data_8ZVY
# 
_entry.id   8ZVY 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8ZVY         pdb_00008zvy 10.2210/pdb8zvy/pdb 
WWPDB D_1300048357 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-28 
_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                        8ZVY 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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              s.padavattan@gmail.com 
_pdbx_contact_author.name_first         Sivaraman 
_pdbx_contact_author.name_last          Padavattan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1732-5421 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Padavattan, S.' 1 0000-0002-1732-5421 
'Jos, S.'        2 0000-0002-7267-0826 
'Kambaru, A.'    3 0000-0003-1795-0080 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3642 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                712 
_citation.page_last                 712 
_citation.title                     
;Structural and functional insights into the nuclear role of Parkinson's disease-associated alpha-synuclein as a histone chaperone.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42003-025-08138-0 
_citation.pdbx_database_id_PubMed   40341765 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Jos, S.'           1 ?                   
primary 'Kambaru, A.'       2 0000-0003-1795-0080 
primary 'Prasad, T.K.'      3 0000-0002-0524-8000 
primary 'Parthasarathi, S.' 4 ?                   
primary 'Kamariah, N.'      5 ?                   
primary 'Nath, S.'          6 ?                   
primary 'Padmanabhan, B.'   7 0000-0001-8434-828X 
primary 'Padavattan, S.'    8 0000-0002-1732-5421 
# 
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 'Histone H2B 1.1,Histone H2A type 1' 20521.707 2   ? ? ? 'Histone H2a-H2b dimer'             
2 polymer     syn 'Isoform 1 of Alpha-synuclein'       2366.337  2   ? ? ? 'Alpha-Synuclein peptide (121-140)' 
3 non-polymer nat 'CHLORIDE ION'                       35.453    2   ? ? ? ?                                   
4 water       nat water                                18.015    228 ? ? ? ?                                   
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 H2B1.1                                                                          
2 'Non-A beta component of AD amyloid,Non-A4 component of amyloid precursor,NACP' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV
SEGTKAVTKYTSAKKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRI
IPRHLQLAVRNDEELNKLLGGVTIAQ
;
;GRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV
SEGTKAVTKYTSAKKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRI
IPRHLQLAVRNDEELNKLLGGVTIAQ
;
A,B ? 
2 'polypeptide(L)' no no DNEAYEMPSEEGYQDYEPEA DNEAYEMPSEEGYQDYEPEA C,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CHLORIDE ION' CL  
4 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   ARG n 
1 3   LYS n 
1 4   GLU n 
1 5   SER n 
1 6   TYR n 
1 7   ALA n 
1 8   ILE n 
1 9   TYR n 
1 10  VAL n 
1 11  TYR n 
1 12  LYS n 
1 13  VAL n 
1 14  LEU n 
1 15  LYS n 
1 16  GLN n 
1 17  VAL n 
1 18  HIS n 
1 19  PRO n 
1 20  ASP n 
1 21  THR n 
1 22  GLY n 
1 23  ILE n 
1 24  SER n 
1 25  SER n 
1 26  LYS n 
1 27  ALA n 
1 28  MET n 
1 29  SER n 
1 30  ILE n 
1 31  MET n 
1 32  ASN n 
1 33  SER n 
1 34  PHE n 
1 35  VAL n 
1 36  ASN n 
1 37  ASP n 
1 38  VAL n 
1 39  PHE n 
1 40  GLU n 
1 41  ARG n 
1 42  ILE n 
1 43  ALA n 
1 44  GLY n 
1 45  GLU n 
1 46  ALA n 
1 47  SER n 
1 48  ARG n 
1 49  LEU n 
1 50  ALA n 
1 51  HIS n 
1 52  TYR n 
1 53  ASN n 
1 54  LYS n 
1 55  ARG n 
1 56  SER n 
1 57  THR n 
1 58  ILE n 
1 59  THR n 
1 60  SER n 
1 61  ARG n 
1 62  GLU n 
1 63  ILE n 
1 64  GLN n 
1 65  THR n 
1 66  ALA n 
1 67  VAL n 
1 68  ARG n 
1 69  LEU n 
1 70  LEU n 
1 71  LEU n 
1 72  PRO n 
1 73  GLY n 
1 74  GLU n 
1 75  LEU n 
1 76  ALA n 
1 77  LYS n 
1 78  HIS n 
1 79  ALA n 
1 80  VAL n 
1 81  SER n 
1 82  GLU n 
1 83  GLY n 
1 84  THR n 
1 85  LYS n 
1 86  ALA n 
1 87  VAL n 
1 88  THR n 
1 89  LYS n 
1 90  TYR n 
1 91  THR n 
1 92  SER n 
1 93  ALA n 
1 94  LYS n 
1 95  LYS n 
1 96  ALA n 
1 97  LYS n 
1 98  THR n 
1 99  ARG n 
1 100 SER n 
1 101 SER n 
1 102 ARG n 
1 103 ALA n 
1 104 GLY n 
1 105 LEU n 
1 106 GLN n 
1 107 PHE n 
1 108 PRO n 
1 109 VAL n 
1 110 GLY n 
1 111 ARG n 
1 112 VAL n 
1 113 HIS n 
1 114 ARG n 
1 115 LEU n 
1 116 LEU n 
1 117 ARG n 
1 118 LYS n 
1 119 GLY n 
1 120 ASN n 
1 121 TYR n 
1 122 ALA n 
1 123 GLU n 
1 124 ARG n 
1 125 VAL n 
1 126 GLY n 
1 127 ALA n 
1 128 GLY n 
1 129 ALA n 
1 130 PRO n 
1 131 VAL n 
1 132 TYR n 
1 133 LEU n 
1 134 ALA n 
1 135 ALA n 
1 136 VAL n 
1 137 LEU n 
1 138 GLU n 
1 139 TYR n 
1 140 LEU n 
1 141 THR n 
1 142 ALA n 
1 143 GLU n 
1 144 ILE n 
1 145 LEU n 
1 146 GLU n 
1 147 LEU n 
1 148 ALA n 
1 149 GLY n 
1 150 ASN n 
1 151 ALA n 
1 152 ALA n 
1 153 ARG n 
1 154 ASP n 
1 155 ASN n 
1 156 LYS n 
1 157 LYS n 
1 158 THR n 
1 159 ARG n 
1 160 ILE n 
1 161 ILE n 
1 162 PRO n 
1 163 ARG n 
1 164 HIS n 
1 165 LEU n 
1 166 GLN n 
1 167 LEU n 
1 168 ALA n 
1 169 VAL n 
1 170 ARG n 
1 171 ASN n 
1 172 ASP n 
1 173 GLU n 
1 174 GLU n 
1 175 LEU n 
1 176 ASN n 
1 177 LYS n 
1 178 LEU n 
1 179 LEU n 
1 180 GLY n 
1 181 GLY n 
1 182 VAL n 
1 183 THR n 
1 184 ILE n 
1 185 ALA n 
1 186 GLN n 
2 1   ASP n 
2 2   ASN n 
2 3   GLU n 
2 4   ALA n 
2 5   TYR n 
2 6   GLU n 
2 7   MET n 
2 8   PRO n 
2 9   SER n 
2 10  GLU n 
2 11  GLU n 
2 12  GLY n 
2 13  TYR n 
2 14  GLN n 
2 15  ASP n 
2 16  TYR n 
2 17  GLU n 
2 18  PRO n 
2 19  GLU n 
2 20  ALA n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1  94  'African clawed frog' ? ? ? ? ? ? ? ? 'Xenopus laevis' 8355 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
1 2 sample 'Biological sequence' 95 186 'African clawed frog' ? ? ? ? ? ? ? ? 'Xenopus laevis' 8355 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       20 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'  ? 'Cl -1'          35.453  
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   33   ?    ?   ?   A . n 
A 1 2   ARG 2   34   ?    ?   ?   A . n 
A 1 3   LYS 3   35   35   LYS LYS A . n 
A 1 4   GLU 4   36   36   GLU GLU A . n 
A 1 5   SER 5   37   37   SER SER A . n 
A 1 6   TYR 6   38   38   TYR TYR A . n 
A 1 7   ALA 7   39   39   ALA ALA A . n 
A 1 8   ILE 8   40   40   ILE ILE A . n 
A 1 9   TYR 9   41   41   TYR TYR A . n 
A 1 10  VAL 10  42   42   VAL VAL A . n 
A 1 11  TYR 11  43   43   TYR TYR A . n 
A 1 12  LYS 12  44   44   LYS LYS A . n 
A 1 13  VAL 13  45   45   VAL VAL A . n 
A 1 14  LEU 14  46   46   LEU LEU A . n 
A 1 15  LYS 15  47   47   LYS LYS A . n 
A 1 16  GLN 16  48   48   GLN GLN A . n 
A 1 17  VAL 17  49   49   VAL VAL A . n 
A 1 18  HIS 18  50   50   HIS HIS A . n 
A 1 19  PRO 19  51   51   PRO PRO A . n 
A 1 20  ASP 20  52   52   ASP ASP A . n 
A 1 21  THR 21  53   53   THR THR A . n 
A 1 22  GLY 22  54   54   GLY GLY A . n 
A 1 23  ILE 23  55   55   ILE ILE A . n 
A 1 24  SER 24  56   56   SER SER A . n 
A 1 25  SER 25  57   57   SER SER A . n 
A 1 26  LYS 26  58   58   LYS LYS A . n 
A 1 27  ALA 27  59   59   ALA ALA A . n 
A 1 28  MET 28  60   60   MET MET A . n 
A 1 29  SER 29  61   61   SER SER A . n 
A 1 30  ILE 30  62   62   ILE ILE A . n 
A 1 31  MET 31  63   63   MET MET A . n 
A 1 32  ASN 32  64   64   ASN ASN A . n 
A 1 33  SER 33  65   65   SER SER A . n 
A 1 34  PHE 34  66   66   PHE PHE A . n 
A 1 35  VAL 35  67   67   VAL VAL A . n 
A 1 36  ASN 36  68   68   ASN ASN A . n 
A 1 37  ASP 37  69   69   ASP ASP A . n 
A 1 38  VAL 38  70   70   VAL VAL A . n 
A 1 39  PHE 39  71   71   PHE PHE A . n 
A 1 40  GLU 40  72   72   GLU GLU A . n 
A 1 41  ARG 41  73   73   ARG ARG A . n 
A 1 42  ILE 42  74   74   ILE ILE A . n 
A 1 43  ALA 43  75   75   ALA ALA A . n 
A 1 44  GLY 44  76   76   GLY GLY A . n 
A 1 45  GLU 45  77   77   GLU GLU A . n 
A 1 46  ALA 46  78   78   ALA ALA A . n 
A 1 47  SER 47  79   79   SER SER A . n 
A 1 48  ARG 48  80   80   ARG ARG A . n 
A 1 49  LEU 49  81   81   LEU LEU A . n 
A 1 50  ALA 50  82   82   ALA ALA A . n 
A 1 51  HIS 51  83   83   HIS HIS A . n 
A 1 52  TYR 52  84   84   TYR TYR A . n 
A 1 53  ASN 53  85   85   ASN ASN A . n 
A 1 54  LYS 54  86   86   LYS LYS A . n 
A 1 55  ARG 55  87   87   ARG ARG A . n 
A 1 56  SER 56  88   88   SER SER A . n 
A 1 57  THR 57  89   89   THR THR A . n 
A 1 58  ILE 58  90   90   ILE ILE A . n 
A 1 59  THR 59  91   91   THR THR A . n 
A 1 60  SER 60  92   92   SER SER A . n 
A 1 61  ARG 61  93   93   ARG ARG A . n 
A 1 62  GLU 62  94   94   GLU GLU A . n 
A 1 63  ILE 63  95   95   ILE ILE A . n 
A 1 64  GLN 64  96   96   GLN GLN A . n 
A 1 65  THR 65  97   97   THR THR A . n 
A 1 66  ALA 66  98   98   ALA ALA A . n 
A 1 67  VAL 67  99   99   VAL VAL A . n 
A 1 68  ARG 68  100  100  ARG ARG A . n 
A 1 69  LEU 69  101  101  LEU LEU A . n 
A 1 70  LEU 70  102  102  LEU LEU A . n 
A 1 71  LEU 71  103  103  LEU LEU A . n 
A 1 72  PRO 72  104  104  PRO PRO A . n 
A 1 73  GLY 73  105  105  GLY GLY A . n 
A 1 74  GLU 74  106  106  GLU GLU A . n 
A 1 75  LEU 75  107  107  LEU LEU A . n 
A 1 76  ALA 76  108  108  ALA ALA A . n 
A 1 77  LYS 77  109  109  LYS LYS A . n 
A 1 78  HIS 78  110  110  HIS HIS A . n 
