data_9OWG
# 
_entry.id   9OWG 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9OWG         pdb_00009owg 10.2210/pdb9owg/pdb 
WWPDB D_1000296613 ?            ?                   
# 
_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       2025-06-18 
_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                        9OWG 
_pdbx_database_status.recvd_initial_deposition_date   2025-06-02 
_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           Y 
# 
_pdbx_database_related.db_name        TargetTrack 
_pdbx_database_related.db_id          CSBID-IDP95774 
_pdbx_database_related.content_type   unspecified 
_pdbx_database_related.details        . 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              k-satchell@northwestern.edu 
_pdbx_contact_author.name_first         Karla 
_pdbx_contact_author.name_last          Satchell 
_pdbx_contact_author.name_mi            F 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3274-7611 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Minasov, G.'                                                  1 ? 
'Wawrzak, Z.'                                                  2 ? 
'Skarina, T.'                                                  3 ? 
'Stogios, P.J.'                                                4 ? 
'Savchenko, A.'                                                5 ? 
'Satchell, K.F.'                                               6 ? 
'Center for Structural Biology of Infectious Diseases (CSBID)' 7 ? 
# 
_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                     
'Crystal Structure of the Immunity Protein (52 domain-containing protein) from Pseudomonas aeruginosa PAO1.' 
_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 'Minasov, G.'                                                  1 ? 
primary 'Wawrzak, Z.'                                                  2 ? 
primary 'Skarina, T.'                                                  3 ? 
primary 'Stogios, P.J.'                                                4 ? 
primary 'Savchenko, A.'                                                5 ? 
primary 'Satchell, K.F.'                                               6 ? 
primary 'Center for Structural Biology of Infectious Diseases (CSBID)' 7 ? 
# 
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 'Immunity protein 52 domain-containing protein'       27601.250 1   ? ? ? ? 
2 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305   1   ? ? ? ? 
3 non-polymer syn 'PHOSPHATE ION'                                       94.971    2   ? ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                        62.068    1   ? ? ? ? 
5 non-polymer syn 'CARBONATE ION'                                       60.009    1   ? ? ? ? 
6 water       nat water                                                 18.015    100 ? ? ? ? 
# 
_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       
;SNAMTDAKAFRRYIFELYFDPARLLELDDDQHLQRIERFLDALAPLHPVLENWYLCGDSLRDALSHNVTEHRQDLAKALS
RDRRTRAVELVLWNGEEDPLKGGLSLDYEASGRAVSSRLQLEDAGSLLQVFDAPASSFVAIFLAVLEIWPETTWGMLAPH
AYFVHQRTFPDRRSIGWIGFCPHPLRATDFPAATELVDIPGRGTLLLNGREPMDETRREHFERVGEADIKLMELGYLPPL
RG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SNAMTDAKAFRRYIFELYFDPARLLELDDDQHLQRIERFLDALAPLHPVLENWYLCGDSLRDALSHNVTEHRQDLAKALS
RDRRTRAVELVLWNGEEDPLKGGLSLDYEASGRAVSSRLQLEDAGSLLQVFDAPASSFVAIFLAVLEIWPETTWGMLAPH
AYFVHQRTFPDRRSIGWIGFCPHPLRATDFPAATELVDIPGRGTLLLNGREPMDETRREHFERVGEADIKLMELGYLPPL
RG
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         CSBID-IDP95774 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 
3 'PHOSPHATE ION'                                       PO4 
4 1,2-ETHANEDIOL                                        EDO 
5 'CARBONATE ION'                                       CO3 
6 water                                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   ASN n 
1 3   ALA n 
1 4   MET n 
1 5   THR n 
1 6   ASP n 
1 7   ALA n 
1 8   LYS n 
1 9   ALA n 
1 10  PHE n 
1 11  ARG n 
1 12  ARG n 
1 13  TYR n 
1 14  ILE n 
1 15  PHE n 
1 16  GLU n 
1 17  LEU n 
1 18  TYR n 
1 19  PHE n 
1 20  ASP n 
1 21  PRO n 
1 22  ALA n 
1 23  ARG n 
1 24  LEU n 
1 25  LEU n 
1 26  GLU n 
1 27  LEU n 
1 28  ASP n 
1 29  ASP n 
1 30  ASP n 
1 31  GLN n 
1 32  HIS n 
1 33  LEU n 
1 34  GLN n 
1 35  ARG n 
1 36  ILE n 
1 37  GLU n 
1 38  ARG n 
1 39  PHE n 
1 40  LEU n 
1 41  ASP n 
1 42  ALA n 
1 43  LEU n 
1 44  ALA n 
1 45  PRO n 
1 46  LEU n 
1 47  HIS n 
1 48  PRO n 
1 49  VAL n 
1 50  LEU n 
1 51  GLU n 
1 52  ASN n 
1 53  TRP n 
1 54  TYR n 
1 55  LEU n 
1 56  CYS n 
1 57  GLY n 
1 58  ASP n 
1 59  SER n 
1 60  LEU n 
1 61  ARG n 
1 62  ASP n 
1 63  ALA n 
1 64  LEU n 
1 65  SER n 
1 66  HIS n 
1 67  ASN n 
1 68  VAL n 
1 69  THR n 
1 70  GLU n 
1 71  HIS n 
1 72  ARG n 
1 73  GLN n 
1 74  ASP n 
1 75  LEU n 
1 76  ALA n 
1 77  LYS n 
1 78  ALA n 
1 79  LEU n 
1 80  SER n 
1 81  ARG n 
1 82  ASP n 
1 83  ARG n 
1 84  ARG n 
1 85  THR n 
1 86  ARG n 
1 87  ALA n 
1 88  VAL n 
1 89  GLU n 
1 90  LEU n 
1 91  VAL n 
1 92  LEU n 
1 93  TRP n 
1 94  ASN n 
1 95  GLY n 
1 96  GLU n 
1 97  GLU n 
1 98  ASP n 
1 99  PRO n 
1 100 LEU n 
1 101 LYS n 
1 102 GLY n 
1 103 GLY n 
1 104 LEU n 
1 105 SER n 
1 106 LEU n 
1 107 ASP n 
1 108 TYR n 
1 109 GLU n 
1 110 ALA n 
1 111 SER n 
1 112 GLY n 
1 113 ARG n 
1 114 ALA n 
1 115 VAL n 
1 116 SER n 
1 117 SER n 
1 118 ARG n 
1 119 LEU n 
1 120 GLN n 
1 121 LEU n 
1 122 GLU n 
1 123 ASP n 
1 124 ALA n 
1 125 GLY n 
1 126 SER n 
1 127 LEU n 
1 128 LEU n 
1 129 GLN n 
1 130 VAL n 
1 131 PHE n 
1 132 ASP n 
1 133 ALA n 
1 134 PRO n 
1 135 ALA n 
1 136 SER n 
1 137 SER n 
1 138 PHE n 
1 139 VAL n 
1 140 ALA n 
1 141 ILE n 
1 142 PHE n 
1 143 LEU n 
1 144 ALA n 
1 145 VAL n 
1 146 LEU n 
1 147 GLU n 
1 148 ILE n 
1 149 TRP n 
1 150 PRO n 
1 151 GLU n 
1 152 THR n 
1 153 THR n 
1 154 TRP n 
1 155 GLY n 
1 156 MET n 
1 157 LEU n 
1 158 ALA n 
1 159 PRO n 
1 160 HIS n 
1 161 ALA n 
1 162 TYR n 
1 163 PHE n 
1 164 VAL n 
1 165 HIS n 
1 166 GLN n 
1 167 ARG n 
1 168 THR n 
1 169 PHE n 
1 170 PRO n 
1 171 ASP n 
1 172 ARG n 
1 173 ARG n 
1 174 SER n 
1 175 ILE n 
1 176 GLY n 
1 177 TRP n 
1 178 ILE n 
1 179 GLY n 
1 180 PHE n 
1 181 CYS n 
1 182 PRO n 
1 183 HIS n 
1 184 PRO n 
1 185 LEU n 
1 186 ARG n 
1 187 ALA n 
1 188 THR n 
1 189 ASP n 
1 190 PHE n 
1 191 PRO n 
1 192 ALA n 
1 193 ALA n 
1 194 THR n 
1 195 GLU n 
1 196 LEU n 
1 197 VAL n 
1 198 ASP n 
1 199 ILE n 
1 200 PRO n 
1 201 GLY n 
1 202 ARG n 
1 203 GLY n 
1 204 THR n 
1 205 LEU n 
1 206 LEU n 
1 207 LEU n 
1 208 ASN n 
1 209 GLY n 
1 210 ARG n 
1 211 GLU n 
1 212 PRO n 
1 213 MET n 
1 214 ASP n 
1 215 GLU n 
1 216 THR n 
1 217 ARG n 
1 218 ARG n 
1 219 GLU n 
1 220 HIS n 
1 221 PHE n 
1 222 GLU n 
1 223 ARG n 
1 224 VAL n 
1 225 GLY n 
1 226 GLU n 
1 227 ALA n 
1 228 ASP n 
1 229 ILE n 
1 230 LYS n 
1 231 LEU n 
1 232 MET n 
1 233 GLU n 
1 234 LEU n 
1 235 GLY n 
1 236 TYR n 
1 237 LEU n 
1 238 PRO n 
1 239 PRO n 
1 240 LEU n 
1 241 ARG n 
1 242 GLY 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                   242 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PA3908 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    PAO1 
_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      'Pseudomonas aeruginosa PAO1' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     208964 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              Magic 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pMCSG53 
_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 
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 
CO3 non-polymer         . 'CARBONATE ION'                                       ?                 'C O3 -2'        60.009  
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  
EPE non-polymer         . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES             'C8 H18 N2 O4 S' 238.305 
GLN 'L-peptide linking' y GLUTAMINE                                             ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                       ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                               ?                 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                             ?                 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                                 ?                 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                            ?                 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                               ?                 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                                ?                 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                            ?                 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                         ?                 'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION'                                       ?                 'O4 P -3'        94.971  
PRO 'L-peptide linking' y PROLINE                                               ?                 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                ?                 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                             ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                            ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                              ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   -2  ?   ?   ?   A . n 
A 1 2   ASN 2   -1  ?   ?   ?   A . n 
A 1 3   ALA 3   0   ?   ?   ?   A . n 
A 1 4   MET 4   1   ?   ?   ?   A . n 
A 1 5   THR 5   2   ?   ?   ?   A . n 
A 1 6   ASP 6   3   ?   ?   ?   A . n 
A 1 7   ALA 7   4   4   ALA ALA A . n 
A 1 8   LYS 8   5   5   LYS LYS A . n 
A 1 9   ALA 9   6   6   ALA ALA A . n 
A 1 10  PHE 10  7   7   PHE PHE A . n 
A 1 11  ARG 11  8   8   ARG ARG A . n 
A 1 12  ARG 12  9   9   ARG ARG A . n 
A 1 13  TYR 13  10  10  TYR TYR A . n 
A 1 14  ILE 14  11  11  ILE ILE A . n 
A 1 15  PHE 15  12  12  PHE PHE A . n 
A 1 16  GLU 16  13  13  GLU GLU A . n 
A 1 17  LEU 17  14  14  LEU LEU A . n 
A 1 18  TYR 18  15  15  TYR TYR A . n 
A 1 19  PHE 19  16  16  PHE PHE A . n 
A 1 20  ASP 20  17  17  ASP ASP A . n 
A 1 21  PRO 21  18  18  PRO PRO A . n 
A 1 22  ALA 22  19  19  ALA ALA A . n 
A 1 23  ARG 23  20  20  ARG ARG A . n 
A 1 24  LEU 24  21  21  LEU LEU A . n 
A 1 25  LEU 25  22  22  LEU LEU A . n 
A 1 26  GLU 26  23  23  GLU GLU A . n 
A 1 27  LEU 27  24  24  LEU LEU A . n 
A 1 28  ASP 28  25  25  ASP ASP A . n 
A 1 29  ASP 29  26  26  ASP ASP A . n 
A 1 30  ASP 30  27  27  ASP ASP A . n 
A 1 31  GLN 31  28  28  GLN GLN A . n 
A 1 32  HIS 32  29  29  HIS HIS A . n 
A 1 33  LEU 33  30  30  LEU LEU A . n 
A 1 34  GLN 34  31  31  GLN GLN A . n 
A 1 35  ARG 35  32  32  ARG ARG A . n 
A 1 36  ILE 36  33  33  ILE ILE A . n 
A 1 37  GLU 37  34  34  GLU GLU A . n 
A 1 38  ARG 38  35  35  ARG ARG A . n 
A 1 39  PHE 39  36  36  PHE PHE A . n 
A 1 40  LEU 40  37  37  LEU LEU A . n 
A 1 41  ASP 41  38  38  ASP ASP A . n 
A 1 42  ALA 42  39  39  ALA ALA A . n 
A 1 43  LEU 43  40  40  LEU LEU A . n 
A 1 44  ALA 44  41  41  ALA ALA A . n 
A 1 45  PRO 45  42  42  PRO PRO A . n 
A 1 46  LEU 46  43  43  LEU LEU A . n 
A 1 47  HIS 47  44  44  HIS HIS A . n 
A 1 48  PRO 48  45  45  PRO PRO A . n 
A 1 49  VAL 49  46  46  VAL VAL A . n 
A 1 50  LEU 50  47  47  LEU LEU A . n 
A 1 51  GLU 51  48  48  GLU GLU A . n 
A 1 52  ASN 52  49  49  ASN ASN A . n 
A 1 53  TRP 53  50  50  TRP TRP A . n 
A 1 54  TYR 54  51  51  TYR TYR A . n 
A 1 55  LEU 55  52  52  LEU LEU A . n 
A 1 56  CYS 56  53  53  CYS CYS A . n 
A 1 57  GLY 57  54  54  GLY GLY A . n 
A 1 58  ASP 58  55  55  ASP ASP A . n 
A 1 59  SER 59  56  56  SER SER A . n 
A 1 60  LEU 60  57  57  LEU LEU A . n 
A 1 61  ARG 61  58  58  ARG ARG A . n 
A 1 62  ASP 62  59  59  ASP ASP A . n 
A 1 63  ALA 63  60  60  ALA ALA A . n 
A 1 64  LEU 64  61  61  LEU LEU A . n 
A 1 65  SER 65  62  62  SER SER A . n 
A 1 66  HIS 66  63  63  HIS HIS A . n 
A 1 67  ASN 67  64  64  ASN ASN A . n 
A 1 68  VAL 68  65  65  VAL VAL A . n 
A 1 69  THR 69  66  66  THR THR A . n 
A 1 70  GLU 70  67  67  GLU GLU A . n 
A 1 71  HIS 71  68  68  HIS HIS A . n 
A 1 72  ARG 72  69  69  ARG ARG A . n 
A 1 73  GLN 73  70  70  GLN GLN A . n 
A 1 74  ASP 74  71  71  ASP ASP A . n 
A 1 75  LEU 75  72  72  LEU LEU A . n 
A 1 76  ALA 76  73  73  ALA ALA A . n 
A 1 77  LYS 77  74  74  LYS LYS A . n 
A 1 78  ALA 78  75  75  ALA ALA A . n 
A 1 79  LEU 79  76  76  LEU LEU A . n 
A 1 80  SER 80  77  77  SER SER A . n 
A 1 81  ARG 81  78  78  ARG ARG A . n 
A 1 82  ASP 82  79  79  ASP ASP A . n 
A 1 83  ARG 83  80  80  ARG ARG A . n 
A 1 84  ARG 84  81  81  ARG ARG A . n 
A 1 85  THR 85  82  82  THR THR A . n 
A 1 86  ARG 86  83  83  ARG ARG A . n 
A 1 87  ALA 87  84  84  ALA ALA A . n 
A 1 88  VAL 88  85  85  VAL VAL A . n 
A 1 89  GLU 89  86  86  GLU GLU A . n 
A 1 90  LEU 90  87  87  LEU LEU A . n 
A 1 91  VAL 91  88  88  VAL VAL A . n 
A 1 92  LEU 92  89  89  LEU LEU A . n 
A 1 93  TRP 93  90  90  TRP TRP A . n 
A 1 94  ASN 94  91  91  ASN ASN A . n 
A 1 95  GLY 95  92  92  GLY GLY A . n 
A 1 96  GLU 96  93  93  GLU GLU A . n 
A 1 97  GLU 97  94  94  GLU GLU A . n 
A 1 98  ASP 98  95  95  ASP ASP A . n 
A 1 99  PRO 99  96  96  PRO PRO A . n 
A 1 100 LEU 100 97  97  LEU LEU A . n 
A 1 101 LYS 101 98  98  LYS LYS A . n 
A 1 102 GLY 102 99  99  GLY GLY A . n 
A 1 103 GLY 103 100 100 GLY GLY A . n 
A 1 104 LEU 104 101 101 LEU LEU A . n 
A 1 105 SER 105 102 102 SER SER A . n 
A 1 106 LEU 106 103 103 LEU LEU A . n 
A 1 107 ASP 107 104 104 ASP ASP A . n 
A 1 108 TYR 108 105 105 TYR TYR A . n 
A 1 109 GLU 109 106 106 GLU GLU A . n 
A 1 110 ALA 110 107 107 ALA ALA A . n 
A 1 111 SER 111 108 108 SER SER A . n 
A 1 112 GLY 112 109 109 GLY GLY A . n 
A 1 113 ARG 113 110 110 ARG ARG A . n 
A 1 114 ALA 114 111 111 ALA ALA A . n 
A 1 115 VAL 115 112 112 VAL VAL A . n 
A 1 116 SER 116 113 113 SER SER A . n 
A 1 117 SER 117 114 114 SER SER A . n 
A 1 118 ARG 118 115 115 ARG ARG A . n 
A 1 119 LEU 119 116 116 LEU LEU A . n 
A 1 120 GLN 120 117 117 GLN GLN A . n 
A 1 121 LEU 121 118 118 LEU LEU A . n 
A 1 122 GLU 122 119 119 GLU GLU A . n 
A 1 123 ASP 123 120 120 ASP ASP A . n 
A 1 124 ALA 124 121 121 ALA ALA A . n 
A 1 125 GLY 125 122 122 GLY GLY A . n 
A 1 126 SER 126 123 123 SER SER A . n 
A 1 127 LEU 127 124 124 LEU LEU A . n 
A 1 128 LEU 128 125 125 LEU LEU A . n 
A 1 129 GLN 129 126 126 GLN GLN A . n 
A 1 130 VAL 130 127 127 VAL VAL A . n 
A 1 131 PHE 131 128 128 PHE PHE A . n 
A 1 132 ASP 132 129 129 ASP ASP A . n 
A 1 133 ALA 133 130 130 ALA ALA A . n 
A 1 134 PRO 134 131 131 PRO PRO A . n 
A 1 135 ALA 135 132 132 ALA ALA A . n 
A 1 136 SER 136 133 133 SER SER A . n 
A 1 137 SER 137 134 134 SER SER A . n 
A 1 138 PHE 138 135 135 PHE PHE A . n 
A 1 139 VAL 139 136 136 VAL VAL A . n 
A 1 140 ALA 140 137 137 ALA ALA A . n 
A 1 141 ILE 141 138 138 ILE ILE A . n 
A 1 142 PHE 142 139 139 PHE PHE A . n 
A 1 143 LEU 143 140 140 LEU LEU A . n 
A 1 144 ALA 144 141 141 ALA ALA A . n 
A 1 145 VAL 145 142 142 VAL VAL A . n 
A 1 146 LEU 146 143 143 LEU LEU A . n 
A 1 147 GLU 147 144 144 GLU GLU A . n 
A 1 148 ILE 148 145 145 ILE ILE A . n 
A 1 149 TRP 149 146 146 TRP TRP A . n 
A 1 150 PRO 150 147 147 PRO PRO A . n 
A 1 151 GLU 151 148 148 GLU GLU A . n 
A 1 152 THR 152 149 149 THR THR A . n 
A 1 153 THR 153 150 150 THR THR A . n 
A 1 154 TRP 154 151 151 TRP TRP A . n 
A 1 155 GLY 155 152 152 GLY GLY A . n 
A 1 156 MET 156 153 153 MET MET A . n 
A 1 157 LEU 157 154 154 LEU LEU A . n 
A 1 158 ALA 158 155 155 ALA ALA A . n 
A 1 159 PRO 159 156 156 PRO PRO A . n 
A 1 160 HIS 160 157 157 HIS HIS A . n 
A 1 161 ALA 161 158 158 ALA ALA A . n 
A 1 162 TYR 162 159 159 TYR TYR A . n 
A 1 163 PHE 163 160 160 PHE PHE A . n 
A 1 164 VAL 164 161 161 VAL VAL A . n 
A 1 165 HIS 165 162 162 HIS HIS A . n 
A 1 166 GLN 166 163 163 GLN GLN A . n 
A 1 167 ARG 167 164 164 ARG ARG A . n 
A 1 168 THR 168 165 165 THR THR A . n 
A 1 169 PHE 169 166 166 PHE PHE A . n 
A 1 170 PRO 170 167 167 PRO PRO A . n 
A 1 171 ASP 171 168 168 ASP ASP A . n 
A 1 172 ARG 172 169 169 ARG ARG A . n 
A 1 173 ARG 173 170 170 ARG ARG A . n 
A 1 174 SER 174 171 171 SER SER A . n 
A 1 175 ILE 175 172 172 ILE ILE A . n 
A 1 176 GLY 176 173 173 GLY GLY A . n 
A 1 177 TRP 177 174 174 TRP TRP A . n 
A 1 178 ILE 178 175 175 ILE ILE A . n 
A 1 179 GLY 179 176 176 GLY GLY A . n 
A 1 180 PHE 180 177 177 PHE PHE A . n 
A 1 181 CYS 181 178 178 CYS CYS A . n 
A 1 182 PRO 182 179 179 PRO PRO A . n 
A 1 183 HIS 183 180 180 HIS HIS A . n 
A 1 184 PRO 184 181 181 PRO PRO A . n 
A 1 185 LEU 185 182 182 LEU LEU A . n 
A 1 186 ARG 186 183 183 ARG ARG A . n 
A 1 187 ALA 187 184 184 ALA ALA A . n 
A 1 188 THR 188 185 185 THR THR A . n 
A 1 189 ASP 189 186 186 ASP ASP A . n 
A 1 190 PHE 190 187 187 PHE PHE A . n 
A 1 191 PRO 191 188 188 PRO PRO A . n 
A 1 192 ALA 192 189 189 ALA ALA A . n 
A 1 193 ALA 193 190 190 ALA ALA A . n 
A 1 194 THR 194 191 191 THR THR A . n 
A 1 195 GLU 195 192 192 GLU GLU A . n 
A 1 196 LEU 196 193 193 LEU LEU A . n 
A 1 197 VAL 197 194 194 VAL VAL A . n 
A 1 198 ASP 198 195 195 ASP ASP A . n 
A 1 199 ILE 199 196 196 ILE ILE A . n 
A 1 200 PRO 200 197 197 PRO PRO A . n 
A 1 201 GLY 201 198 198 GLY GLY A . n 
A 1 202 ARG 202 199 199 ARG ARG A . n 
A 1 203 GLY 203 200 200 GLY GLY A . n 
A 1 204 THR 204 201 201 THR THR A . n 
A 1 205 LEU 205 202 202 LEU LEU A . n 
A 1 206 LEU 206 203 203 LEU LEU A . n 
A 1 207 LEU 207 204 204 LEU LEU A . n 
A 1 208 ASN 208 205 205 ASN ASN A . n 
A 1 209 GLY 209 206 206 GLY GLY A . n 
A 1 210 ARG 210 207 207 ARG ARG A . n 
A 1 211 GLU 211 208 208 GLU GLU A . n 
A 1 212 PRO 212 209 209 PRO PRO A . n 
A 1 213 MET 213 210 210 MET MET A . n 
A 1 214 ASP 214 211 ?   ?   ?   A . n 
A 1 215 GLU 215 212 ?   ?   ?   A . n 
A 1 216 THR 216 213 ?   ?   ?   A . n 
A 1 217 ARG 217 214 ?   ?   ?   A . n 
A 1 218 ARG 218 215 ?   ?   ?   A . n 
A 1 219 GLU 219 216 ?   ?   ?   A . n 
A 1 220 HIS 220 217 ?   ?   ?   A . n 
A 1 221 PHE 221 218 218 PHE PHE A . n 
A 1 222 GLU 222 219 219 GLU GLU A . n 
A 1 223 ARG 223 220 220 ARG ARG A . n 
A 1 224 VAL 224 221 221 VAL VAL A . n 
A 1 225 GLY 225 222 222 GLY GLY A . n 
A 1 226 GLU 226 223 223 GLU GLU A . n 
A 1 227 ALA 227 224 224 ALA ALA A . n 
A 1 228 ASP 228 225 225 ASP ASP A . n 
A 1 229 ILE 229 226 226 ILE ILE A . n 
A 1 230 LYS 230 227 227 LYS LYS A . n 
A 1 231 LEU 231 228 228 LEU LEU A . n 
A 1 232 MET 232 229 229 MET MET A . n 
A 1 233 GLU 233 230 230 GLU GLU A . n 
A 1 234 LEU 234 231 231 LEU LEU A . n 
A 1 235 GLY 235 232 232 GLY GLY A . n 
A 1 236 TYR 236 233 233 TYR TYR A . n 
A 1 237 LEU 237 234 234 LEU LEU A . n 
A 1 238 PRO 238 235 235 PRO PRO A . n 
A 1 239 PRO 239 236 236 PRO PRO A . n 
A 1 240 LEU 240 237 237 LEU LEU A . n 
A 1 241 ARG 241 238 238 ARG ARG A . n 
A 1 242 GLY 242 239 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 EPE 1   301 1   EPE EPE A . 
C 3 PO4 1   302 2   PO4 PO4 A . 
D 3 PO4 1   303 3   PO4 PO4 A . 
E 4 EDO 1   304 4   EDO EDO A . 
F 5 CO3 1   305 5   CO3 CO3 A . 
G 6 HOH 1   401 89  HOH HOH A . 
G 6 HOH 2   402 102 HOH HOH A . 
G 6 HOH 3   403 59  HOH HOH A . 
G 6 HOH 4   404 88  HOH HOH A . 
G 6 HOH 5   405 70  HOH HOH A . 
G 6 HOH 6   406 13  HOH HOH A . 
G 6 HOH 7   407 87  HOH HOH A . 
G 6 HOH 8   408 66  HOH HOH A . 
G 6 HOH 9   409 19  HOH HOH A . 
G 6 HOH 10  410 72  HOH HOH A . 
G 6 HOH 11  411 37  HOH HOH A . 
G 6 HOH 12  412 78  HOH HOH A . 
G 6 HOH 13  413 56  HOH HOH A . 
G 6 HOH 14  414 47  HOH HOH A . 
G 6 HOH 15  415 76  HOH HOH A . 
G 6 HOH 16  416 36  HOH HOH A . 
G 6 HOH 17  417 10  HOH HOH A . 
G 6 HOH 18  418 14  HOH HOH A . 
G 6 HOH 19  419 35  HOH HOH A . 
G 6 HOH 20  420 62  HOH HOH A . 
G 6 HOH 21  421 27  HOH HOH A . 
G 6 HOH 22  422 92  HOH HOH A . 
G 6 HOH 23  423 73  HOH HOH A . 
G 6 HOH 24  424 90  HOH HOH A . 
G 6 HOH 25  425 39  HOH HOH A . 
G 6 HOH 26  426 43  HOH HOH A . 
G 6 HOH 27  427 99  HOH HOH A . 
G 6 HOH 28  428 61  HOH HOH A . 
G 6 HOH 29  429 104 HOH HOH A . 
G 6 HOH 30  430 84  HOH HOH A . 
G 6 HOH 31  431 22  HOH HOH A . 
G 6 HOH 32  432 33  HOH HOH A . 
G 6 HOH 33  433 52  HOH HOH A . 
G 6 HOH 34  434 26  HOH HOH A . 
G 6 HOH 35  435 82  HOH HOH A . 
G 6 HOH 36  436 98  HOH HOH A . 
G 6 HOH 37  437 20  HOH HOH A . 
G 6 HOH 38  438 100 HOH HOH A . 
G 6 HOH 39  439 93  HOH HOH A . 
G 6 HOH 40  440 30  HOH HOH A . 
G 6 HOH 41  441 42  HOH HOH A . 
G 6 HOH 42  442 48  HOH HOH A . 
G 6 HOH 43  443 45  HOH HOH A . 
G 6 HOH 44  444 32  HOH HOH A . 
G 6 HOH 45  445 23  HOH HOH A . 
G 6 HOH 46  446 55  HOH HOH A . 
G 6 HOH 47  447 94  HOH HOH A . 
G 6 HOH 48  448 16  HOH HOH A . 
G 6 HOH 49  449 17  HOH HOH A . 
G 6 HOH 50  450 64  HOH HOH A . 
G 6 HOH 51  451 80  HOH HOH A . 
G 6 HOH 52  452 49  HOH HOH A . 
G 6 HOH 53  453 103 HOH HOH A . 
G 6 HOH 54  454 7   HOH HOH A . 
G 6 HOH 55  455 15  HOH HOH A . 
G 6 HOH 56  456 9   HOH HOH A . 
G 6 HOH 57  457 18  HOH HOH A . 
G 6 HOH 58  458 75  HOH HOH A . 
G 6 HOH 59  459 34  HOH HOH A . 
G 6 HOH 60  460 21  HOH HOH A . 
G 6 HOH 61  461 96  HOH HOH A . 
G 6 HOH 62  462 6   HOH HOH A . 
G 6 HOH 63  463 68  HOH HOH A . 
G 6 HOH 64  464 8   HOH HOH A . 
G 6 HOH 65  465 65  HOH HOH A . 
G 6 HOH 66  466 58  HOH HOH A . 
G 6 HOH 67  467 69  HOH HOH A . 
G 6 HOH 68  468 67  HOH HOH A . 
G 6 HOH 69  469 51  HOH HOH A . 
G 6 HOH 70  470 105 HOH HOH A . 
G 6 HOH 71  471 25  HOH HOH A . 
G 6 HOH 72  472 12  HOH HOH A . 
G 6 HOH 73  473 97  HOH HOH A . 
G 6 HOH 74  474 28  HOH HOH A . 
G 6 HOH 75  475 54  HOH HOH A . 
G 6 HOH 76  476 31  HOH HOH A . 
G 6 HOH 77  477 83  HOH HOH A . 
G 6 HOH 78  478 46  HOH HOH A . 
G 6 HOH 79  479 71  HOH HOH A . 
G 6 HOH 80  480 38  HOH HOH A . 
G 6 HOH 81  481 74  HOH HOH A . 
G 6 HOH 82  482 44  HOH HOH A . 
G 6 HOH 83  483 60  HOH HOH A . 
G 6 HOH 84  484 91  HOH HOH A . 
G 6 HOH 85  485 11  HOH HOH A . 
G 6 HOH 86  486 101 HOH HOH A . 
G 6 HOH 87  487 40  HOH HOH A . 
G 6 HOH 88  488 53  HOH HOH A . 
G 6 HOH 89  489 29  HOH HOH A . 
G 6 HOH 90  490 85  HOH HOH A . 
G 6 HOH 91  491 50  HOH HOH A . 
G 6 HOH 92  492 24  HOH HOH A . 
G 6 HOH 93  493 63  HOH HOH A . 
G 6 HOH 94  494 41  HOH HOH A . 
G 6 HOH 95  495 81  HOH HOH A . 
G 6 HOH 96  496 77  HOH HOH A . 
G 6 HOH 97  497 86  HOH HOH A . 
G 6 HOH 98  498 57  HOH HOH A . 
G 6 HOH 99  499 79  HOH HOH A . 
G 6 HOH 100 500 95  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_reference_DOI 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0411 ? 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .        ? 2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .        ? 3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .        ? 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9OWG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     86.425 
_cell.length_a_esd                 ? 
_cell.length_b                     86.425 
_cell.length_b_esd                 ? 
_cell.length_c                     81.853 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        9 
_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                         9OWG 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'H 3' 
_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                   9OWG 
_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             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.2 
_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    
;Protein: 8.5 mg/ml, 0.3M Sodium chloride, 0.01M HEPES (pH 7.5);
Screen: 0.15M Sodium dihydrogen phosphate, 20% (w/v) PEG 3350;
Cryo: glycerol, paratone
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            292 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-12-09 
_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   1.27815 
_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 21-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.27815 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          34.9 
_reflns.entry_id                                       9OWG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.65 
_reflns.d_resolution_low                               30.00 
_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                                     26908 
_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                     -3.0 
_reflns.percent_possible_obs                           98.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          42.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.013 
_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                                0.054 
_reflns.pdbx_Rpim_I_all                                0.017 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.052 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.052 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.65 
_reflns_shell.d_res_low                                     1.68 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1251 
_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                               9.3 
_reflns_shell.pdbx_chi_squared                              1.004 
_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                               0.390 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.660 
_reflns_shell.pdbx_CC_star                                  0.892 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          89.6 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.81 
_refine.aniso_B[1][2]                            0.41 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.81 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -2.63 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               47.336 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.976 
_refine.correlation_coeff_Fo_to_Fc_free          0.964 
_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                                 9OWG 
_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                            1.65 
_refine.ls_d_res_low                             27.62 
_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                     25678 
_refine.ls_number_reflns_R_free                  1226 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.99 
_refine.ls_percent_reflns_R_free                 4.6 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17294 
_refine.ls_R_factor_R_free                       0.20051 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17168 
_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                       0.098 
_refine.pdbx_overall_ESU_R_Free                  0.095 
_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                             5.433 
_refine.overall_SU_ML                            0.086 
_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                       1.65 
_refine_hist.d_res_low                        27.62 
_refine_hist.number_atoms_solvent             100 
_refine_hist.number_atoms_total               1969 
_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        1836 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_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' ? 0.004 0.012  1955 ? r_bond_refined_d             ? ? ? 
'X-RAY DIFFRACTION' ? 0.001 0.016  1820 ? r_bond_other_d               ? ? ? 
'X-RAY DIFFRACTION' ? 1.430 1.649  2663 ? r_angle_refined_deg          ? ? ? 
'X-RAY DIFFRACTION' ? 0.791 1.570  4184 ? r_angle_other_deg            ? ? ? 
'X-RAY DIFFRACTION' ? 3.113 5.000  236  ? r_dihedral_angle_1_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 1.080 5.000  21   ? r_dihedral_angle_2_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 8.035 10.000 309  ? r_dihedral_angle_3_deg       ? ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?    ? r_dihedral_angle_4_deg       ? ? ? 
'X-RAY DIFFRACTION' ? 0.069 0.200  286  ? r_chiral_restr               ? ? ? 
'X-RAY DIFFRACTION' ? 0.008 0.020  2337 ? r_gen_planes_refined         ? ? ? 
'X-RAY DIFFRACTION' ? 0.013 0.020  475  ? 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' ? 2.753 2.786  935  ? r_mcbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 2.753 2.785  935  ? r_mcbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? 3.813 4.985  1174 ? r_mcangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 3.815 4.988  1175 ? r_mcangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 4.422 3.496  1020 ? r_scbond_it                  ? ? ? 
'X-RAY DIFFRACTION' ? 4.376 3.491  1018 ? r_scbond_other               ? ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?    ? r_scangle_it                 ? ? ? 
'X-RAY DIFFRACTION' ? 6.626 6.122  1487 ? r_scangle_other              ? ? ? 
'X-RAY DIFFRACTION' ? 9.893 32.83  2213 ? r_long_range_B_refined       ? ? ? 
'X-RAY DIFFRACTION' ? 9.903 31.76  2193 ? r_long_range_B_other         ? ? ? 
'X-RAY DIFFRACTION' ? ?     ?      ?    ? 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                          1.650 
_refine_ls_shell.d_res_low                           1.693 
_refine_ls_shell.number_reflns_all                   ? 
_refine_ls_shell.number_reflns_obs                   ? 
_refine_ls_shell.number_reflns_R_free                74 
_refine_ls_shell.number_reflns_R_work                1792 
_refine_ls_shell.percent_reflns_obs                  91.16 
_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                     0.328 
_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      20 
_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                     0.315 
# 
_struct.entry_id                     9OWG 
_struct.title                        
'Crystal Structure of the Immunity Protein (52 domain-containing protein) from Pseudomonas aeruginosa PAO1.' 
_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        9OWG 
_struct_keywords.text            
'52 domain-containing protein, CSBID, Structural Genomics, Center for Structural Biology of Infectious Diseases, ANTITOXIN' 
_struct_keywords.pdbx_keywords   ANTITOXIN 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q9HXA5_PSEAE 
_struct_ref.pdbx_db_accession          Q9HXA5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTDAKAFRRYIFELYFDPARLLELDDDQHLQRIERFLDALAPLHPVLENWYLCGDSLRDALSHNVTEHRQDLAKALSRDR
RTRAVELVLWNGEEDPLKGGLSLDYEASGRAVSSRLQLEDAGSLLQVFDAPASSFVAIFLAVLEIWPETTWGMLAPHAYF
VHQRTFPDRRSIGWIGFCPHPLRATDFPAATELVDIPGRGTLLLNGREPMDETRREHFERVGEADIKLMELGYLPPLRG
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9OWG 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 4 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 242 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9HXA5 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  239 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       239 
# 
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 9OWG SER A 1 ? UNP Q9HXA5 ? ? 'expression tag' -2 1 
1 9OWG ASN A 2 ? UNP Q9HXA5 ? ? 'expression tag' -1 2 
1 9OWG ALA A 3 ? UNP Q9HXA5 ? ? 'expression tag' 0  3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 20  ? GLU A 26  ? ASP A 17  GLU A 23  1 ? 7  
HELX_P HELX_P2  AA2 ASP A 28  ? ALA A 44  ? ASP A 25  ALA A 41  1 ? 17 
HELX_P HELX_P3  AA3 PRO A 45  ? GLU A 51  ? PRO A 42  GLU A 48  5 ? 7  
HELX_P HELX_P4  AA4 SER A 59  ? LEU A 64  ? SER A 56  LEU A 61  1 ? 6  
HELX_P HELX_P5  AA5 HIS A 71  ? GLN A 73  ? HIS A 68  GLN A 70  5 ? 3  
HELX_P HELX_P6  AA6 ASP A 74  ? ARG A 83  ? ASP A 71  ARG A 80  1 ? 10 
HELX_P HELX_P7  AA7 ASP A 98  ? GLY A 102 ? ASP A 95  GLY A 99  5 ? 5  
HELX_P HELX_P8  AA8 ARG A 113 ? VAL A 115 ? ARG A 110 VAL A 112 5 ? 3  
HELX_P HELX_P9  AA9 ALA A 124 ? PHE A 131 ? ALA A 121 PHE A 128 1 ? 8  
HELX_P HELX_P10 AB1 ALA A 133 ? TRP A 149 ? ALA A 130 TRP A 146 1 ? 17 
HELX_P HELX_P11 AB2 HIS A 160 ? ARG A 167 ? HIS A 157 ARG A 164 1 ? 8  
HELX_P HELX_P12 AB3 ARG A 186 ? PHE A 190 ? ARG A 183 PHE A 187 5 ? 5  
HELX_P HELX_P13 AB4 GLU A 222 ? LEU A 234 ? GLU A 219 LEU A 231 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLU 
_struct_mon_prot_cis.label_seq_id           122 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLU 
_struct_mon_prot_cis.auth_seq_id            119 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   ASP 
_struct_mon_prot_cis.pdbx_label_seq_id_2    123 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    ASP 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     120 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -6.33 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
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 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 88  ? TRP A 93  ? VAL A 85  TRP A 90  
AA1 2 SER A 105 ? ALA A 110 ? SER A 102 ALA A 107 
AA1 3 SER A 117 ? GLU A 122 ? SER A 114 GLU A 119 
AA1 4 TYR A 13  ? PHE A 19  ? TYR A 10  PHE A 16  
AA1 5 THR A 152 ? PRO A 159 ? THR A 149 PRO A 156 
AA1 6 ILE A 178 ? CYS A 181 ? ILE A 175 CYS A 178 
AA1 7 GLY A 203 ? ASN A 208 ? GLY A 200 ASN A 205 
AA1 8 THR A 194 ? ILE A 199 ? THR A 191 ILE A 196 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 92  ? N LEU A 89  O LEU A 106 ? O LEU A 103 
AA1 2 3 N SER A 105 ? N SER A 102 O GLU A 122 ? O GLU A 119 
AA1 3 4 O LEU A 119 ? O LEU A 116 N LEU A 17  ? N LEU A 14  
AA1 4 5 N ILE A 14  ? N ILE A 11  O ALA A 158 ? O ALA A 155 
AA1 5 6 N LEU A 157 ? N LEU A 154 O ILE A 178 ? O ILE A 175 
AA1 6 7 N CYS A 181 ? N CYS A 178 O THR A 204 ? O THR A 201 
AA1 7 8 O GLY A 203 ? O GLY A 200 N ILE A 199 ? N ILE A 196 
# 
_pdbx_entry_details.entry_id                   9OWG 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 44  ? ? -172.88 143.23 
2 1 ASP A 55  ? ? -73.17  -76.48 
3 1 ARG A 83  ? ? -145.04 21.02  
4 1 ALA A 84  ? ? -171.50 143.97 
5 1 PRO A 179 ? ? -77.15  45.84  
6 1 ARG A 199 ? ? -140.28 -62.61 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Center for Structural Biology of Infectious Diseases' 
_pdbx_SG_project.initial_of_center     CSBID 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 19.8490 28.7240 20.6330 0.0888 ? -0.0742 ? 0.0292  ? 0.2137 ? -0.0846 ? 0.1762 ? 0.5606 ? -1.2799 
? -0.0180 ? 3.0845 ? 0.6758 ? 2.6955 ? 0.0263  ? 0.0351  ? -0.1027 ? -0.0658 ? -0.1453 ? 0.2596 ? 0.1590  ? -0.2125 ? 0.1190  ? 
2 'X-RAY DIFFRACTION' ? refined 15.9350 25.6230 24.8960 0.1852 ? -0.1499 ? 0.1192  ? 0.2375 ? -0.1498 ? 0.2984 ? 1.6307 ? -2.4762 
? 0.1775  ? 3.9306 ? 0.3912 ? 2.8256 ? -0.2284 ? -0.0026 ? -0.3447 ? 0.4711  ? -0.0818 ? 0.5668 ? 0.5612  ? -0.5409 ? 0.3102  ? 
3 'X-RAY DIFFRACTION' ? refined 26.1050 38.9760 27.3300 0.0380 ? -0.0505 ? -0.0011 ? 0.1125 ? -0.0279 ? 0.0802 ? 1.6314 ? -0.1540 
? -1.4991 ? 1.0410 ? 0.2487 ? 3.0544 ? -0.0626 ? 0.0756  ? -0.0577 ? 0.0289  ? -0.0835 ? 0.0258 ? -0.1094 ? 0.0604  ? 0.1461  ? 
4 'X-RAY DIFFRACTION' ? refined 25.9440 49.9230 29.8370 0.1320 ? -0.0753 ? 0.0098  ? 0.0785 ? -0.0151 ? 0.0401 ? 3.0443 ? -0.6748 
? -2.5757 ? 1.9126 ? 1.2786 ? 4.6354 ? 0.2748  ? 0.0264  ? 0.1599  ? -0.0219 ? -0.1537 ? 0.0052 ? -0.6022 ? 0.2582  ? -0.1210 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 4   ? ? ? A 68  ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? A 69  ? ? ? A 119 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? A 120 ? ? ? A 168 ? ? ? 
4 'X-RAY DIFFRACTION' 4 ? ? A 169 ? ? ? A 238 ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER -2  ? A SER 1   
2  1 Y 1 A ASN -1  ? A ASN 2   
3  1 Y 1 A ALA 0   ? A ALA 3   
4  1 Y 1 A MET 1   ? A MET 4   
5  1 Y 1 A THR 2   ? A THR 5   
6  1 Y 1 A ASP 3   ? A ASP 6   
7  1 Y 1 A ASP 211 ? A ASP 214 
8  1 Y 1 A GLU 212 ? A GLU 215 
9  1 Y 1 A THR 213 ? A THR 216 
10 1 Y 1 A ARG 214 ? A ARG 217 
11 1 Y 1 A ARG 215 ? A ARG 218 
12 1 Y 1 A GLU 216 ? A GLU 219 
13 1 Y 1 A HIS 217 ? A HIS 220 
14 1 Y 1 A GLY 239 ? A GLY 242 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CO3 C    C N N 74  
CO3 O1   O N N 75  
CO3 O2   O N N 76  
CO3 O3   O N N 77  
CYS N    N N N 78  
CYS CA   C N R 79  
CYS C    C N N 80  
CYS O    O N N 81  
CYS CB   C N N 82  
CYS SG   S N N 83  
CYS OXT  O N N 84  
CYS H    H N N 85  
CYS H2   H N N 86  
CYS HA   H N N 87  
CYS HB2  H N N 88  
CYS HB3  H N N 89  
CYS HG   H N N 90  
CYS HXT  H N N 91  
EDO C1   C N N 92  
EDO O1   O N N 93  
EDO C2   C N N 94  
EDO O2   O N N 95  
EDO H11  H N N 96  
EDO H12  H N N 97  
EDO HO1  H N N 98  
EDO H21  H N N 99  
EDO H22  H N N 100 
EDO HO2  H N N 101 
EPE N1   N N N 102 
EPE C2   C N N 103 
EPE C3   C N N 104 
EPE N4   N N N 105 
EPE C5   C N N 106 
EPE C6   C N N 107 
EPE C7   C N N 108 
EPE C8   C N N 109 
EPE O8   O N N 110 
EPE C9   C N N 111 
EPE C10  C N N 112 
EPE S    S N N 113 
EPE O1S  O N N 114 
EPE O2S  O N N 115 
EPE O3S  O N N 116 
EPE H21  H N N 117 
EPE H22  H N N 118 
EPE H31  H N N 119 
EPE H32  H N N 120 
EPE H51  H N N 121 
EPE H52  H N N 122 
EPE H61  H N N 123 
EPE H62  H N N 124 
EPE H71  H N N 125 
EPE H72  H N N 126 
EPE H81  H N N 127 
EPE H82  H N N 128 
EPE HO8  H N N 129 
EPE H91  H N N 130 
EPE H92  H N N 131 
EPE H101 H N N 132 
EPE H102 H N N 133 
EPE HOS3 H N N 134 
GLN N    N N N 135 
GLN CA   C N S 136 
GLN C    C N N 137 
GLN O    O N N 138 
GLN CB   C N N 139 
GLN CG   C N N 140 
GLN CD   C N N 141 
GLN OE1  O N N 142 
GLN NE2  N N N 143 
GLN OXT  O N N 144 
GLN H    H N N 145 
GLN H2   H N N 146 
GLN HA   H N N 147 
GLN HB2  H N N 148 
GLN HB3  H N N 149 
GLN HG2  H N N 150 
GLN HG3  H N N 151 
GLN HE21 H N N 152 
GLN HE22 H N N 153 
GLN HXT  H N N 154 
GLU N    N N N 155 
GLU CA   C N S 156 
GLU C    C N N 157 
GLU O    O N N 158 
GLU CB   C N N 159 
GLU CG   C N N 160 
GLU CD   C N N 161 
GLU OE1  O N N 162 
GLU OE2  O N N 163 
GLU OXT  O N N 164 
GLU H    H N N 165 
GLU H2   H N N 166 
GLU HA   H N N 167 
GLU HB2  H N N 168 
GLU HB3  H N N 169 
GLU HG2  H N N 170 
GLU HG3  H N N 171 
GLU HE2  H N N 172 
GLU HXT  H N N 173 
GLY N    N N N 174 
GLY CA   C N N 175 
GLY C    C N N 176 
GLY O    O N N 177 
GLY OXT  O N N 178 
GLY H    H N N 179 
GLY H2   H N N 180 
GLY HA2  H N N 181 
GLY HA3  H N N 182 
GLY HXT  H N N 183 
HIS N    N N N 184 
HIS CA   C N S 185 
HIS C    C N N 186 
HIS O    O N N 187 
HIS CB   C N N 188 
HIS CG   C Y N 189 
HIS ND1  N Y N 190 
HIS CD2  C Y N 191 
HIS CE1  C Y N 192 
HIS NE2  N Y N 193 
HIS OXT  O N N 194 
HIS H    H N N 195 
HIS H2   H N N 196 
HIS HA   H N N 197 
HIS HB2  H N N 198 
HIS HB3  H N N 199 
HIS HD1  H N N 200 
HIS HD2  H N N 201 
HIS HE1  H N N 202 
HIS HE2  H N N 203 
HIS HXT  H N N 204 
HOH O    O N N 205 
HOH H1   H N N 206 
HOH H2   H N N 207 
ILE N    N N N 208 
ILE CA   C N S 209 
ILE C    C N N 210 
ILE O    O N N 211 
ILE CB   C N S 212 
ILE CG1  C N N 213 
ILE CG2  C N N 214 
ILE CD1  C N N 215 
ILE OXT  O N N 216 
ILE H    H N N 217 
ILE H2   H N N 218 
ILE HA   H N N 219 
ILE HB   H N N 220 
ILE HG12 H N N 221 
ILE HG13 H N N 222 
ILE HG21 H N N 223 
ILE HG22 H N N 224 
ILE HG23 H N N 225 
ILE HD11 H N N 226 
ILE HD12 H N N 227 
ILE HD13 H N N 228 
ILE HXT  H N N 229 
LEU N    N N N 230 
LEU CA   C N S 231 
LEU C    C N N 232 
LEU O    O N N 233 
LEU CB   C N N 234 
LEU CG   C N N 235 
LEU CD1  C N N 236 
LEU CD2  C N N 237 
LEU OXT  O N N 238 
LEU H    H N N 239 
LEU H2   H N N 240 
LEU HA   H N N 241 
LEU HB2  H N N 242 
LEU HB3  H N N 243 
LEU HG   H N N 244 
LEU HD11 H N N 245 
LEU HD12 H N N 246 
LEU HD13 H N N 247 
LEU HD21 H N N 248 
LEU HD22 H N N 249 
LEU HD23 H N N 250 
LEU HXT  H N N 251 
LYS N    N N N 252 
LYS CA   C N S 253 
LYS C    C N N 254 
LYS O    O N N 255 
LYS CB   C N N 256 
LYS CG   C N N 257 
LYS CD   C N N 258 
LYS CE   C N N 259 
LYS NZ   N N N 260 
LYS OXT  O N N 261 
LYS H    H N N 262 
LYS H2   H N N 263 
LYS HA   H N N 264 
LYS HB2  H N N 265 
LYS HB3  H N N 266 
LYS HG2  H N N 267 
LYS HG3  H N N 268 
LYS HD2  H N N 269 
LYS HD3  H N N 270 
LYS HE2  H N N 271 
LYS HE3  H N N 272 
LYS HZ1  H N N 273 
LYS HZ2  H N N 274 
LYS HZ3  H N N 275 
LYS HXT  H N N 276 
MET N    N N N 277 
MET CA   C N S 278 
MET C    C N N 279 
MET O    O N N 280 
MET CB   C N N 281 
MET CG   C N N 282 
MET SD   S N N 283 
MET CE   C N N 284 
MET OXT  O N N 285 
MET H    H N N 286 
MET H2   H N N 287 
MET HA   H N N 288 
MET HB2  H N N 289 
MET HB3  H N N 290 
MET HG2  H N N 291 
MET HG3  H N N 292 
MET HE1  H N N 293 
MET HE2  H N N 294 
MET HE3  H N N 295 
MET HXT  H N N 296 
PHE N    N N N 297 
PHE CA   C N S 298 
PHE C    C N N 299 
PHE O    O N N 300 
PHE CB   C N N 301 
PHE CG   C Y N 302 
PHE CD1  C Y N 303 
PHE CD2  C Y N 304 
PHE CE1  C Y N 305 
PHE CE2  C Y N 306 
PHE CZ   C Y N 307 
PHE OXT  O N N 308 
PHE H    H N N 309 
PHE H2   H N N 310 
PHE HA   H N N 311 
PHE HB2  H N N 312 
PHE HB3  H N N 313 
PHE HD1  H N N 314 
PHE HD2  H N N 315 
PHE HE1  H N N 316 
PHE HE2  H N N 317 
PHE HZ   H N N 318 
PHE HXT  H N N 319 
PO4 P    P N N 320 
PO4 O1   O N N 321 
PO4 O2   O N N 322 
PO4 O3   O N N 323 
PO4 O4   O 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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CO3 C   O1   doub N N 70  
CO3 C   O2   sing N N 71  
CO3 C   O3   sing N N 72  
CYS N   CA   sing N N 73  
CYS N   H    sing N N 74  
CYS N   H2   sing N N 75  
CYS CA  C    sing N N 76  
CYS CA  CB   sing N N 77  
CYS CA  HA   sing N N 78  
CYS C   O    doub N N 79  
CYS C   OXT  sing N N 80  
CYS CB  SG   sing N N 81  
CYS CB  HB2  sing N N 82  
CYS CB  HB3  sing N N 83  
CYS SG  HG   sing N N 84  
CYS OXT HXT  sing N N 85  
EDO C1  O1   sing N N 86  
EDO C1  C2   sing N N 87  
EDO C1  H11  sing N N 88  
EDO C1  H12  sing N N 89  
EDO O1  HO1  sing N N 90  
EDO C2  O2   sing N N 91  
EDO C2  H21  sing N N 92  
EDO C2  H22  sing N N 93  
EDO O2  HO2  sing N N 94  
EPE N1  C2   sing N N 95  
EPE N1  C6   sing N N 96  
EPE N1  C9   sing N N 97  
EPE C2  C3   sing N N 98  
EPE C2  H21  sing N N 99  
EPE C2  H22  sing N N 100 
EPE C3  N4   sing N N 101 
EPE C3  H31  sing N N 102 
EPE C3  H32  sing N N 103 
EPE N4  C5   sing N N 104 
EPE N4  C7   sing N N 105 
EPE C5  C6   sing N N 106 
EPE C5  H51  sing N N 107 
EPE C5  H52  sing N N 108 
EPE C6  H61  sing N N 109 
EPE C6  H62  sing N N 110 
EPE C7  C8   sing N N 111 
EPE C7  H71  sing N N 112 
EPE C7  H72  sing N N 113 
EPE C8  O8   sing N N 114 
EPE C8  H81  sing N N 115 
EPE C8  H82  sing N N 116 
EPE O8  HO8  sing N N 117 
EPE C9  C10  sing N N 118 
EPE C9  H91  sing N N 119 
EPE C9  H92  sing N N 120 
EPE C10 S    sing N N 121 
EPE C10 H101 sing N N 122 
EPE C10 H102 sing N N 123 
EPE S   O1S  doub N N 124 
EPE S   O2S  doub N N 125 
EPE S   O3S  sing N N 126 
EPE O3S HOS3 sing N N 127 
GLN N   CA   sing N N 128 
GLN N   H    sing N N 129 
GLN N   H2   sing N N 130 
GLN CA  C    sing N N 131 
GLN CA  CB   sing N N 132 
GLN CA  HA   sing N N 133 
GLN C   O    doub N N 134 
GLN C   OXT  sing N N 135 
GLN CB  CG   sing N N 136 
GLN CB  HB2  sing N N 137 
GLN CB  HB3  sing N N 138 
GLN CG  CD   sing N N 139 
GLN CG  HG2  sing N N 140 
GLN CG  HG3  sing N N 141 
GLN CD  OE1  doub N N 142 
GLN CD  NE2  sing N N 143 
GLN NE2 HE21 sing N N 144 
GLN NE2 HE22 sing N N 145 
GLN OXT HXT  sing N N 146 
GLU N   CA   sing N N 147 
GLU N   H    sing N N 148 
GLU N   H2   sing N N 149 
GLU CA  C    sing N N 150 
GLU CA  CB   sing N N 151 
GLU CA  HA   sing N N 152 
GLU C   O    doub N N 153 
GLU C   OXT  sing N N 154 
GLU CB  CG   sing N N 155 
GLU CB  HB2  sing N N 156 
GLU CB  HB3  sing N N 157 
GLU CG  CD   sing N N 158 
GLU CG  HG2  sing N N 159 
GLU CG  HG3  sing N N 160 
GLU CD  OE1  doub N N 161 
GLU CD  OE2  sing N N 162 
GLU OE2 HE2  sing N N 163 
GLU OXT HXT  sing N N 164 
GLY N   CA   sing N N 165 
GLY N   H    sing N N 166 
GLY N   H2   sing N N 167 
GLY CA  C    sing N N 168 
GLY CA  HA2  sing N N 169 
GLY CA  HA3  sing N N 170 
GLY C   O    doub N N 171 
GLY C   OXT  sing N N 172 
GLY OXT HXT  sing N N 173 
HIS N   CA   sing N N 174 
HIS N   H    sing N N 175 
HIS N   H2   sing N N 176 
HIS CA  C    sing N N 177 
HIS CA  CB   sing N N 178 
HIS CA  HA   sing N N 179 
HIS C   O    doub N N 180 
HIS C   OXT  sing N N 181 
HIS CB  CG   sing N N 182 
HIS CB  HB2  sing N N 183 
HIS CB  HB3  sing N N 184 
HIS CG  ND1  sing Y N 185 
HIS CG  CD2  doub Y N 186 
HIS ND1 CE1  doub Y N 187 
HIS ND1 HD1  sing N N 188 
HIS CD2 NE2  sing Y N 189 
HIS CD2 HD2  sing N N 190 
HIS CE1 NE2  sing Y N 191 
HIS CE1 HE1  sing N N 192 
HIS NE2 HE2  sing N N 193 
HIS OXT HXT  sing N N 194 
HOH O   H1   sing N N 195 
HOH O   H2   sing N N 196 
ILE N   CA   sing N N 197 
ILE N   H    sing N N 198 
ILE N   H2   sing N N 199 
ILE CA  C    sing N N 200 
ILE CA  CB   sing N N 201 
ILE CA  HA   sing N N 202 
ILE C   O    doub N N 203 
ILE C   OXT  sing N N 204 
ILE CB  CG1  sing N N 205 
ILE CB  CG2  sing N N 206 
ILE CB  HB   sing N N 207 
ILE CG1 CD1  sing N N 208 
ILE CG1 HG12 sing N N 209 
ILE CG1 HG13 sing N N 210 
ILE CG2 HG21 sing N N 211 
ILE CG2 HG22 sing N N 212 
ILE CG2 HG23 sing N N 213 
ILE CD1 HD11 sing N N 214 
ILE CD1 HD12 sing N N 215 
ILE CD1 HD13 sing N N 216 
ILE OXT HXT  sing N N 217 
LEU N   CA   sing N N 218 
LEU N   H    sing N N 219 
LEU N   H2   sing N N 220 
LEU CA  C    sing N N 221 
LEU CA  CB   sing N N 222 
LEU CA  HA   sing N N 223 
LEU C   O    doub N N 224 
LEU C   OXT  sing N N 225 
LEU CB  CG   sing N N 226 
LEU CB  HB2  sing N N 227 
LEU CB  HB3  sing N N 228 
LEU CG  CD1  sing N N 229 
LEU CG  CD2  sing N N 230 
LEU CG  HG   sing N N 231 
LEU CD1 HD11 sing N N 232 
LEU CD1 HD12 sing N N 233 
LEU CD1 HD13 sing N N 234 
LEU CD2 HD21 sing N N 235 
LEU CD2 HD22 sing N N 236 
LEU CD2 HD23 sing N N 237 
LEU OXT HXT  sing N N 238 
LYS N   CA   sing N N 239 
LYS N   H    sing N N 240 
LYS N   H2   sing N N 241 
LYS CA  C    sing N N 242 
LYS CA  CB   sing N N 243 
LYS CA  HA   sing N N 244 
LYS C   O    doub N N 245 
LYS C   OXT  sing N N 246 
LYS CB  CG   sing N N 247 
LYS CB  HB2  sing N N 248 
LYS CB  HB3  sing N N 249 
LYS CG  CD   sing N N 250 
LYS CG  HG2  sing N N 251 
LYS CG  HG3  sing N N 252 
LYS CD  CE   sing N N 253 
LYS CD  HD2  sing N N 254 
LYS CD  HD3  sing N N 255 
LYS CE  NZ   sing N N 256 
LYS CE  HE2  sing N N 257 
LYS CE  HE3  sing N N 258 
LYS NZ  HZ1  sing N N 259 
LYS NZ  HZ2  sing N N 260 
LYS NZ  HZ3  sing N N 261 
LYS OXT HXT  sing N N 262 
MET N   CA   sing N N 263 
MET N   H    sing N N 264 
MET N   H2   sing N N 265 
MET CA  C    sing N N 266 
MET CA  CB   sing N N 267 
MET CA  HA   sing N N 268 
MET C   O    doub N N 269 
MET C   OXT  sing N N 270 
MET CB  CG   sing N N 271 
MET CB  HB2  sing N N 272 
MET CB  HB3  sing N N 273 
MET CG  SD   sing N N 274 
MET CG  HG2  sing N N 275 
MET CG  HG3  sing N N 276 
MET SD  CE   sing N N 277 
MET CE  HE1  sing N N 278 
MET CE  HE2  sing N N 279 
MET CE  HE3  sing N N 280 
MET OXT HXT  sing N N 281 
PHE N   CA   sing N N 282 
PHE N   H    sing N N 283 
PHE N   H2   sing N N 284 
PHE CA  C    sing N N 285 
PHE CA  CB   sing N N 286 
PHE CA  HA   sing N N 287 
PHE C   O    doub N N 288 
PHE C   OXT  sing N N 289 
PHE CB  CG   sing N N 290 
PHE CB  HB2  sing N N 291 
PHE CB  HB3  sing N N 292 
PHE CG  CD1  doub Y N 293 
PHE CG  CD2  sing Y N 294 
PHE CD1 CE1  sing Y N 295 
PHE CD1 HD1  sing N N 296 
PHE CD2 CE2  doub Y N 297 
PHE CD2 HD2  sing N N 298 
PHE CE1 CZ   doub Y N 299 
PHE CE1 HE1  sing N N 300 
PHE CE2 CZ   sing Y N 301 
PHE CE2 HE2  sing N N 302 
PHE CZ  HZ   sing N N 303 
PHE OXT HXT  sing N N 304 
PO4 P   O1   doub N N 305 
PO4 P   O2   sing N N 306 
PO4 P   O3   sing N N 307 
PO4 P   O4   sing N N 308 
PRO N   CA   sing N N 309 
PRO N   CD   sing N N 310 
PRO N   H    sing N N 311 
PRO CA  C    sing N N 312 
PRO CA  CB   sing N N 313 
PRO CA  HA   sing N N 314 
PRO C   O    doub N N 315 
PRO C   OXT  sing N N 316 
PRO CB  CG   sing N N 317 
PRO CB  HB2  sing N N 318 
PRO CB  HB3  sing N N 319 
PRO CG  CD   sing N N 320 
PRO CG  HG2  sing N N 321 
PRO CG  HG3  sing N N 322 
PRO CD  HD2  sing N N 323 
PRO CD  HD3  sing N N 324 
PRO OXT HXT  sing N N 325 
SER N   CA   sing N N 326 
