.812  1.00 51.36 ? 175 LYS   A CG   1 
ATOM   1230 C  CD   . LYS   A 1 171 ? 52.707  10.739  25.096  1.00 54.50 ? 175 LYS   A CD   1 
ATOM   1231 C  CE   . LYS   A 1 171 ? 53.391  10.689  26.421  1.00 56.29 ? 175 LYS   A CE   1 
ATOM   1232 N  NZ   . LYS   A 1 171 ? 54.044  9.395   26.629  1.00 58.07 ? 175 LYS   A NZ   1 
ATOM   1233 N  N    . SER   A 1 172 ? 51.414  14.712  22.075  1.00 38.41 ? 176 SER   A N    1 
ATOM   1234 C  CA   . SER   A 1 172 ? 50.334  14.814  21.104  1.00 34.47 ? 176 SER   A CA   1 
ATOM   1235 C  C    . SER   A 1 172 ? 49.621  13.472  20.973  1.00 32.18 ? 176 SER   A C    1 
ATOM   1236 O  O    . SER   A 1 172 ? 50.259  12.424  20.949  1.00 32.20 ? 176 SER   A O    1 
ATOM   1237 C  CB   . SER   A 1 172 ? 50.858  15.269  19.762  1.00 35.03 ? 176 SER   A CB   1 
ATOM   1238 O  OG   . SER   A 1 172 ? 49.850  15.214  18.760  1.00 34.87 ? 176 SER   A OG   1 
ATOM   1239 N  N    . TYR   A 1 173 ? 48.294  13.527  20.838  1.00 30.18 ? 177 TYR   A N    1 
ATOM   1240 C  CA   . TYR   A 1 173 ? 47.512  12.337  20.559  1.00 28.43 ? 177 TYR   A CA   1 
ATOM   1241 C  C    . TYR   A 1 173 ? 46.851  12.452  19.189  1.00 26.85 ? 177 TYR   A C    1 
ATOM   1242 O  O    . TYR   A 1 173 ? 45.865  11.772  18.932  1.00 25.16 ? 177 TYR   A O    1 
ATOM   1243 C  CB   . TYR   A 1 173 ? 46.526  12.089  21.702  1.00 30.40 ? 177 TYR   A CB   1 
ATOM   1244 C  CG   . TYR   A 1 173 ? 47.231  11.649  22.974  1.00 34.65 ? 177 TYR   A CG   1 
ATOM   1245 C  CD1  . TYR   A 1 173 ? 47.536  10.312  23.203  1.00 37.06 ? 177 TYR   A CD1  1 
ATOM   1246 C  CD2  . TYR   A 1 173 ? 47.631  12.580  23.924  1.00 37.37 ? 177 TYR   A CD2  1 
ATOM   1247 C  CE1  . TYR   A 1 173 ? 48.194  9.911   24.355  1.00 38.83 ? 177 TYR   A CE1  1 
ATOM   1248 C  CE2  . TYR   A 1 173 ? 48.290  12.192  25.078  1.00 39.24 ? 177 TYR   A CE2  1 
ATOM   1249 C  CZ   . TYR   A 1 173 ? 48.572  10.854  25.294  1.00 39.84 ? 177 TYR   A CZ   1 
ATOM   1250 O  OH   . TYR   A 1 173 ? 49.222  10.476  26.435  1.00 43.29 ? 177 TYR   A OH   1 
ATOM   1251 N  N    . SER   A 1 174 ? 47.440  13.252  18.291  1.00 25.27 ? 178 SER   A N    1 
ATOM   1252 C  CA   . SER   A 1 174 ? 47.073  13.185  16.886  1.00 24.61 ? 178 SER   A CA   1 
ATOM   1253 C  C    . SER   A 1 174 ? 47.361  11.782  16.352  1.00 22.39 ? 178 SER   A C    1 
ATOM   1254 O  O    . SER   A 1 174 ? 48.204  11.058  16.873  1.00 22.59 ? 178 SER   A O    1 
ATOM   1255 C  CB   . SER   A 1 174 ? 47.789  14.224  16.067  1.00 26.27 ? 178 SER   A CB   1 
ATOM   1256 O  OG   . SER   A 1 174 ? 49.136  13.844  15.823  1.00 28.27 ? 178 SER   A OG   1 
ATOM   1257 N  N    . LEU   A 1 175 ? 46.647  11.402  15.294  1.00 21.65 ? 179 LEU   A N    1 
ATOM   1258 C  CA   . LEU   A 1 175 ? 46.782  10.078  14.713  1.00 21.32 ? 179 LEU   A CA   1 
ATOM   1259 C  C    . LEU   A 1 175 ? 48.237  9.825   14.322  1.00 22.56 ? 179 LEU   A C    1 
ATOM   1260 O  O    . LEU   A 1 175 ? 48.803  8.783   14.652  1.00 23.00 ? 179 LEU   A O    1 
ATOM   1261 C  CB   . LEU   A 1 175 ? 45.836  10.007  13.518  1.00 21.50 ? 179 LEU   A CB   1 
ATOM   1262 C  CG   . LEU   A 1 175 ? 45.655  8.636   12.870  1.00 22.17 ? 179 LEU   A CG   1 
ATOM   1263 C  CD1  . LEU   A 1 175 ? 44.899  7.711   13.799  1.00 22.40 ? 179 LEU   A CD1  1 
ATOM   1264 C  CD2  . LEU   A 1 175 ? 44.934  8.795   11.537  1.00 22.40 ? 179 LEU   A CD2  1 
ATOM   1265 N  N    . GLY   A 1 176 ? 48.835  10.800  13.626  1.00 23.94 ? 180 GLY   A N    1 
ATOM   1266 C  CA   . GLY   A 1 176 ? 50.206  10.695  13.153  1.00 25.50 ? 180 GLY   A CA   1 
ATOM   1267 C  C    . GLY   A 1 176 ? 51.225  10.610  14.292  1.00 26.87 ? 180 GLY   A C    1 
ATOM   1268 O  O    . GLY   A 1 176 ? 52.192  9.862   14.193  1.00 28.82 ? 180 GLY   A O    1 
ATOM   1269 N  N    . SER   A 1 177 ? 51.006  11.376  15.369  1.00 27.36 ? 181 SER   A N    1 
ATOM   1270 C  CA   . SER   A 1 177 ? 51.899  11.361  16.519  1.00 27.77 ? 181 SER   A CA   1 
ATOM   1271 C  C    . SER   A 1 177 ? 51.897  9.991   17.193  1.00 26.93 ? 181 SER   A C    1 
ATOM   1272 O  O    . SER   A 1 177 ? 52.954  9.479   17.567  1.00 27.70 ? 181 SER   A O    1 
ATOM   1273 C  CB   . SER   A 1 177 ? 51.531  12.434  17.510  1.00 28.28 ? 181 SER   A CB   1 
ATOM   1274 O  OG   . SER   A 1 177 ? 51.704  13.728  16.953  1.00 31.42 ? 181 SER   A OG   1 
ATOM   1275 N  N    . ILE   A 1 178 ? 50.701  9.418   17.386  1.00 25.05 ? 182 ILE   A N    1 
ATOM   1276 C  CA   . ILE   A 1 178 ? 50.580  8.124   18.038  1.00 24.91 ? 182 ILE   A CA   1 
ATOM   1277 C  C    . ILE   A 1 178 ? 51.249  7.078   17.151  1.00 25.47 ? 182 ILE   A C    1 
ATOM   1278 O  O    . ILE   A 1 178 ? 52.015  6.252   17.634  1.00 26.16 ? 182 ILE   A O    1 
ATOM   1279 C  CB   . ILE   A 1 178 ? 49.113  7.763   18.340  1.00 23.97 ? 182 ILE   A CB   1 
ATOM   1280 C  CG1  . ILE   A 1 178 ? 48.451  8.763   19.294  1.00 23.99 ? 182 ILE   A CG1  1 
ATOM   1281 C  CG2  . ILE   A 1 178 ? 49.003  6.330   18.866  1.00 24.43 ? 182 ILE   A CG2  1 
ATOM   1282 C  CD1  . ILE   A 1 178 ? 46.947  8.597   19.423  1.00 24.26 ? 182 ILE   A CD1  1 
ATOM   1283 N  N    . TYR   A 1 179 ? 50.945  7.121   15.849  1.00 25.58 ? 183 TYR   A N    1 
ATOM   1284 C  CA   . TYR   A 1 179 ? 51.443  6.128   14.914  1.00 26.59 ? 183 TYR   A CA   1 
ATOM   1285 C  C    . TYR   A 1 179 ? 52.970  6.115   14.954  1.00 29.56 ? 183 TYR   A C    1 
ATOM   1286 O  O    . TYR   A 1 179 ? 53.569  5.049   15.063  1.00 31.36 ? 183 TYR   A O    1 
ATOM   1287 C  CB   . TYR   A 1 179 ? 50.884  6.407   13.514  1.00 26.28 ? 183 TYR   A CB   1 
ATOM   1288 C  CG   . TYR   A 1 179 ? 51.130  5.305   12.494  1.00 26.57 ? 183 TYR   A CG   1 
ATOM   1289 C  CD1  . TYR   A 1 179 ? 52.377  5.145   11.902  1.00 27.72 ? 183 TYR   A CD1  1 
ATOM   1290 C  CD2  . TYR   A 1 179 ? 50.115  4.435   12.112  1.00 24.97 ? 183 TYR   A CD2  1 
ATOM   1291 C  CE1  . TYR   A 1 179 ? 52.610  4.154   10.963  1.00 27.16 ? 183 TYR   A CE1  1 
ATOM   1292 C  CE2  . TYR   A 1 179 ? 50.331  3.443   11.169  1.00 24.78 ? 183 TYR   A CE2  1 
ATOM   1293 C  CZ   . TYR   A 1 179 ? 51.584  3.301   10.597  1.00 26.04 ? 183 TYR   A CZ   1 
ATOM   1294 O  OH   . TYR   A 1 179 ? 51.822  2.334   9.669   1.00 26.69 ? 183 TYR   A OH   1 
ATOM   1295 N  N    . THR   A 1 180 ? 53.583  7.304   14.879  1.00 32.41 ? 184 THR   A N    1 
ATOM   1296 C  CA   . THR   A 1 180 ? 55.035  7.438   14.855  1.00 34.27 ? 184 THR   A CA   1 
ATOM   1297 C  C    . THR   A 1 180 ? 55.636  6.902   16.155  1.00 34.84 ? 184 THR   A C    1 
ATOM   1298 O  O    . THR   A 1 180 ? 56.652  6.213   16.130  1.00 38.04 ? 184 THR   A O    1 
ATOM   1299 C  CB   . THR   A 1 180 ? 55.410  8.900   14.606  1.00 36.10 ? 184 THR   A CB   1 
ATOM   1300 O  OG1  . THR   A 1 180 ? 54.829  9.260   13.357  1.00 39.30 ? 184 THR   A OG1  1 
ATOM   1301 C  CG2  . THR   A 1 180 ? 56.908  9.124   14.518  1.00 37.69 ? 184 THR   A CG2  1 
ATOM   1302 N  N    . ARG   A 1 181 ? 54.992  7.204   17.287  1.00 35.32 ? 185 ARG   A N    1 
ATOM   1303 C  CA   . ARG   A 1 181 ? 55.450  6.767   18.599  1.00 36.68 ? 185 ARG   A CA   1 
ATOM   1304 C  C    . ARG   A 1 181 ? 55.447  5.241   18.699  1.00 38.17 ? 185 ARG   A C    1 
ATOM   1305 O  O    . ARG   A 1 181 ? 56.392  4.651   19.222  1.00 40.44 ? 185 ARG   A O    1 
ATOM   1306 C  CB   . ARG   A 1 181 ? 54.530  7.437   19.625  1.00 39.34 ? 185 ARG   A CB   1 
ATOM   1307 C  CG   . ARG   A 1 181 ? 54.900  7.334   21.094  1.00 41.72 ? 185 ARG   A CG   1 
ATOM   1308 C  CD   . ARG   A 1 181 ? 54.409  8.550   21.875  1.00 40.66 ? 185 ARG   A CD   1 
ATOM   1309 N  NE   . ARG   A 1 181 ? 52.948  8.634   21.982  1.00 38.84 ? 185 ARG   A NE   1 
ATOM   1310 C  CZ   . ARG   A 1 181 ? 52.167  9.674   21.663  1.00 38.09 ? 185 ARG   A CZ   1 
ATOM   1311 N  NH1  . ARG   A 1 181 ? 52.656  10.766  21.096  1.00 37.87 ? 185 ARG   A NH1  1 
ATOM   1312 N  NH2  . ARG   A 1 181 ? 50.875  9.619   21.923  1.00 36.50 ? 185 ARG   A NH2  1 
ATOM   1313 N  N    . LEU   A 1 182 ? 54.386  4.604   18.185  1.00 37.94 ? 186 LEU   A N    1 
ATOM   1314 C  CA   . LEU   A 1 182 ? 54.199  3.169   18.332  1.00 38.75 ? 186 LEU   A CA   1 
ATOM   1315 C  C    . LEU   A 1 182 ? 55.100  2.412   17.361  1.00 40.30 ? 186 LEU   A C    1 
ATOM   1316 O  O    . LEU   A 1 182 ? 55.658  1.384   17.730  1.00 42.96 ? 186 LEU   A O    1 
ATOM   1317 C  CB   . LEU   A 1 182 ? 52.743  2.758   18.116  1.00 37.07 ? 186 LEU   A CB   1 
ATOM   1318 C  CG   . LEU   A 1 182 ? 51.714  3.256   19.137  1.00 37.85 ? 186 LEU   A CG   1 
ATOM   1319 C  CD1  . LEU   A 1 182 ? 50.361  2.667   18.777  1.00 37.46 ? 186 LEU   A CD1  1 
ATOM   1320 C  CD2  . LEU   A 1 182 ? 52.079  2.923   20.572  1.00 39.47 ? 186 LEU   A CD2  1 
ATOM   1321 N  N    . TYR   A 1 183 ? 55.204  2.897   16.116  1.00 40.64 ? 187 TYR   A N    1 
ATOM   1322 C  CA   . TYR   A 1 183 ? 55.799  2.111   15.046  1.00 42.43 ? 187 TYR   A CA   1 
ATOM   1323 C  C    . TYR   A 1 183 ? 57.128  2.699   14.582  1.00 48.01 ? 187 TYR   A C    1 
ATOM   1324 O  O    . TYR   A 1 183 ? 57.767  2.118   13.707  1.00 51.67 ? 187 TYR   A O    1 
ATOM   1325 C  CB   . TYR   A 1 183 ? 54.767  1.970   13.922  1.00 39.95 ? 187 TYR   A CB   1 
ATOM   1326 C  CG   . TYR   A 1 183 ? 53.588  1.104   14.342  1.00 35.56 ? 187 TYR   A CG   1 
ATOM   1327 C  CD1  . TYR   A 1 183 ? 53.799  -0.145  14.911  1.00 33.95 ? 187 TYR   A CD1  1 
ATOM   1328 C  CD2  . TYR   A 1 183 ? 52.277  1.554   14.227  1.00 32.20 ? 187 TYR   A CD2  1 
ATOM   1329 C  CE1  . TYR   A 1 183 ? 52.746  -0.938  15.321  1.00 31.90 ? 187 TYR   A CE1  1 
ATOM   1330 C  CE2  . TYR   A 1 183 ? 51.210  0.768   14.637  1.00 30.12 ? 187 TYR   A CE2  1 
ATOM   1331 C  CZ   . TYR   A 1 183 ? 51.451  -0.480  15.188  1.00 29.81 ? 187 TYR   A CZ   1 
ATOM   1332 O  OH   . TYR   A 1 183 ? 50.455  -1.303  15.604  1.00 28.73 ? 187 TYR   A OH   1 
ATOM   1333 N  N    . GLY   A 1 184 ? 57.545  3.826   15.177  1.00 50.86 ? 188 GLY   A N    1 
ATOM   1334 C  CA   . GLY   A 1 184 ? 58.852  4.408   14.913  1.00 53.37 ? 188 GLY   A CA   1 
ATOM   1335 C  C    . GLY   A 1 184 ? 58.987  4.922   13.480  1.00 55.73 ? 188 GLY   A C    1 
ATOM   1336 O  O    . GLY   A 1 184 ? 60.099  5.028   12.967  1.00 59.90 ? 188 GLY   A O    1 
ATOM   1337 N  N    . GLN   A 1 185 ? 57.856  5.266   12.852  1.00 55.77 ? 189 GLN   A N    1 
ATOM   1338 C  CA   . GLN   A 1 185 ? 57.832  5.670   11.455  1.00 57.85 ? 189 GLN   A CA   1 
ATOM   1339 C  C    . GLN   A 1 185 ? 56.484  6.313   11.144  1.00 57.87 ? 189 GLN   A C    1 
ATOM   1340 O  O    . GLN   A 1 185 ? 55.490  6.019   11.804  1.00 58.11 ? 189 GLN   A O    1 
ATOM   1341 C  CB   . GLN   A 1 185 ? 58.086  4.473   10.535  1.00 60.71 ? 189 GLN   A CB   1 
ATOM   1342 C  CG   . GLN   A 1 185 ? 57.086  3.330   10.696  1.00 61.74 ? 189 GLN   A CG   1 
ATOM   1343 C  CD   . GLN   A 1 185 ? 57.464  2.089   9.915   1.00 62.07 ? 189 GLN   A CD   1 
ATOM   1344 O  OE1  . GLN   A 1 185 ? 58.598  1.602   9.991   1.00 65.78 ? 189 GLN   A OE1  1 
ATOM   1345 N  NE2  . GLN   A 1 185 ? 56.523  1.565   9.144   1.00 59.40 ? 189 GLN   A NE2  1 
ATOM   1346 N  N    . SER   A 1 186 ? 56.459  7.179   10.126  1.00 59.44 ? 190 SER   A N    1 
ATOM   1347 C  CA   . SER   A 1 186 ? 55.249  7.893   9.751   1.00 60.47 ? 190 SER   A CA   1 
ATOM   1348 C  C    . SER   A 1 186 ? 54.287  6.946   9.030   1.00 59.20 ? 190 SER   A C    1 
ATOM   1349 O  O    . SER   A 1 186 ? 54.718  5.958   8.436   1.00 59.29 ? 190 SER   A O    1 
ATOM   1350 C  CB   . SER   A 1 186 ? 55.575  9.104   8.912   1.00 61.03 ? 190 SER   A CB   1 
ATOM   1351 N  N    . PRO   A 1 187 ? 52.955  7.195   9.083   1.00 57.46 ? 191 PRO   A N    1 
ATOM   1352 C  CA   . PRO   A 1 187 ? 51.985  6.358   8.368   1.00 55.42 ? 191 PRO   A CA   1 
ATOM   1353 C  C    . PRO   A 1 187 ? 51.996  6.586   6.855   1.00 53.45 ? 191 PRO   A C    1 
ATOM   1354 O  O    . PRO   A 1 187 ? 52.346  7.670   6.401   1.00 56.35 ? 191 PRO   A O    1 
ATOM   1355 C  CB   . PRO   A 1 187 ? 50.638  6.747   9.010   1.00 55.77 ? 191 PRO   A CB   1 
ATOM   1356 C  CG   . PRO   A 1 187 ? 50.847  8.169   9.493   1.00 56.52 ? 191 PRO   A CG   1 
ATOM   1357 C  CD   . PRO   A 1 187 ? 52.318  8.269   9.863   1.00 56.27 ? 191 PRO   A CD   1 
ATOM   1358 N  N    . PRO   A 1 188 ? 51.589  5.589   6.031   1.00 50.60 ? 192 PRO   A N    1 
ATOM   1359 C  CA   . PRO   A 1 188 ? 51.685  5.702   4.571   1.00 50.70 ? 192 PRO   A CA   1 
ATOM   1360 C  C    . PRO   A 1 188 ? 50.961  6.912   3.984   1.00 52.52 ? 192 PRO   A C    1 
ATOM   1361 O  O    . PRO   A 1 188 ? 51.584  7.756   3.339   1.00 53.65 ? 192 PRO   A O    1 
ATOM   1362 C  CB   . PRO   A 1 188 ? 51.072  4.384   4.052   1.00 50.15 ? 192 PRO   A CB   1 
ATOM   1363 C  CG   . PRO   A 1 188 ? 51.131  3.440   5.229   1.00 49.94 ? 192 PRO   A CG   1 
ATOM   1364 C  CD   . PRO   A 1 188 ? 50.996  4.312   6.461   1.00 49.95 ? 192 PRO   A CD   1 
ATOM   1365 N  N    . ASP   A 1 189 ? 49.644  6.973   4.231   1.00 52.63 ? 193 ASP   A N    1 
ATOM   1366 C  CA   . ASP   A 1 189 ? 48.735  7.898   3.571   1.00 50.74 ? 193 ASP   A CA   1 
ATOM   1367 C  C    . ASP   A 1 189 ? 48.000  8.712   4.633   1.00 48.07 ? 193 ASP   A C    1 
ATOM   1368 O  O    . ASP   A 1 189 ? 47.319  8.146   5.490   1.00 48.53 ? 193 ASP   A O    1 
ATOM   1369 C  CB   . ASP   A 1 189 ? 47.767  7.139   2.675   1.00 50.35 ? 193 ASP   A CB   1 
ATOM   1370 C  CG   . ASP   A 1 189 ? 46.517  7.887   2.231   1.00 51.55 ? 193 ASP   A CG   1 
ATOM   1371 O  OD1  . ASP   A 1 189 ? 46.441  9.109   2.470   1.00 55.47 ? 193 ASP   A OD1  1 
ATOM   1372 O  OD2  . ASP   A 1 189 ? 45.618  7.231   1.661   1.00 51.17 ? 193 ASP   A OD2  1 
ATOM   1373 N  N    . SER   A 1 190 ? 48.134  10.042  4.542   1.00 45.17 ? 194 SER   A N    1 
ATOM   1374 C  CA   . SER   A 1 190 ? 47.552  10.962  5.507   1.00 42.45 ? 194 SER   A CA   1 
ATOM   1375 C  C    . SER   A 1 190 ? 46.476  11.830  4.852   1.00 39.71 ? 194 SER   A C    1 
ATOM   1376 O  O    . SER   A 1 190 ? 45.877  12.681  5.518   1.00 41.14 ? 194 SER   A O    1 
ATOM   1377 C  CB   . SER   A 1 190 ? 48.631  11.822  6.133   1.00 42.96 ? 194 SER   A CB   1 
ATOM   1378 N  N    . HIS   A 1 191 ? 46.214  11.597  3.557   1.00 33.57 ? 195 HIS   A N    1 
ATOM   1379 C  CA   . HIS   A 1 191 ? 45.438  12.541  2.773   1.00 29.71 ? 195 HIS   A CA   1 
ATOM   1380 C  C    . HIS   A 1 191 ? 44.042  12.016  2.427   1.00 23.28 ? 195 HIS   A C    1 
ATOM   1381 O  O    . HIS   A 1 191 ? 43.253  12.805  1.937   1.00 23.88 ? 195 HIS   A O    1 
ATOM   1382 C  CB   . HIS   A 1 191 ? 46.207  12.996  1.521   1.00 32.89 ? 195 HIS   A CB   1 
ATOM   1383 C  CG   . HIS   A 1 191 ? 46.342  11.954  0.451   1.00 37.36 ? 195 HIS   A CG   1 
ATOM   1384 N  ND1  . HIS   A 1 191 ? 47.148  10.840  0.575   1.00 39.68 ? 195 HIS   A ND1  1 
ATOM   1385 C  CD2  . HIS   A 1 191 ? 45.754  11.849  -0.758  1.00 38.83 ? 195 HIS   A CD2  1 
ATOM   1386 C  CE1  . HIS   A 1 191 ? 47.047  10.098  -0.523  1.00 38.85 ? 195 HIS   A CE1  1 
ATOM   1387 N  NE2  . HIS   A 1 191 ? 46.211  10.696  -1.350  1.00 37.55 ? 195 HIS   A NE2  1 
ATOM   1388 N  N    . THR   A 1 192 ? 43.719  10.733  2.685   1.00 19.28 ? 196 THR   A N    1 
ATOM   1389 C  CA   . THR   A 1 192 ? 42.386  10.202  2.381   1.00 16.74 ? 196 THR   A CA   1 
ATOM   1390 C  C    . THR   A 1 192 ? 41.702  9.653   3.636   1.00 14.88 ? 196 THR   A C    1 
ATOM   1391 O  O    . THR   A 1 192 ? 42.354  9.273   4.604   1.00 14.59 ? 196 THR   A O    1 
ATOM   1392 C  CB   . THR   A 1 192 ? 42.440  9.109   1.308   1.00 17.42 ? 196 THR   A CB   1 
ATOM   1393 O  OG1  . THR   A 1 192 ? 43.016  7.936   1.876   1.00 17.75 ? 196 THR   A OG1  1 
ATOM   1394 C  CG2  . THR   A 1 192 ? 43.244  9.518   0.087   1.00 18.46 ? 196 THR   A CG2  1 
ATOM   1395 N  N    . ALA   A 1 193 ? 40.366  9.554   3.580   1.00 13.56 ? 197 ALA   A N    1 
ATOM   1396 C  CA   . ALA   A 1 193 ? 39.608  8.952   4.666   1.00 13.14 ? 197 ALA   A CA   1 
ATOM   1397 C  C    . ALA   A 1 193 ? 40.033  7.493   4.868   1.00 12.73 ? 197 ALA   A C    1 
ATOM   1398 O  O    . ALA   A 1 193 ? 40.184  7.044   5.995   1.00 12.63 ? 197 ALA   A O    1 
ATOM   1399 C  CB   . ALA   A 1 193 ? 38.119  9.068   4.418   1.00 13.34 ? 197 ALA   A CB   1 
ATOM   1400 N  N    . GLU   A 1 194 ? 40.229  6.747   3.778   1.00 12.72 ? 198 GLU   A N    1 
ATOM   1401 C  CA   . GLU   A 1 194 ? 40.671  5.367   3.875   1.00 13.30 ? 198 GLU   A CA   1 
ATOM   1402 C  C    . GLU   A 1 194 ? 42.045  5.295   4.541   1.00 13.40 ? 198 GLU   A C    1 
ATOM   1403 O  O    . GLU   A 1 194 ? 42.301  4.407   5.356   1.00 13.38 ? 198 GLU   A O    1 
ATOM   1404 C  CB   . GLU   A 1 194 ? 40.690  4.697   2.501   1.00 15.37 ? 198 GLU   A CB   1 
ATOM   1405 C  CG   . GLU   A 1 194 ? 41.130  3.240   2.573   1.00 17.46 ? 198 GLU   A CG   1 
ATOM   1406 C  CD   . GLU   A 1 194 ? 41.088  2.481   1.259   1.00 20.70 ? 198 GLU   A CD   1 
ATOM   1407 O  OE1  . GLU   A 1 194 ? 40.390  2.936   0.354   1.00 26.93 ? 198 GLU   A OE1  1 
ATOM   1408 O  OE2  . GLU   A 1 194 ? 41.731  1.424   1.147   1.00 24.81 ? 198 GLU   A OE2  1 
ATOM   1409 N  N    . GLY   A 1 195 ? 42.942  6.223   4.182   1.00 14.05 ? 199 GLY   A N    1 
ATOM   1410 C  CA   . GLY   A 1 195 ? 44.273  6.220   4.758   1.00 14.06 ? 199 GLY   A CA   1 
ATOM   1411 C  C    . GLY   A 1 195 ? 44.225  6.430   6.268   1.00 14.15 ? 199 GLY   A C    1 
ATOM   1412 O  O    . GLY   A 1 195 ? 44.948  5.777   7.019   1.00 15.36 ? 199 GLY   A O    1 
ATOM   1413 N  N    . ASP   A 1 196 ? 43.334  7.321   6.712   1.00 13.84 ? 200 ASP   A N    1 
ATOM   1414 C  CA   . ASP   A 1 196 ? 43.182  7.601   8.133   1.00 14.46 ? 200 ASP   A CA   1 
ATOM   1415 C  C    . ASP   A 1 196 ? 42.547  6.411   8.856   1.00 13.58 ? 200 ASP   A C    1 
ATOM   1416 O  O    . ASP   A 1 196 ? 42.895  6.109   9.995   1.00 14.38 ? 200 ASP   A O    1 
ATOM   1417 C  CB   . ASP   A 1 196 ? 42.485  8.935   8.350   1.00 16.49 ? 200 ASP   A CB   1 
ATOM   1418 C  CG   . ASP   A 1 196 ? 43.364  10.160  8.109   1.00 20.61 ? 200 ASP   A CG   1 
ATOM   1419 O  OD1  . ASP   A 1 196 ? 44.579  9.993   7.880   1.00 23.34 ? 200 ASP   A OD1  1 
ATOM   1420 O  OD2  . ASP   A 1 196 ? 42.827  11.288  8.132   1.00 27.22 ? 200 ASP   A OD2  1 
ATOM   1421 N  N    . VAL   A 1 197 ? 41.619  5.713   8.204   1.00 13.32 ? 201 VAL   A N    1 
ATOM   1422 C  CA   . VAL   A 1 197 ? 41.043  4.514   8.799   1.00 13.27 ? 201 VAL   A CA   1 
ATOM   1423 C  C    . VAL   A 1 197 ? 42.104  3.426   8.950   1.00 13.28 ? 201 VAL   A C    1 
ATOM   1424 O  O    . VAL   A 1 197 ? 42.162  2.740   9.973   1.00 13.60 ? 201 VAL   A O    1 
ATOM   1425 C  CB   . VAL   A 1 197 ? 39.835  4.032   7.975   1.00 14.45 ? 201 VAL   A CB   1 
ATOM   1426 C  CG1  . VAL   A 1 197 ? 39.470  2.585   8.252   1.00 15.56 ? 201 VAL   A CG1  1 
ATOM   1427 C  CG2  . VAL   A 1 197 ? 38.637  4.939   8.193   1.00 14.63 ? 201 VAL   A CG2  1 
ATOM   1428 N  N    . LEU   A 1 198 ? 42.919  3.221   7.915   1.00 13.37 ? 202 LEU   A N    1 
ATOM   1429 C  CA   . LEU   A 1 198 ? 43.915  2.157   7.952   1.00 14.24 ? 202 LEU   A CA   1 
ATOM   1430 C  C    . LEU   A 1 198 ? 44.986  2.454   9.001   1.00 14.23 ? 202 LEU   A C    1 
ATOM   1431 O  O    . LEU   A 1 198 ? 45.443  1.541   9.690   1.00 14.53 ? 202 LEU   A O    1 
ATOM   1432 C  CB   . LEU   A 1 198 ? 44.512  1.930   6.568   1.00 14.75 ? 202 LEU   A CB   1 
ATOM   1433 C  CG   . LEU   A 1 198 ? 43.572  1.306   5.536   1.00 15.55 ? 202 LEU   A CG   1 
ATOM   1434 C  CD1  . LEU   A 1 198 ? 44.222  1.373   4.166   1.00 15.97 ? 202 LEU   A CD1  1 
ATOM   1435 C  CD2  . LEU   A 1 198 ? 43.208  -0.127  5.884   1.00 16.22 ? 202 LEU   A CD2  1 
ATOM   1436 N  N    . ALA   A 1 199 ? 45.387  3.721   9.136   1.00 14.18 ? 203 ALA   A N    1 
ATOM   1437 C  CA   . ALA   A 1 199 ? 46.353  4.093   10.158  1.00 14.58 ? 203 ALA   A CA   1 
ATOM   1438 C  C    . ALA   A 1 199 ? 45.782  3.844   11.556  1.00 14.31 ? 203 ALA   A C    1 
ATOM   1439 O  O    . ALA   A 1 199 ? 46.471  3.336   12.441  1.00 15.25 ? 203 ALA   A O    1 
ATOM   1440 C  CB   . ALA   A 1 199 ? 46.775  5.539   9.979   1.00 14.96 ? 203 ALA   A CB   1 
ATOM   1441 N  N    . LEU   A 1 200 ? 44.512  4.205   11.760  1.00 13.53 ? 204 LEU   A N    1 
ATOM   1442 C  CA   . LEU   A 1 200 ? 43.850  3.967   13.038  1.00 13.54 ? 204 LEU   A CA   1 
ATOM   1443 C  C    . LEU   A 1 200 ? 43.764  2.473   13.346  1.00 13.80 ? 204 LEU   A C    1 
ATOM   1444 O  O    . LEU   A 1 200 ? 44.023  2.045   14.473  1.00 14.52 ? 204 LEU   A O    1 
ATOM   1445 C  CB   . LEU   A 1 200 ? 42.472  4.622   13.020  1.00 13.95 ? 204 LEU   A CB   1 
ATOM   1446 C  CG   . LEU   A 1 200 ? 41.629  4.418   14.278  1.00 14.58 ? 204 LEU   A CG   1 
ATOM   1447 C  CD1  . LEU   A 1 200 ? 42.360  4.903   15.524  1.00 15.53 ? 204 LEU   A CD1  1 
ATOM   1448 C  CD2  . LEU   A 1 200 ? 40.288  5.118   14.123  1.00 15.04 ? 204 LEU   A CD2  1 
ATOM   1449 N  N    . LEU   A 1 201 ? 43.398  1.673   12.343  1.00 13.78 ? 205 LEU   A N    1 
ATOM   1450 C  CA   . LEU   A 1 201 ? 43.343  0.234   12.519  1.00 14.55 ? 205 LEU   A CA   1 
ATOM   1451 C  C    . LEU   A 1 201 ? 44.702  -0.274  13.004  1.00 14.87 ? 205 LEU   A C    1 
ATOM   1452 O  O    . LEU   A 1 201 ? 44.771  -1.043  13.958  1.00 15.48 ? 205 LEU   A O    1 
ATOM   1453 C  CB   . LEU   A 1 201 ? 42.921  -0.433  11.216  1.00 15.32 ? 205 LEU   A CB   1 
ATOM   1454 C  CG   . LEU   A 1 201 ? 42.997  -1.960  11.211  1.00 16.29 ? 205 LEU   A CG   1 
ATOM   1455 C  CD1  . LEU   A 1 201 ? 42.090  -2.580  12.269  1.00 16.91 ? 205 LEU   A CD1  1 
ATOM   1456 C  CD2  . LEU   A 1 201 ? 42.654  -2.462  9.830   1.00 17.22 ? 205 LEU   A CD2  1 
ATOM   1457 N  N    . SER   A 1 202 ? 45.790  0.162   12.355  1.00 15.52 ? 206 SER   A N    1 
ATOM   1458 C  CA   . SER   A 1 202 ? 47.127  -0.266  12.740  1.00 17.10 ? 206 SER   A CA   1 
ATOM   1459 C  C    . SER   A 1 202 ? 47.426  0.072   14.201  1.00 17.80 ? 206 SER   A C    1 
ATOM   1460 O  O    . SER   A 1 202 ? 47.986  -0.745  14.929  1.00 19.29 ? 206 SER   A O    1 
ATOM   1461 C  CB   . SER   A 1 202 ? 48.178  0.335   11.853  1.00 17.43 ? 206 SER   A CB   1 
ATOM   1462 O  OG   . SER   A 1 202 ? 48.081  -0.160  10.528  1.00 18.48 ? 206 SER   A OG   1 
ATOM   1463 N  N    . ILE   A 1 203 ? 47.058  1.280   14.637  1.00 18.02 ? 207 ILE   A N    1 
ATOM   1464 C  CA   . ILE   A 1 203 ? 47.294  1.681   16.014  1.00 19.25 ? 207 ILE   A CA   1 
ATOM   1465 C  C    . ILE   A 1 203 ? 46.515  0.760   16.948  1.00 19.38 ? 207 ILE   A C    1 
ATOM   1466 O  O    . ILE   A 1 203 ? 47.027  0.318   17.977  1.00 21.39 ? 207 ILE   A O    1 
ATOM   1467 C  CB   . ILE   A 1 203 ? 46.924  3.160   16.212  1.00 20.35 ? 207 ILE   A CB   1 
ATOM   1468 C  CG1  . ILE   A 1 203 ? 47.928  4.067   15.520  1.00 21.14 ? 207 ILE   A CG1  1 
ATOM   1469 C  CG2  . ILE   A 1 203 ? 46.771  3.496   17.694  1.00 21.94 ? 207 ILE   A CG2  1 
ATOM   1470 C  CD1  . ILE   A 1 203 ? 47.419  5.482   15.326  1.00 21.78 ? 207 ILE   A CD1  1 
ATOM   1471 N  N    . CYS   A 1 204 ? 45.266  0.465   16.585  1.00 18.05 ? 208 CYS   A N    1 
ATOM   1472 C  CA   . CYS   A 1 204 ? 44.414  -0.338  17.442  1.00 18.55 ? 208 CYS   A CA   1 
ATOM   1473 C  C    . CYS   A 1 204 ? 44.887  -1.790  17.486  1.00 18.81 ? 208 CYS   A C    1 
ATOM   1474 O  O    . CYS   A 1 204 ? 44.525  -2.512  18.409  1.00 20.48 ? 208 CYS   A O    1 
ATOM   1475 C  CB   . CYS   A 1 204 ? 42.954  -0.195  17.036  1.00 17.77 ? 208 CYS   A CB   1 
ATOM   1476 S  SG   . CYS   A 1 204 ? 42.269  1.443   17.406  1.00 19.18 ? 208 CYS   A SG   1 
ATOM   1477 N  N    . GLN   A 1 205 ? 45.676  -2.217  16.493  1.00 18.51 ? 209 GLN   A N    1 
ATOM   1478 C  CA   . GLN   A 1 205 ? 46.226  -3.565  16.476  1.00 19.93 ? 209 GLN   A CA   1 
ATOM   1479 C  C    . GLN   A 1 205 ? 47.519  -3.691  17.286  1.00 21.81 ? 209 GLN   A C    1 
ATOM   1480 O  O    . GLN   A 1 205 ? 48.069  -4.788  17.367  1.00 23.01 ? 209 GLN   A O    1 
ATOM   1481 C  CB   . GLN   A 1 205 ? 46.471  -4.007  15.036  1.00 19.90 ? 209 GLN   A CB   1 
ATOM   1482 C  CG   . GLN   A 1 205 ? 45.189  -4.282  14.263  1.00 19.73 ? 209 GLN   A CG   1 
ATOM   1483 C  CD   . GLN   A 1 205 ? 45.489  -4.686  12.840  1.00 20.42 ? 209 GLN   A CD   1 
ATOM   1484 O  OE1  . GLN   A 1 205 ? 45.792  -3.841  11.996  1.00 21.44 ? 209 GLN   A OE1  1 
ATOM   1485 N  NE2  . GLN   A 1 205 ? 45.461  -5.985  12.579  1.00 21.67 ? 209 GLN   A NE2  1 
ATOM   1486 N  N    . TRP   A 1 206 ? 47.995  -2.595  17.894  1.00 22.22 ? 210 TRP   A N    1 
ATOM   1487 C  CA   . TRP   A 1 206 ? 49.235  -2.617  18.665  1.00 24.42 ? 210 TRP   A CA   1 
ATOM   1488 C  C    . TRP   A 1 206 ? 49.072  -3.481  19.917  1.00 24.50 ? 210 TRP   A C    1 
ATOM   1489 O  O    . TRP   A 1 206 ? 49.886  -4.371  20.168  1.00 25.87 ? 210 TRP   A O    1 
ATOM   1490 C  CB   . TRP   A 1 206 ? 49.657  -1.181  19.010  1.00 26.72 ? 210 TRP   A CB   1 
ATOM   1491 C  CG   . TRP   A 1 206 ? 50.806  -1.086  19.978  1.00 31.32 ? 210 TRP   A CG   1 
ATOM   1492 C  CD1  . TRP   A 1 206 ? 52.078  -1.533  19.787  1.00 35.10 ? 210 TRP   A CD1  1 
ATOM   1493 C  CD2  . TRP   A 1 206 ? 50.781  -0.479  21.288  1.00 35.17 ? 210 TRP   A CD2  1 
ATOM   1494 N  NE1  . TRP   A 1 206 ? 52.844  -1.267  20.893  1.00 37.08 ? 210 TRP   A NE1  1 
ATOM   1495 C  CE2  . TRP   A 1 206 ? 52.079  -0.618  21.826  1.00 37.47 ? 210 TRP   A CE2  1 
ATOM   1496 C  CE3  . TRP   A 1 206 ? 49.796  0.160   22.052  1.00 38.42 ? 210 TRP   A CE3  1 
ATOM   1497 C  CZ2  . TRP   A 1 206 ? 52.412  -0.141  23.093  1.00 40.69 ? 210 TRP   A CZ2  1 
ATOM   1498 C  CZ3  . TRP   A 1 206 ? 50.129  0.634   23.305  1.00 41.39 ? 210 TRP   A CZ3  1 
ATOM   1499 C  CH2  . TRP   A 1 206 ? 51.418  0.482   23.816  1.00 41.65 ? 210 TRP   A CH2  1 
ATOM   1500 N  N    . ARG   A 1 207 ? 48.031  -3.181  20.706  1.00 23.72 ? 211 ARG   A N    1 
ATOM   1501 C  CA   . ARG   A 1 207 ? 47.631  -3.989  21.847  1.00 24.18 ? 211 ARG   A CA   1 
ATOM   1502 C  C    . ARG   A 1 207 ? 46.151  -4.296  21.671  1.00 21.48 ? 211 ARG   A C    1 
ATOM   1503 O  O    . ARG   A 1 207 ? 45.285  -3.668  22.278  1.00 21.36 ? 211 ARG   A O    1 
ATOM   1504 C  CB   . ARG   A 1 207 ? 47.909  -3.281  23.179  1.00 26.19 ? 211 ARG   A CB   1 
ATOM   1505 C  CG   . ARG   A 1 207 ? 49.385  -3.149  23.525  1.00 28.54 ? 211 ARG   A CG   1 
ATOM   1506 C  CD   . ARG   A 1 207 ? 50.113  -4.477  23.404  1.00 31.15 ? 211 ARG   A CD   1 
ATOM   1507 N  N    . PRO   A 1 208 ? 45.813  -5.233  20.765  1.00 20.11 ? 212 PRO   A N    1 
ATOM   1508 C  CA   . PRO   A 1 208 ? 44.433  -5.363  20.300  1.00 19.86 ? 212 PRO   A CA   1 
ATOM   1509 C  C    . PRO   A 1 208 ? 43.449  -5.859  21.355  1.00 19.09 ? 212 PRO   A C    1 
ATOM   1510 O  O    . PRO   A 1 208 ? 42.316  -5.393  21.398  1.00 18.78 ? 212 PRO   A O    1 
ATOM   1511 C  CB   . PRO   A 1 208 ? 44.574  -6.328  19.110  1.00 20.29 ? 212 PRO   A CB   1 
ATOM   1512 C  CG   . PRO   A 1 208 ? 45.802  -7.133  19.420  1.00 21.22 ? 212 PRO   A CG   1 
ATOM   1513 C  CD   . PRO   A 1 208 ? 46.741  -6.157  20.094  1.00 20.79 ? 212 PRO   A CD   1 
ATOM   1514 N  N    . GLN   A 1 209 ? 43.877  -6.792  22.212  1.00 19.72 ? 213 GLN   A N    1 
ATOM   1515 C  CA   . GLN   A 1 209 ? 42.980  -7.344  23.215  1.00 20.06 ? 213 GLN   A CA   1 
ATOM   1516 C  C    . GLN   A 1 209 ? 42.625  -6.274  24.251  1.00 19.92 ? 213 GLN   A C    1 
ATOM   1517 O  O    . GLN   A 1 209 ? 41.472  -6.169  24.663  1.00 20.14 ? 213 GLN   A O    1 
ATOM   1518 C  CB   . GLN   A 1 209 ? 43.549  -8.601  23.877  1.00 21.87 ? 213 GLN   A CB   1 
ATOM   1519 C  CG   . GLN   A 1 209 ? 43.910  -9.722  22.903  1.00 24.14 ? 213 GLN   A CG   1 
ATOM   1520 C  CD   . GLN   A 1 209 ? 45.348  -9.673  22.426  1.00 28.27 ? 213 GLN   A CD   1 
ATOM   1521 O  OE1  . GLN   A 1 209 ? 45.997  -8.620  22.400  1.00 30.12 ? 213 GLN   A OE1  1 
ATOM   1522 N  NE2  . GLN   A 1 209 ? 45.880  -10.829 22.054  1.00 32.67 ? 213 GLN   A NE2  1 
ATOM   1523 N  N    . ALA   A 1 210 ? 43.611  -5.460  24.644  1.00 20.50 ? 214 ALA   A N    1 
ATOM   1524 C  CA   . ALA   A 1 210 ? 43.383  -4.347  25.553  1.00 20.52 ? 214 ALA   A CA   1 
ATOM   1525 C  C    . ALA   A 1 210 ? 42.457  -3.295  24.938  1.00 19.10 ? 214 ALA   A C    1 
ATOM   1526 O  O    . ALA   A 1 210 ? 41.587  -2.770  25.623  1.00 19.61 ? 214 ALA   A O    1 
ATOM   1527 C  CB   . ALA   A 1 210 ? 44.706  -3.731  25.946  1.00 21.45 ? 214 ALA   A CB   1 
ATOM   1528 N  N    . LEU   A 1 211 ? 42.665  -2.965  23.657  1.00 19.10 ? 215 LEU   A N    1 
ATOM   1529 C  CA   . LEU   A 1 211 ? 41.843  -1.975  22.973  1.00 17.91 ? 215 LEU   A CA   1 
ATOM   1530 C  C    . LEU   A 1 211 ? 40.395  -2.460  22.944  1.00 17.15 ? 215 LEU   A C    1 
ATOM   1531 O  O    . LEU   A 1 211 ? 39.475  -1.717  23.272  1.00 17.89 ? 215 LEU   A O    1 
ATOM   1532 C  CB   . LEU   A 1 211 ? 42.437  -1.744  21.581  1.00 18.56 ? 215 LEU   A CB   1 
ATOM   1533 C  CG   . LEU   A 1 211 ? 41.803  -0.673  20.680  1.00 19.06 ? 215 LEU   A CG   1 
ATOM   1534 C  CD1  . LEU   A 1 211 ? 40.589  -1.196  19.935  1.00 18.95 ? 215 LEU   A CD1  1 
ATOM   1535 C  CD2  . LEU   A 1 211 ? 41.444  0.608   21.420  1.00 19.24 ? 215 LEU   A CD2  1 
ATOM   1536 N  N    . LEU   A 1 212 ? 40.198  -3.729  22.570  1.00 17.10 ? 216 LEU   A N    1 
ATOM   1537 C  CA   . LEU   A 1 212 ? 38.862  -4.283  22.463  1.00 16.98 ? 216 LEU   A CA   1 
ATOM   1538 C  C    . LEU   A 1 212 ? 38.175  -4.295  23.831  1.00 17.39 ? 216 LEU   A C    1 
ATOM   1539 O  O    . LEU   A 1 212 ? 36.990  -3.977  23.923  1.00 17.25 ? 216 LEU   A O    1 
ATOM   1540 C  CB   . LEU   A 1 212 ? 38.933  -5.673  21.841  1.00 17.28 ? 216 LEU   A CB   1 
ATOM   1541 C  CG   . LEU   A 1 212 ? 37.592  -6.363  21.595  1.00 16.28 ? 216 LEU   A CG   1 
ATOM   1542 C  CD1  . LEU   A 1 212 ? 36.670  -5.566  20.676  1.00 16.60 ? 216 LEU   A CD1  1 
ATOM   1543 C  CD2  . LEU   A 1 212 ? 37.895  -7.750  21.057  1.00 16.04 ? 216 LEU   A CD2  1 
ATOM   1544 N  N    . ARG   A 1 213 ? 38.910  -4.672  24.893  1.00 17.71 ? 217 ARG   A N    1 
ATOM   1545 C  CA   . ARG   A 1 213 ? 38.360  -4.642  26.242  1.00 19.44 ? 217 ARG   A CA   1 
ATOM   1546 C  C    . ARG   A 1 213 ? 37.883  -3.236  26.599  1.00 19.27 ? 217 ARG   A C    1 
ATOM   1547 O  O    . ARG   A 1 213 ? 36.805  -3.067  27.169  1.00 19.51 ? 217 ARG   A O    1 
ATOM   1548 C  CB   . ARG   A 1 213 ? 39.366  -5.143  27.284  1.00 22.47 ? 217 ARG   A CB   1 
ATOM   1549 C  CG   . ARG   A 1 213 ? 39.494  -6.656  27.360  1.00 26.17 ? 217 ARG   A CG   1 
ATOM   1550 C  CD   . ARG   A 1 213 ? 40.177  -7.095  28.655  1.00 30.54 ? 217 ARG   A CD   1 
ATOM   1551 N  NE   . ARG   A 1 213 ? 41.606  -6.761  28.677  1.00 34.10 ? 217 ARG   A NE   1 
ATOM   1552 C  CZ   . ARG   A 1 213 ? 42.579  -7.441  28.073  1.00 36.65 ? 217 ARG   A CZ   1 
ATOM   1553 N  NH1  . ARG   A 1 213 ? 42.333  -8.588  27.462  1.00 38.80 ? 217 ARG   A NH1  1 
ATOM   1554 N  NH2  . ARG   A 1 213 ? 43.815  -6.980  28.113  1.00 39.35 ? 217 ARG   A NH2  1 
ATOM   1555 N  N    . TRP   A 1 214 ? 38.677  -2.227  26.234  1.00 18.91 ? 218 TRP   A N    1 
ATOM   1556 C  CA   . TRP   A 1 214 ? 38.328  -0.855  26.549  1.00 19.26 ? 218 TRP   A CA   1 
ATOM   1557 C  C    . TRP   A 1 214 ? 37.071  -0.439  25.788  1.00 18.64 ? 218 TRP   A C    1 
ATOM   1558 O  O    . TRP   A 1 214 ? 36.166  0.157   26.363  1.00 18.44 ? 218 TRP   A O    1 
ATOM   1559 C  CB   . TRP   A 1 214 ? 39.505  0.079   26.249  1.00 20.95 ? 218 TRP   A CB   1 
ATOM   1560 C  CG   . TRP   A 1 214 ? 39.321  1.431   26.877  1.00 23.35 ? 218 TRP   A CG   1 
ATOM   1561 C  CD1  . TRP   A 1 214 ? 39.793  1.843   28.090  1.00 24.95 ? 218 TRP   A CD1  1 
ATOM   1562 C  CD2  . TRP   A 1 214 ? 38.551  2.527   26.346  1.00 25.60 ? 218 TRP   A CD2  1 
ATOM   1563 N  NE1  . TRP   A 1 214 ? 39.396  3.126   28.336  1.00 26.74 ? 218 TRP   A NE1  1 
ATOM   1564 C  CE2  . TRP   A 1 214 ? 38.633  3.572   27.293  1.00 26.14 ? 218 TRP   A CE2  1 
ATOM   1565 C  CE3  . TRP   A 1 214 ? 37.813  2.727   25.175  1.00 25.67 ? 218 TRP   A CE3  1 
ATOM   1566 C  CZ2  . TRP   A 1 214 ? 38.002  4.795   27.099  1.00 28.28 ? 218 TRP   A CZ2  1 
ATOM   1567 C  CZ3  . TRP   A 1 214 ? 37.193  3.945   24.985  1.00 28.10 ? 218 TRP   A CZ3  1 
ATOM   1568 C  CH2  . TRP   A 1 214 ? 37.280  4.954   25.937  1.00 27.38 ? 218 TRP   A CH2  1 
ATOM   1569 N  N    . VAL   A 1 215 ? 37.009  -0.788  24.497  1.00 17.88 ? 219 VAL   A N    1 
ATOM   1570 C  CA   . VAL   A 1 215 ? 35.842  -0.487  23.691  1.00 17.39 ? 219 VAL   A CA   1 
ATOM   1571 C  C    . VAL   A 1 215 ? 34.591  -1.112  24.305  1.00 16.87 ? 219 VAL   A C    1 
ATOM   1572 O  O    . VAL   A 1 215 ? 33.561  -0.455  24.420  1.00 17.04 ? 219 VAL   A O    1 
ATOM   1573 C  CB   . VAL   A 1 215 ? 36.068  -0.946  22.239  1.00 17.85 ? 219 VAL   A CB   1 
ATOM   1574 C  CG1  . VAL   A 1 215 ? 34.771  -0.944  21.443  1.00 18.52 ? 219 VAL   A CG1  1 
ATOM   1575 C  CG2  . VAL   A 1 215 ? 37.124  -0.094  21.551  1.00 18.72 ? 219 VAL   A CG2  1 
ATOM   1576 N  N    . ASP   A 1 216 ? 34.667  -2.388  24.693  1.00 16.91 ? 220 ASP   A N    1 
ATOM   1577 C  CA   . ASP   A 1 216 ? 33.512  -3.066  25.258  1.00 17.64 ? 220 ASP   A CA   1 
ATOM   1578 C  C    . ASP   A 1 216 ? 33.044  -2.370  26.540  1.00 18.47 ? 220 ASP   A C    1 
ATOM   1579 O  O    . ASP   A 1 216 ? 31.846  -2.226  26.782  1.00 20.51 ? 220 ASP   A O    1 
ATOM   1580 C  CB   . ASP   A 1 216 ? 33.823  -4.538  25.459  1.00 17.75 ? 220 ASP   A CB   1 
ATOM   1581 C  CG   . ASP   A 1 216 ? 33.836  -5.393  24.196  1.00 18.12 ? 220 ASP   A CG   1 
ATOM   1582 O  OD1  . ASP   A 1 216 ? 33.287  -4.937  23.170  1.00 18.57 ? 220 ASP   A OD1  1 
ATOM   1583 O  OD2  . ASP   A 1 216 ? 34.396  -6.514  24.247  1.00 18.29 ? 220 ASP   A OD2  1 
ATOM   1584 N  N    . ALA   A 1 217 ? 33.993  -1.897  27.349  1.00 18.76 ? 221 ALA   A N    1 
ATOM   1585 C  CA   . ALA   A 1 217 ? 33.670  -1.301  28.632  1.00 19.94 ? 221 ALA   A CA   1 
ATOM   1586 C  C    . ALA   A 1 217 ? 33.095  0.110   28.484  1.00 20.26 ? 221 ALA   A C    1 
ATOM   1587 O  O    . ALA   A 1 217 ? 32.400  0.583   29.386  1.00 22.56 ? 221 ALA   A O    1 
ATOM   1588 C  CB   . ALA   A 1 217 ? 34.911  -1.311  29.500  1.00 20.98 ? 221 ALA   A CB   1 
ATOM   1589 N  N    . HIS   A 1 218 ? 33.371  0.790   27.358  1.00 18.80 ? 222 HIS   A N    1 
ATOM   1590 C  CA   . HIS   A 1 218 ? 33.086  2.216   27.250  1.00 20.06 ? 222 HIS   A CA   1 
ATOM   1591 C  C    . HIS   A 1 218 ? 32.220  2.601   26.047  1.00 20.07 ? 222 HIS   A C    1 
ATOM   1592 O  O    . HIS   A 1 218 ? 31.972  3.788   25.841  1.00 21.02 ? 222 HIS   A O    1 
ATOM   1593 C  CB   . HIS   A 1 218 ? 34.395  3.009   27.212  1.00 21.72 ? 222 HIS   A CB   1 
ATOM   1594 C  CG   . HIS   A 1 218 ? 35.180  2.892   28.460  1.00 24.15 ? 222 HIS   A CG   1 
ATOM   1595 N  ND1  . HIS   A 1 218 ? 36.175  1.957   28.633  1.00 25.32 ? 222 HIS   A ND1  1 
ATOM   1596 C  CD2  . HIS   A 1 218 ? 35.124  3.598   29.599  1.00 26.96 ? 222 HIS   A CD2  1 
ATOM   1597 C  CE1  . HIS   A 1 218 ? 36.696  2.102   29.843  1.00 27.72 ? 222 HIS   A CE1  1 
ATOM   1598 N  NE2  . HIS   A 1 218 ? 36.076  3.094   30.444  1.00 28.56 ? 222 HIS   A NE2  1 
ATOM   1599 N  N    . ALA   A 1 219 ? 31.717  1.621   25.294  1.00 20.39 ? 223 ALA   A N    1 
ATOM   1600 C  CA   . ALA   A 1 219 ? 30.870  1.887   24.141  1.00 20.23 ? 223 ALA   A CA   1 
ATOM   1601 C  C    . ALA   A 1 219 ? 29.646  2.701   24.555  1.00 19.68 ? 223 ALA   A C    1 
ATOM   1602 O  O    . ALA   A 1 219 ? 29.030  2.416   25.578  1.00 20.28 ? 223 ALA   A O    1 
ATOM   1603 C  CB   . ALA   A 1 219 ? 30.452  0.581   23.499  1.00 21.13 ? 223 ALA   A CB   1 
ATOM   1604 N  N    . ARG   A 1 220 ? 29.308  3.706   23.737  1.00 18.94 ? 224 ARG   A N    1 
ATOM   1605 C  CA   . ARG   A 1 220 ? 28.205  4.616   24.013  1.00 19.97 ? 224 ARG   A CA   1 
ATOM   1606 C  C    . ARG   A 1 220 ? 27.190  4.540   22.881  1.00 18.43 ? 224 ARG   A C    1 
ATOM   1607 O  O    . ARG   A 1 220 ? 27.584  4.457   21.723  1.00 17.28 ? 224 ARG   A O    1 
ATOM   1608 C  CB   . ARG   A 1 220 ? 28.695  6.066   24.076  1.00 23.45 ? 224 ARG   A CB   1 
ATOM   1609 C  CG   . ARG   A 1 220 ? 29.702  6.329   25.186  1.00 26.83 ? 224 ARG   A CG   1 
ATOM   1610 C  CD   . ARG   A 1 220 ? 30.468  7.626   24.954  1.00 29.40 ? 224 ARG   A CD   1 
ATOM   1611 N  NE   . ARG   A 1 220 ? 31.134  7.559   23.649  1.00 31.97 ? 224 ARG   A NE   1 
ATOM   1612 C  CZ   . ARG   A 1 220 ? 31.616  8.588   22.973  1.00 31.25 ? 224 ARG   A CZ   1 
ATOM   1613 N  NH1  . ARG   A 1 220 ? 31.709  9.766   23.561  1.00 34.56 ? 224 ARG   A NH1  1 
ATOM   1614 N  NH2  . ARG   A 1 220 ? 32.025  8.416   21.726  1.00 26.74 ? 224 ARG   A NH2  1 
ATOM   1615 N  N    . PRO   A 1 221 ? 25.872  4.599   23.156  1.00 19.07 ? 225 PRO   A N    1 
ATOM   1616 C  CA   . PRO   A 1 221 ? 24.882  4.630   22.082  1.00 19.15 ? 225 PRO   A CA   1 
ATOM   1617 C  C    . PRO   A 1 221 ? 25.126  5.824   21.168  1.00 18.96 ? 225 PRO   A C    1 
ATOM   1618 O  O    . PRO   A 1 221 ? 25.372  6.936   21.638  1.00 19.26 ? 225 PRO   A O    1 
ATOM   1619 C  CB   . PRO   A 1 221 ? 23.536  4.729   22.802  1.00 20.75 ? 225 PRO   A CB   1 
ATOM   1620 C  CG   . PRO   A 1 221 ? 23.824  4.248   24.197  1.00 21.39 ? 225 PRO   A CG   1 
ATOM   1621 C  CD   . PRO   A 1 221 ? 25.256  4.656   24.495  1.00 20.28 ? 225 PRO   A CD   1 
ATOM   1622 N  N    . PHE   A 1 222 ? 25.024  5.591   19.857  1.00 17.96 ? 226 PHE   A N    1 
ATOM   1623 C  CA   . PHE   A 1 222 ? 25.273  6.653   18.895  1.00 18.41 ? 226 PHE   A CA   1 
ATOM   1624 C  C    . PHE   A 1 222 ? 24.243  7.768   19.054  1.00 19.93 ? 226 PHE   A C    1 
ATOM   1625 O  O    . PHE   A 1 222 ? 24.544  8.927   18.773  1.00 20.26 ? 226 PHE   A O    1 
ATOM   1626 C  CB   . PHE   A 1 222 ? 25.315  6.069   17.484  1.00 18.60 ? 226 PHE   A CB   1 
ATOM   1627 C  CG   . PHE   A 1 222 ? 25.783  7.064   16.440  1.00 18.49 ? 226 PHE   A CG   1 
ATOM   1628 C  CD1  . PHE   A 1 222 ? 27.075  7.568   16.475  1.00 20.21 ? 226 PHE   A CD1  1 
ATOM   1629 C  CD2  . PHE   A 1 222 ? 24.942  7.478   15.414  1.00 21.21 ? 226 PHE   A CD2  1 
ATOM   1630 C  CE1  . PHE   A 1 222 ? 27.501  8.472   15.525  1.00 20.29 ? 226 PHE   A CE1  1 
ATOM   1631 C  CE2  . PHE   A 1 222 ? 25.387  8.378   14.456  1.00 21.97 ? 226 PHE   A CE2  1 
ATOM   1632 C  CZ   . PHE   A 1 222 ? 26.664  8.861   14.513  1.00 21.27 ? 226 PHE   A CZ   1 
ATOM   1633 N  N    . GLY   A 1 223 ? 23.044  7.425   19.546  1.00 20.96 ? 227 GLY   A N    1 
ATOM   1634 C  CA   . GLY   A 1 223 ? 21.986  8.404   19.756  1.00 22.63 ? 227 GLY   A CA   1 
ATOM   1635 C  C    . GLY   A 1 223 ? 22.325  9.456   20.814  1.00 23.61 ? 227 GLY   A C    1 
ATOM   1636 O  O    . GLY   A 1 223 ? 21.657  10.486  20.892  1.00 26.77 ? 227 GLY   A O    1 
ATOM   1637 N  N    . THR   A 1 224 ? 23.371  9.219   21.615  1.00 24.18 ? 228 THR   A N    1 
ATOM   1638 C  CA   . THR   A 1 224 ? 23.810  10.195  22.602  1.00 24.53 ? 228 THR   A CA   1 
ATOM   1639 C  C    . THR   A 1 224 ? 24.677  11.282  21.965  1.00 22.73 ? 228 THR   A C    1 
ATOM   1640 O  O    . THR   A 1 224 ? 25.008  12.256  22.639  1.00 23.54 ? 228 THR   A O    1 
ATOM   1641 C  CB   . THR   A 1 224 ? 24.553  9.523   23.757  1.00 26.05 ? 228 THR   A CB   1 
ATOM   1642 O  OG1  . THR   A 1 224 ? 25.796  8.995   23.305  1.00 26.47 ? 228 THR   A OG1  1 
ATOM   1643 C  CG2  . THR   A 1 224 ? 23.715  8.455   24.438  1.00 27.15 ? 228 THR   A CG2  1 
ATOM   1644 N  N    . ILE   A 1 225 ? 25.052  11.118  20.690  1.00 20.47 ? 229 ILE   A N    1 
ATOM   1645 C  CA   . ILE   A 1 225 ? 25.838  12.119  19.984  1.00 19.86 ? 229 ILE   A CA   1 
ATOM   1646 C  C    . ILE   A 1 225 ? 24.888  13.162  19.409  1.00 20.02 ? 229 ILE   A C    1 
ATOM   1647 O  O    . ILE   A 1 225 ? 24.078  12.851  18.538  1.00 20.27 ? 229 ILE   A O    1 
ATOM   1648 C  CB   . ILE   A 1 225 ? 26.688  11.494  18.863  1.00 19.13 ? 229 ILE   A CB   1 
ATOM   1649 C  CG1  . ILE   A 1 225 ? 27.641  10.408  19.388  1.00 20.19 ? 229 ILE   A CG1  1 
ATOM   1650 C  CG2  . ILE   A 1 225 ? 27.429  12.597  18.102  1.00 19.39 ? 229 ILE   A CG2  1 
ATOM   1651 C  CD1  . ILE   A 1 225 ? 28.765  10.931  20.264  1.00 20.47 ? 229 ILE   A CD1  1 
ATOM   1652 N  N    . ARG   A 1 226 ? 25.015  14.402  19.881  1.00 20.83 ? 230 ARG   A N    1 
ATOM   1653 C  CA   . ARG   A 1 226 ? 24.215  15.490  19.348  1.00 21.22 ? 230 ARG   A CA   1 
ATOM   1654 C  C    . ARG   A 1 226 ? 24.741  15.865  17.964  1.00 20.34 ? 230 ARG   A C    1 
ATOM   1655 O  O    . ARG   A 1 226 ? 25.945  15.855  17.719  1.00 19.65 ? 230 ARG   A O    1 
ATOM   1656 C  CB   . ARG   A 1 226 ? 24.248  16.715  20.265  1.00 24.61 ? 230 ARG   A CB   1 
ATOM   1657 C  CG   . ARG   A 1 226 ? 23.665  16.486  21.653  1.00 27.46 ? 230 ARG   A CG   1 
ATOM   1658 C  CD   . ARG   A 1 226 ? 23.446  17.789  22.412  1.00 31.55 ? 230 ARG   A CD   1 
ATOM   1659 N  N    . PRO   A 1 227 ? 23.855  16.217  17.015  1.00 19.96 ? 231 PRO   A N    1 
ATOM   1660 C  CA   . PRO   A 1 227 ? 24.310  16.685  15.708  1.00 19.00 ? 231 PRO   A CA   1 
ATOM   1661 C  C    . PRO   A 1 227 ? 25.163  17.938  15.856  1.00 18.01 ? 231 PRO   A C    1 
ATOM   1662 O  O    . PRO   A 1 227 ? 24.926  18.783  16.722  1.00 19.07 ? 231 PRO   A O    1 
ATOM   1663 C  CB   . PRO   A 1 227 ? 23.026  16.938  14.909  1.00 20.40 ? 231 PRO   A CB   1 
ATOM   1664 C  CG   . PRO   A 1 227 ? 21.948  17.062  15.946  1.00 22.84 ? 231 PRO   A CG   1 
ATOM   1665 C  CD   . PRO   A 1 227 ? 22.389  16.247  17.147  1.00 21.77 ? 231 PRO   A CD   1 
ATOM   1666 N  N    . MET   A 1 228 ? 26.142  18.062  14.962  1.00 16.72 ? 232 MET   A N    1 
ATOM   1667 C  CA   . MET   A 1 228 ? 27.038  19.206  14.940  1.00 17.25 ? 232 MET   A CA   1 
ATOM   1668 C  C    . MET   A 1 228 ? 26.259  20.508  14.757  1.00 18.72 ? 232 MET   A C    1 
ATOM   1669 O  O    . MET   A 1 228 ? 26.657  21.549  15.277  1.00 22.12 ? 232 MET   A O    1 
ATOM   1670 C  CB   . MET   A 1 228 ? 28.033  19.048  13.789  1.00 15.76 ? 232 MET   A CB   1 
ATOM   1671 C  CG   . MET   A 1 228 ? 29.151  20.062  13.781  1.00 16.31 ? 232 MET   A CG   1 
ATOM   1672 S  SD   . MET   A 1 228 ? 30.398  19.674  12.536  1.00 15.77 ? 232 MET   A SD   1 
ATOM   1673 C  CE   . MET   A 1 228 ? 31.260  18.300  13.310  1.00 15.37 ? 232 MET   A CE   1 
ATOM   1674 N  N    . TYR   A 1 229 ? 25.189  20.442  13.966  1.00 18.79 ? 233 TYR   A N    1 
ATOM   1675 C  CA   . TYR   A 1 229 ? 24.332  21.578  13.678  1.00 20.57 ? 233 TYR   A CA   1 
ATOM   1676 C  C    . TYR   A 1 229 ? 22.979  21.052  13.216  1.00 24.09 ? 233 TYR   A C    1 
ATOM   1677 O  O    . TYR   A 1 229 ? 22.849  19.876  12.888  1.00 23.43 ? 233 TYR   A O    1 
ATOM   1678 C  CB   . TYR   A 1 229 ? 24.924  22.473  12.588  1.00 19.88 ? 233 TYR   A CB   1 
ATOM   1679 C  CG   . TYR   A 1 229 ? 25.339  21.752  11.312  1.00 17.82 ? 233 TYR   A CG   1 
ATOM   1680 C  CD1  . TYR   A 1 229 ? 24.428  21.465  10.303  1.00 18.33 ? 233 TYR   A CD1  1 
ATOM   1681 C  CD2  . TYR   A 1 229 ? 26.665  21.394  11.101  1.00 16.59 ? 233 TYR   A CD2  1 
ATOM   1682 C  CE1  . TYR   A 1 229 ? 24.817  20.811  9.143   1.00 18.09 ? 233 TYR   A CE1  1 
ATOM   1683 C  CE2  . TYR   A 1 229 ? 27.068  20.747  9.943   1.00 16.05 ? 233 TYR   A CE2  1 
ATOM   1684 C  CZ   . TYR   A 1 229 ? 26.145  20.464  8.955   1.00 16.91 ? 233 TYR   A CZ   1 
ATOM   1685 O  OH   . TYR   A 1 229 ? 26.555  19.825  7.823   1.00 16.50 ? 233 TYR   A OH   1 
ATOM   1686 N  N    . GLY   A 1 230 ? 21.988  21.953  13.180  1.00 29.71 ? 234 GLY   A N    1 
ATOM   1687 C  CA   . GLY   A 1 230 ? 20.660  21.631  12.683  1.00 33.70 ? 234 GLY   A CA   1 
ATOM   1688 C  C    . GLY   A 1 230 ? 19.807  20.977  13.751  1.00 38.19 ? 234 GLY   A C    1 
ATOM   1689 O  O    . GLY   A 1 230 ? 19.477  21.694  14.720  1.00 46.80 ? 234 GLY   A O    1 
ATOM   1690 N  N    . ALA   B 1 1   ? 7.524   -31.552 55.139  1.00 43.20 ? 5   ALA   B N    1 
ATOM   1691 C  CA   . ALA   B 1 1   ? 8.132   -30.220 55.364  1.00 43.81 ? 5   ALA   B CA   1 
ATOM   1692 C  C    . ALA   B 1 1   ? 8.766   -29.781 54.055  1.00 42.49 ? 5   ALA   B C    1 
ATOM   1693 O  O    . ALA   B 1 1   ? 9.989   -29.700 53.949  1.00 46.05 ? 5   ALA   B O    1 
ATOM   1694 C  CB   . ALA   B 1 1   ? 9.151   -30.251 56.489  1.00 45.29 ? 5   ALA   B CB   1 
ATOM   1695 N  N    . LEU   B 1 2   ? 7.899   -29.576 53.058  1.00 39.55 ? 6   LEU   B N    1 
ATOM   1696 C  CA   . LEU   B 1 2   ? 8.312   -29.116 51.744  1.00 38.08 ? 6   LEU   B CA   1 
ATOM   1697 C  C    . LEU   B 1 2   ? 8.021   -27.625 51.656  1.00 37.64 ? 6   LEU   B C    1 
ATOM   1698 O  O    . LEU   B 1 2   ? 6.979   -27.172 52.134  1.00 37.66 ? 6   LEU   B O    1 
ATOM   1699 C  CB   . LEU   B 1 2   ? 7.575   -29.879 50.645  1.00 37.04 ? 6   LEU   B CB   1 
ATOM   1700 C  CG   . LEU   B 1 2   ? 7.521   -31.401 50.796  1.00 36.06 ? 6   LEU   B CG   1 
ATOM   1701 C  CD1  . LEU   B 1 2   ? 6.917   -32.060 49.565  1.00 34.62 ? 6   LEU   B CD1  1 
ATOM   1702 C  CD2  . LEU   B 1 2   ? 8.897   -31.957 51.083  1.00 36.57 ? 6   LEU   B CD2  1 
ATOM   1703 N  N    . PRO   B 1 3   ? 8.933   -26.821 51.063  1.00 37.55 ? 7   PRO   B N    1 
ATOM   1704 C  CA   . PRO   B 1 3   ? 8.666   -25.399 50.851  1.00 36.88 ? 7   PRO   B CA   1 
ATOM   1705 C  C    . PRO   B 1 3   ? 7.597   -25.087 49.800  1.00 35.32 ? 7   PRO   B C    1 
ATOM   1706 O  O    . PRO   B 1 3   ? 6.922   -24.068 49.923  1.00 36.21 ? 7   PRO   B O    1 
ATOM   1707 C  CB   . PRO   B 1 3   ? 10.061  -24.847 50.467  1.00 37.70 ? 7   PRO   B CB   1 
ATOM   1708 C  CG   . PRO   B 1 3   ? 10.771  -26.022 49.824  1.00 37.66 ? 7   PRO   B CG   1 
ATOM   1709 C  CD   . PRO   B 1 3   ? 10.283  -27.219 50.628  1.00 37.53 ? 7   PRO   B CD   1 
ATOM   1710 N  N    . HIS   B 1 4   ? 7.426   -25.950 48.784  1.00 34.51 ? 8   HIS   B N    1 
ATOM   1711 C  CA   . HIS   B 1 4   ? 6.651   -25.569 47.603  1.00 34.25 ? 8   HIS   B CA   1 
ATOM   1712 C  C    . HIS   B 1 4   ? 5.901   -26.736 46.957  1.00 31.68 ? 8   HIS   B C    1 
ATOM   1713 O  O    . HIS   B 1 4   ? 5.795   -26.803 45.732  1.00 34.95 ? 8   HIS   B O    1 
ATOM   1714 C  CB   . HIS   B 1 4   ? 7.561   -24.898 46.571  1.00 34.16 ? 8   HIS   B CB   1 
ATOM   1715 C  CG   . HIS   B 1 4   ? 8.185   -23.642 47.084  1.00 36.18 ? 8   HIS   B CG   1 
ATOM   1716 N  ND1  . HIS   B 1 4   ? 9.527   -23.514 47.376  1.00 36.78 ? 8   HIS   B ND1  1 
ATOM   1717 C  CD2  . HIS   B 1 4   ? 7.629   -22.447 47.338  1.00 36.31 ? 8   HIS   B CD2  1 
ATOM   1718 C  CE1  . HIS   B 1 4   ? 9.762   -22.278 47.806  1.00 37.19 ? 8   HIS   B CE1  1 
ATOM   1719 N  NE2  . HIS   B 1 4   ? 8.620   -21.617 47.801  1.00 38.28 ? 8   HIS   B NE2  1 
ATOM   1720 N  N    . GLY   B 1 5   ? 5.337   -27.643 47.759  1.00 28.62 ? 9   GLY   B N    1 
ATOM   1721 C  CA   . GLY   B 1 5   ? 4.649   -28.792 47.189  1.00 25.09 ? 9   GLY   B CA   1 
ATOM   1722 C  C    . GLY   B 1 5   ? 5.629   -29.686 46.430  1.00 21.98 ? 9   GLY   B C    1 
ATOM   1723 O  O    . GLY   B 1 5   ? 6.828   -29.418 46.408  1.00 24.43 ? 9   GLY   B O    1 
ATOM   1724 N  N    A HIS   B 1 6   ? 5.099   -30.765 45.828  0.50 17.93 ? 10  HIS   B N    1 
ATOM   1725 N  N    B HIS   B 1 6   ? 5.135   -30.734 45.782  0.50 19.44 ? 10  HIS   B N    1 
ATOM   1726 C  CA   A HIS   B 1 6   ? 5.882   -31.702 45.030  0.50 15.73 ? 10  HIS   B CA   1 
ATOM   1727 C  CA   B HIS   B 1 6   ? 6.068   -31.639 45.141  0.50 17.91 ? 10  HIS   B CA   1 
ATOM   1728 C  C    A HIS   B 1 6   ? 6.376   -30.995 43.760  0.50 15.27 ? 10  HIS   B C    1 
ATOM   1729 C  C    B HIS   B 1 6   ? 6.340   -31.168 43.715  0.50 16.55 ? 10  HIS   B C    1 
ATOM   1730 O  O    A HIS   B 1 6   ? 5.682   -30.154 43.190  0.50 15.25 ? 10  HIS   B O    1 
ATOM   1731 O  O    B HIS   B 1 6   ? 5.461   -30.694 42.998  0.50 16.97 ? 10  HIS   B O    1 
ATOM   1732 C  CB   A HIS   B 1 6   ? 5.058   -32.956 44.669  0.50 14.29 ? 10  HIS   B CB   1 
ATOM   1733 C  CB   B HIS   B 1 6   ? 5.608   -33.088 45.284  0.50 17.92 ? 10  HIS   B CB   1 
ATOM   1734 C  CG   A HIS   B 1 6   ? 4.853   -34.024 45.724  0.50 13.61 ? 10  HIS   B CG   1 
ATOM   1735 C  CG   B HIS   B 1 6   ? 4.498   -33.466 44.376  0.50 17.99 ? 10  HIS   B CG   1 
ATOM   1736 N  ND1  A HIS   B 1 6   ? 5.467   -34.067 46.958  0.50 13.64 ? 10  HIS   B ND1  1 
ATOM   1737 N  ND1  B HIS   B 1 6   ? 3.732   -34.577 44.643  0.50 18.60 ? 10  HIS   B ND1  1 
ATOM   1738 C  CD2  A HIS   B 1 6   ? 4.077   -35.126 45.673  0.50 12.80 ? 10  HIS   B CD2  1 
ATOM   1739 C  CD2  B HIS   B 1 6   ? 4.038   -32.956 43.226  0.50 18.37 ? 10  HIS   B CD2  1 
ATOM   1740 C  CE1  A HIS   B 1 6   ? 5.058   -35.150 47.630  0.50 12.98 ? 10  HIS   B CE1  1 
ATOM   1741 C  CE1  B HIS   B 1 6   ? 2.838   -34.740 43.671  0.50 17.13 ? 10  HIS   B CE1  1 
ATOM   1742 N  NE2  A HIS   B 1 6   ? 4.223   -35.825 46.855  0.50 12.67 ? 10  HIS   B NE2  1 
ATOM   1743 N  NE2  B HIS   B 1 6   ? 2.988   -33.745 42.816  0.50 18.07 ? 10  HIS   B NE2  1 
ATOM   1744 N  N    . MET   B 1 7   ? 7.601   -31.305 43.324  1.00 15.06 ? 11  MET   B N    1 
ATOM   1745 C  CA   . MET   B 1 7   ? 8.038   -30.938 41.988  1.00 14.88 ? 11  MET   B CA   1 
ATOM   1746 C  C    . MET   B 1 7   ? 7.528   -31.998 41.012  1.00 15.08 ? 11  MET   B C    1 
ATOM   1747 O  O    . MET   B 1 7   ? 7.803   -33.177 41.201  1.00 15.89 ? 11  MET   B O    1 
ATOM   1748 C  CB   . MET   B 1 7   ? 9.570   -30.851 41.957  1.00 15.41 ? 11  MET   B CB   1 
ATOM   1749 C  CG   . MET   B 1 7   ? 10.142  -29.822 42.916  1.00 15.84 ? 11  MET   B CG   1 
ATOM   1750 S  SD   . MET   B 1 7   ? 9.679   -28.129 42.493  1.00 16.55 ? 11  MET   B SD   1 
ATOM   1751 C  CE   . MET   B 1 7   ? 8.532   -27.719 43.815  1.00 16.94 ? 11  MET   B CE   1 
ATOM   1752 N  N    A GLN   B 1 8   ? 6.788   -31.591 39.973  0.50 14.69 ? 12  GLN   B N    1 
ATOM   1753 N  N    B GLN   B 1 8   ? 6.797   -31.572 39.975  0.50 15.34 ? 12  GLN   B N    1 
ATOM   1754 C  CA   A GLN   B 1 8   ? 6.193   -32.559 39.059  0.50 14.76 ? 12  GLN   B CA   1 
ATOM   1755 C  CA   B GLN   B 1 8   ? 6.175   -32.504 39.044  0.50 16.08 ? 12  GLN   B CA   1 
ATOM   1756 C  C    A GLN   B 1 8   ? 7.171   -32.962 37.957  0.50 14.46 ? 12  GLN   B C    1 
ATOM   1757 C  C    B GLN   B 1 8   ? 7.171   -32.954 37.976  0.50 15.03 ? 12  GLN   B C    1 
ATOM   1758 O  O    A GLN   B 1 8   ? 7.108   -34.090 37.474  0.50 14.51 ? 12  GLN   B O    1 
ATOM   1759 O  O    B GLN   B 1 8   ? 7.119   -34.100 37.535  0.50 14.98 ? 12  GLN   B O    1 
ATOM   1760 C  CB   A GLN   B 1 8   ? 4.886   -32.052 38.455  0.50 15.50 ? 12  GLN   B CB   1 
ATOM   1761 C  CB   B GLN   B 1 8   ? 4.963   -31.864 38.369  0.50 18.20 ? 12  GLN   B CB   1 
ATOM   1762 C  CG   A GLN   B 1 8   ? 3.756   -31.977 39.471  0.50 16.15 ? 12  GLN   B CG   1 
ATOM   1763 C  CG   B GLN   B 1 8   ? 3.836   -32.845 38.086  0.50 20.28 ? 12  GLN   B CG   1 
ATOM   1764 C  CD   A GLN   B 1 8   ? 3.454   -33.324 40.090  0.50 17.28 ? 12  GLN   B CD   1 
ATOM   1765 C  CD   B GLN   B 1 8   ? 3.250   -33.428 39.352  0.50 22.46 ? 12  GLN   B CD   1 
ATOM   1766 O  OE1  A GLN   B 1 8   ? 3.413   -33.478 41.317  0.50 18.92 ? 12  GLN   B OE1  1 
ATOM   1767 O  OE1  B GLN   B 1 8   ? 2.700   -32.718 40.201  0.50 25.86 ? 12  GLN   B OE1  1 
ATOM   1768 N  NE2  A GLN   B 1 8   ? 3.223   -34.311 39.236  0.50 18.35 ? 12  GLN   B NE2  1 
ATOM   1769 N  NE2  B GLN   B 1 8   ? 3.373   -34.736 39.495  0.50 23.71 ? 12  GLN   B NE2  1 
ATOM   1770 N  N    . THR   B 1 9   ? 8.045   -32.033 37.549  1.00 14.02 ? 13  THR   B N    1 
ATOM   1771 C  CA   . THR   B 1 9   ? 9.040   -32.302 36.520  1.00 14.14 ? 13  THR   B CA   1 
ATOM   1772 C  C    . THR   B 1 9   ? 10.398  -31.897 37.075  1.00 13.39 ? 13  THR   B C    1 
ATOM   1773 O  O    . THR   B 1 9   ? 10.543  -30.780 37.560  1.00 14.89 ? 13  THR   B O    1 
ATOM   1774 C  CB   . THR   B 1 9   ? 8.757   -31.535 35.227  1.00 15.13 ? 13  THR   B CB   1 
ATOM   1775 O  OG1  . THR   B 1 9   ? 7.456   -31.883 34.769  1.00 15.67 ? 13  THR   B OG1  1 
ATOM   1776 C  CG2  . THR   B 1 9   ? 9.772   -31.880 34.155  1.00 16.05 ? 13  THR   B CG2  1 
ATOM   1777 N  N    . LEU   B 1 10  ? 11.371  -32.811 36.989  1.00 12.91 ? 14  LEU   B N    1 
ATOM   1778 C  CA   . LEU   B 1 10  ? 12.761  -32.482 37.249  1.00 13.42 ? 14  LEU   B CA   1 
ATOM   1779 C  C    . LEU   B 1 10  ? 13.423  -32.275 35.898  1.00 12.81 ? 14  LEU   B C    1 
ATOM   1780 O  O    . LEU   B 1 10  ? 13.402  -33.177 35.056  1.00 13.53 ? 14  LEU   B O    1 
ATOM   1781 C  CB   . LEU   B 1 10  ? 13.467  -33.561 38.063  1.00 14.93 ? 14  LEU   B CB   1 
ATOM   1782 C  CG   . LEU   B 1 10  ? 13.289  -33.456 39.585  1.00 17.57 ? 14  LEU   B CG   1 
ATOM   1783 C  CD1  . LEU   B 1 10  ? 11.869  -33.475 40.057  1.00 19.41 ? 14  LEU   B CD1  1 
ATOM   1784 C  CD2  . LEU   B 1 10  ? 14.128  -34.526 40.235  1.00 18.96 ? 14  LEU   B CD2  1 
ATOM   1785 N  N    . ILE   B 1 11  ? 13.961  -31.074 35.690  1.00 12.26 ? 15  ILE   B N    1 
ATOM   1786 C  CA   . ILE   B 1 11  ? 14.661  -30.768 34.459  1.00 12.65 ? 15  ILE   B CA   1 
ATOM   1787 C  C    . ILE   B 1 11  ? 16.153  -30.783 34.768  1.00 12.03 ? 15  ILE   B C    1 
ATOM   1788 O  O    . ILE   B 1 11  ? 16.705  -29.816 35.299  1.00 12.15 ? 15  ILE   B O    1 
ATOM   1789 C  CB   . ILE   B 1 11  ? 14.219  -29.434 33.839  1.00 14.27 ? 15  ILE   B CB   1 
ATOM   1790 C  CG1  . ILE   B 1 11  ? 12.694  -29.388 33.626  1.00 16.54 ? 15  ILE   B CG1  1 
ATOM   1791 C  CG2  . ILE   B 1 11  ? 14.981  -29.174 32.537  1.00 14.72 ? 15  ILE   B CG2  1 
ATOM   1792 C  CD1  . ILE   B 1 11  ? 11.956  -28.681 34.730  1.00 19.58 ? 15  ILE   B CD1  1 
ATOM   1793 N  N    . PHE   B 1 12  ? 16.788  -31.905 34.451  1.00 11.76 ? 16  PHE   B N    1 
ATOM   1794 C  CA   . PHE   B 1 12  ? 18.228  -32.004 34.576  1.00 11.72 ? 16  PHE   B CA   1 
ATOM   1795 C  C    . PHE   B 1 12  ? 18.833  -31.047 33.559  1.00 11.62 ? 16  PHE   B C    1 
ATOM   1796 O  O    . PHE   B 1 12  ? 18.420  -31.019 32.401  1.00 12.54 ? 16  PHE   B O    1 
ATOM   1797 C  CB   . PHE   B 1 12  ? 18.645  -33.466 34.415  1.00 12.35 ? 16  PHE   B CB   1 
ATOM   1798 C  CG   . PHE   B 1 12  ? 18.128  -34.322 35.558  1.00 12.97 ? 16  PHE   B CG   1 
ATOM   1799 C  CD1  . PHE   B 1 12  ? 18.860  -34.449 36.729  1.00 13.92 ? 16  PHE   B CD1  1 
ATOM   1800 C  CD2  . PHE   B 1 12  ? 16.900  -34.964 35.480  1.00 13.87 ? 16  PHE   B CD2  1 
ATOM   1801 C  CE1  . PHE   B 1 12  ? 18.389  -35.215 37.775  1.00 15.00 ? 16  PHE   B CE1  1 
ATOM   1802 C  CE2  . PHE   B 1 12  ? 16.437  -35.728 36.541  1.00 14.73 ? 16  PHE   B CE2  1 
ATOM   1803 C  CZ   . PHE   B 1 12  ? 17.173  -35.830 37.689  1.00 14.78 ? 16  PHE   B CZ   1 
ATOM   1804 N  N    . PHE   B 1 13  ? 19.811  -30.267 34.009  1.00 11.75 ? 17  PHE   B N    1 
ATOM   1805 C  CA   . PHE   B 1 13  ? 20.211  -29.074 33.291  1.00 11.51 ? 17  PHE   B CA   1 
ATOM   1806 C  C    . PHE   B 1 13  ? 21.718  -28.905 33.384  1.00 11.72 ? 17  PHE   B C    1 
ATOM   1807 O  O    . PHE   B 1 13  ? 22.291  -29.018 34.464  1.00 12.12 ? 17  PHE   B O    1 
ATOM   1808 C  CB   . PHE   B 1 13  ? 19.489  -27.877 33.915  1.00 11.75 ? 17  PHE   B CB   1 
ATOM   1809 C  CG   . PHE   B 1 13  ? 19.812  -26.507 33.344  1.00 12.23 ? 17  PHE   B CG   1 
ATOM   1810 C  CD1  . PHE   B 1 13  ? 19.766  -26.267 31.973  1.00 12.86 ? 17  PHE   B CD1  1 
ATOM   1811 C  CD2  . PHE   B 1 13  ? 20.117  -25.444 34.182  1.00 12.78 ? 17  PHE   B CD2  1 
ATOM   1812 C  CE1  . PHE   B 1 13  ? 20.042  -25.007 31.459  1.00 13.09 ? 17  PHE   B CE1  1 
ATOM   1813 C  CE2  . PHE   B 1 13  ? 20.411  -24.196 33.661  1.00 13.15 ? 17  PHE   B CE2  1 
ATOM   1814 C  CZ   . PHE   B 1 13  ? 20.366  -23.972 32.304  1.00 12.83 ? 17  PHE   B CZ   1 
ATOM   1815 N  N    . ASP   B 1 14  ? 22.336  -28.603 32.246  1.00 11.07 ? 18  ASP   B N    1 
ATOM   1816 C  CA   . ASP   B 1 14  ? 23.748  -28.280 32.237  1.00 11.24 ? 18  ASP   B CA   1 
ATOM   1817 C  C    . ASP   B 1 14  ? 24.036  -27.316 31.098  1.00 10.99 ? 18  ASP   B C    1 
ATOM   1818 O  O    . ASP   B 1 14  ? 23.498  -27.474 30.013  1.00 11.17 ? 18  ASP   B O    1 
ATOM   1819 C  CB   . ASP   B 1 14  ? 24.622  -29.508 32.069  1.00 12.36 ? 18  ASP   B CB   1 
ATOM   1820 C  CG   . ASP   B 1 14  ? 26.080  -29.244 32.390  1.00 13.78 ? 18  ASP   B CG   1 
ATOM   1821 O  OD1  . ASP   B 1 14  ? 26.364  -29.009 33.587  1.00 13.54 ? 18  ASP   B OD1  1 
ATOM   1822 O  OD2  . ASP   B 1 14  ? 26.898  -29.248 31.445  1.00 14.75 ? 18  ASP   B OD2  1 
ATOM   1823 N  N    . MET   B 1 15  ? 24.930  -26.360 31.353  1.00 10.93 ? 19  MET   B N    1 
ATOM   1824 C  CA   . MET   B 1 15  ? 25.421  -25.473 30.317  1.00 10.83 ? 19  MET   B CA   1 
ATOM   1825 C  C    . MET   B 1 15  ? 26.942  -25.497 30.263  1.00 10.87 ? 19  MET   B C    1 
ATOM   1826 O  O    . MET   B 1 15  ? 27.609  -25.739 31.262  1.00 11.97 ? 19  MET   B O    1 
ATOM   1827 C  CB   . MET   B 1 15  ? 24.945  -24.035 30.537  1.00 11.69 ? 19  MET   B CB   1 
ATOM   1828 C  CG   . MET   B 1 15  ? 23.435  -23.945 30.581  1.00 12.34 ? 19  MET   B CG   1 
ATOM   1829 S  SD   . MET   B 1 15  ? 22.770  -22.312 30.214  1.00 14.08 ? 19  MET   B SD   1 
ATOM   1830 C  CE   . MET   B 1 15  ? 23.437  -21.399 31.606  1.00 13.71 ? 19  MET   B CE   1 
ATOM   1831 N  N    A GLU   B 1 16  ? 27.476  -25.260 29.058  0.50 10.86 ? 20  GLU   B N    1 
ATOM   1832 N  N    B GLU   B 1 16  ? 27.471  -25.211 29.073  0.50 10.80 ? 20  GLU   B N    1 
ATOM   1833 C  CA   A GLU   B 1 16  ? 28.881  -24.941 28.862  0.50 11.27 ? 20  GLU   B CA   1 
ATOM   1834 C  CA   B GLU   B 1 16  ? 28.880  -24.915 28.908  0.50 11.04 ? 20  GLU   B CA   1 
ATOM   1835 C  C    A GLU   B 1 16  ? 28.976  -23.436 28.635  0.50 10.95 ? 20  GLU   B C    1 
ATOM   1836 C  C    B GLU   B 1 16  ? 29.005  -23.440 28.566  0.50 10.80 ? 20  GLU   B C    1 
ATOM   1837 O  O    A GLU   B 1 16  ? 28.008  -22.816 28.191  0.50 10.89 ? 20  GLU   B O    1 
ATOM   1838 O  O    B GLU   B 1 16  ? 28.099  -22.857 27.972  0.50 10.77 ? 20  GLU   B O    1 
ATOM   1839 C  CB   A GLU   B 1 16  ? 29.464  -25.694 27.662  0.50 12.44 ? 20  GLU   B CB   1 
ATOM   1840 C  CB   B GLU   B 1 16  ? 29.478  -25.827 27.841  0.50 12.12 ? 20  GLU   B CB   1 
ATOM   1841 C  CG   A GLU   B 1 16  ? 29.283  -27.212 27.694  0.50 13.91 ? 20  GLU   B CG   1 
ATOM   1842 C  CG   B GLU   B 1 16  ? 29.473  -27.286 28.280  0.50 13.33 ? 20  GLU   B CG   1 
ATOM   1843 C  CD   A GLU   B 1 16  ? 30.152  -27.985 28.678  0.50 16.07 ? 20  GLU   B CD   1 
ATOM   1844 C  CD   B GLU   B 1 16  ? 30.116  -28.256 27.313  0.50 14.93 ? 20  GLU   B CD   1 
ATOM   1845 O  OE1  A GLU   B 1 16  ? 30.919  -27.362 29.435  0.50 18.24 ? 20  GLU   B OE1  1 
ATOM   1846 O  OE1  B GLU   B 1 16  ? 30.353  -27.876 26.158  0.50 17.64 ? 20  GLU   B OE1  1 
ATOM   1847 O  OE2  A GLU   B 1 16  ? 30.062  -29.237 28.700  0.50 18.47 ? 20  GLU   B OE2  1 
ATOM   1848 O  OE2  B GLU   B 1 16  ? 30.424  -29.379 27.735  0.50 16.42 ? 20  GLU   B OE2  1 
ATOM   1849 N  N    . ALA   B 1 17  ? 30.139  -22.859 28.950  1.00 10.84 ? 21  ALA   B N    1 
ATOM   1850 C  CA   . ALA   B 1 17  ? 30.345  -21.429 28.807  1.00 10.85 ? 21  ALA   B CA   1 
ATOM   1851 C  C    . ALA   B 1 17  ? 31.775  -21.140 28.360  1.00 11.16 ? 21  ALA   B C    1 
ATOM   1852 O  O    . ALA   B 1 17  ? 32.627  -22.022 28.318  1.00 11.94 ? 21  ALA   B O    1 
ATOM   1853 C  CB   . ALA   B 1 17  ? 30.025  -20.735 30.109  1.00 11.57 ? 21  ALA   B CB   1 
ATOM   1854 N  N    . THR   B 1 18  ? 32.024  -19.864 28.073  1.00 10.80 ? 22  THR   B N    1 
ATOM   1855 C  CA   . THR   B 1 18  ? 33.313  -19.396 27.586  1.00 11.11 ? 22  THR   B CA   1 
ATOM   1856 C  C    . THR   B 1 18  ? 34.401  -19.402 28.652  1.00 11.08 ? 22  THR   B C    1 
ATOM   1857 O  O    . THR   B 1 18  ? 35.570  -19.280 28.314  1.00 12.55 ? 22  THR   B O    1 
ATOM   1858 C  CB   . THR   B 1 18  ? 33.169  -17.984 27.017  1.00 11.56 ? 22  THR   B CB   1 
ATOM   1859 O  OG1  . THR   B 1 18  ? 32.575  -17.125 27.994  1.00 11.62 ? 22  THR   B OG1  1 
ATOM   1860 C  CG2  . THR   B 1 18  ? 32.339  -17.948 25.748  1.00 11.55 ? 22  THR   B CG2  1 
ATOM   1861 N  N    . GLY   B 1 19  ? 34.030  -19.475 29.928  1.00 11.12 ? 23  GLY   B N    1 
ATOM   1862 C  CA   . GLY   B 1 19  ? 34.982  -19.375 31.018  1.00 11.53 ? 23  GLY   B CA   1 
ATOM   1863 C  C    . GLY   B 1 19  ? 34.271  -19.507 32.354  1.00 11.69 ? 23  GLY   B C    1 
ATOM   1864 O  O    . GLY   B 1 19  ? 33.078  -19.786 32.392  1.00 11.32 ? 23  GLY   B O    1 
ATOM   1865 N  N    . LEU   B 1 20  ? 35.021  -19.285 33.434  1.00 12.51 ? 24  LEU   B N    1 
ATOM   1866 C  CA   . LEU   B 1 20  ? 34.485  -19.381 34.782  1.00 12.61 ? 24  LEU   B CA   1 
ATOM   1867 C  C    . LEU   B 1 20  ? 33.849  -18.051 35.183  1.00 13.10 ? 24  LEU   B C    1 
ATOM   1868 O  O    . LEU   B 1 20  ? 34.032  -17.030 34.515  1.00 13.07 ? 24  LEU   B O    1 
ATOM   1869 C  CB   . LEU   B 1 20  ? 35.610  -19.816 35.719  1.00 13.43 ? 24  LEU   B CB   1 
ATOM   1870 C  CG   . LEU   B 1 20  ? 36.152  -21.222 35.465  1.00 14.95 ? 24  LEU   B CG   1 
ATOM   1871 C  CD1  . LEU   B 1 20  ? 37.276  -21.528 36.423  1.00 16.21 ? 24  LEU   B CD1  1 
ATOM   1872 C  CD2  . LEU   B 1 20  ? 35.057  -22.257 35.584  1.00 16.38 ? 24  LEU   B CD2  1 
ATOM   1873 N  N    . PRO   B 1 21  ? 33.041  -18.019 36.267  1.00 13.76 ? 25  PRO   B N    1 
ATOM   1874 C  CA   . PRO   B 1 21  ? 32.283  -16.811 36.598  1.00 14.36 ? 25  PRO   B CA   1 
ATOM   1875 C  C    . PRO   B 1 21  ? 33.042  -15.489 36.656  1.00 15.37 ? 25  PRO   B C    1 
ATOM   1876 O  O    . PRO   B 1 21  ? 32.502  -14.477 36.208  1.00 16.66 ? 25  PRO   B O    1 
ATOM   1877 C  CB   . PRO   B 1 21  ? 31.647  -17.190 37.945  1.00 14.27 ? 25  PRO   B CB   1 
ATOM   1878 C  CG   . PRO   B 1 21  ? 31.404  -18.676 37.797  1.00 13.98 ? 25  PRO   B CG   1 
ATOM   1879 C  CD   . PRO   B 1 21  ? 32.648  -19.179 37.083  1.00 13.94 ? 25  PRO   B CD   1 
ATOM   1880 N  N    . SER   B 1 22  ? 34.290  -15.491 37.141  1.00 16.22 ? 26  SER   B N    1 
ATOM   1881 C  CA   . SER   B 1 22  ? 35.021  -14.232 37.240  1.00 17.60 ? 26  SER   B CA   1 
ATOM   1882 C  C    . SER   B 1 22  ? 35.272  -13.576 35.878  1.00 16.30 ? 26  SER   B C    1 
ATOM   1883 O  O    . SER   B 1 22  ? 35.553  -12.373 35.826  1.00 17.43 ? 26  SER   B O    1 
ATOM   1884 C  CB   . SER   B 1 22  ? 36.301  -14.394 37.996  1.00 19.28 ? 26  SER   B CB   1 
ATOM   1885 O  OG   . SER   B 1 22  ? 37.183  -15.272 37.331  1.00 21.96 ? 26  SER   B OG   1 
ATOM   1886 N  N    . SER   B 1 23  ? 35.183  -14.366 34.799  1.00 14.74 ? 27  SER   B N    1 
ATOM   1887 C  CA   . SER   B 1 23  ? 35.453  -13.910 33.440  1.00 14.01 ? 27  SER   B CA   1 
ATOM   1888 C  C    . SER   B 1 23  ? 34.241  -13.279 32.759  1.00 13.65 ? 27  SER   B C    1 
ATOM   1889 O  O    . SER   B 1 23  ? 34.354  -12.874 31.602  1.00 14.84 ? 27  SER   B O    1 
ATOM   1890 C  CB   . SER   B 1 23  ? 35.989  -15.042 32.575  1.00 13.82 ? 27  SER   B CB   1 
ATOM   1891 O  OG   . SER   B 1 23  ? 34.978  -15.981 32.228  1.00 14.00 ? 27  SER   B OG   1 
ATOM   1892 N  N    . ARG   B 1 24  ? 33.094  -13.203 33.442  1.00 13.35 ? 28  ARG   B N    1 
ATOM   1893 C  CA   . ARG   B 1 24  ? 31.861  -12.690 32.851  1.00 13.41 ? 28  ARG   B CA   1 
ATOM   1894 C  C    . ARG   B 1 24  ? 31.528  -13.528 31.615  1.00 12.36 ? 28  ARG   B C    1 
ATOM   1895 O  O    . ARG   B 1 24  ? 31.473  -13.032 30.477  1.00 12.95 ? 28  ARG   B O    1 
ATOM   1896 C  CB   . ARG   B 1 24  ? 31.926  -11.202 32.492  1.00 14.28 ? 28  ARG   B CB   1 
ATOM   1897 C  CG   . ARG   B 1 24  ? 30.583  -10.590 32.125  1.00 15.86 ? 28  ARG   B CG   1 
ATOM   1898 C  CD   . ARG   B 1 24  ? 30.728  -9.466  31.108  1.00 17.66 ? 28  ARG   B CD   1 
ATOM   1899 N  NE   . ARG   B 1 24  ? 29.472  -9.114  30.440  1.00 19.21 ? 28  ARG   B NE   1 
ATOM   1900 C  CZ   . ARG   B 1 24  ? 28.914  -9.775  29.424  1.00 19.81 ? 28  ARG   B CZ   1 
ATOM   1901 N  NH1  . ARG   B 1 24  ? 27.840  -9.261  28.843  1.00 21.89 ? 28  ARG   B NH1  1 
ATOM   1902 N  NH2  . ARG   B 1 24  ? 29.432  -10.920 28.974  1.00 20.42 ? 28  ARG   B NH2  1 
ATOM   1903 N  N    . PRO   B 1 25  ? 31.335  -14.852 31.794  1.00 12.36 ? 29  PRO   B N    1 
ATOM   1904 C  CA   . PRO   B 1 25  ? 31.239  -15.765 30.657  1.00 12.04 ? 29  PRO   B CA   1 
ATOM   1905 C  C    . PRO   B 1 25  ? 29.875  -15.711 29.988  1.00 12.11 ? 29  PRO   B C    1 
ATOM   1906 O  O    . PRO   B 1 25  ? 28.905  -15.221 30.564  1.00 12.05 ? 29  PRO   B O    1 
ATOM   1907 C  CB   . PRO   B 1 25  ? 31.491  -17.122 31.317  1.00 12.11 ? 29  PRO   B CB   1 
ATOM   1908 C  CG   . PRO   B 1 25  ? 30.838  -16.968 32.673  1.00 11.93 ? 29  PRO   B CG   1 
ATOM   1909 C  CD   . PRO   B 1 25  ? 31.236  -15.549 33.082  1.00 11.73 ? 29  PRO   B CD   1 
ATOM   1910 N  N    . GLU   B 1 26  ? 29.827  -16.289 28.787  1.00 11.83 ? 30  GLU   B N    1 
ATOM   1911 C  CA   . GLU   B 1 26  ? 28.595  -16.449 28.038  1.00 12.04 ? 30  GLU   B CA   1 
ATOM   1912 C  C    . GLU   B 1 26  ? 28.403  -17.920 27.671  1.00 10.97 ? 30  GLU   B C    1 
ATOM   1913 O  O    . GLU   B 1 26  ? 29.352  -18.689 27.552  1.00 11.69 ? 30  GLU   B O    1 
ATOM   1914 C  CB   . GLU   B 1 26  ? 28.611  -15.549 26.807  1.00 13.37 ? 30  GLU   B CB   1 
ATOM   1915 C  CG   . GLU   B 1 26  ? 28.681  -14.076 27.197  1.00 14.66 ? 30  GLU   B CG   1 
ATOM   1916 C  CD   . GLU   B 1 26  ? 28.394  -13.080 26.098  1.00 16.61 ? 30  GLU   B CD   1 
ATOM   1917 O  OE1  . GLU   B 1 26  ? 27.914  -13.470 25.004  1.00 17.85 ? 30  GLU   B OE1  1 
ATOM   1918 O  OE2  . GLU   B 1 26  ? 28.620  -11.882 26.382  1.00 19.30 ? 30  GLU   B OE2  1 
ATOM   1919 N  N    . VAL   B 1 27  ? 27.138  -18.301 27.519  1.00 11.24 ? 31  VAL   B N    1 
ATOM   1920 C  CA   . VAL   B 1 27  ? 26.764  -19.668 27.197  1.00 10.95 ? 31  VAL   B CA   1 
ATOM   1921 C  C    . VAL   B 1 27  ? 27.245  -20.059 25.803  1.00 10.81 ? 31  VAL   B C    1 
ATOM   1922 O  O    . VAL   B 1 27  ? 27.063  -19.317 24.832  1.00 11.28 ? 31  VAL   B O    1 
ATOM   1923 C  CB   . VAL   B 1 27  ? 25.232  -19.807 27.295  1.00 11.28 ? 31  VAL   B CB   1 
ATOM   1924 C  CG1  . VAL   B 1 27  ? 24.747  -21.168 26.803  1.00 11.73 ? 31  VAL   B CG1  1 
ATOM   1925 C  CG2  . VAL   B 1 27  ? 24.752  -19.550 28.716  1.00 11.68 ? 31  VAL   B CG2  1 
ATOM   1926 N  N    . THR   B 1 28  ? 27.770  -21.287 25.705  1.00 10.49 ? 32  THR   B N    1 
ATOM   1927 C  CA   . THR   B 1 28  ? 28.134  -21.913 24.442  1.00 10.68 ? 32  THR   B CA   1 
ATOM   1928 C  C    . THR   B 1 28  ? 27.288  -23.147 24.146  1.00 10.76 ? 32  THR   B C    1 
ATOM   1929 O  O    . THR   B 1 28  ? 27.189  -23.550 22.983  1.00 10.75 ? 32  THR   B O    1 
ATOM   1930 C  CB   . THR   B 1 28  ? 29.614  -22.291 24.441  1.00 11.16 ? 32  THR   B CB   1 
ATOM   1931 O  OG1  . THR   B 1 28  ? 29.841  -23.171 25.545  1.00 11.67 ? 32  THR   B OG1  1 
ATOM   1932 C  CG2  . THR   B 1 28  ? 30.488  -21.055 24.517  1.00 11.83 ? 32  THR   B CG2  1 
ATOM   1933 N  N    . GLU   B 1 29  ? 26.730  -23.790 25.176  1.00 10.73 ? 33  GLU   B N    1 
ATOM   1934 C  CA   . GLU   B 1 29  ? 25.889  -24.953 24.953  1.00 11.02 ? 33  GLU   B CA   1 
ATOM   1935 C  C    . GLU   B 1 29  ? 24.965  -25.127 26.147  1.00 10.80 ? 33  GLU   B C    1 
ATOM   1936 O  O    . GLU   B 1 29  ? 25.333  -24.777 27.265  1.00 10.99 ? 33  GLU   B O    1 
ATOM   1937 C  CB   . GLU   B 1 29  ? 26.742  -26.213 24.774  1.00 12.38 ? 33  GLU   B CB   1 
ATOM   1938 C  CG   . GLU   B 1 29  ? 25.987  -27.434 24.256  1.00 13.99 ? 33  GLU   B CG   1 
ATOM   1939 C  CD   . GLU   B 1 29  ? 26.862  -28.674 24.104  1.00 16.05 ? 33  GLU   B CD   1 
ATOM   1940 O  OE1  . GLU   B 1 29  ? 27.740  -28.883 24.965  1.00 17.01 ? 33  GLU   B OE1  1 
ATOM   1941 O  OE2  . GLU   B 1 29  ? 26.633  -29.473 23.166  1.00 18.68 ? 33  GLU   B OE2  1 
ATOM   1942 N  N    . LEU   B 1 30  ? 23.771  -25.669 25.895  1.00 11.10 ? 34  LEU   B N    1 
ATOM   1943 C  CA   . LEU   B 1 30  ? 22.861  -25.978 26.981  1.00 11.41 ? 34  LEU   B CA   1 
ATOM   1944 C  C    . LEU   B 1 30  ? 22.160  -27.291 26.674  1.00 11.22 ? 34  LEU   B C    1 
ATOM   1945 O  O    . LEU   B 1 30  ? 21.923  -27.627 25.510  1.00 11.74 ? 34  LEU   B O    1 
ATOM   1946 C  CB   . LEU   B 1 30  ? 21.868  -24.849 27.248  1.00 12.90 ? 34  LEU   B CB   1 
ATOM   1947 C  CG   . LEU   B 1 30  ? 20.958  -24.450 26.083  1.00 14.42 ? 34  LEU   B CG   1 
ATOM   1948 C  CD1  . LEU   B 1 30  ? 19.693  -25.283 26.069  1.00 14.96 ? 34  LEU   B CD1  1 
ATOM   1949 C  CD2  . LEU   B 1 30  ? 20.621  -22.975 26.140  1.00 15.82 ? 34  LEU   B CD2  1 
ATOM   1950 N  N    . CYS   B 1 31  ? 21.806  -28.011 27.737  1.00 10.89 ? 35  CYS   B N    1 
ATOM   1951 C  CA   . CYS   B 1 31  ? 20.988  -29.207 27.619  1.00 10.86 ? 35  CYS   B CA   1 
ATOM   1952 C  C    . CYS   B 1 31  ? 19.993  -29.234 28.774  1.00 10.56 ? 35  CYS   B C    1 
ATOM   1953 O  O    . CYS   B 1 31  ? 20.374  -29.015 29.930  1.00 11.03 ? 35  CYS   B O    1 
ATOM   1954 C  CB   . CYS   B 1 31  ? 21.847  -30.468 27.618  1.00 12.21 ? 35  CYS   B CB   1 
ATOM   1955 S  SG   . CYS   B 1 31  ? 20.873  -31.993 27.534  1.00 14.97 ? 35  CYS   B SG   1 
ATOM   1956 N  N    . LEU   B 1 32  ? 18.728  -29.493 28.422  1.00 10.89 ? 36  LEU   B N    1 
ATOM   1957 C  CA   . LEU   B 1 32  ? 17.645  -29.739 29.351  1.00 11.14 ? 36  LEU   B CA   1 
ATOM   1958 C  C    . LEU   B 1 32  ? 17.121  -31.142 29.086  1.00 10.98 ? 36  LEU   B C    1 
ATOM   1959 O  O    . LEU   B 1 32  ? 16.849  -31.485 27.936  1.00 11.51 ? 36  LEU   B O    1 
ATOM   1960 C  CB   . LEU   B 1 32  ? 16.489  -28.760 29.155  1.00 11.96 ? 36  LEU   B CB   1 
ATOM   1961 C  CG   . LEU   B 1 32  ? 16.674  -27.314 29.623  1.00 13.41 ? 36  LEU   B CG   1 
ATOM   1962 C  CD1  . LEU   B 1 32  ? 17.734  -26.567 28.872  1.00 14.96 ? 36  LEU   B CD1  1 
ATOM   1963 C  CD2  . LEU   B 1 32  ? 15.328  -26.589 29.494  1.00 14.21 ? 36  LEU   B CD2  1 
ATOM   1964 N  N    A LEU   B 1 33  ? 16.994  -31.928 30.153  0.50 11.39 ? 37  LEU   B N    1 
ATOM   1965 N  N    B LEU   B 1 33  ? 16.951  -31.931 30.148  0.50 11.10 ? 37  LEU   B N    1 
ATOM   1966 C  CA   A LEU   B 1 33  ? 16.381  -33.241 30.095  0.50 11.85 ? 37  LEU   B CA   1 
ATOM   1967 C  CA   B LEU   B 1 33  ? 16.370  -33.258 30.041  0.50 11.30 ? 37  LEU   B CA   1 
ATOM   1968 C  C    A LEU   B 1 33  ? 15.268  -33.270 31.133  0.50 11.46 ? 37  LEU   B C    1 
ATOM   1969 C  C    B LEU   B 1 33  ? 15.280  -33.376 31.102  0.50 11.19 ? 37  LEU   B C    1 
ATOM   1970 O  O    A LEU   B 1 33  ? 15.532  -33.222 32.337  0.50 11.14 ? 37  LEU   B O    1 
ATOM   1971 O  O    B LEU   B 1 33  ? 15.574  -33.508 32.293  0.50 11.15 ? 37  LEU   B O    1 
ATOM   1972 C  CB   A LEU   B 1 33  ? 17.425  -34.319 30.359  0.50 13.17 ? 37  LEU   B CB   1 
ATOM   1973 C  CB   B LEU   B 1 33  ? 17.463  -34.316 30.188  0.50 11.98 ? 37  LEU   B CB   1 
ATOM   1974 C  CG   A LEU   B 1 33  ? 16.918  -35.760 30.265  0.50 14.36 ? 37  LEU   B CG   1 
ATOM   1975 C  CG   B LEU   B 1 33  ? 17.076  -35.747 29.795  0.50 12.46 ? 37  LEU   B CG   1 
ATOM   1976 C  CD1  A LEU   B 1 33  ? 16.566  -36.113 28.829  0.50 14.97 ? 37  LEU   B CD1  1 
ATOM   1977 C  CD1  B LEU   B 1 33  ? 18.280  -36.655 29.591  0.50 12.35 ? 37  LEU   B CD1  1 
ATOM   1978 C  CD2  A LEU   B 1 33  ? 17.939  -36.732 30.829  0.50 15.31 ? 37  LEU   B CD2  1 
ATOM   1979 C  CD2  B LEU   B 1 33  ? 16.167  -36.356 30.832  0.50 13.18 ? 37  LEU   B CD2  1 
ATOM   1980 N  N    . ALA   B 1 34  ? 14.023  -33.266 30.651  1.00 11.34 ? 38  ALA   B N    1 
ATOM   1981 C  CA   . ALA   B 1 34  ? 12.871  -33.218 31.531  1.00 11.86 ? 38  ALA   B CA   1 
ATOM   1982 C  C    . ALA   B 1 34  ? 12.376  -34.627 31.830  1.00 12.09 ? 38  ALA   B C    1 
ATOM   1983 O  O    . ALA   B 1 34  ? 12.035  -35.382 30.922  1.00 12.53 ? 38  ALA   B O    1 
ATOM   1984 C  CB   . ALA   B 1 34  ? 11.791  -32.380 30.902  1.00 12.42 ? 38  ALA   B CB   1 
ATOM   1985 N  N    . VAL   B 1 35  ? 12.310  -34.933 33.126  1.00 13.31 ? 39  VAL   B N    1 
ATOM   1986 C  CA   . VAL   B 1 35  ? 11.907  -36.231 33.638  1.00 14.81 ? 39  VAL   B CA   1 
ATOM   1987 C  C    . VAL   B 1 35  ? 10.720  -36.006 34.563  1.00 14.18 ? 39  VAL   B C    1 
ATOM   1988 O  O    . VAL   B 1 35  ? 10.796  -35.186 35.467  1.00 14.84 ? 39  VAL   B O    1 
ATOM   1989 C  CB   . VAL   B 1 35  ? 13.104  -36.824 34.406  1.00 16.84 ? 39  VAL   B CB   1 
ATOM   1990 C  CG1  . VAL   B 1 35  ? 12.755  -38.117 35.114  1.00 18.92 ? 39  VAL   B CG1  1 
ATOM   1991 C  CG2  . VAL   B 1 35  ? 14.331  -36.978 33.516  1.00 17.07 ? 39  VAL   B CG2  1 
ATOM   1992 N  N    . HIS   B 1 36  ? 9.629   -36.743 34.349  1.00 14.70 ? 40  HIS   B N    1 
ATOM   1993 C  CA   . HIS   B 1 36  ? 8.493   -36.679 35.245  1.00 14.93 ? 40  HIS   B CA   1 
ATOM   1994 C  C    . HIS   B 1 36  ? 8.876   -37.307 36.582  1.00 14.71 ? 40  HIS   B C    1 
ATOM   1995 O  O    . HIS   B 1 36  ? 9.645   -38.267 36.640  1.00 14.69 ? 40  HIS   B O    1 
ATOM   1996 C  CB   . HIS   B 1 36  ? 7.311   -37.418 34.608  1.00 16.79 ? 40  HIS   B CB   1 
ATOM   1997 C  CG   . HIS   B 1 36  ? 6.025   -37.150 35.285  1.00 18.12 ? 40  HIS   B CG   1 
ATOM   1998 N  ND1  . HIS   B 1 36  ? 5.614   -37.842 36.404  1.00 21.05 ? 40  HIS   B ND1  1 
ATOM   1999 C  CD2  . HIS   B 1 36  ? 5.080   -36.245 35.036  1.00 19.96 ? 40  HIS   B CD2  1 
ATOM   2000 C  CE1  . HIS   B 1 36  ? 4.438   -37.371 36.793  1.00 21.72 ? 40  HIS   B CE1  1 
ATOM   2001 N  NE2  . HIS   B 1 36  ? 4.088   -36.410 35.962  1.00 21.60 ? 40  HIS   B NE2  1 
ATOM   2002 N  N    . ARG   B 1 37  ? 8.297   -36.795 37.666  1.00 15.30 ? 41  ARG   B N    1 
ATOM   2003 C  CA   . ARG   B 1 37  ? 8.663   -37.280 38.991  1.00 15.86 ? 41  ARG   B CA   1 
ATOM   2004 C  C    . ARG   B 1 37  ? 8.429   -38.784 39.139  1.00 16.45 ? 41  ARG   B C    1 
ATOM   2005 O  O    . ARG   B 1 37  ? 9.139   -39.427 39.905  1.00 17.02 ? 41  ARG   B O    1 
ATOM   2006 C  CB   . ARG   B 1 37  ? 7.973   -36.475 40.094  1.00 17.36 ? 41  ARG   B CB   1 
ATOM   2007 C  CG   . ARG   B 1 37  ? 6.469   -36.630 40.174  1.00 17.86 ? 41  ARG   B CG   1 
ATOM   2008 C  CD   . ARG   B 1 37  ? 5.884   -35.917 41.389  1.00 18.00 ? 41  ARG   B CD   1 
ATOM   2009 N  NE   . ARG   B 1 37  ? 6.214   -36.495 42.700  1.00 19.17 ? 41  ARG   B NE   1 
ATOM   2010 C  CZ   . ARG   B 1 37  ? 7.034   -35.995 43.630  1.00 19.55 ? 41  ARG   B CZ   1 
ATOM   2011 N  NH1  . ARG   B 1 37  ? 7.767   -34.919 43.399  1.00 19.49 ? 41  ARG   B NH1  1 
ATOM   2012 N  NH2  . ARG   B 1 37  ? 7.125   -36.586 44.813  1.00 20.59 ? 41  ARG   B NH2  1 
ATOM   2013 N  N    . CYS   B 1 38  ? 7.488   -39.359 38.389  1.00 17.11 ? 42  CYS   B N    1 
ATOM   2014 C  CA   . CYS   B 1 38  ? 7.197   -40.778 38.539  1.00 19.25 ? 42  CYS   B CA   1 
ATOM   2015 C  C    . CYS   B 1 38  ? 8.404   -41.652 38.183  1.00 19.95 ? 42  CYS   B C    1 
ATOM   2016 O  O    . CYS   B 1 38  ? 8.527   -42.770 38.682  1.00 20.64 ? 42  CYS   B O    1 
ATOM   2017 C  CB   . CYS   B 1 38  ? 5.950   -41.183 37.761  1.00 21.66 ? 42  CYS   B CB   1 
ATOM   2018 S  SG   . CYS   B 1 38  ? 6.114   -41.080 35.962  1.00 23.65 ? 42  CYS   B SG   1 
ATOM   2019 N  N    . ALA   B 1 39  ? 9.310   -41.144 37.339  1.00 19.55 ? 43  ALA   B N    1 
ATOM   2020 C  CA   . ALA   B 1 39  ? 10.474  -41.922 36.941  1.00 20.60 ? 43  ALA   B CA   1 
ATOM   2021 C  C    . ALA   B 1 39  ? 11.397  -42.180 38.133  1.00 20.28 ? 43  ALA   B C    1 
ATOM   2022 O  O    . ALA   B 1 39  ? 12.136  -43.162 38.133  1.00 21.80 ? 43  ALA   B O    1 
ATOM   2023 C  CB   . ALA   B 1 39  ? 11.209  -41.236 35.818  1.00 21.71 ? 43  ALA   B CB   1 
ATOM   2024 N  N    . LEU   B 1 40  ? 11.379  -41.276 39.124  1.00 19.89 ? 44  LEU   B N    1 
ATOM   2025 C  CA   . LEU   B 1 40  ? 12.185  -41.399 40.331  1.00 20.73 ? 44  LEU   B CA   1 
ATOM   2026 C  C    . LEU   B 1 40  ? 11.358  -41.965 41.484  1.00 20.66 ? 44  LEU   B C    1 
ATOM   2027 O  O    . LEU   B 1 40  ? 11.886  -42.685 42.325  1.00 21.65 ? 44  LEU   B O    1 
ATOM   2028 C  CB   . LEU   B 1 40  ? 12.770  -40.039 40.713  1.00 22.15 ? 44  LEU   B CB   1 
ATOM   2029 C  CG   . LEU   B 1 40  ? 13.727  -39.398 39.705  1.00 25.50 ? 44  LEU   B CG   1 
ATOM   2030 C  CD1  . LEU   B 1 40  ? 14.243  -38.099 40.300  1.00 27.10 ? 44  LEU   B CD1  1 
ATOM   2031 C  CD2  . LEU   B 1 40  ? 14.888  -40.293 39.325  1.00 27.43 ? 44  LEU   B CD2  1 
ATOM   2032 N  N    . GLU   B 1 41  ? 10.071  -41.608 41.542  1.00 21.05 ? 45  GLU   B N    1 
ATOM   2033 C  CA   . GLU   B 1 41  ? 9.197   -42.035 42.624  1.00 22.85 ? 45  GLU   B CA   1 
ATOM   2034 C  C    . GLU   B 1 41  ? 8.915   -43.532 42.508  1.00 22.98 ? 45  GLU   B C    1 
ATOM   2035 O  O    . GLU   B 1 41  ? 8.860   -44.241 43.520  1.00 25.11 ? 45  GLU   B O    1 
ATOM   2036 C  CB   . GLU   B 1 41  ? 7.928   -41.194 42.493  1.00 25.71 ? 45  GLU   B CB   1 
ATOM   2037 C  CG   . GLU   B 1 41  ? 6.954   -41.290 43.655  1.00 28.75 ? 45  GLU   B CG   1 
ATOM   2038 C  CD   . GLU   B 1 41  ? 5.865   -40.247 43.465  1.00 31.76 ? 45  GLU   B CD   1 
ATOM   2039 O  OE1  . GLU   B 1 41  ? 5.707   -39.419 44.383  1.00 35.41 ? 45  GLU   B OE1  1 
ATOM   2040 O  OE2  . GLU   B 1 41  ? 5.212   -40.234 42.395  1.00 32.28 ? 45  GLU   B OE2  1 
ATOM   2041 N  N    . SER   B 1 42  ? 8.723   -43.987 41.261  1.00 24.14 ? 46  SER   B N    1 
ATOM   2042 C  CA   . SER   B 1 42  ? 8.279   -45.339 40.948  1.00 26.04 ? 46  SER   B CA   1 
ATOM   2043 C  C    . SER   B 1 42  ? 9.112   -45.910 39.801  1.00 27.82 ? 46  SER   B C    1 
ATOM   2044 O  O    . SER   B 1 42  ? 8.591   -46.131 38.710  1.00 28.28 ? 46  SER   B O    1 
ATOM   2045 C  CB   . SER   B 1 42  ? 6.814   -45.340 40.585  1.00 27.05 ? 46  SER   B CB   1 
ATOM   2046 O  OG   . SER   B 1 42  ? 6.020   -44.881 41.670  1.00 28.74 ? 46  SER   B OG   1 
ATOM   2047 N  N    . PRO   B 1 43  ? 10.429  -46.144 39.993  1.00 29.96 ? 47  PRO   B N    1 
ATOM   2048 C  CA   . PRO   B 1 43  ? 11.287  -46.620 38.904  1.00 32.13 ? 47  PRO   B CA   1 
ATOM   2049 C  C    . PRO   B 1 43  ? 10.920  -48.041 38.472  1.00 33.94 ? 47  PRO   B C    1 
ATOM   2050 O  O    . PRO   B 1 43  ? 10.443  -48.823 39.290  1.00 35.65 ? 47  PRO   B O    1 
ATOM   2051 C  CB   . PRO   B 1 43  ? 12.712  -46.512 39.486  1.00 32.82 ? 47  PRO   B CB   1 
ATOM   2052 C  CG   . PRO   B 1 43  ? 12.525  -46.538 40.988  1.00 33.18 ? 47  PRO   B CG   1 
ATOM   2053 C  CD   . PRO   B 1 43  ? 11.151  -45.950 41.259  1.00 31.02 ? 47  PRO   B CD   1 
ATOM   2054 N  N    . PRO   B 1 44  ? 11.090  -48.420 37.182  1.00 39.28 ? 48  PRO   B N    1 
ATOM   2055 C  CA   . PRO   B 1 44  ? 10.675  -49.745 36.712  1.00 42.09 ? 48  PRO   B CA   1 
ATOM   2056 C  C    . PRO   B 1 44  ? 11.470  -50.875 37.359  1.00 44.17 ? 48  PRO   B C    1 
ATOM   2057 O  O    . PRO   B 1 44  ? 12.641  -50.598 37.692  1.00 47.12 ? 48  PRO   B O    1 
ATOM   2058 C  CB   . PRO   B 1 44  ? 10.890  -49.693 35.186  1.00 42.84 ? 48  PRO   B CB   1 
ATOM   2059 C  CG   . PRO   B 1 44  ? 11.061  -48.226 34.870  1.00 42.41 ? 48  PRO   B CG   1 
ATOM   2060 C  CD   . PRO   B 1 44  ? 11.682  -47.605 36.110  1.00 41.13 ? 48  PRO   B CD   1 
ATOM   2061 N  N    . PRO   B 1 51  ? 21.632  -54.202 35.169  1.00 55.98 ? 55  PRO   B N    1 
ATOM   2062 C  CA   . PRO   B 1 51  ? 22.814  -53.492 34.698  1.00 53.80 ? 55  PRO   B CA   1 
ATOM   2063 C  C    . PRO   B 1 51  ? 23.505  -52.711 35.814  1.00 49.75 ? 55  PRO   B C    1 
ATOM   2064 O  O    . PRO   B 1 51  ? 22.890  -52.412 36.836  1.00 50.89 ? 55  PRO   B O    1 
ATOM   2065 C  CB   . PRO   B 1 51  ? 22.227  -52.575 33.616  1.00 55.19 ? 55  PRO   B CB   1 
ATOM   2066 C  CG   . PRO   B 1 51  ? 20.878  -52.182 34.177  1.00 55.67 ? 55  PRO   B CG   1 
ATOM   2067 C  CD   . PRO   B 1 51  ? 20.443  -53.367 35.031  1.00 55.90 ? 55  PRO   B CD   1 
ATOM   2068 N  N    . THR   B 1 52  ? 24.785  -52.382 35.606  1.00 44.58 ? 56  THR   B N    1 
ATOM   2069 C  CA   . THR   B 1 52  ? 25.550  -51.642 36.599  1.00 44.06 ? 56  THR   B CA   1 
ATOM   2070 C  C    . THR   B 1 52  ? 24.985  -50.224 36.708  1.00 39.51 ? 56  THR   B C    1 
ATOM   2071 O  O    . THR   B 1 52  ? 24.743  -49.739 37.810  1.00 42.09 ? 56  THR   B O    1 
ATOM   2072 C  CB   . THR   B 1 52  ? 27.053  -51.677 36.294  1.00 49.19 ? 56  THR   B CB   1 
ATOM   2073 O  OG1  . THR   B 1 52  ? 27.650  -50.752 37.199  1.00 51.19 ? 56  THR   B OG1  1 
ATOM   2074 C  CG2  . THR   B 1 52  ? 27.425  -51.279 34.876  1.00 51.31 ? 56  THR   B CG2  1 
ATOM   2075 N  N    . VAL   B 1 53  ? 24.725  -49.579 35.568  1.00 34.90 ? 57  VAL   B N    1 
ATOM   2076 C  CA   . VAL   B 1 53  ? 24.175  -48.233 35.576  1.00 32.33 ? 57  VAL   B CA   1 
ATOM   2077 C  C    . VAL   B 1 53  ? 22.692  -48.311 35.221  1.00 30.82 ? 57  VAL   B C    1 
ATOM   2078 O  O    . VAL   B 1 53  ? 22.330  -48.953 34.240  1.00 31.32 ? 57  VAL   B O    1 
ATOM   2079 C  CB   . VAL   B 1 53  ? 24.933  -47.306 34.608  1.00 33.36 ? 57  VAL   B CB   1 
ATOM   2080 C  CG1  . VAL   B 1 53  ? 24.412  -45.877 34.668  1.00 32.98 ? 57  VAL   B CG1  1 
ATOM   2081 C  CG2  . VAL   B 1 53  ? 26.436  -47.334 34.861  1.00 34.06 ? 57  VAL   B CG2  1 
ATOM   2082 N  N    . PRO   B 1 54  ? 21.791  -47.642 35.980  1.00 30.67 ? 58  PRO   B N    1 
ATOM   2083 C  CA   . PRO   B 1 54  ? 20.370  -47.619 35.640  1.00 31.22 ? 58  PRO   B CA   1 
ATOM   2084 C  C    . PRO   B 1 54  ? 20.179  -47.058 34.233  1.00 30.75 ? 58  PRO   B C    1 
ATOM   2085 O  O    . PRO   B 1 54  ? 20.848  -46.098 33.851  1.00 29.68 ? 58  PRO   B O    1 
ATOM   2086 C  CB   . PRO   B 1 54  ? 19.712  -46.709 36.694  1.00 32.33 ? 58  PRO   B CB   1 
ATOM   2087 C  CG   . PRO   B 1 54  ? 20.737  -46.555 37.794  1.00 32.75 ? 58  PRO   B CG   1 
ATOM   2088 C  CD   . PRO   B 1 54  ? 22.093  -46.858 37.186  1.00 31.87 ? 58  PRO   B CD   1 
ATOM   2089 N  N    . PRO   B 1 55  ? 19.250  -47.613 33.426  1.00 31.21 ? 59  PRO   B N    1 
ATOM   2090 C  CA   . PRO   B 1 55  ? 18.914  -47.003 32.141  1.00 30.54 ? 59  PRO   B CA   1 
ATOM   2091 C  C    . PRO   B 1 55  ? 18.158  -45.696 32.362  1.00 26.98 ? 59  PRO   B C    1 
ATOM   2092 O  O    . PRO   B 1 55  ? 17.462  -45.536 33.363  1.00 25.83 ? 59  PRO   B O    1 
ATOM   2093 C  CB   . PRO   B 1 55  ? 18.046  -48.076 31.469  1.00 32.29 ? 59  PRO   B CB   1 
ATOM   2094 C  CG   . PRO   B 1 55  ? 17.396  -48.791 32.634  1.00 33.41 ? 59  PRO   B CG   1 
ATOM   2095 C  CD   . PRO   B 1 55  ? 18.469  -48.829 33.706  1.00 32.68 ? 59  PRO   B CD   1 
ATOM   2096 N  N    . PRO   B 1 56  ? 18.259  -44.713 31.443  1.00 25.66 ? 60  PRO   B N    1 
ATOM   2097 C  CA   . PRO   B 1 56  ? 17.430  -43.519 31.545  1.00 23.36 ? 60  PRO   B CA   1 
ATOM   2098 C  C    . PRO   B 1 56  ? 15.960  -43.915 31.441  1.00 19.67 ? 60  PRO   B C    1 
ATOM   2099 O  O    . PRO   B 1 56  ? 15.614  -44.930 30.846  1.00 20.12 ? 60  PRO   B O    1 
ATOM   2100 C  CB   . PRO   B 1 56  ? 17.881  -42.618 30.382  1.00 25.25 ? 60  PRO   B CB   1 
ATOM   2101 C  CG   . PRO   B 1 56  ? 18.589  -43.558 29.431  1.00 27.87 ? 60  PRO   B CG   1 
ATOM   2102 C  CD   . PRO   B 1 56  ? 19.154  -44.685 30.277  1.00 27.61 ? 60  PRO   B CD   1 
ATOM   2103 N  N    . PRO   B 1 57  ? 15.040  -43.099 31.984  1.00 17.14 ? 61  PRO   B N    1 
ATOM   2104 C  CA   . PRO   B 1 57  ? 13.611  -43.338 31.783  1.00 16.63 ? 61  PRO   B CA   1 
ATOM   2105 C  C    . PRO   B 1 57  ? 13.269  -43.313 30.294  1.00 16.63 ? 61  PRO   B C    1 
ATOM   2106 O  O    . PRO   B 1 57  ? 13.875  -42.570 29.531  1.00 17.43 ? 61  PRO   B O    1 
ATOM   2107 C  CB   . PRO   B 1 57  ? 12.930  -42.190 32.536  1.00 17.29 ? 61  PRO   B CB   1 
ATOM   2108 C  CG   . PRO   B 1 57  ? 14.006  -41.618 33.433  1.00 17.79 ? 61  PRO   B CG   1 
ATOM   2109 C  CD   . PRO   B 1 57  ? 15.323  -41.876 32.748  1.00 17.22 ? 61  PRO   B CD   1 
ATOM   2110 N  N    . ARG   B 1 58  ? 12.259  -44.091 29.899  1.00 16.07 ? 62  ARG   B N    1 
ATOM   2111 C  CA   . ARG   B 1 58  ? 11.830  -44.127 28.511  1.00 15.97 ? 62  ARG   B CA   1 
ATOM   2112 C  C    . ARG   B 1 58  ? 11.207  -42.797 28.087  1.00 15.56 ? 62  ARG   B C    1 
ATOM   2113 O  O    . ARG   B 1 58  ? 11.466  -42.304 26.986  1.00 15.81 ? 62  ARG   B O    1 
ATOM   2114 C  CB   . ARG   B 1 58  ? 10.801  -45.240 28.281  1.00 16.29 ? 62  ARG   B CB   1 
ATOM   2115 C  CG   . ARG   B 1 58  ? 10.200  -45.204 26.881  1.00 16.23 ? 62  ARG   B CG   1 
ATOM   2116 C  CD   . ARG   B 1 58  ? 11.217  -45.495 25.809  1.00 16.29 ? 62  ARG   B CD   1 
ATOM   2117 N  NE   . ARG   B 1 58  ? 10.639  -45.383 24.463  1.00 16.23 ? 62  ARG   B NE   1 
ATOM   2118 C  CZ   . ARG   B 1 58  ? 10.586  -44.285 23.718  1.00 15.28 ? 62  ARG   B CZ   1 
ATOM   2119 N  NH1  . ARG   B 1 58  ? 10.893  -43.107 24.233  1.00 15.19 ? 62  ARG   B NH1  1 
ATOM   2120 N  NH2  . ARG   B 1 58  ? 10.259  -44.378 22.438  1.00 15.07 ? 62  ARG   B NH2  1 
ATOM   2121 N  N    . VAL   B 1 59  ? 10.335  -42.250 28.931  1.00 15.71 ? 63  VAL   B N    1 
ATOM   2122 C  CA   . VAL   B 1 59  ? 9.572   -41.071 28.559  1.00 15.70 ? 63  VAL   B CA   1 
ATOM   2123 C  C    . VAL   B 1 59  ? 10.304  -39.863 29.112  1.00 16.10 ? 63  VAL   B C    1 
ATOM   2124 O  O    . VAL   B 1 59  ? 10.194  -39.541 30.291  1.00 20.05 ? 63  VAL   B O    1 
ATOM   2125 C  CB   . VAL   B 1 59  ? 8.121   -41.125 29.058  1.00 16.66 ? 63  VAL   B CB   1 
ATOM   2126 C  CG1  . VAL   B 1 59  ? 7.323   -39.894 28.640  1.00 17.10 ? 63  VAL   B CG1  1 
ATOM   2127 C  CG2  . VAL   B 1 59  ? 7.447   -42.394 28.577  1.00 17.25 ? 63  VAL   B CG2  1 
ATOM   2128 N  N    . VAL   B 1 60  ? 11.072  -39.215 28.248  1.00 14.15 ? 64  VAL   B N    1 
ATOM   2129 C  CA   . VAL   B 1 60  ? 11.766  -37.996 28.609  1.00 14.92 ? 64  VAL   B CA   1 
ATOM   2130 C  C    . VAL   B 1 60  ? 11.705  -37.056 27.417  1.00 13.80 ? 64  VAL   B C    1 
ATOM   2131 O  O    . VAL   B 1 60  ? 11.500  -37.488 26.283  1.00 15.38 ? 64  VAL   B O    1 
ATOM   2132 C  CB   . VAL   B 1 60  ? 13.217  -38.252 29.039  1.00 17.56 ? 64  VAL   B CB   1 
ATOM   2133 C  CG1  . VAL   B 1 60  ? 13.289  -39.144 30.269  1.00 18.76 ? 64  VAL   B CG1  1 
ATOM   2134 C  CG2  . VAL   B 1 60  ? 14.041  -38.821 27.907  1.00 18.97 ? 64  VAL   B CG2  1 
ATOM   2135 N  N    . ASP   B 1 61  ? 11.863  -35.767 27.706  1.00 12.21 ? 65  ASP   B N    1 
ATOM   2136 C  CA   . ASP   B 1 61  ? 12.020  -34.743 26.693  1.00 11.85 ? 65  ASP   B CA   1 
ATOM   2137 C  C    . ASP   B 1 61  ? 13.438  -34.190 26.812  1.00 11.67 ? 65  ASP   B C    1 
ATOM   2138 O  O    . ASP   B 1 61  ? 13.940  -33.990 27.914  1.00 11.90 ? 65  ASP   B O    1 
ATOM   2139 C  CB   . ASP   B 1 61  ? 11.010  -33.621 26.869  1.00 12.60 ? 65  ASP   B CB   1 
ATOM   2140 C  CG   . ASP   B 1 61  ? 9.574   -33.901 26.456  1.00 13.50 ? 65  ASP   B CG   1 
ATOM   2141 O  OD1  . ASP   B 1 61  ? 9.292   -35.011 25.939  1.00 13.78 ? 65  ASP   B OD1  1 
ATOM   2142 O  OD2  . ASP   B 1 61  ? 8.747   -32.982 26.657  1.00 15.25 ? 65  ASP   B OD2  1 
ATOM   2143 N  N    . LYS   B 1 62  ? 14.087  -33.939 25.679  1.00 11.00 ? 66  LYS   B N    1 
ATOM   2144 C  CA   . LYS   B 1 62  ? 15.459  -33.469 25.692  1.00 11.69 ? 66  LYS   B CA   1 
ATOM   2145 C  C    . LYS   B 1 62  ? 15.615  -32.327 24.695  1.00 11.13 ? 66  LYS   B C    1 
ATOM   2146 O  O    . LYS   B 1 62  ? 15.077  -32.374 23.585  1.00 11.92 ? 66  LYS   B O    1 
ATOM   2147 C  CB   . LYS   B 1 62  ? 16.397  -34.633 25.348  1.00 13.98 ? 66  LYS   B CB   1 
ATOM   2148 C  CG   . LYS   B 1 62  ? 17.886  -34.342 25.429  1.00 16.92 ? 66  LYS   B CG   1 
ATOM   2149 C  CD   . LYS   B 1 62  ? 18.736  -35.469 24.849  1.00 20.19 ? 66  LYS   B CD   1 
ATOM   2150 C  CE   . LYS   B 1 62  ? 18.520  -36.791 25.480  1.00 21.77 ? 66  LYS   B CE   1 
ATOM   2151 N  NZ   . LYS   B 1 62  ? 19.448  -37.792 24.946  1.00 21.55 ? 66  LYS   B NZ   1 
ATOM   2152 N  N    . LEU   B 1 63  ? 16.368  -31.312 25.114  1.00 11.07 ? 67  LEU   B N    1 
ATOM   2153 C  CA   . LEU   B 1 63  ? 16.755  -30.210 24.252  1.00 11.51 ? 67  LEU   B CA   1 
ATOM   2154 C  C    . LEU   B 1 63  ? 18.241  -29.962 24.455  1.00 11.85 ? 67  LEU   B C    1 
ATOM   2155 O  O    . LEU   B 1 63  ? 18.651  -29.743 25.590  1.00 13.53 ? 67  LEU   B O    1 
ATOM   2156 C  CB   . LEU   B 1 63  ? 15.951  -28.968 24.621  1.00 12.79 ? 67  LEU   B CB   1 
ATOM   2157 C  CG   . LEU   B 1 63  ? 16.318  -27.685 23.868  1.00 14.05 ? 67  LEU   B CG   1 
ATOM   2158 C  CD1  . LEU   B 1 63  ? 16.009  -27.793 22.389  1.00 14.54 ? 67  LEU   B CD1  1 
ATOM   2159 C  CD2  . LEU   B 1 63  ? 15.578  -26.519 24.488  1.00 15.81 ? 67  LEU   B CD2  1 
ATOM   2160 N  N    . SER   B 1 64  ? 19.028  -30.020 23.382  1.00 11.65 ? 68  SER   B N    1 
ATOM   2161 C  CA   . SER   B 1 64  ? 20.447  -29.699 23.441  1.00 12.56 ? 68  SER   B CA   1 
ATOM   2162 C  C    . SER   B 1 64  ? 20.747  -28.715 22.326  1.00 12.13 ? 68  SER   B C    1 
ATOM   2163 O  O    . SER   B 1 64  ? 20.461  -29.019 21.169  1.00 13.50 ? 68  SER   B O    1 
ATOM   2164 C  CB   . SER   B 1 64  ? 21.307  -30.936 23.312  1.00 15.71 ? 68  SER   B CB   1 
ATOM   2165 O  OG   . SER   B 1 64  ? 22.678  -30.630 23.514  1.00 20.35 ? 68  SER   B OG   1 
ATOM   2166 N  N    . LEU   B 1 65  ? 21.286  -27.543 22.685  1.00 11.60 ? 69  LEU   B N    1 
ATOM   2167 C  CA   . LEU   B 1 65  ? 21.532  -26.470 21.733  1.00 12.42 ? 69  LEU   B CA   1 
ATOM   2168 C  C    . LEU   B 1 65  ? 22.934  -25.923 21.924  1.00 11.65 ? 69  LEU   B C    1 
ATOM   2169 O  O    . LEU   B 1 65  ? 23.327  -25.655 23.064  1.00 12.09 ? 69  LEU   B O    1 
ATOM   2170 C  CB   . LEU   B 1 65  ? 20.546  -25.320 21.926  1.00 13.73 ? 69  LEU   B CB   1 
ATOM   2171 C  CG   . LEU   B 1 65  ? 19.068  -25.632 21.737  1.00 15.35 ? 69  LEU   B CG   1 
ATOM   2172 C  CD1  . LEU   B 1 65  ? 18.224  -24.445 22.131  1.00 16.75 ? 69  LEU   B CD1  1 
ATOM   2173 C  CD2  . LEU   B 1 65  ? 18.782  -26.032 20.308  1.00 15.88 ? 69  LEU   B CD2  1 
ATOM   2174 N  N    . CYS   B 1 66  ? 23.627  -25.674 20.809  1.00 11.53 ? 70  CYS   B N    1 
ATOM   2175 C  CA   . CYS   B 1 66  ? 24.847  -24.879 20.841  1.00 11.60 ? 70  CYS   B CA   1 
ATOM   2176 C  C    . CYS   B 1 66  ? 24.503  -23.414 20.568  1.00 11.89 ? 70  CYS   B C    1 
ATOM   2177 O  O    . CYS   B 1 66  ? 23.564  -23.097 19.842  1.00 12.48 ? 70  CYS   B O    1 
ATOM   2178 C  CB   . CYS   B 1 66  ? 25.883  -25.415 19.862  1.00 12.85 ? 70  CYS   B CB   1 
ATOM   2179 S  SG   . CYS   B 1 66  ? 26.505  -27.056 20.306  1.00 15.04 ? 70  CYS   B SG   1 
ATOM   2180 N  N    . VAL   B 1 67  ? 25.287  -22.518 21.164  1.00 11.42 ? 71  VAL   B N    1 
ATOM   2181 C  CA   . VAL   B 1 67  ? 25.013  -21.090 21.178  1.00 11.96 ? 71  VAL   B CA   1 
ATOM   2182 C  C    . VAL   B 1 67  ? 26.302  -20.353 20.830  1.00 12.54 ? 71  VAL   B C    1 
ATOM   2183 O  O    . VAL   B 1 67  ? 27.363  -20.689 21.345  1.00 13.19 ? 71  VAL   B O    1 
ATOM   2184 C  CB   . VAL   B 1 67  ? 24.513  -20.662 22.573  1.00 12.59 ? 71  VAL   B CB   1 
ATOM   2185 C  CG1  . VAL   B 1 67  ? 24.186  -19.173 22.590  1.00 13.09 ? 71  VAL   B CG1  1 
ATOM   2186 C  CG2  . VAL   B 1 67  ? 23.314  -21.492 23.018  1.00 12.43 ? 71  VAL   B CG2  1 
ATOM   2187 N  N    . ALA   B 1 68  ? 26.203  -19.362 19.944  1.00 13.37 ? 72  ALA   B N    1 
ATOM   2188 C  CA   . ALA   B 1 68  ? 27.333  -18.510 19.621  1.00 13.68 ? 72  ALA   B CA   1 
ATOM   2189 C  C    . ALA   B 1 68  ? 27.490  -17.442 20.698  1.00 13.86 ? 72  ALA   B C    1 
ATOM   2190 O  O    . ALA   B 1 68  ? 26.638  -16.567 20.815  1.00 15.23 ? 72  ALA   B O    1 
ATOM   2191 C  CB   . ALA   B 1 68  ? 27.128  -17.865 18.270  1.00 14.96 ? 72  ALA   B CB   1 
ATOM   2192 N  N    . PRO   B 1 69  ? 28.563  -17.465 21.515  1.00 12.80 ? 73  PRO   B N    1 
ATOM   2193 C  CA   . PRO   B 1 69  ? 28.759  -16.432 22.526  1.00 12.90 ? 73  PRO   B CA   1 
ATOM   2194 C  C    . PRO   B 1 69  ? 29.289  -15.158 21.881  1.00 12.72 ? 73  PRO   B C    1 
ATOM   2195 O  O    . PRO   B 1 69  ? 29.788  -15.185 20.760  1.00 13.48 ? 73  PRO   B O    1 
ATOM   2196 C  CB   . PRO   B 1 69  ? 29.789  -17.072 23.452  1.00 13.11 ? 73  PRO   B CB   1 
ATOM   2197 C  CG   . PRO   B 1 69  ? 30.649  -17.867 22.509  1.00 13.17 ? 73  PRO   B CG   1 
ATOM   2198 C  CD   . PRO   B 1 69  ? 29.663  -18.439 21.505  1.00 12.89 ? 73  PRO   B CD   1 
ATOM   2199 N  N    . GLY   B 1 70  ? 29.214  -14.060 22.628  1.00 13.03 ? 74  GLY   B N    1 
ATOM   2200 C  CA   . GLY   B 1 70  ? 29.668  -12.763 22.163  1.00 12.88 ? 74  GLY   B CA   1 
ATOM   2201 C  C    . GLY   B 1 70  ? 31.159  -12.528 22.357  1.00 12.58 ? 74  GLY   B C    1 
ATOM   2202 O  O    . GLY   B 1 70  ? 31.625  -11.421 22.133  1.00 13.10 ? 74  GLY   B O    1 
ATOM   2203 N  N    . LYS   B 1 71  ? 31.897  -13.549 22.803  1.00 12.82 ? 75  LYS   B N    1 
ATOM   2204 C  CA   . LYS   B 1 71  ? 33.314  -13.418 23.088  1.00 13.06 ? 75  LYS   B CA   1 
ATOM   2205 C  C    . LYS   B 1 71  ? 33.977  -14.764 22.827  1.00 12.64 ? 75  LYS   B C    1 
ATOM   2206 O  O    . LYS   B 1 71  ? 33.304  -15.790 22.709  1.00 12.50 ? 75  LYS   B O    1 
ATOM   2207 C  CB   . LYS   B 1 71  ? 33.534  -12.988 24.547  1.00 14.41 ? 75  LYS   B CB   1 
ATOM   2208 C  CG   . LYS   B 1 71  ? 33.036  -14.003 25.575  1.00 15.96 ? 75  LYS   B CG   1 
ATOM   2209 C  CD   . LYS   B 1 71  ? 32.891  -13.555 27.028  1.00 18.78 ? 75  LYS   B CD   1 
ATOM   2210 C  CE   . LYS   B 1 71  ? 34.078  -12.865 27.552  1.00 22.19 ? 75  LYS   B CE   1 
ATOM   2211 N  NZ   . LYS   B 1 71  ? 33.821  -12.221 28.855  1.00 24.30 ? 75  LYS   B NZ   1 
ATOM   2212 N  N    . ALA   B 1 72  ? 35.306  -14.750 22.777  1.00 12.44 ? 76  ALA   B N    1 
ATOM   2213 C  CA   . ALA   B 1 72  ? 36.079  -15.968 22.626  1.00 12.66 ? 76  ALA   B CA   1 
ATOM   2214 C  C    . ALA   B 1 72  ? 35.949  -16.843 23.869  1.00 12.68 ? 76  ALA   B C    1 
ATOM   2215 O  O    . ALA   B 1 72  ? 35.841  -16.350 24.987  1.00 13.78 ? 76  ALA   B O    1 
ATOM   2216 C  CB   . ALA   B 1 72  ? 37.520  -15.635 22.377  1.00 13.78 ? 76  ALA   B CB   1 
ATOM   2217 N  N    . CYS   B 1 73  ? 35.998  -18.150 23.642  1.00 12.32 ? 77  CYS   B N    1 
ATOM   2218 C  CA   . CYS   B 1 73  ? 36.195  -19.103 24.715  1.00 12.82 ? 77  CYS   B CA   1 
ATOM   2219 C  C    . CYS   B 1 73  ? 37.637  -19.013 25.207  1.00 13.04 ? 77  CYS   B C    1 
ATOM   2220 O  O    . CYS   B 1 73  ? 38.572  -18.841 24.422  1.00 14.68 ? 77  CYS   B O    1 
ATOM   2221 C  CB   . CYS   B 1 73  ? 35.938  -20.526 24.241  1.00 13.65 ? 77  CYS   B CB   1 
ATOM   2222 S  SG   . CYS   B 1 73  ? 34.232  -20.819 23.712  1.00 14.71 ? 77  CYS   B SG   1 
ATOM   2223 N  N    . SER   B 1 74  ? 37.816  -19.140 26.519  1.00 13.00 ? 78  SER   B N    1 
ATOM   2224 C  CA   . SER   B 1 74  ? 39.162  -19.283 27.043  1.00 13.83 ? 78  SER   B CA   1 
ATOM   2225 C  C    . SER   B 1 74  ? 39.776  -20.567 26.499  1.00 14.09 ? 78  SER   B C    1 
ATOM   2226 O  O    . SER   B 1 74  ? 39.073  -21.535 26.192  1.00 13.86 ? 78  SER   B O    1 
ATOM   2227 C  CB   . SER   B 1 74  ? 39.205  -19.277 28.546  1.00 14.95 ? 78  SER   B CB   1 
ATOM   2228 O  OG   . SER   B 1 74  ? 38.627  -20.452 29.089  1.00 15.77 ? 78  SER   B OG   1 
ATOM   2229 N  N    . PRO   B 1 75  ? 41.115  -20.637 26.392  1.00 14.85 ? 79  PRO   B N    1 
ATOM   2230 C  CA   . PRO   B 1 75  ? 41.759  -21.890 26.011  1.00 15.22 ? 79  PRO   B CA   1 
ATOM   2231 C  C    . PRO   B 1 75  ? 41.338  -23.073 26.876  1.00 14.47 ? 79  PRO   B C    1 
ATOM   2232 O  O    . PRO   B 1 75  ? 41.092  -24.158 26.359  1.00 15.58 ? 79  PRO   B O    1 
ATOM   2233 C  CB   . PRO   B 1 75  ? 43.239  -21.527 26.149  1.00 15.75 ? 79  PRO   B CB   1 
ATOM   2234 C  CG   . PRO   B 1 75  ? 43.277  -20.066 25.811  1.00 16.29 ? 79  PRO   B CG   1 
ATOM   2235 C  CD   . PRO   B 1 75  ? 42.054  -19.509 26.491  1.00 15.89 ? 79  PRO   B CD   1 
ATOM   2236 N  N    . ALA   B 1 76  ? 41.227  -22.851 28.192  1.00 14.53 ? 80  ALA   B N    1 
ATOM   2237 C  CA   . ALA   B 1 76  ? 40.818  -23.907 29.102  1.00 14.65 ? 80  ALA   B CA   1 
ATOM   2238 C  C    . ALA   B 1 76  ? 39.400  -24.370 28.788  1.00 14.13 ? 80  ALA   B C    1 
ATOM   2239 O  O    . ALA   B 1 76  ? 39.145  -25.570 28.751  1.00 15.32 ? 80  ALA   B O    1 
ATOM   2240 C  CB   . ALA   B 1 76  ? 40.920  -23.448 30.539  1.00 15.23 ? 80  ALA   B CB   1 
ATOM   2241 N  N    . ALA   B 1 77  ? 38.488  -23.419 28.549  1.00 13.62 ? 81  ALA   B N    1 
ATOM   2242 C  CA   . ALA   B 1 77  ? 37.115  -23.780 28.232  1.00 13.84 ? 81  ALA   B CA   1 
ATOM   2243 C  C    . ALA   B 1 77  ? 37.080  -24.632 26.966  1.00 13.91 ? 81  ALA   B C    1 
ATOM   2244 O  O    . ALA   B 1 77  ? 36.352  -25.616 26.899  1.00 14.60 ? 81  ALA   B O    1 
ATOM   2245 C  CB   . ALA   B 1 77  ? 36.262  -22.544 28.069  1.00 14.07 ? 81  ALA   B CB   1 
ATOM   2246 N  N    . SER   B 1 78  ? 37.842  -24.246 25.944  1.00 14.26 ? 82  SER   B N    1 
ATOM   2247 C  CA   . SER   B 1 78  ? 37.835  -24.988 24.691  1.00 14.79 ? 82  SER   B CA   1 
ATOM   2248 C  C    . SER   B 1 78  ? 38.364  -26.410 24.882  1.00 15.33 ? 82  SER   B C    1 
ATOM   2249 O  O    . SER   B 1 78  ? 37.871  -27.357 24.270  1.00 16.10 ? 82  SER   B O    1 
ATOM   2250 C  CB   . SER   B 1 78  ? 38.614  -24.260 23.631  1.00 15.53 ? 82  SER   B CB   1 
ATOM   2251 O  OG   . SER   B 1 78  ? 37.899  -23.116 23.197  1.00 16.71 ? 82  SER   B OG   1 
ATOM   2252 N  N    . GLU   B 1 79  ? 39.391  -26.568 25.717  1.00 16.00 ? 83  GLU   B N    1 
ATOM   2253 C  CA   . GLU   B 1 79  ? 39.964  -27.887 25.929  1.00 18.59 ? 83  GLU   B CA   1 
ATOM   2254 C  C    . GLU   B 1 79  ? 38.980  -28.811 26.632  1.00 19.30 ? 83  GLU   B C    1 
ATOM   2255 O  O    . GLU   B 1 79  ? 38.908  -29.992 26.305  1.00 21.84 ? 83  GLU   B O    1 
ATOM   2256 C  CB   . GLU   B 1 79  ? 41.284  -27.773 26.679  1.00 21.82 ? 83  GLU   B CB   1 
ATOM   2257 C  CG   . GLU   B 1 79  ? 42.392  -27.317 25.744  1.00 27.11 ? 83  GLU   B CG   1 
ATOM   2258 C  CD   . GLU   B 1 79  ? 43.740  -27.262 26.429  1.00 32.24 ? 83  GLU   B CD   1 
ATOM   2259 O  OE1  . GLU   B 1 79  ? 43.784  -27.464 27.658  1.00 40.00 ? 83  GLU   B OE1  1 
ATOM   2260 O  OE2  . GLU   B 1 79  ? 44.728  -26.987 25.737  1.00 39.10 ? 83  GLU   B OE2  1 
ATOM   2261 N  N    . ILE   B 1 80  ? 38.231  -28.278 27.598  1.00 18.05 ? 84  ILE   B N    1 
ATOM   2262 C  CA   . ILE   B 1 80  ? 37.362  -29.120 28.400  1.00 20.78 ? 84  ILE   B CA   1 
ATOM   2263 C  C    . ILE   B 1 80  ? 36.056  -29.376 27.646  1.00 20.87 ? 84  ILE   B C    1 
ATOM   2264 O  O    . ILE   B 1 80  ? 35.515  -30.477 27.747  1.00 23.68 ? 84  ILE   B O    1 
ATOM   2265 C  CB   . ILE   B 1 80  ? 37.180  -28.541 29.818  1.00 23.90 ? 84  ILE   B CB   1 
ATOM   2266 C  CG1  . ILE   B 1 80  ? 36.468  -29.530 30.731  1.00 28.02 ? 84  ILE   B CG1  1 
ATOM   2267 C  CG2  . ILE   B 1 80  ? 36.489  -27.184 29.806  1.00 25.38 ? 84  ILE   B CG2  1 
ATOM   2268 N  N    . THR   B 1 81  ? 35.562  -28.387 26.873  1.00 19.11 ? 85  THR   B N    1 
ATOM   2269 C  CA   . THR   B 1 81  ? 34.220  -28.476 26.300  1.00 19.21 ? 85  THR   B CA   1 
ATOM   2270 C  C    . THR   B 1 81  ? 34.259  -28.951 24.847  1.00 18.69 ? 85  THR   B C    1 
ATOM   2271 O  O    . THR   B 1 81  ? 33.228  -29.368 24.320  1.00 21.19 ? 85  THR   B O    1 
ATOM   2272 C  CB   . THR   B 1 81  ? 33.467  -27.145 26.386  1.00 18.87 ? 85  THR   B CB   1 
ATOM   2273 O  OG1  . THR   B 1 81  ? 34.070  -26.195 25.502  1.00 18.12 ? 85  THR   B OG1  1 
ATOM   2274 C  CG2  . THR   B 1 81  ? 33.402  -26.583 27.794  1.00 20.00 ? 85  THR   B CG2  1 
ATOM   2275 N  N    . GLY   B 1 82  ? 35.418  -28.823 24.185  1.00 18.27 ? 86  GLY   B N    1 
ATOM   2276 C  CA   . GLY   B 1 82  ? 35.572  -29.135 22.776  1.00 18.47 ? 86  GLY   B CA   1 
ATOM   2277 C  C    . GLY   B 1 82  ? 34.921  -28.106 21.844  1.00 17.48 ? 86  GLY   B C    1 
ATOM   2278 O  O    . GLY   B 1 82  ? 34.723  -28.382 20.662  1.00 19.24 ? 86  GLY   B O    1 
ATOM   2279 N  N    . LEU   B 1 83  ? 34.576  -26.928 22.375  1.00 15.87 ? 87  LEU   B N    1 
ATOM   2280 C  CA   . LEU   B 1 83  ? 33.947  -25.870 21.604  1.00 14.79 ? 87  LEU   B CA   1 
ATOM   2281 C  C    . LEU   B 1 83  ? 34.891  -24.670 21.537  1.00 14.39 ? 87  LEU   B C    1 
ATOM   2282 O  O    . LEU   B 1 83  ? 35.686  -24.444 22.435  1.00 15.75 ? 87  LEU   B O    1 
ATOM   2283 C  CB   . LEU   B 1 83  ? 32.622  -25.457 22.242  1.00 14.75 ? 87  LEU   B CB   1 
ATOM   2284 C  CG   . LEU   B 1 83  ? 31.551  -26.544 22.360  1.00 15.41 ? 87  LEU   B CG   1 
ATOM   2285 C  CD1  . LEU   B 1 83  ? 30.367  -26.034 23.165  1.00 15.54 ? 87  LEU   B CD1  1 
ATOM   2286 C  CD2  . LEU   B 1 83  ? 31.090  -27.034 21.004  1.00 15.96 ? 87  LEU   B CD2  1 
ATOM   2287 N  N    . SER   B 1 84  ? 34.756  -23.885 20.470  1.00 13.64 ? 88  SER   B N    1 
ATOM   2288 C  CA   . SER   B 1 84  ? 35.330  -22.553 20.390  1.00 13.13 ? 88  SER   B CA   1 
ATOM   2289 C  C    . SER   B 1 84  ? 34.328  -21.653 19.683  1.00 12.26 ? 88  SER   B C    1 
ATOM   2290 O  O    . SER   B 1 84  ? 33.483  -22.129 18.933  1.00 11.77 ? 88  SER   B O    1 
ATOM   2291 C  CB   . SER   B 1 84  ? 36.658  -22.552 19.676  1.00 14.40 ? 88  SER   B CB   1 
ATOM   2292 O  OG   . SER   B 1 84  ? 36.476  -22.798 18.289  1.00 15.95 ? 88  SER   B OG   1 
ATOM   2293 N  N    . THR   B 1 85  ? 34.459  -20.346 19.890  1.00 12.52 ? 89  THR   B N    1 
ATOM   2294 C  CA   . THR   B 1 85  ? 33.533  -19.403 19.296  1.00 12.82 ? 89  THR   B CA   1 
ATOM   2295 C  C    . THR   B 1 85  ? 33.629  -19.478 17.771  1.00 12.80 ? 89  THR   B C    1 
ATOM   2296 O  O    . THR   B 1 85  ? 32.613  -19.465 17.073  1.00 13.03 ? 89  THR   B O    1 
ATOM   2297 C  CB   . THR   B 1 85  ? 33.821  -18.019 19.867  1.00 13.25 ? 89  THR   B CB   1 
ATOM   2298 O  OG1  . THR   B 1 85  ? 33.706  -18.168 21.287  1.00 14.13 ? 89  THR   B OG1  1 
ATOM   2299 C  CG2  . THR   B 1 85  ? 32.845  -16.982 19.351  1.00 13.49 ? 89  THR   B CG2  1 
ATOM   2300 N  N    . ALA   B 1 86  ? 34.849  -19.600 17.247  1.00 12.80 ? 90  ALA   B N    1 
ATOM   2301 C  CA   . ALA   B 1 86  ? 35.021  -19.671 15.804  1.00 13.76 ? 90  ALA   B CA   1 
ATOM   2302 C  C    . ALA   B 1 86  ? 34.336  -20.911 15.235  1.00 13.99 ? 90  ALA   B C    1 
ATOM   2303 O  O    . ALA   B 1 86  ? 33.728  -20.844 14.170  1.00 14.88 ? 90  ALA   B O    1 
ATOM   2304 C  CB   . ALA   B 1 86  ? 36.490  -19.654 15.454  1.00 14.57 ? 90  ALA   B CB   1 
ATOM   2305 N  N    . VAL   B 1 87  ? 34.491  -22.061 15.901  1.00 13.60 ? 91  VAL   B N    1 
ATOM   2306 C  CA   . VAL   B 1 87  ? 33.875  -23.289 15.410  1.00 14.47 ? 91  VAL   B CA   1 
ATOM   2307 C  C    . VAL   B 1 87  ? 32.350  -23.222 15.509  1.00 13.48 ? 91  VAL   B C    1 
ATOM   2308 O  O    . VAL   B 1 87  ? 31.654  -23.655 14.597  1.00 13.64 ? 91  VAL   B O    1 
ATOM   2309 C  CB   . VAL   B 1 87  ? 34.464  -24.518 16.118  1.00 16.84 ? 91  VAL   B CB   1 
ATOM   2310 C  CG1  . VAL   B 1 87  ? 33.684  -25.785 15.793  1.00 18.63 ? 91  VAL   B CG1  1 
ATOM   2311 C  CG2  . VAL   B 1 87  ? 35.928  -24.693 15.745  1.00 18.34 ? 91  VAL   B CG2  1 
ATOM   2312 N  N    . LEU   B 1 88  ? 31.815  -22.666 16.599  1.00 12.15 ? 92  LEU   B N    1 
ATOM   2313 C  CA   . LEU   B 1 88  ? 30.378  -22.465 16.710  1.00 12.37 ? 92  LEU   B CA   1 
ATOM   2314 C  C    . LEU   B 1 88  ? 29.872  -21.605 15.545  1.00 12.91 ? 92  LEU   B C    1 
ATOM   2315 O  O    . LEU   B 1 88  ? 28.828  -21.886 14.951  1.00 13.11 ? 92  LEU   B O    1 
ATOM   2316 C  CB   . LEU   B 1 88  ? 30.082  -21.844 18.072  1.00 12.44 ? 92  LEU   B CB   1 
ATOM   2317 C  CG   . LEU   B 1 88  ? 30.279  -22.765 19.275  1.00 12.72 ? 92  LEU   B CG   1 
ATOM   2318 C  CD1  . LEU   B 1 88  ? 30.402  -21.970 20.567  1.00 13.07 ? 92  LEU   B CD1  1 
ATOM   2319 C  CD2  . LEU   B 1 88  ? 29.118  -23.732 19.347  1.00 12.96 ? 92  LEU   B CD2  1 
ATOM   2320 N  N    . ALA   B 1 89  ? 30.623  -20.554 15.202  1.00 13.51 ? 93  ALA   B N    1 
ATOM   2321 C  CA   . ALA   B 1 89  ? 30.236  -19.695 14.092  1.00 13.99 ? 93  ALA   B CA   1 
ATOM   2322 C  C    . ALA   B 1 89  ? 30.282  -20.447 12.758  1.00 14.61 ? 93  ALA   B C    1 
ATOM   2323 O  O    . ALA   B 1 89  ? 29.425  -20.234 11.901  1.00 14.86 ? 93  ALA   B O    1 
ATOM   2324 C  CB   . ALA   B 1 89  ? 31.122  -18.477 14.061  1.00 14.96 ? 93  ALA   B CB   1 
ATOM   2325 N  N    . ALA   B 1 90  ? 31.300  -21.296 12.562  1.00 14.07 ? 94  ALA   B N    1 
ATOM   2326 C  CA   . ALA   B 1 90  ? 31.407  -22.087 11.343  1.00 15.11 ? 94  ALA   B CA   1 
ATOM   2327 C  C    . ALA   B 1 90  ? 30.221  -23.031 11.168  1.00 14.78 ? 94  ALA   B C    1 
ATOM   2328 O  O    . ALA   B 1 90  ? 29.895  -23.425 10.044  1.00 16.31 ? 94  ALA   B O    1 
ATOM   2329 C  CB   . ALA   B 1 90  ? 32.701  -22.869 11.342  1.00 15.79 ? 94  ALA   B CB   1 
ATOM   2330 N  N    . HIS   B 1 91  ? 29.569  -23.389 12.277  1.00 13.99 ? 95  HIS   B N    1 
ATOM   2331 C  CA   . HIS   B 1 91  ? 28.386  -24.229 12.227  1.00 14.21 ? 95  HIS   B CA   1 
ATOM   2332 C  C    . HIS   B 1 91  ? 27.107  -23.395 12.219  1.00 14.13 ? 95  HIS   B C    1 
ATOM   2333 O  O    . HIS   B 1 91  ? 26.023  -23.935 12.437  1.00 15.14 ? 95  HIS   B O    1 
ATOM   2334 C  CB   . HIS   B 1 91  ? 28.396  -25.222 13.389  1.00 14.85 ? 95  HIS   B CB   1 
ATOM   2335 C  CG   . HIS   B 1 91  ? 29.389  -26.308 13.248  1.00 15.73 ? 95  HIS   B CG   1 
ATOM   2336 N  ND1  . HIS   B 1 91  ? 30.731  -26.106 13.463  1.00 17.21 ? 95  HIS   B ND1  1 
ATOM   2337 C  CD2  . HIS   B 1 91  ? 29.251  -27.596 12.912  1.00 16.32 ? 95  HIS   B CD2  1 
ATOM   2338 C  CE1  . HIS   B 1 91  ? 31.374  -27.248 13.265  1.00 18.55 ? 95  HIS   B CE1  1 
ATOM   2339 N  NE2  . HIS   B 1 91  ? 30.496  -28.161 12.937  1.00 17.92 ? 95  HIS   B NE2  1 
ATOM   2340 N  N    . GLY   B 1 92  ? 27.228  -22.083 11.988  1.00 14.10 ? 96  GLY   B N    1 
ATOM   2341 C  CA   . GLY   B 1 92  ? 26.080  -21.205 11.852  1.00 14.20 ? 96  GLY   B CA   1 
ATOM   2342 C  C    . GLY   B 1 92  ? 25.275  -21.011 13.130  1.00 13.94 ? 96  GLY   B C    1 
ATOM   2343 O  O    . GLY   B 1 92  ? 24.089  -20.680 13.052  1.00 15.13 ? 96  GLY   B O    1 
ATOM   2344 N  N    . ARG   B 1 93  ? 25.910  -21.163 14.301  1.00 13.82 ? 97  ARG   B N    1 
ATOM   2345 C  CA   . ARG   B 1 93  ? 25.185  -21.014 15.552  1.00 13.75 ? 97  ARG   B CA   1 
ATOM   2346 C  C    . ARG   B 1 93  ? 24.816  -19.552 15.790  1.00 14.23 ? 97  ARG   B C    1 
ATOM   2347 O  O    . ARG   B 1 93  ? 25.566  -18.636 15.453  1.00 15.97 ? 97  ARG   B O    1 
ATOM   2348 C  CB   . ARG   B 1 93  ? 25.967  -21.571 16.739  1.00 14.07 ? 97  ARG   B CB   1 
ATOM   2349 C  CG   . ARG   B 1 93  ? 26.254  -23.060 16.641  1.00 14.42 ? 97  ARG   B CG   1 
ATOM   2350 C  CD   . ARG   B 1 93  ? 25.021  -23.904 16.451  1.00 14.81 ? 97  ARG   B CD   1 
ATOM   2351 N  NE   . ARG   B 1 93  ? 24.652  -24.044 15.039  1.00 14.80 ? 97  ARG   B NE   1 
ATOM   2352 C  CZ   . ARG   B 1 93  ? 23.518  -24.553 14.577  1.00 15.92 ? 97  ARG   B CZ   1 
ATOM   2353 N  NH1  . ARG   B 1 93  ? 22.556  -24.897 15.409  1.00 16.74 ? 97  ARG   B NH1  1 
ATOM   2354 N  NH2  . ARG   B 1 93  ? 23.336  -24.680 13.269  1.00 16.73 ? 97  ARG   B NH2  1 
ATOM   2355 N  N    . GLN   B 1 94  ? 23.619  -19.370 16.351  1.00 14.54 ? 98  GLN   B N    1 
ATOM   2356 C  CA   . GLN   B 1 94  ? 23.085  -18.062 16.683  1.00 15.88 ? 98  GLN   B CA   1 
ATOM   2357 C  C    . GLN   B 1 94  ? 23.319  -17.739 18.157  1.00 15.15 ? 98  GLN   B C    1 
ATOM   2358 O  O    . GLN   B 1 94  ? 23.534  -18.621 18.988  1.00 14.05 ? 98  GLN   B O    1 
ATOM   2359 C  CB   . GLN   B 1 94  ? 21.590  -18.034 16.380  1.00 17.57 ? 98  GLN   B CB   1 
ATOM   2360 C  CG   . GLN   B 1 94  ? 21.285  -18.142 14.894  1.00 19.87 ? 98  GLN   B CG   1 
ATOM   2361 C  CD   . GLN   B 1 94  ? 19.807  -18.249 14.604  1.00 22.54 ? 98  GLN   B CD   1 
ATOM   2362 O  OE1  . GLN   B 1 94  ? 18.945  -17.964 15.453  1.00 25.44 ? 98  GLN   B OE1  1 
ATOM   2363 N  NE2  . GLN   B 1 94  ? 19.512  -18.705 13.397  1.00 24.91 ? 98  GLN   B NE2  1 
ATOM   2364 N  N    A CYS   B 1 95  ? 23.269  -16.444 18.471  0.80 15.77 ? 99  CYS   B N    1 
ATOM   2365 N  N    B CYS   B 1 95  ? 23.215  -16.447 18.476  0.20 15.95 ? 99  CYS   B N    1 
ATOM   2366 C  CA   A CYS   B 1 95  ? 23.483  -15.972 19.828  0.80 16.25 ? 99  CYS   B CA   1 
ATOM   2367 C  CA   B CYS   B 1 95  ? 23.436  -15.965 19.828  0.20 16.58 ? 99  CYS   B CA   1 
ATOM   2368 C  C    A CYS   B 1 95  ? 22.288  -16.312 20.721  0.80 15.65 ? 99  CYS   B C    1 
ATOM   2369 C  C    B CYS   B 1 95  ? 22.272  -16.338 20.735  0.20 16.05 ? 99  CYS   B C    1 
ATOM   2370 O  O    A CYS   B 1 95  ? 21.265  -16.823 20.263  0.80 16.18 ? 99  CYS   B O    1 
ATOM   2371 O  O    B CYS   B 1 95  ? 21.255  -16.864 20.286  0.20 16.17 ? 99  CYS   B O    1 
ATOM   2372 C  CB   A CYS   B 1 95  ? 23.783  -14.478 19.828  0.80 18.01 ? 99  CYS   B CB   1 
ATOM   2373 C  CB   B CYS   B 1 95  ? 23.571  -14.451 19.854  0.20 17.80 ? 99  CYS   B CB   1 
ATOM   2374 S  SG   A CYS   B 1 95  ? 22.360  -13.468 19.351  0.80 20.85 ? 99  CYS   B SG   1 
ATOM   2375 S  SG   B CYS   B 1 95  ? 24.651  -13.832 18.545  0.20 20.63 ? 99  CYS   B SG   1 
ATOM   2376 N  N    . PHE   B 1 96  ? 22.452  -16.042 22.025  1.00 15.57 ? 100 PHE   B N    1 
ATOM   2377 C  CA   . PHE   B 1 96  ? 21.397  -16.176 23.010  1.00 16.34 ? 100 PHE   B CA   1 
ATOM   2378 C  C    . PHE   B 1 96  ? 20.456  -14.986 22.839  1.00 17.31 ? 100 PHE   B C    1 
ATOM   2379 O  O    . PHE   B 1 96  ? 20.786  -13.875 23.235  1.00 20.61 ? 100 PHE   B O    1 
ATOM   2380 C  CB   . PHE   B 1 96  ? 22.054  -16.268 24.391  1.00 15.84 ? 100 PHE   B CB   1 
ATOM   2381 C  CG   . PHE   B 1 96  ? 21.181  -16.907 25.461  1.00 16.37 ? 100 PHE   B CG   1 
ATOM   2382 C  CD1  . PHE   B 1 96  ? 19.915  -16.414 25.736  1.00 17.51 ? 100 PHE   B CD1  1 
ATOM   2383 C  CD2  . PHE   B 1 96  ? 21.601  -18.041 26.141  1.00 16.71 ? 100 PHE   B CD2  1 
ATOM   2384 C  CE1  . PHE   B 1 96  ? 19.112  -17.014 26.695  1.00 18.41 ? 100 PHE   B CE1  1 
ATOM   2385 C  CE2  . PHE   B 1 96  ? 20.796  -18.636 27.097  1.00 17.24 ? 100 PHE   B CE2  1 
ATOM   2386 C  CZ   . PHE   B 1 96  ? 19.549  -18.127 27.364  1.00 17.96 ? 100 PHE   B CZ   1 
ATOM   2387 N  N    . ASP   B 1 97  ? 19.306  -15.222 22.210  1.00 16.75 ? 101 ASP   B N    1 
ATOM   2388 C  CA   . ASP   B 1 97  ? 18.415  -14.145 21.813  1.00 17.46 ? 101 ASP   B CA   1 
ATOM   2389 C  C    . ASP   B 1 97  ? 16.984  -14.459 22.238  1.00 17.43 ? 101 ASP   B C    1 
ATOM   2390 O  O    . ASP   B 1 97  ? 16.718  -15.459 22.900  1.00 16.85 ? 101 ASP   B O    1 
ATOM   2391 C  CB   . ASP   B 1 97  ? 18.549  -13.883 20.323  1.00 18.93 ? 101 ASP   B CB   1 
ATOM   2392 C  CG   . ASP   B 1 97  ? 18.179  -15.049 19.416  1.00 20.51 ? 101 ASP   B CG   1 
ATOM   2393 O  OD1  . ASP   B 1 97  ? 17.684  -16.081 19.937  1.00 20.03 ? 101 ASP   B OD1  1 
ATOM   2394 O  OD2  . ASP   B 1 97  ? 18.396  -14.911 18.187  1.00 24.80 ? 101 ASP   B OD2  1 
ATOM   2395 N  N    . ASP   B 1 98  ? 16.056  -13.577 21.856  1.00 18.21 ? 102 ASP   B N    1 
ATOM   2396 C  CA   . ASP   B 1 98  ? 14.664  -13.716 22.245  1.00 19.99 ? 102 ASP   B CA   1 
ATOM   2397 C  C    . ASP   B 1 98  ? 14.105  -15.052 21.775  1.00 18.58 ? 102 ASP   B C    1 
ATOM   2398 O  O    . ASP   B 1 98  ? 13.367  -15.702 22.511  1.00 19.35 ? 102 ASP   B O    1 
ATOM   2399 C  CB   . ASP   B 1 98  ? 13.811  -12.582 21.699  1.00 22.96 ? 102 ASP   B CB   1 
ATOM   2400 C  CG   . ASP   B 1 98  ? 13.902  -11.255 22.434  1.00 27.82 ? 102 ASP   B CG   1 
ATOM   2401 O  OD1  . ASP   B 1 98  ? 14.557  -11.212 23.491  1.00 31.74 ? 102 ASP   B OD1  1 
ATOM   2402 O  OD2  . ASP   B 1 98  ? 13.290  -10.277 21.946  1.00 33.82 ? 102 ASP   B OD2  1 
ATOM   2403 N  N    . ASN   B 1 99  ? 14.420  -15.439 20.534  1.00 17.85 ? 103 ASN   B N    1 
ATOM   2404 C  CA   . ASN   B 1 99  ? 13.901  -16.683 19.989  1.00 17.36 ? 103 ASN   B CA   1 
ATOM   2405 C  C    . ASN   B 1 99  ? 14.362  -17.851 20.859  1.00 16.34 ? 103 ASN   B C    1 
ATOM   2406 O  O    . ASN   B 1 99  ? 13.591  -18.764 21.114  1.00 15.41 ? 103 ASN   B O    1 
ATOM   2407 C  CB   . ASN   B 1 99  ? 14.301  -16.885 18.531  1.00 17.54 ? 103 ASN   B CB   1 
ATOM   2408 C  CG   . ASN   B 1 99  ? 13.807  -18.197 17.955  1.00 18.13 ? 103 ASN   B CG   1 
ATOM   2409 O  OD1  . ASN   B 1 99  ? 12.599  -18.383 17.763  1.00 20.22 ? 103 ASN   B OD1  1 
ATOM   2410 N  ND2  . ASN   B 1 99  ? 14.712  -19.119 17.661  1.00 17.60 ? 103 ASN   B ND2  1 
ATOM   2411 N  N    . LEU   B 1 100 ? 15.624  -17.841 21.309  1.00 15.63 ? 104 LEU   B N    1 
ATOM   2412 C  CA   . LEU   B 1 100 ? 16.098  -18.918 22.166  1.00 14.67 ? 104 LEU   B CA   1 
ATOM   2413 C  C    . LEU   B 1 100 ? 15.329  -18.931 23.486  1.00 14.86 ? 104 LEU   B C    1 
ATOM   2414 O  O    . LEU   B 1 100 ? 14.931  -19.990 23.947  1.00 14.11 ? 104 LEU   B O    1 
ATOM   2415 C  CB   . LEU   B 1 100 ? 17.602  -18.818 22.409  1.00 14.30 ? 104 LEU   B CB   1 
ATOM   2416 C  CG   . LEU   B 1 100 ? 18.203  -19.909 23.306  1.00 14.76 ? 104 LEU   B CG   1 
ATOM   2417 C  CD1  . LEU   B 1 100 ? 17.877  -21.300 22.836  1.00 15.81 ? 104 LEU   B CD1  1 
ATOM   2418 C  CD2  . LEU   B 1 100 ? 19.697  -19.761 23.399  1.00 15.83 ? 104 LEU   B CD2  1 
ATOM   2419 N  N    . ALA   B 1 101 ? 15.099  -17.768 24.101  1.00 15.65 ? 105 ALA   B N    1 
ATOM   2420 C  CA   . ALA   B 1 101 ? 14.344  -17.735 25.344  1.00 16.32 ? 105 ALA   B CA   1 
ATOM   2421 C  C    . ALA   B 1 101 ? 12.934  -18.294 25.124  1.00 16.74 ? 105 ALA   B C    1 
ATOM   2422 O  O    . ALA   B 1 101 ? 12.404  -19.024 25.968  1.00 16.84 ? 105 ALA   B O    1 
ATOM   2423 C  CB   . ALA   B 1 101 ? 14.294  -16.328 25.881  1.00 17.04 ? 105 ALA   B CB   1 
ATOM   2424 N  N    . ASN   B 1 102 ? 12.319  -17.938 23.990  1.00 16.88 ? 106 ASN   B N    1 
ATOM   2425 C  CA   . ASN   B 1 102 ? 10.984  -18.422 23.662  1.00 18.18 ? 106 ASN   B CA   1 
ATOM   2426 C  C    . ASN   B 1 102 ? 10.980  -19.936 23.474  1.00 16.15 ? 106 ASN   B C    1 
ATOM   2427 O  O    . ASN   B 1 102 ? 10.042  -20.608 23.888  1.00 17.25 ? 106 ASN   B O    1 
ATOM   2428 C  CB   . ASN   B 1 102 ? 10.418  -17.748 22.419  1.00 19.68 ? 106 ASN   B CB   1 
ATOM   2429 C  CG   . ASN   B 1 102 ? 10.145  -16.276 22.604  1.00 23.38 ? 106 ASN   B CG   1 
ATOM   2430 O  OD1  . ASN   B 1 102 ? 9.945   -15.800 23.728  1.00 27.26 ? 106 ASN   B OD1  1 
ATOM   2431 N  ND2  . ASN   B 1 102 ? 10.103  -15.548 21.498  1.00 25.38 ? 106 ASN   B ND2  1 
ATOM   2432 N  N    A LEU   B 1 103 ? 12.023  -20.474 22.827  0.50 15.40 ? 107 LEU   B N    1 
ATOM   2433 N  N    B LEU   B 1 103 ? 12.029  -20.451 22.829  0.50 15.29 ? 107 LEU   B N    1 
ATOM   2434 C  CA   A LEU   B 1 103 ? 12.150  -21.914 22.634  0.50 14.56 ? 107 LEU   B CA   1 
ATOM   2435 C  CA   B LEU   B 1 103 ? 12.192  -21.880 22.625  0.50 14.29 ? 107 LEU   B CA   1 
ATOM   2436 C  C    A LEU   B 1 103 ? 12.259  -22.616 23.991  0.50 14.09 ? 107 LEU   B C    1 
ATOM   2437 C  C    B LEU   B 1 103 ? 12.273  -22.605 23.972  0.50 14.02 ? 107 LEU   B C    1 
ATOM   2438 O  O    A LEU   B 1 103 ? 11.581  -23.616 24.233  0.50 13.66 ? 107 LEU   B O    1 
ATOM   2439 O  O    B LEU   B 1 103 ? 11.587  -23.605 24.191  0.50 13.73 ? 107 LEU   B O    1 
ATOM   2440 C  CB   A LEU   B 1 103 ? 13.350  -22.204 21.729  0.50 14.60 ? 107 LEU   B CB   1 
ATOM   2441 C  CB   B LEU   B 1 103 ? 13.458  -22.030 21.782  0.50 14.11 ? 107 LEU   B CB   1 
ATOM   2442 C  CG   A LEU   B 1 103 ? 13.782  -23.671 21.588  0.50 14.61 ? 107 LEU   B CG   1 
ATOM   2443 C  CG   B LEU   B 1 103 ? 13.751  -23.427 21.229  0.50 13.84 ? 107 LEU   B CG   1 
ATOM   2444 C  CD1  A LEU   B 1 103 ? 12.693  -24.575 21.035  0.50 14.82 ? 107 LEU   B CD1  1 
ATOM   2445 C  CD1  B LEU   B 1 103 ? 14.896  -23.375 20.240  0.50 13.91 ? 107 LEU   B CD1  1 
ATOM   2446 C  CD2  A LEU   B 1 103 ? 15.011  -23.764 20.700  0.50 14.77 ? 107 LEU   B CD2  1 
ATOM   2447 C  CD2  B LEU   B 1 103 ? 14.063  -24.386 22.351  0.50 13.76 ? 107 LEU   B CD2  1 
ATOM   2448 N  N    . LEU   B 1 104 ? 13.099  -22.081 24.886  1.00 13.69 ? 108 LEU   B N    1 
ATOM   2449 C  CA   . LEU   B 1 104 ? 13.251  -22.655 26.216  1.00 14.27 ? 108 LEU   B CA   1 
ATOM   2450 C  C    . LEU   B 1 104 ? 11.905  -22.688 26.936  1.00 14.62 ? 108 LEU   B C    1 
ATOM   2451 O  O    . LEU   B 1 104 ? 11.540  -23.701 27.532  1.00 14.03 ? 108 LEU   B O    1 
ATOM   2452 C  CB   . LEU   B 1 104 ? 14.287  -21.885 27.033  1.00 15.34 ? 108 LEU   B CB   1 
ATOM   2453 C  CG   . LEU   B 1 104 ? 15.731  -21.975 26.537  1.00 16.88 ? 108 LEU   B CG   1 
ATOM   2454 C  CD1  . LEU   B 1 104 ? 16.618  -21.050 27.338  1.00 17.43 ? 108 LEU   B CD1  1 
ATOM   2455 C  CD2  . LEU   B 1 104 ? 16.262  -23.398 26.586  1.00 17.24 ? 108 LEU   B CD2  1 
ATOM   2456 N  N    . LEU   B 1 105 ? 11.156  -21.583 26.878  1.00 15.34 ? 109 LEU   B N    1 
ATOM   2457 C  CA   . LEU   B 1 105 ? 9.882   -21.517 27.574  1.00 16.46 ? 109 LEU   B CA   1 
ATOM   2458 C  C    . LEU   B 1 105 ? 8.873   -22.476 26.949  1.00 14.98 ? 109 LEU   B C    1 
ATOM   2459 O  O    . LEU   B 1 105 ? 8.094   -23.086 27.674  1.00 15.19 ? 109 LEU   B O    1 
ATOM   2460 C  CB   . LEU   B 1 105 ? 9.355   -20.086 27.604  1.00 19.54 ? 109 LEU   B CB   1 
ATOM   2461 C  CG   . LEU   B 1 105 ? 10.195  -19.083 28.396  1.00 25.38 ? 109 LEU   B CG   1 
ATOM   2462 C  CD1  . LEU   B 1 105 ? 9.664   -17.682 28.200  1.00 27.73 ? 109 LEU   B CD1  1 
ATOM   2463 C  CD2  . LEU   B 1 105 ? 10.234  -19.442 29.862  1.00 28.81 ? 109 LEU   B CD2  1 
ATOM   2464 N  N    . ALA   B 1 106 ? 8.864   -22.606 25.616  1.00 14.48 ? 110 ALA   B N    1 
ATOM   2465 C  CA   . ALA   B 1 106 ? 7.919   -23.513 24.970  1.00 14.48 ? 110 ALA   B CA   1 
ATOM   2466 C  C    . ALA   B 1 106 ? 8.215   -24.962 25.359  1.00 13.61 ? 110 ALA   B C    1 
ATOM   2467 O  O    . ALA   B 1 106 ? 7.305   -25.765 25.547  1.00 13.78 ? 110 ALA   B O    1 
ATOM   2468 C  CB   . ALA   B 1 106 ? 7.952   -23.328 23.471  1.00 15.27 ? 110 ALA   B CB   1 
ATOM   2469 N  N    . PHE   B 1 107 ? 9.504   -25.287 25.470  1.00 12.76 ? 111 PHE   B N    1 
ATOM   2470 C  CA   . PHE   B 1 107 ? 9.926   -26.603 25.924  1.00 12.46 ? 111 PHE   B CA   1 