A 1 79  ALA 79  111  111  ALA ALA A . n 
A 1 80  VAL 80  112  112  VAL VAL A . n 
A 1 81  SER 81  113  113  SER SER A . n 
A 1 82  GLU 82  114  114  GLU GLU A . n 
A 1 83  GLY 83  115  115  GLY GLY A . n 
A 1 84  THR 84  116  116  THR THR A . n 
A 1 85  LYS 85  117  117  LYS LYS A . n 
A 1 86  ALA 86  118  118  ALA ALA A . n 
A 1 87  VAL 87  119  119  VAL VAL A . n 
A 1 88  THR 88  120  120  THR THR A . n 
A 1 89  LYS 89  121  121  LYS LYS A . n 
A 1 90  TYR 90  122  122  TYR TYR A . n 
A 1 91  THR 91  123  123  THR THR A . n 
A 1 92  SER 92  124  124  SER SER A . n 
A 1 93  ALA 93  125  125  ALA ALA A . n 
A 1 94  LYS 94  126  126  LYS LYS A . n 
A 1 95  LYS 95  1014 1014 LYS LYS A . n 
A 1 96  ALA 96  1015 1015 ALA ALA A . n 
A 1 97  LYS 97  1016 1016 LYS LYS A . n 
A 1 98  THR 98  1017 1017 THR THR A . n 
A 1 99  ARG 99  1018 1018 ARG ARG A . n 
A 1 100 SER 100 1019 1019 SER SER A . n 
A 1 101 SER 101 1020 1020 SER SER A . n 
A 1 102 ARG 102 1021 1021 ARG ARG A . n 
A 1 103 ALA 103 1022 1022 ALA ALA A . n 
A 1 104 GLY 104 1023 1023 GLY GLY A . n 
A 1 105 LEU 105 1024 1024 LEU LEU A . n 
A 1 106 GLN 106 1025 1025 GLN GLN A . n 
A 1 107 PHE 107 1026 1026 PHE PHE A . n 
A 1 108 PRO 108 1027 1027 PRO PRO A . n 
A 1 109 VAL 109 1028 1028 VAL VAL A . n 
A 1 110 GLY 110 1029 1029 GLY GLY A . n 
A 1 111 ARG 111 1030 1030 ARG ARG A . n 
A 1 112 VAL 112 1031 1031 VAL VAL A . n 
A 1 113 HIS 113 1032 1032 HIS HIS A . n 
A 1 114 ARG 114 1033 1033 ARG ARG A . n 
A 1 115 LEU 115 1034 1034 LEU LEU A . n 
A 1 116 LEU 116 1035 1035 LEU LEU A . n 
A 1 117 ARG 117 1036 1036 ARG ARG A . n 
A 1 118 LYS 118 1037 1037 LYS LYS A . n 
A 1 119 GLY 119 1038 1038 GLY GLY A . n 
A 1 120 ASN 120 1039 1039 ASN ASN A . n 
A 1 121 TYR 121 1040 1040 TYR TYR A . n 
A 1 122 ALA 122 1041 1041 ALA ALA A . n 
A 1 123 GLU 123 1042 1042 GLU GLU A . n 
A 1 124 ARG 124 1043 1043 ARG ARG A . n 
A 1 125 VAL 125 1044 1044 VAL VAL A . n 
A 1 126 GLY 126 1045 1045 GLY GLY A . n 
A 1 127 ALA 127 1046 1046 ALA ALA A . n 
A 1 128 GLY 128 1047 1047 GLY GLY A . n 
A 1 129 ALA 129 1048 1048 ALA ALA A . n 
A 1 130 PRO 130 1049 1049 PRO PRO A . n 
A 1 131 VAL 131 1050 1050 VAL VAL A . n 
A 1 132 TYR 132 1051 1051 TYR TYR A . n 
A 1 133 LEU 133 1052 1052 LEU LEU A . n 
A 1 134 ALA 134 1053 1053 ALA ALA A . n 
A 1 135 ALA 135 1054 1054 ALA ALA A . n 
A 1 136 VAL 136 1055 1055 VAL VAL A . n 
A 1 137 LEU 137 1056 1056 LEU LEU A . n 
A 1 138 GLU 138 1057 1057 GLU GLU A . n 
A 1 139 TYR 139 1058 1058 TYR TYR A . n 
A 1 140 LEU 140 1059 1059 LEU LEU A . n 
A 1 141 THR 141 1060 1060 THR THR A . n 
A 1 142 ALA 142 1061 1061 ALA ALA A . n 
A 1 143 GLU 143 1062 1062 GLU GLU A . n 
A 1 144 ILE 144 1063 1063 ILE ILE A . n 
A 1 145 LEU 145 1064 1064 LEU LEU A . n 
A 1 146 GLU 146 1065 1065 GLU GLU A . n 
A 1 147 LEU 147 1066 1066 LEU LEU A . n 
A 1 148 ALA 148 1067 1067 ALA ALA A . n 
A 1 149 GLY 149 1068 1068 GLY GLY A . n 
A 1 150 ASN 150 1069 1069 ASN ASN A . n 
A 1 151 ALA 151 1070 1070 ALA ALA A . n 
A 1 152 ALA 152 1071 1071 ALA ALA A . n 
A 1 153 ARG 153 1072 1072 ARG ARG A . n 
A 1 154 ASP 154 1073 1073 ASP ASP A . n 
A 1 155 ASN 155 1074 1074 ASN ASN A . n 
A 1 156 LYS 156 1075 1075 LYS LYS A . n 
A 1 157 LYS 157 1076 1076 LYS LYS A . n 
A 1 158 THR 158 1077 1077 THR THR A . n 
A 1 159 ARG 159 1078 1078 ARG ARG A . n 
A 1 160 ILE 160 1079 1079 ILE ILE A . n 
A 1 161 ILE 161 1080 1080 ILE ILE A . n 
A 1 162 PRO 162 1081 1081 PRO PRO A . n 
A 1 163 ARG 163 1082 1082 ARG ARG A . n 
A 1 164 HIS 164 1083 1083 HIS HIS A . n 
A 1 165 LEU 165 1084 1084 LEU LEU A . n 
A 1 166 GLN 166 1085 1085 GLN GLN A . n 
A 1 167 LEU 167 1086 1086 LEU LEU A . n 
A 1 168 ALA 168 1087 1087 ALA ALA A . n 
A 1 169 VAL 169 1088 1088 VAL VAL A . n 
A 1 170 ARG 170 1089 1089 ARG ARG A . n 
A 1 171 ASN 171 1090 1090 ASN ASN A . n 
A 1 172 ASP 172 1091 1091 ASP ASP A . n 
A 1 173 GLU 173 1092 1092 GLU GLU A . n 
A 1 174 GLU 174 1093 1093 GLU GLU A . n 
A 1 175 LEU 175 1094 1094 LEU LEU A . n 
A 1 176 ASN 176 1095 1095 ASN ASN A . n 
A 1 177 LYS 177 1096 1096 LYS LYS A . n 
A 1 178 LEU 178 1097 1097 LEU LEU A . n 
A 1 179 LEU 179 1098 1098 LEU LEU A . n 
A 1 180 GLY 180 1099 1099 GLY GLY A . n 
A 1 181 GLY 181 1100 1100 GLY GLY A . n 
A 1 182 VAL 182 1101 1101 VAL VAL A . n 
A 1 183 THR 183 1102 1102 THR THR A . n 
A 1 184 ILE 184 1103 1103 ILE ILE A . n 
A 1 185 ALA 185 1104 ?    ?   ?   A . n 
A 1 186 GLN 186 1105 ?    ?   ?   A . n 
B 1 1   GLY 1   33   ?    ?   ?   B . n 
B 1 2   ARG 2   34   ?    ?   ?   B . n 
B 1 3   LYS 3   35   ?    ?   ?   B . n 
B 1 4   GLU 4   36   36   GLU GLU B . n 
B 1 5   SER 5   37   37   SER SER B . n 
B 1 6   TYR 6   38   38   TYR TYR B . n 
B 1 7   ALA 7   39   39   ALA ALA B . n 
B 1 8   ILE 8   40   40   ILE ILE B . n 
B 1 9   TYR 9   41   41   TYR TYR B . n 
B 1 10  VAL 10  42   42   VAL VAL B . n 
B 1 11  TYR 11  43   43   TYR TYR B . n 
B 1 12  LYS 12  44   44   LYS LYS B . n 
B 1 13  VAL 13  45   45   VAL VAL B . n 
B 1 14  LEU 14  46   46   LEU LEU B . n 
B 1 15  LYS 15  47   47   LYS LYS B . n 
B 1 16  GLN 16  48   48   GLN GLN B . n 
B 1 17  VAL 17  49   49   VAL VAL B . n 
B 1 18  HIS 18  50   50   HIS HIS B . n 
B 1 19  PRO 19  51   51   PRO PRO B . n 
B 1 20  ASP 20  52   52   ASP ASP B . n 
B 1 21  THR 21  53   53   THR THR B . n 
B 1 22  GLY 22  54   54   GLY GLY B . n 
B 1 23  ILE 23  55   55   ILE ILE B . n 
B 1 24  SER 24  56   56   SER SER B . n 
B 1 25  SER 25  57   57   SER SER B . n 
B 1 26  LYS 26  58   58   LYS LYS B . n 
B 1 27  ALA 27  59   59   ALA ALA B . n 
B 1 28  MET 28  60   60   MET MET B . n 
B 1 29  SER 29  61   61   SER SER B . n 
B 1 30  ILE 30  62   62   ILE ILE B . n 
B 1 31  MET 31  63   63   MET MET B . n 
B 1 32  ASN 32  64   64   ASN ASN B . n 
B 1 33  SER 33  65   65   SER SER B . n 
B 1 34  PHE 34  66   66   PHE PHE B . n 
B 1 35  VAL 35  67   67   VAL VAL B . n 
B 1 36  ASN 36  68   68   ASN ASN B . n 
B 1 37  ASP 37  69   69   ASP ASP B . n 
B 1 38  VAL 38  70   70   VAL VAL B . n 
B 1 39  PHE 39  71   71   PHE PHE B . n 
B 1 40  GLU 40  72   72   GLU GLU B . n 
B 1 41  ARG 41  73   73   ARG ARG B . n 
B 1 42  ILE 42  74   74   ILE ILE B . n 
B 1 43  ALA 43  75   75   ALA ALA B . n 
B 1 44  GLY 44  76   76   GLY GLY B . n 
B 1 45  GLU 45  77   77   GLU GLU B . n 
B 1 46  ALA 46  78   78   ALA ALA B . n 
B 1 47  SER 47  79   79   SER SER B . n 
B 1 48  ARG 48  80   80   ARG ARG B . n 
B 1 49  LEU 49  81   81   LEU LEU B . n 
B 1 50  ALA 50  82   82   ALA ALA B . n 
B 1 51  HIS 51  83   83   HIS HIS B . n 
B 1 52  TYR 52  84   84   TYR TYR B . n 
B 1 53  ASN 53  85   85   ASN ASN B . n 
B 1 54  LYS 54  86   86   LYS LYS B . n 
B 1 55  ARG 55  87   87   ARG ARG B . n 
B 1 56  SER 56  88   88   SER SER B . n 
B 1 57  THR 57  89   89   THR THR B . n 
B 1 58  ILE 58  90   90   ILE ILE B . n 
B 1 59  THR 59  91   91   THR THR B . n 
B 1 60  SER 60  92   92   SER SER B . n 
B 1 61  ARG 61  93   93   ARG ARG B . n 
B 1 62  GLU 62  94   94   GLU GLU B . n 
B 1 63  ILE 63  95   95   ILE ILE B . n 
B 1 64  GLN 64  96   96   GLN GLN B . n 
B 1 65  THR 65  97   97   THR THR B . n 
B 1 66  ALA 66  98   98   ALA ALA B . n 
B 1 67  VAL 67  99   99   VAL VAL B . n 
B 1 68  ARG 68  100  100  ARG ARG B . n 
B 1 69  LEU 69  101  101  LEU LEU B . n 
B 1 70  LEU 70  102  102  LEU LEU B . n 
B 1 71  LEU 71  103  103  LEU LEU B . n 
B 1 72  PRO 72  104  104  PRO PRO B . n 
B 1 73  GLY 73  105  105  GLY GLY B . n 
B 1 74  GLU 74  106  106  GLU GLU B . n 
B 1 75  LEU 75  107  107  LEU LEU B . n 
B 1 76  ALA 76  108  108  ALA ALA B . n 
B 1 77  LYS 77  109  109  LYS LYS B . n 
B 1 78  HIS 78  110  110  HIS HIS B . n 
B 1 79  ALA 79  111  111  ALA ALA B . n 
B 1 80  VAL 80  112  112  VAL VAL B . n 
B 1 81  SER 81  113  113  SER SER B . n 
B 1 82  GLU 82  114  114  GLU GLU B . n 
B 1 83  GLY 83  115  115  GLY GLY B . n 
B 1 84  THR 84  116  116  THR THR B . n 
B 1 85  LYS 85  117  117  LYS LYS B . n 
B 1 86  ALA 86  118  118  ALA ALA B . n 
B 1 87  VAL 87  119  119  VAL VAL B . n 
B 1 88  THR 88  120  120  THR THR B . n 
B 1 89  LYS 89  121  121  LYS LYS B . n 
B 1 90  TYR 90  122  122  TYR TYR B . n 
B 1 91  THR 91  123  123  THR THR B . n 
B 1 92  SER 92  124  124  SER SER B . n 
B 1 93  ALA 93  125  125  ALA ALA B . n 
B 1 94  LYS 94  126  126  LYS LYS B . n 
B 1 95  LYS 95  1014 1014 LYS LYS B . n 
B 1 96  ALA 96  1015 1015 ALA ALA B . n 
B 1 97  LYS 97  1016 1016 LYS LYS B . n 
B 1 98  THR 98  1017 1017 THR THR B . n 
B 1 99  ARG 99  1018 1018 ARG ARG B . n 
B 1 100 SER 100 1019 1019 SER SER B . n 
B 1 101 SER 101 1020 1020 SER SER B . n 
B 1 102 ARG 102 1021 1021 ARG ARG B . n 
B 1 103 ALA 103 1022 1022 ALA ALA B . n 
B 1 104 GLY 104 1023 1023 GLY GLY B . n 
B 1 105 LEU 105 1024 1024 LEU LEU B . n 
B 1 106 GLN 106 1025 1025 GLN GLN B . n 
B 1 107 PHE 107 1026 1026 PHE PHE B . n 
B 1 108 PRO 108 1027 1027 PRO PRO B . n 
B 1 109 VAL 109 1028 1028 VAL VAL B . n 
B 1 110 GLY 110 1029 1029 GLY GLY B . n 
B 1 111 ARG 111 1030 1030 ARG ARG B . n 
B 1 112 VAL 112 1031 1031 VAL VAL B . n 
B 1 113 HIS 113 1032 1032 HIS HIS B . n 
B 1 114 ARG 114 1033 1033 ARG ARG B . n 
B 1 115 LEU 115 1034 1034 LEU LEU B . n 
B 1 116 LEU 116 1035 1035 LEU LEU B . n 
B 1 117 ARG 117 1036 1036 ARG ARG B . n 
