data_9MYM
# 
_entry.id   9MYM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9MYM         pdb_00009mym 10.2210/pdb9mym/pdb 
WWPDB D_1000292096 ?            ?                   
# 
_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       2025-03-19 
_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                        9MYM 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              shaogeng.tang@yale.edu 
_pdbx_contact_author.name_first         Shaogeng 
_pdbx_contact_author.name_last          Tang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3904-492X 
# 
_audit_author.name               'Tang, S.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0002-3904-492X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            122 
_citation.language                  ? 
_citation.page_first                e2425952122 
_citation.page_last                 e2425952122 
_citation.title                     
'Allosteric inhibition of the IZUMO1-JUNO fertilization complex by the naturally occurring antisperm antibody OBF13.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2425952122 
_citation.pdbx_database_id_PubMed   40042902 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Lu, Y.'    1 0000-0003-0198-8906 
primary 'Ikawa, M.' 2 0000-0001-9859-6217 
primary 'Tang, S.'  3 0000-0002-3904-492X 
# 
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 'Izumo sperm-egg fusion protein 1'       27194.172 1   ? ? ? ? 
2 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   2   ? ? ? ? 
3 non-polymer syn alpha-L-fucopyranose                     164.156   1   ? ? ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                  106.120   2   ? ? ? ? 
5 non-polymer syn 'PENTAETHYLENE GLYCOL'                   238.278   1   ? ? ? ? 
6 non-polymer syn 'CHLORIDE ION'                           35.453    1   ? ? ? ? 
7 non-polymer syn 'CALCIUM ION'                            40.078    2   ? ? ? ? 
8 water       nat water                                    18.015    325 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Oocyte binding/fusion factor,OBF,Sperm-specific protein izumo' 
# 
_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       
;CIKCDQFVTDALKTFENTYLNDHLPHDIHKNVMRMVNHEVSSFGVVTSAEDSYLGAVDENTLEQATWSFLKDLKRITDSD
LKGELFIKELLWMLRHQKDIFNNLARQFQKEVLCPNKCGVMSQTLIWCLKCEKQLHICRKSLDCGERHIEVHRSEDLVLD
CLLSWHRASKGLTDYSFYRVWENSSETLIAKGKEPYLTKSMVGPEDAGNYRCVLDTINQGHATVIRYDVTVLPPK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;CIKCDQFVTDALKTFENTYLNDHLPHDIHKNVMRMVNHEVSSFGVVTSAEDSYLGAVDENTLEQATWSFLKDLKRITDSD
LKGELFIKELLWMLRHQKDIFNNLARQFQKEVLCPNKCGVMSQTLIWCLKCEKQLHICRKSLDCGERHIEVHRSEDLVLD
CLLSWHRASKGLTDYSFYRVWENSSETLIAKGKEPYLTKSMVGPEDAGNYRCVLDTINQGHATVIRYDVTVLPPK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
3 alpha-L-fucopyranose                     FUC 
4 'DI(HYDROXYETHYL)ETHER'                  PEG 
5 'PENTAETHYLENE GLYCOL'                   1PE 
6 'CHLORIDE ION'                           CL  
7 'CALCIUM ION'                            CA  
8 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   CYS n 
1 2   ILE n 
1 3   LYS n 
1 4   CYS n 
1 5   ASP n 
1 6   GLN n 
1 7   PHE n 
1 8   VAL n 
1 9   THR n 
1 10  ASP n 
1 11  ALA n 
1 12  LEU n 
1 13  LYS n 
1 14  THR n 
1 15  PHE n 
1 16  GLU n 
1 17  ASN n 
1 18  THR n 
1 19  TYR n 
1 20  LEU n 
1 21  ASN n 
1 22  ASP n 
1 23  HIS n 
1 24  LEU n 
1 25  PRO n 
1 26  HIS n 
1 27  ASP n 
1 28  ILE n 
1 29  HIS n 
1 30  LYS n 
1 31  ASN n 
1 32  VAL n 
1 33  MET n 
1 34  ARG n 
1 35  MET n 
1 36  VAL n 
1 37  ASN n 
1 38  HIS n 
1 39  GLU n 
1 40  VAL n 
1 41  SER n 
1 42  SER n 
1 43  PHE n 
1 44  GLY n 
1 45  VAL n 
1 46  VAL n 
1 47  THR n 
1 48  SER n 
1 49  ALA n 
1 50  GLU n 
1 51  ASP n 
1 52  SER n 
1 53  TYR n 
1 54  LEU n 
1 55  GLY n 
1 56  ALA n 
1 57  VAL n 
1 58  ASP n 
1 59  GLU n 
1 60  ASN n 
1 61  THR n 
1 62  LEU n 
1 63  GLU n 
1 64  GLN n 
1 65  ALA n 
1 66  THR n 
1 67  TRP n 
1 68  SER n 
1 69  PHE n 
1 70  LEU n 
1 71  LYS n 
1 72  ASP n 
1 73  LEU n 
1 74  LYS n 
1 75  ARG n 
1 76  ILE n 
1 77  THR n 
1 78  ASP n 
1 79  SER n 
1 80  ASP n 
1 81  LEU n 
1 82  LYS n 
1 83  GLY n 
1 84  GLU n 
1 85  LEU n 
1 86  PHE n 
1 87  ILE n 
1 88  LYS n 
1 89  GLU n 
1 90  LEU n 
1 91  LEU n 
1 92  TRP n 
1 93  MET n 
1 94  LEU n 
1 95  ARG n 
1 96  HIS n 
1 97  GLN n 
1 98  LYS n 
1 99  ASP n 
1 100 ILE n 
1 101 PHE n 
1 102 ASN n 
1 103 ASN n 
1 104 LEU n 
1 105 ALA n 
1 106 ARG n 
1 107 GLN n 
1 108 PHE n 
1 109 GLN n 
1 110 LYS n 
1 111 GLU n 
1 112 VAL n 
1 113 LEU n 
1 114 CYS n 
1 115 PRO n 
1 116 ASN n 
1 117 LYS n 
1 118 CYS n 
1 119 GLY n 
1 120 VAL n 
1 121 MET n 
1 122 SER n 
1 123 GLN n 
1 124 THR n 
1 125 LEU n 
1 126 ILE n 
1 127 TRP n 
1 128 CYS n 
1 129 LEU n 
1 130 LYS n 
1 131 CYS n 
1 132 GLU n 
1 133 LYS n 
1 134 GLN n 
1 135 LEU n 
1 136 HIS n 
1 137 ILE n 
1 138 CYS n 
1 139 ARG n 
1 140 LYS n 
1 141 SER n 
1 142 LEU n 
1 143 ASP n 
1 144 CYS n 
1 145 GLY n 
1 146 GLU n 
1 147 ARG n 
1 148 HIS n 
1 149 ILE n 
1 150 GLU n 
1 151 VAL n 
1 152 HIS n 
1 153 ARG n 
1 154 SER n 
1 155 GLU n 
1 156 ASP n 
1 157 LEU n 
1 158 VAL n 
1 159 LEU n 
1 160 ASP n 
1 161 CYS n 
1 162 LEU n 
1 163 LEU n 
1 164 SER n 
1 165 TRP n 
1 166 HIS n 
1 167 ARG n 
1 168 ALA n 
1 169 SER n 
1 170 LYS n 
1 171 GLY n 
1 172 LEU n 
1 173 THR n 
1 174 ASP n 
1 175 TYR n 
1 176 SER n 
1 177 PHE n 
1 178 TYR n 
1 179 ARG n 
1 180 VAL n 
1 181 TRP n 
1 182 GLU n 
1 183 ASN n 
1 184 SER n 
1 185 SER n 
1 186 GLU n 
1 187 THR n 
1 188 LEU n 
1 189 ILE n 
1 190 ALA n 
1 191 LYS n 
1 192 GLY n 
1 193 LYS n 
1 194 GLU n 
1 195 PRO n 
1 196 TYR n 
1 197 LEU n 
1 198 THR n 
1 199 LYS n 
1 200 SER n 
1 201 MET n 
1 202 VAL n 
1 203 GLY n 
1 204 PRO n 
1 205 GLU n 
1 206 ASP n 
1 207 ALA n 
1 208 GLY n 
1 209 ASN n 
1 210 TYR n 
1 211 ARG n 
1 212 CYS n 
1 213 VAL n 
1 214 LEU n 
1 215 ASP n 
1 216 THR n 
1 217 ILE n 
1 218 ASN n 
1 219 GLN n 
1 220 GLY n 
1 221 HIS n 
1 222 ALA n 
1 223 THR n 
1 224 VAL n 
1 225 ILE n 
1 226 ARG n 
1 227 TYR n 
1 228 ASP n 
1 229 VAL n 
1 230 THR n 
1 231 VAL n 
1 232 LEU n 
1 233 PRO n 
1 234 PRO n 
1 235 LYS 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                   235 
_entity_src_gen.gene_src_common_name               'house mouse' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 Izumo1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Mus musculus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10090 
_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               human 
_entity_src_gen.pdbx_host_org_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            Expi293F 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
1PE non-polymer                   . 'PENTAETHYLENE GLYCOL'                   PEG400 'C10 H22 O6'     238.278 
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 
CA  non-polymer                   . 'CALCIUM ION'                            ? 'Ca 2'           40.078  
CL  non-polymer                   . 'CHLORIDE ION'                           ? 'Cl -1'          35.453  
CYS 'L-peptide linking'           y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
FUC 'L-saccharide, alpha linking' . alpha-L-fucopyranose                     
'alpha-L-fucose; 6-deoxy-alpha-L-galactopyranose; L-fucose; fucose' 'C6 H12 O5'      164.156 
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 
NAG 'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
PEG non-polymer                   . 'DI(HYDROXYETHYL)ETHER'                  ? 'C4 H10 O3'      106.120 
PHE 'L-peptide linking'           y PHENYLALANINE                            ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'           y PROLINE                                  ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking'           y SERINE                                   ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking'           y THREONINE                                ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN                               ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'           y TYROSINE                                 ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'           y VALINE                                   ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
FUC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 LFucpa                         
FUC 'COMMON NAME'                         GMML     1.0 a-L-fucopyranose               
FUC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-L-Fucp                       
FUC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Fuc                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
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   CYS 1   22  22  CYS CYS A . n 
A 1 2   ILE 2   23  23  ILE ILE A . n 
A 1 3   LYS 3   24  24  LYS LYS A . n 
A 1 4   CYS 4   25  25  CYS CYS A . n 
A 1 5   ASP 5   26  26  ASP ASP A . n 
A 1 6   GLN 6   27  27  GLN GLN A . n 
A 1 7   PHE 7   28  28  PHE PHE A . n 
A 1 8   VAL 8   29  29  VAL VAL A . n 
A 1 9   THR 9   30  30  THR THR A . n 
A 1 10  ASP 10  31  31  ASP ASP A . n 
A 1 11  ALA 11  32  32  ALA ALA A . n 
A 1 12  LEU 12  33  33  LEU LEU A . n 
A 1 13  LYS 13  34  34  LYS LYS A . n 
A 1 14  THR 14  35  35  THR THR A . n 
A 1 15  PHE 15  36  36  PHE PHE A . n 
A 1 16  GLU 16  37  37  GLU GLU A . n 
A 1 17  ASN 17  38  38  ASN ASN A . n 
A 1 18  THR 18  39  39  THR THR A . n 
A 1 19  TYR 19  40  40  TYR TYR A . n 
A 1 20  LEU 20  41  41  LEU LEU A . n 
A 1 21  ASN 21  42  42  ASN ASN A . n 
A 1 22  ASP 22  43  43  ASP ASP A . n 
A 1 23  HIS 23  44  44  HIS HIS A . n 
A 1 24  LEU 24  45  45  LEU LEU A . n 
A 1 25  PRO 25  46  46  PRO PRO A . n 
A 1 26  HIS 26  47  47  HIS HIS A . n 
A 1 27  ASP 27  48  48  ASP ASP A . n 
A 1 28  ILE 28  49  49  ILE ILE A . n 
A 1 29  HIS 29  50  50  HIS HIS A . n 
A 1 30  LYS 30  51  51  LYS LYS A . n 
A 1 31  ASN 31  52  52  ASN ASN A . n 
A 1 32  VAL 32  53  53  VAL VAL A . n 
A 1 33  MET 33  54  54  MET MET A . n 
A 1 34  ARG 34  55  55  ARG ARG A . n 
A 1 35  MET 35  56  56  MET MET A . n 
A 1 36  VAL 36  57  57  VAL VAL A . n 
A 1 37  ASN 37  58  58  ASN ASN A . n 
A 1 38  HIS 38  59  59  HIS HIS A . n 
A 1 39  GLU 39  60  60  GLU GLU A . n 
A 1 40  VAL 40  61  61  VAL VAL A . n 
A 1 41  SER 41  62  62  SER SER A . n 
A 1 42  SER 42  63  63  SER SER A . n 
A 1 43  PHE 43  64  64  PHE PHE A . n 
A 1 44  GLY 44  65  65  GLY GLY A . n 
A 1 45  VAL 45  66  66  VAL VAL A . n 
A 1 46  VAL 46  67  67  VAL VAL A . n 
A 1 47  THR 47  68  68  THR THR A . n 
A 1 48  SER 48  69  69  SER SER A . n 
A 1 49  ALA 49  70  70  ALA ALA A . n 
A 1 50  GLU 50  71  71  GLU GLU A . n 
A 1 51  ASP 51  72  72  ASP ASP A . n 
A 1 52  SER 52  73  73  SER SER A . n 
A 1 53  TYR 53  74  74  TYR TYR A . n 
A 1 54  LEU 54  75  75  LEU LEU A . n 
A 1 55  GLY 55  76  76  GLY GLY A . n 
A 1 56  ALA 56  77  77  ALA ALA A . n 
A 1 57  VAL 57  78  78  VAL VAL A . n 
A 1 58  ASP 58  79  79  ASP ASP A . n 
A 1 59  GLU 59  80  80  GLU GLU A . n 
A 1 60  ASN 60  81  81  ASN ASN A . n 
A 1 61  THR 61  82  82  THR THR A . n 
A 1 62  LEU 62  83  83  LEU LEU A . n 
A 1 63  GLU 63  84  84  GLU GLU A . n 
A 1 64  GLN 64  85  85  GLN GLN A . n 
A 1 65  ALA 65  86  86  ALA ALA A . n 
A 1 66  THR 66  87  87  THR THR A . n 
A 1 67  TRP 67  88  88  TRP TRP A . n 
A 1 68  SER 68  89  89  SER SER A . n 
A 1 69  PHE 69  90  90  PHE PHE A . n 
A 1 70  LEU 70  91  91  LEU LEU A . n 
A 1 71  LYS 71  92  92  LYS LYS A . n 
A 1 72  ASP 72  93  93  ASP ASP A . n 
A 1 73  LEU 73  94  94  LEU LEU A . n 
A 1 74  LYS 74  95  95  LYS LYS A . n 
A 1 75  ARG 75  96  96  ARG ARG A . n 
A 1 76  ILE 76  97  97  ILE ILE A . n 
A 1 77  THR 77  98  98  THR THR A . n 
A 1 78  ASP 78  99  99  ASP ASP A . n 
A 1 79  SER 79  100 100 SER SER A . n 
A 1 80  ASP 80  101 101 ASP ASP A . n 
A 1 81  LEU 81  102 102 LEU LEU A . n 
A 1 82  LYS 82  103 103 LYS LYS A . n 
A 1 83  GLY 83  104 104 GLY GLY A . n 
A 1 84  GLU 84  105 105 GLU GLU A . n 
A 1 85  LEU 85  106 106 LEU LEU A . n 
A 1 86  PHE 86  107 107 PHE PHE A . n 
A 1 87  ILE 87  108 108 ILE ILE A . n 
A 1 88  LYS 88  109 109 LYS LYS A . n 
A 1 89  GLU 89  110 110 GLU GLU A . n 
A 1 90  LEU 90  111 111 LEU LEU A . n 
A 1 91  LEU 91  112 112 LEU LEU A . n 
A 1 92  TRP 92  113 113 TRP TRP A . n 
A 1 93  MET 93  114 114 MET MET A . n 
A 1 94  LEU 94  115 115 LEU LEU A . n 
A 1 95  ARG 95  116 116 ARG ARG A . n 
A 1 96  HIS 96  117 117 HIS HIS A . n 
A 1 97  GLN 97  118 118 GLN GLN A . n 
A 1 98  LYS 98  119 119 LYS LYS A . n 
A 1 99  ASP 99  120 120 ASP ASP A . n 
A 1 100 ILE 100 121 121 ILE ILE A . n 
A 1 101 PHE 101 122 122 PHE PHE A . n 
A 1 102 ASN 102 123 123 ASN ASN A . n 
A 1 103 ASN 103 124 124 ASN ASN A . n 
A 1 104 LEU 104 125 125 LEU LEU A . n 
A 1 105 ALA 105 126 126 ALA ALA A . n 
A 1 106 ARG 106 127 127 ARG ARG A . n 
A 1 107 GLN 107 128 128 GLN GLN A . n 
A 1 108 PHE 108 129 129 PHE PHE A . n 
A 1 109 GLN 109 130 130 GLN GLN A . n 
A 1 110 LYS 110 131 131 LYS LYS A . n 
A 1 111 GLU 111 132 132 GLU GLU A . n 
A 1 112 VAL 112 133 133 VAL VAL A . n 
A 1 113 LEU 113 134 134 LEU LEU A . n 
A 1 114 CYS 114 135 135 CYS CYS A . n 
A 1 115 PRO 115 136 136 PRO PRO A . n 
A 1 116 ASN 116 137 137 ASN ASN A . n 
A 1 117 LYS 117 138 138 LYS LYS A . n 
A 1 118 CYS 118 139 139 CYS CYS A . n 
A 1 119 GLY 119 140 140 GLY GLY A . n 
A 1 120 VAL 120 141 141 VAL VAL A . n 
A 1 121 MET 121 142 142 MET MET A . n 
A 1 122 SER 122 143 143 SER SER A . n 
A 1 123 GLN 123 144 144 GLN GLN A . n 
A 1 124 THR 124 145 145 THR THR A . n 
A 1 125 LEU 125 146 146 LEU LEU A . n 
A 1 126 ILE 126 147 147 ILE ILE A . n 
A 1 127 TRP 127 148 148 TRP TRP A . n 
A 1 128 CYS 128 149 149 CYS CYS A . n 
A 1 129 LEU 129 150 150 LEU LEU A . n 
A 1 130 LYS 130 151 151 LYS LYS A . n 
A 1 131 CYS 131 152 152 CYS CYS A . n 
A 1 132 GLU 132 153 153 GLU GLU A . n 
A 1 133 LYS 133 154 154 LYS LYS A . n 
A 1 134 GLN 134 155 155 GLN GLN A . n 
A 1 135 LEU 135 156 156 LEU LEU A . n 
A 1 136 HIS 136 157 157 HIS HIS A . n 
A 1 137 ILE 137 158 158 ILE ILE A . n 
A 1 138 CYS 138 159 159 CYS CYS A . n 
A 1 139 ARG 139 160 160 ARG ARG A . n 
A 1 140 LYS 140 161 161 LYS LYS A . n 
A 1 141 SER 141 162 162 SER SER A . n 
A 1 142 LEU 142 163 163 LEU LEU A . n 
A 1 143 ASP 143 164 164 ASP ASP A . n 
A 1 144 CYS 144 165 165 CYS CYS A . n 
A 1 145 GLY 145 166 166 GLY GLY A . n 
A 1 146 GLU 146 167 167 GLU GLU A . n 
A 1 147 ARG 147 168 168 ARG ARG A . n 
A 1 148 HIS 148 169 169 HIS HIS A . n 
A 1 149 ILE 149 170 170 ILE ILE A . n 
A 1 150 GLU 150 171 171 GLU GLU A . n 
A 1 151 VAL 151 172 172 VAL VAL A . n 
A 1 152 HIS 152 173 173 HIS HIS A . n 
A 1 153 ARG 153 174 174 ARG ARG A . n 
A 1 154 SER 154 175 175 SER SER A . n 
A 1 155 GLU 155 176 176 GLU GLU A . n 
A 1 156 ASP 156 177 177 ASP ASP A . n 
A 1 157 LEU 157 178 178 LEU LEU A . n 
A 1 158 VAL 158 179 179 VAL VAL A . n 
A 1 159 LEU 159 180 180 LEU LEU A . n 
A 1 160 ASP 160 181 181 ASP ASP A . n 
A 1 161 CYS 161 182 182 CYS CYS A . n 
A 1 162 LEU 162 183 183 LEU LEU A . n 
A 1 163 LEU 163 184 184 LEU LEU A . n 
A 1 164 SER 164 185 185 SER SER A . n 
A 1 165 TRP 165 186 186 TRP TRP A . n 
A 1 166 HIS 166 187 187 HIS HIS A . n 
A 1 167 ARG 167 188 188 ARG ARG A . n 
A 1 168 ALA 168 189 189 ALA ALA A . n 
A 1 169 SER 169 190 190 SER SER A . n 
A 1 170 LYS 170 191 191 LYS LYS A . n 
A 1 171 GLY 171 192 192 GLY GLY A . n 
A 1 172 LEU 172 193 193 LEU LEU A . n 
A 1 173 THR 173 194 194 THR THR A . n 
A 1 174 ASP 174 195 195 ASP ASP A . n 
A 1 175 TYR 175 196 196 TYR TYR A . n 
A 1 176 SER 176 197 197 SER SER A . n 
A 1 177 PHE 177 198 198 PHE PHE A . n 
A 1 178 TYR 178 199 199 TYR TYR A . n 
A 1 179 ARG 179 200 200 ARG ARG A . n 
A 1 180 VAL 180 201 201 VAL VAL A . n 
A 1 181 TRP 181 202 202 TRP TRP A . n 
A 1 182 GLU 182 203 203 GLU GLU A . n 
A 1 183 ASN 183 204 204 ASN ASN A . n 
A 1 184 SER 184 205 205 SER SER A . n 
A 1 185 SER 185 206 206 SER SER A . n 
A 1 186 GLU 186 207 207 GLU GLU A . n 
A 1 187 THR 187 208 208 THR THR A . n 
A 1 188 LEU 188 209 209 LEU LEU A . n 
A 1 189 ILE 189 210 210 ILE ILE A . n 
A 1 190 ALA 190 211 211 ALA ALA A . n 
A 1 191 LYS 191 212 212 LYS LYS A . n 
A 1 192 GLY 192 213 213 GLY GLY A . n 
A 1 193 LYS 193 214 214 LYS LYS A . n 
A 1 194 GLU 194 215 215 GLU GLU A . n 
A 1 195 PRO 195 216 216 PRO PRO A . n 
A 1 196 TYR 196 217 217 TYR TYR A . n 
A 1 197 LEU 197 218 218 LEU LEU A . n 
A 1 198 THR 198 219 219 THR THR A . n 
A 1 199 LYS 199 220 220 LYS LYS A . n 
A 1 200 SER 200 221 221 SER SER A . n 
A 1 201 MET 201 222 222 MET MET A . n 
A 1 202 VAL 202 223 223 VAL VAL A . n 
A 1 203 GLY 203 224 224 GLY GLY A . n 
A 1 204 PRO 204 225 225 PRO PRO A . n 
A 1 205 GLU 205 226 226 GLU GLU A . n 
A 1 206 ASP 206 227 227 ASP ASP A . n 
A 1 207 ALA 207 228 228 ALA ALA A . n 
A 1 208 GLY 208 229 229 GLY GLY A . n 
A 1 209 ASN 209 230 230 ASN ASN A . n 
A 1 210 TYR 210 231 231 TYR TYR A . n 
A 1 211 ARG 211 232 232 ARG ARG A . n 
A 1 212 CYS 212 233 233 CYS CYS A . n 
A 1 213 VAL 213 234 234 VAL VAL A . n 
A 1 214 LEU 214 235 235 LEU LEU A . n 
A 1 215 ASP 215 236 236 ASP ASP A . n 
A 1 216 THR 216 237 237 THR THR A . n 
A 1 217 ILE 217 238 238 ILE ILE A . n 
A 1 218 ASN 218 239 239 ASN ASN A . n 
A 1 219 GLN 219 240 240 GLN GLN A . n 
A 1 220 GLY 220 241 241 GLY GLY A . n 
A 1 221 HIS 221 242 242 HIS HIS A . n 
A 1 222 ALA 222 243 243 ALA ALA A . n 
A 1 223 THR 223 244 244 THR THR A . n 
A 1 224 VAL 224 245 245 VAL VAL A . n 
A 1 225 ILE 225 246 246 ILE ILE A . n 
A 1 226 ARG 226 247 247 ARG ARG A . n 
A 1 227 TYR 227 248 248 TYR TYR A . n 
A 1 228 ASP 228 249 249 ASP ASP A . n 
A 1 229 VAL 229 250 250 VAL VAL A . n 
A 1 230 THR 230 251 251 THR THR A . n 
A 1 231 VAL 231 252 252 VAL VAL A . n 
A 1 232 LEU 232 253 253 LEU LEU A . n 
A 1 233 PRO 233 254 254 PRO PRO A . n 
A 1 234 PRO 234 255 255 PRO PRO A . n 
A 1 235 LYS 235 256 256 LYS LYS 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 NAG 1   1501 1501 NAG NAG A . 
C 3 FUC 1   1502 1601 FUC FUC A . 
D 2 NAG 1   1503 1701 NAG NAG A . 
E 4 PEG 1   1504 1801 PEG PEG A . 
F 5 1PE 1   1505 1901 1PE 1PE A . 
G 4 PEG 1   1506 1301 PEG PEG A . 
H 6 CL  1   1507 1    CL  CL  A . 
I 7 CA  1   1508 1    CA  CA  A . 
J 7 CA  1   1509 2    CA  CA  A . 
K 8 HOH 1   1601 280  HOH HOH A . 
K 8 HOH 2   1602 308  HOH HOH A . 
K 8 HOH 3   1603 215  HOH HOH A . 
K 8 HOH 4   1604 294  HOH HOH A . 
K 8 HOH 5   1605 315  HOH HOH A . 
K 8 HOH 6   1606 291  HOH HOH A . 
K 8 HOH 7   1607 281  HOH HOH A . 
K 8 HOH 8   1608 306  HOH HOH A . 
K 8 HOH 9   1609 309  HOH HOH A . 
K 8 HOH 10  1610 96   HOH HOH A . 
K 8 HOH 11  1611 193  HOH HOH A . 
K 8 HOH 12  1612 64   HOH HOH A . 
K 8 HOH 13  1613 67   HOH HOH A . 
K 8 HOH 14  1614 226  HOH HOH A . 
K 8 HOH 15  1615 111  HOH HOH A . 
K 8 HOH 16  1616 39   HOH HOH A . 
K 8 HOH 17  1617 32   HOH HOH A . 
K 8 HOH 18  1618 47   HOH HOH A . 
K 8 HOH 19  1619 133  HOH HOH A . 
K 8 HOH 20  1620 122  HOH HOH A . 
K 8 HOH 21  1621 134  HOH HOH A . 
K 8 HOH 22  1622 94   HOH HOH A . 
K 8 HOH 23  1623 184  HOH HOH A . 
K 8 HOH 24  1624 75   HOH HOH A . 
K 8 HOH 25  1625 90   HOH HOH A . 
K 8 HOH 26  1626 13   HOH HOH A . 
K 8 HOH 27  1627 206  HOH HOH A . 
K 8 HOH 28  1628 100  HOH HOH A . 
K 8 HOH 29  1629 246  HOH HOH A . 
K 8 HOH 30  1630 102  HOH HOH A . 
K 8 HOH 31  1631 239  HOH HOH A . 
K 8 HOH 32  1632 199  HOH HOH A . 
K 8 HOH 33  1633 78   HOH HOH A . 
K 8 HOH 34  1634 182  HOH HOH A . 
K 8 HOH 35  1635 21   HOH HOH A . 
K 8 HOH 36  1636 125  HOH HOH A . 
K 8 HOH 37  1637 181  HOH HOH A . 
K 8 HOH 38  1638 169  HOH HOH A . 
K 8 HOH 39  1639 103  HOH HOH A . 
K 8 HOH 40  1640 12   HOH HOH A . 
K 8 HOH 41  1641 4    HOH HOH A . 
K 8 HOH 42  1642 65   HOH HOH A . 
K 8 HOH 43  1643 138  HOH HOH A . 
K 8 HOH 44  1644 192  HOH HOH A . 
K 8 HOH 45  1645 161  HOH HOH A . 
K 8 HOH 46  1646 242  HOH HOH A . 
K 8 HOH 47  1647 170  HOH HOH A . 
K 8 HOH 48  1648 253  HOH HOH A . 
K 8 HOH 49  1649 20   HOH HOH A . 
K 8 HOH 50  1650 106  HOH HOH A . 
K 8 HOH 51  1651 252  HOH HOH A . 
K 8 HOH 52  1652 141  HOH HOH A . 
K 8 HOH 53  1653 88   HOH HOH A . 
K 8 HOH 54  1654 14   HOH HOH A . 
K 8 HOH 55  1655 201  HOH HOH A . 
K 8 HOH 56  1656 120  HOH HOH A . 
K 8 HOH 57  1657 208  HOH HOH A . 
K 8 HOH 58  1658 11   HOH HOH A . 
K 8 HOH 59  1659 17   HOH HOH A . 
K 8 HOH 60  1660 276  HOH HOH A . 
K 8 HOH 61  1661 259  HOH HOH A . 
K 8 HOH 62  1662 8    HOH HOH A . 
K 8 HOH 63  1663 162  HOH HOH A . 
K 8 HOH 64  1664 115  HOH HOH A . 
K 8 HOH 65  1665 317  HOH HOH A . 
K 8 HOH 66  1666 52   HOH HOH A . 
K 8 HOH 67  1667 2    HOH HOH A . 
K 8 HOH 68  1668 235  HOH HOH A . 
K 8 HOH 69  1669 203  HOH HOH A . 
K 8 HOH 70  1670 89   HOH HOH A . 
K 8 HOH 71  1671 93   HOH HOH A . 
K 8 HOH 72  1672 212  HOH HOH A . 
K 8 HOH 73  1673 105  HOH HOH A . 
K 8 HOH 74  1674 76   HOH HOH A . 
K 8 HOH 75  1675 53   HOH HOH A . 
K 8 HOH 76  1676 77   HOH HOH A . 
K 8 HOH 77  1677 108  HOH HOH A . 
K 8 HOH 78  1678 56   HOH HOH A . 
K 8 HOH 79  1679 132  HOH HOH A . 
K 8 HOH 80  1680 204  HOH HOH A . 
K 8 HOH 81  1681 55   HOH HOH A . 
K 8 HOH 82  1682 24   HOH HOH A . 
K 8 HOH 83  1683 256  HOH HOH A . 
K 8 HOH 84  1684 41   HOH HOH A . 
K 8 HOH 85  1685 113  HOH HOH A . 
K 8 HOH 86  1686 68   HOH HOH A . 
K 8 HOH 87  1687 144  HOH HOH A . 
K 8 HOH 88  1688 66   HOH HOH A . 
K 8 HOH 89  1689 44   HOH HOH A . 
K 8 HOH 90  1690 83   HOH HOH A . 
K 8 HOH 91  1691 27   HOH HOH A . 
K 8 HOH 92  1692 194  HOH HOH A . 
K 8 HOH 93  1693 81   HOH HOH A . 
K 8 HOH 94  1694 5    HOH HOH A . 
K 8 HOH 95  1695 296  HOH HOH A . 
K 8 HOH 96  1696 37   HOH HOH A . 
K 8 HOH 97  1697 19   HOH HOH A . 
K 8 HOH 98  1698 117  HOH HOH A . 
K 8 HOH 99  1699 72   HOH HOH A . 
K 8 HOH 100 1700 60   HOH HOH A . 
K 8 HOH 101 1701 157  HOH HOH A . 
K 8 HOH 102 1702 18   HOH HOH A . 
K 8 HOH 103 1703 260  HOH HOH A . 
K 8 HOH 104 1704 29   HOH HOH A . 
K 8 HOH 105 1705 63   HOH HOH A . 
K 8 HOH 106 1706 15   HOH HOH A . 
K 8 HOH 107 1707 22   HOH HOH A . 
K 8 HOH 108 1708 45   HOH HOH A . 
K 8 HOH 109 1709 116  HOH HOH A . 
K 8 HOH 110 1710 48   HOH HOH A . 
K 8 HOH 111 1711 240  HOH HOH A . 
K 8 HOH 112 1712 234  HOH HOH A . 
K 8 HOH 113 1713 98   HOH HOH A . 
K 8 HOH 114 1714 38   HOH HOH A . 
K 8 HOH 115 1715 34   HOH HOH A . 
K 8 HOH 116 1716 191  HOH HOH A . 
K 8 HOH 117 1717 279  HOH HOH A . 
K 8 HOH 118 1718 71   HOH HOH A . 
K 8 HOH 119 1719 26   HOH HOH A . 
K 8 HOH 120 1720 28   HOH HOH A . 
K 8 HOH 121 1721 187  HOH HOH A . 
K 8 HOH 122 1722 243  HOH HOH A . 
K 8 HOH 123 1723 126  HOH HOH A . 
K 8 HOH 124 1724 261  HOH HOH A . 
K 8 HOH 125 1725 140  HOH HOH A . 
K 8 HOH 126 1726 205  HOH HOH A . 
K 8 HOH 127 1727 74   HOH HOH A . 
K 8 HOH 128 1728 31   HOH HOH A . 
K 8 HOH 129 1729 179  HOH HOH A . 
K 8 HOH 130 1730 158  HOH HOH A . 
K 8 HOH 131 1731 50   HOH HOH A . 
K 8 HOH 132 1732 207  HOH HOH A . 
K 8 HOH 133 1733 154  HOH HOH A . 
K 8 HOH 134 1734 288  HOH HOH A . 
K 8 HOH 135 1735 290  HOH HOH A . 
K 8 HOH 136 1736 23   HOH HOH A . 
K 8 HOH 137 1737 166  HOH HOH A . 
K 8 HOH 138 1738 272  HOH HOH A . 
K 8 HOH 139 1739 247  HOH HOH A . 
K 8 HOH 140 1740 35   HOH HOH A . 
K 8 HOH 141 1741 6    HOH HOH A . 
K 8 HOH 142 1742 258  HOH HOH A . 
K 8 HOH 143 1743 51   HOH HOH A . 
K 8 HOH 144 1744 110  HOH HOH A . 
K 8 HOH 145 1745 229  HOH HOH A . 
K 8 HOH 146 1746 202  HOH HOH A . 
K 8 HOH 147 1747 145  HOH HOH A . 
K 8 HOH 148 1748 42   HOH HOH A . 
K 8 HOH 149 1749 58   HOH HOH A . 
K 8 HOH 150 1750 277  HOH HOH A . 
K 8 HOH 151 1751 244  HOH HOH A . 
K 8 HOH 152 1752 174  HOH HOH A . 
K 8 HOH 153 1753 238  HOH HOH A . 
K 8 HOH 154 1754 213  HOH HOH A . 
K 8 HOH 155 1755 25   HOH HOH A . 
K 8 HOH 156 1756 316  HOH HOH A . 
K 8 HOH 157 1757 200  HOH HOH A . 
K 8 HOH 158 1758 171  HOH HOH A . 
K 8 HOH 159 1759 123  HOH HOH A . 
K 8 HOH 160 1760 137  HOH HOH A . 
K 8 HOH 161 1761 172  HOH HOH A . 
K 8 HOH 162 1762 46   HOH HOH A . 
K 8 HOH 163 1763 87   HOH HOH A . 
K 8 HOH 164 1764 49   HOH HOH A . 
K 8 HOH 165 1765 70   HOH HOH A . 
K 8 HOH 166 1766 160  HOH HOH A . 
K 8 HOH 167 1767 16   HOH HOH A . 
K 8 HOH 168 1768 95   HOH HOH A . 
K 8 HOH 169 1769 86   HOH HOH A . 
K 8 HOH 170 1770 104  HOH HOH A . 
K 8 HOH 171 1771 7    HOH HOH A . 
K 8 HOH 172 1772 183  HOH HOH A . 
K 8 HOH 173 1773 227  HOH HOH A . 
K 8 HOH 174 1774 36   HOH HOH A . 
K 8 HOH 175 1775 263  HOH HOH A . 
K 8 HOH 176 1776 107  HOH HOH A . 
K 8 HOH 177 1777 287  HOH HOH A . 
K 8 HOH 178 1778 10   HOH HOH A . 
K 8 HOH 179 1779 118  HOH HOH A . 
K 8 HOH 180 1780 73   HOH HOH A . 
K 8 HOH 181 1781 130  HOH HOH A . 
K 8 HOH 182 1782 190  HOH HOH A . 
K 8 HOH 183 1783 311  HOH HOH A . 
K 8 HOH 184 1784 222  HOH HOH A . 
K 8 HOH 185 1785 270  HOH HOH A . 
K 8 HOH 186 1786 297  HOH HOH A . 
K 8 HOH 187 1787 286  HOH HOH A . 
K 8 HOH 188 1788 323  HOH HOH A . 
K 8 HOH 189 1789 186  HOH HOH A . 
K 8 HOH 190 1790 69   HOH HOH A . 
K 8 HOH 191 1791 9    HOH HOH A . 
K 8 HOH 192 1792 139  HOH HOH A . 
K 8 HOH 193 1793 97   HOH HOH A . 
K 8 HOH 194 1794 124  HOH HOH A . 
K 8 HOH 195 1795 54   HOH HOH A . 
K 8 HOH 196 1796 91   HOH HOH A . 
K 8 HOH 197 1797 142  HOH HOH A . 
K 8 HOH 198 1798 301  HOH HOH A . 
K 8 HOH 199 1799 209  HOH HOH A . 
K 8 HOH 200 1800 303  HOH HOH A . 
K 8 HOH 201 1801 251  HOH HOH A . 
K 8 HOH 202 1802 230  HOH HOH A . 
K 8 HOH 203 1803 302  HOH HOH A . 
K 8 HOH 204 1804 135  HOH HOH A . 
K 8 HOH 205 1805 156  HOH HOH A . 
K 8 HOH 206 1806 299  HOH HOH A . 
K 8 HOH 207 1807 248  HOH HOH A . 
K 8 HOH 208 1808 40   HOH HOH A . 
K 8 HOH 209 1809 180  HOH HOH A . 
K 8 HOH 210 1810 218  HOH HOH A . 
K 8 HOH 211 1811 176  HOH HOH A . 
K 8 HOH 212 1812 220  HOH HOH A . 
K 8 HOH 213 1813 146  HOH HOH A . 
K 8 HOH 214 1814 3    HOH HOH A . 
K 8 HOH 215 1815 109  HOH HOH A . 
K 8 HOH 216 1816 128  HOH HOH A . 
K 8 HOH 217 1817 167  HOH HOH A . 
K 8 HOH 218 1818 310  HOH HOH A . 
K 8 HOH 219 1819 237  HOH HOH A . 
K 8 HOH 220 1820 313  HOH HOH A . 
K 8 HOH 221 1821 231  HOH HOH A . 
K 8 HOH 222 1822 233  HOH HOH A . 
K 8 HOH 223 1823 61   HOH HOH A . 
K 8 HOH 224 1824 43   HOH HOH A . 
K 8 HOH 225 1825 236  HOH HOH A . 
K 8 HOH 226 1826 143  HOH HOH A . 
K 8 HOH 227 1827 232  HOH HOH A . 
K 8 HOH 228 1828 148  HOH HOH A . 
K 8 HOH 229 1829 188  HOH HOH A . 
K 8 HOH 230 1830 99   HOH HOH A . 
K 8 HOH 231 1831 198  HOH HOH A . 
K 8 HOH 232 1832 223  HOH HOH A . 
K 8 HOH 233 1833 285  HOH HOH A . 
K 8 HOH 234 1834 319  HOH HOH A . 
K 8 HOH 235 1835 254  HOH HOH A . 
K 8 HOH 236 1836 82   HOH HOH A . 
K 8 HOH 237 1837 275  HOH HOH A . 
K 8 HOH 238 1838 250  HOH HOH A . 
K 8 HOH 239 1839 257  HOH HOH A . 
K 8 HOH 240 1840 216  HOH HOH A . 
K 8 HOH 241 1841 266  HOH HOH A . 
K 8 HOH 242 1842 1    HOH HOH A . 
K 8 HOH 243 1843 159  HOH HOH A . 
K 8 HOH 244 1844 127  HOH HOH A . 
K 8 HOH 245 1845 62   HOH HOH A . 
K 8 HOH 246 1846 84   HOH HOH A . 
K 8 HOH 247 1847 217  HOH HOH A . 
K 8 HOH 248 1848 164  HOH HOH A . 
K 8 HOH 249 1849 210  HOH HOH A . 
K 8 HOH 250 1850 262  HOH HOH A . 
K 8 HOH 251 1851 30   HOH HOH A . 
K 8 HOH 252 1852 175  HOH HOH A . 
K 8 HOH 253 1853 59   HOH HOH A . 
K 8 HOH 254 1854 165  HOH HOH A . 
K 8 HOH 255 1855 150  HOH HOH A . 
K 8 HOH 256 1856 264  HOH HOH A . 
K 8 HOH 257 1857 155  HOH HOH A . 
K 8 HOH 258 1858 225  HOH HOH A . 
K 8 HOH 259 1859 79   HOH HOH A . 
K 8 HOH 260 1860 196  HOH HOH A . 
K 8 HOH 261 1861 312  HOH HOH A . 
K 8 HOH 262 1862 245  HOH HOH A . 
K 8 HOH 263 1863 305  HOH HOH A . 
K 8 HOH 264 1864 268  HOH HOH A . 
K 8 HOH 265 1865 219  HOH HOH A . 
K 8 HOH 266 1866 149  HOH HOH A . 
K 8 HOH 267 1867 131  HOH HOH A . 
K 8 HOH 268 1868 147  HOH HOH A . 
K 8 HOH 269 1869 173  HOH HOH A . 
K 8 HOH 270 1870 249  HOH HOH A . 
K 8 HOH 271 1871 195  HOH HOH A . 
K 8 HOH 272 1872 307  HOH HOH A . 
K 8 HOH 273 1873 101  HOH HOH A . 
K 8 HOH 274 1874 300  HOH HOH A . 
K 8 HOH 275 1875 265  HOH HOH A . 
K 8 HOH 276 1876 304  HOH HOH A . 
K 8 HOH 277 1877 177  HOH HOH A . 
K 8 HOH 278 1878 33   HOH HOH A . 
K 8 HOH 279 1879 283  HOH HOH A . 
K 8 HOH 280 1880 284  HOH HOH A . 
K 8 HOH 281 1881 298  HOH HOH A . 
K 8 HOH 282 1882 314  HOH HOH A . 
K 8 HOH 283 1883 293  HOH HOH A . 
K 8 HOH 284 1884 121  HOH HOH A . 
K 8 HOH 285 1885 163  HOH HOH A . 
K 8 HOH 286 1886 228  HOH HOH A . 
K 8 HOH 287 1887 92   HOH HOH A . 
K 8 HOH 288 1888 185  HOH HOH A . 
K 8 HOH 289 1889 241  HOH HOH A . 
K 8 HOH 290 1890 214  HOH HOH A . 
K 8 HOH 291 1891 267  HOH HOH A . 
K 8 HOH 292 1892 168  HOH HOH A . 
K 8 HOH 293 1893 57   HOH HOH A . 
K 8 HOH 294 1894 85   HOH HOH A . 
K 8 HOH 295 1895 178  HOH HOH A . 
K 8 HOH 296 1896 152  HOH HOH A . 
K 8 HOH 297 1897 136  HOH HOH A . 
K 8 HOH 298 1898 282  HOH HOH A . 
K 8 HOH 299 1899 320  HOH HOH A . 
K 8 HOH 300 1900 278  HOH HOH A . 
K 8 HOH 301 1901 114  HOH HOH A . 
K 8 HOH 302 1902 119  HOH HOH A . 
K 8 HOH 303 1903 80   HOH HOH A . 
K 8 HOH 304 1904 112  HOH HOH A . 
K 8 HOH 305 1905 189  HOH HOH A . 
K 8 HOH 306 1906 295  HOH HOH A . 
K 8 HOH 307 1907 221  HOH HOH A . 
K 8 HOH 308 1908 271  HOH HOH A . 
K 8 HOH 309 1909 324  HOH HOH A . 
K 8 HOH 310 1910 255  HOH HOH A . 
K 8 HOH 311 1911 197  HOH HOH A . 
K 8 HOH 312 1912 151  HOH HOH A . 
K 8 HOH 313 1913 318  HOH HOH A . 
K 8 HOH 314 1914 224  HOH HOH A . 
K 8 HOH 315 1915 292  HOH HOH A . 
K 8 HOH 316 1916 274  HOH HOH A . 
K 8 HOH 317 1917 289  HOH HOH A . 
K 8 HOH 318 1918 273  HOH HOH A . 
K 8 HOH 319 1919 321  HOH HOH A . 
K 8 HOH 320 1920 269  HOH HOH A . 
K 8 HOH 321 1921 129  HOH HOH A . 
K 8 HOH 322 1922 153  HOH HOH A . 
K 8 HOH 323 1923 322  HOH HOH A . 
K 8 HOH 324 1924 211  HOH HOH A . 
K 8 HOH 325 1925 325  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 34   ? CD  ? A LYS 13  CD  
2  1 Y 1 A LYS 34   ? CE  ? A LYS 13  CE  
3  1 Y 1 A LYS 34   ? NZ  ? A LYS 13  NZ  
4  1 Y 1 A LYS 103  ? NZ  ? A LYS 82  NZ  
5  1 Y 1 A ARG 127  ? NE  ? A ARG 106 NE  
6  1 Y 1 A ARG 127  ? CZ  ? A ARG 106 CZ  
7  1 Y 1 A ARG 127  ? NH1 ? A ARG 106 NH1 
8  1 Y 1 A ARG 127  ? NH2 ? A ARG 106 NH2 
9  1 Y 1 A LYS 131  ? CG  ? A LYS 110 CG  
10 1 Y 1 A LYS 131  ? CD  ? A LYS 110 CD  
11 1 Y 1 A LYS 131  ? CE  ? A LYS 110 CE  
12 1 Y 1 A LYS 131  ? NZ  ? A LYS 110 NZ  
13 1 Y 1 A LYS 151  ? CE  ? A LYS 130 CE  
14 1 Y 1 A LYS 151  ? NZ  ? A LYS 130 NZ  
15 1 Y 1 A ARG 188  ? CG  ? A ARG 167 CG  
16 1 Y 1 A ARG 188  ? CD  ? A ARG 167 CD  
17 1 Y 1 A ARG 188  ? NE  ? A ARG 167 NE  
18 1 Y 1 A ARG 188  ? CZ  ? A ARG 167 CZ  
19 1 Y 1 A ARG 188  ? NH1 ? A ARG 167 NH1 
20 1 Y 1 A ARG 188  ? NH2 ? A ARG 167 NH2 
21 1 N 1 A NAG 1501 ? O1  ? B NAG 1   O1  
22 1 N 1 A FUC 1502 ? O1  ? C FUC 1   O1  
23 1 N 1 A NAG 1503 ? O1  ? D NAG 1   O1  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.9_1692 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9MYM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     103.454 
_cell.length_a_esd                 ? 
_cell.length_b                     103.454 
_cell.length_b_esd                 ? 
_cell.length_c                     139.297 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9MYM 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                97 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 4 2 2' 
_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                   9MYM 
_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             3.43 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          64.10 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '200 mM CaCl2, 100 nM HEPES pH 7.5, 28% PPG P400' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     80 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-05-22 
_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                    'Si(111) and Si(220) double crystal' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97946 
_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                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9MYM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.84 
_reflns.d_resolution_low                               36.58 
_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                                     32920 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.98 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                20 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          27.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.84 
_reflns_shell.d_res_low                                     1.90 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2921 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.790 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9MYM 
_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                            1.843 
_refine.ls_d_res_low                             36.577 
_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                     32920 
_refine.ls_number_reflns_R_free                  1591 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.98 
_refine.ls_percent_reflns_R_free                 4.83 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1706 
_refine.ls_R_factor_R_free                       0.1907 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1695 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 19.58 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.19 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1883 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         71 
_refine_hist.number_atoms_solvent             325 
_refine_hist.number_atoms_total               2279 
_refine_hist.d_res_high                       1.843 
_refine_hist.d_res_low                        36.577 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.018  ? 2111 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.634  ? 2858 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.524 ? 784  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.104  ? 325  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 363  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.843  1.9023 . . 124 2797 100.00 . . . . 0.2482 . . . . . . . . . . . 0.3002 
'X-RAY DIFFRACTION' 1.9023 1.9703 . . 145 2805 100.00 . . . . 0.2003 . . . . . . . . . . . 0.2352 
'X-RAY DIFFRACTION' 1.9703 2.0492 . . 158 2800 100.00 . . . . 0.1819 . . . . . . . . . . . 0.2184 
'X-RAY DIFFRACTION' 2.0492 2.1424 . . 162 2805 100.00 . . . . 0.1723 . . . . . . . . . . . 0.2294 
'X-RAY DIFFRACTION' 2.1424 2.2554 . . 119 2829 100.00 . . . . 0.1625 . . . . . . . . . . . 0.2042 
'X-RAY DIFFRACTION' 2.2554 2.3967 . . 124 2845 100.00 . . . . 0.1647 . . . . . . . . . . . 0.1854 
'X-RAY DIFFRACTION' 2.3967 2.5817 . . 143 2832 100.00 . . . . 0.1678 . . . . . . . . . . . 0.2011 
'X-RAY DIFFRACTION' 2.5817 2.8414 . . 175 2814 100.00 . . . . 0.1769 . . . . . . . . . . . 0.1898 
'X-RAY DIFFRACTION' 2.8414 3.2523 . . 108 2907 100.00 . . . . 0.1683 . . . . . . . . . . . 0.1713 
'X-RAY DIFFRACTION' 3.2523 4.0967 . . 146 2888 100.00 . . . . 0.1529 . . . . . . . . . . . 0.1701 
'X-RAY DIFFRACTION' 4.0967 36.577 . . 187 3007 100.00 . . . . 0.1717 . . . . . . . . . . . 0.1869 
# 
_struct.entry_id                     9MYM 
_struct.title                        'Fertilization IZUMO1 Protein Ectodomain' 
_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        9MYM 
_struct_keywords.text            'Fertilization, Anti-sperm antibody, IZUMO1, Infertility, Contraception, CELL ADHESION' 
_struct_keywords.pdbx_keywords   'CELL ADHESION' 
# 
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 2 ? 
E N N 4 ? 
F N N 5 ? 
G N N 4 ? 
H N N 6 ? 
I N N 7 ? 
J N N 7 ? 
K N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    IZUM1_MOUSE 
_struct_ref.pdbx_db_accession          Q9D9J7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;CIKCDQFVTDALKTFENTYLNDHLPHDIHKNVMRMVNHEVSSFGVVTSAEDSYLGAVDENTLEQATWSFLKDLKRITDSD
LKGELFIKELLWMLRHQKDIFNNLARQFQKEVLCPNKCGVMSQTLIWCLKCEKQLHICRKSLDCGERHIEVHRSEDLVLD
CLLSWHRASKGLTDYSFYRVWENSSETLIAKGKEPYLTKSMVGPEDAGNYRCVLDTINQGHATVIRYDVTVLPPK
;
_struct_ref.pdbx_align_begin           22 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9MYM 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 235 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9D9J7 
_struct_ref_seq.db_align_beg                  22 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  256 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       22 
_struct_ref_seq.pdbx_auth_seq_align_end       256 
# 
_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,H,I,J,K 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 CYS A 1   ? CYS A 4   ? CYS A 22  CYS A 25  5 ? 4  
HELX_P HELX_P2  AA2 ASP A 5   ? THR A 18  ? ASP A 26  THR A 39  1 ? 14 
HELX_P HELX_P3  AA3 TYR A 19  ? HIS A 23  ? TYR A 40  HIS A 44  5 ? 5  
HELX_P HELX_P4  AA4 PRO A 25  ? ASP A 27  ? PRO A 46  ASP A 48  5 ? 3  
HELX_P HELX_P5  AA5 ILE A 28  ? SER A 42  ? ILE A 49  SER A 63  1 ? 15 
HELX_P HELX_P6  AA6 ASP A 51  ? LEU A 54  ? ASP A 72  LEU A 75  5 ? 4  
HELX_P HELX_P7  AA7 GLU A 59  ? SER A 79  ? GLU A 80  SER A 100 1 ? 21 
HELX_P HELX_P8  AA8 LYS A 82  ? VAL A 112 ? LYS A 103 VAL A 133 1 ? 31 
HELX_P HELX_P9  AA9 TRP A 165 ? SER A 169 ? TRP A 186 SER A 190 5 ? 5  
HELX_P HELX_P10 AB1 GLY A 203 ? ALA A 207 ? GLY A 224 ALA A 228 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 1   SG  ? ? ? 1_555 A CYS 128 SG ? ? A CYS 22   A CYS 149  1_555  ? ? ? ? ? ? ? 2.074 ? ? 
disulf2  disulf ? ? A CYS 4   SG  ? ? ? 1_555 A CYS 131 SG ? ? A CYS 25   A CYS 152  1_555  ? ? ? ? ? ? ? 2.074 ? ? 
disulf3  disulf ? ? A CYS 114 SG  ? ? ? 1_555 A CYS 138 SG ? ? A CYS 135  A CYS 159  1_555  ? ? ? ? ? ? ? 2.060 ? ? 
disulf4  disulf ? ? A CYS 118 SG  ? ? ? 1_555 A CYS 144 SG ? ? A CYS 139  A CYS 165  1_555  ? ? ? ? ? ? ? 2.092 ? ? 
disulf5  disulf ? ? A CYS 161 SG  ? ? ? 1_555 A CYS 212 SG ? ? A CYS 182  A CYS 233  1_555  ? ? ? ? ? ? ? 2.086 ? ? 
metalc1  metalc ? ? A ASN 60  OD1 A ? ? 1_555 I CA  .   CA ? ? A ASN 81   A CA  1508 1_555  ? ? ? ? ? ? ? 3.190 ? ? 
metalc2  metalc ? ? A ASN 60  OD1 A ? ? 1_555 I CA  .   CA ? ? A ASN 81   A CA  1508 16_444 ? ? ? ? ? ? ? 3.190 ? ? 
metalc3  metalc ? ? A GLU 84  OE1 ? ? ? 1_555 J CA  .   CA ? ? A GLU 105  A CA  1509 1_555  ? ? ? ? ? ? ? 2.510 ? ? 
metalc4  metalc ? ? A GLU 84  OE2 ? ? ? 1_555 J CA  .   CA ? ? A GLU 105  A CA  1509 1_555  ? ? ? ? ? ? ? 2.918 ? ? 
metalc5  metalc ? ? A GLU 84  OE1 ? ? ? 1_555 J CA  .   CA ? ? A GLU 105  A CA  1509 3_455  ? ? ? ? ? ? ? 2.510 ? ? 
metalc6  metalc ? ? A GLU 84  OE2 ? ? ? 1_555 J CA  .   CA ? ? A GLU 105  A CA  1509 3_455  ? ? ? ? ? ? ? 2.918 ? ? 
metalc7  metalc ? ? I CA  .   CA  ? ? ? 1_555 K HOH .   O  ? ? A CA  1508 A HOH 1718 1_555  ? ? ? ? ? ? ? 2.411 ? ? 
metalc8  metalc ? ? I CA  .   CA  ? ? ? 1_555 K HOH .   O  ? ? A CA  1508 A HOH 1718 16_444 ? ? ? ? ? ? ? 2.411 ? ? 
metalc9  metalc ? ? I CA  .   CA  ? ? ? 1_555 K HOH .   O  ? ? A CA  1508 A HOH 1760 1_555  ? ? ? ? ? ? ? 2.394 ? ? 
metalc10 metalc ? ? I CA  .   CA  ? ? ? 1_555 K HOH .   O  ? ? A CA  1508 A HOH 1760 16_444 ? ? ? ? ? ? ? 2.394 ? ? 
metalc11 metalc ? ? I CA  .   CA  ? ? ? 1_555 K HOH .   O  ? ? A CA  1508 A HOH 1808 1_555  ? ? ? ? ? ? ? 2.456 ? ? 
metalc12 metalc ? ? I CA  .   CA  ? ? ? 1_555 K HOH .   O  ? ? A CA  1508 A HOH 1808 16_444 ? ? ? ? ? ? ? 2.457 ? ? 
metalc13 metalc ? ? I CA  .   CA  ? ? ? 1_555 K HOH .   O  ? ? A CA  1508 A HOH 1878 1_555  ? ? ? ? ? ? ? 2.380 ? ? 
metalc14 metalc ? ? I CA  .   CA  ? ? ? 1_555 K HOH .   O  ? ? A CA  1508 A HOH 1878 16_444 ? ? ? ? ? ? ? 2.380 ? ? 
metalc15 metalc ? ? J CA  .   CA  ? ? ? 1_555 K HOH .   O  ? ? A CA  1509 A HOH 1641 1_555  ? ? ? ? ? ? ? 2.031 ? ? 
metalc16 metalc ? ? J CA  .   CA  ? ? ? 1_555 K HOH .   O  ? ? A CA  1509 A HOH 1641 3_455  ? ? ? ? ? ? ? 2.031 ? ? 
metalc17 metalc ? ? J CA  .   CA  ? ? ? 1_555 K HOH .   O  ? ? A CA  1509 A HOH 1796 1_555  ? ? ? ? ? ? ? 2.637 ? ? 
metalc18 metalc ? ? J CA  .   CA  ? ? ? 1_555 K HOH .   O  ? ? A CA  1509 A HOH 1796 3_455  ? ? ? ? ? ? ? 2.637 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 OD1 A A ASN 60 ? A ASN 81   ? 1_555  0.0   ? 
2  OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1718 ? 1_555  58.4  ? 
3  OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1718 ? 1_555  58.4  ? 
4  OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1718 ? 16_444 140.8 ? 
5  OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1718 ? 16_444 140.8 ? 
6  O   ? K HOH .  ? A HOH 1718 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1718 ? 16_444 150.2 ? 
7  OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1760 ? 1_555  60.8  ? 
8  OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1760 ? 1_555  60.8  ? 
9  O   ? K HOH .  ? A HOH 1718 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1760 ? 1_555  104.9 ? 
10 O   ? K HOH .  ? A HOH 1718 ? 16_444 CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1760 ? 1_555  104.9 ? 
11 OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1760 ? 16_444 60.8  ? 
12 OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1760 ? 16_444 60.8  ? 
13 O   ? K HOH .  ? A HOH 1718 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1760 ? 16_444 104.9 ? 
14 O   ? K HOH .  ? A HOH 1718 ? 16_444 CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1760 ? 16_444 104.9 ? 
15 O   ? K HOH .  ? A HOH 1760 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1760 ? 16_444 0.0   ? 
16 OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1808 ? 1_555  65.5  ? 
17 OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1808 ? 1_555  65.5  ? 
18 O   ? K HOH .  ? A HOH 1718 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1808 ? 1_555  102.0 ? 
19 O   ? K HOH .  ? A HOH 1718 ? 16_444 CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1808 ? 1_555  78.7  ? 
20 O   ? K HOH .  ? A HOH 1760 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1808 ? 1_555  88.8  ? 
21 O   ? K HOH .  ? A HOH 1760 ? 16_444 CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1808 ? 1_555  88.8  ? 
22 OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1808 ? 16_444 113.2 ? 
23 OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1808 ? 16_444 113.2 ? 
24 O   ? K HOH .  ? A HOH 1718 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1808 ? 16_444 78.6  ? 
25 O   ? K HOH .  ? A HOH 1718 ? 16_444 CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1808 ? 16_444 102.0 ? 
26 O   ? K HOH .  ? A HOH 1760 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1808 ? 16_444 88.8  ? 
27 O   ? K HOH .  ? A HOH 1760 ? 16_444 CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1808 ? 16_444 88.8  ? 
28 O   ? K HOH .  ? A HOH 1808 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1808 ? 16_444 177.7 ? 
29 OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 1_555  119.2 ? 
30 OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 1_555  119.2 ? 
31 O   ? K HOH .  ? A HOH 1718 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 1_555  75.1  ? 
32 O   ? K HOH .  ? A HOH 1718 ? 16_444 CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 1_555  75.1  ? 
33 O   ? K HOH .  ? A HOH 1760 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 1_555  180.0 ? 
34 O   ? K HOH .  ? A HOH 1760 ? 16_444 CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 1_555  180.0 ? 
35 O   ? K HOH .  ? A HOH 1808 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 1_555  91.2  ? 
36 O   ? K HOH .  ? A HOH 1808 ? 16_444 CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 1_555  91.2  ? 
37 OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 16_444 119.2 ? 
38 OD1 A A ASN 60 ? A ASN 81   ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 16_444 119.2 ? 
39 O   ? K HOH .  ? A HOH 1718 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 16_444 75.1  ? 
40 O   ? K HOH .  ? A HOH 1718 ? 16_444 CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 16_444 75.1  ? 
41 O   ? K HOH .  ? A HOH 1760 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 16_444 180.0 ? 
42 O   ? K HOH .  ? A HOH 1760 ? 16_444 CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 16_444 180.0 ? 
43 O   ? K HOH .  ? A HOH 1808 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 16_444 91.2  ? 
44 O   ? K HOH .  ? A HOH 1808 ? 16_444 CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 16_444 91.2  ? 
45 O   ? K HOH .  ? A HOH 1878 ? 1_555  CA ? I CA . ? A CA 1508 ? 1_555 O   ? K HOH .  ? A HOH 1878 ? 16_444 0.0   ? 
46 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  47.6  ? 
47 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  0.0   ? 
48 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  47.6  ? 
49 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  47.6  ? 
50 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  0.0   ? 
51 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  47.6  ? 
52 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1641 ? 1_555  108.4 ? 
53 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1641 ? 1_555  61.1  ? 
54 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1641 ? 1_555  108.4 ? 
55 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1641 ? 1_555  61.1  ? 
56 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1641 ? 3_455  108.4 ? 
57 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1641 ? 3_455  61.1  ? 
58 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1641 ? 3_455  108.4 ? 
59 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1641 ? 3_455  61.1  ? 
60 O   ? K HOH .  ? A HOH 1641 ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1641 ? 3_455  0.0   ? 
61 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1796 ? 1_555  71.6  ? 
62 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1796 ? 1_555  118.9 ? 
63 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1796 ? 1_555  71.6  ? 
64 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1796 ? 1_555  118.9 ? 
65 O   ? K HOH .  ? A HOH 1641 ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1796 ? 1_555  180.0 ? 
66 O   ? K HOH .  ? A HOH 1641 ? 3_455  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1796 ? 1_555  180.0 ? 
67 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1796 ? 3_455  71.6  ? 
68 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1796 ? 3_455  118.9 ? 
69 OE1 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1796 ? 3_455  71.6  ? 
70 OE2 ? A GLU 84 ? A GLU 105  ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1796 ? 3_455  118.9 ? 
71 O   ? K HOH .  ? A HOH 1641 ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1796 ? 3_455  180.0 ? 
72 O   ? K HOH .  ? A HOH 1641 ? 3_455  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1796 ? 3_455  180.0 ? 
73 O   ? K HOH .  ? A HOH 1796 ? 1_555  CA ? J CA . ? A CA 1509 ? 1_555 O   ? K HOH .  ? A HOH 1796 ? 3_455  0.0   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 1   ? CYS A 128 ? CYS A 22  ? 1_555 CYS A 149 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 4   ? CYS A 131 ? CYS A 25  ? 1_555 CYS A 152 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 114 ? CYS A 138 ? CYS A 135 ? 1_555 CYS A 159 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS A 118 ? CYS A 144 ? CYS A 139 ? 1_555 CYS A 165 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5 CYS A 161 ? CYS A 212 ? CYS A 182 ? 1_555 CYS A 233 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 56  ? ASP A 58  ? ALA A 77  ASP A 79  
AA1 2 VAL A 120 ? TRP A 127 ? VAL A 141 TRP A 148 
AA1 3 LYS A 133 ? ARG A 139 ? LYS A 154 ARG A 160 
AA2 1 ASP A 143 ? HIS A 152 ? ASP A 164 HIS A 173 
AA2 2 THR A 223 ? LEU A 232 ? THR A 244 LEU A 253 
AA2 3 GLY A 208 ? THR A 216 ? GLY A 229 THR A 237 
AA2 4 LEU A 172 ? VAL A 180 ? LEU A 193 VAL A 201 
AA2 5 GLU A 186 ? GLY A 192 ? GLU A 207 GLY A 213 
AA3 1 LEU A 157 ? ASP A 160 ? LEU A 178 ASP A 181 
AA3 2 TYR A 196 ? LYS A 199 ? TYR A 217 LYS A 220 
# 
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 VAL A 57  ? N VAL A 78  O ILE A 126 ? O ILE A 147 
AA1 2 3 N GLN A 123 ? N GLN A 144 O HIS A 136 ? O HIS A 157 
AA2 1 2 N ARG A 147 ? N ARG A 168 O ARG A 226 ? O ARG A 247 
AA2 2 3 O VAL A 229 ? O VAL A 250 N GLY A 208 ? N GLY A 229 
AA2 3 4 O ASN A 209 ? O ASN A 230 N VAL A 180 ? N VAL A 201 
AA2 4 5 N PHE A 177 ? N PHE A 198 O ILE A 189 ? O ILE A 210 
AA3 1 2 N LEU A 157 ? N LEU A 178 O LYS A 199 ? O LYS A 220 
# 
_pdbx_entry_details.entry_id                   9MYM 
_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   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 1823 ? ? O  A HOH 1896 ? ? 1.66 
2  1 OD2 A ASP 101  ? A O  A HOH 1601 ? ? 1.73 
3  1 O   A HOH 1623 ? ? O  A HOH 1661 ? ? 1.78 
4  1 O   A HOH 1669 ? ? O  A HOH 1734 ? ? 1.80 
5  1 O   A HOH 1751 ? ? O  A HOH 1838 ? ? 1.81 
6  1 O   A HOH 1823 ? ? O  A HOH 1829 ? ? 1.83 
7  1 O   A HOH 1831 ? ? O  A HOH 1873 ? ? 1.84 
8  1 O   A HOH 1764 ? ? O  A HOH 1883 ? ? 1.85 
9  1 OD2 A ASP 31   ? ? O  A HOH 1602 ? ? 1.95 
10 1 O   A HOH 1829 ? ? O  A HOH 1906 ? ? 1.95 
11 1 O   A HOH 1746 ? ? O  A HOH 1910 ? ? 1.96 
12 1 O   A SER 73   ? ? O  A HOH 1603 ? ? 1.98 
13 1 O   A HOH 1725 ? ? O  A HOH 1814 ? ? 2.00 
14 1 O   A HOH 1619 ? ? O  A HOH 1826 ? ? 2.01 
15 1 ND2 A ASN 81   ? B O  A HOH 1604 ? ? 2.07 
16 1 O   A HOH 1792 ? ? O  A HOH 1814 ? ? 2.09 
17 1 NH2 A ARG 174  ? ? O  A HOH 1605 ? ? 2.10 
18 1 O   A HOH 1811 ? ? O  A HOH 1881 ? ? 2.11 
19 1 O7  A NAG 1503 ? ? O  A HOH 1606 ? ? 2.11 
20 1 ND2 A ASN 204  ? ? O5 A NAG 1501 ? ? 2.12 
21 1 O   A ALA 70   ? ? O  A HOH 1607 ? ? 2.14 
22 1 OE1 A GLU 71   ? ? O  A HOH 1608 ? ? 2.17 
23 1 O   A HOH 1724 ? ? O  A HOH 1738 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 C4 A PEG 1504 ? ? 1_555 O4 A PEG 1504 ? ? 2_545 1.44 
2 1 O  A HOH 1806 ? ? 1_555 O  A HOH 1868 ? ? 2_545 1.73 
3 1 O  A HOH 1735 ? ? 1_555 O  A HOH 1809 ? ? 2_545 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 69  ? ? 30.55   -130.57 
2 1 ALA A 70  ? ? 58.14   -139.07 
3 1 CYS A 135 ? ? 37.70   59.97   
4 1 SER A 175 ? ? 79.37   -4.85   
5 1 THR A 194 ? ? -113.72 -96.76  
6 1 SER A 205 ? ? 76.86   -5.29   
7 1 ASN A 239 ? ? -151.04 21.99   
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A PEG 1504 ? E PEG . 
2 1 A CA  1508 ? I CA  . 
3 1 A CA  1509 ? J CA  . 
4 1 A HOH 1641 ? K HOH . 
5 1 A HOH 1760 ? K HOH . 
6 1 A HOH 1796 ? K HOH . 
7 1 A HOH 1878 ? K HOH . 
# 
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 -38.0322 -36.3224 -46.4909 0.2284 ? 0.0004  ? 0.0179  ? 0.1905 ? 0.0018  ? 0.2935 ? 4.8214 ? 
0.2220  ? 2.4568  ? 1.1494 ? 0.3944  ? 2.5710 ? -0.1394 ? -0.0286 ? 0.3440  ? -0.0125 ? 0.0447  ? 0.0802  ? -0.1433 ? -0.0727 ? 
0.1679  ? 
2 'X-RAY DIFFRACTION' ? refined -33.2863 -45.5579 -24.5255 0.8150 ? -0.1048 ? -0.0252 ? 0.9624 ? 0.1304  ? 0.5755 ? 5.8670 ? 
-1.3635 ? -3.3437 ? 0.4585 ? 0.7933  ? 2.0606 ? 0.0339  ? -2.5693 ? -1.3565 ? 1.0712  ? 0.2823  ? 0.5157  ? 1.2805  ? 0.6766  ? 
0.0709  ? 
3 'X-RAY DIFFRACTION' ? refined -27.3985 -44.0234 -44.2076 0.2188 ? -0.0060 ? 0.0113  ? 0.1759 ? -0.0014 ? 0.2794 ? 5.0135 ? 
0.9539  ? 2.9019  ? 1.3229 ? 1.1795  ? 3.3250 ? 0.1030  ? 0.2800  ? -0.3365 ? 0.0427  ? 0.1901  ? -0.1644 ? 0.0471  ? 0.3840  ? 
-0.2764 ? 
4 'X-RAY DIFFRACTION' ? refined -32.9830 -49.1381 -38.2489 0.2963 ? -0.0138 ? -0.0326 ? 0.2649 ? 0.0060  ? 0.3109 ? 8.1434 ? 
1.2552  ? 8.2508  ? 0.8433 ? 0.9098  ? 6.4543 ? 0.4254  ? -0.2588 ? -0.5167 ? 0.2821  ? -0.0305 ? -0.0936 ? 0.4124  ? -0.2698 ? 
-0.3735 ? 
5 'X-RAY DIFFRACTION' ? refined -19.1228 -38.8418 -21.3762 0.2279 ? -0.0166 ? -0.0120 ? 0.2563 ? -0.0107 ? 0.2176 ? 6.6833 ? 
-1.6719 ? 5.3895  ? 0.6333 ? -1.8312 ? 5.8642 ? -0.1603 ? -0.5984 ? 0.1152  ? 0.1840  ? 0.1221  ? 0.1192  ? -0.2492 ? -0.4496 ? 
0.0494  ? 
6 'X-RAY DIFFRACTION' ? refined 6.8285   -48.2076 -11.0218 0.2325 ? -0.0179 ? -0.0180 ? 0.3024 ? -0.0585 ? 0.2286 ? 2.8618 ? 
-3.4408 ? 0.5567  ? 4.5507 ? -0.7802 ? 2.1374 ? -0.4208 ? -0.0893 ? -0.2804 ? 0.1479  ? 0.1847  ? -0.3210 ? 0.1603  ? 0.3376  ? 
0.0944  ? 
7 'X-RAY DIFFRACTION' ? refined 5.5873   -40.2408 -12.0539 0.2296 ? -0.0485 ? 0.0018  ? 0.2874 ? 0.0058  ? 0.2114 ? 3.8326 ? 
-1.6127 ? 1.9226  ? 3.1018 ? -0.6643 ? 1.7041 ? -0.0685 ? 0.2014  ? 0.0364  ? 0.0539  ? -0.0111 ? -0.3981 ? -0.1801 ? 0.3505  ? 
0.0872  ? 
# 
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 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 22 through 63 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 64 through 76 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 77 through 103 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 104 through 132 )
;
5 'X-RAY DIFFRACTION' 5 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 133 through 160 )
;
6 'X-RAY DIFFRACTION' 6 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 161 through 181 )
;
7 'X-RAY DIFFRACTION' 7 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 182 through 256 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1921 ? 6.19 . 
2 1 O ? A HOH 1922 ? 6.19 . 
3 1 O ? A HOH 1923 ? 6.28 . 
4 1 O ? A HOH 1924 ? 6.74 . 
5 1 O ? A HOH 1925 ? 7.21 . 