ATOM   2471 C  C    . PHE   B 1 107 ? 9.463   -26.845 27.359  1.00 12.13 ? 111 PHE   B C    1 
ATOM   2472 O  O    . PHE   B 1 107 ? 8.908   -27.894 27.673  1.00 12.32 ? 111 PHE   B O    1 
ATOM   2473 C  CB   . PHE   B 1 107 ? 11.443  -26.695 25.801  1.00 11.99 ? 111 PHE   B CB   1 
ATOM   2474 C  CG   . PHE   B 1 107 ? 12.020  -28.015 26.285  1.00 11.91 ? 111 PHE   B CG   1 
ATOM   2475 C  CD1  . PHE   B 1 107 ? 12.135  -29.101 25.428  1.00 12.17 ? 111 PHE   B CD1  1 
ATOM   2476 C  CD2  . PHE   B 1 107 ? 12.410  -28.176 27.610  1.00 12.35 ? 111 PHE   B CD2  1 
ATOM   2477 C  CE1  . PHE   B 1 107 ? 12.655  -30.300 25.876  1.00 12.78 ? 111 PHE   B CE1  1 
ATOM   2478 C  CE2  . PHE   B 1 107 ? 12.935  -29.379 28.045  1.00 12.59 ? 111 PHE   B CE2  1 
ATOM   2479 C  CZ   . PHE   B 1 107 ? 13.054  -30.435 27.178  1.00 12.53 ? 111 PHE   B CZ   1 
ATOM   2480 N  N    . LEU   B 1 108 ? 9.688   -25.865 28.237  1.00 12.71 ? 112 LEU   B N    1 
ATOM   2481 C  CA   . LEU   B 1 108 ? 9.266   -25.999 29.624  1.00 13.55 ? 112 LEU   B CA   1 
ATOM   2482 C  C    . LEU   B 1 108 ? 7.747   -26.105 29.726  1.00 13.41 ? 112 LEU   B C    1 
ATOM   2483 O  O    . LEU   B 1 108 ? 7.247   -26.885 30.527  1.00 13.54 ? 112 LEU   B O    1 
ATOM   2484 C  CB   . LEU   B 1 108 ? 9.814   -24.850 30.459  1.00 15.00 ? 112 LEU   B CB   1 
ATOM   2485 C  CG   . LEU   B 1 108 ? 11.330  -24.882 30.684  1.00 16.29 ? 112 LEU   B CG   1 
ATOM   2486 C  CD1  . LEU   B 1 108 ? 11.783  -23.562 31.276  1.00 18.28 ? 112 LEU   B CD1  1 
ATOM   2487 C  CD2  . LEU   B 1 108 ? 11.756  -26.057 31.550  1.00 16.85 ? 112 LEU   B CD2  1 
ATOM   2488 N  N    . ARG   B 1 109 ? 7.013   -25.392 28.862  1.00 13.49 ? 113 ARG   B N    1 
ATOM   2489 C  CA   . ARG   B 1 109 ? 5.556   -25.423 28.913  1.00 14.68 ? 113 ARG   B CA   1 
ATOM   2490 C  C    . ARG   B 1 109 ? 4.975   -26.784 28.531  1.00 14.18 ? 113 ARG   B C    1 
ATOM   2491 O  O    . ARG   B 1 109 ? 3.815   -27.048 28.837  1.00 15.75 ? 113 ARG   B O    1 
ATOM   2492 C  CB   . ARG   B 1 109 ? 4.942   -24.304 28.068  1.00 17.07 ? 113 ARG   B CB   1 
ATOM   2493 C  CG   . ARG   B 1 109 ? 5.067   -22.976 28.801  1.00 20.05 ? 113 ARG   B CG   1 
ATOM   2494 C  CD   . ARG   B 1 109 ? 4.201   -21.890 28.184  1.00 23.69 ? 113 ARG   B CD   1 
ATOM   2495 N  NE   . ARG   B 1 109 ? 4.408   -21.777 26.741  1.00 27.31 ? 113 ARG   B NE   1 
ATOM   2496 C  CZ   . ARG   B 1 109 ? 5.199   -20.899 26.130  1.00 29.94 ? 113 ARG   B CZ   1 
ATOM   2497 N  NH1  . ARG   B 1 109 ? 5.382   -20.989 24.827  1.00 30.40 ? 113 ARG   B NH1  1 
ATOM   2498 N  NH2  . ARG   B 1 109 ? 5.827   -19.955 26.815  1.00 32.14 ? 113 ARG   B NH2  1 
ATOM   2499 N  N    . ARG   B 1 110 ? 5.762   -27.666 27.898  1.00 13.40 ? 114 ARG   B N    1 
ATOM   2500 C  CA   . ARG   B 1 110 ? 5.318   -29.029 27.647  1.00 13.64 ? 114 ARG   B CA   1 
ATOM   2501 C  C    . ARG   B 1 110 ? 5.440   -29.926 28.876  1.00 13.30 ? 114 ARG   B C    1 
ATOM   2502 O  O    . ARG   B 1 110 ? 5.007   -31.080 28.838  1.00 14.55 ? 114 ARG   B O    1 
ATOM   2503 C  CB   . ARG   B 1 110 ? 6.070   -29.661 26.474  1.00 13.96 ? 114 ARG   B CB   1 
ATOM   2504 C  CG   . ARG   B 1 110 ? 5.533   -29.060 25.182  1.00 15.09 ? 114 ARG   B CG   1 
ATOM   2505 C  CD   . ARG   B 1 110 ? 5.905   -29.797 23.949  1.00 14.82 ? 114 ARG   B CD   1 
ATOM   2506 N  NE   . ARG   B 1 110 ? 5.438   -31.182 23.921  1.00 13.69 ? 114 ARG   B NE   1 
ATOM   2507 C  CZ   . ARG   B 1 110 ? 4.259   -31.608 23.486  1.00 13.18 ? 114 ARG   B CZ   1 
ATOM   2508 N  NH1  . ARG   B 1 110 ? 3.303   -30.763 23.137  1.00 12.79 ? 114 ARG   B NH1  1 
ATOM   2509 N  NH2  . ARG   B 1 110 ? 4.044   -32.906 23.420  1.00 12.71 ? 114 ARG   B NH2  1 
ATOM   2510 N  N    . GLN   B 1 111 ? 5.982   -29.395 29.973  1.00 13.08 ? 115 GLN   B N    1 
ATOM   2511 C  CA   . GLN   B 1 111 ? 6.205   -30.193 31.163  1.00 13.49 ? 115 GLN   B CA   1 
ATOM   2512 C  C    . GLN   B 1 111 ? 5.209   -29.781 32.240  1.00 14.19 ? 115 GLN   B C    1 
ATOM   2513 O  O    . GLN   B 1 111 ? 4.971   -28.588 32.448  1.00 14.85 ? 115 GLN   B O    1 
ATOM   2514 C  CB   . GLN   B 1 111 ? 7.607   -29.999 31.737  1.00 13.57 ? 115 GLN   B CB   1 
ATOM   2515 C  CG   . GLN   B 1 111 ? 8.729   -29.970 30.704  1.00 13.21 ? 115 GLN   B CG   1 
ATOM   2516 C  CD   . GLN   B 1 111 ? 8.714   -31.137 29.740  1.00 12.70 ? 115 GLN   B CD   1 
ATOM   2517 O  OE1  . GLN   B 1 111 ? 8.417   -32.282 30.105  1.00 13.64 ? 115 GLN   B OE1  1 
ATOM   2518 N  NE2  . GLN   B 1 111 ? 9.035   -30.850 28.490  1.00 12.46 ? 115 GLN   B NE2  1 
ATOM   2519 N  N    . PRO   B 1 112 ? 4.627   -30.749 32.978  1.00 15.03 ? 116 PRO   B N    1 
ATOM   2520 C  CA   . PRO   B 1 112 ? 3.785   -30.422 34.127  1.00 15.90 ? 116 PRO   B CA   1 
ATOM   2521 C  C    . PRO   B 1 112 ? 4.534   -29.620 35.189  1.00 15.78 ? 116 PRO   B C    1 
ATOM   2522 O  O    . PRO   B 1 112 ? 5.708   -29.870 35.467  1.00 15.57 ? 116 PRO   B O    1 
ATOM   2523 C  CB   . PRO   B 1 112 ? 3.335   -31.778 34.670  1.00 17.14 ? 116 PRO   B CB   1 
ATOM   2524 C  CG   . PRO   B 1 112 ? 3.660   -32.792 33.623  1.00 18.23 ? 116 PRO   B CG   1 
ATOM   2525 C  CD   . PRO   B 1 112 ? 4.691   -32.193 32.707  1.00 16.06 ? 116 PRO   B CD   1 
ATOM   2526 N  N    . GLN   B 1 113 ? 3.825   -28.657 35.780  1.00 16.92 ? 117 GLN   B N    1 
ATOM   2527 C  CA   . GLN   B 1 113 ? 4.383   -27.803 36.815  1.00 17.14 ? 117 GLN   B CA   1 
ATOM   2528 C  C    . GLN   B 1 113 ? 4.017   -28.332 38.201  1.00 16.01 ? 117 GLN   B C    1 
ATOM   2529 O  O    . GLN   B 1 113 ? 2.995   -29.001 38.370  1.00 16.51 ? 117 GLN   B O    1 
ATOM   2530 C  CB   . GLN   B 1 113 ? 3.896   -26.362 36.662  1.00 19.82 ? 117 GLN   B CB   1 
ATOM   2531 C  CG   . GLN   B 1 113 ? 4.632   -25.603 35.561  1.00 22.57 ? 117 GLN   B CG   1 
ATOM   2532 C  CD   . GLN   B 1 113 ? 4.349   -24.117 35.575  1.00 26.36 ? 117 GLN   B CD   1 
ATOM   2533 O  OE1  . GLN   B 1 113 ? 5.062   -23.313 36.191  1.00 28.54 ? 117 GLN   B OE1  1 
ATOM   2534 N  NE2  . GLN   B 1 113 ? 3.259   -23.747 34.932  1.00 29.39 ? 117 GLN   B NE2  1 
ATOM   2535 N  N    . PRO   B 1 114 ? 4.796   -28.016 39.263  1.00 16.03 ? 118 PRO   B N    1 
ATOM   2536 C  CA   . PRO   B 1 114 ? 6.022   -27.209 39.188  1.00 16.11 ? 118 PRO   B CA   1 
ATOM   2537 C  C    . PRO   B 1 114 ? 7.214   -27.856 38.496  1.00 15.59 ? 118 PRO   B C    1 
ATOM   2538 O  O    . PRO   B 1 114 ? 7.384   -29.069 38.589  1.00 15.41 ? 118 PRO   B O    1 
ATOM   2539 C  CB   . PRO   B 1 114 ? 6.375   -26.966 40.676  1.00 17.60 ? 118 PRO   B CB   1 
ATOM   2540 C  CG   . PRO   B 1 114 ? 5.152   -27.286 41.457  1.00 18.49 ? 118 PRO   B CG   1 
ATOM   2541 C  CD   . PRO   B 1 114 ? 4.411   -28.312 40.648  1.00 16.64 ? 118 PRO   B CD   1 
ATOM   2542 N  N    . TRP   B 1 115 ? 8.027   -27.005 37.853  1.00 14.96 ? 119 TRP   B N    1 
ATOM   2543 C  CA   . TRP   B 1 115 ? 9.301   -27.365 37.248  1.00 15.28 ? 119 TRP   B CA   1 
ATOM   2544 C  C    . TRP   B 1 115 ? 10.420  -27.163 38.251  1.00 14.22 ? 119 TRP   B C    1 
ATOM   2545 O  O    . TRP   B 1 115 ? 10.487  -26.104 38.863  1.00 14.28 ? 119 TRP   B O    1 
ATOM   2546 C  CB   . TRP   B 1 115 ? 9.622   -26.441 36.065  1.00 16.41 ? 119 TRP   B CB   1 
ATOM   2547 C  CG   . TRP   B 1 115 ? 8.568   -26.316 35.006  1.00 16.07 ? 119 TRP   B CG   1 
ATOM   2548 C  CD1  . TRP   B 1 115 ? 7.709   -27.269 34.556  1.00 16.40 ? 119 TRP   B CD1  1 
ATOM   2549 C  CD2  . TRP   B 1 115 ? 8.261   -25.111 34.274  1.00 17.35 ? 119 TRP   B CD2  1 
ATOM   2550 N  NE1  . TRP   B 1 115 ? 6.894   -26.746 33.591  1.00 16.80 ? 119 TRP   B NE1  1 
ATOM   2551 C  CE2  . TRP   B 1 115 ? 7.200   -25.424 33.401  1.00 17.53 ? 119 TRP   B CE2  1 
ATOM   2552 C  CE3  . TRP   B 1 115 ? 8.763   -23.803 34.279  1.00 19.46 ? 119 TRP   B CE3  1 
ATOM   2553 C  CZ2  . TRP   B 1 115 ? 6.638   -24.482 32.542  1.00 18.67 ? 119 TRP   B CZ2  1 
ATOM   2554 C  CZ3  . TRP   B 1 115 ? 8.204   -22.872 33.423  1.00 20.13 ? 119 TRP   B CZ3  1 
ATOM   2555 C  CH2  . TRP   B 1 115 ? 7.150   -23.208 32.571  1.00 19.59 ? 119 TRP   B CH2  1 
ATOM   2556 N  N    . CYS   B 1 116 ? 11.366  -28.099 38.304  1.00 13.31 ? 120 CYS   B N    1 
ATOM   2557 C  CA   . CYS   B 1 116 ? 12.568  -27.888 39.095  1.00 13.12 ? 120 CYS   B CA   1 
ATOM   2558 C  C    . CYS   B 1 116 ? 13.805  -28.195 38.256  1.00 12.91 ? 120 CYS   B C    1 
ATOM   2559 O  O    . CYS   B 1 116 ? 14.034  -29.347 37.893  1.00 13.18 ? 120 CYS   B O    1 
ATOM   2560 C  CB   . CYS   B 1 116 ? 12.544  -28.746 40.355  1.00 14.36 ? 120 CYS   B CB   1 
ATOM   2561 S  SG   . CYS   B 1 116 ? 13.873  -28.344 41.519  1.00 15.37 ? 120 CYS   B SG   1 
ATOM   2562 N  N    . LEU   B 1 117 ? 14.628  -27.167 38.010  1.00 13.06 ? 121 LEU   B N    1 
ATOM   2563 C  CA   . LEU   B 1 117 ? 15.916  -27.352 37.358  1.00 13.62 ? 121 LEU   B CA   1 
ATOM   2564 C  C    . LEU   B 1 117 ? 16.866  -28.013 38.350  1.00 13.42 ? 121 LEU   B C    1 
ATOM   2565 O  O    . LEU   B 1 117 ? 16.904  -27.611 39.517  1.00 14.95 ? 121 LEU   B O    1 
ATOM   2566 C  CB   . LEU   B 1 117 ? 16.470  -25.998 36.924  1.00 14.39 ? 121 LEU   B CB   1 
ATOM   2567 C  CG   . LEU   B 1 117 ? 15.644  -25.208 35.908  1.00 16.35 ? 121 LEU   B CG   1 
ATOM   2568 C  CD1  . LEU   B 1 117 ? 16.170  -23.785 35.786  1.00 17.61 ? 121 LEU   B CD1  1 
ATOM   2569 C  CD2  . LEU   B 1 117 ? 15.683  -25.886 34.569  1.00 18.24 ? 121 LEU   B CD2  1 
ATOM   2570 N  N    . VAL   B 1 118 ? 17.634  -29.004 37.884  1.00 12.21 ? 122 VAL   B N    1 
ATOM   2571 C  CA   . VAL   B 1 118 ? 18.589  -29.717 38.713  1.00 12.33 ? 122 VAL   B CA   1 
ATOM   2572 C  C    . VAL   B 1 118 ? 19.935  -29.670 38.000  1.00 11.76 ? 122 VAL   B C    1 
ATOM   2573 O  O    . VAL   B 1 118 ? 20.033  -30.147 36.879  1.00 12.01 ? 122 VAL   B O    1 
ATOM   2574 C  CB   . VAL   B 1 118 ? 18.161  -31.176 38.960  1.00 12.99 ? 122 VAL   B CB   1 
ATOM   2575 C  CG1  . VAL   B 1 118 ? 19.196  -31.920 39.799  1.00 13.58 ? 122 VAL   B CG1  1 
ATOM   2576 C  CG2  . VAL   B 1 118 ? 16.761  -31.264 39.560  1.00 13.67 ? 122 VAL   B CG2  1 
ATOM   2577 N  N    . ALA   B 1 119 ? 20.950  -29.073 38.632  1.00 12.13 ? 123 ALA   B N    1 
ATOM   2578 C  CA   . ALA   B 1 119 ? 22.242  -28.880 37.990  1.00 12.31 ? 123 ALA   B CA   1 
ATOM   2579 C  C    . ALA   B 1 119 ? 23.347  -29.046 39.027  1.00 12.44 ? 123 ALA   B C    1 
ATOM   2580 O  O    . ALA   B 1 119 ? 23.184  -28.651 40.182  1.00 12.62 ? 123 ALA   B O    1 
ATOM   2581 C  CB   . ALA   B 1 119 ? 22.315  -27.522 37.338  1.00 12.66 ? 123 ALA   B CB   1 
ATOM   2582 N  N    . HIS   B 1 120 ? 24.476  -29.603 38.589  1.00 12.78 ? 124 HIS   B N    1 
ATOM   2583 C  CA   . HIS   B 1 120 ? 25.557  -29.949 39.498  1.00 13.59 ? 124 HIS   B CA   1 
ATOM   2584 C  C    . HIS   B 1 120 ? 26.465  -28.734 39.690  1.00 13.75 ? 124 HIS   B C    1 
ATOM   2585 O  O    . HIS   B 1 120 ? 27.070  -28.250 38.739  1.00 14.38 ? 124 HIS   B O    1 
ATOM   2586 C  CB   . HIS   B 1 120 ? 26.316  -31.156 38.944  1.00 15.33 ? 124 HIS   B CB   1 
ATOM   2587 C  CG   . HIS   B 1 120 ? 27.064  -31.897 39.989  1.00 17.51 ? 124 HIS   B CG   1 
ATOM   2588 N  ND1  . HIS   B 1 120 ? 26.389  -32.644 40.932  1.00 19.23 ? 124 HIS   B ND1  1 
ATOM   2589 C  CD2  . HIS   B 1 120 ? 28.364  -32.029 40.258  1.00 19.32 ? 124 HIS   B CD2  1 
ATOM   2590 C  CE1  . HIS   B 1 120 ? 27.276  -33.218 41.735  1.00 20.43 ? 124 HIS   B CE1  1 
ATOM   2591 N  NE2  . HIS   B 1 120 ? 28.482  -32.840 41.352  1.00 20.40 ? 124 HIS   B NE2  1 
ATOM   2592 N  N    . ASN   B 1 121 ? 26.547  -28.220 40.922  1.00 13.61 ? 125 ASN   B N    1 
ATOM   2593 C  CA   . ASN   B 1 121 ? 27.133  -26.905 41.159  1.00 14.19 ? 125 ASN   B CA   1 
ATOM   2594 C  C    . ASN   B 1 121 ? 26.324  -25.845 40.407  1.00 13.76 ? 125 ASN   B C    1 
ATOM   2595 O  O    . ASN   B 1 121 ? 26.850  -24.815 39.998  1.00 14.09 ? 125 ASN   B O    1 
ATOM   2596 C  CB   . ASN   B 1 121 ? 28.628  -26.854 40.821  1.00 15.53 ? 125 ASN   B CB   1 
ATOM   2597 C  CG   . ASN   B 1 121 ? 29.520  -26.775 42.037  1.00 18.44 ? 125 ASN   B CG   1 
ATOM   2598 O  OD1  . ASN   B 1 121 ? 29.177  -26.119 43.027  1.00 20.68 ? 125 ASN   B OD1  1 
ATOM   2599 N  ND2  . ASN   B 1 121 ? 30.652  -27.460 41.992  1.00 20.23 ? 125 ASN   B ND2  1 
ATOM   2600 N  N    . GLY   B 1 122 ? 25.014  -26.072 40.287  1.00 13.23 ? 126 GLY   B N    1 
ATOM   2601 C  CA   . GLY   B 1 122 ? 24.149  -25.125 39.616  1.00 13.23 ? 126 GLY   B CA   1 
ATOM   2602 C  C    . GLY   B 1 122 ? 24.123  -23.743 40.267  1.00 13.35 ? 126 GLY   B C    1 
ATOM   2603 O  O    . GLY   B 1 122 ? 23.913  -22.751 39.576  1.00 13.09 ? 126 GLY   B O    1 
ATOM   2604 N  N    . ASP   B 1 123 ? 24.286  -23.662 41.595  1.00 14.12 ? 127 ASP   B N    1 
ATOM   2605 C  CA   . ASP   B 1 123 ? 24.195  -22.369 42.257  1.00 15.69 ? 127 ASP   B CA   1 
ATOM   2606 C  C    . ASP   B 1 123 ? 25.359  -21.460 41.856  1.00 15.80 ? 127 ASP   B C    1 
ATOM   2607 O  O    . ASP   B 1 123 ? 25.244  -20.227 41.867  1.00 17.36 ? 127 ASP   B O    1 
ATOM   2608 C  CB   . ASP   B 1 123 ? 24.133  -22.524 43.768  1.00 16.88 ? 127 ASP   B CB   1 
ATOM   2609 C  CG   . ASP   B 1 123 ? 22.823  -23.062 44.326  1.00 19.77 ? 127 ASP   B CG   1 
ATOM   2610 O  OD1  . ASP   B 1 123 ? 21.867  -23.214 43.543  1.00 21.30 ? 127 ASP   B OD1  1 
ATOM   2611 O  OD2  . ASP   B 1 123 ? 22.766  -23.292 45.556  1.00 23.42 ? 127 ASP   B OD2  1 
ATOM   2612 N  N    . ARG   B 1 124 ? 26.492  -22.068 41.518  1.00 15.76 ? 128 ARG   B N    1 
ATOM   2613 C  CA   . ARG   B 1 124 ? 27.669  -21.319 41.110  1.00 16.82 ? 128 ARG   B CA   1 
ATOM   2614 C  C    . ARG   B 1 124 ? 27.719  -21.058 39.601  1.00 15.74 ? 128 ARG   B C    1 
ATOM   2615 O  O    . ARG   B 1 124 ? 28.221  -20.015 39.172  1.00 16.82 ? 128 ARG   B O    1 
ATOM   2616 C  CB   . ARG   B 1 124 ? 28.921  -22.120 41.466  1.00 18.94 ? 128 ARG   B CB   1 
ATOM   2617 C  CG   . ARG   B 1 124 ? 30.192  -21.305 41.315  1.00 21.60 ? 128 ARG   B CG   1 
ATOM   2618 C  CD   . ARG   B 1 124 ? 31.375  -22.234 41.444  1.00 23.58 ? 128 ARG   B CD   1 
ATOM   2619 N  NE   . ARG   B 1 124 ? 31.418  -22.801 42.791  1.00 25.82 ? 128 ARG   B NE   1 
ATOM   2620 C  CZ   . ARG   B 1 124 ? 32.042  -23.925 43.106  1.00 27.42 ? 128 ARG   B CZ   1 
ATOM   2621 N  NH1  . ARG   B 1 124 ? 31.988  -24.359 44.348  1.00 29.39 ? 128 ARG   B NH1  1 
ATOM   2622 N  NH2  . ARG   B 1 124 ? 32.706  -24.601 42.180  1.00 28.41 ? 128 ARG   B NH2  1 
ATOM   2623 N  N    . TYR   B 1 125 ? 27.258  -22.022 38.795  1.00 13.54 ? 129 TYR   B N    1 
ATOM   2624 C  CA   . TYR   B 1 125 ? 27.482  -21.994 37.354  1.00 12.99 ? 129 TYR   B CA   1 
ATOM   2625 C  C    . TYR   B 1 125 ? 26.169  -21.768 36.612  1.00 12.42 ? 129 TYR   B C    1 
ATOM   2626 O  O    . TYR   B 1 125 ? 25.890  -20.660 36.162  1.00 12.78 ? 129 TYR   B O    1 
ATOM   2627 C  CB   . TYR   B 1 125 ? 28.147  -23.302 36.922  1.00 13.63 ? 129 TYR   B CB   1 
ATOM   2628 C  CG   . TYR   B 1 125 ? 29.519  -23.577 37.522  1.00 14.46 ? 129 TYR   B CG   1 
ATOM   2629 C  CD1  . TYR   B 1 125 ? 30.507  -22.604 37.559  1.00 15.29 ? 129 TYR   B CD1  1 
ATOM   2630 C  CD2  . TYR   B 1 125 ? 29.832  -24.834 38.025  1.00 16.02 ? 129 TYR   B CD2  1 
ATOM   2631 C  CE1  . TYR   B 1 125 ? 31.757  -22.863 38.093  1.00 16.89 ? 129 TYR   B CE1  1 
ATOM   2632 C  CE2  . TYR   B 1 125 ? 31.077  -25.106 38.562  1.00 17.43 ? 129 TYR   B CE2  1 
ATOM   2633 C  CZ   . TYR   B 1 125 ? 32.044  -24.115 38.604  1.00 17.57 ? 129 TYR   B CZ   1 
ATOM   2634 O  OH   . TYR   B 1 125 ? 33.278  -24.376 39.140  1.00 21.45 ? 129 TYR   B OH   1 
ATOM   2635 N  N    . ASP   B 1 126 ? 25.359  -22.826 36.496  1.00 11.70 ? 130 ASP   B N    1 
ATOM   2636 C  CA   . ASP   B 1 126 ? 24.281  -22.851 35.520  1.00 12.15 ? 130 ASP   B CA   1 
ATOM   2637 C  C    . ASP   B 1 126 ? 23.173  -21.858 35.856  1.00 12.01 ? 130 ASP   B C    1 
ATOM   2638 O  O    . ASP   B 1 126 ? 22.648  -21.185 34.969  1.00 12.58 ? 130 ASP   B O    1 
ATOM   2639 C  CB   . ASP   B 1 126 ? 23.722  -24.254 35.392  1.00 12.10 ? 130 ASP   B CB   1 
ATOM   2640 C  CG   . ASP   B 1 126 ? 24.823  -25.292 35.254  1.00 12.41 ? 130 ASP   B CG   1 
ATOM   2641 O  OD1  . ASP   B 1 126 ? 25.420  -25.647 36.296  1.00 13.13 ? 130 ASP   B OD1  1 
ATOM   2642 O  OD2  . ASP   B 1 126 ? 25.128  -25.662 34.112  1.00 13.62 ? 130 ASP   B OD2  1 
ATOM   2643 N  N    . PHE   B 1 127 ? 22.771  -21.798 37.126  1.00 12.13 ? 131 PHE   B N    1 
ATOM   2644 C  CA   . PHE   B 1 127 ? 21.611  -20.990 37.467  1.00 12.62 ? 131 PHE   B CA   1 
ATOM   2645 C  C    . PHE   B 1 127 ? 21.922  -19.499 37.312  1.00 13.02 ? 131 PHE   B C    1 
ATOM   2646 O  O    . PHE   B 1 127 ? 21.157  -18.779 36.658  1.00 13.48 ? 131 PHE   B O    1 
ATOM   2647 C  CB   . PHE   B 1 127 ? 21.080  -21.341 38.854  1.00 13.05 ? 131 PHE   B CB   1 
ATOM   2648 C  CG   . PHE   B 1 127 ? 20.706  -22.802 39.055  1.00 13.17 ? 131 PHE   B CG   1 
ATOM   2649 C  CD1  . PHE   B 1 127 ? 20.239  -23.594 38.012  1.00 13.53 ? 131 PHE   B CD1  1 
ATOM   2650 C  CD2  . PHE   B 1 127 ? 20.810  -23.371 40.318  1.00 13.90 ? 131 PHE   B CD2  1 
ATOM   2651 C  CE1  . PHE   B 1 127 ? 19.903  -24.918 38.237  1.00 13.74 ? 131 PHE   B CE1  1 
ATOM   2652 C  CE2  . PHE   B 1 127 ? 20.469  -24.689 40.535  1.00 13.90 ? 131 PHE   B CE2  1 
ATOM   2653 C  CZ   . PHE   B 1 127 ? 20.018  -25.458 39.499  1.00 14.26 ? 131 PHE   B CZ   1 
ATOM   2654 N  N    . PRO   B 1 128 ? 23.015  -18.962 37.893  1.00 13.46 ? 132 PRO   B N    1 
ATOM   2655 C  CA   . PRO   B 1 128 ? 23.298  -17.538 37.754  1.00 13.62 ? 132 PRO   B CA   1 
ATOM   2656 C  C    . PRO   B 1 128 ? 23.611  -17.130 36.320  1.00 13.15 ? 132 PRO   B C    1 
ATOM   2657 O  O    . PRO   B 1 128 ? 23.284  -16.017 35.921  1.00 13.81 ? 132 PRO   B O    1 
ATOM   2658 C  CB   . PRO   B 1 128 ? 24.465  -17.261 38.706  1.00 14.42 ? 132 PRO   B CB   1 
ATOM   2659 C  CG   . PRO   B 1 128 ? 25.051  -18.608 39.013  1.00 15.26 ? 132 PRO   B CG   1 
ATOM   2660 C  CD   . PRO   B 1 128 ? 23.945  -19.618 38.831  1.00 14.05 ? 132 PRO   B CD   1 
ATOM   2661 N  N    . LEU   B 1 129 ? 24.221  -18.029 35.542  1.00 12.60 ? 133 LEU   B N    1 
ATOM   2662 C  CA   . LEU   B 1 129 ? 24.504  -17.691 34.155  1.00 12.43 ? 133 LEU   B CA   1 
ATOM   2663 C  C    . LEU   B 1 129 ? 23.208  -17.623 33.345  1.00 12.69 ? 133 LEU   B C    1 
ATOM   2664 O  O    . LEU   B 1 129 ? 23.027  -16.710 32.541  1.00 12.94 ? 133 LEU   B O    1 
ATOM   2665 C  CB   . LEU   B 1 129 ? 25.522  -18.633 33.527  1.00 12.24 ? 133 LEU   B CB   1 
ATOM   2666 C  CG   . LEU   B 1 129 ? 25.876  -18.309 32.071  1.00 12.67 ? 133 LEU   B CG   1 
ATOM   2667 C  CD1  . LEU   B 1 129 ? 26.297  -16.846 31.901  1.00 13.55 ? 133 LEU   B CD1  1 
ATOM   2668 C  CD2  . LEU   B 1 129 ? 26.959  -19.239 31.582  1.00 12.79 ? 133 LEU   B CD2  1 
ATOM   2669 N  N    . LEU   B 1 130 ? 22.304  -18.586 33.541  1.00 12.48 ? 134 LEU   B N    1 
ATOM   2670 C  CA   . LEU   B 1 130 ? 21.024  -18.534 32.845  1.00 13.03 ? 134 LEU   B CA   1 
ATOM   2671 C  C    . LEU   B 1 130 ? 20.306  -17.230 33.191  1.00 13.74 ? 134 LEU   B C    1 
ATOM   2672 O  O    . LEU   B 1 130 ? 19.772  -16.558 32.318  1.00 14.43 ? 134 LEU   B O    1 
ATOM   2673 C  CB   . LEU   B 1 130 ? 20.167  -19.752 33.171  1.00 13.43 ? 134 LEU   B CB   1 
ATOM   2674 C  CG   . LEU   B 1 130 ? 18.775  -19.797 32.531  1.00 14.25 ? 134 LEU   B CG   1 
ATOM   2675 C  CD1  . LEU   B 1 130 ? 18.849  -19.775 31.009  1.00 14.88 ? 134 LEU   B CD1  1 
ATOM   2676 C  CD2  . LEU   B 1 130 ? 18.050  -21.022 33.023  1.00 14.91 ? 134 LEU   B CD2  1 
ATOM   2677 N  N    . GLN   B 1 131 ? 20.288  -16.874 34.479  1.00 14.78 ? 135 GLN   B N    1 
ATOM   2678 C  CA   . GLN   B 1 131 ? 19.650  -15.637 34.901  1.00 16.06 ? 135 GLN   B CA   1 
ATOM   2679 C  C    . GLN   B 1 131 ? 20.304  -14.418 34.246  1.00 15.48 ? 135 GLN   B C    1 
ATOM   2680 O  O    . GLN   B 1 131 ? 19.603  -13.478 33.864  1.00 16.36 ? 135 GLN   B O    1 
ATOM   2681 C  CB   . GLN   B 1 131 ? 19.675  -15.550 36.426  1.00 17.94 ? 135 GLN   B CB   1 
ATOM   2682 C  CG   . GLN   B 1 131 ? 18.602  -16.402 37.085  1.00 21.07 ? 135 GLN   B CG   1 
ATOM   2683 C  CD   . GLN   B 1 131 ? 17.229  -15.765 37.037  1.00 23.23 ? 135 GLN   B CD   1 
ATOM   2684 O  OE1  . GLN   B 1 131 ? 16.701  -15.410 35.976  1.00 24.52 ? 135 GLN   B OE1  1 
ATOM   2685 N  NE2  . GLN   B 1 131 ? 16.617  -15.658 38.202  1.00 24.87 ? 135 GLN   B NE2  1 
ATOM   2686 N  N    . ALA   B 1 132 ? 21.637  -14.436 34.102  1.00 15.14 ? 136 ALA   B N    1 
ATOM   2687 C  CA   . ALA   B 1 132 ? 22.344  -13.321 33.485  1.00 14.80 ? 136 ALA   B CA   1 
ATOM   2688 C  C    . ALA   B 1 132 ? 21.947  -13.180 32.015  1.00 15.40 ? 136 ALA   B C    1 
ATOM   2689 O  O    . ALA   B 1 132 ? 21.687  -12.074 31.542  1.00 17.25 ? 136 ALA   B O    1 
ATOM   2690 C  CB   . ALA   B 1 132 ? 23.837  -13.485 33.622  1.00 15.22 ? 136 ALA   B CB   1 
ATOM   2691 N  N    . GLU   B 1 133 ? 21.925  -14.299 31.284  1.00 14.95 ? 137 GLU   B N    1 
ATOM   2692 C  CA   . GLU   B 1 133 ? 21.583  -14.274 29.870  1.00 15.82 ? 137 GLU   B CA   1 
ATOM   2693 C  C    . GLU   B 1 133 ? 20.148  -13.779 29.684  1.00 16.66 ? 137 GLU   B C    1 
ATOM   2694 O  O    . GLU   B 1 133 ? 19.865  -13.006 28.772  1.00 17.93 ? 137 GLU   B O    1 
ATOM   2695 C  CB   . GLU   B 1 133 ? 21.765  -15.658 29.247  1.00 16.53 ? 137 GLU   B CB   1 
ATOM   2696 C  CG   . GLU   B 1 133 ? 23.214  -16.137 29.149  1.00 16.80 ? 137 GLU   B CG   1 
ATOM   2697 C  CD   . GLU   B 1 133 ? 24.030  -15.636 27.962  1.00 18.31 ? 137 GLU   B CD   1 
ATOM   2698 O  OE1  . GLU   B 1 133 ? 23.588  -14.672 27.293  1.00 20.18 ? 137 GLU   B OE1  1 
ATOM   2699 O  OE2  . GLU   B 1 133 ? 25.111  -16.215 27.689  1.00 18.11 ? 137 GLU   B OE2  1 
ATOM   2700 N  N    . LEU   B 1 134 ? 19.227  -14.224 30.541  1.00 16.94 ? 138 LEU   B N    1 
ATOM   2701 C  CA   . LEU   B 1 134 ? 17.845  -13.778 30.430  1.00 18.17 ? 138 LEU   B CA   1 
ATOM   2702 C  C    . LEU   B 1 134 ? 17.734  -12.290 30.748  1.00 19.29 ? 138 LEU   B C    1 
ATOM   2703 O  O    . LEU   B 1 134 ? 16.983  -11.579 30.083  1.00 20.64 ? 138 LEU   B O    1 
ATOM   2704 C  CB   . LEU   B 1 134 ? 16.925  -14.606 31.319  1.00 19.12 ? 138 LEU   B CB   1 
ATOM   2705 C  CG   . LEU   B 1 134 ? 16.742  -16.065 30.898  1.00 19.98 ? 138 LEU   B CG   1 
ATOM   2706 C  CD1  . LEU   B 1 134 ? 15.994  -16.814 31.975  1.00 21.39 ? 138 LEU   B CD1  1 
ATOM   2707 C  CD2  . LEU   B 1 134 ? 16.019  -16.197 29.566  1.00 20.54 ? 138 LEU   B CD2  1 
ATOM   2708 N  N    . ALA   B 1 135 ? 18.492  -11.828 31.751  1.00 19.73 ? 139 ALA   B N    1 
ATOM   2709 C  CA   . ALA   B 1 135 ? 18.436  -10.433 32.163  1.00 21.44 ? 139 ALA   B CA   1 
ATOM   2710 C  C    . ALA   B 1 135 ? 18.945  -9.519  31.049  1.00 21.57 ? 139 ALA   B C    1 
ATOM   2711 O  O    . ALA   B 1 135 ? 18.413  -8.425  30.861  1.00 23.13 ? 139 ALA   B O    1 
ATOM   2712 C  CB   . ALA   B 1 135 ? 19.204  -10.228 33.450  1.00 21.70 ? 139 ALA   B CB   1 
ATOM   2713 N  N    . MET   B 1 136 ? 19.950  -9.976  30.289  1.00 21.50 ? 140 MET   B N    1 
ATOM   2714 C  CA   . MET   B 1 136 ? 20.471  -9.192  29.179  1.00 23.08 ? 140 MET   B CA   1 
ATOM   2715 C  C    . MET   B 1 136 ? 19.397  -8.984  28.107  1.00 23.68 ? 140 MET   B C    1 
ATOM   2716 O  O    . MET   B 1 136 ? 19.465  -8.004  27.369  1.00 25.96 ? 140 MET   B O    1 
ATOM   2717 C  CB   . MET   B 1 136 ? 21.727  -9.830  28.572  1.00 25.28 ? 140 MET   B CB   1 
ATOM   2718 C  CG   . MET   B 1 136 ? 22.950  -9.793  29.473  1.00 28.12 ? 140 MET   B CG   1 
ATOM   2719 S  SD   . MET   B 1 136 ? 23.478  -8.123  29.909  1.00 35.82 ? 140 MET   B SD   1 
ATOM   2720 C  CE   . MET   B 1 136 ? 24.809  -8.449  31.068  1.00 37.62 ? 140 MET   B CE   1 
ATOM   2721 N  N    . LEU   B 1 137 ? 18.406  -9.889  28.028  1.00 22.77 ? 141 LEU   B N    1 
ATOM   2722 C  CA   . LEU   B 1 137 ? 17.307  -9.786  27.073  1.00 24.21 ? 141 LEU   B CA   1 
ATOM   2723 C  C    . LEU   B 1 137 ? 16.105  -9.059  27.668  1.00 27.33 ? 141 LEU   B C    1 
ATOM   2724 O  O    . LEU   B 1 137 ? 15.111  -8.846  26.971  1.00 29.07 ? 141 LEU   B O    1 
ATOM   2725 C  CB   . LEU   B 1 137 ? 16.877  -11.179 26.622  1.00 23.63 ? 141 LEU   B CB   1 
ATOM   2726 C  CG   . LEU   B 1 137 ? 17.950  -12.010 25.923  1.00 23.41 ? 141 LEU   B CG   1 
ATOM   2727 C  CD1  . LEU   B 1 137 ? 17.414  -13.401 25.664  1.00 22.92 ? 141 LEU   B CD1  1 
ATOM   2728 C  CD2  . LEU   B 1 137 ? 18.412  -11.357 24.638  1.00 24.68 ? 141 LEU   B CD2  1 
ATOM   2729 N  N    . GLY   B 1 138 ? 16.179  -8.719  28.957  1.00 29.07 ? 142 GLY   B N    1 
ATOM   2730 C  CA   . GLY   B 1 138 ? 15.079  -8.058  29.638  1.00 31.72 ? 142 GLY   B CA   1 
ATOM   2731 C  C    . GLY   B 1 138 ? 13.987  -9.046  30.031  1.00 32.55 ? 142 GLY   B C    1 
ATOM   2732 O  O    . GLY   B 1 138 ? 12.830  -8.659  30.178  1.00 35.54 ? 142 GLY   B O    1 
ATOM   2733 N  N    . LEU   B 1 139 ? 14.369  -10.319 30.206  1.00 33.56 ? 143 LEU   B N    1 
ATOM   2734 C  CA   . LEU   B 1 139 ? 13.429  -11.364 30.568  1.00 35.08 ? 143 LEU   B CA   1 
ATOM   2735 C  C    . LEU   B 1 139 ? 13.733  -11.840 31.988  1.00 37.41 ? 143 LEU   B C    1 
ATOM   2736 O  O    . LEU   B 1 139 ? 13.734  -13.033 32.258  1.00 38.48 ? 143 LEU   B O    1 
ATOM   2737 C  CB   . LEU   B 1 139 ? 13.517  -12.479 29.526  1.00 34.70 ? 143 LEU   B CB   1 
ATOM   2738 C  CG   . LEU   B 1 139 ? 13.225  -12.063 28.078  1.00 35.77 ? 143 LEU   B CG   1 
ATOM   2739 C  CD1  . LEU   B 1 139 ? 13.503  -13.195 27.107  1.00 36.81 ? 143 LEU   B CD1  1 
ATOM   2740 C  CD2  . LEU   B 1 139 ? 11.795  -11.574 27.894  1.00 36.31 ? 143 LEU   B CD2  1 
ATOM   2741 N  N    . THR   B 1 140 ? 13.909  -10.879 32.907  1.00 42.70 ? 144 THR   B N    1 
ATOM   2742 C  CA   . THR   B 1 140 ? 14.392  -11.167 34.251  1.00 46.04 ? 144 THR   B CA   1 
ATOM   2743 C  C    . THR   B 1 140 ? 13.409  -12.067 35.006  1.00 48.43 ? 144 THR   B C    1 
ATOM   2744 O  O    . THR   B 1 140 ? 13.839  -12.855 35.845  1.00 52.78 ? 144 THR   B O    1 
ATOM   2745 C  CB   . THR   B 1 140 ? 14.675  -9.870  35.015  1.00 48.13 ? 144 THR   B CB   1 
ATOM   2746 O  OG1  . THR   B 1 140 ? 13.484  -9.089  35.019  1.00 50.12 ? 144 THR   B OG1  1 
ATOM   2747 C  CG2  . THR   B 1 140 ? 15.791  -9.051  34.388  1.00 48.30 ? 144 THR   B CG2  1 
ATOM   2748 N  N    . SER   B 1 141 ? 12.107  -11.974 34.690  1.00 47.40 ? 145 SER   B N    1 
ATOM   2749 C  CA   . SER   B 1 141 ? 11.070  -12.671 35.441  1.00 47.14 ? 145 SER   B CA   1 
ATOM   2750 C  C    . SER   B 1 141 ? 10.550  -13.913 34.710  1.00 46.73 ? 145 SER   B C    1 
ATOM   2751 O  O    . SER   B 1 141 ? 9.576   -14.521 35.154  1.00 45.61 ? 145 SER   B O    1 
ATOM   2752 C  CB   . SER   B 1 141 ? 9.931   -11.740 35.740  1.00 48.43 ? 145 SER   B CB   1 
ATOM   2753 O  OG   . SER   B 1 141 ? 9.197   -11.469 34.554  1.00 50.50 ? 145 SER   B OG   1 
ATOM   2754 N  N    . ALA   B 1 142 ? 11.202  -14.308 33.609  1.00 44.39 ? 146 ALA   B N    1 
ATOM   2755 C  CA   . ALA   B 1 142 ? 10.658  -15.326 32.718  1.00 41.77 ? 146 ALA   B CA   1 
ATOM   2756 C  C    . ALA   B 1 142 ? 10.501  -16.678 33.421  1.00 38.79 ? 146 ALA   B C    1 
ATOM   2757 O  O    . ALA   B 1 142 ? 9.622   -17.457 33.052  1.00 38.54 ? 146 ALA   B O    1 
ATOM   2758 C  CB   . ALA   B 1 142 ? 11.530  -15.448 31.486  1.00 41.75 ? 146 ALA   B CB   1 
ATOM   2759 N  N    . LEU   B 1 143 ? 11.347  -16.953 34.425  1.00 35.24 ? 147 LEU   B N    1 
ATOM   2760 C  CA   . LEU   B 1 143 ? 11.347  -18.237 35.116  1.00 31.98 ? 147 LEU   B CA   1 
ATOM   2761 C  C    . LEU   B 1 143 ? 11.021  -18.082 36.603  1.00 32.71 ? 147 LEU   B C    1 
ATOM   2762 O  O    . LEU   B 1 143 ? 11.355  -18.959 37.396  1.00 31.20 ? 147 LEU   B O    1 
ATOM   2763 C  CB   . LEU   B 1 143 ? 12.722  -18.877 34.933  1.00 31.53 ? 147 LEU   B CB   1 
ATOM   2764 C  CG   . LEU   B 1 143 ? 13.074  -19.347 33.520  1.00 31.22 ? 147 LEU   B CG   1 
ATOM   2765 C  CD1  . LEU   B 1 143 ? 14.464  -19.935 33.527  1.00 31.62 ? 147 LEU   B CD1  1 
ATOM   2766 C  CD2  . LEU   B 1 143 ? 12.076  -20.360 33.006  1.00 32.87 ? 147 LEU   B CD2  1 
ATOM   2767 N  N    . ASP   B 1 144 ? 10.334  -17.004 36.987  1.00 33.55 ? 148 ASP   B N    1 
ATOM   2768 C  CA   . ASP   B 1 144 ? 10.054  -16.758 38.395  1.00 36.83 ? 148 ASP   B CA   1 
ATOM   2769 C  C    . ASP   B 1 144 ? 9.243   -17.910 38.998  1.00 35.89 ? 148 ASP   B C    1 
ATOM   2770 O  O    . ASP   B 1 144 ? 9.369   -18.196 40.187  1.00 39.77 ? 148 ASP   B O    1 
ATOM   2771 C  CB   . ASP   B 1 144 ? 9.399   -15.401 38.612  1.00 39.90 ? 148 ASP   B CB   1 
ATOM   2772 C  CG   . ASP   B 1 144 ? 10.346  -14.208 38.664  1.00 42.65 ? 148 ASP   B CG   1 
ATOM   2773 O  OD1  . ASP   B 1 144 ? 11.581  -14.421 38.607  1.00 43.51 ? 148 ASP   B OD1  1 
ATOM   2774 O  OD2  . ASP   B 1 144 ? 9.838   -13.070 38.774  1.00 46.63 ? 148 ASP   B OD2  1 
ATOM   2775 N  N    . GLY   B 1 145 ? 8.417   -18.572 38.185  1.00 33.37 ? 149 GLY   B N    1 
ATOM   2776 C  CA   . GLY   B 1 145 ? 7.592   -19.672 38.659  1.00 30.44 ? 149 GLY   B CA   1 
ATOM   2777 C  C    . GLY   B 1 145 ? 8.332   -21.012 38.729  1.00 28.01 ? 149 GLY   B C    1 
ATOM   2778 O  O    . GLY   B 1 145 ? 7.787   -21.978 39.260  1.00 27.99 ? 149 GLY   B O    1 
ATOM   2779 N  N    . ALA   B 1 146 ? 9.554   -21.081 38.184  1.00 25.43 ? 150 ALA   B N    1 
ATOM   2780 C  CA   . ALA   B 1 146 ? 10.352  -22.300 38.231  1.00 22.37 ? 150 ALA   B CA   1 
ATOM   2781 C  C    . ALA   B 1 146 ? 11.040  -22.411 39.585  1.00 19.64 ? 150 ALA   B C    1 
ATOM   2782 O  O    . ALA   B 1 146 ? 11.188  -21.427 40.311  1.00 20.79 ? 150 ALA   B O    1 
ATOM   2783 C  CB   . ALA   B 1 146 ? 11.383  -22.310 37.128  1.00 22.63 ? 150 ALA   B CB   1 
ATOM   2784 N  N    . PHE   B 1 147 ? 11.509  -23.620 39.879  1.00 16.64 ? 151 PHE   B N    1 
ATOM   2785 C  CA   . PHE   B 1 147 ? 12.335  -23.890 41.037  1.00 15.91 ? 151 PHE   B CA   1 
ATOM   2786 C  C    . PHE   B 1 147 ? 13.676  -24.433 40.568  1.00 15.02 ? 151 PHE   B C    1 
ATOM   2787 O  O    . PHE   B 1 147 ? 13.838  -24.800 39.401  1.00 14.73 ? 151 PHE   B O    1 
ATOM   2788 C  CB   . PHE   B 1 147 ? 11.630  -24.887 41.960  1.00 16.66 ? 151 PHE   B CB   1 
ATOM   2789 C  CG   . PHE   B 1 147 ? 10.326  -24.318 42.484  1.00 17.38 ? 151 PHE   B CG   1 
ATOM   2790 C  CD1  . PHE   B 1 147 ? 9.150   -24.448 41.752  1.00 17.99 ? 151 PHE   B CD1  1 
ATOM   2791 C  CD2  . PHE   B 1 147 ? 10.295  -23.592 43.668  1.00 18.98 ? 151 PHE   B CD2  1 
ATOM   2792 C  CE1  . PHE   B 1 147 ? 7.968   -23.896 42.214  1.00 19.01 ? 151 PHE   B CE1  1 
ATOM   2793 C  CE2  . PHE   B 1 147 ? 9.110   -23.024 44.114  1.00 20.26 ? 151 PHE   B CE2  1 
ATOM   2794 C  CZ   . PHE   B 1 147 ? 7.950   -23.189 43.394  1.00 20.02 ? 151 PHE   B CZ   1 
ATOM   2795 N  N    . CYS   B 1 148 ? 14.626  -24.497 41.499  1.00 15.41 ? 152 CYS   B N    1 
ATOM   2796 C  CA   . CYS   B 1 148 ? 15.911  -25.095 41.195  1.00 15.44 ? 152 CYS   B CA   1 
ATOM   2797 C  C    . CYS   B 1 148 ? 16.508  -25.731 42.439  1.00 15.02 ? 152 CYS   B C    1 
ATOM   2798 O  O    . CYS   B 1 148 ? 16.175  -25.357 43.569  1.00 16.17 ? 152 CYS   B O    1 
ATOM   2799 C  CB   . CYS   B 1 148 ? 16.871  -24.091 40.574  1.00 16.02 ? 152 CYS   B CB   1 
ATOM   2800 S  SG   . CYS   B 1 148 ? 17.323  -22.725 41.668  1.00 19.01 ? 152 CYS   B SG   1 
ATOM   2801 N  N    A VAL   B 1 149 ? 17.364  -26.724 42.203  0.50 14.91 ? 153 VAL   B N    1 
ATOM   2802 N  N    B VAL   B 1 149 ? 17.399  -26.700 42.185  0.50 14.73 ? 153 VAL   B N    1 
ATOM   2803 C  CA   A VAL   B 1 149 ? 18.179  -27.310 43.245  0.50 15.10 ? 153 VAL   B CA   1 
ATOM   2804 C  CA   B VAL   B 1 149 ? 18.139  -27.434 43.196  0.50 14.79 ? 153 VAL   B CA   1 
ATOM   2805 C  C    A VAL   B 1 149 ? 19.549  -27.593 42.650  0.50 14.53 ? 153 VAL   B C    1 
ATOM   2806 C  C    B VAL   B 1 149 ? 19.545  -27.696 42.666  0.50 14.43 ? 153 VAL   B C    1 
ATOM   2807 O  O    A VAL   B 1 149 ? 19.677  -27.952 41.480  0.50 13.86 ? 153 VAL   B O    1 
ATOM   2808 O  O    B VAL   B 1 149 ? 19.700  -28.167 41.540  0.50 13.76 ? 153 VAL   B O    1 
ATOM   2809 C  CB   A VAL   B 1 149 ? 17.610  -28.609 43.834  0.50 16.36 ? 153 VAL   B CB   1 
ATOM   2810 C  CB   B VAL   B 1 149 ? 17.488  -28.781 43.560  0.50 15.70 ? 153 VAL   B CB   1 
ATOM   2811 C  CG1  A VAL   B 1 149 ? 16.327  -28.377 44.621  0.50 16.94 ? 153 VAL   B CG1  1 
ATOM   2812 C  CG1  B VAL   B 1 149 ? 18.479  -29.693 44.284  0.50 15.96 ? 153 VAL   B CG1  1 
ATOM   2813 C  CG2  A VAL   B 1 149 ? 17.441  -29.654 42.747  0.50 16.39 ? 153 VAL   B CG2  1 
ATOM   2814 C  CG2  B VAL   B 1 149 ? 16.223  -28.596 44.387  0.50 16.57 ? 153 VAL   B CG2  1 
ATOM   2815 N  N    . ASP   B 1 150 ? 20.553  -27.431 43.502  1.00 14.72 ? 154 ASP   B N    1 
ATOM   2816 C  CA   . ASP   B 1 150 ? 21.924  -27.792 43.197  1.00 15.53 ? 154 ASP   B CA   1 
ATOM   2817 C  C    . ASP   B 1 150 ? 22.165  -29.232 43.644  1.00 15.71 ? 154 ASP   B C    1 
ATOM   2818 O  O    . ASP   B 1 150 ? 22.047  -29.541 44.830  1.00 17.12 ? 154 ASP   B O    1 
ATOM   2819 C  CB   . ASP   B 1 150 ? 22.866  -26.835 43.902  1.00 16.85 ? 154 ASP   B CB   1 
ATOM   2820 C  CG   . ASP   B 1 150 ? 24.317  -26.943 43.471  1.00 17.55 ? 154 ASP   B CG   1 
ATOM   2821 O  OD1  . ASP   B 1 150 ? 24.751  -28.079 43.167  1.00 17.92 ? 154 ASP   B OD1  1 
ATOM   2822 O  OD2  . ASP   B 1 150 ? 24.995  -25.889 43.454  1.00 18.59 ? 154 ASP   B OD2  1 
ATOM   2823 N  N    . SER   B 1 151 ? 22.481  -30.122 42.698  1.00 15.56 ? 155 SER   B N    1 
ATOM   2824 C  CA   . SER   B 1 151 ? 22.633  -31.536 43.007  1.00 16.78 ? 155 SER   B CA   1 
ATOM   2825 C  C    . SER   B 1 151 ? 23.847  -31.835 43.892  1.00 18.93 ? 155 SER   B C    1 
ATOM   2826 O  O    . SER   B 1 151 ? 23.878  -32.870 44.555  1.00 20.32 ? 155 SER   B O    1 
ATOM   2827 C  CB   . SER   B 1 151 ? 22.660  -32.380 41.753  1.00 16.50 ? 155 SER   B CB   1 
ATOM   2828 O  OG   . SER   B 1 151 ? 23.674  -31.952 40.856  1.00 16.42 ? 155 SER   B OG   1 
ATOM   2829 N  N    A ILE   B 1 152 ? 24.846  -30.952 43.912  0.50 19.63 ? 156 ILE   B N    1 
ATOM   2830 N  N    B ILE   B 1 152 ? 24.871  -30.970 43.907  0.50 20.20 ? 156 ILE   B N    1 
ATOM   2831 C  CA   A ILE   B 1 152 ? 26.010  -31.226 44.738  0.50 21.29 ? 156 ILE   B CA   1 
ATOM   2832 C  CA   B ILE   B 1 152 ? 26.018  -31.234 44.770  0.50 22.36 ? 156 ILE   B CA   1 
ATOM   2833 C  C    A ILE   B 1 152 ? 25.581  -31.123 46.204  0.50 22.80 ? 156 ILE   B C    1 
ATOM   2834 C  C    B ILE   B 1 152 ? 25.561  -31.142 46.221  0.50 23.55 ? 156 ILE   B C    1 
ATOM   2835 O  O    A ILE   B 1 152 ? 25.976  -31.954 47.020  0.50 24.42 ? 156 ILE   B O    1 
ATOM   2836 O  O    B ILE   B 1 152 ? 25.957  -31.961 47.049  0.50 25.20 ? 156 ILE   B O    1 
ATOM   2837 C  CB   A ILE   B 1 152 ? 27.206  -30.338 44.333  0.50 21.10 ? 156 ILE   B CB   1 
ATOM   2838 C  CB   B ILE   B 1 152 ? 27.216  -30.313 44.469  0.50 23.31 ? 156 ILE   B CB   1 
ATOM   2839 C  CG1  A ILE   B 1 152 ? 28.536  -31.009 44.669  0.50 22.06 ? 156 ILE   B CG1  1 
ATOM   2840 C  CG1  B ILE   B 1 152 ? 27.799  -30.644 43.124  0.50 24.46 ? 156 ILE   B CG1  1 
ATOM   2841 C  CG2  A ILE   B 1 152 ? 27.111  -28.927 44.916  0.50 20.68 ? 156 ILE   B CG2  1 
ATOM   2842 C  CG2  B ILE   B 1 152 ? 28.285  -30.408 45.563  0.50 24.09 ? 156 ILE   B CG2  1 
ATOM   2843 C  CD1  A ILE   B 1 152 ? 29.739  -30.348 44.020  0.50 22.49 ? 156 ILE   B CD1  1 
ATOM   2844 C  CD1  B ILE   B 1 152 ? 28.845  -29.668 42.638  0.50 25.38 ? 156 ILE   B CD1  1 
ATOM   2845 N  N    . THR   B 1 153 ? 24.693  -30.164 46.503  1.00 22.90 ? 157 THR   B N    1 
ATOM   2846 C  CA   . THR   B 1 153 ? 24.133  -29.988 47.832  1.00 24.34 ? 157 THR   B CA   1 
ATOM   2847 C  C    . THR   B 1 153 ? 23.315  -31.224 48.195  1.00 25.22 ? 157 THR   B C    1 
ATOM   2848 O  O    . THR   B 1 153 ? 23.431  -31.737 49.305  1.00 26.89 ? 157 THR   B O    1 
ATOM   2849 C  CB   . THR   B 1 153 ? 23.290  -28.712 47.881  1.00 24.98 ? 157 THR   B CB   1 
ATOM   2850 O  OG1  . THR   B 1 153 ? 24.069  -27.627 47.371  1.00 25.94 ? 157 THR   B OG1  1 
ATOM   2851 C  CG2  . THR   B 1 153 ? 22.833  -28.383 49.292  1.00 26.50 ? 157 THR   B CG2  1 
ATOM   2852 N  N    . ALA   B 1 154 ? 22.495  -31.694 47.248  1.00 24.56 ? 158 ALA   B N    1 
ATOM   2853 C  CA   . ALA   B 1 154 ? 21.606  -32.828 47.466  1.00 25.08 ? 158 ALA   B CA   1 
ATOM   2854 C  C    . ALA   B 1 154 ? 22.413  -34.091 47.748  1.00 26.91 ? 158 ALA   B C    1 
ATOM   2855 O  O    . ALA   B 1 154 ? 22.137  -34.798 48.712  1.00 28.92 ? 158 ALA   B O    1 
ATOM   2856 C  CB   . ALA   B 1 154 ? 20.703  -33.020 46.266  1.00 25.10 ? 158 ALA   B CB   1 
ATOM   2857 N  N    . LEU   B 1 155 ? 23.416  -34.364 46.911  1.00 27.32 ? 159 LEU   B N    1 
ATOM   2858 C  CA   . LEU   B 1 155 ? 24.124  -35.633 46.968  1.00 28.58 ? 159 LEU   B CA   1 
ATOM   2859 C  C    . LEU   B 1 155 ? 25.016  -35.689 48.207  1.00 31.64 ? 159 LEU   B C    1 
ATOM   2860 O  O    . LEU   B 1 155 ? 25.145  -36.746 48.825  1.00 32.36 ? 159 LEU   B O    1 
ATOM   2861 C  CB   . LEU   B 1 155 ? 24.884  -35.824 45.657  1.00 29.15 ? 159 LEU   B CB   1 
ATOM   2862 C  CG   . LEU   B 1 155 ? 23.986  -35.977 44.424  1.00 30.30 ? 159 LEU   B CG   1 
ATOM   2863 C  CD1  . LEU   B 1 155 ? 24.744  -35.739 43.130  1.00 30.16 ? 159 LEU   B CD1  1 
ATOM   2864 C  CD2  . LEU   B 1 155 ? 23.325  -37.345 44.420  1.00 30.82 ? 159 LEU   B CD2  1 
ATOM   2865 N  N    . LYS   B 1 156 ? 25.600  -34.543 48.583  1.00 33.30 ? 160 LYS   B N    1 
ATOM   2866 C  CA   . LYS   B 1 156 ? 26.380  -34.451 49.810  1.00 35.48 ? 160 LYS   B CA   1 
ATOM   2867 C  C    . LYS   B 1 156 ? 25.483  -34.768 51.005  1.00 37.99 ? 160 LYS   B C    1 
ATOM   2868 O  O    . LYS   B 1 156 ? 25.861  -35.547 51.878  1.00 40.03 ? 160 LYS   B O    1 
ATOM   2869 C  CB   . LYS   B 1 156 ? 27.018  -33.066 49.974  1.00 36.62 ? 160 LYS   B CB   1 
ATOM   2870 C  CG   . LYS   B 1 156 ? 28.249  -32.811 49.111  1.00 37.94 ? 160 LYS   B CG   1 
ATOM   2871 N  N    . ALA   B 1 157 ? 24.291  -34.159 51.034  1.00 38.72 ? 161 ALA   B N    1 
ATOM   2872 C  CA   . ALA   B 1 157 ? 23.376  -34.308 52.155  1.00 41.81 ? 161 ALA   B CA   1 
ATOM   2873 C  C    . ALA   B 1 157 ? 22.865  -35.746 52.245  1.00 43.23 ? 161 ALA   B C    1 
ATOM   2874 O  O    . ALA   B 1 157 ? 22.692  -36.276 53.340  1.00 44.90 ? 161 ALA   B O    1 
ATOM   2875 C  CB   . ALA   B 1 157 ? 22.233  -33.325 52.027  1.00 41.22 ? 161 ALA   B CB   1 
ATOM   2876 N  N    . LEU   B 1 158 ? 22.625  -36.369 51.086  1.00 43.14 ? 162 LEU   B N    1 
ATOM   2877 C  CA   . LEU   B 1 158 ? 22.124  -37.733 51.035  1.00 44.29 ? 162 LEU   B CA   1 
ATOM   2878 C  C    . LEU   B 1 158 ? 23.193  -38.703 51.535  1.00 46.95 ? 162 LEU   B C    1 
ATOM   2879 O  O    . LEU   B 1 158 ? 22.876  -39.637 52.271  1.00 46.59 ? 162 LEU   B O    1 
ATOM   2880 C  CB   . LEU   B 1 158 ? 21.662  -38.071 49.620  1.00 44.00 ? 162 LEU   B CB   1 
ATOM   2881 C  CG   . LEU   B 1 158 ? 20.338  -37.430 49.194  1.00 44.67 ? 162 LEU   B CG   1 
ATOM   2882 C  CD1  . LEU   B 1 158 ? 20.159  -37.493 47.692  1.00 45.41 ? 162 LEU   B CD1  1 
ATOM   2883 C  CD2  . LEU   B 1 158 ? 19.164  -38.085 49.896  1.00 45.19 ? 162 LEU   B CD2  1 
ATOM   2884 N  N    . GLU   B 1 159 ? 24.452  -38.473 51.137  1.00 47.71 ? 163 GLU   B N    1 
ATOM   2885 C  CA   . GLU   B 1 159 ? 25.555  -39.301 51.599  1.00 50.80 ? 163 GLU   B CA   1 
ATOM   2886 C  C    . GLU   B 1 159 ? 25.671  -39.185 53.119  1.00 54.66 ? 163 GLU   B C    1 
ATOM   2887 O  O    . GLU   B 1 159 ? 25.901  -40.183 53.798  1.00 54.78 ? 163 GLU   B O    1 
ATOM   2888 C  CB   . GLU   B 1 159 ? 26.855  -38.931 50.884  1.00 51.17 ? 163 GLU   B CB   1 
ATOM   2889 N  N    . ARG   B 1 160 ? 25.478  -37.965 53.644  1.00 58.13 ? 164 ARG   B N    1 
ATOM   2890 C  CA   . ARG   B 1 160 ? 25.564  -37.702 55.075  1.00 60.43 ? 164 ARG   B CA   1 
ATOM   2891 C  C    . ARG   B 1 160 ? 24.563  -38.571 55.837  1.00 61.42 ? 164 ARG   B C    1 
ATOM   2892 O  O    . ARG   B 1 160 ? 24.878  -39.082 56.912  1.00 61.73 ? 164 ARG   B O    1 
ATOM   2893 C  CB   . ARG   B 1 160 ? 25.332  -36.210 55.347  1.00 61.37 ? 164 ARG   B CB   1 
ATOM   2894 N  N    . ALA   B 1 161 ? 23.360  -38.737 55.270  1.00 63.59 ? 165 ALA   B N    1 
ATOM   2895 C  CA   . ALA   B 1 161 ? 22.313  -39.547 55.875  1.00 66.73 ? 165 ALA   B CA   1 
ATOM   2896 C  C    . ALA   B 1 161 ? 22.267  -40.929 55.214  1.00 65.67 ? 165 ALA   B C    1 
ATOM   2897 O  O    . ALA   B 1 161 ? 23.278  -41.661 55.300  1.00 64.80 ? 165 ALA   B O    1 
ATOM   2898 C  CB   . ALA   B 1 161 ? 20.984  -38.832 55.749  1.00 67.80 ? 165 ALA   B CB   1 
ATOM   2899 N  N    . LYS   B 1 171 ? 37.995  -35.733 49.256  1.00 51.31 ? 175 LYS   B N    1 
ATOM   2900 C  CA   . LYS   B 1 171 ? 36.620  -36.266 49.065  1.00 48.58 ? 175 LYS   B CA   1 
ATOM   2901 C  C    . LYS   B 1 171 ? 35.912  -35.389 48.033  1.00 45.55 ? 175 LYS   B C    1 
ATOM   2902 O  O    . LYS   B 1 171 ? 35.184  -34.466 48.396  1.00 49.94 ? 175 LYS   B O    1 
ATOM   2903 C  CB   . LYS   B 1 171 ? 35.874  -36.304 50.406  1.00 51.61 ? 175 LYS   B CB   1 
ATOM   2904 C  CG   . LYS   B 1 171 ? 34.873  -37.439 50.582  1.00 53.13 ? 175 LYS   B CG   1 
ATOM   2905 C  CD   . LYS   B 1 171 ? 33.901  -37.638 49.426  1.00 53.41 ? 175 LYS   B CD   1 
ATOM   2906 C  CE   . LYS   B 1 171 ? 32.829  -38.634 49.744  1.00 54.73 ? 175 LYS   B CE   1 
ATOM   2907 N  NZ   . LYS   B 1 171 ? 33.349  -39.998 49.855  1.00 56.27 ? 175 LYS   B NZ   1 
ATOM   2908 N  N    . SER   B 1 172 ? 36.159  -35.671 46.748  1.00 38.76 ? 176 SER   B N    1 
ATOM   2909 C  CA   . SER   B 1 172 ? 35.633  -34.861 45.659  1.00 34.59 ? 176 SER   B CA   1 
ATOM   2910 C  C    . SER   B 1 172 ? 34.146  -35.145 45.450  1.00 31.95 ? 176 SER   B C    1 
ATOM   2911 O  O    . SER   B 1 172 ? 33.721  -36.298 45.492  1.00 32.50 ? 176 SER   B O    1 
ATOM   2912 C  CB   . SER   B 1 172 ? 36.399  -35.108 44.386  1.00 34.34 ? 176 SER   B CB   1 
ATOM   2913 O  OG   . SER   B 1 172 ? 35.859  -34.357 43.308  1.00 34.97 ? 176 SER   B OG   1 
ATOM   2914 N  N    . TYR   B 1 173 ? 33.370  -34.079 45.208  1.00 30.37 ? 177 TYR   B N    1 
ATOM   2915 C  CA   . TYR   B 1 173 ? 31.977  -34.216 44.812  1.00 29.95 ? 177 TYR   B CA   1 
ATOM   2916 C  C    . TYR   B 1 173 ? 31.797  -33.733 43.376  1.00 27.44 ? 177 TYR   B C    1 
ATOM   2917 O  O    . TYR   B 1 173 ? 30.692  -33.375 42.971  1.00 26.62 ? 177 TYR   B O    1 
ATOM   2918 C  CB   . TYR   B 1 173 ? 31.079  -33.496 45.824  1.00 33.23 ? 177 TYR   B CB   1 
ATOM   2919 C  CG   . TYR   B 1 173 ? 30.958  -34.283 47.119  1.00 36.65 ? 177 TYR   B CG   1 
ATOM   2920 C  CD1  . TYR   B 1 173 ? 30.110  -35.382 47.206  1.00 38.68 ? 177 TYR   B CD1  1 
ATOM   2921 C  CD2  . TYR   B 1 173 ? 31.724  -33.960 48.235  1.00 39.24 ? 177 TYR   B CD2  1 
ATOM   2922 C  CE1  . TYR   B 1 173 ? 30.011  -36.124 48.373  1.00 41.25 ? 177 TYR   B CE1  1 
ATOM   2923 C  CE2  . TYR   B 1 173 ? 31.631  -34.693 49.408  1.00 40.96 ? 177 TYR   B CE2  1 
ATOM   2924 C  CZ   . TYR   B 1 173 ? 30.772  -35.777 49.476  1.00 41.99 ? 177 TYR   B CZ   1 
ATOM   2925 O  OH   . TYR   B 1 173 ? 30.677  -36.502 50.628  1.00 46.11 ? 177 TYR   B OH   1 
ATOM   2926 N  N    . SER   B 1 174 ? 32.881  -33.760 42.590  1.00 26.24 ? 178 SER   B N    1 
ATOM   2927 C  CA   . SER   B 1 174 ? 32.762  -33.535 41.160  1.00 25.24 ? 178 SER   B CA   1 
ATOM   2928 C  C    . SER   B 1 174 ? 31.855  -34.606 40.560  1.00 24.44 ? 178 SER   B C    1 
ATOM   2929 O  O    . SER   B 1 174 ? 31.731  -35.722 41.073  1.00 24.34 ? 178 SER   B O    1 
ATOM   2930 C  CB   . SER   B 1 174 ? 34.101  -33.534 40.475  1.00 26.51 ? 178 SER   B CB   1 
ATOM   2931 O  OG   . SER   B 1 174 ? 34.624  -34.852 40.405  1.00 27.49 ? 178 SER   B OG   1 
ATOM   2932 N  N    . LEU   B 1 175 ? 31.243  -34.258 39.433  1.00 23.27 ? 179 LEU   B N    1 
ATOM   2933 C  CA   . LEU   B 1 175 ? 30.337  -35.168 38.767  1.00 23.33 ? 179 LEU   B CA   1 
ATOM   2934 C  C    . LEU   B 1 175 ? 31.038  -36.502 38.501  1.00 23.53 ? 179 LEU   B C    1 
ATOM   2935 O  O    . LEU   B 1 175 ? 30.491  -37.566 38.793  1.00 23.68 ? 179 LEU   B O    1 
ATOM   2936 C  CB   . LEU   B 1 175 ? 29.870  -34.484 37.486  1.00 23.39 ? 179 LEU   B CB   1 
ATOM   2937 C  CG   . LEU   B 1 175 ? 28.714  -35.161 36.758  1.00 23.49 ? 179 LEU   B CG   1 
ATOM   2938 C  CD1  . LEU   B 1 175 ? 27.436  -35.058 37.575  1.00 23.46 ? 179 LEU   B CD1  1 
ATOM   2939 C  CD2  . LEU   B 1 175 ? 28.547  -34.540 35.384  1.00 23.03 ? 179 LEU   B CD2  1 
ATOM   2940 N  N    . GLY   B 1 176 ? 32.260  -36.441 37.959  1.00 24.56 ? 180 GLY   B N    1 
ATOM   2941 C  CA   . GLY   B 1 176 ? 32.980  -37.649 37.590  1.00 25.34 ? 180 GLY   B CA   1 
ATOM   2942 C  C    . GLY   B 1 176 ? 33.381  -38.485 38.805  1.00 26.28 ? 180 GLY   B C    1 
ATOM   2943 O  O    . GLY   B 1 176 ? 33.354  -39.712 38.746  1.00 27.24 ? 180 GLY   B O    1 
ATOM   2944 N  N    . SER   B 1 177 ? 33.757  -37.816 39.900  1.00 26.60 ? 181 SER   B N    1 
ATOM   2945 C  CA   . SER   B 1 177 ? 34.153  -38.493 41.124  1.00 28.05 ? 181 SER   B CA   1 
ATOM   2946 C  C    . SER   B 1 177 ? 32.991  -39.305 41.691  1.00 27.34 ? 181 SER   B C    1 
ATOM   2947 O  O    . SER   B 1 177 ? 33.161  -40.462 42.064  1.00 27.54 ? 181 SER   B O    1 
ATOM   2948 C  CB   . SER   B 1 177 ? 34.664  -37.511 42.153  1.00 29.90 ? 181 SER   B CB   1 
ATOM   2949 O  OG   . SER   B 1 177 ? 35.917  -36.968 41.760  1.00 33.04 ? 181 SER   B OG   1 
ATOM   2950 N  N    . ILE   B 1 178 ? 31.811  -38.680 41.751  1.00 25.70 ? 182 ILE   B N    1 
ATOM   2951 C  CA   . ILE   B 1 178 ? 30.626  -39.332 42.283  1.00 25.18 ? 182 ILE   B CA   1 
ATOM   2952 C  C    . ILE   B 1 178 ? 30.262  -40.509 41.381  1.00 25.83 ? 182 ILE   B C    1 
ATOM   2953 O  O    . ILE   B 1 178 ? 30.010  -41.609 41.863  1.00 26.38 ? 182 ILE   B O    1 
ATOM   2954 C  CB   . ILE   B 1 178 ? 29.461  -38.339 42.421  1.00 24.83 ? 182 ILE   B CB   1 
ATOM   2955 C  CG1  . ILE   B 1 178 ? 29.791  -37.201 43.386  1.00 25.68 ? 182 ILE   B CG1  1 
ATOM   2956 C  CG2  . ILE   B 1 178 ? 28.180  -39.067 42.833  1.00 24.28 ? 182 ILE   B CG2  1 
ATOM   2957 C  CD1  . ILE   B 1 178 ? 28.791  -36.057 43.348  1.00 26.34 ? 182 ILE   B CD1  1 
ATOM   2958 N  N    . TYR   B 1 179 ? 30.246  -40.271 40.066  1.00 25.08 ? 183 TYR   B N    1 
ATOM   2959 C  CA   . TYR   B 1 179 ? 29.850  -41.298 39.120  1.00 26.06 ? 183 TYR   B CA   1 
ATOM   2960 C  C    . TYR   B 1 179 ? 30.753  -42.520 39.276  1.00 28.75 ? 183 TYR   B C    1 
ATOM   2961 O  O    . TYR   B 1 179 ? 30.267  -43.646 39.307  1.00 29.89 ? 183 TYR   B O    1 
ATOM   2962 C  CB   . TYR   B 1 179 ? 29.889  -40.729 37.699  1.00 25.41 ? 183 TYR   B CB   1 
ATOM   2963 C  CG   . TYR   B 1 179 ? 29.249  -41.615 36.641  1.00 25.41 ? 183 TYR   B CG   1 
ATOM   2964 C  CD1  . TYR   B 1 179 ? 29.944  -42.686 36.096  1.00 26.17 ? 183 TYR   B CD1  1 
ATOM   2965 C  CD2  . TYR   B 1 179 ? 27.966  -41.369 36.170  1.00 24.40 ? 183 TYR   B CD2  1 
ATOM   2966 C  CE1  . TYR   B 1 179 ? 29.380  -43.493 35.124  1.00 25.85 ? 183 TYR   B CE1  1 
ATOM   2967 C  CE2  . TYR   B 1 179 ? 27.390  -42.171 35.197  1.00 24.13 ? 183 TYR   B CE2  1 
ATOM   2968 C  CZ   . TYR   B 1 179 ? 28.100  -43.236 34.672  1.00 24.93 ? 183 TYR   B CZ   1 
ATOM   2969 O  OH   . TYR   B 1 179 ? 27.560  -44.030 33.703  1.00 25.72 ? 183 TYR   B OH   1 
ATOM   2970 N  N    . THR   B 1 180 ? 32.067  -42.290 39.384  1.00 31.45 ? 184 THR   B N    1 
ATOM   2971 C  CA   . THR   B 1 180 ? 33.032  -43.378 39.448  1.00 33.85 ? 184 THR   B CA   1 
ATOM   2972 C  C    . THR   B 1 180 ? 32.829  -44.185 40.731  1.00 34.87 ? 184 THR   B C    1 
ATOM   2973 O  O    . THR   B 1 180 ? 32.955  -45.406 40.720  1.00 36.51 ? 184 THR   B O    1 
ATOM   2974 C  CB   . THR   B 1 180 ? 34.452  -42.815 39.348  1.00 35.50 ? 184 THR   B CB   1 
ATOM   2975 O  OG1  . THR   B 1 180 ? 34.551  -42.116 38.109  1.00 37.49 ? 184 THR   B OG1  1 
ATOM   2976 C  CG2  . THR   B 1 180 ? 35.509  -43.903 39.358  1.00 37.65 ? 184 THR   B CG2  1 
ATOM   2977 N  N    . ARG   B 1 181 ? 32.526  -43.488 41.833  1.00 33.99 ? 185 ARG   B N    1 
ATOM   2978 C  CA   . ARG   B 1 181 ? 32.294  -44.108 43.130  1.00 34.82 ? 185 ARG   B CA   1 
ATOM   2979 C  C    . ARG   B 1 181 ? 31.071  -45.025 43.063  1.00 34.84 ? 185 ARG   B C    1 
ATOM   2980 O  O    . ARG   B 1 181 ? 31.060  -46.098 43.659  1.00 35.66 ? 185 ARG   B O    1 
ATOM   2981 C  CB   . ARG   B 1 181 ? 32.109  -42.969 44.142  1.00 37.18 ? 185 ARG   B CB   1 
ATOM   2982 C  CG   . ARG   B 1 181 ? 32.596  -43.190 45.563  1.00 40.70 ? 185 ARG   B CG   1 
ATOM   2983 C  CD   . ARG   B 1 181 ? 33.223  -41.929 46.153  1.00 39.96 ? 185 ARG   B CD   1 
ATOM   2984 N  NE   . ARG   B 1 181 ? 32.334  -40.765 46.237  1.00 39.03 ? 185 ARG   B NE   1 
ATOM   2985 C  CZ   . ARG   B 1 181 ? 32.679  -39.498 45.996  1.00 39.36 ? 185 ARG   B CZ   1 
ATOM   2986 N  NH1  . ARG   B 1 181 ? 33.913  -39.185 45.634  1.00 39.12 ? 185 ARG   B NH1  1 
ATOM   2987 N  NH2  . ARG   B 1 181 ? 31.783  -38.533 46.125  1.00 39.67 ? 185 ARG   B NH2  1 
ATOM   2988 N  N    . LEU   B 1 182 ? 30.034  -44.600 42.334  1.00 34.74 ? 186 LEU   B N    1 
ATOM   2989 C  CA   . LEU   B 1 182 ? 28.788  -45.353 42.274  1.00 35.07 ? 186 LEU   B CA   1 
ATOM   2990 C  C    . LEU   B 1 182 ? 28.879  -46.476 41.241  1.00 35.27 ? 186 LEU   B C    1 
ATOM   2991 O  O    . LEU   B 1 182 ? 28.399  -47.573 41.499  1.00 38.39 ? 186 LEU   B O    1 
ATOM   2992 C  CB   . LEU   B 1 182 ? 27.605  -44.429 41.974  1.00 34.72 ? 186 LEU   B CB   1 
ATOM   2993 C  CG   . LEU   B 1 182 ? 27.259  -43.394 43.050  1.00 35.46 ? 186 LEU   B CG   1 
ATOM   2994 C  CD1  . LEU   B 1 182 ? 26.044  -42.569 42.640  1.00 35.64 ? 186 LEU   B CD1  1 
ATOM   2995 C  CD2  . LEU   B 1 182 ? 27.036  -44.055 44.399  1.00 37.42 ? 186 LEU   B CD2  1 
ATOM   2996 N  N    . TYR   B 1 183 ? 29.466  -46.204 40.068  1.00 35.43 ? 187 TYR   B N    1 
ATOM   2997 C  CA   . TYR   B 1 183 ? 29.333  -47.110 38.935  1.00 36.82 ? 187 TYR   B CA   1 
ATOM   2998 C  C    . TYR   B 1 183 ? 30.677  -47.700 38.511  1.00 41.86 ? 187 TYR   B C    1 
ATOM   2999 O  O    . TYR   B 1 183 ? 30.774  -48.293 37.435  1.00 43.50 ? 187 TYR   B O    1 
ATOM   3000 C  CB   . TYR   B 1 183 ? 28.610  -46.321 37.841  1.00 33.83 ? 187 TYR   B CB   1 
ATOM   3001 C  CG   . TYR   B 1 183 ? 27.190  -45.938 38.235  1.00 31.13 ? 187 TYR   B CG   1 
ATOM   3002 C  CD1  . TYR   B 1 183 ? 26.296  -46.888 38.728  1.00 30.69 ? 187 TYR   B CD1  1 
ATOM   3003 C  CD2  . TYR   B 1 183 ? 26.759  -44.622 38.165  1.00 29.12 ? 187 TYR   B CD2  1 
ATOM   3004 C  CE1  . TYR   B 1 183 ? 25.008  -46.542 39.103  1.00 29.21 ? 187 TYR   B CE1  1 
ATOM   3005 C  CE2  . TYR   B 1 183 ? 25.473  -44.263 38.535  1.00 27.64 ? 187 TYR   B CE2  1 
ATOM   3006 C  CZ   . TYR   B 1 183 ? 24.592  -45.225 38.999  1.00 28.19 ? 187 TYR   B CZ   1 
ATOM   3007 O  OH   . TYR   B 1 183 ? 23.325  -44.874 39.365  1.00 26.31 ? 187 TYR   B OH   1 
ATOM   3008 N  N    . GLY   B 1 184 ? 31.700  -47.547 39.361  1.00 45.09 ? 188 GLY   B N    1 
ATOM   3009 C  CA   . GLY   B 1 184 ? 32.953  -48.272 39.216  1.00 48.19 ? 188 GLY   B CA   1 
ATOM   3010 C  C    . GLY   B 1 184 ? 33.645  -48.013 37.879  1.00 50.61 ? 188 GLY   B C    1 
ATOM   3011 O  O    . GLY   B 1 184 ? 34.493  -48.798 37.458  1.00 53.77 ? 188 GLY   B O    1 
ATOM   3012 N  N    . GLN   B 1 185 ? 33.305  -46.893 37.237  1.00 50.92 ? 189 GLN   B N    1 
ATOM   3013 C  CA   . GLN   B 1 185 ? 33.844  -46.552 35.933  1.00 52.93 ? 189 GLN   B CA   1 
ATOM   3014 C  C    . GLN   B 1 185 ? 33.514  -45.092 35.646  1.00 53.08 ? 189 GLN   B C    1 
ATOM   3015 O  O    . GLN   B 1 185 ? 32.569  -44.549 36.211  1.00 52.73 ? 189 GLN   B O    1 
ATOM   3016 C  CB   . GLN   B 1 185 ? 33.274  -47.472 34.852  1.00 54.84 ? 189 GLN   B CB   1 
ATOM   3017 N  N    . SER   B 1 186 ? 34.313  -44.468 34.777  1.00 55.61 ? 190 SER   B N    1 
ATOM   3018 C  CA   . SER   B 1 186 ? 34.099  -43.090 34.367  1.00 56.80 ? 190 SER   B CA   1 
ATOM   3019 C  C    . SER   B 1 186 ? 32.783  -42.974 33.596  1.00 56.16 ? 190 SER   B C    1 
ATOM   3020 O  O    . SER   B 1 186 ? 32.357  -43.935 32.954  1.00 57.25 ? 190 SER   B O    1 
ATOM   3021 C  CB   . SER   B 1 186 ? 35.268  -42.605 33.543  1.00 58.70 ? 190 SER   B CB   1 
ATOM   3022 O  OG   . SER   B 1 186 ? 35.018  -41.321 32.989  1.00 62.20 ? 190 SER   B OG   1 
ATOM   3023 N  N    . PRO   B 1 187 ? 32.084  -41.814 33.641  1.00 53.74 ? 191 PRO   B N    1 
ATOM   3024 C  CA   . PRO   B 1 187 ? 30.918  -41.598 32.782  1.00 53.31 ? 191 PRO   B CA   1 
ATOM   3025 C  C    . PRO   B 1 187 ? 31.307  -41.643 31.305  1.00 54.22 ? 191 PRO   B C    1 
ATOM   3026 O  O    . PRO   B 1 187 ? 32.422  -41.268 30.948  1.00 57.27 ? 191 PRO   B O    1 
ATOM   3027 C  CB   . PRO   B 1 187 ? 30.366  -40.224 33.214  1.00 52.71 ? 191 PRO   B CB   1 
ATOM   3028 C  CG   . PRO   B 1 187 ? 31.522  -39.550 33.926  1.00 52.32 ? 191 PRO   B CG   1 
ATOM   3029 C  CD   . PRO   B 1 187 ? 32.346  -40.673 34.536  1.00 52.99 ? 191 PRO   B CD   1 
ATOM   3030 N  N    . PRO   B 1 188 ? 30.405  -42.096 30.402  1.00 54.15 ? 192 PRO   B N    1 
ATOM   3031 C  CA   . PRO   B 1 188 ? 30.729  -42.218 28.979  1.00 55.28 ? 192 PRO   B CA   1 
ATOM   3032 C  C    . PRO   B 1 188 ? 31.364  -40.952 28.408  1.00 57.81 ? 192 PRO   B C    1 
ATOM   3033 O  O    . PRO   B 1 188 ? 32.439  -41.001 27.812  1.00 58.56 ? 192 PRO   B O    1 
ATOM   3034 C  CB   . PRO   B 1 188 ? 29.367  -42.518 28.322  1.00 54.81 ? 192 PRO   B CB   1 
ATOM   3035 C  CG   . PRO   B 1 188 ? 28.543  -43.141 29.423  1.00 54.14 ? 192 PRO   B CG   1 
ATOM   3036 C  CD   . PRO   B 1 188 ? 29.019  -42.488 30.705  1.00 53.64 ? 192 PRO   B CD   1 
ATOM   3037 N  N    . ASP   B 1 189 ? 30.679  -39.822 28.622  1.00 57.92 ? 193 ASP   B N    1 
ATOM   3038 C  CA   . ASP   B 1 189 ? 31.057  -38.540 28.051  1.00 57.49 ? 193 ASP   B CA   1 
ATOM   3039 C  C    . ASP   B 1 189 ? 31.172  -37.507 29.171  1.00 55.51 ? 193 ASP   B C    1 
ATOM   3040 O  O    . ASP   B 1 189 ? 30.294  -37.420 30.033  1.00 57.47 ? 193 ASP   B O    1 
ATOM   3041 C  CB   . ASP   B 1 189 ? 30.056  -38.119 26.986  1.00 57.43 ? 193 ASP   B CB   1 
ATOM   3042 C  CG   . ASP   B 1 189 ? 30.203  -36.699 26.463  1.00 58.29 ? 193 ASP   B CG   1 
ATOM   3043 O  OD1  . ASP   B 1 189 ? 31.253  -36.080 26.731  1.00 60.34 ? 193 ASP   B OD1  1 
ATOM   3044 O  OD2  . ASP   B 1 189 ? 29.254  -36.217 25.813  1.00 56.97 ? 193 ASP   B OD2  1 
ATOM   3045 N  N    . SER   B 1 190 ? 32.258  -36.719 29.125  1.00 50.44 ? 194 SER   B N    1 
ATOM   3046 C  CA   . SER   B 1 190 ? 32.536  -35.684 30.110  1.00 46.45 ? 194 SER   B CA   1 
ATOM   3047 C  C    . SER   B 1 190 ? 32.721  -34.318 29.440  1.00 42.72 ? 194 SER   B C    1 
ATOM   3048 O  O    . SER   B 1 190 ? 33.026  -33.333 30.119  1.00 46.60 ? 194 SER   B O    1 
ATOM   3049 C  CB   . SER   B 1 190 ? 33.749  -36.052 30.932  1.00 47.02 ? 194 SER   B CB   1 
ATOM   3050 N  N    . HIS   B 1 191 ? 32.492  -34.244 28.119  1.00 35.84 ? 195 HIS   B N    1 
ATOM   3051 C  CA   . HIS   B 1 191 ? 32.893  -33.078 27.350  1.00 30.03 ? 195 HIS   B CA   1 
ATOM   3052 C  C    . HIS   B 1 191 ? 31.709  -32.323 26.738  1.00 22.64 ? 195 HIS   B C    1 
ATOM   3053 O  O    . HIS   B 1 191 ? 31.947  -31.289 26.136  1.00 23.50 ? 195 HIS   B O    1 
ATOM   3054 C  CB   . HIS   B 1 191 ? 33.941  -33.456 26.292  1.00 34.16 ? 195 HIS   B CB   1 
ATOM   3055 C  CG   . HIS   B 1 191 ? 33.398  -34.106 25.047  1.00 38.57 ? 195 HIS   B CG   1 
ATOM   3056 N  ND1  . HIS   B 1 191 ? 32.838  -35.369 25.021  1.00 40.38 ? 195 HIS   B ND1  1 
ATOM   3057 C  CD2  . HIS   B 1 191 ? 33.320  -33.647 23.780  1.00 39.77 ? 195 HIS   B CD2  1 
ATOM   3058 C  CE1  . HIS   B 1 191 ? 32.448  -35.659 23.784  1.00 39.75 ? 195 HIS   B CE1  1 
ATOM   3059 N  NE2  . HIS   B 1 191 ? 32.734  -34.632 23.010  1.00 37.53 ? 195 HIS   B NE2  1 
ATOM   3060 N  N    . THR   B 1 192 ? 30.456  -32.792 26.884  1.00 18.69 ? 196 THR   B N    1 
ATOM   3061 C  CA   . THR   B 1 192 ? 29.306  -32.075 26.329  1.00 16.44 ? 196 THR   B CA   1 
ATOM   3062 C  C    . THR   B 1 192 ? 28.278  -31.772 27.420  1.00 14.58 ? 196 THR   B C    1 
ATOM   3063 O  O    . THR   B 1 192 ? 28.206  -32.459 28.434  1.00 15.36 ? 196 THR   B O    1 
ATOM   3064 C  CB   . THR   B 1 192 ? 28.638  -32.843 25.185  1.00 17.98 ? 196 THR   B CB   1 
ATOM   3065 O  OG1  . THR   B 1 192 ? 27.931  -33.963 25.713  1.00 18.44 ? 196 THR   B OG1  1 
ATOM   3066 C  CG2  . THR   B 1 192 ? 29.629  -33.315 24.134  1.00 19.10 ? 196 THR   B CG2  1 
ATOM   3067 N  N    . ALA   B 1 193 ? 27.420  -30.775 27.176  1.00 13.42 ? 197 ALA   B N    1 
ATOM   3068 C  CA   . ALA   B 1 193 ? 26.343  -30.479 28.111  1.00 13.00 ? 197 ALA   B CA   1 
ATOM   3069 C  C    . ALA   B 1 193 ? 25.425  -31.688 28.262  1.00 12.94 ? 197 ALA   B C    1 
ATOM   3070 O  O    . ALA   B 1 193 ? 25.004  -32.008 29.369  1.00 13.20 ? 197 ALA   B O    1 
ATOM   3071 C  CB   . ALA   B 1 193 ? 25.563  -29.252 27.701  1.00 12.85 ? 197 ALA   B CB   1 
ATOM   3072 N  N    . GLU   B 1 194 ? 25.104  -32.359 27.154  1.00 13.29 ? 198 GLU   B N    1 
ATOM   3073 C  CA   . GLU   B 1 194 ? 24.232  -33.520 27.217  1.00 13.71 ? 198 GLU   B CA   1 
ATOM   3074 C  C    . GLU   B 1 194 ? 24.900  -34.644 28.008  1.00 13.38 ? 198 GLU   B C    1 
ATOM   3075 O  O    . GLU   B 1 194 ? 24.243  -35.326 28.793  1.00 13.28 ? 198 GLU   B O    1 
ATOM   3076 C  CB   . GLU   B 1 194 ? 23.824  -33.972 25.816  1.00 14.92 ? 198 GLU   B CB   1 
ATOM   3077 C  CG   . GLU   B 1 194 ? 22.888  -35.179 25.831  1.00 17.28 ? 198 GLU   B CG   1 
ATOM   3078 C  CD   . GLU   B 1 194 ? 22.383  -35.589 24.460  1.00 20.07 ? 198 GLU   B CD   1 
ATOM   3079 O  OE1  . GLU   B 1 194 ? 22.382  -34.752 23.535  1.00 26.14 ? 198 GLU   B OE1  1 
ATOM   3080 O  OE2  . GLU   B 1 194 ? 21.957  -36.747 24.332  1.00 22.52 ? 198 GLU   B OE2  1 
ATOM   3081 N  N    . GLY   B 1 195 ? 26.207  -34.837 27.820  1.00 13.46 ? 199 GLY   B N    1 
ATOM   3082 C  CA   . GLY   B 1 195 ? 26.899  -35.880 28.556  1.00 13.87 ? 199 GLY   B CA   1 
ATOM   3083 C  C    . GLY   B 1 195 ? 26.846  -35.651 30.065  1.00 13.94 ? 199 GLY   B C    1 
ATOM   3084 O  O    . GLY   B 1 195 ? 26.666  -36.589 30.842  1.00 15.07 ? 199 GLY   B O    1 
ATOM   3085 N  N    . ASP   B 1 196 ? 27.002  -34.394 30.473  1.00 13.56 ? 200 ASP   B N    1 
ATOM   3086 C  CA   . ASP   B 1 196 ? 26.976  -34.033 31.881  1.00 14.32 ? 200 ASP   B CA   1 
ATOM   3087 C  C    . ASP   B 1 196 ? 25.570  -34.195 32.454  1.00 13.52 ? 200 ASP   B C    1 
ATOM   3088 O  O    . ASP   B 1 196 ? 25.421  -34.608 33.601  1.00 14.10 ? 200 ASP   B O    1 
ATOM   3089 C  CB   . ASP   B 1 196 ? 27.570  -32.652 32.118  1.00 16.41 ? 200 ASP   B CB   1 
ATOM   3090 C  CG   . ASP   B 1 196 ? 29.096  -32.621 32.115  1.00 20.23 ? 200 ASP   B CG   1 
ATOM   3091 O  OD1  . ASP   B 1 196 ? 29.715  -33.667 31.822  1.00 22.03 ? 200 ASP   B OD1  1 
ATOM   3092 O  OD2  . ASP   B 1 196 ? 29.667  -31.555 32.430  1.00 26.98 ? 200 ASP   B OD2  1 
ATOM   3093 N  N    . VAL   B 1 197 ? 24.542  -33.872 31.666  1.00 12.56 ? 201 VAL   B N    1 
ATOM   3094 C  CA   . VAL   B 1 197 ? 23.166  -34.100 32.087  1.00 12.69 ? 201 VAL   B CA   1 
ATOM   3095 C  C    . VAL   B 1 197 ? 22.892  -35.597 32.259  1.00 13.01 ? 201 VAL   B C    1 
ATOM   3096 O  O    . VAL   B 1 197 ? 22.269  -36.005 33.237  1.00 13.55 ? 201 VAL   B O    1 
ATOM   3097 C  CB   . VAL   B 1 197 ? 22.167  -33.464 31.100  1.00 13.42 ? 201 VAL   B CB   1 
ATOM   3098 C  CG1  . VAL   B 1 197 ? 20.774  -34.055 31.244  1.00 14.75 ? 201 VAL   B CG1  1 
ATOM   3099 C  CG2  . VAL   B 1 197 ? 22.143  -31.946 31.244  1.00 13.85 ? 201 VAL   B CG2  1 
ATOM   3100 N  N    . LEU   B 1 198 ? 23.324  -36.418 31.297  1.00 13.15 ? 202 LEU   B N    1 
ATOM   3101 C  CA   . LEU   B 1 198 ? 23.056  -37.847 31.367  1.00 13.88 ? 202 LEU   B CA   1 
ATOM   3102 C  C    . LEU   B 1 198 ? 23.804  -38.491 32.534  1.00 14.41 ? 202 LEU   B C    1 
ATOM   3103 O  O    . LEU   B 1 198 ? 23.271  -39.385 33.177  1.00 15.88 ? 202 LEU   B O    1 
ATOM   3104 C  CB   . LEU   B 1 198 ? 23.415  -38.523 30.052  1.00 15.01 ? 202 LEU   B CB   1 
ATOM   3105 C  CG   . LEU   B 1 198 ? 22.498  -38.176 28.882  1.00 16.17 ? 202 LEU   B CG   1 
ATOM   3106 C  CD1  . LEU   B 1 198 ? 23.085  -38.716 27.593  1.00 17.14 ? 202 LEU   B CD1  1 
ATOM   3107 C  CD2  . LEU   B 1 198 ? 21.084  -38.671 29.122  1.00 16.57 ? 202 LEU   B CD2  1 
ATOM   3108 N  N    . ALA   B 1 199 ? 25.031  -38.047 32.815  1.00 14.18 ? 203 ALA   B N    1 
ATOM   3109 C  CA   . ALA   B 1 199 ? 25.770  -38.568 33.959  1.00 14.66 ? 203 ALA   B CA   1 
ATOM   3110 C  C    . ALA   B 1 199 ? 25.075  -38.195 35.267  1.00 14.39 ? 203 ALA   B C    1 
ATOM   3111 O  O    . ALA   B 1 199 ? 24.989  -39.009 36.187  1.00 14.89 ? 203 ALA   B O    1 
ATOM   3112 C  CB   . ALA   B 1 199 ? 27.200  -38.082 33.944  1.00 15.42 ? 203 ALA   B CB   1 
ATOM   3113 N  N    . LEU   B 1 200 ? 24.593  -36.952 35.352  1.00 13.87 ? 204 LEU   B N    1 
ATOM   3114 C  CA   . LEU   B 1 200 ? 23.898  -36.478 36.532  1.00 13.98 ? 204 LEU   B CA   1 
ATOM   3115 C  C    . LEU   B 1 200 ? 22.615  -37.280 36.743  1.00 14.02 ? 204 LEU   B C    1 
ATOM   3116 O  O    . LEU   B 1 200 ? 22.305  -37.690 37.856  1.00 15.10 ? 204 LEU   B O    1 
ATOM   3117 C  CB   . LEU   B 1 200 ? 23.608  -34.987 36.408  1.00 14.37 ? 204 LEU   B CB   1 
ATOM   3118 C  CG   . LEU   B 1 200 ? 22.811  -34.393 37.569  1.00 14.62 ? 204 LEU   B CG   1 
ATOM   3119 C  CD1  . LEU   B 1 200 ? 23.511  -34.645 38.904  1.00 15.53 ? 204 LEU   B CD1  1 
ATOM   3120 C  CD2  . LEU   B 1 200 ? 22.568  -32.920 37.323  1.00 14.75 ? 204 LEU   B CD2  1 
ATOM   3121 N  N    . LEU   B 1 201 ? 21.864  -37.512 35.668  1.00 13.84 ? 205 LEU   B N    1 
ATOM   3122 C  CA   . LEU   B 1 201 ? 20.665  -38.326 35.757  1.00 14.48 ? 205 LEU   B CA   1 
ATOM   3123 C  C    . LEU   B 1 201 ? 21.000  -39.701 36.333  1.00 15.24 ? 205 LEU   B C    1 
ATOM   3124 O  O    . LEU   B 1 201 ? 20.302  -40.181 37.226  1.00 15.91 ? 205 LEU   B O    1 
ATOM   3125 C  CB   . LEU   B 1 201 ? 20.022  -38.444 34.373  1.00 15.33 ? 205 LEU   B CB   1 
ATOM   3126 C  CG   . LEU   B 1 201 ? 18.822  -39.392 34.269  1.00 16.53 ? 205 LEU   B CG   1 
ATOM   3127 C  CD1  . LEU   B 1 201 ? 17.696  -38.988 35.209  1.00 17.48 ? 205 LEU   B CD1  1 
ATOM   3128 C  CD2  . LEU   B 1 201 ? 18.328  -39.411 32.839  1.00 17.89 ? 205 LEU   B CD2  1 
ATOM   3129 N  N    . SER   B 1 202 ? 22.051  -40.345 35.807  1.00 15.55 ? 206 SER   B N    1 
ATOM   3130 C  CA   . SER   B 1 202 ? 22.413  -41.680 36.264  1.00 16.32 ? 206 SER   B CA   1 
ATOM   3131 C  C    . SER   B 1 202 ? 22.719  -41.666 37.761  1.00 16.62 ? 206 SER   B C    1 
ATOM   3132 O  O    . SER   B 1 202 ? 22.321  -42.579 38.484  1.00 18.13 ? 206 SER   B O    1 
ATOM   3133 C  CB   . SER   B 1 202 ? 23.572  -42.246 35.478  1.00 17.00 ? 206 SER   B CB   1 
ATOM   3134 O  OG   . SER   B 1 202 ? 23.218  -42.446 34.118  1.00 18.57 ? 206 SER   B OG   1 
ATOM   3135 N  N    . ILE   B 1 203 ? 23.447  -40.640 38.224  1.00 16.79 ? 207 ILE   B N    1 
ATOM   3136 C  CA   . ILE   B 1 203 ? 23.755  -40.507 39.641  1.00 17.72 ? 207 ILE   B CA   1 
ATOM   3137 C  C    . ILE   B 1 203 ? 22.455  -40.382 40.435  1.00 18.03 ? 207 ILE   B C    1 
ATOM   3138 O  O    . ILE   B 1 203 ? 22.281  -41.045 41.452  1.00 20.12 ? 207 ILE   B O    1 
ATOM   3139 C  CB   . ILE   B 1 203 ? 24.709  -39.325 39.884  1.00 18.44 ? 207 ILE   B CB   1 
ATOM   3140 C  CG1  . ILE   B 1 203 ? 26.110  -39.644 39.379  1.00 18.78 ? 207 ILE   B CG1  1 
ATOM   3141 C  CG2  . ILE   B 1 203 ? 24.709  -38.913 41.355  1.00 19.71 ? 207 ILE   B CG2  1 
ATOM   3142 C  CD1  . ILE   B 1 203 ? 26.946  -38.410 39.105  1.00 18.83 ? 207 ILE   B CD1  1 
ATOM   3143 N  N    . CYS   B 1 204 ? 21.522  -39.563 39.946  1.00 17.43 ? 208 CYS   B N    1 
ATOM   3144 C  CA   . CYS   B 1 204 ? 20.287  -39.308 40.668  1.00 17.74 ? 208 CYS   B CA   1 
ATOM   3145 C  C    . CYS   B 1 204 ? 19.367  -40.528 40.658  1.00 18.47 ? 208 CYS   B C    1 
ATOM   3146 O  O    . CYS   B 1 204 ? 18.497  -40.635 41.520  1.00 20.28 ? 208 CYS   B O    1 
ATOM   3147 C  CB   . CYS   B 1 204 ? 19.606  -38.054 40.133  1.00 17.13 ? 208 CYS   B CB   1 
ATOM   3148 S  SG   . CYS   B 1 204 ? 20.517  -36.536 40.528  1.00 18.74 ? 208 CYS   B SG   1 
ATOM   3149 N  N    . GLN   B 1 205 ? 19.601  -41.469 39.732  1.00 18.74 ? 209 GLN   B N    1 
ATOM   3150 C  CA   . GLN   B 1 205 ? 18.836  -42.708 39.684  1.00 19.71 ? 209 GLN   B CA   1 
ATOM   3151 C  C    . GLN   B 1 205 ? 19.397  -43.804 40.596  1.00 21.41 ? 209 GLN   B C    1 
ATOM   3152 O  O    . GLN   B 1 205 ? 18.815  -44.885 40.652  1.00 22.02 ? 209 GLN   B O    1 
ATOM   3153 C  CB   . GLN   B 1 205 ? 18.770  -43.224 38.250  1.00 20.16 ? 209 GLN   B CB   1 
ATOM   3154 C  CG   . GLN   B 1 205 ? 17.901  -42.373 37.335  1.00 20.12 ? 209 GLN   B CG   1 
ATOM   3155 C  CD   . GLN   B 1 205 ? 17.848  -42.951 35.944  1.00 21.06 ? 209 GLN   B CD   1 
ATOM   3156 O  OE1  . GLN   B 1 205 ? 18.780  -42.787 35.155  1.00 22.77 ? 209 GLN   B OE1  1 
ATOM   3157 N  NE2  . GLN   B 1 205 ? 16.780  -43.674 35.646  1.00 22.42 ? 209 GLN   B NE2  1 
ATOM   3158 N  N    . TRP   B 1 206 ? 20.504  -43.541 41.306  1.00 21.85 ? 210 TRP   B N    1 
ATOM   3159 C  CA   . TRP   B 1 206 ? 21.100  -44.527 42.202  1.00 23.78 ? 210 TRP   B CA   1 
ATOM   3160 C  C    . TRP   B 1 206 ? 20.161  -44.844 43.369  1.00 24.17 ? 210 TRP   B C    1 
ATOM   3161 O  O    . TRP   B 1 206 ? 19.878  -46.011 43.645  1.00 24.99 ? 210 TRP   B O    1 
ATOM   3162 C  CB   . TRP   B 1 206 ? 22.465  -44.022 42.690  1.00 26.36 ? 210 TRP   B CB   1 
ATOM   3163 C  CG   . TRP   B 1 206 ? 23.140  -44.916 43.695  1.00 30.45 ? 210 TRP   B CG   1 
ATOM   3164 C  CD1  . TRP   B 1 206 ? 23.573  -46.194 43.505  1.00 34.41 ? 210 TRP   B CD1  1 
ATOM   3165 C  CD2  . TRP   B 1 206 ? 23.509  -44.558 45.042  1.00 35.34 ? 210 TRP   B CD2  1 
ATOM   3166 N  NE1  . TRP   B 1 206 ? 24.151  -46.672 44.650  1.00 35.97 ? 210 TRP   B NE1  1 
ATOM   3167 C  CE2  . TRP   B 1 206 ? 24.137  -45.689 45.606  1.00 37.01 ? 210 TRP   B CE2  1 
ATOM   3168 C  CE3  . TRP   B 1 206 ? 23.368  -43.401 45.820  1.00 39.01 ? 210 TRP   B CE3  1 
ATOM   3169 C  CZ2  . TRP   B 1 206 ? 24.622  -45.694 46.912  1.00 41.37 ? 210 TRP   B CZ2  1 
ATOM   3170 C  CZ3  . TRP   B 1 206 ? 23.854  -43.408 47.111  1.00 41.91 ? 210 TRP   B CZ3  1 
ATOM   3171 C  CH2  . TRP   B 1 206 ? 24.473  -44.538 47.645  1.00 42.57 ? 210 TRP   B CH2  1 
ATOM   3172 N  N    . ARG   B 1 207 ? 19.706  -43.790 44.058  1.00 22.95 ? 211 ARG   B N    1 
ATOM   3173 C  CA   . ARG   B 1 207 ? 18.726  -43.909 45.126  1.00 24.48 ? 211 ARG   B CA   1 
ATOM   3174 C  C    . ARG   B 1 207 ? 17.619  -42.909 44.820  1.00 22.64 ? 211 ARG   B C    1 
ATOM   3175 O  O    . ARG   B 1 207 ? 17.548  -41.826 45.401  1.00 22.49 ? 211 ARG   B O    1 
ATOM   3176 C  CB   . ARG   B 1 207 ? 19.390  -43.687 46.491  1.00 25.73 ? 211 ARG   B CB   1 
ATOM   3177 C  CG   . ARG   B 1 207 ? 20.304  -44.832 46.905  1.00 27.68 ? 211 ARG   B CG   1 
ATOM   3178 C  CD   . ARG   B 1 207 ? 19.567  -46.161 46.921  1.00 30.60 ? 211 ARG   B CD   1 
ATOM   3179 N  N    . PRO   B 1 208 ? 16.760  -43.226 43.832  1.00 22.18 ? 212 PRO   B N    1 
ATOM   3180 C  CA   . PRO   B 1 208 ? 15.919  -42.205 43.214  1.00 21.28 ? 212 PRO   B CA   1 
ATOM   3181 C  C    . PRO   B 1 208 ? 14.849  -41.634 44.140  1.00 20.25 ? 212 PRO   B C    1 
ATOM   3182 O  O    . PRO   B 1 208 ? 14.574  -40.442 44.109  1.00 20.17 ? 212 PRO   B O    1 
ATOM   3183 C  CB   . PRO   B 1 208 ? 15.338  -42.932 41.988  1.00 22.31 ? 212 PRO   B CB   1 
ATOM   3184 C  CG   . PRO   B 1 208 ? 15.395  -44.396 42.339  1.00 23.44 ? 212 PRO   B CG   1 
ATOM   3185 C  CD   . PRO   B 1 208 ? 16.612  -44.553 43.213  1.00 23.04 ? 212 PRO   B CD   1 
ATOM   3186 N  N    . GLN   B 1 209 ? 14.263  -42.481 44.983  1.00 20.77 ? 213 GLN   B N    1 
ATOM   3187 C  CA   . GLN   B 1 209 ? 13.188  -42.026 45.849  1.00 22.11 ? 213 GLN   B CA   1 
ATOM   3188 C  C    . GLN   B 1 209 ? 13.726  -41.057 46.901  1.00 21.69 ? 213 GLN   B C    1 
ATOM   3189 O  O    . GLN   B 1 209 ? 13.094  -40.040 47.182  1.00 21.10 ? 213 GLN   B O    1 
ATOM   3190 C  CB   . GLN   B 1 209 ? 12.468  -43.192 46.520  1.00 23.71 ? 213 GLN   B CB   1 
ATOM   3191 C  CG   . GLN   B 1 209 ? 11.804  -44.166 45.553  1.00 25.62 ? 213 GLN   B CG   1 
ATOM   3192 C  CD   . GLN   B 1 209 ? 12.700  -45.310 45.129  1.00 29.35 ? 213 GLN   B CD   1 
ATOM   3193 O  OE1  . GLN   B 1 209 ? 13.933  -45.261 45.247  1.00 30.48 ? 213 GLN   B OE1  1 
ATOM   3194 N  NE2  . GLN   B 1 209 ? 12.078  -46.358 44.612  1.00 34.41 ? 213 GLN   B NE2  1 
ATOM   3195 N  N    . ALA   B 1 210 ? 14.902  -41.367 47.463  1.00 21.65 ? 214 ALA   B N    1 
ATOM   3196 C  CA   . ALA   B 1 210 ? 15.552  -40.492 48.431  1.00 23.03 ? 214 ALA   B CA   1 
ATOM   3197 C  C    . ALA   B 1 210 ? 15.944  -39.162 47.787  1.00 21.78 ? 214 ALA   B C    1 
ATOM   3198 O  O    . ALA   B 1 210 ? 15.763  -38.108 48.390  1.00 22.86 ? 214 ALA   B O    1 
ATOM   3199 C  CB   . ALA   B 1 210 ? 16.758  -41.180 49.027  1.00 24.10 ? 214 ALA   B CB   1 
ATOM   3200 N  N    . LEU   B 1 211 ? 16.469  -39.220 46.557  1.00 20.65 ? 215 LEU   B N    1 
ATOM   3201 C  CA   . LEU   B 1 211 ? 16.877  -38.023 45.836  1.00 20.31 ? 215 LEU   B CA   1 
ATOM   3202 C  C    . LEU   B 1 211 ? 15.657  -37.134 45.605  1.00 19.40 ? 215 LEU   B C    1 
ATOM   3203 O  O    . LEU   B 1 211 ? 15.698  -35.935 45.856  1.00 19.72 ? 215 LEU   B O    1 
ATOM   3204 C  CB   . LEU   B 1 211 ? 17.580  -38.426 44.537  1.00 20.88 ? 215 LEU   B CB   1 
ATOM   3205 C  CG   . LEU   B 1 211 ? 18.182  -37.311 43.670  1.00 21.73 ? 215 LEU   B CG   1 
ATOM   3206 C  CD1  . LEU   B 1 211 ? 17.147  -36.652 42.783  1.00 22.40 ? 215 LEU   B CD1  1 
ATOM   3207 C  CD2  . LEU   B 1 211 ? 18.900  -36.245 44.496  1.00 22.67 ? 215 LEU   B CD2  1 
ATOM   3208 N  N    . LEU   B 1 212 ? 14.564  -37.733 45.126  1.00 18.93 ? 216 LEU   B N    1 
ATOM   3209 C  CA   . LEU   B 1 212 ? 13.369  -36.965 44.828  1.00 18.22 ? 216 LEU   B CA   1 
ATOM   3210 C  C    . LEU   B 1 212 ? 12.831  -36.295 46.092  1.00 18.75 ? 216 LEU   B C    1 
ATOM   3211 O  O    . LEU   B 1 212 ? 12.415  -35.143 46.044  1.00 18.84 ? 216 LEU   B O    1 
ATOM   3212 C  CB   . LEU   B 1 212 ? 12.321  -37.860 44.172  1.00 17.47 ? 216 LEU   B CB   1 
ATOM   3213 C  CG   . LEU   B 1 212 ? 11.011  -37.169 43.796  1.00 17.24 ? 216 LEU   B CG   1 
ATOM   3214 C  CD1  . LEU   B 1 212 ? 11.221  -36.032 42.819  1.00 17.50 ? 216 LEU   B CD1  1 
ATOM   3215 C  CD2  . LEU   B 1 212 ? 10.051  -38.216 43.267  1.00 17.69 ? 216 LEU   B CD2  1 
ATOM   3216 N  N    . ARG   B 1 213 ? 12.809  -37.023 47.215  1.00 20.21 ? 217 ARG   B N    1 
ATOM   3217 C  CA   . ARG   B 1 213 ? 12.361  -36.458 48.481  1.00 21.88 ? 217 ARG   B CA   1 
ATOM   3218 C  C    . ARG   B 1 213 ? 13.215  -35.247 48.851  1.00 21.89 ? 217 ARG   B C    1 
ATOM   3219 O  O    . ARG   B 1 213 ? 12.698  -34.228 49.301  1.00 21.63 ? 217 ARG   B O    1 
ATOM   3220 C  CB   . ARG   B 1 213 ? 12.404  -37.482 49.626  1.00 25.10 ? 217 ARG   B CB   1 
ATOM   3221 C  CG   . ARG   B 1 213 ? 11.195  -38.404 49.678  1.00 29.77 ? 217 ARG   B CG   1 
ATOM   3222 C  CD   . ARG   B 1 213 ? 11.084  -39.171 51.006  1.00 33.61 ? 217 ARG   B CD   1 
ATOM   3223 N  NE   . ARG   B 1 213 ? 11.920  -40.379 51.036  1.00 38.17 ? 217 ARG   B NE   1 
ATOM   3224 C  CZ   . ARG   B 1 213 ? 11.672  -41.500 50.357  1.00 41.40 ? 217 ARG   B CZ   1 
ATOM   3225 N  NH1  . ARG   B 1 213 ? 10.516  -41.667 49.725  1.00 43.99 ? 217 ARG   B NH1  1 
ATOM   3226 N  NH2  . ARG   B 1 213 ? 12.571  -42.467 50.340  1.00 42.69 ? 217 ARG   B NH2  1 
ATOM   3227 N  N    . TRP   B 1 214 ? 14.533  -35.364 48.672  1.00 20.53 ? 218 TRP   B N    1 
ATOM   3228 C  CA   . TRP   B 1 214 ? 15.414  -34.264 49.016  1.00 21.93 ? 218 TRP   B CA   1 
ATOM   3229 C  C    . TRP   B 1 214 ? 15.117  -33.054 48.132  1.00 21.60 ? 218 TRP   B C    1 
ATOM   3230 O  O    . TRP   B 1 214 ? 15.014  -31.929 48.620  1.00 22.65 ? 218 TRP   B O    1 
ATOM   3231 C  CB   . TRP   B 1 214 ? 16.880  -34.695 48.922  1.00 23.60 ? 218 TRP   B CB   1 
ATOM   3232 C  CG   . TRP   B 1 214 ? 17.773  -33.777 49.706  1.00 26.61 ? 218 TRP   B CG   1 
ATOM   3233 C  CD1  . TRP   B 1 214 ? 18.207  -33.951 50.987  1.00 28.24 ? 218 TRP   B CD1  1 
ATOM   3234 C  CD2  . TRP   B 1 214 ? 18.280  -32.501 49.272  1.00 28.18 ? 218 TRP   B CD2  1 
ATOM   3235 N  NE1  . TRP   B 1 214 ? 18.977  -32.887 51.370  1.00 30.13 ? 218 TRP   B NE1  1 
ATOM   3236 C  CE2  . TRP   B 1 214 ? 19.038  -31.980 50.344  1.00 29.09 ? 218 TRP   B CE2  1 
ATOM   3237 C  CE3  . TRP   B 1 214 ? 18.177  -31.762 48.088  1.00 27.99 ? 218 TRP   B CE3  1 
ATOM   3238 C  CZ2  . TRP   B 1 214 ? 19.683  -30.748 50.264  1.00 30.21 ? 218 TRP   B CZ2  1 
ATOM   3239 C  CZ3  . TRP   B 1 214 ? 18.816  -30.545 48.012  1.00 28.83 ? 218 TRP   B CZ3  1 
ATOM   3240 C  CH2  . TRP   B 1 214 ? 19.552  -30.046 49.086  1.00 29.15 ? 218 TRP   B CH2  1 
ATOM   3241 N  N    . VAL   B 1 215 ? 14.959  -33.291 46.827  1.00 20.03 ? 219 VAL   B N    1 
ATOM   3242 C  CA   . VAL   B 1 215 ? 14.673  -32.214 45.890  1.00 20.05 ? 219 VAL   B CA   1 
ATOM   3243 C  C    . VAL   B 1 215 ? 13.380  -31.501 46.289  1.00 20.18 ? 219 VAL   B C    1 
ATOM   3244 O  O    . VAL   B 1 215 ? 13.333  -30.274 46.322  1.00 21.06 ? 219 VAL   B O    1 
ATOM   3245 C  CB   . VAL   B 1 215 ? 14.619  -32.753 44.451  1.00 20.12 ? 219 VAL   B CB   1 
ATOM   3246 C  CG1  . VAL   B 1 215 ? 13.982  -31.766 43.479  1.00 20.72 ? 219 VAL   B CG1  1 
ATOM   3247 C  CG2  . VAL   B 1 215 ? 16.004  -33.173 43.968  1.00 21.03 ? 219 VAL   B CG2  1 
ATOM   3248 N  N    . ASP   B 1 216 ? 12.327  -32.270 46.583  1.00 20.61 ? 220 ASP   B N    1 
ATOM   3249 C  CA   . ASP   B 1 216 ? 11.053  -31.699 47.006  1.00 21.33 ? 220 ASP   B CA   1 
ATOM   3250 C  C    . ASP   B 1 216 ? 11.237  -30.832 48.255  1.00 23.77 ? 220 ASP   B C    1 
ATOM   3251 O  O    . ASP   B 1 216 ? 10.659  -29.750 48.360  1.00 24.87 ? 220 ASP   B O    1 
ATOM   3252 C  CB   . ASP   B 1 216 ? 10.023  -32.788 47.264  1.00 22.25 ? 220 ASP   B CB   1 
ATOM   3253 C  CG   . ASP   B 1 216 ? 9.390   -33.425 46.034  1.00 22.22 ? 220 ASP   B CG   1 
ATOM   3254 O  OD1  . ASP   B 1 216 ? 9.401   -32.784 44.967  1.00 21.45 ? 220 ASP   B OD1  1 
ATOM   3255 O  OD2  . ASP   B 1 216 ? 8.891   -34.564 46.150  1.00 23.28 ? 220 ASP   B OD2  1 
ATOM   3256 N  N    . ALA   B 1 217 ? 12.067  -31.300 49.191  1.00 24.47 ? 221 ALA   B N    1 
ATOM   3257 C  CA   . ALA   B 1 217 ? 12.227  -30.635 50.475  1.00 26.39 ? 221 ALA   B CA   1 
ATOM   3258 C  C    . ALA   B 1 217 ? 13.053  -29.352 50.372  1.00 26.78 ? 221 ALA   B C    1 
ATOM   3259 O  O    . ALA   B 1 217 ? 12.947  -28.496 51.254  1.00 29.05 ? 221 ALA   B O    1 
ATOM   3260 C  CB   . ALA   B 1 217 ? 12.853  -31.593 51.469  1.00 27.06 ? 221 ALA   B CB   1 
ATOM   3261 N  N    . HIS   B 1 218 ? 13.890  -29.225 49.335  1.00 24.91 ? 222 HIS   B N    1 
ATOM   3262 C  CA   . HIS   B 1 218 ? 14.863  -28.139 49.278  1.00 26.13 ? 222 HIS   B CA   1 
ATOM   3263 C  C    . HIS   B 1 218 ? 14.732  -27.266 48.027  1.00 22.92 ? 222 HIS   B C    1 
ATOM   3264 O  O    . HIS   B 1 218 ? 15.550  -26.377 47.822  1.00 24.40 ? 222 HIS   B O    1 
ATOM   3265 C  CB   . HIS   B 1 218 ? 16.276  -28.717 49.387  1.00 28.78 ? 222 HIS   B CB   1 
ATOM   3266 C  CG   . HIS   B 1 218 ? 16.529  -29.359 50.706  1.00 31.76 ? 222 HIS   B CG   1 
ATOM   3267 N  ND1  . HIS   B 1 218 ? 16.081  -30.624 51.018  1.00 33.75 ? 222 HIS   B ND1  1 
ATOM   3268 C  CD2  . HIS   B 1 218 ? 17.150  -28.900 51.807  1.00 33.76 ? 222 HIS   B CD2  1 
ATOM   3269 C  CE1  . HIS   B 1 218 ? 16.441  -30.919 52.262  1.00 34.78 ? 222 HIS   B CE1  1 
ATOM   3270 N  NE2  . HIS   B 1 218 ? 17.092  -29.888 52.759  1.00 35.72 ? 222 HIS   B NE2  1 
ATOM   3271 N  N    . ALA   B 1 219 ? 13.687  -27.471 47.217  1.00 21.37 ? 223 ALA   B N    1 
ATOM   3272 C  CA   . ALA   B 1 219 ? 13.489  -26.688 46.005  1.00 20.40 ? 223 ALA   B CA   1 
ATOM   3273 C  C    . ALA   B 1 219 ? 13.420  -25.195 46.328  1.00 20.00 ? 223 ALA   B C    1 
ATOM   3274 O  O    . ALA   B 1 219 ? 12.718  -24.788 47.251  1.00 21.16 ? 223 ALA   B O    1 
ATOM   3275 C  CB   . ALA   B 1 219 ? 12.234  -27.160 45.303  1.00 21.21 ? 223 ALA   B CB   1 
ATOM   3276 N  N    . ARG   B 1 220 ? 14.149  -24.394 45.536  1.00 19.50 ? 224 ARG   B N    1 
ATOM   3277 C  CA   . ARG   B 1 220 ? 14.266  -22.959 45.732  1.00 21.15 ? 224 ARG   B CA   1 
ATOM   3278 C  C    . ARG   B 1 220 ? 13.653  -22.229 44.540  1.00 19.74 ? 224 ARG   B C    1 
ATOM   3279 O  O    . ARG   B 1 220 ? 13.924  -22.580 43.391  1.00 17.93 ? 224 ARG   B O    1 
ATOM   3280 C  CB   . ARG   B 1 220 ? 15.760  -22.629 45.854  1.00 23.73 ? 224 ARG   B CB   1 
ATOM   3281 C  CG   . ARG   B 1 220 ? 16.188  -21.173 45.735  1.00 27.86 ? 224 ARG   B CG   1 
ATOM   3282 C  CD   . ARG   B 1 220 ? 17.695  -21.003 45.940  1.00 30.26 ? 224 ARG   B CD   1 
ATOM   3283 N  NE   . ARG   B 1 220 ? 18.131  -19.600 45.895  1.00 34.07 ? 224 ARG   B NE   1 
ATOM   3284 C  CZ   . ARG   B 1 220 ? 19.396  -19.192 45.996  1.00 37.01 ? 224 ARG   B CZ   1 
ATOM   3285 N  NH1  . ARG   B 1 220 ? 20.367  -20.076 46.168  1.00 40.44 ? 224 ARG   B NH1  1 
ATOM   3286 N  NH2  . ARG   B 1 220 ? 19.694  -17.901 45.910  1.00 39.19 ? 224 ARG   B NH2  1 
ATOM   3287 N  N    . PRO   B 1 221 ? 12.839  -21.174 44.749  1.00 20.49 ? 225 PRO   B N    1 
ATOM   3288 C  CA   . PRO   B 1 221 ? 12.326  -20.381 43.631  1.00 20.91 ? 225 PRO   B CA   1 
ATOM   3289 C  C    . PRO   B 1 221 ? 13.469  -19.831 42.785  1.00 19.62 ? 225 PRO   B C    1 
ATOM   3290 O  O    . PRO   B 1 221 ? 14.434  -19.301 43.320  1.00 19.13 ? 225 PRO   B O    1 
ATOM   3291 C  CB   . PRO   B 1 221 ? 11.523  -19.271 44.305  1.00 22.65 ? 225 PRO   B CB   1 
ATOM   3292 C  CG   . PRO   B 1 221 ? 11.171  -19.844 45.648  1.00 23.52 ? 225 PRO   B CG   1 
ATOM   3293 C  CD   . PRO   B 1 221 ? 12.348  -20.701 46.054  1.00 22.79 ? 225 PRO   B CD   1 
ATOM   3294 N  N    . PHE   B 1 222 ? 13.348  -19.943 41.463  1.00 18.89 ? 226 PHE   B N    1 
ATOM   3295 C  CA   . PHE   B 1 222 ? 14.433  -19.553 40.579  1.00 19.64 ? 226 PHE   B CA   1 
ATOM   3296 C  C    . PHE   B 1 222 ? 14.653  -18.042 40.652  1.00 21.09 ? 226 PHE   B C    1 
ATOM   3297 O  O    . PHE   B 1 222 ? 15.765  -17.576 40.438  1.00 21.81 ? 226 PHE   B O    1 
ATOM   3298 C  CB   . PHE   B 1 222 ? 14.144  -20.040 39.157  1.00 19.95 ? 226 PHE   B CB   1 
ATOM   3299 C  CG   . PHE   B 1 222 ? 15.339  -19.881 38.231  1.00 20.26 ? 226 PHE   B CG   1 
ATOM   3300 C  CD1  . PHE   B 1 222 ? 16.470  -20.675 38.384  1.00 22.32 ? 226 PHE   B CD1  1 
ATOM   3301 C  CD2  . PHE   B 1 222 ? 15.340  -18.923 37.227  1.00 21.63 ? 226 PHE   B CD2  1 
ATOM   3302 C  CE1  . PHE   B 1 222 ? 17.560  -20.522 37.543  1.00 22.61 ? 226 PHE   B CE1  1 
ATOM   3303 C  CE2  . PHE   B 1 222 ? 16.434  -18.779 36.386  1.00 22.70 ? 226 PHE   B CE2  1 
ATOM   3304 C  CZ   . PHE   B 1 222 ? 17.547  -19.567 36.558  1.00 22.69 ? 226 PHE   B CZ   1 
ATOM   3305 N  N    . GLY   B 1 223 ? 13.604  -17.282 40.985  1.00 22.37 ? 227 GLY   B N    1 
ATOM   3306 C  CA   . GLY   B 1 223 ? 13.712  -15.837 41.115  1.00 23.98 ? 227 GLY   B CA   1 
ATOM   3307 C  C    . GLY   B 1 223 ? 14.630  -15.397 42.257  1.00 24.76 ? 227 GLY   B C    1 
ATOM   3308 O  O    . GLY   B 1 223 ? 15.010  -14.229 42.318  1.00 27.82 ? 227 GLY   B O    1 
ATOM   3309 N  N    . THR   B 1 224 ? 15.001  -16.312 43.163  1.00 24.17 ? 228 THR   B N    1 
ATOM   3310 C  CA   . THR   B 1 224 ? 15.934  -15.982 44.231  1.00 25.15 ? 228 THR   B CA   1 
ATOM   3311 C  C    . THR   B 1 224 ? 17.385  -16.138 43.771  1.00 23.22 ? 228 THR   B C    1 
ATOM   3312 O  O    . THR   B 1 224 ? 18.294  -15.812 44.532  1.00 24.39 ? 228 THR   B O    1 
ATOM   3313 C  CB   . THR   B 1 224 ? 15.671  -16.821 45.482  1.00 26.77 ? 228 THR   B CB   1 
ATOM   3314 O  OG1  . THR   B 1 224 ? 15.998  -18.176 45.191  1.00 27.55 ? 228 THR   B OG1  1 
ATOM   3315 C  CG2  . THR   B 1 224 ? 14.237  -16.703 45.969  1.00 27.86 ? 228 THR   B CG2  1 
ATOM   3316 N  N    . ILE   B 1 225 ? 17.610  -16.632 42.545  1.00 21.63 ? 229 ILE   B N    1 
ATOM   3317 C  CA   . ILE   B 1 225 ? 18.956  -16.718 41.998  1.00 21.43 ? 229 ILE   B CA   1 
ATOM   3318 C  C    . ILE   B 1 225 ? 19.324  -15.365 41.399  1.00 21.57 ? 229 ILE   B C    1 
ATOM   3319 O  O    . ILE   B 1 225 ? 18.693  -14.922 40.446  1.00 23.47 ? 229 ILE   B O    1 
ATOM   3320 C  CB   . ILE   B 1 225 ? 19.072  -17.816 40.924  1.00 20.95 ? 229 ILE   B CB   1 
ATOM   3321 C  CG1  . ILE   B 1 225 ? 18.665  -19.195 41.437  1.00 21.14 ? 229 ILE   B CG1  1 
ATOM   3322 C  CG2  . ILE   B 1 225 ? 20.478  -17.835 40.322  1.00 21.27 ? 229 ILE   B CG2  1 
ATOM   3323 C  CD1  . ILE   B 1 225 ? 19.619  -19.784 42.458  1.00 21.39 ? 229 ILE   B CD1  1 
ATOM   3324 N  N    . ARG   B 1 226 ? 20.374  -14.741 41.932  1.00 22.12 ? 230 ARG   B N    1 
ATOM   3325 C  CA   . ARG   B 1 226 ? 20.852  -13.478 41.399  1.00 22.30 ? 230 ARG   B CA   1 
ATOM   3326 C  C    . ARG   B 1 226 ? 21.605  -13.741 40.096  1.00 20.33 ? 230 ARG   B C    1 
ATOM   3327 O  O    . ARG   B 1 226 ? 22.321  -14.731 39.983  1.00 19.83 ? 230 ARG   B O    1 
ATOM   3328 C  CB   . ARG   B 1 226 ? 21.759  -12.779 42.415  1.00 25.20 ? 230 ARG   B CB   1 
ATOM   3329 C  CG   . ARG   B 1 226 ? 21.050  -12.323 43.682  1.00 28.30 ? 230 ARG   B CG   1 
ATOM   3330 C  CD   . ARG   B 1 226 ? 22.038  -11.764 44.701  1.00 29.82 ? 230 ARG   B CD   1 
ATOM   3331 N  N    . PRO   B 1 227 ? 21.484  -12.862 39.080  1.00 20.47 ? 231 PRO   B N    1 
ATOM   3332 C  CA   . PRO   B 1 227 ? 22.246  -13.020 37.845  1.00 19.31 ? 231 PRO   B CA   1 
ATOM   3333 C  C    . PRO   B 1 227 ? 23.739  -12.942 38.132  1.00 18.81 ? 231 PRO   B C    1 
ATOM   3334 O  O    . PRO   B 1 227 ? 24.179  -12.189 38.998  1.00 19.98 ? 231 PRO   B O    1 
ATOM   3335 C  CB   . PRO   B 1 227 ? 21.772  -11.870 36.950  1.00 20.56 ? 231 PRO   B CB   1 
ATOM   3336 C  CG   . PRO   B 1 227 ? 21.220  -10.855 37.918  1.00 22.47 ? 231 PRO   B CG   1 
ATOM   3337 C  CD   . PRO   B 1 227 ? 20.672  -11.640 39.085  1.00 21.68 ? 231 PRO   B CD   1 
ATOM   3338 N  N    . MET   B 1 228 ? 24.513  -13.706 37.359  1.00 17.63 ? 232 MET   B N    1 
ATOM   3339 C  CA   . MET   B 1 228 ? 25.954  -13.743 37.522  1.00 17.55 ? 232 MET   B CA   1 
ATOM   3340 C  C    . MET   B 1 228 ? 26.545  -12.345 37.319  1.00 18.21 ? 232 MET   B C    1 
ATOM   3341 O  O    . MET   B 1 228 ? 27.549  -11.997 37.942  1.00 21.14 ? 232 MET   B O    1 
ATOM   3342 C  CB   . MET   B 1 228 ? 26.564  -14.734 36.529  1.00 16.82 ? 232 MET   B CB   1 
ATOM   3343 C  CG   . MET   B 1 228 ? 28.035  -14.990 36.742  1.00 17.19 ? 232 MET   B CG   1 
ATOM   3344 S  SD   . MET   B 1 228 ? 28.669  -16.309 35.688  1.00 16.50 ? 232 MET   B SD   1 
ATOM   3345 C  CE   . MET   B 1 228 ? 27.983  -17.793 36.438  1.00 15.80 ? 232 MET   B CE   1 
ATOM   3346 N  N    . TYR   B 1 229 ? 25.946  -11.579 36.402  1.00 18.96 ? 233 TYR   B N    1 
ATOM   3347 C  CA   . TYR   B 1 229 ? 26.383  -10.226 36.086  1.00 20.01 ? 233 TYR   B CA   1 
ATOM   3348 C  C    . TYR   B 1 229 ? 25.239  -9.491  35.390  1.00 22.89 ? 233 TYR   B C    1 
ATOM   3349 O  O    . TYR   B 1 229 ? 24.261  -10.124 34.980  1.00 21.95 ? 233 TYR   B O    1 
ATOM   3350 C  CB   . TYR   B 1 229 ? 27.625  -10.266 35.187  1.00 19.62 ? 233 TYR   B CB   1 
ATOM   3351 C  CG   . TYR   B 1 229 ? 27.456  -11.103 33.927  1.00 17.98 ? 233 TYR   B CG   1 
ATOM   3352 C  CD1  . TYR   B 1 229 ? 26.827  -10.591 32.796  1.00 18.09 ? 233 TYR   B CD1  1 
ATOM   3353 C  CD2  . TYR   B 1 229 ? 27.943  -12.404 33.858  1.00 17.07 ? 233 TYR   B CD2  1 
ATOM   3354 C  CE1  . TYR   B 1 229 ? 26.660  -11.352 31.649  1.00 17.48 ? 233 TYR   B CE1  1 
ATOM   3355 C  CE2  . TYR   B 1 229 ? 27.782  -13.173 32.720  1.00 16.97 ? 233 TYR   B CE2  1 
ATOM   3356 C  CZ   . TYR   B 1 229 ? 27.141  -12.647 31.609  1.00 17.03 ? 233 TYR   B CZ   1 
ATOM   3357 O  OH   . TYR   B 1 229 ? 26.978  -13.391 30.473  1.00 17.32 ? 233 TYR   B OH   1 
ATOM   3358 N  N    . GLY   B 1 230 ? 25.404  -8.162  35.242  1.00 26.44 ? 234 GLY   B N    1 
ATOM   3359 C  CA   . GLY   B 1 230 ? 24.460  -7.299  34.541  1.00 28.82 ? 234 GLY   B CA   1 
ATOM   3360 C  C    . GLY   B 1 230 ? 25.166  -6.206  33.731  1.00 30.68 ? 234 GLY   B C    1 
ATOM   3361 O  O    . GLY   B 1 230 ? 26.346  -6.333  33.391  1.00 31.66 ? 234 GLY   B O    1 
ATOM   3362 N  N    . VAL   B 1 231 ? 24.420  -5.138  33.407  1.00 31.12 ? 235 VAL   B N    1 
ATOM   3363 C  CA   . VAL   B 1 231 ? 24.944  -4.009  32.645  1.00 32.53 ? 235 VAL   B CA   1 
ATOM   3364 C  C    . VAL   B 1 231 ? 25.468  -2.926  33.592  1.00 34.86 ? 235 VAL   B C    1 
ATOM   3365 O  O    . VAL   B 1 231 ? 25.986  -1.908  33.128  1.00 35.04 ? 235 VAL   B O    1 
ATOM   3366 C  CB   . VAL   B 1 231 ? 23.920  -3.411  31.651  1.00 33.74 ? 235 VAL   B CB   1 
ATOM   3367 C  CG1  . VAL   B 1 231 ? 23.662  -4.330  30.462  1.00 34.31 ? 235 VAL   B CG1  1 
ATOM   3368 C  CG2  . VAL   B 1 231 ? 22.604  -3.019  32.316  1.00 34.46 ? 235 VAL   B CG2  1 
ATOM   3369 N  N    . THR   B 1 232 ? 25.301  -3.127  34.909  1.00 37.32 ? 236 THR   B N    1 
ATOM   3370 C  CA   . THR   B 1 232 ? 25.896  -2.265  35.925  1.00 39.88 ? 236 THR   B CA   1 
ATOM   3371 C  C    . THR   B 1 232 ? 26.715  -3.122  36.870  1.00 40.27 ? 236 THR   B C    1 
ATOM   3372 O  O    . THR   B 1 232 ? 26.453  -4.345  36.885  1.00 38.64 ? 236 THR   B O    1 
ATOM   3373 C  CB   . THR   B 1 232 ? 24.815  -1.495  36.689  1.00 42.82 ? 236 THR   B CB   1 
ATOM   3374 O  OG1  . THR   B 1 232 ? 23.994  -2.480  37.310  1.00 45.65 ? 236 THR   B OG1  1 
ATOM   3375 C  CG2  . THR   B 1 232 ? 23.979  -0.598  35.792  1.00 43.48 ? 236 THR   B CG2  1 
ATOM   3376 N  N    . LEU   C 1 2   ? 21.786  -27.997 -9.276  1.00 29.05 ? 6   LEU   C N    1 
ATOM   3377 C  CA   . LEU   C 1 2   ? 21.165  -28.057 -7.927  1.00 27.99 ? 6   LEU   C CA   1 
ATOM   3378 C  C    . LEU   C 1 2   ? 19.829  -27.333 -7.983  1.00 28.78 ? 6   LEU   C C    1 
ATOM   3379 O  O    . LEU   C 1 2   ? 19.785  -26.140 -8.272  1.00 31.87 ? 6   LEU   C O    1 
ATOM   3380 C  CB   . LEU   C 1 2   ? 22.069  -27.419 -6.877  1.00 27.79 ? 6   LEU   C CB   1 
ATOM   3381 C  CG   . LEU   C 1 2   ? 23.454  -28.043 -6.708  1.00 28.00 ? 6   LEU   C CG   1 
ATOM   3382 C  CD1  . LEU   C 1 2   ? 24.153  -27.308 -5.585  1.00 28.69 ? 6   LEU   C CD1  1 
ATOM   3383 C  CD2  . LEU   C 1 2   ? 23.392  -29.540 -6.440  1.00 28.62 ? 6   LEU   C CD2  1 
ATOM   3384 N  N    . PRO   C 1 3   ? 18.693  -28.020 -7.738  1.00 28.41 ? 7   PRO   C N    1 
ATOM   3385 C  CA   . PRO   C 1 3   ? 17.391  -27.373 -7.899  1.00 28.91 ? 7   PRO   C CA   1 
ATOM   3386 C  C    . PRO   C 1 3   ? 17.135  -26.209 -6.938  1.00 28.34 ? 7   PRO   C C    1 
ATOM   3387 O  O    . PRO   C 1 3   ? 16.384  -25.296 -7.275  1.00 30.60 ? 7   PRO   C O    1 
ATOM   3388 C  CB   . PRO   C 1 3   ? 16.406  -28.544 -7.698  1.00 29.21 ? 7   PRO   C CB   1 
ATOM   3389 C  CG   . PRO   C 1 3   ? 17.164  -29.524 -6.834  1.00 28.77 ? 7   PRO   C CG   1 
ATOM   3390 C  CD   . PRO   C 1 3   ? 18.597  -29.424 -7.307  1.00 29.14 ? 7   PRO   C CD   1 
ATOM   3391 N  N    . HIS   C 1 4   ? 17.756  -26.237 -5.747  1.00 26.72 ? 8   HIS   C N    1 
ATOM   3392 C  CA   . HIS   C 1 4   ? 17.440  -25.276 -4.698  1.00 25.94 ? 8   HIS   C CA   1 
ATOM   3393 C  C    . HIS   C 1 4   ? 18.696  -24.790 -3.976  1.00 25.36 ? 8   HIS   C C    1 
ATOM   3394 O  O    . HIS   C 1 4   ? 18.622  -24.319 -2.836  1.00 26.31 ? 8   HIS   C O    1 
ATOM   3395 C  CB   . HIS   C 1 4   ? 16.441  -25.894 -3.724  1.00 26.55 ? 8   HIS   C CB   1 
ATOM   3396 C  CG   . HIS   C 1 4   ? 15.198  -26.342 -4.409  1.00 27.80 ? 8   HIS   C CG   1 
ATOM   3397 N  ND1  . HIS   C 1 4   ? 14.253  -25.445 -4.857  1.00 29.49 ? 8   HIS   C ND1  1 
ATOM   3398 C  CD2  . HIS   C 1 4   ? 14.753  -27.558 -4.747  1.00 29.34 ? 8   HIS   C CD2  1 
ATOM   3399 C  CE1  . HIS   C 1 4   ? 13.259  -26.109 -5.433  1.00 29.78 ? 8   HIS   C CE1  1 
ATOM   3400 N  NE2  . HIS   C 1 4   ? 13.543  -27.396 -5.377  1.00 29.52 ? 8   HIS   C NE2  1 
ATOM   3401 N  N    . GLY   C 1 5   ? 19.845  -24.869 -4.659  1.00 22.52 ? 9   GLY   C N    1 
ATOM   3402 C  CA   . GLY   C 1 5   ? 21.107  -24.478 -4.054  1.00 20.58 ? 9   GLY   C CA   1 
ATOM   3403 C  C    . GLY   C 1 5   ? 21.553  -25.475 -2.987  1.00 18.18 ? 9   GLY   C C    1 
ATOM   3404 O  O    . GLY   C 1 5   ? 20.988  -26.555 -2.854  1.00 19.93 ? 9   GLY   C O    1 
ATOM   3405 N  N    . HIS   C 1 6   ? 22.612  -25.131 -2.258  1.00 15.26 ? 10  HIS   C N    1 
ATOM   3406 C  CA   . HIS   C 1 6   ? 23.161  -26.035 -1.266  1.00 14.31 ? 10  HIS   C CA   1 
ATOM   3407 C  C    . HIS   C 1 6   ? 22.370  -25.938 0.037   1.00 14.12 ? 10  HIS   C C    1 
ATOM   3408 O  O    . HIS   C 1 6   ? 22.114  -24.849 0.550   1.00 14.12 ? 10  HIS   C O    1 
ATOM   3409 C  CB   . HIS   C 1 6   ? 24.636  -25.716 -1.028  1.00 15.03 ? 10  HIS   C CB   1 
ATOM   3410 C  CG   . HIS   C 1 6   ? 25.523  -26.046 -2.182  1.00 15.91 ? 10  HIS   C CG   1 
ATOM   3411 N  ND1  . HIS   C 1 6   ? 25.916  -27.343 -2.423  1.00 16.86 ? 10  HIS   C ND1  1 
ATOM   3412 C  CD2  . HIS   C 1 6   ? 26.103  -25.294 -3.126  1.00 16.39 ? 10  HIS   C CD2  1 
ATOM   3413 C  CE1  . HIS   C 1 6   ? 26.718  -27.359 -3.490  1.00 17.61 ? 10  HIS   C CE1  1 
ATOM   3414 N  NE2  . HIS   C 1 6   ? 26.834  -26.121 -3.942  1.00 17.35 ? 10  HIS   C NE2  1 
ATOM   3415 N  N    . MET   C 1 7   ? 22.024  -27.103 0.595   1.00 13.84 ? 11  MET   C N    1 
ATOM   3416 C  CA   . MET   C 1 7   ? 21.393  -27.152 1.902   1.00 13.36 ? 11  MET   C CA   1 
ATOM   3417 C  C    . MET   C 1 7   ? 22.421  -26.806 2.980   1.00 13.21 ? 11  MET   C C    1 
ATOM   3418 O  O    . MET   C 1 7   ? 23.519  -27.352 2.984   1.00 13.52 ? 11  MET   C O    1 
ATOM   3419 C  CB   . MET   C 1 7   ? 20.832  -28.556 2.147   1.00 13.76 ? 11  MET   C CB   1 
ATOM   3420 C  CG   . MET   C 1 7   ? 19.786  -29.013 1.126   1.00 14.20 ? 11  MET   C CG   1 
ATOM   3421 S  SD   . MET   C 1 7   ? 18.287  -28.022 1.102   1.00 16.16 ? 11  MET   C SD   1 
ATOM   3422 C  CE   . MET   C 1 7   ? 18.405  -27.135 -0.454  1.00 17.12 ? 11  MET   C CE   1 
ATOM   3423 N  N    . GLN   C 1 8   ? 22.057  -25.901 3.898   1.00 12.76 ? 12  GLN   C N    1 
ATOM   3424 C  CA   . GLN   C 1 8   ? 22.989  -25.454 4.926   1.00 12.55 ? 12  GLN   C CA   1 
ATOM   3425 C  C    . GLN   C 1 8   ? 22.905  -26.297 6.193   1.00 12.32 ? 12  GLN   C C    1 
ATOM   3426 O  O    . GLN   C 1 8   ? 23.906  -26.440 6.888   1.00 12.47 ? 12  GLN   C O    1 
ATOM   3427 C  CB   . GLN   C 1 8   ? 22.803  -23.972 5.244   1.00 12.79 ? 12  GLN   C CB   1 
ATOM   3428 C  CG   . GLN   C 1 8   ? 23.051  -23.084 4.031   1.00 12.78 ? 12  GLN   C CG   1 
ATOM   3429 C  CD   . GLN   C 1 8   ? 24.413  -23.327 3.429   1.00 12.67 ? 12  GLN   C CD   1 
ATOM   3430 O  OE1  . GLN   C 1 8   ? 25.450  -23.028 4.039   1.00 13.71 ? 12  GLN   C OE1  1 
ATOM   3431 N  NE2  . GLN   C 1 8   ? 24.421  -23.893 2.230   1.00 12.65 ? 12  GLN   C NE2  1 
ATOM   3432 N  N    . THR   C 1 9   ? 21.705  -26.796 6.507   1.00 12.17 ? 13  THR   C N    1 
ATOM   3433 C  CA   . THR   C 1 9   ? 21.512  -27.627 7.684   1.00 12.55 ? 13  THR   C CA   1 
ATOM   3434 C  C    . THR   C 1 9   ? 20.784  -28.887 7.237   1.00 12.71 ? 13  THR   C C    1 
ATOM   3435 O  O    . THR   C 1 9   ? 19.751  -28.791 6.575   1.00 14.09 ? 13  THR   C O    1 
ATOM   3436 C  CB   . THR   C 1 9   ? 20.697  -26.915 8.761   1.00 13.54 ? 13  THR   C CB   1 
ATOM   3437 O  OG1  . THR   C 1 9   ? 21.280  -25.650 9.042   1.00 14.62 ? 13  THR   C OG1  1 
ATOM   3438 C  CG2  . THR   C 1 9   ? 20.639  -27.751 10.026  1.00 14.96 ? 13  THR   C CG2  1 
ATOM   3439 N  N    . LEU   C 1 10  ? 21.308  -30.050 7.631   1.00 12.49 ? 14  LEU   C N    1 
ATOM   3440 C  CA   . LEU   C 1 10  ? 20.578  -31.298 7.504   1.00 13.10 ? 14  LEU   C CA   1 
ATOM   3441 C  C    . LEU   C 1 10  ? 19.944  -31.592 8.855   1.00 12.43 ? 14  LEU   C C    1 
ATOM   3442 O  O    . LEU   C 1 10  ? 20.628  -31.613 9.877   1.00 13.27 ? 14  LEU   C O    1 
ATOM   3443 C  CB   . LEU   C 1 10  ? 21.488  -32.430 7.050   1.00 14.79 ? 14  LEU   C CB   1 
ATOM   3444 C  CG   . LEU   C 1 10  ? 21.637  -32.580 5.525   1.00 18.11 ? 14  LEU   C CG   1 
ATOM   3445 C  CD1  . LEU   C 1 10  ? 22.023  -31.349 4.772   1.00 20.42 ? 14  LEU   C CD1  1 
ATOM   3446 C  CD2  . LEU   C 1 10  ? 22.585  -33.739 5.245   1.00 20.06 ? 14  LEU   C CD2  1 
ATOM   3447 N  N    . ILE   C 1 11  ? 18.627  -31.762 8.863   1.00 12.22 ? 15  ILE   C N    1 
ATOM   3448 C  CA   . ILE   C 1 11  ? 17.924  -32.070 10.091  1.00 12.68 ? 15  ILE   C CA   1 
ATOM   3449 C  C    . ILE   C 1 11  ? 17.483  -33.526 10.009  1.00 12.54 ? 15  ILE   C C    1 
ATOM   3450 O  O    . ILE   C 1 11  ? 16.486  -33.837 9.365   1.00 12.87 ? 15  ILE   C O    1 
ATOM   3451 C  CB   . ILE   C 1 11  ? 16.752  -31.112 10.349  1.00 14.98 ? 15  ILE   C CB   1 
ATOM   3452 C  CG1  . ILE   C 1 11  ? 17.206  -29.636 10.346  1.00 17.49 ? 15  ILE   C CG1  1 
ATOM   3453 C  CG2  . ILE   C 1 11  ? 16.048  -31.477 11.653  1.00 15.86 ? 15  ILE   C CG2  1 
ATOM   3454 C  CD1  . ILE   C 1 11  ? 16.956  -28.932 9.041   1.00 20.60 ? 15  ILE   C CD1  1 
ATOM   3455 N  N    . PHE   C 1 12  ? 18.286  -34.401 10.629  1.00 11.98 ? 16  PHE   C N    1 
ATOM   3456 C  CA   . PHE   C 1 12  ? 17.938  -35.805 10.747  1.00 12.35 ? 16  PHE   C CA   1 
ATOM   3457 C  C    . PHE   C 1 12  ? 16.691  -35.875 11.615  1.00 11.58 ? 16  PHE   C C    1 
ATOM   3458 O  O    . PHE   C 1 12  ? 16.618  -35.253 12.671  1.00 12.30 ? 16  PHE   C O    1 
ATOM   3459 C  CB   . PHE   C 1 12  ? 19.141  -36.592 11.281  1.00 12.80 ? 16  PHE   C CB   1 
ATOM   3460 C  CG   . PHE   C 1 12  ? 20.302  -36.549 10.300  1.00 13.60 ? 16  PHE   C CG   1 
ATOM   3461 C  CD1  . PHE   C 1 12  ? 20.406  -37.485 9.277   1.00 14.32 ? 16  PHE   C CD1  1 
ATOM   3462 C  CD2  . PHE   C 1 12  ? 21.253  -35.537 10.365  1.00 14.33 ? 16  PHE   C CD2  1 
ATOM   3463 C  CE1  . PHE   C 1 12  ? 21.431  -37.395 8.342   1.00 14.93 ? 16  PHE   C CE1  1 
ATOM   3464 C  CE2  . PHE   C 1 12  ? 22.289  -35.478 9.449   1.00 15.03 ? 16  PHE   C CE2  1 
ATOM   3465 C  CZ   . PHE   C 1 12  ? 22.375  -36.406 8.445   1.00 15.30 ? 16  PHE   C CZ   1 
ATOM   3466 N  N    . PHE   C 1 13  ? 15.705  -36.643 11.157  1.00 11.57 ? 17  PHE   C N    1 
ATOM   3467 C  CA   . PHE   C 1 13  ? 14.357  -36.540 11.681  1.00 11.80 ? 17  PHE   C CA   1 
ATOM   3468 C  C    . PHE   C 1 13  ? 13.747  -37.926 11.764  1.00 12.01 ? 17  PHE   C C    1 
ATOM   3469 O  O    . PHE   C 1 13  ? 13.838  -38.696 10.820  1.00 12.46 ? 17  PHE   C O    1 
ATOM   3470 C  CB   . PHE   C 1 13  ? 13.552  -35.651 10.732  1.00 12.18 ? 17  PHE   C CB   1 
ATOM   3471 C  CG   . PHE   C 1 13  ? 12.080  -35.460 11.059  1.00 11.93 ? 17  PHE   C CG   1 
ATOM   3472 C  CD1  . PHE   C 1 13  ? 11.672  -35.112 12.343  1.00 12.77 ? 17  PHE   C CD1  1 
ATOM   3473 C  CD2  . PHE   C 1 13  ? 11.099  -35.604 10.080  1.00 12.86 ? 17  PHE   C CD2  1 
ATOM   3474 C  CE1  . PHE   C 1 13  ? 10.326  -34.932 12.636  1.00 12.88 ? 17  PHE   C CE1  1 
ATOM   3475 C  CE2  . PHE   C 1 13  ? 9.761   -35.405 10.383  1.00 13.21 ? 17  PHE   C CE2  1 
ATOM   3476 C  CZ   . PHE   C 1 13  ? 9.377   -35.074 11.648  1.00 13.01 ? 17  PHE   C CZ   1 
ATOM   3477 N  N    . ASP   C 1 14  ? 13.111  -38.214 12.902  1.00 11.84 ? 18  ASP   C N    1 
ATOM   3478 C  CA   . ASP   C 1 14  ? 12.370  -39.447 13.045  1.00 12.29 ? 18  ASP   C CA   1 
ATOM   3479 C  C    . ASP   C 1 14  ? 11.217  -39.233 14.006  1.00 11.70 ? 18  ASP   C C    1 
ATOM   3480 O  O    . ASP   C 1 14  ? 11.377  -38.563 15.027  1.00 11.83 ? 18  ASP   C O    1 
ATOM   3481 C  CB   . ASP   C 1 14  ? 13.234  -40.587 13.546  1.00 12.84 ? 18  ASP   C CB   1 
ATOM   3482 C  CG   . ASP   C 1 14  ? 12.571  -41.939 13.379  1.00 14.36 ? 18  ASP   C CG   1 
ATOM   3483 O  OD1  . ASP   C 1 14  ? 12.457  -42.397 12.215  1.00 15.14 ? 18  ASP   C OD1  1 
ATOM   3484 O  OD2  . ASP   C 1 14  ? 12.108  -42.476 14.405  1.00 15.55 ? 18  ASP   C OD2  1 
ATOM   3485 N  N    . MET   C 1 15  ? 10.086  -39.858 13.686  1.00 11.97 ? 19  MET   C N    1 
ATOM   3486 C  CA   . MET   C 1 15  ? 8.942   -39.858 14.579  1.00 11.74 ? 19  MET   C CA   1 
ATOM   3487 C  C    . MET   C 1 15  ? 8.489   -41.281 14.857  1.00 11.89 ? 19  MET   C C    1 
ATOM   3488 O  O    . MET   C 1 15  ? 8.662   -42.181 14.041  1.00 12.49 ? 19  MET   C O    1 
ATOM   3489 C  CB   . MET   C 1 15  ? 7.778   -39.049 13.996  1.00 12.66 ? 19  MET   C CB   1 
ATOM   3490 C  CG   . MET   C 1 15  ? 8.172   -37.610 13.755  1.00 13.30 ? 19  MET   C CG   1 
ATOM   3491 S  SD   . MET   C 1 15  ? 6.795   -36.446 13.691  1.00 15.08 ? 19  MET   C SD   1 
ATOM   3492 C  CE   . MET   C 1 15  ? 5.942   -37.017 12.223  1.00 14.66 ? 19  MET   C CE   1 
ATOM   3493 N  N    A GLU   C 1 16  ? 7.947   -41.476 16.060  0.50 11.28 ? 20  GLU   C N    1 
ATOM   3494 N  N    B GLU   C 1 16  ? 7.909   -41.463 16.040  0.50 11.89 ? 20  GLU   C N    1 
ATOM   3495 C  CA   A GLU   C 1 16  ? 7.152   -42.653 16.365  0.50 10.99 ? 20  GLU   C CA   1 
ATOM   3496 C  CA   B GLU   C 1 16  ? 7.147   -42.661 16.333  0.50 12.08 ? 20  GLU   C CA   1 
ATOM   3497 C  C    A GLU   C 1 16  ? 5.682   -42.253 16.279  0.50 10.94 ? 20  GLU   C C    1 
ATOM   3498 C  C    B GLU   C 1 16  ? 5.673   -42.279 16.359  0.50 11.58 ? 20  GLU   C C    1 
ATOM   3499 O  O    A GLU   C 1 16  ? 5.338   -41.094 16.508  0.50 11.14 ? 20  GLU   C O    1 
ATOM   3500 O  O    B GLU   C 1 16  ? 5.322   -41.164 16.741  0.50 11.82 ? 20  GLU   C O    1 
ATOM   3501 C  CB   A GLU   C 1 16  ? 7.449   -43.177 17.773  0.50 11.52 ? 20  GLU   C CB   1 
ATOM   3502 C  CB   B GLU   C 1 16  ? 7.646   -43.264 17.645  0.50 13.71 ? 20  GLU   C CB   1 
ATOM   3503 C  CG   A GLU   C 1 16  ? 8.921   -43.507 18.026  0.50 12.17 ? 20  GLU   C CG   1 
ATOM   3504 C  CG   B GLU   C 1 16  ? 9.113   -43.675 17.554  0.50 15.66 ? 20  GLU   C CG   1 
ATOM   3505 C  CD   A GLU   C 1 16  ? 9.491   -44.758 17.361  0.50 13.33 ? 20  GLU   C CD   1 
ATOM   3506 C  CD   B GLU   C 1 16  ? 9.663   -44.452 18.732  0.50 18.18 ? 20  GLU   C CD   1 
ATOM   3507 O  OE1  A GLU   C 1 16  ? 8.736   -45.494 16.693  0.50 13.95 ? 20  GLU   C OE1  1 
ATOM   3508 O  OE1  B GLU   C 1 16  ? 9.056   -44.368 19.822  0.50 20.57 ? 20  GLU   C OE1  1 
ATOM   3509 O  OE2  A GLU   C 1 16  ? 10.722  -44.988 17.496  0.50 14.64 ? 20  GLU   C OE2  1 
ATOM   3510 O  OE2  B GLU   C 1 16  ? 10.675  -45.171 18.553  0.50 20.74 ? 20  GLU   C OE2  1 
ATOM   3511 N  N    . ALA   C 1 17  ? 4.820   -43.217 15.956  1.00 11.27 ? 21  ALA   C N    1 
ATOM   3512 C  CA   . ALA   C 1 17  ? 3.395   -42.968 15.856  1.00 11.25 ? 21  ALA   C CA   1 
ATOM   3513 C  C    . ALA   C 1 17  ? 2.604   -44.155 16.402  1.00 11.64 ? 21  ALA   C C    1 
ATOM   3514 O  O    . ALA   C 1 17  ? 3.153   -45.220 16.703  1.00 13.42 ? 21  ALA   C O    1 
ATOM   3515 C  CB   . ALA   C 1 17  ? 3.040   -42.684 14.408  1.00 11.69 ? 21  ALA   C CB   1 
ATOM   3516 N  N    . THR   C 1 18  ? 1.287   -43.963 16.485  1.00 11.62 ? 22  THR   C N    1 
ATOM   3517 C  CA   . THR   C 1 18  ? 0.379   -44.951 17.047  1.00 11.99 ? 22  THR   C CA   1 
ATOM   3518 C  C    . THR   C 1 18  ? 0.230   -46.186 16.162  1.00 12.22 ? 22  THR   C C    1 
ATOM   3519 O  O    . THR   C 1 18  ? -0.244  -47.221 16.633  1.00 13.61 ? 22  THR   C O    1 
ATOM   3520 C  CB   . THR   C 1 18  ? -0.996  -44.322 17.291  1.00 12.32 ? 22  THR   C CB   1 
ATOM   3521 O  OG1  . THR   C 1 18  ? -1.445  -43.728 16.074  1.00 12.23 ? 22  THR   C OG1  1 
ATOM   3522 C  CG2  . THR   C 1 18  ? -0.974  -43.271 18.382  1.00 12.19 ? 22  THR   C CG2  1 
ATOM   3523 N  N    . GLY   C 1 19  ? 0.550   -46.059 14.876  1.00 11.67 ? 23  GLY   C N    1 
ATOM   3524 C  CA   . GLY   C 1 19  ? 0.395   -47.148 13.929  1.00 11.84 ? 23  GLY   C CA   1 
ATOM   3525 C  C    . GLY   C 1 19  ? 0.966   -46.747 12.572  1.00 12.26 ? 23  GLY   C C    1 
ATOM   3526 O  O    . GLY   C 1 19  ? 1.572   -45.686 12.442  1.00 12.54 ? 23  GLY   C O    1 
ATOM   3527 N  N    . LEU   C 1 20  ? 0.732   -47.588 11.568  1.00 13.15 ? 24  LEU   C N    1 
ATOM   3528 C  CA   . LEU   C 1 20  ? 1.161   -47.308 10.209  1.00 13.66 ? 24  LEU   C CA   1 
ATOM   3529 C  C    . LEU   C 1 20  ? 0.159   -46.387 9.514   1.00 13.98 ? 24  LEU   C C    1 
ATOM   3530 O  O    . LEU   C 1 20  ? -0.951  -46.178 9.998   1.00 13.87 ? 24  LEU   C O    1 
ATOM   3531 C  CB   . LEU   C 1 20  ? 1.363   -48.628 9.470   1.00 14.01 ? 24  LEU   C CB   1 
ATOM   3532 C  CG   . LEU   C 1 20  ? 2.394   -49.569 10.096  1.00 15.17 ? 24  LEU   C CG   1 
ATOM   3533 C  CD1  . LEU   C 1 20  ? 2.460   -50.872 9.327   1.00 16.16 ? 24  LEU   C CD1  1 
ATOM   3534 C  CD2  . LEU   C 1 20  ? 3.769   -48.913 10.168  1.00 16.89 ? 24  LEU   C CD2  1 
ATOM   3535 N  N    . PRO   C 1 21  ? 0.541   -45.782 8.366   1.00 14.53 ? 25  PRO   C N    1 
ATOM   3536 C  CA   . PRO   C 1 21  ? -0.307  -44.783 7.704   1.00 15.04 ? 25  PRO   C CA   1 
ATOM   3537 C  C    . PRO   C 1 21  ? -1.782  -45.124 7.466   1.00 15.65 ? 25  PRO   C C    1 
ATOM   3538 O  O    . PRO   C 1 21  ? -2.651  -44.263 7.619   1.00 16.84 ? 25  PRO   C O    1 
ATOM   3539 C  CB   . PRO   C 1 21  ? 0.472   -44.525 6.399   1.00 15.15 ? 25  PRO   C CB   1 
ATOM   3540 C  CG   . PRO   C 1 21  ? 1.915   -44.711 6.805   1.00 15.28 ? 25  PRO   C CG   1 
ATOM   3541 C  CD   . PRO   C 1 21  ? 1.875   -45.902 7.753   1.00 15.00 ? 25  PRO   C CD   1 
ATOM   3542 N  N    A SER   C 1 22  ? -2.049  -46.389 7.123   0.50 15.87 ? 26  SER   C N    1 
ATOM   3543 N  N    B SER   C 1 22  ? -2.076  -46.384 7.122   0.50 15.77 ? 26  SER   C N    1 
ATOM   3544 C  CA   A SER   C 1 22  ? -3.400  -46.846 6.843   0.50 16.10 ? 26  SER   C CA   1 
ATOM   3545 C  CA   B SER   C 1 22  ? -3.443  -46.786 6.832   0.50 16.00 ? 26  SER   C CA   1 
ATOM   3546 C  C    A SER   C 1 22  ? -4.305  -46.761 8.075   0.50 15.43 ? 26  SER   C C    1 
ATOM   3547 C  C    B SER   C 1 22  ? -4.301  -46.896 8.095   0.50 15.19 ? 26  SER   C C    1 
ATOM   3548 O  O    A SER   C 1 22  ? -5.525  -46.774 7.939   0.50 15.82 ? 26  SER   C O    1 
ATOM   3549 O  O    B SER   C 1 22  ? -5.480  -47.229 8.006   0.50 15.16 ? 26  SER   C O    1 
ATOM   3550 C  CB   A SER   C 1 22  ? -3.368  -48.236 6.273   0.50 16.75 ? 26  SER   C CB   1 
ATOM   3551 C  CB   B SER   C 1 22  ? -3.466  -48.072 6.062   0.50 16.58 ? 26  SER   C CB   1 
ATOM   3552 O  OG   A SER   C 1 22  ? -2.671  -48.244 5.031   0.50 17.73 ? 26  SER   C OG   1 
ATOM   3553 O  OG   B SER   C 1 22  ? -2.791  -49.092 6.781   0.50 17.40 ? 26  SER   C OG   1 
ATOM   3554 N  N    . SER   C 1 23  ? -3.719  -46.638 9.272   1.00 14.98 ? 27  SER   C N    1 
ATOM   3555 C  CA   . SER   C 1 23  ? -4.497  -46.535 10.505  1.00 14.61 ? 27  SER   C CA   1 
ATOM   3556 C  C    . SER   C 1 23  ? -4.853  -45.090 10.894  1.00 14.98 ? 27  SER   C C    1 
ATOM   3557 O  O    . SER   C 1 23  ? -5.469  -44.888 11.939  1.00 15.73 ? 27  SER   C O    1 
ATOM   3558 C  CB   . SER   C 1 23  ? -3.743  -47.174 11.636  1.00 14.46 ? 27  SER   C CB   1 
ATOM   3559 O  OG   . SER   C 1 23  ? -2.629  -46.383 12.039  1.00 14.06 ? 27  SER   C OG   1 
ATOM   3560 N  N    A ARG   C 1 24  ? -4.464  -44.105 10.071  0.50 14.78 ? 28  ARG   C N    1 
ATOM   3561 N  N    B ARG   C 1 24  ? -4.474  -44.100 10.072  0.50 15.01 ? 28  ARG   C N    1 
ATOM   3562 C  CA   A ARG   C 1 24  ? -4.636  -42.691 10.389  0.50 15.00 ? 28  ARG   C CA   1 
ATOM   3563 C  CA   B ARG   C 1 24  ? -4.648  -42.687 10.399  0.50 15.47 ? 28  ARG   C CA   1 
ATOM   3564 C  C    A ARG   C 1 24  ? -3.911  -42.396 11.701  0.50 14.45 ? 28  ARG   C C    1 
ATOM   3565 C  C    B ARG   C 1 24  ? -3.912  -42.395 11.706  0.50 14.63 ? 28  ARG   C C    1 
ATOM   3566 O  O    A ARG   C 1 24  ? -4.508  -42.015 12.710  0.50 14.47 ? 28  ARG   C O    1 
ATOM   3567 O  O    B ARG   C 1 24  ? -4.502  -42.008 12.717  0.50 14.64 ? 28  ARG   C O    1 
ATOM   3568 C  CB   A ARG   C 1 24  ? -6.107  -42.267 10.474  0.50 16.19 ? 28  ARG   C CB   1 
ATOM   3569 C  CB   B ARG   C 1 24  ? -6.119  -42.256 10.490  0.50 17.17 ? 28  ARG   C CB   1 
ATOM   3570 C  CG   A ARG   C 1 24  ? -6.317  -40.770 10.303  0.50 17.77 ? 28  ARG   C CG   1 
ATOM   3571 C  CG   B ARG   C 1 24  ? -6.316  -40.758 10.674  0.50 19.45 ? 28  ARG   C CG   1 
ATOM   3572 C  CD   A ARG   C 1 24  ? -7.761  -40.359 10.571  0.50 19.00 ? 28  ARG   C CD   1 
ATOM   3573 C  CD   B ARG   C 1 24  ? -7.770  -40.372 10.933  0.50 21.49 ? 28  ARG   C CD   1 
ATOM   3574 N  NE   A ARG   C 1 24  ? -7.983  -38.943 10.259  0.50 19.77 ? 28  ARG   C NE   1 
ATOM   3575 N  NE   B ARG   C 1 24  ? -7.893  -39.021 11.493  0.50 23.79 ? 28  ARG   C NE   1 
ATOM   3576 C  CZ   A ARG   C 1 24  ? -7.659  -37.915 11.035  0.50 20.95 ? 28  ARG   C CZ   1 
ATOM   3577 C  CZ   B ARG   C 1 24  ? -8.312  -37.941 10.845  0.50 26.15 ? 28  ARG   C CZ   1 
ATOM   3578 N  NH1  A ARG   C 1 24  ? -7.824  -36.682 10.585  0.50 21.73 ? 28  ARG   C NH1  1 
ATOM   3579 N  NH1  B ARG   C 1 24  ? -8.614  -38.001 9.558   0.50 27.23 ? 28  ARG   C NH1  1 
ATOM   3580 N  NH2  A ARG   C 1 24  ? -7.172  -38.112 12.249  0.50 21.57 ? 28  ARG   C NH2  1 
ATOM   3581 N  NH2  B ARG   C 1 24  ? -8.405  -36.790 11.489  0.50 27.46 ? 28  ARG   C NH2  1 
ATOM   3582 N  N    . PRO   C 1 25  ? -2.579  -42.603 11.737  1.00 13.31 ? 29  PRO   C N    1 
ATOM   3583 C  CA   . PRO   C 1 25  ? -1.844  -42.556 12.995  1.00 12.93 ? 29  PRO   C CA   1 
ATOM   3584 C  C    . PRO   C 1 25  ? -1.582  -41.144 13.490  1.00 13.28 ? 29  PRO   C C    1 
ATOM   3585 O  O    . PRO   C 1 25  ? -1.658  -40.181 12.732  1.00 13.99 ? 29  PRO   C O    1 
ATOM   3586 C  CB   . PRO   C 1 25  ? -0.535  -43.254 12.623  1.00 12.62 ? 29  PRO   C CB   1 
ATOM   3587 C  CG   . PRO   C 1 25  ? -0.339  -42.842 11.181  1.00 12.95 ? 29  PRO   C CG   1 
ATOM   3588 C  CD   . PRO   C 1 25  ? -1.723  -42.889 10.575  1.00 13.24 ? 29  PRO   C CD   1 
ATOM   3589 N  N    . GLU   C 1 26  ? -1.223  -41.068 14.772  1.00 12.87 ? 30  GLU   C N    1 
ATOM   3590 C  CA   . GLU   C 1 26  ? -0.815  -39.824 15.391  1.00 13.93 ? 30  GLU   C CA   1 
ATOM   3591 C  C    . GLU   C 1 26  ? 0.563   -39.986 16.007  1.00 12.68 ? 30  GLU   C C    1 
ATOM   3592 O  O    . GLU   C 1 26  ? 0.950   -41.074 16.399  1.00 12.68 ? 30  GLU   C O    1 
ATOM   3593 C  CB   . GLU   C 1 26  ? -1.849  -39.406 16.423  1.00 16.26 ? 30  GLU   C CB   1 
ATOM   3594 C  CG   . GLU   C 1 26  ? -3.172  -39.148 15.715  1.00 19.24 ? 30  GLU   C CG   1 
ATOM   3595 C  CD   . GLU   C 1 26  ? -4.259  -38.447 16.466  1.00 23.22 ? 30  GLU   C CD   1 
ATOM   3596 O  OE1  . GLU   C 1 26  ? -3.962  -37.764 17.463  1.00 26.44 ? 30  GLU   C OE1  1 
ATOM   3597 O  OE2  . GLU   C 1 26  ? -5.411  -38.607 16.015  1.00 27.46 ? 30  GLU   C OE2  1 
ATOM   3598 N  N    . VAL   C 1 27  ? 1.274   -38.863 16.087  1.00 12.85 ? 31  VAL   C N    1 
ATOM   3599 C  CA   . VAL   C 1 27  ? 2.621   -38.824 16.620  1.00 12.14 ? 31  VAL   C CA   1 
ATOM   3600 C  C    . VAL   C 1 27  ? 2.618   -39.139 18.112  1.00 11.54 ? 31  VAL   C C    1 
ATOM   3601 O  O    . VAL   C 1 27  ? 1.803   -38.599 18.864  1.00 12.96 ? 31  VAL   C O    1 
ATOM   3602 C  CB   . VAL   C 1 27  ? 3.256   -37.447 16.357  1.00 12.98 ? 31  VAL   C CB   1 
ATOM   3603 C  CG1  . VAL   C 1 27  ? 4.603   -37.330 17.039  1.00 13.12 ? 31  VAL   C CG1  1 
ATOM   3604 C  CG2  . VAL   C 1 27  ? 3.408   -37.176 14.867  1.00 13.60 ? 31  VAL   C CG2  1 
ATOM   3605 N  N    . THR   C 1 28  ? 3.571   -39.995 18.533  1.00 11.01 ? 32  THR   C N    1 
ATOM   3606 C  CA   . THR   C 1 28  ? 3.835   -40.276 19.943  1.00 11.23 ? 32  THR   C CA   1 
ATOM   3607 C  C    . THR   C 1 28  ? 5.224   -39.795 20.364  1.00 10.77 ? 32  THR   C C    1 
ATOM   3608 O  O    . THR   C 1 28  ? 5.482   -39.639 21.554  1.00 11.01 ? 32  THR   C O    1 
ATOM   3609 C  CB   . THR   C 1 28  ? 3.714   -41.775 20.234  1.00 11.68 ? 32  THR   C CB   1 
ATOM   3610 O  OG1  . THR   C 1 28  ? 4.647   -42.454 19.398  1.00 12.37 ? 32  THR   C OG1  1 
ATOM   3611 C  CG2  . THR   C 1 28  ? 2.315   -42.311 19.997  1.00 12.75 ? 32  THR   C CG2  1 
ATOM   3612 N  N    . GLU   C 1 29  ? 6.142   -39.617 19.413  1.00 10.57 ? 33  GLU   C N    1 
ATOM   3613 C  CA   . GLU   C 1 29  ? 7.474   -39.143 19.750  1.00 11.06 ? 33  GLU   C CA   1 
ATOM   3614 C  C    . GLU   C 1 29  ? 8.086   -38.515 18.511  1.00 10.90 ? 33  GLU   C C    1 
ATOM   3615 O  O    . GLU   C 1 29  ? 7.807   -38.952 17.401  1.00 11.23 ? 33  GLU   C O    1 
ATOM   3616 C  CB   . GLU   C 1 29  ? 8.363   -40.281 20.265  1.00 12.20 ? 33  GLU   C CB   1 
ATOM   3617 C  CG   . GLU   C 1 29  ? 9.602   -39.815 21.028  1.00 13.54 ? 33  GLU   C CG   1 
ATOM   3618 C  CD   . GLU   C 1 29  ? 10.517  -40.931 21.514  1.00 15.41 ? 33  GLU   C CD   1 
ATOM   3619 O  OE1  . GLU   C 1 29  ? 10.543  -41.997 20.863  1.00 16.15 ? 33  GLU   C OE1  1 
ATOM   3620 O  OE2  . GLU   C 1 29  ? 11.203  -40.743 22.554  1.00 17.61 ? 33  GLU   C OE2  1 
ATOM   3621 N  N    . LEU   C 1 30  ? 8.951   -37.518 18.710  1.00 10.87 ? 34  LEU   C N    1 
ATOM   3622 C  CA   . LEU   C 1 30  ? 9.700   -36.969 17.595  1.00 11.58 ? 34  LEU   C CA   1 
ATOM   3623 C  C    . LEU   C 1 30  ? 11.107  -36.623 18.043  1.00 11.42 ? 34  LEU   C C    1 
ATOM   3624 O  O    . LEU   C 1 30  ? 11.341  -36.291 19.203  1.00 12.55 ? 34  LEU   C O    1 
ATOM   3625 C  CB   . LEU   C 1 30  ? 8.985   -35.774 16.985  1.00 13.12 ? 34  LEU   C CB   1 
ATOM   3626 C  CG   . LEU   C 1 30  ? 8.764   -34.565 17.890  1.00 14.23 ? 34  LEU   C CG   1 
ATOM   3627 C  CD1  . LEU   C 1 30  ? 9.949   -33.613 17.889  1.00 14.55 ? 34  LEU   C CD1  1 
ATOM   3628 C  CD2  . LEU   C 1 30  ? 7.493   -33.843 17.473  1.00 15.91 ? 34  LEU   C CD2  1 
ATOM   3629 N  N    . CYS   C 1 31  ? 12.031  -36.688 17.089  1.00 10.88 ? 35  CYS   C N    1 
ATOM   3630 C  CA   . CYS   C 1 31  ? 13.397  -36.263 17.318  1.00 11.35 ? 35  CYS   C CA   1 
ATOM   3631 C  C    . CYS   C 1 31  ? 13.918  -35.551 16.074  1.00 11.36 ? 35  CYS   C C    1 
ATOM   3632 O  O    . CYS   C 1 31  ? 13.742  -36.045 14.958  1.00 11.08 ? 35  CYS   C O    1 
ATOM   3633 C  CB   . CYS   C 1 31  ? 14.294  -37.434 17.689  1.00 12.44 ? 35  CYS   C CB   1 
ATOM   3634 S  SG   . CYS   C 1 31  ? 16.015  -36.927 17.973  1.00 15.40 ? 35  CYS   C SG   1 
ATOM   3635 N  N    . LEU   C 1 32  ? 14.506  -34.374 16.304  1.00 11.31 ? 36  LEU   C N    1 
ATOM   3636 C  CA   . LEU   C 1 32  ? 15.218  -33.612 15.294  1.00 11.77 ? 36  LEU   C CA   1 
ATOM   3637 C  C    . LEU   C 1 32  ? 16.662  -33.483 15.760  1.00 11.37 ? 36  LEU   C C    1 
ATOM   3638 O  O    . LEU   C 1 32  ? 16.902  -33.128 16.911  1.00 12.06 ? 36  LEU   C O    1 
ATOM   3639 C  CB   . LEU   C 1 32  ? 14.643  -32.207 15.103  1.00 12.73 ? 36  LEU   C CB   1 
ATOM   3640 C  CG   . LEU   C 1 32  ? 13.281  -32.082 14.418  1.00 14.93 ? 36  LEU   C CG   1 
ATOM   3641 C  CD1  . LEU   C 1 32  ? 12.148  -32.713 15.166  1.00 16.01 ? 36  LEU   C CD1  1 
ATOM   3642 C  CD2  . LEU   C 1 32  ? 12.984  -30.610 14.208  1.00 16.69 ? 36  LEU   C CD2  1 
ATOM   3643 N  N    A LEU   C 1 33  ? 17.595  -33.740 14.846  0.50 11.74 ? 37  LEU   C N    1 
ATOM   3644 N  N    B LEU   C 1 33  ? 17.610  -33.742 14.858  0.50 11.40 ? 37  LEU   C N    1 
ATOM   3645 C  CA   A LEU   C 1 33  ? 19.014  -33.567 15.089  0.50 12.12 ? 37  LEU   C CA   1 
ATOM   3646 C  CA   B LEU   C 1 33  ? 19.020  -33.537 15.139  0.50 11.58 ? 37  LEU   C CA   1 
ATOM   3647 C  C    A LEU   C 1 33  ? 19.560  -32.738 13.932  0.50 11.76 ? 37  LEU   C C    1 
ATOM   3648 C  C    B LEU   C 1 33  ? 19.613  -32.758 13.970  0.50 11.50 ? 37  LEU   C C    1 
ATOM   3649 O  O    A LEU   C 1 33  ? 19.617  -33.223 12.801  0.50 11.88 ? 37  LEU   C O    1 
ATOM   3650 O  O    B LEU   C 1 33  ? 19.788  -33.305 12.881  0.50 11.87 ? 37  LEU   C O    1 
ATOM   3651 C  CB   A LEU   C 1 33  ? 19.681  -34.938 15.182  0.50 13.60 ? 37  LEU   C CB   1 
ATOM   3652 C  CB   B LEU   C 1 33  ? 19.737  -34.866 15.373  0.50 12.39 ? 37  LEU   C CB   1 
ATOM   3653 C  CG   A LEU   C 1 33  ? 21.138  -34.966 15.648  0.50 15.03 ? 37  LEU   C CG   1 
ATOM   3654 C  CG   B LEU   C 1 33  ? 21.135  -34.775 15.992  0.50 13.03 ? 37  LEU   C CG   1 
ATOM   3655 C  CD1  A LEU   C 1 33  ? 21.318  -34.314 17.004  0.50 15.75 ? 37  LEU   C CD1  1 
ATOM   3656 C  CD1  B LEU   C 1 33  ? 21.497  -36.104 16.639  0.50 12.97 ? 37  LEU   C CD1  1 
ATOM   3657 C  CD2  A LEU   C 1 33  ? 21.607  -36.412 15.696  0.50 15.75 ? 37  LEU   C CD2  1 
ATOM   3658 C  CD2  B LEU   C 1 33  ? 22.162  -34.380 14.955  0.50 13.47 ? 37  LEU   C CD2  1 
ATOM   3659 N  N    . ALA   C 1 34  ? 19.878  -31.468 14.215  1.00 11.29 ? 38  ALA   C N    1 
ATOM   3660 C  CA   . ALA   C 1 34  ? 20.325  -30.531 13.193  1.00 11.81 ? 38  ALA   C CA   1 
ATOM   3661 C  C    . ALA   C 1 34  ? 21.845  -30.512 13.136  1.00 12.11 ? 38  ALA   C C    1 
ATOM   3662 O  O    . ALA   C 1 34  ? 22.502  -30.263 14.147  1.00 12.67 ? 38  ALA   C O    1 
ATOM   3663 C  CB   . ALA   C 1 34  ? 19.783  -29.154 13.485  1.00 12.63 ? 38  ALA   C CB   1 
ATOM   3664 N  N    . VAL   C 1 35  ? 22.370  -30.749 11.933  1.00 12.71 ? 39  VAL   C N    1 
ATOM   3665 C  CA   . VAL   C 1 35  ? 23.797  -30.825 11.667  1.00 14.12 ? 39  VAL   C CA   1 
ATOM   3666 C  C    . VAL   C 1 35  ? 24.111  -29.842 10.537  1.00 13.05 ? 39  VAL   C C    1 
ATOM   3667 O  O    . VAL   C 1 35  ? 23.499  -29.899 9.476   1.00 13.25 ? 39  VAL   C O    1 
ATOM   3668 C  CB   . VAL   C 1 35  ? 24.121  -32.281 11.253  1.00 16.19 ? 39  VAL   C CB   1 
ATOM   3669 C  CG1  . VAL   C 1 35  ? 25.570  -32.448 10.837  1.00 18.32 ? 39  VAL   C CG1  1 
ATOM   3670 C  CG2  . VAL   C 1 35  ? 23.737  -33.309 12.319  1.00 17.05 ? 39  VAL   C CG2  1 
ATOM   3671 N  N    . HIS   C 1 36  ? 25.061  -28.926 10.750  1.00 12.69 ? 40  HIS   C N    1 
ATOM   3672 C  CA   . HIS   C 1 36  ? 25.490  -28.038 9.683   1.00 12.94 ? 40  HIS   C CA   1 
ATOM   3673 C  C    . HIS   C 1 36  ? 26.174  -28.854 8.588   1.00 12.91 ? 40  HIS   C C    1 
ATOM   3674 O  O    . HIS   C 1 36  ? 26.839  -29.844 8.865   1.00 13.30 ? 40  HIS   C O    1 
ATOM   3675 C  CB   . HIS   C 1 36  ? 26.454  -26.982 10.235  1.00 13.83 ? 40  HIS   C CB   1 
ATOM   3676 C  CG   . HIS   C 1 36  ? 26.766  -25.881 9.282   1.00 14.66 ? 40  HIS   C CG   1 
ATOM   3677 N  ND1  . HIS   C 1 36  ? 27.720  -25.966 8.295   1.00 16.02 ? 40  HIS   C ND1  1 
ATOM   3678 C  CD2  . HIS   C 1 36  ? 26.195  -24.681 9.140   1.00 16.21 ? 40  HIS   C CD2  1 
ATOM   3679 C  CE1  . HIS   C 1 36  ? 27.731  -24.832 7.603   1.00 17.01 ? 40  HIS   C CE1  1 
ATOM   3680 N  NE2  . HIS   C 1 36  ? 26.823  -24.031 8.116   1.00 16.44 ? 40  HIS   C NE2  1 
ATOM   3681 N  N    . ARG   C 1 37  ? 26.019  -28.418 7.335   1.00 12.86 ? 41  ARG   C N    1 
ATOM   3682 C  CA   . ARG   C 1 37  ? 26.562  -29.156 6.215   1.00 13.23 ? 41  ARG   C CA   1 
ATOM   3683 C  C    . ARG   C 1 37  ? 28.062  -29.395 6.383   1.00 13.95 ? 41  ARG   C C    1 
ATOM   3684 O  O    . ARG   C 1 37  ? 28.582  -30.389 5.876   1.00 15.02 ? 41  ARG   C O    1 
ATOM   3685 C  CB   . ARG   C 1 37  ? 26.271  -28.448 4.888   1.00 13.08 ? 41  ARG   C CB   1 
ATOM   3686 C  CG   . ARG   C 1 37  ? 26.885  -27.064 4.739   1.00 13.33 ? 41  ARG   C CG   1 
ATOM   3687 C  CD   . ARG   C 1 37  ? 26.710  -26.523 3.335   1.00 13.56 ? 41  ARG   C CD   1 
ATOM   3688 N  NE   . ARG   C 1 37  ? 27.448  -27.278 2.315   1.00 14.35 ? 41  ARG   C NE   1 
ATOM   3689 C  CZ   . ARG   C 1 37  ? 26.927  -28.006 1.335   1.00 14.57 ? 41  ARG   C CZ   1 
ATOM   3690 N  NH1  . ARG   C 1 37  ? 25.626  -28.278 1.275   1.00 14.51 ? 41  ARG   C NH1  1 
ATOM   3691 N  NH2  . ARG   C 1 37  ? 27.731  -28.494 0.405   1.00 16.06 ? 41  ARG   C NH2  1 
ATOM   3692 N  N    . CYS   C 1 38  ? 28.776  -28.485 7.055   1.00 14.85 ? 42  CYS   C N    1 
ATOM   3693 C  CA   . CYS   C 1 38  ? 30.224  -28.613 7.164   1.00 16.57 ? 42  CYS   C CA   1 
ATOM   3694 C  C    . CYS   C 1 38  ? 30.640  -29.926 7.833   1.00 17.12 ? 42  CYS   C C    1 
ATOM   3695 O  O    . CYS   C 1 38  ? 31.722  -30.440 7.557   1.00 18.53 ? 42  CYS   C O    1 
ATOM   3696 C  CB   . CYS   C 1 38  ? 30.840  -27.380 7.826   1.00 17.70 ? 42  CYS   C CB   1 
ATOM   3697 S  SG   . CYS   C 1 38  ? 30.512  -27.198 9.597   1.00 20.93 ? 42  CYS   C SG   1 
ATOM   3698 N  N    . ALA   C 1 39  ? 29.789  -30.488 8.703   1.00 15.97 ? 43  ALA   C N    1 
ATOM   3699 C  CA   . ALA   C 1 39  ? 30.113  -31.733 9.381   1.00 16.98 ? 43  ALA   C CA   1 
ATOM   3700 C  C    . ALA   C 1 39  ? 30.197  -32.910 8.408   1.00 17.55 ? 43  ALA   C C    1 
ATOM   3701 O  O    . ALA   C 1 39  ? 30.857  -33.906 8.722   1.00 19.41 ? 43  ALA   C O    1 
ATOM   3702 C  CB   . ALA   C 1 39  ? 29.107  -32.009 10.475  1.00 17.20 ? 43  ALA   C CB   1 
ATOM   3703 N  N    . LEU   C 1 40  ? 29.494  -32.806 7.266   1.00 17.52 ? 44  LEU   C N    1 
ATOM   3704 C  CA   . LEU   C 1 40  ? 29.489  -33.829 6.228   1.00 18.65 ? 44  LEU   C CA   1 
ATOM   3705 C  C    . LEU   C 1 40  ? 30.409  -33.448 5.068   1.00 18.64 ? 44  LEU   C C    1 
ATOM   3706 O  O    . LEU   C 1 40  ? 31.014  -34.329 4.463   1.00 19.71 ? 44  LEU   C O    1 
ATOM   3707 C  CB   . LEU   C 1 40  ? 28.085  -34.109 5.697   1.00 20.76 ? 44  LEU   C CB   1 
ATOM   3708 C  CG   . LEU   C 1 40  ? 27.083  -34.749 6.662   1.00 24.97 ? 44  LEU   C CG   1 
ATOM   3709 C  CD1  . LEU   C 1 40  ? 25.956  -35.379 5.849   1.00 27.33 ? 44  LEU   C CD1  1 
ATOM   3710 C  CD2  . LEU   C 1 40  ? 27.679  -35.777 7.581   1.00 27.07 ? 44  LEU   C CD2  1 
ATOM   3711 N  N    . GLU   C 1 41  ? 30.463  -32.158 4.730   1.00 17.61 ? 45  GLU   C N    1 
ATOM   3712 C  CA   . GLU   C 1 41  ? 31.212  -31.679 3.579   1.00 18.38 ? 45  GLU   C CA   1 