SER N   H    sing N N 327 
SER N   H2   sing N N 328 
SER CA  C    sing N N 329 
SER CA  CB   sing N N 330 
SER CA  HA   sing N N 331 
SER C   O    doub N N 332 
SER C   OXT  sing N N 333 
SER CB  OG   sing N N 334 
SER CB  HB2  sing N N 335 
SER CB  HB3  sing N N 336 
SER OG  HG   sing N N 337 
SER OXT HXT  sing N N 338 
THR N   CA   sing N N 339 
THR N   H    sing N N 340 
THR N   H2   sing N N 341 
THR CA  C    sing N N 342 
THR CA  CB   sing N N 343 
THR CA  HA   sing N N 344 
THR C   O    doub N N 345 
THR C   OXT  sing N N 346 
THR CB  OG1  sing N N 347 
THR CB  CG2  sing N N 348 
THR CB  HB   sing N N 349 
THR OG1 HG1  sing N N 350 
THR CG2 HG21 sing N N 351 
THR CG2 HG22 sing N N 352 
THR CG2 HG23 sing N N 353 
THR OXT HXT  sing N N 354 
TRP N   CA   sing N N 355 
TRP N   H    sing N N 356 
TRP N   H2   sing N N 357 
TRP CA  C    sing N N 358 
TRP CA  CB   sing N N 359 
TRP CA  HA   sing N N 360 
TRP C   O    doub N N 361 
TRP C   OXT  sing N N 362 
TRP CB  CG   sing N N 363 
TRP CB  HB2  sing N N 364 
TRP CB  HB3  sing N N 365 
TRP CG  CD1  doub Y N 366 
TRP CG  CD2  sing Y N 367 
TRP CD1 NE1  sing Y N 368 
TRP CD1 HD1  sing N N 369 
TRP CD2 CE2  doub Y N 370 
TRP CD2 CE3  sing Y N 371 
TRP NE1 CE2  sing Y N 372 
TRP NE1 HE1  sing N N 373 
TRP CE2 CZ2  sing Y N 374 
TRP CE3 CZ3  doub Y N 375 
TRP CE3 HE3  sing N N 376 
TRP CZ2 CH2  doub Y N 377 
TRP CZ2 HZ2  sing N N 378 
TRP CZ3 CH2  sing Y N 379 
TRP CZ3 HZ3  sing N N 380 
TRP CH2 HH2  sing N N 381 
TRP OXT HXT  sing N N 382 
TYR N   CA   sing N N 383 
TYR N   H    sing N N 384 
TYR N   H2   sing N N 385 
TYR CA  C    sing N N 386 
TYR CA  CB   sing N N 387 
TYR CA  HA   sing N N 388 
TYR C   O    doub N N 389 
TYR C   OXT  sing N N 390 
TYR CB  CG   sing N N 391 
TYR CB  HB2  sing N N 392 
TYR CB  HB3  sing N N 393 
TYR CG  CD1  doub Y N 394 
TYR CG  CD2  sing Y N 395 
TYR CD1 CE1  sing Y N 396 
TYR CD1 HD1  sing N N 397 
TYR CD2 CE2  doub Y N 398 
TYR CD2 HD2  sing N N 399 
TYR CE1 CZ   doub Y N 400 
TYR CE1 HE1  sing N N 401 
TYR CE2 CZ   sing Y N 402 
TYR CE2 HE2  sing N N 403 
TYR CZ  OH   sing N N 404 
TYR OH  HH   sing N N 405 
TYR OXT HXT  sing N N 406 
VAL N   CA   sing N N 407 
VAL N   H    sing N N 408 
VAL N   H2   sing N N 409 
VAL CA  C    sing N N 410 
VAL CA  CB   sing N N 411 
VAL CA  HA   sing N N 412 
VAL C   O    doub N N 413 
VAL C   OXT  sing N N 414 
VAL CB  CG1  sing N N 415 
VAL CB  CG2  sing N N 416 
VAL CB  HB   sing N N 417 
VAL CG1 HG11 sing N N 418 
VAL CG1 HG12 sing N N 419 
VAL CG1 HG13 sing N N 420 
VAL CG2 HG21 sing N N 421 
VAL CG2 HG22 sing N N 422 
VAL CG2 HG23 sing N N 423 
VAL OXT HXT  sing N N 424 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           75N93022C00035 
_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   4RHO 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9OWG 
_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]   0.011571 
_atom_sites.fract_transf_matrix[1][2]   0.006680 
_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]   0.013361 
_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]   0.012217 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ALA A 1 7   ? 47.216 37.453 34.744 1.00 96.09  ? 4   ALA A N   1 
ATOM   2    C CA  . ALA A 1 7   ? 46.398 37.614 33.518 1.00 96.70  ? 4   ALA A CA  1 
ATOM   3    C C   . ALA A 1 7   ? 45.822 36.263 33.098 1.00 94.32  ? 4   ALA A C   1 
ATOM   4    O O   . ALA A 1 7   ? 46.549 35.397 32.619 1.00 101.27 ? 4   ALA A O   1 
ATOM   5    C CB  . ALA A 1 7   ? 47.239 38.218 32.418 1.00 98.04  ? 4   ALA A CB  1 
ATOM   6    N N   . LYS A 1 8   ? 44.512 36.086 33.302 1.00 89.14  ? 5   LYS A N   1 
ATOM   7    C CA  . LYS A 1 8   ? 43.838 34.851 32.931 1.00 87.60  ? 5   LYS A CA  1 
ATOM   8    C C   . LYS A 1 8   ? 42.344 35.141 32.805 1.00 82.54  ? 5   LYS A C   1 
ATOM   9    O O   . LYS A 1 8   ? 41.742 35.748 33.691 1.00 77.12  ? 5   LYS A O   1 
ATOM   10   C CB  . LYS A 1 8   ? 44.149 33.741 33.939 1.00 94.04  ? 5   LYS A CB  1 
ATOM   11   C CG  . LYS A 1 8   ? 43.523 32.388 33.625 1.00 94.85  ? 5   LYS A CG  1 
ATOM   12   C CD  . LYS A 1 8   ? 43.924 31.291 34.591 1.00 102.14 ? 5   LYS A CD  1 
ATOM   13   C CE  . LYS A 1 8   ? 45.415 31.023 34.599 1.00 105.21 ? 5   LYS A CE  1 
ATOM   14   N NZ  . LYS A 1 8   ? 45.777 29.936 35.540 1.00 107.65 ? 5   LYS A NZ  1 
ATOM   15   N N   . ALA A 1 9   ? 41.760 34.700 31.686 1.00 74.33  ? 6   ALA A N   1 
ATOM   16   C CA  . ALA A 1 9   ? 40.360 34.960 31.398 1.00 76.04  ? 6   ALA A CA  1 
ATOM   17   C C   . ALA A 1 9   ? 39.451 34.222 32.375 1.00 71.94  ? 6   ALA A C   1 
ATOM   18   O O   . ALA A 1 9   ? 39.860 33.243 32.996 1.00 67.72  ? 6   ALA A O   1 
ATOM   19   C CB  . ALA A 1 9   ? 40.058 34.563 29.971 1.00 77.97  ? 6   ALA A CB  1 
ATOM   20   N N   . PHE A 1 10  ? 38.228 34.747 32.531 1.00 66.17  ? 7   PHE A N   1 
ATOM   21   C CA  . PHE A 1 10  ? 37.219 34.110 33.359 1.00 62.48  ? 7   PHE A CA  1 
ATOM   22   C C   . PHE A 1 10  ? 36.594 32.990 32.540 1.00 55.99  ? 7   PHE A C   1 
ATOM   23   O O   . PHE A 1 10  ? 36.233 33.183 31.383 1.00 51.37  ? 7   PHE A O   1 
ATOM   24   C CB  . PHE A 1 10  ? 36.142 35.095 33.818 1.00 63.00  ? 7   PHE A CB  1 
ATOM   25   C CG  . PHE A 1 10  ? 36.603 36.122 34.817 1.00 68.85  ? 7   PHE A CG  1 
ATOM   26   C CD1 . PHE A 1 10  ? 37.004 35.740 36.090 1.00 76.23  ? 7   PHE A CD1 1 
ATOM   27   C CD2 . PHE A 1 10  ? 36.673 37.463 34.476 1.00 69.95  ? 7   PHE A CD2 1 
ATOM   28   C CE1 . PHE A 1 10  ? 37.432 36.683 37.012 1.00 79.14  ? 7   PHE A CE1 1 
ATOM   29   C CE2 . PHE A 1 10  ? 37.102 38.403 35.397 1.00 73.33  ? 7   PHE A CE2 1 
ATOM   30   C CZ  . PHE A 1 10  ? 37.483 38.013 36.663 1.00 79.58  ? 7   PHE A CZ  1 
ATOM   31   N N   . ARG A 1 11  ? 36.485 31.818 33.154 1.00 54.31  ? 8   ARG A N   1 
ATOM   32   C CA  . ARG A 1 11  ? 35.907 30.682 32.473 1.00 49.82  ? 8   ARG A CA  1 
ATOM   33   C C   . ARG A 1 11  ? 34.403 30.874 32.300 1.00 43.64  ? 8   ARG A C   1 
ATOM   34   O O   . ARG A 1 11  ? 33.930 30.898 31.172 1.00 45.57  ? 8   ARG A O   1 
ATOM   35   C CB  . ARG A 1 11  ? 36.195 29.386 33.240 1.00 59.74  ? 8   ARG A CB  1 
ATOM   36   C CG  . ARG A 1 11  ? 37.625 28.880 33.141 1.00 70.51  ? 8   ARG A CG  1 
ATOM   37   C CD  . ARG A 1 11  ? 37.941 28.418 31.726 1.00 77.42  ? 8   ARG A CD  1 
ATOM   38   N NE  . ARG A 1 11  ? 39.269 27.827 31.603 1.00 91.57  ? 8   ARG A NE  1 
ATOM   39   C CZ  . ARG A 1 11  ? 40.219 28.238 30.768 1.00 97.64  ? 8   ARG A CZ  1 
ATOM   40   N NH1 . ARG A 1 11  ? 41.383 27.613 30.738 1.00 98.19  ? 8   ARG A NH1 1 
ATOM   41   N NH2 . ARG A 1 11  ? 40.003 29.259 29.957 1.00 101.96 ? 8   ARG A NH2 1 
ATOM   42   N N   . ARG A 1 12  ? 33.675 31.058 33.409 1.00 38.20  ? 9   ARG A N   1 
ATOM   43   C CA  . ARG A 1 12  ? 32.222 31.105 33.324 1.00 39.01  ? 9   ARG A CA  1 
ATOM   44   C C   . ARG A 1 12  ? 31.685 32.504 33.045 1.00 34.82  ? 9   ARG A C   1 
ATOM   45   O O   . ARG A 1 12  ? 32.053 33.468 33.719 1.00 36.72  ? 9   ARG A O   1 
ATOM   46   C CB  . ARG A 1 12  ? 31.576 30.642 34.632 1.00 41.68  ? 9   ARG A CB  1 
ATOM   47   C CG  . ARG A 1 12  ? 31.912 29.221 35.052 1.00 50.36  ? 9   ARG A CG  1 
ATOM   48   C CD  . ARG A 1 12  ? 31.258 28.904 36.388 1.00 56.72  ? 9   ARG A CD  1 
ATOM   49   N NE  . ARG A 1 12  ? 29.801 28.963 36.341 1.00 63.56  ? 9   ARG A NE  1 
ATOM   50   C CZ  . ARG A 1 12  ? 29.006 28.816 37.398 1.00 65.58  ? 9   ARG A CZ  1 
ATOM   51   N NH1 . ARG A 1 12  ? 29.530 28.673 38.602 1.00 66.03  ? 9   ARG A NH1 1 
ATOM   52   N NH2 . ARG A 1 12  ? 27.693 28.868 37.256 1.00 66.50  ? 9   ARG A NH2 1 
ATOM   53   N N   . TYR A 1 13  ? 30.780 32.566 32.056 1.00 35.27  ? 10  TYR A N   1 
ATOM   54   C CA  . TYR A 1 13  ? 30.070 33.787 31.712 1.00 34.63  ? 10  TYR A CA  1 
ATOM   55   C C   . TYR A 1 13  ? 28.569 33.550 31.667 1.00 38.59  ? 10  TYR A C   1 
ATOM   56   O O   . TYR A 1 13  ? 28.097 32.460 31.334 1.00 39.64  ? 10  TYR A O   1 
ATOM   57   C CB  . TYR A 1 13  ? 30.448 34.396 30.358 1.00 34.45  ? 10  TYR A CB  1 
ATOM   58   C CG  . TYR A 1 13  ? 31.673 35.258 30.328 1.00 34.21  ? 10  TYR A CG  1 
ATOM   59   C CD1 . TYR A 1 13  ? 32.932 34.773 30.620 1.00 38.61  ? 10  TYR A CD1 1 
ATOM   60   C CD2 . TYR A 1 13  ? 31.547 36.612 30.063 1.00 36.21  ? 10  TYR A CD2 1 
ATOM   61   C CE1 . TYR A 1 13  ? 34.037 35.602 30.600 1.00 39.67  ? 10  TYR A CE1 1 
ATOM   62   C CE2 . TYR A 1 13  ? 32.637 37.452 30.044 1.00 39.01  ? 10  TYR A CE2 1 
ATOM   63   C CZ  . TYR A 1 13  ? 33.891 36.948 30.316 1.00 39.74  ? 10  TYR A CZ  1 
ATOM   64   O OH  . TYR A 1 13  ? 34.966 37.789 30.305 1.00 45.64  ? 10  TYR A OH  1 
ATOM   65   N N   . ILE A 1 14  ? 27.842 34.609 32.028 1.00 33.75  ? 11  ILE A N   1 
ATOM   66   C CA  . ILE A 1 14  ? 26.393 34.648 31.944 1.00 33.39  ? 11  ILE A CA  1 
ATOM   67   C C   . ILE A 1 14  ? 26.074 35.394 30.655 1.00 34.06  ? 11  ILE A C   1 
ATOM   68   O O   . ILE A 1 14  ? 26.688 36.421 30.382 1.00 34.36  ? 11  ILE A O   1 
ATOM   69   C CB  . ILE A 1 14  ? 25.771 35.359 33.159 1.00 32.49  ? 11  ILE A CB  1 
ATOM   70   C CG1 . ILE A 1 14  ? 26.133 34.668 34.473 1.00 34.89  ? 11  ILE A CG1 1 
ATOM   71   C CG2 . ILE A 1 14  ? 24.260 35.497 32.986 1.00 34.84  ? 11  ILE A CG2 1 
ATOM   72   C CD1 . ILE A 1 14  ? 25.755 35.446 35.711 1.00 37.97  ? 11  ILE A CD1 1 
ATOM   73   N N   . PHE A 1 15  ? 25.135 34.863 29.861 1.00 33.10  ? 12  PHE A N   1 
ATOM   74   C CA  . PHE A 1 15  ? 24.739 35.498 28.615 1.00 33.75  ? 12  PHE A CA  1 
ATOM   75   C C   . PHE A 1 15  ? 23.222 35.364 28.542 1.00 32.36  ? 12  PHE A C   1 
ATOM   76   O O   . PHE A 1 15  ? 22.701 34.295 28.261 1.00 33.75  ? 12  PHE A O   1 
ATOM   77   C CB  . PHE A 1 15  ? 25.412 34.841 27.408 1.00 35.19  ? 12  PHE A CB  1 
ATOM   78   C CG  . PHE A 1 15  ? 25.306 35.591 26.103 1.00 33.17  ? 12  PHE A CG  1 
ATOM   79   C CD1 . PHE A 1 15  ? 24.704 36.838 26.026 1.00 35.90  ? 12  PHE A CD1 1 
ATOM   80   C CD2 . PHE A 1 15  ? 25.878 35.073 24.953 1.00 38.46  ? 12  PHE A CD2 1 
ATOM   81   C CE1 . PHE A 1 15  ? 24.669 37.542 24.833 1.00 38.23  ? 12  PHE A CE1 1 
ATOM   82   C CE2 . PHE A 1 15  ? 25.816 35.767 23.752 1.00 43.73  ? 12  PHE A CE2 1 
ATOM   83   C CZ  . PHE A 1 15  ? 25.203 37.002 23.697 1.00 39.45  ? 12  PHE A CZ  1 
ATOM   84   N N   . GLU A 1 16  ? 22.520 36.442 28.875 1.00 32.12  ? 13  GLU A N   1 
ATOM   85   C CA  . GLU A 1 16  ? 21.075 36.380 28.928 1.00 31.91  ? 13  GLU A CA  1 
ATOM   86   C C   . GLU A 1 16  ? 20.444 37.620 28.320 1.00 33.80  ? 13  GLU A C   1 
ATOM   87   O O   . GLU A 1 16  ? 20.926 38.731 28.517 1.00 29.75  ? 13  GLU A O   1 
ATOM   88   C CB  . GLU A 1 16  ? 20.570 36.382 30.372 1.00 39.75  ? 13  GLU A CB  1 
ATOM   89   C CG  . GLU A 1 16  ? 20.999 35.207 31.218 1.00 53.64  ? 13  GLU A CG  1 
ATOM   90   C CD  . GLU A 1 16  ? 20.336 35.218 32.588 1.00 62.95  ? 13  GLU A CD  1 
ATOM   91   O OE1 . GLU A 1 16  ? 19.084 35.144 32.636 1.00 67.89  ? 13  GLU A OE1 1 
ATOM   92   O OE2 . GLU A 1 16  ? 21.058 35.322 33.598 1.00 75.80  ? 13  GLU A OE2 1 
ATOM   93   N N   . LEU A 1 17  ? 19.322 37.408 27.633 1.00 33.41  ? 14  LEU A N   1 
ATOM   94   C CA  . LEU A 1 17  ? 18.561 38.516 27.101 1.00 34.14  ? 14  LEU A CA  1 
ATOM   95   C C   . LEU A 1 17  ? 17.130 38.339 27.575 1.00 33.29  ? 14  LEU A C   1 
ATOM   96   O O   . LEU A 1 17  ? 16.614 37.221 27.605 1.00 35.49  ? 14  LEU A O   1 
ATOM   97   C CB  . LEU A 1 17  ? 18.662 38.611 25.584 1.00 39.01  ? 14  LEU A CB  1 
ATOM   98   C CG  . LEU A 1 17  ? 20.091 38.792 25.082 1.00 42.43  ? 14  LEU A CG  1 
ATOM   99   C CD1 . LEU A 1 17  ? 20.701 37.436 24.761 1.00 41.83  ? 14  LEU A CD1 1 
ATOM   100  C CD2 . LEU A 1 17  ? 20.151 39.767 23.924 1.00 50.48  ? 14  LEU A CD2 1 
ATOM   101  N N   . TYR A 1 18  ? 16.539 39.460 27.992 1.00 33.38  ? 15  TYR A N   1 
ATOM   102  C CA  . TYR A 1 18  ? 15.191 39.483 28.522 1.00 34.93  ? 15  TYR A CA  1 
ATOM   103  C C   . TYR A 1 18  ? 14.251 40.160 27.537 1.00 34.63  ? 15  TYR A C   1 
ATOM   104  O O   . TYR A 1 18  ? 14.627 41.135 26.896 1.00 35.45  ? 15  TYR A O   1 
ATOM   105  C CB  . TYR A 1 18  ? 15.116 40.243 29.849 1.00 36.27  ? 15  TYR A CB  1 
ATOM   106  C CG  . TYR A 1 18  ? 15.967 39.663 30.945 1.00 37.16  ? 15  TYR A CG  1 
ATOM   107  C CD1 . TYR A 1 18  ? 17.336 39.868 30.994 1.00 38.88  ? 15  TYR A CD1 1 
ATOM   108  C CD2 . TYR A 1 18  ? 15.408 38.759 31.829 1.00 41.24  ? 15  TYR A CD2 1 
ATOM   109  C CE1 . TYR A 1 18  ? 18.108 39.289 31.992 1.00 41.00  ? 15  TYR A CE1 1 
ATOM   110  C CE2 . TYR A 1 18  ? 16.166 38.154 32.816 1.00 46.07  ? 15  TYR A CE2 1 
ATOM   111  C CZ  . TYR A 1 18  ? 17.519 38.423 32.898 1.00 44.79  ? 15  TYR A CZ  1 
ATOM   112  O OH  . TYR A 1 18  ? 18.240 37.810 33.895 1.00 54.19  ? 15  TYR A OH  1 
ATOM   113  N N   . PHE A 1 19  ? 13.017 39.648 27.488 1.00 33.96  ? 16  PHE A N   1 
ATOM   114  C CA  . PHE A 1 19  ? 11.994 40.151 26.593 1.00 36.79  ? 16  PHE A CA  1 
ATOM   115  C C   . PHE A 1 19  ? 10.794 40.662 27.377 1.00 39.35  ? 16  PHE A C   1 
ATOM   116  O O   . PHE A 1 19  ? 10.506 40.157 28.465 1.00 41.65  ? 16  PHE A O   1 
ATOM   117  C CB  . PHE A 1 19  ? 11.511 39.011 25.693 1.00 36.28  ? 16  PHE A CB  1 
ATOM   118  C CG  . PHE A 1 19  ? 12.615 38.319 24.941 1.00 35.67  ? 16  PHE A CG  1 
ATOM   119  C CD1 . PHE A 1 19  ? 13.394 39.012 24.034 1.00 37.07  ? 16  PHE A CD1 1 
ATOM   120  C CD2 . PHE A 1 19  ? 12.897 36.980 25.176 1.00 36.00  ? 16  PHE A CD2 1 
ATOM   121  C CE1 . PHE A 1 19  ? 14.432 38.379 23.369 1.00 37.40  ? 16  PHE A CE1 1 
ATOM   122  C CE2 . PHE A 1 19  ? 13.932 36.348 24.505 1.00 36.79  ? 16  PHE A CE2 1 
ATOM   123  C CZ  . PHE A 1 19  ? 14.703 37.052 23.610 1.00 35.91  ? 16  PHE A CZ  1 
ATOM   124  N N   A ASP A 1 20  ? 10.114 41.673 26.816 0.50 39.28  ? 17  ASP A N   1 
ATOM   125  N N   B ASP A 1 20  ? 10.110 41.672 26.819 0.50 40.81  ? 17  ASP A N   1 
ATOM   126  C CA  A ASP A 1 20  ? 8.910  42.213 27.423 0.50 41.41  ? 17  ASP A CA  1 
ATOM   127  C CA  B ASP A 1 20  ? 8.910  42.219 27.433 0.50 44.04  ? 17  ASP A CA  1 
ATOM   128  C C   A ASP A 1 20  ? 7.908  41.064 27.511 0.50 43.06  ? 17  ASP A C   1 
ATOM   129  C C   B ASP A 1 20  ? 7.891  41.083 27.509 0.50 44.60  ? 17  ASP A C   1 
ATOM   130  O O   A ASP A 1 20  ? 7.516  40.505 26.486 0.50 43.47  ? 17  ASP A O   1 
ATOM   131  O O   B ASP A 1 20  ? 7.467  40.557 26.480 0.50 45.19  ? 17  ASP A O   1 
ATOM   132  C CB  A ASP A 1 20  ? 8.332  43.366 26.604 0.50 41.62  ? 17  ASP A CB  1 
ATOM   133  C CB  B ASP A 1 20  ? 8.423  43.455 26.672 0.50 46.32  ? 17  ASP A CB  1 
ATOM   134  C CG  A ASP A 1 20  ? 7.101  43.984 27.234 0.50 42.99  ? 17  ASP A CG  1 
ATOM   135  C CG  B ASP A 1 20  ? 7.146  44.056 27.227 0.50 50.09  ? 17  ASP A CG  1 
ATOM   136  O OD1 A ASP A 1 20  ? 7.240  44.619 28.302 0.50 41.30  ? 17  ASP A OD1 1 
ATOM   137  O OD1 B ASP A 1 20  ? 6.575  43.454 28.154 0.50 51.16  ? 17  ASP A OD1 1 
ATOM   138  O OD2 A ASP A 1 20  ? 6.006  43.744 26.701 0.50 42.63  ? 17  ASP A OD2 1 
ATOM   139  O OD2 B ASP A 1 20  ? 6.765  45.148 26.761 0.50 52.62  ? 17  ASP A OD2 1 
ATOM   140  N N   . PRO A 1 21  ? 7.493  40.647 28.727 1.00 44.40  ? 18  PRO A N   1 
ATOM   141  C CA  . PRO A 1 21  ? 6.567  39.525 28.876 1.00 45.08  ? 18  PRO A CA  1 
ATOM   142  C C   . PRO A 1 21  ? 5.247  39.612 28.113 1.00 47.66  ? 18  PRO A C   1 
ATOM   143  O O   . PRO A 1 21  ? 4.859  38.655 27.442 1.00 49.65  ? 18  PRO A O   1 
ATOM   144  C CB  . PRO A 1 21  ? 6.273  39.495 30.384 1.00 48.71  ? 18  PRO A CB  1 
ATOM   145  C CG  . PRO A 1 21  ? 7.456  40.183 31.016 1.00 49.84  ? 18  PRO A CG  1 
ATOM   146  C CD  . PRO A 1 21  ? 7.915  41.220 30.016 1.00 47.28  ? 18  PRO A CD  1 
ATOM   147  N N   . ALA A 1 22  ? 4.585  40.768 28.210 1.00 46.46  ? 19  ALA A N   1 
ATOM   148  C CA  . ALA A 1 22  ? 3.286  40.968 27.577 1.00 52.29  ? 19  ALA A CA  1 
ATOM   149  C C   . ALA A 1 22  ? 3.377  40.882 26.051 1.00 52.53  ? 19  ALA A C   1 
ATOM   150  O O   . ALA A 1 22  ? 2.555  40.223 25.415 1.00 56.94  ? 19  ALA A O   1 
ATOM   151  C CB  . ALA A 1 22  ? 2.715  42.290 28.021 1.00 51.68  ? 19  ALA A CB  1 
ATOM   152  N N   . ARG A 1 23  ? 4.378  41.550 25.467 1.00 48.03  ? 20  ARG A N   1 
ATOM   153  C CA  . ARG A 1 23  ? 4.551  41.563 24.022 1.00 50.44  ? 20  ARG A CA  1 
ATOM   154  C C   . ARG A 1 23  ? 4.993  40.194 23.501 1.00 50.10  ? 20  ARG A C   1 
ATOM   155  O O   . ARG A 1 23  ? 4.510  39.757 22.466 1.00 50.71  ? 20  ARG A O   1 
ATOM   156  C CB  . ARG A 1 23  ? 5.561  42.645 23.634 1.00 52.53  ? 20  ARG A CB  1 
ATOM   157  C CG  . ARG A 1 23  ? 5.113  44.065 23.942 1.00 57.41  ? 20  ARG A CG  1 
ATOM   158  C CD  . ARG A 1 23  ? 6.246  45.051 23.714 1.00 61.01  ? 20  ARG A CD  1 
ATOM   159  N NE  . ARG A 1 23  ? 6.726  45.068 22.342 1.00 63.76  ? 20  ARG A NE  1 
ATOM   160  C CZ  . ARG A 1 23  ? 7.745  45.804 21.910 1.00 67.50  ? 20  ARG A CZ  1 
ATOM   161  N NH1 . ARG A 1 23  ? 8.429  46.553 22.756 1.00 71.73  ? 20  ARG A NH1 1 
ATOM   162  N NH2 . ARG A 1 23  ? 8.097  45.763 20.636 1.00 70.37  ? 20  ARG A NH2 1 
ATOM   163  N N   . LEU A 1 24  ? 5.913  39.515 24.209 1.00 49.64  ? 21  LEU A N   1 
ATOM   164  C CA  . LEU A 1 24  ? 6.401  38.223 23.740 1.00 49.21  ? 21  LEU A CA  1 
ATOM   165  C C   . LEU A 1 24  ? 5.298  37.161 23.819 1.00 50.70  ? 21  LEU A C   1 
ATOM   166  O O   . LEU A 1 24  ? 5.247  36.248 22.995 1.00 52.61  ? 21  LEU A O   1 
ATOM   167  C CB  . LEU A 1 24  ? 7.629  37.806 24.562 1.00 49.40  ? 21  LEU A CB  1 
ATOM   168  C CG  . LEU A 1 24  ? 8.357  36.555 24.066 1.00 51.32  ? 21  LEU A CG  1 
ATOM   169  C CD1 . LEU A 1 24  ? 9.164  36.869 22.817 1.00 52.59  ? 21  LEU A CD1 1 
ATOM   170  C CD2 . LEU A 1 24  ? 9.268  35.965 25.135 1.00 50.55  ? 21  LEU A CD2 1 
ATOM   171  N N   . LEU A 1 25  ? 4.394  37.300 24.788 1.00 53.23  ? 22  LEU A N   1 
ATOM   172  C CA  . LEU A 1 25  ? 3.334  36.317 24.983 1.00 57.00  ? 22  LEU A CA  1 
ATOM   173  C C   . LEU A 1 25  ? 2.318  36.338 23.841 1.00 59.14  ? 22  LEU A C   1 
ATOM   174  O O   . LEU A 1 25  ? 1.610  35.354 23.638 1.00 62.28  ? 22  LEU A O   1 
ATOM   175  C CB  . LEU A 1 25  ? 2.667  36.578 26.339 1.00 59.17  ? 22  LEU A CB  1 
ATOM   176  C CG  . LEU A 1 25  ? 1.508  35.647 26.703 1.00 62.45  ? 22  LEU A CG  1 
ATOM   177  C CD1 . LEU A 1 25  ? 2.014  34.246 27.017 1.00 64.06  ? 22  LEU A CD1 1 
ATOM   178  C CD2 . LEU A 1 25  ? 0.725  36.203 27.881 1.00 65.85  ? 22  LEU A CD2 1 
ATOM   179  N N   . GLU A 1 26  ? 2.243  37.452 23.103 1.00 60.28  ? 23  GLU A N   1 
ATOM   180  C CA  . GLU A 1 26  ? 1.320  37.592 21.982 1.00 63.72  ? 23  GLU A CA  1 
ATOM   181  C C   . GLU A 1 26  ? 1.598  36.559 20.883 1.00 62.63  ? 23  GLU A C   1 
ATOM   182  O O   . GLU A 1 26  ? 0.682  36.130 20.187 1.00 63.84  ? 23  GLU A O   1 
ATOM   183  C CB  . GLU A 1 26  ? 1.440  38.994 21.377 1.00 65.51  ? 23  GLU A CB  1 
ATOM   184  C CG  . GLU A 1 26  ? 1.112  40.119 22.343 1.00 73.04  ? 23  GLU A CG  1 
ATOM   185  C CD  . GLU A 1 26  ? 1.311  41.519 21.785 1.00 76.10  ? 23  GLU A CD  1 
ATOM   186  O OE1 . GLU A 1 26  ? 1.689  41.637 20.605 1.00 78.30  ? 23  GLU A OE1 1 
ATOM   187  O OE2 . GLU A 1 26  ? 1.123  42.488 22.544 1.00 87.16  ? 23  GLU A OE2 1 
ATOM   188  N N   . LEU A 1 27  ? 2.865  36.163 20.720 1.00 59.89  ? 24  LEU A N   1 
ATOM   189  C CA  . LEU A 1 27  ? 3.250  35.222 19.677 1.00 60.53  ? 24  LEU A CA  1 
ATOM   190  C C   . LEU A 1 27  ? 2.677  33.824 19.906 1.00 62.43  ? 24  LEU A C   1 
ATOM   191  O O   . LEU A 1 27  ? 2.534  33.378 21.042 1.00 60.87  ? 24  LEU A O   1 
ATOM   192  C CB  . LEU A 1 27  ? 4.780  35.160 19.628 1.00 56.96  ? 24  LEU A CB  1 
ATOM   193  C CG  . LEU A 1 27  ? 5.487  36.407 19.104 1.00 58.35  ? 24  LEU A CG  1 
ATOM   194  C CD1 . LEU A 1 27  ? 5.352  37.583 20.052 1.00 61.52  ? 24  LEU A CD1 1 
ATOM   195  C CD2 . LEU A 1 27  ? 6.959  36.103 18.874 1.00 61.45  ? 24  LEU A CD2 1 
ATOM   196  N N   . ASP A 1 28  ? 2.355  33.141 18.795 1.00 59.84  ? 25  ASP A N   1 
ATOM   197  C CA  . ASP A 1 28  ? 1.880  31.769 18.844 1.00 62.18  ? 25  ASP A CA  1 
ATOM   198  C C   . ASP A 1 28  ? 3.115  30.880 18.683 1.00 63.12  ? 25  ASP A C   1 
ATOM   199  O O   . ASP A 1 28  ? 4.220  31.392 18.503 1.00 56.82  ? 25  ASP A O   1 
ATOM   200  C CB  . ASP A 1 28  ? 0.770  31.521 17.813 1.00 67.13  ? 25  ASP A CB  1 
ATOM   201  C CG  . ASP A 1 28  ? 1.192  31.631 16.356 1.00 68.60  ? 25  ASP A CG  1 
ATOM   202  O OD1 . ASP A 1 28  ? 2.397  31.795 16.096 1.00 64.91  ? 25  ASP A OD1 1 
ATOM   203  O OD2 . ASP A 1 28  ? 0.301  31.579 15.490 1.00 71.40  ? 25  ASP A OD2 1 
ATOM   204  N N   . ASP A 1 29  ? 2.926  29.555 18.720 1.00 63.55  ? 26  ASP A N   1 
ATOM   205  C CA  . ASP A 1 29  ? 4.030  28.605 18.631 1.00 63.80  ? 26  ASP A CA  1 
ATOM   206  C C   . ASP A 1 29  ? 4.805  28.716 17.318 1.00 65.56  ? 26  ASP A C   1 
ATOM   207  O O   . ASP A 1 29  ? 6.036  28.659 17.330 1.00 57.45  ? 26  ASP A O   1 
ATOM   208  C CB  . ASP A 1 29  ? 3.552  27.167 18.844 1.00 66.62  ? 26  ASP A CB  1 
ATOM   209  C CG  . ASP A 1 29  ? 3.047  26.899 20.251 1.00 72.90  ? 26  ASP A CG  1 
ATOM   210  O OD1 . ASP A 1 29  ? 3.141  27.821 21.093 1.00 75.45  ? 26  ASP A OD1 1 
ATOM   211  O OD2 . ASP A 1 29  ? 2.532  25.782 20.486 1.00 77.79  ? 26  ASP A OD2 1 
ATOM   212  N N   A ASP A 1 30  ? 4.093  28.855 16.194 0.50 64.35  ? 27  ASP A N   1 
ATOM   213  N N   B ASP A 1 30  ? 4.082  28.861 16.202 0.50 65.29  ? 27  ASP A N   1 
ATOM   214  C CA  A ASP A 1 30  ? 4.753  28.947 14.900 0.50 65.93  ? 27  ASP A CA  1 
ATOM   215  C CA  B ASP A 1 30  ? 4.722  28.964 14.900 0.50 67.67  ? 27  ASP A CA  1 
ATOM   216  C C   A ASP A 1 30  ? 5.685  30.157 14.860 0.50 58.94  ? 27  ASP A C   1 
ATOM   217  C C   B ASP A 1 30  ? 5.687  30.146 14.882 0.50 59.61  ? 27  ASP A C   1 
ATOM   218  O O   A ASP A 1 30  ? 6.771  30.075 14.291 0.50 57.86  ? 27  ASP A O   1 
ATOM   219  O O   B ASP A 1 30  ? 6.790  30.036 14.350 0.50 58.13  ? 27  ASP A O   1 
ATOM   220  C CB  A ASP A 1 30  ? 3.738  28.951 13.754 0.50 67.66  ? 27  ASP A CB  1 
ATOM   221  C CB  B ASP A 1 30  ? 3.702  29.121 13.771 0.50 70.92  ? 27  ASP A CB  1 
ATOM   222  C CG  A ASP A 1 30  ? 2.957  27.653 13.652 0.50 71.41  ? 27  ASP A CG  1 
ATOM   223  C CG  B ASP A 1 30  ? 4.351  29.224 12.402 0.50 74.42  ? 27  ASP A CG  1 
ATOM   224  O OD1 A ASP A 1 30  ? 3.212  26.753 14.479 0.50 72.24  ? 27  ASP A OD1 1 
ATOM   225  O OD1 B ASP A 1 30  ? 5.023  28.252 11.997 0.50 74.70  ? 27  ASP A OD1 1 
ATOM   226  O OD2 A ASP A 1 30  ? 2.115  27.545 12.741 0.50 75.33  ? 27  ASP A OD2 1 
ATOM   227  O OD2 B ASP A 1 30  ? 4.211  30.288 11.766 0.50 75.55  ? 27  ASP A OD2 1 
ATOM   228  N N   . GLN A 1 31  ? 5.252  31.274 15.458 1.00 59.66  ? 28  GLN A N   1 
ATOM   229  C CA  . GLN A 1 31  ? 6.053  32.490 15.495 1.00 58.79  ? 28  GLN A CA  1 
ATOM   230  C C   . GLN A 1 31  ? 7.315  32.285 16.335 1.00 52.75  ? 28  GLN A C   1 
ATOM   231  O O   . GLN A 1 31  ? 8.391  32.714 15.929 1.00 54.16  ? 28  GLN A O   1 
ATOM   232  C CB  . GLN A 1 31  ? 5.206  33.667 15.979 1.00 63.06  ? 28  GLN A CB  1 
ATOM   233  C CG  . GLN A 1 31  ? 4.122  34.078 14.993 1.00 71.11  ? 28  GLN A CG  1 
ATOM   234  C CD  . GLN A 1 31  ? 3.250  35.180 15.544 1.00 76.54  ? 28  GLN A CD  1 
ATOM   235  O OE1 . GLN A 1 31  ? 2.519  34.990 16.513 1.00 74.48  ? 28  GLN A OE1 1 
ATOM   236  N NE2 . GLN A 1 31  ? 3.292  36.337 14.903 1.00 81.06  ? 28  GLN A NE2 1 
ATOM   237  N N   . HIS A 1 32  ? 7.187  31.650 17.506 1.00 49.16  ? 29  HIS A N   1 
ATOM   238  C CA  . HIS A 1 32  ? 8.359  31.385 18.328 1.00 48.68  ? 29  HIS A CA  1 
ATOM   239  C C   . HIS A 1 32  ? 9.348  30.520 17.550 1.00 49.60  ? 29  HIS A C   1 
ATOM   240  O O   . HIS A 1 32  ? 10.529 30.844 17.468 1.00 46.69  ? 29  HIS A O   1 
ATOM   241  C CB  . HIS A 1 32  ? 8.000  30.715 19.662 1.00 47.42  ? 29  HIS A CB  1 
ATOM   242  C CG  . HIS A 1 32  ? 7.266  31.582 20.628 1.00 47.63  ? 29  HIS A CG  1 
ATOM   243  N ND1 . HIS A 1 32  ? 7.848  32.707 21.169 1.00 44.68  ? 29  HIS A ND1 1 
ATOM   244  C CD2 . HIS A 1 32  ? 6.051  31.481 21.190 1.00 49.77  ? 29  HIS A CD2 1 
ATOM   245  C CE1 . HIS A 1 32  ? 6.995  33.278 22.003 1.00 47.30  ? 29  HIS A CE1 1 
ATOM   246  N NE2 . HIS A 1 32  ? 5.892  32.551 22.034 1.00 48.53  ? 29  HIS A NE2 1 
ATOM   247  N N   . LEU A 1 33  ? 8.839  29.439 16.938 1.00 49.52  ? 30  LEU A N   1 
ATOM   248  C CA  . LEU A 1 33  ? 9.673  28.522 16.179 1.00 49.24  ? 30  LEU A CA  1 
ATOM   249  C C   . LEU A 1 33  ? 10.375 29.258 15.038 1.00 48.47  ? 30  LEU A C   1 
ATOM   250  O O   . LEU A 1 33  ? 11.526 28.962 14.731 1.00 51.22  ? 30  LEU A O   1 
ATOM   251  C CB  . LEU A 1 33  ? 8.803  27.376 15.644 1.00 52.73  ? 30  LEU A CB  1 
ATOM   252  C CG  . LEU A 1 33  ? 8.156  26.477 16.701 1.00 56.44  ? 30  LEU A CG  1 
ATOM   253  C CD1 . LEU A 1 33  ? 7.500  25.260 16.056 1.00 62.18  ? 30  LEU A CD1 1 
ATOM   254  C CD2 . LEU A 1 33  ? 9.171  26.031 17.742 1.00 57.51  ? 30  LEU A CD2 1 
ATOM   255  N N   . GLN A 1 34  ? 9.681  30.218 14.419 1.00 48.14  ? 31  GLN A N   1 
ATOM   256  C CA  . GLN A 1 34  ? 10.270 30.943 13.307 1.00 52.11  ? 31  GLN A CA  1 
ATOM   257  C C   . GLN A 1 34  ? 11.399 31.835 13.816 1.00 46.49  ? 31  GLN A C   1 
ATOM   258  O O   . GLN A 1 34  ? 12.419 31.995 13.151 1.00 46.61  ? 31  GLN A O   1 
ATOM   259  C CB  . GLN A 1 34  ? 9.222  31.777 12.574 1.00 58.45  ? 31  GLN A CB  1 
ATOM   260  C CG  . GLN A 1 34  ? 9.761  32.440 11.311 1.00 70.30  ? 31  GLN A CG  1 
ATOM   261  C CD  . GLN A 1 34  ? 8.688  33.167 10.534 1.00 78.34  ? 31  GLN A CD  1 
ATOM   262  O OE1 . GLN A 1 34  ? 7.677  32.583 10.147 1.00 82.52  ? 31  GLN A OE1 1 
ATOM   263  N NE2 . GLN A 1 34  ? 8.892  34.455 10.305 1.00 81.35  ? 31  GLN A NE2 1 
ATOM   264  N N   . ARG A 1 35  ? 11.188 32.440 14.983 1.00 46.78  ? 32  ARG A N   1 
ATOM   265  C CA  . ARG A 1 35  ? 12.215 33.305 15.541 1.00 44.01  ? 32  ARG A CA  1 
ATOM   266  C C   . ARG A 1 35  ? 13.455 32.510 15.923 1.00 42.95  ? 32  ARG A C   1 
ATOM   267  O O   . ARG A 1 35  ? 14.565 32.978 15.684 1.00 42.34  ? 32  ARG A O   1 
ATOM   268  C CB  . ARG A 1 35  ? 11.664 34.149 16.686 1.00 45.86  ? 32  ARG A CB  1 
ATOM   269  C CG  . ARG A 1 35  ? 10.653 35.170 16.196 1.00 48.95  ? 32  ARG A CG  1 
ATOM   270  C CD  . ARG A 1 35  ? 10.279 36.156 17.257 1.00 55.58  ? 32  ARG A CD  1 
ATOM   271  N NE  . ARG A 1 35  ? 9.399  37.193 16.747 1.00 53.98  ? 32  ARG A NE  1 
ATOM   272  C CZ  . ARG A 1 35  ? 9.044  38.252 17.462 1.00 57.62  ? 32  ARG A CZ  1 
ATOM   273  N NH1 . ARG A 1 35  ? 9.531  38.404 18.679 1.00 55.60  ? 32  ARG A NH1 1 
ATOM   274  N NH2 . ARG A 1 35  ? 8.232  39.163 16.960 1.00 54.75  ? 32  ARG A NH2 1 
ATOM   275  N N   . ILE A 1 36  ? 13.272 31.336 16.528 1.00 40.38  ? 33  ILE A N   1 
ATOM   276  C CA  . ILE A 1 36  ? 14.424 30.522 16.884 1.00 41.90  ? 33  ILE A CA  1 
ATOM   277  C C   . ILE A 1 36  ? 15.143 30.097 15.606 1.00 41.52  ? 33  ILE A C   1 
ATOM   278  O O   . ILE A 1 36  ? 16.364 30.089 15.572 1.00 39.26  ? 33  ILE A O   1 
ATOM   279  C CB  . ILE A 1 36  ? 14.028 29.336 17.786 1.00 43.35  ? 33  ILE A CB  1 
ATOM   280  C CG1 . ILE A 1 36  ? 13.546 29.817 19.161 1.00 42.87  ? 33  ILE A CG1 1 
ATOM   281  C CG2 . ILE A 1 36  ? 15.183 28.358 17.938 1.00 45.72  ? 33  ILE A CG2 1 
ATOM   282  C CD1 . ILE A 1 36  ? 14.594 30.535 19.973 1.00 43.30  ? 33  ILE A CD1 1 
ATOM   283  N N   . GLU A 1 37  ? 14.381 29.764 14.556 1.00 43.14  ? 34  GLU A N   1 
ATOM   284  C CA  . GLU A 1 37  ? 14.965 29.347 13.291 1.00 49.81  ? 34  GLU A CA  1 
ATOM   285  C C   . GLU A 1 37  ? 15.860 30.463 12.747 1.00 43.50  ? 34  GLU A C   1 
ATOM   286  O O   . GLU A 1 37  ? 17.011 30.231 12.386 1.00 42.15  ? 34  GLU A O   1 
ATOM   287  C CB  . GLU A 1 37  ? 13.827 28.946 12.347 1.00 55.42  ? 34  GLU A CB  1 
ATOM   288  C CG  . GLU A 1 37  ? 14.280 28.478 10.983 1.00 65.01  ? 34  GLU A CG  1 
ATOM   289  C CD  . GLU A 1 37  ? 13.140 28.077 10.058 1.00 75.46  ? 34  GLU A CD  1 
ATOM   290  O OE1 . GLU A 1 37  ? 11.966 28.122 10.494 1.00 70.53  ? 34  GLU A OE1 1 
ATOM   291  O OE2 . GLU A 1 37  ? 13.427 27.744 8.895  1.00 85.96  ? 34  GLU A OE2 1 
ATOM   292  N N   . ARG A 1 38  ? 15.335 31.690 12.730 1.00 41.53  ? 35  ARG A N   1 
ATOM   293  C CA  . ARG A 1 38  ? 16.066 32.847 12.240 1.00 43.43  ? 35  ARG A CA  1 
ATOM   294  C C   . ARG A 1 38  ? 17.304 33.108 13.100 1.00 39.54  ? 35  ARG A C   1 
ATOM   295  O O   . ARG A 1 38  ? 18.352 33.506 12.591 1.00 40.36  ? 35  ARG A O   1 
ATOM   296  C CB  . ARG A 1 38  ? 15.146 34.071 12.239 1.00 43.61  ? 35  ARG A CB  1 
ATOM   297  C CG  . ARG A 1 38  ? 13.949 33.976 11.298 1.00 50.25  ? 35  ARG A CG  1 
ATOM   298  C CD  . ARG A 1 38  ? 12.997 35.126 11.575 1.00 52.55  ? 35  ARG A CD  1 
ATOM   299  N NE  . ARG A 1 38  ? 13.619 36.430 11.406 1.00 57.29  ? 35  ARG A NE  1 
ATOM   300  C CZ  . ARG A 1 38  ? 13.067 37.582 11.773 1.00 56.35  ? 35  ARG A CZ  1 
ATOM   301  N NH1 . ARG A 1 38  ? 11.908 37.589 12.404 1.00 57.97  ? 35  ARG A NH1 1 
ATOM   302  N NH2 . ARG A 1 38  ? 13.709 38.719 11.570 1.00 56.02  ? 35  ARG A NH2 1 
ATOM   303  N N   . PHE A 1 39  ? 17.173 32.889 14.412 1.00 39.81  ? 36  PHE A N   1 
ATOM   304  C CA  . PHE A 1 39  ? 18.273 33.133 15.332 1.00 35.57  ? 36  PHE A CA  1 
ATOM   305  C C   . PHE A 1 39  ? 19.407 32.146 15.062 1.00 33.47  ? 36  PHE A C   1 
ATOM   306  O O   . PHE A 1 39  ? 20.577 32.534 15.012 1.00 35.80  ? 36  PHE A O   1 
ATOM   307  C CB  . PHE A 1 39  ? 17.775 33.089 16.780 1.00 34.87  ? 36  PHE A CB  1 
ATOM   308  C CG  . PHE A 1 39  ? 18.853 33.342 17.800 1.00 32.81  ? 36  PHE A CG  1 
ATOM   309  C CD1 . PHE A 1 39  ? 19.541 34.544 17.823 1.00 33.36  ? 36  PHE A CD1 1 
ATOM   310  C CD2 . PHE A 1 39  ? 19.213 32.363 18.710 1.00 33.95  ? 36  PHE A CD2 1 
ATOM   311  C CE1 . PHE A 1 39  ? 20.539 34.768 18.756 1.00 32.79  ? 36  PHE A CE1 1 
ATOM   312  C CE2 . PHE A 1 39  ? 20.219 32.583 19.633 1.00 33.50  ? 36  PHE A CE2 1 
ATOM   313  C CZ  . PHE A 1 39  ? 20.883 33.783 19.653 1.00 32.02  ? 36  PHE A CZ  1 
ATOM   314  N N   . LEU A 1 40  ? 19.076 30.863 14.906 1.00 35.92  ? 37  LEU A N   1 
ATOM   315  C CA  . LEU A 1 40  ? 20.101 29.875 14.596 1.00 36.83  ? 37  LEU A CA  1 
ATOM   316  C C   . LEU A 1 40  ? 20.796 30.238 13.272 1.00 36.76  ? 37  LEU A C   1 
ATOM   317  O O   . LEU A 1 40  ? 22.006 30.074 13.143 1.00 37.93  ? 37  LEU A O   1 
ATOM   318  C CB  . LEU A 1 40  ? 19.445 28.489 14.557 1.00 37.15  ? 37  LEU A CB  1 
ATOM   319  C CG  . LEU A 1 40  ? 18.806 28.032 15.873 1.00 38.81  ? 37  LEU A CG  1 
ATOM   320  C CD1 . LEU A 1 40  ? 18.373 26.570 15.803 1.00 44.00  ? 37  LEU A CD1 1 
ATOM   321  C CD2 . LEU A 1 40  ? 19.757 28.229 17.041 1.00 39.94  ? 37  LEU A CD2 1 
ATOM   322  N N   . ASP A 1 41  ? 20.037 30.754 12.295 1.00 38.58  ? 38  ASP A N   1 
ATOM   323  C CA  . ASP A 1 41  ? 20.603 31.157 11.012 1.00 40.99  ? 38  ASP A CA  1 
ATOM   324  C C   . ASP A 1 41  ? 21.568 32.320 11.184 1.00 43.41  ? 38  ASP A C   1 
ATOM   325  O O   . ASP A 1 41  ? 22.551 32.411 10.451 1.00 41.74  ? 38  ASP A O   1 
ATOM   326  C CB  . ASP A 1 41  ? 19.520 31.559 10.011 1.00 46.06  ? 38  ASP A CB  1 
ATOM   327  C CG  . ASP A 1 41  ? 18.672 30.412 9.495  1.00 51.35  ? 38  ASP A CG  1 
ATOM   328  O OD1 . ASP A 1 41  ? 18.987 29.247 9.802  1.00 53.62  ? 38  ASP A OD1 1 
ATOM   329  O OD2 . ASP A 1 41  ? 17.677 30.703 8.822  1.00 61.44  ? 38  ASP A OD2 1 
ATOM   330  N N   . ALA A 1 42  ? 21.272 33.204 12.147 1.00 37.10  ? 39  ALA A N   1 
ATOM   331  C CA  . ALA A 1 42  ? 22.109 34.355 12.411 1.00 39.77  ? 39  ALA A CA  1 
ATOM   332  C C   . ALA A 1 42  ? 23.386 33.921 13.125 1.00 37.38  ? 39  ALA A C   1 
ATOM   333  O O   . ALA A 1 42  ? 24.420 34.567 13.001 1.00 38.70  ? 39  ALA A O   1 
ATOM   334  C CB  . ALA A 1 42  ? 21.335 35.373 13.207 1.00 43.53  ? 39  ALA A CB  1 
ATOM   335  N N   . LEU A 1 43  ? 23.303 32.827 13.884 1.00 37.39  ? 40  LEU A N   1 
ATOM   336  C CA  . LEU A 1 43  ? 24.463 32.334 14.612 1.00 35.55  ? 40  LEU A CA  1 
ATOM   337  C C   . LEU A 1 43  ? 25.449 31.602 13.700 1.00 35.22  ? 40  LEU A C   1 
ATOM   338  O O   . LEU A 1 43  ? 26.661 31.698 13.899 1.00 33.46  ? 40  LEU A O   1 
ATOM   339  C CB  . LEU A 1 43  ? 24.001 31.369 15.715 1.00 34.29  ? 40  LEU A CB  1 
ATOM   340  C CG  . LEU A 1 43  ? 23.239 31.951 16.900 1.00 34.15  ? 40  LEU A CG  1 
ATOM   341  C CD1 . LEU A 1 43  ? 23.049 30.883 17.969 1.00 34.17  ? 40  LEU A CD1 1 
ATOM   342  C CD2 . LEU A 1 43  ? 23.972 33.144 17.493 1.00 35.61  ? 40  LEU A CD2 1 
ATOM   343  N N   . ALA A 1 44  ? 24.917 30.889 12.699 1.00 36.40  ? 41  ALA A N   1 
ATOM   344  C CA  . ALA A 1 44  ? 25.687 30.017 11.822 1.00 34.61  ? 41  ALA A CA  1 
ATOM   345  C C   . ALA A 1 44  ? 26.961 30.644 11.251 1.00 35.74  ? 41  ALA A C   1 
ATOM   346  O O   . ALA A 1 44  ? 28.020 30.026 11.315 1.00 36.23  ? 41  ALA A O   1 
ATOM   347  C CB  . ALA A 1 44  ? 24.786 29.498 10.718 1.00 39.19  ? 41  ALA A CB  1 
ATOM   348  N N   . PRO A 1 45  ? 26.932 31.847 10.645 1.00 37.04  ? 42  PRO A N   1 
ATOM   349  C CA  . PRO A 1 45  ? 28.158 32.417 10.075 1.00 38.77  ? 42  PRO A CA  1 
ATOM   350  C C   . PRO A 1 45  ? 29.199 32.956 11.051 1.00 36.65  ? 42  PRO A C   1 
ATOM   351  O O   . PRO A 1 45  ? 30.324 33.255 10.643 1.00 38.27  ? 42  PRO A O   1 
ATOM   352  C CB  . PRO A 1 45  ? 27.680 33.617 9.247  1.00 41.92  ? 42  PRO A CB  1 
ATOM   353  C CG  . PRO A 1 45  ? 26.267 33.901 9.691  1.00 43.99  ? 42  PRO A CG  1 
ATOM   354  C CD  . PRO A 1 45  ? 25.739 32.653 10.368 1.00 39.53  ? 42  PRO A CD  1 
ATOM   355  N N   . LEU A 1 46  ? 28.842 33.025 12.342 1.00 35.64  ? 43  LEU A N   1 
ATOM   356  C CA  . LEU A 1 46  ? 29.719 33.626 13.335 1.00 36.35  ? 43  LEU A CA  1 
ATOM   357  C C   . LEU A 1 46  ? 30.840 32.686 13.760 1.00 36.00  ? 43  LEU A C   1 
ATOM   358  O O   . LEU A 1 46  ? 31.919 33.154 14.103 1.00 38.33  ? 43  LEU A O   1 
ATOM   359  C CB  . LEU A 1 46  ? 28.874 34.079 14.525 1.00 35.02  ? 43  LEU A CB  1 
ATOM   360  C CG  . LEU A 1 46  ? 27.776 35.092 14.207 1.00 36.15  ? 43  LEU A CG  1 
ATOM   361  C CD1 . LEU A 1 46  ? 27.141 35.597 15.496 1.00 37.79  ? 43  LEU A CD1 1 
ATOM   362  C CD2 . LEU A 1 46  ? 28.302 36.270 13.397 1.00 39.21  ? 43  LEU A CD2 1 
ATOM   363  N N   . HIS A 1 47  ? 30.597 31.373 13.732 1.00 37.36  ? 44  HIS A N   1 
ATOM   364  C CA  . HIS A 1 47  ? 31.642 30.436 14.113 1.00 38.40  ? 44  HIS A CA  1 
ATOM   365  C C   . HIS A 1 47  ? 31.176 29.010 13.828 1.00 38.79  ? 44  HIS A C   1 
ATOM   366  O O   . HIS A 1 47  ? 29.990 28.709 13.950 1.00 36.40  ? 44  HIS A O   1 
ATOM   367  C CB  . HIS A 1 47  ? 32.035 30.624 15.587 1.00 38.63  ? 44  HIS A CB  1 
ATOM   368  C CG  . HIS A 1 47  ? 33.254 29.852 15.943 1.00 40.29  ? 44  HIS A CG  1 
ATOM   369  N ND1 . HIS A 1 47  ? 33.313 28.488 16.119 1.00 40.60  ? 44  HIS A ND1 1 
ATOM   370  C CD2 . HIS A 1 47  ? 34.486 30.315 16.196 1.00 43.60  ? 44  HIS A CD2 1 
ATOM   371  C CE1 . HIS A 1 47  ? 34.558 28.147 16.417 1.00 46.89  ? 44  HIS A CE1 1 
ATOM   372  N NE2 . HIS A 1 47  ? 35.292 29.237 16.448 1.00 43.12  ? 44  HIS A NE2 1 
ATOM   373  N N   . PRO A 1 48  ? 32.075 28.101 13.379 1.00 41.59  ? 45  PRO A N   1 
ATOM   374  C CA  . PRO A 1 48  ? 31.688 26.715 13.124 1.00 39.79  ? 45  PRO A CA  1 
ATOM   375  C C   . PRO A 1 48  ? 30.927 25.999 14.243 1.00 38.22  ? 45  PRO A C   1 
ATOM   376  O O   . PRO A 1 48  ? 30.022 25.216 13.957 1.00 38.83  ? 45  PRO A O   1 
ATOM   377  C CB  . PRO A 1 48  ? 33.047 26.031 12.896 1.00 45.09  ? 45  PRO A CB  1 
ATOM   378  C CG  . PRO A 1 48  ? 33.900 27.109 12.274 1.00 46.01  ? 45  PRO A CG  1 
ATOM   379  C CD  . PRO A 1 48  ? 33.466 28.380 12.978 1.00 47.25  ? 45  PRO A CD  1 
ATOM   380  N N   . VAL A 1 49  ? 31.247 26.289 15.516 1.00 39.37  ? 46  VAL A N   1 
ATOM   381  C CA  . VAL A 1 49  ? 30.593 25.596 16.623 1.00 38.85  ? 46  VAL A CA  1 
ATOM   382  C C   . VAL A 1 49  ? 29.148 26.059 16.766 1.00 36.86  ? 46  VAL A C   1 
ATOM   383  O O   . VAL A 1 49  ? 28.402 25.445 17.520 1.00 36.20  ? 46  VAL A O   1 
ATOM   384  C CB  . VAL A 1 49  ? 31.311 25.743 17.982 1.00 40.45  ? 46  VAL A CB  1 
ATOM   385  C CG1 . VAL A 1 49  ? 32.769 25.332 17.890 1.00 45.73  ? 46  VAL A CG1 1 
ATOM   386  C CG2 . VAL A 1 49  ? 31.184 27.140 18.574 1.00 36.90  ? 46  VAL A CG2 1 
ATOM   387  N N   . LEU A 1 50  ? 28.764 27.138 16.063 1.00 33.15  ? 47  LEU A N   1 
ATOM   388  C CA  . LEU A 1 50  ? 27.403 27.644 16.145 1.00 32.01  ? 47  LEU A CA  1 
ATOM   389  C C   . LEU A 1 50  ? 26.562 27.218 14.942 1.00 32.26  ? 47  LEU A C   1 
ATOM   390  O O   . LEU A 1 50  ? 25.402 27.606 14.862 1.00 34.41  ? 47  LEU A O   1 
ATOM   391  C CB  . LEU A 1 50  ? 27.477 29.171 16.183 1.00 32.58  ? 47  LEU A CB  1 
ATOM   392  C CG  . LEU A 1 50  ? 28.168 29.789 17.397 1.00 33.43  ? 47  LEU A CG  1 
ATOM   393  C CD1 . LEU A 1 50  ? 28.196 31.302 17.254 1.00 33.79  ? 47  LEU A CD1 1 
ATOM   394  C CD2 . LEU A 1 50  ? 27.444 29.403 18.682 1.00 35.45  ? 47  LEU A CD2 1 
ATOM   395  N N   . GLU A 1 51  ? 27.123 26.390 14.053 1.00 34.92  ? 48  GLU A N   1 
ATOM   396  C CA  . GLU A 1 51  ? 26.439 26.007 12.822 1.00 37.92  ? 48  GLU A CA  1 
ATOM   397  C C   . GLU A 1 51  ? 25.430 24.870 13.009 1.00 39.74  ? 48  GLU A C   1 
ATOM   398  O O   . GLU A 1 51  ? 24.492 24.776 12.219 1.00 41.71  ? 48  GLU A O   1 
ATOM   399  C CB  . GLU A 1 51  ? 27.470 25.612 11.757 1.00 38.68  ? 48  GLU A CB  1 
ATOM   400  C CG  . GLU A 1 51  ? 28.441 26.730 11.388 1.00 41.88  ? 48  GLU A CG  1 
ATOM   401  C CD  . GLU A 1 51  ? 29.505 26.380 10.354 1.00 46.50  ? 48  GLU A CD  1 
ATOM   402  O OE1 . GLU A 1 51  ? 29.515 25.237 9.879  1.00 47.86  ? 48  GLU A OE1 1 
ATOM   403  O OE2 . GLU A 1 51  ? 30.345 27.256 10.039 1.00 51.35  ? 48  GLU A OE2 1 
ATOM   404  N N   . ASN A 1 52  ? 25.610 24.011 14.024 1.00 33.73  ? 49  ASN A N   1 
ATOM   405  C CA  . ASN A 1 52  ? 24.720 22.875 14.212 1.00 35.88  ? 49  ASN A CA  1 
ATOM   406  C C   . ASN A 1 52  ? 24.077 22.866 15.596 1.00 35.64  ? 49  ASN A C   1 
ATOM   407  O O   . ASN A 1 52  ? 24.766 22.979 16.606 1.00 37.43  ? 49  ASN A O   1 
ATOM   408  C CB  . ASN A 1 52  ? 25.462 21.555 14.003 1.00 37.30  ? 49  ASN A CB  1 
ATOM   409  C CG  . ASN A 1 52  ? 25.870 21.321 12.559 1.00 37.75  ? 49  ASN A CG  1 
ATOM   410  O OD1 . ASN A 1 52  ? 25.050 20.941 11.722 1.00 38.94  ? 49  ASN A OD1 1 
ATOM   411  N ND2 . ASN A 1 52  ? 27.156 21.433 12.285 1.00 40.59  ? 49  ASN A ND2 1 
ATOM   412  N N   . TRP A 1 53  ? 22.751 22.687 15.614 1.00 33.60  ? 50  TRP A N   1 
ATOM   413  C CA  . TRP A 1 53  ? 21.992 22.595 16.848 1.00 35.27  ? 50  TRP A CA  1 
ATOM   414  C C   . TRP A 1 53  ? 21.144 21.333 16.849 1.00 37.25  ? 50  TRP A C   1 
ATOM   415  O O   . TRP A 1 53  ? 20.565 20.965 15.819 1.00 40.50  ? 50  TRP A O   1 
ATOM   416  C CB  . TRP A 1 53  ? 21.165 23.859 17.125 1.00 35.37  ? 50  TRP A CB  1 
ATOM   417  C CG  . TRP A 1 53  ? 22.040 25.059 17.310 1.00 34.10  ? 50  TRP A CG  1 
ATOM   418  C CD1 . TRP A 1 53  ? 22.675 25.801 16.362 1.00 36.50  ? 50  TRP A CD1 1 
ATOM   419  C CD2 . TRP A 1 53  ? 22.545 25.513 18.574 1.00 34.40  ? 50  TRP A CD2 1 
ATOM   420  N NE1 . TRP A 1 53  ? 23.458 26.760 16.955 1.00 35.16  ? 50  TRP A NE1 1 
ATOM   421  C CE2 . TRP A 1 53  ? 23.427 26.581 18.311 1.00 34.28  ? 50  TRP A CE2 1 
ATOM   422  C CE3 . TRP A 1 53  ? 22.343 25.110 19.896 1.00 33.76  ? 50  TRP A CE3 1 
ATOM   423  C CZ2 . TRP A 1 53  ? 24.059 27.282 19.337 1.00 33.11  ? 50  TRP A CZ2 1 
ATOM   424  C CZ3 . TRP A 1 53  ? 22.969 25.798 20.910 1.00 35.65  ? 50  TRP A CZ3 1 
ATOM   425  C CH2 . TRP A 1 53  ? 23.814 26.871 20.629 1.00 35.11  ? 50  TRP A CH2 1 
ATOM   426  N N   . TYR A 1 54  ? 21.071 20.710 18.034 1.00 37.65  ? 51  TYR A N   1 
ATOM   427  C CA  . TYR A 1 54  ? 20.374 19.449 18.198 1.00 37.82  ? 51  TYR A CA  1 
ATOM   428  C C   . TYR A 1 54  ? 19.483 19.414 19.430 1.00 39.89  ? 51  TYR A C   1 
ATOM   429  O O   . TYR A 1 54  ? 19.638 20.194 20.371 1.00 36.69  ? 51  TYR A O   1 
ATOM   430  C CB  . TYR A 1 54  ? 21.355 18.294 18.431 1.00 38.30  ? 51  TYR A CB  1 
ATOM   431  C CG  . TYR A 1 54  ? 22.468 18.156 17.422 1.00 37.14  ? 51  TYR A CG  1 
ATOM   432  C CD1 . TYR A 1 54  ? 23.543 19.031 17.400 1.00 34.85  ? 51  TYR A CD1 1 
ATOM   433  C CD2 . TYR A 1 54  ? 22.385 17.210 16.417 1.00 36.00  ? 51  TYR A CD2 1 
ATOM   434  C CE1 . TYR A 1 54  ? 24.553 18.909 16.463 1.00 35.80  ? 51  TYR A CE1 1 
ATOM   435  C CE2 . TYR A 1 54  ? 23.376 17.087 15.457 1.00 34.55  ? 51  TYR A CE2 1 
ATOM   436  C CZ  . TYR A 1 54  ? 24.465 17.932 15.484 1.00 34.78  ? 51  TYR A CZ  1 
ATOM   437  O OH  . TYR A 1 54  ? 25.417 17.775 14.514 1.00 36.62  ? 51  TYR A OH  1 
ATOM   438  N N   . LEU A 1 55  ? 18.526 18.481 19.389 1.00 42.83  ? 52  LEU A N   1 
ATOM   439  C CA  . LEU A 1 55  ? 17.678 18.195 20.525 1.00 41.80  ? 52  LEU A CA  1 
ATOM   440  C C   . LEU A 1 55  ? 18.570 17.452 21.511 1.00 47.34  ? 52  LEU A C   1 
ATOM   441  O O   . LEU A 1 55  ? 19.492 16.747 21.081 1.00 44.56  ? 52  LEU A O   1 
ATOM   442  C CB  . LEU A 1 55  ? 16.523 17.281 20.091 1.00 46.96  ? 52  LEU A CB  1 
ATOM   443  C CG  . LEU A 1 55  ? 15.559 17.821 19.037 1.00 47.40  ? 52  LEU A CG  1 
ATOM   444  C CD1 . LEU A 1 55  ? 14.409 16.846 18.828 1.00 51.30  ? 52  LEU A CD1 1 
ATOM   445  C CD2 . LEU A 1 55  ? 15.004 19.173 19.435 1.00 48.08  ? 52  LEU A CD2 1 
ATOM   446  N N   . CYS A 1 56  ? 18.305 17.614 22.815 1.00 50.97  ? 53  CYS A N   1 
ATOM   447  C CA  . CYS A 1 56  ? 19.069 16.920 23.842 1.00 54.83  ? 53  CYS A CA  1 
ATOM   448  C C   . CYS A 1 56  ? 18.666 15.445 23.853 1.00 54.27  ? 53  CYS A C   1 
ATOM   449  O O   . CYS A 1 56  ? 17.654 15.088 23.257 1.00 56.90  ? 53  CYS A O   1 
ATOM   450  C CB  . CYS A 1 56  ? 18.854 17.584 25.197 1.00 59.19  ? 53  CYS A CB  1 
ATOM   451  S SG  . CYS A 1 56  ? 19.359 19.325 25.198 1.00 59.19  ? 53  CYS A SG  1 
ATOM   452  N N   . GLY A 1 57  ? 19.455 14.591 24.527 1.00 54.98  ? 54  GLY A N   1 
ATOM   453  C CA  . GLY A 1 57  ? 19.163 13.165 24.573 1.00 59.85  ? 54  GLY A CA  1 
ATOM   454  C C   . GLY A 1 57  ? 19.979 12.403 25.619 1.00 62.17  ? 54  GLY A C   1 
ATOM   455  O O   . GLY A 1 57  ? 20.946 12.929 26.165 1.00 60.81  ? 54  GLY A O   1 
ATOM   456  N N   . ASP A 1 58  ? 19.586 11.136 25.840 1.00 71.29  ? 55  ASP A N   1 
ATOM   457  C CA  . ASP A 1 58  ? 20.202 10.246 26.816 1.00 72.93  ? 55  ASP A CA  1 
ATOM   458  C C   . ASP A 1 58  ? 21.572 9.781  26.324 1.00 64.54  ? 55  ASP A C   1 
ATOM   459  O O   . ASP A 1 58  ? 22.606 10.228 26.821 1.00 64.60  ? 55  ASP A O   1 
ATOM   460  C CB  . ASP A 1 58  ? 19.317 9.020  27.070 1.00 79.34  ? 55  ASP A CB  1 
ATOM   461  C CG  . ASP A 1 58  ? 17.909 9.345  27.536 1.00 89.07  ? 55  ASP A CG  1 
ATOM   462  O OD1 . ASP A 1 58  ? 17.604 10.548 27.694 1.00 91.29  ? 55  ASP A OD1 1 
ATOM   463  O OD2 . ASP A 1 58  ? 17.119 8.392  27.706 1.00 88.84  ? 55  ASP A OD2 1 
ATOM   464  N N   . SER A 1 59  ? 21.562 8.835  25.378 1.00 58.03  ? 56  SER A N   1 
ATOM   465  C CA  . SER A 1 59  ? 22.804 8.337  24.814 1.00 53.85  ? 56  SER A CA  1 
ATOM   466  C C   . SER A 1 59  ? 23.376 9.429  23.921 1.00 47.16  ? 56  SER A C   1 
ATOM   467  O O   . SER A 1 59  ? 22.671 10.368 23.561 1.00 44.56  ? 56  SER A O   1 
ATOM   468  C CB  . SER A 1 59  ? 22.580 7.087  24.028 1.00 59.42  ? 56  SER A CB  1 
ATOM   469  O OG  . SER A 1 59  ? 21.740 7.354  22.916 1.00 61.24  ? 56  SER A OG  1 
ATOM   470  N N   . LEU A 1 60  ? 24.655 9.312  23.573 1.00 48.72  ? 57  LEU A N   1 
ATOM   471  C CA  . LEU A 1 60  ? 25.220 10.313 22.691 1.00 46.24  ? 57  LEU A CA  1 
ATOM   472  C C   . LEU A 1 60  ? 24.559 10.170 21.318 1.00 45.15  ? 57  LEU A C   1 
ATOM   473  O O   . LEU A 1 60  ? 24.357 11.159 20.623 1.00 41.75  ? 57  LEU A O   1 
ATOM   474  C CB  . LEU A 1 60  ? 26.743 10.157 22.645 1.00 47.37  ? 57  LEU A CB  1 
ATOM   475  C CG  . LEU A 1 60  ? 27.470 11.133 21.723 1.00 47.56  ? 57  LEU A CG  1 
ATOM   476  C CD1 . LEU A 1 60  ? 27.364 12.554 22.245 1.00 46.50  ? 57  LEU A CD1 1 
ATOM   477  C CD2 . LEU A 1 60  ? 28.935 10.741 21.581 1.00 47.97  ? 57  LEU A CD2 1 
ATOM   478  N N   . ARG A 1 61  ? 24.167 8.944  20.961 1.00 43.85  ? 58  ARG A N   1 
ATOM   479  C CA  . ARG A 1 61  ? 23.523 8.713  19.674 1.00 46.04  ? 58  ARG A CA  1 
ATOM   480  C C   . ARG A 1 61  ? 22.195 9.468  19.627 1.00 47.46  ? 58  ARG A C   1 
ATOM   481  O O   . ARG A 1 61  ? 21.890 10.160 18.656 1.00 46.06  ? 58  ARG A O   1 
ATOM   482  C CB  . ARG A 1 61  ? 23.394 7.207  19.411 1.00 47.72  ? 58  ARG A CB  1 
ATOM   483  C CG  . ARG A 1 61  ? 22.682 6.832  18.116 1.00 47.50  ? 58  ARG A CG  1 
ATOM   484  C CD  . ARG A 1 61  ? 22.926 5.370  17.759 1.00 49.43  ? 58  ARG A CD  1 
ATOM   485  N NE  . ARG A 1 61  ? 22.518 4.456  18.815 1.00 51.21  ? 58  ARG A NE  1 
ATOM   486  C CZ  . ARG A 1 61  ? 22.859 3.181  18.879 1.00 53.66  ? 58  ARG A CZ  1 
ATOM   487  N NH1 . ARG A 1 61  ? 23.694 2.672  17.993 1.00 54.79  ? 58  ARG A NH1 1 
ATOM   488  N NH2 . ARG A 1 61  ? 22.424 2.430  19.879 1.00 56.80  ? 58  ARG A NH2 1 
ATOM   489  N N   . ASP A 1 62  ? 21.427 9.366  20.709 1.00 47.17  ? 59  ASP A N   1 
ATOM   490  C CA  . ASP A 1 62  ? 20.141 10.032 20.789 1.00 49.90  ? 59  ASP A CA  1 
ATOM   491  C C   . ASP A 1 62  ? 20.303 11.552 20.714 1.00 48.42  ? 59  ASP A C   1 
ATOM   492  O O   . ASP A 1 62  ? 19.503 12.226 20.070 1.00 50.19  ? 59  ASP A O   1 
ATOM   493  C CB  . ASP A 1 62  ? 19.459 9.663  22.112 1.00 59.10  ? 59  ASP A CB  1 
ATOM   494  C CG  . ASP A 1 62  ? 18.065 10.235 22.308 1.00 66.64  ? 59  ASP A CG  1 
ATOM   495  O OD1 . ASP A 1 62  ? 17.529 10.822 21.351 1.00 71.77  ? 59  ASP A OD1 1 
ATOM   496  O OD2 . ASP A 1 62  ? 17.549 10.135 23.445 1.00 79.07  ? 59  ASP A OD2 1 
ATOM   497  N N   . ALA A 1 63  ? 21.347 12.083 21.367 1.00 42.45  ? 60  ALA A N   1 
ATOM   498  C CA  . ALA A 1 63  ? 21.563 13.523 21.464 1.00 41.30  ? 60  ALA A CA  1 
ATOM   499  C C   . ALA A 1 63  ? 22.087 14.175 20.179 1.00 39.30  ? 60  ALA A C   1 
ATOM   500  O O   . ALA A 1 63  ? 22.116 15.405 20.093 1.00 38.60  ? 60  ALA A O   1 
ATOM   501  C CB  . ALA A 1 63  ? 22.509 13.794 22.605 1.00 42.55  ? 60  ALA A CB  1 
ATOM   502  N N   . LEU A 1 64  ? 22.491 13.369 19.189 1.00 38.55  ? 61  LEU A N   1 
ATOM   503  C CA  . LEU A 1 64  ? 23.027 13.884 17.934 1.00 38.53  ? 61  LEU A CA  1 
ATOM   504  C C   . LEU A 1 64  ? 22.185 13.437 16.737 1.00 38.46  ? 61  LEU A C   1 
ATOM   505  O O   . LEU A 1 64  ? 22.546 13.701 15.588 1.00 38.69  ? 61  LEU A O   1 
ATOM   506  C CB  . LEU A 1 64  ? 24.470 13.380 17.793 1.00 37.24  ? 61  LEU A CB  1 
ATOM   507  C CG  . LEU A 1 64  ? 25.485 13.971 18.765 1.00 36.64  ? 61  LEU A CG  1 
ATOM   508  C CD1 . LEU A 1 64  ? 26.882 13.424 18.507 1.00 36.25  ? 61  LEU A CD1 1 
ATOM   509  C CD2 . LEU A 1 64  ? 25.506 15.491 18.641 1.00 36.67  ? 61  LEU A CD2 1 
ATOM   510  N N   . SER A 1 65  ? 21.045 12.778 16.994 1.00 38.59  ? 62  SER A N   1 
ATOM   511  C CA  . SER A 1 65  ? 20.212 12.270 15.910 1.00 39.72  ? 62  SER A CA  1 
ATOM   512  C C   . SER A 1 65  ? 19.293 13.326 15.293 1.00 40.14  ? 62  SER A C   1 
ATOM   513  O O   . SER A 1 65  ? 18.873 13.166 14.145 1.00 42.40  ? 62  SER A O   1 
ATOM   514  C CB  . SER A 1 65  ? 19.361 11.110 16.373 1.00 40.86  ? 62  SER A CB  1 
ATOM   515  O OG  . SER A 1 65  ? 20.139 9.977  16.714 1.00 42.84  ? 62  SER A OG  1 
ATOM   516  N N   . HIS A 1 66  ? 18.974 14.387 16.046 1.00 40.42  ? 63  HIS A N   1 
ATOM   517  C CA  . HIS A 1 66  ? 18.002 15.363 15.573 1.00 40.82  ? 63  HIS A CA  1 
ATOM   518  C C   . HIS A 1 66  ? 18.625 16.753 15.438 1.00 37.91  ? 63  HIS A C   1 
ATOM   519  O O   . HIS A 1 66  ? 18.601 17.550 16.371 1.00 38.96  ? 63  HIS A O   1 
ATOM   520  C CB  . HIS A 1 66  ? 16.805 15.367 16.530 1.00 42.52  ? 63  HIS A CB  1 
ATOM   521  C CG  . HIS A 1 66  ? 16.225 14.006 16.722 1.00 44.52  ? 63  HIS A CG  1 