# 
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 
1PE OH2  O  N N 1   
1PE C12  C  N N 2   
1PE C22  C  N N 3   
1PE OH3  O  N N 4   
1PE C13  C  N N 5   
1PE C23  C  N N 6   
1PE OH4  O  N N 7   
1PE C14  C  N N 8   
1PE C24  C  N N 9   
1PE OH5  O  N N 10  
1PE C15  C  N N 11  
1PE C25  C  N N 12  
1PE OH6  O  N N 13  
1PE C16  C  N N 14  
1PE C26  C  N N 15  
1PE OH7  O  N N 16  
1PE HO2  H  N N 17  
1PE H121 H  N N 18  
1PE H122 H  N N 19  
1PE H221 H  N N 20  
1PE H222 H  N N 21  
1PE H131 H  N N 22  
1PE H132 H  N N 23  
1PE H231 H  N N 24  
1PE H232 H  N N 25  
1PE H141 H  N N 26  
1PE H142 H  N N 27  
1PE H241 H  N N 28  
1PE H242 H  N N 29  
1PE H151 H  N N 30  
1PE H152 H  N N 31  
1PE H251 H  N N 32  
1PE H252 H  N N 33  
1PE H161 H  N N 34  
1PE H162 H  N N 35  
1PE H261 H  N N 36  
1PE H262 H  N N 37  
1PE HO7  H  N N 38  
ALA N    N  N N 39  
ALA CA   C  N S 40  
ALA C    C  N N 41  
ALA O    O  N N 42  
ALA CB   C  N N 43  
ALA OXT  O  N N 44  
ALA H    H  N N 45  
ALA H2   H  N N 46  
ALA HA   H  N N 47  
ALA HB1  H  N N 48  
ALA HB2  H  N N 49  
ALA HB3  H  N N 50  
ALA HXT  H  N N 51  
ARG N    N  N N 52  
ARG CA   C  N S 53  
ARG C    C  N N 54  
ARG O    O  N N 55  
ARG CB   C  N N 56  
ARG CG   C  N N 57  
ARG CD   C  N N 58  
ARG NE   N  N N 59  
ARG CZ   C  N N 60  
ARG NH1  N  N N 61  
ARG NH2  N  N N 62  
ARG OXT  O  N N 63  
ARG H    H  N N 64  
ARG H2   H  N N 65  
ARG HA   H  N N 66  
ARG HB2  H  N N 67  
ARG HB3  H  N N 68  
ARG HG2  H  N N 69  
ARG HG3  H  N N 70  
ARG HD2  H  N N 71  
ARG HD3  H  N N 72  
ARG HE   H  N N 73  
ARG HH11 H  N N 74  
ARG HH12 H  N N 75  
ARG HH21 H  N N 76  
ARG HH22 H  N N 77  
ARG HXT  H  N N 78  
ASN N    N  N N 79  
ASN CA   C  N S 80  
ASN C    C  N N 81  
ASN O    O  N N 82  
ASN CB   C  N N 83  
ASN CG   C  N N 84  
ASN OD1  O  N N 85  
ASN ND2  N  N N 86  
ASN OXT  O  N N 87  
ASN H    H  N N 88  
ASN H2   H  N N 89  
ASN HA   H  N N 90  
ASN HB2  H  N N 91  
ASN HB3  H  N N 92  
ASN HD21 H  N N 93  
ASN HD22 H  N N 94  
ASN HXT  H  N N 95  
ASP N    N  N N 96  
ASP CA   C  N S 97  
ASP C    C  N N 98  
ASP O    O  N N 99  
ASP CB   C  N N 100 
ASP CG   C  N N 101 
ASP OD1  O  N N 102 
ASP OD2  O  N N 103 
ASP OXT  O  N N 104 
ASP H    H  N N 105 
ASP H2   H  N N 106 
ASP HA   H  N N 107 
ASP HB2  H  N N 108 
ASP HB3  H  N N 109 
ASP HD2  H  N N 110 
ASP HXT  H  N N 111 
CA  CA   CA N N 112 
CL  CL   CL N N 113 
CYS N    N  N N 114 
CYS CA   C  N R 115 
CYS C    C  N N 116 
CYS O    O  N N 117 
CYS CB   C  N N 118 
CYS SG   S  N N 119 
CYS OXT  O  N N 120 
CYS H    H  N N 121 
CYS H2   H  N N 122 
CYS HA   H  N N 123 
CYS HB2  H  N N 124 
CYS HB3  H  N N 125 
CYS HG   H  N N 126 
CYS HXT  H  N N 127 
FUC C1   C  N R 128 
FUC C2   C  N S 129 
FUC C3   C  N R 130 
FUC C4   C  N S 131 
FUC C5   C  N S 132 
FUC C6   C  N N 133 
FUC O1   O  N N 134 
FUC O2   O  N N 135 
FUC O3   O  N N 136 
FUC O4   O  N N 137 
FUC O5   O  N N 138 
FUC H1   H  N N 139 
FUC H2   H  N N 140 
FUC H3   H  N N 141 
FUC H4   H  N N 142 
FUC H5   H  N N 143 
FUC H61  H  N N 144 
FUC H62  H  N N 145 
FUC H63  H  N N 146 
FUC HO1  H  N N 147 
FUC HO2  H  N N 148 
FUC HO3  H  N N 149 
FUC HO4  H  N N 150 
GLN N    N  N N 151 
GLN CA   C  N S 152 
GLN C    C  N N 153 
GLN O    O  N N 154 
GLN CB   C  N N 155 
GLN CG   C  N N 156 
GLN CD   C  N N 157 
GLN OE1  O  N N 158 
GLN NE2  N  N N 159 
GLN OXT  O  N N 160 
GLN H    H  N N 161 
GLN H2   H  N N 162 
GLN HA   H  N N 163 
GLN HB2  H  N N 164 
GLN HB3  H  N N 165 
GLN HG2  H  N N 166 
GLN HG3  H  N N 167 
GLN HE21 H  N N 168 
GLN HE22 H  N N 169 
GLN HXT  H  N N 170 
GLU N    N  N N 171 
GLU CA   C  N S 172 
GLU C    C  N N 173 
GLU O    O  N N 174 
GLU CB   C  N N 175 
GLU CG   C  N N 176 
GLU CD   C  N N 177 
GLU OE1  O  N N 178 
GLU OE2  O  N N 179 
GLU OXT  O  N N 180 
GLU H    H  N N 181 
GLU H2   H  N N 182 
GLU HA   H  N N 183 
GLU HB2  H  N N 184 
GLU HB3  H  N N 185 
GLU HG2  H  N N 186 
GLU HG3  H  N N 187 
GLU HE2  H  N N 188 
GLU HXT  H  N N 189 
GLY N    N  N N 190 
GLY CA   C  N N 191 
GLY C    C  N N 192 
GLY O    O  N N 193 
GLY OXT  O  N N 194 
GLY H    H  N N 195 
GLY H2   H  N N 196 
GLY HA2  H  N N 197 
GLY HA3  H  N N 198 
GLY HXT  H  N N 199 
HIS N    N  N N 200 
HIS CA   C  N S 201 
HIS C    C  N N 202 
HIS O    O  N N 203 
HIS CB   C  N N 204 
HIS CG   C  Y N 205 
HIS ND1  N  Y N 206 
HIS CD2  C  Y N 207 
HIS CE1  C  Y N 208 
HIS NE2  N  Y N 209 
HIS OXT  O  N N 210 
HIS H    H  N N 211 
HIS H2   H  N N 212 
HIS HA   H  N N 213 
HIS HB2  H  N N 214 
HIS HB3  H  N N 215 
HIS HD1  H  N N 216 
HIS HD2  H  N N 217 
HIS HE1  H  N N 218 
HIS HE2  H  N N 219 
HIS HXT  H  N N 220 
HOH O    O  N N 221 
HOH H1   H  N N 222 
HOH H2   H  N N 223 
ILE N    N  N N 224 
ILE CA   C  N S 225 
ILE C    C  N N 226 
ILE O    O  N N 227 
ILE CB   C  N S 228 
ILE CG1  C  N N 229 
ILE CG2  C  N N 230 
ILE CD1  C  N N 231 
ILE OXT  O  N N 232 
ILE H    H  N N 233 
ILE H2   H  N N 234 
ILE HA   H  N N 235 
ILE HB   H  N N 236 
ILE HG12 H  N N 237 
ILE HG13 H  N N 238 
ILE HG21 H  N N 239 
ILE HG22 H  N N 240 
ILE HG23 H  N N 241 
ILE HD11 H  N N 242 
ILE HD12 H  N N 243 
ILE HD13 H  N N 244 
ILE HXT  H  N N 245 
LEU N    N  N N 246 
LEU CA   C  N S 247 
LEU C    C  N N 248 
LEU O    O  N N 249 
LEU CB   C  N N 250 
LEU CG   C  N N 251 
LEU CD1  C  N N 252 
LEU CD2  C  N N 253 
LEU OXT  O  N N 254 
LEU H    H  N N 255 
LEU H2   H  N N 256 
LEU HA   H  N N 257 
LEU HB2  H  N N 258 
LEU HB3  H  N N 259 
LEU HG   H  N N 260 
LEU HD11 H  N N 261 
LEU HD12 H  N N 262 
LEU HD13 H  N N 263 
LEU HD21 H  N N 264 
LEU HD22 H  N N 265 
LEU HD23 H  N N 266 
LEU HXT  H  N N 267 
LYS N    N  N N 268 
LYS CA   C  N S 269 
LYS C    C  N N 270 
LYS O    O  N N 271 
LYS CB   C  N N 272 
LYS CG   C  N N 273 
LYS CD   C  N N 274 
LYS CE   C  N N 275 
LYS NZ   N  N N 276 
LYS OXT  O  N N 277 
LYS H    H  N N 278 
LYS H2   H  N N 279 
LYS HA   H  N N 280 
LYS HB2  H  N N 281 
LYS HB3  H  N N 282 
LYS HG2  H  N N 283 
LYS HG3  H  N N 284 
LYS HD2  H  N N 285 
LYS HD3  H  N N 286 
LYS HE2  H  N N 287 
LYS HE3  H  N N 288 
LYS HZ1  H  N N 289 
LYS HZ2  H  N N 290 
LYS HZ3  H  N N 291 
LYS HXT  H  N N 292 
MET N    N  N N 293 
MET CA   C  N S 294 
MET C    C  N N 295 
MET O    O  N N 296 
MET CB   C  N N 297 
MET CG   C  N N 298 
MET SD   S  N N 299 
MET CE   C  N N 300 
MET OXT  O  N N 301 
MET H    H  N N 302 
MET H2   H  N N 303 
MET HA   H  N N 304 
MET HB2  H  N N 305 
MET HB3  H  N N 306 
MET HG2  H  N N 307 
MET HG3  H  N N 308 
MET HE1  H  N N 309 
MET HE2  H  N N 310 
MET HE3  H  N N 311 
MET HXT  H  N N 312 
NAG C1   C  N R 313 
NAG C2   C  N R 314 
NAG C3   C  N R 315 
NAG C4   C  N S 316 
NAG C5   C  N R 317 
NAG C6   C  N N 318 
NAG C7   C  N N 319 
NAG C8   C  N N 320 
NAG N2   N  N N 321 
NAG O1   O  N N 322 
NAG O3   O  N N 323 
NAG O4   O  N N 324 
NAG O5   O  N N 325 
NAG O6   O  N N 326 
NAG O7   O  N N 327 
NAG H1   H  N N 328 
NAG H2   H  N N 329 
NAG H3   H  N N 330 
NAG H4   H  N N 331 
NAG H5   H  N N 332 
NAG H61  H  N N 333 
NAG H62  H  N N 334 
NAG H81  H  N N 335 
NAG H82  H  N N 336 
NAG H83  H  N N 337 
NAG HN2  H  N N 338 
NAG HO1  H  N N 339 
NAG HO3  H  N N 340 
NAG HO4  H  N N 341 
NAG HO6  H  N N 342 
PEG C1   C  N N 343 
PEG O1   O  N N 344 
PEG C2   C  N N 345 
PEG O2   O  N N 346 
PEG C3   C  N N 347 
PEG C4   C  N N 348 
PEG O4   O  N N 349 
PEG H11  H  N N 350 
PEG H12  H  N N 351 
PEG HO1  H  N N 352 
PEG H21  H  N N 353 
PEG H22  H  N N 354 
PEG H31  H  N N 355 
PEG H32  H  N N 356 
PEG H41  H  N N 357 
PEG H42  H  N N 358 
PEG HO4  H  N N 359 
PHE N    N  N N 360 
PHE CA   C  N S 361 
PHE C    C  N N 362 
PHE O    O  N N 363 
PHE CB   C  N N 364 
PHE CG   C  Y N 365 
PHE CD1  C  Y N 366 
PHE CD2  C  Y N 367 
PHE CE1  C  Y N 368 
PHE CE2  C  Y N 369 
PHE CZ   C  Y N 370 
PHE OXT  O  N N 371 
PHE H    H  N N 372 
PHE H2   H  N N 373 
PHE HA   H  N N 374 
PHE HB2  H  N N 375 
PHE HB3  H  N N 376 
PHE HD1  H  N N 377 
PHE HD2  H  N N 378 
PHE HE1  H  N N 379 
PHE HE2  H  N N 380 
PHE HZ   H  N N 381 
PHE HXT  H  N N 382 
PRO N    N  N N 383 
PRO CA   C  N S 384 
PRO C    C  N N 385 
PRO O    O  N N 386 
PRO CB   C  N N 387 
PRO CG   C  N N 388 
PRO CD   C  N N 389 
PRO OXT  O  N N 390 
PRO H    H  N N 391 
PRO HA   H  N N 392 
PRO HB2  H  N N 393 
PRO HB3  H  N N 394 
PRO HG2  H  N N 395 
PRO HG3  H  N N 396 
PRO HD2  H  N N 397 
PRO HD3  H  N N 398 
PRO HXT  H  N N 399 
SER N    N  N N 400 
SER CA   C  N S 401 
SER C    C  N N 402 
SER O    O  N N 403 
SER CB   C  N N 404 
SER OG   O  N N 405 
SER OXT  O  N N 406 
SER H    H  N N 407 
SER H2   H  N N 408 
SER HA   H  N N 409 
SER HB2  H  N N 410 
SER HB3  H  N N 411 
SER HG   H  N N 412 
SER HXT  H  N N 413 
THR N    N  N N 414 
THR CA   C  N S 415 
THR C    C  N N 416 
THR O    O  N N 417 
THR CB   C  N R 418 
THR OG1  O  N N 419 
THR CG2  C  N N 420 
THR OXT  O  N N 421 
THR H    H  N N 422 
THR H2   H  N N 423 
THR HA   H  N N 424 
THR HB   H  N N 425 
THR HG1  H  N N 426 
THR HG21 H  N N 427 
THR HG22 H  N N 428 
THR HG23 H  N N 429 
THR HXT  H  N N 430 
TRP N    N  N N 431 
TRP CA   C  N S 432 
TRP C    C  N N 433 
TRP O    O  N N 434 
TRP CB   C  N N 435 
TRP CG   C  Y N 436 
TRP CD1  C  Y N 437 
TRP CD2  C  Y N 438 
TRP NE1  N  Y N 439 
TRP CE2  C  Y N 440 
TRP CE3  C  Y N 441 
TRP CZ2  C  Y N 442 
TRP CZ3  C  Y N 443 
TRP CH2  C  Y N 444 
TRP OXT  O  N N 445 
TRP H    H  N N 446 
TRP H2   H  N N 447 
TRP HA   H  N N 448 
TRP HB2  H  N N 449 
TRP HB3  H  N N 450 
TRP HD1  H  N N 451 
TRP HE1  H  N N 452 
TRP HE3  H  N N 453 
TRP HZ2  H  N N 454 
TRP HZ3  H  N N 455 
TRP HH2  H  N N 456 
TRP HXT  H  N N 457 
TYR N    N  N N 458 
TYR CA   C  N S 459 
TYR C    C  N N 460 
TYR O    O  N N 461 
TYR CB   C  N N 462 
TYR CG   C  Y N 463 
TYR CD1  C  Y N 464 
TYR CD2  C  Y N 465 
TYR CE1  C  Y N 466 
TYR CE2  C  Y N 467 
TYR CZ   C  Y N 468 
TYR OH   O  N N 469 
TYR OXT  O  N N 470 
TYR H    H  N N 471 
TYR H2   H  N N 472 
TYR HA   H  N N 473 
TYR HB2  H  N N 474 
TYR HB3  H  N N 475 
TYR HD1  H  N N 476 
TYR HD2  H  N N 477 
TYR HE1  H  N N 478 
TYR HE2  H  N N 479 
TYR HH   H  N N 480 
TYR HXT  H  N N 481 
VAL N    N  N N 482 
VAL CA   C  N S 483 
VAL C    C  N N 484 
VAL O    O  N N 485 
VAL CB   C  N N 486 
VAL CG1  C  N N 487 
VAL CG2  C  N N 488 
VAL OXT  O  N N 489 
VAL H    H  N N 490 
VAL H2   H  N N 491 
VAL HA   H  N N 492 
VAL HB   H  N N 493 
VAL HG11 H  N N 494 
VAL HG12 H  N N 495 
VAL HG13 H  N N 496 
VAL HG21 H  N N 497 
VAL HG22 H  N N 498 
VAL HG23 H  N N 499 
VAL HXT  H  N N 500 
# 
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 
1PE OH2 C12  sing N N 1   
1PE OH2 HO2  sing N N 2   
1PE C12 C22  sing N N 3   
1PE C12 H121 sing N N 4   
1PE C12 H122 sing N N 5   
1PE C22 OH3  sing N N 6   
1PE C22 H221 sing N N 7   
1PE C22 H222 sing N N 8   
1PE OH3 C23  sing N N 9   
1PE C13 C23  sing N N 10  
1PE C13 OH4  sing N N 11  
1PE C13 H131 sing N N 12  
1PE C13 H132 sing N N 13  
1PE C23 H231 sing N N 14  
1PE C23 H232 sing N N 15  
1PE OH4 C24  sing N N 16  
1PE C14 C24  sing N N 17  
1PE C14 OH5  sing N N 18  
1PE C14 H141 sing N N 19  
1PE C14 H142 sing N N 20  
1PE C24 H241 sing N N 21  
1PE C24 H242 sing N N 22  
1PE OH5 C25  sing N N 23  
1PE C15 C25  sing N N 24  
1PE C15 OH6  sing N N 25  
1PE C15 H151 sing N N 26  
1PE C15 H152 sing N N 27  
1PE C25 H251 sing N N 28  
1PE C25 H252 sing N N 29  
1PE OH6 C26  sing N N 30  
1PE C16 C26  sing N N 31  
1PE C16 OH7  sing N N 32  
1PE C16 H161 sing N N 33  
1PE C16 H162 sing N N 34  
1PE C26 H261 sing N N 35  
1PE C26 H262 sing N N 36  
1PE OH7 HO7  sing N N 37  
ALA N   CA   sing N N 38  
ALA N   H    sing N N 39  
ALA N   H2   sing N N 40  
ALA CA  C    sing N N 41  
ALA CA  CB   sing N N 42  
ALA CA  HA   sing N N 43  
ALA C   O    doub N N 44  
ALA C   OXT  sing N N 45  
ALA CB  HB1  sing N N 46  
ALA CB  HB2  sing N N 47  
ALA CB  HB3  sing N N 48  
ALA OXT HXT  sing N N 49  
ARG N   CA   sing N N 50  
ARG N   H    sing N N 51  
ARG N   H2   sing N N 52  
ARG CA  C    sing N N 53  
ARG CA  CB   sing N N 54  
ARG CA  HA   sing N N 55  
ARG C   O    doub N N 56  
ARG C   OXT  sing N N 57  
ARG CB  CG   sing N N 58  
ARG CB  HB2  sing N N 59  
ARG CB  HB3  sing N N 60  
ARG CG  CD   sing N N 61  
ARG CG  HG2  sing N N 62  
ARG CG  HG3  sing N N 63  
ARG CD  NE   sing N N 64  
ARG CD  HD2  sing N N 65  
ARG CD  HD3  sing N N 66  
ARG NE  CZ   sing N N 67  
ARG NE  HE   sing N N 68  
ARG CZ  NH1  sing N N 69  
ARG CZ  NH2  doub N N 70  
ARG NH1 HH11 sing N N 71  
ARG NH1 HH12 sing N N 72  
ARG NH2 HH21 sing N N 73  
ARG NH2 HH22 sing N N 74  
ARG OXT HXT  sing N N 75  
ASN N   CA   sing N N 76  
ASN N   H    sing N N 77  
ASN N   H2   sing N N 78  
ASN CA  C    sing N N 79  
ASN CA  CB   sing N N 80  
ASN CA  HA   sing N N 81  
ASN C   O    doub N N 82  
ASN C   OXT  sing N N 83  
ASN CB  CG   sing N N 84  
ASN CB  HB2  sing N N 85  
ASN CB  HB3  sing N N 86  
ASN CG  OD1  doub N N 87  
ASN CG  ND2  sing N N 88  
ASN ND2 HD21 sing N N 89  
ASN ND2 HD22 sing N N 90  
ASN OXT HXT  sing N N 91  
ASP N   CA   sing N N 92  
ASP N   H    sing N N 93  
ASP N   H2   sing N N 94  
ASP CA  C    sing N N 95  
ASP CA  CB   sing N N 96  
ASP CA  HA   sing N N 97  
ASP C   O    doub N N 98  
ASP C   OXT  sing N N 99  
ASP CB  CG   sing N N 100 
ASP CB  HB2  sing N N 101 
ASP CB  HB3  sing N N 102 
ASP CG  OD1  doub N N 103 
ASP CG  OD2  sing N N 104 
ASP OD2 HD2  sing N N 105 
ASP OXT HXT  sing N N 106 
CYS N   CA   sing N N 107 
CYS N   H    sing N N 108 
CYS N   H2   sing N N 109 
CYS CA  C    sing N N 110 
CYS CA  CB   sing N N 111 
CYS CA  HA   sing N N 112 
CYS C   O    doub N N 113 
CYS C   OXT  sing N N 114 
CYS CB  SG   sing N N 115 
CYS CB  HB2  sing N N 116 
CYS CB  HB3  sing N N 117 
CYS SG  HG   sing N N 118 
CYS OXT HXT  sing N N 119 
FUC C1  C2   sing N N 120 
FUC C1  O1   sing N N 121 
FUC C1  O5   sing N N 122 
FUC C1  H1   sing N N 123 
FUC C2  C3   sing N N 124 
FUC C2  O2   sing N N 125 
FUC C2  H2   sing N N 126 
FUC C3  C4   sing N N 127 
FUC C3  O3   sing N N 128 
FUC C3  H3   sing N N 129 
FUC C4  C5   sing N N 130 
FUC C4  O4   sing N N 131 
FUC C4  H4   sing N N 132 
FUC C5  C6   sing N N 133 
FUC C5  O5   sing N N 134 
FUC C5  H5   sing N N 135 
FUC C6  H61  sing N N 136 
FUC C6  H62  sing N N 137 
FUC C6  H63  sing N N 138 
FUC O1  HO1  sing N N 139 
FUC O2  HO2  sing N N 140 
FUC O3  HO3  sing N N 141 
FUC O4  HO4  sing N N 142 
GLN N   CA   sing N N 143 
GLN N   H    sing N N 144 
GLN N   H2   sing N N 145 
GLN CA  C    sing N N 146 
GLN CA  CB   sing N N 147 
GLN CA  HA   sing N N 148 
GLN C   O    doub N N 149 
GLN C   OXT  sing N N 150 
GLN CB  CG   sing N N 151 
GLN CB  HB2  sing N N 152 
GLN CB  HB3  sing N N 153 
GLN CG  CD   sing N N 154 
GLN CG  HG2  sing N N 155 
GLN CG  HG3  sing N N 156 
GLN CD  OE1  doub N N 157 
GLN CD  NE2  sing N N 158 
GLN NE2 HE21 sing N N 159 
GLN NE2 HE22 sing N N 160 
GLN OXT HXT  sing N N 161 
GLU N   CA   sing N N 162 
GLU N   H    sing N N 163 
GLU N   H2   sing N N 164 
GLU CA  C    sing N N 165 
GLU CA  CB   sing N N 166 
GLU CA  HA   sing N N 167 
GLU C   O    doub N N 168 
GLU C   OXT  sing N N 169 
GLU CB  CG   sing N N 170 
GLU CB  HB2  sing N N 171 
GLU CB  HB3  sing N N 172 
GLU CG  CD   sing N N 173 
GLU CG  HG2  sing N N 174 
GLU CG  HG3  sing N N 175 
GLU CD  OE1  doub N N 176 
GLU CD  OE2  sing N N 177 
GLU OE2 HE2  sing N N 178 
GLU OXT HXT  sing N N 179 
GLY N   CA   sing N N 180 
GLY N   H    sing N N 181 
GLY N   H2   sing N N 182 
GLY CA  C    sing N N 183 
GLY CA  HA2  sing N N 184 
GLY CA  HA3  sing N N 185 
GLY C   O    doub N N 186 
GLY C   OXT  sing N N 187 
GLY OXT HXT  sing N N 188 
HIS N   CA   sing N N 189 
HIS N   H    sing N N 190 
HIS N   H2   sing N N 191 
HIS CA  C    sing N N 192 
HIS CA  CB   sing N N 193 
HIS CA  HA   sing N N 194 
HIS C   O    doub N N 195 
HIS C   OXT  sing N N 196 
HIS CB  CG   sing N N 197 
HIS CB  HB2  sing N N 198 
HIS CB  HB3  sing N N 199 
HIS CG  ND1  sing Y N 200 
HIS CG  CD2  doub Y N 201 
HIS ND1 CE1  doub Y N 202 
HIS ND1 HD1  sing N N 203 
HIS CD2 NE2  sing Y N 204 
HIS CD2 HD2  sing N N 205 
HIS CE1 NE2  sing Y N 206 
HIS CE1 HE1  sing N N 207 
HIS NE2 HE2  sing N N 208 
HIS OXT HXT  sing N N 209 
HOH O   H1   sing N N 210 
HOH O   H2   sing N N 211 
ILE N   CA   sing N N 212 
ILE N   H    sing N N 213 
ILE N   H2   sing N N 214 
ILE CA  C    sing N N 215 
ILE CA  CB   sing N N 216 
ILE CA  HA   sing N N 217 
ILE C   O    doub N N 218 
ILE C   OXT  sing N N 219 
ILE CB  CG1  sing N N 220 
ILE CB  CG2  sing N N 221 
ILE CB  HB   sing N N 222 
ILE CG1 CD1  sing N N 223 
ILE CG1 HG12 sing N N 224 
ILE CG1 HG13 sing N N 225 
ILE CG2 HG21 sing N N 226 
ILE CG2 HG22 sing N N 227 
ILE CG2 HG23 sing N N 228 
ILE CD1 HD11 sing N N 229 
ILE CD1 HD12 sing N N 230 
ILE CD1 HD13 sing N N 231 
ILE OXT HXT  sing N N 232 
LEU N   CA   sing N N 233 
LEU N   H    sing N N 234 
LEU N   H2   sing N N 235 
LEU CA  C    sing N N 236 
LEU CA  CB   sing N N 237 
LEU CA  HA   sing N N 238 
LEU C   O    doub N N 239 
LEU C   OXT  sing N N 240 
LEU CB  CG   sing N N 241 
LEU CB  HB2  sing N N 242 
LEU CB  HB3  sing N N 243 
LEU CG  CD1  sing N N 244 
LEU CG  CD2  sing N N 245 
LEU CG  HG   sing N N 246 
LEU CD1 HD11 sing N N 247 
LEU CD1 HD12 sing N N 248 
LEU CD1 HD13 sing N N 249 
LEU CD2 HD21 sing N N 250 
LEU CD2 HD22 sing N N 251 
LEU CD2 HD23 sing N N 252 
LEU OXT HXT  sing N N 253 
LYS N   CA   sing N N 254 
LYS N   H    sing N N 255 
LYS N   H2   sing N N 256 
LYS CA  C    sing N N 257 
LYS CA  CB   sing N N 258 
LYS CA  HA   sing N N 259 
LYS C   O    doub N N 260 
LYS C   OXT  sing N N 261 
LYS CB  CG   sing N N 262 
LYS CB  HB2  sing N N 263 
LYS CB  HB3  sing N N 264 
LYS CG  CD   sing N N 265 
LYS CG  HG2  sing N N 266 
LYS CG  HG3  sing N N 267 
LYS CD  CE   sing N N 268 
LYS CD  HD2  sing N N 269 
LYS CD  HD3  sing N N 270 
LYS CE  NZ   sing N N 271 
LYS CE  HE2  sing N N 272 
LYS CE  HE3  sing N N 273 
LYS NZ  HZ1  sing N N 274 
LYS NZ  HZ2  sing N N 275 
LYS NZ  HZ3  sing N N 276 
LYS OXT HXT  sing N N 277 
MET N   CA   sing N N 278 
MET N   H    sing N N 279 
MET N   H2   sing N N 280 
MET CA  C    sing N N 281 
MET CA  CB   sing N N 282 
MET CA  HA   sing N N 283 
MET C   O    doub N N 284 
MET C   OXT  sing N N 285 
MET CB  CG   sing N N 286 
MET CB  HB2  sing N N 287 
MET CB  HB3  sing N N 288 
MET CG  SD   sing N N 289 
MET CG  HG2  sing N N 290 
MET CG  HG3  sing N N 291 
MET SD  CE   sing N N 292 
MET CE  HE1  sing N N 293 
MET CE  HE2  sing N N 294 
MET CE  HE3  sing N N 295 
MET OXT HXT  sing N N 296 
NAG C1  C2   sing N N 297 
NAG C1  O1   sing N N 298 
NAG C1  O5   sing N N 299 
NAG C1  H1   sing N N 300 
NAG C2  C3   sing N N 301 
NAG C2  N2   sing N N 302 
NAG C2  H2   sing N N 303 
NAG C3  C4   sing N N 304 
NAG C3  O3   sing N N 305 
NAG C3  H3   sing N N 306 
NAG C4  C5   sing N N 307 
NAG C4  O4   sing N N 308 
NAG C4  H4   sing N N 309 
NAG C5  C6   sing N N 310 
NAG C5  O5   sing N N 311 
NAG C5  H5   sing N N 312 
NAG C6  O6   sing N N 313 
NAG C6  H61  sing N N 314 
NAG C6  H62  sing N N 315 
NAG C7  C8   sing N N 316 
NAG C7  N2   sing N N 317 
NAG C7  O7   doub N N 318 
NAG C8  H81  sing N N 319 
NAG C8  H82  sing N N 320 
NAG C8  H83  sing N N 321 
NAG N2  HN2  sing N N 322 
NAG O1  HO1  sing N N 323 
NAG O3  HO3  sing N N 324 
NAG O4  HO4  sing N N 325 
NAG O6  HO6  sing N N 326 
PEG C1  O1   sing N N 327 
PEG C1  C2   sing N N 328 
PEG C1  H11  sing N N 329 
PEG C1  H12  sing N N 330 
PEG O1  HO1  sing N N 331 
PEG C2  O2   sing N N 332 
PEG C2  H21  sing N N 333 
PEG C2  H22  sing N N 334 
PEG O2  C3   sing N N 335 
PEG C3  C4   sing N N 336 
PEG C3  H31  sing N N 337 
PEG C3  H32  sing N N 338 
PEG C4  O4   sing N N 339 
PEG C4  H41  sing N N 340 
PEG C4  H42  sing N N 341 
PEG O4  HO4  sing N N 342 
PHE N   CA   sing N N 343 
PHE N   H    sing N N 344 
PHE N   H2   sing N N 345 
PHE CA  C    sing N N 346 
PHE CA  CB   sing N N 347 
PHE CA  HA   sing N N 348 
PHE C   O    doub N N 349 
PHE C   OXT  sing N N 350 
PHE CB  CG   sing N N 351 
PHE CB  HB2  sing N N 352 
PHE CB  HB3  sing N N 353 
PHE CG  CD1  doub Y N 354 
PHE CG  CD2  sing Y N 355 
PHE CD1 CE1  sing Y N 356 
PHE CD1 HD1  sing N N 357 
PHE CD2 CE2  doub Y N 358 
PHE CD2 HD2  sing N N 359 
PHE CE1 CZ   doub Y N 360 
PHE CE1 HE1  sing N N 361 
PHE CE2 CZ   sing Y N 362 
PHE CE2 HE2  sing N N 363 
PHE CZ  HZ   sing N N 364 
PHE OXT HXT  sing N N 365 
PRO N   CA   sing N N 366 
PRO N   CD   sing N N 367 
PRO N   H    sing N N 368 
PRO CA  C    sing N N 369 
PRO CA  CB   sing N N 370 
PRO CA  HA   sing N N 371 
PRO C   O    doub N N 372 
PRO C   OXT  sing N N 373 
PRO CB  CG   sing N N 374 
PRO CB  HB2  sing N N 375 
PRO CB  HB3  sing N N 376 
PRO CG  CD   sing N N 377 
PRO CG  HG2  sing N N 378 
PRO CG  HG3  sing N N 379 
PRO CD  HD2  sing N N 380 
PRO CD  HD3  sing N N 381 
PRO OXT HXT  sing N N 382 
SER N   CA   sing N N 383 
SER N   H    sing N N 384 
SER N   H2   sing N N 385 
SER CA  C    sing N N 386 
SER CA  CB   sing N N 387 
SER CA  HA   sing N N 388 
SER C   O    doub N N 389 
SER C   OXT  sing N N 390 
SER CB  OG   sing N N 391 
SER CB  HB2  sing N N 392 
SER CB  HB3  sing N N 393 
SER OG  HG   sing N N 394 
SER OXT HXT  sing N N 395 
THR N   CA   sing N N 396 
THR N   H    sing N N 397 
THR N   H2   sing N N 398 
THR CA  C    sing N N 399 
THR CA  CB   sing N N 400 
THR CA  HA   sing N N 401 
THR C   O    doub N N 402 
THR C   OXT  sing N N 403 
THR CB  OG1  sing N N 404 
THR CB  CG2  sing N N 405 
THR CB  HB   sing N N 406 
THR OG1 HG1  sing N N 407 
THR CG2 HG21 sing N N 408 
THR CG2 HG22 sing N N 409 
THR CG2 HG23 sing N N 410 
THR OXT HXT  sing N N 411 
TRP N   CA   sing N N 412 
TRP N   H    sing N N 413 
TRP N   H2   sing N N 414 
TRP CA  C    sing N N 415 
TRP CA  CB   sing N N 416 
TRP CA  HA   sing N N 417 
TRP C   O    doub N N 418 
TRP C   OXT  sing N N 419 
TRP CB  CG   sing N N 420 
TRP CB  HB2  sing N N 421 
TRP CB  HB3  sing N N 422 
TRP CG  CD1  doub Y N 423 
TRP CG  CD2  sing Y N 424 
TRP CD1 NE1  sing Y N 425 
TRP CD1 HD1  sing N N 426 
TRP CD2 CE2  doub Y N 427 
TRP CD2 CE3  sing Y N 428 
TRP NE1 CE2  sing Y N 429 
TRP NE1 HE1  sing N N 430 
TRP CE2 CZ2  sing Y N 431 
TRP CE3 CZ3  doub Y N 432 
TRP CE3 HE3  sing N N 433 
TRP CZ2 CH2  doub Y N 434 
TRP CZ2 HZ2  sing N N 435 
TRP CZ3 CH2  sing Y N 436 
TRP CZ3 HZ3  sing N N 437 
TRP CH2 HH2  sing N N 438 
TRP OXT HXT  sing N N 439 
TYR N   CA   sing N N 440 
TYR N   H    sing N N 441 
TYR N   H2   sing N N 442 
TYR CA  C    sing N N 443 
TYR CA  CB   sing N N 444 
TYR CA  HA   sing N N 445 
TYR C   O    doub N N 446 
TYR C   OXT  sing N N 447 
TYR CB  CG   sing N N 448 
TYR CB  HB2  sing N N 449 
TYR CB  HB3  sing N N 450 
TYR CG  CD1  doub Y N 451 
TYR CG  CD2  sing Y N 452 
TYR CD1 CE1  sing Y N 453 
TYR CD1 HD1  sing N N 454 
TYR CD2 CE2  doub Y N 455 
TYR CD2 HD2  sing N N 456 
TYR CE1 CZ   doub Y N 457 
TYR CE1 HE1  sing N N 458 
TYR CE2 CZ   sing Y N 459 
TYR CE2 HE2  sing N N 460 
TYR CZ  OH   sing N N 461 
TYR OH  HH   sing N N 462 
TYR OXT HXT  sing N N 463 
VAL N   CA   sing N N 464 
VAL N   H    sing N N 465 
VAL N   H2   sing N N 466 
VAL CA  C    sing N N 467 
VAL CA  CB   sing N N 468 
VAL CA  HA   sing N N 469 
VAL C   O    doub N N 470 
VAL C   OXT  sing N N 471 
VAL CB  CG1  sing N N 472 
VAL CB  CG2  sing N N 473 
VAL CB  HB   sing N N 474 
VAL CG1 HG11 sing N N 475 
VAL CG1 HG12 sing N N 476 
VAL CG1 HG13 sing N N 477 
VAL CG2 HG21 sing N N 478 
VAL CG2 HG22 sing N N 479 
VAL CG2 HG23 sing N N 480 
VAL OXT HXT  sing N N 481 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R00HD104924 
_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   5B5K 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9MYM 
_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]   0.009666 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009666 
_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]   0.007179 
_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  
CA 
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . CYS A 1 1   ? -29.730 -39.830 -32.516 1.00 26.54  ? 22   CYS A N   1 
ATOM   2    C  CA  . CYS A 1 1   ? -28.832 -38.662 -32.595 1.00 28.37  ? 22   CYS A CA  1 
ATOM   3    C  C   . CYS A 1 1   ? -28.658 -38.195 -34.051 1.00 26.61  ? 22   CYS A C   1 
ATOM   4    O  O   . CYS A 1 1   ? -28.093 -37.145 -34.289 1.00 26.38  ? 22   CYS A O   1 
ATOM   5    C  CB  . CYS A 1 1   ? -27.421 -38.957 -31.955 1.00 27.58  ? 22   CYS A CB  1 
ATOM   6    S  SG  . CYS A 1 1   ? -27.320 -38.732 -30.200 1.00 34.32  ? 22   CYS A SG  1 
ATOM   7    N  N   . ILE A 1 2   ? -29.102 -38.977 -35.035 1.00 22.50  ? 23   ILE A N   1 
ATOM   8    C  CA  . ILE A 1 2   ? -28.727 -38.648 -36.415 1.00 21.33  ? 23   ILE A CA  1 
ATOM   9    C  C   . ILE A 1 2   ? -29.399 -37.320 -36.870 1.00 23.57  ? 23   ILE A C   1 
ATOM   10   O  O   . ILE A 1 2   ? -28.871 -36.682 -37.769 1.00 26.09  ? 23   ILE A O   1 
ATOM   11   C  CB  . ILE A 1 2   ? -29.105 -39.753 -37.427 1.00 23.36  ? 23   ILE A CB  1 
ATOM   12   C  CG1 . ILE A 1 2   ? -30.608 -40.092 -37.313 1.00 24.44  ? 23   ILE A CG1 1 
ATOM   13   C  CG2 . ILE A 1 2   ? -28.215 -40.993 -37.202 1.00 24.18  ? 23   ILE A CG2 1 
ATOM   14   C  CD1 . ILE A 1 2   ? -31.110 -40.974 -38.464 1.00 24.42  ? 23   ILE A CD1 1 
ATOM   15   N  N   . LYS A 1 3   ? -30.503 -36.921 -36.238 1.00 24.13  ? 24   LYS A N   1 
ATOM   16   C  CA  . LYS A 1 3   ? -31.134 -35.605 -36.584 1.00 21.92  ? 24   LYS A CA  1 
ATOM   17   C  C   . LYS A 1 3   ? -30.196 -34.456 -36.260 1.00 27.09  ? 24   LYS A C   1 
ATOM   18   O  O   . LYS A 1 3   ? -30.396 -33.339 -36.746 1.00 26.73  ? 24   LYS A O   1 
ATOM   19   C  CB  . LYS A 1 3   ? -32.445 -35.388 -35.849 1.00 24.31  ? 24   LYS A CB  1 
ATOM   20   C  CG  . LYS A 1 3   ? -32.250 -35.129 -34.341 1.00 23.91  ? 24   LYS A CG  1 
ATOM   21   C  CD  . LYS A 1 3   ? -33.559 -35.084 -33.553 1.00 28.81  ? 24   LYS A CD  1 
ATOM   22   C  CE  . LYS A 1 3   ? -33.263 -34.623 -32.129 1.00 31.08  ? 24   LYS A CE  1 
ATOM   23   N  NZ  . LYS A 1 3   ? -34.455 -34.832 -31.190 1.00 34.51  ? 24   LYS A NZ  1 
ATOM   24   N  N   . CYS A 1 4   ? -29.197 -34.724 -35.414 1.00 24.77  ? 25   CYS A N   1 
ATOM   25   C  CA  . CYS A 1 4   ? -28.239 -33.689 -34.977 1.00 27.26  ? 25   CYS A CA  1 
ATOM   26   C  C   . CYS A 1 4   ? -27.177 -33.456 -36.015 1.00 31.46  ? 25   CYS A C   1 
ATOM   27   O  O   . CYS A 1 4   ? -26.357 -32.544 -35.874 1.00 30.54  ? 25   CYS A O   1 
ATOM   28   C  CB  . CYS A 1 4   ? -27.524 -34.089 -33.674 1.00 31.19  ? 25   CYS A CB  1 
ATOM   29   S  SG  . CYS A 1 4   ? -28.690 -34.598 -32.331 1.00 29.65  ? 25   CYS A SG  1 
ATOM   30   N  N   . ASP A 1 5   ? -27.142 -34.278 -37.050 1.00 26.16  ? 26   ASP A N   1 
ATOM   31   C  CA  . ASP A 1 5   ? -25.997 -34.255 -37.946 1.00 22.90  ? 26   ASP A CA  1 
ATOM   32   C  C   . ASP A 1 5   ? -26.376 -33.478 -39.231 1.00 26.43  ? 26   ASP A C   1 
ATOM   33   O  O   . ASP A 1 5   ? -27.359 -33.823 -39.895 1.00 24.48  ? 26   ASP A O   1 
ATOM   34   C  CB  . ASP A 1 5   ? -25.588 -35.694 -38.293 1.00 25.91  ? 26   ASP A CB  1 
ATOM   35   C  CG  . ASP A 1 5   ? -24.278 -35.774 -39.024 1.00 30.94  ? 26   ASP A CG  1 
ATOM   36   O  OD1 . ASP A 1 5   ? -23.998 -34.954 -39.954 1.00 28.83  ? 26   ASP A OD1 1 
ATOM   37   O  OD2 . ASP A 1 5   ? -23.558 -36.735 -38.694 1.00 32.76  ? 26   ASP A OD2 1 
ATOM   38   N  N   . GLN A 1 6   ? -25.618 -32.455 -39.576 1.00 27.67  ? 27   GLN A N   1 
ATOM   39   C  CA  . GLN A 1 6   ? -25.918 -31.677 -40.793 1.00 29.00  ? 27   GLN A CA  1 
ATOM   40   C  C   . GLN A 1 6   ? -26.092 -32.545 -42.060 1.00 25.24  ? 27   GLN A C   1 
ATOM   41   O  O   . GLN A 1 6   ? -26.884 -32.221 -42.961 1.00 26.43  ? 27   GLN A O   1 
ATOM   42   C  CB  . GLN A 1 6   ? -24.798 -30.652 -41.063 1.00 28.20  ? 27   GLN A CB  1 
ATOM   43   C  CG  . GLN A 1 6   ? -25.308 -29.629 -42.077 1.00 36.11  ? 27   GLN A CG  1 
ATOM   44   C  CD  . GLN A 1 6   ? -24.277 -28.698 -42.550 1.00 41.21  ? 27   GLN A CD  1 
ATOM   45   O  OE1 . GLN A 1 6   ? -23.386 -28.237 -41.777 1.00 30.06  ? 27   GLN A OE1 1 
ATOM   46   N  NE2 . GLN A 1 6   ? -24.392 -28.338 -43.838 1.00 47.30  ? 27   GLN A NE2 1 
ATOM   47   N  N   . PHE A 1 7   ? -25.322 -33.625 -42.156 1.00 22.02  ? 28   PHE A N   1 
ATOM   48   C  CA  . PHE A 1 7   ? -25.410 -34.447 -43.385 1.00 22.57  ? 28   PHE A CA  1 
ATOM   49   C  C   . PHE A 1 7   ? -26.798 -35.078 -43.526 1.00 25.13  ? 28   PHE A C   1 
ATOM   50   O  O   . PHE A 1 7   ? -27.320 -35.244 -44.636 1.00 23.97  ? 28   PHE A O   1 
ATOM   51   C  CB  . PHE A 1 7   ? -24.379 -35.590 -43.370 1.00 22.10  ? 28   PHE A CB  1 
ATOM   52   C  CG  . PHE A 1 7   ? -22.963 -35.161 -43.711 1.00 22.91  ? 28   PHE A CG  1 
ATOM   53   C  CD1 . PHE A 1 7   ? -22.723 -34.061 -44.547 1.00 32.45  ? 28   PHE A CD1 1 
ATOM   54   C  CD2 . PHE A 1 7   ? -21.876 -35.876 -43.224 1.00 23.64  ? 28   PHE A CD2 1 
ATOM   55   C  CE1 . PHE A 1 7   ? -21.411 -33.650 -44.842 1.00 30.00  ? 28   PHE A CE1 1 
ATOM   56   C  CE2 . PHE A 1 7   ? -20.544 -35.477 -43.550 1.00 25.95  ? 28   PHE A CE2 1 
ATOM   57   C  CZ  . PHE A 1 7   ? -20.336 -34.384 -44.379 1.00 27.03  ? 28   PHE A CZ  1 
ATOM   58   N  N   . VAL A 1 8   ? -27.361 -35.453 -42.383 1.00 25.80  ? 29   VAL A N   1 
ATOM   59   C  CA  . VAL A 1 8   ? -28.680 -36.068 -42.353 1.00 23.74  ? 29   VAL A CA  1 
ATOM   60   C  C   . VAL A 1 8   ? -29.751 -35.061 -42.700 1.00 26.08  ? 29   VAL A C   1 
ATOM   61   O  O   . VAL A 1 8   ? -30.605 -35.306 -43.568 1.00 25.74  ? 29   VAL A O   1 
ATOM   62   C  CB  . VAL A 1 8   ? -28.943 -36.694 -41.000 1.00 25.64  ? 29   VAL A CB  1 
ATOM   63   C  CG1 . VAL A 1 8   ? -30.440 -37.141 -40.873 1.00 28.68  ? 29   VAL A CG1 1 
ATOM   64   C  CG2 . VAL A 1 8   ? -28.001 -37.896 -40.836 1.00 26.19  ? 29   VAL A CG2 1 
ATOM   65   N  N   . THR A 1 9   ? -29.678 -33.887 -42.091 1.00 23.84  ? 30   THR A N   1 
ATOM   66   C  CA  . THR A 1 9   ? -30.724 -32.929 -42.410 1.00 28.86  ? 30   THR A CA  1 
ATOM   67   C  C   . THR A 1 9   ? -30.569 -32.390 -43.873 1.00 26.55  ? 30   THR A C   1 
ATOM   68   O  O   . THR A 1 9   ? -31.589 -32.153 -44.553 1.00 27.29  ? 30   THR A O   1 
ATOM   69   C  CB  . THR A 1 9   ? -30.771 -31.789 -41.366 1.00 35.94  ? 30   THR A CB  1 
ATOM   70   O  OG1 . THR A 1 9   ? -29.519 -31.164 -41.290 1.00 34.85  ? 30   THR A OG1 1 
ATOM   71   C  CG2 . THR A 1 9   ? -31.077 -32.379 -39.982 1.00 42.80  ? 30   THR A CG2 1 
ATOM   72   N  N   . ASP A 1 10  ? -29.344 -32.275 -44.398 1.00 23.57  ? 31   ASP A N   1 
ATOM   73   C  CA  . ASP A 1 10  ? -29.148 -31.927 -45.812 1.00 25.09  ? 31   ASP A CA  1 
ATOM   74   C  C   . ASP A 1 10  ? -29.730 -33.015 -46.745 1.00 28.00  ? 31   ASP A C   1 
ATOM   75   O  O   . ASP A 1 10  ? -30.437 -32.729 -47.737 1.00 27.80  ? 31   ASP A O   1 
ATOM   76   C  CB  . ASP A 1 10  ? -27.680 -31.780 -46.151 1.00 25.93  ? 31   ASP A CB  1 
ATOM   77   C  CG  . ASP A 1 10  ? -27.044 -30.499 -45.606 1.00 38.56  ? 31   ASP A CG  1 
ATOM   78   O  OD1 . ASP A 1 10  ? -27.718 -29.560 -45.163 1.00 34.08  ? 31   ASP A OD1 1 
ATOM   79   O  OD2 . ASP A 1 10  ? -25.817 -30.455 -45.627 1.00 39.09  ? 31   ASP A OD2 1 
ATOM   80   N  N   . ALA A 1 11  ? -29.405 -34.260 -46.443 1.00 24.36  ? 32   ALA A N   1 
ATOM   81   C  CA  . ALA A 1 11  ? -29.939 -35.411 -47.206 1.00 24.99  ? 32   ALA A CA  1 
ATOM   82   C  C   . ALA A 1 11  ? -31.435 -35.496 -47.193 1.00 28.26  ? 32   ALA A C   1 
ATOM   83   O  O   . ALA A 1 11  ? -32.030 -35.887 -48.218 1.00 22.35  ? 32   ALA A O   1 
ATOM   84   C  CB  . ALA A 1 11  ? -29.381 -36.758 -46.638 1.00 26.40  ? 32   ALA A CB  1 
ATOM   85   N  N   . LEU A 1 12  ? -32.065 -35.200 -46.044 1.00 22.31  ? 33   LEU A N   1 
ATOM   86   C  CA  . LEU A 1 12  ? -33.534 -35.261 -46.009 1.00 23.76  ? 33   LEU A CA  1 
ATOM   87   C  C   . LEU A 1 12  ? -34.166 -34.137 -46.830 1.00 23.77  ? 33   LEU A C   1 
ATOM   88   O  O   . LEU A 1 12  ? -35.260 -34.331 -47.350 1.00 24.68  ? 33   LEU A O   1 
ATOM   89   C  CB  . LEU A 1 12  ? -34.071 -35.205 -44.578 1.00 25.10  ? 33   LEU A CB  1 
ATOM   90   C  CG  . LEU A 1 12  ? -33.819 -36.487 -43.751 1.00 28.06  ? 33   LEU A CG  1 
ATOM   91   C  CD1 . LEU A 1 12  ? -34.232 -36.279 -42.264 1.00 32.54  ? 33   LEU A CD1 1 
ATOM   92   C  CD2 . LEU A 1 12  ? -34.489 -37.714 -44.329 1.00 28.37  ? 33   LEU A CD2 1 
ATOM   93   N  N   . LYS A 1 13  ? -33.505 -32.972 -46.909 1.00 26.61  ? 34   LYS A N   1 
ATOM   94   C  CA  . LYS A 1 13  ? -33.992 -31.877 -47.729 1.00 27.88  ? 34   LYS A CA  1 
ATOM   95   C  C   . LYS A 1 13  ? -33.950 -32.257 -49.213 1.00 25.92  ? 34   LYS A C   1 
ATOM   96   O  O   . LYS A 1 13  ? -34.894 -32.007 -49.943 1.00 28.22  ? 34   LYS A O   1 
ATOM   97   C  CB  . LYS A 1 13  ? -33.173 -30.617 -47.495 1.00 33.53  ? 34   LYS A CB  1 
ATOM   98   C  CG  . LYS A 1 13  ? -33.516 -29.956 -46.180 1.00 47.05  ? 34   LYS A CG  1 
ATOM   99   N  N   . THR A 1 14  ? -32.832 -32.852 -49.639 1.00 24.12  ? 35   THR A N   1 
ATOM   100  C  CA  . THR A 1 14  ? -32.688 -33.320 -51.000 1.00 27.94  ? 35   THR A CA  1 
ATOM   101  C  C   . THR A 1 14  ? -33.682 -34.432 -51.314 1.00 23.00  ? 35   THR A C   1 
ATOM   102  O  O   . THR A 1 14  ? -34.268 -34.463 -52.367 1.00 28.77  ? 35   THR A O   1 
ATOM   103  C  CB  . THR A 1 14  ? -31.266 -33.833 -51.225 1.00 29.84  ? 35   THR A CB  1 
ATOM   104  O  OG1 . THR A 1 14  ? -30.384 -32.712 -51.000 1.00 31.25  ? 35   THR A OG1 1 
ATOM   105  C  CG2 . THR A 1 14  ? -31.136 -34.254 -52.657 1.00 32.19  ? 35   THR A CG2 1 
ATOM   106  N  N   . PHE A 1 15  ? -33.875 -35.325 -50.346 1.00 21.22  ? 36   PHE A N   1 
ATOM   107  C  CA  . PHE A 1 15  ? -34.852 -36.410 -50.468 1.00 25.99  ? 36   PHE A CA  1 
ATOM   108  C  C   . PHE A 1 15  ? -36.227 -35.826 -50.799 1.00 26.79  ? 36   PHE A C   1 
ATOM   109  O  O   . PHE A 1 15  ? -36.875 -36.240 -51.747 1.00 25.43  ? 36   PHE A O   1 
ATOM   110  C  CB  . PHE A 1 15  ? -34.903 -37.189 -49.157 1.00 24.59  ? 36   PHE A CB  1 
ATOM   111  C  CG  . PHE A 1 15  ? -35.842 -38.376 -49.169 1.00 23.38  ? 36   PHE A CG  1 
ATOM   112  C  CD1 . PHE A 1 15  ? -35.450 -39.574 -49.749 1.00 23.79  ? 36   PHE A CD1 1 
ATOM   113  C  CD2 . PHE A 1 15  ? -37.088 -38.280 -48.560 1.00 29.50  ? 36   PHE A CD2 1 
ATOM   114  C  CE1 . PHE A 1 15  ? -36.339 -40.705 -49.711 1.00 30.97  ? 36   PHE A CE1 1 
ATOM   115  C  CE2 . PHE A 1 15  ? -37.965 -39.365 -48.518 1.00 24.72  ? 36   PHE A CE2 1 
ATOM   116  C  CZ  . PHE A 1 15  ? -37.592 -40.585 -49.078 1.00 23.90  ? 36   PHE A CZ  1 
ATOM   117  N  N   . GLU A 1 16  ? -36.664 -34.873 -49.992 1.00 25.23  ? 37   GLU A N   1 
ATOM   118  C  CA  . GLU A 1 16  ? -37.970 -34.245 -50.216 1.00 27.04  ? 37   GLU A CA  1 
ATOM   119  C  C   . GLU A 1 16  ? -38.044 -33.441 -51.500 1.00 28.27  ? 37   GLU A C   1 
ATOM   120  O  O   . GLU A 1 16  ? -39.018 -33.561 -52.233 1.00 30.06  ? 37   GLU A O   1 
ATOM   121  C  CB  . GLU A 1 16  ? -38.318 -33.311 -49.058 1.00 29.51  ? 37   GLU A CB  1 
ATOM   122  C  CG  . GLU A 1 16  ? -39.700 -32.695 -49.226 1.00 33.86  ? 37   GLU A CG  1 
ATOM   123  C  CD  . GLU A 1 16  ? -40.132 -31.910 -48.013 1.00 37.69  ? 37   GLU A CD  1 
ATOM   124  O  OE1 . GLU A 1 16  ? -39.390 -31.919 -47.009 1.00 37.31  ? 37   GLU A OE1 1 
ATOM   125  O  OE2 . GLU A 1 16  ? -41.241 -31.319 -48.058 1.00 38.57  ? 37   GLU A OE2 1 
ATOM   126  N  N   A ASN A 1 17  ? -37.039 -32.625 -51.778 0.58 25.00  ? 38   ASN A N   1 
ATOM   127  N  N   B ASN A 1 17  ? -37.032 -32.600 -51.762 0.42 25.88  ? 38   ASN A N   1 
ATOM   128  C  CA  A ASN A 1 17  ? -37.201 -31.645 -52.846 0.58 30.71  ? 38   ASN A CA  1 
ATOM   129  C  CA  B ASN A 1 17  ? -37.156 -31.586 -52.828 0.42 30.62  ? 38   ASN A CA  1 
ATOM   130  C  C   A ASN A 1 17  ? -36.889 -32.218 -54.203 0.58 32.43  ? 38   ASN A C   1 
ATOM   131  C  C   B ASN A 1 17  ? -36.653 -32.056 -54.184 0.42 32.03  ? 38   ASN A C   1 
ATOM   132  O  O   A ASN A 1 17  ? -37.402 -31.745 -55.213 0.58 27.12  ? 38   ASN A O   1 
ATOM   133  O  O   B ASN A 1 17  ? -36.837 -31.361 -55.191 0.42 28.93  ? 38   ASN A O   1 
ATOM   134  C  CB  A ASN A 1 17  ? -36.336 -30.401 -52.584 0.58 31.99  ? 38   ASN A CB  1 
ATOM   135  C  CB  B ASN A 1 17  ? -36.480 -30.221 -52.430 0.42 32.70  ? 38   ASN A CB  1 
ATOM   136  C  CG  A ASN A 1 17  ? -36.825 -29.611 -51.385 0.58 35.78  ? 38   ASN A CG  1 
ATOM   137  C  CG  B ASN A 1 17  ? -34.912 -30.213 -52.475 0.42 35.26  ? 38   ASN A CG  1 
ATOM   138  O  OD1 A ASN A 1 17  ? -37.971 -29.767 -50.986 0.58 38.92  ? 38   ASN A OD1 1 
ATOM   139  O  OD1 B ASN A 1 17  ? -34.270 -31.087 -53.042 0.42 30.18  ? 38   ASN A OD1 1 
ATOM   140  N  ND2 A ASN A 1 17  ? -35.960 -28.772 -50.801 0.58 36.49  ? 38   ASN A ND2 1 
ATOM   141  N  ND2 B ASN A 1 17  ? -34.312 -29.149 -51.889 0.42 34.87  ? 38   ASN A ND2 1 
ATOM   142  N  N   . THR A 1 18  ? -36.039 -33.237 -54.225 1.00 28.80  ? 39   THR A N   1 
ATOM   143  C  CA  . THR A 1 18  ? -35.551 -33.774 -55.511 1.00 29.80  ? 39   THR A CA  1 
ATOM   144  C  C   . THR A 1 18  ? -36.022 -35.181 -55.733 1.00 30.69  ? 39   THR A C   1 
ATOM   145  O  O   . THR A 1 18  ? -36.553 -35.471 -56.776 1.00 33.03  ? 39   THR A O   1 
ATOM   146  C  CB  . THR A 1 18  ? -34.008 -33.762 -55.571 1.00 32.68  ? 39   THR A CB  1 
ATOM   147  O  OG1 . THR A 1 18  ? -33.570 -32.410 -55.535 1.00 33.76  ? 39   THR A OG1 1 
ATOM   148  C  CG2 . THR A 1 18  ? -33.459 -34.407 -56.854 1.00 37.85  ? 39   THR A CG2 1 
ATOM   149  N  N   . TYR A 1 19  ? -35.868 -36.061 -54.742 1.00 25.51  ? 40   TYR A N   1 
ATOM   150  C  CA  . TYR A 1 19  ? -36.072 -37.492 -55.087 1.00 25.05  ? 40   TYR A CA  1 
ATOM   151  C  C   . TYR A 1 19  ? -37.492 -38.019 -54.946 1.00 26.85  ? 40   TYR A C   1 
ATOM   152  O  O   . TYR A 1 19  ? -37.877 -38.970 -55.636 1.00 25.86  ? 40   TYR A O   1 
ATOM   153  C  CB  . TYR A 1 19  ? -35.123 -38.347 -54.247 1.00 25.71  ? 40   TYR A CB  1 
ATOM   154  C  CG  . TYR A 1 19  ? -33.665 -38.067 -54.604 1.00 27.03  ? 40   TYR A CG  1 
ATOM   155  C  CD1 . TYR A 1 19  ? -33.237 -38.078 -55.906 1.00 36.66  ? 40   TYR A CD1 1 
ATOM   156  C  CD2 . TYR A 1 19  ? -32.721 -37.772 -53.607 1.00 32.67  ? 40   TYR A CD2 1 
ATOM   157  C  CE1 . TYR A 1 19  ? -31.908 -37.815 -56.229 1.00 36.18  ? 40   TYR A CE1 1 
ATOM   158  C  CE2 . TYR A 1 19  ? -31.397 -37.533 -53.935 1.00 33.21  ? 40   TYR A CE2 1 
ATOM   159  C  CZ  . TYR A 1 19  ? -31.015 -37.542 -55.240 1.00 38.02  ? 40   TYR A CZ  1 
ATOM   160  O  OH  . TYR A 1 19  ? -29.689 -37.290 -55.570 1.00 38.33  ? 40   TYR A OH  1 
ATOM   161  N  N   . LEU A 1 20  ? -38.281 -37.468 -54.038 1.00 25.31  ? 41   LEU A N   1 
ATOM   162  C  CA  . LEU A 1 20  ? -39.653 -38.008 -53.888 1.00 23.89  ? 41   LEU A CA  1 
ATOM   163  C  C   . LEU A 1 20  ? -40.442 -37.922 -55.186 1.00 26.35  ? 41   LEU A C   1 
ATOM   164  O  O   . LEU A 1 20  ? -41.250 -38.791 -55.438 1.00 25.28  ? 41   LEU A O   1 
ATOM   165  C  CB  . LEU A 1 20  ? -40.435 -37.279 -52.768 1.00 24.18  ? 41   LEU A CB  1 
ATOM   166  C  CG  . LEU A 1 20  ? -40.158 -37.727 -51.336 1.00 28.76  ? 41   LEU A CG  1 
ATOM   167  C  CD1 . LEU A 1 20  ? -41.061 -36.860 -50.385 1.00 22.97  ? 41   LEU A CD1 1 
ATOM   168  C  CD2 . LEU A 1 20  ? -40.320 -39.252 -51.158 1.00 26.21  ? 41   LEU A CD2 1 
ATOM   169  N  N   . ASN A 1 21  ? -40.191 -36.883 -55.982 1.00 23.13  ? 42   ASN A N   1 
ATOM   170  C  CA  . ASN A 1 21  ? -40.825 -36.702 -57.314 1.00 23.46  ? 42   ASN A CA  1 
ATOM   171  C  C   . ASN A 1 21  ? -40.747 -37.968 -58.164 1.00 32.06  ? 42   ASN A C   1 
ATOM   172  O  O   . ASN A 1 21  ? -41.634 -38.246 -58.980 1.00 28.42  ? 42   ASN A O   1 
ATOM   173  C  CB  . ASN A 1 21  ? -40.118 -35.565 -58.092 1.00 31.04  ? 42   ASN A CB  1 
ATOM   174  C  CG  . ASN A 1 21  ? -40.608 -34.184 -57.681 1.00 51.04  ? 42   ASN A CG  1 
ATOM   175  O  OD1 . ASN A 1 21  ? -41.730 -34.049 -57.208 1.00 57.55  ? 42   ASN A OD1 1 
ATOM   176  N  ND2 . ASN A 1 21  ? -39.753 -33.140 -57.854 1.00 56.12  ? 42   ASN A ND2 1 
ATOM   177  N  N   . ASP A 1 22  ? -39.644 -38.707 -57.985 1.00 27.36  ? 43   ASP A N   1 
ATOM   178  C  CA  . ASP A 1 22  ? -39.366 -39.881 -58.818 1.00 30.80  ? 43   ASP A CA  1 
ATOM   179  C  C   . ASP A 1 22  ? -40.122 -41.136 -58.389 1.00 28.94  ? 43   ASP A C   1 
ATOM   180  O  O   . ASP A 1 22  ? -40.148 -42.112 -59.156 1.00 29.31  ? 43   ASP A O   1 
ATOM   181  C  CB  . ASP A 1 22  ? -37.877 -40.237 -58.802 1.00 24.73  ? 43   ASP A CB  1 
ATOM   182  C  CG  . ASP A 1 22  ? -37.015 -39.111 -59.303 1.00 36.24  ? 43   ASP A CG  1 
ATOM   183  O  OD1 . ASP A 1 22  ? -37.457 -38.376 -60.190 1.00 37.49  ? 43   ASP A OD1 1 
ATOM   184  O  OD2 . ASP A 1 22  ? -35.911 -38.955 -58.798 1.00 36.32  ? 43   ASP A OD2 1 
ATOM   185  N  N   . HIS A 1 23  ? -40.723 -41.102 -57.197 1.00 24.54  ? 44   HIS A N   1 
ATOM   186  C  CA  . HIS A 1 23  ? -41.253 -42.309 -56.565 1.00 25.74  ? 44   HIS A CA  1 
ATOM   187  C  C   . HIS A 1 23  ? -42.707 -42.226 -56.151 1.00 23.00  ? 44   HIS A C   1 
ATOM   188  O  O   . HIS A 1 23  ? -43.365 -43.237 -55.961 1.00 26.05  ? 44   HIS A O   1 
ATOM   189  C  CB  . HIS A 1 23  ? -40.407 -42.648 -55.335 1.00 22.45  ? 44   HIS A CB  1 
ATOM   190  C  CG  . HIS A 1 23  ? -38.966 -42.939 -55.654 1.00 25.54  ? 44   HIS A CG  1 
ATOM   191  N  ND1 . HIS A 1 23  ? -38.523 -44.192 -56.047 1.00 26.03  ? 44   HIS A ND1 1 
ATOM   192  C  CD2 . HIS A 1 23  ? -37.861 -42.141 -55.610 1.00 23.39  ? 44   HIS A CD2 1 
ATOM   193  C  CE1 . HIS A 1 23  ? -37.214 -44.150 -56.243 1.00 29.60  ? 44   HIS A CE1 1 
ATOM   194  N  NE2 . HIS A 1 23  ? -36.784 -42.924 -55.975 1.00 29.33  ? 44   HIS A NE2 1 
ATOM   195  N  N   . LEU A 1 24  ? -43.192 -41.009 -55.974 1.00 25.02  ? 45   LEU A N   1 
ATOM   196  C  CA  . LEU A 1 24  ? -44.507 -40.789 -55.376 1.00 21.29  ? 45   LEU A CA  1 
ATOM   197  C  C   . LEU A 1 24  ? -45.230 -39.595 -56.010 1.00 21.69  ? 45   LEU A C   1 
ATOM   198  O  O   . LEU A 1 24  ? -44.586 -38.573 -56.394 1.00 25.95  ? 45   LEU A O   1 
ATOM   199  C  CB  . LEU A 1 24  ? -44.326 -40.513 -53.873 1.00 22.82  ? 45   LEU A CB  1 
ATOM   200  C  CG  . LEU A 1 24  ? -44.626 -41.538 -52.800 1.00 38.22  ? 45   LEU A CG  1 
ATOM   201  C  CD1 . LEU A 1 24  ? -44.782 -42.948 -53.174 1.00 30.13  ? 45   LEU A CD1 1 
ATOM   202  C  CD2 . LEU A 1 24  ? -43.823 -41.312 -51.486 1.00 23.85  ? 45   LEU A CD2 1 
ATOM   203  N  N   . PRO A 1 25  ? -46.577 -39.658 -56.052 1.00 24.80  ? 46   PRO A N   1 
ATOM   204  C  CA  . PRO A 1 25  ? -47.332 -38.488 -56.525 1.00 25.86  ? 46   PRO A CA  1 
ATOM   205  C  C   . PRO A 1 25  ? -47.136 -37.336 -55.511 1.00 25.41  ? 46   PRO A C   1 
ATOM   206  O  O   . PRO A 1 25  ? -47.046 -37.616 -54.303 1.00 24.70  ? 46   PRO A O   1 
ATOM   207  C  CB  . PRO A 1 25  ? -48.796 -38.980 -56.579 1.00 25.81  ? 46   PRO A CB  1 
ATOM   208  C  CG  . PRO A 1 25  ? -48.831 -40.238 -55.750 1.00 30.90  ? 46   PRO A CG  1 
ATOM   209  C  CD  . PRO A 1 25  ? -47.432 -40.793 -55.648 1.00 25.76  ? 46   PRO A CD  1 
ATOM   210  N  N   A HIS A 1 26  ? -47.061 -36.104 -56.003 0.61 24.67  ? 47   HIS A N   1 
ATOM   211  N  N   B HIS A 1 26  ? -47.097 -36.098 -55.989 0.39 25.45  ? 47   HIS A N   1 
ATOM   212  C  CA  A HIS A 1 26  ? -46.779 -34.952 -55.157 0.61 28.75  ? 47   HIS A CA  1 
ATOM   213  C  CA  B HIS A 1 26  ? -46.761 -34.962 -55.137 0.39 27.97  ? 47   HIS A CA  1 
ATOM   214  C  C   A HIS A 1 26  ? -47.717 -34.845 -53.951 0.61 26.15  ? 47   HIS A C   1 
ATOM   215  C  C   B HIS A 1 26  ? -47.743 -34.746 -53.983 0.39 26.28  ? 47   HIS A C   1 
ATOM   216  O  O   A HIS A 1 26  ? -47.285 -34.460 -52.865 0.61 25.79  ? 47   HIS A O   1 
ATOM   217  O  O   B HIS A 1 26  ? -47.364 -34.193 -52.951 0.39 24.91  ? 47   HIS A O   1 
ATOM   218  C  CB  A HIS A 1 26  ? -46.860 -33.649 -55.962 0.61 30.97  ? 47   HIS A CB  1 
ATOM   219  C  CB  B HIS A 1 26  ? -46.654 -33.680 -55.974 0.39 31.01  ? 47   HIS A CB  1 
ATOM   220  C  CG  A HIS A 1 26  ? -46.735 -32.427 -55.106 0.61 33.53  ? 47   HIS A CG  1 
ATOM   221  C  CG  B HIS A 1 26  ? -47.962 -33.156 -56.485 0.39 28.50  ? 47   HIS A CG  1 
ATOM   222  N  ND1 A HIS A 1 26  ? -47.792 -31.581 -54.865 0.61 33.04  ? 47   HIS A ND1 1 
ATOM   223  N  ND1 B HIS A 1 26  ? -48.528 -33.589 -57.666 0.39 37.39  ? 47   HIS A ND1 1 
ATOM   224  C  CD2 A HIS A 1 26  ? -45.702 -31.961 -54.359 0.61 39.54  ? 47   HIS A CD2 1 
ATOM   225  C  CD2 B HIS A 1 26  ? -48.785 -32.193 -56.006 0.39 30.86  ? 47   HIS A CD2 1 
ATOM   226  C  CE1 A HIS A 1 26  ? -47.413 -30.627 -54.035 0.61 32.50  ? 47   HIS A CE1 1 
ATOM   227  C  CE1 B HIS A 1 26  ? -49.655 -32.933 -57.880 0.39 37.11  ? 47   HIS A CE1 1 
ATOM   228  N  NE2 A HIS A 1 26  ? -46.147 -30.833 -53.714 0.61 42.82  ? 47   HIS A NE2 1 
ATOM   229  N  NE2 B HIS A 1 26  ? -49.835 -32.078 -56.886 0.39 33.62  ? 47   HIS A NE2 1 
ATOM   230  N  N   . ASP A 1 27  ? -48.995 -35.180 -54.133 1.00 25.28  ? 48   ASP A N   1 
ATOM   231  C  CA  . ASP A 1 27  ? -49.953 -34.927 -53.037 1.00 24.40  ? 48   ASP A CA  1 
ATOM   232  C  C   . ASP A 1 27  ? -49.853 -35.917 -51.826 1.00 23.60  ? 48   ASP A C   1 
ATOM   233  O  O   . ASP A 1 27  ? -50.673 -35.841 -50.907 1.00 26.10  ? 48   ASP A O   1 
ATOM   234  C  CB  . ASP A 1 27  ? -51.382 -34.856 -53.571 1.00 25.97  ? 48   ASP A CB  1 
ATOM   235  C  CG  . ASP A 1 27  ? -51.767 -33.429 -53.830 1.00 33.74  ? 48   ASP A CG  1 
ATOM   236  O  OD1 . ASP A 1 27  ? -52.242 -33.165 -54.924 1.00 32.18  ? 48   ASP A OD1 1 
ATOM   237  O  OD2 . ASP A 1 27  ? -51.533 -32.546 -52.937 1.00 28.83  ? 48   ASP A OD2 1 
ATOM   238  N  N   A ILE A 1 28  ? -48.831 -36.782 -51.825 0.77 22.53  ? 49   ILE A N   1 
ATOM   239  N  N   B ILE A 1 28  ? -48.819 -36.753 -51.808 0.23 22.54  ? 49   ILE A N   1 
ATOM   240  C  CA  A ILE A 1 28  ? -48.578 -37.572 -50.641 0.77 22.04  ? 49   ILE A CA  1 
ATOM   241  C  CA  B ILE A 1 28  ? -48.546 -37.548 -50.623 0.23 23.19  ? 49   ILE A CA  1 
ATOM   242  C  C   A ILE A 1 28  ? -47.175 -37.238 -50.074 0.77 21.39  ? 49   ILE A C   1 
ATOM   243  C  C   B ILE A 1 28  ? -47.190 -37.171 -50.023 0.23 22.13  ? 49   ILE A C   1 
ATOM   244  O  O   A ILE A 1 28  ? -46.789 -37.777 -49.047 0.77 23.12  ? 49   ILE A O   1 
ATOM   245  O  O   B ILE A 1 28  ? -46.851 -37.612 -48.926 0.23 22.59  ? 49   ILE A O   1 
ATOM   246  C  CB  A ILE A 1 28  ? -48.776 -39.118 -50.918 0.77 28.96  ? 49   ILE A CB  1 
ATOM   247  C  CB  B ILE A 1 28  ? -48.586 -39.055 -50.930 0.23 26.17  ? 49   ILE A CB  1 
ATOM   248  C  CG1 A ILE A 1 28  ? -49.036 -39.871 -49.595 0.77 31.74  ? 49   ILE A CG1 1 
ATOM   249  C  CG1 B ILE A 1 28  ? -49.797 -39.368 -51.796 0.23 22.30  ? 49   ILE A CG1 1 
ATOM   250  C  CG2 A ILE A 1 28  ? -47.629 -39.719 -51.742 0.77 21.03  ? 49   ILE A CG2 1 
ATOM   251  C  CG2 B ILE A 1 28  ? -48.670 -39.873 -49.644 0.23 30.10  ? 49   ILE A CG2 1 
ATOM   252  C  CD1 A ILE A 1 28  ? -49.650 -41.273 -49.742 0.77 26.77  ? 49   ILE A CD1 1 
ATOM   253  C  CD1 B ILE A 1 28  ? -50.091 -40.853 -51.929 0.23 27.32  ? 49   ILE A CD1 1 
ATOM   254  N  N   . HIS A 1 29  ? -46.419 -36.348 -50.733 1.00 22.72  ? 50   HIS A N   1 
ATOM   255  C  CA  . HIS A 1 29  ? -45.059 -36.047 -50.281 1.00 21.49  ? 50   HIS A CA  1 
ATOM   256  C  C   . HIS A 1 29  ? -45.010 -35.497 -48.879 1.00 25.37  ? 50   HIS A C   1 
ATOM   257  O  O   . HIS A 1 29  ? -44.141 -35.896 -48.086 1.00 24.93  ? 50   HIS A O   1 
ATOM   258  C  CB  . HIS A 1 29  ? -44.363 -35.022 -51.193 1.00 23.66  ? 50   HIS A CB  1 
ATOM   259  C  CG  . HIS A 1 29  ? -44.041 -35.570 -52.559 1.00 24.85  ? 50   HIS A CG  1 
ATOM   260  N  ND1 . HIS A 1 29  ? -43.328 -34.853 -53.507 1.00 25.12  ? 50   HIS A ND1 1 
ATOM   261  C  CD2 . HIS A 1 29  ? -44.308 -36.792 -53.114 1.00 25.09  ? 50   HIS A CD2 1 
ATOM   262  C  CE1 . HIS A 1 29  ? -43.186 -35.599 -54.600 1.00 25.15  ? 50   HIS A CE1 1 
ATOM   263  N  NE2 . HIS A 1 29  ? -43.739 -36.785 -54.379 1.00 23.73  ? 50   HIS A NE2 1 
ATOM   264  N  N   . LYS A 1 30  ? -45.873 -34.532 -48.591 1.00 24.56  ? 51   LYS A N   1 
ATOM   265  C  CA  . LYS A 1 30  ? -45.677 -33.829 -47.302 1.00 22.91  ? 51   LYS A CA  1 
ATOM   266  C  C   . LYS A 1 30  ? -45.992 -34.769 -46.134 1.00 27.33  ? 51   LYS A C   1 
ATOM   267  O  O   . LYS A 1 30  ? -45.293 -34.754 -45.107 1.00 24.59  ? 51   LYS A O   1 
ATOM   268  C  CB  . LYS A 1 30  ? -46.549 -32.591 -47.201 1.00 25.40  ? 51   LYS A CB  1 
ATOM   269  C  CG  . LYS A 1 30  ? -45.975 -31.342 -47.941 1.00 33.82  ? 51   LYS A CG  1 
ATOM   270  C  CD  . LYS A 1 30  ? -44.647 -30.869 -47.278 1.00 39.00  ? 51   LYS A CD  1 
ATOM   271  C  CE  . LYS A 1 30  ? -44.261 -29.498 -47.883 1.00 52.05  ? 51   LYS A CE  1 
ATOM   272  N  NZ  . LYS A 1 30  ? -42.939 -28.949 -47.430 1.00 54.28  ? 51   LYS A NZ  1 
ATOM   273  N  N   . ASN A 1 31  ? -47.045 -35.582 -46.258 1.00 22.91  ? 52   ASN A N   1 
ATOM   274  C  CA  . ASN A 1 31  ? -47.326 -36.499 -45.145 1.00 23.15  ? 52   ASN A CA  1 
ATOM   275  C  C   . ASN A 1 31  ? -46.300 -37.638 -45.066 1.00 23.12  ? 52   ASN A C   1 
ATOM   276  O  O   . ASN A 1 31  ? -46.021 -38.151 -43.970 1.00 25.95  ? 52   ASN A O   1 
ATOM   277  C  CB  . ASN A 1 31  ? -48.755 -37.060 -45.205 1.00 26.53  ? 52   ASN A CB  1 
ATOM   278  C  CG  . ASN A 1 31  ? -49.734 -36.095 -44.545 1.00 25.69  ? 52   ASN A CG  1 
ATOM   279  O  OD1 . ASN A 1 31  ? -49.448 -35.580 -43.457 1.00 28.33  ? 52   ASN A OD1 1 
ATOM   280  N  ND2 . ASN A 1 31  ? -50.829 -35.770 -45.212 1.00 26.46  ? 52   ASN A ND2 1 
ATOM   281  N  N   . VAL A 1 32  ? -45.781 -38.047 -46.216 1.00 23.61  ? 53   VAL A N   1 
ATOM   282  C  CA  . VAL A 1 32  ? -44.690 -39.020 -46.146 1.00 21.50  ? 53   VAL A CA  1 
ATOM   283  C  C   . VAL A 1 32  ? -43.469 -38.439 -45.416 1.00 25.19  ? 53   VAL A C   1 
ATOM   284  O  O   . VAL A 1 32  ? -42.792 -39.142 -44.622 1.00 23.20  ? 53   VAL A O   1 
ATOM   285  C  CB  . VAL A 1 32  ? -44.269 -39.469 -47.525 1.00 24.43  ? 53   VAL A CB  1 
ATOM   286  C  CG1 . VAL A 1 32  ? -42.854 -40.137 -47.477 1.00 30.12  ? 53   VAL A CG1 1 
ATOM   287  C  CG2 . VAL A 1 32  ? -45.273 -40.468 -48.044 1.00 26.05  ? 53   VAL A CG2 1 
ATOM   288  N  N   . MET A 1 33  ? -43.166 -37.179 -45.693 1.00 22.21  ? 54   MET A N   1 
ATOM   289  C  CA  . MET A 1 33  ? -42.075 -36.527 -44.939 1.00 25.44  ? 54   MET A CA  1 
ATOM   290  C  C   . MET A 1 33  ? -42.375 -36.385 -43.446 1.00 27.46  ? 54   MET A C   1 
ATOM   291  O  O   . MET A 1 33  ? -41.450 -36.454 -42.643 1.00 25.06  ? 54   MET A O   1 
ATOM   292  C  CB  . MET A 1 33  ? -41.727 -35.149 -45.518 1.00 25.97  ? 54   MET A CB  1 
ATOM   293  C  CG  . MET A 1 33  ? -41.038 -35.198 -46.887 1.00 26.77  ? 54   MET A CG  1 
ATOM   294  S  SD  . MET A 1 33  ? -39.564 -36.284 -46.863 1.00 30.57  ? 54   MET A SD  1 
ATOM   295  C  CE  . MET A 1 33  ? -38.570 -35.543 -45.546 1.00 25.91  ? 54   MET A CE  1 
ATOM   296  N  N   . ARG A 1 34  ? -43.637 -36.195 -43.057 1.00 27.03  ? 55   ARG A N   1 
ATOM   297  C  CA  . ARG A 1 34  ? -43.982 -36.172 -41.645 1.00 25.60  ? 55   ARG A CA  1 
ATOM   298  C  C   . ARG A 1 34  ? -43.660 -37.532 -40.994 1.00 25.02  ? 55   ARG A C   1 
ATOM   299  O  O   . ARG A 1 34  ? -43.108 -37.588 -39.887 1.00 27.80  ? 55   ARG A O   1 
ATOM   300  C  CB  . ARG A 1 34  ? -45.470 -35.813 -41.447 1.00 25.96  ? 55   ARG A CB  1 
ATOM   301  C  CG  . ARG A 1 34  ? -45.682 -34.303 -41.732 1.00 26.08  ? 55   ARG A CG  1 
ATOM   302  C  CD  . ARG A 1 34  ? -47.097 -33.781 -41.490 1.00 27.05  ? 55   ARG A CD  1 
ATOM   303  N  NE  . ARG A 1 34  ? -47.085 -32.400 -42.019 1.00 32.41  ? 55   ARG A NE  1 
ATOM   304  C  CZ  . ARG A 1 34  ? -47.661 -32.004 -43.150 1.00 35.71  ? 55   ARG A CZ  1 
ATOM   305  N  NH1 . ARG A 1 34  ? -48.417 -32.851 -43.866 1.00 27.20  ? 55   ARG A NH1 1 
ATOM   306  N  NH2 . ARG A 1 34  ? -47.552 -30.715 -43.519 1.00 33.58  ? 55   ARG A NH2 1 
ATOM   307  N  N   . MET A 1 35  ? -43.928 -38.602 -41.733 1.00 22.62  ? 56   MET A N   1 
ATOM   308  C  CA  . MET A 1 35  ? -43.588 -39.962 -41.262 1.00 25.76  ? 56   MET A CA  1 
ATOM   309  C  C   . MET A 1 35  ? -42.062 -40.109 -41.131 1.00 23.72  ? 56   MET A C   1 
ATOM   310  O  O   . MET A 1 35  ? -41.536 -40.608 -40.104 1.00 28.52  ? 56   MET A O   1 
ATOM   311  C  CB  . MET A 1 35  ? -44.128 -41.057 -42.218 1.00 30.96  ? 56   MET A CB  1 
ATOM   312  C  CG  . MET A 1 35  ? -43.707 -42.494 -41.834 1.00 33.84  ? 56   MET A CG  1 
ATOM   313  S  SD  . MET A 1 35  ? -44.096 -43.676 -43.215 1.00 34.29  ? 56   MET A SD  1 
ATOM   314  C  CE  . MET A 1 35  ? -42.670 -43.386 -44.305 1.00 32.47  ? 56   MET A CE  1 
ATOM   315  N  N   . VAL A 1 36  ? -41.365 -39.717 -42.180 1.00 21.44  ? 57   VAL A N   1 
ATOM   316  C  CA  . VAL A 1 36  ? -39.883 -39.810 -42.148 1.00 21.43  ? 57   VAL A CA  1 
ATOM   317  C  C   . VAL A 1 36  ? -39.279 -39.016 -40.994 1.00 26.47  ? 57   VAL A C   1 
ATOM   318  O  O   . VAL A 1 36  ? -38.470 -39.535 -40.226 1.00 25.15  ? 57   VAL A O   1 
ATOM   319  C  CB  . VAL A 1 36  ? -39.304 -39.318 -43.461 1.00 24.38  ? 57   VAL A CB  1 
ATOM   320  C  CG1 . VAL A 1 36  ? -37.791 -39.232 -43.406 1.00 23.19  ? 57   VAL A CG1 1 
ATOM   321  C  CG2 . VAL A 1 36  ? -39.711 -40.343 -44.571 1.00 23.32  ? 57   VAL A CG2 1 
ATOM   322  N  N   . ASN A 1 37  ? -39.667 -37.753 -40.892 1.00 23.48  ? 58   ASN A N   1 
ATOM   323  C  CA  . ASN A 1 37  ? -39.105 -36.905 -39.819 1.00 27.23  ? 58   ASN A CA  1 
ATOM   324  C  C   . ASN A 1 37  ? -39.440 -37.425 -38.421 1.00 30.83  ? 58   ASN A C   1 
ATOM   325  O  O   . ASN A 1 37  ? -38.632 -37.307 -37.489 1.00 30.63  ? 58   ASN A O   1 
ATOM   326  C  CB  . ASN A 1 37  ? -39.575 -35.473 -39.997 1.00 28.40  ? 58   ASN A CB  1 
ATOM   327  C  CG  . ASN A 1 37  ? -38.908 -34.803 -41.191 1.00 33.76  ? 58   ASN A CG  1 
ATOM   328  O  OD1 . ASN A 1 37  ? -37.794 -35.101 -41.505 1.00 37.99  ? 58   ASN A OD1 1 
ATOM   329  N  ND2 . ASN A 1 37  ? -39.608 -33.910 -41.852 1.00 33.60  ? 58   ASN A ND2 1 
ATOM   330  N  N   . HIS A 1 38  ? -40.627 -37.991 -38.264 1.00 26.84  ? 59   HIS A N   1 
ATOM   331  C  CA  . HIS A 1 38  ? -41.024 -38.505 -37.012 1.00 31.83  ? 59   HIS A CA  1 
ATOM   332  C  C   . HIS A 1 38  ? -40.103 -39.665 -36.638 1.00 32.02  ? 59   HIS A C   1 
ATOM   333  O  O   . HIS A 1 38  ? -39.645 -39.771 -35.496 1.00 32.80  ? 59   HIS A O   1 
ATOM   334  C  CB  . HIS A 1 38  ? -42.493 -39.005 -37.018 1.00 31.00  ? 59   HIS A CB  1 
ATOM   335  C  CG  . HIS A 1 38  ? -42.852 -39.763 -35.773 1.00 47.67  ? 59   HIS A CG  1 
ATOM   336  N  ND1 . HIS A 1 38  ? -42.995 -39.148 -34.543 1.00 44.34  ? 59   HIS A ND1 1 
ATOM   337  C  CD2 . HIS A 1 38  ? -43.022 -41.089 -35.552 1.00 48.22  ? 59   HIS A CD2 1 
ATOM   338  C  CE1 . HIS A 1 38  ? -43.274 -40.058 -33.627 1.00 45.27  ? 59   HIS A CE1 1 
ATOM   339  N  NE2 . HIS A 1 38  ? -43.298 -41.242 -34.209 1.00 48.46  ? 59   HIS A NE2 1 
ATOM   340  N  N   . GLU A 1 39  ? -39.874 -40.550 -37.598 1.00 26.62  ? 60   GLU A N   1 
ATOM   341  C  CA  . GLU A 1 39  ? -39.054 -41.722 -37.296 1.00 29.09  ? 60   GLU A CA  1 
ATOM   342  C  C   . GLU A 1 39  ? -37.622 -41.265 -36.941 1.00 22.59  ? 60   GLU A C   1 
ATOM   343  O  O   . GLU A 1 39  ? -37.031 -41.738 -35.952 1.00 26.16  ? 60   GLU A O   1 
ATOM   344  C  CB  . GLU A 1 39  ? -39.061 -42.676 -38.507 1.00 26.60  ? 60   GLU A CB  1 
ATOM   345  C  CG  . GLU A 1 39  ? -40.442 -43.345 -38.743 1.00 31.44  ? 60   GLU A CG  1 
ATOM   346  C  CD  . GLU A 1 39  ? -40.889 -44.275 -37.627 1.00 37.21  ? 60   GLU A CD  1 
ATOM   347  O  OE1 . GLU A 1 39  ? -40.025 -44.935 -37.004 1.00 36.85  ? 60   GLU A OE1 1 
ATOM   348  O  OE2 . GLU A 1 39  ? -42.110 -44.356 -37.353 1.00 37.91  ? 60   GLU A OE2 1 
ATOM   349  N  N   . VAL A 1 40  ? -37.086 -40.367 -37.755 1.00 24.33  ? 61   VAL A N   1 
ATOM   350  C  CA  . VAL A 1 40  ? -35.700 -39.947 -37.576 1.00 24.98  ? 61   VAL A CA  1 
ATOM   351  C  C   . VAL A 1 40  ? -35.552 -39.256 -36.214 1.00 30.14  ? 61   VAL A C   1 
ATOM   352  O  O   . VAL A 1 40  ? -34.566 -39.465 -35.442 1.00 25.92  ? 61   VAL A O   1 
ATOM   353  C  CB  . VAL A 1 40  ? -35.269 -39.020 -38.713 1.00 28.51  ? 61   VAL A CB  1 
ATOM   354  C  CG1 . VAL A 1 40  ? -33.965 -38.325 -38.317 1.00 28.43  ? 61   VAL A CG1 1 
ATOM   355  C  CG2 . VAL A 1 40  ? -35.116 -39.826 -40.043 1.00 22.92  ? 61   VAL A CG2 1 
ATOM   356  N  N   . SER A 1 41  ? -36.526 -38.432 -35.882 1.00 29.75  ? 62   SER A N   1 
ATOM   357  C  CA  . SER A 1 41  ? -36.400 -37.694 -34.616 1.00 28.77  ? 62   SER A CA  1 
ATOM   358  C  C   . SER A 1 41  ? -36.434 -38.593 -33.368 1.00 36.71  ? 62   SER A C   1 
ATOM   359  O  O   . SER A 1 41  ? -35.988 -38.161 -32.302 1.00 34.56  ? 62   SER A O   1 
ATOM   360  C  CB  . SER A 1 41  ? -37.493 -36.632 -34.535 1.00 34.81  ? 62   SER A CB  1 
ATOM   361  O  OG  . SER A 1 41  ? -38.703 -37.280 -34.152 1.00 54.06  ? 62   SER A OG  1 
ATOM   362  N  N   . SER A 1 42  ? -36.971 -39.821 -33.486 1.00 33.52  ? 63   SER A N   1 
ATOM   363  C  CA  . SER A 1 42  ? -37.054 -40.768 -32.359 1.00 38.78  ? 63   SER A CA  1 
ATOM   364  C  C   . SER A 1 42  ? -35.763 -41.556 -32.110 1.00 34.37  ? 63   SER A C   1 
ATOM   365  O  O   . SER A 1 42  ? -35.675 -42.291 -31.131 1.00 33.67  ? 63   SER A O   1 
ATOM   366  C  CB  . SER A 1 42  ? -38.237 -41.767 -32.584 1.00 35.27  ? 63   SER A CB  1 
ATOM   367  O  OG  . SER A 1 42  ? -37.966 -42.612 -33.703 1.00 37.95  ? 63   SER A OG  1 
ATOM   368  N  N   . PHE A 1 43  ? -34.740 -41.422 -32.952 1.00 34.89  ? 64   PHE A N   1 
ATOM   369  C  CA  . PHE A 1 43  ? -33.526 -42.189 -32.739 1.00 36.07  ? 64   PHE A CA  1 
ATOM   370  C  C   . PHE A 1 43  ? -32.896 -41.752 -31.413 1.00 33.53  ? 64   PHE A C   1 
ATOM   371  O  O   . PHE A 1 43  ? -32.729 -40.532 -31.130 1.00 36.51  ? 64   PHE A O   1 
ATOM   372  C  CB  . PHE A 1 43  ? -32.479 -41.965 -33.843 1.00 28.50  ? 64   PHE A CB  1 
ATOM   373  C  CG  . PHE A 1 43  ? -32.697 -42.741 -35.094 1.00 26.10  ? 64   PHE A CG  1 
ATOM   374  C  CD1 . PHE A 1 43  ? -33.966 -42.869 -35.687 1.00 27.22  ? 64   PHE A CD1 1 
ATOM   375  C  CD2 . PHE A 1 43  ? -31.624 -43.374 -35.712 1.00 26.72  ? 64   PHE A CD2 1 
ATOM   376  C  CE1 . PHE A 1 43  ? -34.150 -43.602 -36.869 1.00 27.71  ? 64   PHE A CE1 1 
ATOM   377  C  CE2 . PHE A 1 43  ? -31.773 -44.066 -36.866 1.00 26.42  ? 64   PHE A CE2 1 
ATOM   378  C  CZ  . PHE A 1 43  ? -33.029 -44.217 -37.480 1.00 28.45  ? 64   PHE A CZ  1 
ATOM   379  N  N   . GLY A 1 44  ? -32.543 -42.729 -30.591 1.00 37.30  ? 65   GLY A N   1 