ATOM   3713 C  C    . GLU   C 1 41  ? 32.707  -31.717 3.873   1.00 20.14 ? 45  GLU   C C    1 
ATOM   3714 O  O    . GLU   C 1 41  ? 33.512  -31.982 2.980   1.00 21.98 ? 45  GLU   C O    1 
ATOM   3715 C  CB   . GLU   C 1 41  ? 30.777  -30.239 3.325   1.00 19.23 ? 45  GLU   C CB   1 
ATOM   3716 C  CG   . GLU   C 1 41  ? 31.399  -29.589 2.097   1.00 19.38 ? 45  GLU   C CG   1 
ATOM   3717 C  CD   . GLU   C 1 41  ? 30.758  -28.247 1.797   1.00 19.62 ? 45  GLU   C CD   1 
ATOM   3718 O  OE1  . GLU   C 1 41  ? 30.641  -27.923 0.605   1.00 21.13 ? 45  GLU   C OE1  1 
ATOM   3719 O  OE2  . GLU   C 1 41  ? 30.361  -27.539 2.755   1.00 20.09 ? 45  GLU   C OE2  1 
ATOM   3720 N  N    . SER   C 1 42  ? 33.045  -31.390 5.127   1.00 22.25 ? 46  SER   C N    1 
ATOM   3721 C  CA   . SER   C 1 42  ? 34.412  -31.228 5.593   1.00 24.45 ? 46  SER   C CA   1 
ATOM   3722 C  C    . SER   C 1 42  ? 34.559  -31.972 6.915   1.00 26.08 ? 46  SER   C C    1 
ATOM   3723 O  O    . SER   C 1 42  ? 34.786  -31.354 7.955   1.00 27.41 ? 46  SER   C O    1 
ATOM   3724 C  CB   . SER   C 1 42  ? 34.772  -29.762 5.748   1.00 25.50 ? 46  SER   C CB   1 
ATOM   3725 O  OG   . SER   C 1 42  ? 34.585  -29.031 4.539   1.00 25.78 ? 46  SER   C OG   1 
ATOM   3726 N  N    . PRO   C 1 43  ? 34.407  -33.316 6.911   1.00 27.65 ? 47  PRO   C N    1 
ATOM   3727 C  CA   . PRO   C 1 43  ? 34.375  -34.091 8.152   1.00 30.36 ? 47  PRO   C CA   1 
ATOM   3728 C  C    . PRO   C 1 43  ? 35.758  -34.102 8.796   1.00 33.85 ? 47  PRO   C C    1 
ATOM   3729 O  O    . PRO   C 1 43  ? 36.753  -34.196 8.084   1.00 33.40 ? 47  PRO   C O    1 
ATOM   3730 C  CB   . PRO   C 1 43  ? 33.909  -35.478 7.678   1.00 30.78 ? 47  PRO   C CB   1 
ATOM   3731 C  CG   . PRO   C 1 43  ? 34.404  -35.573 6.262   1.00 30.67 ? 47  PRO   C CG   1 
ATOM   3732 C  CD   . PRO   C 1 43  ? 34.307  -34.160 5.709   1.00 29.09 ? 47  PRO   C CD   1 
ATOM   3733 N  N    . PRO   C 1 44  ? 35.875  -33.918 10.134  1.00 40.31 ? 48  PRO   C N    1 
ATOM   3734 C  CA   . PRO   C 1 44  ? 37.142  -34.145 10.836  1.00 43.94 ? 48  PRO   C CA   1 
ATOM   3735 C  C    . PRO   C 1 44  ? 37.431  -35.630 11.066  1.00 46.20 ? 48  PRO   C C    1 
ATOM   3736 O  O    . PRO   C 1 44  ? 37.254  -36.438 10.128  1.00 46.00 ? 48  PRO   C O    1 
ATOM   3737 C  CB   . PRO   C 1 44  ? 36.976  -33.372 12.170  1.00 45.18 ? 48  PRO   C CB   1 
ATOM   3738 C  CG   . PRO   C 1 44  ? 35.688  -32.581 12.015  1.00 45.26 ? 48  PRO   C CG   1 
ATOM   3739 C  CD   . PRO   C 1 44  ? 34.839  -33.372 11.027  1.00 42.63 ? 48  PRO   C CD   1 
ATOM   3740 N  N    . THR   C 1 52  ? 35.370  -47.663 13.916  1.00 44.98 ? 56  THR   C N    1 
ATOM   3741 C  CA   . THR   C 1 52  ? 34.290  -48.519 13.364  1.00 45.00 ? 56  THR   C CA   1 
ATOM   3742 C  C    . THR   C 1 52  ? 33.111  -47.631 12.978  1.00 41.79 ? 56  THR   C C    1 
ATOM   3743 O  O    . THR   C 1 52  ? 32.887  -47.354 11.801  1.00 44.71 ? 56  THR   C O    1 
ATOM   3744 C  CB   . THR   C 1 52  ? 33.888  -49.584 14.386  1.00 47.96 ? 56  THR   C CB   1 
ATOM   3745 N  N    . VAL   C 1 53  ? 32.375  -47.172 13.992  1.00 36.75 ? 57  VAL   C N    1 
ATOM   3746 C  CA   . VAL   C 1 53  ? 31.261  -46.270 13.773  1.00 33.77 ? 57  VAL   C CA   1 
ATOM   3747 C  C    . VAL   C 1 53  ? 31.763  -44.850 14.006  1.00 33.10 ? 57  VAL   C C    1 
ATOM   3748 O  O    . VAL   C 1 53  ? 32.349  -44.567 15.048  1.00 33.83 ? 57  VAL   C O    1 
ATOM   3749 C  CB   . VAL   C 1 53  ? 30.060  -46.578 14.682  1.00 33.67 ? 57  VAL   C CB   1 
ATOM   3750 C  CG1  . VAL   C 1 53  ? 28.903  -45.625 14.404  1.00 33.65 ? 57  VAL   C CG1  1 
ATOM   3751 C  CG2  . VAL   C 1 53  ? 29.610  -48.031 14.552  1.00 33.24 ? 57  VAL   C CG2  1 
ATOM   3752 N  N    . PRO   C 1 54  ? 31.561  -43.916 13.049  1.00 32.51 ? 58  PRO   C N    1 
ATOM   3753 C  CA   . PRO   C 1 54  ? 31.984  -42.531 13.249  1.00 32.28 ? 58  PRO   C CA   1 
ATOM   3754 C  C    . PRO   C 1 54  ? 31.247  -41.935 14.445  1.00 31.01 ? 58  PRO   C C    1 
ATOM   3755 O  O    . PRO   C 1 54  ? 30.070  -42.217 14.651  1.00 30.37 ? 58  PRO   C O    1 
ATOM   3756 C  CB   . PRO   C 1 54  ? 31.665  -41.811 11.929  1.00 33.48 ? 58  PRO   C CB   1 
ATOM   3757 C  CG   . PRO   C 1 54  ? 30.786  -42.762 11.143  1.00 33.71 ? 58  PRO   C CG   1 
ATOM   3758 C  CD   . PRO   C 1 54  ? 30.958  -44.148 11.728  1.00 33.08 ? 58  PRO   C CD   1 
ATOM   3759 N  N    . PRO   C 1 55  ? 31.912  -41.111 15.288  1.00 32.31 ? 59  PRO   C N    1 
ATOM   3760 C  CA   . PRO   C 1 55  ? 31.222  -40.431 16.383  1.00 31.00 ? 59  PRO   C CA   1 
ATOM   3761 C  C    . PRO   C 1 55  ? 30.328  -39.362 15.766  1.00 28.34 ? 59  PRO   C C    1 
ATOM   3762 O  O    . PRO   C 1 55  ? 30.608  -38.894 14.664  1.00 27.16 ? 59  PRO   C O    1 
ATOM   3763 C  CB   . PRO   C 1 55  ? 32.368  -39.832 17.201  1.00 33.48 ? 59  PRO   C CB   1 
ATOM   3764 C  CG   . PRO   C 1 55  ? 33.427  -39.560 16.159  1.00 34.52 ? 59  PRO   C CG   1 
ATOM   3765 C  CD   . PRO   C 1 55  ? 33.336  -40.746 15.207  1.00 35.03 ? 59  PRO   C CD   1 
ATOM   3766 N  N    . PRO   C 1 56  ? 29.239  -38.942 16.444  1.00 26.22 ? 60  PRO   C N    1 
ATOM   3767 C  CA   . PRO   C 1 56  ? 28.457  -37.805 15.975  1.00 23.76 ? 60  PRO   C CA   1 
ATOM   3768 C  C    . PRO   C 1 56  ? 29.332  -36.555 15.948  1.00 20.11 ? 60  PRO   C C    1 
ATOM   3769 O  O    . PRO   C 1 56  ? 30.342  -36.461 16.653  1.00 21.14 ? 60  PRO   C O    1 
ATOM   3770 C  CB   . PRO   C 1 56  ? 27.285  -37.681 16.966  1.00 26.20 ? 60  PRO   C CB   1 
ATOM   3771 C  CG   . PRO   C 1 56  ? 27.744  -38.466 18.182  1.00 28.52 ? 60  PRO   C CG   1 
ATOM   3772 C  CD   . PRO   C 1 56  ? 28.706  -39.524 17.686  1.00 27.43 ? 60  PRO   C CD   1 
ATOM   3773 N  N    . PRO   C 1 57  ? 28.955  -35.544 15.140  1.00 16.76 ? 61  PRO   C N    1 
ATOM   3774 C  CA   . PRO   C 1 57  ? 29.623  -34.244 15.185  1.00 16.08 ? 61  PRO   C CA   1 
ATOM   3775 C  C    . PRO   C 1 57  ? 29.510  -33.653 16.588  1.00 15.39 ? 61  PRO   C C    1 
ATOM   3776 O  O    . PRO   C 1 57  ? 28.514  -33.849 17.266  1.00 16.34 ? 61  PRO   C O    1 
ATOM   3777 C  CB   . PRO   C 1 57  ? 28.872  -33.402 14.141  1.00 16.79 ? 61  PRO   C CB   1 
ATOM   3778 C  CG   . PRO   C 1 57  ? 28.163  -34.411 13.275  1.00 17.44 ? 61  PRO   C CG   1 
ATOM   3779 C  CD   . PRO   C 1 57  ? 27.849  -35.583 14.172  1.00 17.28 ? 61  PRO   C CD   1 
ATOM   3780 N  N    . ARG   C 1 58  ? 30.531  -32.912 17.012  1.00 14.61 ? 62  ARG   C N    1 
ATOM   3781 C  CA   . ARG   C 1 58  ? 30.501  -32.250 18.308  1.00 14.79 ? 62  ARG   C CA   1 
ATOM   3782 C  C    . ARG   C 1 58  ? 29.377  -31.216 18.371  1.00 14.09 ? 62  ARG   C C    1 
ATOM   3783 O  O    . ARG   C 1 58  ? 28.697  -31.108 19.387  1.00 14.15 ? 62  ARG   C O    1 
ATOM   3784 C  CB   . ARG   C 1 58  ? 31.840  -31.560 18.597  1.00 15.36 ? 62  ARG   C CB   1 
ATOM   3785 C  CG   . ARG   C 1 58  ? 31.844  -30.670 19.833  1.00 15.35 ? 62  ARG   C CG   1 
ATOM   3786 C  CD   . ARG   C 1 58  ? 31.669  -31.472 21.097  1.00 15.49 ? 62  ARG   C CD   1 
ATOM   3787 N  NE   . ARG   C 1 58  ? 31.525  -30.642 22.296  1.00 15.08 ? 62  ARG   C NE   1 
ATOM   3788 C  CZ   . ARG   C 1 58  ? 30.385  -30.171 22.782  1.00 14.10 ? 62  ARG   C CZ   1 
ATOM   3789 N  NH1  . ARG   C 1 58  ? 29.239  -30.303 22.122  1.00 13.85 ? 62  ARG   C NH1  1 
ATOM   3790 N  NH2  . ARG   C 1 58  ? 30.387  -29.567 23.958  1.00 14.86 ? 62  ARG   C NH2  1 
ATOM   3791 N  N    . VAL   C 1 59  ? 29.241  -30.422 17.306  1.00 13.45 ? 63  VAL   C N    1 
ATOM   3792 C  CA   . VAL   C 1 59  ? 28.298  -29.322 17.287  1.00 13.39 ? 63  VAL   C CA   1 
ATOM   3793 C  C    . VAL   C 1 59  ? 27.030  -29.809 16.602  1.00 13.84 ? 63  VAL   C C    1 
ATOM   3794 O  O    . VAL   C 1 59  ? 27.004  -29.992 15.383  1.00 16.05 ? 63  VAL   C O    1 
ATOM   3795 C  CB   . VAL   C 1 59  ? 28.880  -28.080 16.590  1.00 14.25 ? 63  VAL   C CB   1 
ATOM   3796 C  CG1  . VAL   C 1 59  ? 27.876  -26.933 16.576  1.00 14.63 ? 63  VAL   C CG1  1 
ATOM   3797 C  CG2  . VAL   C 1 59  ? 30.190  -27.643 17.231  1.00 15.64 ? 63  VAL   C CG2  1 
ATOM   3798 N  N    . VAL   C 1 60  ? 25.995  -30.054 17.401  1.00 13.35 ? 64  VAL   C N    1 
ATOM   3799 C  CA   . VAL   C 1 60  ? 24.699  -30.463 16.898  1.00 13.80 ? 64  VAL   C CA   1 
ATOM   3800 C  C    . VAL   C 1 60  ? 23.653  -29.821 17.799  1.00 12.99 ? 64  VAL   C C    1 
ATOM   3801 O  O    . VAL   C 1 60  ? 23.944  -29.501 18.952  1.00 15.08 ? 64  VAL   C O    1 
ATOM   3802 C  CB   . VAL   C 1 60  ? 24.485  -31.987 16.842  1.00 15.94 ? 64  VAL   C CB   1 
ATOM   3803 C  CG1  . VAL   C 1 60  ? 25.492  -32.685 15.938  1.00 17.27 ? 64  VAL   C CG1  1 
ATOM   3804 C  CG2  . VAL   C 1 60  ? 24.503  -32.604 18.226  1.00 17.36 ? 64  VAL   C CG2  1 
ATOM   3805 N  N    . ASP   C 1 61  ? 22.442  -29.659 17.262  1.00 11.73 ? 65  ASP   C N    1 
ATOM   3806 C  CA   . ASP   C 1 61  ? 21.281  -29.303 18.054  1.00 11.79 ? 65  ASP   C CA   1 
ATOM   3807 C  C    . ASP   C 1 61  ? 20.322  -30.487 18.029  1.00 11.63 ? 65  ASP   C C    1 
ATOM   3808 O  O    . ASP   C 1 61  ? 20.140  -31.113 16.989  1.00 12.47 ? 65  ASP   C O    1 
ATOM   3809 C  CB   . ASP   C 1 61  ? 20.558  -28.089 17.491  1.00 12.55 ? 65  ASP   C CB   1 
ATOM   3810 C  CG   . ASP   C 1 61  ? 21.188  -26.726 17.732  1.00 13.90 ? 65  ASP   C CG   1 
ATOM   3811 O  OD1  . ASP   C 1 61  ? 22.280  -26.648 18.376  1.00 14.26 ? 65  ASP   C OD1  1 
ATOM   3812 O  OD2  . ASP   C 1 61  ? 20.562  -25.741 17.278  1.00 15.57 ? 65  ASP   C OD2  1 
ATOM   3813 N  N    . LYS   C 1 62  ? 19.720  -30.793 19.176  1.00 11.35 ? 66  LYS   C N    1 
ATOM   3814 C  CA   . LYS   C 1 62  ? 18.868  -31.959 19.306  1.00 12.01 ? 66  LYS   C CA   1 
ATOM   3815 C  C    . LYS   C 1 62  ? 17.601  -31.573 20.052  1.00 11.44 ? 66  LYS   C C    1 
ATOM   3816 O  O    . LYS   C 1 62  ? 17.651  -30.872 21.067  1.00 11.84 ? 66  LYS   C O    1 
ATOM   3817 C  CB   . LYS   C 1 62  ? 19.601  -33.084 20.045  1.00 14.24 ? 66  LYS   C CB   1 
ATOM   3818 C  CG   . LYS   C 1 62  ? 18.865  -34.415 20.067  1.00 17.66 ? 66  LYS   C CG   1 
ATOM   3819 C  CD   . LYS   C 1 62  ? 19.574  -35.448 20.943  1.00 20.88 ? 66  LYS   C CD   1 
ATOM   3820 C  CE   . LYS   C 1 62  ? 20.933  -35.842 20.487  1.00 22.81 ? 66  LYS   C CE   1 
ATOM   3821 N  NZ   . LYS   C 1 62  ? 21.542  -36.801 21.417  1.00 22.53 ? 66  LYS   C NZ   1 
ATOM   3822 N  N    . LEU   C 1 63  ? 16.473  -32.074 19.551  1.00 11.10 ? 67  LEU   C N    1 
ATOM   3823 C  CA   . LEU   C 1 63  ? 15.198  -31.957 20.233  1.00 11.35 ? 67  LEU   C CA   1 
ATOM   3824 C  C    . LEU   C 1 63  ? 14.521  -33.320 20.192  1.00 12.03 ? 67  LEU   C C    1 
ATOM   3825 O  O    . LEU   C 1 63  ? 14.362  -33.875 19.110  1.00 13.48 ? 67  LEU   C O    1 
ATOM   3826 C  CB   . LEU   C 1 63  ? 14.342  -30.903 19.537  1.00 12.52 ? 67  LEU   C CB   1 
ATOM   3827 C  CG   . LEU   C 1 63  ? 12.916  -30.748 20.065  1.00 13.62 ? 67  LEU   C CG   1 
ATOM   3828 C  CD1  . LEU   C 1 63  ? 12.886  -30.226 21.489  1.00 13.67 ? 67  LEU   C CD1  1 
ATOM   3829 C  CD2  . LEU   C 1 63  ? 12.127  -29.860 19.127  1.00 15.44 ? 67  LEU   C CD2  1 
ATOM   3830 N  N    . SER   C 1 64  ? 14.143  -33.852 21.355  1.00 11.96 ? 68  SER   C N    1 
ATOM   3831 C  CA   . SER   C 1 64  ? 13.389  -35.099 21.418  1.00 12.93 ? 68  SER   C CA   1 
ATOM   3832 C  C    . SER   C 1 64  ? 12.210  -34.877 22.354  1.00 12.52 ? 68  SER   C C    1 
ATOM   3833 O  O    . SER   C 1 64  ? 12.419  -34.468 23.500  1.00 13.67 ? 68  SER   C O    1 
ATOM   3834 C  CB   . SER   C 1 64  ? 14.254  -36.261 21.884  1.00 15.80 ? 68  SER   C CB   1 
ATOM   3835 O  OG   . SER   C 1 64  ? 13.548  -37.497 21.864  1.00 19.68 ? 68  SER   C OG   1 
ATOM   3836 N  N    . LEU   C 1 65  ? 10.995  -35.156 21.872  1.00 12.14 ? 69  LEU   C N    1 
ATOM   3837 C  CA   . LEU   C 1 65  ? 9.776   -34.919 22.637  1.00 12.54 ? 69  LEU   C CA   1 
ATOM   3838 C  C    . LEU   C 1 65  ? 8.847   -36.122 22.527  1.00 11.85 ? 69  LEU   C C    1 
ATOM   3839 O  O    . LEU   C 1 65  ? 8.656   -36.658 21.438  1.00 12.16 ? 69  LEU   C O    1 
ATOM   3840 C  CB   . LEU   C 1 65  ? 9.030   -33.697 22.095  1.00 14.32 ? 69  LEU   C CB   1 
ATOM   3841 C  CG   . LEU   C 1 65  ? 9.748   -32.349 22.135  1.00 15.83 ? 69  LEU   C CG   1 
ATOM   3842 C  CD1  . LEU   C 1 65  ? 8.929   -31.319 21.389  1.00 16.83 ? 69  LEU   C CD1  1 
ATOM   3843 C  CD2  . LEU   C 1 65  ? 10.015  -31.863 23.549  1.00 16.68 ? 69  LEU   C CD2  1 
ATOM   3844 N  N    . CYS   C 1 66  ? 8.222   -36.489 23.648  1.00 11.52 ? 70  CYS   C N    1 
ATOM   3845 C  CA   . CYS   C 1 66  ? 7.115   -37.420 23.618  1.00 11.72 ? 70  CYS   C CA   1 
ATOM   3846 C  C    . CYS   C 1 66  ? 5.819   -36.627 23.498  1.00 11.45 ? 70  CYS   C C    1 
ATOM   3847 O  O    . CYS   C 1 66  ? 5.716   -35.505 24.010  1.00 12.05 ? 70  CYS   C O    1 
ATOM   3848 C  CB   . CYS   C 1 66  ? 7.126   -38.312 24.849  1.00 12.68 ? 70  CYS   C CB   1 
ATOM   3849 S  SG   . CYS   C 1 66  ? 8.518   -39.472 24.879  1.00 15.70 ? 70  CYS   C SG   1 
ATOM   3850 N  N    . VAL   C 1 67  ? 4.826   -37.244 22.851  1.00 11.15 ? 71  VAL   C N    1 
ATOM   3851 C  CA   . VAL   C 1 67  ? 3.606   -36.553 22.466  1.00 11.25 ? 71  VAL   C CA   1 
ATOM   3852 C  C    . VAL   C 1 67  ? 2.421   -37.447 22.801  1.00 11.59 ? 71  VAL   C C    1 
ATOM   3853 O  O    . VAL   C 1 67  ? 2.440   -38.623 22.488  1.00 12.25 ? 71  VAL   C O    1 
ATOM   3854 C  CB   . VAL   C 1 67  ? 3.611   -36.204 20.965  1.00 11.73 ? 71  VAL   C CB   1 
ATOM   3855 C  CG1  . VAL   C 1 67  ? 2.336   -35.467 20.573  1.00 11.97 ? 71  VAL   C CG1  1 
ATOM   3856 C  CG2  . VAL   C 1 67  ? 4.837   -35.381 20.579  1.00 11.87 ? 71  VAL   C CG2  1 
ATOM   3857 N  N    . ALA   C 1 68  ? 1.379   -36.868 23.401  1.00 11.82 ? 72  ALA   C N    1 
ATOM   3858 C  CA   . ALA   C 1 68  ? 0.152   -37.595 23.670  1.00 12.43 ? 72  ALA   C CA   1 
ATOM   3859 C  C    . ALA   C 1 68  ? -0.699  -37.638 22.414  1.00 12.76 ? 72  ALA   C C    1 
ATOM   3860 O  O    . ALA   C 1 68  ? -1.147  -36.588 21.957  1.00 14.35 ? 72  ALA   C O    1 
ATOM   3861 C  CB   . ALA   C 1 68  ? -0.615  -36.930 24.789  1.00 13.25 ? 72  ALA   C CB   1 
ATOM   3862 N  N    . PRO   C 1 69  ? -0.979  -38.832 21.852  1.00 13.92 ? 73  PRO   C N    1 
ATOM   3863 C  CA   . PRO   C 1 69  ? -1.795  -38.925 20.646  1.00 15.19 ? 73  PRO   C CA   1 
ATOM   3864 C  C    . PRO   C 1 69  ? -3.268  -38.813 21.006  1.00 17.42 ? 73  PRO   C C    1 
ATOM   3865 O  O    . PRO   C 1 69  ? -3.651  -39.033 22.148  1.00 18.64 ? 73  PRO   C O    1 
ATOM   3866 C  CB   . PRO   C 1 69  ? -1.418  -40.321 20.129  1.00 15.38 ? 73  PRO   C CB   1 
ATOM   3867 C  CG   . PRO   C 1 69  ? -1.211  -41.104 21.400  1.00 15.21 ? 73  PRO   C CG   1 
ATOM   3868 C  CD   . PRO   C 1 69  ? -0.463  -40.135 22.292  1.00 14.53 ? 73  PRO   C CD   1 
ATOM   3869 N  N    . GLY   C 1 70  ? -4.104  -38.509 20.022  1.00 20.61 ? 74  GLY   C N    1 
ATOM   3870 C  CA   . GLY   C 1 70  ? -5.536  -38.463 20.292  1.00 22.40 ? 74  GLY   C CA   1 
ATOM   3871 C  C    . GLY   C 1 70  ? -6.233  -39.833 20.290  1.00 23.19 ? 74  GLY   C C    1 
ATOM   3872 O  O    . GLY   C 1 70  ? -7.455  -39.858 20.261  1.00 25.91 ? 74  GLY   C O    1 
ATOM   3873 N  N    . LYS   C 1 71  ? -5.491  -40.953 20.380  1.00 22.94 ? 75  LYS   C N    1 
ATOM   3874 C  CA   . LYS   C 1 71  ? -6.036  -42.293 20.168  1.00 21.95 ? 75  LYS   C CA   1 
ATOM   3875 C  C    . LYS   C 1 71  ? -5.094  -43.334 20.772  1.00 21.99 ? 75  LYS   C C    1 
ATOM   3876 O  O    . LYS   C 1 71  ? -3.975  -43.004 21.142  1.00 22.02 ? 75  LYS   C O    1 
ATOM   3877 C  CB   . LYS   C 1 71  ? -6.210  -42.604 18.675  1.00 21.77 ? 75  LYS   C CB   1 
ATOM   3878 C  CG   . LYS   C 1 71  ? -4.915  -42.646 17.859  1.00 21.40 ? 75  LYS   C CG   1 
ATOM   3879 C  CD   . LYS   C 1 71  ? -5.101  -42.835 16.354  1.00 21.81 ? 75  LYS   C CD   1 
ATOM   3880 C  CE   . LYS   C 1 71  ? -5.700  -44.157 16.013  1.00 22.19 ? 75  LYS   C CE   1 
ATOM   3881 N  NZ   . LYS   C 1 71  ? -5.787  -44.332 14.561  1.00 22.41 ? 75  LYS   C NZ   1 
ATOM   3882 N  N    . ALA   C 1 72  ? -5.533  -44.601 20.806  1.00 21.19 ? 76  ALA   C N    1 
ATOM   3883 C  CA   . ALA   C 1 72  ? -4.729  -45.681 21.350  1.00 21.77 ? 76  ALA   C CA   1 
ATOM   3884 C  C    . ALA   C 1 72  ? -3.550  -45.970 20.422  1.00 19.41 ? 76  ALA   C C    1 
ATOM   3885 O  O    . ALA   C 1 72  ? -3.681  -45.903 19.200  1.00 19.67 ? 76  ALA   C O    1 
ATOM   3886 C  CB   . ALA   C 1 72  ? -5.575  -46.925 21.535  1.00 23.65 ? 76  ALA   C CB   1 
ATOM   3887 N  N    . CYS   C 1 73  ? -2.411  -46.327 21.018  1.00 19.82 ? 77  CYS   C N    1 
ATOM   3888 C  CA   . CYS   C 1 73  ? -1.314  -46.932 20.288  1.00 19.00 ? 77  CYS   C CA   1 
ATOM   3889 C  C    . CYS   C 1 73  ? -1.692  -48.375 20.002  1.00 18.30 ? 77  CYS   C C    1 
ATOM   3890 O  O    . CYS   C 1 73  ? -2.249  -49.064 20.860  1.00 19.94 ? 77  CYS   C O    1 
ATOM   3891 C  CB   . CYS   C 1 73  ? -0.017  -46.960 21.084  1.00 20.16 ? 77  CYS   C CB   1 
ATOM   3892 S  SG   . CYS   C 1 73  ? 0.658   -45.328 21.469  1.00 21.90 ? 77  CYS   C SG   1 
ATOM   3893 N  N    . SER   C 1 74  ? -1.378  -48.836 18.794  1.00 16.99 ? 78  SER   C N    1 
ATOM   3894 C  CA   . SER   C 1 74  ? -1.539  -50.240 18.488  1.00 19.10 ? 78  SER   C CA   1 
ATOM   3895 C  C    . SER   C 1 74  ? -0.584  -51.059 19.345  1.00 18.81 ? 78  SER   C C    1 
ATOM   3896 O  O    . SER   C 1 74  ? 0.490   -50.599 19.717  1.00 18.76 ? 78  SER   C O    1 
ATOM   3897 C  CB   . SER   C 1 74  ? -1.315  -50.515 17.052  1.00 20.52 ? 78  SER   C CB   1 
ATOM   3898 O  OG   . SER   C 1 74  ? 0.029   -50.295 16.679  1.00 21.29 ? 78  SER   C OG   1 
ATOM   3899 N  N    . PRO   C 1 75  ? -0.946  -52.318 19.657  1.00 19.21 ? 79  PRO   C N    1 
ATOM   3900 C  CA   . PRO   C 1 75  ? -0.007  -53.237 20.296  1.00 19.18 ? 79  PRO   C CA   1 
ATOM   3901 C  C    . PRO   C 1 75  ? 1.333   -53.358 19.577  1.00 17.98 ? 79  PRO   C C    1 
ATOM   3902 O  O    . PRO   C 1 75  ? 2.366   -53.400 20.225  1.00 18.39 ? 79  PRO   C O    1 
ATOM   3903 C  CB   . PRO   C 1 75  ? -0.798  -54.547 20.299  1.00 20.44 ? 79  PRO   C CB   1 
ATOM   3904 C  CG   . PRO   C 1 75  ? -2.236  -54.095 20.394  1.00 21.27 ? 79  PRO   C CG   1 
ATOM   3905 C  CD   . PRO   C 1 75  ? -2.299  -52.880 19.503  1.00 20.86 ? 79  PRO   C CD   1 
ATOM   3906 N  N    . ALA   C 1 76  ? 1.322   -53.419 18.239  1.00 18.41 ? 80  ALA   C N    1 
ATOM   3907 C  CA   . ALA   C 1 76  ? 2.561   -53.513 17.481  1.00 19.69 ? 80  ALA   C CA   1 
ATOM   3908 C  C    . ALA   C 1 76  ? 3.431   -52.276 17.705  1.00 18.91 ? 80  ALA   C C    1 
ATOM   3909 O  O    . ALA   C 1 76  ? 4.644   -52.395 17.839  1.00 19.92 ? 80  ALA   C O    1 
ATOM   3910 C  CB   . ALA   C 1 76  ? 2.269   -53.713 16.014  1.00 21.31 ? 80  ALA   C CB   1 
ATOM   3911 N  N    . ALA   C 1 77  ? 2.817   -51.084 17.731  1.00 18.15 ? 81  ALA   C N    1 
ATOM   3912 C  CA   . ALA   C 1 77  ? 3.562   -49.857 17.953  1.00 17.93 ? 81  ALA   C CA   1 
ATOM   3913 C  C    . ALA   C 1 77  ? 4.176   -49.864 19.349  1.00 16.94 ? 81  ALA   C C    1 
ATOM   3914 O  O    . ALA   C 1 77  ? 5.347   -49.533 19.509  1.00 17.53 ? 81  ALA   C O    1 
ATOM   3915 C  CB   . ALA   C 1 77  ? 2.667   -48.651 17.758  1.00 18.32 ? 81  ALA   C CB   1 
ATOM   3916 N  N    . SER   C 1 78  ? 3.389   -50.273 20.356  1.00 15.90 ? 82  SER   C N    1 
ATOM   3917 C  CA   . SER   C 1 78  ? 3.859   -50.276 21.736  1.00 16.73 ? 82  SER   C CA   1 
ATOM   3918 C  C    . SER   C 1 78  ? 5.013   -51.255 21.926  1.00 17.02 ? 82  SER   C C    1 
ATOM   3919 O  O    . SER   C 1 78  ? 5.922   -50.983 22.704  1.00 18.50 ? 82  SER   C O    1 
ATOM   3920 C  CB   . SER   C 1 78  ? 2.741   -50.588 22.673  1.00 17.74 ? 82  SER   C CB   1 
ATOM   3921 O  OG   . SER   C 1 78  ? 1.837   -49.499 22.736  1.00 19.42 ? 82  SER   C OG   1 
ATOM   3922 N  N    . GLU   C 1 79  ? 4.962   -52.407 21.245  1.00 17.74 ? 83  GLU   C N    1 
ATOM   3923 C  CA   . GLU   C 1 79  ? 6.028   -53.396 21.329  1.00 20.42 ? 83  GLU   C CA   1 
ATOM   3924 C  C    . GLU   C 1 79  ? 7.356   -52.873 20.793  1.00 21.88 ? 83  GLU   C C    1 
ATOM   3925 O  O    . GLU   C 1 79  ? 8.410   -53.280 21.275  1.00 25.27 ? 83  GLU   C O    1 
ATOM   3926 C  CB   . GLU   C 1 79  ? 5.642   -54.678 20.594  1.00 22.57 ? 83  GLU   C CB   1 
ATOM   3927 C  CG   . GLU   C 1 79  ? 4.707   -55.526 21.438  1.00 25.86 ? 83  GLU   C CG   1 
ATOM   3928 C  CD   . GLU   C 1 79  ? 4.157   -56.732 20.709  1.00 28.25 ? 83  GLU   C CD   1 
ATOM   3929 O  OE1  . GLU   C 1 79  ? 4.296   -56.810 19.473  1.00 32.36 ? 83  GLU   C OE1  1 
ATOM   3930 O  OE2  . GLU   C 1 79  ? 3.570   -57.585 21.394  1.00 32.72 ? 83  GLU   C OE2  1 
ATOM   3931 N  N    . ILE   C 1 80  ? 7.324   -51.997 19.787  1.00 22.80 ? 84  ILE   C N    1 
ATOM   3932 C  CA   . ILE   C 1 80  ? 8.558   -51.426 19.271  1.00 25.41 ? 84  ILE   C CA   1 
ATOM   3933 C  C    . ILE   C 1 80  ? 9.092   -50.377 20.246  1.00 26.38 ? 84  ILE   C C    1 
ATOM   3934 O  O    . ILE   C 1 80  ? 10.291  -50.355 20.518  1.00 28.44 ? 84  ILE   C O    1 
ATOM   3935 C  CB   . ILE   C 1 80  ? 8.350   -50.832 17.867  1.00 29.28 ? 84  ILE   C CB   1 
ATOM   3936 C  CG1  . ILE   C 1 80  ? 7.978   -51.918 16.864  1.00 31.40 ? 84  ILE   C CG1  1 
ATOM   3937 C  CG2  . ILE   C 1 80  ? 9.583   -50.041 17.419  1.00 30.44 ? 84  ILE   C CG2  1 
ATOM   3938 C  CD1  . ILE   C 1 80  ? 7.405   -51.388 15.565  1.00 33.41 ? 84  ILE   C CD1  1 
ATOM   3939 N  N    . THR   C 1 81  ? 8.212   -49.499 20.750  1.00 25.06 ? 85  THR   C N    1 
ATOM   3940 C  CA   . THR   C 1 81  ? 8.654   -48.252 21.375  1.00 25.07 ? 85  THR   C CA   1 
ATOM   3941 C  C    . THR   C 1 81  ? 8.661   -48.313 22.901  1.00 25.19 ? 85  THR   C C    1 
ATOM   3942 O  O    . THR   C 1 81  ? 9.424   -47.593 23.560  1.00 27.39 ? 85  THR   C O    1 
ATOM   3943 C  CB   . THR   C 1 81  ? 7.781   -47.098 20.882  1.00 25.58 ? 85  THR   C CB   1 
ATOM   3944 O  OG1  . THR   C 1 81  ? 6.418   -47.297 21.251  1.00 23.44 ? 85  THR   C OG1  1 
ATOM   3945 C  CG2  . THR   C 1 81  ? 7.807   -46.992 19.372  1.00 26.77 ? 85  THR   C CG2  1 
ATOM   3946 N  N    . GLY   C 1 82  ? 7.789   -49.131 23.472  1.00 23.49 ? 86  GLY   C N    1 
ATOM   3947 C  CA   . GLY   C 1 82  ? 7.515   -49.068 24.893  1.00 25.29 ? 86  GLY   C CA   1 
ATOM   3948 C  C    . GLY   C 1 82  ? 6.680   -47.841 25.241  1.00 24.17 ? 86  GLY   C C    1 
ATOM   3949 O  O    . GLY   C 1 82  ? 6.537   -47.527 26.416  1.00 30.18 ? 86  GLY   C O    1 
ATOM   3950 N  N    . LEU   C 1 83  ? 6.090   -47.181 24.228  1.00 20.21 ? 87  LEU   C N    1 
ATOM   3951 C  CA   . LEU   C 1 83  ? 5.135   -46.117 24.466  1.00 17.66 ? 87  LEU   C CA   1 
ATOM   3952 C  C    . LEU   C 1 83  ? 3.735   -46.708 24.334  1.00 17.81 ? 87  LEU   C C    1 
ATOM   3953 O  O    . LEU   C 1 83  ? 3.489   -47.568 23.488  1.00 19.52 ? 87  LEU   C O    1 
ATOM   3954 C  CB   . LEU   C 1 83  ? 5.331   -44.924 23.525  1.00 17.51 ? 87  LEU   C CB   1 
ATOM   3955 C  CG   . LEU   C 1 83  ? 6.702   -44.242 23.575  1.00 17.02 ? 87  LEU   C CG   1 
ATOM   3956 C  CD1  . LEU   C 1 83  ? 6.806   -43.169 22.499  1.00 17.59 ? 87  LEU   C CD1  1 
ATOM   3957 C  CD2  . LEU   C 1 83  ? 6.985   -43.652 24.954  1.00 17.76 ? 87  LEU   C CD2  1 
ATOM   3958 N  N    . SER   C 1 84  ? 2.837   -46.240 25.197  1.00 17.68 ? 88  SER   C N    1 
ATOM   3959 C  CA   . SER   C 1 84  ? 1.410   -46.484 25.085  1.00 17.17 ? 88  SER   C CA   1 
ATOM   3960 C  C    . SER   C 1 84  ? 0.716   -45.187 25.477  1.00 17.07 ? 88  SER   C C    1 
ATOM   3961 O  O    . SER   C 1 84  ? 1.308   -44.340 26.121  1.00 16.15 ? 88  SER   C O    1 
ATOM   3962 C  CB   . SER   C 1 84  ? 0.965   -47.613 25.973  1.00 18.11 ? 88  SER   C CB   1 
ATOM   3963 O  OG   . SER   C 1 84  ? 1.114   -47.242 27.338  1.00 19.01 ? 88  SER   C OG   1 
ATOM   3964 N  N    A THR   C 1 85  ? -0.560  -45.055 25.113  0.50 17.19 ? 89  THR   C N    1 
ATOM   3965 N  N    B THR   C 1 85  ? -0.557  -45.038 25.123  0.50 17.94 ? 89  THR   C N    1 
ATOM   3966 C  CA   A THR   C 1 85  ? -1.288  -43.831 25.407  0.50 17.93 ? 89  THR   C CA   1 
ATOM   3967 C  CA   B THR   C 1 85  ? -1.240  -43.796 25.442  0.50 19.30 ? 89  THR   C CA   1 
ATOM   3968 C  C    A THR   C 1 85  ? -1.413  -43.663 26.928  0.50 17.84 ? 89  THR   C C    1 
ATOM   3969 C  C    B THR   C 1 85  ? -1.380  -43.654 26.958  0.50 18.64 ? 89  THR   C C    1 
ATOM   3970 O  O    A THR   C 1 85  ? -1.256  -42.556 27.438  0.50 18.11 ? 89  THR   C O    1 
ATOM   3971 O  O    B THR   C 1 85  ? -1.207  -42.560 27.491  0.50 18.50 ? 89  THR   C O    1 
ATOM   3972 C  CB   A THR   C 1 85  ? -2.615  -43.846 24.644  0.50 18.18 ? 89  THR   C CB   1 
ATOM   3973 C  CB   B THR   C 1 85  ? -2.554  -43.745 24.674  0.50 20.83 ? 89  THR   C CB   1 
ATOM   3974 O  OG1  A THR   C 1 85  ? -2.231  -44.083 23.289  0.50 18.31 ? 89  THR   C OG1  1 
ATOM   3975 O  OG1  B THR   C 1 85  ? -3.272  -44.932 24.986  0.50 23.51 ? 89  THR   C OG1  1 
ATOM   3976 C  CG2  A THR   C 1 85  ? -3.364  -42.527 24.738  0.50 17.53 ? 89  THR   C CG2  1 
ATOM   3977 C  CG2  B THR   C 1 85  ? -2.280  -43.697 23.184  0.50 20.56 ? 89  THR   C CG2  1 
ATOM   3978 N  N    . ALA   C 1 86  ? -1.596  -44.765 27.670  1.00 18.51 ? 90  ALA   C N    1 
ATOM   3979 C  CA   . ALA   C 1 86  ? -1.678  -44.707 29.126  1.00 18.85 ? 90  ALA   C CA   1 
ATOM   3980 C  C    . ALA   C 1 86  ? -0.359  -44.245 29.761  1.00 17.27 ? 90  ALA   C C    1 
ATOM   3981 O  O    . ALA   C 1 86  ? -0.364  -43.446 30.698  1.00 18.07 ? 90  ALA   C O    1 
ATOM   3982 C  CB   . ALA   C 1 86  ? -2.131  -46.028 29.695  1.00 20.11 ? 90  ALA   C CB   1 
ATOM   3983 N  N    . VAL   C 1 87  ? 0.778   -44.756 29.274  1.00 16.45 ? 91  VAL   C N    1 
ATOM   3984 C  CA   . VAL   C 1 87  ? 2.081   -44.340 29.769  1.00 16.47 ? 91  VAL   C CA   1 
ATOM   3985 C  C    . VAL   C 1 87  ? 2.322   -42.860 29.473  1.00 15.00 ? 91  VAL   C C    1 
ATOM   3986 O  O    . VAL   C 1 87  ? 2.764   -42.112 30.338  1.00 14.66 ? 91  VAL   C O    1 
ATOM   3987 C  CB   . VAL   C 1 87  ? 3.185   -45.225 29.166  1.00 18.85 ? 91  VAL   C CB   1 
ATOM   3988 C  CG1  . VAL   C 1 87  ? 4.571   -44.610 29.314  1.00 20.35 ? 91  VAL   C CG1  1 
ATOM   3989 C  CG2  . VAL   C 1 87  ? 3.152   -46.629 29.751  1.00 20.92 ? 91  VAL   C CG2  1 
ATOM   3990 N  N    . LEU   C 1 88  ? 2.040   -42.426 28.242  1.00 14.27 ? 92  LEU   C N    1 
ATOM   3991 C  CA   . LEU   C 1 88  ? 2.219   -41.026 27.903  1.00 14.22 ? 92  LEU   C CA   1 
ATOM   3992 C  C    . LEU   C 1 88  ? 1.344   -40.131 28.783  1.00 14.67 ? 92  LEU   C C    1 
ATOM   3993 O  O    . LEU   C 1 88  ? 1.782   -39.068 29.237  1.00 14.43 ? 92  LEU   C O    1 
ATOM   3994 C  CB   . LEU   C 1 88  ? 1.925   -40.863 26.415  1.00 14.46 ? 92  LEU   C CB   1 
ATOM   3995 C  CG   . LEU   C 1 88  ? 2.962   -41.509 25.490  1.00 15.01 ? 92  LEU   C CG   1 
ATOM   3996 C  CD1  . LEU   C 1 88  ? 2.395   -41.709 24.102  1.00 15.44 ? 92  LEU   C CD1  1 
ATOM   3997 C  CD2  . LEU   C 1 88  ? 4.245   -40.694 25.415  1.00 15.59 ? 92  LEU   C CD2  1 
ATOM   3998 N  N    . ALA   C 1 89  ? 0.119   -40.581 29.057  1.00 15.62 ? 93  ALA   C N    1 
ATOM   3999 C  CA   . ALA   C 1 89  ? -0.803  -39.823 29.892  1.00 16.30 ? 93  ALA   C CA   1 
ATOM   4000 C  C    . ALA   C 1 89  ? -0.299  -39.738 31.332  1.00 16.51 ? 93  ALA   C C    1 
ATOM   4001 O  O    . ALA   C 1 89  ? -0.433  -38.706 31.980  1.00 18.30 ? 93  ALA   C O    1 
ATOM   4002 C  CB   . ALA   C 1 89  ? -2.180  -40.447 29.845  1.00 18.10 ? 93  ALA   C CB   1 
ATOM   4003 N  N    . ALA   C 1 90  ? 0.279   -40.826 31.841  1.00 16.12 ? 94  ALA   C N    1 
ATOM   4004 C  CA   . ALA   C 1 90  ? 0.776   -40.857 33.209  1.00 16.52 ? 94  ALA   C CA   1 
ATOM   4005 C  C    . ALA   C 1 90  ? 1.940   -39.886 33.386  1.00 16.04 ? 94  ALA   C C    1 
ATOM   4006 O  O    . ALA   C 1 90  ? 2.187   -39.431 34.498  1.00 18.31 ? 94  ALA   C O    1 
ATOM   4007 C  CB   . ALA   C 1 90  ? 1.183   -42.263 33.580  1.00 17.20 ? 94  ALA   C CB   1 
ATOM   4008 N  N    . HIS   C 1 91  ? 2.650   -39.571 32.292  1.00 15.06 ? 95  HIS   C N    1 
ATOM   4009 C  CA   . HIS   C 1 91  ? 3.745   -38.609 32.314  1.00 15.42 ? 95  HIS   C CA   1 
ATOM   4010 C  C    . HIS   C 1 91  ? 3.268   -37.199 31.957  1.00 14.99 ? 95  HIS   C C    1 
ATOM   4011 O  O    . HIS   C 1 91  ? 4.082   -36.304 31.741  1.00 15.97 ? 95  HIS   C O    1 
ATOM   4012 C  CB   . HIS   C 1 91  ? 4.865   -39.067 31.380  1.00 15.89 ? 95  HIS   C CB   1 
ATOM   4013 C  CG   . HIS   C 1 91  ? 5.634   -40.247 31.873  1.00 16.62 ? 95  HIS   C CG   1 
ATOM   4014 N  ND1  . HIS   C 1 91  ? 5.139   -41.536 31.859  1.00 18.02 ? 95  HIS   C ND1  1 
ATOM   4015 C  CD2  . HIS   C 1 91  ? 6.864   -40.328 32.412  1.00 17.19 ? 95  HIS   C CD2  1 
ATOM   4016 C  CE1  . HIS   C 1 91  ? 6.059   -42.355 32.356  1.00 18.36 ? 95  HIS   C CE1  1 
ATOM   4017 N  NE2  . HIS   C 1 91  ? 7.102   -41.645 32.707  1.00 18.80 ? 95  HIS   C NE2  1 
ATOM   4018 N  N    . GLY   C 1 92  ? 1.953   -37.009 31.853  1.00 15.57 ? 96  GLY   C N    1 
ATOM   4019 C  CA   . GLY   C 1 92  ? 1.365   -35.695 31.625  1.00 15.22 ? 96  GLY   C CA   1 
ATOM   4020 C  C    . GLY   C 1 92  ? 1.692   -35.096 30.258  1.00 14.88 ? 96  GLY   C C    1 
ATOM   4021 O  O    . GLY   C 1 92  ? 1.707   -33.873 30.119  1.00 16.63 ? 96  GLY   C O    1 
ATOM   4022 N  N    . ARG   C 1 93  ? 1.963   -35.940 29.256  1.00 13.45 ? 97  ARG   C N    1 
ATOM   4023 C  CA   . ARG   C 1 93  ? 2.348   -35.430 27.945  1.00 12.93 ? 97  ARG   C CA   1 
ATOM   4024 C  C    . ARG   C 1 93  ? 1.196   -34.666 27.302  1.00 12.50 ? 97  ARG   C C    1 
ATOM   4025 O  O    . ARG   C 1 93  ? 0.023   -35.042 27.438  1.00 13.92 ? 97  ARG   C O    1 
ATOM   4026 C  CB   . ARG   C 1 93  ? 2.836   -36.530 27.001  1.00 12.79 ? 97  ARG   C CB   1 
ATOM   4027 C  CG   . ARG   C 1 93  ? 4.082   -37.267 27.464  1.00 13.07 ? 97  ARG   C CG   1 
ATOM   4028 C  CD   . ARG   C 1 93  ? 5.281   -36.374 27.674  1.00 13.56 ? 97  ARG   C CD   1 
ATOM   4029 N  NE   . ARG   C 1 93  ? 5.274   -35.767 29.008  1.00 14.05 ? 97  ARG   C NE   1 
ATOM   4030 C  CZ   . ARG   C 1 93  ? 6.114   -34.830 29.437  1.00 15.71 ? 97  ARG   C CZ   1 
ATOM   4031 N  NH1  . ARG   C 1 93  ? 6.984   -34.280 28.611  1.00 16.11 ? 97  ARG   C NH1  1 
ATOM   4032 N  NH2  . ARG   C 1 93  ? 6.058   -34.431 30.695  1.00 17.04 ? 97  ARG   C NH2  1 
ATOM   4033 N  N    . GLN   C 1 94  ? 1.569   -33.583 26.604  1.00 12.27 ? 98  GLN   C N    1 
ATOM   4034 C  CA   . GLN   C 1 94  ? 0.636   -32.771 25.835  1.00 12.67 ? 98  GLN   C CA   1 
ATOM   4035 C  C    . GLN   C 1 94  ? 0.570   -33.292 24.407  1.00 12.41 ? 98  GLN   C C    1 
ATOM   4036 O  O    . GLN   C 1 94  ? 1.442   -34.021 23.935  1.00 12.02 ? 98  GLN   C O    1 
ATOM   4037 C  CB   . GLN   C 1 94  ? 1.076   -31.306 25.873  1.00 14.08 ? 98  GLN   C CB   1 
ATOM   4038 C  CG   . GLN   C 1 94  ? 0.930   -30.680 27.256  1.00 16.35 ? 98  GLN   C CG   1 
ATOM   4039 C  CD   . GLN   C 1 94  ? 1.612   -29.337 27.428  1.00 19.35 ? 98  GLN   C CD   1 
ATOM   4040 O  OE1  . GLN   C 1 94  ? 1.954   -28.621 26.476  1.00 18.97 ? 98  GLN   C OE1  1 
ATOM   4041 N  NE2  . GLN   C 1 94  ? 1.840   -28.992 28.688  1.00 23.55 ? 98  GLN   C NE2  1 
ATOM   4042 N  N    . CYS   C 1 95  ? -0.488  -32.880 23.718  1.00 12.98 ? 99  CYS   C N    1 
ATOM   4043 C  CA   . CYS   C 1 95  ? -0.711  -33.326 22.359  1.00 13.47 ? 99  CYS   C CA   1 
ATOM   4044 C  C    . CYS   C 1 95  ? 0.105   -32.491 21.375  1.00 12.82 ? 99  CYS   C C    1 
ATOM   4045 O  O    . CYS   C 1 95  ? 0.894   -31.622 21.754  1.00 13.13 ? 99  CYS   C O    1 
ATOM   4046 C  CB   . CYS   C 1 95  ? -2.202  -33.325 22.066  1.00 14.83 ? 99  CYS   C CB   1 
ATOM   4047 S  SG   . CYS   C 1 95  ? -2.921  -31.688 21.821  1.00 18.91 ? 99  CYS   C SG   1 
ATOM   4048 N  N    . PHE   C 1 96  ? -0.089  -32.787 20.090  1.00 12.79 ? 100 PHE   C N    1 
ATOM   4049 C  CA   . PHE   C 1 96  ? 0.510   -32.003 19.030  1.00 13.50 ? 100 PHE   C CA   1 
ATOM   4050 C  C    . PHE   C 1 96  ? -0.321  -30.736 18.867  1.00 14.45 ? 100 PHE   C C    1 
ATOM   4051 O  O    . PHE   C 1 96  ? -1.349  -30.753 18.197  1.00 16.93 ? 100 PHE   C O    1 
ATOM   4052 C  CB   . PHE   C 1 96  ? 0.559   -32.851 17.758  1.00 14.20 ? 100 PHE   C CB   1 
ATOM   4053 C  CG   . PHE   C 1 96  ? 1.638   -32.409 16.779  1.00 15.31 ? 100 PHE   C CG   1 
ATOM   4054 C  CD1  . PHE   C 1 96  ? 1.617   -31.135 16.224  1.00 16.41 ? 100 PHE   C CD1  1 
ATOM   4055 C  CD2  . PHE   C 1 96  ? 2.684   -33.262 16.434  1.00 15.82 ? 100 PHE   C CD2  1 
ATOM   4056 C  CE1  . PHE   C 1 96  ? 2.610   -30.739 15.337  1.00 17.73 ? 100 PHE   C CE1  1 
ATOM   4057 C  CE2  . PHE   C 1 96  ? 3.676   -32.853 15.556  1.00 16.84 ? 100 PHE   C CE2  1 
ATOM   4058 C  CZ   . PHE   C 1 96  ? 3.640   -31.595 15.022  1.00 17.19 ? 100 PHE   C CZ   1 
ATOM   4059 N  N    . ASP   C 1 97  ? 0.121   -29.656 19.509  1.00 14.29 ? 101 ASP   C N    1 
ATOM   4060 C  CA   . ASP   C 1 97  ? -0.670  -28.444 19.635  1.00 15.48 ? 101 ASP   C CA   1 
ATOM   4061 C  C    . ASP   C 1 97  ? 0.126   -27.243 19.126  1.00 16.05 ? 101 ASP   C C    1 
ATOM   4062 O  O    . ASP   C 1 97  ? 1.239   -27.379 18.620  1.00 15.73 ? 101 ASP   C O    1 
ATOM   4063 C  CB   . ASP   C 1 97  ? -1.137  -28.285 21.073  1.00 17.12 ? 101 ASP   C CB   1 
ATOM   4064 C  CG   . ASP   C 1 97  ? -0.042  -28.187 22.121  1.00 19.52 ? 101 ASP   C CG   1 
ATOM   4065 O  OD1  . ASP   C 1 97  ? 1.133   -27.990 21.737  1.00 18.41 ? 101 ASP   C OD1  1 
ATOM   4066 O  OD2  . ASP   C 1 97  ? -0.383  -28.346 23.320  1.00 23.11 ? 101 ASP   C OD2  1 
ATOM   4067 N  N    . ASP   C 1 98  ? -0.477  -26.056 19.251  1.00 17.58 ? 102 ASP   C N    1 
ATOM   4068 C  CA   . ASP   C 1 98  ? 0.143   -24.827 18.777  1.00 19.03 ? 102 ASP   C CA   1 
ATOM   4069 C  C    . ASP   C 1 98  ? 1.504   -24.599 19.424  1.00 18.74 ? 102 ASP   C C    1 
ATOM   4070 O  O    . ASP   C 1 98  ? 2.455   -24.219 18.740  1.00 19.15 ? 102 ASP   C O    1 
ATOM   4071 C  CB   . ASP   C 1 98  ? -0.745  -23.623 19.035  1.00 20.90 ? 102 ASP   C CB   1 
ATOM   4072 C  CG   . ASP   C 1 98  ? -1.867  -23.402 18.041  1.00 25.57 ? 102 ASP   C CG   1 
ATOM   4073 O  OD1  . ASP   C 1 98  ? -1.925  -24.154 17.046  1.00 29.74 ? 102 ASP   C OD1  1 
ATOM   4074 O  OD2  . ASP   C 1 98  ? -2.664  -22.465 18.270  1.00 30.59 ? 102 ASP   C OD2  1 
ATOM   4075 N  N    . ASN   C 1 99  ? 1.599   -24.853 20.733  1.00 17.95 ? 103 ASN   C N    1 
ATOM   4076 C  CA   . ASN   C 1 99  ? 2.841   -24.644 21.456  1.00 18.48 ? 103 ASN   C CA   1 
ATOM   4077 C  C    . ASN   C 1 99  ? 3.932   -25.544 20.876  1.00 17.49 ? 103 ASN   C C    1 
ATOM   4078 O  O    . ASN   C 1 99  ? 5.078   -25.118 20.718  1.00 17.33 ? 103 ASN   C O    1 
ATOM   4079 C  CB   . ASN   C 1 99  ? 2.672   -24.866 22.954  1.00 18.87 ? 103 ASN   C CB   1 
ATOM   4080 C  CG   . ASN   C 1 99  ? 3.970   -24.666 23.699  1.00 19.75 ? 103 ASN   C CG   1 
ATOM   4081 O  OD1  . ASN   C 1 99  ? 4.467   -23.533 23.780  1.00 22.15 ? 103 ASN   C OD1  1 
ATOM   4082 N  ND2  . ASN   C 1 99  ? 4.528   -25.734 24.254  1.00 18.43 ? 103 ASN   C ND2  1 
ATOM   4083 N  N    . LEU   C 1 100 ? 3.585   -26.798 20.562  1.00 15.79 ? 104 LEU   C N    1 
ATOM   4084 C  CA   . LEU   C 1 100 ? 4.570   -27.701 19.979  1.00 14.99 ? 104 LEU   C CA   1 
ATOM   4085 C  C    . LEU   C 1 100 ? 5.022   -27.190 18.615  1.00 15.36 ? 104 LEU   C C    1 
ATOM   4086 O  O    . LEU   C 1 100 ? 6.210   -27.217 18.308  1.00 14.63 ? 104 LEU   C O    1 
ATOM   4087 C  CB   . LEU   C 1 100 ? 4.050   -29.132 19.878  1.00 14.75 ? 104 LEU   C CB   1 
ATOM   4088 C  CG   . LEU   C 1 100 ? 5.012   -30.144 19.246  1.00 15.68 ? 104 LEU   C CG   1 
ATOM   4089 C  CD1  . LEU   C 1 100 ? 6.362   -30.195 19.902  1.00 16.51 ? 104 LEU   C CD1  1 
ATOM   4090 C  CD2  . LEU   C 1 100 ? 4.409   -31.536 19.263  1.00 16.57 ? 104 LEU   C CD2  1 
ATOM   4091 N  N    . ALA   C 1 101 ? 4.081   -26.726 17.792  1.00 16.75 ? 105 ALA   C N    1 
ATOM   4092 C  CA   . ALA   C 1 101 ? 4.436   -26.213 16.477  1.00 17.68 ? 105 ALA   C CA   1 
ATOM   4093 C  C    . ALA   C 1 101 ? 5.388   -25.033 16.620  1.00 18.17 ? 105 ALA   C C    1 
ATOM   4094 O  O    . ALA   C 1 101 ? 6.383   -24.944 15.902  1.00 19.22 ? 105 ALA   C O    1 
ATOM   4095 C  CB   . ALA   C 1 101 ? 3.197   -25.831 15.714  1.00 18.04 ? 105 ALA   C CB   1 
ATOM   4096 N  N    . ASN   C 1 102 ? 5.091   -24.150 17.573  1.00 18.85 ? 106 ASN   C N    1 
ATOM   4097 C  CA   . ASN   C 1 102 ? 5.929   -22.983 17.798  1.00 19.54 ? 106 ASN   C CA   1 
ATOM   4098 C  C    . ASN   C 1 102 ? 7.334   -23.398 18.244  1.00 17.58 ? 106 ASN   C C    1 
ATOM   4099 O  O    . ASN   C 1 102 ? 8.316   -22.800 17.806  1.00 18.74 ? 106 ASN   C O    1 
ATOM   4100 C  CB   . ASN   C 1 102 ? 5.312   -22.052 18.831  1.00 22.39 ? 106 ASN   C CB   1 
ATOM   4101 C  CG   . ASN   C 1 102 ? 4.079   -21.345 18.321  1.00 25.64 ? 106 ASN   C CG   1 
ATOM   4102 O  OD1  . ASN   C 1 102 ? 3.922   -21.133 17.112  1.00 30.29 ? 106 ASN   C OD1  1 
ATOM   4103 N  ND2  . ASN   C 1 102 ? 3.197   -20.962 19.230  1.00 27.74 ? 106 ASN   C ND2  1 
ATOM   4104 N  N    A LEU   C 1 103 ? 7.419   -24.388 19.146  0.50 15.95 ? 107 LEU   C N    1 
ATOM   4105 N  N    B LEU   C 1 103 ? 7.398   -24.380 19.149  0.50 16.45 ? 107 LEU   C N    1 
ATOM   4106 C  CA   A LEU   C 1 103 ? 8.696   -24.916 19.617  0.50 14.77 ? 107 LEU   C CA   1 
ATOM   4107 C  CA   B LEU   C 1 103 ? 8.655   -24.942 19.618  0.50 15.30 ? 107 LEU   C CA   1 
ATOM   4108 C  C    A LEU   C 1 103 ? 9.501   -25.466 18.435  0.50 14.43 ? 107 LEU   C C    1 
ATOM   4109 C  C    B LEU   C 1 103 ? 9.482   -25.453 18.436  0.50 14.72 ? 107 LEU   C C    1 
ATOM   4110 O  O    A LEU   C 1 103 ? 10.696  -25.195 18.312  0.50 14.02 ? 107 LEU   C O    1 
ATOM   4111 O  O    B LEU   C 1 103 ? 10.668  -25.144 18.314  0.50 14.34 ? 107 LEU   C O    1 
ATOM   4112 C  CB   A LEU   C 1 103 ? 8.456   -25.973 20.700  0.50 14.30 ? 107 LEU   C CB   1 
ATOM   4113 C  CB   B LEU   C 1 103 ? 8.275   -26.054 20.593  0.50 15.28 ? 107 LEU   C CB   1 
ATOM   4114 C  CG   A LEU   C 1 103 ? 9.664   -26.799 21.163  0.50 13.80 ? 107 LEU   C CG   1 
ATOM   4115 C  CG   B LEU   C 1 103 ? 9.384   -26.590 21.499  0.50 14.98 ? 107 LEU   C CG   1 
ATOM   4116 C  CD1  A LEU   C 1 103 ? 10.787  -25.934 21.698  0.50 13.50 ? 107 LEU   C CD1  1 
ATOM   4117 C  CD1  B LEU   C 1 103 ? 8.741   -27.446 22.570  0.50 15.00 ? 107 LEU   C CD1  1 
ATOM   4118 C  CD2  A LEU   C 1 103 ? 9.271   -27.817 22.226  0.50 13.95 ? 107 LEU   C CD2  1 
ATOM   4119 C  CD2  B LEU   C 1 103 ? 10.429  -27.369 20.730  0.50 14.80 ? 107 LEU   C CD2  1 
ATOM   4120 N  N    . LEU   C 1 104 ? 8.846   -26.240 17.559  1.00 14.59 ? 108 LEU   C N    1 
ATOM   4121 C  CA   . LEU   C 1 104 ? 9.522   -26.799 16.393  1.00 14.94 ? 108 LEU   C CA   1 
ATOM   4122 C  C    . LEU   C 1 104 ? 10.058  -25.675 15.507  1.00 15.24 ? 108 LEU   C C    1 
ATOM   4123 O  O    . LEU   C 1 104 ? 11.199  -25.726 15.055  1.00 14.96 ? 108 LEU   C O    1 
ATOM   4124 C  CB   . LEU   C 1 104 ? 8.590   -27.713 15.601  1.00 16.13 ? 108 LEU   C CB   1 
ATOM   4125 C  CG   . LEU   C 1 104 ? 8.170   -29.008 16.291  1.00 17.47 ? 108 LEU   C CG   1 
ATOM   4126 C  CD1  . LEU   C 1 104 ? 7.141   -29.720 15.435  1.00 18.86 ? 108 LEU   C CD1  1 
ATOM   4127 C  CD2  . LEU   C 1 104 ? 9.362   -29.906 16.566  1.00 18.49 ? 108 LEU   C CD2  1 
ATOM   4128 N  N    . LEU   C 1 105 ? 9.224   -24.663 15.263  1.00 15.90 ? 109 LEU   C N    1 
ATOM   4129 C  CA   . LEU   C 1 105 ? 9.613   -23.568 14.391  1.00 17.58 ? 109 LEU   C CA   1 
ATOM   4130 C  C    . LEU   C 1 105 ? 10.761  -22.777 15.019  1.00 15.71 ? 109 LEU   C C    1 
ATOM   4131 O  O    . LEU   C 1 105 ? 11.677  -22.365 14.313  1.00 16.05 ? 109 LEU   C O    1 
ATOM   4132 C  CB   . LEU   C 1 105 ? 8.419   -22.672 14.065  1.00 20.45 ? 109 LEU   C CB   1 
ATOM   4133 C  CG   . LEU   C 1 105 ? 7.269   -23.347 13.313  1.00 24.92 ? 109 LEU   C CG   1 
ATOM   4134 C  CD1  . LEU   C 1 105 ? 5.967   -22.542 13.321  1.00 26.84 ? 109 LEU   C CD1  1 
ATOM   4135 C  CD2  . LEU   C 1 105 ? 7.722   -23.629 11.898  1.00 27.99 ? 109 LEU   C CD2  1 
ATOM   4136 N  N    . ALA   C 1 106 ? 10.736  -22.582 16.343  1.00 14.58 ? 110 ALA   C N    1 
ATOM   4137 C  CA   . ALA   C 1 106 ? 11.801  -21.833 17.002  1.00 14.06 ? 110 ALA   C CA   1 
ATOM   4138 C  C    . ALA   C 1 106 ? 13.117  -22.607 16.914  1.00 13.16 ? 110 ALA   C C    1 
ATOM   4139 O  O    . ALA   C 1 106 ? 14.186  -22.023 16.735  1.00 13.32 ? 110 ALA   C O    1 
ATOM   4140 C  CB   . ALA   C 1 106 ? 11.452  -21.535 18.443  1.00 14.05 ? 110 ALA   C CB   1 
ATOM   4141 N  N    . PHE   C 1 107 ? 13.036  -23.931 17.063  1.00 12.54 ? 111 PHE   C N    1 
ATOM   4142 C  CA   . PHE   C 1 107 ? 14.203  -24.784 16.909  1.00 11.98 ? 111 PHE   C CA   1 
ATOM   4143 C  C    . PHE   C 1 107 ? 14.755  -24.675 15.489  1.00 12.50 ? 111 PHE   C C    1 
ATOM   4144 O  O    . PHE   C 1 107 ? 15.956  -24.515 15.308  1.00 12.41 ? 111 PHE   C O    1 
ATOM   4145 C  CB   . PHE   C 1 107 ? 13.812  -26.214 17.282  1.00 11.93 ? 111 PHE   C CB   1 
ATOM   4146 C  CG   . PHE   C 1 107 ? 14.936  -27.223 17.108  1.00 12.02 ? 111 PHE   C CG   1 
ATOM   4147 C  CD1  . PHE   C 1 107 ? 15.139  -27.884 15.907  1.00 12.14 ? 111 PHE   C CD1  1 
ATOM   4148 C  CD2  . PHE   C 1 107 ? 15.775  -27.526 18.170  1.00 12.25 ? 111 PHE   C CD2  1 
ATOM   4149 C  CE1  . PHE   C 1 107 ? 16.171  -28.803 15.773  1.00 12.37 ? 111 PHE   C CE1  1 
ATOM   4150 C  CE2  . PHE   C 1 107 ? 16.783  -28.467 18.032  1.00 12.65 ? 111 PHE   C CE2  1 
ATOM   4151 C  CZ   . PHE   C 1 107 ? 16.978  -29.099 16.833  1.00 12.67 ? 111 PHE   C CZ   1 
ATOM   4152 N  N    . LEU   C 1 108 ? 13.877  -24.759 14.485  1.00 13.12 ? 112 LEU   C N    1 
ATOM   4153 C  CA   . LEU   C 1 108 ? 14.325  -24.682 13.101  1.00 14.51 ? 112 LEU   C CA   1 
ATOM   4154 C  C    . LEU   C 1 108 ? 14.931  -23.312 12.797  1.00 14.74 ? 112 LEU   C C    1 
ATOM   4155 O  O    . LEU   C 1 108 ? 15.937  -23.231 12.089  1.00 15.42 ? 112 LEU   C O    1 
ATOM   4156 C  CB   . LEU   C 1 108 ? 13.178  -25.032 12.163  1.00 16.48 ? 112 LEU   C CB   1 
ATOM   4157 C  CG   . LEU   C 1 108 ? 12.758  -26.503 12.224  1.00 18.43 ? 112 LEU   C CG   1 
ATOM   4158 C  CD1  . LEU   C 1 108 ? 11.424  -26.717 11.540  1.00 20.10 ? 112 LEU   C CD1  1 
ATOM   4159 C  CD2  . LEU   C 1 108 ? 13.836  -27.395 11.638  1.00 19.65 ? 112 LEU   C CD2  1 
ATOM   4160 N  N    . ARG   C 1 109 ? 14.381  -22.254 13.400  1.00 14.63 ? 113 ARG   C N    1 
ATOM   4161 C  CA   . ARG   C 1 109 ? 14.862  -20.903 13.157  1.00 16.32 ? 113 ARG   C CA   1 
ATOM   4162 C  C    . ARG   C 1 109 ? 16.273  -20.688 13.700  1.00 14.91 ? 113 ARG   C C    1 
ATOM   4163 O  O    . ARG   C 1 109 ? 16.941  -19.734 13.307  1.00 17.38 ? 113 ARG   C O    1 
ATOM   4164 C  CB   . ARG   C 1 109 ? 13.863  -19.867 13.673  1.00 18.33 ? 113 ARG   C CB   1 
ATOM   4165 C  CG   . ARG   C 1 109 ? 12.705  -19.754 12.689  1.00 22.04 ? 113 ARG   C CG   1 
ATOM   4166 C  CD   . ARG   C 1 109 ? 11.837  -18.534 12.880  1.00 26.17 ? 113 ARG   C CD   1 
ATOM   4167 N  NE   . ARG   C 1 109 ? 11.455  -18.395 14.286  1.00 28.86 ? 113 ARG   C NE   1 
ATOM   4168 C  CZ   . ARG   C 1 109 ? 10.314  -18.781 14.858  1.00 30.15 ? 113 ARG   C CZ   1 
ATOM   4169 N  NH1  . ARG   C 1 109 ? 10.194  -18.700 16.168  1.00 28.75 ? 113 ARG   C NH1  1 
ATOM   4170 N  NH2  . ARG   C 1 109 ? 9.317   -19.282 14.147  1.00 32.70 ? 113 ARG   C NH2  1 
ATOM   4171 N  N    . ARG   C 1 110 ? 16.758  -21.587 14.558  1.00 13.77 ? 114 ARG   C N    1 
ATOM   4172 C  CA   . ARG   C 1 110 ? 18.140  -21.517 15.007  1.00 14.03 ? 114 ARG   C CA   1 
ATOM   4173 C  C    . ARG   C 1 110 ? 19.114  -22.142 14.008  1.00 14.16 ? 114 ARG   C C    1 
ATOM   4174 O  O    . ARG   C 1 110 ? 20.326  -22.090 14.217  1.00 14.79 ? 114 ARG   C O    1 
ATOM   4175 C  CB   . ARG   C 1 110 ? 18.286  -22.149 16.392  1.00 14.54 ? 114 ARG   C CB   1 
ATOM   4176 C  CG   . ARG   C 1 110 ? 17.695  -21.210 17.432  1.00 15.39 ? 114 ARG   C CG   1 
ATOM   4177 C  CD   . ARG   C 1 110 ? 18.116  -21.507 18.829  1.00 15.19 ? 114 ARG   C CD   1 
ATOM   4178 N  NE   . ARG   C 1 110 ? 19.570  -21.493 19.026  1.00 14.32 ? 114 ARG   C NE   1 
ATOM   4179 C  CZ   . ARG   C 1 110 ? 20.317  -20.431 19.319  1.00 14.14 ? 114 ARG   C CZ   1 
ATOM   4180 N  NH1  . ARG   C 1 110 ? 19.799  -19.214 19.339  1.00 14.38 ? 114 ARG   C NH1  1 
ATOM   4181 N  NH2  . ARG   C 1 110 ? 21.594  -20.589 19.614  1.00 14.07 ? 114 ARG   C NH2  1 
ATOM   4182 N  N    . GLN   C 1 111 ? 18.595  -22.696 12.913  1.00 13.87 ? 115 GLN   C N    1 
ATOM   4183 C  CA   . GLN   C 1 111 ? 19.420  -23.371 11.928  1.00 14.06 ? 115 GLN   C CA   1 
ATOM   4184 C  C    . GLN   C 1 111 ? 19.534  -22.519 10.667  1.00 14.01 ? 115 GLN   C C    1 
ATOM   4185 O  O    . GLN   C 1 111 ? 18.539  -21.996 10.164  1.00 15.01 ? 115 GLN   C O    1 
ATOM   4186 C  CB   . GLN   C 1 111 ? 18.818  -24.720 11.542  1.00 13.92 ? 115 GLN   C CB   1 
ATOM   4187 C  CG   . GLN   C 1 111 ? 18.299  -25.548 12.717  1.00 13.50 ? 115 GLN   C CG   1 
ATOM   4188 C  CD   . GLN   C 1 111 ? 19.281  -25.711 13.850  1.00 13.19 ? 115 GLN   C CD   1 
ATOM   4189 O  OE1  . GLN   C 1 111 ? 20.490  -25.852 13.645  1.00 13.57 ? 115 GLN   C OE1  1 
ATOM   4190 N  NE2  . GLN   C 1 111 ? 18.754  -25.683 15.065  1.00 12.52 ? 115 GLN   C NE2  1 
ATOM   4191 N  N    . PRO   C 1 112 ? 20.732  -22.415 10.060  1.00 14.29 ? 116 PRO   C N    1 
ATOM   4192 C  CA   . PRO   C 1 112 ? 20.857  -21.730 8.771   1.00 15.01 ? 116 PRO   C CA   1 
ATOM   4193 C  C    . PRO   C 1 112 ? 20.047  -22.402 7.674   1.00 14.77 ? 116 PRO   C C    1 
ATOM   4194 O  O    . PRO   C 1 112 ? 19.974  -23.630 7.602   1.00 14.50 ? 116 PRO   C O    1 
ATOM   4195 C  CB   . PRO   C 1 112 ? 22.345  -21.751 8.432   1.00 16.63 ? 116 PRO   C CB   1 
ATOM   4196 C  CG   . PRO   C 1 112 ? 22.985  -22.660 9.424   1.00 18.28 ? 116 PRO   C CG   1 
ATOM   4197 C  CD   . PRO   C 1 112 ? 22.018  -22.920 10.558  1.00 15.76 ? 116 PRO   C CD   1 
ATOM   4198 N  N    . GLN   C 1 113 ? 19.450  -21.559 6.829   1.00 15.59 ? 117 GLN   C N    1 
ATOM   4199 C  CA   . GLN   C 1 113 ? 18.635  -22.010 5.719   1.00 16.21 ? 117 GLN   C CA   1 
ATOM   4200 C  C    . GLN   C 1 113 ? 19.460  -22.018 4.442   1.00 15.72 ? 117 GLN   C C    1 
ATOM   4201 O  O    . GLN   C 1 113 ? 20.395  -21.227 4.301   1.00 16.75 ? 117 GLN   C O    1 
ATOM   4202 C  CB   . GLN   C 1 113 ? 17.425  -21.103 5.515   1.00 18.16 ? 117 GLN   C CB   1 
ATOM   4203 C  CG   . GLN   C 1 113 ? 16.421  -21.228 6.654   1.00 20.84 ? 117 GLN   C CG   1 
ATOM   4204 C  CD   . GLN   C 1 113 ? 15.077  -20.612 6.343   1.00 25.45 ? 117 GLN   C CD   1 
ATOM   4205 O  OE1  . GLN   C 1 113 ? 14.249  -21.193 5.628   1.00 30.34 ? 117 GLN   C OE1  1 
ATOM   4206 N  NE2  . GLN   C 1 113 ? 14.841  -19.440 6.909   1.00 29.71 ? 117 GLN   C NE2  1 
ATOM   4207 N  N    . PRO   C 1 114 ? 19.098  -22.850 3.439   1.00 15.80 ? 118 PRO   C N    1 
ATOM   4208 C  CA   . PRO   C 1 114 ? 17.991  -23.817 3.532   1.00 15.68 ? 118 PRO   C CA   1 
ATOM   4209 C  C    . PRO   C 1 114 ? 18.190  -24.995 4.480   1.00 15.18 ? 118 PRO   C C    1 
ATOM   4210 O  O    . PRO   C 1 114 ? 19.311  -25.491 4.606   1.00 15.44 ? 118 PRO   C O    1 
ATOM   4211 C  CB   . PRO   C 1 114 ? 17.841  -24.342 2.098   1.00 17.03 ? 118 PRO   C CB   1 
ATOM   4212 C  CG   . PRO   C 1 114 ? 18.649  -23.436 1.245   1.00 17.31 ? 118 PRO   C CG   1 
ATOM   4213 C  CD   . PRO   C 1 114 ? 19.686  -22.782 2.097   1.00 16.95 ? 118 PRO   C CD   1 
ATOM   4214 N  N    . TRP   C 1 115 ? 17.066  -25.417 5.085   1.00 15.11 ? 119 TRP   C N    1 
ATOM   4215 C  CA   . TRP   C 1 115 ? 16.932  -26.579 5.954   1.00 16.25 ? 119 TRP   C CA   1 
ATOM   4216 C  C    . TRP   C 1 115 ? 16.518  -27.770 5.101   1.00 15.16 ? 119 TRP   C C    1 
ATOM   4217 O  O    . TRP   C 1 115 ? 15.618  -27.609 4.289   1.00 15.12 ? 119 TRP   C O    1 
ATOM   4218 C  CB   . TRP   C 1 115 ? 15.803  -26.392 6.994   1.00 18.25 ? 119 TRP   C CB   1 
ATOM   4219 C  CG   . TRP   C 1 115 ? 15.799  -25.152 7.841   1.00 17.75 ? 119 TRP   C CG   1 
ATOM   4220 C  CD1  . TRP   C 1 115 ? 16.868  -24.486 8.339   1.00 18.43 ? 119 TRP   C CD1  1 
ATOM   4221 C  CD2  . TRP   C 1 115 ? 14.631  -24.415 8.258   1.00 18.66 ? 119 TRP   C CD2  1 
ATOM   4222 N  NE1  . TRP   C 1 115 ? 16.457  -23.397 9.054   1.00 19.42 ? 119 TRP   C NE1  1 
ATOM   4223 C  CE2  . TRP   C 1 115 ? 15.088  -23.319 9.016   1.00 19.95 ? 119 TRP   C CE2  1 
ATOM   4224 C  CE3  . TRP   C 1 115 ? 13.252  -24.569 8.067   1.00 22.28 ? 119 TRP   C CE3  1 
ATOM   4225 C  CZ2  . TRP   C 1 115 ? 14.224  -22.377 9.574   1.00 20.97 ? 119 TRP   C CZ2  1 
ATOM   4226 C  CZ3  . TRP   C 1 115 ? 12.397  -23.636 8.622   1.00 22.92 ? 119 TRP   C CZ3  1 
ATOM   4227 C  CH2  . TRP   C 1 115 ? 12.877  -22.552 9.364   1.00 22.21 ? 119 TRP   C CH2  1 
ATOM   4228 N  N    . CYS   C 1 116 ? 17.095  -28.952 5.345   1.00 13.60 ? 120 CYS   C N    1 
ATOM   4229 C  CA   . CYS   C 1 116 ? 16.629  -30.168 4.695   1.00 14.10 ? 120 CYS   C CA   1 
ATOM   4230 C  C    . CYS   C 1 116 ? 16.399  -31.253 5.741   1.00 13.46 ? 120 CYS   C C    1 
ATOM   4231 O  O    . CYS   C 1 116 ? 17.354  -31.722 6.354   1.00 13.46 ? 120 CYS   C O    1 
ATOM   4232 C  CB   . CYS   C 1 116 ? 17.631  -30.650 3.656   1.00 14.87 ? 120 CYS   C CB   1 
ATOM   4233 S  SG   . CYS   C 1 116 ? 16.973  -31.979 2.620   1.00 16.74 ? 120 CYS   C SG   1 
ATOM   4234 N  N    . LEU   C 1 117 ? 15.130  -31.646 5.911   1.00 13.12 ? 121 LEU   C N    1 
ATOM   4235 C  CA   . LEU   C 1 117 ? 14.792  -32.788 6.744   1.00 13.31 ? 121 LEU   C CA   1 
ATOM   4236 C  C    . LEU   C 1 117 ? 15.267  -34.058 6.041   1.00 13.12 ? 121 LEU   C C    1 
ATOM   4237 O  O    . LEU   C 1 117 ? 15.074  -34.204 4.832   1.00 14.86 ? 121 LEU   C O    1 
ATOM   4238 C  CB   . LEU   C 1 117 ? 13.289  -32.857 6.976   1.00 15.19 ? 121 LEU   C CB   1 
ATOM   4239 C  CG   . LEU   C 1 117 ? 12.651  -31.700 7.739   1.00 17.17 ? 121 LEU   C CG   1 
ATOM   4240 C  CD1  . LEU   C 1 117 ? 11.138  -31.800 7.611   1.00 18.12 ? 121 LEU   C CD1  1 
ATOM   4241 C  CD2  . LEU   C 1 117 ? 13.063  -31.721 9.197   1.00 18.76 ? 121 LEU   C CD2  1 
ATOM   4242 N  N    . VAL   C 1 118 ? 15.853  -34.974 6.808   1.00 12.40 ? 122 VAL   C N    1 
ATOM   4243 C  CA   . VAL   C 1 118 ? 16.329  -36.256 6.313   1.00 13.17 ? 122 VAL   C CA   1 
ATOM   4244 C  C    . VAL   C 1 118 ? 15.734  -37.355 7.185   1.00 12.63 ? 122 VAL   C C    1 
ATOM   4245 O  O    . VAL   C 1 118 ? 15.977  -37.374 8.387   1.00 12.31 ? 122 VAL   C O    1 
ATOM   4246 C  CB   . VAL   C 1 118 ? 17.866  -36.352 6.317   1.00 13.87 ? 122 VAL   C CB   1 
ATOM   4247 C  CG1  . VAL   C 1 118 ? 18.360  -37.701 5.799   1.00 14.42 ? 122 VAL   C CG1  1 
ATOM   4248 C  CG2  . VAL   C 1 118 ? 18.524  -35.221 5.531   1.00 14.72 ? 122 VAL   C CG2  1 
ATOM   4249 N  N    . ALA   C 1 119 ? 14.952  -38.264 6.589   1.00 13.14 ? 123 ALA   C N    1 
ATOM   4250 C  CA   . ALA   C 1 119 ? 14.276  -39.305 7.348   1.00 13.07 ? 123 ALA   C CA   1 
ATOM   4251 C  C    . ALA   C 1 119 ? 14.221  -40.588 6.528   1.00 13.55 ? 123 ALA   C C    1 
ATOM   4252 O  O    . ALA   C 1 119 ? 14.082  -40.557 5.306   1.00 13.99 ? 123 ALA   C O    1 
ATOM   4253 C  CB   . ALA   C 1 119 ? 12.888  -38.844 7.742   1.00 12.96 ? 123 ALA   C CB   1 
ATOM   4254 N  N    . HIS   C 1 120 ? 14.315  -41.726 7.217   1.00 14.15 ? 124 HIS   C N    1 
ATOM   4255 C  CA   . HIS   C 1 120 ? 14.406  -43.014 6.551   1.00 15.14 ? 124 HIS   C CA   1 
ATOM   4256 C  C    . HIS   C 1 120 ? 13.008  -43.542 6.234   1.00 15.11 ? 124 HIS   C C    1 
ATOM   4257 O  O    . HIS   C 1 120 ? 12.215  -43.794 7.126   1.00 15.28 ? 124 HIS   C O    1 
ATOM   4258 C  CB   . HIS   C 1 120 ? 15.209  -43.976 7.426   1.00 16.08 ? 124 HIS   C CB   1 
ATOM   4259 C  CG   . HIS   C 1 120 ? 15.792  -45.088 6.642   1.00 18.74 ? 124 HIS   C CG   1 
ATOM   4260 N  ND1  . HIS   C 1 120 ? 16.864  -44.893 5.799   1.00 20.64 ? 124 HIS   C ND1  1 
ATOM   4261 C  CD2  . HIS   C 1 120 ? 15.454  -46.375 6.541   1.00 20.31 ? 124 HIS   C CD2  1 
ATOM   4262 C  CE1  . HIS   C 1 120 ? 17.165  -46.049 5.231   1.00 21.23 ? 124 HIS   C CE1  1 
ATOM   4263 N  NE2  . HIS   C 1 120 ? 16.317  -46.963 5.668   1.00 21.34 ? 124 HIS   C NE2  1 
ATOM   4264 N  N    . ASN   C 1 121 ? 12.709  -43.714 4.947   1.00 15.31 ? 125 ASN   C N    1 
ATOM   4265 C  CA   . ASN   C 1 121 ? 11.339  -43.936 4.514   1.00 16.27 ? 125 ASN   C CA   1 
ATOM   4266 C  C    . ASN   C 1 121 ? 10.498  -42.723 4.890   1.00 15.51 ? 125 ASN   C C    1 
ATOM   4267 O  O    . ASN   C 1 121 ? 9.301   -42.835 5.133   1.00 16.13 ? 125 ASN   C O    1 
ATOM   4268 C  CB   . ASN   C 1 121 ? 10.732  -45.238 5.034   1.00 17.58 ? 125 ASN   C CB   1 
ATOM   4269 C  CG   . ASN   C 1 121 ? 10.460  -46.240 3.942   1.00 19.24 ? 125 ASN   C CG   1 
ATOM   4270 O  OD1  . ASN   C 1 121 ? 10.119  -45.864 2.816   1.00 21.46 ? 125 ASN   C OD1  1 
ATOM   4271 N  ND2  . ASN   C 1 121 ? 10.617  -47.513 4.262   1.00 21.03 ? 125 ASN   C ND2  1 
ATOM   4272 N  N    . GLY   C 1 122 ? 11.126  -41.542 4.883   1.00 14.99 ? 126 GLY   C N    1 
ATOM   4273 C  CA   . GLY   C 1 122 ? 10.433  -40.321 5.236   1.00 14.83 ? 126 GLY   C CA   1 
ATOM   4274 C  C    . GLY   C 1 122 ? 9.236   -40.019 4.338   1.00 14.56 ? 126 GLY   C C    1 
ATOM   4275 O  O    . GLY   C 1 122 ? 8.264   -39.438 4.803   1.00 14.39 ? 126 GLY   C O    1 
ATOM   4276 N  N    . ASP   C 1 123 ? 9.282   -40.401 3.056   1.00 16.11 ? 127 ASP   C N    1 
ATOM   4277 C  CA   . ASP   C 1 123 ? 8.180   -40.092 2.161   1.00 16.69 ? 127 ASP   C CA   1 
ATOM   4278 C  C    . ASP   C 1 123 ? 6.930   -40.878 2.535   1.00 17.04 ? 127 ASP   C C    1 
ATOM   4279 O  O    . ASP   C 1 123 ? 5.825   -40.419 2.253   1.00 18.64 ? 127 ASP   C O    1 
ATOM   4280 C  CB   . ASP   C 1 123 ? 8.559   -40.347 0.713   1.00 17.84 ? 127 ASP   C CB   1 
ATOM   4281 C  CG   . ASP   C 1 123 ? 9.596   -39.387 0.153   1.00 18.84 ? 127 ASP   C CG   1 
ATOM   4282 O  OD1  . ASP   C 1 123 ? 10.020  -38.482 0.920   1.00 21.77 ? 127 ASP   C OD1  1 
ATOM   4283 O  OD2  . ASP   C 1 123 ? 9.908   -39.500 -1.053  1.00 22.90 ? 127 ASP   C OD2  1 
ATOM   4284 N  N    . ARG   C 1 124 ? 7.123   -42.044 3.161   1.00 16.54 ? 128 ARG   C N    1 
ATOM   4285 C  CA   . ARG   C 1 124 ? 6.020   -42.898 3.571   1.00 16.98 ? 128 ARG   C CA   1 
ATOM   4286 C  C    . ARG   C 1 124 ? 5.525   -42.550 4.975   1.00 16.05 ? 128 ARG   C C    1 
ATOM   4287 O  O    . ARG   C 1 124 ? 4.324   -42.607 5.248   1.00 16.77 ? 128 ARG   C O    1 
ATOM   4288 C  CB   . ARG   C 1 124 ? 6.503   -44.350 3.549   1.00 18.80 ? 128 ARG   C CB   1 
ATOM   4289 C  CG   . ARG   C 1 124 ? 5.406   -45.355 3.841   1.00 20.65 ? 128 ARG   C CG   1 
ATOM   4290 C  CD   . ARG   C 1 124 ? 5.991   -46.750 3.941   1.00 21.91 ? 128 ARG   C CD   1 
ATOM   4291 N  NE   . ARG   C 1 124 ? 6.463   -47.276 2.663   1.00 23.51 ? 128 ARG   C NE   1 
ATOM   4292 C  CZ   . ARG   C 1 124 ? 6.993   -48.482 2.545   1.00 24.03 ? 128 ARG   C CZ   1 
ATOM   4293 N  NH1  . ARG   C 1 124 ? 7.384   -48.886 1.360   1.00 25.43 ? 128 ARG   C NH1  1 
ATOM   4294 N  NH2  . ARG   C 1 124 ? 7.138   -49.261 3.609   1.00 24.85 ? 128 ARG   C NH2  1 
ATOM   4295 N  N    . TYR   C 1 125 ? 6.461   -42.247 5.881   1.00 14.91 ? 129 TYR   C N    1 
ATOM   4296 C  CA   . TYR   C 1 125 ? 6.150   -42.143 7.300   1.00 14.42 ? 129 TYR   C CA   1 
ATOM   4297 C  C    . TYR   C 1 125 ? 6.230   -40.692 7.784   1.00 13.45 ? 129 TYR   C C    1 
ATOM   4298 O  O    . TYR   C 1 125 ? 5.210   -40.035 7.962   1.00 13.78 ? 129 TYR   C O    1 
ATOM   4299 C  CB   . TYR   C 1 125 ? 7.086   -43.080 8.071   1.00 14.71 ? 129 TYR   C CB   1 
ATOM   4300 C  CG   . TYR   C 1 125 ? 6.956   -44.556 7.716   1.00 15.39 ? 129 TYR   C CG   1 
ATOM   4301 C  CD1  . TYR   C 1 125 ? 5.718   -45.180 7.604   1.00 16.07 ? 129 TYR   C CD1  1 
ATOM   4302 C  CD2  . TYR   C 1 125 ? 8.089   -45.332 7.509   1.00 16.63 ? 129 TYR   C CD2  1 
ATOM   4303 C  CE1  . TYR   C 1 125 ? 5.619   -46.530 7.304   1.00 16.95 ? 129 TYR   C CE1  1 
ATOM   4304 C  CE2  . TYR   C 1 125 ? 8.005   -46.678 7.194   1.00 17.40 ? 129 TYR   C CE2  1 
ATOM   4305 C  CZ   . TYR   C 1 125 ? 6.764   -47.283 7.101   1.00 17.72 ? 129 TYR   C CZ   1 
ATOM   4306 O  OH   . TYR   C 1 125 ? 6.659   -48.609 6.768   1.00 20.18 ? 129 TYR   C OH   1 
ATOM   4307 N  N    . ASP   C 1 126 ? 7.448   -40.188 7.992   1.00 12.69 ? 130 ASP   C N    1 
ATOM   4308 C  CA   . ASP   C 1 126 ? 7.654   -38.997 8.807   1.00 13.08 ? 130 ASP   C CA   1 
ATOM   4309 C  C    . ASP   C 1 126 ? 7.154   -37.715 8.139   1.00 12.98 ? 130 ASP   C C    1 
ATOM   4310 O  O    . ASP   C 1 126 ? 6.553   -36.867 8.791   1.00 13.19 ? 130 ASP   C O    1 
ATOM   4311 C  CB   . ASP   C 1 126 ? 9.120   -38.868 9.168   1.00 12.94 ? 130 ASP   C CB   1 
ATOM   4312 C  CG   . ASP   C 1 126 ? 9.715   -40.179 9.657   1.00 13.65 ? 130 ASP   C CG   1 
ATOM   4313 O  OD1  . ASP   C 1 126 ? 10.020  -41.042 8.800   1.00 14.40 ? 130 ASP   C OD1  1 
ATOM   4314 O  OD2  . ASP   C 1 126 ? 9.802   -40.355 10.889  1.00 14.33 ? 130 ASP   C OD2  1 
ATOM   4315 N  N    . PHE   C 1 127 ? 7.404   -37.563 6.838   1.00 13.46 ? 131 PHE   C N    1 
ATOM   4316 C  CA   . PHE   C 1 127 ? 7.079   -36.319 6.159   1.00 13.37 ? 131 PHE   C CA   1 
ATOM   4317 C  C    . PHE   C 1 127 ? 5.566   -36.139 6.031   1.00 13.76 ? 131 PHE   C C    1 
ATOM   4318 O  O    . PHE   C 1 127 ? 5.043   -35.096 6.418   1.00 13.94 ? 131 PHE   C O    1 
ATOM   4319 C  CB   . PHE   C 1 127 ? 7.792   -36.225 4.810   1.00 13.75 ? 131 PHE   C CB   1 
ATOM   4320 C  CG   . PHE   C 1 127 ? 9.307   -36.332 4.864   1.00 13.78 ? 131 PHE   C CG   1 
ATOM   4321 C  CD1  . PHE   C 1 127 ? 10.035  -35.913 5.976   1.00 14.52 ? 131 PHE   C CD1  1 
ATOM   4322 C  CD2  . PHE   C 1 127 ? 10.006  -36.831 3.772   1.00 13.85 ? 131 PHE   C CD2  1 
ATOM   4323 C  CE1  . PHE   C 1 127 ? 11.416  -36.013 5.999   1.00 13.97 ? 131 PHE   C CE1  1 
ATOM   4324 C  CE2  . PHE   C 1 127 ? 11.385  -36.924 3.795   1.00 14.27 ? 131 PHE   C CE2  1 
ATOM   4325 C  CZ   . PHE   C 1 127 ? 12.088  -36.528 4.919   1.00 14.51 ? 131 PHE   C CZ   1 
ATOM   4326 N  N    . PRO   C 1 128 ? 4.801   -37.108 5.489   1.00 14.10 ? 132 PRO   C N    1 
ATOM   4327 C  CA   . PRO   C 1 128 ? 3.356   -36.924 5.390   1.00 14.86 ? 132 PRO   C CA   1 
ATOM   4328 C  C    . PRO   C 1 128 ? 2.676   -36.823 6.755   1.00 13.77 ? 132 PRO   C C    1 
ATOM   4329 O  O    . PRO   C 1 128 ? 1.683   -36.114 6.885   1.00 14.26 ? 132 PRO   C O    1 
ATOM   4330 C  CB   . PRO   C 1 128 ? 2.871   -38.121 4.555   1.00 15.11 ? 132 PRO   C CB   1 
ATOM   4331 C  CG   . PRO   C 1 128 ? 3.981   -39.135 4.648   1.00 16.20 ? 132 PRO   C CG   1 
ATOM   4332 C  CD   . PRO   C 1 128 ? 5.263   -38.367 4.877   1.00 15.45 ? 132 PRO   C CD   1 
ATOM   4333 N  N    . LEU   C 1 129 ? 3.206   -37.491 7.787   1.00 13.75 ? 133 LEU   C N    1 
ATOM   4334 C  CA   . LEU   C 1 129 ? 2.579   -37.382 9.096   1.00 13.37 ? 133 LEU   C CA   1 
ATOM   4335 C  C    . LEU   C 1 129 ? 2.824   -35.988 9.690   1.00 13.24 ? 133 LEU   C C    1 
ATOM   4336 O  O    . LEU   C 1 129 ? 1.913   -35.370 10.233  1.00 13.57 ? 133 LEU   C O    1 
ATOM   4337 C  CB   . LEU   C 1 129 ? 3.024   -38.485 10.049  1.00 13.57 ? 133 LEU   C CB   1 
ATOM   4338 C  CG   . LEU   C 1 129 ? 2.353   -38.441 11.427  1.00 13.78 ? 133 LEU   C CG   1 
ATOM   4339 C  CD1  . LEU   C 1 129 ? 0.845   -38.377 11.343  1.00 14.55 ? 133 LEU   C CD1  1 
ATOM   4340 C  CD2  . LEU   C 1 129 ? 2.784   -39.643 12.253  1.00 14.43 ? 133 LEU   C CD2  1 
ATOM   4341 N  N    . LEU   C 1 130 ? 4.053   -35.466 9.580   1.00 12.95 ? 134 LEU   C N    1 
ATOM   4342 C  CA   . LEU   C 1 130 ? 4.314   -34.106 10.031  1.00 13.33 ? 134 LEU   C CA   1 
ATOM   4343 C  C    . LEU   C 1 130 ? 3.404   -33.116 9.303   1.00 14.18 ? 134 LEU   C C    1 
ATOM   4344 O  O    . LEU   C 1 130 ? 2.818   -32.237 9.924   1.00 14.36 ? 134 LEU   C O    1 
ATOM   4345 C  CB   . LEU   C 1 130 ? 5.785   -33.754 9.823   1.00 13.21 ? 134 LEU   C CB   1 
ATOM   4346 C  CG   . LEU   C 1 130 ? 6.191   -32.334 10.228  1.00 14.18 ? 134 LEU   C CG   1 
ATOM   4347 C  CD1  . LEU   C 1 130 ? 5.925   -32.069 11.700  1.00 14.42 ? 134 LEU   C CD1  1 
ATOM   4348 C  CD2  . LEU   C 1 130 ? 7.650   -32.115 9.893   1.00 14.74 ? 134 LEU   C CD2  1 
ATOM   4349 N  N    A GLN   C 1 131 ? 3.292   -33.264 7.983   0.50 14.51 ? 135 GLN   C N    1 
ATOM   4350 N  N    B GLN   C 1 131 ? 3.309   -33.245 7.976   0.50 15.06 ? 135 GLN   C N    1 
ATOM   4351 C  CA   A GLN   C 1 131 ? 2.447   -32.376 7.206   0.50 15.40 ? 135 GLN   C CA   1 
ATOM   4352 C  CA   B GLN   C 1 131 ? 2.435   -32.383 7.196   0.50 16.59 ? 135 GLN   C CA   1 
ATOM   4353 C  C    A GLN   C 1 131 ? 0.988   -32.472 7.661   0.50 15.76 ? 135 GLN   C C    1 
ATOM   4354 C  C    B GLN   C 1 131 ? 0.995   -32.467 7.700   0.50 16.47 ? 135 GLN   C C    1 
ATOM   4355 O  O    A GLN   C 1 131 ? 0.302   -31.456 7.718   0.50 16.61 ? 135 GLN   C O    1 
ATOM   4356 O  O    B GLN   C 1 131 ? 0.334   -31.442 7.833   0.50 17.33 ? 135 GLN   C O    1 
ATOM   4357 C  CB   A GLN   C 1 131 ? 2.595   -32.687 5.719   0.50 15.85 ? 135 GLN   C CB   1 
ATOM   4358 C  CB   B GLN   C 1 131 ? 2.496   -32.727 5.708   0.50 18.24 ? 135 GLN   C CB   1 
ATOM   4359 C  CG   A GLN   C 1 131 ? 2.026   -31.600 4.818   0.50 16.13 ? 135 GLN   C CG   1 
ATOM   4360 C  CG   B GLN   C 1 131 ? 3.699   -32.137 4.986   0.50 19.93 ? 135 GLN   C CG   1 
ATOM   4361 C  CD   A GLN   C 1 131 ? 2.976   -30.440 4.623   0.50 17.35 ? 135 GLN   C CD   1 
ATOM   4362 C  CD   B GLN   C 1 131 ? 3.644   -30.627 4.869   0.50 22.13 ? 135 GLN   C CD   1 
ATOM   4363 O  OE1  A GLN   C 1 131 ? 3.209   -29.611 5.514   0.50 19.18 ? 135 GLN   C OE1  1 
ATOM   4364 O  OE1  B GLN   C 1 131 ? 3.040   -29.931 5.693   0.50 24.68 ? 135 GLN   C OE1  1 
ATOM   4365 N  NE2  A GLN   C 1 131 ? 3.574   -30.409 3.446   0.50 17.61 ? 135 GLN   C NE2  1 
ATOM   4366 N  NE2  B GLN   C 1 131 ? 4.303   -30.102 3.848   0.50 23.09 ? 135 GLN   C NE2  1 
ATOM   4367 N  N    . ALA   C 1 132 ? 0.515   -33.685 7.974   1.00 15.92 ? 136 ALA   C N    1 
ATOM   4368 C  CA   . ALA   C 1 132 ? -0.847  -33.891 8.456   1.00 16.57 ? 136 ALA   C CA   1 
ATOM   4369 C  C    . ALA   C 1 132 ? -1.072  -33.205 9.804   1.00 16.82 ? 136 ALA   C C    1 
ATOM   4370 O  O    . ALA   C 1 132 ? -2.102  -32.564 10.019  1.00 19.36 ? 136 ALA   C O    1 
ATOM   4371 C  CB   . ALA   C 1 132 ? -1.146  -35.379 8.567   1.00 16.94 ? 136 ALA   C CB   1 
ATOM   4372 N  N    . GLU   C 1 133 ? -0.123  -33.372 10.726  1.00 17.34 ? 137 GLU   C N    1 
ATOM   4373 C  CA   . GLU   C 1 133 ? -0.251  -32.794 12.051  1.00 17.45 ? 137 GLU   C CA   1 
ATOM   4374 C  C    . GLU   C 1 133 ? -0.288  -31.269 11.922  1.00 18.27 ? 137 GLU   C C    1 
ATOM   4375 O  O    . GLU   C 1 133 ? -1.094  -30.610 12.566  1.00 20.24 ? 137 GLU   C O    1 
ATOM   4376 C  CB   . GLU   C 1 133 ? 0.875   -33.267 12.982  1.00 17.48 ? 137 GLU   C CB   1 
ATOM   4377 C  CG   . GLU   C 1 133 ? 0.834   -34.752 13.351  1.00 18.36 ? 137 GLU   C CG   1 
ATOM   4378 C  CD   . GLU   C 1 133 ? -0.069  -35.188 14.502  1.00 19.48 ? 137 GLU   C CD   1 
ATOM   4379 O  OE1  . GLU   C 1 133 ? -0.955  -34.410 14.924  1.00 20.21 ? 137 GLU   C OE1  1 
ATOM   4380 O  OE2  . GLU   C 1 133 ? 0.138   -36.326 15.012  1.00 19.90 ? 137 GLU   C OE2  1 
ATOM   4381 N  N    . LEU   C 1 134 ? 0.587   -30.699 11.088  1.00 18.85 ? 138 LEU   C N    1 
ATOM   4382 C  CA   . LEU   C 1 134 ? 0.604   -29.258 10.877  1.00 20.08 ? 138 LEU   C CA   1 
ATOM   4383 C  C    . LEU   C 1 134 ? -0.697  -28.795 10.221  1.00 21.25 ? 138 LEU   C C    1 
ATOM   4384 O  O    . LEU   C 1 134 ? -1.229  -27.752 10.590  1.00 22.55 ? 138 LEU   C O    1 
ATOM   4385 C  CB   . LEU   C 1 134 ? 1.827   -28.835 10.067  1.00 20.21 ? 138 LEU   C CB   1 
ATOM   4386 C  CG   . LEU   C 1 134 ? 3.179   -29.002 10.769  1.00 20.36 ? 138 LEU   C CG   1 
ATOM   4387 C  CD1  . LEU   C 1 134 ? 4.343   -28.765 9.828   1.00 21.18 ? 138 LEU   C CD1  1 
ATOM   4388 C  CD2  . LEU   C 1 134 ? 3.314   -28.094 11.981  1.00 20.86 ? 138 LEU   C CD2  1 
ATOM   4389 N  N    . ALA   C 1 135 ? -1.214  -29.573 9.262   1.00 21.64 ? 139 ALA   C N    1 
ATOM   4390 C  CA   . ALA   C 1 135 ? -2.451  -29.214 8.581   1.00 23.96 ? 139 ALA   C CA   1 
ATOM   4391 C  C    . ALA   C 1 135 ? -3.623  -29.149 9.559   1.00 24.58 ? 139 ALA   C C    1 
ATOM   4392 O  O    . ALA   C 1 135 ? -4.474  -28.267 9.437   1.00 27.18 ? 139 ALA   C O    1 
ATOM   4393 C  CB   . ALA   C 1 135 ? -2.737  -30.179 7.451   1.00 24.38 ? 139 ALA   C CB   1 
ATOM   4394 N  N    A MET   C 1 136 ? -3.678  -30.081 10.520  0.50 25.01 ? 140 MET   C N    1 
ATOM   4395 N  N    B MET   C 1 136 ? -3.672  -30.099 10.505  0.50 24.49 ? 140 MET   C N    1 
ATOM   4396 C  CA   A MET   C 1 136 ? -4.777  -30.112 11.475  0.50 26.12 ? 140 MET   C CA   1 
ATOM   4397 C  CA   B MET   C 1 136 ? -4.741  -30.141 11.492  0.50 24.91 ? 140 MET   C CA   1 
ATOM   4398 C  C    A MET   C 1 136 ? -4.756  -28.856 12.349  0.50 25.90 ? 140 MET   C C    1 
ATOM   4399 C  C    B MET   C 1 136 ? -4.764  -28.827 12.277  0.50 25.26 ? 140 MET   C C    1 
ATOM   4400 O  O    A MET   C 1 136 ? -5.789  -28.471 12.888  0.50 27.39 ? 140 MET   C O    1 
ATOM   4401 O  O    B MET   C 1 136 ? -5.832  -28.370 12.676  0.50 26.71 ? 140 MET   C O    1 
ATOM   4402 C  CB   A MET   C 1 136 ? -4.745  -31.387 12.331  0.50 27.73 ? 140 MET   C CB   1 
ATOM   4403 C  CB   B MET   C 1 136 ? -4.574  -31.316 12.467  0.50 25.54 ? 140 MET   C CB   1 
ATOM   4404 C  CG   A MET   C 1 136 ? -5.475  -32.559 11.692  0.50 30.80 ? 140 MET   C CG   1 
ATOM   4405 C  CG   B MET   C 1 136 ? -4.573  -32.714 11.846  0.50 26.73 ? 140 MET   C CG   1 
ATOM   4406 S  SD   A MET   C 1 136 ? -5.289  -34.159 12.507  0.50 35.05 ? 140 MET   C SD   1 
ATOM   4407 S  SD   B MET   C 1 136 ? -6.111  -33.251 11.068  0.50 30.39 ? 140 MET   C SD   1 
ATOM   4408 C  CE   A MET   C 1 136 ? -6.236  -34.175 14.032  0.50 36.50 ? 140 MET   C CE   1 
ATOM   4409 C  CE   B MET   C 1 136 ? -7.234  -32.037 11.761  0.50 31.63 ? 140 MET   C CE   1 
ATOM   4410 N  N    . LEU   C 1 137 ? -3.582  -28.220 12.478  1.00 24.66 ? 141 LEU   C N    1 
ATOM   4411 C  CA   . LEU   C 1 137 ? -3.434  -26.986 13.242  1.00 24.59 ? 141 LEU   C CA   1 
ATOM   4412 C  C    . LEU   C 1 137 ? -3.631  -25.742 12.375  1.00 27.84 ? 141 LEU   C C    1 
ATOM   4413 O  O    . LEU   C 1 137 ? -3.570  -24.626 12.887  1.00 29.59 ? 141 LEU   C O    1 
ATOM   4414 C  CB   . LEU   C 1 137 ? -2.050  -26.957 13.890  1.00 23.34 ? 141 LEU   C CB   1 
ATOM   4415 C  CG   . LEU   C 1 137 ? -1.805  -27.984 14.997  1.00 22.30 ? 141 LEU   C CG   1 
ATOM   4416 C  CD1  . LEU   C 1 137 ? -0.366  -27.918 15.436  1.00 22.50 ? 141 LEU   C CD1  1 
ATOM   4417 C  CD2  . LEU   C 1 137 ? -2.745  -27.752 16.171  1.00 22.35 ? 141 LEU   C CD2  1 
ATOM   4418 N  N    . GLY   C 1 138 ? -3.829  -25.923 11.064  1.00 28.67 ? 142 GLY   C N    1 
ATOM   4419 C  CA   . GLY   C 1 138 ? -3.941  -24.801 10.147  1.00 31.05 ? 142 GLY   C CA   1 
ATOM   4420 C  C    . GLY   C 1 138 ? -2.591  -24.139 9.877   1.00 32.44 ? 142 GLY   C C    1 
ATOM   4421 O  O    . GLY   C 1 138 ? -2.534  -22.965 9.519   1.00 36.12 ? 142 GLY   C O    1 
ATOM   4422 N  N    . LEU   C 1 139 ? -1.506  -24.905 10.019  1.00 32.69 ? 143 LEU   C N    1 
ATOM   4423 C  CA   . LEU   C 1 139 ? -0.170  -24.390 9.781   1.00 35.30 ? 143 LEU   C CA   1 
ATOM   4424 C  C    . LEU   C 1 139 ? 0.396   -25.052 8.523   1.00 39.21 ? 143 LEU   C C    1 
ATOM   4425 O  O    . LEU   C 1 139 ? 1.547   -25.470 8.501   1.00 41.09 ? 143 LEU   C O    1 
ATOM   4426 C  CB   . LEU   C 1 139 ? 0.680   -24.623 11.031  1.00 34.90 ? 143 LEU   C CB   1 
ATOM   4427 C  CG   . LEU   C 1 139 ? 0.122   -24.022 12.328  1.00 34.62 ? 143 LEU   C CG   1 
ATOM   4428 C  CD1  . LEU   C 1 139 ? 0.978   -24.382 13.525  1.00 35.11 ? 143 LEU   C CD1  1 
ATOM   4429 C  CD2  . LEU   C 1 139 ? -0.024  -22.510 12.241  1.00 35.95 ? 143 LEU   C CD2  1 
ATOM   4430 N  N    . THR   C 1 140 ? -0.424  -25.079 7.459   1.00 43.82 ? 144 THR   C N    1 
ATOM   4431 C  CA   . THR   C 1 140 ? -0.115  -25.789 6.224   1.00 46.59 ? 144 THR   C CA   1 
ATOM   4432 C  C    . THR   C 1 140 ? 1.205   -25.302 5.625   1.00 48.31 ? 144 THR   C C    1 
ATOM   4433 O  O    . THR   C 1 140 ? 1.978   -26.109 5.115   1.00 51.82 ? 144 THR   C O    1 
ATOM   4434 C  CB   . THR   C 1 140 ? -1.268  -25.616 5.234   1.00 48.32 ? 144 THR   C CB   1 
ATOM   4435 N  N    . SER   C 1 141 ? 1.461   -23.988 5.705   1.00 49.70 ? 145 SER   C N    1 
ATOM   4436 C  CA   . SER   C 1 141 ? 2.543   -23.356 4.960   1.00 48.98 ? 145 SER   C CA   1 
ATOM   4437 C  C    . SER   C 1 141 ? 3.771   -23.079 5.831   1.00 47.37 ? 145 SER   C C    1 
ATOM   4438 O  O    . SER   C 1 141 ? 4.720   -22.447 5.367   1.00 46.63 ? 145 SER   C O    1 
ATOM   4439 C  CB   . SER   C 1 141 ? 2.052   -22.083 4.314   1.00 50.26 ? 145 SER   C CB   1 
ATOM   4440 O  OG   . SER   C 1 141 ? 1.601   -21.157 5.294   1.00 51.25 ? 145 SER   C OG   1 
ATOM   4441 N  N    . ALA   C 1 142 ? 3.774   -23.566 7.079   1.00 44.79 ? 146 ALA   C N    1 
ATOM   4442 C  CA   . ALA   C 1 142 ? 4.811   -23.208 8.037   1.00 42.49 ? 146 ALA   C CA   1 
ATOM   4443 C  C    . ALA   C 1 142 ? 6.192   -23.691 7.583   1.00 38.51 ? 146 ALA   C C    1 
ATOM   4444 O  O    . ALA   C 1 142 ? 7.198   -23.064 7.906   1.00 38.94 ? 146 ALA   C O    1 
ATOM   4445 C  CB   . ALA   C 1 142 ? 4.463   -23.755 9.405   1.00 42.37 ? 146 ALA   C CB   1 
ATOM   4446 N  N    . LEU   C 1 143 ? 6.240   -24.808 6.847   1.00 35.06 ? 147 LEU   C N    1 
ATOM   4447 C  CA   . LEU   C 1 143 ? 7.500   -25.370 6.382   1.00 32.79 ? 147 LEU   C CA   1 
ATOM   4448 C  C    . LEU   C 1 143 ? 7.615   -25.277 4.860   1.00 33.84 ? 147 LEU   C C    1 
ATOM   4449 O  O    . LEU   C 1 143 ? 8.371   -26.034 4.257   1.00 33.30 ? 147 LEU   C O    1 
ATOM   4450 C  CB   . LEU   C 1 143 ? 7.612   -26.818 6.863   1.00 32.97 ? 147 LEU   C CB   1 
ATOM   4451 C  CG   . LEU   C 1 143 ? 7.713   -27.024 8.377   1.00 32.97 ? 147 LEU   C CG   1 
ATOM   4452 C  CD1  . LEU   C 1 143 ? 7.847   -28.502 8.720   1.00 33.04 ? 147 LEU   C CD1  1 
ATOM   4453 C  CD2  . LEU   C 1 143 ? 8.885   -26.243 8.948   1.00 33.77 ? 147 LEU   C CD2  1 
ATOM   4454 N  N    . ASP   C 1 144 ? 6.919   -24.313 4.242   1.00 35.96 ? 148 ASP   C N    1 
ATOM   4455 C  CA   . ASP   C 1 144 ? 6.926   -24.192 2.789   1.00 38.36 ? 148 ASP   C CA   1 
ATOM   4456 C  C    . ASP   C 1 144 ? 8.329   -23.880 2.264   1.00 38.03 ? 148 ASP   C C    1 
ATOM   4457 O  O    . ASP   C 1 144 ? 8.641   -24.223 1.124   1.00 42.06 ? 148 ASP   C O    1 
ATOM   4458 C  CB   . ASP   C 1 144 ? 5.876   -23.207 2.289   1.00 41.32 ? 148 ASP   C CB   1 
ATOM   4459 C  CG   . ASP   C 1 144 ? 4.510   -23.813 1.997   1.00 44.62 ? 148 ASP   C CG   1 
ATOM   4460 O  OD1  . ASP   C 1 144 ? 4.363   -25.046 2.167   1.00 46.60 ? 148 ASP   C OD1  1 
ATOM   4461 O  OD2  . ASP   C 1 144 ? 3.604   -23.051 1.595   1.00 48.05 ? 148 ASP   C OD2  1 
ATOM   4462 N  N    . GLY   C 1 145 ? 9.171   -23.241 3.084   1.00 34.12 ? 149 GLY   C N    1 
ATOM   4463 C  CA   . GLY   C 1 145 ? 10.519  -22.885 2.665   1.00 32.14 ? 149 GLY   C CA   1 
ATOM   4464 C  C    . GLY   C 1 145 ? 11.543  -23.981 2.961   1.00 29.17 ? 149 GLY   C C    1 
ATOM   4465 O  O    . GLY   C 1 145 ? 12.715  -23.841 2.624   1.00 29.37 ? 149 GLY   C O    1 
ATOM   4466 N  N    . ALA   C 1 146 ? 11.100  -25.064 3.605   1.00 25.94 ? 150 ALA   C N    1 
ATOM   4467 C  CA   . ALA   C 1 146 ? 11.988  -26.152 3.982   1.00 22.31 ? 150 ALA   C CA   1 
ATOM   4468 C  C    . ALA   C 1 146 ? 12.062  -27.164 2.848   1.00 19.34 ? 150 ALA   C C    1 
ATOM   4469 O  O    . ALA   C 1 146 ? 11.236  -27.157 1.931   1.00 19.52 ? 150 ALA   C O    1 
ATOM   4470 C  CB   . ALA   C 1 146 ? 11.496  -26.822 5.234   1.00 22.64 ? 150 ALA   C CB   1 
ATOM   4471 N  N    . PHE   C 1 147 ? 13.055  -28.049 2.955   1.00 16.84 ? 151 PHE   C N    1 
ATOM   4472 C  CA   . PHE   C 1 147 ? 13.250  -29.122 1.998   1.00 16.73 ? 151 PHE   C CA   1 
ATOM   4473 C  C    . PHE   C 1 147 ? 13.288  -30.444 2.747   1.00 15.66 ? 151 PHE   C C    1 
ATOM   4474 O  O    . PHE   C 1 147 ? 13.387  -30.467 3.974   1.00 15.00 ? 151 PHE   C O    1 
ATOM   4475 C  CB   . PHE   C 1 147 ? 14.527  -28.889 1.193   1.00 17.43 ? 151 PHE   C CB   1 
ATOM   4476 C  CG   . PHE   C 1 147 ? 14.459  -27.587 0.409   1.00 18.22 ? 151 PHE   C CG   1 
ATOM   4477 C  CD1  . PHE   C 1 147 ? 14.845  -26.382 0.983   1.00 19.17 ? 151 PHE   C CD1  1 
ATOM   4478 C  CD2  . PHE   C 1 147 ? 13.937  -27.564 -0.876  1.00 19.96 ? 151 PHE   C CD2  1 
ATOM   4479 C  CE1  . PHE   C 1 147 ? 14.737  -25.193 0.276   1.00 20.34 ? 151 PHE   C CE1  1 
ATOM   4480 C  CE2  . PHE   C 1 147 ? 13.814  -26.374 -1.569  1.00 21.25 ? 151 PHE   C CE2  1 
ATOM   4481 C  CZ   . PHE   C 1 147 ? 14.220  -25.195 -0.997  1.00 21.23 ? 151 PHE   C CZ   1 
ATOM   4482 N  N    . CYS   C 1 148 ? 13.194  -31.533 1.986   1.00 16.31 ? 152 CYS   C N    1 
ATOM   4483 C  CA   . CYS   C 1 148 ? 13.283  -32.855 2.567   1.00 16.08 ? 152 CYS   C CA   1 
ATOM   4484 C  C    . CYS   C 1 148 ? 13.876  -33.837 1.566   1.00 15.92 ? 152 CYS   C C    1 
ATOM   4485 O  O    . CYS   C 1 148 ? 13.765  -33.655 0.343   1.00 17.15 ? 152 CYS   C O    1 
ATOM   4486 C  CB   . CYS   C 1 148 ? 11.930  -33.320 3.099   1.00 17.42 ? 152 CYS   C CB   1 
ATOM   4487 S  SG   . CYS   C 1 148 ? 10.681  -33.597 1.812   1.00 19.19 ? 152 CYS   C SG   1 
ATOM   4488 N  N    A VAL   C 1 149 ? 14.516  -34.875 2.107   0.50 15.90 ? 153 VAL   C N    1 
ATOM   4489 N  N    B VAL   C 1 149 ? 14.452  -34.905 2.137   0.50 15.66 ? 153 VAL   C N    1 
ATOM   4490 C  CA   A VAL   C 1 149 ? 14.941  -36.020 1.328   0.50 16.46 ? 153 VAL   C CA   1 
ATOM   4491 C  CA   B VAL   C 1 149 ? 15.068  -36.013 1.426   0.50 16.05 ? 153 VAL   C CA   1 
ATOM   4492 C  C    A VAL   C 1 149 ? 14.680  -37.270 2.155   0.50 15.92 ? 153 VAL   C C    1 
ATOM   4493 C  C    B VAL   C 1 149 ? 14.756  -37.303 2.179   0.50 15.78 ? 153 VAL   C C    1 
ATOM   4494 O  O    A VAL   C 1 149 ? 14.769  -37.256 3.386   0.50 15.26 ? 153 VAL   C O    1 
ATOM   4495 O  O    B VAL   C 1 149 ? 14.918  -37.363 3.402   0.50 15.17 ? 153 VAL   C O    1 
ATOM   4496 C  CB   A VAL   C 1 149 ? 16.414  -35.990 0.880   0.50 17.72 ? 153 VAL   C CB   1 
ATOM   4497 C  CB   B VAL   C 1 149 ? 16.595  -35.861 1.300   0.50 16.82 ? 153 VAL   C CB   1 
ATOM   4498 C  CG1  A VAL   C 1 149 ? 16.704  -34.815 -0.040  0.50 18.72 ? 153 VAL   C CG1  1 
ATOM   4499 C  CG1  B VAL   C 1 149 ? 17.258  -37.187 0.946   0.50 17.34 ? 153 VAL   C CG1  1 
ATOM   4500 C  CG2  A VAL   C 1 149 ? 17.363  -36.018 2.065   0.50 17.62 ? 153 VAL   C CG2  1 
ATOM   4501 C  CG2  B VAL   C 1 149 ? 16.978  -34.789 0.294   0.50 17.94 ? 153 VAL   C CG2  1 
ATOM   4502 N  N    . ASP   C 1 150 ? 14.361  -38.345 1.434   1.00 16.04 ? 154 ASP   C N    1 
ATOM   4503 C  CA   . ASP   C 1 150 ? 14.161  -39.663 2.012   1.00 16.81 ? 154 ASP   C CA   1 
ATOM   4504 C  C    . ASP   C 1 150 ? 15.481  -40.421 1.910   1.00 16.56 ? 154 ASP   C C    1 
ATOM   4505 O  O    . ASP   C 1 150 ? 15.972  -40.666 0.804   1.00 17.84 ? 154 ASP   C O    1 
ATOM   4506 C  CB   . ASP   C 1 150 ? 13.058  -40.403 1.276   1.00 17.87 ? 154 ASP   C CB   1 
ATOM   4507 C  CG   . ASP   C 1 150 ? 12.610  -41.705 1.911   1.00 18.99 ? 154 ASP   C CG   1 
ATOM   4508 O  OD1  . ASP   C 1 150 ? 13.471  -42.380 2.513   1.00 19.85 ? 154 ASP   C OD1  1 
ATOM   4509 O  OD2  . ASP   C 1 150 ? 11.398  -42.017 1.796   1.00 20.34 ? 154 ASP   C OD2  1 
ATOM   4510 N  N    . SER   C 1 151 ? 16.046  -40.806 3.055   1.00 17.07 ? 155 SER   C N    1 
ATOM   4511 C  CA   . SER   C 1 151 ? 17.350  -41.441 3.083   1.00 17.79 ? 155 SER   C CA   1 
ATOM   4512 C  C    . SER   C 1 151 ? 17.339  -42.835 2.459   1.00 19.38 ? 155 SER   C C    1 
ATOM   4513 O  O    . SER   C 1 151 ? 18.390  -43.303 2.044   1.00 20.58 ? 155 SER   C O    1 
ATOM   4514 C  CB   . SER   C 1 151 ? 17.946  -41.475 4.468   1.00 18.42 ? 155 SER   C CB   1 
ATOM   4515 O  OG   . SER   C 1 151 ? 17.078  -42.082 5.401   1.00 18.66 ? 155 SER   C OG   1 
ATOM   4516 N  N    . ILE   C 1 152 ? 16.182  -43.498 2.370   1.00 20.57 ? 156 ILE   C N    1 
ATOM   4517 C  CA   . ILE   C 1 152 ? 16.168  -44.803 1.732   1.00 21.96 ? 156 ILE   C CA   1 
ATOM   4518 C  C    . ILE   C 1 152 ? 16.424  -44.611 0.234   1.00 22.84 ? 156 ILE   C C    1 
ATOM   4519 O  O    . ILE   C 1 152 ? 17.172  -45.384 -0.358  1.00 24.96 ? 156 ILE   C O    1 
ATOM   4520 C  CB   . ILE   C 1 152 ? 14.887  -45.593 2.075   1.00 23.91 ? 156 ILE   C CB   1 
ATOM   4521 C  CG1  . ILE   C 1 152 ? 15.129  -47.081 1.969   1.00 26.70 ? 156 ILE   C CG1  1 
ATOM   4522 C  CG2  . ILE   C 1 152 ? 13.679  -45.154 1.248   1.00 25.73 ? 156 ILE   C CG2  1 
ATOM   4523 C  CD1  . ILE   C 1 152 ? 13.959  -47.921 2.443   1.00 27.49 ? 156 ILE   C CD1  1 
ATOM   4524 N  N    . THR   C 1 153 ? 15.851  -43.549 -0.354  1.00 23.47 ? 157 THR   C N    1 
ATOM   4525 C  CA   . THR   C 1 153 ? 16.066  -43.219 -1.756  1.00 24.66 ? 157 THR   C CA   1 
ATOM   4526 C  C    . THR   C 1 153 ? 17.549  -42.915 -1.970  1.00 25.48 ? 157 THR   C C    1 
ATOM   4527 O  O    . THR   C 1 153 ? 18.154  -43.406 -2.918  1.00 28.88 ? 157 THR   C O    1 
ATOM   4528 C  CB   . THR   C 1 153 ? 15.178  -42.042 -2.174  1.00 24.51 ? 157 THR   C CB   1 
ATOM   4529 O  OG1  . THR   C 1 153 ? 13.837  -42.336 -1.786  1.00 25.66 ? 157 THR   C OG1  1 
ATOM   4530 C  CG2  . THR   C 1 153 ? 15.208  -41.784 -3.672  1.00 24.97 ? 157 THR   C CG2  1 
ATOM   4531 N  N    . ALA   C 1 154 ? 18.134  -42.112 -1.070  1.00 24.89 ? 158 ALA   C N    1 
ATOM   4532 C  CA   . ALA   C 1 154 ? 19.530  -41.708 -1.169  1.00 25.77 ? 158 ALA   C CA   1 
ATOM   4533 C  C    . ALA   C 1 154 ? 20.467  -42.907 -1.047  1.00 27.38 ? 158 ALA   C C    1 
ATOM   4534 O  O    . ALA   C 1 154 ? 21.379  -43.072 -1.858  1.00 29.66 ? 158 ALA   C O    1 
ATOM   4535 C  CB   . ALA   C 1 154 ? 19.831  -40.679 -0.103  1.00 25.47 ? 158 ALA   C CB   1 
ATOM   4536 N  N    . LEU   C 1 155 ? 20.244  -43.744 -0.030  1.00 28.23 ? 159 LEU   C N    1 
ATOM   4537 C  CA   . LEU   C 1 155 ? 21.192  -44.797 0.300   1.00 30.77 ? 159 LEU   C CA   1 
ATOM   4538 C  C    . LEU   C 1 155 ? 21.093  -45.943 -0.711  1.00 33.99 ? 159 LEU   C C    1 
ATOM   4539 O  O    . LEU   C 1 155 ? 22.094  -46.600 -0.977  1.00 35.64 ? 159 LEU   C O    1 
ATOM   4540 C  CB   . LEU   C 1 155 ? 20.985  -45.243 1.749   1.00 30.92 ? 159 LEU   C CB   1 
ATOM   4541 C  CG   . LEU   C 1 155 ? 21.220  -44.165 2.817   1.00 31.15 ? 159 LEU   C CG   1 
ATOM   4542 C  CD1  . LEU   C 1 155 ? 20.555  -44.537 4.130   1.00 30.87 ? 159 LEU   C CD1  1 
ATOM   4543 C  CD2  . LEU   C 1 155 ? 22.694  -43.895 3.037   1.00 31.46 ? 159 LEU   C CD2  1 
ATOM   4544 N  N    . LYS   C 1 156 ? 19.902  -46.160 -1.291  1.00 34.54 ? 160 LYS   C N    1 
ATOM   4545 C  CA   . LYS   C 1 156 ? 19.731  -47.084 -2.406  1.00 37.43 ? 160 LYS   C CA   1 
ATOM   4546 C  C    . LYS   C 1 156 ? 20.518  -46.598 -3.618  1.00 39.96 ? 160 LYS   C C    1 
ATOM   4547 O  O    . LYS   C 1 156 ? 21.223  -47.377 -4.261  1.00 41.89 ? 160 LYS   C O    1 
ATOM   4548 C  CB   . LYS   C 1 156 ? 18.266  -47.213 -2.838  1.00 39.40 ? 160 LYS   C CB   1 
ATOM   4549 C  CG   . LYS   C 1 156 ? 17.430  -48.193 -2.032  1.00 42.69 ? 160 LYS   C CG   1 
ATOM   4550 C  CD   . LYS   C 1 156 ? 16.011  -48.366 -2.558  1.00 45.22 ? 160 LYS   C CD   1 
ATOM   4551 C  CE   . LYS   C 1 156 ? 15.246  -49.400 -1.799  1.00 46.46 ? 160 LYS   C CE   1 
ATOM   4552 N  NZ   . LYS   C 1 156 ? 13.822  -49.360 -2.135  1.00 47.27 ? 160 LYS   C NZ   1 
ATOM   4553 N  N    . ALA   C 1 157 ? 20.363  -45.307 -3.940  1.00 41.07 ? 161 ALA   C N    1 
ATOM   4554 C  CA   . ALA   C 1 157 ? 21.013  -44.723 -5.101  1.00 43.72 ? 161 ALA   C CA   1 
ATOM   4555 C  C    . ALA   C 1 157 ? 22.530  -44.824 -4.961  1.00 45.69 ? 161 ALA   C C    1 
ATOM   4556 O  O    . ALA   C 1 157 ? 23.222  -45.069 -5.943  1.00 49.93 ? 161 ALA   C O    1 
ATOM   4557 C  CB   . ALA   C 1 157 ? 20.566  -43.292 -5.294  1.00 43.48 ? 161 ALA   C CB   1 
ATOM   4558 N  N    . LEU   C 1 158 ? 23.036  -44.655 -3.735  1.00 45.73 ? 162 LEU   C N    1 
ATOM   4559 C  CA   . LEU   C 1 158 ? 24.468  -44.676 -3.480  1.00 46.65 ? 162 LEU   C CA   1 
ATOM   4560 C  C    . LEU   C 1 158 ? 25.003  -46.108 -3.424  1.00 50.78 ? 162 LEU   C C    1 
ATOM   4561 O  O    . LEU   C 1 158 ? 26.182  -46.323 -3.692  1.00 52.95 ? 162 LEU   C O    1 
ATOM   4562 C  CB   . LEU   C 1 158 ? 24.760  -43.896 -2.200  1.00 47.48 ? 162 LEU   C CB   1 
ATOM   4563 C  CG   . LEU   C 1 158 ? 24.466  -42.394 -2.273  1.00 46.77 ? 162 LEU   C CG   1 
ATOM   4564 C  CD1  . LEU   C 1 158 ? 24.387  -41.780 -0.891  1.00 48.13 ? 162 LEU   C CD1  1 
ATOM   4565 C  CD2  . LEU   C 1 158 ? 25.507  -41.676 -3.114  1.00 48.01 ? 162 LEU   C CD2  1 
ATOM   4566 N  N    . GLU   C 1 159 ? 24.151  -47.082 -3.074  1.00 52.66 ? 163 GLU   C N    1 
ATOM   4567 C  CA   . GLU   C 1 159 ? 24.534  -48.487 -3.136  1.00 56.13 ? 163 GLU   C CA   1 
ATOM   4568 C  C    . GLU   C 1 159 ? 24.320  -49.006 -4.568  1.00 57.46 ? 163 GLU   C C    1 
ATOM   4569 O  O    . GLU   C 1 159 ? 25.292  -48.936 -5.356  1.00 60.50 ? 163 GLU   C O    1 
ATOM   4570 C  CB   . GLU   C 1 159 ? 23.746  -49.324 -2.128  1.00 57.61 ? 163 GLU   C CB   1 
ATOM   4571 N  N    . LYS   C 1 171 ? 17.940  -57.492 -1.165  1.00 46.72 ? 175 LYS   C N    1 
ATOM   4572 C  CA   . LYS   C 1 171 ? 18.607  -56.677 -0.116  1.00 44.99 ? 175 LYS   C CA   1 
ATOM   4573 C  C    . LYS   C 1 171 ? 17.548  -55.849 0.609   1.00 40.65 ? 175 LYS   C C    1 
ATOM   4574 O  O    . LYS   C 1 171 ? 16.744  -55.177 -0.036  1.00 40.94 ? 175 LYS   C O    1 
ATOM   4575 C  CB   . LYS   C 1 171 ? 19.682  -55.762 -0.719  1.00 47.70 ? 175 LYS   C CB   1 
ATOM   4576 C  CG   . LYS   C 1 171 ? 21.045  -55.801 -0.036  1.00 49.44 ? 175 LYS   C CG   1 
ATOM   4577 C  CD   . LYS   C 1 171 ? 22.148  -55.084 -0.808  1.00 49.07 ? 175 LYS   C CD   1 
ATOM   4578 N  N    . SER   C 1 172 ? 17.545  -55.929 1.946   1.00 36.15 ? 176 SER   C N    1 
ATOM   4579 C  CA   . SER   C 1 172 ? 16.726  -55.064 2.781   1.00 33.88 ? 176 SER   C CA   1 
ATOM   4580 C  C    . SER   C 1 172 ? 17.372  -53.684 2.892   1.00 32.13 ? 176 SER   C C    1 
ATOM   4581 O  O    . SER   C 1 172 ? 18.582  -53.591 3.077   1.00 31.86 ? 176 SER   C O    1 
ATOM   4582 C  CB   . SER   C 1 172 ? 16.525  -55.656 4.154   1.00 34.22 ? 176 SER   C CB   1 
ATOM   4583 O  OG   . SER   C 1 172 ? 15.861  -54.740 5.014   1.00 33.73 ? 176 SER   C OG   1 
ATOM   4584 N  N    . TYR   C 1 173 ? 16.550  -52.629 2.805   1.00 30.44 ? 177 TYR   C N    1 
ATOM   4585 C  CA   . TYR   C 1 173 ? 17.012  -51.265 3.024   1.00 29.39 ? 177 TYR   C CA   1 
ATOM   4586 C  C    . TYR   C 1 173 ? 16.358  -50.679 4.272   1.00 27.20 ? 177 TYR   C C    1 
ATOM   4587 O  O    . TYR   C 1 173 ? 16.306  -49.456 4.433   1.00 25.97 ? 177 TYR   C O    1 
ATOM   4588 C  CB   . TYR   C 1 173 ? 16.807  -50.424 1.758   1.00 31.21 ? 177 TYR   C CB   1 
ATOM   4589 C  CG   . TYR   C 1 173 ? 17.798  -50.825 0.676   1.00 34.52 ? 177 TYR   C CG   1 
ATOM   4590 C  CD1  . TYR   C 1 173 ? 19.120  -50.393 0.719   1.00 36.95 ? 177 TYR   C CD1  1 
ATOM   4591 C  CD2  . TYR   C 1 173 ? 17.432  -51.690 -0.349  1.00 36.55 ? 177 TYR   C CD2  1 
ATOM   4592 C  CE1  . TYR   C 1 173 ? 20.041  -50.785 -0.241  1.00 40.04 ? 177 TYR   C CE1  1 
ATOM   4593 C  CE2  . TYR   C 1 173 ? 18.342  -52.088 -1.311  1.00 38.23 ? 177 TYR   C CE2  1 
ATOM   4594 C  CZ   . TYR   C 1 173 ? 19.649  -51.635 -1.260  1.00 39.57 ? 177 TYR   C CZ   1 
ATOM   4595 O  OH   . TYR   C 1 173 ? 20.528  -52.045 -2.227  1.00 44.40 ? 177 TYR   C OH   1 
ATOM   4596 N  N    . SER   C 1 174 ? 15.937  -51.554 5.194   1.00 25.34 ? 178 SER   C N    1 
ATOM   4597 C  CA   . SER   C 1 174 ? 15.564  -51.111 6.527   1.00 24.82 ? 178 SER   C CA   1 
ATOM   4598 C  C    . SER   C 1 174 ? 16.772  -50.465 7.203   1.00 23.73 ? 178 SER   C C    1 
ATOM   4599 O  O    . SER   C 1 174 ? 17.918  -50.780 6.898   1.00 23.04 ? 178 SER   C O    1 
ATOM   4600 C  CB   . SER   C 1 174 ? 15.024  -52.233 7.368   1.00 25.14 ? 178 SER   C CB   1 
ATOM   4601 O  OG   . SER   C 1 174 ? 16.070  -53.077 7.834   1.00 26.19 ? 178 SER   C OG   1 
ATOM   4602 N  N    . LEU   C 1 175 ? 16.494  -49.565 8.144   1.00 23.50 ? 179 LEU   C N    1 
ATOM   4603 C  CA   . LEU   C 1 175 ? 17.542  -48.854 8.854   1.00 22.93 ? 179 LEU   C CA   1 
ATOM   4604 C  C    . LEU   C 1 175 ? 18.511  -49.853 9.488   1.00 23.55 ? 179 LEU   C C    1 
ATOM   4605 O  O    . LEU   C 1 175 ? 19.722  -49.720 9.350   1.00 23.41 ? 179 LEU   C O    1 
ATOM   4606 C  CB   . LEU   C 1 175 ? 16.880  -47.948 9.887   1.00 22.72 ? 179 LEU   C CB   1 
ATOM   4607 C  CG   . LEU   C 1 175 ? 17.812  -46.973 10.605  1.00 22.56 ? 179 LEU   C CG   1 
ATOM   4608 C  CD1  . LEU   C 1 175 ? 18.293  -45.888 9.662   1.00 23.38 ? 179 LEU   C CD1  1 
ATOM   4609 C  CD2  . LEU   C 1 175 ? 17.104  -46.376 11.799  1.00 22.03 ? 179 LEU   C CD2  1 
ATOM   4610 N  N    . GLY   C 1 176 ? 17.967  -50.871 10.162  1.00 24.76 ? 180 GLY   C N    1 
ATOM   4611 C  CA   . GLY   C 1 176 ? 18.781  -51.866 10.841  1.00 25.82 ? 180 GLY   C CA   1 
ATOM   4612 C  C    . GLY   C 1 176 ? 19.608  -52.706 9.864   1.00 26.81 ? 180 GLY   C C    1 
ATOM   4613 O  O    . GLY   C 1 176 ? 20.766  -53.021 10.140  1.00 27.69 ? 180 GLY   C O    1 
ATOM   4614 N  N    . SER   C 1 177 ? 19.015  -53.057 8.716   1.00 27.50 ? 181 SER   C N    1 
ATOM   4615 C  CA   . SER   C 1 177 ? 19.710  -53.844 7.706   1.00 27.81 ? 181 SER   C CA   1 
ATOM   4616 C  C    . SER   C 1 177 ? 20.926  -53.088 7.179   1.00 26.86 ? 181 SER   C C    1 
ATOM   4617 O  O    . SER   C 1 177 ? 22.012  -53.654 7.087   1.00 27.77 ? 181 SER   C O    1 
ATOM   4618 C  CB   . SER   C 1 177 ? 18.796  -54.225 6.572   1.00 29.10 ? 181 SER   C CB   1 
ATOM   4619 O  OG   . SER   C 1 177 ? 17.815  -55.156 7.006   1.00 31.80 ? 181 SER   C OG   1 
ATOM   4620 N  N    . ILE   C 1 178 ? 20.727  -51.812 6.827   1.00 24.48 ? 182 ILE   C N    1 
ATOM   4621 C  CA   . ILE   C 1 178 ? 21.801  -50.992 6.282   1.00 24.93 ? 182 ILE   C CA   1 
ATOM   4622 C  C    . ILE   C 1 178 ? 22.902  -50.834 7.330   1.00 25.10 ? 182 ILE   C C    1 
ATOM   4623 O  O    . ILE   C 1 178 ? 24.084  -51.007 7.030   1.00 25.76 ? 182 ILE   C O    1 
ATOM   4624 C  CB   . ILE   C 1 178 ? 21.283  -49.620 5.815   1.00 23.61 ? 182 ILE   C CB   1 
ATOM   4625 C  CG1  . ILE   C 1 178 ? 20.286  -49.746 4.665   1.00 24.45 ? 182 ILE   C CG1  1 
ATOM   4626 C  CG2  . ILE   C 1 178 ? 22.450  -48.707 5.441   1.00 23.35 ? 182 ILE   C CG2  1 
ATOM   4627 C  CD1  . ILE   C 1 178 ? 19.490  -48.481 4.398   1.00 25.25 ? 182 ILE   C CD1  1 
ATOM   4628 N  N    . TYR   C 1 179 ? 22.492  -50.501 8.560   1.00 24.89 ? 183 TYR   C N    1 
ATOM   4629 C  CA   . TYR   C 1 179 ? 23.425  -50.266 9.649   1.00 25.16 ? 183 TYR   C CA   1 
ATOM   4630 C  C    . TYR   C 1 179 ? 24.278  -51.513 9.867   1.00 27.81 ? 183 TYR   C C    1 
ATOM   4631 O  O    . TYR   C 1 179 ? 25.491  -51.409 10.033  1.00 29.55 ? 183 TYR   C O    1 
ATOM   4632 C  CB   . TYR   C 1 179 ? 22.655  -49.879 10.916  1.00 24.19 ? 183 TYR   C CB   1 
ATOM   4633 C  CG   . TYR   C 1 179 ? 23.536  -49.355 12.039  1.00 23.87 ? 183 TYR   C CG   1 
ATOM   4634 C  CD1  . TYR   C 1 179 ? 24.237  -50.227 12.859  1.00 23.92 ? 183 TYR   C CD1  1 
ATOM   4635 C  CD2  . TYR   C 1 179 ? 23.673  -47.991 12.271  1.00 21.69 ? 183 TYR   C CD2  1 
ATOM   4636 C  CE1  . TYR   C 1 179 ? 25.051  -49.764 13.880  1.00 23.14 ? 183 TYR   C CE1  1 
ATOM   4637 C  CE2  . TYR   C 1 179 ? 24.474  -47.515 13.298  1.00 21.37 ? 183 TYR   C CE2  1 
ATOM   4638 C  CZ   . TYR   C 1 179 ? 25.172  -48.403 14.098  1.00 22.24 ? 183 TYR   C CZ   1 
ATOM   4639 O  OH   . TYR   C 1 179 ? 25.956  -47.954 15.116  1.00 24.08 ? 183 TYR   C OH   1 
ATOM   4640 N  N    . THR   C 1 180 ? 23.631  -52.685 9.864   1.00 29.18 ? 184 THR   C N    1 
ATOM   4641 C  CA   . THR   C 1 180 ? 24.314  -53.947 10.117  1.00 31.31 ? 184 THR   C CA   1 
ATOM   4642 C  C    . THR   C 1 180 ? 25.312  -54.231 8.996   1.00 32.18 ? 184 THR   C C    1 
ATOM   4643 O  O    . THR   C 1 180 ? 26.424  -54.675 9.258   1.00 34.50 ? 184 THR   C O    1 
ATOM   4644 C  CB   . THR   C 1 180 ? 23.291  -55.075 10.262  1.00 32.83 ? 184 THR   C CB   1 
ATOM   4645 O  OG1  . THR   C 1 180 ? 22.491  -54.758 11.396  1.00 34.87 ? 184 THR   C OG1  1 
ATOM   4646 C  CG2  . THR   C 1 180 ? 23.934  -56.423 10.524  1.00 34.55 ? 184 THR   C CG2  1 
ATOM   4647 N  N    . ARG   C 1 181 ? 24.909  -53.959 7.750   1.00 32.47 ? 185 ARG   C N    1 
ATOM   4648 C  CA   . ARG   C 1 181 ? 25.754  -54.196 6.587   1.00 33.81 ? 185 ARG   C CA   1 
ATOM   4649 C  C    . ARG   C 1 181 ? 26.993  -53.296 6.629   1.00 34.19 ? 185 ARG   C C    1 
ATOM   4650 O  O    . ARG   C 1 181 ? 28.070  -53.707 6.199   1.00 35.99 ? 185 ARG   C O    1 
ATOM   4651 C  CB   . ARG   C 1 181 ? 24.857  -53.984 5.360   1.00 37.86 ? 185 ARG   C CB   1 
ATOM   4652 C  CG   . ARG   C 1 181 ? 25.283  -54.568 4.025   1.00 41.24 ? 185 ARG   C CG   1 
ATOM   4653 C  CD   . ARG   C 1 181 ? 24.069  -54.947 3.181   1.00 40.43 ? 185 ARG   C CD   1 
ATOM   4654 N  NE   . ARG   C 1 181 ? 23.191  -53.820 2.843   1.00 38.54 ? 185 ARG   C NE   1 
ATOM   4655 C  CZ   . ARG   C 1 181 ? 21.871  -53.740 3.027   1.00 37.34 ? 185 ARG   C CZ   1 
ATOM   4656 N  NH1  . ARG   C 1 181 ? 21.198  -54.722 3.605   1.00 38.12 ? 185 ARG   C NH1  1 
ATOM   4657 N  NH2  . ARG   C 1 181 ? 21.216  -52.665 2.618   1.00 36.48 ? 185 ARG   C NH2  1 
ATOM   4658 N  N    . LEU   C 1 182 ? 26.847  -52.071 7.158   1.00 33.41 ? 186 LEU   C N    1 
ATOM   4659 C  CA   . LEU   C 1 182 ? 27.952  -51.121 7.214   1.00 33.19 ? 186 LEU   C CA   1 
ATOM   4660 C  C    . LEU   C 1 182 ? 28.824  -51.354 8.447   1.00 32.09 ? 186 LEU   C C    1 
ATOM   4661 O  O    . LEU   C 1 182 ? 30.043  -51.267 8.355   1.00 35.26 ? 186 LEU   C O    1 
ATOM   4662 C  CB   . LEU   C 1 182 ? 27.460  -49.673 7.199   1.00 32.76 ? 186 LEU   C CB   1 
ATOM   4663 C  CG   . LEU   C 1 182 ? 26.750  -49.192 5.929   1.00 34.37 ? 186 LEU   C CG   1 
ATOM   4664 C  CD1  . LEU   C 1 182 ? 26.372  -47.729 6.100   1.00 34.31 ? 186 LEU   C CD1  1 
ATOM   4665 C  CD2  . LEU   C 1 182 ? 27.581  -49.390 4.676   1.00 36.00 ? 186 LEU   C CD2  1 
ATOM   4666 N  N    . TYR   C 1 183 ? 28.209  -51.599 9.611   1.00 32.41 ? 187 TYR   C N    1 
ATOM   4667 C  CA   . TYR   C 1 183 ? 28.937  -51.521 10.872  1.00 32.09 ? 187 TYR   C CA   1 
ATOM   4668 C  C    . TYR   C 1 183 ? 28.981  -52.856 11.622  1.00 35.44 ? 187 TYR   C C    1 
ATOM   4669 O  O    . TYR   C 1 183 ? 29.626  -52.937 12.665  1.00 39.04 ? 187 TYR   C O    1 
ATOM   4670 C  CB   . TYR   C 1 183 ? 28.307  -50.378 11.673  1.00 30.46 ? 187 TYR   C CB   1 
ATOM   4671 C  CG   . TYR   C 1 183 ? 28.496  -49.002 11.046  1.00 28.83 ? 187 TYR   C CG   1 
ATOM   4672 C  CD1  . TYR   C 1 183 ? 29.746  -48.556 10.622  1.00 27.69 ? 187 TYR   C CD1  1 
ATOM   4673 C  CD2  . TYR   C 1 183 ? 27.413  -48.153 10.859  1.00 27.85 ? 187 TYR   C CD2  1 
ATOM   4674 C  CE1  . TYR   C 1 183 ? 29.915  -47.301 10.056  1.00 28.19 ? 187 TYR   C CE1  1 
ATOM   4675 C  CE2  . TYR   C 1 183 ? 27.566  -46.900 10.286  1.00 27.53 ? 187 TYR   C CE2  1 
ATOM   4676 C  CZ   . TYR   C 1 183 ? 28.821  -46.471 9.889   1.00 27.23 ? 187 TYR   C CZ   1 
ATOM   4677 O  OH   . TYR   C 1 183 ? 28.964  -45.237 9.327   1.00 26.35 ? 187 TYR   C OH   1 
ATOM   4678 N  N    . GLY   C 1 184 ? 28.304  -53.893 11.112  1.00 35.23 ? 188 GLY   C N    1 
ATOM   4679 C  CA   . GLY   C 1 184 ? 28.518  -55.257 11.576  1.00 36.66 ? 188 GLY   C CA   1 
ATOM   4680 C  C    . GLY   C 1 184 ? 27.792  -55.608 12.877  1.00 38.42 ? 188 GLY   C C    1 
ATOM   4681 O  O    . GLY   C 1 184 ? 28.026  -56.679 13.431  1.00 42.01 ? 188 GLY   C O    1 
ATOM   4682 N  N    . GLN   C 1 185 ? 26.894  -54.736 13.347  1.00 38.99 ? 189 GLN   C N    1 
ATOM   4683 C  CA   . GLN   C 1 185 ? 26.077  -55.005 14.521  1.00 39.51 ? 189 GLN   C CA   1 
ATOM   4684 C  C    . GLN   C 1 185 ? 24.801  -54.176 14.404  1.00 38.27 ? 189 GLN   C C    1 
ATOM   4685 O  O    . GLN   C 1 185 ? 24.738  -53.262 13.585  1.00 38.63 ? 189 GLN   C O    1 
ATOM   4686 C  CB   . GLN   C 1 185 ? 26.821  -54.660 15.813  1.00 40.34 ? 189 GLN   C CB   1 
ATOM   4687 N  N    . SER   C 1 186 ? 23.790  -54.510 15.214  1.00 38.77 ? 190 SER   C N    1 
ATOM   4688 C  CA   . SER   C 1 186 ? 22.556  -53.743 15.252  1.00 39.27 ? 190 SER   C CA   1 
ATOM   4689 C  C    . SER   C 1 186 ? 22.840  -52.371 15.864  1.00 39.30 ? 190 SER   C C    1 
ATOM   4690 O  O    . SER   C 1 186 ? 23.783  -52.221 16.640  1.00 40.11 ? 190 SER   C O    1 
ATOM   4691 C  CB   . SER   C 1 186 ? 21.468  -54.478 16.011  1.00 39.86 ? 190 SER   C CB   1 
ATOM   4692 N  N    . PRO   C 1 187 ? 22.058  -51.323 15.514  1.00 36.03 ? 191 PRO   C N    1 
ATOM   4693 C  CA   . PRO   C 1 187 ? 22.181  -50.017 16.163  1.00 36.24 ? 191 PRO   C CA   1 
ATOM   4694 C  C    . PRO   C 1 187 ? 21.979  -50.086 17.675  1.00 34.82 ? 191 PRO   C C    1 
ATOM   4695 O  O    . PRO   C 1 187 ? 21.190  -50.894 18.161  1.00 35.64 ? 191 PRO   C O    1 
ATOM   4696 C  CB   . PRO   C 1 187 ? 21.102  -49.127 15.519  1.00 36.57 ? 191 PRO   C CB   1 
ATOM   4697 C  CG   . PRO   C 1 187 ? 20.599  -49.896 14.317  1.00 36.74 ? 191 PRO   C CG   1 
ATOM   4698 C  CD   . PRO   C 1 187 ? 21.042  -51.338 14.452  1.00 36.56 ? 191 PRO   C CD   1 
ATOM   4699 N  N    . PRO   C 1 188 ? 22.651  -49.207 18.453  1.00 34.30 ? 192 PRO   C N    1 
ATOM   4700 C  CA   . PRO   C 1 188 ? 22.473  -49.163 19.908  1.00 34.91 ? 192 PRO   C CA   1 
ATOM   4701 C  C    . PRO   C 1 188 ? 21.019  -49.150 20.381  1.00 34.66 ? 192 PRO   C C    1 
ATOM   4702 O  O    . PRO   C 1 188 ? 20.678  -49.838 21.342  1.00 37.91 ? 192 PRO   C O    1 
ATOM   4703 C  CB   . PRO   C 1 188 ? 23.204  -47.870 20.317  1.00 35.57 ? 192 PRO   C CB   1 
ATOM   4704 C  CG   . PRO   C 1 188 ? 24.217  -47.635 19.224  1.00 35.50 ? 192 PRO   C CG   1 
ATOM   4705 C  CD   . PRO   C 1 188 ? 23.618  -48.212 17.962  1.00 34.08 ? 192 PRO   C CD   1 
ATOM   4706 N  N    . ASP   C 1 189 ? 20.175  -48.355 19.710  1.00 32.83 ? 193 ASP   C N    1 
ATOM   4707 C  CA   . ASP   C 1 189 ? 18.813  -48.104 20.158  1.00 32.25 ? 193 ASP   C CA   1 
ATOM   4708 C  C    . ASP   C 1 189 ? 17.889  -48.060 18.944  1.00 30.83 ? 193 ASP   C C    1 
ATOM   4709 O  O    . ASP   C 1 189 ? 18.082  -47.249 18.036  1.00 31.69 ? 193 ASP   C O    1 
ATOM   4710 C  CB   . ASP   C 1 189 ? 18.753  -46.835 20.996  1.00 34.00 ? 193 ASP   C CB   1 
ATOM   4711 C  CG   . ASP   C 1 189 ? 17.383  -46.206 21.212  1.00 35.42 ? 193 ASP   C CG   1 
ATOM   4712 O  OD1  . ASP   C 1 189 ? 16.391  -46.770 20.728  1.00 36.27 ? 193 ASP   C OD1  1 
ATOM   4713 O  OD2  . ASP   C 1 189 ? 17.331  -45.125 21.838  1.00 39.25 ? 193 ASP   C OD2  1 
ATOM   4714 N  N    . SER   C 1 190 ? 16.888  -48.948 18.945  1.00 28.67 ? 194 SER   C N    1 
ATOM   4715 C  CA   . SER   C 1 190 ? 15.915  -49.008 17.868  1.00 28.19 ? 194 SER   C CA   1 
ATOM   4716 C  C    . SER   C 1 190 ? 14.500  -48.845 18.419  1.00 27.07 ? 194 SER   C C    1 
ATOM   4717 O  O    . SER   C 1 190 ? 13.530  -49.033 17.680  1.00 28.56 ? 194 SER   C O    1 
ATOM   4718 C  CB   . SER   C 1 190 ? 16.068  -50.283 17.085  1.00 30.69 ? 194 SER   C CB   1 
ATOM   4719 O  OG   . SER   C 1 190 ? 16.127  -51.401 17.953  1.00 33.72 ? 194 SER   C OG   1 
ATOM   4720 N  N    . HIS   C 1 191 ? 14.391  -48.447 19.701  1.00 22.96 ? 195 HIS   C N    1 
ATOM   4721 C  CA   . HIS   C 1 191 ? 13.094  -48.349 20.345  1.00 20.91 ? 195 HIS   C CA   1 
ATOM   4722 C  C    . HIS   C 1 191 ? 12.665  -46.897 20.530  1.00 18.13 ? 195 HIS   C C    1 
ATOM   4723 O  O    . HIS   C 1 191 ? 11.544  -46.671 20.964  1.00 19.79 ? 195 HIS   C O    1 
ATOM   4724 C  CB   . HIS   C 1 191 ? 13.037  -49.147 21.658  1.00 22.45 ? 195 HIS   C CB   1 
ATOM   4725 C  CG   . HIS   C 1 191 ? 13.842  -48.602 22.788  1.00 25.39 ? 195 HIS   C CG   1 
ATOM   4726 N  ND1  . HIS   C 1 191 ? 15.216  -48.700 22.846  1.00 27.75 ? 195 HIS   C ND1  1 
ATOM   4727 C  CD2  . HIS   C 1 191 ? 13.468  -47.958 23.910  1.00 27.80 ? 195 HIS   C CD2  1 
ATOM   4728 C  CE1  . HIS   C 1 191 ? 15.649  -48.125 23.962  1.00 28.49 ? 195 HIS   C CE1  1 
ATOM   4729 N  NE2  . HIS   C 1 191 ? 14.602  -47.669 24.624  1.00 28.71 ? 195 HIS   C NE2  1 
ATOM   4730 N  N    . THR   C 1 192 ? 13.538  -45.930 20.211  1.00 16.11 ? 196 THR   C N    1 
ATOM   4731 C  CA   . THR   C 1 192 ? 13.222  -44.518 20.398  1.00 14.66 ? 196 THR   C CA   1 
ATOM   4732 C  C    . THR   C 1 192 ? 13.452  -43.746 19.102  1.00 13.98 ? 196 THR   C C    1 
ATOM   4733 O  O    . THR   C 1 192 ? 14.270  -44.130 18.264  1.00 14.45 ? 196 THR   C O    1 
ATOM   4734 C  CB   . THR   C 1 192 ? 14.030  -43.874 21.528  1.00 15.55 ? 196 THR   C CB   1 
ATOM   4735 O  OG1  . THR   C 1 192 ? 15.376  -43.668 21.097  1.00 16.69 ? 196 THR   C OG1  1 
ATOM   4736 C  CG2  . THR   C 1 192 ? 13.981  -44.672 22.816  1.00 16.77 ? 196 THR   C CG2  1 
ATOM   4737 N  N    . ALA   C 1 193 ? 12.756  -42.608 18.977  1.00 13.10 ? 197 ALA   C N    1 
ATOM   4738 C  CA   . ALA   C 1 193 ? 12.961  -41.724 17.838  1.00 12.53 ? 197 ALA   C CA   1 
ATOM   4739 C  C    . ALA   C 1 193 ? 14.413  -41.251 17.797  1.00 13.22 ? 197 ALA   C C    1 
ATOM   4740 O  O    . ALA   C 1 193 ? 15.011  -41.178 16.731  1.00 13.45 ? 197 ALA   C O    1 
ATOM   4741 C  CB   . ALA   C 1 193 ? 12.006  -40.552 17.874  1.00 12.88 ? 197 ALA   C CB   1 
ATOM   4742 N  N    . GLU   C 1 194 ? 14.980  -40.921 18.960  1.00 13.22 ? 198 GLU   C N    1 
ATOM   4743 C  CA   . GLU   C 1 194 ? 16.357  -40.452 19.008  1.00 13.49 ? 198 GLU   C CA   1 
ATOM   4744 C  C    . GLU   C 1 194 ? 17.309  -41.561 18.555  1.00 13.46 ? 198 GLU   C C    1 
ATOM   4745 O  O    . GLU   C 1 194 ? 18.272  -41.310 17.833  1.00 13.47 ? 198 GLU   C O    1 
ATOM   4746 C  CB   . GLU   C 1 194 ? 16.704  -39.965 20.413  1.00 15.06 ? 198 GLU   C CB   1 
ATOM   4747 C  CG   . GLU   C 1 194 ? 18.132  -39.451 20.515  1.00 16.65 ? 198 GLU   C CG   1 
ATOM   4748 C  CD   . GLU   C 1 194 ? 18.492  -38.836 21.855  1.00 19.85 ? 198 GLU   C CD   1 
ATOM   4749 O  OE1  . GLU   C 1 194 ? 17.579  -38.444 22.590  1.00 26.67 ? 198 GLU   C OE1  1 
ATOM   4750 O  OE2  . GLU   C 1 194 ? 19.689  -38.728 22.146  1.00 23.93 ? 198 GLU   C OE2  1 
ATOM   4751 N  N    . GLY   C 1 195 ? 17.032  -42.803 18.962  1.00 13.98 ? 199 GLY   C N    1 
ATOM   4752 C  CA   . GLY   C 1 195 ? 17.873  -43.915 18.560  1.00 14.11 ? 199 GLY   C CA   1 
ATOM   4753 C  C    . GLY   C 1 195 ? 17.887  -44.089 17.042  1.00 13.74 ? 199 GLY   C C    1 
ATOM   4754 O  O    . GLY   C 1 195 ? 18.938  -44.333 16.450  1.00 14.25 ? 199 GLY   C O    1 
ATOM   4755 N  N    . ASP   C 1 196 ? 16.714  -43.926 16.422  1.00 13.77 ? 200 ASP   C N    1 
ATOM   4756 C  CA   . ASP   C 1 196 ? 16.593  -44.062 14.978  1.00 14.76 ? 200 ASP   C CA   1 
ATOM   4757 C  C    . ASP   C 1 196 ? 17.291  -42.902 14.263  1.00 14.02 ? 200 ASP   C C    1 
ATOM   4758 O  O    . ASP   C 1 196 ? 17.874  -43.091 13.191  1.00 14.41 ? 200 ASP   C O    1 
ATOM   4759 C  CB   . ASP   C 1 196 ? 15.141  -44.244 14.563  1.00 16.75 ? 200 ASP   C CB   1 
ATOM   4760 C  CG   . ASP   C 1 196 ? 14.586  -45.645 14.804  1.00 20.50 ? 200 ASP   C CG   1 
ATOM   4761 O  OD1  . ASP   C 1 196 ? 15.369  -46.537 15.211  1.00 21.89 ? 200 ASP   C OD1  1 
ATOM   4762 O  OD2  . ASP   C 1 196 ? 13.365  -45.838 14.606  1.00 25.34 ? 200 ASP   C OD2  1 
ATOM   4763 N  N    . VAL   C 1 197 ? 17.225  -41.695 14.836  1.00 12.98 ? 201 VAL   C N    1 
ATOM   4764 C  CA   . VAL   C 1 197 ? 17.942  -40.561 14.278  1.00 12.97 ? 201 VAL   C CA   1 
ATOM   4765 C  C    . VAL   C 1 197 ? 19.454  -40.777 14.361  1.00 13.12 ? 201 VAL   C C    1 
ATOM   4766 O  O    . VAL   C 1 197 ? 20.178  -40.513 13.402  1.00 13.46 ? 201 VAL   C O    1 
ATOM   4767 C  CB   . VAL   C 1 197 ? 17.529  -39.258 14.984  1.00 13.74 ? 201 VAL   C CB   1 
ATOM   4768 C  CG1  . VAL   C 1 197 ? 18.534  -38.145 14.735  1.00 14.23 ? 201 VAL   C CG1  1 
ATOM   4769 C  CG2  . VAL   C 1 197 ? 16.137  -38.829 14.558  1.00 14.17 ? 201 VAL   C CG2  1 
ATOM   4770 N  N    . LEU   C 1 198 ? 19.946  -41.225 15.518  1.00 13.58 ? 202 LEU   C N    1 
ATOM   4771 C  CA   . LEU   C 1 198 ? 21.377  -41.428 15.693  1.00 14.12 ? 202 LEU   C CA   1 
ATOM   4772 C  C    . LEU   C 1 198 ? 21.904  -42.537 14.780  1.00 14.20 ? 202 LEU   C C    1 
ATOM   4773 O  O    . LEU   C 1 198 ? 22.999  -42.403 14.236  1.00 15.01 ? 202 LEU   C O    1 
ATOM   4774 C  CB   . LEU   C 1 198 ? 21.665  -41.691 17.168  1.00 14.64 ? 202 LEU   C CB   1 
ATOM   4775 C  CG   . LEU   C 1 198 ? 21.518  -40.472 18.085  1.00 15.69 ? 202 LEU   C CG   1 
ATOM   4776 C  CD1  . LEU   C 1 198 ? 21.721  -40.897 19.528  1.00 16.61 ? 202 LEU   C CD1  1 
ATOM   4777 C  CD2  . LEU   C 1 198 ? 22.482  -39.344 17.724  1.00 16.22 ? 202 LEU   C CD2  1 
ATOM   4778 N  N    . ALA   C 1 199 ? 21.133  -43.613 14.591  1.00 14.40 ? 203 ALA   C N    1 
ATOM   4779 C  CA   . ALA   C 1 199 ? 21.531  -44.672 13.670  1.00 14.81 ? 203 ALA   C CA   1 
ATOM   4780 C  C    . ALA   C 1 199 ? 21.604  -44.137 12.243  1.00 14.58 ? 203 ALA   C C    1 
ATOM   4781 O  O    . ALA   C 1 199 ? 22.533  -44.460 11.506  1.00 15.84 ? 203 ALA   C O    1 
ATOM   4782 C  CB   . ALA   C 1 199 ? 20.585  -45.842 13.744  1.00 15.43 ? 203 ALA   C CB   1 
ATOM   4783 N  N    . LEU   C 1 200 ? 20.599  -43.343 11.857  1.00 13.81 ? 204 LEU   C N    1 
ATOM   4784 C  CA   . LEU   C 1 200 ? 20.559  -42.763 10.525  1.00 14.14 ? 204 LEU   C CA   1 
ATOM   4785 C  C    . LEU   C 1 200 ? 21.751  -41.830 10.323  1.00 14.12 ? 204 LEU   C C    1 
ATOM   4786 O  O    . LEU   C 1 200 ? 22.381  -41.854 9.266   1.00 15.03 ? 204 LEU   C O    1 
ATOM   4787 C  CB   . LEU   C 1 200 ? 19.237  -42.039 10.295  1.00 14.63 ? 204 LEU   C CB   1 
ATOM   4788 C  CG   . LEU   C 1 200 ? 19.107  -41.307 8.954   1.00 15.58 ? 204 LEU   C CG   1 
ATOM   4789 C  CD1  . LEU   C 1 200 ? 19.310  -42.226 7.765   1.00 16.63 ? 204 LEU   C CD1  1 
ATOM   4790 C  CD2  . LEU   C 1 200 ? 17.766  -40.618 8.893   1.00 16.49 ? 204 LEU   C CD2  1 
ATOM   4791 N  N    . LEU   C 1 201 ? 22.068  -41.023 11.339  1.00 14.01 ? 205 LEU   C N    1 
ATOM   4792 C  CA   . LEU   C 1 201 ? 23.209  -40.130 11.258  1.00 14.80 ? 205 LEU   C CA   1 
ATOM   4793 C  C    . LEU   C 1 201 ? 24.474  -40.945 10.982  1.00 15.13 ? 205 LEU   C C    1 
ATOM   4794 O  O    . LEU   C 1 201 ? 25.265  -40.590 10.112  1.00 15.93 ? 205 LEU   C O    1 
ATOM   4795 C  CB   . LEU   C 1 201 ? 23.328  -39.319 12.548  1.00 15.27 ? 205 LEU   C CB   1 
ATOM   4796 C  CG   . LEU   C 1 201 ? 24.579  -38.444 12.665  1.00 16.22 ? 205 LEU   C CG   1 
ATOM   4797 C  CD1  . LEU   C 1 201 ? 24.683  -37.465 11.513  1.00 16.54 ? 205 LEU   C CD1  1 
ATOM   4798 C  CD2  . LEU   C 1 201 ? 24.585  -37.733 14.003  1.00 17.40 ? 205 LEU   C CD2  1 
ATOM   4799 N  N    . SER   C 1 202 ? 24.671  -42.038 11.727  1.00 15.88 ? 206 SER   C N    1 
ATOM   4800 C  CA   . SER   C 1 202 ? 25.870  -42.852 11.572  1.00 16.80 ? 206 SER   C CA   1 
ATOM   4801 C  C    . SER   C 1 202 ? 25.979  -43.407 10.152  1.00 17.62 ? 206 SER   C C    1 
ATOM   4802 O  O    . SER   C 1 202 ? 27.066  -43.443 9.574   1.00 18.66 ? 206 SER   C O    1 
ATOM   4803 C  CB   . SER   C 1 202 ? 25.908  -43.974 12.573  1.00 17.41 ? 206 SER   C CB   1 
ATOM   4804 O  OG   . SER   C 1 202 ? 25.997  -43.488 13.901  1.00 18.74 ? 206 SER   C OG   1 
ATOM   4805 N  N    . ILE   C 1 203 ? 24.852  -43.862 9.599   1.00 17.33 ? 207 ILE   C N    1 
ATOM   4806 C  CA   . ILE   C 1 203 ? 24.834  -44.371 8.237   1.00 18.72 ? 207 ILE   C CA   1 
ATOM   4807 C  C    . ILE   C 1 203 ? 25.211  -43.259 7.259   1.00 18.74 ? 207 ILE   C C    1 
ATOM   4808 O  O    . ILE   C 1 203 ? 25.941  -43.498 6.303   1.00 20.77 ? 207 ILE   C O    1 
ATOM   4809 C  CB   . ILE   C 1 203 ? 23.460  -44.965 7.897   1.00 19.78 ? 207 ILE   C CB   1 
ATOM   4810 C  CG1  . ILE   C 1 203 ? 23.213  -46.265 8.665   1.00 20.20 ? 207 ILE   C CG1  1 
ATOM   4811 C  CG2  . ILE   C 1 203 ? 23.316  -45.141 6.385   1.00 20.73 ? 207 ILE   C CG2  1 
ATOM   4812 C  CD1  . ILE   C 1 203 ? 21.754  -46.681 8.701   1.00 20.75 ? 207 ILE   C CD1  1 
ATOM   4813 N  N    . CYS   C 1 204 ? 24.684  -42.050 7.481   1.00 17.38 ? 208 CYS   C N    1 
ATOM   4814 C  CA   . CYS   C 1 204 ? 24.951  -40.942 6.577   1.00 17.79 ? 208 CYS   C CA   1 
ATOM   4815 C  C    . CYS   C 1 204 ? 26.401  -40.473 6.698   1.00 18.13 ? 208 CYS   C C    1 
ATOM   4816 O  O    . CYS   C 1 204 ? 26.920  -39.856 5.768   1.00 19.55 ? 208 CYS   C O    1 
ATOM   4817 C  CB   . CYS   C 1 204 ? 23.926  -39.834 6.782   1.00 17.91 ? 208 CYS   C CB   1 
ATOM   4818 S  SG   . CYS   C 1 204 ? 22.288  -40.313 6.172   1.00 19.57 ? 208 CYS   C SG   1 
ATOM   4819 N  N    . GLN   C 1 205 ? 27.057  -40.768 7.828   1.00 18.52 ? 209 GLN   C N    1 
ATOM   4820 C  CA   . GLN   C 1 205 ? 28.455  -40.399 8.024   1.00 19.82 ? 209 GLN   C CA   1 
ATOM   4821 C  C    . GLN   C 1 205 ? 29.421  -41.434 7.445   1.00 21.68 ? 209 GLN   C C    1 
ATOM   4822 O  O    . GLN   C 1 205 ? 30.628  -41.217 7.496   1.00 23.32 ? 209 GLN   C O    1 
ATOM   4823 C  CB   . GLN   C 1 205 ? 28.765  -40.195 9.506   1.00 19.78 ? 209 GLN   C CB   1 
ATOM   4824 C  CG   . GLN   C 1 205 ? 28.142  -38.940 10.103  1.00 20.07 ? 209 GLN   C CG   1 
ATOM   4825 C  CD   . GLN   C 1 205 ? 28.451  -38.821 11.575  1.00 21.46 ? 209 GLN   C CD   1 
ATOM   4826 O  OE1  . GLN   C 1 205 ? 27.862  -39.511 12.408  1.00 23.10 ? 209 GLN   C OE1  1 
ATOM   4827 N  NE2  . GLN   C 1 205 ? 29.424  -37.988 11.897  1.00 22.50 ? 209 GLN   C NE2  1 
ATOM   4828 N  N    . TRP   C 1 206 ? 28.908  -42.534 6.883   1.00 22.23 ? 210 TRP   C N    1 
ATOM   4829 C  CA   . TRP   C 1 206 ? 29.751  -43.555 6.277   1.00 24.47 ? 210 TRP   C CA   1 
ATOM   4830 C  C    . TRP   C 1 206 ? 30.543  -42.976 5.101   1.00 23.49 ? 210 TRP   C C    1 
ATOM   4831 O  O    . TRP   C 1 206 ? 31.766  -43.124 5.028   1.00 25.12 ? 210 TRP   C O    1 
ATOM   4832 C  CB   . TRP   C 1 206 ? 28.873  -44.738 5.844   1.00 26.36 ? 210 TRP   C CB   1 
ATOM   4833 C  CG   . TRP   C 1 206 ? 29.623  -45.843 5.156   1.00 30.04 ? 210 TRP   C CG   1 
ATOM   4834 C  CD1  . TRP   C 1 206 ? 30.677  -46.546 5.656   1.00 32.73 ? 210 TRP   C CD1  1 
ATOM   4835 C  CD2  . TRP   C 1 206 ? 29.385  -46.350 3.826   1.00 34.21 ? 210 TRP   C CD2  1 
ATOM   4836 N  NE1  . TRP   C 1 206 ? 31.101  -47.467 4.739   1.00 35.79 ? 210 TRP   C NE1  1 
ATOM   4837 C  CE2  . TRP   C 1 206 ? 30.334  -47.371 3.608   1.00 35.12 ? 210 TRP   C CE2  1 
ATOM   4838 C  CE3  . TRP   C 1 206 ? 28.464  -46.055 2.814   1.00 36.21 ? 210 TRP   C CE3  1 
ATOM   4839 C  CZ2  . TRP   C 1 206 ? 30.390  -48.090 2.416   1.00 38.46 ? 210 TRP   C CZ2  1 
ATOM   4840 C  CZ3  . TRP   C 1 206 ? 28.524  -46.765 1.633   1.00 38.49 ? 210 TRP   C CZ3  1 
ATOM   4841 C  CH2  . TRP   C 1 206 ? 29.473  -47.768 1.440   1.00 38.75 ? 210 TRP   C CH2  1 
ATOM   4842 N  N    . ARG   C 1 207 ? 29.827  -42.348 4.159   1.00 22.26 ? 211 ARG   C N    1 
ATOM   4843 C  CA   . ARG   C 1 207 ? 30.424  -41.665 3.017   1.00 22.53 ? 211 ARG   C CA   1 
ATOM   4844 C  C    . ARG   C 1 207 ? 29.758  -40.297 2.936   1.00 21.47 ? 211 ARG   C C    1 
ATOM   4845 O  O    . ARG   C 1 207 ? 28.839  -40.071 2.146   1.00 19.63 ? 211 ARG   C O    1 
ATOM   4846 C  CB   . ARG   C 1 207 ? 30.276  -42.446 1.706   1.00 24.67 ? 211 ARG   C CB   1 
ATOM   4847 C  CG   . ARG   C 1 207 ? 31.065  -43.748 1.662   1.00 26.96 ? 211 ARG   C CG   1 
ATOM   4848 C  CD   . ARG   C 1 207 ? 32.571  -43.533 1.699   1.00 29.86 ? 211 ARG   C CD   1 
ATOM   4849 N  N    . PRO   C 1 208 ? 30.156  -39.370 3.831   1.00 20.67 ? 212 PRO   C N    1 
ATOM   4850 C  CA   . PRO   C 1 208 ? 29.372  -38.162 4.073   1.00 20.03 ? 212 PRO   C CA   1 
ATOM   4851 C  C    . PRO   C 1 208 ? 29.349  -37.170 2.913   1.00 18.87 ? 212 PRO   C C    1 
ATOM   4852 O  O    . PRO   C 1 208 ? 28.315  -36.570 2.651   1.00 19.73 ? 212 PRO   C O    1 
ATOM   4853 C  CB   . PRO   C 1 208 ? 30.018  -37.581 5.340   1.00 20.66 ? 212 PRO   C CB   1 
ATOM   4854 C  CG   . PRO   C 1 208 ? 31.438  -38.078 5.304   1.00 21.74 ? 212 PRO   C CG   1 
ATOM   4855 C  CD   . PRO   C 1 208 ? 31.363  -39.452 4.667   1.00 21.94 ? 212 PRO   C CD   1 
ATOM   4856 N  N    . GLN   C 1 209 ? 30.476  -37.012 2.211   1.00 19.65 ? 213 GLN   C N    1 
ATOM   4857 C  CA   . GLN   C 1 209 ? 30.539  -36.037 1.128   1.00 20.39 ? 213 GLN   C CA   1 
ATOM   4858 C  C    . GLN   C 1 209 ? 29.608  -36.440 -0.024  1.00 19.99 ? 213 GLN   C C    1 
ATOM   4859 O  O    . GLN   C 1 209 ? 28.900  -35.630 -0.591  1.00 19.33 ? 213 GLN   C O    1 
ATOM   4860 C  CB   . GLN   C 1 209 ? 31.984  -35.849 0.657   1.00 22.31 ? 213 GLN   C CB   1 
ATOM   4861 C  CG   . GLN   C 1 209 ? 32.940  -35.400 1.760   1.00 24.57 ? 213 GLN   C CG   1 
ATOM   4862 C  CD   . GLN   C 1 209 ? 33.734  -36.532 2.380   1.00 28.00 ? 213 GLN   C CD   1 
ATOM   4863 O  OE1  . GLN   C 1 209 ? 33.255  -37.664 2.517   1.00 29.38 ? 213 GLN   C OE1  1 
ATOM   4864 N  NE2  . GLN   C 1 209 ? 34.985  -36.255 2.718   1.00 31.55 ? 213 GLN   C NE2  1 
ATOM   4865 N  N    . ALA   C 1 210 ? 29.632  -37.716 -0.383  1.00 21.57 ? 214 ALA   C N    1 
ATOM   4866 C  CA   . ALA   C 1 210 ? 28.727  -38.340 -1.332  1.00 20.29 ? 214 ALA   C CA   1 
ATOM   4867 C  C    . ALA   C 1 210 ? 27.276  -38.239 -0.872  1.00 18.87 ? 214 ALA   C C    1 
ATOM   4868 O  O    . ALA   C 1 210 ? 26.440  -37.891 -1.704  1.00 20.15 ? 214 ALA   C O    1 
ATOM   4869 C  CB   . ALA   C 1 210 ? 29.130  -39.790 -1.580  1.00 22.03 ? 214 ALA   C CB   1 
ATOM   4870 N  N    . LEU   C 1 211 ? 26.993  -38.487 0.451   1.00 20.75 ? 215 LEU   C N    1 
ATOM   4871 C  CA   . LEU   C 1 211 ? 25.630  -38.337 0.946   1.00 18.02 ? 215 LEU   C CA   1 
ATOM   4872 C  C    . LEU   C 1 211 ? 25.153  -36.891 0.715   1.00 18.31 ? 215 LEU   C C    1 
ATOM   4873 O  O    . LEU   C 1 211 ? 24.071  -36.651 0.177   1.00 19.16 ? 215 LEU   C O    1 
ATOM   4874 C  CB   . LEU   C 1 211 ? 25.559  -38.831 2.385   1.00 18.81 ? 215 LEU   C CB   1 
ATOM   4875 C  CG   . LEU   C 1 211 ? 24.165  -38.945 3.012   1.00 20.35 ? 215 LEU   C CG   1 
ATOM   4876 C  CD1  . LEU   C 1 211 ? 23.741  -37.621 3.596   1.00 21.04 ? 215 LEU   C CD1  1 
ATOM   4877 C  CD2  . LEU   C 1 211 ? 23.085  -39.450 2.057   1.00 20.96 ? 215 LEU   C CD2  1 
ATOM   4878 N  N    . LEU   C 1 212 ? 25.977  -35.912 1.095   1.00 17.40 ? 216 LEU   C N    1 
ATOM   4879 C  CA   . LEU   C 1 212 ? 25.586  -34.512 1.020   1.00 17.33 ? 216 LEU   C CA   1 
ATOM   4880 C  C    . LEU   C 1 212 ? 25.387  -34.047 -0.427  1.00 17.59 ? 216 LEU   C C    1 
ATOM   4881 O  O    . LEU   C 1 212 ? 24.472  -33.282 -0.711  1.00 18.38 ? 216 LEU   C O    1 
ATOM   4882 C  CB   . LEU   C 1 212 ? 26.634  -33.685 1.750   1.00 18.06 ? 216 LEU   C CB   1 
ATOM   4883 C  CG   . LEU   C 1 212 ? 26.348  -32.185 1.786   1.00 17.78 ? 216 LEU   C CG   1 
ATOM   4884 C  CD1  . LEU   C 1 212 ? 25.037  -31.853 2.489   1.00 18.35 ? 216 LEU   C CD1  1 
ATOM   4885 C  CD2  . LEU   C 1 212 ? 27.530  -31.510 2.453   1.00 17.92 ? 216 LEU   C CD2  1 
ATOM   4886 N  N    . ARG   C 1 213 ? 26.238  -34.505 -1.348  1.00 19.35 ? 217 ARG   C N    1 
ATOM   4887 C  CA   . ARG   C 1 213 ? 26.063  -34.193 -2.761  1.00 20.36 ? 217 ARG   C CA   1 
ATOM   4888 C  C    . ARG   C 1 213 ? 24.702  -34.682 -3.261  1.00 20.35 ? 217 ARG   C C    1 
ATOM   4889 O  O    . ARG   C 1 213 ? 24.003  -33.985 -3.993  1.00 20.22 ? 217 ARG   C O    1 
ATOM   4890 C  CB   . ARG   C 1 213 ? 27.189  -34.832 -3.584  1.00 23.21 ? 217 ARG   C CB   1 
ATOM   4891 C  CG   . ARG   C 1 213 ? 28.504  -34.071 -3.546  1.00 25.92 ? 217 ARG   C CG   1 
ATOM   4892 C  CD   . ARG   C 1 213 ? 29.427  -34.554 -4.646  1.00 28.39 ? 217 ARG   C CD   1 
ATOM   4893 N  NE   . ARG   C 1 213 ? 30.069  -35.833 -4.313  1.00 31.22 ? 217 ARG   C NE   1 
ATOM   4894 C  CZ   . ARG   C 1 213 ? 31.170  -35.959 -3.575  1.00 31.69 ? 217 ARG   C CZ   1 
ATOM   4895 N  NH1  . ARG   C 1 213 ? 31.795  -34.885 -3.124  1.00 34.01 ? 217 ARG   C NH1  1 
ATOM   4896 N  NH2  . ARG   C 1 213 ? 31.660  -37.156 -3.307  1.00 32.86 ? 217 ARG   C NH2  1 
ATOM   4897 N  N    . TRP   C 1 214 ? 24.331  -35.900 -2.872  1.00 20.68 ? 218 TRP   C N    1 
ATOM   4898 C  CA   . TRP   C 1 214 ? 23.061  -36.459 -3.291  1.00 21.57 ? 218 TRP   C CA   1 
ATOM   4899 C  C    . TRP   C 1 214 ? 21.904  -35.622 -2.743  1.00 20.53 ? 218 TRP   C C    1 
ATOM   4900 O  O    . TRP   C 1 214 ? 20.972  -35.290 -3.476  1.00 21.13 ? 218 TRP   C O    1 
ATOM   4901 C  CB   . TRP   C 1 214 ? 22.965  -37.928 -2.866  1.00 24.00 ? 218 TRP   C CB   1 
ATOM   4902 C  CG   . TRP   C 1 214 ? 21.898  -38.665 -3.628  1.00 26.59 ? 218 TRP   C CG   1 
ATOM   4903 C  CD1  . TRP   C 1 214 ? 22.071  -39.423 -4.750  1.00 28.46 ? 218 TRP   C CD1  1 
ATOM   4904 C  CD2  . TRP   C 1 214 ? 20.481  -38.658 -3.361  1.00 28.85 ? 218 TRP   C CD2  1 
ATOM   4905 N  NE1  . TRP   C 1 214 ? 20.870  -39.912 -5.177  1.00 30.88 ? 218 TRP   C NE1  1 
ATOM   4906 C  CE2  . TRP   C 1 214 ? 19.877  -39.465 -4.351  1.00 29.90 ? 218 TRP   C CE2  1 
ATOM   4907 C  CE3  . TRP   C 1 214 ? 19.672  -38.070 -2.385  1.00 29.38 ? 218 TRP   C CE3  1 
ATOM   4908 C  CZ2  . TRP   C 1 214 ? 18.503  -39.685 -4.399  1.00 32.15 ? 218 TRP   C CZ2  1 
ATOM   4909 C  CZ3  . TRP   C 1 214 ? 18.312  -38.289 -2.436  1.00 31.42 ? 218 TRP   C CZ3  1 
ATOM   4910 C  CH2  . TRP   C 1 214 ? 17.740  -39.083 -3.426  1.00 31.92 ? 218 TRP   C CH2  1 
ATOM   4911 N  N    . VAL   C 1 215 ? 21.987  -35.245 -1.459  1.00 18.81 ? 219 VAL   C N    1 
ATOM   4912 C  CA   . VAL   C 1 215 ? 20.947  -34.440 -0.838  1.00 19.28 ? 219 VAL   C CA   1 
ATOM   4913 C  C    . VAL   C 1 215 ? 20.779  -33.122 -1.599  1.00 18.82 ? 219 VAL   C C    1 
ATOM   4914 O  O    . VAL   C 1 215 ? 19.663  -32.711 -1.896  1.00 20.72 ? 219 VAL   C O    1 
ATOM   4915 C  CB   . VAL   C 1 215 ? 21.258  -34.214 0.653   1.00 19.09 ? 219 VAL   C CB   1 
ATOM   4916 C  CG1  . VAL   C 1 215 ? 20.396  -33.116 1.265   1.00 19.45 ? 219 VAL   C CG1  1 
ATOM   4917 C  CG2  . VAL   C 1 215 ? 21.130  -35.511 1.432   1.00 20.13 ? 219 VAL   C CG2  1 
ATOM   4918 N  N    . ASP   C 1 216 ? 21.890  -32.438 -1.879  1.00 18.72 ? 220 ASP   C N    1 
ATOM   4919 C  CA   . ASP   C 1 216 ? 21.838  -31.141 -2.533  1.00 18.66 ? 220 ASP   C CA   1 
ATOM   4920 C  C    . ASP   C 1 216 ? 21.206  -31.284 -3.916  1.00 20.43 ? 220 ASP   C C    1 
ATOM   4921 O  O    . ASP   C 1 216 ? 20.431  -30.434 -4.338  1.00 22.13 ? 220 ASP   C O    1 
ATOM   4922 C  CB   . ASP   C 1 216 ? 23.225  -30.514 -2.599  1.00 18.69 ? 220 ASP   C CB   1 
ATOM   4923 C  CG   . ASP   C 1 216 ? 23.707  -29.877 -1.303  1.00 18.53 ? 220 ASP   C CG   1 
ATOM   4924 O  OD1  . ASP   C 1 216 ? 22.854  -29.603 -0.428  1.00 18.60 ? 220 ASP   C OD1  1 
ATOM   4925 O  OD2  . ASP   C 1 216 ? 24.931  -29.667 -1.172  1.00 18.16 ? 220 ASP   C OD2  1 
ATOM   4926 N  N    . ALA   C 1 217 ? 21.523  -32.381 -4.606  1.00 21.21 ? 221 ALA   C N    1 
ATOM   4927 C  CA   . ALA   C 1 217 ? 21.012  -32.613 -5.948  1.00 22.56 ? 221 ALA   C CA   1 
ATOM   4928 C  C    . ALA   C 1 217 ? 19.520  -32.961 -5.959  1.00 23.27 ? 221 ALA   C C    1 
ATOM   4929 O  O    . ALA   C 1 217 ? 18.842  -32.692 -6.947  1.00 25.41 ? 221 ALA   C O    1 
ATOM   4930 C  CB   . ALA   C 1 217 ? 21.830  -33.703 -6.604  1.00 23.38 ? 221 ALA   C CB   1 
ATOM   4931 N  N    . HIS   C 1 218 ? 19.000  -33.558 -4.880  1.00 22.64 ? 222 HIS   C N    1 
ATOM   4932 C  CA   . HIS   C 1 218 ? 17.676  -34.169 -4.906  1.00 23.49 ? 222 HIS   C CA   1 
ATOM   4933 C  C    . HIS   C 1 218 ? 16.702  -33.586 -3.881  1.00 21.81 ? 222 HIS   C C    1 
ATOM   4934 O  O    . HIS   C 1 218 ? 15.581  -34.080 -3.771  1.00 22.49 ? 222 HIS   C O    1 
ATOM   4935 C  CB   . HIS   C 1 218 ? 17.797  -35.680 -4.695  1.00 25.46 ? 222 HIS   C CB   1 
ATOM   4936 C  CG   . HIS   C 1 218 ? 18.485  -36.361 -5.817  1.00 29.06 ? 222 HIS   C CG   1 
ATOM   4937 N  ND1  . HIS   C 1 218 ? 19.847  -36.552 -5.859  1.00 31.05 ? 222 HIS   C ND1  1 
ATOM   4938 C  CD2  . HIS   C 1 218 ? 18.000  -36.886 -6.947  1.00 31.61 ? 222 HIS   C CD2  1 
ATOM   4939 C  CE1  . HIS   C 1 218 ? 20.165  -37.174 -6.986  1.00 32.82 ? 222 HIS   C CE1  1 
ATOM   4940 N  NE2  . HIS   C 1 218 ? 19.061  -37.385 -7.661  1.00 33.75 ? 222 HIS   C NE2  1 
ATOM   4941 N  N    . ALA   C 1 219 ? 17.102  -32.527 -3.166  1.00 21.95 ? 223 ALA   C N    1 
ATOM   4942 C  CA   . ALA   C 1 219 ? 16.249  -31.874 -2.183  1.00 21.81 ? 223 ALA   C CA   1 
ATOM   4943 C  C    . ALA   C 1 219 ? 14.899  -31.492 -2.794  1.00 21.56 ? 223 ALA   C C    1 
ATOM   4944 O  O    . ALA   C 1 219 ? 14.849  -30.883 -3.863  1.00 22.27 ? 223 ALA   C O    1 
ATOM   4945 C  CB   . ALA   C 1 219 ? 16.957  -30.650 -1.643  1.00 22.57 ? 223 ALA   C CB   1 
ATOM   4946 N  N    A ARG   C 1 220 ? 13.819  -31.839 -2.085  0.50 21.46 ? 224 ARG   C N    1 
ATOM   4947 N  N    B ARG   C 1 220 ? 13.819  -31.849 -2.090  0.50 21.83 ? 224 ARG   C N    1 
ATOM   4948 C  CA   A ARG   C 1 220 ? 12.458  -31.599 -2.535  0.50 22.46 ? 224 ARG   C CA   1 
ATOM   4949 C  CA   B ARG   C 1 220 ? 12.458  -31.598 -2.532  0.50 22.97 ? 224 ARG   C CA   1 
ATOM   4950 C  C    A ARG   C 1 220 ? 11.798  -30.587 -1.601  0.50 21.03 ? 224 ARG   C C    1 
ATOM   4951 C  C    B ARG   C 1 220 ? 11.806  -30.580 -1.600  0.50 21.25 ? 224 ARG   C C    1 
ATOM   4952 O  O    A ARG   C 1 220 ? 11.899  -30.722 -0.383  0.50 19.88 ? 224 ARG   C O    1 
ATOM   4953 O  O    B ARG   C 1 220 ? 11.914  -30.710 -0.382  0.50 20.09 ? 224 ARG   C O    1 