B 1 118 LYS 118 1037 1037 LYS LYS B . n 
B 1 119 GLY 119 1038 1038 GLY GLY B . n 
B 1 120 ASN 120 1039 1039 ASN ASN B . n 
B 1 121 TYR 121 1040 1040 TYR TYR B . n 
B 1 122 ALA 122 1041 1041 ALA ALA B . n 
B 1 123 GLU 123 1042 1042 GLU GLU B . n 
B 1 124 ARG 124 1043 1043 ARG ARG B . n 
B 1 125 VAL 125 1044 1044 VAL VAL B . n 
B 1 126 GLY 126 1045 1045 GLY GLY B . n 
B 1 127 ALA 127 1046 1046 ALA ALA B . n 
B 1 128 GLY 128 1047 1047 GLY GLY B . n 
B 1 129 ALA 129 1048 1048 ALA ALA B . n 
B 1 130 PRO 130 1049 1049 PRO PRO B . n 
B 1 131 VAL 131 1050 1050 VAL VAL B . n 
B 1 132 TYR 132 1051 1051 TYR TYR B . n 
B 1 133 LEU 133 1052 1052 LEU LEU B . n 
B 1 134 ALA 134 1053 1053 ALA ALA B . n 
B 1 135 ALA 135 1054 1054 ALA ALA B . n 
B 1 136 VAL 136 1055 1055 VAL VAL B . n 
B 1 137 LEU 137 1056 1056 LEU LEU B . n 
B 1 138 GLU 138 1057 1057 GLU GLU B . n 
B 1 139 TYR 139 1058 1058 TYR TYR B . n 
B 1 140 LEU 140 1059 1059 LEU LEU B . n 
B 1 141 THR 141 1060 1060 THR THR B . n 
B 1 142 ALA 142 1061 1061 ALA ALA B . n 
B 1 143 GLU 143 1062 1062 GLU GLU B . n 
B 1 144 ILE 144 1063 1063 ILE ILE B . n 
B 1 145 LEU 145 1064 1064 LEU LEU B . n 
B 1 146 GLU 146 1065 1065 GLU GLU B . n 
B 1 147 LEU 147 1066 1066 LEU LEU B . n 
B 1 148 ALA 148 1067 1067 ALA ALA B . n 
B 1 149 GLY 149 1068 1068 GLY GLY B . n 
B 1 150 ASN 150 1069 1069 ASN ASN B . n 
B 1 151 ALA 151 1070 1070 ALA ALA B . n 
B 1 152 ALA 152 1071 1071 ALA ALA B . n 
B 1 153 ARG 153 1072 1072 ARG ARG B . n 
B 1 154 ASP 154 1073 1073 ASP ASP B . n 
B 1 155 ASN 155 1074 1074 ASN ASN B . n 
B 1 156 LYS 156 1075 1075 LYS LYS B . n 
B 1 157 LYS 157 1076 1076 LYS LYS B . n 
B 1 158 THR 158 1077 1077 THR THR B . n 
B 1 159 ARG 159 1078 1078 ARG ARG B . n 
B 1 160 ILE 160 1079 1079 ILE ILE B . n 
B 1 161 ILE 161 1080 1080 ILE ILE B . n 
B 1 162 PRO 162 1081 1081 PRO PRO B . n 
B 1 163 ARG 163 1082 1082 ARG ARG B . n 
B 1 164 HIS 164 1083 1083 HIS HIS B . n 
B 1 165 LEU 165 1084 1084 LEU LEU B . n 
B 1 166 GLN 166 1085 1085 GLN GLN B . n 
B 1 167 LEU 167 1086 1086 LEU LEU B . n 
B 1 168 ALA 168 1087 1087 ALA ALA B . n 
B 1 169 VAL 169 1088 1088 VAL VAL B . n 
B 1 170 ARG 170 1089 1089 ARG ARG B . n 
B 1 171 ASN 171 1090 1090 ASN ASN B . n 
B 1 172 ASP 172 1091 1091 ASP ASP B . n 
B 1 173 GLU 173 1092 1092 GLU GLU B . n 
B 1 174 GLU 174 1093 1093 GLU GLU B . n 
B 1 175 LEU 175 1094 1094 LEU LEU B . n 
B 1 176 ASN 176 1095 1095 ASN ASN B . n 
B 1 177 LYS 177 1096 1096 LYS LYS B . n 
B 1 178 LEU 178 1097 1097 LEU LEU B . n 
B 1 179 LEU 179 1098 1098 LEU LEU B . n 
B 1 180 GLY 180 1099 1099 GLY GLY B . n 
B 1 181 GLY 181 1100 1100 GLY GLY B . n 
B 1 182 VAL 182 1101 1101 VAL VAL B . n 
B 1 183 THR 183 1102 1102 THR THR B . n 
B 1 184 ILE 184 1103 ?    ?   ?   B . n 
B 1 185 ALA 185 1104 ?    ?   ?   B . n 
B 1 186 GLN 186 1105 ?    ?   ?   B . n 
C 2 1   ASP 1   121  ?    ?   ?   C . n 
C 2 2   ASN 2   122  ?    ?   ?   C . n 
C 2 3   GLU 3   123  ?    ?   ?   C . n 
C 2 4   ALA 4   124  ?    ?   ?   C . n 
C 2 5   TYR 5   125  ?    ?   ?   C . n 
C 2 6   GLU 6   126  ?    ?   ?   C . n 
C 2 7   MET 7   127  ?    ?   ?   C . n 
C 2 8   PRO 8   128  ?    ?   ?   C . n 
C 2 9   SER 9   129  ?    ?   ?   C . n 
C 2 10  GLU 10  130  ?    ?   ?   C . n 
C 2 11  GLU 11  131  131  GLU GLU C . n 
C 2 12  GLY 12  132  132  GLY GLY C . n 
C 2 13  TYR 13  133  133  TYR TYR C . n 
C 2 14  GLN 14  134  134  GLN GLN C . n 
C 2 15  ASP 15  135  135  ASP ASP C . n 
C 2 16  TYR 16  136  136  TYR TYR C . n 
C 2 17  GLU 17  137  137  GLU GLU C . n 
C 2 18  PRO 18  138  138  PRO PRO C . n 
C 2 19  GLU 19  139  139  GLU GLU C . n 
C 2 20  ALA 20  140  140  ALA ALA C . n 
D 2 1   ASP 1   121  ?    ?   ?   D . n 
D 2 2   ASN 2   122  ?    ?   ?   D . n 
D 2 3   GLU 3   123  ?    ?   ?   D . n 
D 2 4   ALA 4   124  ?    ?   ?   D . n 
D 2 5   TYR 5   125  ?    ?   ?   D . n 
D 2 6   GLU 6   126  ?    ?   ?   D . n 
D 2 7   MET 7   127  ?    ?   ?   D . n 
D 2 8   PRO 8   128  128  PRO PRO D . n 
D 2 9   SER 9   129  129  SER SER D . n 
D 2 10  GLU 10  130  130  GLU GLU D . n 
D 2 11  GLU 11  131  131  GLU GLU D . n 
D 2 12  GLY 12  132  132  GLY GLY D . n 
D 2 13  TYR 13  133  133  TYR TYR D . n 
D 2 14  GLN 14  134  134  GLN GLN D . n 
D 2 15  ASP 15  135  135  ASP ASP D . n 
D 2 16  TYR 16  136  136  TYR TYR D . n 
D 2 17  GLU 17  137  137  GLU GLU D . n 
D 2 18  PRO 18  138  138  PRO PRO D . n 
D 2 19  GLU 19  139  139  GLU GLU D . n 
D 2 20  ALA 20  140  140  ALA ALA D . 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 
E 3 CL  1   1201 2   CL  CL  A . 
F 3 CL  1   1201 1   CL  CL  B . 
G 4 HOH 1   1301 194 HOH HOH A . 
G 4 HOH 2   1302 12  HOH HOH A . 
G 4 HOH 3   1303 215 HOH HOH A . 
G 4 HOH 4   1304 40  HOH HOH A . 
G 4 HOH 5   1305 2   HOH HOH A . 
G 4 HOH 6   1306 21  HOH HOH A . 
G 4 HOH 7   1307 85  HOH HOH A . 
G 4 HOH 8   1308 9   HOH HOH A . 
G 4 HOH 9   1309 36  HOH HOH A . 
G 4 HOH 10  1310 150 HOH HOH A . 
G 4 HOH 11  1311 42  HOH HOH A . 
G 4 HOH 12  1312 18  HOH HOH A . 
G 4 HOH 13  1313 16  HOH HOH A . 
G 4 HOH 14  1314 116 HOH HOH A . 
G 4 HOH 15  1315 100 HOH HOH A . 
G 4 HOH 16  1316 74  HOH HOH A . 
G 4 HOH 17  1317 15  HOH HOH A . 
G 4 HOH 18  1318 68  HOH HOH A . 
G 4 HOH 19  1319 47  HOH HOH A . 
G 4 HOH 20  1320 55  HOH HOH A . 
G 4 HOH 21  1321 7   HOH HOH A . 
G 4 HOH 22  1322 193 HOH HOH A . 
G 4 HOH 23  1323 48  HOH HOH A . 
G 4 HOH 24  1324 58  HOH HOH A . 
G 4 HOH 25  1325 14  HOH HOH A . 
G 4 HOH 26  1326 73  HOH HOH A . 
G 4 HOH 27  1327 211 HOH HOH A . 
G 4 HOH 28  1328 35  HOH HOH A . 
G 4 HOH 29  1329 148 HOH HOH A . 
G 4 HOH 30  1330 198 HOH HOH A . 
G 4 HOH 31  1331 71  HOH HOH A . 
G 4 HOH 32  1332 178 HOH HOH A . 
G 4 HOH 33  1333 81  HOH HOH A . 
G 4 HOH 34  1334 17  HOH HOH A . 
G 4 HOH 35  1335 23  HOH HOH A . 
G 4 HOH 36  1336 171 HOH HOH A . 
G 4 HOH 37  1337 181 HOH HOH A . 
G 4 HOH 38  1338 31  HOH HOH A . 
G 4 HOH 39  1339 121 HOH HOH A . 
G 4 HOH 40  1340 13  HOH HOH A . 
G 4 HOH 41  1341 199 HOH HOH A . 
G 4 HOH 42  1342 26  HOH HOH A . 
G 4 HOH 43  1343 97  HOH HOH A . 
G 4 HOH 44  1344 86  HOH HOH A . 
G 4 HOH 45  1345 37  HOH HOH A . 
G 4 HOH 46  1346 177 HOH HOH A . 
G 4 HOH 47  1347 130 HOH HOH A . 
G 4 HOH 48  1348 3   HOH HOH A . 
G 4 HOH 49  1349 76  HOH HOH A . 
G 4 HOH 50  1350 103 HOH HOH A . 
G 4 HOH 51  1351 154 HOH HOH A . 
G 4 HOH 52  1352 157 HOH HOH A . 
G 4 HOH 53  1353 145 HOH HOH A . 
G 4 HOH 54  1354 43  HOH HOH A . 
G 4 HOH 55  1355 175 HOH HOH A . 
G 4 HOH 56  1356 108 HOH HOH A . 
G 4 HOH 57  1357 227 HOH HOH A . 
G 4 HOH 58  1358 101 HOH HOH A . 
G 4 HOH 59  1359 96  HOH HOH A . 
G 4 HOH 60  1360 159 HOH HOH A . 
G 4 HOH 61  1361 30  HOH HOH A . 
G 4 HOH 62  1362 146 HOH HOH A . 
G 4 HOH 63  1363 218 HOH HOH A . 
G 4 HOH 64  1364 131 HOH HOH A . 
G 4 HOH 65  1365 226 HOH HOH A . 
G 4 HOH 66  1366 79  HOH HOH A . 
G 4 HOH 67  1367 138 HOH HOH A . 
G 4 HOH 68  1368 120 HOH HOH A . 
G 4 HOH 69  1369 228 HOH HOH A . 
G 4 HOH 70  1370 205 HOH HOH A . 
G 4 HOH 71  1371 191 HOH HOH A . 
G 4 HOH 72  1372 197 HOH HOH A . 
G 4 HOH 73  1373 66  HOH HOH A . 
G 4 HOH 74  1374 65  HOH HOH A . 
G 4 HOH 75  1375 186 HOH HOH A . 
G 4 HOH 76  1376 225 HOH HOH A . 
G 4 HOH 77  1377 169 HOH HOH A . 
G 4 HOH 78  1378 166 HOH HOH A . 
G 4 HOH 79  1379 221 HOH HOH A . 
G 4 HOH 80  1380 105 HOH HOH A . 
G 4 HOH 81  1381 10  HOH HOH A . 
H 4 HOH 1   1301 214 HOH HOH B . 
H 4 HOH 2   1302 25  HOH HOH B . 
H 4 HOH 3   1303 22  HOH HOH B . 
H 4 HOH 4   1304 91  HOH HOH B . 
H 4 HOH 5   1305 212 HOH HOH B . 
H 4 HOH 6   1306 61  HOH HOH B . 
H 4 HOH 7   1307 27  HOH HOH B . 
H 4 HOH 8   1308 117 HOH HOH B . 
H 4 HOH 9   1309 84  HOH HOH B . 
H 4 HOH 10  1310 53  HOH HOH B . 
H 4 HOH 11  1311 49  HOH HOH B . 
H 4 HOH 12  1312 180 HOH HOH B . 
H 4 HOH 13  1313 113 HOH HOH B . 
H 4 HOH 14  1314 19  HOH HOH B . 
H 4 HOH 15  1315 54  HOH HOH B . 
H 4 HOH 16  1316 220 HOH HOH B . 
H 4 HOH 17  1317 222 HOH HOH B . 
H 4 HOH 18  1318 38  HOH HOH B . 
H 4 HOH 19  1319 104 HOH HOH B . 
H 4 HOH 20  1320 135 HOH HOH B . 
H 4 HOH 21  1321 33  HOH HOH B . 
H 4 HOH 22  1322 187 HOH HOH B . 
H 4 HOH 23  1323 172 HOH HOH B . 
H 4 HOH 24  1324 200 HOH HOH B . 
H 4 HOH 25  1325 173 HOH HOH B . 
H 4 HOH 26  1326 155 HOH HOH B . 
H 4 HOH 27  1327 75  HOH HOH B . 
H 4 HOH 28  1328 124 HOH HOH B . 
H 4 HOH 29  1329 5   HOH HOH B . 
H 4 HOH 30  1330 78  HOH HOH B . 
H 4 HOH 31  1331 20  HOH HOH B . 
H 4 HOH 32  1332 110 HOH HOH B . 
H 4 HOH 33  1333 185 HOH HOH B . 
H 4 HOH 34  1334 94  HOH HOH B . 
H 4 HOH 35  1335 52  HOH HOH B . 
H 4 HOH 36  1336 24  HOH HOH B . 
H 4 HOH 37  1337 4   HOH HOH B . 
H 4 HOH 38  1338 39  HOH HOH B . 
H 4 HOH 39  1339 93  HOH HOH B . 
H 4 HOH 40  1340 77  HOH HOH B . 
H 4 HOH 41  1341 80  HOH HOH B . 
H 4 HOH 42  1342 95  HOH HOH B . 
H 4 HOH 43  1343 141 HOH HOH B . 
H 4 HOH 44  1344 118 HOH HOH B . 
H 4 HOH 45  1345 162 HOH HOH B . 
H 4 HOH 46  1346 143 HOH HOH B . 
H 4 HOH 47  1347 62  HOH HOH B . 
H 4 HOH 48  1348 164 HOH HOH B . 
H 4 HOH 49  1349 216 HOH HOH B . 
H 4 HOH 50  1350 46  HOH HOH B . 
H 4 HOH 51  1351 45  HOH HOH B . 
H 4 HOH 52  1352 83  HOH HOH B . 
H 4 HOH 53  1353 88  HOH HOH B . 
H 4 HOH 54  1354 6   HOH HOH B . 
H 4 HOH 55  1355 28  HOH HOH B . 