ATOM   380  C  CA  . GLY A 1 44  ? -31.991 -42.396 -29.280 1.00 40.32  ? 65   GLY A CA  1 
ATOM   381  C  C   . GLY A 1 44  ? -32.928 -41.855 -28.201 1.00 42.40  ? 65   GLY A C   1 
ATOM   382  O  O   . GLY A 1 44  ? -32.473 -41.500 -27.120 1.00 53.85  ? 65   GLY A O   1 
ATOM   383  N  N   . VAL A 1 45  ? -34.230 -41.806 -28.435 1.00 47.41  ? 66   VAL A N   1 
ATOM   384  C  CA  . VAL A 1 45  ? -35.121 -41.454 -27.341 1.00 48.46  ? 66   VAL A CA  1 
ATOM   385  C  C   . VAL A 1 45  ? -35.133 -42.593 -26.302 1.00 51.24  ? 66   VAL A C   1 
ATOM   386  O  O   . VAL A 1 45  ? -35.254 -43.785 -26.603 1.00 51.08  ? 66   VAL A O   1 
ATOM   387  C  CB  . VAL A 1 45  ? -36.615 -41.182 -27.779 1.00 67.30  ? 66   VAL A CB  1 
ATOM   388  C  CG1 . VAL A 1 45  ? -36.734 -40.018 -28.759 1.00 63.10  ? 66   VAL A CG1 1 
ATOM   389  C  CG2 . VAL A 1 45  ? -37.255 -42.421 -28.334 1.00 68.15  ? 66   VAL A CG2 1 
ATOM   390  N  N   . VAL A 1 46  ? -35.041 -42.185 -25.056 1.00 52.46  ? 67   VAL A N   1 
ATOM   391  C  CA  . VAL A 1 46  ? -35.173 -43.112 -23.954 1.00 57.92  ? 67   VAL A CA  1 
ATOM   392  C  C   . VAL A 1 46  ? -36.604 -43.155 -23.415 1.00 73.77  ? 67   VAL A C   1 
ATOM   393  O  O   . VAL A 1 46  ? -37.266 -42.126 -23.284 1.00 71.34  ? 67   VAL A O   1 
ATOM   394  C  CB  . VAL A 1 46  ? -34.195 -42.716 -22.833 1.00 61.04  ? 67   VAL A CB  1 
ATOM   395  C  CG1 . VAL A 1 46  ? -34.332 -43.660 -21.635 1.00 67.24  ? 67   VAL A CG1 1 
ATOM   396  C  CG2 . VAL A 1 46  ? -32.771 -42.693 -23.395 1.00 59.46  ? 67   VAL A CG2 1 
ATOM   397  N  N   . THR A 1 47  ? -37.080 -44.356 -23.116 1.00 84.02  ? 68   THR A N   1 
ATOM   398  C  CA  . THR A 1 47  ? -38.300 -44.530 -22.337 1.00 89.40  ? 68   THR A CA  1 
ATOM   399  C  C   . THR A 1 47  ? -37.943 -45.195 -21.022 1.00 99.41  ? 68   THR A C   1 
ATOM   400  O  O   . THR A 1 47  ? -38.038 -46.418 -20.906 1.00 107.05 ? 68   THR A O   1 
ATOM   401  C  CB  . THR A 1 47  ? -39.330 -45.388 -23.066 1.00 88.46  ? 68   THR A CB  1 
ATOM   402  O  OG1 . THR A 1 47  ? -38.817 -46.718 -23.202 1.00 90.07  ? 68   THR A OG1 1 
ATOM   403  C  CG2 . THR A 1 47  ? -39.620 -44.811 -24.445 1.00 83.45  ? 68   THR A CG2 1 
ATOM   404  N  N   . SER A 1 48  ? -37.533 -44.375 -20.052 1.00 101.23 ? 69   SER A N   1 
ATOM   405  C  CA  . SER A 1 48  ? -37.009 -44.812 -18.752 1.00 105.81 ? 69   SER A CA  1 
ATOM   406  C  C   . SER A 1 48  ? -36.290 -46.154 -18.827 1.00 108.08 ? 69   SER A C   1 
ATOM   407  O  O   . SER A 1 48  ? -35.418 -46.372 -19.682 1.00 103.39 ? 69   SER A O   1 
ATOM   408  C  CB  . SER A 1 48  ? -38.138 -44.896 -17.716 1.00 113.58 ? 69   SER A CB  1 
ATOM   409  O  OG  . SER A 1 48  ? -38.832 -43.664 -17.605 1.00 114.43 ? 69   SER A OG  1 
ATOM   410  N  N   . ALA A 1 49  ? -36.666 -47.043 -17.913 1.00 110.87 ? 70   ALA A N   1 
ATOM   411  C  CA  . ALA A 1 49  ? -36.380 -48.458 -18.061 1.00 112.87 ? 70   ALA A CA  1 
ATOM   412  C  C   . ALA A 1 49  ? -34.888 -48.749 -18.196 1.00 111.79 ? 70   ALA A C   1 
ATOM   413  O  O   . ALA A 1 49  ? -34.048 -48.134 -17.532 1.00 109.58 ? 70   ALA A O   1 
ATOM   414  C  CB  . ALA A 1 49  ? -37.141 -49.010 -19.287 1.00 106.48 ? 70   ALA A CB  1 
ATOM   415  N  N   . GLU A 1 50  ? -34.583 -49.677 -19.099 1.00 109.58 ? 71   GLU A N   1 
ATOM   416  C  CA  . GLU A 1 50  ? -33.223 -50.122 -19.350 1.00 104.96 ? 71   GLU A CA  1 
ATOM   417  C  C   . GLU A 1 50  ? -32.696 -49.690 -20.723 1.00 92.59  ? 71   GLU A C   1 
ATOM   418  O  O   . GLU A 1 50  ? -31.753 -50.285 -21.244 1.00 86.90  ? 71   GLU A O   1 
ATOM   419  C  CB  . GLU A 1 50  ? -33.149 -51.640 -19.229 1.00 109.65 ? 71   GLU A CB  1 
ATOM   420  C  CG  . GLU A 1 50  ? -34.129 -52.383 -20.114 1.00 107.31 ? 71   GLU A CG  1 
ATOM   421  C  CD  . GLU A 1 50  ? -34.092 -53.882 -19.872 1.00 118.01 ? 71   GLU A CD  1 
ATOM   422  O  OE1 . GLU A 1 50  ? -33.221 -54.341 -19.093 1.00 127.00 ? 71   GLU A OE1 1 
ATOM   423  O  OE2 . GLU A 1 50  ? -34.935 -54.603 -20.452 1.00 116.30 ? 71   GLU A OE2 1 
ATOM   424  N  N   . ASP A 1 51  ? -33.297 -48.670 -21.321 1.00 87.68  ? 72   ASP A N   1 
ATOM   425  C  CA  . ASP A 1 51  ? -32.794 -48.246 -22.628 1.00 78.39  ? 72   ASP A CA  1 
ATOM   426  C  C   . ASP A 1 51  ? -32.200 -46.823 -22.597 1.00 80.29  ? 72   ASP A C   1 
ATOM   427  O  O   . ASP A 1 51  ? -32.174 -46.121 -23.619 1.00 73.67  ? 72   ASP A O   1 
ATOM   428  C  CB  . ASP A 1 51  ? -33.891 -48.380 -23.702 1.00 74.09  ? 72   ASP A CB  1 
ATOM   429  C  CG  . ASP A 1 51  ? -35.033 -47.408 -23.518 1.00 79.32  ? 72   ASP A CG  1 
ATOM   430  O  OD1 . ASP A 1 51  ? -35.155 -46.837 -22.415 1.00 87.40  ? 72   ASP A OD1 1 
ATOM   431  O  OD2 . ASP A 1 51  ? -35.831 -47.239 -24.474 1.00 77.74  ? 72   ASP A OD2 1 
ATOM   432  N  N   . SER A 1 52  ? -31.670 -46.426 -21.434 1.00 85.80  ? 73   SER A N   1 
ATOM   433  C  CA  . SER A 1 52  ? -30.998 -45.128 -21.273 1.00 77.70  ? 73   SER A CA  1 
ATOM   434  C  C   . SER A 1 52  ? -29.706 -45.097 -22.063 1.00 70.65  ? 73   SER A C   1 
ATOM   435  O  O   . SER A 1 52  ? -29.109 -44.041 -22.300 1.00 72.86  ? 73   SER A O   1 
ATOM   436  C  CB  . SER A 1 52  ? -30.723 -44.846 -19.794 1.00 85.20  ? 73   SER A CB  1 
ATOM   437  O  OG  . SER A 1 52  ? -31.923 -44.925 -19.046 1.00 91.02  ? 73   SER A OG  1 
ATOM   438  N  N   . TYR A 1 53  ? -29.274 -46.284 -22.458 1.00 72.17  ? 74   TYR A N   1 
ATOM   439  C  CA  . TYR A 1 53  ? -28.093 -46.439 -23.274 1.00 77.00  ? 74   TYR A CA  1 
ATOM   440  C  C   . TYR A 1 53  ? -28.307 -45.690 -24.592 1.00 72.67  ? 74   TYR A C   1 
ATOM   441  O  O   . TYR A 1 53  ? -27.357 -45.224 -25.240 1.00 66.22  ? 74   TYR A O   1 
ATOM   442  C  CB  . TYR A 1 53  ? -27.788 -47.939 -23.487 1.00 85.72  ? 74   TYR A CB  1 
ATOM   443  C  CG  . TYR A 1 53  ? -28.666 -48.727 -24.456 1.00 88.61  ? 74   TYR A CG  1 
ATOM   444  C  CD1 . TYR A 1 53  ? -28.447 -48.650 -25.838 1.00 80.66  ? 74   TYR A CD1 1 
ATOM   445  C  CD2 . TYR A 1 53  ? -29.663 -49.604 -23.996 1.00 90.88  ? 74   TYR A CD2 1 
ATOM   446  C  CE1 . TYR A 1 53  ? -29.207 -49.369 -26.737 1.00 73.73  ? 74   TYR A CE1 1 
ATOM   447  C  CE2 . TYR A 1 53  ? -30.439 -50.342 -24.909 1.00 88.78  ? 74   TYR A CE2 1 
ATOM   448  C  CZ  . TYR A 1 53  ? -30.197 -50.207 -26.284 1.00 80.25  ? 74   TYR A CZ  1 
ATOM   449  O  OH  . TYR A 1 53  ? -30.913 -50.903 -27.232 1.00 71.83  ? 74   TYR A OH  1 
ATOM   450  N  N   . LEU A 1 54  ? -29.577 -45.549 -24.966 1.00 68.59  ? 75   LEU A N   1 
ATOM   451  C  CA  . LEU A 1 54  ? -29.930 -44.868 -26.205 1.00 66.09  ? 75   LEU A CA  1 
ATOM   452  C  C   . LEU A 1 54  ? -29.657 -43.367 -26.224 1.00 59.94  ? 75   LEU A C   1 
ATOM   453  O  O   . LEU A 1 54  ? -29.555 -42.799 -27.302 1.00 49.15  ? 75   LEU A O   1 
ATOM   454  C  CB  . LEU A 1 54  ? -31.413 -45.089 -26.509 1.00 70.70  ? 75   LEU A CB  1 
ATOM   455  C  CG  . LEU A 1 54  ? -31.750 -46.161 -27.532 1.00 69.43  ? 75   LEU A CG  1 
ATOM   456  C  CD1 . LEU A 1 54  ? -30.481 -46.687 -28.158 1.00 68.15  ? 75   LEU A CD1 1 
ATOM   457  C  CD2 . LEU A 1 54  ? -32.565 -47.263 -26.898 1.00 67.88  ? 75   LEU A CD2 1 
ATOM   458  N  N   . GLY A 1 55  ? -29.541 -42.744 -25.037 1.00 69.14  ? 76   GLY A N   1 
ATOM   459  C  CA  . GLY A 1 55  ? -29.708 -41.307 -24.879 1.00 56.73  ? 76   GLY A CA  1 
ATOM   460  C  C   . GLY A 1 55  ? -28.566 -40.427 -25.358 1.00 55.08  ? 76   GLY A C   1 
ATOM   461  O  O   . GLY A 1 55  ? -28.770 -39.265 -25.645 1.00 47.04  ? 76   GLY A O   1 
ATOM   462  N  N   . ALA A 1 56  ? -27.362 -40.995 -25.427 1.00 30.07  ? 77   ALA A N   1 
ATOM   463  C  CA  . ALA A 1 56  ? -26.174 -40.239 -25.937 1.00 28.59  ? 77   ALA A CA  1 
ATOM   464  C  C   . ALA A 1 56  ? -25.147 -41.218 -26.510 1.00 27.77  ? 77   ALA A C   1 
ATOM   465  O  O   . ALA A 1 56  ? -25.038 -42.366 -26.005 1.00 28.97  ? 77   ALA A O   1 
ATOM   466  C  CB  . ALA A 1 56  ? -25.560 -39.428 -24.791 1.00 30.03  ? 77   ALA A CB  1 
ATOM   467  N  N   . VAL A 1 57  ? -24.356 -40.774 -27.460 1.00 26.23  ? 78   VAL A N   1 
ATOM   468  C  CA  . VAL A 1 57  ? -23.263 -41.590 -28.001 1.00 25.79  ? 78   VAL A CA  1 
ATOM   469  C  C   . VAL A 1 57  ? -22.086 -40.681 -28.261 1.00 30.15  ? 78   VAL A C   1 
ATOM   470  O  O   . VAL A 1 57  ? -22.246 -39.445 -28.230 1.00 27.09  ? 78   VAL A O   1 
ATOM   471  C  CB  . VAL A 1 57  ? -23.674 -42.294 -29.306 1.00 24.59  ? 78   VAL A CB  1 
ATOM   472  C  CG1 . VAL A 1 57  ? -24.822 -43.362 -29.039 1.00 25.49  ? 78   VAL A CG1 1 
ATOM   473  C  CG2 . VAL A 1 57  ? -24.087 -41.311 -30.376 1.00 24.66  ? 78   VAL A CG2 1 
ATOM   474  N  N   . ASP A 1 58  ? -20.915 -41.241 -28.529 1.00 25.35  ? 79   ASP A N   1 
ATOM   475  C  CA  . ASP A 1 58  ? -19.771 -40.327 -28.806 1.00 25.08  ? 79   ASP A CA  1 
ATOM   476  C  C   . ASP A 1 58  ? -19.849 -39.893 -30.275 1.00 24.02  ? 79   ASP A C   1 
ATOM   477  O  O   . ASP A 1 58  ? -20.763 -40.322 -31.032 1.00 23.42  ? 79   ASP A O   1 
ATOM   478  C  CB  . ASP A 1 58  ? -18.422 -40.964 -28.431 1.00 26.10  ? 79   ASP A CB  1 
ATOM   479  C  CG  . ASP A 1 58  ? -18.091 -42.210 -29.249 1.00 27.40  ? 79   ASP A CG  1 
ATOM   480  O  OD1 . ASP A 1 58  ? -18.866 -42.582 -30.125 1.00 29.24  ? 79   ASP A OD1 1 
ATOM   481  O  OD2 . ASP A 1 58  ? -17.036 -42.819 -28.953 1.00 30.86  ? 79   ASP A OD2 1 
ATOM   482  N  N   . GLU A 1 59  ? -18.921 -39.037 -30.715 1.00 23.66  ? 80   GLU A N   1 
ATOM   483  C  CA  . GLU A 1 59  ? -19.050 -38.495 -32.072 1.00 22.79  ? 80   GLU A CA  1 
ATOM   484  C  C   . GLU A 1 59  ? -18.754 -39.566 -33.130 1.00 24.98  ? 80   GLU A C   1 
ATOM   485  O  O   . GLU A 1 59  ? -19.364 -39.563 -34.188 1.00 24.99  ? 80   GLU A O   1 
ATOM   486  C  CB  . GLU A 1 59  ? -18.124 -37.266 -32.257 1.00 23.30  ? 80   GLU A CB  1 
ATOM   487  C  CG  . GLU A 1 59  ? -18.467 -36.140 -31.248 1.00 24.68  ? 80   GLU A CG  1 
ATOM   488  C  CD  . GLU A 1 59  ? -17.791 -34.811 -31.640 1.00 33.74  ? 80   GLU A CD  1 
ATOM   489  O  OE1 . GLU A 1 59  ? -16.641 -34.569 -31.216 1.00 27.78  ? 80   GLU A OE1 1 
ATOM   490  O  OE2 . GLU A 1 59  ? -18.440 -34.051 -32.381 1.00 33.84  ? 80   GLU A OE2 1 
ATOM   491  N  N   A ASN A 1 60  ? -17.823 -40.481 -32.833 0.72 24.98  ? 81   ASN A N   1 
ATOM   492  N  N   B ASN A 1 60  ? -17.837 -40.484 -32.830 0.28 25.05  ? 81   ASN A N   1 
ATOM   493  C  CA  A ASN A 1 60  ? -17.505 -41.547 -33.789 0.72 25.64  ? 81   ASN A CA  1 
ATOM   494  C  CA  B ASN A 1 60  ? -17.507 -41.543 -33.783 0.28 26.00  ? 81   ASN A CA  1 
ATOM   495  C  C   A ASN A 1 60  ? -18.724 -42.453 -34.054 0.72 27.33  ? 81   ASN A C   1 
ATOM   496  C  C   B ASN A 1 60  ? -18.697 -42.472 -34.043 0.28 26.57  ? 81   ASN A C   1 
ATOM   497  O  O   A ASN A 1 60  ? -18.986 -42.890 -35.180 0.72 26.44  ? 81   ASN A O   1 
ATOM   498  O  O   B ASN A 1 60  ? -18.920 -42.921 -35.169 0.28 26.40  ? 81   ASN A O   1 
ATOM   499  C  CB  A ASN A 1 60  ? -16.314 -42.396 -33.283 0.72 29.13  ? 81   ASN A CB  1 
ATOM   500  C  CB  B ASN A 1 60  ? -16.306 -42.358 -33.289 0.28 29.57  ? 81   ASN A CB  1 
ATOM   501  C  CG  A ASN A 1 60  ? -14.970 -41.700 -33.462 0.72 35.44  ? 81   ASN A CG  1 
ATOM   502  C  CG  B ASN A 1 60  ? -15.863 -43.409 -34.294 0.28 33.29  ? 81   ASN A CG  1 
ATOM   503  O  OD1 A ASN A 1 60  ? -14.850 -40.711 -34.192 0.72 42.03  ? 81   ASN A OD1 1 
ATOM   504  O  OD1 B ASN A 1 60  ? -15.669 -43.123 -35.472 0.28 38.13  ? 81   ASN A OD1 1 
ATOM   505  N  ND2 A ASN A 1 60  ? -13.936 -42.209 -32.754 0.72 38.36  ? 81   ASN A ND2 1 
ATOM   506  N  ND2 B ASN A 1 60  ? -15.708 -44.634 -33.829 0.28 37.47  ? 81   ASN A ND2 1 
ATOM   507  N  N   . THR A 1 61  ? -19.456 -42.766 -32.991 1.00 26.65  ? 82   THR A N   1 
ATOM   508  C  CA  . THR A 1 61  ? -20.657 -43.620 -33.120 1.00 26.23  ? 82   THR A CA  1 
ATOM   509  C  C   . THR A 1 61  ? -21.745 -42.896 -33.884 1.00 31.60  ? 82   THR A C   1 
ATOM   510  O  O   . THR A 1 61  ? -22.389 -43.490 -34.741 1.00 25.38  ? 82   THR A O   1 
ATOM   511  C  CB  . THR A 1 61  ? -21.163 -44.023 -31.743 1.00 23.95  ? 82   THR A CB  1 
ATOM   512  O  OG1 . THR A 1 61  ? -20.129 -44.755 -31.055 1.00 25.40  ? 82   THR A OG1 1 
ATOM   513  C  CG2 . THR A 1 61  ? -22.439 -44.897 -31.793 1.00 24.31  ? 82   THR A CG2 1 
ATOM   514  N  N   . LEU A 1 62  ? -21.983 -41.625 -33.557 1.00 22.55  ? 83   LEU A N   1 
ATOM   515  C  CA  . LEU A 1 62  ? -22.909 -40.820 -34.360 1.00 23.80  ? 83   LEU A CA  1 
ATOM   516  C  C   . LEU A 1 62  ? -22.510 -40.858 -35.846 1.00 26.82  ? 83   LEU A C   1 
ATOM   517  O  O   . LEU A 1 62  ? -23.350 -40.999 -36.736 1.00 25.06  ? 83   LEU A O   1 
ATOM   518  C  CB  . LEU A 1 62  ? -22.950 -39.365 -33.855 1.00 20.76  ? 83   LEU A CB  1 
ATOM   519  C  CG  . LEU A 1 62  ? -23.761 -38.417 -34.761 1.00 27.48  ? 83   LEU A CG  1 
ATOM   520  C  CD1 . LEU A 1 62  ? -25.201 -38.982 -35.042 1.00 29.04  ? 83   LEU A CD1 1 
ATOM   521  C  CD2 . LEU A 1 62  ? -23.830 -37.055 -34.064 1.00 29.17  ? 83   LEU A CD2 1 
ATOM   522  N  N   . GLU A 1 63  ? -21.217 -40.689 -36.117 1.00 22.86  ? 84   GLU A N   1 
ATOM   523  C  CA  . GLU A 1 63  ? -20.742 -40.680 -37.504 1.00 22.82  ? 84   GLU A CA  1 
ATOM   524  C  C   . GLU A 1 63  ? -21.036 -42.007 -38.202 1.00 22.58  ? 84   GLU A C   1 
ATOM   525  O  O   . GLU A 1 63  ? -21.519 -42.032 -39.334 1.00 24.85  ? 84   GLU A O   1 
ATOM   526  C  CB  . GLU A 1 63  ? -19.248 -40.377 -37.559 1.00 24.37  ? 84   GLU A CB  1 
ATOM   527  C  CG  . GLU A 1 63  ? -18.720 -40.239 -39.020 1.00 25.66  ? 84   GLU A CG  1 
ATOM   528  C  CD  . GLU A 1 63  ? -17.257 -39.846 -39.037 1.00 35.22  ? 84   GLU A CD  1 
ATOM   529  O  OE1 . GLU A 1 63  ? -16.478 -40.329 -38.166 1.00 33.16  ? 84   GLU A OE1 1 
ATOM   530  O  OE2 . GLU A 1 63  ? -16.891 -39.051 -39.922 1.00 30.96  ? 84   GLU A OE2 1 
ATOM   531  N  N   . GLN A 1 64  ? -20.799 -43.122 -37.516 1.00 25.72  ? 85   GLN A N   1 
ATOM   532  C  CA  . GLN A 1 64  ? -21.118 -44.408 -38.111 1.00 26.25  ? 85   GLN A CA  1 
ATOM   533  C  C   . GLN A 1 64  ? -22.594 -44.531 -38.410 1.00 27.16  ? 85   GLN A C   1 
ATOM   534  O  O   . GLN A 1 64  ? -22.985 -45.097 -39.454 1.00 24.08  ? 85   GLN A O   1 
ATOM   535  C  CB  . GLN A 1 64  ? -20.744 -45.551 -37.184 1.00 26.97  ? 85   GLN A CB  1 
ATOM   536  C  CG  . GLN A 1 64  ? -19.289 -45.772 -36.959 1.00 35.71  ? 85   GLN A CG  1 
ATOM   537  C  CD  . GLN A 1 64  ? -19.150 -46.969 -36.010 1.00 49.84  ? 85   GLN A CD  1 
ATOM   538  O  OE1 . GLN A 1 64  ? -19.206 -46.823 -34.768 1.00 51.76  ? 85   GLN A OE1 1 
ATOM   539  N  NE2 . GLN A 1 64  ? -19.095 -48.154 -36.587 1.00 51.77  ? 85   GLN A NE2 1 
ATOM   540  N  N   . ALA A 1 65  ? -23.422 -44.098 -37.448 1.00 23.49  ? 86   ALA A N   1 
ATOM   541  C  CA  . ALA A 1 65  ? -24.887 -44.189 -37.596 1.00 26.47  ? 86   ALA A CA  1 
ATOM   542  C  C   . ALA A 1 65  ? -25.400 -43.293 -38.754 1.00 24.81  ? 86   ALA A C   1 
ATOM   543  O  O   . ALA A 1 65  ? -26.306 -43.645 -39.530 1.00 24.90  ? 86   ALA A O   1 
ATOM   544  C  CB  . ALA A 1 65  ? -25.591 -43.767 -36.258 1.00 24.14  ? 86   ALA A CB  1 
ATOM   545  N  N   . THR A 1 66  ? -24.814 -42.113 -38.870 1.00 18.98  ? 87   THR A N   1 
ATOM   546  C  CA  . THR A 1 66  ? -25.160 -41.209 -39.930 1.00 23.06  ? 87   THR A CA  1 
ATOM   547  C  C   . THR A 1 66  ? -24.854 -41.842 -41.302 1.00 25.20  ? 87   THR A C   1 
ATOM   548  O  O   . THR A 1 66  ? -25.705 -41.820 -42.202 1.00 21.75  ? 87   THR A O   1 
ATOM   549  C  CB  . THR A 1 66  ? -24.373 -39.862 -39.776 1.00 20.57  ? 87   THR A CB  1 
ATOM   550  O  OG1 . THR A 1 66  ? -24.994 -39.114 -38.738 1.00 25.30  ? 87   THR A OG1 1 
ATOM   551  C  CG2 . THR A 1 66  ? -24.397 -39.010 -41.087 1.00 22.00  ? 87   THR A CG2 1 
ATOM   552  N  N   . TRP A 1 67  ? -23.642 -42.386 -41.467 1.00 22.49  ? 88   TRP A N   1 
ATOM   553  C  CA  . TRP A 1 67  ? -23.291 -42.916 -42.759 1.00 21.78  ? 88   TRP A CA  1 
ATOM   554  C  C   . TRP A 1 67  ? -24.098 -44.184 -43.109 1.00 25.38  ? 88   TRP A C   1 
ATOM   555  O  O   . TRP A 1 67  ? -24.426 -44.422 -44.281 1.00 24.14  ? 88   TRP A O   1 
ATOM   556  C  CB  . TRP A 1 67  ? -21.781 -43.170 -42.830 1.00 20.83  ? 88   TRP A CB  1 
ATOM   557  C  CG  . TRP A 1 67  ? -21.145 -41.825 -43.103 1.00 29.43  ? 88   TRP A CG  1 
ATOM   558  C  CD1 . TRP A 1 67  ? -20.526 -40.985 -42.182 1.00 28.10  ? 88   TRP A CD1 1 
ATOM   559  C  CD2 . TRP A 1 67  ? -21.164 -41.109 -44.353 1.00 26.69  ? 88   TRP A CD2 1 
ATOM   560  N  NE1 . TRP A 1 67  ? -20.086 -39.827 -42.827 1.00 29.20  ? 88   TRP A NE1 1 
ATOM   561  C  CE2 . TRP A 1 67  ? -20.481 -39.874 -44.145 1.00 28.86  ? 88   TRP A CE2 1 
ATOM   562  C  CE3 . TRP A 1 67  ? -21.666 -41.406 -45.640 1.00 24.05  ? 88   TRP A CE3 1 
ATOM   563  C  CZ2 . TRP A 1 67  ? -20.290 -38.915 -45.181 1.00 29.82  ? 88   TRP A CZ2 1 
ATOM   564  C  CZ3 . TRP A 1 67  ? -21.447 -40.463 -46.685 1.00 27.12  ? 88   TRP A CZ3 1 
ATOM   565  C  CH2 . TRP A 1 67  ? -20.762 -39.236 -46.444 1.00 28.82  ? 88   TRP A CH2 1 
ATOM   566  N  N   . SER A 1 68  ? -24.453 -44.969 -42.098 1.00 23.31  ? 89   SER A N   1 
ATOM   567  C  CA  . SER A 1 68  ? -25.311 -46.162 -42.293 1.00 20.83  ? 89   SER A CA  1 
ATOM   568  C  C   . SER A 1 68  ? -26.650 -45.670 -42.808 1.00 22.71  ? 89   SER A C   1 
ATOM   569  O  O   . SER A 1 68  ? -27.211 -46.233 -43.731 1.00 23.78  ? 89   SER A O   1 
ATOM   570  C  CB  . SER A 1 68  ? -25.514 -46.930 -40.947 1.00 25.39  ? 89   SER A CB  1 
ATOM   571  O  OG  . SER A 1 68  ? -26.406 -48.053 -41.110 1.00 27.08  ? 89   SER A OG  1 
ATOM   572  N  N   . PHE A 1 69  ? -27.169 -44.636 -42.142 1.00 20.19  ? 90   PHE A N   1 
ATOM   573  C  CA  . PHE A 1 69  ? -28.470 -44.049 -42.538 1.00 24.66  ? 90   PHE A CA  1 
ATOM   574  C  C   . PHE A 1 69  ? -28.406 -43.498 -43.976 1.00 24.79  ? 90   PHE A C   1 
ATOM   575  O  O   . PHE A 1 69  ? -29.289 -43.795 -44.819 1.00 22.98  ? 90   PHE A O   1 
ATOM   576  C  CB  . PHE A 1 69  ? -28.900 -42.971 -41.530 1.00 19.81  ? 90   PHE A CB  1 
ATOM   577  C  CG  . PHE A 1 69  ? -30.190 -42.252 -41.957 1.00 20.83  ? 90   PHE A CG  1 
ATOM   578  C  CD1 . PHE A 1 69  ? -30.125 -41.091 -42.684 1.00 23.54  ? 90   PHE A CD1 1 
ATOM   579  C  CD2 . PHE A 1 69  ? -31.410 -42.772 -41.599 1.00 24.78  ? 90   PHE A CD2 1 
ATOM   580  C  CE1 . PHE A 1 69  ? -31.281 -40.442 -43.088 1.00 28.05  ? 90   PHE A CE1 1 
ATOM   581  C  CE2 . PHE A 1 69  ? -32.589 -42.140 -42.005 1.00 27.89  ? 90   PHE A CE2 1 
ATOM   582  C  CZ  . PHE A 1 69  ? -32.509 -40.997 -42.744 1.00 25.14  ? 90   PHE A CZ  1 
ATOM   583  N  N   . LEU A 1 70  ? -27.396 -42.679 -44.290 1.00 21.22  ? 91   LEU A N   1 
ATOM   584  C  CA  . LEU A 1 70  ? -27.282 -42.104 -45.647 1.00 21.37  ? 91   LEU A CA  1 
ATOM   585  C  C   . LEU A 1 70  ? -27.213 -43.172 -46.734 1.00 23.74  ? 91   LEU A C   1 
ATOM   586  O  O   . LEU A 1 70  ? -27.753 -42.981 -47.853 1.00 22.80  ? 91   LEU A O   1 
ATOM   587  C  CB  . LEU A 1 70  ? -26.025 -41.192 -45.792 1.00 20.16  ? 91   LEU A CB  1 
ATOM   588  C  CG  . LEU A 1 70  ? -26.081 -39.965 -44.839 1.00 25.79  ? 91   LEU A CG  1 
ATOM   589  C  CD1 . LEU A 1 70  ? -24.718 -39.229 -44.840 1.00 23.37  ? 91   LEU A CD1 1 
ATOM   590  C  CD2 . LEU A 1 70  ? -27.168 -38.958 -45.264 1.00 25.23  ? 91   LEU A CD2 1 
ATOM   591  N  N   . LYS A 1 71  ? -26.455 -44.241 -46.468 1.00 22.61  ? 92   LYS A N   1 
ATOM   592  C  CA  . LYS A 1 71  ? -26.347 -45.320 -47.463 1.00 21.20  ? 92   LYS A CA  1 
ATOM   593  C  C   . LYS A 1 71  ? -27.736 -45.911 -47.743 1.00 25.23  ? 92   LYS A C   1 
ATOM   594  O  O   . LYS A 1 71  ? -28.111 -46.182 -48.923 1.00 22.56  ? 92   LYS A O   1 
ATOM   595  C  CB  . LYS A 1 71  ? -25.406 -46.414 -46.952 1.00 21.30  ? 92   LYS A CB  1 
ATOM   596  C  CG  . LYS A 1 71  ? -25.352 -47.638 -47.842 1.00 23.79  ? 92   LYS A CG  1 
ATOM   597  C  CD  . LYS A 1 71  ? -24.301 -48.673 -47.275 1.00 36.04  ? 92   LYS A CD  1 
ATOM   598  C  CE  . LYS A 1 71  ? -24.316 -49.957 -48.092 1.00 45.28  ? 92   LYS A CE  1 
ATOM   599  N  NZ  . LYS A 1 71  ? -23.166 -50.838 -47.701 1.00 57.58  ? 92   LYS A NZ  1 
ATOM   600  N  N   . ASP A 1 72  ? -28.501 -46.117 -46.674 1.00 21.98  ? 93   ASP A N   1 
ATOM   601  C  CA  . ASP A 1 72  ? -29.849 -46.775 -46.848 1.00 24.80  ? 93   ASP A CA  1 
ATOM   602  C  C   . ASP A 1 72  ? -30.861 -45.820 -47.458 1.00 23.76  ? 93   ASP A C   1 
ATOM   603  O  O   . ASP A 1 72  ? -31.694 -46.216 -48.285 1.00 22.50  ? 93   ASP A O   1 
ATOM   604  C  CB  . ASP A 1 72  ? -30.395 -47.347 -45.490 1.00 23.02  ? 93   ASP A CB  1 
ATOM   605  C  CG  . ASP A 1 72  ? -30.731 -48.830 -45.566 1.00 29.72  ? 93   ASP A CG  1 
ATOM   606  O  OD1 . ASP A 1 72  ? -30.613 -49.458 -46.664 1.00 29.08  ? 93   ASP A OD1 1 
ATOM   607  O  OD2 . ASP A 1 72  ? -31.118 -49.412 -44.520 1.00 26.01  ? 93   ASP A OD2 1 
ATOM   608  N  N   . LEU A 1 73  ? -30.784 -44.550 -47.109 1.00 20.86  ? 94   LEU A N   1 
ATOM   609  C  CA  . LEU A 1 73  ? -31.649 -43.556 -47.755 1.00 22.65  ? 94   LEU A CA  1 
ATOM   610  C  C   . LEU A 1 73  ? -31.355 -43.467 -49.283 1.00 24.14  ? 94   LEU A C   1 
ATOM   611  O  O   . LEU A 1 73  ? -32.265 -43.364 -50.126 1.00 25.38  ? 94   LEU A O   1 
ATOM   612  C  CB  . LEU A 1 73  ? -31.440 -42.167 -47.119 1.00 22.20  ? 94   LEU A CB  1 
ATOM   613  C  CG  . LEU A 1 73  ? -32.452 -41.070 -47.559 1.00 26.53  ? 94   LEU A CG  1 
ATOM   614  C  CD1 . LEU A 1 73  ? -33.802 -41.367 -46.906 1.00 25.50  ? 94   LEU A CD1 1 
ATOM   615  C  CD2 . LEU A 1 73  ? -32.000 -39.646 -47.157 1.00 26.50  ? 94   LEU A CD2 1 
ATOM   616  N  N   . LYS A 1 74  ? -30.066 -43.499 -49.653 1.00 23.21  ? 95   LYS A N   1 
ATOM   617  C  CA  . LYS A 1 74  ? -29.711 -43.413 -51.072 1.00 21.76  ? 95   LYS A CA  1 
ATOM   618  C  C   . LYS A 1 74  ? -30.171 -44.710 -51.773 1.00 23.78  ? 95   LYS A C   1 
ATOM   619  O  O   . LYS A 1 74  ? -30.596 -44.692 -52.925 1.00 22.98  ? 95   LYS A O   1 
ATOM   620  C  CB  . LYS A 1 74  ? -28.189 -43.208 -51.280 1.00 22.84  ? 95   LYS A CB  1 
ATOM   621  C  CG  . LYS A 1 74  ? -27.730 -43.058 -52.741 1.00 24.97  ? 95   LYS A CG  1 
ATOM   622  C  CD  . LYS A 1 74  ? -28.396 -41.752 -53.312 1.00 32.66  ? 95   LYS A CD  1 
ATOM   623  C  CE  . LYS A 1 74  ? -27.758 -41.290 -54.633 1.00 40.80  ? 95   LYS A CE  1 
ATOM   624  N  NZ  . LYS A 1 74  ? -28.421 -40.013 -54.964 1.00 38.80  ? 95   LYS A NZ  1 
ATOM   625  N  N   . ARG A 1 75  ? -30.052 -45.834 -51.080 1.00 23.35  ? 96   ARG A N   1 
ATOM   626  C  CA  . ARG A 1 75  ? -30.466 -47.089 -51.699 1.00 22.40  ? 96   ARG A CA  1 
ATOM   627  C  C   . ARG A 1 75  ? -31.923 -46.981 -52.117 1.00 26.23  ? 96   ARG A C   1 
ATOM   628  O  O   . ARG A 1 75  ? -32.316 -47.390 -53.217 1.00 25.02  ? 96   ARG A O   1 
ATOM   629  C  CB  . ARG A 1 75  ? -30.286 -48.238 -50.709 1.00 21.26  ? 96   ARG A CB  1 
ATOM   630  C  CG  . ARG A 1 75  ? -30.754 -49.623 -51.278 1.00 25.66  ? 96   ARG A CG  1 
ATOM   631  C  CD  . ARG A 1 75  ? -30.649 -50.725 -50.178 1.00 27.25  ? 96   ARG A CD  1 
ATOM   632  N  NE  . ARG A 1 75  ? -31.617 -50.482 -49.085 1.00 26.52  ? 96   ARG A NE  1 
ATOM   633  C  CZ  . ARG A 1 75  ? -32.906 -50.826 -49.145 1.00 33.00  ? 96   ARG A CZ  1 
ATOM   634  N  NH1 . ARG A 1 75  ? -33.714 -50.569 -48.116 1.00 30.57  ? 96   ARG A NH1 1 
ATOM   635  N  NH2 . ARG A 1 75  ? -33.406 -51.400 -50.256 1.00 26.01  ? 96   ARG A NH2 1 
ATOM   636  N  N   . ILE A 1 76  ? -32.705 -46.411 -51.205 1.00 21.50  ? 97   ILE A N   1 
ATOM   637  C  CA  . ILE A 1 76  ? -34.160 -46.209 -51.427 1.00 24.96  ? 97   ILE A CA  1 
ATOM   638  C  C   . ILE A 1 76  ? -34.428 -45.280 -52.599 1.00 21.20  ? 97   ILE A C   1 
ATOM   639  O  O   . ILE A 1 76  ? -35.273 -45.577 -53.484 1.00 24.79  ? 97   ILE A O   1 
ATOM   640  C  CB  . ILE A 1 76  ? -34.821 -45.585 -50.120 1.00 34.64  ? 97   ILE A CB  1 
ATOM   641  C  CG1 . ILE A 1 76  ? -34.916 -46.599 -48.982 1.00 39.58  ? 97   ILE A CG1 1 
ATOM   642  C  CG2 . ILE A 1 76  ? -36.125 -44.913 -50.413 1.00 36.13  ? 97   ILE A CG2 1 
ATOM   643  C  CD1 . ILE A 1 76  ? -35.798 -47.711 -49.239 1.00 38.92  ? 97   ILE A CD1 1 
ATOM   644  N  N   . THR A 1 77  ? -33.677 -44.175 -52.710 1.00 22.96  ? 98   THR A N   1 
ATOM   645  C  CA  . THR A 1 77  ? -33.974 -43.260 -53.792 1.00 23.67  ? 98   THR A CA  1 
ATOM   646  C  C   . THR A 1 77  ? -33.435 -43.766 -55.117 1.00 25.89  ? 98   THR A C   1 
ATOM   647  O  O   . THR A 1 77  ? -34.007 -43.496 -56.178 1.00 24.83  ? 98   THR A O   1 
ATOM   648  C  CB  . THR A 1 77  ? -33.445 -41.810 -53.519 1.00 29.77  ? 98   THR A CB  1 
ATOM   649  O  OG1 . THR A 1 77  ? -32.053 -41.812 -53.290 1.00 30.79  ? 98   THR A OG1 1 
ATOM   650  C  CG2 . THR A 1 77  ? -34.102 -41.251 -52.267 1.00 32.11  ? 98   THR A CG2 1 
ATOM   651  N  N   . ASP A 1 78  ? -32.382 -44.577 -55.059 1.00 22.12  ? 99   ASP A N   1 
ATOM   652  C  CA  . ASP A 1 78  ? -31.874 -45.200 -56.273 1.00 25.49  ? 99   ASP A CA  1 
ATOM   653  C  C   . ASP A 1 78  ? -32.771 -46.350 -56.754 1.00 25.05  ? 99   ASP A C   1 
ATOM   654  O  O   . ASP A 1 78  ? -32.614 -46.829 -57.874 1.00 25.84  ? 99   ASP A O   1 
ATOM   655  C  CB  . ASP A 1 78  ? -30.457 -45.769 -56.061 1.00 26.53  ? 99   ASP A CB  1 
ATOM   656  C  CG  . ASP A 1 78  ? -29.384 -44.728 -56.115 1.00 36.86  ? 99   ASP A CG  1 
ATOM   657  O  OD1 . ASP A 1 78  ? -29.629 -43.556 -56.506 1.00 31.79  ? 99   ASP A OD1 1 
ATOM   658  O  OD2 . ASP A 1 78  ? -28.271 -45.122 -55.750 1.00 32.46  ? 99   ASP A OD2 1 
ATOM   659  N  N   . SER A 1 79  ? -33.672 -46.826 -55.898 1.00 24.09  ? 100  SER A N   1 
ATOM   660  C  CA  . SER A 1 79  ? -34.458 -48.023 -56.225 1.00 26.95  ? 100  SER A CA  1 
ATOM   661  C  C   . SER A 1 79  ? -35.523 -47.759 -57.268 1.00 29.87  ? 100  SER A C   1 
ATOM   662  O  O   . SER A 1 79  ? -35.810 -46.595 -57.586 1.00 27.47  ? 100  SER A O   1 
ATOM   663  C  CB  . SER A 1 79  ? -35.166 -48.594 -54.985 1.00 22.55  ? 100  SER A CB  1 
ATOM   664  O  OG  . SER A 1 79  ? -36.259 -47.738 -54.643 1.00 23.60  ? 100  SER A OG  1 
ATOM   665  N  N   A ASP A 1 80  ? -36.113 -48.843 -57.779 0.53 24.36  ? 101  ASP A N   1 
ATOM   666  N  N   B ASP A 1 80  ? -36.131 -48.828 -57.774 0.47 24.34  ? 101  ASP A N   1 
ATOM   667  C  CA  A ASP A 1 80  ? -37.218 -48.758 -58.727 0.53 29.06  ? 101  ASP A CA  1 
ATOM   668  C  CA  B ASP A 1 80  ? -37.219 -48.687 -58.728 0.47 28.30  ? 101  ASP A CA  1 
ATOM   669  C  C   A ASP A 1 80  ? -38.566 -48.842 -58.010 0.53 27.84  ? 101  ASP A C   1 
ATOM   670  C  C   B ASP A 1 80  ? -38.565 -48.553 -58.030 0.47 28.91  ? 101  ASP A C   1 
ATOM   671  O  O   A ASP A 1 80  ? -39.612 -49.084 -58.637 0.53 27.06  ? 101  ASP A O   1 
ATOM   672  O  O   B ASP A 1 80  ? -39.597 -48.361 -58.693 0.47 24.48  ? 101  ASP A O   1 
ATOM   673  C  CB  A ASP A 1 80  ? -37.123 -49.876 -59.780 0.53 34.15  ? 101  ASP A CB  1 
ATOM   674  C  CB  B ASP A 1 80  ? -37.245 -49.883 -59.692 0.47 33.41  ? 101  ASP A CB  1 
ATOM   675  C  CG  A ASP A 1 80  ? -37.135 -51.266 -59.160 0.53 44.19  ? 101  ASP A CG  1 
ATOM   676  C  CG  B ASP A 1 80  ? -36.023 -49.935 -60.557 0.47 37.42  ? 101  ASP A CG  1 
ATOM   677  O  OD1 A ASP A 1 80  ? -36.892 -51.403 -57.929 0.53 48.51  ? 101  ASP A OD1 1 
ATOM   678  O  OD1 B ASP A 1 80  ? -35.607 -48.834 -60.983 0.47 33.80  ? 101  ASP A OD1 1 
ATOM   679  O  OD2 A ASP A 1 80  ? -37.374 -52.232 -59.916 0.53 50.96  ? 101  ASP A OD2 1 
ATOM   680  O  OD2 B ASP A 1 80  ? -35.508 -51.053 -60.813 0.47 42.48  ? 101  ASP A OD2 1 
ATOM   681  N  N   . LEU A 1 81  ? -38.560 -48.638 -56.704 1.00 25.92  ? 102  LEU A N   1 
ATOM   682  C  CA  . LEU A 1 81  ? -39.818 -48.719 -55.953 1.00 26.48  ? 102  LEU A CA  1 
ATOM   683  C  C   . LEU A 1 81  ? -40.698 -47.505 -56.124 1.00 25.15  ? 102  LEU A C   1 
ATOM   684  O  O   . LEU A 1 81  ? -40.220 -46.368 -56.060 1.00 25.23  ? 102  LEU A O   1 
ATOM   685  C  CB  . LEU A 1 81  ? -39.553 -48.921 -54.455 1.00 23.01  ? 102  LEU A CB  1 
ATOM   686  C  CG  . LEU A 1 81  ? -38.745 -50.162 -54.124 1.00 27.15  ? 102  LEU A CG  1 
ATOM   687  C  CD1 . LEU A 1 81  ? -38.455 -50.225 -52.625 1.00 26.13  ? 102  LEU A CD1 1 
ATOM   688  C  CD2 . LEU A 1 81  ? -39.495 -51.408 -54.633 1.00 30.81  ? 102  LEU A CD2 1 
ATOM   689  N  N   . LYS A 1 82  ? -42.005 -47.743 -56.261 1.00 21.73  ? 103  LYS A N   1 
ATOM   690  C  CA  . LYS A 1 82  ? -42.910 -46.598 -56.344 1.00 21.97  ? 103  LYS A CA  1 
ATOM   691  C  C   . LYS A 1 82  ? -44.105 -46.818 -55.438 1.00 21.45  ? 103  LYS A C   1 
ATOM   692  O  O   . LYS A 1 82  ? -44.354 -47.929 -54.958 1.00 24.66  ? 103  LYS A O   1 
ATOM   693  C  CB  . LYS A 1 82  ? -43.373 -46.364 -57.818 1.00 27.84  ? 103  LYS A CB  1 
ATOM   694  C  CG  . LYS A 1 82  ? -42.211 -45.866 -58.787 1.00 34.83  ? 103  LYS A CG  1 
ATOM   695  C  CD  . LYS A 1 82  ? -42.793 -45.360 -60.121 1.00 48.31  ? 103  LYS A CD  1 
ATOM   696  C  CE  . LYS A 1 82  ? -41.687 -44.944 -61.091 1.00 53.17  ? 103  LYS A CE  1 
ATOM   697  N  N   . GLY A 1 83  ? -44.861 -45.740 -55.189 1.00 23.60  ? 104  GLY A N   1 
ATOM   698  C  CA  . GLY A 1 83  ? -46.179 -45.934 -54.575 1.00 23.98  ? 104  GLY A CA  1 
ATOM   699  C  C   . GLY A 1 83  ? -46.145 -46.549 -53.162 1.00 24.79  ? 104  GLY A C   1 
ATOM   700  O  O   . GLY A 1 83  ? -45.239 -46.295 -52.384 1.00 24.53  ? 104  GLY A O   1 
ATOM   701  N  N   . GLU A 1 84  ? -47.130 -47.397 -52.870 1.00 24.22  ? 105  GLU A N   1 
ATOM   702  C  CA  . GLU A 1 84  ? -47.161 -48.064 -51.602 1.00 24.02  ? 105  GLU A CA  1 
ATOM   703  C  C   . GLU A 1 84  ? -45.963 -48.945 -51.300 1.00 22.35  ? 105  GLU A C   1 
ATOM   704  O  O   . GLU A 1 84  ? -45.534 -48.992 -50.132 1.00 23.16  ? 105  GLU A O   1 
ATOM   705  C  CB  . GLU A 1 84  ? -48.413 -48.916 -51.509 1.00 23.48  ? 105  GLU A CB  1 
ATOM   706  C  CG  . GLU A 1 84  ? -49.653 -48.002 -51.290 1.00 33.20  ? 105  GLU A CG  1 
ATOM   707  C  CD  . GLU A 1 84  ? -50.809 -48.927 -51.027 1.00 41.90  ? 105  GLU A CD  1 
ATOM   708  O  OE1 . GLU A 1 84  ? -51.352 -49.375 -52.043 1.00 33.02  ? 105  GLU A OE1 1 
ATOM   709  O  OE2 . GLU A 1 84  ? -51.081 -49.255 -49.843 1.00 46.64  ? 105  GLU A OE2 1 
ATOM   710  N  N   . LEU A 1 85  ? -45.442 -49.650 -52.310 1.00 22.77  ? 106  LEU A N   1 
ATOM   711  C  CA  . LEU A 1 85  ? -44.230 -50.424 -52.069 1.00 26.52  ? 106  LEU A CA  1 
ATOM   712  C  C   . LEU A 1 85  ? -43.057 -49.543 -51.626 1.00 22.28  ? 106  LEU A C   1 
ATOM   713  O  O   . LEU A 1 85  ? -42.244 -49.932 -50.743 1.00 24.21  ? 106  LEU A O   1 
ATOM   714  C  CB  . LEU A 1 85  ? -43.855 -51.218 -53.326 1.00 25.57  ? 106  LEU A CB  1 
ATOM   715  C  CG  . LEU A 1 85  ? -44.706 -52.474 -53.468 1.00 31.56  ? 106  LEU A CG  1 
ATOM   716  C  CD1 . LEU A 1 85  ? -44.360 -53.130 -54.845 1.00 30.06  ? 106  LEU A CD1 1 
ATOM   717  C  CD2 . LEU A 1 85  ? -44.406 -53.470 -52.312 1.00 29.42  ? 106  LEU A CD2 1 
ATOM   718  N  N   . PHE A 1 86  ? -42.939 -48.370 -52.242 1.00 21.90  ? 107  PHE A N   1 
ATOM   719  C  CA  . PHE A 1 86  ? -41.906 -47.411 -51.844 1.00 22.04  ? 107  PHE A CA  1 
ATOM   720  C  C   . PHE A 1 86  ? -42.090 -46.959 -50.424 1.00 21.51  ? 107  PHE A C   1 
ATOM   721  O  O   . PHE A 1 86  ? -41.157 -46.902 -49.631 1.00 23.04  ? 107  PHE A O   1 
ATOM   722  C  CB  . PHE A 1 86  ? -41.929 -46.175 -52.768 1.00 23.89  ? 107  PHE A CB  1 
ATOM   723  C  CG  . PHE A 1 86  ? -40.938 -45.111 -52.390 1.00 26.18  ? 107  PHE A CG  1 
ATOM   724  C  CD1 . PHE A 1 86  ? -39.596 -45.187 -52.816 1.00 24.59  ? 107  PHE A CD1 1 
ATOM   725  C  CD2 . PHE A 1 86  ? -41.352 -43.975 -51.686 1.00 26.36  ? 107  PHE A CD2 1 
ATOM   726  C  CE1 . PHE A 1 86  ? -38.634 -44.163 -52.508 1.00 23.31  ? 107  PHE A CE1 1 
ATOM   727  C  CE2 . PHE A 1 86  ? -40.454 -42.964 -51.366 1.00 24.52  ? 107  PHE A CE2 1 
ATOM   728  C  CZ  . PHE A 1 86  ? -39.079 -43.014 -51.769 1.00 26.60  ? 107  PHE A CZ  1 
ATOM   729  N  N   . ILE A 1 87  ? -43.323 -46.586 -50.091 1.00 19.82  ? 108  ILE A N   1 
ATOM   730  C  CA  . ILE A 1 87  ? -43.581 -46.131 -48.721 1.00 20.41  ? 108  ILE A CA  1 
ATOM   731  C  C   . ILE A 1 87  ? -43.320 -47.238 -47.694 1.00 21.52  ? 108  ILE A C   1 
ATOM   732  O  O   . ILE A 1 87  ? -42.780 -46.968 -46.605 1.00 25.12  ? 108  ILE A O   1 
ATOM   733  C  CB  . ILE A 1 87  ? -45.078 -45.622 -48.554 1.00 21.18  ? 108  ILE A CB  1 
ATOM   734  C  CG1 . ILE A 1 87  ? -45.230 -44.350 -49.430 1.00 23.35  ? 108  ILE A CG1 1 
ATOM   735  C  CG2 . ILE A 1 87  ? -45.328 -45.160 -47.075 1.00 25.74  ? 108  ILE A CG2 1 
ATOM   736  C  CD1 . ILE A 1 87  ? -46.698 -43.846 -49.583 1.00 26.97  ? 108  ILE A CD1 1 
ATOM   737  N  N   . LYS A 1 88  ? -43.755 -48.454 -48.027 1.00 24.37  ? 109  LYS A N   1 
ATOM   738  C  CA  . LYS A 1 88  ? -43.565 -49.594 -47.116 1.00 26.40  ? 109  LYS A CA  1 
ATOM   739  C  C   . LYS A 1 88  ? -42.071 -49.816 -46.852 1.00 24.47  ? 109  LYS A C   1 
ATOM   740  O  O   . LYS A 1 88  ? -41.612 -49.943 -45.697 1.00 26.48  ? 109  LYS A O   1 
ATOM   741  C  CB  . LYS A 1 88  ? -44.192 -50.846 -47.720 1.00 22.63  ? 109  LYS A CB  1 
ATOM   742  C  CG  . LYS A 1 88  ? -44.215 -52.045 -46.756 1.00 27.36  ? 109  LYS A CG  1 
ATOM   743  C  CD  . LYS A 1 88  ? -44.757 -53.352 -47.416 1.00 42.15  ? 109  LYS A CD  1 
ATOM   744  C  CE  . LYS A 1 88  ? -46.188 -53.634 -46.986 1.00 58.57  ? 109  LYS A CE  1 
ATOM   745  N  NZ  . LYS A 1 88  ? -46.294 -53.904 -45.512 1.00 61.71  ? 109  LYS A NZ  1 
ATOM   746  N  N   . GLU A 1 89  ? -41.302 -49.845 -47.934 1.00 21.91  ? 110  GLU A N   1 
ATOM   747  C  CA  . GLU A 1 89  ? -39.859 -50.084 -47.773 1.00 24.41  ? 110  GLU A CA  1 
ATOM   748  C  C   . GLU A 1 89  ? -39.196 -48.883 -47.084 1.00 25.25  ? 110  GLU A C   1 
ATOM   749  O  O   . GLU A 1 89  ? -38.273 -49.066 -46.330 1.00 22.92  ? 110  GLU A O   1 
ATOM   750  C  CB  . GLU A 1 89  ? -39.177 -50.368 -49.135 1.00 23.49  ? 110  GLU A CB  1 
ATOM   751  C  CG  . GLU A 1 89  ? -37.644 -50.596 -49.040 1.00 25.48  ? 110  GLU A CG  1 
ATOM   752  C  CD  . GLU A 1 89  ? -37.235 -51.804 -48.157 1.00 31.12  ? 110  GLU A CD  1 
ATOM   753  O  OE1 . GLU A 1 89  ? -38.092 -52.656 -47.823 1.00 33.60  ? 110  GLU A OE1 1 
ATOM   754  O  OE2 . GLU A 1 89  ? -36.042 -51.919 -47.874 1.00 29.66  ? 110  GLU A OE2 1 
ATOM   755  N  N   . LEU A 1 90  ? -39.632 -47.660 -47.375 1.00 21.11  ? 111  LEU A N   1 
ATOM   756  C  CA  . LEU A 1 90  ? -39.099 -46.515 -46.670 1.00 21.26  ? 111  LEU A CA  1 
ATOM   757  C  C   . LEU A 1 90  ? -39.276 -46.624 -45.167 1.00 22.71  ? 111  LEU A C   1 
ATOM   758  O  O   . LEU A 1 90  ? -38.347 -46.351 -44.408 1.00 23.73  ? 111  LEU A O   1 
ATOM   759  C  CB  . LEU A 1 90  ? -39.776 -45.258 -47.196 1.00 21.88  ? 111  LEU A CB  1 
ATOM   760  C  CG  . LEU A 1 90  ? -39.415 -43.964 -46.479 1.00 23.32  ? 111  LEU A CG  1 
ATOM   761  C  CD1 . LEU A 1 90  ? -37.918 -43.580 -46.658 1.00 21.57  ? 111  LEU A CD1 1 
ATOM   762  C  CD2 . LEU A 1 90  ? -40.298 -42.829 -47.153 1.00 24.21  ? 111  LEU A CD2 1 
ATOM   763  N  N   . LEU A 1 91  ? -40.471 -46.997 -44.705 1.00 22.66  ? 112  LEU A N   1 
ATOM   764  C  CA  . LEU A 1 91  ? -40.716 -47.088 -43.269 1.00 24.00  ? 112  LEU A CA  1 
ATOM   765  C  C   . LEU A 1 91  ? -39.869 -48.240 -42.710 1.00 23.13  ? 112  LEU A C   1 
ATOM   766  O  O   . LEU A 1 91  ? -39.308 -48.163 -41.617 1.00 23.25  ? 112  LEU A O   1 
ATOM   767  C  CB  . LEU A 1 91  ? -42.193 -47.331 -42.961 1.00 22.22  ? 112  LEU A CB  1 
ATOM   768  C  CG  . LEU A 1 91  ? -42.567 -47.565 -41.498 1.00 29.78  ? 112  LEU A CG  1 
ATOM   769  C  CD1 . LEU A 1 91  ? -42.049 -46.446 -40.598 1.00 32.00  ? 112  LEU A CD1 1 
ATOM   770  C  CD2 . LEU A 1 91  ? -44.094 -47.700 -41.393 1.00 35.89  ? 112  LEU A CD2 1 
ATOM   771  N  N   . TRP A 1 92  ? -39.812 -49.344 -43.433 1.00 21.60  ? 113  TRP A N   1 
ATOM   772  C  CA  . TRP A 1 92  ? -39.024 -50.485 -42.932 1.00 22.68  ? 113  TRP A CA  1 
ATOM   773  C  C   . TRP A 1 92  ? -37.530 -50.139 -42.856 1.00 22.42  ? 113  TRP A C   1 
ATOM   774  O  O   . TRP A 1 92  ? -36.825 -50.575 -41.938 1.00 22.99  ? 113  TRP A O   1 
ATOM   775  C  CB  . TRP A 1 92  ? -39.224 -51.658 -43.891 1.00 28.20  ? 113  TRP A CB  1 
ATOM   776  C  CG  . TRP A 1 92  ? -40.368 -52.525 -43.579 1.00 28.11  ? 113  TRP A CG  1 
ATOM   777  C  CD1 . TRP A 1 92  ? -41.049 -52.609 -42.383 1.00 39.56  ? 113  TRP A CD1 1 
ATOM   778  C  CD2 . TRP A 1 92  ? -40.871 -53.590 -44.415 1.00 31.63  ? 113  TRP A CD2 1 
ATOM   779  N  NE1 . TRP A 1 92  ? -41.963 -53.667 -42.443 1.00 42.90  ? 113  TRP A NE1 1 
ATOM   780  C  CE2 . TRP A 1 92  ? -41.866 -54.277 -43.672 1.00 42.49  ? 113  TRP A CE2 1 
ATOM   781  C  CE3 . TRP A 1 92  ? -40.562 -54.035 -45.710 1.00 36.77  ? 113  TRP A CE3 1 
ATOM   782  C  CZ2 . TRP A 1 92  ? -42.586 -55.357 -44.203 1.00 47.41  ? 113  TRP A CZ2 1 
ATOM   783  C  CZ3 . TRP A 1 92  ? -41.264 -55.147 -46.221 1.00 30.73  ? 113  TRP A CZ3 1 
ATOM   784  C  CH2 . TRP A 1 92  ? -42.263 -55.780 -45.465 1.00 41.40  ? 113  TRP A CH2 1 
ATOM   785  N  N   . MET A 1 93  ? -37.055 -49.369 -43.840 1.00 22.76  ? 114  MET A N   1 
ATOM   786  C  CA  . MET A 1 93  ? -35.673 -48.920 -43.849 1.00 23.34  ? 114  MET A CA  1 
ATOM   787  C  C   . MET A 1 93  ? -35.428 -48.051 -42.603 1.00 25.59  ? 114  MET A C   1 
ATOM   788  O  O   . MET A 1 93  ? -34.403 -48.159 -41.923 1.00 23.44  ? 114  MET A O   1 
ATOM   789  C  CB  . MET A 1 93  ? -35.337 -48.174 -45.144 1.00 20.94  ? 114  MET A CB  1 
ATOM   790  C  CG  . MET A 1 93  ? -33.863 -47.630 -45.187 1.00 22.64  ? 114  MET A CG  1 
ATOM   791  S  SD  . MET A 1 93  ? -33.711 -46.061 -44.278 1.00 25.56  ? 114  MET A SD  1 
ATOM   792  C  CE  . MET A 1 93  ? -34.512 -45.021 -45.510 1.00 26.18  ? 114  MET A CE  1 
ATOM   793  N  N   . LEU A 1 94  ? -36.355 -47.166 -42.297 1.00 22.03  ? 115  LEU A N   1 
ATOM   794  C  CA  . LEU A 1 94  ? -36.131 -46.283 -41.146 1.00 21.83  ? 115  LEU A CA  1 
ATOM   795  C  C   . LEU A 1 94  ? -36.117 -47.104 -39.842 1.00 26.26  ? 115  LEU A C   1 
ATOM   796  O  O   . LEU A 1 94  ? -35.369 -46.799 -38.896 1.00 25.34  ? 115  LEU A O   1 
ATOM   797  C  CB  . LEU A 1 94  ? -37.227 -45.209 -41.086 1.00 21.57  ? 115  LEU A CB  1 
ATOM   798  C  CG  . LEU A 1 94  ? -37.139 -44.231 -42.276 1.00 28.41  ? 115  LEU A CG  1 
ATOM   799  C  CD1 . LEU A 1 94  ? -38.481 -43.513 -42.362 1.00 27.45  ? 115  LEU A CD1 1 
ATOM   800  C  CD2 . LEU A 1 94  ? -35.995 -43.226 -42.063 1.00 30.48  ? 115  LEU A CD2 1 
ATOM   801  N  N   . ARG A 1 95  ? -36.983 -48.129 -39.774 1.00 22.50  ? 116  ARG A N   1 
ATOM   802  C  CA  . ARG A 1 95  ? -37.022 -48.984 -38.577 1.00 24.12  ? 116  ARG A CA  1 
ATOM   803  C  C   . ARG A 1 95  ? -35.730 -49.799 -38.483 1.00 24.22  ? 116  ARG A C   1 
ATOM   804  O  O   . ARG A 1 95  ? -35.210 -50.033 -37.397 1.00 25.51  ? 116  ARG A O   1 
ATOM   805  C  CB  . ARG A 1 95  ? -38.217 -49.927 -38.609 1.00 25.64  ? 116  ARG A CB  1 
ATOM   806  C  CG  . ARG A 1 95  ? -39.592 -49.198 -38.501 1.00 38.11  ? 116  ARG A CG  1 
ATOM   807  C  CD  . ARG A 1 95  ? -39.840 -48.633 -37.170 1.00 48.37  ? 116  ARG A CD  1 
ATOM   808  N  NE  . ARG A 1 95  ? -40.955 -47.674 -37.115 1.00 54.40  ? 116  ARG A NE  1 
ATOM   809  C  CZ  . ARG A 1 95  ? -42.255 -47.978 -37.098 1.00 53.92  ? 116  ARG A CZ  1 
ATOM   810  N  NH1 . ARG A 1 95  ? -42.655 -49.244 -37.177 1.00 57.33  ? 116  ARG A NH1 1 
ATOM   811  N  NH2 . ARG A 1 95  ? -43.166 -46.997 -37.012 1.00 47.30  ? 116  ARG A NH2 1 
ATOM   812  N  N   . HIS A 1 96  ? -35.258 -50.279 -39.620 1.00 23.72  ? 117  HIS A N   1 
ATOM   813  C  CA  . HIS A 1 96  ? -34.001 -51.007 -39.654 1.00 24.36  ? 117  HIS A CA  1 
ATOM   814  C  C   . HIS A 1 96  ? -32.816 -50.114 -39.215 1.00 23.47  ? 117  HIS A C   1 
ATOM   815  O  O   . HIS A 1 96  ? -31.909 -50.520 -38.450 1.00 24.69  ? 117  HIS A O   1 
ATOM   816  C  CB  . HIS A 1 96  ? -33.764 -51.535 -41.086 1.00 24.57  ? 117  HIS A CB  1 
ATOM   817  C  CG  . HIS A 1 96  ? -32.432 -52.209 -41.241 1.00 27.77  ? 117  HIS A CG  1 
ATOM   818  N  ND1 . HIS A 1 96  ? -32.014 -53.243 -40.410 1.00 30.05  ? 117  HIS A ND1 1 
ATOM   819  C  CD2 . HIS A 1 96  ? -31.398 -51.954 -42.072 1.00 30.94  ? 117  HIS A CD2 1 
ATOM   820  C  CE1 . HIS A 1 96  ? -30.793 -53.609 -40.751 1.00 34.69  ? 117  HIS A CE1 1 
ATOM   821  N  NE2 . HIS A 1 96  ? -30.395 -52.845 -41.751 1.00 37.80  ? 117  HIS A NE2 1 
ATOM   822  N  N   . GLN A 1 97  ? -32.796 -48.897 -39.727 1.00 22.19  ? 118  GLN A N   1 
ATOM   823  C  CA  . GLN A 1 97  ? -31.690 -47.997 -39.327 1.00 24.68  ? 118  GLN A CA  1 
ATOM   824  C  C   . GLN A 1 97  ? -31.750 -47.660 -37.834 1.00 25.10  ? 118  GLN A C   1 
ATOM   825  O  O   . GLN A 1 97  ? -30.734 -47.445 -37.183 1.00 25.76  ? 118  GLN A O   1 
ATOM   826  C  CB  . GLN A 1 97  ? -31.715 -46.723 -40.191 1.00 21.76  ? 118  GLN A CB  1 
ATOM   827  C  CG  . GLN A 1 97  ? -31.115 -46.999 -41.607 1.00 24.57  ? 118  GLN A CG  1 
ATOM   828  C  CD  . GLN A 1 97  ? -29.712 -47.554 -41.558 1.00 25.98  ? 118  GLN A CD  1 
ATOM   829  O  OE1 . GLN A 1 97  ? -28.882 -47.124 -40.759 1.00 26.35  ? 118  GLN A OE1 1 
ATOM   830  N  NE2 . GLN A 1 97  ? -29.449 -48.546 -42.371 1.00 23.74  ? 118  GLN A NE2 1 
ATOM   831  N  N   . LYS A 1 98  ? -32.963 -47.560 -37.293 1.00 24.29  ? 119  LYS A N   1 
ATOM   832  C  CA  . LYS A 1 98  ? -33.119 -47.352 -35.872 1.00 23.71  ? 119  LYS A CA  1 
ATOM   833  C  C   . LYS A 1 98  ? -32.526 -48.539 -35.112 1.00 28.02  ? 119  LYS A C   1 
ATOM   834  O  O   . LYS A 1 98  ? -31.859 -48.345 -34.093 1.00 27.91  ? 119  LYS A O   1 
ATOM   835  C  CB  . LYS A 1 98  ? -34.575 -47.133 -35.505 1.00 27.82  ? 119  LYS A CB  1 
ATOM   836  C  CG  . LYS A 1 98  ? -34.745 -46.661 -34.050 1.00 35.67  ? 119  LYS A CG  1 
ATOM   837  C  CD  . LYS A 1 98  ? -36.087 -45.961 -33.920 1.00 45.04  ? 119  LYS A CD  1 
ATOM   838  C  CE  . LYS A 1 98  ? -36.658 -46.228 -32.615 1.00 52.53  ? 119  LYS A CE  1 
ATOM   839  N  NZ  . LYS A 1 98  ? -38.034 -45.680 -32.524 1.00 60.69  ? 119  LYS A NZ  1 
ATOM   840  N  N   A ASP A 1 99  ? -32.759 -49.762 -35.590 0.57 25.28  ? 120  ASP A N   1 
ATOM   841  N  N   B ASP A 1 99  ? -32.741 -49.739 -35.629 0.43 25.21  ? 120  ASP A N   1 
ATOM   842  C  CA  A ASP A 1 99  ? -32.155 -50.934 -34.923 0.57 30.23  ? 120  ASP A CA  1 
ATOM   843  C  CA  B ASP A 1 99  ? -32.175 -50.935 -35.015 0.43 30.05  ? 120  ASP A CA  1 
ATOM   844  C  C   A ASP A 1 99  ? -30.626 -50.856 -34.995 0.57 27.58  ? 120  ASP A C   1 
ATOM   845  C  C   B ASP A 1 99  ? -30.646 -50.913 -35.101 0.43 27.65  ? 120  ASP A C   1 
ATOM   846  O  O   A ASP A 1 99  ? -29.914 -51.200 -34.032 0.57 28.60  ? 120  ASP A O   1 
ATOM   847  O  O   B ASP A 1 99  ? -29.939 -51.346 -34.176 0.43 28.20  ? 120  ASP A O   1 
ATOM   848  C  CB  A ASP A 1 99  ? -32.596 -52.266 -35.544 0.57 29.34  ? 120  ASP A CB  1 
ATOM   849  C  CB  B ASP A 1 99  ? -32.735 -52.175 -35.698 0.43 30.51  ? 120  ASP A CB  1 
ATOM   850  C  CG  A ASP A 1 99  ? -34.070 -52.602 -35.307 0.57 30.14  ? 120  ASP A CG  1 
ATOM   851  C  CG  B ASP A 1 99  ? -32.415 -53.445 -34.961 0.43 36.20  ? 120  ASP A CG  1 
ATOM   852  O  OD1 A ASP A 1 99  ? -34.668 -52.151 -34.318 0.57 33.51  ? 120  ASP A OD1 1 
ATOM   853  O  OD1 B ASP A 1 99  ? -32.322 -53.405 -33.716 0.43 47.05  ? 120  ASP A OD1 1 
ATOM   854  O  OD2 A ASP A 1 99  ? -34.617 -53.372 -36.122 0.57 33.03  ? 120  ASP A OD2 1 
ATOM   855  O  OD2 B ASP A 1 99  ? -32.284 -54.493 -35.624 0.43 44.02  ? 120  ASP A OD2 1 
ATOM   856  N  N   A ILE A 1 100 ? -30.119 -50.431 -36.147 0.57 27.37  ? 121  ILE A N   1 
ATOM   857  N  N   B ILE A 1 100 ? -30.135 -50.407 -36.216 0.43 26.72  ? 121  ILE A N   1 
ATOM   858  C  CA  A ILE A 1 100 ? -28.657 -50.317 -36.324 0.57 24.77  ? 121  ILE A CA  1 
ATOM   859  C  CA  B ILE A 1 100 ? -28.677 -50.279 -36.382 0.43 26.33  ? 121  ILE A CA  1 
ATOM   860  C  C   A ILE A 1 100 ? -28.138 -49.275 -35.352 0.57 27.20  ? 121  ILE A C   1 
ATOM   861  C  C   B ILE A 1 100 ? -28.147 -49.277 -35.373 0.43 26.72  ? 121  ILE A C   1 
ATOM   862  O  O   A ILE A 1 100 ? -27.128 -49.487 -34.686 0.57 24.31  ? 121  ILE A O   1 
ATOM   863  O  O   B ILE A 1 100 ? -27.141 -49.516 -34.709 0.43 25.29  ? 121  ILE A O   1 
ATOM   864  C  CB  A ILE A 1 100 ? -28.278 -49.937 -37.777 0.57 26.83  ? 121  ILE A CB  1 
ATOM   865  C  CB  B ILE A 1 100 ? -28.300 -49.829 -37.809 0.43 25.73  ? 121  ILE A CB  1 
ATOM   866  C  CG1 A ILE A 1 100 ? -28.501 -51.147 -38.680 0.57 29.85  ? 121  ILE A CG1 1 
ATOM   867  C  CG1 B ILE A 1 100 ? -28.574 -50.963 -38.789 0.43 29.25  ? 121  ILE A CG1 1 
ATOM   868  C  CG2 A ILE A 1 100 ? -26.791 -49.459 -37.880 0.57 31.63  ? 121  ILE A CG2 1 
ATOM   869  C  CG2 B ILE A 1 100 ? -26.806 -49.416 -37.891 0.43 30.98  ? 121  ILE A CG2 1 
ATOM   870  C  CD1 A ILE A 1 100 ? -28.455 -50.839 -40.153 0.57 32.81  ? 121  ILE A CD1 1 
ATOM   871  C  CD1 B ILE A 1 100 ? -27.730 -52.192 -38.530 0.43 29.19  ? 121  ILE A CD1 1 
ATOM   872  N  N   . PHE A 1 101 ? -28.826 -48.144 -35.267 1.00 24.11  ? 122  PHE A N   1 
ATOM   873  C  CA  . PHE A 1 101 ? -28.417 -47.113 -34.298 1.00 28.10  ? 122  PHE A CA  1 
ATOM   874  C  C   . PHE A 1 101 ? -28.379 -47.734 -32.890 1.00 28.95  ? 122  PHE A C   1 
ATOM   875  O  O   . PHE A 1 101 ? -27.411 -47.547 -32.095 1.00 26.97  ? 122  PHE A O   1 
ATOM   876  C  CB  . PHE A 1 101 ? -29.363 -45.872 -34.317 1.00 24.92  ? 122  PHE A CB  1 
ATOM   877  C  CG  . PHE A 1 101 ? -28.990 -44.847 -33.216 1.00 26.74  ? 122  PHE A CG  1 
ATOM   878  C  CD1 . PHE A 1 101 ? -29.530 -44.922 -31.958 1.00 29.74  ? 122  PHE A CD1 1 
ATOM   879  C  CD2 . PHE A 1 101 ? -28.028 -43.883 -33.460 1.00 31.11  ? 122  PHE A CD2 1 
ATOM   880  C  CE1 . PHE A 1 101 ? -29.125 -44.053 -30.934 1.00 33.98  ? 122  PHE A CE1 1 
ATOM   881  C  CE2 . PHE A 1 101 ? -27.632 -42.999 -32.422 1.00 31.89  ? 122  PHE A CE2 1 
ATOM   882  C  CZ  . PHE A 1 101 ? -28.168 -43.099 -31.190 1.00 29.76  ? 122  PHE A CZ  1 
ATOM   883  N  N   . ASN A 1 102 ? -29.431 -48.467 -32.536 1.00 25.00  ? 123  ASN A N   1 
ATOM   884  C  CA  . ASN A 1 102 ? -29.477 -49.048 -31.186 1.00 26.84  ? 123  ASN A CA  1 
ATOM   885  C  C   . ASN A 1 102 ? -28.333 -50.035 -30.938 1.00 29.58  ? 123  ASN A C   1 
ATOM   886  O  O   . ASN A 1 102 ? -27.777 -50.088 -29.842 1.00 31.57  ? 123  ASN A O   1 
ATOM   887  C  CB  . ASN A 1 102 ? -30.834 -49.748 -30.932 1.00 33.79  ? 123  ASN A CB  1 
ATOM   888  C  CG  . ASN A 1 102 ? -31.967 -48.746 -30.857 1.00 46.05  ? 123  ASN A CG  1 
ATOM   889  O  OD1 . ASN A 1 102 ? -31.725 -47.538 -30.762 1.00 39.24  ? 123  ASN A OD1 1 
ATOM   890  N  ND2 . ASN A 1 102 ? -33.195 -49.223 -30.897 1.00 40.90  ? 123  ASN A ND2 1 
ATOM   891  N  N   . ASN A 1 103 ? -27.994 -50.828 -31.950 1.00 29.82  ? 124  ASN A N   1 
ATOM   892  C  CA  . ASN A 1 103 ? -26.875 -51.772 -31.829 1.00 31.76  ? 124  ASN A CA  1 
ATOM   893  C  C   . ASN A 1 103 ? -25.540 -51.014 -31.647 1.00 31.20  ? 124  ASN A C   1 
ATOM   894  O  O   . ASN A 1 103 ? -24.641 -51.422 -30.860 1.00 31.35  ? 124  ASN A O   1 
ATOM   895  C  CB  . ASN A 1 103 ? -26.776 -52.671 -33.075 1.00 34.54  ? 124  ASN A CB  1 
ATOM   896  C  CG  . ASN A 1 103 ? -27.965 -53.623 -33.219 1.00 46.65  ? 124  ASN A CG  1 
ATOM   897  O  OD1 . ASN A 1 103 ? -28.612 -53.940 -32.238 1.00 48.23  ? 124  ASN A OD1 1 
ATOM   898  N  ND2 . ASN A 1 103 ? -28.241 -54.091 -34.459 1.00 52.12  ? 124  ASN A ND2 1 
ATOM   899  N  N   . LEU A 1 104 ? -25.363 -49.970 -32.443 1.00 27.16  ? 125  LEU A N   1 
ATOM   900  C  CA  . LEU A 1 104 ? -24.166 -49.103 -32.273 1.00 28.01  ? 125  LEU A CA  1 
ATOM   901  C  C   . LEU A 1 104 ? -24.092 -48.463 -30.894 1.00 31.93  ? 125  LEU A C   1 
ATOM   902  O  O   . LEU A 1 104 ? -23.018 -48.374 -30.273 1.00 29.74  ? 125  LEU A O   1 
ATOM   903  C  CB  . LEU A 1 104 ? -24.142 -47.972 -33.351 1.00 23.75  ? 125  LEU A CB  1 
ATOM   904  C  CG  . LEU A 1 104 ? -23.805 -48.475 -34.759 1.00 31.19  ? 125  LEU A CG  1 
ATOM   905  C  CD1 . LEU A 1 104 ? -24.069 -47.360 -35.785 1.00 29.96  ? 125  LEU A CD1 1 
ATOM   906  C  CD2 . LEU A 1 104 ? -22.359 -48.948 -34.841 1.00 30.84  ? 125  LEU A CD2 1 
ATOM   907  N  N   . ALA A 1 105 ? -25.223 -47.960 -30.412 1.00 26.84  ? 126  ALA A N   1 
ATOM   908  C  CA  . ALA A 1 105 ? -25.256 -47.367 -29.075 1.00 26.76  ? 126  ALA A CA  1 
ATOM   909  C  C   . ALA A 1 105 ? -24.956 -48.392 -27.983 1.00 31.48  ? 126  ALA A C   1 
ATOM   910  O  O   . ALA A 1 105 ? -24.230 -48.100 -27.009 1.00 33.64  ? 126  ALA A O   1 
ATOM   911  C  CB  . ALA A 1 105 ? -26.618 -46.696 -28.838 1.00 31.07  ? 126  ALA A CB  1 
ATOM   912  N  N   . ARG A 1 106 ? -25.510 -49.593 -28.127 1.00 30.76  ? 127  ARG A N   1 
ATOM   913  C  CA  . ARG A 1 106 ? -25.286 -50.669 -27.177 1.00 33.78  ? 127  ARG A CA  1 
ATOM   914  C  C   . ARG A 1 106 ? -23.798 -51.063 -27.193 1.00 38.16  ? 127  ARG A C   1 
ATOM   915  O  O   . ARG A 1 106 ? -23.182 -51.242 -26.125 1.00 36.45  ? 127  ARG A O   1 
ATOM   916  C  CB  . ARG A 1 106 ? -26.239 -51.861 -27.484 1.00 32.61  ? 127  ARG A CB  1 
ATOM   917  C  CG  . ARG A 1 106 ? -26.098 -53.095 -26.604 1.00 47.52  ? 127  ARG A CG  1 
ATOM   918  C  CD  . ARG A 1 106 ? -27.196 -54.159 -26.978 1.00 55.69  ? 127  ARG A CD  1 
ATOM   919  N  N   . GLN A 1 107 ? -23.189 -51.142 -28.371 1.00 40.35  ? 128  GLN A N   1 
ATOM   920  C  CA  . GLN A 1 107 ? -21.758 -51.461 -28.478 1.00 39.06  ? 128  GLN A CA  1 
ATOM   921  C  C   . GLN A 1 107 ? -20.905 -50.348 -27.844 1.00 35.86  ? 128  GLN A C   1 
ATOM   922  O  O   . GLN A 1 107 ? -19.938 -50.627 -27.132 1.00 37.31  ? 128  GLN A O   1 
ATOM   923  C  CB  . GLN A 1 107 ? -21.392 -51.672 -29.944 1.00 44.40  ? 128  GLN A CB  1 
ATOM   924  C  CG  . GLN A 1 107 ? -19.924 -51.954 -30.313 1.00 46.35  ? 128  GLN A CG  1 
ATOM   925  C  CD  . GLN A 1 107 ? -19.762 -52.188 -31.847 1.00 65.07  ? 128  GLN A CD  1 
ATOM   926  O  OE1 . GLN A 1 107 ? -19.471 -53.311 -32.284 1.00 74.89  ? 128  GLN A OE1 1 
ATOM   927  N  NE2 . GLN A 1 107 ? -19.993 -51.140 -32.658 1.00 52.59  ? 128  GLN A NE2 1 
ATOM   928  N  N   . PHE A 1 108 ? -21.318 -49.107 -28.042 1.00 28.52  ? 129  PHE A N   1 
ATOM   929  C  CA  . PHE A 1 108 ? -20.610 -47.960 -27.524 1.00 29.16  ? 129  PHE A CA  1 
ATOM   930  C  C   . PHE A 1 108 ? -20.656 -48.029 -26.004 1.00 40.79  ? 129  PHE A C   1 
ATOM   931  O  O   . PHE A 1 108 ? -19.645 -47.860 -25.304 1.00 32.59  ? 129  PHE A O   1 
ATOM   932  C  CB  . PHE A 1 108 ? -21.240 -46.642 -28.043 1.00 28.00  ? 129  PHE A CB  1 
ATOM   933  C  CG  . PHE A 1 108 ? -20.848 -45.457 -27.217 1.00 31.61  ? 129  PHE A CG  1 
ATOM   934  C  CD1 . PHE A 1 108 ? -19.542 -44.918 -27.311 1.00 27.41  ? 129  PHE A CD1 1 
ATOM   935  C  CD2 . PHE A 1 108 ? -21.744 -44.895 -26.308 1.00 30.69  ? 129  PHE A CD2 1 
ATOM   936  C  CE1 . PHE A 1 108 ? -19.164 -43.857 -26.510 1.00 30.92  ? 129  PHE A CE1 1 
ATOM   937  C  CE2 . PHE A 1 108 ? -21.341 -43.829 -25.486 1.00 34.55  ? 129  PHE A CE2 1 
ATOM   938  C  CZ  . PHE A 1 108 ? -20.054 -43.315 -25.605 1.00 32.19  ? 129  PHE A CZ  1 
ATOM   939  N  N   . GLN A 1 109 ? -21.859 -48.293 -25.502 1.00 29.99  ? 130  GLN A N   1 
ATOM   940  C  CA  . GLN A 1 109 ? -22.083 -48.362 -24.087 1.00 38.22  ? 130  GLN A CA  1 
ATOM   941  C  C   . GLN A 1 109 ? -21.250 -49.463 -23.474 1.00 42.85  ? 130  GLN A C   1 
ATOM   942  O  O   . GLN A 1 109 ? -20.656 -49.290 -22.416 1.00 38.98  ? 130  GLN A O   1 
ATOM   943  C  CB  . GLN A 1 109 ? -23.545 -48.613 -23.792 1.00 44.06  ? 130  GLN A CB  1 
ATOM   944  C  CG  . GLN A 1 109 ? -23.820 -48.731 -22.325 1.00 64.71  ? 130  GLN A CG  1 
ATOM   945  C  CD  . GLN A 1 109 ? -24.802 -47.692 -21.941 1.00 76.79  ? 130  GLN A CD  1 
ATOM   946  O  OE1 . GLN A 1 109 ? -25.192 -46.884 -22.796 1.00 81.06  ? 130  GLN A OE1 1 
ATOM   947  N  NE2 . GLN A 1 109 ? -25.223 -47.682 -20.669 1.00 80.03  ? 130  GLN A NE2 1 
ATOM   948  N  N   . LYS A 1 110 ? -21.213 -50.603 -24.141 1.00 39.90  ? 131  LYS A N   1 
ATOM   949  C  CA  . LYS A 1 110 ? -20.519 -51.753 -23.577 1.00 43.49  ? 131  LYS A CA  1 
ATOM   950  C  C   . LYS A 1 110 ? -18.989 -51.618 -23.650 1.00 44.91  ? 131  LYS A C   1 
ATOM   951  O  O   . LYS A 1 110 ? -18.283 -51.962 -22.699 1.00 50.99  ? 131  LYS A O   1 
ATOM   952  C  CB  . LYS A 1 110 ? -20.989 -53.042 -24.286 1.00 41.12  ? 131  LYS A CB  1 
ATOM   953  N  N   . GLU A 1 111 ? -18.451 -51.156 -24.772 1.00 43.37  ? 132  GLU A N   1 
ATOM   954  C  CA  . GLU A 1 111 ? -16.995 -51.224 -24.939 1.00 44.75  ? 132  GLU A CA  1 
ATOM   955  C  C   . GLU A 1 111 ? -16.267 -49.888 -24.829 1.00 47.83  ? 132  GLU A C   1 
ATOM   956  O  O   . GLU A 1 111 ? -15.101 -49.856 -24.460 1.00 53.17  ? 132  GLU A O   1 
ATOM   957  C  CB  . GLU A 1 111 ? -16.636 -51.823 -26.289 1.00 48.45  ? 132  GLU A CB  1 
ATOM   958  C  CG  . GLU A 1 111 ? -17.175 -53.236 -26.564 1.00 57.14  ? 132  GLU A CG  1 
ATOM   959  C  CD  . GLU A 1 111 ? -16.964 -53.619 -28.031 1.00 71.25  ? 132  GLU A CD  1 
ATOM   960  O  OE1 . GLU A 1 111 ? -16.995 -52.704 -28.908 1.00 71.80  ? 132  GLU A OE1 1 
ATOM   961  O  OE2 . GLU A 1 111 ? -16.746 -54.829 -28.305 1.00 78.33  ? 132  GLU A OE2 1 
ATOM   962  N  N   . VAL A 1 112 ? -16.939 -48.789 -25.156 1.00 35.05  ? 133  VAL A N   1 
ATOM   963  C  CA  . VAL A 1 112 ? -16.236 -47.522 -25.351 1.00 28.44  ? 133  VAL A CA  1 
ATOM   964  C  C   . VAL A 1 112 ? -16.483 -46.489 -24.247 1.00 33.18  ? 133  VAL A C   1 
ATOM   965  O  O   . VAL A 1 112 ? -15.575 -45.696 -23.933 1.00 32.70  ? 133  VAL A O   1 
ATOM   966  C  CB  . VAL A 1 112 ? -16.639 -46.907 -26.747 1.00 33.41  ? 133  VAL A CB  1 
ATOM   967  C  CG1 . VAL A 1 112 ? -15.972 -45.551 -27.008 1.00 31.63  ? 133  VAL A CG1 1 
ATOM   968  C  CG2 . VAL A 1 112 ? -16.261 -47.880 -27.910 1.00 35.74  ? 133  VAL A CG2 1 
ATOM   969  N  N   . LEU A 1 113 ? -17.713 -46.463 -23.714 1.00 26.52  ? 134  LEU A N   1 
ATOM   970  C  CA  . LEU A 1 113 ? -18.145 -45.562 -22.660 1.00 26.78  ? 134  LEU A CA  1 
ATOM   971  C  C   . LEU A 1 113 ? -17.436 -45.905 -21.335 1.00 30.96  ? 134  LEU A C   1 
ATOM   972  O  O   . LEU A 1 113 ? -17.497 -47.049 -20.910 1.00 30.05  ? 134  LEU A O   1 
ATOM   973  C  CB  . LEU A 1 113 ? -19.645 -45.685 -22.445 1.00 28.23  ? 134  LEU A CB  1 
ATOM   974  C  CG  . LEU A 1 113 ? -20.177 -44.839 -21.313 1.00 30.50  ? 134  LEU A CG  1 
ATOM   975  C  CD1 . LEU A 1 113 ? -19.963 -43.326 -21.597 1.00 29.36  ? 134  LEU A CD1 1 
ATOM   976  C  CD2 . LEU A 1 113 ? -21.628 -45.145 -21.196 1.00 35.26  ? 134  LEU A CD2 1 
ATOM   977  N  N   . CYS A 1 114 ? -16.809 -44.929 -20.689 1.00 26.03  ? 135  CYS A N   1 
ATOM   978  C  CA  . CYS A 1 114 ? -16.155 -45.109 -19.349 1.00 29.06  ? 135  CYS A CA  1 
ATOM   979  C  C   . CYS A 1 114 ? -15.451 -46.473 -19.165 1.00 30.79  ? 135  CYS A C   1 
ATOM   980  O  O   . CYS A 1 114 ? -15.813 -47.253 -18.275 1.00 27.86  ? 135  CYS A O   1 
ATOM   981  C  CB  . CYS A 1 114 ? -17.169 -44.926 -18.209 1.00 34.87  ? 135  CYS A CB  1 
ATOM   982  S  SG  . CYS A 1 114 ? -17.996 -43.274 -18.287 1.00 34.40  ? 135  CYS A SG  1 
ATOM   983  N  N   . PRO A 1 115 ? -14.467 -46.767 -20.012 1.00 27.97  ? 136  PRO A N   1 
ATOM   984  C  CA  . PRO A 1 115 ? -13.758 -48.035 -19.858 1.00 24.76  ? 136  PRO A CA  1 
ATOM   985  C  C   . PRO A 1 115 ? -12.693 -47.996 -18.777 1.00 28.88  ? 136  PRO A C   1 
ATOM   986  O  O   . PRO A 1 115 ? -12.115 -49.051 -18.470 1.00 30.43  ? 136  PRO A O   1 
ATOM   987  C  CB  . PRO A 1 115 ? -13.088 -48.222 -21.225 1.00 27.91  ? 136  PRO A CB  1 
ATOM   988  C  CG  . PRO A 1 115 ? -12.722 -46.763 -21.606 1.00 30.70  ? 136  PRO A CG  1 
ATOM   989  C  CD  . PRO A 1 115 ? -13.947 -45.967 -21.149 1.00 24.69  ? 136  PRO A CD  1 
ATOM   990  N  N   . ASN A 1 116 ? -12.469 -46.836 -18.146 1.00 25.36  ? 137  ASN A N   1 
ATOM   991  C  CA  . ASN A 1 116 ? -11.427 -46.770 -17.125 1.00 25.20  ? 137  ASN A CA  1 
ATOM   992  C  C   . ASN A 1 116 ? -11.845 -47.567 -15.898 1.00 27.70  ? 137  ASN A C   1 
ATOM   993  O  O   . ASN A 1 116 ? -13.065 -47.622 -15.552 1.00 30.21  ? 137  ASN A O   1 
ATOM   994  C  CB  . ASN A 1 116 ? -11.132 -45.328 -16.744 1.00 25.36  ? 137  ASN A CB  1 
ATOM   995  C  CG  . ASN A 1 116 ? -12.395 -44.585 -16.321 1.00 27.63  ? 137  ASN A CG  1 
ATOM   996  O  OD1 . ASN A 1 116 ? -13.408 -44.648 -17.014 1.00 28.00  ? 137  ASN A OD1 1 
ATOM   997  N  ND2 . ASN A 1 116 ? -12.347 -43.895 -15.195 1.00 26.08  ? 137  ASN A ND2 1 
ATOM   998  N  N   . LYS A 1 117 ? -10.860 -48.244 -15.275 1.00 26.13  ? 138  LYS A N   1 
ATOM   999  C  CA  . LYS A 1 117 ? -11.085 -49.028 -14.054 1.00 31.85  ? 138  LYS A CA  1 
ATOM   1000 C  C   . LYS A 1 117 ? -10.592 -48.292 -12.801 1.00 28.39  ? 138  LYS A C   1 
ATOM   1001 O  O   . LYS A 1 117 ? -10.810 -48.721 -11.664 1.00 28.61  ? 138  LYS A O   1 
ATOM   1002 C  CB  . LYS A 1 117 ? -10.376 -50.397 -14.169 1.00 35.46  ? 138  LYS A CB  1 
ATOM   1003 C  CG  . LYS A 1 117 ? -10.845 -51.132 -15.430 1.00 38.52  ? 138  LYS A CG  1 
ATOM   1004 C  CD  . LYS A 1 117 ? -10.346 -52.568 -15.420 1.00 46.29  ? 138  LYS A CD  1 
ATOM   1005 C  CE  . LYS A 1 117 ? -8.928  -52.681 -15.861 1.00 41.07  ? 138  LYS A CE  1 
ATOM   1006 N  NZ  . LYS A 1 117 ? -8.558  -54.138 -16.229 1.00 41.39  ? 138  LYS A NZ  1 
ATOM   1007 N  N   . CYS A 1 118 ? -9.945  -47.156 -13.020 1.00 29.70  ? 139  CYS A N   1 
ATOM   1008 C  CA  . CYS A 1 118 ? -9.537  -46.287 -11.940 1.00 27.37  ? 139  CYS A CA  1 
ATOM   1009 C  C   . CYS A 1 118 ? -9.414  -44.905 -12.608 1.00 25.98  ? 139  CYS A C   1 
ATOM   1010 O  O   . CYS A 1 118 ? -9.606  -44.762 -13.813 1.00 27.42  ? 139  CYS A O   1 
ATOM   1011 C  CB  . CYS A 1 118 ? -8.208  -46.739 -11.311 1.00 26.36  ? 139  CYS A CB  1 
ATOM   1012 S  SG  . CYS A 1 118 ? -6.899  -46.730 -12.659 1.00 30.86  ? 139  CYS A SG  1 
ATOM   1013 N  N   . GLY A 1 119 ? -9.101  -43.891 -11.820 1.00 27.16  ? 140  GLY A N   1 
ATOM   1014 C  CA  . GLY A 1 119 ? -8.832  -42.568 -12.356 1.00 24.40  ? 140  GLY A CA  1 
ATOM   1015 C  C   . GLY A 1 119 ? -10.105 -41.904 -12.877 1.00 30.94  ? 140  GLY A C   1 
ATOM   1016 O  O   . GLY A 1 119 ? -11.202 -42.397 -12.654 1.00 27.39  ? 140  GLY A O   1 
ATOM   1017 N  N   . VAL A 1 120 ? -9.947  -40.788 -13.584 1.00 29.23  ? 141  VAL A N   1 
ATOM   1018 C  CA  . VAL A 1 120 ? -11.099 -40.032 -14.060 1.00 25.76  ? 141  VAL A CA  1 
ATOM   1019 C  C   . VAL A 1 120 ? -10.959 -39.792 -15.538 1.00 24.39  ? 141  VAL A C   1 
ATOM   1020 O  O   . VAL A 1 120 ? -9.993  -39.174 -15.967 1.00 25.46  ? 141  VAL A O   1 
ATOM   1021 C  CB  . VAL A 1 120 ? -11.228 -38.689 -13.331 1.00 24.42  ? 141  VAL A CB  1 
ATOM   1022 C  CG1 . VAL A 1 120 ? -12.548 -38.009 -13.764 1.00 35.09  ? 141  VAL A CG1 1 