ATOM   4954 C  CB   A ARG   C 1 220 ? 11.747  -32.958 -2.543  0.50 24.71 ? 224 ARG   C CB   1 
ATOM   4955 C  CB   B ARG   C 1 220 ? 11.704  -32.932 -2.499  0.50 25.89 ? 224 ARG   C CB   1 
ATOM   4956 C  CG   A ARG   C 1 220 ? 10.243  -32.925 -2.764  0.50 26.67 ? 224 ARG   C CG   1 
ATOM   4957 C  CG   B ARG   C 1 220 ? 10.192  -32.814 -2.603  0.50 28.47 ? 224 ARG   C CG   1 
ATOM   4958 C  CD   A ARG   C 1 220 ? 9.625   -34.320 -2.838  0.50 27.67 ? 224 ARG   C CD   1 
ATOM   4959 C  CD   B ARG   C 1 220 ? 9.464   -34.071 -2.141  0.50 30.55 ? 224 ARG   C CD   1 
ATOM   4960 N  NE   A ARG   C 1 220 ? 8.156   -34.310 -2.865  0.50 28.84 ? 224 ARG   C NE   1 
ATOM   4961 N  NE   B ARG   C 1 220 ? 10.130  -35.297 -2.595  0.50 33.07 ? 224 ARG   C NE   1 
ATOM   4962 C  CZ   A ARG   C 1 220 ? 7.394   -35.394 -2.825  0.50 29.48 ? 224 ARG   C CZ   1 
ATOM   4963 C  CZ   B ARG   C 1 220 ? 9.681   -36.528 -2.393  0.50 32.89 ? 224 ARG   C CZ   1 
ATOM   4964 N  NH1  A ARG   C 1 220 ? 7.948   -36.588 -2.720  0.50 30.30 ? 224 ARG   C NH1  1 
ATOM   4965 N  NH1  B ARG   C 1 220 ? 8.452   -36.728 -1.951  0.50 33.35 ? 224 ARG   C NH1  1 
ATOM   4966 N  NH2  A ARG   C 1 220 ? 6.077   -35.285 -2.882  0.50 29.99 ? 224 ARG   C NH2  1 
ATOM   4967 N  NH2  B ARG   C 1 220 ? 10.456  -37.557 -2.675  0.50 32.46 ? 224 ARG   C NH2  1 
ATOM   4968 N  N    . PRO   C 1 221 ? 11.096  -29.547 -2.112  1.00 21.21 ? 225 PRO   C N    1 
ATOM   4969 C  CA   . PRO   C 1 221 ? 10.380  -28.615 -1.238  1.00 21.24 ? 225 PRO   C CA   1 
ATOM   4970 C  C    . PRO   C 1 221 ? 9.394   -29.389 -0.377  1.00 21.00 ? 225 PRO   C C    1 
ATOM   4971 O  O    . PRO   C 1 221 ? 8.672   -30.254 -0.874  1.00 21.34 ? 225 PRO   C O    1 
ATOM   4972 C  CB   . PRO   C 1 221 ? 9.669   -27.646 -2.196  1.00 23.07 ? 225 PRO   C CB   1 
ATOM   4973 C  CG   . PRO   C 1 221 ? 10.459  -27.766 -3.469  1.00 23.81 ? 225 PRO   C CG   1 
ATOM   4974 C  CD   . PRO   C 1 221 ? 10.955  -29.204 -3.538  1.00 22.22 ? 225 PRO   C CD   1 
ATOM   4975 N  N    . PHE   C 1 222 ? 9.354   -29.050 0.911   1.00 21.00 ? 226 PHE   C N    1 
ATOM   4976 C  CA   . PHE   C 1 222 ? 8.495   -29.760 1.839   1.00 21.28 ? 226 PHE   C CA   1 
ATOM   4977 C  C    . PHE   C 1 222 ? 7.029   -29.554 1.465   1.00 22.57 ? 226 PHE   C C    1 
ATOM   4978 O  O    . PHE   C 1 222 ? 6.202   -30.430 1.718   1.00 22.27 ? 226 PHE   C O    1 
ATOM   4979 C  CB   . PHE   C 1 222 ? 8.804   -29.339 3.278   1.00 21.61 ? 226 PHE   C CB   1 
ATOM   4980 C  CG   . PHE   C 1 222 ? 8.142   -30.250 4.297   1.00 20.87 ? 226 PHE   C CG   1 
ATOM   4981 C  CD1  . PHE   C 1 222 ? 8.576   -31.559 4.464   1.00 22.27 ? 226 PHE   C CD1  1 
ATOM   4982 C  CD2  . PHE   C 1 222 ? 7.057   -29.814 5.050   1.00 22.16 ? 226 PHE   C CD2  1 
ATOM   4983 C  CE1  . PHE   C 1 222 ? 7.960   -32.398 5.375   1.00 21.70 ? 226 PHE   C CE1  1 
ATOM   4984 C  CE2  . PHE   C 1 222 ? 6.446   -30.663 5.960   1.00 23.14 ? 226 PHE   C CE2  1 
ATOM   4985 C  CZ   . PHE   C 1 222 ? 6.894   -31.954 6.112   1.00 22.35 ? 226 PHE   C CZ   1 
ATOM   4986 N  N    . GLY   C 1 223 ? 6.720   -28.414 0.838   1.00 24.49 ? 227 GLY   C N    1 
ATOM   4987 C  CA   . GLY   C 1 223 ? 5.364   -28.108 0.409   1.00 25.73 ? 227 GLY   C CA   1 
ATOM   4988 C  C    . GLY   C 1 223 ? 4.818   -29.096 -0.624  1.00 25.90 ? 227 GLY   C C    1 
ATOM   4989 O  O    . GLY   C 1 223 ? 3.606   -29.154 -0.833  1.00 29.52 ? 227 GLY   C O    1 
ATOM   4990 N  N    . THR   C 1 224 ? 5.689   -29.887 -1.262  1.00 24.76 ? 228 THR   C N    1 
ATOM   4991 C  CA   . THR   C 1 224 ? 5.233   -30.863 -2.240  1.00 26.02 ? 228 THR   C CA   1 
ATOM   4992 C  C    . THR   C 1 224 ? 4.843   -32.175 -1.562  1.00 23.98 ? 228 THR   C C    1 
ATOM   4993 O  O    . THR   C 1 224 ? 4.359   -33.083 -2.239  1.00 26.33 ? 228 THR   C O    1 
ATOM   4994 C  CB   . THR   C 1 224 ? 6.285   -31.096 -3.326  1.00 27.88 ? 228 THR   C CB   1 
ATOM   4995 O  OG1  . THR   C 1 224 ? 7.409   -31.731 -2.732  1.00 28.22 ? 228 THR   C OG1  1 
ATOM   4996 C  CG2  . THR   C 1 224 ? 6.713   -29.813 -4.013  1.00 28.38 ? 228 THR   C CG2  1 
ATOM   4997 N  N    . ILE   C 1 225 ? 5.048   -32.274 -0.241  1.00 21.89 ? 229 ILE   C N    1 
ATOM   4998 C  CA   . ILE   C 1 225 ? 4.636   -33.450 0.506   1.00 21.11 ? 229 ILE   C CA   1 
ATOM   4999 C  C    . ILE   C 1 225 ? 3.167   -33.297 0.864   1.00 21.57 ? 229 ILE   C C    1 
ATOM   5000 O  O    . ILE   C 1 225 ? 2.808   -32.365 1.575   1.00 22.41 ? 229 ILE   C O    1 
ATOM   5001 C  CB   . ILE   C 1 225 ? 5.470   -33.634 1.786   1.00 20.73 ? 229 ILE   C CB   1 
ATOM   5002 C  CG1  . ILE   C 1 225 ? 6.945   -33.839 1.487   1.00 21.54 ? 229 ILE   C CG1  1 
ATOM   5003 C  CG2  . ILE   C 1 225 ? 4.905   -34.765 2.646   1.00 20.64 ? 229 ILE   C CG2  1 
ATOM   5004 C  CD1  . ILE   C 1 225 ? 7.269   -35.120 0.738   1.00 21.61 ? 229 ILE   C CD1  1 
ATOM   5005 N  N    . ARG   C 1 226 ? 2.347   -34.229 0.382   1.00 22.72 ? 230 ARG   C N    1 
ATOM   5006 C  CA   . ARG   C 1 226 ? 0.931   -34.222 0.685   1.00 24.46 ? 230 ARG   C CA   1 
ATOM   5007 C  C    . ARG   C 1 226 ? 0.749   -34.734 2.108   1.00 22.92 ? 230 ARG   C C    1 
ATOM   5008 O  O    . ARG   C 1 226 ? 1.424   -35.672 2.520   1.00 23.63 ? 230 ARG   C O    1 
ATOM   5009 C  CB   . ARG   C 1 226 ? 0.159   -35.086 -0.316  1.00 27.31 ? 230 ARG   C CB   1 
ATOM   5010 C  CG   . ARG   C 1 226 ? 0.037   -34.510 -1.718  1.00 30.25 ? 230 ARG   C CG   1 
ATOM   5011 C  CD   . ARG   C 1 226 ? -0.939  -35.338 -2.537  1.00 34.35 ? 230 ARG   C CD   1 
ATOM   5012 N  N    . PRO   C 1 227 ? -0.180  -34.151 2.889   1.00 22.27 ? 231 PRO   C N    1 
ATOM   5013 C  CA   . PRO   C 1 227 ? -0.475  -34.670 4.219   1.00 21.07 ? 231 PRO   C CA   1 
ATOM   5014 C  C    . PRO   C 1 227 ? -0.960  -36.110 4.120   1.00 20.41 ? 231 PRO   C C    1 
ATOM   5015 O  O    . PRO   C 1 227 ? -1.672  -36.471 3.184   1.00 21.97 ? 231 PRO   C O    1 
ATOM   5016 C  CB   . PRO   C 1 227 ? -1.546  -33.725 4.753   1.00 23.19 ? 231 PRO   C CB   1 
ATOM   5017 C  CG   . PRO   C 1 227 ? -2.187  -33.179 3.511   1.00 24.86 ? 231 PRO   C CG   1 
ATOM   5018 C  CD   . PRO   C 1 227 ? -1.046  -33.019 2.527   1.00 23.96 ? 231 PRO   C CD   1 
ATOM   5019 N  N    . MET   C 1 228 ? -0.601  -36.901 5.135   1.00 18.76 ? 232 MET   C N    1 
ATOM   5020 C  CA   . MET   C 1 228 ? -0.971  -38.306 5.206   1.00 19.27 ? 232 MET   C CA   1 
ATOM   5021 C  C    . MET   C 1 228 ? -2.489  -38.469 5.177   1.00 20.57 ? 232 MET   C C    1 
ATOM   5022 O  O    . MET   C 1 228 ? -3.000  -39.438 4.619   1.00 23.47 ? 232 MET   C O    1 
ATOM   5023 C  CB   . MET   C 1 228 ? -0.419  -38.919 6.491   1.00 17.56 ? 232 MET   C CB   1 
ATOM   5024 C  CG   . MET   C 1 228 ? -0.596  -40.411 6.569   1.00 17.97 ? 232 MET   C CG   1 
ATOM   5025 S  SD   . MET   C 1 228 ? 0.238   -41.121 7.994   1.00 18.02 ? 232 MET   C SD   1 
ATOM   5026 C  CE   . MET   C 1 228 ? 1.940   -41.054 7.428   1.00 16.59 ? 232 MET   C CE   1 
ATOM   5027 N  N    . TYR   C 1 229 ? -3.189  -37.517 5.792   1.00 20.88 ? 233 TYR   C N    1 
ATOM   5028 C  CA   . TYR   C 1 229 ? -4.640  -37.494 5.840   1.00 21.92 ? 233 TYR   C CA   1 
ATOM   5029 C  C    . TYR   C 1 229 ? -5.064  -36.058 6.120   1.00 25.34 ? 233 TYR   C C    1 
ATOM   5030 O  O    . TYR   C 1 229 ? -4.224  -35.226 6.451   1.00 26.20 ? 233 TYR   C O    1 
ATOM   5031 C  CB   . TYR   C 1 229 ? -5.179  -38.463 6.900   1.00 20.11 ? 233 TYR   C CB   1 
ATOM   5032 C  CG   . TYR   C 1 229 ? -4.550  -38.307 8.280   1.00 19.05 ? 233 TYR   C CG   1 
ATOM   5033 C  CD1  . TYR   C 1 229 ? -4.946  -37.301 9.148   1.00 19.95 ? 233 TYR   C CD1  1 
ATOM   5034 C  CD2  . TYR   C 1 229 ? -3.552  -39.168 8.707   1.00 17.94 ? 233 TYR   C CD2  1 
ATOM   5035 C  CE1  . TYR   C 1 229 ? -4.376  -37.161 10.401  1.00 19.95 ? 233 TYR   C CE1  1 
ATOM   5036 C  CE2  . TYR   C 1 229 ? -2.982  -39.051 9.965   1.00 17.88 ? 233 TYR   C CE2  1 
ATOM   5037 C  CZ   . TYR   C 1 229 ? -3.390  -38.041 10.816  1.00 18.85 ? 233 TYR   C CZ   1 
ATOM   5038 O  OH   . TYR   C 1 229 ? -2.829  -37.907 12.055  1.00 19.87 ? 233 TYR   C OH   1 
ATOM   5039 N  N    . GLY   C 1 230 ? -6.371  -35.791 5.999   1.00 29.49 ? 234 GLY   C N    1 
ATOM   5040 C  CA   . GLY   C 1 230 ? -6.925  -34.474 6.277   1.00 34.62 ? 234 GLY   C CA   1 
ATOM   5041 C  C    . GLY   C 1 230 ? -7.798  -34.473 7.532   1.00 39.58 ? 234 GLY   C C    1 
ATOM   5042 O  O    . GLY   C 1 230 ? -7.932  -35.490 8.211   1.00 40.89 ? 234 GLY   C O    1 
ATOM   5043 N  N    . VAL   C 1 231 ? -8.394  -33.308 7.824   1.00 45.84 ? 235 VAL   C N    1 
ATOM   5044 C  CA   . VAL   C 1 231 ? -9.305  -33.146 8.947   1.00 47.67 ? 235 VAL   C CA   1 
ATOM   5045 C  C    . VAL   C 1 231 ? -10.680 -33.714 8.551   1.00 49.85 ? 235 VAL   C C    1 
ATOM   5046 O  O    . VAL   C 1 231 ? -11.163 -34.610 9.280   1.00 53.89 ? 235 VAL   C O    1 
ATOM   5047 C  CB   . VAL   C 1 231 ? -9.414  -31.665 9.363   1.00 49.99 ? 235 VAL   C CB   1 
HETATM 5048 C  C4   . A1B7T D 2 .   ? 34.839  15.634  9.989   1.00 12.14 ? 301 A1B7T A C4   1 
HETATM 5049 C  C5   . A1B7T D 2 .   ? 36.050  15.716  9.349   1.00 12.22 ? 301 A1B7T A C5   1 
HETATM 5050 C  C6   . A1B7T D 2 .   ? 36.694  16.947  9.308   1.00 12.69 ? 301 A1B7T A C6   1 
HETATM 5051 C  C7   . A1B7T D 2 .   ? 36.110  18.056  9.914   1.00 12.72 ? 301 A1B7T A C7   1 
HETATM 5052 C  C8   . A1B7T D 2 .   ? 37.969  17.065  8.541   1.00 13.75 ? 301 A1B7T A C8   1 
HETATM 5053 C  C13  . A1B7T D 2 .   ? 41.167  16.630  11.945  1.00 16.37 ? 301 A1B7T A C13  1 
HETATM 5054 C  C15  . A1B7T D 2 .   ? 41.375  14.287  12.238  1.00 16.36 ? 301 A1B7T A C15  1 
HETATM 5055 C  C17  . A1B7T D 2 .   ? 39.620  15.106  11.036  1.00 14.45 ? 301 A1B7T A C17  1 
HETATM 5056 C  C20  . A1B7T D 2 .   ? 41.983  19.380  9.254   1.00 18.44 ? 301 A1B7T A C20  1 
HETATM 5057 C  C21  . A1B7T D 2 .   ? 42.522  20.647  9.373   1.00 19.36 ? 301 A1B7T A C21  1 
HETATM 5058 C  C22  . A1B7T D 2 .   ? 41.900  21.725  8.781   1.00 18.07 ? 301 A1B7T A C22  1 
HETATM 5059 C  C24  . A1B7T D 2 .   ? 40.190  20.256  7.939   1.00 17.55 ? 301 A1B7T A C24  1 
HETATM 5060 F  F1   . A1B7T D 2 .   ? 34.311  18.991  11.094  1.00 13.89 ? 301 A1B7T A F1   1 
HETATM 5061 C  C2   . A1B7T D 2 .   ? 34.895  17.896  10.535  1.00 12.30 ? 301 A1B7T A C2   1 
HETATM 5062 C  C3   . A1B7T D 2 .   ? 34.224  16.701  10.597  1.00 12.17 ? 301 A1B7T A C3   1 
HETATM 5063 O  O9   . A1B7T D 2 .   ? 37.983  16.762  7.361   1.00 15.32 ? 301 A1B7T A O9   1 
HETATM 5064 N  N10  . A1B7T D 2 .   ? 39.077  17.476  9.178   1.00 14.39 ? 301 A1B7T A N10  1 
HETATM 5065 C  C11  . A1B7T D 2 .   ? 39.202  17.554  10.636  1.00 14.07 ? 301 A1B7T A C11  1 
HETATM 5066 C  C12  . A1B7T D 2 .   ? 40.018  16.419  11.208  1.00 14.90 ? 301 A1B7T A C12  1 
HETATM 5067 C  C14  . A1B7T D 2 .   ? 41.861  15.554  12.470  1.00 16.78 ? 301 A1B7T A C14  1 
HETATM 5068 N  N16  . A1B7T D 2 .   ? 40.272  14.045  11.533  1.00 15.20 ? 301 A1B7T A N16  1 
HETATM 5069 C  C18  . A1B7T D 2 .   ? 40.290  17.753  8.406   1.00 16.13 ? 301 A1B7T A C18  1 
HETATM 5070 C  C19  . A1B7T D 2 .   ? 40.811  19.162  8.535   1.00 17.91 ? 301 A1B7T A C19  1 
HETATM 5071 C  C23  . A1B7T D 2 .   ? 40.739  21.525  8.066   1.00 18.46 ? 301 A1B7T A C23  1 
HETATM 5072 CL CL25 . A1B7T D 2 .   ? 38.737  20.018  7.019   1.00 18.80 ? 301 A1B7T A CL25 1 
HETATM 5073 CL CL26 . A1B7T D 2 .   ? 39.959  22.889  7.387   1.00 20.63 ? 301 A1B7T A CL26 1 
HETATM 5074 F  F27  . A1B7T D 2 .   ? 34.211  14.429  10.017  1.00 13.64 ? 301 A1B7T A F27  1 
HETATM 5075 MG MG   . MG    E 3 .   ? 39.626  12.026  10.929  1.00 13.26 ? 302 MG    A MG   1 
HETATM 5076 C  C1   . EDO   F 4 .   ? 43.766  13.423  14.876  1.00 26.67 ? 303 EDO   A C1   1 
HETATM 5077 O  O1   . EDO   F 4 .   ? 44.765  13.443  13.920  1.00 25.73 ? 303 EDO   A O1   1 
HETATM 5078 C  C2   . EDO   F 4 .   ? 43.831  14.543  15.811  1.00 29.57 ? 303 EDO   A C2   1 
HETATM 5079 O  O2   . EDO   F 4 .   ? 42.587  15.052  16.114  1.00 32.89 ? 303 EDO   A O2   1 
HETATM 5080 X  UNK  . UNX   G 5 .   ? 38.226  25.434  7.182   1.00 21.91 ? 304 UNX   A UNK  1 
HETATM 5081 X  UNK  . UNX   H 5 .   ? 41.536  28.302  4.972   1.00 13.07 ? 305 UNX   A UNK  1 
HETATM 5082 C  C4   . A1B7T I 2 .   ? 28.286  -22.299 33.356  1.00 12.40 ? 301 A1B7T B C4   1 
HETATM 5083 C  C5   . A1B7T I 2 .   ? 29.127  -23.274 32.871  1.00 12.44 ? 301 A1B7T B C5   1 
HETATM 5084 C  C6   . A1B7T I 2 .   ? 30.497  -23.095 33.006  1.00 12.47 ? 301 A1B7T B C6   1 
HETATM 5085 C  C7   . A1B7T I 2 .   ? 30.988  -21.948 33.625  1.00 12.33 ? 301 A1B7T B C7   1 
HETATM 5086 C  C8   . A1B7T I 2 .   ? 31.429  -24.100 32.414  1.00 13.78 ? 301 A1B7T B C8   1 
HETATM 5087 C  C13  . A1B7T I 2 .   ? 32.587  -26.793 36.078  1.00 17.22 ? 301 A1B7T B C13  1 
HETATM 5088 C  C15  . A1B7T I 2 .   ? 30.795  -28.350 36.194  1.00 17.51 ? 301 A1B7T B C15  1 
HETATM 5089 C  C17  . A1B7T I 2 .   ? 30.540  -26.452 34.953  1.00 15.63 ? 301 A1B7T B C17  1 
HETATM 5090 C  C20  . A1B7T I 2 .   ? 35.568  -25.979 33.642  1.00 19.09 ? 301 A1B7T B C20  1 
HETATM 5091 C  C21  . A1B7T I 2 .   ? 36.890  -25.655 33.887  1.00 20.55 ? 301 A1B7T B C21  1 
HETATM 5092 C  C22  . A1B7T I 2 .   ? 37.444  -24.524 33.319  1.00 19.62 ? 301 A1B7T B C22  1 
HETATM 5093 C  C24  . A1B7T I 2 .   ? 35.336  -24.050 32.255  1.00 17.45 ? 301 A1B7T B C24  1 
HETATM 5094 F  F1   . A1B7T I 2 .   ? 30.572  -19.904 34.698  1.00 13.84 ? 301 A1B7T B F1   1 
HETATM 5095 C  C2   . A1B7T I 2 .   ? 30.088  -21.015 34.086  1.00 12.56 ? 301 A1B7T B C2   1 
HETATM 5096 C  C3   . A1B7T I 2 .   ? 28.727  -21.149 33.970  1.00 12.35 ? 301 A1B7T B C3   1 
HETATM 5097 O  O9   . A1B7T I 2 .   ? 31.339  -24.372 31.224  1.00 15.39 ? 301 A1B7T B O9   1 
HETATM 5098 N  N10  . A1B7T I 2 .   ? 32.340  -24.697 33.211  1.00 14.59 ? 301 A1B7T B N10  1 
HETATM 5099 C  C11  . A1B7T I 2 .   ? 32.329  -24.692 34.678  1.00 14.57 ? 301 A1B7T B C11  1 
HETATM 5100 C  C12  . A1B7T I 2 .   ? 31.809  -25.993 35.251  1.00 15.66 ? 301 A1B7T B C12  1 
HETATM 5101 C  C14  . A1B7T I 2 .   ? 32.083  -27.989 36.559  1.00 17.55 ? 301 A1B7T B C14  1 
HETATM 5102 N  N16  . A1B7T I 2 .   ? 30.022  -27.602 35.401  1.00 16.14 ? 301 A1B7T B N16  1 
HETATM 5103 C  C18  . A1B7T I 2 .   ? 33.333  -25.581 32.583  1.00 15.80 ? 301 A1B7T B C18  1 
HETATM 5104 C  C19  . A1B7T I 2 .   ? 34.768  -25.185 32.825  1.00 16.97 ? 301 A1B7T B C19  1 
HETATM 5105 C  C23  . A1B7T I 2 .   ? 36.663  -23.728 32.506  1.00 18.41 ? 301 A1B7T B C23  1 
HETATM 5106 CL CL25 . A1B7T I 2 .   ? 34.407  -23.070 31.178  1.00 19.03 ? 301 A1B7T B CL25 1 
HETATM 5107 CL CL26 . A1B7T I 2 .   ? 37.375  -22.348 31.781  1.00 19.49 ? 301 A1B7T B CL26 1 
HETATM 5108 F  F27  . A1B7T I 2 .   ? 26.940  -22.490 33.229  1.00 14.41 ? 301 A1B7T B F27  1 
HETATM 5109 MG MG   . MG    J 3 .   ? 28.104  -28.343 34.546  1.00 13.63 ? 302 MG    B MG   1 
HETATM 5110 C  C1   . EDO   K 4 .   ? 27.265  -13.616 19.752  1.00 33.93 ? 303 EDO   B C1   1 
HETATM 5111 O  O1   . EDO   K 4 .   ? 27.342  -14.340 18.543  1.00 36.17 ? 303 EDO   B O1   1 
HETATM 5112 C  C2   . EDO   K 4 .   ? 26.918  -12.192 19.553  1.00 34.94 ? 303 EDO   B C2   1 
HETATM 5113 O  O2   . EDO   K 4 .   ? 26.586  -11.484 20.734  1.00 35.00 ? 303 EDO   B O2   1 
HETATM 5114 X  UNK  . UNX   L 5 .   ? 4.462   -27.981 50.697  1.00 26.33 ? 304 UNX   B UNK  1 
HETATM 5115 X  UNK  . UNX   M 5 .   ? 34.691  -20.424 40.092  1.00 9.55  ? 305 UNX   B UNK  1 
HETATM 5116 C  C4   . A1B7T N 2 .   ? 5.638   -42.150 11.369  1.00 13.79 ? 301 A1B7T C C4   1 
HETATM 5117 C  C5   . A1B7T N 2 .   ? 6.162   -43.145 12.155  1.00 13.61 ? 301 A1B7T C C5   1 
HETATM 5118 C  C6   . A1B7T N 2 .   ? 5.522   -44.380 12.170  1.00 13.82 ? 301 A1B7T C C6   1 
HETATM 5119 C  C7   . A1B7T N 2 .   ? 4.379   -44.577 11.398  1.00 14.34 ? 301 A1B7T C C7   1 
HETATM 5120 C  C8   . A1B7T N 2 .   ? 6.057   -45.444 13.068  1.00 15.73 ? 301 A1B7T C C8   1 
HETATM 5121 C  C13  . A1B7T N 2 .   ? 8.746   -47.988 10.202  1.00 17.06 ? 301 A1B7T C C13  1 
HETATM 5122 C  C15  . A1B7T N 2 .   ? 10.791  -46.783 10.149  1.00 16.95 ? 301 A1B7T C C15  1 
HETATM 5123 C  C17  . A1B7T N 2 .   ? 8.923   -45.767 10.978  1.00 15.77 ? 301 A1B7T C C17  1 
HETATM 5124 C  C20  . A1B7T N 2 .   ? 6.559   -50.129 12.736  1.00 19.88 ? 301 A1B7T C C20  1 
HETATM 5125 C  C21  . A1B7T N 2 .   ? 5.851   -51.311 12.613  1.00 20.28 ? 301 A1B7T C C21  1 
HETATM 5126 C  C22  . A1B7T N 2 .   ? 4.538   -51.381 13.038  1.00 20.05 ? 301 A1B7T C C22  1 
HETATM 5127 C  C24  . A1B7T N 2 .   ? 4.652   -49.073 13.712  1.00 19.28 ? 301 A1B7T C C24  1 
HETATM 5128 F  F1   . A1B7T N 2 .   ? 2.777   -43.721 9.902   1.00 15.69 ? 301 A1B7T C F1   1 
HETATM 5129 C  C2   . A1B7T N 2 .   ? 3.914   -43.533 10.637  1.00 13.80 ? 301 A1B7T C C2   1 
HETATM 5130 C  C3   . A1B7T N 2 .   ? 4.515   -42.302 10.592  1.00 13.84 ? 301 A1B7T C C3   1 
HETATM 5131 O  O9   . A1B7T N 2 .   ? 6.186   -45.201 14.262  1.00 17.71 ? 301 A1B7T C O9   1 
HETATM 5132 N  N10  . A1B7T N 2 .   ? 6.437   -46.628 12.532  1.00 15.60 ? 301 A1B7T C N10  1 
HETATM 5133 C  C11  . A1B7T N 2 .   ? 6.662   -46.878 11.103  1.00 15.17 ? 301 A1B7T C C11  1 
HETATM 5134 C  C12  . A1B7T N 2 .   ? 8.131   -46.882 10.757  1.00 15.78 ? 301 A1B7T C C12  1 
HETATM 5135 C  C14  . A1B7T N 2 .   ? 10.092  -47.947 9.890   1.00 17.05 ? 301 A1B7T C C14  1 
HETATM 5136 N  N16  . A1B7T N 2 .   ? 10.228  -45.696 10.686  1.00 15.97 ? 301 A1B7T C N16  1 
HETATM 5137 C  C18  . A1B7T N 2 .   ? 6.796   -47.731 13.438  1.00 17.12 ? 301 A1B7T C C18  1 
HETATM 5138 C  C19  . A1B7T N 2 .   ? 5.974   -48.989 13.284  1.00 18.96 ? 301 A1B7T C C19  1 
HETATM 5139 C  C23  . A1B7T N 2 .   ? 3.946   -50.261 13.585  1.00 19.76 ? 301 A1B7T C C23  1 
HETATM 5140 CL CL25 . A1B7T N 2 .   ? 3.908   -47.702 14.448  1.00 20.70 ? 301 A1B7T C CL25 1 
HETATM 5141 CL CL26 . A1B7T N 2 .   ? 2.308   -50.367 14.109  1.00 21.34 ? 301 A1B7T C CL26 1 
HETATM 5142 F  F27  . A1B7T N 2 .   ? 6.252   -40.946 11.379  1.00 15.47 ? 301 A1B7T C F27  1 
HETATM 5143 MG MG   . MG    O 3 .   ? 11.421  -43.975 11.403  1.00 13.62 ? 302 MG    C MG   1 
HETATM 5144 C  C1   . EDO   P 4 .   ? 13.137  -48.419 8.201   1.00 29.23 ? 303 EDO   C C1   1 
HETATM 5145 O  O1   . EDO   P 4 .   ? 13.612  -49.315 9.148   1.00 29.28 ? 303 EDO   C O1   1 
HETATM 5146 C  C2   . EDO   P 4 .   ? 12.791  -49.035 6.916   1.00 30.84 ? 303 EDO   C C2   1 
HETATM 5147 O  O2   . EDO   P 4 .   ? 11.530  -48.691 6.471   1.00 30.55 ? 303 EDO   C O2   1 
HETATM 5148 C  C1   . EDO   Q 4 .   ? 23.808  -21.672 -1.480  1.00 29.87 ? 304 EDO   C C1   1 
HETATM 5149 O  O1   . EDO   Q 4 .   ? 23.706  -22.562 -2.531  1.00 24.16 ? 304 EDO   C O1   1 
HETATM 5150 C  C2   . EDO   Q 4 .   ? 22.513  -21.246 -0.955  1.00 31.41 ? 304 EDO   C C2   1 
HETATM 5151 O  O2   . EDO   Q 4 .   ? 21.935  -22.262 -0.209  1.00 30.73 ? 304 EDO   C O2   1 
HETATM 5152 X  UNK  . UNX   R 5 .   ? -1.230  -54.569 16.206  1.00 18.35 ? 305 UNX   C UNK  1 
HETATM 5153 X  UNK  . UNX   S 5 .   ? -0.984  -50.266 13.179  1.00 39.65 ? 306 UNX   C UNK  1 
HETATM 5154 O  O    . HOH   T 6 .   ? 47.095  24.394  5.015   1.00 35.38 ? 401 HOH   A O    1 
HETATM 5155 O  O    . HOH   T 6 .   ? 40.683  14.533  7.823   1.00 36.35 ? 402 HOH   A O    1 
HETATM 5156 O  O    . HOH   T 6 .   ? 48.972  24.884  -1.086  1.00 54.36 ? 403 HOH   A O    1 
HETATM 5157 O  O    . HOH   T 6 .   ? 39.496  4.787   -1.093  1.00 44.27 ? 404 HOH   A O    1 
HETATM 5158 O  O    . HOH   T 6 .   ? 37.783  -12.228 25.410  1.00 36.95 ? 405 HOH   A O    1 
HETATM 5159 O  O    . HOH   T 6 .   ? 34.090  13.656  24.086  1.00 45.27 ? 406 HOH   A O    1 
HETATM 5160 O  O    . HOH   T 6 .   ? 29.878  -8.499  3.990   1.00 14.95 ? 407 HOH   A O    1 
HETATM 5161 O  O    . HOH   T 6 .   ? 36.847  14.167  20.187  1.00 23.51 ? 408 HOH   A O    1 
HETATM 5162 O  O    . HOH   T 6 .   ? 23.277  8.682   -3.395  1.00 25.74 ? 409 HOH   A O    1 
HETATM 5163 O  O    . HOH   T 6 .   ? 19.220  0.231   3.694   1.00 30.91 ? 410 HOH   A O    1 
HETATM 5164 O  O    . HOH   T 6 .   ? 37.763  12.738  10.369  1.00 13.59 ? 411 HOH   A O    1 
HETATM 5165 O  O    . HOH   T 6 .   ? 40.629  16.295  -5.847  1.00 33.39 ? 412 HOH   A O    1 
HETATM 5166 O  O    . HOH   T 6 .   ? 40.385  12.429  9.036   1.00 17.83 ? 413 HOH   A O    1 
HETATM 5167 O  O    . HOH   T 6 .   ? 20.023  10.631  17.359  1.00 43.66 ? 414 HOH   A O    1 
HETATM 5168 O  O    A HOH   T 6 .   ? 27.893  16.073  19.454  0.50 24.38 ? 415 HOH   A O    1 
HETATM 5169 O  O    B HOH   T 6 .   ? 27.919  17.605  19.116  0.50 33.73 ? 415 HOH   A O    1 
HETATM 5170 O  O    . HOH   T 6 .   ? 54.156  2.478   8.481   1.00 44.86 ? 416 HOH   A O    1 
HETATM 5171 O  O    . HOH   T 6 .   ? 36.178  -9.128  9.956   1.00 25.86 ? 417 HOH   A O    1 
HETATM 5172 O  O    . HOH   T 6 .   ? 23.711  13.381  24.627  1.00 49.74 ? 418 HOH   A O    1 
HETATM 5173 O  O    . HOH   T 6 .   ? 21.365  18.924  10.929  1.00 37.61 ? 419 HOH   A O    1 
HETATM 5174 O  O    . HOH   T 6 .   ? 47.360  -2.822  10.132  1.00 21.16 ? 420 HOH   A O    1 
HETATM 5175 O  O    . HOH   T 6 .   ? 24.808  -10.464 18.865  1.00 38.84 ? 421 HOH   A O    1 
HETATM 5176 O  O    . HOH   T 6 .   ? 38.716  11.473  12.687  1.00 14.60 ? 422 HOH   A O    1 
HETATM 5177 O  O    . HOH   T 6 .   ? 21.443  12.598  18.331  1.00 38.01 ? 423 HOH   A O    1 
HETATM 5178 O  O    . HOH   T 6 .   ? 29.305  -2.651  26.137  1.00 21.89 ? 424 HOH   A O    1 
HETATM 5179 O  O    . HOH   T 6 .   ? 49.575  1.261   8.743   1.00 25.59 ? 425 HOH   A O    1 
HETATM 5180 O  O    . HOH   T 6 .   ? 36.468  7.456   -1.384  1.00 23.05 ? 426 HOH   A O    1 
HETATM 5181 O  O    . HOH   T 6 .   ? 32.391  19.331  17.263  1.00 23.99 ? 427 HOH   A O    1 
HETATM 5182 O  O    . HOH   T 6 .   ? 24.501  -2.268  17.089  1.00 19.59 ? 428 HOH   A O    1 
HETATM 5183 O  O    . HOH   T 6 .   ? 39.242  12.141  25.137  1.00 41.24 ? 429 HOH   A O    1 
HETATM 5184 O  O    . HOH   T 6 .   ? 28.841  17.184  -7.757  1.00 32.54 ? 430 HOH   A O    1 
HETATM 5185 O  O    . HOH   T 6 .   ? 24.916  18.060  3.010   1.00 28.89 ? 431 HOH   A O    1 
HETATM 5186 O  O    . HOH   T 6 .   ? 28.002  10.366  23.937  1.00 41.92 ? 432 HOH   A O    1 
HETATM 5187 O  O    . HOH   T 6 .   ? 47.023  8.682   8.094   1.00 33.74 ? 433 HOH   A O    1 
HETATM 5188 O  O    . HOH   T 6 .   ? 28.754  23.576  13.203  1.00 27.65 ? 434 HOH   A O    1 
HETATM 5189 O  O    . HOH   T 6 .   ? 19.810  9.693   -5.027  1.00 43.12 ? 435 HOH   A O    1 
HETATM 5190 O  O    A HOH   T 6 .   ? 39.387  22.940  -7.498  0.50 21.45 ? 436 HOH   A O    1 
HETATM 5191 O  O    B HOH   T 6 .   ? 37.831  25.177  -6.767  0.50 28.76 ? 436 HOH   A O    1 
HETATM 5192 O  O    . HOH   T 6 .   ? 34.506  -8.873  5.985   1.00 24.35 ? 437 HOH   A O    1 
HETATM 5193 O  O    . HOH   T 6 .   ? 15.522  13.293  2.673   1.00 49.84 ? 438 HOH   A O    1 
HETATM 5194 O  O    . HOH   T 6 .   ? 37.905  -14.177 19.089  1.00 37.08 ? 439 HOH   A O    1 
HETATM 5195 O  O    . HOH   T 6 .   ? 21.622  5.163   20.060  1.00 35.77 ? 440 HOH   A O    1 
HETATM 5196 O  O    . HOH   T 6 .   ? 20.393  2.031   13.258  1.00 41.64 ? 441 HOH   A O    1 
HETATM 5197 O  O    . HOH   T 6 .   ? 21.616  8.155   13.731  1.00 33.55 ? 442 HOH   A O    1 
HETATM 5198 O  O    . HOH   T 6 .   ? 23.299  20.768  4.977   1.00 37.78 ? 443 HOH   A O    1 
HETATM 5199 O  O    . HOH   T 6 .   ? 23.424  -7.346  11.276  1.00 35.70 ? 444 HOH   A O    1 
HETATM 5200 O  O    . HOH   T 6 .   ? 29.994  14.358  20.028  1.00 29.90 ? 445 HOH   A O    1 
HETATM 5201 O  O    . HOH   T 6 .   ? 23.033  20.560  17.502  1.00 48.68 ? 446 HOH   A O    1 
HETATM 5202 O  O    . HOH   T 6 .   ? 39.327  7.266   1.032   1.00 19.60 ? 447 HOH   A O    1 
HETATM 5203 O  O    . HOH   T 6 .   ? 26.932  -6.839  29.851  1.00 31.88 ? 448 HOH   A O    1 
HETATM 5204 O  O    . HOH   T 6 .   ? 26.458  10.841  -10.403 1.00 41.92 ? 449 HOH   A O    1 
HETATM 5205 O  O    . HOH   T 6 .   ? 38.941  24.320  -2.383  1.00 26.22 ? 450 HOH   A O    1 
HETATM 5206 O  O    . HOH   T 6 .   ? 34.516  26.872  2.771   1.00 27.85 ? 451 HOH   A O    1 
HETATM 5207 O  O    . HOH   T 6 .   ? 55.064  11.903  20.542  1.00 46.11 ? 452 HOH   A O    1 
HETATM 5208 O  O    A HOH   T 6 .   ? 29.626  -12.086 16.111  0.50 18.69 ? 453 HOH   A O    1 
HETATM 5209 O  O    B HOH   T 6 .   ? 28.648  -12.363 16.684  0.50 23.09 ? 453 HOH   A O    1 
HETATM 5210 O  O    . HOH   T 6 .   ? 27.060  -8.869  22.451  1.00 26.38 ? 454 HOH   A O    1 
HETATM 5211 O  O    . HOH   T 6 .   ? 38.885  8.347   12.399  1.00 12.72 ? 455 HOH   A O    1 
HETATM 5212 O  O    . HOH   T 6 .   ? 20.050  -1.824  15.275  1.00 54.93 ? 456 HOH   A O    1 
HETATM 5213 O  O    . HOH   T 6 .   ? 36.697  -7.725  25.073  1.00 27.42 ? 457 HOH   A O    1 
HETATM 5214 O  O    . HOH   T 6 .   ? 47.356  4.806   6.155   1.00 24.19 ? 458 HOH   A O    1 
HETATM 5215 O  O    . HOH   T 6 .   ? 42.537  17.853  15.416  1.00 29.12 ? 459 HOH   A O    1 
HETATM 5216 O  O    . HOH   T 6 .   ? 44.693  -7.664  15.075  1.00 27.87 ? 460 HOH   A O    1 
HETATM 5217 O  O    . HOH   T 6 .   ? 34.006  15.899  -15.889 1.00 19.29 ? 461 HOH   A O    1 
HETATM 5218 O  O    . HOH   T 6 .   ? 33.024  24.291  5.814   1.00 12.38 ? 462 HOH   A O    1 
HETATM 5219 O  O    . HOH   T 6 .   ? 30.785  18.816  -5.677  1.00 29.51 ? 463 HOH   A O    1 
HETATM 5220 O  O    . HOH   T 6 .   ? 35.121  9.899   24.297  1.00 23.54 ? 464 HOH   A O    1 
HETATM 5221 O  O    . HOH   T 6 .   ? 44.274  15.534  -4.937  1.00 34.87 ? 465 HOH   A O    1 
HETATM 5222 O  O    A HOH   T 6 .   ? 23.212  16.893  0.881   0.50 32.63 ? 466 HOH   A O    1 
HETATM 5223 O  O    B HOH   T 6 .   ? 22.818  18.542  2.128   0.50 25.15 ? 466 HOH   A O    1 
HETATM 5224 O  O    . HOH   T 6 .   ? 23.708  -4.285  23.249  1.00 40.28 ? 467 HOH   A O    1 
HETATM 5225 O  O    . HOH   T 6 .   ? 28.531  10.086  -5.917  1.00 15.53 ? 468 HOH   A O    1 
HETATM 5226 O  O    . HOH   T 6 .   ? 40.791  -14.457 14.565  1.00 33.18 ? 469 HOH   A O    1 
HETATM 5227 O  O    . HOH   T 6 .   ? 37.115  27.969  -0.821  1.00 43.69 ? 470 HOH   A O    1 
HETATM 5228 O  O    . HOH   T 6 .   ? 49.421  26.754  2.325   1.00 32.14 ? 471 HOH   A O    1 
HETATM 5229 O  O    . HOH   T 6 .   ? 26.129  16.810  0.294   1.00 16.01 ? 472 HOH   A O    1 
HETATM 5230 O  O    . HOH   T 6 .   ? 41.886  -2.454  28.388  1.00 30.36 ? 473 HOH   A O    1 
HETATM 5231 O  O    . HOH   T 6 .   ? 20.713  12.712  13.477  1.00 36.01 ? 474 HOH   A O    1 
HETATM 5232 O  O    . HOH   T 6 .   ? 33.662  5.998   25.482  1.00 40.46 ? 475 HOH   A O    1 
HETATM 5233 O  O    . HOH   T 6 .   ? 22.274  -2.276  24.976  1.00 42.50 ? 476 HOH   A O    1 
HETATM 5234 O  O    . HOH   T 6 .   ? 31.585  -13.626 19.204  1.00 15.82 ? 477 HOH   A O    1 
HETATM 5235 O  O    . HOH   T 6 .   ? 40.199  15.634  21.897  1.00 36.26 ? 478 HOH   A O    1 
HETATM 5236 O  O    . HOH   T 6 .   ? 25.706  -10.915 16.501  1.00 43.44 ? 479 HOH   A O    1 
HETATM 5237 O  O    . HOH   T 6 .   ? 31.614  29.682  14.192  1.00 24.86 ? 480 HOH   A O    1 
HETATM 5238 O  O    . HOH   T 6 .   ? 27.926  16.371  2.287   1.00 15.65 ? 481 HOH   A O    1 
HETATM 5239 O  O    . HOH   T 6 .   ? 37.635  17.762  2.041   1.00 17.72 ? 482 HOH   A O    1 
HETATM 5240 O  O    . HOH   T 6 .   ? 22.524  15.528  4.464   1.00 22.47 ? 483 HOH   A O    1 
HETATM 5241 O  O    . HOH   T 6 .   ? 46.449  -9.102  11.415  1.00 46.06 ? 484 HOH   A O    1 
HETATM 5242 O  O    . HOH   T 6 .   ? 36.211  18.741  21.074  1.00 32.76 ? 485 HOH   A O    1 
HETATM 5243 O  O    . HOH   T 6 .   ? 41.143  8.815   28.209  1.00 42.84 ? 486 HOH   A O    1 
HETATM 5244 O  O    . HOH   T 6 .   ? 47.555  9.175   28.613  1.00 51.70 ? 487 HOH   A O    1 
HETATM 5245 O  O    . HOH   T 6 .   ? 34.406  -7.844  8.510   1.00 29.98 ? 488 HOH   A O    1 
HETATM 5246 O  O    . HOH   T 6 .   ? 18.422  3.677   -1.716  1.00 37.61 ? 489 HOH   A O    1 
HETATM 5247 O  O    . HOH   T 6 .   ? 35.117  25.584  4.809   1.00 23.56 ? 490 HOH   A O    1 
HETATM 5248 O  O    . HOH   T 6 .   ? 47.812  13.162  12.386  1.00 37.30 ? 491 HOH   A O    1 
HETATM 5249 O  O    . HOH   T 6 .   ? 28.887  21.890  17.034  1.00 44.65 ? 492 HOH   A O    1 
HETATM 5250 O  O    . HOH   T 6 .   ? 40.798  12.895  -12.466 1.00 37.49 ? 493 HOH   A O    1 
HETATM 5251 O  O    . HOH   T 6 .   ? 41.413  11.144  11.548  1.00 15.73 ? 494 HOH   A O    1 
HETATM 5252 O  O    . HOH   T 6 .   ? 43.634  5.846   -0.004  1.00 35.55 ? 495 HOH   A O    1 
HETATM 5253 O  O    . HOH   T 6 .   ? 21.459  -1.601  19.491  1.00 44.68 ? 496 HOH   A O    1 
HETATM 5254 O  O    . HOH   T 6 .   ? 39.634  -8.360  24.213  1.00 29.23 ? 497 HOH   A O    1 
HETATM 5255 O  O    . HOH   T 6 .   ? 45.839  -1.023  8.397   1.00 18.29 ? 498 HOH   A O    1 
HETATM 5256 O  O    . HOH   T 6 .   ? 23.695  -9.427  14.491  1.00 34.90 ? 499 HOH   A O    1 
HETATM 5257 O  O    . HOH   T 6 .   ? 36.205  23.663  -2.917  1.00 15.50 ? 500 HOH   A O    1 
HETATM 5258 O  O    A HOH   T 6 .   ? 24.142  18.631  6.735   0.50 31.88 ? 501 HOH   A O    1 
HETATM 5259 O  O    B HOH   T 6 .   ? 24.539  19.203  5.992   0.50 28.00 ? 501 HOH   A O    1 
HETATM 5260 O  O    . HOH   T 6 .   ? 18.439  9.553   -2.773  1.00 29.45 ? 502 HOH   A O    1 
HETATM 5261 O  O    . HOH   T 6 .   ? 26.902  15.070  21.992  1.00 41.46 ? 503 HOH   A O    1 
HETATM 5262 O  O    . HOH   T 6 .   ? 17.587  12.719  -0.239  1.00 34.26 ? 504 HOH   A O    1 
HETATM 5263 O  O    . HOH   T 6 .   ? 46.601  -6.441  24.256  1.00 28.29 ? 505 HOH   A O    1 
HETATM 5264 O  O    . HOH   T 6 .   ? 34.629  7.294   23.621  1.00 26.86 ? 506 HOH   A O    1 
HETATM 5265 O  O    . HOH   T 6 .   ? 44.257  24.707  -1.204  1.00 33.98 ? 507 HOH   A O    1 
HETATM 5266 O  O    . HOH   T 6 .   ? 23.629  15.217  -6.028  1.00 29.76 ? 508 HOH   A O    1 
HETATM 5267 O  O    . HOH   T 6 .   ? 44.797  8.929   -3.233  1.00 39.42 ? 509 HOH   A O    1 
HETATM 5268 O  O    . HOH   T 6 .   ? 46.132  -0.933  20.541  1.00 25.63 ? 510 HOH   A O    1 
HETATM 5269 O  O    . HOH   T 6 .   ? 45.636  22.613  5.993   1.00 29.58 ? 511 HOH   A O    1 
HETATM 5270 O  O    . HOH   T 6 .   ? 22.570  2.029   20.519  1.00 34.28 ? 512 HOH   A O    1 
HETATM 5271 O  O    . HOH   T 6 .   ? 35.572  24.171  -5.494  1.00 20.77 ? 513 HOH   A O    1 
HETATM 5272 O  O    . HOH   T 6 .   ? 34.416  -13.798 19.416  1.00 27.93 ? 514 HOH   A O    1 
HETATM 5273 O  O    A HOH   T 6 .   ? 41.986  -7.639  3.352   0.50 26.47 ? 515 HOH   A O    1 
HETATM 5274 O  O    B HOH   T 6 .   ? 42.903  -6.332  4.553   0.50 33.22 ? 515 HOH   A O    1 
HETATM 5275 O  O    . HOH   T 6 .   ? 40.792  -12.069 8.969   1.00 21.95 ? 516 HOH   A O    1 
HETATM 5276 O  O    . HOH   T 6 .   ? 44.111  -12.085 8.850   1.00 22.47 ? 517 HOH   A O    1 
HETATM 5277 O  O    . HOH   T 6 .   ? 42.581  16.639  20.268  1.00 33.88 ? 518 HOH   A O    1 
HETATM 5278 O  O    . HOH   T 6 .   ? 42.643  -2.986  3.641   1.00 44.87 ? 519 HOH   A O    1 
HETATM 5279 O  O    . HOH   T 6 .   ? 23.007  25.405  10.191  1.00 28.05 ? 520 HOH   A O    1 
HETATM 5280 O  O    . HOH   T 6 .   ? 24.600  18.880  0.553   1.00 46.56 ? 521 HOH   A O    1 
HETATM 5281 O  O    . HOH   T 6 .   ? 32.074  17.574  20.688  1.00 45.75 ? 522 HOH   A O    1 
HETATM 5282 O  O    . HOH   T 6 .   ? 45.693  -0.862  23.283  1.00 45.97 ? 523 HOH   A O    1 
HETATM 5283 O  O    . HOH   T 6 .   ? 44.967  4.286   1.753   1.00 40.01 ? 524 HOH   A O    1 
HETATM 5284 O  O    . HOH   T 6 .   ? 39.857  4.225   31.133  1.00 45.43 ? 525 HOH   A O    1 
HETATM 5285 O  O    . HOH   T 6 .   ? 26.157  18.912  -3.813  1.00 44.29 ? 526 HOH   A O    1 
HETATM 5286 O  O    . HOH   T 6 .   ? 41.558  8.226   11.819  1.00 16.91 ? 527 HOH   A O    1 
HETATM 5287 O  O    . HOH   T 6 .   ? 33.444  24.003  17.411  1.00 46.83 ? 528 HOH   A O    1 
HETATM 5288 O  O    . HOH   T 6 .   ? 50.935  -6.299  17.965  1.00 55.89 ? 529 HOH   A O    1 
HETATM 5289 O  O    . HOH   T 6 .   ? 43.822  12.468  11.104  1.00 31.77 ? 530 HOH   A O    1 
HETATM 5290 O  O    . HOH   T 6 .   ? 22.821  24.701  14.453  1.00 43.18 ? 531 HOH   A O    1 
HETATM 5291 O  O    . HOH   T 6 .   ? 43.841  -9.740  12.512  1.00 29.05 ? 532 HOH   A O    1 
HETATM 5292 O  O    . HOH   T 6 .   ? 46.293  -10.654 9.136   1.00 36.76 ? 533 HOH   A O    1 
HETATM 5293 O  O    . HOH   T 6 .   ? 30.819  14.708  -14.274 1.00 33.41 ? 534 HOH   A O    1 
HETATM 5294 O  O    . HOH   T 6 .   ? 47.267  -7.655  16.116  1.00 35.27 ? 535 HOH   A O    1 
HETATM 5295 O  O    A HOH   T 6 .   ? 35.095  29.317  16.558  0.50 15.99 ? 536 HOH   A O    1 
HETATM 5296 O  O    B HOH   T 6 .   ? 35.836  28.660  15.677  0.50 21.32 ? 536 HOH   A O    1 
HETATM 5297 O  O    . HOH   T 6 .   ? 17.309  1.360   4.534   1.00 45.84 ? 537 HOH   A O    1 
HETATM 5298 O  O    . HOH   T 6 .   ? 38.380  17.303  23.028  1.00 52.40 ? 538 HOH   A O    1 
HETATM 5299 O  O    . HOH   T 6 .   ? 24.826  -7.520  23.447  1.00 44.41 ? 539 HOH   A O    1 
HETATM 5300 O  O    . HOH   T 6 .   ? 43.073  8.629   30.081  1.00 42.73 ? 540 HOH   A O    1 
HETATM 5301 O  O    . HOH   T 6 .   ? 44.703  15.723  18.846  1.00 45.43 ? 541 HOH   A O    1 
HETATM 5302 O  O    . HOH   T 6 .   ? 22.905  -4.145  18.987  1.00 37.03 ? 542 HOH   A O    1 
HETATM 5303 O  O    . HOH   T 6 .   ? 32.825  28.744  3.530   1.00 36.53 ? 543 HOH   A O    1 
HETATM 5304 O  O    . HOH   T 6 .   ? 30.973  23.888  16.357  1.00 45.56 ? 544 HOH   A O    1 
HETATM 5305 O  O    . HOH   T 6 .   ? 31.590  28.662  16.743  1.00 38.05 ? 545 HOH   A O    1 
HETATM 5306 O  O    . HOH   T 6 .   ? 21.277  17.253  2.943   1.00 37.35 ? 546 HOH   A O    1 
HETATM 5307 O  O    . HOH   T 6 .   ? 16.781  7.441   -2.971  1.00 53.41 ? 547 HOH   A O    1 
HETATM 5308 O  O    . HOH   T 6 .   ? 48.252  10.227  9.989   1.00 43.47 ? 548 HOH   A O    1 
HETATM 5309 O  O    . HOH   T 6 .   ? 48.102  2.302   6.967   1.00 33.23 ? 549 HOH   A O    1 
HETATM 5310 O  O    . HOH   T 6 .   ? 19.214  15.234  -0.485  1.00 54.87 ? 550 HOH   A O    1 
HETATM 5311 O  O    . HOH   T 6 .   ? 24.248  19.927  -1.891  1.00 44.40 ? 551 HOH   A O    1 
HETATM 5312 O  O    . HOH   T 6 .   ? 45.000  22.427  -2.595  1.00 45.97 ? 552 HOH   A O    1 
HETATM 5313 O  O    . HOH   T 6 .   ? 31.317  -15.088 16.698  1.00 25.30 ? 553 HOH   A O    1 
HETATM 5314 O  O    . HOH   T 6 .   ? 39.743  -10.452 25.369  1.00 45.90 ? 554 HOH   A O    1 
HETATM 5315 O  O    . HOH   T 6 .   ? 15.811  15.981  2.458   1.00 56.39 ? 555 HOH   A O    1 
HETATM 5316 O  O    . HOH   T 6 .   ? 35.792  15.929  21.933  1.00 33.21 ? 556 HOH   A O    1 
HETATM 5317 O  O    . HOH   T 6 .   ? 47.131  3.933   3.359   1.00 33.25 ? 557 HOH   A O    1 
HETATM 5318 O  O    . HOH   T 6 .   ? 27.650  28.547  7.224   1.00 36.33 ? 558 HOH   A O    1 
HETATM 5319 O  O    . HOH   T 6 .   ? 32.089  24.640  -5.798  1.00 28.73 ? 559 HOH   A O    1 
HETATM 5320 O  O    . HOH   T 6 .   ? 29.986  13.572  22.535  1.00 46.85 ? 560 HOH   A O    1 
HETATM 5321 O  O    . HOH   T 6 .   ? 41.132  15.832  -10.785 1.00 43.93 ? 561 HOH   A O    1 
HETATM 5322 O  O    . HOH   T 6 .   ? 16.819  11.685  -2.652  1.00 42.01 ? 562 HOH   A O    1 
HETATM 5323 O  O    . HOH   T 6 .   ? 34.338  10.197  26.840  1.00 41.25 ? 563 HOH   A O    1 
HETATM 5324 O  O    . HOH   T 6 .   ? 42.536  11.633  -11.220 1.00 28.41 ? 564 HOH   A O    1 
HETATM 5325 O  O    . HOH   T 6 .   ? 30.540  -7.863  34.476  1.00 31.66 ? 565 HOH   A O    1 
HETATM 5326 O  O    . HOH   T 6 .   ? 50.849  -0.646  6.807   1.00 48.20 ? 566 HOH   A O    1 
HETATM 5327 O  O    . HOH   T 6 .   ? 29.637  19.318  17.352  1.00 30.69 ? 567 HOH   A O    1 
HETATM 5328 O  O    . HOH   T 6 .   ? 27.448  25.698  13.076  1.00 45.03 ? 568 HOH   A O    1 
HETATM 5329 O  O    . HOH   T 6 .   ? 36.621  20.139  23.289  1.00 46.65 ? 569 HOH   A O    1 
HETATM 5330 O  O    . HOH   T 6 .   ? 21.415  1.540   22.857  1.00 46.27 ? 570 HOH   A O    1 
HETATM 5331 O  O    . HOH   T 6 .   ? 40.289  11.297  27.842  1.00 49.57 ? 571 HOH   A O    1 
HETATM 5332 O  O    . HOH   T 6 .   ? 19.247  -0.420  13.133  1.00 52.18 ? 572 HOH   A O    1 
HETATM 5333 O  O    . HOH   T 6 .   ? 41.603  14.737  -8.350  1.00 27.53 ? 573 HOH   A O    1 
HETATM 5334 O  O    . HOH   T 6 .   ? 24.973  26.197  12.058  1.00 34.31 ? 574 HOH   A O    1 
HETATM 5335 O  O    . HOH   T 6 .   ? 45.879  -13.830 4.025   1.00 42.96 ? 575 HOH   A O    1 
HETATM 5336 O  O    . HOH   T 6 .   ? 33.696  19.420  20.336  1.00 40.75 ? 576 HOH   A O    1 
HETATM 5337 O  O    . HOH   T 6 .   ? 44.238  14.685  -7.597  1.00 33.83 ? 577 HOH   A O    1 
HETATM 5338 O  O    . HOH   T 6 .   ? 47.024  -1.188  5.875   1.00 28.71 ? 578 HOH   A O    1 
HETATM 5339 O  O    . HOH   T 6 .   ? 45.720  -2.206  3.685   1.00 36.65 ? 579 HOH   A O    1 
HETATM 5340 O  O    . HOH   T 6 .   ? 48.847  25.720  11.695  1.00 37.15 ? 580 HOH   A O    1 
HETATM 5341 O  O    . HOH   U 6 .   ? 10.950  -17.305 41.561  1.00 40.46 ? 401 HOH   B O    1 
HETATM 5342 O  O    . HOH   U 6 .   ? 2.520   -36.978 39.464  1.00 32.68 ? 402 HOH   B O    1 
HETATM 5343 O  O    . HOH   U 6 .   ? 23.500  -33.298 21.772  1.00 42.26 ? 403 HOH   B O    1 
HETATM 5344 O  O    . HOH   U 6 .   ? 22.193  -49.210 31.703  1.00 47.55 ? 404 HOH   B O    1 
HETATM 5345 O  O    . HOH   U 6 .   ? 6.576   -33.322 25.353  1.00 13.56 ? 405 HOH   B O    1 
HETATM 5346 O  O    . HOH   U 6 .   ? 31.287  -28.010 31.881  1.00 42.08 ? 406 HOH   B O    1 
HETATM 5347 O  O    . HOH   U 6 .   ? 33.913  -26.784 39.766  1.00 28.53 ? 407 HOH   B O    1 
HETATM 5348 O  O    . HOH   U 6 .   ? 34.209  -27.580 18.269  1.00 36.87 ? 408 HOH   B O    1 
HETATM 5349 O  O    . HOH   U 6 .   ? 20.756  -43.399 33.611  1.00 21.44 ? 409 HOH   B O    1 
HETATM 5350 O  O    . HOH   U 6 .   ? 17.468  -18.031 18.249  1.00 20.34 ? 410 HOH   B O    1 
HETATM 5351 O  O    . HOH   U 6 .   ? 19.568  -12.916 17.026  1.00 48.89 ? 411 HOH   B O    1 
HETATM 5352 O  O    . HOH   U 6 .   ? 27.926  -9.850  24.916  1.00 21.85 ? 412 HOH   B O    1 
HETATM 5353 O  O    . HOH   U 6 .   ? 5.893   -20.888 35.726  1.00 48.79 ? 413 HOH   B O    1 
HETATM 5354 O  O    . HOH   U 6 .   ? 30.613  -12.673 36.174  1.00 28.52 ? 414 HOH   B O    1 
HETATM 5355 O  O    . HOH   U 6 .   ? 8.823   -28.066 47.569  1.00 24.54 ? 415 HOH   B O    1 
HETATM 5356 O  O    . HOH   U 6 .   ? 5.538   -21.680 40.566  1.00 41.03 ? 416 HOH   B O    1 
HETATM 5357 O  O    . HOH   U 6 .   ? 26.889  -27.841 36.157  1.00 15.57 ? 417 HOH   B O    1 
HETATM 5358 O  O    . HOH   U 6 .   ? 23.212  -18.816 42.744  1.00 34.80 ? 418 HOH   B O    1 
HETATM 5359 O  O    . HOH   U 6 .   ? 21.821  -19.852 12.013  1.00 34.73 ? 419 HOH   B O    1 
HETATM 5360 O  O    . HOH   U 6 .   ? 15.601  -42.180 27.586  1.00 44.20 ? 420 HOH   B O    1 
HETATM 5361 O  O    . HOH   U 6 .   ? 19.410  -23.911 44.188  1.00 25.81 ? 421 HOH   B O    1 
HETATM 5362 O  O    . HOH   U 6 .   ? 26.039  -12.423 23.135  1.00 35.10 ? 422 HOH   B O    1 
HETATM 5363 O  O    . HOH   U 6 .   ? 29.115  -28.731 32.774  1.00 19.57 ? 423 HOH   B O    1 
HETATM 5364 O  O    . HOH   U 6 .   ? 27.162  -24.388 43.446  1.00 23.68 ? 424 HOH   B O    1 
HETATM 5365 O  O    . HOH   U 6 .   ? 23.731  -15.800 41.941  1.00 40.66 ? 425 HOH   B O    1 
HETATM 5366 O  O    . HOH   U 6 .   ? 26.063  -10.349 27.221  1.00 37.29 ? 426 HOH   B O    1 
HETATM 5367 O  O    . HOH   U 6 .   ? 24.595  -22.282 47.177  1.00 42.62 ? 427 HOH   B O    1 
HETATM 5368 O  O    . HOH   U 6 .   ? 30.486  -21.460 44.871  1.00 40.44 ? 428 HOH   B O    1 
HETATM 5369 O  O    . HOH   U 6 .   ? 37.539  -14.834 26.339  1.00 36.83 ? 429 HOH   B O    1 
HETATM 5370 O  O    . HOH   U 6 .   ? 23.865  -38.576 24.117  1.00 40.03 ? 430 HOH   B O    1 
HETATM 5371 O  O    . HOH   U 6 .   ? 22.558  -9.746  32.981  1.00 35.29 ? 431 HOH   B O    1 
HETATM 5372 O  O    . HOH   U 6 .   ? 16.554  -14.835 16.260  1.00 39.03 ? 432 HOH   B O    1 
HETATM 5373 O  O    A HOH   U 6 .   ? 10.128  -39.429 32.955  0.50 19.24 ? 433 HOH   B O    1 
HETATM 5374 O  O    B HOH   U 6 .   ? 9.133   -38.218 32.006  0.50 17.44 ? 433 HOH   B O    1 
HETATM 5375 O  O    . HOH   U 6 .   ? 9.054   -20.174 41.963  1.00 30.76 ? 434 HOH   B O    1 
HETATM 5376 O  O    . HOH   U 6 .   ? 7.521   -19.498 24.215  1.00 34.15 ? 435 HOH   B O    1 
HETATM 5377 O  O    . HOH   U 6 .   ? 26.335  -30.302 20.636  1.00 34.82 ? 436 HOH   B O    1 
HETATM 5378 O  O    . HOH   U 6 .   ? 39.081  -20.934 22.184  1.00 24.51 ? 437 HOH   B O    1 
HETATM 5379 O  O    . HOH   U 6 .   ? 27.692  -26.411 33.856  1.00 13.68 ? 438 HOH   B O    1 
HETATM 5380 O  O    . HOH   U 6 .   ? 25.318  -31.481 24.365  1.00 20.51 ? 439 HOH   B O    1 
HETATM 5381 O  O    . HOH   U 6 .   ? 3.163   -26.752 31.698  1.00 30.91 ? 440 HOH   B O    1 
HETATM 5382 O  O    . HOH   U 6 .   ? 38.857  -22.592 17.065  1.00 31.38 ? 441 HOH   B O    1 
HETATM 5383 O  O    . HOH   U 6 .   ? 30.980  -22.957 7.623   1.00 21.59 ? 442 HOH   B O    1 
HETATM 5384 O  O    . HOH   U 6 .   ? 25.415  -42.859 32.568  1.00 27.19 ? 443 HOH   B O    1 
HETATM 5385 O  O    . HOH   U 6 .   ? 29.227  -45.890 32.683  1.00 43.55 ? 444 HOH   B O    1 
HETATM 5386 O  O    . HOH   U 6 .   ? 22.634  -18.925 45.262  1.00 48.35 ? 445 HOH   B O    1 
HETATM 5387 O  O    . HOH   U 6 .   ? 30.024  -36.304 32.477  1.00 33.90 ? 446 HOH   B O    1 
HETATM 5388 O  O    . HOH   U 6 .   ? 25.167  -13.433 25.477  1.00 29.04 ? 447 HOH   B O    1 
HETATM 5389 O  O    . HOH   U 6 .   ? 43.963  -30.171 27.662  1.00 45.81 ? 448 HOH   B O    1 
HETATM 5390 O  O    . HOH   U 6 .   ? 29.310  -39.350 46.887  1.00 44.34 ? 449 HOH   B O    1 
HETATM 5391 O  O    . HOH   U 6 .   ? 24.565  -29.891 35.665  1.00 13.46 ? 450 HOH   B O    1 
HETATM 5392 O  O    . HOH   U 6 .   ? 17.028  -12.952 34.867  1.00 36.02 ? 451 HOH   B O    1 
HETATM 5393 O  O    . HOH   U 6 .   ? 26.877  -35.664 23.870  1.00 36.34 ? 452 HOH   B O    1 
HETATM 5394 O  O    . HOH   U 6 .   ? 4.801   -42.614 40.770  1.00 31.80 ? 453 HOH   B O    1 
HETATM 5395 O  O    A HOH   U 6 .   ? 24.006  -29.058 21.724  0.50 16.43 ? 454 HOH   B O    1 
HETATM 5396 O  O    B HOH   U 6 .   ? 24.024  -30.587 21.378  0.50 28.43 ? 454 HOH   B O    1 
HETATM 5397 O  O    . HOH   U 6 .   ? 28.656  -17.701 40.550  1.00 30.62 ? 455 HOH   B O    1 
HETATM 5398 O  O    . HOH   U 6 .   ? 34.494  -15.953 29.540  1.00 13.80 ? 456 HOH   B O    1 
HETATM 5399 O  O    . HOH   U 6 .   ? 22.392  -25.469 47.162  1.00 26.18 ? 457 HOH   B O    1 
HETATM 5400 O  O    . HOH   U 6 .   ? 26.408  -27.185 48.715  1.00 47.14 ? 458 HOH   B O    1 
HETATM 5401 O  O    . HOH   U 6 .   ? 37.482  -32.339 42.425  1.00 42.35 ? 459 HOH   B O    1 
HETATM 5402 O  O    . HOH   U 6 .   ? 30.030  -34.661 29.248  1.00 35.44 ? 460 HOH   B O    1 
HETATM 5403 O  O    . HOH   U 6 .   ? 35.659  -41.367 42.740  1.00 42.26 ? 461 HOH   B O    1 
HETATM 5404 O  O    . HOH   U 6 .   ? 7.300   -34.235 33.368  1.00 28.99 ? 462 HOH   B O    1 
HETATM 5405 O  O    . HOH   U 6 .   ? 7.132   -24.243 37.853  1.00 20.63 ? 463 HOH   B O    1 
HETATM 5406 O  O    . HOH   U 6 .   ? 4.255   -32.829 26.859  1.00 12.76 ? 464 HOH   B O    1 
HETATM 5407 O  O    . HOH   U 6 .   ? 20.289  -22.816 46.643  1.00 45.74 ? 465 HOH   B O    1 
HETATM 5408 O  O    . HOH   U 6 .   ? 28.834  -7.053  32.465  1.00 26.10 ? 466 HOH   B O    1 
HETATM 5409 O  O    . HOH   U 6 .   ? 15.508  -46.528 28.603  1.00 44.33 ? 467 HOH   B O    1 
HETATM 5410 O  O    . HOH   U 6 .   ? 8.021   -19.209 35.528  1.00 55.14 ? 468 HOH   B O    1 
HETATM 5411 O  O    . HOH   U 6 .   ? 28.147  -17.655 15.199  1.00 33.14 ? 469 HOH   B O    1 
HETATM 5412 O  O    . HOH   U 6 .   ? 14.813  -43.899 38.102  1.00 29.21 ? 470 HOH   B O    1 
HETATM 5413 O  O    . HOH   U 6 .   ? 8.272   -35.786 48.566  1.00 28.97 ? 471 HOH   B O    1 
HETATM 5414 O  O    . HOH   U 6 .   ? 25.148  -15.322 22.807  1.00 16.15 ? 472 HOH   B O    1 
HETATM 5415 O  O    . HOH   U 6 .   ? 24.588  -30.601 51.577  1.00 38.85 ? 473 HOH   B O    1 
HETATM 5416 O  O    . HOH   U 6 .   ? 8.598   -36.988 27.785  1.00 22.29 ? 474 HOH   B O    1 
HETATM 5417 O  O    . HOH   U 6 .   ? 21.486  -12.957 26.497  1.00 23.92 ? 475 HOH   B O    1 
HETATM 5418 O  O    A HOH   U 6 .   ? 13.584  -15.780 37.200  0.50 28.07 ? 476 HOH   B O    1 
HETATM 5419 O  O    B HOH   U 6 .   ? 14.087  -15.677 34.992  0.50 27.28 ? 476 HOH   B O    1 
HETATM 5420 O  O    . HOH   U 6 .   ? 36.232  -40.696 45.206  1.00 48.04 ? 477 HOH   B O    1 
HETATM 5421 O  O    . HOH   U 6 .   ? 32.555  -23.770 25.894  1.00 16.86 ? 478 HOH   B O    1 
HETATM 5422 O  O    . HOH   U 6 .   ? 1.922   -34.501 36.752  1.00 43.93 ? 479 HOH   B O    1 
HETATM 5423 O  O    . HOH   U 6 .   ? 27.414  -39.187 30.035  1.00 24.57 ? 480 HOH   B O    1 
HETATM 5424 O  O    . HOH   U 6 .   ? 25.587  -16.863 24.976  1.00 15.09 ? 481 HOH   B O    1 
HETATM 5425 O  O    . HOH   U 6 .   ? 30.184  -18.050 17.447  1.00 26.30 ? 482 HOH   B O    1 
HETATM 5426 O  O    . HOH   U 6 .   ? 27.583  -6.945  36.742  1.00 35.13 ? 483 HOH   B O    1 
HETATM 5427 O  O    . HOH   U 6 .   ? 21.710  -15.845 44.183  1.00 41.93 ? 484 HOH   B O    1 
HETATM 5428 O  O    . HOH   U 6 .   ? 15.722  -37.882 51.222  1.00 35.17 ? 485 HOH   B O    1 
HETATM 5429 O  O    . HOH   U 6 .   ? 1.467   -29.973 40.564  1.00 23.97 ? 486 HOH   B O    1 
HETATM 5430 O  O    . HOH   U 6 .   ? 20.493  -41.058 43.847  1.00 25.36 ? 487 HOH   B O    1 
HETATM 5431 O  O    . HOH   U 6 .   ? 35.591  -30.860 19.533  1.00 31.11 ? 488 HOH   B O    1 
HETATM 5432 O  O    A HOH   U 6 .   ? 19.291  -40.321 26.271  0.50 31.04 ? 489 HOH   B O    1 
HETATM 5433 O  O    B HOH   U 6 .   ? 17.916  -39.556 26.988  0.50 35.01 ? 489 HOH   B O    1 
HETATM 5434 O  O    . HOH   U 6 .   ? 14.097  -42.067 25.883  1.00 47.36 ? 490 HOH   B O    1 
HETATM 5435 O  O    . HOH   U 6 .   ? 25.407  -12.223 28.374  1.00 38.86 ? 491 HOH   B O    1 
HETATM 5436 O  O    . HOH   U 6 .   ? 33.635  -34.288 36.648  1.00 35.97 ? 492 HOH   B O    1 
HETATM 5437 O  O    . HOH   U 6 .   ? 10.454  -16.829 18.876  1.00 32.58 ? 493 HOH   B O    1 
HETATM 5438 O  O    . HOH   U 6 .   ? 36.930  -19.320 21.189  1.00 13.77 ? 494 HOH   B O    1 
HETATM 5439 O  O    . HOH   U 6 .   ? 14.889  -46.322 34.378  1.00 46.34 ? 495 HOH   B O    1 
HETATM 5440 O  O    . HOH   U 6 .   ? 29.993  -26.748 45.712  1.00 37.54 ? 496 HOH   B O    1 
HETATM 5441 O  O    . HOH   U 6 .   ? 21.543  -41.266 31.834  1.00 19.26 ? 497 HOH   B O    1 
HETATM 5442 O  O    . HOH   U 6 .   ? 40.866  -27.321 30.270  1.00 31.91 ? 498 HOH   B O    1 
HETATM 5443 O  O    . HOH   U 6 .   ? 28.367  -30.257 35.271  1.00 16.13 ? 499 HOH   B O    1 
HETATM 5444 O  O    . HOH   U 6 .   ? 38.711  -14.154 35.128  0.50 21.03 ? 500 HOH   B O    1 
HETATM 5445 O  O    . HOH   U 6 .   ? 30.920  -31.441 35.052  1.00 37.10 ? 501 HOH   B O    1 
HETATM 5446 O  O    A HOH   U 6 .   ? 9.164   -34.811 31.339  0.50 19.46 ? 502 HOH   B O    1 
HETATM 5447 O  O    B HOH   U 6 .   ? 9.323   -36.080 30.394  0.50 23.79 ? 502 HOH   B O    1 
HETATM 5448 O  O    . HOH   U 6 .   ? 19.988  -26.429 46.187  1.00 27.90 ? 503 HOH   B O    1 
HETATM 5449 O  O    . HOH   U 6 .   ? 23.082  -14.594 16.204  1.00 31.79 ? 504 HOH   B O    1 
HETATM 5450 O  O    . HOH   U 6 .   ? 33.977  -31.212 45.005  1.00 48.93 ? 505 HOH   B O    1 
HETATM 5451 O  O    . HOH   U 6 .   ? 3.230   -38.068 42.507  1.00 29.26 ? 506 HOH   B O    1 
HETATM 5452 O  O    . HOH   U 6 .   ? 9.393   -43.602 31.368  1.00 24.76 ? 507 HOH   B O    1 
HETATM 5453 O  O    . HOH   U 6 .   ? 1.353   -27.587 34.575  1.00 38.79 ? 508 HOH   B O    1 
HETATM 5454 O  O    . HOH   U 6 .   ? 10.103  -34.481 50.693  1.00 37.34 ? 509 HOH   B O    1 
HETATM 5455 O  O    . HOH   U 6 .   ? 11.294  -46.208 31.722  1.00 25.11 ? 510 HOH   B O    1 
HETATM 5456 O  O    . HOH   U 6 .   ? 37.265  -18.554 18.595  1.00 20.35 ? 511 HOH   B O    1 
HETATM 5457 O  O    . HOH   U 6 .   ? 32.287  -30.148 11.636  1.00 38.89 ? 512 HOH   B O    1 
HETATM 5458 O  O    . HOH   U 6 .   ? 16.999  -10.917 20.914  1.00 29.50 ? 513 HOH   B O    1 
HETATM 5459 O  O    . HOH   U 6 .   ? 10.215  -40.190 46.419  1.00 30.51 ? 514 HOH   B O    1 
HETATM 5460 O  O    . HOH   U 6 .   ? 17.700  -25.138 46.125  1.00 42.77 ? 515 HOH   B O    1 
HETATM 5461 O  O    . HOH   U 6 .   ? 25.372  -50.557 32.821  1.00 52.94 ? 516 HOH   B O    1 
HETATM 5462 O  O    . HOH   U 6 .   ? 31.779  -29.426 40.013  1.00 29.71 ? 517 HOH   B O    1 
HETATM 5463 O  O    . HOH   U 6 .   ? 15.306  -13.588 18.332  1.00 28.20 ? 518 HOH   B O    1 
HETATM 5464 O  O    . HOH   U 6 .   ? 30.652  -35.081 20.869  1.00 39.97 ? 519 HOH   B O    1 
HETATM 5465 O  O    . HOH   U 6 .   ? 16.324  -45.849 39.238  1.00 31.81 ? 520 HOH   B O    1 
HETATM 5466 O  O    . HOH   U 6 .   ? 32.719  -25.267 18.716  1.00 28.78 ? 521 HOH   B O    1 
HETATM 5467 O  O    A HOH   U 6 .   ? 2.750   -30.720 42.676  0.50 18.67 ? 522 HOH   B O    1 
HETATM 5468 O  O    B HOH   U 6 .   ? 2.872   -29.538 43.238  0.50 18.47 ? 522 HOH   B O    1 
HETATM 5469 O  O    . HOH   U 6 .   ? 15.952  -44.378 47.356  1.00 29.94 ? 523 HOH   B O    1 
HETATM 5470 O  O    . HOH   U 6 .   ? 28.342  -17.417 11.404  1.00 34.99 ? 524 HOH   B O    1 
HETATM 5471 O  O    . HOH   U 6 .   ? 35.657  -17.733 38.717  1.00 21.52 ? 525 HOH   B O    1 
HETATM 5472 O  O    . HOH   U 6 .   ? 30.218  -23.826 46.802  1.00 58.89 ? 526 HOH   B O    1 
HETATM 5473 O  O    . HOH   U 6 .   ? 9.026   -42.815 46.271  1.00 45.13 ? 527 HOH   B O    1 
HETATM 5474 O  O    . HOH   U 6 .   ? 26.106  -32.157 35.377  1.00 17.19 ? 528 HOH   B O    1 
HETATM 5475 O  O    . HOH   U 6 .   ? 31.664  -31.387 38.227  1.00 23.11 ? 529 HOH   B O    1 
HETATM 5476 O  O    . HOH   U 6 .   ? 13.873  -47.136 32.282  1.00 37.92 ? 530 HOH   B O    1 
HETATM 5477 O  O    . HOH   U 6 .   ? 12.819  -44.471 35.327  1.00 31.07 ? 531 HOH   B O    1 
HETATM 5478 O  O    . HOH   U 6 .   ? 36.756  -16.335 28.301  1.00 38.73 ? 532 HOH   B O    1 
HETATM 5479 O  O    . HOH   U 6 .   ? 29.973  -48.411 34.359  1.00 48.62 ? 533 HOH   B O    1 
HETATM 5480 O  O    . HOH   U 6 .   ? 26.441  -15.507 15.621  1.00 49.94 ? 534 HOH   B O    1 
HETATM 5481 O  O    . HOH   U 6 .   ? 34.975  -32.712 21.313  1.00 45.27 ? 535 HOH   B O    1 
HETATM 5482 O  O    . HOH   U 6 .   ? 26.063  -37.663 25.434  1.00 35.82 ? 536 HOH   B O    1 
HETATM 5483 O  O    . HOH   U 6 .   ? 39.018  -12.085 37.281  1.00 40.99 ? 537 HOH   B O    1 
HETATM 5484 O  O    . HOH   U 6 .   ? 25.806  -41.191 30.649  1.00 32.54 ? 538 HOH   B O    1 
HETATM 5485 O  O    . HOH   U 6 .   ? 40.107  -15.652 26.166  1.00 44.36 ? 539 HOH   B O    1 
HETATM 5486 O  O    . HOH   U 6 .   ? 26.960  -39.485 27.329  1.00 36.41 ? 540 HOH   B O    1 
HETATM 5487 O  O    . HOH   U 6 .   ? 41.374  -30.047 29.616  1.00 39.26 ? 541 HOH   B O    1 
HETATM 5488 O  O    . HOH   U 6 .   ? 27.619  -22.595 45.397  1.00 33.71 ? 542 HOH   B O    1 
HETATM 5489 O  O    . HOH   U 6 .   ? 35.774  -15.681 17.947  1.00 29.14 ? 543 HOH   B O    1 
HETATM 5490 O  O    . HOH   U 6 .   ? 33.125  -29.710 33.589  1.00 48.14 ? 544 HOH   B O    1 
HETATM 5491 O  O    . HOH   U 6 .   ? 4.067   -30.317 51.718  1.00 37.32 ? 545 HOH   B O    1 
HETATM 5492 O  O    . HOH   U 6 .   ? 24.792  -44.963 30.771  1.00 48.18 ? 546 HOH   B O    1 
HETATM 5493 O  O    . HOH   U 6 .   ? 34.679  -28.444 13.421  1.00 44.38 ? 547 HOH   B O    1 
HETATM 5494 O  O    . HOH   U 6 .   ? 7.529   -19.674 44.105  1.00 52.52 ? 548 HOH   B O    1 
HETATM 5495 O  O    . HOH   U 6 .   ? 39.595  -19.835 17.768  1.00 42.00 ? 549 HOH   B O    1 
HETATM 5496 O  O    . HOH   U 6 .   ? 27.039  -15.546 40.380  1.00 31.95 ? 550 HOH   B O    1 
HETATM 5497 O  O    . HOH   U 6 .   ? 31.363  -10.125 35.960  1.00 40.43 ? 551 HOH   B O    1 
HETATM 5498 O  O    . HOH   U 6 .   ? 32.080  -32.278 12.902  1.00 26.97 ? 552 HOH   B O    1 
HETATM 5499 O  O    . HOH   U 6 .   ? 10.577  -44.522 33.961  1.00 27.34 ? 553 HOH   B O    1 
HETATM 5500 O  O    . HOH   U 6 .   ? 33.661  -29.430 15.877  1.00 27.71 ? 554 HOH   B O    1 
HETATM 5501 O  O    . HOH   U 6 .   ? 26.507  -28.735 51.004  1.00 49.52 ? 555 HOH   B O    1 
HETATM 5502 O  O    . HOH   U 6 .   ? 22.468  -42.381 29.558  1.00 28.87 ? 556 HOH   B O    1 
HETATM 5503 O  O    . HOH   U 6 .   ? 30.798  -17.234 41.829  1.00 41.65 ? 557 HOH   B O    1 
HETATM 5504 O  O    . HOH   U 6 .   ? 41.092  -26.728 33.100  1.00 42.23 ? 558 HOH   B O    1 
HETATM 5505 O  O    . HOH   U 6 .   ? 21.047  -42.129 27.066  1.00 37.65 ? 559 HOH   B O    1 
HETATM 5506 O  O    . HOH   U 6 .   ? 24.843  -42.160 28.687  1.00 43.47 ? 560 HOH   B O    1 
HETATM 5507 O  O    . HOH   U 6 .   ? 25.553  -41.621 26.409  1.00 58.72 ? 561 HOH   B O    1 
HETATM 5508 O  O    . HOH   V 6 .   ? 4.748   -56.633 17.386  1.00 38.78 ? 401 HOH   C O    1 
HETATM 5509 O  O    . HOH   V 6 .   ? -3.412  -39.207 24.541  1.00 33.79 ? 402 HOH   C O    1 
HETATM 5510 O  O    . HOH   V 6 .   ? -3.585  -23.615 15.353  1.00 38.27 ? 403 HOH   C O    1 
HETATM 5511 O  O    . HOH   V 6 .   ? 7.697   -26.036 -0.219  1.00 44.63 ? 404 HOH   C O    1 
HETATM 5512 O  O    . HOH   V 6 .   ? 31.075  -29.058 -1.565  1.00 33.06 ? 405 HOH   C O    1 
HETATM 5513 O  O    . HOH   V 6 .   ? 9.460   -43.586 1.658   1.00 26.54 ? 406 HOH   C O    1 
HETATM 5514 O  O    . HOH   V 6 .   ? 15.872  -38.664 24.438  1.00 43.24 ? 407 HOH   C O    1 
HETATM 5515 O  O    . HOH   V 6 .   ? 11.819  -47.057 16.470  1.00 29.19 ? 408 HOH   C O    1 
HETATM 5516 O  O    . HOH   V 6 .   ? 27.022  -30.792 -2.136  1.00 36.00 ? 409 HOH   C O    1 
HETATM 5517 O  O    . HOH   V 6 .   ? 21.344  -23.546 18.379  1.00 13.88 ? 410 HOH   C O    1 
HETATM 5518 O  O    . HOH   V 6 .   ? 32.482  -27.553 4.803   1.00 29.57 ? 411 HOH   C O    1 
HETATM 5519 O  O    . HOH   V 6 .   ? -0.414  -26.381 25.000  1.00 30.11 ? 412 HOH   C O    1 
HETATM 5520 O  O    . HOH   V 6 .   ? -2.854  -35.229 16.494  1.00 30.94 ? 413 HOH   C O    1 
HETATM 5521 O  O    . HOH   V 6 .   ? 0.386   -49.207 28.881  1.00 37.26 ? 414 HOH   C O    1 
HETATM 5522 O  O    . HOH   V 6 .   ? -3.798  -42.137 6.640   1.00 29.98 ? 415 HOH   C O    1 
HETATM 5523 O  O    . HOH   V 6 .   ? 2.863   -33.174 -4.382  1.00 50.06 ? 416 HOH   C O    1 
HETATM 5524 O  O    . HOH   V 6 .   ? 2.483   -31.383 30.346  1.00 30.04 ? 417 HOH   C O    1 
HETATM 5525 O  O    . HOH   V 6 .   ? 5.235   -38.185 1.021   1.00 31.15 ? 418 HOH   C O    1 
HETATM 5526 O  O    . HOH   V 6 .   ? 27.580  -41.282 14.317  1.00 22.96 ? 419 HOH   C O    1 
HETATM 5527 O  O    . HOH   V 6 .   ? 21.178  -23.965 -7.812  1.00 37.62 ? 420 HOH   C O    1 
HETATM 5528 O  O    . HOH   V 6 .   ? 4.158   -26.991 6.284   1.00 48.78 ? 421 HOH   C O    1 
HETATM 5529 O  O    . HOH   V 6 .   ? 11.293  -44.733 13.332  1.00 16.57 ? 422 HOH   C O    1 
HETATM 5530 O  O    . HOH   V 6 .   ? 11.580  -43.053 9.571   1.00 14.91 ? 423 HOH   C O    1 
HETATM 5531 O  O    . HOH   V 6 .   ? -0.716  -49.894 23.288  1.00 28.68 ? 424 HOH   C O    1 
HETATM 5532 O  O    . HOH   V 6 .   ? 11.573  -38.050 23.537  1.00 22.66 ? 425 HOH   C O    1 
HETATM 5533 O  O    . HOH   V 6 .   ? 25.572  -51.015 18.181  1.00 45.88 ? 426 HOH   C O    1 
HETATM 5534 O  O    . HOH   V 6 .   ? 27.249  -49.770 16.555  1.00 40.37 ? 427 HOH   C O    1 
HETATM 5535 O  O    . HOH   V 6 .   ? 9.712   -42.885 11.689  1.00 13.52 ? 428 HOH   C O    1 
HETATM 5536 O  O    . HOH   V 6 .   ? 20.627  -41.051 23.056  1.00 43.48 ? 429 HOH   C O    1 
HETATM 5537 O  O    . HOH   V 6 .   ? 30.286  -38.715 -4.978  1.00 46.49 ? 430 HOH   C O    1 
HETATM 5538 O  O    . HOH   V 6 .   ? 25.544  -45.418 15.835  1.00 24.46 ? 431 HOH   C O    1 
HETATM 5539 O  O    . HOH   V 6 .   ? 28.369  -26.139 -6.125  1.00 22.73 ? 432 HOH   C O    1 
HETATM 5540 O  O    . HOH   V 6 .   ? 12.184  -52.028 19.648  1.00 44.31 ? 433 HOH   C O    1 
HETATM 5541 O  O    . HOH   V 6 .   ? 2.279   -42.882 3.549   1.00 24.90 ? 434 HOH   C O    1 
HETATM 5542 O  O    . HOH   V 6 .   ? 17.113  -42.781 23.107  1.00 33.39 ? 435 HOH   C O    1 
HETATM 5543 O  O    . HOH   V 6 .   ? 17.346  -19.603 10.335  1.00 35.08 ? 436 HOH   C O    1 
HETATM 5544 O  O    . HOH   V 6 .   ? 9.497   -46.405 14.288  1.00 28.79 ? 437 HOH   C O    1 
HETATM 5545 O  O    . HOH   V 6 .   ? 0.625   -28.946 6.320   1.00 40.60 ? 438 HOH   C O    1 
HETATM 5546 O  O    . HOH   V 6 .   ? 12.630  -49.814 15.276  1.00 42.26 ? 439 HOH   C O    1 
HETATM 5547 O  O    . HOH   V 6 .   ? 9.446   -22.456 5.635   1.00 42.26 ? 440 HOH   C O    1 
HETATM 5548 O  O    . HOH   V 6 .   ? 8.941   -50.029 6.910   1.00 28.70 ? 441 HOH   C O    1 
HETATM 5549 O  O    . HOH   V 6 .   ? 6.048   -38.242 -1.771  1.00 54.74 ? 442 HOH   C O    1 
HETATM 5550 O  O    . HOH   V 6 .   ? 24.579  -27.103 17.050  1.00 23.28 ? 443 HOH   C O    1 
HETATM 5551 O  O    . HOH   V 6 .   ? 19.131  -28.090 -4.068  1.00 23.51 ? 444 HOH   C O    1 
HETATM 5552 O  O    . HOH   V 6 .   ? 22.254  -19.665 5.468   1.00 36.72 ? 445 HOH   C O    1 
HETATM 5553 O  O    . HOH   V 6 .   ? -7.016  -47.824 5.866   1.00 27.42 ? 446 HOH   C O    1 
HETATM 5554 O  O    . HOH   V 6 .   ? 8.031   -20.145 16.912  1.00 30.42 ? 447 HOH   C O    1 
HETATM 5555 O  O    . HOH   V 6 .   ? 2.758   -28.166 23.901  1.00 18.83 ? 448 HOH   C O    1 
HETATM 5556 O  O    . HOH   V 6 .   ? 17.870  -47.635 15.360  1.00 28.84 ? 449 HOH   C O    1 
HETATM 5557 O  O    . HOH   V 6 .   ? 14.139  -41.302 10.122  1.00 13.11 ? 450 HOH   C O    1 
HETATM 5558 O  O    . HOH   V 6 .   ? 12.388  -40.083 -2.267  1.00 26.12 ? 451 HOH   C O    1 
HETATM 5559 O  O    . HOH   V 6 .   ? 25.256  -21.450 6.248   1.00 34.12 ? 452 HOH   C O    1 
HETATM 5560 O  O    . HOH   V 6 .   ? 2.770   -40.742 36.812  1.00 29.21 ? 453 HOH   C O    1 
HETATM 5561 O  O    . HOH   V 6 .   ? 2.659   -37.530 0.953   1.00 36.84 ? 454 HOH   C O    1 
HETATM 5562 O  O    . HOH   V 6 .   ? -2.958  -45.468 14.618  1.00 13.39 ? 455 HOH   C O    1 
HETATM 5563 O  O    . HOH   V 6 .   ? 16.811  -22.438 -2.047  1.00 44.90 ? 456 HOH   C O    1 
HETATM 5564 O  O    . HOH   V 6 .   ? 11.514  -36.396 -0.018  1.00 27.40 ? 457 HOH   C O    1 
HETATM 5565 O  O    . HOH   V 6 .   ? 13.689  -40.291 21.514  1.00 18.87 ? 458 HOH   C O    1 
HETATM 5566 O  O    . HOH   V 6 .   ? 22.120  -56.388 7.087   1.00 41.11 ? 459 HOH   C O    1 
HETATM 5567 O  O    . HOH   V 6 .   ? 14.751  -23.832 4.456   1.00 22.10 ? 460 HOH   C O    1 
HETATM 5568 O  O    . HOH   V 6 .   ? -2.070  -31.908 15.056  1.00 25.26 ? 461 HOH   C O    1 
HETATM 5569 O  O    . HOH   V 6 .   ? 28.182  -22.784 3.864   1.00 15.72 ? 462 HOH   C O    1 
HETATM 5570 O  O    A HOH   V 6 .   ? 26.103  -28.363 13.356  0.50 14.23 ? 463 HOH   C O    1 
HETATM 5571 O  O    B HOH   V 6 .   ? 26.697  -29.313 13.075  0.50 26.59 ? 463 HOH   C O    1 
HETATM 5572 O  O    . HOH   V 6 .   ? -1.520  -35.301 19.553  1.00 17.66 ? 464 HOH   C O    1 
HETATM 5573 O  O    . HOH   V 6 .   ? -6.218  -40.170 13.896  1.00 24.71 ? 465 HOH   C O    1 
HETATM 5574 O  O    A HOH   V 6 .   ? 8.772   -41.488 -2.585  0.50 27.54 ? 466 HOH   C O    1 
HETATM 5575 O  O    B HOH   V 6 .   ? 7.803   -40.001 -2.809  0.50 34.03 ? 466 HOH   C O    1 
HETATM 5576 O  O    . HOH   V 6 .   ? 21.937  -21.613 16.401  1.00 15.07 ? 467 HOH   C O    1 
HETATM 5577 O  O    . HOH   V 6 .   ? 10.931  -25.122 -0.133  1.00 36.87 ? 468 HOH   C O    1 
HETATM 5578 O  O    . HOH   V 6 .   ? 33.766  -29.363 9.597   1.00 35.60 ? 469 HOH   C O    1 
HETATM 5579 O  O    . HOH   V 6 .   ? 19.673  -21.269 -1.481  1.00 48.39 ? 470 HOH   C O    1 
HETATM 5580 O  O    . HOH   V 6 .   ? 17.116  -44.374 -5.313  1.00 43.00 ? 471 HOH   C O    1 
HETATM 5581 O  O    . HOH   V 6 .   ? 30.652  -36.636 9.244   1.00 32.15 ? 472 HOH   C O    1 
HETATM 5582 O  O    . HOH   V 6 .   ? 32.997  -32.447 0.280   1.00 35.83 ? 473 HOH   C O    1 
HETATM 5583 O  O    . HOH   V 6 .   ? -2.239  -43.374 32.760  1.00 30.04 ? 474 HOH   C O    1 
HETATM 5584 O  O    . HOH   V 6 .   ? 5.714   -46.242 17.122  1.00 28.39 ? 475 HOH   C O    1 
HETATM 5585 O  O    . HOH   V 6 .   ? 12.808  -44.824 -2.536  1.00 43.22 ? 476 HOH   C O    1 
HETATM 5586 O  O    . HOH   V 6 .   ? 4.762   -27.177 3.954   1.00 42.87 ? 477 HOH   C O    1 
HETATM 5587 O  O    . HOH   V 6 .   ? 1.689   -25.824 26.570  1.00 30.08 ? 478 HOH   C O    1 
HETATM 5588 O  O    . HOH   V 6 .   ? -8.575  -39.924 7.504   1.00 39.10 ? 479 HOH   C O    1 
HETATM 5589 O  O    . HOH   V 6 .   ? 14.676  -48.877 13.795  1.00 36.57 ? 480 HOH   C O    1 
HETATM 5590 O  O    . HOH   V 6 .   ? 20.951  -45.801 17.788  1.00 25.30 ? 481 HOH   C O    1 
HETATM 5591 O  O    . HOH   V 6 .   ? -1.055  -46.520 3.476   1.00 37.00 ? 482 HOH   C O    1 
HETATM 5592 O  O    . HOH   V 6 .   ? -1.500  -40.026 26.195  1.00 27.23 ? 483 HOH   C O    1 
HETATM 5593 O  O    . HOH   V 6 .   ? -7.884  -38.779 17.388  1.00 48.39 ? 484 HOH   C O    1 
HETATM 5594 O  O    . HOH   V 6 .   ? 13.993  -38.058 -1.371  1.00 27.49 ? 485 HOH   C O    1 
HETATM 5595 O  O    . HOH   V 6 .   ? 23.883  -27.805 14.519  1.00 27.99 ? 486 HOH   C O    1 
HETATM 5596 O  O    . HOH   V 6 .   ? 14.836  -45.540 26.504  1.00 43.33 ? 487 HOH   C O    1 
HETATM 5597 O  O    . HOH   V 6 .   ? 10.442  -47.291 0.369   1.00 33.98 ? 488 HOH   C O    1 
HETATM 5598 O  O    . HOH   V 6 .   ? 3.825   -21.307 21.991  1.00 38.61 ? 489 HOH   C O    1 
HETATM 5599 O  O    . HOH   V 6 .   ? 26.990  -42.267 3.865   1.00 25.29 ? 490 HOH   C O    1 
HETATM 5600 O  O    . HOH   V 6 .   ? 29.813  -32.949 -0.156  1.00 31.58 ? 491 HOH   C O    1 
HETATM 5601 O  O    . HOH   V 6 .   ? 5.768   -54.679 16.523  1.00 31.90 ? 492 HOH   C O    1 
HETATM 5602 O  O    . HOH   V 6 .   ? 4.659   -45.315 19.643  1.00 20.83 ? 493 HOH   C O    1 
HETATM 5603 O  O    . HOH   V 6 .   ? 25.100  -41.060 15.673  1.00 20.35 ? 494 HOH   C O    1 
HETATM 5604 O  O    . HOH   V 6 .   ? 25.478  -32.298 -5.801  1.00 39.73 ? 495 HOH   C O    1 
HETATM 5605 O  O    A HOH   V 6 .   ? 26.560  -21.163 8.133   0.50 22.74 ? 496 HOH   C O    1 
HETATM 5606 O  O    B HOH   V 6 .   ? 28.012  -21.012 8.692   0.50 22.72 ? 496 HOH   C O    1 
HETATM 5607 O  O    . HOH   V 6 .   ? -0.001  -48.287 6.111   1.00 22.66 ? 497 HOH   C O    1 
HETATM 5608 O  O    . HOH   V 6 .   ? -3.502  -35.721 13.807  1.00 36.36 ? 498 HOH   C O    1 
HETATM 5609 O  O    A HOH   V 6 .   ? 27.743  -33.661 20.342  0.50 25.76 ? 499 HOH   C O    1 
HETATM 5610 O  O    B HOH   V 6 .   ? 27.358  -34.978 19.464  0.50 27.44 ? 499 HOH   C O    1 
HETATM 5611 O  O    . HOH   V 6 .   ? -8.201  -45.352 19.989  1.00 40.23 ? 500 HOH   C O    1 
HETATM 5612 O  O    . HOH   V 6 .   ? 0.020   -36.523 17.935  1.00 19.86 ? 501 HOH   C O    1 
HETATM 5613 O  O    . HOH   V 6 .   ? 30.108  -24.933 3.980   1.00 26.42 ? 502 HOH   C O    1 
HETATM 5614 O  O    . HOH   V 6 .   ? -1.941  -41.844 3.415   1.00 36.77 ? 503 HOH   C O    1 
HETATM 5615 O  O    . HOH   V 6 .   ? 15.253  -51.278 11.078  1.00 36.74 ? 504 HOH   C O    1 
HETATM 5616 O  O    . HOH   V 6 .   ? 19.447  -43.148 21.885  1.00 35.87 ? 505 HOH   C O    1 
HETATM 5617 O  O    . HOH   V 6 .   ? 13.263  -44.945 11.094  1.00 16.45 ? 506 HOH   C O    1 
HETATM 5618 O  O    . HOH   V 6 .   ? -2.085  -30.716 24.825  1.00 20.17 ? 507 HOH   C O    1 
HETATM 5619 O  O    . HOH   V 6 .   ? 19.774  -18.681 7.138   1.00 33.12 ? 508 HOH   C O    1 
HETATM 5620 O  O    . HOH   V 6 .   ? 3.321   -36.249 -1.516  1.00 36.77 ? 509 HOH   C O    1 
HETATM 5621 O  O    . HOH   V 6 .   ? -2.701  -47.315 26.614  1.00 27.92 ? 510 HOH   C O    1 
HETATM 5622 O  O    . HOH   V 6 .   ? -1.991  -47.346 23.887  1.00 21.76 ? 511 HOH   C O    1 
HETATM 5623 O  O    . HOH   V 6 .   ? 5.617   -45.795 0.253   1.00 31.49 ? 512 HOH   C O    1 
HETATM 5624 O  O    . HOH   V 6 .   ? -6.094  -35.738 17.813  1.00 35.43 ? 513 HOH   C O    1 
HETATM 5625 O  O    . HOH   V 6 .   ? -7.974  -42.354 14.224  1.00 34.30 ? 514 HOH   C O    1 
HETATM 5626 O  O    . HOH   V 6 .   ? 31.074  -30.389 14.971  1.00 21.40 ? 515 HOH   C O    1 
HETATM 5627 O  O    . HOH   V 6 .   ? 3.646   -41.644 0.630   1.00 46.46 ? 516 HOH   C O    1 
HETATM 5628 O  O    . HOH   V 6 .   ? 33.137  -32.977 15.531  1.00 24.03 ? 517 HOH   C O    1 
HETATM 5629 O  O    . HOH   V 6 .   ? 2.036   -54.243 23.098  1.00 35.58 ? 518 HOH   C O    1 
HETATM 5630 O  O    A HOH   V 6 .   ? 26.251  -38.535 -4.645  0.50 26.93 ? 519 HOH   C O    1 
HETATM 5631 O  O    B HOH   V 6 .   ? 27.658  -38.416 -4.442  0.50 35.09 ? 519 HOH   C O    1 
HETATM 5632 O  O    . HOH   V 6 .   ? 31.962  -39.599 0.588   1.00 26.30 ? 520 HOH   C O    1 
HETATM 5633 O  O    . HOH   V 6 .   ? 13.619  -52.100 2.053   1.00 51.14 ? 521 HOH   C O    1 
HETATM 5634 O  O    . HOH   V 6 .   ? -0.915  -24.858 22.511  1.00 24.26 ? 522 HOH   C O    1 
HETATM 5635 O  O    . HOH   V 6 .   ? 15.669  -43.401 11.064  1.00 16.23 ? 523 HOH   C O    1 
HETATM 5636 O  O    . HOH   V 6 .   ? 13.395  -47.677 11.756  1.00 28.72 ? 524 HOH   C O    1 
HETATM 5637 O  O    . HOH   V 6 .   ? -8.692  -38.342 22.684  1.00 39.87 ? 525 HOH   C O    1 
HETATM 5638 O  O    . HOH   V 6 .   ? 23.223  -50.568 1.473   1.00 48.01 ? 526 HOH   C O    1 
HETATM 5639 O  O    . HOH   V 6 .   ? 31.394  -34.494 11.746  1.00 34.26 ? 527 HOH   C O    1 
HETATM 5640 O  O    . HOH   V 6 .   ? 32.159  -38.748 8.772   1.00 36.36 ? 528 HOH   C O    1 
HETATM 5641 O  O    . HOH   V 6 .   ? 29.090  -30.875 -1.244  1.00 37.86 ? 529 HOH   C O    1 
HETATM 5642 O  O    . HOH   V 6 .   ? 33.338  -35.730 15.590  1.00 37.90 ? 530 HOH   C O    1 
HETATM 5643 O  O    . HOH   V 6 .   ? 12.330  -50.818 4.123   1.00 40.87 ? 531 HOH   C O    1 
HETATM 5644 O  O    . HOH   V 6 .   ? 0.784   -38.833 1.781   1.00 53.49 ? 532 HOH   C O    1 
HETATM 5645 O  O    . HOH   V 6 .   ? -3.770  -32.568 16.701  1.00 39.16 ? 533 HOH   C O    1 
HETATM 5646 O  O    . HOH   V 6 .   ? -2.412  -48.053 1.608   1.00 31.70 ? 534 HOH   C O    1 
HETATM 5647 O  O    . HOH   V 6 .   ? 33.960  -26.132 6.294   1.00 52.40 ? 535 HOH   C O    1 
HETATM 5648 O  O    . HOH   V 6 .   ? 32.070  -34.798 -7.003  1.00 41.95 ? 536 HOH   C O    1 
HETATM 5649 O  O    . HOH   V 6 .   ? 11.963  -40.003 -4.905  1.00 46.20 ? 537 HOH   C O    1 
HETATM 5650 O  O    . HOH   V 6 .   ? 28.926  -21.601 6.385   1.00 26.82 ? 538 HOH   C O    1 
HETATM 5651 O  O    . HOH   V 6 .   ? 23.404  -44.798 17.207  1.00 33.19 ? 539 HOH   C O    1 
HETATM 5652 O  O    . HOH   V 6 .   ? 15.115  -41.023 23.800  1.00 45.70 ? 540 HOH   C O    1 
HETATM 5653 O  O    . HOH   V 6 .   ? 17.232  -49.957 13.776  1.00 42.02 ? 541 HOH   C O    1 
HETATM 5654 O  O    . HOH   V 6 .   ? -10.454 -35.745 5.351   1.00 52.19 ? 542 HOH   C O    1 
HETATM 5655 O  O    . HOH   V 6 .   ? 17.744  -52.478 14.652  1.00 44.20 ? 543 HOH   C O    1 
HETATM 5656 O  O    . HOH   V 6 .   ? 21.200  -44.671 20.315  1.00 38.42 ? 544 HOH   C O    1 
HETATM 5657 O  O    . HOH   V 6 .   ? -8.339  -36.227 19.058  1.00 50.99 ? 545 HOH   C O    1 
HETATM 5658 O  O    . HOH   V 6 .   ? 10.935  -48.670 13.238  1.00 34.18 ? 546 HOH   C O    1 
HETATM 5659 O  O    . HOH   V 6 .   ? 11.167  -24.199 -2.624  1.00 43.70 ? 547 HOH   C O    1 
HETATM 5660 O  O    . HOH   V 6 .   ? 7.685   -43.967 -0.344  1.00 33.30 ? 548 HOH   C O    1 
HETATM 5661 O  O    . HOH   V 6 .   ? 0.763   -40.774 3.246   1.00 35.94 ? 549 HOH   C O    1 
HETATM 5662 O  O    . HOH   V 6 .   ? -2.438  -26.828 26.727  1.00 37.86 ? 550 HOH   C O    1 
HETATM 5663 O  O    . HOH   V 6 .   ? 18.381  -19.519 -0.067  1.00 51.17 ? 551 HOH   C O    1 
HETATM 5664 O  O    . HOH   V 6 .   ? 27.238  -30.544 -5.308  1.00 35.41 ? 552 HOH   C O    1 
HETATM 5665 O  O    . HOH   V 6 .   ? 6.487   -42.336 -1.918  1.00 45.33 ? 553 HOH   C O    1 
HETATM 5666 O  O    . HOH   V 6 .   ? 7.795   -45.868 30.957  1.00 36.41 ? 554 HOH   C O    1 
HETATM 5667 O  O    . HOH   V 6 .   ? 25.513  -41.781 18.284  1.00 27.49 ? 555 HOH   C O    1 
HETATM 5668 O  O    . HOH   V 6 .   ? 35.042  -31.366 16.789  1.00 33.93 ? 556 HOH   C O    1 
HETATM 5669 O  O    . HOH   V 6 .   ? 25.355  -40.153 20.483  1.00 32.70 ? 557 HOH   C O    1 
HETATM 5670 O  O    . HOH   V 6 .   ? 24.207  -43.718 19.580  1.00 42.14 ? 558 HOH   C 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    . ALA   A 1   ? 0.5618 0.4145 0.3373 -0.0691 -0.0515 -0.0049 5   ALA   A N    
2    C  CA   . ALA   A 1   ? 0.5354 0.3777 0.3286 -0.0601 -0.0353 -0.0041 5   ALA   A CA   
3    C  C    . ALA   A 1   ? 0.4942 0.3307 0.3231 -0.0525 -0.0287 -0.0022 5   ALA   A C    
4    O  O    . ALA   A 1   ? 0.5117 0.3313 0.3899 -0.0683 -0.0509 0.0047  5   ALA   A O    
5    C  CB   . ALA   A 1   ? 0.5553 0.4090 0.3547 -0.0561 -0.0255 -0.0139 5   ALA   A CB   
6    N  N    . LEU   A 2   ? 0.4518 0.2932 0.2762 -0.0220 -0.0005 0.0055  6   LEU   A N    
7    C  CA   . LEU   A 2   ? 0.4313 0.2771 0.2566 -0.0068 0.0108  0.0005  6   LEU   A CA   
8    C  C    . LEU   A 2   ? 0.4402 0.2862 0.2671 0.0094  0.0225  0.0094  6   LEU   A C    
9    O  O    . LEU   A 2   ? 0.4361 0.3265 0.2863 0.0006  0.0443  0.0530  6   LEU   A O    
10   C  CB   . LEU   A 2   ? 0.4311 0.2731 0.2379 -0.0140 0.0156  -0.0018 6   LEU   A CB   
11   C  CG   . LEU   A 2   ? 0.4292 0.2744 0.2422 -0.0235 0.0155  -0.0063 6   LEU   A CG   
12   C  CD1  . LEU   A 2   ? 0.4444 0.2864 0.2607 -0.0266 0.0140  -0.0189 6   LEU   A CD1  
13   C  CD2  . LEU   A 2   ? 0.4305 0.2741 0.2506 -0.0236 0.0123  -0.0167 6   LEU   A CD2  
14   N  N    . PRO   A 3   ? 0.4432 0.2913 0.2536 0.0373  0.0215  0.0093  7   PRO   A N    
15   C  CA   . PRO   A 3   ? 0.4390 0.2947 0.2685 0.0390  0.0298  0.0094  7   PRO   A CA   
16   C  C    . PRO   A 3   ? 0.4095 0.2976 0.2682 0.0372  0.0461  0.0076  7   PRO   A C    
17   O  O    . PRO   A 3   ? 0.4127 0.3438 0.2837 0.0488  0.0638  0.0276  7   PRO   A O    
18   C  CB   . PRO   A 3   ? 0.4510 0.2815 0.2756 0.0489  0.0285  0.0002  7   PRO   A CB   
19   C  CG   . PRO   A 3   ? 0.4635 0.2792 0.2900 0.0461  0.0195  0.0049  7   PRO   A CG   
20   C  CD   . PRO   A 3   ? 0.4483 0.2737 0.2667 0.0485  0.0211  0.0019  7   PRO   A CD   
21   N  N    . HIS   A 4   ? 0.3858 0.2929 0.2532 0.0261  0.0496  0.0090  8   HIS   A N    
22   C  CA   . HIS   A 4   ? 0.3746 0.2763 0.2483 0.0272  0.0520  0.0064  8   HIS   A CA   
23   C  C    . HIS   A 4   ? 0.3589 0.2677 0.2302 0.0204  0.0517  0.0055  8   HIS   A C    
24   O  O    . HIS   A 4   ? 0.3746 0.2725 0.2472 0.0101  0.0465  -0.0006 8   HIS   A O    
25   C  CB   . HIS   A 4   ? 0.3886 0.3171 0.2471 0.0171  0.0647  0.0169  8   HIS   A CB   
26   C  CG   . HIS   A 4   ? 0.4121 0.3143 0.2617 0.0156  0.0719  0.0177  8   HIS   A CG   
27   N  ND1  . HIS   A 4   ? 0.4218 0.3356 0.2691 0.0117  0.0936  0.0173  8   HIS   A ND1  
28   C  CD2  . HIS   A 4   ? 0.4322 0.3212 0.2685 0.0136  0.0782  0.0258  8   HIS   A CD2  
29   C  CE1  . HIS   A 4   ? 0.4348 0.3315 0.2848 0.0150  0.0980  0.0187  8   HIS   A CE1  
30   N  NE2  . HIS   A 4   ? 0.4418 0.3060 0.2784 0.0170  0.0883  0.0232  8   HIS   A NE2  
31   N  N    . GLY   A 5   ? 0.3529 0.2226 0.2191 0.0142  0.0525  0.0007  9   GLY   A N    
32   C  CA   . GLY   A 5   ? 0.3272 0.2162 0.2009 0.0043  0.0647  0.0136  9   GLY   A CA   
33   C  C    . GLY   A 5   ? 0.3029 0.1831 0.2015 0.0000  0.0587  0.0022  9   GLY   A C    
34   O  O    . GLY   A 5   ? 0.3312 0.1788 0.2301 0.0000  0.0664  0.0072  9   GLY   A O    
35   N  N    . HIS   A 6   ? 0.2804 0.1547 0.1754 -0.0101 0.0434  0.0119  10  HIS   A N    
36   C  CA   . HIS   A 6   ? 0.2658 0.1534 0.1461 -0.0085 0.0232  0.0139  10  HIS   A CA   
37   C  C    . HIS   A 6   ? 0.2510 0.1452 0.1494 -0.0105 0.0181  0.0130  10  HIS   A C    
38   O  O    . HIS   A 6   ? 0.2345 0.1571 0.1625 -0.0045 0.0187  0.0219  10  HIS   A O    
39   C  CB   . HIS   A 6   ? 0.2771 0.1654 0.1505 -0.0001 0.0150  0.0162  10  HIS   A CB   
40   C  CG   . HIS   A 6   ? 0.2764 0.1782 0.1581 0.0009  0.0016  0.0197  10  HIS   A CG   
41   N  ND1  . HIS   A 6   ? 0.2824 0.2038 0.1619 -0.0011 -0.0097 0.0190  10  HIS   A ND1  
42   C  CD2  . HIS   A 6   ? 0.2813 0.2021 0.1677 -0.0065 -0.0012 0.0232  10  HIS   A CD2  
43   C  CE1  . HIS   A 6   ? 0.2886 0.2076 0.1781 -0.0095 -0.0134 0.0330  10  HIS   A CE1  
44   N  NE2  . HIS   A 6   ? 0.2823 0.2115 0.1658 -0.0081 -0.0050 0.0294  10  HIS   A NE2  
45   N  N    . MET   A 7   ? 0.2361 0.1383 0.1316 -0.0120 0.0088  0.0135  11  MET   A N    
46   C  CA   . MET   A 7   ? 0.2288 0.1471 0.1316 -0.0086 0.0085  0.0124  11  MET   A CA   
47   C  C    . MET   A 7   ? 0.2127 0.1363 0.1343 -0.0096 0.0018  0.0114  11  MET   A C    
48   O  O    . MET   A 7   ? 0.2121 0.1488 0.1511 -0.0081 -0.0067 -0.0029 11  MET   A O    
49   C  CB   . MET   A 7   ? 0.2282 0.1512 0.1346 -0.0076 0.0065  0.0123  11  MET   A CB   
50   C  CG   . MET   A 7   ? 0.2329 0.1588 0.1399 -0.0063 0.0075  0.0124  11  MET   A CG   
51   S  SD   . MET   A 7   ? 0.2399 0.1666 0.1712 0.0006  0.0202  0.0092  11  MET   A SD   
52   C  CE   . MET   A 7   ? 0.2549 0.1948 0.1742 -0.0035 0.0225  0.0043  11  MET   A CE   
53   N  N    . GLN   A 8   ? 0.1952 0.1376 0.1338 -0.0111 0.0048  0.0162  12  GLN   A N    
54   C  CA   . GLN   A 8   ? 0.1939 0.1371 0.1335 -0.0168 0.0094  0.0140  12  GLN   A CA   
55   C  C    . GLN   A 8   ? 0.1945 0.1449 0.1271 -0.0152 0.0126  0.0047  12  GLN   A C    
56   O  O    . GLN   A 8   ? 0.1988 0.1489 0.1396 -0.0115 0.0143  -0.0015 12  GLN   A O    
57   C  CB   . GLN   A 8   ? 0.1942 0.1476 0.1457 -0.0156 0.0051  0.0144  12  GLN   A CB   
58   C  CG   . GLN   A 8   ? 0.1987 0.1426 0.1578 -0.0213 0.0084  0.0143  12  GLN   A CG   
59   C  CD   . GLN   A 8   ? 0.1883 0.1470 0.1581 -0.0130 0.0120  0.0141  12  GLN   A CD   
60   O  OE1  . GLN   A 8   ? 0.2092 0.1517 0.1677 -0.0074 0.0171  0.0172  12  GLN   A OE1  
61   N  NE2  . GLN   A 8   ? 0.1821 0.1408 0.1587 -0.0098 0.0145  0.0167  12  GLN   A NE2  
62   N  N    . THR   A 9   ? 0.2029 0.1434 0.1304 -0.0151 0.0215  0.0015  13  THR   A N    
63   C  CA   . THR   A 9   ? 0.2061 0.1456 0.1373 -0.0205 0.0158  0.0056  13  THR   A CA   
64   C  C    . THR   A 9   ? 0.2083 0.1375 0.1426 -0.0136 0.0120  0.0048  13  THR   A C    
65   O  O    . THR   A 9   ? 0.2002 0.1363 0.1873 -0.0146 0.0282  -0.0028 13  THR   A O    
66   C  CB   . THR   A 9   ? 0.2215 0.1694 0.1383 -0.0298 0.0069  0.0073  13  THR   A CB   
67   O  OG1  . THR   A 9   ? 0.2371 0.1680 0.1381 -0.0225 -0.0116 -0.0048 13  THR   A OG1  
68   C  CG2  . THR   A 9   ? 0.2338 0.2037 0.1455 -0.0367 0.0023  0.0232  13  THR   A CG2  
69   N  N    . LEU   A 10  ? 0.2102 0.1266 0.1309 -0.0142 0.0064  0.0123  14  LEU   A N    
70   C  CA   . LEU   A 10  ? 0.2181 0.1361 0.1348 -0.0145 0.0024  0.0174  14  LEU   A CA   
71   C  C    . LEU   A 10  ? 0.2092 0.1321 0.1249 -0.0132 0.0071  0.0105  14  LEU   A C    
72   O  O    . LEU   A 10  ? 0.2135 0.1414 0.1296 -0.0089 0.0223  0.0128  14  LEU   A O    
73   C  CB   . LEU   A 10  ? 0.2332 0.1776 0.1662 -0.0184 -0.0143 0.0300  14  LEU   A CB   
74   C  CG   . LEU   A 10  ? 0.2712 0.2383 0.1855 -0.0103 -0.0421 0.0448  14  LEU   A CG   
75   C  CD1  . LEU   A 10  ? 0.2922 0.2782 0.2141 -0.0065 -0.0309 0.0381  14  LEU   A CD1  
76   C  CD2  . LEU   A 10  ? 0.2846 0.2502 0.2086 -0.0071 -0.0438 0.0603  14  LEU   A CD2  
77   N  N    . ILE   A 11  ? 0.2090 0.1317 0.1110 -0.0104 0.0061  0.0110  15  ILE   A N    
78   C  CA   . ILE   A 11  ? 0.2152 0.1265 0.1129 -0.0163 -0.0013 0.0110  15  ILE   A CA   
79   C  C    . ILE   A 11  ? 0.2082 0.1244 0.1110 -0.0165 -0.0042 0.0105  15  ILE   A C    
80   O  O    . ILE   A 11  ? 0.2125 0.1302 0.1289 -0.0152 0.0059  0.0036  15  ILE   A O    
81   C  CB   . ILE   A 11  ? 0.2298 0.1634 0.1429 -0.0121 -0.0001 0.0159  15  ILE   A CB   
82   C  CG1  . ILE   A 11  ? 0.2701 0.1926 0.1809 -0.0198 -0.0003 0.0278  15  ILE   A CG1  
83   C  CG2  . ILE   A 11  ? 0.2339 0.1764 0.1450 -0.0093 -0.0083 0.0184  15  ILE   A CG2  
84   C  CD1  . ILE   A 11  ? 0.2917 0.2384 0.2149 -0.0107 0.0106  0.0130  15  ILE   A CD1  
85   N  N    . PHE   A 12  ? 0.2050 0.1087 0.1154 -0.0128 -0.0136 0.0087  16  PHE   A N    
86   C  CA   . PHE   A 12  ? 0.2057 0.1136 0.1248 -0.0167 -0.0191 -0.0006 16  PHE   A CA   
87   C  C    . PHE   A 12  ? 0.2060 0.1133 0.1229 -0.0149 -0.0204 -0.0007 16  PHE   A C    
88   O  O    . PHE   A 12  ? 0.2306 0.1176 0.1264 -0.0061 -0.0242 -0.0039 16  PHE   A O    
89   C  CB   . PHE   A 12  ? 0.2035 0.1236 0.1326 -0.0190 -0.0155 0.0012  16  PHE   A CB   
90   C  CG   . PHE   A 12  ? 0.2089 0.1402 0.1504 -0.0180 -0.0209 0.0076  16  PHE   A CG   
91   C  CD1  . PHE   A 12  ? 0.2235 0.1406 0.1596 -0.0220 -0.0266 0.0026  16  PHE   A CD1  
92   C  CD2  . PHE   A 12  ? 0.2121 0.1395 0.1545 -0.0223 -0.0234 0.0085  16  PHE   A CD2  
93   C  CE1  . PHE   A 12  ? 0.2260 0.1646 0.1643 -0.0172 -0.0298 0.0064  16  PHE   A CE1  
94   C  CE2  . PHE   A 12  ? 0.2152 0.1484 0.1719 -0.0181 -0.0247 0.0147  16  PHE   A CE2  
95   C  CZ   . PHE   A 12  ? 0.2211 0.1577 0.1585 -0.0138 -0.0246 0.0183  16  PHE   A CZ   
96   N  N    . PHE   A 13  ? 0.1994 0.1137 0.1204 -0.0182 -0.0232 -0.0005 17  PHE   A N    
97   C  CA   . PHE   A 13  ? 0.1851 0.1151 0.1188 -0.0211 -0.0243 -0.0015 17  PHE   A CA   
98   C  C    . PHE   A 13  ? 0.1873 0.1174 0.1188 -0.0191 -0.0260 -0.0010 17  PHE   A C    
99   O  O    . PHE   A 13  ? 0.2047 0.1290 0.1133 -0.0239 -0.0314 0.0020  17  PHE   A O    
100  C  CB   . PHE   A 13  ? 0.1943 0.1227 0.1223 -0.0179 -0.0178 -0.0094 17  PHE   A CB   
101  C  CG   . PHE   A 13  ? 0.1905 0.1324 0.1301 -0.0185 -0.0178 -0.0032 17  PHE   A CG   
102  C  CD1  . PHE   A 13  ? 0.1986 0.1472 0.1325 -0.0105 -0.0171 -0.0021 17  PHE   A CD1  
103  C  CD2  . PHE   A 13  ? 0.1974 0.1428 0.1458 -0.0151 -0.0116 -0.0051 17  PHE   A CD2  
104  C  CE1  . PHE   A 13  ? 0.1986 0.1531 0.1379 -0.0125 -0.0192 0.0016  17  PHE   A CE1  
105  C  CE2  . PHE   A 13  ? 0.1994 0.1470 0.1550 -0.0195 -0.0127 -0.0024 17  PHE   A CE2  
106  C  CZ   . PHE   A 13  ? 0.1922 0.1414 0.1567 -0.0195 -0.0168 0.0052  17  PHE   A CZ   
107  N  N    . ASP   A 14  ? 0.1779 0.1134 0.1096 -0.0162 -0.0221 -0.0035 18  ASP   A N    
108  C  CA   . ASP   A 14  ? 0.1839 0.1150 0.1179 -0.0132 -0.0201 -0.0007 18  ASP   A CA   
109  C  C    . ASP   A 14  ? 0.1847 0.1122 0.1080 -0.0099 -0.0225 -0.0043 18  ASP   A C    
110  O  O    . ASP   A 14  ? 0.1965 0.1233 0.1179 -0.0095 -0.0322 -0.0111 18  ASP   A O    
111  C  CB   . ASP   A 14  ? 0.1885 0.1250 0.1347 -0.0098 -0.0108 0.0007  18  ASP   A CB   
112  C  CG   . ASP   A 14  ? 0.2018 0.1430 0.1621 -0.0194 -0.0090 -0.0012 18  ASP   A CG   
113  O  OD1  . ASP   A 14  ? 0.2191 0.1511 0.1705 -0.0333 -0.0141 -0.0019 18  ASP   A OD1  
114  O  OD2  . ASP   A 14  ? 0.2151 0.1704 0.1717 -0.0191 0.0025  0.0041  18  ASP   A OD2  
115  N  N    . MET   A 15  ? 0.1978 0.1110 0.1024 -0.0097 -0.0230 0.0007  19  MET   A N    
116  C  CA   . MET   A 15  ? 0.1889 0.1167 0.1095 -0.0074 -0.0239 0.0018  19  MET   A CA   
117  C  C    . MET   A 15  ? 0.1821 0.1170 0.1168 -0.0045 -0.0204 0.0030  19  MET   A C    
118  O  O    . MET   A 15  ? 0.1907 0.1217 0.1222 -0.0001 -0.0289 0.0018  19  MET   A O    
119  C  CB   . MET   A 15  ? 0.1939 0.1321 0.1164 -0.0099 -0.0177 -0.0008 19  MET   A CB   
120  C  CG   . MET   A 15  ? 0.1965 0.1420 0.1285 -0.0156 -0.0141 0.0012  19  MET   A CG   
121  S  SD   . MET   A 15  ? 0.2053 0.1677 0.1546 -0.0112 -0.0160 -0.0002 19  MET   A SD   
122  C  CE   . MET   A 15  ? 0.2006 0.1818 0.1479 -0.0127 -0.0161 -0.0077 19  MET   A CE   
123  N  N    A GLU   A 16  ? 0.1802 0.1097 0.1204 -0.0017 -0.0200 0.0091  20  GLU   A N    
124  N  N    B GLU   A 16  ? 0.1784 0.1110 0.1165 -0.0056 -0.0212 0.0061  20  GLU   A N    
125  C  CA   A GLU   A 16  ? 0.1774 0.1117 0.1393 -0.0031 -0.0153 0.0059  20  GLU   A CA   
126  C  CA   B GLU   A 16  ? 0.1753 0.1143 0.1313 -0.0093 -0.0180 0.0017  20  GLU   A CA   
127  C  C    A GLU   A 16  ? 0.1705 0.1079 0.1350 -0.0045 -0.0117 0.0057  20  GLU   A C    
128  C  C    B GLU   A 16  ? 0.1700 0.1098 0.1321 -0.0086 -0.0136 0.0028  20  GLU   A C    
129  O  O    A GLU   A 16  ? 0.1699 0.1071 0.1273 -0.0019 -0.0127 0.0047  20  GLU   A O    
130  O  O    B GLU   A 16  ? 0.1730 0.1083 0.1259 -0.0076 -0.0169 -0.0002 20  GLU   A O    
131  C  CB   A GLU   A 16  ? 0.1887 0.1245 0.1542 -0.0029 -0.0085 0.0114  20  GLU   A CB   
132  C  CB   B GLU   A 16  ? 0.1858 0.1285 0.1419 -0.0139 -0.0128 0.0040  20  GLU   A CB   
133  C  CG   A GLU   A 16  ? 0.2028 0.1394 0.1771 0.0060  -0.0058 0.0124  20  GLU   A CG   
134  C  CG   B GLU   A 16  ? 0.1913 0.1452 0.1563 -0.0102 -0.0156 0.0018  20  GLU   A CG   
135  C  CD   A GLU   A 16  ? 0.2167 0.1706 0.2097 0.0121  -0.0109 0.0080  20  GLU   A CD   
136  C  CD   B GLU   A 16  ? 0.2083 0.1689 0.1653 -0.0094 -0.0065 0.0048  20  GLU   A CD   
137  O  OE1  A GLU   A 16  ? 0.2359 0.1943 0.2391 0.0174  -0.0160 -0.0069 20  GLU   A OE1  
138  O  OE1  B GLU   A 16  ? 0.2366 0.2180 0.1754 -0.0067 -0.0081 0.0028  20  GLU   A OE1  
139  O  OE2  A GLU   A 16  ? 0.2324 0.2127 0.2354 0.0291  -0.0015 0.0025  20  GLU   A OE2  
140  O  OE2  B GLU   A 16  ? 0.2138 0.2038 0.1916 -0.0009 0.0126  0.0081  20  GLU   A OE2  
141  N  N    . ALA   A 17  ? 0.1621 0.1102 0.1428 -0.0064 -0.0120 -0.0033 21  ALA   A N    
142  C  CA   . ALA   A 17  ? 0.1612 0.1076 0.1422 -0.0038 -0.0070 -0.0005 21  ALA   A CA   
143  C  C    . ALA   A 17  ? 0.1606 0.1108 0.1505 -0.0050 0.0015  -0.0022 21  ALA   A C    
144  O  O    . ALA   A 17  ? 0.1608 0.1233 0.1738 -0.0013 -0.0005 -0.0057 21  ALA   A O    
145  C  CB   . ALA   A 17  ? 0.1628 0.1140 0.1504 -0.0023 -0.0022 0.0026  21  ALA   A CB   
146  N  N    . THR   A 18  ? 0.1570 0.1121 0.1423 0.0000  0.0042  -0.0033 22  THR   A N    
147  C  CA   . THR   A 18  ? 0.1618 0.1087 0.1430 -0.0057 -0.0010 -0.0031 22  THR   A CA   
148  C  C    . THR   A 18  ? 0.1651 0.1167 0.1505 -0.0120 -0.0045 -0.0037 22  THR   A C    
149  O  O    . THR   A 18  ? 0.1856 0.1259 0.1591 -0.0275 0.0025  -0.0135 22  THR   A O    
150  C  CB   . THR   A 18  ? 0.1636 0.1133 0.1455 -0.0029 -0.0004 0.0042  22  THR   A CB   
151  O  OG1  . THR   A 18  ? 0.1717 0.1153 0.1430 -0.0007 -0.0016 0.0069  22  THR   A OG1  
152  C  CG2  . THR   A 18  ? 0.1736 0.1215 0.1426 0.0002  -0.0031 0.0055  22  THR   A CG2  
153  N  N    . GLY   A 19  ? 0.1672 0.1029 0.1508 -0.0172 -0.0071 -0.0054 23  GLY   A N    
154  C  CA   . GLY   A 19  ? 0.1647 0.1026 0.1555 -0.0125 -0.0118 -0.0049 23  GLY   A CA   
155  C  C    . GLY   A 19  ? 0.1633 0.1080 0.1545 -0.0142 -0.0139 -0.0063 23  GLY   A C    
156  O  O    . GLY   A 19  ? 0.1640 0.1038 0.1480 -0.0198 -0.0187 -0.0104 23  GLY   A O    
157  N  N    . LEU   A 20  ? 0.1816 0.1268 0.1575 -0.0181 -0.0205 -0.0086 24  LEU   A N    
158  C  CA   . LEU   A 20  ? 0.1813 0.1272 0.1582 -0.0238 -0.0192 -0.0071 24  LEU   A CA   
159  C  C    . LEU   A 20  ? 0.1883 0.1438 0.1474 -0.0174 -0.0212 -0.0155 24  LEU   A C    
160  O  O    . LEU   A 20  ? 0.1908 0.1404 0.1503 -0.0091 -0.0137 -0.0187 24  LEU   A O    
161  C  CB   . LEU   A 20  ? 0.1835 0.1261 0.1718 -0.0270 -0.0206 -0.0066 24  LEU   A CB   
162  C  CG   . LEU   A 20  ? 0.1819 0.1454 0.1957 -0.0320 -0.0218 -0.0106 24  LEU   A CG   
163  C  CD1  . LEU   A 20  ? 0.1900 0.1614 0.2119 -0.0367 -0.0305 -0.0105 24  LEU   A CD1  
164  C  CD2  . LEU   A 20  ? 0.1871 0.1582 0.2263 -0.0256 -0.0182 -0.0135 24  LEU   A CD2  
165  N  N    . PRO   A 21  ? 0.1933 0.1391 0.1490 -0.0233 -0.0301 -0.0073 25  PRO   A N    
166  C  CA   . PRO   A 21  ? 0.1970 0.1471 0.1388 -0.0266 -0.0291 -0.0143 25  PRO   A CA   
167  C  C    . PRO   A 21  ? 0.2108 0.1570 0.1360 -0.0155 -0.0235 -0.0104 25  PRO   A C    
168  O  O    . PRO   A 21  ? 0.2143 0.1819 0.1437 -0.0163 -0.0199 -0.0077 25  PRO   A O    
169  C  CB   . PRO   A 21  ? 0.2005 0.1510 0.1455 -0.0283 -0.0341 -0.0105 25  PRO   A CB   
170  C  CG   . PRO   A 21  ? 0.2016 0.1563 0.1425 -0.0236 -0.0340 -0.0072 25  PRO   A CG   
171  C  CD   . PRO   A 21  ? 0.1998 0.1601 0.1489 -0.0221 -0.0346 -0.0075 25  PRO   A CD   
172  N  N    . SER   A 22  ? 0.2320 0.1541 0.1453 -0.0159 -0.0221 -0.0155 26  SER   A N    
173  C  CA   . SER   A 22  ? 0.2389 0.1565 0.1600 -0.0099 -0.0203 -0.0192 26  SER   A CA   
174  C  C    . SER   A 22  ? 0.2246 0.1351 0.1640 -0.0050 -0.0207 -0.0166 26  SER   A C    
175  O  O    . SER   A 22  ? 0.2332 0.1512 0.1648 0.0196  -0.0226 -0.0100 26  SER   A O    
176  C  CB   . SER   A 22  ? 0.2790 0.1654 0.1678 -0.0197 -0.0316 -0.0333 26  SER   A CB   
177  O  OG   . SER   A 22  ? 0.3341 0.2413 0.2051 -0.0172 -0.0129 -0.0121 26  SER   A OG   
178  N  N    . SER   A 23  ? 0.2074 0.1233 0.1630 0.0020  -0.0285 -0.0165 27  SER   A N    
179  C  CA   . SER   A 23  ? 0.2019 0.1287 0.1570 -0.0038 -0.0198 -0.0204 27  SER   A CA   
180  C  C    . SER   A 23  ? 0.1897 0.1276 0.1515 0.0047  -0.0156 -0.0222 27  SER   A C    
181  O  O    . SER   A 23  ? 0.1977 0.1541 0.1553 -0.0008 -0.0206 -0.0112 27  SER   A O    
182  C  CB   . SER   A 23  ? 0.1890 0.1344 0.1688 -0.0123 -0.0148 -0.0196 27  SER   A CB   
183  O  OG   . SER   A 23  ? 0.1879 0.1392 0.1642 -0.0046 -0.0106 -0.0233 27  SER   A OG   
184  N  N    . ARG   A 24  ? 0.1861 0.1340 0.1444 0.0057  -0.0134 -0.0250 28  ARG   A N    
185  C  CA   . ARG   A 24  ? 0.1824 0.1396 0.1464 0.0117  -0.0103 -0.0187 28  ARG   A CA   
186  C  C    . ARG   A 24  ? 0.1739 0.1281 0.1382 0.0056  -0.0108 -0.0121 28  ARG   A C    
187  O  O    . ARG   A 24  ? 0.1807 0.1396 0.1470 0.0148  -0.0092 -0.0143 28  ARG   A O    
188  C  CB   . ARG   A 24  ? 0.1981 0.1456 0.1558 0.0210  -0.0108 -0.0214 28  ARG   A CB   
189  C  CG   . ARG   A 24  ? 0.2081 0.1717 0.1898 0.0199  -0.0109 -0.0188 28  ARG   A CG   
190  C  CD   . ARG   A 24  ? 0.2277 0.1944 0.2196 0.0192  -0.0214 -0.0077 28  ARG   A CD   
191  N  NE   . ARG   A 24  ? 0.2497 0.2232 0.2503 0.0127  -0.0300 -0.0118 28  ARG   A NE   
192  C  CZ   . ARG   A 24  ? 0.2743 0.2286 0.2521 0.0218  -0.0325 -0.0133 28  ARG   A CZ   
193  N  NH1  . ARG   A 24  ? 0.2938 0.2270 0.2445 0.0384  -0.0384 -0.0258 28  ARG   A NH1  
194  N  NH2  . ARG   A 24  ? 0.2769 0.2600 0.2704 0.0214  -0.0383 0.0057  28  ARG   A NH2  
195  N  N    . PRO   A 25  ? 0.1794 0.1233 0.1256 0.0060  -0.0122 -0.0165 29  PRO   A N    
196  C  CA   . PRO   A 25  ? 0.1741 0.1238 0.1297 0.0034  -0.0047 -0.0149 29  PRO   A CA   
197  C  C    . PRO   A 25  ? 0.1722 0.1268 0.1307 -0.0019 -0.0042 -0.0133 29  PRO   A C    
198  O  O    . PRO   A 25  ? 0.1695 0.1319 0.1235 -0.0063 -0.0081 -0.0123 29  PRO   A O    
199  C  CB   . PRO   A 25  ? 0.1755 0.1244 0.1352 0.0001  -0.0107 -0.0136 29  PRO   A CB   
200  C  CG   . PRO   A 25  ? 0.1749 0.1219 0.1353 0.0056  -0.0141 -0.0075 29  PRO   A CG   
201  C  CD   . PRO   A 25  ? 0.1810 0.1208 0.1247 0.0052  -0.0116 -0.0078 29  PRO   A CD   
202  N  N    . GLU   A 26  ? 0.1731 0.1232 0.1257 -0.0057 -0.0103 -0.0160 30  GLU   A N    
203  C  CA   . GLU   A 26  ? 0.1744 0.1192 0.1374 -0.0033 -0.0140 -0.0153 30  GLU   A CA   
204  C  C    . GLU   A 26  ? 0.1651 0.1214 0.1420 -0.0057 -0.0121 -0.0101 30  GLU   A C    
205  O  O    . GLU   A 26  ? 0.1601 0.1149 0.1458 -0.0130 -0.0156 -0.0018 30  GLU   A O    
206  C  CB   . GLU   A 26  ? 0.1913 0.1431 0.1553 0.0044  -0.0241 -0.0175 30  GLU   A CB   
207  C  CG   . GLU   A 26  ? 0.2083 0.1607 0.1696 0.0145  -0.0256 -0.0269 30  GLU   A CG   
208  C  CD   . GLU   A 26  ? 0.2384 0.1983 0.1890 0.0317  -0.0351 -0.0243 30  GLU   A CD   
209  O  OE1  . GLU   A 26  ? 0.2609 0.2553 0.1689 0.0383  -0.0339 -0.0216 30  GLU   A OE1  
210  O  OE2  . GLU   A 26  ? 0.2835 0.2193 0.2219 0.0593  -0.0465 -0.0318 30  GLU   A OE2  
211  N  N    . VAL   A 27  ? 0.1582 0.1174 0.1400 -0.0056 -0.0090 -0.0087 31  VAL   A N    
212  C  CA   . VAL   A 27  ? 0.1610 0.1174 0.1311 0.0005  -0.0132 -0.0072 31  VAL   A CA   
213  C  C    . VAL   A 27  ? 0.1647 0.1090 0.1271 0.0023  -0.0225 -0.0036 31  VAL   A C    
214  O  O    . VAL   A 27  ? 0.1648 0.1241 0.1459 0.0037  -0.0300 0.0015  31  VAL   A O    
215  C  CB   . VAL   A 27  ? 0.1666 0.1284 0.1323 -0.0019 -0.0066 -0.0082 31  VAL   A CB   
216  C  CG1  . VAL   A 27  ? 0.1737 0.1273 0.1440 -0.0010 -0.0065 -0.0078 31  VAL   A CG1  
217  C  CG2  . VAL   A 27  ? 0.1732 0.1371 0.1305 0.0033  -0.0061 -0.0111 31  VAL   A CG2  
218  N  N    . THR   A 28  ? 0.1612 0.1110 0.1188 0.0004  -0.0212 0.0052  32  THR   A N    
219  C  CA   . THR   A 28  ? 0.1676 0.1106 0.1229 0.0056  -0.0226 -0.0021 32  THR   A CA   
220  C  C    . THR   A 28  ? 0.1664 0.1116 0.1202 0.0015  -0.0211 -0.0031 32  THR   A C    
221  O  O    . THR   A 28  ? 0.1726 0.1176 0.1213 0.0019  -0.0089 -0.0067 32  THR   A O    
222  C  CB   . THR   A 28  ? 0.1768 0.1159 0.1321 0.0040  -0.0192 0.0032  32  THR   A CB   
223  O  OG1  . THR   A 28  ? 0.1754 0.1279 0.1389 -0.0021 -0.0246 0.0000  32  THR   A OG1  
224  C  CG2  . THR   A 28  ? 0.1871 0.1202 0.1452 0.0068  -0.0172 0.0049  32  THR   A CG2  
225  N  N    . GLU   A 29  ? 0.1790 0.1056 0.1110 0.0002  -0.0158 -0.0047 33  GLU   A N    
226  C  CA   . GLU   A 29  ? 0.1876 0.1068 0.1238 0.0026  -0.0156 0.0005  33  GLU   A CA   
227  C  C    . GLU   A 29  ? 0.1862 0.1087 0.1116 0.0011  -0.0209 -0.0056 33  GLU   A C    
228  O  O    . GLU   A 29  ? 0.1917 0.0996 0.1154 0.0018  -0.0149 -0.0130 33  GLU   A O    
229  C  CB   . GLU   A 29  ? 0.2005 0.1266 0.1471 0.0057  -0.0054 0.0040  33  GLU   A CB   
230  C  CG   . GLU   A 29  ? 0.2174 0.1458 0.1716 0.0109  -0.0109 -0.0057 33  GLU   A CG   
231  C  CD   . GLU   A 29  ? 0.2373 0.1763 0.1958 0.0083  -0.0018 -0.0035 33  GLU   A CD   
232  O  OE1  . GLU   A 29  ? 0.2492 0.1992 0.2272 -0.0028 -0.0216 0.0180  33  GLU   A OE1  
233  O  OE2  . GLU   A 29  ? 0.2579 0.2109 0.2225 0.0361  0.0126  -0.0088 33  GLU   A OE2  
234  N  N    . LEU   A 30  ? 0.2001 0.1093 0.1138 -0.0031 -0.0261 -0.0019 34  LEU   A N    
235  C  CA   . LEU   A 30  ? 0.1997 0.1134 0.1252 -0.0062 -0.0177 0.0013  34  LEU   A CA   
236  C  C    . LEU   A 30  ? 0.1930 0.1112 0.1218 -0.0086 -0.0207 0.0022  34  LEU   A C    
237  O  O    . LEU   A 30  ? 0.2280 0.1227 0.1286 0.0011  -0.0267 -0.0006 34  LEU   A O    
238  C  CB   . LEU   A 30  ? 0.2099 0.1318 0.1598 -0.0063 -0.0115 0.0037  34  LEU   A CB   
239  C  CG   . LEU   A 30  ? 0.2196 0.1542 0.1843 -0.0055 -0.0140 -0.0032 34  LEU   A CG   
240  C  CD1  . LEU   A 30  ? 0.2286 0.1587 0.2040 -0.0102 -0.0094 -0.0125 34  LEU   A CD1  
241  C  CD2  . LEU   A 30  ? 0.2305 0.1751 0.2212 0.0049  -0.0134 -0.0018 34  LEU   A CD2  
242  N  N    . CYS   A 31  ? 0.1848 0.1155 0.1114 -0.0075 -0.0199 0.0003  35  CYS   A N    
243  C  CA   . CYS   A 31  ? 0.1840 0.1182 0.1180 -0.0098 -0.0169 -0.0013 35  CYS   A CA   
244  C  C    . CYS   A 31  ? 0.1848 0.1176 0.1112 -0.0110 -0.0172 -0.0029 35  CYS   A C    
245  O  O    . CYS   A 31  ? 0.1883 0.1090 0.1178 -0.0161 -0.0241 -0.0070 35  CYS   A O    
246  C  CB   . CYS   A 31  ? 0.1850 0.1399 0.1334 -0.0064 -0.0040 0.0005  35  CYS   A CB   
247  S  SG   . CYS   A 31  ? 0.2181 0.1730 0.2314 0.0142  0.0113  -0.0070 35  CYS   A SG   
248  N  N    . LEU   A 32  ? 0.1942 0.1144 0.1096 -0.0113 -0.0173 0.0016  36  LEU   A N    
249  C  CA   . LEU   A 32  ? 0.1928 0.1156 0.1154 -0.0082 -0.0142 0.0034  36  LEU   A CA   
250  C  C    . LEU   A 32  ? 0.1969 0.1152 0.1108 -0.0056 -0.0140 -0.0005 36  LEU   A C    
251  O  O    . LEU   A 32  ? 0.2120 0.1177 0.1084 0.0021  -0.0190 -0.0042 36  LEU   A O    
252  C  CB   . LEU   A 32  ? 0.1931 0.1291 0.1360 -0.0126 -0.0100 0.0008  36  LEU   A CB   
253  C  CG   . LEU   A 32  ? 0.1999 0.1564 0.1705 -0.0100 0.0000  -0.0055 36  LEU   A CG   
254  C  CD1  . LEU   A 32  ? 0.2240 0.1831 0.1848 -0.0141 -0.0042 -0.0016 36  LEU   A CD1  
255  C  CD2  . LEU   A 32  ? 0.2164 0.1765 0.2011 -0.0181 -0.0032 -0.0147 36  LEU   A CD2  
256  N  N    A LEU   A 33  ? 0.1926 0.1109 0.1159 -0.0064 -0.0142 0.0017  37  LEU   A N    
257  N  N    B LEU   A 33  ? 0.1956 0.1073 0.1127 -0.0066 -0.0134 0.0008  37  LEU   A N    
258  C  CA   A LEU   A 33  ? 0.1927 0.1217 0.1244 -0.0023 -0.0106 0.0012  37  LEU   A CA   
259  C  CA   B LEU   A 33  ? 0.1984 0.1162 0.1187 -0.0028 -0.0096 -0.0002 37  LEU   A CA   
260  C  C    A LEU   A 33  ? 0.1855 0.1153 0.1194 -0.0015 -0.0112 0.0000  37  LEU   A C    
261  C  C    B LEU   A 33  ? 0.1897 0.1129 0.1155 -0.0024 -0.0102 -0.0005 37  LEU   A C    
262  O  O    A LEU   A 33  ? 0.1858 0.1122 0.1216 -0.0046 -0.0119 -0.0065 37  LEU   A O    
263  O  O    B LEU   A 33  ? 0.1947 0.1121 0.1164 -0.0075 -0.0105 -0.0056 37  LEU   A O    
264  C  CB   A LEU   A 33  ? 0.1965 0.1391 0.1432 -0.0029 -0.0098 0.0040  37  LEU   A CB   
265  C  CB   B LEU   A 33  ? 0.2041 0.1273 0.1335 -0.0030 -0.0081 0.0009  37  LEU   A CB   
266  C  CG   A LEU   A 33  ? 0.2044 0.1594 0.1614 0.0073  -0.0129 0.0111  37  LEU   A CG   
267  C  CG   B LEU   A 33  ? 0.2146 0.1437 0.1439 0.0064  -0.0095 0.0047  37  LEU   A CG   
268  C  CD1  A LEU   A 33  ? 0.2048 0.1595 0.1732 0.0137  -0.0121 0.0032  37  LEU   A CD1  
269  C  CD1  B LEU   A 33  ? 0.2191 0.1478 0.1378 0.0044  -0.0065 0.0069  37  LEU   A CD1  
270  C  CD2  A LEU   A 33  ? 0.2107 0.1776 0.1702 0.0040  -0.0170 0.0096  37  LEU   A CD2  
271  C  CD2  B LEU   A 33  ? 0.2234 0.1419 0.1620 0.0098  -0.0072 0.0095  37  LEU   A CD2  
272  N  N    . ALA   A 34  ? 0.1844 0.1139 0.1178 -0.0029 -0.0074 0.0015  38  ALA   A N    
273  C  CA   . ALA   A 34  ? 0.1858 0.1238 0.1200 -0.0024 0.0008  0.0026  38  ALA   A CA   
274  C  C    . ALA   A 34  ? 0.1935 0.1195 0.1386 -0.0028 0.0076  0.0030  38  ALA   A C    
275  O  O    . ALA   A 34  ? 0.2066 0.1274 0.1404 0.0021  0.0081  -0.0009 38  ALA   A O    
276  C  CB   . ALA   A 34  ? 0.1927 0.1433 0.1364 -0.0045 0.0011  0.0060  38  ALA   A CB   
277  N  N    . VAL   A 35  ? 0.1966 0.1278 0.1442 -0.0051 0.0137  0.0137  39  VAL   A N    
278  C  CA   . VAL   A 35  ? 0.2055 0.1410 0.1616 -0.0003 0.0130  0.0142  39  VAL   A CA   
279  C  C    . VAL   A 35  ? 0.2052 0.1354 0.1460 0.0043  0.0078  0.0131  39  VAL   A C    
280  O  O    . VAL   A 35  ? 0.2125 0.1275 0.1561 0.0088  0.0112  0.0101  39  VAL   A O    
281  C  CB   . VAL   A 35  ? 0.2085 0.1771 0.1912 -0.0098 0.0156  0.0168  39  VAL   A CB   
282  C  CG1  . VAL   A 35  ? 0.2259 0.2035 0.2258 -0.0094 0.0143  0.0281  39  VAL   A CG1  
283  C  CG2  . VAL   A 35  ? 0.2156 0.1940 0.2090 -0.0189 0.0140  0.0183  39  VAL   A CG2  
284  N  N    . HIS   A 36  ? 0.2057 0.1336 0.1177 -0.0004 0.0157  0.0057  40  HIS   A N    
285  C  CA   . HIS   A 36  ? 0.2051 0.1326 0.1370 -0.0046 0.0207  0.0068  40  HIS   A CA   
286  C  C    . HIS   A 36  ? 0.1974 0.1332 0.1444 -0.0070 0.0180  0.0141  40  HIS   A C    
287  O  O    . HIS   A 36  ? 0.1873 0.1402 0.1456 -0.0025 0.0142  0.0211  40  HIS   A O    
288  C  CB   . HIS   A 36  ? 0.2204 0.1439 0.1414 -0.0109 0.0153  -0.0049 40  HIS   A CB   
289  C  CG   . HIS   A 36  ? 0.2326 0.1692 0.1479 -0.0154 0.0240  -0.0074 40  HIS   A CG   
290  N  ND1  . HIS   A 36  ? 0.2587 0.1786 0.1726 -0.0106 0.0312  0.0115  40  HIS   A ND1  
291  C  CD2  . HIS   A 36  ? 0.2468 0.2085 0.1682 -0.0279 0.0140  -0.0028 40  HIS   A CD2  
292  C  CE1  . HIS   A 36  ? 0.2512 0.2101 0.1890 -0.0161 0.0312  0.0109  40  HIS   A CE1  
293  N  NE2  . HIS   A 36  ? 0.2605 0.2148 0.1734 -0.0369 0.0146  0.0020  40  HIS   A NE2  
294  N  N    . ARG   A 37  ? 0.1931 0.1400 0.1375 -0.0070 0.0104  0.0138  41  ARG   A N    
295  C  CA   . ARG   A 37  ? 0.2012 0.1474 0.1428 -0.0065 0.0033  0.0191  41  ARG   A CA   
296  C  C    . ARG   A 37  ? 0.2076 0.1629 0.1544 -0.0029 0.0067  0.0224  41  ARG   A C    
297  O  O    . ARG   A 37  ? 0.2097 0.1923 0.1618 0.0007  -0.0057 0.0308  41  ARG   A O    
298  C  CB   . ARG   A 37  ? 0.2141 0.1526 0.1427 -0.0085 0.0049  0.0127  41  ARG   A CB   
299  C  CG   . ARG   A 37  ? 0.2220 0.1560 0.1476 -0.0115 0.0016  0.0175  41  ARG   A CG   
300  C  CD   . ARG   A 37  ? 0.2188 0.1648 0.1508 -0.0111 0.0012  0.0214  41  ARG   A CD   
301  N  NE   . ARG   A 37  ? 0.2185 0.1685 0.1563 -0.0117 -0.0034 0.0280  41  ARG   A NE   
302  C  CZ   . ARG   A 37  ? 0.2252 0.1816 0.1334 -0.0074 -0.0092 0.0249  41  ARG   A CZ   
303  N  NH1  . ARG   A 37  ? 0.2323 0.1829 0.1241 -0.0098 -0.0125 0.0174  41  ARG   A NH1  
304  N  NH2  . ARG   A 37  ? 0.2396 0.1912 0.1512 -0.0122 -0.0176 0.0282  41  ARG   A NH2  
305  N  N    . CYS   A 38  ? 0.2177 0.1579 0.1586 -0.0012 0.0134  0.0330  42  CYS   A N    
306  C  CA   . CYS   A 38  ? 0.2479 0.1808 0.1876 0.0132  0.0149  0.0361  42  CYS   A CA   
307  C  C    . CYS   A 38  ? 0.2478 0.1864 0.2034 0.0220  0.0189  0.0468  42  CYS   A C    
308  O  O    . CYS   A 38  ? 0.2590 0.2008 0.2330 0.0345  0.0124  0.0601  42  CYS   A O    
309  C  CB   . CYS   A 38  ? 0.2760 0.1759 0.1941 0.0138  0.0250  0.0273  42  CYS   A CB   
310  S  SG   . CYS   A 38  ? 0.3482 0.2374 0.2082 0.0298  0.0187  0.0099  42  CYS   A SG   
311  N  N    . ALA   A 39  ? 0.2368 0.1889 0.2065 0.0208  0.0303  0.0524  43  ALA   A N    
312  C  CA   . ALA   A 39  ? 0.2383 0.2080 0.2334 0.0176  0.0318  0.0573  43  ALA   A CA   
313  C  C    . ALA   A 39  ? 0.2309 0.2154 0.2572 0.0151  0.0231  0.0572  43  ALA   A C    
314  O  O    . ALA   A 39  ? 0.2307 0.2511 0.2925 0.0270  0.0270  0.0412  43  ALA   A O    
315  C  CB   . ALA   A 39  ? 0.2496 0.2241 0.2260 0.0125  0.0328  0.0603  43  ALA   A CB   
316  N  N    . LEU   A 40  ? 0.2201 0.2148 0.2628 0.0176  0.0213  0.0554  44  LEU   A N    
317  C  CA   . LEU   A 40  ? 0.2368 0.2239 0.2821 0.0131  0.0083  0.0673  44  LEU   A CA   
318  C  C    . LEU   A 40  ? 0.2290 0.2208 0.2762 0.0000  -0.0062 0.0689  44  LEU   A C    
319  O  O    . LEU   A 40  ? 0.2368 0.2390 0.2883 -0.0181 -0.0219 0.0786  44  LEU   A O    
320  C  CB   . LEU   A 40  ? 0.2677 0.2265 0.3194 0.0161  0.0253  0.0618  44  LEU   A CB   
321  C  CG   . LEU   A 40  ? 0.3225 0.2360 0.3725 0.0220  0.0416  0.0734  44  LEU   A CG   
322  C  CD1  . LEU   A 40  ? 0.3724 0.2574 0.4039 0.0295  0.0460  0.0666  44  LEU   A CD1  
323  C  CD2  . LEU   A 40  ? 0.3406 0.2679 0.4027 0.0103  0.0487  0.0661  44  LEU   A CD2  
324  N  N    . GLU   A 41  ? 0.2254 0.2112 0.2612 -0.0066 -0.0285 0.0694  45  GLU   A N    
325  C  CA   . GLU   A 41  ? 0.2426 0.2286 0.2679 -0.0214 -0.0208 0.0714  45  GLU   A CA   
326  C  C    . GLU   A 41  ? 0.2607 0.2422 0.2805 -0.0040 -0.0209 0.0875  45  GLU   A C    
327  O  O    . GLU   A 41  ? 0.2745 0.2877 0.2869 0.0001  -0.0292 0.0947  45  GLU   A O    
328  C  CB   . GLU   A 41  ? 0.2496 0.2176 0.2755 -0.0293 -0.0219 0.0729  45  GLU   A CB   
329  C  CG   . GLU   A 41  ? 0.2660 0.2107 0.2910 -0.0334 -0.0111 0.0685  45  GLU   A CG   
330  C  CD   . GLU   A 41  ? 0.2690 0.2033 0.3162 -0.0316 -0.0066 0.0727  45  GLU   A CD   
331  O  OE1  . GLU   A 41  ? 0.2902 0.2461 0.3439 -0.0247 0.0200  0.0617  45  GLU   A OE1  
332  O  OE2  . GLU   A 41  ? 0.2461 0.2181 0.3443 -0.0370 -0.0134 0.0898  45  GLU   A OE2  
333  N  N    . SER   A 42  ? 0.2916 0.2621 0.3030 0.0209  0.0000  0.0871  46  SER   A N    
334  C  CA   . SER   A 42  ? 0.3228 0.2871 0.3396 0.0465  0.0214  0.0942  46  SER   A CA   
335  C  C    . SER   A 42  ? 0.3278 0.3375 0.3816 0.0840  0.0497  0.0871  46  SER   A C    
336  O  O    . SER   A 42  ? 0.3287 0.3557 0.3819 0.1117  0.0361  0.0836  46  SER   A O    
337  C  CB   . SER   A 42  ? 0.3602 0.2855 0.3480 0.0439  0.0263  0.0790  46  SER   A CB   
338  O  OG   . SER   A 42  ? 0.4090 0.2660 0.3501 0.0286  0.0339  0.0890  46  SER   A OG   
339  N  N    . PRO   A 43  ? 0.3465 0.3938 0.4499 0.0858  0.0726  0.1126  47  PRO   A N    
340  C  CA   . PRO   A 43  ? 0.3618 0.4238 0.4815 0.1062  0.0891  0.1510  47  PRO   A CA   
341  C  C    . PRO   A 43  ? 0.4056 0.4719 0.5338 0.1556  0.0888  0.1637  47  PRO   A C    
342  O  O    . PRO   A 43  ? 0.4246 0.4458 0.5283 0.1314  0.1160  0.2119  47  PRO   A O    
343  C  CB   . PRO   A 43  ? 0.3628 0.4182 0.5000 0.1078  0.0784  0.1343  47  PRO   A CB   
344  C  CG   . PRO   A 43  ? 0.3650 0.4299 0.5071 0.0759  0.0919  0.1192  47  PRO   A CG   
345  C  CD   . PRO   A 43  ? 0.3453 0.4212 0.4820 0.0776  0.0849  0.1116  47  PRO   A CD   
346  N  N    . PRO   A 44  ? 0.4856 0.5624 0.5654 0.1913  0.0889  0.1675  48  PRO   A N    
347  C  CA   . PRO   A 44  ? 0.5383 0.6134 0.6290 0.1945  0.0977  0.1304  48  PRO   A CA   
348  C  C    . PRO   A 44  ? 0.5412 0.6779 0.6867 0.1498  0.1147  0.1350  48  PRO   A C    
349  O  O    . PRO   A 44  ? 0.5186 0.6838 0.7597 0.1399  0.1337  0.1603  48  PRO   A O    
350  C  CB   . PRO   A 44  ? 0.5654 0.6403 0.6323 0.1909  0.0959  0.1325  48  PRO   A CB   
351  C  CG   . PRO   A 44  ? 0.5680 0.6252 0.6175 0.1910  0.0746  0.1397  48  PRO   A CG   
352  C  CD   . PRO   A 44  ? 0.5381 0.6128 0.5998 0.1983  0.0680  0.1576  48  PRO   A CD   
353  N  N    . PRO   A 50  ? 0.6836 0.8129 1.2639 0.0594  -0.2047 -0.0312 54  PRO   A N    
354  C  CA   . PRO   A 50  ? 0.6123 0.7588 1.2451 0.0602  -0.2169 -0.0203 54  PRO   A CA   
355  C  C    . PRO   A 50  ? 0.5103 0.7200 1.1944 0.0953  -0.2332 -0.0266 54  PRO   A C    
356  O  O    . PRO   A 50  ? 0.4927 0.6985 1.2276 0.1019  -0.2153 -0.0324 54  PRO   A O    
357  C  CB   . PRO   A 50  ? 0.6071 0.7974 1.2544 0.0683  -0.2119 -0.0226 54  PRO   A CB   
358  C  CG   . PRO   A 50  ? 0.6521 0.8293 1.2615 0.0589  -0.2073 -0.0273 54  PRO   A CG   
359  C  CD   . PRO   A 50  ? 0.6422 0.8219 1.2643 0.0591  -0.2095 -0.0313 54  PRO   A CD   
360  N  N    . PRO   A 51  ? 0.4719 0.6559 1.1383 0.0977  -0.1872 -0.0344 55  PRO   A N    
361  C  CA   . PRO   A 51  ? 0.4351 0.6439 1.0867 0.0973  -0.1694 -0.0495 55  PRO   A CA   
362  C  C    . PRO   A 51  ? 0.3952 0.6061 1.0268 0.0896  -0.1417 -0.0332 55  PRO   A C    
363  O  O    . PRO   A 51  ? 0.4252 0.6222 0.9884 0.1251  -0.1433 -0.0441 55  PRO   A O    
364  C  CB   . PRO   A 51  ? 0.4827 0.6501 1.0918 0.1120  -0.1781 -0.0334 55  PRO   A CB   
365  C  CG   . PRO   A 51  ? 0.4684 0.6439 1.1055 0.1069  -0.1883 -0.0396 55  PRO   A CG   
366  C  CD   . PRO   A 51  ? 0.4824 0.6428 1.1175 0.0918  -0.1915 -0.0315 55  PRO   A CD   
367  N  N    . THR   A 52  ? 0.3138 0.5943 0.9663 0.0830  -0.1297 -0.0512 56  THR   A N    
368  C  CA   . THR   A 52  ? 0.3251 0.5853 0.9186 0.0597  -0.1030 -0.0437 56  THR   A CA   
369  C  C    . THR   A 52  ? 0.3316 0.5120 0.7832 0.0748  -0.1012 -0.0389 56  THR   A C    
370  O  O    . THR   A 52  ? 0.3862 0.5465 0.7574 0.0986  -0.1271 -0.0399 56  THR   A O    
371  C  CB   . THR   A 52  ? 0.3563 0.6122 0.9698 0.0350  -0.0937 -0.0378 56  THR   A CB   
372  O  OG1  . THR   A 52  ? 0.3884 0.6736 0.9967 0.0431  -0.0748 -0.0261 56  THR   A OG1  
373  C  CG2  . THR   A 52  ? 0.3336 0.6350 0.9897 0.0112  -0.0953 -0.0455 56  THR   A CG2  
374  N  N    . VAL   A 53  ? 0.2534 0.4323 0.7181 0.0284  -0.0678 -0.0441 57  VAL   A N    
375  C  CA   . VAL   A 53  ? 0.2433 0.3814 0.6656 0.0080  -0.0699 -0.0406 57  VAL   A CA   
376  C  C    . VAL   A 53  ? 0.2469 0.3598 0.6099 0.0164  -0.0646 -0.0352 57  VAL   A C    
377  O  O    . VAL   A 53  ? 0.2682 0.3646 0.6021 0.0533  -0.0744 -0.0325 57  VAL   A O    
378  C  CB   . VAL   A 53  ? 0.2456 0.3752 0.6666 -0.0037 -0.0569 -0.0407 57  VAL   A CB   
379  C  CG1  . VAL   A 53  ? 0.2361 0.3633 0.6706 -0.0073 -0.0647 -0.0361 57  VAL   A CG1  
380  C  CG2  . VAL   A 53  ? 0.2699 0.3747 0.6894 -0.0072 -0.0362 -0.0364 57  VAL   A CG2  
381  N  N    . PRO   A 54  ? 0.2338 0.3668 0.5871 -0.0005 -0.0780 -0.0212 58  PRO   A N    
382  C  CA   . PRO   A 54  ? 0.2398 0.3564 0.5565 0.0034  -0.0769 -0.0103 58  PRO   A CA   
383  C  C    . PRO   A 54  ? 0.2541 0.3495 0.5317 -0.0051 -0.0593 -0.0292 58  PRO   A C    
384  O  O    . PRO   A 54  ? 0.2161 0.3477 0.5050 -0.0077 -0.0630 -0.0240 58  PRO   A O    
385  C  CB   . PRO   A 54  ? 0.2632 0.4068 0.5753 -0.0140 -0.0744 -0.0056 58  PRO   A CB   
386  C  CG   . PRO   A 54  ? 0.2805 0.4089 0.5845 -0.0208 -0.0718 -0.0102 58  PRO   A CG   
387  C  CD   . PRO   A 54  ? 0.2519 0.3931 0.5830 -0.0126 -0.0710 -0.0118 58  PRO   A CD   
388  N  N    . PRO   A 55  ? 0.2826 0.3666 0.5121 0.0051  -0.0479 -0.0404 59  PRO   A N    
389  C  CA   . PRO   A 55  ? 0.2718 0.3671 0.4853 -0.0022 -0.0196 -0.0443 59  PRO   A CA   
390  C  C    . PRO   A 55  ? 0.2669 0.3245 0.4032 -0.0169 -0.0109 -0.0470 59  PRO   A C    
391  O  O    . PRO   A 55  ? 0.2656 0.2967 0.3820 -0.0196 -0.0185 -0.0720 59  PRO   A O    
392  C  CB   . PRO   A 55  ? 0.3056 0.3737 0.5084 0.0052  -0.0265 -0.0465 59  PRO   A CB   
393  C  CG   . PRO   A 55  ? 0.3313 0.3734 0.5239 0.0059  -0.0363 -0.0437 59  PRO   A CG   
394  C  CD   . PRO   A 55  ? 0.3197 0.3747 0.5313 0.0081  -0.0502 -0.0383 59  PRO   A CD   
395  N  N    . PRO   A 56  ? 0.2746 0.2912 0.3565 -0.0225 0.0156  -0.0290 60  PRO   A N    
396  C  CA   . PRO   A 56  ? 0.2630 0.2601 0.3198 -0.0166 0.0064  -0.0200 60  PRO   A CA   
397  C  C    . PRO   A 56  ? 0.2215 0.2279 0.2621 0.0045  0.0027  -0.0244 60  PRO   A C    
398  O  O    . PRO   A 56  ? 0.1983 0.2314 0.2766 -0.0070 0.0148  -0.0327 60  PRO   A O    
399  C  CB   . PRO   A 56  ? 0.3012 0.2881 0.3414 -0.0089 0.0158  -0.0028 60  PRO   A CB   
400  C  CG   . PRO   A 56  ? 0.3183 0.3327 0.3727 -0.0075 0.0252  -0.0071 60  PRO   A CG   
401  C  CD   . PRO   A 56  ? 0.3079 0.3220 0.3735 -0.0280 0.0167  -0.0124 60  PRO   A CD   
402  N  N    . PRO   A 57  ? 0.2206 0.2127 0.2071 0.0094  0.0007  -0.0188 61  PRO   A N    
403  C  CA   . PRO   A 57  ? 0.2163 0.2044 0.2063 0.0097  0.0079  -0.0052 61  PRO   A CA   
404  C  C    . PRO   A 57  ? 0.2185 0.1955 0.2013 0.0155  0.0070  -0.0012 61  PRO   A C    
405  O  O    . PRO   A 57  ? 0.2395 0.2003 0.1918 0.0119  0.0169  0.0050  61  PRO   A O    
406  C  CB   . PRO   A 57  ? 0.2255 0.2299 0.2071 0.0066  0.0108  -0.0070 61  PRO   A CB   
407  C  CG   . PRO   A 57  ? 0.2274 0.2286 0.2216 0.0078  0.0115  -0.0111 61  PRO   A CG   
408  C  CD   . PRO   A 57  ? 0.2292 0.2169 0.2140 0.0105  0.0075  -0.0142 61  PRO   A CD   
409  N  N    . ARG   A 58  ? 0.2150 0.1795 0.1941 0.0169  -0.0009 0.0084  62  ARG   A N    
410  C  CA   . ARG   A 58  ? 0.2205 0.1800 0.1938 0.0157  0.0002  0.0014  62  ARG   A CA   
411  C  C    . ARG   A 58  ? 0.2177 0.1644 0.1781 0.0163  0.0027  -0.0047 62  ARG   A C    
412  O  O    . ARG   A 58  ? 0.2088 0.1680 0.1814 0.0145  0.0045  0.0024  62  ARG   A O    
413  C  CB   . ARG   A 58  ? 0.2261 0.1822 0.2080 0.0210  0.0026  0.0016  62  ARG   A CB   
414  C  CG   . ARG   A 58  ? 0.2333 0.1805 0.2127 0.0235  0.0039  0.0021  62  ARG   A CG   
415  C  CD   . ARG   A 58  ? 0.2351 0.1898 0.2160 0.0230  0.0032  0.0025  62  ARG   A CD   
416  N  NE   . ARG   A 58  ? 0.2362 0.1640 0.2122 0.0153  0.0026  -0.0043 62  ARG   A NE   
417  C  CZ   . ARG   A 58  ? 0.2200 0.1550 0.1859 0.0025  0.0076  -0.0027 62  ARG   A CZ   
418  N  NH1  . ARG   A 58  ? 0.2306 0.1483 0.1760 0.0077  0.0063  0.0005  62  ARG   A NH1  
419  N  NH2  . ARG   A 58  ? 0.2116 0.1551 0.1811 -0.0030 0.0061  -0.0033 62  ARG   A NH2  
420  N  N    . VAL   A 59  ? 0.2078 0.1662 0.1578 0.0199  0.0002  -0.0039 63  VAL   A N    
421  C  CA   . VAL   A 59  ? 0.2188 0.1632 0.1507 0.0235  0.0032  -0.0058 63  VAL   A CA   
422  C  C    . VAL   A 59  ? 0.2262 0.1632 0.1471 0.0315  0.0055  -0.0032 63  VAL   A C    
423  O  O    . VAL   A 59  ? 0.2832 0.1782 0.1529 0.0531  -0.0051 -0.0035 63  VAL   A O    
424  C  CB   . VAL   A 59  ? 0.2260 0.1769 0.1600 0.0147  0.0118  -0.0054 63  VAL   A CB   
425  C  CG1  . VAL   A 59  ? 0.2261 0.1836 0.1620 0.0140  0.0083  -0.0034 63  VAL   A CG1  
426  C  CG2  . VAL   A 59  ? 0.2371 0.1770 0.1896 0.0135  0.0104  -0.0019 63  VAL   A CG2  
427  N  N    . VAL   A 60  ? 0.2225 0.1513 0.1496 0.0311  0.0016  -0.0079 64  VAL   A N    
428  C  CA   . VAL   A 60  ? 0.2324 0.1479 0.1614 0.0248  -0.0072 -0.0115 64  VAL   A CA   
429  C  C    . VAL   A 60  ? 0.2300 0.1392 0.1443 0.0215  -0.0007 -0.0054 64  VAL   A C    
430  O  O    . VAL   A 60  ? 0.2614 0.1657 0.1463 0.0313  -0.0128 -0.0153 64  VAL   A O    
431  C  CB   . VAL   A 60  ? 0.2520 0.1720 0.2113 0.0122  -0.0181 -0.0179 64  VAL   A CB   
432  C  CG1  . VAL   A 60  ? 0.2643 0.1896 0.2323 0.0068  -0.0342 -0.0291 64  VAL   A CG1  
433  C  CG2  . VAL   A 60  ? 0.2673 0.1932 0.2376 0.0007  -0.0066 -0.0280 64  VAL   A CG2  
434  N  N    . ASP   A 61  ? 0.2088 0.1240 0.1268 0.0101  0.0035  0.0043  65  ASP   A N    
435  C  CA   . ASP   A 61  ? 0.2042 0.1194 0.1144 0.0043  0.0000  -0.0013 65  ASP   A CA   
436  C  C    . ASP   A 61  ? 0.2023 0.1198 0.1206 0.0017  -0.0011 -0.0068 65  ASP   A C    
437  O  O    . ASP   A 61  ? 0.2211 0.1176 0.1232 -0.0036 -0.0034 -0.0071 65  ASP   A O    
438  C  CB   . ASP   A 61  ? 0.2078 0.1346 0.1256 0.0045  0.0000  -0.0040 65  ASP   A CB   
439  C  CG   . ASP   A 61  ? 0.2174 0.1559 0.1463 -0.0011 0.0071  -0.0083 65  ASP   A CG   
440  O  OD1  . ASP   A 61  ? 0.2180 0.1928 0.1433 -0.0060 0.0237  -0.0302 65  ASP   A OD1  
441  O  OD2  . ASP   A 61  ? 0.2188 0.1844 0.1715 -0.0003 0.0061  -0.0057 65  ASP   A OD2  
442  N  N    . LYS   A 62  ? 0.1980 0.1120 0.1162 0.0008  -0.0015 -0.0113 66  LYS   A N    
443  C  CA   . LYS   A 62  ? 0.2123 0.1131 0.1287 -0.0012 0.0036  -0.0096 66  LYS   A CA   
444  C  C    . LYS   A 62  ? 0.2208 0.1088 0.1175 -0.0049 -0.0010 -0.0075 66  LYS   A C    
445  O  O    . LYS   A 62  ? 0.2403 0.1105 0.1250 -0.0007 -0.0095 -0.0127 66  LYS   A O    
446  C  CB   . LYS   A 62  ? 0.2372 0.1523 0.1900 -0.0100 0.0200  -0.0134 66  LYS   A CB   
447  C  CG   . LYS   A 62  ? 0.2622 0.1839 0.2522 -0.0167 0.0330  -0.0038 66  LYS   A CG   
448  C  CD   . LYS   A 62  ? 0.2718 0.2436 0.2874 -0.0388 0.0462  0.0025  66  LYS   A CD   
449  C  CE   . LYS   A 62  ? 0.2887 0.2808 0.2925 -0.0330 0.0470  -0.0154 66  LYS   A CE   
450  N  NZ   . LYS   A 62  ? 0.2747 0.2886 0.2941 -0.0501 0.0357  -0.0312 66  LYS   A NZ   
451  N  N    . LEU   A 63  ? 0.2272 0.1110 0.1079 -0.0015 -0.0029 -0.0039 67  LEU   A N    
452  C  CA   . LEU   A 63  ? 0.2363 0.1104 0.1131 -0.0050 -0.0088 -0.0019 67  LEU   A CA   
453  C  C    . LEU   A 63  ? 0.2473 0.1079 0.1096 -0.0079 -0.0103 -0.0045 67  LEU   A C    
454  O  O    . LEU   A 63  ? 0.2912 0.1247 0.1115 -0.0284 -0.0180 -0.0044 67  LEU   A O    
455  C  CB   . LEU   A 63  ? 0.2379 0.1338 0.1338 -0.0072 -0.0106 0.0032  67  LEU   A CB   
456  C  CG   . LEU   A 63  ? 0.2384 0.1563 0.1501 0.0035  -0.0038 0.0118  67  LEU   A CG   
457  C  CD1  . LEU   A 63  ? 0.2340 0.1532 0.1532 -0.0005 -0.0086 0.0086  67  LEU   A CD1  
458  C  CD2  . LEU   A 63  ? 0.2547 0.1956 0.1810 0.0164  0.0018  0.0204  67  LEU   A CD2  
459  N  N    . SER   A 64  ? 0.2485 0.1059 0.1060 -0.0022 -0.0142 -0.0052 68  SER   A N    
460  C  CA   . SER   A 64  ? 0.2510 0.1141 0.1250 -0.0012 -0.0141 -0.0026 68  SER   A CA   
461  C  C    . SER   A 64  ? 0.2546 0.1120 0.1181 -0.0010 -0.0172 -0.0062 68  SER   A C    
462  O  O    . SER   A 64  ? 0.2897 0.1023 0.1240 0.0116  -0.0093 -0.0174 68  SER   A O    
463  C  CB   . SER   A 64  ? 0.2697 0.1567 0.1841 -0.0069 -0.0130 -0.0062 68  SER   A CB   
464  O  OG   . SER   A 64  ? 0.3119 0.2040 0.2607 -0.0318 -0.0140 -0.0057 68  SER   A OG   
465  N  N    . LEU   A 65  ? 0.2440 0.1130 0.1103 -0.0012 -0.0208 -0.0036 69  LEU   A N    
466  C  CA   . LEU   A 65  ? 0.2315 0.1242 0.1269 -0.0028 -0.0263 -0.0029 69  LEU   A CA   
467  C  C    . LEU   A 65  ? 0.2190 0.1211 0.1170 0.0010  -0.0231 -0.0037 69  LEU   A C    
468  O  O    . LEU   A 65  ? 0.2211 0.1164 0.1164 -0.0029 -0.0177 -0.0060 69  LEU   A O    
469  C  CB   . LEU   A 65  ? 0.2413 0.1577 0.1470 -0.0058 -0.0211 -0.0026 69  LEU   A CB   
470  C  CG   . LEU   A 65  ? 0.2568 0.1818 0.1802 -0.0208 -0.0170 -0.0057 69  LEU   A CG   
471  C  CD1  . LEU   A 65  ? 0.2581 0.1928 0.2102 -0.0264 -0.0174 -0.0081 69  LEU   A CD1  
472  C  CD2  . LEU   A 65  ? 0.2733 0.1946 0.1864 -0.0417 -0.0263 -0.0095 69  LEU   A CD2  
473  N  N    . CYS   A 66  ? 0.1963 0.1213 0.1183 0.0028  -0.0221 -0.0024 70  CYS   A N    
474  C  CA   . CYS   A 66  ? 0.1948 0.1247 0.1259 0.0071  -0.0269 -0.0020 70  CYS   A CA   
475  C  C    . CYS   A 66  ? 0.1879 0.1270 0.1325 0.0031  -0.0282 -0.0104 70  CYS   A C    
476  O  O    . CYS   A 66  ? 0.1958 0.1256 0.1528 0.0097  -0.0343 -0.0243 70  CYS   A O    
477  C  CB   . CYS   A 66  ? 0.2025 0.1475 0.1367 0.0017  -0.0241 0.0040  70  CYS   A CB   
478  S  SG   . CYS   A 66  ? 0.2128 0.2063 0.1783 0.0035  -0.0136 0.0248  70  CYS   A SG   
479  N  N    . VAL   A 67  ? 0.1812 0.1290 0.1338 0.0068  -0.0270 -0.0149 71  VAL   A N    
480  C  CA   . VAL   A 67  ? 0.1872 0.1342 0.1451 0.0086  -0.0228 -0.0178 71  VAL   A CA   
481  C  C    . VAL   A 67  ? 0.1894 0.1327 0.1610 0.0134  -0.0258 -0.0204 71  VAL   A C    
482  O  O    . VAL   A 67  ? 0.1854 0.1341 0.1760 0.0090  -0.0333 -0.0082 71  VAL   A O    
483  C  CB   . VAL   A 67  ? 0.1955 0.1448 0.1552 0.0030  -0.0097 -0.0185 71  VAL   A CB   
484  C  CG1  . VAL   A 67  ? 0.2035 0.1662 0.1705 0.0072  -0.0095 -0.0207 71  VAL   A CG1  
485  C  CG2  . VAL   A 67  ? 0.1956 0.1486 0.1521 -0.0017 -0.0095 -0.0192 71  VAL   A CG2  
486  N  N    . ALA   A 68  ? 0.2034 0.1428 0.1700 0.0147  -0.0371 -0.0163 72  ALA   A N    
487  C  CA   . ALA   A 68  ? 0.2164 0.1438 0.1775 0.0256  -0.0337 -0.0202 72  ALA   A CA   
488  C  C    . ALA   A 68  ? 0.2012 0.1385 0.1802 0.0171  -0.0229 -0.0152 72  ALA   A C    
489  O  O    . ALA   A 68  ? 0.1990 0.1627 0.2135 0.0055  -0.0245 -0.0322 72  ALA   A O    
490  C  CB   . ALA   A 68  ? 0.2411 0.1688 0.1911 0.0337  -0.0436 -0.0271 72  ALA   A CB   
491  N  N    . PRO   A 69  ? 0.1946 0.1317 0.1550 0.0251  -0.0240 -0.0081 73  PRO   A N    
492  C  CA   . PRO   A 69  ? 0.1918 0.1373 0.1616 0.0197  -0.0153 -0.0077 73  PRO   A CA   
493  C  C    . PRO   A 69  ? 0.1918 0.1416 0.1488 0.0215  -0.0165 -0.0048 73  PRO   A C    
494  O  O    . PRO   A 69  ? 0.2050 0.1554 0.1550 0.0215  -0.0109 0.0003  73  PRO   A O    
495  C  CB   . PRO   A 69  ? 0.1965 0.1363 0.1571 0.0199  -0.0203 -0.0092 73  PRO   A CB   
496  C  CG   . PRO   A 69  ? 0.2039 0.1336 0.1657 0.0171  -0.0196 -0.0105 73  PRO   A CG   
497  C  CD   . PRO   A 69  ? 0.2006 0.1402 0.1561 0.0163  -0.0200 -0.0137 73  PRO   A CD   
498  N  N    . GLY   A 70  ? 0.1962 0.1519 0.1478 0.0241  -0.0162 -0.0047 74  GLY   A N    
499  C  CA   . GLY   A 70  ? 0.1912 0.1534 0.1457 0.0236  -0.0208 -0.0012 74  GLY   A CA   
500  C  C    . GLY   A 70  ? 0.1924 0.1469 0.1400 0.0271  -0.0177 0.0007  74  GLY   A C    
501  O  O    . GLY   A 70  ? 0.1982 0.1585 0.1443 0.0354  -0.0224 0.0090  74  GLY   A O    
502  N  N    . LYS   A 71  ? 0.1869 0.1353 0.1527 0.0224  -0.0157 0.0073  75  LYS   A N    
503  C  CA   . LYS   A 71  ? 0.1900 0.1394 0.1539 0.0199  -0.0150 0.0026  75  LYS   A CA   
504  C  C    . LYS   A 71  ? 0.1894 0.1344 0.1552 0.0218  -0.0171 0.0041  75  LYS   A C    
505  O  O    . LYS   A 71  ? 0.1857 0.1310 0.1552 0.0284  -0.0144 0.0045  75  LYS   A O    
506  C  CB   . LYS   A 71  ? 0.1945 0.1500 0.1578 0.0161  -0.0150 -0.0009 75  LYS   A CB   
507  C  CG   . LYS   A 71  ? 0.2108 0.1619 0.1701 0.0244  -0.0188 0.0017  75  LYS   A CG   
508  C  CD   . LYS   A 71  ? 0.2356 0.1936 0.1833 0.0293  -0.0238 -0.0043 75  LYS   A CD   
509  C  CE   . LYS   A 71  ? 0.2688 0.2107 0.2176 0.0335  -0.0282 -0.0161 75  LYS   A CE   
510  N  NZ   . LYS   A 71  ? 0.2884 0.2335 0.2242 0.0437  -0.0386 -0.0108 75  LYS   A NZ   
511  N  N    . ALA   A 72  ? 0.1993 0.1382 0.1599 0.0195  -0.0180 0.0026  76  ALA   A N    
512  C  CA   . ALA   A 72  ? 0.1949 0.1480 0.1658 0.0135  -0.0134 -0.0002 76  ALA   A CA   
513  C  C    . ALA   A 72  ? 0.1978 0.1546 0.1645 0.0096  -0.0126 -0.0017 76  ALA   A C    
514  O  O    . ALA   A 72  ? 0.2026 0.1738 0.1755 0.0213  -0.0054 -0.0060 76  ALA   A O    
515  C  CB   . ALA   A 72  ? 0.2094 0.1572 0.1817 0.0138  -0.0086 0.0096  76  ALA   A CB   
516  N  N    . CYS   A 73  ? 0.1895 0.1526 0.1486 0.0060  -0.0151 -0.0111 77  CYS   A N    
517  C  CA   . CYS   A 73  ? 0.1829 0.1588 0.1574 -0.0009 -0.0127 -0.0093 77  CYS   A CA   
518  C  C    . CYS   A 73  ? 0.1968 0.1530 0.1840 -0.0022 -0.0041 -0.0118 77  CYS   A C    
519  O  O    . CYS   A 73  ? 0.2198 0.1709 0.1996 -0.0270 0.0000  0.0030  77  CYS   A O    
520  C  CB   . CYS   A 73  ? 0.1905 0.1613 0.1490 0.0001  -0.0143 -0.0068 77  CYS   A CB   
521  S  SG   . CYS   A 73  ? 0.2032 0.1676 0.1646 -0.0056 -0.0081 -0.0037 77  CYS   A SG   
522  N  N    . SER   A 74  ? 0.1924 0.1480 0.1885 -0.0143 -0.0031 -0.0286 78  SER   A N    
523  C  CA   . SER   A 74  ? 0.2144 0.1653 0.2166 -0.0286 -0.0039 -0.0341 78  SER   A CA   
524  C  C    . SER   A 74  ? 0.2138 0.1592 0.2266 -0.0289 -0.0045 -0.0417 78  SER   A C    
525  O  O    . SER   A 74  ? 0.2080 0.1510 0.2421 -0.0351 -0.0121 -0.0493 78  SER   A O    
526  C  CB   . SER   A 74  ? 0.2212 0.1961 0.2234 -0.0313 -0.0039 -0.0402 78  SER   A CB   
527  O  OG   . SER   A 74  ? 0.2225 0.2056 0.2079 -0.0239 -0.0065 -0.0384 78  SER   A OG   
528  N  N    . PRO   A 75  ? 0.2220 0.1706 0.2499 -0.0389 -0.0027 -0.0427 79  PRO   A N    
529  C  CA   . PRO   A 75  ? 0.2298 0.1859 0.2515 -0.0415 0.0072  -0.0484 79  PRO   A CA   
530  C  C    . PRO   A 75  ? 0.2048 0.1811 0.2193 -0.0458 0.0170  -0.0526 79  PRO   A C    
531  O  O    . PRO   A 75  ? 0.2297 0.1912 0.2314 -0.0406 0.0327  -0.0603 79  PRO   A O    
532  C  CB   . PRO   A 75  ? 0.2400 0.1891 0.2744 -0.0438 0.0054  -0.0305 79  PRO   A CB   
533  C  CG   . PRO   A 75  ? 0.2486 0.1923 0.2784 -0.0413 0.0050  -0.0400 79  PRO   A CG   
534  C  CD   . PRO   A 75  ? 0.2352 0.1775 0.2719 -0.0352 -0.0008 -0.0455 79  PRO   A CD   
535  N  N    . ALA   A 76  ? 0.2049 0.2024 0.2203 -0.0459 0.0175  -0.0570 80  ALA   A N    
536  C  CA   . ALA   A 76  ? 0.2076 0.2176 0.2112 -0.0448 0.0133  -0.0487 80  ALA   A CA   
537  C  C    . ALA   A 76  ? 0.2045 0.2219 0.2008 -0.0434 0.0045  -0.0314 80  ALA   A C    
538  O  O    . ALA   A 76  ? 0.2057 0.2422 0.2417 -0.0363 -0.0077 -0.0244 80  ALA   A O    
539  C  CB   . ALA   A 76  ? 0.2168 0.2222 0.2109 -0.0521 0.0120  -0.0497 80  ALA   A CB   
540  N  N    . ALA   A 77  ? 0.2012 0.2211 0.1763 -0.0321 -0.0040 -0.0220 81  ALA   A N    
541  C  CA   . ALA   A 77  ? 0.2039 0.2114 0.1787 -0.0337 -0.0059 -0.0108 81  ALA   A CA   
542  C  C    . ALA   A 77  ? 0.1997 0.1929 0.1859 -0.0309 -0.0087 -0.0122 81  ALA   A C    