ATOM   522  N ND1 . HIS A 1 66  ? 15.681 13.225 15.726 1.00 48.58  ? 63  HIS A ND1 1 
ATOM   523  C CD2 . HIS A 1 66  ? 16.134 13.283 17.845 1.00 47.16  ? 63  HIS A CD2 1 
ATOM   524  C CE1 . HIS A 1 66  ? 15.277 12.072 16.245 1.00 48.00  ? 63  HIS A CE1 1 
ATOM   525  N NE2 . HIS A 1 66  ? 15.550 12.090 17.531 1.00 45.92  ? 63  HIS A NE2 1 
ATOM   526  N N   . ASN A 1 67  ? 19.119 17.029 14.229 1.00 38.67  ? 64  ASN A N   1 
ATOM   527  C CA  . ASN A 1 67  ? 19.765 18.281 13.882 1.00 37.35  ? 64  ASN A CA  1 
ATOM   528  C C   . ASN A 1 67  ? 18.684 19.257 13.416 1.00 38.92  ? 64  ASN A C   1 
ATOM   529  O O   . ASN A 1 67  ? 18.166 19.118 12.306 1.00 40.20  ? 64  ASN A O   1 
ATOM   530  C CB  . ASN A 1 67  ? 20.794 18.023 12.788 1.00 39.43  ? 64  ASN A CB  1 
ATOM   531  C CG  . ASN A 1 67  ? 21.614 19.243 12.465 1.00 37.69  ? 64  ASN A CG  1 
ATOM   532  O OD1 . ASN A 1 67  ? 21.074 20.346 12.377 1.00 39.21  ? 64  ASN A OD1 1 
ATOM   533  N ND2 . ASN A 1 67  ? 22.921 19.066 12.408 1.00 36.52  ? 64  ASN A ND2 1 
ATOM   534  N N   . VAL A 1 68  ? 18.348 20.243 14.261 1.00 40.28  ? 65  VAL A N   1 
ATOM   535  C CA  . VAL A 1 68  ? 17.274 21.178 13.954 1.00 40.75  ? 65  VAL A CA  1 
ATOM   536  C C   . VAL A 1 68  ? 17.697 22.187 12.887 1.00 44.23  ? 65  VAL A C   1 
ATOM   537  O O   . VAL A 1 68  ? 16.832 22.825 12.288 1.00 44.17  ? 65  VAL A O   1 
ATOM   538  C CB  . VAL A 1 68  ? 16.757 21.899 15.215 1.00 44.84  ? 65  VAL A CB  1 
ATOM   539  C CG1 . VAL A 1 68  ? 16.268 20.904 16.256 1.00 46.74  ? 65  VAL A CG1 1 
ATOM   540  C CG2 . VAL A 1 68  ? 17.788 22.833 15.821 1.00 41.22  ? 65  VAL A CG2 1 
ATOM   541  N N   . THR A 1 69  ? 19.009 22.366 12.690 1.00 40.62  ? 66  THR A N   1 
ATOM   542  C CA  . THR A 1 69  ? 19.510 23.271 11.663 1.00 41.91  ? 66  THR A CA  1 
ATOM   543  C C   . THR A 1 69  ? 19.445 22.600 10.287 1.00 44.26  ? 66  THR A C   1 
ATOM   544  O O   . THR A 1 69  ? 19.552 23.278 9.268  1.00 48.75  ? 66  THR A O   1 
ATOM   545  C CB  . THR A 1 69  ? 20.859 23.883 12.073 1.00 40.68  ? 66  THR A CB  1 
ATOM   546  O OG1 . THR A 1 69  ? 21.709 22.875 12.622 1.00 39.73  ? 66  THR A OG1 1 
ATOM   547  C CG2 . THR A 1 69  ? 20.710 24.939 13.143 1.00 42.02  ? 66  THR A CG2 1 
ATOM   548  N N   . GLU A 1 70  ? 19.275 21.270 10.249 1.00 42.54  ? 67  GLU A N   1 
ATOM   549  C CA  . GLU A 1 70  ? 19.103 20.569 8.983  1.00 44.99  ? 67  GLU A CA  1 
ATOM   550  C C   . GLU A 1 70  ? 17.628 20.284 8.739  1.00 47.79  ? 67  GLU A C   1 
ATOM   551  O O   . GLU A 1 70  ? 17.157 20.355 7.608  1.00 54.13  ? 67  GLU A O   1 
ATOM   552  C CB  . GLU A 1 70  ? 19.780 19.197 8.929  1.00 51.39  ? 67  GLU A CB  1 
ATOM   553  C CG  . GLU A 1 70  ? 21.289 19.210 8.831  1.00 56.55  ? 67  GLU A CG  1 
ATOM   554  C CD  . GLU A 1 70  ? 21.881 17.813 8.697  1.00 62.15  ? 67  GLU A CD  1 
ATOM   555  O OE1 . GLU A 1 70  ? 21.112 16.828 8.787  1.00 67.45  ? 67  GLU A OE1 1 
ATOM   556  O OE2 . GLU A 1 70  ? 23.093 17.709 8.438  1.00 70.93  ? 67  GLU A OE2 1 
ATOM   557  N N   . HIS A 1 71  ? 16.925 19.913 9.810  1.00 46.25  ? 68  HIS A N   1 
ATOM   558  C CA  . HIS A 1 71  ? 15.525 19.540 9.729  1.00 48.93  ? 68  HIS A CA  1 
ATOM   559  C C   . HIS A 1 71  ? 14.696 20.454 10.626 1.00 50.60  ? 68  HIS A C   1 
ATOM   560  O O   . HIS A 1 71  ? 14.516 20.171 11.811 1.00 49.62  ? 68  HIS A O   1 
ATOM   561  C CB  . HIS A 1 71  ? 15.399 18.061 10.099 1.00 51.32  ? 68  HIS A CB  1 
ATOM   562  C CG  . HIS A 1 71  ? 16.208 17.171 9.211  1.00 53.87  ? 68  HIS A CG  1 
ATOM   563  N ND1 . HIS A 1 71  ? 17.216 16.361 9.683  1.00 54.77  ? 68  HIS A ND1 1 
ATOM   564  C CD2 . HIS A 1 71  ? 16.167 16.976 7.889  1.00 57.86  ? 68  HIS A CD2 1 
ATOM   565  C CE1 . HIS A 1 71  ? 17.754 15.697 8.672  1.00 55.74  ? 68  HIS A CE1 1 
ATOM   566  N NE2 . HIS A 1 71  ? 17.128 16.052 7.572  1.00 57.83  ? 68  HIS A NE2 1 
ATOM   567  N N   . ARG A 1 72  ? 14.175 21.523 10.014 1.00 59.00  ? 69  ARG A N   1 
ATOM   568  C CA  . ARG A 1 72  ? 13.394 22.556 10.682 1.00 65.66  ? 69  ARG A CA  1 
ATOM   569  C C   . ARG A 1 72  ? 12.236 21.979 11.497 1.00 65.38  ? 69  ARG A C   1 
ATOM   570  O O   . ARG A 1 72  ? 11.951 22.465 12.590 1.00 65.21  ? 69  ARG A O   1 
ATOM   571  C CB  . ARG A 1 72  ? 12.788 23.504 9.640  1.00 79.21  ? 69  ARG A CB  1 
ATOM   572  C CG  . ARG A 1 72  ? 13.788 24.101 8.659  1.00 91.07  ? 69  ARG A CG  1 
ATOM   573  C CD  . ARG A 1 72  ? 13.109 24.983 7.625  1.00 104.44 ? 69  ARG A CD  1 
ATOM   574  N NE  . ARG A 1 72  ? 14.001 25.459 6.569  1.00 116.11 ? 69  ARG A NE  1 
ATOM   575  C CZ  . ARG A 1 72  ? 15.101 26.187 6.749  1.00 118.73 ? 69  ARG A CZ  1 
ATOM   576  N NH1 . ARG A 1 72  ? 15.816 26.563 5.705  1.00 113.38 ? 69  ARG A NH1 1 
ATOM   577  N NH2 . ARG A 1 72  ? 15.484 26.545 7.963  1.00 120.02 ? 69  ARG A NH2 1 
ATOM   578  N N   . GLN A 1 73  ? 11.554 20.956 10.961 1.00 63.38  ? 70  GLN A N   1 
ATOM   579  C CA  . GLN A 1 73  ? 10.396 20.407 11.655 1.00 66.42  ? 70  GLN A CA  1 
ATOM   580  C C   . GLN A 1 73  ? 10.784 19.826 13.017 1.00 63.77  ? 70  GLN A C   1 
ATOM   581  O O   . GLN A 1 73  ? 9.909  19.586 13.846 1.00 67.28  ? 70  GLN A O   1 
ATOM   582  C CB  . GLN A 1 73  ? 9.627  19.364 10.828 1.00 70.73  ? 70  GLN A CB  1 
ATOM   583  C CG  . GLN A 1 73  ? 10.368 18.071 10.488 1.00 79.07  ? 70  GLN A CG  1 
ATOM   584  C CD  . GLN A 1 73  ? 11.497 18.186 9.492  1.00 83.27  ? 70  GLN A CD  1 
ATOM   585  O OE1 . GLN A 1 73  ? 11.787 19.253 8.954  1.00 80.60  ? 70  GLN A OE1 1 
ATOM   586  N NE2 . GLN A 1 73  ? 12.121 17.055 9.202  1.00 87.78  ? 70  GLN A NE2 1 
ATOM   587  N N   . ASP A 1 74  ? 12.083 19.603 13.258 1.00 59.31  ? 71  ASP A N   1 
ATOM   588  C CA  . ASP A 1 74  ? 12.485 19.070 14.550 1.00 59.23  ? 71  ASP A CA  1 
ATOM   589  C C   . ASP A 1 74  ? 12.256 20.108 15.653 1.00 59.81  ? 71  ASP A C   1 
ATOM   590  O O   . ASP A 1 74  ? 12.005 19.726 16.791 1.00 64.49  ? 71  ASP A O   1 
ATOM   591  C CB  . ASP A 1 74  ? 13.936 18.585 14.566 1.00 55.62  ? 71  ASP A CB  1 
ATOM   592  C CG  . ASP A 1 74  ? 14.254 17.421 13.643 1.00 57.56  ? 71  ASP A CG  1 
ATOM   593  O OD1 . ASP A 1 74  ? 13.337 16.940 12.935 1.00 60.26  ? 71  ASP A OD1 1 
ATOM   594  O OD2 . ASP A 1 74  ? 15.429 16.996 13.651 1.00 55.89  ? 71  ASP A OD2 1 
ATOM   595  N N   . LEU A 1 75  ? 12.343 21.409 15.330 1.00 60.02  ? 72  LEU A N   1 
ATOM   596  C CA  . LEU A 1 75  ? 12.132 22.451 16.336 1.00 62.82  ? 72  LEU A CA  1 
ATOM   597  C C   . LEU A 1 75  ? 10.854 22.216 17.133 1.00 67.42  ? 72  LEU A C   1 
ATOM   598  O O   . LEU A 1 75  ? 10.853 22.365 18.354 1.00 64.26  ? 72  LEU A O   1 
ATOM   599  C CB  . LEU A 1 75  ? 12.078 23.838 15.685 1.00 68.66  ? 72  LEU A CB  1 
ATOM   600  C CG  . LEU A 1 75  ? 13.404 24.443 15.235 1.00 68.14  ? 72  LEU A CG  1 
ATOM   601  C CD1 . LEU A 1 75  ? 13.210 25.900 14.839 1.00 67.03  ? 72  LEU A CD1 1 
ATOM   602  C CD2 . LEU A 1 75  ? 14.444 24.355 16.344 1.00 70.34  ? 72  LEU A CD2 1 
ATOM   603  N N   . ALA A 1 76  ? 9.771  21.869 16.430 1.00 64.34  ? 73  ALA A N   1 
ATOM   604  C CA  . ALA A 1 76  ? 8.485  21.633 17.065 1.00 70.02  ? 73  ALA A CA  1 
ATOM   605  C C   . ALA A 1 76  ? 8.566  20.459 18.041 1.00 75.47  ? 73  ALA A C   1 
ATOM   606  O O   . ALA A 1 76  ? 7.755  20.363 18.959 1.00 78.62  ? 73  ALA A O   1 
ATOM   607  C CB  . ALA A 1 76  ? 7.440  21.395 16.006 1.00 68.77  ? 73  ALA A CB  1 
ATOM   608  N N   . LYS A 1 77  ? 9.537  19.560 17.826 1.00 74.16  ? 74  LYS A N   1 
ATOM   609  C CA  . LYS A 1 77  ? 9.703  18.407 18.700 1.00 82.06  ? 74  LYS A CA  1 
ATOM   610  C C   . LYS A 1 77  ? 10.389 18.862 19.989 1.00 78.63  ? 74  LYS A C   1 
ATOM   611  O O   . LYS A 1 77  ? 10.134 18.311 21.057 1.00 80.54  ? 74  LYS A O   1 
ATOM   612  C CB  . LYS A 1 77  ? 10.475 17.296 17.978 1.00 87.97  ? 74  LYS A CB  1 
ATOM   613  C CG  . LYS A 1 77  ? 10.656 16.001 18.759 1.00 93.38  ? 74  LYS A CG  1 
ATOM   614  C CD  . LYS A 1 77  ? 11.431 14.948 17.988 1.00 100.11 ? 74  LYS A CD  1 
ATOM   615  C CE  . LYS A 1 77  ? 11.617 13.653 18.750 1.00 106.57 ? 74  LYS A CE  1 
ATOM   616  N NZ  . LYS A 1 77  ? 10.320 13.008 19.072 1.00 109.93 ? 74  LYS A NZ  1 
ATOM   617  N N   . ALA A 1 78  ? 11.277 19.859 19.872 1.00 70.94  ? 75  ALA A N   1 
ATOM   618  C CA  . ALA A 1 78  ? 11.956 20.407 21.036 1.00 71.36  ? 75  ALA A CA  1 
ATOM   619  C C   . ALA A 1 78  ? 10.907 21.029 21.953 1.00 80.64  ? 75  ALA A C   1 
ATOM   620  O O   . ALA A 1 78  ? 10.850 20.726 23.141 1.00 83.84  ? 75  ALA A O   1 
ATOM   621  C CB  . ALA A 1 78  ? 12.987 21.430 20.618 1.00 65.46  ? 75  ALA A CB  1 
ATOM   622  N N   . LEU A 1 79  ? 10.058 21.873 21.356 1.00 78.53  ? 76  LEU A N   1 
ATOM   623  C CA  . LEU A 1 79  ? 9.003  22.572 22.068 1.00 78.05  ? 76  LEU A CA  1 
ATOM   624  C C   . LEU A 1 79  ? 8.027  21.582 22.698 1.00 84.24  ? 76  LEU A C   1 
ATOM   625  O O   . LEU A 1 79  ? 7.756  21.667 23.892 1.00 85.09  ? 76  LEU A O   1 
ATOM   626  C CB  . LEU A 1 79  ? 8.302  23.506 21.076 1.00 77.99  ? 76  LEU A CB  1 
ATOM   627  C CG  . LEU A 1 79  ? 7.133  24.313 21.632 1.00 80.92  ? 76  LEU A CG  1 
ATOM   628  C CD1 . LEU A 1 79  ? 7.623  25.369 22.603 1.00 75.79  ? 76  LEU A CD1 1 
ATOM   629  C CD2 . LEU A 1 79  ? 6.354  24.963 20.502 1.00 82.45  ? 76  LEU A CD2 1 
ATOM   630  N N   . SER A 1 80  ? 7.528  20.636 21.891 1.00 91.13  ? 77  SER A N   1 
ATOM   631  C CA  . SER A 1 80  ? 6.565  19.637 22.338 1.00 88.47  ? 77  SER A CA  1 
ATOM   632  C C   . SER A 1 80  ? 7.080  18.843 23.540 1.00 91.17  ? 77  SER A C   1 
ATOM   633  O O   . SER A 1 80  ? 6.307  18.497 24.430 1.00 91.15  ? 77  SER A O   1 
ATOM   634  C CB  . SER A 1 80  ? 6.208  18.714 21.203 1.00 86.60  ? 77  SER A CB  1 
ATOM   635  O OG  . SER A 1 80  ? 5.292  17.725 21.633 1.00 89.58  ? 77  SER A OG  1 
ATOM   636  N N   . ARG A 1 81  ? 8.387  18.559 23.551 1.00 92.46  ? 78  ARG A N   1 
ATOM   637  C CA  . ARG A 1 81  ? 9.023  17.789 24.610 1.00 96.09  ? 78  ARG A CA  1 
ATOM   638  C C   . ARG A 1 81  ? 9.391  18.652 25.818 1.00 93.00  ? 78  ARG A C   1 
ATOM   639  O O   . ARG A 1 81  ? 9.241  18.219 26.959 1.00 92.16  ? 78  ARG A O   1 
ATOM   640  C CB  . ARG A 1 81  ? 10.351 17.214 24.103 1.00 103.48 ? 78  ARG A CB  1 
ATOM   641  C CG  . ARG A 1 81  ? 11.116 16.388 25.129 1.00 108.48 ? 78  ARG A CG  1 
ATOM   642  C CD  . ARG A 1 81  ? 12.537 16.098 24.682 1.00 110.80 ? 78  ARG A CD  1 
ATOM   643  N NE  . ARG A 1 81  ? 12.654 15.368 23.429 1.00 110.61 ? 78  ARG A NE  1 
ATOM   644  C CZ  . ARG A 1 81  ? 13.810 15.075 22.841 1.00 106.86 ? 78  ARG A CZ  1 
ATOM   645  N NH1 . ARG A 1 81  ? 14.950 15.487 23.371 1.00 95.77  ? 78  ARG A NH1 1 
ATOM   646  N NH2 . ARG A 1 81  ? 13.821 14.397 21.706 1.00 105.03 ? 78  ARG A NH2 1 
ATOM   647  N N   . ASP A 1 82  ? 9.876  19.871 25.549 1.00 82.08  ? 79  ASP A N   1 
ATOM   648  C CA  . ASP A 1 82  ? 10.405 20.754 26.580 1.00 80.70  ? 79  ASP A CA  1 
ATOM   649  C C   . ASP A 1 82  ? 9.373  21.723 27.159 1.00 84.53  ? 79  ASP A C   1 
ATOM   650  O O   . ASP A 1 82  ? 9.527  22.152 28.302 1.00 77.38  ? 79  ASP A O   1 
ATOM   651  C CB  . ASP A 1 82  ? 11.566 21.566 25.998 1.00 77.03  ? 79  ASP A CB  1 
ATOM   652  C CG  . ASP A 1 82  ? 12.653 20.710 25.363 1.00 76.36  ? 79  ASP A CG  1 
ATOM   653  O OD1 . ASP A 1 82  ? 12.538 19.460 25.422 1.00 78.14  ? 79  ASP A OD1 1 
ATOM   654  O OD2 . ASP A 1 82  ? 13.561 21.292 24.744 1.00 63.67  ? 79  ASP A OD2 1 
ATOM   655  N N   . ARG A 1 83  ? 8.341  22.085 26.385 1.00 88.58  ? 80  ARG A N   1 
ATOM   656  C CA  . ARG A 1 83  ? 7.368  23.055 26.871 1.00 95.30  ? 80  ARG A CA  1 
ATOM   657  C C   . ARG A 1 83  ? 6.790  22.620 28.216 1.00 105.44 ? 80  ARG A C   1 
ATOM   658  O O   . ARG A 1 83  ? 6.592  21.431 28.466 1.00 104.62 ? 80  ARG A O   1 
ATOM   659  C CB  . ARG A 1 83  ? 6.218  23.270 25.884 1.00 99.55  ? 80  ARG A CB  1 
ATOM   660  C CG  . ARG A 1 83  ? 5.341  22.051 25.628 1.00 100.93 ? 80  ARG A CG  1 
ATOM   661  C CD  . ARG A 1 83  ? 4.204  22.451 24.712 1.00 103.13 ? 80  ARG A CD  1 
ATOM   662  N NE  . ARG A 1 83  ? 3.442  23.513 25.359 1.00 106.79 ? 80  ARG A NE  1 
ATOM   663  C CZ  . ARG A 1 83  ? 3.327  24.759 24.908 1.00 103.92 ? 80  ARG A CZ  1 
ATOM   664  N NH1 . ARG A 1 83  ? 2.645  25.651 25.604 1.00 107.15 ? 80  ARG A NH1 1 
ATOM   665  N NH2 . ARG A 1 83  ? 3.924  25.125 23.786 1.00 100.35 ? 80  ARG A NH2 1 
ATOM   666  N N   . ARG A 1 84  ? 6.501  23.613 29.065 1.00 110.08 ? 81  ARG A N   1 
ATOM   667  C CA  . ARG A 1 84  ? 5.937  23.364 30.380 1.00 113.62 ? 81  ARG A CA  1 
ATOM   668  C C   . ARG A 1 84  ? 4.424  23.544 30.261 1.00 105.00 ? 81  ARG A C   1 
ATOM   669  O O   . ARG A 1 84  ? 3.939  23.981 29.218 1.00 96.06  ? 81  ARG A O   1 
ATOM   670  C CB  . ARG A 1 84  ? 6.585  24.297 31.408 1.00 120.44 ? 81  ARG A CB  1 
ATOM   671  C CG  . ARG A 1 84  ? 8.108  24.305 31.337 1.00 124.02 ? 81  ARG A CG  1 
ATOM   672  C CD  . ARG A 1 84  ? 8.782  25.084 32.452 1.00 126.34 ? 81  ARG A CD  1 
ATOM   673  N NE  . ARG A 1 84  ? 8.631  24.437 33.748 1.00 136.35 ? 81  ARG A NE  1 
ATOM   674  C CZ  . ARG A 1 84  ? 9.133  23.243 34.060 1.00 136.72 ? 81  ARG A CZ  1 
ATOM   675  N NH1 . ARG A 1 84  ? 9.855  22.573 33.179 1.00 133.19 ? 81  ARG A NH1 1 
ATOM   676  N NH2 . ARG A 1 84  ? 8.936  22.732 35.264 1.00 140.49 ? 81  ARG A NH2 1 
ATOM   677  N N   . THR A 1 85  ? 3.686  23.229 31.332 1.00 106.95 ? 82  THR A N   1 
ATOM   678  C CA  . THR A 1 85  ? 2.233  23.326 31.306 1.00 110.20 ? 82  THR A CA  1 
ATOM   679  C C   . THR A 1 85  ? 1.756  24.780 31.369 1.00 103.51 ? 82  THR A C   1 
ATOM   680  O O   . THR A 1 85  ? 0.551  25.020 31.345 1.00 115.51 ? 82  THR A O   1 
ATOM   681  C CB  . THR A 1 85  ? 1.602  22.503 32.438 1.00 118.50 ? 82  THR A CB  1 
ATOM   682  O OG1 . THR A 1 85  ? 2.057  23.030 33.685 1.00 125.44 ? 82  THR A OG1 1 
ATOM   683  C CG2 . THR A 1 85  ? 1.935  21.029 32.355 1.00 120.25 ? 82  THR A CG2 1 
ATOM   684  N N   . ARG A 1 86  ? 2.688  25.742 31.448 1.00 94.66  ? 83  ARG A N   1 
ATOM   685  C CA  . ARG A 1 86  ? 2.313  27.148 31.520 1.00 89.98  ? 83  ARG A CA  1 
ATOM   686  C C   . ARG A 1 86  ? 3.315  28.032 30.780 1.00 86.86  ? 83  ARG A C   1 
ATOM   687  O O   . ARG A 1 86  ? 3.385  29.232 31.047 1.00 84.71  ? 83  ARG A O   1 
ATOM   688  C CB  . ARG A 1 86  ? 2.249  27.600 32.983 1.00 94.64  ? 83  ARG A CB  1 
ATOM   689  C CG  . ARG A 1 86  ? 1.214  26.861 33.816 1.00 96.41  ? 83  ARG A CG  1 
ATOM   690  C CD  . ARG A 1 86  ? 1.290  27.222 35.282 1.00 99.00  ? 83  ARG A CD  1 
ATOM   691  N NE  . ARG A 1 86  ? 0.287  26.487 36.038 1.00 104.62 ? 83  ARG A NE  1 
ATOM   692  C CZ  . ARG A 1 86  ? 0.556  25.523 36.913 1.00 106.76 ? 83  ARG A CZ  1 
ATOM   693  N NH1 . ARG A 1 86  ? 1.796  25.089 37.067 1.00 105.64 ? 83  ARG A NH1 1 
ATOM   694  N NH2 . ARG A 1 86  ? -0.429 24.932 37.566 1.00 106.56 ? 83  ARG A NH2 1 
ATOM   695  N N   . ALA A 1 87  ? 4.091  27.459 29.850 1.00 77.50  ? 84  ALA A N   1 
ATOM   696  C CA  . ALA A 1 87  ? 5.047  28.306 29.154 1.00 70.19  ? 84  ALA A CA  1 
ATOM   697  C C   . ALA A 1 87  ? 5.719  27.591 27.987 1.00 66.26  ? 84  ALA A C   1 
ATOM   698  O O   . ALA A 1 87  ? 5.994  26.393 28.040 1.00 68.93  ? 84  ALA A O   1 
ATOM   699  C CB  . ALA A 1 87  ? 6.101  28.793 30.124 1.00 67.83  ? 84  ALA A CB  1 
ATOM   700  N N   . VAL A 1 88  ? 5.962  28.373 26.931 1.00 61.48  ? 85  VAL A N   1 
ATOM   701  C CA  . VAL A 1 88  ? 6.705  27.926 25.769 1.00 60.69  ? 85  VAL A CA  1 
ATOM   702  C C   . VAL A 1 88  ? 8.151  27.795 26.232 1.00 57.78  ? 85  VAL A C   1 
ATOM   703  O O   . VAL A 1 88  ? 8.660  28.703 26.887 1.00 53.23  ? 85  VAL A O   1 
ATOM   704  C CB  . VAL A 1 88  ? 6.571  28.937 24.611 1.00 61.63  ? 85  VAL A CB  1 
ATOM   705  C CG1 . VAL A 1 88  ? 7.584  28.699 23.498 1.00 63.25  ? 85  VAL A CG1 1 
ATOM   706  C CG2 . VAL A 1 88  ? 5.155  28.992 24.065 1.00 66.88  ? 85  VAL A CG2 1 
ATOM   707  N N   . GLU A 1 89  ? 8.788  26.654 25.952 1.00 56.86  ? 86  GLU A N   1 
ATOM   708  C CA  . GLU A 1 89  ? 10.175 26.495 26.355 1.00 56.42  ? 86  GLU A CA  1 
ATOM   709  C C   . GLU A 1 89  ? 10.887 25.528 25.421 1.00 54.24  ? 86  GLU A C   1 
ATOM   710  O O   . GLU A 1 89  ? 10.315 24.529 24.998 1.00 53.93  ? 86  GLU A O   1 
ATOM   711  C CB  . GLU A 1 89  ? 10.324 25.962 27.782 1.00 62.29  ? 86  GLU A CB  1 
ATOM   712  C CG  . GLU A 1 89  ? 11.784 25.831 28.196 1.00 66.19  ? 86  GLU A CG  1 
ATOM   713  C CD  . GLU A 1 89  ? 12.051 25.344 29.607 1.00 79.59  ? 86  GLU A CD  1 
ATOM   714  O OE1 . GLU A 1 89  ? 13.243 25.241 29.975 1.00 86.40  ? 86  GLU A OE1 1 
ATOM   715  O OE2 . GLU A 1 89  ? 11.077 25.069 30.331 1.00 79.56  ? 86  GLU A OE2 1 
ATOM   716  N N   . LEU A 1 90  ? 12.141 25.846 25.097 1.00 49.91  ? 87  LEU A N   1 
ATOM   717  C CA  . LEU A 1 90  ? 12.905 24.933 24.266 1.00 53.76  ? 87  LEU A CA  1 
ATOM   718  C C   . LEU A 1 90  ? 14.376 25.027 24.635 1.00 47.18  ? 87  LEU A C   1 
ATOM   719  O O   . LEU A 1 90  ? 14.888 26.094 24.986 1.00 43.98  ? 87  LEU A O   1 
ATOM   720  C CB  . LEU A 1 90  ? 12.616 25.146 22.775 1.00 64.07  ? 87  LEU A CB  1 
ATOM   721  C CG  . LEU A 1 90  ? 12.880 26.522 22.179 1.00 69.11  ? 87  LEU A CG  1 
ATOM   722  C CD1 . LEU A 1 90  ? 14.354 26.714 21.848 1.00 75.58  ? 87  LEU A CD1 1 
ATOM   723  C CD2 . LEU A 1 90  ? 12.019 26.723 20.942 1.00 73.59  ? 87  LEU A CD2 1 
ATOM   724  N N   . VAL A 1 91  ? 15.000 23.848 24.634 1.00 44.84  ? 88  VAL A N   1 
ATOM   725  C CA  . VAL A 1 91  ? 16.398 23.688 24.977 1.00 42.10  ? 88  VAL A CA  1 
ATOM   726  C C   . VAL A 1 91  ? 17.082 22.938 23.837 1.00 42.71  ? 88  VAL A C   1 
ATOM   727  O O   . VAL A 1 91  ? 16.584 21.923 23.364 1.00 43.93  ? 88  VAL A O   1 
ATOM   728  C CB  . VAL A 1 91  ? 16.522 22.956 26.325 1.00 47.71  ? 88  VAL A CB  1 
ATOM   729  C CG1 . VAL A 1 91  ? 17.958 22.573 26.648 1.00 51.86  ? 88  VAL A CG1 1 
ATOM   730  C CG2 . VAL A 1 91  ? 15.907 23.783 27.446 1.00 50.29  ? 88  VAL A CG2 1 
ATOM   731  N N   . LEU A 1 92  ? 18.212 23.481 23.390 1.00 40.02  ? 89  LEU A N   1 
ATOM   732  C CA  . LEU A 1 92  ? 18.993 22.905 22.310 1.00 40.65  ? 89  LEU A CA  1 
ATOM   733  C C   . LEU A 1 92  ? 20.451 22.901 22.738 1.00 37.76  ? 89  LEU A C   1 
ATOM   734  O O   . LEU A 1 92  ? 20.836 23.678 23.607 1.00 37.25  ? 89  LEU A O   1 
ATOM   735  C CB  . LEU A 1 92  ? 18.844 23.809 21.083 1.00 40.39  ? 89  LEU A CB  1 
ATOM   736  C CG  . LEU A 1 92  ? 17.448 23.953 20.486 1.00 39.50  ? 89  LEU A CG  1 
ATOM   737  C CD1 . LEU A 1 92  ? 17.490 24.914 19.313 1.00 42.46  ? 89  LEU A CD1 1 
ATOM   738  C CD2 . LEU A 1 92  ? 16.913 22.606 20.019 1.00 42.53  ? 89  LEU A CD2 1 
ATOM   739  N N   . TRP A 1 93  ? 21.250 22.006 22.155 1.00 36.32  ? 90  TRP A N   1 
ATOM   740  C CA  . TRP A 1 93  ? 22.678 22.025 22.417 1.00 37.65  ? 90  TRP A CA  1 
ATOM   741  C C   . TRP A 1 93  ? 23.364 21.986 21.053 1.00 36.28  ? 90  TRP A C   1 
ATOM   742  O O   . TRP A 1 93  ? 22.739 21.594 20.063 1.00 36.01  ? 90  TRP A O   1 
ATOM   743  C CB  . TRP A 1 93  ? 23.134 20.914 23.365 1.00 37.88  ? 90  TRP A CB  1 
ATOM   744  C CG  . TRP A 1 93  ? 23.178 19.536 22.794 1.00 36.56  ? 90  TRP A CG  1 
ATOM   745  C CD1 . TRP A 1 93  ? 22.173 18.823 22.213 1.00 38.60  ? 90  TRP A CD1 1 
ATOM   746  C CD2 . TRP A 1 93  ? 24.328 18.681 22.806 1.00 37.54  ? 90  TRP A CD2 1 
ATOM   747  N NE1 . TRP A 1 93  ? 22.626 17.585 21.850 1.00 41.32  ? 90  TRP A NE1 1 
ATOM   748  C CE2 . TRP A 1 93  ? 23.947 17.469 22.197 1.00 39.19  ? 90  TRP A CE2 1 
ATOM   749  C CE3 . TRP A 1 93  ? 25.640 18.829 23.265 1.00 38.29  ? 90  TRP A CE3 1 
ATOM   750  C CZ2 . TRP A 1 93  ? 24.840 16.410 22.041 1.00 41.86  ? 90  TRP A CZ2 1 
ATOM   751  C CZ3 . TRP A 1 93  ? 26.523 17.787 23.104 1.00 40.16  ? 90  TRP A CZ3 1 
ATOM   752  C CH2 . TRP A 1 93  ? 26.124 16.593 22.503 1.00 42.15  ? 90  TRP A CH2 1 
ATOM   753  N N   . ASN A 1 94  ? 24.634 22.386 20.999 1.00 35.27  ? 91  ASN A N   1 
ATOM   754  C CA  . ASN A 1 94  ? 25.298 22.487 19.707 1.00 33.86  ? 91  ASN A CA  1 
ATOM   755  C C   . ASN A 1 94  ? 26.087 21.225 19.340 1.00 34.82  ? 91  ASN A C   1 
ATOM   756  O O   . ASN A 1 94  ? 26.891 21.262 18.411 1.00 34.69  ? 91  ASN A O   1 
ATOM   757  C CB  . ASN A 1 94  ? 26.200 23.715 19.621 1.00 35.84  ? 91  ASN A CB  1 
ATOM   758  C CG  . ASN A 1 94  ? 27.378 23.656 20.562 1.00 34.59  ? 91  ASN A CG  1 
ATOM   759  O OD1 . ASN A 1 94  ? 27.458 22.776 21.418 1.00 35.16  ? 91  ASN A OD1 1 
ATOM   760  N ND2 . ASN A 1 94  ? 28.277 24.614 20.425 1.00 36.33  ? 91  ASN A ND2 1 
ATOM   761  N N   . GLY A 1 95  ? 25.898 20.134 20.087 1.00 34.80  ? 92  GLY A N   1 
ATOM   762  C CA  . GLY A 1 95  ? 26.537 18.865 19.767 1.00 37.15  ? 92  GLY A CA  1 
ATOM   763  C C   . GLY A 1 95  ? 27.953 18.695 20.314 1.00 42.15  ? 92  GLY A C   1 
ATOM   764  O O   . GLY A 1 95  ? 28.567 17.644 20.098 1.00 42.28  ? 92  GLY A O   1 
ATOM   765  N N   . GLU A 1 96  ? 28.486 19.737 20.958 1.00 40.62  ? 93  GLU A N   1 
ATOM   766  C CA  . GLU A 1 96  ? 29.806 19.685 21.567 1.00 45.63  ? 93  GLU A CA  1 
ATOM   767  C C   . GLU A 1 96  ? 29.633 19.575 23.082 1.00 48.00  ? 93  GLU A C   1 
ATOM   768  O O   . GLU A 1 96  ? 28.989 20.422 23.705 1.00 45.14  ? 93  GLU A O   1 
ATOM   769  C CB  . GLU A 1 96  ? 30.639 20.905 21.172 1.00 47.79  ? 93  GLU A CB  1 
ATOM   770  C CG  . GLU A 1 96  ? 31.970 20.963 21.891 1.00 51.41  ? 93  GLU A CG  1 
ATOM   771  C CD  . GLU A 1 96  ? 32.838 19.736 21.677 1.00 58.72  ? 93  GLU A CD  1 
ATOM   772  O OE1 . GLU A 1 96  ? 33.094 19.012 22.671 1.00 60.78  ? 93  GLU A OE1 1 
ATOM   773  O OE2 . GLU A 1 96  ? 33.270 19.523 20.528 1.00 57.99  ? 93  GLU A OE2 1 
ATOM   774  N N   . GLU A 1 97  ? 30.228 18.522 23.657 1.00 57.49  ? 94  GLU A N   1 
ATOM   775  C CA  . GLU A 1 97  ? 30.160 18.226 25.082 1.00 59.01  ? 94  GLU A CA  1 
ATOM   776  C C   . GLU A 1 97  ? 31.010 19.153 25.943 1.00 51.74  ? 94  GLU A C   1 
ATOM   777  O O   . GLU A 1 97  ? 30.539 19.679 26.944 1.00 53.35  ? 94  GLU A O   1 
ATOM   778  C CB  . GLU A 1 97  ? 30.744 16.835 25.361 1.00 63.95  ? 94  GLU A CB  1 
ATOM   779  C CG  . GLU A 1 97  ? 29.938 15.669 24.826 1.00 69.72  ? 94  GLU A CG  1 
ATOM   780  C CD  . GLU A 1 97  ? 28.623 15.423 25.545 1.00 79.30  ? 94  GLU A CD  1 
ATOM   781  O OE1 . GLU A 1 97  ? 28.310 16.174 26.498 1.00 86.19  ? 94  GLU A OE1 1 
ATOM   782  O OE2 . GLU A 1 97  ? 27.930 14.456 25.173 1.00 73.34  ? 94  GLU A OE2 1 
ATOM   783  N N   . ASP A 1 98  ? 32.271 19.313 25.541 1.00 55.37  ? 95  ASP A N   1 
ATOM   784  C CA  . ASP A 1 98  ? 33.282 20.021 26.309 1.00 55.36  ? 95  ASP A CA  1 
ATOM   785  C C   . ASP A 1 98  ? 33.183 21.540 26.167 1.00 49.72  ? 95  ASP A C   1 
ATOM   786  O O   . ASP A 1 98  ? 33.269 22.076 25.067 1.00 48.37  ? 95  ASP A O   1 
ATOM   787  C CB  . ASP A 1 98  ? 34.653 19.507 25.858 1.00 58.82  ? 95  ASP A CB  1 
ATOM   788  C CG  . ASP A 1 98  ? 35.850 20.027 26.635 1.00 67.37  ? 95  ASP A CG  1 
ATOM   789  O OD1 . ASP A 1 98  ? 35.651 20.813 27.586 1.00 62.41  ? 95  ASP A OD1 1 
ATOM   790  O OD2 . ASP A 1 98  ? 36.978 19.624 26.282 1.00 72.86  ? 95  ASP A OD2 1 
ATOM   791  N N   . PRO A 1 99  ? 33.040 22.289 27.285 1.00 55.33  ? 96  PRO A N   1 
ATOM   792  C CA  . PRO A 1 99  ? 33.011 23.751 27.234 1.00 54.06  ? 96  PRO A CA  1 
ATOM   793  C C   . PRO A 1 99  ? 34.319 24.334 26.695 1.00 55.24  ? 96  PRO A C   1 
ATOM   794  O O   . PRO A 1 99  ? 34.357 25.464 26.217 1.00 57.36  ? 96  PRO A O   1 
ATOM   795  C CB  . PRO A 1 99  ? 32.806 24.159 28.703 1.00 57.02  ? 96  PRO A CB  1 
ATOM   796  C CG  . PRO A 1 99  ? 32.171 22.950 29.341 1.00 58.37  ? 96  PRO A CG  1 
ATOM   797  C CD  . PRO A 1 99  ? 32.815 21.774 28.644 1.00 59.23  ? 96  PRO A CD  1 
ATOM   798  N N   . LEU A 1 100 ? 35.399 23.549 26.774 1.00 53.51  ? 97  LEU A N   1 
ATOM   799  C CA  . LEU A 1 100 ? 36.696 24.000 26.297 1.00 54.47  ? 97  LEU A CA  1 
ATOM   800  C C   . LEU A 1 100 ? 36.743 23.978 24.770 1.00 55.45  ? 97  LEU A C   1 
ATOM   801  O O   . LEU A 1 100 ? 37.644 24.571 24.181 1.00 57.63  ? 97  LEU A O   1 
ATOM   802  C CB  . LEU A 1 100 ? 37.790 23.105 26.888 1.00 59.37  ? 97  LEU A CB  1 
ATOM   803  C CG  . LEU A 1 100 ? 37.846 23.047 28.414 1.00 61.42  ? 97  LEU A CG  1 
ATOM   804  C CD1 . LEU A 1 100 ? 39.159 22.438 28.881 1.00 64.33  ? 97  LEU A CD1 1 
ATOM   805  C CD2 . LEU A 1 100 ? 37.642 24.423 29.031 1.00 63.70  ? 97  LEU A CD2 1 
ATOM   806  N N   . LYS A 1 101 ? 35.776 23.300 24.132 1.00 52.47  ? 98  LYS A N   1 
ATOM   807  C CA  . LYS A 1 101 ? 35.754 23.222 22.678 1.00 53.87  ? 98  LYS A CA  1 
ATOM   808  C C   . LYS A 1 101 ? 34.520 23.923 22.109 1.00 49.33  ? 98  LYS A C   1 
ATOM   809  O O   . LYS A 1 101 ? 34.091 23.636 20.996 1.00 51.47  ? 98  LYS A O   1 
ATOM   810  C CB  . LYS A 1 101 ? 35.892 21.764 22.231 1.00 59.67  ? 98  LYS A CB  1 
ATOM   811  C CG  . LYS A 1 101 ? 37.216 21.126 22.640 1.00 68.48  ? 98  LYS A CG  1 
ATOM   812  C CD  . LYS A 1 101 ? 37.467 19.722 22.118 1.00 75.27  ? 98  LYS A CD  1 
ATOM   813  C CE  . LYS A 1 101 ? 36.478 18.684 22.603 1.00 79.95  ? 98  LYS A CE  1 
ATOM   814  N NZ  . LYS A 1 101 ? 36.812 17.339 22.076 1.00 79.90  ? 98  LYS A NZ  1 
ATOM   815  N N   . GLY A 1 102 ? 33.949 24.857 22.870 1.00 40.51  ? 99  GLY A N   1 
ATOM   816  C CA  . GLY A 1 102 ? 32.814 25.619 22.371 1.00 38.90  ? 99  GLY A CA  1 
ATOM   817  C C   . GLY A 1 102 ? 31.451 24.964 22.605 1.00 38.61  ? 99  GLY A C   1 
ATOM   818  O O   . GLY A 1 102 ? 30.480 25.334 21.946 1.00 38.22  ? 99  GLY A O   1 
ATOM   819  N N   . GLY A 1 103 ? 31.381 23.976 23.507 1.00 40.69  ? 100 GLY A N   1 
ATOM   820  C CA  . GLY A 1 103 ? 30.101 23.365 23.838 1.00 36.09  ? 100 GLY A CA  1 
ATOM   821  C C   . GLY A 1 103 ? 29.136 24.441 24.329 1.00 37.04  ? 100 GLY A C   1 
ATOM   822  O O   . GLY A 1 103 ? 29.525 25.298 25.119 1.00 36.46  ? 100 GLY A O   1 
ATOM   823  N N   . LEU A 1 104 ? 27.884 24.385 23.868 1.00 35.07  ? 101 LEU A N   1 
ATOM   824  C CA  . LEU A 1 104 ? 26.946 25.425 24.237 1.00 36.40  ? 101 LEU A CA  1 
ATOM   825  C C   . LEU A 1 104 ? 25.514 24.908 24.180 1.00 38.88  ? 101 LEU A C   1 
ATOM   826  O O   . LEU A 1 104 ? 25.179 24.040 23.373 1.00 37.21  ? 101 LEU A O   1 
ATOM   827  C CB  . LEU A 1 104 ? 27.165 26.576 23.247 1.00 39.69  ? 101 LEU A CB  1 
ATOM   828  C CG  . LEU A 1 104 ? 26.538 27.924 23.594 1.00 42.20  ? 101 LEU A CG  1 
ATOM   829  C CD1 . LEU A 1 104 ? 27.333 28.614 24.695 1.00 40.09  ? 101 LEU A CD1 1 
ATOM   830  C CD2 . LEU A 1 104 ? 26.476 28.810 22.359 1.00 40.91  ? 101 LEU A CD2 1 
ATOM   831  N N   A SER A 1 105 ? 24.682 25.451 25.074 0.50 37.22  ? 102 SER A N   1 
ATOM   832  N N   B SER A 1 105 ? 24.676 25.440 25.076 0.50 36.53  ? 102 SER A N   1 
ATOM   833  C CA  A SER A 1 105 ? 23.273 25.116 25.141 0.50 36.92  ? 102 SER A CA  1 
ATOM   834  C CA  B SER A 1 105 ? 23.267 25.101 25.095 0.50 35.84  ? 102 SER A CA  1 
ATOM   835  C C   A SER A 1 105 ? 22.470 26.407 25.053 0.50 35.72  ? 102 SER A C   1 
ATOM   836  C C   B SER A 1 105 ? 22.481 26.402 25.022 0.50 35.09  ? 102 SER A C   1 
ATOM   837  O O   A SER A 1 105 ? 22.944 27.472 25.455 0.50 33.80  ? 102 SER A O   1 
ATOM   838  O O   B SER A 1 105 ? 22.975 27.465 25.407 0.50 33.24  ? 102 SER A O   1 
ATOM   839  C CB  A SER A 1 105 ? 22.937 24.329 26.384 0.50 40.60  ? 102 SER A CB  1 
ATOM   840  C CB  B SER A 1 105 ? 22.871 24.272 26.293 0.50 38.66  ? 102 SER A CB  1 
ATOM   841  O OG  A SER A 1 105 ? 23.615 23.080 26.391 0.50 41.10  ? 102 SER A OG  1 
ATOM   842  O OG  B SER A 1 105 ? 23.053 24.987 27.501 0.50 36.91  ? 102 SER A OG  1 
ATOM   843  N N   . LEU A 1 106 ? 21.269 26.293 24.484 1.00 36.23  ? 103 LEU A N   1 
ATOM   844  C CA  . LEU A 1 106 ? 20.364 27.415 24.329 1.00 34.95  ? 103 LEU A CA  1 
ATOM   845  C C   . LEU A 1 106 ? 19.077 27.094 25.067 1.00 35.95  ? 103 LEU A C   1 
ATOM   846  O O   . LEU A 1 106 ? 18.548 25.991 24.950 1.00 39.44  ? 103 LEU A O   1 
ATOM   847  C CB  . LEU A 1 106 ? 20.169 27.640 22.825 1.00 38.15  ? 103 LEU A CB  1 
ATOM   848  C CG  . LEU A 1 106 ? 19.376 28.863 22.370 1.00 42.72  ? 103 LEU A CG  1 
ATOM   849  C CD1 . LEU A 1 106 ? 19.750 29.214 20.942 1.00 46.77  ? 103 LEU A CD1 1 
ATOM   850  C CD2 . LEU A 1 106 ? 17.874 28.616 22.431 1.00 50.66  ? 103 LEU A CD2 1 
ATOM   851  N N   . ASP A 1 107 ? 18.615 28.055 25.869 1.00 34.21  ? 104 ASP A N   1 
ATOM   852  C CA  . ASP A 1 107 ? 17.377 27.900 26.609 1.00 38.81  ? 104 ASP A CA  1 
ATOM   853  C C   . ASP A 1 107 ? 16.526 29.134 26.328 1.00 38.06  ? 104 ASP A C   1 
ATOM   854  O O   . ASP A 1 107 ? 16.906 30.258 26.653 1.00 39.32  ? 104 ASP A O   1 
ATOM   855  C CB  . ASP A 1 107 ? 17.610 27.711 28.110 1.00 43.17  ? 104 ASP A CB  1 
ATOM   856  C CG  . ASP A 1 107 ? 16.344 27.348 28.876 1.00 55.16  ? 104 ASP A CG  1 
ATOM   857  O OD1 . ASP A 1 107 ? 15.360 28.119 28.805 1.00 56.40  ? 104 ASP A OD1 1 
ATOM   858  O OD2 . ASP A 1 107 ? 16.357 26.304 29.557 1.00 67.44  ? 104 ASP A OD2 1 
ATOM   859  N N   . TYR A 1 108 ? 15.361 28.902 25.728 1.00 38.42  ? 105 TYR A N   1 
ATOM   860  C CA  . TYR A 1 108 ? 14.421 29.953 25.382 1.00 37.31  ? 105 TYR A CA  1 
ATOM   861  C C   . TYR A 1 108 ? 13.104 29.681 26.097 1.00 42.74  ? 105 TYR A C   1 
ATOM   862  O O   . TYR A 1 108 ? 12.619 28.558 26.080 1.00 44.21  ? 105 TYR A O   1 
ATOM   863  C CB  . TYR A 1 108 ? 14.191 29.947 23.871 1.00 39.16  ? 105 TYR A CB  1 
ATOM   864  C CG  . TYR A 1 108 ? 13.191 30.938 23.332 1.00 37.64  ? 105 TYR A CG  1 
ATOM   865  C CD1 . TYR A 1 108 ? 13.389 32.306 23.412 1.00 39.54  ? 105 TYR A CD1 1 
ATOM   866  C CD2 . TYR A 1 108 ? 12.012 30.493 22.751 1.00 44.26  ? 105 TYR A CD2 1 
ATOM   867  C CE1 . TYR A 1 108 ? 12.466 33.205 22.900 1.00 38.84  ? 105 TYR A CE1 1 
ATOM   868  C CE2 . TYR A 1 108 ? 11.082 31.375 22.231 1.00 44.70  ? 105 TYR A CE2 1 
ATOM   869  C CZ  . TYR A 1 108 ? 11.311 32.735 22.296 1.00 45.25  ? 105 TYR A CZ  1 
ATOM   870  O OH  . TYR A 1 108 ? 10.385 33.597 21.774 1.00 45.33  ? 105 TYR A OH  1 
ATOM   871  N N   . GLU A 1 109 ? 12.549 30.705 26.745 1.00 40.74  ? 106 GLU A N   1 
ATOM   872  C CA  . GLU A 1 109 ? 11.285 30.504 27.428 1.00 46.49  ? 106 GLU A CA  1 
ATOM   873  C C   . GLU A 1 109 ? 10.419 31.735 27.192 1.00 41.82  ? 106 GLU A C   1 
ATOM   874  O O   . GLU A 1 109 ? 10.924 32.842 27.085 1.00 42.11  ? 106 GLU A O   1 
ATOM   875  C CB  . GLU A 1 109 ? 11.555 30.208 28.906 1.00 52.40  ? 106 GLU A CB  1 
ATOM   876  C CG  . GLU A 1 109 ? 10.325 29.747 29.662 1.00 66.27  ? 106 GLU A CG  1 
ATOM   877  C CD  . GLU A 1 109 ? 10.585 29.355 31.105 1.00 76.31  ? 106 GLU A CD  1 
ATOM   878  O OE1 . GLU A 1 109 ? 11.749 29.488 31.550 1.00 72.98  ? 106 GLU A OE1 1 
ATOM   879  O OE2 . GLU A 1 109 ? 9.628  28.887 31.773 1.00 83.11  ? 106 GLU A OE2 1 
ATOM   880  N N   . ALA A 1 110 ? 9.109  31.519 27.058 1.00 45.49  ? 107 ALA A N   1 
ATOM   881  C CA  . ALA A 1 110 ? 8.158  32.599 26.858 1.00 47.91  ? 107 ALA A CA  1 
ATOM   882  C C   . ALA A 1 110 ? 6.913  32.228 27.650 1.00 52.22  ? 107 ALA A C   1 
ATOM   883  O O   . ALA A 1 110 ? 6.181  31.325 27.254 1.00 56.54  ? 107 ALA A O   1 
ATOM   884  C CB  . ALA A 1 110 ? 7.877  32.794 25.387 1.00 51.23  ? 107 ALA A CB  1 
ATOM   885  N N   . SER A 1 111 ? 6.684  32.931 28.761 1.00 53.41  ? 108 SER A N   1 
ATOM   886  C CA  . SER A 1 111 ? 5.592  32.570 29.652 1.00 56.07  ? 108 SER A CA  1 
ATOM   887  C C   . SER A 1 111 ? 4.595  33.690 29.923 1.00 59.04  ? 108 SER A C   1 
ATOM   888  O O   . SER A 1 111 ? 3.499  33.412 30.398 1.00 65.65  ? 108 SER A O   1 
ATOM   889  C CB  . SER A 1 111 ? 6.183  32.178 30.962 1.00 60.07  ? 108 SER A CB  1 
ATOM   890  O OG  . SER A 1 111 ? 6.702  33.335 31.608 1.00 57.14  ? 108 SER A OG  1 
ATOM   891  N N   . GLY A 1 112 ? 4.988  34.944 29.703 1.00 56.84  ? 109 GLY A N   1 
ATOM   892  C CA  . GLY A 1 112 ? 4.112  36.054 30.047 1.00 57.27  ? 109 GLY A CA  1 
ATOM   893  C C   . GLY A 1 112 ? 4.558  36.708 31.357 1.00 55.38  ? 109 GLY A C   1 
ATOM   894  O O   . GLY A 1 112 ? 3.934  37.652 31.831 1.00 53.89  ? 109 GLY A O   1 
ATOM   895  N N   . ARG A 1 113 ? 5.649  36.171 31.926 1.00 51.05  ? 110 ARG A N   1 
ATOM   896  C CA  . ARG A 1 113 ? 6.277  36.670 33.140 1.00 49.68  ? 110 ARG A CA  1 
ATOM   897  C C   . ARG A 1 113 ? 7.737  36.960 32.792 1.00 45.04  ? 110 ARG A C   1 
ATOM   898  O O   . ARG A 1 113 ? 8.349  36.195 32.052 1.00 44.65  ? 110 ARG A O   1 
ATOM   899  C CB  . ARG A 1 113 ? 6.078  35.644 34.254 1.00 52.72  ? 110 ARG A CB  1 
ATOM   900  C CG  . ARG A 1 113 ? 4.611  35.477 34.615 1.00 58.11  ? 110 ARG A CG  1 
ATOM   901  C CD  . ARG A 1 113 ? 4.281  34.270 35.451 1.00 62.87  ? 110 ARG A CD  1 
ATOM   902  N NE  . ARG A 1 113 ? 4.623  33.062 34.709 1.00 63.76  ? 110 ARG A NE  1 
ATOM   903  C CZ  . ARG A 1 113 ? 3.735  32.249 34.143 1.00 68.89  ? 110 ARG A CZ  1 
ATOM   904  N NH1 . ARG A 1 113 ? 2.468  32.613 34.058 1.00 72.17  ? 110 ARG A NH1 1 
ATOM   905  N NH2 . ARG A 1 113 ? 4.135  31.150 33.528 1.00 72.69  ? 110 ARG A NH2 1 
ATOM   906  N N   . ALA A 1 114 ? 8.276  38.056 33.347 1.00 43.44  ? 111 ALA A N   1 
ATOM   907  C CA  . ALA A 1 114 ? 9.628  38.510 33.036 1.00 42.88  ? 111 ALA A CA  1 
ATOM   908  C C   . ALA A 1 114 ? 10.681 37.427 33.261 1.00 42.10  ? 111 ALA A C   1 
ATOM   909  O O   . ALA A 1 114 ? 11.563 37.242 32.426 1.00 40.83  ? 111 ALA A O   1 
ATOM   910  C CB  . ALA A 1 114 ? 9.943  39.741 33.847 1.00 43.38  ? 111 ALA A CB  1 
ATOM   911  N N   . VAL A 1 115 ? 10.569 36.730 34.394 1.00 46.72  ? 112 VAL A N   1 
ATOM   912  C CA  . VAL A 1 115 ? 11.536 35.709 34.776 1.00 46.22  ? 112 VAL A CA  1 
ATOM   913  C C   . VAL A 1 115 ? 11.631 34.604 33.722 1.00 46.58  ? 112 VAL A C   1 
ATOM   914  O O   . VAL A 1 115 ? 12.708 34.062 33.496 1.00 47.64  ? 112 VAL A O   1 
ATOM   915  C CB  . VAL A 1 115 ? 11.179 35.128 36.162 1.00 49.54  ? 112 VAL A CB  1 
ATOM   916  C CG1 . VAL A 1 115 ? 9.800  34.480 36.177 1.00 51.69  ? 112 VAL A CG1 1 
ATOM   917  C CG2 . VAL A 1 115 ? 12.226 34.144 36.664 1.00 52.04  ? 112 VAL A CG2 1 
ATOM   918  N N   . SER A 1 116 ? 10.500 34.266 33.090 1.00 47.66  ? 113 SER A N   1 
ATOM   919  C CA  . SER A 1 116 ? 10.458 33.184 32.122 1.00 47.34  ? 113 SER A CA  1 
ATOM   920  C C   . SER A 1 116 ? 10.127 33.683 30.715 1.00 43.30  ? 113 SER A C   1 
ATOM   921  O O   . SER A 1 116 ? 9.431  33.019 29.949 1.00 45.51  ? 113 SER A O   1 
ATOM   922  C CB  . SER A 1 116 ? 9.519  32.120 32.611 1.00 49.24  ? 113 SER A CB  1 
ATOM   923  O OG  . SER A 1 116 ? 8.390  32.708 33.215 1.00 51.97  ? 113 SER A OG  1 
ATOM   924  N N   . SER A 1 117 ? 10.669 34.859 30.396 1.00 41.04  ? 114 SER A N   1 
ATOM   925  C CA  . SER A 1 117 ? 10.576 35.477 29.085 1.00 37.56  ? 114 SER A CA  1 
ATOM   926  C C   . SER A 1 117 ? 11.991 35.909 28.745 1.00 34.73  ? 114 SER A C   1 
ATOM   927  O O   . SER A 1 117 ? 12.334 37.075 28.922 1.00 37.09  ? 114 SER A O   1 
ATOM   928  C CB  . SER A 1 117 ? 9.628  36.637 29.057 1.00 39.17  ? 114 SER A CB  1 
ATOM   929  O OG  . SER A 1 117 ? 8.305  36.221 29.360 1.00 41.78  ? 114 SER A OG  1 
ATOM   930  N N   . ARG A 1 118 ? 12.803 34.945 28.296 1.00 35.61  ? 115 ARG A N   1 
ATOM   931  C CA  . ARG A 1 118 ? 14.196 35.260 28.057 1.00 36.46  ? 115 ARG A CA  1 
ATOM   932  C C   . ARG A 1 118 ? 14.883 34.194 27.213 1.00 35.49  ? 115 ARG A C   1 
ATOM   933  O O   . ARG A 1 118 ? 14.357 33.115 26.942 1.00 36.00  ? 115 ARG A O   1 
ATOM   934  C CB  . ARG A 1 118 ? 14.927 35.342 29.398 1.00 39.31  ? 115 ARG A CB  1 
ATOM   935  C CG  . ARG A 1 118 ? 15.025 34.015 30.132 1.00 45.57  ? 115 ARG A CG  1 
ATOM   936  C CD  . ARG A 1 118 ? 15.771 34.155 31.449 1.00 59.23  ? 115 ARG A CD  1 
ATOM   937  N NE  . ARG A 1 118 ? 16.050 32.860 32.060 1.00 70.95  ? 115 ARG A NE  1 
ATOM   938  C CZ  . ARG A 1 118 ? 15.130 31.959 32.388 1.00 74.01  ? 115 ARG A CZ  1 
ATOM   939  N NH1 . ARG A 1 118 ? 15.493 30.806 32.918 1.00 82.77  ? 115 ARG A NH1 1 
ATOM   940  N NH2 . ARG A 1 118 ? 13.851 32.202 32.171 1.00 83.86  ? 115 ARG A NH2 1 
ATOM   941  N N   . LEU A 1 119 ? 16.119 34.521 26.845 1.00 33.01  ? 116 LEU A N   1 
ATOM   942  C CA  . LEU A 1 119 ? 16.958 33.651 26.048 1.00 31.93  ? 116 LEU A CA  1 
ATOM   943  C C   . LEU A 1 119 ? 18.322 33.586 26.710 1.00 31.66  ? 116 LEU A C   1 
ATOM   944  O O   . LEU A 1 119 ? 18.878 34.614 27.067 1.00 33.25  ? 116 LEU A O   1 
ATOM   945  C CB  . LEU A 1 119 ? 17.057 34.229 24.634 1.00 34.56  ? 116 LEU A CB  1 
ATOM   946  C CG  . LEU A 1 119 ? 18.028 33.520 23.688 1.00 36.93  ? 116 LEU A CG  1 
ATOM   947  C CD1 . LEU A 1 119 ? 17.536 32.140 23.328 1.00 37.23  ? 116 LEU A CD1 1 
ATOM   948  C CD2 . LEU A 1 119 ? 18.228 34.339 22.423 1.00 41.10  ? 116 LEU A CD2 1 
ATOM   949  N N   . GLN A 1 120 ? 18.837 32.371 26.888 1.00 35.77  ? 117 GLN A N   1 
ATOM   950  C CA  . GLN A 1 120 ? 20.139 32.259 27.509 1.00 39.27  ? 117 GLN A CA  1 
ATOM   951  C C   . GLN A 1 120 ? 20.999 31.268 26.732 1.00 35.76  ? 117 GLN A C   1 
ATOM   952  O O   . GLN A 1 120 ? 20.488 30.287 26.199 1.00 36.13  ? 117 GLN A O   1 
ATOM   953  C CB  . GLN A 1 120 ? 19.957 31.889 28.980 1.00 47.70  ? 117 GLN A CB  1 
ATOM   954  C CG  . GLN A 1 120 ? 21.247 31.950 29.781 1.00 64.11  ? 117 GLN A CG  1 
ATOM   955  C CD  . GLN A 1 120 ? 21.013 31.911 31.273 1.00 68.15  ? 117 GLN A CD  1 
ATOM   956  O OE1 . GLN A 1 120 ? 19.876 31.882 31.742 1.00 74.55  ? 117 GLN A OE1 1 
ATOM   957  N NE2 . GLN A 1 120 ? 22.095 31.969 32.034 1.00 62.06  ? 117 GLN A NE2 1 
ATOM   958  N N   . LEU A 1 121 ? 22.278 31.631 26.570 1.00 36.44  ? 118 LEU A N   1 
ATOM   959  C CA  . LEU A 1 121 ? 23.288 30.783 25.957 1.00 35.88  ? 118 LEU A CA  1 
ATOM   960  C C   . LEU A 1 121 ? 24.223 30.402 27.100 1.00 34.95  ? 118 LEU A C   1 
ATOM   961  O O   . LEU A 1 121 ? 24.744 31.278 27.768 1.00 35.38  ? 118 LEU A O   1 
ATOM   962  C CB  . LEU A 1 121 ? 24.018 31.526 24.832 1.00 44.26  ? 118 LEU A CB  1 
ATOM   963  C CG  . LEU A 1 121 ? 23.208 31.841 23.574 1.00 47.63  ? 118 LEU A CG  1 
ATOM   964  C CD1 . LEU A 1 121 ? 24.100 32.441 22.495 1.00 49.78  ? 118 LEU A CD1 1 
ATOM   965  C CD2 . LEU A 1 121 ? 22.543 30.588 23.028 1.00 52.34  ? 118 LEU A CD2 1 
ATOM   966  N N   . GLU A 1 122 ? 24.364 29.101 27.372 1.00 34.54  ? 119 GLU A N   1 
ATOM   967  C CA  . GLU A 1 122 ? 25.164 28.637 28.493 1.00 39.63  ? 119 GLU A CA  1 
ATOM   968  C C   . GLU A 1 122 ? 26.138 27.543 28.076 1.00 36.92  ? 119 GLU A C   1 
ATOM   969  O O   . GLU A 1 122 ? 25.776 26.700 27.268 1.00 39.32  ? 119 GLU A O   1 
ATOM   970  C CB  . GLU A 1 122 ? 24.231 27.981 29.514 1.00 48.16  ? 119 GLU A CB  1 
ATOM   971  C CG  . GLU A 1 122 ? 23.113 28.884 29.995 1.00 63.94  ? 119 GLU A CG  1 
ATOM   972  C CD  . GLU A 1 122 ? 22.133 28.218 30.946 1.00 70.05  ? 119 GLU A CD  1 
ATOM   973  O OE1 . GLU A 1 122 ? 21.186 28.895 31.389 1.00 73.78  ? 119 GLU A OE1 1 
ATOM   974  O OE2 . GLU A 1 122 ? 22.308 27.017 31.222 1.00 75.23  ? 119 GLU A OE2 1 
ATOM   975  N N   . ASP A 1 123 ? 27.407 27.598 28.490 1.00 35.12  ? 120 ASP A N   1 
ATOM   976  C CA  . ASP A 1 123 ? 28.037 28.673 29.217 1.00 37.44  ? 120 ASP A CA  1 
ATOM   977  C C   . ASP A 1 123 ? 28.758 29.465 28.124 1.00 34.76  ? 120 ASP A C   1 
ATOM   978  O O   . ASP A 1 123 ? 29.594 28.906 27.408 1.00 37.91  ? 120 ASP A O   1 
ATOM   979  C CB  . ASP A 1 123 ? 29.000 28.137 30.283 1.00 42.11  ? 120 ASP A CB  1 
ATOM   980  C CG  . ASP A 1 123 ? 29.603 29.227 31.152 1.00 44.81  ? 120 ASP A CG  1 
ATOM   981  O OD1 . ASP A 1 123 ? 30.203 30.137 30.586 1.00 35.93  ? 120 ASP A OD1 1 
ATOM   982  O OD2 . ASP A 1 123 ? 29.462 29.150 32.389 1.00 52.09  ? 120 ASP A OD2 1 
ATOM   983  N N   . ALA A 1 124 ? 28.416 30.748 27.988 1.00 34.83  ? 121 ALA A N   1 
ATOM   984  C CA  . ALA A 1 124 ? 28.968 31.601 26.941 1.00 35.81  ? 121 ALA A CA  1 
ATOM   985  C C   . ALA A 1 124 ? 30.493 31.711 27.037 1.00 33.78  ? 121 ALA A C   1 
ATOM   986  O O   . ALA A 1 124 ? 31.163 32.101 26.074 1.00 34.40  ? 121 ALA A O   1 
ATOM   987  C CB  . ALA A 1 124 ? 28.299 32.945 27.011 1.00 38.13  ? 121 ALA A CB  1 
ATOM   988  N N   . GLY A 1 125 ? 31.052 31.356 28.195 1.00 34.96  ? 122 GLY A N   1 
ATOM   989  C CA  . GLY A 1 125 ? 32.496 31.418 28.332 1.00 34.14  ? 122 GLY A CA  1 
ATOM   990  C C   . GLY A 1 125 ? 33.185 30.480 27.340 1.00 35.41  ? 122 GLY A C   1 
ATOM   991  O O   . GLY A 1 125 ? 34.352 30.673 27.009 1.00 38.01  ? 122 GLY A O   1 
ATOM   992  N N   A SER A 1 126 ? 32.432 29.477 26.878 0.50 37.22  ? 123 SER A N   1 
ATOM   993  N N   B SER A 1 126 ? 32.446 29.462 26.873 0.50 36.10  ? 123 SER A N   1 
ATOM   994  C CA  A SER A 1 126 ? 32.918 28.500 25.920 0.50 41.07  ? 123 SER A CA  1 
ATOM   995  C CA  B SER A 1 126 ? 32.979 28.513 25.906 0.50 39.23  ? 123 SER A CA  1 
ATOM   996  C C   A SER A 1 126 ? 33.151 29.154 24.558 0.50 40.86  ? 123 SER A C   1 
ATOM   997  C C   B SER A 1 126 ? 33.210 29.212 24.570 0.50 40.73  ? 123 SER A C   1 
ATOM   998  O O   A SER A 1 126 ? 34.049 28.751 23.832 0.50 38.90  ? 123 SER A O   1 
ATOM   999  O O   B SER A 1 126 ? 34.166 28.898 23.871 0.50 42.93  ? 123 SER A O   1 
ATOM   1000 C CB  A SER A 1 126 ? 31.952 27.357 25.822 0.50 42.99  ? 123 SER A CB  1 
ATOM   1001 C CB  B SER A 1 126 ? 32.072 27.327 25.710 0.50 38.30  ? 123 SER A CB  1 
ATOM   1002 O OG  A SER A 1 126 ? 31.755 26.770 27.101 0.50 49.87  ? 123 SER A OG  1 
ATOM   1003 O OG  B SER A 1 126 ? 30.839 27.718 25.124 0.50 40.49  ? 123 SER A OG  1 
ATOM   1004 N N   . LEU A 1 127 ? 32.307 30.138 24.212 1.00 44.70  ? 124 LEU A N   1 
ATOM   1005 C CA  . LEU A 1 127 ? 32.436 30.869 22.955 1.00 44.30  ? 124 LEU A CA  1 
ATOM   1006 C C   . LEU A 1 127 ? 33.611 31.821 23.036 1.00 44.99  ? 124 LEU A C   1 
ATOM   1007 O O   . LEU A 1 127 ? 34.388 31.958 22.102 1.00 44.36  ? 124 LEU A O   1 
ATOM   1008 C CB  . LEU A 1 127 ? 31.177 31.688 22.654 1.00 45.97  ? 124 LEU A CB  1 
ATOM   1009 C CG  . LEU A 1 127 ? 29.944 30.930 22.194 1.00 43.89  ? 124 LEU A CG  1 
ATOM   1010 C CD1 . LEU A 1 127 ? 28.871 31.907 21.725 1.00 43.28  ? 124 LEU A CD1 1 
ATOM   1011 C CD2 . LEU A 1 127 ? 30.298 29.965 21.068 1.00 47.21  ? 124 LEU A CD2 1 
ATOM   1012 N N   . LEU A 1 128 ? 33.703 32.501 24.169 1.00 52.48  ? 125 LEU A N   1 
ATOM   1013 C CA  . LEU A 1 128 ? 34.753 33.474 24.367 1.00 55.46  ? 125 LEU A CA  1 
ATOM   1014 C C   . LEU A 1 128 ? 36.122 32.876 24.072 1.00 57.77  ? 125 LEU A C   1 
ATOM   1015 O O   . LEU A 1 128 ? 37.028 33.603 23.670 1.00 72.59  ? 125 LEU A O   1 
ATOM   1016 C CB  . LEU A 1 128 ? 34.659 33.988 25.804 1.00 53.12  ? 125 LEU A CB  1 
ATOM   1017 C CG  . LEU A 1 128 ? 35.682 35.048 26.184 1.00 52.56  ? 125 LEU A CG  1 
ATOM   1018 C CD1 . LEU A 1 128 ? 35.399 36.342 25.441 1.00 47.70  ? 125 LEU A CD1 1 
ATOM   1019 C CD2 . LEU A 1 128 ? 35.655 35.284 27.685 1.00 59.36  ? 125 LEU A CD2 1 
ATOM   1020 N N   . GLN A 1 129 ? 36.281 31.558 24.228 1.00 58.93  ? 126 GLN A N   1 
ATOM   1021 C CA  . GLN A 1 129 ? 37.613 31.025 23.988 1.00 58.17  ? 126 GLN A CA  1 
ATOM   1022 C C   . GLN A 1 129 ? 37.778 30.527 22.552 1.00 55.11  ? 126 GLN A C   1 
ATOM   1023 O O   . GLN A 1 129 ? 38.902 30.476 22.074 1.00 52.71  ? 126 GLN A O   1 
ATOM   1024 C CB  . GLN A 1 129 ? 37.981 29.940 25.000 1.00 74.25  ? 126 GLN A CB  1 
ATOM   1025 C CG  . GLN A 1 129 ? 37.112 28.697 24.951 1.00 82.18  ? 126 GLN A CG  1 
ATOM   1026 C CD  . GLN A 1 129 ? 37.590 27.695 25.971 1.00 98.89  ? 126 GLN A CD  1 
ATOM   1027 O OE1 . GLN A 1 129 ? 38.099 26.631 25.628 1.00 117.15 ? 126 GLN A OE1 1 
ATOM   1028 N NE2 . GLN A 1 129 ? 37.498 28.062 27.240 1.00 101.99 ? 126 GLN A NE2 1 
ATOM   1029 N N   . VAL A 1 130 ? 36.685 30.161 21.864 1.00 42.78  ? 127 VAL A N   1 
ATOM   1030 C CA  . VAL A 1 130 ? 36.825 29.688 20.493 1.00 39.90  ? 127 VAL A CA  1 
ATOM   1031 C C   . VAL A 1 130 ? 36.779 30.875 19.524 1.00 34.62  ? 127 VAL A C   1 
ATOM   1032 O O   . VAL A 1 130 ? 37.310 30.777 18.425 1.00 36.62  ? 127 VAL A O   1 
ATOM   1033 C CB  . VAL A 1 130 ? 35.788 28.608 20.118 1.00 42.07  ? 127 VAL A CB  1 
ATOM   1034 C CG1 . VAL A 1 130 ? 35.937 27.383 21.002 1.00 47.16  ? 127 VAL A CG1 1 
ATOM   1035 C CG2 . VAL A 1 130 ? 34.357 29.114 20.150 1.00 45.47  ? 127 VAL A CG2 1 
ATOM   1036 N N   . PHE A 1 131 ? 36.107 31.975 19.901 1.00 35.33  ? 128 PHE A N   1 
ATOM   1037 C CA  . PHE A 1 131 ? 36.080 33.132 19.015 1.00 36.43  ? 128 PHE A CA  1 
ATOM   1038 C C   . PHE A 1 131 ? 37.468 33.759 18.887 1.00 38.97  ? 128 PHE A C   1 
ATOM   1039 O O   . PHE A 1 131 ? 38.091 34.062 19.891 1.00 41.83  ? 128 PHE A O   1 
ATOM   1040 C CB  . PHE A 1 131 ? 35.151 34.251 19.499 1.00 34.32  ? 128 PHE A CB  1 
ATOM   1041 C CG  . PHE A 1 131 ? 33.663 34.008 19.419 1.00 31.57  ? 128 PHE A CG  1 
ATOM   1042 C CD1 . PHE A 1 131 ? 33.099 33.468 18.278 1.00 34.73  ? 128 PHE A CD1 1 
ATOM   1043 C CD2 . PHE A 1 131 ? 32.810 34.581 20.347 1.00 33.93  ? 128 PHE A CD2 1 
ATOM   1044 C CE1 . PHE A 1 131 ? 31.723 33.344 18.149 1.00 34.52  ? 128 PHE A CE1 1 
ATOM   1045 C CE2 . PHE A 1 131 ? 31.434 34.467 20.217 1.00 32.85  ? 128 PHE A CE2 1 
ATOM   1046 C CZ  . PHE A 1 131 ? 30.890 33.847 19.118 1.00 32.51  ? 128 PHE A CZ  1 
ATOM   1047 N N   . ASP A 1 132 ? 37.888 34.020 17.646 1.00 40.18  ? 129 ASP A N   1 
ATOM   1048 C CA  . ASP A 1 132 ? 39.178 34.641 17.373 1.00 45.46  ? 129 ASP A CA  1 
ATOM   1049 C C   . ASP A 1 132 ? 39.067 36.156 17.582 1.00 43.03  ? 129 ASP A C   1 
ATOM   1050 O O   . ASP A 1 132 ? 40.059 36.814 17.851 1.00 45.34  ? 129 ASP A O   1 
ATOM   1051 C CB  . ASP A 1 132 ? 39.696 34.246 15.987 1.00 47.31  ? 129 ASP A CB  1 
ATOM   1052 C CG  . ASP A 1 132 ? 38.769 34.618 14.844 1.00 60.85  ? 129 ASP A CG  1 
ATOM   1053 O OD1 . ASP A 1 132 ? 37.611 34.158 14.865 1.00 77.98  ? 129 ASP A OD1 1 
ATOM   1054 O OD2 . ASP A 1 132 ? 39.218 35.342 13.934 1.00 73.01  ? 129 ASP A OD2 1 
ATOM   1055 N N   . ALA A 1 133 ? 37.851 36.704 17.469 1.00 36.36  ? 130 ALA A N   1 
ATOM   1056 C CA  . ALA A 1 133 ? 37.598 38.127 17.672 1.00 33.93  ? 130 ALA A CA  1 
ATOM   1057 C C   . ALA A 1 133 ? 36.289 38.228 18.448 1.00 35.22  ? 130 ALA A C   1 
ATOM   1058 O O   . ALA A 1 133 ? 35.264 38.649 17.910 1.00 35.34  ? 130 ALA A O   1 
ATOM   1059 C CB  . ALA A 1 133 ? 37.534 38.842 16.341 1.00 37.40  ? 130 ALA A CB  1 
ATOM   1060 N N   . PRO A 1 134 ? 36.306 37.847 19.744 1.00 37.68  ? 131 PRO A N   1 
ATOM   1061 C CA  . PRO A 1 134 ? 35.085 37.763 20.554 1.00 34.99  ? 131 PRO A CA  1 
ATOM   1062 C C   . PRO A 1 134 ? 34.224 39.005 20.780 1.00 32.02  ? 131 PRO A C   1 
ATOM   1063 O O   . PRO A 1 134 ? 33.009 38.882 20.807 1.00 33.68  ? 131 PRO A O   1 
ATOM   1064 C CB  . PRO A 1 134 ? 35.581 37.219 21.904 1.00 38.01  ? 131 PRO A CB  1 
ATOM   1065 C CG  . PRO A 1 134 ? 37.060 37.521 21.935 1.00 42.78  ? 131 PRO A CG  1 
ATOM   1066 C CD  . PRO A 1 134 ? 37.520 37.490 20.498 1.00 38.80  ? 131 PRO A CD  1 
ATOM   1067 N N   . ALA A 1 135 ? 34.814 40.197 20.921 1.00 32.67  ? 132 ALA A N   1 
ATOM   1068 C CA  . ALA A 1 135 ? 33.975 41.366 21.165 1.00 33.77  ? 132 ALA A CA  1 
ATOM   1069 C C   . ALA A 1 135 ? 32.954 41.557 20.038 1.00 33.28  ? 132 ALA A C   1 
ATOM   1070 O O   . ALA A 1 135 ? 31.748 41.657 20.273 1.00 31.48  ? 132 ALA A O   1 
ATOM   1071 C CB  . ALA A 1 135 ? 34.828 42.591 21.335 1.00 35.83  ? 132 ALA A CB  1 
ATOM   1072 N N   . SER A 1 136 ? 33.444 41.611 18.800 1.00 30.85  ? 133 SER A N   1 
ATOM   1073 C CA  . SER A 1 136 ? 32.571 41.798 17.651 1.00 30.00  ? 133 SER A CA  1 
ATOM   1074 C C   . SER A 1 136 ? 31.614 40.620 17.461 1.00 29.61  ? 133 SER A C   1 
ATOM   1075 O O   . SER A 1 136 ? 30.465 40.836 17.105 1.00 31.05  ? 133 SER A O   1 
ATOM   1076 C CB  . SER A 1 136 ? 33.378 42.042 16.400 1.00 32.14  ? 133 SER A CB  1 
ATOM   1077 O OG  . SER A 1 136 ? 34.259 40.950 16.135 1.00 32.54  ? 133 SER A OG  1 
ATOM   1078 N N   . SER A 1 137 ? 32.083 39.383 17.679 1.00 30.31  ? 134 SER A N   1 