ATOM   1023 C  CG2 . VAL A 1 120 ? -11.211 -38.888 -11.768 1.00 27.27  ? 141  VAL A CG2 1 
ATOM   1024 N  N   . MET A 1 121 ? -11.904 -40.313 -16.325 1.00 25.05  ? 142  MET A N   1 
ATOM   1025 C  CA  . MET A 1 121 ? -11.831 -40.179 -17.759 1.00 25.29  ? 142  MET A CA  1 
ATOM   1026 C  C   . MET A 1 121 ? -12.902 -39.187 -18.217 1.00 30.52  ? 142  MET A C   1 
ATOM   1027 O  O   . MET A 1 121 ? -13.984 -39.151 -17.633 1.00 27.59  ? 142  MET A O   1 
ATOM   1028 C  CB  . MET A 1 121 ? -12.043 -41.525 -18.442 1.00 22.66  ? 142  MET A CB  1 
ATOM   1029 C  CG  . MET A 1 121 ? -11.933 -41.386 -19.967 1.00 23.68  ? 142  MET A CG  1 
ATOM   1030 S  SD  . MET A 1 121 ? -12.121 -43.059 -20.732 1.00 28.40  ? 142  MET A SD  1 
ATOM   1031 C  CE  . MET A 1 121 ? -11.617 -42.705 -22.436 1.00 27.72  ? 142  MET A CE  1 
ATOM   1032 N  N   . SER A 1 122 ? -12.571 -38.334 -19.199 1.00 26.24  ? 143  SER A N   1 
ATOM   1033 C  CA  . SER A 1 122 ? -13.546 -37.382 -19.767 1.00 25.65  ? 143  SER A CA  1 
ATOM   1034 C  C   . SER A 1 122 ? -13.799 -37.766 -21.230 1.00 29.27  ? 143  SER A C   1 
ATOM   1035 O  O   . SER A 1 122 ? -12.854 -38.012 -21.996 1.00 27.73  ? 143  SER A O   1 
ATOM   1036 C  CB  . SER A 1 122 ? -13.015 -35.942 -19.685 1.00 24.21  ? 143  SER A CB  1 
ATOM   1037 O  OG  . SER A 1 122 ? -12.700 -35.587 -18.332 1.00 26.94  ? 143  SER A OG  1 
ATOM   1038 N  N   . GLN A 1 123 ? -15.065 -37.822 -21.610 1.00 22.42  ? 144  GLN A N   1 
ATOM   1039 C  CA  . GLN A 1 123 ? -15.438 -38.203 -22.982 1.00 24.26  ? 144  GLN A CA  1 
ATOM   1040 C  C   . GLN A 1 123 ? -16.418 -37.191 -23.543 1.00 25.63  ? 144  GLN A C   1 
ATOM   1041 O  O   . GLN A 1 123 ? -17.190 -36.583 -22.771 1.00 31.84  ? 144  GLN A O   1 
ATOM   1042 C  CB  . GLN A 1 123 ? -16.088 -39.601 -23.026 1.00 27.66  ? 144  GLN A CB  1 
ATOM   1043 C  CG  . GLN A 1 123 ? -15.144 -40.708 -22.503 1.00 32.37  ? 144  GLN A CG  1 
ATOM   1044 C  CD  . GLN A 1 123 ? -15.728 -42.128 -22.616 1.00 31.99  ? 144  GLN A CD  1 
ATOM   1045 O  OE1 . GLN A 1 123 ? -16.575 -42.537 -21.826 1.00 34.55  ? 144  GLN A OE1 1 
ATOM   1046 N  NE2 . GLN A 1 123 ? -15.242 -42.879 -23.581 1.00 30.36  ? 144  GLN A NE2 1 
ATOM   1047 N  N   . THR A 1 124 ? -16.422 -37.054 -24.866 1.00 21.86  ? 145  THR A N   1 
ATOM   1048 C  CA  . THR A 1 124 ? -17.295 -36.053 -25.500 1.00 23.00  ? 145  THR A CA  1 
ATOM   1049 C  C   . THR A 1 124 ? -18.513 -36.798 -26.016 1.00 20.85  ? 145  THR A C   1 
ATOM   1050 O  O   . THR A 1 124 ? -18.358 -37.704 -26.873 1.00 26.13  ? 145  THR A O   1 
ATOM   1051 C  CB  . THR A 1 124 ? -16.590 -35.339 -26.665 1.00 25.24  ? 145  THR A CB  1 
ATOM   1052 O  OG1 . THR A 1 124 ? -15.528 -34.540 -26.124 1.00 26.76  ? 145  THR A OG1 1 
ATOM   1053 C  CG2 . THR A 1 124 ? -17.542 -34.413 -27.393 1.00 22.09  ? 145  THR A CG2 1 
ATOM   1054 N  N   . LEU A 1 125 ? -19.697 -36.442 -25.505 1.00 23.82  ? 146  LEU A N   1 
ATOM   1055 C  CA  . LEU A 1 125 ? -20.918 -37.136 -25.953 1.00 22.50  ? 146  LEU A CA  1 
ATOM   1056 C  C   . LEU A 1 125 ? -21.848 -36.161 -26.657 1.00 26.65  ? 146  LEU A C   1 
ATOM   1057 O  O   . LEU A 1 125 ? -21.853 -34.955 -26.370 1.00 24.76  ? 146  LEU A O   1 
ATOM   1058 C  CB  . LEU A 1 125 ? -21.667 -37.753 -24.780 1.00 24.09  ? 146  LEU A CB  1 
ATOM   1059 C  CG  . LEU A 1 125 ? -20.864 -38.767 -23.958 1.00 24.73  ? 146  LEU A CG  1 
ATOM   1060 C  CD1 . LEU A 1 125 ? -21.819 -39.473 -22.961 1.00 29.10  ? 146  LEU A CD1 1 
ATOM   1061 C  CD2 . LEU A 1 125 ? -20.248 -39.783 -24.889 1.00 29.17  ? 146  LEU A CD2 1 
ATOM   1062 N  N   . ILE A 1 126 ? -22.625 -36.717 -27.573 1.00 22.95  ? 147  ILE A N   1 
ATOM   1063 C  CA  . ILE A 1 126 ? -23.770 -35.999 -28.138 1.00 24.25  ? 147  ILE A CA  1 
ATOM   1064 C  C   . ILE A 1 126 ? -25.026 -36.605 -27.553 1.00 25.16  ? 147  ILE A C   1 
ATOM   1065 O  O   . ILE A 1 126 ? -25.232 -37.823 -27.623 1.00 26.16  ? 147  ILE A O   1 
ATOM   1066 C  CB  . ILE A 1 126 ? -23.851 -36.090 -29.685 1.00 24.65  ? 147  ILE A CB  1 
ATOM   1067 C  CG1 . ILE A 1 126 ? -22.536 -35.722 -30.377 1.00 25.14  ? 147  ILE A CG1 1 
ATOM   1068 C  CG2 . ILE A 1 126 ? -24.980 -35.209 -30.203 1.00 23.65  ? 147  ILE A CG2 1 
ATOM   1069 C  CD1 . ILE A 1 126 ? -21.985 -34.355 -29.994 1.00 28.93  ? 147  ILE A CD1 1 
ATOM   1070 N  N   . TRP A 1 127 ? -25.833 -35.766 -26.936 1.00 24.39  ? 148  TRP A N   1 
ATOM   1071 C  CA  . TRP A 1 127 ? -27.111 -36.190 -26.342 1.00 23.53  ? 148  TRP A CA  1 
ATOM   1072 C  C   . TRP A 1 127 ? -28.182 -36.122 -27.404 1.00 26.63  ? 148  TRP A C   1 
ATOM   1073 O  O   . TRP A 1 127 ? -28.386 -35.073 -28.008 1.00 27.29  ? 148  TRP A O   1 
ATOM   1074 C  CB  . TRP A 1 127 ? -27.446 -35.308 -25.142 1.00 26.30  ? 148  TRP A CB  1 
ATOM   1075 C  CG  . TRP A 1 127 ? -26.520 -35.674 -24.036 1.00 31.17  ? 148  TRP A CG  1 
ATOM   1076 C  CD1 . TRP A 1 127 ? -25.242 -35.238 -23.840 1.00 29.96  ? 148  TRP A CD1 1 
ATOM   1077 C  CD2 . TRP A 1 127 ? -26.775 -36.658 -23.031 1.00 34.60  ? 148  TRP A CD2 1 
ATOM   1078 N  NE1 . TRP A 1 127 ? -24.703 -35.840 -22.714 1.00 32.96  ? 148  TRP A NE1 1 
ATOM   1079 C  CE2 . TRP A 1 127 ? -25.622 -36.729 -22.212 1.00 35.44  ? 148  TRP A CE2 1 
ATOM   1080 C  CE3 . TRP A 1 127 ? -27.897 -37.459 -22.715 1.00 33.04  ? 148  TRP A CE3 1 
ATOM   1081 C  CZ2 . TRP A 1 127 ? -25.541 -37.586 -21.098 1.00 45.01  ? 148  TRP A CZ2 1 
ATOM   1082 C  CZ3 . TRP A 1 127 ? -27.802 -38.330 -21.611 1.00 36.86  ? 148  TRP A CZ3 1 
ATOM   1083 C  CH2 . TRP A 1 127 ? -26.638 -38.377 -20.822 1.00 43.21  ? 148  TRP A CH2 1 
ATOM   1084 N  N   . CYS A 1 128 ? -28.907 -37.224 -27.608 1.00 26.10  ? 149  CYS A N   1 
ATOM   1085 C  CA  . CYS A 1 128 ? -29.796 -37.338 -28.795 1.00 28.84  ? 149  CYS A CA  1 
ATOM   1086 C  C   . CYS A 1 128 ? -31.092 -36.533 -28.760 1.00 28.36  ? 149  CYS A C   1 
ATOM   1087 O  O   . CYS A 1 128 ? -31.695 -36.308 -29.783 1.00 29.52  ? 149  CYS A O   1 
ATOM   1088 C  CB  . CYS A 1 128 ? -30.138 -38.816 -29.006 1.00 27.51  ? 149  CYS A CB  1 
ATOM   1089 S  SG  . CYS A 1 128 ? -28.704 -39.875 -29.160 1.00 28.54  ? 149  CYS A SG  1 
ATOM   1090 N  N   . LEU A 1 129 ? -31.580 -36.146 -27.588 1.00 27.63  ? 150  LEU A N   1 
ATOM   1091 C  CA  . LEU A 1 129 ? -32.886 -35.527 -27.563 1.00 27.61  ? 150  LEU A CA  1 
ATOM   1092 C  C   . LEU A 1 129 ? -32.776 -34.106 -28.072 1.00 28.96  ? 150  LEU A C   1 
ATOM   1093 O  O   . LEU A 1 129 ? -33.576 -33.638 -28.883 1.00 30.92  ? 150  LEU A O   1 
ATOM   1094 C  CB  . LEU A 1 129 ? -33.465 -35.569 -26.108 1.00 33.08  ? 150  LEU A CB  1 
ATOM   1095 C  CG  . LEU A 1 129 ? -34.894 -35.074 -25.918 1.00 40.85  ? 150  LEU A CG  1 
ATOM   1096 C  CD1 . LEU A 1 129 ? -35.870 -35.775 -26.871 1.00 41.55  ? 150  LEU A CD1 1 
ATOM   1097 C  CD2 . LEU A 1 129 ? -35.333 -35.213 -24.401 1.00 41.57  ? 150  LEU A CD2 1 
ATOM   1098 N  N   . LYS A 1 130 ? -31.801 -33.372 -27.554 1.00 27.77  ? 151  LYS A N   1 
ATOM   1099 C  CA  . LYS A 1 130 ? -31.716 -31.964 -27.952 1.00 37.22  ? 151  LYS A CA  1 
ATOM   1100 C  C   . LYS A 1 130 ? -30.375 -31.590 -28.625 1.00 33.11  ? 151  LYS A C   1 
ATOM   1101 O  O   . LYS A 1 130 ? -30.124 -30.412 -28.870 1.00 31.73  ? 151  LYS A O   1 
ATOM   1102 C  CB  . LYS A 1 130 ? -31.969 -31.076 -26.751 1.00 45.15  ? 151  LYS A CB  1 
ATOM   1103 C  CG  . LYS A 1 130 ? -33.448 -30.907 -26.412 1.00 48.61  ? 151  LYS A CG  1 
ATOM   1104 C  CD  . LYS A 1 130 ? -33.610 -30.186 -25.055 1.00 56.74  ? 151  LYS A CD  1 
ATOM   1105 N  N   . CYS A 1 131 ? -29.566 -32.600 -28.947 1.00 29.23  ? 152  CYS A N   1 
ATOM   1106 C  CA  . CYS A 1 131 ? -28.334 -32.463 -29.732 1.00 24.57  ? 152  CYS A CA  1 
ATOM   1107 C  C   . CYS A 1 131 ? -27.207 -31.720 -29.028 1.00 31.51  ? 152  CYS A C   1 
ATOM   1108 O  O   . CYS A 1 131 ? -26.288 -31.213 -29.691 1.00 33.60  ? 152  CYS A O   1 
ATOM   1109 C  CB  . CYS A 1 131 ? -28.622 -31.763 -31.074 1.00 30.64  ? 152  CYS A CB  1 
ATOM   1110 S  SG  . CYS A 1 131 ? -29.732 -32.824 -32.071 1.00 31.66  ? 152  CYS A SG  1 
ATOM   1111 N  N   . GLU A 1 132 ? -27.254 -31.673 -27.699 1.00 27.86  ? 153  GLU A N   1 
ATOM   1112 C  CA  . GLU A 1 132 ? -26.217 -30.987 -26.956 1.00 27.55  ? 153  GLU A CA  1 
ATOM   1113 C  C   . GLU A 1 132 ? -24.933 -31.812 -26.929 1.00 29.26  ? 153  GLU A C   1 
ATOM   1114 O  O   . GLU A 1 132 ? -24.950 -33.024 -26.684 1.00 27.49  ? 153  GLU A O   1 
ATOM   1115 C  CB  . GLU A 1 132 ? -26.694 -30.704 -25.539 1.00 31.61  ? 153  GLU A CB  1 
ATOM   1116 C  CG  . GLU A 1 132 ? -27.672 -29.506 -25.421 1.00 53.08  ? 153  GLU A CG  1 
ATOM   1117 C  CD  . GLU A 1 132 ? -26.961 -28.122 -25.542 1.00 73.44  ? 153  GLU A CD  1 
ATOM   1118 O  OE1 . GLU A 1 132 ? -25.858 -27.965 -24.955 1.00 72.08  ? 153  GLU A OE1 1 
ATOM   1119 O  OE2 . GLU A 1 132 ? -27.495 -27.209 -26.241 1.00 77.94  ? 153  GLU A OE2 1 
ATOM   1120 N  N   . LYS A 1 133 ? -23.802 -31.134 -27.104 1.00 26.03  ? 154  LYS A N   1 
ATOM   1121 C  CA  . LYS A 1 133 ? -22.531 -31.795 -26.921 1.00 28.34  ? 154  LYS A CA  1 
ATOM   1122 C  C   . LYS A 1 133 ? -22.013 -31.545 -25.507 1.00 28.35  ? 154  LYS A C   1 
ATOM   1123 O  O   . LYS A 1 133 ? -22.001 -30.399 -25.030 1.00 33.75  ? 154  LYS A O   1 
ATOM   1124 C  CB  . LYS A 1 133 ? -21.512 -31.287 -27.965 1.00 28.62  ? 154  LYS A CB  1 
ATOM   1125 C  CG  . LYS A 1 133 ? -20.186 -32.025 -27.890 1.00 31.22  ? 154  LYS A CG  1 
ATOM   1126 C  CD  . LYS A 1 133 ? -19.380 -31.773 -29.171 1.00 31.09  ? 154  LYS A CD  1 
ATOM   1127 C  CE  . LYS A 1 133 ? -18.682 -30.470 -28.991 1.00 31.63  ? 154  LYS A CE  1 
ATOM   1128 N  NZ  . LYS A 1 133 ? -17.681 -30.222 -30.053 1.00 33.99  ? 154  LYS A NZ  1 
ATOM   1129 N  N   . GLN A 1 134 ? -21.572 -32.572 -24.805 1.00 22.57  ? 155  GLN A N   1 
ATOM   1130 C  CA  . GLN A 1 134 ? -21.206 -32.288 -23.393 1.00 27.96  ? 155  GLN A CA  1 
ATOM   1131 C  C   . GLN A 1 134 ? -20.067 -33.184 -23.045 1.00 23.41  ? 155  GLN A C   1 
ATOM   1132 O  O   . GLN A 1 134 ? -19.926 -34.274 -23.607 1.00 27.08  ? 155  GLN A O   1 
ATOM   1133 C  CB  . GLN A 1 134 ? -22.392 -32.530 -22.441 1.00 38.53  ? 155  GLN A CB  1 
ATOM   1134 C  CG  . GLN A 1 134 ? -23.616 -31.576 -22.680 1.00 60.01  ? 155  GLN A CG  1 
ATOM   1135 C  CD  . GLN A 1 134 ? -24.612 -31.561 -21.508 1.00 70.11  ? 155  GLN A CD  1 
ATOM   1136 O  OE1 . GLN A 1 134 ? -24.347 -32.162 -20.459 1.00 73.82  ? 155  GLN A OE1 1 
ATOM   1137 N  NE2 . GLN A 1 134 ? -25.756 -30.871 -21.681 1.00 67.30  ? 155  GLN A NE2 1 
ATOM   1138 N  N   . LEU A 1 135 ? -19.242 -32.698 -22.151 1.00 24.51  ? 156  LEU A N   1 
ATOM   1139 C  CA  . LEU A 1 135 ? -18.147 -33.503 -21.655 1.00 26.64  ? 156  LEU A CA  1 
ATOM   1140 C  C   . LEU A 1 135 ? -18.700 -34.441 -20.583 1.00 35.71  ? 156  LEU A C   1 
ATOM   1141 O  O   . LEU A 1 135 ? -19.215 -33.971 -19.615 1.00 39.61  ? 156  LEU A O   1 
ATOM   1142 C  CB  . LEU A 1 135 ? -17.079 -32.558 -21.073 1.00 31.89  ? 156  LEU A CB  1 
ATOM   1143 C  CG  . LEU A 1 135 ? -15.756 -33.236 -20.798 1.00 33.05  ? 156  LEU A CG  1 
ATOM   1144 C  CD1 . LEU A 1 135 ? -15.221 -33.665 -22.160 1.00 25.44  ? 156  LEU A CD1 1 
ATOM   1145 C  CD2 . LEU A 1 135 ? -14.780 -32.269 -20.044 1.00 26.49  ? 156  LEU A CD2 1 
ATOM   1146 N  N   . HIS A 1 136 ? -18.603 -35.743 -20.750 1.00 24.46  ? 157  HIS A N   1 
ATOM   1147 C  CA  . HIS A 1 136 ? -19.118 -36.701 -19.783 1.00 28.83  ? 157  HIS A CA  1 
ATOM   1148 C  C   . HIS A 1 136 ? -17.985 -37.165 -18.872 1.00 27.23  ? 157  HIS A C   1 
ATOM   1149 O  O   . HIS A 1 136 ? -16.946 -37.561 -19.413 1.00 30.70  ? 157  HIS A O   1 
ATOM   1150 C  CB  . HIS A 1 136 ? -19.678 -37.912 -20.553 1.00 31.75  ? 157  HIS A CB  1 
ATOM   1151 C  CG  . HIS A 1 136 ? -20.256 -38.982 -19.670 1.00 31.96  ? 157  HIS A CG  1 
ATOM   1152 N  ND1 . HIS A 1 136 ? -21.468 -38.835 -19.027 1.00 36.73  ? 157  HIS A ND1 1 
ATOM   1153 C  CD2 . HIS A 1 136 ? -19.795 -40.218 -19.331 1.00 31.72  ? 157  HIS A CD2 1 
ATOM   1154 C  CE1 . HIS A 1 136 ? -21.718 -39.919 -18.311 1.00 44.81  ? 157  HIS A CE1 1 
ATOM   1155 N  NE2 . HIS A 1 136 ? -20.740 -40.786 -18.504 1.00 39.85  ? 157  HIS A NE2 1 
ATOM   1156 N  N   . ILE A 1 137 ? -18.191 -37.211 -17.551 1.00 26.91  ? 158  ILE A N   1 
ATOM   1157 C  CA  . ILE A 1 137 ? -17.083 -37.541 -16.632 1.00 26.08  ? 158  ILE A CA  1 
ATOM   1158 C  C   . ILE A 1 137 ? -17.269 -38.960 -16.113 1.00 34.49  ? 158  ILE A C   1 
ATOM   1159 O  O   . ILE A 1 137 ? -18.348 -39.289 -15.615 1.00 28.84  ? 158  ILE A O   1 
ATOM   1160 C  CB  . ILE A 1 137 ? -17.001 -36.561 -15.429 1.00 29.29  ? 158  ILE A CB  1 
ATOM   1161 C  CG1 . ILE A 1 137 ? -16.975 -35.108 -15.912 1.00 33.89  ? 158  ILE A CG1 1 
ATOM   1162 C  CG2 . ILE A 1 137 ? -15.718 -36.825 -14.584 1.00 27.12  ? 158  ILE A CG2 1 
ATOM   1163 C  CD1 . ILE A 1 137 ? -15.911 -34.882 -16.989 1.00 30.01  ? 158  ILE A CD1 1 
ATOM   1164 N  N   . CYS A 1 138 ? -16.236 -39.788 -16.254 1.00 29.72  ? 159  CYS A N   1 
ATOM   1165 C  CA  . CYS A 1 138 ? -16.272 -41.149 -15.736 1.00 32.69  ? 159  CYS A CA  1 
ATOM   1166 C  C   . CYS A 1 138 ? -15.410 -41.210 -14.492 1.00 27.30  ? 159  CYS A C   1 
ATOM   1167 O  O   . CYS A 1 138 ? -14.199 -41.465 -14.619 1.00 28.70  ? 159  CYS A O   1 
ATOM   1168 C  CB  . CYS A 1 138 ? -15.737 -42.142 -16.781 1.00 29.07  ? 159  CYS A CB  1 
ATOM   1169 S  SG  . CYS A 1 138 ? -16.433 -41.948 -18.490 1.00 30.21  ? 159  CYS A SG  1 
ATOM   1170 N  N   . ARG A 1 139 ? -15.988 -40.966 -13.320 1.00 27.05  ? 160  ARG A N   1 
ATOM   1171 C  CA  . ARG A 1 139 ? -15.173 -40.743 -12.162 1.00 31.89  ? 160  ARG A CA  1 
ATOM   1172 C  C   . ARG A 1 139 ? -15.029 -42.007 -11.296 1.00 26.94  ? 160  ARG A C   1 
ATOM   1173 O  O   . ARG A 1 139 ? -16.015 -42.524 -10.743 1.00 33.40  ? 160  ARG A O   1 
ATOM   1174 C  CB  . ARG A 1 139 ? -15.737 -39.598 -11.305 1.00 33.57  ? 160  ARG A CB  1 
ATOM   1175 C  CG  . ARG A 1 139 ? -14.909 -39.406 -10.031 1.00 32.96  ? 160  ARG A CG  1 
ATOM   1176 C  CD  . ARG A 1 139 ? -15.447 -38.290 -9.152  1.00 46.26  ? 160  ARG A CD  1 
ATOM   1177 N  NE  . ARG A 1 139 ? -16.080 -37.270 -9.979  1.00 52.85  ? 160  ARG A NE  1 
ATOM   1178 C  CZ  . ARG A 1 139 ? -15.428 -36.276 -10.571 1.00 45.14  ? 160  ARG A CZ  1 
ATOM   1179 N  NH1 . ARG A 1 139 ? -14.113 -36.148 -10.410 1.00 45.33  ? 160  ARG A NH1 1 
ATOM   1180 N  NH2 . ARG A 1 139 ? -16.109 -35.407 -11.302 1.00 51.91  ? 160  ARG A NH2 1 
ATOM   1181 N  N   A LYS A 1 140 ? -13.800 -42.490 -11.171 0.41 26.22  ? 161  LYS A N   1 
ATOM   1182 N  N   B LYS A 1 140 ? -13.802 -42.488 -11.169 0.59 25.86  ? 161  LYS A N   1 
ATOM   1183 C  CA  A LYS A 1 140 ? -13.489 -43.595 -10.264 0.41 29.87  ? 161  LYS A CA  1 
ATOM   1184 C  CA  B LYS A 1 140 ? -13.508 -43.577 -10.239 0.59 30.37  ? 161  LYS A CA  1 
ATOM   1185 C  C   A LYS A 1 140 ? -12.397 -43.112 -9.284  0.41 28.67  ? 161  LYS A C   1 
ATOM   1186 C  C   B LYS A 1 140 ? -12.410 -43.100 -9.267  0.59 28.88  ? 161  LYS A C   1 
ATOM   1187 O  O   A LYS A 1 140 ? -11.883 -42.006 -9.456  0.41 26.49  ? 161  LYS A O   1 
ATOM   1188 O  O   B LYS A 1 140 ? -11.910 -41.985 -9.421  0.59 26.18  ? 161  LYS A O   1 
ATOM   1189 C  CB  A LYS A 1 140 ? -13.068 -44.828 -11.072 0.41 28.55  ? 161  LYS A CB  1 
ATOM   1190 C  CB  B LYS A 1 140 ? -13.121 -44.829 -11.025 0.59 29.07  ? 161  LYS A CB  1 
ATOM   1191 C  CG  A LYS A 1 140 ? -14.259 -45.387 -11.896 0.41 31.02  ? 161  LYS A CG  1 
ATOM   1192 C  CG  B LYS A 1 140 ? -14.385 -45.439 -11.688 0.59 28.80  ? 161  LYS A CG  1 
ATOM   1193 C  CD  A LYS A 1 140 ? -13.912 -46.643 -12.678 0.41 36.43  ? 161  LYS A CD  1 
ATOM   1194 C  CD  B LYS A 1 140 ? -14.095 -46.703 -12.440 0.59 35.42  ? 161  LYS A CD  1 
ATOM   1195 C  CE  A LYS A 1 140 ? -15.143 -47.159 -13.470 0.41 34.31  ? 161  LYS A CE  1 
ATOM   1196 C  CE  B LYS A 1 140 ? -15.399 -47.361 -12.899 0.59 31.20  ? 161  LYS A CE  1 
ATOM   1197 N  NZ  A LYS A 1 140 ? -15.403 -46.354 -14.758 0.41 30.42  ? 161  LYS A NZ  1 
ATOM   1198 N  NZ  B LYS A 1 140 ? -15.054 -48.550 -13.674 0.59 39.86  ? 161  LYS A NZ  1 
ATOM   1199 N  N   . SER A 1 141 ? -12.085 -43.881 -8.240  1.00 29.00  ? 162  SER A N   1 
ATOM   1200 C  CA  . SER A 1 141 ? -10.995 -43.467 -7.319  1.00 25.40  ? 162  SER A CA  1 
ATOM   1201 C  C   . SER A 1 141 ? -9.721  -43.135 -8.071  1.00 30.50  ? 162  SER A C   1 
ATOM   1202 O  O   . SER A 1 141 ? -9.302  -43.870 -8.974  1.00 26.01  ? 162  SER A O   1 
ATOM   1203 C  CB  . SER A 1 141 ? -10.669 -44.534 -6.275  1.00 26.37  ? 162  SER A CB  1 
ATOM   1204 O  OG  . SER A 1 141 ? -11.825 -44.695 -5.469  1.00 37.76  ? 162  SER A OG  1 
ATOM   1205 N  N   A LEU A 1 142 ? -9.060  -42.061 -7.649  0.85 25.65  ? 163  LEU A N   1 
ATOM   1206 N  N   B LEU A 1 142 ? -9.091  -42.026 -7.705  0.15 28.70  ? 163  LEU A N   1 
ATOM   1207 C  CA  A LEU A 1 142 ? -7.927  -41.556 -8.472  0.85 27.10  ? 163  LEU A CA  1 
ATOM   1208 C  CA  B LEU A 1 142 ? -7.923  -41.550 -8.444  0.15 27.80  ? 163  LEU A CA  1 
ATOM   1209 C  C   A LEU A 1 142 ? -6.700  -42.497 -8.421  0.85 27.26  ? 163  LEU A C   1 
ATOM   1210 C  C   B LEU A 1 142 ? -6.752  -42.520 -8.431  0.15 28.89  ? 163  LEU A C   1 
ATOM   1211 O  O   A LEU A 1 142 ? -5.934  -42.624 -9.394  0.85 31.57  ? 163  LEU A O   1 
ATOM   1212 O  O   B LEU A 1 142 ? -6.082  -42.719 -9.451  0.15 30.15  ? 163  LEU A O   1 
ATOM   1213 C  CB  A LEU A 1 142 ? -7.514  -40.169 -7.939  0.85 30.15  ? 163  LEU A CB  1 
ATOM   1214 C  CB  B LEU A 1 142 ? -7.456  -40.215 -7.874  0.15 27.84  ? 163  LEU A CB  1 
ATOM   1215 C  CG  A LEU A 1 142 ? -6.363  -39.460 -8.607  0.85 26.96  ? 163  LEU A CG  1 
ATOM   1216 C  CG  B LEU A 1 142 ? -7.878  -39.025 -8.721  0.15 23.11  ? 163  LEU A CG  1 
ATOM   1217 C  CD1 A LEU A 1 142 ? -6.688  -39.243 -10.092 0.85 26.41  ? 163  LEU A CD1 1 
ATOM   1218 C  CD1 B LEU A 1 142 ? -7.216  -37.790 -8.141  0.15 25.73  ? 163  LEU A CD1 1 
ATOM   1219 C  CD2 A LEU A 1 142 ? -6.126  -38.115 -7.788  0.85 26.83  ? 163  LEU A CD2 1 
ATOM   1220 C  CD2 B LEU A 1 142 ? -7.491  -39.225 -10.177 0.15 28.16  ? 163  LEU A CD2 1 
ATOM   1221 N  N   . ASP A 1 143 ? -6.497  -43.110 -7.270  1.00 29.98  ? 164  ASP A N   1 
ATOM   1222 C  CA  . ASP A 1 143 ? -5.318  -43.947 -7.123  1.00 33.90  ? 164  ASP A CA  1 
ATOM   1223 C  C   . ASP A 1 143 ? -5.473  -45.305 -7.790  1.00 26.15  ? 164  ASP A C   1 
ATOM   1224 O  O   . ASP A 1 143 ? -6.267  -46.144 -7.335  1.00 28.51  ? 164  ASP A O   1 
ATOM   1225 C  CB  . ASP A 1 143 ? -4.986  -44.137 -5.671  1.00 36.03  ? 164  ASP A CB  1 
ATOM   1226 C  CG  . ASP A 1 143 ? -3.590  -44.688 -5.485  1.00 51.19  ? 164  ASP A CG  1 
ATOM   1227 O  OD1 . ASP A 1 143 ? -2.697  -43.960 -4.941  1.00 51.44  ? 164  ASP A OD1 1 
ATOM   1228 O  OD2 . ASP A 1 143 ? -3.389  -45.834 -5.953  1.00 32.99  ? 164  ASP A OD2 1 
ATOM   1229 N  N   . CYS A 1 144 ? -4.642  -45.529 -8.810  1.00 23.71  ? 165  CYS A N   1 
ATOM   1230 C  CA  . CYS A 1 144 ? -4.753  -46.699 -9.660  1.00 22.55  ? 165  CYS A CA  1 
ATOM   1231 C  C   . CYS A 1 144 ? -3.977  -47.881 -9.081  1.00 24.72  ? 165  CYS A C   1 
ATOM   1232 O  O   . CYS A 1 144 ? -4.124  -49.031 -9.571  1.00 28.55  ? 165  CYS A O   1 
ATOM   1233 C  CB  . CYS A 1 144 ? -4.232  -46.374 -11.057 1.00 28.12  ? 165  CYS A CB  1 
ATOM   1234 S  SG  . CYS A 1 144 ? -5.523  -45.338 -11.920 1.00 32.29  ? 165  CYS A SG  1 
ATOM   1235 N  N   . GLY A 1 145 ? -3.136  -47.604 -8.075  1.00 25.46  ? 166  GLY A N   1 
ATOM   1236 C  CA  . GLY A 1 145 ? -2.369  -48.698 -7.452  1.00 28.64  ? 166  GLY A CA  1 
ATOM   1237 C  C   . GLY A 1 145 ? -0.863  -48.438 -7.455  1.00 28.94  ? 166  GLY A C   1 
ATOM   1238 O  O   . GLY A 1 145 ? -0.423  -47.285 -7.705  1.00 25.89  ? 166  GLY A O   1 
ATOM   1239 N  N   . GLU A 1 146 ? -0.077  -49.489 -7.180  1.00 24.48  ? 167  GLU A N   1 
ATOM   1240 C  CA  . GLU A 1 146 ? 1.353   -49.300 -6.864  1.00 23.03  ? 167  GLU A CA  1 
ATOM   1241 C  C   . GLU A 1 146 ? 2.127   -50.336 -7.635  1.00 27.14  ? 167  GLU A C   1 
ATOM   1242 O  O   . GLU A 1 146 ? 1.807   -51.513 -7.620  1.00 27.54  ? 167  GLU A O   1 
ATOM   1243 C  CB  . GLU A 1 146 ? 1.644   -49.408 -5.359  1.00 28.05  ? 167  GLU A CB  1 
ATOM   1244 C  CG  . GLU A 1 146 ? 3.127   -49.138 -5.048  1.00 28.86  ? 167  GLU A CG  1 
ATOM   1245 C  CD  . GLU A 1 146 ? 3.466   -49.336 -3.573  1.00 48.29  ? 167  GLU A CD  1 
ATOM   1246 O  OE1 . GLU A 1 146 ? 3.029   -50.341 -2.961  1.00 42.94  ? 167  GLU A OE1 1 
ATOM   1247 O  OE2 . GLU A 1 146 ? 4.166   -48.457 -3.046  1.00 40.80  ? 167  GLU A OE2 1 
ATOM   1248 N  N   . ARG A 1 147 ? 3.128   -49.858 -8.355  1.00 23.58  ? 168  ARG A N   1 
ATOM   1249 C  CA  . ARG A 1 147 ? 4.044   -50.733 -9.102  1.00 23.74  ? 168  ARG A CA  1 
ATOM   1250 C  C   . ARG A 1 147 ? 5.267   -51.102 -8.261  1.00 24.98  ? 168  ARG A C   1 
ATOM   1251 O  O   . ARG A 1 147 ? 5.825   -50.218 -7.642  1.00 28.23  ? 168  ARG A O   1 
ATOM   1252 C  CB  . ARG A 1 147 ? 4.538   -50.004 -10.351 1.00 25.71  ? 168  ARG A CB  1 
ATOM   1253 C  CG  . ARG A 1 147 ? 3.401   -49.594 -11.304 1.00 29.72  ? 168  ARG A CG  1 
ATOM   1254 C  CD  . ARG A 1 147 ? 3.360   -50.450 -12.540 1.00 32.81  ? 168  ARG A CD  1 
ATOM   1255 N  NE  . ARG A 1 147 ? 2.109   -50.219 -13.277 1.00 35.90  ? 168  ARG A NE  1 
ATOM   1256 C  CZ  . ARG A 1 147 ? 1.982   -49.278 -14.208 1.00 32.98  ? 168  ARG A CZ  1 
ATOM   1257 N  NH1 . ARG A 1 147 ? 3.002   -48.534 -14.482 1.00 25.51  ? 168  ARG A NH1 1 
ATOM   1258 N  NH2 . ARG A 1 147 ? 0.849   -49.088 -14.875 1.00 30.89  ? 168  ARG A NH2 1 
ATOM   1259 N  N   . HIS A 1 148 ? 5.731   -52.350 -8.315  1.00 26.24  ? 169  HIS A N   1 
ATOM   1260 C  CA  . HIS A 1 148 ? 6.949   -52.713 -7.569  1.00 26.45  ? 169  HIS A CA  1 
ATOM   1261 C  C   . HIS A 1 148 ? 8.017   -52.829 -8.630  1.00 25.61  ? 169  HIS A C   1 
ATOM   1262 O  O   . HIS A 1 148 ? 7.841   -53.618 -9.546  1.00 30.77  ? 169  HIS A O   1 
ATOM   1263 C  CB  . HIS A 1 148 ? 6.776   -54.025 -6.818  1.00 29.03  ? 169  HIS A CB  1 
ATOM   1264 C  CG  . HIS A 1 148 ? 5.814   -53.923 -5.683  1.00 42.15  ? 169  HIS A CG  1 
ATOM   1265 N  ND1 . HIS A 1 148 ? 5.242   -55.030 -5.081  1.00 49.88  ? 169  HIS A ND1 1 
ATOM   1266 C  CD2 . HIS A 1 148 ? 5.297   -52.835 -5.057  1.00 47.12  ? 169  HIS A CD2 1 
ATOM   1267 C  CE1 . HIS A 1 148 ? 4.422   -54.619 -4.127  1.00 51.95  ? 169  HIS A CE1 1 
ATOM   1268 N  NE2 . HIS A 1 148 ? 4.431   -53.296 -4.099  1.00 48.71  ? 169  HIS A NE2 1 
ATOM   1269 N  N   A ILE A 1 149 ? 9.070   -52.008 -8.546  0.40 25.27  ? 170  ILE A N   1 
ATOM   1270 N  N   B ILE A 1 149 ? 9.087   -52.028 -8.538  0.60 24.13  ? 170  ILE A N   1 
ATOM   1271 C  CA  A ILE A 1 149 ? 10.050  -51.897 -9.629  0.40 26.22  ? 170  ILE A CA  1 
ATOM   1272 C  CA  B ILE A 1 149 ? 10.034  -51.912 -9.648  0.60 24.29  ? 170  ILE A CA  1 
ATOM   1273 C  C   A ILE A 1 149 ? 11.415  -52.260 -9.086  0.40 28.60  ? 170  ILE A C   1 
ATOM   1274 C  C   B ILE A 1 149 ? 11.406  -52.244 -9.107  0.60 28.66  ? 170  ILE A C   1 
ATOM   1275 O  O   A ILE A 1 149 ? 11.772  -51.813 -7.994  0.40 28.69  ? 170  ILE A O   1 
ATOM   1276 O  O   B ILE A 1 149 ? 11.755  -51.763 -8.029  0.60 27.22  ? 170  ILE A O   1 
ATOM   1277 C  CB  A ILE A 1 149 ? 10.127  -50.462 -10.219 0.40 30.59  ? 170  ILE A CB  1 
ATOM   1278 C  CB  B ILE A 1 149 ? 10.081  -50.485 -10.259 0.60 29.68  ? 170  ILE A CB  1 
ATOM   1279 C  CG1 A ILE A 1 149 ? 8.814   -50.071 -10.890 0.40 30.69  ? 170  ILE A CG1 1 
ATOM   1280 C  CG1 B ILE A 1 149 ? 8.848   -50.212 -11.113 0.60 31.81  ? 170  ILE A CG1 1 
ATOM   1281 C  CG2 A ILE A 1 149 ? 11.295  -50.337 -11.211 0.40 31.53  ? 170  ILE A CG2 1 
ATOM   1282 C  CG2 B ILE A 1 149 ? 11.349  -50.304 -11.109 0.60 30.69  ? 170  ILE A CG2 1 
ATOM   1283 C  CD1 A ILE A 1 149 ? 8.474   -50.893 -12.116 0.40 25.25  ? 170  ILE A CD1 1 
ATOM   1284 C  CD1 B ILE A 1 149 ? 8.804   -48.799 -11.697 0.60 28.83  ? 170  ILE A CD1 1 
ATOM   1285 N  N   . GLU A 1 150 ? 12.177  -53.076 -9.819  1.00 29.41  ? 171  GLU A N   1 
ATOM   1286 C  CA  . GLU A 1 150 ? 13.547  -53.301 -9.433  1.00 28.09  ? 171  GLU A CA  1 
ATOM   1287 C  C   . GLU A 1 150 ? 14.417  -52.932 -10.611 1.00 33.86  ? 171  GLU A C   1 
ATOM   1288 O  O   . GLU A 1 150 ? 14.088  -53.246 -11.741 1.00 30.87  ? 171  GLU A O   1 
ATOM   1289 C  CB  . GLU A 1 150 ? 13.830  -54.744 -8.961  1.00 34.13  ? 171  GLU A CB  1 
ATOM   1290 C  CG  . GLU A 1 150 ? 13.070  -55.027 -7.685  1.00 36.55  ? 171  GLU A CG  1 
ATOM   1291 C  CD  . GLU A 1 150 ? 13.322  -56.406 -7.125  1.00 40.75  ? 171  GLU A CD  1 
ATOM   1292 O  OE1 . GLU A 1 150 ? 13.744  -57.340 -7.857  1.00 34.12  ? 171  GLU A OE1 1 
ATOM   1293 O  OE2 . GLU A 1 150 ? 13.099  -56.556 -5.915  1.00 44.46  ? 171  GLU A OE2 1 
ATOM   1294 N  N   A VAL A 1 151 ? 15.537  -52.267 -10.337 0.67 29.87  ? 172  VAL A N   1 
ATOM   1295 N  N   B VAL A 1 151 ? 15.519  -52.235 -10.328 0.33 31.19  ? 172  VAL A N   1 
ATOM   1296 C  CA  A VAL A 1 151 ? 16.462  -51.896 -11.409 0.67 30.95  ? 172  VAL A CA  1 
ATOM   1297 C  CA  B VAL A 1 151 ? 16.489  -51.845 -11.354 0.33 32.68  ? 172  VAL A CA  1 
ATOM   1298 C  C   A VAL A 1 151 ? 17.887  -52.074 -10.886 0.67 33.16  ? 172  VAL A C   1 
ATOM   1299 C  C   B VAL A 1 151 ? 17.895  -52.125 -10.848 0.33 34.08  ? 172  VAL A C   1 
ATOM   1300 O  O   A VAL A 1 151 ? 18.173  -51.777 -9.725  0.67 38.13  ? 172  VAL A O   1 
ATOM   1301 O  O   B VAL A 1 151 ? 18.189  -51.910 -9.673  0.33 37.33  ? 172  VAL A O   1 
ATOM   1302 C  CB  A VAL A 1 151 ? 16.210  -50.453 -11.894 0.67 37.20  ? 172  VAL A CB  1 
ATOM   1303 C  CB  B VAL A 1 151 ? 16.381  -50.355 -11.721 0.33 36.99  ? 172  VAL A CB  1 
ATOM   1304 C  CG1 A VAL A 1 151 ? 16.333  -49.487 -10.740 0.67 32.49  ? 172  VAL A CG1 1 
ATOM   1305 C  CG1 B VAL A 1 151 ? 17.242  -50.029 -12.952 0.33 38.25  ? 172  VAL A CG1 1 
ATOM   1306 C  CG2 A VAL A 1 151 ? 17.162  -50.064 -13.055 0.67 36.32  ? 172  VAL A CG2 1 
ATOM   1307 C  CG2 B VAL A 1 151 ? 14.953  -49.988 -11.982 0.33 35.07  ? 172  VAL A CG2 1 
ATOM   1308 N  N   . HIS A 1 152 ? 18.762  -52.613 -11.722 1.00 34.60  ? 173  HIS A N   1 
ATOM   1309 C  CA  . HIS A 1 152 ? 20.160  -52.803 -11.335 1.00 38.38  ? 173  HIS A CA  1 
ATOM   1310 C  C   . HIS A 1 152 ? 20.928  -51.460 -11.391 1.00 43.54  ? 173  HIS A C   1 
ATOM   1311 O  O   . HIS A 1 152 ? 20.644  -50.613 -12.249 1.00 41.60  ? 173  HIS A O   1 
ATOM   1312 C  CB  . HIS A 1 152 ? 20.810  -53.857 -12.229 1.00 41.83  ? 173  HIS A CB  1 
ATOM   1313 C  CG  . HIS A 1 152 ? 20.307  -55.239 -11.957 1.00 51.92  ? 173  HIS A CG  1 
ATOM   1314 N  ND1 . HIS A 1 152 ? 20.831  -56.033 -10.958 1.00 54.08  ? 173  HIS A ND1 1 
ATOM   1315 C  CD2 . HIS A 1 152 ? 19.288  -55.944 -12.503 1.00 47.59  ? 173  HIS A CD2 1 
ATOM   1316 C  CE1 . HIS A 1 152 ? 20.172  -57.176 -10.913 1.00 50.45  ? 173  HIS A CE1 1 
ATOM   1317 N  NE2 . HIS A 1 152 ? 19.249  -57.158 -11.856 1.00 46.46  ? 173  HIS A NE2 1 
ATOM   1318 N  N   . ARG A 1 153 ? 21.859  -51.273 -10.451 1.00 41.68  ? 174  ARG A N   1 
ATOM   1319 C  CA  . ARG A 1 153 ? 22.738  -50.105 -10.431 1.00 42.59  ? 174  ARG A CA  1 
ATOM   1320 C  C   . ARG A 1 153 ? 23.340  -49.847 -11.804 1.00 49.56  ? 174  ARG A C   1 
ATOM   1321 O  O   . ARG A 1 153 ? 23.834  -50.774 -12.456 1.00 48.60  ? 174  ARG A O   1 
ATOM   1322 C  CB  . ARG A 1 153 ? 23.852  -50.291 -9.419  1.00 45.21  ? 174  ARG A CB  1 
ATOM   1323 C  CG  . ARG A 1 153 ? 24.637  -49.021 -9.155  1.00 57.96  ? 174  ARG A CG  1 
ATOM   1324 C  CD  . ARG A 1 153 ? 25.671  -49.324 -8.096  1.00 67.23  ? 174  ARG A CD  1 
ATOM   1325 N  NE  . ARG A 1 153 ? 25.052  -50.106 -7.021  1.00 79.59  ? 174  ARG A NE  1 
ATOM   1326 C  CZ  . ARG A 1 153 ? 25.471  -50.132 -5.754  1.00 83.50  ? 174  ARG A CZ  1 
ATOM   1327 N  NH1 . ARG A 1 153 ? 24.829  -50.878 -4.855  1.00 83.31  ? 174  ARG A NH1 1 
ATOM   1328 N  NH2 . ARG A 1 153 ? 26.521  -49.406 -5.379  1.00 80.62  ? 174  ARG A NH2 1 
ATOM   1329 N  N   . SER A 1 154 ? 23.271  -48.585 -12.228 1.00 52.11  ? 175  SER A N   1 
ATOM   1330 C  CA  . SER A 1 154 ? 23.844  -48.083 -13.487 1.00 57.47  ? 175  SER A CA  1 
ATOM   1331 C  C   . SER A 1 154 ? 22.991  -48.390 -14.738 1.00 55.68  ? 175  SER A C   1 
ATOM   1332 O  O   . SER A 1 154 ? 23.329  -47.936 -15.833 1.00 56.37  ? 175  SER A O   1 
ATOM   1333 C  CB  . SER A 1 154 ? 25.275  -48.606 -13.686 1.00 61.69  ? 175  SER A CB  1 
ATOM   1334 O  OG  . SER A 1 154 ? 26.106  -48.206 -12.608 1.00 61.62  ? 175  SER A OG  1 
ATOM   1335 N  N   . GLU A 1 155 ? 21.899  -49.144 -14.593 1.00 47.89  ? 176  GLU A N   1 
ATOM   1336 C  CA  . GLU A 1 155 ? 20.924  -49.272 -15.687 1.00 43.99  ? 176  GLU A CA  1 
ATOM   1337 C  C   . GLU A 1 155 ? 19.942  -48.098 -15.677 1.00 45.59  ? 176  GLU A C   1 
ATOM   1338 O  O   . GLU A 1 155 ? 19.943  -47.280 -14.760 1.00 48.19  ? 176  GLU A O   1 
ATOM   1339 C  CB  . GLU A 1 155 ? 20.155  -50.602 -15.593 1.00 38.35  ? 176  GLU A CB  1 
ATOM   1340 C  CG  . GLU A 1 155 ? 21.125  -51.812 -15.552 1.00 44.92  ? 176  GLU A CG  1 
ATOM   1341 C  CD  . GLU A 1 155 ? 21.844  -52.073 -16.875 1.00 65.70  ? 176  GLU A CD  1 
ATOM   1342 O  OE1 . GLU A 1 155 ? 21.403  -51.533 -17.912 1.00 71.07  ? 176  GLU A OE1 1 
ATOM   1343 O  OE2 . GLU A 1 155 ? 22.857  -52.818 -16.871 1.00 73.93  ? 176  GLU A OE2 1 
ATOM   1344 N  N   . ASP A 1 156 ? 19.093  -48.018 -16.697 1.00 40.33  ? 177  ASP A N   1 
ATOM   1345 C  CA  . ASP A 1 156 ? 18.091  -46.976 -16.760 1.00 40.26  ? 177  ASP A CA  1 
ATOM   1346 C  C   . ASP A 1 156 ? 16.810  -47.382 -15.999 1.00 42.79  ? 177  ASP A C   1 
ATOM   1347 O  O   . ASP A 1 156 ? 16.310  -48.502 -16.142 1.00 40.59  ? 177  ASP A O   1 
ATOM   1348 C  CB  . ASP A 1 156 ? 17.731  -46.665 -18.209 1.00 44.94  ? 177  ASP A CB  1 
ATOM   1349 C  CG  . ASP A 1 156 ? 18.753  -45.761 -18.912 1.00 60.40  ? 177  ASP A CG  1 
ATOM   1350 O  OD1 . ASP A 1 156 ? 19.832  -45.449 -18.348 1.00 61.28  ? 177  ASP A OD1 1 
ATOM   1351 O  OD2 . ASP A 1 156 ? 18.461  -45.365 -20.063 1.00 64.61  ? 177  ASP A OD2 1 
ATOM   1352 N  N   . LEU A 1 157 ? 16.309  -46.450 -15.200 1.00 40.69  ? 178  LEU A N   1 
ATOM   1353 C  CA  . LEU A 1 157 ? 14.993  -46.515 -14.566 1.00 36.63  ? 178  LEU A CA  1 
ATOM   1354 C  C   . LEU A 1 157 ? 13.910  -45.823 -15.421 1.00 41.20  ? 178  LEU A C   1 
ATOM   1355 O  O   . LEU A 1 157 ? 14.009  -44.640 -15.734 1.00 38.92  ? 178  LEU A O   1 
ATOM   1356 C  CB  . LEU A 1 157 ? 15.061  -45.851 -13.187 1.00 35.47  ? 178  LEU A CB  1 
ATOM   1357 C  CG  . LEU A 1 157 ? 13.692  -45.693 -12.475 1.00 34.58  ? 178  LEU A CG  1 
ATOM   1358 C  CD1 . LEU A 1 157 ? 13.157  -47.048 -11.995 1.00 31.90  ? 178  LEU A CD1 1 
ATOM   1359 C  CD2 . LEU A 1 157 ? 13.722  -44.671 -11.322 1.00 39.90  ? 178  LEU A CD2 1 
ATOM   1360 N  N   . VAL A 1 158 ? 12.879  -46.565 -15.791 1.00 34.12  ? 179  VAL A N   1 
ATOM   1361 C  CA  . VAL A 1 158 ? 11.772  -45.997 -16.554 1.00 31.83  ? 179  VAL A CA  1 
ATOM   1362 C  C   . VAL A 1 158 ? 10.495  -46.206 -15.719 1.00 37.40  ? 179  VAL A C   1 
ATOM   1363 O  O   . VAL A 1 158 ? 10.224  -47.330 -15.243 1.00 33.11  ? 179  VAL A O   1 
ATOM   1364 C  CB  . VAL A 1 158 ? 11.623  -46.648 -17.923 1.00 40.67  ? 179  VAL A CB  1 
ATOM   1365 C  CG1 . VAL A 1 158 ? 10.352  -46.116 -18.626 1.00 34.86  ? 179  VAL A CG1 1 
ATOM   1366 C  CG2 . VAL A 1 158 ? 12.894  -46.399 -18.768 1.00 42.93  ? 179  VAL A CG2 1 
ATOM   1367 N  N   . LEU A 1 159 ? 9.773   -45.123 -15.476 1.00 31.49  ? 180  LEU A N   1 
ATOM   1368 C  CA  . LEU A 1 159 ? 8.451   -45.208 -14.823 1.00 27.07  ? 180  LEU A CA  1 
ATOM   1369 C  C   . LEU A 1 159 ? 7.423   -44.928 -15.928 1.00 32.83  ? 180  LEU A C   1 
ATOM   1370 O  O   . LEU A 1 159 ? 7.530   -43.910 -16.629 1.00 31.56  ? 180  LEU A O   1 
ATOM   1371 C  CB  . LEU A 1 159 ? 8.292   -44.197 -13.702 1.00 24.84  ? 180  LEU A CB  1 
ATOM   1372 C  CG  . LEU A 1 159 ? 9.418   -44.066 -12.660 1.00 34.67  ? 180  LEU A CG  1 
ATOM   1373 C  CD1 . LEU A 1 159 ? 9.112   -42.972 -11.634 1.00 30.48  ? 180  LEU A CD1 1 
ATOM   1374 C  CD2 . LEU A 1 159 ? 9.585   -45.392 -11.977 1.00 32.97  ? 180  LEU A CD2 1 
ATOM   1375 N  N   . ASP A 1 160 ? 6.454   -45.821 -16.060 1.00 26.50  ? 181  ASP A N   1 
ATOM   1376 C  CA  . ASP A 1 160 ? 5.419   -45.728 -17.097 1.00 27.25  ? 181  ASP A CA  1 
ATOM   1377 C  C   . ASP A 1 160 ? 4.113   -45.296 -16.450 1.00 30.71  ? 181  ASP A C   1 
ATOM   1378 O  O   . ASP A 1 160 ? 3.687   -45.899 -15.468 1.00 30.45  ? 181  ASP A O   1 
ATOM   1379 C  CB  . ASP A 1 160 ? 5.233   -47.053 -17.777 1.00 31.62  ? 181  ASP A CB  1 
ATOM   1380 C  CG  . ASP A 1 160 ? 4.278   -46.982 -18.960 1.00 46.90  ? 181  ASP A CG  1 
ATOM   1381 O  OD1 . ASP A 1 160 ? 3.815   -45.880 -19.341 1.00 44.59  ? 181  ASP A OD1 1 
ATOM   1382 O  OD2 . ASP A 1 160 ? 4.057   -48.050 -19.546 1.00 48.72  ? 181  ASP A OD2 1 
ATOM   1383 N  N   . CYS A 1 161 ? 3.507   -44.228 -16.946 1.00 26.08  ? 182  CYS A N   1 
ATOM   1384 C  CA  . CYS A 1 161 ? 2.226   -43.799 -16.349 1.00 26.14  ? 182  CYS A CA  1 
ATOM   1385 C  C   . CYS A 1 161 ? 1.081   -43.887 -17.374 1.00 26.09  ? 182  CYS A C   1 
ATOM   1386 O  O   . CYS A 1 161 ? -0.013  -43.405 -17.138 1.00 25.80  ? 182  CYS A O   1 
ATOM   1387 C  CB  . CYS A 1 161 ? 2.343   -42.361 -15.817 1.00 26.56  ? 182  CYS A CB  1 
ATOM   1388 S  SG  . CYS A 1 161 ? 0.903   -41.791 -14.873 1.00 28.37  ? 182  CYS A SG  1 
ATOM   1389 N  N   . LEU A 1 162 ? 1.363   -44.476 -18.523 1.00 25.47  ? 183  LEU A N   1 
ATOM   1390 C  CA  . LEU A 1 162 ? 0.334   -44.548 -19.572 1.00 26.66  ? 183  LEU A CA  1 
ATOM   1391 C  C   . LEU A 1 162 ? -0.703  -45.668 -19.306 1.00 31.14  ? 183  LEU A C   1 
ATOM   1392 O  O   . LEU A 1 162 ? -0.309  -46.830 -19.103 1.00 30.79  ? 183  LEU A O   1 
ATOM   1393 C  CB  . LEU A 1 162 ? 0.992   -44.790 -20.919 1.00 27.53  ? 183  LEU A CB  1 
ATOM   1394 C  CG  . LEU A 1 162 ? 0.052   -44.794 -22.158 1.00 27.31  ? 183  LEU A CG  1 
ATOM   1395 C  CD1 . LEU A 1 162 ? -0.523  -43.429 -22.433 1.00 29.16  ? 183  LEU A CD1 1 
ATOM   1396 C  CD2 . LEU A 1 162 ? 0.834   -45.307 -23.362 1.00 33.39  ? 183  LEU A CD2 1 
ATOM   1397 N  N   . LEU A 1 163 ? -1.998  -45.308 -19.293 1.00 25.25  ? 184  LEU A N   1 
ATOM   1398 C  CA  . LEU A 1 163 ? -3.075  -46.317 -19.252 1.00 23.23  ? 184  LEU A CA  1 
ATOM   1399 C  C   . LEU A 1 163 ? -3.767  -46.331 -20.620 1.00 29.49  ? 184  LEU A C   1 
ATOM   1400 O  O   . LEU A 1 163 ? -3.747  -45.340 -21.360 1.00 27.52  ? 184  LEU A O   1 
ATOM   1401 C  CB  . LEU A 1 163 ? -4.104  -45.983 -18.145 1.00 23.91  ? 184  LEU A CB  1 
ATOM   1402 C  CG  . LEU A 1 163 ? -3.482  -45.812 -16.742 1.00 29.09  ? 184  LEU A CG  1 
ATOM   1403 C  CD1 . LEU A 1 163 ? -4.640  -45.592 -15.726 1.00 27.64  ? 184  LEU A CD1 1 
ATOM   1404 C  CD2 . LEU A 1 163 ? -2.715  -47.050 -16.403 1.00 32.13  ? 184  LEU A CD2 1 
ATOM   1405 N  N   . SER A 1 164 ? -4.432  -47.435 -20.931 1.00 27.21  ? 185  SER A N   1 
ATOM   1406 C  CA  . SER A 1 164 ? -4.907  -47.635 -22.272 1.00 32.50  ? 185  SER A CA  1 
ATOM   1407 C  C   . SER A 1 164 ? -5.957  -46.609 -22.665 1.00 33.09  ? 185  SER A C   1 
ATOM   1408 O  O   . SER A 1 164 ? -6.185  -46.371 -23.848 1.00 31.43  ? 185  SER A O   1 
ATOM   1409 C  CB  . SER A 1 164 ? -5.481  -49.060 -22.414 1.00 36.28  ? 185  SER A CB  1 
ATOM   1410 O  OG  . SER A 1 164 ? -6.549  -49.195 -21.493 1.00 40.41  ? 185  SER A OG  1 
ATOM   1411 N  N   . TRP A 1 165 ? -6.614  -45.993 -21.691 1.00 28.94  ? 186  TRP A N   1 
ATOM   1412 C  CA  . TRP A 1 165 ? -7.762  -45.115 -22.026 1.00 27.09  ? 186  TRP A CA  1 
ATOM   1413 C  C   . TRP A 1 165 ? -7.283  -43.633 -22.090 1.00 25.91  ? 186  TRP A C   1 
ATOM   1414 O  O   . TRP A 1 165 ? -8.026  -42.744 -22.493 1.00 26.92  ? 186  TRP A O   1 
ATOM   1415 C  CB  . TRP A 1 165 ? -8.909  -45.334 -21.003 1.00 28.41  ? 186  TRP A CB  1 
ATOM   1416 C  CG  . TRP A 1 165 ? -8.508  -45.175 -19.529 1.00 27.28  ? 186  TRP A CG  1 
ATOM   1417 C  CD1 . TRP A 1 165 ? -8.173  -46.174 -18.636 1.00 28.20  ? 186  TRP A CD1 1 
ATOM   1418 C  CD2 . TRP A 1 165 ? -8.433  -43.952 -18.811 1.00 24.51  ? 186  TRP A CD2 1 
ATOM   1419 N  NE1 . TRP A 1 165 ? -7.866  -45.615 -17.395 1.00 24.72  ? 186  TRP A NE1 1 
ATOM   1420 C  CE2 . TRP A 1 165 ? -8.008  -44.252 -17.488 1.00 24.91  ? 186  TRP A CE2 1 
ATOM   1421 C  CE3 . TRP A 1 165 ? -8.628  -42.606 -19.171 1.00 23.19  ? 186  TRP A CE3 1 
ATOM   1422 C  CZ2 . TRP A 1 165 ? -7.816  -43.242 -16.507 1.00 22.59  ? 186  TRP A CZ2 1 
ATOM   1423 C  CZ3 . TRP A 1 165 ? -8.463  -41.624 -18.228 1.00 21.93  ? 186  TRP A CZ3 1 
ATOM   1424 C  CH2 . TRP A 1 165 ? -8.069  -41.935 -16.872 1.00 24.67  ? 186  TRP A CH2 1 
ATOM   1425 N  N   . HIS A 1 166 ? -6.030  -43.372 -21.688 1.00 25.64  ? 187  HIS A N   1 
ATOM   1426 C  CA  . HIS A 1 166 ? -5.550  -41.980 -21.704 1.00 25.85  ? 187  HIS A CA  1 
ATOM   1427 C  C   . HIS A 1 166 ? -5.604  -41.390 -23.080 1.00 28.48  ? 187  HIS A C   1 
ATOM   1428 O  O   . HIS A 1 166 ? -6.006  -40.241 -23.202 1.00 29.83  ? 187  HIS A O   1 
ATOM   1429 C  CB  . HIS A 1 166 ? -4.094  -41.839 -21.187 1.00 27.54  ? 187  HIS A CB  1 
ATOM   1430 C  CG  . HIS A 1 166 ? -3.952  -42.085 -19.720 1.00 28.34  ? 187  HIS A CG  1 
ATOM   1431 N  ND1 . HIS A 1 166 ? -2.723  -42.209 -19.105 1.00 26.62  ? 187  HIS A ND1 1 
ATOM   1432 C  CD2 . HIS A 1 166 ? -4.886  -42.176 -18.737 1.00 25.83  ? 187  HIS A CD2 1 
ATOM   1433 C  CE1 . HIS A 1 166 ? -2.904  -42.403 -17.804 1.00 29.18  ? 187  HIS A CE1 1 
ATOM   1434 N  NE2 . HIS A 1 166 ? -4.209  -42.400 -17.562 1.00 26.00  ? 187  HIS A NE2 1 
ATOM   1435 N  N   . ARG A 1 167 ? -5.256  -42.199 -24.091 1.00 29.42  ? 188  ARG A N   1 
ATOM   1436 C  CA  . ARG A 1 167 ? -5.238  -41.693 -25.476 1.00 37.54  ? 188  ARG A CA  1 
ATOM   1437 C  C   . ARG A 1 167 ? -6.630  -41.218 -25.892 1.00 41.36  ? 188  ARG A C   1 
ATOM   1438 O  O   . ARG A 1 167 ? -6.727  -40.259 -26.647 1.00 49.01  ? 188  ARG A O   1 
ATOM   1439 C  CB  . ARG A 1 167 ? -4.722  -42.752 -26.453 1.00 40.42  ? 188  ARG A CB  1 
ATOM   1440 N  N   . ALA A 1 168 ? -7.705  -41.826 -25.361 1.00 37.14  ? 189  ALA A N   1 
ATOM   1441 C  CA  . ALA A 1 168 ? -9.078  -41.402 -25.742 1.00 34.05  ? 189  ALA A CA  1 
ATOM   1442 C  C   . ALA A 1 168 ? -9.674  -40.341 -24.801 1.00 35.45  ? 189  ALA A C   1 
ATOM   1443 O  O   . ALA A 1 168 ? -10.713 -39.735 -25.117 1.00 41.49  ? 189  ALA A O   1 
ATOM   1444 C  CB  . ALA A 1 168 ? -10.013 -42.597 -25.835 1.00 34.20  ? 189  ALA A CB  1 
ATOM   1445 N  N   . SER A 1 169 ? -9.009  -40.040 -23.691 1.00 24.80  ? 190  SER A N   1 
ATOM   1446 C  CA  . SER A 1 169 ? -9.622  -39.141 -22.727 1.00 24.31  ? 190  SER A CA  1 
ATOM   1447 C  C   . SER A 1 169 ? -9.444  -37.707 -23.215 1.00 31.57  ? 190  SER A C   1 
ATOM   1448 O  O   . SER A 1 169 ? -8.449  -37.401 -23.882 1.00 31.72  ? 190  SER A O   1 
ATOM   1449 C  CB  . SER A 1 169 ? -9.025  -39.360 -21.308 1.00 26.01  ? 190  SER A CB  1 
ATOM   1450 O  OG  . SER A 1 169 ? -9.839  -38.750 -20.296 1.00 26.68  ? 190  SER A OG  1 
ATOM   1451 N  N   . LYS A 1 170 ? -10.401 -36.836 -22.907 1.00 28.49  ? 191  LYS A N   1 
ATOM   1452 C  CA  . LYS A 1 170 ? -10.369 -35.438 -23.368 1.00 25.06  ? 191  LYS A CA  1 
ATOM   1453 C  C   . LYS A 1 170 ? -9.861  -34.478 -22.304 1.00 29.20  ? 191  LYS A C   1 
ATOM   1454 O  O   . LYS A 1 170 ? -10.101 -34.662 -21.139 1.00 28.44  ? 191  LYS A O   1 
ATOM   1455 C  CB  . LYS A 1 170 ? -11.753 -34.971 -23.812 1.00 25.01  ? 191  LYS A CB  1 
ATOM   1456 C  CG  . LYS A 1 170 ? -12.392 -35.857 -24.883 1.00 29.23  ? 191  LYS A CG  1 
ATOM   1457 C  CD  . LYS A 1 170 ? -11.654 -35.858 -26.230 1.00 30.27  ? 191  LYS A CD  1 
ATOM   1458 C  CE  . LYS A 1 170 ? -12.290 -36.926 -27.054 1.00 41.15  ? 191  LYS A CE  1 
ATOM   1459 N  NZ  . LYS A 1 170 ? -11.465 -37.226 -28.215 1.00 44.82  ? 191  LYS A NZ  1 
ATOM   1460 N  N   . GLY A 1 171 ? -9.179  -33.425 -22.727 1.00 25.88  ? 192  GLY A N   1 
ATOM   1461 C  CA  . GLY A 1 171 ? -8.765  -32.421 -21.779 1.00 24.30  ? 192  GLY A CA  1 
ATOM   1462 C  C   . GLY A 1 171 ? -7.562  -32.767 -20.907 1.00 28.77  ? 192  GLY A C   1 
ATOM   1463 O  O   . GLY A 1 171 ? -7.358  -32.122 -19.901 1.00 27.63  ? 192  GLY A O   1 
ATOM   1464 N  N   . LEU A 1 172 ? -6.749  -33.760 -21.284 1.00 29.18  ? 193  LEU A N   1 
ATOM   1465 C  CA  . LEU A 1 172 ? -5.569  -34.036 -20.441 1.00 24.73  ? 193  LEU A CA  1 
ATOM   1466 C  C   . LEU A 1 172 ? -4.545  -32.918 -20.622 1.00 27.51  ? 193  LEU A C   1 
ATOM   1467 O  O   . LEU A 1 172 ? -4.426  -32.359 -21.753 1.00 27.82  ? 193  LEU A O   1 
ATOM   1468 C  CB  . LEU A 1 172 ? -4.898  -35.351 -20.833 1.00 26.36  ? 193  LEU A CB  1 
ATOM   1469 C  CG  . LEU A 1 172 ? -5.755  -36.607 -20.509 1.00 25.44  ? 193  LEU A CG  1 
ATOM   1470 C  CD1 . LEU A 1 172 ? -5.026  -37.793 -21.135 1.00 29.03  ? 193  LEU A CD1 1 
ATOM   1471 C  CD2 . LEU A 1 172 ? -5.964  -36.756 -19.029 1.00 23.04  ? 193  LEU A CD2 1 
ATOM   1472 N  N   . THR A 1 173 ? -3.779  -32.647 -19.585 1.00 34.44  ? 194  THR A N   1 
ATOM   1473 C  CA  . THR A 1 173 ? -2.709  -31.675 -19.696 1.00 35.58  ? 194  THR A CA  1 
ATOM   1474 C  C   . THR A 1 173 ? -1.363  -32.380 -19.544 1.00 39.07  ? 194  THR A C   1 
ATOM   1475 O  O   . THR A 1 173 ? -0.841  -32.893 -20.510 1.00 56.91  ? 194  THR A O   1 
ATOM   1476 C  CB  . THR A 1 173 ? -2.880  -30.510 -18.692 1.00 35.75  ? 194  THR A CB  1 
ATOM   1477 O  OG1 . THR A 1 173 ? -3.053  -31.000 -17.361 1.00 34.72  ? 194  THR A OG1 1 
ATOM   1478 C  CG2 . THR A 1 173 ? -4.153  -29.730 -19.050 1.00 35.97  ? 194  THR A CG2 1 
ATOM   1479 N  N   . ASP A 1 174 ? -0.776  -32.385 -18.368 1.00 30.35  ? 195  ASP A N   1 
ATOM   1480 C  CA  . ASP A 1 174 ? 0.586   -32.933 -18.224 1.00 29.44  ? 195  ASP A CA  1 
ATOM   1481 C  C   . ASP A 1 174 ? 0.566   -34.152 -17.315 1.00 26.54  ? 195  ASP A C   1 
ATOM   1482 O  O   . ASP A 1 174 ? -0.252  -34.239 -16.407 1.00 28.73  ? 195  ASP A O   1 
ATOM   1483 C  CB  . ASP A 1 174 ? 1.556   -31.907 -17.563 1.00 30.59  ? 195  ASP A CB  1 
ATOM   1484 C  CG  . ASP A 1 174 ? 1.921   -30.772 -18.466 1.00 44.70  ? 195  ASP A CG  1 
ATOM   1485 O  OD1 . ASP A 1 174 ? 2.102   -30.977 -19.678 1.00 46.67  ? 195  ASP A OD1 1 
ATOM   1486 O  OD2 . ASP A 1 174 ? 2.044   -29.653 -17.949 1.00 58.84  ? 195  ASP A OD2 1 
ATOM   1487 N  N   . TYR A 1 175 ? 1.547   -35.023 -17.515 1.00 29.24  ? 196  TYR A N   1 
ATOM   1488 C  CA  . TYR A 1 175 ? 1.946   -36.016 -16.506 1.00 28.44  ? 196  TYR A CA  1 
ATOM   1489 C  C   . TYR A 1 175 ? 3.042   -35.377 -15.658 1.00 27.15  ? 196  TYR A C   1 
ATOM   1490 O  O   . TYR A 1 175 ? 4.093   -34.957 -16.221 1.00 29.25  ? 196  TYR A O   1 
ATOM   1491 C  CB  . TYR A 1 175 ? 2.521   -37.258 -17.164 1.00 27.18  ? 196  TYR A CB  1 
ATOM   1492 C  CG  . TYR A 1 175 ? 1.571   -38.065 -18.011 1.00 25.68  ? 196  TYR A CG  1 
ATOM   1493 C  CD1 . TYR A 1 175 ? 1.324   -37.737 -19.338 1.00 30.19  ? 196  TYR A CD1 1 
ATOM   1494 C  CD2 . TYR A 1 175 ? 0.961   -39.188 -17.486 1.00 29.60  ? 196  TYR A CD2 1 
ATOM   1495 C  CE1 . TYR A 1 175 ? 0.458   -38.538 -20.149 1.00 29.22  ? 196  TYR A CE1 1 
ATOM   1496 C  CE2 . TYR A 1 175 ? 0.108   -39.972 -18.270 1.00 22.73  ? 196  TYR A CE2 1 
ATOM   1497 C  CZ  . TYR A 1 175 ? -0.138  -39.660 -19.578 1.00 26.23  ? 196  TYR A CZ  1 
ATOM   1498 O  OH  . TYR A 1 175 ? -1.007  -40.460 -20.326 1.00 29.93  ? 196  TYR A OH  1 
ATOM   1499 N  N   . SER A 1 176 ? 2.819   -35.325 -14.337 1.00 26.43  ? 197  SER A N   1 
ATOM   1500 C  CA  . SER A 1 176 ? 3.868   -34.866 -13.405 1.00 30.58  ? 197  SER A CA  1 
ATOM   1501 C  C   . SER A 1 176 ? 4.450   -36.092 -12.723 1.00 31.48  ? 197  SER A C   1 
ATOM   1502 O  O   . SER A 1 176 ? 3.686   -36.964 -12.314 1.00 29.40  ? 197  SER A O   1 
ATOM   1503 C  CB  . SER A 1 176 ? 3.278   -33.911 -12.360 1.00 28.96  ? 197  SER A CB  1 
ATOM   1504 O  OG  . SER A 1 176 ? 2.911   -32.674 -12.973 1.00 30.61  ? 197  SER A OG  1 
ATOM   1505 N  N   . PHE A 1 177 ? 5.774   -36.172 -12.608 1.00 27.04  ? 198  PHE A N   1 
ATOM   1506 C  CA  . PHE A 1 177 ? 6.358   -37.208 -11.776 1.00 26.36  ? 198  PHE A CA  1 
ATOM   1507 C  C   . PHE A 1 177 ? 7.011   -36.552 -10.563 1.00 28.92  ? 198  PHE A C   1 
ATOM   1508 O  O   . PHE A 1 177 ? 7.751   -35.547 -10.694 1.00 29.30  ? 198  PHE A O   1 
ATOM   1509 C  CB  . PHE A 1 177 ? 7.391   -38.021 -12.555 1.00 26.69  ? 198  PHE A CB  1 
ATOM   1510 C  CG  . PHE A 1 177 ? 6.790   -38.864 -13.615 1.00 30.62  ? 198  PHE A CG  1 
ATOM   1511 C  CD1 . PHE A 1 177 ? 6.491   -40.194 -13.355 1.00 27.03  ? 198  PHE A CD1 1 
ATOM   1512 C  CD2 . PHE A 1 177 ? 6.489   -38.335 -14.861 1.00 28.27  ? 198  PHE A CD2 1 
ATOM   1513 C  CE1 . PHE A 1 177 ? 5.904   -41.032 -14.354 1.00 22.48  ? 198  PHE A CE1 1 
ATOM   1514 C  CE2 . PHE A 1 177 ? 5.891   -39.173 -15.893 1.00 28.86  ? 198  PHE A CE2 1 
ATOM   1515 C  CZ  . PHE A 1 177 ? 5.625   -40.531 -15.627 1.00 24.34  ? 198  PHE A CZ  1 
ATOM   1516 N  N   . TYR A 1 178 ? 6.778   -37.179 -9.405  1.00 28.67  ? 199  TYR A N   1 
ATOM   1517 C  CA  . TYR A 1 178 ? 7.358   -36.774 -8.131  1.00 27.80  ? 199  TYR A CA  1 
ATOM   1518 C  C   . TYR A 1 178 ? 8.239   -37.832 -7.520  1.00 34.51  ? 199  TYR A C   1 
ATOM   1519 O  O   . TYR A 1 178 ? 7.913   -39.009 -7.538  1.00 28.20  ? 199  TYR A O   1 
ATOM   1520 C  CB  . TYR A 1 178 ? 6.279   -36.435 -7.073  1.00 28.17  ? 199  TYR A CB  1 
ATOM   1521 C  CG  . TYR A 1 178 ? 5.399   -35.298 -7.511  1.00 32.74  ? 199  TYR A CG  1 
ATOM   1522 C  CD1 . TYR A 1 178 ? 4.265   -35.523 -8.282  1.00 34.96  ? 199  TYR A CD1 1 
ATOM   1523 C  CD2 . TYR A 1 178 ? 5.713   -33.987 -7.164  1.00 30.17  ? 199  TYR A CD2 1 
ATOM   1524 C  CE1 . TYR A 1 178 ? 3.438   -34.425 -8.673  1.00 29.46  ? 199  TYR A CE1 1 
ATOM   1525 C  CE2 . TYR A 1 178 ? 4.905   -32.894 -7.582  1.00 28.14  ? 199  TYR A CE2 1 
ATOM   1526 C  CZ  . TYR A 1 178 ? 3.796   -33.142 -8.304  1.00 29.94  ? 199  TYR A CZ  1 
ATOM   1527 O  OH  . TYR A 1 178 ? 3.048   -32.076 -8.676  1.00 44.63  ? 199  TYR A OH  1 
ATOM   1528 N  N   . ARG A 1 179 ? 9.311   -37.379 -6.902  1.00 27.16  ? 200  ARG A N   1 
ATOM   1529 C  CA  . ARG A 1 179 ? 10.056  -38.234 -5.958  1.00 25.67  ? 200  ARG A CA  1 
ATOM   1530 C  C   . ARG A 1 179 ? 9.389   -38.064 -4.592  1.00 29.85  ? 200  ARG A C   1 
ATOM   1531 O  O   . ARG A 1 179 ? 9.151   -36.933 -4.151  1.00 35.93  ? 200  ARG A O   1 
ATOM   1532 C  CB  . ARG A 1 179 ? 11.530  -37.812 -5.928  1.00 27.94  ? 200  ARG A CB  1 
ATOM   1533 C  CG  . ARG A 1 179 ? 12.370  -38.602 -4.953  1.00 33.20  ? 200  ARG A CG  1 
ATOM   1534 C  CD  . ARG A 1 179 ? 12.611  -40.031 -5.505  1.00 35.65  ? 200  ARG A CD  1 
ATOM   1535 N  NE  . ARG A 1 179 ? 13.438  -40.822 -4.597  1.00 44.36  ? 200  ARG A NE  1 
ATOM   1536 C  CZ  . ARG A 1 179 ? 14.767  -40.872 -4.662  1.00 45.21  ? 200  ARG A CZ  1 
ATOM   1537 N  NH1 . ARG A 1 179 ? 15.433  -40.177 -5.614  1.00 45.81  ? 200  ARG A NH1 1 
ATOM   1538 N  NH2 . ARG A 1 179 ? 15.430  -41.611 -3.773  1.00 45.79  ? 200  ARG A NH2 1 
ATOM   1539 N  N   . VAL A 1 180 ? 9.066   -39.172 -3.923  1.00 30.06  ? 201  VAL A N   1 
ATOM   1540 C  CA  . VAL A 1 180 ? 8.437   -39.090 -2.588  1.00 31.78  ? 201  VAL A CA  1 
ATOM   1541 C  C   . VAL A 1 180 ? 9.417   -39.499 -1.515  1.00 34.54  ? 201  VAL A C   1 
ATOM   1542 O  O   . VAL A 1 180 ? 9.776   -40.662 -1.446  1.00 31.13  ? 201  VAL A O   1 
ATOM   1543 C  CB  . VAL A 1 180 ? 7.189   -40.030 -2.496  1.00 30.34  ? 201  VAL A CB  1 
ATOM   1544 C  CG1 . VAL A 1 180 ? 6.540   -39.837 -1.127  1.00 31.20  ? 201  VAL A CG1 1 
ATOM   1545 C  CG2 . VAL A 1 180 ? 6.237   -39.751 -3.622  1.00 33.44  ? 201  VAL A CG2 1 
ATOM   1546 N  N   . TRP A 1 181 ? 9.902   -38.552 -0.706  1.00 28.29  ? 202  TRP A N   1 
ATOM   1547 C  CA  . TRP A 1 181 ? 10.963  -38.811 0.239   1.00 29.44  ? 202  TRP A CA  1 
ATOM   1548 C  C   . TRP A 1 181 ? 10.464  -39.576 1.471   1.00 32.76  ? 202  TRP A C   1 
ATOM   1549 O  O   . TRP A 1 181 ? 9.266   -39.717 1.658   1.00 38.63  ? 202  TRP A O   1 
ATOM   1550 C  CB  . TRP A 1 181 ? 11.587  -37.472 0.678   1.00 34.04  ? 202  TRP A CB  1 
ATOM   1551 C  CG  . TRP A 1 181 ? 12.039  -36.680 -0.545  1.00 35.94  ? 202  TRP A CG  1 
ATOM   1552 C  CD1 . TRP A 1 181 ? 11.471  -35.563 -1.055  1.00 38.08  ? 202  TRP A CD1 1 
ATOM   1553 C  CD2 . TRP A 1 181 ? 13.137  -37.010 -1.411  1.00 37.19  ? 202  TRP A CD2 1 
ATOM   1554 N  NE1 . TRP A 1 181 ? 12.177  -35.127 -2.155  1.00 35.09  ? 202  TRP A NE1 1 
ATOM   1555 C  CE2 . TRP A 1 181 ? 13.208  -35.996 -2.395  1.00 37.56  ? 202  TRP A CE2 1 
ATOM   1556 C  CE3 . TRP A 1 181 ? 14.107  -38.032 -1.411  1.00 42.12  ? 202  TRP A CE3 1 
ATOM   1557 C  CZ2 . TRP A 1 181 ? 14.185  -35.992 -3.406  1.00 39.86  ? 202  TRP A CZ2 1 
ATOM   1558 C  CZ3 . TRP A 1 181 ? 15.091  -38.022 -2.400  1.00 46.50  ? 202  TRP A CZ3 1 
ATOM   1559 C  CH2 . TRP A 1 181 ? 15.110  -37.010 -3.397  1.00 41.42  ? 202  TRP A CH2 1 
ATOM   1560 N  N   . GLU A 1 182 ? 11.405  -39.990 2.292   1.00 36.43  ? 203  GLU A N   1 
ATOM   1561 C  CA  . GLU A 1 182 ? 11.138  -40.838 3.448   1.00 43.55  ? 203  GLU A CA  1 
ATOM   1562 C  C   . GLU A 1 182 ? 10.416  -40.045 4.512   1.00 43.42  ? 203  GLU A C   1 
ATOM   1563 O  O   . GLU A 1 182 ? 9.904   -40.642 5.441   1.00 46.62  ? 203  GLU A O   1 
ATOM   1564 C  CB  . GLU A 1 182 ? 12.446  -41.440 3.999   1.00 42.33  ? 203  GLU A CB  1 
ATOM   1565 C  CG  . GLU A 1 182 ? 12.956  -42.565 3.046   1.00 62.55  ? 203  GLU A CG  1 
ATOM   1566 C  CD  . GLU A 1 182 ? 14.404  -42.963 3.286   1.00 73.58  ? 203  GLU A CD  1 
ATOM   1567 O  OE1 . GLU A 1 182 ? 15.226  -42.081 3.621   1.00 77.76  ? 203  GLU A OE1 1 
ATOM   1568 O  OE2 . GLU A 1 182 ? 14.729  -44.164 3.125   1.00 79.04  ? 203  GLU A OE2 1 
ATOM   1569 N  N   . ASN A 1 183 ? 10.370  -38.712 4.386   1.00 40.58  ? 204  ASN A N   1 
ATOM   1570 C  CA  . ASN A 1 183 ? 9.692   -37.891 5.406   1.00 47.66  ? 204  ASN A CA  1 
ATOM   1571 C  C   . ASN A 1 183 ? 8.377   -37.527 4.852   1.00 42.84  ? 204  ASN A C   1 
ATOM   1572 O  O   . ASN A 1 183 ? 7.706   -36.603 5.327   1.00 48.68  ? 204  ASN A O   1 
ATOM   1573 C  CB  . ASN A 1 183 ? 10.446  -36.633 5.753   1.00 45.15  ? 204  ASN A CB  1 
ATOM   1574 C  CG  . ASN A 1 183 ? 10.970  -35.947 4.533   1.00 39.56  ? 204  ASN A CG  1 
ATOM   1575 O  OD1 . ASN A 1 183 ? 10.352  -35.933 3.457   1.00 38.10  ? 204  ASN A OD1 1 
ATOM   1576 N  ND2 . ASN A 1 183 ? 12.177  -35.495 4.657   1.00 57.47  ? 204  ASN A ND2 1 
ATOM   1577 N  N   . SER A 1 184 ? 8.099   -38.196 3.743   1.00 43.49  ? 205  SER A N   1 
ATOM   1578 C  CA  . SER A 1 184 ? 6.826   -38.168 3.032   1.00 47.99  ? 205  SER A CA  1 
ATOM   1579 C  C   . SER A 1 184 ? 6.590   -36.878 2.178   1.00 49.00  ? 205  SER A C   1 
ATOM   1580 O  O   . SER A 1 184 ? 5.627   -36.798 1.460   1.00 47.13  ? 205  SER A O   1 
ATOM   1581 C  CB  . SER A 1 184 ? 5.666   -38.416 4.030   1.00 54.57  ? 205  SER A CB  1 
ATOM   1582 O  OG  . SER A 1 184 ? 5.547   -39.825 4.371   1.00 52.03  ? 205  SER A OG  1 
ATOM   1583 N  N   . SER A 1 185 ? 7.468   -35.888 2.236   1.00 42.50  ? 206  SER A N   1 
ATOM   1584 C  CA  . SER A 1 185 ? 7.357   -34.766 1.303   1.00 40.61  ? 206  SER A CA  1 
ATOM   1585 C  C   . SER A 1 185 ? 7.744   -35.183 -0.112  1.00 40.22  ? 206  SER A C   1 
ATOM   1586 O  O   . SER A 1 185 ? 8.284   -36.252 -0.334  1.00 37.18  ? 206  SER A O   1 
ATOM   1587 C  CB  . SER A 1 185 ? 8.233   -33.629 1.733   1.00 41.89  ? 206  SER A CB  1 
ATOM   1588 O  OG  . SER A 1 185 ? 9.596   -33.995 1.568   1.00 45.92  ? 206  SER A OG  1 
ATOM   1589 N  N   . GLU A 1 186 ? 7.474   -34.333 -1.087  1.00 31.48  ? 207  GLU A N   1 
ATOM   1590 C  CA  . GLU A 1 186 ? 7.777   -34.780 -2.452  1.00 28.98  ? 207  GLU A CA  1 
ATOM   1591 C  C   . GLU A 1 186 ? 8.401   -33.670 -3.287  1.00 36.34  ? 207  GLU A C   1 
ATOM   1592 O  O   . GLU A 1 186 ? 8.246   -32.502 -2.973  1.00 35.05  ? 207  GLU A O   1 
ATOM   1593 C  CB  . GLU A 1 186 ? 6.542   -35.368 -3.173  1.00 35.96  ? 207  GLU A CB  1 
ATOM   1594 C  CG  . GLU A 1 186 ? 5.312   -34.545 -3.156  1.00 50.50  ? 207  GLU A CG  1 
ATOM   1595 C  CD  . GLU A 1 186 ? 4.194   -35.153 -4.011  1.00 53.84  ? 207  GLU A CD  1 
ATOM   1596 O  OE1 . GLU A 1 186 ? 4.126   -36.414 -4.190  1.00 46.71  ? 207  GLU A OE1 1 
ATOM   1597 O  OE2 . GLU A 1 186 ? 3.388   -34.346 -4.517  1.00 58.03  ? 207  GLU A OE2 1 
ATOM   1598 N  N   . THR A 1 187 ? 9.144   -34.074 -4.318  1.00 32.98  ? 208  THR A N   1 
ATOM   1599 C  CA  . THR A 1 187 ? 9.813   -33.127 -5.199  1.00 37.80  ? 208  THR A CA  1 
ATOM   1600 C  C   . THR A 1 187 ? 9.395   -33.424 -6.638  1.00 32.77  ? 208  THR A C   1 
ATOM   1601 O  O   . THR A 1 187 ? 9.441   -34.584 -7.092  1.00 31.26  ? 208  THR A O   1 
ATOM   1602 C  CB  . THR A 1 187 ? 11.325  -33.206 -5.078  1.00 32.90  ? 208  THR A CB  1 
ATOM   1603 O  OG1 . THR A 1 187 ? 11.743  -32.869 -3.748  1.00 40.00  ? 208  THR A OG1 1 
ATOM   1604 C  CG2 . THR A 1 187 ? 12.002  -32.204 -6.096  1.00 40.92  ? 208  THR A CG2 1 
ATOM   1605 N  N   . LEU A 1 188 ? 8.964   -32.399 -7.354  1.00 30.53  ? 209  LEU A N   1 
ATOM   1606 C  CA  . LEU A 1 188 ? 8.569   -32.602 -8.742  1.00 30.43  ? 209  LEU A CA  1 
ATOM   1607 C  C   . LEU A 1 188 ? 9.835   -32.871 -9.569  1.00 37.64  ? 209  LEU A C   1 
ATOM   1608 O  O   . LEU A 1 188 ? 10.747  -32.058 -9.526  1.00 36.52  ? 209  LEU A O   1 
ATOM   1609 C  CB  . LEU A 1 188 ? 7.856   -31.361 -9.271  1.00 30.10  ? 209  LEU A CB  1 
ATOM   1610 C  CG  . LEU A 1 188 ? 7.492   -31.431 -10.741 1.00 31.11  ? 209  LEU A CG  1 
ATOM   1611 C  CD1 . LEU A 1 188 ? 6.283   -32.312 -10.897 1.00 29.99  ? 209  LEU A CD1 1 
ATOM   1612 C  CD2 . LEU A 1 188 ? 7.204   -30.019 -11.295 1.00 38.47  ? 209  LEU A CD2 1 
ATOM   1613 N  N   . ILE A 1 189 ? 9.914   -33.982 -10.305 1.00 28.48  ? 210  ILE A N   1 
ATOM   1614 C  CA  . ILE A 1 189 ? 11.143  -34.244 -11.035 1.00 32.01  ? 210  ILE A CA  1 
ATOM   1615 C  C   . ILE A 1 189 ? 10.931  -34.261 -12.557 1.00 34.56  ? 210  ILE A C   1 
ATOM   1616 O  O   . ILE A 1 189 ? 11.896  -34.214 -13.296 1.00 37.22  ? 210  ILE A O   1 
ATOM   1617 C  CB  . ILE A 1 189 ? 11.808  -35.576 -10.577 1.00 33.83  ? 210  ILE A CB  1 
ATOM   1618 C  CG1 . ILE A 1 189 ? 10.884  -36.753 -10.788 1.00 37.38  ? 210  ILE A CG1 1 
ATOM   1619 C  CG2 . ILE A 1 189 ? 12.366  -35.433 -9.067  1.00 35.59  ? 210  ILE A CG2 1 
ATOM   1620 C  CD1 . ILE A 1 189 ? 11.454  -38.059 -10.181 1.00 36.50  ? 210  ILE A CD1 1 
ATOM   1621 N  N   . ALA A 1 190 ? 9.688   -34.257 -13.009 1.00 32.63  ? 211  ALA A N   1 
ATOM   1622 C  CA  . ALA A 1 190 ? 9.390   -34.085 -14.430 1.00 35.11  ? 211  ALA A CA  1 
ATOM   1623 C  C   . ALA A 1 190 ? 7.959   -33.641 -14.584 1.00 34.90  ? 211  ALA A C   1 
ATOM   1624 O  O   . ALA A 1 190 ? 7.113   -33.993 -13.784 1.00 30.45  ? 211  ALA A O   1 
ATOM   1625 C  CB  . ALA A 1 190 ? 9.623   -35.374 -15.235 1.00 37.04  ? 211  ALA A CB  1 
ATOM   1626 N  N   . LYS A 1 191 ? 7.685   -32.878 -15.639 1.00 33.85  ? 212  LYS A N   1 
ATOM   1627 C  CA  . LYS A 1 191 ? 6.313   -32.479 -15.925 1.00 30.33  ? 212  LYS A CA  1 
ATOM   1628 C  C   . LYS A 1 191 ? 6.224   -32.178 -17.431 1.00 33.06  ? 212  LYS A C   1 
ATOM   1629 O  O   . LYS A 1 191 ? 7.001   -31.364 -17.941 1.00 34.45  ? 212  LYS A O   1 
ATOM   1630 C  CB  . LYS A 1 191 ? 5.924   -31.250 -15.098 1.00 34.55  ? 212  LYS A CB  1 
ATOM   1631 C  CG  . LYS A 1 191 ? 4.486   -30.782 -15.355 1.00 38.47  ? 212  LYS A CG  1 
ATOM   1632 C  CD  . LYS A 1 191 ? 4.279   -29.429 -14.742 1.00 48.28  ? 212  LYS A CD  1 
ATOM   1633 C  CE  . LYS A 1 191 ? 2.800   -29.160 -14.460 1.00 52.17  ? 212  LYS A CE  1 
ATOM   1634 N  NZ  . LYS A 1 191 ? 2.145   -28.529 -15.595 1.00 59.68  ? 212  LYS A NZ  1 
ATOM   1635 N  N   . GLY A 1 192 ? 5.302   -32.817 -18.147 1.00 29.48  ? 213  GLY A N   1 
ATOM   1636 C  CA  . GLY A 1 192 ? 5.193   -32.540 -19.564 1.00 33.86  ? 213  GLY A CA  1 
ATOM   1637 C  C   . GLY A 1 192 ? 4.238   -33.541 -20.197 1.00 31.79  ? 213  GLY A C   1 
ATOM   1638 O  O   . GLY A 1 192 ? 3.522   -34.270 -19.521 1.00 30.04  ? 213  GLY A O   1 
ATOM   1639 N  N   . LYS A 1 193 ? 4.193   -33.553 -21.520 1.00 30.71  ? 214  LYS A N   1 
ATOM   1640 C  CA  . LYS A 1 193 ? 3.233   -34.424 -22.169 1.00 35.67  ? 214  LYS A CA  1 
ATOM   1641 C  C   . LYS A 1 193 ? 3.668   -35.899 -22.178 1.00 37.45  ? 214  LYS A C   1 
ATOM   1642 O  O   . LYS A 1 193 ? 2.854   -36.762 -22.467 1.00 33.77  ? 214  LYS A O   1 
ATOM   1643 C  CB  . LYS A 1 193 ? 3.008   -33.933 -23.617 1.00 42.19  ? 214  LYS A CB  1 
ATOM   1644 C  CG  . LYS A 1 193 ? 2.125   -32.689 -23.638 1.00 56.02  ? 214  LYS A CG  1 
ATOM   1645 C  CD  . LYS A 1 193 ? 1.658   -32.327 -25.046 1.00 63.00  ? 214  LYS A CD  1 
ATOM   1646 C  CE  . LYS A 1 193 ? 0.674   -31.152 -25.031 1.00 63.81  ? 214  LYS A CE  1 
ATOM   1647 N  NZ  . LYS A 1 193 ? 0.188   -30.857 -26.451 1.00 72.55  ? 214  LYS A NZ  1 
ATOM   1648 N  N   . GLU A 1 194 ? 4.952   -36.177 -21.913 1.00 34.56  ? 215  GLU A N   1 
ATOM   1649 C  CA  . GLU A 1 194 ? 5.441   -37.571 -21.920 1.00 42.70  ? 215  GLU A CA  1 
ATOM   1650 C  C   . GLU A 1 194 ? 4.813   -38.427 -20.774 1.00 31.06  ? 215  GLU A C   1 
ATOM   1651 O  O   . GLU A 1 194 ? 4.909   -38.086 -19.600 1.00 29.67  ? 215  GLU A O   1 
ATOM   1652 C  CB  . GLU A 1 194 ? 6.972   -37.626 -21.811 1.00 39.83  ? 215  GLU A CB  1 
ATOM   1653 C  CG  . GLU A 1 194 ? 7.777   -36.788 -22.819 1.00 41.02  ? 215  GLU A CG  1 
ATOM   1654 C  CD  . GLU A 1 194 ? 7.824   -35.288 -22.490 1.00 50.90  ? 215  GLU A CD  1 
ATOM   1655 O  OE1 . GLU A 1 194 ? 8.371   -34.514 -23.339 1.00 63.25  ? 215  GLU A OE1 1 
ATOM   1656 O  OE2 . GLU A 1 194 ? 7.322   -34.884 -21.402 1.00 52.01  ? 215  GLU A OE2 1 
ATOM   1657 N  N   . PRO A 1 195 ? 4.187   -39.580 -21.129 1.00 28.88  ? 216  PRO A N   1 
ATOM   1658 C  CA  . PRO A 1 195 ? 3.559   -40.424 -20.107 1.00 28.67  ? 216  PRO A CA  1 
ATOM   1659 C  C   . PRO A 1 195 ? 4.583   -41.275 -19.343 1.00 34.86  ? 216  PRO A C   1 
ATOM   1660 O  O   . PRO A 1 195 ? 4.211   -42.272 -18.718 1.00 33.68  ? 216  PRO A O   1 
ATOM   1661 C  CB  . PRO A 1 195 ? 2.620   -41.313 -20.935 1.00 33.89  ? 216  PRO A CB  1 
ATOM   1662 C  CG  . PRO A 1 195 ? 3.281   -41.398 -22.289 1.00 35.56  ? 216  PRO A CG  1 
ATOM   1663 C  CD  . PRO A 1 195 ? 3.916   -40.049 -22.511 1.00 32.83  ? 216  PRO A CD  1 
ATOM   1664 N  N   . TYR A 1 196 ? 5.854   -40.912 -19.410 1.00 30.25  ? 217  TYR A N   1 
ATOM   1665 C  CA  . TYR A 1 196 ? 6.877   -41.709 -18.702 1.00 30.70  ? 217  TYR A CA  1 