543  O  O    . ALA   A 77  ? 0.2260 0.1977 0.2069 -0.0238 0.0007  0.0088  81  ALA   A O    
544  C  CB   . ALA   A 77  ? 0.2043 0.2214 0.1717 -0.0393 -0.0013 -0.0139 81  ALA   A CB   
545  N  N    . SER   A 78  ? 0.2056 0.1616 0.1970 -0.0376 -0.0029 -0.0176 82  SER   A N    
546  C  CA   . SER   A 78  ? 0.2053 0.1578 0.2014 -0.0335 -0.0042 -0.0233 82  SER   A CA   
547  C  C    . SER   A 78  ? 0.2103 0.1602 0.2165 -0.0308 -0.0008 -0.0227 82  SER   A C    
548  O  O    . SER   A 78  ? 0.2313 0.1717 0.2368 -0.0231 -0.0116 -0.0328 82  SER   A O    
549  C  CB   . SER   A 78  ? 0.2079 0.1584 0.1966 -0.0324 -0.0006 -0.0253 82  SER   A CB   
550  O  OG   . SER   A 78  ? 0.2177 0.1838 0.2062 -0.0246 -0.0022 -0.0234 82  SER   A OG   
551  N  N    . GLU   A 79  ? 0.2150 0.1649 0.2426 -0.0306 -0.0085 -0.0249 83  GLU   A N    
552  C  CA   . GLU   A 79  ? 0.2329 0.2020 0.2897 -0.0183 -0.0208 -0.0263 83  GLU   A CA   
553  C  C    . GLU   A 79  ? 0.2418 0.2248 0.3097 -0.0067 -0.0491 -0.0153 83  GLU   A C    
554  O  O    . GLU   A 79  ? 0.2830 0.2611 0.3408 0.0317  -0.0262 -0.0110 83  GLU   A O    
555  C  CB   . GLU   A 79  ? 0.2683 0.2271 0.3276 -0.0353 -0.0205 -0.0362 83  GLU   A CB   
556  C  CG   . GLU   A 79  ? 0.3375 0.2679 0.3707 -0.0453 -0.0127 -0.0351 83  GLU   A CG   
557  C  CD   . GLU   A 79  ? 0.3960 0.2755 0.4284 -0.0700 -0.0118 -0.0449 83  GLU   A CD   
558  O  OE1  . GLU   A 79  ? 0.4647 0.3230 0.4621 -0.0955 -0.0642 -0.0602 83  GLU   A OE1  
559  O  OE2  . GLU   A 79  ? 0.4768 0.3326 0.5098 -0.0703 0.0348  -0.0215 83  GLU   A OE2  
560  N  N    A ILE   A 80  ? 0.2420 0.2096 0.3066 -0.0075 -0.0606 0.0028  84  ILE   A N    
561  N  N    B ILE   A 80  ? 0.2399 0.2129 0.3127 -0.0135 -0.0613 -0.0032 84  ILE   A N    
562  C  CA   A ILE   A 80  ? 0.2724 0.2265 0.3304 0.0030  -0.0739 0.0154  84  ILE   A CA   
563  C  CA   B ILE   A 80  ? 0.2712 0.2288 0.3420 -0.0069 -0.0771 0.0070  84  ILE   A CA   
564  C  C    A ILE   A 80  ? 0.2814 0.2054 0.3493 0.0002  -0.0848 0.0284  84  ILE   A C    
565  C  C    B ILE   A 80  ? 0.2800 0.2053 0.3560 -0.0073 -0.0877 0.0236  84  ILE   A C    
566  O  O    A ILE   A 80  ? 0.3003 0.1939 0.4079 -0.0035 -0.1184 0.0168  84  ILE   A O    
567  O  O    B ILE   A 80  ? 0.3005 0.1932 0.4165 -0.0145 -0.1271 0.0133  84  ILE   A O    
568  C  CB   A ILE   A 80  ? 0.3006 0.2562 0.3399 0.0146  -0.0608 0.0329  84  ILE   A CB   
569  C  CB   B ILE   A 80  ? 0.2992 0.2632 0.3607 -0.0033 -0.0646 0.0145  84  ILE   A CB   
570  C  CG1  A ILE   A 80  ? 0.3257 0.2710 0.3437 0.0222  -0.0551 0.0431  84  ILE   A CG1  
571  C  CG1  B ILE   A 80  ? 0.3138 0.2766 0.3795 -0.0018 -0.0578 0.0123  84  ILE   A CG1  
572  C  CG2  A ILE   A 80  ? 0.3149 0.2700 0.3534 0.0155  -0.0555 0.0312  84  ILE   A CG2  
573  C  CG2  B ILE   A 80  ? 0.3181 0.2774 0.3764 -0.0123 -0.0655 0.0061  84  ILE   A CG2  
574  N  N    . THR   A 81  ? 0.2863 0.1735 0.3407 -0.0121 -0.0933 0.0243  85  THR   A N    
575  C  CA   . THR   A 81  ? 0.2944 0.1863 0.3124 -0.0115 -0.0900 0.0195  85  THR   A CA   
576  C  C    . THR   A 81  ? 0.2953 0.1736 0.2973 -0.0003 -0.0873 0.0079  85  THR   A C    
577  O  O    . THR   A 81  ? 0.3162 0.2047 0.3442 -0.0070 -0.0975 0.0174  85  THR   A O    
578  C  CB   . THR   A 81  ? 0.2892 0.1964 0.2926 -0.0304 -0.0840 0.0222  85  THR   A CB   
579  O  OG1  . THR   A 81  ? 0.2749 0.1750 0.2931 -0.0362 -0.0932 0.0245  85  THR   A OG1  
580  C  CG2  . THR   A 81  ? 0.3007 0.2121 0.3024 -0.0443 -0.0775 0.0292  85  THR   A CG2  
581  N  N    . GLY   A 82  ? 0.2578 0.1853 0.3073 -0.0059 -0.0673 -0.0195 86  GLY   A N    
582  C  CA   . GLY   A 82  ? 0.2455 0.1779 0.3070 0.0085  -0.0512 -0.0254 86  GLY   A CA   
583  C  C    . GLY   A 82  ? 0.2354 0.1763 0.2645 -0.0067 -0.0417 -0.0334 86  GLY   A C    
584  O  O    . GLY   A 82  ? 0.2492 0.2450 0.2902 -0.0091 -0.0270 -0.0414 86  GLY   A O    
585  N  N    . LEU   A 83  ? 0.2226 0.1638 0.2170 -0.0033 -0.0435 -0.0285 87  LEU   A N    
586  C  CA   . LEU   A 83  ? 0.2143 0.1531 0.1902 0.0035  -0.0358 -0.0219 87  LEU   A CA   
587  C  C    . LEU   A 83  ? 0.2154 0.1543 0.1704 0.0049  -0.0400 -0.0254 87  LEU   A C    
588  O  O    . LEU   A 83  ? 0.2360 0.1472 0.1987 -0.0004 -0.0613 -0.0270 87  LEU   A O    
589  C  CB   . LEU   A 83  ? 0.2148 0.1663 0.1998 0.0036  -0.0349 -0.0143 87  LEU   A CB   
590  C  CG   . LEU   A 83  ? 0.2056 0.1679 0.2074 0.0018  -0.0306 -0.0063 87  LEU   A CG   
591  C  CD1  . LEU   A 83  ? 0.2099 0.1797 0.2196 0.0009  -0.0294 0.0010  87  LEU   A CD1  
592  C  CD2  . LEU   A 83  ? 0.2100 0.1781 0.2183 0.0040  -0.0271 -0.0110 87  LEU   A CD2  
593  N  N    . SER   A 84  ? 0.2030 0.1530 0.1551 0.0008  -0.0299 -0.0179 88  SER   A N    
594  C  CA   . SER   A 84  ? 0.1973 0.1449 0.1474 -0.0048 -0.0195 -0.0097 88  SER   A CA   
595  C  C    . SER   A 84  ? 0.1977 0.1358 0.1456 0.0008  -0.0212 -0.0063 88  SER   A C    
596  O  O    . SER   A 84  ? 0.2001 0.1392 0.1407 -0.0028 -0.0146 -0.0073 88  SER   A O    
597  C  CB   . SER   A 84  ? 0.2116 0.1640 0.1613 -0.0204 -0.0157 -0.0138 88  SER   A CB   
598  O  OG   . SER   A 84  ? 0.2376 0.1904 0.1634 -0.0401 -0.0064 -0.0189 88  SER   A OG   
599  N  N    . THR   A 85  ? 0.1917 0.1368 0.1493 0.0032  -0.0147 -0.0041 89  THR   A N    
600  C  CA   . THR   A 85  ? 0.1948 0.1410 0.1478 0.0052  -0.0134 -0.0008 89  THR   A CA   
601  C  C    . THR   A 85  ? 0.2075 0.1324 0.1483 -0.0006 -0.0143 0.0056  89  THR   A C    
602  O  O    . THR   A 85  ? 0.2135 0.1400 0.1518 0.0072  -0.0228 -0.0020 89  THR   A O    
603  C  CB   . THR   A 85  ? 0.1996 0.1559 0.1478 0.0154  -0.0118 0.0004  89  THR   A CB   
604  O  OG1  . THR   A 85  ? 0.1907 0.1760 0.1481 0.0183  -0.0171 0.0017  89  THR   A OG1  
605  C  CG2  . THR   A 85  ? 0.2036 0.1589 0.1536 0.0120  -0.0062 0.0020  89  THR   A CG2  
606  N  N    . ALA   A 86  ? 0.2218 0.1368 0.1426 -0.0124 -0.0121 0.0033  90  ALA   A N    
607  C  CA   . ALA   A 86  ? 0.2444 0.1416 0.1427 -0.0247 -0.0113 0.0158  90  ALA   A CA   
608  C  C    . ALA   A 86  ? 0.2521 0.1488 0.1418 -0.0283 -0.0071 0.0098  90  ALA   A C    
609  O  O    . ALA   A 86  ? 0.2720 0.1555 0.1409 -0.0379 -0.0223 0.0075  90  ALA   A O    
610  C  CB   . ALA   A 86  ? 0.2600 0.1413 0.1445 -0.0303 -0.0086 0.0223  90  ALA   A CB   
611  N  N    . VAL   A 87  ? 0.2457 0.1510 0.1428 -0.0189 -0.0007 0.0010  91  VAL   A N    
612  C  CA   . VAL   A 87  ? 0.2501 0.1555 0.1684 -0.0170 0.0064  -0.0019 91  VAL   A CA   
613  C  C    . VAL   A 87  ? 0.2389 0.1395 0.1446 -0.0082 -0.0024 -0.0002 91  VAL   A C    
614  O  O    . VAL   A 87  ? 0.2416 0.1451 0.1370 -0.0236 -0.0157 0.0016  91  VAL   A O    
615  C  CB   . VAL   A 87  ? 0.2607 0.1811 0.2402 -0.0096 0.0118  -0.0141 91  VAL   A CB   
616  C  CG1  . VAL   A 87  ? 0.2677 0.1920 0.2880 -0.0092 0.0084  -0.0313 91  VAL   A CG1  
617  C  CG2  . VAL   A 87  ? 0.2680 0.2102 0.2563 -0.0121 0.0324  -0.0230 91  VAL   A CG2  
618  N  N    . LEU   A 88  ? 0.2227 0.1224 0.1224 -0.0074 -0.0116 -0.0052 92  LEU   A N    
619  C  CA   . LEU   A 88  ? 0.2201 0.1234 0.1246 -0.0008 -0.0141 0.0027  92  LEU   A CA   
620  C  C    . LEU   A 88  ? 0.2269 0.1308 0.1330 0.0009  -0.0217 0.0112  92  LEU   A C    
621  O  O    . LEU   A 88  ? 0.2380 0.1376 0.1215 0.0055  -0.0257 0.0106  92  LEU   A O    
622  C  CB   . LEU   A 88  ? 0.2108 0.1249 0.1272 -0.0021 -0.0108 0.0064  92  LEU   A CB   
623  C  CG   . LEU   A 88  ? 0.2091 0.1282 0.1355 0.0024  -0.0175 -0.0009 92  LEU   A CG   
624  C  CD1  . LEU   A 88  ? 0.2100 0.1281 0.1379 0.0059  -0.0147 -0.0004 92  LEU   A CD1  
625  C  CD2  . LEU   A 88  ? 0.2140 0.1329 0.1460 0.0046  -0.0192 0.0007  92  LEU   A CD2  
626  N  N    . ALA   A 89  ? 0.2289 0.1341 0.1406 0.0092  -0.0330 0.0130  93  ALA   A N    
627  C  CA   . ALA   A 89  ? 0.2399 0.1482 0.1617 0.0034  -0.0425 0.0162  93  ALA   A CA   
628  C  C    . ALA   A 89  ? 0.2427 0.1647 0.1551 -0.0037 -0.0409 0.0285  93  ALA   A C    
629  O  O    . ALA   A 89  ? 0.2550 0.1680 0.1660 -0.0250 -0.0416 0.0234  93  ALA   A O    
630  C  CB   . ALA   A 89  ? 0.2548 0.1631 0.1811 0.0224  -0.0493 0.0156  93  ALA   A CB   
631  N  N    . ALA   A 90  ? 0.2474 0.1779 0.1462 -0.0199 -0.0311 0.0278  94  ALA   A N    
632  C  CA   . ALA   A 90  ? 0.2581 0.2028 0.1393 -0.0194 -0.0291 0.0244  94  ALA   A CA   
633  C  C    . ALA   A 90  ? 0.2586 0.2004 0.1242 -0.0142 -0.0259 0.0061  94  ALA   A C    
634  O  O    . ALA   A 90  ? 0.3048 0.2238 0.1221 -0.0067 -0.0169 0.0023  94  ALA   A O    
635  C  CB   . ALA   A 90  ? 0.2662 0.2270 0.1603 -0.0216 -0.0259 0.0290  94  ALA   A CB   
636  N  N    . HIS   A 91  ? 0.2505 0.1719 0.1122 -0.0122 -0.0241 -0.0018 95  HIS   A N    
637  C  CA   . HIS   A 91  ? 0.2483 0.1692 0.1254 -0.0097 -0.0165 -0.0142 95  HIS   A CA   
638  C  C    . HIS   A 91  ? 0.2532 0.1675 0.1165 -0.0139 -0.0072 -0.0119 95  HIS   A C    
639  O  O    . HIS   A 91  ? 0.2761 0.1678 0.1289 -0.0175 0.0099  -0.0142 95  HIS   A O    
640  C  CB   . HIS   A 91  ? 0.2553 0.1807 0.1356 -0.0045 -0.0168 -0.0095 95  HIS   A CB   
641  C  CG   . HIS   A 91  ? 0.2505 0.2006 0.1555 0.0001  -0.0173 -0.0057 95  HIS   A CG   
642  N  ND1  . HIS   A 91  ? 0.2625 0.2275 0.2077 -0.0014 -0.0106 -0.0106 95  HIS   A ND1  
643  C  CD2  . HIS   A 91  ? 0.2594 0.2030 0.1826 0.0039  -0.0176 -0.0063 95  HIS   A CD2  
644  C  CE1  . HIS   A 91  ? 0.2567 0.2328 0.2222 -0.0039 -0.0129 -0.0112 95  HIS   A CE1  
645  N  NE2  . HIS   A 91  ? 0.2614 0.2376 0.2090 0.0102  -0.0107 -0.0107 95  HIS   A NE2  
646  N  N    . GLY   A 92  ? 0.2361 0.1730 0.1165 -0.0219 -0.0136 -0.0012 96  GLY   A N    
647  C  CA   . GLY   A 92  ? 0.2408 0.1857 0.1214 -0.0253 -0.0259 -0.0042 96  GLY   A CA   
648  C  C    . GLY   A 92  ? 0.2345 0.1910 0.1261 -0.0222 -0.0229 -0.0073 96  GLY   A C    
649  O  O    . GLY   A 92  ? 0.2506 0.2160 0.1564 -0.0326 -0.0273 -0.0098 96  GLY   A O    
650  N  N    . ARG   A 93  ? 0.2222 0.1739 0.1341 -0.0145 -0.0314 -0.0018 97  ARG   A N    
651  C  CA   . ARG   A 93  ? 0.2263 0.1836 0.1362 -0.0139 -0.0294 -0.0030 97  ARG   A CA   
652  C  C    . ARG   A 93  ? 0.2376 0.1836 0.1436 -0.0031 -0.0322 -0.0069 97  ARG   A C    
653  O  O    . ARG   A 93  ? 0.2638 0.1924 0.1733 0.0121  -0.0379 -0.0052 97  ARG   A O    
654  C  CB   . ARG   A 93  ? 0.2201 0.1797 0.1371 -0.0241 -0.0283 -0.0021 97  ARG   A CB   
655  C  CG   . ARG   A 93  ? 0.2220 0.1754 0.1470 -0.0271 -0.0296 0.0021  97  ARG   A CG   
656  C  CD   . ARG   A 93  ? 0.2274 0.1769 0.1541 -0.0266 -0.0268 0.0044  97  ARG   A CD   
657  N  NE   . ARG   A 93  ? 0.2312 0.1763 0.1551 -0.0345 -0.0233 0.0096  97  ARG   A NE   
658  C  CZ   . ARG   A 93  ? 0.2489 0.1783 0.1752 -0.0313 -0.0223 0.0065  97  ARG   A CZ   
659  N  NH1  . ARG   A 93  ? 0.2483 0.1778 0.1887 -0.0330 -0.0201 0.0115  97  ARG   A NH1  
660  N  NH2  . ARG   A 93  ? 0.2552 0.1848 0.1795 -0.0392 -0.0319 0.0117  97  ARG   A NH2  
661  N  N    . GLN   A 94  ? 0.2372 0.1922 0.1530 -0.0022 -0.0350 -0.0064 98  GLN   A N    
662  C  CA   . GLN   A 94  ? 0.2353 0.1998 0.1657 0.0087  -0.0379 -0.0132 98  GLN   A CA   
663  C  C    . GLN   A 94  ? 0.2060 0.2035 0.1695 0.0156  -0.0382 -0.0204 98  GLN   A C    
664  O  O    . GLN   A 94  ? 0.1965 0.1934 0.1625 0.0150  -0.0387 -0.0242 98  GLN   A O    
665  C  CB   . GLN   A 94  ? 0.2656 0.2149 0.2016 0.0030  -0.0419 -0.0244 98  GLN   A CB   
666  C  CG   . GLN   A 94  ? 0.2986 0.2517 0.2236 0.0000  -0.0507 -0.0281 98  GLN   A CG   
667  C  CD   . GLN   A 94  ? 0.3526 0.2574 0.2720 -0.0123 -0.0467 -0.0341 98  GLN   A CD   
668  O  OE1  . GLN   A 94  ? 0.4007 0.3218 0.3108 -0.0141 -0.0296 -0.0456 98  GLN   A OE1  
669  N  NE2  . GLN   A 94  ? 0.3762 0.2648 0.2783 0.0011  -0.0577 -0.0357 98  GLN   A NE2  
670  N  N    . CYS   A 95  ? 0.1993 0.2215 0.2004 0.0162  -0.0353 -0.0322 99  CYS   A N    
671  C  CA   . CYS   A 95  ? 0.2154 0.2282 0.2138 0.0214  -0.0232 -0.0334 99  CYS   A CA   
672  C  C    . CYS   A 95  ? 0.1935 0.1974 0.2343 0.0138  -0.0225 -0.0396 99  CYS   A C    
673  O  O    . CYS   A 95  ? 0.1981 0.1925 0.2228 0.0111  -0.0158 -0.0403 99  CYS   A O    
674  C  CB   . CYS   A 95  ? 0.2458 0.2484 0.2547 0.0375  -0.0168 -0.0261 99  CYS   A CB   
675  S  SG   . CYS   A 95  ? 0.2739 0.3040 0.3765 0.0490  -0.0311 -0.0010 99  CYS   A SG   
676  N  N    . PHE   A 96  ? 0.1881 0.1802 0.2349 0.0148  -0.0173 -0.0364 100 PHE   A N    
677  C  CA   . PHE   A 96  ? 0.1875 0.1803 0.2476 0.0006  -0.0162 -0.0360 100 PHE   A CA   
678  C  C    . PHE   A 96  ? 0.1907 0.1848 0.2860 0.0059  -0.0195 -0.0212 100 PHE   A C    
679  O  O    . PHE   A 96  ? 0.2045 0.2082 0.3961 0.0001  0.0005  -0.0554 100 PHE   A O    
680  C  CB   . PHE   A 96  ? 0.1965 0.1825 0.2376 -0.0105 -0.0119 -0.0386 100 PHE   A CB   
681  C  CG   . PHE   A 96  ? 0.1939 0.1914 0.2283 -0.0107 -0.0070 -0.0340 100 PHE   A CG   
682  C  CD1  . PHE   A 96  ? 0.2025 0.2218 0.2507 -0.0220 -0.0180 -0.0113 100 PHE   A CD1  
683  C  CD2  . PHE   A 96  ? 0.2035 0.2072 0.2312 -0.0141 -0.0059 -0.0295 100 PHE   A CD2  
684  C  CE1  . PHE   A 96  ? 0.2169 0.2221 0.2543 -0.0286 -0.0238 -0.0116 100 PHE   A CE1  
685  C  CE2  . PHE   A 96  ? 0.2156 0.2194 0.2271 -0.0096 -0.0124 -0.0307 100 PHE   A CE2  
686  C  CZ   . PHE   A 96  ? 0.2243 0.2243 0.2457 -0.0211 -0.0213 -0.0194 100 PHE   A CZ   
687  N  N    . ASP   A 97  ? 0.1878 0.1800 0.2537 0.0115  -0.0362 -0.0039 101 ASP   A N    
688  C  CA   . ASP   A 97  ? 0.1994 0.2093 0.2725 0.0104  -0.0478 0.0029  101 ASP   A CA   
689  C  C    . ASP   A 97  ? 0.1826 0.2150 0.2823 0.0078  -0.0577 0.0104  101 ASP   A C    
690  O  O    . ASP   A 97  ? 0.1817 0.1883 0.2521 0.0059  -0.0545 0.0041  101 ASP   A O    
691  C  CB   . ASP   A 97  ? 0.2440 0.2256 0.2753 0.0116  -0.0617 0.0209  101 ASP   A CB   
692  C  CG   . ASP   A 97  ? 0.2852 0.2612 0.2638 0.0078  -0.0653 0.0122  101 ASP   A CG   
693  O  OD1  . ASP   A 97  ? 0.2950 0.2343 0.2527 0.0059  -0.0739 -0.0012 101 ASP   A OD1  
694  O  OD2  . ASP   A 97  ? 0.3708 0.3344 0.2738 -0.0013 -0.0664 0.0267  101 ASP   A OD2  
695  N  N    . ASP   A 98  ? 0.1772 0.2222 0.3169 0.0096  -0.0648 0.0057  102 ASP   A N    
696  C  CA   . ASP   A 98  ? 0.1874 0.2346 0.3571 0.0014  -0.0590 0.0071  102 ASP   A CA   
697  C  C    . ASP   A 98  ? 0.1796 0.2350 0.3368 -0.0032 -0.0589 0.0034  102 ASP   A C    
698  O  O    . ASP   A 98  ? 0.1996 0.2227 0.3450 0.0027  -0.0388 0.0097  102 ASP   A O    
699  C  CB   . ASP   A 98  ? 0.1960 0.2713 0.4234 0.0014  -0.0713 -0.0045 102 ASP   A CB   
700  C  CG   . ASP   A 98  ? 0.2587 0.3364 0.4863 0.0118  -0.0578 -0.0259 102 ASP   A CG   
701  O  OD1  . ASP   A 98  ? 0.3043 0.4068 0.5061 0.0122  -0.0705 -0.0383 102 ASP   A OD1  
702  O  OD2  . ASP   A 98  ? 0.2988 0.4424 0.6001 0.0393  -0.0857 -0.0316 102 ASP   A OD2  
703  N  N    . ASN   A 99  ? 0.1872 0.2169 0.3109 0.0010  -0.0747 -0.0093 103 ASN   A N    
704  C  CA   . ASN   A 99  ? 0.2121 0.2183 0.3164 0.0063  -0.0742 -0.0116 103 ASN   A CA   
705  C  C    . ASN   A 99  ? 0.2049 0.1932 0.2828 -0.0036 -0.0668 -0.0106 103 ASN   A C    
706  O  O    . ASN   A 99  ? 0.2167 0.1794 0.2881 -0.0132 -0.0666 -0.0159 103 ASN   A O    
707  C  CB   . ASN   A 99  ? 0.2289 0.2264 0.3124 0.0130  -0.0872 -0.0134 103 ASN   A CB   
708  C  CG   . ASN   A 99  ? 0.2349 0.2324 0.3391 0.0147  -0.0796 -0.0237 103 ASN   A CG   
709  O  OD1  . ASN   A 99  ? 0.2525 0.2469 0.3652 0.0036  -0.0781 -0.0243 103 ASN   A OD1  
710  N  ND2  . ASN   A 99  ? 0.2251 0.2192 0.3524 0.0290  -0.0819 -0.0252 103 ASN   A ND2  
711  N  N    . LEU   A 100 ? 0.1947 0.1844 0.2551 -0.0016 -0.0536 -0.0040 104 LEU   A N    
712  C  CA   . LEU   A 100 ? 0.1833 0.1739 0.2432 -0.0027 -0.0430 -0.0067 104 LEU   A CA   
713  C  C    . LEU   A 100 ? 0.1693 0.1679 0.2440 0.0071  -0.0378 -0.0094 104 LEU   A C    
714  O  O    . LEU   A 100 ? 0.1630 0.1561 0.2547 0.0018  -0.0369 -0.0086 104 LEU   A O    
715  C  CB   . LEU   A 100 ? 0.1955 0.1682 0.2272 -0.0020 -0.0389 -0.0135 104 LEU   A CB   
716  C  CG   . LEU   A 100 ? 0.1992 0.1787 0.2406 0.0019  -0.0378 -0.0044 104 LEU   A CG   
717  C  CD1  . LEU   A 100 ? 0.2183 0.2085 0.2533 0.0087  -0.0338 -0.0085 104 LEU   A CD1  
718  C  CD2  . LEU   A 100 ? 0.2098 0.1933 0.2543 -0.0065 -0.0379 0.0055  104 LEU   A CD2  
719  N  N    . ALA   A 101 ? 0.1700 0.1832 0.2576 0.0186  -0.0358 -0.0051 105 ALA   A N    
720  C  CA   . ALA   A 101 ? 0.1750 0.1980 0.2655 0.0225  -0.0202 -0.0075 105 ALA   A CA   
721  C  C    . ALA   A 101 ? 0.1902 0.2001 0.2923 0.0248  -0.0216 -0.0039 105 ALA   A C    
722  O  O    . ALA   A 101 ? 0.2112 0.2128 0.2914 0.0270  -0.0173 0.0041  105 ALA   A O    
723  C  CB   . ALA   A 101 ? 0.1892 0.2017 0.2776 0.0309  -0.0212 -0.0149 105 ALA   A CB   
724  N  N    . ASN   A 102 ? 0.1918 0.1976 0.3245 0.0102  -0.0238 -0.0095 106 ASN   A N    
725  C  CA   . ASN   A 102 ? 0.1975 0.2001 0.3378 -0.0042 -0.0343 -0.0039 106 ASN   A CA   
726  C  C    . ASN   A 102 ? 0.2038 0.1686 0.3059 -0.0075 -0.0235 0.0007  106 ASN   A C    
727  O  O    . ASN   A 102 ? 0.2133 0.1738 0.3177 -0.0089 -0.0312 0.0214  106 ASN   A O    
728  C  CB   . ASN   A 102 ? 0.2159 0.2447 0.3683 -0.0043 -0.0490 -0.0029 106 ASN   A CB   
729  C  CG   . ASN   A 102 ? 0.2436 0.3078 0.4138 0.0016  -0.0318 -0.0115 106 ASN   A CG   
730  O  OD1  . ASN   A 102 ? 0.2541 0.3924 0.4366 -0.0002 -0.0023 -0.0172 106 ASN   A OD1  
731  N  ND2  . ASN   A 102 ? 0.2649 0.3606 0.4539 -0.0085 -0.0479 0.0061  106 ASN   A ND2  
732  N  N    A LEU   A 103 ? 0.1968 0.1580 0.2869 -0.0021 -0.0262 -0.0038 107 LEU   A N    
733  N  N    B LEU   A 103 ? 0.1922 0.1554 0.2876 -0.0038 -0.0252 -0.0011 107 LEU   A N    
734  C  CA   A LEU   A 103 ? 0.1994 0.1539 0.2686 -0.0029 -0.0201 -0.0108 107 LEU   A CA   
735  C  CA   B LEU   A 103 ? 0.1908 0.1490 0.2684 -0.0081 -0.0162 -0.0050 107 LEU   A CA   
736  C  C    A LEU   A 103 ? 0.1833 0.1491 0.2555 -0.0007 -0.0089 -0.0114 107 LEU   A C    
737  C  C    B LEU   A 103 ? 0.1797 0.1471 0.2566 -0.0036 -0.0073 -0.0092 107 LEU   A C    
738  O  O    A LEU   A 103 ? 0.1800 0.1543 0.2371 0.0067  -0.0071 -0.0113 107 LEU   A O    
739  O  O    B LEU   A 103 ? 0.1793 0.1521 0.2468 0.0035  -0.0044 -0.0107 107 LEU   A O    
740  C  CB   A LEU   A 103 ? 0.2075 0.1521 0.2545 -0.0013 -0.0251 -0.0117 107 LEU   A CB   
741  C  CB   B LEU   A 103 ? 0.1911 0.1445 0.2545 -0.0079 -0.0205 -0.0027 107 LEU   A CB   
742  C  CG   A LEU   A 103 ? 0.2154 0.1491 0.2529 0.0029  -0.0288 -0.0118 107 LEU   A CG   
743  C  CG   B LEU   A 103 ? 0.1939 0.1379 0.2474 -0.0098 -0.0195 0.0022  107 LEU   A CG   
744  C  CD1  A LEU   A 103 ? 0.2219 0.1517 0.2518 0.0056  -0.0334 -0.0135 107 LEU   A CD1  
745  C  CD1  B LEU   A 103 ? 0.1980 0.1404 0.2435 -0.0069 -0.0218 0.0037  107 LEU   A CD1  
746  C  CD2  A LEU   A 103 ? 0.2173 0.1582 0.2550 0.0040  -0.0272 -0.0177 107 LEU   A CD2  
747  C  CD2  B LEU   A 103 ? 0.1906 0.1412 0.2479 -0.0100 -0.0186 0.0008  107 LEU   A CD2  
748  N  N    . LEU   A 104 ? 0.1773 0.1481 0.2549 0.0003  -0.0036 -0.0116 108 LEU   A N    
749  C  CA   . LEU   A 104 ? 0.1775 0.1557 0.2531 0.0011  -0.0010 -0.0203 108 LEU   A CA   
750  C  C    . LEU   A 104 ? 0.1782 0.1584 0.2460 0.0047  0.0001  -0.0145 108 LEU   A C    
751  O  O    . LEU   A 104 ? 0.1716 0.1661 0.2244 0.0058  0.0017  -0.0091 108 LEU   A O    
752  C  CB   . LEU   A 104 ? 0.1864 0.1564 0.2705 0.0070  0.0005  -0.0267 108 LEU   A CB   
753  C  CG   . LEU   A 104 ? 0.2061 0.1741 0.2881 -0.0004 0.0053  -0.0303 108 LEU   A CG   
754  C  CD1  . LEU   A 104 ? 0.2203 0.1749 0.3129 -0.0019 0.0061  -0.0393 108 LEU   A CD1  
755  C  CD2  . LEU   A 104 ? 0.2035 0.1742 0.3029 -0.0071 0.0158  -0.0383 108 LEU   A CD2  
756  N  N    . LEU   A 105 ? 0.1835 0.1695 0.2637 0.0082  0.0051  -0.0127 109 LEU   A N    
757  C  CA   . LEU   A 105 ? 0.2021 0.1957 0.2746 0.0000  0.0183  -0.0050 109 LEU   A CA   
758  C  C    . LEU   A 105 ? 0.1943 0.1930 0.2466 0.0015  0.0249  -0.0038 109 LEU   A C    
759  O  O    . LEU   A 105 ? 0.2004 0.1760 0.2381 -0.0014 0.0354  -0.0079 109 LEU   A O    
760  C  CB   . LEU   A 105 ? 0.2182 0.2493 0.3201 -0.0050 0.0289  -0.0014 109 LEU   A CB   
761  C  CG   . LEU   A 105 ? 0.2706 0.2937 0.3538 -0.0082 0.0289  0.0205  109 LEU   A CG   
762  C  CD1  . LEU   A 105 ? 0.2983 0.3305 0.3536 -0.0049 0.0363  0.0167  109 LEU   A CD1  
763  C  CD2  . LEU   A 105 ? 0.2874 0.3428 0.3842 -0.0034 0.0374  0.0231  109 LEU   A CD2  
764  N  N    . ALA   A 106 ? 0.1800 0.1756 0.2334 0.0004  0.0180  0.0007  110 ALA   A N    
765  C  CA   . ALA   A 106 ? 0.1691 0.1763 0.2257 0.0065  0.0193  -0.0010 110 ALA   A CA   
766  C  C    . ALA   A 106 ? 0.1712 0.1607 0.2042 0.0033  0.0202  -0.0025 110 ALA   A C    
767  O  O    . ALA   A 106 ? 0.1894 0.1608 0.1993 0.0064  0.0197  0.0053  110 ALA   A O    
768  C  CB   . ALA   A 106 ? 0.1677 0.1776 0.2303 0.0055  0.0177  -0.0035 110 ALA   A CB   
769  N  N    . PHE   A 107 ? 0.1765 0.1499 0.1877 -0.0003 0.0210  0.0062  111 PHE   A N    
770  C  CA   . PHE   A 107 ? 0.1659 0.1374 0.1725 -0.0035 0.0189  0.0024  111 PHE   A CA   
771  C  C    . PHE   A 107 ? 0.1688 0.1465 0.1681 -0.0031 0.0171  -0.0032 111 PHE   A C    
772  O  O    . PHE   A 107 ? 0.1840 0.1465 0.1582 -0.0008 0.0198  -0.0040 111 PHE   A O    
773  C  CB   . PHE   A 107 ? 0.1674 0.1351 0.1861 -0.0034 0.0119  0.0032  111 PHE   A CB   
774  C  CG   . PHE   A 107 ? 0.1654 0.1312 0.1909 0.0035  0.0079  0.0033  111 PHE   A CG   
775  C  CD1  . PHE   A 107 ? 0.1525 0.1393 0.1990 0.0031  0.0076  0.0046  111 PHE   A CD1  
776  C  CD2  . PHE   A 107 ? 0.1650 0.1432 0.1925 0.0054  0.0071  0.0038  111 PHE   A CD2  
777  C  CE1  . PHE   A 107 ? 0.1515 0.1348 0.2010 0.0056  0.0053  0.0022  111 PHE   A CE1  
778  C  CE2  . PHE   A 107 ? 0.1654 0.1451 0.1999 0.0015  0.0045  0.0000  111 PHE   A CE2  
779  C  CZ   . PHE   A 107 ? 0.1510 0.1441 0.2033 0.0040  0.0054  0.0082  111 PHE   A CZ   
780  N  N    . LEU   A 108 ? 0.1804 0.1557 0.1853 0.0003  0.0210  -0.0115 112 LEU   A N    
781  C  CA   . LEU   A 108 ? 0.1913 0.1669 0.1844 -0.0018 0.0197  -0.0217 112 LEU   A CA   
782  C  C    . LEU   A 108 ? 0.1906 0.1706 0.1778 -0.0059 0.0225  -0.0183 112 LEU   A C    
783  O  O    . LEU   A 108 ? 0.2034 0.2004 0.1504 -0.0216 0.0042  -0.0180 112 LEU   A O    
784  C  CB   . LEU   A 108 ? 0.2108 0.1826 0.2121 0.0015  0.0218  -0.0408 112 LEU   A CB   
785  C  CG   . LEU   A 108 ? 0.2269 0.1926 0.2468 -0.0054 0.0202  -0.0480 112 LEU   A CG   
786  C  CD1  . LEU   A 108 ? 0.2600 0.2070 0.2808 -0.0025 0.0156  -0.0688 112 LEU   A CD1  
787  C  CD2  . LEU   A 108 ? 0.2420 0.2162 0.2741 -0.0075 0.0148  -0.0525 112 LEU   A CD2  
788  N  N    . ARG   A 109 ? 0.1963 0.1728 0.1742 -0.0102 0.0194  -0.0119 113 ARG   A N    
789  C  CA   . ARG   A 109 ? 0.2166 0.1816 0.1966 -0.0180 0.0267  0.0018  113 ARG   A CA   
790  C  C    . ARG   A 109 ? 0.2110 0.1704 0.1954 -0.0239 0.0013  0.0006  113 ARG   A C    
791  O  O    . ARG   A 109 ? 0.2402 0.1842 0.2523 -0.0384 0.0118  0.0195  113 ARG   A O    
792  C  CB   . ARG   A 109 ? 0.2258 0.2013 0.2510 -0.0179 0.0223  0.0001  113 ARG   A CB   
793  C  CG   . ARG   A 109 ? 0.2601 0.2537 0.3005 -0.0089 0.0371  -0.0104 113 ARG   A CG   
794  C  CD   . ARG   A 109 ? 0.2872 0.3324 0.3648 0.0042  0.0244  -0.0062 113 ARG   A CD   
795  N  NE   . ARG   A 109 ? 0.3377 0.3900 0.3937 0.0254  0.0332  -0.0101 113 ARG   A NE   
796  C  CZ   . ARG   A 109 ? 0.3651 0.3952 0.4537 0.0428  0.0288  -0.0160 113 ARG   A CZ   
797  N  NH1  . ARG   A 109 ? 0.3210 0.4206 0.4558 0.0124  0.0403  -0.0199 113 ARG   A NH1  
798  N  NH2  . ARG   A 109 ? 0.4507 0.4279 0.4909 0.0631  0.0281  -0.0364 113 ARG   A NH2  
799  N  N    . ARG   A 110 ? 0.1998 0.1607 0.1755 -0.0131 -0.0117 -0.0129 114 ARG   A N    
800  C  CA   . ARG   A 110 ? 0.2067 0.1710 0.1851 -0.0020 -0.0077 -0.0100 114 ARG   A CA   
801  C  C    . ARG   A 110 ? 0.1993 0.1647 0.1710 -0.0099 0.0013  -0.0070 114 ARG   A C    
802  O  O    . ARG   A 110 ? 0.2209 0.1763 0.1797 0.0042  -0.0168 -0.0079 114 ARG   A O    
803  C  CB   . ARG   A 110 ? 0.2205 0.1926 0.1786 0.0246  -0.0101 -0.0241 114 ARG   A CB   
804  C  CG   . ARG   A 110 ? 0.2432 0.2315 0.2014 0.0379  -0.0218 -0.0183 114 ARG   A CG   
805  C  CD   . ARG   A 110 ? 0.2385 0.2281 0.2035 0.0349  -0.0139 -0.0217 114 ARG   A CD   
806  N  NE   . ARG   A 110 ? 0.2158 0.2010 0.1651 0.0311  -0.0065 -0.0282 114 ARG   A NE   
807  C  CZ   . ARG   A 110 ? 0.2109 0.1972 0.1537 0.0299  0.0099  -0.0237 114 ARG   A CZ   
808  N  NH1  . ARG   A 110 ? 0.2150 0.2068 0.1620 0.0322  0.0210  -0.0394 114 ARG   A NH1  
809  N  NH2  . ARG   A 110 ? 0.2055 0.1760 0.1544 0.0239  0.0172  -0.0217 114 ARG   A NH2  
810  N  N    . GLN   A 111 ? 0.1982 0.1679 0.1569 -0.0074 0.0103  -0.0028 115 GLN   A N    
811  C  CA   . GLN   A 111 ? 0.2042 0.1733 0.1524 -0.0111 0.0120  0.0031  115 GLN   A CA   
812  C  C    . GLN   A 111 ? 0.2086 0.1836 0.1562 -0.0172 0.0170  -0.0043 115 GLN   A C    
813  O  O    . GLN   A 111 ? 0.2192 0.2109 0.1824 -0.0015 0.0197  0.0142  115 GLN   A O    
814  C  CB   . GLN   A 111 ? 0.2035 0.1788 0.1539 -0.0111 0.0050  -0.0015 115 GLN   A CB   
815  C  CG   . GLN   A 111 ? 0.1880 0.1645 0.1593 -0.0137 0.0051  -0.0048 115 GLN   A CG   
816  C  CD   . GLN   A 111 ? 0.1884 0.1590 0.1547 -0.0087 0.0042  -0.0031 115 GLN   A CD   
817  O  OE1  . GLN   A 111 ? 0.1926 0.1609 0.1671 -0.0054 0.0077  0.0012  115 GLN   A OE1  
818  N  NE2  . GLN   A 111 ? 0.1910 0.1575 0.1498 -0.0028 0.0121  -0.0042 115 GLN   A NE2  
819  N  N    . PRO   A 112 ? 0.2167 0.1852 0.1556 -0.0099 0.0231  -0.0004 116 PRO   A N    
820  C  CA   . PRO   A 112 ? 0.2231 0.1829 0.1490 -0.0124 0.0187  0.0016  116 PRO   A CA   
821  C  C    . PRO   A 112 ? 0.2109 0.1827 0.1528 -0.0140 0.0174  -0.0002 116 PRO   A C    
822  O  O    . PRO   A 112 ? 0.2105 0.1762 0.1585 -0.0191 0.0167  -0.0058 116 PRO   A O    
823  C  CB   . PRO   A 112 ? 0.2471 0.1928 0.1708 -0.0049 0.0125  0.0033  116 PRO   A CB   
824  C  CG   . PRO   A 112 ? 0.2451 0.2076 0.1988 -0.0032 0.0164  0.0175  116 PRO   A CG   
825  C  CD   . PRO   A 112 ? 0.2286 0.2034 0.1611 -0.0021 0.0152  0.0018  116 PRO   A CD   
826  N  N    . GLN   A 113 ? 0.2112 0.1975 0.1691 -0.0218 0.0254  0.0066  117 GLN   A N    
827  C  CA   . GLN   A 113 ? 0.2103 0.1960 0.1705 -0.0135 0.0207  0.0071  117 GLN   A CA   
828  C  C    . GLN   A 113 ? 0.2189 0.1873 0.1671 -0.0135 0.0244  0.0132  117 GLN   A C    
829  O  O    . GLN   A 113 ? 0.2106 0.1895 0.1883 -0.0202 0.0063  0.0081  117 GLN   A O    
830  C  CB   . GLN   A 113 ? 0.2199 0.2233 0.2113 -0.0009 0.0197  0.0015  117 GLN   A CB   
831  C  CG   . GLN   A 113 ? 0.2452 0.2564 0.2577 0.0000  0.0113  0.0132  117 GLN   A CG   
832  C  CD   . GLN   A 113 ? 0.2661 0.3005 0.3589 0.0133  0.0012  0.0029  117 GLN   A CD   
833  O  OE1  . GLN   A 113 ? 0.3269 0.3330 0.4296 0.0089  0.0077  -0.0208 117 GLN   A OE1  
834  N  NE2  . GLN   A 113 ? 0.2988 0.3372 0.4513 -0.0032 -0.0138 -0.0077 117 GLN   A NE2  
835  N  N    . PRO   A 114 ? 0.2290 0.1834 0.1781 -0.0216 0.0163  0.0185  118 PRO   A N    
836  C  CA   . PRO   A 114 ? 0.2179 0.1805 0.1706 -0.0173 0.0189  0.0133  118 PRO   A CA   
837  C  C    . PRO   A 114 ? 0.2036 0.1741 0.1647 -0.0189 0.0113  0.0007  118 PRO   A C    
838  O  O    . PRO   A 114 ? 0.2250 0.1721 0.1763 -0.0060 0.0115  -0.0049 118 PRO   A O    
839  C  CB   . PRO   A 114 ? 0.2342 0.2016 0.1856 -0.0169 0.0135  0.0039  118 PRO   A CB   
840  C  CG   . PRO   A 114 ? 0.2365 0.2097 0.1744 -0.0108 0.0069  0.0113  118 PRO   A CG   
841  C  CD   . PRO   A 114 ? 0.2318 0.2048 0.1758 -0.0148 0.0105  0.0155  118 PRO   A CD   
842  N  N    . TRP   A 115 ? 0.2005 0.1648 0.1612 -0.0187 0.0105  0.0001  119 TRP   A N    
843  C  CA   . TRP   A 115 ? 0.2173 0.1753 0.1801 -0.0251 0.0114  0.0025  119 TRP   A CA   
844  C  C    . TRP   A 115 ? 0.2080 0.1558 0.1584 -0.0132 0.0171  0.0012  119 TRP   A C    
845  O  O    . TRP   A 115 ? 0.2119 0.1577 0.1685 -0.0168 0.0207  -0.0007 119 TRP   A O    
846  C  CB   . TRP   A 115 ? 0.2260 0.2023 0.1978 -0.0107 0.0081  0.0085  119 TRP   A CB   
847  C  CG   . TRP   A 115 ? 0.2290 0.2193 0.1821 0.0013  0.0154  -0.0016 119 TRP   A CG   
848  C  CD1  . TRP   A 115 ? 0.2260 0.2257 0.1871 0.0046  0.0223  -0.0030 119 TRP   A CD1  
849  C  CD2  . TRP   A 115 ? 0.2278 0.2418 0.1962 0.0113  0.0046  -0.0140 119 TRP   A CD2  
850  N  NE1  . TRP   A 115 ? 0.2351 0.2338 0.2226 0.0107  0.0098  -0.0167 119 TRP   A NE1  
851  C  CE2  . TRP   A 115 ? 0.2371 0.2579 0.2178 0.0199  0.0079  -0.0169 119 TRP   A CE2  
852  C  CE3  . TRP   A 115 ? 0.2532 0.2719 0.2238 0.0279  -0.0214 -0.0133 119 TRP   A CE3  
853  C  CZ2  . TRP   A 115 ? 0.2438 0.2650 0.2244 0.0202  -0.0004 -0.0239 119 TRP   A CZ2  
854  C  CZ3  . TRP   A 115 ? 0.2489 0.2709 0.2505 0.0321  -0.0170 -0.0146 119 TRP   A CZ3  
855  C  CH2  . TRP   A 115 ? 0.2397 0.2738 0.2446 0.0262  -0.0118 -0.0160 119 TRP   A CH2  
856  N  N    . CYS   A 116 ? 0.2026 0.1333 0.1447 -0.0069 0.0116  -0.0085 120 CYS   A N    
857  C  CA   . CYS   A 116 ? 0.2096 0.1417 0.1479 -0.0103 0.0101  -0.0045 120 CYS   A CA   
858  C  C    . CYS   A 116 ? 0.2040 0.1379 0.1409 -0.0110 0.0049  -0.0065 120 CYS   A C    
859  O  O    . CYS   A 116 ? 0.2020 0.1284 0.1376 -0.0096 0.0067  0.0026  120 CYS   A O    
860  C  CB   . CYS   A 116 ? 0.2333 0.1592 0.1512 -0.0112 0.0063  0.0004  120 CYS   A CB   
861  S  SG   . CYS   A 116 ? 0.2775 0.2021 0.1461 -0.0151 -0.0091 -0.0087 120 CYS   A SG   
862  N  N    . LEU   A 117 ? 0.2064 0.1379 0.1386 -0.0073 0.0058  -0.0100 121 LEU   A N    
863  C  CA   . LEU   A 117 ? 0.2119 0.1359 0.1370 -0.0046 0.0014  -0.0089 121 LEU   A CA   
864  C  C    . LEU   A 117 ? 0.2100 0.1360 0.1326 -0.0079 0.0010  -0.0158 121 LEU   A C    
865  O  O    . LEU   A 117 ? 0.2194 0.1831 0.1365 -0.0228 0.0025  -0.0275 121 LEU   A O    
866  C  CB   . LEU   A 117 ? 0.2295 0.1452 0.1582 0.0084  -0.0111 -0.0119 121 LEU   A CB   
867  C  CG   . LEU   A 117 ? 0.2514 0.1819 0.1827 0.0180  -0.0285 -0.0092 121 LEU   A CG   
868  C  CD1  . LEU   A 117 ? 0.2700 0.2014 0.1969 0.0326  -0.0315 -0.0191 121 LEU   A CD1  
869  C  CD2  . LEU   A 117 ? 0.2657 0.1822 0.1947 0.0152  -0.0379 -0.0324 121 LEU   A CD2  
870  N  N    . VAL   A 118 ? 0.2127 0.1320 0.1232 -0.0201 -0.0014 -0.0106 122 VAL   A N    
871  C  CA   . VAL   A 118 ? 0.2069 0.1241 0.1280 -0.0177 -0.0044 -0.0076 122 VAL   A CA   
872  C  C    . VAL   A 118 ? 0.2075 0.1210 0.1250 -0.0164 -0.0099 -0.0085 122 VAL   A C    
873  O  O    . VAL   A 118 ? 0.2027 0.1169 0.1267 -0.0236 -0.0032 -0.0142 122 VAL   A O    
874  C  CB   . VAL   A 118 ? 0.2190 0.1326 0.1427 -0.0161 -0.0122 0.0031  122 VAL   A CB   
875  C  CG1  . VAL   A 118 ? 0.2227 0.1369 0.1525 -0.0105 -0.0189 0.0074  122 VAL   A CG1  
876  C  CG2  . VAL   A 118 ? 0.2214 0.1357 0.1527 -0.0118 -0.0131 0.0072  122 VAL   A CG2  
877  N  N    . ALA   A 119 ? 0.2007 0.1241 0.1167 -0.0170 -0.0189 -0.0161 123 ALA   A N    
878  C  CA   . ALA   A 119 ? 0.2088 0.1273 0.1196 -0.0094 -0.0260 -0.0071 123 ALA   A CA   
879  C  C    . ALA   A 119 ? 0.2142 0.1277 0.1201 -0.0121 -0.0289 -0.0048 123 ALA   A C    
880  O  O    . ALA   A 119 ? 0.2181 0.1444 0.1204 -0.0159 -0.0226 -0.0104 123 ALA   A O    
881  C  CB   . ALA   A 119 ? 0.2094 0.1228 0.1274 -0.0055 -0.0277 -0.0118 123 ALA   A CB   
882  N  N    . HIS   A 120 ? 0.2111 0.1460 0.1280 -0.0179 -0.0375 -0.0075 124 HIS   A N    
883  C  CA   . HIS   A 120 ? 0.2198 0.1486 0.1561 -0.0216 -0.0466 -0.0075 124 HIS   A CA   
884  C  C    . HIS   A 120 ? 0.2191 0.1440 0.1538 -0.0211 -0.0415 -0.0089 124 HIS   A C    
885  O  O    . HIS   A 120 ? 0.2291 0.1582 0.1464 -0.0282 -0.0505 -0.0059 124 HIS   A O    
886  C  CB   . HIS   A 120 ? 0.2335 0.1688 0.1752 -0.0139 -0.0471 -0.0115 124 HIS   A CB   
887  C  CG   . HIS   A 120 ? 0.2438 0.2065 0.2022 -0.0170 -0.0624 -0.0072 124 HIS   A CG   
888  N  ND1  . HIS   A 120 ? 0.2672 0.2330 0.2211 -0.0186 -0.0679 0.0023  124 HIS   A ND1  
889  C  CD2  . HIS   A 120 ? 0.2676 0.2182 0.2220 -0.0250 -0.0672 0.0053  124 HIS   A CD2  
890  C  CE1  . HIS   A 120 ? 0.2729 0.2346 0.2366 -0.0233 -0.0793 0.0118  124 HIS   A CE1  
891  N  NE2  . HIS   A 120 ? 0.2743 0.2337 0.2454 -0.0247 -0.0803 0.0079  124 HIS   A NE2  
892  N  N    . ASN   A 121 ? 0.2225 0.1432 0.1549 -0.0186 -0.0466 -0.0099 125 ASN   A N    
893  C  CA   . ASN   A 121 ? 0.2318 0.1414 0.1694 -0.0184 -0.0404 -0.0147 125 ASN   A CA   
894  C  C    . ASN   A 121 ? 0.2312 0.1271 0.1521 -0.0062 -0.0334 -0.0130 125 ASN   A C    
895  O  O    . ASN   A 121 ? 0.2314 0.1165 0.1546 -0.0069 -0.0378 -0.0053 125 ASN   A O    
896  C  CB   . ASN   A 121 ? 0.2474 0.1654 0.1876 -0.0314 -0.0415 -0.0162 125 ASN   A CB   
897  C  CG   . ASN   A 121 ? 0.2804 0.1978 0.2137 -0.0370 -0.0437 -0.0361 125 ASN   A CG   
898  O  OD1  . ASN   A 121 ? 0.3175 0.1973 0.2499 -0.0258 -0.0286 -0.0637 125 ASN   A OD1  
899  N  ND2  . ASN   A 121 ? 0.3060 0.2310 0.2582 -0.0588 -0.0616 -0.0411 125 ASN   A ND2  
900  N  N    . GLY   A 122 ? 0.2197 0.1210 0.1540 0.0003  -0.0262 -0.0133 126 GLY   A N    
901  C  CA   . GLY   A 122 ? 0.2160 0.1250 0.1487 -0.0035 -0.0211 -0.0128 126 GLY   A CA   
902  C  C    . GLY   A 122 ? 0.2163 0.1281 0.1405 -0.0042 -0.0184 -0.0104 126 GLY   A C    
903  O  O    . GLY   A 122 ? 0.2119 0.1295 0.1351 -0.0024 -0.0134 0.0015  126 GLY   A O    
904  N  N    . ASP   A 123 ? 0.2367 0.1425 0.1403 -0.0008 -0.0162 -0.0047 127 ASP   A N    
905  C  CA   . ASP   A 123 ? 0.2642 0.1608 0.1393 0.0025  -0.0102 -0.0079 127 ASP   A CA   
906  C  C    . ASP   A 123 ? 0.2631 0.1565 0.1499 0.0095  -0.0110 -0.0094 127 ASP   A C    
907  O  O    . ASP   A 123 ? 0.2662 0.1652 0.1752 0.0136  -0.0034 -0.0100 127 ASP   A O    
908  C  CB   . ASP   A 123 ? 0.2968 0.1807 0.1355 0.0051  -0.0092 -0.0100 127 ASP   A CB   
909  C  CG   . ASP   A 123 ? 0.3338 0.2061 0.1589 -0.0013 0.0017  -0.0020 127 ASP   A CG   
910  O  OD1  . ASP   A 123 ? 0.3641 0.2203 0.1915 -0.0106 0.0066  -0.0049 127 ASP   A OD1  
911  O  OD2  . ASP   A 123 ? 0.4064 0.2663 0.1688 0.0122  -0.0073 0.0060  127 ASP   A OD2  
912  N  N    . ARG   A 124 ? 0.2613 0.1482 0.1549 0.0054  -0.0129 -0.0134 128 ARG   A N    
913  C  CA   . ARG   A 124 ? 0.2575 0.1492 0.1597 0.0016  -0.0145 -0.0129 128 ARG   A CA   
914  C  C    . ARG   A 124 ? 0.2374 0.1461 0.1610 -0.0012 -0.0181 -0.0089 128 ARG   A C    
915  O  O    . ARG   A 124 ? 0.2314 0.1545 0.1555 0.0032  -0.0100 -0.0078 128 ARG   A O    
916  C  CB   . ARG   A 124 ? 0.2690 0.1715 0.1764 -0.0024 -0.0233 -0.0191 128 ARG   A CB   
917  C  CG   . ARG   A 124 ? 0.2838 0.1877 0.1978 -0.0049 -0.0376 -0.0075 128 ARG   A CG   
918  C  CD   . ARG   A 124 ? 0.3040 0.2097 0.2357 -0.0148 -0.0493 -0.0074 128 ARG   A CD   
919  N  NE   . ARG   A 124 ? 0.3226 0.2339 0.2639 -0.0164 -0.0697 -0.0221 128 ARG   A NE   
920  C  CZ   . ARG   A 124 ? 0.3396 0.2500 0.3238 -0.0154 -0.0869 -0.0386 128 ARG   A CZ   
921  N  NH1  . ARG   A 124 ? 0.3832 0.2713 0.3439 0.0115  -0.1022 -0.0288 128 ARG   A NH1  
922  N  NH2  . ARG   A 124 ? 0.3187 0.2469 0.3476 -0.0236 -0.0952 -0.0472 128 ARG   A NH2  
923  N  N    . TYR   A 125 ? 0.2166 0.1387 0.1505 -0.0011 -0.0239 -0.0027 129 TYR   A N    
924  C  CA   . TYR   A 125 ? 0.2054 0.1345 0.1503 -0.0114 -0.0181 -0.0055 129 TYR   A CA   
925  C  C    . TYR   A 125 ? 0.1862 0.1289 0.1347 -0.0064 -0.0122 -0.0063 129 TYR   A C    
926  O  O    . TYR   A 125 ? 0.1930 0.1264 0.1479 -0.0038 -0.0120 -0.0104 129 TYR   A O    
927  C  CB   . TYR   A 125 ? 0.2005 0.1447 0.1525 -0.0150 -0.0275 -0.0014 129 TYR   A CB   
928  C  CG   . TYR   A 125 ? 0.2063 0.1514 0.1615 -0.0248 -0.0354 0.0011  129 TYR   A CG   
929  C  CD1  . TYR   A 125 ? 0.2090 0.1555 0.1770 -0.0295 -0.0541 0.0053  129 TYR   A CD1  
930  C  CD2  . TYR   A 125 ? 0.2157 0.1556 0.1835 -0.0300 -0.0437 0.0057  129 TYR   A CD2  
931  C  CE1  . TYR   A 125 ? 0.2205 0.1704 0.1931 -0.0430 -0.0505 0.0074  129 TYR   A CE1  
932  C  CE2  . TYR   A 125 ? 0.2182 0.1813 0.1967 -0.0397 -0.0502 0.0039  129 TYR   A CE2  
933  C  CZ   . TYR   A 125 ? 0.2222 0.1784 0.2144 -0.0452 -0.0503 -0.0001 129 TYR   A CZ   
934  O  OH   . TYR   A 125 ? 0.2602 0.2317 0.2556 -0.0844 -0.0568 -0.0079 129 TYR   A OH   
935  N  N    . ASP   A 126 ? 0.1793 0.1324 0.1304 -0.0031 -0.0206 -0.0081 130 ASP   A N    
936  C  CA   . ASP   A 126 ? 0.1759 0.1326 0.1319 -0.0066 -0.0103 -0.0098 130 ASP   A CA   
937  C  C    . ASP   A 126 ? 0.1756 0.1342 0.1299 -0.0096 -0.0074 -0.0045 130 ASP   A C    
938  O  O    . ASP   A 126 ? 0.1747 0.1548 0.1298 -0.0163 -0.0032 -0.0005 130 ASP   A O    
939  C  CB   . ASP   A 126 ? 0.1743 0.1312 0.1347 -0.0064 -0.0100 -0.0072 130 ASP   A CB   
940  C  CG   . ASP   A 126 ? 0.1746 0.1485 0.1357 -0.0052 -0.0068 -0.0077 130 ASP   A CG   
941  O  OD1  . ASP   A 126 ? 0.1893 0.1693 0.1410 -0.0069 -0.0110 -0.0111 130 ASP   A OD1  
942  O  OD2  . ASP   A 126 ? 0.1987 0.1593 0.1314 0.0001  -0.0086 -0.0158 130 ASP   A OD2  
943  N  N    . PHE   A 127 ? 0.1727 0.1382 0.1275 -0.0094 -0.0015 -0.0075 131 PHE   A N    
944  C  CA   . PHE   A 127 ? 0.1783 0.1467 0.1344 -0.0090 0.0015  -0.0014 131 PHE   A CA   
945  C  C    . PHE   A 127 ? 0.1767 0.1466 0.1401 -0.0076 0.0031  -0.0009 131 PHE   A C    
946  O  O    . PHE   A 127 ? 0.1664 0.1612 0.1408 -0.0132 0.0077  0.0029  131 PHE   A O    
947  C  CB   . PHE   A 127 ? 0.1915 0.1456 0.1384 -0.0108 0.0039  0.0076  131 PHE   A CB   
948  C  CG   . PHE   A 127 ? 0.2051 0.1395 0.1363 -0.0093 0.0065  0.0097  131 PHE   A CG   
949  C  CD1  . PHE   A 127 ? 0.2157 0.1500 0.1431 -0.0098 0.0042  0.0070  131 PHE   A CD1  
950  C  CD2  . PHE   A 127 ? 0.2143 0.1495 0.1440 -0.0039 0.0003  0.0109  131 PHE   A CD2  
951  C  CE1  . PHE   A 127 ? 0.2188 0.1392 0.1478 -0.0129 0.0043  0.0031  131 PHE   A CE1  
952  C  CE2  . PHE   A 127 ? 0.2249 0.1473 0.1435 -0.0052 -0.0010 0.0171  131 PHE   A CE2  
953  C  CZ   . PHE   A 127 ? 0.2301 0.1458 0.1563 -0.0021 0.0060  0.0131  131 PHE   A CZ   
954  N  N    . PRO   A 128 ? 0.1831 0.1475 0.1512 -0.0031 -0.0003 -0.0064 132 PRO   A N    
955  C  CA   . PRO   A 128 ? 0.1929 0.1471 0.1575 -0.0013 0.0025  -0.0109 132 PRO   A CA   
956  C  C    . PRO   A 128 ? 0.1873 0.1465 0.1551 0.0017  0.0043  -0.0127 132 PRO   A C    
957  O  O    . PRO   A 128 ? 0.1840 0.1487 0.1474 0.0023  0.0036  -0.0175 132 PRO   A O    
958  C  CB   . PRO   A 128 ? 0.2074 0.1568 0.1589 -0.0023 -0.0013 -0.0137 132 PRO   A CB   
959  C  CG   . PRO   A 128 ? 0.2104 0.1552 0.1736 -0.0051 -0.0042 -0.0152 132 PRO   A CG   
960  C  CD   . PRO   A 128 ? 0.1959 0.1496 0.1643 -0.0043 -0.0027 -0.0134 132 PRO   A CD   
961  N  N    . LEU   A 129 ? 0.1803 0.1369 0.1452 -0.0024 0.0002  -0.0085 133 LEU   A N    
962  C  CA   . LEU   A 129 ? 0.1760 0.1403 0.1454 -0.0045 -0.0048 -0.0050 133 LEU   A CA   
963  C  C    . LEU   A 129 ? 0.1697 0.1442 0.1472 -0.0041 0.0035  -0.0094 133 LEU   A C    
964  O  O    . LEU   A 129 ? 0.1709 0.1456 0.1489 -0.0021 0.0062  -0.0109 133 LEU   A O    
965  C  CB   . LEU   A 129 ? 0.1725 0.1389 0.1439 -0.0103 -0.0132 -0.0071 133 LEU   A CB   
966  C  CG   . LEU   A 129 ? 0.1750 0.1440 0.1472 -0.0124 -0.0226 -0.0075 133 LEU   A CG   
967  C  CD1  . LEU   A 129 ? 0.1755 0.1415 0.1613 -0.0165 -0.0230 -0.0082 133 LEU   A CD1  
968  C  CD2  . LEU   A 129 ? 0.1845 0.1527 0.1451 -0.0202 -0.0237 -0.0016 133 LEU   A CD2  
969  N  N    . LEU   A 130 ? 0.1571 0.1437 0.1564 -0.0089 0.0052  -0.0063 134 LEU   A N    
970  C  CA   . LEU   A 130 ? 0.1717 0.1525 0.1650 -0.0127 0.0088  -0.0093 134 LEU   A CA   
971  C  C    . LEU   A 130 ? 0.1776 0.1608 0.1686 -0.0106 0.0152  -0.0092 134 LEU   A C    
972  O  O    . LEU   A 130 ? 0.1871 0.1744 0.1676 -0.0139 0.0214  -0.0205 134 LEU   A O    
973  C  CB   . LEU   A 130 ? 0.1702 0.1592 0.1895 -0.0118 0.0131  -0.0061 134 LEU   A CB   
974  C  CG   . LEU   A 130 ? 0.1806 0.1687 0.2067 -0.0149 0.0104  -0.0120 134 LEU   A CG   
975  C  CD1  . LEU   A 130 ? 0.2019 0.1778 0.2203 -0.0162 0.0043  -0.0196 134 LEU   A CD1  
976  C  CD2  . LEU   A 130 ? 0.1811 0.1678 0.2267 -0.0185 0.0174  -0.0102 134 LEU   A CD2  
977  N  N    . GLN   A 131 ? 0.1815 0.1637 0.1708 -0.0054 0.0189  -0.0067 135 GLN   A N    
978  C  CA   . GLN   A 131 ? 0.1877 0.1902 0.1894 0.0000  0.0193  -0.0059 135 GLN   A CA   
979  C  C    . GLN   A 131 ? 0.1830 0.1857 0.1898 0.0019  0.0201  -0.0121 135 GLN   A C    
980  O  O    . GLN   A 131 ? 0.1871 0.1999 0.2283 -0.0044 0.0182  -0.0086 135 GLN   A O    
981  C  CB   . GLN   A 131 ? 0.2164 0.2179 0.1982 -0.0054 0.0176  -0.0003 135 GLN   A CB   
982  C  CG   . GLN   A 131 ? 0.2420 0.2556 0.2285 -0.0087 0.0205  0.0266  135 GLN   A CG   
983  C  CD   . GLN   A 131 ? 0.2756 0.2890 0.2609 -0.0356 0.0130  0.0482  135 GLN   A CD   
984  O  OE1  . GLN   A 131 ? 0.2823 0.3069 0.2923 -0.0434 0.0035  0.0642  135 GLN   A OE1  
985  N  NE2  . GLN   A 131 ? 0.2865 0.3523 0.2651 -0.0300 0.0273  0.0604  135 GLN   A NE2  
986  N  N    . ALA   A 132 ? 0.1677 0.1811 0.1977 0.0089  0.0133  -0.0105 136 ALA   A N    
987  C  CA   . ALA   A 132 ? 0.1660 0.1829 0.1904 0.0156  0.0059  -0.0130 136 ALA   A CA   
988  C  C    . ALA   A 132 ? 0.1667 0.1938 0.1996 0.0081  0.0007  -0.0141 136 ALA   A C    
989  O  O    . ALA   A 132 ? 0.1684 0.2115 0.2082 0.0103  -0.0006 -0.0193 136 ALA   A O    
990  C  CB   . ALA   A 132 ? 0.1684 0.1704 0.1796 0.0157  0.0033  -0.0077 136 ALA   A CB   
991  N  N    . GLU   A 133 ? 0.1574 0.1910 0.1950 0.0007  -0.0023 -0.0185 137 GLU   A N    
992  C  CA   . GLU   A 133 ? 0.1678 0.2056 0.2001 -0.0042 -0.0013 -0.0193 137 GLU   A CA   
993  C  C    . GLU   A 133 ? 0.1651 0.2103 0.2163 -0.0035 -0.0039 -0.0222 137 GLU   A C    
994  O  O    . GLU   A 133 ? 0.1759 0.2350 0.2306 -0.0027 -0.0086 -0.0166 137 GLU   A O    
995  C  CB   . GLU   A 133 ? 0.1734 0.2142 0.2145 0.0009  -0.0009 -0.0188 137 GLU   A CB   
996  C  CG   . GLU   A 133 ? 0.1705 0.2197 0.2208 -0.0007 -0.0035 -0.0234 137 GLU   A CG   
997  C  CD   . GLU   A 133 ? 0.1784 0.2313 0.2324 -0.0022 -0.0071 -0.0181 137 GLU   A CD   
998  O  OE1  . GLU   A 133 ? 0.1926 0.2753 0.2455 -0.0052 -0.0225 -0.0222 137 GLU   A OE1  
999  O  OE2  . GLU   A 133 ? 0.1919 0.2173 0.2431 -0.0136 -0.0042 -0.0054 137 GLU   A OE2  
1000 N  N    . LEU   A 134 ? 0.1647 0.2262 0.2291 -0.0101 -0.0065 -0.0120 138 LEU   A N    
1001 C  CA   . LEU   A 134 ? 0.1723 0.2409 0.2560 -0.0143 -0.0081 -0.0040 138 LEU   A CA   
1002 C  C    . LEU   A 134 ? 0.1777 0.2614 0.2748 -0.0065 0.0005  -0.0055 138 LEU   A C    
1003 O  O    . LEU   A 134 ? 0.1752 0.2815 0.3006 -0.0139 -0.0011 -0.0094 138 LEU   A O    
1004 C  CB   . LEU   A 134 ? 0.1781 0.2429 0.2745 -0.0293 -0.0174 0.0033  138 LEU   A CB   
1005 C  CG   . LEU   A 134 ? 0.2106 0.2387 0.2937 -0.0256 -0.0207 0.0027  138 LEU   A CG   
1006 C  CD1  . LEU   A 134 ? 0.2242 0.2433 0.3146 -0.0309 -0.0245 0.0098  138 LEU   A CD1  
1007 C  CD2  . LEU   A 134 ? 0.2283 0.2422 0.2884 -0.0163 -0.0192 0.0049  138 LEU   A CD2  
1008 N  N    . ALA   A 135 ? 0.1701 0.2708 0.2643 0.0053  0.0105  -0.0142 139 ALA   A N    
1009 C  CA   . ALA   A 135 ? 0.1840 0.2948 0.2949 0.0154  0.0189  -0.0259 139 ALA   A CA   
1010 C  C    . ALA   A 135 ? 0.1935 0.3002 0.3119 0.0315  0.0142  -0.0249 139 ALA   A C    
1011 O  O    . ALA   A 135 ? 0.1922 0.3290 0.3271 0.0308  0.0197  -0.0144 139 ALA   A O    
1012 C  CB   . ALA   A 135 ? 0.1969 0.3027 0.2899 0.0196  0.0241  -0.0346 139 ALA   A CB   
1013 N  N    A MET   A 136 ? 0.1892 0.2988 0.3233 0.0332  0.0169  -0.0321 140 MET   A N    
1014 N  N    B MET   A 136 ? 0.1854 0.2956 0.3093 0.0329  0.0079  -0.0283 140 MET   A N    
1015 C  CA   A MET   A 136 ? 0.2156 0.3081 0.3390 0.0383  0.0057  -0.0282 140 MET   A CA   
1016 C  CA   B MET   A 136 ? 0.2067 0.3040 0.3173 0.0362  -0.0059 -0.0235 140 MET   A CA   
1017 C  C    A MET   A 136 ? 0.2142 0.3243 0.3421 0.0366  -0.0036 -0.0225 140 MET   A C    
1018 C  C    B MET   A 136 ? 0.2103 0.3220 0.3276 0.0356  -0.0134 -0.0215 140 MET   A C    
1019 O  O    A MET   A 136 ? 0.2323 0.3308 0.3637 0.0387  -0.0183 -0.0083 140 MET   A O    
1020 O  O    B MET   A 136 ? 0.2308 0.3309 0.3483 0.0410  -0.0301 -0.0101 140 MET   A O    
1021 C  CB   A MET   A 136 ? 0.2351 0.3297 0.3594 0.0353  0.0135  -0.0234 140 MET   A CB   
1022 C  CB   B MET   A 136 ? 0.2175 0.3175 0.3173 0.0317  -0.0103 -0.0161 140 MET   A CB   
1023 C  CG   A MET   A 136 ? 0.2824 0.3641 0.3902 0.0256  0.0094  -0.0300 140 MET   A CG   
1024 C  CG   B MET   A 136 ? 0.2500 0.3434 0.3278 0.0235  -0.0224 -0.0131 140 MET   A CG   
1025 S  SD   A MET   A 136 ? 0.3907 0.4000 0.4864 0.0336  0.0331  -0.0261 140 MET   A SD   
1026 S  SD   B MET   A 136 ? 0.3207 0.3739 0.3573 0.0259  -0.0091 -0.0181 140 MET   A SD   
1027 C  CE   A MET   A 136 ? 0.3809 0.4154 0.4893 0.0331  0.0429  -0.0408 140 MET   A CE   
1028 C  CE   B MET   A 136 ? 0.2979 0.3859 0.3764 0.0385  -0.0321 -0.0146 140 MET   A CE   
1029 N  N    . LEU   A 137 ? 0.2030 0.3240 0.3305 0.0320  -0.0059 -0.0361 141 LEU   A N    
1030 C  CA   . LEU   A 137 ? 0.2076 0.3613 0.3476 0.0145  -0.0104 -0.0503 141 LEU   A CA   
1031 C  C    . LEU   A 137 ? 0.2087 0.4057 0.4029 -0.0175 -0.0001 -0.0714 141 LEU   A C    
1032 O  O    . LEU   A 137 ? 0.2130 0.4447 0.4340 -0.0287 -0.0123 -0.0911 141 LEU   A O    
1033 C  CB   . LEU   A 137 ? 0.2016 0.3611 0.3295 0.0191  -0.0248 -0.0487 141 LEU   A CB   
1034 C  CG   . LEU   A 137 ? 0.2210 0.3626 0.3394 0.0124  -0.0100 -0.0406 141 LEU   A CG   
1035 C  CD1  . LEU   A 137 ? 0.2040 0.3688 0.3391 0.0180  0.0053  -0.0436 141 LEU   A CD1  
1036 C  CD2  . LEU   A 137 ? 0.2482 0.3628 0.3612 0.0181  -0.0115 -0.0353 141 LEU   A CD2  
1037 N  N    . GLY   A 138 ? 0.2131 0.4357 0.4241 -0.0500 0.0501  -0.0803 142 GLY   A N    
1038 C  CA   . GLY   A 138 ? 0.2079 0.4692 0.4739 -0.0627 0.0617  -0.0798 142 GLY   A CA   
1039 C  C    . GLY   A 138 ? 0.2273 0.4604 0.4889 -0.0916 0.0981  -0.0867 142 GLY   A C    
1040 O  O    . GLY   A 138 ? 0.2782 0.5168 0.5762 -0.1280 0.1133  -0.0794 142 GLY   A O    
1041 N  N    . LEU   A 139 ? 0.2524 0.4553 0.5002 -0.0779 0.0988  -0.0888 143 LEU   A N    
1042 C  CA   . LEU   A 139 ? 0.2521 0.4464 0.5383 -0.0777 0.1110  -0.0836 143 LEU   A CA   
1043 C  C    . LEU   A 139 ? 0.2950 0.4519 0.5588 -0.0445 0.1226  -0.0696 143 LEU   A C    
1044 O  O    . LEU   A 139 ? 0.2513 0.4129 0.5792 -0.0451 0.1446  -0.0360 143 LEU   A O    
1045 C  CB   . LEU   A 139 ? 0.2465 0.4241 0.5471 -0.0810 0.1166  -0.0791 143 LEU   A CB   
1046 C  CG   . LEU   A 139 ? 0.2877 0.4396 0.5506 -0.0608 0.1234  -0.0680 143 LEU   A CG   
1047 C  CD1  . LEU   A 139 ? 0.2973 0.4368 0.5786 -0.0387 0.1236  -0.0703 143 LEU   A CD1  
1048 C  CD2  . LEU   A 139 ? 0.2922 0.4524 0.5568 -0.0603 0.1222  -0.0740 143 LEU   A CD2  
1049 N  N    . THR   A 140 ? 0.3532 0.4646 0.5864 -0.0082 0.1345  -0.0770 144 THR   A N    
1050 C  CA   . THR   A 140 ? 0.4233 0.4888 0.6130 0.0160  0.1217  -0.0819 144 THR   A CA   
1051 C  C    . THR   A 140 ? 0.4568 0.4914 0.6111 0.0389  0.1097  -0.0503 144 THR   A C    
1052 O  O    . THR   A 140 ? 0.4814 0.5309 0.6120 0.0262  0.1169  -0.0708 144 THR   A O    
1053 C  CB   . THR   A 140 ? 0.4526 0.4912 0.6431 0.0204  0.1260  -0.0926 144 THR   A CB   
1054 O  OG1  . THR   A 140 ? 0.4909 0.5637 0.7080 0.0364  0.1245  -0.1078 144 THR   A OG1  
1055 C  CG2  . THR   A 140 ? 0.4530 0.4668 0.6270 0.0263  0.1222  -0.1066 144 THR   A CG2  
1056 N  N    . SER   A 141 ? 0.4928 0.5073 0.6143 0.0440  0.0734  -0.0372 145 SER   A N    
1057 C  CA   . SER   A 141 ? 0.5116 0.5009 0.6148 0.0370  0.0523  -0.0203 145 SER   A CA   
1058 C  C    . SER   A 141 ? 0.4506 0.4629 0.5968 0.0218  0.0378  -0.0138 145 SER   A C    
1059 O  O    . SER   A 141 ? 0.4011 0.4647 0.5615 -0.0004 0.0158  0.0094  145 SER   A O    
1060 C  CB   . SER   A 141 ? 0.5070 0.5040 0.6170 0.0647  0.0564  -0.0045 145 SER   A CB   
1061 O  OG   . SER   A 141 ? 0.5390 0.5084 0.5924 0.0715  0.0650  -0.0196 145 SER   A OG   
1062 N  N    . ALA   A 142 ? 0.3893 0.4132 0.6027 0.0062  0.0262  -0.0093 146 ALA   A N    
1063 C  CA   . ALA   A 142 ? 0.3525 0.3785 0.6299 -0.0199 0.0119  -0.0107 146 ALA   A CA   
1064 C  C    . ALA   A 142 ? 0.3278 0.3341 0.6739 -0.0444 0.0131  -0.0105 146 ALA   A C    
1065 O  O    . ALA   A 142 ? 0.3700 0.3282 0.6998 -0.0718 0.0510  -0.0067 146 ALA   A O    
1066 C  CB   . ALA   A 142 ? 0.3685 0.3960 0.6217 -0.0173 0.0119  -0.0280 146 ALA   A CB   
1067 N  N    . LEU   A 143 ? 0.2961 0.3000 0.7096 -0.0142 -0.0345 0.0184  147 LEU   A N    
1068 C  CA   . LEU   A 143 ? 0.3069 0.3048 0.7371 -0.0068 -0.0350 0.0371  147 LEU   A CA   
1069 C  C    . LEU   A 143 ? 0.3332 0.2776 0.7319 -0.0139 -0.0553 0.0383  147 LEU   A C    
1070 O  O    . LEU   A 143 ? 0.3356 0.3165 0.7631 -0.0142 -0.0882 0.0649  147 LEU   A O    
1071 C  CB   . LEU   A 143 ? 0.2769 0.3475 0.7537 0.0058  -0.0316 0.0513  147 LEU   A CB   
1072 C  CG   . LEU   A 143 ? 0.3152 0.4440 0.7827 0.0097  -0.0208 0.0462  147 LEU   A CG   
1073 C  CD1  . LEU   A 143 ? 0.3232 0.4837 0.7691 0.0201  -0.0082 0.0632  147 LEU   A CD1  
1074 C  CD2  . LEU   A 143 ? 0.3310 0.4551 0.7996 -0.0134 -0.0073 0.0572  147 LEU   A CD2  
1075 N  N    . ASP   A 144 ? 0.4033 0.2974 0.7143 0.0004  -0.0523 0.0052  148 ASP   A N    
1076 C  CA   . ASP   A 144 ? 0.4477 0.3429 0.6888 -0.0025 -0.0464 0.0229  148 ASP   A CA   
1077 C  C    . ASP   A 144 ? 0.4134 0.3393 0.6802 0.0054  -0.0319 0.0160  148 ASP   A C    
1078 O  O    . ASP   A 144 ? 0.4237 0.3710 0.6662 0.0225  0.0043  0.0485  148 ASP   A O    
1079 C  CB   . ASP   A 144 ? 0.4472 0.4283 0.6704 -0.0014 -0.0352 -0.0069 148 ASP   A CB   
1080 C  CG   . ASP   A 144 ? 0.4293 0.4427 0.6509 0.0020  -0.0191 -0.0047 148 ASP   A CG   
1081 O  OD1  . ASP   A 144 ? 0.3860 0.4502 0.6157 0.0081  -0.0131 -0.0371 148 ASP   A OD1  
1082 O  OD2  . ASP   A 144 ? 0.4602 0.5031 0.6380 0.0175  -0.0104 -0.0353 148 ASP   A OD2  
1083 N  N    . GLY   A 145 ? 0.3650 0.3343 0.6760 0.0071  -0.0381 0.0256  149 GLY   A N    
1084 C  CA   . GLY   A 145 ? 0.2975 0.2844 0.6437 -0.0386 -0.0267 0.0188  149 GLY   A CA   
1085 C  C    . GLY   A 145 ? 0.2884 0.2619 0.5632 -0.0318 -0.0130 0.0241  149 GLY   A C    
1086 O  O    . GLY   A 145 ? 0.2614 0.2382 0.5795 -0.0472 -0.0202 0.0253  149 GLY   A O    
1087 N  N    . ALA   A 146 ? 0.2681 0.2450 0.4734 -0.0285 -0.0200 -0.0051 150 ALA   A N    
1088 C  CA   . ALA   A 146 ? 0.2439 0.2037 0.3545 -0.0160 0.0074  -0.0214 150 ALA   A CA   
1089 C  C    . ALA   A 146 ? 0.2312 0.1715 0.2980 -0.0006 0.0323  -0.0145 150 ALA   A C    
1090 O  O    . ALA   A 146 ? 0.2258 0.1936 0.3558 0.0117  0.0335  -0.0325 150 ALA   A O    
1091 C  CB   . ALA   A 146 ? 0.2826 0.2172 0.3536 -0.0338 0.0007  -0.0175 150 ALA   A CB   
1092 N  N    . PHE   A 147 ? 0.2333 0.1556 0.2151 0.0015  0.0265  -0.0089 151 PHE   A N    
1093 C  CA   . PHE   A 147 ? 0.2368 0.1454 0.1908 0.0056  0.0295  -0.0084 151 PHE   A CA   
1094 C  C    . PHE   A 147 ? 0.2321 0.1411 0.1603 0.0131  0.0231  -0.0062 151 PHE   A C    
1095 O  O    . PHE   A 147 ? 0.2187 0.1495 0.1521 0.0066  0.0219  0.0012  151 PHE   A O    
1096 C  CB   . PHE   A 147 ? 0.2466 0.1572 0.1880 0.0053  0.0359  0.0005  151 PHE   A CB   
1097 C  CG   . PHE   A 147 ? 0.2721 0.1655 0.1967 0.0003  0.0531  0.0169  151 PHE   A CG   
1098 C  CD1  . PHE   A 147 ? 0.2984 0.1701 0.2190 0.0003  0.0627  0.0124  151 PHE   A CD1  
1099 C  CD2  . PHE   A 147 ? 0.2777 0.1797 0.2113 -0.0009 0.0559  0.0151  151 PHE   A CD2  
1100 C  CE1  . PHE   A 147 ? 0.2978 0.1935 0.2149 0.0059  0.0657  0.0144  151 PHE   A CE1  
1101 C  CE2  . PHE   A 147 ? 0.2850 0.1765 0.2123 -0.0059 0.0593  0.0174  151 PHE   A CE2  
1102 C  CZ   . PHE   A 147 ? 0.2950 0.2043 0.2252 -0.0011 0.0659  0.0175  151 PHE   A CZ   
1103 N  N    . CYS   A 148 ? 0.2477 0.1546 0.1409 0.0092  0.0205  -0.0065 152 CYS   A N    
1104 C  CA   . CYS   A 148 ? 0.2519 0.1676 0.1500 0.0042  0.0092  -0.0106 152 CYS   A CA   
1105 C  C    . CYS   A 148 ? 0.2662 0.1622 0.1410 -0.0052 0.0025  -0.0103 152 CYS   A C    
1106 O  O    . CYS   A 148 ? 0.2809 0.1833 0.1443 -0.0038 0.0152  -0.0020 152 CYS   A O    
1107 C  CB   . CYS   A 148 ? 0.2643 0.1743 0.1713 0.0053  0.0115  -0.0104 152 CYS   A CB   
1108 S  SG   . CYS   A 148 ? 0.2935 0.1720 0.2141 0.0202  0.0225  -0.0155 152 CYS   A SG   
1109 N  N    A VAL   A 149 ? 0.2610 0.1557 0.1398 -0.0051 -0.0054 -0.0041 153 VAL   A N    
1110 N  N    B VAL   A 149 ? 0.2599 0.1547 0.1356 -0.0061 -0.0075 -0.0016 153 VAL   A N    
1111 C  CA   A VAL   A 149 ? 0.2724 0.1677 0.1513 -0.0136 -0.0121 -0.0061 153 VAL   A CA   
1112 C  CA   B VAL   A 149 ? 0.2707 0.1660 0.1439 -0.0147 -0.0149 -0.0016 153 VAL   A CA   
1113 C  C    A VAL   A 149 ? 0.2661 0.1650 0.1332 -0.0144 -0.0174 -0.0089 153 VAL   A C    
1114 C  C    B VAL   A 149 ? 0.2659 0.1639 0.1285 -0.0155 -0.0179 -0.0064 153 VAL   A C    
1115 O  O    A VAL   A 149 ? 0.2661 0.1705 0.1268 -0.0158 -0.0280 -0.0051 153 VAL   A O    
1116 O  O    B VAL   A 149 ? 0.2658 0.1686 0.1217 -0.0167 -0.0264 -0.0029 153 VAL   A O    
1117 C  CB   A VAL   A 149 ? 0.2770 0.1808 0.1799 -0.0131 -0.0142 0.0028  153 VAL   A CB   
1118 C  CB   B VAL   A 149 ? 0.2719 0.1759 0.1671 -0.0163 -0.0205 0.0097  153 VAL   A CB   
1119 C  CG1  A VAL   A 149 ? 0.2856 0.1934 0.1946 -0.0169 -0.0117 0.0070  153 VAL   A CG1  
1120 C  CG1  B VAL   A 149 ? 0.2724 0.1715 0.1831 -0.0200 -0.0204 0.0216  153 VAL   A CG1  
1121 C  CG2  A VAL   A 149 ? 0.2772 0.1713 0.1787 -0.0202 -0.0139 0.0006  153 VAL   A CG2  
1122 C  CG2  B VAL   A 149 ? 0.2769 0.1838 0.1777 -0.0207 -0.0189 0.0164  153 VAL   A CG2  
1123 N  N    . ASP   A 150 ? 0.2712 0.1596 0.1321 -0.0147 -0.0182 -0.0083 154 ASP   A N    
1124 C  CA   . ASP   A 150 ? 0.2799 0.1665 0.1400 -0.0211 -0.0203 -0.0091 154 ASP   A CA   
1125 C  C    . ASP   A 150 ? 0.2807 0.1719 0.1386 -0.0294 -0.0289 -0.0069 154 ASP   A C    
1126 O  O    . ASP   A 150 ? 0.2959 0.1819 0.1339 -0.0322 -0.0371 -0.0022 154 ASP   A O    
1127 C  CB   . ASP   A 150 ? 0.2976 0.1751 0.1544 -0.0127 -0.0206 -0.0150 154 ASP   A CB   
1128 C  CG   . ASP   A 150 ? 0.3123 0.1907 0.1752 -0.0139 -0.0223 -0.0117 154 ASP   A CG   
1129 O  OD1  . ASP   A 150 ? 0.3220 0.1852 0.1812 -0.0056 -0.0239 -0.0064 154 ASP   A OD1  
1130 O  OD2  . ASP   A 150 ? 0.3422 0.2011 0.2059 0.0000  -0.0229 -0.0049 154 ASP   A OD2  
1131 N  N    . SER   A 151 ? 0.2700 0.1733 0.1514 -0.0264 -0.0277 -0.0032 155 SER   A N    
1132 C  CA   . SER   A 151 ? 0.2699 0.1740 0.1723 -0.0280 -0.0419 -0.0040 155 SER   A CA   
1133 C  C    . SER   A 151 ? 0.2881 0.1851 0.1921 -0.0314 -0.0545 -0.0102 155 SER   A C    
1134 O  O    . SER   A 151 ? 0.2983 0.1904 0.2053 -0.0310 -0.0690 -0.0020 155 SER   A O    
1135 C  CB   . SER   A 151 ? 0.2529 0.1794 0.1701 -0.0240 -0.0409 -0.0060 155 SER   A CB   
1136 O  OG   . SER   A 151 ? 0.2461 0.1856 0.1670 -0.0051 -0.0348 -0.0010 155 SER   A OG   
1137 N  N    A ILE   A 152 ? 0.2983 0.1897 0.2029 -0.0340 -0.0581 -0.0087 156 ILE   A N    
1138 N  N    B ILE   A 152 ? 0.3057 0.1931 0.2090 -0.0320 -0.0547 -0.0046 156 ILE   A N    
1139 C  CA   A ILE   A 152 ? 0.3044 0.1950 0.2208 -0.0428 -0.0608 -0.0081 156 ILE   A CA   
1140 C  CA   B ILE   A 152 ? 0.3149 0.2045 0.2305 -0.0429 -0.0576 -0.0036 156 ILE   A CA   
1141 C  C    A ILE   A 152 ? 0.3185 0.2185 0.2178 -0.0453 -0.0591 -0.0138 156 ILE   A C    
1142 C  C    B ILE   A 152 ? 0.3233 0.2234 0.2247 -0.0449 -0.0569 -0.0112 156 ILE   A C    
1143 O  O    A ILE   A 152 ? 0.3213 0.2375 0.2352 -0.0562 -0.0657 -0.0145 156 ILE   A O    
1144 O  O    B ILE   A 152 ? 0.3260 0.2407 0.2402 -0.0562 -0.0631 -0.0113 156 ILE   A O    
1145 C  CB   A ILE   A 152 ? 0.3097 0.1929 0.2413 -0.0373 -0.0668 -0.0109 156 ILE   A CB   
1146 C  CB   B ILE   A 152 ? 0.3328 0.2087 0.2652 -0.0348 -0.0600 0.0003  156 ILE   A CB   
1147 C  CG1  A ILE   A 152 ? 0.3032 0.1834 0.2642 -0.0342 -0.0580 0.0009  156 ILE   A CG1  
1148 C  CG1  B ILE   A 152 ? 0.3370 0.2097 0.2830 -0.0343 -0.0464 0.0138  156 ILE   A CG1  
1149 C  CG2  A ILE   A 152 ? 0.3066 0.1943 0.2330 -0.0404 -0.0683 -0.0101 156 ILE   A CG2  
1150 C  CG2  B ILE   A 152 ? 0.3349 0.2152 0.2694 -0.0376 -0.0636 0.0068  156 ILE   A CG2  
1151 C  CD1  A ILE   A 152 ? 0.3023 0.1852 0.2658 -0.0351 -0.0563 0.0095  156 ILE   A CD1  
1152 C  CD1  B ILE   A 152 ? 0.3454 0.2071 0.3051 -0.0361 -0.0460 0.0146  156 ILE   A CD1  
1153 N  N    . THR   A 153 ? 0.3266 0.2210 0.1902 -0.0473 -0.0508 -0.0113 157 THR   A N    
1154 C  CA   . THR   A 153 ? 0.3517 0.2396 0.1867 -0.0444 -0.0481 -0.0187 157 THR   A CA   
1155 C  C    . THR   A 153 ? 0.3578 0.2442 0.1790 -0.0509 -0.0638 -0.0074 157 THR   A C    
1156 O  O    . THR   A 153 ? 0.3743 0.2742 0.1994 -0.0544 -0.0838 -0.0139 157 THR   A O    
1157 C  CB   . THR   A 153 ? 0.3582 0.2438 0.1847 -0.0377 -0.0277 -0.0197 157 THR   A CB   
1158 O  OG1  . THR   A 153 ? 0.3700 0.2506 0.1965 -0.0268 -0.0056 -0.0195 157 THR   A OG1  
1159 C  CG2  . THR   A 153 ? 0.3744 0.2549 0.1924 -0.0351 -0.0196 -0.0229 157 THR   A CG2  
1160 N  N    . ALA   A 154 ? 0.3610 0.2302 0.1796 -0.0487 -0.0750 0.0032  158 ALA   A N    
1161 C  CA   . ALA   A 154 ? 0.3546 0.2342 0.1967 -0.0493 -0.0776 0.0197  158 ALA   A CA   
1162 C  C    . ALA   A 154 ? 0.3516 0.2379 0.2071 -0.0496 -0.0913 0.0265  158 ALA   A C    
1163 O  O    . ALA   A 154 ? 0.3838 0.2630 0.2113 -0.0514 -0.1083 0.0382  158 ALA   A O    
1164 C  CB   . ALA   A 154 ? 0.3396 0.2196 0.1947 -0.0474 -0.0837 0.0209  158 ALA   A CB   
1165 N  N    . LEU   A 155 ? 0.3551 0.2402 0.2278 -0.0532 -0.0925 0.0343  159 LEU   A N    
1166 C  CA   . LEU   A 155 ? 0.3569 0.2626 0.2536 -0.0486 -0.0926 0.0354  159 LEU   A CA   
1167 C  C    . LEU   A 155 ? 0.3693 0.2963 0.2864 -0.0535 -0.1103 0.0158  159 LEU   A C    
1168 O  O    . LEU   A 155 ? 0.3653 0.2832 0.3123 -0.0458 -0.1218 0.0052  159 LEU   A O    
1169 C  CB   . LEU   A 155 ? 0.3717 0.2915 0.2674 -0.0463 -0.0748 0.0480  159 LEU   A CB   
1170 C  CG   . LEU   A 155 ? 0.4107 0.3315 0.2658 -0.0310 -0.0514 0.0385  159 LEU   A CG   
1171 C  CD1  . LEU   A 155 ? 0.4093 0.3489 0.2643 -0.0305 -0.0645 0.0402  159 LEU   A CD1  
1172 C  CD2  . LEU   A 155 ? 0.4248 0.3376 0.2850 -0.0264 -0.0391 0.0492  159 LEU   A CD2  
1173 N  N    . LYS   A 156 ? 0.3780 0.3045 0.3058 -0.0635 -0.1372 -0.0006 160 LYS   A N    
1174 C  CA   . LYS   A 156 ? 0.4288 0.3454 0.3252 -0.0709 -0.1497 -0.0092 160 LYS   A CA   
1175 C  C    . LYS   A 156 ? 0.4447 0.4013 0.3158 -0.0848 -0.1603 0.0081  160 LYS   A C    
1176 O  O    . LYS   A 156 ? 0.4672 0.4024 0.3325 -0.0691 -0.1787 0.0144  160 LYS   A O    
1177 C  CB   . LYS   A 156 ? 0.4518 0.3743 0.3754 -0.0704 -0.1508 -0.0401 160 LYS   A CB   
1178 C  CG   . LYS   A 156 ? 0.4675 0.3632 0.4290 -0.0741 -0.1390 -0.0497 160 LYS   A CG   
1179 C  CD   . LYS   A 156 ? 0.4945 0.3906 0.4863 -0.0483 -0.1190 -0.0618 160 LYS   A CD   
1180 C  CE   . LYS   A 156 ? 0.5171 0.3959 0.5212 -0.0445 -0.1090 -0.0646 160 LYS   A CE   
1181 N  NZ   . LYS   A 156 ? 0.5292 0.4258 0.5639 -0.0257 -0.1045 -0.0725 160 LYS   A NZ   
1182 N  N    . ALA   A 157 ? 0.4498 0.4469 0.2890 -0.0998 -0.1713 0.0325  161 ALA   A N    
1183 C  CA   . ALA   A 157 ? 0.4733 0.4820 0.2853 -0.0968 -0.1703 0.0546  161 ALA   A CA   
1184 C  C    . ALA   A 157 ? 0.4729 0.4771 0.2898 -0.0943 -0.1894 0.0985  161 ALA   A C    
1185 O  O    . ALA   A 157 ? 0.5126 0.5158 0.3009 -0.0707 -0.2003 0.1162  161 ALA   A O    
1186 C  CB   . ALA   A 157 ? 0.4787 0.4975 0.2816 -0.1031 -0.1489 0.0545  161 ALA   A CB   
1187 N  N    . LEU   A 158 ? 0.4520 0.4462 0.3175 -0.1046 -0.1903 0.1151  162 LEU   A N    
1188 C  CA   . LEU   A 158 ? 0.4702 0.4223 0.3564 -0.0976 -0.1929 0.1475  162 LEU   A CA   
1189 C  C    . LEU   A 158 ? 0.4726 0.4300 0.4025 -0.0932 -0.1975 0.1415  162 LEU   A C    
1190 O  O    . LEU   A 158 ? 0.4808 0.3800 0.4051 -0.0957 -0.2096 0.1313  162 LEU   A O    
1191 C  CB   . LEU   A 158 ? 0.5023 0.4146 0.4098 -0.1004 -0.1804 0.1251  162 LEU   A CB   
1192 C  CG   . LEU   A 158 ? 0.5223 0.4234 0.4720 -0.1045 -0.1660 0.1144  162 LEU   A CG   
1193 C  CD1  . LEU   A 158 ? 0.5339 0.4277 0.4969 -0.1149 -0.1599 0.0880  162 LEU   A CD1  
1194 C  CD2  . LEU   A 158 ? 0.5552 0.4223 0.4836 -0.0898 -0.1606 0.1122  162 LEU   A CD2  
1195 N  N    . GLU   A 159 ? 0.4754 0.4327 0.4390 -0.1193 -0.2065 0.1177  163 GLU   A N    
1196 C  CA   . GLU   A 159 ? 0.4890 0.5029 0.4887 -0.1172 -0.2216 0.1100  163 GLU   A CA   
1197 C  C    . GLU   A 159 ? 0.5239 0.5143 0.4937 -0.1280 -0.2299 0.0896  163 GLU   A C    
1198 O  O    . GLU   A 159 ? 0.5101 0.5501 0.5342 -0.1265 -0.2390 0.0860  163 GLU   A O    
1199 C  CB   . GLU   A 159 ? 0.5509 0.5123 0.5482 -0.1049 -0.2064 0.1285  163 GLU   A CB   
1200 C  CG   . GLU   A 159 ? 0.6032 0.5729 0.6123 -0.0764 -0.1909 0.1180  163 GLU   A CG   
1201 C  CD   . GLU   A 159 ? 0.6219 0.6062 0.6660 -0.0588 -0.1852 0.1375  163 GLU   A CD   
1202 O  OE1  . GLU   A 159 ? 0.6883 0.6371 0.7094 -0.0081 -0.1839 0.1295  163 GLU   A OE1  
1203 O  OE2  . GLU   A 159 ? 0.6236 0.6348 0.7486 -0.0456 -0.1891 0.1113  163 GLU   A OE2  
1204 N  N    . ARG   A 160 ? 0.5499 0.5104 0.4689 -0.1183 -0.2511 0.0662  164 ARG   A N    
1205 C  CA   . ARG   A 160 ? 0.5922 0.5489 0.4590 -0.0983 -0.2557 0.0821  164 ARG   A CA   
1206 C  C    . ARG   A 160 ? 0.6252 0.5899 0.4684 -0.0811 -0.2657 0.0968  164 ARG   A C    
1207 O  O    . ARG   A 160 ? 0.6703 0.6285 0.4504 -0.0410 -0.2776 0.0957  164 ARG   A O    
1208 C  CB   . ARG   A 160 ? 0.5876 0.5620 0.4873 -0.1068 -0.2384 0.0646  164 ARG   A CB   
1209 N  N    . ALA   A 161 ? 0.6465 0.5715 0.4786 -0.0745 -0.2605 0.1230  165 ALA   A N    
1210 C  CA   . ALA   A 161 ? 0.6608 0.6023 0.4583 -0.0644 -0.2416 0.1715  165 ALA   A CA   
1211 C  C    . ALA   A 161 ? 0.6607 0.6287 0.5000 -0.0503 -0.2450 0.1669  165 ALA   A C    
1212 O  O    . ALA   A 161 ? 0.6999 0.6037 0.4664 -0.0622 -0.2217 0.1749  165 ALA   A O    
1213 C  CB   . ALA   A 161 ? 0.6616 0.5726 0.4682 -0.0734 -0.2194 0.1975  165 ALA   A CB   
1214 N  N    . SER   A 162 ? 0.6431 0.6664 0.5374 -0.0463 -0.2252 0.1663  166 SER   A N    
1215 C  CA   . SER   A 162 ? 0.6592 0.6981 0.6016 -0.0329 -0.2302 0.1529  166 SER   A CA   
1216 C  C    . SER   A 162 ? 0.6737 0.7307 0.6539 -0.0378 -0.2575 0.1382  166 SER   A C    
1217 O  O    . SER   A 162 ? 0.6916 0.7895 0.7725 0.0000  -0.2250 0.1176  166 SER   A O    
1218 C  CB   . SER   A 162 ? 0.6623 0.6939 0.5976 -0.0443 -0.1890 0.1461  166 SER   A CB   
1219 N  N    . SER   A 163 ? 0.6963 0.7403 0.7076 -0.0364 -0.2865 0.1082  167 SER   A N    
1220 C  CA   . SER   A 163 ? 0.7253 0.7495 0.7609 -0.0478 -0.2879 0.0805  167 SER   A CA   
1221 C  C    . SER   A 163 ? 0.7357 0.7692 0.8062 -0.0483 -0.3051 0.0314  167 SER   A C    
1222 O  O    . SER   A 163 ? 0.7650 0.7675 0.8949 -0.0562 -0.3037 -0.0121 167 SER   A O    
1223 C  CB   . SER   A 163 ? 0.7386 0.7473 0.7725 -0.0510 -0.2810 0.0816  167 SER   A CB   
1224 N  N    . LYS   A 171 ? 0.5920 0.6545 0.5793 -0.0286 -0.1816 -0.1245 175 LYS   A N    
1225 C  CA   . LYS   A 171 ? 0.5518 0.6363 0.5774 -0.0367 -0.1896 -0.1234 175 LYS   A CA   
1226 C  C    . LYS   A 171 ? 0.5129 0.5678 0.5324 -0.0818 -0.1806 -0.1333 175 LYS   A C    
1227 O  O    . LYS   A 171 ? 0.5091 0.5943 0.5002 -0.0632 -0.2104 -0.1447 175 LYS   A O    
1228 C  CB   . LYS   A 171 ? 0.5976 0.6444 0.6212 -0.0330 -0.1599 -0.1404 175 LYS   A CB   
1229 C  CG   . LYS   A 171 ? 0.6453 0.6496 0.6565 -0.0313 -0.1447 -0.1471 175 LYS   A CG   
1230 C  CD   . LYS   A 171 ? 0.6745 0.6820 0.7141 -0.0032 -0.1312 -0.1334 175 LYS   A CD   
1231 C  CE   . LYS   A 171 ? 0.7090 0.6849 0.7447 0.0021  -0.1184 -0.1115 175 LYS   A CE   
1232 N  NZ   . LYS   A 171 ? 0.7358 0.6822 0.7882 0.0136  -0.0964 -0.0959 175 LYS   A NZ   
1233 N  N    . SER   A 172 ? 0.4356 0.5030 0.5206 -0.0960 -0.1951 -0.0990 176 SER   A N    
1234 C  CA   . SER   A 172 ? 0.4213 0.4032 0.4850 -0.0987 -0.1785 -0.0958 176 SER   A CA   
1235 C  C    . SER   A 172 ? 0.3779 0.3932 0.4513 -0.0830 -0.1735 -0.0716 176 SER   A C    
1236 O  O    . SER   A 172 ? 0.3767 0.4031 0.4435 -0.0783 -0.1837 -0.0439 176 SER   A O    
1237 C  CB   . SER   A 172 ? 0.4416 0.3812 0.5082 -0.1039 -0.1625 -0.0893 176 SER   A CB   
1238 O  OG   . SER   A 172 ? 0.4536 0.3562 0.5150 -0.1162 -0.1568 -0.0820 176 SER   A OG   
1239 N  N    . TYR   A 173 ? 0.3618 0.3590 0.4256 -0.0824 -0.1604 -0.0769 177 TYR   A N    
1240 C  CA   . TYR   A 173 ? 0.3482 0.3534 0.3784 -0.0790 -0.1580 -0.0702 177 TYR   A CA   
1241 C  C    . TYR   A 173 ? 0.3289 0.3262 0.3648 -0.0613 -0.1273 -0.0298 177 TYR   A C    
1242 O  O    . TYR   A 173 ? 0.3270 0.2799 0.3491 -0.0583 -0.1197 -0.0253 177 TYR   A O    
1243 C  CB   . TYR   A 173 ? 0.3796 0.4040 0.3715 -0.0801 -0.1509 -0.0738 177 TYR   A CB   
1244 C  CG   . TYR   A 173 ? 0.4392 0.4943 0.3828 -0.0695 -0.1480 -0.0382 177 TYR   A CG   
1245 C  CD1  . TYR   A 173 ? 0.4934 0.5344 0.3800 -0.0630 -0.1479 -0.0264 177 TYR   A CD1  
1246 C  CD2  . TYR   A 173 ? 0.4807 0.5518 0.3873 -0.0727 -0.1653 -0.0419 177 TYR   A CD2  
1247 C  CE1  . TYR   A 173 ? 0.4955 0.5813 0.3985 -0.0664 -0.1695 -0.0176 177 TYR   A CE1  
1248 C  CE2  . TYR   A 173 ? 0.4982 0.6017 0.3908 -0.0681 -0.1848 -0.0282 177 TYR   A CE2  
1249 C  CZ   . TYR   A 173 ? 0.5110 0.6094 0.3933 -0.0694 -0.1900 -0.0212 177 TYR   A CZ   
1250 O  OH   . TYR   A 173 ? 0.5436 0.7030 0.3982 -0.0756 -0.2103 0.0000  177 TYR   A OH   
1251 N  N    . SER   A 174 ? 0.3228 0.2897 0.3477 -0.0570 -0.1240 -0.0298 178 SER   A N    
1252 C  CA   . SER   A 174 ? 0.3111 0.2806 0.3431 -0.0587 -0.1082 -0.0229 178 SER   A CA   
1253 C  C    . SER   A 174 ? 0.2829 0.2666 0.3011 -0.0551 -0.0995 -0.0132 178 SER   A C    
1254 O  O    . SER   A 174 ? 0.2818 0.2674 0.3090 -0.0549 -0.1108 -0.0184 178 SER   A O    
1255 C  CB   . SER   A 174 ? 0.3309 0.2914 0.3758 -0.0612 -0.0916 -0.0156 178 SER   A CB   
1256 O  OG   . SER   A 174 ? 0.3335 0.3264 0.4142 -0.0708 -0.0902 -0.0050 178 SER   A OG   
1257 N  N    . LEU   A 175 ? 0.2695 0.2657 0.2872 -0.0517 -0.0885 -0.0023 179 LEU   A N    
1258 C  CA   . LEU   A 175 ? 0.2776 0.2612 0.2713 -0.0434 -0.0799 -0.0032 179 LEU   A CA   
1259 C  C    . LEU   A 175 ? 0.2877 0.2717 0.2976 -0.0541 -0.0705 -0.0042 179 LEU   A C    
1260 O  O    . LEU   A 175 ? 0.2962 0.2675 0.3099 -0.0491 -0.0587 -0.0250 179 LEU   A O    
1261 C  CB   . LEU   A 175 ? 0.2864 0.2633 0.2672 -0.0352 -0.0780 -0.0058 179 LEU   A CB   
1262 C  CG   . LEU   A 175 ? 0.2951 0.2724 0.2747 -0.0299 -0.0680 -0.0099 179 LEU   A CG   
1263 C  CD1  . LEU   A 175 ? 0.3038 0.2613 0.2859 -0.0342 -0.0712 -0.0062 179 LEU   A CD1  
1264 C  CD2  . LEU   A 175 ? 0.2988 0.2882 0.2639 -0.0306 -0.0641 -0.0153 179 LEU   A CD2  
1265 N  N    . GLY   A 176 ? 0.3029 0.2790 0.3274 -0.0618 -0.0689 0.0090  180 GLY   A N    
1266 C  CA   . GLY   A 176 ? 0.3074 0.2952 0.3662 -0.0654 -0.0649 0.0094  180 GLY   A CA   
1267 C  C    . GLY   A 176 ? 0.3201 0.3168 0.3839 -0.0624 -0.0720 0.0108  180 GLY   A C    
1268 O  O    . GLY   A 176 ? 0.2955 0.3669 0.4323 -0.0716 -0.0574 0.0168  180 GLY   A O    
1269 N  N    . SER   A 177 ? 0.3212 0.3234 0.3949 -0.0669 -0.0825 0.0031  181 SER   A N    
1270 C  CA   . SER   A 177 ? 0.3084 0.3281 0.4183 -0.0779 -0.0837 0.0011  181 SER   A CA   
1271 C  C    . SER   A 177 ? 0.2777 0.3126 0.4327 -0.0683 -0.0908 -0.0031 181 SER   A C    
1272 O  O    . SER   A 177 ? 0.2724 0.3056 0.4744 -0.0673 -0.0911 -0.0123 181 SER   A O    
1273 C  CB   . SER   A 177 ? 0.3309 0.3263 0.4169 -0.0947 -0.0862 -0.0054 181 SER   A CB   
1274 O  OG   . SER   A 177 ? 0.4075 0.3471 0.4389 -0.1131 -0.0671 0.0084  181 SER   A OG   
1275 N  N    . ILE   A 178 ? 0.2672 0.2879 0.3965 -0.0611 -0.1010 -0.0024 182 ILE   A N    
1276 C  CA   . ILE   A 178 ? 0.2684 0.2903 0.3875 -0.0617 -0.0946 -0.0006 182 ILE   A CA   
1277 C  C    . ILE   A 178 ? 0.2452 0.3055 0.4171 -0.0567 -0.0865 -0.0040 182 ILE   A C    
1278 O  O    . ILE   A 178 ? 0.2507 0.2987 0.4445 -0.0616 -0.0952 0.0039  182 ILE   A O    
1279 C  CB   . ILE   A 178 ? 0.2730 0.2696 0.3680 -0.0632 -0.0936 0.0021  182 ILE   A CB   
1280 C  CG1  . ILE   A 178 ? 0.2819 0.2838 0.3455 -0.0671 -0.0910 0.0094  182 ILE   A CG1  
1281 C  CG2  . ILE   A 178 ? 0.2814 0.2762 0.3706 -0.0679 -0.0941 0.0034  182 ILE   A CG2  
1282 C  CD1  . ILE   A 178 ? 0.2840 0.2877 0.3499 -0.0615 -0.0895 0.0051  182 ILE   A CD1  
1283 N  N    . TYR   A 179 ? 0.2343 0.3172 0.4203 -0.0480 -0.0724 -0.0068 183 TYR   A N    
1284 C  CA   . TYR   A 179 ? 0.2276 0.3377 0.4449 -0.0554 -0.0641 -0.0230 183 TYR   A CA   
1285 C  C    . TYR   A 179 ? 0.2314 0.3802 0.5112 -0.0585 -0.0814 -0.0394 183 TYR   A C    
1286 O  O    . TYR   A 179 ? 0.2580 0.3960 0.5375 -0.0478 -0.0809 -0.0657 183 TYR   A O    
1287 C  CB   . TYR   A 179 ? 0.2385 0.3359 0.4242 -0.0578 -0.0368 -0.0253 183 TYR   A CB   
1288 C  CG   . TYR   A 179 ? 0.2427 0.3473 0.4194 -0.0649 -0.0172 -0.0235 183 TYR   A CG   
1289 C  CD1  . TYR   A 179 ? 0.2541 0.3602 0.4386 -0.0692 -0.0050 -0.0313 183 TYR   A CD1  
1290 C  CD2  . TYR   A 179 ? 0.2287 0.3385 0.3816 -0.0575 -0.0217 -0.0123 183 TYR   A CD2  
1291 C  CE1  . TYR   A 179 ? 0.2508 0.3503 0.4308 -0.0647 -0.0061 -0.0301 183 TYR   A CE1  
1292 C  CE2  . TYR   A 179 ? 0.2273 0.3212 0.3929 -0.0579 -0.0097 -0.0168 183 TYR   A CE2  
1293 C  CZ   . TYR   A 179 ? 0.2436 0.3380 0.4076 -0.0609 -0.0032 -0.0265 183 TYR   A CZ   
1294 O  OH   . TYR   A 179 ? 0.2772 0.3313 0.4055 -0.0404 -0.0080 -0.0198 183 TYR   A OH   
1295 N  N    . THR   A 180 ? 0.2410 0.4112 0.5790 -0.0628 -0.0841 -0.0438 184 THR   A N    
1296 C  CA   . THR   A 180 ? 0.2413 0.4277 0.6331 -0.0659 -0.0907 -0.0536 184 THR   A CA   
1297 C  C    . THR   A 180 ? 0.2352 0.4229 0.6656 -0.0475 -0.1230 -0.0669 184 THR   A C    
1298 O  O    . THR   A 180 ? 0.2649 0.4683 0.7119 -0.0208 -0.1235 -0.1065 184 THR   A O    
1299 C  CB   . THR   A 180 ? 0.2625 0.4543 0.6547 -0.0849 -0.0830 -0.0302 184 THR   A CB   
1300 O  OG1  . THR   A 180 ? 0.3245 0.4929 0.6756 -0.0916 -0.0581 -0.0039 184 THR   A OG1  
1301 C  CG2  . THR   A 180 ? 0.2702 0.4946 0.6671 -0.0864 -0.0710 -0.0256 184 THR   A CG2  
1302 N  N    . ARG   A 181 ? 0.2406 0.4219 0.6794 -0.0119 -0.1603 -0.0692 185 ARG   A N    
1303 C  CA   . ARG   A 181 ? 0.2442 0.4503 0.6990 0.0012  -0.1958 -0.0569 185 ARG   A CA   
1304 C  C    . ARG   A 181 ? 0.2552 0.4718 0.7231 0.0161  -0.2235 -0.0499 185 ARG   A C    
1305 O  O    . ARG   A 181 ? 0.2660 0.5077 0.7626 0.0250  -0.2424 -0.0464 185 ARG   A O    
1306 C  CB   . ARG   A 181 ? 0.2986 0.4933 0.7028 0.0152  -0.1814 -0.0521 185 ARG   A CB   
1307 C  CG   . ARG   A 181 ? 0.3618 0.5264 0.6969 0.0250  -0.1704 -0.0589 185 ARG   A CG   
1308 C  CD   . ARG   A 181 ? 0.3697 0.5117 0.6635 0.0263  -0.1839 -0.0678 185 ARG   A CD   
1309 N  NE   . ARG   A 181 ? 0.3721 0.5071 0.5965 0.0207  -0.2086 -0.0705 185 ARG   A NE   
1310 C  CZ   . ARG   A 181 ? 0.3712 0.5104 0.5656 0.0294  -0.1979 -0.0688 185 ARG   A CZ   
1311 N  NH1  . ARG   A 181 ? 0.3713 0.5118 0.5556 0.0506  -0.1858 -0.0563 185 ARG   A NH1  
1312 N  NH2  . ARG   A 181 ? 0.3642 0.5047 0.5178 0.0271  -0.2236 -0.0724 185 ARG   A NH2  
1313 N  N    . LEU   A 182 ? 0.2835 0.4370 0.7210 0.0005  -0.2337 -0.0353 186 LEU   A N    
1314 C  CA   . LEU   A 182 ? 0.3009 0.4359 0.7355 0.0048  -0.2309 -0.0278 186 LEU   A CA   
1315 C  C    . LEU   A 182 ? 0.2724 0.4656 0.7932 -0.0025 -0.2031 -0.0479 186 LEU   A C    
1316 O  O    . LEU   A 182 ? 0.3103 0.4634 0.8586 0.0177  -0.2135 -0.0453 186 LEU   A O    
1317 C  CB   . LEU   A 182 ? 0.3087 0.4093 0.6901 -0.0038 -0.2545 0.0049  186 LEU   A CB   
1318 C  CG   . LEU   A 182 ? 0.3623 0.4150 0.6605 -0.0312 -0.2590 0.0282  186 LEU   A CG   
1319 C  CD1  . LEU   A 182 ? 0.3760 0.3890 0.6581 -0.0419 -0.2528 0.0361  186 LEU   A CD1  
1320 C  CD2  . LEU   A 182 ? 0.3993 0.4423 0.6577 -0.0576 -0.2614 0.0255  186 LEU   A CD2  
1321 N  N    . TYR   A 183 ? 0.2433 0.4752 0.8254 -0.0252 -0.1455 -0.0750 187 TYR   A N    
1322 C  CA   . TYR   A 183 ? 0.2631 0.5169 0.8318 -0.0488 -0.0902 -0.1020 187 TYR   A CA   
1323 C  C    . TYR   A 183 ? 0.3155 0.5940 0.9144 -0.0744 -0.0177 -0.1480 187 TYR   A C    
1324 O  O    . TYR   A 183 ? 0.3319 0.6604 0.9707 -0.0833 0.0284  -0.1914 187 TYR   A O    
1325 C  CB   . TYR   A 183 ? 0.2827 0.4648 0.7702 -0.0419 -0.0748 -0.0714 187 TYR   A CB   
1326 C  CG   . TYR   A 183 ? 0.2490 0.4265 0.6755 -0.0212 -0.1063 -0.0475 187 TYR   A CG   
1327 C  CD1  . TYR   A 183 ? 0.2329 0.4279 0.6291 -0.0193 -0.1218 -0.0310 187 TYR   A CD1  
1328 C  CD2  . TYR   A 183 ? 0.2302 0.3906 0.6025 -0.0333 -0.1045 -0.0292 187 TYR   A CD2  
1329 C  CE1  . TYR   A 183 ? 0.2220 0.3997 0.5900 0.0022  -0.1170 -0.0209 187 TYR   A CE1  
1330 C  CE2  . TYR   A 183 ? 0.2092 0.3744 0.5607 -0.0288 -0.1225 -0.0313 187 TYR   A CE2  
1331 C  CZ   . TYR   A 183 ? 0.2113 0.3828 0.5384 -0.0060 -0.1315 -0.0158 187 TYR   A CZ   
1332 O  OH   . TYR   A 183 ? 0.2441 0.3581 0.4894 0.0282  -0.1194 0.0487  187 TYR   A OH   
1333 N  N    . GLY   A 184 ? 0.3606 0.6127 0.9588 -0.1013 0.0171  -0.1824 188 GLY   A N    
1334 C  CA   . GLY   A 184 ? 0.3966 0.6490 0.9819 -0.1387 0.0443  -0.1835 188 GLY   A CA   
1335 C  C    . GLY   A 184 ? 0.4181 0.6960 1.0033 -0.1596 0.0934  -0.1829 188 GLY   A C    
1336 O  O    . GLY   A 184 ? 0.4270 0.7977 1.0510 -0.1338 0.1111  -0.1876 188 GLY   A O    
1337 N  N    . GLN   A 185 ? 0.4345 0.6870 0.9972 -0.1752 0.0998  -0.1872 189 GLN   A N    
1338 C  CA   . GLN   A 185 ? 0.4723 0.7184 1.0071 -0.1986 0.1269  -0.1567 189 GLN   A CA   
1339 C  C    . GLN   A 185 ? 0.4868 0.7258 0.9859 -0.2170 0.1421  -0.1094 189 GLN   A C    
1340 O  O    . GLN   A 185 ? 0.4707 0.7557 0.9813 -0.2272 0.1297  -0.1266 189 GLN   A O    
1341 C  CB   . GLN   A 185 ? 0.5096 0.7634 1.0333 -0.1573 0.1344  -0.1647 189 GLN   A CB   
1342 C  CG   . GLN   A 185 ? 0.5125 0.7742 1.0589 -0.1514 0.1216  -0.1805 189 GLN   A CG   
1343 C  CD   . GLN   A 185 ? 0.5168 0.7883 1.0529 -0.1340 0.1312  -0.1916 189 GLN   A CD   
1344 O  OE1  . GLN   A 185 ? 0.6035 0.8234 1.0723 -0.0631 0.1331  -0.2045 189 GLN   A OE1  
1345 N  NE2  . GLN   A 185 ? 0.4497 0.7612 1.0461 -0.1650 0.1736  -0.1690 189 GLN   A NE2  
1346 N  N    . SER   A 186 ? 0.5243 0.7459 0.9881 -0.2473 0.1564  -0.0746 190 SER   A N    
1347 C  CA   . SER   A 186 ? 0.5839 0.7412 0.9724 -0.2207 0.1837  -0.0274 190 SER   A CA   
1348 C  C    . SER   A 186 ? 0.5902 0.7180 0.9411 -0.2107 0.1960  -0.0048 190 SER   A C    
1349 O  O    . SER   A 186 ? 0.6116 0.7154 0.9256 -0.2157 0.2332  0.0017  190 SER   A O    
1350 C  CB   . SER   A 186 ? 0.5956 0.7713 0.9520 -0.2246 0.1989  -0.0121 190 SER   A CB   
1351 N  N    . PRO   A 187 ? 0.6270 0.6595 0.8966 -0.1621 0.2018  0.0652  191 PRO   A N    
1352 C  CA   . PRO   A 187 ? 0.6168 0.6327 0.8560 -0.1325 0.1930  0.0916  191 PRO   A CA   
1353 C  C    . PRO   A 187 ? 0.6093 0.5783 0.8431 -0.1059 0.1915  0.1218  191 PRO   A C    
1354 O  O    . PRO   A 187 ? 0.7139 0.5769 0.8502 -0.0905 0.2318  0.1472  191 PRO   A O    
1355 C  CB   . PRO   A 187 ? 0.6236 0.6417 0.8534 -0.1394 0.2029  0.0929  191 PRO   A CB   
1356 C  CG   . PRO   A 187 ? 0.6416 0.6418 0.8637 -0.1371 0.2022  0.0856  191 PRO   A CG   
1357 C  CD   . PRO   A 187 ? 0.6229 0.6470 0.8678 -0.1574 0.2155  0.0860  191 PRO   A CD   
1358 N  N    . PRO   A 188 ? 0.5791 0.5200 0.8232 -0.0199 0.1683  0.1397  192 PRO   A N    
1359 C  CA   . PRO   A 188 ? 0.5807 0.5319 0.8137 0.0000  0.1598  0.1403  192 PRO   A CA   
1360 C  C    . PRO   A 188 ? 0.6321 0.5642 0.7990 0.0159  0.1336  0.1466  192 PRO   A C    
1361 O  O    . PRO   A 188 ? 0.6357 0.6223 0.7803 0.0223  0.1724  0.1363  192 PRO   A O    
1362 C  CB   . PRO   A 188 ? 0.5590 0.5259 0.8204 -0.0028 0.1444  0.1326  192 PRO   A CB   
1363 C  CG   . PRO   A 188 ? 0.5577 0.5151 0.8244 -0.0231 0.1522  0.1322  192 PRO   A CG   
1364 C  CD   . PRO   A 188 ? 0.5463 0.5169 0.8346 -0.0243 0.1583  0.1346  192 PRO   A CD   
1365 N  N    . ASP   A 189 ? 0.6538 0.5816 0.7640 0.0358  0.0937  0.1218  193 ASP   A N    
1366 C  CA   . ASP   A 189 ? 0.6898 0.5505 0.6873 0.0164  0.0698  0.0907  193 ASP   A CA   
1367 C  C    . ASP   A 189 ? 0.6615 0.4737 0.6910 -0.0152 0.0487  0.0606  193 ASP   A C    
1368 O  O    . ASP   A 189 ? 0.6977 0.4698 0.6763 -0.0736 0.0628  0.0238  193 ASP   A O    
1369 C  CB   . ASP   A 189 ? 0.6934 0.5806 0.6388 0.0203  0.0545  0.1176  193 ASP   A CB   
1370 C  CG   . ASP   A 189 ? 0.7319 0.6085 0.6180 0.0363  0.0618  0.1354  193 ASP   A CG   
1371 O  OD1  . ASP   A 189 ? 0.8024 0.6564 0.6485 0.0719  0.0297  0.0695  193 ASP   A OD1  
1372 O  OD2  . ASP   A 189 ? 0.7084 0.6584 0.5773 0.0519  0.0647  0.1671  193 ASP   A OD2  
1373 N  N    . SER   A 190 ? 0.6166 0.4478 0.6516 -0.0340 0.0156  0.0277  194 SER   A N    
1374 C  CA   . SER   A 190 ? 0.5596 0.4366 0.6165 -0.0278 -0.0203 0.0236  194 SER   A CA   
1375 C  C    . SER   A 190 ? 0.5395 0.4214 0.5478 -0.0340 -0.0283 0.0203  194 SER   A C    
1376 O  O    . SER   A 190 ? 0.5727 0.4340 0.5563 -0.0118 -0.0148 0.0196  194 SER   A O    
1377 C  CB   . SER   A 190 ? 0.5733 0.4440 0.6148 -0.0424 -0.0332 -0.0202 194 SER   A CB   
1378 N  N    . HIS   A 191 ? 0.4361 0.3392 0.5002 -0.0586 -0.0223 0.0600  195 HIS   A N    
1379 C  CA   . HIS   A 191 ? 0.3244 0.3598 0.4444 -0.0315 -0.0131 0.0260  195 HIS   A CA   
1380 C  C    . HIS   A 191 ? 0.2836 0.2496 0.3512 -0.0303 -0.0066 0.0413  195 HIS   A C    
1381 O  O    . HIS   A 191 ? 0.2719 0.2519 0.3835 -0.0267 -0.0048 0.0403  195 HIS   A O    
1382 C  CB   . HIS   A 191 ? 0.3822 0.3891 0.4782 -0.0426 -0.0027 0.0387  195 HIS   A CB   
1383 C  CG   . HIS   A 191 ? 0.4349 0.4867 0.4977 -0.0106 -0.0109 -0.0042 195 HIS   A CG   
1384 N  ND1  . HIS   A 191 ? 0.4804 0.5054 0.5216 0.0147  -0.0358 0.0043  195 HIS   A ND1  
1385 C  CD2  . HIS   A 191 ? 0.4446 0.5221 0.5086 -0.0103 -0.0198 -0.0011 195 HIS   A CD2  
1386 C  CE1  . HIS   A 191 ? 0.4591 0.5118 0.5050 0.0215  0.0011  -0.0091 195 HIS   A CE1  
1387 N  NE2  . HIS   A 191 ? 0.4153 0.5312 0.4803 -0.0177 0.0034  -0.0250 195 HIS   A NE2  
1388 N  N    . THR   A 192 ? 0.2183 0.2316 0.2824 -0.0194 -0.0106 0.0500  196 THR   A N    
1389 C  CA   . THR   A 192 ? 0.2044 0.1989 0.2325 -0.0089 -0.0026 0.0525  196 THR   A CA   
1390 C  C    . THR   A 192 ? 0.1889 0.1714 0.2050 -0.0086 -0.0144 0.0409  196 THR   A C    
1391 O  O    . THR   A 192 ? 0.1883 0.1643 0.2017 -0.0165 -0.0168 0.0347  196 THR   A O    
1392 C  CB   . THR   A 192 ? 0.2187 0.2160 0.2270 0.0060  0.0065  0.0534  196 THR   A CB   
1393 O  OG1  . THR   A 192 ? 0.2413 0.2151 0.2179 0.0133  0.0092  0.0478  196 THR   A OG1  
1394 C  CG2  . THR   A 192 ? 0.2222 0.2407 0.2382 0.0198  0.0159  0.0521  196 THR   A CG2  
1395 N  N    . ALA   A 193 ? 0.1860 0.1490 0.1802 -0.0014 -0.0101 0.0406  197 ALA   A N    
1396 C  CA   . ALA   A 193 ? 0.1811 0.1505 0.1674 0.0023  -0.0077 0.0271  197 ALA   A CA   
1397 C  C    . ALA   A 193 ? 0.1791 0.1489 0.1556 0.0061  -0.0080 0.0219  197 ALA   A C    
1398 O  O    . ALA   A 193 ? 0.1893 0.1429 0.1473 0.0122  -0.0117 0.0102  197 ALA   A O    
1399 C  CB   . ALA   A 193 ? 0.1857 0.1461 0.1749 0.0014  -0.0087 0.0315  197 ALA   A CB   
1400 N  N    . GLU   A 194 ? 0.1757 0.1537 0.1537 0.0039  -0.0088 0.0190  198 GLU   A N    
1401 C  CA   . GLU   A 194 ? 0.1869 0.1584 0.1601 -0.0004 -0.0033 0.0110  198 GLU   A CA   
1402 C  C    . GLU   A 194 ? 0.1881 0.1613 0.1596 0.0003  -0.0046 0.0122  198 GLU   A C    
1403 O  O    . GLU   A 194 ? 0.1908 0.1664 0.1511 0.0011  -0.0118 0.0095  198 GLU   A O    
1404 C  CB   . GLU   A 194 ? 0.2254 0.1890 0.1695 0.0001  -0.0085 0.0054  198 GLU   A CB   
1405 C  CG   . GLU   A 194 ? 0.2599 0.1998 0.2037 0.0065  -0.0070 -0.0070 198 GLU   A CG   
1406 C  CD   . GLU   A 194 ? 0.3123 0.2395 0.2345 0.0081  -0.0045 -0.0257 198 GLU   A CD   
1407 O  OE1  . GLU   A 194 ? 0.4348 0.3295 0.2589 0.0100  -0.0323 -0.0207 198 GLU   A OE1  
1408 O  OE2  . GLU   A 194 ? 0.3460 0.2535 0.3430 -0.0003 0.0160  -0.0501 198 GLU   A OE2  
1409 N  N    . GLY   A 195 ? 0.1915 0.1718 0.1703 -0.0018 -0.0041 0.0191  199 GLY   A N    
1410 C  CA   . GLY   A 195 ? 0.1816 0.1687 0.1840 -0.0106 0.0015  0.0175  199 GLY   A CA   
1411 C  C    . GLY   A 195 ? 0.1789 0.1723 0.1862 -0.0035 -0.0085 0.0232  199 GLY   A C    
1412 O  O    . GLY   A 195 ? 0.1885 0.1797 0.2152 0.0145  -0.0128 0.0269  199 GLY   A O    
1413 N  N    . ASP   A 196 ? 0.1748 0.1623 0.1887 -0.0026 -0.0152 0.0235  200 ASP   A N    
1414 C  CA   . ASP   A 196 ? 0.1819 0.1720 0.1952 -0.0104 -0.0145 0.0109  200 ASP   A CA   
1415 C  C    . ASP   A 196 ? 0.1687 0.1660 0.1812 -0.0058 -0.0182 0.0097  200 ASP   A C    
1416 O  O    . ASP   A 196 ? 0.1901 0.1738 0.1821 -0.0264 -0.0325 0.0069  200 ASP   A O    
1417 C  CB   . ASP   A 196 ? 0.2054 0.1894 0.2316 0.0058  -0.0114 0.0183  200 ASP   A CB   
1418 C  CG   . ASP   A 196 ? 0.2396 0.2230 0.3202 -0.0050 0.0055  0.0154  200 ASP   A CG   
1419 O  OD1  . ASP   A 196 ? 0.2496 0.2640 0.3730 -0.0129 0.0251  0.0101  200 ASP   A OD1  
1420 O  OD2  . ASP   A 196 ? 0.3308 0.2596 0.4438 0.0184  0.0359  0.0198  200 ASP   A OD2  
1421 N  N    . VAL   A 197 ? 0.1719 0.1608 0.1734 -0.0017 -0.0209 0.0077  201 VAL   A N    
1422 C  CA   . VAL   A 197 ? 0.1650 0.1570 0.1823 -0.0016 -0.0178 0.0071  201 VAL   A CA   
1423 C  C    . VAL   A 197 ? 0.1763 0.1578 0.1703 0.0012  -0.0202 0.0134  201 VAL   A C    
1424 O  O    . VAL   A 197 ? 0.1899 0.1577 0.1691 0.0006  -0.0184 0.0142  201 VAL   A O    
1425 C  CB   . VAL   A 197 ? 0.1715 0.1655 0.2120 0.0010  -0.0252 0.0064  201 VAL   A CB   
1426 C  CG1  . VAL   A 197 ? 0.1862 0.1727 0.2322 -0.0029 -0.0200 -0.0003 201 VAL   A CG1  
1427 C  CG2  . VAL   A 197 ? 0.1768 0.1682 0.2106 0.0032  -0.0197 -0.0063 201 VAL   A CG2  
1428 N  N    . LEU   A 198 ? 0.1824 0.1640 0.1613 0.0105  -0.0146 0.0274  202 LEU   A N    
1429 C  CA   . LEU   A 198 ? 0.1903 0.1733 0.1771 0.0143  -0.0101 0.0170  202 LEU   A CA   
1430 C  C    . LEU   A 198 ? 0.1870 0.1716 0.1818 0.0098  -0.0137 0.0199  202 LEU   A C    
1431 O  O    . LEU   A 198 ? 0.1954 0.1693 0.1874 0.0079  -0.0128 0.0182  202 LEU   A O    
1432 C  CB   . LEU   A 198 ? 0.1962 0.1824 0.1818 0.0257  -0.0095 0.0146  202 LEU   A CB   
1433 C  CG   . LEU   A 198 ? 0.2011 0.1856 0.2039 0.0243  -0.0120 0.0066  202 LEU   A CG   
1434 C  CD1  . LEU   A 198 ? 0.2081 0.1927 0.2058 0.0311  -0.0105 -0.0011 202 LEU   A CD1  
1435 C  CD2  . LEU   A 198 ? 0.2223 0.1879 0.2059 0.0156  -0.0208 0.0027  202 LEU   A CD2  
1436 N  N    . ALA   A 199 ? 0.1837 0.1726 0.1822 0.0027  -0.0253 0.0206  203 ALA   A N    
1437 C  CA   . ALA   A 199 ? 0.1812 0.1769 0.1956 -0.0010 -0.0302 0.0171  203 ALA   A CA   
1438 C  C    . ALA   A 199 ? 0.1817 0.1732 0.1886 -0.0076 -0.0347 0.0155  203 ALA   A C    
1439 O  O    . ALA   A 199 ? 0.1828 0.1881 0.2085 -0.0090 -0.0428 0.0169  203 ALA   A O    
1440 C  CB   . ALA   A 199 ? 0.1888 0.1834 0.1962 -0.0107 -0.0347 0.0184  203 ALA   A CB   
1441 N  N    . LEU   A 200 ? 0.1786 0.1631 0.1721 -0.0084 -0.0264 0.0176  204 LEU   A N    
1442 C  CA   . LEU   A 200 ? 0.1877 0.1562 0.1706 -0.0140 -0.0282 0.0118  204 LEU   A CA   
1443 C  C    . LEU   A 200 ? 0.1944 0.1614 0.1683 -0.0132 -0.0300 0.0149  204 LEU   A C    
1444 O  O    . LEU   A 200 ? 0.2114 0.1721 0.1680 -0.0195 -0.0312 0.0187  204 LEU   A O    
1445 C  CB   . LEU   A 200 ? 0.1981 0.1482 0.1837 -0.0109 -0.0232 0.0064  204 LEU   A CB   
1446 C  CG   . LEU   A 200 ? 0.2115 0.1490 0.1933 -0.0162 -0.0157 0.0153  204 LEU   A CG   
1447 C  CD1  . LEU   A 200 ? 0.2310 0.1612 0.1978 -0.0102 -0.0165 0.0141  204 LEU   A CD1  
1448 C  CD2  . LEU   A 200 ? 0.2144 0.1668 0.1903 -0.0133 -0.0075 0.0214  204 LEU   A CD2  
1449 N  N    . LEU   A 201 ? 0.2009 0.1548 0.1677 -0.0101 -0.0383 0.0187  205 LEU   A N    
1450 C  CA   . LEU   A 201 ? 0.2028 0.1606 0.1894 -0.0054 -0.0418 0.0128  205 LEU   A CA   
1451 C  C    . LEU   A 201 ? 0.2001 0.1664 0.1982 -0.0006 -0.0452 0.0201  205 LEU   A C    
1452 O  O    . LEU   A 201 ? 0.1967 0.1868 0.2045 -0.0003 -0.0469 0.0342  205 LEU   A O    
1453 C  CB   . LEU   A 201 ? 0.2138 0.1706 0.1977 -0.0020 -0.0379 0.0038  205 LEU   A CB   
1454 C  CG   . LEU   A 201 ? 0.2260 0.1727 0.2199 -0.0023 -0.0365 -0.0006 205 LEU   A CG   
1455 C  CD1  . LEU   A 201 ? 0.2302 0.1725 0.2395 -0.0016 -0.0335 -0.0073 205 LEU   A CD1  
1456 C  CD2  . LEU   A 201 ? 0.2385 0.1800 0.2356 -0.0045 -0.0398 -0.0096 205 LEU   A CD2  
1457 N  N    . SER   A 202 ? 0.1983 0.1819 0.2091 0.0013  -0.0463 0.0273  206 SER   A N    
1458 C  CA   . SER   A 202 ? 0.2082 0.2046 0.2367 0.0108  -0.0506 0.0336  206 SER   A CA   
1459 C  C    . SER   A 202 ? 0.2132 0.2228 0.2400 -0.0058 -0.0634 0.0412  206 SER   A C    
1460 O  O    . SER   A 202 ? 0.2177 0.2370 0.2780 0.0105  -0.0765 0.0419  206 SER   A O    
1461 C  CB   . SER   A 202 ? 0.2013 0.2178 0.2429 0.0071  -0.0471 0.0318  206 SER   A CB   
1462 O  OG   . SER   A 202 ? 0.2070 0.2394 0.2554 0.0076  -0.0419 0.0197  206 SER   A OG   
1463 N  N    . ILE   A 203 ? 0.2207 0.2355 0.2283 -0.0184 -0.0707 0.0415  207 ILE   A N    
1464 C  CA   . ILE   A 203 ? 0.2411 0.2490 0.2412 -0.0364 -0.0717 0.0364  207 ILE   A CA   
1465 C  C    . ILE   A 203 ? 0.2477 0.2603 0.2284 -0.0357 -0.0824 0.0513  207 ILE   A C    
1466 O  O    . ILE   A 203 ? 0.2861 0.2768 0.2495 -0.0464 -0.0979 0.0747  207 ILE   A O    
1467 C  CB   . ILE   A 203 ? 0.2633 0.2507 0.2593 -0.0456 -0.0640 0.0281  207 ILE   A CB   
1468 C  CG1  . ILE   A 203 ? 0.2584 0.2549 0.2899 -0.0480 -0.0616 0.0216  207 ILE   A CG1  
1469 C  CG2  . ILE   A 203 ? 0.2951 0.2686 0.2699 -0.0521 -0.0641 0.0173  207 ILE   A CG2  
1470 C  CD1  . ILE   A 203 ? 0.2652 0.2515 0.3107 -0.0513 -0.0656 0.0235  207 ILE   A CD1  
1471 N  N    . CYS   A 204 ? 0.2309 0.2477 0.2070 -0.0278 -0.0696 0.0536  208 CYS   A N    
1472 C  CA   . CYS   A 204 ? 0.2481 0.2433 0.2132 -0.0258 -0.0576 0.0474  208 CYS   A CA   
1473 C  C    . CYS   A 204 ? 0.2445 0.2427 0.2272 -0.0244 -0.0635 0.0656  208 CYS   A C    
1474 O  O    . CYS   A 204 ? 0.2946 0.2497 0.2337 -0.0246 -0.0474 0.0775  208 CYS   A O    
1475 C  CB   . CYS   A 204 ? 0.2415 0.2432 0.1902 -0.0221 -0.0508 0.0413  208 CYS   A CB   
1476 S  SG   . CYS   A 204 ? 0.2747 0.2495 0.2043 -0.0315 -0.0460 0.0082  208 CYS   A SG   
1477 N  N    . GLN   A 205 ? 0.2202 0.2306 0.2525 -0.0239 -0.0604 0.0740  209 GLN   A N    
1478 C  CA   . GLN   A 205 ? 0.2479 0.2404 0.2690 -0.0131 -0.0645 0.0765  209 GLN   A CA   
1479 C  C    . GLN   A 205 ? 0.2634 0.2646 0.3007 0.0031  -0.0834 0.0816  209 GLN   A C    
1480 O  O    . GLN   A 205 ? 0.2814 0.2664 0.3265 0.0224  -0.0981 0.0760  209 GLN   A O    
1481 C  CB   . GLN   A 205 ? 0.2497 0.2253 0.2812 -0.0113 -0.0543 0.0689  209 GLN   A CB   
1482 C  CG   . GLN   A 205 ? 0.2492 0.2208 0.2793 -0.0021 -0.0525 0.0642  209 GLN   A CG   
1483 C  CD   . GLN   A 205 ? 0.2513 0.2311 0.2934 0.0154  -0.0446 0.0470  209 GLN   A CD   
1484 O  OE1  . GLN   A 205 ? 0.2492 0.2589 0.3062 0.0422  -0.0220 0.0513  209 GLN   A OE1  
1485 N  NE2  . GLN   A 205 ? 0.2673 0.2419 0.3141 0.0127  -0.0530 0.0341  209 GLN   A NE2  
1486 N  N    . TRP   A 206 ? 0.2749 0.2782 0.2908 -0.0011 -0.0990 0.0930  210 TRP   A N    
1487 C  CA   . TRP   A 206 ? 0.2810 0.3238 0.3230 -0.0078 -0.1033 0.0891  210 TRP   A CA   
1488 C  C    . TRP   A 206 ? 0.2892 0.3030 0.3386 -0.0019 -0.0856 0.0836  210 TRP   A C    
1489 O  O    . TRP   A 206 ? 0.2852 0.3311 0.3664 0.0143  -0.0784 0.0915  210 TRP   A O    
1490 C  CB   . TRP   A 206 ? 0.3096 0.3430 0.3624 -0.0269 -0.1018 0.0937  210 TRP   A CB   
1491 C  CG   . TRP   A 206 ? 0.3673 0.4150 0.4075 -0.0577 -0.1242 0.0842  210 TRP   A CG   
1492 C  CD1  . TRP   A 206 ? 0.4024 0.4681 0.4630 -0.0294 -0.1197 0.0719  210 TRP   A CD1  
1493 C  CD2  . TRP   A 206 ? 0.4473 0.4504 0.4387 -0.0660 -0.1126 0.0652  210 TRP   A CD2  
1494 N  NE1  . TRP   A 206 ? 0.4268 0.5093 0.4725 -0.0465 -0.1265 0.0549  210 TRP   A NE1  
1495 C  CE2  . TRP   A 206 ? 0.4591 0.4938 0.4705 -0.0511 -0.1184 0.0584  210 TRP   A CE2  
1496 C  CE3  . TRP   A 206 ? 0.4956 0.4996 0.4645 -0.0659 -0.1117 0.0713  210 TRP   A CE3  
1497 C  CZ2  . TRP   A 206 ? 0.5095 0.5414 0.4949 -0.0503 -0.1156 0.0409  210 TRP   A CZ2  
1498 C  CZ3  . TRP   A 206 ? 0.5275 0.5420 0.5029 -0.0667 -0.1192 0.0413  210 TRP   A CZ3  
1499 C  CH2  . TRP   A 206 ? 0.5197 0.5596 0.5030 -0.0538 -0.1196 0.0442  210 TRP   A CH2  
1500 N  N    . ARG   A 207 ? 0.2879 0.2937 0.3194 -0.0204 -0.0818 0.0676  211 ARG   A N    
1501 C  CA   . ARG   A 207 ? 0.3043 0.2943 0.3200 -0.0178 -0.0745 0.0582  211 ARG   A CA   
1502 C  C    . ARG   A 207 ? 0.2875 0.2604 0.2680 -0.0145 -0.0702 0.0480  211 ARG   A C    
1503 O  O    . ARG   A 207 ? 0.2845 0.2633 0.2638 -0.0302 -0.0710 0.0415  211 ARG   A O    
1504 C  CB   . ARG   A 207 ? 0.3404 0.3238 0.3309 -0.0120 -0.0880 0.0629  211 ARG   A CB   
1505 C  CG   . ARG   A 207 ? 0.3470 0.3545 0.3825 -0.0075 -0.0830 0.0648  211 ARG   A CG   
1506 C  CD   . ARG   A 207 ? 0.3562 0.3886 0.4385 0.0084  -0.0769 0.0537  211 ARG   A CD   
1507 N  N    . PRO   A 208 ? 0.2635 0.2308 0.2698 -0.0151 -0.0626 0.0451  212 PRO   A N    
1508 C  CA   . PRO   A 208 ? 0.2598 0.2286 0.2661 -0.0228 -0.0542 0.0417  212 PRO   A CA   
1509 C  C    . PRO   A 208 ? 0.2635 0.2124 0.2490 -0.0123 -0.0583 0.0387  212 PRO   A C    
1510 O  O    . PRO   A 208 ? 0.2715 0.1981 0.2437 0.0041  -0.0550 0.0342  212 PRO   A O    
1511 C  CB   . PRO   A 208 ? 0.2633 0.2386 0.2688 -0.0268 -0.0469 0.0386  212 PRO   A CB   
1512 C  CG   . PRO   A 208 ? 0.2699 0.2489 0.2872 -0.0217 -0.0429 0.0336  212 PRO   A CG   
1513 C  CD   . PRO   A 208 ? 0.2560 0.2501 0.2835 -0.0167 -0.0566 0.0387  212 PRO   A CD   
1514 N  N    . GLN   A 209 ? 0.2744 0.2073 0.2672 -0.0042 -0.0744 0.0373  213 GLN   A N    
1515 C  CA   . GLN   A 209 ? 0.2886 0.2034 0.2702 -0.0059 -0.0732 0.0478  213 GLN   A CA   
1516 C  C    . GLN   A 209 ? 0.2877 0.2049 0.2641 -0.0155 -0.0724 0.0482  213 GLN   A C    
1517 O  O    . GLN   A 209 ? 0.2982 0.2108 0.2563 -0.0126 -0.0682 0.0401  213 GLN   A O    
1518 C  CB   . GLN   A 209 ? 0.3341 0.2055 0.2913 0.0101  -0.0737 0.0539  213 GLN   A CB   
1519 C  CG   . GLN   A 209 ? 0.3803 0.2096 0.3271 0.0249  -0.0831 0.0612  213 GLN   A CG   
1520 C  CD   . GLN   A 209 ? 0.4241 0.2595 0.3906 0.0341  -0.0647 0.0592  213 GLN   A CD   
1521 O  OE1  . GLN   A 209 ? 0.4301 0.2977 0.4164 0.0211  -0.0944 0.0642  213 GLN   A OE1  
1522 N  NE2  . GLN   A 209 ? 0.4750 0.3131 0.4530 0.0434  -0.0446 0.0274  213 GLN   A NE2  
1523 N  N    . ALA   A 210 ? 0.2903 0.2208 0.2676 -0.0194 -0.0708 0.0477  214 ALA   A N    
1524 C  CA   . ALA   A 210 ? 0.2906 0.2285 0.2604 -0.0301 -0.0765 0.0385  214 ALA   A CA   
1525 C  C    . ALA   A 210 ? 0.2737 0.2106 0.2413 -0.0313 -0.0682 0.0265  214 ALA   A C    
1526 O  O    . ALA   A 210 ? 0.2785 0.2130 0.2537 -0.0322 -0.0724 0.0209  214 ALA   A O    
1527 C  CB   . ALA   A 210 ? 0.2958 0.2447 0.2742 -0.0301 -0.0869 0.0388  214 ALA   A CB   
1528 N  N    . LEU   A 211 ? 0.2770 0.2049 0.2436 -0.0217 -0.0572 0.0217  215 LEU   A N    
1529 C  CA   . LEU   A 211 ? 0.2770 0.1804 0.2228 -0.0224 -0.0484 0.0135  215 LEU   A CA   
1530 C  C    . LEU   A 211 ? 0.2702 0.1647 0.2164 -0.0153 -0.0414 0.0083  215 LEU   A C    
1531 O  O    . LEU   A 211 ? 0.2871 0.1650 0.2274 -0.0243 -0.0315 -0.0049 215 LEU   A O    
1532 C  CB   . LEU   A 211 ? 0.2888 0.1838 0.2323 -0.0194 -0.0437 0.0272  215 LEU   A CB   
1533 C  CG   . LEU   A 211 ? 0.2932 0.1978 0.2330 -0.0142 -0.0457 0.0302  215 LEU   A CG   
1534 C  CD1  . LEU   A 211 ? 0.2844 0.1949 0.2406 -0.0142 -0.0395 0.0327  215 LEU   A CD1  
1535 C  CD2  . LEU   A 211 ? 0.2946 0.1974 0.2391 -0.0193 -0.0468 0.0327  215 LEU   A CD2  
1536 N  N    . LEU   A 212 ? 0.2554 0.1631 0.2309 -0.0126 -0.0449 0.0093  216 LEU   A N    
1537 C  CA   . LEU   A 212 ? 0.2547 0.1660 0.2245 -0.0153 -0.0325 0.0074  216 LEU   A CA   
1538 C  C    . LEU   A 212 ? 0.2615 0.1813 0.2176 -0.0191 -0.0404 0.0114  216 LEU   A C    
1539 O  O    . LEU   A 212 ? 0.2624 0.1704 0.2225 -0.0210 -0.0464 0.0000  216 LEU   A O    
1540 C  CB   . LEU   A 212 ? 0.2591 0.1772 0.2199 -0.0073 -0.0281 0.0035  216 LEU   A CB   
1541 C  CG   . LEU   A 212 ? 0.2563 0.1634 0.1986 -0.0101 -0.0177 0.0040  216 LEU   A CG   
1542 C  CD1  . LEU   A 212 ? 0.2525 0.1732 0.2049 -0.0162 -0.0199 0.0064  216 LEU   A CD1  
1543 C  CD2  . LEU   A 212 ? 0.2597 0.1582 0.1914 -0.0071 -0.0243 0.0082  216 LEU   A CD2  
1544 N  N    . ARG   A 213 ? 0.2674 0.1793 0.2260 -0.0294 -0.0456 0.0169  217 ARG   A N    
1545 C  CA   . ARG   A 213 ? 0.2839 0.2087 0.2460 -0.0425 -0.0327 0.0179  217 ARG   A CA   
1546 C  C    . ARG   A 213 ? 0.2832 0.2225 0.2264 -0.0377 -0.0386 0.0118  217 ARG   A C    
1547 O  O    . ARG   A 213 ? 0.2974 0.2235 0.2202 -0.0341 -0.0351 0.0018  217 ARG   A O    
1548 C  CB   . ARG   A 213 ? 0.3023 0.2667 0.2845 -0.0246 -0.0413 0.0261  217 ARG   A CB   
1549 C  CG   . ARG   A 213 ? 0.3519 0.3012 0.3409 -0.0286 -0.0483 0.0358  217 ARG   A CG   
1550 C  CD   . ARG   A 213 ? 0.4066 0.3740 0.3796 -0.0155 -0.0638 0.0612  217 ARG   A CD   
1551 N  NE   . ARG   A 213 ? 0.4302 0.4361 0.4294 -0.0128 -0.0692 0.0794  217 ARG   A NE   
1552 C  CZ   . ARG   A 213 ? 0.4573 0.4750 0.4603 0.0041  -0.0660 0.0859  217 ARG   A CZ   
1553 N  NH1  . ARG   A 213 ? 0.5011 0.4913 0.4817 0.0108  -0.0734 0.0814  217 ARG   A NH1  
1554 N  NH2  . ARG   A 213 ? 0.4769 0.5224 0.4956 -0.0080 -0.0609 0.1120  217 ARG   A NH2  
1555 N  N    . TRP   A 214 ? 0.2988 0.2117 0.2078 -0.0403 -0.0377 0.0084  218 TRP   A N    
1556 C  CA   . TRP   A 214 ? 0.3085 0.2144 0.2087 -0.0466 -0.0329 -0.0010 218 TRP   A CA   
1557 C  C    . TRP   A 214 ? 0.3118 0.1974 0.1990 -0.0386 -0.0232 -0.0051 218 TRP   A C    
1558 O  O    . TRP   A 214 ? 0.3066 0.1946 0.1992 -0.0392 -0.0261 -0.0085 218 TRP   A O    
1559 C  CB   . TRP   A 214 ? 0.3235 0.2304 0.2420 -0.0544 -0.0270 -0.0046 218 TRP   A CB   
1560 C  CG   . TRP   A 214 ? 0.3624 0.2435 0.2812 -0.0507 -0.0191 -0.0160 218 TRP   A CG   
1561 C  CD1  . TRP   A 214 ? 0.3920 0.2557 0.3001 -0.0531 -0.0207 -0.0240 218 TRP   A CD1  
1562 C  CD2  . TRP   A 214 ? 0.3892 0.2546 0.3288 -0.0520 0.0039  -0.0014 218 TRP   A CD2  
1563 N  NE1  . TRP   A 214 ? 0.4102 0.2669 0.3387 -0.0665 -0.0096 -0.0269 218 TRP   A NE1  
1564 C  CE2  . TRP   A 214 ? 0.4015 0.2557 0.3360 -0.0558 -0.0023 -0.0040 218 TRP   A CE2  
1565 C  CE3  . TRP   A 214 ? 0.3849 0.2366 0.3536 -0.0480 0.0024  0.0278  218 TRP   A CE3  
1566 C  CZ2  . TRP   A 214 ? 0.4264 0.2731 0.3749 -0.0533 0.0167  0.0166  218 TRP   A CZ2  
1567 C  CZ3  . TRP   A 214 ? 0.4173 0.2617 0.3886 -0.0404 0.0143  0.0270  218 TRP   A CZ3  
1568 C  CH2  . TRP   A 214 ? 0.4118 0.2621 0.3663 -0.0643 0.0114  0.0312  218 TRP   A CH2  
1569 N  N    . VAL   A 215 ? 0.2998 0.1878 0.1917 -0.0345 -0.0295 -0.0068 219 VAL   A N    
1570 C  CA   . VAL   A 215 ? 0.2887 0.1773 0.1948 -0.0271 -0.0247 -0.0066 219 VAL   A CA   
1571 C  C    . VAL   A 215 ? 0.2840 0.1690 0.1879 -0.0222 -0.0257 -0.0117 219 VAL   A C    
1572 O  O    . VAL   A 215 ? 0.2921 0.1706 0.1846 -0.0192 -0.0133 -0.0100 219 VAL   A O    
1573 C  CB   . VAL   A 215 ? 0.2810 0.1988 0.1985 -0.0268 -0.0294 -0.0108 219 VAL   A CB   
1574 C  CG1  . VAL   A 215 ? 0.2816 0.2198 0.2023 -0.0238 -0.0296 -0.0149 219 VAL   A CG1  
1575 C  CG2  . VAL   A 215 ? 0.2839 0.2123 0.2149 -0.0289 -0.0306 -0.0089 219 VAL   A CG2  
1576 N  N    . ASP   A 216 ? 0.2814 0.1755 0.1853 -0.0194 -0.0195 -0.0039 220 ASP   A N    
1577 C  CA   . ASP   A 216 ? 0.2969 0.1796 0.1936 -0.0262 -0.0143 -0.0080 220 ASP   A CA   
1578 C  C    . ASP   A 216 ? 0.2978 0.2012 0.2026 -0.0233 -0.0064 -0.0081 220 ASP   A C    
1579 O  O    . ASP   A 216 ? 0.3012 0.2465 0.2314 -0.0166 -0.0103 -0.0193 220 ASP   A O    
1580 C  CB   . ASP   A 216 ? 0.3058 0.1764 0.1921 -0.0241 -0.0131 0.0010  220 ASP   A CB   
1581 C  CG   . ASP   A 216 ? 0.3116 0.1836 0.1931 -0.0306 -0.0181 -0.0023 220 ASP   A CG   
1582 O  OD1  . ASP   A 216 ? 0.3152 0.1877 0.2025 -0.0339 -0.0193 -0.0036 220 ASP   A OD1  
1583 O  OD2  . ASP   A 216 ? 0.3177 0.1758 0.2012 -0.0393 -0.0212 -0.0028 220 ASP   A OD2  
1584 N  N    . ALA   A 217 ? 0.3092 0.2099 0.1937 -0.0175 -0.0092 -0.0107 221 ALA   A N    
1585 C  CA   . ALA   A 217 ? 0.3376 0.2245 0.1955 -0.0176 -0.0001 -0.0110 221 ALA   A CA   
1586 C  C    . ALA   A 217 ? 0.3567 0.2243 0.1887 -0.0049 0.0108  -0.0187 221 ALA   A C    
1587 O  O    . ALA   A 217 ? 0.3893 0.2554 0.2125 -0.0092 0.0479  -0.0091 221 ALA   A O    
1588 C  CB   . ALA   A 217 ? 0.3522 0.2434 0.2012 -0.0200 -0.0126 -0.0119 221 ALA   A CB   
1589 N  N    . HIS   A 218 ? 0.3353 0.1979 0.1810 -0.0061 0.0054  -0.0232 222 HIS   A N    
1590 C  CA   . HIS   A 218 ? 0.3413 0.2043 0.2162 0.0009  -0.0005 -0.0146 222 HIS   A CA   
1591 C  C    . HIS   A 218 ? 0.3442 0.2100 0.2082 -0.0015 0.0085  -0.0106 222 HIS   A C    
1592 O  O    . HIS   A 218 ? 0.3509 0.2124 0.2353 0.0082  0.0123  -0.0092 222 HIS   A O    
1593 C  CB   . HIS   A 218 ? 0.3482 0.2156 0.2613 0.0002  -0.0039 -0.0259 222 HIS   A CB   
1594 C  CG   . HIS   A 218 ? 0.3686 0.2655 0.2832 0.0027  -0.0217 -0.0561 222 HIS   A CG   
1595 N  ND1  . HIS   A 218 ? 0.3714 0.2834 0.3070 -0.0013 -0.0337 -0.0381 222 HIS   A ND1  
1596 C  CD2  . HIS   A 218 ? 0.4036 0.3105 0.3101 0.0101  -0.0408 -0.0820 222 HIS   A CD2  
1597 C  CE1  . HIS   A 218 ? 0.3991 0.3235 0.3305 0.0083  -0.0515 -0.0715 222 HIS   A CE1  
1598 N  NE2  . HIS   A 218 ? 0.4180 0.3409 0.3262 0.0175  -0.0558 -0.0807 222 HIS   A NE2  
1599 N  N    . ALA   A 219 ? 0.3569 0.2085 0.2090 0.0052  0.0036  -0.0116 223 ALA   A N    
1600 C  CA   . ALA   A 219 ? 0.3542 0.2096 0.2049 0.0190  0.0084  -0.0066 223 ALA   A CA   
1601 C  C    . ALA   A 219 ? 0.3488 0.2054 0.1932 0.0167  0.0211  -0.0130 223 ALA   A C    
1602 O  O    . ALA   A 219 ? 0.3424 0.2148 0.2133 0.0138  0.0283  0.0102  223 ALA   A O    
1603 C  CB   . ALA   A 219 ? 0.3622 0.2313 0.2091 0.0182  -0.0053 -0.0207 223 ALA   A CB   
1604 N  N    . ARG   A 220 ? 0.3402 0.2178 0.1616 0.0185  0.0394  -0.0086 224 ARG   A N    
1605 C  CA   . ARG   A 220 ? 0.3462 0.2275 0.1849 0.0231  0.0442  -0.0113 224 ARG   A CA   
1606 C  C    . ARG   A 220 ? 0.3139 0.2089 0.1774 0.0180  0.0651  -0.0089 224 ARG   A C    
1607 O  O    . ARG   A 220 ? 0.2764 0.2182 0.1618 0.0204  0.0567  -0.0231 224 ARG   A O    
1608 C  CB   . ARG   A 220 ? 0.3885 0.2457 0.2567 0.0236  0.0345  -0.0231 224 ARG   A CB   
1609 C  CG   . ARG   A 220 ? 0.4342 0.2801 0.3049 0.0136  0.0207  -0.0110 224 ARG   A CG   
1610 C  CD   . ARG   A 220 ? 0.4733 0.3112 0.3325 -0.0041 0.0364  0.0082  224 ARG   A CD   
1611 N  NE   . ARG   A 220 ? 0.4991 0.3466 0.3689 -0.0098 0.0599  0.0294  224 ARG   A NE   
1612 C  CZ   . ARG   A 220 ? 0.5309 0.3135 0.3429 -0.0106 0.0503  0.0336  224 ARG   A CZ   
1613 N  NH1  . ARG   A 220 ? 0.5820 0.3508 0.3804 -0.0161 0.0427  0.0139  224 ARG   A NH1  
1614 N  NH2  . ARG   A 220 ? 0.4705 0.2487 0.2966 -0.0256 0.0408  0.0481  224 ARG   A NH2  
1615 N  N    . PRO   A 221 ? 0.3173 0.2179 0.1894 0.0155  0.0846  -0.0070 225 PRO   A N    
1616 C  CA   . PRO   A 221 ? 0.3042 0.2205 0.2027 0.0125  0.0808  -0.0003 225 PRO   A CA   
1617 C  C    . PRO   A 221 ? 0.2965 0.2175 0.2063 -0.0011 0.0722  -0.0005 225 PRO   A C    
1618 O  O    . PRO   A 221 ? 0.3096 0.2138 0.2082 -0.0024 0.0693  0.0000  225 PRO   A O    
1619 C  CB   . PRO   A 221 ? 0.3139 0.2439 0.2305 0.0165  0.0917  -0.0025 225 PRO   A CB   
1620 C  CG   . PRO   A 221 ? 0.3286 0.2551 0.2290 0.0205  0.0954  -0.0004 225 PRO   A CG   
1621 C  CD   . PRO   A 221 ? 0.3266 0.2423 0.2015 0.0181  0.0936  -0.0049 225 PRO   A CD   
1622 N  N    . PHE   A 222 ? 0.2792 0.1983 0.2049 -0.0046 0.0617  0.0013  226 PHE   A N    
1623 C  CA   . PHE   A 222 ? 0.2788 0.2132 0.2073 -0.0070 0.0656  0.0082  226 PHE   A CA   
1624 C  C    . PHE   A 222 ? 0.2909 0.2283 0.2378 0.0036  0.0679  0.0168  226 PHE   A C    
1625 O  O    . PHE   A 222 ? 0.3044 0.2150 0.2501 0.0089  0.0675  0.0062  226 PHE   A O    
1626 C  CB   . PHE   A 222 ? 0.2714 0.2137 0.2213 -0.0119 0.0545  -0.0011 226 PHE   A CB   
1627 C  CG   . PHE   A 222 ? 0.2603 0.2134 0.2284 -0.0275 0.0548  0.0011  226 PHE   A CG   
1628 C  CD1  . PHE   A 222 ? 0.2741 0.2468 0.2469 -0.0282 0.0448  0.0071  226 PHE   A CD1  
1629 C  CD2  . PHE   A 222 ? 0.2873 0.2530 0.2654 -0.0433 0.0534  0.0358  226 PHE   A CD2  
1630 C  CE1  . PHE   A 222 ? 0.2728 0.2368 0.2613 -0.0403 0.0483  0.0099  226 PHE   A CE1  
1631 C  CE2  . PHE   A 222 ? 0.2980 0.2554 0.2811 -0.0397 0.0429  0.0477  226 PHE   A CE2  
1632 C  CZ   . PHE   A 222 ? 0.2876 0.2446 0.2758 -0.0379 0.0538  0.0321  226 PHE   A CZ   
1633 N  N    . GLY   A 223 ? 0.2868 0.2327 0.2766 0.0187  0.0759  0.0245  227 GLY   A N    
1634 C  CA   . GLY   A 223 ? 0.3095 0.2499 0.3003 0.0310  0.0892  0.0175  227 GLY   A CA   
1635 C  C    . GLY   A 223 ? 0.3415 0.2464 0.3091 0.0332  0.0951  0.0152  227 GLY   A C    
1636 O  O    . GLY   A 223 ? 0.3787 0.2766 0.3617 0.0620  0.1055  0.0123  227 GLY   A O    
1637 N  N    . THR   A 224 ? 0.3890 0.2476 0.2819 0.0360  0.0885  0.0169  228 THR   A N    
1638 C  CA   . THR   A 224 ? 0.4261 0.2467 0.2592 0.0307  0.1019  0.0012  228 THR   A CA   
1639 C  C    . THR   A 224 ? 0.4088 0.2247 0.2300 0.0367  0.0920  -0.0042 228 THR   A C    
1640 O  O    . THR   A 224 ? 0.4324 0.2273 0.2344 0.0277  0.0897  -0.0077 228 THR   A O    
1641 C  CB   . THR   A 224 ? 0.4731 0.2616 0.2550 0.0276  0.0869  0.0018  228 THR   A CB   
1642 O  OG1  . THR   A 224 ? 0.5020 0.2619 0.2415 0.0478  0.0549  0.0126  228 THR   A OG1  
1643 C  CG2  . THR   A 224 ? 0.4914 0.2717 0.2683 0.0207  0.0950  0.0010  228 THR   A CG2  
1644 N  N    . ILE   A 225 ? 0.3636 0.1906 0.2233 0.0442  0.0909  0.0054  229 ILE   A N    
1645 C  CA   . ILE   A 225 ? 0.3348 0.1961 0.2235 0.0486  0.0800  0.0092  229 ILE   A CA   
1646 C  C    . ILE   A 225 ? 0.3321 0.2102 0.2181 0.0404  0.0752  0.0178  229 ILE   A C    
1647 O  O    . ILE   A 225 ? 0.3226 0.2147 0.2328 0.0321  0.0642  0.0127  229 ILE   A O    
1648 C  CB   . ILE   A 225 ? 0.3286 0.1814 0.2168 0.0543  0.0693  0.0159  229 ILE   A CB   
1649 C  CG1  . ILE   A 225 ? 0.3345 0.1903 0.2422 0.0531  0.0533  0.0204  229 ILE   A CG1  
1650 C  CG2  . ILE   A 225 ? 0.3250 0.1881 0.2236 0.0560  0.0791  0.0158  229 ILE   A CG2  
1651 C  CD1  . ILE   A 225 ? 0.3508 0.1852 0.2415 0.0511  0.0482  0.0302  229 ILE   A CD1  
1652 N  N    . ARG   A 226 ? 0.3403 0.2265 0.2246 0.0484  0.0851  0.0069  230 ARG   A N    
1653 C  CA   . ARG   A 226 ? 0.3434 0.2418 0.2209 0.0482  0.0802  0.0204  230 ARG   A CA   
1654 C  C    . ARG   A 226 ? 0.3187 0.2307 0.2232 0.0377  0.0834  0.0016  230 ARG   A C    
1655 O  O    . ARG   A 226 ? 0.3012 0.2403 0.2049 0.0386  0.0698  0.0075  230 ARG   A O    
1656 C  CB   . ARG   A 226 ? 0.3986 0.2758 0.2607 0.0521  0.0828  -0.0029 230 ARG   A CB   
1657 C  CG   . ARG   A 226 ? 0.4439 0.3202 0.2790 0.0542  0.0911  -0.0005 230 ARG   A CG   
1658 C  CD   . ARG   A 226 ? 0.5029 0.3540 0.3416 0.0537  0.0836  -0.0283 230 ARG   A CD   
1659 N  N    . PRO   A 227 ? 0.2994 0.2275 0.2313 0.0270  0.0819  0.0138  231 PRO   A N    
1660 C  CA   . PRO   A 227 ? 0.2957 0.2132 0.2127 0.0276  0.0741  -0.0014 231 PRO   A CA   
1661 C  C    . PRO   A 227 ? 0.2798 0.2022 0.2023 0.0253  0.0632  -0.0117 231 PRO   A C    
1662 O  O    . PRO   A 227 ? 0.3121 0.2085 0.2037 0.0217  0.0715  -0.0216 231 PRO   A O    
1663 C  CB   . PRO   A 227 ? 0.2996 0.2333 0.2422 0.0282  0.0678  0.0077  231 PRO   A CB   
1664 C  CG   . PRO   A 227 ? 0.3134 0.2861 0.2681 0.0310  0.0749  0.0164  231 PRO   A CG   
1665 C  CD   . PRO   A 227 ? 0.3057 0.2645 0.2566 0.0307  0.0874  0.0218  231 PRO   A CD   
1666 N  N    . MET   A 228 ? 0.2550 0.1789 0.2014 0.0155  0.0467  -0.0195 232 MET   A N    
1667 C  CA   . MET   A 228 ? 0.2642 0.1755 0.2153 0.0090  0.0355  -0.0096 232 MET   A CA   
1668 C  C    . MET   A 228 ? 0.2859 0.1852 0.2402 0.0214  0.0476  -0.0127 232 MET   A C    
1669 O  O    . MET   A 228 ? 0.3471 0.1986 0.2945 0.0264  0.0361  -0.0455 232 MET   A O    
1670 C  CB   . MET   A 228 ? 0.2377 0.1627 0.1983 0.0031  0.0166  -0.0160 232 MET   A CB   
1671 C  CG   . MET   A 228 ? 0.2486 0.1648 0.2060 -0.0058 0.0034  -0.0066 232 MET   A CG   
1672 S  SD   . MET   A 228 ? 0.2399 0.1838 0.1751 -0.0274 -0.0153 0.0016  232 MET   A SD   
1673 C  CE   . MET   A 228 ? 0.2450 0.1665 0.1722 -0.0191 0.0053  -0.0044 232 MET   A CE   
1674 N  N    . TYR   A 229 ? 0.2798 0.1919 0.2423 0.0402  0.0584  0.0097  233 TYR   A N    
1675 C  CA   . TYR   A 229 ? 0.2910 0.2360 0.2546 0.0617  0.0698  0.0226  233 TYR   A CA   
1676 C  C    . TYR   A 229 ? 0.3102 0.3048 0.3003 0.0644  0.0629  0.0291  233 TYR   A C    
1677 O  O    . TYR   A 229 ? 0.2871 0.3093 0.2935 0.0788  0.0825  0.0361  233 TYR   A O    
1678 C  CB   . TYR   A 229 ? 0.2820 0.2229 0.2502 0.0549  0.0622  0.0219  233 TYR   A CB   
1679 C  CG   . TYR   A 229 ? 0.2381 0.2159 0.2228 0.0469  0.0480  0.0275  233 TYR   A CG   
1680 C  CD1  . TYR   A 229 ? 0.2235 0.2327 0.2400 0.0415  0.0465  0.0257  233 TYR   A CD1  
1681 C  CD2  . TYR   A 229 ? 0.2193 0.2028 0.2081 0.0482  0.0323  0.0252  233 TYR   A CD2  
1682 C  CE1  . TYR   A 229 ? 0.2124 0.2452 0.2294 0.0423  0.0360  0.0270  233 TYR   A CE1  
1683 C  CE2  . TYR   A 229 ? 0.1986 0.2047 0.2064 0.0347  0.0346  0.0218  233 TYR   A CE2  
1684 C  CZ   . TYR   A 229 ? 0.2024 0.2223 0.2176 0.0387  0.0269  0.0233  233 TYR   A CZ   
1685 O  OH   . TYR   A 229 ? 0.1835 0.2428 0.2003 0.0098  -0.0026 0.0098  233 TYR   A OH   
1686 N  N    . GLY   A 230 ? 0.3705 0.3686 0.3894 0.1021  0.0483  0.0380  234 GLY   A N    
1687 C  CA   . GLY   A 230 ? 0.4050 0.4371 0.4383 0.0810  0.0373  0.0345  234 GLY   A CA   
1688 C  C    . GLY   A 230 ? 0.4704 0.5090 0.4717 0.0868  0.0756  0.0258  234 GLY   A C    
1689 O  O    . GLY   A 230 ? 0.6195 0.5952 0.5634 0.0938  0.0835  -0.0302 234 GLY   A O    
1690 N  N    . ALA   B 1   ? 0.5831 0.6893 0.3691 0.0229  0.0372  0.0283  5   ALA   B N    
1691 C  CA   . ALA   B 1   ? 0.6014 0.6830 0.3803 0.0168  0.0131  0.0255  5   ALA   B CA   
1692 C  C    . ALA   B 1   ? 0.5890 0.6562 0.3690 -0.0053 0.0260  0.0148  5   ALA   B C    
1693 O  O    . ALA   B 1   ? 0.5847 0.7507 0.4142 0.0119  -0.0486 0.0022  5   ALA   B O    
1694 C  CB   . ALA   B 1   ? 0.6300 0.7041 0.3867 0.0287  -0.0121 0.0287  5   ALA   B CB   
1695 N  N    . LEU   B 2   ? 0.5520 0.5658 0.3849 -0.0150 0.0384  0.0224  6   LEU   B N    
1696 C  CA   . LEU   B 2   ? 0.5555 0.5142 0.3771 -0.0277 0.0575  0.0044  6   LEU   B CA   
1697 C  C    . LEU   B 2   ? 0.5503 0.4874 0.3925 -0.0546 0.0559  -0.0152 6   LEU   B C    
1698 O  O    . LEU   B 2   ? 0.5492 0.4756 0.4059 -0.0604 0.0490  -0.0104 6   LEU   B O    
1699 C  CB   . LEU   B 2   ? 0.5656 0.4624 0.3791 -0.0286 0.0651  0.0025  6   LEU   B CB   
1700 C  CG   . LEU   B 2   ? 0.5609 0.4430 0.3662 -0.0004 0.0683  0.0229  6   LEU   B CG   
1701 C  CD1  . LEU   B 2   ? 0.5293 0.4031 0.3831 0.0010  0.0511  0.0334  6   LEU   B CD1  
1702 C  CD2  . LEU   B 2   ? 0.5609 0.4521 0.3764 -0.0099 0.0557  0.0164  6   LEU   B CD2  
1703 N  N    . PRO   B 3   ? 0.5340 0.4793 0.4132 -0.0582 0.0689  -0.0252 7   PRO   B N    
1704 C  CA   . PRO   B 3   ? 0.5166 0.4690 0.4157 -0.0676 0.0573  -0.0309 7   PRO   B CA   
1705 C  C    . PRO   B 3   ? 0.4963 0.4569 0.3885 -0.0871 0.0539  -0.0495 7   PRO   B C    
1706 O  O    . PRO   B 3   ? 0.5057 0.4659 0.4041 -0.0640 0.0602  -0.0464 7   PRO   B O    
1707 C  CB   . PRO   B 3   ? 0.5155 0.4676 0.4493 -0.0760 0.0495  -0.0412 7   PRO   B CB   
1708 C  CG   . PRO   B 3   ? 0.5119 0.4645 0.4544 -0.0680 0.0621  -0.0303 7   PRO   B CG   
1709 C  CD   . PRO   B 3   ? 0.5194 0.4781 0.4282 -0.0646 0.0582  -0.0254 7   PRO   B CD   
1710 N  N    . HIS   B 4   ? 0.4855 0.4297 0.3961 -0.0981 0.0524  -0.0689 8   HIS   B N    
1711 C  CA   . HIS   B 4   ? 0.5252 0.4190 0.3572 -0.1091 0.0361  -0.0771 8   HIS   B CA   
1712 C  C    . HIS   B 4   ? 0.5041 0.4091 0.2903 -0.1246 0.0614  -0.0412 8   HIS   B C    
1713 O  O    . HIS   B 4   ? 0.5770 0.4529 0.2978 -0.1324 0.0447  -0.0579 8   HIS   B O    
1714 C  CB   . HIS   B 4   ? 0.5347 0.4145 0.3486 -0.0992 0.0377  -0.0926 8   HIS   B CB   
1715 C  CG   . HIS   B 4   ? 0.5400 0.4265 0.4079 -0.0989 0.0232  -0.1155 8   HIS   B CG   
1716 N  ND1  . HIS   B 4   ? 0.5424 0.4304 0.4247 -0.0757 0.0142  -0.1162 8   HIS   B ND1  
1717 C  CD2  . HIS   B 4   ? 0.5217 0.4304 0.4275 -0.0735 0.0383  -0.1110 8   HIS   B CD2  
1718 C  CE1  . HIS   B 4   ? 0.5407 0.4315 0.4407 -0.0813 0.0073  -0.1189 8   HIS   B CE1  
1719 N  NE2  . HIS   B 4   ? 0.5577 0.4430 0.4536 -0.0716 0.0170  -0.1291 8   HIS   B NE2  
1720 N  N    . GLY   B 5   ? 0.4388 0.4073 0.2411 -0.1011 0.0802  -0.0442 9   GLY   B N    
1721 C  CA   . GLY   B 5   ? 0.3261 0.3872 0.2397 -0.0808 0.0919  -0.0253 9   GLY   B CA   
1722 C  C    . GLY   B 5   ? 0.2604 0.3580 0.2166 -0.0669 0.0585  -0.0141 9   GLY   B C    
1723 O  O    . GLY   B 5   ? 0.2794 0.4095 0.2393 -0.1072 0.0524  -0.0352 9   GLY   B O    
1724 N  N    A HIS   B 6   ? 0.1954 0.3114 0.1743 -0.0377 0.0507  -0.0024 10  HIS   B N    
1725 N  N    B HIS   B 6   ? 0.2045 0.3345 0.1994 -0.0470 0.0492  -0.0045 10  HIS   B N    
1726 C  CA   A HIS   B 6   ? 0.1670 0.2812 0.1494 -0.0291 0.0372  0.0150  10  HIS   B CA   
1727 C  CA   B HIS   B 6   ? 0.1784 0.3200 0.1818 -0.0348 0.0371  0.0164  10  HIS   B CA   
1728 C  C    A HIS   B 6   ? 0.1595 0.2716 0.1489 -0.0252 0.0298  0.0165  10  HIS   B C    
1729 C  C    B HIS   B 6   ? 0.1623 0.2930 0.1736 -0.0258 0.0291  0.0139  10  HIS   B C    
1730 O  O    A HIS   B 6   ? 0.1503 0.2700 0.1590 -0.0280 0.0291  0.0162  10  HIS   B O    
1731 O  O    B HIS   B 6   ? 0.1694 0.2906 0.1845 -0.0217 0.0230  0.0120  10  HIS   B O    
1732 C  CB   A HIS   B 6   ? 0.1570 0.2549 0.1311 -0.0168 0.0368  0.0264  10  HIS   B CB   
1733 C  CB   B HIS   B 6   ? 0.1683 0.3184 0.1941 -0.0287 0.0367  0.0255  10  HIS   B CB   
1734 C  CG   A HIS   B 6   ? 0.1430 0.2465 0.1275 -0.0094 0.0356  0.0264  10  HIS   B CG   
1735 C  CG   B HIS   B 6   ? 0.1600 0.3239 0.1993 -0.0243 0.0285  0.0445  10  HIS   B CG   
1736 N  ND1  A HIS   B 6   ? 0.1364 0.2419 0.1398 -0.0061 0.0263  0.0385  10  HIS   B ND1  
1737 N  ND1  B HIS   B 6   ? 0.1616 0.3298 0.2153 -0.0271 0.0316  0.0560  10  HIS   B ND1  
1738 C  CD2  A HIS   B 6   ? 0.1238 0.2449 0.1174 -0.0034 0.0293  0.0303  10  HIS   B CD2  
1739 C  CD2  B HIS   B 6   ? 0.1605 0.3283 0.2089 -0.0221 0.0298  0.0562  10  HIS   B CD2  
1740 C  CE1  A HIS   B 6   ? 0.1180 0.2378 0.1372 -0.0051 0.0284  0.0367  10  HIS   B CE1  
1741 C  CE1  B HIS   B 6   ? 0.1292 0.3355 0.1860 -0.0106 0.0403  0.0731  10  HIS   B CE1  
1742 N  NE2  A HIS   B 6   ? 0.1188 0.2366 0.1260 -0.0012 0.0303  0.0342  10  HIS   B NE2  
1743 N  NE2  B HIS   B 6   ? 0.1554 0.3237 0.2072 -0.0222 0.0332  0.0605  10  HIS   B NE2  
1744 N  N    . MET   B 7   ? 0.1540 0.2653 0.1529 -0.0229 0.0212  0.0147  11  MET   B N    
1745 C  CA   . MET   B 7   ? 0.1618 0.2507 0.1529 -0.0193 0.0247  0.0115  11  MET   B CA   
1746 C  C    . MET   B 7   ? 0.1750 0.2373 0.1607 -0.0236 0.0115  0.0185  11  MET   B C    
1747 O  O    . MET   B 7   ? 0.2053 0.2344 0.1638 -0.0099 -0.0083 0.0059  11  MET   B O    
1748 C  CB   . MET   B 7   ? 0.1632 0.2561 0.1662 -0.0278 0.0294  0.0047  11  MET   B CB   
1749 C  CG   . MET   B 7   ? 0.1779 0.2496 0.1742 -0.0242 0.0379  -0.0023 11  MET   B CG   
1750 S  SD   . MET   B 7   ? 0.1871 0.2509 0.1906 -0.0193 0.0410  -0.0113 11  MET   B SD   
1751 C  CE   . MET   B 7   ? 0.2070 0.2585 0.1779 -0.0407 0.0441  -0.0133 11  MET   B CE   
1752 N  N    A GLN   B 8   ? 0.1784 0.2221 0.1574 -0.0217 0.0151  0.0252  12  GLN   B N    
1753 N  N    B GLN   B 8   ? 0.1854 0.2358 0.1614 -0.0189 0.0158  0.0227  12  GLN   B N    
1754 C  CA   A GLN   B 8   ? 0.1793 0.2198 0.1615 -0.0186 0.0117  0.0260  12  GLN   B CA   
1755 C  CA   B GLN   B 8   ? 0.1947 0.2433 0.1727 -0.0169 0.0160  0.0173  12  GLN   B CA   
1756 C  C    A GLN   B 8   ? 0.1735 0.2160 0.1598 -0.0169 0.0047  0.0144  12  GLN   B C    
1757 C  C    B GLN   B 8   ? 0.1793 0.2257 0.1657 -0.0182 0.0065  0.0113  12  GLN   B C    
1758 O  O    A GLN   B 8   ? 0.1754 0.2173 0.1583 -0.0222 0.0074  0.0110  12  GLN   B O    
1759 O  O    B GLN   B 8   ? 0.1798 0.2269 0.1625 -0.0225 0.0096  0.0071  12  GLN   B O    
1760 C  CB   A GLN   B 8   ? 0.1927 0.2208 0.1752 -0.0184 0.0050  0.0375  12  GLN   B CB   
1761 C  CB   B GLN   B 8   ? 0.2231 0.2682 0.2001 -0.0069 0.0104  0.0246  12  GLN   B CB   
1762 C  CG   A GLN   B 8   ? 0.2044 0.2283 0.1807 -0.0112 0.0064  0.0410  12  GLN   B CG   
1763 C  CG   B GLN   B 8   ? 0.2509 0.2898 0.2297 -0.0087 0.0084  0.0199  12  GLN   B CG   
1764 C  CD   A GLN   B 8   ? 0.2208 0.2331 0.2026 -0.0042 0.0036  0.0497  12  GLN   B CD   
1765 C  CD   B GLN   B 8   ? 0.2890 0.3084 0.2559 -0.0111 0.0151  0.0329  12  GLN   B CD   
1766 O  OE1  A GLN   B 8   ? 0.2320 0.2736 0.2132 -0.0045 -0.0028 0.0551  12  GLN   B OE1  
1767 O  OE1  B GLN   B 8   ? 0.3297 0.3575 0.2951 0.0078  0.0023  0.0148  12  GLN   B OE1  
1768 N  NE2  A GLN   B 8   ? 0.2444 0.2315 0.2213 -0.0034 0.0002  0.0525  12  GLN   B NE2  
1769 N  NE2  B GLN   B 8   ? 0.3147 0.3117 0.2742 -0.0092 0.0173  0.0401  12  GLN   B NE2  
1770 N  N    . THR   B 9   ? 0.1602 0.2114 0.1608 -0.0178 0.0047  -0.0016 13  THR   B N    
1771 C  CA   . THR   B 9   ? 0.1517 0.2227 0.1626 -0.0230 -0.0006 0.0004  13  THR   B CA   
1772 C  C    . THR   B 9   ? 0.1473 0.2057 0.1557 -0.0240 0.0015  -0.0030 13  THR   B C    
1773 O  O    . THR   B 9   ? 0.1676 0.2059 0.1923 -0.0219 -0.0043 -0.0152 13  THR   B O    
1774 C  CB   . THR   B 9   ? 0.1665 0.2480 0.1601 -0.0124 -0.0014 -0.0051 13  THR   B CB   
1775 O  OG1  . THR   B 9   ? 0.1729 0.2563 0.1659 -0.0057 -0.0102 -0.0073 13  THR   B OG1  
1776 C  CG2  . THR   B 9   ? 0.1749 0.2637 0.1710 -0.0033 0.0026  -0.0014 13  THR   B CG2  
1777 N  N    . LEU   B 10  ? 0.1481 0.2010 0.1412 -0.0259 0.0082  0.0047  14  LEU   B N    
1778 C  CA   . LEU   B 10  ? 0.1495 0.2106 0.1498 -0.0256 0.0157  0.0086  14  LEU   B CA   
1779 C  C    . LEU   B 10  ? 0.1508 0.1990 0.1367 -0.0272 0.0107  -0.0062 14  LEU   B C    
1780 O  O    . LEU   B 10  ? 0.1718 0.1917 0.1505 -0.0424 0.0151  -0.0185 14  LEU   B O    
1781 C  CB   . LEU   B 10  ? 0.1589 0.2353 0.1728 -0.0176 0.0080  0.0226  14  LEU   B CB   
1782 C  CG   . LEU   B 10  ? 0.2003 0.2755 0.1915 -0.0158 0.0073  0.0525  14  LEU   B CG   
1783 C  CD1  . LEU   B 10  ? 0.2229 0.3014 0.2130 0.0026  0.0075  0.0514  14  LEU   B CD1  
1784 C  CD2  . LEU   B 10  ? 0.2139 0.2846 0.2217 -0.0120 0.0158  0.0633  14  LEU   B CD2  
1785 N  N    . ILE   B 11  ? 0.1405 0.1932 0.1318 -0.0211 0.0092  -0.0075 15  ILE   B N    
1786 C  CA   . ILE   B 11  ? 0.1395 0.2073 0.1337 -0.0235 0.0105  -0.0033 15  ILE   B CA   
1787 C  C    . ILE   B 11  ? 0.1362 0.1939 0.1269 -0.0268 0.0050  0.0016  15  ILE   B C    
1788 O  O    . ILE   B 11  ? 0.1391 0.1931 0.1294 -0.0160 -0.0034 -0.0080 15  ILE   B O    
1789 C  CB   . ILE   B 11  ? 0.1601 0.2290 0.1528 -0.0178 0.0133  0.0093  15  ILE   B CB   
1790 C  CG1  . ILE   B 11  ? 0.1770 0.2562 0.1950 -0.0151 0.0213  0.0196  15  ILE   B CG1  
1791 C  CG2  . ILE   B 11  ? 0.1647 0.2388 0.1555 -0.0201 0.0116  0.0145  15  ILE   B CG2  
1792 C  CD1  . ILE   B 11  ? 0.2297 0.2785 0.2357 -0.0084 0.0216  0.0034  15  ILE   B CD1  
1793 N  N    . PHE   B 12  ? 0.1357 0.1904 0.1204 -0.0330 0.0011  0.0037  16  PHE   B N    
1794 C  CA   . PHE   B 12  ? 0.1379 0.1840 0.1232 -0.0353 -0.0033 0.0094  16  PHE   B CA   
1795 C  C    . PHE   B 12  ? 0.1390 0.1926 0.1099 -0.0362 -0.0102 0.0120  16  PHE   B C    
1796 O  O    . PHE   B 12  ? 0.1525 0.2128 0.1109 -0.0380 -0.0150 0.0117  16  PHE   B O    
1797 C  CB   . PHE   B 12  ? 0.1478 0.1815 0.1396 -0.0296 -0.0031 0.0118  16  PHE   B CB   
1798 C  CG   . PHE   B 12  ? 0.1597 0.1838 0.1490 -0.0322 -0.0049 0.0182  16  PHE   B CG   
1799 C  CD1  . PHE   B 12  ? 0.1710 0.1970 0.1607 -0.0384 -0.0120 0.0242  16  PHE   B CD1  
1800 C  CD2  . PHE   B 12  ? 0.1664 0.1968 0.1638 -0.0388 -0.0073 0.0265  16  PHE   B CD2  
1801 C  CE1  . PHE   B 12  ? 0.1944 0.2100 0.1655 -0.0338 -0.0158 0.0355  16  PHE   B CE1  
1802 C  CE2  . PHE   B 12  ? 0.1776 0.2033 0.1786 -0.0419 -0.0069 0.0344  16  PHE   B CE2  
1803 C  CZ   . PHE   B 12  ? 0.1915 0.2017 0.1683 -0.0359 -0.0018 0.0414  16  PHE   B CZ   
1804 N  N    . PHE   B 13  ? 0.1397 0.1919 0.1148 -0.0350 -0.0123 0.0150  17  PHE   B N    
1805 C  CA   . PHE   B 13  ? 0.1356 0.1858 0.1158 -0.0305 -0.0116 0.0134  17  PHE   B CA   
1806 C  C    . PHE   B 13  ? 0.1355 0.1863 0.1233 -0.0358 -0.0086 0.0103  17  PHE   B C    
1807 O  O    . PHE   B 13  ? 0.1298 0.2094 0.1214 -0.0446 -0.0036 0.0158  17  PHE   B O    
1808 C  CB   . PHE   B 13  ? 0.1406 0.1909 0.1147 -0.0214 -0.0136 0.0110  17  PHE   B CB   
1809 C  CG   . PHE   B 13  ? 0.1446 0.1919 0.1283 -0.0232 -0.0122 0.0084  17  PHE   B CG   
1810 C  CD1  . PHE   B 13  ? 0.1683 0.1906 0.1297 -0.0247 -0.0025 0.0090  17  PHE   B CD1  
1811 C  CD2  . PHE   B 13  ? 0.1583 0.1887 0.1383 -0.0184 -0.0105 0.0066  17  PHE   B CD2  
1812 C  CE1  . PHE   B 13  ? 0.1715 0.1896 0.1362 -0.0201 0.0020  0.0100  17  PHE   B CE1  
1813 C  CE2  . PHE   B 13  ? 0.1652 0.1884 0.1459 -0.0234 -0.0092 0.0060  17  PHE   B CE2  
1814 C  CZ   . PHE   B 13  ? 0.1595 0.1863 0.1417 -0.0208 0.0043  0.0085  17  PHE   B CZ   
1815 N  N    . ASP   B 14  ? 0.1333 0.1704 0.1170 -0.0359 -0.0137 0.0100  18  ASP   B N    
1816 C  CA   . ASP   B 14  ? 0.1362 0.1699 0.1208 -0.0342 -0.0078 0.0133  18  ASP   B CA   
1817 C  C    . ASP   B 14  ? 0.1380 0.1668 0.1127 -0.0338 -0.0129 0.0117  18  ASP   B C    
1818 O  O    . ASP   B 14  ? 0.1441 0.1614 0.1188 -0.0411 -0.0189 0.0067  18  ASP   B O    
1819 C  CB   . ASP   B 14  ? 0.1552 0.1786 0.1359 -0.0279 -0.0072 0.0095  18  ASP   B CB   
1820 C  CG   . ASP   B 14  ? 0.1604 0.2045 0.1585 -0.0245 -0.0083 0.0072  18  ASP   B CG   
1821 O  OD1  . ASP   B 14  ? 0.1360 0.2207 0.1575 -0.0288 -0.0252 0.0144  18  ASP   B OD1  
1822 O  OD2  . ASP   B 14  ? 0.1688 0.2184 0.1730 -0.0254 -0.0030 0.0039  18  ASP   B OD2  
1823 N  N    . MET   B 15  ? 0.1410 0.1648 0.1096 -0.0361 -0.0105 0.0099  19  MET   B N    
1824 C  CA   . MET   B 15  ? 0.1381 0.1601 0.1133 -0.0258 -0.0092 0.0145  19  MET   B CA   