ATOM   1079 C CA  . SER A 1 137 ? 31.226 38.217 17.484 1.00 29.21  ? 134 SER A CA  1 
ATOM   1080 C C   . SER A 1 137 ? 30.073 38.233 18.488 1.00 32.31  ? 134 SER A C   1 
ATOM   1081 O O   . SER A 1 137 ? 28.929 37.923 18.132 1.00 29.62  ? 134 SER A O   1 
ATOM   1082 C CB  . SER A 1 137 ? 32.035 36.940 17.535 1.00 31.47  ? 134 SER A CB  1 
ATOM   1083 O OG  . SER A 1 137 ? 33.012 36.919 16.492 1.00 31.86  ? 134 SER A OG  1 
ATOM   1084 N N   . PHE A 1 138 ? 30.371 38.576 19.746 1.00 29.70  ? 135 PHE A N   1 
ATOM   1085 C CA  . PHE A 1 138 ? 29.302 38.669 20.743 1.00 30.76  ? 135 PHE A CA  1 
ATOM   1086 C C   . PHE A 1 138 ? 28.343 39.796 20.389 1.00 29.68  ? 135 PHE A C   1 
ATOM   1087 O O   . PHE A 1 138 ? 27.133 39.631 20.492 1.00 31.21  ? 135 PHE A O   1 
ATOM   1088 C CB  . PHE A 1 138 ? 29.820 38.805 22.180 1.00 29.91  ? 135 PHE A CB  1 
ATOM   1089 C CG  . PHE A 1 138 ? 30.191 37.507 22.850 1.00 30.78  ? 135 PHE A CG  1 
ATOM   1090 C CD1 . PHE A 1 138 ? 29.195 36.578 23.124 1.00 34.14  ? 135 PHE A CD1 1 
ATOM   1091 C CD2 . PHE A 1 138 ? 31.496 37.194 23.180 1.00 34.08  ? 135 PHE A CD2 1 
ATOM   1092 C CE1 . PHE A 1 138 ? 29.500 35.381 23.756 1.00 34.38  ? 135 PHE A CE1 1 
ATOM   1093 C CE2 . PHE A 1 138 ? 31.801 35.987 23.796 1.00 37.59  ? 135 PHE A CE2 1 
ATOM   1094 C CZ  . PHE A 1 138 ? 30.802 35.081 24.074 1.00 33.97  ? 135 PHE A CZ  1 
ATOM   1095 N N   . VAL A 1 139 ? 28.874 40.932 19.938 1.00 31.45  ? 136 VAL A N   1 
ATOM   1096 C CA  . VAL A 1 139 ? 27.994 42.008 19.522 1.00 28.91  ? 136 VAL A CA  1 
ATOM   1097 C C   . VAL A 1 139 ? 27.080 41.528 18.393 1.00 31.66  ? 136 VAL A C   1 
ATOM   1098 O O   . VAL A 1 139 ? 25.917 41.923 18.341 1.00 33.20  ? 136 VAL A O   1 
ATOM   1099 C CB  . VAL A 1 139 ? 28.779 43.272 19.117 1.00 32.98  ? 136 VAL A CB  1 
ATOM   1100 C CG1 . VAL A 1 139 ? 27.909 44.285 18.393 1.00 31.34  ? 136 VAL A CG1 1 
ATOM   1101 C CG2 . VAL A 1 139 ? 29.472 43.891 20.314 1.00 34.63  ? 136 VAL A CG2 1 
ATOM   1102 N N   . ALA A 1 140 ? 27.598 40.702 17.471 1.00 30.25  ? 137 ALA A N   1 
ATOM   1103 C CA  . ALA A 1 140 ? 26.785 40.204 16.373 1.00 31.61  ? 137 ALA A CA  1 
ATOM   1104 C C   . ALA A 1 140 ? 25.614 39.379 16.912 1.00 30.56  ? 137 ALA A C   1 
ATOM   1105 O O   . ALA A 1 140 ? 24.520 39.427 16.347 1.00 32.17  ? 137 ALA A O   1 
ATOM   1106 C CB  . ALA A 1 140 ? 27.625 39.407 15.402 1.00 31.04  ? 137 ALA A CB  1 
ATOM   1107 N N   . ILE A 1 141 ? 25.853 38.627 17.994 1.00 29.85  ? 138 ILE A N   1 
ATOM   1108 C CA  . ILE A 1 141 ? 24.794 37.822 18.603 1.00 30.93  ? 138 ILE A CA  1 
ATOM   1109 C C   . ILE A 1 141 ? 23.727 38.761 19.164 1.00 28.90  ? 138 ILE A C   1 
ATOM   1110 O O   . ILE A 1 141 ? 22.534 38.552 18.930 1.00 30.12  ? 138 ILE A O   1 
ATOM   1111 C CB  . ILE A 1 141 ? 25.343 36.825 19.642 1.00 30.26  ? 138 ILE A CB  1 
ATOM   1112 C CG1 . ILE A 1 141 ? 26.357 35.858 19.022 1.00 31.92  ? 138 ILE A CG1 1 
ATOM   1113 C CG2 . ILE A 1 141 ? 24.190 36.070 20.306 1.00 32.01  ? 138 ILE A CG2 1 
ATOM   1114 C CD1 . ILE A 1 141 ? 26.987 34.893 19.992 1.00 32.71  ? 138 ILE A CD1 1 
ATOM   1115 N N   . PHE A 1 142 ? 24.142 39.820 19.868 1.00 28.87  ? 139 PHE A N   1 
ATOM   1116 C CA  . PHE A 1 142 ? 23.180 40.799 20.373 1.00 30.78  ? 139 PHE A CA  1 
ATOM   1117 C C   . PHE A 1 142 ? 22.375 41.411 19.226 1.00 34.52  ? 139 PHE A C   1 
ATOM   1118 O O   . PHE A 1 142 ? 21.160 41.574 19.331 1.00 34.20  ? 139 PHE A O   1 
ATOM   1119 C CB  . PHE A 1 142 ? 23.880 41.901 21.170 1.00 30.89  ? 139 PHE A CB  1 
ATOM   1120 C CG  . PHE A 1 142 ? 24.263 41.582 22.594 1.00 27.82  ? 139 PHE A CG  1 
ATOM   1121 C CD1 . PHE A 1 142 ? 23.310 41.611 23.598 1.00 33.10  ? 139 PHE A CD1 1 
ATOM   1122 C CD2 . PHE A 1 142 ? 25.553 41.221 22.933 1.00 30.15  ? 139 PHE A CD2 1 
ATOM   1123 C CE1 . PHE A 1 142 ? 23.658 41.357 24.917 1.00 33.68  ? 139 PHE A CE1 1 
ATOM   1124 C CE2 . PHE A 1 142 ? 25.893 40.943 24.249 1.00 32.02  ? 139 PHE A CE2 1 
ATOM   1125 C CZ  . PHE A 1 142 ? 24.944 41.015 25.238 1.00 31.74  ? 139 PHE A CZ  1 
ATOM   1126 N N   . LEU A 1 143 ? 23.058 41.781 18.133 1.00 31.85  ? 140 LEU A N   1 
ATOM   1127 C CA  . LEU A 1 143 ? 22.393 42.364 16.974 1.00 33.81  ? 140 LEU A CA  1 
ATOM   1128 C C   . LEU A 1 143 ? 21.307 41.434 16.435 1.00 34.01  ? 140 LEU A C   1 
ATOM   1129 O O   . LEU A 1 143 ? 20.220 41.903 16.089 1.00 35.59  ? 140 LEU A O   1 
ATOM   1130 C CB  . LEU A 1 143 ? 23.452 42.660 15.913 1.00 33.13  ? 140 LEU A CB  1 
ATOM   1131 C CG  . LEU A 1 143 ? 24.365 43.847 16.215 1.00 34.22  ? 140 LEU A CG  1 
ATOM   1132 C CD1 . LEU A 1 143 ? 25.418 44.007 15.145 1.00 39.21  ? 140 LEU A CD1 1 
ATOM   1133 C CD2 . LEU A 1 143 ? 23.557 45.132 16.307 1.00 35.94  ? 140 LEU A CD2 1 
ATOM   1134 N N   . ALA A 1 144 ? 21.610 40.134 16.349 1.00 32.10  ? 141 ALA A N   1 
ATOM   1135 C CA  . ALA A 1 144 ? 20.649 39.153 15.861 1.00 34.95  ? 141 ALA A CA  1 
ATOM   1136 C C   . ALA A 1 144 ? 19.421 39.104 16.771 1.00 34.75  ? 141 ALA A C   1 
ATOM   1137 O O   . ALA A 1 144 ? 18.280 39.054 16.297 1.00 38.23  ? 141 ALA A O   1 
ATOM   1138 C CB  . ALA A 1 144 ? 21.298 37.801 15.784 1.00 35.99  ? 141 ALA A CB  1 
ATOM   1139 N N   . VAL A 1 145 ? 19.646 39.123 18.091 1.00 31.53  ? 142 VAL A N   1 
ATOM   1140 C CA  . VAL A 1 145 ? 18.513 39.036 19.001 1.00 33.29  ? 142 VAL A CA  1 
ATOM   1141 C C   . VAL A 1 145 ? 17.630 40.269 18.852 1.00 34.82  ? 142 VAL A C   1 
ATOM   1142 O O   . VAL A 1 145 ? 16.404 40.162 18.822 1.00 37.07  ? 142 VAL A O   1 
ATOM   1143 C CB  . VAL A 1 145 ? 18.961 38.853 20.461 1.00 31.69  ? 142 VAL A CB  1 
ATOM   1144 C CG1 . VAL A 1 145 ? 17.765 38.870 21.401 1.00 33.69  ? 142 VAL A CG1 1 
ATOM   1145 C CG2 . VAL A 1 145 ? 19.780 37.584 20.658 1.00 31.62  ? 142 VAL A CG2 1 
ATOM   1146 N N   . LEU A 1 146 ? 18.259 41.442 18.770 1.00 34.62  ? 143 LEU A N   1 
ATOM   1147 C CA  . LEU A 1 146 ? 17.522 42.694 18.660 1.00 37.89  ? 143 LEU A CA  1 
ATOM   1148 C C   . LEU A 1 146 ? 16.680 42.748 17.386 1.00 44.14  ? 143 LEU A C   1 
ATOM   1149 O O   . LEU A 1 146 ? 15.568 43.273 17.405 1.00 41.95  ? 143 LEU A O   1 
ATOM   1150 C CB  . LEU A 1 146 ? 18.515 43.855 18.703 1.00 40.41  ? 143 LEU A CB  1 
ATOM   1151 C CG  . LEU A 1 146 ? 19.224 44.066 20.038 1.00 40.11  ? 143 LEU A CG  1 
ATOM   1152 C CD1 . LEU A 1 146 ? 20.053 45.346 20.001 1.00 45.03  ? 143 LEU A CD1 1 
ATOM   1153 C CD2 . LEU A 1 146 ? 18.214 44.127 21.181 1.00 37.56  ? 143 LEU A CD2 1 
ATOM   1154 N N   . GLU A 1 147 ? 17.218 42.228 16.283 1.00 41.05  ? 144 GLU A N   1 
ATOM   1155 C CA  . GLU A 1 147 ? 16.466 42.279 15.037 1.00 46.44  ? 144 GLU A CA  1 
ATOM   1156 C C   . GLU A 1 147 ? 15.311 41.274 15.052 1.00 44.06  ? 144 GLU A C   1 
ATOM   1157 O O   . GLU A 1 147 ? 14.235 41.565 14.532 1.00 47.44  ? 144 GLU A O   1 
ATOM   1158 C CB  . GLU A 1 147 ? 17.391 42.054 13.839 1.00 52.57  ? 144 GLU A CB  1 
ATOM   1159 C CG  . GLU A 1 147 ? 18.094 40.712 13.830 1.00 66.97  ? 144 GLU A CG  1 
ATOM   1160 C CD  . GLU A 1 147 ? 19.011 40.482 12.639 1.00 85.81  ? 144 GLU A CD  1 
ATOM   1161 O OE1 . GLU A 1 147 ? 19.961 41.276 12.464 1.00 89.57  ? 144 GLU A OE1 1 
ATOM   1162 O OE2 . GLU A 1 147 ? 18.781 39.502 11.896 1.00 88.96  ? 144 GLU A OE2 1 
ATOM   1163 N N   . ILE A 1 148 ? 15.513 40.112 15.677 1.00 39.00  ? 145 ILE A N   1 
ATOM   1164 C CA  . ILE A 1 148 ? 14.502 39.061 15.688 1.00 41.70  ? 145 ILE A CA  1 
ATOM   1165 C C   . ILE A 1 148 ? 13.433 39.296 16.750 1.00 45.88  ? 145 ILE A C   1 
ATOM   1166 O O   . ILE A 1 148 ? 12.264 38.985 16.516 1.00 42.88  ? 145 ILE A O   1 
ATOM   1167 C CB  . ILE A 1 148 ? 15.174 37.684 15.840 1.00 40.68  ? 145 ILE A CB  1 
ATOM   1168 C CG1 . ILE A 1 148 ? 16.105 37.419 14.654 1.00 41.17  ? 145 ILE A CG1 1 
ATOM   1169 C CG2 . ILE A 1 148 ? 14.131 36.588 15.994 1.00 43.15  ? 145 ILE A CG2 1 
ATOM   1170 C CD1 . ILE A 1 148 ? 16.917 36.162 14.777 1.00 44.16  ? 145 ILE A CD1 1 
ATOM   1171 N N   . TRP A 1 149 ? 13.847 39.819 17.910 1.00 40.67  ? 146 TRP A N   1 
ATOM   1172 C CA  . TRP A 1 149 ? 12.946 40.090 19.015 1.00 41.23  ? 146 TRP A CA  1 
ATOM   1173 C C   . TRP A 1 149 ? 12.902 41.577 19.322 1.00 36.10  ? 146 TRP A C   1 
ATOM   1174 O O   . TRP A 1 149 ? 13.673 42.054 20.152 1.00 40.43  ? 146 TRP A O   1 
ATOM   1175 C CB  . TRP A 1 149 ? 13.392 39.325 20.256 1.00 38.98  ? 146 TRP A CB  1 
ATOM   1176 C CG  . TRP A 1 149 ? 13.108 37.860 20.274 1.00 39.11  ? 146 TRP A CG  1 
ATOM   1177 C CD1 . TRP A 1 149 ? 11.931 37.258 20.597 1.00 40.12  ? 146 TRP A CD1 1 
ATOM   1178 C CD2 . TRP A 1 149 ? 13.995 36.812 19.863 1.00 36.34  ? 146 TRP A CD2 1 
ATOM   1179 N NE1 . TRP A 1 149 ? 12.058 35.898 20.510 1.00 41.78  ? 146 TRP A NE1 1 
ATOM   1180 C CE2 . TRP A 1 149 ? 13.308 35.595 20.048 1.00 37.93  ? 146 TRP A CE2 1 
ATOM   1181 C CE3 . TRP A 1 149 ? 15.314 36.780 19.402 1.00 37.06  ? 146 TRP A CE3 1 
ATOM   1182 C CZ2 . TRP A 1 149 ? 13.890 34.363 19.754 1.00 36.61  ? 146 TRP A CZ2 1 
ATOM   1183 C CZ3 . TRP A 1 149 ? 15.889 35.562 19.123 1.00 37.19  ? 146 TRP A CZ3 1 
ATOM   1184 C CH2 . TRP A 1 149 ? 15.191 34.372 19.311 1.00 35.10  ? 146 TRP A CH2 1 
ATOM   1185 N N   . PRO A 1 150 ? 11.999 42.353 18.691 1.00 40.30  ? 147 PRO A N   1 
ATOM   1186 C CA  . PRO A 1 150 ? 11.872 43.771 19.022 1.00 42.72  ? 147 PRO A CA  1 
ATOM   1187 C C   . PRO A 1 150 ? 11.389 43.955 20.468 1.00 40.76  ? 147 PRO A C   1 
ATOM   1188 O O   . PRO A 1 150 ? 11.439 45.061 20.998 1.00 43.57  ? 147 PRO A O   1 
ATOM   1189 C CB  . PRO A 1 150 ? 10.867 44.303 17.988 1.00 46.26  ? 147 PRO A CB  1 
ATOM   1190 C CG  . PRO A 1 150 ? 10.101 43.074 17.534 1.00 48.84  ? 147 PRO A CG  1 
ATOM   1191 C CD  . PRO A 1 150 ? 11.093 41.935 17.611 1.00 44.53  ? 147 PRO A CD  1 
ATOM   1192 N N   . GLU A 1 151 ? 10.984 42.851 21.122 1.00 43.11  ? 148 GLU A N   1 
ATOM   1193 C CA  . GLU A 1 151 ? 10.488 42.897 22.487 1.00 41.69  ? 148 GLU A CA  1 
ATOM   1194 C C   . GLU A 1 151 ? 11.639 42.895 23.501 1.00 37.87  ? 148 GLU A C   1 
ATOM   1195 O O   . GLU A 1 151 ? 11.388 42.972 24.698 1.00 38.42  ? 148 GLU A O   1 
ATOM   1196 C CB  . GLU A 1 151 ? 9.593  41.697 22.840 1.00 44.20  ? 148 GLU A CB  1 
ATOM   1197 C CG  . GLU A 1 151 ? 8.418  41.438 21.911 1.00 51.94  ? 148 GLU A CG  1 
ATOM   1198 C CD  . GLU A 1 151 ? 8.733  40.784 20.577 1.00 51.90  ? 148 GLU A CD  1 
ATOM   1199 O OE1 . GLU A 1 151 ? 9.915  40.432 20.346 1.00 46.40  ? 148 GLU A OE1 1 
ATOM   1200 O OE2 . GLU A 1 151 ? 7.793  40.608 19.770 1.00 52.38  ? 148 GLU A OE2 1 
ATOM   1201 N N   . THR A 1 152 ? 12.892 42.827 23.032 1.00 37.29  ? 149 THR A N   1 
ATOM   1202 C CA  . THR A 1 152 ? 14.032 42.779 23.940 1.00 34.99  ? 149 THR A CA  1 
ATOM   1203 C C   . THR A 1 152 ? 14.084 44.024 24.827 1.00 38.82  ? 149 THR A C   1 
ATOM   1204 O O   . THR A 1 152 ? 14.059 45.147 24.319 1.00 38.64  ? 149 THR A O   1 
ATOM   1205 C CB  . THR A 1 152 ? 15.342 42.639 23.162 1.00 36.88  ? 149 THR A CB  1 
ATOM   1206 O OG1 . THR A 1 152 ? 15.271 41.481 22.327 1.00 37.42  ? 149 THR A OG1 1 
ATOM   1207 C CG2 . THR A 1 152 ? 16.532 42.542 24.085 1.00 37.01  ? 149 THR A CG2 1 
ATOM   1208 N N   . THR A 1 153 ? 14.229 43.805 26.145 1.00 36.19  ? 150 THR A N   1 
ATOM   1209 C CA  . THR A 1 153 ? 14.254 44.885 27.127 1.00 37.55  ? 150 THR A CA  1 
ATOM   1210 C C   . THR A 1 153 ? 15.608 44.995 27.839 1.00 36.56  ? 150 THR A C   1 
ATOM   1211 O O   . THR A 1 153 ? 15.909 46.021 28.449 1.00 35.47  ? 150 THR A O   1 
ATOM   1212 C CB  . THR A 1 153 ? 13.140 44.705 28.164 1.00 41.07  ? 150 THR A CB  1 
ATOM   1213 O OG1 . THR A 1 153 ? 13.311 43.440 28.803 1.00 39.43  ? 150 THR A OG1 1 
ATOM   1214 C CG2 . THR A 1 153 ? 11.754 44.774 27.562 1.00 47.47  ? 150 THR A CG2 1 
ATOM   1215 N N   . TRP A 1 154 ? 16.424 43.941 27.784 1.00 32.82  ? 151 TRP A N   1 
ATOM   1216 C CA  . TRP A 1 154 ? 17.721 44.018 28.439 1.00 30.27  ? 151 TRP A CA  1 
ATOM   1217 C C   . TRP A 1 154 ? 18.579 42.865 27.939 1.00 30.21  ? 151 TRP A C   1 
ATOM   1218 O O   . TRP A 1 154 ? 18.069 41.815 27.572 1.00 31.39  ? 151 TRP A O   1 
ATOM   1219 C CB  . TRP A 1 154 ? 17.594 43.919 29.975 1.00 31.62  ? 151 TRP A CB  1 
ATOM   1220 C CG  . TRP A 1 154 ? 18.858 44.279 30.697 1.00 30.71  ? 151 TRP A CG  1 
ATOM   1221 C CD1 . TRP A 1 154 ? 19.750 43.459 31.328 1.00 30.46  ? 151 TRP A CD1 1 
ATOM   1222 C CD2 . TRP A 1 154 ? 19.305 45.613 30.955 1.00 29.80  ? 151 TRP A CD2 1 
ATOM   1223 N NE1 . TRP A 1 154 ? 20.758 44.192 31.894 1.00 30.18  ? 151 TRP A NE1 1 
ATOM   1224 C CE2 . TRP A 1 154 ? 20.508 45.519 31.689 1.00 30.14  ? 151 TRP A CE2 1 
ATOM   1225 C CE3 . TRP A 1 154 ? 18.820 46.877 30.618 1.00 30.56  ? 151 TRP A CE3 1 
ATOM   1226 C CZ2 . TRP A 1 154 ? 21.224 46.648 32.073 1.00 31.52  ? 151 TRP A CZ2 1 
ATOM   1227 C CZ3 . TRP A 1 154 ? 19.529 47.987 31.007 1.00 32.14  ? 151 TRP A CZ3 1 
ATOM   1228 C CH2 . TRP A 1 154 ? 20.711 47.871 31.725 1.00 33.28  ? 151 TRP A CH2 1 
ATOM   1229 N N   . GLY A 1 155 ? 19.890 43.052 27.988 1.00 28.38  ? 152 GLY A N   1 
ATOM   1230 C CA  . GLY A 1 155 ? 20.802 41.988 27.630 1.00 28.24  ? 152 GLY A CA  1 
ATOM   1231 C C   . GLY A 1 155 ? 22.100 42.155 28.398 1.00 27.85  ? 152 GLY A C   1 
ATOM   1232 O O   . GLY A 1 155 ? 22.541 43.285 28.583 1.00 29.02  ? 152 GLY A O   1 
ATOM   1233 N N   . MET A 1 156 ? 22.702 41.036 28.811 1.00 27.78  ? 153 MET A N   1 
ATOM   1234 C CA  . MET A 1 156 ? 23.948 41.127 29.546 1.00 27.74  ? 153 MET A CA  1 
ATOM   1235 C C   . MET A 1 156 ? 24.827 39.914 29.243 1.00 27.84  ? 153 MET A C   1 
ATOM   1236 O O   . MET A 1 156 ? 24.362 38.780 29.251 1.00 28.12  ? 153 MET A O   1 
ATOM   1237 C CB  . MET A 1 156 ? 23.695 41.169 31.063 1.00 29.71  ? 153 MET A CB  1 
ATOM   1238 C CG  . MET A 1 156 ? 24.951 40.948 31.920 1.00 30.29  ? 153 MET A CG  1 
ATOM   1239 S SD  . MET A 1 156 ? 24.646 40.749 33.706 1.00 31.56  ? 153 MET A SD  1 
ATOM   1240 C CE  . MET A 1 156 ? 24.434 38.973 33.734 1.00 33.25  ? 153 MET A CE  1 
ATOM   1241 N N   . LEU A 1 157 ? 26.099 40.216 28.977 1.00 28.56  ? 154 LEU A N   1 
ATOM   1242 C CA  . LEU A 1 157 ? 27.177 39.252 28.862 1.00 30.57  ? 154 LEU A CA  1 
ATOM   1243 C C   . LEU A 1 157 ? 28.177 39.657 29.939 1.00 27.98  ? 154 LEU A C   1 
ATOM   1244 O O   . LEU A 1 157 ? 28.742 40.739 29.862 1.00 29.52  ? 154 LEU A O   1 
ATOM   1245 C CB  . LEU A 1 157 ? 27.835 39.263 27.479 1.00 31.11  ? 154 LEU A CB  1 
ATOM   1246 C CG  . LEU A 1 157 ? 29.085 38.389 27.375 1.00 30.76  ? 154 LEU A CG  1 
ATOM   1247 C CD1 . LEU A 1 157 ? 28.733 36.928 27.475 1.00 29.99  ? 154 LEU A CD1 1 
ATOM   1248 C CD2 . LEU A 1 157 ? 29.851 38.685 26.094 1.00 34.89  ? 154 LEU A CD2 1 
ATOM   1249 N N   . ALA A 1 158 ? 28.357 38.807 30.951 1.00 28.00  ? 155 ALA A N   1 
ATOM   1250 C CA  . ALA A 1 158 ? 29.260 39.148 32.038 1.00 30.73  ? 155 ALA A CA  1 
ATOM   1251 C C   . ALA A 1 158 ? 29.857 37.909 32.669 1.00 28.75  ? 155 ALA A C   1 
ATOM   1252 O O   . ALA A 1 158 ? 29.222 36.860 32.749 1.00 30.63  ? 155 ALA A O   1 
ATOM   1253 C CB  . ALA A 1 158 ? 28.512 39.905 33.110 1.00 32.72  ? 155 ALA A CB  1 
ATOM   1254 N N   . PRO A 1 159 ? 31.083 38.021 33.219 1.00 28.75  ? 156 PRO A N   1 
ATOM   1255 C CA  . PRO A 1 159 ? 31.659 36.902 33.944 1.00 29.56  ? 156 PRO A CA  1 
ATOM   1256 C C   . PRO A 1 159 ? 30.713 36.556 35.099 1.00 28.14  ? 156 PRO A C   1 
ATOM   1257 O O   . PRO A 1 159 ? 30.202 37.442 35.790 1.00 29.82  ? 156 PRO A O   1 
ATOM   1258 C CB  . PRO A 1 159 ? 33.009 37.439 34.447 1.00 32.05  ? 156 PRO A CB  1 
ATOM   1259 C CG  . PRO A 1 159 ? 33.300 38.639 33.554 1.00 33.22  ? 156 PRO A CG  1 
ATOM   1260 C CD  . PRO A 1 159 ? 31.944 39.222 33.218 1.00 31.46  ? 156 PRO A CD  1 
ATOM   1261 N N   . HIS A 1 160 ? 30.520 35.261 35.343 1.00 29.48  ? 157 HIS A N   1 
ATOM   1262 C CA  . HIS A 1 160 ? 29.647 34.792 36.396 1.00 32.46  ? 157 HIS A CA  1 
ATOM   1263 C C   . HIS A 1 160 ? 30.111 35.327 37.748 1.00 31.59  ? 157 HIS A C   1 
ATOM   1264 O O   . HIS A 1 160 ? 29.310 35.854 38.518 1.00 31.40  ? 157 HIS A O   1 
ATOM   1265 C CB  . HIS A 1 160 ? 29.647 33.263 36.418 1.00 36.56  ? 157 HIS A CB  1 
ATOM   1266 C CG  . HIS A 1 160 ? 28.636 32.679 37.340 1.00 38.24  ? 157 HIS A CG  1 
ATOM   1267 N ND1 . HIS A 1 160 ? 28.985 32.205 38.584 1.00 40.89  ? 157 HIS A ND1 1 
ATOM   1268 C CD2 . HIS A 1 160 ? 27.301 32.601 37.271 1.00 39.80  ? 157 HIS A CD2 1 
ATOM   1269 C CE1 . HIS A 1 160 ? 27.891 31.788 39.207 1.00 40.80  ? 157 HIS A CE1 1 
ATOM   1270 N NE2 . HIS A 1 160 ? 26.862 32.003 38.424 1.00 38.79  ? 157 HIS A NE2 1 
ATOM   1271 N N   . ALA A 1 161 ? 31.421 35.202 38.025 1.00 31.65  ? 158 ALA A N   1 
ATOM   1272 C CA  . ALA A 1 161 ? 31.984 35.639 39.296 1.00 35.79  ? 158 ALA A CA  1 
ATOM   1273 C C   . ALA A 1 161 ? 31.743 37.126 39.529 1.00 30.35  ? 158 ALA A C   1 
ATOM   1274 O O   . ALA A 1 161 ? 31.486 37.522 40.663 1.00 34.73  ? 158 ALA A O   1 
ATOM   1275 C CB  . ALA A 1 161 ? 33.456 35.332 39.348 1.00 37.05  ? 158 ALA A CB  1 
ATOM   1276 N N   . TYR A 1 162 ? 31.864 37.928 38.465 1.00 33.47  ? 159 TYR A N   1 
ATOM   1277 C CA  . TYR A 1 162 ? 31.634 39.360 38.555 1.00 33.70  ? 159 TYR A CA  1 
ATOM   1278 C C   . TYR A 1 162 ? 30.183 39.645 38.946 1.00 34.02  ? 159 TYR A C   1 
ATOM   1279 O O   . TYR A 1 162 ? 29.920 40.397 39.889 1.00 33.41  ? 159 TYR A O   1 
ATOM   1280 C CB  . TYR A 1 162 ? 31.875 40.090 37.232 1.00 36.40  ? 159 TYR A CB  1 
ATOM   1281 C CG  . TYR A 1 162 ? 31.655 41.577 37.360 1.00 35.60  ? 159 TYR A CG  1 
ATOM   1282 C CD1 . TYR A 1 162 ? 32.561 42.372 38.041 1.00 41.60  ? 159 TYR A CD1 1 
ATOM   1283 C CD2 . TYR A 1 162 ? 30.458 42.154 36.967 1.00 36.48  ? 159 TYR A CD2 1 
ATOM   1284 C CE1 . TYR A 1 162 ? 32.335 43.725 38.225 1.00 39.88  ? 159 TYR A CE1 1 
ATOM   1285 C CE2 . TYR A 1 162 ? 30.201 43.500 37.171 1.00 37.90  ? 159 TYR A CE2 1 
ATOM   1286 C CZ  . TYR A 1 162 ? 31.151 44.290 37.793 1.00 38.10  ? 159 TYR A CZ  1 
ATOM   1287 O OH  . TYR A 1 162 ? 30.902 45.623 37.987 1.00 37.47  ? 159 TYR A OH  1 
ATOM   1288 N N   . PHE A 1 163 ? 29.239 39.059 38.196 1.00 30.45  ? 160 PHE A N   1 
ATOM   1289 C CA  . PHE A 1 163 ? 27.828 39.310 38.454 1.00 30.70  ? 160 PHE A CA  1 
ATOM   1290 C C   . PHE A 1 163 ? 27.470 38.950 39.894 1.00 30.92  ? 160 PHE A C   1 
ATOM   1291 O O   . PHE A 1 163 ? 26.890 39.761 40.612 1.00 32.77  ? 160 PHE A O   1 
ATOM   1292 C CB  . PHE A 1 163 ? 26.921 38.513 37.517 1.00 30.20  ? 160 PHE A CB  1 
ATOM   1293 C CG  . PHE A 1 163 ? 25.459 38.790 37.756 1.00 31.60  ? 160 PHE A CG  1 
ATOM   1294 C CD1 . PHE A 1 163 ? 24.911 40.025 37.442 1.00 36.58  ? 160 PHE A CD1 1 
ATOM   1295 C CD2 . PHE A 1 163 ? 24.666 37.859 38.401 1.00 37.91  ? 160 PHE A CD2 1 
ATOM   1296 C CE1 . PHE A 1 163 ? 23.574 40.291 37.701 1.00 37.29  ? 160 PHE A CE1 1 
ATOM   1297 C CE2 . PHE A 1 163 ? 23.332 38.128 38.668 1.00 41.43  ? 160 PHE A CE2 1 
ATOM   1298 C CZ  . PHE A 1 163 ? 22.788 39.343 38.314 1.00 38.72  ? 160 PHE A CZ  1 
ATOM   1299 N N   . VAL A 1 164 ? 27.853 37.744 40.323 1.00 30.19  ? 161 VAL A N   1 
ATOM   1300 C CA  . VAL A 1 164 ? 27.492 37.263 41.648 1.00 32.49  ? 161 VAL A CA  1 
ATOM   1301 C C   . VAL A 1 164 ? 28.186 38.010 42.790 1.00 35.56  ? 161 VAL A C   1 
ATOM   1302 O O   . VAL A 1 164 ? 27.538 38.351 43.779 1.00 37.78  ? 161 VAL A O   1 
ATOM   1303 C CB  . VAL A 1 164 ? 27.734 35.744 41.770 1.00 35.17  ? 161 VAL A CB  1 
ATOM   1304 C CG1 . VAL A 1 164 ? 27.605 35.257 43.209 1.00 41.13  ? 161 VAL A CG1 1 
ATOM   1305 C CG2 . VAL A 1 164 ? 26.826 34.947 40.841 1.00 37.18  ? 161 VAL A CG2 1 
ATOM   1306 N N   . HIS A 1 165 ? 29.481 38.304 42.660 1.00 34.44  ? 162 HIS A N   1 
ATOM   1307 C CA  . HIS A 1 165 ? 30.191 38.851 43.803 1.00 35.88  ? 162 HIS A CA  1 
ATOM   1308 C C   . HIS A 1 165 ? 30.655 40.297 43.700 1.00 37.13  ? 162 HIS A C   1 
ATOM   1309 O O   . HIS A 1 165 ? 31.101 40.841 44.710 1.00 39.72  ? 162 HIS A O   1 
ATOM   1310 C CB  . HIS A 1 165 ? 31.478 38.042 44.012 1.00 39.65  ? 162 HIS A CB  1 
ATOM   1311 C CG  . HIS A 1 165 ? 31.239 36.594 44.274 1.00 42.24  ? 162 HIS A CG  1 
ATOM   1312 N ND1 . HIS A 1 165 ? 30.713 36.131 45.461 1.00 47.42  ? 162 HIS A ND1 1 
ATOM   1313 C CD2 . HIS A 1 165 ? 31.538 35.510 43.552 1.00 43.12  ? 162 HIS A CD2 1 
ATOM   1314 C CE1 . HIS A 1 165 ? 30.634 34.809 45.413 1.00 46.96  ? 162 HIS A CE1 1 
ATOM   1315 N NE2 . HIS A 1 165 ? 31.121 34.413 44.261 1.00 47.12  ? 162 HIS A NE2 1 
ATOM   1316 N N   A GLN A 1 166 ? 30.514 40.939 42.542 0.60 35.94  ? 163 GLN A N   1 
ATOM   1317 N N   B GLN A 1 166 ? 30.546 40.905 42.511 0.40 36.70  ? 163 GLN A N   1 
ATOM   1318 C CA  A GLN A 1 166 ? 31.023 42.300 42.459 0.60 38.41  ? 163 GLN A CA  1 
ATOM   1319 C CA  B GLN A 1 166 ? 31.079 42.248 42.328 0.40 38.92  ? 163 GLN A CA  1 
ATOM   1320 C C   A GLN A 1 166 ? 30.006 43.284 41.895 0.60 35.54  ? 163 GLN A C   1 
ATOM   1321 C C   B GLN A 1 166 ? 30.103 43.214 41.656 0.40 36.39  ? 163 GLN A C   1 
ATOM   1322 O O   A GLN A 1 166 ? 30.249 44.481 41.961 0.60 31.50  ? 163 GLN A O   1 
ATOM   1323 O O   B GLN A 1 166 ? 30.496 44.331 41.332 0.40 38.11  ? 163 GLN A O   1 
ATOM   1324 C CB  A GLN A 1 166 ? 32.276 42.341 41.584 0.60 40.12  ? 163 GLN A CB  1 
ATOM   1325 C CB  B GLN A 1 166 ? 32.351 42.153 41.484 0.40 39.90  ? 163 GLN A CB  1 
ATOM   1326 C CG  A GLN A 1 166 ? 33.419 41.471 42.086 0.60 45.51  ? 163 GLN A CG  1 
ATOM   1327 C CG  B GLN A 1 166 ? 33.416 41.241 42.081 0.40 44.03  ? 163 GLN A CG  1 
ATOM   1328 C CD  A GLN A 1 166 ? 34.615 41.571 41.168 0.60 49.76  ? 163 GLN A CD  1 
ATOM   1329 C CD  B GLN A 1 166 ? 33.943 41.714 43.412 0.40 47.05  ? 163 GLN A CD  1 
ATOM   1330 O OE1 A GLN A 1 166 ? 35.201 42.638 40.998 0.60 53.47  ? 163 GLN A OE1 1 
ATOM   1331 O OE1 B GLN A 1 166 ? 33.600 42.791 43.896 0.40 50.08  ? 163 GLN A OE1 1 
ATOM   1332 N NE2 A GLN A 1 166 ? 34.987 40.457 40.557 0.60 50.91  ? 163 GLN A NE2 1 
ATOM   1333 N NE2 B GLN A 1 166 ? 34.821 40.920 44.002 0.40 51.04  ? 163 GLN A NE2 1 
ATOM   1334 N N   . ARG A 1 167 ? 28.852 42.817 41.404 1.00 34.27  ? 164 ARG A N   1 
ATOM   1335 C CA  . ARG A 1 167 ? 27.911 43.769 40.816 1.00 34.08  ? 164 ARG A CA  1 
ATOM   1336 C C   . ARG A 1 167 ? 27.646 44.876 41.841 1.00 33.96  ? 164 ARG A C   1 
ATOM   1337 O O   . ARG A 1 167 ? 27.492 44.613 43.032 1.00 35.81  ? 164 ARG A O   1 
ATOM   1338 C CB  . ARG A 1 167 ? 26.614 43.130 40.309 1.00 31.74  ? 164 ARG A CB  1 
ATOM   1339 C CG  . ARG A 1 167 ? 25.706 42.536 41.371 1.00 32.38  ? 164 ARG A CG  1 
ATOM   1340 C CD  . ARG A 1 167 ? 24.428 42.017 40.728 1.00 32.15  ? 164 ARG A CD  1 
ATOM   1341 N NE  . ARG A 1 167 ? 23.459 41.575 41.728 1.00 34.85  ? 164 ARG A NE  1 
ATOM   1342 C CZ  . ARG A 1 167 ? 23.602 40.523 42.529 1.00 36.06  ? 164 ARG A CZ  1 
ATOM   1343 N NH1 . ARG A 1 167 ? 24.631 39.711 42.386 1.00 36.22  ? 164 ARG A NH1 1 
ATOM   1344 N NH2 . ARG A 1 167 ? 22.668 40.235 43.423 1.00 35.89  ? 164 ARG A NH2 1 
ATOM   1345 N N   . THR A 1 168 ? 27.603 46.123 41.363 1.00 33.85  ? 165 THR A N   1 
ATOM   1346 C CA  . THR A 1 168 ? 27.452 47.287 42.222 1.00 33.77  ? 165 THR A CA  1 
ATOM   1347 C C   . THR A 1 168 ? 26.125 47.285 42.975 1.00 35.56  ? 165 THR A C   1 
ATOM   1348 O O   . THR A 1 168 ? 26.088 47.512 44.182 1.00 35.27  ? 165 THR A O   1 
ATOM   1349 C CB  . THR A 1 168 ? 27.531 48.588 41.409 1.00 37.45  ? 165 THR A CB  1 
ATOM   1350 O OG1 . THR A 1 168 ? 28.747 48.603 40.662 1.00 37.29  ? 165 THR A OG1 1 
ATOM   1351 C CG2 . THR A 1 168 ? 27.447 49.828 42.271 1.00 40.93  ? 165 THR A CG2 1 
ATOM   1352 N N   . PHE A 1 169 ? 25.037 47.013 42.250 1.00 34.51  ? 166 PHE A N   1 
ATOM   1353 C CA  . PHE A 1 169 ? 23.706 47.081 42.831 1.00 34.41  ? 166 PHE A CA  1 
ATOM   1354 C C   . PHE A 1 169 ? 23.176 45.677 43.065 1.00 36.40  ? 166 PHE A C   1 
ATOM   1355 O O   . PHE A 1 169 ? 22.872 44.941 42.122 1.00 35.78  ? 166 PHE A O   1 
ATOM   1356 C CB  . PHE A 1 169 ? 22.797 47.897 41.918 1.00 35.68  ? 166 PHE A CB  1 
ATOM   1357 C CG  . PHE A 1 169 ? 23.269 49.309 41.723 1.00 33.40  ? 166 PHE A CG  1 
ATOM   1358 C CD1 . PHE A 1 169 ? 23.200 50.235 42.755 1.00 37.49  ? 166 PHE A CD1 1 
ATOM   1359 C CD2 . PHE A 1 169 ? 23.907 49.674 40.552 1.00 33.82  ? 166 PHE A CD2 1 
ATOM   1360 C CE1 . PHE A 1 169 ? 23.671 51.524 42.577 1.00 40.31  ? 166 PHE A CE1 1 
ATOM   1361 C CE2 . PHE A 1 169 ? 24.395 50.958 40.384 1.00 36.25  ? 166 PHE A CE2 1 
ATOM   1362 C CZ  . PHE A 1 169 ? 24.268 51.882 41.392 1.00 38.06  ? 166 PHE A CZ  1 
ATOM   1363 N N   . PRO A 1 170 ? 22.957 45.305 44.339 1.00 40.55  ? 167 PRO A N   1 
ATOM   1364 C CA  . PRO A 1 170 ? 22.528 43.948 44.661 1.00 41.41  ? 167 PRO A CA  1 
ATOM   1365 C C   . PRO A 1 170 ? 21.153 43.578 44.117 1.00 35.09  ? 167 PRO A C   1 
ATOM   1366 O O   . PRO A 1 170 ? 20.929 42.441 43.707 1.00 37.70  ? 167 PRO A O   1 
ATOM   1367 C CB  . PRO A 1 170 ? 22.511 43.955 46.204 1.00 43.36  ? 167 PRO A CB  1 
ATOM   1368 C CG  . PRO A 1 170 ? 22.287 45.416 46.582 1.00 44.13  ? 167 PRO A CG  1 
ATOM   1369 C CD  . PRO A 1 170 ? 23.025 46.195 45.515 1.00 45.65  ? 167 PRO A CD  1 
ATOM   1370 N N   . ASP A 1 171 ? 20.275 44.576 44.050 1.00 35.91  ? 168 ASP A N   1 
ATOM   1371 C CA  . ASP A 1 171 ? 18.886 44.380 43.674 1.00 36.25  ? 168 ASP A CA  1 
ATOM   1372 C C   . ASP A 1 171 ? 18.574 44.800 42.242 1.00 33.73  ? 168 ASP A C   1 
ATOM   1373 O O   . ASP A 1 171 ? 17.402 44.980 41.909 1.00 34.31  ? 168 ASP A O   1 
ATOM   1374 C CB  . ASP A 1 171 ? 17.995 45.128 44.674 1.00 36.18  ? 168 ASP A CB  1 
ATOM   1375 C CG  . ASP A 1 171 ? 18.390 46.585 44.891 1.00 43.36  ? 168 ASP A CG  1 
ATOM   1376 O OD1 . ASP A 1 171 ? 19.407 46.999 44.334 1.00 47.62  ? 168 ASP A OD1 1 
ATOM   1377 O OD2 . ASP A 1 171 ? 17.688 47.273 45.643 1.00 48.73  ? 168 ASP A OD2 1 
ATOM   1378 N N   . ARG A 1 172 ? 19.611 44.962 41.412 1.00 32.49  ? 169 ARG A N   1 
ATOM   1379 C CA  . ARG A 1 172 ? 19.438 45.369 40.033 1.00 30.36  ? 169 ARG A CA  1 
ATOM   1380 C C   . ARG A 1 172 ? 20.181 44.433 39.087 1.00 30.02  ? 169 ARG A C   1 
ATOM   1381 O O   . ARG A 1 172 ? 21.072 43.692 39.490 1.00 32.41  ? 169 ARG A O   1 
ATOM   1382 C CB  . ARG A 1 172 ? 20.081 46.741 39.793 1.00 32.00  ? 169 ARG A CB  1 
ATOM   1383 C CG  . ARG A 1 172 ? 19.442 47.883 40.569 1.00 32.06  ? 169 ARG A CG  1 
ATOM   1384 C CD  . ARG A 1 172 ? 18.129 48.338 39.985 1.00 35.09  ? 169 ARG A CD  1 
ATOM   1385 N NE  . ARG A 1 172 ? 17.440 49.267 40.868 1.00 33.70  ? 169 ARG A NE  1 
ATOM   1386 C CZ  . ARG A 1 172 ? 16.326 49.908 40.561 1.00 34.00  ? 169 ARG A CZ  1 
ATOM   1387 N NH1 . ARG A 1 172 ? 15.843 49.834 39.338 1.00 34.82  ? 169 ARG A NH1 1 
ATOM   1388 N NH2 . ARG A 1 172 ? 15.741 50.694 41.448 1.00 37.45  ? 169 ARG A NH2 1 
ATOM   1389 N N   . ARG A 1 173 ? 19.756 44.473 37.836 1.00 31.97  ? 170 ARG A N   1 
ATOM   1390 C CA  . ARG A 1 173 ? 20.483 43.781 36.790 1.00 33.19  ? 170 ARG A CA  1 
ATOM   1391 C C   . ARG A 1 173 ? 21.800 44.534 36.590 1.00 34.86  ? 170 ARG A C   1 
ATOM   1392 O O   . ARG A 1 173 ? 22.059 45.544 37.255 1.00 36.56  ? 170 ARG A O   1 
ATOM   1393 C CB  . ARG A 1 173 ? 19.679 43.766 35.491 1.00 34.68  ? 170 ARG A CB  1 
ATOM   1394 C CG  . ARG A 1 173 ? 18.300 43.130 35.602 1.00 36.71  ? 170 ARG A CG  1 
ATOM   1395 C CD  . ARG A 1 173 ? 17.727 42.851 34.221 1.00 41.94  ? 170 ARG A CD  1 
ATOM   1396 N NE  . ARG A 1 173 ? 16.371 42.306 34.192 1.00 37.28  ? 170 ARG A NE  1 
ATOM   1397 C CZ  . ARG A 1 173 ? 15.976 41.191 34.785 1.00 51.85  ? 170 ARG A CZ  1 
ATOM   1398 N NH1 . ARG A 1 173 ? 16.819 40.487 35.520 1.00 52.48  ? 170 ARG A NH1 1 
ATOM   1399 N NH2 . ARG A 1 173 ? 14.718 40.800 34.670 1.00 51.11  ? 170 ARG A NH2 1 
ATOM   1400 N N   . SER A 1 174 ? 22.642 44.010 35.695 1.00 29.62  ? 171 SER A N   1 
ATOM   1401 C CA  . SER A 1 174 ? 23.911 44.616 35.329 1.00 28.56  ? 171 SER A CA  1 
ATOM   1402 C C   . SER A 1 174 ? 24.031 44.639 33.806 1.00 29.41  ? 171 SER A C   1 
ATOM   1403 O O   . SER A 1 174 ? 23.468 43.786 33.116 1.00 29.61  ? 171 SER A O   1 
ATOM   1404 C CB  . SER A 1 174 ? 25.074 43.886 35.961 1.00 31.48  ? 171 SER A CB  1 
ATOM   1405 O OG  . SER A 1 174 ? 26.317 44.415 35.509 1.00 32.09  ? 171 SER A OG  1 
ATOM   1406 N N   . ILE A 1 175 ? 24.779 45.609 33.282 1.00 28.75  ? 172 ILE A N   1 
ATOM   1407 C CA  . ILE A 1 175 ? 24.982 45.693 31.844 1.00 29.95  ? 172 ILE A CA  1 
ATOM   1408 C C   . ILE A 1 175 ? 26.097 44.723 31.450 1.00 31.29  ? 172 ILE A C   1 
ATOM   1409 O O   . ILE A 1 175 ? 26.227 44.360 30.283 1.00 30.35  ? 172 ILE A O   1 
ATOM   1410 C CB  . ILE A 1 175 ? 25.295 47.143 31.411 1.00 30.80  ? 172 ILE A CB  1 
ATOM   1411 C CG1 . ILE A 1 175 ? 25.161 47.338 29.897 1.00 32.15  ? 172 ILE A CG1 1 
ATOM   1412 C CG2 . ILE A 1 175 ? 26.654 47.586 31.927 1.00 31.26  ? 172 ILE A CG2 1 
ATOM   1413 C CD1 . ILE A 1 175 ? 23.771 47.088 29.362 1.00 31.69  ? 172 ILE A CD1 1 
ATOM   1414 N N   . GLY A 1 176 ? 26.933 44.336 32.423 1.00 29.48  ? 173 GLY A N   1 
ATOM   1415 C CA  . GLY A 1 176 ? 28.033 43.415 32.159 1.00 33.53  ? 173 GLY A CA  1 
ATOM   1416 C C   . GLY A 1 176 ? 29.125 43.993 31.257 1.00 33.02  ? 173 GLY A C   1 
ATOM   1417 O O   . GLY A 1 176 ? 29.212 45.201 31.046 1.00 32.82  ? 173 GLY A O   1 
ATOM   1418 N N   . TRP A 1 177 ? 29.959 43.104 30.701 1.00 32.42  ? 174 TRP A N   1 
ATOM   1419 C CA  . TRP A 1 177 ? 31.020 43.500 29.785 1.00 31.02  ? 174 TRP A CA  1 
ATOM   1420 C C   . TRP A 1 177 ? 30.421 44.075 28.505 1.00 32.26  ? 174 TRP A C   1 
ATOM   1421 O O   . TRP A 1 177 ? 30.812 45.144 28.029 1.00 32.95  ? 174 TRP A O   1 
ATOM   1422 C CB  . TRP A 1 177 ? 31.980 42.336 29.500 1.00 32.51  ? 174 TRP A CB  1 
ATOM   1423 C CG  . TRP A 1 177 ? 32.950 42.635 28.398 1.00 33.23  ? 174 TRP A CG  1 
ATOM   1424 C CD1 . TRP A 1 177 ? 33.666 43.784 28.229 1.00 38.19  ? 174 TRP A CD1 1 
ATOM   1425 C CD2 . TRP A 1 177 ? 33.424 41.725 27.388 1.00 35.40  ? 174 TRP A CD2 1 
ATOM   1426 N NE1 . TRP A 1 177 ? 34.487 43.684 27.137 1.00 39.47  ? 174 TRP A NE1 1 
ATOM   1427 C CE2 . TRP A 1 177 ? 34.377 42.424 26.614 1.00 39.62  ? 174 TRP A CE2 1 
ATOM   1428 C CE3 . TRP A 1 177 ? 33.122 40.400 27.051 1.00 38.89  ? 174 TRP A CE3 1 
ATOM   1429 C CZ2 . TRP A 1 177 ? 35.012 41.850 25.513 1.00 42.17  ? 174 TRP A CZ2 1 
ATOM   1430 C CZ3 . TRP A 1 177 ? 33.765 39.829 25.974 1.00 38.40  ? 174 TRP A CZ3 1 
ATOM   1431 C CH2 . TRP A 1 177 ? 34.689 40.548 25.216 1.00 41.00  ? 174 TRP A CH2 1 
ATOM   1432 N N   . ILE A 1 178 ? 29.494 43.314 27.928 1.00 29.89  ? 175 ILE A N   1 
ATOM   1433 C CA  . ILE A 1 178 ? 28.765 43.740 26.752 1.00 32.01  ? 175 ILE A CA  1 
ATOM   1434 C C   . ILE A 1 178 ? 27.293 43.584 27.095 1.00 30.12  ? 175 ILE A C   1 
ATOM   1435 O O   . ILE A 1 178 ? 26.886 42.538 27.589 1.00 29.33  ? 175 ILE A O   1 
ATOM   1436 C CB  . ILE A 1 178 ? 29.144 42.930 25.500 1.00 32.79  ? 175 ILE A CB  1 
ATOM   1437 C CG1 . ILE A 1 178 ? 30.642 43.004 25.189 1.00 33.11  ? 175 ILE A CG1 1 
ATOM   1438 C CG2 . ILE A 1 178 ? 28.309 43.399 24.314 1.00 36.21  ? 175 ILE A CG2 1 
ATOM   1439 C CD1 . ILE A 1 178 ? 31.054 42.132 24.028 1.00 33.80  ? 175 ILE A CD1 1 
ATOM   1440 N N   . GLY A 1 179 ? 26.507 44.628 26.836 1.00 30.08  ? 176 GLY A N   1 
ATOM   1441 C CA  . GLY A 1 179 ? 25.106 44.527 27.168 1.00 31.02  ? 176 GLY A CA  1 
ATOM   1442 C C   . GLY A 1 179 ? 24.240 45.441 26.318 1.00 30.35  ? 176 GLY A C   1 
ATOM   1443 O O   . GLY A 1 179 ? 24.744 46.264 25.550 1.00 31.13  ? 176 GLY A O   1 
ATOM   1444 N N   . PHE A 1 180 ? 22.933 45.246 26.479 1.00 27.90  ? 177 PHE A N   1 
ATOM   1445 C CA  . PHE A 1 180 ? 21.931 46.011 25.770 1.00 30.66  ? 177 PHE A CA  1 
ATOM   1446 C C   . PHE A 1 180 ? 21.044 46.777 26.738 1.00 32.17  ? 177 PHE A C   1 
ATOM   1447 O O   . PHE A 1 180 ? 20.467 46.195 27.655 1.00 30.69  ? 177 PHE A O   1 
ATOM   1448 C CB  . PHE A 1 180 ? 21.007 45.108 24.943 1.00 31.75  ? 177 PHE A CB  1 
ATOM   1449 C CG  . PHE A 1 180 ? 19.827 45.833 24.342 1.00 32.69  ? 177 PHE A CG  1 
ATOM   1450 C CD1 . PHE A 1 180 ? 20.001 46.818 23.384 1.00 34.77  ? 177 PHE A CD1 1 
ATOM   1451 C CD2 . PHE A 1 180 ? 18.536 45.573 24.780 1.00 34.09  ? 177 PHE A CD2 1 
ATOM   1452 C CE1 . PHE A 1 180 ? 18.912 47.493 22.852 1.00 34.66  ? 177 PHE A CE1 1 
ATOM   1453 C CE2 . PHE A 1 180 ? 17.451 46.254 24.256 1.00 34.27  ? 177 PHE A CE2 1 
ATOM   1454 C CZ  . PHE A 1 180 ? 17.639 47.214 23.288 1.00 34.46  ? 177 PHE A CZ  1 
ATOM   1455 N N   . CYS A 1 181 ? 20.923 48.079 26.470 1.00 31.82  ? 178 CYS A N   1 
ATOM   1456 C CA  . CYS A 1 181 ? 20.063 48.993 27.201 1.00 33.18  ? 178 CYS A CA  1 
ATOM   1457 C C   . CYS A 1 181 ? 19.071 49.572 26.195 1.00 35.74  ? 178 CYS A C   1 
ATOM   1458 O O   . CYS A 1 181 ? 19.475 50.148 25.188 1.00 36.76  ? 178 CYS A O   1 
ATOM   1459 C CB  . CYS A 1 181 ? 20.876 50.092 27.869 1.00 36.61  ? 178 CYS A CB  1 
ATOM   1460 S SG  . CYS A 1 181 ? 19.863 51.390 28.628 1.00 38.00  ? 178 CYS A SG  1 
ATOM   1461 N N   . PRO A 1 182 ? 17.747 49.459 26.426 1.00 34.27  ? 179 PRO A N   1 
ATOM   1462 C CA  . PRO A 1 182 ? 16.761 49.934 25.454 1.00 37.66  ? 179 PRO A CA  1 
ATOM   1463 C C   . PRO A 1 182 ? 16.540 51.443 25.417 1.00 39.62  ? 179 PRO A C   1 
ATOM   1464 O O   . PRO A 1 182 ? 15.401 51.894 25.395 1.00 40.17  ? 179 PRO A O   1 
ATOM   1465 C CB  . PRO A 1 182 ? 15.485 49.219 25.918 1.00 38.10  ? 179 PRO A CB  1 
ATOM   1466 C CG  . PRO A 1 182 ? 15.646 49.164 27.420 1.00 37.56  ? 179 PRO A CG  1 
ATOM   1467 C CD  . PRO A 1 182 ? 17.121 48.889 27.624 1.00 34.55  ? 179 PRO A CD  1 
ATOM   1468 N N   . HIS A 1 183 ? 17.634 52.213 25.417 1.00 39.13  ? 180 HIS A N   1 
ATOM   1469 C CA  . HIS A 1 183 ? 17.509 53.655 25.311 1.00 40.89  ? 180 HIS A CA  1 
ATOM   1470 C C   . HIS A 1 183 ? 18.751 54.217 24.632 1.00 43.29  ? 180 HIS A C   1 
ATOM   1471 O O   . HIS A 1 183 ? 19.818 53.599 24.690 1.00 43.07  ? 180 HIS A O   1 
ATOM   1472 C CB  . HIS A 1 183 ? 17.430 54.368 26.670 1.00 41.40  ? 180 HIS A CB  1 
ATOM   1473 C CG  . HIS A 1 183 ? 16.390 53.884 27.625 1.00 43.16  ? 180 HIS A CG  1 
ATOM   1474 N ND1 . HIS A 1 183 ? 15.160 54.494 27.713 1.00 46.78  ? 180 HIS A ND1 1 
ATOM   1475 C CD2 . HIS A 1 183 ? 16.318 52.800 28.403 1.00 42.44  ? 180 HIS A CD2 1 
ATOM   1476 C CE1 . HIS A 1 183 ? 14.413 53.842 28.588 1.00 49.19  ? 180 HIS A CE1 1 
ATOM   1477 N NE2 . HIS A 1 183 ? 15.101 52.814 29.026 1.00 44.80  ? 180 HIS A NE2 1 
ATOM   1478 N N   . PRO A 1 184 ? 18.650 55.386 23.954 1.00 46.12  ? 181 PRO A N   1 
ATOM   1479 C CA  . PRO A 1 184 ? 19.817 56.037 23.373 1.00 47.29  ? 181 PRO A CA  1 
ATOM   1480 C C   . PRO A 1 184 ? 20.692 56.498 24.538 1.00 43.25  ? 181 PRO A C   1 
ATOM   1481 O O   . PRO A 1 184 ? 20.179 56.835 25.599 1.00 47.82  ? 181 PRO A O   1 
ATOM   1482 C CB  . PRO A 1 184 ? 19.269 57.231 22.569 1.00 52.12  ? 181 PRO A CB  1 
ATOM   1483 C CG  . PRO A 1 184 ? 17.758 57.009 22.498 1.00 52.68  ? 181 PRO A CG  1 
ATOM   1484 C CD  . PRO A 1 184 ? 17.406 56.121 23.676 1.00 47.91  ? 181 PRO A CD  1 
ATOM   1485 N N   . LEU A 1 185 ? 22.013 56.456 24.354 1.00 46.35  ? 182 LEU A N   1 
ATOM   1486 C CA  . LEU A 1 185 ? 22.952 56.872 25.381 1.00 43.84  ? 182 LEU A CA  1 
ATOM   1487 C C   . LEU A 1 185 ? 23.976 57.810 24.749 1.00 47.27  ? 182 LEU A C   1 
ATOM   1488 O O   . LEU A 1 185 ? 24.250 57.713 23.557 1.00 49.02  ? 182 LEU A O   1 
ATOM   1489 C CB  . LEU A 1 185 ? 23.625 55.629 25.967 1.00 40.76  ? 182 LEU A CB  1 
ATOM   1490 C CG  . LEU A 1 185 ? 22.716 54.629 26.682 1.00 40.45  ? 182 LEU A CG  1 
ATOM   1491 C CD1 . LEU A 1 185 ? 23.549 53.501 27.259 1.00 38.62  ? 182 LEU A CD1 1 
ATOM   1492 C CD2 . LEU A 1 185 ? 21.912 55.296 27.790 1.00 44.18  ? 182 LEU A CD2 1 
ATOM   1493 N N   . ARG A 1 186 ? 24.536 58.708 25.566 1.00 48.61  ? 183 ARG A N   1 
ATOM   1494 C CA  . ARG A 1 186 ? 25.507 59.676 25.094 1.00 54.11  ? 183 ARG A CA  1 
ATOM   1495 C C   . ARG A 1 186 ? 26.885 59.284 25.625 1.00 51.48  ? 183 ARG A C   1 
ATOM   1496 O O   . ARG A 1 186 ? 27.036 58.988 26.802 1.00 49.56  ? 183 ARG A O   1 
ATOM   1497 C CB  . ARG A 1 186 ? 25.048 61.079 25.510 1.00 62.29  ? 183 ARG A CB  1 
ATOM   1498 C CG  . ARG A 1 186 ? 23.647 61.416 25.012 1.00 65.75  ? 183 ARG A CG  1 
ATOM   1499 C CD  . ARG A 1 186 ? 23.162 62.813 25.360 1.00 75.06  ? 183 ARG A CD  1 
ATOM   1500 N NE  . ARG A 1 186 ? 23.932 63.884 24.738 1.00 87.20  ? 183 ARG A NE  1 
ATOM   1501 C CZ  . ARG A 1 186 ? 24.034 64.092 23.426 1.00 89.47  ? 183 ARG A CZ  1 
ATOM   1502 N NH1 . ARG A 1 186 ? 23.401 63.305 22.573 1.00 83.71  ? 183 ARG A NH1 1 
ATOM   1503 N NH2 . ARG A 1 186 ? 24.761 65.098 22.970 1.00 91.83  ? 183 ARG A NH2 1 
ATOM   1504 N N   . ALA A 1 187 ? 27.887 59.309 24.735 1.00 56.31  ? 184 ALA A N   1 
ATOM   1505 C CA  . ALA A 1 187 ? 29.256 58.931 25.060 1.00 54.95  ? 184 ALA A CA  1 
ATOM   1506 C C   . ALA A 1 187 ? 29.812 59.752 26.221 1.00 59.29  ? 184 ALA A C   1 
ATOM   1507 O O   . ALA A 1 187 ? 30.603 59.244 27.014 1.00 55.92  ? 184 ALA A O   1 
ATOM   1508 C CB  . ALA A 1 187 ? 30.124 59.084 23.832 1.00 59.78  ? 184 ALA A CB  1 
ATOM   1509 N N   . THR A 1 188 ? 29.379 61.012 26.319 1.00 65.11  ? 185 THR A N   1 
ATOM   1510 C CA  . THR A 1 188 ? 29.860 61.925 27.344 1.00 69.67  ? 185 THR A CA  1 
ATOM   1511 C C   . THR A 1 188 ? 29.490 61.443 28.749 1.00 64.80  ? 185 THR A C   1 
ATOM   1512 O O   . THR A 1 188 ? 30.126 61.857 29.715 1.00 69.31  ? 185 THR A O   1 
ATOM   1513 C CB  . THR A 1 188 ? 29.364 63.351 27.064 1.00 75.28  ? 185 THR A CB  1 
ATOM   1514 O OG1 . THR A 1 188 ? 27.938 63.358 27.091 1.00 80.16  ? 185 THR A OG1 1 
ATOM   1515 C CG2 . THR A 1 188 ? 29.835 63.879 25.727 1.00 80.95  ? 185 THR A CG2 1 
ATOM   1516 N N   . ASP A 1 189 ? 28.485 60.563 28.872 1.00 57.66  ? 186 ASP A N   1 
ATOM   1517 C CA  . ASP A 1 189 ? 28.093 60.088 30.192 1.00 58.62  ? 186 ASP A CA  1 
ATOM   1518 C C   . ASP A 1 189 ? 28.856 58.833 30.601 1.00 53.27  ? 186 ASP A C   1 
ATOM   1519 O O   . ASP A 1 189 ? 28.779 58.442 31.765 1.00 60.40  ? 186 ASP A O   1 
ATOM   1520 C CB  . ASP A 1 189 ? 26.600 59.762 30.296 1.00 53.96  ? 186 ASP A CB  1 
ATOM   1521 C CG  . ASP A 1 189 ? 25.688 60.953 30.075 1.00 62.20  ? 186 ASP A CG  1 
ATOM   1522 O OD1 . ASP A 1 189 ? 25.866 61.965 30.784 1.00 72.05  ? 186 ASP A OD1 1 
ATOM   1523 O OD2 . ASP A 1 189 ? 24.773 60.837 29.249 1.00 63.94  ? 186 ASP A OD2 1 
ATOM   1524 N N   . PHE A 1 190 ? 29.594 58.212 29.672 1.00 55.34  ? 187 PHE A N   1 
ATOM   1525 C CA  . PHE A 1 190 ? 30.281 56.978 30.023 1.00 49.59  ? 187 PHE A CA  1 
ATOM   1526 C C   . PHE A 1 190 ? 31.797 57.115 29.970 1.00 52.68  ? 187 PHE A C   1 
ATOM   1527 O O   . PHE A 1 190 ? 32.334 58.067 29.407 1.00 50.71  ? 187 PHE A O   1 
ATOM   1528 C CB  . PHE A 1 190 ? 29.780 55.811 29.161 1.00 47.70  ? 187 PHE A CB  1 
ATOM   1529 C CG  . PHE A 1 190 ? 28.337 55.465 29.420 1.00 41.89  ? 187 PHE A CG  1 
ATOM   1530 C CD1 . PHE A 1 190 ? 27.313 56.301 29.004 1.00 43.20  ? 187 PHE A CD1 1 
ATOM   1531 C CD2 . PHE A 1 190 ? 28.018 54.390 30.232 1.00 40.89  ? 187 PHE A CD2 1 
ATOM   1532 C CE1 . PHE A 1 190 ? 25.992 56.003 29.293 1.00 41.04  ? 187 PHE A CE1 1 
ATOM   1533 C CE2 . PHE A 1 190 ? 26.697 54.108 30.547 1.00 38.48  ? 187 PHE A CE2 1 
ATOM   1534 C CZ  . PHE A 1 190 ? 25.688 54.911 30.073 1.00 39.59  ? 187 PHE A CZ  1 
ATOM   1535 N N   . PRO A 1 191 ? 32.526 56.156 30.590 1.00 50.82  ? 188 PRO A N   1 
ATOM   1536 C CA  . PRO A 1 191 ? 33.989 56.163 30.582 1.00 56.41  ? 188 PRO A CA  1 
ATOM   1537 C C   . PRO A 1 191 ? 34.563 56.064 29.172 1.00 58.15  ? 188 PRO A C   1 
ATOM   1538 O O   . PRO A 1 191 ? 33.879 55.636 28.242 1.00 48.76  ? 188 PRO A O   1 
ATOM   1539 C CB  . PRO A 1 191 ? 34.368 54.906 31.384 1.00 53.68  ? 188 PRO A CB  1 
ATOM   1540 C CG  . PRO A 1 191 ? 33.151 54.622 32.238 1.00 54.72  ? 188 PRO A CG  1 
ATOM   1541 C CD  . PRO A 1 191 ? 31.979 55.034 31.373 1.00 51.40  ? 188 PRO A CD  1 
ATOM   1542 N N   . ALA A 1 192 ? 35.837 56.443 29.035 1.00 59.86  ? 189 ALA A N   1 
ATOM   1543 C CA  . ALA A 1 192 ? 36.521 56.408 27.751 1.00 60.15  ? 189 ALA A CA  1 
ATOM   1544 C C   . ALA A 1 192 ? 36.693 54.971 27.253 1.00 59.14  ? 189 ALA A C   1 
ATOM   1545 O O   . ALA A 1 192 ? 36.763 54.740 26.048 1.00 59.43  ? 189 ALA A O   1 
ATOM   1546 C CB  . ALA A 1 192 ? 37.853 57.103 27.880 1.00 63.80  ? 189 ALA A CB  1 
ATOM   1547 N N   . ALA A 1 193 ? 36.772 54.011 28.183 1.00 51.27  ? 190 ALA A N   1 
ATOM   1548 C CA  . ALA A 1 193 ? 36.951 52.608 27.840 1.00 51.88  ? 190 ALA A CA  1 
ATOM   1549 C C   . ALA A 1 193 ? 35.668 52.000 27.269 1.00 50.62  ? 190 ALA A C   1 
ATOM   1550 O O   . ALA A 1 193 ? 35.712 50.908 26.705 1.00 51.76  ? 190 ALA A O   1 
ATOM   1551 C CB  . ALA A 1 193 ? 37.392 51.839 29.064 1.00 54.88  ? 190 ALA A CB  1 
ATOM   1552 N N   . THR A 1 194 ? 34.538 52.703 27.425 1.00 44.25  ? 191 THR A N   1 
ATOM   1553 C CA  . THR A 1 194 ? 33.253 52.210 26.945 1.00 45.05  ? 191 THR A CA  1 
ATOM   1554 C C   . THR A 1 194 ? 32.998 52.625 25.500 1.00 47.48  ? 191 THR A C   1 
ATOM   1555 O O   . THR A 1 194 ? 33.239 53.764 25.124 1.00 47.21  ? 191 THR A O   1 
ATOM   1556 C CB  . THR A 1 194 ? 32.089 52.726 27.810 1.00 44.33  ? 191 THR A CB  1 
ATOM   1557 O OG1 . THR A 1 194 ? 32.162 52.126 29.103 1.00 43.06  ? 191 THR A OG1 1 
ATOM   1558 C CG2 . THR A 1 194 ? 30.718 52.400 27.259 1.00 46.45  ? 191 THR A CG2 1 
ATOM   1559 N N   . GLU A 1 195 ? 32.551 51.662 24.690 1.00 41.58  ? 192 GLU A N   1 
ATOM   1560 C CA  . GLU A 1 195 ? 32.139 51.929 23.326 1.00 42.16  ? 192 GLU A CA  1 
ATOM   1561 C C   . GLU A 1 195 ? 30.623 51.769 23.290 1.00 40.50  ? 192 GLU A C   1 
ATOM   1562 O O   . GLU A 1 195 ? 30.098 50.781 23.813 1.00 39.01  ? 192 GLU A O   1 
ATOM   1563 C CB  . GLU A 1 195 ? 32.774 50.987 22.297 1.00 41.35  ? 192 GLU A CB  1 
ATOM   1564 C CG  . GLU A 1 195 ? 32.133 51.168 20.929 1.00 44.37  ? 192 GLU A CG  1 
ATOM   1565 C CD  . GLU A 1 195 ? 32.566 50.273 19.782 1.00 45.28  ? 192 GLU A CD  1 
ATOM   1566 O OE1 . GLU A 1 195 ? 33.486 49.449 19.961 1.00 44.49  ? 192 GLU A OE1 1 
ATOM   1567 O OE2 . GLU A 1 195 ? 31.954 50.404 18.705 1.00 39.72  ? 192 GLU A OE2 1 
ATOM   1568 N N   . LEU A 1 196 ? 29.940 52.774 22.729 1.00 39.80  ? 193 LEU A N   1 
ATOM   1569 C CA  . LEU A 1 196 ? 28.494 52.759 22.569 1.00 38.32  ? 193 LEU A CA  1 
ATOM   1570 C C   . LEU A 1 196 ? 28.153 52.487 21.104 1.00 41.49  ? 193 LEU A C   1 
ATOM   1571 O O   . LEU A 1 196 ? 28.670 53.158 20.212 1.00 41.75  ? 193 LEU A O   1 
ATOM   1572 C CB  . LEU A 1 196 ? 27.918 54.122 22.967 1.00 41.29  ? 193 LEU A CB  1 
ATOM   1573 C CG  . LEU A 1 196 ? 28.101 54.568 24.415 1.00 42.51  ? 193 LEU A CG  1 
ATOM   1574 C CD1 . LEU A 1 196 ? 27.277 55.819 24.686 1.00 48.07  ? 193 LEU A CD1 1 
ATOM   1575 C CD2 . LEU A 1 196 ? 27.710 53.473 25.389 1.00 39.67  ? 193 LEU A CD2 1 
ATOM   1576 N N   . VAL A 1 197 ? 27.284 51.502 20.862 1.00 36.84  ? 194 VAL A N   1 
ATOM   1577 C CA  . VAL A 1 197 ? 26.831 51.197 19.518 1.00 38.62  ? 194 VAL A CA  1 
ATOM   1578 C C   . VAL A 1 197 ? 25.336 51.500 19.479 1.00 38.28  ? 194 VAL A C   1 
ATOM   1579 O O   . VAL A 1 197 ? 24.541 50.820 20.127 1.00 37.84  ? 194 VAL A O   1 
ATOM   1580 C CB  . VAL A 1 197 ? 27.132 49.742 19.103 1.00 38.02  ? 194 VAL A CB  1 
ATOM   1581 C CG1 . VAL A 1 197 ? 26.632 49.451 17.695 1.00 41.98  ? 194 VAL A CG1 1 
ATOM   1582 C CG2 . VAL A 1 197 ? 28.617 49.424 19.212 1.00 41.79  ? 194 VAL A CG2 1 
ATOM   1583 N N   . ASP A 1 198 ? 24.972 52.552 18.737 1.00 43.07  ? 195 ASP A N   1 
ATOM   1584 C CA  . ASP A 1 198 ? 23.585 52.968 18.619 1.00 42.50  ? 195 ASP A CA  1 
ATOM   1585 C C   . ASP A 1 198 ? 22.817 52.009 17.713 1.00 46.62  ? 195 ASP A C   1 
ATOM   1586 O O   . ASP A 1 198 ? 23.247 51.716 16.601 1.00 50.37  ? 195 ASP A O   1 
ATOM   1587 C CB  . ASP A 1 198 ? 23.459 54.386 18.059 1.00 46.71  ? 195 ASP A CB  1 
ATOM   1588 C CG  . ASP A 1 198 ? 22.016 54.852 17.956 1.00 51.93  ? 195 ASP A CG  1 
ATOM   1589 O OD1 . ASP A 1 198 ? 21.341 54.893 19.001 1.00 56.53  ? 195 ASP A OD1 1 
ATOM   1590 O OD2 . ASP A 1 198 ? 21.575 55.164 16.840 1.00 56.62  ? 195 ASP A OD2 1 
ATOM   1591 N N   . ILE A 1 199 ? 21.664 51.545 18.204 1.00 44.55  ? 196 ILE A N   1 
ATOM   1592 C CA  . ILE A 1 199 ? 20.792 50.664 17.452 1.00 48.36  ? 196 ILE A CA  1 
ATOM   1593 C C   . ILE A 1 199 ? 19.475 51.424 17.317 1.00 48.94  ? 196 ILE A C   1 
ATOM   1594 O O   . ILE A 1 199 ? 18.629 51.339 18.200 1.00 46.44  ? 196 ILE A O   1 
ATOM   1595 C CB  . ILE A 1 199 ? 20.607 49.298 18.149 1.00 48.44  ? 196 ILE A CB  1 
ATOM   1596 C CG1 . ILE A 1 199 ? 21.928 48.676 18.619 1.00 50.79  ? 196 ILE A CG1 1 
ATOM   1597 C CG2 . ILE A 1 199 ? 19.820 48.349 17.257 1.00 53.77  ? 196 ILE A CG2 1 
ATOM   1598 C CD1 . ILE A 1 199 ? 22.923 48.407 17.512 1.00 55.52  ? 196 ILE A CD1 1 
ATOM   1599 N N   . PRO A 1 200 ? 19.276 52.236 16.248 1.00 52.81  ? 197 PRO A N   1 
ATOM   1600 C CA  . PRO A 1 200 ? 18.044 53.018 16.096 1.00 54.30  ? 197 PRO A CA  1 
ATOM   1601 C C   . PRO A 1 200 ? 16.794 52.145 16.189 1.00 54.40  ? 197 PRO A C   1 
ATOM   1602 O O   . PRO A 1 200 ? 16.756 51.054 15.629 1.00 59.96  ? 197 PRO A O   1 
ATOM   1603 C CB  . PRO A 1 200 ? 18.161 53.681 14.713 1.00 59.32  ? 197 PRO A CB  1 
ATOM   1604 C CG  . PRO A 1 200 ? 19.324 52.990 14.026 1.00 58.73  ? 197 PRO A CG  1 
ATOM   1605 C CD  . PRO A 1 200 ? 20.203 52.424 15.122 1.00 56.88  ? 197 PRO A CD  1 
ATOM   1606 N N   . GLY A 1 201 ? 15.787 52.630 16.922 1.00 58.12  ? 198 GLY A N   1 
ATOM   1607 C CA  . GLY A 1 201 ? 14.549 51.893 17.117 1.00 65.42  ? 198 GLY A CA  1 
ATOM   1608 C C   . GLY A 1 201 ? 14.692 50.755 18.130 1.00 63.56  ? 198 GLY A C   1 
ATOM   1609 O O   . GLY A 1 201 ? 13.813 49.901 18.231 1.00 60.00  ? 198 GLY A O   1 
ATOM   1610 N N   . ARG A 1 202 ? 15.808 50.737 18.873 1.00 55.95  ? 199 ARG A N   1 
ATOM   1611 C CA  . ARG A 1 202 ? 16.035 49.695 19.865 1.00 51.18  ? 199 ARG A CA  1 
ATOM   1612 C C   . ARG A 1 202 ? 16.671 50.282 21.123 1.00 46.76  ? 199 ARG A C   1 
ATOM   1613 O O   . ARG A 1 202 ? 16.094 50.212 22.206 1.00 44.82  ? 199 ARG A O   1 
ATOM   1614 C CB  . ARG A 1 202 ? 16.943 48.590 19.314 1.00 52.24  ? 199 ARG A CB  1 
ATOM   1615 C CG  . ARG A 1 202 ? 16.331 47.696 18.242 1.00 57.82  ? 199 ARG A CG  1 
ATOM   1616 C CD  . ARG A 1 202 ? 15.215 46.815 18.787 1.00 57.77  ? 199 ARG A CD  1 
ATOM   1617 N NE  . ARG A 1 202 ? 14.727 45.836 17.824 1.00 58.84  ? 199 ARG A NE  1 
ATOM   1618 C CZ  . ARG A 1 202 ? 14.105 46.123 16.686 1.00 68.60  ? 199 ARG A CZ  1 
ATOM   1619 N NH1 . ARG A 1 202 ? 13.799 47.374 16.392 1.00 74.26  ? 199 ARG A NH1 1 
ATOM   1620 N NH2 . ARG A 1 202 ? 13.731 45.148 15.876 1.00 69.09  ? 199 ARG A NH2 1 
ATOM   1621 N N   . GLY A 1 203 ? 17.879 50.832 20.966 1.00 43.06  ? 200 GLY A N   1 
ATOM   1622 C CA  . GLY A 1 203 ? 18.607 51.381 22.093 1.00 39.98  ? 200 GLY A CA  1 
ATOM   1623 C C   . GLY A 1 203 ? 20.107 51.419 21.830 1.00 39.06  ? 200 GLY A C   1 
ATOM   1624 O O   . GLY A 1 203 ? 20.540 51.901 20.782 1.00 40.92  ? 200 GLY A O   1 
ATOM   1625 N N   . THR A 1 204 ? 20.875 50.858 22.765 1.00 34.77  ? 201 THR A N   1 
ATOM   1626 C CA  . THR A 1 204 ? 22.321 50.896 22.678 1.00 35.62  ? 201 THR A CA  1 
ATOM   1627 C C   . THR A 1 204 ? 22.972 49.614 23.185 1.00 37.34  ? 201 THR A C   1 
ATOM   1628 O O   . THR A 1 204 ? 22.536 49.013 24.170 1.00 35.60  ? 201 THR A O   1 
ATOM   1629 C CB  . THR A 1 204 ? 22.854 52.035 23.563 1.00 37.45  ? 201 THR A CB  1 
ATOM   1630 O OG1 . THR A 1 204 ? 22.131 53.230 23.260 1.00 39.58  ? 201 THR A OG1 1 
ATOM   1631 C CG2 . THR A 1 204 ? 24.343 52.266 23.429 1.00 39.82  ? 201 THR A CG2 1 
ATOM   1632 N N   . LEU A 1 205 ? 24.037 49.221 22.487 1.00 36.01  ? 202 LEU A N   1 
ATOM   1633 C CA  . LEU A 1 205 ? 24.895 48.139 22.930 1.00 33.65  ? 202 LEU A CA  1 
ATOM   1634 C C   . LEU A 1 205 ? 26.126 48.791 23.549 1.00 36.35  ? 202 LEU A C   1 
ATOM   1635 O O   . LEU A 1 205 ? 26.698 49.708 22.962 1.00 39.44  ? 202 LEU A O   1 