ATOM   1666 C  C   . TYR A 1 196 ? 8.040   -40.881 -18.195 1.00 37.67  ? 217  TYR A C   1 
ATOM   1667 O  O   . TYR A 1 196 ? 8.270   -39.774 -18.641 1.00 35.82  ? 217  TYR A O   1 
ATOM   1668 C  CB  . TYR A 1 196 ? 7.420   -42.796 -19.627 1.00 35.28  ? 217  TYR A CB  1 
ATOM   1669 C  CG  . TYR A 1 196 ? 8.008   -42.220 -20.880 1.00 43.14  ? 217  TYR A CG  1 
ATOM   1670 C  CD1 . TYR A 1 196 ? 9.322   -41.766 -20.897 1.00 55.82  ? 217  TYR A CD1 1 
ATOM   1671 C  CD2 . TYR A 1 196 ? 7.245   -42.065 -22.047 1.00 47.50  ? 217  TYR A CD2 1 
ATOM   1672 C  CE1 . TYR A 1 196 ? 9.884   -41.188 -22.056 1.00 55.00  ? 217  TYR A CE1 1 
ATOM   1673 C  CE2 . TYR A 1 196 ? 7.810   -41.493 -23.215 1.00 52.66  ? 217  TYR A CE2 1 
ATOM   1674 C  CZ  . TYR A 1 196 ? 9.121   -41.055 -23.192 1.00 56.97  ? 217  TYR A CZ  1 
ATOM   1675 O  OH  . TYR A 1 196 ? 9.700   -40.488 -24.298 1.00 68.27  ? 217  TYR A OH  1 
ATOM   1676 N  N   . LEU A 1 197 ? 8.805   -41.453 -17.286 1.00 33.11  ? 218  LEU A N   1 
ATOM   1677 C  CA  . LEU A 1 197 ? 9.970   -40.780 -16.773 1.00 33.34  ? 218  LEU A CA  1 
ATOM   1678 C  C   . LEU A 1 197 ? 11.170  -41.684 -16.989 1.00 35.71  ? 218  LEU A C   1 
ATOM   1679 O  O   . LEU A 1 197 ? 11.086  -42.872 -16.708 1.00 32.07  ? 218  LEU A O   1 
ATOM   1680 C  CB  . LEU A 1 197 ? 9.749   -40.463 -15.306 1.00 26.44  ? 218  LEU A CB  1 
ATOM   1681 C  CG  . LEU A 1 197 ? 11.051  -40.061 -14.563 1.00 43.10  ? 218  LEU A CG  1 
ATOM   1682 C  CD1 . LEU A 1 197 ? 11.407  -38.673 -14.936 1.00 48.63  ? 218  LEU A CD1 1 
ATOM   1683 C  CD2 . LEU A 1 197 ? 10.829  -40.160 -13.103 1.00 50.37  ? 218  LEU A CD2 1 
ATOM   1684 N  N   . THR A 1 198 ? 12.273  -41.164 -17.525 1.00 34.02  ? 219  THR A N   1 
ATOM   1685 C  CA  . THR A 1 198 ? 13.502  -41.938 -17.595 1.00 37.10  ? 219  THR A CA  1 
ATOM   1686 C  C   . THR A 1 198 ? 14.561  -41.281 -16.712 1.00 39.40  ? 219  THR A C   1 
ATOM   1687 O  O   . THR A 1 198 ? 14.753  -40.077 -16.761 1.00 43.05  ? 219  THR A O   1 
ATOM   1688 C  CB  . THR A 1 198 ? 14.049  -42.051 -19.016 1.00 44.81  ? 219  THR A CB  1 
ATOM   1689 O  OG1 . THR A 1 198 ? 13.041  -42.612 -19.851 1.00 47.18  ? 219  THR A OG1 1 
ATOM   1690 C  CG2 . THR A 1 198 ? 15.250  -42.980 -19.055 1.00 49.94  ? 219  THR A CG2 1 
ATOM   1691 N  N   . LYS A 1 199 ? 15.210  -42.085 -15.876 1.00 40.06  ? 220  LYS A N   1 
ATOM   1692 C  CA  . LYS A 1 199 ? 16.390  -41.665 -15.123 1.00 43.21  ? 220  LYS A CA  1 
ATOM   1693 C  C   . LYS A 1 199 ? 17.523  -42.560 -15.571 1.00 45.44  ? 220  LYS A C   1 
ATOM   1694 O  O   . LYS A 1 199 ? 17.418  -43.782 -15.496 1.00 46.67  ? 220  LYS A O   1 
ATOM   1695 C  CB  . LYS A 1 199 ? 16.141  -41.763 -13.626 1.00 41.77  ? 220  LYS A CB  1 
ATOM   1696 C  CG  . LYS A 1 199 ? 17.426  -41.635 -12.776 1.00 58.71  ? 220  LYS A CG  1 
ATOM   1697 C  CD  . LYS A 1 199 ? 18.187  -40.332 -12.985 1.00 60.32  ? 220  LYS A CD  1 
ATOM   1698 C  CE  . LYS A 1 199 ? 19.255  -40.171 -11.926 1.00 59.43  ? 220  LYS A CE  1 
ATOM   1699 N  NZ  . LYS A 1 199 ? 20.232  -41.297 -11.943 1.00 63.29  ? 220  LYS A NZ  1 
ATOM   1700 N  N   A SER A 1 200 ? 18.593  -41.943 -16.056 0.41 45.78  ? 221  SER A N   1 
ATOM   1701 N  N   B SER A 1 200 ? 18.592  -41.957 -16.087 0.59 45.53  ? 221  SER A N   1 
ATOM   1702 C  CA  A SER A 1 200 ? 19.747  -42.656 -16.578 0.41 50.92  ? 221  SER A CA  1 
ATOM   1703 C  CA  B SER A 1 200 ? 19.742  -42.706 -16.584 0.59 51.09  ? 221  SER A CA  1 
ATOM   1704 C  C   A SER A 1 200 ? 20.731  -43.001 -15.467 0.41 52.37  ? 221  SER A C   1 
ATOM   1705 C  C   B SER A 1 200 ? 20.707  -43.024 -15.460 0.59 52.46  ? 221  SER A C   1 
ATOM   1706 O  O   A SER A 1 200 ? 20.817  -42.275 -14.474 0.41 52.17  ? 221  SER A O   1 
ATOM   1707 O  O   B SER A 1 200 ? 20.761  -42.304 -14.459 0.59 52.10  ? 221  SER A O   1 
ATOM   1708 C  CB  A SER A 1 200 ? 20.442  -41.806 -17.634 0.41 52.20  ? 221  SER A CB  1 
ATOM   1709 C  CB  B SER A 1 200 ? 20.475  -41.921 -17.673 0.59 52.15  ? 221  SER A CB  1 
ATOM   1710 O  OG  A SER A 1 200 ? 21.681  -42.370 -17.973 0.41 56.69  ? 221  SER A OG  1 
ATOM   1711 O  OG  B SER A 1 200 ? 19.649  -41.776 -18.812 0.59 53.65  ? 221  SER A OG  1 
ATOM   1712 N  N   . MET A 1 201 ? 21.465  -44.102 -15.633 1.00 52.13  ? 222  MET A N   1 
ATOM   1713 C  CA  . MET A 1 201 ? 22.511  -44.487 -14.678 1.00 53.93  ? 222  MET A CA  1 
ATOM   1714 C  C   . MET A 1 201 ? 22.099  -44.457 -13.222 1.00 49.75  ? 222  MET A C   1 
ATOM   1715 O  O   . MET A 1 201 ? 22.659  -43.686 -12.438 1.00 53.35  ? 222  MET A O   1 
ATOM   1716 C  CB  . MET A 1 201 ? 23.725  -43.569 -14.834 1.00 59.63  ? 222  MET A CB  1 
ATOM   1717 C  CG  . MET A 1 201 ? 24.421  -43.697 -16.162 1.00 73.71  ? 222  MET A CG  1 
ATOM   1718 S  SD  . MET A 1 201 ? 25.851  -44.780 -16.073 1.00 97.41  ? 222  MET A SD  1 
ATOM   1719 C  CE  . MET A 1 201 ? 26.043  -44.978 -14.292 1.00 63.99  ? 222  MET A CE  1 
ATOM   1720 N  N   . VAL A 1 202 ? 21.106  -45.263 -12.847 1.00 47.00  ? 223  VAL A N   1 
ATOM   1721 C  CA  . VAL A 1 202 ? 20.617  -45.143 -11.492 1.00 38.17  ? 223  VAL A CA  1 
ATOM   1722 C  C   . VAL A 1 202 ? 21.682  -45.575 -10.526 1.00 43.11  ? 223  VAL A C   1 
ATOM   1723 O  O   . VAL A 1 202 ? 22.567  -46.380 -10.848 1.00 45.87  ? 223  VAL A O   1 
ATOM   1724 C  CB  . VAL A 1 202 ? 19.332  -45.959 -11.252 1.00 41.91  ? 223  VAL A CB  1 
ATOM   1725 C  CG1 . VAL A 1 202 ? 18.268  -45.453 -12.127 1.00 43.73  ? 223  VAL A CG1 1 
ATOM   1726 C  CG2 . VAL A 1 202 ? 19.572  -47.409 -11.532 1.00 36.85  ? 223  VAL A CG2 1 
ATOM   1727 N  N   . GLY A 1 203 ? 21.617  -45.002 -9.340  1.00 43.45  ? 224  GLY A N   1 
ATOM   1728 C  CA  . GLY A 1 203 ? 22.480  -45.428 -8.259  1.00 43.13  ? 224  GLY A CA  1 
ATOM   1729 C  C   . GLY A 1 203 ? 21.607  -45.674 -7.040  1.00 41.43  ? 224  GLY A C   1 
ATOM   1730 O  O   . GLY A 1 203 ? 20.387  -45.510 -7.103  1.00 41.09  ? 224  GLY A O   1 
ATOM   1731 N  N   . PRO A 1 204 ? 22.225  -46.086 -5.922  1.00 44.99  ? 225  PRO A N   1 
ATOM   1732 C  CA  . PRO A 1 204 ? 21.448  -46.414 -4.729  1.00 42.10  ? 225  PRO A CA  1 
ATOM   1733 C  C   . PRO A 1 204 ? 20.585  -45.235 -4.274  1.00 47.43  ? 225  PRO A C   1 
ATOM   1734 O  O   . PRO A 1 204 ? 19.532  -45.451 -3.681  1.00 44.07  ? 225  PRO A O   1 
ATOM   1735 C  CB  . PRO A 1 204 ? 22.515  -46.781 -3.689  1.00 51.72  ? 225  PRO A CB  1 
ATOM   1736 C  CG  . PRO A 1 204 ? 23.818  -46.314 -4.268  1.00 56.20  ? 225  PRO A CG  1 
ATOM   1737 C  CD  . PRO A 1 204 ? 23.671  -46.287 -5.740  1.00 52.84  ? 225  PRO A CD  1 
ATOM   1738 N  N   . GLU A 1 205 ? 21.010  -44.010 -4.573  1.00 45.69  ? 226  GLU A N   1 
ATOM   1739 C  CA  . GLU A 1 205 ? 20.285  -42.836 -4.118  1.00 41.80  ? 226  GLU A CA  1 
ATOM   1740 C  C   . GLU A 1 205 ? 18.933  -42.696 -4.838  1.00 46.36  ? 226  GLU A C   1 
ATOM   1741 O  O   . GLU A 1 205 ? 18.089  -41.905 -4.417  1.00 45.53  ? 226  GLU A O   1 
ATOM   1742 C  CB  . GLU A 1 205 ? 21.141  -41.573 -4.329  1.00 44.99  ? 226  GLU A CB  1 
ATOM   1743 C  CG  . GLU A 1 205 ? 21.426  -41.224 -5.816  1.00 60.49  ? 226  GLU A CG  1 
ATOM   1744 C  CD  . GLU A 1 205 ? 22.595  -42.020 -6.443  1.00 62.74  ? 226  GLU A CD  1 
ATOM   1745 O  OE1 . GLU A 1 205 ? 23.101  -42.963 -5.789  1.00 56.49  ? 226  GLU A OE1 1 
ATOM   1746 O  OE2 . GLU A 1 205 ? 22.993  -41.702 -7.601  1.00 63.69  ? 226  GLU A OE2 1 
ATOM   1747 N  N   . ASP A 1 206 ? 18.725  -43.463 -5.911  1.00 40.07  ? 227  ASP A N   1 
ATOM   1748 C  CA  . ASP A 1 206 ? 17.462  -43.365 -6.674  1.00 36.80  ? 227  ASP A CA  1 
ATOM   1749 C  C   . ASP A 1 206 ? 16.419  -44.332 -6.125  1.00 36.08  ? 227  ASP A C   1 
ATOM   1750 O  O   . ASP A 1 206 ? 15.251  -44.294 -6.537  1.00 34.00  ? 227  ASP A O   1 
ATOM   1751 C  CB  . ASP A 1 206 ? 17.728  -43.630 -8.168  1.00 36.17  ? 227  ASP A CB  1 
ATOM   1752 C  CG  . ASP A 1 206 ? 18.653  -42.584 -8.784  1.00 48.14  ? 227  ASP A CG  1 
ATOM   1753 O  OD1 . ASP A 1 206 ? 18.307  -41.385 -8.694  1.00 45.72  ? 227  ASP A OD1 1 
ATOM   1754 O  OD2 . ASP A 1 206 ? 19.727  -42.950 -9.318  1.00 45.98  ? 227  ASP A OD2 1 
ATOM   1755 N  N   . ALA A 1 207 ? 16.833  -45.213 -5.198  1.00 36.83  ? 228  ALA A N   1 
ATOM   1756 C  CA  . ALA A 1 207 ? 15.876  -46.133 -4.573  1.00 32.48  ? 228  ALA A CA  1 
ATOM   1757 C  C   . ALA A 1 207 ? 14.880  -45.344 -3.752  1.00 37.15  ? 228  ALA A C   1 
ATOM   1758 O  O   . ALA A 1 207 ? 15.252  -44.337 -3.121  1.00 34.72  ? 228  ALA A O   1 
ATOM   1759 C  CB  . ALA A 1 207 ? 16.574  -47.170 -3.686  1.00 31.67  ? 228  ALA A CB  1 
ATOM   1760 N  N   . GLY A 1 208 ? 13.637  -45.819 -3.743  1.00 33.87  ? 229  GLY A N   1 
ATOM   1761 C  CA  . GLY A 1 208 ? 12.562  -45.228 -2.943  1.00 34.07  ? 229  GLY A CA  1 
ATOM   1762 C  C   . GLY A 1 208 ? 11.229  -45.115 -3.665  1.00 30.83  ? 229  GLY A C   1 
ATOM   1763 O  O   . GLY A 1 208 ? 10.929  -45.905 -4.549  1.00 30.79  ? 229  GLY A O   1 
ATOM   1764 N  N   . ASN A 1 209 ? 10.430  -44.121 -3.305  1.00 26.91  ? 230  ASN A N   1 
ATOM   1765 C  CA  . ASN A 1 209 ? 9.046   -44.024 -3.781  1.00 27.04  ? 230  ASN A CA  1 
ATOM   1766 C  C   . ASN A 1 209 ? 8.874   -42.860 -4.735  1.00 26.58  ? 230  ASN A C   1 
ATOM   1767 O  O   . ASN A 1 209 ? 9.519   -41.835 -4.555  1.00 26.37  ? 230  ASN A O   1 
ATOM   1768 C  CB  . ASN A 1 209 ? 8.101   -43.864 -2.598  1.00 26.94  ? 230  ASN A CB  1 
ATOM   1769 C  CG  . ASN A 1 209 ? 8.056   -45.122 -1.766  1.00 36.39  ? 230  ASN A CG  1 
ATOM   1770 O  OD1 . ASN A 1 209 ? 7.637   -46.148 -2.230  1.00 30.91  ? 230  ASN A OD1 1 
ATOM   1771 N  ND2 . ASN A 1 209 ? 8.602   -45.065 -0.592  1.00 34.62  ? 230  ASN A ND2 1 
ATOM   1772 N  N   . TYR A 1 210 ? 8.010   -43.053 -5.743  1.00 27.36  ? 231  TYR A N   1 
ATOM   1773 C  CA  . TYR A 1 210 ? 7.722   -42.056 -6.770  1.00 24.85  ? 231  TYR A CA  1 
ATOM   1774 C  C   . TYR A 1 210 ? 6.226   -42.078 -7.014  1.00 26.30  ? 231  TYR A C   1 
ATOM   1775 O  O   . TYR A 1 210 ? 5.512   -43.051 -6.664  1.00 25.45  ? 231  TYR A O   1 
ATOM   1776 C  CB  . TYR A 1 210 ? 8.431   -42.352 -8.112  1.00 24.34  ? 231  TYR A CB  1 
ATOM   1777 C  CG  . TYR A 1 210 ? 9.938   -42.358 -8.041  1.00 27.74  ? 231  TYR A CG  1 
ATOM   1778 C  CD1 . TYR A 1 210 ? 10.675  -41.335 -8.628  1.00 27.64  ? 231  TYR A CD1 1 
ATOM   1779 C  CD2 . TYR A 1 210 ? 10.638  -43.436 -7.435  1.00 28.70  ? 231  TYR A CD2 1 
ATOM   1780 C  CE1 . TYR A 1 210 ? 12.076  -41.347 -8.623  1.00 26.15  ? 231  TYR A CE1 1 
ATOM   1781 C  CE2 . TYR A 1 210 ? 12.071  -43.459 -7.437  1.00 27.58  ? 231  TYR A CE2 1 
ATOM   1782 C  CZ  . TYR A 1 210 ? 12.755  -42.401 -8.000  1.00 27.66  ? 231  TYR A CZ  1 
ATOM   1783 O  OH  . TYR A 1 210 ? 14.125  -42.412 -7.974  1.00 30.55  ? 231  TYR A OH  1 
ATOM   1784 N  N   . ARG A 1 211 ? 5.740   -41.032 -7.654  1.00 26.37  ? 232  ARG A N   1 
ATOM   1785 C  CA  . ARG A 1 211 ? 4.307   -40.967 -7.934  1.00 25.09  ? 232  ARG A CA  1 
ATOM   1786 C  C   . ARG A 1 211 ? 4.135   -40.242 -9.241  1.00 24.99  ? 232  ARG A C   1 
ATOM   1787 O  O   . ARG A 1 211 ? 4.788   -39.237 -9.485  1.00 29.72  ? 232  ARG A O   1 
ATOM   1788 C  CB  . ARG A 1 211 ? 3.640   -40.209 -6.767  1.00 27.61  ? 232  ARG A CB  1 
ATOM   1789 C  CG  . ARG A 1 211 ? 2.192   -39.979 -6.750  1.00 39.98  ? 232  ARG A CG  1 
ATOM   1790 C  CD  . ARG A 1 211 ? 1.912   -39.094 -5.492  1.00 45.71  ? 232  ARG A CD  1 
ATOM   1791 N  NE  . ARG A 1 211 ? 0.724   -38.325 -5.729  1.00 61.12  ? 232  ARG A NE  1 
ATOM   1792 C  CZ  . ARG A 1 211 ? 0.666   -37.008 -5.751  1.00 61.87  ? 232  ARG A CZ  1 
ATOM   1793 N  NH1 . ARG A 1 211 ? 1.734   -36.288 -5.482  1.00 52.68  ? 232  ARG A NH1 1 
ATOM   1794 N  NH2 . ARG A 1 211 ? -0.489  -36.417 -6.021  1.00 71.99  ? 232  ARG A NH2 1 
ATOM   1795 N  N   . CYS A 1 212 ? 3.220   -40.730 -10.080 1.00 22.50  ? 233  CYS A N   1 
ATOM   1796 C  CA  . CYS A 1 212 ? 2.790   -39.976 -11.268 1.00 21.90  ? 233  CYS A CA  1 
ATOM   1797 C  C   . CYS A 1 212 ? 1.428   -39.364 -11.003 1.00 25.15  ? 233  CYS A C   1 
ATOM   1798 O  O   . CYS A 1 212 ? 0.571   -40.025 -10.430 1.00 27.04  ? 233  CYS A O   1 
ATOM   1799 C  CB  . CYS A 1 212 ? 2.650   -40.921 -12.475 1.00 26.82  ? 233  CYS A CB  1 
ATOM   1800 S  SG  . CYS A 1 212 ? 1.803   -40.164 -13.928 1.00 33.51  ? 233  CYS A SG  1 
ATOM   1801 N  N   A VAL A 1 213 ? 1.200   -38.120 -11.408 0.30 25.55  ? 234  VAL A N   1 
ATOM   1802 N  N   B VAL A 1 213 ? 1.216   -38.144 -11.500 0.70 24.25  ? 234  VAL A N   1 
ATOM   1803 C  CA  A VAL A 1 213 ? -0.166  -37.601 -11.377 0.30 25.20  ? 234  VAL A CA  1 
ATOM   1804 C  CA  B VAL A 1 213 ? -0.087  -37.472 -11.427 0.70 25.60  ? 234  VAL A CA  1 
ATOM   1805 C  C   A VAL A 1 213 ? -0.442  -36.920 -12.697 0.30 26.27  ? 234  VAL A C   1 
ATOM   1806 C  C   B VAL A 1 213 ? -0.377  -36.952 -12.794 0.70 28.03  ? 234  VAL A C   1 
ATOM   1807 O  O   A VAL A 1 213 ? 0.302   -36.027 -13.138 0.30 27.47  ? 234  VAL A O   1 
ATOM   1808 O  O   B VAL A 1 213 ? 0.428   -36.180 -13.363 0.70 27.52  ? 234  VAL A O   1 
ATOM   1809 C  CB  A VAL A 1 213 ? -0.425  -36.633 -10.197 0.30 30.10  ? 234  VAL A CB  1 
ATOM   1810 C  CB  B VAL A 1 213 ? -0.117  -36.290 -10.449 0.70 28.58  ? 234  VAL A CB  1 
ATOM   1811 C  CG1 A VAL A 1 213 ? 0.525   -35.465 -10.221 0.30 26.01  ? 234  VAL A CG1 1 
ATOM   1812 C  CG1 B VAL A 1 213 ? -1.559  -35.758 -10.317 0.70 31.39  ? 234  VAL A CG1 1 
ATOM   1813 C  CG2 A VAL A 1 213 ? -1.887  -36.148 -10.220 0.30 26.60  ? 234  VAL A CG2 1 
ATOM   1814 C  CG2 B VAL A 1 213 ? 0.388   -36.712 -9.115  0.70 27.24  ? 234  VAL A CG2 1 
ATOM   1815 N  N   . LEU A 1 214 ? -1.487  -37.408 -13.353 1.00 25.40  ? 235  LEU A N   1 
ATOM   1816 C  CA  . LEU A 1 214 ? -1.915  -36.929 -14.647 1.00 24.65  ? 235  LEU A CA  1 
ATOM   1817 C  C   . LEU A 1 214 ? -3.046  -35.933 -14.438 1.00 25.31  ? 235  LEU A C   1 
ATOM   1818 O  O   . LEU A 1 214 ? -4.012  -36.257 -13.754 1.00 28.41  ? 235  LEU A O   1 
ATOM   1819 C  CB  . LEU A 1 214 ? -2.388  -38.086 -15.537 1.00 25.43  ? 235  LEU A CB  1 
ATOM   1820 C  CG  . LEU A 1 214 ? -3.069  -37.690 -16.877 1.00 24.58  ? 235  LEU A CG  1 
ATOM   1821 C  CD1 . LEU A 1 214 ? -2.177  -36.858 -17.851 1.00 25.04  ? 235  LEU A CD1 1 
ATOM   1822 C  CD2 . LEU A 1 214 ? -3.578  -38.969 -17.614 1.00 26.58  ? 235  LEU A CD2 1 
ATOM   1823 N  N   . ASP A 1 215 ? -2.915  -34.726 -15.022 1.00 28.70  ? 236  ASP A N   1 
ATOM   1824 C  CA  . ASP A 1 215 ? -3.820  -33.619 -14.707 1.00 27.49  ? 236  ASP A CA  1 
ATOM   1825 C  C   . ASP A 1 215 ? -4.732  -33.327 -15.927 1.00 26.47  ? 236  ASP A C   1 
ATOM   1826 O  O   . ASP A 1 215 ? -4.520  -33.853 -17.016 1.00 28.18  ? 236  ASP A O   1 
ATOM   1827 C  CB  . ASP A 1 215 ? -3.027  -32.365 -14.332 1.00 24.42  ? 236  ASP A CB  1 
ATOM   1828 C  CG  . ASP A 1 215 ? -3.810  -31.410 -13.361 1.00 47.48  ? 236  ASP A CG  1 
ATOM   1829 O  OD1 . ASP A 1 215 ? -4.993  -31.667 -12.983 1.00 38.16  ? 236  ASP A OD1 1 
ATOM   1830 O  OD2 . ASP A 1 215 ? -3.231  -30.358 -13.008 1.00 50.33  ? 236  ASP A OD2 1 
ATOM   1831 N  N   . THR A 1 216 ? -5.775  -32.528 -15.698 1.00 25.68  ? 237  THR A N   1 
ATOM   1832 C  CA  . THR A 1 216 ? -6.680  -32.158 -16.811 1.00 22.42  ? 237  THR A CA  1 
ATOM   1833 C  C   . THR A 1 216 ? -6.886  -30.649 -16.783 1.00 24.66  ? 237  THR A C   1 
ATOM   1834 O  O   . THR A 1 216 ? -6.492  -29.972 -15.825 1.00 29.02  ? 237  THR A O   1 
ATOM   1835 C  CB  . THR A 1 216 ? -8.097  -32.818 -16.724 1.00 27.88  ? 237  THR A CB  1 
ATOM   1836 O  OG1 . THR A 1 216 ? -8.797  -32.310 -15.566 1.00 27.55  ? 237  THR A OG1 1 
ATOM   1837 C  CG2 . THR A 1 216 ? -8.009  -34.355 -16.653 1.00 23.99  ? 237  THR A CG2 1 
ATOM   1838 N  N   . ILE A 1 217 ? -7.494  -30.135 -17.839 1.00 25.51  ? 238  ILE A N   1 
ATOM   1839 C  CA  . ILE A 1 217 ? -7.723  -28.681 -17.908 1.00 30.87  ? 238  ILE A CA  1 
ATOM   1840 C  C   . ILE A 1 217 ? -8.625  -28.193 -16.765 1.00 27.25  ? 238  ILE A C   1 
ATOM   1841 O  O   . ILE A 1 217 ? -8.303  -27.183 -16.045 1.00 28.97  ? 238  ILE A O   1 
ATOM   1842 C  CB  . ILE A 1 217 ? -8.361  -28.316 -19.233 1.00 26.18  ? 238  ILE A CB  1 
ATOM   1843 C  CG1 . ILE A 1 217 ? -7.348  -28.593 -20.345 1.00 28.99  ? 238  ILE A CG1 1 
ATOM   1844 C  CG2 . ILE A 1 217 ? -8.684  -26.795 -19.228 1.00 25.50  ? 238  ILE A CG2 1 
ATOM   1845 C  CD1 . ILE A 1 217 ? -7.943  -28.578 -21.775 1.00 32.46  ? 238  ILE A CD1 1 
ATOM   1846 N  N   . ASN A 1 218 ? -9.740  -28.885 -16.557 1.00 34.93  ? 239  ASN A N   1 
ATOM   1847 C  CA  . ASN A 1 218 ? -10.645 -28.423 -15.529 1.00 35.42  ? 239  ASN A CA  1 
ATOM   1848 C  C   . ASN A 1 218 ? -11.476 -29.511 -14.863 1.00 34.89  ? 239  ASN A C   1 
ATOM   1849 O  O   . ASN A 1 218 ? -12.481 -29.224 -14.253 1.00 35.54  ? 239  ASN A O   1 
ATOM   1850 C  CB  . ASN A 1 218 ? -11.553 -27.317 -16.096 1.00 36.43  ? 239  ASN A CB  1 
ATOM   1851 C  CG  . ASN A 1 218 ? -12.646 -27.842 -17.048 1.00 38.18  ? 239  ASN A CG  1 
ATOM   1852 O  OD1 . ASN A 1 218 ? -12.604 -28.980 -17.526 1.00 35.37  ? 239  ASN A OD1 1 
ATOM   1853 N  ND2 . ASN A 1 218 ? -13.644 -27.008 -17.292 1.00 37.12  ? 239  ASN A ND2 1 
ATOM   1854 N  N   . GLN A 1 219 ? -11.019 -30.761 -14.925 1.00 26.30  ? 240  GLN A N   1 
ATOM   1855 C  CA  . GLN A 1 219 ? -11.789 -31.835 -14.292 1.00 27.24  ? 240  GLN A CA  1 
ATOM   1856 C  C   . GLN A 1 219 ? -11.007 -32.505 -13.178 1.00 33.99  ? 240  GLN A C   1 
ATOM   1857 O  O   . GLN A 1 219 ? -11.396 -33.584 -12.748 1.00 30.90  ? 240  GLN A O   1 
ATOM   1858 C  CB  . GLN A 1 219 ? -12.207 -32.886 -15.361 1.00 25.15  ? 240  GLN A CB  1 
ATOM   1859 C  CG  . GLN A 1 219 ? -13.108 -32.245 -16.437 1.00 26.30  ? 240  GLN A CG  1 
ATOM   1860 C  CD  . GLN A 1 219 ? -14.393 -31.701 -15.890 1.00 35.06  ? 240  GLN A CD  1 
ATOM   1861 O  OE1 . GLN A 1 219 ? -14.983 -32.304 -14.978 1.00 31.18  ? 240  GLN A OE1 1 
ATOM   1862 N  NE2 . GLN A 1 219 ? -14.875 -30.564 -16.455 1.00 32.19  ? 240  GLN A NE2 1 
ATOM   1863 N  N   . GLY A 1 220 ? -9.925  -31.875 -12.697 1.00 29.50  ? 241  GLY A N   1 
ATOM   1864 C  CA  . GLY A 1 220 ? -9.137  -32.442 -11.604 1.00 28.51  ? 241  GLY A CA  1 
ATOM   1865 C  C   . GLY A 1 220 ? -8.137  -33.478 -12.113 1.00 25.85  ? 241  GLY A C   1 
ATOM   1866 O  O   . GLY A 1 220 ? -7.970  -33.673 -13.304 1.00 31.30  ? 241  GLY A O   1 
ATOM   1867 N  N   . HIS A 1 221 ? -7.454  -34.135 -11.187 1.00 26.75  ? 242  HIS A N   1 
ATOM   1868 C  CA  . HIS A 1 221 ? -6.474  -35.141 -11.580 1.00 21.31  ? 242  HIS A CA  1 
ATOM   1869 C  C   . HIS A 1 221 ? -7.188  -36.313 -12.244 1.00 27.86  ? 242  HIS A C   1 
ATOM   1870 O  O   . HIS A 1 221 ? -8.295  -36.648 -11.813 1.00 27.57  ? 242  HIS A O   1 
ATOM   1871 C  CB  . HIS A 1 221 ? -5.751  -35.647 -10.359 1.00 24.37  ? 242  HIS A CB  1 
ATOM   1872 C  CG  . HIS A 1 221 ? -5.079  -34.573 -9.566  1.00 33.46  ? 242  HIS A CG  1 
ATOM   1873 N  ND1 . HIS A 1 221 ? -4.351  -33.559 -10.154 1.00 37.21  ? 242  HIS A ND1 1 
ATOM   1874 C  CD2 . HIS A 1 221 ? -4.981  -34.386 -8.229  1.00 39.29  ? 242  HIS A CD2 1 
ATOM   1875 C  CE1 . HIS A 1 221 ? -3.832  -32.791 -9.210  1.00 38.42  ? 242  HIS A CE1 1 
ATOM   1876 N  NE2 . HIS A 1 221 ? -4.218  -33.261 -8.033  1.00 44.73  ? 242  HIS A NE2 1 
ATOM   1877 N  N   . ALA A 1 222 ? -6.561  -36.918 -13.259 1.00 23.88  ? 243  ALA A N   1 
ATOM   1878 C  CA  . ALA A 1 222 ? -7.156  -38.030 -14.017 1.00 23.61  ? 243  ALA A CA  1 
ATOM   1879 C  C   . ALA A 1 222 ? -6.554  -39.408 -13.648 1.00 26.16  ? 243  ALA A C   1 
ATOM   1880 O  O   . ALA A 1 222 ? -7.180  -40.452 -13.860 1.00 24.77  ? 243  ALA A O   1 
ATOM   1881 C  CB  . ALA A 1 222 ? -6.973  -37.816 -15.560 1.00 24.69  ? 243  ALA A CB  1 
ATOM   1882 N  N   . THR A 1 223 ? -5.320  -39.415 -13.170 1.00 24.66  ? 244  THR A N   1 
ATOM   1883 C  CA  . THR A 1 223 ? -4.706  -40.714 -12.798 1.00 21.92  ? 244  THR A CA  1 
ATOM   1884 C  C   . THR A 1 223 ? -3.611  -40.422 -11.782 1.00 21.78  ? 244  THR A C   1 
ATOM   1885 O  O   . THR A 1 223 ? -2.883  -39.440 -11.920 1.00 24.35  ? 244  THR A O   1 
ATOM   1886 C  CB  . THR A 1 223 ? -4.134  -41.417 -14.040 1.00 23.79  ? 244  THR A CB  1 
ATOM   1887 O  OG1 . THR A 1 223 ? -5.199  -41.984 -14.812 1.00 25.59  ? 244  THR A OG1 1 
ATOM   1888 C  CG2 . THR A 1 223 ? -3.139  -42.575 -13.645 1.00 24.73  ? 244  THR A CG2 1 
ATOM   1889 N  N   . VAL A 1 224 ? -3.507  -41.293 -10.791 1.00 21.10  ? 245  VAL A N   1 
ATOM   1890 C  CA  . VAL A 1 224 ? -2.277  -41.378 -9.987  1.00 21.07  ? 245  VAL A CA  1 
ATOM   1891 C  C   . VAL A 1 224 ? -1.781  -42.820 -9.955  1.00 24.07  ? 245  VAL A C   1 
ATOM   1892 O  O   . VAL A 1 224 ? -2.563  -43.721 -9.734  1.00 27.55  ? 245  VAL A O   1 
ATOM   1893 C  CB  . VAL A 1 224 ? -2.554  -40.935 -8.537  1.00 26.61  ? 245  VAL A CB  1 
ATOM   1894 C  CG1 . VAL A 1 224 ? -1.364  -41.356 -7.539  1.00 25.56  ? 245  VAL A CG1 1 
ATOM   1895 C  CG2 . VAL A 1 224 ? -2.792  -39.438 -8.523  1.00 28.19  ? 245  VAL A CG2 1 
ATOM   1896 N  N   . ILE A 1 225 ? -0.490  -43.022 -10.169 1.00 22.36  ? 246  ILE A N   1 
ATOM   1897 C  CA  . ILE A 1 225 ? 0.119   -44.354 -9.970  1.00 22.68  ? 246  ILE A CA  1 
ATOM   1898 C  C   . ILE A 1 225 ? 1.304   -44.136 -9.057  1.00 23.00  ? 246  ILE A C   1 
ATOM   1899 O  O   . ILE A 1 225 ? 2.011   -43.101 -9.203  1.00 25.77  ? 246  ILE A O   1 
ATOM   1900 C  CB  . ILE A 1 225 ? 0.568   -44.935 -11.333 1.00 24.63  ? 246  ILE A CB  1 
ATOM   1901 C  CG1 . ILE A 1 225 ? -0.644  -45.215 -12.237 1.00 24.24  ? 246  ILE A CG1 1 
ATOM   1902 C  CG2 . ILE A 1 225 ? 1.359   -46.238 -11.159 1.00 24.26  ? 246  ILE A CG2 1 
ATOM   1903 C  CD1 . ILE A 1 225 ? -0.242  -45.503 -13.672 1.00 23.69  ? 246  ILE A CD1 1 
ATOM   1904 N  N   . ARG A 1 226 ? 1.533   -45.075 -8.135  1.00 21.08  ? 247  ARG A N   1 
ATOM   1905 C  CA  . ARG A 1 226 ? 2.701   -45.011 -7.261  1.00 23.67  ? 247  ARG A CA  1 
ATOM   1906 C  C   . ARG A 1 226 ? 3.735   -46.057 -7.670  1.00 25.40  ? 247  ARG A C   1 
ATOM   1907 O  O   . ARG A 1 226 ? 3.371   -47.114 -8.168  1.00 25.03  ? 247  ARG A O   1 
ATOM   1908 C  CB  . ARG A 1 226 ? 2.232   -45.238 -5.813  1.00 22.38  ? 247  ARG A CB  1 
ATOM   1909 C  CG  . ARG A 1 226 ? 1.500   -43.968 -5.281  1.00 24.86  ? 247  ARG A CG  1 
ATOM   1910 C  CD  . ARG A 1 226 ? 0.761   -44.258 -3.957  1.00 35.32  ? 247  ARG A CD  1 
ATOM   1911 N  NE  . ARG A 1 226 ? -0.350  -45.200 -4.231  1.00 40.90  ? 247  ARG A NE  1 
ATOM   1912 C  CZ  . ARG A 1 226 ? -0.431  -46.478 -3.826  1.00 48.04  ? 247  ARG A CZ  1 
ATOM   1913 N  NH1 . ARG A 1 226 ? 0.514   -47.025 -3.062  1.00 39.44  ? 247  ARG A NH1 1 
ATOM   1914 N  NH2 . ARG A 1 226 ? -1.479  -47.234 -4.181  1.00 38.38  ? 247  ARG A NH2 1 
ATOM   1915 N  N   . TYR A 1 227 ? 5.011   -45.789 -7.386  1.00 23.62  ? 248  TYR A N   1 
ATOM   1916 C  CA  . TYR A 1 227 ? 6.074   -46.742 -7.735  1.00 24.42  ? 248  TYR A CA  1 
ATOM   1917 C  C   . TYR A 1 227 ? 6.968   -46.897 -6.519  1.00 26.57  ? 248  TYR A C   1 
ATOM   1918 O  O   . TYR A 1 227 ? 7.435   -45.900 -5.926  1.00 28.64  ? 248  TYR A O   1 
ATOM   1919 C  CB  . TYR A 1 227 ? 6.918   -46.204 -8.908  1.00 21.73  ? 248  TYR A CB  1 
ATOM   1920 C  CG  . TYR A 1 227 ? 6.077   -45.680 -10.055 1.00 25.73  ? 248  TYR A CG  1 
ATOM   1921 C  CD1 . TYR A 1 227 ? 5.849   -46.471 -11.193 1.00 26.96  ? 248  TYR A CD1 1 
ATOM   1922 C  CD2 . TYR A 1 227 ? 5.540   -44.394 -10.016 1.00 21.99  ? 248  TYR A CD2 1 
ATOM   1923 C  CE1 . TYR A 1 227 ? 5.076   -45.993 -12.274 1.00 23.37  ? 248  TYR A CE1 1 
ATOM   1924 C  CE2 . TYR A 1 227 ? 4.764   -43.911 -11.115 1.00 23.08  ? 248  TYR A CE2 1 
ATOM   1925 C  CZ  . TYR A 1 227 ? 4.542   -44.724 -12.218 1.00 25.40  ? 248  TYR A CZ  1 
ATOM   1926 O  OH  . TYR A 1 227 ? 3.767   -44.255 -13.289 1.00 26.26  ? 248  TYR A OH  1 
ATOM   1927 N  N   . ASP A 1 228 ? 7.247   -48.146 -6.185  1.00 21.60  ? 249  ASP A N   1 
ATOM   1928 C  CA  . ASP A 1 228 ? 8.207   -48.477 -5.160  1.00 22.60  ? 249  ASP A CA  1 
ATOM   1929 C  C   . ASP A 1 228 ? 9.456   -49.020 -5.880  1.00 31.57  ? 249  ASP A C   1 
ATOM   1930 O  O   . ASP A 1 228 ? 9.365   -50.066 -6.441  1.00 27.90  ? 249  ASP A O   1 
ATOM   1931 C  CB  . ASP A 1 228 ? 7.533   -49.549 -4.263  1.00 27.74  ? 249  ASP A CB  1 
ATOM   1932 C  CG  . ASP A 1 228 ? 8.411   -50.032 -3.138  1.00 46.66  ? 249  ASP A CG  1 
ATOM   1933 O  OD1 . ASP A 1 228 ? 9.623   -50.100 -3.331  1.00 47.71  ? 249  ASP A OD1 1 
ATOM   1934 O  OD2 . ASP A 1 228 ? 7.873   -50.374 -2.054  1.00 52.44  ? 249  ASP A OD2 1 
ATOM   1935 N  N   . VAL A 1 229 ? 10.599  -48.338 -5.833  1.00 26.80  ? 250  VAL A N   1 
ATOM   1936 C  CA  . VAL A 1 229 ? 11.763  -48.694 -6.626  1.00 28.09  ? 250  VAL A CA  1 
ATOM   1937 C  C   . VAL A 1 229 ? 12.887  -49.173 -5.770  1.00 32.43  ? 250  VAL A C   1 
ATOM   1938 O  O   . VAL A 1 229 ? 13.339  -48.472 -4.815  1.00 29.62  ? 250  VAL A O   1 
ATOM   1939 C  CB  . VAL A 1 229 ? 12.225  -47.470 -7.499  1.00 31.67  ? 250  VAL A CB  1 
ATOM   1940 C  CG1 . VAL A 1 229 ? 13.527  -47.763 -8.254  1.00 29.18  ? 250  VAL A CG1 1 
ATOM   1941 C  CG2 . VAL A 1 229 ? 11.064  -47.029 -8.468  1.00 29.09  ? 250  VAL A CG2 1 
ATOM   1942 N  N   . THR A 1 230 ? 13.344  -50.387 -6.090  1.00 27.19  ? 251  THR A N   1 
ATOM   1943 C  CA  . THR A 1 230 ? 14.506  -50.967 -5.426  1.00 31.58  ? 251  THR A CA  1 
ATOM   1944 C  C   . THR A 1 230 ? 15.684  -50.912 -6.366  1.00 35.37  ? 251  THR A C   1 
ATOM   1945 O  O   . THR A 1 230 ? 15.548  -51.265 -7.543  1.00 30.89  ? 251  THR A O   1 
ATOM   1946 C  CB  . THR A 1 230 ? 14.197  -52.411 -5.024  1.00 34.50  ? 251  THR A CB  1 
ATOM   1947 O  OG1 . THR A 1 230 ? 13.130  -52.375 -4.070  1.00 34.85  ? 251  THR A OG1 1 
ATOM   1948 C  CG2 . THR A 1 230 ? 15.390  -53.097 -4.428  1.00 36.47  ? 251  THR A CG2 1 
ATOM   1949 N  N   . VAL A 1 231 ? 16.833  -50.472 -5.888  1.00 29.88  ? 252  VAL A N   1 
ATOM   1950 C  CA  . VAL A 1 231 ? 17.996  -50.525 -6.771  1.00 35.02  ? 252  VAL A CA  1 
ATOM   1951 C  C   . VAL A 1 231 ? 18.854  -51.697 -6.358  1.00 37.76  ? 252  VAL A C   1 
ATOM   1952 O  O   . VAL A 1 231 ? 19.319  -51.785 -5.208  1.00 38.95  ? 252  VAL A O   1 
ATOM   1953 C  CB  . VAL A 1 231 ? 18.813  -49.210 -6.776  1.00 35.51  ? 252  VAL A CB  1 
ATOM   1954 C  CG1 . VAL A 1 231 ? 20.053  -49.337 -7.669  1.00 40.77  ? 252  VAL A CG1 1 
ATOM   1955 C  CG2 . VAL A 1 231 ? 17.950  -48.095 -7.297  1.00 34.06  ? 252  VAL A CG2 1 
ATOM   1956 N  N   . LEU A 1 232 ? 19.052  -52.619 -7.292  1.00 33.62  ? 253  LEU A N   1 
ATOM   1957 C  CA  . LEU A 1 232 ? 19.813  -53.838 -6.984  1.00 35.04  ? 253  LEU A CA  1 
ATOM   1958 C  C   . LEU A 1 232 ? 21.306  -53.647 -7.203  1.00 36.97  ? 253  LEU A C   1 
ATOM   1959 O  O   . LEU A 1 232 ? 21.709  -52.819 -8.008  1.00 44.64  ? 253  LEU A O   1 
ATOM   1960 C  CB  . LEU A 1 232 ? 19.291  -54.999 -7.852  1.00 36.36  ? 253  LEU A CB  1 
ATOM   1961 C  CG  . LEU A 1 232 ? 17.803  -55.312 -7.688  1.00 44.04  ? 253  LEU A CG  1 
ATOM   1962 C  CD1 . LEU A 1 232 ? 17.386  -56.447 -8.594  1.00 39.65  ? 253  LEU A CD1 1 
ATOM   1963 C  CD2 . LEU A 1 232 ? 17.495  -55.633 -6.239  1.00 47.23  ? 253  LEU A CD2 1 
ATOM   1964 N  N   . PRO A 1 233 ? 22.150  -54.416 -6.495  1.00 47.65  ? 254  PRO A N   1 
ATOM   1965 C  CA  . PRO A 1 233 ? 23.569  -54.368 -6.869  1.00 47.70  ? 254  PRO A CA  1 
ATOM   1966 C  C   . PRO A 1 233 ? 23.749  -54.788 -8.324  1.00 48.40  ? 254  PRO A C   1 
ATOM   1967 O  O   . PRO A 1 233 ? 22.839  -55.405 -8.886  1.00 48.64  ? 254  PRO A O   1 
ATOM   1968 C  CB  . PRO A 1 233 ? 24.234  -55.360 -5.913  1.00 51.75  ? 254  PRO A CB  1 
ATOM   1969 C  CG  . PRO A 1 233 ? 23.126  -56.175 -5.371  1.00 48.97  ? 254  PRO A CG  1 
ATOM   1970 C  CD  . PRO A 1 233 ? 21.912  -55.313 -5.356  1.00 49.57  ? 254  PRO A CD  1 
ATOM   1971 N  N   . PRO A 1 234 ? 24.881  -54.410 -8.942  1.00 55.06  ? 255  PRO A N   1 
ATOM   1972 C  CA  . PRO A 1 234 ? 25.185  -54.858 -10.309 1.00 54.22  ? 255  PRO A CA  1 
ATOM   1973 C  C   . PRO A 1 234 ? 25.141  -56.384 -10.447 1.00 56.58  ? 255  PRO A C   1 
ATOM   1974 O  O   . PRO A 1 234 ? 25.596  -57.083 -9.537  1.00 54.33  ? 255  PRO A O   1 
ATOM   1975 C  CB  . PRO A 1 234 ? 26.626  -54.350 -10.535 1.00 57.42  ? 255  PRO A CB  1 
ATOM   1976 C  CG  . PRO A 1 234 ? 26.816  -53.264 -9.568  1.00 59.65  ? 255  PRO A CG  1 
ATOM   1977 C  CD  . PRO A 1 234 ? 25.994  -53.633 -8.359  1.00 57.38  ? 255  PRO A CD  1 
ATOM   1978 N  N   . LYS A 1 235 ? 24.616  -56.903 -11.553 1.00 61.83  ? 256  LYS A N   1 
ATOM   1979 C  CA  . LYS A 1 235 ? 24.865  -58.308 -11.876 1.00 62.21  ? 256  LYS A CA  1 
ATOM   1980 C  C   . LYS A 1 235 ? 26.358  -58.537 -12.003 1.00 59.77  ? 256  LYS A C   1 
ATOM   1981 O  O   . LYS A 1 235 ? 26.895  -59.473 -11.409 1.00 73.21  ? 256  LYS A O   1 
ATOM   1982 C  CB  . LYS A 1 235 ? 24.155  -58.711 -13.166 1.00 65.49  ? 256  LYS A CB  1 
ATOM   1983 C  CG  . LYS A 1 235 ? 22.674  -58.472 -13.138 1.00 57.75  ? 256  LYS A CG  1 
ATOM   1984 C  CD  . LYS A 1 235 ? 22.011  -58.937 -14.445 1.00 55.30  ? 256  LYS A CD  1 
ATOM   1985 C  CE  . LYS A 1 235 ? 20.504  -58.727 -14.434 1.00 60.29  ? 256  LYS A CE  1 
ATOM   1986 N  NZ  . LYS A 1 235 ? 19.828  -59.297 -15.634 1.00 59.82  ? 256  LYS A NZ  1 
HETATM 1987 C  C1  . NAG B 2 .   ? 12.391  -33.049 3.643   1.00 57.19  ? 1501 NAG A C1  1 
HETATM 1988 C  C2  . NAG B 2 .   ? 13.035  -31.818 3.041   1.00 69.55  ? 1501 NAG A C2  1 
HETATM 1989 C  C3  . NAG B 2 .   ? 14.534  -31.961 3.142   1.00 67.06  ? 1501 NAG A C3  1 
HETATM 1990 C  C4  . NAG B 2 .   ? 14.998  -33.034 2.165   1.00 67.85  ? 1501 NAG A C4  1 
HETATM 1991 C  C5  . NAG B 2 .   ? 13.976  -34.155 2.017   1.00 59.46  ? 1501 NAG A C5  1 
HETATM 1992 C  C6  . NAG B 2 .   ? 14.634  -35.463 1.672   1.00 63.42  ? 1501 NAG A C6  1 
HETATM 1993 C  C7  . NAG B 2 .   ? 11.365  -31.545 1.224   1.00 78.22  ? 1501 NAG A C7  1 
HETATM 1994 C  C8  . NAG B 2 .   ? 11.164  -31.433 -0.262  1.00 60.50  ? 1501 NAG A C8  1 
HETATM 1995 N  N2  . NAG B 2 .   ? 12.637  -31.660 1.643   1.00 81.83  ? 1501 NAG A N2  1 
HETATM 1996 O  O3  . NAG B 2 .   ? 14.880  -32.326 4.476   1.00 84.74  ? 1501 NAG A O3  1 
HETATM 1997 O  O4  . NAG B 2 .   ? 15.109  -32.457 0.872   1.00 78.12  ? 1501 NAG A O4  1 
HETATM 1998 O  O5  . NAG B 2 .   ? 13.187  -34.317 3.218   1.00 50.01  ? 1501 NAG A O5  1 
HETATM 1999 O  O6  . NAG B 2 .   ? 16.049  -35.332 1.681   1.00 63.62  ? 1501 NAG A O6  1 
HETATM 2000 O  O7  . NAG B 2 .   ? 10.420  -31.496 2.013   1.00 88.76  ? 1501 NAG A O7  1 
HETATM 2001 C  C1  . FUC C 3 .   ? 15.664  -38.551 2.485   1.00 71.76  ? 1502 FUC A C1  1 
HETATM 2002 C  C2  . FUC C 3 .   ? 17.167  -38.029 2.487   1.00 75.18  ? 1502 FUC A C2  1 
HETATM 2003 C  C3  . FUC C 3 .   ? 17.733  -37.617 3.912   1.00 71.17  ? 1502 FUC A C3  1 
HETATM 2004 C  C4  . FUC C 3 .   ? 16.652  -37.096 4.951   1.00 67.36  ? 1502 FUC A C4  1 
HETATM 2005 C  C5  . FUC C 3 .   ? 15.232  -37.726 4.797   1.00 71.43  ? 1502 FUC A C5  1 
HETATM 2006 C  C6  . FUC C 3 .   ? 15.081  -39.097 5.508   1.00 74.97  ? 1502 FUC A C6  1 
HETATM 2007 O  O2  . FUC C 3 .   ? 17.459  -37.007 1.479   1.00 75.77  ? 1502 FUC A O2  1 
HETATM 2008 O  O3  . FUC C 3 .   ? 18.520  -38.713 4.507   1.00 77.56  ? 1502 FUC A O3  1 
HETATM 2009 O  O4  . FUC C 3 .   ? 17.129  -37.311 6.299   1.00 75.74  ? 1502 FUC A O4  1 
HETATM 2010 O  O5  . FUC C 3 .   ? 14.769  -37.861 3.389   1.00 71.68  ? 1502 FUC A O5  1 
HETATM 2011 C  C1  . NAG D 2 .   ? 17.765  -31.208 1.613   1.00 73.62  ? 1503 NAG A C1  1 
HETATM 2012 C  C2  . NAG D 2 .   ? 17.529  -31.227 0.115   1.00 70.28  ? 1503 NAG A C2  1 
HETATM 2013 C  C3  . NAG D 2 .   ? 18.226  -30.023 -0.526  1.00 68.91  ? 1503 NAG A C3  1 
HETATM 2014 C  C4  . NAG D 2 .   ? 17.666  -28.741 0.095   1.00 72.42  ? 1503 NAG A C4  1 
HETATM 2015 C  C5  . NAG D 2 .   ? 17.706  -28.785 1.639   1.00 72.90  ? 1503 NAG A C5  1 
HETATM 2016 C  C6  . NAG D 2 .   ? 16.905  -27.679 2.289   1.00 72.84  ? 1503 NAG A C6  1 
HETATM 2017 C  C7  . NAG D 2 .   ? 17.227  -33.120 -1.436  1.00 70.26  ? 1503 NAG A C7  1 
HETATM 2018 C  C8  . NAG D 2 .   ? 17.767  -34.447 -1.911  1.00 62.95  ? 1503 NAG A C8  1 
HETATM 2019 N  N2  . NAG D 2 .   ? 17.940  -32.499 -0.482  1.00 74.45  ? 1503 NAG A N2  1 
HETATM 2020 O  O3  . NAG D 2 .   ? 18.081  -29.992 -1.944  1.00 73.97  ? 1503 NAG A O3  1 
HETATM 2021 O  O4  . NAG D 2 .   ? 18.411  -27.613 -0.370  1.00 81.48  ? 1503 NAG A O4  1 
HETATM 2022 O  O5  . NAG D 2 .   ? 17.177  -30.019 2.165   1.00 76.92  ? 1503 NAG A O5  1 
HETATM 2023 O  O6  . NAG D 2 .   ? 16.400  -28.107 3.548   1.00 70.64  ? 1503 NAG A O6  1 
HETATM 2024 O  O7  . NAG D 2 .   ? 16.201  -32.623 -1.915  1.00 70.84  ? 1503 NAG A O7  1 
HETATM 2025 C  C1  . PEG E 4 .   ? 1.811   -53.084 -14.721 1.00 50.24  ? 1504 PEG A C1  1 
HETATM 2026 O  O1  . PEG E 4 .   ? 2.277   -52.752 -16.021 1.00 60.60  ? 1504 PEG A O1  1 
HETATM 2027 C  C2  . PEG E 4 .   ? 2.846   -53.853 -13.855 1.00 51.70  ? 1504 PEG A C2  1 
HETATM 2028 O  O2  . PEG E 4 .   ? 2.423   -53.900 -12.466 1.00 53.63  ? 1504 PEG A O2  1 
HETATM 2029 C  C3  . PEG E 4 .   ? 1.069   -53.497 -12.156 1.00 38.73  ? 1504 PEG A C3  1 
HETATM 2030 C  C4  . PEG E 4 .   ? 0.731   -52.916 -10.805 1.00 40.85  ? 1504 PEG A C4  1 
HETATM 2031 O  O4  . PEG E 4 .   ? -0.000  -51.727 -11.139 1.00 32.83  ? 1504 PEG A O4  1 
HETATM 2032 O  OH2 . 1PE F 5 .   ? -16.097 -28.970 -13.290 1.00 68.88  ? 1505 1PE A OH2 1 
HETATM 2033 C  C12 . 1PE F 5 .   ? -16.121 -27.974 -14.248 1.00 68.27  ? 1505 1PE A C12 1 
HETATM 2034 C  C22 . 1PE F 5 .   ? -17.049 -28.389 -15.435 1.00 51.81  ? 1505 1PE A C22 1 
HETATM 2035 O  OH3 . 1PE F 5 .   ? -17.111 -27.545 -16.617 1.00 52.60  ? 1505 1PE A OH3 1 
HETATM 2036 C  C13 . 1PE F 5 .   ? -17.210 -28.107 -19.077 1.00 39.64  ? 1505 1PE A C13 1 
HETATM 2037 C  C23 . 1PE F 5 .   ? -16.460 -28.094 -17.792 1.00 24.86  ? 1505 1PE A C23 1 
HETATM 2038 O  OH4 . 1PE F 5 .   ? -16.230 -28.463 -20.054 1.00 48.86  ? 1505 1PE A OH4 1 
HETATM 2039 C  C14 . 1PE F 5 .   ? -14.316 -27.687 -21.189 1.00 43.01  ? 1505 1PE A C14 1 
HETATM 2040 C  C24 . 1PE F 5 .   ? -15.085 -27.637 -19.921 1.00 34.94  ? 1505 1PE A C24 1 
HETATM 2041 O  OH5 . 1PE F 5 .   ? -13.097 -28.162 -20.775 1.00 52.19  ? 1505 1PE A OH5 1 
HETATM 2042 C  C15 . 1PE F 5 .   ? -12.716 -25.738 -20.824 1.00 24.72  ? 1505 1PE A C15 1 
HETATM 2043 C  C25 . 1PE F 5 .   ? -12.131 -27.155 -20.683 1.00 36.69  ? 1505 1PE A C25 1 
HETATM 2044 O  OH6 . 1PE F 5 .   ? -11.989 -24.868 -19.954 1.00 49.84  ? 1505 1PE A OH6 1 
HETATM 2045 C  C16 . 1PE F 5 .   ? -12.692 -22.784 -20.589 1.00 55.64  ? 1505 1PE A C16 1 
HETATM 2046 C  C26 . 1PE F 5 .   ? -11.516 -23.625 -20.503 1.00 45.96  ? 1505 1PE A C26 1 
HETATM 2047 O  OH7 . 1PE F 5 .   ? -13.608 -23.217 -19.586 1.00 41.73  ? 1505 1PE A OH7 1 
HETATM 2048 C  C1  . PEG G 4 .   ? -46.656 -39.716 -38.762 1.00 79.12  ? 1506 PEG A C1  1 
HETATM 2049 O  O1  . PEG G 4 .   ? -45.778 -40.444 -37.887 1.00 77.15  ? 1506 PEG A O1  1 
HETATM 2050 C  C2  . PEG G 4 .   ? -47.025 -40.533 -40.051 1.00 71.46  ? 1506 PEG A C2  1 
HETATM 2051 O  O2  . PEG G 4 .   ? -47.584 -39.640 -41.045 1.00 64.40  ? 1506 PEG A O2  1 
HETATM 2052 C  C3  . PEG G 4 .   ? -48.630 -38.842 -40.450 1.00 64.41  ? 1506 PEG A C3  1 
HETATM 2053 C  C4  . PEG G 4 .   ? -48.642 -37.418 -40.976 1.00 63.09  ? 1506 PEG A C4  1 
HETATM 2054 O  O4  . PEG G 4 .   ? -49.677 -36.715 -40.318 1.00 67.69  ? 1506 PEG A O4  1 
HETATM 2055 CL CL  . CL  H 6 .   ? -6.235  -54.762 -14.419 1.00 32.21  ? 1507 CL  A CL  1 
HETATM 2056 CA CA  . CA  I 7 .   ? -14.034 -37.693 -34.824 0.50 33.07  2 1508 CA  A CA  1 
HETATM 2057 CA CA  . CA  J 7 .   ? -51.727 -51.727 -51.252 0.49 95.98  2 1509 CA  A CA  1 
HETATM 2058 O  O   . HOH K 8 .   ? -37.129 -53.859 -59.381 1.00 45.86  ? 1601 HOH A O   1 
HETATM 2059 O  O   . HOH K 8 .   ? -24.169 -31.425 -45.240 1.00 52.66  ? 1602 HOH A O   1 
HETATM 2060 O  O   . HOH K 8 .   ? -28.939 -42.081 -22.043 1.00 57.56  ? 1603 HOH A O   1 
HETATM 2061 O  O   . HOH K 8 .   ? -17.182 -45.797 -32.961 1.00 50.77  ? 1604 HOH A O   1 
HETATM 2062 O  O   . HOH K 8 .   ? 27.108  -47.554 -6.180  1.00 71.64  ? 1605 HOH A O   1 
HETATM 2063 O  O   . HOH K 8 .   ? 14.896  -31.008 -1.514  1.00 67.74  ? 1606 HOH A O   1 
HETATM 2064 O  O   . HOH K 8 .   ? -32.212 -47.453 -18.385 1.00 65.68  ? 1607 HOH A O   1 
HETATM 2065 O  O   . HOH K 8 .   ? -31.240 -55.085 -18.596 1.00 64.36  ? 1608 HOH A O   1 
HETATM 2066 O  O   . HOH K 8 .   ? -12.135 -35.119 -10.610 1.00 64.62  ? 1609 HOH A O   1 
HETATM 2067 O  O   . HOH K 8 .   ? -16.923 -43.089 -37.384 1.00 37.42  ? 1610 HOH A O   1 
HETATM 2068 O  O   . HOH K 8 .   ? 14.624  -46.443 3.647   1.00 51.14  ? 1611 HOH A O   1 
HETATM 2069 O  O   . HOH K 8 .   ? -51.240 -48.671 -54.278 1.00 35.33  ? 1612 HOH A O   1 
HETATM 2070 O  O   . HOH K 8 .   ? 17.187  -50.600 -16.792 1.00 59.88  ? 1613 HOH A O   1 
HETATM 2071 O  O   . HOH K 8 .   ? -37.960 -44.560 -30.442 1.00 53.71  ? 1614 HOH A O   1 
HETATM 2072 O  O   . HOH K 8 .   ? -6.108  -30.335 -11.373 1.00 44.28  ? 1615 HOH A O   1 
HETATM 2073 O  O   . HOH K 8 .   ? -35.876 -53.111 -56.635 1.00 32.54  ? 1616 HOH A O   1 
HETATM 2074 O  O   . HOH K 8 .   ? -9.144  -36.618 -19.295 1.00 29.54  ? 1617 HOH A O   1 
HETATM 2075 O  O   . HOH K 8 .   ? 18.068  -59.317 -11.976 1.00 39.52  ? 1618 HOH A O   1 
HETATM 2076 O  O   . HOH K 8 .   ? -31.470 -48.352 -59.459 1.00 52.10  ? 1619 HOH A O   1 
HETATM 2077 O  O   . HOH K 8 .   ? -50.447 -30.298 -52.812 1.00 44.71  ? 1620 HOH A O   1 
HETATM 2078 O  O   . HOH K 8 .   ? 5.132   -46.183 -3.466  1.00 41.43  ? 1621 HOH A O   1 
HETATM 2079 O  O   . HOH K 8 .   ? -52.271 -34.256 -57.183 1.00 44.04  ? 1622 HOH A O   1 
HETATM 2080 O  O   . HOH K 8 .   ? -17.761 -49.451 -21.591 1.00 43.60  ? 1623 HOH A O   1 
HETATM 2081 O  O   . HOH K 8 .   ? 12.233  -41.760 -2.590  1.00 43.64  ? 1624 HOH A O   1 
HETATM 2082 O  O   . HOH K 8 .   ? -7.915  -46.478 -5.398  1.00 37.23  ? 1625 HOH A O   1 
HETATM 2083 O  O   . HOH K 8 .   ? -18.404 -37.779 -41.570 1.00 26.59  ? 1626 HOH A O   1 
HETATM 2084 O  O   . HOH K 8 .   ? 2.674   -30.853 -11.162 1.00 50.45  ? 1627 HOH A O   1 
HETATM 2085 O  O   . HOH K 8 .   ? -22.747 -28.471 -39.288 1.00 50.85  ? 1628 HOH A O   1 
HETATM 2086 O  O   . HOH K 8 .   ? -42.947 -36.665 -33.807 1.00 57.31  ? 1629 HOH A O   1 
HETATM 2087 O  O   . HOH K 8 .   ? -3.803  -44.343 -24.038 1.00 31.92  ? 1630 HOH A O   1 
HETATM 2088 O  O   . HOH K 8 .   ? 20.217  -61.844 -15.342 1.00 49.59  ? 1631 HOH A O   1 
HETATM 2089 O  O   . HOH K 8 .   ? 2.719   -48.459 -21.730 1.00 50.80  ? 1632 HOH A O   1 
HETATM 2090 O  O   . HOH K 8 .   ? -14.607 -33.573 -12.364 1.00 40.59  ? 1633 HOH A O   1 
HETATM 2091 O  O   . HOH K 8 .   ? -30.957 -41.475 -55.686 1.00 36.05  ? 1634 HOH A O   1 
HETATM 2092 O  O   . HOH K 8 .   ? 0.528   -32.767 -14.030 1.00 32.80  ? 1635 HOH A O   1 
HETATM 2093 O  O   . HOH K 8 .   ? -7.486  -44.841 -25.513 1.00 47.41  ? 1636 HOH A O   1 
HETATM 2094 O  O   . HOH K 8 .   ? -14.947 -36.348 -30.313 1.00 30.50  ? 1637 HOH A O   1 
HETATM 2095 O  O   . HOH K 8 .   ? 24.805  -52.962 -13.516 1.00 57.76  ? 1638 HOH A O   1 
HETATM 2096 O  O   . HOH K 8 .   ? 3.279   -41.140 4.405   1.00 44.24  ? 1639 HOH A O   1 
HETATM 2097 O  O   . HOH K 8 .   ? -21.120 -37.462 -38.054 1.00 29.20  ? 1640 HOH A O   1 
HETATM 2098 O  O   . HOH K 8 .   ? -51.727 -51.727 -49.221 0.25 33.99  ? 1641 HOH A O   1 
HETATM 2099 O  O   . HOH K 8 .   ? -35.655 -36.969 -29.980 1.00 43.16  ? 1642 HOH A O   1 
HETATM 2100 O  O   . HOH K 8 .   ? -13.150 -40.730 -25.060 1.00 41.55  ? 1643 HOH A O   1 
HETATM 2101 O  O   . HOH K 8 .   ? -22.830 -36.671 -18.398 1.00 44.61  ? 1644 HOH A O   1 
HETATM 2102 O  O   . HOH K 8 .   ? 8.361   -35.108 -18.991 1.00 45.68  ? 1645 HOH A O   1 
HETATM 2103 O  O   . HOH K 8 .   ? -26.963 -27.070 -44.734 1.00 60.10  ? 1646 HOH A O   1 
HETATM 2104 O  O   . HOH K 8 .   ? -10.152 -50.517 -19.457 1.00 52.36  ? 1647 HOH A O   1 
HETATM 2105 O  O   . HOH K 8 .   ? -34.538 -36.756 -59.348 1.00 57.47  ? 1648 HOH A O   1 
HETATM 2106 O  O   . HOH K 8 .   ? -31.196 -49.155 -54.847 1.00 24.07  ? 1649 HOH A O   1 
HETATM 2107 O  O   . HOH K 8 .   ? -15.718 -41.853 -26.856 1.00 41.18  ? 1650 HOH A O   1 
HETATM 2108 O  O   . HOH K 8 .   ? -44.464 -43.546 -38.289 1.00 48.99  ? 1651 HOH A O   1 
HETATM 2109 O  O   . HOH K 8 .   ? -27.422 -46.711 -53.794 1.00 38.82  ? 1652 HOH A O   1 
HETATM 2110 O  O   . HOH K 8 .   ? -29.469 -29.218 -43.113 1.00 50.30  ? 1653 HOH A O   1 
HETATM 2111 O  O   . HOH K 8 .   ? -34.788 -54.267 -48.043 1.00 23.74  ? 1654 HOH A O   1 
HETATM 2112 O  O   . HOH K 8 .   ? -25.161 -50.412 -41.175 1.00 44.19  ? 1655 HOH A O   1 
HETATM 2113 O  O   . HOH K 8 .   ? -44.186 -37.317 -58.714 1.00 40.89  ? 1656 HOH A O   1 
HETATM 2114 O  O   . HOH K 8 .   ? -29.428 -48.289 -20.702 1.00 64.70  ? 1657 HOH A O   1 
HETATM 2115 O  O   . HOH K 8 .   ? -26.601 -46.827 -51.031 1.00 26.88  ? 1658 HOH A O   1 
HETATM 2116 O  O   . HOH K 8 .   ? -10.648 -36.729 -16.829 1.00 26.05  ? 1659 HOH A O   1 
HETATM 2117 O  O   . HOH K 8 .   ? -15.593 -24.850 -20.328 1.00 29.37  ? 1660 HOH A O   1 
HETATM 2118 O  O   . HOH K 8 .   ? -18.996 -49.400 -20.314 1.00 55.76  ? 1661 HOH A O   1 
HETATM 2119 O  O   . HOH K 8 .   ? -21.475 -46.718 -40.964 1.00 33.02  ? 1662 HOH A O   1 
HETATM 2120 O  O   . HOH K 8 .   ? -33.435 -51.998 -31.722 1.00 43.54  ? 1663 HOH A O   1 
HETATM 2121 O  O   . HOH K 8 .   ? 15.020  -37.956 -15.138 1.00 48.85  ? 1664 HOH A O   1 
HETATM 2122 O  O   . HOH K 8 .   ? 20.069  -36.756 2.065   1.00 72.93  ? 1665 HOH A O   1 
HETATM 2123 O  O   . HOH K 8 .   ? -36.983 -32.370 -45.899 1.00 40.80  ? 1666 HOH A O   1 
HETATM 2124 O  O   . HOH K 8 .   ? -32.206 -38.518 -34.562 1.00 25.64  ? 1667 HOH A O   1 
HETATM 2125 O  O   . HOH K 8 .   ? -14.266 -20.626 -19.266 1.00 26.65  ? 1668 HOH A O   1 
HETATM 2126 O  O   . HOH K 8 .   ? 8.495   -37.278 -17.651 1.00 44.86  ? 1669 HOH A O   1 
HETATM 2127 O  O   . HOH K 8 .   ? -41.636 -32.916 -52.305 1.00 34.24  ? 1670 HOH A O   1 
HETATM 2128 O  O   . HOH K 8 .   ? -12.186 -37.229 -8.855  1.00 36.94  ? 1671 HOH A O   1 
HETATM 2129 O  O   . HOH K 8 .   ? 3.686   -38.516 0.688   1.00 43.05  ? 1672 HOH A O   1 
HETATM 2130 O  O   . HOH K 8 .   ? -8.225  -25.743 -13.756 1.00 42.20  ? 1673 HOH A O   1 
HETATM 2131 O  O   . HOH K 8 .   ? -24.520 -31.555 -31.716 1.00 37.91  ? 1674 HOH A O   1 
HETATM 2132 O  O   . HOH K 8 .   ? -32.659 -37.873 -31.780 1.00 29.94  ? 1675 HOH A O   1 
HETATM 2133 O  O   . HOH K 8 .   ? -9.704  -36.366 -9.509  1.00 43.24  ? 1676 HOH A O   1 
HETATM 2134 O  O   . HOH K 8 .   ? -18.323 -31.366 -32.810 1.00 38.36  ? 1677 HOH A O   1 
HETATM 2135 O  O   . HOH K 8 .   ? -26.816 -48.845 -44.401 1.00 28.58  ? 1678 HOH A O   1 
HETATM 2136 O  O   . HOH K 8 .   ? -3.385  -28.675 -15.976 1.00 46.35  ? 1679 HOH A O   1 
HETATM 2137 O  O   . HOH K 8 .   ? -42.923 -31.917 -50.119 1.00 51.22  ? 1680 HOH A O   1 
HETATM 2138 O  O   . HOH K 8 .   ? -26.155 -30.628 -33.942 1.00 37.91  ? 1681 HOH A O   1 
HETATM 2139 O  O   . HOH K 8 .   ? -47.914 -33.399 -50.393 1.00 25.29  ? 1682 HOH A O   1 
HETATM 2140 O  O   . HOH K 8 .   ? 24.610  -42.903 -9.451  1.00 62.86  ? 1683 HOH A O   1 
HETATM 2141 O  O   . HOH K 8 .   ? -30.984 -37.747 -25.112 1.00 28.38  ? 1684 HOH A O   1 
HETATM 2142 O  O   . HOH K 8 .   ? -27.923 -49.876 -46.948 1.00 43.17  ? 1685 HOH A O   1 
HETATM 2143 O  O   . HOH K 8 .   ? -12.066 -39.741 -7.851  1.00 34.74  ? 1686 HOH A O   1 
HETATM 2144 O  O   . HOH K 8 .   ? 13.825  -49.557 -15.634 1.00 42.46  ? 1687 HOH A O   1 
HETATM 2145 O  O   . HOH K 8 .   ? -14.958 -33.958 -33.301 1.00 31.52  ? 1688 HOH A O   1 
HETATM 2146 O  O   . HOH K 8 .   ? -20.176 -37.204 -35.344 1.00 25.19  ? 1689 HOH A O   1 
HETATM 2147 O  O   . HOH K 8 .   ? -20.557 -48.483 -31.499 1.00 39.37  ? 1690 HOH A O   1 
HETATM 2148 O  O   . HOH K 8 .   ? -10.765 -30.662 -18.693 1.00 29.51  ? 1691 HOH A O   1 
HETATM 2149 O  O   . HOH K 8 .   ? 13.521  -35.235 7.049   1.00 45.85  ? 1692 HOH A O   1 
HETATM 2150 O  O   . HOH K 8 .   ? -13.013 -45.188 -24.814 1.00 35.92  ? 1693 HOH A O   1 
HETATM 2151 O  O   . HOH K 8 .   ? -33.210 -51.145 -44.999 1.00 28.29  ? 1694 HOH A O   1 
HETATM 2152 O  O   . HOH K 8 .   ? -44.274 -33.807 -58.251 1.00 71.59  ? 1695 HOH A O   1 
HETATM 2153 O  O   . HOH K 8 .   ? -37.458 -45.922 -36.766 1.00 43.04  ? 1696 HOH A O   1 
HETATM 2154 O  O   . HOH K 8 .   ? -10.948 -33.433 -18.814 1.00 26.24  ? 1697 HOH A O   1 
HETATM 2155 O  O   . HOH K 8 .   ? -36.597 -33.788 -32.589 1.00 43.59  ? 1698 HOH A O   1 
HETATM 2156 O  O   . HOH K 8 .   ? -35.078 -40.874 -56.988 1.00 32.94  ? 1699 HOH A O   1 
HETATM 2157 O  O   . HOH K 8 .   ? -36.627 -50.166 -35.022 1.00 33.51  ? 1700 HOH A O   1 
HETATM 2158 O  O   . HOH K 8 .   ? -33.161 -38.965 -26.240 1.00 42.08  ? 1701 HOH A O   1 
HETATM 2159 O  O   . HOH K 8 .   ? 1.507   -47.799 -17.240 1.00 32.35  ? 1702 HOH A O   1 
HETATM 2160 O  O   . HOH K 8 .   ? -13.718 -40.516 -38.396 1.00 55.38  ? 1703 HOH A O   1 
HETATM 2161 O  O   . HOH K 8 .   ? -17.103 -44.171 -14.522 1.00 33.47  ? 1704 HOH A O   1 
HETATM 2162 O  O   . HOH K 8 .   ? -18.714 -41.221 -12.847 1.00 40.75  ? 1705 HOH A O   1 
HETATM 2163 O  O   . HOH K 8 .   ? -33.515 -45.306 -30.965 1.00 32.92  ? 1706 HOH A O   1 
HETATM 2164 O  O   . HOH K 8 .   ? -33.418 -54.565 -38.408 1.00 33.84  ? 1707 HOH A O   1 
HETATM 2165 O  O   . HOH K 8 .   ? -6.149  -31.366 -23.701 1.00 31.98  ? 1708 HOH A O   1 
HETATM 2166 O  O   . HOH K 8 .   ? -43.142 -35.319 -38.265 1.00 37.39  ? 1709 HOH A O   1 
HETATM 2167 O  O   . HOH K 8 .   ? 4.816   -43.712 -4.045  1.00 34.84  ? 1710 HOH A O   1 
HETATM 2168 O  O   . HOH K 8 .   ? 23.990  -55.357 -13.798 1.00 49.75  ? 1711 HOH A O   1 
HETATM 2169 O  O   . HOH K 8 .   ? -25.685 -35.118 -46.909 1.00 27.97  ? 1712 HOH A O   1 
HETATM 2170 O  O   . HOH K 8 .   ? -34.042 -31.597 -43.315 1.00 49.77  ? 1713 HOH A O   1 
HETATM 2171 O  O   . HOH K 8 .   ? 17.290  -50.264 -3.127  1.00 38.31  ? 1714 HOH A O   1 
HETATM 2172 O  O   . HOH K 8 .   ? -27.711 -37.969 -53.176 1.00 37.92  ? 1715 HOH A O   1 
HETATM 2173 O  O   . HOH K 8 .   ? 15.951  -40.607 -10.008 1.00 53.63  ? 1716 HOH A O   1 
HETATM 2174 O  O   . HOH K 8 .   ? -18.012 -49.005 -18.295 1.00 52.97  ? 1717 HOH A O   1 
HETATM 2175 O  O   . HOH K 8 .   ? -15.947 -38.728 -35.865 1.00 34.43  ? 1718 HOH A O   1 
HETATM 2176 O  O   . HOH K 8 .   ? 6.043   -36.085 -17.914 1.00 32.21  ? 1719 HOH A O   1 
HETATM 2177 O  O   . HOH K 8 .   ? -15.583 -32.296 -29.926 1.00 30.27  ? 1720 HOH A O   1 
HETATM 2178 O  O   . HOH K 8 .   ? -9.202  -48.712 -22.320 1.00 41.72  ? 1721 HOH A O   1 
HETATM 2179 O  O   . HOH K 8 .   ? -28.700 -29.436 -39.216 1.00 55.00  ? 1722 HOH A O   1 
HETATM 2180 O  O   . HOH K 8 .   ? 10.578  -52.379 -5.276  1.00 39.54  ? 1723 HOH A O   1 
HETATM 2181 O  O   . HOH K 8 .   ? -36.514 -35.684 -59.595 1.00 53.73  ? 1724 HOH A O   1 
HETATM 2182 O  O   . HOH K 8 .   ? -17.674 -53.260 -20.258 1.00 49.50  ? 1725 HOH A O   1 
HETATM 2183 O  O   . HOH K 8 .   ? -0.542  -29.862 -13.744 1.00 47.65  ? 1726 HOH A O   1 
HETATM 2184 O  O   . HOH K 8 .   ? 5.868   -53.381 -11.564 1.00 34.54  ? 1727 HOH A O   1 
HETATM 2185 O  O   . HOH K 8 .   ? -39.228 -34.402 -55.002 1.00 32.90  ? 1728 HOH A O   1 
HETATM 2186 O  O   . HOH K 8 .   ? -8.393  -54.585 -19.025 1.00 53.02  ? 1729 HOH A O   1 
HETATM 2187 O  O   . HOH K 8 .   ? 15.488  -59.234 -6.665  1.00 40.67  ? 1730 HOH A O   1 
HETATM 2188 O  O   . HOH K 8 .   ? -42.900 -50.285 -57.155 1.00 31.65  ? 1731 HOH A O   1 
HETATM 2189 O  O   . HOH K 8 .   ? -29.760 -55.483 -36.472 1.00 59.87  ? 1732 HOH A O   1 
HETATM 2190 O  O   . HOH K 8 .   ? -35.806 -45.238 -28.982 1.00 51.68  ? 1733 HOH A O   1 
HETATM 2191 O  O   . HOH K 8 .   ? 9.685   -37.333 -19.005 1.00 53.16  ? 1734 HOH A O   1 
HETATM 2192 O  O   . HOH K 8 .   ? -17.448 -48.118 -15.680 1.00 61.30  ? 1735 HOH A O   1 
HETATM 2193 O  O   . HOH K 8 .   ? -23.294 -31.785 -38.059 1.00 29.49  ? 1736 HOH A O   1 
HETATM 2194 O  O   . HOH K 8 .   ? 11.332  -29.436 -8.542  1.00 53.04  ? 1737 HOH A O   1 
HETATM 2195 O  O   . HOH K 8 .   ? -37.240 -33.668 -59.122 1.00 53.08  ? 1738 HOH A O   1 
HETATM 2196 O  O   . HOH K 8 .   ? -41.652 -31.192 -45.225 1.00 56.78  ? 1739 HOH A O   1 
HETATM 2197 O  O   . HOH K 8 .   ? -6.562  -35.246 -23.792 1.00 25.03  ? 1740 HOH A O   1 
HETATM 2198 O  O   . HOH K 8 .   ? -48.849 -48.005 -55.082 1.00 26.48  ? 1741 HOH A O   1 
HETATM 2199 O  O   . HOH K 8 .   ? -37.199 -53.587 -37.358 1.00 51.68  ? 1742 HOH A O   1 
HETATM 2200 O  O   . HOH K 8 .   ? 7.707   -42.347 4.713   1.00 32.61  ? 1743 HOH A O   1 
HETATM 2201 O  O   . HOH K 8 .   ? -20.646 -34.880 -34.029 1.00 36.06  ? 1744 HOH A O   1 
HETATM 2202 O  O   . HOH K 8 .   ? -17.337 -43.149 -8.266  1.00 51.83  ? 1745 HOH A O   1 
HETATM 2203 O  O   . HOH K 8 .   ? 4.777   -44.880 -21.863 1.00 57.33  ? 1746 HOH A O   1 
HETATM 2204 O  O   . HOH K 8 .   ? -24.609 -54.176 -30.022 1.00 46.39  ? 1747 HOH A O   1 
HETATM 2205 O  O   . HOH K 8 .   ? -4.329  -49.675 -19.124 1.00 36.81  ? 1748 HOH A O   1 
HETATM 2206 O  O   . HOH K 8 .   ? -10.172 -35.691 -14.283 1.00 31.87  ? 1749 HOH A O   1 
HETATM 2207 O  O   . HOH K 8 .   ? -37.570 -45.905 -26.343 1.00 55.81  ? 1750 HOH A O   1 
HETATM 2208 O  O   . HOH K 8 .   ? 0.108   -36.509 -23.300 1.00 55.53  ? 1751 HOH A O   1 
HETATM 2209 O  O   . HOH K 8 .   ? -48.517 -29.081 -45.690 1.00 46.74  ? 1752 HOH A O   1 
HETATM 2210 O  O   . HOH K 8 .   ? -27.831 -34.006 -50.626 1.00 40.26  ? 1753 HOH A O   1 
HETATM 2211 O  O   . HOH K 8 .   ? 21.761  -60.004 -17.661 1.00 52.06  ? 1754 HOH A O   1 
HETATM 2212 O  O   . HOH K 8 .   ? -16.522 -38.175 -29.054 1.00 26.02  ? 1755 HOH A O   1 
HETATM 2213 O  O   . HOH K 8 .   ? -30.808 -30.174 -52.329 1.00 61.99  ? 1756 HOH A O   1 
HETATM 2214 O  O   . HOH K 8 .   ? -47.489 -48.509 -48.039 1.00 47.24  ? 1757 HOH A O   1 
HETATM 2215 O  O   . HOH K 8 .   ? -26.163 -53.972 -36.486 1.00 52.11  ? 1758 HOH A O   1 
HETATM 2216 O  O   . HOH K 8 .   ? -47.530 -36.038 -58.870 1.00 46.96  ? 1759 HOH A O   1 
HETATM 2217 O  O   . HOH K 8 .   ? -12.341 -39.386 -34.824 0.50 42.41  ? 1760 HOH A O   1 
HETATM 2218 O  O   . HOH K 8 .   ? 13.051  -48.926 -1.957  1.00 50.15  ? 1761 HOH A O   1 
HETATM 2219 O  O   . HOH K 8 .   ? -22.481 -46.510 -44.878 1.00 35.57  ? 1762 HOH A O   1 
HETATM 2220 O  O   . HOH K 8 .   ? 8.949   -29.717 -6.211  1.00 43.55  ? 1763 HOH A O   1 
HETATM 2221 O  O   . HOH K 8 .   ? -8.248  -33.379 -25.492 1.00 31.52  ? 1764 HOH A O   1 
HETATM 2222 O  O   . HOH K 8 .   ? -19.684 -29.964 -21.231 1.00 30.32  ? 1765 HOH A O   1 
HETATM 2223 O  O   . HOH K 8 .   ? 0.032   -48.647 -21.362 1.00 44.61  ? 1766 HOH A O   1 
HETATM 2224 O  O   . HOH K 8 .   ? -8.264  -29.608 -13.495 1.00 29.78  ? 1767 HOH A O   1 
HETATM 2225 O  O   . HOH K 8 .   ? -29.893 -30.140 -48.980 1.00 42.36  ? 1768 HOH A O   1 
HETATM 2226 O  O   . HOH K 8 .   ? -20.642 -36.112 -16.398 1.00 35.56  ? 1769 HOH A O   1 
HETATM 2227 O  O   . HOH K 8 .   ? -46.024 -30.428 -40.139 1.00 44.83  ? 1770 HOH A O   1 
HETATM 2228 O  O   . HOH K 8 .   ? -15.653 -40.216 -30.890 1.00 27.97  ? 1771 HOH A O   1 
HETATM 2229 O  O   . HOH K 8 .   ? -48.130 -56.176 -45.704 1.00 48.20  ? 1772 HOH A O   1 
HETATM 2230 O  O   . HOH K 8 .   ? 5.968   -31.528 -22.669 1.00 47.44  ? 1773 HOH A O   1 
HETATM 2231 O  O   . HOH K 8 .   ? -28.398 -45.273 -38.262 1.00 30.41  ? 1774 HOH A O   1 
HETATM 2232 O  O   . HOH K 8 .   ? -37.415 -46.942 -15.069 1.00 62.38  ? 1775 HOH A O   1 
HETATM 2233 O  O   . HOH K 8 .   ? -2.312  -31.075 -23.357 1.00 48.00  ? 1776 HOH A O   1 
HETATM 2234 O  O   . HOH K 8 .   ? -0.638  -33.534 -6.675  1.00 58.76  ? 1777 HOH A O   1 
HETATM 2235 O  O   . HOH K 8 .   ? -46.941 -50.051 -54.843 1.00 26.61  ? 1778 HOH A O   1 
HETATM 2236 O  O   . HOH K 8 .   ? -5.404  -26.942 -15.434 1.00 39.56  ? 1779 HOH A O   1 
HETATM 2237 O  O   . HOH K 8 .   ? -14.906 -39.025 -26.500 1.00 29.45  ? 1780 HOH A O   1 
HETATM 2238 O  O   . HOH K 8 .   ? 14.283  -51.915 -14.396 1.00 44.93  ? 1781 HOH A O   1 
HETATM 2239 O  O   . HOH K 8 .   ? 9.951   -32.940 -17.569 1.00 44.08  ? 1782 HOH A O   1 
HETATM 2240 O  O   . HOH K 8 .   ? -8.523  -37.932 -27.125 1.00 57.95  ? 1783 HOH A O   1 
HETATM 2241 O  O   . HOH K 8 .   ? -46.600 -56.168 -43.595 1.00 56.69  ? 1784 HOH A O   1 
HETATM 2242 O  O   . HOH K 8 .   ? -12.386 -48.936 -25.317 1.00 55.33  ? 1785 HOH A O   1 
HETATM 2243 O  O   . HOH K 8 .   ? 22.685  -54.167 -19.538 1.00 66.48  ? 1786 HOH A O   1 
HETATM 2244 O  O   . HOH K 8 .   ? -26.447 -39.462 -57.146 1.00 65.91  ? 1787 HOH A O   1 
HETATM 2245 O  O   . HOH K 8 .   ? -38.830 -39.565 -62.572 1.00 59.57  ? 1788 HOH A O   1 
HETATM 2246 O  O   . HOH K 8 .   ? -16.680 -45.220 -30.711 1.00 48.29  ? 1789 HOH A O   1 
HETATM 2247 O  O   . HOH K 8 .   ? -8.547  -33.730 -8.421  1.00 39.37  ? 1790 HOH A O   1 
HETATM 2248 O  O   . HOH K 8 .   ? -7.953  -48.313 -16.023 1.00 23.87  ? 1791 HOH A O   1 
HETATM 2249 O  O   . HOH K 8 .   ? -16.102 -51.169 -20.793 1.00 43.93  ? 1792 HOH A O   1 
HETATM 2250 O  O   . HOH K 8 .   ? 22.088  -55.445 -15.630 1.00 53.47  ? 1793 HOH A O   1 
HETATM 2251 O  O   . HOH K 8 .   ? -43.606 -32.414 -44.256 1.00 35.19  ? 1794 HOH A O   1 
HETATM 2252 O  O   . HOH K 8 .   ? -49.999 -32.608 -46.418 1.00 27.01  ? 1795 HOH A O   1 
HETATM 2253 O  O   . HOH K 8 .   ? -51.727 -51.727 -53.889 0.25 37.76  ? 1796 HOH A O   1 
HETATM 2254 O  O   . HOH K 8 .   ? -36.815 -32.856 -43.275 1.00 42.09  ? 1797 HOH A O   1 
HETATM 2255 O  O   . HOH K 8 .   ? 22.917  -40.781 -10.653 1.00 73.56  ? 1798 HOH A O   1 
HETATM 2256 O  O   . HOH K 8 .   ? -22.694 -35.477 -20.482 1.00 44.07  ? 1799 HOH A O   1 
HETATM 2257 O  O   . HOH K 8 .   ? -29.478 -28.334 -47.297 1.00 60.47  ? 1800 HOH A O   1 
HETATM 2258 O  O   . HOH K 8 .   ? -33.725 -38.800 -28.849 1.00 40.94  ? 1801 HOH A O   1 
HETATM 2259 O  O   . HOH K 8 .   ? 17.613  -40.193 7.131   1.00 55.70  ? 1802 HOH A O   1 
HETATM 2260 O  O   . HOH K 8 .   ? -43.084 -51.479 -39.197 1.00 60.22  ? 1803 HOH A O   1 
HETATM 2261 O  O   . HOH K 8 .   ? -10.513 -44.505 -2.716  1.00 51.23  ? 1804 HOH A O   1 
HETATM 2262 O  O   . HOH K 8 .   ? -43.683 -50.758 -43.542 1.00 46.00  ? 1805 HOH A O   1 
HETATM 2263 O  O   . HOH K 8 .   ? -13.553 -51.800 -18.252 1.00 61.43  ? 1806 HOH A O   1 
HETATM 2264 O  O   . HOH K 8 .   ? -4.516  -27.565 -12.538 1.00 59.86  ? 1807 HOH A O   1 
HETATM 2265 O  O   . HOH K 8 .   ? -14.432 -38.162 -32.446 1.00 29.78  ? 1808 HOH A O   1 
HETATM 2266 O  O   . HOH K 8 .   ? 17.738  -53.493 -14.539 1.00 30.56  ? 1809 HOH A O   1 
HETATM 2267 O  O   . HOH K 8 .   ? -35.508 -39.150 -24.449 1.00 52.29  ? 1810 HOH A O   1 
HETATM 2268 O  O   . HOH K 8 .   ? 5.589   -31.930 -0.292  1.00 45.13  ? 1811 HOH A O   1 
HETATM 2269 O  O   . HOH K 8 .   ? 19.660  -56.160 -15.937 1.00 53.17  ? 1812 HOH A O   1 
HETATM 2270 O  O   . HOH K 8 .   ? -32.708 -50.720 -59.389 1.00 51.09  ? 1813 HOH A O   1 
HETATM 2271 O  O   . HOH K 8 .   ? -17.826 -51.367 -19.626 1.00 35.46  ? 1814 HOH A O   1 
HETATM 2272 O  O   . HOH K 8 .   ? -5.222  -37.691 -24.923 1.00 49.81  ? 1815 HOH A O   1 
HETATM 2273 O  O   . HOH K 8 .   ? 18.492  -38.770 -16.188 1.00 56.94  ? 1816 HOH A O   1 
HETATM 2274 O  O   . HOH K 8 .   ? -35.851 -48.150 -29.489 1.00 52.97  ? 1817 HOH A O   1 
HETATM 2275 O  O   . HOH K 8 .   ? 20.999  -57.326 -17.862 1.00 58.26  ? 1818 HOH A O   1 
HETATM 2276 O  O   . HOH K 8 .   ? -31.060 -39.933 -50.898 1.00 35.43  ? 1819 HOH A O   1 
HETATM 2277 O  O   . HOH K 8 .   ? 25.521  -45.268 -10.321 1.00 66.23  ? 1820 HOH A O   1 
HETATM 2278 O  O   . HOH K 8 .   ? -44.381 -29.593 -51.350 1.00 60.39  ? 1821 HOH A O   1 
HETATM 2279 O  O   . HOH K 8 .   ? 19.651  -48.390 -2.416  1.00 50.14  ? 1822 HOH A O   1 
HETATM 2280 O  O   . HOH K 8 .   ? -30.596 -33.667 -24.593 1.00 38.74  ? 1823 HOH A O   1 
HETATM 2281 O  O   . HOH K 8 .   ? 14.657  -37.982 -7.847  1.00 34.12  ? 1824 HOH A O   1 
HETATM 2282 O  O   . HOH K 8 .   ? -24.319 -32.675 -47.435 1.00 28.42  ? 1825 HOH A O   1 
HETATM 2283 O  O   . HOH K 8 .   ? -30.629 -49.403 -57.966 1.00 40.11  ? 1826 HOH A O   1 
HETATM 2284 O  O   . HOH K 8 .   ? -18.177 -31.632 -15.142 1.00 57.53  ? 1827 HOH A O   1 
HETATM 2285 O  O   . HOH K 8 .   ? -7.393  -49.896 -18.413 1.00 48.80  ? 1828 HOH A O   1 
HETATM 2286 O  O   . HOH K 8 .   ? -29.581 -32.334 -25.336 1.00 47.97  ? 1829 HOH A O   1 
HETATM 2287 O  O   . HOH K 8 .   ? 10.057  -55.214 -5.832  1.00 40.80  ? 1830 HOH A O   1 
HETATM 2288 O  O   . HOH K 8 .   ? -43.523 -40.782 -60.011 1.00 62.87  ? 1831 HOH A O   1 
HETATM 2289 O  O   . HOH K 8 .   ? 2.952   -38.722 -2.097  1.00 46.91  ? 1832 HOH A O   1 
HETATM 2290 O  O   . HOH K 8 .   ? -35.864 -35.008 -38.792 1.00 50.80  ? 1833 HOH A O   1 
HETATM 2291 O  O   . HOH K 8 .   ? -31.239 -42.808 -59.328 1.00 59.04  ? 1834 HOH A O   1 
HETATM 2292 O  O   . HOH K 8 .   ? 9.851   -56.184 -8.798  1.00 45.27  ? 1835 HOH A O   1 
HETATM 2293 O  O   . HOH K 8 .   ? -1.408  -39.262 -23.443 1.00 53.23  ? 1836 HOH A O   1 
HETATM 2294 O  O   . HOH K 8 .   ? -34.914 -55.728 -33.718 1.00 62.69  ? 1837 HOH A O   1 
HETATM 2295 O  O   . HOH K 8 .   ? -1.099  -35.187 -23.002 1.00 58.38  ? 1838 HOH A O   1 
HETATM 2296 O  O   . HOH K 8 .   ? -25.004 -52.004 -23.356 1.00 48.71  ? 1839 HOH A O   1 
HETATM 2297 O  O   . HOH K 8 .   ? -26.755 -29.610 -37.562 1.00 49.70  ? 1840 HOH A O   1 
HETATM 2298 O  O   . HOH K 8 .   ? -12.393 -29.519 -10.852 1.00 58.46  ? 1841 HOH A O   1 
HETATM 2299 O  O   . HOH K 8 .   ? -46.790 -43.894 -57.369 1.00 24.76  ? 1842 HOH A O   1 
HETATM 2300 O  O   . HOH K 8 .   ? -46.594 -28.878 -50.909 1.00 51.45  ? 1843 HOH A O   1 
HETATM 2301 O  O   . HOH K 8 .   ? -13.258 -42.940 -26.415 1.00 45.56  ? 1844 HOH A O   1 
HETATM 2302 O  O   . HOH K 8 .   ? -32.448 -40.924 -57.889 1.00 35.65  ? 1845 HOH A O   1 
HETATM 2303 O  O   . HOH K 8 .   ? 5.548   -50.916 -18.240 1.00 54.45  ? 1846 HOH A O   1 
HETATM 2304 O  O   . HOH K 8 .   ? 10.232  -30.749 -16.726 1.00 60.03  ? 1847 HOH A O   1 
HETATM 2305 O  O   . HOH K 8 .   ? -18.227 -47.576 -30.261 1.00 45.30  ? 1848 HOH A O   1 
HETATM 2306 O  O   . HOH K 8 .   ? -27.093 -27.859 -30.252 1.00 58.22  ? 1849 HOH A O   1 
HETATM 2307 O  O   . HOH K 8 .   ? -40.637 -34.664 -36.291 1.00 54.67  ? 1850 HOH A O   1 
HETATM 2308 O  O   . HOH K 8 .   ? -45.675 -50.319 -57.206 1.00 32.36  ? 1851 HOH A O   1 