H 4 HOH 56  1356 192 HOH HOH B . 
H 4 HOH 57  1357 133 HOH HOH B . 
H 4 HOH 58  1358 127 HOH HOH B . 
H 4 HOH 59  1359 140 HOH HOH B . 
H 4 HOH 60  1360 92  HOH HOH B . 
H 4 HOH 61  1361 89  HOH HOH B . 
H 4 HOH 62  1362 60  HOH HOH B . 
H 4 HOH 63  1363 29  HOH HOH B . 
H 4 HOH 64  1364 99  HOH HOH B . 
H 4 HOH 65  1365 67  HOH HOH B . 
H 4 HOH 66  1366 8   HOH HOH B . 
H 4 HOH 67  1367 209 HOH HOH B . 
H 4 HOH 68  1368 167 HOH HOH B . 
H 4 HOH 69  1369 142 HOH HOH B . 
H 4 HOH 70  1370 190 HOH HOH B . 
H 4 HOH 71  1371 196 HOH HOH B . 
H 4 HOH 72  1372 160 HOH HOH B . 
H 4 HOH 73  1373 129 HOH HOH B . 
H 4 HOH 74  1374 106 HOH HOH B . 
H 4 HOH 75  1375 41  HOH HOH B . 
H 4 HOH 76  1376 163 HOH HOH B . 
H 4 HOH 77  1377 161 HOH HOH B . 
H 4 HOH 78  1378 204 HOH HOH B . 
H 4 HOH 79  1379 44  HOH HOH B . 
H 4 HOH 80  1380 112 HOH HOH B . 
H 4 HOH 81  1381 195 HOH HOH B . 
H 4 HOH 82  1382 59  HOH HOH B . 
H 4 HOH 83  1383 217 HOH HOH B . 
H 4 HOH 84  1384 56  HOH HOH B . 
H 4 HOH 85  1385 107 HOH HOH B . 
H 4 HOH 86  1386 176 HOH HOH B . 
H 4 HOH 87  1387 122 HOH HOH B . 
H 4 HOH 88  1388 125 HOH HOH B . 
H 4 HOH 89  1389 136 HOH HOH B . 
H 4 HOH 90  1390 134 HOH HOH B . 
H 4 HOH 91  1391 137 HOH HOH B . 
H 4 HOH 92  1392 63  HOH HOH B . 
H 4 HOH 93  1393 165 HOH HOH B . 
H 4 HOH 94  1394 111 HOH HOH B . 
H 4 HOH 95  1395 51  HOH HOH B . 
H 4 HOH 96  1396 183 HOH HOH B . 
H 4 HOH 97  1397 57  HOH HOH B . 
H 4 HOH 98  1398 168 HOH HOH B . 
H 4 HOH 99  1399 224 HOH HOH B . 
H 4 HOH 100 1400 201 HOH HOH B . 
H 4 HOH 101 1401 149 HOH HOH B . 
H 4 HOH 102 1402 184 HOH HOH B . 
H 4 HOH 103 1403 202 HOH HOH B . 
H 4 HOH 104 1404 115 HOH HOH B . 
H 4 HOH 105 1405 223 HOH HOH B . 
H 4 HOH 106 1406 188 HOH HOH B . 
H 4 HOH 107 1407 206 HOH HOH B . 
H 4 HOH 108 1408 153 HOH HOH B . 
H 4 HOH 109 1409 64  HOH HOH B . 
H 4 HOH 110 1410 98  HOH HOH B . 
H 4 HOH 111 1411 90  HOH HOH B . 
H 4 HOH 112 1412 203 HOH HOH B . 
H 4 HOH 113 1413 213 HOH HOH B . 
H 4 HOH 114 1414 208 HOH HOH B . 
H 4 HOH 115 1415 70  HOH HOH B . 
H 4 HOH 116 1416 114 HOH HOH B . 
H 4 HOH 117 1417 151 HOH HOH B . 
H 4 HOH 118 1418 170 HOH HOH B . 
H 4 HOH 119 1419 69  HOH HOH B . 
H 4 HOH 120 1420 144 HOH HOH B . 
H 4 HOH 121 1421 182 HOH HOH B . 
H 4 HOH 122 1422 189 HOH HOH B . 
H 4 HOH 123 1423 82  HOH HOH B . 
H 4 HOH 124 1424 147 HOH HOH B . 
H 4 HOH 125 1425 174 HOH HOH B . 
I 4 HOH 1   201  152 HOH HOH C . 
J 4 HOH 1   201  119 HOH HOH D . 
J 4 HOH 2   202  210 HOH HOH D . 
J 4 HOH 3   203  132 HOH HOH D . 
J 4 HOH 4   204  126 HOH HOH D . 
J 4 HOH 5   205  139 HOH HOH D . 
J 4 HOH 6   206  32  HOH HOH D . 
J 4 HOH 7   207  11  HOH HOH D . 
J 4 HOH 8   208  219 HOH HOH D . 
J 4 HOH 9   209  1   HOH HOH D . 
J 4 HOH 10  210  156 HOH HOH D . 
J 4 HOH 11  211  179 HOH HOH D . 
J 4 HOH 12  212  50  HOH HOH D . 
J 4 HOH 13  213  123 HOH HOH D . 
J 4 HOH 14  214  34  HOH HOH D . 
J 4 HOH 15  215  128 HOH HOH D . 
J 4 HOH 16  216  158 HOH HOH D . 
J 4 HOH 17  217  87  HOH HOH D . 
J 4 HOH 18  218  72  HOH HOH D . 
J 4 HOH 19  219  102 HOH HOH D . 
J 4 HOH 20  220  109 HOH HOH D . 
J 4 HOH 21  221  207 HOH HOH D . 
# 
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 0 C GLU 131 ? CG  ? C GLU 11 CG  
2  1 Y 0 C GLU 131 ? CD  ? C GLU 11 CD  
3  1 Y 0 C GLU 131 ? OE1 ? C GLU 11 OE1 
4  1 Y 0 C GLU 131 ? OE2 ? C GLU 11 OE2 
5  1 Y 0 C TYR 133 ? CG  ? C TYR 13 CG  
6  1 Y 0 C TYR 133 ? CD1 ? C TYR 13 CD1 
7  1 Y 0 C TYR 133 ? CD2 ? C TYR 13 CD2 
8  1 Y 0 C TYR 133 ? CE1 ? C TYR 13 CE1 
9  1 Y 0 C TYR 133 ? CE2 ? C TYR 13 CE2 
10 1 Y 0 C TYR 133 ? CZ  ? C TYR 13 CZ  
11 1 Y 0 C TYR 133 ? OH  ? C TYR 13 OH  
12 1 Y 0 C ASP 135 ? CG  ? C ASP 15 CG  
13 1 Y 0 C ASP 135 ? OD1 ? C ASP 15 OD1 
14 1 Y 0 C ASP 135 ? OD2 ? C ASP 15 OD2 
15 1 Y 0 C GLU 137 ? CG  ? C GLU 17 CG  
16 1 Y 0 C GLU 137 ? CD  ? C GLU 17 CD  
17 1 Y 0 C GLU 137 ? OE1 ? C GLU 17 OE1 
18 1 Y 0 C GLU 137 ? OE2 ? C GLU 17 OE2 
# 
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  ? ? ? 1.21.2_5419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? iMOSFLM ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZVY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.005 
_cell.length_a_esd                 ? 
_cell.length_b                     68.240 
_cell.length_b_esd                 ? 
_cell.length_c                     102.576 
_cell.length_c_esd                 ? 
_cell.volume                       427021.960 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZVY 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZVY 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.43 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.34 
_exptl_crystal.description                  solid 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM Tris pH 8.0 and 10% PEG 8000.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-09-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.99 
_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                        'ELETTRA BEAMLINE 11.2C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.99 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   11.2C 
_diffrn_source.pdbx_synchrotron_site       ELETTRA 
# 
_reflns.B_iso_Wilson_estimate                          34.36 
_reflns.entry_id                                       8ZVY 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.72 
_reflns.d_resolution_low                               68.24 
_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                                     46279 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          37.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.0 
_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                                    1.72 
_reflns_shell.d_res_low                                     1.75 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2444 
_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                                  0.879 
_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                               47.62 
_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                                 8ZVY 
_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                            1.72 
_refine.ls_d_res_low                             45.48 
_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                     46130 
_refine.ls_number_reflns_R_free                  2316 
_refine.ls_number_reflns_R_work                  43814 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.79 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1921 
_refine.ls_R_factor_R_free                       0.2203 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1906 
_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                      6w4l 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 24.4012 
_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                            0.2318 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.72 
_refine_hist.d_res_low                        45.48 
_refine_hist.number_atoms_solvent             228 
_refine_hist.number_atoms_total               3233 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3003 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         2 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0065  ? 3111 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8856  ? 4215 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0536  ? 483  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0097  ? 544  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.1420 ? 1201 ? f_dihedral_angle_d ? ? 
# 
_refine_ls_restr_ncs.pdbx_ordinal        1 
_refine_ls_restr_ncs.pdbx_refine_id      'X-RAY DIFFRACTION' 
_refine_ls_restr_ncs.dom_id              d_2 
_refine_ls_restr_ncs.pdbx_ens_id         ens_1 
_refine_ls_restr_ncs.rms_dev_position    2.50759650669 
_refine_ls_restr_ncs.weight_position     ? 
_refine_ls_restr_ncs.rms_dev_B_iso       ? 
_refine_ls_restr_ncs.weight_B_iso        ? 
_refine_ls_restr_ncs.pdbx_type           'Torsion NCS' 
_refine_ls_restr_ncs.pdbx_asym_id        A 
_refine_ls_restr_ncs.pdbx_auth_asym_id   A 
_refine_ls_restr_ncs.pdbx_number         ? 
_refine_ls_restr_ncs.pdbx_rms            ? 
_refine_ls_restr_ncs.pdbx_weight         ? 
_refine_ls_restr_ncs.ncs_model_details   ? 
# 
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' 1.72 1.76  . . 133 2553 99.63  . . . . 0.3140 . . . . . . . . . . . 0.3683 
'X-RAY DIFFRACTION' 1.76 1.79  . . 133 2571 99.96  . . . . 0.2732 . . . . . . . . . . . 0.2861 
'X-RAY DIFFRACTION' 1.79 1.84  . . 129 2516 100.00 . . . . 0.2479 . . . . . . . . . . . 0.2933 
'X-RAY DIFFRACTION' 1.84 1.88  . . 145 2528 99.85  . . . . 0.2270 . . . . . . . . . . . 0.2713 
'X-RAY DIFFRACTION' 1.88 1.93  . . 132 2505 98.40  . . . . 0.2700 . . . . . . . . . . . 0.3255 
'X-RAY DIFFRACTION' 1.93 1.99  . . 135 2568 99.89  . . . . 0.2437 . . . . . . . . . . . 0.3030 
'X-RAY DIFFRACTION' 1.99 2.05  . . 133 2553 100.00 . . . . 0.2362 . . . . . . . . . . . 0.3065 
'X-RAY DIFFRACTION' 2.05 2.13  . . 113 2551 99.25  . . . . 0.2132 . . . . . . . . . . . 0.2469 
'X-RAY DIFFRACTION' 2.13 2.21  . . 140 2567 100.00 . . . . 0.1959 . . . . . . . . . . . 0.2609 
'X-RAY DIFFRACTION' 2.21 2.31  . . 139 2537 99.66  . . . . 0.1945 . . . . . . . . . . . 0.2517 
'X-RAY DIFFRACTION' 2.31 2.43  . . 127 2590 100.00 . . . . 0.1835 . . . . . . . . . . . 0.2193 
'X-RAY DIFFRACTION' 2.43 2.59  . . 144 2574 100.00 . . . . 0.1873 . . . . . . . . . . . 0.2321 
'X-RAY DIFFRACTION' 2.59 2.79  . . 137 2595 99.93  . . . . 0.2103 . . . . . . . . . . . 0.2432 
'X-RAY DIFFRACTION' 2.79 3.07  . . 147 2585 100.00 . . . . 0.2028 . . . . . . . . . . . 0.2458 
'X-RAY DIFFRACTION' 3.07 3.51  . . 146 2602 100.00 . . . . 0.1986 . . . . . . . . . . . 0.2349 
'X-RAY DIFFRACTION' 3.51 4.42  . . 152 2639 100.00 . . . . 0.1623 . . . . . . . . . . . 0.1681 
'X-RAY DIFFRACTION' 4.42 45.48 . . 131 2780 99.83  . . . . 0.1681 . . . . . . . . . . . 0.1838 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.matrix[1][1]   0.563830745708 
_struct_ncs_oper.matrix[1][2]   -0.74523461808 
_struct_ncs_oper.matrix[1][3]   -0.355977884438 
_struct_ncs_oper.matrix[2][1]   0.736463557724 
_struct_ncs_oper.matrix[2][2]   0.648753621609 
_struct_ncs_oper.matrix[2][3]   -0.191677245898 
_struct_ncs_oper.matrix[3][1]   0.373786460883 
_struct_ncs_oper.matrix[3][2]   -0.154091214755 
_struct_ncs_oper.matrix[3][3]   0.914625376422 
_struct_ncs_oper.vector[1]      18.3064624572 
_struct_ncs_oper.vector[2]      -6.68472953237 
_struct_ncs_oper.vector[3]      -23.8872756249 
_struct_ncs_oper.details        ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
ens_1 d_1 
;(chain "A" and (resid 37 through 56 or resid 58 through 60 or resid 62 through 63 or resid 66 through 67 or resid 69 through 71 or resid 73 through 91 or resid 93 through 101 or resid 103 through 106 or resid 108 through 115 or resid 117 through 1102))
;
ens_1 d_2 
;(chain "B" and (resid 37 through 56 or resid 58 through 60 or resid 62 through 63 or resid 66 through 67 or resid 69 through 71 or resid 73 through 91 or resid 93 through 101 or resid 103 through 106 or resid 108 through 115 or resid 117 through 1102))
;
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
ens_1 d_1 1  A SER 5  . A SER 24  . A SER 37  A SER 56   ? ? 
ens_1 d_1 2  A LYS 26 . A MET 28  . A LYS 58  A MET 60   ? ? 
ens_1 d_1 3  A ILE 30 . A MET 31  . A ILE 62  A MET 63   ? ? 
ens_1 d_1 4  A PHE 34 . A VAL 35  . A PHE 66  A VAL 67   ? ? 
ens_1 d_1 5  A ASP 37 . A PHE 39  . A ASP 69  A PHE 71   ? ? 
ens_1 d_1 6  A ARG 41 . A THR 59  . A ARG 73  A THR 91   ? ? 
ens_1 d_1 7  A ARG 61 . A LEU 69  . A ARG 93  A LEU 101  ? ? 
ens_1 d_1 8  A LEU 71 . A GLU 74  . A LEU 103 A GLU 106  ? ? 
ens_1 d_1 9  A ALA 76 . A GLY 83  . A ALA 108 A GLY 115  ? ? 
ens_1 d_1 10 A LYS 85 . A THR 183 . A LYS 117 A THR 1102 ? ? 
ens_1 d_2 1  B SER 5  . B SER 24  . B SER 37  B SER 56   ? ? 
ens_1 d_2 2  B LYS 26 . B MET 28  . B LYS 58  B MET 60   ? ? 
ens_1 d_2 3  B ILE 30 . B MET 31  . B ILE 62  B MET 63   ? ? 
ens_1 d_2 4  B PHE 34 . B VAL 35  . B PHE 66  B VAL 67   ? ? 
ens_1 d_2 5  B ASP 37 . B PHE 39  . B ASP 69  B PHE 71   ? ? 
ens_1 d_2 6  B ARG 41 . B THR 59  . B ARG 73  B THR 91   ? ? 
ens_1 d_2 7  B ARG 61 . B LEU 69  . B ARG 93  B LEU 101  ? ? 
ens_1 d_2 8  B LEU 71 . B GLU 74  . B LEU 103 B GLU 106  ? ? 
ens_1 d_2 9  B ALA 76 . B GLY 83  . B ALA 108 B GLY 115  ? ? 
ens_1 d_2 10 B LYS 85 . B THR 183 . B LYS 117 B THR 1102 ? ? 