ATOM   1636 C CB  . LEU A 1 205 ? 25.280 47.240 21.757 1.00 35.27  ? 202 LEU A CB  1 
ATOM   1637 C CG  . LEU A 1 205 ? 24.153 46.428 21.137 1.00 37.24  ? 202 LEU A CG  1 
ATOM   1638 C CD1 . LEU A 1 205 ? 24.684 45.543 20.017 1.00 37.85  ? 202 LEU A CD1 1 
ATOM   1639 C CD2 . LEU A 1 205 ? 23.475 45.566 22.188 1.00 34.43  ? 202 LEU A CD2 1 
ATOM   1640 N N   . LEU A 1 206 ? 26.487 48.360 24.758 1.00 36.21  ? 203 LEU A N   1 
ATOM   1641 C CA  . LEU A 1 206 ? 27.668 48.885 25.421 1.00 35.14  ? 203 LEU A CA  1 
ATOM   1642 C C   . LEU A 1 206 ? 28.746 47.812 25.464 1.00 37.06  ? 203 LEU A C   1 
ATOM   1643 O O   . LEU A 1 206 ? 28.440 46.664 25.763 1.00 34.81  ? 203 LEU A O   1 
ATOM   1644 C CB  . LEU A 1 206 ? 27.342 49.314 26.858 1.00 35.98  ? 203 LEU A CB  1 
ATOM   1645 C CG  . LEU A 1 206 ? 26.345 50.457 27.028 1.00 35.06  ? 203 LEU A CG  1 
ATOM   1646 C CD1 . LEU A 1 206 ? 24.911 49.971 26.943 1.00 37.78  ? 203 LEU A CD1 1 
ATOM   1647 C CD2 . LEU A 1 206 ? 26.585 51.194 28.338 1.00 38.33  ? 203 LEU A CD2 1 
ATOM   1648 N N   . LEU A 1 207 ? 29.980 48.211 25.124 1.00 32.53  ? 204 LEU A N   1 
ATOM   1649 C CA  . LEU A 1 207 ? 31.170 47.380 25.243 1.00 37.36  ? 204 LEU A CA  1 
ATOM   1650 C C   . LEU A 1 207 ? 32.022 48.099 26.279 1.00 36.23  ? 204 LEU A C   1 
ATOM   1651 O O   . LEU A 1 207 ? 32.607 49.134 25.982 1.00 40.22  ? 204 LEU A O   1 
ATOM   1652 C CB  . LEU A 1 207 ? 31.939 47.236 23.925 1.00 38.73  ? 204 LEU A CB  1 
ATOM   1653 C CG  . LEU A 1 207 ? 31.259 46.457 22.803 1.00 48.98  ? 204 LEU A CG  1 
ATOM   1654 C CD1 . LEU A 1 207 ? 30.209 47.298 22.087 1.00 53.74  ? 204 LEU A CD1 1 
ATOM   1655 C CD2 . LEU A 1 207 ? 32.309 45.946 21.819 1.00 49.76  ? 204 LEU A CD2 1 
ATOM   1656 N N   . ASN A 1 208 ? 32.027 47.577 27.504 1.00 35.75  ? 205 ASN A N   1 
ATOM   1657 C CA  . ASN A 1 208 ? 32.700 48.247 28.603 1.00 35.37  ? 205 ASN A CA  1 
ATOM   1658 C C   . ASN A 1 208 ? 34.134 47.772 28.760 1.00 40.49  ? 205 ASN A C   1 
ATOM   1659 O O   . ASN A 1 208 ? 34.412 46.828 29.497 1.00 41.50  ? 205 ASN A O   1 
ATOM   1660 C CB  . ASN A 1 208 ? 31.863 48.110 29.868 1.00 36.06  ? 205 ASN A CB  1 
ATOM   1661 C CG  . ASN A 1 208 ? 30.496 48.715 29.663 1.00 38.89  ? 205 ASN A CG  1 
ATOM   1662 O OD1 . ASN A 1 208 ? 30.385 49.842 29.187 1.00 39.43  ? 205 ASN A OD1 1 
ATOM   1663 N ND2 . ASN A 1 208 ? 29.455 47.939 29.904 1.00 37.44  ? 205 ASN A ND2 1 
ATOM   1664 N N   . GLY A 1 209 ? 35.027 48.479 28.057 1.00 43.36  ? 206 GLY A N   1 
ATOM   1665 C CA  . GLY A 1 209 ? 36.447 48.200 28.104 1.00 48.47  ? 206 GLY A CA  1 
ATOM   1666 C C   . GLY A 1 209 ? 36.791 46.900 27.399 1.00 48.52  ? 206 GLY A C   1 
ATOM   1667 O O   . GLY A 1 209 ? 36.010 46.382 26.607 1.00 45.03  ? 206 GLY A O   1 
ATOM   1668 N N   . ARG A 1 210 ? 37.967 46.387 27.742 1.00 46.73  ? 207 ARG A N   1 
ATOM   1669 C CA  . ARG A 1 210 ? 38.498 45.165 27.179 1.00 49.29  ? 207 ARG A CA  1 
ATOM   1670 C C   . ARG A 1 210 ? 37.948 43.981 27.977 1.00 49.59  ? 207 ARG A C   1 
ATOM   1671 O O   . ARG A 1 210 ? 37.441 44.150 29.088 1.00 53.68  ? 207 ARG A O   1 
ATOM   1672 C CB  . ARG A 1 210 ? 40.026 45.275 27.235 1.00 55.67  ? 207 ARG A CB  1 
ATOM   1673 C CG  . ARG A 1 210 ? 40.578 46.491 26.497 1.00 64.07  ? 207 ARG A CG  1 
ATOM   1674 C CD  . ARG A 1 210 ? 42.014 46.791 26.882 1.00 76.55  ? 207 ARG A CD  1 
ATOM   1675 N NE  . ARG A 1 210 ? 42.972 45.739 26.579 1.00 83.47  ? 207 ARG A NE  1 
ATOM   1676 C CZ  . ARG A 1 210 ? 44.120 45.923 25.935 1.00 89.71  ? 207 ARG A CZ  1 
ATOM   1677 N NH1 . ARG A 1 210 ? 44.926 44.899 25.718 1.00 97.42  ? 207 ARG A NH1 1 
ATOM   1678 N NH2 . ARG A 1 210 ? 44.476 47.130 25.531 1.00 90.36  ? 207 ARG A NH2 1 
ATOM   1679 N N   . GLU A 1 211 ? 38.038 42.790 27.378 1.00 48.42  ? 208 GLU A N   1 
ATOM   1680 C CA  . GLU A 1 211 ? 37.613 41.548 28.004 1.00 52.21  ? 208 GLU A CA  1 
ATOM   1681 C C   . GLU A 1 211 ? 38.087 41.484 29.456 1.00 53.68  ? 208 GLU A C   1 
ATOM   1682 O O   . GLU A 1 211 ? 39.282 41.578 29.731 1.00 52.14  ? 208 GLU A O   1 
ATOM   1683 C CB  . GLU A 1 211 ? 38.181 40.377 27.202 1.00 61.40  ? 208 GLU A CB  1 
ATOM   1684 C CG  . GLU A 1 211 ? 37.988 39.018 27.848 1.00 60.11  ? 208 GLU A CG  1 
ATOM   1685 C CD  . GLU A 1 211 ? 38.576 37.879 27.034 1.00 68.71  ? 208 GLU A CD  1 
ATOM   1686 O OE1 . GLU A 1 211 ? 39.028 38.137 25.895 1.00 60.52  ? 208 GLU A OE1 1 
ATOM   1687 O OE2 . GLU A 1 211 ? 38.655 36.754 27.570 1.00 75.35  ? 208 GLU A OE2 1 
ATOM   1688 N N   . PRO A 1 212 ? 37.160 41.369 30.433 1.00 48.97  ? 209 PRO A N   1 
ATOM   1689 C CA  . PRO A 1 212 ? 37.531 41.248 31.843 1.00 53.60  ? 209 PRO A CA  1 
ATOM   1690 C C   . PRO A 1 212 ? 38.453 40.041 31.973 1.00 57.14  ? 209 PRO A C   1 
ATOM   1691 O O   . PRO A 1 212 ? 38.141 38.975 31.448 1.00 63.60  ? 209 PRO A O   1 
ATOM   1692 C CB  . PRO A 1 212 ? 36.191 41.077 32.575 1.00 48.49  ? 209 PRO A CB  1 
ATOM   1693 C CG  . PRO A 1 212 ? 35.171 41.694 31.633 1.00 45.89  ? 209 PRO A CG  1 
ATOM   1694 C CD  . PRO A 1 212 ? 35.703 41.438 30.239 1.00 47.41  ? 209 PRO A CD  1 
ATOM   1695 N N   . MET A 1 213 ? 39.573 40.212 32.685 1.00 62.09  ? 210 MET A N   1 
ATOM   1696 C CA  . MET A 1 213 ? 40.556 39.144 32.778 1.00 64.83  ? 210 MET A CA  1 
ATOM   1697 C C   . MET A 1 213 ? 40.604 38.595 34.208 1.00 68.44  ? 210 MET A C   1 
ATOM   1698 O O   . MET A 1 213 ? 40.626 39.423 35.132 1.00 65.91  ? 210 MET A O   1 
ATOM   1699 C CB  . MET A 1 213 ? 41.929 39.699 32.384 1.00 68.24  ? 210 MET A CB  1 
ATOM   1700 C CG  . MET A 1 213 ? 42.033 39.988 30.884 1.00 69.49  ? 210 MET A CG  1 
ATOM   1701 S SD  . MET A 1 213 ? 41.721 38.592 29.760 1.00 86.67  ? 210 MET A SD  1 
ATOM   1702 C CE  . MET A 1 213 ? 42.534 37.267 30.643 1.00 90.90  ? 210 MET A CE  1 
ATOM   1703 N N   . PHE A 1 221 ? 36.167 45.678 38.633 1.00 88.20  ? 218 PHE A N   1 
ATOM   1704 C CA  . PHE A 1 221 ? 36.112 46.147 37.222 1.00 79.44  ? 218 PHE A CA  1 
ATOM   1705 C C   . PHE A 1 221 ? 35.279 47.419 37.135 1.00 72.34  ? 218 PHE A C   1 
ATOM   1706 O O   . PHE A 1 221 ? 34.091 47.369 36.815 1.00 58.80  ? 218 PHE A O   1 
ATOM   1707 C CB  . PHE A 1 221 ? 35.568 45.051 36.304 1.00 89.01  ? 218 PHE A CB  1 
ATOM   1708 C CG  . PHE A 1 221 ? 36.437 43.822 36.238 1.00 99.43  ? 218 PHE A CG  1 
ATOM   1709 C CD1 . PHE A 1 221 ? 37.735 43.903 35.757 1.00 104.65 ? 218 PHE A CD1 1 
ATOM   1710 C CD2 . PHE A 1 221 ? 35.972 42.594 36.679 1.00 105.13 ? 218 PHE A CD2 1 
ATOM   1711 C CE1 . PHE A 1 221 ? 38.543 42.778 35.703 1.00 106.54 ? 218 PHE A CE1 1 
ATOM   1712 C CE2 . PHE A 1 221 ? 36.782 41.471 36.629 1.00 106.79 ? 218 PHE A CE2 1 
ATOM   1713 C CZ  . PHE A 1 221 ? 38.066 41.565 36.142 1.00 106.96 ? 218 PHE A CZ  1 
ATOM   1714 N N   . GLU A 1 222 ? 35.937 48.549 37.420 1.00 67.34  ? 219 GLU A N   1 
ATOM   1715 C CA  . GLU A 1 222 ? 35.306 49.858 37.377 1.00 68.15  ? 219 GLU A CA  1 
ATOM   1716 C C   . GLU A 1 222 ? 34.702 50.104 35.996 1.00 54.79  ? 219 GLU A C   1 
ATOM   1717 O O   . GLU A 1 222 ? 33.773 50.895 35.865 1.00 57.12  ? 219 GLU A O   1 
ATOM   1718 C CB  . GLU A 1 222 ? 36.304 50.976 37.697 1.00 72.52  ? 219 GLU A CB  1 
ATOM   1719 C CG  . GLU A 1 222 ? 37.466 51.096 36.718 1.00 83.35  ? 219 GLU A CG  1 
ATOM   1720 C CD  . GLU A 1 222 ? 38.448 49.935 36.667 1.00 99.89  ? 219 GLU A CD  1 
ATOM   1721 O OE1 . GLU A 1 222 ? 38.284 48.979 37.450 1.00 101.35 ? 219 GLU A OE1 1 
ATOM   1722 O OE2 . GLU A 1 222 ? 39.377 49.989 35.836 1.00 116.60 ? 219 GLU A OE2 1 
ATOM   1723 N N   . ARG A 1 223 ? 35.260 49.449 34.969 1.00 50.99  ? 220 ARG A N   1 
ATOM   1724 C CA  . ARG A 1 223 ? 34.764 49.598 33.610 1.00 47.84  ? 220 ARG A CA  1 
ATOM   1725 C C   . ARG A 1 223 ? 33.282 49.235 33.549 1.00 49.15  ? 220 ARG A C   1 
ATOM   1726 O O   . ARG A 1 223 ? 32.485 49.952 32.942 1.00 50.59  ? 220 ARG A O   1 
ATOM   1727 C CB  . ARG A 1 223 ? 35.606 48.747 32.654 1.00 54.40  ? 220 ARG A CB  1 
ATOM   1728 C CG  . ARG A 1 223 ? 37.036 49.241 32.485 1.00 67.80  ? 220 ARG A CG  1 
ATOM   1729 C CD  . ARG A 1 223 ? 37.877 48.316 31.627 1.00 84.19  ? 220 ARG A CD  1 
ATOM   1730 N NE  . ARG A 1 223 ? 39.188 48.886 31.331 1.00 98.14  ? 220 ARG A NE  1 
ATOM   1731 C CZ  . ARG A 1 223 ? 40.145 48.279 30.634 1.00 97.65  ? 220 ARG A CZ  1 
ATOM   1732 N NH1 . ARG A 1 223 ? 41.275 48.913 30.379 1.00 107.30 ? 220 ARG A NH1 1 
ATOM   1733 N NH2 . ARG A 1 223 ? 39.964 47.057 30.165 1.00 97.77  ? 220 ARG A NH2 1 
ATOM   1734 N N   . VAL A 1 224 ? 32.921 48.113 34.171 1.00 41.99  ? 221 VAL A N   1 
ATOM   1735 C CA  . VAL A 1 224 ? 31.532 47.685 34.170 1.00 38.86  ? 221 VAL A CA  1 
ATOM   1736 C C   . VAL A 1 224 ? 30.788 48.436 35.272 1.00 40.33  ? 221 VAL A C   1 
ATOM   1737 O O   . VAL A 1 224 ? 29.677 48.901 35.061 1.00 37.71  ? 221 VAL A O   1 
ATOM   1738 C CB  . VAL A 1 224 ? 31.400 46.155 34.325 1.00 38.95  ? 221 VAL A CB  1 
ATOM   1739 C CG1 . VAL A 1 224 ? 29.954 45.720 34.504 1.00 36.84  ? 221 VAL A CG1 1 
ATOM   1740 C CG2 . VAL A 1 224 ? 32.032 45.409 33.159 1.00 41.22  ? 221 VAL A CG2 1 
ATOM   1741 N N   . GLY A 1 225 ? 31.431 48.576 36.439 1.00 39.53  ? 222 GLY A N   1 
ATOM   1742 C CA  . GLY A 1 225 ? 30.813 49.237 37.569 1.00 38.83  ? 222 GLY A CA  1 
ATOM   1743 C C   . GLY A 1 225 ? 30.394 50.666 37.251 1.00 41.40  ? 222 GLY A C   1 
ATOM   1744 O O   . GLY A 1 225 ? 29.282 51.065 37.572 1.00 37.89  ? 222 GLY A O   1 
ATOM   1745 N N   . GLU A 1 226 ? 31.283 51.426 36.602 1.00 43.71  ? 223 GLU A N   1 
ATOM   1746 C CA  . GLU A 1 226 ? 30.986 52.811 36.274 1.00 47.13  ? 223 GLU A CA  1 
ATOM   1747 C C   . GLU A 1 226 ? 29.811 52.895 35.306 1.00 39.25  ? 223 GLU A C   1 
ATOM   1748 O O   . GLU A 1 226 ? 29.030 53.842 35.378 1.00 39.14  ? 223 GLU A O   1 
ATOM   1749 C CB  . GLU A 1 226 ? 32.227 53.525 35.736 1.00 50.54  ? 223 GLU A CB  1 
ATOM   1750 C CG  . GLU A 1 226 ? 33.311 53.701 36.788 1.00 58.88  ? 223 GLU A CG  1 
ATOM   1751 C CD  . GLU A 1 226 ? 34.575 54.396 36.310 1.00 69.77  ? 223 GLU A CD  1 
ATOM   1752 O OE1 . GLU A 1 226 ? 35.481 54.589 37.142 1.00 83.45  ? 223 GLU A OE1 1 
ATOM   1753 O OE2 . GLU A 1 226 ? 34.656 54.731 35.109 1.00 70.56  ? 223 GLU A OE2 1 
ATOM   1754 N N   . ALA A 1 227 ? 29.694 51.911 34.409 1.00 38.14  ? 224 ALA A N   1 
ATOM   1755 C CA  . ALA A 1 227 ? 28.593 51.899 33.455 1.00 37.16  ? 224 ALA A CA  1 
ATOM   1756 C C   . ALA A 1 227 ? 27.280 51.610 34.189 1.00 35.47  ? 224 ALA A C   1 
ATOM   1757 O O   . ALA A 1 227 ? 26.271 52.248 33.915 1.00 32.92  ? 224 ALA A O   1 
ATOM   1758 C CB  . ALA A 1 227 ? 28.856 50.903 32.345 1.00 36.19  ? 224 ALA A CB  1 
ATOM   1759 N N   . ASP A 1 228 ? 27.278 50.612 35.078 1.00 34.85  ? 225 ASP A N   1 
ATOM   1760 C CA  . ASP A 1 228 ? 26.087 50.307 35.861 1.00 35.07  ? 225 ASP A CA  1 
ATOM   1761 C C   . ASP A 1 228 ? 25.657 51.519 36.677 1.00 37.39  ? 225 ASP A C   1 
ATOM   1762 O O   . ASP A 1 228 ? 24.464 51.786 36.804 1.00 36.27  ? 225 ASP A O   1 
ATOM   1763 C CB  . ASP A 1 228 ? 26.290 49.105 36.781 1.00 34.16  ? 225 ASP A CB  1 
ATOM   1764 C CG  . ASP A 1 228 ? 26.137 47.753 36.113 1.00 35.60  ? 225 ASP A CG  1 
ATOM   1765 O OD1 . ASP A 1 228 ? 25.584 47.708 34.994 1.00 34.33  ? 225 ASP A OD1 1 
ATOM   1766 O OD2 . ASP A 1 228 ? 26.605 46.764 36.705 1.00 35.71  ? 225 ASP A OD2 1 
ATOM   1767 N N   . ILE A 1 229 ? 26.634 52.207 37.277 1.00 36.97  ? 226 ILE A N   1 
ATOM   1768 C CA  . ILE A 1 229 ? 26.336 53.380 38.074 1.00 38.27  ? 226 ILE A CA  1 
ATOM   1769 C C   . ILE A 1 229 ? 25.616 54.423 37.230 1.00 37.16  ? 226 ILE A C   1 
ATOM   1770 O O   . ILE A 1 229 ? 24.574 54.927 37.638 1.00 37.76  ? 226 ILE A O   1 
ATOM   1771 C CB  . ILE A 1 229 ? 27.611 53.919 38.751 1.00 42.61  ? 226 ILE A CB  1 
ATOM   1772 C CG1 . ILE A 1 229 ? 28.041 52.962 39.865 1.00 41.24  ? 226 ILE A CG1 1 
ATOM   1773 C CG2 . ILE A 1 229 ? 27.385 55.320 39.291 1.00 43.34  ? 226 ILE A CG2 1 
ATOM   1774 C CD1 . ILE A 1 229 ? 29.295 53.346 40.571 1.00 45.99  ? 226 ILE A CD1 1 
ATOM   1775 N N   . LYS A 1 230 ? 26.144 54.711 36.040 1.00 39.81  ? 227 LYS A N   1 
ATOM   1776 C CA  . LYS A 1 230 ? 25.524 55.720 35.203 1.00 39.58  ? 227 LYS A CA  1 
ATOM   1777 C C   . LYS A 1 230 ? 24.122 55.279 34.793 1.00 37.77  ? 227 LYS A C   1 
ATOM   1778 O O   . LYS A 1 230 ? 23.201 56.084 34.789 1.00 41.80  ? 227 LYS A O   1 
ATOM   1779 C CB  . LYS A 1 230 ? 26.395 56.032 33.988 1.00 39.64  ? 227 LYS A CB  1 
ATOM   1780 C CG  . LYS A 1 230 ? 25.839 57.132 33.094 1.00 46.21  ? 227 LYS A CG  1 
ATOM   1781 C CD  . LYS A 1 230 ? 25.567 58.421 33.853 1.00 49.95  ? 227 LYS A CD  1 
ATOM   1782 C CE  . LYS A 1 230 ? 26.793 58.980 34.539 1.00 52.96  ? 227 LYS A CE  1 
ATOM   1783 N NZ  . LYS A 1 230 ? 26.450 60.172 35.351 1.00 56.64  ? 227 LYS A NZ  1 
ATOM   1784 N N   . LEU A 1 231 ? 23.964 54.002 34.431 1.00 35.44  ? 228 LEU A N   1 
ATOM   1785 C CA  . LEU A 1 231 ? 22.663 53.494 34.025 1.00 35.22  ? 228 LEU A CA  1 
ATOM   1786 C C   . LEU A 1 231 ? 21.649 53.618 35.161 1.00 35.62  ? 228 LEU A C   1 
ATOM   1787 O O   . LEU A 1 231 ? 20.500 53.978 34.924 1.00 35.64  ? 228 LEU A O   1 
ATOM   1788 C CB  . LEU A 1 231 ? 22.853 52.044 33.570 1.00 35.17  ? 228 LEU A CB  1 
ATOM   1789 C CG  . LEU A 1 231 ? 23.593 51.885 32.241 1.00 34.34  ? 228 LEU A CG  1 
ATOM   1790 C CD1 . LEU A 1 231 ? 23.845 50.423 31.936 1.00 36.28  ? 228 LEU A CD1 1 
ATOM   1791 C CD2 . LEU A 1 231 ? 22.782 52.491 31.103 1.00 39.06  ? 228 LEU A CD2 1 
ATOM   1792 N N   . MET A 1 232 ? 22.103 53.382 36.395 1.00 35.68  ? 229 MET A N   1 
ATOM   1793 C CA  . MET A 1 232 ? 21.218 53.448 37.548 1.00 34.17  ? 229 MET A CA  1 
ATOM   1794 C C   . MET A 1 232 ? 20.814 54.913 37.781 1.00 36.34  ? 229 MET A C   1 
ATOM   1795 O O   . MET A 1 232 ? 19.653 55.191 38.064 1.00 39.33  ? 229 MET A O   1 
ATOM   1796 C CB  . MET A 1 232 ? 21.926 52.878 38.783 1.00 34.11  ? 229 MET A CB  1 
ATOM   1797 C CG  . MET A 1 232 ? 21.162 53.029 40.077 1.00 35.23  ? 229 MET A CG  1 
ATOM   1798 S SD  . MET A 1 232 ? 19.700 51.946 40.060 1.00 34.07  ? 229 MET A SD  1 
ATOM   1799 C CE  . MET A 1 232 ? 18.578 52.862 41.114 1.00 35.97  ? 229 MET A CE  1 
ATOM   1800 N N   . GLU A 1 233 ? 21.765 55.852 37.633 1.00 36.21  ? 230 GLU A N   1 
ATOM   1801 C CA  . GLU A 1 233 ? 21.503 57.277 37.827 1.00 37.36  ? 230 GLU A CA  1 
ATOM   1802 C C   . GLU A 1 233 ? 20.485 57.791 36.809 1.00 39.70  ? 230 GLU A C   1 
ATOM   1803 O O   . GLU A 1 233 ? 19.718 58.709 37.103 1.00 40.57  ? 230 GLU A O   1 
ATOM   1804 C CB  . GLU A 1 233 ? 22.815 58.066 37.740 1.00 40.18  ? 230 GLU A CB  1 
ATOM   1805 C CG  . GLU A 1 233 ? 23.747 57.834 38.916 1.00 42.17  ? 230 GLU A CG  1 
ATOM   1806 C CD  . GLU A 1 233 ? 25.163 58.356 38.761 1.00 43.19  ? 230 GLU A CD  1 
ATOM   1807 O OE1 . GLU A 1 233 ? 25.536 58.749 37.636 1.00 44.66  ? 230 GLU A OE1 1 
ATOM   1808 O OE2 . GLU A 1 233 ? 25.873 58.416 39.776 1.00 45.95  ? 230 GLU A OE2 1 
ATOM   1809 N N   . LEU A 1 234 ? 20.499 57.200 35.603 1.00 41.92  ? 231 LEU A N   1 
ATOM   1810 C CA  . LEU A 1 234 ? 19.585 57.563 34.531 1.00 41.56  ? 231 LEU A CA  1 
ATOM   1811 C C   . LEU A 1 234 ? 18.223 56.896 34.730 1.00 40.98  ? 231 LEU A C   1 
ATOM   1812 O O   . LEU A 1 234 ? 17.260 57.246 34.054 1.00 41.55  ? 231 LEU A O   1 
ATOM   1813 C CB  . LEU A 1 234 ? 20.214 57.114 33.206 1.00 44.03  ? 231 LEU A CB  1 
ATOM   1814 C CG  . LEU A 1 234 ? 21.516 57.812 32.810 1.00 45.55  ? 231 LEU A CG  1 
ATOM   1815 C CD1 . LEU A 1 234 ? 21.994 57.340 31.447 1.00 46.50  ? 231 LEU A CD1 1 
ATOM   1816 C CD2 . LEU A 1 234 ? 21.336 59.321 32.794 1.00 54.07  ? 231 LEU A CD2 1 
ATOM   1817 N N   . GLY A 1 235 ? 18.143 55.949 35.673 1.00 37.69  ? 232 GLY A N   1 
ATOM   1818 C CA  . GLY A 1 235 ? 16.909 55.226 35.924 1.00 38.50  ? 232 GLY A CA  1 
ATOM   1819 C C   . GLY A 1 235 ? 16.689 54.128 34.881 1.00 36.45  ? 232 GLY A C   1 
ATOM   1820 O O   . GLY A 1 235 ? 15.581 53.621 34.737 1.00 38.13  ? 232 GLY A O   1 
ATOM   1821 N N   . TYR A 1 236 ? 17.768 53.732 34.197 1.00 37.69  ? 233 TYR A N   1 
ATOM   1822 C CA  . TYR A 1 236 ? 17.693 52.726 33.145 1.00 35.04  ? 233 TYR A CA  1 
ATOM   1823 C C   . TYR A 1 236 ? 18.110 51.326 33.589 1.00 38.63  ? 233 TYR A C   1 
ATOM   1824 O O   . TYR A 1 236 ? 17.931 50.387 32.815 1.00 37.92  ? 233 TYR A O   1 
ATOM   1825 C CB  . TYR A 1 236 ? 18.591 53.131 31.975 1.00 36.76  ? 233 TYR A CB  1 
ATOM   1826 C CG  . TYR A 1 236 ? 18.137 54.325 31.176 1.00 39.74  ? 233 TYR A CG  1 
ATOM   1827 C CD1 . TYR A 1 236 ? 16.867 54.866 31.303 1.00 40.57  ? 233 TYR A CD1 1 
ATOM   1828 C CD2 . TYR A 1 236 ? 19.032 54.971 30.337 1.00 40.09  ? 233 TYR A CD2 1 
ATOM   1829 C CE1 . TYR A 1 236 ? 16.476 55.967 30.554 1.00 44.34  ? 233 TYR A CE1 1 
ATOM   1830 C CE2 . TYR A 1 236 ? 18.663 56.080 29.598 1.00 42.14  ? 233 TYR A CE2 1 
ATOM   1831 C CZ  . TYR A 1 236 ? 17.382 56.581 29.706 1.00 43.22  ? 233 TYR A CZ  1 
ATOM   1832 O OH  . TYR A 1 236 ? 17.044 57.682 28.964 1.00 48.64  ? 233 TYR A OH  1 
ATOM   1833 N N   . LEU A 1 237 ? 18.692 51.181 34.789 1.00 32.81  ? 234 LEU A N   1 
ATOM   1834 C CA  . LEU A 1 237 ? 19.128 49.866 35.233 1.00 33.43  ? 234 LEU A CA  1 
ATOM   1835 C C   . LEU A 1 237 ? 17.920 49.179 35.867 1.00 33.75  ? 234 LEU A C   1 
ATOM   1836 O O   . LEU A 1 237 ? 17.394 49.623 36.887 1.00 33.98  ? 234 LEU A O   1 
ATOM   1837 C CB  . LEU A 1 237 ? 20.304 50.020 36.204 1.00 33.05  ? 234 LEU A CB  1 
ATOM   1838 C CG  . LEU A 1 237 ? 21.063 48.736 36.527 1.00 33.13  ? 234 LEU A CG  1 
ATOM   1839 C CD1 . LEU A 1 237 ? 21.896 48.308 35.329 1.00 33.43  ? 234 LEU A CD1 1 
ATOM   1840 C CD2 . LEU A 1 237 ? 21.963 48.906 37.741 1.00 36.24  ? 234 LEU A CD2 1 
ATOM   1841 N N   . PRO A 1 238 ? 17.395 48.084 35.271 1.00 34.25  ? 235 PRO A N   1 
ATOM   1842 C CA  . PRO A 1 238 ? 16.193 47.457 35.804 1.00 34.56  ? 235 PRO A CA  1 
ATOM   1843 C C   . PRO A 1 238 ? 16.399 46.663 37.085 1.00 32.80  ? 235 PRO A C   1 
ATOM   1844 O O   . PRO A 1 238 ? 17.481 46.153 37.358 1.00 31.98  ? 235 PRO A O   1 
ATOM   1845 C CB  . PRO A 1 238 ? 15.751 46.471 34.702 1.00 36.71  ? 235 PRO A CB  1 
ATOM   1846 C CG  . PRO A 1 238 ? 16.611 46.804 33.507 1.00 36.29  ? 235 PRO A CG  1 
ATOM   1847 C CD  . PRO A 1 238 ? 17.883 47.401 34.063 1.00 34.33  ? 235 PRO A CD  1 
ATOM   1848 N N   . PRO A 1 239 ? 15.349 46.538 37.913 1.00 33.74  ? 236 PRO A N   1 
ATOM   1849 C CA  . PRO A 1 239 ? 15.441 45.719 39.118 1.00 35.31  ? 236 PRO A CA  1 
ATOM   1850 C C   . PRO A 1 239 ? 15.546 44.254 38.702 1.00 36.25  ? 236 PRO A C   1 
ATOM   1851 O O   . PRO A 1 239 ? 15.135 43.898 37.597 1.00 37.75  ? 236 PRO A O   1 
ATOM   1852 C CB  . PRO A 1 239 ? 14.122 46.004 39.843 1.00 40.69  ? 236 PRO A CB  1 
ATOM   1853 C CG  . PRO A 1 239 ? 13.173 46.447 38.748 1.00 45.06  ? 236 PRO A CG  1 
ATOM   1854 C CD  . PRO A 1 239 ? 14.040 47.178 37.742 1.00 38.03  ? 236 PRO A CD  1 
ATOM   1855 N N   . LEU A 1 240 ? 16.125 43.422 39.572 1.00 37.44  ? 237 LEU A N   1 
ATOM   1856 C CA  . LEU A 1 240 ? 16.186 41.985 39.336 1.00 44.43  ? 237 LEU A CA  1 
ATOM   1857 C C   . LEU A 1 240 ? 14.781 41.392 39.289 1.00 46.68  ? 237 LEU A C   1 
ATOM   1858 O O   . LEU A 1 240 ? 14.527 40.462 38.532 1.00 55.71  ? 237 LEU A O   1 
ATOM   1859 C CB  . LEU A 1 240 ? 16.981 41.316 40.459 1.00 45.41  ? 237 LEU A CB  1 
ATOM   1860 C CG  . LEU A 1 240 ? 18.492 41.470 40.393 1.00 41.52  ? 237 LEU A CG  1 
ATOM   1861 C CD1 . LEU A 1 240 ? 19.162 40.653 41.480 1.00 47.56  ? 237 LEU A CD1 1 
ATOM   1862 C CD2 . LEU A 1 240 ? 18.998 41.011 39.029 1.00 43.08  ? 237 LEU A CD2 1 
ATOM   1863 N N   . ARG A 1 241 ? 13.884 41.935 40.116 1.00 56.99  ? 238 ARG A N   1 
ATOM   1864 C CA  . ARG A 1 241 ? 12.519 41.444 40.220 1.00 61.81  ? 238 ARG A CA  1 
ATOM   1865 C C   . ARG A 1 241 ? 11.574 42.363 39.436 1.00 67.28  ? 238 ARG A C   1 
ATOM   1866 O O   . ARG A 1 241 ? 11.172 43.401 40.014 1.00 69.28  ? 238 ARG A O   1 
ATOM   1867 C CB  . ARG A 1 241 ? 12.164 41.378 41.705 1.00 69.26  ? 238 ARG A CB  1 
ATOM   1868 C CG  . ARG A 1 241 ? 13.071 40.464 42.519 1.00 65.75  ? 238 ARG A CG  1 
ATOM   1869 C CD  . ARG A 1 241 ? 12.771 40.604 43.999 1.00 68.78  ? 238 ARG A CD  1 
ATOM   1870 N NE  . ARG A 1 241 ? 11.377 40.312 44.295 1.00 60.16  ? 238 ARG A NE  1 
ATOM   1871 C CZ  . ARG A 1 241 ? 10.504 41.201 44.764 1.00 66.58  ? 238 ARG A CZ  1 
ATOM   1872 N NH1 . ARG A 1 241 ? 9.260  40.838 45.021 1.00 70.28  ? 238 ARG A NH1 1 
ATOM   1873 N NH2 . ARG A 1 241 ? 10.880 42.451 44.980 1.00 55.45  ? 238 ARG A NH2 1 
HETATM 1874 N N1  . EPE B 2 .   ? 29.908 31.046 43.454 1.00 91.32  ? 301 EPE A N1  1 
HETATM 1875 C C2  . EPE B 2 .   ? 29.571 31.799 42.233 1.00 81.66  ? 301 EPE A C2  1 
HETATM 1876 C C3  . EPE B 2 .   ? 30.802 32.359 41.563 1.00 77.19  ? 301 EPE A C3  1 
HETATM 1877 N N4  . EPE B 2 .   ? 31.719 31.271 41.217 1.00 89.29  ? 301 EPE A N4  1 
HETATM 1878 C C5  . EPE B 2 .   ? 32.138 30.627 42.467 1.00 92.75  ? 301 EPE A C5  1 
HETATM 1879 C C6  . EPE B 2 .   ? 30.939 30.027 43.161 1.00 93.36  ? 301 EPE A C6  1 
HETATM 1880 C C7  . EPE B 2 .   ? 32.849 31.737 40.405 1.00 86.64  ? 301 EPE A C7  1 
HETATM 1881 C C8  . EPE B 2 .   ? 32.615 31.624 38.916 1.00 77.04  ? 301 EPE A C8  1 
HETATM 1882 O O8  . EPE B 2 .   ? 33.572 30.786 38.303 1.00 63.51  ? 301 EPE A O8  1 
HETATM 1883 C C9  . EPE B 2 .   ? 28.695 30.470 44.089 1.00 95.99  ? 301 EPE A C9  1 
HETATM 1884 C C10 . EPE B 2 .   ? 28.333 29.039 43.689 1.00 104.85 ? 301 EPE A C10 1 
HETATM 1885 S S   . EPE B 2 .   ? 27.610 28.875 42.076 1.00 106.69 ? 301 EPE A S   1 
HETATM 1886 O O1S . EPE B 2 .   ? 26.911 30.097 41.804 1.00 102.55 ? 301 EPE A O1S 1 
HETATM 1887 O O2S . EPE B 2 .   ? 26.861 27.651 42.078 1.00 105.24 ? 301 EPE A O2S 1 
HETATM 1888 O O3S . EPE B 2 .   ? 28.830 28.717 41.140 1.00 90.70  ? 301 EPE A O3S 1 
HETATM 1889 P P   . PO4 C 3 .   ? 23.515 31.143 39.364 1.00 62.83  ? 302 PO4 A P   1 
HETATM 1890 O O1  . PO4 C 3 .   ? 24.108 32.088 38.341 1.00 59.55  ? 302 PO4 A O1  1 
HETATM 1891 O O2  . PO4 C 3 .   ? 22.159 31.676 39.799 1.00 59.55  ? 302 PO4 A O2  1 
HETATM 1892 O O3  . PO4 C 3 .   ? 23.354 29.754 38.733 1.00 58.45  ? 302 PO4 A O3  1 
HETATM 1893 O O4  . PO4 C 3 .   ? 24.435 31.037 40.569 1.00 70.47  ? 302 PO4 A O4  1 
HETATM 1894 P P   . PO4 D 3 .   ? 34.461 27.523 30.148 1.00 95.18  ? 303 PO4 A P   1 
HETATM 1895 O O1  . PO4 D 3 .   ? 35.305 28.780 30.000 1.00 87.72  ? 303 PO4 A O1  1 
HETATM 1896 O O2  . PO4 D 3 .   ? 32.973 27.885 30.109 1.00 63.55  ? 303 PO4 A O2  1 
HETATM 1897 O O3  . PO4 D 3 .   ? 34.784 26.571 29.004 1.00 94.65  ? 303 PO4 A O3  1 
HETATM 1898 O O4  . PO4 D 3 .   ? 34.785 26.854 31.478 1.00 90.06  ? 303 PO4 A O4  1 
HETATM 1899 C C1  . EDO E 4 .   ? 18.031 56.992 17.872 1.00 79.90  ? 304 EDO A C1  1 
HETATM 1900 O O1  . EDO E 4 .   ? 18.404 56.376 16.651 1.00 70.07  ? 304 EDO A O1  1 
HETATM 1901 C C2  . EDO E 4 .   ? 16.877 56.331 18.536 1.00 76.38  ? 304 EDO A C2  1 
HETATM 1902 O O2  . EDO E 4 .   ? 16.262 55.342 17.732 1.00 70.47  ? 304 EDO A O2  1 
HETATM 1903 C C   . CO3 F 5 .   ? 36.190 35.342 12.016 1.00 69.21  ? 305 CO3 A C   1 
HETATM 1904 O O1  . CO3 F 5 .   ? 37.244 34.647 11.838 1.00 64.23  ? 305 CO3 A O1  1 
HETATM 1905 O O2  . CO3 F 5 .   ? 35.633 35.913 11.022 1.00 62.25  ? 305 CO3 A O2  1 
HETATM 1906 O O3  . CO3 F 5 .   ? 35.695 35.472 13.192 1.00 49.61  ? 305 CO3 A O3  1 
HETATM 1907 O O   . HOH G 6 .   ? 46.689 47.796 25.355 1.00 59.30  ? 401 HOH A O   1 
HETATM 1908 O O   . HOH G 6 .   ? 23.871 32.653 36.074 0.50 41.58  ? 402 HOH A O   1 
HETATM 1909 O O   . HOH G 6 .   ? 23.514 34.323 39.008 1.00 48.46  ? 403 HOH A O   1 
HETATM 1910 O O   . HOH G 6 .   ? 34.856 31.494 36.370 1.00 54.32  ? 404 HOH A O   1 
HETATM 1911 O O   . HOH G 6 .   ? 12.965 30.599 33.769 1.00 59.61  ? 405 HOH A O   1 
HETATM 1912 O O   . HOH G 6 .   ? 30.613 29.605 10.606 1.00 40.20  ? 406 HOH A O   1 
HETATM 1913 O O   . HOH G 6 .   ? 37.480 36.754 30.625 1.00 48.20  ? 407 HOH A O   1 
HETATM 1914 O O   . HOH G 6 .   ? 34.943 19.029 18.781 1.00 51.71  ? 408 HOH A O   1 
HETATM 1915 O O   A HOH G 6 .   ? 16.566 46.605 47.753 0.60 37.66  ? 409 HOH A O   1 
HETATM 1916 O O   B HOH G 6 .   ? 15.694 45.111 47.567 0.40 31.46  ? 409 HOH A O   1 
HETATM 1917 O O   . HOH G 6 .   ? 26.268 62.502 33.188 1.00 62.09  ? 410 HOH A O   1 
HETATM 1918 O O   . HOH G 6 .   ? 21.557 39.353 12.263 1.00 43.59  ? 411 HOH A O   1 
HETATM 1919 O O   . HOH G 6 .   ? 39.454 46.937 36.560 1.00 78.41  ? 412 HOH A O   1 
HETATM 1920 O O   . HOH G 6 .   ? 10.912 39.397 14.418 1.00 50.66  ? 413 HOH A O   1 
HETATM 1921 O O   . HOH G 6 .   ? 5.294  40.916 20.072 1.00 46.12  ? 414 HOH A O   1 
HETATM 1922 O O   . HOH G 6 .   ? 19.100 54.306 20.102 1.00 49.06  ? 415 HOH A O   1 
HETATM 1923 O O   . HOH G 6 .   ? 12.993 51.617 26.284 1.00 56.38  ? 416 HOH A O   1 
HETATM 1924 O O   . HOH G 6 .   ? 28.373 46.839 38.590 1.00 34.21  ? 417 HOH A O   1 
HETATM 1925 O O   . HOH G 6 .   ? 27.573 42.155 35.412 1.00 42.33  ? 418 HOH A O   1 
HETATM 1926 O O   . HOH G 6 .   ? 23.231 26.449 10.680 0.50 31.90  ? 419 HOH A O   1 
HETATM 1927 O O   . HOH G 6 .   ? 3.610  23.325 37.672 1.00 51.02  ? 420 HOH A O   1 
HETATM 1928 O O   . HOH G 6 .   ? 38.787 42.931 24.888 1.00 56.52  ? 421 HOH A O   1 
HETATM 1929 O O   . HOH G 6 .   ? 14.744 56.836 33.519 1.00 49.47  ? 422 HOH A O   1 
HETATM 1930 O O   . HOH G 6 .   ? 30.270 57.130 33.453 1.00 57.76  ? 423 HOH A O   1 
HETATM 1931 O O   . HOH G 6 .   ? 27.073 37.617 46.251 1.00 50.70  ? 424 HOH A O   1 
HETATM 1932 O O   . HOH G 6 .   ? 31.320 33.181 8.212  1.00 47.36  ? 425 HOH A O   1 
HETATM 1933 O O   . HOH G 6 .   ? 19.897 60.058 39.356 1.00 42.76  ? 426 HOH A O   1 
HETATM 1934 O O   . HOH G 6 .   ? 11.262 47.288 19.605 0.50 44.70  ? 427 HOH A O   1 
HETATM 1935 O O   A HOH G 6 .   ? 9.004  45.068 30.207 0.50 35.97  ? 428 HOH A O   1 
HETATM 1936 O O   B HOH G 6 .   ? 9.936  46.581 30.329 0.50 49.59  ? 428 HOH A O   1 
HETATM 1937 O O   . HOH G 6 .   ? 39.910 47.716 39.116 1.00 77.09  ? 429 HOH A O   1 
HETATM 1938 O O   . HOH G 6 .   ? 19.692 5.671  22.938 1.00 55.37  ? 430 HOH A O   1 
HETATM 1939 O O   . HOH G 6 .   ? 28.108 23.059 9.317  1.00 41.08  ? 431 HOH A O   1 
HETATM 1940 O O   . HOH G 6 .   ? 24.192 32.283 30.425 1.00 36.72  ? 432 HOH A O   1 
HETATM 1941 O O   . HOH G 6 .   ? 28.478 58.911 40.011 1.00 51.89  ? 433 HOH A O   1 
HETATM 1942 O O   . HOH G 6 .   ? 23.135 27.667 13.305 1.00 48.38  ? 434 HOH A O   1 
HETATM 1943 O O   . HOH G 6 .   ? 21.524 36.001 36.132 1.00 60.56  ? 435 HOH A O   1 
HETATM 1944 O O   A HOH G 6 .   ? 22.418 20.733 26.938 0.50 48.94  ? 436 HOH A O   1 
HETATM 1945 O O   . HOH G 6 .   ? 27.738 23.068 16.442 1.00 40.36  ? 437 HOH A O   1 
HETATM 1946 O O   . HOH G 6 .   ? 14.285 46.368 21.928 0.50 36.38  ? 438 HOH A O   1 
HETATM 1947 O O   . HOH G 6 .   ? 32.773 34.297 10.166 1.00 60.28  ? 439 HOH A O   1 
HETATM 1948 O O   . HOH G 6 .   ? 16.147 49.989 30.819 1.00 37.83  ? 440 HOH A O   1 
HETATM 1949 O O   . HOH G 6 .   ? 22.821 55.186 21.517 1.00 46.95  ? 441 HOH A O   1 
HETATM 1950 O O   A HOH G 6 .   ? 14.782 56.571 26.013 0.50 36.54  ? 442 HOH A O   1 
HETATM 1951 O O   B HOH G 6 .   ? 14.085 55.687 24.654 0.50 42.02  ? 442 HOH A O   1 
HETATM 1952 O O   . HOH G 6 .   ? 6.250  36.112 27.593 1.00 46.96  ? 443 HOH A O   1 
HETATM 1953 O O   . HOH G 6 .   ? 16.188 19.257 23.684 1.00 46.50  ? 444 HOH A O   1 
HETATM 1954 O O   . HOH G 6 .   ? 22.216 14.365 12.977 1.00 34.43  ? 445 HOH A O   1 
HETATM 1955 O O   . HOH G 6 .   ? 0.042  39.582 26.219 1.00 53.64  ? 446 HOH A O   1 
HETATM 1956 O O   . HOH G 6 .   ? 29.664 56.377 36.117 1.00 49.36  ? 447 HOH A O   1 
HETATM 1957 O O   . HOH G 6 .   ? 32.094 35.960 14.123 1.00 32.20  ? 448 HOH A O   1 
HETATM 1958 O O   . HOH G 6 .   ? 31.051 24.457 7.773  1.00 41.04  ? 449 HOH A O   1 
HETATM 1959 O O   . HOH G 6 .   ? 28.909 22.761 14.365 1.00 54.42  ? 450 HOH A O   1 
HETATM 1960 O O   . HOH G 6 .   ? 15.061 43.802 42.673 1.00 42.25  ? 451 HOH A O   1 
HETATM 1961 O O   . HOH G 6 .   ? 13.735 48.890 22.579 1.00 47.80  ? 452 HOH A O   1 
HETATM 1962 O O   . HOH G 6 .   ? 5.476  29.343 35.084 1.00 68.68  ? 453 HOH A O   1 
HETATM 1963 O O   . HOH G 6 .   ? 35.442 35.663 16.439 1.00 32.68  ? 454 HOH A O   1 
HETATM 1964 O O   . HOH G 6 .   ? 14.010 51.530 31.182 1.00 49.10  ? 455 HOH A O   1 
HETATM 1965 O O   . HOH G 6 .   ? 11.762 39.484 30.816 1.00 35.29  ? 456 HOH A O   1 
HETATM 1966 O O   . HOH G 6 .   ? 14.866 47.602 30.447 1.00 37.82  ? 457 HOH A O   1 
HETATM 1967 O O   . HOH G 6 .   ? 26.666 53.928 17.040 1.00 50.93  ? 458 HOH A O   1 
HETATM 1968 O O   . HOH G 6 .   ? 19.273 15.014 18.924 1.00 39.50  ? 459 HOH A O   1 
HETATM 1969 O O   . HOH G 6 .   ? 29.349 25.648 27.966 1.00 42.25  ? 460 HOH A O   1 
HETATM 1970 O O   . HOH G 6 .   ? 41.166 39.372 17.662 1.00 50.18  ? 461 HOH A O   1 
HETATM 1971 O O   . HOH G 6 .   ? 23.814 39.175 13.655 1.00 32.96  ? 462 HOH A O   1 
HETATM 1972 O O   . HOH G 6 .   ? 2.407  39.493 30.363 1.00 55.62  ? 463 HOH A O   1 
HETATM 1973 O O   . HOH G 6 .   ? 17.665 52.351 37.500 1.00 33.17  ? 464 HOH A O   1 
HETATM 1974 O O   . HOH G 6 .   ? 14.895 9.679  18.821 1.00 62.24  ? 465 HOH A O   1 
HETATM 1975 O O   . HOH G 6 .   ? 30.956 53.653 18.641 1.00 53.83  ? 466 HOH A O   1 
HETATM 1976 O O   . HOH G 6 .   ? 4.283  39.662 33.797 1.00 60.00  ? 467 HOH A O   1 
HETATM 1977 O O   . HOH G 6 .   ? 26.903 21.394 25.369 1.00 50.68  ? 468 HOH A O   1 
HETATM 1978 O O   . HOH G 6 .   ? 12.887 44.070 35.865 1.00 49.94  ? 469 HOH A O   1 
HETATM 1979 O O   . HOH G 6 .   ? 38.248 45.775 40.581 1.00 60.03  ? 470 HOH A O   1 
HETATM 1980 O O   . HOH G 6 .   ? 33.365 33.835 36.261 1.00 35.41  ? 471 HOH A O   1 
HETATM 1981 O O   . HOH G 6 .   ? 24.065 16.403 12.336 1.00 32.86  ? 472 HOH A O   1 
HETATM 1982 O O   . HOH G 6 .   ? 38.427 28.504 16.982 1.00 55.86  ? 473 HOH A O   1 
HETATM 1983 O O   . HOH G 6 .   ? 19.860 39.636 35.509 1.00 39.52  ? 474 HOH A O   1 
HETATM 1984 O O   . HOH G 6 .   ? 15.075 50.732 34.659 0.50 45.71  ? 475 HOH A O   1 
HETATM 1985 O O   . HOH G 6 .   ? 31.191 55.290 21.867 1.00 52.04  ? 476 HOH A O   1 
HETATM 1986 O O   . HOH G 6 .   ? 30.446 38.013 47.752 1.00 58.10  ? 477 HOH A O   1 
HETATM 1987 O O   . HOH G 6 .   ? 14.533 43.664 32.258 1.00 56.10  ? 478 HOH A O   1 
HETATM 1988 O O   . HOH G 6 .   ? 20.017 44.772 15.239 1.00 47.34  ? 479 HOH A O   1 
HETATM 1989 O O   A HOH G 6 .   ? 25.010 46.697 39.246 0.50 28.01  ? 480 HOH A O   1 
HETATM 1990 O O   B HOH G 6 .   ? 23.811 45.207 39.592 0.50 28.21  ? 480 HOH A O   1 
HETATM 1991 O O   . HOH G 6 .   ? 35.717 49.094 21.940 1.00 45.36  ? 481 HOH A O   1 
HETATM 1992 O O   . HOH G 6 .   ? 35.741 48.650 24.656 1.00 44.66  ? 482 HOH A O   1 
HETATM 1993 O O   . HOH G 6 .   ? 27.956 31.077 34.137 1.00 50.61  ? 483 HOH A O   1 
HETATM 1994 O O   . HOH G 6 .   ? 4.133  25.236 34.094 1.00 64.87  ? 484 HOH A O   1 
HETATM 1995 O O   . HOH G 6 .   ? 21.540 41.496 34.221 1.00 33.08  ? 485 HOH A O   1 
HETATM 1996 O O   . HOH G 6 .   ? 21.132 59.027 27.721 0.50 39.90  ? 486 HOH A O   1 
HETATM 1997 O O   . HOH G 6 .   ? 32.560 36.630 11.594 1.00 42.34  ? 487 HOH A O   1 
HETATM 1998 O O   . HOH G 6 .   ? 19.902 5.533  20.336 1.00 52.97  ? 488 HOH A O   1 
HETATM 1999 O O   . HOH G 6 .   ? 19.761 15.035 11.646 1.00 44.72  ? 489 HOH A O   1 
HETATM 2000 O O   . HOH G 6 .   ? 17.219 33.803 7.963  1.00 65.41  ? 490 HOH A O   1 
HETATM 2001 O O   A HOH G 6 .   ? 37.358 56.998 31.876 0.50 42.33  ? 491 HOH A O   1 
HETATM 2002 O O   B HOH G 6 .   ? 36.801 58.346 31.250 0.50 44.46  ? 491 HOH A O   1 
HETATM 2003 O O   . HOH G 6 .   ? 1.531  35.702 34.818 1.00 47.52  ? 492 HOH A O   1 
HETATM 2004 O O   . HOH G 6 .   ? 32.878 30.988 10.941 1.00 47.63  ? 493 HOH A O   1 
HETATM 2005 O O   . HOH G 6 .   ? 12.353 42.005 31.774 1.00 42.93  ? 494 HOH A O   1 
HETATM 2006 O O   . HOH G 6 .   ? 22.767 13.846 9.961  0.50 35.55  ? 495 HOH A O   1 
HETATM 2007 O O   . HOH G 6 .   ? 38.130 40.693 23.471 1.00 50.78  ? 496 HOH A O   1 
HETATM 2008 O O   . HOH G 6 .   ? 17.505 45.748 15.126 1.00 53.70  ? 497 HOH A O   1 
HETATM 2009 O O   A HOH G 6 .   ? 7.712  37.403 12.679 0.50 46.50  ? 498 HOH A O   1 
HETATM 2010 O O   B HOH G 6 .   ? 7.013  37.386 14.269 0.50 46.84  ? 498 HOH A O   1 
HETATM 2011 O O   . HOH G 6 .   ? 40.011 44.864 37.563 1.00 71.57  ? 499 HOH A O   1 
HETATM 2012 O O   . HOH G 6 .   ? 34.220 29.785 9.355  1.00 57.74  ? 500 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ALA A 7   ? 0.8726 1.3124 1.4657 -0.0477 -0.2508 -0.2548 4   ALA A N   
2    C CA  . ALA A 7   ? 0.8886 1.3169 1.4686 -0.0653 -0.2133 -0.2329 4   ALA A CA  
3    C C   . ALA A 7   ? 0.8761 1.2936 1.4138 -0.0455 -0.1968 -0.2201 4   ALA A C   
4    O O   . ALA A 7   ? 0.9441 1.3957 1.5079 -0.0360 -0.1915 -0.2220 4   ALA A O   
5    C CB  . ALA A 7   ? 0.8678 1.3397 1.5173 -0.0917 -0.1941 -0.2322 4   ALA A CB  
6    N N   . LYS A 8   ? 0.8480 1.2178 1.3209 -0.0390 -0.1892 -0.2076 5   LYS A N   
7    C CA  . LYS A 8   ? 0.8481 1.2020 1.2783 -0.0230 -0.1735 -0.1953 5   LYS A CA  
8    C C   . LYS A 8   ? 0.8160 1.1257 1.1943 -0.0291 -0.1579 -0.1802 5   LYS A C   
9    O O   . LYS A 8   ? 0.7677 1.0461 1.1163 -0.0278 -0.1702 -0.1826 5   LYS A O   
10   C CB  . LYS A 8   ? 0.9416 1.2874 1.3438 0.0071  -0.1953 -0.2053 5   LYS A CB  
11   C CG  . LYS A 8   ? 0.9738 1.2998 1.3303 0.0238  -0.1802 -0.1938 5   LYS A CG  
12   C CD  . LYS A 8   ? 1.0798 1.3945 1.4063 0.0545  -0.2010 -0.2038 5   LYS A CD  
13   C CE  . LYS A 8   ? 1.0854 1.4479 1.4642 0.0646  -0.2177 -0.2198 5   LYS A CE  
14   N NZ  . LYS A 8   ? 1.1334 1.4803 1.4763 0.0979  -0.2391 -0.2299 5   LYS A NZ  
15   N N   . ALA A 9   ? 0.7158 1.0240 1.0841 -0.0346 -0.1313 -0.1653 6   ALA A N   
16   C CA  . ALA A 9   ? 0.7629 1.0363 1.0899 -0.0410 -0.1156 -0.1517 6   ALA A CA  
17   C C   . ALA A 9   ? 0.7423 0.9787 1.0123 -0.0222 -0.1230 -0.1502 6   ALA A C   
18   O O   . ALA A 9   ? 0.6938 0.9289 0.9500 -0.0029 -0.1346 -0.1563 6   ALA A O   
19   C CB  . ALA A 9   ? 0.7830 1.0652 1.1143 -0.0487 -0.0888 -0.1387 6   ALA A CB  
20   N N   . PHE A 10  ? 0.6907 0.8961 0.9273 -0.0275 -0.1159 -0.1425 7   PHE A N   
21   C CA  . PHE A 10  ? 0.6736 0.8433 0.8571 -0.0126 -0.1169 -0.1389 7   PHE A CA  
22   C C   . PHE A 10  ? 0.5981 0.7647 0.7645 -0.0101 -0.0968 -0.1279 7   PHE A C   
23   O O   . PHE A 10  ? 0.5318 0.7084 0.7116 -0.0232 -0.0795 -0.1195 7   PHE A O   
24   C CB  . PHE A 10  ? 0.6981 0.8396 0.8559 -0.0184 -0.1156 -0.1352 7   PHE A CB  
25   C CG  . PHE A 10  ? 0.7735 0.9071 0.9352 -0.0176 -0.1376 -0.1464 7   PHE A CG  
26   C CD1 . PHE A 10  ? 0.8793 0.9976 1.0191 0.0015  -0.1587 -0.1566 7   PHE A CD1 
27   C CD2 . PHE A 10  ? 0.7783 0.9165 0.9629 -0.0352 -0.1382 -0.1474 7   PHE A CD2 
28   C CE1 . PHE A 10  ? 0.9190 1.0276 1.0603 0.0033  -0.1815 -0.1682 7   PHE A CE1 
29   C CE2 . PHE A 10  ? 0.8237 0.9517 1.0107 -0.0350 -0.1599 -0.1585 7   PHE A CE2 
30   C CZ  . PHE A 10  ? 0.9144 1.0286 1.0807 -0.0157 -0.1824 -0.1694 7   PHE A CZ  
31   N N   . ARG A 11  ? 0.5934 0.7426 0.7275 0.0075  -0.1001 -0.1286 8   ARG A N   
32   C CA  . ARG A 11  ? 0.5453 0.6871 0.6604 0.0100  -0.0830 -0.1195 8   ARG A CA  
33   C C   . ARG A 11  ? 0.4832 0.6023 0.5726 0.0014  -0.0675 -0.1095 8   ARG A C   
34   O O   . ARG A 11  ? 0.5009 0.6293 0.6013 -0.0099 -0.0524 -0.1022 8   ARG A O   
35   C CB  . ARG A 11  ? 0.6878 0.8112 0.7707 0.0313  -0.0906 -0.1230 8   ARG A CB  
36   C CG  . ARG A 11  ? 0.8070 0.9567 0.9152 0.0427  -0.1030 -0.1322 8   ARG A CG  
37   C CD  . ARG A 11  ? 0.8770 1.0528 1.0115 0.0355  -0.0876 -0.1265 8   ARG A CD  
38   N NE  . ARG A 11  ? 1.0396 1.2420 1.1975 0.0487  -0.0972 -0.1348 8   ARG A NE  
39   C CZ  . ARG A 11  ? 1.0858 1.3295 1.2944 0.0409  -0.0947 -0.1378 8   ARG A CZ  
40   N NH1 . ARG A 11  ? 1.0776 1.3464 1.3065 0.0555  -0.1034 -0.1461 8   ARG A NH1 
41   N NH2 . ARG A 11  ? 1.1258 1.3847 1.3633 0.0195  -0.0825 -0.1324 8   ARG A NH2 
42   N N   . ARG A 12  ? 0.4349 0.5252 0.4911 0.0079  -0.0717 -0.1100 9   ARG A N   
43   C CA  . ARG A 12  ? 0.4591 0.5304 0.4924 0.0017  -0.0561 -0.1014 9   ARG A CA  
44   C C   . ARG A 12  ? 0.3992 0.4764 0.4471 -0.0111 -0.0541 -0.0998 9   ARG A C   
45   O O   . ARG A 12  ? 0.4232 0.4974 0.4745 -0.0101 -0.0673 -0.1058 9   ARG A O   
46   C CB  . ARG A 12  ? 0.5198 0.5555 0.5082 0.0151  -0.0570 -0.1013 9   ARG A CB  
47   C CG  . ARG A 12  ? 0.6448 0.6628 0.6058 0.0299  -0.0574 -0.1018 9   ARG A CG  
48   C CD  . ARG A 12  ? 0.7551 0.7324 0.6674 0.0430  -0.0561 -0.1010 9   ARG A CD  
49   N NE  . ARG A 12  ? 0.8507 0.8148 0.7491 0.0337  -0.0364 -0.0924 9   ARG A NE  
50   C CZ  . ARG A 12  ? 0.9006 0.8311 0.7597 0.0418  -0.0291 -0.0896 9   ARG A CZ  
51   N NH1 . ARG A 12  ? 0.9272 0.8295 0.7519 0.0608  -0.0413 -0.0947 9   ARG A NH1 
52   N NH2 . ARG A 12  ? 0.9154 0.8412 0.7702 0.0320  -0.0099 -0.0825 9   ARG A NH2 
53   N N   . TYR A 13  ? 0.4015 0.4840 0.4546 -0.0219 -0.0384 -0.0924 10  TYR A N   
54   C CA  . TYR A 13  ? 0.3907 0.4744 0.4504 -0.0318 -0.0345 -0.0900 10  TYR A CA  
55   C C   . TYR A 13  ? 0.4516 0.5231 0.4914 -0.0326 -0.0209 -0.0841 10  TYR A C   
56   O O   . TYR A 13  ? 0.4680 0.5377 0.5003 -0.0321 -0.0109 -0.0805 10  TYR A O   
57   C CB  . TYR A 13  ? 0.3712 0.4763 0.4614 -0.0443 -0.0295 -0.0879 10  TYR A CB  
58   C CG  . TYR A 13  ? 0.3547 0.4734 0.4717 -0.0496 -0.0401 -0.0934 10  TYR A CG  
59   C CD1 . TYR A 13  ? 0.4004 0.5327 0.5340 -0.0448 -0.0501 -0.0996 10  TYR A CD1 
60   C CD2 . TYR A 13  ? 0.3777 0.4945 0.5034 -0.0594 -0.0407 -0.0933 10  TYR A CD2 
61   C CE1 . TYR A 13  ? 0.3980 0.5464 0.5626 -0.0517 -0.0597 -0.1059 10  TYR A CE1 
62   C CE2 . TYR A 13  ? 0.4009 0.5283 0.5530 -0.0672 -0.0493 -0.0986 10  TYR A CE2 
63   C CZ  . TYR A 13  ? 0.3967 0.5420 0.5713 -0.0643 -0.0587 -0.1053 10  TYR A CZ  
64   O OH  . TYR A 13  ? 0.4559 0.6153 0.6627 -0.0739 -0.0671 -0.1118 10  TYR A OH  
65   N N   . ILE A 14  ? 0.3954 0.4587 0.4279 -0.0338 -0.0213 -0.0841 11  ILE A N   
66   C CA  . ILE A 14  ? 0.3967 0.4544 0.4174 -0.0349 -0.0091 -0.0798 11  ILE A CA  
67   C C   . ILE A 14  ? 0.3936 0.4664 0.4338 -0.0446 -0.0049 -0.0778 11  ILE A C   
68   O O   . ILE A 14  ? 0.3929 0.4685 0.4439 -0.0486 -0.0119 -0.0796 11  ILE A O   
69   C CB  . ILE A 14  ? 0.3996 0.4379 0.3969 -0.0268 -0.0117 -0.0813 11  ILE A CB  
70   C CG1 . ILE A 14  ? 0.4458 0.4629 0.4169 -0.0146 -0.0164 -0.0835 11  ILE A CG1 
71   C CG2 . ILE A 14  ? 0.4309 0.4700 0.4229 -0.0280 0.0018  -0.0777 11  ILE A CG2 
72   C CD1 . ILE A 14  ? 0.5014 0.4954 0.4456 -0.0041 -0.0213 -0.0856 11  ILE A CD1 
73   N N   . PHE A 15  ? 0.3781 0.4581 0.4212 -0.0480 0.0061  -0.0745 12  PHE A N   
74   C CA  . PHE A 15  ? 0.3788 0.4692 0.4344 -0.0539 0.0093  -0.0731 12  PHE A CA  
75   C C   . PHE A 15  ? 0.3623 0.4545 0.4127 -0.0526 0.0174  -0.0726 12  PHE A C   
76   O O   . PHE A 15  ? 0.3774 0.4745 0.4302 -0.0545 0.0244  -0.0719 12  PHE A O   
77   C CB  . PHE A 15  ? 0.3885 0.4902 0.4583 -0.0588 0.0120  -0.0714 12  PHE A CB  
78   C CG  . PHE A 15  ? 0.3585 0.4654 0.4364 -0.0630 0.0144  -0.0698 12  PHE A CG  
79   C CD1 . PHE A 15  ? 0.3968 0.4977 0.4693 -0.0625 0.0128  -0.0703 12  PHE A CD1 
80   C CD2 . PHE A 15  ? 0.4201 0.5341 0.5068 -0.0657 0.0183  -0.0677 12  PHE A CD2 
81   C CE1 . PHE A 15  ? 0.4263 0.5260 0.5001 -0.0647 0.0151  -0.0687 12  PHE A CE1 
82   C CE2 . PHE A 15  ? 0.4866 0.5999 0.5748 -0.0678 0.0216  -0.0657 12  PHE A CE2 
83   C CZ  . PHE A 15  ? 0.4377 0.5428 0.5185 -0.0672 0.0200  -0.0662 12  PHE A CZ  
84   N N   . GLU A 16  ? 0.3629 0.4508 0.4066 -0.0490 0.0161  -0.0738 13  GLU A N   
85   C CA  . GLU A 16  ? 0.3587 0.4523 0.4012 -0.0463 0.0237  -0.0746 13  GLU A CA  
86   C C   . GLU A 16  ? 0.3817 0.4779 0.4245 -0.0432 0.0208  -0.0762 13  GLU A C   
87   O O   . GLU A 16  ? 0.3373 0.4217 0.3712 -0.0409 0.0139  -0.0764 13  GLU A O   
88   C CB  . GLU A 16  ? 0.4670 0.5496 0.4935 -0.0394 0.0275  -0.0747 13  GLU A CB  
89   C CG  . GLU A 16  ? 0.6495 0.7220 0.6663 -0.0389 0.0315  -0.0731 13  GLU A CG  
90   C CD  . GLU A 16  ? 0.7793 0.8371 0.7754 -0.0306 0.0385  -0.0725 13  GLU A CD  
91   O OE1 . GLU A 16  ? 0.8373 0.9039 0.8382 -0.0305 0.0501  -0.0724 13  GLU A OE1 
92   O OE2 . GLU A 16  ? 0.9553 0.9934 0.9311 -0.0234 0.0324  -0.0728 13  GLU A OE2 
93   N N   . LEU A 17  ? 0.3691 0.4792 0.4211 -0.0426 0.0254  -0.0781 14  LEU A N   
94   C CA  . LEU A 17  ? 0.3785 0.4907 0.4278 -0.0361 0.0222  -0.0808 14  LEU A CA  
95   C C   . LEU A 17  ? 0.3610 0.4873 0.4166 -0.0308 0.0287  -0.0842 14  LEU A C   
96   O O   . LEU A 17  ? 0.3797 0.5193 0.4493 -0.0359 0.0361  -0.0851 14  LEU A O   
97   C CB  . LEU A 17  ? 0.4371 0.5531 0.4918 -0.0378 0.0188  -0.0814 14  LEU A CB  
98   C CG  . LEU A 17  ? 0.4858 0.5895 0.5369 -0.0437 0.0159  -0.0774 14  LEU A CG  
99   C CD1 . LEU A 17  ? 0.4719 0.5832 0.5341 -0.0507 0.0193  -0.0756 14  LEU A CD1 
100  C CD2 . LEU A 17  ? 0.5939 0.6879 0.6360 -0.0407 0.0128  -0.0772 14  LEU A CD2 
101  N N   . TYR A 18  ? 0.3672 0.4891 0.4119 -0.0207 0.0267  -0.0862 15  TYR A N   
102  C CA  . TYR A 18  ? 0.3795 0.5166 0.4309 -0.0134 0.0339  -0.0897 15  TYR A CA  
103  C C   . TYR A 18  ? 0.3686 0.5197 0.4273 -0.0051 0.0285  -0.0956 15  TYR A C   
104  O O   . TYR A 18  ? 0.3889 0.5255 0.4325 0.0000  0.0194  -0.0956 15  TYR A O   
105  C CB  . TYR A 18  ? 0.4088 0.5300 0.4391 -0.0038 0.0359  -0.0883 15  TYR A CB  
106  C CG  . TYR A 18  ? 0.4302 0.5340 0.4477 -0.0077 0.0392  -0.0838 15  TYR A CG  
107  C CD1 . TYR A 18  ? 0.4622 0.5467 0.4682 -0.0119 0.0295  -0.0815 15  TYR A CD1 
108  C CD2 . TYR A 18  ? 0.4794 0.5878 0.4993 -0.0081 0.0528  -0.0825 15  TYR A CD2 
109  C CE1 . TYR A 18  ? 0.4981 0.5675 0.4922 -0.0131 0.0301  -0.0791 15  TYR A CE1 
110  C CE2 . TYR A 18  ? 0.5529 0.6414 0.5559 -0.0093 0.0555  -0.0787 15  TYR A CE2 
111  C CZ  . TYR A 18  ? 0.5476 0.6170 0.5373 -0.0107 0.0427  -0.0776 15  TYR A CZ  
112  O OH  . TYR A 18  ? 0.6789 0.7289 0.6509 -0.0091 0.0432  -0.0754 15  TYR A OH  
113  N N   . PHE A 19  ? 0.3436 0.5216 0.4249 -0.0035 0.0348  -0.1009 16  PHE A N   
114  C CA  . PHE A 19  ? 0.3695 0.5661 0.4620 0.0061  0.0283  -0.1087 16  PHE A CA  
115  C C   . PHE A 19  ? 0.3943 0.6076 0.4932 0.0182  0.0345  -0.1132 16  PHE A C   
116  O O   . PHE A 19  ? 0.4192 0.6385 0.5248 0.0149  0.0480  -0.1108 16  PHE A O   
117  C CB  . PHE A 19  ? 0.3453 0.5660 0.4671 -0.0028 0.0281  -0.1140 16  PHE A CB  
118  C CG  . PHE A 19  ? 0.3442 0.5504 0.4607 -0.0139 0.0242  -0.1097 16  PHE A CG  
119  C CD1 . PHE A 19  ? 0.3755 0.5615 0.4715 -0.0097 0.0144  -0.1076 16  PHE A CD1 
120  C CD2 . PHE A 19  ? 0.3427 0.5528 0.4722 -0.0279 0.0320  -0.1072 16  PHE A CD2 
121  C CE1 . PHE A 19  ? 0.3850 0.5591 0.4768 -0.0189 0.0130  -0.1032 16  PHE A CE1 
122  C CE2 . PHE A 19  ? 0.3594 0.5560 0.4823 -0.0358 0.0286  -0.1033 16  PHE A CE2 
123  C CZ  . PHE A 19  ? 0.3594 0.5399 0.4649 -0.0311 0.0195  -0.1014 16  PHE A CZ  
124  N N   A ASP A 20  ? 0.3932 0.6118 0.4873 0.0339  0.0253  -0.1195 17  ASP A N   
125  N N   B ASP A 20  ? 0.4126 0.6313 0.5067 0.0339  0.0254  -0.1195 17  ASP A N   
126  C CA  A ASP A 20  ? 0.4109 0.6494 0.5130 0.0485  0.0302  -0.1251 17  ASP A CA  
127  C CA  B ASP A 20  ? 0.4444 0.6827 0.5463 0.0485  0.0303  -0.1251 17  ASP A CA  
128  C C   A ASP A 20  ? 0.4036 0.6826 0.5498 0.0399  0.0412  -0.1308 17  ASP A C   
129  C C   B ASP A 20  ? 0.4229 0.7022 0.5692 0.0402  0.0411  -0.1309 17  ASP A C   
130  O O   A ASP A 20  ? 0.3933 0.6935 0.5646 0.0352  0.0342  -0.1379 17  ASP A O   
131  O O   B ASP A 20  ? 0.4149 0.7159 0.5863 0.0362  0.0339  -0.1383 17  ASP A O   
132  C CB  A ASP A 20  ? 0.4173 0.6560 0.5078 0.0680  0.0162  -0.1325 17  ASP A CB  
133  C CB  B ASP A 20  ? 0.4795 0.7142 0.5660 0.0684  0.0162  -0.1317 17  ASP A CB  
134  C CG  A ASP A 20  ? 0.4249 0.6854 0.5231 0.0861  0.0207  -0.1390 17  ASP A CG  
135  C CG  B ASP A 20  ? 0.5165 0.7745 0.6120 0.0867  0.0201  -0.1387 17  ASP A CG  
136  O OD1 A ASP A 20  ? 0.4176 0.6594 0.4919 0.0937  0.0271  -0.1340 17  ASP A OD1 
137  O OD1 B ASP A 20  ? 0.5149 0.7955 0.6333 0.0825  0.0357  -0.1385 17  ASP A OD1 
138  O OD2 A ASP A 20  ? 0.3971 0.6949 0.5275 0.0922  0.0182  -0.1495 17  ASP A OD2 
139  O OD2 B ASP A 20  ? 0.5574 0.8078 0.6338 0.1061  0.0086  -0.1439 17  ASP A OD2 
140  N N   . PRO A 21  ? 0.4143 0.7026 0.5701 0.0369  0.0591  -0.1279 18  PRO A N   
141  C CA  . PRO A 21  ? 0.3964 0.7209 0.5952 0.0256  0.0730  -0.1325 18  PRO A CA  
142  C C   . PRO A 21  ? 0.4011 0.7698 0.6397 0.0327  0.0674  -0.1462 18  PRO A C   
143  O O   . PRO A 21  ? 0.4065 0.7996 0.6801 0.0196  0.0661  -0.1526 18  PRO A O   
144  C CB  . PRO A 21  ? 0.4461 0.7666 0.6377 0.0282  0.0943  -0.1266 18  PRO A CB  
145  C CG  . PRO A 21  ? 0.4924 0.7669 0.6344 0.0343  0.0894  -0.1171 18  PRO A CG  
146  C CD  . PRO A 21  ? 0.4707 0.7316 0.5939 0.0440  0.0674  -0.1200 18  PRO A CD  
147  N N   . ALA A 22  ? 0.3853 0.7627 0.6170 0.0544  0.0625  -0.1515 19  ALA A N   
148  C CA  . ALA A 22  ? 0.4317 0.8537 0.7011 0.0656  0.0557  -0.1661 19  ALA A CA  
149  C C   . ALA A 22  ? 0.4317 0.8570 0.7070 0.0661  0.0328  -0.1746 19  ALA A C   
150  O O   . ALA A 22  ? 0.4604 0.9237 0.7793 0.0610  0.0284  -0.1864 19  ALA A O   
151  C CB  . ALA A 22  ? 0.4297 0.8527 0.6809 0.0920  0.0540  -0.1690 19  ALA A CB  
152  N N   . ARG A 23  ? 0.4033 0.7875 0.6340 0.0723  0.0186  -0.1690 20  ARG A N   
153  C CA  . ARG A 23  ? 0.4374 0.8159 0.6631 0.0756  -0.0016 -0.1755 20  ARG A CA  
154  C C   . ARG A 23  ? 0.4252 0.8069 0.6711 0.0527  -0.0006 -0.1745 20  ARG A C   
155  O O   . ARG A 23  ? 0.4195 0.8200 0.6870 0.0530  -0.0136 -0.1853 20  ARG A O   
156  C CB  . ARG A 23  ? 0.4985 0.8281 0.6691 0.0866  -0.0120 -0.1679 20  ARG A CB  
157  C CG  . ARG A 23  ? 0.5724 0.8923 0.7165 0.1115  -0.0168 -0.1704 20  ARG A CG  
158  C CD  . ARG A 23  ? 0.6544 0.9201 0.7434 0.1165  -0.0234 -0.1609 20  ARG A CD  
159  N NE  . ARG A 23  ? 0.7016 0.9474 0.7736 0.1173  -0.0371 -0.1624 20  ARG A NE  
160  C CZ  . ARG A 23  ? 0.7793 0.9784 0.8071 0.1188  -0.0415 -0.1544 20  ARG A CZ  
161  N NH1 . ARG A 23  ? 0.8524 1.0211 0.8516 0.1176  -0.0353 -0.1453 20  ARG A NH1 
162  N NH2 . ARG A 23  ? 0.8266 1.0082 0.8388 0.1208  -0.0515 -0.1557 20  ARG A NH2 
163  N N   . LEU A 24  ? 0.4294 0.7907 0.6659 0.0344  0.0133  -0.1622 21  LEU A N   
164  C CA  . LEU A 24  ? 0.4201 0.7794 0.6699 0.0143  0.0143  -0.1605 21  LEU A CA  
165  C C   . LEU A 24  ? 0.4078 0.8090 0.7094 0.0022  0.0214  -0.1703 21  LEU A C   
166  O O   . LEU A 24  ? 0.4234 0.8321 0.7433 -0.0086 0.0140  -0.1760 21  LEU A O   
167  C CB  . LEU A 24  ? 0.4414 0.7687 0.6667 0.0009  0.0270  -0.1459 21  LEU A CB  
168  C CG  . LEU A 24  ? 0.4680 0.7849 0.6969 -0.0170 0.0272  -0.1426 21  LEU A CG  
169  C CD1 . LEU A 24  ? 0.4998 0.7941 0.7042 -0.0117 0.0110  -0.1419 21  LEU A CD1 
170  C CD2 . LEU A 24  ? 0.4708 0.7654 0.6844 -0.0293 0.0422  -0.1305 21  LEU A CD2 
171  N N   . LEU A 25  ? 0.4230 0.8510 0.7486 0.0044  0.0359  -0.1727 22  LEU A N   
172  C CA  . LEU A 25  ? 0.4392 0.9083 0.8181 -0.0094 0.0467  -0.1814 22  LEU A CA  
173  C C   . LEU A 25  ? 0.4414 0.9482 0.8574 -0.0022 0.0274  -0.1998 22  LEU A C   
174  O O   . LEU A 25  ? 0.4554 0.9933 0.9175 -0.0177 0.0301  -0.2091 22  LEU A O   
175  C CB  . LEU A 25  ? 0.4568 0.9429 0.8484 -0.0067 0.0697  -0.1783 22  LEU A CB  
176  C CG  . LEU A 25  ? 0.4642 0.9946 0.9139 -0.0220 0.0867  -0.1864 22  LEU A CG  
177  C CD1 . LEU A 25  ? 0.4893 1.0020 0.9424 -0.0491 0.1018  -0.1786 22  LEU A CD1 
178  C CD2 . LEU A 25  ? 0.4967 1.0475 0.9575 -0.0121 0.1079  -0.1849 22  LEU A CD2 
179  N N   . GLU A 26  ? 0.4644 0.9666 0.8592 0.0214  0.0072  -0.2057 23  GLU A N   
180  C CA  . GLU A 26  ? 0.4883 1.0218 0.9107 0.0336  -0.0149 -0.2243 23  GLU A CA  
181  C C   . GLU A 26  ? 0.4736 1.0014 0.9047 0.0199  -0.0289 -0.2299 23  GLU A C   
182  O O   . GLU A 26  ? 0.4636 1.0264 0.9355 0.0198  -0.0425 -0.2469 23  GLU A O   