HETATM 2309 O  O   . HOH K 8 .   ? -5.609  -52.114 -15.820 1.00 48.76  ? 1852 HOH A O   1 
HETATM 2310 O  O   . HOH K 8 .   ? -42.494 -32.958 -39.797 1.00 39.44  ? 1853 HOH A O   1 
HETATM 2311 O  O   . HOH K 8 .   ? -41.557 -52.189 -57.991 1.00 49.53  ? 1854 HOH A O   1 
HETATM 2312 O  O   . HOH K 8 .   ? -22.481 -47.969 -43.211 1.00 45.71  ? 1855 HOH A O   1 
HETATM 2313 O  O   . HOH K 8 .   ? 17.566  -40.859 -0.767  1.00 58.64  ? 1856 HOH A O   1 
HETATM 2314 O  O   . HOH K 8 .   ? -30.198 -53.800 -48.012 1.00 37.11  ? 1857 HOH A O   1 
HETATM 2315 O  O   . HOH K 8 .   ? -28.355 -33.501 -20.941 1.00 68.97  ? 1858 HOH A O   1 
HETATM 2316 O  O   . HOH K 8 .   ? -38.076 -36.886 -29.424 1.00 42.62  ? 1859 HOH A O   1 
HETATM 2317 O  O   . HOH K 8 .   ? -22.247 -54.814 -28.602 1.00 52.14  ? 1860 HOH A O   1 
HETATM 2318 O  O   . HOH K 8 .   ? -39.672 -38.791 -30.799 1.00 59.62  ? 1861 HOH A O   1 
HETATM 2319 O  O   . HOH K 8 .   ? 1.182   -31.345 -5.443  1.00 63.59  ? 1862 HOH A O   1 
HETATM 2320 O  O   . HOH K 8 .   ? -41.632 -31.860 -60.906 1.00 66.32  ? 1863 HOH A O   1 
HETATM 2321 O  O   . HOH K 8 .   ? -25.076 -56.232 -34.582 1.00 64.45  ? 1864 HOH A O   1 
HETATM 2322 O  O   . HOH K 8 .   ? -24.226 -49.998 -43.596 1.00 53.01  ? 1865 HOH A O   1 
HETATM 2323 O  O   . HOH K 8 .   ? 2.886   -34.246 0.545   1.00 61.54  ? 1866 HOH A O   1 
HETATM 2324 O  O   . HOH K 8 .   ? -17.767 -43.544 -39.875 1.00 49.55  ? 1867 HOH A O   1 
HETATM 2325 O  O   . HOH K 8 .   ? 13.271  -49.959 -18.035 1.00 48.64  ? 1868 HOH A O   1 
HETATM 2326 O  O   . HOH K 8 .   ? -33.520 -57.190 -38.117 1.00 49.90  ? 1869 HOH A O   1 
HETATM 2327 O  O   . HOH K 8 .   ? -33.099 -29.982 -31.340 1.00 65.28  ? 1870 HOH A O   1 
HETATM 2328 O  O   . HOH K 8 .   ? -25.549 -42.542 -21.771 1.00 53.02  ? 1871 HOH A O   1 
HETATM 2329 O  O   . HOH K 8 .   ? -27.209 -55.073 -41.352 1.00 58.20  ? 1872 HOH A O   1 
HETATM 2330 O  O   . HOH K 8 .   ? -45.113 -41.446 -59.354 1.00 53.46  ? 1873 HOH A O   1 
HETATM 2331 O  O   . HOH K 8 .   ? -1.731  -37.732 -2.521  1.00 47.10  ? 1874 HOH A O   1 
HETATM 2332 O  O   . HOH K 8 .   ? -16.317 -49.596 -31.291 1.00 73.62  ? 1875 HOH A O   1 
HETATM 2333 O  O   . HOH K 8 .   ? 4.977   -28.926 -7.183  1.00 61.07  ? 1876 HOH A O   1 
HETATM 2334 O  O   . HOH K 8 .   ? -8.155  -49.196 -25.860 1.00 59.58  ? 1877 HOH A O   1 
HETATM 2335 O  O   . HOH K 8 .   ? -15.717 -36.010 -34.824 0.50 27.61  ? 1878 HOH A O   1 
HETATM 2336 O  O   . HOH K 8 .   ? -7.230  -30.670 -8.745  1.00 53.41  ? 1879 HOH A O   1 
HETATM 2337 O  O   . HOH K 8 .   ? -47.375 -39.835 -60.008 1.00 64.86  ? 1880 HOH A O   1 
HETATM 2338 O  O   . HOH K 8 .   ? 3.670   -32.099 -1.152  1.00 60.57  ? 1881 HOH A O   1 
HETATM 2339 O  O   . HOH K 8 .   ? -9.990  -29.242 -9.591  1.00 59.97  ? 1882 HOH A O   1 
HETATM 2340 O  O   . HOH K 8 .   ? -6.434  -33.193 -25.791 1.00 53.66  ? 1883 HOH A O   1 
HETATM 2341 O  O   . HOH K 8 .   ? -20.986 -30.949 -33.373 1.00 43.58  ? 1884 HOH A O   1 
HETATM 2342 O  O   . HOH K 8 .   ? -10.283 -46.098 -24.370 1.00 41.52  ? 1885 HOH A O   1 
HETATM 2343 O  O   . HOH K 8 .   ? -9.812  -26.825 -12.155 1.00 52.34  ? 1886 HOH A O   1 
HETATM 2344 O  O   . HOH K 8 .   ? -48.703 -30.762 -50.412 1.00 36.77  ? 1887 HOH A O   1 
HETATM 2345 O  O   . HOH K 8 .   ? 10.875  -30.128 -13.576 1.00 50.45  ? 1888 HOH A O   1 
HETATM 2346 O  O   . HOH K 8 .   ? -26.090 -31.764 -49.670 1.00 46.11  ? 1889 HOH A O   1 
HETATM 2347 O  O   . HOH K 8 .   ? -24.310 -52.131 -36.540 1.00 56.23  ? 1890 HOH A O   1 
HETATM 2348 O  O   . HOH K 8 .   ? -7.499  -44.789 -28.438 1.00 53.93  ? 1891 HOH A O   1 
HETATM 2349 O  O   . HOH K 8 .   ? -37.934 -38.073 -24.565 1.00 50.15  ? 1892 HOH A O   1 
HETATM 2350 O  O   . HOH K 8 .   ? -28.565 -49.256 -54.480 1.00 36.75  ? 1893 HOH A O   1 
HETATM 2351 O  O   . HOH K 8 .   ? -48.380 -46.621 -57.563 1.00 36.98  ? 1894 HOH A O   1 
HETATM 2352 O  O   . HOH K 8 .   ? -20.514 -29.978 -18.502 1.00 59.30  ? 1895 HOH A O   1 
HETATM 2353 O  O   . HOH K 8 .   ? -30.605 -34.916 -23.506 1.00 45.93  ? 1896 HOH A O   1 
HETATM 2354 O  O   . HOH K 8 .   ? -11.082 -53.563 -19.774 1.00 46.99  ? 1897 HOH A O   1 
HETATM 2355 O  O   . HOH K 8 .   ? -25.595 -39.496 -17.572 1.00 54.84  ? 1898 HOH A O   1 
HETATM 2356 O  O   . HOH K 8 .   ? -22.880 -40.412 -14.630 1.00 64.53  ? 1899 HOH A O   1 
HETATM 2357 O  O   . HOH K 8 .   ? -27.045 -50.794 -49.880 1.00 64.20  ? 1900 HOH A O   1 
HETATM 2358 O  O   . HOH K 8 .   ? -22.720 -33.145 -33.358 1.00 37.23  ? 1901 HOH A O   1 
HETATM 2359 O  O   . HOH K 8 .   ? -18.886 -45.963 -41.087 1.00 48.06  ? 1902 HOH A O   1 
HETATM 2360 O  O   . HOH K 8 .   ? -2.281  -45.967 -26.046 1.00 48.61  ? 1903 HOH A O   1 
HETATM 2361 O  O   . HOH K 8 .   ? -46.675 -48.380 -58.820 1.00 47.82  ? 1904 HOH A O   1 
HETATM 2362 O  O   . HOH K 8 .   ? 6.518   -53.172 -14.325 1.00 45.73  ? 1905 HOH A O   1 
HETATM 2363 O  O   . HOH K 8 .   ? -29.958 -30.939 -24.022 1.00 62.90  ? 1906 HOH A O   1 
HETATM 2364 O  O   . HOH K 8 .   ? -40.309 -43.048 -29.469 1.00 55.32  ? 1907 HOH A O   1 
HETATM 2365 O  O   . HOH K 8 .   ? 0.987   -40.316 -24.854 1.00 60.05  ? 1908 HOH A O   1 
HETATM 2366 O  O   . HOH K 8 .   ? 14.159  -31.486 -16.416 1.00 61.03  ? 1909 HOH A O   1 
HETATM 2367 O  O   . HOH K 8 .   ? 4.665   -44.510 -23.787 1.00 62.91  ? 1910 HOH A O   1 
HETATM 2368 O  O   . HOH K 8 .   ? -51.766 -27.808 -52.904 1.00 51.33  ? 1911 HOH A O   1 
HETATM 2369 O  O   . HOH K 8 .   ? 2.716   -41.504 -2.761  1.00 45.90  ? 1912 HOH A O   1 
HETATM 2370 O  O   . HOH K 8 .   ? -34.223 -34.754 -60.997 1.00 66.96  ? 1913 HOH A O   1 
HETATM 2371 O  O   . HOH K 8 .   ? 9.582   -45.284 -22.997 1.00 64.95  ? 1914 HOH A O   1 
HETATM 2372 O  O   . HOH K 8 .   ? 7.929   -46.597 -22.351 1.00 58.15  ? 1915 HOH A O   1 
HETATM 2373 O  O   . HOH K 8 .   ? -16.340 -59.008 -25.557 1.00 62.92  ? 1916 HOH A O   1 
HETATM 2374 O  O   . HOH K 8 .   ? 21.599  -36.805 -8.271  1.00 60.89  ? 1917 HOH A O   1 
HETATM 2375 O  O   . HOH K 8 .   ? -49.349 -43.143 -58.743 1.00 57.21  ? 1918 HOH A O   1 
HETATM 2376 O  O   . HOH K 8 .   ? -32.632 -59.783 -34.828 1.00 63.75  ? 1919 HOH A O   1 
HETATM 2377 O  O   . HOH K 8 .   ? 8.754   -26.843 -9.338  1.00 60.47  ? 1920 HOH A O   1 
HETATM 2378 O  O   . HOH K 8 .   ? -45.791 -52.716 -58.607 1.00 39.91  ? 1921 HOH A O   1 
HETATM 2379 O  O   . HOH K 8 .   ? -39.219 -37.271 -27.099 1.00 45.30  ? 1922 HOH A O   1 
HETATM 2380 O  O   . HOH K 8 .   ? -1.088  -37.621 -27.479 1.00 67.70  ? 1923 HOH A O   1 
HETATM 2381 O  O   . HOH K 8 .   ? -49.452 -49.936 -58.892 1.00 61.38  ? 1924 HOH A O   1 
HETATM 2382 O  O   . HOH K 8 .   ? 14.126  -25.844 -8.133  1.00 74.01  ? 1925 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   . CYS A 1   ? 0.3242 0.3801 0.3039 0.0069  -0.0030 -0.0234 22  CYS A N   
2    C CA  . CYS A 1   ? 0.3462 0.3955 0.3361 0.0139  -0.0047 -0.0423 22  CYS A CA  
3    C C   . CYS A 1   ? 0.3265 0.3510 0.3334 0.0144  -0.0021 -0.0454 22  CYS A C   
4    O O   . CYS A 1   ? 0.3220 0.3400 0.3405 0.0171  -0.0041 -0.0574 22  CYS A O   
5    C CB  . CYS A 1   ? 0.3373 0.3855 0.3253 0.0147  -0.0138 -0.0427 22  CYS A CB  
6    S SG  . CYS A 1   ? 0.4171 0.4990 0.3878 0.0167  -0.0183 -0.0491 22  CYS A SG  
7    N N   . ILE A 2   ? 0.2777 0.2901 0.2869 0.0107  0.0007  -0.0336 23  ILE A N   
8    C CA  . ILE A 2   ? 0.2639 0.2597 0.2869 0.0103  0.0025  -0.0353 23  ILE A CA  
9    C C   . ILE A 2   ? 0.2903 0.2838 0.3216 0.0117  0.0058  -0.0436 23  ILE A C   
10   O O   . ILE A 2   ? 0.3215 0.3051 0.3648 0.0097  0.0049  -0.0449 23  ILE A O   
11   C CB  . ILE A 2   ? 0.2925 0.2786 0.3164 0.0077  0.0036  -0.0245 23  ILE A CB  
12   C CG1 . ILE A 2   ? 0.3069 0.2981 0.3238 0.0050  0.0076  -0.0171 23  ILE A CG1 
13   C CG2 . ILE A 2   ? 0.3045 0.2864 0.3277 0.0083  -0.0046 -0.0191 23  ILE A CG2 
14   C CD1 . ILE A 2   ? 0.3091 0.2889 0.3301 0.0025  0.0076  -0.0093 23  ILE A CD1 
15   N N   . LYS A 3   ? 0.2949 0.3002 0.3216 0.0148  0.0081  -0.0488 24  LYS A N   
16   C CA  . LYS A 3   ? 0.2642 0.2655 0.3031 0.0189  0.0071  -0.0598 24  LYS A CA  
17   C C   . LYS A 3   ? 0.3280 0.3226 0.3786 0.0214  -0.0013 -0.0728 24  LYS A C   
18   O O   . LYS A 3   ? 0.3224 0.3047 0.3885 0.0228  -0.0070 -0.0792 24  LYS A O   
19   C CB  . LYS A 3   ? 0.2891 0.3114 0.3233 0.0246  0.0100  -0.0681 24  LYS A CB  
20   C CG  . LYS A 3   ? 0.2784 0.3258 0.3045 0.0304  0.0074  -0.0821 24  LYS A CG  
21   C CD  . LYS A 3   ? 0.3311 0.4131 0.3505 0.0356  0.0123  -0.0905 24  LYS A CD  
22   C CE  . LYS A 3   ? 0.3523 0.4640 0.3647 0.0429  0.0086  -0.1090 24  LYS A CE  
23   N NZ  . LYS A 3   ? 0.3830 0.5442 0.3840 0.0461  0.0154  -0.1150 24  LYS A NZ  
24   N N   . CYS A 4   ? 0.2982 0.2999 0.3430 0.0215  -0.0045 -0.0760 25  CYS A N   
25   C CA  . CYS A 4   ? 0.3273 0.3243 0.3841 0.0233  -0.0141 -0.0892 25  CYS A CA  
26   C C   . CYS A 4   ? 0.3813 0.3621 0.4521 0.0149  -0.0170 -0.0803 25  CYS A C   
27   O O   . CYS A 4   ? 0.3669 0.3414 0.4521 0.0128  -0.0262 -0.0875 25  CYS A O   
28   C CB  . CYS A 4   ? 0.3752 0.3895 0.4204 0.0262  -0.0171 -0.0957 25  CYS A CB  
29   S SG  . CYS A 4   ? 0.3517 0.3999 0.3750 0.0327  -0.0122 -0.1013 25  CYS A SG  
30   N N   . ASP A 5   ? 0.3160 0.2939 0.3839 0.0094  -0.0100 -0.0654 26  ASP A N   
31   C CA  . ASP A 5   ? 0.2720 0.2476 0.3506 0.0015  -0.0110 -0.0578 26  ASP A CA  
32   C C   . ASP A 5   ? 0.3158 0.2818 0.4065 -0.0057 -0.0113 -0.0492 26  ASP A C   
33   O O   . ASP A 5   ? 0.2939 0.2574 0.3787 -0.0050 -0.0058 -0.0429 26  ASP A O   
34   C CB  . ASP A 5   ? 0.3104 0.2942 0.3797 0.0018  -0.0052 -0.0503 26  ASP A CB  
35   C CG  . ASP A 5   ? 0.3675 0.3602 0.4481 -0.0036 -0.0059 -0.0475 26  ASP A CG  
36   O OD1 . ASP A 5   ? 0.3359 0.3303 0.4290 -0.0122 -0.0061 -0.0421 26  ASP A OD1 
37   O OD2 . ASP A 5   ? 0.3888 0.3897 0.4661 0.0004  -0.0069 -0.0495 26  ASP A OD2 
38   N N   . GLN A 6   ? 0.3273 0.2889 0.4352 -0.0141 -0.0192 -0.0469 27  GLN A N   
39   C CA  . GLN A 6   ? 0.3428 0.2965 0.4626 -0.0239 -0.0222 -0.0339 27  GLN A CA  
40   C C   . GLN A 6   ? 0.2940 0.2605 0.4048 -0.0282 -0.0114 -0.0206 27  GLN A C   
41   O O   . GLN A 6   ? 0.3104 0.2714 0.4225 -0.0320 -0.0114 -0.0110 27  GLN A O   
42   C CB  . GLN A 6   ? 0.3261 0.2789 0.4666 -0.0372 -0.0329 -0.0273 27  GLN A CB  
43   C CG  . GLN A 6   ? 0.4262 0.3653 0.5806 -0.0479 -0.0415 -0.0122 27  GLN A CG  
44   C CD  . GLN A 6   ? 0.4832 0.4240 0.6586 -0.0659 -0.0526 0.0016  27  GLN A CD  
45   O OE1 . GLN A 6   ? 0.3385 0.2772 0.5266 -0.0683 -0.0616 -0.0062 27  GLN A OE1 
46   N NE2 . GLN A 6   ? 0.5568 0.5027 0.7375 -0.0806 -0.0539 0.0243  27  GLN A NE2 
47   N N   . PHE A 7   ? 0.2494 0.2342 0.3529 -0.0268 -0.0041 -0.0217 28  PHE A N   
48   C CA  . PHE A 7   ? 0.2532 0.2538 0.3504 -0.0290 0.0042  -0.0141 28  PHE A CA  
49   C C   . PHE A 7   ? 0.2933 0.2834 0.3781 -0.0214 0.0085  -0.0147 28  PHE A C   
50   O O   . PHE A 7   ? 0.2777 0.2734 0.3598 -0.0245 0.0121  -0.0073 28  PHE A O   
51   C CB  . PHE A 7   ? 0.2411 0.2626 0.3359 -0.0245 0.0083  -0.0208 28  PHE A CB  
52   C CG  . PHE A 7   ? 0.2388 0.2843 0.3472 -0.0337 0.0070  -0.0184 28  PHE A CG  
53   C CD1 . PHE A 7   ? 0.3528 0.4078 0.4723 -0.0493 0.0049  -0.0043 28  PHE A CD1 
54   C CD2 . PHE A 7   ? 0.2419 0.3030 0.3534 -0.0279 0.0065  -0.0285 28  PHE A CD2 
55   C CE1 . PHE A 7   ? 0.3078 0.3906 0.4415 -0.0609 0.0036  0.0005  28  PHE A CE1 
56   C CE2 . PHE A 7   ? 0.2565 0.3464 0.3829 -0.0370 0.0058  -0.0269 28  PHE A CE2 
57   C CZ  . PHE A 7   ? 0.2624 0.3652 0.3994 -0.0542 0.0053  -0.0118 28  PHE A CZ  
58   N N   . VAL A 8   ? 0.3080 0.2872 0.3852 -0.0125 0.0079  -0.0230 29  VAL A N   
59   C CA  . VAL A 8   ? 0.2873 0.2603 0.3544 -0.0070 0.0114  -0.0227 29  VAL A CA  
60   C C   . VAL A 8   ? 0.3187 0.2816 0.3909 -0.0084 0.0093  -0.0197 29  VAL A C   
61   O O   . VAL A 8   ? 0.3154 0.2779 0.3848 -0.0092 0.0122  -0.0136 29  VAL A O   
62   C CB  . VAL A 8   ? 0.3148 0.2867 0.3726 -0.0001 0.0110  -0.0291 29  VAL A CB  
63   C CG1 . VAL A 8   ? 0.3567 0.3266 0.4065 0.0028  0.0143  -0.0268 29  VAL A CG1 
64   C CG2 . VAL A 8   ? 0.3210 0.2992 0.3751 0.0018  0.0102  -0.0296 29  VAL A CG2 
65   N N   . THR A 9   ? 0.2898 0.2441 0.3720 -0.0081 0.0018  -0.0249 30  THR A N   
66   C CA  . THR A 9   ? 0.3544 0.2969 0.4453 -0.0071 -0.0038 -0.0242 30  THR A CA  
67   C C   . THR A 9   ? 0.3234 0.2630 0.4225 -0.0183 -0.0071 -0.0079 30  THR A C   
68   O O   . THR A 9   ? 0.3341 0.2681 0.4347 -0.0180 -0.0086 -0.0022 30  THR A O   
69   C CB  . THR A 9   ? 0.4432 0.3760 0.5464 -0.0013 -0.0148 -0.0382 30  THR A CB  
70   O OG1 . THR A 9   ? 0.4271 0.3556 0.5414 -0.0085 -0.0224 -0.0368 30  THR A OG1 
71   C CG2 . THR A 9   ? 0.5298 0.4754 0.6211 0.0092  -0.0100 -0.0531 30  THR A CG2 
72   N N   . ASP A 10  ? 0.2812 0.2300 0.3846 -0.0288 -0.0076 0.0008  31  ASP A N   
73   C CA  . ASP A 10  ? 0.2962 0.2536 0.4036 -0.0417 -0.0089 0.0191  31  ASP A CA  
74   C C   . ASP A 10  ? 0.3329 0.3055 0.4255 -0.0394 0.0016  0.0223  31  ASP A C   
75   O O   . ASP A 10  ? 0.3303 0.3033 0.4225 -0.0440 -0.0003 0.0336  31  ASP A O   
76   C CB  . ASP A 10  ? 0.2983 0.2749 0.4120 -0.0539 -0.0088 0.0268  31  ASP A CB  
77   C CG  . ASP A 10  ? 0.4567 0.4186 0.5900 -0.0620 -0.0230 0.0296  31  ASP A CG  
78   O OD1 . ASP A 10  ? 0.4049 0.3400 0.5498 -0.0589 -0.0357 0.0266  31  ASP A OD1 
79   O OD2 . ASP A 10  ? 0.4555 0.4347 0.5950 -0.0711 -0.0227 0.0333  31  ASP A OD2 
80   N N   . ALA A 11  ? 0.2865 0.2708 0.3685 -0.0322 0.0102  0.0123  32  ALA A N   
81   C CA  . ALA A 11  ? 0.2944 0.2901 0.3651 -0.0280 0.0172  0.0109  32  ALA A CA  
82   C C   . ALA A 11  ? 0.3419 0.3230 0.4087 -0.0226 0.0167  0.0108  32  ALA A C   
83   O O   . ALA A 11  ? 0.2661 0.2551 0.3279 -0.0237 0.0188  0.0152  32  ALA A O   
84   C CB  . ALA A 11  ? 0.3120 0.3146 0.3766 -0.0194 0.0212  -0.0015 32  ALA A CB  
85   N N   . LEU A 12  ? 0.2712 0.2364 0.3401 -0.0163 0.0142  0.0039  33  LEU A N   
86   C CA  . LEU A 12  ? 0.2924 0.2506 0.3598 -0.0111 0.0142  0.0028  33  LEU A CA  
87   C C   . LEU A 12  ? 0.2920 0.2427 0.3686 -0.0149 0.0072  0.0117  33  LEU A C   
88   O O   . LEU A 12  ? 0.3040 0.2548 0.3789 -0.0127 0.0076  0.0140  33  LEU A O   
89   C CB  . LEU A 12  ? 0.3108 0.2646 0.3785 -0.0032 0.0140  -0.0080 33  LEU A CB  
90   C CG  . LEU A 12  ? 0.3493 0.3104 0.4063 -0.0005 0.0191  -0.0121 33  LEU A CG  
91   C CD1 . LEU A 12  ? 0.4051 0.3707 0.4605 0.0052  0.0189  -0.0211 33  LEU A CD1 
92   C CD2 . LEU A 12  ? 0.3544 0.3189 0.4048 -0.0011 0.0224  -0.0077 33  LEU A CD2 
93   N N   . LYS A 13  ? 0.3265 0.2697 0.4147 -0.0212 -0.0014 0.0174  34  LYS A N   
94   C CA  . LYS A 13  ? 0.3424 0.2754 0.4417 -0.0270 -0.0124 0.0298  34  LYS A CA  
95   C C   . LYS A 13  ? 0.3148 0.2647 0.4054 -0.0365 -0.0089 0.0456  34  LYS A C   
96   O O   . LYS A 13  ? 0.3446 0.2913 0.4363 -0.0370 -0.0134 0.0532  34  LYS A O   
97   C CB  . LYS A 13  ? 0.4127 0.3325 0.5288 -0.0344 -0.0255 0.0352  34  LYS A CB  
98   C CG  . LYS A 13  ? 0.5857 0.4877 0.7144 -0.0227 -0.0339 0.0170  34  LYS A CG  
99   N N   . THR A 14  ? 0.2874 0.2591 0.3701 -0.0433 -0.0014 0.0487  35  THR A N   
100  C CA  . THR A 14  ? 0.3302 0.3281 0.4031 -0.0506 0.0032  0.0589  35  THR A CA  
101  C C   . THR A 14  ? 0.2701 0.2720 0.3317 -0.0410 0.0094  0.0495  35  THR A C   
102  O O   . THR A 14  ? 0.3413 0.3536 0.3980 -0.0442 0.0081  0.0575  35  THR A O   
103  C CB  . THR A 14  ? 0.3460 0.3729 0.4148 -0.0560 0.0104  0.0571  35  THR A CB  
104  O OG1 . THR A 14  ? 0.3605 0.3847 0.4421 -0.0680 0.0030  0.0690  35  THR A OG1 
105  C CG2 . THR A 14  ? 0.3673 0.4297 0.4261 -0.0624 0.0149  0.0646  35  THR A CG2 
106  N N   . PHE A 15  ? 0.2514 0.2448 0.3102 -0.0302 0.0144  0.0337  36  PHE A N   
107  C CA  . PHE A 15  ? 0.3141 0.3074 0.3660 -0.0226 0.0178  0.0257  36  PHE A CA  
108  C C   . PHE A 15  ? 0.3263 0.3094 0.3821 -0.0218 0.0127  0.0319  36  PHE A C   
109  O O   . PHE A 15  ? 0.3078 0.2999 0.3586 -0.0223 0.0125  0.0345  36  PHE A O   
110  C CB  . PHE A 15  ? 0.3000 0.2828 0.3515 -0.0147 0.0206  0.0138  36  PHE A CB  
111  C CG  . PHE A 15  ? 0.2865 0.2680 0.3339 -0.0099 0.0217  0.0084  36  PHE A CG  
112  C CD1 . PHE A 15  ? 0.2899 0.2810 0.3331 -0.0079 0.0219  0.0020  36  PHE A CD1 
113  C CD2 . PHE A 15  ? 0.3659 0.3388 0.4164 -0.0072 0.0211  0.0085  36  PHE A CD2 
114  C CE1 . PHE A 15  ? 0.3826 0.3681 0.4258 -0.0048 0.0192  -0.0022 36  PHE A CE1 
115  C CE2 . PHE A 15  ? 0.3057 0.2789 0.3548 -0.0057 0.0210  0.0063  36  PHE A CE2 
116  C CZ  . PHE A 15  ? 0.2952 0.2716 0.3412 -0.0053 0.0191  0.0021  36  PHE A CZ  
117  N N   . GLU A 16  ? 0.3089 0.2747 0.3751 -0.0192 0.0074  0.0317  37  GLU A N   
118  C CA  . GLU A 16  ? 0.3321 0.2890 0.4062 -0.0160 0.0005  0.0346  37  GLU A CA  
119  C C   . GLU A 16  ? 0.3463 0.3049 0.4229 -0.0245 -0.0081 0.0516  37  GLU A C   
120  O O   . GLU A 16  ? 0.3684 0.3303 0.4436 -0.0234 -0.0107 0.0556  37  GLU A O   
121  C CB  . GLU A 16  ? 0.3639 0.3053 0.4519 -0.0088 -0.0057 0.0262  37  GLU A CB  
122  C CG  . GLU A 16  ? 0.4171 0.3524 0.5169 -0.0023 -0.0140 0.0250  37  GLU A CG  
123  C CD  . GLU A 16  ? 0.4631 0.3907 0.5781 0.0088  -0.0200 0.0095  37  GLU A CD  
124  O OE1 . GLU A 16  ? 0.4588 0.3865 0.5724 0.0107  -0.0168 0.0002  37  GLU A OE1 
125  O OE2 . GLU A 16  ? 0.4708 0.3955 0.5994 0.0169  -0.0284 0.0045  37  GLU A OE2 
126  N N   A ASN A 17  ? 0.3038 0.2618 0.3844 -0.0344 -0.0137 0.0636  38  ASN A N   
127  N N   B ASN A 17  ? 0.3150 0.2725 0.3959 -0.0344 -0.0139 0.0636  38  ASN A N   
128  C CA  A ASN A 17  ? 0.3746 0.3314 0.4608 -0.0448 -0.0260 0.0845  38  ASN A CA  
129  C CA  B ASN A 17  ? 0.3734 0.3296 0.4603 -0.0453 -0.0265 0.0850  38  ASN A CA  
130  C C   A ASN A 17  ? 0.3915 0.3791 0.4617 -0.0545 -0.0205 0.0963  38  ASN A C   
131  C C   B ASN A 17  ? 0.3859 0.3735 0.4574 -0.0568 -0.0214 0.0987  38  ASN A C   
132  O O   A ASN A 17  ? 0.3228 0.3155 0.3922 -0.0614 -0.0290 0.1128  38  ASN A O   
133  O O   B ASN A 17  ? 0.3445 0.3379 0.4169 -0.0676 -0.0313 0.1196  38  ASN A O   
134  C CB  A ASN A 17  ? 0.3906 0.3331 0.4918 -0.0546 -0.0383 0.0964  38  ASN A CB  
135  C CB  B ASN A 17  ? 0.4004 0.3368 0.5054 -0.0529 -0.0410 0.0952  38  ASN A CB  
136  C CG  A ASN A 17  ? 0.4422 0.3543 0.5628 -0.0431 -0.0490 0.0826  38  ASN A CG  
137  C CG  B ASN A 17  ? 0.4285 0.3811 0.5301 -0.0658 -0.0364 0.1029  38  ASN A CG  
138  O OD1 A ASN A 17  ? 0.4832 0.3882 0.6074 -0.0297 -0.0492 0.0691  38  ASN A OD1 
139  O OD1 B ASN A 17  ? 0.3591 0.3423 0.4452 -0.0704 -0.0237 0.1036  38  ASN A OD1 
140  N ND2 A ASN A 17  ? 0.4513 0.3492 0.5858 -0.0480 -0.0584 0.0841  38  ASN A ND2 
141  N ND2 B ASN A 17  ? 0.4241 0.3570 0.5437 -0.0714 -0.0491 0.1077  38  ASN A ND2 
142  N N   . THR A 18  ? 0.3418 0.3522 0.4000 -0.0541 -0.0077 0.0866  39  THR A N   
143  C CA  . THR A 18  ? 0.3465 0.3953 0.3903 -0.0619 -0.0024 0.0931  39  THR A CA  
144  C C   . THR A 18  ? 0.3574 0.4184 0.3903 -0.0506 0.0058  0.0739  39  THR A C   
145  O O   . THR A 18  ? 0.3837 0.4632 0.4081 -0.0518 0.0047  0.0769  39  THR A O   
146  C CB  . THR A 18  ? 0.3749 0.4498 0.4170 -0.0710 0.0031  0.0960  39  THR A CB  
147  O OG1 . THR A 18  ? 0.3878 0.4530 0.4418 -0.0854 -0.0074 0.1180  39  THR A OG1 
148  C CG2 . THR A 18  ? 0.4283 0.5541 0.4558 -0.0766 0.0101  0.0971  39  THR A CG2 
149  N N   . TYR A 19  ? 0.2951 0.3445 0.3296 -0.0400 0.0119  0.0549  40  TYR A N   
150  C CA  . TYR A 19  ? 0.2874 0.3503 0.3142 -0.0313 0.0163  0.0376  40  TYR A CA  
151  C C   . TYR A 19  ? 0.3154 0.3607 0.3440 -0.0242 0.0134  0.0318  40  TYR A C   
152  O O   . TYR A 19  ? 0.3004 0.3582 0.3239 -0.0201 0.0128  0.0222  40  TYR A O   
153  C CB  . TYR A 19  ? 0.2954 0.3574 0.3241 -0.0248 0.0211  0.0219  40  TYR A CB  
154  C CG  . TYR A 19  ? 0.3030 0.3937 0.3303 -0.0310 0.0248  0.0240  40  TYR A CG  
155  C CD1 . TYR A 19  ? 0.4139 0.5454 0.4334 -0.0365 0.0265  0.0270  40  TYR A CD1 
156  C CD2 . TYR A 19  ? 0.3751 0.4569 0.4092 -0.0318 0.0264  0.0230  40  TYR A CD2 
157  C CE1 . TYR A 19  ? 0.3962 0.5627 0.4156 -0.0437 0.0308  0.0296  40  TYR A CE1 
158  C CE2 . TYR A 19  ? 0.3716 0.4836 0.4066 -0.0383 0.0297  0.0250  40  TYR A CE2 
159  C CZ  . TYR A 19  ? 0.4204 0.5757 0.4486 -0.0447 0.0322  0.0289  40  TYR A CZ  
160  O OH  . TYR A 19  ? 0.4106 0.6048 0.4409 -0.0527 0.0364  0.0317  40  TYR A OH  
161  N N   . LEU A 20  ? 0.3015 0.3212 0.3390 -0.0221 0.0109  0.0351  41  LEU A N   
162  C CA  . LEU A 20  ? 0.2855 0.2956 0.3264 -0.0165 0.0089  0.0299  41  LEU A CA  
163  C C   . LEU A 20  ? 0.3138 0.3366 0.3508 -0.0188 0.0039  0.0359  41  LEU A C   
164  O O   . LEU A 20  ? 0.2996 0.3245 0.3365 -0.0151 0.0025  0.0282  41  LEU A O   
165  C CB  . LEU A 20  ? 0.2919 0.2827 0.3443 -0.0132 0.0072  0.0311  41  LEU A CB  
166  C CG  . LEU A 20  ? 0.3519 0.3339 0.4069 -0.0093 0.0121  0.0221  41  LEU A CG  
167  C CD1 . LEU A 20  ? 0.2775 0.2512 0.3440 -0.0046 0.0100  0.0207  41  LEU A CD1 
168  C CD2 . LEU A 20  ? 0.3199 0.3048 0.3713 -0.0078 0.0144  0.0143  41  LEU A CD2 
169  N N   . ASN A 21  ? 0.2709 0.3025 0.3054 -0.0260 -0.0005 0.0511  42  ASN A N   
170  C CA  . ASN A 21  ? 0.2716 0.3200 0.2998 -0.0299 -0.0066 0.0604  42  ASN A CA  
171  C C   . ASN A 21  ? 0.3759 0.4496 0.3927 -0.0270 -0.0036 0.0467  42  ASN A C   
172  O O   . ASN A 21  ? 0.3277 0.4109 0.3413 -0.0258 -0.0086 0.0460  42  ASN A O   
173  C CB  . ASN A 21  ? 0.3644 0.4265 0.3884 -0.0422 -0.0116 0.0821  42  ASN A CB  
174  C CG  . ASN A 21  ? 0.6218 0.6565 0.6609 -0.0450 -0.0229 0.0979  42  ASN A CG  
175  O OD1 . ASN A 21  ? 0.7072 0.7220 0.7573 -0.0366 -0.0276 0.0923  42  ASN A OD1 
176  N ND2 . ASN A 21  ? 0.6850 0.7201 0.7271 -0.0569 -0.0289 0.1169  42  ASN A ND2 
177  N N   . ASP A 22  ? 0.3137 0.3995 0.3262 -0.0248 0.0028  0.0342  43  ASP A N   
178  C CA  . ASP A 22  ? 0.3509 0.4639 0.3554 -0.0196 0.0032  0.0165  43  ASP A CA  
179  C C   . ASP A 22  ? 0.3309 0.4255 0.3432 -0.0103 -0.0005 -0.0016 43  ASP A C   
180  O O   . ASP A 22  ? 0.3307 0.4431 0.3400 -0.0047 -0.0047 -0.0184 43  ASP A O   
181  C CB  . ASP A 22  ? 0.2677 0.4033 0.2686 -0.0185 0.0091  0.0065  43  ASP A CB  
182  C CG  . ASP A 22  ? 0.4070 0.5685 0.4013 -0.0306 0.0124  0.0254  43  ASP A CG  
183  O OD1 . ASP A 22  ? 0.4201 0.5968 0.4075 -0.0393 0.0086  0.0428  43  ASP A OD1 
184  O OD2 . ASP A 22  ? 0.4055 0.5720 0.4026 -0.0326 0.0173  0.0248  43  ASP A OD2 
185  N N   . HIS A 23  ? 0.2823 0.3449 0.3053 -0.0094 -0.0003 0.0017  44  HIS A N   
186  C CA  . HIS A 23  ? 0.3001 0.3454 0.3324 -0.0045 -0.0043 -0.0107 44  HIS A CA  
187  C C   . HIS A 23  ? 0.2675 0.2975 0.3090 -0.0063 -0.0073 -0.0040 44  HIS A C   
188  O O   . HIS A 23  ? 0.3061 0.3280 0.3556 -0.0054 -0.0129 -0.0111 44  HIS A O   
189  C CB  . HIS A 23  ? 0.2621 0.2918 0.2991 -0.0028 -0.0009 -0.0142 44  HIS A CB  
190  C CG  . HIS A 23  ? 0.2974 0.3438 0.3293 0.0008  0.0010  -0.0246 44  HIS A CG  
191  N ND1 . HIS A 23  ? 0.3000 0.3538 0.3352 0.0086  -0.0059 -0.0446 44  HIS A ND1 
192  C CD2 . HIS A 23  ? 0.2676 0.3269 0.2944 -0.0021 0.0076  -0.0192 44  HIS A CD2 
193  C CE1 . HIS A 23  ? 0.3395 0.4139 0.3713 0.0118  -0.0023 -0.0525 44  HIS A CE1 
194  N NE2 . HIS A 23  ? 0.3365 0.4153 0.3627 0.0042  0.0066  -0.0360 44  HIS A NE2 
195  N N   . LEU A 24  ? 0.2937 0.3204 0.3366 -0.0090 -0.0050 0.0095  45  LEU A N   
196  C CA  . LEU A 24  ? 0.2458 0.2628 0.3002 -0.0090 -0.0066 0.0139  45  LEU A CA  
197  C C   . LEU A 24  ? 0.2488 0.2704 0.3050 -0.0094 -0.0107 0.0246  45  LEU A C   
198  O O   . LEU A 24  ? 0.3039 0.3272 0.3547 -0.0116 -0.0115 0.0342  45  LEU A O   
199  C CB  . LEU A 24  ? 0.2672 0.2718 0.3281 -0.0085 -0.0009 0.0154  45  LEU A CB  
200  C CG  . LEU A 24  ? 0.4620 0.4608 0.5295 -0.0100 0.0004  0.0115  45  LEU A CG  
201  C CD1 . LEU A 24  ? 0.3594 0.3565 0.4290 -0.0121 -0.0062 0.0054  45  LEU A CD1 
202  C CD2 . LEU A 24  ? 0.2827 0.2746 0.3490 -0.0097 0.0064  0.0122  45  LEU A CD2 
203  N N   . PRO A 25  ? 0.2843 0.3072 0.3508 -0.0080 -0.0151 0.0247  46  PRO A N   
204  C CA  . PRO A 25  ? 0.2954 0.3197 0.3677 -0.0065 -0.0216 0.0341  46  PRO A CA  
205  C C   . PRO A 25  ? 0.2907 0.3024 0.3724 -0.0031 -0.0204 0.0376  46  PRO A C   
206  O O   . PRO A 25  ? 0.2813 0.2891 0.3682 -0.0011 -0.0136 0.0304  46  PRO A O   
207  C CB  . PRO A 25  ? 0.2883 0.3195 0.3729 -0.0047 -0.0258 0.0298  46  PRO A CB  
208  C CG  . PRO A 25  ? 0.3519 0.3820 0.4401 -0.0071 -0.0204 0.0211  46  PRO A CG  
209  C CD  . PRO A 25  ? 0.2932 0.3167 0.3687 -0.0088 -0.0160 0.0173  46  PRO A CD  
210  N N   A HIS A 26  ? 0.2823 0.2885 0.3667 -0.0031 -0.0288 0.0485  47  HIS A N   
211  N N   B HIS A 26  ? 0.2919 0.2981 0.3768 -0.0029 -0.0289 0.0484  47  HIS A N   
212  C CA  A HIS A 26  ? 0.3351 0.3262 0.4310 0.0007  -0.0319 0.0499  47  HIS A CA  
213  C CA  B HIS A 26  ? 0.3253 0.3164 0.4211 0.0007  -0.0317 0.0498  47  HIS A CA  
214  C C   A HIS A 26  ? 0.2961 0.2879 0.4096 0.0104  -0.0301 0.0365  47  HIS A C   
215  C C   B HIS A 26  ? 0.2977 0.2888 0.4121 0.0107  -0.0311 0.0370  47  HIS A C   
216  O O   A HIS A 26  ? 0.2918 0.2775 0.4106 0.0143  -0.0268 0.0293  47  HIS A O   
217  O O   B HIS A 26  ? 0.2804 0.2640 0.4021 0.0153  -0.0297 0.0303  47  HIS A O   
218  C CB  A HIS A 26  ? 0.3641 0.3462 0.4664 -0.0011 -0.0474 0.0655  47  HIS A CB  
219  C CB  B HIS A 26  ? 0.3654 0.3475 0.4654 -0.0023 -0.0464 0.0663  47  HIS A CB  
220  C CG  A HIS A 26  ? 0.3970 0.3595 0.5174 0.0048  -0.0559 0.0639  47  HIS A CG  
221  C CG  B HIS A 26  ? 0.3290 0.3111 0.4428 0.0032  -0.0594 0.0694  47  HIS A CG  
222  N ND1 A HIS A 26  ? 0.3859 0.3406 0.5289 0.0155  -0.0690 0.0590  47  HIS A ND1 
223  N ND1 B HIS A 26  ? 0.4397 0.4359 0.5449 -0.0006 -0.0634 0.0765  47  HIS A ND1 
224  C CD2 A HIS A 26  ? 0.4767 0.4270 0.5986 0.0034  -0.0543 0.0626  47  HIS A CD2 
225  C CD2 B HIS A 26  ? 0.3549 0.3258 0.4919 0.0135  -0.0712 0.0650  47  HIS A CD2 
226  C CE1 A HIS A 26  ? 0.3797 0.3173 0.5377 0.0212  -0.0764 0.0534  47  HIS A CE1 
227  C CE1 B HIS A 26  ? 0.4317 0.4245 0.5539 0.0063  -0.0767 0.0783  47  HIS A CE1 
228  N NE2 A HIS A 26  ? 0.5160 0.4499 0.6611 0.0132  -0.0675 0.0563  47  HIS A NE2 
229  N NE2 B HIS A 26  ? 0.3857 0.3633 0.5285 0.0155  -0.0820 0.0707  47  HIS A NE2 
230  N N   . ASP A 27  ? 0.2779 0.2821 0.4005 0.0141  -0.0323 0.0322  48  ASP A N   
231  C CA  . ASP A 27  ? 0.2569 0.2716 0.3985 0.0236  -0.0310 0.0192  48  ASP A CA  
232  C C   . ASP A 27  ? 0.2434 0.2720 0.3813 0.0211  -0.0168 0.0104  48  ASP A C   
233  O O   . ASP A 27  ? 0.2640 0.3121 0.4155 0.0270  -0.0136 0.0002  48  ASP A O   
234  C CB  . ASP A 27  ? 0.2674 0.2959 0.4235 0.0284  -0.0387 0.0175  48  ASP A CB  
235  C CG  . ASP A 27  ? 0.3636 0.3811 0.5375 0.0385  -0.0550 0.0180  48  ASP A CG  
236  O OD1 . ASP A 27  ? 0.3442 0.3586 0.5198 0.0376  -0.0665 0.0278  48  ASP A OD1 
237  O OD2 . ASP A 27  ? 0.2995 0.3097 0.4861 0.0476  -0.0584 0.0084  48  ASP A OD2 
238  N N   A ILE A 28  ? 0.2379 0.2595 0.3587 0.0126  -0.0096 0.0146  49  ILE A N   
239  N N   B ILE A 28  ? 0.2380 0.2594 0.3589 0.0128  -0.0097 0.0145  49  ILE A N   
240  C CA  A ILE A 28  ? 0.2300 0.2600 0.3474 0.0095  0.0003  0.0100  49  ILE A CA  
241  C CA  B ILE A 28  ? 0.2447 0.2744 0.3621 0.0096  0.0004  0.0099  49  ILE A CA  
242  C C   A ILE A 28  ? 0.2297 0.2454 0.3374 0.0095  0.0037  0.0094  49  ILE A C   
243  C C   B ILE A 28  ? 0.2389 0.2548 0.3473 0.0100  0.0037  0.0090  49  ILE A C   
244  O O   A ILE A 28  ? 0.2513 0.2724 0.3548 0.0073  0.0107  0.0066  49  ILE A O   
245  O O   B ILE A 28  ? 0.2436 0.2659 0.3488 0.0086  0.0106  0.0054  49  ILE A O   
246  C CB  A ILE A 28  ? 0.3179 0.3529 0.4294 -0.0004 0.0027  0.0141  49  ILE A CB  
247  C CB  B ILE A 28  ? 0.2841 0.3165 0.3939 -0.0002 0.0028  0.0142  49  ILE A CB  
248  C CG1 A ILE A 28  ? 0.3469 0.3975 0.4616 -0.0055 0.0097  0.0134  49  ILE A CG1 
249  C CG1 B ILE A 28  ? 0.2287 0.2714 0.3471 -0.0015 -0.0031 0.0156  49  ILE A CG1 
250  C CG2 A ILE A 28  ? 0.2281 0.2468 0.3243 -0.0048 0.0012  0.0172  49  ILE A CG2 
251  C CG2 B ILE A 28  ? 0.3294 0.3741 0.4404 -0.0055 0.0098  0.0137  49  ILE A CG2 
252  C CD1 A ILE A 28  ? 0.2806 0.3379 0.3986 -0.0165 0.0074  0.0194  49  ILE A CD1 
253  C CD1 B ILE A 28  ? 0.2913 0.3376 0.4092 -0.0112 -0.0039 0.0179  49  ILE A CD1 
254  N N   . HIS A 29  ? 0.2530 0.2524 0.3579 0.0107  -0.0022 0.0139  50  HIS A N   
255  C CA  . HIS A 29  ? 0.2438 0.2315 0.3412 0.0091  0.0002  0.0142  50  HIS A CA  
256  C C   . HIS A 29  ? 0.2893 0.2801 0.3945 0.0159  0.0025  0.0035  50  HIS A C   
257  O O   . HIS A 29  ? 0.2866 0.2769 0.3836 0.0136  0.0087  0.0011  50  HIS A O   
258  C CB  . HIS A 29  ? 0.2761 0.2498 0.3731 0.0067  -0.0085 0.0239  50  HIS A CB  
259  C CG  . HIS A 29  ? 0.2939 0.2721 0.3781 -0.0011 -0.0090 0.0341  50  HIS A CG  
260  N ND1 . HIS A 29  ? 0.2998 0.2752 0.3796 -0.0075 -0.0154 0.0470  50  HIS A ND1 
261  C CD2 . HIS A 29  ? 0.2963 0.2854 0.3717 -0.0038 -0.0050 0.0320  50  HIS A CD2 
262  C CE1 . HIS A 29  ? 0.2997 0.2896 0.3664 -0.0128 -0.0134 0.0511  50  HIS A CE1 
263  N NE2 . HIS A 29  ? 0.2803 0.2763 0.3449 -0.0094 -0.0079 0.0402  50  HIS A NE2 
264  N N   . LYS A 30  ? 0.2721 0.2672 0.3940 0.0254  -0.0042 -0.0046 51  LYS A N   
265  C CA  . LYS A 30  ? 0.2468 0.2465 0.3770 0.0342  -0.0044 -0.0191 51  LYS A CA  
266  C C   . LYS A 30  ? 0.2957 0.3230 0.4198 0.0331  0.0080  -0.0259 51  LYS A C   
267  O O   . LYS A 30  ? 0.2613 0.2930 0.3798 0.0342  0.0123  -0.0323 51  LYS A O   
268  C CB  . LYS A 30  ? 0.2703 0.2712 0.4236 0.0477  -0.0167 -0.0314 51  LYS A CB  
269  C CG  . LYS A 30  ? 0.3842 0.3529 0.5478 0.0487  -0.0341 -0.0247 51  LYS A CG  
270  C CD  . LYS A 30  ? 0.4559 0.4093 0.6168 0.0469  -0.0356 -0.0276 51  LYS A CD  
271  C CE  . LYS A 30  ? 0.6257 0.5483 0.8038 0.0472  -0.0569 -0.0206 51  LYS A CE  
272  N NZ  . LYS A 30  ? 0.6596 0.5646 0.8383 0.0426  -0.0617 -0.0200 51  LYS A NZ  
273  N N   . ASN A 31  ? 0.2324 0.2804 0.3578 0.0297  0.0127  -0.0230 52  ASN A N   
274  C CA  . ASN A 31  ? 0.2276 0.3044 0.3474 0.0246  0.0230  -0.0239 52  ASN A CA  
275  C C   . ASN A 31  ? 0.2377 0.3010 0.3398 0.0125  0.0275  -0.0114 52  ASN A C   
276  O O   . ASN A 31  ? 0.2708 0.3494 0.3659 0.0084  0.0331  -0.0107 52  ASN A O   
277  C CB  . ASN A 31  ? 0.2574 0.3641 0.3867 0.0217  0.0257  -0.0223 52  ASN A CB  
278  C CG  . ASN A 31  ? 0.2299 0.3690 0.3773 0.0356  0.0248  -0.0408 52  ASN A CG  
279  O OD1 . ASN A 31  ? 0.2574 0.4134 0.4055 0.0432  0.0275  -0.0544 52  ASN A OD1 
280  N ND2 . ASN A 31  ? 0.2312 0.3794 0.3947 0.0412  0.0193  -0.0444 52  ASN A ND2 
281  N N   . VAL A 32  ? 0.2542 0.2928 0.3501 0.0074  0.0237  -0.0024 53  VAL A N   
282  C CA  . VAL A 32  ? 0.2362 0.2615 0.3190 -0.0003 0.0254  0.0046  53  VAL A CA  
283  C C   . VAL A 32  ? 0.2877 0.3049 0.3646 0.0032  0.0268  -0.0003 53  VAL A C   
284  O O   . VAL A 32  ? 0.2648 0.2832 0.3333 -0.0011 0.0294  0.0023  53  VAL A O   
285  C CB  . VAL A 32  ? 0.2809 0.2881 0.3592 -0.0036 0.0208  0.0098  53  VAL A CB  
286  C CG1 . VAL A 32  ? 0.3610 0.3547 0.4286 -0.0067 0.0209  0.0112  53  VAL A CG1 
287  C CG2 . VAL A 32  ? 0.2978 0.3117 0.3802 -0.0093 0.0183  0.0144  53  VAL A CG2 
288  N N   . MET A 33  ? 0.2514 0.2587 0.3339 0.0102  0.0227  -0.0062 54  MET A N   
289  C CA  . MET A 33  ? 0.2953 0.2957 0.3757 0.0134  0.0223  -0.0122 54  MET A CA  
290  C C   . MET A 33  ? 0.3131 0.3358 0.3945 0.0184  0.0261  -0.0229 54  MET A C   
291  O O   . MET A 33  ? 0.2853 0.3075 0.3594 0.0178  0.0277  -0.0254 54  MET A O   
292  C CB  . MET A 33  ? 0.3044 0.2877 0.3948 0.0180  0.0134  -0.0146 54  MET A CB  
293  C CG  . MET A 33  ? 0.3212 0.2891 0.4068 0.0105  0.0103  -0.0019 54  MET A CG  
294  S SD  . MET A 33  ? 0.3749 0.3413 0.4452 0.0032  0.0167  0.0024  54  MET A SD  
295  C CE  . MET A 33  ? 0.3164 0.2790 0.3893 0.0065  0.0156  -0.0062 54  MET A CE  
296  N N   . ARG A 34  ? 0.2965 0.3438 0.3868 0.0234  0.0276  -0.0300 55  ARG A N   
297  C CA  . ARG A 34  ? 0.2676 0.3483 0.3570 0.0272  0.0328  -0.0405 55  ARG A CA  
298  C C   . ARG A 34  ? 0.2614 0.3539 0.3352 0.0145  0.0394  -0.0265 55  ARG A C   
299  O O   . ARG A 34  ? 0.2948 0.4014 0.3601 0.0144  0.0419  -0.0299 55  ARG A O   
300  C CB  . ARG A 34  ? 0.2563 0.3703 0.3598 0.0345  0.0339  -0.0510 55  ARG A CB  
301  C CG  . ARG A 34  ? 0.2551 0.3581 0.3776 0.0507  0.0231  -0.0696 55  ARG A CG  
302  C CD  . ARG A 34  ? 0.2497 0.3874 0.3907 0.0628  0.0217  -0.0862 55  ARG A CD  
303  N NE  . ARG A 34  ? 0.3197 0.4309 0.4809 0.0771  0.0057  -0.0998 55  ARG A NE  
304  C CZ  . ARG A 34  ? 0.3636 0.4554 0.5378 0.0794  -0.0039 -0.0944 55  ARG A CZ  
305  N NH1 . ARG A 34  ? 0.2543 0.3548 0.4246 0.0705  0.0019  -0.0799 55  ARG A NH1 
306  N NH2 . ARG A 34  ? 0.3391 0.4041 0.5328 0.0911  -0.0218 -0.1044 55  ARG A NH2 
307  N N   . MET A 35  ? 0.2351 0.3182 0.3062 0.0040  0.0394  -0.0108 56  MET A N   
308  C CA  . MET A 35  ? 0.2778 0.3629 0.3382 -0.0090 0.0403  0.0048  56  MET A CA  
309  C C   . MET A 35  ? 0.2635 0.3235 0.3142 -0.0088 0.0373  0.0058  56  MET A C   
310  O O   . MET A 35  ? 0.3242 0.3935 0.3658 -0.0135 0.0376  0.0110  56  MET A O   
311  C CB  . MET A 35  ? 0.3463 0.4198 0.4104 -0.0188 0.0363  0.0183  56  MET A CB  
312  C CG  . MET A 35  ? 0.3872 0.4535 0.4451 -0.0319 0.0314  0.0347  56  MET A CG  
313  S SD  . MET A 35  ? 0.3984 0.4397 0.4647 -0.0393 0.0214  0.0435  56  MET A SD  
314  C CE  . MET A 35  ? 0.3884 0.3953 0.4499 -0.0287 0.0179  0.0321  56  MET A CE  
315  N N   . VAL A 36  ? 0.2432 0.2754 0.2960 -0.0045 0.0338  0.0024  57  VAL A N   
316  C CA  . VAL A 36  ? 0.2517 0.2648 0.2979 -0.0041 0.0313  0.0020  57  VAL A CA  
317  C C   . VAL A 36  ? 0.3134 0.3360 0.3564 0.0012  0.0327  -0.0073 57  VAL A C   
318  O O   . VAL A 36  ? 0.2991 0.3226 0.3340 -0.0016 0.0317  -0.0042 57  VAL A O   
319  C CB  . VAL A 36  ? 0.2946 0.2873 0.3443 -0.0014 0.0286  -0.0003 57  VAL A CB  
320  C CG1 . VAL A 36  ? 0.2847 0.2659 0.3305 -0.0007 0.0269  -0.0024 57  VAL A CG1 
321  C CG2 . VAL A 36  ? 0.2832 0.2690 0.3337 -0.0061 0.0260  0.0067  57  VAL A CG2 
322  N N   . ASN A 37  ? 0.2707 0.2994 0.3219 0.0096  0.0326  -0.0200 58  ASN A N   
323  C CA  . ASN A 37  ? 0.3154 0.3529 0.3664 0.0165  0.0314  -0.0333 58  ASN A CA  
324  C C   . ASN A 37  ? 0.3530 0.4240 0.3942 0.0148  0.0360  -0.0341 58  ASN A C   
325  O O   . ASN A 37  ? 0.3507 0.4283 0.3847 0.0163  0.0350  -0.0392 58  ASN A O   
326  C CB  . ASN A 37  ? 0.3257 0.3615 0.3919 0.0273  0.0264  -0.0490 58  ASN A CB  
327  C CG  . ASN A 37  ? 0.4016 0.4050 0.4762 0.0261  0.0192  -0.0448 58  ASN A CG  
328  O OD1 . ASN A 37  ? 0.4619 0.4508 0.5308 0.0201  0.0188  -0.0372 58  ASN A OD1 
329  N ND2 . ASN A 37  ? 0.3973 0.3930 0.4863 0.0313  0.0127  -0.0487 58  ASN A ND2 
330  N N   . HIS A 38  ? 0.2942 0.3905 0.3352 0.0104  0.0406  -0.0279 59  HIS A N   
331  C CA  . HIS A 38  ? 0.3475 0.4830 0.3790 0.0055  0.0452  -0.0243 59  HIS A CA  
332  C C   . HIS A 38  ? 0.3582 0.4822 0.3762 -0.0061 0.0423  -0.0058 59  HIS A C   
333  O O   . HIS A 38  ? 0.3648 0.5094 0.3719 -0.0077 0.0424  -0.0056 59  HIS A O   
334  C CB  . HIS A 38  ? 0.3247 0.4926 0.3604 -0.0010 0.0503  -0.0166 59  HIS A CB  
335  C CG  . HIS A 38  ? 0.5248 0.7376 0.5489 -0.0121 0.0546  -0.0048 59  HIS A CG  
336  N ND1 . HIS A 38  ? 0.4690 0.7283 0.4875 -0.0054 0.0593  -0.0197 59  HIS A ND1 
337  C CD2 . HIS A 38  ? 0.5320 0.7510 0.5491 -0.0303 0.0530  0.0218  59  HIS A CD2 
338  C CE1 . HIS A 38  ? 0.4720 0.7696 0.4783 -0.0205 0.0623  -0.0008 59  HIS A CE1 
339  N NE2 . HIS A 38  ? 0.5212 0.7927 0.5274 -0.0367 0.0576  0.0263  59  HIS A NE2 
340  N N   . GLU A 39  ? 0.2993 0.3926 0.3195 -0.0134 0.0380  0.0084  60  GLU A N   
341  C CA  . GLU A 39  ? 0.3378 0.4174 0.3501 -0.0227 0.0314  0.0247  60  GLU A CA  
342  C C   . GLU A 39  ? 0.2619 0.3272 0.2692 -0.0157 0.0285  0.0153  60  GLU A C   
343  O O   . GLU A 39  ? 0.3073 0.3816 0.3049 -0.0198 0.0248  0.0225  60  GLU A O   
344  C CB  . GLU A 39  ? 0.3142 0.3627 0.3338 -0.0278 0.0248  0.0348  60  GLU A CB  
345  C CG  . GLU A 39  ? 0.3689 0.4312 0.3944 -0.0379 0.0249  0.0473  60  GLU A CG  
346  C CD  . GLU A 39  ? 0.4354 0.5229 0.4553 -0.0530 0.0217  0.0679  60  GLU A CD  
347  O OE1 . GLU A 39  ? 0.4362 0.5144 0.4494 -0.0580 0.0136  0.0785  60  GLU A OE1 
348  O OE2 . GLU A 39  ? 0.4326 0.5523 0.4556 -0.0610 0.0263  0.0752  60  GLU A OE2 
349  N N   . VAL A 40  ? 0.2883 0.3331 0.3030 -0.0067 0.0289  0.0017  61  VAL A N   
350  C CA  . VAL A 40  ? 0.3015 0.3326 0.3151 -0.0019 0.0254  -0.0060 61  VAL A CA  
351  C C   . VAL A 40  ? 0.3608 0.4168 0.3677 0.0025  0.0265  -0.0165 61  VAL A C   
352  O O   . VAL A 40  ? 0.3092 0.3667 0.3088 0.0021  0.0225  -0.0159 61  VAL A O   
353  C CB  . VAL A 40  ? 0.3495 0.3600 0.3738 0.0037  0.0251  -0.0154 61  VAL A CB  
354  C CG1 . VAL A 40  ? 0.3501 0.3545 0.3757 0.0075  0.0217  -0.0245 61  VAL A CG1 
355  C CG2 . VAL A 40  ? 0.2839 0.2753 0.3118 -0.0001 0.0233  -0.0068 61  VAL A CG2 
356  N N   . SER A 41  ? 0.3471 0.4260 0.3573 0.0081  0.0309  -0.0282 62  SER A N   
357  C CA  . SER A 41  ? 0.3269 0.4341 0.3322 0.0151  0.0309  -0.0441 62  SER A CA  
358  C C   . SER A 41  ? 0.4222 0.5625 0.4101 0.0071  0.0322  -0.0323 62  SER A C   
359  O O   . SER A 41  ? 0.3900 0.5526 0.3703 0.0118  0.0308  -0.0437 62  SER A O   
360  C CB  . SER A 41  ? 0.3926 0.5215 0.4084 0.0255  0.0334  -0.0636 62  SER A CB  
361  O OG  . SER A 41  ? 0.6261 0.7918 0.6363 0.0198  0.0404  -0.0552 62  SER A OG  
362  N N   . SER A 42  ? 0.3822 0.5267 0.3647 -0.0059 0.0331  -0.0088 63  SER A N   
363  C CA  . SER A 42  ? 0.4439 0.6189 0.4108 -0.0178 0.0317  0.0099  63  SER A CA  
364  C C   . SER A 42  ? 0.3986 0.5487 0.3586 -0.0228 0.0215  0.0233  63  SER A C   
365  O O   . SER A 42  ? 0.3868 0.5589 0.3338 -0.0329 0.0171  0.0405  63  SER A O   
366  C CB  . SER A 42  ? 0.3945 0.5835 0.3623 -0.0323 0.0334  0.0327  63  SER A CB  
367  O OG  . SER A 42  ? 0.4406 0.5836 0.4176 -0.0375 0.0261  0.0461  63  SER A OG  
368  N N   . PHE A 43  ? 0.4280 0.4007 0.4971 -0.1353 -0.0202 -0.1568 64  PHE A N   
369  C CA  . PHE A 43  ? 0.4534 0.4109 0.5061 -0.1284 -0.0515 -0.1632 64  PHE A CA  
370  C C   . PHE A 43  ? 0.4190 0.4366 0.4186 -0.1261 -0.0449 -0.1610 64  PHE A C   
371  O O   . PHE A 43  ? 0.4404 0.5127 0.4341 -0.1306 -0.0236 -0.1985 64  PHE A O   
372  C CB  . PHE A 43  ? 0.3642 0.3077 0.4110 -0.0876 -0.0626 -0.1583 64  PHE A CB  
373  C CG  . PHE A 43  ? 0.3405 0.2470 0.4040 -0.0767 -0.0659 -0.1376 64  PHE A CG  
374  C CD1 . PHE A 43  ? 0.3526 0.2503 0.4314 -0.0849 -0.0534 -0.1243 64  PHE A CD1 
375  C CD2 . PHE A 43  ? 0.3505 0.2464 0.4183 -0.0543 -0.0805 -0.1337 64  PHE A CD2 
376  C CE1 . PHE A 43  ? 0.3534 0.2423 0.4570 -0.0706 -0.0561 -0.1166 64  PHE A CE1 
377  C CE2 . PHE A 43  ? 0.3412 0.2268 0.4359 -0.0402 -0.0832 -0.1217 64  PHE A CE2 
378  C CZ  . PHE A 43  ? 0.3583 0.2445 0.4782 -0.0468 -0.0734 -0.1172 64  PHE A CZ  
379  N N   . GLY A 44  ? 0.4802 0.4929 0.4443 -0.1176 -0.0600 -0.1175 65  GLY A N   
380  C CA  . GLY A 44  ? 0.5126 0.5955 0.4240 -0.1132 -0.0546 -0.1126 65  GLY A CA  
381  C C   . GLY A 44  ? 0.5291 0.6627 0.4193 -0.1381 -0.0223 -0.1029 65  GLY A C   
382  O O   . GLY A 44  ? 0.6646 0.8688 0.5127 -0.1349 -0.0167 -0.1053 65  GLY A O   
383  N N   . VAL A 45  ? 0.5926 0.6983 0.5106 -0.1628 -0.0008 -0.0925 66  VAL A N   
384  C CA  . VAL A 45  ? 0.5988 0.7487 0.4938 -0.1854 0.0282  -0.0758 66  VAL A CA  
385  C C   . VAL A 45  ? 0.6474 0.7968 0.5028 -0.1779 0.0208  -0.0125 66  VAL A C   
386  O O   . VAL A 45  ? 0.6624 0.7481 0.5302 -0.1700 0.0070  0.0298  66  VAL A O   
387  C CB  . VAL A 45  ? 0.8338 0.9557 0.7676 -0.2143 0.0548  -0.0750 66  VAL A CB  
388  C CG1 . VAL A 45  ? 0.7652 0.8935 0.7389 -0.2188 0.0693  -0.1298 66  VAL A CG1 
389  C CG2 . VAL A 45  ? 0.8602 0.9075 0.8217 -0.2174 0.0437  -0.0350 66  VAL A CG2 
390  N N   . VAL A 46  ? 0.6524 0.8777 0.4632 -0.1803 0.0342  -0.0070 67  VAL A N   
391  C CA  . VAL A 46  ? 0.7301 0.9697 0.5010 -0.1720 0.0347  0.0557  67  VAL A CA  
392  C C   . VAL A 46  ? 0.9313 1.1650 0.7064 -0.2006 0.0649  0.0858  67  VAL A C   
393  O O   . VAL A 46  ? 0.8862 1.1551 0.6693 -0.2252 0.0889  0.0520  67  VAL A O   
394  C CB  . VAL A 46  ? 0.7544 1.0953 0.4697 -0.1538 0.0302  0.0470  67  VAL A CB  
395  C CG1 . VAL A 46  ? 0.8390 1.2064 0.5094 -0.1396 0.0333  0.1178  67  VAL A CG1 
396  C CG2 . VAL A 46  ? 0.7329 1.0796 0.4465 -0.1258 0.0001  0.0157  67  VAL A CG2 
397  N N   . THR A 47  ? 1.0775 1.2641 0.8509 -0.1970 0.0661  0.1499  68  THR A N   
398  C CA  . THR A 47  ? 1.1462 1.3374 0.9134 -0.2192 0.0949  0.1882  68  THR A CA  
399  C C   . THR A 47  ? 1.2753 1.5133 0.9884 -0.1971 0.0971  0.2467  68  THR A C   
400  O O   . THR A 47  ? 1.3885 1.5733 1.1056 -0.1833 0.0964  0.3074  68  THR A O   
401  C CB  . THR A 47  ? 1.1485 1.2457 0.9669 -0.2364 0.1029  0.2159  68  THR A CB  
402  O OG1 . THR A 47  ? 1.1862 1.2260 1.0101 -0.2125 0.0876  0.2634  68  THR A OG1 
403  C CG2 . THR A 47  ? 1.0799 1.1391 0.9518 -0.2520 0.0979  0.1602  68  THR A CG2 
404  N N   . SER A 48  ? 1.2795 1.6208 0.9458 -0.1928 0.1023  0.2268  69  SER A N   
405  C CA  . SER A 48  ? 1.3322 1.7486 0.9395 -0.1658 0.1020  0.2732  69  SER A CA  
406  C C   . SER A 48  ? 1.3787 1.7489 0.9788 -0.1285 0.0832  0.3326  69  SER A C   
407  O O   . SER A 48  ? 1.3262 1.6583 0.9438 -0.1117 0.0574  0.3123  69  SER A O   
408  C CB  . SER A 48  ? 1.4276 1.8720 1.0160 -0.1828 0.1332  0.3159  69  SER A CB  
409  O OG  . SER A 48  ? 1.4216 1.9087 1.0175 -0.2172 0.1534  0.2630  69  SER A OG  
410  N N   . ALA A 49  ? 1.4208 1.7954 0.9963 -0.1145 0.0991  0.4078  70  ALA A N   
411  C CA  . ALA A 49  ? 1.4667 1.7693 1.0526 -0.0857 0.0944  0.4762  70  ALA A CA  
412  C C   . ALA A 49  ? 1.4522 1.7809 1.0144 -0.0439 0.0636  0.4746  70  ALA A C   
413  O O   . ALA A 49  ? 1.4043 1.8415 0.9177 -0.0249 0.0517  0.4518  70  ALA A O   
414  C CB  . ALA A 49  ? 1.4050 1.5782 1.0626 -0.1109 0.0986  0.4731  70  ALA A CB  
415  N N   . GLU A 50  ? 1.4439 1.6742 1.0452 -0.0317 0.0515  0.4942  71  GLU A N   
416  C CA  . GLU A 50  ? 1.3884 1.6243 0.9752 0.0084  0.0232  0.4993  71  GLU A CA  
417  C C   . GLU A 50  ? 1.2351 1.4209 0.8620 -0.0022 -0.0043 0.4291  71  GLU A C   
418  O O   . GLU A 50  ? 1.1720 1.3239 0.8060 0.0256  -0.0265 0.4365  71  GLU A O   
419  C CB  . GLU A 50  ? 1.4675 1.6322 1.0664 0.0382  0.0335  0.5852  71  GLU A CB  
420  C CG  . GLU A 50  ? 1.4574 1.4918 1.1279 0.0103  0.0504  0.5990  71  GLU A CG  
421  C CD  . GLU A 50  ? 1.6102 1.5762 1.2976 0.0390  0.0697  0.6861  71  GLU A CD  
422  O OE1 . GLU A 50  ? 1.7219 1.7403 1.3632 0.0853  0.0670  0.7379  71  GLU A OE1 
423  O OE2 . GLU A 50  ? 1.6020 1.4654 1.3514 0.0163  0.0902  0.7025  71  GLU A OE2 
424  N N   . ASP A 51  ? 1.1652 1.3468 0.8194 -0.0400 -0.0012 0.3637  72  ASP A N   
425  C CA  . ASP A 51  ? 1.0490 1.1881 0.7412 -0.0461 -0.0247 0.3007  72  ASP A CA  
426  C C   . ASP A 51  ? 1.0509 1.2773 0.7223 -0.0518 -0.0339 0.2260  72  ASP A C   
427  O O   . ASP A 51  ? 0.9639 1.1636 0.6716 -0.0679 -0.0411 0.1663  72  ASP A O   
428  C CB  . ASP A 51  ? 1.0044 1.0487 0.7620 -0.0800 -0.0142 0.2853  72  ASP A CB  
429  C CG  . ASP A 51  ? 1.0585 1.1316 0.8237 -0.1178 0.0105  0.2555  72  ASP A CG  
430  O OD1 . ASP A 51  ? 1.1480 1.3037 0.8691 -0.1202 0.0248  0.2604  72  ASP A OD1 
431  O OD2 . ASP A 51  ? 1.0401 1.0570 0.8567 -0.1442 0.0165  0.2279  72  ASP A OD2 
432  N N   . SER A 52  ? 1.1033 1.4376 0.7189 -0.0362 -0.0321 0.2291  73  SER A N   
433  C CA  . SER A 52  ? 0.9759 1.4031 0.5734 -0.0405 -0.0373 0.1564  73  SER A CA  
434  C C   . SER A 52  ? 0.8869 1.3047 0.4928 -0.0171 -0.0683 0.1202  73  SER A C   
435  O O   . SER A 52  ? 0.8968 1.3654 0.5062 -0.0228 -0.0728 0.0509  73  SER A O   
436  C CB  . SER A 52  ? 1.0486 1.6028 0.5857 -0.0278 -0.0283 0.1692  73  SER A CB  
437  O OG  . SER A 52  ? 1.1227 1.6845 0.6511 -0.0478 0.0006  0.2069  73  SER A OG  
438  N N   . TYR A 53  ? 0.9263 1.2772 0.5384 0.0095  -0.0868 0.1683  74  TYR A N   
439  C CA  . TYR A 53  ? 0.9917 1.3195 0.6144 0.0333  -0.1172 0.1427  74  TYR A CA  
440  C C   . TYR A 53  ? 0.9379 1.2085 0.6146 0.0081  -0.1198 0.0775  74  TYR A C   
441  O O   . TYR A 53  ? 0.8503 1.1294 0.5364 0.0188  -0.1392 0.0283  74  TYR A O   
442  C CB  . TYR A 53  ? 1.1256 1.3784 0.7532 0.0633  -0.1304 0.2124  74  TYR A CB  
443  C CG  . TYR A 53  ? 1.1850 1.3113 0.8705 0.0457  -0.1236 0.2359  74  TYR A CG  
444  C CD1 . TYR A 53  ? 1.0917 1.1472 0.8260 0.0386  -0.1411 0.1924  74  TYR A CD1 
445  C CD2 . TYR A 53  ? 1.2260 1.3071 0.9198 0.0382  -0.0992 0.3013  74  TYR A CD2 
446  C CE1 . TYR A 53  ? 1.0197 0.9726 0.8093 0.0228  -0.1359 0.2068  74  TYR A CE1 
447  C CE2 . TYR A 53  ? 1.2164 1.1868 0.9699 0.0201  -0.0917 0.3152  74  TYR A CE2 
448  C CZ  . TYR A 53  ? 1.1123 1.0234 0.9134 0.0122  -0.1113 0.2649  74  TYR A CZ  
449  O OH  . TYR A 53  ? 1.0173 0.8320 0.8799 -0.0057 -0.1057 0.2696  74  TYR A OH  
450  N N   . LEU A 54  ? 0.8920 1.1100 0.6041 -0.0242 -0.0982 0.0782  75  LEU A N   
451  C CA  . LEU A 54  ? 0.8593 1.0284 0.6235 -0.0457 -0.0965 0.0240  75  LEU A CA  
452  C C   . LEU A 54  ? 0.7583 0.9962 0.5230 -0.0584 -0.0858 -0.0480 75  LEU A C   
453  O O   . LEU A 54  ? 0.6191 0.8247 0.4235 -0.0640 -0.0882 -0.0939 75  LEU A O   
454  C CB  . LEU A 54  ? 0.9256 1.0350 0.7258 -0.0760 -0.0739 0.0443  75  LEU A CB  
455  C CG  . LEU A 54  ? 0.9281 0.9353 0.7746 -0.0750 -0.0846 0.0693  75  LEU A CG  
456  C CD1 . LEU A 54  ? 0.9200 0.9003 0.7689 -0.0437 -0.1170 0.0640  75  LEU A CD1 
457  C CD2 . LEU A 54  ? 0.9215 0.8919 0.7658 -0.0803 -0.0692 0.1378  75  LEU A CD2 
458  N N   . GLY A 55  ? 0.8562 1.1907 0.5801 -0.0621 -0.0712 -0.0578 76  GLY A N   
459  C CA  . GLY A 55  ? 0.6752 1.0723 0.4079 -0.0848 -0.0464 -0.1213 76  GLY A CA  
460  C C   . GLY A 55  ? 0.6387 1.0629 0.3914 -0.0733 -0.0528 -0.1847 76  GLY A C   
461  O O   . GLY A 55  ? 0.5209 0.9340 0.3323 -0.0845 -0.0241 -0.2161 76  GLY A O   
462  N N   . ALA A 56  ? 0.3529 0.5309 0.2585 -0.0498 -0.0135 0.0368  77  ALA A N   
463  C CA  . ALA A 56  ? 0.3391 0.4856 0.2617 -0.0351 -0.0158 0.0186  77  ALA A CA  
464  C C   . ALA A 56  ? 0.3391 0.4462 0.2697 -0.0352 -0.0281 0.0368  77  ALA A C   
465  O O   . ALA A 56  ? 0.3578 0.4654 0.2776 -0.0456 -0.0408 0.0616  77  ALA A O   
466  C CB  . ALA A 56  ? 0.3494 0.5269 0.2646 -0.0322 -0.0181 0.0000  77  ALA A CB  
467  N N   . VAL A 57  ? 0.3230 0.4007 0.2728 -0.0249 -0.0271 0.0243  78  VAL A N   
468  C CA  . VAL A 57  ? 0.3224 0.3730 0.2846 -0.0218 -0.0386 0.0328  78  VAL A CA  
469  C C   . VAL A 57  ? 0.3744 0.4204 0.3506 -0.0141 -0.0375 0.0126  78  VAL A C   
470  O O   . VAL A 57  ? 0.3328 0.3863 0.3104 -0.0120 -0.0287 -0.0051 78  VAL A O   
471  C CB  . VAL A 57  ? 0.3121 0.3353 0.2868 -0.0202 -0.0375 0.0407  78  VAL A CB  
472  C CG1 . VAL A 57  ? 0.3271 0.3521 0.2896 -0.0309 -0.0422 0.0644  78  VAL A CG1 
473  C CG2 . VAL A 57  ? 0.3125 0.3274 0.2969 -0.0155 -0.0230 0.0252  78  VAL A CG2 
474  N N   . ASP A 58  ? 0.3131 0.3479 0.3022 -0.0101 -0.0480 0.0134  79  ASP A N   
475  C CA  . ASP A 58  ? 0.3042 0.3412 0.3076 -0.0060 -0.0458 -0.0060 79  ASP A CA  
476  C C   . ASP A 58  ? 0.2907 0.3130 0.3089 -0.0056 -0.0353 -0.0133 79  ASP A C   
477  O O   . ASP A 58  ? 0.2875 0.2976 0.3047 -0.0061 -0.0302 -0.0051 79  ASP A O   
478  C CB  . ASP A 58  ? 0.3123 0.3534 0.3257 -0.0017 -0.0610 -0.0067 79  ASP A CB  
479  C CG  . ASP A 58  ? 0.3286 0.3544 0.3581 0.0041  -0.0711 -0.0003 79  ASP A CG  
480  O OD1 . ASP A 58  ? 0.3557 0.3678 0.3876 0.0038  -0.0655 0.0050  79  ASP A OD1 
481  O OD2 . ASP A 58  ? 0.3674 0.3963 0.4087 0.0104  -0.0870 -0.0030 79  ASP A OD2 
482  N N   . GLU A 59  ? 0.2809 0.3063 0.3118 -0.0071 -0.0326 -0.0272 80  GLU A N   
483  C CA  . GLU A 59  ? 0.2699 0.2856 0.3103 -0.0116 -0.0233 -0.0308 80  GLU A CA  
484  C C   . GLU A 59  ? 0.2937 0.3090 0.3464 -0.0086 -0.0241 -0.0278 80  GLU A C   
485  O O   . GLU A 59  ? 0.2962 0.3034 0.3500 -0.0111 -0.0168 -0.0249 80  GLU A O   
486  C CB  . GLU A 59  ? 0.2712 0.2928 0.3212 -0.0193 -0.0223 -0.0430 80  GLU A CB  
487  C CG  . GLU A 59  ? 0.2922 0.3116 0.3340 -0.0200 -0.0247 -0.0509 80  GLU A CG  
488  C CD  . GLU A 59  ? 0.4049 0.4192 0.4577 -0.0305 -0.0265 -0.0602 80  GLU A CD  
489  O OE1 . GLU A 59  ? 0.3220 0.3502 0.3832 -0.0340 -0.0318 -0.0683 80  GLU A OE1 
490  O OE2 . GLU A 59  ? 0.4121 0.4078 0.4657 -0.0363 -0.0246 -0.0579 80  GLU A OE2 
491  N N   A ASN A 60  ? 0.2869 0.3122 0.3502 -0.0018 -0.0351 -0.0309 81  ASN A N   
492  N N   B ASN A 60  ? 0.2879 0.3130 0.3510 -0.0018 -0.0351 -0.0307 81  ASN A N   
493  C CA  A ASN A 60  ? 0.2888 0.3165 0.3687 0.0049  -0.0395 -0.0345 81  ASN A CA  
494  C CA  B ASN A 60  ? 0.2933 0.3211 0.3732 0.0048  -0.0395 -0.0345 81  ASN A CA  
495  C C   A ASN A 60  ? 0.3195 0.3266 0.3925 0.0080  -0.0416 -0.0210 81  ASN A C   
496  C C   B ASN A 60  ? 0.3096 0.3169 0.3830 0.0082  -0.0420 -0.0212 81  ASN A C   
497  O O   A ASN A 60  ? 0.3057 0.3109 0.3878 0.0100  -0.0384 -0.0243 81  ASN A O   
498  O O   B ASN A 60  ? 0.3047 0.3106 0.3877 0.0105  -0.0391 -0.0249 81  ASN A O   
499  C CB  A ASN A 60  ? 0.3234 0.3634 0.4199 0.0151  -0.0566 -0.0429 81  ASN A CB  
500  C CB  B ASN A 60  ? 0.3289 0.3693 0.4254 0.0148  -0.0561 -0.0431 81  ASN A CB  
501  C CG  A ASN A 60  ? 0.3884 0.4576 0.5005 0.0123  -0.0537 -0.0610 81  ASN A CG  
502  C CG  B ASN A 60  ? 0.3655 0.4137 0.4857 0.0252  -0.0636 -0.0551 81  ASN A CG  
503  O OD1 A ASN A 60  ? 0.4678 0.5486 0.5804 0.0006  -0.0397 -0.0662 81  ASN A OD1 
504  O OD1 B ASN A 60  ? 0.4173 0.4837 0.5477 0.0218  -0.0522 -0.0669 81  ASN A OD1 
505  N ND2 A ASN A 60  ? 0.4169 0.4986 0.5420 0.0212  -0.0693 -0.0693 81  ASN A ND2 
506  N ND2 B ASN A 60  ? 0.4193 0.4553 0.5491 0.0374  -0.0851 -0.0525 81  ASN A ND2 
507  N N   . THR A 61  ? 0.3201 0.3158 0.3767 0.0070  -0.0477 -0.0058 82  THR A N   
508  C CA  . THR A 61  ? 0.3230 0.3014 0.3722 0.0060  -0.0508 0.0098  82  THR A CA  
509  C C   . THR A 61  ? 0.3948 0.3694 0.4363 0.0006  -0.0337 0.0104  82  THR A C   
510  O O   . THR A 61  ? 0.3180 0.2822 0.3640 0.0017  -0.0329 0.0140  82  THR A O   
511  C CB  . THR A 61  ? 0.3008 0.2778 0.3316 0.0009  -0.0604 0.0278  82  THR A CB  
512  O OG1 . THR A 61  ? 0.3167 0.2935 0.3549 0.0059  -0.0806 0.0298  82  THR A OG1 
513  C CG2 . THR A 61  ? 0.3127 0.2759 0.3350 -0.0050 -0.0643 0.0472  82  THR A CG2 
514  N N   . LEU A 62  ? 0.2813 0.2628 0.3128 -0.0042 -0.0230 0.0059  83  LEU A N   
515  C CA  . LEU A 62  ? 0.3003 0.2756 0.3283 -0.0078 -0.0107 0.0044  83  LEU A CA  
516  C C   . LEU A 62  ? 0.3350 0.3082 0.3759 -0.0084 -0.0066 -0.0015 83  LEU A C   
517  O O   . LEU A 62  ? 0.3156 0.2807 0.3557 -0.0094 -0.0016 0.0023  83  LEU A O   
518  C CB  . LEU A 62  ? 0.2623 0.2420 0.2845 -0.0108 -0.0058 -0.0044 83  LEU A CB  
519  C CG  . LEU A 62  ? 0.3513 0.3192 0.3738 -0.0136 0.0013  -0.0068 83  LEU A CG  
520  C CD1 . LEU A 62  ? 0.3746 0.3375 0.3912 -0.0116 0.0050  0.0019  83  LEU A CD1 
521  C CD2 . LEU A 62  ? 0.3732 0.3416 0.3937 -0.0139 -0.0004 -0.0179 83  LEU A CD2 
522  N N   . GLU A 63  ? 0.2765 0.2629 0.3290 -0.0090 -0.0082 -0.0119 84  GLU A N   
523  C CA  . GLU A 63  ? 0.2686 0.2663 0.3323 -0.0125 -0.0032 -0.0193 84  GLU A CA  
524  C C   . GLU A 63  ? 0.2628 0.2596 0.3357 -0.0042 -0.0076 -0.0205 84  GLU A C   
525  O O   . GLU A 63  ? 0.2908 0.2892 0.3643 -0.0070 -0.0013 -0.0212 84  GLU A O   
526  C CB  . GLU A 63  ? 0.2755 0.2982 0.3521 -0.0157 -0.0045 -0.0321 84  GLU A CB  
527  C CG  . GLU A 63  ? 0.2803 0.3281 0.3666 -0.0239 0.0028  -0.0405 84  GLU A CG  
528  C CD  . GLU A 63  ? 0.3859 0.4670 0.4853 -0.0305 0.0027  -0.0534 84  GLU A CD  
529  O OE1 . GLU A 63  ? 0.3537 0.4427 0.4636 -0.0206 -0.0063 -0.0621 84  GLU A OE1 
530  O OE2 . GLU A 63  ? 0.3254 0.4265 0.4244 -0.0474 0.0105  -0.0535 84  GLU A OE2 
531  N N   . GLN A 64  ? 0.3018 0.2934 0.3819 0.0057  -0.0212 -0.0201 85  GLN A N   
532  C CA  . GLN A 64  ? 0.3070 0.2913 0.3992 0.0143  -0.0307 -0.0220 85  GLN A CA  
533  C C   . GLN A 64  ? 0.3291 0.2941 0.4089 0.0103  -0.0256 -0.0082 85  GLN A C   
534  O O   . GLN A 64  ? 0.2875 0.2517 0.3756 0.0133  -0.0257 -0.0132 85  GLN A O   
535  C CB  . GLN A 64  ? 0.3171 0.2894 0.4182 0.0237  -0.0521 -0.0186 85  GLN A CB  
536  C CG  . GLN A 64  ? 0.4153 0.4062 0.5353 0.0324  -0.0628 -0.0355 85  GLN A CG  
537  C CD  . GLN A 64  ? 0.5991 0.5685 0.7262 0.0410  -0.0894 -0.0266 85  GLN A CD  
538  O OE1 . GLN A 64  ? 0.6316 0.5922 0.7429 0.0356  -0.0953 -0.0103 85  GLN A OE1 
539  N NE2 . GLN A 64  ? 0.6195 0.5787 0.7686 0.0529  -0.1074 -0.0355 85  GLN A NE2 
540  N N   . ALA A 65  ? 0.2923 0.2460 0.3542 0.0043  -0.0227 0.0070  86  ALA A N   
541  C CA  . ALA A 65  ? 0.3377 0.2792 0.3890 -0.0001 -0.0179 0.0193  86  ALA A CA  
542  C C   . ALA A 65  ? 0.3167 0.2610 0.3651 -0.0036 -0.0040 0.0143  86  ALA A C   
543  O O   . ALA A 65  ? 0.3199 0.2575 0.3687 -0.0039 -0.0019 0.0174  86  ALA A O   
544  C CB  . ALA A 65  ? 0.3137 0.2563 0.3473 -0.0060 -0.0162 0.0316  86  ALA A CB  
545  N N   . THR A 66  ? 0.2408 0.1937 0.2865 -0.0079 0.0032  0.0079  87  THR A N   
546  C CA  . THR A 66  ? 0.2936 0.2466 0.3360 -0.0141 0.0117  0.0068  87  THR A CA  
547  C C   . THR A 66  ? 0.3136 0.2784 0.3654 -0.0139 0.0128  -0.0001 87  THR A C   
548  O O   . THR A 66  ? 0.2726 0.2332 0.3207 -0.0161 0.0165  0.0034  87  THR A O   
549  C CB  . THR A 66  ? 0.2611 0.2192 0.3011 -0.0220 0.0142  0.0030  87  THR A CB  
550  O OG1 . THR A 66  ? 0.3274 0.2745 0.3592 -0.0208 0.0132  0.0056  87  THR A OG1 
551  C CG2 . THR A 66  ? 0.2794 0.2393 0.3171 -0.0333 0.0187  0.0050  87  THR A CG2 
552  N N   . TRP A 67  ? 0.2683 0.2527 0.3335 -0.0105 0.0089  -0.0125 88  TRP A N   
553  C CA  . TRP A 67  ? 0.2483 0.2549 0.3243 -0.0095 0.0103  -0.0249 88  TRP A CA  
554  C C   . TRP A 67  ? 0.2954 0.2900 0.3790 0.0008  0.0028  -0.0266 88  TRP A C   
555  O O   . TRP A 67  ? 0.2749 0.2813 0.3611 0.0001  0.0060  -0.0332 88  TRP A O   
556  C CB  . TRP A 67  ? 0.2201 0.2589 0.3126 -0.0066 0.0073  -0.0431 88  TRP A CB  
557  C CG  . TRP A 67  ? 0.3255 0.3833 0.4096 -0.0236 0.0172  -0.0405 88  TRP A CG  
558  C CD1 . TRP A 67  ? 0.3109 0.3653 0.3916 -0.0295 0.0169  -0.0365 88  TRP A CD1 
559  C CD2 . TRP A 67  ? 0.2862 0.3654 0.3625 -0.0397 0.0264  -0.0381 88  TRP A CD2 
560  N NE1 . TRP A 67  ? 0.3212 0.3926 0.3955 -0.0489 0.0239  -0.0325 88  TRP A NE1 
561  C CE2 . TRP A 67  ? 0.3133 0.3998 0.3833 -0.0567 0.0296  -0.0312 88  TRP A CE2 
562  C CE3 . TRP A 67  ? 0.2484 0.3434 0.3222 -0.0431 0.0308  -0.0406 88  TRP A CE3 
563  C CZ2 . TRP A 67  ? 0.3223 0.4286 0.3822 -0.0798 0.0354  -0.0226 88  TRP A CZ2 
564  C CZ3 . TRP A 67  ? 0.2826 0.4030 0.3448 -0.0651 0.0383  -0.0336 88  TRP A CZ3 
565  C CH2 . TRP A 67  ? 0.3051 0.4299 0.3602 -0.0845 0.0399  -0.0228 88  TRP A CH2 
566  N N   . SER A 68  ? 0.2759 0.2477 0.3622 0.0080  -0.0084 -0.0192 89  SER A N   
567  C CA  . SER A 68  ? 0.2480 0.2020 0.3416 0.0142  -0.0190 -0.0163 89  SER A CA  
568  C C   . SER A 68  ? 0.2795 0.2247 0.3588 0.0068  -0.0086 -0.0050 89  SER A C   
569  O O   . SER A 68  ? 0.2911 0.2362 0.3763 0.0091  -0.0103 -0.0097 89  SER A O   
570  C CB  . SER A 68  ? 0.3135 0.2438 0.4073 0.0163  -0.0342 -0.0022 89  SER A CB  
571  O OG  . SER A 68  ? 0.3395 0.2494 0.4401 0.0179  -0.0469 0.0048  89  SER A OG  
572  N N   . PHE A 69  ? 0.2552 0.1939 0.3179 -0.0006 0.0000  0.0077  90  PHE A N   
573  C CA  . PHE A 69  ? 0.3180 0.2494 0.3695 -0.0057 0.0078  0.0165  90  PHE A CA  
574  C C   . PHE A 69  ? 0.3161 0.2594 0.3662 -0.0095 0.0147  0.0100  90  PHE A C   
575  O O   . PHE A 69  ? 0.2941 0.2350 0.3439 -0.0094 0.0153  0.0110  90  PHE A O   
576  C CB  . PHE A 69  ? 0.2623 0.1893 0.3012 -0.0097 0.0129  0.0245  90  PHE A CB  
577  C CG  . PHE A 69  ? 0.2793 0.2010 0.3111 -0.0119 0.0183  0.0289  90  PHE A CG  
578  C CD1 . PHE A 69  ? 0.3155 0.2358 0.3429 -0.0157 0.0217  0.0271  90  PHE A CD1 
579  C CD2 . PHE A 69  ? 0.3305 0.2498 0.3614 -0.0115 0.0174  0.0356  90  PHE A CD2 
580  C CE1 . PHE A 69  ? 0.3764 0.2891 0.4001 -0.0158 0.0223  0.0303  90  PHE A CE1 
581  C CE2 . PHE A 69  ? 0.3712 0.2894 0.3991 -0.0115 0.0210  0.0366  90  PHE A CE2 
582  C CZ  . PHE A 69  ? 0.3389 0.2521 0.3640 -0.0120 0.0225  0.0331  90  PHE A CZ  
583  N N   . LEU A 70  ? 0.2666 0.2250 0.3146 -0.0152 0.0192  0.0048  91  LEU A N   
584  C CA  . LEU A 70  ? 0.2647 0.2397 0.3077 -0.0243 0.0247  0.0029  91  LEU A CA  
585  C C   . LEU A 70  ? 0.2845 0.2798 0.3376 -0.0195 0.0232  -0.0104 91  LEU A C   
586  O O   . LEU A 70  ? 0.2719 0.2761 0.3182 -0.0252 0.0265  -0.0089 91  LEU A O   
587  C CB  . LEU A 70  ? 0.2433 0.2386 0.2840 -0.0357 0.0282  0.0005  91  LEU A CB  
588  C CG  . LEU A 70  ? 0.3246 0.2984 0.3568 -0.0412 0.0271  0.0114  91  LEU A CG  
589  C CD1 . LEU A 70  ? 0.2870 0.2804 0.3204 -0.0533 0.0283  0.0086  91  LEU A CD1 
590  C CD2 . LEU A 70  ? 0.3285 0.2809 0.3491 -0.0477 0.0254  0.0243  91  LEU A CD2 
591  N N   . LYS A 71  ? 0.2610 0.2667 0.3314 -0.0088 0.0164  -0.0256 92  LYS A N   
592  C CA  . LYS A 71  ? 0.2312 0.2574 0.3167 -0.0006 0.0115  -0.0448 92  LYS A CA  
593  C C   . LYS A 71  ? 0.2905 0.2932 0.3748 0.0030  0.0071  -0.0379 92  LYS A C   
594  O O   . LYS A 71  ? 0.2508 0.2701 0.3362 0.0029  0.0084  -0.0470 92  LYS A O   
595  C CB  . LYS A 71  ? 0.2227 0.2547 0.3320 0.0140  -0.0015 -0.0632 92  LYS A CB  
596  C CG  . LYS A 71  ? 0.2416 0.2897 0.3727 0.0270  -0.0122 -0.0879 92  LYS A CG  
597  C CD  . LYS A 71  ? 0.3862 0.4373 0.5460 0.0441  -0.0307 -0.1090 92  LYS A CD  
598  C CE  . LYS A 71  ? 0.4907 0.5519 0.6778 0.0606  -0.0471 -0.1375 92  LYS A CE  
599  N NZ  . LYS A 71  ? 0.6328 0.7030 0.8519 0.0792  -0.0675 -0.1635 92  LYS A NZ  
600  N N   . ASP A 72  ? 0.2613 0.2306 0.3431 0.0048  0.0021  -0.0223 93  ASP A N   
601  C CA  . ASP A 72  ? 0.3032 0.2528 0.3863 0.0063  -0.0031 -0.0151 93  ASP A CA  
602  C C   . ASP A 72  ? 0.2956 0.2451 0.3622 -0.0019 0.0073  -0.0045 93  ASP A C   
603  O O   . ASP A 72  ? 0.2789 0.2288 0.3472 -0.0012 0.0057  -0.0067 93  ASP A O   
604  C CB  . ASP A 72  ? 0.2893 0.2113 0.3741 0.0064  -0.0123 0.0003  93  ASP A CB  
605  C CG  . ASP A 72  ? 0.3732 0.2798 0.4763 0.0120  -0.0302 -0.0032 93  ASP A CG  
606  O OD1 . ASP A 72  ? 0.3574 0.2732 0.4745 0.0192  -0.0360 -0.0216 93  ASP A OD1 
607  O OD2 . ASP A 72  ? 0.3327 0.2185 0.4369 0.0081  -0.0408 0.0123  93  ASP A OD2 
608  N N   . LEU A 73  ? 0.2641 0.2122 0.3163 -0.0090 0.0154  0.0055  94  LEU A N   
609  C CA  . LEU A 73  ? 0.2920 0.2374 0.3311 -0.0157 0.0204  0.0146  94  LEU A CA  