# 
_struct_ncs_ens.id        ens_1 
_struct_ncs_ens.details   ? 
# 
_struct_ncs_ens_gen.ens_id     ens_1 
_struct_ncs_ens_gen.dom_id_1   d_2 
_struct_ncs_ens_gen.dom_id_2   d_1 
_struct_ncs_ens_gen.oper_id    1 
# 
_struct.entry_id                     8ZVY 
_struct.title                        'Alpha-Synuclein with H2a-H2b dimer complex structure.' 
_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        8ZVY 
_struct_keywords.text            
;Parkinson's disease, histone chaperone, alpha-synuclein, H2a-H2b dimer, (H3-H4)2 tetramer, Neurodegeneration, NUCLEAR PROTEIN
;
_struct_keywords.pdbx_keywords   'NUCLEAR PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP H2B11_XENLA P02281 ? 1 
;RKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVS
EGTKAVTKYTSAK
;
34  
2 UNP H2A1_XENLA  P06897 ? 1 
;KAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEE
LNKLLGGVTIAQ
;
14  
3 UNP SYUA_HUMAN  P37840 ? 2 DNEAYEMPSEEGYQDYEPEA                                                                             121 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8ZVY A 2  ? 94  ? P02281 34  ? 126 ? 34   126  
2 2 8ZVY A 95 ? 186 ? P06897 14  ? 105 ? 1014 1105 
3 1 8ZVY B 2  ? 94  ? P02281 34  ? 126 ? 34   126  
4 2 8ZVY B 95 ? 186 ? P06897 14  ? 105 ? 1014 1105 
5 3 8ZVY C 1  ? 20  ? P37840 121 ? 140 ? 121  140  
6 3 8ZVY D 1  ? 20  ? P37840 121 ? 140 ? 121  140  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8ZVY GLY A 1 ? UNP P02281 ? ? 'expression tag' 33 1 
3 8ZVY GLY B 1 ? UNP P02281 ? ? 'expression tag' 33 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 3240  ? 
1 MORE         -17   ? 
1 'SSA (A^2)'  19790 ? 
# 
_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 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 cross-linking                      
'The binding between Alpha-Synuclein peptide and Histone H2a-H2b dimer was analysed using EDC- and DSS-mediated cross-linking.' 
2 1 'isothermal titration calorimetry' 
;Biophysical studies such as ITC and MicroScale thermophoresis (MST) were performed to quantify the binding interactions between Alpha-Synuclein and Histone H2a-H2b dimer.
;
# 
_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 TYR A 6   ? HIS A 18  ? TYR A 38   HIS A 50   1 ? 13 
HELX_P HELX_P2  AA2 SER A 24  ? ASN A 53  ? SER A 56   ASN A 85   1 ? 30 
HELX_P HELX_P3  AA3 THR A 59  ? LEU A 71  ? THR A 91   LEU A 103  1 ? 13 
HELX_P HELX_P4  AA4 PRO A 72  ? THR A 91  ? PRO A 104  THR A 123  1 ? 20 
HELX_P HELX_P5  AA5 ARG A 99  ? GLY A 104 ? ARG A 1018 GLY A 1023 5 ? 6  
HELX_P HELX_P6  AA6 PRO A 108 ? GLY A 119 ? PRO A 1027 GLY A 1038 1 ? 12 
HELX_P HELX_P7  AA7 ALA A 127 ? ASN A 155 ? ALA A 1046 ASN A 1074 1 ? 29 
HELX_P HELX_P8  AA8 ILE A 161 ? ASN A 171 ? ILE A 1080 ASN A 1090 1 ? 11 
HELX_P HELX_P9  AA9 ASP A 172 ? VAL A 182 ? ASP A 1091 VAL A 1101 1 ? 11 
HELX_P HELX_P10 AB1 TYR B 6   ? HIS B 18  ? TYR B 38   HIS B 50   1 ? 13 
HELX_P HELX_P11 AB2 SER B 24  ? HIS B 51  ? SER B 56   HIS B 83   1 ? 28 
HELX_P HELX_P12 AB3 THR B 59  ? LEU B 71  ? THR B 91   LEU B 103  1 ? 13 
HELX_P HELX_P13 AB4 GLY B 73  ? THR B 91  ? GLY B 105  THR B 123  1 ? 19 
HELX_P HELX_P14 AB5 THR B 98  ? GLY B 104 ? THR B 1017 GLY B 1023 1 ? 7  
HELX_P HELX_P15 AB6 PRO B 108 ? GLY B 119 ? PRO B 1027 GLY B 1038 1 ? 12 
HELX_P HELX_P16 AB7 ALA B 127 ? ASN B 155 ? ALA B 1046 ASN B 1074 1 ? 29 
HELX_P HELX_P17 AB8 ILE B 161 ? ASN B 171 ? ILE B 1080 ASN B 1090 1 ? 11 
HELX_P HELX_P18 AB9 ASP B 172 ? GLY B 180 ? ASP B 1091 GLY B 1099 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel 
AA2 1 2 ? parallel 
AA3 1 2 ? parallel 
AA4 1 2 ? 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 GLY A 22  ? ILE A 23  ? GLY A 54   ILE A 55   
AA1 2 ARG A 159 ? ILE A 160 ? ARG A 1078 ILE A 1079 
AA2 1 THR A 57  ? ILE A 58  ? THR A 89   ILE A 90   
AA2 2 ARG A 124 ? VAL A 125 ? ARG A 1043 VAL A 1044 
AA3 1 GLY B 22  ? ILE B 23  ? GLY B 54   ILE B 55   
AA3 2 ARG B 159 ? ILE B 160 ? ARG B 1078 ILE B 1079 
AA4 1 THR B 57  ? ILE B 58  ? THR B 89   ILE B 90   
AA4 2 ARG B 124 ? VAL B 125 ? ARG B 1043 VAL B 1044 
# 
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 GLY A 22 ? N GLY A 54 O ILE A 160 ? O ILE A 1079 
AA2 1 2 N ILE A 58 ? N ILE A 90 O ARG A 124 ? O ARG A 1043 
AA3 1 2 N GLY B 22 ? N GLY B 54 O ILE B 160 ? O ILE B 1079 
AA4 1 2 N ILE B 58 ? N ILE B 90 O ARG B 124 ? O ARG B 1043 
# 
_pdbx_entry_details.entry_id                   8ZVY 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ALA A 1015 ? ? 82.91 -1.83  
2 1 GLU C 137  ? ? 68.97 161.60 
3 1 GLU D 139  ? ? 85.67 4.64   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
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 -3.68298708867  4.80461009245  13.4394913318  0.293808779258 ? 0.00755710775954 ? -0.0212276524768 
? 0.162783465092 ? 0.00244811336714  ? 0.314808811099 ? 3.2632382278  ? 0.5780952067    ? 0.329144113792   ? 2.58293639185 ? 
-0.00418253785931 ? 2.87307769392 ? -0.126163414187 ? 0.198698061125   ? 0.573028408094  ? -0.180464308859 ? 0.0380986635718  ? 
-0.0809800783914 ? -0.488910738445 ? 0.0844988379947 ? -0.0145926115276 ? 
2 'X-RAY DIFFRACTION' ? refined 8.00086659127   -8.77557588943 -13.6707323148 0.138622106507 ? -0.019047648898  ? 0.00115306852284 
? 0.242394335842 ? -0.00549282251577 ? 0.227122541907 ? 1.80270509835 ? -0.386934045015 ? -0.0614348670815 ? 3.21841638751 ? 
-0.669182346823   ? 3.05663858949 ? 0.0114459072628 ? -0.0506514201528 ? 0.137598124875  ? 0.0660096394713 ? -0.0532313279329 ? 
-0.0255164038142 ? -0.20309993521  ? -0.144666445385 ? 0.0392350863927  ? 
3 'X-RAY DIFFRACTION' ? refined -2.45343752248  25.1783994929  10.0438568678  1.49935430985  ? -0.217995613407  ? -0.3151126527    
? 0.751092783603 ? 0.0825565999382   ? 1.1674966271   ? 3.6248040306  ? -2.43983097619  ? 3.00490062154    ? 5.43556368555 ? 
-3.76270714267    ? 8.14712354336 ? -0.831362593305 ? 0.384663347547   ? 0.886491564822  ? -1.30343199087  ? 1.30632233019    ? 
1.21887082142    ? -0.923683125041 ? -0.632828904969 ? -0.637694298087  ? 
4 'X-RAY DIFFRACTION' ? refined -0.795325952068 4.70321158719  -35.3912639634 0.669206263303 ? 0.186813776327   ? -0.0280405652665 
? 0.749914976469 ? 0.050410229791    ? 0.756686781365 ? 3.29972212747 ? -1.34541185241  ? 2.73126064374    ? 7.07444803335 ? 
-4.41866842452    ? 3.94526003818 ? 0.0550624280351 ? 0.0968063194325  ? -0.266466168743 ? -0.381047747417 ? -0.297930747128  ? 