1825 C  C    . MET   B 15  ? 0.1393 0.1562 0.1176 -0.0278 -0.0122 0.0148  19  MET   B C    
1826 O  O    . MET   B 15  ? 0.1541 0.1777 0.1228 -0.0298 -0.0149 0.0306  19  MET   B O    
1827 C  CB   . MET   B 15  ? 0.1490 0.1668 0.1282 -0.0257 -0.0044 0.0074  19  MET   B CB   
1828 C  CG   . MET   B 15  ? 0.1528 0.1766 0.1395 -0.0171 -0.0029 0.0041  19  MET   B CG   
1829 S  SD   . MET   B 15  ? 0.1783 0.1942 0.1622 -0.0089 -0.0085 0.0025  19  MET   B SD   
1830 C  CE   . MET   B 15  ? 0.1680 0.1993 0.1534 -0.0024 0.0108  -0.0149 19  MET   B CE   
1831 N  N    A GLU   B 16  ? 0.1394 0.1522 0.1210 -0.0256 -0.0118 0.0169  20  GLU   B N    
1832 N  N    B GLU   B 16  ? 0.1411 0.1531 0.1162 -0.0240 -0.0117 0.0154  20  GLU   B N    
1833 C  CA   A GLU   B 16  ? 0.1430 0.1483 0.1368 -0.0259 -0.0107 0.0164  20  GLU   B CA   
1834 C  CA   B GLU   B 16  ? 0.1444 0.1502 0.1247 -0.0232 -0.0090 0.0145  20  GLU   B CA   
1835 C  C    A GLU   B 16  ? 0.1390 0.1449 0.1319 -0.0230 -0.0101 0.0127  20  GLU   B C    
1836 C  C    B GLU   B 16  ? 0.1384 0.1464 0.1256 -0.0215 -0.0091 0.0117  20  GLU   B C    
1837 O  O    A GLU   B 16  ? 0.1373 0.1499 0.1264 -0.0266 -0.0156 0.0133  20  GLU   B O    
1838 O  O    B GLU   B 16  ? 0.1354 0.1547 0.1189 -0.0239 -0.0115 0.0130  20  GLU   B O    
1839 C  CB   A GLU   B 16  ? 0.1553 0.1590 0.1582 -0.0216 -0.0065 0.0120  20  GLU   B CB   
1840 C  CB   B GLU   B 16  ? 0.1587 0.1632 0.1384 -0.0177 -0.0043 0.0106  20  GLU   B CB   
1841 C  CG   A GLU   B 16  ? 0.1753 0.1659 0.1873 -0.0245 -0.0038 0.0138  20  GLU   B CG   
1842 C  CG   B GLU   B 16  ? 0.1786 0.1708 0.1570 -0.0173 -0.0019 0.0142  20  GLU   B CG   
1843 C  CD   A GLU   B 16  ? 0.2055 0.1850 0.2200 -0.0154 -0.0129 0.0148  20  GLU   B CD   
1844 C  CD   B GLU   B 16  ? 0.2046 0.1904 0.1722 -0.0103 0.0021  0.0059  20  GLU   B CD   
1845 O  OE1  A GLU   B 16  ? 0.2246 0.2128 0.2555 -0.0144 -0.0182 0.0009  20  GLU   B OE1  
1846 O  OE1  B GLU   B 16  ? 0.2479 0.2312 0.1911 -0.0010 0.0013  0.0158  20  GLU   B OE1  
1847 O  OE2  A GLU   B 16  ? 0.2542 0.1911 0.2563 -0.0071 -0.0088 0.0065  20  GLU   B OE2  
1848 O  OE2  B GLU   B 16  ? 0.2344 0.1938 0.1956 -0.0009 0.0125  -0.0037 20  GLU   B OE2  
1849 N  N    . ALA   B 17  ? 0.1399 0.1356 0.1363 -0.0203 -0.0135 0.0103  21  ALA   B N    
1850 C  CA   . ALA   B 17  ? 0.1435 0.1330 0.1357 -0.0238 -0.0087 0.0097  21  ALA   B CA   
1851 C  C    . ALA   B 17  ? 0.1408 0.1411 0.1420 -0.0185 -0.0085 0.0033  21  ALA   B C    
1852 O  O    . ALA   B 17  ? 0.1505 0.1425 0.1607 -0.0140 -0.0129 0.0080  21  ALA   B O    
1853 C  CB   . ALA   B 17  ? 0.1528 0.1403 0.1464 -0.0243 -0.0025 0.0064  21  ALA   B CB   
1854 N  N    . THR   B 18  ? 0.1411 0.1353 0.1336 -0.0141 -0.0058 0.0028  22  THR   B N    
1855 C  CA   . THR   B 18  ? 0.1361 0.1484 0.1375 -0.0170 -0.0048 -0.0001 22  THR   B CA   
1856 C  C    . THR   B 18  ? 0.1227 0.1537 0.1444 -0.0162 -0.0011 -0.0002 22  THR   B C    
1857 O  O    . THR   B 18  ? 0.1191 0.1974 0.1604 -0.0208 0.0009  -0.0112 22  THR   B O    
1858 C  CB   . THR   B 18  ? 0.1462 0.1496 0.1434 -0.0173 -0.0059 0.0053  22  THR   B CB   
1859 O  OG1  . THR   B 18  ? 0.1481 0.1463 0.1471 -0.0192 0.0000  0.0035  22  THR   B OG1  
1860 C  CG2  . THR   B 18  ? 0.1498 0.1480 0.1408 -0.0158 -0.0062 0.0115  22  THR   B CG2  
1861 N  N    . GLY   B 19  ? 0.1209 0.1629 0.1386 -0.0220 -0.0111 0.0008  23  GLY   B N    
1862 C  CA   . GLY   B 19  ? 0.1252 0.1659 0.1468 -0.0181 -0.0148 0.0083  23  GLY   B CA   
1863 C  C    . GLY   B 19  ? 0.1319 0.1673 0.1448 -0.0159 -0.0199 0.0116  23  GLY   B C    
1864 O  O    . GLY   B 19  ? 0.1250 0.1700 0.1347 -0.0146 -0.0276 0.0129  23  GLY   B O    
1865 N  N    . LEU   B 20  ? 0.1463 0.1808 0.1482 -0.0215 -0.0269 0.0171  24  LEU   B N    
1866 C  CA   . LEU   B 20  ? 0.1478 0.1885 0.1427 -0.0206 -0.0287 0.0199  24  LEU   B CA   
1867 C  C    . LEU   B 20  ? 0.1612 0.1928 0.1435 -0.0149 -0.0278 0.0249  24  LEU   B C    
1868 O  O    . LEU   B 20  ? 0.1707 0.1792 0.1465 -0.0165 -0.0206 0.0182  24  LEU   B O    
1869 C  CB   . LEU   B 20  ? 0.1554 0.1984 0.1563 -0.0134 -0.0301 0.0355  24  LEU   B CB   
1870 C  CG   . LEU   B 20  ? 0.1709 0.2180 0.1790 -0.0027 -0.0318 0.0353  24  LEU   B CG   
1871 C  CD1  . LEU   B 20  ? 0.1819 0.2367 0.1972 0.0054  -0.0393 0.0368  24  LEU   B CD1  
1872 C  CD2  . LEU   B 20  ? 0.1936 0.2206 0.2082 -0.0052 -0.0364 0.0389  24  LEU   B CD2  
1873 N  N    . PRO   B 21  ? 0.1685 0.2077 0.1465 -0.0135 -0.0308 0.0204  25  PRO   B N    
1874 C  CA   . PRO   B 21  ? 0.1806 0.2135 0.1512 -0.0156 -0.0254 0.0139  25  PRO   B CA   
1875 C  C    . PRO   B 21  ? 0.2008 0.2175 0.1656 -0.0212 -0.0222 0.0051  25  PRO   B C    
1876 O  O    . PRO   B 21  ? 0.2437 0.2141 0.1750 -0.0175 -0.0135 0.0047  25  PRO   B O    
1877 C  CB   . PRO   B 21  ? 0.1805 0.2244 0.1370 -0.0160 -0.0367 0.0185  25  PRO   B CB   
1878 C  CG   . PRO   B 21  ? 0.1770 0.2237 0.1304 -0.0184 -0.0379 0.0231  25  PRO   B CG   
1879 C  CD   . PRO   B 21  ? 0.1775 0.2181 0.1340 -0.0172 -0.0387 0.0201  25  PRO   B CD   
1880 N  N    . SER   B 22  ? 0.2105 0.2229 0.1826 -0.0224 -0.0281 0.0048  26  SER   B N    
1881 C  CA   . SER   B 22  ? 0.2233 0.2380 0.2074 -0.0349 -0.0344 -0.0013 26  SER   B CA   
1882 C  C    . SER   B 22  ? 0.2052 0.2090 0.2051 -0.0345 -0.0332 -0.0021 26  SER   B C    
1883 O  O    . SER   B 22  ? 0.2440 0.2162 0.2020 -0.0443 -0.0439 -0.0162 26  SER   B O    
1884 C  CB   . SER   B 22  ? 0.2320 0.2599 0.2404 -0.0375 -0.0461 0.0106  26  SER   B CB   
1885 O  OG   . SER   B 22  ? 0.2367 0.2861 0.3114 -0.0134 -0.0490 0.0119  26  SER   B OG   
1886 N  N    . SER   B 23  ? 0.1847 0.1917 0.1836 -0.0395 -0.0296 0.0049  27  SER   B N    
1887 C  CA   . SER   B 23  ? 0.1842 0.1685 0.1795 -0.0390 -0.0216 0.0009  27  SER   B CA   
1888 C  C    . SER   B 23  ? 0.1902 0.1536 0.1747 -0.0321 -0.0188 -0.0023 27  SER   B C    
1889 O  O    . SER   B 23  ? 0.2081 0.1709 0.1849 -0.0237 -0.0163 0.0026  27  SER   B O    
1890 C  CB   . SER   B 23  ? 0.1787 0.1711 0.1752 -0.0257 -0.0230 0.0077  27  SER   B CB   
1891 O  OG   . SER   B 23  ? 0.1781 0.1762 0.1776 -0.0239 -0.0253 0.0021  27  SER   B OG   
1892 N  N    . ARG   B 24  ? 0.1924 0.1575 0.1573 -0.0296 -0.0227 -0.0046 28  ARG   B N    
1893 C  CA   . ARG   B 24  ? 0.1888 0.1575 0.1631 -0.0252 -0.0189 -0.0066 28  ARG   B CA   
1894 C  C    . ARG   B 24  ? 0.1747 0.1472 0.1476 -0.0217 -0.0166 -0.0001 28  ARG   B C    
1895 O  O    . ARG   B 24  ? 0.1799 0.1556 0.1564 -0.0154 -0.0163 0.0088  28  ARG   B O    
1896 C  CB   . ARG   B 24  ? 0.2052 0.1629 0.1742 -0.0292 -0.0189 -0.0076 28  ARG   B CB   
1897 C  CG   . ARG   B 24  ? 0.2225 0.1748 0.2051 -0.0323 -0.0257 -0.0003 28  ARG   B CG   
1898 C  CD   . ARG   B 24  ? 0.2567 0.1923 0.2217 -0.0363 -0.0255 0.0064  28  ARG   B CD   
1899 N  NE   . ARG   B 24  ? 0.2784 0.2074 0.2438 -0.0225 -0.0232 0.0174  28  ARG   B NE   
1900 C  CZ   . ARG   B 24  ? 0.2945 0.2313 0.2266 -0.0290 -0.0255 0.0202  28  ARG   B CZ   
1901 N  NH1  . ARG   B 24  ? 0.3189 0.2720 0.2406 -0.0274 -0.0277 0.0198  28  ARG   B NH1  
1902 N  NH2  . ARG   B 24  ? 0.3355 0.2353 0.2048 -0.0411 -0.0266 0.0182  28  ARG   B NH2  
1903 N  N    . PRO   B 25  ? 0.1751 0.1507 0.1436 -0.0259 -0.0172 -0.0082 29  PRO   B N    
1904 C  CA   . PRO   B 25  ? 0.1705 0.1462 0.1407 -0.0220 -0.0178 -0.0096 29  PRO   B CA   
1905 C  C    . PRO   B 25  ? 0.1690 0.1515 0.1393 -0.0210 -0.0154 -0.0101 29  PRO   B C    
1906 O  O    . PRO   B 25  ? 0.1673 0.1637 0.1268 -0.0177 -0.0169 -0.0171 29  PRO   B O    
1907 C  CB   . PRO   B 25  ? 0.1680 0.1464 0.1455 -0.0246 -0.0185 -0.0070 29  PRO   B CB   
1908 C  CG   . PRO   B 25  ? 0.1694 0.1431 0.1405 -0.0328 -0.0187 -0.0019 29  PRO   B CG   
1909 C  CD   . PRO   B 25  ? 0.1663 0.1424 0.1369 -0.0304 -0.0154 -0.0086 29  PRO   B CD   
1910 N  N    . GLU   B 26  ? 0.1700 0.1489 0.1306 -0.0217 -0.0133 -0.0043 30  GLU   B N    
1911 C  CA   . GLU   B 26  ? 0.1748 0.1427 0.1399 -0.0234 -0.0189 -0.0047 30  GLU   B CA   
1912 C  C    . GLU   B 26  ? 0.1496 0.1323 0.1348 -0.0191 -0.0170 -0.0005 30  GLU   B C    
1913 O  O    . GLU   B 26  ? 0.1507 0.1492 0.1441 -0.0192 -0.0145 -0.0084 30  GLU   B O    
1914 C  CB   . GLU   B 26  ? 0.2045 0.1538 0.1496 -0.0197 -0.0231 0.0008  30  GLU   B CB   
1915 C  CG   . GLU   B 26  ? 0.2404 0.1630 0.1534 -0.0254 -0.0254 -0.0068 30  GLU   B CG   
1916 C  CD   . GLU   B 26  ? 0.2826 0.1746 0.1737 -0.0230 -0.0245 0.0031  30  GLU   B CD   
1917 O  OE1  . GLU   B 26  ? 0.3074 0.2048 0.1660 -0.0111 -0.0118 -0.0033 30  GLU   B OE1  
1918 O  OE2  . GLU   B 26  ? 0.3415 0.1909 0.2008 -0.0371 -0.0339 -0.0031 30  GLU   B OE2  
1919 N  N    . VAL   B 27  ? 0.1457 0.1387 0.1425 -0.0116 -0.0216 0.0029  31  VAL   B N    
1920 C  CA   . VAL   B 27  ? 0.1354 0.1407 0.1399 -0.0186 -0.0184 0.0086  31  VAL   B CA   
1921 C  C    . VAL   B 27  ? 0.1359 0.1406 0.1342 -0.0214 -0.0185 0.0150  31  VAL   B C    
1922 O  O    . VAL   B 27  ? 0.1556 0.1264 0.1463 -0.0193 -0.0194 0.0194  31  VAL   B O    
1923 C  CB   . VAL   B 27  ? 0.1332 0.1492 0.1459 -0.0111 -0.0190 0.0091  31  VAL   B CB   
1924 C  CG1  . VAL   B 27  ? 0.1340 0.1567 0.1548 -0.0127 -0.0205 0.0077  31  VAL   B CG1  
1925 C  CG2  . VAL   B 27  ? 0.1424 0.1502 0.1512 -0.0112 -0.0153 0.0080  31  VAL   B CG2  
1926 N  N    . THR   B 28  ? 0.1414 0.1394 0.1176 -0.0179 -0.0187 0.0199  32  THR   B N    
1927 C  CA   . THR   B 28  ? 0.1473 0.1436 0.1149 -0.0246 -0.0119 0.0180  32  THR   B CA   
1928 C  C    . THR   B 28  ? 0.1476 0.1482 0.1130 -0.0266 -0.0115 0.0130  32  THR   B C    
1929 O  O    . THR   B 28  ? 0.1539 0.1451 0.1091 -0.0238 -0.0047 0.0082  32  THR   B O    
1930 C  CB   . THR   B 28  ? 0.1493 0.1482 0.1263 -0.0268 -0.0050 0.0218  32  THR   B CB   
1931 O  OG1  . THR   B 28  ? 0.1644 0.1441 0.1349 -0.0273 -0.0039 0.0293  32  THR   B OG1  
1932 C  CG2  . THR   B 28  ? 0.1546 0.1550 0.1400 -0.0306 -0.0016 0.0160  32  THR   B CG2  
1933 N  N    . GLU   B 29  ? 0.1452 0.1494 0.1128 -0.0295 -0.0129 0.0099  33  GLU   B N    
1934 C  CA   . GLU   B 29  ? 0.1483 0.1520 0.1184 -0.0317 -0.0129 0.0063  33  GLU   B CA   
1935 C  C    . GLU   B 29  ? 0.1414 0.1487 0.1203 -0.0329 -0.0160 0.0034  33  GLU   B C    
1936 O  O    . GLU   B 29  ? 0.1400 0.1586 0.1188 -0.0346 -0.0253 0.0090  33  GLU   B O    
1937 C  CB   . GLU   B 29  ? 0.1631 0.1648 0.1425 -0.0260 -0.0070 0.0059  33  GLU   B CB   
1938 C  CG   . GLU   B 29  ? 0.1875 0.1848 0.1590 -0.0290 -0.0050 -0.0011 33  GLU   B CG   
1939 C  CD   . GLU   B 29  ? 0.2208 0.2033 0.1857 -0.0179 -0.0023 -0.0028 33  GLU   B CD   
1940 O  OE1  . GLU   B 29  ? 0.2198 0.2176 0.2088 -0.0060 0.0043  0.0196  33  GLU   B OE1  
1941 O  OE2  . GLU   B 29  ? 0.2794 0.2207 0.2094 -0.0109 0.0029  -0.0222 33  GLU   B OE2  
1942 N  N    . LEU   B 30  ? 0.1420 0.1578 0.1217 -0.0383 -0.0154 0.0045  34  LEU   B N    
1943 C  CA   . LEU   B 30  ? 0.1447 0.1651 0.1236 -0.0383 -0.0140 0.0071  34  LEU   B CA   
1944 C  C    . LEU   B 30  ? 0.1480 0.1647 0.1134 -0.0363 -0.0087 0.0029  34  LEU   B C    
1945 O  O    . LEU   B 30  ? 0.1632 0.1781 0.1045 -0.0494 -0.0139 0.0032  34  LEU   B O    
1946 C  CB   . LEU   B 30  ? 0.1602 0.1758 0.1541 -0.0353 -0.0123 0.0053  34  LEU   B CB   
1947 C  CG   . LEU   B 30  ? 0.1720 0.1944 0.1815 -0.0230 -0.0201 0.0070  34  LEU   B CG   
1948 C  CD1  . LEU   B 30  ? 0.1757 0.2005 0.1920 -0.0224 -0.0236 0.0070  34  LEU   B CD1  
1949 C  CD2  . LEU   B 30  ? 0.1853 0.2024 0.2131 -0.0253 -0.0240 0.0141  34  LEU   B CD2  
1950 N  N    . CYS   B 31  ? 0.1404 0.1635 0.1099 -0.0324 -0.0076 0.0044  35  CYS   B N    
1951 C  CA   . CYS   B 31  ? 0.1316 0.1618 0.1191 -0.0272 -0.0068 0.0015  35  CYS   B CA   
1952 C  C    . CYS   B 31  ? 0.1318 0.1579 0.1112 -0.0202 -0.0101 0.0000  35  CYS   B C    
1953 O  O    . CYS   B 31  ? 0.1389 0.1652 0.1149 -0.0213 -0.0156 -0.0022 35  CYS   B O    
1954 C  CB   . CYS   B 31  ? 0.1469 0.1708 0.1460 -0.0219 -0.0005 -0.0003 35  CYS   B CB   
1955 S  SG   . CYS   B 31  ? 0.1752 0.1751 0.2185 -0.0217 0.0042  -0.0113 35  CYS   B SG   
1956 N  N    . LEU   B 32  ? 0.1309 0.1699 0.1128 -0.0223 -0.0078 0.0009  36  LEU   B N    
1957 C  CA   . LEU   B 32  ? 0.1373 0.1736 0.1122 -0.0228 -0.0062 0.0010  36  LEU   B CA   
1958 C  C    . LEU   B 32  ? 0.1363 0.1735 0.1074 -0.0258 -0.0039 -0.0023 36  LEU   B C    
1959 O  O    . LEU   B 32  ? 0.1445 0.1770 0.1158 -0.0462 -0.0188 -0.0043 36  LEU   B O    
1960 C  CB   . LEU   B 32  ? 0.1433 0.1849 0.1261 -0.0133 -0.0038 0.0057  36  LEU   B CB   
1961 C  CG   . LEU   B 32  ? 0.1627 0.1900 0.1567 -0.0036 -0.0111 -0.0035 36  LEU   B CG   
1962 C  CD1  . LEU   B 32  ? 0.1897 0.2050 0.1735 -0.0046 -0.0070 -0.0017 36  LEU   B CD1  
1963 C  CD2  . LEU   B 32  ? 0.1695 0.1928 0.1775 -0.0016 -0.0181 -0.0014 36  LEU   B CD2  
1964 N  N    A LEU   B 33  ? 0.1407 0.1755 0.1165 -0.0247 -0.0085 0.0023  37  LEU   B N    
1965 N  N    B LEU   B 33  ? 0.1372 0.1742 0.1101 -0.0256 -0.0071 0.0003  37  LEU   B N    
1966 C  CA   A LEU   B 33  ? 0.1481 0.1778 0.1240 -0.0207 -0.0045 0.0021  37  LEU   B CA   
1967 C  CA   B LEU   B 33  ? 0.1434 0.1756 0.1104 -0.0218 -0.0021 -0.0003 37  LEU   B CA   
1968 C  C    A LEU   B 33  ? 0.1433 0.1720 0.1199 -0.0236 -0.0047 0.0041  37  LEU   B C    
1969 C  C    B LEU   B 33  ? 0.1401 0.1722 0.1127 -0.0237 -0.0019 0.0028  37  LEU   B C    
1970 O  O    A LEU   B 33  ? 0.1394 0.1646 0.1192 -0.0300 -0.0069 0.0031  37  LEU   B O    
1971 O  O    B LEU   B 33  ? 0.1373 0.1721 0.1141 -0.0282 -0.0040 0.0064  37  LEU   B O    
1972 C  CB   A LEU   B 33  ? 0.1578 0.1957 0.1467 -0.0106 -0.0060 0.0073  37  LEU   B CB   
1973 C  CB   B LEU   B 33  ? 0.1481 0.1880 0.1190 -0.0155 -0.0003 0.0022  37  LEU   B CB   
1974 C  CG   A LEU   B 33  ? 0.1754 0.1973 0.1727 -0.0032 -0.0017 0.0133  37  LEU   B CG   
1975 C  CG   B LEU   B 33  ? 0.1588 0.1887 0.1256 -0.0091 0.0042  0.0015  37  LEU   B CG   
1976 C  CD1  A LEU   B 33  ? 0.1807 0.2010 0.1869 -0.0037 -0.0063 0.0091  37  LEU   B CD1  
1977 C  CD1  B LEU   B 33  ? 0.1617 0.1889 0.1184 -0.0074 0.0088  0.0018  37  LEU   B CD1  
1978 C  CD2  A LEU   B 33  ? 0.1881 0.2109 0.1827 0.0021  -0.0046 0.0149  37  LEU   B CD2  
1979 C  CD2  B LEU   B 33  ? 0.1615 0.1952 0.1440 -0.0134 0.0107  0.0015  37  LEU   B CD2  
1980 N  N    . ALA   B 34  ? 0.1429 0.1737 0.1140 -0.0203 -0.0019 0.0051  38  ALA   B N    
1981 C  CA   . ALA   B 34  ? 0.1462 0.1763 0.1280 -0.0210 0.0013  -0.0013 38  ALA   B CA   
1982 C  C    . ALA   B 34  ? 0.1532 0.1727 0.1334 -0.0227 0.0033  -0.0046 38  ALA   B C    
1983 O  O    . ALA   B 34  ? 0.1558 0.1761 0.1440 -0.0202 -0.0120 -0.0076 38  ALA   B O    
1984 C  CB   . ALA   B 34  ? 0.1517 0.1818 0.1383 -0.0128 0.0029  -0.0010 38  ALA   B CB   
1985 N  N    . VAL   B 35  ? 0.1776 0.1876 0.1403 -0.0321 0.0074  -0.0019 39  VAL   B N    
1986 C  CA   . VAL   B 35  ? 0.1944 0.2038 0.1642 -0.0346 0.0117  0.0004  39  VAL   B CA   
1987 C  C    . VAL   B 35  ? 0.1895 0.1923 0.1567 -0.0366 0.0120  0.0039  39  VAL   B C    
1988 O  O    . VAL   B 35  ? 0.2051 0.1929 0.1658 -0.0376 0.0136  -0.0037 39  VAL   B O    
1989 C  CB   . VAL   B 35  ? 0.2101 0.2328 0.1968 -0.0168 0.0137  0.0091  39  VAL   B CB   
1990 C  CG1  . VAL   B 35  ? 0.2396 0.2581 0.2211 -0.0086 0.0093  0.0220  39  VAL   B CG1  
1991 C  CG2  . VAL   B 35  ? 0.2064 0.2468 0.1953 -0.0150 0.0120  0.0116  39  VAL   B CG2  
1992 N  N    . HIS   B 36  ? 0.1886 0.2172 0.1527 -0.0375 0.0162  -0.0044 40  HIS   B N    
1993 C  CA   . HIS   B 36  ? 0.1793 0.2184 0.1695 -0.0324 0.0153  -0.0043 40  HIS   B CA   
1994 C  C    . HIS   B 36  ? 0.1730 0.2109 0.1750 -0.0252 0.0206  0.0038  40  HIS   B C    
1995 O  O    . HIS   B 36  ? 0.1802 0.2157 0.1621 -0.0141 0.0378  0.0093  40  HIS   B O    
1996 C  CB   . HIS   B 36  ? 0.2020 0.2451 0.1906 -0.0372 -0.0032 -0.0109 40  HIS   B CB   
1997 C  CG   . HIS   B 36  ? 0.2131 0.2725 0.2029 -0.0204 -0.0001 -0.0202 40  HIS   B CG   
1998 N  ND1  . HIS   B 36  ? 0.2323 0.2951 0.2722 -0.0176 0.0301  -0.0002 40  HIS   B ND1  
1999 C  CD2  . HIS   B 36  ? 0.2464 0.2973 0.2145 -0.0127 -0.0116 -0.0095 40  HIS   B CD2  
2000 C  CE1  . HIS   B 36  ? 0.2390 0.3087 0.2775 -0.0080 0.0199  -0.0028 40  HIS   B CE1  
2001 N  NE2  . HIS   B 36  ? 0.2424 0.3273 0.2509 -0.0131 -0.0030 -0.0035 40  HIS   B NE2  
2002 N  N    . ARG   B 37  ? 0.1849 0.2159 0.1805 -0.0204 0.0260  0.0142  41  ARG   B N    
2003 C  CA   . ARG   B 37  ? 0.2048 0.2115 0.1860 -0.0222 0.0269  0.0236  41  ARG   B CA   
2004 C  C    . ARG   B 37  ? 0.2093 0.2204 0.1950 -0.0229 0.0346  0.0291  41  ARG   B C    
2005 O  O    . ARG   B 37  ? 0.2107 0.2194 0.2164 -0.0154 0.0267  0.0350  41  ARG   B O    
2006 C  CB   . ARG   B 37  ? 0.2229 0.2287 0.2080 -0.0160 0.0333  0.0189  41  ARG   B CB   
2007 C  CG   . ARG   B 37  ? 0.2207 0.2311 0.2265 -0.0168 0.0300  0.0166  41  ARG   B CG   
2008 C  CD   . ARG   B 37  ? 0.2159 0.2401 0.2279 -0.0106 0.0383  0.0157  41  ARG   B CD   
2009 N  NE   . ARG   B 37  ? 0.2362 0.2557 0.2364 -0.0057 0.0330  0.0154  41  ARG   B NE   
2010 C  CZ   . ARG   B 37  ? 0.2378 0.2805 0.2244 0.0146  0.0269  0.0281  41  ARG   B CZ   
2011 N  NH1  . ARG   B 37  ? 0.2389 0.2891 0.2124 0.0143  0.0221  0.0269  41  ARG   B NH1  
2012 N  NH2  . ARG   B 37  ? 0.2520 0.2915 0.2388 0.0188  0.0275  0.0403  41  ARG   B NH2  
2013 N  N    . CYS   B 38  ? 0.2110 0.2295 0.2095 -0.0234 0.0286  0.0332  42  CYS   B N    
2014 C  CA   . CYS   B 38  ? 0.2337 0.2443 0.2533 -0.0353 0.0310  0.0237  42  CYS   B CA   
2015 C  C    . CYS   B 38  ? 0.2467 0.2382 0.2730 -0.0304 0.0322  0.0250  42  CYS   B C    
2016 O  O    . CYS   B 38  ? 0.2691 0.2339 0.2809 -0.0360 0.0368  0.0298  42  CYS   B O    
2017 C  CB   . CYS   B 38  ? 0.2588 0.2914 0.2728 -0.0376 0.0163  0.0110  42  CYS   B CB   
2018 S  SG   . CYS   B 38  ? 0.2856 0.3386 0.2741 -0.0394 0.0167  -0.0099 42  CYS   B SG   
2019 N  N    . ALA   B 39  ? 0.2361 0.2278 0.2787 -0.0184 0.0449  0.0200  43  ALA   B N    
2020 C  CA   . ALA   B 39  ? 0.2438 0.2265 0.3123 -0.0091 0.0481  0.0190  43  ALA   B CA   
2021 C  C    . ALA   B 39  ? 0.2259 0.2299 0.3144 -0.0006 0.0475  0.0250  43  ALA   B C    
2022 O  O    . ALA   B 39  ? 0.2594 0.2195 0.3493 0.0033  0.0358  0.0150  43  ALA   B O    
2023 C  CB   . ALA   B 39  ? 0.2650 0.2449 0.3150 0.0013  0.0585  0.0168  43  ALA   B CB   
2024 N  N    . LEU   B 40  ? 0.2089 0.2332 0.3133 -0.0010 0.0436  0.0290  44  LEU   B N    
2025 C  CA   . LEU   B 40  ? 0.2081 0.2608 0.3187 -0.0087 0.0491  0.0367  44  LEU   B CA   
2026 C  C    . LEU   B 40  ? 0.2086 0.2715 0.3047 -0.0106 0.0420  0.0476  44  LEU   B C    
2027 O  O    . LEU   B 40  ? 0.2070 0.2899 0.3255 0.0044  0.0399  0.0616  44  LEU   B O    
2028 C  CB   . LEU   B 40  ? 0.2150 0.2786 0.3480 -0.0243 0.0544  0.0312  44  LEU   B CB   
2029 C  CG   . LEU   B 40  ? 0.2569 0.3163 0.3958 -0.0478 0.0850  0.0218  44  LEU   B CG   
2030 C  CD1  . LEU   B 40  ? 0.2703 0.3394 0.4197 -0.0653 0.1036  0.0093  44  LEU   B CD1  
2031 C  CD2  . LEU   B 40  ? 0.2778 0.3366 0.4278 -0.0449 0.0822  0.0189  44  LEU   B CD2  
2032 N  N    . GLU   B 41  ? 0.2137 0.2865 0.2993 -0.0139 0.0460  0.0541  45  GLU   B N    
2033 C  CA   . GLU   B 41  ? 0.2324 0.3183 0.3174 -0.0296 0.0527  0.0584  45  GLU   B CA   
2034 C  C    . GLU   B 41  ? 0.2457 0.3055 0.3217 -0.0293 0.0722  0.0720  45  GLU   B C    
2035 O  O    . GLU   B 41  ? 0.2644 0.3429 0.3466 -0.0387 0.0729  0.0942  45  GLU   B O    
2036 C  CB   . GLU   B 41  ? 0.2494 0.3644 0.3631 -0.0202 0.0507  0.0510  45  GLU   B CB   
2037 C  CG   . GLU   B 41  ? 0.2695 0.4192 0.4036 -0.0088 0.0509  0.0283  45  GLU   B CG   
2038 C  CD   . GLU   B 41  ? 0.2935 0.4436 0.4693 0.0076  0.0382  0.0097  45  GLU   B CD   
2039 O  OE1  . GLU   B 41  ? 0.3393 0.4504 0.5555 -0.0106 0.0439  -0.0381 45  GLU   B OE1  
2040 O  OE2  . GLU   B 41  ? 0.2727 0.4435 0.5102 0.0299  -0.0058 0.0315  45  GLU   B OE2  
2041 N  N    . SER   B 42  ? 0.2848 0.2843 0.3479 -0.0491 0.0914  0.0510  46  SER   B N    
2042 C  CA   . SER   B 42  ? 0.3237 0.2919 0.3737 -0.0635 0.0977  0.0465  46  SER   B CA   
2043 C  C    . SER   B 42  ? 0.3634 0.2948 0.3986 -0.0520 0.1034  0.0391  46  SER   B C    
2044 O  O    . SER   B 42  ? 0.4063 0.2656 0.4027 -0.0456 0.0895  0.0318  46  SER   B O    
2045 C  CB   . SER   B 42  ? 0.3272 0.3188 0.3818 -0.0700 0.0979  0.0236  46  SER   B CB   
2046 O  OG   . SER   B 42  ? 0.3389 0.3645 0.3885 -0.0867 0.1124  0.0145  46  SER   B OG   
2047 N  N    . PRO   B 43  ? 0.3895 0.3035 0.4454 -0.0406 0.1151  0.0662  47  PRO   B N    
2048 C  CA   . PRO   B 43  ? 0.4096 0.3342 0.4769 -0.0371 0.1311  0.0706  47  PRO   B CA   
2049 C  C    . PRO   B 43  ? 0.4666 0.3298 0.4928 -0.0464 0.1484  0.0955  47  PRO   B C    
2050 O  O    . PRO   B 43  ? 0.4916 0.3474 0.5155 -0.0566 0.1533  0.1283  47  PRO   B O    
2051 C  CB   . PRO   B 43  ? 0.4041 0.3504 0.4925 -0.0440 0.1274  0.0701  47  PRO   B CB   
2052 C  CG   . PRO   B 43  ? 0.4062 0.3507 0.5035 -0.0324 0.1109  0.0568  47  PRO   B CG   
2053 C  CD   . PRO   B 43  ? 0.3871 0.3190 0.4722 -0.0430 0.1080  0.0642  47  PRO   B CD   
2054 N  N    . PRO   B 44  ? 0.5550 0.4056 0.5316 -0.0214 0.1458  0.0818  48  PRO   B N    
2055 C  CA   . PRO   B 44  ? 0.5932 0.4473 0.5584 -0.0117 0.1474  0.0607  48  PRO   B CA   
2056 C  C    . PRO   B 44  ? 0.5966 0.4925 0.5889 0.0304  0.1501  0.0562  48  PRO   B C    
2057 O  O    . PRO   B 44  ? 0.6291 0.5158 0.6452 0.0288  0.1511  0.0365  48  PRO   B O    
2058 C  CB   . PRO   B 44  ? 0.6174 0.4512 0.5589 -0.0079 0.1432  0.0688  48  PRO   B CB   
2059 C  CG   . PRO   B 44  ? 0.6196 0.4488 0.5426 -0.0124 0.1421  0.0818  48  PRO   B CG   
2060 C  CD   . PRO   B 44  ? 0.5839 0.4362 0.5425 -0.0198 0.1467  0.0909  48  PRO   B CD   
2061 N  N    . PRO   B 51  ? 0.6883 0.5546 0.8838 0.0170  -0.1502 -0.0352 55  PRO   B N    
2062 C  CA   . PRO   B 51  ? 0.6867 0.5041 0.8531 0.0340  -0.1431 -0.0239 55  PRO   B CA   
2063 C  C    . PRO   B 51  ? 0.6382 0.4332 0.8189 0.0559  -0.1260 0.0009  55  PRO   B C    
2064 O  O    . PRO   B 51  ? 0.6769 0.4385 0.8178 0.0476  -0.1158 0.0014  55  PRO   B O    
2065 C  CB   . PRO   B 51  ? 0.6857 0.5497 0.8615 0.0407  -0.1546 -0.0236 55  PRO   B CB   
2066 C  CG   . PRO   B 51  ? 0.6942 0.5470 0.8739 0.0398  -0.1532 -0.0205 55  PRO   B CG   
2067 C  CD   . PRO   B 51  ? 0.6908 0.5443 0.8887 0.0147  -0.1499 -0.0294 55  PRO   B CD   
2068 N  N    . THR   B 52  ? 0.5902 0.3293 0.7743 0.0939  -0.1249 0.0143  56  THR   B N    
2069 C  CA   . THR   B 52  ? 0.5718 0.3638 0.7384 0.0881  -0.1131 0.0256  56  THR   B CA   
2070 C  C    . THR   B 52  ? 0.5202 0.3358 0.6453 0.0636  -0.0961 0.0430  56  THR   B C    
2071 O  O    . THR   B 52  ? 0.5938 0.3469 0.6584 0.0778  -0.0912 0.0787  56  THR   B O    
2072 C  CB   . THR   B 52  ? 0.6121 0.4860 0.7709 0.0419  -0.1048 0.0137  56  THR   B CB   
2073 O  OG1  . THR   B 52  ? 0.6218 0.5191 0.8039 0.0504  -0.1185 -0.0051 56  THR   B OG1  
2074 C  CG2  . THR   B 52  ? 0.6409 0.5354 0.7730 0.0348  -0.1016 0.0098  56  THR   B CG2  
2075 N  N    . VAL   B 53  ? 0.4120 0.3171 0.5968 0.0773  -0.0775 0.0315  57  VAL   B N    
2076 C  CA   . VAL   B 53  ? 0.3665 0.3026 0.5592 0.0595  -0.0748 0.0380  57  VAL   B CA   
2077 C  C    . VAL   B 53  ? 0.3622 0.2953 0.5132 0.0534  -0.0749 0.0388  57  VAL   B C    
2078 O  O    . VAL   B 53  ? 0.3386 0.3152 0.5360 0.0483  -0.0883 0.0265  57  VAL   B O    
2079 C  CB   . VAL   B 53  ? 0.3616 0.3327 0.5729 0.0623  -0.0714 0.0472  57  VAL   B CB   
2080 C  CG1  . VAL   B 53  ? 0.3615 0.3166 0.5748 0.0473  -0.0662 0.0434  57  VAL   B CG1  
2081 C  CG2  . VAL   B 53  ? 0.3552 0.3380 0.6009 0.0582  -0.0567 0.0505  57  VAL   B CG2  
2082 N  N    . PRO   B 54  ? 0.3448 0.3247 0.4955 0.0625  -0.0840 0.0502  58  PRO   B N    
2083 C  CA   . PRO   B 54  ? 0.3510 0.3352 0.4998 0.0495  -0.0667 0.0368  58  PRO   B CA   
2084 C  C    . PRO   B 54  ? 0.3439 0.3373 0.4870 0.0489  -0.0741 0.0207  58  PRO   B C    
2085 O  O    . PRO   B 54  ? 0.3273 0.3265 0.4739 0.0609  -0.0765 0.0423  58  PRO   B O    
2086 C  CB   . PRO   B 54  ? 0.3581 0.3696 0.5005 0.0549  -0.0623 0.0440  58  PRO   B CB   
2087 C  CG   . PRO   B 54  ? 0.3700 0.3629 0.5115 0.0513  -0.0691 0.0376  58  PRO   B CG   
2088 C  CD   . PRO   B 54  ? 0.3545 0.3506 0.5055 0.0586  -0.0728 0.0441  58  PRO   B CD   
2089 N  N    . PRO   B 55  ? 0.3670 0.3304 0.4884 0.0386  -0.0656 -0.0033 59  PRO   B N    
2090 C  CA   . PRO   B 55  ? 0.3505 0.3368 0.4728 0.0347  -0.0569 -0.0160 59  PRO   B CA   
2091 C  C    . PRO   B 55  ? 0.3164 0.3099 0.3985 0.0190  -0.0446 -0.0064 59  PRO   B C    
2092 O  O    . PRO   B 55  ? 0.2978 0.3007 0.3829 0.0110  -0.0541 0.0073  59  PRO   B O    
2093 C  CB   . PRO   B 55  ? 0.3800 0.3461 0.5007 0.0156  -0.0582 -0.0257 59  PRO   B CB   
2094 C  CG   . PRO   B 55  ? 0.3997 0.3606 0.5090 0.0121  -0.0657 -0.0181 59  PRO   B CG   
2095 C  CD   . PRO   B 55  ? 0.3840 0.3484 0.5090 0.0244  -0.0665 -0.0002 59  PRO   B CD   
2096 N  N    . PRO   B 56  ? 0.2945 0.3270 0.3531 0.0137  -0.0172 -0.0135 60  PRO   B N    
2097 C  CA   . PRO   B 56  ? 0.2700 0.3022 0.3151 0.0017  -0.0192 -0.0017 60  PRO   B CA   
2098 C  C    . PRO   B 56  ? 0.2488 0.2471 0.2514 0.0017  -0.0148 0.0030  60  PRO   B C    
2099 O  O    . PRO   B 56  ? 0.2528 0.2346 0.2767 0.0085  -0.0186 0.0019  60  PRO   B O    
2100 C  CB   . PRO   B 56  ? 0.3069 0.3159 0.3366 0.0005  -0.0014 0.0000  60  PRO   B CB   
2101 C  CG   . PRO   B 56  ? 0.3400 0.3587 0.3602 0.0118  0.0008  -0.0080 60  PRO   B CG   
2102 C  CD   . PRO   B 56  ? 0.3320 0.3523 0.3644 0.0166  -0.0050 -0.0140 60  PRO   B CD   
2103 N  N    . PRO   B 57  ? 0.2291 0.2159 0.2062 -0.0067 -0.0166 0.0069  61  PRO   B N    
2104 C  CA   . PRO   B 57  ? 0.2237 0.2086 0.1994 -0.0065 -0.0115 0.0076  61  PRO   B CA   
2105 C  C    . PRO   B 57  ? 0.2270 0.2073 0.1975 -0.0120 -0.0149 0.0107  61  PRO   B C    
2106 O  O    . PRO   B 57  ? 0.2307 0.2227 0.2088 -0.0114 -0.0041 0.0042  61  PRO   B O    
2107 C  CB   . PRO   B 57  ? 0.2304 0.2190 0.2072 0.0028  -0.0067 0.0059  61  PRO   B CB   
2108 C  CG   . PRO   B 57  ? 0.2362 0.2203 0.2191 -0.0005 -0.0048 0.0032  61  PRO   B CG   
2109 C  CD   . PRO   B 57  ? 0.2309 0.2152 0.2082 -0.0029 -0.0090 0.0058  61  PRO   B CD   
2110 N  N    . ARG   B 58  ? 0.2329 0.2030 0.1745 -0.0248 -0.0158 0.0229  62  ARG   B N    
2111 C  CA   . ARG   B 58  ? 0.2378 0.1943 0.1744 -0.0271 -0.0118 0.0124  62  ARG   B CA   
2112 C  C    . ARG   B 58  ? 0.2297 0.1873 0.1740 -0.0286 -0.0069 0.0151  62  ARG   B C    
2113 O  O    . ARG   B 58  ? 0.2349 0.1872 0.1784 -0.0236 -0.0097 0.0165  62  ARG   B O    
2114 C  CB   . ARG   B 58  ? 0.2329 0.1965 0.1895 -0.0335 -0.0035 0.0151  62  ARG   B CB   
2115 C  CG   . ARG   B 58  ? 0.2265 0.1925 0.1974 -0.0439 -0.0036 0.0120  62  ARG   B CG   
2116 C  CD   . ARG   B 58  ? 0.2290 0.1918 0.1981 -0.0398 -0.0013 0.0074  62  ARG   B CD   
2117 N  NE   . ARG   B 58  ? 0.2129 0.2069 0.1966 -0.0409 -0.0004 0.0073  62  ARG   B NE   
2118 C  CZ   . ARG   B 58  ? 0.1930 0.2038 0.1835 -0.0339 -0.0017 0.0039  62  ARG   B CZ   
2119 N  NH1  . ARG   B 58  ? 0.1923 0.2063 0.1783 -0.0370 0.0028  0.0065  62  ARG   B NH1  
2120 N  NH2  . ARG   B 58  ? 0.1857 0.2036 0.1832 -0.0327 -0.0006 0.0015  62  ARG   B NH2  
2121 N  N    . VAL   B 59  ? 0.2480 0.1782 0.1707 -0.0348 -0.0053 0.0151  63  VAL   B N    
2122 C  CA   . VAL   B 59  ? 0.2434 0.1869 0.1660 -0.0345 -0.0019 0.0067  63  VAL   B CA   
2123 C  C    . VAL   B 59  ? 0.2593 0.1915 0.1608 -0.0371 0.0028  -0.0074 63  VAL   B C    
2124 O  O    . VAL   B 59  ? 0.3421 0.2567 0.1626 -0.0850 0.0234  -0.0148 63  VAL   B O    
2125 C  CB   . VAL   B 59  ? 0.2411 0.2156 0.1763 -0.0263 -0.0038 0.0063  63  VAL   B CB   
2126 C  CG1  . VAL   B 59  ? 0.2520 0.2251 0.1727 -0.0166 -0.0047 0.0036  63  VAL   B CG1  
2127 C  CG2  . VAL   B 59  ? 0.2384 0.2230 0.1939 -0.0374 0.0015  0.0092  63  VAL   B CG2  
2128 N  N    . VAL   B 60  ? 0.2149 0.1678 0.1546 -0.0268 -0.0008 -0.0105 64  VAL   B N    
2129 C  CA   . VAL   B 60  ? 0.2169 0.1779 0.1718 -0.0289 -0.0113 -0.0066 64  VAL   B CA   
2130 C  C    . VAL   B 60  ? 0.1977 0.1676 0.1588 -0.0339 -0.0010 -0.0105 64  VAL   B C    
2131 O  O    . VAL   B 60  ? 0.2269 0.1876 0.1699 -0.0468 -0.0041 -0.0147 64  VAL   B O    
2132 C  CB   . VAL   B 60  ? 0.2341 0.2121 0.2207 -0.0355 -0.0243 0.0034  64  VAL   B CB   
2133 C  CG1  . VAL   B 60  ? 0.2515 0.2213 0.2397 -0.0327 -0.0447 0.0115  64  VAL   B CG1  
2134 C  CG2  . VAL   B 60  ? 0.2403 0.2352 0.2453 -0.0205 -0.0212 0.0000  64  VAL   B CG2  
2135 N  N    . ASP   B 61  ? 0.1713 0.1630 0.1294 -0.0327 0.0003  -0.0142 65  ASP   B N    
2136 C  CA   . ASP   B 61  ? 0.1541 0.1712 0.1249 -0.0270 -0.0023 -0.0119 65  ASP   B CA   
2137 C  C    . ASP   B 61  ? 0.1454 0.1694 0.1285 -0.0249 -0.0054 -0.0094 65  ASP   B C    
2138 O  O    . ASP   B 61  ? 0.1356 0.1883 0.1281 -0.0187 -0.0061 -0.0048 65  ASP   B O    
2139 C  CB   . ASP   B 61  ? 0.1570 0.1822 0.1396 -0.0229 0.0020  -0.0117 65  ASP   B CB   
2140 C  CG   . ASP   B 61  ? 0.1625 0.1968 0.1536 -0.0128 -0.0018 -0.0145 65  ASP   B CG   
2141 O  OD1  . ASP   B 61  ? 0.1638 0.2001 0.1596 -0.0027 -0.0075 -0.0218 65  ASP   B OD1  
2142 O  OD2  . ASP   B 61  ? 0.1788 0.2126 0.1877 -0.0056 -0.0019 -0.0283 65  ASP   B OD2  
2143 N  N    . LYS   B 62  ? 0.1314 0.1602 0.1261 -0.0222 -0.0087 -0.0070 66  LYS   B N    
2144 C  CA   . LYS   B 62  ? 0.1375 0.1668 0.1396 -0.0319 -0.0045 -0.0099 66  LYS   B CA   
2145 C  C    . LYS   B 62  ? 0.1313 0.1734 0.1178 -0.0333 -0.0053 -0.0096 66  LYS   B C    
2146 O  O    . LYS   B 62  ? 0.1550 0.1826 0.1150 -0.0529 -0.0067 -0.0125 66  LYS   B O    
2147 C  CB   . LYS   B 62  ? 0.1499 0.1871 0.1940 -0.0236 -0.0052 -0.0171 66  LYS   B CB   
2148 C  CG   . LYS   B 62  ? 0.1661 0.2208 0.2557 -0.0233 0.0086  -0.0109 66  LYS   B CG   
2149 C  CD   . LYS   B 62  ? 0.1999 0.2601 0.3070 0.0028  0.0146  -0.0075 66  LYS   B CD   
2150 C  CE   . LYS   B 62  ? 0.2260 0.2843 0.3167 0.0163  0.0085  -0.0019 66  LYS   B CE   
2151 N  NZ   . LYS   B 62  ? 0.2339 0.2864 0.2982 0.0265  -0.0022 -0.0158 66  LYS   B NZ   
2152 N  N    . LEU   B 63  ? 0.1340 0.1777 0.1087 -0.0402 -0.0020 -0.0031 67  LEU   B N    
2153 C  CA   . LEU   B 63  ? 0.1471 0.1823 0.1079 -0.0434 -0.0031 -0.0046 67  LEU   B CA   
2154 C  C    . LEU   B 63  ? 0.1474 0.1932 0.1096 -0.0508 -0.0078 -0.0067 67  LEU   B C    
2155 O  O    . LEU   B 63  ? 0.1526 0.2489 0.1125 -0.0686 -0.0149 -0.0049 67  LEU   B O    
2156 C  CB   . LEU   B 63  ? 0.1685 0.1923 0.1251 -0.0313 0.0027  -0.0037 67  LEU   B CB   
2157 C  CG   . LEU   B 63  ? 0.1977 0.1910 0.1448 -0.0214 0.0063  -0.0023 67  LEU   B CG   
2158 C  CD1  . LEU   B 63  ? 0.2020 0.1985 0.1518 -0.0142 0.0018  -0.0032 67  LEU   B CD1  
2159 C  CD2  . LEU   B 63  ? 0.2307 0.1980 0.1720 -0.0087 0.0109  -0.0002 67  LEU   B CD2  
2160 N  N    . SER   B 64  ? 0.1487 0.1835 0.1104 -0.0560 -0.0088 -0.0052 68  SER   B N    
2161 C  CA   . SER   B 64  ? 0.1559 0.1948 0.1264 -0.0596 -0.0086 -0.0032 68  SER   B CA   
2162 C  C    . SER   B 64  ? 0.1535 0.1955 0.1118 -0.0597 -0.0100 -0.0055 68  SER   B C    
2163 O  O    . SER   B 64  ? 0.1887 0.2073 0.1168 -0.0837 -0.0133 -0.0171 68  SER   B O    
2164 C  CB   . SER   B 64  ? 0.1843 0.2304 0.1819 -0.0418 -0.0090 0.0078  68  SER   B CB   
2165 O  OG   . SER   B 64  ? 0.2216 0.2977 0.2538 -0.0438 -0.0141 0.0244  68  SER   B OG   
2166 N  N    . LEU   B 65  ? 0.1480 0.1870 0.1057 -0.0557 -0.0063 0.0036  69  LEU   B N    
2167 C  CA   . LEU   B 65  ? 0.1574 0.1881 0.1260 -0.0433 -0.0032 0.0104  69  LEU   B CA   
2168 C  C    . LEU   B 65  ? 0.1501 0.1724 0.1198 -0.0368 -0.0072 0.0121  69  LEU   B C    
2169 O  O    . LEU   B 65  ? 0.1369 0.1966 0.1255 -0.0471 -0.0148 0.0169  69  LEU   B O    
2170 C  CB   . LEU   B 65  ? 0.1701 0.2048 0.1468 -0.0291 -0.0009 0.0122  69  LEU   B CB   
2171 C  CG   . LEU   B 65  ? 0.1681 0.2403 0.1746 -0.0164 -0.0044 0.0057  69  LEU   B CG   
2172 C  CD1  . LEU   B 65  ? 0.1792 0.2547 0.2024 -0.0079 -0.0082 0.0077  69  LEU   B CD1  
2173 C  CD2  . LEU   B 65  ? 0.1629 0.2648 0.1755 -0.0151 -0.0055 0.0014  69  LEU   B CD2  
2174 N  N    . CYS   B 66  ? 0.1515 0.1612 0.1253 -0.0333 -0.0060 0.0130  70  CYS   B N    
2175 C  CA   . CYS   B 66  ? 0.1521 0.1592 0.1294 -0.0278 -0.0032 0.0179  70  CYS   B CA   
2176 C  C    . CYS   B 66  ? 0.1537 0.1617 0.1362 -0.0195 -0.0130 0.0153  70  CYS   B C    
2177 O  O    . CYS   B 66  ? 0.1602 0.1636 0.1500 -0.0267 -0.0256 0.0248  70  CYS   B O    
2178 C  CB   . CYS   B 66  ? 0.1741 0.1703 0.1439 -0.0163 0.0053  0.0207  70  CYS   B CB   
2179 S  SG   . CYS   B 66  ? 0.2046 0.1881 0.1786 -0.0010 0.0196  0.0251  70  CYS   B SG   
2180 N  N    . VAL   B 67  ? 0.1495 0.1458 0.1385 -0.0152 -0.0164 0.0148  71  VAL   B N    
2181 C  CA   . VAL   B 67  ? 0.1611 0.1483 0.1449 -0.0152 -0.0218 0.0112  71  VAL   B CA   
2182 C  C    . VAL   B 67  ? 0.1735 0.1487 0.1542 -0.0210 -0.0208 0.0153  71  VAL   B C    
2183 O  O    . VAL   B 67  ? 0.1782 0.1495 0.1732 -0.0216 -0.0274 0.0264  71  VAL   B O    
2184 C  CB   . VAL   B 67  ? 0.1685 0.1571 0.1525 -0.0132 -0.0212 0.0007  71  VAL   B CB   
2185 C  CG1  . VAL   B 67  ? 0.1783 0.1609 0.1580 -0.0137 -0.0235 -0.0052 71  VAL   B CG1  
2186 C  CG2  . VAL   B 67  ? 0.1638 0.1620 0.1463 -0.0100 -0.0189 0.0009  71  VAL   B CG2  
2187 N  N    . ALA   B 68  ? 0.1883 0.1497 0.1698 -0.0225 -0.0321 0.0216  72  ALA   B N    
2188 C  CA   . ALA   B 68  ? 0.2013 0.1556 0.1626 -0.0299 -0.0250 0.0198  72  ALA   B CA   
2189 C  C    . ALA   B 68  ? 0.1993 0.1531 0.1741 -0.0265 -0.0212 0.0136  72  ALA   B C    
2190 O  O    . ALA   B 68  ? 0.2028 0.1706 0.2052 -0.0173 -0.0337 -0.0010 72  ALA   B O    
2191 C  CB   . ALA   B 68  ? 0.2325 0.1687 0.1670 -0.0359 -0.0268 0.0253  72  ALA   B CB   
2192 N  N    . PRO   B 69  ? 0.1922 0.1393 0.1548 -0.0322 -0.0130 0.0145  73  PRO   B N    
2193 C  CA   . PRO   B 69  ? 0.1932 0.1420 0.1548 -0.0315 -0.0105 0.0113  73  PRO   B CA   
2194 C  C    . PRO   B 69  ? 0.1955 0.1413 0.1464 -0.0311 -0.0103 0.0127  73  PRO   B C    
2195 O  O    . PRO   B 69  ? 0.2138 0.1456 0.1527 -0.0335 -0.0065 0.0100  73  PRO   B O    
2196 C  CB   . PRO   B 69  ? 0.2032 0.1467 0.1480 -0.0299 -0.0129 0.0155  73  PRO   B CB   
2197 C  CG   . PRO   B 69  ? 0.1972 0.1481 0.1549 -0.0277 -0.0158 0.0141  73  PRO   B CG   
2198 C  CD   . PRO   B 69  ? 0.1921 0.1415 0.1561 -0.0291 -0.0147 0.0132  73  PRO   B CD   
2199 N  N    . GLY   B 70  ? 0.2047 0.1449 0.1452 -0.0273 -0.0088 0.0153  74  GLY   B N    
2200 C  CA   . GLY   B 70  ? 0.2038 0.1406 0.1448 -0.0253 -0.0098 0.0175  74  GLY   B CA   
2201 C  C    . GLY   B 70  ? 0.2031 0.1370 0.1376 -0.0225 -0.0110 0.0169  74  GLY   B C    
2202 O  O    . GLY   B 70  ? 0.2137 0.1381 0.1459 -0.0259 -0.0068 0.0201  74  GLY   B O    
2203 N  N    . LYS   B 71  ? 0.1947 0.1393 0.1530 -0.0244 -0.0128 0.0198  75  LYS   B N    
2204 C  CA   . LYS   B 71  ? 0.1929 0.1540 0.1492 -0.0255 -0.0099 0.0143  75  LYS   B CA   
2205 C  C    . LYS   B 71  ? 0.1799 0.1580 0.1421 -0.0228 -0.0111 0.0155  75  LYS   B C    
2206 O  O    . LYS   B 71  ? 0.1862 0.1518 0.1366 -0.0185 -0.0155 0.0209  75  LYS   B O    
2207 C  CB   . LYS   B 71  ? 0.2130 0.1707 0.1635 -0.0237 -0.0168 -0.0070 75  LYS   B CB   
2208 C  CG   . LYS   B 71  ? 0.2407 0.1966 0.1689 -0.0252 -0.0216 0.0028  75  LYS   B CG   
2209 C  CD   . LYS   B 71  ? 0.2971 0.2246 0.1917 -0.0290 -0.0104 0.0022  75  LYS   B CD   
2210 C  CE   . LYS   B 71  ? 0.3283 0.2912 0.2234 -0.0515 -0.0237 0.0023  75  LYS   B CE   
2211 N  NZ   . LYS   B 71  ? 0.3568 0.3620 0.2043 -0.0817 -0.0091 0.0095  75  LYS   B NZ   
2212 N  N    . ALA   B 72  ? 0.1736 0.1602 0.1388 -0.0285 -0.0134 0.0152  76  ALA   B N    
2213 C  CA   . ALA   B 72  ? 0.1755 0.1676 0.1376 -0.0207 -0.0142 0.0168  76  ALA   B CA   
2214 C  C    . ALA   B 72  ? 0.1709 0.1728 0.1381 -0.0163 -0.0142 0.0177  76  ALA   B C    
2215 O  O    . ALA   B 72  ? 0.2013 0.1736 0.1485 -0.0076 -0.0050 0.0083  76  ALA   B O    
2216 C  CB   . ALA   B 72  ? 0.1811 0.1867 0.1555 -0.0188 -0.0099 0.0127  76  ALA   B CB   
2217 N  N    . CYS   B 73  ? 0.1657 0.1689 0.1335 -0.0128 -0.0136 0.0219  77  CYS   B N    
2218 C  CA   . CYS   B 73  ? 0.1631 0.1852 0.1386 -0.0114 -0.0147 0.0279  77  CYS   B CA   
2219 C  C    . CYS   B 73  ? 0.1572 0.1854 0.1528 -0.0123 -0.0119 0.0260  77  CYS   B C    
2220 O  O    . CYS   B 73  ? 0.1659 0.2130 0.1786 -0.0097 0.0022  0.0314  77  CYS   B O    
2221 C  CB   . CYS   B 73  ? 0.1740 0.1893 0.1552 -0.0149 -0.0118 0.0297  77  CYS   B CB   
2222 S  SG   . CYS   B 73  ? 0.1813 0.2082 0.1693 -0.0271 -0.0125 0.0209  77  CYS   B SG   
2223 N  N    . SER   B 74  ? 0.1587 0.1828 0.1522 -0.0069 -0.0204 0.0161  78  SER   B N    
2224 C  CA   . SER   B 74  ? 0.1659 0.1941 0.1655 -0.0008 -0.0255 0.0101  78  SER   B CA   
2225 C  C    . SER   B 74  ? 0.1589 0.2002 0.1760 -0.0007 -0.0329 -0.0007 78  SER   B C    
2226 O  O    . SER   B 74  ? 0.1403 0.1901 0.1961 0.0072  -0.0404 -0.0056 78  SER   B O    
2227 C  CB   . SER   B 74  ? 0.1981 0.2043 0.1652 0.0044  -0.0311 0.0013  78  SER   B CB   
2228 O  OG   . SER   B 74  ? 0.2326 0.2125 0.1538 0.0112  -0.0274 0.0102  78  SER   B OG   
2229 N  N    . PRO   B 75  ? 0.1572 0.2117 0.1953 -0.0013 -0.0353 -0.0054 79  PRO   B N    
2230 C  CA   . PRO   B 75  ? 0.1567 0.2208 0.2007 0.0078  -0.0352 -0.0117 79  PRO   B CA   
2231 C  C    . PRO   B 75  ? 0.1454 0.2124 0.1916 0.0128  -0.0342 -0.0184 79  PRO   B C    
2232 O  O    . PRO   B 75  ? 0.1663 0.2111 0.2143 0.0208  -0.0352 -0.0260 79  PRO   B O    
2233 C  CB   . PRO   B 75  ? 0.1541 0.2273 0.2168 0.0058  -0.0321 -0.0095 79  PRO   B CB   
2234 C  CG   . PRO   B 75  ? 0.1661 0.2363 0.2165 -0.0052 -0.0429 -0.0118 79  PRO   B CG   
2235 C  CD   . PRO   B 75  ? 0.1724 0.2231 0.2082 -0.0043 -0.0454 -0.0125 79  PRO   B CD   
2236 N  N    . ALA   B 76  ? 0.1507 0.2145 0.1865 0.0182  -0.0410 -0.0203 80  ALA   B N    
2237 C  CA   . ALA   B 76  ? 0.1572 0.2193 0.1802 0.0159  -0.0399 -0.0174 80  ALA   B CA   
2238 C  C    . ALA   B 76  ? 0.1548 0.2073 0.1748 0.0155  -0.0317 -0.0109 80  ALA   B C    
2239 O  O    . ALA   B 76  ? 0.1750 0.2064 0.2003 0.0156  -0.0322 -0.0154 80  ALA   B O    
2240 C  CB   . ALA   B 76  ? 0.1608 0.2381 0.1795 0.0192  -0.0456 -0.0164 80  ALA   B CB   
2241 N  N    . ALA   B 77  ? 0.1510 0.2003 0.1661 0.0121  -0.0321 -0.0103 81  ALA   B N    
2242 C  CA   . ALA   B 77  ? 0.1492 0.2016 0.1748 0.0057  -0.0245 0.0013  81  ALA   B CA   
2243 C  C    . ALA   B 77  ? 0.1538 0.1980 0.1766 0.0050  -0.0259 0.0026  81  ALA   B C    
2244 O  O    . ALA   B 77  ? 0.1637 0.2169 0.1742 -0.0168 -0.0190 0.0054  81  ALA   B O    
2245 C  CB   . ALA   B 77  ? 0.1469 0.2038 0.1839 0.0092  -0.0178 -0.0069 81  ALA   B CB   
2246 N  N    . SER   B 78  ? 0.1601 0.1972 0.1843 0.0010  -0.0221 -0.0019 82  SER   B N    
2247 C  CA   . SER   B 78  ? 0.1716 0.2119 0.1785 -0.0085 -0.0243 -0.0050 82  SER   B CA   
2248 C  C    . SER   B 78  ? 0.1767 0.2154 0.1902 -0.0069 -0.0207 -0.0138 82  SER   B C    
2249 O  O    . SER   B 78  ? 0.1861 0.2257 0.1999 -0.0234 -0.0402 -0.0090 82  SER   B O    
2250 C  CB   . SER   B 78  ? 0.1787 0.2233 0.1877 -0.0093 -0.0131 -0.0075 82  SER   B CB   
2251 O  OG   . SER   B 78  ? 0.2025 0.2329 0.1994 -0.0048 -0.0080 -0.0059 82  SER   B OG   
2252 N  N    . GLU   B 79  ? 0.1768 0.2116 0.2194 0.0003  -0.0331 -0.0159 83  GLU   B N    
2253 C  CA   . GLU   B 79  ? 0.2136 0.2269 0.2657 0.0065  -0.0410 -0.0096 83  GLU   B CA   
2254 C  C    . GLU   B 79  ? 0.2374 0.2255 0.2702 0.0073  -0.0476 0.0030  83  GLU   B C    
2255 O  O    . GLU   B 79  ? 0.2883 0.2354 0.3060 -0.0013 -0.0302 -0.0300 83  GLU   B O    
2256 C  CB   . GLU   B 79  ? 0.2367 0.2732 0.3191 0.0146  -0.0625 -0.0079 83  GLU   B CB   
2257 C  CG   . GLU   B 79  ? 0.2810 0.3607 0.3883 0.0018  -0.0547 0.0056  83  GLU   B CG   
2258 C  CD   . GLU   B 79  ? 0.3028 0.4581 0.4639 -0.0089 -0.0766 0.0015  83  GLU   B CD   
2259 O  OE1  . GLU   B 79  ? 0.3998 0.5745 0.5454 -0.0135 -0.1245 0.0240  83  GLU   B OE1  
2260 O  OE2  . GLU   B 79  ? 0.3466 0.5504 0.5884 -0.0241 -0.0241 -0.0042 83  GLU   B OE2  
2261 N  N    . ILE   B 80  ? 0.2121 0.2183 0.2554 0.0075  -0.0460 0.0288  84  ILE   B N    
2262 C  CA   . ILE   B 80  ? 0.2608 0.2491 0.2796 -0.0092 -0.0470 0.0515  84  ILE   B CA   
2263 C  C    . ILE   B 80  ? 0.2509 0.2404 0.3015 -0.0260 -0.0484 0.0833  84  ILE   B C    
2264 O  O    . ILE   B 80  ? 0.3089 0.2539 0.3368 -0.0409 -0.0685 0.1078  84  ILE   B O    
2265 C  CB   . ILE   B 80  ? 0.3130 0.2960 0.2990 -0.0222 -0.0213 0.0469  84  ILE   B CB   
2266 C  CG1  . ILE   B 80  ? 0.3710 0.3546 0.3389 -0.0526 0.0118  0.0477  84  ILE   B CG1  
2267 C  CG2  . ILE   B 80  ? 0.3110 0.3365 0.3165 -0.0101 -0.0343 0.0339  84  ILE   B CG2  
2268 N  N    . THR   B 81  ? 0.2110 0.2415 0.2735 -0.0392 -0.0458 0.0938  85  THR   B N    
2269 C  CA   . THR   B 81  ? 0.2099 0.2383 0.2814 -0.0523 -0.0410 0.0897  85  THR   B CA   
2270 C  C    . THR   B 81  ? 0.2181 0.2151 0.2767 -0.0549 -0.0433 0.0712  85  THR   B C    
2271 O  O    . THR   B 81  ? 0.2341 0.2549 0.3160 -0.0687 -0.0400 0.0680  85  THR   B O    
2272 C  CB   . THR   B 81  ? 0.1852 0.2583 0.2735 -0.0305 -0.0340 0.0861  85  THR   B CB   
2273 O  OG1  . THR   B 81  ? 0.1689 0.2475 0.2718 -0.0291 -0.0432 0.0987  85  THR   B OG1  
2274 C  CG2  . THR   B 81  ? 0.1962 0.2824 0.2810 -0.0234 -0.0300 0.0855  85  THR   B CG2  
2275 N  N    . GLY   B 82  ? 0.2173 0.2066 0.2702 -0.0278 -0.0551 0.0506  86  GLY   B N    
2276 C  CA   . GLY   B 82  ? 0.2319 0.1978 0.2721 -0.0196 -0.0575 0.0294  86  GLY   B CA   
2277 C  C    . GLY   B 82  ? 0.2279 0.2027 0.2334 -0.0137 -0.0497 0.0226  86  GLY   B C    
2278 O  O    . GLY   B 82  ? 0.2349 0.2415 0.2544 0.0114  -0.0505 -0.0023 86  GLY   B O    
2279 N  N    . LEU   B 83  ? 0.2126 0.1854 0.2047 -0.0219 -0.0505 0.0301  87  LEU   B N    
2280 C  CA   . LEU   B 83  ? 0.2003 0.1731 0.1886 -0.0306 -0.0407 0.0274  87  LEU   B CA   
2281 C  C    . LEU   B 83  ? 0.1939 0.1795 0.1732 -0.0307 -0.0378 0.0288  87  LEU   B C    
2282 O  O    . LEU   B 83  ? 0.2164 0.2039 0.1781 -0.0386 -0.0486 0.0378  87  LEU   B O    
2283 C  CB   . LEU   B 83  ? 0.1997 0.1736 0.1868 -0.0343 -0.0384 0.0241  87  LEU   B CB   
2284 C  CG   . LEU   B 83  ? 0.1951 0.1820 0.2083 -0.0334 -0.0338 0.0222  87  LEU   B CG   
2285 C  CD1  . LEU   B 83  ? 0.1925 0.1826 0.2154 -0.0289 -0.0339 0.0254  87  LEU   B CD1  
2286 C  CD2  . LEU   B 83  ? 0.1943 0.1889 0.2231 -0.0327 -0.0402 0.0122  87  LEU   B CD2  
2287 N  N    . SER   B 84  ? 0.1874 0.1822 0.1485 -0.0269 -0.0344 0.0213  88  SER   B N    
2288 C  CA   . SER   B 84  ? 0.1794 0.1781 0.1412 -0.0202 -0.0258 0.0131  88  SER   B CA   
2289 C  C    . SER   B 84  ? 0.1714 0.1617 0.1326 -0.0258 -0.0180 0.0131  88  SER   B C    
2290 O  O    . SER   B 84  ? 0.1776 0.1523 0.1172 -0.0371 -0.0036 0.0085  88  SER   B O    
2291 C  CB   . SER   B 84  ? 0.1818 0.1979 0.1674 -0.0191 -0.0239 0.0041  88  SER   B CB   
2292 O  OG   . SER   B 84  ? 0.1882 0.2419 0.1756 -0.0123 -0.0225 -0.0062 88  SER   B OG   
2293 N  N    . THR   B 85  ? 0.1792 0.1599 0.1364 -0.0198 -0.0231 0.0091  89  THR   B N    
2294 C  CA   . THR   B 85  ? 0.1816 0.1665 0.1390 -0.0171 -0.0170 0.0138  89  THR   B CA   
2295 C  C    . THR   B 85  ? 0.1790 0.1698 0.1374 -0.0238 -0.0169 0.0159  89  THR   B C    
2296 O  O    . THR   B 85  ? 0.1775 0.1742 0.1433 -0.0241 -0.0184 0.0202  89  THR   B O    
2297 C  CB   . THR   B 85  ? 0.1942 0.1634 0.1457 -0.0134 -0.0187 0.0117  89  THR   B CB   
2298 O  OG1  . THR   B 85  ? 0.2165 0.1728 0.1477 -0.0167 -0.0205 0.0175  89  THR   B OG1  
2299 C  CG2  . THR   B 85  ? 0.1993 0.1539 0.1590 -0.0160 -0.0230 0.0084  89  THR   B CG2  
2300 N  N    . ALA   B 86  ? 0.1745 0.1869 0.1246 -0.0244 -0.0167 0.0141  90  ALA   B N    
2301 C  CA   . ALA   B 86  ? 0.1823 0.2101 0.1303 -0.0320 -0.0103 0.0066  90  ALA   B CA   
2302 C  C    . ALA   B 86  ? 0.1761 0.2141 0.1410 -0.0328 -0.0086 0.0050  90  ALA   B C    
2303 O  O    . ALA   B 86  ? 0.1941 0.2305 0.1405 -0.0413 -0.0176 0.0165  90  ALA   B O    
2304 C  CB   . ALA   B 86  ? 0.1847 0.2315 0.1373 -0.0397 -0.0081 0.0043  90  ALA   B CB   
2305 N  N    . VAL   B 87  ? 0.1709 0.2030 0.1427 -0.0251 -0.0023 -0.0016 91  VAL   B N    
2306 C  CA   . VAL   B 87  ? 0.1786 0.2047 0.1664 -0.0203 -0.0047 -0.0090 91  VAL   B CA   
2307 C  C    . VAL   B 87  ? 0.1760 0.1867 0.1492 -0.0250 -0.0060 0.0017  91  VAL   B C    
2308 O  O    . VAL   B 87  ? 0.1765 0.2003 0.1412 -0.0215 -0.0032 -0.0058 91  VAL   B O    
2309 C  CB   . VAL   B 87  ? 0.2067 0.2203 0.2128 -0.0118 -0.0166 -0.0109 91  VAL   B CB   
2310 C  CG1  . VAL   B 87  ? 0.2235 0.2243 0.2598 -0.0059 -0.0333 -0.0125 91  VAL   B CG1  
2311 C  CG2  . VAL   B 87  ? 0.2266 0.2395 0.2305 0.0010  -0.0142 -0.0267 91  VAL   B CG2  
2312 N  N    . LEU   B 88  ? 0.1611 0.1716 0.1287 -0.0258 -0.0138 0.0071  92  LEU   B N    
2313 C  CA   . LEU   B 88  ? 0.1627 0.1788 0.1286 -0.0278 -0.0084 0.0151  92  LEU   B CA   
2314 C  C    . LEU   B 88  ? 0.1673 0.1874 0.1356 -0.0282 -0.0057 0.0253  92  LEU   B C    
2315 O  O    . LEU   B 88  ? 0.1687 0.1984 0.1310 -0.0227 -0.0058 0.0299  92  LEU   B O    
2316 C  CB   . LEU   B 88  ? 0.1554 0.1821 0.1350 -0.0230 -0.0008 0.0172  92  LEU   B CB   
2317 C  CG   . LEU   B 88  ? 0.1621 0.1864 0.1345 -0.0198 -0.0022 0.0168  92  LEU   B CG   
2318 C  CD1  . LEU   B 88  ? 0.1712 0.1886 0.1367 -0.0248 -0.0002 0.0186  92  LEU   B CD1  
2319 C  CD2  . LEU   B 88  ? 0.1680 0.1913 0.1332 -0.0214 -0.0077 0.0224  92  LEU   B CD2  
2320 N  N    . ALA   B 89  ? 0.1830 0.1914 0.1386 -0.0355 -0.0184 0.0325  93  ALA   B N    
2321 C  CA   . ALA   B 89  ? 0.1874 0.2054 0.1388 -0.0387 -0.0155 0.0407  93  ALA   B CA   
2322 C  C    . ALA   B 89  ? 0.1861 0.2227 0.1463 -0.0327 -0.0060 0.0350  93  ALA   B C    
2323 O  O    . ALA   B 89  ? 0.1879 0.2391 0.1373 -0.0338 -0.0073 0.0334  93  ALA   B O    
2324 C  CB   . ALA   B 89  ? 0.2074 0.2111 0.1495 -0.0458 -0.0204 0.0428  93  ALA   B CB   
2325 N  N    . ALA   B 90  ? 0.1701 0.2307 0.1337 -0.0329 0.0057  0.0282  94  ALA   B N    
2326 C  CA   . ALA   B 90  ? 0.1848 0.2606 0.1286 -0.0270 0.0004  0.0238  94  ALA   B CA   
2327 C  C    . ALA   B 90  ? 0.1910 0.2519 0.1183 -0.0261 -0.0020 0.0117  94  ALA   B C    
2328 O  O    . ALA   B 90  ? 0.2238 0.2702 0.1255 -0.0271 -0.0082 0.0025  94  ALA   B O    
2329 C  CB   . ALA   B 90  ? 0.1815 0.2832 0.1352 -0.0219 0.0021  0.0225  94  ALA   B CB   
2330 N  N    . HIS   B 91  ? 0.1849 0.2446 0.1020 -0.0285 -0.0072 0.0040  95  HIS   B N    
2331 C  CA   . HIS   B 91  ? 0.1920 0.2336 0.1143 -0.0314 -0.0089 -0.0042 95  HIS   B CA   
2332 C  C    . HIS   B 91  ? 0.1920 0.2278 0.1170 -0.0285 -0.0085 -0.0069 95  HIS   B C    
2333 O  O    . HIS   B 91  ? 0.1909 0.2420 0.1423 -0.0333 -0.0117 -0.0185 95  HIS   B O    
2334 C  CB   . HIS   B 91  ? 0.2020 0.2266 0.1354 -0.0268 -0.0066 0.0012  95  HIS   B CB   
2335 C  CG   . HIS   B 91  ? 0.2193 0.2340 0.1444 -0.0207 -0.0101 0.0057  95  HIS   B CG   
2336 N  ND1  . HIS   B 91  ? 0.2277 0.2459 0.1802 -0.0110 -0.0127 0.0009  95  HIS   B ND1  
2337 C  CD2  . HIS   B 91  ? 0.2284 0.2340 0.1576 -0.0189 -0.0153 0.0030  95  HIS   B CD2  
2338 C  CE1  . HIS   B 91  ? 0.2480 0.2506 0.2060 -0.0068 -0.0206 0.0006  95  HIS   B CE1  
2339 N  NE2  . HIS   B 91  ? 0.2497 0.2446 0.1863 -0.0059 -0.0194 0.0019  95  HIS   B NE2  
2340 N  N    . GLY   B 92  ? 0.1804 0.2329 0.1225 -0.0211 -0.0067 0.0095  96  GLY   B N    
2341 C  CA   . GLY   B 92  ? 0.1837 0.2318 0.1240 -0.0180 -0.0142 0.0155  96  GLY   B CA   
2342 C  C    . GLY   B 92  ? 0.1759 0.2215 0.1320 -0.0107 -0.0159 0.0112  96  GLY   B C    
2343 O  O    . GLY   B 92  ? 0.1770 0.2491 0.1484 0.0012  -0.0054 0.0195  96  GLY   B O    
2344 N  N    . ARG   B 93  ? 0.1816 0.2123 0.1309 -0.0148 -0.0139 0.0135  97  ARG   B N    
2345 C  CA   . ARG   B 93  ? 0.1823 0.2050 0.1353 -0.0165 -0.0135 0.0129  97  ARG   B CA   
2346 C  C    . ARG   B 93  ? 0.1978 0.2012 0.1416 -0.0232 -0.0219 0.0039  97  ARG   B C    
2347 O  O    . ARG   B 93  ? 0.2206 0.2151 0.1710 -0.0324 -0.0177 0.0029  97  ARG   B O    
2348 C  CB   . ARG   B 93  ? 0.1897 0.2192 0.1257 -0.0193 -0.0149 0.0126  97  ARG   B CB   
2349 C  CG   . ARG   B 93  ? 0.1919 0.2231 0.1329 -0.0225 -0.0156 0.0220  97  ARG   B CG   
2350 C  CD   . ARG   B 93  ? 0.1925 0.2289 0.1413 -0.0217 -0.0198 0.0196  97  ARG   B CD   
2351 N  NE   . ARG   B 93  ? 0.1864 0.2326 0.1432 -0.0267 -0.0222 0.0199  97  ARG   B NE   
2352 C  CZ   . ARG   B 93  ? 0.1941 0.2375 0.1733 -0.0300 -0.0285 0.0150  97  ARG   B CZ   
2353 N  NH1  . ARG   B 93  ? 0.1978 0.2471 0.1911 -0.0318 -0.0274 0.0151  97  ARG   B NH1  
2354 N  NH2  . ARG   B 93  ? 0.1973 0.2587 0.1794 -0.0322 -0.0341 0.0235  97  ARG   B NH2  
2355 N  N    . GLN   B 94  ? 0.2021 0.1943 0.1561 -0.0203 -0.0222 -0.0001 98  GLN   B N    
2356 C  CA   . GLN   B 94  ? 0.2273 0.1959 0.1800 -0.0203 -0.0257 -0.0055 98  GLN   B CA   
2357 C  C    . GLN   B 94  ? 0.2181 0.1800 0.1773 -0.0127 -0.0325 0.0013  98  GLN   B C    
2358 O  O    . GLN   B 94  ? 0.2023 0.1748 0.1564 -0.0158 -0.0241 0.0017  98  GLN   B O    
2359 C  CB   . GLN   B 94  ? 0.2419 0.2310 0.1944 -0.0212 -0.0370 -0.0092 98  GLN   B CB   
2360 C  CG   . GLN   B 94  ? 0.2799 0.2653 0.2097 -0.0254 -0.0432 -0.0075 98  GLN   B CG   
2361 C  CD   . GLN   B 94  ? 0.2973 0.3077 0.2513 -0.0321 -0.0529 0.0014  98  GLN   B CD   
2362 O  OE1  . GLN   B 94  ? 0.3295 0.3389 0.2981 -0.0162 -0.0505 -0.0075 98  GLN   B OE1  
2363 N  NE2  . GLN   B 94  ? 0.3445 0.3438 0.2581 -0.0384 -0.0519 0.0076  98  GLN   B NE2  
2364 N  N    A CYS   B 95  ? 0.2255 0.1780 0.1954 -0.0068 -0.0363 -0.0004 99  CYS   B N    
2365 N  N    B CYS   B 95  ? 0.2276 0.1828 0.1957 -0.0126 -0.0341 -0.0030 99  CYS   B N    
2366 C  CA   A CYS   B 95  ? 0.2337 0.1812 0.2025 -0.0031 -0.0369 -0.0075 99  CYS   B CA   
2367 C  CA   B CYS   B 95  ? 0.2359 0.1885 0.2052 -0.0119 -0.0376 -0.0088 99  CYS   B CA   
2368 C  C    A CYS   B 95  ? 0.2172 0.1664 0.2108 -0.0037 -0.0435 -0.0180 99  CYS   B C    
2369 C  C    B CYS   B 95  ? 0.2242 0.1759 0.2096 -0.0079 -0.0423 -0.0146 99  CYS   B C    
2370 O  O    A CYS   B 95  ? 0.2158 0.1880 0.2106 0.0016  -0.0406 -0.0375 99  CYS   B O    
2371 O  O    B CYS   B 95  ? 0.2241 0.1806 0.2096 -0.0056 -0.0427 -0.0206 99  CYS   B O    
2372 C  CB   A CYS   B 95  ? 0.2542 0.1954 0.2345 -0.0085 -0.0288 0.0026  99  CYS   B CB   
2373 C  CB   B CYS   B 95  ? 0.2536 0.1966 0.2261 -0.0167 -0.0352 -0.0054 99  CYS   B CB   
2374 S  SG   A CYS   B 95  ? 0.2864 0.1949 0.3107 0.0000  -0.0107 0.0357  99  CYS   B SG   
2375 S  SG   B CYS   B 95  ? 0.2927 0.2254 0.2658 -0.0330 -0.0180 0.0063  99  CYS   B SG   
2376 N  N    . PHE   B 96  ? 0.2154 0.1649 0.2112 -0.0031 -0.0465 -0.0182 100 PHE   B N    
2377 C  CA   . PHE   B 96  ? 0.2138 0.1734 0.2334 0.0009  -0.0480 -0.0161 100 PHE   B CA   
2378 C  C    . PHE   B 96  ? 0.2250 0.1697 0.2631 0.0024  -0.0499 -0.0117 100 PHE   B C    
2379 O  O    . PHE   B 96  ? 0.2586 0.1743 0.3501 0.0077  -0.0816 -0.0264 100 PHE   B O    
2380 C  CB   . PHE   B 96  ? 0.1967 0.1813 0.2238 -0.0024 -0.0412 -0.0219 100 PHE   B CB   
2381 C  CG   . PHE   B 96  ? 0.2005 0.2011 0.2203 -0.0028 -0.0340 -0.0183 100 PHE   B CG   
2382 C  CD1  . PHE   B 96  ? 0.2059 0.2211 0.2380 0.0084  -0.0244 0.0026  100 PHE   B CD1  
2383 C  CD2  . PHE   B 96  ? 0.2052 0.2142 0.2151 -0.0047 -0.0282 -0.0146 100 PHE   B CD2  
2384 C  CE1  . PHE   B 96  ? 0.2154 0.2390 0.2451 0.0086  -0.0165 0.0066  100 PHE   B CE1  
2385 C  CE2  . PHE   B 96  ? 0.2105 0.2206 0.2239 -0.0066 -0.0273 -0.0002 100 PHE   B CE2  
2386 C  CZ   . PHE   B 96  ? 0.2170 0.2349 0.2303 -0.0001 -0.0232 0.0041  100 PHE   B CZ   
2387 N  N    . ASP   B 97  ? 0.2165 0.1667 0.2531 0.0020  -0.0439 0.0064  101 ASP   B N    
2388 C  CA   . ASP   B 97  ? 0.2296 0.1798 0.2540 0.0090  -0.0412 0.0209  101 ASP   B CA   
2389 C  C    . ASP   B 97  ? 0.2273 0.1746 0.2604 0.0104  -0.0471 0.0327  101 ASP   B C    
2390 O  O    . ASP   B 97  ? 0.2256 0.1604 0.2541 0.0098  -0.0499 0.0275  101 ASP   B O    
2391 C  CB   . ASP   B 97  ? 0.2518 0.2057 0.2615 -0.0041 -0.0328 0.0351  101 ASP   B CB   
2392 C  CG   . ASP   B 97  ? 0.2911 0.2328 0.2553 -0.0145 -0.0276 0.0292  101 ASP   B CG   
2393 O  OD1  . ASP   B 97  ? 0.2758 0.2273 0.2579 -0.0096 -0.0359 0.0357  101 ASP   B OD1  
2394 O  OD2  . ASP   B 97  ? 0.3728 0.3097 0.2596 -0.0304 -0.0253 0.0290  101 ASP   B OD2  
2395 N  N    . ASP   B 98  ? 0.2342 0.1692 0.2885 0.0150  -0.0477 0.0442  102 ASP   B N    
2396 C  CA   . ASP   B 98  ? 0.2385 0.2020 0.3189 0.0180  -0.0527 0.0392  102 ASP   B CA   
2397 C  C    . ASP   B 98  ? 0.2230 0.1860 0.2968 0.0290  -0.0406 0.0438  102 ASP   B C    
2398 O  O    . ASP   B 98  ? 0.2300 0.1822 0.3228 0.0206  -0.0341 0.0462  102 ASP   B O    
2399 C  CB   . ASP   B 98  ? 0.2676 0.2247 0.3799 0.0336  -0.0761 0.0423  102 ASP   B CB   
2400 C  CG   . ASP   B 98  ? 0.3418 0.2714 0.4435 0.0270  -0.0874 0.0212  102 ASP   B CG   
2401 O  OD1  . ASP   B 98  ? 0.3865 0.3205 0.4990 0.0115  -0.1100 0.0137  102 ASP   B OD1  
2402 O  OD2  . ASP   B 98  ? 0.4286 0.3092 0.5469 0.0554  -0.0924 0.0316  102 ASP   B OD2  
2403 N  N    . ASN   B 99  ? 0.2238 0.1810 0.2733 0.0067  -0.0361 0.0474  103 ASN   B N    
2404 C  CA   . ASN   B 99  ? 0.2173 0.1804 0.2617 -0.0028 -0.0366 0.0455  103 ASN   B CA   
2405 C  C    . ASN   B 99  ? 0.2032 0.1773 0.2401 -0.0095 -0.0326 0.0442  103 ASN   B C    
2406 O  O    . ASN   B 99  ? 0.1824 0.1821 0.2209 -0.0152 -0.0379 0.0417  103 ASN   B O    
2407 C  CB   . ASN   B 99  ? 0.2281 0.1825 0.2558 -0.0171 -0.0377 0.0515  103 ASN   B CB   
2408 C  CG   . ASN   B 99  ? 0.2353 0.1808 0.2728 -0.0097 -0.0366 0.0476  103 ASN   B CG   
2409 O  OD1  . ASN   B 99  ? 0.2438 0.2148 0.3095 -0.0195 -0.0508 0.0340  103 ASN   B OD1  
2410 N  ND2  . ASN   B 99  ? 0.2313 0.1721 0.2652 -0.0110 -0.0390 0.0419  103 ASN   B ND2  
2411 N  N    . LEU   B 100 ? 0.2007 0.1626 0.2306 -0.0020 -0.0337 0.0468  104 LEU   B N    
2412 C  CA   . LEU   B 100 ? 0.1855 0.1523 0.2195 0.0065  -0.0232 0.0318  104 LEU   B CA   
2413 C  C    . LEU   B 100 ? 0.1891 0.1479 0.2274 0.0051  -0.0184 0.0251  104 LEU   B C    
2414 O  O    . LEU   B 100 ? 0.1878 0.1430 0.2051 0.0043  -0.0175 0.0223  104 LEU   B O    
2415 C  CB   . LEU   B 100 ? 0.1767 0.1552 0.2111 0.0050  -0.0203 0.0243  104 LEU   B CB   
2416 C  CG   . LEU   B 100 ? 0.1832 0.1691 0.2081 0.0031  -0.0150 0.0294  104 LEU   B CG   
2417 C  CD1  . LEU   B 100 ? 0.1956 0.1888 0.2163 -0.0024 -0.0168 0.0252  104 LEU   B CD1  
2418 C  CD2  . LEU   B 100 ? 0.1885 0.1901 0.2227 -0.0017 -0.0171 0.0290  104 LEU   B CD2  
2419 N  N    . ALA   B 101 ? 0.1997 0.1438 0.2511 0.0025  -0.0123 0.0210  105 ALA   B N    
2420 C  CA   . ALA   B 101 ? 0.2137 0.1566 0.2497 0.0074  -0.0158 0.0137  105 ALA   B CA   
2421 C  C    . ALA   B 101 ? 0.2134 0.1636 0.2588 -0.0001 -0.0097 0.0148  105 ALA   B C    
2422 O  O    . ALA   B 101 ? 0.2165 0.1614 0.2619 -0.0044 -0.0010 0.0136  105 ALA   B O    
2423 C  CB   . ALA   B 101 ? 0.2259 0.1633 0.2581 0.0133  -0.0158 0.0046  105 ALA   B CB   
2424 N  N    . ASN   B 102 ? 0.2032 0.1653 0.2728 0.0092  -0.0154 0.0217  106 ASN   B N    
2425 C  CA   . ASN   B 102 ? 0.2113 0.2032 0.2762 0.0060  -0.0186 0.0243  106 ASN   B CA   
2426 C  C    . ASN   B 102 ? 0.1804 0.1924 0.2408 0.0080  -0.0152 0.0254  106 ASN   B C    
2427 O  O    . ASN   B 102 ? 0.1953 0.1976 0.2625 0.0067  -0.0049 0.0372  106 ASN   B O    
2428 C  CB   . ASN   B 102 ? 0.2259 0.2254 0.2961 0.0145  -0.0227 0.0389  106 ASN   B CB   
2429 C  CG   . ASN   B 102 ? 0.2913 0.2570 0.3398 0.0328  -0.0230 0.0240  106 ASN   B CG   
2430 O  OD1  . ASN   B 102 ? 0.3551 0.2976 0.3830 0.0607  -0.0366 -0.0064 106 ASN   B OD1  
2431 N  ND2  . ASN   B 102 ? 0.3019 0.2874 0.3750 0.0405  -0.0353 0.0467  106 ASN   B ND2  
2432 N  N    A LEU   B 103 ? 0.1801 0.1788 0.2260 0.0008  -0.0140 0.0228  107 LEU   B N    
2433 N  N    B LEU   B 103 ? 0.1765 0.1827 0.2215 0.0001  -0.0141 0.0203  107 LEU   B N    
2434 C  CA   A LEU   B 103 ? 0.1719 0.1726 0.2087 -0.0076 -0.0170 0.0159  107 LEU   B CA   
2435 C  CA   B LEU   B 103 ? 0.1639 0.1780 0.2010 -0.0073 -0.0155 0.0111  107 LEU   B CA   
2436 C  C    A LEU   B 103 ? 0.1668 0.1679 0.2004 -0.0096 -0.0160 0.0070  107 LEU   B C    
2437 C  C    B LEU   B 103 ? 0.1639 0.1714 0.1974 -0.0091 -0.0146 0.0052  107 LEU   B C    
2438 O  O    A LEU   B 103 ? 0.1619 0.1656 0.1913 -0.0073 -0.0143 0.0060  107 LEU   B O    
2439 O  O    B LEU   B 103 ? 0.1609 0.1699 0.1907 -0.0076 -0.0123 0.0044  107 LEU   B O    
2440 C  CB   A LEU   B 103 ? 0.1794 0.1743 0.2008 -0.0086 -0.0167 0.0186  107 LEU   B CB   
2441 C  CB   B LEU   B 103 ? 0.1664 0.1822 0.1873 -0.0084 -0.0159 0.0106  107 LEU   B CB   
2442 C  CG   A LEU   B 103 ? 0.1810 0.1741 0.1997 -0.0118 -0.0160 0.0160  107 LEU   B CG   
2443 C  CG   B LEU   B 103 ? 0.1603 0.1884 0.1769 -0.0114 -0.0174 0.0035  107 LEU   B CG   
2444 C  CD1  A LEU   B 103 ? 0.1852 0.1752 0.2025 -0.0133 -0.0151 0.0172  107 LEU   B CD1  
2445 C  CD1  B LEU   B 103 ? 0.1647 0.1934 0.1701 -0.0169 -0.0201 0.0055  107 LEU   B CD1  
2446 C  CD2  A LEU   B 103 ? 0.1851 0.1770 0.1988 -0.0131 -0.0174 0.0167  107 LEU   B CD2  
2447 C  CD2  B LEU   B 103 ? 0.1577 0.1881 0.1766 -0.0083 -0.0124 0.0039  107 LEU   B CD2  
2448 N  N    . LEU   B 104 ? 0.1587 0.1613 0.2000 -0.0112 -0.0125 0.0027  108 LEU   B N    
2449 C  CA   . LEU   B 104 ? 0.1731 0.1664 0.2025 -0.0111 -0.0166 0.0016  108 LEU   B CA   
2450 C  C    . LEU   B 104 ? 0.1806 0.1756 0.1993 -0.0044 -0.0146 -0.0043 108 LEU   B C    
2451 O  O    . LEU   B 104 ? 0.1832 0.1789 0.1709 -0.0072 -0.0133 -0.0078 108 LEU   B O    
2452 C  CB   . LEU   B 104 ? 0.1897 0.1780 0.2150 -0.0108 -0.0205 -0.0033 108 LEU   B CB   
2453 C  CG   . LEU   B 104 ? 0.2045 0.1991 0.2374 -0.0108 -0.0137 0.0067  108 LEU   B CG   
2454 C  CD1  . LEU   B 104 ? 0.2043 0.2025 0.2553 -0.0118 -0.0229 0.0171  108 LEU   B CD1  
2455 C  CD2  . LEU   B 104 ? 0.1985 0.2001 0.2563 -0.0120 -0.0143 -0.0010 108 LEU   B CD2  
2456 N  N    . LEU   B 105 ? 0.1958 0.1752 0.2118 -0.0048 -0.0115 -0.0039 109 LEU   B N    
2457 C  CA   . LEU   B 105 ? 0.1974 0.1987 0.2291 0.0030  -0.0112 -0.0096 109 LEU   B CA   
2458 C  C    . LEU   B 105 ? 0.1797 0.1810 0.2084 0.0144  -0.0067 -0.0126 109 LEU   B C    
2459 O  O    . LEU   B 105 ? 0.1838 0.1921 0.2012 0.0016  -0.0057 -0.0194 109 LEU   B O    
2460 C  CB   . LEU   B 105 ? 0.2357 0.2217 0.2850 0.0188  -0.0008 -0.0210 109 LEU   B CB   
2461 C  CG   . LEU   B 105 ? 0.3138 0.2901 0.3604 0.0102  -0.0218 -0.0339 109 LEU   B CG   
2462 C  CD1  . LEU   B 105 ? 0.3442 0.3085 0.4008 0.0225  -0.0254 -0.0288 109 LEU   B CD1  
2463 C  CD2  . LEU   B 105 ? 0.3857 0.3318 0.3771 0.0156  -0.0154 -0.0301 109 LEU   B CD2  
2464 N  N    . ALA   B 106 ? 0.1679 0.1791 0.2029 0.0114  -0.0030 -0.0107 110 ALA   B N    
2465 C  CA   . ALA   B 106 ? 0.1755 0.1781 0.1966 0.0133  -0.0041 -0.0133 110 ALA   B CA   
2466 C  C    . ALA   B 106 ? 0.1651 0.1736 0.1783 0.0083  -0.0011 -0.0117 110 ALA   B C    
2467 O  O    . ALA   B 106 ? 0.1688 0.1696 0.1851 0.0093  0.0027  -0.0127 110 ALA   B O    
2468 C  CB   . ALA   B 106 ? 0.1884 0.1898 0.2018 0.0166  -0.0018 -0.0110 110 ALA   B CB   
2469 N  N    . PHE   B 107 ? 0.1561 0.1580 0.1704 0.0049  -0.0013 -0.0029 111 PHE   B N    
2470 C  CA   . PHE   B 107 ? 0.1543 0.1588 0.1601 0.0039  -0.0012 -0.0039 111 PHE   B CA   
2471 C  C    . PHE   B 107 ? 0.1526 0.1550 0.1530 0.0001  -0.0044 -0.0064 111 PHE   B C    
2472 O  O    . PHE   B 107 ? 0.1637 0.1560 0.1483 -0.0043 -0.0019 -0.0058 111 PHE   B O    
2473 C  CB   . PHE   B 107 ? 0.1470 0.1505 0.1579 0.0025  -0.0007 -0.0003 111 PHE   B CB   
2474 C  CG   . PHE   B 107 ? 0.1343 0.1493 0.1687 0.0046  -0.0019 0.0000  111 PHE   B CG   
2475 C  CD1  . PHE   B 107 ? 0.1338 0.1517 0.1766 0.0022  -0.0033 0.0019  111 PHE   B CD1  
2476 C  CD2  . PHE   B 107 ? 0.1465 0.1464 0.1760 0.0033  -0.0043 0.0001  111 PHE   B CD2  
2477 C  CE1  . PHE   B 107 ? 0.1395 0.1535 0.1924 0.0053  0.0042  -0.0017 111 PHE   B CE1  
2478 C  CE2  . PHE   B 107 ? 0.1419 0.1522 0.1841 0.0034  -0.0074 0.0009  111 PHE   B CE2  
2479 C  CZ   . PHE   B 107 ? 0.1386 0.1477 0.1898 0.0066  0.0006  0.0016  111 PHE   B CZ   
2480 N  N    . LEU   B 108 ? 0.1616 0.1595 0.1617 -0.0072 -0.0121 -0.0089 112 LEU   B N    
2481 C  CA   . LEU   B 108 ? 0.1707 0.1772 0.1667 -0.0064 -0.0110 -0.0188 112 LEU   B CA   
2482 C  C    . LEU   B 108 ? 0.1661 0.1817 0.1618 -0.0082 -0.0074 -0.0252 112 LEU   B C    
2483 O  O    . LEU   B 108 ? 0.1645 0.2018 0.1481 -0.0081 -0.0085 -0.0195 112 LEU   B O    
2484 C  CB   . LEU   B 108 ? 0.1969 0.1894 0.1836 -0.0094 -0.0219 -0.0241 112 LEU   B CB   
2485 C  CG   . LEU   B 108 ? 0.2079 0.2051 0.2058 -0.0095 -0.0273 -0.0239 112 LEU   B CG   
2486 C  CD1  . LEU   B 108 ? 0.2379 0.2184 0.2381 -0.0098 -0.0351 -0.0327 112 LEU   B CD1  
2487 C  CD2  . LEU   B 108 ? 0.2214 0.2138 0.2050 -0.0084 -0.0260 -0.0246 112 LEU   B CD2  
2488 N  N    . ARG   B 109 ? 0.1601 0.1853 0.1672 -0.0018 0.0021  -0.0160 113 ARG   B N    
2489 C  CA   . ARG   B 109 ? 0.1630 0.2017 0.1931 0.0007  0.0023  -0.0289 113 ARG   B CA   
2490 C  C    . ARG   B 109 ? 0.1510 0.2051 0.1827 -0.0017 -0.0054 -0.0204 113 ARG   B C    
2491 O  O    . ARG   B 109 ? 0.1436 0.2206 0.2342 -0.0024 -0.0066 -0.0339 113 ARG   B O    
2492 C  CB   . ARG   B 109 ? 0.1952 0.2135 0.2398 0.0077  0.0013  -0.0277 113 ARG   B CB   
2493 C  CG   . ARG   B 109 ? 0.2347 0.2349 0.2921 0.0081  -0.0007 -0.0470 113 ARG   B CG   
2494 C  CD   . ARG   B 109 ? 0.2919 0.2635 0.3447 0.0204  -0.0055 -0.0286 113 ARG   B CD   
2495 N  NE   . ARG   B 109 ? 0.3565 0.3020 0.3791 0.0134  -0.0013 -0.0406 113 ARG   B NE   
2496 C  CZ   . ARG   B 109 ? 0.3804 0.3326 0.4245 -0.0040 -0.0060 -0.0329 113 ARG   B CZ   
2497 N  NH1  . ARG   B 109 ? 0.3737 0.3534 0.4277 0.0318  0.0167  -0.0398 113 ARG   B NH1  
2498 N  NH2  . ARG   B 109 ? 0.4288 0.3516 0.4408 -0.0158 -0.0181 -0.0491 113 ARG   B NH2  
2499 N  N    . ARG   B 110 ? 0.1487 0.2071 0.1531 -0.0083 -0.0101 -0.0210 114 ARG   B N    
2500 C  CA   . ARG   B 110 ? 0.1616 0.2018 0.1546 -0.0144 -0.0079 -0.0174 114 ARG   B CA   
2501 C  C    . ARG   B 110 ? 0.1619 0.1964 0.1469 -0.0167 -0.0056 -0.0213 114 ARG   B C    
2502 O  O    . ARG   B 110 ? 0.1777 0.2098 0.1652 -0.0275 -0.0085 -0.0175 114 ARG   B O    
2503 C  CB   . ARG   B 110 ? 0.1896 0.1959 0.1450 -0.0180 -0.0090 -0.0213 114 ARG   B CB   
2504 C  CG   . ARG   B 110 ? 0.2151 0.1959 0.1621 -0.0176 -0.0066 -0.0077 114 ARG   B CG   
2505 C  CD   . ARG   B 110 ? 0.2056 0.1991 0.1582 -0.0211 -0.0047 -0.0052 114 ARG   B CD   
2506 N  NE   . ARG   B 110 ? 0.1858 0.1945 0.1396 -0.0241 -0.0079 -0.0054 114 ARG   B NE   
2507 C  CZ   . ARG   B 110 ? 0.1827 0.1865 0.1313 -0.0208 -0.0088 -0.0113 114 ARG   B CZ   
2508 N  NH1  . ARG   B 110 ? 0.1772 0.1828 0.1259 -0.0225 -0.0224 -0.0177 114 ARG   B NH1  
2509 N  NH2  . ARG   B 110 ? 0.1668 0.1804 0.1354 -0.0268 -0.0065 -0.0128 114 ARG   B NH2  
2510 N  N    . GLN   B 111 ? 0.1581 0.2006 0.1381 -0.0154 -0.0021 -0.0176 115 GLN   B N    
2511 C  CA   . GLN   B 111 ? 0.1690 0.2022 0.1412 -0.0091 0.0043  -0.0129 115 GLN   B CA   
2512 C  C    . GLN   B 111 ? 0.1769 0.2180 0.1441 -0.0034 0.0073  -0.0136 115 GLN   B C    
2513 O  O    . GLN   B 111 ? 0.1826 0.2202 0.1612 0.0017  0.0125  -0.0175 115 GLN   B O    
2514 C  CB   . GLN   B 111 ? 0.1719 0.2016 0.1419 -0.0049 -0.0018 -0.0121 115 GLN   B CB   
2515 C  CG   . GLN   B 111 ? 0.1643 0.1906 0.1469 -0.0074 -0.0034 -0.0093 115 GLN   B CG   
2516 C  CD   . GLN   B 111 ? 0.1551 0.1839 0.1434 -0.0081 -0.0040 -0.0064 115 GLN   B CD   
2517 O  OE1  . GLN   B 111 ? 0.1668 0.1814 0.1700 -0.0097 -0.0051 -0.0073 115 GLN   B OE1  
2518 N  NE2  . GLN   B 111 ? 0.1472 0.1821 0.1441 -0.0095 -0.0066 -0.0080 115 GLN   B NE2  
2519 N  N    . PRO   B 112 ? 0.1870 0.2330 0.1509 -0.0053 0.0134  -0.0098 116 PRO   B N    
2520 C  CA   . PRO   B 112 ? 0.2039 0.2468 0.1533 -0.0051 0.0210  -0.0075 116 PRO   B CA   
2521 C  C    . PRO   B 112 ? 0.1961 0.2474 0.1561 -0.0031 0.0233  -0.0091 116 PRO   B C    
2522 O  O    . PRO   B 112 ? 0.1923 0.2411 0.1580 0.0045  0.0212  -0.0101 116 PRO   B O    
2523 C  CB   . PRO   B 112 ? 0.2242 0.2652 0.1619 -0.0245 0.0298  0.0026  116 PRO   B CB   
2524 C  CG   . PRO   B 112 ? 0.2299 0.2611 0.2016 -0.0124 0.0291  0.0029  116 PRO   B CG   
2525 C  CD   . PRO   B 112 ? 0.2081 0.2409 0.1611 -0.0107 0.0159  -0.0017 116 PRO   B CD   
2526 N  N    . GLN   B 113 ? 0.2040 0.2617 0.1772 0.0125  0.0286  -0.0076 117 GLN   B N    
2527 C  CA   . GLN   B 113 ? 0.2082 0.2653 0.1777 0.0002  0.0301  -0.0075 117 GLN   B CA   
2528 C  C    . GLN   B 113 ? 0.1837 0.2557 0.1686 -0.0069 0.0313  -0.0145 117 GLN   B C    
2529 O  O    . GLN   B 113 ? 0.1737 0.2800 0.1736 -0.0009 0.0332  -0.0247 117 GLN   B O    
2530 C  CB   . GLN   B 113 ? 0.2513 0.2848 0.2169 0.0177  0.0227  0.0037  117 GLN   B CB   
2531 C  CG   . GLN   B 113 ? 0.2925 0.3051 0.2600 0.0209  0.0252  0.0206  117 GLN   B CG   
2532 C  CD   . GLN   B 113 ? 0.3322 0.3276 0.3418 0.0245  -0.0073 0.0227  117 GLN   B CD   
2533 O  OE1  . GLN   B 113 ? 0.3511 0.3519 0.3812 0.0248  -0.0237 0.0050  117 GLN   B OE1  
2534 N  NE2  . GLN   B 113 ? 0.3477 0.3589 0.4100 0.0381  -0.0462 0.0320  117 GLN   B NE2  
2535 N  N    . PRO   B 114 ? 0.1664 0.2539 0.1887 -0.0161 0.0287  -0.0211 118 PRO   B N    
2536 C  CA   . PRO   B 114 ? 0.1745 0.2454 0.1922 -0.0145 0.0281  -0.0201 118 PRO   B CA   
2537 C  C    . PRO   B 114 ? 0.1830 0.2320 0.1772 -0.0099 0.0220  -0.0167 118 PRO   B C    
2538 O  O    . PRO   B 114 ? 0.1980 0.2205 0.1669 -0.0228 0.0228  -0.0124 118 PRO   B O    
2539 C  CB   . PRO   B 114 ? 0.1927 0.2679 0.2081 -0.0167 0.0183  -0.0348 118 PRO   B CB   
2540 C  CG   . PRO   B 114 ? 0.2153 0.2738 0.2133 -0.0183 0.0218  -0.0179 118 PRO   B CG   
2541 C  CD   . PRO   B 114 ? 0.1897 0.2618 0.1806 -0.0191 0.0254  -0.0175 118 PRO   B CD   
2542 N  N    . TRP   B 115 ? 0.1624 0.2317 0.1741 -0.0075 0.0179  -0.0170 119 TRP   B N    
2543 C  CA   . TRP   B 115 ? 0.1716 0.2375 0.1711 -0.0075 0.0194  -0.0185 119 TRP   B CA   
2544 C  C    . TRP   B 115 ? 0.1558 0.2155 0.1686 -0.0099 0.0202  -0.0142 119 TRP   B C    
2545 O  O    . TRP   B 115 ? 0.1621 0.2174 0.1629 0.0031  0.0111  -0.0178 119 TRP   B O    
2546 C  CB   . TRP   B 115 ? 0.1951 0.2399 0.1881 -0.0067 0.0230  -0.0117 119 TRP   B CB   
2547 C  CG   . TRP   B 115 ? 0.2029 0.2356 0.1718 -0.0116 0.0193  -0.0269 119 TRP   B CG   
2548 C  CD1  . TRP   B 115 ? 0.2074 0.2415 0.1740 -0.0013 0.0113  -0.0328 119 TRP   B CD1  
2549 C  CD2  . TRP   B 115 ? 0.2359 0.2374 0.1857 -0.0094 0.0030  -0.0253 119 TRP   B CD2  
2550 N  NE1  . TRP   B 115 ? 0.2208 0.2404 0.1769 0.0036  0.0100  -0.0291 119 TRP   B NE1  
2551 C  CE2  . TRP   B 115 ? 0.2440 0.2474 0.1745 -0.0076 0.0082  -0.0309 119 TRP   B CE2  
2552 C  CE3  . TRP   B 115 ? 0.2793 0.2532 0.2067 -0.0296 -0.0155 -0.0182 119 TRP   B CE3  
2553 C  CZ2  . TRP   B 115 ? 0.2705 0.2515 0.1874 -0.0136 -0.0074 -0.0238 119 TRP   B CZ2  
2554 C  CZ3  . TRP   B 115 ? 0.2915 0.2496 0.2235 -0.0310 -0.0228 -0.0177 119 TRP   B CZ3  
2555 C  CH2  . TRP   B 115 ? 0.2833 0.2574 0.2035 -0.0228 -0.0118 -0.0101 119 TRP   B CH2  
2556 N  N    . CYS   B 116 ? 0.1479 0.2003 0.1575 -0.0155 0.0064  -0.0186 120 CYS   B N    
2557 C  CA   . CYS   B 116 ? 0.1483 0.1999 0.1500 -0.0189 0.0084  -0.0182 120 CYS   B CA   
2558 C  C    . CYS   B 116 ? 0.1511 0.1964 0.1427 -0.0234 0.0095  -0.0157 120 CYS   B C    
2559 O  O    . CYS   B 116 ? 0.1546 0.1979 0.1482 -0.0221 0.0088  -0.0225 120 CYS   B O    
2560 C  CB   . CYS   B 116 ? 0.1674 0.2211 0.1569 -0.0193 0.0142  -0.0139 120 CYS   B CB   
2561 S  SG   . CYS   B 116 ? 0.1816 0.2512 0.1509 -0.0233 0.0082  -0.0078 120 CYS   B SG   
2562 N  N    . LEU   B 117 ? 0.1496 0.1943 0.1521 -0.0229 0.0088  -0.0144 121 LEU   B N    
2563 C  CA   . LEU   B 117 ? 0.1588 0.2039 0.1547 -0.0294 0.0099  -0.0055 121 LEU   B CA   
2564 C  C    . LEU   B 117 ? 0.1596 0.2099 0.1400 -0.0260 0.0026  -0.0098 121 LEU   B C    
2565 O  O    . LEU   B 117 ? 0.1830 0.2419 0.1428 -0.0104 -0.0136 -0.0237 121 LEU   B O    
2566 C  CB   . LEU   B 117 ? 0.1736 0.2095 0.1636 -0.0395 0.0121  0.0007  121 LEU   B CB   
2567 C  CG   . LEU   B 117 ? 0.2023 0.2220 0.1966 -0.0314 0.0112  0.0171  121 LEU   B CG   
2568 C  CD1  . LEU   B 117 ? 0.2378 0.2289 0.2022 -0.0344 0.0080  0.0108  121 LEU   B CD1  
2569 C  CD2  . LEU   B 117 ? 0.2347 0.2365 0.2219 -0.0302 -0.0074 0.0113  121 LEU   B CD2  
2570 N  N    . VAL   B 118 ? 0.1449 0.1932 0.1257 -0.0332 -0.0031 -0.0030 122 VAL   B N    
2571 C  CA   . VAL   B 118 ? 0.1451 0.1992 0.1241 -0.0339 -0.0029 0.0020  122 VAL   B CA   
2572 C  C    . VAL   B 118 ? 0.1398 0.1929 0.1140 -0.0362 -0.0086 0.0084  122 VAL   B C    
2573 O  O    . VAL   B 118 ? 0.1405 0.2018 0.1139 -0.0266 -0.0120 0.0062  122 VAL   B O    
2574 C  CB   . VAL   B 118 ? 0.1473 0.2051 0.1410 -0.0348 -0.0024 0.0136  122 VAL   B CB   
2575 C  CG1  . VAL   B 118 ? 0.1598 0.2086 0.1475 -0.0333 -0.0045 0.0208  122 VAL   B CG1  
2576 C  CG2  . VAL   B 118 ? 0.1548 0.2064 0.1579 -0.0345 0.0013  0.0170  122 VAL   B CG2  
2577 N  N    . ALA   B 119 ? 0.1437 0.2011 0.1159 -0.0407 -0.0113 0.0107  123 ALA   B N    
2578 C  CA   . ALA   B 119 ? 0.1417 0.2052 0.1205 -0.0379 -0.0154 0.0113  123 ALA   B CA   
2579 C  C    . ALA   B 119 ? 0.1484 0.2097 0.1146 -0.0372 -0.0185 0.0159  123 ALA   B C    
2580 O  O    . ALA   B 119 ? 0.1559 0.2135 0.1098 -0.0388 -0.0034 0.0165  123 ALA   B O    
2581 C  CB   . ALA   B 119 ? 0.1446 0.2032 0.1332 -0.0419 -0.0124 0.0078  123 ALA   B CB   
2582 N  N    . HIS   B 120 ? 0.1528 0.2153 0.1173 -0.0377 -0.0184 0.0210  124 HIS   B N    
2583 C  CA   . HIS   B 120 ? 0.1544 0.2270 0.1348 -0.0359 -0.0248 0.0286  124 HIS   B CA   
2584 C  C    . HIS   B 120 ? 0.1559 0.2306 0.1358 -0.0380 -0.0215 0.0224  124 HIS   B C    
2585 O  O    . HIS   B 120 ? 0.1557 0.2514 0.1392 -0.0337 -0.0156 0.0306  124 HIS   B O    
2586 C  CB   . HIS   B 120 ? 0.1811 0.2380 0.1633 -0.0336 -0.0244 0.0259  124 HIS   B CB   
2587 C  CG   . HIS   B 120 ? 0.2120 0.2633 0.1900 -0.0200 -0.0333 0.0297  124 HIS   B CG   
2588 N  ND1  . HIS   B 120 ? 0.2330 0.2785 0.2191 -0.0199 -0.0290 0.0394  124 HIS   B ND1  
2589 C  CD2  . HIS   B 120 ? 0.2274 0.2869 0.2195 -0.0221 -0.0315 0.0293  124 HIS   B CD2  
2590 C  CE1  . HIS   B 120 ? 0.2392 0.2994 0.2373 -0.0161 -0.0309 0.0465  124 HIS   B CE1  
2591 N  NE2  . HIS   B 120 ? 0.2391 0.2924 0.2434 -0.0253 -0.0306 0.0454  124 HIS   B NE2  
2592 N  N    . ASN   B 121 ? 0.1553 0.2370 0.1246 -0.0426 -0.0266 0.0271  125 ASN   B N    
2593 C  CA   . ASN   B 121 ? 0.1563 0.2410 0.1416 -0.0414 -0.0213 0.0201  125 ASN   B CA   
2594 C  C    . ASN   B 121 ? 0.1525 0.2330 0.1371 -0.0429 -0.0147 0.0167  125 ASN   B C    
2595 O  O    . ASN   B 121 ? 0.1595 0.2377 0.1380 -0.0385 -0.0093 0.0168  125 ASN   B O    
2596 C  CB   . ASN   B 121 ? 0.1663 0.2702 0.1534 -0.0383 -0.0122 0.0162  125 ASN   B CB   
2597 C  CG   . ASN   B 121 ? 0.1896 0.3224 0.1885 -0.0387 -0.0271 -0.0006 125 ASN   B CG   
2598 O  OD1  . ASN   B 121 ? 0.2080 0.3653 0.2124 -0.0534 -0.0361 -0.0367 125 ASN   B OD1  
2599 N  ND2  . ASN   B 121 ? 0.2128 0.3543 0.2015 -0.0200 -0.0380 0.0105  125 ASN   B ND2  
2600 N  N    . GLY   B 122 ? 0.1525 0.2148 0.1351 -0.0460 -0.0116 0.0141  126 GLY   B N    
2601 C  CA   . GLY   B 122 ? 0.1501 0.2200 0.1324 -0.0433 -0.0178 0.0050  126 GLY   B CA   
2602 C  C    . GLY   B 122 ? 0.1636 0.2190 0.1245 -0.0404 -0.0116 0.0016  126 GLY   B C    
2603 O  O    . GLY   B 122 ? 0.1679 0.2059 0.1234 -0.0310 -0.0111 -0.0036 126 GLY   B O    
2604 N  N    . ASP   B 123 ? 0.1804 0.2295 0.1264 -0.0485 -0.0114 0.0021  127 ASP   B N    
2605 C  CA   . ASP   B 123 ? 0.2077 0.2543 0.1340 -0.0481 -0.0028 -0.0139 127 ASP   B CA   
2606 C  C    . ASP   B 123 ? 0.2271 0.2382 0.1350 -0.0604 -0.0119 -0.0109 127 ASP   B C    
2607 O  O    . ASP   B 123 ? 0.2421 0.2347 0.1827 -0.0578 -0.0080 -0.0204 127 ASP   B O    
2608 C  CB   . ASP   B 123 ? 0.2297 0.2793 0.1324 -0.0507 0.0043  -0.0170 127 ASP   B CB   
2609 C  CG   . ASP   B 123 ? 0.2560 0.3273 0.1679 -0.0567 0.0172  -0.0092 127 ASP   B CG   
2610 O  OD1  . ASP   B 123 ? 0.2715 0.3500 0.1875 -0.0719 0.0127  -0.0157 127 ASP   B OD1  
2611 O  OD2  . ASP   B 123 ? 0.3225 0.3873 0.1799 -0.0496 0.0219  0.0017  127 ASP   B OD2  
2612 N  N    . ARG   B 124 ? 0.2227 0.2463 0.1298 -0.0730 -0.0175 -0.0062 128 ARG   B N    
2613 C  CA   . ARG   B 124 ? 0.2188 0.2682 0.1521 -0.0751 -0.0197 0.0046  128 ARG   B CA   
2614 C  C    . ARG   B 124 ? 0.2085 0.2392 0.1504 -0.0666 -0.0136 0.0082  128 ARG   B C    
2615 O  O    . ARG   B 124 ? 0.2337 0.2410 0.1643 -0.0770 -0.0035 -0.0027 128 ARG   B O    
2616 C  CB   . ARG   B 124 ? 0.2432 0.3109 0.1655 -0.0748 -0.0320 0.0218  128 ARG   B CB   
2617 C  CG   . ARG   B 124 ? 0.2694 0.3522 0.1989 -0.0953 -0.0310 0.0308  128 ARG   B CG   
2618 C  CD   . ARG   B 124 ? 0.2751 0.3891 0.2314 -0.0997 -0.0267 0.0337  128 ARG   B CD   
2619 N  NE   . ARG   B 124 ? 0.2976 0.4350 0.2484 -0.1190 -0.0452 0.0366  128 ARG   B NE   
2620 C  CZ   . ARG   B 124 ? 0.3254 0.4325 0.2838 -0.1315 -0.0433 0.0320  128 ARG   B CZ   
2621 N  NH1  . ARG   B 124 ? 0.3596 0.4506 0.3065 -0.1575 -0.0389 0.0589  128 ARG   B NH1  
2622 N  NH2  . ARG   B 124 ? 0.3129 0.4556 0.3110 -0.1450 -0.0344 0.0198  128 ARG   B NH2  
2623 N  N    . TYR   B 125 ? 0.1576 0.2156 0.1412 -0.0645 -0.0106 0.0202  129 TYR   B N    
2624 C  CA   . TYR   B 125 ? 0.1496 0.2036 0.1404 -0.0451 -0.0100 0.0194  129 TYR   B CA   
2625 C  C    . TYR   B 125 ? 0.1544 0.1841 0.1332 -0.0385 -0.0076 0.0075  129 TYR   B C    
2626 O  O    . TYR   B 125 ? 0.1666 0.1781 0.1407 -0.0254 -0.0106 -0.0044 129 TYR   B O    
2627 C  CB   . TYR   B 125 ? 0.1472 0.2197 0.1507 -0.0372 -0.0127 0.0292  129 TYR   B CB   
2628 C  CG   . TYR   B 125 ? 0.1433 0.2364 0.1696 -0.0400 -0.0134 0.0477  129 TYR   B CG   
2629 C  CD1  . TYR   B 125 ? 0.1481 0.2453 0.1874 -0.0424 -0.0306 0.0612  129 TYR   B CD1  
2630 C  CD2  . TYR   B 125 ? 0.1590 0.2591 0.1906 -0.0373 -0.0161 0.0631  129 TYR   B CD2  
2631 C  CE1  . TYR   B 125 ? 0.1429 0.2772 0.2213 -0.0482 -0.0316 0.0599  129 TYR   B CE1  
2632 C  CE2  . TYR   B 125 ? 0.1579 0.2797 0.2246 -0.0425 -0.0228 0.0668  129 TYR   B CE2  
2633 C  CZ   . TYR   B 125 ? 0.1466 0.2823 0.2386 -0.0443 -0.0372 0.0708  129 TYR   B CZ   
2634 O  OH   . TYR   B 125 ? 0.1709 0.3604 0.2837 -0.0200 -0.0512 0.0807  129 TYR   B OH   
2635 N  N    . ASP   B 126 ? 0.1454 0.1725 0.1266 -0.0312 -0.0042 0.0062  130 ASP   B N    
2636 C  CA   . ASP   B 126 ? 0.1497 0.1716 0.1401 -0.0247 -0.0096 -0.0008 130 ASP   B CA   
2637 C  C    . ASP   B 126 ? 0.1506 0.1718 0.1339 -0.0214 -0.0034 -0.0064 130 ASP   B C    
2638 O  O    . ASP   B 126 ? 0.1584 0.1837 0.1358 -0.0108 -0.0008 -0.0071 130 ASP   B O    
2639 C  CB   . ASP   B 126 ? 0.1553 0.1644 0.1400 -0.0201 -0.0103 0.0027  130 ASP   B CB   
2640 C  CG   . ASP   B 126 ? 0.1492 0.1778 0.1445 -0.0183 -0.0044 -0.0018 130 ASP   B CG   
2641 O  OD1  . ASP   B 126 ? 0.1610 0.1883 0.1494 -0.0111 -0.0070 0.0059  130 ASP   B OD1  
2642 O  OD2  . ASP   B 126 ? 0.1803 0.1911 0.1461 -0.0152 -0.0092 -0.0074 130 ASP   B OD2  
2643 N  N    . PHE   B 127 ? 0.1532 0.1750 0.1325 -0.0175 -0.0062 -0.0119 131 PHE   B N    
2644 C  CA   . PHE   B 127 ? 0.1547 0.1838 0.1407 -0.0162 0.0000  -0.0154 131 PHE   B CA   
2645 C  C    . PHE   B 127 ? 0.1656 0.1846 0.1445 -0.0108 -0.0005 -0.0146 131 PHE   B C    
2646 O  O    . PHE   B 127 ? 0.1586 0.1890 0.1645 0.0081  0.0038  -0.0206 131 PHE   B O    
2647 C  CB   . PHE   B 127 ? 0.1597 0.1934 0.1425 -0.0197 0.0031  -0.0128 131 PHE   B CB   
2648 C  CG   . PHE   B 127 ? 0.1553 0.1998 0.1451 -0.0250 0.0110  -0.0155 131 PHE   B CG   
2649 C  CD1  . PHE   B 127 ? 0.1636 0.2055 0.1450 -0.0231 0.0120  -0.0138 131 PHE   B CD1  
2650 C  CD2  . PHE   B 127 ? 0.1671 0.2150 0.1457 -0.0243 0.0121  -0.0119 131 PHE   B CD2  
2651 C  CE1  . PHE   B 127 ? 0.1585 0.2059 0.1575 -0.0260 0.0116  -0.0201 131 PHE   B CE1  
2652 C  CE2  . PHE   B 127 ? 0.1621 0.2178 0.1480 -0.0238 0.0147  -0.0199 131 PHE   B CE2  
2653 C  CZ   . PHE   B 127 ? 0.1683 0.2119 0.1615 -0.0328 0.0117  -0.0235 131 PHE   B CZ   
2654 N  N    . PRO   B 128 ? 0.1706 0.1856 0.1549 -0.0179 -0.0009 -0.0148 132 PRO   B N    
2655 C  CA   . PRO   B 128 ? 0.1760 0.1853 0.1561 -0.0166 -0.0051 -0.0096 132 PRO   B CA   
2656 C  C    . PRO   B 128 ? 0.1680 0.1800 0.1516 -0.0160 -0.0041 -0.0148 132 PRO   B C    
2657 O  O    . PRO   B 128 ? 0.1800 0.1876 0.1568 -0.0112 -0.0098 -0.0094 132 PRO   B O    
2658 C  CB   . PRO   B 128 ? 0.1912 0.1969 0.1596 -0.0243 -0.0106 -0.0197 132 PRO   B CB   
2659 C  CG   . PRO   B 128 ? 0.1945 0.2116 0.1734 -0.0240 -0.0163 -0.0152 132 PRO   B CG   
2660 C  CD   . PRO   B 128 ? 0.1808 0.1946 0.1584 -0.0218 -0.0071 -0.0169 132 PRO   B CD   
2661 N  N    . LEU   B 129 ? 0.1648 0.1620 0.1517 -0.0104 -0.0044 -0.0058 133 LEU   B N    
2662 C  CA   . LEU   B 129 ? 0.1552 0.1633 0.1537 -0.0103 -0.0021 -0.0073 133 LEU   B CA   
2663 C  C    . LEU   B 129 ? 0.1558 0.1662 0.1602 -0.0012 -0.0012 -0.0133 133 LEU   B C    
2664 O  O    . LEU   B 129 ? 0.1615 0.1641 0.1660 0.0044  0.0006  -0.0130 133 LEU   B O    
2665 C  CB   . LEU   B 129 ? 0.1549 0.1610 0.1489 -0.0114 -0.0038 -0.0080 133 LEU   B CB   
2666 C  CG   . LEU   B 129 ? 0.1643 0.1697 0.1473 -0.0054 -0.0087 -0.0056 133 LEU   B CG   
2667 C  CD1  . LEU   B 129 ? 0.1726 0.1750 0.1669 -0.0073 -0.0091 0.0027  133 LEU   B CD1  
2668 C  CD2  . LEU   B 129 ? 0.1668 0.1838 0.1352 0.0014  -0.0065 -0.0068 133 LEU   B CD2  
2669 N  N    . LEU   B 130 ? 0.1420 0.1607 0.1715 0.0025  -0.0063 -0.0169 134 LEU   B N    
2670 C  CA   . LEU   B 130 ? 0.1470 0.1672 0.1809 0.0042  -0.0090 -0.0196 134 LEU   B CA   
2671 C  C    . LEU   B 130 ? 0.1589 0.1695 0.1934 0.0045  -0.0082 -0.0206 134 LEU   B C    
2672 O  O    . LEU   B 130 ? 0.1824 0.1703 0.1955 0.0123  -0.0116 -0.0190 134 LEU   B O    
2673 C  CB   . LEU   B 130 ? 0.1499 0.1628 0.1973 0.0082  -0.0098 -0.0222 134 LEU   B CB   
2674 C  CG   . LEU   B 130 ? 0.1583 0.1735 0.2096 0.0113  -0.0196 -0.0241 134 LEU   B CG   
2675 C  CD1  . LEU   B 130 ? 0.1610 0.1907 0.2136 0.0108  -0.0298 -0.0261 134 LEU   B CD1  
2676 C  CD2  . LEU   B 130 ? 0.1559 0.1821 0.2284 0.0117  -0.0137 -0.0230 134 LEU   B CD2  
2677 N  N    . GLN   B 131 ? 0.1749 0.1827 0.2039 0.0074  0.0014  -0.0204 135 GLN   B N    
2678 C  CA   . GLN   B 131 ? 0.1904 0.1930 0.2266 0.0182  -0.0008 -0.0206 135 GLN   B CA   
2679 C  C    . GLN   B 131 ? 0.1961 0.1782 0.2138 0.0202  -0.0071 -0.0218 135 GLN   B C    
2680 O  O    . GLN   B 131 ? 0.1999 0.1914 0.2301 0.0247  -0.0112 -0.0232 135 GLN   B O    
2681 C  CB   . GLN   B 131 ? 0.2139 0.2308 0.2368 0.0181  0.0088  -0.0173 135 GLN   B CB   
2682 C  CG   . GLN   B 131 ? 0.2471 0.2689 0.2843 0.0262  0.0266  -0.0084 135 GLN   B CG   
2683 C  CD   . GLN   B 131 ? 0.2454 0.3297 0.3075 0.0344  0.0322  0.0081  135 GLN   B CD   
2684 O  OE1  . GLN   B 131 ? 0.2347 0.3583 0.3384 0.0153  0.0341  0.0403  135 GLN   B OE1  
2685 N  NE2  . GLN   B 131 ? 0.2741 0.3503 0.3203 0.0556  0.0510  -0.0117 135 GLN   B NE2  
2686 N  N    . ALA   B 132 ? 0.2067 0.1644 0.2038 0.0186  -0.0061 -0.0259 136 ALA   B N    
2687 C  CA   . ALA   B 132 ? 0.2079 0.1627 0.1915 0.0158  -0.0085 -0.0274 136 ALA   B CA   
2688 C  C    . ALA   B 132 ? 0.2140 0.1679 0.2030 0.0206  -0.0193 -0.0123 136 ALA   B C    
2689 O  O    . ALA   B 132 ? 0.2446 0.1765 0.2342 0.0225  -0.0260 -0.0033 136 ALA   B O    
2690 C  CB   . ALA   B 132 ? 0.2112 0.1779 0.1889 0.0098  -0.0185 -0.0276 136 ALA   B CB   
2691 N  N    . GLU   B 133 ? 0.2018 0.1630 0.2030 0.0241  -0.0178 -0.0069 137 GLU   B N    
2692 C  CA   . GLU   B 133 ? 0.2117 0.1795 0.2098 0.0208  -0.0237 -0.0091 137 GLU   B CA   
2693 C  C    . GLU   B 133 ? 0.2183 0.1914 0.2230 0.0320  -0.0191 -0.0087 137 GLU   B C    
2694 O  O    . GLU   B 133 ? 0.2284 0.2169 0.2357 0.0264  -0.0200 0.0058  137 GLU   B O    
2695 C  CB   . GLU   B 133 ? 0.2256 0.1864 0.2161 0.0312  -0.0232 -0.0112 137 GLU   B CB   
2696 C  CG   . GLU   B 133 ? 0.2294 0.1886 0.2203 0.0365  -0.0203 -0.0046 137 GLU   B CG   
2697 C  CD   . GLU   B 133 ? 0.2505 0.1998 0.2454 0.0298  -0.0188 0.0081  137 GLU   B CD   
2698 O  OE1  . GLU   B 133 ? 0.2927 0.2298 0.2442 0.0447  -0.0207 0.0214  137 GLU   B OE1  
2699 O  OE2  . GLU   B 133 ? 0.2590 0.1735 0.2555 0.0251  -0.0043 0.0000  137 GLU   B OE2  
2700 N  N    . LEU   B 134 ? 0.2041 0.2045 0.2349 0.0340  -0.0217 -0.0056 138 LEU   B N    
2701 C  CA   . LEU   B 134 ? 0.2199 0.2089 0.2613 0.0539  -0.0228 -0.0083 138 LEU   B CA   
2702 C  C    . LEU   B 134 ? 0.2402 0.2099 0.2827 0.0612  -0.0172 -0.0096 138 LEU   B C    
2703 O  O    . LEU   B 134 ? 0.2667 0.2135 0.3038 0.0786  -0.0296 -0.0171 138 LEU   B O    
2704 C  CB   . LEU   B 134 ? 0.2128 0.2398 0.2737 0.0501  -0.0175 0.0021  138 LEU   B CB   
2705 C  CG   . LEU   B 134 ? 0.2307 0.2428 0.2855 0.0371  -0.0115 0.0140  138 LEU   B CG   
2706 C  CD1  . LEU   B 134 ? 0.2540 0.2650 0.2937 0.0317  -0.0064 0.0252  138 LEU   B CD1  
2707 C  CD2  . LEU   B 134 ? 0.2350 0.2482 0.2970 0.0323  -0.0127 0.0158  138 LEU   B CD2  
2708 N  N    . ALA   B 135 ? 0.2710 0.1979 0.2807 0.0756  -0.0256 -0.0191 139 ALA   B N    
2709 C  CA   . ALA   B 135 ? 0.3033 0.2042 0.3070 0.0787  -0.0252 -0.0243 139 ALA   B CA   
2710 C  C    . ALA   B 135 ? 0.3227 0.1838 0.3130 0.0720  -0.0316 -0.0263 139 ALA   B C    
2711 O  O    . ALA   B 135 ? 0.3584 0.1930 0.3273 0.0904  -0.0505 -0.0251 139 ALA   B O    
2712 C  CB   . ALA   B 135 ? 0.3134 0.2141 0.2968 0.0816  -0.0180 -0.0321 139 ALA   B CB   
2713 N  N    . MET   B 136 ? 0.3257 0.1764 0.3146 0.0663  -0.0346 -0.0258 140 MET   B N    
2714 C  CA   . MET   B 136 ? 0.3603 0.1892 0.3274 0.0514  -0.0328 -0.0177 140 MET   B CA   
2715 C  C    . MET   B 136 ? 0.3694 0.1995 0.3308 0.0550  -0.0438 -0.0030 140 MET   B C    
2716 O  O    . MET   B 136 ? 0.4152 0.2255 0.3456 0.0508  -0.0453 0.0188  140 MET   B O    
2717 C  CB   . MET   B 136 ? 0.3861 0.2350 0.3393 0.0460  -0.0088 -0.0198 140 MET   B CB   
2718 C  CG   . MET   B 136 ? 0.4145 0.2922 0.3614 0.0412  -0.0082 -0.0176 140 MET   B CG   
2719 S  SD   . MET   B 136 ? 0.4879 0.3985 0.4743 -0.0254 -0.0183 -0.0448 140 MET   B SD   
2720 C  CE   . MET   B 136 ? 0.5140 0.4257 0.4896 0.0074  -0.0133 -0.0137 140 MET   B CE   
2721 N  N    . LEU   B 137 ? 0.3431 0.1950 0.3269 0.0697  -0.0613 -0.0256 141 LEU   B N    
2722 C  CA   . LEU   B 137 ? 0.3618 0.2167 0.3412 0.0952  -0.0727 -0.0276 141 LEU   B CA   
2723 C  C    . LEU   B 137 ? 0.3719 0.2677 0.3988 0.1316  -0.0822 -0.0478 141 LEU   B C    
2724 O  O    . LEU   B 137 ? 0.4035 0.2821 0.4187 0.1447  -0.0966 -0.0460 141 LEU   B O    
2725 C  CB   . LEU   B 137 ? 0.3445 0.2263 0.3269 0.0822  -0.0864 -0.0269 141 LEU   B CB   
2726 C  CG   . LEU   B 137 ? 0.3330 0.2321 0.3241 0.0822  -0.0822 -0.0190 141 LEU   B CG   
2727 C  CD1  . LEU   B 137 ? 0.3324 0.2263 0.3119 0.0839  -0.0792 -0.0256 141 LEU   B CD1  
2728 C  CD2  . LEU   B 137 ? 0.3621 0.2493 0.3264 0.0758  -0.0798 -0.0172 141 LEU   B CD2  
2729 N  N    . GLY   B 138 ? 0.3827 0.3031 0.4187 0.1556  -0.0600 -0.0730 142 GLY   B N    
2730 C  CA   . GLY   B 138 ? 0.3770 0.3598 0.4681 0.1640  -0.0519 -0.0842 142 GLY   B CA   
2731 C  C    . GLY   B 138 ? 0.3478 0.3935 0.4952 0.1815  -0.0455 -0.0904 142 GLY   B C    
2732 O  O    . GLY   B 138 ? 0.3560 0.4524 0.5418 0.2001  -0.0377 -0.1007 142 GLY   B O    
2733 N  N    . LEU   B 139 ? 0.3460 0.4132 0.5159 0.1881  -0.0395 -0.0948 143 LEU   B N    
2734 C  CA   . LEU   B 139 ? 0.3485 0.4381 0.5463 0.1826  -0.0184 -0.0956 143 LEU   B CA   
2735 C  C    . LEU   B 139 ? 0.3810 0.4585 0.5816 0.1911  -0.0110 -0.0862 143 LEU   B C    
2736 O  O    . LEU   B 139 ? 0.3651 0.4680 0.6286 0.2325  0.0211  -0.0619 143 LEU   B O    
2737 C  CB   . LEU   B 139 ? 0.3185 0.4378 0.5622 0.1741  -0.0132 -0.0982 143 LEU   B CB   
2738 C  CG   . LEU   B 139 ? 0.3490 0.4466 0.5632 0.1708  -0.0076 -0.1041 143 LEU   B CG   
2739 C  CD1  . LEU   B 139 ? 0.3727 0.4553 0.5704 0.1562  -0.0179 -0.1097 143 LEU   B CD1  
2740 C  CD2  . LEU   B 139 ? 0.3606 0.4412 0.5775 0.1749  -0.0160 -0.1087 143 LEU   B CD2  
2741 N  N    . THR   B 140 ? 0.4837 0.5177 0.6209 0.1557  -0.0268 -0.0976 144 THR   B N    
2742 C  CA   . THR   B 140 ? 0.5473 0.5386 0.6631 0.1375  -0.0370 -0.0891 144 THR   B CA   
2743 C  C    . THR   B 140 ? 0.5863 0.5766 0.6772 0.1209  -0.0324 -0.0533 144 THR   B C    
2744 O  O    . THR   B 140 ? 0.6596 0.6446 0.7011 0.0992  -0.0531 -0.0250 144 THR   B O    
2745 C  CB   . THR   B 140 ? 0.5656 0.5591 0.7039 0.1349  -0.0153 -0.1270 144 THR   B CB   
2746 O  OG1  . THR   B 140 ? 0.5971 0.5788 0.7282 0.1433  -0.0043 -0.1444 144 THR   B OG1  
2747 C  CG2  . THR   B 140 ? 0.5712 0.5431 0.7207 0.1416  0.0042  -0.1470 144 THR   B CG2  
2748 N  N    . SER   B 141 ? 0.5817 0.5431 0.6760 0.1229  -0.0274 -0.0412 145 SER   B N    
2749 C  CA   . SER   B 141 ? 0.5931 0.5069 0.6910 0.1236  -0.0188 -0.0473 145 SER   B CA   
2750 C  C    . SER   B 141 ? 0.5988 0.4988 0.6776 0.1119  -0.0071 -0.0559 145 SER   B C    
2751 O  O    . SER   B 141 ? 0.5765 0.4602 0.6960 0.1374  0.0065  -0.0694 145 SER   B O    
2752 C  CB   . SER   B 141 ? 0.5965 0.5263 0.7173 0.1323  -0.0187 -0.0266 145 SER   B CB   
2753 O  OG   . SER   B 141 ? 0.5926 0.5613 0.7648 0.1507  -0.0284 -0.0068 145 SER   B OG   
2754 N  N    . ALA   B 142 ? 0.6214 0.4195 0.6454 0.0938  -0.0189 -0.0741 146 ALA   B N    
2755 C  CA   . ALA   B 142 ? 0.5501 0.4254 0.6112 0.0739  -0.0384 -0.0539 146 ALA   B CA   
2756 C  C    . ALA   B 142 ? 0.4850 0.3880 0.6007 0.0504  -0.0603 -0.0756 146 ALA   B C    
2757 O  O    . ALA   B 142 ? 0.4221 0.4382 0.6041 0.0751  -0.0786 -0.1106 146 ALA   B O    
2758 C  CB   . ALA   B 142 ? 0.5472 0.4399 0.5990 0.0758  -0.0338 -0.0576 146 ALA   B CB   
2759 N  N    . LEU   B 143 ? 0.4211 0.3445 0.5733 0.0368  -0.0461 -0.0687 147 LEU   B N    
2760 C  CA   . LEU   B 143 ? 0.3584 0.3273 0.5291 0.0349  -0.0305 -0.0735 147 LEU   B CA   
2761 C  C    . LEU   B 143 ? 0.3561 0.3449 0.5415 0.0301  -0.0197 -0.0379 147 LEU   B C    
2762 O  O    . LEU   B 143 ? 0.3230 0.3331 0.5290 0.0250  -0.0100 -0.0312 147 LEU   B O    
2763 C  CB   . LEU   B 143 ? 0.3655 0.3092 0.5230 0.0314  -0.0240 -0.0916 147 LEU   B CB   
2764 C  CG   . LEU   B 143 ? 0.3454 0.3157 0.5249 0.0347  0.0093  -0.0860 147 LEU   B CG   
2765 C  CD1  . LEU   B 143 ? 0.3421 0.3355 0.5239 0.0324  0.0155  -0.0744 147 LEU   B CD1  
2766 C  CD2  . LEU   B 143 ? 0.3663 0.3340 0.5483 0.0353  0.0036  -0.1021 147 LEU   B CD2  
2767 N  N    . ASP   B 144 ? 0.3923 0.3408 0.5416 0.0367  -0.0017 -0.0304 148 ASP   B N    
2768 C  CA   . ASP   B 144 ? 0.4576 0.3773 0.5644 0.0359  -0.0038 -0.0285 148 ASP   B CA   
2769 C  C    . ASP   B 144 ? 0.4292 0.3811 0.5533 0.0313  -0.0091 -0.0269 148 ASP   B C    
2770 O  O    . ASP   B 144 ? 0.4878 0.4447 0.5785 0.0370  -0.0064 -0.0035 148 ASP   B O    
2771 C  CB   . ASP   B 144 ? 0.5181 0.3902 0.6077 0.0444  0.0014  -0.0493 148 ASP   B CB   
2772 C  CG   . ASP   B 144 ? 0.5605 0.4134 0.6463 0.0323  0.0129  -0.0616 148 ASP   B CG   
2773 O  OD1  . ASP   B 144 ? 0.5724 0.4611 0.6195 0.0255  0.0159  -0.0721 148 ASP   B OD1  
2774 O  OD2  . ASP   B 144 ? 0.6270 0.4372 0.7073 0.0650  0.0215  -0.0635 148 ASP   B OD2  
2775 N  N    . GLY   B 145 ? 0.4067 0.3376 0.5234 0.0468  -0.0074 -0.0278 149 GLY   B N    
2776 C  CA   . GLY   B 145 ? 0.3423 0.3111 0.5030 0.0553  -0.0160 -0.0232 149 GLY   B CA   
2777 C  C    . GLY   B 145 ? 0.3074 0.2921 0.4646 0.0411  -0.0174 -0.0206 149 GLY   B C    
2778 O  O    . GLY   B 145 ? 0.3101 0.2706 0.4828 0.0391  -0.0427 -0.0273 149 GLY   B O    
2779 N  N    . ALA   B 146 ? 0.2769 0.2581 0.4311 0.0280  -0.0428 -0.0137 150 ALA   B N    
2780 C  CA   . ALA   B 146 ? 0.2403 0.2464 0.3630 0.0101  -0.0290 -0.0381 150 ALA   B CA   
2781 C  C    . ALA   B 146 ? 0.2101 0.2246 0.3114 0.0059  0.0025  -0.0489 150 ALA   B C    
2782 O  O    . ALA   B 146 ? 0.2169 0.2186 0.3544 0.0089  -0.0176 -0.0557 150 ALA   B O    
2783 C  CB   . ALA   B 146 ? 0.2701 0.2533 0.3361 0.0147  -0.0449 -0.0375 150 ALA   B CB   
2784 N  N    . PHE   B 147 ? 0.1835 0.2025 0.2460 -0.0174 0.0193  -0.0520 151 PHE   B N    
2785 C  CA   . PHE   B 147 ? 0.1784 0.2060 0.2198 -0.0199 0.0302  -0.0523 151 PHE   B CA   
2786 C  C    . PHE   B 147 ? 0.1693 0.2069 0.1944 -0.0256 0.0262  -0.0414 151 PHE   B C    
2787 O  O    . PHE   B 147 ? 0.1574 0.2174 0.1848 -0.0183 0.0226  -0.0308 151 PHE   B O    
2788 C  CB   . PHE   B 147 ? 0.1859 0.2322 0.2146 -0.0190 0.0355  -0.0484 151 PHE   B CB   
2789 C  CG   . PHE   B 147 ? 0.1861 0.2472 0.2270 -0.0223 0.0436  -0.0567 151 PHE   B CG   
2790 C  CD1  . PHE   B 147 ? 0.1915 0.2647 0.2270 -0.0221 0.0437  -0.0542 151 PHE   B CD1  
2791 C  CD2  . PHE   B 147 ? 0.1983 0.2913 0.2314 -0.0206 0.0519  -0.0690 151 PHE   B CD2  
2792 C  CE1  . PHE   B 147 ? 0.1963 0.2822 0.2435 -0.0210 0.0493  -0.0634 151 PHE   B CE1  
2793 C  CE2  . PHE   B 147 ? 0.2079 0.3153 0.2466 -0.0111 0.0519  -0.0829 151 PHE   B CE2  
2794 C  CZ   . PHE   B 147 ? 0.2028 0.3101 0.2475 -0.0087 0.0582  -0.0723 151 PHE   B CZ   
2795 N  N    . CYS   B 148 ? 0.1841 0.2221 0.1791 -0.0287 0.0290  -0.0389 152 CYS   B N    
2796 C  CA   . CYS   B 148 ? 0.1768 0.2344 0.1755 -0.0403 0.0194  -0.0300 152 CYS   B CA   
2797 C  C    . CYS   B 148 ? 0.1741 0.2390 0.1574 -0.0458 0.0188  -0.0259 152 CYS   B C    
2798 O  O    . CYS   B 148 ? 0.1971 0.2562 0.1608 -0.0404 0.0219  -0.0294 152 CYS   B O    
2799 C  CB   . CYS   B 148 ? 0.1913 0.2377 0.1795 -0.0459 0.0208  -0.0292 152 CYS   B CB   
2800 S  SG   . CYS   B 148 ? 0.2287 0.2758 0.2176 -0.0720 0.0177  -0.0467 152 CYS   B SG   
2801 N  N    A VAL   B 149 ? 0.1736 0.2409 0.1520 -0.0448 0.0125  -0.0185 153 VAL   B N    
2802 N  N    B VAL   B 149 ? 0.1696 0.2389 0.1510 -0.0451 0.0083  -0.0176 153 VAL   B N    
2803 C  CA   A VAL   B 149 ? 0.1727 0.2501 0.1508 -0.0445 0.0117  -0.0127 153 VAL   B CA   
2804 C  CA   B VAL   B 149 ? 0.1660 0.2467 0.1493 -0.0455 0.0052  -0.0121 153 VAL   B CA   
2805 C  C    A VAL   B 149 ? 0.1674 0.2550 0.1295 -0.0413 0.0031  -0.0124 153 VAL   B C    
2806 C  C    B VAL   B 149 ? 0.1648 0.2531 0.1302 -0.0404 0.0009  -0.0139 153 VAL   B C    
2807 O  O    A VAL   B 149 ? 0.1606 0.2426 0.1233 -0.0369 -0.0005 -0.0094 153 VAL   B O    
2808 O  O    B VAL   B 149 ? 0.1543 0.2426 0.1258 -0.0324 -0.0060 -0.0159 153 VAL   B O    
2809 C  CB   A VAL   B 149 ? 0.1876 0.2541 0.1799 -0.0465 0.0127  -0.0065 153 VAL   B CB   
2810 C  CB   B VAL   B 149 ? 0.1748 0.2476 0.1740 -0.0480 -0.0005 -0.0042 153 VAL   B CB   
2811 C  CG1  A VAL   B 149 ? 0.1981 0.2603 0.1849 -0.0464 0.0191  -0.0062 153 VAL   B CG1  
2812 C  CG1  B VAL   B 149 ? 0.1716 0.2446 0.1902 -0.0514 -0.0003 0.0032  153 VAL   B CG1  
2813 C  CG2  A VAL   B 149 ? 0.1906 0.2559 0.1762 -0.0494 0.0142  -0.0047 153 VAL   B CG2  
2814 C  CG2  B VAL   B 149 ? 0.1837 0.2566 0.1893 -0.0467 0.0058  -0.0039 153 VAL   B CG2  
2815 N  N    . ASP   B 150 ? 0.1686 0.2638 0.1269 -0.0477 -0.0016 -0.0095 154 ASP   B N    
2816 C  CA   . ASP   B 150 ? 0.1765 0.2784 0.1352 -0.0475 -0.0051 -0.0001 154 ASP   B CA   
2817 C  C    . ASP   B 150 ? 0.1797 0.2820 0.1353 -0.0505 -0.0069 0.0212  154 ASP   B C    
2818 O  O    . ASP   B 150 ? 0.2077 0.3079 0.1347 -0.0429 -0.0028 0.0284  154 ASP   B O    
2819 C  CB   . ASP   B 150 ? 0.1979 0.2855 0.1565 -0.0605 -0.0108 -0.0010 154 ASP   B CB   
2820 C  CG   . ASP   B 150 ? 0.2057 0.2995 0.1615 -0.0592 -0.0080 0.0031  154 ASP   B CG   
2821 O  OD1  . ASP   B 150 ? 0.2152 0.3099 0.1556 -0.0543 0.0004  0.0070  154 ASP   B OD1  
2822 O  OD2  . ASP   B 150 ? 0.2130 0.3072 0.1860 -0.0754 -0.0144 0.0070  154 ASP   B OD2  
2823 N  N    . SER   B 151 ? 0.1850 0.2657 0.1403 -0.0445 -0.0083 0.0376  155 SER   B N    
2824 C  CA   . SER   B 151 ? 0.2029 0.2682 0.1663 -0.0505 -0.0232 0.0435  155 SER   B CA   
2825 C  C    . SER   B 151 ? 0.2380 0.2941 0.1868 -0.0571 -0.0517 0.0510  155 SER   B C    
2826 O  O    . SER   B 151 ? 0.2583 0.2916 0.2221 -0.0579 -0.0561 0.0652  155 SER   B O    
2827 C  CB   . SER   B 151 ? 0.1998 0.2554 0.1715 -0.0465 -0.0248 0.0405  155 SER   B CB   
2828 O  OG   . SER   B 151 ? 0.2011 0.2528 0.1698 -0.0426 -0.0211 0.0386  155 SER   B OG   
2829 N  N    A ILE   B 152 ? 0.2454 0.3094 0.1908 -0.0637 -0.0615 0.0558  156 ILE   B N    
2830 N  N    B ILE   B 152 ? 0.2484 0.3122 0.2067 -0.0630 -0.0585 0.0566  156 ILE   B N    
2831 C  CA   A ILE   B 152 ? 0.2596 0.3361 0.2131 -0.0597 -0.0747 0.0538  156 ILE   B CA   
2832 C  CA   B ILE   B 152 ? 0.2659 0.3456 0.2379 -0.0527 -0.0730 0.0561  156 ILE   B CA   
2833 C  C    A ILE   B 152 ? 0.2906 0.3569 0.2187 -0.0580 -0.0799 0.0496  156 ILE   B C    
2834 C  C    B ILE   B 152 ? 0.2951 0.3621 0.2373 -0.0542 -0.0790 0.0513  156 ILE   B C    
2835 O  O    A ILE   B 152 ? 0.3222 0.3671 0.2384 -0.0453 -0.0851 0.0558  156 ILE   B O    
2836 O  O    B ILE   B 152 ? 0.3283 0.3739 0.2551 -0.0404 -0.0825 0.0579  156 ILE   B O    
2837 C  CB   A ILE   B 152 ? 0.2592 0.3317 0.2108 -0.0646 -0.0873 0.0529  156 ILE   B CB   
2838 C  CB   B ILE   B 152 ? 0.2689 0.3485 0.2683 -0.0546 -0.0834 0.0596  156 ILE   B CB   
2839 C  CG1  A ILE   B 152 ? 0.2581 0.3328 0.2471 -0.0653 -0.0650 0.0486  156 ILE   B CG1  
2840 C  CG1  B ILE   B 152 ? 0.2740 0.3564 0.2990 -0.0445 -0.0612 0.0544  156 ILE   B CG1  
2841 C  CG2  A ILE   B 152 ? 0.2537 0.3378 0.1942 -0.0579 -0.0947 0.0472  156 ILE   B CG2  
2842 C  CG2  B ILE   B 152 ? 0.2742 0.3616 0.2793 -0.0530 -0.0882 0.0569  156 ILE   B CG2  
2843 C  CD1  A ILE   B 152 ? 0.2640 0.3349 0.2555 -0.0697 -0.0578 0.0479  156 ILE   B CD1  
2844 C  CD1  B ILE   B 152 ? 0.2785 0.3603 0.3252 -0.0497 -0.0572 0.0540  156 ILE   B CD1  
2845 N  N    . THR   B 153 ? 0.2981 0.3627 0.2091 -0.0540 -0.0715 0.0455  157 THR   B N    
2846 C  CA   . THR   B 153 ? 0.3228 0.3895 0.2124 -0.0675 -0.0660 0.0368  157 THR   B CA   
2847 C  C    . THR   B 153 ? 0.3422 0.4170 0.1989 -0.0680 -0.0492 0.0453  157 THR   B C    
2848 O  O    . THR   B 153 ? 0.3677 0.4377 0.2162 -0.0603 -0.0689 0.0717  157 THR   B O    
2849 C  CB   . THR   B 153 ? 0.3360 0.3932 0.2197 -0.0689 -0.0472 0.0182  157 THR   B CB   
2850 O  OG1  . THR   B 153 ? 0.3388 0.4100 0.2366 -0.0671 -0.0211 0.0058  157 THR   B OG1  
2851 C  CG2  . THR   B 153 ? 0.3704 0.3960 0.2402 -0.0717 -0.0320 0.0079  157 THR   B CG2  
2852 N  N    . ALA   B 154 ? 0.3301 0.4150 0.1880 -0.0643 -0.0445 0.0473  158 ALA   B N    
2853 C  CA   . ALA   B 154 ? 0.3570 0.4129 0.1830 -0.0654 -0.0351 0.0606  158 ALA   B CA   
2854 C  C    . ALA   B 154 ? 0.3870 0.4067 0.2284 -0.0671 -0.0481 0.0808  158 ALA   B C    
2855 O  O    . ALA   B 154 ? 0.4286 0.4306 0.2397 -0.0483 -0.0463 0.1062  158 ALA   B O    
2856 C  CB   . ALA   B 154 ? 0.3285 0.4195 0.2053 -0.0635 -0.0371 0.0526  158 ALA   B CB   
2857 N  N    . LEU   B 155 ? 0.3917 0.3837 0.2625 -0.0669 -0.0626 0.0947  159 LEU   B N    
2858 C  CA   . LEU   B 155 ? 0.4110 0.3826 0.2920 -0.0584 -0.0849 0.1109  159 LEU   B CA   
2859 C  C    . LEU   B 155 ? 0.4499 0.4253 0.3267 -0.0562 -0.1195 0.1349  159 LEU   B C    
2860 O  O    . LEU   B 155 ? 0.4587 0.4190 0.3517 -0.0416 -0.1315 0.1338  159 LEU   B O    
2861 C  CB   . LEU   B 155 ? 0.4241 0.3575 0.3257 -0.0602 -0.0679 0.1131  159 LEU   B CB   
2862 C  CG   . LEU   B 155 ? 0.4372 0.3817 0.3322 -0.0671 -0.0586 0.0967  159 LEU   B CG   
2863 C  CD1  . LEU   B 155 ? 0.4286 0.3862 0.3309 -0.0585 -0.0503 0.0887  159 LEU   B CD1  
2864 C  CD2  . LEU   B 155 ? 0.4293 0.3824 0.3589 -0.0635 -0.0573 0.0845  159 LEU   B CD2  
2865 N  N    . LYS   B 156 ? 0.4942 0.4482 0.3226 -0.0471 -0.1608 0.1386  160 LYS   B N    
2866 C  CA   . LYS   B 156 ? 0.5042 0.4977 0.3459 -0.0329 -0.1831 0.1598  160 LYS   B CA   
2867 C  C    . LYS   B 156 ? 0.5610 0.5486 0.3337 -0.0287 -0.1822 0.1773  160 LYS   B C    
2868 O  O    . LYS   B 156 ? 0.5938 0.5602 0.3667 -0.0263 -0.2134 0.1890  160 LYS   B O    
2869 C  CB   . LYS   B 156 ? 0.5192 0.5055 0.3664 -0.0295 -0.1879 0.1568  160 LYS   B CB   
2870 C  CG   . LYS   B 156 ? 0.5189 0.5154 0.4070 -0.0155 -0.1742 0.1641  160 LYS   B CG   
2871 N  N    . ALA   B 157 ? 0.5661 0.5909 0.3140 -0.0335 -0.1726 0.2005  161 ALA   B N    
2872 C  CA   . ALA   B 157 ? 0.6142 0.6386 0.3356 -0.0352 -0.1366 0.1974  161 ALA   B CA   
2873 C  C    . ALA   B 157 ? 0.6067 0.6568 0.3790 -0.0500 -0.1181 0.2349  161 ALA   B C    
2874 O  O    . ALA   B 157 ? 0.6336 0.6721 0.4001 -0.0226 -0.0994 0.2473  161 ALA   B O    
2875 C  CB   . ALA   B 157 ? 0.6276 0.6401 0.2981 -0.0163 -0.1376 0.1932  161 ALA   B CB   
2876 N  N    . LEU   B 158 ? 0.5820 0.6578 0.3992 -0.0643 -0.1116 0.2603  162 LEU   B N    
2877 C  CA   . LEU   B 158 ? 0.5653 0.6717 0.4459 -0.0763 -0.1125 0.2814  162 LEU   B CA   
2878 C  C    . LEU   B 158 ? 0.6067 0.6787 0.4983 -0.0796 -0.1454 0.3060  162 LEU   B C    
2879 O  O    . LEU   B 158 ? 0.5801 0.6694 0.5203 -0.0897 -0.1495 0.3098  162 LEU   B O    
2880 C  CB   . LEU   B 158 ? 0.5228 0.6821 0.4668 -0.0816 -0.1024 0.2752  162 LEU   B CB   
2881 C  CG   . LEU   B 158 ? 0.4977 0.7167 0.4827 -0.0838 -0.0945 0.2640  162 LEU   B CG   
2882 C  CD1  . LEU   B 158 ? 0.4740 0.7534 0.4977 -0.0761 -0.1060 0.2373  162 LEU   B CD1  
2883 C  CD2  . LEU   B 158 ? 0.5001 0.7089 0.5078 -0.0923 -0.0917 0.2698  162 LEU   B CD2  
2884 N  N    . GLU   B 159 ? 0.6227 0.6678 0.5223 -0.0998 -0.1727 0.3306  163 GLU   B N    
2885 C  CA   . GLU   B 159 ? 0.6544 0.6973 0.5784 -0.0982 -0.1842 0.3112  163 GLU   B CA   
2886 C  C    . GLU   B 159 ? 0.7407 0.7551 0.5811 -0.0895 -0.1884 0.3258  163 GLU   B C    
2887 O  O    . GLU   B 159 ? 0.7378 0.7366 0.6069 -0.0841 -0.1789 0.3448  163 GLU   B O    
2888 C  CB   . GLU   B 159 ? 0.6624 0.6777 0.6039 -0.1179 -0.1568 0.3160  163 GLU   B CB   
2889 N  N    . ARG   B 160 ? 0.8123 0.8203 0.5760 -0.0946 -0.1811 0.3089  164 ARG   B N    
2890 C  CA   . ARG   B 160 ? 0.8296 0.8872 0.5790 -0.0891 -0.1849 0.2915  164 ARG   B CA   
2891 C  C    . ARG   B 160 ? 0.8402 0.9231 0.5703 -0.0864 -0.1862 0.3247  164 ARG   B C    
2892 O  O    . ARG   B 160 ? 0.8652 0.9539 0.5263 -0.0821 -0.1863 0.3057  164 ARG   B O    
2893 C  CB   . ARG   B 160 ? 0.8539 0.8846 0.5932 -0.0956 -0.1612 0.2722  164 ARG   B CB   
2894 N  N    . ALA   B 161 ? 0.8242 0.9529 0.6388 -0.1012 -0.1654 0.3192  165 ALA   B N    
2895 C  CA   . ALA   B 161 ? 0.8205 0.9873 0.7273 -0.1031 -0.1296 0.2936  165 ALA   B CA   
2896 C  C    . ALA   B 161 ? 0.8000 0.9488 0.7464 -0.0976 -0.1373 0.3010  165 ALA   B C    
2897 O  O    . ALA   B 161 ? 0.7817 0.9453 0.7352 -0.0988 -0.1411 0.3084  165 ALA   B O    
2898 C  CB   . ALA   B 161 ? 0.8292 0.9993 0.7473 -0.0959 -0.1099 0.2905  165 ALA   B CB   
2899 N  N    . LYS   B 171 ? 0.6839 0.7497 0.5158 0.0566  -0.2101 0.0758  175 LYS   B N    
2900 C  CA   . LYS   B 171 ? 0.6582 0.7044 0.4829 0.0752  -0.2187 0.1144  175 LYS   B CA   
2901 C  C    . LYS   B 171 ? 0.5936 0.6691 0.4678 0.0709  -0.1973 0.1151  175 LYS   B C    
2902 O  O    . LYS   B 171 ? 0.6857 0.6834 0.5281 0.0816  -0.1845 0.1302  175 LYS   B O    
2903 C  CB   . LYS   B 171 ? 0.7198 0.7284 0.5125 0.0512  -0.1863 0.0885  175 LYS   B CB   
2904 C  CG   . LYS   B 171 ? 0.7422 0.7415 0.5348 0.0502  -0.1777 0.0838  175 LYS   B CG   
2905 C  CD   . LYS   B 171 ? 0.7814 0.7443 0.5035 0.0609  -0.1763 0.0942  175 LYS   B CD   
2906 C  CE   . LYS   B 171 ? 0.8031 0.7441 0.5321 0.0605  -0.1517 0.0927  175 LYS   B CE   
2907 N  NZ   . LYS   B 171 ? 0.8243 0.7598 0.5536 0.0681  -0.1437 0.0998  175 LYS   B NZ   
2908 N  N    . SER   B 172 ? 0.4494 0.5672 0.4558 0.0518  -0.1963 0.0976  176 SER   B N    
2909 C  CA   . SER   B 172 ? 0.3538 0.5358 0.4246 0.0135  -0.1810 0.0871  176 SER   B CA   
2910 C  C    . SER   B 172 ? 0.3482 0.4913 0.3742 0.0107  -0.1660 0.0819  176 SER   B C    
2911 O  O    . SER   B 172 ? 0.3734 0.4793 0.3821 0.0288  -0.1431 0.0843  176 SER   B O    
2912 C  CB   . SER   B 172 ? 0.3278 0.5474 0.4296 -0.0075 -0.1856 0.0820  176 SER   B CB   
2913 O  OG   . SER   B 172 ? 0.3375 0.5535 0.4373 -0.0119 -0.1760 0.0909  176 SER   B OG   
2914 N  N    . TYR   B 173 ? 0.3418 0.4656 0.3463 0.0045  -0.1522 0.0720  177 TYR   B N    
2915 C  CA   . TYR   B 173 ? 0.3344 0.4585 0.3449 0.0117  -0.1216 0.0833  177 TYR   B CA   
2916 C  C    . TYR   B 173 ? 0.2885 0.4193 0.3345 0.0159  -0.0978 0.0811  177 TYR   B C    
2917 O  O    . TYR   B 173 ? 0.2792 0.4047 0.3274 0.0296  -0.0829 0.0596  177 TYR   B O    
2918 C  CB   . TYR   B 173 ? 0.4081 0.4863 0.3679 0.0128  -0.1150 0.0661  177 TYR   B CB   
2919 C  CG   . TYR   B 173 ? 0.4857 0.5322 0.3745 0.0094  -0.1223 0.0793  177 TYR   B CG   
2920 C  CD1  . TYR   B 173 ? 0.5213 0.5577 0.3903 0.0009  -0.1145 0.0828  177 TYR   B CD1  
2921 C  CD2  . TYR   B 173 ? 0.5431 0.5643 0.3835 -0.0067 -0.1385 0.0773  177 TYR   B CD2  
2922 C  CE1  . TYR   B 173 ? 0.5613 0.5943 0.4114 -0.0026 -0.1151 0.0965  177 TYR   B CE1  
2923 C  CE2  . TYR   B 173 ? 0.5740 0.6000 0.3823 -0.0051 -0.1279 0.0862  177 TYR   B CE2  
2924 C  CZ   . TYR   B 173 ? 0.6047 0.5963 0.3941 -0.0030 -0.1141 0.0924  177 TYR   B CZ   
2925 O  OH   . TYR   B 173 ? 0.6938 0.6456 0.4124 0.0111  -0.1080 0.1214  177 TYR   B OH   
2926 N  N    . SER   B 174 ? 0.2753 0.4082 0.3134 0.0093  -0.0970 0.0973  178 SER   B N    
2927 C  CA   . SER   B 174 ? 0.2556 0.3938 0.3093 0.0052  -0.0806 0.0967  178 SER   B CA   
2928 C  C    . SER   B 174 ? 0.2632 0.3775 0.2877 0.0058  -0.0716 0.0989  178 SER   B C    
2929 O  O    . SER   B 174 ? 0.2513 0.3790 0.2943 0.0086  -0.0761 0.1094  178 SER   B O    
2930 C  CB   . SER   B 174 ? 0.2665 0.4064 0.3341 -0.0053 -0.0660 0.0918  178 SER   B CB   
2931 O  OG   . SER   B 174 ? 0.2410 0.4271 0.3761 -0.0004 -0.0502 0.0819  178 SER   B OG   
2932 N  N    . LEU   B 175 ? 0.2431 0.3587 0.2821 0.0013  -0.0611 0.0942  179 LEU   B N    
2933 C  CA   . LEU   B 175 ? 0.2446 0.3592 0.2826 0.0026  -0.0554 0.0813  179 LEU   B CA   
2934 C  C    . LEU   B 175 ? 0.2206 0.3707 0.3024 0.0089  -0.0488 0.0879  179 LEU   B C    
2935 O  O    . LEU   B 175 ? 0.2355 0.3708 0.2934 -0.0003 -0.0495 0.0927  179 LEU   B O    
2936 C  CB   . LEU   B 175 ? 0.2571 0.3542 0.2771 0.0000  -0.0409 0.0865  179 LEU   B CB   
2937 C  CG   . LEU   B 175 ? 0.2618 0.3500 0.2806 -0.0010 -0.0434 0.0828  179 LEU   B CG   
2938 C  CD1  . LEU   B 175 ? 0.2526 0.3457 0.2929 0.0031  -0.0434 0.0841  179 LEU   B CD1  
2939 C  CD2  . LEU   B 175 ? 0.2602 0.3436 0.2713 0.0089  -0.0533 0.0792  179 LEU   B CD2  
2940 N  N    . GLY   B 176 ? 0.2287 0.3827 0.3216 0.0041  -0.0378 0.0857  180 GLY   B N    
2941 C  CA   . GLY   B 176 ? 0.2246 0.3856 0.3524 0.0095  -0.0325 0.0764  180 GLY   B CA   
2942 C  C    . GLY   B 176 ? 0.2270 0.3933 0.3781 0.0139  -0.0481 0.0812  180 GLY   B C    
2943 O  O    . GLY   B 176 ? 0.2235 0.3992 0.4124 0.0238  -0.0429 0.0614  180 GLY   B O    
2944 N  N    . SER   B 177 ? 0.2299 0.3967 0.3839 0.0134  -0.0549 0.0892  181 SER   B N    
2945 C  CA   . SER   B 177 ? 0.2400 0.4252 0.4003 0.0131  -0.0745 0.1039  181 SER   B CA   
2946 C  C    . SER   B 177 ? 0.2404 0.3947 0.4033 0.0172  -0.0924 0.0995  181 SER   B C    
2947 O  O    . SER   B 177 ? 0.2460 0.3888 0.4114 0.0283  -0.1035 0.1011  181 SER   B O    
2948 C  CB   . SER   B 177 ? 0.2683 0.4514 0.4162 -0.0021 -0.0801 0.0973  181 SER   B CB   
2949 O  OG   . SER   B 177 ? 0.2831 0.5290 0.4432 -0.0020 -0.0732 0.1016  181 SER   B OG   
2950 N  N    . ILE   B 178 ? 0.2291 0.3720 0.3753 0.0176  -0.0886 0.1072  182 ILE   B N    
2951 C  CA   . ILE   B 178 ? 0.2390 0.3636 0.3540 0.0166  -0.0856 0.1074  182 ILE   B CA   
2952 C  C    . ILE   B 178 ? 0.2444 0.3558 0.3810 0.0238  -0.0718 0.1050  182 ILE   B C    
2953 O  O    . ILE   B 178 ? 0.2543 0.3458 0.4021 0.0291  -0.0794 0.1242  182 ILE   B O    
2954 C  CB   . ILE   B 178 ? 0.2501 0.3645 0.3287 0.0164  -0.0867 0.1124  182 ILE   B CB   
2955 C  CG1  . ILE   B 178 ? 0.2702 0.3769 0.3285 0.0106  -0.0804 0.1141  182 ILE   B CG1  
2956 C  CG2  . ILE   B 178 ? 0.2295 0.3731 0.3199 0.0170  -0.0994 0.1046  182 ILE   B CG2  
2957 C  CD1  . ILE   B 178 ? 0.2639 0.3953 0.3416 0.0135  -0.0750 0.1015  182 ILE   B CD1  
2958 N  N    . TYR   B 179 ? 0.2458 0.3312 0.3759 0.0343  -0.0651 0.0947  183 TYR   B N    
2959 C  CA   . TYR   B 179 ? 0.2538 0.3336 0.4025 0.0398  -0.0563 0.0675  183 TYR   B CA   
2960 C  C    . TYR   B 179 ? 0.2912 0.3485 0.4525 0.0576  -0.0747 0.0644  183 TYR   B C    
2961 O  O    . TYR   B 179 ? 0.3209 0.3329 0.4817 0.0558  -0.0936 0.0372  183 TYR   B O    
2962 C  CB   . TYR   B 179 ? 0.2516 0.3299 0.3837 0.0414  -0.0442 0.0482  183 TYR   B CB   
2963 C  CG   . TYR   B 179 ? 0.2508 0.3284 0.3861 0.0402  -0.0349 0.0393  183 TYR   B CG   
2964 C  CD1  . TYR   B 179 ? 0.2583 0.3336 0.4023 0.0466  -0.0382 0.0225  183 TYR   B CD1  
2965 C  CD2  . TYR   B 179 ? 0.2482 0.3150 0.3637 0.0356  -0.0223 0.0533  183 TYR   B CD2  
2966 C  CE1  . TYR   B 179 ? 0.2656 0.3093 0.4071 0.0482  -0.0236 0.0099  183 TYR   B CE1  
2967 C  CE2  . TYR   B 179 ? 0.2483 0.3021 0.3660 0.0333  -0.0154 0.0385  183 TYR   B CE2  
2968 C  CZ   . TYR   B 179 ? 0.2544 0.3098 0.3827 0.0332  -0.0175 0.0249  183 TYR   B CZ   
2969 O  OH   . TYR   B 179 ? 0.2588 0.3087 0.4095 0.0088  -0.0039 0.0219  183 TYR   B OH   
2970 N  N    . THR   B 180 ? 0.3008 0.3789 0.5150 0.0846  -0.0859 0.0594  184 THR   B N    
2971 C  CA   . THR   B 180 ? 0.3318 0.3992 0.5551 0.1053  -0.0926 0.0692  184 THR   B CA   
2972 C  C    . THR   B 180 ? 0.3457 0.3940 0.5852 0.0877  -0.1032 0.0878  184 THR   B C    
2973 O  O    . THR   B 180 ? 0.3629 0.4010 0.6230 0.0979  -0.1103 0.0761  184 THR   B O    
2974 C  CB   . THR   B 180 ? 0.3253 0.4342 0.5892 0.1218  -0.0739 0.0725  184 THR   B CB   
2975 O  OG1  . THR   B 180 ? 0.3588 0.4519 0.6136 0.1381  -0.0283 0.0560  184 THR   B OG1  
2976 C  CG2  . THR   B 180 ? 0.3589 0.4441 0.6275 0.1356  -0.0678 0.0670  184 THR   B CG2  
2977 N  N    . ARG   B 181 ? 0.3322 0.3939 0.5653 0.0737  -0.1315 0.1070  185 ARG   B N    
2978 C  CA   . ARG   B 181 ? 0.3520 0.3780 0.5929 0.0647  -0.1554 0.1358  185 ARG   B CA   
2979 C  C    . ARG   B 181 ? 0.3609 0.3700 0.5928 0.0633  -0.1599 0.1444  185 ARG   B C    
2980 O  O    . ARG   B 181 ? 0.3925 0.3714 0.5908 0.0229  -0.1856 0.1482  185 ARG   B O    
2981 C  CB   . ARG   B 181 ? 0.3946 0.4102 0.6076 0.0544  -0.1489 0.1260  185 ARG   B CB   
2982 C  CG   . ARG   B 181 ? 0.4626 0.4548 0.6288 0.0380  -0.1516 0.1164  185 ARG   B CG   
2983 C  CD   . ARG   B 181 ? 0.4642 0.4432 0.6108 0.0266  -0.1680 0.1428  185 ARG   B CD   
2984 N  NE   . ARG   B 181 ? 0.4589 0.4580 0.5660 0.0146  -0.1745 0.1363  185 ARG   B NE   
2985 C  CZ   . ARG   B 181 ? 0.4784 0.4652 0.5519 0.0091  -0.2051 0.1367  185 ARG   B CZ   
2986 N  NH1  . ARG   B 181 ? 0.4910 0.4576 0.5375 -0.0064 -0.2174 0.1427  185 ARG   B NH1  
2987 N  NH2  . ARG   B 181 ? 0.4823 0.4880 0.5367 0.0097  -0.2216 0.1291  185 ARG   B NH2  
2988 N  N    . LEU   B 182 ? 0.3540 0.3743 0.5917 0.0587  -0.1570 0.1543  186 LEU   B N    
2989 C  CA   . LEU   B 182 ? 0.3625 0.3612 0.6087 0.0548  -0.1358 0.1369  186 LEU   B CA   
2990 C  C    . LEU   B 182 ? 0.3445 0.3569 0.6384 0.0781  -0.1325 0.1133  186 LEU   B C    
2991 O  O    . LEU   B 182 ? 0.4205 0.3530 0.6852 0.0683  -0.1188 0.1093  186 LEU   B O    
2992 C  CB   . LEU   B 182 ? 0.3662 0.3655 0.5872 0.0491  -0.1314 0.1575  186 LEU   B CB   
2993 C  CG   . LEU   B 182 ? 0.3802 0.3906 0.5765 0.0402  -0.0998 0.1716  186 LEU   B CG   
2994 C  CD1  . LEU   B 182 ? 0.3703 0.4073 0.5764 0.0304  -0.0925 0.1696  186 LEU   B CD1  
2995 C  CD2  . LEU   B 182 ? 0.4122 0.4247 0.5845 0.0228  -0.0817 0.1674  186 LEU   B CD2  
2996 N  N    . TYR   B 183 ? 0.3368 0.3689 0.6401 0.0867  -0.1232 0.0582  187 TYR   B N    
2997 C  CA   . TYR   B 183 ? 0.3469 0.3905 0.6614 0.0940  -0.1154 0.0370  187 TYR   B CA   
2998 C  C    . TYR   B 183 ? 0.3949 0.4693 0.7264 0.1352  -0.1025 -0.0294 187 TYR   B C    
2999 O  O    . TYR   B 183 ? 0.4144 0.4862 0.7521 0.1580  -0.0889 -0.0640 187 TYR   B O    
3000 C  CB   . TYR   B 183 ? 0.3111 0.3512 0.6227 0.0643  -0.1085 0.0339  187 TYR   B CB   
3001 C  CG   . TYR   B 183 ? 0.2965 0.3123 0.5737 0.0473  -0.0980 0.0566  187 TYR   B CG   
3002 C  CD1  . TYR   B 183 ? 0.3095 0.3022 0.5543 0.0559  -0.0955 0.0846  187 TYR   B CD1  
3003 C  CD2  . TYR   B 183 ? 0.2880 0.3049 0.5132 0.0355  -0.1085 0.0808  187 TYR   B CD2  
3004 C  CE1  . TYR   B 183 ? 0.3014 0.2782 0.5300 0.0311  -0.0895 0.0892  187 TYR   B CE1  
3005 C  CE2  . TYR   B 183 ? 0.2788 0.2855 0.4858 0.0404  -0.1031 0.0846  187 TYR   B CE2  
3006 C  CZ   . TYR   B 183 ? 0.2984 0.2764 0.4962 0.0390  -0.1005 0.0970  187 TYR   B CZ   
3007 O  OH   . TYR   B 183 ? 0.3068 0.2521 0.4405 0.0197  -0.0750 0.1247  187 TYR   B OH   
3008 N  N    . GLY   B 184 ? 0.4226 0.5292 0.7615 0.1500  -0.1166 -0.0771 188 GLY   B N    
3009 C  CA   . GLY   B 184 ? 0.4058 0.6299 0.7950 0.1624  -0.1010 -0.1046 188 GLY   B CA   
3010 C  C    . GLY   B 184 ? 0.4468 0.6755 0.8005 0.1870  -0.0756 -0.1289 188 GLY   B C    
3011 O  O    . GLY   B 184 ? 0.4298 0.7527 0.8603 0.2139  -0.0729 -0.1321 188 GLY   B O    
3012 N  N    . GLN   B 185 ? 0.4285 0.7020 0.8043 0.2069  -0.0644 -0.1361 189 GLN   B N    
3013 C  CA   . GLN   B 185 ? 0.4595 0.7438 0.8075 0.2013  -0.0442 -0.1425 189 GLN   B CA   
3014 C  C    . GLN   B 185 ? 0.4488 0.7761 0.7918 0.2276  -0.0200 -0.1363 189 GLN   B C    
3015 O  O    . GLN   B 185 ? 0.4516 0.7613 0.7903 0.2598  -0.0466 -0.1441 189 GLN   B O    
3016 C  CB   . GLN   B 185 ? 0.4801 0.7693 0.8342 0.1801  -0.0537 -0.1415 189 GLN   B CB   
3017 N  N    . SER   B 186 ? 0.5013 0.8102 0.8011 0.1935  0.0004  -0.1299 190 SER   B N    
3018 C  CA   . SER   B 186 ? 0.5377 0.8161 0.8040 0.1467  0.0403  -0.1444 190 SER   B CA   
3019 C  C    . SER   B 186 ? 0.5338 0.8173 0.7827 0.1305  0.0647  -0.1389 190 SER   B C    
3020 O  O    . SER   B 186 ? 0.5313 0.8603 0.7834 0.1375  0.0563  -0.1721 190 SER   B O    
3021 C  CB   . SER   B 186 ? 0.5765 0.8330 0.8207 0.1281  0.0578  -0.1400 190 SER   B CB   
3022 O  OG   . SER   B 186 ? 0.6524 0.8660 0.8447 0.1074  0.0541  -0.1148 190 SER   B OG   
3023 N  N    . PRO   B 187 ? 0.5163 0.7904 0.7350 0.0943  0.1169  -0.1286 191 PRO   B N    
3024 C  CA   . PRO   B 187 ? 0.5169 0.7749 0.7335 0.0654  0.1215  -0.1111 191 PRO   B CA   
3025 C  C    . PRO   B 187 ? 0.5558 0.7595 0.7445 0.0475  0.1367  -0.1023 191 PRO   B C    
3026 O  O    . PRO   B 187 ? 0.5921 0.8511 0.7326 0.0144  0.1730  -0.1433 191 PRO   B O    
3027 C  CB   . PRO   B 187 ? 0.4970 0.7799 0.7257 0.0735  0.1291  -0.1149 191 PRO   B CB   
3028 C  CG   . PRO   B 187 ? 0.4977 0.7728 0.7172 0.0762  0.1337  -0.1247 191 PRO   B CG   
3029 C  CD   . PRO   B 187 ? 0.5039 0.7843 0.7253 0.0799  0.1260  -0.1204 191 PRO   B CD   
3030 N  N    . PRO   B 188 ? 0.6190 0.6711 0.7674 0.0055  0.1389  -0.0727 192 PRO   B N    
3031 C  CA   . PRO   B 188 ? 0.6656 0.6595 0.7752 -0.0052 0.1340  -0.0620 192 PRO   B CA   
3032 C  C    . PRO   B 188 ? 0.7377 0.6627 0.7959 -0.0123 0.1389  -0.0389 192 PRO   B C    
3033 O  O    . PRO   B 188 ? 0.7690 0.6437 0.8120 0.0308  0.1598  -0.0771 192 PRO   B O    
3034 C  CB   . PRO   B 188 ? 0.6457 0.6604 0.7761 -0.0027 0.1343  -0.0571 192 PRO   B CB   
3035 C  CG   . PRO   B 188 ? 0.6269 0.6601 0.7699 0.0071  0.1371  -0.0631 192 PRO   B CG   
3036 C  CD   . PRO   B 188 ? 0.6068 0.6578 0.7731 0.0043  0.1278  -0.0572 192 PRO   B CD   
3037 N  N    . ASP   B 189 ? 0.7842 0.6346 0.7816 -0.0392 0.1179  -0.0081 193 ASP   B N    
3038 C  CA   . ASP   B 189 ? 0.7924 0.6383 0.7534 -0.0587 0.0673  -0.0055 193 ASP   B CA   
3039 C  C    . ASP   B 189 ? 0.7160 0.6446 0.7482 -0.0919 0.0452  -0.0058 193 ASP   B C    
3040 O  O    . ASP   B 189 ? 0.6782 0.7267 0.7785 -0.0703 0.0453  -0.0530 193 ASP   B O    
3041 C  CB   . ASP   B 189 ? 0.8194 0.6231 0.7395 -0.0607 0.0716  0.0378  193 ASP   B CB   
3042 C  CG   . ASP   B 189 ? 0.8508 0.6464 0.7174 -0.0706 0.0720  0.0634  193 ASP   B CG   
3043 O  OD1  . ASP   B 189 ? 0.9053 0.6661 0.7210 -0.0795 0.0360  0.0690  193 ASP   B OD1  
3044 O  OD2  . ASP   B 189 ? 0.8500 0.5945 0.7199 -0.0642 0.0928  0.0796  193 ASP   B OD2  
3045 N  N    . SER   B 190 ? 0.6395 0.5969 0.6800 -0.0771 0.0217  -0.0010 194 SER   B N    
3046 C  CA   . SER   B 190 ? 0.5846 0.5512 0.6288 -0.0742 -0.0012 0.0346  194 SER   B CA   
3047 C  C    . SER   B 190 ? 0.5343 0.5285 0.5602 -0.0618 -0.0279 0.0251  194 SER   B C    
3048 O  O    . SER   B 190 ? 0.5764 0.5486 0.6455 -0.1045 -0.0349 -0.0001 194 SER   B O    
3049 C  CB   . SER   B 190 ? 0.6002 0.5716 0.6144 -0.0671 -0.0286 0.0344  194 SER   B CB   
3050 N  N    . HIS   B 191 ? 0.4048 0.4358 0.5211 -0.0536 0.0052  0.0503  195 HIS   B N    
3051 C  CA   . HIS   B 191 ? 0.3489 0.3627 0.4294 -0.0021 -0.0089 0.0348  195 HIS   B CA   
3052 C  C    . HIS   B 191 ? 0.2258 0.2774 0.3570 -0.0316 0.0234  0.0364  195 HIS   B C    
3053 O  O    . HIS   B 191 ? 0.2247 0.3024 0.3659 -0.0213 0.0145  0.0491  195 HIS   B O    
3054 C  CB   . HIS   B 191 ? 0.3775 0.4446 0.4756 -0.0037 0.0082  0.0189  195 HIS   B CB   
3055 C  CG   . HIS   B 191 ? 0.4748 0.5069 0.4835 0.0076  -0.0262 0.0123  195 HIS   B CG   
3056 N  ND1  . HIS   B 191 ? 0.5234 0.5085 0.5023 0.0081  -0.0345 0.0191  195 HIS   B ND1  
3057 C  CD2  . HIS   B 191 ? 0.4798 0.5554 0.4757 0.0299  -0.0310 0.0138  195 HIS   B CD2  
3058 C  CE1  . HIS   B 191 ? 0.5133 0.4962 0.5008 0.0186  -0.0232 -0.0067 195 HIS   B CE1  
3059 N  NE2  . HIS   B 191 ? 0.4696 0.4929 0.4633 0.0547  -0.0164 0.0062  195 HIS   B NE2  
3060 N  N    . THR   B 192 ? 0.2055 0.2055 0.2990 -0.0125 0.0145  0.0527  196 THR   B N    
3061 C  CA   . THR   B 192 ? 0.1887 0.1862 0.2497 -0.0090 0.0294  0.0461  196 THR   B CA   
3062 C  C    . THR   B 192 ? 0.1625 0.1761 0.2154 -0.0102 0.0136  0.0482  196 THR   B C    
3063 O  O    . THR   B 192 ? 0.1600 0.1973 0.2261 -0.0091 0.0134  0.0566  196 THR   B O    
3064 C  CB   . THR   B 192 ? 0.2275 0.2015 0.2539 -0.0030 0.0422  0.0374  196 THR   B CB   
3065 O  OG1  . THR   B 192 ? 0.2385 0.2177 0.2444 -0.0232 0.0520  0.0250  196 THR   B OG1  
3066 C  CG2  . THR   B 192 ? 0.2584 0.2056 0.2615 0.0023  0.0531  0.0326  196 THR   B CG2  
3067 N  N    . ALA   B 193 ? 0.1536 0.1750 0.1811 -0.0114 0.0121  0.0329  197 ALA   B N    
3068 C  CA   . ALA   B 193 ? 0.1482 0.1734 0.1721 -0.0151 0.0024  0.0248  197 ALA   B CA   
3069 C  C    . ALA   B 193 ? 0.1570 0.1692 0.1654 -0.0143 0.0029  0.0216  197 ALA   B C    
3070 O  O    . ALA   B 193 ? 0.1792 0.1738 0.1485 -0.0107 -0.0011 0.0133  197 ALA   B O    
3071 C  CB   . ALA   B 193 ? 0.1477 0.1630 0.1774 -0.0155 0.0051  0.0163  197 ALA   B CB   
3072 N  N    . GLU   B 194 ? 0.1626 0.1780 0.1643 -0.0056 0.0047  0.0195  198 GLU   B N    
3073 C  CA   . GLU   B 194 ? 0.1653 0.1827 0.1730 -0.0066 -0.0022 0.0155  198 GLU   B CA   
3074 C  C    . GLU   B 194 ? 0.1597 0.1758 0.1728 -0.0071 0.0019  0.0196  198 GLU   B C    
3075 O  O    . GLU   B 194 ? 0.1598 0.1782 0.1663 -0.0104 0.0040  0.0176  198 GLU   B O    
3076 C  CB   . GLU   B 194 ? 0.1801 0.2119 0.1748 -0.0140 -0.0062 0.0135  198 GLU   B CB   
3077 C  CG   . GLU   B 194 ? 0.2047 0.2372 0.2146 -0.0226 -0.0072 0.0013  198 GLU   B CG   
3078 C  CD   . GLU   B 194 ? 0.2449 0.2802 0.2373 -0.0287 -0.0233 -0.0023 198 GLU   B CD   
3079 O  OE1  . GLU   B 194 ? 0.3451 0.3726 0.2753 -0.0378 -0.0125 0.0134  198 GLU   B OE1  
3080 O  OE2  . GLU   B 194 ? 0.2704 0.2883 0.2970 -0.0183 -0.0359 -0.0318 198 GLU   B OE2  
3081 N  N    . GLY   B 195 ? 0.1651 0.1682 0.1780 -0.0019 0.0098  0.0229  199 GLY   B N    
3082 C  CA   . GLY   B 195 ? 0.1631 0.1770 0.1866 0.0058  0.0054  0.0243  199 GLY   B CA   
3083 C  C    . GLY   B 195 ? 0.1662 0.1776 0.1855 0.0035  0.0066  0.0315  199 GLY   B C    
3084 O  O    . GLY   B 195 ? 0.1929 0.1885 0.1911 0.0075  0.0066  0.0412  199 GLY   B O    
3085 N  N    . ASP   B 196 ? 0.1571 0.1699 0.1881 -0.0033 0.0020  0.0408  200 ASP   B N    
3086 C  CA   . ASP   B 196 ? 0.1641 0.1876 0.1923 -0.0100 -0.0039 0.0320  200 ASP   B CA   
3087 C  C    . ASP   B 196 ? 0.1587 0.1832 0.1717 -0.0051 -0.0093 0.0320  200 ASP   B C    
3088 O  O    . ASP   B 196 ? 0.1686 0.2023 0.1648 -0.0140 -0.0123 0.0368  200 ASP   B O    
3089 C  CB   . ASP   B 196 ? 0.1923 0.1955 0.2356 -0.0153 -0.0034 0.0263  200 ASP   B CB   
3090 C  CG   . ASP   B 196 ? 0.2089 0.2398 0.3200 -0.0146 0.0023  0.0066  200 ASP   B CG   
3091 O  OD1  . ASP   B 196 ? 0.2210 0.2707 0.3452 0.0041  0.0129  0.0018  200 ASP   B OD1  
3092 O  OD2  . ASP   B 196 ? 0.2648 0.2781 0.4821 -0.0387 0.0104  -0.0158 200 ASP   B OD2  
3093 N  N    . VAL   B 197 ? 0.1506 0.1682 0.1583 -0.0123 -0.0105 0.0322  201 VAL   B N    
3094 C  CA   . VAL   B 197 ? 0.1522 0.1644 0.1656 -0.0100 -0.0054 0.0303  201 VAL   B CA   
3095 C  C    . VAL   B 197 ? 0.1555 0.1660 0.1727 -0.0093 -0.0034 0.0275  201 VAL   B C    
3096 O  O    . VAL   B 197 ? 0.1639 0.1795 0.1714 -0.0064 -0.0055 0.0310  201 VAL   B O    
3097 C  CB   . VAL   B 197 ? 0.1586 0.1657 0.1855 -0.0089 -0.0100 0.0311  201 VAL   B CB   
3098 C  CG1  . VAL   B 197 ? 0.1604 0.1890 0.2108 -0.0066 -0.0156 0.0241  201 VAL   B CG1  
3099 C  CG2  . VAL   B 197 ? 0.1715 0.1715 0.1830 -0.0155 -0.0081 0.0168  201 VAL   B CG2  
3100 N  N    . LEU   B 198 ? 0.1624 0.1632 0.1740 -0.0175 -0.0007 0.0247  202 LEU   B N    
3101 C  CA   . LEU   B 198 ? 0.1795 0.1636 0.1841 -0.0168 0.0028  0.0272  202 LEU   B CA   
3102 C  C    . LEU   B 198 ? 0.1821 0.1753 0.1900 -0.0143 0.0040  0.0324  202 LEU   B C    
3103 O  O    . LEU   B 198 ? 0.2023 0.1817 0.2193 -0.0220 0.0113  0.0396  202 LEU   B O    
3104 C  CB   . LEU   B 198 ? 0.1938 0.1822 0.1940 -0.0179 0.0040  0.0182  202 LEU   B CB   
3105 C  CG   . LEU   B 198 ? 0.2102 0.2083 0.1957 -0.0138 -0.0035 0.0126  202 LEU   B CG   
3106 C  CD1  . LEU   B 198 ? 0.2184 0.2268 0.2057 -0.0188 0.0013  0.0073  202 LEU   B CD1  