610  C C   . LEU A 73  ? 0.3043 0.2735 0.3395 -0.0212 0.0226  0.0075  94  LEU A C   
611  O O   . LEU A 73  ? 0.3220 0.2909 0.3516 -0.0235 0.0222  0.0111  94  LEU A O   
612  C CB  . LEU A 73  ? 0.2928 0.2295 0.3212 -0.0216 0.0234  0.0238  94  LEU A CB  
613  C CG  . LEU A 73  ? 0.3549 0.2796 0.3735 -0.0259 0.0223  0.0337  94  LEU A CG  
614  C CD1 . LEU A 73  ? 0.3443 0.2573 0.3673 -0.0182 0.0208  0.0360  94  LEU A CD1 
615  C CD2 . LEU A 73  ? 0.3603 0.2747 0.3720 -0.0323 0.0200  0.0397  94  LEU A CD2 
616  N N   . LYS A 74  ? 0.2825 0.2787 0.3205 -0.0245 0.0251  -0.0035 95  LYS A N   
617  C CA  . LYS A 74  ? 0.2542 0.2857 0.2868 -0.0327 0.0285  -0.0114 95  LYS A CA  
618  C C   . LYS A 74  ? 0.2717 0.3141 0.3176 -0.0216 0.0236  -0.0287 95  LYS A C   
619  O O   . LYS A 74  ? 0.2576 0.3193 0.2963 -0.0265 0.0249  -0.0315 95  LYS A O   
620  C CB  . LYS A 74  ? 0.2543 0.3241 0.2894 -0.0399 0.0330  -0.0226 95  LYS A CB  
621  C CG  . LYS A 74  ? 0.2670 0.3876 0.2942 -0.0528 0.0382  -0.0309 95  LYS A CG  
622  C CD  . LYS A 74  ? 0.3770 0.4852 0.3787 -0.0727 0.0388  -0.0035 95  LYS A CD  
623  C CE  . LYS A 74  ? 0.4672 0.6291 0.4539 -0.0949 0.0436  -0.0025 95  LYS A CE  
624  N NZ  . LYS A 74  ? 0.4583 0.5939 0.4220 -0.1137 0.0380  0.0287  95  LYS A NZ  
625  N N   . ARG A 75  ? 0.2640 0.2936 0.3295 -0.0075 0.0155  -0.0402 96  ARG A N   
626  C CA  . ARG A 75  ? 0.2449 0.2793 0.3271 0.0033  0.0063  -0.0580 96  ARG A CA  
627  C C   . ARG A 75  ? 0.3024 0.3189 0.3753 -0.0001 0.0063  -0.0450 96  ARG A C   
628  O O   . ARG A 75  ? 0.2802 0.3152 0.3551 0.0012  0.0044  -0.0568 96  ARG A O   
629  C CB  . ARG A 75  ? 0.2313 0.2406 0.3357 0.0163  -0.0080 -0.0644 96  ARG A CB  
630  C CG  . ARG A 75  ? 0.2811 0.2861 0.4076 0.0280  -0.0237 -0.0830 96  ARG A CG  
631  C CD  . ARG A 75  ? 0.3061 0.2756 0.4537 0.0371  -0.0436 -0.0818 96  ARG A CD  
632  N NE  . ARG A 75  ? 0.3131 0.2468 0.4479 0.0271  -0.0425 -0.0505 96  ARG A NE  
633  C CZ  . ARG A 75  ? 0.4017 0.3168 0.5353 0.0220  -0.0461 -0.0383 96  ARG A CZ  
634  N NH1 . ARG A 75  ? 0.3813 0.2760 0.5040 0.0119  -0.0436 -0.0127 96  ARG A NH1 
635  N NH2 . ARG A 75  ? 0.3072 0.2302 0.4510 0.0263  -0.0518 -0.0537 96  ARG A NH2 
636  N N   . ILE A 76  ? 0.2560 0.2411 0.3199 -0.0040 0.0082  -0.0230 97  ILE A N   
637  C CA  . ILE A 76  ? 0.3072 0.2766 0.3645 -0.0065 0.0079  -0.0107 97  ILE A CA  
638  C C   . ILE A 76  ? 0.2596 0.2459 0.2999 -0.0150 0.0130  -0.0064 97  ILE A C   
639  O O   . ILE A 76  ? 0.3034 0.2953 0.3432 -0.0146 0.0100  -0.0093 97  ILE A O   
640  C CB  . ILE A 76  ? 0.4403 0.3837 0.4922 -0.0086 0.0100  0.0080  97  ILE A CB  
641  C CG1 . ILE A 76  ? 0.5038 0.4313 0.5690 -0.0047 0.0030  0.0099  97  ILE A CG1 
642  C CG2 . ILE A 76  ? 0.4641 0.4006 0.5080 -0.0114 0.0113  0.0182  97  ILE A CG2 
643  C CD1 . ILE A 76  ? 0.4937 0.4136 0.5714 -0.0030 -0.0061 0.0079  97  ILE A CD1 
644  N N   . THR A 77  ? 0.2834 0.2797 0.3094 -0.0247 0.0185  0.0011  98  THR A N   
645  C CA  . THR A 77  ? 0.2945 0.3025 0.3023 -0.0365 0.0191  0.0110  98  THR A CA  
646  C C   . THR A 77  ? 0.3089 0.3607 0.3142 -0.0411 0.0209  -0.0043 98  THR A C   
647  O O   . THR A 77  ? 0.2953 0.3602 0.2880 -0.0485 0.0190  0.0005  98  THR A O   
648  C CB  . THR A 77  ? 0.3795 0.3794 0.3723 -0.0496 0.0200  0.0286  98  THR A CB  
649  O OG1 . THR A 77  ? 0.3847 0.4060 0.3793 -0.0546 0.0252  0.0214  98  THR A OG1 
650  C CG2 . THR A 77  ? 0.4205 0.3823 0.4173 -0.0428 0.0168  0.0386  98  THR A CG2 
651  N N   . ASP A 78  ? 0.2479 0.3256 0.2671 -0.0352 0.0230  -0.0257 99  ASP A N   
652  C CA  . ASP A 78  ? 0.2726 0.4011 0.2947 -0.0358 0.0241  -0.0488 99  ASP A CA  
653  C C   . ASP A 78  ? 0.2633 0.3885 0.3000 -0.0223 0.0162  -0.0655 99  ASP A C   
654  O O   . ASP A 78  ? 0.2587 0.4263 0.2969 -0.0219 0.0157  -0.0861 99  ASP A O   
655  C CB  . ASP A 78  ? 0.2690 0.4310 0.3079 -0.0298 0.0261  -0.0734 99  ASP A CB  
656  C CG  . ASP A 78  ? 0.3953 0.5860 0.4193 -0.0478 0.0350  -0.0641 99  ASP A CG  
657  O OD1 . ASP A 78  ? 0.3400 0.5288 0.3390 -0.0678 0.0382  -0.0385 99  ASP A OD1 
658  O OD2 . ASP A 78  ? 0.3264 0.5407 0.3661 -0.0418 0.0363  -0.0831 99  ASP A OD2 
659  N N   . SER A 79  ? 0.2625 0.3420 0.3110 -0.0124 0.0095  -0.0581 100 SER A N   
660  C CA  . SER A 79  ? 0.2949 0.3674 0.3616 -0.0009 -0.0009 -0.0737 100 SER A CA  
661  C C   . SER A 79  ? 0.3334 0.4146 0.3871 -0.0066 -0.0010 -0.0684 100 SER A C   
662  O O   . SER A 79  ? 0.3102 0.3931 0.3405 -0.0191 0.0047  -0.0477 100 SER A O   
663  C CB  . SER A 79  ? 0.2502 0.2751 0.3315 0.0058  -0.0087 -0.0627 100 SER A CB  
664  O OG  . SER A 79  ? 0.2760 0.2783 0.3425 -0.0018 -0.0042 -0.0376 100 SER A OG  
665  N N   A ASP A 80  ? 0.2572 0.3409 0.3277 0.0027  -0.0107 -0.0868 101 ASP A N   
666  N N   B ASP A 80  ? 0.2571 0.3403 0.3273 0.0026  -0.0106 -0.0863 101 ASP A N   
667  C CA  A ASP A 80  ? 0.3173 0.4079 0.3788 -0.0008 -0.0131 -0.0841 101 ASP A CA  
668  C CA  B ASP A 80  ? 0.3081 0.3988 0.3683 -0.0015 -0.0125 -0.0828 101 ASP A CA  
669  C C   A ASP A 80  ? 0.3143 0.3616 0.3820 0.0004  -0.0181 -0.0658 101 ASP A C   
670  C C   B ASP A 80  ? 0.3293 0.3775 0.3916 -0.0018 -0.0160 -0.0614 101 ASP A C   
671  O O   A ASP A 80  ? 0.3037 0.3515 0.3729 0.0007  -0.0234 -0.0671 101 ASP A O   
672  O O   B ASP A 80  ? 0.2749 0.3249 0.3304 -0.0045 -0.0186 -0.0561 101 ASP A O   
673  C CB  A ASP A 80  ? 0.3652 0.4893 0.4428 0.0084  -0.0216 -0.1183 101 ASP A CB  
674  C CB  B ASP A 80  ? 0.3576 0.4762 0.4358 0.0085  -0.0222 -0.1160 101 ASP A CB  
675  C CG  A ASP A 80  ? 0.4897 0.5876 0.6018 0.0234  -0.0369 -0.1373 101 ASP A CG  
676  C CG  B ASP A 80  ? 0.3899 0.5666 0.4652 0.0084  -0.0176 -0.1419 101 ASP A CG  
677  O OD1 A ASP A 80  ? 0.5530 0.6156 0.6746 0.0254  -0.0393 -0.1252 101 ASP A OD1 
678  O OD1 B ASP A 80  ? 0.3442 0.5481 0.3920 -0.0070 -0.0061 -0.1267 101 ASP A OD1 
679  O OD2 A ASP A 80  ? 0.5645 0.6770 0.6946 0.0325  -0.0488 -0.1644 101 ASP A OD2 
680  O OD2 B ASP A 80  ? 0.4388 0.6351 0.5402 0.0229  -0.0272 -0.1773 101 ASP A OD2 
681  N N   . LEU A 81  ? 0.2992 0.3149 0.3707 0.0003  -0.0162 -0.0500 102 LEU A N   
682  C CA  . LEU A 81  ? 0.3141 0.3001 0.3920 -0.0006 -0.0195 -0.0343 102 LEU A CA  
683  C C   . LEU A 81  ? 0.3038 0.2874 0.3643 -0.0063 -0.0146 -0.0161 102 LEU A C   
684  O O   . LEU A 81  ? 0.3100 0.2952 0.3534 -0.0110 -0.0086 -0.0051 102 LEU A O   
685  C CB  . LEU A 81  ? 0.2756 0.2365 0.3623 -0.0005 -0.0196 -0.0239 102 LEU A CB  
686  C CG  . LEU A 81  ? 0.3233 0.2776 0.4305 0.0058  -0.0302 -0.0389 102 LEU A CG  
687  C CD1 . LEU A 81  ? 0.3171 0.2482 0.4276 0.0032  -0.0309 -0.0239 102 LEU A CD1 
688  C CD2 . LEU A 81  ? 0.3649 0.3128 0.4929 0.0090  -0.0454 -0.0512 102 LEU A CD2 
689  N N   . LYS A 82  ? 0.2602 0.2376 0.3278 -0.0058 -0.0196 -0.0131 103 LYS A N   
690  C CA  . LYS A 82  ? 0.2682 0.2422 0.3242 -0.0080 -0.0184 0.0014  103 LYS A CA  
691  C C   . LYS A 82  ? 0.2605 0.2231 0.3313 -0.0069 -0.0200 0.0075  103 LYS A C   
692  O O   . LYS A 82  ? 0.2970 0.2552 0.3847 -0.0082 -0.0232 0.0035  103 LYS A O   
693  C CB  . LYS A 82  ? 0.3401 0.3323 0.3852 -0.0096 -0.0237 -0.0021 103 LYS A CB  
694  C CG  . LYS A 82  ? 0.4282 0.4433 0.4521 -0.0161 -0.0210 -0.0041 103 LYS A CG  
695  C CD  . LYS A 82  ? 0.5985 0.6315 0.6057 -0.0215 -0.0276 0.0002  103 LYS A CD  
696  C CE  . LYS A 82  ? 0.6568 0.7221 0.6413 -0.0330 -0.0247 0.0001  103 LYS A CE  
697  N N   . GLY A 83  ? 0.2688 0.2614 0.3665 -0.0678 -0.0117 -0.0074 104 GLY A N   
698  C CA  . GLY A 83  ? 0.2835 0.2387 0.3890 -0.0544 -0.0080 -0.0141 104 GLY A CA  
699  C C   . GLY A 83  ? 0.2939 0.2497 0.3984 -0.0384 0.0021  -0.0193 104 GLY A C   
700  O O   . GLY A 83  ? 0.2886 0.2557 0.3878 -0.0371 0.0017  -0.0196 104 GLY A O   
701  N N   . GLU A 84  ? 0.2879 0.2357 0.3967 -0.0311 0.0085  -0.0188 105 GLU A N   
702  C CA  . GLU A 84  ? 0.2828 0.2410 0.3888 -0.0264 0.0131  -0.0151 105 GLU A CA  
703  C C   . GLU A 84  ? 0.2627 0.2239 0.3627 -0.0221 0.0101  -0.0119 105 GLU A C   
704  O O   . GLU A 84  ? 0.2713 0.2428 0.3660 -0.0223 0.0111  -0.0089 105 GLU A O   
705  C CB  . GLU A 84  ? 0.2748 0.2315 0.3858 -0.0295 0.0134  -0.0055 105 GLU A CB  
706  C CG  . GLU A 84  ? 0.3897 0.3632 0.5087 -0.0295 0.0170  -0.0154 105 GLU A CG  
707  C CD  . GLU A 84  ? 0.4928 0.4839 0.6153 -0.0381 0.0183  -0.0005 105 GLU A CD  
708  O OE1 . GLU A 84  ? 0.3877 0.3516 0.5153 -0.0403 0.0142  0.0057  105 GLU A OE1 
709  O OE2 . GLU A 84  ? 0.5392 0.5748 0.6580 -0.0464 0.0209  0.0085  105 GLU A OE2 
710  N N   . LEU A 85  ? 0.2683 0.2260 0.3709 -0.0155 0.0032  -0.0171 106 LEU A N   
711  C CA  . LEU A 85  ? 0.3133 0.2792 0.4150 -0.0046 -0.0064 -0.0246 106 LEU A CA  
712  C C   . LEU A 85  ? 0.2534 0.2447 0.3484 -0.0073 0.0012  -0.0285 106 LEU A C   
713  O O   . LEU A 85  ? 0.2782 0.2711 0.3706 -0.0020 -0.0035 -0.0298 106 LEU A O   
714  C CB  . LEU A 85  ? 0.2954 0.2714 0.4048 0.0110  -0.0190 -0.0424 106 LEU A CB  
715  C CG  . LEU A 85  ? 0.3811 0.3191 0.4991 0.0188  -0.0414 -0.0391 106 LEU A CG  
716  C CD1 . LEU A 85  ? 0.3530 0.3080 0.4811 0.0418  -0.0573 -0.0671 106 LEU A CD1 
717  C CD2 . LEU A 85  ? 0.3624 0.2733 0.4822 0.0202  -0.0669 -0.0300 106 LEU A CD2 
718  N N   . PHE A 86  ? 0.2441 0.2517 0.3365 -0.0188 0.0067  -0.0271 107 PHE A N   
719  C CA  . PHE A 86  ? 0.2413 0.2687 0.3276 -0.0275 0.0063  -0.0238 107 PHE A CA  
720  C C   . PHE A 86  ? 0.2425 0.2494 0.3254 -0.0258 0.0072  -0.0203 107 PHE A C   
721  O O   . PHE A 86  ? 0.2608 0.2756 0.3389 -0.0233 0.0070  -0.0205 107 PHE A O   
722  C CB  . PHE A 86  ? 0.2611 0.3005 0.3460 -0.0493 -0.0017 -0.0138 107 PHE A CB  
723  C CG  . PHE A 86  ? 0.2874 0.3405 0.3668 -0.0650 -0.0130 -0.0029 107 PHE A CG  
724  C CD1 . PHE A 86  ? 0.2496 0.3602 0.3245 -0.0746 -0.0129 0.0007  107 PHE A CD1 
725  C CD2 . PHE A 86  ? 0.3017 0.3174 0.3824 -0.0701 -0.0299 0.0018  107 PHE A CD2 
726  C CE1 . PHE A 86  ? 0.2298 0.3566 0.2991 -0.0960 -0.0281 0.0182  107 PHE A CE1 
727  C CE2 . PHE A 86  ? 0.2788 0.2972 0.3558 -0.0856 -0.0508 0.0143  107 PHE A CE2 
728  C CZ  . PHE A 86  ? 0.2899 0.3607 0.3600 -0.1030 -0.0503 0.0280  107 PHE A CZ  
729  N N   . ILE A 87  ? 0.2258 0.2151 0.3122 -0.0258 0.0075  -0.0207 108 ILE A N   
730  C CA  . ILE A 87  ? 0.2331 0.2249 0.3175 -0.0203 0.0076  -0.0253 108 ILE A CA  
731  C C   . ILE A 87  ? 0.2459 0.2475 0.3242 -0.0177 0.0144  -0.0191 108 ILE A C   
732  O O   . ILE A 87  ? 0.2901 0.3021 0.3624 -0.0154 0.0146  -0.0206 108 ILE A O   
733  C CB  . ILE A 87  ? 0.2392 0.2335 0.3321 -0.0158 0.0054  -0.0357 108 ILE A CB  
734  C CG1 . ILE A 87  ? 0.2716 0.2433 0.3722 -0.0196 -0.0150 -0.0423 108 ILE A CG1 
735  C CG2 . ILE A 87  ? 0.2874 0.3112 0.3795 -0.0050 0.0047  -0.0499 108 ILE A CG2 
736  C CD1 . ILE A 87  ? 0.3139 0.2828 0.4280 -0.0115 -0.0242 -0.0592 108 ILE A CD1 
737  N N   . LYS A 88  ? 0.2836 0.2781 0.3642 -0.0200 0.0133  -0.0105 109 LYS A N   
738  C CA  . LYS A 88  ? 0.3110 0.3050 0.3872 -0.0250 0.0057  0.0024  109 LYS A CA  
739  C C   . LYS A 88  ? 0.2897 0.2774 0.3628 -0.0181 -0.0008 -0.0027 109 LYS A C   
740  O O   . LYS A 88  ? 0.3157 0.3088 0.3816 -0.0225 -0.0034 0.0039  109 LYS A O   
741  C CB  . LYS A 88  ? 0.2680 0.2414 0.3506 -0.0290 -0.0095 0.0134  109 LYS A CB  
742  C CG  . LYS A 88  ? 0.3317 0.2969 0.4109 -0.0439 -0.0323 0.0362  109 LYS A CG  
743  C CD  . LYS A 88  ? 0.5278 0.4575 0.6162 -0.0482 -0.0638 0.0490  109 LYS A CD  
744  C CE  . LYS A 88  ? 0.7298 0.6798 0.8156 -0.0757 -0.0667 0.0791  109 LYS A CE  
745  N NZ  . LYS A 88  ? 0.7616 0.7471 0.8359 -0.1054 -0.0746 0.1082  109 LYS A NZ  
746  N N   . GLU A 89  ? 0.2556 0.2427 0.3342 -0.0079 -0.0037 -0.0158 110 GLU A N   
747  C CA  . GLU A 89  ? 0.2842 0.2803 0.3629 0.0013  -0.0106 -0.0259 110 GLU A CA  
748  C C   . GLU A 89  ? 0.2930 0.3031 0.3632 -0.0042 0.0005  -0.0234 110 GLU A C   
749  O O   . GLU A 89  ? 0.2643 0.2754 0.3313 -0.0011 -0.0037 -0.0244 110 GLU A O   
750  C CB  . GLU A 89  ? 0.2607 0.2833 0.3486 0.0145  -0.0158 -0.0461 110 GLU A CB  
751  C CG  . GLU A 89  ? 0.2745 0.3281 0.3657 0.0272  -0.0233 -0.0638 110 GLU A CG  
752  C CD  . GLU A 89  ? 0.3547 0.3758 0.4518 0.0401  -0.0491 -0.0702 110 GLU A CD  
753  O OE1 . GLU A 89  ? 0.3999 0.3773 0.4993 0.0368  -0.0680 -0.0588 110 GLU A OE1 
754  O OE2 . GLU A 89  ? 0.3285 0.3697 0.4289 0.0509  -0.0561 -0.0851 110 GLU A OE2 
755  N N   . LEU A 90  ? 0.2394 0.2546 0.3079 -0.0117 0.0072  -0.0209 111 LEU A N   
756  C CA  . LEU A 90  ? 0.2424 0.2598 0.3054 -0.0153 0.0054  -0.0191 111 LEU A CA  
757  C C   . LEU A 90  ? 0.2644 0.2774 0.3210 -0.0111 0.0075  -0.0186 111 LEU A C   
758  O O   . LEU A 90  ? 0.2788 0.2930 0.3299 -0.0094 0.0050  -0.0183 111 LEU A O   
759  C CB  . LEU A 90  ? 0.2516 0.2617 0.3179 -0.0224 -0.0031 -0.0187 111 LEU A CB  
760  C CG  . LEU A 90  ? 0.2739 0.2738 0.3385 -0.0231 -0.0198 -0.0199 111 LEU A CG  
761  C CD1 . LEU A 90  ? 0.2492 0.2610 0.3093 -0.0353 -0.0288 -0.0074 111 LEU A CD1 
762  C CD2 . LEU A 90  ? 0.2887 0.2690 0.3622 -0.0286 -0.0428 -0.0228 111 LEU A CD2 
763  N N   . LEU A 91  ? 0.2620 0.2804 0.3186 -0.0120 0.0118  -0.0173 112 LEU A N   
764  C CA  . LEU A 91  ? 0.2745 0.3140 0.3233 -0.0135 0.0141  -0.0154 112 LEU A CA  
765  C C   . LEU A 91  ? 0.2689 0.2982 0.3117 -0.0207 0.0083  -0.0015 112 LEU A C   
766  O O   . LEU A 91  ? 0.2703 0.3084 0.3046 -0.0225 0.0071  0.0012  112 LEU A O   
767  C CB  . LEU A 91  ? 0.2407 0.3128 0.2909 -0.0192 0.0191  -0.0137 112 LEU A CB  
768  C CG  . LEU A 91  ? 0.3223 0.4463 0.3628 -0.0282 0.0220  -0.0082 112 LEU A CG  
769  C CD1 . LEU A 91  ? 0.3451 0.4888 0.3820 -0.0118 0.0215  -0.0299 112 LEU A CD1 
770  C CD2 . LEU A 91  ? 0.3802 0.5592 0.4242 -0.0360 0.0275  -0.0079 112 LEU A CD2 
771  N N   . TRP A 92  ? 0.2546 0.2628 0.3033 -0.0232 -0.0019 0.0052  113 TRP A N   
772  C CA  . TRP A 92  ? 0.2753 0.2634 0.3231 -0.0271 -0.0217 0.0138  113 TRP A CA  
773  C C   . TRP A 92  ? 0.2732 0.2571 0.3214 -0.0143 -0.0219 0.0002  113 TRP A C   
774  O O   . TRP A 92  ? 0.2853 0.2593 0.3290 -0.0177 -0.0335 0.0058  113 TRP A O   
775  C CB  . TRP A 92  ? 0.3500 0.3114 0.4099 -0.0233 -0.0440 0.0132  113 TRP A CB  
776  C CG  . TRP A 92  ? 0.3518 0.3055 0.4106 -0.0443 -0.0612 0.0383  113 TRP A CG  
777  C CD1 . TRP A 92  ? 0.4919 0.4724 0.5386 -0.0716 -0.0615 0.0652  113 TRP A CD1 
778  C CD2 . TRP A 92  ? 0.4029 0.3253 0.4735 -0.0436 -0.0895 0.0422  113 TRP A CD2 
779  N NE1 . TRP A 92  ? 0.5369 0.5068 0.5862 -0.0949 -0.0891 0.0929  113 TRP A NE1 
780  C CE2 . TRP A 92  ? 0.5418 0.4664 0.6063 -0.0764 -0.1090 0.0790  113 TRP A CE2 
781  C CE3 . TRP A 92  ? 0.4700 0.3712 0.5558 -0.0188 -0.1038 0.0174  113 TRP A CE3 
782  C CZ2 . TRP A 92  ? 0.6119 0.5035 0.6858 -0.0869 -0.1458 0.0961  113 TRP A CZ2 
783  C CZ3 . TRP A 92  ? 0.4017 0.2681 0.4980 -0.0217 -0.1405 0.0264  113 TRP A CZ3 
784  C CH2 . TRP A 92  ? 0.5427 0.3973 0.6331 -0.0566 -0.1629 0.0677  113 TRP A CH2 
785  N N   . MET A 93  ? 0.2716 0.2680 0.3250 -0.0040 -0.0120 -0.0142 114 MET A N   
786  C CA  . MET A 93  ? 0.2747 0.2838 0.3285 0.0027  -0.0117 -0.0230 114 MET A CA  
787  C C   . MET A 93  ? 0.3080 0.3142 0.3502 -0.0026 -0.0062 -0.0151 114 MET A C   
788  O O   . MET A 93  ? 0.2829 0.2858 0.3220 -0.0002 -0.0111 -0.0156 114 MET A O   
789  C CB  . MET A 93  ? 0.2323 0.2720 0.2913 0.0027  -0.0056 -0.0301 114 MET A CB  
790  C CG  . MET A 93  ? 0.2432 0.3150 0.3020 0.0017  -0.0070 -0.0330 114 MET A CG  
791  S SD  . MET A 93  ? 0.2894 0.3449 0.3368 -0.0115 -0.0078 -0.0157 114 MET A SD  
792  C CE  . MET A 93  ? 0.2935 0.3578 0.3436 -0.0275 -0.0129 -0.0064 114 MET A CE  
793  N N   . LEU A 94  ? 0.2631 0.2733 0.3008 -0.0061 0.0006  -0.0128 115 LEU A N   
794  C CA  . LEU A 94  ? 0.2622 0.2756 0.2916 -0.0038 0.0000  -0.0143 115 LEU A CA  
795  C C   . LEU A 94  ? 0.3198 0.3384 0.3395 -0.0093 -0.0002 -0.0064 115 LEU A C   
796  O O   . LEU A 94  ? 0.3109 0.3289 0.3231 -0.0074 -0.0026 -0.0064 115 LEU A O   
797  C CB  . LEU A 94  ? 0.2548 0.2785 0.2863 0.0017  -0.0016 -0.0250 115 LEU A CB  
798  C CG  . LEU A 94  ? 0.3434 0.3526 0.3835 0.0003  -0.0134 -0.0266 115 LEU A CG  
799  C CD1 . LEU A 94  ? 0.3276 0.3406 0.3747 0.0083  -0.0211 -0.0416 115 LEU A CD1 
800  C CD2 . LEU A 94  ? 0.3744 0.3707 0.4128 -0.0014 -0.0313 -0.0229 115 LEU A CD2 
801  N N   . ARG A 95  ? 0.2702 0.2954 0.2894 -0.0208 -0.0018 0.0047  116 ARG A N   
802  C CA  . ARG A 95  ? 0.2910 0.3256 0.2997 -0.0381 -0.0106 0.0226  116 ARG A CA  
803  C C   . ARG A 95  ? 0.3043 0.3004 0.3155 -0.0379 -0.0289 0.0267  116 ARG A C   
804  O O   . ARG A 95  ? 0.3242 0.3191 0.3260 -0.0475 -0.0371 0.0367  116 ARG A O   
805  C CB  . ARG A 95  ? 0.3052 0.3557 0.3135 -0.0593 -0.0184 0.0425  116 ARG A CB  
806  C CG  . ARG A 95  ? 0.4446 0.5524 0.4512 -0.0600 -0.0009 0.0356  116 ARG A CG  
807  C CD  . ARG A 95  ? 0.5573 0.7288 0.5519 -0.0637 0.0071  0.0312  116 ARG A CD  
808  N NE  . ARG A 95  ? 0.6114 0.8452 0.6104 -0.0492 0.0201  0.0058  116 ARG A NE  
809  C CZ  . ARG A 95  ? 0.5844 0.8798 0.5846 -0.0632 0.0246  0.0119  116 ARG A CZ  
810  N NH1 . ARG A 95  ? 0.6289 0.9247 0.6246 -0.0981 0.0146  0.0507  116 ARG A NH1 
811  N NH2 . ARG A 95  ? 0.4772 0.8346 0.4854 -0.0414 0.0328  -0.0226 116 ARG A NH2 
812  N N   . HIS A 96  ? 0.3014 0.2731 0.3266 -0.0257 -0.0383 0.0157  117 HIS A N   
813  C CA  . HIS A 96  ? 0.3153 0.2615 0.3488 -0.0163 -0.0597 0.0068  117 HIS A CA  
814  C C   . HIS A 96  ? 0.3024 0.2578 0.3315 -0.0072 -0.0479 -0.0021 117 HIS A C   
815  O O   . HIS A 96  ? 0.3239 0.2625 0.3516 -0.0075 -0.0624 -0.0012 117 HIS A O   
816  C CB  . HIS A 96  ? 0.3125 0.2566 0.3646 0.0028  -0.0704 -0.0152 117 HIS A CB  
817  C CG  . HIS A 96  ? 0.3508 0.2877 0.4168 0.0220  -0.0947 -0.0383 117 HIS A CG  
818  N ND1 . HIS A 96  ? 0.3918 0.2884 0.4614 0.0188  -0.1322 -0.0341 117 HIS A ND1 
819  C CD2 . HIS A 96  ? 0.3743 0.3488 0.4523 0.0433  -0.0900 -0.0667 117 HIS A CD2 
820  C CE1 . HIS A 96  ? 0.4428 0.3463 0.5291 0.0442  -0.1506 -0.0660 117 HIS A CE1 
821  N NE2 . HIS A 96  ? 0.4617 0.4215 0.5529 0.0595  -0.1226 -0.0869 117 HIS A NE2 
822  N N   . GLN A 97  ? 0.2792 0.2567 0.3073 -0.0015 -0.0279 -0.0087 118 GLN A N   
823  C CA  . GLN A 97  ? 0.3101 0.2934 0.3343 0.0026  -0.0239 -0.0113 118 GLN A CA  
824  C C   . GLN A 97  ? 0.3232 0.2979 0.3327 -0.0033 -0.0231 -0.0019 118 GLN A C   
825  O O   . GLN A 97  ? 0.3354 0.3021 0.3412 -0.0009 -0.0273 -0.0017 118 GLN A O   
826  C CB  . GLN A 97  ? 0.2658 0.2686 0.2923 0.0022  -0.0161 -0.0125 118 GLN A CB  
827  C CG  . GLN A 97  ? 0.2864 0.3213 0.3257 0.0045  -0.0172 -0.0213 118 GLN A CG  
828  C CD  . GLN A 97  ? 0.2951 0.3503 0.3416 0.0130  -0.0247 -0.0328 118 GLN A CD  
829  O OE1 . GLN A 97  ? 0.3038 0.3528 0.3448 0.0109  -0.0271 -0.0271 118 GLN A OE1 
830  N NE2 . GLN A 97  ? 0.2536 0.3343 0.3143 0.0264  -0.0323 -0.0540 118 GLN A NE2 
831  N N   . LYS A 98  ? 0.3111 0.2994 0.3125 -0.0105 -0.0174 0.0038  119 LYS A N   
832  C CA  . LYS A 98  ? 0.3033 0.3073 0.2903 -0.0164 -0.0166 0.0090  119 LYS A CA  
833  C C   . LYS A 98  ? 0.3658 0.3516 0.3474 -0.0318 -0.0319 0.0252  119 LYS A C   
834  O O   . LYS A 98  ? 0.3681 0.3522 0.3400 -0.0338 -0.0349 0.0283  119 LYS A O   
835  C CB  . LYS A 98  ? 0.3422 0.3913 0.3236 -0.0216 -0.0083 0.0078  119 LYS A CB  
836  C CG  . LYS A 98  ? 0.4316 0.5252 0.3986 -0.0223 -0.0061 0.0035  119 LYS A CG  
837  C CD  . LYS A 98  ? 0.5290 0.6851 0.4973 -0.0126 0.0017  -0.0162 119 LYS A CD  
838  C CE  . LYS A 98  ? 0.6028 0.8370 0.5562 -0.0270 0.0053  -0.0121 119 LYS A CE  
839  N NZ  . LYS A 98  ? 0.6770 0.9942 0.6348 -0.0159 0.0125  -0.0370 119 LYS A NZ  
840  N N   A ASP A 99  ? 0.3350 0.3015 0.3240 -0.0427 -0.0488 0.0354  120 ASP A N   
841  N N   B ASP A 99  ? 0.3341 0.3003 0.3236 -0.0419 -0.0484 0.0346  120 ASP A N   
842  C CA  A ASP A 99  ? 0.4087 0.3434 0.3966 -0.0583 -0.0793 0.0508  120 ASP A CA  
843  C CA  B ASP A 99  ? 0.4062 0.3405 0.3952 -0.0572 -0.0790 0.0498  120 ASP A CA  
844  C C   A ASP A 99  ? 0.3817 0.2877 0.3784 -0.0388 -0.0868 0.0332  120 ASP A C   
845  C C   B ASP A 99  ? 0.3824 0.2874 0.3807 -0.0380 -0.0878 0.0323  120 ASP A C   
846  O O   A ASP A 99  ? 0.4032 0.2896 0.3938 -0.0476 -0.1032 0.0419  120 ASP A O   
847  O O   B ASP A 99  ? 0.3983 0.2814 0.3916 -0.0470 -0.1066 0.0410  120 ASP A O   
848  C CB  A ASP A 99  ? 0.4032 0.3083 0.4032 -0.0687 -0.1122 0.0604  120 ASP A CB  
849  C CB  B ASP A 99  ? 0.4163 0.3258 0.4171 -0.0669 -0.1080 0.0587  120 ASP A CB  
850  C CG  A ASP A 99  ? 0.4066 0.3416 0.3970 -0.0986 -0.1138 0.0883  120 ASP A CG  
851  C CG  B ASP A 99  ? 0.5018 0.3713 0.5024 -0.0906 -0.1557 0.0811  120 ASP A CG  
852  O OD1 A ASP A 99  ? 0.4381 0.4248 0.4105 -0.1189 -0.0981 0.1046  120 ASP A OD1 
853  O OD1 B ASP A 99  ? 0.6407 0.5229 0.6240 -0.1153 -0.1591 0.1039  120 ASP A OD1 
854  O OD2 A ASP A 99  ? 0.4463 0.3602 0.4485 -0.1014 -0.1343 0.0924  120 ASP A OD2 
855  O OD2 B ASP A 99  ? 0.6094 0.4351 0.6281 -0.0850 -0.1960 0.0755  120 ASP A OD2 
856  N N   A ILE A 100 ? 0.3722 0.2844 0.3833 -0.0156 -0.0765 0.0101  121 ILE A N   
857  N N   B ILE A 100 ? 0.3635 0.2767 0.3751 -0.0148 -0.0756 0.0093  121 ILE A N   
858  C CA  A ILE A 100 ? 0.3372 0.2457 0.3585 0.0017  -0.0819 -0.0080 121 ILE A CA  
859  C CA  B ILE A 100 ? 0.3563 0.2664 0.3778 0.0021  -0.0807 -0.0085 121 ILE A CA  
860  C C   A ILE A 100 ? 0.3714 0.2840 0.3780 -0.0016 -0.0671 0.0002  121 ILE A C   
861  C C   B ILE A 100 ? 0.3652 0.2781 0.3719 -0.0015 -0.0671 0.0000  121 ILE A C   
862  O O   A ILE A 100 ? 0.3406 0.2360 0.3470 0.0002  -0.0790 -0.0011 121 ILE A O   
863  O O   B ILE A 100 ? 0.3529 0.2482 0.3597 0.0002  -0.0794 -0.0013 121 ILE A O   
864  C CB  A ILE A 100 ? 0.3463 0.2901 0.3832 0.0195  -0.0714 -0.0298 121 ILE A CB  
865  C CB  B ILE A 100 ? 0.3317 0.2780 0.3679 0.0192  -0.0690 -0.0293 121 ILE A CB  
866  C CG1 A ILE A 100 ? 0.3796 0.3195 0.4349 0.0317  -0.0945 -0.0484 121 ILE A CG1 
867  C CG1 B ILE A 100 ? 0.3704 0.3164 0.4247 0.0311  -0.0892 -0.0476 121 ILE A CG1 
868  C CG2 A ILE A 100 ? 0.3962 0.3655 0.4399 0.0305  -0.0697 -0.0430 121 ILE A CG2 
869  C CG2 B ILE A 100 ? 0.3879 0.3580 0.4312 0.0302  -0.0689 -0.0426 121 ILE A CG2 
870  C CD1 A ILE A 100 ? 0.3960 0.3868 0.4638 0.0454  -0.0821 -0.0686 121 ILE A CD1 
871  C CD1 B ILE A 100 ? 0.3732 0.2925 0.4434 0.0451  -0.1289 -0.0668 121 ILE A CD1 
872  N N   . PHE A 101 ? 0.3291 0.2616 0.3255 -0.0036 -0.0471 0.0050  122 PHE A N   
873  C CA  . PHE A 101 ? 0.3836 0.3165 0.3676 -0.0019 -0.0419 0.0080  122 PHE A CA  
874  C C   . PHE A 101 ? 0.4024 0.3253 0.3724 -0.0146 -0.0506 0.0199  122 PHE A C   
875  O O   . PHE A 101 ? 0.3843 0.2916 0.3489 -0.0130 -0.0563 0.0214  122 PHE A O   
876  C CB  . PHE A 101 ? 0.3383 0.2914 0.3171 0.0034  -0.0324 0.0034  122 PHE A CB  
877  C CG  . PHE A 101 ? 0.3655 0.3165 0.3338 0.0116  -0.0375 -0.0006 122 PHE A CG  
878  C CD1 . PHE A 101 ? 0.4006 0.3743 0.3548 0.0098  -0.0356 -0.0024 122 PHE A CD1 
879  C CD2 . PHE A 101 ? 0.4252 0.3585 0.3983 0.0184  -0.0483 -0.0007 122 PHE A CD2 
880  C CE1 . PHE A 101 ? 0.4566 0.4323 0.4023 0.0220  -0.0433 -0.0118 122 PHE A CE1 
881  C CE2 . PHE A 101 ? 0.4414 0.3640 0.4064 0.0282  -0.0605 -0.0054 122 PHE A CE2 
882  C CZ  . PHE A 101 ? 0.4123 0.3542 0.3644 0.0335  -0.0574 -0.0143 122 PHE A CZ  
883  N N   . ASN A 102 ? 0.3501 0.2868 0.3130 -0.0325 -0.0541 0.0327  123 ASN A N   
884  C CA  . ASN A 102 ? 0.3770 0.3191 0.3237 -0.0556 -0.0662 0.0523  123 ASN A CA  
885  C C   . ASN A 102 ? 0.4266 0.3178 0.3795 -0.0620 -0.0947 0.0592  123 ASN A C   
886  O O   . ASN A 102 ? 0.4584 0.3417 0.3993 -0.0729 -0.1035 0.0696  123 ASN A O   
887  C CB  . ASN A 102 ? 0.4555 0.4350 0.3934 -0.0842 -0.0709 0.0736  123 ASN A CB  
888  C CG  . ASN A 102 ? 0.5909 0.6366 0.5222 -0.0758 -0.0452 0.0609  123 ASN A CG  
889  O OD1 . ASN A 102 ? 0.5012 0.5569 0.4328 -0.0495 -0.0319 0.0368  123 ASN A OD1 
890  N ND2 . ASN A 102 ? 0.5118 0.6029 0.4394 -0.0970 -0.0447 0.0751  123 ASN A ND2 
891  N N   . ASN A 103 ? 0.4333 0.2931 0.4065 -0.0526 -0.1133 0.0491  124 ASN A N   
892  C CA  . ASN A 103 ? 0.4692 0.2820 0.4556 -0.0491 -0.1493 0.0432  124 ASN A CA  
893  C C   . ASN A 103 ? 0.4617 0.2729 0.4511 -0.0283 -0.1370 0.0258  124 ASN A C   
894  O O   . ASN A 103 ? 0.4740 0.2539 0.4631 -0.0321 -0.1591 0.0282  124 ASN A O   
895  C CB  . ASN A 103 ? 0.5018 0.2960 0.5147 -0.0311 -0.1749 0.0210  124 ASN A CB  
896  C CG  . ASN A 103 ? 0.6600 0.4396 0.6729 -0.0540 -0.2016 0.0418  124 ASN A CG  
897  O OD1 . ASN A 103 ? 0.6866 0.4645 0.6813 -0.0906 -0.2142 0.0777  124 ASN A OD1 
898  N ND2 . ASN A 103 ? 0.7235 0.5002 0.7565 -0.0347 -0.2130 0.0206  124 ASN A ND2 
899  N N   . LEU A 104 ? 0.3983 0.2411 0.3924 -0.0094 -0.1082 0.0106  125 LEU A N   
900  C CA  . LEU A 104 ? 0.4068 0.2555 0.4019 0.0031  -0.0987 0.0026  125 LEU A CA  
901  C C   . LEU A 104 ? 0.4675 0.3049 0.4410 -0.0070 -0.0931 0.0186  125 LEU A C   
902  O O   . LEU A 104 ? 0.4461 0.2648 0.4190 -0.0039 -0.1012 0.0180  125 LEU A O   
903  C CB  . LEU A 104 ? 0.3379 0.2258 0.3388 0.0133  -0.0769 -0.0046 125 LEU A CB  
904  C CG  . LEU A 104 ? 0.4136 0.3346 0.4368 0.0257  -0.0808 -0.0254 125 LEU A CG  
905  C CD1 . LEU A 104 ? 0.3836 0.3474 0.4074 0.0227  -0.0626 -0.0211 125 LEU A CD1 
906  C CD2 . LEU A 104 ? 0.3991 0.3336 0.4390 0.0397  -0.0964 -0.0456 125 LEU A CD2 
907  N N   . ALA A 105 ? 0.4017 0.2594 0.3587 -0.0162 -0.0798 0.0287  126 ALA A N   
908  C CA  . ALA A 105 ? 0.4049 0.2699 0.3419 -0.0215 -0.0764 0.0363  126 ALA A CA  
909  C C   . ALA A 105 ? 0.4747 0.3201 0.4012 -0.0442 -0.0962 0.0539  126 ALA A C   
910  O O   . ALA A 105 ? 0.5096 0.3429 0.4256 -0.0449 -0.1002 0.0573  126 ALA A O   
911  C CB  . ALA A 105 ? 0.4475 0.3602 0.3729 -0.0214 -0.0616 0.0331  126 ALA A CB  
912  N N   . ARG A 106 ? 0.4672 0.3051 0.3964 -0.0658 -0.1151 0.0682  127 ARG A N   
913  C CA  . ARG A 106 ? 0.5169 0.3287 0.4378 -0.0964 -0.1480 0.0924  127 ARG A CA  
914  C C   . ARG A 106 ? 0.5866 0.3401 0.5232 -0.0821 -0.1719 0.0798  127 ARG A C   
915  O O   . ARG A 106 ? 0.5758 0.3075 0.5015 -0.0965 -0.1879 0.0928  127 ARG A O   
916  C CB  . ARG A 106 ? 0.5021 0.3106 0.4262 -0.1255 -0.1760 0.1143  127 ARG A CB  
917  C CG  . ARG A 106 ? 0.7050 0.4778 0.6226 -0.1674 -0.2273 0.1485  127 ARG A CG  
918  C CD  . ARG A 106 ? 0.8077 0.5799 0.7283 -0.2011 -0.2612 0.1766  127 ARG A CD  
919  N N   . GLN A 107 ? 0.6103 0.3502 0.5726 -0.0530 -0.1736 0.0521  128 GLN A N   
920  C CA  . GLN A 107 ? 0.5985 0.3055 0.5800 -0.0336 -0.1947 0.0311  128 GLN A CA  
921  C C   . GLN A 107 ? 0.5590 0.2739 0.5296 -0.0249 -0.1712 0.0307  128 GLN A C   
922  O O   . GLN A 107 ? 0.5828 0.2795 0.5555 -0.0250 -0.1861 0.0293  128 GLN A O   
923  C CB  . GLN A 107 ? 0.6502 0.3757 0.6610 -0.0032 -0.1966 -0.0034 128 GLN A CB  
924  C CG  . GLN A 107 ? 0.6665 0.3915 0.7033 0.0245  -0.2155 -0.0373 128 GLN A CG  
925  C CD  . GLN A 107 ? 0.8774 0.6526 0.9424 0.0540  -0.2156 -0.0755 128 GLN A CD  
926  O OE1 . GLN A 107 ? 0.9975 0.7593 1.0887 0.0733  -0.2581 -0.1068 128 GLN A OE1 
927  N NE2 . GLN A 107 ? 0.7009 0.5359 0.7613 0.0570  -0.1746 -0.0737 128 GLN A NE2 
928  N N   . PHE A 108 ? 0.4573 0.2090 0.4174 -0.0177 -0.1366 0.0317  129 PHE A N   
929  C CA  . PHE A 108 ? 0.4674 0.2218 0.4189 -0.0087 -0.1229 0.0324  129 PHE A CA  
930  C C   . PHE A 108 ? 0.6282 0.3652 0.5566 -0.0255 -0.1303 0.0493  129 PHE A C   
931  O O   . PHE A 108 ? 0.5337 0.2450 0.4594 -0.0230 -0.1385 0.0507  129 PHE A O   
932  C CB  . PHE A 108 ? 0.4431 0.2309 0.3900 0.0010  -0.0999 0.0302  129 PHE A CB  
933  C CG  . PHE A 108 ? 0.4952 0.2767 0.4293 0.0079  -0.0982 0.0336  129 PHE A CG  
934  C CD1 . PHE A 108 ? 0.4441 0.2108 0.3866 0.0153  -0.1054 0.0343  129 PHE A CD1 
935  C CD2 . PHE A 108 ? 0.4845 0.2821 0.3995 0.0083  -0.0938 0.0336  129 PHE A CD2 
936  C CE1 . PHE A 108 ? 0.4975 0.2484 0.4290 0.0217  -0.1121 0.0389  129 PHE A CE1 
937  C CE2 . PHE A 108 ? 0.5395 0.3284 0.4448 0.0211  -0.1007 0.0296  129 PHE A CE2 
938  C CZ  . PHE A 108 ? 0.5175 0.2744 0.4312 0.0273  -0.1118 0.0343  129 PHE A CZ  
939  N N   . GLN A 109 ? 0.4886 0.2507 0.4002 -0.0454 -0.1276 0.0633  130 GLN A N   
940  C CA  . GLN A 109 ? 0.5970 0.3712 0.4839 -0.0673 -0.1329 0.0810  130 GLN A CA  
941  C C   . GLN A 109 ? 0.6722 0.3954 0.5604 -0.0885 -0.1669 0.0966  130 GLN A C   
942  O O   . GLN A 109 ? 0.6318 0.3430 0.5061 -0.0959 -0.1730 0.1049  130 GLN A O   
943  C CB  . GLN A 109 ? 0.6566 0.4898 0.5275 -0.0912 -0.1266 0.0951  130 GLN A CB  
944  C CG  . GLN A 109 ? 0.9137 0.7877 0.7572 -0.1202 -0.1323 0.1154  130 GLN A CG  
945  C CD  . GLN A 109 ? 1.0426 1.0031 0.8721 -0.1066 -0.1061 0.0983  130 GLN A CD  
946  O OE1 . GLN A 109 ? 1.0893 1.0589 0.9317 -0.0750 -0.0895 0.0726  130 GLN A OE1 
947  N NE2 . GLN A 109 ? 1.0682 1.1003 0.8724 -0.1292 -0.1061 0.1090  130 GLN A NE2 
948  N N   . LYS A 110 ? 0.6374 0.3334 0.5454 -0.0951 -0.1934 0.0962  131 LYS A N   
949  C CA  . LYS A 110 ? 0.6833 0.3667 0.6024 -0.1051 -0.2274 0.0972  131 LYS A CA  
950  C C   . LYS A 110 ? 0.6974 0.3724 0.6364 -0.0742 -0.2252 0.0703  131 LYS A C   
951  O O   . LYS A 110 ? 0.7779 0.4460 0.7135 -0.0817 -0.2407 0.0753  131 LYS A O   
952  C CB  . LYS A 110 ? 0.6507 0.3246 0.5870 -0.1117 -0.2628 0.0989  131 LYS A CB  
953  N N   . GLU A 111 ? 0.6688 0.3510 0.6279 -0.0439 -0.2088 0.0446  132 GLU A N   
954  C CA  . GLU A 111 ? 0.6786 0.3640 0.6579 -0.0220 -0.2139 0.0228  132 GLU A CA  
955  C C   . GLU A 111 ? 0.7144 0.4143 0.6886 -0.0101 -0.1828 0.0192  132 GLU A C   
956  O O   . GLU A 111 ? 0.7787 0.4810 0.7604 -0.0031 -0.1865 0.0120  132 GLU A O   
957  C CB  . GLU A 111 ? 0.7130 0.4050 0.7230 0.0017  -0.2312 -0.0055 132 GLU A CB  
958  C CG  . GLU A 111 ? 0.8236 0.5006 0.8470 -0.0015 -0.2732 -0.0071 132 GLU A CG  
959  C CD  . GLU A 111 ? 0.9856 0.6800 1.0417 0.0299  -0.2866 -0.0436 132 GLU A CD  
960  O OE1 . GLU A 111 ? 0.9835 0.7019 1.0426 0.0432  -0.2565 -0.0592 132 GLU A OE1 
961  O OE2 . GLU A 111 ? 1.0693 0.7569 1.1500 0.0444  -0.3320 -0.0584 132 GLU A OE2 
962  N N   . VAL A 112 ? 0.4842 0.3534 0.4943 -0.0104 -0.1603 -0.0078 133 VAL A N   
963  C CA  . VAL A 112 ? 0.3913 0.3009 0.3884 -0.0011 -0.1245 -0.0172 133 VAL A CA  
964  C C   . VAL A 112 ? 0.4410 0.3765 0.4432 -0.0218 -0.0944 0.0010  133 VAL A C   
965  O O   . VAL A 112 ? 0.4314 0.3876 0.4234 -0.0179 -0.0757 -0.0032 133 VAL A O   
966  C CB  . VAL A 112 ? 0.4498 0.3751 0.4444 0.0118  -0.1183 -0.0302 133 VAL A CB  
967  C CG1 . VAL A 112 ? 0.4155 0.3832 0.4029 0.0151  -0.0885 -0.0310 133 VAL A CG1 
968  C CG2 . VAL A 112 ? 0.4881 0.3985 0.4715 0.0431  -0.1496 -0.0560 133 VAL A CG2 
969  N N   . LEU A 113 ? 0.3502 0.2898 0.3677 -0.0410 -0.0928 0.0204  134 LEU A N   
970  C CA  . LEU A 113 ? 0.3420 0.3134 0.3621 -0.0525 -0.0691 0.0334  134 LEU A CA  
971  C C   . LEU A 113 ? 0.3932 0.3732 0.4098 -0.0584 -0.0680 0.0430  134 LEU A C   
972  O O   . LEU A 113 ? 0.3827 0.3503 0.4089 -0.0686 -0.0891 0.0586  134 LEU A O   
973  C CB  . LEU A 113 ? 0.3484 0.3380 0.3861 -0.0674 -0.0715 0.0545  134 LEU A CB  
974  C CG  . LEU A 113 ? 0.3616 0.3979 0.3993 -0.0707 -0.0500 0.0651  134 LEU A CG  
975  C CD1 . LEU A 113 ? 0.3503 0.3914 0.3737 -0.0545 -0.0299 0.0422  134 LEU A CD1 
976  C CD2 . LEU A 113 ? 0.4049 0.4731 0.4618 -0.0841 -0.0551 0.0904  134 LEU A CD2 
977  N N   . CYS A 114 ? 0.3286 0.3272 0.3332 -0.0534 -0.0480 0.0356  135 CYS A N   
978  C CA  . CYS A 114 ? 0.3639 0.3770 0.3634 -0.0576 -0.0444 0.0435  135 CYS A CA  
979  C C   . CYS A 114 ? 0.3924 0.3827 0.3947 -0.0613 -0.0657 0.0509  135 CYS A C   
980  O O   . CYS A 114 ? 0.3479 0.3487 0.3619 -0.0757 -0.0763 0.0743  135 CYS A O   
981  C CB  . CYS A 114 ? 0.4203 0.4771 0.4274 -0.0660 -0.0361 0.0623  135 CYS A CB  
982  S SG  . CYS A 114 ? 0.4084 0.4909 0.4077 -0.0517 -0.0170 0.0463  135 CYS A SG  
983  N N   . PRO A 115 ? 0.3684 0.3335 0.3609 -0.0468 -0.0749 0.0328  136 PRO A N   
984  C CA  . PRO A 115 ? 0.3363 0.2759 0.3284 -0.0428 -0.0999 0.0337  136 PRO A CA  
985  C C   . PRO A 115 ? 0.3871 0.3400 0.3703 -0.0434 -0.0913 0.0366  136 PRO A C   
986  O O   . PRO A 115 ? 0.4133 0.3459 0.3970 -0.0409 -0.1131 0.0397  136 PRO A O   
987  C CB  . PRO A 115 ? 0.3854 0.3094 0.3658 -0.0174 -0.1109 0.0079  136 PRO A CB  
988  C CG  . PRO A 115 ? 0.4125 0.3699 0.3839 -0.0134 -0.0809 -0.0003 136 PRO A CG  
989  C CD  . PRO A 115 ? 0.3295 0.2971 0.3116 -0.0314 -0.0656 0.0127  136 PRO A CD  
990  N N   . ASN A 116 ? 0.3351 0.3177 0.3108 -0.0464 -0.0652 0.0355  137 ASN A N   
991  C CA  . ASN A 116 ? 0.3320 0.3270 0.2985 -0.0468 -0.0587 0.0371  137 ASN A CA  
992  C C   . ASN A 116 ? 0.3566 0.3622 0.3337 -0.0618 -0.0666 0.0610  137 ASN A C   
993  O O   . ASN A 116 ? 0.3772 0.4027 0.3680 -0.0745 -0.0666 0.0797  137 ASN A O   
994  C CB  . ASN A 116 ? 0.3301 0.3469 0.2865 -0.0459 -0.0375 0.0288  137 ASN A CB  
995  C CG  . ASN A 116 ? 0.3511 0.3867 0.3122 -0.0507 -0.0275 0.0328  137 ASN A CG  
996  O OD1 . ASN A 116 ? 0.3539 0.3857 0.3244 -0.0521 -0.0299 0.0354  137 ASN A OD1 
997  N ND2 . ASN A 116 ? 0.3261 0.3856 0.2793 -0.0493 -0.0184 0.0313  137 ASN A ND2 
998  N N   . LYS A 117 ? 0.3400 0.3399 0.3130 -0.0608 -0.0756 0.0647  138 LYS A N   
999  C CA  . LYS A 117 ? 0.4034 0.4189 0.3880 -0.0771 -0.0853 0.0926  138 LYS A CA  
1000 C C   . LYS A 117 ? 0.3493 0.4063 0.3231 -0.0780 -0.0633 0.0942  138 LYS A C   
1001 O O   . LYS A 117 ? 0.3387 0.4279 0.3205 -0.0903 -0.0654 0.1187  138 LYS A O   
1002 C CB  . LYS A 117 ? 0.4609 0.4365 0.4499 -0.0747 -0.1176 0.0968  138 LYS A CB  
1003 C CG  . LYS A 117 ? 0.5126 0.4417 0.5091 -0.0675 -0.1471 0.0884  138 LYS A CG  
1004 C CD  . LYS A 117 ? 0.6247 0.5069 0.6273 -0.0633 -0.1908 0.0928  138 LYS A CD  
1005 C CE  . LYS A 117 ? 0.5706 0.4392 0.5506 -0.0316 -0.1930 0.0609  138 LYS A CE  
1006 N NZ  . LYS A 117 ? 0.5936 0.4032 0.5758 -0.0147 -0.2466 0.0527  138 LYS A NZ  
1007 N N   . CYS A 118 ? 0.3711 0.4300 0.3276 -0.0656 -0.0456 0.0699  139 CYS A N   
1008 C CA  . CYS A 118 ? 0.3353 0.4251 0.2794 -0.0632 -0.0302 0.0650  139 CYS A CA  
1009 C C   . CYS A 118 ? 0.3247 0.4045 0.2579 -0.0537 -0.0208 0.0415  139 CYS A C   
1010 O O   . CYS A 118 ? 0.3489 0.4070 0.2858 -0.0511 -0.0235 0.0345  139 CYS A O   
1011 C CB  . CYS A 118 ? 0.3259 0.4133 0.2624 -0.0627 -0.0338 0.0663  139 CYS A CB  
1012 S SG  . CYS A 118 ? 0.3969 0.4507 0.3248 -0.0501 -0.0397 0.0470  139 CYS A SG  
1013 N N   . GLY A 119 ? 0.3389 0.4337 0.2595 -0.0485 -0.0143 0.0305  140 GLY A N   
1014 C CA  . GLY A 119 ? 0.3124 0.3892 0.2254 -0.0432 -0.0156 0.0122  140 GLY A CA  
1015 C C   . GLY A 119 ? 0.3944 0.4698 0.3113 -0.0374 -0.0142 0.0049  140 GLY A C   
1016 O O   . GLY A 119 ? 0.3394 0.4379 0.2632 -0.0364 -0.0095 0.0139  140 GLY A O   
1017 N N   . VAL A 120 ? 0.3814 0.4331 0.2961 -0.0354 -0.0208 -0.0074 141 VAL A N   
1018 C CA  . VAL A 120 ? 0.3383 0.3850 0.2556 -0.0275 -0.0223 -0.0167 141 VAL A CA  
1019 C C   . VAL A 120 ? 0.3254 0.3483 0.2528 -0.0353 -0.0263 -0.0131 141 VAL A C   
1020 O O   . VAL A 120 ? 0.3436 0.3523 0.2715 -0.0425 -0.0360 -0.0115 141 VAL A O   
1021 C CB  . VAL A 120 ? 0.3279 0.3681 0.2317 -0.0127 -0.0347 -0.0382 141 VAL A CB  
1022 C CG1 . VAL A 120 ? 0.4629 0.5023 0.3682 0.0010  -0.0372 -0.0497 141 VAL A CG1 
1023 C CG2 . VAL A 120 ? 0.3567 0.4332 0.2464 0.0005  -0.0315 -0.0447 141 VAL A CG2 
1024 N N   . MET A 121 ? 0.3296 0.3554 0.2669 -0.0353 -0.0204 -0.0079 142 MET A N   
1025 C CA  . MET A 121 ? 0.3341 0.3466 0.2801 -0.0396 -0.0234 -0.0047 142 MET A CA  
1026 C C   . MET A 121 ? 0.4022 0.4056 0.3519 -0.0347 -0.0264 -0.0123 142 MET A C   
1027 O O   . MET A 121 ? 0.3617 0.3772 0.3095 -0.0256 -0.0220 -0.0179 142 MET A O   
1028 C CB  . MET A 121 ? 0.2972 0.3133 0.2503 -0.0402 -0.0205 0.0032  142 MET A CB  
1029 C CG  . MET A 121 ? 0.3091 0.3223 0.2682 -0.0388 -0.0239 0.0034  142 MET A CG  
1030 S SD  . MET A 121 ? 0.3689 0.3782 0.3318 -0.0310 -0.0307 0.0039  142 MET A SD  
1031 C CE  . MET A 121 ? 0.3544 0.3808 0.3180 -0.0213 -0.0338 0.0003  142 MET A CE  
1032 N N   . SER A 122 ? 0.3506 0.3401 0.3062 -0.0401 -0.0358 -0.0101 143 SER A N   
1033 C CA  . SER A 122 ? 0.3459 0.3217 0.3069 -0.0359 -0.0426 -0.0160 143 SER A CA  
1034 C C   . SER A 122 ? 0.3852 0.3687 0.3582 -0.0410 -0.0378 -0.0056 143 SER A C   
1035 O O   . SER A 122 ? 0.3599 0.3567 0.3371 -0.0482 -0.0393 0.0061  143 SER A O   
1036 C CB  . SER A 122 ? 0.3365 0.2857 0.2976 -0.0400 -0.0663 -0.0187 143 SER A CB  
1037 O OG  . SER A 122 ? 0.3788 0.3186 0.3260 -0.0313 -0.0754 -0.0331 143 SER A OG  
1038 N N   . GLN A 123 ? 0.2970 0.2804 0.2744 -0.0347 -0.0327 -0.0099 144 GLN A N   
1039 C CA  . GLN A 123 ? 0.3146 0.3052 0.3020 -0.0369 -0.0297 -0.0030 144 GLN A CA  
1040 C C   . GLN A 123 ? 0.3331 0.3134 0.3275 -0.0343 -0.0349 -0.0059 144 GLN A C   
1041 O O   . GLN A 123 ? 0.4162 0.3879 0.4058 -0.0247 -0.0376 -0.0173 144 GLN A O   
1042 C CB  . GLN A 123 ? 0.3543 0.3533 0.3432 -0.0336 -0.0219 -0.0026 144 GLN A CB  
1043 C CG  . GLN A 123 ? 0.4148 0.4174 0.3976 -0.0343 -0.0224 -0.0002 144 GLN A CG  
1044 C CD  . GLN A 123 ? 0.4096 0.4088 0.3972 -0.0336 -0.0268 0.0031  144 GLN A CD  
1045 O OE1 . GLN A 123 ? 0.4390 0.4425 0.4314 -0.0387 -0.0261 0.0104  144 GLN A OE1 
1046 N NE2 . GLN A 123 ? 0.3904 0.3860 0.3771 -0.0262 -0.0359 -0.0009 144 GLN A NE2 
1047 N N   . THR A 124 ? 0.2796 0.2672 0.2838 -0.0390 -0.0370 0.0031  145 THR A N   
1048 C CA  . THR A 124 ? 0.2948 0.2715 0.3076 -0.0382 -0.0444 0.0032  145 THR A CA  
1049 C C   . THR A 124 ? 0.2632 0.2498 0.2793 -0.0314 -0.0328 -0.0007 145 THR A C   
1050 O O   . THR A 124 ? 0.3239 0.3260 0.3428 -0.0322 -0.0284 0.0039  145 THR A O   
1051 C CB  . THR A 124 ? 0.3155 0.3028 0.3408 -0.0508 -0.0563 0.0223  145 THR A CB  
1052 O OG1 . THR A 124 ? 0.3380 0.3143 0.3644 -0.0621 -0.0736 0.0315  145 THR A OG1 
1053 C CG2 . THR A 124 ? 0.2760 0.2510 0.3122 -0.0509 -0.0656 0.0248  145 THR A CG2 
1054 N N   . LEU A 125 ? 0.3027 0.2845 0.3179 -0.0221 -0.0311 -0.0098 146 LEU A N   
1055 C CA  . LEU A 125 ? 0.2791 0.2755 0.3005 -0.0193 -0.0223 -0.0082 146 LEU A CA  
1056 C C   . LEU A 125 ? 0.3307 0.3225 0.3593 -0.0138 -0.0268 -0.0105 146 LEU A C   
1057 O O   . LEU A 125 ? 0.3134 0.2877 0.3395 -0.0067 -0.0387 -0.0180 146 LEU A O   
1058 C CB  . LEU A 125 ? 0.2939 0.3100 0.3115 -0.0139 -0.0148 -0.0093 146 LEU A CB  
1059 C CG  . LEU A 125 ? 0.3021 0.3230 0.3147 -0.0204 -0.0127 -0.0042 146 LEU A CG  
1060 C CD1 . LEU A 125 ? 0.3450 0.4000 0.3606 -0.0202 -0.0074 0.0056  146 LEU A CD1 
1061 C CD2 . LEU A 125 ? 0.3605 0.3707 0.3773 -0.0288 -0.0169 0.0015  146 LEU A CD2 
1062 N N   . ILE A 126 ? 0.2771 0.2804 0.3144 -0.0162 -0.0217 -0.0050 147 ILE A N   
1063 C CA  . ILE A 126 ? 0.2905 0.2959 0.3350 -0.0097 -0.0231 -0.0065 147 ILE A CA  
1064 C C   . ILE A 126 ? 0.2928 0.3244 0.3388 -0.0039 -0.0145 -0.0057 147 ILE A C   
1065 O O   . ILE A 126 ? 0.2997 0.3433 0.3508 -0.0136 -0.0112 0.0043  147 ILE A O   
1066 C CB  . ILE A 126 ? 0.2910 0.2996 0.3459 -0.0165 -0.0247 0.0018  147 ILE A CB  
1067 C CG1 . ILE A 126 ? 0.2970 0.3048 0.3536 -0.0246 -0.0322 0.0103  147 ILE A CG1 
1068 C CG2 . ILE A 126 ? 0.2759 0.2842 0.3386 -0.0100 -0.0275 0.0008  147 ILE A CG2 
1069 C CD1 . ILE A 126 ? 0.3513 0.3386 0.4095 -0.0279 -0.0472 0.0136  147 ILE A CD1 
1070 N N   . TRP A 127 ? 0.2803 0.3239 0.3223 0.0130  -0.0151 -0.0148 148 TRP A N   
1071 C CA  . TRP A 127 ? 0.2531 0.3432 0.2979 0.0211  -0.0065 -0.0093 148 TRP A CA  
1072 C C   . TRP A 127 ? 0.2852 0.3842 0.3424 0.0195  -0.0054 -0.0028 148 TRP A C   
1073 O O   . TRP A 127 ? 0.2999 0.3800 0.3570 0.0300  -0.0120 -0.0130 148 TRP A O   
1074 C CB  . TRP A 127 ? 0.2852 0.3984 0.3157 0.0492  -0.0087 -0.0264 148 TRP A CB  
1075 C CG  . TRP A 127 ? 0.3494 0.4655 0.3693 0.0479  -0.0076 -0.0285 148 TRP A CG  
1076 C CD1 . TRP A 127 ? 0.3516 0.4242 0.3624 0.0456  -0.0173 -0.0394 148 TRP A CD1 
1077 C CD2 . TRP A 127 ? 0.3749 0.5440 0.3958 0.0439  0.0025  -0.0129 148 TRP A CD2 
1078 N NE1 . TRP A 127 ? 0.3855 0.4787 0.3882 0.0447  -0.0121 -0.0370 148 TRP A NE1 
1079 C CE2 . TRP A 127 ? 0.3948 0.5476 0.4041 0.0430  0.0000  -0.0198 148 TRP A CE2 
1080 C CE3 . TRP A 127 ? 0.3289 0.5645 0.3619 0.0388  0.0109  0.0112  148 TRP A CE3 
1081 C CZ2 . TRP A 127 ? 0.5011 0.6997 0.5095 0.0385  0.0069  -0.0051 148 TRP A CZ2 
1082 C CZ3 . TRP A 127 ? 0.3604 0.6447 0.3954 0.0306  0.0154  0.0310  148 TRP A CZ3 
1083 C CH2 . TRP A 127 ? 0.4516 0.7163 0.4738 0.0316  0.0140  0.0217  148 TRP A CH2 
1084 N N   . CYS A 128 ? 0.2652 0.3918 0.3348 0.0054  -0.0012 0.0161  149 CYS A N   
1085 C CA  . CYS A 128 ? 0.2948 0.4236 0.3775 -0.0008 -0.0027 0.0237  149 CYS A CA  
1086 C C   . CYS A 128 ? 0.2757 0.4407 0.3611 0.0170  0.0014  0.0218  149 CYS A C   
1087 O O   . CYS A 128 ? 0.2894 0.4492 0.3832 0.0154  -0.0002 0.0235  149 CYS A O   
1088 C CB  . CYS A 128 ? 0.2699 0.4088 0.3664 -0.0232 -0.0085 0.0453  149 CYS A CB  
1089 S SG  . CYS A 128 ? 0.2992 0.3942 0.3910 -0.0367 -0.0196 0.0428  149 CYS A SG  
1090 N N   . LEU A 129 ? 0.2539 0.4644 0.3315 0.0371  0.0062  0.0180  150 LEU A N   
1091 C CA  . LEU A 129 ? 0.2370 0.4956 0.3164 0.0585  0.0093  0.0164  150 LEU A CA  
1092 C C   . LEU A 129 ? 0.2718 0.4872 0.3415 0.0822  -0.0007 -0.0109 150 LEU A C   
1093 O O   . LEU A 129 ? 0.2936 0.5109 0.3704 0.0884  -0.0027 -0.0115 150 LEU A O   
1094 C CB  . LEU A 129 ? 0.2815 0.6220 0.3534 0.0801  0.0163  0.0203  150 LEU A CB  
1095 C CG  . LEU A 129 ? 0.3536 0.7719 0.4265 0.1077  0.0209  0.0217  150 LEU A CG  
1096 C CD1 . LEU A 129 ? 0.3466 0.7881 0.4440 0.0813  0.0238  0.0524  150 LEU A CD1 
1097 C CD2 . LEU A 129 ? 0.3314 0.8528 0.3954 0.1318  0.0286  0.0286  150 LEU A CD2 
1098 N N   . LYS A 130 ? 0.2752 0.4502 0.3299 0.0951  -0.0114 -0.0322 151 LYS A N   
1099 C CA  . LYS A 130 ? 0.4126 0.5407 0.4610 0.1160  -0.0313 -0.0547 151 LYS A CA  
1100 C C   . LYS A 130 ? 0.3830 0.4399 0.4350 0.0942  -0.0458 -0.0533 151 LYS A C   
1101 O O   . LYS A 130 ? 0.3811 0.3929 0.4314 0.1050  -0.0701 -0.0657 151 LYS A O   
1102 C CB  . LYS A 130 ? 0.5144 0.6592 0.5419 0.1596  -0.0442 -0.0841 151 LYS A CB  
1103 C CG  . LYS A 130 ? 0.5345 0.7543 0.5581 0.1932  -0.0374 -0.0900 151 LYS A CG  
1104 C CD  . LYS A 130 ? 0.6349 0.8886 0.6323 0.2450  -0.0502 -0.1236 151 LYS A CD  
1105 N N   . CYS A 131 ? 0.3332 0.3856 0.3917 0.0644  -0.0346 -0.0357 152 CYS A N   
1106 C CA  . CYS A 131 ? 0.2860 0.2969 0.3505 0.0424  -0.0436 -0.0269 152 CYS A CA  
1107 C C   . CYS A 131 ? 0.3893 0.3636 0.4445 0.0454  -0.0619 -0.0365 152 CYS A C   
1108 O O   . CYS A 131 ? 0.4229 0.3674 0.4863 0.0289  -0.0769 -0.0255 152 CYS A O   
1109 C CB  . CYS A 131 ? 0.3637 0.3584 0.4419 0.0363  -0.0537 -0.0185 152 CYS A CB  
1110 S SG  . CYS A 131 ? 0.3596 0.3938 0.4494 0.0273  -0.0339 -0.0053 152 CYS A SG  
1111 N N   . GLU A 132 ? 0.3450 0.3289 0.3846 0.0652  -0.0625 -0.0537 153 GLU A N   
1112 C CA  . GLU A 132 ? 0.3569 0.3035 0.3864 0.0697  -0.0835 -0.0655 153 GLU A CA  
1113 C C   . GLU A 132 ? 0.3786 0.3231 0.4101 0.0430  -0.0739 -0.0497 153 GLU A C   
1114 O O   . GLU A 132 ? 0.3456 0.3231 0.3759 0.0351  -0.0513 -0.0419 153 GLU A O   
1115 C CB  . GLU A 132 ? 0.4085 0.3750 0.4176 0.1053  -0.0877 -0.0925 153 GLU A CB  
1116 C CG  . GLU A 132 ? 0.6864 0.6428 0.6875 0.1435  -0.1113 -0.1186 153 GLU A CG  
1117 C CD  . GLU A 132 ? 0.9711 0.8480 0.9714 0.1484  -0.1579 -0.1322 153 GLU A CD  
1118 O OE1 . GLU A 132 ? 0.9663 0.8116 0.9607 0.1404  -0.1736 -0.1353 153 GLU A OE1 
1119 O OE2 . GLU A 132 ? 1.0363 0.8809 1.0442 0.1575  -0.1824 -0.1365 153 GLU A OE2 
1120 N N   . LYS A 133 ? 0.3492 0.2558 0.3843 0.0297  -0.0957 -0.0436 154 LYS A N   
1121 C CA  . LYS A 133 ? 0.3772 0.2878 0.4116 0.0100  -0.0888 -0.0312 154 LYS A CA  
1122 C C   . LYS A 133 ? 0.3877 0.2838 0.4055 0.0230  -0.0992 -0.0491 154 LYS A C   
1123 O O   . LYS A 133 ? 0.4703 0.3295 0.4824 0.0378  -0.1294 -0.0652 154 LYS A O   
1124 C CB  . LYS A 133 ? 0.3799 0.2768 0.4306 -0.0156 -0.1055 -0.0060 154 LYS A CB  
1125 C CG  . LYS A 133 ? 0.4070 0.3225 0.4568 -0.0329 -0.0967 0.0083  154 LYS A CG  
1126 C CD  . LYS A 133 ? 0.3924 0.3283 0.4605 -0.0559 -0.1052 0.0397  154 LYS A CD  
1127 C CE  . LYS A 133 ? 0.4068 0.3094 0.4856 -0.0703 -0.1422 0.0541  154 LYS A CE  
1128 N NZ  . LYS A 133 ? 0.4175 0.3570 0.5171 -0.0977 -0.1529 0.0948  154 LYS A NZ  
1129 N N   . GLN A 134 ? 0.3089 0.2302 0.3185 0.0197  -0.0796 -0.0481 155 GLN A N   
1130 C CA  . GLN A 134 ? 0.3853 0.2997 0.3775 0.0363  -0.0892 -0.0673 155 GLN A CA  
1131 C C   . GLN A 134 ? 0.3247 0.2494 0.3152 0.0182  -0.0771 -0.0549 155 GLN A C   
1132 O O   . GLN A 134 ? 0.3612 0.3086 0.3591 0.0031  -0.0572 -0.0386 155 GLN A O   
1133 C CB  . GLN A 134 ? 0.5099 0.4654 0.4888 0.0663  -0.0767 -0.0857 155 GLN A CB  
1134 C CG  . GLN A 134 ? 0.7835 0.7365 0.7603 0.0938  -0.0902 -0.1034 155 GLN A CG  
1135 C CD  . GLN A 134 ? 0.8994 0.9065 0.8581 0.1331  -0.0842 -0.1257 155 GLN A CD  
1136 O OE1 . GLN A 134 ? 0.9373 0.9823 0.8854 0.1385  -0.0724 -0.1268 155 GLN A OE1 
1137 N NE2 . GLN A 134 ? 0.8607 0.8807 0.8158 0.1626  -0.0929 -0.1420 155 GLN A NE2 
1138 N N   . LEU A 135 ? 0.3489 0.2531 0.3291 0.0220  -0.0937 -0.0647 156 LEU A N   
1139 C CA  . LEU A 135 ? 0.3732 0.2893 0.3499 0.0081  -0.0831 -0.0551 156 LEU A CA  
1140 C C   . LEU A 135 ? 0.4783 0.4351 0.4433 0.0225  -0.0616 -0.0630 156 LEU A C   
1141 O O   . LEU A 135 ? 0.5289 0.4961 0.4801 0.0472  -0.0679 -0.0831 156 LEU A O   
1142 C CB  . LEU A 135 ? 0.4537 0.3326 0.4251 0.0052  -0.1128 -0.0607 156 LEU A CB  
1143 C CG  . LEU A 135 ? 0.4649 0.3547 0.4361 -0.0138 -0.1051 -0.0457 156 LEU A CG  
1144 C CD1 . LEU A 135 ? 0.3573 0.2631 0.3462 -0.0376 -0.0967 -0.0175 156 LEU A CD1 
1145 C CD2 . LEU A 135 ? 0.3958 0.2491 0.3615 -0.0163 -0.1384 -0.0518 156 LEU A CD2 
1146 N N   . HIS A 136 ? 0.3252 0.3083 0.2960 0.0088  -0.0408 -0.0464 157 HIS A N   
1147 C CA  . HIS A 136 ? 0.3680 0.3933 0.3342 0.0149  -0.0254 -0.0432 157 HIS A CA  
1148 C C   . HIS A 136 ? 0.3499 0.3768 0.3079 0.0090  -0.0246 -0.0411 157 HIS A C   
1149 O O   . HIS A 136 ? 0.3988 0.4061 0.3614 -0.0077 -0.0257 -0.0313 157 HIS A O   
1150 C CB  . HIS A 136 ? 0.3945 0.4363 0.3756 -0.0001 -0.0131 -0.0233 157 HIS A CB  
1151 C CG  . HIS A 136 ? 0.3812 0.4675 0.3654 -0.0025 -0.0039 -0.0086 157 HIS A CG  
1152 N ND1 . HIS A 136 ? 0.4247 0.5619 0.4090 0.0111  0.0015  -0.0063 157 HIS A ND1 
1153 C CD2 . HIS A 136 ? 0.3741 0.4673 0.3637 -0.0178 -0.0027 0.0087  157 HIS A CD2 
1154 C CE1 . HIS A 136 ? 0.5102 0.6901 0.5023 0.0001  0.0062  0.0173  157 HIS A CE1 
1155 N NE2 . HIS A 136 ? 0.4570 0.6038 0.4533 -0.0187 0.0017  0.0265  157 HIS A NE2 
1156 N N   . ILE A 137 ? 0.3387 0.3987 0.2849 0.0240  -0.0217 -0.0484 158 ILE A N   
1157 C CA  . ILE A 137 ? 0.3309 0.3918 0.2682 0.0195  -0.0224 -0.0477 158 ILE A CA  
1158 C C   . ILE A 137 ? 0.4213 0.5235 0.3657 0.0084  -0.0080 -0.0250 158 ILE A C   
1159 O O   . ILE A 137 ? 0.3315 0.4850 0.2793 0.0157  -0.0006 -0.0161 158 ILE A O   
1160 C CB  . ILE A 137 ? 0.3757 0.4443 0.2928 0.0459  -0.0349 -0.0732 158 ILE A CB  
1161 C CG1 . ILE A 137 ? 0.4524 0.4706 0.3645 0.0581  -0.0605 -0.0956 158 ILE A CG1 
1162 C CG2 . ILE A 137 ? 0.3530 0.4159 0.2615 0.0387  -0.0377 -0.0724 158 ILE A CG2 
1163 C CD1 . ILE A 137 ? 0.4159 0.3831 0.3412 0.0298  -0.0713 -0.0815 158 ILE A CD1 
1164 N N   . CYS A 138 ? 0.3656 0.4494 0.3141 -0.0093 -0.0076 -0.0129 159 CYS A N   
1165 C CA  . CYS A 138 ? 0.3915 0.5021 0.3484 -0.0217 -0.0030 0.0099  159 CYS A CA  
1166 C C   . CYS A 138 ? 0.3219 0.4484 0.2671 -0.0186 -0.0023 0.0081  159 CYS A C   
1167 O O   . CYS A 138 ? 0.3503 0.4476 0.2925 -0.0267 -0.0061 0.0073  159 CYS A O   
1168 C CB  . CYS A 138 ? 0.3535 0.4297 0.3214 -0.0375 -0.0088 0.0205  159 CYS A CB  
1169 S SG  . CYS A 138 ? 0.3731 0.4235 0.3512 -0.0384 -0.0120 0.0166  159 CYS A SG  
1170 N N   . ARG A 139 ? 0.3036 0.4831 0.2412 -0.0045 0.0022  0.0072  160 ARG A N   
1171 C CA  . ARG A 139 ? 0.3651 0.5592 0.2874 0.0043  0.0012  -0.0017 160 ARG A CA  
1172 C C   . ARG A 139 ? 0.2851 0.5220 0.2163 -0.0101 0.0059  0.0281  160 ARG A C   
1173 O O   . ARG A 139 ? 0.3419 0.6439 0.2830 -0.0113 0.0106  0.0513  160 ARG A O   
1174 C CB  . ARG A 139 ? 0.3807 0.6111 0.2838 0.0371  -0.0015 -0.0277 160 ARG A CB  
1175 C CG  . ARG A 139 ? 0.3724 0.6222 0.2577 0.0492  -0.0051 -0.0392 160 ARG A CG  
1176 C CD  . ARG A 139 ? 0.5364 0.8230 0.3981 0.0904  -0.0140 -0.0722 160 ARG A CD  
1177 N NE  . ARG A 139 ? 0.6333 0.8827 0.4919 0.1063  -0.0260 -0.0956 160 ARG A NE  
1178 C CZ  . ARG A 139 ? 0.5639 0.7340 0.4173 0.1064  -0.0482 -0.1183 160 ARG A CZ  
1179 N NH1 . ARG A 139 ? 0.5825 0.7075 0.4325 0.0918  -0.0597 -0.1202 160 ARG A NH1 
1180 N NH2 . ARG A 139 ? 0.6594 0.8002 0.5128 0.1199  -0.0612 -0.1351 160 ARG A NH2 
1181 N N   A LYS A 140 ? 0.2633 0.3776 0.3553 -0.0349 -0.0104 -0.0080 161 LYS A N   
1182 N N   B LYS A 140 ? 0.2587 0.3731 0.3507 -0.0349 -0.0104 -0.0079 161 LYS A N   
1183 C CA  A LYS A 140 ? 0.2996 0.4126 0.4228 -0.0280 0.0136  0.0151  161 LYS A CA  
1184 C CA  B LYS A 140 ? 0.3059 0.4192 0.4288 -0.0274 0.0140  0.0157  161 LYS A CA  
1185 C C   A LYS A 140 ? 0.3123 0.4101 0.3671 -0.0069 0.0193  0.0234  161 LYS A C   
1186 C C   B LYS A 140 ? 0.3150 0.4128 0.3694 -0.0065 0.0196  0.0238  161 LYS A C   
1187 O O   A LYS A 140 ? 0.3078 0.3958 0.3028 -0.0035 0.0019  0.0085  161 LYS A O   
1188 O O   B LYS A 140 ? 0.3040 0.3923 0.2984 -0.0026 0.0023  0.0093  161 LYS A O   
1189 C CB  A LYS A 140 ? 0.2702 0.3748 0.4399 -0.0505 0.0077  0.0000  161 LYS A CB  
1190 C CB  B LYS A 140 ? 0.2759 0.3814 0.4473 -0.0498 0.0087  0.0014  161 LYS A CB  
1191 C CG  A LYS A 140 ? 0.2715 0.3895 0.5176 -0.0680 -0.0012 -0.0076 161 LYS A CG  
1192 C CG  B LYS A 140 ? 0.2402 0.3609 0.4931 -0.0656 0.0037  -0.0013 161 LYS A CG  
1193 C CD  A LYS A 140 ? 0.3293 0.4337 0.6213 -0.0872 -0.0108 -0.0246 161 LYS A CD  
1194 C CD  B LYS A 140 ? 0.3117 0.4200 0.6140 -0.0851 -0.0051 -0.0170 161 LYS A CD  
1195 C CE  A LYS A 140 ? 0.2720 0.3874 0.6442 -0.1033 -0.0262 -0.0351 161 LYS A CE  
1196 C CE  B LYS A 140 ? 0.2226 0.3453 0.6173 -0.0991 -0.0117 -0.0170 161 LYS A CE  
1197 N NZ  A LYS A 140 ? 0.2389 0.3488 0.5680 -0.1065 -0.0576 -0.0674 161 LYS A NZ  
1198 N NZ  B LYS A 140 ? 0.3339 0.4324 0.7482 -0.1106 -0.0247 -0.0353 161 LYS A NZ  
1199 N N   . SER A 141 ? 0.3146 0.4091 0.3783 0.0091  0.0422  0.0472  162 SER A N   
1200 C CA  . SER A 141 ? 0.2962 0.3743 0.2945 0.0315  0.0422  0.0513  162 SER A CA  
1201 C C   . SER A 141 ? 0.3769 0.4408 0.3413 0.0151  0.0176  0.0222  162 SER A C   
1202 O O   . SER A 141 ? 0.3105 0.3725 0.3053 -0.0076 0.0123  0.0072  162 SER A O   
1203 C CB  . SER A 141 ? 0.3051 0.3785 0.3184 0.0499  0.0683  0.0771  162 SER A CB  
1204 O OG  . SER A 141 ? 0.4361 0.5231 0.4755 0.0708  0.0954  0.1096  162 SER A OG  
1205 N N   A LEU A 142 ? 0.3398 0.3922 0.2426 0.0289  0.0030  0.0157  163 LEU A N   
1206 N N   B LEU A 142 ? 0.3781 0.4310 0.2813 0.0278  0.0022  0.0149  163 LEU A N   
1207 C CA  A LEU A 142 ? 0.3696 0.4120 0.2481 0.0111  -0.0203 -0.0098 163 LEU A CA  
1208 C CA  B LEU A 142 ? 0.3787 0.4210 0.2565 0.0117  -0.0202 -0.0095 163 LEU A CA  
1209 C C   A LEU A 142 ? 0.3699 0.4064 0.2596 0.0064  -0.0171 -0.0125 163 LEU A C   
1210 C C   B LEU A 142 ? 0.3898 0.4268 0.2811 0.0062  -0.0165 -0.0121 163 LEU A C   
1211 O O   A LEU A 142 ? 0.4228 0.4574 0.3194 -0.0136 -0.0273 -0.0302 163 LEU A O   
1212 O O   B LEU A 142 ? 0.4027 0.4384 0.3046 -0.0147 -0.0256 -0.0296 163 LEU A O   
1213 C CB  A LEU A 142 ? 0.4324 0.4622 0.2510 0.0269  -0.0387 -0.0147 163 LEU A CB  
1214 C CB  B LEU A 142 ? 0.4034 0.4328 0.2216 0.0280  -0.0382 -0.0140 163 LEU A CB  
1215 C CG  A LEU A 142 ? 0.3939 0.4062 0.2243 -0.0006 -0.0497 -0.0261 163 LEU A CG  
1216 C CG  B LEU A 142 ? 0.3445 0.3624 0.1709 0.0061  -0.0471 -0.0225 163 LEU A CG  
1217 C CD1 A LEU A 142 ? 0.3877 0.3812 0.2344 -0.0134 -0.0545 -0.0351 163 LEU A CD1 
1218 C CD1 B LEU A 142 ? 0.3804 0.3904 0.2067 0.0028  -0.0501 -0.0192 163 LEU A CD1 
1219 C CD2 A LEU A 142 ? 0.3944 0.4031 0.2220 0.0043  -0.0522 -0.0205 163 LEU A CD2 
1220 C CD2 B LEU A 142 ? 0.4072 0.4102 0.2527 -0.0120 -0.0541 -0.0361 163 LEU A CD2 
1221 N N   . ASP A 143 ? 0.4064 0.4395 0.2933 0.0286  -0.0021 0.0064  164 ASP A N   
1222 C CA  . ASP A 143 ? 0.4558 0.4831 0.3489 0.0279  0.0001  0.0045  164 ASP A CA  
1223 C C   . ASP A 143 ? 0.3383 0.3697 0.2856 0.0100  0.0147  0.0052  164 ASP A C   
1224 O O   . ASP A 143 ? 0.3558 0.3901 0.3371 0.0169  0.0361  0.0247  164 ASP A O   
1225 C CB  . ASP A 143 ? 0.4949 0.5139 0.3603 0.0617  0.0092  0.0231  164 ASP A CB  
1226 C CG  . ASP A 143 ? 0.6906 0.7033 0.5512 0.0638  0.0036  0.0168  164 ASP A CG  
1227 O OD1 . ASP A 143 ? 0.7094 0.7141 0.5310 0.0779  -0.0164 0.0090  164 ASP A OD1 
1228 O OD2 . ASP A 143 ? 0.4463 0.4617 0.3456 0.0502  0.0167  0.0180  164 ASP A OD2 
1229 N N   . CYS A 144 ? 0.3055 0.3351 0.2604 -0.0102 0.0035  -0.0146 165 CYS A N   
1230 C CA  . CYS A 144 ? 0.2763 0.3047 0.2756 -0.0274 0.0104  -0.0209 165 CYS A CA  
1231 C C   . CYS A 144 ? 0.3018 0.3231 0.3144 -0.0182 0.0245  -0.0106 165 CYS A C   
1232 O O   . CYS A 144 ? 0.3388 0.3547 0.3912 -0.0284 0.0326  -0.0122 165 CYS A O   
1233 C CB  . CYS A 144 ? 0.3496 0.3769 0.3421 -0.0469 -0.0065 -0.0461 165 CYS A CB  
1234 S SG  . CYS A 144 ? 0.4014 0.4347 0.3908 -0.0580 -0.0197 -0.0575 165 CYS A SG  
1235 N N   . GLY A 145 ? 0.3232 0.3421 0.3022 0.0021  0.0245  -0.0021 166 GLY A N   
1236 C CA  . GLY A 145 ? 0.3633 0.3752 0.3499 0.0149  0.0376  0.0083  166 GLY A CA  
1237 C C   . GLY A 145 ? 0.3754 0.3878 0.3364 0.0182  0.0229  -0.0037 166 GLY A C   
1238 O O   . GLY A 145 ? 0.3433 0.3610 0.2796 0.0136  0.0031  -0.0163 166 GLY A O   
1239 N N   . GLU A 146 ? 0.3173 0.3245 0.2884 0.0261  0.0325  0.0011  167 GLU A N   
1240 C CA  . GLU A 146 ? 0.3046 0.3152 0.2551 0.0360  0.0200  -0.0054 167 GLU A CA  
1241 C C   . GLU A 146 ? 0.3487 0.3588 0.3237 0.0254  0.0260  -0.0129 167 GLU A C   
1242 O O   . GLU A 146 ? 0.3496 0.3495 0.3472 0.0270  0.0434  -0.0047 167 GLU A O   
1243 C CB  . GLU A 146 ? 0.3795 0.3834 0.3027 0.0699  0.0235  0.0106  167 GLU A CB  
1244 C CG  . GLU A 146 ? 0.3933 0.4024 0.3006 0.0798  0.0042  0.0008  167 GLU A CG  
1245 C CD  . GLU A 146 ? 0.6533 0.6526 0.5290 0.1183  0.0043  0.0136  167 GLU A CD  
1246 O OE1 . GLU A 146 ? 0.5888 0.5771 0.4658 0.1364  0.0289  0.0328  167 GLU A OE1 
1247 O OE2 . GLU A 146 ? 0.5665 0.5673 0.4166 0.1314  -0.0216 0.0044  167 GLU A OE2 
1248 N N   . ARG A 147 ? 0.3010 0.3215 0.2734 0.0147  0.0119  -0.0277 168 ARG A N   
1249 C CA  . ARG A 147 ? 0.2968 0.3190 0.2864 0.0092  0.0171  -0.0348 168 ARG A CA  
1250 C C   . ARG A 147 ? 0.3125 0.3397 0.2969 0.0287  0.0156  -0.0290 168 ARG A C   
1251 O O   . ARG A 147 ? 0.3555 0.3920 0.3253 0.0372  -0.0007 -0.0296 168 ARG A O   
1252 C CB  . ARG A 147 ? 0.3174 0.3511 0.3085 -0.0087 0.0066  -0.0498 168 ARG A CB  
1253 C CG  . ARG A 147 ? 0.3698 0.3981 0.3612 -0.0254 0.0051  -0.0585 168 ARG A CG  
1254 C CD  . ARG A 147 ? 0.4078 0.4274 0.4115 -0.0337 0.0116  -0.0698 168 ARG A CD  
1255 N NE  . ARG A 147 ? 0.4490 0.4601 0.4547 -0.0457 0.0074  -0.0788 168 ARG A NE  
1256 C CZ  . ARG A 147 ? 0.4155 0.4313 0.4063 -0.0546 -0.0018 -0.0894 168 ARG A CZ  
1257 N NH1 . ARG A 147 ? 0.3209 0.3493 0.2992 -0.0544 -0.0049 -0.0895 168 ARG A NH1 
1258 N NH2 . ARG A 147 ? 0.3914 0.3995 0.3826 -0.0629 -0.0078 -0.0990 168 ARG A NH2 
1259 N N   . HIS A 148 ? 0.3264 0.3468 0.3237 0.0356  0.0290  -0.0258 169 HIS A N   
1260 C CA  . HIS A 148 ? 0.3284 0.3554 0.3211 0.0556  0.0264  -0.0214 169 HIS A CA  
1261 C C   . HIS A 148 ? 0.3076 0.3491 0.3165 0.0450  0.0238  -0.0324 169 HIS A C   
1262 O O   . HIS A 148 ? 0.3723 0.4047 0.3920 0.0366  0.0358  -0.0372 169 HIS A O   
1263 C CB  . HIS A 148 ? 0.3669 0.3756 0.3603 0.0749  0.0454  -0.0073 169 HIS A CB  
1264 C CG  . HIS A 148 ? 0.5428 0.5389 0.5197 0.0916  0.0528  0.0092  169 HIS A CG  
1265 N ND1 . HIS A 148 ? 0.6451 0.6217 0.6282 0.1060  0.0761  0.0275  169 HIS A ND1 
1266 C CD2 . HIS A 148 ? 0.6123 0.6116 0.5665 0.0983  0.0418  0.0120  169 HIS A CD2 
1267 C CE1 . HIS A 148 ? 0.6793 0.6501 0.6443 0.1223  0.0818  0.0430  169 HIS A CE1 
1268 N NE2 . HIS A 148 ? 0.6408 0.6245 0.5852 0.1188  0.0603  0.0327  169 HIS A NE2 
1269 N N   A ILE A 149 ? 0.2947 0.3581 0.3074 0.0460  0.0076  -0.0363 170 ILE A N   
1270 N N   B ILE A 149 ? 0.2802 0.3436 0.2930 0.0463  0.0078  -0.0362 170 ILE A N   
1271 C CA  A ILE A 149 ? 0.2938 0.3760 0.3265 0.0354  0.0078  -0.0428 170 ILE A CA  
1272 C CA  B ILE A 149 ? 0.2694 0.3513 0.3021 0.0352  0.0082  -0.0428 170 ILE A CA  
1273 C C   A ILE A 149 ? 0.3136 0.4127 0.3604 0.0519  0.0033  -0.0392 170 ILE A C   
1274 C C   B ILE A 149 ? 0.3142 0.4134 0.3611 0.0514  0.0033  -0.0393 170 ILE A C   
1275 O O   A ILE A 149 ? 0.3143 0.4189 0.3571 0.0650  -0.0137 -0.0370 170 ILE A O   
1276 O O   B ILE A 149 ? 0.2954 0.4004 0.3385 0.0640  -0.0140 -0.0372 170 ILE A O   
1277 C CB  A ILE A 149 ? 0.3418 0.4398 0.3807 0.0177  -0.0061 -0.0479 170 ILE A CB  
1278 C CB  B ILE A 149 ? 0.3307 0.4278 0.3691 0.0173  -0.0053 -0.0481 170 ILE A CB  
1279 C CG1 A ILE A 149 ? 0.3531 0.4360 0.3771 0.0024  -0.0023 -0.0529 170 ILE A CG1 
1280 C CG1 B ILE A 149 ? 0.3667 0.4494 0.3923 0.0013  0.0006  -0.0537 170 ILE A CG1 
1281 C CG2 A ILE A 149 ? 0.3374 0.4586 0.4020 0.0117  -0.0018 -0.0484 170 ILE A CG2 
1282 C CG2 B ILE A 149 ? 0.3262 0.4483 0.3915 0.0125  -0.0033 -0.0481 170 ILE A CG2 
1283 C CD1 A ILE A 149 ? 0.2876 0.3598 0.3120 -0.0040 0.0139  -0.0589 170 ILE A CD1 
1284 C CD1 B ILE A 149 ? 0.3251 0.4187 0.3515 -0.0144 -0.0109 -0.0573 170 ILE A CD1 
1285 N N   . GLU A 150 ? 0.3166 0.4229 0.3779 0.0544  0.0166  -0.0394 171 GLU A N   
1286 C CA  . GLU A 150 ? 0.2857 0.4145 0.3672 0.0687  0.0115  -0.0359 171 GLU A CA  
1287 C C   . GLU A 150 ? 0.3409 0.4957 0.4500 0.0580  0.0167  -0.0362 171 GLU A C   
1288 O O   . GLU A 150 ? 0.3082 0.4545 0.4100 0.0507  0.0329  -0.0390 171 GLU A O   
1289 C CB  . GLU A 150 ? 0.3695 0.4846 0.4428 0.0905  0.0250  -0.0314 171 GLU A CB  
1290 C CG  . GLU A 150 ? 0.4164 0.5080 0.4642 0.1056  0.0226  -0.0259 171 GLU A CG  
1291 C CD  . GLU A 150 ? 0.4781 0.5532 0.5170 0.1289  0.0370  -0.0185 171 GLU A CD  
1292 O OE1 . GLU A 150 ? 0.3922 0.4641 0.4399 0.1302  0.0519  -0.0196 171 GLU A OE1 
1293 O OE2 . GLU A 150 ? 0.5357 0.5985 0.5549 0.1494  0.0338  -0.0108 171 GLU A OE2 
1294 N N   A VAL A 151 ? 0.2688 0.4549 0.4113 0.0593  0.0025  -0.0328 172 VAL A N   
1295 N N   B VAL A 151 ? 0.2856 0.4716 0.4279 0.0589  0.0020  -0.0329 172 VAL A N   
1296 C CA  A VAL A 151 ? 0.2609 0.4765 0.4387 0.0511  0.0114  -0.0273 172 VAL A CA  
1297 C CA  B VAL A 151 ? 0.2819 0.4986 0.4612 0.0510  0.0099  -0.0272 172 VAL A CA  
1298 C C   A VAL A 151 ? 0.2643 0.5123 0.4833 0.0647  0.0031  -0.0211 172 VAL A C   