-1.40184142414   ? 1.21862285402   ? 1.70221901185   ? 0.137418611195   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1 A 35  ? A 182 A 1103 ? ? '(chain A and resseq 35:1103)' 
2 'X-RAY DIFFRACTION' 2 B 1 B 36  ? B 180 B 1102 ? ? '(chain B and resseq 36:1102)' 
3 'X-RAY DIFFRACTION' 3 C 1 C 131 ? C 10  C 140  ? ? '(chain C and resseq 130:140)' 
4 'X-RAY DIFFRACTION' 4 D 1 D 128 ? D 13  D 140  ? ? '(chain D and resseq 127:140)' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 33   ? A GLY 1   
2  1 Y 1 A ARG 34   ? A ARG 2   
3  1 Y 1 A ALA 1104 ? A ALA 185 
4  1 Y 1 A GLN 1105 ? A GLN 186 
5  1 Y 1 B GLY 33   ? B GLY 1   
6  1 Y 1 B ARG 34   ? B ARG 2   
7  1 Y 1 B LYS 35   ? B LYS 3   
8  1 Y 1 B ILE 1103 ? B ILE 184 
9  1 Y 1 B ALA 1104 ? B ALA 185 
10 1 Y 1 B GLN 1105 ? B GLN 186 
11 1 Y 1 C ASP 121  ? C ASP 1   
12 1 Y 1 C ASN 122  ? C ASN 2   
13 1 Y 1 C GLU 123  ? C GLU 3   
14 1 Y 1 C ALA 124  ? C ALA 4   
15 1 Y 1 C TYR 125  ? C TYR 5   
16 1 Y 1 C GLU 126  ? C GLU 6   
17 1 Y 1 C MET 127  ? C MET 7   
18 1 Y 1 C PRO 128  ? C PRO 8   
19 1 Y 1 C SER 129  ? C SER 9   
20 1 Y 1 C GLU 130  ? C GLU 10  
21 1 Y 1 D ASP 121  ? D ASP 1   
22 1 Y 1 D ASN 122  ? D ASN 2   
23 1 Y 1 D GLU 123  ? D GLU 3   
24 1 Y 1 D ALA 124  ? D ALA 4   
25 1 Y 1 D TYR 125  ? D TYR 5   
26 1 Y 1 D GLU 126  ? D GLU 6   
27 1 Y 1 D MET 127  ? D MET 7   
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
GLN N    N  N N 75  
GLN CA   C  N S 76  
GLN C    C  N N 77  
GLN O    O  N N 78  
GLN CB   C  N N 79  
GLN CG   C  N N 80  
GLN CD   C  N N 81  
GLN OE1  O  N N 82  
GLN NE2  N  N N 83  
GLN OXT  O  N N 84  
GLN H    H  N N 85  
GLN H2   H  N N 86  
GLN HA   H  N N 87  
GLN HB2  H  N N 88  
GLN HB3  H  N N 89  
GLN HG2  H  N N 90  
GLN HG3  H  N N 91  
GLN HE21 H  N N 92  
GLN HE22 H  N N 93  
GLN HXT  H  N N 94  
GLU N    N  N N 95  
GLU CA   C  N S 96  
GLU C    C  N N 97  
GLU O    O  N N 98  
GLU CB   C  N N 99  
GLU CG   C  N N 100 
GLU CD   C  N N 101 
GLU OE1  O  N N 102 
GLU OE2  O  N N 103 
GLU OXT  O  N N 104 
GLU H    H  N N 105 
GLU H2   H  N N 106 
GLU HA   H  N N 107 
GLU HB2  H  N N 108 
GLU HB3  H  N N 109 
GLU HG2  H  N N 110 
GLU HG3  H  N N 111 
GLU HE2  H  N N 112 
GLU HXT  H  N N 113 
GLY N    N  N N 114 
GLY CA   C  N N 115 
GLY C    C  N N 116 
GLY O    O  N N 117 
GLY OXT  O  N N 118 
GLY H    H  N N 119 
GLY H2   H  N N 120 
GLY HA2  H  N N 121 
GLY HA3  H  N N 122 
GLY HXT  H  N N 123 
HIS N    N  N N 124 
HIS CA   C  N S 125 
HIS C    C  N N 126 
HIS O    O  N N 127 
HIS CB   C  N N 128 
HIS CG   C  Y N 129 
HIS ND1  N  Y N 130 
HIS CD2  C  Y N 131 
HIS CE1  C  Y N 132 
HIS NE2  N  Y N 133 
HIS OXT  O  N N 134 
HIS H    H  N N 135 
HIS H2   H  N N 136 
HIS HA   H  N N 137 
HIS HB2  H  N N 138 
HIS HB3  H  N N 139 
HIS HD1  H  N N 140 
HIS HD2  H  N N 141 
HIS HE1  H  N N 142 
HIS HE2  H  N N 143 
HIS HXT  H  N N 144 
HOH O    O  N N 145 
HOH H1   H  N N 146 
HOH H2   H  N N 147 
ILE N    N  N N 148 
ILE CA   C  N S 149 
ILE C    C  N N 150 
ILE O    O  N N 151 
ILE CB   C  N S 152 
ILE CG1  C  N N 153 
ILE CG2  C  N N 154 
ILE CD1  C  N N 155 
ILE OXT  O  N N 156 
ILE H    H  N N 157 
ILE H2   H  N N 158 
ILE HA   H  N N 159 
ILE HB   H  N N 160 
ILE HG12 H  N N 161 
ILE HG13 H  N N 162 
ILE HG21 H  N N 163 
ILE HG22 H  N N 164 
ILE HG23 H  N N 165 
ILE HD11 H  N N 166 
ILE HD12 H  N N 167 
ILE HD13 H  N N 168 
ILE HXT  H  N N 169 
LEU N    N  N N 170 
LEU CA   C  N S 171 
LEU C    C  N N 172 
LEU O    O  N N 173 
LEU CB   C  N N 174 
LEU CG   C  N N 175 
LEU CD1  C  N N 176 
LEU CD2  C  N N 177 
LEU OXT  O  N N 178 
LEU H    H  N N 179 
LEU H2   H  N N 180 
LEU HA   H  N N 181 
LEU HB2  H  N N 182 
LEU HB3  H  N N 183 
LEU HG   H  N N 184 
LEU HD11 H  N N 185 
LEU HD12 H  N N 186 
LEU HD13 H  N N 187 
LEU HD21 H  N N 188 
LEU HD22 H  N N 189 
LEU HD23 H  N N 190 
LEU HXT  H  N N 191 
LYS N    N  N N 192 
LYS CA   C  N S 193 
LYS C    C  N N 194 
LYS O    O  N N 195 
LYS CB   C  N N 196 
LYS CG   C  N N 197 
LYS CD   C  N N 198 
LYS CE   C  N N 199 
LYS NZ   N  N N 200 
LYS OXT  O  N N 201 
LYS H    H  N N 202 
LYS H2   H  N N 203 
LYS HA   H  N N 204 
LYS HB2  H  N N 205 
LYS HB3  H  N N 206 
LYS HG2  H  N N 207 
LYS HG3  H  N N 208 
LYS HD2  H  N N 209 
LYS HD3  H  N N 210 
LYS HE2  H  N N 211 
LYS HE3  H  N N 212 
LYS HZ1  H  N N 213 
LYS HZ2  H  N N 214 
LYS HZ3  H  N N 215 
LYS HXT  H  N N 216 
MET N    N  N N 217 
MET CA   C  N S 218 
MET C    C  N N 219 
MET O    O  N N 220 
MET CB   C  N N 221 
MET CG   C  N N 222 
MET SD   S  N N 223 
MET CE   C  N N 224 
MET OXT  O  N N 225 
MET H    H  N N 226 
MET H2   H  N N 227 
MET HA   H  N N 228 
MET HB2  H  N N 229 
MET HB3  H  N N 230 
MET HG2  H  N N 231 
MET HG3  H  N N 232 
MET HE1  H  N N 233 
MET HE2  H  N N 234 
MET HE3  H  N N 235 
MET HXT  H  N N 236 
PHE N    N  N N 237 
PHE CA   C  N S 238 
PHE C    C  N N 239 
PHE O    O  N N 240 
PHE CB   C  N N 241 
PHE CG   C  Y N 242 
PHE CD1  C  Y N 243 
PHE CD2  C  Y N 244 
PHE CE1  C  Y N 245 
PHE CE2  C  Y N 246 
PHE CZ   C  Y N 247 
PHE OXT  O  N N 248 
PHE H    H  N N 249 
PHE H2   H  N N 250 
PHE HA   H  N N 251 
PHE HB2  H  N N 252 
PHE HB3  H  N N 253 
PHE HD1  H  N N 254 
PHE HD2  H  N N 255 
PHE HE1  H  N N 256 
PHE HE2  H  N N 257 
PHE HZ   H  N N 258 
PHE HXT  H  N N 259 
PRO N    N  N N 260 
PRO CA   C  N S 261 
PRO C    C  N N 262 
PRO O    O  N N 263 
PRO CB   C  N N 264 
PRO CG   C  N N 265 
PRO CD   C  N N 266 
PRO OXT  O  N N 267 
PRO H    H  N N 268 
PRO HA   H  N N 269 
PRO HB2  H  N N 270 
PRO HB3  H  N N 271 
PRO HG2  H  N N 272 
PRO HG3  H  N N 273 
PRO HD2  H  N N 274 
PRO HD3  H  N N 275 
PRO HXT  H  N N 276 
SER N    N  N N 277 
SER CA   C  N S 278 
SER C    C  N N 279 
SER O    O  N N 280 
SER CB   C  N N 281 
SER OG   O  N N 282 
SER OXT  O  N N 283 
SER H    H  N N 284 
SER H2   H  N N 285 
SER HA   H  N N 286 
SER HB2  H  N N 287 
SER HB3  H  N N 288 
SER HG   H  N N 289 
SER HXT  H  N N 290 
THR N    N  N N 291 
THR CA   C  N S 292 
THR C    C  N N 293 
THR O    O  N N 294 
THR CB   C  N R 295 
THR OG1  O  N N 296 
THR CG2  C  N N 297 
THR OXT  O  N N 298 
THR H    H  N N 299 
THR H2   H  N N 300 
THR HA   H  N N 301 
THR HB   H  N N 302 
THR HG1  H  N N 303 
THR HG21 H  N N 304 
THR HG22 H  N N 305 
THR HG23 H  N N 306 
THR HXT  H  N N 307 
TYR N    N  N N 308 
TYR CA   C  N S 309 
TYR C    C  N N 310 
TYR O    O  N N 311 
TYR CB   C  N N 312 
TYR CG   C  Y N 313 
TYR CD1  C  Y N 314 
TYR CD2  C  Y N 315 
TYR CE1  C  Y N 316 
TYR CE2  C  Y N 317 
TYR CZ   C  Y N 318 
TYR OH   O  N N 319 
TYR OXT  O  N N 320 
TYR H    H  N N 321 
TYR H2   H  N N 322 
TYR HA   H  N N 323 
TYR HB2  H  N N 324 
TYR HB3  H  N N 325 
TYR HD1  H  N N 326 
TYR HD2  H  N N 327 
TYR HE1  H  N N 328 
TYR HE2  H  N N 329 
TYR HH   H  N N 330 
TYR HXT  H  N N 331 
VAL N    N  N N 332 
VAL CA   C  N S 333 
VAL C    C  N N 334 
VAL O    O  N N 335 
VAL CB   C  N N 336 
VAL CG1  C  N N 337 
VAL CG2  C  N N 338 
VAL OXT  O  N N 339 
VAL H    H  N N 340 
VAL H2   H  N N 341 
VAL HA   H  N N 342 
VAL HB   H  N N 343 
VAL HG11 H  N N 344 
VAL HG12 H  N N 345 
VAL HG13 H  N N 346 
VAL HG21 H  N N 347 
VAL HG22 H  N N 348 
VAL HG23 H  N N 349 
VAL HXT  H  N N 350 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TYR N   CA   sing N N 293 
TYR N   H    sing N N 294 
TYR N   H2   sing N N 295 
TYR CA  C    sing N N 296 
TYR CA  CB   sing N N 297 
TYR CA  HA   sing N N 298 
TYR C   O    doub N N 299 
TYR C   OXT  sing N N 300 
TYR CB  CG   sing N N 301 
TYR CB  HB2  sing N N 302 
TYR CB  HB3  sing N N 303 
TYR CG  CD1  doub Y N 304 
TYR CG  CD2  sing Y N 305 
TYR CD1 CE1  sing Y N 306 
TYR CD1 HD1  sing N N 307 
TYR CD2 CE2  doub Y N 308 
TYR CD2 HD2  sing N N 309 
TYR CE1 CZ   doub Y N 310 
TYR CE1 HE1  sing N N 311 
TYR CE2 CZ   sing Y N 312 
TYR CE2 HE2  sing N N 313 
TYR CZ  OH   sing N N 314 
TYR OH  HH   sing N N 315 
TYR OXT HXT  sing N N 316 
VAL N   CA   sing N N 317 
VAL N   H    sing N N 318 
VAL N   H2   sing N N 319 
VAL CA  C    sing N N 320 
VAL CA  CB   sing N N 321 
VAL CA  HA   sing N N 322 
VAL C   O    doub N N 323 
VAL C   OXT  sing N N 324 
VAL CB  CG1  sing N N 325 
VAL CB  CG2  sing N N 326 
VAL CB  HB   sing N N 327 
VAL CG1 HG11 sing N N 328 
VAL CG1 HG12 sing N N 329 
VAL CG1 HG13 sing N N 330 
VAL CG2 HG21 sing N N 331 
VAL CG2 HG22 sing N N 332 
VAL CG2 HG23 sing N N 333 
VAL OXT HXT  sing N N 334 
# 
_pdbx_audit_support.funding_organization   'Science and Engineering Research Board (SERB)' 
_pdbx_audit_support.country                India 
_pdbx_audit_support.grant_number           ECR/2018/002219 
_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   6W4L 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8ZVY 
_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]   0.016392 
_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]   0.014654 
_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]   0.009749 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? ?       ?       ? ? ?        ?        ? ? ?   ? ? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LYS A 1 3   ? -14.35819 13.55540  16.42923  1.000 84.45271  ? 35   LYS A N   1 
ATOM   2    C  CA  . LYS A 1 3   ? -14.29257 14.98836  16.70238  1.000 94.84277  ? 35   LYS A CA  1 
ATOM   3    C  C   . LYS A 1 3   ? -12.92718 15.35785  17.27633  1.000 92.62203  ? 35   LYS A C   1 
ATOM   4    O  O   . LYS A 1 3   ? -12.50683 16.51658  17.22821  1.000 90.28709  ? 35   LYS A O   1 
ATOM   5    C  CB  . LYS A 1 3   ? -15.41115 15.40268  17.66402  1.000 97.88969  ? 35   LYS A CB  1 
ATOM   6    C  CG  . LYS A 1 3   ? -15.47045 16.89419  17.96441  1.000 97.64639  ? 35   LYS A CG  1 
ATOM   7    C  CD  . LYS A 1 3   ? -16.62678 17.22588  18.89109  1.000 95.93535  ? 35   LYS A CD  1 
ATOM   8    C  CE  . LYS A 1 3   ? -16.57805 16.38322  20.15460  1.000 101.17192 ? 35   LYS A CE  1 
ATOM   9    N  NZ  . LYS A 1 3   ? -17.67607 16.73368  21.09798  1.000 104.20457 ? 35   LYS A NZ  1 
ATOM   10   N  N   . GLU A 1 4   ? -12.24098 14.35308  17.81470  1.000 85.23336  ? 36   GLU A N   1 
ATOM   11   C  CA  A GLU A 1 4   ? -10.92735 14.57498  18.40014  0.518 79.18219  ? 36   GLU A CA  1 
ATOM   12   C  CA  B GLU A 1 4   ? -10.92031 14.55627  18.39600  0.482 79.18490  ? 36   GLU A CA  1 
ATOM   13   C  C   . GLU A 1 4   ? -9.92612  14.96766  17.31969  1.000 76.50665  ? 36   GLU A C   1 