183  C CB  . GLU A 26  ? 0.5315 1.0449 0.9127 0.0632  -0.0336 -0.2266 23  GLU A CB  
184  C CG  . GLU A 26  ? 0.6304 1.1464 0.9982 0.0807  -0.0237 -0.2229 23  GLU A CG  
185  C CD  . GLU A 26  ? 0.6949 1.1821 1.0144 0.1091  -0.0412 -0.2238 23  GLU A CD  
186  O OE1 . GLU A 26  ? 0.7381 1.2030 1.0338 0.1160  -0.0604 -0.2272 23  GLU A OE1 
187  O OE2 . GLU A 26  ? 0.8427 1.3249 1.1440 0.1247  -0.0346 -0.2204 23  GLU A OE2 
188  N N   . LEU A 27  ? 0.4662 0.9501 0.8592 0.0094  -0.0265 -0.2164 24  LEU A N   
189  C CA  . LEU A 27  ? 0.4786 0.9501 0.8710 -0.0010 -0.0392 -0.2201 24  LEU A CA  
190  C C   . LEU A 27  ? 0.4774 0.9761 0.9186 -0.0260 -0.0302 -0.2264 24  LEU A C   
191  O O   . LEU A 27  ? 0.4481 0.9566 0.9079 -0.0414 -0.0069 -0.2197 24  LEU A O   
192  C CB  . LEU A 27  ? 0.4674 0.8878 0.8089 -0.0059 -0.0345 -0.2030 24  LEU A CB  
193  C CG  . LEU A 27  ? 0.5128 0.8997 0.8043 0.0151  -0.0451 -0.1973 24  LEU A CG  
194  C CD1 . LEU A 27  ? 0.5573 0.9441 0.8360 0.0275  -0.0363 -0.1920 24  LEU A CD1 
195  C CD2 . LEU A 27  ? 0.5793 0.9230 0.8322 0.0067  -0.0410 -0.1830 24  LEU A CD2 
196  N N   . ASP A 28  ? 0.4360 0.9429 0.8945 -0.0293 -0.0492 -0.2396 25  ASP A N   
197  C CA  . ASP A 28  ? 0.4449 0.9711 0.9464 -0.0545 -0.0438 -0.2466 25  ASP A CA  
198  C C   . ASP A 28  ? 0.4840 0.9647 0.9495 -0.0689 -0.0388 -0.2334 25  ASP A C   
199  O O   . ASP A 28  ? 0.4337 0.8762 0.8488 -0.0583 -0.0403 -0.2209 25  ASP A O   
200  C CB  . ASP A 28  ? 0.4814 1.0439 1.0253 -0.0502 -0.0684 -0.2702 25  ASP A CB  
201  C CG  . ASP A 28  ? 0.5206 1.0559 1.0299 -0.0341 -0.0975 -0.2769 25  ASP A CG  
202  O OD1 . ASP A 28  ? 0.5079 0.9960 0.9622 -0.0292 -0.0963 -0.2622 25  ASP A OD1 
203  O OD2 . ASP A 28  ? 0.5378 1.0997 1.0754 -0.0255 -0.1213 -0.2973 25  ASP A OD2 
204  N N   . ASP A 29  ? 0.4795 0.9639 0.9711 -0.0926 -0.0329 -0.2368 26  ASP A N   
205  C CA  . ASP A 29  ? 0.5077 0.9499 0.9665 -0.1059 -0.0273 -0.2251 26  ASP A CA  
206  C C   . ASP A 29  ? 0.5538 0.9646 0.9724 -0.0915 -0.0499 -0.2260 26  ASP A C   
207  O O   . ASP A 29  ? 0.4786 0.8509 0.8533 -0.0899 -0.0443 -0.2114 26  ASP A O   
208  C CB  . ASP A 29  ? 0.5290 0.9793 1.0229 -0.1333 -0.0183 -0.2306 26  ASP A CB  
209  C CG  . ASP A 29  ? 0.5930 1.0613 1.1154 -0.1502 0.0111  -0.2248 26  ASP A CG  
210  O OD1 . ASP A 29  ? 0.6276 1.1000 1.1389 -0.1391 0.0240  -0.2159 26  ASP A OD1 
211  O OD2 . ASP A 29  ? 0.6417 1.1178 1.1959 -0.1739 0.0213  -0.2296 26  ASP A OD2 
212  N N   A ASP A 30  ? 0.5283 0.9551 0.9614 -0.0803 -0.0751 -0.2434 27  ASP A N   
213  N N   B ASP A 30  ? 0.5399 0.9673 0.9735 -0.0803 -0.0750 -0.2435 27  ASP A N   
214  C CA  A ASP A 30  ? 0.5730 0.9672 0.9646 -0.0646 -0.0960 -0.2448 27  ASP A CA  
215  C CA  B ASP A 30  ? 0.5944 0.9896 0.9869 -0.0644 -0.0962 -0.2451 27  ASP A CA  
216  C C   A ASP A 30  ? 0.5103 0.8769 0.8523 -0.0443 -0.0933 -0.2310 27  ASP A C   
217  C C   B ASP A 30  ? 0.5185 0.8852 0.8608 -0.0447 -0.0929 -0.2309 27  ASP A C   
218  O O   A ASP A 30  ? 0.5239 0.8519 0.8224 -0.0391 -0.0949 -0.2214 27  ASP A O   
219  O O   B ASP A 30  ? 0.5272 0.8552 0.8263 -0.0403 -0.0938 -0.2209 27  ASP A O   
220  C CB  A ASP A 30  ? 0.5804 0.9959 0.9943 -0.0531 -0.1251 -0.2674 27  ASP A CB  
221  C CB  B ASP A 30  ? 0.6213 1.0386 1.0345 -0.0505 -0.1254 -0.2675 27  ASP A CB  
222  C CG  A ASP A 30  ? 0.6050 1.0420 1.0661 -0.0757 -0.1301 -0.2818 27  ASP A CG  
223  C CG  B ASP A 30  ? 0.6951 1.0734 1.0591 -0.0316 -0.1465 -0.2689 27  ASP A CG  
224  O OD1 A ASP A 30  ? 0.6133 1.0451 1.0860 -0.1003 -0.1087 -0.2727 27  ASP A OD1 
225  O OD1 B ASP A 30  ? 0.7149 1.0639 1.0594 -0.0415 -0.1466 -0.2646 27  ASP A OD1 
226  O OD2 A ASP A 30  ? 0.6407 1.0966 1.1246 -0.0682 -0.1558 -0.3023 27  ASP A OD2 
227  O OD2 B ASP A 30  ? 0.7183 1.0925 1.0597 -0.0058 -0.1614 -0.2735 27  ASP A OD2 
228  N N   . GLN A 31  ? 0.5105 0.8966 0.8597 -0.0330 -0.0886 -0.2305 28  GLN A N   
229  C CA  . GLN A 31  ? 0.5232 0.8829 0.8275 -0.0154 -0.0857 -0.2183 28  GLN A CA  
230  C C   . GLN A 31  ? 0.4644 0.7961 0.7434 -0.0278 -0.0642 -0.1984 28  GLN A C   
231  O O   . GLN A 31  ? 0.5077 0.8052 0.7448 -0.0197 -0.0644 -0.1880 28  GLN A O   
232  C CB  . GLN A 31  ? 0.5637 0.9502 0.8821 -0.0004 -0.0865 -0.2238 28  GLN A CB  
233  C CG  . GLN A 31  ? 0.6532 1.0620 0.9865 0.0189  -0.1118 -0.2438 28  GLN A CG  
234  C CD  . GLN A 31  ? 0.7070 1.1449 1.0562 0.0346  -0.1117 -0.2498 28  GLN A CD  
235  O OE1 . GLN A 31  ? 0.6540 1.1292 1.0467 0.0239  -0.0987 -0.2527 28  GLN A OE1 
236  N NE2 . GLN A 31  ? 0.7829 1.2020 1.0949 0.0613  -0.1258 -0.2518 28  GLN A NE2 
237  N N   . HIS A 32  ? 0.4061 0.7515 0.7100 -0.0466 -0.0454 -0.1935 29  HIS A N   
238  C CA  . HIS A 32  ? 0.4171 0.7358 0.6967 -0.0566 -0.0275 -0.1764 29  HIS A CA  
239  C C   . HIS A 32  ? 0.4473 0.7353 0.7019 -0.0615 -0.0318 -0.1717 29  HIS A C   
240  O O   . HIS A 32  ? 0.4313 0.6912 0.6512 -0.0564 -0.0284 -0.1601 29  HIS A O   
241  C CB  . HIS A 32  ? 0.3875 0.7208 0.6932 -0.0746 -0.0069 -0.1727 29  HIS A CB  
242  C CG  . HIS A 32  ? 0.3766 0.7340 0.6991 -0.0689 0.0026  -0.1733 29  HIS A CG  
243  N ND1 . HIS A 32  ? 0.3538 0.6962 0.6474 -0.0562 0.0068  -0.1638 29  HIS A ND1 
244  C CD2 . HIS A 32  ? 0.3779 0.7714 0.7417 -0.0741 0.0102  -0.1818 29  HIS A CD2 
245  C CE1 . HIS A 32  ? 0.3726 0.7391 0.6855 -0.0519 0.0154  -0.1665 29  HIS A CE1 
246  N NE2 . HIS A 32  ? 0.3625 0.7620 0.7193 -0.0623 0.0186  -0.1772 29  HIS A NE2 
247  N N   . LEU A 33  ? 0.4378 0.7323 0.7114 -0.0708 -0.0401 -0.1819 30  LEU A N   
248  C CA  . LEU A 33  ? 0.4520 0.7171 0.7016 -0.0744 -0.0448 -0.1788 30  LEU A CA  
249  C C   . LEU A 33  ? 0.4633 0.7041 0.6743 -0.0544 -0.0576 -0.1766 30  LEU A C   
250  O O   . LEU A 33  ? 0.5181 0.7297 0.6981 -0.0533 -0.0535 -0.1666 30  LEU A O   
251  C CB  . LEU A 33  ? 0.4828 0.7597 0.7607 -0.0860 -0.0552 -0.1931 30  LEU A CB  
252  C CG  . LEU A 33  ? 0.5115 0.8067 0.8262 -0.1092 -0.0396 -0.1947 30  LEU A CG  
253  C CD1 . LEU A 33  ? 0.5753 0.8740 0.9130 -0.1229 -0.0505 -0.2082 30  LEU A CD1 
254  C CD2 . LEU A 33  ? 0.5406 0.8114 0.8330 -0.1191 -0.0179 -0.1777 30  LEU A CD2 
255  N N   . GLN A 34  ? 0.4550 0.7071 0.6669 -0.0376 -0.0719 -0.1860 31  GLN A N   
256  C CA  . GLN A 34  ? 0.5281 0.7525 0.6991 -0.0176 -0.0825 -0.1839 31  GLN A CA  
257  C C   . GLN A 34  ? 0.4731 0.6775 0.6155 -0.0139 -0.0676 -0.1673 31  GLN A C   
258  O O   . GLN A 34  ? 0.4964 0.6705 0.6037 -0.0068 -0.0661 -0.1590 31  GLN A O   
259  C CB  . GLN A 34  ? 0.6027 0.8406 0.7775 0.0015  -0.1019 -0.1984 31  GLN A CB  
260  C CG  . GLN A 34  ? 0.7807 0.9832 0.9069 0.0237  -0.1131 -0.1970 31  GLN A CG  
261  C CD  . GLN A 34  ? 0.8797 1.0916 1.0050 0.0455  -0.1351 -0.2131 31  GLN A CD  
262  O OE1 . GLN A 34  ? 0.9154 1.1503 1.0696 0.0457  -0.1523 -0.2303 31  GLN A OE1 
263  N NE2 . GLN A 34  ? 0.9351 1.1284 1.0272 0.0643  -0.1354 -0.2085 31  GLN A NE2 
264  N N   . ARG A 35  ? 0.4660 0.6872 0.6240 -0.0184 -0.0567 -0.1631 32  ARG A N   
265  C CA  . ARG A 35  ? 0.4452 0.6481 0.5789 -0.0161 -0.0445 -0.1491 32  ARG A CA  
266  C C   . ARG A 35  ? 0.4406 0.6266 0.5646 -0.0289 -0.0318 -0.1372 32  ARG A C   
267  O O   . ARG A 35  ? 0.4493 0.6125 0.5469 -0.0247 -0.0270 -0.1274 32  ARG A O   
268  C CB  . ARG A 35  ? 0.4572 0.6790 0.6061 -0.0156 -0.0378 -0.1486 32  ARG A CB  
269  C CG  . ARG A 35  ? 0.4926 0.7255 0.6418 0.0024  -0.0510 -0.1591 32  ARG A CG  
270  C CD  . ARG A 35  ? 0.5708 0.8154 0.7254 0.0065  -0.0440 -0.1570 32  ARG A CD  
271  N NE  . ARG A 35  ? 0.5502 0.8015 0.6993 0.0269  -0.0572 -0.1668 32  ARG A NE  
272  C CZ  . ARG A 35  ? 0.5959 0.8519 0.7412 0.0363  -0.0541 -0.1659 32  ARG A CZ  
273  N NH1 . ARG A 35  ? 0.5714 0.8244 0.7167 0.0267  -0.0388 -0.1558 32  ARG A NH1 
274  N NH2 . ARG A 35  ? 0.5606 0.8213 0.6983 0.0571  -0.0672 -0.1756 32  ARG A NH2 
275  N N   . ILE A 36  ? 0.3974 0.5940 0.5427 -0.0441 -0.0258 -0.1382 33  ILE A N   
276  C CA  . ILE A 36  ? 0.4264 0.6056 0.5598 -0.0536 -0.0154 -0.1280 33  ILE A CA  
277  C C   . ILE A 36  ? 0.4372 0.5938 0.5464 -0.0470 -0.0220 -0.1270 33  ILE A C   
278  O O   . ILE A 36  ? 0.4211 0.5600 0.5107 -0.0460 -0.0148 -0.1171 33  ILE A O   
279  C CB  . ILE A 36  ? 0.4342 0.6233 0.5895 -0.0700 -0.0070 -0.1293 33  ILE A CB  
280  C CG1 . ILE A 36  ? 0.4172 0.6227 0.5889 -0.0747 0.0039  -0.1271 33  ILE A CG1 
281  C CG2 . ILE A 36  ? 0.4773 0.6445 0.6153 -0.0763 0.0003  -0.1207 33  ILE A CG2 
282  C CD1 . ILE A 36  ? 0.4334 0.6258 0.5860 -0.0713 0.0124  -0.1157 33  ILE A CD1 
283  N N   . GLU A 37  ? 0.4569 0.6145 0.5675 -0.0413 -0.0362 -0.1381 34  GLU A N   
284  C CA  . GLU A 37  ? 0.5587 0.6917 0.6420 -0.0324 -0.0432 -0.1380 34  GLU A CA  
285  C C   . GLU A 37  ? 0.4958 0.6089 0.5481 -0.0186 -0.0395 -0.1292 34  GLU A C   
286  O O   . GLU A 37  ? 0.4925 0.5855 0.5233 -0.0168 -0.0319 -0.1202 34  GLU A O   
287  C CB  . GLU A 37  ? 0.6253 0.7639 0.7164 -0.0270 -0.0620 -0.1537 34  GLU A CB  
288  C CG  . GLU A 37  ? 0.7671 0.8769 0.8259 -0.0153 -0.0716 -0.1555 34  GLU A CG  
289  C CD  . GLU A 37  ? 0.8957 1.0096 0.9615 -0.0089 -0.0938 -0.1730 34  GLU A CD  
290  O OE1 . GLU A 37  ? 0.8111 0.9553 0.9133 -0.0153 -0.1013 -0.1845 34  GLU A OE1 
291  O OE2 . GLU A 37  ? 1.0479 1.1351 1.0829 0.0035  -0.1038 -0.1757 34  GLU A OE2 
292  N N   . ARG A 38  ? 0.4695 0.5880 0.5201 -0.0092 -0.0437 -0.1318 35  ARG A N   
293  C CA  . ARG A 38  ? 0.5110 0.6075 0.5313 0.0027  -0.0393 -0.1239 35  ARG A CA  
294  C C   . ARG A 38  ? 0.4634 0.5559 0.4831 -0.0069 -0.0223 -0.1102 35  ARG A C   
295  O O   . ARG A 38  ? 0.4883 0.5598 0.4852 -0.0027 -0.0143 -0.1015 35  ARG A O   
296  C CB  . ARG A 38  ? 0.5117 0.6145 0.5308 0.0142  -0.0475 -0.1302 35  ARG A CB  
297  C CG  . ARG A 38  ? 0.5946 0.7017 0.6129 0.0279  -0.0672 -0.1454 35  ARG A CG  
298  C CD  . ARG A 38  ? 0.6176 0.7377 0.6412 0.0387  -0.0746 -0.1522 35  ARG A CD  
299  N NE  . ARG A 38  ? 0.6983 0.7912 0.6872 0.0495  -0.0681 -0.1431 35  ARG A NE  
300  C CZ  . ARG A 38  ? 0.6865 0.7827 0.6717 0.0591  -0.0708 -0.1455 35  ARG A CZ  
301  N NH1 . ARG A 38  ? 0.6850 0.8150 0.7025 0.0593  -0.0786 -0.1561 35  ARG A NH1 
302  N NH2 . ARG A 38  ? 0.7044 0.7697 0.6544 0.0673  -0.0641 -0.1367 35  ARG A NH2 
303  N N   . PHE A 39  ? 0.4515 0.5641 0.4968 -0.0196 -0.0165 -0.1090 36  PHE A N   
304  C CA  . PHE A 39  ? 0.3982 0.5085 0.4447 -0.0277 -0.0038 -0.0984 36  PHE A CA  
305  C C   . PHE A 39  ? 0.3773 0.4773 0.4170 -0.0320 0.0027  -0.0923 36  PHE A C   
306  O O   . PHE A 39  ? 0.4134 0.5033 0.4435 -0.0318 0.0112  -0.0838 36  PHE A O   
307  C CB  . PHE A 39  ? 0.3750 0.5050 0.4447 -0.0372 -0.0004 -0.0995 36  PHE A CB  
308  C CG  . PHE A 39  ? 0.3501 0.4767 0.4197 -0.0437 0.0093  -0.0905 36  PHE A CG  
309  C CD1 . PHE A 39  ? 0.3645 0.4804 0.4222 -0.0401 0.0120  -0.0850 36  PHE A CD1 
310  C CD2 . PHE A 39  ? 0.3596 0.4911 0.4391 -0.0530 0.0150  -0.0881 36  PHE A CD2 
311  C CE1 . PHE A 39  ? 0.3569 0.4712 0.4176 -0.0464 0.0183  -0.0787 36  PHE A CE1 
312  C CE2 . PHE A 39  ? 0.3554 0.4834 0.4338 -0.0566 0.0210  -0.0815 36  PHE A CE2 
313  C CZ  . PHE A 39  ? 0.3414 0.4626 0.4126 -0.0536 0.0218  -0.0775 36  PHE A CZ  
314  N N   . LEU A 40  ? 0.4053 0.5081 0.4512 -0.0360 -0.0008 -0.0969 37  LEU A N   
315  C CA  . LEU A 40  ? 0.4241 0.5151 0.4599 -0.0374 0.0044  -0.0918 37  LEU A CA  
316  C C   . LEU A 40  ? 0.4386 0.5095 0.4485 -0.0252 0.0056  -0.0881 37  LEU A C   
317  O O   . LEU A 40  ? 0.4587 0.5218 0.4606 -0.0245 0.0152  -0.0802 37  LEU A O   
318  C CB  . LEU A 40  ? 0.4254 0.5178 0.4682 -0.0431 -0.0012 -0.0987 37  LEU A CB  
319  C CG  . LEU A 40  ? 0.4334 0.5416 0.4993 -0.0561 0.0017  -0.1011 37  LEU A CG  
320  C CD1 . LEU A 40  ? 0.4998 0.6029 0.5691 -0.0638 -0.0009 -0.1064 37  LEU A CD1 
321  C CD2 . LEU A 40  ? 0.4467 0.5563 0.5142 -0.0604 0.0126  -0.0922 37  LEU A CD2 
322  N N   . ASP A 41  ? 0.4692 0.5312 0.4651 -0.0145 -0.0035 -0.0939 38  ASP A N   
323  C CA  . ASP A 41  ? 0.5184 0.5556 0.4831 -0.0010 -0.0011 -0.0902 38  ASP A CA  
324  C C   . ASP A 41  ? 0.5533 0.5842 0.5118 -0.0011 0.0123  -0.0799 38  ASP A C   
325  O O   . ASP A 41  ? 0.5442 0.5579 0.4838 0.0042  0.0227  -0.0725 38  ASP A O   
326  C CB  . ASP A 41  ? 0.5922 0.6182 0.5394 0.0128  -0.0156 -0.0996 38  ASP A CB  
327  C CG  . ASP A 41  ? 0.6582 0.6850 0.6076 0.0149  -0.0307 -0.1111 38  ASP A CG  
328  O OD1 . ASP A 41  ? 0.6825 0.7130 0.6415 0.0058  -0.0283 -0.1105 38  ASP A OD1 
329  O OD2 . ASP A 41  ? 0.7898 0.8131 0.7315 0.0258  -0.0458 -0.1215 38  ASP A OD2 
330  N N   . ALA A 42  ? 0.4637 0.5078 0.4381 -0.0076 0.0126  -0.0797 39  ALA A N   
331  C CA  . ALA A 42  ? 0.5009 0.5383 0.4715 -0.0100 0.0237  -0.0714 39  ALA A CA  
332  C C   . ALA A 42  ? 0.4615 0.5093 0.4493 -0.0209 0.0349  -0.0642 39  ALA A C   
333  O O   . ALA A 42  ? 0.4815 0.5223 0.4666 -0.0231 0.0462  -0.0568 39  ALA A O   
334  C CB  . ALA A 42  ? 0.5432 0.5886 0.5220 -0.0117 0.0183  -0.0747 39  ALA A CB  
335  N N   . LEU A 43  ? 0.4502 0.5143 0.4560 -0.0276 0.0316  -0.0670 40  LEU A N   
336  C CA  . LEU A 43  ? 0.4189 0.4927 0.4392 -0.0350 0.0394  -0.0618 40  LEU A CA  
337  C C   . LEU A 43  ? 0.4211 0.4863 0.4307 -0.0295 0.0471  -0.0574 40  LEU A C   
338  O O   . LEU A 43  ? 0.3938 0.4647 0.4127 -0.0323 0.0568  -0.0518 40  LEU A O   
339  C CB  . LEU A 43  ? 0.3930 0.4807 0.4288 -0.0418 0.0339  -0.0661 40  LEU A CB  
340  C CG  . LEU A 43  ? 0.3833 0.4820 0.4322 -0.0476 0.0298  -0.0691 40  LEU A CG  
341  C CD1 . LEU A 43  ? 0.3772 0.4841 0.4367 -0.0539 0.0289  -0.0711 40  LEU A CD1 
342  C CD2 . LEU A 43  ? 0.3996 0.4995 0.4536 -0.0506 0.0339  -0.0647 40  LEU A CD2 
343  N N   . ALA A 44  ? 0.4466 0.4987 0.4375 -0.0209 0.0423  -0.0608 41  ALA A N   
344  C CA  . ALA A 44  ? 0.4326 0.4736 0.4086 -0.0132 0.0482  -0.0577 41  ALA A CA  
345  C C   . ALA A 44  ? 0.4506 0.4859 0.4214 -0.0097 0.0642  -0.0488 41  ALA A C   
346  O O   . ALA A 44  ? 0.4521 0.4944 0.4299 -0.0092 0.0727  -0.0448 41  ALA A O   
347  C CB  . ALA A 44  ? 0.5051 0.5272 0.4565 -0.0027 0.0384  -0.0638 41  ALA A CB  
348  N N   . PRO A 45  ? 0.4758 0.4976 0.4337 -0.0066 0.0702  -0.0454 42  PRO A N   
349  C CA  . PRO A 45  ? 0.5011 0.5163 0.4554 -0.0053 0.0889  -0.0364 42  PRO A CA  
350  C C   . PRO A 45  ? 0.4559 0.4934 0.4432 -0.0187 0.0978  -0.0324 42  PRO A C   
351  O O   . PRO A 45  ? 0.4742 0.5125 0.4670 -0.0197 0.1144  -0.0257 42  PRO A O   
352  C CB  . PRO A 45  ? 0.5589 0.5478 0.4860 0.0008  0.0921  -0.0344 42  PRO A CB  
353  C CG  . PRO A 45  ? 0.5852 0.5751 0.5109 0.0008  0.0736  -0.0430 42  PRO A CG  
354  C CD  . PRO A 45  ? 0.5164 0.5258 0.4595 -0.0026 0.0604  -0.0502 42  PRO A CD  
355  N N   . LEU A 46  ? 0.4293 0.4853 0.4395 -0.0285 0.0870  -0.0370 43  LEU A N   
356  C CA  . LEU A 46  ? 0.4221 0.4969 0.4618 -0.0403 0.0912  -0.0353 43  LEU A CA  
357  C C   . LEU A 46  ? 0.4035 0.4994 0.4649 -0.0411 0.0948  -0.0348 43  LEU A C   
358  O O   . LEU A 46  ? 0.4200 0.5308 0.5055 -0.0480 0.1027  -0.0325 43  LEU A O   
359  C CB  . LEU A 46  ? 0.3999 0.4815 0.4490 -0.0472 0.0778  -0.0406 43  LEU A CB  
360  C CG  . LEU A 46  ? 0.4267 0.4903 0.4564 -0.0449 0.0732  -0.0420 43  LEU A CG  
361  C CD1 . LEU A 46  ? 0.4402 0.5133 0.4822 -0.0514 0.0626  -0.0465 43  LEU A CD1 
362  C CD2 . LEU A 46  ? 0.4759 0.5207 0.4931 -0.0452 0.0860  -0.0358 43  LEU A CD2 
363  N N   . HIS A 47  ? 0.4232 0.5198 0.4764 -0.0338 0.0886  -0.0377 44  HIS A N   
364  C CA  . HIS A 47  ? 0.4255 0.5391 0.4944 -0.0313 0.0911  -0.0377 44  HIS A CA  
365  C C   . HIS A 47  ? 0.4407 0.5438 0.4890 -0.0217 0.0847  -0.0404 44  HIS A C   
366  O O   . HIS A 47  ? 0.4188 0.5106 0.4535 -0.0224 0.0741  -0.0446 44  HIS A O   
367  C CB  . HIS A 47  ? 0.4122 0.5466 0.5087 -0.0398 0.0835  -0.0414 44  HIS A CB  
368  C CG  . HIS A 47  ? 0.4210 0.5744 0.5353 -0.0354 0.0857  -0.0421 44  HIS A CG  
369  N ND1 . HIS A 47  ? 0.4290 0.5808 0.5326 -0.0261 0.0806  -0.0445 44  HIS A ND1 
370  C CD2 . HIS A 47  ? 0.4456 0.6210 0.5897 -0.0391 0.0918  -0.0418 44  HIS A CD2 
371  C CE1 . HIS A 47  ? 0.4951 0.6671 0.6191 -0.0217 0.0834  -0.0454 44  HIS A CE1 
372  N NE2 . HIS A 47  ? 0.4325 0.6217 0.5841 -0.0298 0.0903  -0.0441 44  HIS A NE2 
373  N N   . PRO A 48  ? 0.4764 0.5821 0.5217 -0.0123 0.0913  -0.0385 45  PRO A N   
374  C CA  . PRO A 48  ? 0.4658 0.5573 0.4884 -0.0031 0.0847  -0.0413 45  PRO A CA  
375  C C   . PRO A 48  ? 0.4463 0.5367 0.4690 -0.0083 0.0709  -0.0471 45  PRO A C   
376  O O   . PRO A 48  ? 0.4670 0.5393 0.4691 -0.0063 0.0636  -0.0504 45  PRO A O   
377  C CB  . PRO A 48  ? 0.5275 0.6297 0.5558 0.0070  0.0941  -0.0386 45  PRO A CB  
378  C CG  . PRO A 48  ? 0.5304 0.6436 0.5741 0.0055  0.1104  -0.0328 45  PRO A CG  
379  C CD  . PRO A 48  ? 0.5374 0.6581 0.5996 -0.0094 0.1066  -0.0337 45  PRO A CD  
380  N N   . VAL A 49  ? 0.4478 0.5553 0.4925 -0.0153 0.0672  -0.0487 46  VAL A N   
381  C CA  . VAL A 49  ? 0.4443 0.5469 0.4849 -0.0190 0.0571  -0.0531 46  VAL A CA  
382  C C   . VAL A 49  ? 0.4232 0.5177 0.4597 -0.0279 0.0513  -0.0557 46  VAL A C   
383  O O   . VAL A 49  ? 0.4188 0.5064 0.4500 -0.0319 0.0455  -0.0590 46  VAL A O   
384  C CB  . VAL A 49  ? 0.4530 0.5716 0.5122 -0.0209 0.0536  -0.0547 46  VAL A CB  
385  C CG1 . VAL A 49  ? 0.5119 0.6444 0.5812 -0.0110 0.0577  -0.0539 46  VAL A CG1 
386  C CG2 . VAL A 49  ? 0.3972 0.5282 0.4764 -0.0308 0.0524  -0.0548 46  VAL A CG2 
387  N N   . LEU A 50  ? 0.3754 0.4701 0.4138 -0.0302 0.0538  -0.0543 47  LEU A N   
388  C CA  . LEU A 50  ? 0.3634 0.4534 0.3994 -0.0362 0.0475  -0.0578 47  LEU A CA  
389  C C   . LEU A 50  ? 0.3784 0.4523 0.3950 -0.0310 0.0440  -0.0605 47  LEU A C   
390  O O   . LEU A 50  ? 0.4063 0.4785 0.4226 -0.0341 0.0375  -0.0649 47  LEU A O   
391  C CB  . LEU A 50  ? 0.3646 0.4618 0.4113 -0.0400 0.0504  -0.0555 47  LEU A CB  
392  C CG  . LEU A 50  ? 0.3639 0.4756 0.4305 -0.0461 0.0508  -0.0546 47  LEU A CG  
393  C CD1 . LEU A 50  ? 0.3661 0.4788 0.4387 -0.0502 0.0536  -0.0525 47  LEU A CD1 
394  C CD2 . LEU A 50  ? 0.3880 0.5015 0.4572 -0.0505 0.0434  -0.0585 47  LEU A CD2 
395  N N   . GLU A 51  ? 0.4213 0.4836 0.4216 -0.0220 0.0470  -0.0590 48  GLU A N   
396  C CA  . GLU A 51  ? 0.4731 0.5165 0.4509 -0.0147 0.0421  -0.0623 48  GLU A CA  
397  C C   . GLU A 51  ? 0.5012 0.5354 0.4732 -0.0187 0.0314  -0.0696 48  GLU A C   
398  O O   . GLU A 51  ? 0.5335 0.5566 0.4947 -0.0162 0.0228  -0.0754 48  GLU A O   
399  C CB  . GLU A 51  ? 0.4930 0.5244 0.4520 -0.0018 0.0507  -0.0574 48  GLU A CB  
400  C CG  . GLU A 51  ? 0.5292 0.5677 0.4942 0.0009  0.0643  -0.0500 48  GLU A CG  
401  C CD  . GLU A 51  ? 0.5963 0.6252 0.5450 0.0139  0.0767  -0.0444 48  GLU A CD  
402  O OE1 . GLU A 51  ? 0.6251 0.6395 0.5537 0.0231  0.0733  -0.0463 48  GLU A OE1 
403  O OE2 . GLU A 51  ? 0.6532 0.6883 0.6093 0.0146  0.0908  -0.0380 48  GLU A OE2 
404  N N   . ASN A 52  ? 0.4222 0.4589 0.4002 -0.0245 0.0316  -0.0699 49  ASN A N   
405  C CA  . ASN A 52  ? 0.4557 0.4799 0.4273 -0.0302 0.0242  -0.0762 49  ASN A CA  
406  C C   . ASN A 52  ? 0.4434 0.4779 0.4329 -0.0433 0.0242  -0.0780 49  ASN A C   
407  O O   . ASN A 52  ? 0.4615 0.5033 0.4573 -0.0444 0.0298  -0.0737 49  ASN A O   
408  C CB  . ASN A 52  ? 0.4871 0.4925 0.4374 -0.0230 0.0256  -0.0748 49  ASN A CB  
409  C CG  . ASN A 52  ? 0.5060 0.4952 0.4328 -0.0090 0.0249  -0.0743 49  ASN A CG  
410  O OD1 . ASN A 52  ? 0.5312 0.5042 0.4441 -0.0076 0.0158  -0.0805 49  ASN A OD1 
411  N ND2 . ASN A 52  ? 0.5428 0.5350 0.4641 0.0021  0.0344  -0.0676 49  ASN A ND2 
412  N N   . TRP A 53  ? 0.4151 0.4494 0.4121 -0.0524 0.0180  -0.0850 50  TRP A N   
413  C CA  . TRP A 53  ? 0.4283 0.4705 0.4413 -0.0650 0.0204  -0.0869 50  TRP A CA  
414  C C   . TRP A 53  ? 0.4596 0.4868 0.4687 -0.0743 0.0175  -0.0931 50  TRP A C   
415  O O   . TRP A 53  ? 0.5046 0.5244 0.5098 -0.0738 0.0086  -0.0998 50  TRP A O   
416  C CB  . TRP A 53  ? 0.4152 0.4790 0.4497 -0.0690 0.0191  -0.0892 50  TRP A CB  
417  C CG  . TRP A 53  ? 0.3948 0.4689 0.4317 -0.0623 0.0230  -0.0829 50  TRP A CG  
418  C CD1 . TRP A 53  ? 0.4278 0.5014 0.4575 -0.0530 0.0226  -0.0800 50  TRP A CD1 
419  C CD2 . TRP A 53  ? 0.3937 0.4755 0.4378 -0.0648 0.0290  -0.0782 50  TRP A CD2 
420  N NE1 . TRP A 53  ? 0.4052 0.4884 0.4421 -0.0520 0.0280  -0.0744 50  TRP A NE1 
421  C CE2 . TRP A 53  ? 0.3894 0.4779 0.4349 -0.0585 0.0305  -0.0738 50  TRP A CE2 
422  C CE3 . TRP A 53  ? 0.3850 0.4655 0.4319 -0.0712 0.0334  -0.0776 50  TRP A CE3 
423  C CZ2 . TRP A 53  ? 0.3694 0.4659 0.4226 -0.0594 0.0336  -0.0702 50  TRP A CZ2 
424  C CZ3 . TRP A 53  ? 0.4060 0.4924 0.4561 -0.0694 0.0364  -0.0736 50  TRP A CZ3 
425  C CH2 . TRP A 53  ? 0.3947 0.4900 0.4493 -0.0639 0.0352  -0.0706 50  TRP A CH2 
426  N N   . TYR A 54  ? 0.4671 0.4875 0.4759 -0.0827 0.0249  -0.0911 51  TYR A N   
427  C CA  . TYR A 54  ? 0.4776 0.4788 0.4806 -0.0938 0.0256  -0.0956 51  TYR A CA  
428  C C   . TYR A 54  ? 0.4964 0.5034 0.5157 -0.1082 0.0347  -0.0963 51  TYR A C   
429  O O   . TYR A 54  ? 0.4490 0.4690 0.4760 -0.1070 0.0413  -0.0917 51  TYR A O   
430  C CB  . TYR A 54  ? 0.5038 0.4754 0.4760 -0.0880 0.0293  -0.0910 51  TYR A CB  
431  C CG  . TYR A 54  ? 0.4986 0.4618 0.4506 -0.0716 0.0243  -0.0885 51  TYR A CG  
432  C CD1 . TYR A 54  ? 0.4636 0.4426 0.4179 -0.0593 0.0266  -0.0826 51  TYR A CD1 
433  C CD2 . TYR A 54  ? 0.4983 0.4386 0.4308 -0.0687 0.0174  -0.0928 51  TYR A CD2 
434  C CE1 . TYR A 54  ? 0.4827 0.4561 0.4212 -0.0445 0.0250  -0.0800 51  TYR A CE1 
435  C CE2 . TYR A 54  ? 0.4897 0.4213 0.4016 -0.0519 0.0145  -0.0902 51  TYR A CE2 
436  C CZ  . TYR A 54  ? 0.4854 0.4347 0.4013 -0.0399 0.0196  -0.0835 51  TYR A CZ  
437  O OH  . TYR A 54  ? 0.5174 0.4590 0.4148 -0.0237 0.0195  -0.0808 51  TYR A OH  
438  N N   . LEU A 55  ? 0.5357 0.5315 0.5599 -0.1223 0.0354  -0.1024 52  LEU A N   
439  C CA  . LEU A 55  ? 0.5186 0.5143 0.5553 -0.1376 0.0478  -0.1026 52  LEU A CA  
440  C C   . LEU A 55  ? 0.6098 0.5748 0.6140 -0.1338 0.0585  -0.0941 52  LEU A C   
441  O O   . LEU A 55  ? 0.5918 0.5333 0.5677 -0.1243 0.0540  -0.0918 52  LEU A O   
442  C CB  . LEU A 55  ? 0.5812 0.5706 0.6322 -0.1549 0.0458  -0.1122 52  LEU A CB  
443  C CG  . LEU A 55  ? 0.5671 0.5843 0.6495 -0.1578 0.0317  -0.1236 52  LEU A CG  
444  C CD1 . LEU A 55  ? 0.6118 0.6240 0.7132 -0.1777 0.0304  -0.1341 52  LEU A CD1 
445  C CD2 . LEU A 55  ? 0.5534 0.6079 0.6653 -0.1557 0.0337  -0.1242 52  LEU A CD2 
446  N N   . CYS A 56  ? 0.6558 0.6197 0.6612 -0.1389 0.0720  -0.0897 53  CYS A N   
447  C CA  . CYS A 56  ? 0.7272 0.6583 0.6977 -0.1335 0.0817  -0.0824 53  CYS A CA  
448  C C   . CYS A 56  ? 0.7390 0.6331 0.6899 -0.1457 0.0883  -0.0840 53  CYS A C   
449  O O   . CYS A 56  ? 0.7633 0.6628 0.7356 -0.1615 0.0871  -0.0912 53  CYS A O   
450  C CB  . CYS A 56  ? 0.7794 0.7166 0.7527 -0.1335 0.0937  -0.0776 53  CYS A CB  
451  S SG  . CYS A 56  ? 0.7603 0.7354 0.7532 -0.1199 0.0847  -0.0763 53  CYS A SG  
452  N N   . GLY A 57  ? 0.7746 0.6299 0.6844 -0.1379 0.0943  -0.0781 54  GLY A N   
453  C CA  . GLY A 57  ? 0.8594 0.6716 0.7429 -0.1484 0.1013  -0.0788 54  GLY A CA  
454  C C   . GLY A 57  ? 0.9203 0.6877 0.7542 -0.1372 0.1104  -0.0714 54  GLY A C   
455  O O   . GLY A 57  ? 0.9064 0.6781 0.7261 -0.1183 0.1072  -0.0669 54  GLY A O   
456  N N   . ASP A 58  ? 1.0599 0.7822 0.8664 -0.1487 0.1205  -0.0711 55  ASP A N   
457  C CA  . ASP A 58  ? 1.1163 0.7860 0.8684 -0.1388 0.1305  -0.0645 55  ASP A CA  
458  C C   . ASP A 58  ? 1.0279 0.6796 0.7447 -0.1146 0.1156  -0.0639 55  ASP A C   
459  O O   . ASP A 58  ? 1.0316 0.6890 0.7337 -0.0926 0.1102  -0.0605 55  ASP A O   
460  C CB  . ASP A 58  ? 1.2192 0.8429 0.9523 -0.1604 0.1465  -0.0647 55  ASP A CB  
461  C CG  . ASP A 58  ? 1.3235 0.9655 1.0950 -0.1863 0.1641  -0.0659 55  ASP A CG  
462  O OD1 . ASP A 58  ? 1.3228 1.0125 1.1330 -0.1855 0.1631  -0.0666 55  ASP A OD1 
463  O OD2 . ASP A 58  ? 1.3343 0.9430 1.0980 -0.2075 0.1788  -0.0667 55  ASP A OD2 
464  N N   . SER A 59  ? 0.9579 0.5862 0.6604 -0.1184 0.1091  -0.0678 56  SER A N   
465  C CA  . SER A 59  ? 0.9215 0.5333 0.5911 -0.0947 0.0960  -0.0677 56  SER A CA  
466  C C   . SER A 59  ? 0.8070 0.4724 0.5123 -0.0829 0.0812  -0.0701 56  SER A C   
467  O O   . SER A 59  ? 0.7454 0.4518 0.4956 -0.0952 0.0797  -0.0730 56  SER A O   
468  C CB  . SER A 59  ? 1.0145 0.5854 0.6578 -0.1016 0.0930  -0.0714 56  SER A CB  
469  O OG  . SER A 59  ? 1.0149 0.6135 0.6982 -0.1186 0.0854  -0.0787 56  SER A OG  
470  N N   . LEU A 60  ? 0.8340 0.4982 0.5187 -0.0584 0.0712  -0.0690 57  LEU A N   
471  C CA  . LEU A 60  ? 0.7760 0.4876 0.4932 -0.0483 0.0603  -0.0706 57  LEU A CA  
472  C C   . LEU A 60  ? 0.7549 0.4726 0.4878 -0.0592 0.0535  -0.0762 57  LEU A C   
473  O O   . LEU A 60  ? 0.6867 0.4440 0.4554 -0.0617 0.0480  -0.0783 57  LEU A O   
474  C CB  . LEU A 60  ? 0.7982 0.5087 0.4927 -0.0201 0.0533  -0.0687 57  LEU A CB  
475  C CG  . LEU A 60  ? 0.7747 0.5314 0.5007 -0.0091 0.0451  -0.0694 57  LEU A CG  
476  C CD1 . LEU A 60  ? 0.7334 0.5336 0.4997 -0.0146 0.0464  -0.0682 57  LEU A CD1 
477  C CD2 . LEU A 60  ? 0.7885 0.5418 0.4923 0.0179  0.0397  -0.0685 57  LEU A CD2 
478  N N   . ARG A 61  ? 0.7625 0.4372 0.4663 -0.0660 0.0533  -0.0790 58  ARG A N   
479  C CA  . ARG A 61  ? 0.7866 0.4616 0.5011 -0.0753 0.0443  -0.0859 58  ARG A CA  
480  C C   . ARG A 61  ? 0.7782 0.4850 0.5400 -0.0991 0.0458  -0.0906 58  ARG A C   
481  O O   . ARG A 61  ? 0.7411 0.4782 0.5306 -0.0998 0.0361  -0.0954 58  ARG A O   
482  C CB  . ARG A 61  ? 0.8415 0.4591 0.5123 -0.0782 0.0431  -0.0886 58  ARG A CB  
483  C CG  . ARG A 61  ? 0.8391 0.4495 0.5162 -0.0883 0.0315  -0.0974 58  ARG A CG  
484  C CD  . ARG A 61  ? 0.9008 0.4513 0.5259 -0.0835 0.0278  -0.0994 58  ARG A CD  
485  N NE  . ARG A 61  ? 0.9466 0.4528 0.5461 -0.0980 0.0405  -0.0971 58  ARG A NE  
486  C CZ  . ARG A 61  ? 1.0154 0.4620 0.5611 -0.0922 0.0412  -0.0965 58  ARG A CZ  
487  N NH1 . ARG A 61  ? 1.0479 0.4745 0.5593 -0.0696 0.0296  -0.0978 58  ARG A NH1 
488  N NH2 . ARG A 61  ? 1.0772 0.4816 0.5992 -0.1069 0.0552  -0.0938 58  ARG A NH2 
489  N N   . ASP A 62  ? 0.7744 0.4739 0.5438 -0.1166 0.0588  -0.0892 59  ASP A N   
490  C CA  . ASP A 62  ? 0.7830 0.5141 0.5987 -0.1386 0.0623  -0.0939 59  ASP A CA  
491  C C   . ASP A 62  ? 0.7348 0.5185 0.5862 -0.1303 0.0583  -0.0926 59  ASP A C   
492  O O   . ASP A 62  ? 0.7345 0.5499 0.6223 -0.1391 0.0517  -0.0990 59  ASP A O   
493  C CB  . ASP A 62  ? 0.9068 0.6189 0.7197 -0.1555 0.0813  -0.0904 59  ASP A CB  
494  C CG  . ASP A 62  ? 0.9752 0.7194 0.8372 -0.1791 0.0881  -0.0955 59  ASP A CG  
495  O OD1 . ASP A 62  ? 1.0165 0.7955 0.9146 -0.1832 0.0756  -0.1034 59  ASP A OD1 
496  O OD2 . ASP A 62  ? 1.1356 0.8703 0.9984 -0.1909 0.1065  -0.0914 59  ASP A OD2 
497  N N   . ALA A 63  ? 0.6606 0.4518 0.5004 -0.1129 0.0612  -0.0852 60  ALA A N   
498  C CA  . ALA A 63  ? 0.6210 0.4566 0.4912 -0.1062 0.0589  -0.0834 60  ALA A CA  
499  C C   . ALA A 63  ? 0.5839 0.4438 0.4655 -0.0939 0.0460  -0.0856 60  ALA A C   
500  O O   . ALA A 63  ? 0.5545 0.4493 0.4626 -0.0910 0.0439  -0.0849 60  ALA A O   
501  C CB  . ALA A 63  ? 0.6437 0.4758 0.4971 -0.0926 0.0649  -0.0762 60  ALA A CB  
502  N N   . LEU A 64  ? 0.5892 0.4273 0.4479 -0.0862 0.0383  -0.0879 61  LEU A N   
503  C CA  . LEU A 64  ? 0.5823 0.4366 0.4447 -0.0727 0.0285  -0.0892 61  LEU A CA  
504  C C   . LEU A 64  ? 0.5848 0.4287 0.4476 -0.0796 0.0182  -0.0977 61  LEU A C   
505  O O   . LEU A 64  ? 0.5880 0.4362 0.4456 -0.0672 0.0098  -0.0993 61  LEU A O   
506  C CB  . LEU A 64  ? 0.5819 0.4201 0.4127 -0.0512 0.0284  -0.0841 61  LEU A CB  
507  C CG  . LEU A 64  ? 0.5675 0.4226 0.4020 -0.0403 0.0342  -0.0777 61  LEU A CG  
508  C CD1 . LEU A 64  ? 0.5751 0.4187 0.3832 -0.0181 0.0328  -0.0746 61  LEU A CD1 
509  C CD2 . LEU A 64  ? 0.5417 0.4392 0.4122 -0.0410 0.0339  -0.0765 61  LEU A CD2 
510  N N   . SER A 65  ? 0.5891 0.4187 0.4584 -0.0994 0.0187  -0.1038 62  SER A N   
511  C CA  . SER A 65  ? 0.6064 0.4248 0.4777 -0.1071 0.0063  -0.1140 62  SER A CA  
512  C C   . SER A 65  ? 0.5867 0.4420 0.4964 -0.1125 -0.0025 -0.1215 62  SER A C   
513  O O   . SER A 65  ? 0.6175 0.4676 0.5256 -0.1104 -0.0170 -0.1302 62  SER A O   
514  C CB  . SER A 65  ? 0.6324 0.4210 0.4988 -0.1280 0.0100  -0.1190 62  SER A CB  
515  O OG  . SER A 65  ? 0.6871 0.4315 0.5091 -0.1213 0.0153  -0.1138 62  SER A OG  
516  N N   . HIS A 66  ? 0.5685 0.4581 0.5092 -0.1176 0.0048  -0.1186 63  HIS A N   
517  C CA  . HIS A 66  ? 0.5503 0.4737 0.5267 -0.1224 -0.0033 -0.1264 63  HIS A CA  
518  C C   . HIS A 66  ? 0.5023 0.4527 0.4852 -0.1069 -0.0028 -0.1204 63  HIS A C   
519  O O   . HIS A 66  ? 0.5025 0.4745 0.5031 -0.1098 0.0065  -0.1154 63  HIS A O   
520  C CB  . HIS A 66  ? 0.5551 0.4949 0.5656 -0.1443 0.0049  -0.1305 63  HIS A CB  
521  C CG  . HIS A 66  ? 0.5919 0.5028 0.5966 -0.1623 0.0075  -0.1357 63  HIS A CG  
522  N ND1 . HIS A 66  ? 0.6495 0.5440 0.6521 -0.1683 -0.0070 -0.1470 63  HIS A ND1 
523  C CD2 . HIS A 66  ? 0.6344 0.5255 0.6317 -0.1755 0.0238  -0.1307 63  HIS A CD2 
524  C CE1 . HIS A 66  ? 0.6534 0.5201 0.6501 -0.1867 0.0008  -0.1487 63  HIS A CE1 
525  N NE2 . HIS A 66  ? 0.6299 0.4930 0.6218 -0.1909 0.0206  -0.1384 63  HIS A NE2 
526  N N   . ASN A 67  ? 0.5188 0.4648 0.4856 -0.0908 -0.0128 -0.1214 64  ASN A N   
527  C CA  . ASN A 67  ? 0.4953 0.4601 0.4634 -0.0761 -0.0118 -0.1157 64  ASN A CA  
528  C C   . ASN A 67  ? 0.4988 0.4877 0.4923 -0.0782 -0.0213 -0.1240 64  ASN A C   
529  O O   . ASN A 67  ? 0.5194 0.5008 0.5070 -0.0733 -0.0354 -0.1329 64  ASN A O   
530  C CB  . ASN A 67  ? 0.5397 0.4836 0.4747 -0.0574 -0.0151 -0.1124 64  ASN A CB  
531  C CG  . ASN A 67  ? 0.5125 0.4721 0.4471 -0.0435 -0.0100 -0.1050 64  ASN A CG  
532  O OD1 . ASN A 67  ? 0.5189 0.4988 0.4719 -0.0445 -0.0124 -0.1070 64  ASN A OD1 
533  N ND2 . ASN A 67  ? 0.5068 0.4581 0.4227 -0.0317 -0.0017 -0.0966 64  ASN A ND2 
534  N N   . VAL A 68  ? 0.4984 0.5144 0.5174 -0.0836 -0.0147 -0.1216 65  VAL A N   
535  C CA  . VAL A 68  ? 0.4880 0.5282 0.5317 -0.0845 -0.0233 -0.1298 65  VAL A CA  
536  C C   . VAL A 68  ? 0.5375 0.5773 0.5657 -0.0661 -0.0300 -0.1286 65  VAL A C   
537  O O   . VAL A 68  ? 0.5294 0.5809 0.5680 -0.0619 -0.0415 -0.1373 65  VAL A O   
538  C CB  . VAL A 68  ? 0.5215 0.5881 0.5939 -0.0944 -0.0134 -0.1277 65  VAL A CB  
539  C CG1 . VAL A 68  ? 0.5426 0.6058 0.6273 -0.1124 -0.0040 -0.1285 65  VAL A CG1 
540  C CG2 . VAL A 68  ? 0.4769 0.5481 0.5411 -0.0863 -0.0031 -0.1160 65  VAL A CG2 
541  N N   . THR A 69  ? 0.5039 0.5309 0.5082 -0.0549 -0.0221 -0.1180 66  THR A N   
542  C CA  . THR A 69  ? 0.5283 0.5498 0.5142 -0.0382 -0.0244 -0.1151 66  THR A CA  
543  C C   . THR A 69  ? 0.5757 0.5716 0.5341 -0.0267 -0.0361 -0.1212 66  THR A C   
544  O O   . THR A 69  ? 0.6420 0.6286 0.5815 -0.0117 -0.0406 -0.1216 66  THR A O   
545  C CB  . THR A 69  ? 0.5142 0.5378 0.4934 -0.0330 -0.0095 -0.1021 66  THR A CB  
546  O OG1 . THR A 69  ? 0.5075 0.5221 0.4797 -0.0360 -0.0018 -0.0968 66  THR A OG1 
547  C CG2 . THR A 69  ? 0.5157 0.5624 0.5184 -0.0403 -0.0032 -0.0988 66  THR A CG2 
548  N N   . GLU A 70  ? 0.5613 0.5415 0.5134 -0.0329 -0.0410 -0.1260 67  GLU A N   
549  C CA  . GLU A 70  ? 0.6103 0.5637 0.5353 -0.0223 -0.0548 -0.1337 67  GLU A CA  
550  C C   . GLU A 70  ? 0.6369 0.5970 0.5818 -0.0313 -0.0733 -0.1499 67  GLU A C   
551  O O   . GLU A 70  ? 0.7264 0.6741 0.6561 -0.0193 -0.0898 -0.1594 67  GLU A O   
552  C CB  . GLU A 70  ? 0.7085 0.6345 0.6096 -0.0222 -0.0521 -0.1311 67  GLU A CB  
553  C CG  . GLU A 70  ? 0.7858 0.7008 0.6620 -0.0086 -0.0373 -0.1178 67  GLU A CG  
554  C CD  . GLU A 70  ? 0.8754 0.7613 0.7245 -0.0051 -0.0368 -0.1168 67  GLU A CD  
555  O OE1 . GLU A 70  ? 0.9472 0.8190 0.7964 -0.0160 -0.0470 -0.1257 67  GLU A OE1 
556  O OE2 . GLU A 70  ? 0.9973 0.8734 0.8243 0.0089  -0.0264 -0.1077 67  GLU A OE2 
557  N N   . HIS A 71  ? 0.5999 0.5788 0.5785 -0.0520 -0.0701 -0.1534 68  HIS A N   
558  C CA  . HIS A 71  ? 0.6206 0.6112 0.6272 -0.0646 -0.0850 -0.1692 68  HIS A CA  
559  C C   . HIS A 71  ? 0.6147 0.6444 0.6632 -0.0749 -0.0802 -0.1713 68  HIS A C   
560  O O   . HIS A 71  ? 0.5905 0.6330 0.6618 -0.0920 -0.0669 -0.1676 68  HIS A O   
561  C CB  . HIS A 71  ? 0.6573 0.6290 0.6635 -0.0811 -0.0838 -0.1723 68  HIS A CB  
562  C CG  . HIS A 71  ? 0.7180 0.6492 0.6796 -0.0687 -0.0892 -0.1706 68  HIS A CG  
563  N ND1 . HIS A 71  ? 0.7452 0.6533 0.6826 -0.0693 -0.0757 -0.1599 68  HIS A ND1 
564  C CD2 . HIS A 71  ? 0.7852 0.6936 0.7194 -0.0531 -0.1065 -0.1785 68  HIS A CD2 
565  C CE1 . HIS A 71  ? 0.7819 0.6559 0.6800 -0.0547 -0.0840 -0.1611 68  HIS A CE1 
566  N NE2 . HIS A 71  ? 0.8102 0.6825 0.7046 -0.0449 -0.1025 -0.1721 68  HIS A NE2 
567  N N   . ARG A 72  ? 0.6762 0.7695 0.7958 -0.0767 -0.0524 -0.3012 69  ARG A N   
568  C CA  . ARG A 72  ? 0.7336 0.8687 0.8923 -0.0878 -0.0473 -0.3017 69  ARG A CA  
569  C C   . ARG A 72  ? 0.7085 0.8593 0.9163 -0.1225 -0.0439 -0.3180 69  ARG A C   
570  O O   . ARG A 72  ? 0.6916 0.8615 0.9245 -0.1389 -0.0271 -0.3084 69  ARG A O   
571  C CB  . ARG A 72  ? 0.8953 1.0591 1.0550 -0.0625 -0.0672 -0.3160 69  ARG A CB  
572  C CG  . ARG A 72  ? 1.0670 1.2149 1.1781 -0.0253 -0.0695 -0.3010 69  ARG A CG  
573  C CD  . ARG A 72  ? 1.2306 1.4010 1.3365 0.0019  -0.0889 -0.3161 69  ARG A CD  
574  N NE  . ARG A 72  ? 1.4021 1.5522 1.4572 0.0401  -0.0892 -0.3019 69  ARG A NE  
575  C CZ  . ARG A 72  ? 1.4446 1.5860 1.4803 0.0508  -0.0692 -0.2711 69  ARG A CZ  
576  N NH1 . ARG A 72  ? 1.3973 1.5208 1.3898 0.0858  -0.0676 -0.2588 69  ARG A NH1 
577  N NH2 . ARG A 72  ? 1.4501 1.5999 1.5100 0.0277  -0.0507 -0.2528 69  ARG A NH2 
578  N N   . GLN A 73  ? 0.6811 0.8232 0.9038 -0.1329 -0.0596 -0.3429 70  GLN A N   
579  C CA  . GLN A 73  ? 0.6951 0.8551 0.9733 -0.1674 -0.0551 -0.3588 70  GLN A CA  
580  C C   . GLN A 73  ? 0.6697 0.8048 0.9485 -0.1937 -0.0249 -0.3381 70  GLN A C   
581  O O   . GLN A 73  ? 0.6937 0.8453 1.0171 -0.2219 -0.0114 -0.3429 70  GLN A O   
582  C CB  . GLN A 73  ? 0.7453 0.8975 1.0444 -0.1761 -0.0793 -0.3905 70  GLN A CB  
583  C CG  . GLN A 73  ? 0.8831 0.9776 1.1435 -0.1768 -0.0827 -0.3901 70  GLN A CG  
584  C CD  . GLN A 73  ? 0.9679 1.0333 1.1625 -0.1381 -0.0940 -0.3815 70  GLN A CD  
585  O OE1 . GLN A 73  ? 0.9340 1.0194 1.1089 -0.1091 -0.0993 -0.3747 70  GLN A OE1 
586  N NE2 . GLN A 73  ? 1.0534 1.0689 1.2126 -0.1362 -0.0972 -0.3818 70  GLN A NE2 
587  N N   . ASP A 74  ? 0.6426 0.7386 0.8720 -0.1829 -0.0133 -0.3150 71  ASP A N   
588  C CA  . ASP A 74  ? 0.6529 0.7218 0.8758 -0.2028 0.0133  -0.2961 71  ASP A CA  
589  C C   . ASP A 74  ? 0.6438 0.7428 0.8857 -0.2079 0.0314  -0.2817 71  ASP A C   
590  O O   . ASP A 74  ? 0.7026 0.7915 0.9559 -0.2288 0.0534  -0.2735 71  ASP A O   
591  C CB  . ASP A 74  ? 0.6413 0.6636 0.8084 -0.1876 0.0190  -0.2766 71  ASP A CB  
592  C CG  . ASP A 74  ? 0.6879 0.6711 0.8276 -0.1817 0.0045  -0.2883 71  ASP A CG  
593  O OD1 . ASP A 74  ? 0.7122 0.7011 0.8760 -0.1901 -0.0130 -0.3137 71  ASP A OD1 
594  O OD2 . ASP A 74  ? 0.6940 0.6408 0.7885 -0.1675 0.0097  -0.2727 71  ASP A OD2 
595  N N   . LEU A 75  ? 0.6357 0.7673 0.8774 -0.1871 0.0230  -0.2783 72  LEU A N   
596  C CA  . LEU A 75  ? 0.6578 0.8152 0.9137 -0.1888 0.0370  -0.2662 72  LEU A CA  
597  C C   . LEU A 75  ? 0.6927 0.8732 0.9954 -0.2150 0.0505  -0.2761 72  LEU A C   
598  O O   . LEU A 75  ? 0.6543 0.8303 0.9569 -0.2240 0.0724  -0.2616 72  LEU A O   
599  C CB  . LEU A 75  ? 0.7201 0.9116 0.9770 -0.1649 0.0223  -0.2678 72  LEU A CB  
600  C CG  . LEU A 75  ? 0.7330 0.9069 0.9489 -0.1392 0.0179  -0.2498 72  LEU A CG  
601  C CD1 . LEU A 75  ? 0.7068 0.9123 0.9275 -0.1196 0.0087  -0.2491 72  LEU A CD1 
602  C CD2 . LEU A 75  ? 0.7776 0.9235 0.9713 -0.1427 0.0355  -0.2265 72  LEU A CD2 
603  N N   . ALA A 76  ? 0.6318 0.8377 0.9749 -0.2253 0.0369  -0.3011 73  ALA A N   
604  C CA  . ALA A 76  ? 0.6755 0.9106 1.0743 -0.2513 0.0497  -0.3122 73  ALA A CA  
605  C C   . ALA A 76  ? 0.7578 0.9540 1.1554 -0.2777 0.0764  -0.3012 73  ALA A C   
606  O O   . ALA A 76  ? 0.7805 0.9926 1.2137 -0.2978 0.0991  -0.2990 73  ALA A O   
607  C CB  . ALA A 76  ? 0.6338 0.9012 1.0778 -0.2560 0.0254  -0.3434 73  ALA A CB  
608  N N   . LYS A 77  ? 0.7730 0.9168 1.1278 -0.2759 0.0750  -0.2939 74  LYS A N   
609  C CA  . LYS A 77  ? 0.8919 0.9900 1.2359 -0.2976 0.0995  -0.2828 74  LYS A CA  
610  C C   . LYS A 77  ? 0.8663 0.9464 1.1747 -0.2897 0.1242  -0.2555 74  LYS A C   
611  O O   . LYS A 77  ? 0.8973 0.9556 1.2071 -0.3068 0.1520  -0.2446 74  LYS A O   
612  C CB  . LYS A 77  ? 0.9957 1.0432 1.3033 -0.2951 0.0869  -0.2865 74  LYS A CB  
613  C CG  . LYS A 77  ? 1.0881 1.0804 1.3793 -0.3164 0.1100  -0.2767 74  LYS A CG  
614  C CD  . LYS A 77  ? 1.2036 1.1450 1.4547 -0.3102 0.0949  -0.2815 74  LYS A CD  
615  C CE  . LYS A 77  ? 1.3128 1.1936 1.5426 -0.3298 0.1176  -0.2717 74  LYS A CE  
616  N NZ  . LYS A 77  ? 1.3338 1.2207 1.6222 -0.3664 0.1316  -0.2837 74  LYS A NZ  
617  N N   . ALA A 78  ? 0.7779 0.8641 1.0534 -0.2625 0.1135  -0.2447 75  ALA A N   
618  C CA  . ALA A 78  ? 0.7988 0.8701 1.0422 -0.2517 0.1302  -0.2223 75  ALA A CA  
619  C C   . ALA A 78  ? 0.8942 0.9987 1.1709 -0.2609 0.1483  -0.2213 75  ALA A C   
620  O O   . ALA A 78  ? 0.9466 1.0283 1.2105 -0.2680 0.1742  -0.2076 75  ALA A O   
621  C CB  . ALA A 78  ? 0.7312 0.8095 0.9465 -0.2237 0.1124  -0.2142 75  ALA A CB  
622  N N   . LEU A 79  ? 0.8364 0.9939 1.1535 -0.2582 0.1347  -0.2363 76  LEU A N   
623  C CA  . LEU A 79  ? 0.8052 1.0026 1.1577 -0.2632 0.1489  -0.2377 76  LEU A CA  
624  C C   . LEU A 79  ? 0.8723 1.0673 1.2611 -0.2924 0.1759  -0.2401 76  LEU A C   
625  O O   . LEU A 79  ? 0.8864 1.0755 1.2710 -0.2958 0.2039  -0.2259 76  LEU A O   
626  C CB  . LEU A 79  ? 0.7743 1.0265 1.1623 -0.2534 0.1247  -0.2569 76  LEU A CB  
627  C CG  . LEU A 79  ? 0.7812 1.0831 1.2102 -0.2550 0.1352  -0.2619 76  LEU A CG  
628  C CD1 . LEU A 79  ? 0.7302 1.0258 1.1234 -0.2351 0.1442  -0.2432 76  LEU A CD1 
629  C CD2 . LEU A 79  ? 0.7707 1.1241 1.2377 -0.2469 0.1088  -0.2855 76  LEU A CD2 
630  N N   . SER A 80  ? 0.9476 1.1441 1.3705 -0.3125 0.1676  -0.2577 77  SER A N   
631  C CA  . SER A 80  ? 0.8995 1.0945 1.3675 -0.3444 0.1917  -0.2621 77  SER A CA  
632  C C   . SER A 80  ? 0.9667 1.1031 1.3939 -0.3525 0.2257  -0.2379 77  SER A C   
633  O O   . SER A 80  ? 0.9569 1.0953 1.4110 -0.3708 0.2583  -0.2304 77  SER A O   
634  C CB  . SER A 80  ? 0.8650 1.0591 1.3663 -0.3617 0.1707  -0.2856 77  SER A CB  
635  O OG  . SER A 80  ? 0.8873 1.0779 1.4382 -0.3958 0.1943  -0.2898 77  SER A OG  
636  N N   . ARG A 81  ? 1.0222 1.1066 1.3841 -0.3368 0.2187  -0.2254 78  ARG A N   
637  C CA  . ARG A 81  ? 1.1053 1.1279 1.4178 -0.3385 0.2459  -0.2038 78  ARG A CA  
638  C C   . ARG A 81  ? 1.0803 1.0981 1.3551 -0.3171 0.2625  -0.1835 78  ARG A C   
639  O O   . ARG A 81  ? 1.0866 1.0728 1.3421 -0.3220 0.2952  -0.1674 78  ARG A O   
640  C CB  . ARG A 81  ? 1.2341 1.2068 1.4906 -0.3251 0.2277  -0.2002 78  ARG A CB  
641  C CG  . ARG A 81  ? 1.3395 1.2443 1.5378 -0.3222 0.2516  -0.1793 78  ARG A CG  
642  C CD  . ARG A 81  ? 1.4007 1.2663 1.5428 -0.3013 0.2311  -0.1750 78  ARG A CD  
643  N NE  . ARG A 81  ? 1.3978 1.2555 1.5490 -0.3085 0.2093  -0.1911 78  ARG A NE  
644  C CZ  . ARG A 81  ? 1.3742 1.2035 1.4825 -0.2900 0.1906  -0.1895 78  ARG A CZ  
645  N NH1 . ARG A 81  ? 1.2554 1.0670 1.3164 -0.2650 0.1897  -0.1736 78  ARG A NH1 
646  N NH2 . ARG A 81  ? 1.3519 1.1724 1.4662 -0.2948 0.1715  -0.2050 78  ARG A NH2 
647  N N   . ASP A 82  ? 0.9370 0.9827 1.1990 -0.2922 0.2395  -0.1846 79  ASP A N   
648  C CA  . ASP A 82  ? 0.9359 0.9727 1.1574 -0.2683 0.2463  -0.1683 79  ASP A CA  
649  C C   . ASP A 82  ? 0.9588 1.0415 1.2116 -0.2656 0.2589  -0.1690 79  ASP A C   
650  O O   . ASP A 82  ? 0.8848 0.9509 1.1043 -0.2503 0.2752  -0.1543 79  ASP A O   
651  C CB  . ASP A 82  ? 0.8988 0.9370 1.0909 -0.2433 0.2145  -0.1683 79  ASP A CB  
652  C CG  . ASP A 82  ? 0.9140 0.9124 1.0750 -0.2412 0.2012  -0.1673 79  ASP A CG  
653  O OD1 . ASP A 82  ? 0.9499 0.9135 1.1056 -0.2582 0.2153  -0.1668 79  ASP A OD1 
654  O OD2 . ASP A 82  ? 0.7566 0.7602 0.9022 -0.2232 0.1772  -0.1674 79  ASP A OD2 
655  N N   . ARG A 83  ? 0.9709 1.1103 1.2843 -0.2769 0.2497  -0.1868 80  ARG A N   
656  C CA  . ARG A 83  ? 1.0301 1.2170 1.3738 -0.2713 0.2597  -0.1886 80  ARG A CA  
657  C C   . ARG A 83  ? 1.1657 1.3350 1.5054 -0.2788 0.3021  -0.1728 80  ARG A C   
658  O O   . ARG A 83  ? 1.1631 1.3025 1.5092 -0.3007 0.3257  -0.1677 80  ARG A O   
659  C CB  . ARG A 83  ? 1.0391 1.2889 1.4544 -0.2850 0.2466  -0.2118 80  ARG A CB  
660  C CG  . ARG A 83  ? 1.0365 1.2924 1.5059 -0.3187 0.2622  -0.2218 80  ARG A CG  
661  C CD  . ARG A 83  ? 1.0174 1.3418 1.5592 -0.3269 0.2445  -0.2472 80  ARG A CD  
662  N NE  . ARG A 83  ? 1.0420 1.4120 1.6034 -0.3142 0.2569  -0.2446 80  ARG A NE  
663  C CZ  . ARG A 83  ? 0.9922 1.4016 1.5547 -0.2909 0.2325  -0.2541 80  ARG A CZ  
664  N NH1 . ARG A 83  ? 1.0170 1.4619 1.5921 -0.2784 0.2464  -0.2504 80  ARG A NH1 
665  N NH2 . ARG A 83  ? 0.9525 1.3618 1.4983 -0.2777 0.1960  -0.2657 80  ARG A NH2 
666  N N   . ARG A 84  ? 1.2231 1.4092 1.5502 -0.2589 0.3123  -0.1648 81  ARG A N   
667  C CA  . ARG A 84  ? 1.2764 1.4472 1.5932 -0.2591 0.3543  -0.1482 81  ARG A CA  
668  C C   . ARG A 84  ? 1.1203 1.3557 1.5134 -0.2754 0.3714  -0.1585 81  ARG A C   
669  O O   . ARG A 84  ? 0.9724 1.2608 1.4166 -0.2812 0.3456  -0.1792 81  ARG A O   
670  C CB  . ARG A 84  ? 1.3933 1.5383 1.6444 -0.2237 0.3538  -0.1340 81  ARG A CB  
671  C CG  . ARG A 84  ? 1.4762 1.5708 1.6651 -0.2066 0.3276  -0.1290 81  ARG A CG  
672  C CD  . ARG A 84  ? 1.5381 1.6000 1.6622 -0.1726 0.3261  -0.1163 81  ARG A CD  
673  N NE  . ARG A 84  ? 1.6935 1.7101 1.7769 -0.1666 0.3643  -0.0983 81  ARG A NE  
674  C CZ  . ARG A 84  ? 1.7271 1.6891 1.7783 -0.1747 0.3809  -0.0878 81  ARG A CZ  
675  N NH1 . ARG A 84  ? 1.6861 1.6332 1.7411 -0.1886 0.3609  -0.0942 81  ARG A NH1 
676  N NH2 . ARG A 84  ? 1.8032 1.7218 1.8129 -0.1658 0.4179  -0.0702 81  ARG A NH2 
677  N N   . THR A 85  ? 1.1439 1.3754 1.5442 -0.2802 0.4153  -0.1439 82  THR A N   
678  C CA  . THR A 85  ? 1.1373 1.4328 1.6166 -0.2967 0.4366  -0.1519 82  THR A CA  
679  C C   . THR A 85  ? 1.0318 1.3812 1.5198 -0.2701 0.4231  -0.1591 82  THR A C   
680  O O   . THR A 85  ? 1.1419 1.5515 1.6955 -0.2784 0.4380  -0.1671 82  THR A O   
681  C CB  . THR A 85  ? 1.2478 1.5210 1.7333 -0.3102 0.4930  -0.1311 82  THR A CB  
682  O OG1 . THR A 85  ? 1.3748 1.6082 1.7830 -0.2763 0.5118  -0.1094 82  THR A OG1 
683  C CG2 . THR A 85  ? 1.2891 1.5085 1.7713 -0.3390 0.5087  -0.1245 82  THR A CG2 
684  N N   . ARG A 86  ? 0.9478 1.2759 1.3728 -0.2383 0.3950  -0.1569 83  ARG A N   
685  C CA  . ARG A 86  ? 0.8745 1.2447 1.2997 -0.2112 0.3802  -0.1633 83  ARG A CA  
686  C C   . ARG A 86  ? 0.8501 1.2109 1.2392 -0.1915 0.3328  -0.1724 83  ARG A C   
687  O O   . ARG A 86  ? 0.8281 1.1990 1.1913 -0.1635 0.3189  -0.1728 83  ARG A O   
688  C CB  . ARG A 86  ? 0.9591 1.3041 1.3326 -0.1843 0.4102  -0.1430 83  ARG A CB  
689  C CG  . ARG A 86  ? 0.9674 1.3223 1.3734 -0.1989 0.4635  -0.1301 83  ARG A CG  
690  C CD  . ARG A 86  ? 1.0347 1.3523 1.3744 -0.1673 0.4940  -0.1079 83  ARG A CD  
691  N NE  . ARG A 86  ? 1.0919 1.4187 1.4643 -0.1814 0.5498  -0.0930 83  ARG A NE  
692  C CZ  . ARG A 86  ? 1.1528 1.4191 1.4843 -0.1852 0.5878  -0.0707 83  ARG A CZ  
693  N NH1 . ARG A 86  ? 1.1861 1.3810 1.4467 -0.1779 0.5727  -0.0636 83  ARG A NH1 
694  N NH2 . ARG A 86  ? 1.1345 1.4130 1.5012 -0.1981 0.6417  -0.0560 83  ARG A NH2 
695  N N   . ALA A 87  ? 0.7392 1.0793 1.1260 -0.2051 0.3089  -0.1792 84  ALA A N   
696  C CA  . ALA A 87  ? 0.6599 0.9916 1.0151 -0.1864 0.2686  -0.1851 84  ALA A CA  
697  C C   . ALA A 87  ? 0.6123 0.9302 0.9750 -0.2024 0.2459  -0.1938 84  ALA A C   
698  O O   . ALA A 87  ? 0.6580 0.9433 1.0174 -0.2215 0.2594  -0.1887 84  ALA A O   
699  C CB  . ALA A 87  ? 0.6718 0.9514 0.9540 -0.1607 0.2668  -0.1684 84  ALA A CB  
700  N N   . VAL A 88  ? 0.5419 0.8828 0.9111 -0.1918 0.2119  -0.2066 85  VAL A N   
701  C CA  . VAL A 88  ? 0.5374 0.8644 0.9039 -0.1983 0.1874  -0.2139 85  VAL A CA  
702  C C   . VAL A 88  ? 0.5404 0.8090 0.8460 -0.1874 0.1840  -0.1968 85  VAL A C   
703  O O   . VAL A 88  ? 0.4989 0.7540 0.7695 -0.1661 0.1793  -0.1873 85  VAL A O   
704  C CB  . VAL A 88  ? 0.5317 0.8959 0.9139 -0.1840 0.1554  -0.2293 85  VAL A CB  
705  C CG1 . VAL A 88  ? 0.5663 0.9076 0.9290 -0.1815 0.1308  -0.2318 85  VAL A CG1 
706  C CG2 . VAL A 88  ? 0.5576 0.9812 1.0020 -0.1931 0.1544  -0.2498 85  VAL A CG2 
707  N N   . GLU A 89  ? 0.5444 0.7779 0.8380 -0.2011 0.1860  -0.1937 86  GLU A N   
708  C CA  . GLU A 89  ? 0.5740 0.7559 0.8135 -0.1893 0.1813  -0.1789 86  GLU A CA  
709  C C   . GLU A 89  ? 0.5557 0.7148 0.7903 -0.1994 0.1701  -0.1821 86  GLU A C   
710  O O   . GLU A 89  ? 0.5421 0.7037 0.8033 -0.2204 0.1781  -0.1905 86  GLU A O   
711  C CB  . GLU A 89  ? 0.6737 0.8146 0.8782 -0.1882 0.2091  -0.1629 86  GLU A CB  
712  C CG  . GLU A 89  ? 0.7586 0.8482 0.9078 -0.1728 0.1998  -0.1504 86  GLU A CG  
713  C CD  . GLU A 89  ? 0.9594 1.0016 1.0627 -0.1649 0.2234  -0.1352 86  GLU A CD  
714  O OE1 . GLU A 89  ? 1.0740 1.0756 1.1329 -0.1500 0.2131  -0.1271 86  GLU A OE1 
715  O OE2 . GLU A 89  ? 0.9549 1.0008 1.0669 -0.1721 0.2523  -0.1315 86  GLU A OE2 
716  N N   . LEU A 90  ? 0.5188 0.6562 0.7214 -0.1838 0.1511  -0.1757 87  LEU A N   
717  C CA  . LEU A 90  ? 0.5790 0.6924 0.7710 -0.1889 0.1420  -0.1769 87  LEU A CA  
718  C C   . LEU A 90  ? 0.5228 0.5989 0.6708 -0.1721 0.1345  -0.1626 87  LEU A C   
719  O O   . LEU A 90  ? 0.4846 0.5652 0.6211 -0.1550 0.1243  -0.1565 87  LEU A O   
720  C CB  . LEU A 90  ? 0.6893 0.8352 0.9098 -0.1894 0.1210  -0.1922 87  LEU A CB  
721  C CG  . LEU A 90  ? 0.7435 0.9163 0.9660 -0.1695 0.1005  -0.1933 87  LEU A CG  
722  C CD1 . LEU A 90  ? 0.8447 0.9914 1.0356 -0.1540 0.0883  -0.1813 87  LEU A CD1 
723  C CD2 . LEU A 90  ? 0.7764 0.9874 1.0322 -0.1709 0.0861  -0.2119 87  LEU A CD2 
724  N N   . VAL A 91  ? 0.5136 0.5512 0.6387 -0.1778 0.1404  -0.1581 88  VAL A N   
725  C CA  . VAL A 91  ? 0.5042 0.5055 0.5899 -0.1626 0.1341  -0.1460 88  VAL A CA  
726  C C   . VAL A 91  ? 0.5169 0.5073 0.5983 -0.1632 0.1231  -0.1490 88  VAL A C   
727  O O   . VAL A 91  ? 0.5333 0.5143 0.6214 -0.1784 0.1294  -0.1566 88  VAL A O   
728  C CB  . VAL A 91  ? 0.6017 0.5590 0.6518 -0.1629 0.1549  -0.1359 88  VAL A CB  
729  C CG1 . VAL A 91  ? 0.6814 0.5988 0.6900 -0.1466 0.1471  -0.1261 88  VAL A CG1 
730  C CG2 . VAL A 91  ? 0.6321 0.5986 0.6800 -0.1564 0.1654  -0.1321 88  VAL A CG2 
731  N N   . LEU A 92  ? 0.4854 0.4775 0.5575 -0.1460 0.1066  -0.1430 89  LEU A N   
732  C CA  . LEU A 92  ? 0.4989 0.4821 0.5633 -0.1406 0.0968  -0.1433 89  LEU A CA  
733  C C   . LEU A 92  ? 0.4791 0.4385 0.5169 -0.1236 0.0917  -0.1304 89  LEU A C   
734  O O   . LEU A 92  ? 0.4735 0.4338 0.5079 -0.1147 0.0888  -0.1237 89  LEU A O   
735  C CB  . LEU A 92  ? 0.4744 0.4957 0.5643 -0.1337 0.0819  -0.1491 89  LEU A CB  
736  C CG  . LEU A 92  ? 0.4432 0.4948 0.5628 -0.1457 0.0808  -0.1649 89  LEU A CG  
737  C CD1 . LEU A 92  ? 0.4658 0.5479 0.5995 -0.1320 0.0651  -0.1684 89  LEU A CD1 
738  C CD2 . LEU A 92  ? 0.4871 0.5220 0.6068 -0.1606 0.0850  -0.1762 89  LEU A CD2 
739  N N   . TRP A 93  ? 0.4742 0.4119 0.4935 -0.1180 0.0893  -0.1280 90  TRP A N   
740  C CA  . TRP A 93  ? 0.5021 0.4248 0.5034 -0.1002 0.0827  -0.1169 90  TRP A CA  
741  C C   . TRP A 93  ? 0.4782 0.4140 0.4863 -0.0896 0.0740  -0.1153 90  TRP A C   
742  O O   . TRP A 93  ? 0.4712 0.4129 0.4838 -0.0953 0.0739  -0.1240 90  TRP A O   
743  C CB  . TRP A 93  ? 0.5336 0.4096 0.4958 -0.0977 0.0916  -0.1128 90  TRP A CB  
744  C CG  . TRP A 93  ? 0.5348 0.3804 0.4739 -0.1016 0.0974  -0.1161 90  TRP A CG  
745  C CD1 . TRP A 93  ? 0.5608 0.4008 0.5049 -0.1189 0.1040  -0.1263 90  TRP A CD1 
746  C CD2 . TRP A 93  ? 0.5688 0.3823 0.4751 -0.0864 0.0953  -0.1101 90  TRP A CD2 