1299 C C   B VAL A 151 ? 0.2764 0.5239 0.4946 0.0657  0.0031  -0.0212 172 VAL A C   
1300 O O   A VAL A 151 ? 0.3228 0.5756 0.5505 0.0725  -0.0217 -0.0240 172 VAL A O   
1301 O O   B VAL A 151 ? 0.3137 0.5654 0.5393 0.0748  -0.0208 -0.0241 172 VAL A O   
1302 C CB  A VAL A 151 ? 0.3320 0.5572 0.5241 0.0292  0.0018  -0.0266 172 VAL A CB  
1303 C CB  B VAL A 151 ? 0.3257 0.5553 0.5245 0.0298  -0.0024 -0.0261 172 VAL A CB  
1304 C CG1 A VAL A 151 ? 0.2656 0.4967 0.4722 0.0265  -0.0302 -0.0296 172 VAL A CG1 
1305 C CG1 B VAL A 151 ? 0.3201 0.5782 0.5550 0.0232  0.0149  -0.0152 172 VAL A CG1 
1306 C CG2 A VAL A 151 ? 0.2976 0.5536 0.5289 0.0230  0.0171  -0.0154 172 VAL A CG2 
1307 C CG2 B VAL A 151 ? 0.3245 0.5244 0.4838 0.0177  -0.0013 -0.0332 172 VAL A CG2 
1308 N N   . HIS A 152 ? 0.2683 0.5368 0.5095 0.0713  0.0232  -0.0133 173 HIS A N   
1309 C CA  . HIS A 152 ? 0.2885 0.5931 0.5767 0.0844  0.0173  -0.0059 173 HIS A CA  
1310 C C   . HIS A 152 ? 0.3205 0.6627 0.6711 0.0683  0.0000  0.0013  173 HIS A C   
1311 O O   . HIS A 152 ? 0.2915 0.6374 0.6516 0.0497  0.0081  0.0066  173 HIS A O   
1312 C CB  . HIS A 152 ? 0.3286 0.6423 0.6184 0.0999  0.0470  0.0018  173 HIS A CB  
1313 C CG  . HIS A 152 ? 0.4845 0.7625 0.7256 0.1181  0.0578  -0.0054 173 HIS A CG  
1314 N ND1 . HIS A 152 ? 0.5116 0.7903 0.7529 0.1391  0.0501  -0.0059 173 HIS A ND1 
1315 C CD2 . HIS A 152 ? 0.4588 0.6970 0.6524 0.1183  0.0731  -0.0126 173 HIS A CD2 
1316 C CE1 . HIS A 152 ? 0.4932 0.7335 0.6900 0.1509  0.0636  -0.0106 173 HIS A CE1 
1317 N NE2 . HIS A 152 ? 0.4595 0.6753 0.6305 0.1376  0.0766  -0.0153 173 HIS A NE2 
1318 N N   . ARG A 153 ? 0.2742 0.6417 0.6677 0.0763  -0.0256 0.0010  174 ARG A N   
1319 C CA  . ARG A 153 ? 0.2484 0.6536 0.7161 0.0617  -0.0459 0.0078  174 ARG A CA  
1320 C C   . ARG A 153 ? 0.3116 0.7477 0.8240 0.0513  -0.0149 0.0277  174 ARG A C   
1321 O O   . ARG A 153 ? 0.2958 0.7441 0.8068 0.0667  0.0148  0.0375  174 ARG A O   
1322 C CB  . ARG A 153 ? 0.2572 0.6897 0.7709 0.0777  -0.0737 0.0051  174 ARG A CB  
1323 C CG  . ARG A 153 ? 0.3807 0.8459 0.9755 0.0614  -0.1063 0.0073  174 ARG A CG  
1324 C CD  . ARG A 153 ? 0.4831 0.9657 1.1057 0.0802  -0.1357 0.0008  174 ARG A CD  
1325 N NE  . ARG A 153 ? 0.6720 1.1224 1.2297 0.1073  -0.1512 -0.0163 174 ARG A NE  
1326 C CZ  . ARG A 153 ? 0.7305 1.1694 1.2726 0.1249  -0.1847 -0.0275 174 ARG A CZ  
1327 N NH1 . ARG A 153 ? 0.7616 1.1676 1.2362 0.1528  -0.1914 -0.0392 174 ARG A NH1 
1328 N NH2 . ARG A 153 ? 0.6740 1.1290 1.2603 0.1154  -0.2082 -0.0264 174 ARG A NH2 
1329 N N   . SER A 154 ? 0.3289 0.7746 0.8766 0.0280  -0.0209 0.0346  175 SER A N   
1330 C CA  . SER A 154 ? 0.3704 0.8463 0.9669 0.0179  0.0084  0.0580  175 SER A CA  
1331 C C   . SER A 154 ? 0.3773 0.8272 0.9109 0.0199  0.0464  0.0621  175 SER A C   
1332 O O   . SER A 154 ? 0.3711 0.8397 0.9312 0.0158  0.0736  0.0822  175 SER A O   
1333 C CB  . SER A 154 ? 0.3880 0.9091 1.0469 0.0318  0.0224  0.0748  175 SER A CB  
1334 O OG  . SER A 154 ? 0.3689 0.9022 1.0700 0.0283  -0.0159 0.0664  175 SER A OG  
1335 N N   . GLU A 155 ? 0.3197 0.7267 0.7732 0.0280  0.0481  0.0441  176 GLU A N   
1336 C CA  . GLU A 155 ? 0.3001 0.6771 0.6944 0.0276  0.0733  0.0423  176 GLU A CA  
1337 C C   . GLU A 155 ? 0.3325 0.6889 0.7107 0.0052  0.0578  0.0359  176 GLU A C   
1338 O O   . GLU A 155 ? 0.3554 0.7152 0.7602 -0.0083 0.0270  0.0309  176 GLU A O   
1339 C CB  . GLU A 155 ? 0.2640 0.6036 0.5895 0.0442  0.0802  0.0260  176 GLU A CB  
1340 C CG  . GLU A 155 ? 0.3381 0.6938 0.6748 0.0687  0.0945  0.0313  176 GLU A CG  
1341 C CD  . GLU A 155 ? 0.5912 0.9669 0.9379 0.0835  0.1297  0.0485  176 GLU A CD  
1342 O OE1 . GLU A 155 ? 0.6687 1.0357 0.9962 0.0788  0.1459  0.0536  176 GLU A OE1 
1343 O OE2 . GLU A 155 ? 0.6794 1.0792 1.0503 0.1032  0.1419  0.0578  176 GLU A OE2 
1344 N N   . ASP A 156 ? 0.2895 0.6220 0.6208 0.0040  0.0770  0.0345  177 ASP A N   
1345 C CA  . ASP A 156 ? 0.3029 0.6141 0.6126 -0.0146 0.0644  0.0280  177 ASP A CA  
1346 C C   . ASP A 156 ? 0.3666 0.6394 0.6199 -0.0157 0.0457  0.0056  177 ASP A C   
1347 O O   . ASP A 156 ? 0.3598 0.6110 0.5715 -0.0026 0.0559  -0.0041 177 ASP A O   
1348 C CB  . ASP A 156 ? 0.3738 0.6767 0.6570 -0.0125 0.0923  0.0366  177 ASP A CB  
1349 C CG  . ASP A 156 ? 0.5381 0.8761 0.8808 -0.0170 0.1101  0.0640  177 ASP A CG  
1350 O OD1 . ASP A 156 ? 0.5136 0.8866 0.9282 -0.0230 0.1013  0.0768  177 ASP A OD1 
1351 O OD2 . ASP A 156 ? 0.6020 0.9321 0.9208 -0.0128 0.1335  0.0737  177 ASP A OD2 
1352 N N   . LEU A 157 ? 0.3419 0.6063 0.5979 -0.0302 0.0189  -0.0010 178 LEU A N   
1353 C CA  . LEU A 157 ? 0.3184 0.5490 0.5246 -0.0324 0.0040  -0.0174 178 LEU A CA  
1354 C C   . LEU A 157 ? 0.3942 0.6045 0.5667 -0.0437 0.0102  -0.0208 178 LEU A C   
1355 O O   . LEU A 157 ? 0.3567 0.5742 0.5478 -0.0568 0.0052  -0.0139 178 LEU A O   
1356 C CB  . LEU A 157 ? 0.2984 0.5296 0.5198 -0.0359 -0.0297 -0.0228 178 LEU A CB  
1357 C CG  . LEU A 157 ? 0.3146 0.5130 0.4862 -0.0361 -0.0440 -0.0356 178 LEU A CG  
1358 C CD1 . LEU A 157 ? 0.2980 0.4783 0.4356 -0.0198 -0.0345 -0.0412 178 LEU A CD1 
1359 C CD2 . LEU A 157 ? 0.3801 0.5757 0.5604 -0.0381 -0.0786 -0.0407 178 LEU A CD2 
1360 N N   . VAL A 158 ? 0.3288 0.5128 0.4548 -0.0381 0.0196  -0.0315 179 VAL A N   
1361 C CA  . VAL A 158 ? 0.3178 0.4818 0.4099 -0.0461 0.0222  -0.0376 179 VAL A CA  
1362 C C   . VAL A 158 ? 0.4067 0.5457 0.4685 -0.0482 0.0072  -0.0506 179 VAL A C   
1363 O O   . VAL A 158 ? 0.3595 0.4875 0.4112 -0.0386 0.0097  -0.0559 179 VAL A O   
1364 C CB  . VAL A 158 ? 0.4415 0.5960 0.5076 -0.0355 0.0453  -0.0396 179 VAL A CB  
1365 C CG1 . VAL A 158 ? 0.3889 0.5198 0.4160 -0.0412 0.0428  -0.0496 179 VAL A CG1 
1366 C CG2 . VAL A 158 ? 0.4518 0.6327 0.5465 -0.0289 0.0656  -0.0217 179 VAL A CG2 
1367 N N   . LEU A 159 ? 0.3379 0.4691 0.3893 -0.0592 -0.0072 -0.0531 180 LEU A N   
1368 C CA  . LEU A 159 ? 0.2988 0.4084 0.3214 -0.0597 -0.0175 -0.0624 180 LEU A CA  
1369 C C   . LEU A 159 ? 0.3857 0.4805 0.3813 -0.0655 -0.0111 -0.0696 180 LEU A C   
1370 O O   . LEU A 159 ? 0.3689 0.4675 0.3627 -0.0726 -0.0108 -0.0662 180 LEU A O   
1371 C CB  . LEU A 159 ? 0.2705 0.3793 0.2940 -0.0629 -0.0402 -0.0615 180 LEU A CB  
1372 C CG  . LEU A 159 ? 0.3808 0.5043 0.4321 -0.0566 -0.0555 -0.0568 180 LEU A CG  
1373 C CD1 . LEU A 159 ? 0.3336 0.4484 0.3759 -0.0564 -0.0827 -0.0600 180 LEU A CD1 
1374 C CD2 . LEU A 159 ? 0.3608 0.4824 0.4095 -0.0408 -0.0488 -0.0568 180 LEU A CD2 
1375 N N   . ASP A 160 ? 0.3171 0.3947 0.2951 -0.0615 -0.0070 -0.0788 181 ASP A N   
1376 C CA  . ASP A 160 ? 0.3397 0.4019 0.2937 -0.0643 -0.0051 -0.0893 181 ASP A CA  
1377 C C   . ASP A 160 ? 0.3904 0.4424 0.3341 -0.0701 -0.0174 -0.0933 181 ASP A C   
1378 O O   . ASP A 160 ? 0.3860 0.4338 0.3373 -0.0669 -0.0193 -0.0912 181 ASP A O   
1379 C CB  . ASP A 160 ? 0.4013 0.4501 0.3500 -0.0554 0.0041  -0.0990 181 ASP A CB  
1380 C CG  . ASP A 160 ? 0.6090 0.6406 0.5325 -0.0545 0.0016  -0.1132 181 ASP A CG  
1381 O OD1 . ASP A 160 ? 0.5848 0.6168 0.4927 -0.0601 -0.0040 -0.1139 181 ASP A OD1 
1382 O OD2 . ASP A 160 ? 0.6391 0.6549 0.5571 -0.0460 0.0038  -0.1247 181 ASP A OD2 
1383 N N   . CYS A 161 ? 0.3120 0.3926 0.2863 -0.0057 0.0179  -0.0304 182 CYS A N   
1384 C CA  . CYS A 161 ? 0.3225 0.3802 0.2906 -0.0116 0.0130  -0.0249 182 CYS A CA  
1385 C C   . CYS A 161 ? 0.3291 0.3762 0.2860 -0.0055 0.0091  -0.0315 182 CYS A C   
1386 O O   . CYS A 161 ? 0.3322 0.3637 0.2842 -0.0095 0.0063  -0.0270 182 CYS A O   
1387 C CB  . CYS A 161 ? 0.3326 0.3864 0.2902 -0.0235 0.0170  -0.0135 182 CYS A CB  
1388 S SG  . CYS A 161 ? 0.3659 0.3960 0.3159 -0.0271 0.0123  -0.0082 182 CYS A SG  
1389 N N   . LEU A 162 ? 0.3197 0.3763 0.2717 0.0060  0.0083  -0.0430 183 LEU A N   
1390 C CA  . LEU A 162 ? 0.3430 0.3886 0.2815 0.0138  0.0014  -0.0512 183 LEU A CA  
1391 C C   . LEU A 162 ? 0.3987 0.4260 0.3585 0.0191  -0.0145 -0.0590 183 LEU A C   
1392 O O   . LEU A 162 ? 0.3870 0.4160 0.3667 0.0263  -0.0220 -0.0671 183 LEU A O   
1393 C CB  . LEU A 162 ? 0.3540 0.4170 0.2749 0.0280  0.0048  -0.0624 183 LEU A CB  
1394 C CG  . LEU A 162 ? 0.3621 0.4146 0.2609 0.0393  -0.0037 -0.0728 183 LEU A CG  
1395 C CD1 . LEU A 162 ? 0.3946 0.4406 0.2729 0.0291  0.0018  -0.0593 183 LEU A CD1 
1396 C CD2 . LEU A 162 ? 0.4385 0.5116 0.3186 0.0591  -0.0009 -0.0870 183 LEU A CD2 
1397 N N   . LEU A 163 ? 0.3297 0.3402 0.2896 0.0152  -0.0204 -0.0551 184 LEU A N   
1398 C CA  . LEU A 163 ? 0.3008 0.2956 0.2862 0.0198  -0.0370 -0.0604 184 LEU A CA  
1399 C C   . LEU A 163 ? 0.3880 0.3736 0.3588 0.0304  -0.0487 -0.0742 184 LEU A C   
1400 O O   . LEU A 163 ? 0.3723 0.3610 0.3125 0.0307  -0.0418 -0.0736 184 LEU A O   
1401 C CB  . LEU A 163 ? 0.3064 0.2927 0.3095 0.0088  -0.0354 -0.0441 184 LEU A CB  
1402 C CG  . LEU A 163 ? 0.3672 0.3620 0.3759 0.0006  -0.0241 -0.0303 184 LEU A CG  
1403 C CD1 . LEU A 163 ? 0.3455 0.3351 0.3695 -0.0052 -0.0222 -0.0150 184 LEU A CD1 
1404 C CD2 . LEU A 163 ? 0.3971 0.3966 0.4268 0.0048  -0.0298 -0.0338 184 LEU A CD2 
1405 N N   . SER A 164 ? 0.3557 0.3281 0.3501 0.0388  -0.0688 -0.0854 185 SER A N   
1406 C CA  . SER A 164 ? 0.4310 0.3939 0.4099 0.0530  -0.0844 -0.1035 185 SER A CA  
1407 C C   . SER A 164 ? 0.4466 0.4002 0.4107 0.0480  -0.0847 -0.0972 185 SER A C   
1408 O O   . SER A 164 ? 0.4361 0.3851 0.3729 0.0593  -0.0926 -0.1092 185 SER A O   
1409 C CB  . SER A 164 ? 0.4723 0.4183 0.4877 0.0622  -0.1115 -0.1172 185 SER A CB  
1410 O OG  . SER A 164 ? 0.5146 0.4507 0.5700 0.0486  -0.1168 -0.1004 185 SER A OG  
1411 N N   . TRP A 165 ? 0.3894 0.3406 0.3696 0.0332  -0.0768 -0.0789 186 TRP A N   
1412 C CA  . TRP A 165 ? 0.3716 0.3124 0.3452 0.0299  -0.0805 -0.0741 186 TRP A CA  
1413 C C   . TRP A 165 ? 0.3664 0.3149 0.3032 0.0232  -0.0619 -0.0642 186 TRP A C   
1414 O O   . TRP A 165 ? 0.3862 0.3265 0.3102 0.0215  -0.0641 -0.0608 186 TRP A O   
1415 C CB  . TRP A 165 ? 0.3759 0.3112 0.3925 0.0207  -0.0843 -0.0606 186 TRP A CB  
1416 C CG  . TRP A 165 ? 0.3533 0.3010 0.3822 0.0101  -0.0663 -0.0430 186 TRP A CG  
1417 C CD1 . TRP A 165 ? 0.3535 0.3067 0.4114 0.0079  -0.0661 -0.0366 186 TRP A CD1 
1418 C CD2 . TRP A 165 ? 0.3222 0.2760 0.3330 0.0024  -0.0489 -0.0307 186 TRP A CD2 
1419 N NE1 . TRP A 165 ? 0.3070 0.2712 0.3611 0.0000  -0.0481 -0.0208 186 TRP A NE1 
1420 C CE2 . TRP A 165 ? 0.3190 0.2830 0.3442 -0.0027 -0.0383 -0.0188 186 TRP A CE2 
1421 C CE3 . TRP A 165 ? 0.3162 0.2664 0.2987 0.0003  -0.0432 -0.0293 186 TRP A CE3 
1422 C CZ2 . TRP A 165 ? 0.2927 0.2628 0.3027 -0.0079 -0.0233 -0.0081 186 TRP A CZ2 
1423 C CZ3 . TRP A 165 ? 0.3020 0.2566 0.2745 -0.0060 -0.0297 -0.0186 186 TRP A CZ3 
1424 C CH2 . TRP A 165 ? 0.3292 0.2937 0.3144 -0.0092 -0.0200 -0.0093 186 TRP A CH2 
1425 N N   . HIS A 166 ? 0.3623 0.3259 0.2862 0.0192  -0.0459 -0.0591 187 HIS A N   
1426 C CA  . HIS A 166 ? 0.3717 0.3412 0.2691 0.0112  -0.0317 -0.0478 187 HIS A CA  
1427 C C   . HIS A 166 ? 0.4164 0.3846 0.2811 0.0181  -0.0343 -0.0515 187 HIS A C   
1428 O O   . HIS A 166 ? 0.4402 0.4017 0.2916 0.0116  -0.0320 -0.0418 187 HIS A O   
1429 C CB  . HIS A 166 ? 0.3887 0.3759 0.2819 0.0061  -0.0168 -0.0418 187 HIS A CB  
1430 C CG  . HIS A 166 ? 0.3904 0.3787 0.3076 -0.0017 -0.0128 -0.0346 187 HIS A CG  
1431 N ND1 . HIS A 166 ? 0.3629 0.3650 0.2837 -0.0052 -0.0041 -0.0312 187 HIS A ND1 
1432 C CD2 . HIS A 166 ? 0.3550 0.3342 0.2921 -0.0056 -0.0157 -0.0288 187 HIS A CD2 
1433 C CE1 . HIS A 166 ? 0.3904 0.3894 0.3289 -0.0103 -0.0034 -0.0247 187 HIS A CE1 
1434 N NE2 . HIS A 166 ? 0.3511 0.3379 0.2990 -0.0101 -0.0090 -0.0224 187 HIS A NE2 
1435 N N   . ARG A 167 ? 0.4308 0.4045 0.2825 0.0330  -0.0407 -0.0660 188 ARG A N   
1436 C CA  . ARG A 167 ? 0.5457 0.5216 0.3591 0.0433  -0.0423 -0.0691 188 ARG A CA  
1437 C C   . ARG A 167 ? 0.6025 0.5565 0.4125 0.0436  -0.0574 -0.0698 188 ARG A C   
1438 O O   . ARG A 167 ? 0.7095 0.6624 0.4900 0.0440  -0.0551 -0.0622 188 ARG A O   
1439 C CB  . ARG A 167 ? 0.5842 0.5696 0.3819 0.0644  -0.0489 -0.0887 188 ARG A CB  
1440 N N   . ALA A 168 ? 0.5432 0.4811 0.3868 0.0422  -0.0724 -0.0758 189 ALA A N   
1441 C CA  . ALA A 168 ? 0.5093 0.4281 0.3563 0.0428  -0.0880 -0.0765 189 ALA A CA  
1442 C C   . ALA A 168 ? 0.5237 0.4378 0.3855 0.0277  -0.0798 -0.0597 189 ALA A C   
1443 O O   . ALA A 168 ? 0.6046 0.5054 0.4666 0.0277  -0.0898 -0.0579 189 ALA A O   
1444 C CB  . ALA A 168 ? 0.5046 0.4101 0.3846 0.0508  -0.1115 -0.0912 189 ALA A CB  
1445 N N   . SER A 169 ? 0.3822 0.3067 0.2536 0.0168  -0.0629 -0.0485 190 SER A N   
1446 C CA  . SER A 169 ? 0.3730 0.2924 0.2581 0.0068  -0.0575 -0.0367 190 SER A CA  
1447 C C   . SER A 169 ? 0.4768 0.3909 0.3320 0.0025  -0.0537 -0.0280 190 SER A C   
1448 O O   . SER A 169 ? 0.4849 0.4070 0.3134 0.0025  -0.0472 -0.0247 190 SER A O   
1449 C CB  . SER A 169 ? 0.3847 0.3152 0.2885 -0.0006 -0.0440 -0.0296 190 SER A CB  
1450 O OG  . SER A 169 ? 0.3890 0.3157 0.3090 -0.0050 -0.0410 -0.0216 190 SER A OG  
1451 N N   . LYS A 170 ? 0.4394 0.3416 0.3017 -0.0006 -0.0581 -0.0229 191 LYS A N   
1452 C CA  . LYS A 170 ? 0.4070 0.2995 0.2456 -0.0048 -0.0589 -0.0140 191 LYS A CA  
1453 C C   . LYS A 170 ? 0.4584 0.3508 0.3001 -0.0143 -0.0494 -0.0046 191 LYS A C   
1454 O O   . LYS A 170 ? 0.4410 0.3364 0.3032 -0.0150 -0.0450 -0.0059 191 LYS A O   
1455 C CB  . LYS A 170 ? 0.4102 0.2863 0.2536 -0.0002 -0.0738 -0.0161 191 LYS A CB  
1456 C CG  . LYS A 170 ? 0.4657 0.3374 0.3076 0.0105  -0.0891 -0.0275 191 LYS A CG  
1457 C CD  . LYS A 170 ? 0.4917 0.3653 0.2930 0.0168  -0.0912 -0.0287 191 LYS A CD  
1458 C CE  . LYS A 170 ? 0.6305 0.4988 0.4340 0.0303  -0.1091 -0.0450 191 LYS A CE  
1459 N NZ  . LYS A 170 ? 0.6880 0.5636 0.4513 0.0411  -0.1090 -0.0501 191 LYS A NZ  
1460 N N   . GLY A 171 ? 0.4243 0.3131 0.2460 -0.0208 -0.0478 0.0059  192 GLY A N   
1461 C CA  . GLY A 171 ? 0.4043 0.2876 0.2313 -0.0290 -0.0450 0.0129  192 GLY A CA  
1462 C C   . GLY A 171 ? 0.4538 0.3513 0.2879 -0.0346 -0.0340 0.0144  192 GLY A C   
1463 O O   . GLY A 171 ? 0.4389 0.3306 0.2804 -0.0384 -0.0345 0.0157  192 GLY A O   
1464 N N   . LEU A 172 ? 0.4540 0.3694 0.2855 -0.0334 -0.0258 0.0128  193 LEU A N   
1465 C CA  . LEU A 172 ? 0.3900 0.3189 0.2306 -0.0387 -0.0169 0.0147  193 LEU A CA  
1466 C C   . LEU A 172 ? 0.4267 0.3564 0.2621 -0.0498 -0.0157 0.0289  193 LEU A C   
1467 O O   . LEU A 172 ? 0.4353 0.3655 0.2563 -0.0522 -0.0164 0.0394  193 LEU A O   
1468 C CB  . LEU A 172 ? 0.4038 0.3522 0.2455 -0.0336 -0.0095 0.0091  193 LEU A CB  
1469 C CG  . LEU A 172 ? 0.3876 0.3351 0.2440 -0.0245 -0.0131 -0.0034 193 LEU A CG  
1470 C CD1 . LEU A 172 ? 0.4282 0.3916 0.2833 -0.0178 -0.0098 -0.0104 193 LEU A CD1 
1471 C CD2 . LEU A 172 ? 0.3513 0.2974 0.2266 -0.0263 -0.0110 -0.0036 193 LEU A CD2 
1472 N N   . THR A 173 ? 0.5098 0.4412 0.3575 -0.0561 -0.0146 0.0307  194 THR A N   
1473 C CA  . THR A 173 ? 0.5220 0.4555 0.3741 -0.0681 -0.0158 0.0452  194 THR A CA  
1474 C C   . THR A 173 ? 0.5544 0.5129 0.4172 -0.0714 -0.0053 0.0481  194 THR A C   
1475 O O   . THR A 173 ? 0.7754 0.7546 0.6323 -0.0695 0.0047  0.0534  194 THR A O   
1476 C CB  . THR A 173 ? 0.5291 0.4396 0.3897 -0.0729 -0.0294 0.0449  194 THR A CB  
1477 O OG1 . THR A 173 ? 0.5150 0.4232 0.3811 -0.0659 -0.0302 0.0311  194 THR A OG1 
1478 C CG2 . THR A 173 ? 0.5426 0.4303 0.3937 -0.0689 -0.0398 0.0434  194 THR A CG2 
1479 N N   . ASP A 174 ? 0.4394 0.3971 0.3169 -0.0746 -0.0083 0.0444  195 ASP A N   
1480 C CA  . ASP A 174 ? 0.4151 0.3966 0.3070 -0.0787 -0.0004 0.0486  195 ASP A CA  
1481 C C   . ASP A 174 ? 0.3751 0.3621 0.2712 -0.0699 0.0026  0.0342  195 ASP A C   
1482 O O   . ASP A 174 ? 0.4091 0.3806 0.3017 -0.0642 -0.0032 0.0248  195 ASP A O   
1483 C CB  . ASP A 174 ? 0.4246 0.4016 0.3363 -0.0914 -0.0100 0.0585  195 ASP A CB  
1484 C CG  . ASP A 174 ? 0.6011 0.5783 0.5191 -0.1035 -0.0125 0.0791  195 ASP A CG  
1485 O OD1 . ASP A 174 ? 0.6220 0.6191 0.5324 -0.1033 0.0000  0.0906  195 ASP A OD1 
1486 O OD2 . ASP A 174 ? 0.7826 0.7399 0.7133 -0.1123 -0.0284 0.0843  195 ASP A OD2 
1487 N N   . TYR A 175 ? 0.3981 0.4091 0.3037 -0.0688 0.0115  0.0346  196 TYR A N   
1488 C CA  . TYR A 175 ? 0.3824 0.3994 0.2987 -0.0640 0.0118  0.0254  196 TYR A CA  
1489 C C   . TYR A 175 ? 0.3600 0.3786 0.2930 -0.0732 0.0053  0.0312  196 TYR A C   
1490 O O   . TYR A 175 ? 0.3761 0.4118 0.3236 -0.0819 0.0087  0.0431  196 TYR A O   
1491 C CB  . TYR A 175 ? 0.3568 0.3979 0.2779 -0.0568 0.0218  0.0213  196 TYR A CB  
1492 C CG  . TYR A 175 ? 0.3429 0.3820 0.2507 -0.0456 0.0241  0.0124  196 TYR A CG  
1493 C CD1 . TYR A 175 ? 0.4038 0.4477 0.2956 -0.0431 0.0281  0.0160  196 TYR A CD1 
1494 C CD2 . TYR A 175 ? 0.3929 0.4259 0.3060 -0.0373 0.0206  0.0014  196 TYR A CD2 
1495 C CE1 . TYR A 175 ? 0.3970 0.4372 0.2761 -0.0307 0.0261  0.0047  196 TYR A CE1 
1496 C CE2 . TYR A 175 ? 0.3090 0.3385 0.2162 -0.0273 0.0183  -0.0075 196 TYR A CE2 
1497 C CZ  . TYR A 175 ? 0.3583 0.3902 0.2480 -0.0234 0.0199  -0.0078 196 TYR A CZ  
1498 O OH  . TYR A 175 ? 0.4093 0.4347 0.2933 -0.0119 0.0133  -0.0194 196 TYR A OH  
1499 N N   . SER A 176 ? 0.3562 0.3594 0.2884 -0.0704 -0.0043 0.0237  197 SER A N   
1500 C CA  . SER A 176 ? 0.4042 0.4064 0.3514 -0.0764 -0.0148 0.0254  197 SER A CA  
1501 C C   . SER A 176 ? 0.4084 0.4243 0.3633 -0.0701 -0.0117 0.0194  197 SER A C   
1502 O O   . SER A 176 ? 0.3869 0.3993 0.3310 -0.0602 -0.0081 0.0123  197 SER A O   
1503 C CB  . SER A 176 ? 0.3967 0.3712 0.3326 -0.0739 -0.0305 0.0190  197 SER A CB  
1504 O OG  . SER A 176 ? 0.4229 0.3828 0.3574 -0.0810 -0.0372 0.0253  197 SER A OG  
1505 N N   . PHE A 177 ? 0.3394 0.3714 0.3166 -0.0761 -0.0137 0.0239  198 PHE A N   
1506 C CA  . PHE A 177 ? 0.3251 0.3658 0.3104 -0.0700 -0.0152 0.0179  198 PHE A CA  
1507 C C   . PHE A 177 ? 0.3594 0.3880 0.3513 -0.0729 -0.0332 0.0161  198 PHE A C   
1508 O O   . PHE A 177 ? 0.3584 0.3864 0.3686 -0.0839 -0.0427 0.0229  198 PHE A O   
1509 C CB  . PHE A 177 ? 0.3119 0.3830 0.3191 -0.0707 -0.0044 0.0215  198 PHE A CB  
1510 C CG  . PHE A 177 ? 0.3616 0.4428 0.3590 -0.0628 0.0093  0.0182  198 PHE A CG  
1511 C CD1 . PHE A 177 ? 0.3162 0.3986 0.3121 -0.0520 0.0110  0.0091  198 PHE A CD1 
1512 C CD2 . PHE A 177 ? 0.3324 0.4197 0.3221 -0.0655 0.0181  0.0244  198 PHE A CD2 
1513 C CE1 . PHE A 177 ? 0.2590 0.3472 0.2481 -0.0431 0.0190  0.0031  198 PHE A CE1 
1514 C CE2 . PHE A 177 ? 0.3416 0.4364 0.3184 -0.0550 0.0278  0.0180  198 PHE A CE2 
1515 C CZ  . PHE A 177 ? 0.2840 0.3785 0.2622 -0.0435 0.0269  0.0060  198 PHE A CZ  
1516 N N   . TYR A 178 ? 0.3634 0.3835 0.3426 -0.0627 -0.0388 0.0082  199 TYR A N   
1517 C CA  . TYR A 178 ? 0.3567 0.3646 0.3351 -0.0604 -0.0576 0.0032  199 TYR A CA  
1518 C C   . TYR A 178 ? 0.4330 0.4544 0.4239 -0.0563 -0.0598 0.0021  199 TYR A C   
1519 O O   . TYR A 178 ? 0.3515 0.3818 0.3384 -0.0492 -0.0491 0.0021  199 TYR A O   
1520 C CB  . TYR A 178 ? 0.3805 0.3651 0.3249 -0.0478 -0.0649 -0.0051 199 TYR A CB  
1521 C CG  . TYR A 178 ? 0.4479 0.4157 0.3802 -0.0497 -0.0667 -0.0063 199 TYR A CG  
1522 C CD1 . TYR A 178 ? 0.4789 0.4485 0.4009 -0.0478 -0.0512 -0.0037 199 TYR A CD1 
1523 C CD2 . TYR A 178 ? 0.4212 0.3696 0.3555 -0.0532 -0.0871 -0.0107 199 TYR A CD2 
1524 C CE1 . TYR A 178 ? 0.4183 0.3711 0.3300 -0.0489 -0.0548 -0.0051 199 TYR A CE1 
1525 C CE2 . TYR A 178 ? 0.4044 0.3348 0.3298 -0.0546 -0.0915 -0.0120 199 TYR A CE2 
1526 C CZ  . TYR A 178 ? 0.4301 0.3638 0.3436 -0.0521 -0.0746 -0.0090 199 TYR A CZ  
1527 O OH  . TYR A 178 ? 0.6246 0.5402 0.5309 -0.0529 -0.0807 -0.0105 199 TYR A OH  
1528 N N   . ARG A 179 ? 0.3349 0.3548 0.3423 -0.0603 -0.0772 0.0009  200 ARG A N   
1529 C CA  . ARG A 179 ? 0.3125 0.3377 0.3251 -0.0535 -0.0859 -0.0023 200 ARG A CA  
1530 C C   . ARG A 179 ? 0.3856 0.3874 0.3611 -0.0395 -0.0985 -0.0104 200 ARG A C   
1531 O O   . ARG A 179 ? 0.4742 0.4557 0.4353 -0.0379 -0.1133 -0.0168 200 ARG A O   
1532 C CB  . ARG A 179 ? 0.3251 0.3608 0.3758 -0.0636 -0.1007 0.0002  200 ARG A CB  
1533 C CG  . ARG A 179 ? 0.3877 0.4276 0.4461 -0.0567 -0.1132 -0.0036 200 ARG A CG  
1534 C CD  . ARG A 179 ? 0.4056 0.4704 0.4787 -0.0535 -0.0953 0.0001  200 ARG A CD  
1535 N NE  . ARG A 179 ? 0.5113 0.5798 0.5943 -0.0469 -0.1083 -0.0024 200 ARG A NE  
1536 C CZ  . ARG A 179 ? 0.5027 0.5891 0.6259 -0.0528 -0.1174 -0.0008 200 ARG A CZ  
1537 N NH1 . ARG A 179 ? 0.4920 0.5976 0.6511 -0.0660 -0.1126 0.0059  200 ARG A NH1 
1538 N NH2 . ARG A 179 ? 0.5080 0.5948 0.6372 -0.0453 -0.1313 -0.0038 200 ARG A NH2 
1539 N N   . VAL A 180 ? 0.3925 0.3975 0.3520 -0.0280 -0.0931 -0.0095 201 VAL A N   
1540 C CA  . VAL A 180 ? 0.4328 0.4214 0.3534 -0.0118 -0.1019 -0.0141 201 VAL A CA  
1541 C C   . VAL A 180 ? 0.4681 0.4558 0.3885 -0.0051 -0.1198 -0.0165 201 VAL A C   
1542 O O   . VAL A 180 ? 0.4163 0.4174 0.3490 -0.0039 -0.1143 -0.0099 201 VAL A O   
1543 C CB  . VAL A 180 ? 0.4194 0.4133 0.3202 -0.0025 -0.0822 -0.0061 201 VAL A CB  
1544 C CG1 . VAL A 180 ? 0.4479 0.4305 0.3072 0.0159  -0.0882 -0.0081 201 VAL A CG1 
1545 C CG2 . VAL A 180 ? 0.4569 0.4523 0.3615 -0.0091 -0.0661 -0.0040 201 VAL A CG2 
1546 N N   . TRP A 181 ? 0.3983 0.3689 0.3075 -0.0003 -0.1443 -0.0270 202 TRP A N   
1547 C CA  . TRP A 181 ? 0.4126 0.3808 0.3252 0.0053  -0.1662 -0.0311 202 TRP A CA  
1548 C C   . TRP A 181 ? 0.4699 0.4347 0.3403 0.0257  -0.1661 -0.0289 202 TRP A C   
1549 O O   . TRP A 181 ? 0.5549 0.5190 0.3938 0.0358  -0.1500 -0.0245 202 TRP A O   
1550 C CB  . TRP A 181 ? 0.4768 0.4242 0.3921 0.0046  -0.1968 -0.0447 202 TRP A CB  
1551 C CG  . TRP A 181 ? 0.4842 0.4370 0.4446 -0.0170 -0.1958 -0.0412 202 TRP A CG  
1552 C CD1 . TRP A 181 ? 0.5165 0.4558 0.4747 -0.0225 -0.1970 -0.0442 202 TRP A CD1 
1553 C CD2 . TRP A 181 ? 0.4742 0.4506 0.4884 -0.0345 -0.1915 -0.0314 202 TRP A CD2 
1554 N NE1 . TRP A 181 ? 0.4580 0.4100 0.4652 -0.0435 -0.1950 -0.0347 202 TRP A NE1 
1555 C CE2 . TRP A 181 ? 0.4694 0.4464 0.5113 -0.0506 -0.1902 -0.0267 202 TRP A CE2 
1556 C CE3 . TRP A 181 ? 0.5198 0.5178 0.5627 -0.0369 -0.1897 -0.0260 202 TRP A CE3 
1557 C CZ2 . TRP A 181 ? 0.4720 0.4749 0.5677 -0.0686 -0.1836 -0.0142 202 TRP A CZ2 
1558 C CZ3 . TRP A 181 ? 0.5488 0.5719 0.6460 -0.0535 -0.1843 -0.0169 202 TRP A CZ3 
1559 C CH2 . TRP A 181 ? 0.4747 0.5021 0.5970 -0.0690 -0.1796 -0.0100 202 TRP A CH2 
1560 N N   . GLU A 182 ? 0.5161 0.4799 0.3881 0.0316  -0.1849 -0.0307 203 GLU A N   
1561 C CA  . GLU A 182 ? 0.6185 0.5821 0.4541 0.0501  -0.1859 -0.0245 203 GLU A CA  
1562 C C   . GLU A 182 ? 0.6414 0.5877 0.4206 0.0717  -0.1957 -0.0342 203 GLU A C   
1563 O O   . GLU A 182 ? 0.6938 0.6432 0.4345 0.0897  -0.1904 -0.0260 203 GLU A O   
1564 C CB  . GLU A 182 ? 0.5959 0.5620 0.4505 0.0506  -0.2068 -0.0247 203 GLU A CB  
1565 C CG  . GLU A 182 ? 0.8280 0.8161 0.7323 0.0355  -0.1916 -0.0130 203 GLU A CG  
1566 C CD  . GLU A 182 ? 0.9546 0.9481 0.8931 0.0320  -0.2128 -0.0156 203 GLU A CD  
1567 O OE1 . GLU A 182 ? 1.0078 0.9913 0.9555 0.0305  -0.2384 -0.0275 203 GLU A OE1 
1568 O OE2 . GLU A 182 ? 1.0119 1.0192 0.9720 0.0308  -0.2057 -0.0059 203 GLU A OE2 
1569 N N   . ASN A 183 ? 0.6128 0.5417 0.3874 0.0713  -0.2103 -0.0507 204 ASN A N   
1570 C CA  . ASN A 183 ? 0.7242 0.6369 0.4500 0.0937  -0.2169 -0.0630 204 ASN A CA  
1571 C C   . ASN A 183 ? 0.6675 0.5828 0.3776 0.0956  -0.1956 -0.0609 204 ASN A C   
1572 O O   . ASN A 183 ? 0.7527 0.6568 0.4400 0.1087  -0.1947 -0.0719 204 ASN A O   
1573 C CB  . ASN A 183 ? 0.6958 0.5855 0.4343 0.0935  -0.2435 -0.0823 204 ASN A CB  
1574 C CG  . ASN A 183 ? 0.6103 0.4957 0.3971 0.0694  -0.2533 -0.0851 204 ASN A CG  
1575 O OD1 . ASN A 183 ? 0.5858 0.4790 0.3830 0.0573  -0.2386 -0.0789 204 ASN A OD1 
1576 N ND2 . ASN A 183 ? 0.8289 0.7050 0.6497 0.0610  -0.2771 -0.0915 204 ASN A ND2 
1577 N N   . SER A 184 ? 0.6596 0.5917 0.4013 0.0777  -0.1724 -0.0460 205 SER A N   
1578 C CA  . SER A 184 ? 0.7146 0.6548 0.4540 0.0750  -0.1456 -0.0384 205 SER A CA  
1579 C C   . SER A 184 ? 0.7277 0.6535 0.4807 0.0649  -0.1510 -0.0505 205 SER A C   
1580 O O   . SER A 184 ? 0.7011 0.6324 0.4573 0.0606  -0.1314 -0.0451 205 SER A O   
1581 C CB  . SER A 184 ? 0.8125 0.7590 0.5020 0.1001  -0.1323 -0.0327 205 SER A CB  
1582 O OG  . SER A 184 ? 0.7733 0.7397 0.4641 0.1022  -0.1162 -0.0109 205 SER A OG  
1583 N N   . SER A 185 ? 0.6477 0.5546 0.4125 0.0603  -0.1792 -0.0653 206 SER A N   
1584 C CA  . SER A 185 ? 0.6202 0.5148 0.4078 0.0465  -0.1846 -0.0713 206 SER A CA  
1585 C C   . SER A 185 ? 0.5931 0.5053 0.4296 0.0203  -0.1675 -0.0564 206 SER A C   
1586 O O   . SER A 185 ? 0.5416 0.4731 0.3980 0.0132  -0.1568 -0.0457 206 SER A O   
1587 C CB  . SER A 185 ? 0.6424 0.5118 0.4376 0.0468  -0.2219 -0.0882 206 SER A CB  
1588 O OG  . SER A 185 ? 0.6772 0.5545 0.5132 0.0312  -0.2341 -0.0828 206 SER A OG  
1589 N N   . GLU A 186 ? 0.4784 0.3845 0.3333 0.0074  -0.1655 -0.0560 207 GLU A N   
1590 C CA  . GLU A 186 ? 0.4268 0.3532 0.3209 -0.0137 -0.1466 -0.0412 207 GLU A CA  
1591 C C   . GLU A 186 ? 0.5107 0.4301 0.4399 -0.0319 -0.1594 -0.0391 207 GLU A C   
1592 O O   . GLU A 186 ? 0.5049 0.3999 0.4272 -0.0290 -0.1804 -0.0490 207 GLU A O   
1593 C CB  . GLU A 186 ? 0.5152 0.4532 0.3980 -0.0125 -0.1175 -0.0330 207 GLU A CB  
1594 C CG  . GLU A 186 ? 0.7130 0.6356 0.5700 -0.0037 -0.1157 -0.0391 207 GLU A CG  
1595 C CD  . GLU A 186 ? 0.7514 0.6871 0.6072 -0.0055 -0.0892 -0.0297 207 GLU A CD  
1596 O OE1 . GLU A 186 ? 0.6525 0.6069 0.5155 -0.0062 -0.0727 -0.0204 207 GLU A OE1 
1597 O OE2 . GLU A 186 ? 0.8098 0.7351 0.6600 -0.0061 -0.0876 -0.0321 207 GLU A OE2 
1598 N N   . THR A 187 ? 0.4476 0.3899 0.4157 -0.0493 -0.1474 -0.0256 208 THR A N   
1599 C CA  . THR A 187 ? 0.4951 0.4387 0.5022 -0.0683 -0.1552 -0.0168 208 THR A CA  
1600 C C   . THR A 187 ? 0.4213 0.3855 0.4384 -0.0784 -0.1271 -0.0027 208 THR A C   
1601 O O   . THR A 187 ? 0.3934 0.3814 0.4127 -0.0769 -0.1059 0.0022  208 THR A O   
1602 C CB  . THR A 187 ? 0.4142 0.3713 0.4644 -0.0790 -0.1693 -0.0115 208 THR A CB  
1603 O OG1 . THR A 187 ? 0.5148 0.4497 0.5552 -0.0688 -0.2001 -0.0262 208 THR A OG1 
1604 C CG2 . THR A 187 ? 0.4975 0.4618 0.5954 -0.1009 -0.1743 0.0043  208 THR A CG2 
1605 N N   . LEU A 188 ? 0.3950 0.3484 0.4165 -0.0869 -0.1288 0.0027  209 LEU A N   
1606 C CA  . LEU A 188 ? 0.3859 0.3577 0.4127 -0.0949 -0.1043 0.0160  209 LEU A CA  
1607 C C   . LEU A 188 ? 0.4524 0.4565 0.5214 -0.1091 -0.0956 0.0323  209 LEU A C   
1608 O O   . LEU A 188 ? 0.4267 0.4306 0.5302 -0.1216 -0.1120 0.0407  209 LEU A O   
1609 C CB  . LEU A 188 ? 0.3902 0.3413 0.4123 -0.1007 -0.1110 0.0197  209 LEU A CB  
1610 C CG  . LEU A 188 ? 0.3960 0.3644 0.4216 -0.1087 -0.0888 0.0348  209 LEU A CG  
1611 C CD1 . LEU A 188 ? 0.3930 0.3624 0.3842 -0.0951 -0.0706 0.0263  209 LEU A CD1 
1612 C CD2 . LEU A 188 ? 0.4927 0.4419 0.5271 -0.1194 -0.1009 0.0444  209 LEU A CD2 
1613 N N   . ILE A 189 ? 0.3266 0.3592 0.3963 -0.1063 -0.0715 0.0367  210 ILE A N   
1614 C CA  . ILE A 189 ? 0.3466 0.4141 0.4554 -0.1160 -0.0622 0.0509  210 ILE A CA  
1615 C C   . ILE A 189 ? 0.3708 0.4616 0.4805 -0.1201 -0.0386 0.0649  210 ILE A C   
1616 O O   . ILE A 189 ? 0.3833 0.5058 0.5250 -0.1283 -0.0290 0.0807  210 ILE A O   
1617 C CB  . ILE A 189 ? 0.3606 0.4478 0.4770 -0.1070 -0.0570 0.0434  210 ILE A CB  
1618 C CG1 . ILE A 189 ? 0.4156 0.5040 0.5005 -0.0928 -0.0404 0.0337  210 ILE A CG1 
1619 C CG2 . ILE A 189 ? 0.3871 0.4554 0.5097 -0.1045 -0.0841 0.0332  210 ILE A CG2 
1620 C CD1 . ILE A 189 ? 0.3980 0.4988 0.4901 -0.0832 -0.0401 0.0259  210 ILE A CD1 
1621 N N   . ALA A 190 ? 0.3628 0.4389 0.4381 -0.1138 -0.0303 0.0603  211 ALA A N   
1622 C CA  . ALA A 190 ? 0.3905 0.4830 0.4606 -0.1166 -0.0124 0.0731  211 ALA A CA  
1623 C C   . ALA A 190 ? 0.4089 0.4723 0.4450 -0.1124 -0.0147 0.0671  211 ALA A C   
1624 O O   . ALA A 190 ? 0.3673 0.4090 0.3807 -0.1026 -0.0207 0.0513  211 ALA A O   
1625 C CB  . ALA A 190 ? 0.4055 0.5302 0.4718 -0.1059 0.0094  0.0705  211 ALA A CB  
1626 N N   . LYS A 191 ? 0.3955 0.4612 0.4293 -0.1194 -0.0091 0.0817  212 LYS A N   
1627 C CA  . LYS A 191 ? 0.3696 0.4098 0.3730 -0.1148 -0.0111 0.0766  212 LYS A CA  
1628 C C   . LYS A 191 ? 0.4001 0.4575 0.3984 -0.1184 0.0031  0.0940  212 LYS A C   
1629 O O   . LYS A 191 ? 0.4056 0.4761 0.4273 -0.1316 0.0033  0.1158  212 LYS A O   
1630 C CB  . LYS A 191 ? 0.4342 0.4393 0.4392 -0.1205 -0.0341 0.0741  212 LYS A CB  
1631 C CG  . LYS A 191 ? 0.5020 0.4813 0.4786 -0.1145 -0.0371 0.0682  212 LYS A CG  
1632 C CD  . LYS A 191 ? 0.6347 0.5820 0.6177 -0.1201 -0.0609 0.0677  212 LYS A CD  
1633 C CE  . LYS A 191 ? 0.7027 0.6228 0.6567 -0.1081 -0.0664 0.0532  212 LYS A CE  
1634 N NZ  . LYS A 191 ? 0.8021 0.7161 0.7496 -0.1126 -0.0639 0.0650  212 LYS A NZ  
1635 N N   . GLY A 192 ? 0.3644 0.4224 0.3335 -0.1067 0.0140  0.0861  213 GLY A N   
1636 C CA  . GLY A 192 ? 0.4185 0.4919 0.3762 -0.1071 0.0259  0.1014  213 GLY A CA  
1637 C C   . GLY A 192 ? 0.4028 0.4762 0.3290 -0.0903 0.0343  0.0858  213 GLY A C   
1638 O O   . GLY A 192 ? 0.3887 0.4464 0.3063 -0.0815 0.0291  0.0664  213 GLY A O   
1639 N N   . LYS A 193 ? 0.3889 0.4798 0.2982 -0.0854 0.0459  0.0955  214 LYS A N   
1640 C CA  . LYS A 193 ? 0.4630 0.5496 0.3429 -0.0688 0.0486  0.0790  214 LYS A CA  
1641 C C   . LYS A 193 ? 0.4783 0.5855 0.3592 -0.0542 0.0566  0.0621  214 LYS A C   
1642 O O   . LYS A 193 ? 0.4403 0.5387 0.3041 -0.0404 0.0535  0.0446  214 LYS A O   
1643 C CB  . LYS A 193 ? 0.5503 0.6471 0.4057 -0.0652 0.0559  0.0936  214 LYS A CB  
1644 C CG  . LYS A 193 ? 0.7378 0.8039 0.5867 -0.0753 0.0430  0.1038  214 LYS A CG  
1645 C CD  . LYS A 193 ? 0.8348 0.9055 0.6536 -0.0691 0.0472  0.1155  214 LYS A CD  
1646 C CE  . LYS A 193 ? 0.8581 0.8946 0.6717 -0.0778 0.0314  0.1233  214 LYS A CE  
1647 N NZ  . LYS A 193 ? 0.9786 1.0189 0.7591 -0.0701 0.0343  0.1352  214 LYS A NZ  
1648 N N   . GLU A 194 ? 0.4248 0.5593 0.3289 -0.0569 0.0650  0.0676  215 GLU A N   
1649 C CA  . GLU A 194 ? 0.5201 0.6743 0.4281 -0.0420 0.0711  0.0510  215 GLU A CA  
1650 C C   . GLU A 194 ? 0.3790 0.5077 0.2933 -0.0385 0.0582  0.0310  215 GLU A C   
1651 O O   . GLU A 194 ? 0.3607 0.4751 0.2914 -0.0490 0.0500  0.0328  215 GLU A O   
1652 C CB  . GLU A 194 ? 0.4623 0.6524 0.3988 -0.0460 0.0821  0.0623  215 GLU A CB  
1653 C CG  . GLU A 194 ? 0.4648 0.6884 0.4053 -0.0513 0.0976  0.0886  215 GLU A CG  
1654 C CD  . GLU A 194 ? 0.5891 0.7986 0.5464 -0.0741 0.0902  0.1127  215 GLU A CD  
1655 O OE1 . GLU A 194 ? 0.7351 0.9698 0.6982 -0.0808 0.1018  0.1393  215 GLU A OE1 
1656 O OE2 . GLU A 194 ? 0.6123 0.7864 0.5773 -0.0841 0.0725  0.1058  215 GLU A OE2 
1657 N N   . PRO A 195 ? 0.3571 0.4812 0.2591 -0.0224 0.0553  0.0123  216 PRO A N   
1658 C CA  . PRO A 195 ? 0.3581 0.4609 0.2702 -0.0199 0.0439  -0.0016 216 PRO A CA  
1659 C C   . PRO A 195 ? 0.4237 0.5408 0.3599 -0.0179 0.0446  -0.0064 216 PRO A C   
1660 O O   . PRO A 195 ? 0.4096 0.5152 0.3548 -0.0120 0.0364  -0.0176 216 PRO A O   
1661 C CB  . PRO A 195 ? 0.4324 0.5266 0.3289 -0.0042 0.0382  -0.0174 216 PRO A CB  
1662 C CG  . PRO A 195 ? 0.4502 0.5712 0.3298 0.0078  0.0486  -0.0182 216 PRO A CG  
1663 C CD  . PRO A 195 ? 0.4115 0.5470 0.2887 -0.0058 0.0601  0.0046  216 PRO A CD  
1664 N N   . TYR A 196 ? 0.3522 0.4952 0.3020 -0.0227 0.0536  0.0037  217 TYR A N   
1665 C CA  . TYR A 196 ? 0.3446 0.5023 0.3196 -0.0201 0.0530  -0.0010 217 TYR A CA  
1666 C C   . TYR A 196 ? 0.4198 0.5937 0.4177 -0.0338 0.0562  0.0144  217 TYR A C   
1667 O O   . TYR A 196 ? 0.3940 0.5756 0.3916 -0.0440 0.0617  0.0303  217 TYR A O   
1668 C CB  . TYR A 196 ? 0.3940 0.5773 0.3692 -0.0015 0.0600  -0.0133 217 TYR A CB  
1669 C CG  . TYR A 196 ? 0.4865 0.7014 0.4512 0.0024  0.0762  -0.0032 217 TYR A CG  
1670 C CD1 . TYR A 196 ? 0.6281 0.8767 0.6159 -0.0039 0.0880  0.0120  217 TYR A CD1 
1671 C CD2 . TYR A 196 ? 0.5531 0.7657 0.4860 0.0121  0.0797  -0.0060 217 TYR A CD2 
1672 C CE1 . TYR A 196 ? 0.6085 0.8920 0.5893 -0.0008 0.1060  0.0270  217 TYR A CE1 
1673 C CE2 . TYR A 196 ? 0.6120 0.8573 0.5317 0.0168  0.0967  0.0072  217 TYR A CE2 
1674 C CZ  . TYR A 196 ? 0.6461 0.9277 0.5906 0.0099  0.1109  0.0252  217 TYR A CZ  
1675 O OH  . TYR A 196 ? 0.7800 1.0987 0.7154 0.0139  0.1299  0.0433  217 TYR A OH  
1676 N N   . LEU A 197 ? 0.3526 0.5319 0.3736 -0.0339 0.0510  0.0106  218 LEU A N   
1677 C CA  . LEU A 197 ? 0.3412 0.5361 0.3895 -0.0459 0.0505  0.0235  218 LEU A CA  
1678 C C   . LEU A 197 ? 0.3516 0.5807 0.4245 -0.0363 0.0575  0.0195  218 LEU A C   
1679 O O   . LEU A 197 ? 0.3066 0.5317 0.3803 -0.0239 0.0528  0.0041  218 LEU A O   
1680 C CB  . LEU A 197 ? 0.2622 0.4282 0.3143 -0.0547 0.0337  0.0225  218 LEU A CB  
1681 C CG  . LEU A 197 ? 0.4579 0.6369 0.5429 -0.0642 0.0266  0.0306  218 LEU A CG  
1682 C CD1 . LEU A 197 ? 0.5221 0.7066 0.6189 -0.0792 0.0271  0.0481  218 LEU A CD1 
1683 C CD2 . LEU A 197 ? 0.5601 0.7119 0.6418 -0.0652 0.0091  0.0237  218 LEU A CD2 
1684 N N   . THR A 198 ? 0.3107 0.5752 0.4068 -0.0411 0.0687  0.0341  219 THR A N   
1685 C CA  . THR A 198 ? 0.3279 0.6280 0.4537 -0.0322 0.0751  0.0313  219 THR A CA  
1686 C C   . THR A 198 ? 0.3408 0.6496 0.5065 -0.0482 0.0668  0.0450  219 THR A C   
1687 O O   . THR A 198 ? 0.3827 0.6930 0.5602 -0.0647 0.0663  0.0639  219 THR A O   
1688 C CB  . THR A 198 ? 0.4108 0.7557 0.5362 -0.0200 0.0976  0.0370  219 THR A CB  
1689 O OG1 . THR A 198 ? 0.4578 0.7913 0.5437 -0.0037 0.1012  0.0221  219 THR A OG1 
1690 C CG2 . THR A 198 ? 0.4529 0.8356 0.6090 -0.0064 0.1039  0.0302  219 THR A CG2 
1691 N N   . LYS A 199 ? 0.3411 0.6522 0.5288 -0.0434 0.0570  0.0352  220 LYS A N   
1692 C CA  . LYS A 199 ? 0.3621 0.6871 0.5928 -0.0550 0.0478  0.0457  220 LYS A CA  
1693 C C   . LYS A 199 ? 0.3650 0.7346 0.6269 -0.0417 0.0591  0.0425  220 LYS A C   
1694 O O   . LYS A 199 ? 0.3842 0.7513 0.6378 -0.0246 0.0574  0.0239  220 LYS A O   
1695 C CB  . LYS A 199 ? 0.3580 0.6442 0.5848 -0.0597 0.0231  0.0367  220 LYS A CB  
1696 C CG  . LYS A 199 ? 0.5533 0.8527 0.8246 -0.0668 0.0091  0.0418  220 LYS A CG  
1697 C CD  . LYS A 199 ? 0.5558 0.8730 0.8630 -0.0851 0.0079  0.0631  220 LYS A CD  
1698 C CE  . LYS A 199 ? 0.5304 0.8488 0.8790 -0.0926 -0.0140 0.0651  220 LYS A CE  
1699 N NZ  . LYS A 199 ? 0.5582 0.9098 0.9369 -0.0804 -0.0090 0.0589  220 LYS A NZ  
1700 N N   A SER A 200 ? 0.3425 0.7539 0.6432 -0.0491 0.0704  0.0618  221 SER A N   
1701 N N   B SER A 200 ? 0.3391 0.7513 0.6395 -0.0487 0.0710  0.0618  221 SER A N   
1702 C CA  A SER A 200 ? 0.3789 0.8417 0.7141 -0.0356 0.0848  0.0619  221 SER A CA  
1703 C CA  B SER A 200 ? 0.3813 0.8442 0.7158 -0.0348 0.0849  0.0610  221 SER A CA  
1704 C C   A SER A 200 ? 0.3821 0.8474 0.7604 -0.0393 0.0666  0.0586  221 SER A C   
1705 C C   B SER A 200 ? 0.3839 0.8483 0.7611 -0.0389 0.0664  0.0580  221 SER A C   
1706 O O   A SER A 200 ? 0.3837 0.8229 0.7758 -0.0571 0.0458  0.0655  221 SER A O   
1707 O O   B SER A 200 ? 0.3842 0.8215 0.7739 -0.0566 0.0455  0.0645  221 SER A O   
1708 C CB  A SER A 200 ? 0.3699 0.8828 0.7308 -0.0420 0.1079  0.0889  221 SER A CB  
1709 C CB  B SER A 200 ? 0.3684 0.8838 0.7292 -0.0397 0.1090  0.0873  221 SER A CB  
1710 O OG  A SER A 200 ? 0.3995 0.9574 0.7971 -0.0301 0.1198  0.0898  221 SER A OG  
1711 O OG  B SER A 200 ? 0.4008 0.9193 0.7183 -0.0312 0.1272  0.0889  221 SER A OG  
1712 N N   . MET A 201 ? 0.3623 0.8575 0.7609 -0.0207 0.0723  0.0466  222 MET A N   
1713 C CA  . MET A 201 ? 0.3673 0.8706 0.8112 -0.0222 0.0556  0.0440  222 MET A CA  
1714 C C   . MET A 201 ? 0.3361 0.7861 0.7682 -0.0322 0.0248  0.0360  222 MET A C   
1715 O O   . MET A 201 ? 0.3737 0.8178 0.8354 -0.0488 0.0078  0.0472  222 MET A O   
1716 C CB  . MET A 201 ? 0.4050 0.9525 0.9084 -0.0372 0.0615  0.0698  222 MET A CB  
1717 C CG  . MET A 201 ? 0.5641 1.1594 1.0771 -0.0244 0.0918  0.0763  222 MET A CG  
1718 S SD  . MET A 201 ? 0.8364 1.4692 1.3956 -0.0062 0.0933  0.0640  222 MET A SD  
1719 C CE  . MET A 201 ? 0.4146 1.0150 1.0017 -0.0178 0.0538  0.0566  222 MET A CE  
1720 N N   . VAL A 202 ? 0.3284 0.7396 0.7177 -0.0218 0.0164  0.0177  223 VAL A N   
1721 C CA  . VAL A 202 ? 0.2384 0.6020 0.6101 -0.0302 -0.0093 0.0136  223 VAL A CA  
1722 C C   . VAL A 202 ? 0.2864 0.6558 0.6958 -0.0290 -0.0287 0.0111  223 VAL A C   
1723 O O   . VAL A 202 ? 0.2992 0.7020 0.7415 -0.0168 -0.0234 0.0062  223 VAL A O   
1724 C CB  . VAL A 202 ? 0.3146 0.6395 0.6383 -0.0198 -0.0133 -0.0009 223 VAL A CB  
1725 C CG1 . VAL A 202 ? 0.3520 0.6687 0.6408 -0.0219 0.0020  0.0015  223 VAL A CG1 
1726 C CG2 . VAL A 202 ? 0.2437 0.5809 0.5757 0.0004  -0.0113 -0.0159 223 VAL A CG2 
1727 N N   . GLY A 203 ? 0.3032 0.6405 0.7074 -0.0402 -0.0524 0.0137  224 GLY A N   
1728 C CA  . GLY A 203 ? 0.2915 0.6251 0.7223 -0.0380 -0.0760 0.0098  224 GLY A CA  
1729 C C   . GLY A 203 ? 0.3016 0.5854 0.6873 -0.0353 -0.0962 0.0022  224 GLY A C   
1730 O O   . GLY A 203 ? 0.3211 0.5785 0.6615 -0.0355 -0.0898 0.0007  224 GLY A O   
1731 N N   . PRO A 204 ? 0.3462 0.6191 0.7442 -0.0316 -0.1205 -0.0015 225 PRO A N   
1732 C CA  . PRO A 204 ? 0.3386 0.5690 0.6919 -0.0261 -0.1381 -0.0062 225 PRO A CA  
1733 C C   . PRO A 204 ? 0.4293 0.6290 0.7436 -0.0351 -0.1441 -0.0033 225 PRO A C   
1734 O O   . PRO A 204 ? 0.4123 0.5823 0.6797 -0.0291 -0.1461 -0.0054 225 PRO A O   
1735 C CB  . PRO A 204 ? 0.4517 0.6817 0.8317 -0.0222 -0.1649 -0.0082 225 PRO A CB  
1736 C CG  . PRO A 204 ? 0.4746 0.7441 0.9167 -0.0301 -0.1638 -0.0037 225 PRO A CG  
1737 C CD  . PRO A 204 ? 0.4170 0.7192 0.8716 -0.0312 -0.1318 -0.0002 225 PRO A CD  
1738 N N   . GLU A 205 ? 0.3971 0.6055 0.7335 -0.0487 -0.1467 0.0026  226 GLU A N   
1739 C CA  . GLU A 205 ? 0.3688 0.5465 0.6729 -0.0559 -0.1568 0.0030  226 GLU A CA  
1740 C C   . GLU A 205 ? 0.4433 0.6108 0.7073 -0.0555 -0.1337 0.0040  226 GLU A C   
1741 O O   . GLU A 205 ? 0.4540 0.5932 0.6826 -0.0573 -0.1401 0.0023  226 GLU A O   
1742 C CB  . GLU A 205 ? 0.3910 0.5800 0.7383 -0.0718 -0.1684 0.0107  226 GLU A CB  
1743 C CG  . GLU A 205 ? 0.5626 0.7899 0.9458 -0.0824 -0.1416 0.0237  226 GLU A CG  
1744 C CD  . GLU A 205 ? 0.5575 0.8324 0.9940 -0.0795 -0.1296 0.0285  226 GLU A CD  
1745 O OE1 . GLU A 205 ? 0.4753 0.7512 0.9200 -0.0688 -0.1411 0.0202  226 GLU A OE1 
1746 O OE2 . GLU A 205 ? 0.5460 0.8588 1.0153 -0.0864 -0.1079 0.0413  226 GLU A OE2 
1747 N N   . ASP A 206 ? 0.3542 0.5444 0.6238 -0.0514 -0.1089 0.0050  227 ASP A N   
1748 C CA  . ASP A 206 ? 0.3273 0.5087 0.5623 -0.0507 -0.0890 0.0053  227 ASP A CA  
1749 C C   . ASP A 206 ? 0.3388 0.4967 0.5353 -0.0386 -0.0886 -0.0006 227 ASP A C   
1750 O O   . ASP A 206 ? 0.3264 0.4721 0.4932 -0.0372 -0.0762 -0.0008 227 ASP A O   
1751 C CB  . ASP A 206 ? 0.2998 0.5169 0.5575 -0.0506 -0.0644 0.0086  227 ASP A CB  
1752 C CG  . ASP A 206 ? 0.4293 0.6738 0.7261 -0.0640 -0.0608 0.0208  227 ASP A CG  
1753 O OD1 . ASP A 206 ? 0.4069 0.6350 0.6953 -0.0760 -0.0669 0.0275  227 ASP A OD1 
1754 O OD2 . ASP A 206 ? 0.3752 0.6580 0.7140 -0.0623 -0.0529 0.0246  227 ASP A OD2 
1755 N N   . ALA A 207 ? 0.3490 0.5014 0.5492 -0.0301 -0.1028 -0.0035 228 ALA A N   
1756 C CA  . ALA A 207 ? 0.3115 0.4427 0.4798 -0.0198 -0.1038 -0.0038 228 ALA A CA  
1757 C C   . ALA A 207 ? 0.3945 0.4976 0.5194 -0.0202 -0.1092 -0.0014 228 ALA A C   
1758 O O   . ALA A 207 ? 0.3687 0.4622 0.4883 -0.0241 -0.1242 -0.0029 228 ALA A O   
1759 C CB  . ALA A 207 ? 0.2972 0.4276 0.4785 -0.0110 -0.1199 -0.0041 228 ALA A CB  
1760 N N   . GLY A 208 ? 0.3665 0.4571 0.4634 -0.0148 -0.0987 0.0017  229 GLY A N   
1761 C CA  . GLY A 208 ? 0.3907 0.4588 0.4452 -0.0115 -0.1004 0.0048  229 GLY A CA  
1762 C C   . GLY A 208 ? 0.3568 0.4205 0.3942 -0.0127 -0.0822 0.0071  229 GLY A C   
1763 O O   . GLY A 208 ? 0.3482 0.4210 0.4006 -0.0128 -0.0704 0.0076  229 GLY A O   
1764 N N   . ASN A 209 ? 0.3221 0.3711 0.3291 -0.0124 -0.0819 0.0068  230 ASN A N   
1765 C CA  . ASN A 209 ? 0.3316 0.3750 0.3207 -0.0117 -0.0665 0.0100  230 ASN A CA  
1766 C C   . ASN A 209 ? 0.3256 0.3685 0.3159 -0.0208 -0.0610 0.0049  230 ASN A C   
1767 O O   . ASN A 209 ? 0.3237 0.3624 0.3159 -0.0257 -0.0721 0.0006  230 ASN A O   
1768 C CB  . ASN A 209 ? 0.3473 0.3769 0.2995 -0.0010 -0.0684 0.0153  230 ASN A CB  
1769 C CG  . ASN A 209 ? 0.4666 0.4986 0.4176 0.0076  -0.0702 0.0263  230 ASN A CG  
1770 O OD1 . ASN A 209 ? 0.3894 0.4273 0.3579 0.0066  -0.0616 0.0337  230 ASN A OD1 
1771 N ND2 . ASN A 209 ? 0.4516 0.4783 0.3856 0.0157  -0.0844 0.0272  230 ASN A ND2 
1772 N N   . TYR A 210 ? 0.3341 0.3801 0.3254 -0.0230 -0.0460 0.0062  231 TYR A N   
1773 C CA  . TYR A 210 ? 0.3026 0.3484 0.2934 -0.0310 -0.0393 0.0038  231 TYR A CA  
1774 C C   . TYR A 210 ? 0.3304 0.3668 0.3021 -0.0272 -0.0293 0.0058  231 TYR A C   
1775 O O   . TYR A 210 ? 0.3209 0.3565 0.2897 -0.0203 -0.0252 0.0104  231 TYR A O   
1776 C CB  . TYR A 210 ? 0.2802 0.3465 0.2980 -0.0370 -0.0307 0.0027  231 TYR A CB  
1777 C CG  . TYR A 210 ? 0.3086 0.3913 0.3540 -0.0411 -0.0378 0.0025  231 TYR A CG  
1778 C CD1 . TYR A 210 ? 0.2984 0.3914 0.3602 -0.0515 -0.0382 0.0056  231 TYR A CD1 
1779 C CD2 . TYR A 210 ? 0.3135 0.4034 0.3736 -0.0348 -0.0443 0.0011  231 TYR A CD2 
1780 C CE1 . TYR A 210 ? 0.2618 0.3747 0.3569 -0.0560 -0.0437 0.0078  231 TYR A CE1 
1781 C CE2 . TYR A 210 ? 0.2827 0.3911 0.3740 -0.0381 -0.0509 0.0008  231 TYR A CE2 
1782 C CZ  . TYR A 210 ? 0.2738 0.3942 0.3829 -0.0487 -0.0503 0.0043  231 TYR A CZ  
1783 O OH  . TYR A 210 ? 0.2913 0.4328 0.4366 -0.0525 -0.0565 0.0062  231 TYR A OH  
1784 N N   . ARG A 211 ? 0.3362 0.3663 0.2993 -0.0324 -0.0261 0.0041  232 ARG A N   
1785 C CA  . ARG A 211 ? 0.3279 0.3497 0.2759 -0.0288 -0.0178 0.0056  232 ARG A CA  
1786 C C   . ARG A 211 ? 0.3254 0.3480 0.2763 -0.0364 -0.0125 0.0042  232 ARG A C   
1787 O O   . ARG A 211 ? 0.3845 0.4061 0.3386 -0.0440 -0.0176 0.0041  232 ARG A O   
1788 C CB  . ARG A 211 ? 0.3735 0.3804 0.2953 -0.0214 -0.0235 0.0051  232 ARG A CB  
1789 C CG  . ARG A 211 ? 0.5375 0.5376 0.4438 -0.0154 -0.0161 0.0070  232 ARG A CG  
1790 C CD  . ARG A 211 ? 0.6234 0.6117 0.5018 -0.0048 -0.0241 0.0032  232 ARG A CD  
1791 N NE  . ARG A 211 ? 0.8255 0.8058 0.6911 -0.0008 -0.0197 0.0011  232 ARG A NE  
1792 C CZ  . ARG A 211 ? 0.8440 0.8092 0.6976 -0.0005 -0.0293 -0.0076 232 ARG A CZ  
1793 N NH1 . ARG A 211 ? 0.7306 0.6862 0.5846 -0.0046 -0.0454 -0.0144 232 ARG A NH1 
1794 N NH2 . ARG A 211 ? 0.9772 0.9362 0.8220 0.0041  -0.0248 -0.0093 232 ARG A NH2 
1795 N N   . CYS A 212 ? 0.2933 0.3172 0.2443 -0.0344 -0.0039 0.0043  233 CYS A N   
1796 C CA  . CYS A 212 ? 0.2881 0.3097 0.2343 -0.0393 0.0004  0.0038  233 CYS A CA  
1797 C C   . CYS A 212 ? 0.3401 0.3458 0.2697 -0.0359 0.0001  0.0041  233 CYS A C   
1798 O O   . CYS A 212 ? 0.3652 0.3689 0.2934 -0.0288 0.0024  0.0056  233 CYS A O   
1799 C CB  . CYS A 212 ? 0.3437 0.3763 0.2990 -0.0366 0.0073  0.0010  233 CYS A CB  
1800 S SG  . CYS A 212 ? 0.4344 0.4621 0.3768 -0.0386 0.0116  0.0007  233 CYS A SG  
1801 N N   A VAL A 213 ? 0.3517 0.3474 0.2718 -0.0407 -0.0028 0.0041  234 VAL A N   
1802 N N   B VAL A 213 ? 0.3348 0.3311 0.2555 -0.0410 -0.0024 0.0042  234 VAL A N   
1803 C CA  A VAL A 213 ? 0.3559 0.3383 0.2631 -0.0360 -0.0025 0.0032  234 VAL A CA  
1804 C CA  B VAL A 213 ? 0.3613 0.3431 0.2682 -0.0369 -0.0032 0.0032  234 VAL A CA  
1805 C C   A VAL A 213 ? 0.3716 0.3501 0.2765 -0.0420 -0.0017 0.0046  234 VAL A C   
1806 C C   B VAL A 213 ? 0.3932 0.3728 0.2989 -0.0425 -0.0013 0.0048  234 VAL A C   
1807 O O   A VAL A 213 ? 0.3869 0.3640 0.2930 -0.0505 -0.0056 0.0081  234 VAL A O   
1808 O O   B VAL A 213 ? 0.3856 0.3664 0.2937 -0.0512 -0.0039 0.0087  234 VAL A O   
1809 C CB  A VAL A 213 ? 0.4278 0.3960 0.3199 -0.0307 -0.0107 0.0001  234 VAL A CB  
1810 C CB  B VAL A 213 ? 0.4086 0.3751 0.3021 -0.0346 -0.0132 0.0001  234 VAL A CB  
1811 C CG1 A VAL A 213 ? 0.3789 0.3380 0.2715 -0.0388 -0.0225 -0.0012 234 VAL A CG1 
1812 C CG1 B VAL A 213 ? 0.4524 0.4073 0.3330 -0.0266 -0.0125 -0.0023 234 VAL A CG1 
1813 C CG2 A VAL A 213 ? 0.3903 0.3487 0.2717 -0.0235 -0.0088 -0.0014 234 VAL A CG2 
1814 C CG2 B VAL A 213 ? 0.3921 0.3611 0.2817 -0.0279 -0.0171 -0.0018 234 VAL A CG2 
1815 N N   . LEU A 214 ? 0.3609 0.3389 0.2654 -0.0377 0.0026  0.0036  235 LEU A N   
1816 C CA  . LEU A 214 ? 0.3546 0.3286 0.2535 -0.0406 0.0028  0.0045  235 LEU A CA  
1817 C C   . LEU A 214 ? 0.3718 0.3286 0.2613 -0.0382 -0.0024 0.0040  235 LEU A C   
1818 O O   . LEU A 214 ? 0.4112 0.3656 0.3027 -0.0304 -0.0013 0.0018  235 LEU A O   
1819 C CB  . LEU A 214 ? 0.3600 0.3415 0.2645 -0.0353 0.0061  0.0009  235 LEU A CB  
1820 C CG  . LEU A 214 ? 0.3547 0.3304 0.2489 -0.0345 0.0041  0.0002  235 LEU A CG  
1821 C CD1 . LEU A 214 ? 0.3625 0.3438 0.2452 -0.0411 0.0064  0.0067  235 LEU A CD1 
1822 C CD2 . LEU A 214 ? 0.3762 0.3563 0.2774 -0.0263 0.0025  -0.0073 235 LEU A CD2 
1823 N N   . ASP A 215 ? 0.4207 0.3671 0.3026 -0.0445 -0.0080 0.0075  236 ASP A N   
1824 C CA  . ASP A 215 ? 0.4143 0.3417 0.2885 -0.0417 -0.0161 0.0056  236 ASP A CA  
1825 C C   . ASP A 215 ? 0.4053 0.3258 0.2746 -0.0416 -0.0176 0.0076  236 ASP A C   
1826 O O   . ASP A 215 ? 0.4245 0.3541 0.2923 -0.0439 -0.0134 0.0106  236 ASP A O   
1827 C CB  . ASP A 215 ? 0.3800 0.2950 0.2530 -0.0486 -0.0270 0.0079  236 ASP A CB  
1828 C CG  . ASP A 215 ? 0.6814 0.5764 0.5464 -0.0397 -0.0379 -0.0005 236 ASP A CG  
1829 O OD1 . ASP A 215 ? 0.5649 0.4596 0.4253 -0.0278 -0.0340 -0.0062 236 ASP A OD1 
1830 O OD2 . ASP A 215 ? 0.7221 0.6023 0.5878 -0.0438 -0.0517 -0.0012 236 ASP A OD2 
1831 N N   . THR A 216 ? 0.4018 0.3066 0.2672 -0.0365 -0.0245 0.0045  237 THR A N   
1832 C CA  . THR A 216 ? 0.3649 0.2607 0.2260 -0.0359 -0.0289 0.0064  237 THR A CA  
1833 C C   . THR A 216 ? 0.4023 0.2767 0.2580 -0.0381 -0.0415 0.0082  237 THR A C   
1834 O O   . THR A 216 ? 0.4603 0.3259 0.3165 -0.0377 -0.0479 0.0049  237 THR A O   
1835 C CB  . THR A 216 ? 0.4306 0.3286 0.3001 -0.0254 -0.0271 0.0007  237 THR A CB  
1836 O OG1 . THR A 216 ? 0.4270 0.3199 0.2996 -0.0166 -0.0286 -0.0041 237 THR A OG1 
1837 C CG2 . THR A 216 ? 0.3714 0.2873 0.2529 -0.0230 -0.0186 -0.0007 237 THR A CG2 
1838 N N   . ILE A 217 ? 0.4182 0.2824 0.2686 -0.0395 -0.0477 0.0126  238 ILE A N   
1839 C CA  . ILE A 217 ? 0.4947 0.3356 0.3425 -0.0420 -0.0624 0.0156  238 ILE A CA  
1840 C C   . ILE A 217 ? 0.4516 0.2808 0.3031 -0.0293 -0.0690 0.0026  238 ILE A C   
1841 O O   . ILE A 217 ? 0.4788 0.2915 0.3303 -0.0285 -0.0811 -0.0013 238 ILE A O   
1842 C CB  . ILE A 217 ? 0.4407 0.2729 0.2810 -0.0436 -0.0682 0.0229  238 ILE A CB  
1843 C CG1 . ILE A 217 ? 0.4749 0.3203 0.3063 -0.0537 -0.0614 0.0372  238 ILE A CG1 
1844 C CG2 . ILE A 217 ? 0.4409 0.2460 0.2820 -0.0454 -0.0861 0.0262  238 ILE A CG2 
1845 C CD1 . ILE A 217 ? 0.5247 0.3676 0.3411 -0.0518 -0.0644 0.0439  238 ILE A CD1 
1846 N N   . ASN A 218 ? 0.5441 0.3826 0.4006 -0.0179 -0.0622 -0.0043 239 ASN A N   
1847 C CA  . ASN A 218 ? 0.5508 0.3843 0.4107 -0.0032 -0.0654 -0.0149 239 ASN A CA  
1848 C C   . ASN A 218 ? 0.5330 0.3889 0.4038 0.0082  -0.0512 -0.0184 239 ASN A C   
1849 O O   . ASN A 218 ? 0.5387 0.3966 0.4152 0.0222  -0.0509 -0.0244 239 ASN A O   
1850 C CB  . ASN A 218 ? 0.5704 0.3828 0.4309 0.0006  -0.0802 -0.0167 239 ASN A CB  
1851 C CG  . ASN A 218 ? 0.5880 0.4060 0.4568 0.0028  -0.0783 -0.0139 239 ASN A CG  
1852 O OD1 . ASN A 218 ? 0.5455 0.3797 0.4186 -0.0009 -0.0688 -0.0099 239 ASN A OD1 
1853 N ND2 . ASN A 218 ? 0.5779 0.3812 0.4511 0.0103  -0.0901 -0.0176 239 ASN A ND2 
1854 N N   . GLN A 219 ? 0.4163 0.2905 0.2926 0.0030  -0.0396 -0.0134 240 GLN A N   
1855 C CA  . GLN A 219 ? 0.4155 0.3111 0.3084 0.0118  -0.0274 -0.0123 240 GLN A CA  
1856 C C   . GLN A 219 ? 0.4972 0.4073 0.3870 0.0136  -0.0172 -0.0110 240 GLN A C   
1857 O O   . GLN A 219 ? 0.4465 0.3758 0.3518 0.0173  -0.0066 -0.0055 240 GLN A O   
1858 C CB  . GLN A 219 ? 0.3811 0.2841 0.2902 0.0063  -0.0263 -0.0075 240 GLN A CB  
1859 C CG  . GLN A 219 ? 0.3998 0.2885 0.3109 0.0069  -0.0382 -0.0091 240 GLN A CG  
1860 C CD  . GLN A 219 ? 0.5058 0.3958 0.4306 0.0193  -0.0393 -0.0119 240 GLN A CD  
1861 O OE1 . GLN A 219 ? 0.4438 0.3539 0.3870 0.0278  -0.0283 -0.0095 240 GLN A OE1 
1862 N NE2 . GLN A 219 ? 0.4782 0.3489 0.3961 0.0213  -0.0523 -0.0155 240 GLN A NE2 
1863 N N   . GLY A 220 ? 0.4493 0.3497 0.3219 0.0108  -0.0223 -0.0149 241 GLY A N   
1864 C CA  . GLY A 220 ? 0.4347 0.3467 0.3018 0.0136  -0.0155 -0.0146 241 GLY A CA  
1865 C C   . GLY A 220 ? 0.3957 0.3170 0.2697 0.0010  -0.0109 -0.0083 241 GLY A C   
1866 O O   . GLY A 220 ? 0.4639 0.3826 0.3428 -0.0086 -0.0130 -0.0055 241 GLY A O   
1867 N N   . HIS A 221 ? 0.4039 0.3363 0.2761 0.0031  -0.0054 -0.0068 242 HIS A N   
1868 C CA  . HIS A 221 ? 0.3292 0.2710 0.2096 -0.0067 -0.0019 -0.0023 242 HIS A CA  
1869 C C   . HIS A 221 ? 0.4019 0.3546 0.3020 -0.0075 0.0042  0.0028  242 HIS A C   
1870 O O   . HIS A 221 ? 0.3919 0.3521 0.3034 0.0005  0.0092  0.0067  242 HIS A O   
1871 C CB  . HIS A 221 ? 0.3662 0.3172 0.2424 -0.0024 0.0013  -0.0012 242 HIS A CB  
1872 C CG  . HIS A 221 ? 0.4916 0.4303 0.3495 0.0009  -0.0085 -0.0086 242 HIS A CG  
1873 N ND1 . HIS A 221 ? 0.5451 0.4683 0.4003 -0.0088 -0.0204 -0.0121 242 HIS A ND1 
1874 C CD2 . HIS A 221 ? 0.5704 0.5097 0.4129 0.0133  -0.0103 -0.0127 242 HIS A CD2 
1875 C CE1 . HIS A 221 ? 0.5682 0.4804 0.4111 -0.0034 -0.0318 -0.0195 242 HIS A CE1 
1876 N NE2 . HIS A 221 ? 0.6489 0.5701 0.4805 0.0115  -0.0262 -0.0218 242 HIS A NE2 
1877 N N   . ALA A 222 ? 0.3489 0.3037 0.2548 -0.0155 0.0028  0.0027  243 ALA A N   
1878 C CA  . ALA A 222 ? 0.3373 0.2979 0.2617 -0.0151 0.0030  0.0038  243 ALA A CA  
1879 C C   . ALA A 222 ? 0.3604 0.3333 0.3003 -0.0153 0.0061  0.0065  243 ALA A C   
1880 O O   . ALA A 222 ? 0.3339 0.3111 0.2963 -0.0132 0.0044  0.0088  243 ALA A O   
1881 C CB  . ALA A 222 ? 0.3560 0.3096 0.2725 -0.0194 -0.0030 -0.0010 243 ALA A CB  
1882 N N   . THR A 223 ? 0.3428 0.3198 0.2743 -0.0181 0.0081  0.0060  244 THR A N   
1883 C CA  . THR A 223 ? 0.2995 0.2869 0.2464 -0.0176 0.0093  0.0084  244 THR A CA  
1884 C C   . THR A 223 ? 0.3002 0.2912 0.2362 -0.0186 0.0111  0.0098  244 THR A C   
1885 O O   . THR A 223 ? 0.3392 0.3254 0.2606 -0.0229 0.0088  0.0061  244 THR A O   
1886 C CB  . THR A 223 ? 0.3204 0.3101 0.2736 -0.0193 0.0053  0.0011  244 THR A CB  
1887 O OG1 . THR A 223 ? 0.3400 0.3251 0.3071 -0.0160 -0.0004 -0.0013 244 THR A OG1 
1888 C CG2 . THR A 223 ? 0.3245 0.3239 0.2914 -0.0184 0.0048  0.0010  244 THR A CG2 
1889 N N   . VAL A 224 ? 0.2858 0.2845 0.2315 -0.0149 0.0132  0.0164  245 VAL A N   
1890 C CA  . VAL A 224 ? 0.2862 0.2889 0.2256 -0.0154 0.0117  0.0165  245 VAL A CA  
1891 C C   . VAL A 224 ? 0.3142 0.3255 0.2750 -0.0152 0.0103  0.0198  245 VAL A C   
1892 O O   . VAL A 224 ? 0.3514 0.3655 0.3298 -0.0123 0.0113  0.0280  245 VAL A O   
1893 C CB  . VAL A 224 ? 0.3616 0.3643 0.2850 -0.0077 0.0136  0.0219  245 VAL A CB  
1894 C CG1 . VAL A 224 ? 0.3481 0.3555 0.2674 -0.0060 0.0097  0.0236  245 VAL A CG1 
1895 C CG2 . VAL A 224 ? 0.3926 0.3838 0.2946 -0.0063 0.0106  0.0146  245 VAL A CG2 
1896 N N   . ILE A 225 ? 0.2902 0.3059 0.2533 -0.0183 0.0071  0.0143  246 ILE A N   
1897 C CA  . ILE A 225 ? 0.2853 0.3081 0.2686 -0.0164 0.0036  0.0162  246 ILE A CA  
1898 C C   . ILE A 225 ? 0.2904 0.3170 0.2664 -0.0167 0.0007  0.0168  246 ILE A C   
1899 O O   . ILE A 225 ? 0.3296 0.3557 0.2938 -0.0210 -0.0005 0.0114  246 ILE A O   
1900 C CB  . ILE A 225 ? 0.3042 0.3311 0.3006 -0.0166 0.0011  0.0055  246 ILE A CB  
1901 C CG1 . ILE A 225 ? 0.2992 0.3194 0.3026 -0.0145 -0.0005 0.0030  246 ILE A CG1 
1902 C CG2 . ILE A 225 ? 0.2902 0.3235 0.3082 -0.0128 -0.0049 0.0041  246 ILE A CG2 
1903 C CD1 . ILE A 225 ? 0.2908 0.3142 0.2953 -0.0112 -0.0034 -0.0106 246 ILE A CD1 
1904 N N   . ARG A 226 ? 0.2618 0.2916 0.2473 -0.0128 -0.0025 0.0246  247 ARG A N   
1905 C CA  . ARG A 226 ? 0.2954 0.3283 0.2758 -0.0119 -0.0083 0.0247  247 ARG A CA  
1906 C C   . ARG A 226 ? 0.3063 0.3474 0.3113 -0.0122 -0.0137 0.0204  247 ARG A C   
1907 O O   . ARG A 226 ? 0.2948 0.3365 0.3199 -0.0100 -0.0148 0.0210  247 ARG A O   
1908 C CB  . ARG A 226 ? 0.2838 0.3151 0.2515 -0.0048 -0.0084 0.0378  247 ARG A CB  
1909 C CG  . ARG A 226 ? 0.3272 0.3525 0.2649 -0.0007 -0.0044 0.0373  247 ARG A CG  
1910 C CD  . ARG A 226 ? 0.4635 0.4926 0.3859 0.0103  0.0000  0.0521  247 ARG A CD  
1911 N NE  . ARG A 226 ? 0.5241 0.5601 0.4697 0.0098  0.0084  0.0665  247 ARG A NE  
1912 C CZ  . ARG A 226 ? 0.6052 0.6477 0.5724 0.0105  0.0080  0.0827  247 ARG A CZ  
1913 N NH1 . ARG A 226 ? 0.4967 0.5406 0.4614 0.0133  0.0008  0.0872  247 ARG A NH1 
1914 N NH2 . ARG A 226 ? 0.4721 0.5191 0.4672 0.0081  0.0128  0.0957  247 ARG A NH2 
1915 N N   . TYR A 227 ? 0.2815 0.3283 0.2877 -0.0137 -0.0192 0.0159  248 TYR A N   
1916 C CA  . TYR A 227 ? 0.2796 0.3371 0.3110 -0.0120 -0.0242 0.0109  248 TYR A CA  
1917 C C   . TYR A 227 ? 0.3066 0.3647 0.3381 -0.0099 -0.0340 0.0153  248 TYR A C   
1918 O O   . TYR A 227 ? 0.3387 0.3944 0.3553 -0.0123 -0.0382 0.0144  248 TYR A O   
1919 C CB  . TYR A 227 ? 0.2384 0.3093 0.2779 -0.0159 -0.0198 0.0005  248 TYR A CB  
1920 C CG  . TYR A 227 ? 0.2930 0.3621 0.3226 -0.0180 -0.0109 -0.0031 248 TYR A CG  
1921 C CD1 . TYR A 227 ? 0.3032 0.3777 0.3434 -0.0124 -0.0083 -0.0110 248 TYR A CD1 
1922 C CD2 . TYR A 227 ? 0.2552 0.3160 0.2643 -0.0239 -0.0075 -0.0001 248 TYR A CD2 
1923 C CE1 . TYR A 227 ? 0.2626 0.3346 0.2907 -0.0128 -0.0020 -0.0148 248 TYR A CE1 
1924 C CE2 . TYR A 227 ? 0.2729 0.3313 0.2729 -0.0256 -0.0005 -0.0027 248 TYR A CE2 
1925 C CZ  . TYR A 227 ? 0.2974 0.3617 0.3058 -0.0200 0.0023  -0.0095 248 TYR A CZ  
1926 O OH  . TYR A 227 ? 0.3135 0.3743 0.3098 -0.0201 0.0070  -0.0123 248 TYR A OH  
1927 N N   . ASP A 228 ? 0.2371 0.2967 0.2871 -0.0049 -0.0405 0.0192  249 ASP A N   
1928 C CA  . ASP A 228 ? 0.2479 0.3089 0.3018 -0.0019 -0.0518 0.0228  249 ASP A CA  
1929 C C   . ASP A 228 ? 0.3464 0.4220 0.4312 -0.0010 -0.0562 0.0118  249 ASP A C   
1930 O O   . ASP A 228 ? 0.2924 0.3700 0.3976 0.0035  -0.0573 0.0088  249 ASP A O   
1931 C CB  . ASP A 228 ? 0.3154 0.3683 0.3703 0.0038  -0.0559 0.0386  249 ASP A CB  
1932 C CG  . ASP A 228 ? 0.5548 0.6072 0.6110 0.0086  -0.0689 0.0452  249 ASP A CG  
1933 O OD1 . ASP A 228 ? 0.5598 0.6198 0.6331 0.0084  -0.0770 0.0351  249 ASP A OD1 
1934 O OD2 . ASP A 228 ? 0.6351 0.6814 0.6761 0.0134  -0.0709 0.0620  249 ASP A OD2 
1935 N N   . VAL A 229 ? 0.2806 0.3667 0.3712 -0.0043 -0.0601 0.0061  250 VAL A N   
1936 C CA  . VAL A 229 ? 0.2796 0.3863 0.4013 -0.0029 -0.0603 -0.0033 250 VAL A CA  
1937 C C   . VAL A 229 ? 0.3271 0.4384 0.4668 0.0005  -0.0749 -0.0024 250 VAL A C   
1938 O O   . VAL A 229 ? 0.2966 0.4026 0.4264 -0.0027 -0.0850 0.0013  250 VAL A O   
1939 C CB  . VAL A 229 ? 0.3190 0.4412 0.4429 -0.0109 -0.0507 -0.0076 250 VAL A CB  
1940 C CG1 . VAL A 229 ? 0.2664 0.4176 0.4247 -0.0084 -0.0481 -0.0141 250 VAL A CG1 
1941 C CG2 . VAL A 229 ? 0.2945 0.4114 0.3992 -0.0133 -0.0368 -0.0086 250 VAL A CG2 
1942 N N   . THR A 230 ? 0.2491 0.3685 0.4156 0.0086  -0.0790 -0.0074 251 THR A N   
1943 C CA  . THR A 230 ? 0.2945 0.4207 0.4847 0.0133  -0.0939 -0.0080 251 THR A CA  
1944 C C   . THR A 230 ? 0.3215 0.4776 0.5448 0.0153  -0.0890 -0.0192 251 THR A C   
1945 O O   . THR A 230 ? 0.2573 0.4265 0.4899 0.0209  -0.0774 -0.0283 251 THR A O   
1946 C CB  . THR A 230 ? 0.3324 0.4458 0.5328 0.0222  -0.1044 -0.0040 251 THR A CB  
1947 O OG1 . THR A 230 ? 0.3540 0.4452 0.5248 0.0199  -0.1064 0.0114  251 THR A OG1 
1948 C CG2 . THR A 230 ? 0.3462 0.4660 0.5733 0.0284  -0.1209 -0.0053 251 THR A CG2 
1949 N N   . VAL A 231 ? 0.2416 0.4105 0.4834 0.0123  -0.0977 -0.0185 252 VAL A N   
1950 C CA  . VAL A 231 ? 0.2822 0.4858 0.5624 0.0155  -0.0914 -0.0264 252 VAL A CA  
1951 C C   . VAL A 231 ? 0.3048 0.5145 0.6156 0.0269  -0.1061 -0.0314 252 VAL A C   
1952 O O   . VAL A 231 ? 0.3225 0.5209 0.6367 0.0258  -0.1248 -0.0260 252 VAL A O   
1953 C CB  . VAL A 231 ? 0.2777 0.4993 0.5721 0.0034  -0.0899 -0.0212 252 VAL A CB  
1954 C CG1 . VAL A 231 ? 0.3146 0.5794 0.6550 0.0076  -0.0809 -0.0254 252 VAL A CG1 
1955 C CG2 . VAL A 231 ? 0.2708 0.4855 0.5377 -0.0069 -0.0763 -0.0165 252 VAL A CG2 
1956 N N   . LEU A 232 ? 0.2399 0.4663 0.5714 0.0398  -0.0996 -0.0430 253 LEU A N   
1957 C CA  . LEU A 232 ? 0.2460 0.4764 0.6088 0.0531  -0.1151 -0.0500 253 LEU A CA  
1958 C C   . LEU A 232 ? 0.2436 0.5120 0.6490 0.0563  -0.1147 -0.0545 253 LEU A C   
1959 O O   . LEU A 232 ? 0.3274 0.6261 0.7428 0.0521  -0.0972 -0.0542 253 LEU A O   
1960 C CB  . LEU A 232 ? 0.2626 0.4895 0.6294 0.0685  -0.1127 -0.0634 253 LEU A CB  
1961 C CG  . LEU A 232 ? 0.3824 0.5735 0.7174 0.0652  -0.1149 -0.0576 253 LEU A CG  
1962 C CD1 . LEU A 232 ? 0.3247 0.5114 0.6706 0.0810  -0.1176 -0.0731 253 LEU A CD1 
1963 C CD2 . LEU A 232 ? 0.4358 0.5975 0.7612 0.0593  -0.1331 -0.0413 253 LEU A CD2 
1964 N N   . PRO A 233 ? 0.3691 0.6381 0.8032 0.0639  -0.1342 -0.0565 254 PRO A N   
1965 C CA  . PRO A 233 ? 0.3396 0.6508 0.8221 0.0698  -0.1322 -0.0623 254 PRO A CA  
1966 C C   . PRO A 233 ? 0.3318 0.6771 0.8301 0.0856  -0.1114 -0.0769 254 PRO A C   
1967 O O   . PRO A 233 ? 0.3482 0.6770 0.8231 0.0947  -0.1070 -0.0859 254 PRO A O   
1968 C CB  . PRO A 233 ? 0.3883 0.6863 0.8917 0.0783  -0.1576 -0.0638 254 PRO A CB  
1969 C CG  . PRO A 233 ? 0.3764 0.6331 0.8510 0.0814  -0.1705 -0.0614 254 PRO A CG  
1970 C CD  . PRO A 233 ? 0.4066 0.6425 0.8342 0.0676  -0.1581 -0.0516 254 PRO A CD  
1971 N N   . PRO A 234 ? 0.3869 0.7808 0.9241 0.0893  -0.0987 -0.0782 255 PRO A N   
1972 C CA  . PRO A 234 ? 0.3617 0.7909 0.9074 0.1082  -0.0770 -0.0912 255 PRO A CA  
1973 C C   . PRO A 234 ? 0.3999 0.8086 0.9411 0.1296  -0.0884 -0.1088 255 PRO A C   
1974 O O   . PRO A 234 ? 0.3748 0.7619 0.9275 0.1304  -0.1095 -0.1080 255 PRO A O   
1975 C CB  . PRO A 234 ? 0.3735 0.8490 0.9591 0.1062  -0.0657 -0.0817 255 PRO A CB  
1976 C CG  . PRO A 234 ? 0.4015 0.8686 0.9964 0.0820  -0.0771 -0.0639 255 PRO A CG  
1977 C CD  . PRO A 234 ? 0.4005 0.8126 0.9671 0.0763  -0.1037 -0.0650 255 PRO A CD  
1978 N N   . LYS A 235 ? 0.4713 0.8836 0.9945 0.1466  -0.0766 -0.1246 256 LYS A N   
1979 C CA  . LYS A 235 ? 0.4793 0.8790 1.0054 0.1684  -0.0869 -0.1432 256 LYS A CA  
1980 C C   . LYS A 235 ? 0.4246 0.8605 0.9857 0.1781  -0.0819 -0.1441 256 LYS A C   
1981 O O   . LYS A 235 ? 0.5951 1.0141 1.1723 0.1845  -0.1011 -0.1495 256 LYS A O   
1982 C CB  . LYS A 235 ? 0.5298 0.9298 1.0287 0.1863  -0.0755 -0.1617 256 LYS A CB  
1983 C CG  . LYS A 235 ? 0.4531 0.8204 0.9206 0.1776  -0.0798 -0.1607 256 LYS A CG  
1984 C CD  . LYS A 235 ? 0.4326 0.7969 0.8718 0.1967  -0.0724 -0.1810 256 LYS A CD  
1985 C CE  . LYS A 235 ? 0.5162 0.8470 0.9276 0.1884  -0.0783 -0.1797 256 LYS A CE  
1986 N NZ  . LYS A 235 ? 0.5231 0.8431 0.9068 0.2069  -0.0778 -0.2010 256 LYS A NZ  
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