ATOM   14   O  O   . GLU A 1 4   ? -9.96672  14.46123  16.19498  1.000 73.79850  ? 36   GLU A O   1 
ATOM   15   C  CB  A GLU A 1 4   ? -10.46107 13.31768  19.13431  0.518 74.44492  ? 36   GLU A CB  1 
ATOM   16   C  CB  B GLU A 1 4   ? -10.44464 13.27473  19.07782  0.482 74.44992  ? 36   GLU A CB  1 
ATOM   17   C  CG  A GLU A 1 4   ? -11.56440 12.28429  19.36973  0.518 74.72305  ? 36   GLU A CG  1 
ATOM   18   C  CG  B GLU A 1 4   ? -9.11268  13.39766  19.79088  0.482 72.19893  ? 36   GLU A CG  1 
ATOM   19   C  CD  A GLU A 1 4   ? -12.63351 12.75226  20.34801  0.518 75.23883  ? 36   GLU A CD  1 
ATOM   20   C  CD  B GLU A 1 4   ? -9.23526  14.12425  21.11040  0.482 75.76975  ? 36   GLU A CD  1 
ATOM   21   O  OE1 A GLU A 1 4   ? -12.36959 13.69560  21.12537  0.518 76.99367  ? 36   GLU A OE1 1 
ATOM   22   O  OE1 B GLU A 1 4   ? -9.39966  15.36261  21.10185  0.482 78.53441  ? 36   GLU A OE1 1 
ATOM   23   O  OE2 A GLU A 1 4   ? -13.74107 12.17223  20.33541  0.518 73.62685  ? 36   GLU A OE2 1 
ATOM   24   O  OE2 B GLU A 1 4   ? -9.18653  13.44991  22.15860  0.482 76.50370  ? 36   GLU A OE2 1 
ATOM   25   N  N   . SER A 1 5   ? -9.02071  15.88325  17.66286  1.000 66.26413  ? 37   SER A N   1 
ATOM   26   C  CA  . SER A 1 5   ? -8.05986  16.38916  16.69221  1.000 59.32906  ? 37   SER A CA  1 
ATOM   27   C  C   . SER A 1 5   ? -6.70855  15.70310  16.85905  1.000 60.73319  ? 37   SER A C   1 
ATOM   28   O  O   . SER A 1 5   ? -6.04433  15.85171  17.89107  1.000 57.46447  ? 37   SER A O   1 
ATOM   29   C  CB  . SER A 1 5   ? -7.89870  17.90105  16.81468  1.000 64.10086  ? 37   SER A CB  1 
ATOM   30   O  OG  . SER A 1 5   ? -6.94010  18.36121  15.87922  1.000 67.18477  ? 37   SER A OG  1 
ATOM   31   N  N   . TYR A 1 6   ? -6.29936  14.97735  15.82424  1.000 50.93421  ? 38   TYR A N   1 
ATOM   32   C  CA  . TYR A 1 6   ? -4.95950  14.43532  15.69851  1.000 46.48533  ? 38   TYR A CA  1 
ATOM   33   C  C   . TYR A 1 6   ? -4.08634  15.30777  14.81557  1.000 47.22327  ? 38   TYR A C   1 
ATOM   34   O  O   . TYR A 1 6   ? -3.00760  14.87267  14.40506  1.000 49.81124  ? 38   TYR A O   1 
ATOM   35   C  CB  . TYR A 1 6   ? -5.01519  13.02046  15.12040  1.000 44.86842  ? 38   TYR A CB  1 
ATOM   36   C  CG  . TYR A 1 6   ? -5.79259  12.02453  15.94747  1.000 45.54542  ? 38   TYR A CG  1 
ATOM   37   C  CD1 . TYR A 1 6   ? -7.15835  11.85058  15.76888  1.000 48.19817  ? 38   TYR A CD1 1 
ATOM   38   C  CD2 . TYR A 1 6   ? -5.15215  11.24183  16.89463  1.000 45.74994  ? 38   TYR A CD2 1 
ATOM   39   C  CE1 . TYR A 1 6   ? -7.86317  10.92706  16.52293  1.000 51.66745  ? 38   TYR A CE1 1 
ATOM   40   C  CE2 . TYR A 1 6   ? -5.84721  10.32006  17.64577  1.000 47.42030  ? 38   TYR A CE2 1 
ATOM   41   C  CZ  . TYR A 1 6   ? -7.19610  10.16705  17.46038  1.000 47.98210  ? 38   TYR A CZ  1 
ATOM   42   O  OH  . TYR A 1 6   ? -7.87109  9.24114   18.22174  1.000 52.62615  ? 38   TYR A OH  1 
ATOM   43   N  N   . ALA A 1 7   ? -4.54011  16.52482  14.50254  1.000 48.27170  ? 39   ALA A N   1 
ATOM   44   C  CA  . ALA A 1 7   ? -3.89140  17.31319  13.46236  1.000 50.93425  ? 39   ALA A CA  1 
ATOM   45   C  C   . ALA A 1 7   ? -2.42561  17.55537  13.78874  1.000 51.75739  ? 39   ALA A C   1 
ATOM   46   O  O   . ALA A 1 7   ? -1.56272  17.44060  12.91148  1.000 51.56378  ? 39   ALA A O   1 
ATOM   47   C  CB  . ALA A 1 7   ? -4.62532  18.64281  13.27129  1.000 54.07262  ? 39   ALA A CB  1 
ATOM   48   N  N   . ILE A 1 8   ? -2.12565  17.87663  15.05271  1.000 54.60775  ? 40   ILE A N   1 
ATOM   49   C  CA  . ILE A 1 8   ? -0.74902  18.15343  15.45016  1.000 53.58022  ? 40   ILE A CA  1 
ATOM   50   C  C   . ILE A 1 8   ? 0.14661   16.96334  15.13706  1.000 50.66598  ? 40   ILE A C   1 
ATOM   51   O  O   . ILE A 1 8   ? 1.26965   17.12131  14.64334  1.000 51.26356  ? 40   ILE A O   1 
ATOM   52   C  CB  . ILE A 1 8   ? -0.69847  18.50822  16.94785  1.000 59.62119  ? 40   ILE A CB  1 
ATOM   53   C  CG1 . ILE A 1 8   ? -1.34592  19.87398  17.20909  1.000 60.89322  ? 40   ILE A CG1 1 
ATOM   54   C  CG2 . ILE A 1 8   ? 0.73139   18.45552  17.46687  1.000 64.71123  ? 40   ILE A CG2 1 
ATOM   55   C  CD1 . ILE A 1 8   ? -0.77922  21.01435  16.39531  1.000 74.61184  ? 40   ILE A CD1 1 
ATOM   56   N  N   . TYR A 1 9   ? -0.34396  15.75320  15.40355  1.000 50.90828  ? 41   TYR A N   1 
ATOM   57   C  CA  . TYR A 1 9   ? 0.44276   14.54375  15.20010  1.000 51.89062  ? 41   TYR A CA  1 
ATOM   58   C  C   . TYR A 1 9   ? 0.50443   14.12696  13.73658  1.000 49.92914  ? 41   TYR A C   1 
ATOM   59   O  O   . TYR A 1 9   ? 1.53042   13.59687  13.29531  1.000 49.30700  ? 41   TYR A O   1 
ATOM   60   C  CB  . TYR A 1 9   ? -0.12809  13.43743  16.08455  1.000 45.49487  ? 41   TYR A CB  1 
ATOM   61   C  CG  . TYR A 1 9   ? -0.41149  13.97918  17.47133  1.000 51.50870  ? 41   TYR A CG  1 
ATOM   62   C  CD1 . TYR A 1 9   ? 0.62902   14.36069  18.30366  1.000 46.18629  ? 41   TYR A CD1 1 
ATOM   63   C  CD2 . TYR A 1 9   ? -1.71103  14.18694  17.91186  1.000 47.98723  ? 41   TYR A CD2 1 
ATOM   64   C  CE1 . TYR A 1 9   ? 0.38628   14.88411  19.56132  1.000 51.77103  ? 41   TYR A CE1 1 
ATOM   65   C  CE2 . TYR A 1 9   ? -1.96709  14.71485  19.16524  1.000 51.69489  ? 41   TYR A CE2 1 
ATOM   66   C  CZ  . TYR A 1 9   ? -0.91385  15.05655  19.98836  1.000 55.34477  ? 41   TYR A CZ  1 
ATOM   67   O  OH  . TYR A 1 9   ? -1.15809  15.58457  21.23974  1.000 57.01078  ? 41   TYR A OH  1 
ATOM   68   N  N   . VAL A 1 10  ? -0.57257  14.34576  12.97848  1.000 48.45246  ? 42   VAL A N   1 
ATOM   69   C  CA  . VAL A 1 10  ? -0.51507  14.14677  11.53312  1.000 47.88183  ? 42   VAL A CA  1 
ATOM   70   C  C   . VAL A 1 10  ? 0.58763   14.99747  10.92442  1.000 48.24218  ? 42   VAL A C   1 
ATOM   71   O  O   . VAL A 1 10  ? 1.36633   14.52297  10.08995  1.000 49.41608  ? 42   VAL A O   1 
ATOM   72   C  CB  . VAL A 1 10  ? -1.88226  14.45539  10.89695  1.000 47.31174  ? 42   VAL A CB  1 
ATOM   73   C  CG1 . VAL A 1 10  ? -1.80375  14.38768  9.37514   1.000 46.30043  ? 42   VAL A CG1 1 
ATOM   74   C  CG2 . VAL A 1 10  ? -2.93123  13.49588  11.41638  1.000 44.07448  ? 42   VAL A CG2 1 
ATOM   75   N  N   . TYR A 1 11  ? 0.67954   16.26948  11.33631  1.000 48.88669  ? 43   TYR A N   1 
ATOM   76   C  CA  . TYR A 1 11  ? 1.73019   17.14150  10.82213  1.000 49.60133  ? 43   TYR A CA  1 
ATOM   77   C  C   . TYR A 1 11  ? 3.11776   16.62812  11.17852  1.000 53.51747  ? 43   TYR A C   1 
ATOM   78   O  O   . TYR A 1 11  ? 4.02424   16.65021  10.33933  1.000 51.59535  ? 43   TYR A O   1 
ATOM   79   C  CB  . TYR A 1 11  ? 1.54442   18.56497  11.34885  1.000 53.51621  ? 43   TYR A CB  1 
ATOM   80   C  CG  . TYR A 1 11  ? 2.28372   19.59958  10.53015  1.000 56.52076  ? 43   TYR A CG  1 
ATOM   81   C  CD1 . TYR A 1 11  ? 1.80385   20.03185  9.30182   1.000 59.12175  ? 43   TYR A CD1 1 
ATOM   82   C  CD2 . TYR A 1 11  ? 3.48778   20.11808  10.98400  1.000 59.62290  ? 43   TYR A CD2 1 
ATOM   83   C  CE1 . TYR A 1 11  ? 2.49876   20.96639  8.56009   1.000 64.58303  ? 43   TYR A CE1 1 
ATOM   84   C  CE2 . TYR A 1 11  ? 4.18623   21.05388  10.25142  1.000 58.76488  ? 43   TYR A CE2 1 
ATOM   85   C  CZ  . TYR A 1 11  ? 3.68726   21.47122  9.04065   1.000 65.81117  ? 43   TYR A CZ  1 
ATOM   86   O  OH  . TYR A 1 11  ? 4.37489   22.40181  8.29980   1.000 70.32820  ? 43   TYR A OH  1 
ATOM   87   N  N   . LYS A 1 12  ? 3.30283   16.15477  12.41454  1.000 49.35635  ? 44   LYS A N   1 
ATOM   88   C  CA  . LYS A 1 12  ? 4.61034   15.64953  12.81622  1.000 52.78948  ? 44   LYS A CA  1 
ATOM   89   C  C   . LYS A 1 12  ? 5.02006   14.48740  11.92042  1.000 50.25950  ? 44   LYS A C   1 
ATOM   90   O  O   . LYS A 1 12  ? 6.16620   14.41018  11.46269  1.000 50.92570  ? 44   LYS A O   1 
ATOM   91   C  CB  . LYS A 1 12  ? 4.57103   15.21873  14.28765  1.000 50.33834  ? 44   LYS A CB  1 
ATOM   92   C  CG  . LYS A 1 12  ? 4.21828   16.36477  15.24131  1.000 63.37852  ? 44   LYS A CG  1 
ATOM   93   C  CD  . LYS A 1 12  ? 4.92692   16.36190  16.58570  1.000 66.18688  ? 44   LYS A CD  1 
ATOM   94   C  CE  . LYS A 1 12  ? 4.67340   17.71461  17.23860  1.000 65.14102  ? 44   LYS A CE  1 
ATOM   95   N  NZ  . LYS A 1 12  ? 5.65791   18.75755  16.83079  1.000 78.98899  ? 44   LYS A NZ  1 
ATOM   96   N  N   . VAL A 1 13  ? 4.08231   13.57867  11.64550  1.000 52.40230  ? 45   VAL A N   1 
ATOM   97   C  CA  . VAL A 1 13  ? 4.35937   12.47052  10.73678  1.000 47.56074  ? 45   VAL A CA  1 
ATOM   98   C  C   . VAL A 1 13  ? 4.64844   12.98575  9.33138   1.000 48.13916  ? 45   VAL A C   1 
ATOM   99   O  O   . VAL A 1 13  ? 5.54444   12.48271  8.64149   1.000 52.56473  ? 45   VAL A O   1 
ATOM   100  C  CB  . VAL A 1 13  ? 3.18651   11.47480  10.75020  1.000 45.08851  ? 45   VAL A CB  1 
ATOM   101  C  CG1 . VAL A 1 13  ? 3.38292   10.40302  9.68993   1.000 45.38114  ? 45   VAL A CG1 1 
ATOM   102  C  CG2 . VAL A 1 13  ? 3.04414   10.86225  12.13667  1.000 45.22275  ? 45   VAL A CG2 1 
ATOM   103  N  N   . LEU A 1 14  ? 3.89686   13.99413  8.88114   1.000 48.51972  ? 46   LEU A N   1 
ATOM   104  C  CA  . LEU A 1 14  ? 4.12425   14.52614  7.54043   1.000 50.32669  ? 46   LEU A CA  1 
ATOM   105  C  C   . LEU A 1 14  ? 5.55721   15.01209  7.37338   1.000 54.62205  ? 46   LEU A C   1 
ATOM   106  O  O   . LEU A 1 14  ? 6.17136   14.80457  6.32135   1.000 60.75420  ? 46   LEU A O   1 
ATOM   107  C  CB  . LEU A 1 14  ? 3.14009   15.65830  7.23761   1.000 54.74589  ? 46   LEU A CB  1 
ATOM   108  C  CG  . LEU A 1 14  ? 3.37499   16.39188  5.90654   1.000 54.08058  ? 46   LEU A CG  1 
ATOM   109  C  CD1 . LEU A 1 14  ? 3.32954   15.42155  4.73190   1.000 57.45361  ? 46   LEU A CD1 1 
ATOM   110  C  CD2 . LEU A 1 14  ? 2.37149   17.52446  5.69876   1.000 54.40761  ? 46   LEU A CD2 1 
ATOM   111  N  N   . LYS A 1 15  ? 6.11471   15.65033  8.40083   1.000 57.58853  ? 47   LYS A N   1 
ATOM   112  C  CA  . LYS A 1 15  ? 7.47373   16.15948  8.27255   1.000 60.20682  ? 47   LYS A CA  1 
ATOM   113  C  C   . LYS A 1 15  ? 8.50947   15.04717  8.28956   1.000 60.99304  ? 47   LYS A C   1 
ATOM   114  O  O   . LYS A 1 15  ? 9.62835   15.25836  7.81206   1.000 65.77773  ? 47   LYS A O   1 
ATOM   115  C  CB  . LYS A 1 15  ? 7.75210   17.19647  9.35713   1.000 58.19975  ? 47   LYS A CB  1 
ATOM   116  C  CG  . LYS A 1 15  ? 7.04998   18.51464  9.07818   1.000 68.13318  ? 47   LYS A CG  1 