3107 C  CD2  . LEU   B 198 ? 0.2093 0.2152 0.2051 -0.0034 -0.0126 0.0107  202 LEU   B CD2  
3108 N  N    . ALA   B 199 ? 0.1747 0.1816 0.1823 -0.0126 0.0022  0.0414  203 ALA   B N    
3109 C  CA   . ALA   B 199 ? 0.1750 0.1868 0.1952 -0.0061 -0.0055 0.0440  203 ALA   B CA   
3110 C  C    . ALA   B 199 ? 0.1681 0.1883 0.1901 -0.0063 -0.0058 0.0471  203 ALA   B C    
3111 O  O    . ALA   B 199 ? 0.1793 0.1920 0.1943 -0.0056 -0.0019 0.0493  203 ALA   B O    
3112 C  CB   . ALA   B 199 ? 0.1813 0.2004 0.2041 -0.0092 -0.0009 0.0456  203 ALA   B CB   
3113 N  N    . LEU   B 200 ? 0.1646 0.1868 0.1753 -0.0048 -0.0023 0.0377  204 LEU   B N    
3114 C  CA   . LEU   B 200 ? 0.1561 0.1991 0.1757 -0.0114 -0.0051 0.0356  204 LEU   B CA   
3115 C  C    . LEU   B 200 ? 0.1592 0.1990 0.1743 -0.0119 -0.0054 0.0373  204 LEU   B C    
3116 O  O    . LEU   B 200 ? 0.1773 0.2187 0.1778 -0.0130 0.0006  0.0494  204 LEU   B O    
3117 C  CB   . LEU   B 200 ? 0.1475 0.2050 0.1933 -0.0126 -0.0024 0.0284  204 LEU   B CB   
3118 C  CG   . LEU   B 200 ? 0.1470 0.2096 0.1987 -0.0129 0.0049  0.0256  204 LEU   B CG   
3119 C  CD1  . LEU   B 200 ? 0.1615 0.2228 0.2056 -0.0204 0.0030  0.0236  204 LEU   B CD1  
3120 C  CD2  . LEU   B 200 ? 0.1458 0.2097 0.2050 -0.0119 0.0129  0.0220  204 LEU   B CD2  
3121 N  N    . LEU   B 201 ? 0.1605 0.1926 0.1725 -0.0115 -0.0092 0.0374  205 LEU   B N    
3122 C  CA   . LEU   B 201 ? 0.1636 0.1952 0.1913 -0.0150 -0.0151 0.0406  205 LEU   B CA   
3123 C  C    . LEU   B 201 ? 0.1743 0.1995 0.2049 -0.0160 -0.0071 0.0456  205 LEU   B C    
3124 O  O    . LEU   B 201 ? 0.1828 0.2079 0.2136 -0.0107 0.0077  0.0524  205 LEU   B O    
3125 C  CB   . LEU   B 201 ? 0.1787 0.2023 0.2014 -0.0183 -0.0239 0.0411  205 LEU   B CB   
3126 C  CG   . LEU   B 201 ? 0.1916 0.2139 0.2225 -0.0311 -0.0227 0.0438  205 LEU   B CG   
3127 C  CD1  . LEU   B 201 ? 0.1933 0.2259 0.2449 -0.0280 -0.0251 0.0499  205 LEU   B CD1  
3128 C  CD2  . LEU   B 201 ? 0.2088 0.2316 0.2392 -0.0464 -0.0243 0.0378  205 LEU   B CD2  
3129 N  N    . SER   B 202 ? 0.1805 0.1949 0.2155 -0.0054 -0.0046 0.0500  206 SER   B N    
3130 C  CA   . SER   B 202 ? 0.1934 0.1978 0.2287 0.0007  -0.0021 0.0498  206 SER   B CA   
3131 C  C    . SER   B 202 ? 0.1892 0.2148 0.2274 -0.0030 -0.0005 0.0642  206 SER   B C    
3132 O  O    . SER   B 202 ? 0.2094 0.2190 0.2601 -0.0087 0.0016  0.0770  206 SER   B O    
3133 C  CB   . SER   B 202 ? 0.2056 0.2046 0.2357 0.0079  -0.0006 0.0420  206 SER   B CB   
3134 O  OG   . SER   B 202 ? 0.2446 0.2141 0.2469 0.0212  -0.0017 0.0373  206 SER   B OG   
3135 N  N    . ILE   B 203 ? 0.1888 0.2324 0.2167 -0.0069 -0.0011 0.0702  207 ILE   B N    
3136 C  CA   . ILE   B 203 ? 0.1962 0.2605 0.2165 -0.0081 -0.0023 0.0704  207 ILE   B CA   
3137 C  C    . ILE   B 203 ? 0.2070 0.2710 0.2070 -0.0029 -0.0001 0.0814  207 ILE   B C    
3138 O  O    . ILE   B 203 ? 0.2378 0.3078 0.2188 0.0098  -0.0012 0.1105  207 ILE   B O    
3139 C  CB   . ILE   B 203 ? 0.1977 0.2868 0.2158 -0.0115 -0.0103 0.0611  207 ILE   B CB   
3140 C  CG1  . ILE   B 203 ? 0.1995 0.2963 0.2177 -0.0107 -0.0117 0.0590  207 ILE   B CG1  
3141 C  CG2  . ILE   B 203 ? 0.2171 0.3045 0.2273 -0.0177 -0.0036 0.0526  207 ILE   B CG2  
3142 C  CD1  . ILE   B 203 ? 0.1841 0.3060 0.2250 -0.0156 -0.0090 0.0519  207 ILE   B CD1  
3143 N  N    . CYS   B 204 ? 0.1987 0.2625 0.2008 0.0005  0.0029  0.0761  208 CYS   B N    
3144 C  CA   . CYS   B 204 ? 0.2076 0.2662 0.2001 -0.0051 0.0039  0.0617  208 CYS   B CA   
3145 C  C    . CYS   B 204 ? 0.2182 0.2612 0.2220 -0.0034 0.0188  0.0725  208 CYS   B C    
3146 O  O    . CYS   B 204 ? 0.2324 0.2912 0.2467 -0.0251 0.0348  0.0573  208 CYS   B O    
3147 C  CB   . CYS   B 204 ? 0.2042 0.2615 0.1850 -0.0107 0.0039  0.0654  208 CYS   B CB   
3148 S  SG   . CYS   B 204 ? 0.2358 0.2851 0.1908 -0.0136 -0.0107 0.0420  208 CYS   B SG   
3149 N  N    . GLN   B 205 ? 0.2204 0.2551 0.2366 -0.0002 0.0199  0.0759  209 GLN   B N    
3150 C  CA   . GLN   B 205 ? 0.2224 0.2593 0.2673 0.0028  0.0193  0.0802  209 GLN   B CA   
3151 C  C    . GLN   B 205 ? 0.2518 0.2647 0.2968 0.0048  0.0168  0.0971  209 GLN   B C    
3152 O  O    . GLN   B 205 ? 0.2635 0.2592 0.3138 0.0005  0.0217  0.1087  209 GLN   B O    
3153 C  CB   . GLN   B 205 ? 0.2308 0.2604 0.2747 0.0000  0.0158  0.0758  209 GLN   B CB   
3154 C  CG   . GLN   B 205 ? 0.2317 0.2482 0.2844 0.0016  0.0177  0.0741  209 GLN   B CG   
3155 C  CD   . GLN   B 205 ? 0.2577 0.2427 0.2996 -0.0023 0.0162  0.0694  209 GLN   B CD   
3156 O  OE1  . GLN   B 205 ? 0.3012 0.2528 0.3109 -0.0122 0.0431  0.0524  209 GLN   B OE1  
3157 N  NE2  . GLN   B 205 ? 0.2845 0.2607 0.3065 -0.0198 0.0108  0.0644  209 GLN   B NE2  
3158 N  N    . TRP   B 206 ? 0.2562 0.2725 0.3012 0.0124  0.0068  0.1177  210 TRP   B N    
3159 C  CA   . TRP   B 206 ? 0.2871 0.3039 0.3125 0.0210  0.0029  0.1306  210 TRP   B CA   
3160 C  C    . TRP   B 206 ? 0.2894 0.3051 0.3237 0.0200  0.0106  0.1214  210 TRP   B C    
3161 O  O    . TRP   B 206 ? 0.3060 0.3039 0.3394 0.0209  0.0203  0.1305  210 TRP   B O    
3162 C  CB   . TRP   B 206 ? 0.3090 0.3418 0.3506 0.0331  -0.0179 0.1360  210 TRP   B CB   
3163 C  CG   . TRP   B 206 ? 0.3742 0.3939 0.3885 0.0403  -0.0402 0.1490  210 TRP   B CG   
3164 C  CD1  . TRP   B 206 ? 0.4270 0.4307 0.4497 0.0443  -0.0401 0.1216  210 TRP   B CD1  
3165 C  CD2  . TRP   B 206 ? 0.4385 0.4837 0.4202 0.0354  -0.0543 0.1228  210 TRP   B CD2  
3166 N  NE1  . TRP   B 206 ? 0.4487 0.4643 0.4535 0.0518  -0.0494 0.1227  210 TRP   B NE1  
3167 C  CE2  . TRP   B 206 ? 0.4712 0.4816 0.4532 0.0429  -0.0455 0.1226  210 TRP   B CE2  
3168 C  CE3  . TRP   B 206 ? 0.4996 0.5363 0.4462 0.0451  -0.0698 0.1120  210 TRP   B CE3  
3169 C  CZ2  . TRP   B 206 ? 0.5270 0.5582 0.4863 0.0356  -0.0623 0.0906  210 TRP   B CZ2  
3170 C  CZ3  . TRP   B 206 ? 0.5504 0.5831 0.4588 0.0340  -0.0793 0.1031  210 TRP   B CZ3  
3171 C  CH2  . TRP   B 206 ? 0.5469 0.5713 0.4989 0.0428  -0.0647 0.0871  210 TRP   B CH2  
3172 N  N    . ARG   B 207 ? 0.2600 0.3180 0.2938 0.0348  0.0168  0.1209  211 ARG   B N    
3173 C  CA   . ARG   B 207 ? 0.2717 0.3387 0.3194 0.0283  0.0260  0.1083  211 ARG   B CA   
3174 C  C    . ARG   B 207 ? 0.2577 0.3166 0.2858 0.0190  0.0222  0.0926  211 ARG   B C    
3175 O  O    . ARG   B 207 ? 0.2423 0.3366 0.2756 0.0004  0.0238  0.0764  211 ARG   B O    
3176 C  CB   . ARG   B 207 ? 0.2889 0.3653 0.3233 0.0382  0.0255  0.1112  211 ARG   B CB   
3177 C  CG   . ARG   B 207 ? 0.3176 0.3682 0.3659 0.0440  0.0357  0.1130  211 ARG   B CG   
3178 C  CD   . ARG   B 207 ? 0.3686 0.3777 0.4162 0.0470  0.0294  0.1028  211 ARG   B CD   
3179 N  N    . PRO   B 208 ? 0.2573 0.2930 0.2923 0.0110  0.0236  0.0806  212 PRO   B N    
3180 C  CA   . PRO   B 208 ? 0.2390 0.2905 0.2789 0.0047  0.0208  0.0801  212 PRO   B CA   
3181 C  C    . PRO   B 208 ? 0.2400 0.2675 0.2617 -0.0104 0.0255  0.0829  212 PRO   B C    
3182 O  O    . PRO   B 208 ? 0.2334 0.2561 0.2768 -0.0193 0.0161  0.0753  212 PRO   B O    
3183 C  CB   . PRO   B 208 ? 0.2527 0.3094 0.2854 0.0091  0.0157  0.0710  212 PRO   B CB   
3184 C  CG   . PRO   B 208 ? 0.2745 0.3127 0.3032 0.0072  0.0144  0.0646  212 PRO   B CG   
3185 C  CD   . PRO   B 208 ? 0.2758 0.3003 0.2992 0.0089  0.0161  0.0843  212 PRO   B CD   
3186 N  N    . GLN   B 209 ? 0.2473 0.2627 0.2789 -0.0182 0.0261  0.0914  213 GLN   B N    
3187 C  CA   . GLN   B 209 ? 0.2582 0.2897 0.2920 -0.0294 0.0369  0.0954  213 GLN   B CA   
3188 C  C    . GLN   B 209 ? 0.2407 0.3005 0.2829 -0.0223 0.0262  0.0908  213 GLN   B C    
3189 O  O    . GLN   B 209 ? 0.2168 0.3095 0.2753 -0.0103 0.0330  0.0966  213 GLN   B O    
3190 C  CB   . GLN   B 209 ? 0.2829 0.3008 0.3172 -0.0561 0.0406  0.0978  213 GLN   B CB   
3191 C  CG   . GLN   B 209 ? 0.3118 0.3249 0.3367 -0.0749 0.0431  0.0972  213 GLN   B CG   
3192 C  CD   . GLN   B 209 ? 0.3660 0.3450 0.4041 -0.0699 0.0355  0.0797  213 GLN   B CD   
3193 O  OE1  . GLN   B 209 ? 0.3930 0.3631 0.4017 -0.0373 0.0357  0.0893  213 GLN   B OE1  
3194 N  NE2  . GLN   B 209 ? 0.4252 0.4007 0.4814 -0.0846 0.0236  0.0657  213 GLN   B NE2  
3195 N  N    . ALA   B 210 ? 0.2417 0.3035 0.2774 -0.0154 0.0085  0.0820  214 ALA   B N    
3196 C  CA   . ALA   B 210 ? 0.2643 0.3232 0.2875 -0.0059 -0.0033 0.0600  214 ALA   B CA   
3197 C  C    . ALA   B 210 ? 0.2343 0.3184 0.2746 -0.0132 -0.0174 0.0532  214 ALA   B C    
3198 O  O    . ALA   B 210 ? 0.2524 0.3250 0.2911 -0.0188 -0.0368 0.0561  214 ALA   B O    
3199 C  CB   . ALA   B 210 ? 0.2783 0.3352 0.3020 -0.0003 -0.0190 0.0527  214 ALA   B CB   
3200 N  N    . LEU   B 211 ? 0.2264 0.2900 0.2682 -0.0196 -0.0108 0.0519  215 LEU   B N    
3201 C  CA   . LEU   B 211 ? 0.2276 0.2839 0.2602 -0.0320 -0.0141 0.0437  215 LEU   B CA   
3202 C  C    . LEU   B 211 ? 0.2199 0.2679 0.2491 -0.0381 -0.0125 0.0440  215 LEU   B C    
3203 O  O    . LEU   B 211 ? 0.2185 0.2712 0.2593 -0.0249 -0.0139 0.0265  215 LEU   B O    
3204 C  CB   . LEU   B 211 ? 0.2369 0.2989 0.2573 -0.0364 -0.0077 0.0570  215 LEU   B CB   
3205 C  CG   . LEU   B 211 ? 0.2545 0.3047 0.2662 -0.0433 -0.0024 0.0501  215 LEU   B CG   
3206 C  CD1  . LEU   B 211 ? 0.2824 0.3163 0.2523 -0.0323 -0.0014 0.0464  215 LEU   B CD1  
3207 C  CD2  . LEU   B 211 ? 0.2755 0.3250 0.2605 -0.0495 -0.0097 0.0439  215 LEU   B CD2  
3208 N  N    . LEU   B 212 ? 0.2058 0.2679 0.2452 -0.0269 -0.0122 0.0487  216 LEU   B N    
3209 C  CA   . LEU   B 212 ? 0.1975 0.2551 0.2397 -0.0343 -0.0153 0.0434  216 LEU   B CA   
3210 C  C    . LEU   B 212 ? 0.2142 0.2600 0.2380 -0.0399 -0.0222 0.0378  216 LEU   B C    
3211 O  O    . LEU   B 212 ? 0.2273 0.2536 0.2349 -0.0387 -0.0305 0.0343  216 LEU   B O    
3212 C  CB   . LEU   B 212 ? 0.1907 0.2415 0.2315 -0.0314 -0.0024 0.0371  216 LEU   B CB   
3213 C  CG   . LEU   B 212 ? 0.1888 0.2454 0.2206 -0.0301 -0.0067 0.0384  216 LEU   B CG   
3214 C  CD1  . LEU   B 212 ? 0.1877 0.2510 0.2261 -0.0274 -0.0065 0.0388  216 LEU   B CD1  
3215 C  CD2  . LEU   B 212 ? 0.1948 0.2467 0.2305 -0.0293 -0.0049 0.0340  216 LEU   B CD2  
3216 N  N    . ARG   B 213 ? 0.2397 0.2793 0.2488 -0.0253 -0.0185 0.0483  217 ARG   B N    
3217 C  CA   . ARG   B 213 ? 0.2664 0.3024 0.2623 -0.0248 -0.0041 0.0405  217 ARG   B CA   
3218 C  C    . ARG   B 213 ? 0.2770 0.3027 0.2521 -0.0125 -0.0176 0.0265  217 ARG   B C    
3219 O  O    . ARG   B 213 ? 0.2840 0.3054 0.2324 -0.0012 -0.0152 0.0172  217 ARG   B O    
3220 C  CB   . ARG   B 213 ? 0.3195 0.3368 0.2973 -0.0128 -0.0024 0.0657  217 ARG   B CB   
3221 C  CG   . ARG   B 213 ? 0.3810 0.3973 0.3524 -0.0341 0.0077  0.0674  217 ARG   B CG   
3222 C  CD   . ARG   B 213 ? 0.4530 0.4444 0.3794 -0.0272 0.0082  0.1004  217 ARG   B CD   
3223 N  NE   . ARG   B 213 ? 0.5128 0.4922 0.4451 -0.0366 0.0055  0.0802  217 ARG   B NE   
3224 C  CZ   . ARG   B 213 ? 0.5715 0.5215 0.4800 -0.0485 -0.0043 0.0771  217 ARG   B CZ   
3225 N  NH1  . ARG   B 213 ? 0.6065 0.5660 0.4986 -0.0440 -0.0277 0.0629  217 ARG   B NH1  
3226 N  NH2  . ARG   B 213 ? 0.5764 0.5650 0.4805 -0.0363 -0.0042 0.0880  217 ARG   B NH2  
3227 N  N    . TRP   B 214 ? 0.2706 0.2860 0.2233 -0.0242 -0.0133 0.0267  218 TRP   B N    
3228 C  CA   . TRP   B 214 ? 0.2870 0.3136 0.2324 -0.0350 -0.0322 0.0218  218 TRP   B CA   
3229 C  C    . TRP   B 214 ? 0.2782 0.2920 0.2504 -0.0301 -0.0399 0.0070  218 TRP   B C    
3230 O  O    . TRP   B 214 ? 0.3222 0.2943 0.2440 -0.0304 -0.0673 0.0052  218 TRP   B O    
3231 C  CB   . TRP   B 214 ? 0.3028 0.3281 0.2655 -0.0305 -0.0358 0.0299  218 TRP   B CB   
3232 C  CG   . TRP   B 214 ? 0.3368 0.3808 0.2934 -0.0487 -0.0354 0.0217  218 TRP   B CG   
3233 C  CD1  . TRP   B 214 ? 0.3466 0.4179 0.3083 -0.0583 -0.0447 0.0236  218 TRP   B CD1  
3234 C  CD2  . TRP   B 214 ? 0.3542 0.4031 0.3131 -0.0540 -0.0193 0.0285  218 TRP   B CD2  
3235 N  NE1  . TRP   B 214 ? 0.3774 0.4287 0.3386 -0.0723 -0.0334 0.0237  218 TRP   B NE1  
3236 C  CE2  . TRP   B 214 ? 0.3621 0.4153 0.3276 -0.0741 -0.0292 0.0328  218 TRP   B CE2  
3237 C  CE3  . TRP   B 214 ? 0.3437 0.4036 0.3159 -0.0621 -0.0018 0.0388  218 TRP   B CE3  
3238 C  CZ2  . TRP   B 214 ? 0.3772 0.4303 0.3401 -0.0837 -0.0102 0.0309  218 TRP   B CZ2  
3239 C  CZ3  . TRP   B 214 ? 0.3509 0.4058 0.3386 -0.0624 0.0105  0.0282  218 TRP   B CZ3  
3240 C  CH2  . TRP   B 214 ? 0.3501 0.4151 0.3422 -0.0729 -0.0029 0.0377  218 TRP   B CH2  
3241 N  N    . VAL   B 215 ? 0.2524 0.2715 0.2368 -0.0210 -0.0354 0.0128  219 VAL   B N    
3242 C  CA   . VAL   B 215 ? 0.2651 0.2684 0.2281 -0.0337 -0.0269 0.0110  219 VAL   B CA   
3243 C  C    . VAL   B 215 ? 0.2802 0.2723 0.2141 -0.0214 -0.0332 0.0107  219 VAL   B C    
3244 O  O    . VAL   B 215 ? 0.3349 0.2745 0.1905 -0.0192 -0.0390 0.0076  219 VAL   B O    
3245 C  CB   . VAL   B 215 ? 0.2612 0.2718 0.2314 -0.0359 -0.0208 0.0027  219 VAL   B CB   
3246 C  CG1  . VAL   B 215 ? 0.2684 0.2738 0.2447 -0.0294 -0.0191 0.0018  219 VAL   B CG1  
3247 C  CG2  . VAL   B 215 ? 0.2681 0.2757 0.2552 -0.0325 -0.0193 0.0035  219 VAL   B CG2  
3248 N  N    . ASP   B 216 ? 0.2942 0.2827 0.2059 -0.0225 -0.0230 0.0096  220 ASP   B N    
3249 C  CA   . ASP   B 216 ? 0.2973 0.2901 0.2228 -0.0017 -0.0291 0.0107  220 ASP   B CA   
3250 C  C    . ASP   B 216 ? 0.3514 0.3061 0.2455 0.0131  -0.0312 -0.0053 220 ASP   B C    
3251 O  O    . ASP   B 216 ? 0.4007 0.3096 0.2347 0.0380  -0.0228 -0.0182 220 ASP   B O    
3252 C  CB   . ASP   B 216 ? 0.2910 0.3097 0.2445 -0.0046 -0.0113 0.0133  220 ASP   B CB   
3253 C  CG   . ASP   B 216 ? 0.2630 0.3188 0.2623 -0.0050 -0.0084 0.0118  220 ASP   B CG   
3254 O  OD1  . ASP   B 216 ? 0.2368 0.3392 0.2389 -0.0055 0.0064  -0.0024 220 ASP   B OD1  
3255 O  OD2  . ASP   B 216 ? 0.2639 0.3379 0.2825 -0.0263 0.0050  0.0182  220 ASP   B OD2  
3256 N  N    . ALA   B 217 ? 0.3793 0.3173 0.2329 -0.0023 -0.0416 -0.0054 221 ALA   B N    
3257 C  CA   . ALA   B 217 ? 0.4102 0.3416 0.2507 -0.0113 -0.0458 -0.0234 221 ALA   B CA   
3258 C  C    . ALA   B 217 ? 0.4161 0.3502 0.2512 -0.0273 -0.0450 -0.0390 221 ALA   B C    
3259 O  O    . ALA   B 217 ? 0.4636 0.3843 0.2558 -0.0320 -0.0020 -0.0671 221 ALA   B O    
3260 C  CB   . ALA   B 217 ? 0.4288 0.3470 0.2522 -0.0031 -0.0568 -0.0179 221 ALA   B CB   
3261 N  N    . HIS   B 218 ? 0.3599 0.3421 0.2441 -0.0412 -0.0594 -0.0251 222 HIS   B N    
3262 C  CA   . HIS   B 218 ? 0.3481 0.3588 0.2858 -0.0502 -0.0709 -0.0308 222 HIS   B CA   
3263 C  C    . HIS   B 218 ? 0.2830 0.3259 0.2617 -0.0523 -0.0348 -0.0429 222 HIS   B C    
3264 O  O    . HIS   B 218 ? 0.2836 0.3532 0.2903 -0.0616 -0.0217 -0.0478 222 HIS   B O    
3265 C  CB   . HIS   B 218 ? 0.3757 0.3890 0.3286 -0.0475 -0.1045 -0.0274 222 HIS   B CB   
3266 C  CG   . HIS   B 218 ? 0.4439 0.4321 0.3306 -0.0511 -0.1357 -0.0230 222 HIS   B CG   
3267 N  ND1  . HIS   B 218 ? 0.4754 0.4570 0.3499 -0.0525 -0.1499 -0.0116 222 HIS   B ND1  
3268 C  CD2  . HIS   B 218 ? 0.4911 0.4477 0.3438 -0.0632 -0.1575 -0.0234 222 HIS   B CD2  
3269 C  CE1  . HIS   B 218 ? 0.4921 0.4572 0.3723 -0.0574 -0.1755 0.0047  222 HIS   B CE1  
3270 N  NE2  . HIS   B 218 ? 0.5206 0.4696 0.3669 -0.0512 -0.1745 -0.0129 222 HIS   B NE2  
3271 N  N    . ALA   B 219 ? 0.2700 0.3116 0.2302 -0.0434 -0.0176 -0.0339 223 ALA   B N    
3272 C  CA   . ALA   B 219 ? 0.2606 0.2832 0.2313 -0.0442 -0.0054 -0.0309 223 ALA   B CA   
3273 C  C    . ALA   B 219 ? 0.2584 0.2873 0.2140 -0.0472 0.0133  -0.0334 223 ALA   B C    
3274 O  O    . ALA   B 219 ? 0.2743 0.3066 0.2231 -0.0470 0.0334  -0.0369 223 ALA   B O    
3275 C  CB   . ALA   B 219 ? 0.2827 0.2849 0.2381 -0.0482 -0.0207 -0.0204 223 ALA   B CB   
3276 N  N    . ARG   B 220 ? 0.2508 0.2828 0.2074 -0.0491 0.0240  -0.0443 224 ARG   B N    
3277 C  CA   . ARG   B 220 ? 0.2770 0.2930 0.2337 -0.0453 0.0296  -0.0564 224 ARG   B CA   
3278 C  C    . ARG   B 220 ? 0.2435 0.2720 0.2343 -0.0371 0.0361  -0.0711 224 ARG   B C    
3279 O  O    . ARG   B 220 ? 0.2214 0.2447 0.2151 -0.0304 0.0425  -0.0625 224 ARG   B O    
3280 C  CB   . ARG   B 220 ? 0.2976 0.3286 0.2751 -0.0570 0.0069  -0.0535 224 ARG   B CB   
3281 C  CG   . ARG   B 220 ? 0.3736 0.3530 0.3317 -0.0493 0.0153  -0.0562 224 ARG   B CG   
3282 C  CD   . ARG   B 220 ? 0.4005 0.3673 0.3819 -0.0613 0.0072  -0.0612 224 ARG   B CD   
3283 N  NE   . ARG   B 220 ? 0.4662 0.3815 0.4466 -0.0604 0.0250  -0.0430 224 ARG   B NE   
3284 C  CZ   . ARG   B 220 ? 0.4987 0.4198 0.4876 -0.0503 -0.0088 -0.0562 224 ARG   B CZ   
3285 N  NH1  . ARG   B 220 ? 0.5211 0.4742 0.5409 -0.0234 -0.0159 -0.0422 224 ARG   B NH1  
3286 N  NH2  . ARG   B 220 ? 0.5556 0.4286 0.5046 -0.0463 0.0028  -0.0556 224 ARG   B NH2  
3287 N  N    . PRO   B 221 ? 0.2525 0.2867 0.2393 -0.0223 0.0501  -0.0988 225 PRO   B N    
3288 C  CA   . PRO   B 221 ? 0.2474 0.2846 0.2623 -0.0213 0.0499  -0.0899 225 PRO   B CA   
3289 C  C    . PRO   B 221 ? 0.2303 0.2539 0.2611 -0.0257 0.0311  -0.0751 225 PRO   B C    
3290 O  O    . PRO   B 221 ? 0.2311 0.2479 0.2475 -0.0386 0.0189  -0.0602 225 PRO   B O    
3291 C  CB   . PRO   B 221 ? 0.2666 0.2994 0.2943 -0.0074 0.0551  -0.0941 225 PRO   B CB   
3292 C  CG   . PRO   B 221 ? 0.2806 0.3292 0.2836 -0.0024 0.0597  -0.1002 225 PRO   B CG   
3293 C  CD   . PRO   B 221 ? 0.2791 0.3247 0.2618 -0.0064 0.0622  -0.1030 225 PRO   B CD   
3294 N  N    . PHE   B 222 ? 0.2208 0.2395 0.2573 -0.0311 0.0348  -0.0688 226 PHE   B N    
3295 C  CA   . PHE   B 222 ? 0.2203 0.2604 0.2653 -0.0245 0.0372  -0.0674 226 PHE   B CA   
3296 C  C    . PHE   B 222 ? 0.2404 0.2684 0.2923 -0.0393 0.0519  -0.0576 226 PHE   B C    
3297 O  O    . PHE   B 222 ? 0.2334 0.2876 0.3075 -0.0483 0.0424  -0.0699 226 PHE   B O    
3298 C  CB   . PHE   B 222 ? 0.2270 0.2663 0.2647 -0.0166 0.0228  -0.0627 226 PHE   B CB   
3299 C  CG   . PHE   B 222 ? 0.2210 0.2774 0.2713 -0.0116 0.0236  -0.0715 226 PHE   B CG   
3300 C  CD1  . PHE   B 222 ? 0.2366 0.3161 0.2952 -0.0083 0.0225  -0.0665 226 PHE   B CD1  
3301 C  CD2  . PHE   B 222 ? 0.2322 0.2998 0.2896 -0.0013 0.0339  -0.0575 226 PHE   B CD2  
3302 C  CE1  . PHE   B 222 ? 0.2330 0.3276 0.2982 -0.0024 0.0246  -0.0649 226 PHE   B CE1  
3303 C  CE2  . PHE   B 222 ? 0.2425 0.3097 0.3102 -0.0012 0.0388  -0.0452 226 PHE   B CE2  
3304 C  CZ   . PHE   B 222 ? 0.2360 0.3188 0.3070 0.0005  0.0379  -0.0665 226 PHE   B CZ   
3305 N  N    . GLY   B 223 ? 0.2553 0.2622 0.3321 -0.0444 0.0560  -0.0568 227 GLY   B N    
3306 C  CA   . GLY   B 223 ? 0.2973 0.2664 0.3472 -0.0340 0.0723  -0.0629 227 GLY   B CA   
3307 C  C    . GLY   B 223 ? 0.3141 0.2683 0.3582 -0.0531 0.0722  -0.0777 227 GLY   B C    
3308 O  O    . GLY   B 223 ? 0.3739 0.2696 0.4134 -0.0587 0.0699  -0.0646 227 GLY   B O    
3309 N  N    . THR   B 224 ? 0.3190 0.2781 0.3210 -0.0636 0.0747  -0.0916 228 THR   B N    
3310 C  CA   . THR   B 224 ? 0.3351 0.3159 0.3047 -0.0740 0.0728  -0.1039 228 THR   B CA   
3311 C  C    . THR   B 224 ? 0.3248 0.3032 0.2542 -0.0741 0.0589  -0.1202 228 THR   B C    
3312 O  O    . THR   B 224 ? 0.3317 0.3336 0.2613 -0.0956 0.0458  -0.1176 228 THR   B O    
3313 C  CB   . THR   B 224 ? 0.3441 0.3638 0.3090 -0.0890 0.0736  -0.0943 228 THR   B CB   
3314 O  OG1  . THR   B 224 ? 0.3601 0.3754 0.3112 -0.0982 0.0577  -0.0691 228 THR   B OG1  
3315 C  CG2  . THR   B 224 ? 0.3404 0.3834 0.3346 -0.0842 0.0666  -0.1087 228 THR   B CG2  
3316 N  N    . ILE   B 225 ? 0.3128 0.2690 0.2401 -0.0672 0.0614  -0.1076 229 ILE   B N    
3317 C  CA   . ILE   B 225 ? 0.3140 0.2604 0.2396 -0.0670 0.0648  -0.0927 229 ILE   B CA   
3318 C  C    . ILE   B 225 ? 0.3164 0.2690 0.2341 -0.0600 0.0637  -0.0830 229 ILE   B C    
3319 O  O    . ILE   B 225 ? 0.3207 0.2955 0.2753 -0.0533 0.0513  -0.0634 229 ILE   B O    
3320 C  CB   . ILE   B 225 ? 0.3150 0.2526 0.2282 -0.0675 0.0677  -0.0831 229 ILE   B CB   
3321 C  CG1  . ILE   B 225 ? 0.3047 0.2617 0.2368 -0.0690 0.0725  -0.0731 229 ILE   B CG1  
3322 C  CG2  . ILE   B 225 ? 0.3153 0.2532 0.2394 -0.0694 0.0707  -0.0838 229 ILE   B CG2  
3323 C  CD1  . ILE   B 225 ? 0.3144 0.2666 0.2316 -0.0633 0.0718  -0.0680 229 ILE   B CD1  
3324 N  N    . ARG   B 226 ? 0.3207 0.2833 0.2363 -0.0619 0.0627  -0.0827 230 ARG   B N    
3325 C  CA   . ARG   B 226 ? 0.3242 0.2769 0.2460 -0.0559 0.0679  -0.0794 230 ARG   B CA   
3326 C  C    . ARG   B 226 ? 0.2834 0.2476 0.2413 -0.0484 0.0593  -0.0696 230 ARG   B C    
3327 O  O    . ARG   B 226 ? 0.2643 0.2582 0.2310 -0.0380 0.0512  -0.0690 230 ARG   B O    
3328 C  CB   . ARG   B 226 ? 0.3640 0.3128 0.2804 -0.0755 0.0538  -0.0811 230 ARG   B CB   
3329 C  CG   . ARG   B 226 ? 0.4148 0.3561 0.3042 -0.0714 0.0631  -0.0823 230 ARG   B CG   
3330 C  CD   . ARG   B 226 ? 0.4263 0.3788 0.3278 -0.0849 0.0522  -0.0920 230 ARG   B CD   
3331 N  N    . PRO   B 227 ? 0.2715 0.2465 0.2598 -0.0298 0.0521  -0.0676 231 PRO   B N    
3332 C  CA   . PRO   B 227 ? 0.2628 0.2281 0.2425 -0.0339 0.0407  -0.0622 231 PRO   B CA   
3333 C  C    . PRO   B 227 ? 0.2564 0.2239 0.2343 -0.0346 0.0388  -0.0614 231 PRO   B C    
3334 O  O    . PRO   B 227 ? 0.2583 0.2612 0.2395 -0.0545 0.0366  -0.0682 231 PRO   B O    
3335 C  CB   . PRO   B 227 ? 0.2844 0.2272 0.2696 -0.0308 0.0426  -0.0561 231 PRO   B CB   
3336 C  CG   . PRO   B 227 ? 0.3150 0.2513 0.2872 -0.0156 0.0566  -0.0561 231 PRO   B CG   
3337 C  CD   . PRO   B 227 ? 0.2959 0.2478 0.2799 -0.0193 0.0608  -0.0633 231 PRO   B CD   
3338 N  N    . MET   B 228 ? 0.2390 0.2075 0.2232 -0.0350 0.0260  -0.0560 232 MET   B N    
3339 C  CA   . MET   B 228 ? 0.2336 0.2111 0.2219 -0.0357 0.0138  -0.0379 232 MET   B CA   
3340 C  C    . MET   B 228 ? 0.2540 0.1962 0.2415 -0.0256 0.0109  -0.0438 232 MET   B C    
3341 O  O    . MET   B 228 ? 0.2936 0.2318 0.2779 -0.0363 -0.0098 -0.0617 232 MET   B O    
3342 C  CB   . MET   B 228 ? 0.2207 0.2078 0.2103 -0.0361 0.0102  -0.0244 232 MET   B CB   
3343 C  CG   . MET   B 228 ? 0.2236 0.2249 0.2046 -0.0370 -0.0026 -0.0132 232 MET   B CG   
3344 S  SD   . MET   B 228 ? 0.2000 0.2428 0.1839 -0.0251 -0.0015 -0.0010 232 MET   B SD   
3345 C  CE   . MET   B 228 ? 0.2015 0.2225 0.1762 -0.0283 -0.0091 -0.0269 232 MET   B CE   
3346 N  N    . TYR   B 229 ? 0.2725 0.1865 0.2614 -0.0171 0.0273  -0.0356 233 TYR   B N    
3347 C  CA   . TYR   B 229 ? 0.3004 0.1917 0.2678 -0.0203 0.0276  -0.0274 233 TYR   B CA   
3348 C  C    . TYR   B 229 ? 0.3354 0.2187 0.3155 -0.0036 0.0206  -0.0237 233 TYR   B C    
3349 O  O    . TYR   B 229 ? 0.3455 0.2004 0.2880 0.0107  0.0278  -0.0311 233 TYR   B O    
3350 C  CB   . TYR   B 229 ? 0.2817 0.1910 0.2727 -0.0131 0.0218  -0.0195 233 TYR   B CB   
3351 C  CG   . TYR   B 229 ? 0.2638 0.1772 0.2420 0.0043  0.0269  -0.0059 233 TYR   B CG   
3352 C  CD1  . TYR   B 229 ? 0.2669 0.1771 0.2433 0.0197  0.0234  -0.0100 233 TYR   B CD1  
3353 C  CD2  . TYR   B 229 ? 0.2532 0.1749 0.2203 0.0076  0.0247  0.0029  233 TYR   B CD2  
3354 C  CE1  . TYR   B 229 ? 0.2595 0.1800 0.2245 0.0264  0.0276  0.0035  233 TYR   B CE1  
3355 C  CE2  . TYR   B 229 ? 0.2517 0.1805 0.2125 0.0156  0.0319  0.0021  233 TYR   B CE2  
3356 C  CZ   . TYR   B 229 ? 0.2550 0.1742 0.2175 0.0234  0.0265  0.0000  233 TYR   B CZ   
3357 O  OH   . TYR   B 229 ? 0.2554 0.2066 0.1960 0.0284  0.0279  0.0069  233 TYR   B OH   
3358 N  N    . GLY   B 230 ? 0.3898 0.2362 0.3784 -0.0136 -0.0057 -0.0015 234 GLY   B N    
3359 C  CA   . GLY   B 230 ? 0.4191 0.2770 0.3987 0.0034  -0.0143 0.0066  234 GLY   B CA   
3360 C  C    . GLY   B 230 ? 0.4402 0.3202 0.4050 0.0003  -0.0110 0.0125  234 GLY   B C    
3361 O  O    . GLY   B 230 ? 0.4451 0.3542 0.4035 0.0229  -0.0015 0.0145  234 GLY   B O    
3362 N  N    . VAL   B 231 ? 0.4649 0.3338 0.3836 0.0226  -0.0083 0.0134  235 VAL   B N    
3363 C  CA   . VAL   B 231 ? 0.4926 0.3490 0.3941 0.0251  -0.0069 0.0265  235 VAL   B CA   
3364 C  C    . VAL   B 231 ? 0.5330 0.3973 0.3940 0.0080  -0.0088 0.0199  235 VAL   B C    
3365 O  O    . VAL   B 231 ? 0.5248 0.4240 0.3826 -0.0061 0.0031  0.0294  235 VAL   B O    
3366 C  CB   . VAL   B 231 ? 0.5110 0.3603 0.4105 0.0425  -0.0079 0.0356  235 VAL   B CB   
3367 C  CG1  . VAL   B 231 ? 0.5111 0.3702 0.4223 0.0396  -0.0095 0.0260  235 VAL   B CG1  
3368 C  CG2  . VAL   B 231 ? 0.5131 0.3708 0.4253 0.0503  -0.0033 0.0400  235 VAL   B CG2  
3369 N  N    . THR   B 232 ? 0.5938 0.4291 0.3949 0.0122  -0.0102 0.0177  236 THR   B N    
3370 C  CA   . THR   B 232 ? 0.6303 0.4608 0.4239 0.0204  -0.0144 0.0064  236 THR   B CA   
3371 C  C    . THR   B 232 ? 0.6616 0.4462 0.4221 0.0179  -0.0061 0.0412  236 THR   B C    
3372 O  O    . THR   B 232 ? 0.6877 0.4450 0.3352 0.0064  -0.0391 0.0558  236 THR   B O    
3373 C  CB   . THR   B 232 ? 0.6706 0.5020 0.4541 0.0227  0.0063  -0.0048 236 THR   B CB   
3374 O  OG1  . THR   B 232 ? 0.7014 0.5616 0.4715 -0.0068 0.0348  -0.0048 236 THR   B OG1  
3375 C  CG2  . THR   B 232 ? 0.6707 0.5031 0.4780 0.0348  0.0031  -0.0154 236 THR   B CG2  
3376 N  N    . LEU   C 2   ? 0.3650 0.4190 0.3198 -0.0550 0.0168  0.0463  6   LEU   C N    
3377 C  CA   . LEU   C 2   ? 0.3665 0.3943 0.3025 -0.0572 -0.0006 0.0308  6   LEU   C CA   
3378 C  C    . LEU   C 2   ? 0.3750 0.3914 0.3270 -0.0501 -0.0018 0.0316  6   LEU   C C    
3379 O  O    . LEU   C 2   ? 0.4109 0.3999 0.4000 -0.0294 0.0108  0.0742  6   LEU   C O    
3380 C  CB   . LEU   C 2   ? 0.3716 0.3947 0.2893 -0.0506 -0.0064 0.0253  6   LEU   C CB   
3381 C  CG   . LEU   C 2   ? 0.3745 0.3942 0.2948 -0.0608 -0.0044 0.0121  6   LEU   C CG   
3382 C  CD1  . LEU   C 2   ? 0.3772 0.4165 0.2962 -0.0618 -0.0134 0.0032  6   LEU   C CD1  
3383 C  CD2  . LEU   C 2   ? 0.3923 0.3880 0.3069 -0.0640 -0.0066 0.0141  6   LEU   C CD2  
3384 N  N    . PRO   C 3   ? 0.3692 0.3960 0.3140 -0.0436 -0.0002 0.0324  7   PRO   C N    
3385 C  CA   . PRO   C 3   ? 0.3782 0.4021 0.3179 -0.0307 -0.0140 0.0322  7   PRO   C CA   
3386 C  C    . PRO   C 3   ? 0.3751 0.4177 0.2838 -0.0094 -0.0281 0.0375  7   PRO   C C    
3387 O  O    . PRO   C 3   ? 0.4123 0.4512 0.2990 0.0216  -0.0084 0.0584  7   PRO   C O    
3388 C  CB   . PRO   C 3   ? 0.3769 0.4020 0.3307 -0.0456 -0.0184 0.0220  7   PRO   C CB   
3389 C  CG   . PRO   C 3   ? 0.3708 0.3886 0.3336 -0.0509 -0.0184 0.0132  7   PRO   C CG   
3390 C  CD   . PRO   C 3   ? 0.3761 0.3958 0.3352 -0.0466 -0.0110 0.0162  7   PRO   C CD   
3391 N  N    . HIS   C 4   ? 0.3324 0.4053 0.2773 -0.0143 -0.0353 0.0341  8   HIS   C N    
3392 C  CA   . HIS   C 4   ? 0.3168 0.3953 0.2733 -0.0201 -0.0295 0.0344  8   HIS   C CA   
3393 C  C    . HIS   C 4   ? 0.3237 0.3915 0.2483 -0.0356 -0.0188 0.0184  8   HIS   C C    
3394 O  O    . HIS   C 4   ? 0.3484 0.3936 0.2577 -0.0371 -0.0110 0.0152  8   HIS   C O    
3395 C  CB   . HIS   C 4   ? 0.3417 0.3935 0.2732 -0.0123 -0.0177 0.0404  8   HIS   C CB   
3396 C  CG   . HIS   C 4   ? 0.3571 0.4147 0.2844 -0.0338 -0.0167 0.0341  8   HIS   C CG   
3397 N  ND1  . HIS   C 4   ? 0.3963 0.4171 0.3071 -0.0353 -0.0200 0.0545  8   HIS   C ND1  
3398 C  CD2  . HIS   C 4   ? 0.3837 0.4274 0.3035 -0.0341 -0.0104 0.0389  8   HIS   C CD2  
3399 C  CE1  . HIS   C 4   ? 0.3881 0.4284 0.3147 -0.0453 -0.0184 0.0480  8   HIS   C CE1  
3400 N  NE2  . HIS   C 4   ? 0.3720 0.4328 0.3165 -0.0388 -0.0142 0.0326  8   HIS   C NE2  
3401 N  N    . GLY   C 5   ? 0.2830 0.3395 0.2329 -0.0515 -0.0263 0.0137  9   GLY   C N    
3402 C  CA   . GLY   C 5   ? 0.2797 0.3100 0.1921 -0.0588 -0.0268 0.0356  9   GLY   C CA   
3403 C  C    . GLY   C 5   ? 0.2537 0.2727 0.1642 -0.0699 -0.0211 0.0257  9   GLY   C C    
3404 O  O    . GLY   C 5   ? 0.2739 0.2932 0.1901 -0.0834 -0.0343 0.0468  9   GLY   C O    
3405 N  N    . HIS   C 6   ? 0.2252 0.2190 0.1353 -0.0636 0.0039  0.0139  10  HIS   C N    
3406 C  CA   . HIS   C 6   ? 0.2224 0.1967 0.1245 -0.0585 0.0170  0.0071  10  HIS   C CA   
3407 C  C    . HIS   C 6   ? 0.2230 0.1911 0.1222 -0.0524 0.0128  0.0038  10  HIS   C C    
3408 O  O    . HIS   C 6   ? 0.2133 0.1881 0.1349 -0.0404 0.0118  0.0052  10  HIS   C O    
3409 C  CB   . HIS   C 6   ? 0.2269 0.2105 0.1335 -0.0485 0.0178  0.0011  10  HIS   C CB   
3410 C  CG   . HIS   C 6   ? 0.2434 0.2137 0.1472 -0.0415 0.0298  -0.0027 10  HIS   C CG   
3411 N  ND1  . HIS   C 6   ? 0.2568 0.2244 0.1593 -0.0312 0.0382  -0.0092 10  HIS   C ND1  
3412 C  CD2  . HIS   C 6   ? 0.2478 0.2068 0.1680 -0.0428 0.0324  -0.0003 10  HIS   C CD2  
3413 C  CE1  . HIS   C 6   ? 0.2721 0.2219 0.1750 -0.0418 0.0499  -0.0019 10  HIS   C CE1  
3414 N  NE2  . HIS   C 6   ? 0.2711 0.2105 0.1774 -0.0406 0.0408  -0.0041 10  HIS   C NE2  
3415 N  N    . MET   C 7   ? 0.2183 0.1857 0.1217 -0.0520 0.0097  0.0001  11  MET   C N    
3416 C  CA   . MET   C 7   ? 0.2024 0.1795 0.1256 -0.0466 0.0081  0.0068  11  MET   C CA   
3417 C  C    . MET   C 7   ? 0.1947 0.1711 0.1359 -0.0373 0.0089  0.0019  11  MET   C C    
3418 O  O    . MET   C 7   ? 0.1972 0.1714 0.1452 -0.0311 0.0046  -0.0016 11  MET   C O    
3419 C  CB   . MET   C 7   ? 0.2070 0.1860 0.1297 -0.0558 0.0110  0.0115  11  MET   C CB   
3420 C  CG   . MET   C 7   ? 0.2150 0.1940 0.1303 -0.0543 0.0071  0.0179  11  MET   C CG   
3421 S  SD   . MET   C 7   ? 0.2223 0.2240 0.1674 -0.0450 -0.0045 0.0307  11  MET   C SD   
3422 C  CE   . MET   C 7   ? 0.2512 0.2399 0.1594 -0.0346 -0.0124 0.0256  11  MET   C CE   
3423 N  N    . GLN   C 8   ? 0.1833 0.1706 0.1307 -0.0296 0.0122  0.0022  12  GLN   C N    
3424 C  CA   . GLN   C 8   ? 0.1809 0.1628 0.1330 -0.0282 0.0124  0.0086  12  GLN   C CA   
3425 C  C    . GLN   C 8   ? 0.1762 0.1596 0.1320 -0.0293 0.0102  0.0090  12  GLN   C C    
3426 O  O    . GLN   C 8   ? 0.1783 0.1541 0.1413 -0.0256 0.0102  0.0202  12  GLN   C O    
3427 C  CB   . GLN   C 8   ? 0.1860 0.1609 0.1388 -0.0268 0.0094  0.0098  12  GLN   C CB   
3428 C  CG   . GLN   C 8   ? 0.1854 0.1570 0.1430 -0.0243 0.0089  0.0118  12  GLN   C CG   
3429 C  CD   . GLN   C 8   ? 0.1808 0.1584 0.1421 -0.0285 0.0085  0.0105  12  GLN   C CD   
3430 O  OE1  . GLN   C 8   ? 0.1905 0.1691 0.1611 -0.0298 0.0049  0.0137  12  GLN   C OE1  
3431 N  NE2  . GLN   C 8   ? 0.1752 0.1556 0.1498 -0.0217 0.0013  0.0052  12  GLN   C NE2  
3432 N  N    . THR   C 9   ? 0.1756 0.1562 0.1305 -0.0398 -0.0024 0.0181  13  THR   C N    
3433 C  CA   . THR   C 9   ? 0.1780 0.1616 0.1372 -0.0393 0.0053  0.0217  13  THR   C CA   
3434 C  C    . THR   C 9   ? 0.1751 0.1611 0.1468 -0.0406 0.0068  0.0199  13  THR   C C    
3435 O  O    . THR   C 9   ? 0.1803 0.1702 0.1846 -0.0325 -0.0086 0.0289  13  THR   C O    
3436 C  CB   . THR   C 9   ? 0.2082 0.1714 0.1346 -0.0334 0.0074  0.0178  13  THR   C CB   
3437 O  OG1  . THR   C 9   ? 0.2224 0.1791 0.1540 -0.0276 0.0044  0.0002  13  THR   C OG1  
3438 C  CG2  . THR   C 9   ? 0.2358 0.1893 0.1432 -0.0267 0.0236  0.0223  13  THR   C CG2  
3439 N  N    . LEU   C 10  ? 0.1616 0.1654 0.1475 -0.0372 0.0176  0.0115  14  LEU   C N    
3440 C  CA   . LEU   C 10  ? 0.1770 0.1709 0.1496 -0.0411 0.0230  0.0099  14  LEU   C CA   
3441 C  C    . LEU   C 10  ? 0.1766 0.1634 0.1322 -0.0398 0.0102  0.0086  14  LEU   C C    
3442 O  O    . LEU   C 10  ? 0.1726 0.1899 0.1416 -0.0441 -0.0024 0.0070  14  LEU   C O    
3443 C  CB   . LEU   C 10  ? 0.1910 0.1913 0.1795 -0.0328 0.0420  0.0041  14  LEU   C CB   
3444 C  CG   . LEU   C 10  ? 0.2408 0.2377 0.2092 -0.0172 0.0597  -0.0130 14  LEU   C CG   
3445 C  CD1  . LEU   C 10  ? 0.2817 0.2719 0.2223 -0.0023 0.0599  -0.0130 14  LEU   C CD1  
3446 C  CD2  . LEU   C 10  ? 0.2652 0.2555 0.2415 -0.0107 0.0712  -0.0104 14  LEU   C CD2  
3447 N  N    . ILE   C 11  ? 0.1819 0.1628 0.1193 -0.0450 0.0000  0.0111  15  ILE   C N    
3448 C  CA   . ILE   C 11  ? 0.1861 0.1687 0.1269 -0.0529 0.0097  0.0044  15  ILE   C CA   
3449 C  C    . ILE   C 11  ? 0.1808 0.1652 0.1303 -0.0502 0.0097  -0.0035 15  ILE   C C    
3450 O  O    . ILE   C 11  ? 0.1770 0.1789 0.1331 -0.0486 0.0093  -0.0044 15  ILE   C O    
3451 C  CB   . ILE   C 11  ? 0.2132 0.1993 0.1566 -0.0445 0.0088  0.0036  15  ILE   C CB   
3452 C  CG1  . ILE   C 11  ? 0.2481 0.2268 0.1896 -0.0562 0.0185  0.0056  15  ILE   C CG1  
3453 C  CG2  . ILE   C 11  ? 0.2224 0.2212 0.1587 -0.0417 0.0182  -0.0104 15  ILE   C CG2  
3454 C  CD1  . ILE   C 11  ? 0.2849 0.2661 0.2315 -0.0450 -0.0055 0.0103  15  ILE   C CD1  
3455 N  N    . PHE   C 12  ? 0.1757 0.1511 0.1282 -0.0530 0.0102  -0.0107 16  PHE   C N    
3456 C  CA   . PHE   C 12  ? 0.1812 0.1480 0.1397 -0.0467 0.0180  -0.0157 16  PHE   C CA   
3457 C  C    . PHE   C 12  ? 0.1759 0.1421 0.1219 -0.0546 0.0140  -0.0235 16  PHE   C C    
3458 O  O    . PHE   C 12  ? 0.1785 0.1695 0.1194 -0.0591 0.0210  -0.0331 16  PHE   C O    
3459 C  CB   . PHE   C 12  ? 0.1869 0.1477 0.1515 -0.0379 0.0235  -0.0176 16  PHE   C CB   
3460 C  CG   . PHE   C 12  ? 0.1985 0.1523 0.1659 -0.0355 0.0337  -0.0144 16  PHE   C CG   
3461 C  CD1  . PHE   C 12  ? 0.2105 0.1561 0.1772 -0.0401 0.0374  -0.0217 16  PHE   C CD1  
3462 C  CD2  . PHE   C 12  ? 0.2127 0.1545 0.1769 -0.0396 0.0360  -0.0201 16  PHE   C CD2  
3463 C  CE1  . PHE   C 12  ? 0.2233 0.1677 0.1763 -0.0245 0.0440  -0.0261 16  PHE   C CE1  
3464 C  CE2  . PHE   C 12  ? 0.2178 0.1592 0.1939 -0.0396 0.0407  -0.0156 16  PHE   C CE2  
3465 C  CZ   . PHE   C 12  ? 0.2237 0.1828 0.1747 -0.0264 0.0485  -0.0142 16  PHE   C CZ   
3466 N  N    . PHE   C 13  ? 0.1731 0.1421 0.1243 -0.0575 0.0159  -0.0275 17  PHE   C N    
3467 C  CA   . PHE   C 13  ? 0.1800 0.1447 0.1234 -0.0515 0.0156  -0.0248 17  PHE   C CA   
3468 C  C    . PHE   C 13  ? 0.1828 0.1498 0.1234 -0.0530 0.0151  -0.0242 17  PHE   C C    
3469 O  O    . PHE   C 13  ? 0.1953 0.1566 0.1212 -0.0551 0.0168  -0.0271 17  PHE   C O    
3470 C  CB   . PHE   C 13  ? 0.1856 0.1464 0.1305 -0.0465 0.0059  -0.0215 17  PHE   C CB   
3471 C  CG   . PHE   C 13  ? 0.1793 0.1409 0.1329 -0.0409 0.0025  -0.0165 17  PHE   C CG   
3472 C  CD1  . PHE   C 13  ? 0.1814 0.1658 0.1378 -0.0344 0.0082  -0.0125 17  PHE   C CD1  
3473 C  CD2  . PHE   C 13  ? 0.1885 0.1565 0.1434 -0.0348 0.0014  -0.0096 17  PHE   C CD2  
3474 C  CE1  . PHE   C 13  ? 0.1802 0.1643 0.1449 -0.0291 0.0008  -0.0114 17  PHE   C CE1  
3475 C  CE2  . PHE   C 13  ? 0.1863 0.1628 0.1526 -0.0342 -0.0097 -0.0059 17  PHE   C CE2  
3476 C  CZ   . PHE   C 13  ? 0.1794 0.1569 0.1579 -0.0329 0.0003  -0.0054 17  PHE   C CZ   
3477 N  N    . ASP   C 14  ? 0.1692 0.1533 0.1272 -0.0554 0.0215  -0.0253 18  ASP   C N    
3478 C  CA   . ASP   C 14  ? 0.1761 0.1568 0.1341 -0.0512 0.0190  -0.0220 18  ASP   C CA   
3479 C  C    . ASP   C 14  ? 0.1691 0.1528 0.1227 -0.0483 0.0141  -0.0186 18  ASP   C C    
3480 O  O    . ASP   C 14  ? 0.1628 0.1526 0.1339 -0.0437 0.0057  -0.0274 18  ASP   C O    
3481 C  CB   . ASP   C 14  ? 0.1810 0.1695 0.1373 -0.0445 0.0215  -0.0135 18  ASP   C CB   
3482 C  CG   . ASP   C 14  ? 0.1991 0.1778 0.1685 -0.0450 0.0161  -0.0168 18  ASP   C CG   
3483 O  OD1  . ASP   C 14  ? 0.2176 0.1787 0.1789 -0.0491 0.0087  -0.0196 18  ASP   C OD1  
3484 O  OD2  . ASP   C 14  ? 0.2204 0.1911 0.1793 -0.0473 0.0149  -0.0093 18  ASP   C OD2  
3485 N  N    . MET   C 15  ? 0.1694 0.1583 0.1271 -0.0465 0.0112  -0.0223 19  MET   C N    
3486 C  CA   . MET   C 15  ? 0.1667 0.1532 0.1259 -0.0391 0.0099  -0.0131 19  MET   C CA   
3487 C  C    . MET   C 15  ? 0.1635 0.1500 0.1380 -0.0369 0.0135  -0.0200 19  MET   C C    
3488 O  O    . MET   C 15  ? 0.1700 0.1590 0.1455 -0.0405 0.0267  -0.0290 19  MET   C O    
3489 C  CB   . MET   C 15  ? 0.1782 0.1654 0.1374 -0.0365 0.0057  -0.0126 19  MET   C CB   
3490 C  CG   . MET   C 15  ? 0.1956 0.1682 0.1415 -0.0418 -0.0036 -0.0098 19  MET   C CG   
3491 S  SD   . MET   C 15  ? 0.2268 0.1983 0.1478 -0.0289 -0.0169 -0.0031 19  MET   C SD   
3492 C  CE   . MET   C 15  ? 0.2285 0.1887 0.1397 -0.0304 -0.0260 0.0052  19  MET   C CE   
3493 N  N    A GLU   C 16  ? 0.1544 0.1430 0.1312 -0.0338 0.0092  -0.0197 20  GLU   C N    
3494 N  N    B GLU   C 16  ? 0.1646 0.1479 0.1391 -0.0371 0.0128  -0.0203 20  GLU   C N    
3495 C  CA   A GLU   C 16  ? 0.1495 0.1396 0.1281 -0.0302 0.0086  -0.0163 20  GLU   C CA   
3496 C  CA   B GLU   C 16  ? 0.1651 0.1455 0.1483 -0.0359 0.0124  -0.0186 20  GLU   C CA   
3497 C  C    A GLU   C 16  ? 0.1502 0.1378 0.1275 -0.0302 -0.0006 -0.0131 20  GLU   C C    
3498 C  C    B GLU   C 16  ? 0.1586 0.1397 0.1415 -0.0354 0.0016  -0.0149 20  GLU   C C    
3499 O  O    A GLU   C 16  ? 0.1568 0.1448 0.1216 -0.0255 0.0014  -0.0167 20  GLU   C O    
3500 O  O    B GLU   C 16  ? 0.1563 0.1483 0.1443 -0.0353 0.0102  -0.0228 20  GLU   C O    
3501 C  CB   A GLU   C 16  ? 0.1510 0.1512 0.1352 -0.0285 0.0062  -0.0103 20  GLU   C CB   
3502 C  CB   B GLU   C 16  ? 0.1873 0.1653 0.1682 -0.0362 0.0078  -0.0099 20  GLU   C CB   
3503 C  CG   A GLU   C 16  ? 0.1516 0.1670 0.1438 -0.0211 0.0099  -0.0101 20  GLU   C CG   
3504 C  CG   B GLU   C 16  ? 0.1993 0.1935 0.2022 -0.0286 0.0112  -0.0108 20  GLU   C CG   
3505 C  CD   A GLU   C 16  ? 0.1620 0.1798 0.1644 -0.0141 0.0106  -0.0133 20  GLU   C CD   
3506 C  CD   B GLU   C 16  ? 0.2338 0.2262 0.2307 -0.0185 0.0089  -0.0008 20  GLU   C CD   
3507 O  OE1  A GLU   C 16  ? 0.1662 0.1796 0.1843 -0.0104 0.0111  -0.0184 20  GLU   C OE1  
3508 O  OE1  B GLU   C 16  ? 0.2660 0.2569 0.2586 -0.0192 0.0206  -0.0013 20  GLU   C OE1  
3509 O  OE2  A GLU   C 16  ? 0.1726 0.2097 0.1739 -0.0090 0.0065  -0.0127 20  GLU   C OE2  
3510 O  OE2  B GLU   C 16  ? 0.2545 0.2618 0.2714 -0.0032 0.0041  0.0042  20  GLU   C OE2  
3511 N  N    . ALA   C 17  ? 0.1556 0.1313 0.1411 -0.0275 -0.0003 -0.0196 21  ALA   C N    
3512 C  CA   . ALA   C 17  ? 0.1505 0.1366 0.1402 -0.0258 -0.0046 -0.0127 21  ALA   C CA   
3513 C  C    . ALA   C 17  ? 0.1517 0.1395 0.1510 -0.0268 -0.0089 -0.0075 21  ALA   C C    
3514 O  O    . ALA   C 17  ? 0.1541 0.1529 0.2027 -0.0144 -0.0034 0.0001  21  ALA   C O    
3515 C  CB   . ALA   C 17  ? 0.1545 0.1473 0.1423 -0.0264 -0.0049 -0.0139 21  ALA   C CB   
3516 N  N    . THR   C 18  ? 0.1519 0.1462 0.1433 -0.0264 -0.0073 -0.0098 22  THR   C N    
3517 C  CA   . THR   C 18  ? 0.1561 0.1532 0.1462 -0.0326 -0.0046 -0.0060 22  THR   C CA   
3518 C  C    . THR   C 18  ? 0.1612 0.1493 0.1536 -0.0354 -0.0071 -0.0069 22  THR   C C    
3519 O  O    . THR   C 18  ? 0.1999 0.1539 0.1631 -0.0383 -0.0156 0.0005  22  THR   C O    
3520 C  CB   . THR   C 18  ? 0.1511 0.1657 0.1512 -0.0315 -0.0006 -0.0078 22  THR   C CB   
3521 O  OG1  . THR   C 18  ? 0.1479 0.1644 0.1523 -0.0309 -0.0023 -0.0067 22  THR   C OG1  
3522 C  CG2  . THR   C 18  ? 0.1450 0.1692 0.1487 -0.0316 0.0060  -0.0107 22  THR   C CG2  
3523 N  N    . GLY   C 19  ? 0.1609 0.1294 0.1529 -0.0449 -0.0081 -0.0168 23  GLY   C N    
3524 C  CA   . GLY   C 19  ? 0.1603 0.1324 0.1569 -0.0460 -0.0018 -0.0198 23  GLY   C CA   
3525 C  C    . GLY   C 19  ? 0.1724 0.1332 0.1601 -0.0478 0.0012  -0.0194 23  GLY   C C    
3526 O  O    . GLY   C 19  ? 0.1730 0.1340 0.1693 -0.0512 0.0020  -0.0265 23  GLY   C O    
3527 N  N    . LEU   C 20  ? 0.1858 0.1504 0.1634 -0.0411 0.0099  -0.0320 24  LEU   C N    
3528 C  CA   . LEU   C 20  ? 0.1943 0.1570 0.1675 -0.0438 0.0122  -0.0357 24  LEU   C CA   
3529 C  C    . LEU   C 20  ? 0.2080 0.1683 0.1549 -0.0442 0.0052  -0.0381 24  LEU   C C    
3530 O  O    . LEU   C 20  ? 0.2012 0.1743 0.1512 -0.0480 -0.0055 -0.0320 24  LEU   C O    
3531 C  CB   . LEU   C 20  ? 0.1900 0.1510 0.1912 -0.0556 0.0168  -0.0402 24  LEU   C CB   
3532 C  CG   . LEU   C 20  ? 0.2085 0.1532 0.2146 -0.0523 0.0103  -0.0455 24  LEU   C CG   
3533 C  CD1  . LEU   C 20  ? 0.2312 0.1564 0.2263 -0.0504 0.0159  -0.0503 24  LEU   C CD1  
3534 C  CD2  . LEU   C 20  ? 0.2159 0.1727 0.2532 -0.0517 0.0136  -0.0456 24  LEU   C CD2  
3535 N  N    . PRO   C 21  ? 0.2195 0.1757 0.1570 -0.0535 0.0125  -0.0373 25  PRO   C N    
3536 C  CA   . PRO   C 21  ? 0.2344 0.1844 0.1527 -0.0513 0.0127  -0.0312 25  PRO   C CA   
3537 C  C    . PRO   C 21  ? 0.2412 0.2000 0.1533 -0.0480 0.0010  -0.0342 25  PRO   C C    
3538 O  O    . PRO   C 21  ? 0.2538 0.2179 0.1680 -0.0444 -0.0113 -0.0284 25  PRO   C O    
3539 C  CB   . PRO   C 21  ? 0.2362 0.1847 0.1544 -0.0520 0.0145  -0.0308 25  PRO   C CB   
3540 C  CG   . PRO   C 21  ? 0.2365 0.1889 0.1552 -0.0528 0.0207  -0.0279 25  PRO   C CG   
3541 C  CD   . PRO   C 21  ? 0.2312 0.1791 0.1595 -0.0507 0.0171  -0.0369 25  PRO   C CD   
3542 N  N    A SER   C 22  ? 0.2462 0.2010 0.1556 -0.0471 0.0000  -0.0324 26  SER   C N    
3543 N  N    B SER   C 22  ? 0.2372 0.1998 0.1619 -0.0464 -0.0025 -0.0304 26  SER   C N    
3544 C  CA   A SER   C 22  ? 0.2426 0.2010 0.1679 -0.0434 -0.0058 -0.0370 26  SER   C CA   
3545 C  CA   B SER   C 22  ? 0.2301 0.1990 0.1786 -0.0411 -0.0093 -0.0326 26  SER   C CA   
3546 C  C    A SER   C 22  ? 0.2193 0.1947 0.1723 -0.0425 -0.0134 -0.0366 26  SER   C C    
3547 C  C    B SER   C 22  ? 0.2117 0.1875 0.1780 -0.0394 -0.0166 -0.0338 26  SER   C C    
3548 O  O    A SER   C 22  ? 0.2141 0.2039 0.1829 -0.0414 -0.0152 -0.0393 26  SER   C O    
3549 O  O    B SER   C 22  ? 0.2034 0.1795 0.1930 -0.0299 -0.0204 -0.0288 26  SER   C O    
3550 C  CB   A SER   C 22  ? 0.2538 0.2043 0.1783 -0.0427 -0.0013 -0.0414 26  SER   C CB   
3551 C  CB   B SER   C 22  ? 0.2316 0.2035 0.1946 -0.0420 -0.0062 -0.0381 26  SER   C CB   
3552 O  OG   A SER   C 22  ? 0.2733 0.2114 0.1887 -0.0438 0.0081  -0.0471 26  SER   C OG   
3553 O  OG   B SER   C 22  ? 0.2324 0.2111 0.2176 -0.0434 -0.0102 -0.0305 26  SER   C OG   
3554 N  N    . SER   C 23  ? 0.2033 0.1893 0.1766 -0.0368 -0.0176 -0.0368 27  SER   C N    
3555 C  CA   . SER   C 23  ? 0.1935 0.1882 0.1734 -0.0403 -0.0175 -0.0274 27  SER   C CA   
3556 C  C    . SER   C 23  ? 0.1930 0.1977 0.1782 -0.0265 -0.0221 -0.0245 27  SER   C C    
3557 O  O    . SER   C 23  ? 0.2070 0.2092 0.1813 -0.0301 -0.0018 -0.0184 27  SER   C O    
3558 C  CB   . SER   C 23  ? 0.1922 0.1804 0.1767 -0.0328 -0.0087 -0.0184 27  SER   C CB   
3559 O  OG   . SER   C 23  ? 0.1970 0.1693 0.1677 -0.0278 -0.0120 -0.0188 27  SER   C OG   
3560 N  N    A ARG   C 24  ? 0.1899 0.1981 0.1734 -0.0248 -0.0247 -0.0223 28  ARG   C N    
3561 N  N    B ARG   C 24  ? 0.1912 0.2048 0.1742 -0.0289 -0.0292 -0.0231 28  ARG   C N    
3562 C  CA   A ARG   C 24  ? 0.1867 0.1955 0.1874 -0.0195 -0.0246 -0.0181 28  ARG   C CA   
3563 C  CA   B ARG   C 24  ? 0.1899 0.2060 0.1916 -0.0255 -0.0330 -0.0223 28  ARG   C CA   
3564 C  C    A ARG   C 24  ? 0.1810 0.1844 0.1835 -0.0165 -0.0193 -0.0207 28  ARG   C C    
3565 C  C    B ARG   C 24  ? 0.1812 0.1900 0.1843 -0.0194 -0.0239 -0.0230 28  ARG   C C    
3566 O  O    A ARG   C 24  ? 0.1712 0.1771 0.2013 -0.0052 -0.0165 -0.0211 28  ARG   C O    
3567 O  O    B ARG   C 24  ? 0.1722 0.1820 0.2018 -0.0080 -0.0208 -0.0233 28  ARG   C O    
3568 C  CB   A ARG   C 24  ? 0.1967 0.2115 0.2067 -0.0144 -0.0207 -0.0175 28  ARG   C CB   
3569 C  CB   B ARG   C 24  ? 0.1997 0.2364 0.2160 -0.0250 -0.0374 -0.0257 28  ARG   C CB   
3570 C  CG   A ARG   C 24  ? 0.2225 0.2281 0.2244 -0.0049 -0.0143 -0.0055 28  ARG   C CG   
3571 C  CG   B ARG   C 24  ? 0.2353 0.2607 0.2428 -0.0199 -0.0403 -0.0214 28  ARG   C CG   
3572 C  CD   A ARG   C 24  ? 0.2388 0.2388 0.2441 0.0026  -0.0005 0.0001  28  ARG   C CD   
3573 C  CD   B ARG   C 24  ? 0.2533 0.2953 0.2679 -0.0164 -0.0296 -0.0200 28  ARG   C CD   
3574 N  NE   A ARG   C 24  ? 0.2581 0.2407 0.2522 0.0120  0.0046  0.0086  28  ARG   C NE   
3575 N  NE   B ARG   C 24  ? 0.2884 0.3142 0.3013 -0.0186 -0.0354 -0.0254 28  ARG   C NE   
3576 C  CZ   A ARG   C 24  ? 0.2763 0.2446 0.2751 -0.0015 0.0048  0.0133  28  ARG   C CZ   
3577 C  CZ   B ARG   C 24  ? 0.3216 0.3416 0.3301 -0.0148 -0.0331 -0.0196 28  ARG   C CZ   
3578 N  NH1  A ARG   C 24  ? 0.2940 0.2506 0.2808 0.0001  0.0135  0.0218  28  ARG   C NH1  
3579 N  NH1  B ARG   C 24  ? 0.3346 0.3667 0.3333 -0.0119 -0.0377 -0.0164 28  ARG   C NH1  
3580 N  NH2  A ARG   C 24  ? 0.2909 0.2502 0.2782 -0.0095 0.0041  0.0122  28  ARG   C NH2  
3581 N  NH2  B ARG   C 24  ? 0.3382 0.3595 0.3456 -0.0079 -0.0128 -0.0282 28  ARG   C NH2  
3582 N  N    . PRO   C 25  ? 0.1705 0.1671 0.1680 -0.0176 -0.0198 -0.0215 29  PRO   C N    
3583 C  CA   . PRO   C 25  ? 0.1677 0.1600 0.1636 -0.0207 -0.0274 -0.0258 29  PRO   C CA   
3584 C  C    . PRO   C 25  ? 0.1781 0.1573 0.1692 -0.0155 -0.0350 -0.0218 29  PRO   C C    
3585 O  O    . PRO   C 25  ? 0.1983 0.1762 0.1568 -0.0182 -0.0363 -0.0155 29  PRO   C O    
3586 C  CB   . PRO   C 25  ? 0.1676 0.1483 0.1633 -0.0193 -0.0264 -0.0255 29  PRO   C CB   
3587 C  CG   . PRO   C 25  ? 0.1718 0.1546 0.1655 -0.0180 -0.0131 -0.0251 29  PRO   C CG   
3588 C  CD   . PRO   C 25  ? 0.1776 0.1615 0.1637 -0.0217 -0.0148 -0.0247 29  PRO   C CD   
3589 N  N    . GLU   C 26  ? 0.1660 0.1569 0.1661 -0.0151 -0.0407 -0.0252 30  GLU   C N    
3590 C  CA   . GLU   C 26  ? 0.1778 0.1676 0.1835 -0.0150 -0.0433 -0.0309 30  GLU   C CA   
3591 C  C    . GLU   C 26  ? 0.1657 0.1527 0.1634 -0.0138 -0.0309 -0.0257 30  GLU   C C    
3592 O  O    . GLU   C 26  ? 0.1693 0.1558 0.1564 -0.0128 -0.0192 -0.0188 30  GLU   C O    
3593 C  CB   . GLU   C 26  ? 0.1857 0.2142 0.2178 -0.0083 -0.0466 -0.0532 30  GLU   C CB   
3594 C  CG   . GLU   C 26  ? 0.2057 0.2650 0.2600 0.0012  -0.0649 -0.0595 30  GLU   C CG   
3595 C  CD   . GLU   C 26  ? 0.2524 0.3251 0.3046 0.0146  -0.0488 -0.0833 30  GLU   C CD   
3596 O  OE1  . GLU   C 26  ? 0.3239 0.3672 0.3133 0.0197  -0.0367 -0.0970 30  GLU   C OE1  
3597 O  OE2  . GLU   C 26  ? 0.2593 0.4052 0.3786 0.0131  -0.0601 -0.1024 30  GLU   C OE2  
3598 N  N    . VAL   C 27  ? 0.1695 0.1468 0.1719 -0.0134 -0.0309 -0.0150 31  VAL   C N    
3599 C  CA   . VAL   C 27  ? 0.1620 0.1471 0.1519 -0.0135 -0.0269 -0.0192 31  VAL   C CA   
3600 C  C    . VAL   C 27  ? 0.1475 0.1506 0.1404 -0.0106 -0.0142 -0.0249 31  VAL   C C    
3601 O  O    . VAL   C 27  ? 0.1538 0.1715 0.1668 0.0007  -0.0202 -0.0319 31  VAL   C O    
3602 C  CB   . VAL   C 27  ? 0.1819 0.1566 0.1545 -0.0165 -0.0281 -0.0141 31  VAL   C CB   
3603 C  CG1  . VAL   C 27  ? 0.1882 0.1622 0.1481 -0.0150 -0.0364 -0.0087 31  VAL   C CG1  
3604 C  CG2  . VAL   C 27  ? 0.1930 0.1686 0.1549 -0.0170 -0.0379 -0.0124 31  VAL   C CG2  
3605 N  N    . THR   C 28  ? 0.1416 0.1552 0.1213 -0.0058 -0.0029 -0.0241 32  THR   C N    
3606 C  CA   . THR   C 28  ? 0.1399 0.1656 0.1210 -0.0124 -0.0001 -0.0250 32  THR   C CA   
3607 C  C    . THR   C 28  ? 0.1331 0.1543 0.1216 -0.0069 0.0011  -0.0234 32  THR   C C    
3608 O  O    . THR   C 28  ? 0.1392 0.1558 0.1233 -0.0072 -0.0045 -0.0157 32  THR   C O    
3609 C  CB   . THR   C 28  ? 0.1427 0.1732 0.1279 -0.0170 0.0091  -0.0189 32  THR   C CB   
3610 O  OG1  . THR   C 28  ? 0.1549 0.1731 0.1418 -0.0137 0.0159  -0.0187 32  THR   C OG1  
3611 C  CG2  . THR   C 28  ? 0.1464 0.1949 0.1431 -0.0191 0.0081  -0.0211 32  THR   C CG2  
3612 N  N    . GLU   C 29  ? 0.1295 0.1527 0.1192 -0.0205 -0.0040 -0.0193 33  GLU   C N    
3613 C  CA   . GLU   C 29  ? 0.1342 0.1583 0.1275 -0.0208 -0.0020 -0.0232 33  GLU   C CA   
3614 C  C    . GLU   C 29  ? 0.1412 0.1518 0.1208 -0.0255 -0.0029 -0.0274 33  GLU   C C    
3615 O  O    . GLU   C 29  ? 0.1490 0.1583 0.1193 -0.0297 -0.0063 -0.0280 33  GLU   C O    
3616 C  CB   . GLU   C 29  ? 0.1505 0.1702 0.1425 -0.0137 0.0012  -0.0133 33  GLU   C CB   
3617 C  CG   . GLU   C 29  ? 0.1623 0.1938 0.1582 -0.0166 0.0044  -0.0106 33  GLU   C CG   
3618 C  CD   . GLU   C 29  ? 0.1911 0.2159 0.1784 -0.0081 0.0056  -0.0078 33  GLU   C CD   
3619 O  OE1  . GLU   C 29  ? 0.2166 0.2129 0.1839 -0.0017 0.0189  -0.0029 33  GLU   C OE1  
3620 O  OE2  . GLU   C 29  ? 0.2219 0.2578 0.1891 -0.0055 -0.0046 0.0069  33  GLU   C OE2  
3621 N  N    . LEU   C 30  ? 0.1451 0.1517 0.1161 -0.0332 0.0055  -0.0254 34  LEU   C N    
3622 C  CA   . LEU   C 30  ? 0.1554 0.1596 0.1249 -0.0353 0.0070  -0.0222 34  LEU   C CA   
3623 C  C    . LEU   C 30  ? 0.1567 0.1554 0.1214 -0.0373 0.0064  -0.0235 34  LEU   C C    
3624 O  O    . LEU   C 30  ? 0.1665 0.1881 0.1220 -0.0349 0.0035  -0.0269 34  LEU   C O    
3625 C  CB   . LEU   C 30  ? 0.1644 0.1792 0.1548 -0.0296 0.0051  -0.0138 34  LEU   C CB   
3626 C  CG   . LEU   C 30  ? 0.1802 0.1802 0.1801 -0.0246 0.0030  -0.0136 34  LEU   C CG   
3627 C  CD1  . LEU   C 30  ? 0.1919 0.1711 0.1898 -0.0247 0.0008  -0.0129 34  LEU   C CD1  
3628 C  CD2  . LEU   C 30  ? 0.1891 0.2008 0.2143 -0.0241 0.0000  -0.0053 34  LEU   C CD2  
3629 N  N    . CYS   C 31  ? 0.1549 0.1478 0.1106 -0.0328 0.0039  -0.0227 35  CYS   C N    
3630 C  CA   . CYS   C 31  ? 0.1590 0.1561 0.1162 -0.0368 0.0038  -0.0205 35  CYS   C CA   
3631 C  C    . CYS   C 31  ? 0.1600 0.1553 0.1160 -0.0375 0.0075  -0.0207 35  CYS   C C    
3632 O  O    . CYS   C 31  ? 0.1618 0.1396 0.1192 -0.0395 0.0054  -0.0266 35  CYS   C O    
3633 C  CB   . CYS   C 31  ? 0.1683 0.1617 0.1424 -0.0336 0.0016  -0.0093 35  CYS   C CB   
3634 S  SG   . CYS   C 31  ? 0.1777 0.1933 0.2140 -0.0275 -0.0125 0.0110  35  CYS   C SG   
3635 N  N    . LEU   C 32  ? 0.1650 0.1524 0.1119 -0.0350 0.0083  -0.0170 36  LEU   C N    
3636 C  CA   . LEU   C 32  ? 0.1676 0.1627 0.1168 -0.0349 0.0103  -0.0182 36  LEU   C CA   
3637 C  C    . LEU   C 32  ? 0.1668 0.1524 0.1127 -0.0356 0.0046  -0.0214 36  LEU   C C    
3638 O  O    . LEU   C 32  ? 0.1678 0.1808 0.1095 -0.0406 0.0063  -0.0224 36  LEU   C O    
3639 C  CB   . LEU   C 32  ? 0.1810 0.1679 0.1346 -0.0290 0.0113  -0.0156 36  LEU   C CB   
3640 C  CG   . LEU   C 32  ? 0.1984 0.1937 0.1751 -0.0201 -0.0023 -0.0155 36  LEU   C CG   
3641 C  CD1  . LEU   C 32  ? 0.2117 0.2104 0.1862 -0.0189 -0.0006 -0.0130 36  LEU   C CD1  
3642 C  CD2  . LEU   C 32  ? 0.2195 0.2061 0.2086 -0.0136 -0.0091 -0.0141 36  LEU   C CD2  
3643 N  N    A LEU   C 33  ? 0.1755 0.1547 0.1157 -0.0365 0.0075  -0.0201 37  LEU   C N    
3644 N  N    B LEU   C 33  ? 0.1731 0.1530 0.1069 -0.0401 0.0042  -0.0196 37  LEU   C N    
3645 C  CA   A LEU   C 33  ? 0.1761 0.1575 0.1267 -0.0255 0.0060  -0.0169 37  LEU   C CA   
3646 C  CA   B LEU   C 33  ? 0.1731 0.1550 0.1118 -0.0318 0.0013  -0.0166 37  LEU   C CA   
3647 C  C    A LEU   C 33  ? 0.1687 0.1540 0.1239 -0.0259 0.0013  -0.0121 37  LEU   C C    
3648 C  C    B LEU   C 33  ? 0.1686 0.1536 0.1145 -0.0298 -0.0007 -0.0105 37  LEU   C C    
3649 O  O    A LEU   C 33  ? 0.1675 0.1593 0.1245 -0.0244 0.0077  -0.0129 37  LEU   C O    
3650 O  O    B LEU   C 33  ? 0.1743 0.1595 0.1171 -0.0285 0.0066  -0.0111 37  LEU   C O    
3651 C  CB   A LEU   C 33  ? 0.1980 0.1655 0.1532 -0.0198 0.0035  -0.0177 37  LEU   C CB   
3652 C  CB   B LEU   C 33  ? 0.1876 0.1601 0.1227 -0.0322 -0.0054 -0.0167 37  LEU   C CB   
3653 C  CG   A LEU   C 33  ? 0.2081 0.1846 0.1783 -0.0073 0.0038  -0.0208 37  LEU   C CG   
3654 C  CG   B LEU   C 33  ? 0.1959 0.1713 0.1276 -0.0272 -0.0081 -0.0190 37  LEU   C CG   
3655 C  CD1  A LEU   C 33  ? 0.2168 0.1941 0.1873 -0.0062 -0.0039 -0.0238 37  LEU   C CD1  
3656 C  CD1  B LEU   C 33  ? 0.1981 0.1753 0.1192 -0.0287 -0.0090 -0.0160 37  LEU   C CD1  
3657 C  CD2  A LEU   C 33  ? 0.2146 0.1894 0.1941 -0.0027 0.0040  -0.0225 37  LEU   C CD2  
3658 C  CD2  B LEU   C 33  ? 0.1959 0.1761 0.1397 -0.0307 -0.0091 -0.0145 37  LEU   C CD2  
3659 N  N    . ALA   C 34  ? 0.1633 0.1496 0.1158 -0.0270 -0.0001 -0.0051 38  ALA   C N    
3660 C  CA   . ALA   C 34  ? 0.1699 0.1533 0.1252 -0.0269 -0.0009 0.0040  38  ALA   C CA   
3661 C  C    . ALA   C 34  ? 0.1727 0.1573 0.1299 -0.0314 -0.0014 0.0138  38  ALA   C C    
3662 O  O    . ALA   C 34  ? 0.1764 0.1769 0.1278 -0.0275 -0.0044 0.0080  38  ALA   C O    
3663 C  CB   . ALA   C 34  ? 0.1797 0.1582 0.1421 -0.0267 -0.0005 0.0088  38  ALA   C CB   
3664 N  N    . VAL   C 35  ? 0.1755 0.1730 0.1344 -0.0316 0.0081  0.0225  39  VAL   C N    
3665 C  CA   . VAL   C 35  ? 0.1896 0.1940 0.1526 -0.0278 0.0133  0.0269  39  VAL   C CA   
3666 C  C    . VAL   C 35  ? 0.1714 0.1876 0.1366 -0.0330 0.0108  0.0202  39  VAL   C C    
3667 O  O    . VAL   C 35  ? 0.1654 0.1897 0.1481 -0.0493 0.0040  0.0240  39  VAL   C O    
3668 C  CB   . VAL   C 35  ? 0.2266 0.2022 0.1860 -0.0119 0.0184  0.0370  39  VAL   C CB   
3669 C  CG1  . VAL   C 35  ? 0.2565 0.2289 0.2104 -0.0125 0.0328  0.0401  39  VAL   C CG1  
3670 C  CG2  . VAL   C 35  ? 0.2395 0.2127 0.1955 -0.0111 0.0260  0.0344  39  VAL   C CG2  
3671 N  N    . HIS   C 36  ? 0.1816 0.1885 0.1118 -0.0390 0.0116  0.0208  40  HIS   C N    
3672 C  CA   . HIS   C 36  ? 0.1844 0.1789 0.1281 -0.0385 0.0098  0.0221  40  HIS   C CA   
3673 C  C    . HIS   C 36  ? 0.1877 0.1684 0.1344 -0.0326 0.0091  0.0207  40  HIS   C C    
3674 O  O    . HIS   C 36  ? 0.1757 0.1829 0.1467 -0.0197 0.0156  0.0202  40  HIS   C O    
3675 C  CB   . HIS   C 36  ? 0.2088 0.1804 0.1363 -0.0404 -0.0031 0.0097  40  HIS   C CB   
3676 C  CG   . HIS   C 36  ? 0.2261 0.1789 0.1517 -0.0350 -0.0068 0.0142  40  HIS   C CG   
3677 N  ND1  . HIS   C 36  ? 0.2362 0.1968 0.1754 -0.0443 -0.0029 0.0237  40  HIS   C ND1  
3678 C  CD2  . HIS   C 36  ? 0.2616 0.1872 0.1669 -0.0254 -0.0076 0.0073  40  HIS   C CD2  
3679 C  CE1  . HIS   C 36  ? 0.2547 0.2015 0.1897 -0.0274 -0.0101 0.0249  40  HIS   C CE1  
3680 N  NE2  . HIS   C 36  ? 0.2699 0.1858 0.1689 -0.0344 -0.0074 0.0030  40  HIS   C NE2  
3681 N  N    . ARG   C 37  ? 0.1857 0.1695 0.1334 -0.0302 0.0210  0.0217  41  ARG   C N    
3682 C  CA   . ARG   C 37  ? 0.1910 0.1792 0.1323 -0.0271 0.0184  0.0173  41  ARG   C CA   
3683 C  C    . ARG   C 37  ? 0.1944 0.1933 0.1421 -0.0126 0.0198  0.0237  41  ARG   C C    
3684 O  O    . ARG   C 37  ? 0.2158 0.1930 0.1619 -0.0010 0.0333  0.0149  41  ARG   C O    
3685 C  CB   . ARG   C 37  ? 0.1931 0.1786 0.1250 -0.0289 0.0228  0.0151  41  ARG   C CB   
3686 C  CG   . ARG   C 37  ? 0.1958 0.1774 0.1332 -0.0300 0.0217  0.0102  41  ARG   C CG   
3687 C  CD   . ARG   C 37  ? 0.2024 0.1774 0.1354 -0.0295 0.0203  0.0075  41  ARG   C CD   
3688 N  NE   . ARG   C 37  ? 0.2081 0.1917 0.1453 -0.0254 0.0228  0.0052  41  ARG   C NE   
3689 C  CZ   . ARG   C 37  ? 0.2180 0.1970 0.1384 -0.0200 0.0253  -0.0033 41  ARG   C CZ   
3690 N  NH1  . ARG   C 37  ? 0.2234 0.1923 0.1353 -0.0236 0.0202  -0.0125 41  ARG   C NH1  
3691 N  NH2  . ARG   C 37  ? 0.2298 0.2243 0.1561 -0.0228 0.0359  -0.0098 41  ARG   C NH2  
3692 N  N    . CYS   C 38  ? 0.1965 0.2064 0.1612 -0.0151 0.0185  0.0289  42  CYS   C N    
3693 C  CA   . CYS   C 38  ? 0.2039 0.2452 0.1803 -0.0204 0.0156  0.0268  42  CYS   C CA   
3694 C  C    . CYS   C 38  ? 0.2066 0.2532 0.1904 -0.0192 0.0217  0.0250  42  CYS   C C    
3695 O  O    . CYS   C 38  ? 0.2152 0.2752 0.2134 -0.0039 0.0331  0.0303  42  CYS   C O    
3696 C  CB   . CYS   C 38  ? 0.2160 0.2644 0.1918 -0.0334 0.0046  0.0318  42  CYS   C CB   
3697 S  SG   . CYS   C 38  ? 0.2686 0.3271 0.1993 -0.0260 -0.0071 0.0090  42  CYS   C SG   
3698 N  N    . ALA   C 39  ? 0.1955 0.2334 0.1777 -0.0147 0.0175  0.0282  43  ALA   C N    
3699 C  CA   . ALA   C 39  ? 0.2185 0.2374 0.1890 -0.0101 0.0207  0.0404  43  ALA   C CA   
3700 C  C    . ALA   C 39  ? 0.2289 0.2303 0.2075 0.0043  0.0326  0.0441  43  ALA   C C    
3701 O  O    . ALA   C 39  ? 0.2531 0.2504 0.2338 0.0191  0.0301  0.0515  43  ALA   C O    
3702 C  CB   . ALA   C 39  ? 0.2323 0.2428 0.1784 -0.0086 0.0213  0.0408  43  ALA   C CB   
3703 N  N    . LEU   C 40  ? 0.2290 0.2228 0.2139 0.0106  0.0295  0.0451  44  LEU   C N    
3704 C  CA   . LEU   C 40  ? 0.2585 0.2260 0.2241 0.0025  0.0446  0.0441  44  LEU   C CA   
3705 C  C    . LEU   C 40  ? 0.2576 0.2134 0.2373 -0.0005 0.0565  0.0342  44  LEU   C C    
3706 O  O    . LEU   C 40  ? 0.2788 0.2233 0.2467 0.0104  0.0838  0.0275  44  LEU   C O    
3707 C  CB   . LEU   C 40  ? 0.2743 0.2591 0.2553 -0.0142 0.0361  0.0500  44  LEU   C CB   
3708 C  CG   . LEU   C 40  ? 0.3072 0.3322 0.3093 -0.0501 0.0362  0.0607  44  LEU   C CG   
3709 C  CD1  . LEU   C 40  ? 0.3378 0.3724 0.3281 -0.0657 0.0262  0.0526  44  LEU   C CD1  
3710 C  CD2  . LEU   C 40  ? 0.3354 0.3485 0.3445 -0.0489 0.0345  0.0633  44  LEU   C CD2  
3711 N  N    . GLU   C 41  ? 0.2466 0.2039 0.2186 -0.0066 0.0614  0.0252  45  GLU   C N    
3712 C  CA   . GLU   C 41  ? 0.2509 0.2170 0.2303 -0.0210 0.0610  0.0280  45  GLU   C CA   
3713 C  C    . GLU   C 41  ? 0.2530 0.2557 0.2564 -0.0173 0.0689  0.0370  45  GLU   C C    
3714 O  O    . GLU   C 41  ? 0.2849 0.2695 0.2807 -0.0073 0.0786  0.0270  45  GLU   C O    
3715 C  CB   . GLU   C 41  ? 0.2669 0.2217 0.2419 -0.0286 0.0506  0.0221  45  GLU   C CB   
3716 C  CG   . GLU   C 41  ? 0.2693 0.2109 0.2561 -0.0409 0.0461  0.0178  45  GLU   C CG   
3717 C  CD   . GLU   C 41  ? 0.2609 0.2088 0.2754 -0.0437 0.0370  0.0135  45  GLU   C CD   
3718 O  OE1  . GLU   C 41  ? 0.2726 0.2161 0.3140 -0.0482 0.0196  0.0415  45  GLU   C OE1  
3719 O  OE2  . GLU   C 41  ? 0.2548 0.2028 0.3054 -0.0296 0.0523  0.0125  45  GLU   C OE2  
3720 N  N    . SER   C 42  ? 0.2567 0.3172 0.2713 -0.0197 0.0556  0.0370  46  SER   C N    
3721 C  CA   . SER   C 42  ? 0.2683 0.3663 0.2943 -0.0144 0.0524  0.0552  46  SER   C CA   
3722 C  C    . SER   C 42  ? 0.2692 0.4138 0.3078 0.0129  0.0471  0.0638  46  SER   C C    
3723 O  O    . SER   C 42  ? 0.2688 0.4374 0.3349 0.0068  0.0305  0.0578  46  SER   C O    
3724 C  CB   . SER   C 42  ? 0.2896 0.3729 0.3063 -0.0273 0.0412  0.0523  46  SER   C CB   
3725 O  OG   . SER   C 42  ? 0.2724 0.3830 0.3238 -0.0555 0.0472  0.0738  46  SER   C OG   
3726 N  N    . PRO   C 43  ? 0.2887 0.4309 0.3310 0.0277  0.0491  0.0874  47  PRO   C N    
3727 C  CA   . PRO   C 43  ? 0.3108 0.4802 0.3623 0.0370  0.0504  0.1007  47  PRO   C CA   
3728 C  C    . PRO   C 43  ? 0.3191 0.5882 0.3788 0.0768  0.0483  0.0878  47  PRO   C C    
3729 O  O    . PRO   C 43  ? 0.3222 0.5810 0.3658 0.0606  0.0773  0.1201  47  PRO   C O    
3730 C  CB   . PRO   C 43  ? 0.3303 0.4565 0.3826 0.0443  0.0524  0.0976  47  PRO   C CB   
3731 C  CG   . PRO   C 43  ? 0.3304 0.4418 0.3930 0.0422  0.0446  0.0881  47  PRO   C CG   
3732 C  CD   . PRO   C 43  ? 0.3128 0.4292 0.3633 0.0294  0.0485  0.0923  47  PRO   C CD   
3733 N  N    . PRO   C 44  ? 0.4164 0.7125 0.4025 0.1014  0.0293  0.0707  48  PRO   C N    
3734 C  CA   . PRO   C 44  ? 0.4653 0.7440 0.4601 0.1181  -0.0016 0.0633  48  PRO   C CA   
3735 C  C    . PRO   C 44  ? 0.5393 0.7374 0.4784 0.1271  -0.0103 0.0698  48  PRO   C C    
3736 O  O    . PRO   C 44  ? 0.5775 0.7032 0.4670 0.1513  -0.0032 0.0775  48  PRO   C O    
3737 C  CB   . PRO   C 44  ? 0.4698 0.7759 0.4709 0.1216  -0.0118 0.0517  48  PRO   C CB   
3738 C  CG   . PRO   C 44  ? 0.4698 0.7779 0.4717 0.1110  0.0015  0.0483  48  PRO   C CG   
3739 C  CD   . PRO   C 44  ? 0.4381 0.7595 0.4220 0.1185  0.0112  0.0529  48  PRO   C CD   
3740 N  N    . THR   C 52  ? 0.3136 0.5613 0.8342 0.1609  -0.0128 -0.0023 56  THR   C N    
3741 C  CA   . THR   C 52  ? 0.3542 0.5403 0.8151 0.1348  -0.0053 0.0102  56  THR   C CA   
3742 C  C    . THR   C 52  ? 0.3366 0.5063 0.7446 0.1111  0.0049  0.0005  56  THR   C C    
3743 O  O    . THR   C 52  ? 0.3610 0.5704 0.7674 0.1200  0.0105  0.0068  56  THR   C O    
3744 C  CB   . THR   C 52  ? 0.4141 0.5821 0.8257 0.1025  0.0005  0.0192  56  THR   C CB   
3745 N  N    . VAL   C 53  ? 0.3422 0.3678 0.6860 0.0818  -0.0045 -0.0001 57  VAL   C N    
3746 C  CA   . VAL   C 53  ? 0.3223 0.3192 0.6414 0.0568  -0.0056 -0.0005 57  VAL   C CA   
3747 C  C    . VAL   C 53  ? 0.3367 0.3103 0.6106 0.0536  -0.0050 -0.0083 57  VAL   C C    
3748 O  O    . VAL   C 53  ? 0.3267 0.3348 0.6235 0.0669  -0.0202 -0.0086 57  VAL   C O    
3749 C  CB   . VAL   C 53  ? 0.3440 0.3016 0.6337 0.0418  0.0108  0.0082  57  VAL   C CB   
3750 C  CG1  . VAL   C 53  ? 0.3317 0.3115 0.6353 0.0381  0.0142  0.0129  57  VAL   C CG1  
3751 C  CG2  . VAL   C 53  ? 0.3382 0.3004 0.6244 0.0368  0.0294  0.0048  57  VAL   C CG2  
3752 N  N    . PRO   C 54  ? 0.3516 0.2733 0.6103 0.0314  -0.0100 -0.0218 58  PRO   C N    
3753 C  CA   . PRO   C 54  ? 0.3546 0.2716 0.6003 0.0142  -0.0199 -0.0140 58  PRO   C CA   
3754 C  C    . PRO   C 54  ? 0.3526 0.2530 0.5727 0.0195  -0.0465 -0.0164 58  PRO   C C    
3755 O  O    . PRO   C 54  ? 0.3622 0.2282 0.5635 0.0301  -0.0345 -0.0080 58  PRO   C O    
3756 C  CB   . PRO   C 54  ? 0.3763 0.2858 0.6099 0.0103  -0.0116 -0.0074 58  PRO   C CB   
3757 C  CG   . PRO   C 54  ? 0.3795 0.2956 0.6057 0.0125  -0.0064 -0.0004 58  PRO   C CG   
3758 C  CD   . PRO   C 54  ? 0.3756 0.2806 0.6007 0.0217  -0.0038 -0.0160 58  PRO   C CD   
3759 N  N    . PRO   C 55  ? 0.3621 0.2985 0.5668 0.0226  -0.0619 -0.0152 59  PRO   C N    
3760 C  CA   . PRO   C 55  ? 0.3602 0.2966 0.5211 0.0135  -0.0643 0.0010  59  PRO   C CA   
3761 C  C    . PRO   C 55  ? 0.3367 0.2798 0.4602 0.0096  -0.0482 -0.0029 59  PRO   C C    
3762 O  O    . PRO   C 55  ? 0.3218 0.2510 0.4591 0.0176  -0.0442 -0.0264 59  PRO   C O    
3763 C  CB   . PRO   C 55  ? 0.3784 0.3432 0.5504 0.0048  -0.0681 -0.0101 59  PRO   C CB   
3764 C  CG   . PRO   C 55  ? 0.3816 0.3471 0.5827 -0.0077 -0.0629 -0.0118 59  PRO   C CG   
3765 C  CD   . PRO   C 55  ? 0.3857 0.3473 0.5978 -0.0008 -0.0493 -0.0168 59  PRO   C CD   
3766 N  N    . PRO   C 56  ? 0.3412 0.2656 0.3891 0.0086  -0.0431 0.0152  60  PRO   C N    
3767 C  CA   . PRO   C 56  ? 0.3022 0.2491 0.3512 -0.0081 -0.0331 0.0148  60  PRO   C CA   
3768 C  C    . PRO   C 56  ? 0.2535 0.2268 0.2837 0.0024  -0.0256 0.0118  60  PRO   C C    
3769 O  O    . PRO   C 56  ? 0.2692 0.2232 0.3105 0.0122  -0.0373 0.0189  60  PRO   C O    
3770 C  CB   . PRO   C 56  ? 0.3290 0.2921 0.3742 -0.0044 -0.0289 0.0208  60  PRO   C CB   
3771 C  CG   . PRO   C 56  ? 0.3615 0.3199 0.4020 0.0073  -0.0217 0.0318  60  PRO   C CG   
3772 C  CD   . PRO   C 56  ? 0.3547 0.2844 0.4027 0.0044  -0.0307 0.0282  60  PRO   C CD   
3773 N  N    . PRO   C 57  ? 0.2014 0.2129 0.2224 -0.0027 -0.0042 0.0005  61  PRO   C N    
3774 C  CA   . PRO   C 57  ? 0.1954 0.2076 0.2078 -0.0017 0.0033  0.0030  61  PRO   C CA   
3775 C  C    . PRO   C 57  ? 0.1816 0.2030 0.2000 -0.0059 0.0104  0.0052  61  PRO   C C    
3776 O  O    . PRO   C 57  ? 0.1899 0.2180 0.2129 -0.0133 0.0175  0.0144  61  PRO   C O    
3777 C  CB   . PRO   C 57  ? 0.2068 0.2160 0.2149 0.0087  0.0091  0.0044  61  PRO   C CB   
3778 C  CG   . PRO   C 57  ? 0.2080 0.2301 0.2244 0.0019  0.0033  0.0081  61  PRO   C CG   
3779 C  CD   . PRO   C 57  ? 0.2089 0.2218 0.2258 -0.0034 -0.0046 0.0041  61  PRO   C CD   
3780 N  N    . ARG   C 58  ? 0.1705 0.2016 0.1827 -0.0082 0.0145  0.0036  62  ARG   C N    
3781 C  CA   . ARG   C 58  ? 0.1713 0.2007 0.1899 -0.0113 0.0092  -0.0018 62  ARG   C CA   
3782 C  C    . ARG   C 58  ? 0.1654 0.1979 0.1718 -0.0135 0.0100  -0.0024 62  ARG   C C    
3783 O  O    . ARG   C 58  ? 0.1612 0.2021 0.1743 -0.0128 0.0084  0.0094  62  ARG   C O    
3784 C  CB   . ARG   C 58  ? 0.1681 0.2131 0.2021 -0.0129 0.0128  -0.0011 62  ARG   C CB   
3785 C  CG   . ARG   C 58  ? 0.1714 0.2077 0.2040 -0.0198 0.0081  0.0004  62  ARG   C CG   
3786 C  CD   . ARG   C 58  ? 0.1727 0.2144 0.2013 -0.0196 0.0119  0.0016  62  ARG   C CD   
3787 N  NE   . ARG   C 58  ? 0.1821 0.2056 0.1852 -0.0401 -0.0027 0.0077  62  ARG   C NE   
3788 C  CZ   . ARG   C 58  ? 0.1717 0.1923 0.1716 -0.0337 -0.0075 0.0074  62  ARG   C CZ   
3789 N  NH1  . ARG   C 58  ? 0.1669 0.2000 0.1590 -0.0318 -0.0012 0.0122  62  ARG   C NH1  
3790 N  NH2  . ARG   C 58  ? 0.1854 0.1976 0.1816 -0.0424 -0.0076 0.0035  62  ARG   C NH2  
3791 N  N    . VAL   C 59  ? 0.1593 0.2021 0.1496 -0.0154 0.0058  -0.0082 63  VAL   C N    
3792 C  CA   . VAL   C 59  ? 0.1679 0.2007 0.1399 -0.0168 0.0019  -0.0037 63  VAL   C CA   
3793 C  C    . VAL   C 59  ? 0.1632 0.2155 0.1472 -0.0180 0.0010  -0.0049 63  VAL   C C    
3794 O  O    . VAL   C 59  ? 0.1716 0.2868 0.1513 -0.0277 -0.0086 -0.0093 63  VAL   C O    
3795 C  CB   . VAL   C 59  ? 0.1795 0.2053 0.1566 -0.0188 0.0039  0.0018  63  VAL   C CB   
3796 C  CG1  . VAL   C 59  ? 0.1812 0.2102 0.1644 -0.0182 0.0008  0.0031  63  VAL   C CG1  
3797 C  CG2  . VAL   C 59  ? 0.1971 0.2096 0.1874 -0.0275 0.0018  -0.0004 63  VAL   C CG2  
3798 N  N    . VAL   C 60  ? 0.1616 0.2004 0.1451 -0.0179 -0.0021 -0.0037 64  VAL   C N    
3799 C  CA   . VAL   C 60  ? 0.1583 0.1983 0.1677 -0.0166 -0.0003 -0.0077 64  VAL   C CA   
3800 C  C    . VAL   C 60  ? 0.1498 0.1935 0.1500 -0.0295 0.0011  -0.0071 64  VAL   C C    
3801 O  O    . VAL   C 60  ? 0.1711 0.2377 0.1641 -0.0364 0.0016  -0.0083 64  VAL   C O    
3802 C  CB   . VAL   C 60  ? 0.1835 0.2095 0.2124 -0.0152 0.0002  -0.0236 64  VAL   C CB   
3803 C  CG1  . VAL   C 60  ? 0.1912 0.2263 0.2385 -0.0053 0.0040  -0.0256 64  VAL   C CG1  
3804 C  CG2  . VAL   C 60  ? 0.2101 0.2132 0.2362 -0.0209 0.0014  -0.0147 64  VAL   C CG2  
3805 N  N    . ASP   C 61  ? 0.1479 0.1642 0.1334 -0.0293 0.0003  0.0000  65  ASP   C N    
3806 C  CA   . ASP   C 61  ? 0.1507 0.1632 0.1338 -0.0344 -0.0004 -0.0069 65  ASP   C CA   
3807 C  C    . ASP   C 61  ? 0.1476 0.1642 0.1299 -0.0364 0.0001  -0.0120 65  ASP   C C    
3808 O  O    . ASP   C 61  ? 0.1678 0.1730 0.1329 -0.0428 0.0110  -0.0197 65  ASP   C O    
3809 C  CB   . ASP   C 61  ? 0.1612 0.1697 0.1457 -0.0268 -0.0010 -0.0044 65  ASP   C CB   
3810 C  CG   . ASP   C 61  ? 0.1883 0.1785 0.1611 -0.0257 -0.0051 0.0008  65  ASP   C CG   
3811 O  OD1  . ASP   C 61  ? 0.1974 0.1819 0.1622 -0.0215 -0.0111 0.0007  65  ASP   C OD1  
3812 O  OD2  . ASP   C 61  ? 0.1983 0.2078 0.1855 -0.0133 -0.0202 0.0149  65  ASP   C OD2  
3813 N  N    . LYS   C 62  ? 0.1551 0.1585 0.1176 -0.0340 -0.0049 -0.0136 66  LYS   C N    
3814 C  CA   . LYS   C 62  ? 0.1562 0.1660 0.1341 -0.0366 -0.0072 -0.0078 66  LYS   C CA   
3815 C  C    . LYS   C 62  ? 0.1546 0.1622 0.1178 -0.0387 -0.0059 -0.0105 66  LYS   C C    
3816 O  O    . LYS   C 62  ? 0.1511 0.1746 0.1241 -0.0378 -0.0041 -0.0229 66  LYS   C O    
3817 C  CB   . LYS   C 62  ? 0.1783 0.1793 0.1832 -0.0383 -0.0163 0.0073  66  LYS   C CB   
3818 C  CG   . LYS   C 62  ? 0.2242 0.1985 0.2481 -0.0431 -0.0162 0.0240  66  LYS   C CG   
3819 C  CD   . LYS   C 62  ? 0.2711 0.2249 0.2971 -0.0218 -0.0244 0.0340  66  LYS   C CD   
3820 C  CE   . LYS   C 62  ? 0.2928 0.2541 0.3197 -0.0094 -0.0280 0.0337  66  LYS   C CE   
3821 N  NZ   . LYS   C 62  ? 0.3029 0.2412 0.3116 -0.0090 -0.0378 0.0292  66  LYS   C NZ   
3822 N  N    . LEU   C 63  ? 0.1506 0.1667 0.1043 -0.0395 0.0008  -0.0188 67  LEU   C N    
3823 C  CA   . LEU   C 63  ? 0.1461 0.1673 0.1176 -0.0389 -0.0005 -0.0174 67  LEU   C CA   
3824 C  C    . LEU   C 63  ? 0.1535 0.1801 0.1235 -0.0522 -0.0003 -0.0251 67  LEU   C C    
3825 O  O    . LEU   C 63  ? 0.1875 0.2006 0.1238 -0.0723 0.0089  -0.0318 67  LEU   C O    
3826 C  CB   . LEU   C 63  ? 0.1617 0.1727 0.1410 -0.0299 -0.0004 -0.0108 67  LEU   C CB   
3827 C  CG   . LEU   C 63  ? 0.1653 0.1912 0.1608 -0.0169 -0.0029 -0.0041 67  LEU   C CG   
3828 C  CD1  . LEU   C 63  ? 0.1568 0.1954 0.1670 -0.0110 -0.0019 -0.0068 67  LEU   C CD1  
3829 C  CD2  . LEU   C 63  ? 0.1868 0.2145 0.1854 -0.0017 -0.0028 0.0038  67  LEU   C CD2  
3830 N  N    . SER   C 64  ? 0.1432 0.1888 0.1222 -0.0481 0.0013  -0.0282 68  SER   C N    
3831 C  CA   . SER   C 64  ? 0.1565 0.1925 0.1422 -0.0474 0.0092  -0.0315 68  SER   C CA   
3832 C  C    . SER   C 64  ? 0.1524 0.1900 0.1332 -0.0506 0.0122  -0.0326 68  SER   C C    
3833 O  O    . SER   C 64  ? 0.1713 0.2148 0.1329 -0.0541 0.0034  -0.0300 68  SER   C O    
3834 C  CB   . SER   C 64  ? 0.1912 0.2134 0.1957 -0.0399 0.0092  -0.0265 68  SER   C CB   
3835 O  OG   . SER   C 64  ? 0.2451 0.2332 0.2692 -0.0381 0.0198  -0.0280 68  SER   C OG   
3836 N  N    . LEU   C 65  ? 0.1570 0.1870 0.1171 -0.0413 0.0095  -0.0344 69  LEU   C N    
3837 C  CA   . LEU   C 65  ? 0.1559 0.1906 0.1297 -0.0361 0.0132  -0.0290 69  LEU   C CA   
3838 C  C    . LEU   C 65  ? 0.1532 0.1780 0.1189 -0.0287 0.0122  -0.0264 69  LEU   C C    
3839 O  O    . LEU   C 65  ? 0.1657 0.1775 0.1188 -0.0334 0.0085  -0.0228 69  LEU   C O    
3840 C  CB   . LEU   C 65  ? 0.1897 0.1989 0.1552 -0.0214 0.0135  -0.0335 69  LEU   C CB   
3841 C  CG   . LEU   C 65  ? 0.2156 0.2111 0.1747 -0.0239 0.0114  -0.0324 69  LEU   C CG   
3842 C  CD1  . LEU   C 65  ? 0.2270 0.2208 0.1914 -0.0171 0.0063  -0.0336 69  LEU   C CD1  
3843 C  CD2  . LEU   C 65  ? 0.2361 0.2167 0.1808 -0.0230 0.0126  -0.0419 69  LEU   C CD2  
3844 N  N    . CYS   C 66  ? 0.1452 0.1756 0.1168 -0.0292 0.0044  -0.0189 70  CYS   C N    
3845 C  CA   . CYS   C 66  ? 0.1442 0.1732 0.1279 -0.0200 0.0101  -0.0167 70  CYS   C CA   
3846 C  C    . CYS   C 66  ? 0.1378 0.1682 0.1289 -0.0194 0.0039  -0.0193 70  CYS   C C    
3847 O  O    . CYS   C 66  ? 0.1405 0.1717 0.1454 -0.0203 0.0011  -0.0216 70  CYS   C O    
3848 C  CB   . CYS   C 66  ? 0.1593 0.1877 0.1346 -0.0112 0.0157  -0.0070 70  CYS   C CB   
3849 S  SG   . CYS   C 66  ? 0.1880 0.2237 0.1848 0.0081  0.0152  0.0111  70  CYS   C SG   
3850 N  N    . VAL   C 67  ? 0.1338 0.1647 0.1251 -0.0192 0.0081  -0.0191 71  VAL   C N    
3851 C  CA   . VAL   C 67  ? 0.1338 0.1694 0.1242 -0.0171 0.0067  -0.0215 71  VAL   C CA   
3852 C  C    . VAL   C 67  ? 0.1335 0.1738 0.1329 -0.0165 0.0060  -0.0199 71  VAL   C C    
3853 O  O    . VAL   C 67  ? 0.1364 0.1796 0.1494 -0.0173 0.0144  -0.0254 71  VAL   C O    
3854 C  CB   . VAL   C 67  ? 0.1410 0.1765 0.1281 -0.0142 0.0059  -0.0205 71  VAL   C CB   
3855 C  CG1  . VAL   C 67  ? 0.1427 0.1816 0.1305 -0.0092 0.0067  -0.0210 71  VAL   C CG1  
3856 C  CG2  . VAL   C 67  ? 0.1518 0.1677 0.1314 -0.0141 0.0075  -0.0185 71  VAL   C CG2  
3857 N  N    . ALA   C 68  ? 0.1293 0.1762 0.1436 -0.0183 0.0055  -0.0288 72  ALA   C N    
3858 C  CA   . ALA   C 68  ? 0.1312 0.1867 0.1542 -0.0195 0.0000  -0.0270 72  ALA   C CA   
3859 C  C    . ALA   C 68  ? 0.1333 0.1891 0.1623 -0.0208 -0.0044 -0.0248 72  ALA   C C    
3860 O  O    . ALA   C 68  ? 0.1652 0.2020 0.1779 -0.0270 -0.0250 -0.0140 72  ALA   C O    
3861 C  CB   . ALA   C 68  ? 0.1323 0.2021 0.1689 -0.0134 0.0048  -0.0308 72  ALA   C CB   
3862 N  N    . PRO   C 69  ? 0.1482 0.1970 0.1835 -0.0203 -0.0022 -0.0299 73  PRO   C N    
3863 C  CA   . PRO   C 69  ? 0.1627 0.2129 0.2013 -0.0246 -0.0102 -0.0327 73  PRO   C CA   
3864 C  C    . PRO   C 69  ? 0.1689 0.2367 0.2562 -0.0181 -0.0165 -0.0364 73  PRO   C C    
3865 O  O    . PRO   C 69  ? 0.1708 0.2607 0.2764 -0.0139 0.0199  -0.0212 73  PRO   C O    
3866 C  CB   . PRO   C 69  ? 0.1736 0.2115 0.1994 -0.0284 -0.0053 -0.0421 73  PRO   C CB   
3867 C  CG   . PRO   C 69  ? 0.1647 0.2016 0.2116 -0.0229 -0.0054 -0.0424 73  PRO   C CG   
3868 C  CD   . PRO   C 69  ? 0.1544 0.2016 0.1958 -0.0216 -0.0042 -0.0335 73  PRO   C CD   
3869 N  N    . GLY   C 70  ? 0.1996 0.2734 0.3100 -0.0276 -0.0454 -0.0430 74  GLY   C N    
3870 C  CA   . GLY   C 70  ? 0.2002 0.3001 0.3507 -0.0266 -0.0188 -0.0630 74  GLY   C CA   
3871 C  C    . GLY   C 70  ? 0.2027 0.3130 0.3651 -0.0395 -0.0053 -0.0899 74  GLY   C C    
3872 O  O    . GLY   C 70  ? 0.2052 0.3558 0.4233 -0.0392 0.0203  -0.1131 74  GLY   C O    
3873 N  N    . LYS   C 71  ? 0.1921 0.3193 0.3601 -0.0469 0.0132  -0.0978 75  LYS   C N    
3874 C  CA   . LYS   C 71  ? 0.1998 0.3204 0.3138 -0.0435 0.0173  -0.0912 75  LYS   C CA   
3875 C  C    . LYS   C 71  ? 0.2274 0.3120 0.2959 -0.0512 0.0268  -0.0858 75  LYS   C C    
3876 O  O    . LYS   C 71  ? 0.2373 0.3200 0.2793 -0.0606 0.0237  -0.0944 75  LYS   C O    
3877 C  CB   . LYS   C 71  ? 0.1879 0.3234 0.3155 -0.0564 0.0015  -0.0843 75  LYS   C CB   
3878 C  CG   . LYS   C 71  ? 0.1994 0.3262 0.2873 -0.0454 0.0020  -0.0846 75  LYS   C CG   
3879 C  CD   . LYS   C 71  ? 0.2092 0.3331 0.2861 -0.0388 0.0068  -0.0773 75  LYS   C CD   
3880 C  CE   . LYS   C 71  ? 0.2242 0.3405 0.2784 -0.0418 0.0006  -0.0750 75  LYS   C CE   
3881 N  NZ   . LYS   C 71  ? 0.2323 0.3418 0.2772 -0.0413 -0.0015 -0.0755 75  LYS   C NZ   
3882 N  N    . ALA   C 72  ? 0.2153 0.3030 0.2867 -0.0559 0.0379  -0.0630 76  ALA   C N    
3883 C  CA   . ALA   C 72  ? 0.2400 0.3036 0.2836 -0.0563 0.0296  -0.0553 76  ALA   C CA   
3884 C  C    . ALA   C 72  ? 0.2378 0.2717 0.2280 -0.0527 0.0208  -0.0412 76  ALA   C C    
3885 O  O    . ALA   C 72  ? 0.2207 0.2898 0.2366 -0.0417 0.0006  -0.0429 76  ALA   C O    
3886 C  CB   . ALA   C 72  ? 0.2767 0.3145 0.3072 -0.0595 0.0356  -0.0481 76  ALA   C CB   
3887 N  N    . CYS   C 73  ? 0.2793 0.2652 0.2084 -0.0470 0.0110  -0.0271 77  CYS   C N    
3888 C  CA   . CYS   C 73  ? 0.2783 0.2423 0.2012 -0.0553 0.0063  -0.0041 77  CYS   C CA   
3889 C  C    . CYS   C 73  ? 0.2563 0.2381 0.2007 -0.0618 -0.0049 0.0008  77  CYS   C C    
3890 O  O    . CYS   C 73  ? 0.2833 0.2515 0.2227 -0.0709 0.0043  0.0158  77  CYS   C O    
3891 C  CB   . CYS   C 73  ? 0.3040 0.2436 0.2184 -0.0485 -0.0089 -0.0015 77  CYS   C CB   
3892 S  SG   . CYS   C 73  ? 0.3348 0.2772 0.2200 -0.0806 -0.0145 0.0057  77  CYS   C SG   
3893 N  N    . SER   C 74  ? 0.2430 0.2068 0.1954 -0.0664 -0.0227 -0.0102 78  SER   C N    
3894 C  CA   . SER   C 74  ? 0.2707 0.2118 0.2430 -0.0520 -0.0366 -0.0064 78  SER   C CA   
3895 C  C    . SER   C 74  ? 0.2645 0.2032 0.2469 -0.0570 -0.0426 -0.0121 78  SER   C C    
3896 O  O    . SER   C 74  ? 0.2680 0.1999 0.2448 -0.0499 -0.0518 -0.0247 78  SER   C O    
3897 C  CB   . SER   C 74  ? 0.3014 0.2335 0.2447 -0.0396 -0.0506 -0.0193 78  SER   C CB   
3898 O  OG   . SER   C 74  ? 0.3132 0.2716 0.2240 -0.0218 -0.0459 -0.0293 78  SER   C OG   
3899 N  N    . PRO   C 75  ? 0.2575 0.1983 0.2738 -0.0694 -0.0536 -0.0100 79  PRO   C N    
3900 C  CA   . PRO   C 75  ? 0.2649 0.1959 0.2679 -0.0616 -0.0606 -0.0103 79  PRO   C CA   
3901 C  C    . PRO   C 75  ? 0.2713 0.1887 0.2231 -0.0485 -0.0629 -0.0091 79  PRO   C C    
3902 O  O    . PRO   C 75  ? 0.2783 0.1978 0.2226 -0.0478 -0.0727 -0.0208 79  PRO   C O    
3903 C  CB   . PRO   C 75  ? 0.2777 0.1941 0.3047 -0.0618 -0.0553 -0.0045 79  PRO   C CB   
3904 C  CG   . PRO   C 75  ? 0.2683 0.2228 0.3168 -0.0757 -0.0630 -0.0025 79  PRO   C CG   
3905 C  CD   . PRO   C 75  ? 0.2584 0.2226 0.3115 -0.0684 -0.0662 -0.0081 79  PRO   C CD   
3906 N  N    . ALA   C 76  ? 0.2796 0.2080 0.2118 -0.0416 -0.0697 -0.0192 80  ALA   C N    
3907 C  CA   . ALA   C 76  ? 0.3011 0.2386 0.2082 -0.0268 -0.0608 -0.0125 80  ALA   C CA   
3908 C  C    . ALA   C 76  ? 0.2935 0.2255 0.1994 -0.0174 -0.0426 -0.0105 80  ALA   C C    
3909 O  O    . ALA   C 76  ? 0.2975 0.2379 0.2213 -0.0149 -0.0334 -0.0001 80  ALA   C O    
3910 C  CB   . ALA   C 76  ? 0.3377 0.2551 0.2166 -0.0286 -0.0640 -0.0279 80  ALA   C CB   
3911 N  N    . ALA   C 77  ? 0.2840 0.2322 0.1731 -0.0153 -0.0295 -0.0035 81  ALA   C N    
3912 C  CA   . ALA   C 77  ? 0.2642 0.2327 0.1843 -0.0226 -0.0094 0.0053  81  ALA   C CA   
3913 C  C    . ALA   C 77  ? 0.2410 0.2132 0.1895 -0.0434 -0.0079 0.0055  81  ALA   C C    
3914 O  O    . ALA   C 77  ? 0.2395 0.2250 0.2015 -0.0617 0.0001  0.0152  81  ALA   C O    
3915 C  CB   . ALA   C 77  ? 0.2793 0.2306 0.1861 -0.0199 -0.0134 0.0224  81  ALA   C CB   
3916 N  N    . SER   C 78  ? 0.2299 0.1952 0.1789 -0.0602 -0.0117 -0.0032 82  SER   C N    
3917 C  CA   . SER   C 78  ? 0.2370 0.2113 0.1874 -0.0658 -0.0146 -0.0078 82  SER   C CA   
3918 C  C    . SER   C 78  ? 0.2342 0.2073 0.2050 -0.0679 -0.0289 0.0004  82  SER   C C    
3919 O  O    . SER   C 78  ? 0.2441 0.2181 0.2405 -0.0697 -0.0485 -0.0193 82  SER   C O    
3920 C  CB   . SER   C 78  ? 0.2538 0.2355 0.1845 -0.0687 -0.0085 -0.0138 82  SER   C CB   
3921 O  OG   . SER   C 78  ? 0.2663 0.2658 0.2055 -0.0561 -0.0067 -0.0202 82  SER   C OG   
3922 N  N    . GLU   C 79  ? 0.2399 0.1966 0.2374 -0.0593 -0.0360 -0.0056 83  GLU   C N    
3923 C  CA   . GLU   C 79  ? 0.2701 0.2111 0.2946 -0.0417 -0.0502 -0.0054 83  GLU   C CA   
3924 C  C    . GLU   C 79  ? 0.2625 0.2269 0.3420 -0.0179 -0.0408 -0.0133 83  GLU   C C    
3925 O  O    . GLU   C 79  ? 0.2662 0.3185 0.3752 -0.0185 -0.0786 -0.0056 83  GLU   C O    
3926 C  CB   . GLU   C 79  ? 0.3052 0.2042 0.3479 -0.0384 -0.0435 -0.0083 83  GLU   C CB   
3927 C  CG   . GLU   C 79  ? 0.3392 0.2715 0.3716 -0.0460 -0.0415 -0.0013 83  GLU   C CG   
3928 C  CD   . GLU   C 79  ? 0.3712 0.2938 0.4082 -0.0602 -0.0649 -0.0175 83  GLU   C CD   
3929 O  OE1  . GLU   C 79  ? 0.4313 0.3459 0.4523 -0.0611 -0.0488 -0.0550 83  GLU   C OE1  
3930 O  OE2  . GLU   C 79  ? 0.4247 0.3604 0.4579 -0.0446 -0.0857 0.0312  83  GLU   C OE2  
3931 N  N    . ILE   C 80  ? 0.2719 0.2283 0.3660 -0.0315 -0.0311 -0.0119 84  ILE   C N    
3932 C  CA   . ILE   C 80  ? 0.2657 0.2788 0.4210 -0.0255 -0.0104 -0.0122 84  ILE   C CA   
3933 C  C    . ILE   C 80  ? 0.2753 0.2468 0.4800 -0.0326 0.0089  -0.0319 84  ILE   C C    
3934 O  O    . ILE   C 80  ? 0.2913 0.2405 0.5485 -0.0300 0.0048  -0.0437 84  ILE   C O    
3935 C  CB   . ILE   C 80  ? 0.3235 0.3424 0.4467 -0.0459 0.0074  0.0068  84  ILE   C CB   
3936 C  CG1  . ILE   C 80  ? 0.3580 0.3843 0.4508 -0.0351 -0.0091 -0.0044 84  ILE   C CG1  
3937 C  CG2  . ILE   C 80  ? 0.3312 0.3750 0.4504 -0.0585 0.0227  0.0064  84  ILE   C CG2  
3938 C  CD1  . ILE   C 80  ? 0.3709 0.4253 0.4732 -0.0268 -0.0116 -0.0029 84  ILE   C CD1  
3939 N  N    . THR   C 81  ? 0.2324 0.2548 0.4649 -0.0454 0.0380  -0.0261 85  THR   C N    
3940 C  CA   . THR   C 81  ? 0.2354 0.2546 0.4624 -0.0442 0.0232  -0.0318 85  THR   C CA   
3941 C  C    . THR   C 81  ? 0.2361 0.2563 0.4643 -0.0467 -0.0105 -0.0608 85  THR   C C    
3942 O  O    . THR   C 81  ? 0.2606 0.2783 0.5016 -0.0904 -0.0173 -0.0804 85  THR   C O    
3943 C  CB   . THR   C 81  ? 0.2360 0.2707 0.4651 -0.0308 0.0731  -0.0189 85  THR   C CB   
3944 O  OG1  . THR   C 81  ? 0.2255 0.2278 0.4371 -0.0439 0.0872  -0.0176 85  THR   C OG1  
3945 C  CG2  . THR   C 81  ? 0.2771 0.2730 0.4669 -0.0261 0.0882  0.0032  85  THR   C CG2  
3946 N  N    . GLY   C 82  ? 0.2346 0.2676 0.3900 -0.0342 -0.0261 -0.0482 86  GLY   C N    
3947 C  CA   . GLY   C 82  ? 0.2842 0.3012 0.3752 -0.0402 -0.0383 -0.0510 86  GLY   C CA   
3948 C  C    . GLY   C 82  ? 0.3204 0.3008 0.2971 -0.0276 -0.0276 -0.0407 86  GLY   C C    
3949 O  O    . GLY   C 82  ? 0.4770 0.3437 0.3259 -0.0221 -0.0593 -0.0843 86  GLY   C O    
3950 N  N    . LEU   C 83  ? 0.2404 0.2703 0.2568 -0.0572 -0.0229 -0.0462 87  LEU   C N    
3951 C  CA   . LEU   C 83  ? 0.2076 0.2576 0.2057 -0.0589 -0.0107 -0.0436 87  LEU   C CA   
3952 C  C    . LEU   C 83  ? 0.2039 0.2689 0.2037 -0.0507 -0.0096 -0.0578 87  LEU   C C    
3953 O  O    . LEU   C 83  ? 0.2262 0.2679 0.2472 -0.0502 0.0134  -0.0839 87  LEU   C O    
3954 C  CB   . LEU   C 83  ? 0.2008 0.2553 0.2090 -0.0424 -0.0091 -0.0375 87  LEU   C CB   
3955 C  CG   . LEU   C 83  ? 0.1905 0.2401 0.2159 -0.0282 0.0092  -0.0185 87  LEU   C CG   
3956 C  CD1  . LEU   C 83  ? 0.1921 0.2392 0.2370 -0.0162 0.0148  -0.0144 87  LEU   C CD1  
3957 C  CD2  . LEU   C 83  ? 0.1960 0.2462 0.2323 -0.0274 0.0039  -0.0173 87  LEU   C CD2  
3958 N  N    . SER   C 84  ? 0.2208 0.2545 0.1964 -0.0445 -0.0092 -0.0573 88  SER   C N    
3959 C  CA   . SER   C 84  ? 0.2235 0.2380 0.1907 -0.0394 0.0000  -0.0503 88  SER   C CA   
3960 C  C    . SER   C 84  ? 0.2184 0.2348 0.1952 -0.0315 0.0023  -0.0464 88  SER   C C    
3961 O  O    . SER   C 84  ? 0.2113 0.2387 0.1634 -0.0400 -0.0007 -0.0366 88  SER   C O    
3962 C  CB   . SER   C 84  ? 0.2485 0.2352 0.2043 -0.0411 -0.0006 -0.0422 88  SER   C CB   
3963 O  OG   . SER   C 84  ? 0.2786 0.2325 0.2112 -0.0533 0.0097  -0.0457 88  SER   C OG   
3964 N  N    A THR   C 85  ? 0.2179 0.2340 0.2011 -0.0258 -0.0009 -0.0589 89  THR   C N    
3965 N  N    B THR   C 85  ? 0.2216 0.2389 0.2211 -0.0317 -0.0002 -0.0530 89  THR   C N    
3966 C  CA   A THR   C 85  ? 0.2167 0.2440 0.2206 -0.0165 -0.0012 -0.0604 89  THR   C CA   
3967 C  CA   B THR   C 85  ? 0.2299 0.2472 0.2559 -0.0252 0.0047  -0.0515 89  THR   C CA   
3968 C  C    A THR   C 85  ? 0.2145 0.2352 0.2280 -0.0203 0.0073  -0.0593 89  THR   C C    
3969 C  C    B THR   C 85  ? 0.2197 0.2356 0.2529 -0.0243 0.0081  -0.0535 89  THR   C C    
3970 O  O    A THR   C 85  ? 0.2223 0.2268 0.2390 -0.0219 -0.0045 -0.0593 89  THR   C O    
3971 O  O    B THR   C 85  ? 0.2230 0.2258 0.2541 -0.0222 -0.0076 -0.0527 89  THR   C O    
3972 C  CB   A THR   C 85  ? 0.2193 0.2605 0.2108 -0.0060 0.0031  -0.0617 89  THR   C CB   
3973 C  CB   B THR   C 85  ? 0.2366 0.2742 0.2804 -0.0220 0.0083  -0.0450 89  THR   C CB   
3974 O  OG1  A THR   C 85  ? 0.2077 0.2800 0.2077 0.0061  -0.0136 -0.0750 89  THR   C OG1  
3975 O  OG1  B THR   C 85  ? 0.2482 0.2836 0.3615 -0.0316 0.0082  -0.0344 89  THR   C OG1  
3976 C  CG2  A THR   C 85  ? 0.2132 0.2551 0.1978 -0.0057 -0.0017 -0.0619 89  THR   C CG2  
3977 C  CG2  B THR   C 85  ? 0.2304 0.2746 0.2762 -0.0206 0.0048  -0.0449 89  THR   C CG2  
3978 N  N    . ALA   C 86  ? 0.2205 0.2396 0.2430 -0.0309 0.0107  -0.0585 90  ALA   C N    
3979 C  CA   . ALA   C 86  ? 0.2377 0.2374 0.2409 -0.0335 0.0313  -0.0468 90  ALA   C CA   
3980 C  C    . ALA   C 86  ? 0.2270 0.2267 0.2025 -0.0328 0.0341  -0.0301 90  ALA   C C    
3981 O  O    . ALA   C 86  ? 0.2553 0.2393 0.1918 -0.0577 0.0424  -0.0283 90  ALA   C O    
3982 C  CB   . ALA   C 86  ? 0.2610 0.2420 0.2609 -0.0373 0.0430  -0.0533 90  ALA   C CB   
3983 N  N    . VAL   C 87  ? 0.2175 0.2179 0.1895 -0.0285 0.0245  -0.0119 91  VAL   C N    
3984 C  CA   . VAL   C 87  ? 0.2260 0.2134 0.1864 -0.0272 0.0051  -0.0006 91  VAL   C CA   
3985 C  C    . VAL   C 87  ? 0.2017 0.2092 0.1589 -0.0240 0.0014  -0.0092 91  VAL   C C    
3986 O  O    . VAL   C 87  ? 0.1910 0.2107 0.1551 -0.0285 -0.0064 -0.0053 91  VAL   C O    
3987 C  CB   . VAL   C 87  ? 0.2454 0.2237 0.2471 -0.0154 -0.0038 0.0059  91  VAL   C CB   
3988 C  CG1  . VAL   C 87  ? 0.2436 0.2423 0.2872 -0.0035 -0.0106 0.0066  91  VAL   C CG1  
3989 C  CG2  . VAL   C 87  ? 0.2847 0.2336 0.2764 -0.0225 -0.0083 0.0077  91  VAL   C CG2  
3990 N  N    . LEU   C 88  ? 0.1959 0.1996 0.1466 -0.0220 0.0071  -0.0169 92  LEU   C N    
3991 C  CA   . LEU   C 88  ? 0.1998 0.1982 0.1422 -0.0204 0.0104  -0.0156 92  LEU   C CA   
3992 C  C    . LEU   C 88  ? 0.2104 0.2008 0.1461 -0.0199 0.0091  -0.0226 92  LEU   C C    
3993 O  O    . LEU   C 88  ? 0.2170 0.2025 0.1286 -0.0147 0.0041  -0.0274 92  LEU   C O    
3994 C  CB   . LEU   C 88  ? 0.2101 0.1947 0.1443 -0.0196 0.0079  -0.0119 92  LEU   C CB   
3995 C  CG   . LEU   C 88  ? 0.2180 0.1992 0.1531 -0.0214 0.0148  -0.0187 92  LEU   C CG   
3996 C  CD1  . LEU   C 88  ? 0.2269 0.2080 0.1517 -0.0226 0.0192  -0.0244 92  LEU   C CD1  
3997 C  CD2  . LEU   C 88  ? 0.2291 0.1947 0.1685 -0.0260 0.0191  -0.0235 92  LEU   C CD2  
3998 N  N    . ALA   C 89  ? 0.2117 0.2152 0.1665 -0.0237 0.0126  -0.0315 93  ALA   C N    
3999 C  CA   . ALA   C 89  ? 0.2179 0.2182 0.1831 -0.0257 0.0246  -0.0350 93  ALA   C CA   
4000 C  C    . ALA   C 89  ? 0.2286 0.2179 0.1806 -0.0277 0.0238  -0.0240 93  ALA   C C    
4001 O  O    . ALA   C 89  ? 0.2587 0.2283 0.2081 -0.0188 0.0410  -0.0329 93  ALA   C O    
4002 C  CB   . ALA   C 89  ? 0.2245 0.2486 0.2145 -0.0319 0.0264  -0.0365 93  ALA   C CB   
4003 N  N    . ALA   C 90  ? 0.2438 0.2121 0.1563 -0.0280 0.0198  -0.0218 94  ALA   C N    
4004 C  CA   . ALA   C 90  ? 0.2676 0.2120 0.1479 -0.0279 0.0175  -0.0130 94  ALA   C CA   
4005 C  C    . ALA   C 90  ? 0.2599 0.2162 0.1334 -0.0263 0.0052  -0.0064 94  ALA   C C    
4006 O  O    . ALA   C 90  ? 0.3211 0.2521 0.1225 -0.0292 -0.0042 0.0071  94  ALA   C O    
4007 C  CB   . ALA   C 90  ? 0.2881 0.2149 0.1505 -0.0262 0.0178  -0.0092 94  ALA   C CB   
4008 N  N    . HIS   C 91  ? 0.2481 0.2050 0.1190 -0.0369 -0.0057 -0.0012 95  HIS   C N    
4009 C  CA   . HIS   C 91  ? 0.2488 0.2099 0.1268 -0.0354 -0.0073 -0.0059 95  HIS   C CA   
4010 C  C    . HIS   C 91  ? 0.2452 0.2088 0.1153 -0.0305 -0.0021 -0.0074 95  HIS   C C    
4011 O  O    . HIS   C 91  ? 0.2528 0.2326 0.1212 -0.0410 -0.0051 -0.0079 95  HIS   C O    
4012 C  CB   . HIS   C 91  ? 0.2398 0.2082 0.1557 -0.0375 -0.0026 -0.0038 95  HIS   C CB   
4013 C  CG   . HIS   C 91  ? 0.2502 0.2143 0.1667 -0.0324 -0.0033 0.0068  95  HIS   C CG   
4014 N  ND1  . HIS   C 91  ? 0.2623 0.2196 0.2027 -0.0258 -0.0042 0.0120  95  HIS   C ND1  
4015 C  CD2  . HIS   C 91  ? 0.2534 0.2162 0.1833 -0.0304 -0.0064 0.0009  95  HIS   C CD2  
4016 C  CE1  . HIS   C 91  ? 0.2570 0.2190 0.2214 -0.0220 -0.0055 0.0129  95  HIS   C CE1  
4017 N  NE2  . HIS   C 91  ? 0.2640 0.2328 0.2175 -0.0197 -0.0106 0.0039  95  HIS   C NE2  
4018 N  N    . GLY   C 92  ? 0.2466 0.2078 0.1369 -0.0202 0.0099  -0.0084 96  GLY   C N    
4019 C  CA   . GLY   C 92  ? 0.2389 0.2086 0.1308 -0.0186 0.0079  -0.0038 96  GLY   C CA   
4020 C  C    . GLY   C 92  ? 0.2293 0.2047 0.1312 -0.0166 0.0073  -0.0032 96  GLY   C C    
4021 O  O    . GLY   C 92  ? 0.2737 0.2136 0.1443 -0.0174 0.0054  -0.0058 96  GLY   C O    
4022 N  N    . ARG   C 93  ? 0.1965 0.1893 0.1250 -0.0166 0.0003  0.0010  97  ARG   C N    
4023 C  CA   . ARG   C 93  ? 0.1777 0.1911 0.1222 -0.0142 0.0067  -0.0060 97  ARG   C CA   
4024 C  C    . ARG   C 93  ? 0.1601 0.1968 0.1178 -0.0105 0.0124  -0.0086 97  ARG   C C    
4025 O  O    . ARG   C 93  ? 0.1655 0.2180 0.1454 -0.0062 0.0084  -0.0042 97  ARG   C O    
4026 C  CB   . ARG   C 93  ? 0.1697 0.1980 0.1181 -0.0158 0.0105  -0.0091 97  ARG   C CB   
4027 C  CG   . ARG   C 93  ? 0.1743 0.1949 0.1272 -0.0173 0.0048  -0.0132 97  ARG   C CG   
4028 C  CD   . ARG   C 93  ? 0.1749 0.2035 0.1368 -0.0212 0.0023  -0.0135 97  ARG   C CD   
4029 N  NE   . ARG   C 93  ? 0.1786 0.2077 0.1472 -0.0274 0.0016  -0.0213 97  ARG   C NE   
4030 C  CZ   . ARG   C 93  ? 0.2024 0.2145 0.1799 -0.0283 -0.0044 -0.0336 97  ARG   C CZ   
4031 N  NH1  . ARG   C 93  ? 0.1988 0.2087 0.2046 -0.0302 -0.0039 -0.0371 97  ARG   C NH1  
4032 N  NH2  . ARG   C 93  ? 0.2248 0.2353 0.1871 -0.0311 -0.0085 -0.0429 97  ARG   C NH2  
4033 N  N    . GLN   C 94  ? 0.1526 0.1887 0.1247 0.0006  0.0055  -0.0075 98  GLN   C N    
4034 C  CA   . GLN   C 94  ? 0.1655 0.1933 0.1225 0.0005  0.0104  -0.0081 98  GLN   C CA   
4035 C  C    . GLN   C 94  ? 0.1506 0.1894 0.1315 0.0037  0.0129  -0.0134 98  GLN   C C    
4036 O  O    . GLN   C 94  ? 0.1518 0.1698 0.1351 0.0012  0.0181  -0.0196 98  GLN   C O    
4037 C  CB   . GLN   C 94  ? 0.1925 0.2005 0.1420 0.0000  0.0117  -0.0206 98  GLN   C CB   
4038 C  CG   . GLN   C 94  ? 0.2330 0.2276 0.1603 -0.0025 0.0178  -0.0333 98  GLN   C CG   
4039 C  CD   . GLN   C 94  ? 0.2711 0.2530 0.2109 -0.0160 0.0094  -0.0408 98  GLN   C CD   
4040 O  OE1  . GLN   C 94  ? 0.2357 0.2341 0.2510 -0.0095 -0.0052 -0.0277 98  GLN   C OE1  
4041 N  NE2  . GLN   C 94  ? 0.3447 0.3083 0.2416 -0.0343 0.0096  -0.0539 98  GLN   C NE2  
4042 N  N    . CYS   C 95  ? 0.1517 0.2106 0.1310 0.0107  0.0093  -0.0084 99  CYS   C N    
4043 C  CA   . CYS   C 95  ? 0.1551 0.2197 0.1369 0.0001  -0.0012 -0.0063 99  CYS   C CA   
4044 C  C    . CYS   C 95  ? 0.1419 0.1961 0.1490 -0.0010 -0.0022 -0.0058 99  CYS   C C    
4045 O  O    . CYS   C 95  ? 0.1533 0.1960 0.1495 -0.0036 -0.0065 0.0033  99  CYS   C O    
4046 C  CB   . CYS   C 95  ? 0.1609 0.2580 0.1443 0.0067  -0.0090 -0.0036 99  CYS   C CB   
4047 S  SG   . CYS   C 95  ? 0.1736 0.3269 0.2177 0.0432  0.0047  0.0078  99  CYS   C SG   
4048 N  N    . PHE   C 96  ? 0.1449 0.1888 0.1520 -0.0070 -0.0010 -0.0031 100 PHE   C N    
4049 C  CA   . PHE   C 96  ? 0.1565 0.1861 0.1700 -0.0033 0.0001  -0.0008 100 PHE   C CA   
4050 C  C    . PHE   C 96  ? 0.1570 0.1886 0.2035 0.0015  -0.0099 -0.0013 100 PHE   C C    
4051 O  O    . PHE   C 96  ? 0.1916 0.2152 0.2364 0.0140  -0.0427 -0.0081 100 PHE   C O    
4052 C  CB   . PHE   C 96  ? 0.1755 0.1955 0.1685 -0.0058 0.0069  -0.0044 100 PHE   C CB   
4053 C  CG   . PHE   C 96  ? 0.1937 0.2166 0.1714 -0.0076 0.0184  -0.0017 100 PHE   C CG   
4054 C  CD1  . PHE   C 96  ? 0.2123 0.2269 0.1843 -0.0020 0.0337  0.0026  100 PHE   C CD1  
4055 C  CD2  . PHE   C 96  ? 0.2096 0.2190 0.1722 -0.0094 0.0233  -0.0101 100 PHE   C CD2  
4056 C  CE1  . PHE   C 96  ? 0.2343 0.2423 0.1970 -0.0064 0.0461  0.0024  100 PHE   C CE1  
4057 C  CE2  . PHE   C 96  ? 0.2167 0.2464 0.1765 -0.0067 0.0238  -0.0167 100 PHE   C CE2  
4058 C  CZ   . PHE   C 96  ? 0.2176 0.2534 0.1820 -0.0132 0.0338  -0.0066 100 PHE   C CZ   
4059 N  N    . ASP   C 97  ? 0.1424 0.1852 0.2153 0.0046  -0.0067 -0.0047 101 ASP   C N    
4060 C  CA   . ASP   C 97  ? 0.1651 0.1900 0.2328 0.0112  -0.0015 0.0002  101 ASP   C CA   
4061 C  C    . ASP   C 97  ? 0.1715 0.1823 0.2559 0.0168  -0.0042 0.0046  101 ASP   C C    
4062 O  O    . ASP   C 97  ? 0.1782 0.1836 0.2359 0.0229  -0.0075 0.0223  101 ASP   C O    
4063 C  CB   . ASP   C 97  ? 0.1861 0.2205 0.2436 0.0089  0.0081  -0.0093 101 ASP   C CB   
4064 C  CG   . ASP   C 97  ? 0.2105 0.2819 0.2489 0.0163  0.0080  -0.0076 101 ASP   C CG   
4065 O  OD1  . ASP   C 97  ? 0.2001 0.2439 0.2553 0.0029  -0.0005 -0.0250 101 ASP   C OD1  
4066 O  OD2  . ASP   C 97  ? 0.2531 0.3592 0.2656 0.0411  0.0263  -0.0103 101 ASP   C OD2  
4067 N  N    . ASP   C 98  ? 0.1764 0.1888 0.3027 0.0292  -0.0026 0.0077  102 ASP   C N    
4068 C  CA   . ASP   C 98  ? 0.2017 0.1934 0.3278 0.0264  -0.0048 0.0129  102 ASP   C CA   
4069 C  C    . ASP   C 98  ? 0.1942 0.1826 0.3351 0.0234  0.0023  0.0034  102 ASP   C C    
4070 O  O    . ASP   C 98  ? 0.1767 0.2022 0.3487 0.0127  -0.0078 0.0205  102 ASP   C O    
4071 C  CB   . ASP   C 98  ? 0.2192 0.2082 0.3666 0.0392  0.0038  0.0103  102 ASP   C CB   
4072 C  CG   . ASP   C 98  ? 0.2933 0.2771 0.4009 0.0502  -0.0123 0.0034  102 ASP   C CG   
4073 O  OD1  . ASP   C 98  ? 0.3736 0.3314 0.4246 0.0542  -0.0189 -0.0196 102 ASP   C OD1  
4074 O  OD2  . ASP   C 98  ? 0.3308 0.3503 0.4810 0.1081  -0.0119 0.0123  102 ASP   C OD2  
4075 N  N    . ASN   C 99  ? 0.1801 0.1811 0.3207 0.0181  0.0023  -0.0125 103 ASN   C N    
4076 C  CA   . ASN   C 99  ? 0.1821 0.1899 0.3302 0.0150  0.0004  -0.0221 103 ASN   C CA   
4077 C  C    . ASN   C 99  ? 0.1701 0.1846 0.3097 0.0046  -0.0005 -0.0304 103 ASN   C C    
4078 O  O    . ASN   C 99  ? 0.1600 0.1802 0.3181 0.0009  0.0011  -0.0385 103 ASN   C O    
4079 C  CB   . ASN   C 99  ? 0.1866 0.2025 0.3276 0.0162  -0.0011 -0.0370 103 ASN   C CB   
4080 C  CG   . ASN   C 99  ? 0.1902 0.2144 0.3459 0.0201  -0.0057 -0.0363 103 ASN   C CG   
4081 O  OD1  . ASN   C 99  ? 0.2111 0.2362 0.3942 -0.0012 -0.0116 -0.0564 103 ASN   C OD1  
4082 N  ND2  . ASN   C 99  ? 0.1734 0.2151 0.3117 0.0245  -0.0081 -0.0421 103 ASN   C ND2  
4083 N  N    . LEU   C 100 ? 0.1505 0.1716 0.2776 0.0103  -0.0023 -0.0252 104 LEU   C N    
4084 C  CA   . LEU   C 100 ? 0.1504 0.1635 0.2556 0.0087  -0.0033 -0.0192 104 LEU   C CA   
4085 C  C    . LEU   C 100 ? 0.1534 0.1692 0.2608 0.0025  -0.0094 -0.0048 104 LEU   C C    
4086 O  O    . LEU   C 100 ? 0.1553 0.1658 0.2347 0.0017  -0.0029 -0.0037 104 LEU   C O    
4087 C  CB   . LEU   C 100 ? 0.1615 0.1589 0.2400 0.0033  0.0059  -0.0179 104 LEU   C CB   
4088 C  CG   . LEU   C 100 ? 0.1740 0.1697 0.2521 0.0013  0.0200  -0.0239 104 LEU   C CG   
4089 C  CD1  . LEU   C 100 ? 0.2009 0.1777 0.2485 -0.0029 0.0107  -0.0271 104 LEU   C CD1  
4090 C  CD2  . LEU   C 100 ? 0.1861 0.1714 0.2719 0.0019  0.0265  -0.0283 104 LEU   C CD2  
4091 N  N    . ALA   C 101 ? 0.1685 0.2003 0.2676 0.0026  -0.0105 0.0130  105 ALA   C N    
4092 C  CA   . ALA   C 101 ? 0.1796 0.2052 0.2866 -0.0005 -0.0143 0.0317  105 ALA   C CA   
4093 C  C    . ALA   C 101 ? 0.1798 0.2079 0.3027 0.0032  -0.0198 0.0343  105 ALA   C C    
4094 O  O    . ALA   C 101 ? 0.1906 0.2300 0.3096 0.0075  -0.0133 0.0492  105 ALA   C O    
4095 C  CB   . ALA   C 101 ? 0.1878 0.2132 0.2844 -0.0028 -0.0213 0.0401  105 ALA   C CB   
4096 N  N    . ASN   C 102 ? 0.1824 0.1995 0.3343 -0.0003 -0.0134 0.0272  106 ASN   C N    
4097 C  CA   . ASN   C 102 ? 0.1851 0.2082 0.3488 -0.0052 -0.0096 0.0242  106 ASN   C CA   
4098 C  C    . ASN   C 102 ? 0.1705 0.1836 0.3139 -0.0035 0.0009  0.0106  106 ASN   C C    
4099 O  O    . ASN   C 102 ? 0.1712 0.1909 0.3496 -0.0095 0.0142  0.0171  106 ASN   C O    
4100 C  CB   . ASN   C 102 ? 0.2390 0.2220 0.3898 0.0154  -0.0052 0.0200  106 ASN   C CB   
4101 C  CG   . ASN   C 102 ? 0.2796 0.2735 0.4209 0.0406  -0.0148 0.0346  106 ASN   C CG   
4102 O  OD1  . ASN   C 102 ? 0.3732 0.3177 0.4596 0.0640  -0.0278 0.0625  106 ASN   C OD1  
4103 N  ND2  . ASN   C 102 ? 0.3195 0.2734 0.4609 0.0542  0.0069  0.0224  106 ASN   C ND2  
4104 N  N    A LEU   C 103 ? 0.1433 0.1892 0.2733 -0.0083 -0.0014 0.0015  107 LEU   C N    
4105 N  N    B LEU   C 103 ? 0.1618 0.1835 0.2795 -0.0092 0.0005  0.0033  107 LEU   C N    
4106 C  CA   A LEU   C 103 ? 0.1431 0.1810 0.2370 -0.0126 -0.0090 -0.0050 107 LEU   C CA   
4107 C  CA   B LEU   C 103 ? 0.1682 0.1695 0.2437 -0.0120 -0.0070 -0.0005 107 LEU   C CA   
4108 C  C    A LEU   C 103 ? 0.1427 0.1801 0.2253 -0.0134 -0.0155 -0.0009 107 LEU   C C    
4109 C  C    B LEU   C 103 ? 0.1566 0.1743 0.2284 -0.0146 -0.0162 0.0013  107 LEU   C C    
4110 O  O    A LEU   C 103 ? 0.1449 0.1725 0.2151 -0.0153 -0.0066 0.0028  107 LEU   C O    
4111 O  O    B LEU   C 103 ? 0.1598 0.1691 0.2158 -0.0178 -0.0077 0.0074  107 LEU   C O    
4112 C  CB   A LEU   C 103 ? 0.1396 0.1853 0.2184 -0.0106 -0.0050 -0.0120 107 LEU   C CB   
4113 C  CB   B LEU   C 103 ? 0.1831 0.1658 0.2317 -0.0095 -0.0003 -0.0053 107 LEU   C CB   
4114 C  CG   A LEU   C 103 ? 0.1360 0.1824 0.2056 -0.0129 -0.0026 -0.0147 107 LEU   C CG   
4115 C  CG   B LEU   C 103 ? 0.1974 0.1524 0.2194 -0.0100 0.0002  -0.0062 107 LEU   C CG   
4116 C  CD1  A LEU   C 103 ? 0.1341 0.1790 0.1999 -0.0086 -0.0042 -0.0169 107 LEU   C CD1  
4117 C  CD1  B LEU   C 103 ? 0.1992 0.1591 0.2114 -0.0105 0.0030  -0.0115 107 LEU   C CD1  
4118 C  CD2  A LEU   C 103 ? 0.1372 0.1930 0.1996 -0.0154 -0.0043 -0.0162 107 LEU   C CD2  
4119 C  CD2  B LEU   C 103 ? 0.2032 0.1456 0.2133 -0.0081 -0.0018 -0.0003 107 LEU   C CD2  
4120 N  N    . LEU   C 104 ? 0.1483 0.1784 0.2275 -0.0149 -0.0209 0.0009  108 LEU   C N    
4121 C  CA   . LEU   C 104 ? 0.1598 0.1817 0.2260 -0.0137 -0.0292 -0.0002 108 LEU   C CA   
4122 C  C    . LEU   C 104 ? 0.1685 0.1891 0.2211 -0.0174 -0.0279 0.0006  108 LEU   C C    
4123 O  O    . LEU   C 104 ? 0.1783 0.1883 0.2016 -0.0103 -0.0158 0.0028  108 LEU   C O    
4124 C  CB   . LEU   C 104 ? 0.1674 0.1967 0.2487 -0.0098 -0.0433 -0.0102 108 LEU   C CB   
4125 C  CG   . LEU   C 104 ? 0.1902 0.2092 0.2644 -0.0060 -0.0421 -0.0107 108 LEU   C CG   
4126 C  CD1  . LEU   C 104 ? 0.1985 0.2163 0.3018 -0.0126 -0.0489 -0.0128 108 LEU   C CD1  
4127 C  CD2  . LEU   C 104 ? 0.2031 0.2079 0.2913 -0.0011 -0.0441 -0.0117 108 LEU   C CD2  
4128 N  N    . LEU   C 105 ? 0.1731 0.1961 0.2349 -0.0149 -0.0311 0.0048  109 LEU   C N    
4129 C  CA   . LEU   C 105 ? 0.2031 0.2174 0.2473 -0.0129 -0.0339 0.0221  109 LEU   C CA   
4130 C  C    . LEU   C 105 ? 0.1790 0.1962 0.2215 -0.0002 -0.0337 0.0284  109 LEU   C C    
4131 O  O    . LEU   C 105 ? 0.1903 0.2062 0.2133 -0.0121 -0.0332 0.0366  109 LEU   C O    
4132 C  CB   . LEU   C 105 ? 0.2321 0.2557 0.2893 -0.0006 -0.0460 0.0389  109 LEU   C CB   
4133 C  CG   . LEU   C 105 ? 0.2887 0.3226 0.3354 -0.0063 -0.0628 0.0334  109 LEU   C CG   
4134 C  CD1  . LEU   C 105 ? 0.3243 0.3297 0.3656 0.0082  -0.0592 0.0448  109 LEU   C CD1  
4135 C  CD2  . LEU   C 105 ? 0.3330 0.3789 0.3514 -0.0030 -0.0552 0.0281  109 LEU   C CD2  
4136 N  N    . ALA   C 106 ? 0.1597 0.1816 0.2126 -0.0047 -0.0266 0.0252  110 ALA   C N    
4137 C  CA   . ALA   C 106 ? 0.1602 0.1721 0.2016 -0.0054 -0.0228 0.0209  110 ALA   C CA   
4138 C  C    . ALA   C 106 ? 0.1530 0.1645 0.1823 -0.0100 -0.0229 0.0211  110 ALA   C C    
4139 O  O    . ALA   C 106 ? 0.1573 0.1680 0.1807 -0.0091 -0.0172 0.0259  110 ALA   C O    
4140 C  CB   . ALA   C 106 ? 0.1509 0.1711 0.2117 0.0004  -0.0181 0.0138  110 ALA   C CB   
4141 N  N    . PHE   C 107 ? 0.1451 0.1610 0.1702 -0.0131 -0.0182 0.0143  111 PHE   C N    
4142 C  CA   . PHE   C 107 ? 0.1498 0.1503 0.1551 -0.0150 -0.0176 0.0128  111 PHE   C CA   
4143 C  C    . PHE   C 107 ? 0.1632 0.1598 0.1519 -0.0188 -0.0199 0.0082  111 PHE   C C    
4144 O  O    . PHE   C 107 ? 0.1673 0.1722 0.1320 -0.0245 -0.0200 0.0099  111 PHE   C O    
4145 C  CB   . PHE   C 107 ? 0.1410 0.1490 0.1630 -0.0136 -0.0134 0.0117  111 PHE   C CB   
4146 C  CG   . PHE   C 107 ? 0.1434 0.1470 0.1663 -0.0109 -0.0040 0.0069  111 PHE   C CG   
4147 C  CD1  . PHE   C 107 ? 0.1428 0.1488 0.1695 -0.0143 -0.0068 0.0040  111 PHE   C CD1  
4148 C  CD2  . PHE   C 107 ? 0.1483 0.1520 0.1649 -0.0063 -0.0014 0.0106  111 PHE   C CD2  
4149 C  CE1  . PHE   C 107 ? 0.1480 0.1491 0.1726 -0.0142 -0.0004 0.0034  111 PHE   C CE1  
4150 C  CE2  . PHE   C 107 ? 0.1490 0.1598 0.1716 -0.0048 0.0001  0.0146  111 PHE   C CE2  
4151 C  CZ   . PHE   C 107 ? 0.1511 0.1489 0.1814 -0.0104 0.0019  0.0087  111 PHE   C CZ   
4152 N  N    . LEU   C 108 ? 0.1690 0.1702 0.1591 -0.0249 -0.0263 0.0127  112 LEU   C N    
4153 C  CA   . LEU   C 108 ? 0.1999 0.1892 0.1620 -0.0261 -0.0321 0.0050  112 LEU   C CA   
4154 C  C    . LEU   C 108 ? 0.2050 0.1936 0.1612 -0.0289 -0.0278 0.0047  112 LEU   C C    
4155 O  O    . LEU   C 108 ? 0.2321 0.2015 0.1521 -0.0274 -0.0061 -0.0062 112 LEU   C O    
4156 C  CB   . LEU   C 108 ? 0.2328 0.2123 0.1809 -0.0281 -0.0527 -0.0013 112 LEU   C CB   
4157 C  CG   . LEU   C 108 ? 0.2617 0.2213 0.2172 -0.0298 -0.0625 -0.0067 112 LEU   C CG   
4158 C  CD1  . LEU   C 108 ? 0.2765 0.2408 0.2464 -0.0307 -0.0783 -0.0141 112 LEU   C CD1  
4159 C  CD2  . LEU   C 108 ? 0.2846 0.2384 0.2235 -0.0224 -0.0631 -0.0091 112 LEU   C CD2  
4160 N  N    . ARG   C 109 ? 0.1996 0.1932 0.1630 -0.0231 -0.0261 0.0139  113 ARG   C N    
4161 C  CA   . ARG   C 109 ? 0.2241 0.2035 0.1922 -0.0304 -0.0172 0.0229  113 ARG   C CA   
4162 C  C    . ARG   C 109 ? 0.2103 0.1750 0.1812 -0.0250 -0.0014 0.0115  113 ARG   C C    
4163 O  O    . ARG   C 109 ? 0.2315 0.1926 0.2361 -0.0357 0.0081  0.0258  113 ARG   C O    
4164 C  CB   . ARG   C 109 ? 0.2390 0.2151 0.2422 -0.0300 -0.0262 0.0196  113 ARG   C CB   
4165 C  CG   . ARG   C 109 ? 0.2890 0.2714 0.2769 -0.0231 -0.0484 0.0284  113 ARG   C CG   
4166 C  CD   . ARG   C 109 ? 0.3350 0.3118 0.3474 -0.0051 -0.0292 0.0158  113 ARG   C CD   
4167 N  NE   . ARG   C 109 ? 0.3752 0.3575 0.3636 0.0072  -0.0372 0.0173  113 ARG   C NE   
4168 C  CZ   . ARG   C 109 ? 0.3714 0.3711 0.4029 -0.0138 -0.0417 0.0133  113 ARG   C CZ   
4169 N  NH1  . ARG   C 109 ? 0.3803 0.3291 0.3829 0.0108  -0.0406 0.0134  113 ARG   C NH1  
4170 N  NH2  . ARG   C 109 ? 0.3847 0.4395 0.4183 -0.0208 -0.0596 0.0114  113 ARG   C NH2  
4171 N  N    . ARG   C 110 ? 0.1956 0.1728 0.1547 -0.0234 0.0027  0.0015  114 ARG   C N    
4172 C  CA   . ARG   C 110 ? 0.1884 0.1769 0.1675 -0.0200 0.0036  0.0006  114 ARG   C CA   
4173 C  C    . ARG   C 110 ? 0.1974 0.1901 0.1504 -0.0186 0.0054  0.0014  114 ARG   C C    
4174 O  O    . ARG   C 110 ? 0.1994 0.2028 0.1597 -0.0198 0.0150  -0.0148 114 ARG   C O    
4175 C  CB   . ARG   C 110 ? 0.1876 0.2006 0.1642 -0.0219 -0.0052 -0.0066 114 ARG   C CB   
4176 C  CG   . ARG   C 110 ? 0.1878 0.2202 0.1767 -0.0085 0.0035  -0.0045 114 ARG   C CG   
4177 C  CD   . ARG   C 110 ? 0.1922 0.2137 0.1711 -0.0063 -0.0050 -0.0122 114 ARG   C CD   
4178 N  NE   . ARG   C 110 ? 0.1858 0.2073 0.1510 -0.0089 -0.0077 -0.0095 114 ARG   C NE   
4179 C  CZ   . ARG   C 110 ? 0.1780 0.2083 0.1507 -0.0039 -0.0106 -0.0067 114 ARG   C CZ   
4180 N  NH1  . ARG   C 110 ? 0.1845 0.2090 0.1528 -0.0026 -0.0209 -0.0086 114 ARG   C NH1  
4181 N  NH2  . ARG   C 110 ? 0.1750 0.2099 0.1495 0.0054  -0.0089 -0.0076 114 ARG   C NH2  
4182 N  N    . GLN   C 111 ? 0.1877 0.1856 0.1534 -0.0189 0.0055  0.0012  115 GLN   C N    
4183 C  CA   . GLN   C 111 ? 0.1957 0.1904 0.1480 -0.0141 0.0099  0.0115  115 GLN   C CA   
4184 C  C    . GLN   C 111 ? 0.2051 0.1870 0.1400 -0.0116 0.0020  0.0106  115 GLN   C C    
4185 O  O    . GLN   C 111 ? 0.1953 0.2099 0.1649 -0.0041 0.0216  0.0197  115 GLN   C O    
4186 C  CB   . GLN   C 111 ? 0.2033 0.1793 0.1462 -0.0053 0.0070  0.0048  115 GLN   C CB   
4187 C  CG   . GLN   C 111 ? 0.1902 0.1688 0.1538 -0.0142 0.0046  0.0025  115 GLN   C CG   
4188 C  CD   . GLN   C 111 ? 0.1825 0.1635 0.1550 -0.0171 0.0066  -0.0028 115 GLN   C CD   
4189 O  OE1  . GLN   C 111 ? 0.1811 0.1701 0.1641 -0.0202 0.0082  0.0011  115 GLN   C OE1  
4190 N  NE2  . GLN   C 111 ? 0.1642 0.1733 0.1381 -0.0211 -0.0036 0.0022  115 GLN   C NE2  
4191 N  N    . PRO   C 112 ? 0.2133 0.2068 0.1229 -0.0161 0.0012  0.0066  116 PRO   C N    
4192 C  CA   . PRO   C 112 ? 0.2232 0.2106 0.1362 -0.0224 -0.0003 0.0157  116 PRO   C CA   
4193 C  C    . PRO   C 112 ? 0.2172 0.2001 0.1438 -0.0176 -0.0048 0.0181  116 PRO   C C    
4194 O  O    . PRO   C 112 ? 0.2143 0.1933 0.1430 -0.0089 -0.0031 0.0155  116 PRO   C O    
4195 C  CB   . PRO   C 112 ? 0.2309 0.2519 0.1491 -0.0286 0.0053  0.0117  116 PRO   C CB   
4196 C  CG   . PRO   C 112 ? 0.2376 0.2583 0.1986 -0.0192 0.0132  0.0267  116 PRO   C CG   
4197 C  CD   . PRO   C 112 ? 0.2275 0.2362 0.1352 -0.0145 -0.0020 0.0137  116 PRO   C CD   
4198 N  N    . GLN   C 113 ? 0.2416 0.1979 0.1528 -0.0167 -0.0094 0.0256  117 GLN   C N    
4199 C  CA   . GLN   C 113 ? 0.2392 0.2148 0.1617 -0.0133 -0.0081 0.0159  117 GLN   C CA   
4200 C  C    . GLN   C 113 ? 0.2367 0.2011 0.1591 -0.0214 -0.0056 0.0227  117 GLN   C C    
4201 O  O    . GLN   C 113 ? 0.2555 0.2017 0.1790 -0.0255 0.0001  0.0211  117 GLN   C O    
4202 C  CB   . GLN   C 113 ? 0.2602 0.2385 0.1911 0.0052  -0.0074 0.0178  117 GLN   C CB   
4203 C  CG   . GLN   C 113 ? 0.2805 0.2810 0.2304 0.0101  0.0064  0.0260  117 GLN   C CG   
4204 C  CD   . GLN   C 113 ? 0.3167 0.3371 0.3130 0.0347  -0.0093 0.0033  117 GLN   C CD   
4205 O  OE1  . GLN   C 113 ? 0.3437 0.4135 0.3955 0.0200  -0.0475 -0.0026 117 GLN   C OE1  
4206 N  NE2  . GLN   C 113 ? 0.3762 0.3323 0.4201 0.0476  -0.0174 -0.0102 117 GLN   C NE2  
4207 N  N    . PRO   C 114 ? 0.2362 0.2136 0.1503 -0.0342 -0.0043 0.0201  118 PRO   C N    
4208 C  CA   . PRO   C 114 ? 0.2271 0.2154 0.1531 -0.0259 -0.0115 0.0199  118 PRO   C CA   
4209 C  C    . PRO   C 114 ? 0.2191 0.1930 0.1645 -0.0205 -0.0127 0.0098  118 PRO   C C    
4210 O  O    . PRO   C 114 ? 0.2121 0.2081 0.1661 -0.0212 -0.0033 -0.0086 118 PRO   C O    
4211 C  CB   . PRO   C 114 ? 0.2427 0.2393 0.1649 -0.0282 -0.0262 0.0161  118 PRO   C CB   
4212 C  CG   . PRO   C 114 ? 0.2473 0.2479 0.1621 -0.0264 -0.0103 0.0131  118 PRO   C CG   
4213 C  CD   . PRO   C 114 ? 0.2505 0.2398 0.1536 -0.0301 -0.0029 0.0150  118 PRO   C CD   
4214 N  N    . TRP   C 115 ? 0.2167 0.1863 0.1709 -0.0224 -0.0139 0.0192  119 TRP   C N    
4215 C  CA   . TRP   C 115 ? 0.2448 0.1952 0.1773 -0.0326 -0.0092 0.0160  119 TRP   C CA   
4216 C  C    . TRP   C 115 ? 0.2194 0.1883 0.1680 -0.0381 -0.0130 0.0172  119 TRP   C C    
4217 O  O    . TRP   C 115 ? 0.2192 0.1917 0.1634 -0.0276 -0.0209 0.0123  119 TRP   C O    
4218 C  CB   . TRP   C 115 ? 0.2586 0.2322 0.2024 -0.0167 -0.0006 0.0203  119 TRP   C CB   
4219 C  CG   . TRP   C 115 ? 0.2535 0.2659 0.1546 -0.0020 0.0025  0.0172  119 TRP   C CG   
4220 C  CD1  . TRP   C 115 ? 0.2671 0.2662 0.1666 0.0024  0.0067  0.0065  119 TRP   C CD1  
4221 C  CD2  . TRP   C 115 ? 0.2561 0.2833 0.1694 0.0138  -0.0059 0.0034  119 TRP   C CD2  
4222 N  NE1  . TRP   C 115 ? 0.2591 0.2760 0.2027 0.0165  0.0108  -0.0013 119 TRP   C NE1  
4223 C  CE2  . TRP   C 115 ? 0.2679 0.2946 0.1954 0.0170  -0.0017 0.0024  119 TRP   C CE2  
4224 C  CE3  . TRP   C 115 ? 0.2762 0.3427 0.2276 0.0190  -0.0001 -0.0281 119 TRP   C CE3  
4225 C  CZ2  . TRP   C 115 ? 0.2882 0.3041 0.2044 0.0224  -0.0005 -0.0063 119 TRP   C CZ2  
4226 C  CZ3  . TRP   C 115 ? 0.2742 0.3394 0.2572 0.0253  -0.0025 -0.0292 119 TRP   C CZ3  
4227 C  CH2  . TRP   C 115 ? 0.2841 0.3181 0.2413 0.0231  0.0024  -0.0119 119 TRP   C CH2  
4228 N  N    . CYS   C 116 ? 0.1943 0.1748 0.1474 -0.0452 -0.0032 0.0018  120 CYS   C N    
4229 C  CA   . CYS   C 116 ? 0.2086 0.1806 0.1462 -0.0459 0.0000  0.0030  120 CYS   C CA   
4230 C  C    . CYS   C 116 ? 0.1972 0.1755 0.1385 -0.0423 0.0013  -0.0029 120 CYS   C C    
4231 O  O    . CYS   C 116 ? 0.2053 0.1806 0.1256 -0.0455 0.0049  -0.0044 120 CYS   C O    
4232 C  CB   . CYS   C 116 ? 0.2200 0.1883 0.1566 -0.0424 0.0049  0.0000  120 CYS   C CB   
4233 S  SG   . CYS   C 116 ? 0.2587 0.2233 0.1538 -0.0478 0.0151  -0.0182 120 CYS   C SG   
4234 N  N    . LEU   C 117 ? 0.1869 0.1736 0.1379 -0.0387 -0.0030 -0.0042 121 LEU   C N    
4235 C  CA   . LEU   C 117 ? 0.1895 0.1765 0.1397 -0.0439 0.0015  -0.0125 121 LEU   C CA   
4236 C  C    . LEU   C 117 ? 0.1949 0.1677 0.1356 -0.0449 0.0080  -0.0160 121 LEU   C C    
4237 O  O    . LEU   C 117 ? 0.2418 0.1784 0.1443 -0.0298 -0.0006 -0.0206 121 LEU   C O    
4238 C  CB   . LEU   C 117 ? 0.1937 0.2117 0.1715 -0.0391 0.0001  -0.0109 121 LEU   C CB   
4239 C  CG   . LEU   C 117 ? 0.2028 0.2441 0.2053 -0.0269 0.0063  -0.0198 121 LEU   C CG   
4240 C  CD1  . LEU   C 117 ? 0.2043 0.2602 0.2240 -0.0245 -0.0029 -0.0226 121 LEU   C CD1  
4241 C  CD2  . LEU   C 117 ? 0.2210 0.2705 0.2210 -0.0197 -0.0019 -0.0312 121 LEU   C CD2  
4242 N  N    . VAL   C 118 ? 0.1914 0.1641 0.1155 -0.0540 0.0150  -0.0158 122 VAL   C N    
4243 C  CA   . VAL   C 118 ? 0.2063 0.1659 0.1280 -0.0459 0.0203  -0.0105 122 VAL   C CA   
4244 C  C    . VAL   C 118 ? 0.1950 0.1626 0.1220 -0.0504 0.0162  -0.0159 122 VAL   C C    
4245 O  O    . VAL   C 118 ? 0.1983 0.1573 0.1119 -0.0550 0.0187  -0.0072 122 VAL   C O    
4246 C  CB   . VAL   C 118 ? 0.2081 0.1736 0.1451 -0.0433 0.0251  -0.0049 122 VAL   C CB   
4247 C  CG1  . VAL   C 118 ? 0.2137 0.1775 0.1564 -0.0346 0.0288  -0.0019 122 VAL   C CG1  
4248 C  CG2  . VAL   C 118 ? 0.2123 0.1900 0.1568 -0.0434 0.0363  -0.0004 122 VAL   C CG2  
4249 N  N    . ALA   C 119 ? 0.2073 0.1641 0.1277 -0.0536 0.0170  -0.0235 123 ALA   C N    
4250 C  CA   . ALA   C 119 ? 0.2070 0.1664 0.1231 -0.0526 0.0249  -0.0291 123 ALA   C CA   
4251 C  C    . ALA   C 119 ? 0.2092 0.1716 0.1341 -0.0555 0.0304  -0.0361 123 ALA   C C    
4252 O  O    . ALA   C 119 ? 0.2130 0.1848 0.1337 -0.0527 0.0279  -0.0295 123 ALA   C O    
4253 C  CB   . ALA   C 119 ? 0.2035 0.1637 0.1252 -0.0579 0.0272  -0.0340 123 ALA   C CB   
4254 N  N    . HIS   C 120 ? 0.2246 0.1725 0.1405 -0.0424 0.0353  -0.0410 124 HIS   C N    
4255 C  CA   . HIS   C 120 ? 0.2368 0.1815 0.1568 -0.0457 0.0355  -0.0516 124 HIS   C CA   
4256 C  C    . HIS   C 120 ? 0.2433 0.1746 0.1562 -0.0547 0.0344  -0.0475 124 HIS   C C    
4257 O  O    . HIS   C 120 ? 0.2410 0.1850 0.1543 -0.0569 0.0397  -0.0457 124 HIS   C O    
4258 C  CB   . HIS   C 120 ? 0.2476 0.1824 0.1809 -0.0426 0.0362  -0.0502 124 HIS   C CB   
4259 C  CG   . HIS   C 120 ? 0.2813 0.2056 0.2250 -0.0351 0.0460  -0.0635 124 HIS   C CG   
4260 N  ND1  . HIS   C 120 ? 0.2974 0.2331 0.2537 -0.0371 0.0548  -0.0606 124 HIS   C ND1  
4261 C  CD2  . HIS   C 120 ? 0.3014 0.2180 0.2520 -0.0495 0.0508  -0.0600 124 HIS   C CD2  
4262 C  CE1  . HIS   C 120 ? 0.3052 0.2298 0.2717 -0.0386 0.0585  -0.0617 124 HIS   C CE1  
4263 N  NE2  . HIS   C 120 ? 0.3000 0.2338 0.2767 -0.0436 0.0606  -0.0653 124 HIS   C NE2  
4264 N  N    . ASN   C 121 ? 0.2445 0.1822 0.1547 -0.0538 0.0311  -0.0544 125 ASN   C N    
4265 C  CA   . ASN   C 121 ? 0.2489 0.2067 0.1624 -0.0610 0.0262  -0.0460 125 ASN   C CA   
4266 C  C    . ASN   C 121 ? 0.2355 0.2029 0.1507 -0.0684 0.0239  -0.0416 125 ASN   C C    
4267 O  O    . ASN   C 121 ? 0.2280 0.2072 0.1774 -0.0699 0.0169  -0.0412 125 ASN   C O    
4268 C  CB   . ASN   C 121 ? 0.2691 0.2085 0.1903 -0.0602 0.0289  -0.0519 125 ASN   C CB   
4269 C  CG   . ASN   C 121 ? 0.2840 0.2348 0.2122 -0.0626 0.0282  -0.0687 125 ASN   C CG   
4270 O  OD1  . ASN   C 121 ? 0.3185 0.2535 0.2432 -0.0836 0.0053  -0.0788 125 ASN   C OD1  
4271 N  ND2  . ASN   C 121 ? 0.3083 0.2423 0.2483 -0.0631 0.0352  -0.0812 125 ASN   C ND2  
4272 N  N    . GLY   C 122 ? 0.2204 0.2070 0.1420 -0.0715 0.0169  -0.0297 126 GLY   C N    
4273 C  CA   . GLY   C 122 ? 0.2252 0.2012 0.1369 -0.0739 0.0129  -0.0238 126 GLY   C CA   
4274 C  C    . GLY   C 122 ? 0.2220 0.2029 0.1281 -0.0760 0.0117  -0.0240 126 GLY   C C    
4275 O  O    . GLY   C 122 ? 0.2126 0.2100 0.1240 -0.0670 0.0026  -0.0237 126 GLY   C O    
4276 N  N    . ASP   C 123 ? 0.2432 0.2327 0.1361 -0.0751 0.0156  -0.0271 127 ASP   C N    
4277 C  CA   . ASP   C 123 ? 0.2570 0.2491 0.1281 -0.0805 0.0148  -0.0231 127 ASP   C CA   
4278 C  C    . ASP   C 123 ? 0.2438 0.2578 0.1458 -0.0799 0.0080  -0.0360 127 ASP   C C    
4279 O  O    . ASP   C 123 ? 0.2401 0.2785 0.1894 -0.0762 0.0043  -0.0138 127 ASP   C O    
4280 C  CB   . ASP   C 123 ? 0.2850 0.2724 0.1204 -0.0841 0.0112  -0.0223 127 ASP   C CB   
4281 C  CG   . ASP   C 123 ? 0.3171 0.2657 0.1329 -0.0800 0.0110  0.0007  127 ASP   C CG   
4282 O  OD1  . ASP   C 123 ? 0.3808 0.3524 0.0937 -0.0916 0.0192  -0.0141 127 ASP   C OD1  
4283 O  OD2  . ASP   C 123 ? 0.3471 0.3752 0.1476 -0.0835 0.0167  -0.0060 127 ASP   C OD2  
4284 N  N    . ARG   C 124 ? 0.2322 0.2532 0.1428 -0.0903 0.0091  -0.0399 128 ARG   C N    
4285 C  CA   . ARG   C 124 ? 0.2429 0.2431 0.1588 -0.0859 0.0166  -0.0343 128 ARG   C CA   
4286 C  C    . ARG   C 124 ? 0.2323 0.2192 0.1582 -0.0758 0.0147  -0.0318 128 ARG   C C    
4287 O  O    . ARG   C 124 ? 0.2333 0.2277 0.1758 -0.0605 0.0039  -0.0209 128 ARG   C O    
4288 C  CB   . ARG   C 124 ? 0.2703 0.2477 0.1962 -0.0831 0.0177  -0.0495 128 ARG   C CB   
4289 C  CG   . ARG   C 124 ? 0.2899 0.2525 0.2421 -0.0860 0.0236  -0.0457 128 ARG   C CG   
4290 C  CD   . ARG   C 124 ? 0.2958 0.2568 0.2799 -0.0861 0.0224  -0.0630 128 ARG   C CD   
4291 N  NE   . ARG   C 124 ? 0.2901 0.2759 0.3270 -0.0811 0.0323  -0.0721 128 ARG   C NE   
4292 C  CZ   . ARG   C 124 ? 0.2792 0.2794 0.3545 -0.0845 0.0250  -0.1056 128 ARG   C CZ   
4293 N  NH1  . ARG   C 124 ? 0.2859 0.3096 0.3704 -0.0667 0.0403  -0.1243 128 ARG   C NH1  
4294 N  NH2  . ARG   C 124 ? 0.2800 0.2656 0.3983 -0.0889 0.0276  -0.1037 128 ARG   C NH2  
4295 N  N    . TYR   C 125 ? 0.2120 0.1989 0.1556 -0.0712 0.0182  -0.0222 129 TYR   C N    
4296 C  CA   . TYR   C 125 ? 0.2128 0.1833 0.1517 -0.0595 0.0222  -0.0225 129 TYR   C CA   
4297 C  C    . TYR   C 125 ? 0.1980 0.1822 0.1308 -0.0517 0.0137  -0.0242 129 TYR   C C    
4298 O  O    . TYR   C 125 ? 0.2028 0.1813 0.1392 -0.0469 0.0013  -0.0227 129 TYR   C O    
4299 C  CB   . TYR   C 125 ? 0.2167 0.1825 0.1597 -0.0571 0.0280  -0.0307 129 TYR   C CB   
4300 C  CG   . TYR   C 125 ? 0.2322 0.1769 0.1757 -0.0633 0.0337  -0.0296 129 TYR   C CG   
4301 C  CD1  . TYR   C 125 ? 0.2427 0.1794 0.1883 -0.0642 0.0433  -0.0356 129 TYR   C CD1  
4302 C  CD2  . TYR   C 125 ? 0.2519 0.1826 0.1972 -0.0613 0.0357  -0.0365 129 TYR   C CD2  
4303 C  CE1  . TYR   C 125 ? 0.2545 0.1802 0.2092 -0.0680 0.0426  -0.0399 129 TYR   C CE1  
4304 C  CE2  . TYR   C 125 ? 0.2634 0.1843 0.2133 -0.0617 0.0401  -0.0447 129 TYR   C CE2  
4305 C  CZ   . TYR   C 125 ? 0.2635 0.1839 0.2259 -0.0675 0.0427  -0.0405 129 TYR   C CZ   
4306 O  OH   . TYR   C 125 ? 0.3136 0.1929 0.2601 -0.0629 0.0346  -0.0539 129 TYR   C OH   
4307 N  N    . ASP   C 126 ? 0.1877 0.1762 0.1183 -0.0450 0.0099  -0.0226 130 ASP   C N    
4308 C  CA   . ASP   C 126 ? 0.1908 0.1767 0.1293 -0.0402 0.0029  -0.0231 130 ASP   C CA   
4309 C  C    . ASP   C 126 ? 0.1842 0.1796 0.1294 -0.0414 -0.0026 -0.0151 130 ASP   C C    
4310 O  O    . ASP   C 126 ? 0.1893 0.1859 0.1256 -0.0318 -0.0001 -0.0080 130 ASP   C O    
4311 C  CB   . ASP   C 126 ? 0.1849 0.1720 0.1345 -0.0369 0.0057  -0.0289 130 ASP   C CB   
4312 C  CG   . ASP   C 126 ? 0.1999 0.1772 0.1413 -0.0353 0.0061  -0.0225 130 ASP   C CG   
4313 O  OD1  . ASP   C 126 ? 0.2091 0.1846 0.1533 -0.0407 0.0054  -0.0300 130 ASP   C OD1  
4314 O  OD2  . ASP   C 126 ? 0.2167 0.1867 0.1408 -0.0266 0.0020  -0.0277 130 ASP   C OD2  
4315 N  N    . PHE   C 127 ? 0.1926 0.1866 0.1321 -0.0499 -0.0022 -0.0107 131 PHE   C N    
4316 C  CA   . PHE   C 127 ? 0.1918 0.1932 0.1229 -0.0491 -0.0008 -0.0026 131 PHE   C CA   
4317 C  C    . PHE   C 127 ? 0.1944 0.2050 0.1234 -0.0492 -0.0027 0.0013  131 PHE   C C    
4318 O  O    . PHE   C 127 ? 0.1913 0.2177 0.1204 -0.0425 -0.0039 0.0019  131 PHE   C O    
4319 C  CB   . PHE   C 127 ? 0.2056 0.1941 0.1226 -0.0512 0.0028  -0.0048 131 PHE   C CB   
4320 C  CG   . PHE   C 127 ? 0.2056 0.1962 0.1215 -0.0509 0.0020  -0.0027 131 PHE   C CG   
4321 C  CD1  . PHE   C 127 ? 0.2125 0.2043 0.1347 -0.0537 -0.0014 -0.0066 131 PHE   C CD1  
4322 C  CD2  . PHE   C 127 ? 0.2021 0.2002 0.1236 -0.0582 0.0049  -0.0083 131 PHE   C CD2  
4323 C  CE1  . PHE   C 127 ? 0.2063 0.1989 0.1254 -0.0584 0.0018  -0.0088 131 PHE   C CE1  
4324 C  CE2  . PHE   C 127 ? 0.2000 0.2133 0.1288 -0.0553 0.0059  -0.0080 131 PHE   C CE2  
4325 C  CZ   . PHE   C 127 ? 0.2050 0.2098 0.1364 -0.0591 0.0028  -0.0135 131 PHE   C CZ   
4326 N  N    . PRO   C 128 ? 0.1879 0.2214 0.1264 -0.0491 -0.0108 -0.0042 132 PRO   C N    
4327 C  CA   . PRO   C 128 ? 0.1943 0.2269 0.1435 -0.0498 -0.0093 -0.0064 132 PRO   C CA   
4328 C  C    . PRO   C 128 ? 0.1791 0.2164 0.1275 -0.0451 -0.0218 -0.0114 132 PRO   C C    
4329 O  O    . PRO   C 128 ? 0.1784 0.2283 0.1350 -0.0354 -0.0237 -0.0009 132 PRO   C O    
4330 C  CB   . PRO   C 128 ? 0.1984 0.2331 0.1423 -0.0530 -0.0162 -0.0130 132 PRO   C CB   
4331 C  CG   . PRO   C 128 ? 0.2134 0.2393 0.1627 -0.0557 -0.0179 -0.0126 132 PRO   C CG   
4332 C  CD   . PRO   C 128 ? 0.2011 0.2351 0.1505 -0.0505 -0.0114 -0.0090 132 PRO   C CD   
4333 N  N    . LEU   C 129 ? 0.1793 0.2115 0.1314 -0.0484 -0.0146 -0.0060 133 LEU   C N    
4334 C  CA   . LEU   C 129 ? 0.1789 0.2038 0.1250 -0.0440 -0.0174 -0.0052 133 LEU   C CA   
4335 C  C    . LEU   C 129 ? 0.1772 0.2016 0.1241 -0.0394 -0.0179 -0.0052 133 LEU   C C    
4336 O  O    . LEU   C 129 ? 0.1836 0.2021 0.1297 -0.0441 -0.0104 -0.0068 133 LEU   C O    
4337 C  CB   . LEU   C 129 ? 0.1919 0.1974 0.1262 -0.0458 -0.0144 -0.0058 133 LEU   C CB   
4338 C  CG   . LEU   C 129 ? 0.2125 0.1952 0.1156 -0.0373 -0.0165 0.0019  133 LEU   C CG   
4339 C  CD1  . LEU   C 129 ? 0.2231 0.2016 0.1280 -0.0391 -0.0107 0.0066  133 LEU   C CD1  
4340 C  CD2  . LEU   C 129 ? 0.2300 0.1944 0.1237 -0.0363 -0.0110 0.0060  133 LEU   C CD2  
4341 N  N    . LEU   C 130 ? 0.1764 0.1913 0.1242 -0.0353 -0.0139 0.0002  134 LEU   C N    
4342 C  CA   . LEU   C 130 ? 0.1786 0.1914 0.1364 -0.0321 -0.0155 0.0061  134 LEU   C CA   
4343 C  C    . LEU   C 130 ? 0.1897 0.2063 0.1426 -0.0261 -0.0144 0.0073  134 LEU   C C    
4344 O  O    . LEU   C 130 ? 0.1948 0.2037 0.1470 -0.0231 -0.0146 0.0057  134 LEU   C O    
4345 C  CB   . LEU   C 130 ? 0.1738 0.1875 0.1403 -0.0366 -0.0208 0.0068  134 LEU   C CB   
4346 C  CG   . LEU   C 130 ? 0.1916 0.1854 0.1617 -0.0342 -0.0155 0.0077  134 LEU   C CG   
4347 C  CD1  . LEU   C 130 ? 0.1943 0.1855 0.1679 -0.0333 -0.0183 -0.0030 134 LEU   C CD1  
4348 C  CD2  . LEU   C 130 ? 0.1940 0.1874 0.1783 -0.0386 -0.0171 0.0109  134 LEU   C CD2  
4349 N  N    A GLN   C 131 ? 0.1933 0.2156 0.1421 -0.0201 -0.0130 0.0059  135 GLN   C N    
4350 N  N    B GLN   C 131 ? 0.2075 0.2178 0.1467 -0.0214 -0.0092 0.0024  135 GLN   C N    
4351 C  CA   A GLN   C 131 ? 0.2056 0.2372 0.1423 -0.0147 -0.0152 0.0142  135 GLN   C CA   
4352 C  CA   B GLN   C 131 ? 0.2290 0.2408 0.1604 -0.0134 -0.0096 0.0124  135 GLN   C CA   
4353 C  C    A GLN   C 131 ? 0.2042 0.2508 0.1436 -0.0056 -0.0172 0.0121  135 GLN   C C    
4354 C  C    B GLN   C 131 ? 0.2205 0.2526 0.1525 -0.0054 -0.0153 0.0121  135 GLN   C C    
4355 O  O    A GLN   C 131 ? 0.2087 0.2588 0.1636 0.0039  -0.0110 0.0107  135 GLN   C O    
4356 O  O    B GLN   C 131 ? 0.2229 0.2628 0.1725 0.0048  -0.0100 0.0160  135 GLN   C O    
4357 C  CB   A GLN   C 131 ? 0.2131 0.2462 0.1429 -0.0171 -0.0137 0.0170  135 GLN   C CB   
4358 C  CB   B GLN   C 131 ? 0.2645 0.2568 0.1714 -0.0145 -0.0029 0.0076  135 GLN   C CB   
4359 C  CG   A GLN   C 131 ? 0.2136 0.2518 0.1473 -0.0163 -0.0141 0.0242  135 GLN   C CG   
4360 C  CG   B GLN   C 131 ? 0.2899 0.2682 0.1991 -0.0180 0.0080  0.0157  135 GLN   C CG   
4361 C  CD   A GLN   C 131 ? 0.2326 0.2609 0.1654 -0.0236 -0.0173 0.0301  135 GLN   C CD   
4362 C  CD   B GLN   C 131 ? 0.3293 0.2798 0.2314 -0.0125 0.0168  0.0182  135 GLN   C CD   
4363 O  OE1  A GLN   C 131 ? 0.2744 0.2522 0.2019 -0.0403 0.0020  0.0277  135 GLN   C OE1  
4364 O  OE1  B GLN   C 131 ? 0.3740 0.3009 0.2627 -0.0040 0.0376  0.0211  135 GLN   C OE1  
4365 N  NE2  A GLN   C 131 ? 0.2312 0.2754 0.1626 -0.0303 -0.0243 0.0368  135 GLN   C NE2  
4366 N  NE2  B GLN   C 131 ? 0.3386 0.3016 0.2369 -0.0130 0.0119  0.0282  135 GLN   C NE2  
4367 N  N    . ALA   C 132 ? 0.2006 0.2636 0.1403 -0.0101 -0.0221 0.0076  136 ALA   C N    
4368 C  CA   . ALA   C 132 ? 0.2001 0.2841 0.1451 -0.0042 -0.0218 0.0000  136 ALA   C CA   
4369 C  C    . ALA   C 132 ? 0.1929 0.3016 0.1444 0.0053  -0.0164 -0.0011 136 ALA   C C    
4370 O  O    . ALA   C 132 ? 0.2322 0.3335 0.1697 0.0271  -0.0186 -0.0126 136 ALA   C O    
4371 C  CB   . ALA   C 132 ? 0.2081 0.2897 0.1457 -0.0155 -0.0288 -0.0050 136 ALA   C CB   
4372 N  N    . GLU   C 133 ? 0.1916 0.3102 0.1569 0.0179  -0.0187 -0.0082 137 GLU   C N    
4373 C  CA   . GLU   C 133 ? 0.2013 0.3054 0.1560 0.0169  -0.0187 -0.0079 137 GLU   C CA   
4374 C  C    . GLU   C 133 ? 0.2239 0.3104 0.1598 0.0274  -0.0199 -0.0072 137 GLU   C C    
4375 O  O    . GLU   C 133 ? 0.2588 0.3317 0.1785 0.0276  0.0028  -0.0213 137 GLU   C O    
4376 C  CB   . GLU   C 133 ? 0.2102 0.2996 0.1541 0.0083  -0.0271 -0.0055 137 GLU   C CB   
4377 C  CG   . GLU   C 133 ? 0.2334 0.2954 0.1686 0.0121  -0.0248 -0.0060 137 GLU   C CG   
4378 C  CD   . GLU   C 133 ? 0.2517 0.2785 0.2097 0.0086  -0.0058 -0.0010 137 GLU   C CD   
4379 O  OE1  . GLU   C 133 ? 0.2716 0.2570 0.2392 0.0096  -0.0171 -0.0005 137 GLU   C OE1  
4380 O  OE2  . GLU   C 133 ? 0.2569 0.2618 0.2373 0.0043  -0.0023 -0.0013 137 GLU   C OE2  
4381 N  N    . LEU   C 134 ? 0.2404 0.3103 0.1655 0.0303  -0.0133 -0.0134 138 LEU   C N    
4382 C  CA   . LEU   C 134 ? 0.2528 0.3098 0.2003 0.0394  -0.0142 -0.0131 138 LEU   C CA   
4383 C  C    . LEU   C 134 ? 0.2630 0.3412 0.2031 0.0535  -0.0149 -0.0037 138 LEU   C C    
4384 O  O    . LEU   C 134 ? 0.2857 0.3534 0.2177 0.0719  -0.0246 -0.0064 138 LEU   C O    
4385 C  CB   . LEU   C 134 ? 0.2641 0.2861 0.2176 0.0292  -0.0135 -0.0007 138 LEU   C CB   
4386 C  CG   . LEU   C 134 ? 0.2553 0.2776 0.2404 0.0230  -0.0168 0.0031  138 LEU   C CG   
4387 C  CD1  . LEU   C 134 ? 0.2631 0.2856 0.2559 0.0207  -0.0102 -0.0042 138 LEU   C CD1  
4388 C  CD2  . LEU   C 134 ? 0.2485 0.2823 0.2615 0.0200  -0.0269 0.0025  138 LEU   C CD2  