747  N NE1 . TRP A 93  ? 0.6177 0.4205 0.5316 -0.1159 0.1056  -0.1270 90  TRP A NE1 
748  C CE2 . TRP A 93  ? 0.6050 0.3909 0.4931 -0.0950 0.1012  -0.1166 90  TRP A CE2 
749  C CE3 . TRP A 93  ? 0.5852 0.3917 0.4779 -0.0657 0.0874  -0.1012 90  TRP A CE3 
750  C CZ2 . TRP A 93  ? 0.6634 0.4123 0.5146 -0.0818 0.1006  -0.1134 90  TRP A CZ2 
751  C CZ3 . TRP A 93  ? 0.6302 0.4052 0.4905 -0.0524 0.0870  -0.0982 90  TRP A CZ3 
752  C CH2 . TRP A 93  ? 0.6732 0.4183 0.5101 -0.0597 0.0941  -0.1037 90  TRP A CH2 
753  N N   . ASN A 94  ? 0.4632 0.4037 0.4731 -0.0729 0.0667  -0.1048 91  ASN A N   
754  C CA  . ASN A 94  ? 0.4373 0.3935 0.4557 -0.0604 0.0622  -0.1002 91  ASN A CA  
755  C C   . ASN A 94  ? 0.4690 0.3967 0.4574 -0.0499 0.0648  -0.0978 91  ASN A C   
756  O O   . ASN A 94  ? 0.4629 0.4009 0.4542 -0.0344 0.0630  -0.0910 91  ASN A O   
757  C CB  . ASN A 94  ? 0.4436 0.4273 0.4905 -0.0489 0.0553  -0.0889 91  ASN A CB  
758  C CG  . ASN A 94  ? 0.4325 0.4047 0.4767 -0.0394 0.0508  -0.0811 91  ASN A CG  
759  O OD1 . ASN A 94  ? 0.4596 0.4010 0.4750 -0.0397 0.0530  -0.0840 91  ASN A OD1 
760  N ND2 . ASN A 94  ? 0.4364 0.4323 0.5117 -0.0305 0.0441  -0.0716 91  ASN A ND2 
761  N N   . GLY A 95  ? 0.4914 0.3815 0.4491 -0.0562 0.0706  -0.1020 92  GLY A N   
762  C CA  . GLY A 95  ? 0.5437 0.4005 0.4671 -0.0461 0.0728  -0.1012 92  GLY A CA  
763  C C   . GLY A 95  ? 0.6148 0.4612 0.5255 -0.0267 0.0696  -0.0907 92  GLY A C   
764  O O   . GLY A 95  ? 0.6363 0.4544 0.5156 -0.0148 0.0711  -0.0896 92  GLY A O   
765  N N   . GLU A 96  ? 0.5788 0.4490 0.5155 -0.0220 0.0634  -0.0843 93  GLU A N   
766  C CA  . GLU A 96  ? 0.6448 0.5105 0.5782 -0.0038 0.0567  -0.0770 93  GLU A CA  
767  C C   . GLU A 96  ? 0.6915 0.5293 0.6029 -0.0060 0.0551  -0.0802 93  GLU A C   
768  O O   . GLU A 96  ? 0.6464 0.4954 0.5732 -0.0162 0.0534  -0.0827 93  GLU A O   
769  C CB  . GLU A 96  ? 0.6411 0.5516 0.6227 0.0045  0.0486  -0.0683 93  GLU A CB  
770  C CG  . GLU A 96  ? 0.6836 0.5959 0.6736 0.0215  0.0385  -0.0632 93  GLU A CG  
771  C CD  . GLU A 96  ? 0.7941 0.6838 0.7528 0.0397  0.0408  -0.0610 93  GLU A CD  
772  O OE1 . GLU A 96  ? 0.8435 0.6987 0.7670 0.0476  0.0370  -0.0652 93  GLU A OE1 
773  O OE2 . GLU A 96  ? 0.7774 0.6821 0.7436 0.0488  0.0467  -0.0548 93  GLU A OE2 
774  N N   . GLU A 97  ? 0.8383 0.6372 0.7088 0.0067  0.0559  -0.0799 94  GLU A N   
775  C CA  . GLU A 97  ? 0.8812 0.6434 0.7173 0.0108  0.0560  -0.0821 94  GLU A CA  
776  C C   . GLU A 97  ? 0.7769 0.5562 0.6325 0.0255  0.0388  -0.0809 94  GLU A C   
777  O O   . GLU A 97  ? 0.8023 0.5730 0.6516 0.0230  0.0364  -0.0839 94  GLU A O   
778  C CB  . GLU A 97  ? 0.9777 0.6911 0.7608 0.0261  0.0598  -0.0816 94  GLU A CB  
779  C CG  . GLU A 97  ? 1.0734 0.7512 0.8241 0.0129  0.0756  -0.0844 94  GLU A CG  
780  C CD  . GLU A 97  ? 1.2108 0.8594 0.9428 -0.0079 0.0913  -0.0877 94  GLU A CD  
781  O OE1 . GLU A 97  ? 1.2938 0.9486 1.0323 -0.0097 0.0910  -0.0870 94  GLU A OE1 
782  O OE2 . GLU A 97  ? 1.1525 0.7704 0.8635 -0.0215 0.1039  -0.0909 94  GLU A OE2 
783  N N   . ASP A 98  ? 0.8071 0.6098 0.6869 0.0422  0.0266  -0.0771 95  ASP A N   
784  C CA  . ASP A 98  ? 0.7943 0.6123 0.6968 0.0583  0.0066  -0.0780 95  ASP A CA  
785  C C   . ASP A 98  ? 0.6884 0.5513 0.6494 0.0478  -0.0032 -0.0771 95  ASP A C   
786  O O   . ASP A 98  ? 0.6450 0.5450 0.6479 0.0400  0.0006  -0.0710 95  ASP A O   
787  C CB  . ASP A 98  ? 0.8315 0.6602 0.7431 0.0791  -0.0004 -0.0742 95  ASP A CB  
788  C CG  . ASP A 98  ? 0.9258 0.7702 0.8635 0.0985  -0.0237 -0.0774 95  ASP A CG  
789  O OD1 . ASP A 98  ? 0.8612 0.7038 0.8060 0.0973  -0.0373 -0.0835 95  ASP A OD1 
790  O OD2 . ASP A 98  ? 0.9862 0.8447 0.9374 0.1161  -0.0293 -0.0746 95  ASP A OD2 
791  N N   . PRO A 99  ? 0.7612 0.6181 0.7230 0.0500  -0.0167 -0.0830 96  PRO A N   
792  C CA  . PRO A 99  ? 0.7151 0.6089 0.7300 0.0417  -0.0289 -0.0832 96  PRO A CA  
793  C C   . PRO A 99  ? 0.6971 0.6307 0.7711 0.0492  -0.0427 -0.0785 96  PRO A C   
794  O O   . PRO A 99  ? 0.6953 0.6632 0.8209 0.0390  -0.0469 -0.0746 96  PRO A O   
795  C CB  . PRO A 99  ? 0.7696 0.6371 0.7594 0.0507  -0.0437 -0.0923 96  PRO A CB  
796  C CG  . PRO A 99  ? 0.8270 0.6440 0.7468 0.0554  -0.0281 -0.0941 96  PRO A CG  
797  C CD  . PRO A 99  ? 0.8450 0.6543 0.7511 0.0619  -0.0196 -0.0896 96  PRO A CD  
798  N N   . LEU A 100 ? 0.6790 0.6075 0.7466 0.0674  -0.0485 -0.0782 97  LEU A N   
799  C CA  . LEU A 100 ? 0.6572 0.6265 0.7858 0.0754  -0.0595 -0.0732 97  LEU A CA  
800  C C   . LEU A 100 ? 0.6500 0.6499 0.8070 0.0671  -0.0388 -0.0597 97  LEU A C   
801  O O   . LEU A 100 ? 0.6445 0.6841 0.8610 0.0691  -0.0411 -0.0516 97  LEU A O   
802  C CB  . LEU A 100 ? 0.7304 0.6851 0.8400 0.1007  -0.0723 -0.0784 97  LEU A CB  
803  C CG  . LEU A 100 ? 0.7807 0.6996 0.8534 0.1159  -0.0944 -0.0925 97  LEU A CG  
804  C CD1 . LEU A 100 ? 0.8180 0.7356 0.8906 0.1436  -0.1129 -0.0985 97  LEU A CD1 
805  C CD2 . LEU A 100 ? 0.7927 0.7255 0.9021 0.1076  -0.1139 -0.0991 97  LEU A CD2 
806  N N   . LYS A 101 ? 0.6326 0.6131 0.7478 0.0588  -0.0185 -0.0574 98  LYS A N   
807  C CA  . LYS A 101 ? 0.6375 0.6406 0.7688 0.0555  -0.0004 -0.0463 98  LYS A CA  
808  C C   . LYS A 101 ? 0.5764 0.5861 0.7116 0.0360  0.0093  -0.0455 98  LYS A C   
809  O O   . LYS A 101 ? 0.6055 0.6190 0.7311 0.0336  0.0244  -0.0406 98  LYS A O   
810  C CB  . LYS A 101 ? 0.7360 0.7127 0.8183 0.0681  0.0110  -0.0457 98  LYS A CB  
811  C CG  . LYS A 101 ? 0.8480 0.8238 0.9302 0.0912  0.0015  -0.0455 98  LYS A CG  
812  C CD  . LYS A 101 ? 0.9588 0.9084 0.9925 0.1070  0.0124  -0.0440 98  LYS A CD  
813  C CE  . LYS A 101 ? 1.0607 0.9537 1.0230 0.1017  0.0176  -0.0531 98  LYS A CE  
814  N NZ  . LYS A 101 ? 1.0851 0.9495 1.0010 0.1182  0.0261  -0.0520 98  LYS A NZ  
815  N N   . GLY A 102 ? 0.4604 0.4709 0.6077 0.0247  -0.0008 -0.0513 99  GLY A N   
816  C CA  . GLY A 102 ? 0.4345 0.4547 0.5887 0.0086  0.0065  -0.0513 99  GLY A CA  
817  C C   . GLY A 102 ? 0.4567 0.4479 0.5624 -0.0014 0.0153  -0.0605 99  GLY A C   
818  O O   . GLY A 102 ? 0.4475 0.4486 0.5560 -0.0126 0.0234  -0.0615 99  GLY A O   
819  N N   . GLY A 103 ? 0.5092 0.4648 0.5718 0.0031  0.0147  -0.0671 100 GLY A N   
820  C CA  . GLY A 103 ? 0.4736 0.4012 0.4963 -0.0085 0.0255  -0.0746 100 GLY A CA  
821  C C   . GLY A 103 ? 0.4772 0.4159 0.5141 -0.0204 0.0227  -0.0791 100 GLY A C   
822  O O   . GLY A 103 ? 0.4628 0.4070 0.5154 -0.0151 0.0086  -0.0799 100 GLY A O   
823  N N   . LEU A 104 ? 0.4530 0.3947 0.4845 -0.0350 0.0343  -0.0833 101 LEU A N   
824  C CA  . LEU A 104 ? 0.4602 0.4164 0.5063 -0.0443 0.0323  -0.0875 101 LEU A CA  
825  C C   . LEU A 104 ? 0.5000 0.4482 0.5289 -0.0592 0.0471  -0.0949 101 LEU A C   
826  O O   . LEU A 104 ? 0.4832 0.4267 0.5038 -0.0654 0.0562  -0.0971 101 LEU A O   
827  C CB  . LEU A 104 ? 0.4753 0.4687 0.5639 -0.0446 0.0262  -0.0826 101 LEU A CB  
828  C CG  . LEU A 104 ? 0.4946 0.5049 0.6036 -0.0492 0.0189  -0.0853 101 LEU A CG  
829  C CD1 . LEU A 104 ? 0.4676 0.4708 0.5848 -0.0402 0.0022  -0.0847 101 LEU A CD1 
830  C CD2 . LEU A 104 ? 0.4576 0.4982 0.5985 -0.0507 0.0190  -0.0803 101 LEU A CD2 
831  N N   A SER A 105 ? 0.4808 0.4273 0.5060 -0.0639 0.0486  -0.0992 102 SER A N   
832  N N   B SER A 105 ? 0.4721 0.4184 0.4971 -0.0640 0.0488  -0.0992 102 SER A N   
833  C CA  A SER A 105 ? 0.4793 0.4250 0.4982 -0.0787 0.0635  -0.1060 102 SER A CA  
834  C CA  B SER A 105 ? 0.4653 0.4115 0.4847 -0.0790 0.0636  -0.1060 102 SER A CA  
835  C C   A SER A 105 ? 0.4444 0.4223 0.4904 -0.0823 0.0589  -0.1098 102 SER A C   
836  C C   B SER A 105 ? 0.4361 0.4143 0.4825 -0.0824 0.0588  -0.1097 102 SER A C   
837  O O   A SER A 105 ? 0.4140 0.3999 0.4703 -0.0727 0.0456  -0.1071 102 SER A O   
838  O O   B SER A 105 ? 0.4064 0.3929 0.4635 -0.0727 0.0454  -0.1070 102 SER A O   
839  C CB  A SER A 105 ? 0.5509 0.4590 0.5327 -0.0791 0.0763  -0.1061 102 SER A CB  
840  C CB  B SER A 105 ? 0.5257 0.4347 0.5085 -0.0805 0.0773  -0.1064 102 SER A CB  
841  O OG  A SER A 105 ? 0.5781 0.4526 0.5308 -0.0752 0.0812  -0.1030 102 SER A OG  
842  O OG  B SER A 105 ? 0.5111 0.4100 0.4810 -0.0684 0.0709  -0.1048 102 SER A OG  
843  N N   . LEU A 106 ? 0.4407 0.4363 0.4993 -0.0956 0.0682  -0.1172 103 LEU A N   
844  C CA  . LEU A 106 ? 0.4063 0.4332 0.4884 -0.0980 0.0649  -0.1224 103 LEU A CA  
845  C C   . LEU A 106 ? 0.4210 0.4466 0.4984 -0.1087 0.0808  -0.1287 103 LEU A C   
846  O O   . LEU A 106 ? 0.4701 0.4851 0.5431 -0.1215 0.0947  -0.1324 103 LEU A O   
847  C CB  . LEU A 106 ? 0.4297 0.4843 0.5352 -0.1001 0.0594  -0.1263 103 LEU A CB  
848  C CG  . LEU A 106 ? 0.4688 0.5566 0.5976 -0.0983 0.0528  -0.1317 103 LEU A CG  
849  C CD1 . LEU A 106 ? 0.5105 0.6145 0.6518 -0.0913 0.0447  -0.1302 103 LEU A CD1 
850  C CD2 . LEU A 106 ? 0.5603 0.6650 0.6993 -0.1103 0.0622  -0.1443 103 LEU A CD2 
851  N N   . ASP A 107 ? 0.3957 0.4299 0.4741 -0.1026 0.0795  -0.1293 104 ASP A N   
852  C CA  . ASP A 107 ? 0.4534 0.4910 0.5301 -0.1100 0.0971  -0.1335 104 ASP A CA  
853  C C   . ASP A 107 ? 0.4225 0.4984 0.5249 -0.1072 0.0903  -0.1403 104 ASP A C   
854  O O   . ASP A 107 ? 0.4391 0.5170 0.5376 -0.0930 0.0762  -0.1379 104 ASP A O   
855  C CB  . ASP A 107 ? 0.5332 0.5346 0.5725 -0.0998 0.1063  -0.1266 104 ASP A CB  
856  C CG  . ASP A 107 ? 0.6863 0.6875 0.7219 -0.1075 0.1318  -0.1277 104 ASP A CG  
857  O OD1 . ASP A 107 ? 0.6829 0.7178 0.7421 -0.1089 0.1340  -0.1335 104 ASP A OD1 
858  O OD2 . ASP A 107 ? 0.8624 0.8289 0.8710 -0.1108 0.1507  -0.1219 104 ASP A OD2 
859  N N   . TYR A 108 ? 0.4085 0.5135 0.5376 -0.1202 0.0990  -0.1499 105 TYR A N   
860  C CA  . TYR A 108 ? 0.3731 0.5171 0.5273 -0.1167 0.0932  -0.1585 105 TYR A CA  
861  C C   . TYR A 108 ? 0.4329 0.5918 0.5989 -0.1254 0.1143  -0.1635 105 TYR A C   
862  O O   . TYR A 108 ? 0.4494 0.6048 0.6255 -0.1425 0.1310  -0.1660 105 TYR A O   
863  C CB  . TYR A 108 ? 0.3787 0.5500 0.5592 -0.1215 0.0820  -0.1679 105 TYR A CB  
864  C CG  . TYR A 108 ? 0.3377 0.5495 0.5430 -0.1161 0.0742  -0.1789 105 TYR A CG  
865  C CD1 . TYR A 108 ? 0.3615 0.5799 0.5609 -0.0993 0.0611  -0.1760 105 TYR A CD1 
866  C CD2 . TYR A 108 ? 0.4009 0.6440 0.6368 -0.1275 0.0787  -0.1937 105 TYR A CD2 
867  C CE1 . TYR A 108 ? 0.3351 0.5878 0.5525 -0.0917 0.0536  -0.1864 105 TYR A CE1 
868  C CE2 . TYR A 108 ? 0.3859 0.6679 0.6444 -0.1198 0.0696  -0.2057 105 TYR A CE2 
869  C CZ  . TYR A 108 ? 0.3956 0.6815 0.6420 -0.1008 0.0575  -0.2015 105 TYR A CZ  
870  O OH  . TYR A 108 ? 0.3788 0.7003 0.6429 -0.0908 0.0483  -0.2136 105 TYR A OH  
871  N N   . GLU A 109 ? 0.4031 0.5768 0.5679 -0.1132 0.1145  -0.1642 106 GLU A N   
872  C CA  . GLU A 109 ? 0.4652 0.6573 0.6439 -0.1192 0.1374  -0.1676 106 GLU A CA  
873  C C   . GLU A 109 ? 0.3851 0.6188 0.5850 -0.1081 0.1284  -0.1768 106 GLU A C   
874  O O   . GLU A 109 ? 0.3945 0.6254 0.5801 -0.0909 0.1083  -0.1757 106 GLU A O   
875  C CB  . GLU A 109 ? 0.5664 0.7191 0.7052 -0.1109 0.1554  -0.1550 106 GLU A CB  
876  C CG  . GLU A 109 ? 0.7338 0.8990 0.8850 -0.1188 0.1872  -0.1542 106 GLU A CG  
877  C CD  . GLU A 109 ? 0.8920 1.0117 0.9957 -0.1076 0.2087  -0.1401 106 GLU A CD  
878  O OE1 . GLU A 109 ? 0.8780 0.9566 0.9382 -0.0920 0.1943  -0.1332 106 GLU A OE1 
879  O OE2 . GLU A 109 ? 0.9739 1.0988 1.0850 -0.1138 0.2404  -0.1359 106 GLU A OE2 
880  N N   . ALA A 110 ? 0.4060 0.6789 0.6432 -0.1184 0.1427  -0.1866 107 ALA A N   
881  C CA  . ALA A 110 ? 0.4150 0.7311 0.6741 -0.1066 0.1358  -0.1969 107 ALA A CA  
882  C C   . ALA A 110 ? 0.4531 0.7943 0.7365 -0.1138 0.1651  -0.1984 107 ALA A C   
883  O O   . ALA A 110 ? 0.4859 0.8512 0.8112 -0.1355 0.1781  -0.2062 107 ALA A O   
884  C CB  . ALA A 110 ? 0.4351 0.7847 0.7263 -0.1102 0.1153  -0.2119 107 ALA A CB  
885  N N   . SER A 111 ? 0.4789 0.8137 0.7368 -0.0949 0.1754  -0.1910 108 SER A N   
886  C CA  . SER A 111 ? 0.5004 0.8542 0.7756 -0.0986 0.2088  -0.1881 108 SER A CA  
887  C C   . SER A 111 ? 0.5201 0.9151 0.8077 -0.0787 0.2096  -0.1948 108 SER A C   
888  O O   . SER A 111 ? 0.5829 1.0099 0.9015 -0.0837 0.2374  -0.1954 108 SER A O   
889  C CB  . SER A 111 ? 0.5861 0.8867 0.8093 -0.0901 0.2287  -0.1702 108 SER A CB  
890  O OG  . SER A 111 ? 0.5727 0.8503 0.7480 -0.0596 0.2125  -0.1658 108 SER A OG  
891  N N   . GLY A 112 ? 0.5019 0.8934 0.7641 -0.0554 0.1815  -0.1985 109 GLY A N   
892  C CA  . GLY A 112 ? 0.4963 0.9194 0.7604 -0.0322 0.1811  -0.2042 109 GLY A CA  
893  C C   . GLY A 112 ? 0.5070 0.8870 0.7100 -0.0050 0.1848  -0.1916 109 GLY A C   
894  O O   . GLY A 112 ? 0.4866 0.8823 0.6785 0.0189  0.1851  -0.1943 109 GLY A O   
895  N N   . ARG A 113 ? 0.4844 0.8088 0.6463 -0.0070 0.1859  -0.1791 110 ARG A N   
896  C CA  . ARG A 113 ? 0.5048 0.7790 0.6038 0.0194  0.1836  -0.1688 110 ARG A CA  
897  C C   . ARG A 113 ? 0.4692 0.7012 0.5407 0.0211  0.1501  -0.1675 110 ARG A C   
898  O O   . ARG A 113 ? 0.4600 0.6870 0.5495 -0.0008 0.1453  -0.1669 110 ARG A O   
899  C CB  . ARG A 113 ? 0.5582 0.8081 0.6367 0.0172  0.2211  -0.1552 110 ARG A CB  
900  C CG  . ARG A 113 ? 0.6002 0.8958 0.7118 0.0164  0.2568  -0.1551 110 ARG A CG  
901  C CD  . ARG A 113 ? 0.6675 0.9462 0.7749 0.0056  0.3005  -0.1405 110 ARG A CD  
902  N NE  . ARG A 113 ? 0.6689 0.9445 0.8091 -0.0295 0.3042  -0.1408 110 ARG A NE  
903  C CZ  . ARG A 113 ? 0.6980 1.0164 0.9032 -0.0592 0.3256  -0.1453 110 ARG A CZ  
904  N NH1 . ARG A 113 ? 0.7035 1.0810 0.9575 -0.0592 0.3404  -0.1525 110 ARG A NH1 
905  N NH2 . ARG A 113 ? 0.7433 1.0493 0.9692 -0.0884 0.3262  -0.1458 110 ARG A NH2 
906  N N   . ALA A 114 ? 0.4730 0.6748 0.5027 0.0478  0.1274  -0.1674 111 ALA A N   
907  C CA  . ALA A 114 ? 0.4837 0.6498 0.4955 0.0502  0.0941  -0.1670 111 ALA A CA  
908  C C   . ALA A 114 ? 0.4910 0.6200 0.4884 0.0377  0.0974  -0.1584 111 ALA A C   
909  O O   . ALA A 114 ? 0.4710 0.5953 0.4849 0.0235  0.0805  -0.1585 111 ALA A O   
910  C CB  . ALA A 114 ? 0.5150 0.6498 0.4834 0.0812  0.0723  -0.1687 111 ALA A CB  
911  N N   . VAL A 115 ? 0.5696 0.6716 0.5336 0.0456  0.1206  -0.1504 112 VAL A N   
912  C CA  . VAL A 115 ? 0.5851 0.6457 0.5253 0.0395  0.1244  -0.1423 112 VAL A CA  
913  C C   . VAL A 115 ? 0.5694 0.6495 0.5507 0.0070  0.1342  -0.1415 112 VAL A C   
914  O O   . VAL A 115 ? 0.5941 0.6481 0.5678 0.0000  0.1229  -0.1383 112 VAL A O   
915  C CB  . VAL A 115 ? 0.6535 0.6817 0.5470 0.0561  0.1535  -0.1328 112 VAL A CB  
916  C CG1 . VAL A 115 ? 0.6592 0.7234 0.5813 0.0423  0.1948  -0.1291 112 VAL A CG1 
917  C CG2 . VAL A 115 ? 0.7138 0.6915 0.5718 0.0561  0.1549  -0.1249 112 VAL A CG2 
918  N N   . SER A 116 ? 0.5532 0.6792 0.5784 -0.0109 0.1540  -0.1457 113 SER A N   
919  C CA  . SER A 116 ? 0.5308 0.6738 0.5939 -0.0404 0.1628  -0.1472 113 SER A CA  
920  C C   . SER A 116 ? 0.4486 0.6375 0.5588 -0.0514 0.1448  -0.1592 113 SER A C   
921  O O   . SER A 116 ? 0.4521 0.6734 0.6034 -0.0721 0.1556  -0.1656 113 SER A O   
922  C CB  . SER A 116 ? 0.5491 0.6984 0.6233 -0.0541 0.2014  -0.1422 113 SER A CB  
923  O OG  . SER A 116 ? 0.5730 0.7487 0.6528 -0.0417 0.2185  -0.1432 113 SER A OG  
924  N N   . SER A 117 ? 0.4234 0.6107 0.5249 -0.0362 0.1160  -0.1624 114 SER A N   
925  C CA  . SER A 117 ? 0.3583 0.5774 0.4914 -0.0404 0.0963  -0.1715 114 SER A CA  
926  C C   . SER A 117 ? 0.3383 0.5266 0.4547 -0.0351 0.0708  -0.1663 114 SER A C   
927  O O   . SER A 117 ? 0.3763 0.5545 0.4783 -0.0182 0.0516  -0.1664 114 SER A O   
928  C CB  . SER A 117 ? 0.3653 0.6159 0.5071 -0.0248 0.0907  -0.1798 114 SER A CB  
929  O OG  . SER A 117 ? 0.3789 0.6643 0.5441 -0.0300 0.1159  -0.1847 114 SER A OG  
930  N N   . ARG A 118 ? 0.3536 0.5263 0.4731 -0.0496 0.0716  -0.1616 115 ARG A N   
931  C CA  . ARG A 118 ? 0.3770 0.5228 0.4854 -0.0449 0.0508  -0.1553 115 ARG A CA  
932  C C   . ARG A 118 ? 0.3624 0.5035 0.4825 -0.0607 0.0531  -0.1520 115 ARG A C   
933  O O   . ARG A 118 ? 0.3622 0.5125 0.4930 -0.0756 0.0698  -0.1547 115 ARG A O   
934  C CB  . ARG A 118 ? 0.4394 0.5438 0.5102 -0.0309 0.0468  -0.1490 115 ARG A CB  
935  C CG  . ARG A 118 ? 0.5337 0.6138 0.5838 -0.0371 0.0674  -0.1436 115 ARG A CG  
936  C CD  . ARG A 118 ? 0.7359 0.7720 0.7425 -0.0177 0.0602  -0.1389 115 ARG A CD  
937  N NE  . ARG A 118 ? 0.9029 0.9089 0.8839 -0.0212 0.0783  -0.1325 115 ARG A NE  
938  C CZ  . ARG A 118 ? 0.9426 0.9504 0.9191 -0.0302 0.1090  -0.1298 115 ARG A CZ  
939  N NH1 . ARG A 118 ? 1.0742 1.0474 1.0233 -0.0324 0.1246  -0.1229 115 ARG A NH1 
940  N NH2 . ARG A 118 ? 1.0469 1.0909 1.0483 -0.0371 0.1245  -0.1341 115 ARG A NH2 
941  N N   . LEU A 119 ? 0.3371 0.4617 0.4552 -0.0567 0.0357  -0.1460 116 LEU A N   
942  C CA  . LEU A 119 ? 0.3232 0.4412 0.4487 -0.0666 0.0358  -0.1413 116 LEU A CA  
943  C C   . LEU A 119 ? 0.3367 0.4212 0.4450 -0.0593 0.0254  -0.1330 116 LEU A C   
944  O O   . LEU A 119 ? 0.3601 0.4360 0.4673 -0.0480 0.0084  -0.1311 116 LEU A O   
945  C CB  . LEU A 119 ? 0.3411 0.4818 0.4900 -0.0667 0.0257  -0.1423 116 LEU A CB  
946  C CG  . LEU A 119 ? 0.3713 0.5056 0.5262 -0.0719 0.0246  -0.1360 116 LEU A CG  
947  C CD1 . LEU A 119 ? 0.3743 0.5114 0.5289 -0.0847 0.0389  -0.1413 116 LEU A CD1 
948  C CD2 . LEU A 119 ? 0.4134 0.5639 0.5842 -0.0659 0.0153  -0.1339 116 LEU A CD2 
949  N N   . GLN A 120 ? 0.3995 0.4645 0.4951 -0.0651 0.0344  -0.1292 117 GLN A N   
950  C CA  . GLN A 120 ? 0.4586 0.4942 0.5390 -0.0560 0.0228  -0.1231 117 GLN A CA  
951  C C   . GLN A 120 ? 0.4138 0.4447 0.5000 -0.0627 0.0254  -0.1180 117 GLN A C   
952  O O   . GLN A 120 ? 0.4174 0.4526 0.5028 -0.0739 0.0405  -0.1198 117 GLN A O   
953  C CB  . GLN A 120 ? 0.5881 0.5931 0.6312 -0.0467 0.0295  -0.1236 117 GLN A CB  
954  C CG  . GLN A 120 ? 0.8126 0.7863 0.8369 -0.0318 0.0118  -0.1208 117 GLN A CG  
955  C CD  . GLN A 120 ? 0.8891 0.8301 0.8700 -0.0152 0.0141  -0.1226 117 GLN A CD  
956  O OE1 . GLN A 120 ? 0.9747 0.9174 0.9404 -0.0150 0.0319  -0.1240 117 GLN A OE1 
957  N NE2 . GLN A 120 ? 0.8282 0.7401 0.7897 0.0010  -0.0047 -0.1230 117 GLN A NE2 
958  N N   . LEU A 121 ? 0.4204 0.4461 0.5177 -0.0556 0.0094  -0.1123 118 LEU A N   
959  C CA  . LEU A 121 ? 0.4137 0.4342 0.5153 -0.0570 0.0103  -0.1063 118 LEU A CA  
960  C C   . LEU A 121 ? 0.4195 0.4095 0.4990 -0.0456 0.0016  -0.1051 118 LEU A C   
961  O O   . LEU A 121 ? 0.4250 0.4094 0.5099 -0.0356 -0.0162 -0.1062 118 LEU A O   
962  C CB  . LEU A 121 ? 0.5009 0.5435 0.6373 -0.0563 0.0013  -0.0997 118 LEU A CB  
963  C CG  . LEU A 121 ? 0.5298 0.5983 0.6813 -0.0625 0.0089  -0.1007 118 LEU A CG  
964  C CD1 . LEU A 121 ? 0.5433 0.6258 0.7221 -0.0585 0.0042  -0.0907 118 LEU A CD1 
965  C CD2 . LEU A 121 ? 0.5943 0.6627 0.7315 -0.0707 0.0241  -0.1055 118 LEU A CD2 
966  N N   . GLU A 122 ? 0.4311 0.3982 0.4828 -0.0458 0.0131  -0.1042 119 GLU A N   
967  C CA  . GLU A 122 ? 0.5166 0.4503 0.5387 -0.0315 0.0055  -0.1042 119 GLU A CA  
968  C C   . GLU A 122 ? 0.4881 0.4106 0.5039 -0.0287 0.0074  -0.0998 119 GLU A C   
969  O O   . GLU A 122 ? 0.5184 0.4437 0.5315 -0.0392 0.0230  -0.0980 119 GLU A O   
970  C CB  . GLU A 122 ? 0.6491 0.5534 0.6271 -0.0302 0.0225  -0.1068 119 GLU A CB  
971  C CG  . GLU A 122 ? 0.8457 0.7599 0.8237 -0.0310 0.0258  -0.1109 119 GLU A CG  
972  C CD  . GLU A 122 ? 0.9448 0.8333 0.8833 -0.0301 0.0485  -0.1109 119 GLU A CD  
973  O OE1 . GLU A 122 ? 0.9896 0.8871 0.9266 -0.0287 0.0541  -0.1135 119 GLU A OE1 
974  O OE2 . GLU A 122 ? 1.0301 0.8889 0.9393 -0.0303 0.0623  -0.1073 119 GLU A OE2 
975  N N   . ASP A 123 ? 0.4301 0.4273 0.4769 -0.0213 0.0983  -0.0233 120 ASP A N   
976  C CA  . ASP A 123 ? 0.4526 0.4694 0.5005 -0.0161 0.0829  -0.0135 120 ASP A CA  
977  C C   . ASP A 123 ? 0.4100 0.4468 0.4638 -0.0186 0.0716  -0.0143 120 ASP A C   
978  O O   . ASP A 123 ? 0.4496 0.4868 0.5039 -0.0134 0.0774  -0.0115 120 ASP A O   
979  C CB  . ASP A 123 ? 0.5149 0.5291 0.5559 -0.0007 0.0882  0.0016  120 ASP A CB  
980  C CG  . ASP A 123 ? 0.5412 0.5786 0.5825 0.0021  0.0726  0.0096  120 ASP A CG  
981  O OD1 . ASP A 123 ? 0.4201 0.4778 0.4672 -0.0018 0.0605  0.0091  120 ASP A OD1 
982  O OD2 . ASP A 123 ? 0.6369 0.6709 0.6714 0.0075  0.0737  0.0158  120 ASP A OD2 
983  N N   . ALA A 124 ? 0.4051 0.4561 0.4622 -0.0261 0.0572  -0.0178 121 ALA A N   
984  C CA  . ALA A 124 ? 0.4112 0.4778 0.4717 -0.0297 0.0475  -0.0188 121 ALA A CA  
985  C C   . ALA A 124 ? 0.3804 0.4610 0.4419 -0.0224 0.0449  -0.0080 121 ALA A C   
986  O O   . ALA A 124 ? 0.3836 0.4753 0.4478 -0.0244 0.0413  -0.0079 121 ALA A O   
987  C CB  . ALA A 124 ? 0.4381 0.5118 0.4986 -0.0368 0.0353  -0.0225 121 ALA A CB  
988  N N   . GLY A 125 ? 0.3954 0.4781 0.4546 -0.0137 0.0471  0.0012  122 GLY A N   
989  C CA  . GLY A 125 ? 0.3774 0.4803 0.4391 -0.0061 0.0443  0.0112  122 GLY A CA  
990  C C   . GLY A 125 ? 0.3932 0.4946 0.4576 0.0009  0.0546  0.0130  122 GLY A C   
991  O O   . GLY A 125 ? 0.4177 0.5396 0.4869 0.0049  0.0518  0.0188  122 GLY A O   
992  N N   A SER A 126 ? 0.4254 0.5025 0.4863 0.0013  0.0674  0.0069  123 SER A N   
993  N N   B SER A 126 ? 0.4111 0.4883 0.4721 0.0015  0.0676  0.0070  123 SER A N   
994  C CA  A SER A 126 ? 0.4769 0.5459 0.5376 0.0071  0.0800  0.0063  123 SER A CA  
995  C CA  B SER A 126 ? 0.4532 0.5231 0.5141 0.0074  0.0798  0.0067  123 SER A CA  
996  C C   A SER A 126 ? 0.4687 0.5498 0.5338 -0.0017 0.0735  -0.0001 123 SER A C   
997  C C   B SER A 126 ? 0.4665 0.5492 0.5319 -0.0016 0.0728  0.0003  123 SER A C   
998  O O   A SER A 126 ? 0.4414 0.5282 0.5083 0.0041  0.0792  0.0027  123 SER A O   
999  O O   B SER A 126 ? 0.4909 0.5815 0.5586 0.0041  0.0773  0.0038  123 SER A O   
1000 C CB  A SER A 126 ? 0.5138 0.5517 0.5679 0.0058  0.0960  -0.0011 123 SER A CB  
1001 C CB  B SER A 126 ? 0.4539 0.4928 0.5084 0.0064  0.0964  -0.0008 123 SER A CB  
1002 O OG  A SER A 126 ? 0.6075 0.6318 0.6556 0.0144  0.1034  0.0061  123 SER A OG  
1003 O OG  B SER A 126 ? 0.4832 0.5168 0.5384 -0.0091 0.0924  -0.0151 123 SER A OG  
1004 N N   . LEU A 127 ? 0.5161 0.6003 0.5818 -0.0144 0.0628  -0.0084 124 LEU A N   
1005 C CA  . LEU A 127 ? 0.5072 0.6016 0.5741 -0.0220 0.0564  -0.0135 124 LEU A CA  
1006 C C   . LEU A 127 ? 0.5072 0.6239 0.5782 -0.0213 0.0473  -0.0050 124 LEU A C   
1007 O O   . LEU A 127 ? 0.4953 0.6221 0.5681 -0.0216 0.0480  -0.0040 124 LEU A O   
1008 C CB  . LEU A 127 ? 0.5298 0.6219 0.5946 -0.0327 0.0481  -0.0227 124 LEU A CB  
1009 C CG  . LEU A 127 ? 0.5088 0.5873 0.5713 -0.0378 0.0554  -0.0348 124 LEU A CG  
1010 C CD1 . LEU A 127 ? 0.4989 0.5848 0.5605 -0.0458 0.0451  -0.0423 124 LEU A CD1 
1011 C CD2 . LEU A 127 ? 0.5535 0.6265 0.6137 -0.0374 0.0666  -0.0401 124 LEU A CD2 
1012 N N   . LEU A 128 ? 0.5992 0.7237 0.6711 -0.0219 0.0392  0.0000  125 LEU A N   
1013 C CA  . LEU A 128 ? 0.6284 0.7751 0.7038 -0.0248 0.0308  0.0057  125 LEU A CA  
1014 C C   . LEU A 128 ? 0.6494 0.8141 0.7311 -0.0161 0.0363  0.0128  125 LEU A C   
1015 O O   . LEU A 128 ? 0.8291 1.0136 0.9151 -0.0211 0.0317  0.0149  125 LEU A O   
1016 C CB  . LEU A 128 ? 0.5974 0.7492 0.6715 -0.0256 0.0239  0.0090  125 LEU A CB  
1017 C CG  . LEU A 128 ? 0.5815 0.7573 0.6583 -0.0320 0.0153  0.0126  125 LEU A CG  
1018 C CD1 . LEU A 128 ? 0.5230 0.6934 0.5959 -0.0454 0.0095  0.0069  125 LEU A CD1 
1019 C CD2 . LEU A 128 ? 0.6662 0.8488 0.7405 -0.0312 0.0102  0.0155  125 LEU A CD2 
1020 N N   . GLN A 129 ? 0.6667 0.8239 0.7485 -0.0031 0.0477  0.0166  126 GLN A N   
1021 C CA  . GLN A 129 ? 0.6484 0.8251 0.7365 0.0077  0.0534  0.0247  126 GLN A CA  
1022 C C   . GLN A 129 ? 0.6125 0.7810 0.7002 0.0080  0.0625  0.0202  126 GLN A C   
1023 O O   . GLN A 129 ? 0.5733 0.7619 0.6673 0.0129  0.0650  0.0251  126 GLN A O   
1024 C CB  . GLN A 129 ? 0.8523 1.0291 0.9397 0.0256  0.0616  0.0346  126 GLN A CB  
1025 C CG  . GLN A 129 ? 0.9676 1.1085 1.0462 0.0325  0.0765  0.0318  126 GLN A CG  
1026 C CD  . GLN A 129 ? 1.1808 1.3204 1.2562 0.0524  0.0860  0.0441  126 GLN A CD  
1027 O OE1 . GLN A 129 ? 1.4159 1.5462 1.4890 0.0670  0.1008  0.0494  126 GLN A OE1 
1028 N NE2 . GLN A 129 ? 1.2172 1.3669 1.2909 0.0544  0.0780  0.0497  126 GLN A NE2 
1029 N N   . VAL A 130 ? 0.4675 0.6096 0.5480 0.0024  0.0676  0.0102  127 VAL A N   
1030 C CA  . VAL A 130 ? 0.4341 0.5694 0.5123 0.0016  0.0763  0.0045  127 VAL A CA  
1031 C C   . VAL A 130 ? 0.3640 0.5099 0.4416 -0.0113 0.0663  -0.0003 127 VAL A C   
1032 O O   . VAL A 130 ? 0.3880 0.5384 0.4649 -0.0116 0.0710  -0.0019 127 VAL A O   
1033 C CB  . VAL A 130 ? 0.4745 0.5795 0.5444 0.0010  0.0886  -0.0051 127 VAL A CB  
1034 C CG1 . VAL A 130 ? 0.5450 0.6340 0.6125 0.0149  0.1023  0.0010  127 VAL A CG1 
1035 C CG2 . VAL A 130 ? 0.5224 0.6170 0.5882 -0.0119 0.0811  -0.0154 127 VAL A CG2 
1036 N N   . PHE A 131 ? 0.3731 0.5200 0.4490 -0.0211 0.0541  -0.0024 128 PHE A N   
1037 C CA  . PHE A 131 ? 0.3861 0.5392 0.4586 -0.0313 0.0465  -0.0051 128 PHE A CA  
1038 C C   . PHE A 131 ? 0.4086 0.5846 0.4873 -0.0324 0.0446  0.0021  128 PHE A C   
1039 O O   . PHE A 131 ? 0.4377 0.6287 0.5229 -0.0315 0.0405  0.0082  128 PHE A O   
1040 C CB  . PHE A 131 ? 0.3628 0.5104 0.4308 -0.0395 0.0356  -0.0074 128 PHE A CB  
1041 C CG  . PHE A 131 ? 0.3353 0.4664 0.3977 -0.0413 0.0351  -0.0160 128 PHE A CG  
1042 C CD1 . PHE A 131 ? 0.3789 0.5040 0.4364 -0.0426 0.0400  -0.0241 128 PHE A CD1 
1043 C CD2 . PHE A 131 ? 0.3675 0.4929 0.4287 -0.0439 0.0283  -0.0168 128 PHE A CD2 
1044 C CE1 . PHE A 131 ? 0.3802 0.4973 0.4338 -0.0460 0.0384  -0.0332 128 PHE A CE1 
1045 C CE2 . PHE A 131 ? 0.3582 0.4740 0.4159 -0.0460 0.0273  -0.0249 128 PHE A CE2 
1046 C CZ  . PHE A 131 ? 0.3556 0.4693 0.4103 -0.0474 0.0320  -0.0333 128 PHE A CZ  
1047 N N   . ASP A 132 ? 0.4236 0.6035 0.4993 -0.0360 0.0473  0.0007  129 ASP A N   
1048 C CA  . ASP A 132 ? 0.4811 0.6832 0.5628 -0.0394 0.0471  0.0063  129 ASP A CA  
1049 C C   . ASP A 132 ? 0.4515 0.6545 0.5288 -0.0523 0.0378  0.0067  129 ASP A C   
1050 O O   . ASP A 132 ? 0.4723 0.6944 0.5557 -0.0584 0.0362  0.0106  129 ASP A O   
1051 C CB  . ASP A 132 ? 0.5047 0.7088 0.5839 -0.0376 0.0558  0.0048  129 ASP A CB  
1052 C CG  . ASP A 132 ? 0.6866 0.8735 0.7517 -0.0436 0.0548  -0.0020 129 ASP A CG  
1053 O OD1 . ASP A 132 ? 0.9111 1.0814 0.9702 -0.0422 0.0540  -0.0085 129 ASP A OD1 
1054 O OD2 . ASP A 132 ? 0.8407 1.0326 0.9007 -0.0495 0.0553  -0.0008 129 ASP A OD2 
1055 N N   . ALA A 133 ? 0.3774 0.5600 0.4438 -0.0565 0.0328  0.0023  130 ALA A N   
1056 C CA  . ALA A 133 ? 0.3513 0.5274 0.4102 -0.0667 0.0262  0.0029  130 ALA A CA  
1057 C C   . ALA A 133 ? 0.3746 0.5344 0.4289 -0.0649 0.0205  -0.0004 130 ALA A C   
1058 O O   . ALA A 133 ? 0.3845 0.5295 0.4285 -0.0651 0.0182  -0.0035 130 ALA A O   
1059 C CB  . ALA A 133 ? 0.4019 0.5699 0.4490 -0.0712 0.0283  0.0026  130 ALA A CB  
1060 N N   . PRO A 134 ? 0.4017 0.5664 0.4635 -0.0623 0.0182  0.0006  131 PRO A N   
1061 C CA  . PRO A 134 ? 0.3735 0.5239 0.4321 -0.0599 0.0144  -0.0026 131 PRO A CA  
1062 C C   . PRO A 134 ? 0.3439 0.4799 0.3926 -0.0657 0.0086  -0.0043 131 PRO A C   
1063 O O   . PRO A 134 ? 0.3701 0.4943 0.4149 -0.0622 0.0070  -0.0083 131 PRO A O   
1064 C CB  . PRO A 134 ? 0.4052 0.5667 0.4723 -0.0561 0.0140  0.0007  131 PRO A CB  
1065 C CG  . PRO A 134 ? 0.4555 0.6405 0.5294 -0.0597 0.0143  0.0057  131 PRO A CG  
1066 C CD  . PRO A 134 ? 0.4047 0.5918 0.4777 -0.0607 0.0194  0.0055  131 PRO A CD  
1067 N N   . ALA A 135 ? 0.3538 0.4898 0.3977 -0.0746 0.0067  -0.0019 132 ALA A N   
1068 C CA  . ALA A 135 ? 0.3779 0.4950 0.4100 -0.0784 0.0035  -0.0030 132 ALA A CA  
1069 C C   . ALA A 135 ? 0.3793 0.4836 0.4016 -0.0727 0.0038  -0.0042 132 ALA A C   
1070 O O   . ALA A 135 ? 0.3610 0.4556 0.3794 -0.0676 0.0010  -0.0068 132 ALA A O   
1071 C CB  . ALA A 135 ? 0.4067 0.5218 0.4328 -0.0904 0.0045  -0.0011 132 ALA A CB  
1072 N N   . SER A 136 ? 0.3488 0.4560 0.3671 -0.0732 0.0072  -0.0023 133 SER A N   
1073 C CA  . SER A 136 ? 0.3441 0.4439 0.3515 -0.0671 0.0071  -0.0029 133 SER A CA  
1074 C C   . SER A 136 ? 0.3348 0.4418 0.3484 -0.0597 0.0056  -0.0093 133 SER A C   
1075 O O   . SER A 136 ? 0.3563 0.4599 0.3633 -0.0543 0.0025  -0.0118 133 SER A O   
1076 C CB  . SER A 136 ? 0.3727 0.4751 0.3734 -0.0694 0.0118  0.0005  133 SER A CB  
1077 O OG  . SER A 136 ? 0.3682 0.4874 0.3807 -0.0699 0.0155  -0.0009 133 SER A OG  
1078 N N   . SER A 137 ? 0.3362 0.4536 0.3618 -0.0592 0.0087  -0.0122 134 SER A N   
1079 C CA  . SER A 137 ? 0.3197 0.4402 0.3498 -0.0549 0.0102  -0.0198 134 SER A CA  
1080 C C   . SER A 137 ? 0.3599 0.4750 0.3925 -0.0532 0.0064  -0.0233 134 SER A C   
1081 O O   . SER A 137 ? 0.3255 0.4429 0.3570 -0.0510 0.0052  -0.0300 134 SER A O   
1082 C CB  . SER A 137 ? 0.3432 0.4698 0.3827 -0.0538 0.0173  -0.0209 134 SER A CB  
1083 O OG  . SER A 137 ? 0.3467 0.4798 0.3838 -0.0546 0.0215  -0.0185 134 SER A OG  
1084 N N   . PHE A 138 ? 0.3271 0.4378 0.3632 -0.0549 0.0048  -0.0195 135 PHE A N   
1085 C CA  . PHE A 138 ? 0.3422 0.4469 0.3796 -0.0534 0.0019  -0.0224 135 PHE A CA  
1086 C C   . PHE A 138 ? 0.3336 0.4327 0.3614 -0.0511 -0.0027 -0.0224 135 PHE A C   
1087 O O   . PHE A 138 ? 0.3519 0.4529 0.3810 -0.0475 -0.0044 -0.0275 135 PHE A O   
1088 C CB  . PHE A 138 ? 0.3310 0.4331 0.3721 -0.0555 0.0013  -0.0186 135 PHE A CB  
1089 C CG  . PHE A 138 ? 0.3376 0.4441 0.3877 -0.0529 0.0061  -0.0188 135 PHE A CG  
1090 C CD1 . PHE A 138 ? 0.3806 0.4825 0.4340 -0.0501 0.0098  -0.0246 135 PHE A CD1 
1091 C CD2 . PHE A 138 ? 0.3748 0.4905 0.4293 -0.0527 0.0082  -0.0132 135 PHE A CD2 
1092 C CE1 . PHE A 138 ? 0.3824 0.4827 0.4409 -0.0466 0.0168  -0.0237 135 PHE A CE1 
1093 C CE2 . PHE A 138 ? 0.4165 0.5347 0.4770 -0.0468 0.0139  -0.0115 135 PHE A CE2 
1094 C CZ  . PHE A 138 ? 0.3740 0.4814 0.4353 -0.0435 0.0190  -0.0163 135 PHE A CZ  
1095 N N   . VAL A 139 ? 0.3617 0.4541 0.3792 -0.0525 -0.0036 -0.0165 136 VAL A N   
1096 C CA  . VAL A 139 ? 0.3363 0.4204 0.3418 -0.0472 -0.0062 -0.0145 136 VAL A CA  
1097 C C   . VAL A 139 ? 0.3671 0.4643 0.3715 -0.0405 -0.0079 -0.0190 136 VAL A C   
1098 O O   . VAL A 139 ? 0.3870 0.4867 0.3878 -0.0334 -0.0111 -0.0204 136 VAL A O   
1099 C CB  . VAL A 139 ? 0.3971 0.4670 0.3887 -0.0501 -0.0038 -0.0069 136 VAL A CB  
1100 C CG1 . VAL A 139 ? 0.3849 0.4448 0.3608 -0.0409 -0.0044 -0.0029 136 VAL A CG1 
1101 C CG2 . VAL A 139 ? 0.4218 0.4804 0.4133 -0.0586 -0.0024 -0.0051 136 VAL A CG2 
1102 N N   . ALA A 140 ? 0.3448 0.4526 0.3518 -0.0427 -0.0055 -0.0217 137 ALA A N   
1103 C CA  . ALA A 140 ? 0.3576 0.4807 0.3626 -0.0386 -0.0071 -0.0279 137 ALA A CA  
1104 C C   . ALA A 140 ? 0.3372 0.4708 0.3530 -0.0385 -0.0083 -0.0378 137 ALA A C   
1105 O O   . ALA A 140 ? 0.3533 0.5019 0.3671 -0.0340 -0.0121 -0.0428 137 ALA A O   
1106 C CB  . ALA A 140 ? 0.3481 0.4779 0.3532 -0.0424 -0.0026 -0.0302 137 ALA A CB  
1107 N N   . ILE A 141 ? 0.3266 0.4543 0.3533 -0.0435 -0.0047 -0.0404 138 ILE A N   
1108 C CA  . ILE A 141 ? 0.3348 0.4689 0.3712 -0.0451 -0.0035 -0.0497 138 ILE A CA  
1109 C C   . ILE A 141 ? 0.3093 0.4446 0.3441 -0.0394 -0.0089 -0.0483 138 ILE A C   
1110 O O   . ILE A 141 ? 0.3179 0.4695 0.3566 -0.0376 -0.0110 -0.0560 138 ILE A O   
1111 C CB  . ILE A 141 ? 0.3268 0.4507 0.3721 -0.0498 0.0032  -0.0507 138 ILE A CB  
1112 C CG1 . ILE A 141 ? 0.3478 0.4706 0.3942 -0.0526 0.0102  -0.0517 138 ILE A CG1 
1113 C CG2 . ILE A 141 ? 0.3452 0.4723 0.3987 -0.0523 0.0063  -0.0600 138 ILE A CG2 
1114 C CD1 . ILE A 141 ? 0.3592 0.4715 0.4120 -0.0534 0.0179  -0.0500 138 ILE A CD1 
1115 N N   . PHE A 142 ? 0.3161 0.4358 0.3448 -0.0367 -0.0107 -0.0392 139 PHE A N   
1116 C CA  . PHE A 142 ? 0.3426 0.4596 0.3673 -0.0297 -0.0141 -0.0370 139 PHE A CA  
1117 C C   . PHE A 142 ? 0.3880 0.5188 0.4048 -0.0201 -0.0183 -0.0362 139 PHE A C   
1118 O O   . PHE A 142 ? 0.3784 0.5227 0.3982 -0.0134 -0.0211 -0.0398 139 PHE A O   
1119 C CB  . PHE A 142 ? 0.3544 0.4488 0.3702 -0.0299 -0.0135 -0.0282 139 PHE A CB  
1120 C CG  . PHE A 142 ? 0.3166 0.4016 0.3388 -0.0361 -0.0112 -0.0289 139 PHE A CG  
1121 C CD1 . PHE A 142 ? 0.3827 0.4663 0.4087 -0.0337 -0.0112 -0.0321 139 PHE A CD1 
1122 C CD2 . PHE A 142 ? 0.3468 0.4274 0.3710 -0.0434 -0.0090 -0.0261 139 PHE A CD2 
1123 C CE1 . PHE A 142 ? 0.3919 0.4668 0.4210 -0.0386 -0.0090 -0.0321 139 PHE A CE1 
1124 C CE2 . PHE A 142 ? 0.3708 0.4464 0.3992 -0.0473 -0.0077 -0.0260 139 PHE A CE2 
1125 C CZ  . PHE A 142 ? 0.3681 0.4398 0.3980 -0.0451 -0.0077 -0.0289 139 PHE A CZ  
1126 N N   . LEU A 143 ? 0.3583 0.4875 0.3642 -0.0184 -0.0186 -0.0309 140 LEU A N   
1127 C CA  . LEU A 143 ? 0.3822 0.5250 0.3774 -0.0075 -0.0224 -0.0283 140 LEU A CA  
1128 C C   . LEU A 143 ? 0.3705 0.5461 0.3756 -0.0072 -0.0260 -0.0403 140 LEU A C   
1129 O O   . LEU A 143 ? 0.3851 0.5795 0.3875 0.0037  -0.0306 -0.0403 140 LEU A O   
1130 C CB  . LEU A 143 ? 0.3803 0.5155 0.3627 -0.0084 -0.0205 -0.0217 140 LEU A CB  
1131 C CG  . LEU A 143 ? 0.4086 0.5138 0.3777 -0.0083 -0.0163 -0.0099 140 LEU A CG  
1132 C CD1 . LEU A 143 ? 0.4770 0.5773 0.4352 -0.0112 -0.0130 -0.0046 140 LEU A CD1 
1133 C CD2 . LEU A 143 ? 0.4388 0.5327 0.3939 0.0053  -0.0168 -0.0019 140 LEU A CD2 
1134 N N   . ALA A 144 ? 0.3402 0.5233 0.3559 -0.0190 -0.0228 -0.0505 141 ALA A N   
1135 C CA  . ALA A 144 ? 0.3635 0.5759 0.3885 -0.0233 -0.0239 -0.0647 141 ALA A CA  
1136 C C   . ALA A 144 ? 0.3531 0.5774 0.3898 -0.0220 -0.0253 -0.0707 141 ALA A C   
1137 O O   . ALA A 144 ? 0.3855 0.6411 0.4260 -0.0183 -0.0297 -0.0781 141 ALA A O   
1138 C CB  . ALA A 144 ? 0.3757 0.5837 0.4078 -0.0368 -0.0167 -0.0739 141 ALA A CB  
1139 N N   . VAL A 145 ? 0.3176 0.5201 0.3600 -0.0249 -0.0214 -0.0676 142 VAL A N   
1140 C CA  . VAL A 145 ? 0.3330 0.5454 0.3862 -0.0243 -0.0213 -0.0734 142 VAL A CA  
1141 C C   . VAL A 145 ? 0.3502 0.5750 0.3976 -0.0085 -0.0277 -0.0669 142 VAL A C   
1142 O O   . VAL A 145 ? 0.3661 0.6199 0.4224 -0.0051 -0.0302 -0.0744 142 VAL A O   
1143 C CB  . VAL A 145 ? 0.3201 0.5060 0.3778 -0.0294 -0.0156 -0.0705 142 VAL A CB  
1144 C CG1 . VAL A 145 ? 0.3391 0.5343 0.4065 -0.0279 -0.0148 -0.0756 142 VAL A CG1 
1145 C CG2 . VAL A 145 ? 0.3214 0.4956 0.3841 -0.0416 -0.0081 -0.0753 142 VAL A CG2 
1146 N N   . LEU A 146 ? 0.3601 0.5628 0.3922 0.0011  -0.0289 -0.0531 143 LEU A N   
1147 C CA  . LEU A 146 ? 0.4036 0.6097 0.4263 0.0187  -0.0324 -0.0445 143 LEU A CA  
1148 C C   . LEU A 146 ? 0.4710 0.7146 0.4914 0.0291  -0.0387 -0.0468 143 LEU A C   
1149 O O   . LEU A 146 ? 0.4356 0.7006 0.4575 0.0428  -0.0420 -0.0458 143 LEU A O   
1150 C CB  . LEU A 146 ? 0.4540 0.6236 0.4578 0.0241  -0.0296 -0.0301 143 LEU A CB  
1151 C CG  . LEU A 146 ? 0.4610 0.5979 0.4651 0.0157  -0.0244 -0.0275 143 LEU A CG  
1152 C CD1 . LEU A 146 ? 0.5410 0.6446 0.5252 0.0201  -0.0208 -0.0151 143 LEU A CD1 
1153 C CD2 . LEU A 146 ? 0.4246 0.5648 0.4377 0.0191  -0.0235 -0.0315 143 LEU A CD2 
1154 N N   . GLU A 147 ? 0.4301 0.6836 0.4461 0.0235  -0.0402 -0.0498 144 GLU A N   
1155 C CA  . GLU A 147 ? 0.4869 0.7788 0.4986 0.0331  -0.0469 -0.0523 144 GLU A CA  
1156 C C   . GLU A 147 ? 0.4359 0.7711 0.4671 0.0252  -0.0497 -0.0701 144 GLU A C   
1157 O O   . GLU A 147 ? 0.4651 0.8395 0.4978 0.0370  -0.0561 -0.0721 144 GLU A O   
1158 C CB  . GLU A 147 ? 0.5696 0.8589 0.5688 0.0291  -0.0470 -0.0506 144 GLU A CB  
1159 C CG  . GLU A 147 ? 0.7500 1.0352 0.7593 0.0082  -0.0423 -0.0631 144 GLU A CG  
1160 C CD  . GLU A 147 ? 0.9935 1.2763 0.9903 0.0049  -0.0414 -0.0619 144 GLU A CD  
1161 O OE1 . GLU A 147 ? 1.0552 1.3104 1.0376 0.0102  -0.0390 -0.0481 144 GLU A OE1 
1162 O OE2 . GLU A 147 ? 1.0237 1.3315 1.0247 -0.0043 -0.0419 -0.0756 144 GLU A OE2 
1163 N N   . ILE A 148 ? 0.3691 0.6978 0.4148 0.0057  -0.0439 -0.0827 145 ILE A N   
1164 C CA  . ILE A 148 ? 0.3852 0.7503 0.4486 -0.0062 -0.0436 -0.1015 145 ILE A CA  
1165 C C   . ILE A 148 ? 0.4298 0.8064 0.5067 -0.0020 -0.0432 -0.1037 145 ILE A C   
1166 O O   . ILE A 148 ? 0.3730 0.7938 0.4622 -0.0031 -0.0465 -0.1156 145 ILE A O   
1167 C CB  . ILE A 148 ? 0.3756 0.7243 0.4457 -0.0282 -0.0347 -0.1136 145 ILE A CB  
1168 C CG1 . ILE A 148 ? 0.3875 0.7316 0.4448 -0.0314 -0.0349 -0.1131 145 ILE A CG1 
1169 C CG2 . ILE A 148 ? 0.3910 0.7701 0.4784 -0.0436 -0.0310 -0.1341 145 ILE A CG2 
1170 C CD1 . ILE A 148 ? 0.4318 0.7537 0.4925 -0.0494 -0.0245 -0.1221 145 ILE A CD1 
1171 N N   . TRP A 149 ? 0.3770 0.7162 0.4519 0.0016  -0.0389 -0.0934 146 TRP A N   
1172 C CA  . TRP A 149 ? 0.3789 0.7227 0.4646 0.0059  -0.0370 -0.0944 146 TRP A CA  
1173 C C   . TRP A 149 ? 0.3240 0.6508 0.3966 0.0273  -0.0395 -0.0775 146 TRP A C   
1174 O O   . TRP A 149 ? 0.3955 0.6807 0.4599 0.0275  -0.0351 -0.0682 146 TRP A O   
1175 C CB  . TRP A 149 ? 0.3581 0.6713 0.4514 -0.0095 -0.0278 -0.0986 146 TRP A CB  
1176 C CG  . TRP A 149 ? 0.3506 0.6776 0.4579 -0.0297 -0.0214 -0.1161 146 TRP A CG  
1177 C CD1 . TRP A 149 ? 0.3478 0.7048 0.4717 -0.0377 -0.0183 -0.1302 146 TRP A CD1 
1178 C CD2 . TRP A 149 ? 0.3214 0.6330 0.4263 -0.0446 -0.0157 -0.1220 146 TRP A CD2 
1179 N NE1 . TRP A 149 ? 0.3671 0.7224 0.4977 -0.0582 -0.0096 -0.1446 146 TRP A NE1 
1180 C CE2 . TRP A 149 ? 0.3317 0.6588 0.4504 -0.0617 -0.0078 -0.1396 146 TRP A CE2 
1181 C CE3 . TRP A 149 ? 0.3435 0.6285 0.4360 -0.0452 -0.0151 -0.1142 146 TRP A CE3 
1182 C CZ2 . TRP A 149 ? 0.3198 0.6330 0.4380 -0.0782 0.0014  -0.1492 146 TRP A CZ2 
1183 C CZ3 . TRP A 149 ? 0.3480 0.6232 0.4418 -0.0601 -0.0071 -0.1232 146 TRP A CZ3 
1184 C CH2 . TRP A 149 ? 0.3139 0.6004 0.4194 -0.0758 0.0015  -0.1401 146 TRP A CH2 
1185 N N   . PRO A 150 ? 0.3678 0.7260 0.4373 0.0464  -0.0458 -0.0731 147 PRO A N   
1186 C CA  . PRO A 150 ? 0.4099 0.7478 0.4652 0.0685  -0.0454 -0.0568 147 PRO A CA  
1187 C C   . PRO A 150 ? 0.3869 0.7103 0.4512 0.0685  -0.0395 -0.0578 147 PRO A C   
1188 O O   . PRO A 150 ? 0.4362 0.7315 0.4877 0.0829  -0.0362 -0.0457 147 PRO A O   
1189 C CB  . PRO A 150 ? 0.4403 0.8242 0.4930 0.0895  -0.0530 -0.0537 147 PRO A CB  
1190 C CG  . PRO A 150 ? 0.4479 0.8858 0.5218 0.0750  -0.0575 -0.0732 147 PRO A CG  
1191 C CD  . PRO A 150 ? 0.4000 0.8145 0.4775 0.0485  -0.0529 -0.0832 147 PRO A CD  
1192 N N   . GLU A 151 ? 0.4052 0.7435 0.4893 0.0509  -0.0366 -0.0725 148 GLU A N   
1193 C CA  . GLU A 151 ? 0.3879 0.7152 0.4808 0.0494  -0.0304 -0.0747 148 GLU A CA  
1194 C C   . GLU A 151 ? 0.3603 0.6347 0.4440 0.0388  -0.0239 -0.0695 148 GLU A C   
1195 O O   . GLU A 151 ? 0.3710 0.6305 0.4582 0.0371  -0.0183 -0.0703 148 GLU A O   
1196 C CB  . GLU A 151 ? 0.4002 0.7622 0.5168 0.0337  -0.0276 -0.0924 148 GLU A CB  
1197 C CG  . GLU A 151 ? 0.4731 0.8969 0.6035 0.0379  -0.0339 -0.1026 148 GLU A CG  
1198 C CD  . GLU A 151 ? 0.4653 0.9122 0.5944 0.0290  -0.0394 -0.1098 148 GLU A CD  
1199 O OE1 . GLU A 151 ? 0.4107 0.8234 0.5290 0.0188  -0.0375 -0.1071 148 GLU A OE1 
1200 O OE2 . GLU A 151 ? 0.4497 0.9513 0.5889 0.0321  -0.0455 -0.1187 148 GLU A OE2 
1201 N N   . THR A 152 ? 0.3653 0.6143 0.4371 0.0323  -0.0247 -0.0644 149 THR A N   
1202 C CA  . THR A 152 ? 0.3528 0.5594 0.4171 0.0220  -0.0196 -0.0602 149 THR A CA  
1203 C C   . THR A 152 ? 0.4158 0.5922 0.4670 0.0328  -0.0164 -0.0502 149 THR A C   
1204 O O   . THR A 152 ? 0.4210 0.5891 0.4579 0.0479  -0.0177 -0.0405 149 THR A O   
1205 C CB  . THR A 152 ? 0.3856 0.5758 0.4398 0.0155  -0.0212 -0.0556 149 THR A CB  
1206 O OG1 . THR A 152 ? 0.3804 0.5963 0.4450 0.0056  -0.0228 -0.0658 149 THR A OG1 
1207 C CG2 . THR A 152 ? 0.4009 0.5554 0.4495 0.0051  -0.0168 -0.0518 149 THR A CG2 
1208 N N   . THR A 153 ? 0.3880 0.5451 0.4418 0.0246  -0.0111 -0.0525 150 THR A N   
1209 C CA  . THR A 153 ? 0.4191 0.5470 0.4603 0.0318  -0.0068 -0.0459 150 THR A CA  
1210 C C   . THR A 153 ? 0.4224 0.5144 0.4521 0.0200  -0.0042 -0.0422 150 THR A C   
1211 O O   . THR A 153 ? 0.4231 0.4867 0.4378 0.0235  -0.0006 -0.0367 150 THR A O   
1212 C CB  . THR A 153 ? 0.4563 0.5954 0.5085 0.0340  -0.0025 -0.0520 150 THR A CB  
1213 O OG1 . THR A 153 ? 0.4302 0.5732 0.4946 0.0175  0.0001  -0.0604 150 THR A OG1 
1214 C CG2 . THR A 153 ? 0.5202 0.6990 0.5844 0.0472  -0.0048 -0.0555 150 THR A CG2 
1215 N N   . TRP A 154 ? 0.3722 0.4663 0.4085 0.0059  -0.0052 -0.0456 151 TRP A N   
1216 C CA  . TRP A 154 ? 0.3518 0.4196 0.3788 -0.0040 -0.0036 -0.0420 151 TRP A CA  
1217 C C   . TRP A 154 ? 0.3456 0.4220 0.3802 -0.0146 -0.0051 -0.0441 151 TRP A C   
1218 O O   . TRP A 154 ? 0.3494 0.4461 0.3969 -0.0174 -0.0047 -0.0507 151 TRP A O   
1219 C CB  . TRP A 154 ? 0.3731 0.4285 0.3997 -0.0086 0.0008  -0.0444 151 TRP A CB  
1220 C CG  . TRP A 154 ? 0.3735 0.4053 0.3878 -0.0171 0.0015  -0.0406 151 TRP A CG  
1221 C CD1 . TRP A 154 ? 0.3699 0.4006 0.3867 -0.0273 0.0017  -0.0411 151 TRP A CD1 
1222 C CD2 . TRP A 154 ? 0.3760 0.3832 0.3728 -0.0160 0.0031  -0.0363 151 TRP A CD2 
1223 N NE1 . TRP A 154 ? 0.3766 0.3896 0.3803 -0.0332 0.0015  -0.0379 151 TRP A NE1 
1224 C CE2 . TRP A 154 ? 0.3858 0.3824 0.3768 -0.0281 0.0030  -0.0359 151 TRP A CE2 
1225 C CE3 . TRP A 154 ? 0.3948 0.3871 0.3791 -0.0057 0.0057  -0.0328 151 TRP A CE3 
1226 C CZ2 . TRP A 154 ? 0.4166 0.3901 0.3906 -0.0334 0.0052  -0.0342 151 TRP A CZ2 
1227 C CZ3 . TRP A 154 ? 0.4309 0.3938 0.3964 -0.0099 0.0097  -0.0301 151 TRP A CZ3 
1228 C CH2 . TRP A 154 ? 0.4497 0.4040 0.4107 -0.0252 0.0093  -0.0319 151 TRP A CH2 
1229 N N   . GLY A 155 ? 0.3304 0.3911 0.3567 -0.0210 -0.0056 -0.0392 152 GLY A N   
1230 C CA  . GLY A 155 ? 0.3243 0.3914 0.3570 -0.0293 -0.0058 -0.0400 152 GLY A CA  
1231 C C   . GLY A 155 ? 0.3266 0.3790 0.3525 -0.0365 -0.0053 -0.0355 152 GLY A C   
1232 O O   . GLY A 155 ? 0.3503 0.3879 0.3642 -0.0371 -0.0059 -0.0316 152 GLY A O   
1233 N N   . MET A 156 ? 0.3219 0.3790 0.3546 -0.0418 -0.0033 -0.0362 153 MET A N   
1234 C CA  . MET A 156 ? 0.3250 0.3760 0.3526 -0.0474 -0.0038 -0.0318 153 MET A CA  
1235 C C   . MET A 156 ? 0.3206 0.3813 0.3557 -0.0494 -0.0020 -0.0301 153 MET A C   
1236 O O   . MET A 156 ? 0.3201 0.3851 0.3629 -0.0478 0.0024  -0.0332 153 MET A O   
1237 C CB  . MET A 156 ? 0.3536 0.3975 0.3775 -0.0483 -0.0019 -0.0325 153 MET A CB  
1238 C CG  . MET A 156 ? 0.3616 0.4073 0.3819 -0.0534 -0.0027 -0.0285 153 MET A CG  
1239 S SD  . MET A 156 ? 0.3811 0.4221 0.3957 -0.0534 -0.0003 -0.0290 153 MET A SD  
1240 C CE  . MET A 156 ? 0.3967 0.4445 0.4218 -0.0485 0.0060  -0.0278 153 MET A CE  
1241 N N   . LEU A 157 ? 0.3299 0.3930 0.3620 -0.0531 -0.0042 -0.0255 154 LEU A N   
1242 C CA  . LEU A 157 ? 0.3502 0.4233 0.3880 -0.0536 -0.0024 -0.0221 154 LEU A CA  
1243 C C   . LEU A 157 ? 0.3176 0.3944 0.3508 -0.0574 -0.0049 -0.0181 154 LEU A C   
1244 O O   . LEU A 157 ? 0.3396 0.4152 0.3665 -0.0638 -0.0082 -0.0175 154 LEU A O   
1245 C CB  . LEU A 157 ? 0.3542 0.4337 0.3940 -0.0545 -0.0029 -0.0208 154 LEU A CB  
1246 C CG  . LEU A 157 ? 0.3441 0.4350 0.3895 -0.0539 -0.0004 -0.0165 154 LEU A CG  
1247 C CD1 . LEU A 157 ? 0.3326 0.4228 0.3841 -0.0482 0.0064  -0.0178 154 LEU A CD1 
1248 C CD2 . LEU A 157 ? 0.3942 0.4914 0.4399 -0.0563 -0.0010 -0.0150 154 LEU A CD2 
1249 N N   . ALA A 158 ? 0.3160 0.3971 0.3508 -0.0540 -0.0025 -0.0156 155 ALA A N   
1250 C CA  . ALA A 158 ? 0.3490 0.4393 0.3790 -0.0571 -0.0059 -0.0123 155 ALA A CA  
1251 C C   . ALA A 158 ? 0.3191 0.4207 0.3525 -0.0492 -0.0025 -0.0062 155 ALA A C   
1252 O O   . ALA A 158 ? 0.3448 0.4381 0.3806 -0.0421 0.0041  -0.0055 155 ALA A O   
1253 C CB  . ALA A 158 ? 0.3811 0.4602 0.4018 -0.0600 -0.0072 -0.0159 155 ALA A CB  
1254 N N   . PRO A 159 ? 0.3127 0.4342 0.3452 -0.0502 -0.0064 -0.0015 156 PRO A N   
1255 C CA  . PRO A 159 ? 0.3184 0.4525 0.3520 -0.0394 -0.0033 0.0063  156 PRO A CA  
1256 C C   . PRO A 159 ? 0.3077 0.4279 0.3333 -0.0350 0.0002  0.0063  156 PRO A C   
1257 O O   . PRO A 159 ? 0.3335 0.4477 0.3515 -0.0420 -0.0035 0.0014  156 PRO A O   
1258 C CB  . PRO A 159 ? 0.3403 0.5038 0.3735 -0.0436 -0.0105 0.0093  156 PRO A CB  
1259 C CG  . PRO A 159 ? 0.3544 0.5183 0.3894 -0.0577 -0.0149 0.0029  156 PRO A CG  
1260 C CD  . PRO A 159 ? 0.3439 0.4778 0.3736 -0.0618 -0.0131 -0.0037 156 PRO A CD  
1261 N N   . HIS A 160 ? 0.3270 0.4404 0.3526 -0.0233 0.0090  0.0121  157 HIS A N   
1262 C CA  . HIS A 160 ? 0.3724 0.4710 0.3899 -0.0187 0.0148  0.0131  157 HIS A CA  
1263 C C   . HIS A 160 ? 0.3599 0.4732 0.3670 -0.0188 0.0083  0.0162  157 HIS A C   
1264 O O   . HIS A 160 ? 0.3635 0.4664 0.3629 -0.0235 0.0076  0.0115  157 HIS A O   
1265 C CB  . HIS A 160 ? 0.4278 0.5162 0.4449 -0.0056 0.0275  0.0205  157 HIS A CB  
1266 C CG  . HIS A 160 ? 0.4587 0.5268 0.4673 -0.0020 0.0368  0.0209  157 HIS A CG  
1267 N ND1 . HIS A 160 ? 0.4951 0.5664 0.4921 0.0083  0.0398  0.0307  157 HIS A ND1 
1268 C CD2 . HIS A 160 ? 0.4850 0.5326 0.4945 -0.0080 0.0431  0.0128  157 HIS A CD2 
1269 C CE1 . HIS A 160 ? 0.5036 0.5527 0.4939 0.0085  0.0493  0.0288  157 HIS A CE1 
1270 N NE2 . HIS A 160 ? 0.4797 0.5153 0.4786 -0.0019 0.0516  0.0175  157 HIS A NE2 
1271 N N   . ALA A 161 ? 0.3516 0.4922 0.3588 -0.0137 0.0035  0.0236  158 ALA A N   
1272 C CA  . ALA A 161 ? 0.4002 0.5620 0.3974 -0.0140 -0.0033 0.0262  158 ALA A CA  
1273 C C   . ALA A 161 ? 0.3329 0.4944 0.3256 -0.0315 -0.0117 0.0149  158 ALA A C   
1274 O O   . ALA A 161 ? 0.3922 0.5545 0.3728 -0.0341 -0.0140 0.0128  158 ALA A O   
1275 C CB  . ALA A 161 ? 0.4027 0.6008 0.4039 -0.0066 -0.0080 0.0346  158 ALA A CB  
1276 N N   . TYR A 162 ? 0.3707 0.5297 0.3710 -0.0428 -0.0149 0.0080  159 TYR A N   
1277 C CA  . TYR A 162 ? 0.3780 0.5301 0.3722 -0.0588 -0.0199 -0.0022 159 TYR A CA  
1278 C C   . TYR A 162 ? 0.3946 0.5166 0.3813 -0.0593 -0.0153 -0.0075 159 TYR A C   
1279 O O   . TYR A 162 ? 0.3922 0.5100 0.3670 -0.0660 -0.0172 -0.0127 159 TYR A O   
1280 C CB  . TYR A 162 ? 0.4111 0.5588 0.4129 -0.0683 -0.0212 -0.0069 159 TYR A CB  
1281 C CG  . TYR A 162 ? 0.4084 0.5434 0.4006 -0.0838 -0.0235 -0.0165 159 TYR A CG  
1282 C CD1 . TYR A 162 ? 0.4806 0.6340 0.4658 -0.0966 -0.0286 -0.0212 159 TYR A CD1 
1283 C CD2 . TYR A 162 ? 0.4311 0.5354 0.4193 -0.0849 -0.0196 -0.0214 159 TYR A CD2 
1284 C CE1 . TYR A 162 ? 0.4685 0.6046 0.4420 -0.1118 -0.0280 -0.0310 159 TYR A CE1 
1285 C CE2 . TYR A 162 ? 0.4586 0.5461 0.4350 -0.0966 -0.0193 -0.0293 159 TYR A CE2 
1286 C CZ  . TYR A 162 ? 0.4596 0.5601 0.4278 -0.1107 -0.0227 -0.0343 159 TYR A CZ  
1287 O OH  . TYR A 162 ? 0.4635 0.5421 0.4178 -0.1233 -0.0198 -0.0430 159 TYR A OH  
1288 N N   . PHE A 163 ? 0.3533 0.4561 0.3472 -0.0530 -0.0089 -0.0071 160 PHE A N   
1289 C CA  . PHE A 163 ? 0.3658 0.4451 0.3556 -0.0531 -0.0043 -0.0125 160 PHE A CA  
1290 C C   . PHE A 163 ? 0.3728 0.4502 0.3517 -0.0487 -0.0014 -0.0105 160 PHE A C   
1291 O O   . PHE A 163 ? 0.4027 0.4703 0.3719 -0.0539 -0.0018 -0.0162 160 PHE A O   
1292 C CB  . PHE A 163 ? 0.3600 0.4268 0.3604 -0.0472 0.0023  -0.0128 160 PHE A CB  
1293 C CG  . PHE A 163 ? 0.3842 0.4335 0.3829 -0.0474 0.0068  -0.0189 160 PHE A CG  
1294 C CD1 . PHE A 163 ? 0.4511 0.4915 0.4471 -0.0527 0.0039  -0.0253 160 PHE A CD1 
1295 C CD2 . PHE A 163 ? 0.4667 0.5084 0.4651 -0.0418 0.0149  -0.0179 160 PHE A CD2 
1296 C CE1 . PHE A 163 ? 0.4645 0.4926 0.4598 -0.0508 0.0082  -0.0303 160 PHE A CE1 
1297 C CE2 . PHE A 163 ? 0.5152 0.5452 0.5135 -0.0425 0.0193  -0.0240 160 PHE A CE2 
1298 C CZ  . PHE A 163 ? 0.4827 0.5079 0.4803 -0.0463 0.0154  -0.0301 160 PHE A CZ  
1299 N N   . VAL A 164 ? 0.3608 0.4464 0.3397 -0.0383 0.0024  -0.0017 161 VAL A N   
1300 C CA  . VAL A 164 ? 0.3951 0.4773 0.3621 -0.0320 0.0068  0.0020  161 VAL A CA  
1301 C C   . VAL A 164 ? 0.4328 0.5323 0.3860 -0.0367 -0.0009 0.0012  161 VAL A C   
1302 O O   . VAL A 164 ? 0.4681 0.5582 0.4092 -0.0385 0.0009  -0.0021 161 VAL A O   
1303 C CB  . VAL A 164 ? 0.4288 0.5111 0.3965 -0.0176 0.0154  0.0132  161 VAL A CB  
1304 C CG1 . VAL A 164 ? 0.5098 0.5911 0.4617 -0.0094 0.0199  0.0198  161 VAL A CG1 
1305 C CG2 . VAL A 164 ? 0.4578 0.5188 0.4360 -0.0156 0.0259  0.0112  161 VAL A CG2 
1306 N N   . HIS A 165 ? 0.4091 0.5356 0.3639 -0.0400 -0.0093 0.0030  162 HIS A N   
1307 C CA  . HIS A 165 ? 0.4242 0.5733 0.3658 -0.0449 -0.0165 0.0017  162 HIS A CA  
1308 C C   . HIS A 165 ? 0.4385 0.5950 0.3771 -0.0637 -0.0242 -0.0099 162 HIS A C   
1309 O O   . HIS A 165 ? 0.4701 0.6432 0.3959 -0.0710 -0.0293 -0.0142 162 HIS A O   