4389 N  N    . ALA   C 135 ? 0.2508 0.3631 0.2083 0.0654  -0.0314 0.0007  139 ALA   C N    
4390 C  CA   . ALA   C 135 ? 0.2647 0.4113 0.2341 0.0781  -0.0400 -0.0035 139 ALA   C CA   
4391 C  C    . ALA   C 135 ? 0.2606 0.4242 0.2490 0.0867  -0.0405 0.0004  139 ALA   C C    
4392 O  O    . ALA   C 135 ? 0.3013 0.4527 0.2785 0.1175  -0.0396 0.0029  139 ALA   C O    
4393 C  CB   . ALA   C 135 ? 0.2666 0.4279 0.2318 0.0689  -0.0432 -0.0094 139 ALA   C CB   
4394 N  N    A MET   C 136 ? 0.2645 0.4372 0.2483 0.0915  -0.0438 -0.0012 140 MET   C N    
4395 N  N    B MET   C 136 ? 0.2617 0.4258 0.2427 0.0867  -0.0361 0.0058  140 MET   C N    
4396 C  CA   A MET   C 136 ? 0.2688 0.4523 0.2712 0.0910  -0.0344 -0.0113 140 MET   C CA   
4397 C  CA   B MET   C 136 ? 0.2690 0.4224 0.2549 0.0822  -0.0254 0.0109  140 MET   C CA   
4398 C  C    A MET   C 136 ? 0.2776 0.4332 0.2731 0.0945  -0.0254 0.0004  140 MET   C C    
4399 C  C    B MET   C 136 ? 0.2783 0.4203 0.2610 0.0914  -0.0220 0.0113  140 MET   C C    
4400 O  O    A MET   C 136 ? 0.2850 0.4570 0.2986 0.0956  -0.0150 0.0025  140 MET   C O    
4401 O  O    B MET   C 136 ? 0.2860 0.4470 0.2816 0.0966  -0.0160 0.0135  140 MET   C O    
4402 C  CB   A MET   C 136 ? 0.2915 0.4666 0.2954 0.0874  -0.0303 -0.0220 140 MET   C CB   
4403 C  CB   B MET   C 136 ? 0.2853 0.4207 0.2644 0.0696  -0.0121 0.0128  140 MET   C CB   
4404 C  CG   A MET   C 136 ? 0.3261 0.5081 0.3357 0.0744  -0.0393 -0.0431 140 MET   C CG   
4405 C  CG   B MET   C 136 ? 0.3065 0.4215 0.2872 0.0516  -0.0103 0.0193  140 MET   C CG   
4406 S  SD   A MET   C 136 ? 0.3813 0.5332 0.4171 0.0598  -0.0448 -0.0587 140 MET   C SD   
4407 S  SD   B MET   C 136 ? 0.3578 0.4501 0.3467 0.0105  -0.0139 -0.0064 140 MET   C SD   
4408 C  CE   A MET   C 136 ? 0.3881 0.5641 0.4347 0.0553  -0.0401 -0.0467 140 MET   C CE   
4409 C  CE   B MET   C 136 ? 0.3610 0.4668 0.3739 0.0152  -0.0145 0.0019  140 MET   C CE   
4410 N  N    . LEU   C 137 ? 0.2836 0.3993 0.2540 0.0895  -0.0204 0.0095  141 LEU   C N    
4411 C  CA   . LEU   C 137 ? 0.2981 0.3716 0.2646 0.0945  -0.0273 0.0206  141 LEU   C CA   
4412 C  C    . LEU   C 137 ? 0.3891 0.3823 0.2861 0.1067  -0.0342 0.0229  141 LEU   C C    
4413 O  O    . LEU   C 137 ? 0.4395 0.3622 0.3225 0.1316  -0.0486 0.0287  141 LEU   C O    
4414 C  CB   . LEU   C 137 ? 0.2972 0.3422 0.2472 0.0799  -0.0158 0.0248  141 LEU   C CB   
4415 C  CG   . LEU   C 137 ? 0.2848 0.3131 0.2491 0.0612  -0.0182 0.0245  141 LEU   C CG   
4416 C  CD1  . LEU   C 137 ? 0.2890 0.3141 0.2516 0.0605  -0.0241 0.0251  141 LEU   C CD1  
4417 C  CD2  . LEU   C 137 ? 0.2899 0.3135 0.2455 0.0437  -0.0155 0.0287  141 LEU   C CD2  
4418 N  N    . GLY   C 138 ? 0.4220 0.3884 0.2787 0.1185  -0.0488 0.0459  142 GLY   C N    
4419 C  CA   . GLY   C 138 ? 0.4764 0.3920 0.3111 0.1116  -0.0484 0.0618  142 GLY   C CA   
4420 C  C    . GLY   C 138 ? 0.5126 0.3902 0.3297 0.1075  -0.0579 0.0793  142 GLY   C C    
4421 O  O    . GLY   C 138 ? 0.5846 0.3855 0.4021 0.0999  -0.0354 0.0765  142 GLY   C O    
4422 N  N    . LEU   C 139 ? 0.5382 0.3724 0.3312 0.1153  -0.0409 0.0906  143 LEU   C N    
4423 C  CA   . LEU   C 139 ? 0.5744 0.3987 0.3681 0.0985  -0.0366 0.1061  143 LEU   C CA   
4424 C  C    . LEU   C 139 ? 0.6281 0.4457 0.4159 0.1057  -0.0069 0.0872  143 LEU   C C    
4425 O  O    . LEU   C 139 ? 0.6558 0.4189 0.4864 0.1334  0.0282  0.1325  143 LEU   C O    
4426 C  CB   . LEU   C 139 ? 0.5643 0.3693 0.3922 0.0959  -0.0524 0.1050  143 LEU   C CB   
4427 C  CG   . LEU   C 139 ? 0.5730 0.3734 0.3688 0.0950  -0.0721 0.1085  143 LEU   C CG   
4428 C  CD1  . LEU   C 139 ? 0.5738 0.3780 0.3821 0.1057  -0.0810 0.1050  143 LEU   C CD1  
4429 C  CD2  . LEU   C 139 ? 0.5798 0.3816 0.4045 0.1136  -0.0748 0.0819  143 LEU   C CD2  
4430 N  N    . THR   C 140 ? 0.6913 0.5395 0.4339 0.0997  -0.0026 0.0714  144 THR   C N    
4431 C  CA   . THR   C 140 ? 0.7131 0.5776 0.4793 0.0868  -0.0059 0.0483  144 THR   C CA   
4432 C  C    . THR   C 140 ? 0.7305 0.5915 0.5136 0.0922  0.0249  0.0457  144 THR   C C    
4433 O  O    . THR   C 140 ? 0.7779 0.6084 0.5823 0.1044  0.0238  0.0168  144 THR   C O    
4434 C  CB   . THR   C 140 ? 0.7461 0.6304 0.4592 0.0617  -0.0069 0.0497  144 THR   C CB   
4435 N  N    . SER   C 141 ? 0.7112 0.6004 0.5767 0.0862  0.0272  0.0520  145 SER   C N    
4436 C  CA   . SER   C 141 ? 0.6680 0.5901 0.6029 0.0907  0.0103  0.0577  145 SER   C CA   
4437 C  C    . SER   C 141 ? 0.6488 0.5665 0.5842 0.0973  -0.0031 0.0704  145 SER   C C    
4438 O  O    . SER   C 141 ? 0.6259 0.5367 0.6090 0.1172  -0.0025 0.0807  145 SER   C O    
4439 C  CB   . SER   C 141 ? 0.6764 0.5948 0.6382 0.0892  0.0146  0.0550  145 SER   C CB   
4440 O  OG   . SER   C 141 ? 0.6622 0.5945 0.6905 0.0982  0.0132  0.0287  145 SER   C OG   
4441 N  N    . ALA   C 142 ? 0.5860 0.5516 0.5640 0.1032  -0.0321 0.0631  146 ALA   C N    
4442 C  CA   . ALA   C 142 ? 0.5504 0.5085 0.5555 0.0797  -0.0259 0.0419  146 ALA   C CA   
4443 C  C    . ALA   C 142 ? 0.4905 0.4525 0.5199 0.0472  -0.0703 0.0416  146 ALA   C C    
4444 O  O    . ALA   C 142 ? 0.5174 0.4050 0.5571 0.0277  -0.0924 0.0224  146 ALA   C O    
4445 C  CB   . ALA   C 142 ? 0.5563 0.5008 0.5526 0.0911  -0.0194 0.0476  146 ALA   C CB   
4446 N  N    . LEU   C 143 ? 0.4320 0.4327 0.4673 0.0235  -0.0822 0.0540  147 LEU   C N    
4447 C  CA   . LEU   C 143 ? 0.3853 0.4296 0.4307 0.0038  -0.0910 0.0626  147 LEU   C CA   
4448 C  C    . LEU   C 143 ? 0.4004 0.4468 0.4384 0.0078  -0.0845 0.0581  147 LEU   C C    
4449 O  O    . LEU   C 143 ? 0.4174 0.4367 0.4111 -0.0243 -0.0952 0.0326  147 LEU   C O    
4450 C  CB   . LEU   C 143 ? 0.3784 0.4441 0.4299 0.0099  -0.0927 0.0641  147 LEU   C CB   
4451 C  CG   . LEU   C 143 ? 0.3885 0.4390 0.4249 0.0026  -0.0716 0.0783  147 LEU   C CG   
4452 C  CD1  . LEU   C 143 ? 0.3827 0.4387 0.4338 -0.0013 -0.0593 0.0800  147 LEU   C CD1  
4453 C  CD2  . LEU   C 143 ? 0.4090 0.4546 0.4194 -0.0054 -0.0797 0.0810  147 LEU   C CD2  
4454 N  N    . ASP   C 144 ? 0.4142 0.5047 0.4470 0.0427  -0.0850 0.0659  148 ASP   C N    
4455 C  CA   . ASP   C 144 ? 0.4587 0.5360 0.4626 0.0631  -0.0830 0.0656  148 ASP   C CA   
4456 C  C    . ASP   C 144 ? 0.4656 0.5055 0.4738 0.0430  -0.0697 0.0572  148 ASP   C C    
4457 O  O    . ASP   C 144 ? 0.5215 0.5690 0.5073 0.0505  -0.0576 0.0418  148 ASP   C O    
4458 C  CB   . ASP   C 144 ? 0.5007 0.5802 0.4887 0.0892  -0.0905 0.0732  148 ASP   C CB   
4459 C  CG   . ASP   C 144 ? 0.5276 0.6326 0.5351 0.0812  -0.0895 0.0721  148 ASP   C CG   
4460 O  OD1  . ASP   C 144 ? 0.5604 0.6527 0.5573 0.0893  -0.0999 0.0548  148 ASP   C OD1  
4461 O  OD2  . ASP   C 144 ? 0.6042 0.6772 0.5442 0.1076  -0.1005 0.0954  148 ASP   C OD2  
4462 N  N    . GLY   C 145 ? 0.4147 0.4238 0.4579 0.0462  -0.0585 0.0638  149 GLY   C N    
4463 C  CA   . GLY   C 145 ? 0.3955 0.3867 0.4387 0.0421  -0.0619 0.0506  149 GLY   C CA   
4464 C  C    . GLY   C 145 ? 0.3666 0.3406 0.4011 0.0192  -0.0389 0.0288  149 GLY   C C    
4465 O  O    . GLY   C 145 ? 0.3624 0.3401 0.4133 0.0316  -0.0401 0.0067  149 GLY   C O    
4466 N  N    . ALA   C 146 ? 0.3243 0.3125 0.3486 0.0241  -0.0558 0.0239  150 ALA   C N    
4467 C  CA   . ALA   C 146 ? 0.2730 0.2782 0.2962 -0.0015 -0.0336 0.0175  150 ALA   C CA   
4468 C  C    . ALA   C 146 ? 0.2385 0.2558 0.2405 -0.0309 -0.0285 0.0361  150 ALA   C C    
4469 O  O    . ALA   C 146 ? 0.2261 0.2512 0.2642 -0.0238 -0.0302 0.0395  150 ALA   C O    
4470 C  CB   . ALA   C 146 ? 0.2898 0.3090 0.2611 -0.0031 -0.0445 -0.0011 150 ALA   C CB   
4471 N  N    . PHE   C 147 ? 0.2138 0.2363 0.1895 -0.0431 -0.0306 0.0357  151 PHE   C N    
4472 C  CA   . PHE   C 147 ? 0.2148 0.2471 0.1738 -0.0506 -0.0265 0.0357  151 PHE   C CA   
4473 C  C    . PHE   C 147 ? 0.2053 0.2346 0.1551 -0.0528 -0.0169 0.0217  151 PHE   C C    
4474 O  O    . PHE   C 147 ? 0.1892 0.2283 0.1522 -0.0353 -0.0128 0.0247  151 PHE   C O    
4475 C  CB   . PHE   C 147 ? 0.2194 0.2597 0.1830 -0.0605 -0.0231 0.0316  151 PHE   C CB   
4476 C  CG   . PHE   C 147 ? 0.2245 0.2773 0.1904 -0.0600 -0.0289 0.0530  151 PHE   C CG   
4477 C  CD1  . PHE   C 147 ? 0.2379 0.2826 0.2077 -0.0730 -0.0290 0.0674  151 PHE   C CD1  
4478 C  CD2  . PHE   C 147 ? 0.2614 0.2963 0.2006 -0.0828 -0.0334 0.0533  151 PHE   C CD2  
4479 C  CE1  . PHE   C 147 ? 0.2527 0.2906 0.2295 -0.0773 -0.0269 0.0684  151 PHE   C CE1  
4480 C  CE2  . PHE   C 147 ? 0.2736 0.3099 0.2236 -0.0705 -0.0452 0.0672  151 PHE   C CE2  
4481 C  CZ   . PHE   C 147 ? 0.2648 0.3010 0.2408 -0.0778 -0.0419 0.0714  151 PHE   C CZ   
4482 N  N    . CYS   C 148 ? 0.2222 0.2462 0.1512 -0.0532 -0.0028 0.0146  152 CYS   C N    
4483 C  CA   . CYS   C 148 ? 0.2211 0.2346 0.1551 -0.0645 -0.0067 0.0007  152 CYS   C CA   
4484 C  C    . CYS   C 148 ? 0.2203 0.2381 0.1462 -0.0755 0.0014  -0.0042 152 CYS   C C    
4485 O  O    . CYS   C 148 ? 0.2524 0.2438 0.1555 -0.0692 -0.0038 0.0079  152 CYS   C O    
4486 C  CB   . CYS   C 148 ? 0.2295 0.2587 0.1733 -0.0692 -0.0048 -0.0021 152 CYS   C CB   
4487 S  SG   . CYS   C 148 ? 0.2381 0.2980 0.1927 -0.0707 -0.0161 0.0038  152 CYS   C SG   
4488 N  N    A VAL   C 149 ? 0.2342 0.2231 0.1465 -0.0752 0.0054  -0.0121 153 VAL   C N    
4489 N  N    B VAL   C 149 ? 0.2311 0.2216 0.1421 -0.0753 0.0074  -0.0136 153 VAL   C N    
4490 C  CA   A VAL   C 149 ? 0.2432 0.2329 0.1493 -0.0745 0.0146  -0.0198 153 VAL   C CA   
4491 C  CA   B VAL   C 149 ? 0.2376 0.2314 0.1407 -0.0753 0.0179  -0.0226 153 VAL   C CA   
4492 C  C    A VAL   C 149 ? 0.2452 0.2233 0.1364 -0.0716 0.0169  -0.0278 153 VAL   C C    
4493 C  C    B VAL   C 149 ? 0.2434 0.2248 0.1311 -0.0736 0.0185  -0.0279 153 VAL   C C    
4494 O  O    A VAL   C 149 ? 0.2318 0.2143 0.1336 -0.0684 0.0292  -0.0285 153 VAL   C O    
4495 O  O    B VAL   C 149 ? 0.2319 0.2174 0.1269 -0.0745 0.0277  -0.0294 153 VAL   C O    
4496 C  CB   A VAL   C 149 ? 0.2480 0.2490 0.1762 -0.0752 0.0163  -0.0199 153 VAL   C CB   
4497 C  CB   B VAL   C 149 ? 0.2391 0.2426 0.1574 -0.0735 0.0227  -0.0263 153 VAL   C CB   
4498 C  CG1  A VAL   C 149 ? 0.2590 0.2655 0.1865 -0.0792 0.0134  -0.0138 153 VAL   C CG1  
4499 C  CG1  B VAL   C 149 ? 0.2380 0.2436 0.1770 -0.0737 0.0306  -0.0206 153 VAL   C CG1  
4500 C  CG2  A VAL   C 149 ? 0.2462 0.2505 0.1728 -0.0738 0.0205  -0.0206 153 VAL   C CG2  
4501 C  CG2  B VAL   C 149 ? 0.2491 0.2572 0.1751 -0.0769 0.0226  -0.0177 153 VAL   C CG2  
4502 N  N    . ASP   C 150 ? 0.2527 0.2252 0.1316 -0.0713 0.0211  -0.0309 154 ASP   C N    
4503 C  CA   . ASP   C 150 ? 0.2628 0.2331 0.1425 -0.0803 0.0312  -0.0311 154 ASP   C CA   
4504 C  C    . ASP   C 150 ? 0.2617 0.2211 0.1462 -0.0815 0.0419  -0.0356 154 ASP   C C    
4505 O  O    . ASP   C 150 ? 0.2954 0.2282 0.1540 -0.0764 0.0489  -0.0467 154 ASP   C O    
4506 C  CB   . ASP   C 150 ? 0.2617 0.2586 0.1585 -0.0854 0.0323  -0.0408 154 ASP   C CB   
4507 C  CG   . ASP   C 150 ? 0.2722 0.2647 0.1843 -0.0915 0.0239  -0.0448 154 ASP   C CG   
4508 O  OD1  . ASP   C 150 ? 0.2841 0.2704 0.1996 -0.0880 0.0292  -0.0461 154 ASP   C OD1  
4509 O  OD2  . ASP   C 150 ? 0.2667 0.3119 0.1942 -0.0926 0.0236  -0.0639 154 ASP   C OD2  
4510 N  N    . SER   C 151 ? 0.2641 0.2262 0.1581 -0.0859 0.0433  -0.0394 155 SER   C N    
4511 C  CA   . SER   C 151 ? 0.2704 0.2261 0.1793 -0.0822 0.0526  -0.0469 155 SER   C CA   
4512 C  C    . SER   C 151 ? 0.3003 0.2283 0.2077 -0.0832 0.0526  -0.0480 155 SER   C C    
4513 O  O    . SER   C 151 ? 0.3159 0.2231 0.2427 -0.0782 0.0669  -0.0711 155 SER   C O    
4514 C  CB   . SER   C 151 ? 0.2697 0.2335 0.1963 -0.0772 0.0458  -0.0342 155 SER   C CB   
4515 O  OG   . SER   C 151 ? 0.2577 0.2443 0.2067 -0.0735 0.0460  -0.0324 155 SER   C OG   
4516 N  N    . ILE   C 152 ? 0.3216 0.2390 0.2210 -0.0923 0.0471  -0.0663 156 ILE   C N    
4517 C  CA   . ILE   C 152 ? 0.3374 0.2320 0.2649 -0.0975 0.0519  -0.0597 156 ILE   C CA   
4518 C  C    . ILE   C 152 ? 0.3578 0.2541 0.2558 -0.0976 0.0454  -0.0861 156 ILE   C C    
4519 O  O    . ILE   C 152 ? 0.3765 0.2733 0.2986 -0.0792 0.0604  -0.0823 156 ILE   C O    
4520 C  CB   . ILE   C 152 ? 0.3288 0.2542 0.3253 -0.1030 0.0401  -0.0679 156 ILE   C CB   
4521 C  CG1  . ILE   C 152 ? 0.3406 0.2791 0.3947 -0.0879 0.0528  -0.0375 156 ILE   C CG1  
4522 C  CG2  . ILE   C 152 ? 0.3619 0.2745 0.3411 -0.0898 0.0412  -0.0614 156 ILE   C CG2  
4523 C  CD1  . ILE   C 152 ? 0.3475 0.2902 0.4067 -0.1009 0.0540  -0.0331 156 ILE   C CD1  
4524 N  N    . THR   C 153 ? 0.3878 0.2702 0.2335 -0.1095 0.0462  -0.0814 157 THR   C N    
4525 C  CA   . THR   C 153 ? 0.4182 0.2944 0.2243 -0.1060 0.0395  -0.0874 157 THR   C CA   
4526 C  C    . THR   C 153 ? 0.4371 0.3001 0.2308 -0.1136 0.0621  -0.0936 157 THR   C C    
4527 O  O    . THR   C 153 ? 0.4973 0.3191 0.2808 -0.0943 0.0873  -0.1218 157 THR   C O    
4528 C  CB   . THR   C 153 ? 0.4063 0.3171 0.2077 -0.1035 0.0261  -0.0733 157 THR   C CB   
4529 O  OG1  . THR   C 153 ? 0.4023 0.3372 0.2354 -0.0944 0.0092  -0.0541 157 THR   C OG1  
4530 C  CG2  . THR   C 153 ? 0.4084 0.3245 0.2157 -0.1063 0.0275  -0.0591 157 THR   C CG2  
4531 N  N    . ALA   C 154 ? 0.4278 0.2868 0.2310 -0.1294 0.0761  -0.0894 158 ALA   C N    
4532 C  CA   . ALA   C 154 ? 0.4248 0.3066 0.2474 -0.1200 0.1011  -0.0932 158 ALA   C CA   
4533 C  C    . ALA   C 154 ? 0.4384 0.3106 0.2913 -0.1123 0.1146  -0.1092 158 ALA   C C    
4534 O  O    . ALA   C 154 ? 0.4770 0.3010 0.3486 -0.1061 0.1537  -0.1160 158 ALA   C O    
4535 C  CB   . ALA   C 154 ? 0.4089 0.2937 0.2651 -0.1365 0.0985  -0.0872 158 ALA   C CB   
4536 N  N    . LEU   C 155 ? 0.4387 0.3101 0.3235 -0.1004 0.1257  -0.1089 159 LEU   C N    
4537 C  CA   . LEU   C 155 ? 0.4495 0.3413 0.3783 -0.0841 0.1161  -0.1149 159 LEU   C CA   
4538 C  C    . LEU   C 155 ? 0.4876 0.3550 0.4486 -0.0762 0.1106  -0.1504 159 LEU   C C    
4539 O  O    . LEU   C 155 ? 0.4917 0.3726 0.4898 -0.0752 0.1083  -0.1609 159 LEU   C O    
4540 C  CB   . LEU   C 155 ? 0.4334 0.3478 0.3935 -0.0808 0.1159  -0.0988 159 LEU   C CB   
4541 C  CG   . LEU   C 155 ? 0.4259 0.3792 0.3784 -0.0836 0.1012  -0.0837 159 LEU   C CG   
4542 C  CD1  . LEU   C 155 ? 0.4189 0.3704 0.3835 -0.0765 0.1031  -0.0736 159 LEU   C CD1  
4543 C  CD2  . LEU   C 155 ? 0.4211 0.3794 0.3948 -0.0916 0.0962  -0.0759 159 LEU   C CD2  
4544 N  N    . LYS   C 156 ? 0.5087 0.3356 0.4679 -0.0775 0.1035  -0.2050 160 LYS   C N    
4545 C  CA   . LYS   C 156 ? 0.5655 0.3513 0.5052 -0.0757 0.1189  -0.2290 160 LYS   C CA   
4546 C  C    . LYS   C 156 ? 0.6071 0.3970 0.5142 -0.0656 0.1643  -0.2561 160 LYS   C C    
4547 O  O    . LYS   C 156 ? 0.6213 0.4144 0.5558 -0.0471 0.1694  -0.2563 160 LYS   C O    
4548 C  CB   . LYS   C 156 ? 0.5825 0.3637 0.5508 -0.0766 0.1004  -0.2247 160 LYS   C CB   
4549 C  CG   . LYS   C 156 ? 0.5935 0.4211 0.6073 -0.0798 0.0867  -0.1825 160 LYS   C CG   
4550 C  CD   . LYS   C 156 ? 0.6029 0.4590 0.6560 -0.0914 0.0578  -0.1572 160 LYS   C CD   
4551 C  CE   . LYS   C 156 ? 0.5963 0.4863 0.6826 -0.1002 0.0460  -0.1448 160 LYS   C CE   
4552 N  NZ   . LYS   C 156 ? 0.6021 0.4953 0.6987 -0.1098 0.0258  -0.1493 160 LYS   C NZ   
4553 N  N    . ALA   C 157 ? 0.6280 0.4212 0.5110 -0.0823 0.2186  -0.2514 161 ALA   C N    
4554 C  CA   . ALA   C 157 ? 0.6492 0.4918 0.5201 -0.0878 0.2634  -0.2473 161 ALA   C CA   
4555 C  C    . ALA   C 157 ? 0.6341 0.5297 0.5722 -0.0924 0.3179  -0.2285 161 ALA   C C    
4556 O  O    . ALA   C 157 ? 0.7105 0.5906 0.5959 -0.0359 0.3378  -0.2541 161 ALA   C O    
4557 C  CB   . ALA   C 157 ? 0.6560 0.4988 0.4970 -0.1005 0.2634  -0.2316 161 ALA   C CB   
4558 N  N    . LEU   C 158 ? 0.6284 0.4899 0.6190 -0.0930 0.3544  -0.2466 162 LEU   C N    
4559 C  CA   . LEU   C 158 ? 0.5984 0.4906 0.6832 -0.0950 0.3878  -0.2529 162 LEU   C CA   
4560 C  C    . LEU   C 158 ? 0.6417 0.4895 0.7980 -0.0797 0.3990  -0.2509 162 LEU   C C    
4561 O  O    . LEU   C 158 ? 0.6633 0.5170 0.8314 -0.0479 0.4206  -0.2485 162 LEU   C O    
4562 C  CB   . LEU   C 158 ? 0.5966 0.5014 0.7061 -0.1402 0.3496  -0.2339 162 LEU   C CB   
4563 C  CG   . LEU   C 158 ? 0.5960 0.4978 0.6829 -0.1613 0.3420  -0.2509 162 LEU   C CG   
4564 C  CD1  . LEU   C 158 ? 0.6333 0.5048 0.6903 -0.1879 0.3052  -0.2534 162 LEU   C CD1  
4565 C  CD2  . LEU   C 158 ? 0.5971 0.5313 0.6956 -0.1777 0.3297  -0.2341 162 LEU   C CD2  
4566 N  N    . GLU   C 159 ? 0.6654 0.4644 0.8709 -0.0769 0.4071  -0.2769 163 GLU   C N    
4567 C  CA   . GLU   C 159 ? 0.6905 0.4836 0.9586 -0.0642 0.3845  -0.2282 163 GLU   C CA   
4568 C  C    . GLU   C 159 ? 0.6936 0.5225 0.9669 -0.0757 0.3842  -0.2341 163 GLU   C C    
4569 O  O    . GLU   C 159 ? 0.6590 0.6169 1.0226 -0.1127 0.3842  -0.2174 163 GLU   C O    
4570 C  CB   . GLU   C 159 ? 0.6904 0.4918 1.0065 -0.0939 0.3538  -0.2082 163 GLU   C CB   
4571 N  N    . LYS   C 171 ? 0.6840 0.5115 0.5794 0.0326  0.0498  -0.1315 175 LYS   C N    
4572 C  CA   . LYS   C 171 ? 0.6754 0.4613 0.5726 0.0444  0.0648  -0.1369 175 LYS   C CA   
4573 C  C    . LYS   C 171 ? 0.6587 0.3589 0.5265 0.0203  0.0442  -0.1467 175 LYS   C C    
4574 O  O    . LYS   C 171 ? 0.6599 0.3926 0.5031 0.0284  0.0353  -0.1631 175 LYS   C O    
4575 C  CB   . LYS   C 171 ? 0.6862 0.5278 0.5985 0.0386  0.0685  -0.1218 175 LYS   C CB   
4576 C  CG   . LYS   C 171 ? 0.7157 0.5564 0.6061 0.0292  0.0535  -0.1253 175 LYS   C CG   
4577 C  CD   . LYS   C 171 ? 0.7072 0.5604 0.5967 0.0325  0.0676  -0.1264 175 LYS   C CD   
4578 N  N    . SER   C 172 ? 0.5996 0.2648 0.5089 0.0018  0.0419  -0.1331 176 SER   C N    
4579 C  CA   . SER   C 172 ? 0.5595 0.2541 0.4737 -0.0270 0.0446  -0.1300 176 SER   C CA   
4580 C  C    . SER   C 172 ? 0.5305 0.2488 0.4414 -0.0231 0.0465  -0.1266 176 SER   C C    
4581 O  O    . SER   C 172 ? 0.5206 0.2370 0.4530 -0.0139 0.0909  -0.1287 176 SER   C O    
4582 C  CB   . SER   C 172 ? 0.5667 0.2519 0.4817 -0.0328 0.0284  -0.1246 176 SER   C CB   
4583 O  OG   . SER   C 172 ? 0.5630 0.2524 0.4659 -0.0553 0.0235  -0.1354 176 SER   C OG   
4584 N  N    . TYR   C 173 ? 0.5021 0.2429 0.4114 -0.0196 0.0545  -0.1425 177 TYR   C N    
4585 C  CA   . TYR   C 173 ? 0.4965 0.2377 0.3822 -0.0158 0.0597  -0.1235 177 TYR   C CA   
4586 C  C    . TYR   C 173 ? 0.4399 0.2195 0.3739 -0.0117 0.0552  -0.1056 177 TYR   C C    
4587 O  O    . TYR   C 173 ? 0.4191 0.2148 0.3529 0.0006  0.0502  -0.0996 177 TYR   C O    
4588 C  CB   . TYR   C 173 ? 0.5354 0.2671 0.3830 0.0082  0.0596  -0.1171 177 TYR   C CB   
4589 C  CG   . TYR   C 173 ? 0.5838 0.3326 0.3949 0.0150  0.0898  -0.1161 177 TYR   C CG   
4590 C  CD1  . TYR   C 173 ? 0.6092 0.3996 0.3948 0.0204  0.0966  -0.1233 177 TYR   C CD1  
4591 C  CD2  . TYR   C 173 ? 0.6145 0.3782 0.3958 0.0212  0.0959  -0.1309 177 TYR   C CD2  
4592 C  CE1  . TYR   C 173 ? 0.6465 0.4512 0.4233 0.0391  0.1106  -0.1315 177 TYR   C CE1  
4593 C  CE2  . TYR   C 173 ? 0.6427 0.4085 0.4011 0.0332  0.1134  -0.1391 177 TYR   C CE2  
4594 C  CZ   . TYR   C 173 ? 0.6509 0.4463 0.4062 0.0539  0.1296  -0.1493 177 TYR   C CZ   
4595 O  OH   . TYR   C 173 ? 0.6948 0.5565 0.4357 0.0915  0.1740  -0.1172 177 TYR   C OH   
4596 N  N    . SER   C 174 ? 0.3881 0.2232 0.3515 -0.0208 0.0550  -0.1121 178 SER   C N    
4597 C  CA   . SER   C 174 ? 0.3601 0.2206 0.3624 -0.0151 0.0603  -0.1073 178 SER   C CA   
4598 C  C    . SER   C 174 ? 0.3508 0.2096 0.3412 -0.0206 0.0543  -0.0955 178 SER   C C    
4599 O  O    . SER   C 174 ? 0.3495 0.1941 0.3318 -0.0215 0.0467  -0.0787 178 SER   C O    
4600 C  CB   . SER   C 174 ? 0.3513 0.2296 0.3740 -0.0287 0.0678  -0.1012 178 SER   C CB   
4601 O  OG   . SER   C 174 ? 0.3547 0.2449 0.3952 -0.0376 0.0608  -0.0805 178 SER   C OG   
4602 N  N    . LEU   C 175 ? 0.3371 0.2165 0.3391 -0.0211 0.0560  -0.0922 179 LEU   C N    
4603 C  CA   . LEU   C 175 ? 0.3322 0.2147 0.3240 -0.0266 0.0573  -0.0700 179 LEU   C CA   
4604 C  C    . LEU   C 175 ? 0.3461 0.2134 0.3351 -0.0297 0.0564  -0.0581 179 LEU   C C    
4605 O  O    . LEU   C 175 ? 0.3558 0.2110 0.3226 -0.0348 0.0592  -0.0511 179 LEU   C O    
4606 C  CB   . LEU   C 175 ? 0.3269 0.2219 0.3143 -0.0284 0.0496  -0.0716 179 LEU   C CB   
4607 C  CG   . LEU   C 175 ? 0.3168 0.2301 0.3101 -0.0290 0.0401  -0.0662 179 LEU   C CG   
4608 C  CD1  . LEU   C 175 ? 0.3187 0.2512 0.3181 -0.0408 0.0359  -0.0609 179 LEU   C CD1  
4609 C  CD2  . LEU   C 175 ? 0.3159 0.2227 0.2985 -0.0206 0.0349  -0.0616 179 LEU   C CD2  
4610 N  N    . GLY   C 176 ? 0.3549 0.2193 0.3666 -0.0341 0.0708  -0.0507 180 GLY   C N    
4611 C  CA   . GLY   C 176 ? 0.3661 0.2233 0.3914 -0.0287 0.0631  -0.0421 180 GLY   C CA   
4612 C  C    . GLY   C 176 ? 0.3850 0.2238 0.4099 -0.0175 0.0672  -0.0370 180 GLY   C C    
4613 O  O    . GLY   C 176 ? 0.3863 0.2303 0.4352 -0.0201 0.0582  -0.0143 180 GLY   C O    
4614 N  N    . SER   C 177 ? 0.3976 0.2166 0.4305 -0.0261 0.0678  -0.0431 181 SER   C N    
4615 C  CA   . SER   C 177 ? 0.3860 0.2191 0.4513 -0.0162 0.0782  -0.0362 181 SER   C CA   
4616 C  C    . SER   C 177 ? 0.3714 0.2158 0.4334 -0.0060 0.0765  -0.0451 181 SER   C C    
4617 O  O    . SER   C 177 ? 0.3697 0.2192 0.4661 0.0066  0.0746  -0.0497 181 SER   C O    
4618 C  CB   . SER   C 177 ? 0.4096 0.2292 0.4668 -0.0311 0.0699  -0.0417 181 SER   C CB   
4619 O  OG   . SER   C 177 ? 0.4447 0.2400 0.5234 -0.0471 0.0746  -0.0357 181 SER   C OG   
4620 N  N    . ILE   C 178 ? 0.3456 0.1982 0.3863 -0.0032 0.0819  -0.0547 182 ILE   C N    
4621 C  CA   . ILE   C 178 ? 0.3467 0.2123 0.3881 -0.0012 0.0794  -0.0448 182 ILE   C CA   
4622 C  C    . ILE   C 178 ? 0.3450 0.2071 0.4013 0.0075  0.0698  -0.0369 182 ILE   C C    
4623 O  O    . ILE   C 178 ? 0.3455 0.1989 0.4343 0.0195  0.0716  -0.0367 182 ILE   C O    
4624 C  CB   . ILE   C 178 ? 0.3255 0.2121 0.3595 0.0065  0.0777  -0.0554 182 ILE   C CB   
4625 C  CG1  . ILE   C 178 ? 0.3494 0.2235 0.3561 0.0111  0.0683  -0.0605 182 ILE   C CG1  
4626 C  CG2  . ILE   C 178 ? 0.3255 0.2073 0.3544 -0.0010 0.0762  -0.0550 182 ILE   C CG2  
4627 C  CD1  . ILE   C 178 ? 0.3647 0.2311 0.3634 0.0185  0.0621  -0.0615 182 ILE   C CD1  
4628 N  N    . TYR   C 179 ? 0.3487 0.1966 0.4001 0.0155  0.0594  -0.0318 183 TYR   C N    
4629 C  CA   . TYR   C 179 ? 0.3473 0.1965 0.4121 0.0154  0.0542  -0.0272 183 TYR   C CA   
4630 C  C    . TYR   C 179 ? 0.3666 0.2194 0.4706 0.0325  0.0447  -0.0450 183 TYR   C C    
4631 O  O    . TYR   C 179 ? 0.3616 0.2494 0.5117 0.0192  0.0376  -0.0638 183 TYR   C O    
4632 C  CB   . TYR   C 179 ? 0.3419 0.1982 0.3788 0.0095  0.0402  -0.0213 183 TYR   C CB   
4633 C  CG   . TYR   C 179 ? 0.3303 0.2103 0.3660 0.0104  0.0378  -0.0123 183 TYR   C CG   
4634 C  CD1  . TYR   C 179 ? 0.3311 0.2096 0.3679 0.0198  0.0287  -0.0162 183 TYR   C CD1  
4635 C  CD2  . TYR   C 179 ? 0.2923 0.2028 0.3290 0.0191  0.0480  -0.0175 183 TYR   C CD2  
4636 C  CE1  . TYR   C 179 ? 0.3285 0.2065 0.3440 0.0300  0.0262  -0.0142 183 TYR   C CE1  
4637 C  CE2  . TYR   C 179 ? 0.2848 0.1995 0.3274 0.0120  0.0444  -0.0172 183 TYR   C CE2  
4638 C  CZ   . TYR   C 179 ? 0.3014 0.2127 0.3307 0.0139  0.0355  -0.0178 183 TYR   C CZ   
4639 O  OH   . TYR   C 179 ? 0.2974 0.2731 0.3443 0.0208  0.0097  0.0023  183 TYR   C OH   
4640 N  N    . THR   C 180 ? 0.3973 0.2115 0.4997 0.0310  0.0462  -0.0399 184 THR   C N    
4641 C  CA   . THR   C 180 ? 0.4052 0.2375 0.5466 0.0566  0.0487  -0.0404 184 THR   C CA   
4642 C  C    . THR   C 180 ? 0.4142 0.2356 0.5728 0.0667  0.0562  -0.0592 184 THR   C C    
4643 O  O    . THR   C 180 ? 0.4211 0.2700 0.6197 0.0770  0.0250  -0.0635 184 THR   C O    
4644 C  CB   . THR   C 180 ? 0.4446 0.2342 0.5684 0.0413  0.0559  -0.0271 184 THR   C CB   
4645 O  OG1  . THR   C 180 ? 0.4718 0.2732 0.5798 0.0183  0.0682  0.0134  184 THR   C OG1  
4646 C  CG2  . THR   C 180 ? 0.4553 0.2669 0.5905 0.0521  0.0446  -0.0063 184 THR   C CG2  
4647 N  N    . ARG   C 181 ? 0.4205 0.2308 0.5820 0.0734  0.0690  -0.0871 185 ARG   C N    
4648 C  CA   . ARG   C 181 ? 0.3979 0.2621 0.6245 0.1228  0.0902  -0.0978 185 ARG   C CA   
4649 C  C    . ARG   C 181 ? 0.3780 0.2925 0.6283 0.1342  0.1091  -0.0945 185 ARG   C C    
4650 O  O    . ARG   C 181 ? 0.3846 0.3342 0.6484 0.1478  0.1201  -0.1100 185 ARG   C O    
4651 C  CB   . ARG   C 181 ? 0.4558 0.3468 0.6357 0.1264  0.0779  -0.0906 185 ARG   C CB   
4652 C  CG   . ARG   C 181 ? 0.5273 0.3971 0.6423 0.1099  0.0596  -0.0953 185 ARG   C CG   
4653 C  CD   . ARG   C 181 ? 0.5371 0.3739 0.6249 0.0899  0.0632  -0.1133 185 ARG   C CD   
4654 N  NE   . ARG   C 181 ? 0.5390 0.3613 0.5638 0.0870  0.0797  -0.1274 185 ARG   C NE   
4655 C  CZ   . ARG   C 181 ? 0.5450 0.3547 0.5190 0.0770  0.0898  -0.1391 185 ARG   C CZ   
4656 N  NH1  . ARG   C 181 ? 0.5610 0.3639 0.5235 0.0861  0.0979  -0.1247 185 ARG   C NH1  
4657 N  NH2  . ARG   C 181 ? 0.5474 0.3608 0.4778 0.0764  0.1006  -0.1456 185 ARG   C NH2  
4658 N  N    . LEU   C 182 ? 0.3811 0.2804 0.6077 0.0949  0.1183  -0.0810 186 LEU   C N    
4659 C  CA   . LEU   C 182 ? 0.3749 0.2778 0.6083 0.0889  0.1274  -0.0537 186 LEU   C CA   
4660 C  C    . LEU   C 182 ? 0.3569 0.2571 0.6050 0.0857  0.1047  -0.0401 186 LEU   C C    
4661 O  O    . LEU   C 182 ? 0.3656 0.3002 0.6736 0.0670  0.0951  -0.0425 186 LEU   C O    
4662 C  CB   . LEU   C 182 ? 0.3566 0.2877 0.6004 0.1034  0.1527  -0.0519 186 LEU   C CB   
4663 C  CG   . LEU   C 182 ? 0.3919 0.3041 0.6099 0.0922  0.1665  -0.0350 186 LEU   C CG   
4664 C  CD1  . LEU   C 182 ? 0.3921 0.3034 0.6079 0.0971  0.1811  -0.0286 186 LEU   C CD1  
4665 C  CD2  . LEU   C 182 ? 0.4135 0.3364 0.6177 0.0906  0.1730  -0.0360 186 LEU   C CD2  
4666 N  N    . TYR   C 183 ? 0.3627 0.2772 0.5913 0.0737  0.0631  -0.0232 187 TYR   C N    
4667 C  CA   . TYR   C 183 ? 0.3682 0.2770 0.5741 0.0804  0.0438  -0.0019 187 TYR   C CA   
4668 C  C    . TYR   C 183 ? 0.4284 0.3114 0.6066 0.0693  0.0330  0.0304  187 TYR   C C    
4669 O  O    . TYR   C 183 ? 0.4842 0.3430 0.6560 0.0633  -0.0089 0.0375  187 TYR   C O    
4670 C  CB   . TYR   C 183 ? 0.3554 0.2687 0.5329 0.0658  0.0302  0.0018  187 TYR   C CB   
4671 C  CG   . TYR   C 183 ? 0.3355 0.2587 0.5012 0.0774  0.0360  -0.0009 187 TYR   C CG   
4672 C  CD1  . TYR   C 183 ? 0.3203 0.2501 0.4815 0.0897  0.0416  -0.0007 187 TYR   C CD1  
4673 C  CD2  . TYR   C 183 ? 0.3234 0.2549 0.4796 0.0755  0.0475  0.0067  187 TYR   C CD2  
4674 C  CE1  . TYR   C 183 ? 0.3277 0.2689 0.4745 0.0796  0.0457  -0.0008 187 TYR   C CE1  
4675 C  CE2  . TYR   C 183 ? 0.3284 0.2456 0.4718 0.0718  0.0587  0.0040  187 TYR   C CE2  
4676 C  CZ   . TYR   C 183 ? 0.3195 0.2589 0.4560 0.0776  0.0629  -0.0049 187 TYR   C CZ   
4677 O  OH   . TYR   C 183 ? 0.2862 0.2719 0.4430 0.0594  0.1101  -0.0094 187 TYR   C OH   
4678 N  N    . GLY   C 184 ? 0.4330 0.2926 0.6127 0.0769  0.0568  0.0333  188 GLY   C N    
4679 C  CA   . GLY   C 184 ? 0.4656 0.2957 0.6316 0.0909  0.0624  0.0490  188 GLY   C CA   
4680 C  C    . GLY   C 184 ? 0.5153 0.3047 0.6395 0.1129  0.0584  0.0781  188 GLY   C C    
4681 O  O    . GLY   C 184 ? 0.5821 0.3117 0.7020 0.1229  0.0479  0.0936  188 GLY   C O    
4682 N  N    . GLN   C 185 ? 0.5227 0.3304 0.6281 0.1079  0.0802  0.0811  189 GLN   C N    
4683 C  CA   . GLN   C 185 ? 0.5250 0.3519 0.6241 0.1165  0.0666  0.0931  189 GLN   C CA   
4684 C  C    . GLN   C 185 ? 0.5298 0.3136 0.6106 0.1078  0.0620  0.1178  189 GLN   C C    
4685 O  O    . GLN   C 185 ? 0.5514 0.2924 0.6238 0.1075  0.0469  0.1072  189 GLN   C O    
4686 C  CB   . GLN   C 185 ? 0.5142 0.4039 0.6146 0.1443  0.0656  0.1095  189 GLN   C CB   
4687 N  N    . SER   C 186 ? 0.5405 0.3292 0.6031 0.0961  0.0593  0.1029  190 SER   C N    
4688 C  CA   . SER   C 186 ? 0.5291 0.3597 0.6033 0.0610  0.0522  0.1127  190 SER   C CA   
4689 C  C    . SER   C 186 ? 0.5366 0.3618 0.5948 0.0522  0.0347  0.1041  190 SER   C C    
4690 O  O    . SER   C 186 ? 0.5455 0.3500 0.6283 0.0627  0.0037  0.1269  190 SER   C O    
4691 C  CB   . SER   C 186 ? 0.5300 0.3929 0.5914 0.0430  0.0602  0.1144  190 SER   C CB   
4692 N  N    . PRO   C 187 ? 0.5007 0.3538 0.5144 0.0309  0.0626  0.1090  191 PRO   C N    
4693 C  CA   . PRO   C 187 ? 0.4902 0.3787 0.5078 0.0124  0.0688  0.0987  191 PRO   C CA   
4694 C  C    . PRO   C 187 ? 0.4575 0.3626 0.5027 0.0050  0.0637  0.0884  191 PRO   C C    
4695 O  O    . PRO   C 187 ? 0.4673 0.3692 0.5176 -0.0340 0.0695  0.0752  191 PRO   C O    
4696 C  CB   . PRO   C 187 ? 0.5205 0.3784 0.4903 0.0259  0.0627  0.1151  191 PRO   C CB   
4697 C  CG   . PRO   C 187 ? 0.5132 0.3722 0.5103 0.0165  0.0683  0.1024  191 PRO   C CG   
4698 C  CD   . PRO   C 187 ? 0.5075 0.3702 0.5112 0.0146  0.0695  0.1137  191 PRO   C CD   
4699 N  N    . PRO   C 188 ? 0.3841 0.3856 0.5333 0.0150  0.0503  0.0724  192 PRO   C N    
4700 C  CA   . PRO   C 188 ? 0.3812 0.4018 0.5434 0.0168  0.0397  0.0686  192 PRO   C CA   
4701 C  C    . PRO   C 188 ? 0.3731 0.4083 0.5354 0.0098  0.0305  0.0622  192 PRO   C C    
4702 O  O    . PRO   C 188 ? 0.4153 0.4774 0.5477 0.0003  0.0150  0.0833  192 PRO   C O    
4703 C  CB   . PRO   C 188 ? 0.3651 0.4192 0.5672 0.0177  0.0394  0.0531  192 PRO   C CB   
4704 C  CG   . PRO   C 188 ? 0.3761 0.4115 0.5612 0.0204  0.0410  0.0591  192 PRO   C CG   
4705 C  CD   . PRO   C 188 ? 0.3580 0.3855 0.5511 0.0170  0.0447  0.0642  192 PRO   C CD   
4706 N  N    . ASP   C 189 ? 0.3495 0.3932 0.5046 -0.0047 0.0109  0.0306  193 ASP   C N    
4707 C  CA   . ASP   C 189 ? 0.3486 0.3730 0.5038 -0.0296 0.0035  0.0183  193 ASP   C CA   
4708 C  C    . ASP   C 189 ? 0.3476 0.3346 0.4890 -0.0211 0.0029  0.0217  193 ASP   C C    
4709 O  O    . ASP   C 189 ? 0.3708 0.3525 0.4807 -0.0216 0.0092  0.0196  193 ASP   C O    
4710 C  CB   . ASP   C 189 ? 0.3639 0.4029 0.5249 -0.0029 0.0112  0.0005  193 ASP   C CB   
4711 C  CG   . ASP   C 189 ? 0.3750 0.4196 0.5510 -0.0086 0.0216  0.0020  193 ASP   C CG   
4712 O  OD1  . ASP   C 189 ? 0.3654 0.3829 0.6298 -0.0132 0.0267  -0.0169 193 ASP   C OD1  
4713 O  OD2  . ASP   C 189 ? 0.4536 0.4584 0.5792 -0.0013 0.0335  0.0016  193 ASP   C OD2  
4714 N  N    . SER   C 190 ? 0.3155 0.3312 0.4423 -0.0109 0.0035  0.0029  194 SER   C N    
4715 C  CA   . SER   C 190 ? 0.3372 0.3202 0.4137 -0.0110 0.0111  -0.0068 194 SER   C CA   
4716 C  C    . SER   C 190 ? 0.3233 0.3269 0.3781 -0.0319 0.0148  -0.0151 194 SER   C C    
4717 O  O    . SER   C 190 ? 0.3267 0.3782 0.3801 -0.0427 0.0148  -0.0248 194 SER   C O    
4718 C  CB   . SER   C 190 ? 0.4005 0.3370 0.4284 -0.0128 -0.0045 -0.0170 194 SER   C CB   
4719 O  OG   . SER   C 190 ? 0.4630 0.3508 0.4674 -0.0110 -0.0012 -0.0048 194 SER   C OG   
4720 N  N    . HIS   C 191 ? 0.2786 0.2469 0.3466 -0.0406 0.0246  0.0027  195 HIS   C N    
4721 C  CA   . HIS   C 191 ? 0.2584 0.2254 0.3107 -0.0261 0.0196  0.0143  195 HIS   C CA   
4722 C  C    . HIS   C 191 ? 0.2108 0.2044 0.2736 -0.0319 0.0240  0.0110  195 HIS   C C    
4723 O  O    . HIS   C 191 ? 0.2138 0.2190 0.3190 -0.0355 0.0193  0.0160  195 HIS   C O    
4724 C  CB   . HIS   C 191 ? 0.2849 0.2512 0.3165 -0.0302 0.0205  0.0237  195 HIS   C CB   
4725 C  CG   . HIS   C 191 ? 0.3318 0.3007 0.3322 -0.0203 0.0094  0.0082  195 HIS   C CG   
4726 N  ND1  . HIS   C 191 ? 0.3469 0.3444 0.3627 -0.0151 0.0095  -0.0067 195 HIS   C ND1  
4727 C  CD2  . HIS   C 191 ? 0.3533 0.3465 0.3564 -0.0081 0.0158  0.0025  195 HIS   C CD2  
4728 C  CE1  . HIS   C 191 ? 0.3603 0.3711 0.3509 -0.0111 -0.0057 -0.0099 195 HIS   C CE1  
4729 N  NE2  . HIS   C 191 ? 0.3708 0.3676 0.3522 -0.0023 -0.0086 -0.0116 195 HIS   C NE2  
4730 N  N    . THR   C 192 ? 0.1840 0.1860 0.2421 -0.0078 0.0337  0.0245  196 THR   C N    
4731 C  CA   . THR   C 192 ? 0.1710 0.1798 0.2060 -0.0136 0.0312  0.0190  196 THR   C CA   
4732 C  C    . THR   C 192 ? 0.1698 0.1710 0.1901 -0.0090 0.0284  0.0068  196 THR   C C    
4733 O  O    . THR   C 192 ? 0.1784 0.1693 0.2014 -0.0070 0.0325  -0.0008 196 THR   C O    
4734 C  CB   . THR   C 192 ? 0.1809 0.2072 0.2024 -0.0127 0.0255  0.0241  196 THR   C CB   
4735 O  OG1  . THR   C 192 ? 0.1923 0.2475 0.1942 -0.0305 0.0290  0.0334  196 THR   C OG1  
4736 C  CG2  . THR   C 192 ? 0.1950 0.2323 0.2097 -0.0144 0.0190  0.0290  196 THR   C CG2  
4737 N  N    . ALA   C 193 ? 0.1609 0.1673 0.1693 -0.0068 0.0284  0.0011  197 ALA   C N    
4738 C  CA   . ALA   C 193 ? 0.1549 0.1560 0.1649 -0.0103 0.0302  0.0005  197 ALA   C CA   
4739 C  C    . ALA   C 193 ? 0.1616 0.1691 0.1716 -0.0131 0.0239  -0.0070 197 ALA   C C    
4740 O  O    . ALA   C 193 ? 0.1772 0.1705 0.1633 -0.0268 0.0225  -0.0039 197 ALA   C O    
4741 C  CB   . ALA   C 193 ? 0.1567 0.1691 0.1635 -0.0054 0.0359  0.0068  197 ALA   C CB   
4742 N  N    . GLU   C 194 ? 0.1574 0.1778 0.1670 -0.0099 0.0183  -0.0053 198 GLU   C N    
4743 C  CA   . GLU   C 194 ? 0.1625 0.1777 0.1722 -0.0146 0.0132  -0.0027 198 GLU   C CA   
4744 C  C    . GLU   C 194 ? 0.1613 0.1745 0.1755 -0.0134 0.0153  0.0041  198 GLU   C C    
4745 O  O    . GLU   C 194 ? 0.1582 0.1721 0.1813 -0.0103 0.0191  0.0075  198 GLU   C O    
4746 C  CB   . GLU   C 194 ? 0.1906 0.2011 0.1804 -0.0136 0.0070  -0.0104 198 GLU   C CB   
4747 C  CG   . GLU   C 194 ? 0.1998 0.2363 0.1963 -0.0172 -0.0028 -0.0165 198 GLU   C CG   
4748 C  CD   . GLU   C 194 ? 0.2546 0.2758 0.2236 -0.0225 -0.0072 -0.0355 198 GLU   C CD   
4749 O  OE1  . GLU   C 194 ? 0.3352 0.3807 0.2971 -0.0236 0.0220  -0.0602 198 GLU   C OE1  
4750 O  OE2  . GLU   C 194 ? 0.3014 0.3112 0.2964 -0.0267 -0.0432 -0.0397 198 GLU   C OE2  
4751 N  N    . GLY   C 195 ? 0.1673 0.1777 0.1859 -0.0136 0.0266  0.0092  199 GLY   C N    
4752 C  CA   . GLY   C 195 ? 0.1723 0.1790 0.1848 -0.0053 0.0241  0.0122  199 GLY   C CA   
4753 C  C    . GLY   C 195 ? 0.1692 0.1688 0.1838 -0.0068 0.0285  0.0047  199 GLY   C C    
4754 O  O    . GLY   C 195 ? 0.1685 0.1717 0.2009 -0.0066 0.0292  -0.0008 199 GLY   C O    
4755 N  N    . ASP   C 196 ? 0.1692 0.1684 0.1856 -0.0055 0.0283  0.0012  200 ASP   C N    
4756 C  CA   . ASP   C 196 ? 0.1904 0.1794 0.1910 -0.0092 0.0254  -0.0064 200 ASP   C CA   
4757 C  C    . ASP   C 196 ? 0.1787 0.1706 0.1831 -0.0138 0.0266  -0.0208 200 ASP   C C    
4758 O  O    . ASP   C 196 ? 0.1980 0.1648 0.1844 -0.0088 0.0377  -0.0265 200 ASP   C O    
4759 C  CB   . ASP   C 196 ? 0.2069 0.2057 0.2237 -0.0133 0.0162  0.0026  200 ASP   C CB   
4760 C  CG   . ASP   C 196 ? 0.2371 0.2336 0.3081 -0.0223 0.0028  0.0230  200 ASP   C CG   
4761 O  OD1  . ASP   C 196 ? 0.2631 0.2375 0.3311 -0.0073 -0.0023 0.0335  200 ASP   C OD1  
4762 O  OD2  . ASP   C 196 ? 0.2540 0.3112 0.3974 -0.0443 -0.0170 0.0385  200 ASP   C OD2  
4763 N  N    . VAL   C 197 ? 0.1640 0.1620 0.1669 -0.0132 0.0232  -0.0154 201 VAL   C N    
4764 C  CA   . VAL   C 197 ? 0.1657 0.1536 0.1733 -0.0132 0.0179  -0.0141 201 VAL   C CA   
4765 C  C    . VAL   C 197 ? 0.1657 0.1573 0.1752 -0.0126 0.0243  -0.0104 201 VAL   C C    
4766 O  O    . VAL   C 197 ? 0.1709 0.1632 0.1771 -0.0215 0.0304  -0.0038 201 VAL   C O    
4767 C  CB   . VAL   C 197 ? 0.1762 0.1548 0.1908 -0.0114 0.0170  -0.0149 201 VAL   C CB   
4768 C  CG1  . VAL   C 197 ? 0.1824 0.1644 0.1937 -0.0134 0.0191  -0.0079 201 VAL   C CG1  
4769 C  CG2  . VAL   C 197 ? 0.1794 0.1613 0.1973 -0.0113 0.0157  -0.0211 201 VAL   C CG2  
4770 N  N    . LEU   C 198 ? 0.1664 0.1654 0.1841 -0.0095 0.0222  -0.0023 202 LEU   C N    
4771 C  CA   . LEU   C 198 ? 0.1692 0.1748 0.1924 -0.0052 0.0222  -0.0028 202 LEU   C CA   
4772 C  C    . LEU   C 198 ? 0.1707 0.1704 0.1981 -0.0004 0.0199  -0.0014 202 LEU   C C    
4773 O  O    . LEU   C 198 ? 0.1758 0.1858 0.2084 -0.0027 0.0266  -0.0061 202 LEU   C O    
4774 C  CB   . LEU   C 198 ? 0.1698 0.1916 0.1948 -0.0053 0.0096  -0.0077 202 LEU   C CB   
4775 C  CG   . LEU   C 198 ? 0.1870 0.2062 0.2027 -0.0044 0.0140  -0.0149 202 LEU   C CG   
4776 C  CD1  . LEU   C 198 ? 0.2063 0.2187 0.2057 -0.0076 0.0102  -0.0128 202 LEU   C CD1  
4777 C  CD2  . LEU   C 198 ? 0.2024 0.2051 0.2086 -0.0042 0.0106  -0.0163 202 LEU   C CD2  
4778 N  N    . ALA   C 199 ? 0.1677 0.1672 0.2123 -0.0013 0.0297  -0.0059 203 ALA   C N    
4779 C  CA   . ALA   C 199 ? 0.1787 0.1629 0.2211 -0.0073 0.0347  -0.0097 203 ALA   C CA   
4780 C  C    . ALA   C 199 ? 0.1804 0.1540 0.2193 -0.0082 0.0352  -0.0131 203 ALA   C C    
4781 O  O    . ALA   C 199 ? 0.2013 0.1583 0.2421 -0.0014 0.0489  -0.0241 203 ALA   C O    
4782 C  CB   . ALA   C 199 ? 0.1960 0.1562 0.2340 -0.0090 0.0383  -0.0097 203 ALA   C CB   
4783 N  N    . LEU   C 200 ? 0.1759 0.1475 0.2011 -0.0076 0.0356  -0.0150 204 LEU   C N    
4784 C  CA   . LEU   C 200 ? 0.1813 0.1599 0.1960 -0.0175 0.0362  -0.0144 204 LEU   C CA   
4785 C  C    . LEU   C 200 ? 0.1752 0.1606 0.2003 -0.0139 0.0384  -0.0196 204 LEU   C C    
4786 O  O    . LEU   C 200 ? 0.1930 0.1799 0.1978 -0.0184 0.0452  -0.0157 204 LEU   C O    
4787 C  CB   . LEU   C 200 ? 0.1871 0.1687 0.2001 -0.0233 0.0210  -0.0056 204 LEU   C CB   
4788 C  CG   . LEU   C 200 ? 0.1991 0.1809 0.2120 -0.0293 0.0191  0.0053  204 LEU   C CG   
4789 C  CD1  . LEU   C 200 ? 0.2058 0.1983 0.2278 -0.0275 0.0178  0.0033  204 LEU   C CD1  
4790 C  CD2  . LEU   C 200 ? 0.2007 0.1996 0.2262 -0.0332 0.0140  0.0099  204 LEU   C CD2  
4791 N  N    . LEU   C 201 ? 0.1640 0.1756 0.1926 -0.0157 0.0401  -0.0192 205 LEU   C N    
4792 C  CA   . LEU   C 201 ? 0.1715 0.1814 0.2093 -0.0170 0.0348  -0.0273 205 LEU   C CA   
4793 C  C    . LEU   C 201 ? 0.1719 0.1757 0.2272 -0.0105 0.0359  -0.0205 205 LEU   C C    
4794 O  O    . LEU   C 201 ? 0.1745 0.1849 0.2457 -0.0046 0.0429  -0.0184 205 LEU   C O    
4795 C  CB   . LEU   C 201 ? 0.1755 0.1872 0.2175 -0.0206 0.0320  -0.0350 205 LEU   C CB   
4796 C  CG   . LEU   C 201 ? 0.1752 0.2071 0.2337 -0.0244 0.0236  -0.0282 205 LEU   C CG   
4797 C  CD1  . LEU   C 201 ? 0.1710 0.2072 0.2503 -0.0277 0.0216  -0.0270 205 LEU   C CD1  
4798 C  CD2  . LEU   C 201 ? 0.1983 0.2206 0.2420 -0.0359 0.0274  -0.0319 205 LEU   C CD2  
4799 N  N    . SER   C 202 ? 0.1741 0.1853 0.2438 -0.0078 0.0471  -0.0057 206 SER   C N    
4800 C  CA   . SER   C 202 ? 0.1875 0.1901 0.2604 0.0029  0.0506  -0.0047 206 SER   C CA   
4801 C  C    . SER   C 202 ? 0.2142 0.1834 0.2717 0.0079  0.0640  -0.0146 206 SER   C C    
4802 O  O    . SER   C 202 ? 0.2235 0.1977 0.2876 0.0063  0.0768  -0.0140 206 SER   C O    
4803 C  CB   . SER   C 202 ? 0.1893 0.1945 0.2776 0.0105  0.0431  0.0018  206 SER   C CB   
4804 O  OG   . SER   C 202 ? 0.2071 0.2135 0.2915 0.0131  0.0392  -0.0059 206 SER   C OG   
4805 N  N    . ILE   C 203 ? 0.2263 0.1819 0.2502 0.0098  0.0683  -0.0272 207 ILE   C N    
4806 C  CA   . ILE   C 203 ? 0.2643 0.1912 0.2556 0.0011  0.0713  -0.0293 207 ILE   C CA   
4807 C  C    . ILE   C 203 ? 0.2672 0.1992 0.2453 0.0000  0.0786  -0.0294 207 ILE   C C    
4808 O  O    . ILE   C 203 ? 0.3072 0.2130 0.2689 -0.0043 0.1050  -0.0413 207 ILE   C O    
4809 C  CB   . ILE   C 203 ? 0.2880 0.1983 0.2651 -0.0165 0.0651  -0.0339 207 ILE   C CB   
4810 C  CG1  . ILE   C 203 ? 0.2905 0.1893 0.2875 -0.0199 0.0598  -0.0399 207 ILE   C CG1  
4811 C  CG2  . ILE   C 203 ? 0.2998 0.2167 0.2709 -0.0261 0.0624  -0.0316 207 ILE   C CG2  
4812 C  CD1  . ILE   C 203 ? 0.2925 0.1949 0.3007 -0.0215 0.0664  -0.0422 207 ILE   C CD1  
4813 N  N    . CYS   C 204 ? 0.2541 0.1911 0.2151 -0.0039 0.0795  -0.0246 208 CYS   C N    
4814 C  CA   . CYS   C 204 ? 0.2516 0.1964 0.2277 0.0039  0.0747  -0.0149 208 CYS   C CA   
4815 C  C    . CYS   C 204 ? 0.2347 0.2098 0.2440 0.0145  0.0869  -0.0025 208 CYS   C C    
4816 O  O    . CYS   C 204 ? 0.2404 0.2403 0.2619 0.0013  0.0947  0.0130  208 CYS   C O    
4817 C  CB   . CYS   C 204 ? 0.2498 0.2048 0.2256 0.0030  0.0759  -0.0182 208 CYS   C CB   
4818 S  SG   . CYS   C 204 ? 0.2801 0.2340 0.2292 -0.0054 0.0542  -0.0307 208 CYS   C SG   
4819 N  N    . GLN   C 205 ? 0.2218 0.2139 0.2679 0.0146  0.0780  -0.0036 209 GLN   C N    
4820 C  CA   . GLN   C 205 ? 0.2215 0.2403 0.2912 0.0176  0.0805  -0.0053 209 GLN   C CA   
4821 C  C    . GLN   C 205 ? 0.2449 0.2711 0.3077 0.0376  0.0885  -0.0066 209 GLN   C C    
4822 O  O    . GLN   C 205 ? 0.2391 0.3260 0.3209 0.0492  0.0937  -0.0166 209 GLN   C O    
4823 C  CB   . GLN   C 205 ? 0.2104 0.2370 0.3041 0.0101  0.0689  -0.0156 209 GLN   C CB   
4824 C  CG   . GLN   C 205 ? 0.2066 0.2463 0.3095 0.0005  0.0625  -0.0219 209 GLN   C CG   
4825 C  CD   . GLN   C 205 ? 0.2245 0.2645 0.3261 -0.0029 0.0444  -0.0270 209 GLN   C CD   
4826 O  OE1  . GLN   C 205 ? 0.2374 0.3322 0.3080 0.0045  0.0377  -0.0076 209 GLN   C OE1  
4827 N  NE2  . GLN   C 205 ? 0.2372 0.2823 0.3354 -0.0170 0.0294  -0.0468 209 GLN   C NE2  
4828 N  N    . TRP   C 206 ? 0.2630 0.2711 0.3106 0.0437  0.1133  -0.0059 210 TRP   C N    
4829 C  CA   . TRP   C 206 ? 0.2962 0.2865 0.3468 0.0564  0.1121  -0.0140 210 TRP   C CA   
4830 C  C    . TRP   C 206 ? 0.2803 0.2829 0.3293 0.0509  0.1053  -0.0135 210 TRP   C C    
4831 O  O    . TRP   C 206 ? 0.2809 0.3291 0.3443 0.0662  0.1091  0.0055  210 TRP   C O    
4832 C  CB   . TRP   C 206 ? 0.3408 0.2851 0.3753 0.0548  0.1292  -0.0266 210 TRP   C CB   
4833 C  CG   . TRP   C 206 ? 0.4098 0.3058 0.4257 0.0675  0.1380  -0.0391 210 TRP   C CG   
4834 C  CD1  . TRP   C 206 ? 0.4097 0.3649 0.4689 0.0708  0.1253  -0.0363 210 TRP   C CD1  
4835 C  CD2  . TRP   C 206 ? 0.4870 0.3612 0.4513 0.0603  0.1275  -0.0451 210 TRP   C CD2  
4836 N  NE1  . TRP   C 206 ? 0.4734 0.3931 0.4930 0.0788  0.1281  -0.0511 210 TRP   C NE1  
4837 C  CE2  . TRP   C 206 ? 0.4730 0.3918 0.4694 0.0682  0.1312  -0.0556 210 TRP   C CE2  
4838 C  CE3  . TRP   C 206 ? 0.5364 0.3882 0.4513 0.0634  0.1216  -0.0663 210 TRP   C CE3  
4839 C  CZ2  . TRP   C 206 ? 0.5330 0.4362 0.4918 0.0670  0.1202  -0.0742 210 TRP   C CZ2  
4840 C  CZ3  . TRP   C 206 ? 0.5639 0.4202 0.4783 0.0736  0.1236  -0.0826 210 TRP   C CZ3  
4841 C  CH2  . TRP   C 206 ? 0.5540 0.4283 0.4898 0.0758  0.1156  -0.0723 210 TRP   C CH2  
4842 N  N    . ARG   C 207 ? 0.2886 0.2484 0.3087 0.0324  0.1081  -0.0039 211 ARG   C N    
4843 C  CA   . ARG   C 207 ? 0.2977 0.2520 0.3062 0.0145  0.0996  -0.0047 211 ARG   C CA   
4844 C  C    . ARG   C 207 ? 0.3011 0.2426 0.2719 0.0043  0.0837  -0.0078 211 ARG   C C    
4845 O  O    . ARG   C 207 ? 0.3066 0.2059 0.2331 0.0095  0.0905  0.0006  211 ARG   C O    
4846 C  CB   . ARG   C 207 ? 0.3347 0.2658 0.3367 0.0020  0.0899  -0.0061 211 ARG   C CB   
4847 C  CG   . ARG   C 207 ? 0.3675 0.2858 0.3710 0.0094  0.0833  0.0024  211 ARG   C CG   
4848 C  CD   . ARG   C 207 ? 0.3909 0.3394 0.4041 0.0014  0.0737  0.0060  211 ARG   C CD   
4849 N  N    . PRO   C 208 ? 0.2763 0.2499 0.2592 -0.0137 0.0814  -0.0102 212 PRO   C N    
4850 C  CA   . PRO   C 208 ? 0.2812 0.2361 0.2434 -0.0181 0.0817  -0.0058 212 PRO   C CA   
4851 C  C    . PRO   C 208 ? 0.2638 0.2360 0.2172 -0.0296 0.0863  -0.0079 212 PRO   C C    
4852 O  O    . PRO   C 208 ? 0.2705 0.2306 0.2482 -0.0246 0.0956  -0.0069 212 PRO   C O    
4853 C  CB   . PRO   C 208 ? 0.2972 0.2419 0.2456 -0.0203 0.0818  -0.0102 212 PRO   C CB   
4854 C  CG   . PRO   C 208 ? 0.3011 0.2584 0.2664 -0.0205 0.0759  -0.0055 212 PRO   C CG   
4855 C  CD   . PRO   C 208 ? 0.2956 0.2664 0.2713 -0.0111 0.0798  -0.0107 212 PRO   C CD   
4856 N  N    . GLN   C 209 ? 0.2726 0.2527 0.2211 -0.0336 0.0888  -0.0193 213 GLN   C N    
4857 C  CA   . GLN   C 209 ? 0.2809 0.2542 0.2396 -0.0372 0.0944  -0.0027 213 GLN   C CA   
4858 C  C    . GLN   C 209 ? 0.2822 0.2532 0.2240 -0.0259 0.0975  0.0094  213 GLN   C C    
4859 O  O    . GLN   C 209 ? 0.3009 0.2228 0.2108 -0.0214 0.0982  0.0114  213 GLN   C O    
4860 C  CB   . GLN   C 209 ? 0.2802 0.2935 0.2738 -0.0400 0.0967  -0.0164 213 GLN   C CB   
4861 C  CG   . GLN   C 209 ? 0.2868 0.3300 0.3167 -0.0466 0.0895  -0.0202 213 GLN   C CG   
4862 C  CD   . GLN   C 209 ? 0.3233 0.3672 0.3731 -0.0432 0.0774  -0.0136 213 GLN   C CD   
4863 O  OE1  . GLN   C 209 ? 0.3362 0.3991 0.3808 -0.0582 0.0834  -0.0017 213 GLN   C OE1  
4864 N  NE2  . GLN   C 209 ? 0.3486 0.3998 0.4504 -0.0404 0.0592  -0.0135 213 GLN   C NE2  
4865 N  N    . ALA   C 210 ? 0.3249 0.2412 0.2532 -0.0209 0.0705  0.0532  214 ALA   C N    
4866 C  CA   . ALA   C 210 ? 0.3396 0.2477 0.1834 -0.0264 0.0817  0.0067  214 ALA   C CA   
4867 C  C    . ALA   C 210 ? 0.3326 0.2758 0.1086 -0.0391 0.0710  -0.0240 214 ALA   C C    
4868 O  O    . ALA   C 210 ? 0.3082 0.2444 0.2129 -0.0486 0.0625  -0.0562 214 ALA   C O    
4869 C  CB   . ALA   C 210 ? 0.3535 0.2648 0.2185 -0.0118 0.0799  0.0005  214 ALA   C CB   
4870 N  N    . LEU   C 211 ? 0.3076 0.3341 0.1467 -0.0491 0.0911  0.0124  215 LEU   C N    
4871 C  CA   . LEU   C 211 ? 0.2952 0.2568 0.1324 -0.0501 0.0697  -0.0349 215 LEU   C CA   
4872 C  C    . LEU   C 211 ? 0.2713 0.2299 0.1943 -0.0615 0.0500  -0.0261 215 LEU   C C    
4873 O  O    . LEU   C 211 ? 0.3015 0.2106 0.2159 -0.0684 0.0333  -0.0273 215 LEU   C O    
4874 C  CB   . LEU   C 211 ? 0.2983 0.2618 0.1545 -0.0520 0.0761  -0.0253 215 LEU   C CB   
4875 C  CG   . LEU   C 211 ? 0.2952 0.2839 0.1941 -0.0500 0.0787  -0.0316 215 LEU   C CG   
4876 C  CD1  . LEU   C 211 ? 0.3071 0.2917 0.2003 -0.0347 0.0743  -0.0363 215 LEU   C CD1  
4877 C  CD2  . LEU   C 211 ? 0.3004 0.2975 0.1981 -0.0529 0.0791  -0.0331 215 LEU   C CD2  
4878 N  N    . LEU   C 212 ? 0.2649 0.1935 0.2027 -0.0387 0.0450  -0.0443 216 LEU   C N    
4879 C  CA   . LEU   C 212 ? 0.2630 0.1927 0.2026 -0.0513 0.0352  -0.0212 216 LEU   C CA   
4880 C  C    . LEU   C 212 ? 0.2703 0.1999 0.1979 -0.0492 0.0378  -0.0300 216 LEU   C C    
4881 O  O    . LEU   C 212 ? 0.2639 0.2281 0.2063 -0.0584 0.0276  -0.0341 216 LEU   C O    
4882 C  CB   . LEU   C 212 ? 0.2786 0.2024 0.2049 -0.0508 0.0251  -0.0133 216 LEU   C CB   
4883 C  CG   . LEU   C 212 ? 0.2703 0.1941 0.2112 -0.0549 0.0197  -0.0113 216 LEU   C CG   
4884 C  CD1  . LEU   C 212 ? 0.2747 0.2009 0.2216 -0.0513 0.0184  -0.0125 216 LEU   C CD1  
4885 C  CD2  . LEU   C 212 ? 0.2659 0.1989 0.2158 -0.0595 0.0150  -0.0094 216 LEU   C CD2  
4886 N  N    . ARG   C 213 ? 0.2946 0.2377 0.2028 -0.0416 0.0444  -0.0262 217 ARG   C N    
4887 C  CA   . ARG   C 213 ? 0.3213 0.2539 0.1982 -0.0435 0.0431  -0.0279 217 ARG   C CA   
4888 C  C    . ARG   C 213 ? 0.3302 0.2521 0.1909 -0.0438 0.0376  -0.0347 217 ARG   C C    
4889 O  O    . ARG   C 213 ? 0.3238 0.2643 0.1800 -0.0611 0.0340  -0.0294 217 ARG   C O    
4890 C  CB   . ARG   C 213 ? 0.3529 0.2920 0.2369 -0.0216 0.0559  -0.0252 217 ARG   C CB   
4891 C  CG   . ARG   C 213 ? 0.3922 0.3157 0.2769 -0.0229 0.0508  -0.0175 217 ARG   C CG   
4892 C  CD   . ARG   C 213 ? 0.4155 0.3513 0.3117 -0.0054 0.0713  -0.0097 217 ARG   C CD   
4893 N  NE   . ARG   C 213 ? 0.4631 0.3692 0.3539 0.0005  0.0756  -0.0215 217 ARG   C NE   
4894 C  CZ   . ARG   C 213 ? 0.4568 0.3954 0.3516 -0.0042 0.0793  -0.0210 217 ARG   C CZ   
4895 N  NH1  . ARG   C 213 ? 0.4956 0.4063 0.3903 -0.0099 0.0678  -0.0401 217 ARG   C NH1  
4896 N  NH2  . ARG   C 213 ? 0.4583 0.4130 0.3772 0.0086  0.1197  -0.0281 217 ARG   C NH2  
4897 N  N    . TRP   C 214 ? 0.3360 0.2563 0.1934 -0.0570 0.0329  -0.0452 218 TRP   C N    
4898 C  CA   . TRP   C 214 ? 0.3490 0.2526 0.2179 -0.0702 0.0336  -0.0579 218 TRP   C CA   
4899 C  C    . TRP   C 214 ? 0.3184 0.2511 0.2106 -0.0773 0.0249  -0.0492 218 TRP   C C    
4900 O  O    . TRP   C 214 ? 0.3342 0.2540 0.2144 -0.0796 0.0194  -0.0648 218 TRP   C O    
4901 C  CB   . TRP   C 214 ? 0.3883 0.2625 0.2610 -0.0712 0.0333  -0.0604 218 TRP   C CB   
4902 C  CG   . TRP   C 214 ? 0.4188 0.2863 0.3049 -0.0907 0.0302  -0.0793 218 TRP   C CG   
4903 C  CD1  . TRP   C 214 ? 0.4490 0.3241 0.3079 -0.0950 0.0383  -0.0822 218 TRP   C CD1  
4904 C  CD2  . TRP   C 214 ? 0.4484 0.3103 0.3373 -0.0919 0.0588  -0.0494 218 TRP   C CD2  
4905 N  NE1  . TRP   C 214 ? 0.4646 0.3489 0.3597 -0.0930 0.0359  -0.0768 218 TRP   C NE1  
4906 C  CE2  . TRP   C 214 ? 0.4527 0.3370 0.3463 -0.1023 0.0515  -0.0570 218 TRP   C CE2  
4907 C  CE3  . TRP   C 214 ? 0.4513 0.3178 0.3470 -0.0965 0.0773  -0.0329 218 TRP   C CE3  
4908 C  CZ2  . TRP   C 214 ? 0.4722 0.3666 0.3827 -0.0869 0.0521  -0.0390 218 TRP   C CZ2  
4909 C  CZ3  . TRP   C 214 ? 0.4613 0.3566 0.3757 -0.0923 0.0632  -0.0305 218 TRP   C CZ3  
4910 C  CH2  . TRP   C 214 ? 0.4670 0.3679 0.3778 -0.0874 0.0617  -0.0327 218 TRP   C CH2  
4911 N  N    . VAL   C 215 ? 0.2865 0.2255 0.2027 -0.0741 0.0213  -0.0409 219 VAL   C N    
4912 C  CA   . VAL   C 215 ? 0.2831 0.2413 0.2079 -0.0644 0.0150  -0.0380 219 VAL   C CA   
4913 C  C    . VAL   C 215 ? 0.2723 0.2494 0.1932 -0.0587 0.0115  -0.0379 219 VAL   C C    
4914 O  O    . VAL   C 215 ? 0.2993 0.2914 0.1966 -0.0537 -0.0045 -0.0359 219 VAL   C O    
4915 C  CB   . VAL   C 215 ? 0.2765 0.2382 0.2107 -0.0517 0.0169  -0.0358 219 VAL   C CB   
4916 C  CG1  . VAL   C 215 ? 0.2829 0.2416 0.2142 -0.0433 0.0136  -0.0331 219 VAL   C CG1  
4917 C  CG2  . VAL   C 215 ? 0.2863 0.2561 0.2221 -0.0536 0.0098  -0.0266 219 VAL   C CG2  
4918 N  N    . ASP   C 216 ? 0.2751 0.2532 0.1828 -0.0589 0.0156  -0.0296 220 ASP   C N    
4919 C  CA   . ASP   C 216 ? 0.2690 0.2490 0.1907 -0.0505 0.0057  -0.0314 220 ASP   C CA   
4920 C  C    . ASP   C 216 ? 0.2910 0.2796 0.2053 -0.0557 -0.0086 -0.0327 220 ASP   C C    
4921 O  O    . ASP   C 216 ? 0.3056 0.2896 0.2457 -0.0468 -0.0314 -0.0406 220 ASP   C O    
4922 C  CB   . ASP   C 216 ? 0.2671 0.2405 0.2023 -0.0506 0.0054  -0.0222 220 ASP   C CB   
4923 C  CG   . ASP   C 216 ? 0.2664 0.2340 0.2038 -0.0397 0.0092  -0.0183 220 ASP   C CG   
4924 O  OD1  . ASP   C 216 ? 0.2664 0.2175 0.2228 -0.0354 0.0199  -0.0195 220 ASP   C OD1  
4925 O  OD2  . ASP   C 216 ? 0.2662 0.2269 0.1967 -0.0399 -0.0058 -0.0025 220 ASP   C OD2  
4926 N  N    . ALA   C 217 ? 0.3043 0.3020 0.1995 -0.0606 0.0003  -0.0344 221 ALA   C N    
4927 C  CA   . ALA   C 217 ? 0.3199 0.3411 0.1958 -0.0633 -0.0066 -0.0327 221 ALA   C CA   
4928 C  C    . ALA   C 217 ? 0.3226 0.3622 0.1994 -0.0656 -0.0090 -0.0371 221 ALA   C C    
4929 O  O    . ALA   C 217 ? 0.3462 0.4178 0.2014 -0.0638 -0.0130 -0.0185 221 ALA   C O    
4930 C  CB   . ALA   C 217 ? 0.3318 0.3574 0.1991 -0.0574 -0.0032 -0.0339 221 ALA   C CB   
4931 N  N    . HIS   C 218 ? 0.3096 0.3496 0.2009 -0.0786 -0.0084 -0.0401 222 HIS   C N    
4932 C  CA   . HIS   C 218 ? 0.3077 0.3482 0.2363 -0.0827 -0.0087 -0.0491 222 HIS   C CA   
4933 C  C    . HIS   C 218 ? 0.2848 0.3316 0.2121 -0.0978 -0.0061 -0.0287 222 HIS   C C    
4934 O  O    . HIS   C 218 ? 0.2917 0.3252 0.2373 -0.1022 -0.0029 -0.0270 222 HIS   C O    
4935 C  CB   . HIS   C 218 ? 0.3259 0.3545 0.2868 -0.0856 -0.0089 -0.0528 222 HIS   C CB   
4936 C  CG   . HIS   C 218 ? 0.3845 0.3848 0.3346 -0.0732 -0.0205 -0.0966 222 HIS   C CG   
4937 N  ND1  . HIS   C 218 ? 0.3933 0.4007 0.3855 -0.0726 -0.0167 -0.1144 222 HIS   C ND1  
4938 C  CD2  . HIS   C 218 ? 0.4108 0.4347 0.3552 -0.0660 -0.0407 -0.1236 222 HIS   C CD2  
4939 C  CE1  . HIS   C 218 ? 0.4231 0.4310 0.3926 -0.0762 -0.0240 -0.1350 222 HIS   C CE1  
4940 N  NE2  . HIS   C 218 ? 0.4314 0.4575 0.3933 -0.0539 -0.0321 -0.1277 222 HIS   C NE2  
4941 N  N    . ALA   C 219 ? 0.3002 0.3283 0.2055 -0.0889 0.0009  -0.0231 223 ALA   C N    
4942 C  CA   . ALA   C 219 ? 0.2863 0.3503 0.1920 -0.0794 -0.0092 -0.0057 223 ALA   C CA   
4943 C  C    . ALA   C 219 ? 0.2966 0.3622 0.1600 -0.0803 -0.0206 0.0184  223 ALA   C C    
4944 O  O    . ALA   C 219 ? 0.3047 0.3681 0.1733 -0.0787 -0.0171 0.0413  223 ALA   C O    
4945 C  CB   . ALA   C 219 ? 0.2842 0.3536 0.2195 -0.0720 -0.0083 -0.0262 223 ALA   C CB   
4946 N  N    A ARG   C 220 ? 0.2869 0.3701 0.1584 -0.0756 -0.0316 0.0304  224 ARG   C N    
4947 N  N    B ARG   C 220 ? 0.3010 0.3655 0.1629 -0.0785 -0.0221 0.0284  224 ARG   C N    
4948 C  CA   A ARG   C 220 ? 0.2923 0.3889 0.1719 -0.0702 -0.0338 0.0369  224 ARG   C CA   
4949 C  CA   B ARG   C 220 ? 0.3113 0.3809 0.1806 -0.0729 -0.0205 0.0335  224 ARG   C CA   
4950 C  C    A ARG   C 220 ? 0.2746 0.3623 0.1619 -0.0770 -0.0387 0.0473  224 ARG   C C    
4951 C  C    B ARG   C 220 ? 0.2847 0.3564 0.1663 -0.0779 -0.0316 0.0460  224 ARG   C C    
4952 O  O    A ARG   C 220 ? 0.2592 0.3422 0.1539 -0.0758 -0.0405 0.0449  224 ARG   C O    
4953 O  O    B ARG   C 220 ? 0.2682 0.3370 0.1581 -0.0768 -0.0344 0.0433  224 ARG   C O    
4954 C  CB   A ARG   C 220 ? 0.3186 0.4068 0.2133 -0.0654 -0.0474 0.0303  224 ARG   C CB   
4955 C  CB   B ARG   C 220 ? 0.3593 0.3930 0.2311 -0.0725 -0.0209 0.0218  224 ARG   C CB   
4956 C  CG   A ARG   C 220 ? 0.3347 0.4486 0.2299 -0.0484 -0.0633 0.0363  224 ARG   C CG   
4957 C  CG   B ARG   C 220 ? 0.3918 0.4281 0.2619 -0.0575 -0.0206 0.0221  224 ARG   C CG   
4958 C  CD   A ARG   C 220 ? 0.3437 0.4608 0.2468 -0.0422 -0.0792 0.0369  224 ARG   C CD   
4959 C  CD   B ARG   C 220 ? 0.4318 0.4365 0.2921 -0.0562 -0.0108 0.0225  224 ARG   C CD   
4960 N  NE   A ARG   C 220 ? 0.3450 0.4917 0.2587 -0.0440 -0.0784 0.0377  224 ARG   C NE   
4961 N  NE   B ARG   C 220 ? 0.4812 0.4437 0.3315 -0.0483 -0.0020 0.0221  224 ARG   C NE   
4962 C  CZ   A ARG   C 220 ? 0.3565 0.5003 0.2630 -0.0377 -0.0806 0.0327  224 ARG   C CZ   
4963 C  CZ   B ARG   C 220 ? 0.4953 0.4442 0.3102 -0.0518 0.0231  0.0418  224 ARG   C CZ   
4964 N  NH1  A ARG   C 220 ? 0.3644 0.5169 0.2700 -0.0264 -0.0867 0.0311  224 ARG   C NH1  
4965 N  NH1  B ARG   C 220 ? 0.5100 0.4592 0.2978 -0.0463 0.0242  0.0349  224 ARG   C NH1  
4966 N  NH2  A ARG   C 220 ? 0.3588 0.5053 0.2751 -0.0363 -0.0753 0.0271  224 ARG   C NH2  
4967 N  NH2  B ARG   C 220 ? 0.5014 0.4334 0.2986 -0.0453 0.0309  0.0710  224 ARG   C NH2  
4968 N  N    . PRO   C 221 ? 0.2866 0.3567 0.1623 -0.0782 -0.0340 0.0571  225 PRO   C N    
4969 C  CA   . PRO   C 221 ? 0.2877 0.3359 0.1833 -0.0699 -0.0373 0.0658  225 PRO   C CA   
4970 C  C    . PRO   C 221 ? 0.2833 0.3127 0.2019 -0.0738 -0.0377 0.0568  225 PRO   C C    
4971 O  O    . PRO   C 221 ? 0.2907 0.3074 0.2127 -0.0749 -0.0410 0.0436  225 PRO   C O    
4972 C  CB   . PRO   C 221 ? 0.3068 0.3581 0.2114 -0.0636 -0.0485 0.0681  225 PRO   C CB   
4973 C  CG   . PRO   C 221 ? 0.3191 0.3774 0.2080 -0.0661 -0.0402 0.0658  225 PRO   C CG   
4974 C  CD   . PRO   C 221 ? 0.3046 0.3666 0.1729 -0.0662 -0.0405 0.0683  225 PRO   C CD   
4975 N  N    . PHE   C 222 ? 0.2794 0.3092 0.2092 -0.0744 -0.0387 0.0508  226 PHE   C N    
4976 C  CA   . PHE   C 222 ? 0.2905 0.3045 0.2133 -0.0679 -0.0321 0.0613  226 PHE   C CA   
4977 C  C    . PHE   C 222 ? 0.2973 0.3368 0.2233 -0.0696 -0.0317 0.0633  226 PHE   C C    
4978 O  O    . PHE   C 222 ? 0.2827 0.3468 0.2165 -0.0748 -0.0118 0.0516  226 PHE   C O    
4979 C  CB   . PHE   C 222 ? 0.3053 0.3020 0.2135 -0.0607 -0.0394 0.0571  226 PHE   C CB   
4980 C  CG   . PHE   C 222 ? 0.3099 0.2780 0.2050 -0.0505 -0.0447 0.0593  226 PHE   C CG   
4981 C  CD1  . PHE   C 222 ? 0.3457 0.2906 0.2099 -0.0434 -0.0414 0.0513  226 PHE   C CD1  
4982 C  CD2  . PHE   C 222 ? 0.3417 0.2861 0.2141 -0.0446 -0.0304 0.0698  226 PHE   C CD2  
4983 C  CE1  . PHE   C 222 ? 0.3460 0.2641 0.2141 -0.0421 -0.0404 0.0526  226 PHE   C CE1  
4984 C  CE2  . PHE   C 222 ? 0.3418 0.2981 0.2393 -0.0415 -0.0191 0.0760  226 PHE   C CE2  
4985 C  CZ   . PHE   C 222 ? 0.3456 0.2765 0.2270 -0.0502 -0.0278 0.0634  226 PHE   C CZ   
4986 N  N    . GLY   C 223 ? 0.2896 0.3707 0.2701 -0.0529 -0.0319 0.0761  227 GLY   C N    
4987 C  CA   . GLY   C 223 ? 0.2915 0.4032 0.2826 -0.0527 -0.0367 0.0901  227 GLY   C CA   
4988 C  C    . GLY   C 223 ? 0.2824 0.4152 0.2865 -0.0613 -0.0442 0.0938  227 GLY   C C    
4989 O  O    . GLY   C 223 ? 0.2840 0.4759 0.3615 -0.0258 -0.0635 0.1043  227 GLY   C O    
4990 N  N    . THR   C 224 ? 0.2857 0.4223 0.2325 -0.0740 -0.0320 0.0976  228 THR   C N    
4991 C  CA   . THR   C 224 ? 0.3189 0.4414 0.2283 -0.0792 -0.0430 0.0830  228 THR   C CA   
4992 C  C    . THR   C 224 ? 0.2992 0.4402 0.1717 -0.0839 -0.0397 0.0704  228 THR   C C    
4993 O  O    . THR   C 224 ? 0.3293 0.4683 0.2024 -0.0941 -0.0377 0.0612  228 THR   C O    
4994 C  CB   . THR   C 224 ? 0.3573 0.4648 0.2369 -0.0920 -0.0251 0.0639  228 THR   C CB   
4995 O  OG1  . THR   C 224 ? 0.3644 0.4749 0.2328 -0.0887 -0.0128 0.0529  228 THR   C OG1  
4996 C  CG2  . THR   C 224 ? 0.3733 0.4716 0.2334 -0.0915 -0.0117 0.0692  228 THR   C CG2  
4997 N  N    . ILE   C 225 ? 0.2731 0.3945 0.1640 -0.0707 -0.0454 0.0575  229 ILE   C N    
4998 C  CA   . ILE   C 225 ? 0.2607 0.3825 0.1586 -0.0661 -0.0382 0.0552  229 ILE   C CA   
4999 C  C    . ILE   C 225 ? 0.2731 0.3942 0.1522 -0.0542 -0.0299 0.0600  229 ILE   C C    
5000 O  O    . ILE   C 225 ? 0.2722 0.3999 0.1793 -0.0495 -0.0148 0.0390  229 ILE   C O    
5001 C  CB   . ILE   C 225 ? 0.2553 0.3663 0.1659 -0.0678 -0.0402 0.0526  229 ILE   C CB   
5002 C  CG1  . ILE   C 225 ? 0.2571 0.3697 0.1915 -0.0635 -0.0396 0.0418  229 ILE   C CG1  
5003 C  CG2  . ILE   C 225 ? 0.2457 0.3531 0.1852 -0.0686 -0.0403 0.0502  229 ILE   C CG2  
5004 C  CD1  . ILE   C 225 ? 0.2544 0.3683 0.1984 -0.0704 -0.0362 0.0291  229 ILE   C CD1  
5005 N  N    . ARG   C 226 ? 0.2755 0.4154 0.1722 -0.0642 -0.0229 0.0638  230 ARG   C N    
5006 C  CA   . ARG   C 226 ? 0.2952 0.4421 0.1917 -0.0651 -0.0235 0.0784  230 ARG   C CA   
5007 C  C    . ARG   C 226 ? 0.2694 0.4128 0.1884 -0.0584 -0.0433 0.0791  230 ARG   C C    
5008 O  O    . ARG   C 226 ? 0.2753 0.4220 0.2004 -0.0610 -0.0584 0.0856  230 ARG   C O    
5009 C  CB   . ARG   C 226 ? 0.3154 0.4869 0.2354 -0.0796 -0.0390 0.0680  230 ARG   C CB   
5010 C  CG   . ARG   C 226 ? 0.3674 0.5296 0.2522 -0.0695 -0.0429 0.0722  230 ARG   C CG   
5011 C  CD   . ARG   C 226 ? 0.4166 0.5716 0.3167 -0.0814 -0.0643 0.0596  230 ARG   C CD   
5012 N  N    . PRO   C 227 ? 0.2725 0.3844 0.1892 -0.0614 -0.0389 0.0791  231 PRO   C N    
5013 C  CA   . PRO   C 227 ? 0.2589 0.3680 0.1734 -0.0605 -0.0500 0.0670  231 PRO   C CA   
5014 C  C    . PRO   C 227 ? 0.2458 0.3603 0.1693 -0.0669 -0.0531 0.0430  231 PRO   C C    
5015 O  O    . PRO   C 227 ? 0.2737 0.3845 0.1766 -0.0898 -0.0606 0.0371  231 PRO   C O    
5016 C  CB   . PRO   C 227 ? 0.2808 0.3881 0.2120 -0.0551 -0.0362 0.0613  231 PRO   C CB   
5017 C  CG   . PRO   C 227 ? 0.2960 0.4101 0.2383 -0.0264 -0.0311 0.0770  231 PRO   C CG   
5018 C  CD   . PRO   C 227 ? 0.2905 0.4041 0.2155 -0.0391 -0.0349 0.0805  231 PRO   C CD   
5019 N  N    . MET   C 228 ? 0.2519 0.3048 0.1560 -0.0748 -0.0467 0.0225  232 MET   C N    
5020 C  CA   . MET   C 228 ? 0.2556 0.2989 0.1774 -0.0772 -0.0339 0.0035  232 MET   C CA   
5021 C  C    . MET   C 228 ? 0.2633 0.3223 0.1956 -0.0704 -0.0567 0.0117  232 MET   C C    
5022 O  O    . MET   C 228 ? 0.2955 0.3476 0.2487 -0.0926 -0.0733 -0.0046 232 MET   C O    
5023 C  CB   . MET   C 228 ? 0.2361 0.2607 0.1705 -0.0789 -0.0178 -0.0052 232 MET   C CB   
5024 C  CG   . MET   C 228 ? 0.2432 0.2528 0.1867 -0.0896 -0.0094 -0.0170 232 MET   C CG   
5025 S  SD   . MET   C 228 ? 0.2769 0.2269 0.1807 -0.0766 0.0115  -0.0151 232 MET   C SD   
5026 C  CE   . MET   C 228 ? 0.2531 0.2117 0.1652 -0.0744 -0.0130 -0.0056 232 MET   C CE   
5027 N  N    . TYR   C 229 ? 0.2457 0.3257 0.2217 -0.0498 -0.0635 0.0323  233 TYR   C N    
5028 C  CA   . TYR   C 229 ? 0.2482 0.3401 0.2443 -0.0242 -0.0676 0.0510  233 TYR   C CA   
5029 C  C    . TYR   C 229 ? 0.2802 0.3574 0.3250 -0.0135 -0.0650 0.0526  233 TYR   C C    
5030 O  O    . TYR   C 229 ? 0.2782 0.3631 0.3539 -0.0188 -0.0558 0.0773  233 TYR   C O    
5031 C  CB   . TYR   C 229 ? 0.2151 0.3184 0.2304 -0.0118 -0.0735 0.0462  233 TYR   C CB   
5032 C  CG   . TYR   C 229 ? 0.2263 0.2827 0.2147 -0.0024 -0.0586 0.0322  233 TYR   C CG   
5033 C  CD1  . TYR   C 229 ? 0.2387 0.2853 0.2339 0.0334  -0.0589 0.0355  233 TYR   C CD1  
5034 C  CD2  . TYR   C 229 ? 0.2178 0.2584 0.2052 -0.0028 -0.0479 0.0272  233 TYR   C CD2  
5035 C  CE1  . TYR   C 229 ? 0.2529 0.2719 0.2332 0.0414  -0.0581 0.0146  233 TYR   C CE1  
5036 C  CE2  . TYR   C 229 ? 0.2192 0.2555 0.2047 0.0138  -0.0528 0.0216  233 TYR   C CE2  
5037 C  CZ   . TYR   C 229 ? 0.2402 0.2649 0.2110 0.0312  -0.0639 0.0151  233 TYR   C CZ   
5038 O  OH   . TYR   C 229 ? 0.2920 0.2637 0.1989 0.0448  -0.0586 -0.0115 233 TYR   C OH   
5039 N  N    . GLY   C 230 ? 0.2947 0.4122 0.4134 -0.0027 -0.0688 0.0591  234 GLY   C N    
5040 C  CA   . GLY   C 230 ? 0.3890 0.4331 0.4932 0.0125  -0.0716 0.0427  234 GLY   C CA   
5041 C  C    . GLY   C 230 ? 0.4585 0.4934 0.5520 0.0381  -0.0587 0.0247  234 GLY   C C    
5042 O  O    . GLY   C 230 ? 0.5075 0.5114 0.5344 0.0579  -0.1257 0.0365  234 GLY   C O    
5043 N  N    . VAL   C 231 ? 0.5347 0.5340 0.6729 0.0661  -0.0650 0.0159  235 VAL   C N    
5044 C  CA   . VAL   C 231 ? 0.5489 0.5682 0.6939 0.0754  -0.0444 -0.0028 235 VAL   C CA   
5045 C  C    . VAL   C 231 ? 0.5742 0.5906 0.7293 0.0508  -0.0447 -0.0073 235 VAL   C C    
5046 O  O    . VAL   C 231 ? 0.6551 0.6375 0.7547 0.0386  -0.0103 -0.0176 235 VAL   C O    
5047 C  CB   . VAL   C 231 ? 0.5782 0.5897 0.7313 0.0706  -0.0693 -0.0033 235 VAL   C CB   
5048 C  C4   . A1B7T D .   ? 0.1819 0.1286 0.1507 -0.0180 -0.0216 -0.0148 301 A1B7T A C4   
5049 C  C5   . A1B7T D .   ? 0.1713 0.1308 0.1620 -0.0127 -0.0265 -0.0234 301 A1B7T A C5   
5050 C  C6   . A1B7T D .   ? 0.1736 0.1402 0.1681 -0.0134 -0.0250 -0.0136 301 A1B7T A C6   
5051 C  C7   . A1B7T D .   ? 0.1787 0.1384 0.1661 -0.0105 -0.0288 -0.0151 301 A1B7T A C7   
5052 C  C8   . A1B7T D .   ? 0.1779 0.1598 0.1846 -0.0145 -0.0232 -0.0137 301 A1B7T A C8   
5053 C  C13  . A1B7T D .   ? 0.2048 0.1502 0.2669 -0.0257 -0.0760 -0.0021 301 A1B7T A C13  
5054 C  C15  . A1B7T D .   ? 0.1885 0.1657 0.2673 -0.0149 -0.0769 0.0030  301 A1B7T A C15  
5055 C  C17  . A1B7T D .   ? 0.1773 0.1448 0.2269 -0.0207 -0.0602 -0.0039 301 A1B7T A C17  
5056 C  C20  . A1B7T D .   ? 0.2236 0.2061 0.2709 -0.0457 -0.0134 -0.0130 301 A1B7T A C20  
5057 C  C21  . A1B7T D .   ? 0.2294 0.2191 0.2872 -0.0524 -0.0091 -0.0064 301 A1B7T A C21  
5058 C  C22  . A1B7T D .   ? 0.2118 0.2061 0.2684 -0.0491 -0.0046 -0.0172 301 A1B7T A C22  
5059 C  C24  . A1B7T D .   ? 0.2128 0.2074 0.2464 -0.0383 -0.0080 -0.0088 301 A1B7T A C24  
5060 F  F1   . A1B7T D .   ? 0.1917 0.1578 0.1782 0.0038  -0.0204 -0.0390 301 A1B7T A F1   
5061 C  C2   . A1B7T D .   ? 0.1800 0.1333 0.1539 -0.0040 -0.0246 -0.0204 301 A1B7T A C2   
5062 C  C3   . A1B7T D .   ? 0.1751 0.1365 0.1505 -0.0073 -0.0189 -0.0106 301 A1B7T A C3   
5063 O  O9   . A1B7T D .   ? 0.1883 0.1953 0.1982 -0.0246 -0.0170 -0.0227 301 A1B7T A O9   
5064 N  N10  . A1B7T D .   ? 0.1843 0.1560 0.2062 -0.0162 -0.0319 -0.0105 301 A1B7T A N10  
5065 C  C11  . A1B7T D .   ? 0.1869 0.1360 0.2114 -0.0210 -0.0461 -0.0179 301 A1B7T A C11  
5066 C  C12  . A1B7T D .   ? 0.1859 0.1501 0.2300 -0.0215 -0.0567 -0.0025 301 A1B7T A C12  
5067 C  C14  . A1B7T D .   ? 0.1950 0.1672 0.2749 -0.0233 -0.0858 -0.0002 301 A1B7T A C14  
5068 N  N16  . A1B7T D .   ? 0.1791 0.1717 0.2265 -0.0104 -0.0622 -0.0011 301 A1B7T A N16  
5069 C  C18  . A1B7T D .   ? 0.2044 0.1828 0.2256 -0.0214 -0.0235 -0.0115 301 A1B7T A C18  
5070 C  C19  . A1B7T D .   ? 0.2182 0.2049 0.2572 -0.0334 -0.0117 -0.0131 301 A1B7T A C19  
5071 C  C23  . A1B7T D .   ? 0.2278 0.2162 0.2572 -0.0350 -0.0072 -0.0132 301 A1B7T A C23  
5072 CL CL25 . A1B7T D .   ? 0.2466 0.1996 0.2680 -0.0233 -0.0218 0.0013  301 A1B7T A CL25 
5073 CL CL26 . A1B7T D .   ? 0.2676 0.2457 0.2706 -0.0380 -0.0168 -0.0113 301 A1B7T A CL26 
5074 F  F27  . A1B7T D .   ? 0.2066 0.1344 0.1771 -0.0310 -0.0127 -0.0134 301 A1B7T A F27  
5075 MG MG   . MG    E .   ? 0.1831 0.1588 0.1616 -0.0156 -0.0174 0.0111  302 MG    A MG   
5076 C  C1   . EDO   F .   ? 0.3406 0.3285 0.3440 -0.0660 -0.1318 0.0926  303 EDO   A C1   
5077 O  O1   . EDO   F .   ? 0.3364 0.3094 0.3316 -0.0434 -0.1197 0.0626  303 EDO   A O1   
5078 C  C2   . EDO   F .   ? 0.3922 0.3619 0.3692 -0.0542 -0.1070 0.0872  303 EDO   A C2   
5079 O  O2   . EDO   F .   ? 0.4136 0.4313 0.4045 -0.0449 -0.1039 0.0929  303 EDO   A O2   
5080 X  UNK  . UNX   G .   ? 0.3787 0.2461 0.2075 -0.1338 0.0182  -0.0932 304 UNX   A UNK  
5081 X  UNK  . UNX   H .   ? 0.1048 0.2015 0.1900 -0.0425 0.0122  -0.1847 305 UNX   A UNK  
5082 C  C4   . A1B7T I .   ? 0.1510 0.1785 0.1417 -0.0300 -0.0152 0.0116  301 A1B7T B C4   
5083 C  C5   . A1B7T I .   ? 0.1495 0.1698 0.1532 -0.0308 -0.0206 0.0189  301 A1B7T B C5   
5084 C  C6   . A1B7T I .   ? 0.1479 0.1721 0.1538 -0.0237 -0.0218 0.0175  301 A1B7T B C6   
5085 C  C7   . A1B7T I .   ? 0.1486 0.1750 0.1449 -0.0231 -0.0247 0.0117  301 A1B7T B C7   
5086 C  C8   . A1B7T I .   ? 0.1590 0.1814 0.1830 -0.0157 -0.0309 0.0117  301 A1B7T B C8   
5087 C  C13  . A1B7T I .   ? 0.1994 0.2148 0.2401 -0.0186 -0.0691 0.0529  301 A1B7T B C13  
5088 C  C15  . A1B7T I .   ? 0.2109 0.2102 0.2441 -0.0212 -0.0752 0.0599  301 A1B7T B C15  
5089 C  C17  . A1B7T I .   ? 0.1866 0.2010 0.2060 -0.0084 -0.0522 0.0397  301 A1B7T B C17  
5090 C  C20  . A1B7T I .   ? 0.1740 0.2680 0.2834 -0.0032 -0.0382 0.0375  301 A1B7T B C20  
5091 C  C21  . A1B7T I .   ? 0.1848 0.2783 0.3174 -0.0129 -0.0298 0.0428  301 A1B7T B C21  
5092 C  C22  . A1B7T I .   ? 0.1669 0.2810 0.2973 -0.0135 -0.0229 0.0351  301 A1B7T B C22  
5093 C  C24  . A1B7T I .   ? 0.1708 0.2380 0.2542 -0.0105 -0.0270 0.0233  301 A1B7T B C24  
5094 F  F1   . A1B7T I .   ? 0.1947 0.1782 0.1529 -0.0278 -0.0308 0.0069  301 A1B7T B F1   
5095 C  C2   . A1B7T I .   ? 0.1605 0.1751 0.1414 -0.0260 -0.0248 0.0102  301 A1B7T B C2   
5096 C  C3   . A1B7T I .   ? 0.1535 0.1746 0.1408 -0.0262 -0.0169 0.0139  301 A1B7T B C3   
5097 O  O9   . A1B7T I .   ? 0.1738 0.2102 0.2007 -0.0025 -0.0412 -0.0036 301 A1B7T B O9   
5098 N  N10  . A1B7T I .   ? 0.1599 0.1878 0.2065 -0.0143 -0.0364 0.0222  301 A1B7T B N10  
5099 C  C11  . A1B7T I .   ? 0.1625 0.1871 0.2040 -0.0212 -0.0522 0.0174  301 A1B7T B C11  
5100 C  C12  . A1B7T I .   ? 0.1874 0.2029 0.2046 -0.0129 -0.0550 0.0392  301 A1B7T B C12  
5101 C  C14  . A1B7T I .   ? 0.2038 0.2174 0.2456 -0.0162 -0.0757 0.0676  301 A1B7T B C14  
5102 N  N16  . A1B7T I .   ? 0.1789 0.2082 0.2259 -0.0119 -0.0571 0.0458  301 A1B7T B N16  
5103 C  C18  . A1B7T I .   ? 0.1712 0.1959 0.2329 -0.0110 -0.0313 0.0210  301 A1B7T B C18  
5104 C  C19  . A1B7T I .   ? 0.1684 0.2213 0.2549 -0.0057 -0.0296 0.0249  301 A1B7T B C19  
5105 C  C23  . A1B7T I .   ? 0.1732 0.2594 0.2670 -0.0161 -0.0251 0.0220  301 A1B7T B C23  
5106 CL CL25 . A1B7T I .   ? 0.2086 0.2592 0.2553 -0.0218 -0.0159 0.0390  301 A1B7T B CL25 
5107 CL CL26 . A1B7T I .   ? 0.2177 0.2882 0.2345 -0.0118 -0.0219 0.0103  301 A1B7T B CL26 
5108 F  F27  . A1B7T I .   ? 0.1596 0.2149 0.1728 -0.0328 -0.0115 0.0086  301 A1B7T B F27  
5109 MG MG   . MG    J .   ? 0.1654 0.2007 0.1515 -0.0167 0.0027  0.0323  302 MG    B MG   
5110 C  C1   . EDO   K .   ? 0.4117 0.3998 0.4774 -0.0099 -0.0628 0.0123  303 EDO   B C1   
5111 O  O1   . EDO   K .   ? 0.4630 0.4006 0.5105 0.0152  -0.0659 0.0073  303 EDO   B O1   
5112 C  C2   . EDO   K .   ? 0.4280 0.4138 0.4857 -0.0057 -0.0493 0.0123  303 EDO   B C2   
5113 O  O2   . EDO   K .   ? 0.4112 0.4551 0.4634 -0.0103 -0.0460 0.0077  303 EDO   B O2   
5114 X  UNK  . UNX   L .   ? 0.4123 0.3238 0.2640 0.1150  0.1870  0.0339  304 UNX   B UNK  
5115 X  UNK  . UNX   M .   ? 0.1565 0.1215 0.0847 -0.0506 -0.1076 0.0475  305 UNX   B UNK  
5116 C  C4   . A1B7T N .   ? 0.1999 0.1597 0.1641 -0.0472 0.0157  -0.0394 301 A1B7T C C4   
5117 C  C5   . A1B7T N .   ? 0.1922 0.1587 0.1660 -0.0385 0.0176  -0.0403 301 A1B7T C C5   
5118 C  C6   . A1B7T N .   ? 0.1883 0.1576 0.1789 -0.0365 0.0189  -0.0422 301 A1B7T C C6   
5119 C  C7   . A1B7T N .   ? 0.1864 0.1763 0.1821 -0.0493 0.0196  -0.0406 301 A1B7T C C7   
5120 C  C8   . A1B7T N .   ? 0.2192 0.1668 0.2116 -0.0219 0.0184  -0.0361 301 A1B7T C C8   
5121 C  C13  . A1B7T N .   ? 0.2173 0.1640 0.2667 -0.0311 0.0276  -0.0565 301 A1B7T C C13  
5122 C  C15  . A1B7T N .   ? 0.2037 0.1678 0.2723 -0.0279 0.0430  -0.0677 301 A1B7T C C15  
5123 C  C17  . A1B7T N .   ? 0.2050 0.1556 0.2384 -0.0308 0.0277  -0.0494 301 A1B7T C C17  
5124 C  C20  . A1B7T N .   ? 0.2648 0.1952 0.2954 -0.0273 0.0253  -0.0291 301 A1B7T C C20  
5125 C  C21  . A1B7T N .   ? 0.2752 0.1967 0.2985 -0.0274 0.0254  -0.0199 301 A1B7T C C21  
5126 C  C22  . A1B7T N .   ? 0.2664 0.1959 0.2992 -0.0396 0.0170  -0.0164 301 A1B7T C C22  
5127 C  C24  . A1B7T N .   ? 0.2632 0.1972 0.2722 -0.0305 0.0262  -0.0189 301 A1B7T C C24  
5128 F  F1   . A1B7T N .   ? 0.1944 0.2248 0.1766 -0.0615 -0.0049 -0.0445 301 A1B7T C F1   
5129 C  C2   . A1B7T N .   ? 0.1747 0.1807 0.1690 -0.0514 0.0136  -0.0425 301 A1B7T C C2   
5130 C  C3   . A1B7T N .   ? 0.1913 0.1699 0.1643 -0.0463 0.0157  -0.0341 301 A1B7T C C3   
5131 O  O9   . A1B7T N .   ? 0.2501 0.1826 0.2402 -0.0242 0.0000  -0.0373 301 A1B7T C O9   
5132 N  N10  . A1B7T N .   ? 0.2152 0.1614 0.2161 -0.0273 0.0172  -0.0415 301 A1B7T C N10  
5133 C  C11  . A1B7T N .   ? 0.2045 0.1526 0.2191 -0.0330 0.0154  -0.0464 301 A1B7T C C11  
5134 C  C12  . A1B7T N .   ? 0.2112 0.1605 0.2279 -0.0318 0.0248  -0.0538 301 A1B7T C C12  
5135 C  C14  . A1B7T N .   ? 0.2153 0.1624 0.2698 -0.0212 0.0389  -0.0729 301 A1B7T C C14  
5136 N  N16  . A1B7T N .   ? 0.2079 0.1546 0.2440 -0.0260 0.0323  -0.0530 301 A1B7T C N16  
5137 C  C18  . A1B7T N .   ? 0.2261 0.1789 0.2453 -0.0223 0.0249  -0.0280 301 A1B7T C C18  
5138 C  C19  . A1B7T N .   ? 0.2544 0.1923 0.2736 -0.0280 0.0180  -0.0296 301 A1B7T C C19  
5139 C  C23  . A1B7T N .   ? 0.2624 0.2143 0.2740 -0.0381 0.0200  -0.0147 301 A1B7T C C23  
5140 CL CL25 . A1B7T N .   ? 0.2573 0.2344 0.2947 -0.0326 0.0330  -0.0225 301 A1B7T C CL25 
5141 CL CL26 . A1B7T N .   ? 0.2907 0.2466 0.2735 -0.0443 0.0178  -0.0092 301 A1B7T C CL26 
5142 F  F27  . A1B7T N .   ? 0.2432 0.1706 0.1738 -0.0692 -0.0018 -0.0274 301 A1B7T C F27  
5143 MG MG   . MG    O .   ? 0.1977 0.1632 0.1563 -0.0372 0.0241  -0.0205 302 MG    C MG   
5144 C  C1   . EDO   P .   ? 0.3613 0.3086 0.4406 -0.0098 0.1757  -0.0510 303 EDO   C C1   
5145 O  O1   . EDO   P .   ? 0.3613 0.3206 0.4303 -0.0169 0.1333  -0.0621 303 EDO   C O1   
5146 C  C2   . EDO   P .   ? 0.3965 0.3299 0.4452 -0.0156 0.1672  -0.0301 303 EDO   C C2   
5147 O  O2   . EDO   P .   ? 0.3838 0.3511 0.4257 0.0027  0.1871  -0.0227 303 EDO   C O2   
5148 C  C1   . EDO   Q .   ? 0.4293 0.3198 0.3857 -0.0424 0.0731  0.0163  304 EDO   C C1   
5149 O  O1   . EDO   Q .   ? 0.3609 0.2110 0.3461 -0.0552 0.0834  0.0153  304 EDO   C O1   
5150 C  C2   . EDO   Q .   ? 0.4473 0.3449 0.4010 -0.0364 0.0820  0.0203  304 EDO   C C2   
5151 O  O2   . EDO   Q .   ? 0.4867 0.2822 0.3987 -0.0299 0.0749  0.0390  304 EDO   C O2   
5152 X  UNK  . UNX   R .   ? 0.3829 0.0727 0.2413 0.0479  -0.2714 -0.0832 305 UNX   C UNK  
5153 X  UNK  . UNX   S .   ? 0.3237 0.1170 1.0656 -0.1622 0.3336  -0.3108 306 UNX   C UNK  
5154 O  O    . HOH   T .   ? 0.3715 0.4402 0.5324 -0.0619 0.0370  -0.1454 401 HOH   A O    
5155 O  O    . HOH   T .   ? 0.6542 0.3339 0.3928 0.1136  0.0613  -0.0220 402 HOH   A O    
5156 O  O    . HOH   T .   ? 0.7037 0.6664 0.6953 0.0909  -0.0635 -0.2981 403 HOH   A O    
5157 O  O    . HOH   T .   ? 0.3176 0.6389 0.7253 0.1212  -0.0356 0.0437  404 HOH   A O    
5158 O  O    . HOH   T .   ? 0.5855 0.4912 0.3271 0.0106  -0.0399 0.0345  405 HOH   A O    
5159 O  O    . HOH   T .   ? 1.0903 0.3646 0.2649 0.0335  -0.0873 -0.1145 406 HOH   A O    
5160 O  O    . HOH   T .   ? 0.2164 0.1631 0.1883 0.0100  0.0379  -0.0056 407 HOH   A O    
5161 O  O    . HOH   T .   ? 0.3917 0.2320 0.2695 -0.0074 -0.0906 -0.0060 408 HOH   A O    
5162 O  O    . HOH   T .   ? 0.2500 0.2579 0.4699 0.0055  -0.0541 -0.0815 409 HOH   A O    
5163 O  O    . HOH   T .   ? 0.2708 0.3476 0.5558 -0.0164 -0.0468 0.0852  410 HOH   A O    
5164 O  O    . HOH   T .   ? 0.2146 0.1491 0.1524 -0.0133 -0.0440 -0.0027 411 HOH   A O    
5165 O  O    . HOH   T .   ? 0.3558 0.4961 0.4165 0.0364  -0.0049 0.0177  412 HOH   A O    
5166 O  O    . HOH   T .   ? 0.2379 0.1967 0.2428 -0.0412 0.0229  -0.0035 413 HOH   A O    
5167 O  O    . HOH   T .   ? 0.3837 0.4583 0.8166 0.0354  -0.0294 0.0826  414 HOH   A O    
5168 O  O    A HOH   T .   ? 0.2681 0.4166 0.2415 0.0309  0.0186  -0.0734 415 HOH   A O    
5169 O  O    B HOH   T .   ? 0.3672 0.5455 0.3686 0.0804  0.1269  -0.2080 415 HOH   A O    
5170 O  O    . HOH   T .   ? 0.3893 0.6088 0.7061 -0.0470 0.1379  -0.0573 416 HOH   A O    
5171 O  O    . HOH   T .   ? 0.5398 0.2301 0.2124 -0.0315 0.1263  -0.0161 417 HOH   A O    
5172 O  O    . HOH   T .   ? 0.8339 0.5276 0.5283 -0.0965 0.2392  -0.1116 418 HOH   A O    
5173 O  O    . HOH   T .   ? 0.4230 0.4336 0.5722 0.1058  -0.0178 -0.1524 419 HOH   A O    
5174 O  O    . HOH   T .   ? 0.2825 0.2120 0.3092 0.0120  -0.0409 0.0257  420 HOH   A O    
5175 O  O    . HOH   T .   ? 0.5132 0.3864 0.5760 -0.0554 0.0784  0.1738  421 HOH   A O    
5176 O  O    . HOH   T .   ? 0.2169 0.1884 0.1493 -0.0043 -0.0295 0.0102  422 HOH   A O    
5177 O  O    . HOH   T .   ? 0.3980 0.4525 0.5937 0.0022  -0.0332 -0.0772 423 HOH   A O    
5178 O  O    . HOH   T .   ? 0.4008 0.2036 0.2270 -0.0071 0.0302  -0.0011 424 HOH   A O    
5179 O  O    . HOH   T .   ? 0.3344 0.2943 0.3435 -0.0606 -0.0132 0.0368  425 HOH   A O    
5180 O  O    . HOH   T .   ? 0.3889 0.2690 0.2178 -0.0281 -0.0023 0.0049  426 HOH   A O    
5181 O  O    . HOH   T .   ? 0.4265 0.2080 0.2767 0.0385  0.0674  -0.0259 427 HOH   A O    
5182 O  O    . HOH   T .   ? 0.2307 0.2542 0.2594 0.0249  0.0247  0.0286  428 HOH   A O    
5183 O  O    . HOH   T .   ? 0.6921 0.3466 0.5282 -0.1497 0.0146  -0.0908 429 HOH   A O    
5184 O  O    . HOH   T .   ? 0.5247 0.3116 0.3999 0.0496  0.0906  0.0379  430 HOH   A O    
5185 O  O    . HOH   T .   ? 0.3382 0.3005 0.4590 -0.0372 0.0085  -0.0498 431 HOH   A O    
5186 O  O    . HOH   T .   ? 0.4862 0.6473 0.4592 0.0587  0.0423  0.0161  432 HOH   A O    
5187 O  O    . HOH   T .   ? 0.3538 0.3495 0.5785 0.0016  0.0396  0.0567  433 HOH   A O    
5188 O  O    . HOH   T .   ? 0.3426 0.3627 0.3450 -0.0291 0.0460  0.0100  434 HOH   A O    
5189 O  O    . HOH   T .   ? 0.5403 0.5544 0.5436 -0.0068 -0.1210 -0.0455 435 HOH   A O    
5190 O  O    A HOH   T .   ? 0.4007 0.2189 0.1951 -0.1740 0.0205  0.0410  436 HOH   A O    
5191 O  O    B HOH   T .   ? 0.3642 0.4369 0.2914 -0.2485 -0.0636 0.1262  436 HOH   A O    
5192 O  O    . HOH   T .   ? 0.3274 0.2556 0.3419 -0.0450 0.0037  0.0198  437 HOH   A O    
5193 O  O    . HOH   T .   ? 0.3049 0.7822 0.8066 0.1740  -0.1768 -0.3216 438 HOH   A O    
5194 O  O    . HOH   T .   ? 0.6413 0.4847 0.2827 -0.1581 -0.0051 0.0881  439 HOH   A O    
5195 O  O    . HOH   T .   ? 0.3629 0.3827 0.6133 -0.0828 -0.0402 0.1664  440 HOH   A O    
5196 O  O    . HOH   T .   ? 0.3719 0.5311 0.6790 0.0068  0.0516  -0.1294 441 HOH   A O    
5197 O  O    . HOH   T .   ? 0.3762 0.4024 0.4961 -0.0763 -0.0145 0.0836  442 HOH   A O    
5198 O  O    . HOH   T .   ? 0.6147 0.4320 0.3887 -0.0819 0.0012  -0.0009 443 HOH   A O    
5199 O  O    . HOH   T .   ? 0.2729 0.5474 0.5360 -0.0823 -0.0310 0.0390  444 HOH   A O    
5200 O  O    . HOH   T .   ? 0.4021 0.4182 0.3155 -0.0800 0.0154  0.0364  445 HOH   A O    
5201 O  O    . HOH   T .   ? 0.5402 0.5924 0.7167 0.0814  0.0929  -0.2873 446 HOH   A O    
5202 O  O    . HOH   T .   ? 0.3148 0.2164 0.2136 0.0097  -0.0743 -0.0031 447 HOH   A O    
5203 O  O    . HOH   T .   ? 0.3111 0.4749 0.4252 -0.0189 0.0269  -0.1288 448 HOH   A O    
5204 O  O    . HOH   T .   ? 0.4617 0.6359 0.4951 -0.0754 0.0615  -0.1867 449 HOH   A O    
5205 O  O    . HOH   T .   ? 0.3677 0.2464 0.3821 -0.0101 -0.0038 0.0463  450 HOH   A O    
5206 O  O    . HOH   T .   ? 0.3891 0.3534 0.3157 0.0154  -0.0584 -0.0886 451 HOH   A O    
5207 O  O    . HOH   T .   ? 0.3544 0.6986 0.6986 -0.0496 -0.1675 -0.1481 452 HOH   A O    
5208 O  O    A HOH   T .   ? 0.2503 0.2576 0.2020 -0.0671 0.0076  -0.0054 453 HOH   A O    
5209 O  O    B HOH   T .   ? 0.3263 0.2089 0.3419 -0.0208 -0.0484 -0.0399 453 HOH   A O    
5210 O  O    . HOH   T .   ? 0.3255 0.4182 0.2586 -0.1002 -0.0219 0.0868  454 HOH   A O    
5211 O  O    . HOH   T .   ? 0.2023 0.1555 0.1254 -0.0194 -0.0188 0.0143  455 HOH   A O    
5212 O  O    . HOH   T .   ? 0.7552 0.6052 0.7266 0.2043  0.0262  -0.1321 456 HOH   A O    
5213 O  O    . HOH   T .   ? 0.3681 0.3331 0.3404 -0.1007 -0.0953 0.0607  457 HOH   A O    
5214 O  O    . HOH   T .   ? 0.2461 0.3603 0.3126 0.0690  -0.0015 0.0241  458 HOH   A O    
5215 O  O    . HOH   T .   ? 0.3184 0.3550 0.4328 -0.0711 -0.1154 0.0278  459 HOH   A O    
5216 O  O    . HOH   T .   ? 0.3043 0.2549 0.4997 -0.0311 -0.0014 0.1252  460 HOH   A O    
5217 O  O    . HOH   T .   ? 0.3125 0.2563 0.1642 0.0117  -0.0074 0.0530  461 HOH   A O    
5218 O  O    . HOH   T .   ? 0.1915 0.1168 0.1619 0.0077  -0.0120 -0.0184 462 HOH   A O    
5219 O  O    . HOH   T .   ? 0.4260 0.3618 0.3333 -0.0124 -0.0242 0.0136  463 HOH   A O    
5220 O  O    . HOH   T .   ? 0.5062 0.2185 0.1695 -0.0080 0.0030  -0.0145 464 HOH   A O    
5221 O  O    . HOH   T .   ? 0.3607 0.4757 0.4882 -0.0651 0.0914  -0.0545 465 HOH   A O    
5222 O  O    A HOH   T .   ? 0.5815 0.2227 0.4356 0.0213  0.0050  -0.1144 466 HOH   A O    
5223 O  O    B HOH   T .   ? 0.1919 0.4593 0.3041 -0.0245 -0.0452 0.1454  466 HOH   A O    
5224 O  O    . HOH   T .   ? 0.4906 0.5875 0.4522 -0.0951 0.0870  -0.1230 467 HOH   A O    
5225 O  O    . HOH   T .   ? 0.2227 0.1837 0.1834 -0.0159 0.0199  0.0167  468 HOH   A O    
5226 O  O    . HOH   T .   ? 0.4668 0.3961 0.3976 0.0567  0.0688  -0.0322 469 HOH   A O    
5227 O  O    . HOH   T .   ? 0.6079 0.4622 0.5898 -0.2336 -0.2480 0.1830  470 HOH   A O    
5228 O  O    . HOH   T .   ? 0.3941 0.2911 0.5356 -0.1245 0.0635  -0.1855 471 HOH   A O    
5229 O  O    . HOH   T .   ? 0.2139 0.2065 0.1876 0.0169  -0.0264 -0.0233 472 HOH   A O    
5230 O  O    . HOH   T .   ? 0.4503 0.4424 0.2608 -0.0704 -0.0693 0.0175  473 HOH   A O    
5231 O  O    . HOH   T .   ? 0.3668 0.5265 0.4747 -0.0102 0.0761  0.1636  474 HOH   A O    
5232 O  O    . HOH   T .   ? 0.5984 0.4656 0.4730 0.0678  -0.0671 0.1001  475 HOH   A O    
5233 O  O    . HOH   T .   ? 0.4871 0.5565 0.5711 -0.1030 0.1486  0.0509  476 HOH   A O    
5234 O  O    . HOH   T .   ? 0.2758 0.1668 0.1583 0.0232  0.0474  0.0040  477 HOH   A O    
5235 O  O    . HOH   T .   ? 0.6270 0.3684 0.3820 0.0100  -0.1622 -0.1198 478 HOH   A O    
5236 O  O    . HOH   T .   ? 0.6916 0.4562 0.5025 -0.0234 0.1276  0.0032  479 HOH   A O    
5237 O  O    . HOH   T .   ? 0.3315 0.2688 0.3443 0.0526  0.0222  -0.0722 480 HOH   A O    
5238 O  O    . HOH   T .   ? 0.2033 0.1733 0.2181 0.0131  -0.0469 -0.0360 481 HOH   A O    
5239 O  O    . HOH   T .   ? 0.2196 0.2388 0.2148 -0.0416 0.0162  -0.0434 482 HOH   A O    
5240 O  O    . HOH   T .   ? 0.2371 0.3343 0.2823 0.0122  0.0359  -0.0102 483 HOH   A O    
5241 O  O    . HOH   T .   ? 0.6185 0.3686 0.7629 0.1074  -0.1156 -0.0440 484 HOH   A O    
5242 O  O    . HOH   T .   ? 0.6316 0.3227 0.2900 -0.1087 -0.0088 -0.0444 485 HOH   A O    
5243 O  O    . HOH   T .   ? 0.4864 0.6796 0.4617 -0.0356 0.0390  0.0064  486 HOH   A O    
5244 O  O    . HOH   T .   ? 0.6056 0.6791 0.6796 -0.1679 -0.2132 -0.0952 487 HOH   A O    
5245 O  O    . HOH   T .   ? 0.3451 0.3605 0.4333 -0.1104 -0.0245 0.0639  488 HOH   A O    
5246 O  O    . HOH   T .   ? 0.5001 0.4737 0.4549 -0.1839 0.0133  -0.0806 489 HOH   A O    
5247 O  O    . HOH   T .   ? 0.3475 0.1668 0.3806 -0.0346 0.1158  -0.0439 490 HOH   A O    
5248 O  O    . HOH   T .   ? 0.4290 0.4208 0.5674 0.0262  0.0031  0.1152  491 HOH   A O    
5249 O  O    . HOH   T .   ? 0.6426 0.5212 0.5325 0.1553  -0.1990 -0.2076 492 HOH   A O    
5250 O  O    . HOH   T .   ? 0.4851 0.6412 0.2980 0.0674  0.0264  -0.0118 493 HOH   A O    
5251 O  O    . HOH   T .   ? 0.1843 0.1564 0.2567 0.0166  -0.0356 -0.0099 494 HOH   A O    
5252 O  O    . HOH   T .   ? 0.5002 0.4880 0.3622 0.0424  0.0546  0.0409  495 HOH   A O    
5253 O  O    . HOH   T .   ? 0.3553 0.6096 0.7327 -0.0919 0.1380  0.0157  496 HOH   A O    
5254 O  O    . HOH   T .   ? 0.4274 0.3790 0.3040 -0.1101 -0.0747 0.0800  497 HOH   A O    
5255 O  O    . HOH   T .   ? 0.2456 0.2045 0.2446 0.0129  -0.0337 0.0119  498 HOH   A O    
5256 O  O    . HOH   T .   ? 0.3830 0.5099 0.4332 -0.2728 0.1240  -0.1831 499 HOH   A O    
5257 O  O    . HOH   T .   ? 0.2484 0.1668 0.1736 -0.0098 0.0078  -0.0101 500 HOH   A O    
5258 O  O    A HOH   T .   ? 0.4105 0.2972 0.5035 -0.0065 -0.0181 0.0145  501 HOH   A O    
5259 O  O    B HOH   T .   ? 0.2781 0.4629 0.3226 0.1066  -0.0813 -0.1077 501 HOH   A O    
5260 O  O    . HOH   T .   ? 0.2989 0.2954 0.5247 0.0230  -0.1690 -0.0075 502 HOH   A O    
5261 O  O    . HOH   T .   ? 0.7519 0.3618 0.4615 -0.0174 -0.2081 -0.1493 503 HOH   A O    
5262 O  O    . HOH   T .   ? 0.2836 0.3932 0.6247 0.0585  -0.1330 0.1111  504 HOH   A O    
5263 O  O    . HOH   T .   ? 0.3635 0.3282 0.3829 -0.0118 -0.0604 0.0845  505 HOH   A O    
5264 O  O    . HOH   T .   ? 0.5711 0.2531 0.1961 -0.0967 0.0733  -0.0650 506 HOH   A O    
5265 O  O    . HOH   T .   ? 0.4032 0.3776 0.5101 -0.0764 0.1186  -0.0608 507 HOH   A O    
5266 O  O    . HOH   T .   ? 0.3472 0.4338 0.3498 0.1072  -0.1520 -0.0272 508 HOH   A O    
5267 O  O    . HOH   T .   ? 0.4234 0.7031 0.3713 0.1381  0.0313  0.0185  509 HOH   A O    
5268 O  O    . HOH   T .   ? 0.3784 0.3394 0.2558 -0.0098 -0.1092 0.0764  510 HOH   A O    
5269 O  O    . HOH   T .   ? 0.3386 0.3872 0.3978 -0.0313 -0.0791 -0.0497 511 HOH   A O    
5270 O  O    . HOH   T .   ? 0.4023 0.3408 0.5593 0.0660  0.1469  0.1083  512 HOH   A O    
5271 O  O    . HOH   T .   ? 0.3960 0.1737 0.2193 -0.0616 -0.0264 -0.0009 513 HOH   A O    
5272 O  O    . HOH   T .   ? 0.3223 0.2322 0.5064 -0.0379 -0.0147 0.0078  514 HOH   A O    
5273 O  O    A HOH   T .   ? 0.3206 0.1978 0.4872 0.0102  0.1469  0.1369  515 HOH   A O    
5274 O  O    B HOH   T .   ? 0.2783 0.7481 0.2356 -0.1128 -0.0045 0.2039  515 HOH   A O    
5275 O  O    . HOH   T .   ? 0.2879 0.2790 0.2670 -0.0191 -0.0563 0.0915  516 HOH   A O    
5276 O  O    . HOH   T .   ? 0.2949 0.2356 0.3232 0.0488  -0.0791 0.0105  517 HOH   A O    
5277 O  O    . HOH   T .   ? 0.4915 0.3294 0.4663 -0.0925 -0.1735 -0.0825 518 HOH   A O    
5278 O  O    . HOH   T .   ? 0.6828 0.4225 0.5996 0.1148  -0.1798 -0.2474 519 HOH   A O    
5279 O  O    . HOH   T .   ? 0.3421 0.3849 0.3388 0.1071  0.0533  0.0151  520 HOH   A O    
5280 O  O    . HOH   T .   ? 0.5469 0.5634 0.6584 -0.1084 -0.0516 0.1343  521 HOH   A O    
5281 O  O    . HOH   T .   ? 0.6351 0.4719 0.6311 -0.1298 0.1238  -0.2588 522 HOH   A O    
5282 O  O    . HOH   T .   ? 0.4604 0.5749 0.7113 -0.2229 -0.2556 0.1427  523 HOH   A O    
5283 O  O    . HOH   T .   ? 0.5183 0.4925 0.5091 0.0868  0.0936  0.0746  524 HOH   A O    
5284 O  O    . HOH   T .   ? 0.7343 0.5554 0.4362 -0.2383 0.0216  -0.1314 525 HOH   A O    
5285 O  O    . HOH   T .   ? 0.3843 0.4601 0.8384 0.0330  -0.1958 0.0548  526 HOH   A O    
5286 O  O    . HOH   T .   ? 0.2417 0.1937 0.2069 -0.0219 -0.0188 0.0146  527 HOH   A O    
5287 O  O    . HOH   T .   ? 0.7349 0.5865 0.4577 0.2367  -0.1834 -0.2064 528 HOH   A O    
5288 O  O    . HOH   T .   ? 0.7041 0.6161 0.8034 0.2037  -0.1907 -0.0643 529 HOH   A O    
5289 O  O    . HOH   T .   ? 0.3712 0.2996 0.5361 -0.0490 -0.0295 -0.0244 530 HOH   A O    
5290 O  O    . HOH   T .   ? 0.6597 0.3992 0.5818 0.1879  0.0537  -0.1721 531 HOH   A O    
5291 O  O    . HOH   T .   ? 0.4072 0.3954 0.3011 0.1145  -0.0460 -0.0257 532 HOH   A O    
5292 O  O    . HOH   T .   ? 0.3696 0.4202 0.6069 0.0586  -0.0251 -0.0381 533 HOH   A O    
5293 O  O    . HOH   T .   ? 0.4894 0.4290 0.3508 0.1485  0.0717  0.0474  534 HOH   A O    
5294 O  O    . HOH   T .   ? 0.3271 0.4951 0.5178 0.0376  0.0271  0.1724  535 HOH   A O    
5295 O  O    A HOH   T .   ? 0.2475 0.1789 0.1810 -0.0392 -0.0248 -0.0203 536 HOH   A O    
5296 O  O    B HOH   T .   ? 0.2831 0.2917 0.2352 -0.0832 -0.0209 -0.0567 536 HOH   A O    
5297 O  O    . HOH   T .   ? 0.4549 0.6818 0.6049 0.0165  0.0395  0.0612  537 HOH   A O    
5298 O  O    . HOH   T .   ? 0.7360 0.7308 0.5240 0.0103  0.0045  -0.2473 538 HOH   A O    
5299 O  O    . HOH   T .   ? 0.7223 0.5473 0.4175 -0.0312 0.1064  0.0096  539 HOH   A O    
5300 O  O    . HOH   T .   ? 0.4956 0.7609 0.3668 -0.0238 -0.0814 -0.1301 540 HOH   A O    
5301 O  O    . HOH   T .   ? 0.5792 0.3621 0.7848 -0.0937 -0.2478 0.0645  541 HOH   A O    
5302 O  O    . HOH   T .   ? 0.4820 0.5809 0.3439 -0.0062 0.0668  0.0754  542 HOH   A O    
5303 O  O    . HOH   T .   ? 0.6822 0.3445 0.3613 0.1248  -0.1789 -0.0914 543 HOH   A O    
5304 O  O    . HOH   T .   ? 0.7613 0.5996 0.3701 0.2217  0.0593  -0.0186 544 HOH   A O    
5305 O  O    . HOH   T .   ? 0.4526 0.6434 0.3495 -0.1488 0.0498  -0.0698 545 HOH   A O    
5306 O  O    . HOH   T .   ? 0.5101 0.4587 0.4502 -0.0097 -0.0561 0.0693  546 HOH   A O    
5307 O  O    . HOH   T .   ? 0.6196 0.5393 0.8703 -0.0414 -0.0546 -0.1895 547 HOH   A O    
5308 O  O    . HOH   T .   ? 0.4301 0.7104 0.5111 0.0176  -0.0660 0.0673  548 HOH   A O    
5309 O  O    . HOH   T .   ? 0.2529 0.4375 0.5719 -0.0264 -0.0249 0.0828  549 HOH   A O    
5310 O  O    . HOH   T .   ? 1.0244 0.5093 0.5508 0.2607  0.2556  0.1086  550 HOH   A O    
5311 O  O    . HOH   T .   ? 0.6392 0.4177 0.6299 -0.2039 -0.2142 0.0134  551 HOH   A O    
5312 O  O    . HOH   T .   ? 0.7053 0.7183 0.3230 -0.1843 0.0941  -0.0892 552 HOH   A O    
5313 O  O    . HOH   T .   ? 0.4106 0.3407 0.2099 0.1214  0.0238  0.0190  553 HOH   A O    
5314 O  O    . HOH   T .   ? 0.7114 0.3832 0.6492 -0.1189 -0.1294 0.1061  554 HOH   A O    
5315 O  O    . HOH   T .   ? 0.7297 0.7860 0.6268 0.2437  -0.0673 -0.1289 555 HOH   A O    
5316 O  O    . HOH   T .   ? 0.5570 0.3320 0.3727 -0.0791 0.0722  -0.0695 556 HOH   A O    
5317 O  O    . HOH   T .   ? 0.3166 0.4608 0.4857 0.0776  -0.0020 -0.0777 557 HOH   A O    
5318 O  O    . HOH   T .   ? 0.6227 0.2785 0.4790 0.0375  0.1421  0.0345  558 HOH   A O    
5319 O  O    . HOH   T .   ? 0.4489 0.3816 0.2611 0.0644  0.0288  0.0608  559 HOH   A O    
5320 O  O    . HOH   T .   ? 0.6474 0.4717 0.6607 -0.1153 0.1946  0.0244  560 HOH   A O    
5321 O  O    . HOH   T .   ? 0.5018 0.6926 0.4746 0.0768  0.0996  0.0393  561 HOH   A O    
5322 O  O    . HOH   T .   ? 0.5109 0.4748 0.6102 0.1884  -0.0271 0.0575  562 HOH   A O    
5323 O  O    . HOH   T .   ? 0.7497 0.5721 0.2452 0.1094  0.0391  -0.0163 563 HOH   A O    
5324 O  O    . HOH   T .   ? 0.5039 0.2753 0.3001 -0.0618 0.0094  0.0489  564 HOH   A O    
5325 O  O    . HOH   T .   ? 0.5026 0.3186 0.3815 -0.0950 0.0214  0.0241  565 HOH   A O    
5326 O  O    . HOH   T .   ? 0.5543 0.4630 0.8139 0.1173  0.0946  -0.1038 566 HOH   A O    
5327 O  O    . HOH   T .   ? 0.4521 0.3020 0.4120 0.0635  -0.0912 -0.1317 567 HOH   A O    
5328 O  O    . HOH   T .   ? 0.7553 0.6238 0.3319 0.0018  0.0073  -0.0245 568 HOH   A O    
5329 O  O    . HOH   T .   ? 0.7783 0.5570 0.4369 -0.2535 -0.0142 0.0466  569 HOH   A O    
5330 O  O    . HOH   T .   ? 0.4952 0.4195 0.8432 -0.0080 0.2062  0.0226  570 HOH   A O    
5331 O  O    . HOH   T .   ? 0.5941 0.6382 0.6513 0.1076  -0.1712 -0.3016 571 HOH   A O    
5332 O  O    . HOH   T .   ? 0.5734 0.5443 0.8648 0.0324  0.1502  -0.0423 572 HOH   A O    
5333 O  O    . HOH   T .   ? 0.4052 0.2492 0.3915 -0.0204 0.0552  0.0434  573 HOH   A O    
5334 O  O    . HOH   T .   ? 0.5846 0.3391 0.3796 0.1347  -0.0231 -0.0066 574 HOH   A O    
5335 O  O    . HOH   T .   ? 0.3888 0.5841 0.6591 0.1269  0.0089  0.1623  575 HOH   A O    
5336 O  O    . HOH   T .   ? 0.6160 0.5449 0.3871 -0.0268 0.1061  -0.1097 576 HOH   A O    
5337 O  O    . HOH   T .   ? 0.4173 0.3146 0.5534 -0.0734 0.0557  0.0298  577 HOH   A O    
5338 O  O    . HOH   T .   ? 0.3558 0.3887 0.3464 0.0294  0.0961  0.0247  578 HOH   A O    
5339 O  O    . HOH   T .   ? 0.6145 0.4623 0.3156 0.1547  0.0690  -0.0158 579 HOH   A O    
5340 O  O    . HOH   T .   ? 0.4915 0.4964 0.4234 0.0670  -0.0419 0.0931  580 HOH   A O    
5341 O  O    . HOH   U .   ? 0.2570 0.5712 0.7089 0.0015  0.0352  0.1338  401 HOH   B O    
5342 O  O    . HOH   U .   ? 0.4420 0.3916 0.4078 -0.0401 0.1873  -0.0623 402 HOH   B O    
5343 O  O    . HOH   U .   ? 0.4185 0.4671 0.7199 0.1068  0.1395  0.2268  403 HOH   B O    
5344 O  O    . HOH   U .   ? 0.7870 0.4518 0.5676 0.1115  -0.0906 -0.0365 404 HOH   B O    
5345 O  O    . HOH   U .   ? 0.1224 0.2170 0.1757 0.0028  0.0052  -0.0457 405 HOH   B O    
5346 O  O    . HOH   U .   ? 0.4968 0.6576 0.4445 -0.1643 0.0588  -0.0941 406 HOH   B O    
5347 O  O    . HOH   U .   ? 0.2531 0.3674 0.4634 0.0303  -0.0803 0.0541  407 HOH   B O    
5348 O  O    . HOH   U .   ? 0.5571 0.4462 0.3977 -0.0035 0.0290  0.0378  408 HOH   B O    
5349 O  O    . HOH   U .   ? 0.2497 0.2569 0.3078 -0.0477 -0.0111 0.0471  409 HOH   B O    
5350 O  O    . HOH   U .   ? 0.2420 0.2006 0.3301 -0.0015 -0.1042 0.0205  410 HOH   B O    
5351 O  O    . HOH   U .   ? 0.7923 0.6913 0.3736 -0.2622 -0.0396 0.2133  411 HOH   B O    
5352 O  O    . HOH   U .   ? 0.3278 0.2044 0.2978 -0.0474 -0.0349 0.0385  412 HOH   B O    
5353 O  O    . HOH   U .   ? 0.6465 0.6043 0.6028 -0.1417 -0.0180 -0.0642 413 HOH   B O    
5354 O  O    . HOH   U .   ? 0.2966 0.4476 0.3393 -0.0359 -0.0077 -0.0564 414 HOH   B O    
5355 O  O    . HOH   U .   ? 0.2979 0.3701 0.2644 -0.0128 0.0550  -0.0322 415 HOH   B O    
5356 O  O    . HOH   U .   ? 0.3888 0.6113 0.5587 0.1314  0.0408  0.0227  416 HOH   B O    
5357 O  O    . HOH   U .   ? 0.1957 0.2204 0.1755 0.0072  -0.0127 0.0305  417 HOH   B O    
5358 O  O    . HOH   U .   ? 0.3690 0.5320 0.4209 0.0202  -0.0111 -0.1243 418 HOH   B O    
5359 O  O    . HOH   U .   ? 0.4309 0.4414 0.4470 0.0385  -0.1130 -0.1603 419 HOH   B O    
5360 O  O    . HOH   U .   ? 0.6677 0.5297 0.4818 0.1708  0.2706  0.0976  420 HOH   B O    
5361 O  O    . HOH   U .   ? 0.2814 0.3953 0.3039 -0.0314 0.0608  -0.0494 421 HOH   B O    
5362 O  O    . HOH   U .   ? 0.3628 0.5090 0.4619 0.0351  0.0475  0.0907  422 HOH   B O    
5363 O  O    . HOH   U .   ? 0.1576 0.3463 0.2396 0.0249  0.0000  0.0025  423 HOH   B O    
5364 O  O    . HOH   U .   ? 0.2790 0.3527 0.2679 -0.0402 -0.0270 -0.0494 424 HOH   B O    
5365 O  O    . HOH   U .   ? 0.6935 0.4987 0.3527 0.2018  -0.1163 -0.1797 425 HOH   B O    
5366 O  O    . HOH   U .   ? 0.4569 0.5053 0.4543 0.0888  0.0195  -0.0359 426 HOH   B O    
5367 O  O    . HOH   U .   ? 0.6821 0.7178 0.2193 -0.2545 -0.0483 -0.0619 427 HOH   B O    
5368 O  O    . HOH   U .   ? 0.2998 0.9175 0.3189 -0.0160 0.0040  -0.0636 428 HOH   B O    
5369 O  O    . HOH   U .   ? 0.4541 0.5871 0.3582 -0.2209 -0.0347 -0.1557 429 HOH   B O    
5370 O  O    . HOH   U .   ? 0.6354 0.5188 0.3666 0.1213  0.0923  0.0563  430 HOH   B O    
5371 O  O    . HOH   U .   ? 0.5810 0.3014 0.4583 0.0305  -0.1222 0.0037  431 HOH   B O    
5372 O  O    . HOH   U .   ? 0.5648 0.5465 0.3716 -0.0031 -0.0459 0.0890  432 HOH   B O    
5373 O  O    A HOH   U .   ? 0.2284 0.2970 0.2053 -0.0435 0.0253  -0.0320 433 HOH   B O    
5374 O  O    B HOH   U .   ? 0.2028 0.3018 0.1578 0.0362  -0.0395 -0.0025 433 HOH   B O    
5375 O  O    . HOH   U .   ? 0.3286 0.3469 0.4929 0.0345  0.0855  -0.0989 434 HOH   B O    
5376 O  O    . HOH   U .   ? 0.2949 0.3337 0.6687 0.0486  0.0194  0.0713  435 HOH   B O    
5377 O  O    . HOH   U .   ? 0.4365 0.4786 0.4077 0.0534  -0.1096 0.0047  436 HOH   B O    
5378 O  O    . HOH   U .   ? 0.2400 0.3201 0.3710 -0.0328 0.0107  0.0904  437 HOH   B O    
5379 O  O    . HOH   U .   ? 0.1769 0.2000 0.1427 -0.0326 -0.0216 0.0087  438 HOH   B O    
5380 O  O    . HOH   U .   ? 0.2912 0.2797 0.2082 -0.0577 -0.0088 0.0535  439 HOH   B O    
5381 O  O    . HOH   U .   ? 0.2671 0.3978 0.5094 0.0652  0.0195  0.0758  440 HOH   B O    
5382 O  O    . HOH   U .   ? 0.2349 0.6675 0.2898 -0.0139 0.0358  0.0092  441 HOH   B O    
5383 O  O    . HOH   U .   ? 0.2961 0.3534 0.1708 -0.0979 0.0105  0.0344  442 HOH   B O    
5384 O  O    . HOH   U .   ? 0.2814 0.4132 0.3384 0.0574  0.0192  0.0258  443 HOH   B O    
5385 O  O    . HOH   U .   ? 0.5694 0.4180 0.6671 0.1246  0.0406  -0.0606 444 HOH   B O    
5386 O  O    . HOH   U .   ? 0.6281 0.5868 0.6221 -0.0434 0.2315  -0.0860 445 HOH   B O    
5387 O  O    . HOH   U .   ? 0.4861 0.4037 0.3981 0.0129  0.0289  0.0649  446 HOH   B O    
5388 O  O    . HOH   U .   ? 0.3754 0.3175 0.4105 -0.0140 -0.0794 0.0467  447 HOH   B O    
5389 O  O    . HOH   U .   ? 0.4588 0.4083 0.8732 0.0755  -0.1299 0.0843  448 HOH   B O    
5390 O  O    . HOH   U .   ? 0.6397 0.5781 0.4665 -0.1309 -0.0696 0.1129  449 HOH   B O    
5391 O  O    . HOH   U .   ? 0.1711 0.2318 0.1083 -0.0293 0.0056  0.0260  450 HOH   B O    
5392 O  O    . HOH   U .   ? 0.4066 0.4949 0.4668 0.0129  0.1166  -0.0184 451 HOH   B O    
5393 O  O    . HOH   U .   ? 0.5696 0.5106 0.3004 -0.0134 0.0111  -0.0765 452 HOH   B O    
5394 O  O    . HOH   U .   ? 0.2010 0.6158 0.3915 0.0782  0.0463  0.0085  453 HOH   B O    
5395 O  O    A HOH   U .   ? 0.2120 0.2206 0.1916 -0.0583 0.0251  -0.0102 454 HOH   B O    
5396 O  O    B HOH   U .   ? 0.3476 0.5178 0.2148 0.1540  0.0010  0.1087  454 HOH   B O    
5397 O  O    . HOH   U .   ? 0.4630 0.3401 0.3601 -0.1953 0.0264  -0.1003 455 HOH   B O    
5398 O  O    . HOH   U .   ? 0.1910 0.1758 0.1574 -0.0545 -0.0165 -0.0013 456 HOH   B O    
5399 O  O    . HOH   U .   ? 0.3078 0.4806 0.2061 -0.1380 0.0087  -0.0328 457 HOH   B O    
5400 O  O    . HOH   U .   ? 0.3635 0.7394 0.6880 -0.1394 -0.1132 0.1516  458 HOH   B O    
5401 O  O    . HOH   U .   ? 0.3833 0.4231 0.8027 -0.0731 -0.1509 -0.0905 459 HOH   B O    
5402 O  O    . HOH   U .   ? 0.3455 0.5004 0.5007 -0.0222 -0.0348 0.1805  460 HOH   B O    
5403 O  O    . HOH   U .   ? 0.3496 0.5499 0.7059 0.0312  -0.0990 0.1224  461 HOH   B O    
5404 O  O    . HOH   U .   ? 0.3732 0.3336 0.3945 0.0411  -0.0955 0.0186  462 HOH   B O    
5405 O  O    . HOH   U .   ? 0.2710 0.2147 0.2981 -0.0180 0.0190  -0.0208 463 HOH   B O    
5406 O  O    . HOH   U .   ? 0.1432 0.1991 0.1424 -0.0120 -0.0094 0.0079  464 HOH   B O    
5407 O  O    . HOH   U .   ? 0.5087 0.6489 0.5802 -0.1143 0.2268  0.0043  465 HOH   B O    
5408 O  O    . HOH   U .   ? 0.4186 0.2541 0.3188 0.0218  0.0322  -0.0139 466 HOH   B O    
5409 O  O    . HOH   U .   ? 0.7143 0.5212 0.4489 0.0664  0.0100  -0.1733 467 HOH   B O    
5410 O  O    . HOH   U .   ? 0.3931 0.7298 0.9722 0.1275  -0.1663 -0.1561 468 HOH   B O    
5411 O  O    . HOH   U .   ? 0.4082 0.4516 0.3993 -0.0704 0.1052  -0.0858 469 HOH   B O    
5412 O  O    . HOH   U .   ? 0.3192 0.3247 0.4658 0.0045  0.1082  0.0925  470 HOH   B O    
5413 O  O    . HOH   U .   ? 0.3347 0.3585 0.4071 -0.0109 -0.0104 0.0930  471 HOH   B O    
5414 O  O    . HOH   U .   ? 0.2159 0.2041 0.1933 -0.0129 -0.0364 0.0186  472 HOH   B O    
5415 O  O    . HOH   U .   ? 0.5688 0.4837 0.4236 0.0100  0.0500  0.0320  473 HOH   B O    
5416 O  O    . HOH   U .   ? 0.2479 0.2754 0.3237 -0.0051 0.0234  0.0137  474 HOH   B O    
5417 O  O    . HOH   U .   ? 0.3077 0.2973 0.3039 0.0611  0.0125  -0.0085 475 HOH   B O    
5418 O  O    A HOH   U .   ? 0.2129 0.2929 0.5607 0.0457  -0.0394 -0.1203 476 HOH   B O    
5419 O  O    B HOH   U .   ? 0.1660 0.2614 0.6090 0.0063  0.0012  -0.0963 476 HOH   B O    
5420 O  O    . HOH   U .   ? 0.6003 0.5710 0.6540 0.0530  -0.2563 0.0387  477 HOH   B O    
5421 O  O    . HOH   U .   ? 0.1780 0.2320 0.2305 0.0050  -0.0514 -0.0269 478 HOH   B O    
5422 O  O    . HOH   U .   ? 0.4684 0.5366 0.6639 0.0821  0.0858  0.2617  479 HOH   B O    
5423 O  O    . HOH   U .   ? 0.3460 0.1906 0.3969 0.0472  0.0763  0.0129  480 HOH   B O    
5424 O  O    . HOH   U .   ? 0.1945 0.1545 0.2240 0.0124  -0.0490 0.0214  481 HOH   B O    
5425 O  O    . HOH   U .   ? 0.3078 0.3516 0.3396 -0.0342 -0.0441 0.0349  482 HOH   B O    
5426 O  O    . HOH   U .   ? 0.5539 0.2880 0.4929 -0.1114 -0.0494 -0.1001 483 HOH   B O    
5427 O  O    . HOH   U .   ? 0.5475 0.6358 0.4099 -0.2498 -0.1353 0.1332  484 HOH   B O    
5428 O  O    . HOH   U .   ? 0.3806 0.6631 0.2925 -0.0187 -0.0544 0.0666  485 HOH   B O    
5429 O  O    . HOH   U .   ? 0.2275 0.3739 0.3092 -0.0416 0.0562  0.0088  486 HOH   B O    
5430 O  O    . HOH   U .   ? 0.3721 0.3404 0.2509 -0.0371 0.0067  0.1156  487 HOH   B O    
5431 O  O    . HOH   U .   ? 0.3541 0.3871 0.4405 0.0077  0.0080  -0.0708 488 HOH   B O    
5432 O  O    A HOH   U .   ? 0.4576 0.2671 0.4546 -0.0636 -0.2020 0.0451  489 HOH   B O    
5433 O  O    B HOH   U .   ? 0.4137 0.6175 0.2990 -0.0951 -0.0249 -0.2359 489 HOH   B O    
5434 O  O    . HOH   U .   ? 0.3087 0.7142 0.7764 -0.2080 0.1902  -0.3354 490 HOH   B O    
5435 O  O    . HOH   U .   ? 0.6988 0.3048 0.4727 0.0962  -0.2117 -0.0666 491 HOH   B O    
5436 O  O    . HOH   U .   ? 0.4329 0.3848 0.5488 -0.0503 0.1260  0.0701  492 HOH   B O    
5437 O  O    . HOH   U .   ? 0.3227 0.5072 0.4080 0.0297  -0.1031 -0.0096 493 HOH   B O    
5438 O  O    . HOH   U .   ? 0.1780 0.1783 0.1668 -0.0472 -0.0072 0.0048  494 HOH   B O    
5439 O  O    . HOH   U .   ? 0.5478 0.5185 0.6941 -0.2352 -0.1043 0.0469  495 HOH   B O    
5440 O  O    . HOH   U .   ? 0.5415 0.5523 0.3323 -0.2233 -0.1119 0.1532  496 HOH   B O    
5441 O  O    . HOH   U .   ? 0.2563 0.2264 0.2491 -0.0481 -0.0311 0.0485  497 HOH   B O    
5442 O  O    . HOH   U .   ? 0.3368 0.4279 0.4474 0.0209  -0.1172 0.0599  498 HOH   B O    
5443 O  O    . HOH   U .   ? 0.1928 0.2019 0.2182 -0.0100 -0.0381 0.0342  499 HOH   B O    
5444 O  O    . HOH   U .   ? 0.1833 0.2728 0.3427 0.0000  -0.0625 0.0000  500 HOH   B O    
5445 O  O    . HOH   U .   ? 0.3784 0.3741 0.6569 -0.0011 0.0087  -0.0600 501 HOH   B O    
5446 O  O    A HOH   U .   ? 0.1623 0.2917 0.2851 -0.0594 -0.0744 0.0964  502 HOH   B O    
5447 O  O    B HOH   U .   ? 0.1778 0.3547 0.3713 0.0128  0.0094  -0.0147 502 HOH   B O    
5448 O  O    . HOH   U .   ? 0.3036 0.5222 0.2339 -0.0987 0.0343  -0.1380 503 HOH   B O    
5449 O  O    . HOH   U .   ? 0.5985 0.2811 0.3282 0.0250  -0.1119 0.1137  504 HOH   B O    
5450 O  O    . HOH   U .   ? 0.7382 0.5725 0.5484 -0.1656 0.0259  -0.0364 505 HOH   B O    
5451 O  O    . HOH   U .   ? 0.3160 0.3272 0.4686 -0.0240 -0.0266 0.0160  506 HOH   B O    
5452 O  O    . HOH   U .   ? 0.3130 0.3343 0.2935 0.0251  0.0669  0.0969  507 HOH   B O    
5453 O  O    . HOH   U .   ? 0.2565 0.6729 0.5441 0.1138  -0.0918 -0.1288 508 HOH   B O    
5454 O  O    . HOH   U .   ? 0.4407 0.5244 0.4535 -0.0519 0.1452  0.0096  509 HOH   B O    
5455 O  O    . HOH   U .   ? 0.3702 0.2923 0.2916 -0.0921 -0.0356 0.1050  510 HOH   B O    
5456 O  O    . HOH   U .   ? 0.2325 0.3601 0.1803 -0.1193 -0.0185 0.0287  511 HOH   B O    
5457 O  O    . HOH   U .   ? 0.5867 0.4990 0.3919 0.0705  -0.0745 -0.1111 512 HOH   B O    
5458 O  O    . HOH   U .   ? 0.4525 0.2045 0.4637 0.0370  -0.0147 0.0690  513 HOH   B O    
5459 O  O    . HOH   U .   ? 0.3207 0.4173 0.4209 -0.0193 -0.0051 0.0650  514 HOH   B O    
5460 O  O    . HOH   U .   ? 0.5746 0.7058 0.3444 0.0471  0.0291  -0.0839 515 HOH   B O    
5461 O  O    . HOH   U .   ? 0.6601 0.5324 0.8189 0.1276  0.1660  -0.1831 516 HOH   B O    
5462 O  O    . HOH   U .   ? 0.3333 0.4553 0.3402 0.0980  0.0918  0.0963  517 HOH   B O    
5463 O  O    . HOH   U .   ? 0.4031 0.2850 0.3830 -0.0576 -0.0907 0.1204  518 HOH   B O    
5464 O  O    . HOH   U .   ? 0.7982 0.3059 0.4145 0.0068  -0.1347 0.0303  519 HOH   B O    
5465 O  O    . HOH   U .   ? 0.2918 0.3282 0.5884 -0.0135 0.0913  0.0350  520 HOH   B O    
5466 O  O    . HOH   U .   ? 0.3488 0.3595 0.3849 -0.0633 0.0188  -0.0089 521 HOH   B O    
5467 O  O    A HOH   U .   ? 0.2034 0.3180 0.1877 -0.0209 0.0496  0.0042  522 HOH   B O    
5468 O  O    B HOH   U .   ? 0.2270 0.3048 0.1700 -0.0192 0.0379  0.0265  522 HOH   B O    
5469 O  O    . HOH   U .   ? 0.3136 0.4078 0.4160 0.0066  0.0580  0.1286  523 HOH   B O    
5470 O  O    . HOH   U .   ? 0.3780 0.5928 0.3585 0.1660  -0.0081 -0.0851 524 HOH   B O    
5471 O  O    . HOH   U .   ? 0.2216 0.3226 0.2734 -0.0480 -0.0347 -0.0187 525 HOH   B O    
5472 O  O    . HOH   U .   ? 0.6933 0.9519 0.5923 -0.1690 -0.1461 -0.1504 526 HOH   B O    
5473 O  O    . HOH   U .   ? 0.4347 0.5280 0.7517 -0.0561 0.0033  0.1422  527 HOH   B O    
5474 O  O    . HOH   U .   ? 0.2083 0.2481 0.1966 -0.0131 0.0009  0.0169  528 HOH   B O    
5475 O  O    . HOH   U .   ? 0.3015 0.2762 0.3002 -0.0288 -0.0932 0.0876  529 HOH   B O    
5476 O  O    . HOH   U .   ? 0.5078 0.4170 0.5159 0.1402  0.0630  0.0531  530 HOH   B O    
5477 O  O    . HOH   U .   ? 0.5013 0.2853 0.3939 -0.0305 -0.0757 0.0801  531 HOH   B O    
5478 O  O    . HOH   U .   ? 0.3086 0.5117 0.6510 -0.0690 0.2069  -0.0991 532 HOH   B O    
5479 O  O    . HOH   U .   ? 0.6931 0.5044 0.6495 0.1313  0.0151  -0.0830 533 HOH   B O    
5480 O  O    . HOH   U .   ? 0.6198 0.7212 0.5563 -0.1223 -0.0258 0.3003  534 HOH   B O    
5481 O  O    . HOH   U .   ? 0.3220 0.4907 0.9072 -0.0148 -0.1281 0.0114  535 HOH   B O    
5482 O  O    . HOH   U .   ? 0.5289 0.4173 0.4147 -0.1134 0.0691  -0.0239 536 HOH   B O    
5483 O  O    . HOH   U .   ? 0.3074 0.4779 0.7721 -0.0003 0.0299  0.0907  537 HOH   B O    
5484 O  O    . HOH   U .   ? 0.3599 0.3283 0.5479 0.0024  0.0327  0.0533  538 HOH   B O    
5485 O  O    . HOH   U .   ? 0.5459 0.5414 0.5980 -0.1106 -0.0304 -0.1500 539 HOH   B O    
5486 O  O    . HOH   U .   ? 0.4813 0.3636 0.5385 0.0878  -0.0074 -0.0568 540 HOH   B O    
5487 O  O    . HOH   U .   ? 0.4047 0.4529 0.6341 -0.0176 0.0075  -0.0455 541 HOH   B O    
5488 O  O    . HOH   U .   ? 0.3884 0.5708 0.3214 -0.1050 -0.0677 -0.1671 542 HOH   B O    
5489 O  O    . HOH   U .   ? 0.4728 0.3049 0.3294 -0.0328 0.1003  -0.0181 543 HOH   B O    
5490 O  O    . HOH   U .   ? 0.7229 0.4350 0.6709 -0.0831 -0.0745 -0.1060 544 HOH   B O    
5491 O  O    . HOH   U .   ? 0.3472 0.4002 0.6705 -0.0972 0.1685  -0.0633 545 HOH   B O    
5492 O  O    . HOH   U .   ? 0.5941 0.4894 0.7469 -0.0313 -0.0286 -0.0241 546 HOH   B O    
5493 O  O    . HOH   U .   ? 0.7328 0.4697 0.4834 0.0511  0.0042  -0.1145 547 HOH   B O    
5494 O  O    . HOH   U .   ? 0.5430 0.4742 0.9779 0.0931  0.1750  -0.2066 548 HOH   B O    
5495 O  O    . HOH   U .   ? 0.3978 0.8213 0.3766 0.0240  0.0956  0.0534  549 HOH   B O    
5496 O  O    . HOH   U .   ? 0.5222 0.3267 0.3649 -0.0984 -0.1125 -0.0189 550 HOH   B O    
5497 O  O    . HOH   U .   ? 0.5189 0.7095 0.3074 -0.0538 0.0042  -0.0377 551 HOH   B O    
5498 O  O    . HOH   U .   ? 0.3461 0.4084 0.2701 -0.0172 0.0275  0.0045  552 HOH   B O    
5499 O  O    . HOH   U .   ? 0.3443 0.3201 0.3743 -0.0555 -0.0305 0.0645  553 HOH   B O    
5500 O  O    . HOH   U .   ? 0.3843 0.2783 0.3901 -0.0253 0.0586  0.0079  554 HOH   B O    
5501 O  O    . HOH   U .   ? 0.5469 0.7519 0.5826 -0.1247 -0.1436 0.0544  555 HOH   B O    
5502 O  O    . HOH   U .   ? 0.4940 0.2298 0.3728 -0.0168 0.0524  0.0161  556 HOH   B O    
5503 O  O    . HOH   U .   ? 0.4677 0.6544 0.4604 -0.1440 0.0177  -0.2542 557 HOH   B O    
5504 O  O    . HOH   U .   ? 0.4337 0.7672 0.4036 -0.1245 -0.1033 0.0468  558 HOH   B O    
5505 O  O    . HOH   U .   ? 0.6963 0.3735 0.3607 -0.1460 0.0796  -0.0481 559 HOH   B O    
5506 O  O    . HOH   U .   ? 0.3493 0.4832 0.8189 0.0171  -0.0140 -0.0887 560 HOH   B O    
5507 O  O    . HOH   U .   ? 0.8808 0.6841 0.6662 0.0450  0.4135  -0.1126 561 HOH   B O    
5508 O  O    . HOH   V .   ? 0.4223 0.4452 0.6060 -0.0711 -0.1712 0.0332  401 HOH   C O    
5509 O  O    . HOH   V .   ? 0.3109 0.5960 0.3768 -0.0215 0.0244  0.1283  402 HOH   C O    
5510 O  O    . HOH   V .   ? 0.6048 0.4728 0.3762 0.1246  -0.0361 0.0048  403 HOH   C O    
5511 O  O    . HOH   V .   ? 0.5852 0.3677 0.7427 -0.0148 0.1172  0.0899  404 HOH   C O    
5512 O  O    . HOH   V .   ? 0.4954 0.3670 0.3935 -0.0241 0.1273  -0.0214 405 HOH   C O    
5513 O  O    . HOH   V .   ? 0.3554 0.3831 0.2697 -0.1024 -0.0030 -0.0606 406 HOH   C O    
5514 O  O    . HOH   V .   ? 0.5005 0.3875 0.7547 0.0222  0.2393  0.1351  407 HOH   C O    
5515 O  O    . HOH   V .   ? 0.3153 0.4193 0.3744 -0.0297 -0.0342 0.0334  408 HOH   C O    
5516 O  O    . HOH   V .   ? 0.3489 0.2729 0.7461 -0.0496 0.1493  -0.0245 409 HOH   C O    
5517 O  O    . HOH   V .   ? 0.1822 0.1854 0.1595 -0.0146 -0.0198 0.0287  410 HOH   C O    
5518 O  O    . HOH   V .   ? 0.5336 0.3234 0.2665 -0.0662 0.0503  0.0310  411 HOH   C O    
5519 O  O    . HOH   V .   ? 0.4134 0.4101 0.3204 0.0656  0.0753  -0.0456 412 HOH   C O    
5520 O  O    . HOH   V .   ? 0.3952 0.3752 0.4053 0.0395  0.0627  0.0050  413 HOH   C O    
5521 O  O    . HOH   V .   ? 0.6440 0.3396 0.4318 -0.1751 0.0704  0.0603  414 HOH   C O    
5522 O  O    . HOH   V .   ? 0.3927 0.3495 0.3966 -0.0519 -0.0440 -0.0160 415 HOH   C O    
5523 O  O    . HOH   V .   ? 0.6959 0.8736 0.3324 -0.1052 -0.2650 0.0504  416 HOH   C O    
5524 O  O    . HOH   V .   ? 0.3677 0.3743 0.3994 -0.0577 -0.0868 -0.0121 417 HOH   C O    
5525 O  O    . HOH   V .   ? 0.5829 0.4109 0.1895 0.0273  0.0019  0.0159  418 HOH   C O    
5526 O  O    . HOH   V .   ? 0.2300 0.2913 0.3507 0.0136  0.0272  -0.0248 419 HOH   C O    
5527 O  O    . HOH   V .   ? 0.4585 0.4852 0.4856 0.0959  -0.1655 -0.0807 420 HOH   C O    
5528 O  O    . HOH   V .   ? 0.4589 0.7565 0.6377 -0.2538 -0.1040 0.1072  421 HOH   C O    
5529 O  O    . HOH   V .   ? 0.2223 0.1858 0.2214 -0.0216 0.0166  -0.0203 422 HOH   C O    
5530 O  O    . HOH   V .   ? 0.2030 0.1918 0.1717 -0.0172 0.0188  -0.0399 423 HOH   C O    
5531 O  O    . HOH   V .   ? 0.3205 0.3092 0.4598 -0.0114 0.0505  0.0876  424 HOH   C O    
5532 O  O    . HOH   V .   ? 0.3128 0.3449 0.2029 -0.0246 0.0230  -0.0054 425 HOH   C O    
5533 O  O    . HOH   V .   ? 0.4354 0.4947 0.8130 0.0898  0.0827  0.2092  426 HOH   C O    
5534 O  O    . HOH   V .   ? 0.5445 0.3708 0.6184 0.0617  -0.0968 0.0468  427 HOH   C O    
5535 O  O    . HOH   V .   ? 0.1791 0.1767 0.1579 -0.0497 0.0359  -0.0406 428 HOH   C O    
5536 O  O    . HOH   V .   ? 0.6137 0.5660 0.4721 0.1498  0.0532  0.0595  429 HOH   C O    
5537 O  O    . HOH   V .   ? 0.5339 0.7153 0.5171 0.1128  0.1472  0.1593  430 HOH   C O    
5538 O  O    . HOH   V .   ? 0.3475 0.2653 0.3165 -0.0065 0.0279  0.0032  431 HOH   C O    
5539 O  O    . HOH   V .   ? 0.3666 0.2571 0.2399 -0.0105 0.0724  -0.0169 432 HOH   C O    
5540 O  O    . HOH   V .   ? 0.3063 0.4325 0.9446 0.0369  -0.1131 -0.1847 433 HOH   C O    
5541 O  O    . HOH   V .   ? 0.2831 0.3929 0.2699 -0.1181 -0.0612 -0.0070 434 HOH   C O    
5542 O  O    . HOH   V .   ? 0.4000 0.4854 0.3833 -0.0519 0.0012  0.0498  435 HOH   C O    
5543 O  O    . HOH   V .   ? 0.5062 0.3430 0.4835 0.1030  -0.0067 0.0760  436 HOH   C O    
5544 O  O    . HOH   V .   ? 0.3732 0.4280 0.2925 -0.0489 0.0021  0.0266  437 HOH   C O    
5545 O  O    . HOH   V .   ? 0.5473 0.6077 0.3873 -0.0885 0.0291  0.1088  438 HOH   C O    
5546 O  O    . HOH   V .   ? 0.5003 0.6354 0.4699 -0.0185 0.0511  0.0266  439 HOH   C O    
5547 O  O    . HOH   V .   ? 0.4849 0.4291 0.6915 -0.0969 -0.0414 0.0645  440 HOH   C O    
5548 O  O    . HOH   V .   ? 0.3710 0.2403 0.4792 -0.0410 0.0191  -0.0883 441 HOH   C O    
5549 O  O    . HOH   V .   ? 0.6194 0.9944 0.4661 -0.0720 0.0992  0.1442  442 HOH   C O    
5550 O  O    . HOH   V .   ? 0.3015 0.2585 0.3246 -0.0511 -0.0165 0.0313  443 HOH   C O    
5551 O  O    . HOH   V .   ? 0.3375 0.3521 0.2036 -0.0875 -0.0348 0.0129  444 HOH   C O    
5552 O  O    . HOH   V .   ? 0.4846 0.5026 0.4078 -0.1484 0.0481  -0.0916 445 HOH   C O    
5553 O  O    . HOH   V .   ? 0.3642 0.2914 0.3860 0.0389  -0.1754 -0.1046 446 HOH   C O    
5554 O  O    . HOH   V .   ? 0.3030 0.2508 0.6018 -0.0094 -0.0086 0.0616  447 HOH   C O    
5555 O  O    . HOH   V .   ? 0.1816 0.2241 0.3097 0.0058  -0.0406 -0.0346 448 HOH   C O    
5556 O  O    . HOH   V .   ? 0.3089 0.3646 0.4221 0.0039  0.0684  0.0315  449 HOH   C O    
5557 O  O    . HOH   V .   ? 0.1937 0.1637 0.1404 -0.0354 0.0196  -0.0173 450 HOH   C O    
5558 O  O    . HOH   V .   ? 0.4192 0.3719 0.2012 -0.1513 0.0299  -0.0303 451 HOH   C O    
5559 O  O    . HOH   V .   ? 0.4180 0.4573 0.4210 -0.1440 0.1241  -0.2494 452 HOH   C O    
5560 O  O    . HOH   V .   ? 0.3089 0.5639 0.2368 -0.0445 -0.0045 0.1341  453 HOH   C O    
5561 O  O    . HOH   V .   ? 0.5336 0.6100 0.2561 0.0848  -0.0522 -0.1309 454 HOH   C O    
5562 O  O    . HOH   V .   ? 0.1641 0.1799 0.1645 -0.0324 -0.0163 -0.0327 455 HOH   C O    
5563 O  O    . HOH   V .   ? 0.7849 0.4638 0.4572 0.0887  0.0514  0.0948  456 HOH   C O    
5564 O  O    . HOH   V .   ? 0.3874 0.3780 0.2756 -0.1110 -0.0354 0.0390  457 HOH   C O    
5565 O  O    . HOH   V .   ? 0.2491 0.2668 0.2010 -0.0415 0.0527  -0.0493 458 HOH   C O    
5566 O  O    . HOH   V .   ? 0.6018 0.3880 0.5721 0.0525  0.0661  -0.0869 459 HOH   C O    
5567 O  O    . HOH   V .   ? 0.2564 0.2656 0.3174 0.0143  -0.0200 0.0733  460 HOH   C O    
5568 O  O    . HOH   V .   ? 0.4309 0.3129 0.2157 -0.0013 -0.0254 0.0173  461 HOH   C O    
5569 O  O    . HOH   V .   ? 0.2092 0.2331 0.1547 -0.0439 -0.0061 0.0260  462 HOH   C O    
5570 O  O    A HOH   V .   ? 0.2258 0.2081 0.1066 -0.0669 -0.0058 0.0319  463 HOH   C O    
5571 O  O    B HOH   V .   ? 0.3120 0.4124 0.2858 -0.0464 -0.0151 0.0135  463 HOH   C O    
5572 O  O    . HOH   V .   ? 0.2485 0.2327 0.1899 -0.0514 -0.0169 -0.0152 464 HOH   C O    
5573 O  O    . HOH   V .   ? 0.3092 0.3062 0.3235 0.0380  -0.0441 -0.0489 465 HOH   C O    
5574 O  O    A HOH   V .   ? 0.4419 0.3506 0.2539 -0.1989 0.0592  -0.1612 466 HOH   C O    
5575 O  O    B HOH   V .   ? 0.6626 0.4001 0.2300 -0.1221 0.0490  -0.0363 466 HOH   C O    
5576 O  O    . HOH   V .   ? 0.1922 0.2099 0.1702 -0.0144 0.0022  0.0168  467 HOH   C O    
5577 O  O    . HOH   V .   ? 0.5201 0.4075 0.4733 -0.0140 -0.1265 0.1203  468 HOH   C O    
5578 O  O    . HOH   V .   ? 0.3440 0.5285 0.4801 -0.0116 -0.0090 0.0011  469 HOH   C O    
5579 O  O    . HOH   V .   ? 0.6660 0.6441 0.5283 0.2011  0.0516  0.2816  470 HOH   C O    
5580 O  O    . HOH   V .   ? 0.7610 0.6265 0.2462 -0.0061 -0.0143 -0.1612 471 HOH   C O    
5581 O  O    . HOH   V .   ? 0.3282 0.2994 0.5938 -0.0041 0.1317  0.1563  472 HOH   C O    
5582 O  O    . HOH   V .   ? 0.6523 0.3449 0.3639 0.0011  0.0937  -0.0068 473 HOH   C O    
5583 O  O    . HOH   V .   ? 0.3461 0.4206 0.3748 -0.0948 0.1594  -0.1314 474 HOH   C O    
5584 O  O    . HOH   V .   ? 0.3232 0.3143 0.4410 -0.0560 -0.0015 -0.0508 475 HOH   C O    
5585 O  O    . HOH   V .   ? 0.7767 0.3271 0.5382 -0.2131 -0.0564 -0.0829 476 HOH   C O    
5586 O  O    . HOH   V .   ? 0.6031 0.4001 0.6253 -0.0376 -0.3135 0.0448  477 HOH   C O    
5587 O  O    . HOH   V .   ? 0.3498 0.3682 0.4246 0.0056  -0.0579 -0.0315 478 HOH   C O    
5588 O  O    . HOH   V .   ? 0.3688 0.6286 0.4880 -0.0941 -0.1010 0.0444  479 HOH   C O    
5589 O  O    . HOH   V .   ? 0.4251 0.4145 0.5496 -0.0230 -0.0195 0.1265  480 HOH   C O    
5590 O  O    . HOH   V .   ? 0.2860 0.3544 0.3206 0.1018  0.0078  0.0676  481 HOH   C O    
5591 O  O    . HOH   V .   ? 0.4675 0.6060 0.3323 -0.0422 -0.0558 -0.1044 482 HOH   C O    
5592 O  O    . HOH   V .   ? 0.3598 0.3995 0.2752 0.0965  -0.0069 -0.0559 483 HOH   C O    
5593 O  O    . HOH   V .   ? 0.6466 0.7446 0.4471 -0.0597 0.0025  -0.0487 484 HOH   C O    
5594 O  O    . HOH   V .   ? 0.5315 0.3463 0.1666 -0.1762 -0.0471 -0.0036 485 HOH   C O    
5595 O  O    . HOH   V .   ? 0.4411 0.1987 0.4235 -0.0743 -0.0051 0.0077  486 HOH   C O    
5596 O  O    . HOH   V .   ? 0.5303 0.7042 0.4115 0.1752  -0.1358 -0.2757 487 HOH   C O    
5597 O  O    . HOH   V .   ? 0.3827 0.5491 0.3590 -0.1297 0.0295  -0.1686 488 HOH   C O    
5598 O  O    . HOH   V .   ? 0.6416 0.2842 0.5411 0.0375  -0.0527 -0.0786 489 HOH   C O    
5599 O  O    . HOH   V .   ? 0.3113 0.3456 0.3039 -0.0167 0.1441  -0.0171 490 HOH   C O    
5600 O  O    . HOH   V .   ? 0.5930 0.3259 0.2810 -0.1840 0.1662  -0.0462 491 HOH   C O    
5601 O  O    . HOH   V .   ? 0.4561 0.3051 0.4507 -0.0486 -0.0315 -0.1276 492 HOH   C O    
5602 O  O    . HOH   V .   ? 0.3550 0.1893 0.2469 -0.0578 -0.0040 -0.0285 493 HOH   C O    
5603 O  O    . HOH   V .   ? 0.2279 0.2609 0.2844 0.0167  0.0264  -0.0188 494 HOH   C O    
5604 O  O    . HOH   V .   ? 0.5647 0.5638 0.3808 -0.1986 0.0085  0.0830  495 HOH   C O    
5605 O  O    A HOH   V .   ? 0.3926 0.2286 0.2426 0.0192  -0.0118 -0.0060 496 HOH   C O    
5606 O  O    B HOH   V .   ? 0.2830 0.2131 0.3672 -0.0421 -0.0339 -0.0275 496 HOH   C O    
5607 O  O    . HOH   V .   ? 0.3450 0.2503 0.2655 -0.0437 -0.0377 -0.0932 497 HOH   C O    
5608 O  O    . HOH   V .   ? 0.3382 0.5099 0.5333 0.0380  -0.0461 -0.1549 498 HOH   C O    
5609 O  O    A HOH   V .   ? 0.3460 0.2415 0.3911 -0.1122 0.0103  0.0996  499 HOH   C O    
5610 O  O    B HOH   V .   ? 0.3429 0.4045 0.2949 0.0719  0.1477  0.1148  499 HOH   C O    
5611 O  O    . HOH   V .   ? 0.2522 0.5007 0.7756 -0.1154 0.0595  0.0140  500 HOH   C O    
5612 O  O    . HOH   V .   ? 0.2483 0.2047 0.3014 0.0272  0.0180  -0.0348 501 HOH   C O    
5613 O  O    . HOH   V .   ? 0.3053 0.2469 0.4516 -0.0046 -0.0041 -0.0303 502 HOH   C O    
5614 O  O    . HOH   V .   ? 0.5186 0.4884 0.3900 -0.0045 -0.1075 -0.0532 503 HOH   C O    
5615 O  O    . HOH   V .   ? 0.3439 0.4702 0.5816 0.0369  0.0974  0.1806  504 HOH   C O    
5616 O  O    . HOH   V .   ? 0.3571 0.5475 0.4581 -0.0968 -0.0445 0.0435  505 HOH   C O    
5617 O  O    . HOH   V .   ? 0.1901 0.2097 0.2250 -0.0236 0.0253  -0.0084 506 HOH   C O    
5618 O  O    . HOH   V .   ? 0.2048 0.3150 0.2465 0.0546  -0.0264 -0.1043 507 HOH   C O    
5619 O  O    . HOH   V .   ? 0.6608 0.1959 0.4015 -0.0082 -0.1637 -0.0097 508 HOH   C O    
5620 O  O    . HOH   V .   ? 0.4903 0.5242 0.3826 -0.1191 0.0657  -0.1198 509 HOH   C O    
5621 O  O    . HOH   V .   ? 0.3033 0.3492 0.4083 -0.1250 0.0965  -0.1853 510 HOH   C O    
5622 O  O    . HOH   V .   ? 0.2792 0.3070 0.2405 -0.0530 -0.0126 -0.0754 511 HOH   C O    
5623 O  O    . HOH   V .   ? 0.4804 0.4410 0.2749 -0.1806 -0.0400 -0.0411 512 HOH   C O    
5624 O  O    . HOH   V .   ? 0.4309 0.5304 0.3846 0.0814  -0.0701 -0.0429 513 HOH   C O    
5625 O  O    . HOH   V .   ? 0.4200 0.5190 0.3641 0.0062  -0.0674 0.0198  514 HOH   C O    
5626 O  O    . HOH   V .   ? 0.2904 0.2817 0.2408 -0.0026 0.0933  0.0203  515 HOH   C O    
5627 O  O    . HOH   V .   ? 0.6147 0.5894 0.5610 -0.0793 -0.2456 0.0173  516 HOH   C O    
5628 O  O    . HOH   V .   ? 0.2492 0.3250 0.3386 -0.0294 0.0739  -0.0309 517 HOH   C O    
5629 O  O    . HOH   V .   ? 0.5605 0.3897 0.4014 -0.0897 -0.1033 0.0852  518 HOH   C O    
5630 O  O    A HOH   V .   ? 0.4065 0.3552 0.2613 0.0569  -0.0419 -0.1392 519 HOH   C O    
5631 O  O    B HOH   V .   ? 0.7085 0.2603 0.3644 -0.1810 -0.1892 0.0206  519 HOH   C O    
5632 O  O    . HOH   V .   ? 0.2802 0.2861 0.4329 -0.0022 0.1078  0.0430  520 HOH   C O    
5633 O  O    . HOH   V .   ? 0.5911 0.8360 0.5158 -0.1951 -0.0957 0.0241  521 HOH   C O    
5634 O  O    . HOH   V .   ? 0.2393 0.3218 0.3605 0.0251  0.0073  -0.0478 522 HOH   C O    
5635 O  O    . HOH   V .   ? 0.2122 0.1803 0.2240 -0.0492 0.0358  -0.0147 523 HOH   C O    
5636 O  O    . HOH   V .   ? 0.3525 0.2916 0.4471 -0.0478 0.0143  -0.0043 524 HOH   C O    
5637 O  O    . HOH   V .   ? 0.3390 0.4376 0.7382 -0.0119 0.1617  -0.1217 525 HOH   C O    
5638 O  O    . HOH   V .   ? 0.6025 0.4306 0.7910 -0.0544 0.0740  -0.0722 526 HOH   C O    
5639 O  O    . HOH   V .   ? 0.3803 0.5402 0.3811 0.1100  -0.0603 -0.1507 527 HOH   C O    
5640 O  O    . HOH   V .   ? 0.3677 0.4644 0.5494 0.0009  0.0335  0.1110  528 HOH   C O    
5641 O  O    . HOH   V .   ? 0.8191 0.2612 0.3582 -0.0630 0.0676  0.0349  529 HOH   C O    
5642 O  O    . HOH   V .   ? 0.4646 0.3550 0.6202 0.0725  -0.0342 0.0459  530 HOH   C O    
5643 O  O    . HOH   V .   ? 0.4996 0.4443 0.6090 -0.0464 0.0970  -0.1282 531 HOH   C O    
5644 O  O    . HOH   V .   ? 0.5672 0.9665 0.4985 -0.0964 -0.1399 -0.1467 532 HOH   C O    
5645 O  O    . HOH   V .   ? 0.3833 0.7560 0.3484 0.2449  -0.0006 -0.0718 533 HOH   C O    
5646 O  O    . HOH   V .   ? 0.4965 0.2682 0.4397 -0.0098 0.0215  -0.0077 534 HOH   C O    
5647 O  O    . HOH   V .   ? 0.5662 0.6623 0.7622 -0.2800 0.1128  0.2107  535 HOH   C O    
5648 O  O    . HOH   V .   ? 0.6485 0.5758 0.3694 0.2019  0.1662  0.0985  536 HOH   C O    
5649 O  O    . HOH   V .   ? 0.7273 0.7683 0.2597 0.0604  -0.0386 -0.0162 537 HOH   C O    
5650 O  O    . HOH   V .   ? 0.3063 0.5219 0.1908 -0.0267 -0.0073 -0.0054 538 HOH   C O    
5651 O  O    . HOH   V .   ? 0.3512 0.3090 0.6006 0.0553  0.1038  0.1260  539 HOH   C O    
5652 O  O    . HOH   V .   ? 0.4584 0.8214 0.4566 -0.1909 -0.2257 0.1145  540 HOH   C O    
5653 O  O    . HOH   V .   ? 0.5498 0.5183 0.5284 0.0412  0.0178  0.1263  541 HOH   C O    
5654 O  O    . HOH   V .   ? 0.5728 0.9752 0.4348 -0.0992 -0.0328 0.0549  542 HOH   C O    
5655 O  O    . HOH   V .   ? 0.5163 0.4753 0.6877 -0.1196 0.1133  -0.0577 543 HOH   C O    
5656 O  O    . HOH   V .   ? 0.4869 0.4111 0.5616 -0.0125 -0.1098 0.0156  544 HOH   C O    
5657 O  O    . HOH   V .   ? 0.4606 0.8742 0.6023 -0.0207 0.0070  -0.0005 545 HOH   C O    
5658 O  O    . HOH   V .   ? 0.3946 0.4900 0.4140 -0.0144 0.0108  0.0039  546 HOH   C O    
5659 O  O    . HOH   V .   ? 0.5919 0.5838 0.4844 -0.0001 -0.0706 0.1342  547 HOH   C O    
5660 O  O    . HOH   V .   ? 0.4590 0.4599 0.3461 -0.1285 -0.0696 -0.0512 548 HOH   C O    
5661 O  O    . HOH   V .   ? 0.4773 0.5653 0.3229 -0.0828 -0.0557 -0.1363 549 HOH   C O    
5662 O  O    . HOH   V .   ? 0.5086 0.5105 0.4193 -0.0232 0.2043  -0.0573 550 HOH   C O    
5663 O  O    . HOH   V .   ? 0.7899 0.5397 0.6147 0.2393  0.1798  0.2341  551 HOH   C O    
5664 O  O    . HOH   V .   ? 0.3814 0.3794 0.5844 -0.0279 0.0747  0.0113  552 HOH   C O    
5665 O  O    . HOH   V .   ? 0.5945 0.6266 0.5011 -0.0712 -0.0716 -0.0230 553 HOH   C O    
5666 O  O    . HOH   V .   ? 0.4185 0.5323 0.4326 -0.1014 -0.1005 0.1187  554 HOH   C O    
5667 O  O    . HOH   V .   ? 0.3193 0.4035 0.3217 0.0550  -0.0293 0.0381  555 HOH   C O    
5668 O  O    . HOH   V .   ? 0.3800 0.4928 0.4163 -0.0624 0.0406  0.0035  556 HOH   C O    
5669 O  O    . HOH   V .   ? 0.3342 0.5566 0.3517 0.0681  -0.0460 -0.0575 557 HOH   C O    
5670 O  O    . HOH   V .   ? 0.4735 0.5088 0.6187 0.0040  -0.0979 0.0076  558 HOH   C O    
# 