1310 C CB  . HIS A 165 ? 0.4595 0.6436 0.4032 -0.0342 -0.0206 0.0128  162 HIS A CB  
1311 C CG  . HIS A 165 ? 0.4954 0.6722 0.4374 -0.0140 -0.0114 0.0261  162 HIS A CG  
1312 N ND1 . HIS A 165 ? 0.5688 0.7376 0.4951 -0.0053 -0.0063 0.0312  162 HIS A ND1 
1313 C CD2 . HIS A 165 ? 0.5036 0.6793 0.4552 -0.0008 -0.0051 0.0358  162 HIS A CD2 
1314 C CE1 . HIS A 165 ? 0.5663 0.7254 0.4926 0.0121  0.0039  0.0436  162 HIS A CE1 
1315 N NE2 . HIS A 165 ? 0.5622 0.7244 0.5036 0.0150  0.0050  0.0462  162 HIS A NE2 
1316 N N   A GLN A 166 ? 0.4249 0.5676 0.3728 -0.0722 -0.0239 -0.0156 163 GLN A N   
1317 N N   B GLN A 166 ? 0.4341 0.5776 0.3826 -0.0719 -0.0239 -0.0153 163 GLN A N   
1318 C CA  A GLN A 166 ? 0.4568 0.6028 0.3995 -0.0906 -0.0285 -0.0263 163 GLN A CA  
1319 C CA  B GLN A 166 ? 0.4625 0.6094 0.4069 -0.0902 -0.0286 -0.0256 163 GLN A CA  
1320 C C   A GLN A 166 ? 0.4337 0.5434 0.3732 -0.0978 -0.0234 -0.0345 163 GLN A C   
1321 C C   B GLN A 166 ? 0.4429 0.5540 0.3854 -0.0973 -0.0236 -0.0336 163 GLN A C   
1322 O O   A GLN A 166 ? 0.3878 0.4906 0.3182 -0.1129 -0.0241 -0.0438 163 GLN A O   
1323 O O   B GLN A 166 ? 0.4679 0.5742 0.4059 -0.1118 -0.0246 -0.0414 163 GLN A O   
1324 C CB  A GLN A 166 ? 0.4659 0.6377 0.4206 -0.0960 -0.0334 -0.0246 163 GLN A CB  
1325 C CB  B GLN A 166 ? 0.4615 0.6359 0.4184 -0.0938 -0.0335 -0.0228 163 GLN A CB  
1326 C CG  A GLN A 166 ? 0.5188 0.7326 0.4775 -0.0878 -0.0389 -0.0161 163 GLN A CG  
1327 C CG  B GLN A 166 ? 0.4992 0.7144 0.4591 -0.0844 -0.0385 -0.0139 163 GLN A CG  
1328 C CD  A GLN A 166 ? 0.5591 0.7998 0.5315 -0.0935 -0.0429 -0.0153 163 GLN A CD  
1329 C CD  B GLN A 166 ? 0.5337 0.7741 0.4796 -0.0925 -0.0447 -0.0188 163 GLN A CD  
1330 O OE1 A GLN A 166 ? 0.6039 0.8530 0.5747 -0.1123 -0.0460 -0.0249 163 GLN A OE1 
1331 O OE1 B GLN A 166 ? 0.5810 0.8074 0.5143 -0.1080 -0.0448 -0.0306 163 GLN A OE1 
1332 N NE2 A GLN A 166 ? 0.5655 0.8180 0.5506 -0.0779 -0.0412 -0.0042 163 GLN A NE2 
1333 N NE2 B GLN A 166 ? 0.5709 0.8504 0.5180 -0.0817 -0.0496 -0.0099 163 GLN A NE2 
1334 N N   . ARG A 167 ? 0.4232 0.5100 0.3688 -0.0871 -0.0174 -0.0316 164 ARG A N   
1335 C CA  . ARG A 167 ? 0.4315 0.4888 0.3746 -0.0910 -0.0130 -0.0381 164 ARG A CA  
1336 C C   . ARG A 167 ? 0.4408 0.4842 0.3653 -0.1009 -0.0113 -0.0472 164 ARG A C   
1337 O O   . ARG A 167 ? 0.4656 0.5141 0.3807 -0.0992 -0.0112 -0.0477 164 ARG A O   
1338 C CB  . ARG A 167 ? 0.4043 0.4453 0.3563 -0.0787 -0.0072 -0.0353 164 ARG A CB  
1339 C CG  . ARG A 167 ? 0.4160 0.4511 0.3631 -0.0712 -0.0024 -0.0345 164 ARG A CG  
1340 C CD  . ARG A 167 ? 0.4136 0.4360 0.3717 -0.0625 0.0037  -0.0341 164 ARG A CD  
1341 N NE  . ARG A 167 ? 0.4519 0.4668 0.4054 -0.0572 0.0101  -0.0347 164 ARG A NE  
1342 C CZ  . ARG A 167 ? 0.4657 0.4875 0.4167 -0.0520 0.0131  -0.0291 164 ARG A CZ  
1343 N NH1 . ARG A 167 ? 0.4615 0.4989 0.4157 -0.0490 0.0103  -0.0217 164 ARG A NH1 
1344 N NH2 . ARG A 167 ? 0.4686 0.4811 0.4140 -0.0483 0.0202  -0.0301 164 ARG A NH2 
1345 N N   . THR A 168 ? 0.4483 0.4719 0.3657 -0.1109 -0.0088 -0.0541 165 THR A N   
1346 C CA  . THR A 168 ? 0.4599 0.4656 0.3575 -0.1222 -0.0051 -0.0641 165 THR A CA  
1347 C C   . THR A 168 ? 0.4918 0.4773 0.3819 -0.1129 0.0009  -0.0657 165 THR A C   
1348 O O   . THR A 168 ? 0.4931 0.4783 0.3687 -0.1178 0.0019  -0.0710 165 THR A O   
1349 C CB  . THR A 168 ? 0.5175 0.4974 0.4078 -0.1322 0.0000  -0.0698 165 THR A CB  
1350 O OG1 . THR A 168 ? 0.5067 0.5053 0.4045 -0.1418 -0.0044 -0.0687 165 THR A OG1 
1351 C CG2 . THR A 168 ? 0.5771 0.5336 0.4444 -0.1455 0.0063  -0.0814 165 THR A CG2 
1352 N N   . PHE A 169 ? 0.4796 0.4514 0.3800 -0.0998 0.0051  -0.0615 166 PHE A N   
1353 C CA  . PHE A 169 ? 0.4856 0.4401 0.3814 -0.0909 0.0119  -0.0634 166 PHE A CA  
1354 C C   . PHE A 169 ? 0.5013 0.4713 0.4101 -0.0794 0.0117  -0.0568 166 PHE A C   
1355 O O   . PHE A 169 ? 0.4858 0.4624 0.4113 -0.0716 0.0112  -0.0516 166 PHE A O   
1356 C CB  . PHE A 169 ? 0.5094 0.4397 0.4063 -0.0845 0.0179  -0.0644 166 PHE A CB  
1357 C CG  . PHE A 169 ? 0.4938 0.4010 0.3741 -0.0952 0.0216  -0.0703 166 PHE A CG  
1358 C CD1 . PHE A 169 ? 0.5593 0.4465 0.4184 -0.1035 0.0277  -0.0790 166 PHE A CD1 
1359 C CD2 . PHE A 169 ? 0.4986 0.4037 0.3827 -0.0991 0.0200  -0.0677 166 PHE A CD2 
1360 C CE1 . PHE A 169 ? 0.6093 0.4711 0.4512 -0.1154 0.0336  -0.0855 166 PHE A CE1 
1361 C CE2 . PHE A 169 ? 0.5432 0.4238 0.4103 -0.1106 0.0257  -0.0732 166 PHE A CE2 
1362 C CZ  . PHE A 169 ? 0.5808 0.4385 0.4267 -0.1192 0.0330  -0.0824 166 PHE A CZ  
1363 N N   . PRO A 170 ? 0.5561 0.5291 0.4555 -0.0784 0.0137  -0.0576 167 PRO A N   
1364 C CA  . PRO A 170 ? 0.5603 0.5444 0.4687 -0.0686 0.0159  -0.0509 167 PRO A CA  
1365 C C   . PRO A 170 ? 0.4788 0.4537 0.4005 -0.0591 0.0228  -0.0506 167 PRO A C   
1366 O O   . PRO A 170 ? 0.5043 0.4881 0.4396 -0.0532 0.0245  -0.0455 167 PRO A O   
1367 C CB  . PRO A 170 ? 0.5909 0.5753 0.4812 -0.0704 0.0181  -0.0529 167 PRO A CB  
1368 C CG  . PRO A 170 ? 0.6125 0.5774 0.4868 -0.0789 0.0205  -0.0633 167 PRO A CG  
1369 C CD  . PRO A 170 ? 0.6313 0.5940 0.5092 -0.0868 0.0160  -0.0655 167 PRO A CD  
1370 N N   . ASP A 171 ? 0.4963 0.4540 0.4139 -0.0580 0.0273  -0.0566 168 ASP A N   
1371 C CA  . ASP A 171 ? 0.4979 0.4519 0.4275 -0.0487 0.0338  -0.0576 168 ASP A CA  
1372 C C   . ASP A 171 ? 0.4620 0.4158 0.4038 -0.0446 0.0318  -0.0574 168 ASP A C   
1373 O O   . ASP A 171 ? 0.4671 0.4197 0.4167 -0.0365 0.0365  -0.0595 168 ASP A O   
1374 C CB  . ASP A 171 ? 0.5064 0.4449 0.4231 -0.0466 0.0414  -0.0633 168 ASP A CB  
1375 C CG  . ASP A 171 ? 0.6104 0.5290 0.5082 -0.0523 0.0416  -0.0687 168 ASP A CG  
1376 O OD1 . ASP A 171 ? 0.6655 0.5837 0.5600 -0.0597 0.0357  -0.0682 168 ASP A OD1 
1377 O OD2 . ASP A 171 ? 0.6877 0.5904 0.5734 -0.0501 0.0490  -0.0739 168 ASP A OD2 
1378 N N   . ARG A 172 ? 0.4793 0.3796 0.3756 -0.0732 0.0601  -0.0252 169 ARG A N   
1379 C CA  . ARG A 172 ? 0.4426 0.3507 0.3600 -0.0725 0.0527  -0.0324 169 ARG A CA  
1380 C C   . ARG A 172 ? 0.4306 0.3498 0.3599 -0.0671 0.0479  -0.0264 169 ARG A C   
1381 O O   . ARG A 172 ? 0.4634 0.3857 0.3823 -0.0630 0.0478  -0.0153 169 ARG A O   
1382 C CB  . ARG A 172 ? 0.4662 0.3773 0.3724 -0.0776 0.0421  -0.0343 169 ARG A CB  
1383 C CG  . ARG A 172 ? 0.4763 0.3724 0.3692 -0.0830 0.0477  -0.0419 169 ARG A CG  
1384 C CD  . ARG A 172 ? 0.5119 0.4009 0.4205 -0.0765 0.0530  -0.0508 169 ARG A CD  
1385 N NE  . ARG A 172 ? 0.5039 0.3764 0.3998 -0.0791 0.0616  -0.0575 169 ARG A NE  
1386 C CZ  . ARG A 172 ? 0.5066 0.3733 0.4117 -0.0709 0.0671  -0.0653 169 ARG A CZ  
1387 N NH1 . ARG A 172 ? 0.5060 0.3858 0.4312 -0.0592 0.0626  -0.0673 169 ARG A NH1 
1388 N NH2 . ARG A 172 ? 0.5600 0.4102 0.4525 -0.0727 0.0768  -0.0712 169 ARG A NH2 
1389 N N   . ARG A 173 ? 0.4459 0.3725 0.3959 -0.0650 0.0447  -0.0342 170 ARG A N   
1390 C CA  . ARG A 173 ? 0.4541 0.3921 0.4148 -0.0609 0.0394  -0.0309 170 ARG A CA  
1391 C C   . ARG A 173 ? 0.4763 0.4243 0.4237 -0.0624 0.0268  -0.0235 170 ARG A C   
1392 O O   . ARG A 173 ? 0.5042 0.4493 0.4354 -0.0686 0.0238  -0.0232 170 ARG A O   
1393 C CB  . ARG A 173 ? 0.4619 0.4107 0.4451 -0.0583 0.0379  -0.0432 170 ARG A CB  
1394 C CG  . ARG A 173 ? 0.4814 0.4301 0.4833 -0.0603 0.0506  -0.0568 170 ARG A CG  
1395 C CD  . ARG A 173 ? 0.5321 0.5032 0.5579 -0.0576 0.0474  -0.0710 170 ARG A CD  
1396 N NE  . ARG A 173 ? 0.4616 0.4440 0.5107 -0.0622 0.0589  -0.0898 170 ARG A NE  
1397 C CZ  . ARG A 173 ? 0.6478 0.6172 0.7050 -0.0713 0.0774  -0.0954 170 ARG A CZ  
1398 N NH1 . ARG A 173 ? 0.6708 0.6124 0.7108 -0.0724 0.0862  -0.0801 170 ARG A NH1 
1399 N NH2 . ARG A 173 ? 0.6248 0.6101 0.7067 -0.0786 0.0887  -0.1165 170 ARG A NH2 
1400 N N   . SER A 174 ? 0.4033 0.3639 0.3582 -0.0586 0.0216  -0.0195 171 SER A N   
1401 C CA  . SER A 174 ? 0.3874 0.3626 0.3350 -0.0616 0.0116  -0.0147 171 SER A CA  
1402 C C   . SER A 174 ? 0.3915 0.3741 0.3518 -0.0586 0.0074  -0.0180 171 SER A C   
1403 O O   . SER A 174 ? 0.3887 0.3721 0.3641 -0.0527 0.0110  -0.0224 171 SER A O   
1404 C CB  . SER A 174 ? 0.4218 0.4118 0.3622 -0.0575 0.0096  -0.0045 171 SER A CB  
1405 O OG  . SER A 174 ? 0.4226 0.4348 0.3615 -0.0619 0.0005  -0.0031 171 SER A OG  
1406 N N   . ILE A 175 ? 0.3837 0.3717 0.3366 -0.0639 0.0018  -0.0172 172 ILE A N   
1407 C CA  . ILE A 175 ? 0.3947 0.3889 0.3544 -0.0601 -0.0011 -0.0184 172 ILE A CA  
1408 C C   . ILE A 175 ? 0.4024 0.4160 0.3705 -0.0572 -0.0034 -0.0135 172 ILE A C   
1409 O O   . ILE A 175 ? 0.3852 0.4059 0.3618 -0.0522 -0.0043 -0.0152 172 ILE A O   
1410 C CB  . ILE A 175 ? 0.4137 0.3981 0.3585 -0.0667 -0.0012 -0.0184 172 ILE A CB  
1411 C CG1 . ILE A 175 ? 0.4301 0.4151 0.3762 -0.0586 -0.0022 -0.0185 172 ILE A CG1 
1412 C CG2 . ILE A 175 ? 0.4189 0.4137 0.3552 -0.0802 -0.0021 -0.0162 172 ILE A CG2 
1413 C CD1 . ILE A 175 ? 0.4217 0.4064 0.3759 -0.0454 -0.0028 -0.0244 172 ILE A CD1 
1414 N N   . GLY A 176 ? 0.3770 0.4018 0.3412 -0.0583 -0.0043 -0.0075 173 GLY A N   
1415 C CA  . GLY A 176 ? 0.4188 0.4647 0.3903 -0.0512 -0.0059 -0.0014 173 GLY A CA  
1416 C C   . GLY A 176 ? 0.4052 0.4707 0.3787 -0.0572 -0.0104 -0.0022 173 GLY A C   
1417 O O   . GLY A 176 ? 0.4070 0.4679 0.3721 -0.0693 -0.0111 -0.0063 173 GLY A O   
1418 N N   . TRP A 177 ? 0.3878 0.4719 0.3717 -0.0484 -0.0106 0.0015  174 TRP A N   
1419 C CA  . TRP A 177 ? 0.3616 0.4669 0.3498 -0.0536 -0.0128 0.0002  174 TRP A CA  
1420 C C   . TRP A 177 ? 0.3842 0.4715 0.3701 -0.0571 -0.0105 -0.0047 174 TRP A C   
1421 O O   . TRP A 177 ? 0.3960 0.4823 0.3736 -0.0680 -0.0093 -0.0066 174 TRP A O   
1422 C CB  . TRP A 177 ? 0.3685 0.4979 0.3688 -0.0401 -0.0123 0.0055  174 TRP A CB  
1423 C CG  . TRP A 177 ? 0.3684 0.5188 0.3754 -0.0449 -0.0124 0.0028  174 TRP A CG  
1424 C CD1 . TRP A 177 ? 0.4274 0.5928 0.4308 -0.0618 -0.0134 -0.0016 174 TRP A CD1 
1425 C CD2 . TRP A 177 ? 0.3889 0.5486 0.4073 -0.0337 -0.0088 0.0036  174 TRP A CD2 
1426 N NE1 . TRP A 177 ? 0.4352 0.6178 0.4466 -0.0622 -0.0105 -0.0030 174 TRP A NE1 
1427 C CE2 . TRP A 177 ? 0.4343 0.6157 0.4551 -0.0441 -0.0087 0.0003  174 TRP A CE2 
1428 C CE3 . TRP A 177 ? 0.4344 0.5829 0.4602 -0.0174 -0.0027 0.0054  174 TRP A CE3 
1429 C CZ2 . TRP A 177 ? 0.4590 0.6538 0.4893 -0.0373 -0.0046 -0.0004 174 TRP A CZ2 
1430 C CZ3 . TRP A 177 ? 0.4211 0.5815 0.4562 -0.0109 0.0014  0.0036  174 TRP A CZ3 
1431 C CH2 . TRP A 177 ? 0.4453 0.6300 0.4826 -0.0199 -0.0003 0.0011  174 TRP A CH2 
1432 N N   . ILE A 178 ? 0.3564 0.4307 0.3487 -0.0472 -0.0081 -0.0076 175 ILE A N   
1433 C CA  . ILE A 178 ? 0.3877 0.4518 0.3767 -0.0457 -0.0077 -0.0130 175 ILE A CA  
1434 C C   . ILE A 178 ? 0.3683 0.4168 0.3592 -0.0418 -0.0069 -0.0189 175 ILE A C   
1435 O O   . ILE A 178 ? 0.3555 0.4017 0.3570 -0.0380 -0.0031 -0.0215 175 ILE A O   
1436 C CB  . ILE A 178 ? 0.3903 0.4671 0.3882 -0.0387 -0.0061 -0.0161 175 ILE A CB  
1437 C CG1 . ILE A 178 ? 0.3873 0.4841 0.3866 -0.0421 -0.0056 -0.0110 175 ILE A CG1 
1438 C CG2 . ILE A 178 ? 0.4377 0.5094 0.4285 -0.0347 -0.0072 -0.0221 175 ILE A CG2 
1439 C CD1 . ILE A 178 ? 0.3892 0.4979 0.3972 -0.0343 -0.0024 -0.0143 175 ILE A CD1 
1440 N N   . GLY A 179 ? 0.3752 0.4123 0.3552 -0.0419 -0.0082 -0.0210 176 GLY A N   
1441 C CA  . GLY A 179 ? 0.3880 0.4178 0.3727 -0.0375 -0.0077 -0.0282 176 GLY A CA  
1442 C C   . GLY A 179 ? 0.3834 0.4110 0.3585 -0.0291 -0.0101 -0.0313 176 GLY A C   
1443 O O   . GLY A 179 ? 0.4001 0.4231 0.3593 -0.0268 -0.0103 -0.0251 176 GLY A O   
1444 N N   . PHE A 180 ? 0.3478 0.3799 0.3322 -0.0234 -0.0104 -0.0408 177 PHE A N   
1445 C CA  . PHE A 180 ? 0.3832 0.4212 0.3604 -0.0099 -0.0137 -0.0445 177 PHE A CA  
1446 C C   . PHE A 180 ? 0.4086 0.4322 0.3813 -0.0079 -0.0111 -0.0443 177 PHE A C   
1447 O O   . PHE A 180 ? 0.3843 0.4096 0.3720 -0.0141 -0.0080 -0.0515 177 PHE A O   
1448 C CB  . PHE A 180 ? 0.3797 0.4499 0.3765 -0.0028 -0.0172 -0.0614 177 PHE A CB  
1449 C CG  . PHE A 180 ? 0.3873 0.4753 0.3793 0.0148  -0.0226 -0.0671 177 PHE A CG  
1450 C CD1 . PHE A 180 ? 0.4228 0.5084 0.3898 0.0311  -0.0262 -0.0566 177 PHE A CD1 
1451 C CD2 . PHE A 180 ? 0.3922 0.4997 0.4032 0.0170  -0.0225 -0.0819 177 PHE A CD2 
1452 C CE1 . PHE A 180 ? 0.4178 0.5217 0.3771 0.0535  -0.0311 -0.0592 177 PHE A CE1 
1453 C CE2 . PHE A 180 ? 0.3873 0.5192 0.3955 0.0370  -0.0284 -0.0873 177 PHE A CE2 
1454 C CZ  . PHE A 180 ? 0.3992 0.5298 0.3803 0.0574  -0.0335 -0.0749 177 PHE A CZ  
1455 N N   . CYS A 181 ? 0.4175 0.4241 0.3674 0.0019  -0.0100 -0.0357 178 CYS A N   
1456 C CA  . CYS A 181 ? 0.4432 0.4329 0.3845 0.0082  -0.0058 -0.0347 178 CYS A CA  
1457 C C   . CYS A 181 ? 0.4735 0.4773 0.4072 0.0338  -0.0094 -0.0356 178 CYS A C   
1458 O O   . CYS A 181 ? 0.4956 0.4926 0.4082 0.0454  -0.0093 -0.0260 178 CYS A O   
1459 C CB  . CYS A 181 ? 0.5078 0.4583 0.4247 -0.0019 0.0027  -0.0235 178 CYS A CB  
1460 S SG  . CYS A 181 ? 0.5409 0.4617 0.4411 0.0081  0.0117  -0.0217 178 CYS A SG  
1461 N N   . PRO A 182 ? 0.4420 0.4686 0.3912 0.0451  -0.0118 -0.0468 179 PRO A N   
1462 C CA  . PRO A 182 ? 0.4779 0.5309 0.4220 0.0737  -0.0175 -0.0491 179 PRO A CA  
1463 C C   . PRO A 182 ? 0.5252 0.5440 0.4361 0.0954  -0.0102 -0.0329 179 PRO A C   
1464 O O   . PRO A 182 ? 0.5261 0.5618 0.4383 0.1183  -0.0115 -0.0363 179 PRO A O   
1465 C CB  . PRO A 182 ? 0.4589 0.5520 0.4364 0.0736  -0.0206 -0.0698 179 PRO A CB  
1466 C CG  . PRO A 182 ? 0.4610 0.5224 0.4435 0.0528  -0.0109 -0.0688 179 PRO A CG  
1467 C CD  . PRO A 182 ? 0.4365 0.4681 0.4079 0.0325  -0.0083 -0.0580 179 PRO A CD  
1468 N N   . HIS A 183 ? 0.5448 0.5155 0.4262 0.0879  -0.0005 -0.0165 180 HIS A N   
1469 C CA  . HIS A 183 ? 0.5937 0.5210 0.4388 0.1071  0.0118  -0.0007 180 HIS A CA  
1470 C C   . HIS A 183 ? 0.6468 0.5367 0.4612 0.1011  0.0214  0.0143  180 HIS A C   
1471 O O   . HIS A 183 ? 0.6398 0.5323 0.4641 0.0753  0.0197  0.0115  180 HIS A O   
1472 C CB  . HIS A 183 ? 0.6160 0.5021 0.4549 0.0948  0.0248  -0.0001 180 HIS A CB  
1473 C CG  . HIS A 183 ? 0.6201 0.5323 0.4874 0.0933  0.0203  -0.0146 180 HIS A CG  
1474 N ND1 . HIS A 183 ? 0.6647 0.5829 0.5297 0.1203  0.0228  -0.0155 180 HIS A ND1 
1475 C CD2 . HIS A 183 ? 0.5920 0.5298 0.4905 0.0717  0.0143  -0.0286 180 HIS A CD2 
1476 C CE1 . HIS A 183 ? 0.6759 0.6217 0.5713 0.1111  0.0194  -0.0311 180 HIS A CE1 
1477 N NE2 . HIS A 183 ? 0.6112 0.5657 0.5253 0.0813  0.0152  -0.0385 180 HIS A NE2 
1478 N N   . PRO A 184 ? 0.7076 0.5617 0.4831 0.1260  0.0337  0.0311  181 PRO A N   
1479 C CA  . PRO A 184 ? 0.7480 0.5578 0.4911 0.1178  0.0488  0.0455  181 PRO A CA  
1480 C C   . PRO A 184 ? 0.7121 0.4780 0.4530 0.0826  0.0641  0.0426  181 PRO A C   
1481 O O   . PRO A 184 ? 0.7734 0.5245 0.5191 0.0782  0.0687  0.0370  181 PRO A O   
1482 C CB  . PRO A 184 ? 0.8357 0.6100 0.5344 0.1565  0.0626  0.0649  181 PRO A CB  
1483 C CG  . PRO A 184 ? 0.8224 0.6433 0.5359 0.1908  0.0474  0.0592  181 PRO A CG  
1484 C CD  . PRO A 184 ? 0.7353 0.5901 0.4948 0.1655  0.0355  0.0377  181 PRO A CD  
1485 N N   . LEU A 185 ? 0.7575 0.5099 0.4936 0.0565  0.0712  0.0438  182 LEU A N   
1486 C CA  . LEU A 185 ? 0.7359 0.4582 0.4714 0.0210  0.0846  0.0376  182 LEU A CA  
1487 C C   . LEU A 185 ? 0.8063 0.4811 0.5085 0.0105  0.1082  0.0474  182 LEU A C   
1488 O O   . LEU A 185 ? 0.8315 0.5105 0.5205 0.0236  0.1087  0.0574  182 LEU A O   
1489 C CB  . LEU A 185 ? 0.6684 0.4383 0.4418 -0.0051 0.0676  0.0239  182 LEU A CB  
1490 C CG  . LEU A 185 ? 0.6404 0.4506 0.4457 0.0001  0.0493  0.0135  182 LEU A CG  
1491 C CD1 . LEU A 185 ? 0.5961 0.4410 0.4300 -0.0238 0.0383  0.0041  182 LEU A CD1 
1492 C CD2 . LEU A 185 ? 0.6977 0.4833 0.4976 0.0014  0.0568  0.0099  182 LEU A CD2 
1493 N N   . ARG A 186 ? 0.8428 0.4729 0.5310 -0.0151 0.1294  0.0425  183 ARG A N   
1494 C CA  . ARG A 186 ? 0.9399 0.5191 0.5969 -0.0314 0.1578  0.0481  183 ARG A CA  
1495 C C   . ARG A 186 ? 0.8899 0.4955 0.5707 -0.0752 0.1570  0.0316  183 ARG A C   
1496 O O   . ARG A 186 ? 0.8502 0.4786 0.5539 -0.0967 0.1484  0.0161  183 ARG A O   
1497 C CB  . ARG A 186 ? 1.0805 0.5854 0.7007 -0.0264 0.1875  0.0530  183 ARG A CB  
1498 C CG  . ARG A 186 ? 1.1370 0.6251 0.7358 0.0230  0.1861  0.0701  183 ARG A CG  
1499 C CD  . ARG A 186 ? 1.2947 0.7036 0.8534 0.0342  0.2183  0.0778  183 ARG A CD  
1500 N NE  . ARG A 186 ? 1.4875 0.8233 1.0022 0.0259  0.2556  0.0887  183 ARG A NE  
1501 C CZ  . ARG A 186 ? 1.5329 0.8497 1.0167 0.0515  0.2648  0.1097  183 ARG A CZ  
1502 N NH1 . ARG A 186 ? 1.4388 0.8099 0.9317 0.0878  0.2370  0.1203  183 ARG A NH1 
1503 N NH2 . ARG A 186 ? 1.6014 0.8440 1.0434 0.0400  0.3039  0.1188  183 ARG A NH2 
1504 N N   . ALA A 187 ? 0.9538 0.5584 0.6273 -0.0865 0.1667  0.0352  184 ALA A N   
1505 C CA  . ALA A 187 ? 0.9174 0.5556 0.6146 -0.1248 0.1662  0.0197  184 ALA A CA  
1506 C C   . ALA A 187 ? 0.9808 0.5957 0.6759 -0.1617 0.1849  0.0018  184 ALA A C   
1507 O O   . ALA A 187 ? 0.9126 0.5752 0.6370 -0.1893 0.1738  -0.0157 184 ALA A O   
1508 C CB  . ALA A 187 ? 0.9866 0.6155 0.6693 -0.1288 0.1808  0.0275  184 ALA A CB  
1509 N N   . THR A 188 ? 1.0907 0.6335 0.7496 -0.1604 0.2137  0.0059  185 THR A N   
1510 C CA  . THR A 188 ? 1.1612 0.6729 0.8129 -0.1973 0.2371  -0.0134 185 THR A CA  
1511 C C   . THR A 188 ? 1.0775 0.6290 0.7556 -0.2054 0.2154  -0.0292 185 THR A C   
1512 O O   . THR A 188 ? 1.1316 0.6866 0.8151 -0.2416 0.2256  -0.0514 185 THR A O   
1513 C CB  . THR A 188 ? 1.2804 0.6965 0.8832 -0.1887 0.2761  -0.0033 185 THR A CB  
1514 O OG1 . THR A 188 ? 1.3521 0.7506 0.9430 -0.1457 0.2659  0.0126  185 THR A OG1 
1515 C CG2 . THR A 188 ? 1.3778 0.7490 0.9487 -0.1827 0.3023  0.0129  185 THR A CG2 
1516 N N   . ASP A 189 ? 0.9710 0.5546 0.6650 -0.1736 0.1870  -0.0197 186 ASP A N   
1517 C CA  . ASP A 189 ? 0.9650 0.5818 0.6804 -0.1797 0.1692  -0.0326 186 ASP A CA  
1518 C C   . ASP A 189 ? 0.8590 0.5532 0.6116 -0.1927 0.1422  -0.0419 186 ASP A C   
1519 O O   . ASP A 189 ? 0.9344 0.6586 0.7020 -0.2020 0.1296  -0.0533 186 ASP A O   
1520 C CB  . ASP A 189 ? 0.9069 0.5204 0.6227 -0.1424 0.1554  -0.0209 186 ASP A CB  
1521 C CG  . ASP A 189 ? 1.0469 0.5895 0.7268 -0.1221 0.1797  -0.0110 186 ASP A CG  
1522 O OD1 . ASP A 189 ? 1.1933 0.6901 0.8539 -0.1432 0.2041  -0.0220 186 ASP A OD1 
1523 O OD2 . ASP A 189 ? 1.0737 0.6102 0.7456 -0.0843 0.1740  0.0061  186 ASP A OD2 
1524 N N   . PHE A 190 ? 0.8708 0.5958 0.6359 -0.1916 0.1347  -0.0362 187 PHE A N   
1525 C CA  . PHE A 190 ? 0.7631 0.5589 0.5620 -0.1979 0.1104  -0.0426 187 PHE A CA  
1526 C C   . PHE A 190 ? 0.7890 0.6144 0.5980 -0.2301 0.1180  -0.0562 187 PHE A C   
1527 O O   . PHE A 190 ? 0.7819 0.5719 0.5729 -0.2477 0.1430  -0.0594 187 PHE A O   
1528 C CB  . PHE A 190 ? 0.7254 0.5476 0.5391 -0.1667 0.0902  -0.0275 187 PHE A CB  
1529 C CG  . PHE A 190 ? 0.6549 0.4680 0.4687 -0.1395 0.0792  -0.0203 187 PHE A CG  
1530 C CD1 . PHE A 190 ? 0.6958 0.4603 0.4850 -0.1206 0.0913  -0.0114 187 PHE A CD1 
1531 C CD2 . PHE A 190 ? 0.6215 0.4734 0.4585 -0.1342 0.0599  -0.0237 187 PHE A CD2 
1532 C CE1 . PHE A 190 ? 0.6671 0.4316 0.4604 -0.0969 0.0815  -0.0079 187 PHE A CE1 
1533 C CE2 . PHE A 190 ? 0.5927 0.4373 0.4317 -0.1138 0.0531  -0.0202 187 PHE A CE2 
1534 C CZ  . PHE A 190 ? 0.6264 0.4315 0.4461 -0.0959 0.0629  -0.0137 187 PHE A CZ  
1535 N N   . PRO A 191 ? 0.7334 0.6261 0.5713 -0.2377 0.0980  -0.0650 188 PRO A N   
1536 C CA  . PRO A 191 ? 0.7840 0.7214 0.6377 -0.2656 0.1016  -0.0798 188 PRO A CA  
1537 C C   . PRO A 191 ? 0.8066 0.7415 0.6612 -0.2622 0.1098  -0.0710 188 PRO A C   
1538 O O   . PRO A 191 ? 0.6965 0.6115 0.5447 -0.2337 0.1046  -0.0525 188 PRO A O   
1539 C CB  . PRO A 191 ? 0.7159 0.7257 0.5979 -0.2576 0.0742  -0.0827 188 PRO A CB  
1540 C CG  . PRO A 191 ? 0.7372 0.7296 0.6122 -0.2389 0.0633  -0.0763 188 PRO A CG  
1541 C CD  . PRO A 191 ? 0.7228 0.6520 0.5780 -0.2188 0.0730  -0.0611 188 PRO A CD  
1542 N N   . ALA A 192 ? 0.8167 0.7773 0.6802 -0.2925 0.1227  -0.0864 189 ALA A N   
1543 C CA  . ALA A 192 ? 0.8201 0.7809 0.6845 -0.2940 0.1337  -0.0805 189 ALA A CA  
1544 C C   . ALA A 192 ? 0.7814 0.7948 0.6708 -0.2675 0.1085  -0.0692 189 ALA A C   
1545 O O   . ALA A 192 ? 0.7904 0.7926 0.6750 -0.2546 0.1130  -0.0572 189 ALA A O   
1546 C CB  . ALA A 192 ? 0.8555 0.8399 0.7287 -0.3361 0.1539  -0.1040 189 ALA A CB  
1547 N N   . ALA A 193 ? 0.6556 0.7235 0.5689 -0.2587 0.0842  -0.0728 190 ALA A N   
1548 C CA  . ALA A 193 ? 0.6407 0.7539 0.5765 -0.2334 0.0634  -0.0629 190 ALA A CA  
1549 C C   . ALA A 193 ? 0.6401 0.7173 0.5657 -0.2003 0.0545  -0.0440 190 ALA A C   
1550 O O   . ALA A 193 ? 0.6421 0.7427 0.5817 -0.1800 0.0430  -0.0359 190 ALA A O   
1551 C CB  . ALA A 193 ? 0.6508 0.8254 0.6088 -0.2316 0.0442  -0.0705 190 ALA A CB  
1552 N N   . THR A 194 ? 0.5852 0.6087 0.4874 -0.1954 0.0608  -0.0392 191 THR A N   
1553 C CA  . THR A 194 ? 0.6065 0.6039 0.5012 -0.1657 0.0524  -0.0252 191 THR A CA  
1554 C C   . THR A 194 ? 0.6553 0.6185 0.5303 -0.1549 0.0641  -0.0149 191 THR A C   
1555 O O   . THR A 194 ? 0.6718 0.5979 0.5240 -0.1682 0.0849  -0.0148 191 THR A O   
1556 C CB  . THR A 194 ? 0.6135 0.5765 0.4941 -0.1612 0.0526  -0.0250 191 THR A CB  
1557 O OG1 . THR A 194 ? 0.5812 0.5770 0.4778 -0.1648 0.0394  -0.0318 191 THR A OG1 
1558 C CG2 . THR A 194 ? 0.6506 0.5900 0.5239 -0.1324 0.0464  -0.0137 191 THR A CG2 
1559 N N   . GLU A 195 ? 0.5737 0.5501 0.4561 -0.1310 0.0523  -0.0069 192 GLU A N   
1560 C CA  . GLU A 195 ? 0.5964 0.5472 0.4580 -0.1150 0.0596  0.0032  192 GLU A CA  
1561 C C   . GLU A 195 ? 0.5834 0.5177 0.4374 -0.0896 0.0501  0.0088  192 GLU A C   
1562 O O   . GLU A 195 ? 0.5490 0.5084 0.4245 -0.0810 0.0343  0.0048  192 GLU A O   
1563 C CB  . GLU A 195 ? 0.5708 0.5545 0.4457 -0.1078 0.0544  0.0044  192 GLU A CB  
1564 C CG  . GLU A 195 ? 0.6244 0.5860 0.4752 -0.0866 0.0585  0.0145  192 GLU A CG  
1565 C CD  . GLU A 195 ? 0.6240 0.6138 0.4826 -0.0769 0.0543  0.0149  192 GLU A CD  
1566 O OE1 . GLU A 195 ? 0.5931 0.6194 0.4779 -0.0861 0.0497  0.0081  192 GLU A OE1 
1567 O OE2 . GLU A 195 ? 0.5652 0.5417 0.4020 -0.0578 0.0557  0.0219  192 GLU A OE2 
1568 N N   . LEU A 196 ? 0.5992 0.4910 0.4219 -0.0778 0.0619  0.0177  193 LEU A N   
1569 C CA  . LEU A 196 ? 0.5866 0.4684 0.4009 -0.0509 0.0538  0.0226  193 LEU A CA  
1570 C C   . LEU A 196 ? 0.6282 0.5183 0.4298 -0.0270 0.0507  0.0300  193 LEU A C   
1571 O O   . LEU A 196 ? 0.6482 0.5149 0.4231 -0.0257 0.0656  0.0392  193 LEU A O   
1572 C CB  . LEU A 196 ? 0.6512 0.4814 0.4360 -0.0482 0.0698  0.0286  193 LEU A CB  
1573 C CG  . LEU A 196 ? 0.6687 0.4861 0.4601 -0.0712 0.0750  0.0194  193 LEU A CG  
1574 C CD1 . LEU A 196 ? 0.7672 0.5307 0.5283 -0.0618 0.0911  0.0254  193 LEU A CD1 
1575 C CD2 . LEU A 196 ? 0.6087 0.4660 0.4327 -0.0720 0.0547  0.0100  193 LEU A CD2 
1576 N N   . VAL A 197 ? 0.5522 0.4758 0.3715 -0.0093 0.0331  0.0246  194 VAL A N   
1577 C CA  . VAL A 197 ? 0.5729 0.5132 0.3812 0.0138  0.0277  0.0276  194 VAL A CA  
1578 C C   . VAL A 197 ? 0.5715 0.5121 0.3708 0.0401  0.0207  0.0286  194 VAL A C   
1579 O O   . VAL A 197 ? 0.5489 0.5141 0.3745 0.0413  0.0085  0.0170  194 VAL A O   
1580 C CB  . VAL A 197 ? 0.5404 0.5262 0.3779 0.0108  0.0150  0.0158  194 VAL A CB  
1581 C CG1 . VAL A 197 ? 0.5877 0.5948 0.4123 0.0334  0.0094  0.0154  194 VAL A CG1 
1582 C CG2 . VAL A 197 ? 0.5826 0.5735 0.4316 -0.0118 0.0215  0.0150  194 VAL A CG2 
1583 N N   . ASP A 198 ? 0.6544 0.5668 0.4152 0.0621  0.0307  0.0429  195 ASP A N   
1584 C CA  . ASP A 198 ? 0.6499 0.5660 0.3987 0.0927  0.0249  0.0459  195 ASP A CA  
1585 C C   . ASP A 198 ? 0.6780 0.6524 0.4407 0.1128  0.0058  0.0348  195 ASP A C   
1586 O O   . ASP A 198 ? 0.7243 0.7145 0.4751 0.1193  0.0046  0.0367  195 ASP A O   
1587 C CB  . ASP A 198 ? 0.7369 0.6024 0.4352 0.1156  0.0436  0.0674  195 ASP A CB  
1588 C CG  . ASP A 198 ? 0.8049 0.6780 0.4899 0.1531  0.0376  0.0719  195 ASP A CG  
1589 O OD1 . ASP A 198 ? 0.8565 0.7305 0.5609 0.1498  0.0338  0.0641  195 ASP A OD1 
1590 O OD2 . ASP A 198 ? 0.8716 0.7530 0.5265 0.1868  0.0367  0.0831  195 ASP A OD2 
1591 N N   . ILE A 199 ? 0.6323 0.6402 0.4202 0.1211  -0.0074 0.0212  196 ILE A N   
1592 C CA  . ILE A 199 ? 0.6544 0.7234 0.4596 0.1371  -0.0245 0.0049  196 ILE A CA  
1593 C C   . ILE A 199 ? 0.6629 0.7438 0.4527 0.1717  -0.0287 0.0089  196 ILE A C   
1594 O O   . ILE A 199 ? 0.6196 0.7124 0.4324 0.1707  -0.0329 -0.0010 196 ILE A O   
1595 C CB  . ILE A 199 ? 0.6277 0.7314 0.4813 0.1129  -0.0338 -0.0191 196 ILE A CB  
1596 C CG1 . ILE A 199 ? 0.6594 0.7432 0.5271 0.0817  -0.0273 -0.0191 196 ILE A CG1 
1597 C CG2 . ILE A 199 ? 0.6682 0.8349 0.5399 0.1236  -0.0478 -0.0405 196 ILE A CG2 
1598 C CD1 . ILE A 199 ? 0.7222 0.8103 0.5770 0.0800  -0.0248 -0.0152 196 ILE A CD1 
1599 N N   . PRO A 200 ? 0.7273 0.8038 0.4754 0.2056  -0.0261 0.0253  197 PRO A N   
1600 C CA  . PRO A 200 ? 0.7480 0.8372 0.4777 0.2455  -0.0296 0.0321  197 PRO A CA  
1601 C C   . PRO A 200 ? 0.7096 0.8768 0.4805 0.2523  -0.0501 0.0045  197 PRO A C   
1602 O O   . PRO A 200 ? 0.7536 0.9751 0.5492 0.2420  -0.0629 -0.0168 197 PRO A O   
1603 C CB  . PRO A 200 ? 0.8301 0.9147 0.5089 0.2814  -0.0257 0.0522  197 PRO A CB  
1604 C CG  . PRO A 200 ? 0.8221 0.9081 0.5011 0.2575  -0.0245 0.0489  197 PRO A CG  
1605 C CD  . PRO A 200 ? 0.7952 0.8559 0.5098 0.2103  -0.0187 0.0390  197 PRO A CD  
1606 N N   . GLY A 201 ? 0.7525 0.9240 0.5316 0.2674  -0.0507 0.0032  198 GLY A N   
1607 C CA  . GLY A 201 ? 0.8062 1.0521 0.6270 0.2717  -0.0671 -0.0247 198 GLY A CA  
1608 C C   . GLY A 201 ? 0.7636 1.0172 0.6340 0.2271  -0.0676 -0.0484 198 GLY A C   
1609 O O   . GLY A 201 ? 0.6852 0.9999 0.5944 0.2210  -0.0780 -0.0763 198 GLY A O   
1610 N N   . ARG A 202 ? 0.6883 0.8811 0.5564 0.1962  -0.0550 -0.0380 199 ARG A N   
1611 C CA  . ARG A 202 ? 0.6145 0.8077 0.5222 0.1584  -0.0535 -0.0554 199 ARG A CA  
1612 C C   . ARG A 202 ? 0.5828 0.7113 0.4823 0.1399  -0.0396 -0.0405 199 ARG A C   
1613 O O   . ARG A 202 ? 0.5525 0.6785 0.4718 0.1309  -0.0370 -0.0482 199 ARG A O   
1614 C CB  . ARG A 202 ? 0.6200 0.8247 0.5399 0.1357  -0.0558 -0.0649 199 ARG A CB  
1615 C CG  . ARG A 202 ? 0.6621 0.9354 0.5994 0.1430  -0.0683 -0.0889 199 ARG A CG  
1616 C CD  . ARG A 202 ? 0.6310 0.9516 0.6123 0.1313  -0.0723 -0.1190 199 ARG A CD  
1617 N NE  . ARG A 202 ? 0.6155 1.0022 0.6177 0.1297  -0.0814 -0.1480 199 ARG A NE  
1618 C CZ  . ARG A 202 ? 0.7247 1.1668 0.7149 0.1580  -0.0943 -0.1551 199 ARG A CZ  
1619 N NH1 . ARG A 202 ? 0.8094 1.2464 0.7656 0.1945  -0.0987 -0.1327 199 ARG A NH1 
1620 N NH2 . ARG A 202 ? 0.7032 1.2072 0.7147 0.1508  -0.1015 -0.1860 199 ARG A NH2 
1621 N N   . GLY A 203 ? 0.5616 0.6415 0.4327 0.1324  -0.0300 -0.0213 200 GLY A N   
1622 C CA  . GLY A 203 ? 0.5436 0.5686 0.4068 0.1115  -0.0169 -0.0107 200 GLY A CA  
1623 C C   . GLY A 203 ? 0.5469 0.5417 0.3953 0.0923  -0.0092 -0.0003 200 GLY A C   
1624 O O   . GLY A 203 ? 0.5833 0.5677 0.4038 0.1053  -0.0053 0.0115  200 GLY A O   
1625 N N   . THR A 204 ? 0.4893 0.4750 0.3568 0.0627  -0.0070 -0.0053 201 THR A N   
1626 C CA  . THR A 204 ? 0.5099 0.4745 0.3686 0.0430  0.0001  0.0020  201 THR A CA  
1627 C C   . THR A 204 ? 0.5138 0.5013 0.4034 0.0209  -0.0055 -0.0085 201 THR A C   
1628 O O   . THR A 204 ? 0.4816 0.4780 0.3930 0.0127  -0.0087 -0.0173 201 THR A O   
1629 C CB  . THR A 204 ? 0.5560 0.4721 0.3947 0.0298  0.0150  0.0113  201 THR A CB  
1630 O OG1 . THR A 204 ? 0.6030 0.4891 0.4116 0.0525  0.0241  0.0218  201 THR A OG1 
1631 C CG2 . THR A 204 ? 0.5952 0.4934 0.4241 0.0084  0.0247  0.0166  201 THR A CG2 
1632 N N   . LEU A 205 ? 0.4950 0.4893 0.3836 0.0135  -0.0047 -0.0061 202 LEU A N   
1633 C CA  . LEU A 205 ? 0.4520 0.4621 0.3642 -0.0042 -0.0070 -0.0120 202 LEU A CA  
1634 C C   . LEU A 205 ? 0.4967 0.4852 0.3992 -0.0226 0.0016  -0.0041 202 LEU A C   
1635 O O   . LEU A 205 ? 0.5499 0.5188 0.4298 -0.0240 0.0106  0.0040  202 LEU A O   
1636 C CB  . LEU A 205 ? 0.4613 0.4977 0.3811 0.0001  -0.0109 -0.0169 202 LEU A CB  
1637 C CG  . LEU A 205 ? 0.4714 0.5381 0.4052 0.0132  -0.0191 -0.0310 202 LEU A CG  
1638 C CD1 . LEU A 205 ? 0.4694 0.5595 0.4091 0.0142  -0.0206 -0.0378 202 LEU A CD1 
1639 C CD2 . LEU A 205 ? 0.4243 0.4989 0.3849 0.0055  -0.0207 -0.0427 202 LEU A CD2 
1640 N N   . LEU A 206 ? 0.4883 0.4811 0.4063 -0.0367 0.0003  -0.0075 203 LEU A N   
1641 C CA  . LEU A 206 ? 0.4788 0.4643 0.3919 -0.0557 0.0065  -0.0047 203 LEU A CA  
1642 C C   . LEU A 206 ? 0.4864 0.5025 0.4192 -0.0622 0.0023  -0.0067 203 LEU A C   
1643 O O   . LEU A 206 ? 0.4466 0.4786 0.3972 -0.0558 -0.0037 -0.0100 203 LEU A O   
1644 C CB  . LEU A 206 ? 0.4942 0.4667 0.4060 -0.0649 0.0078  -0.0071 203 LEU A CB  
1645 C CG  . LEU A 206 ? 0.5003 0.4393 0.3922 -0.0588 0.0146  -0.0054 203 LEU A CG  
1646 C CD1 . LEU A 206 ? 0.5295 0.4751 0.4305 -0.0399 0.0077  -0.0084 203 LEU A CD1 
1647 C CD2 . LEU A 206 ? 0.5501 0.4720 0.4343 -0.0761 0.0212  -0.0088 203 LEU A CD2 
1648 N N   . LEU A 207 ? 0.4282 0.4507 0.3569 -0.0741 0.0081  -0.0049 204 LEU A N   
1649 C CA  . LEU A 207 ? 0.4722 0.5281 0.4192 -0.0798 0.0052  -0.0065 204 LEU A CA  
1650 C C   . LEU A 207 ? 0.4560 0.5191 0.4015 -0.0996 0.0087  -0.0098 204 LEU A C   
1651 O O   . LEU A 207 ? 0.5140 0.5667 0.4472 -0.1148 0.0193  -0.0116 204 LEU A O   
1652 C CB  . LEU A 207 ? 0.4858 0.5531 0.4326 -0.0783 0.0097  -0.0052 204 LEU A CB  
1653 C CG  . LEU A 207 ? 0.6145 0.6832 0.5630 -0.0604 0.0062  -0.0055 204 LEU A CG  
1654 C CD1 . LEU A 207 ? 0.6914 0.7334 0.6169 -0.0510 0.0087  -0.0026 204 LEU A CD1 
1655 C CD2 . LEU A 207 ? 0.6150 0.7055 0.5701 -0.0602 0.0097  -0.0059 204 LEU A CD2 
1656 N N   . ASN A 208 ? 0.4411 0.5204 0.3966 -0.0997 0.0016  -0.0115 205 ASN A N   
1657 C CA  . ASN A 208 ? 0.4328 0.5251 0.3859 -0.1180 0.0029  -0.0176 205 ASN A CA  
1658 C C   . ASN A 208 ? 0.4755 0.6177 0.4452 -0.1237 -0.0005 -0.0210 205 ASN A C   
1659 O O   . ASN A 208 ? 0.4745 0.6465 0.4557 -0.1127 -0.0096 -0.0184 205 ASN A O   
1660 C CB  . ASN A 208 ? 0.4458 0.5288 0.3952 -0.1143 -0.0021 -0.0178 205 ASN A CB  
1661 C CG  . ASN A 208 ? 0.5011 0.5402 0.4362 -0.1091 0.0025  -0.0163 205 ASN A CG  
1662 O OD1 . ASN A 208 ? 0.5224 0.5342 0.4415 -0.1173 0.0124  -0.0176 205 ASN A OD1 
1663 N ND2 . ASN A 208 ? 0.4833 0.5153 0.4238 -0.0937 -0.0022 -0.0134 205 ASN A ND2 
1664 N N   . GLY A 209 ? 0.5093 0.6596 0.4785 -0.1400 0.0085  -0.0265 206 GLY A N   
1665 C CA  . GLY A 209 ? 0.5499 0.7540 0.5374 -0.1482 0.0070  -0.0328 206 GLY A CA  
1666 C C   . GLY A 209 ? 0.5373 0.7650 0.5411 -0.1260 0.0011  -0.0250 206 GLY A C   
1667 O O   . GLY A 209 ? 0.5040 0.7030 0.5036 -0.1101 0.0014  -0.0173 206 GLY A O   
1668 N N   . ARG A 210 ? 0.4896 0.7734 0.5124 -0.1247 -0.0038 -0.0286 207 ARG A N   
1669 C CA  . ARG A 210 ? 0.5076 0.8182 0.5469 -0.1030 -0.0071 -0.0221 207 ARG A CA  
1670 C C   . ARG A 210 ? 0.5118 0.8200 0.5521 -0.0767 -0.0161 -0.0116 207 ARG A C   
1671 O O   . ARG A 210 ? 0.5691 0.8703 0.6002 -0.0774 -0.0213 -0.0107 207 ARG A O   
1672 C CB  . ARG A 210 ? 0.5603 0.9356 0.6193 -0.1128 -0.0068 -0.0315 207 ARG A CB  
1673 C CG  . ARG A 210 ? 0.6682 1.0411 0.7249 -0.1434 0.0071  -0.0435 207 ARG A CG  
1674 C CD  . ARG A 210 ? 0.7952 1.2394 0.8736 -0.1608 0.0078  -0.0590 207 ARG A CD  
1675 N NE  . ARG A 210 ? 0.8561 1.3565 0.9588 -0.1405 0.0026  -0.0564 207 ARG A NE  
1676 C CZ  . ARG A 210 ? 0.9140 1.4590 1.0357 -0.1532 0.0111  -0.0672 207 ARG A CZ  
1677 N NH1 . ARG A 210 ? 0.9870 1.5833 1.1309 -0.1298 0.0059  -0.0637 207 ARG A NH1 
1678 N NH2 . ARG A 210 ? 0.9258 1.4632 1.0440 -0.1889 0.0271  -0.0816 207 ARG A NH2 
1679 N N   . GLU A 211 ? 0.4935 0.8031 0.5429 -0.0541 -0.0150 -0.0040 208 GLU A N   
1680 C CA  . GLU A 211 ? 0.5446 0.8454 0.5937 -0.0281 -0.0174 0.0066  208 GLU A CA  
1681 C C   . GLU A 211 ? 0.5518 0.8881 0.5994 -0.0216 -0.0258 0.0099  208 GLU A C   
1682 O O   . GLU A 211 ? 0.5094 0.9029 0.5686 -0.0211 -0.0308 0.0064  208 GLU A O   
1683 C CB  . GLU A 211 ? 0.6530 0.9650 0.7149 -0.0071 -0.0120 0.0114  208 GLU A CB  
1684 C CG  . GLU A 211 ? 0.6405 0.9426 0.7007 0.0220  -0.0094 0.0236  208 GLU A CG  
1685 C CD  . GLU A 211 ? 0.7437 1.0516 0.8151 0.0433  -0.0005 0.0275  208 GLU A CD  
1686 O OE1 . GLU A 211 ? 0.6332 0.9521 0.7140 0.0341  0.0024  0.0197  208 GLU A OE1 
1687 O OE2 . GLU A 211 ? 0.8309 1.1322 0.8998 0.0701  0.0050  0.0390  208 GLU A OE2 
1688 N N   . PRO A 212 ? 0.5064 0.8147 0.5392 -0.0169 -0.0277 0.0153  209 PRO A N   
1689 C CA  . PRO A 212 ? 0.5566 0.8972 0.5826 -0.0075 -0.0355 0.0198  209 PRO A CA  
1690 C C   . PRO A 212 ? 0.5867 0.9635 0.6207 0.0242  -0.0362 0.0316  209 PRO A C   
1691 O O   . PRO A 212 ? 0.6789 1.0240 0.7135 0.0443  -0.0268 0.0414  209 PRO A O   
1692 C CB  . PRO A 212 ? 0.5149 0.8048 0.5225 -0.0041 -0.0324 0.0259  209 PRO A CB  
1693 C CG  . PRO A 212 ? 0.4979 0.7405 0.5049 -0.0226 -0.0264 0.0180  209 PRO A CG  
1694 C CD  . PRO A 212 ? 0.5103 0.7594 0.5317 -0.0214 -0.0224 0.0156  209 PRO A CD  
1695 N N   . MET A 213 ? 0.6250 1.0693 0.6646 0.0292  -0.0463 0.0294  210 MET A N   
1696 C CA  . MET A 213 ? 0.6426 1.1300 0.6903 0.0634  -0.0475 0.0410  210 MET A CA  
1697 C C   . MET A 213 ? 0.6882 1.1951 0.7169 0.0912  -0.0536 0.0551  210 MET A C   
1698 O O   . MET A 213 ? 0.6492 1.1849 0.6699 0.0754  -0.0640 0.0462  210 MET A O   
1699 C CB  . MET A 213 ? 0.6522 1.2163 0.7241 0.0521  -0.0544 0.0266  210 MET A CB  
1700 C CG  . MET A 213 ? 0.6690 1.2141 0.7569 0.0331  -0.0450 0.0173  210 MET A CG  
1701 S SD  . MET A 213 ? 0.9023 1.3981 0.9924 0.0617  -0.0308 0.0316  210 MET A SD  
1702 C CE  . MET A 213 ? 0.9422 1.4799 1.0314 0.1111  -0.0330 0.0505  210 MET A CE  
1703 N N   . PHE A 221 ? 1.0084 1.3957 0.9471 -0.0878 -0.0623 -0.0262 218 PHE A N   
1704 C CA  . PHE A 221 ? 0.9023 1.2594 0.8565 -0.1038 -0.0535 -0.0313 218 PHE A CA  
1705 C C   . PHE A 221 ? 0.8326 1.1399 0.7761 -0.1318 -0.0433 -0.0439 218 PHE A C   
1706 O O   . PHE A 221 ? 0.6830 0.9321 0.6191 -0.1260 -0.0365 -0.0357 218 PHE A O   
1707 C CB  . PHE A 221 ? 1.0339 1.3534 0.9947 -0.0790 -0.0490 -0.0127 218 PHE A CB  
1708 C CG  . PHE A 221 ? 1.1489 1.5093 1.1197 -0.0503 -0.0545 0.0000  218 PHE A CG  
1709 C CD1 . PHE A 221 ? 1.1897 1.6071 1.1792 -0.0537 -0.0593 -0.0074 218 PHE A CD1 
1710 C CD2 . PHE A 221 ? 1.2309 1.5717 1.1916 -0.0193 -0.0525 0.0190  218 PHE A CD2 
1711 C CE1 . PHE A 221 ? 1.1975 1.6541 1.1962 -0.0235 -0.0636 0.0049  218 PHE A CE1 
1712 C CE2 . PHE A 221 ? 1.2395 1.6120 1.2059 0.0106  -0.0545 0.0324  218 PHE A CE2 
1713 C CZ  . PHE A 221 ? 1.2154 1.6473 1.2011 0.0101  -0.0610 0.0257  218 PHE A CZ  
1714 N N   . GLU A 222 ? 0.7607 1.0939 0.7040 -0.1619 -0.0410 -0.0652 219 GLU A N   
1715 C CA  . GLU A 222 ? 0.7914 1.0762 0.7219 -0.1893 -0.0276 -0.0785 219 GLU A CA  
1716 C C   . GLU A 222 ? 0.6405 0.8680 0.5730 -0.1885 -0.0160 -0.0704 219 GLU A C   
1717 O O   . GLU A 222 ? 0.6934 0.8654 0.6114 -0.1965 -0.0049 -0.0719 219 GLU A O   
1718 C CB  . GLU A 222 ? 0.8335 1.1555 0.7664 -0.2251 -0.0222 -0.1054 219 GLU A CB  
1719 C CG  . GLU A 222 ? 0.9519 1.3090 0.9060 -0.2379 -0.0185 -0.1132 219 GLU A CG  
1720 C CD  . GLU A 222 ? 1.1305 1.5593 1.1054 -0.2152 -0.0344 -0.1056 219 GLU A CD  
1721 O OE1 . GLU A 222 ? 1.1428 1.5948 1.1132 -0.1870 -0.0484 -0.0925 219 GLU A OE1 
1722 O OE2 . GLU A 222 ? 1.3257 1.7849 1.3197 -0.2244 -0.0307 -0.1120 219 GLU A OE2 
1723 N N   . ARG A 223 ? 0.5813 0.8254 0.5304 -0.1772 -0.0183 -0.0622 220 ARG A N   
1724 C CA  . ARG A 223 ? 0.5567 0.7548 0.5060 -0.1738 -0.0089 -0.0545 220 ARG A CA  
1725 C C   . ARG A 223 ? 0.5936 0.7410 0.5329 -0.1545 -0.0087 -0.0418 220 ARG A C   
1726 O O   . ARG A 223 ? 0.6312 0.7313 0.5595 -0.1578 0.0009  -0.0410 220 ARG A O   
1727 C CB  . ARG A 223 ? 0.6225 0.8531 0.5910 -0.1617 -0.0128 -0.0479 220 ARG A CB  
1728 C CG  . ARG A 223 ? 0.7712 1.0518 0.7527 -0.1836 -0.0097 -0.0628 220 ARG A CG  
1729 C CD  . ARG A 223 ? 0.9599 1.2772 0.9617 -0.1685 -0.0138 -0.0561 220 ARG A CD  
1730 N NE  . ARG A 223 ? 1.1160 1.4802 1.1324 -0.1922 -0.0078 -0.0723 220 ARG A NE  
1731 C CZ  . ARG A 223 ? 1.0889 1.4957 1.1256 -0.1845 -0.0093 -0.0713 220 ARG A CZ  
1732 N NH1 . ARG A 223 ? 1.1923 1.6413 1.2432 -0.2103 -0.0012 -0.0889 220 ARG A NH1 
1733 N NH2 . ARG A 223 ? 1.0886 1.4941 1.1319 -0.1529 -0.0163 -0.0544 220 ARG A NH2 
1734 N N   . VAL A 224 ? 0.4980 0.6566 0.4406 -0.1332 -0.0180 -0.0320 221 VAL A N   
1735 C CA  . VAL A 224 ? 0.4740 0.5911 0.4111 -0.1177 -0.0161 -0.0233 221 VAL A CA  
1736 C C   . VAL A 224 ? 0.5053 0.6011 0.4258 -0.1273 -0.0128 -0.0295 221 VAL A C   
1737 O O   . VAL A 224 ? 0.4882 0.5431 0.4014 -0.1262 -0.0063 -0.0295 221 VAL A O   
1738 C CB  . VAL A 224 ? 0.4686 0.5969 0.4144 -0.0932 -0.0214 -0.0110 221 VAL A CB  
1739 C CG1 . VAL A 224 ? 0.4561 0.5457 0.3978 -0.0824 -0.0168 -0.0064 221 VAL A CG1 
1740 C CG2 . VAL A 224 ? 0.4871 0.6303 0.4486 -0.0830 -0.0221 -0.0061 221 VAL A CG2 
1741 N N   . GLY A 225 ? 0.4865 0.6146 0.4007 -0.1357 -0.0175 -0.0361 222 GLY A N   
1742 C CA  . GLY A 225 ? 0.4888 0.6008 0.3858 -0.1453 -0.0141 -0.0436 222 GLY A CA  
1743 C C   . GLY A 225 ? 0.5381 0.6102 0.4245 -0.1657 -0.0013 -0.0551 222 GLY A C   
1744 O O   . GLY A 225 ? 0.5103 0.5436 0.3856 -0.1633 0.0053  -0.0550 222 GLY A O   
1745 N N   . GLU A 226 ? 0.5640 0.6434 0.4531 -0.1846 0.0045  -0.0644 223 GLU A N   
1746 C CA  . GLU A 226 ? 0.6273 0.6613 0.5019 -0.2034 0.0217  -0.0740 223 GLU A CA  
1747 C C   . GLU A 226 ? 0.5461 0.5289 0.4161 -0.1848 0.0280  -0.0610 223 GLU A C   
1748 O O   . GLU A 226 ? 0.5655 0.5027 0.4189 -0.1879 0.0408  -0.0638 223 GLU A O   
1749 C CB  . GLU A 226 ? 0.6638 0.7145 0.5420 -0.2287 0.0306  -0.0867 223 GLU A CB  
1750 C CG  . GLU A 226 ? 0.7495 0.8559 0.6317 -0.2517 0.0261  -0.1064 223 GLU A CG  
1751 C CD  . GLU A 226 ? 0.8766 1.0074 0.7667 -0.2814 0.0368  -0.1238 223 GLU A CD  
1752 O OE1 . GLU A 226 ? 1.0298 1.2150 0.9259 -0.3026 0.0331  -0.1441 223 GLU A OE1 
1753 O OE2 . GLU A 226 ? 0.8972 0.9963 0.7873 -0.2833 0.0492  -0.1180 223 GLU A OE2 
1754 N N   . ALA A 227 ? 0.5238 0.5171 0.4083 -0.1645 0.0195  -0.0480 224 ALA A N   
1755 C CA  . ALA A 227 ? 0.5240 0.4818 0.4061 -0.1456 0.0228  -0.0382 224 ALA A CA  
1756 C C   . ALA A 227 ? 0.5083 0.4506 0.3887 -0.1322 0.0205  -0.0361 224 ALA A C   
1757 O O   . ALA A 227 ? 0.4908 0.3984 0.3615 -0.1242 0.0281  -0.0349 224 ALA A O   
1758 C CB  . ALA A 227 ? 0.4995 0.4775 0.3978 -0.1309 0.0150  -0.0293 224 ALA A CB  
1759 N N   . ASP A 228 ? 0.4888 0.4571 0.3780 -0.1273 0.0114  -0.0348 225 ASP A N   
1760 C CA  . ASP A 228 ? 0.4970 0.4512 0.3843 -0.1176 0.0122  -0.0340 225 ASP A CA  
1761 C C   . ASP A 228 ? 0.5415 0.4688 0.4101 -0.1296 0.0220  -0.0430 225 ASP A C   
1762 O O   . ASP A 228 ? 0.5369 0.4387 0.4021 -0.1205 0.0277  -0.0431 225 ASP A O   
1763 C CB  . ASP A 228 ? 0.4746 0.4556 0.3677 -0.1114 0.0050  -0.0297 225 ASP A CB  
1764 C CG  . ASP A 228 ? 0.4836 0.4748 0.3940 -0.0946 0.0010  -0.0208 225 ASP A CG  
1765 O OD1 . ASP A 228 ? 0.4682 0.4478 0.3881 -0.0875 0.0024  -0.0204 225 ASP A OD1 
1766 O OD2 . ASP A 228 ? 0.4779 0.4887 0.3900 -0.0879 -0.0023 -0.0146 225 ASP A OD2 
1767 N N   . ILE A 229 ? 0.5366 0.4738 0.3943 -0.1506 0.0247  -0.0526 226 ILE A N   
1768 C CA  . ILE A 229 ? 0.5685 0.4785 0.4069 -0.1656 0.0367  -0.0644 226 ILE A CA  
1769 C C   . ILE A 229 ? 0.5745 0.4348 0.4025 -0.1611 0.0513  -0.0630 226 ILE A C   
1770 O O   . ILE A 229 ? 0.5956 0.4252 0.4137 -0.1543 0.0597  -0.0647 226 ILE A O   
1771 C CB  . ILE A 229 ? 0.6173 0.5533 0.4483 -0.1927 0.0379  -0.0795 226 ILE A CB  
1772 C CG1 . ILE A 229 ? 0.5826 0.5671 0.4169 -0.1900 0.0237  -0.0797 226 ILE A CG1 
1773 C CG2 . ILE A 229 ? 0.6462 0.5445 0.4559 -0.2128 0.0559  -0.0952 226 ILE A CG2 
1774 C CD1 . ILE A 229 ? 0.6301 0.6573 0.4600 -0.2135 0.0208  -0.0964 226 ILE A CD1 
1775 N N   . LYS A 230 ? 0.6102 0.4630 0.4391 -0.1616 0.0550  -0.0586 227 LYS A N   
1776 C CA  . LYS A 230 ? 0.6290 0.4325 0.4421 -0.1530 0.0704  -0.0541 227 LYS A CA  
1777 C C   . LYS A 230 ? 0.6064 0.4022 0.4263 -0.1228 0.0650  -0.0439 227 LYS A C   
1778 O O   . LYS A 230 ? 0.6743 0.4337 0.4801 -0.1115 0.0765  -0.0428 227 LYS A O   
1779 C CB  . LYS A 230 ? 0.6328 0.4305 0.4425 -0.1581 0.0765  -0.0497 227 LYS A CB  
1780 C CG  . LYS A 230 ? 0.7428 0.4843 0.5287 -0.1463 0.0956  -0.0420 227 LYS A CG  
1781 C CD  . LYS A 230 ? 0.8150 0.5068 0.5759 -0.1591 0.1179  -0.0514 227 LYS A CD  
1782 C CE  . LYS A 230 ? 0.8537 0.5490 0.6095 -0.1983 0.1293  -0.0701 227 LYS A CE  
1783 N NZ  . LYS A 230 ? 0.9248 0.5705 0.6565 -0.2123 0.1524  -0.0826 227 LYS A NZ  
1784 N N   . LEU A 231 ? 0.5575 0.3893 0.3997 -0.1097 0.0489  -0.0378 228 LEU A N   
1785 C CA  . LEU A 231 ? 0.5500 0.3845 0.4034 -0.0851 0.0439  -0.0330 228 LEU A CA  
1786 C C   . LEU A 231 ? 0.5585 0.3838 0.4108 -0.0827 0.0479  -0.0389 228 LEU A C   
1787 O O   . LEU A 231 ? 0.5636 0.3752 0.4152 -0.0648 0.0523  -0.0382 228 LEU A O   
1788 C CB  . LEU A 231 ? 0.5284 0.4019 0.4059 -0.0788 0.0296  -0.0298 228 LEU A CB  
1789 C CG  . LEU A 231 ? 0.5139 0.3968 0.3937 -0.0756 0.0262  -0.0239 228 LEU A CG  
1790 C CD1 . LEU A 231 ? 0.5193 0.4373 0.4219 -0.0713 0.0147  -0.0228 228 LEU A CD1 
1791 C CD2 . LEU A 231 ? 0.5826 0.4480 0.4534 -0.0554 0.0301  -0.0189 228 LEU A CD2 
1792 N N   . MET A 232 ? 0.5567 0.3917 0.4070 -0.0995 0.0470  -0.0451 229 MET A N   
1793 C CA  . MET A 232 ? 0.5414 0.3685 0.3885 -0.0989 0.0519  -0.0510 229 MET A CA  
1794 C C   . MET A 232 ? 0.5903 0.3751 0.4151 -0.1011 0.0681  -0.0564 229 MET A C   
1795 O O   . MET A 232 ? 0.6331 0.4035 0.4576 -0.0879 0.0746  -0.0581 229 MET A O   
1796 C CB  . MET A 232 ? 0.5341 0.3832 0.3784 -0.1148 0.0472  -0.0550 229 MET A CB  
1797 C CG  . MET A 232 ? 0.5547 0.3940 0.3898 -0.1171 0.0541  -0.0616 229 MET A CG  
1798 S SD  . MET A 232 ? 0.5302 0.3776 0.3868 -0.0970 0.0535  -0.0575 229 MET A SD  
1799 C CE  . MET A 232 ? 0.5678 0.3881 0.4107 -0.0971 0.0682  -0.0672 229 MET A CE  
1800 N N   . GLU A 233 ? 0.6016 0.3655 0.4084 -0.1178 0.0772  -0.0600 230 GLU A N   
1801 C CA  . GLU A 233 ? 0.6411 0.3553 0.4229 -0.1222 0.0979  -0.0658 230 GLU A CA  
1802 C C   . GLU A 233 ? 0.6821 0.3673 0.4591 -0.0927 0.1054  -0.0550 230 GLU A C   
1803 O O   . GLU A 233 ? 0.7111 0.3583 0.4718 -0.0834 0.1212  -0.0569 230 GLU A O   
1804 C CB  . GLU A 233 ? 0.6873 0.3862 0.4531 -0.1495 0.1088  -0.0736 230 GLU A CB  
1805 C CG  . GLU A 233 ? 0.7017 0.4322 0.4682 -0.1783 0.1036  -0.0887 230 GLU A CG  
1806 C CD  . GLU A 233 ? 0.7147 0.4511 0.4750 -0.2079 0.1103  -0.0999 230 GLU A CD  
1807 O OE1 . GLU A 233 ? 0.7413 0.4572 0.4982 -0.2067 0.1187  -0.0934 230 GLU A OE1 
1808 O OE2 . GLU A 233 ? 0.7418 0.5045 0.4994 -0.2325 0.1087  -0.1166 230 GLU A OE2 
1809 N N   . LEU A 234 ? 0.6992 0.4047 0.4889 -0.0763 0.0942  -0.0438 231 LEU A N   
1810 C CA  . LEU A 234 ? 0.7008 0.3920 0.4861 -0.0446 0.0974  -0.0330 231 LEU A CA  
1811 C C   . LEU A 234 ? 0.6764 0.3970 0.4836 -0.0227 0.0876  -0.0348 231 LEU A C   
1812 O O   . LEU A 234 ? 0.6854 0.4025 0.4907 0.0063  0.0897  -0.0290 231 LEU A O   
1813 C CB  . LEU A 234 ? 0.7246 0.4336 0.5146 -0.0386 0.0883  -0.0234 231 LEU A CB  
1814 C CG  . LEU A 234 ? 0.7601 0.4409 0.5295 -0.0589 0.1009  -0.0215 231 LEU A CG  
1815 C CD1 . LEU A 234 ? 0.7645 0.4638 0.5382 -0.0491 0.0926  -0.0112 231 LEU A CD1 
1816 C CD2 . LEU A 234 ? 0.9015 0.5170 0.6359 -0.0555 0.1278  -0.0189 231 LEU A CD2 
1817 N N   . GLY A 235 ? 0.6180 0.3689 0.4450 -0.0360 0.0784  -0.0431 232 GLY A N   
1818 C CA  . GLY A 235 ? 0.6108 0.3907 0.4611 -0.0212 0.0723  -0.0476 232 GLY A CA  
1819 C C   . GLY A 235 ? 0.5624 0.3843 0.4381 -0.0093 0.0573  -0.0454 232 GLY A C   
1820 O O   . GLY A 235 ? 0.5674 0.4170 0.4643 0.0053  0.0534  -0.0511 232 GLY A O   
1821 N N   . TYR A 236 ? 0.5758 0.4053 0.4508 -0.0181 0.0499  -0.0398 233 TYR A N   
1822 C CA  . TYR A 236 ? 0.5231 0.3890 0.4191 -0.0089 0.0374  -0.0391 233 TYR A CA  
1823 C C   . TYR A 236 ? 0.5528 0.4453 0.4697 -0.0245 0.0301  -0.0435 233 TYR A C   
1824 O O   . TYR A 236 ? 0.5277 0.4488 0.4641 -0.0187 0.0225  -0.0462 233 TYR A O   
1825 C CB  . TYR A 236 ? 0.5530 0.4095 0.4340 -0.0057 0.0359  -0.0294 233 TYR A CB  
1826 C CG  . TYR A 236 ? 0.6069 0.4378 0.4650 0.0170  0.0440  -0.0213 233 TYR A CG  
1827 C CD1 . TYR A 236 ? 0.6189 0.4468 0.4755 0.0397  0.0485  -0.0229 233 TYR A CD1 
1828 C CD2 . TYR A 236 ? 0.6274 0.4335 0.4621 0.0168  0.0499  -0.0109 233 TYR A CD2 
1829 C CE1 . TYR A 236 ? 0.6839 0.4858 0.5150 0.0664  0.0574  -0.0123 233 TYR A CE1 
1830 C CE2 . TYR A 236 ? 0.6732 0.4476 0.4803 0.0404  0.0610  -0.0002 233 TYR A CE2 
1831 C CZ  . TYR A 236 ? 0.6889 0.4603 0.4928 0.0672  0.0646  0.0001  233 TYR A CZ  
1832 O OH  . TYR A 236 ? 0.7795 0.5168 0.5516 0.0958  0.0771  0.0138  233 TYR A OH  
1833 N N   . LEU A 237 ? 0.4843 0.3672 0.3948 -0.0427 0.0334  -0.0442 234 LEU A N   
1834 C CA  . LEU A 237 ? 0.4809 0.3840 0.4052 -0.0524 0.0289  -0.0446 234 LEU A CA  
1835 C C   . LEU A 237 ? 0.4765 0.3886 0.4172 -0.0489 0.0339  -0.0525 234 LEU A C   
1836 O O   . LEU A 237 ? 0.4865 0.3852 0.4192 -0.0520 0.0417  -0.0559 234 LEU A O   
1837 C CB  . LEU A 237 ? 0.4841 0.3798 0.3918 -0.0694 0.0294  -0.0411 234 LEU A CB  
1838 C CG  . LEU A 237 ? 0.4756 0.3917 0.3913 -0.0741 0.0243  -0.0368 234 LEU A CG  
1839 C CD1 . LEU A 237 ? 0.4714 0.4026 0.3959 -0.0712 0.0169  -0.0322 234 LEU A CD1 
1840 C CD2 . LEU A 237 ? 0.5203 0.4379 0.4186 -0.0868 0.0243  -0.0353 234 LEU A CD2 
1841 N N   . PRO A 238 ? 0.4671 0.4023 0.4317 -0.0441 0.0322  -0.0579 235 PRO A N   
1842 C CA  . PRO A 238 ? 0.4619 0.4066 0.4445 -0.0440 0.0406  -0.0687 235 PRO A CA  
1843 C C   . PRO A 238 ? 0.4454 0.3781 0.4228 -0.0560 0.0498  -0.0660 235 PRO A C   
1844 O O   . PRO A 238 ? 0.4405 0.3674 0.4070 -0.0615 0.0476  -0.0562 235 PRO A O   
1845 C CB  . PRO A 238 ? 0.4706 0.4442 0.4799 -0.0399 0.0378  -0.0783 235 PRO A CB  
1846 C CG  . PRO A 238 ? 0.4661 0.4447 0.4681 -0.0332 0.0262  -0.0712 235 PRO A CG  
1847 C CD  . PRO A 238 ? 0.4582 0.4116 0.4343 -0.0407 0.0246  -0.0570 235 PRO A CD  
1848 N N   . PRO A 239 ? 0.4560 0.3862 0.4397 -0.0582 0.0615  -0.0741 236 PRO A N   
1849 C CA  . PRO A 239 ? 0.4834 0.3993 0.4586 -0.0673 0.0734  -0.0703 236 PRO A CA  
1850 C C   . PRO A 239 ? 0.4883 0.4095 0.4793 -0.0703 0.0796  -0.0711 236 PRO A C   
1851 O O   . PRO A 239 ? 0.4929 0.4338 0.5076 -0.0681 0.0770  -0.0817 236 PRO A O   
1852 C CB  . PRO A 239 ? 0.5496 0.4643 0.5321 -0.0683 0.0861  -0.0816 236 PRO A CB  
1853 C CG  . PRO A 239 ? 0.5876 0.5286 0.5956 -0.0584 0.0811  -0.0950 236 PRO A CG  
1854 C CD  . PRO A 239 ? 0.5016 0.4437 0.4993 -0.0498 0.0649  -0.0865 236 PRO A CD  
1855 N N   . LEU A 240 ? 0.5148 0.4178 0.4899 -0.0738 0.0887  -0.0601 237 LEU A N   
1856 C CA  . LEU A 240 ? 0.6022 0.4985 0.5873 -0.0757 0.1011  -0.0597 237 LEU A CA  
1857 C C   . LEU A 240 ? 0.6212 0.5205 0.6318 -0.0841 0.1196  -0.0785 237 LEU A C   
1858 O O   . LEU A 240 ? 0.7266 0.6316 0.7583 -0.0887 0.1278  -0.0890 237 LEU A O   
1859 C CB  . LEU A 240 ? 0.6322 0.5043 0.5886 -0.0728 0.1102  -0.0412 237 LEU A CB  
1860 C CG  . LEU A 240 ? 0.5873 0.4657 0.5246 -0.0644 0.0942  -0.0248 237 LEU A CG  
1861 C CD1 . LEU A 240 ? 0.6789 0.5397 0.5882 -0.0562 0.1043  -0.0066 237 LEU A CD1 
1862 C CD2 . LEU A 240 ? 0.5966 0.4875 0.5526 -0.0615 0.0868  -0.0270 237 LEU A CD2 
1863 N N   . ARG A 241 ? 0.7528 0.6501 0.7621 -0.0875 0.1276  -0.0849 238 ARG A N   
1864 C CA  . ARG A 241 ? 0.8029 0.7078 0.8378 -0.0974 0.1470  -0.1048 238 ARG A CA  
1865 C C   . ARG A 241 ? 0.8501 0.7941 0.9119 -0.0932 0.1353  -0.1235 238 ARG A C   
1866 O O   . ARG A 241 ? 0.8780 0.8230 0.9313 -0.0879 0.1321  -0.1230 238 ARG A O   
1867 C CB  . ARG A 241 ? 0.9130 0.7911 0.9272 -0.1021 0.1658  -0.0987 238 ARG A CB  
1868 C CG  . ARG A 241 ? 0.8916 0.7324 0.8739 -0.1005 0.1780  -0.0774 238 ARG A CG  
1869 C CD  . ARG A 241 ? 0.9469 0.7644 0.9019 -0.1019 0.1934  -0.0695 238 ARG A CD  
1870 N NE  . ARG A 241 ? 0.8305 0.6481 0.8071 -0.1147 0.2173  -0.0885 238 ARG A NE  
1871 C CZ  . ARG A 241 ? 0.9051 0.7364 0.8882 -0.1173 0.2181  -0.0999 238 ARG A CZ  
1872 N NH1 . ARG A 241 ? 0.9429 0.7786 0.9486 -0.1296 0.2417  -0.1185 238 ARG A NH1 
1873 N NH2 . ARG A 241 ? 0.7665 0.6064 0.7339 -0.1084 0.1975  -0.0942 238 ARG A NH2 
# 