ATOM   117  C  CD  . LYS A 1 15  ? 6.77968   18.65341  7.57312   1.000 67.12902  ? 47   LYS A CD  1 
ATOM   118  C  CE  . LYS A 1 15  ? 6.31248   20.03152  7.17844   1.000 72.89104  ? 47   LYS A CE  1 
ATOM   119  N  NZ  . LYS A 1 15  ? 6.61020   20.26983  5.74163   1.000 77.29721  ? 47   LYS A NZ  1 
ATOM   120  N  N   . GLN A 1 16  ? 8.16624   13.87021  8.82321   1.000 60.61223  ? 48   GLN A N   1 
ATOM   121  C  CA  . GLN A 1 16  ? 9.08031   12.73731  8.73927   1.000 59.02425  ? 48   GLN A CA  1 
ATOM   122  C  C   . GLN A 1 16  ? 9.13194   12.17750  7.32358   1.000 59.60186  ? 48   GLN A C   1 
ATOM   123  O  O   . GLN A 1 16  ? 10.21622  11.92072  6.79286   1.000 66.06082  ? 48   GLN A O   1 
ATOM   124  C  CB  . GLN A 1 16  ? 8.66762   11.64238  9.72088   1.000 62.08373  ? 48   GLN A CB  1 
ATOM   125  C  CG  . GLN A 1 16  ? 8.85568   11.97790  11.18778  1.000 60.93570  ? 48   GLN A CG  1 
ATOM   126  C  CD  . GLN A 1 16  ? 8.34353   10.86830  12.09008  1.000 65.01344  ? 48   GLN A CD  1 
ATOM   127  O  OE1 . GLN A 1 16  ? 7.42716   10.12903  11.72702  1.000 60.60517  ? 48   GLN A OE1 1 
ATOM   128  N  NE2 . GLN A 1 16  ? 8.93731   10.74586  13.27277  1.000 69.47643  ? 48   GLN A NE2 1 
ATOM   129  N  N   . VAL A 1 17  ? 7.97341   11.98866  6.68928   1.000 61.15735  ? 49   VAL A N   1 
ATOM   130  C  CA  . VAL A 1 17  ? 7.94787   11.31109  5.39311   1.000 59.40326  ? 49   VAL A CA  1 
ATOM   131  C  C   . VAL A 1 17  ? 8.18484   12.27593  4.23648   1.000 61.19414  ? 49   VAL A C   1 
ATOM   132  O  O   . VAL A 1 17  ? 8.71218   11.87089  3.19659   1.000 61.48732  ? 49   VAL A O   1 
ATOM   133  C  CB  . VAL A 1 17  ? 6.63157   10.53298  5.18325   1.000 57.76921  ? 49   VAL A CB  1 
ATOM   134  C  CG1 . VAL A 1 17  ? 6.41962   9.50659   6.29260   1.000 52.96823  ? 49   VAL A CG1 1 
ATOM   135  C  CG2 . VAL A 1 17  ? 5.43659   11.48034  5.07141   1.000 54.58016  ? 49   VAL A CG2 1 
ATOM   136  N  N   . HIS A 1 18  ? 7.81224   13.54180  4.38959   1.000 65.65880  ? 50   HIS A N   1 
ATOM   137  C  CA  . HIS A 1 18  ? 8.02295   14.55788  3.35717   1.000 63.77076  ? 50   HIS A CA  1 
ATOM   138  C  C   . HIS A 1 18  ? 8.38686   15.86956  4.03691   1.000 65.56154  ? 50   HIS A C   1 
ATOM   139  O  O   . HIS A 1 18  ? 7.54259   16.75628  4.21395   1.000 61.68147  ? 50   HIS A O   1 
ATOM   140  C  CB  . HIS A 1 18  ? 6.78117   14.70613  2.47329   1.000 64.12375  ? 50   HIS A CB  1 
ATOM   141  C  CG  . HIS A 1 18  ? 6.55621   13.55220  1.54369   1.000 64.30289  ? 50   HIS A CG  1 
ATOM   142  N  ND1 . HIS A 1 18  ? 7.37191   13.30049  0.46159   1.000 63.84013  ? 50   HIS A ND1 1 
ATOM   143  C  CD2 . HIS A 1 18  ? 5.61268   12.57887  1.53789   1.000 60.19060  ? 50   HIS A CD2 1 
ATOM   144  C  CE1 . HIS A 1 18  ? 6.93682   12.22761  -0.17539  1.000 65.90565  ? 50   HIS A CE1 1 
ATOM   145  N  NE2 . HIS A 1 18  ? 5.86828   11.77326  0.45404   1.000 58.68150  ? 50   HIS A NE2 1 
ATOM   146  N  N   . PRO A 1 19  ? 9.65924   16.03897  4.40594   1.000 69.38722  ? 51   PRO A N   1 
ATOM   147  C  CA  . PRO A 1 19  ? 10.04147  17.19043  5.24307   1.000 69.65994  ? 51   PRO A CA  1 
ATOM   148  C  C   . PRO A 1 19  ? 9.72573   18.54497  4.63391   1.000 73.70638  ? 51   PRO A C   1 
ATOM   149  O  O   . PRO A 1 19  ? 9.52802   19.51078  5.38160   1.000 74.11359  ? 51   PRO A O   1 
ATOM   150  C  CB  . PRO A 1 19  ? 11.55315  16.99585  5.42129   1.000 69.80636  ? 51   PRO A CB  1 
ATOM   151  C  CG  . PRO A 1 19  ? 11.76655  15.53469  5.24644   1.000 73.13399  ? 51   PRO A CG  1 
ATOM   152  C  CD  . PRO A 1 19  ? 10.78096  15.10862  4.19687   1.000 69.42109  ? 51   PRO A CD  1 
ATOM   153  N  N   . ASP A 1 20  ? 9.68290   18.66007  3.30703   1.000 71.22686  ? 52   ASP A N   1 
ATOM   154  C  CA  . ASP A 1 20  ? 9.48729   19.95150  2.65833   1.000 81.07500  ? 52   ASP A CA  1 
ATOM   155  C  C   . ASP A 1 20  ? 8.11127   20.08780  2.01378   1.000 78.41756  ? 52   ASP A C   1 
ATOM   156  O  O   . ASP A 1 20  ? 7.91676   20.96210  1.16387   1.000 75.48959  ? 52   ASP A O   1 
ATOM   157  C  CB  . ASP A 1 20  ? 10.57933  20.19771  1.61664   1.000 86.72066  ? 52   ASP A CB  1 
ATOM   158  C  CG  . ASP A 1 20  ? 11.96381  20.25823  2.22730   1.000 88.32438  ? 52   ASP A CG  1 
ATOM   159  O  OD1 . ASP A 1 20  ? 12.10334  20.82999  3.32876   1.000 88.10742  ? 52   ASP A OD1 1 
ATOM   160  O  OD2 . ASP A 1 20  ? 12.91187  19.73769  1.60414   1.000 95.69519  ? 52   ASP A OD2 1 
ATOM   161  N  N   . THR A 1 21  ? 7.14858   19.25817  2.40746   1.000 71.79584  ? 53   THR A N   1 
ATOM   162  C  CA  . THR A 1 21  ? 5.82000   19.26740  1.81007   1.000 71.09874  ? 53   THR A CA  1 
ATOM   163  C  C   . THR A 1 21  ? 4.79027   19.72457  2.83419   1.000 63.44932  ? 53   THR A C   1 
ATOM   164  O  O   . THR A 1 21  ? 4.71710   19.17607  3.93894   1.000 72.40778  ? 53   THR A O   1 
ATOM   165  C  CB  . THR A 1 21  ? 5.46056   17.88319  1.26167   1.000 68.86341  ? 53   THR A CB  1 
ATOM   166  O  OG1 . THR A 1 21  ? 6.38469   17.53046  0.22256   1.000 70.72289  ? 53   THR A OG1 1 
ATOM   167  C  CG2 . THR A 1 21  ? 4.04494   17.87150  0.71198   1.000 70.55308  ? 53   THR A CG2 1 
ATOM   168  N  N   . GLY A 1 22  ? 3.99085   20.72695  2.46261   1.000 71.56312  ? 54   GLY A N   1 
ATOM   169  C  CA  . GLY A 1 22  ? 2.91157   21.18398  3.30830   1.000 72.08645  ? 54   GLY A CA  1 
ATOM   170  C  C   . GLY A 1 22  ? 1.64229   20.37784  3.10573   1.000 66.30734  ? 54   GLY A C   1 
ATOM   171  O  O   . GLY A 1 22  ? 1.58609   19.42136  2.33421   1.000 63.77363  ? 54   GLY A O   1 
ATOM   172  N  N   . ILE A 1 23  ? 0.60471   20.78182  3.83162   1.000 63.51174  ? 55   ILE A N   1 
ATOM   173  C  CA  . ILE A 1 23  ? -0.72317  20.19297  3.69603   1.000 64.06876  ? 55   ILE A CA  1 
ATOM   174  C  C   . ILE A 1 23  ? -1.74766  21.28426  3.96281   1.000 71.31428  ? 55   ILE A C   1 
ATOM   175  O  O   . ILE A 1 23  ? -1.57943  22.10541  4.87008   1.000 71.35336  ? 55   ILE A O   1 
ATOM   176  C  CB  . ILE A 1 23  ? -0.92743  18.98162  4.63724   1.000 60.89630  ? 55   ILE A CB  1 
ATOM   177  C  CG1 . ILE A 1 23  ? -2.25178  18.27376  4.31733   1.000 56.92669  ? 55   ILE A CG1 1 
ATOM   178  C  CG2 . ILE A 1 23  ? -0.87448  19.40703  6.10041   1.000 62.07286  ? 55   ILE A CG2 1 
ATOM   179  C  CD1 . ILE A 1 23  ? -2.50894  17.00723  5.13337   1.000 58.52025  ? 55   ILE A CD1 1 
ATOM   180  N  N   . SER A 1 24  ? -2.78491  21.32344  3.13476   1.000 63.10603  ? 56   SER A N   1 
ATOM   181  C  CA  . SER A 1 24  ? -3.80710  22.33157  3.30568   1.000 68.21715  ? 56   SER A CA  1 
ATOM   182  C  C   . SER A 1 24  ? -4.67556  22.01745  4.51777   1.000 61.59764  ? 56   SER A C   1 
ATOM   183  O  O   . SER A 1 24  ? -4.64013  20.92121  5.08743   1.000 62.53455  ? 56   SER A O   1 
ATOM   184  C  CB  . SER A 1 24  ? -4.68549  22.42218  2.07103   1.000 78.69385  ? 56   SER A CB  1 
ATOM   185  O  OG  . SER A 1 24  ? -5.61612  21.36297  2.00688   1.000 67.66227  ? 56   SER A OG  1 
ATOM   186  N  N   . SER A 1 25  ? -5.47543  23.01135  4.89860   1.000 73.69687  ? 57   SER A N   1 
ATOM   187  C  CA  . SER A 1 25  ? -6.38195  22.86217  6.02763   1.000 68.27331  ? 57   SER A CA  1 
ATOM   188  C  C   . SER A 1 25  ? -7.46764  21.83520  5.73422   1.000 57.52337  ? 57   SER A C   1 
ATOM   189  O  O   . SER A 1 25  ? -7.81217  21.02066  6.59914   1.000 56.19362  ? 57   SER A O   1 
ATOM   190  C  CB  . SER A 1 25  ? -6.99663  24.22095  6.36520   1.000 73.70928  ? 57   SER A CB  1 
ATOM   191  O  OG  . SER A 1 25  ? -7.56450  24.21305  7.66008   1.000 82.72735  ? 57   SER A OG  1 
ATOM   192  N  N   . LYS A 1 26  ? -8.02013  21.85396  4.52080   1.000 68.39646  ? 58   LYS A N   1 
ATOM   193  C  CA  . LYS A 1 26  ? -9.08827  20.91505  4.19320   1.000 68.67414  ? 58   LYS A CA  1 
ATOM   194  C  C   . LYS A 1 26  ? -8.55958  19.49152  4.08093   1.000 64.56294  ? 58   LYS A C   1 
ATOM   195  O  O   . LYS A 1 26  ? -9.23686  18.54151  4.48922   1.000 58.72216  ? 58   LYS A O   1 
ATOM   196  C  CB  . LYS A 1 26  ? -9.77953  21.35064  2.90230   1.000 72.60670  ? 58   LYS A CB  1 
ATOM   197  C  CG  . LYS A 1 26  ? -10.53780 22.65334  3.05666   1.000 81.98999  ? 58   LYS A CG  1 
ATOM   198  C  CD  . LYS A 1 26  ? -11.56317 22.85459  1.95792   1.000 90.29496  ? 58   LYS A CD  1 
ATOM   199  C  CE  . LYS A 1 26  ? -12.07975 24.28440  1.98688   1.000 85.77583  ? 58   LYS A CE  1 
ATOM   200  N  NZ  . LYS A 1 26  ? -12.82756 24.65030  0.75790   1.000 93.67196  ? 58   LYS A NZ  1 
ATOM   201  N  N   . ALA A 1 27  ? -7.33988  19.32406  3.56219   1.000 64.01517  ? 59   ALA A N   1 
ATOM   202  C  CA  . ALA A 1 27  ? -6.73890  17.99476  3.52373   1.000 56.07244  ? 59   ALA A CA  1 
ATOM   203  C  C   . ALA A 1 27  ? -6.43146  17.48708  4.92727   1.000 54.28654  ? 59   ALA A C   1 
ATOM   204  O  O   . ALA A 1 27  ? -6.57275  16.29252  5.20238   1.000 52.03962  ? 59   ALA A O   1 
ATOM   205  C  CB  . ALA A 1 27  ? -5.47766  18.00420  2.66403   1.000 57.73079  ? 59   ALA A CB  1 
ATOM   206  N  N   . MET A 1 28  ? -6.00063  18.37062  5.82978   1.000 49.92966  ? 60   MET A N   1 
ATOM   207  C  CA  . MET A 1 28  ? -5.78127  17.93138  7.20548   1.000 52.37240  ? 60   MET A CA  1 
ATOM   208  C  C   . MET A 1 28  ? -7.08946  17.49709  7.85653   1.000 48.38746  ? 60   MET A C   1 
ATOM   209  O  O   . MET A 1 28  ? -7.10458  16.55879  8.65626   1.000 50.93105  ? 60   MET A O   1 
ATOM   210  C  CB  . MET A 1 28  ? -5.10809  19.04009  8.02019   1.000 54.14665  ? 60   MET A CB  1 
ATOM   211  C  CG  . MET A 1 28  ? -4.96398  18.69022  9.48597   1.000 55.58294  ? 60   MET A CG  1 
ATOM   212  S  SD  . MET A 1 28  ? -3.75741  17.36189  9.73193   1.000 52.69719  ? 60   MET A SD  1 
ATOM   213  C  CE  . MET A 1 28  ? -2.23656  18.22291  9.33106   1.000 56.85858  ? 60   MET A CE  1 
ATOM   214  N  N   . SER A 1 29  ? -8.20329  18.15753  7.52640   1.000 55.71270  ? 61   SER A N   1 
ATOM   215  C  CA  . SER A 1 29  ? -9.48732  17.73745  8.08948   1.000 55.35479  ? 61   SER A CA  1 
ATOM   216  C  C   . SER A 1 29  ? -9.86231  16.33214  7.63322   1.000 53.63760  ? 61   SER A C   1 
ATOM   217  O  O   . SER A 1 29  ? -10.41462 15.54274  8.41127   1.000 54.63859  ? 61   SER A O   1 
ATOM   218  C  CB  . SER A 1 29  ? -10.58211 18.73183  7.71366   1.000 58.11215  ? 61   SER A CB  1 
ATOM   219  O  OG  . SER A 1 29  ? -10.41614 19.96195  8.40268   1.000 64.26040  ? 61   SER A OG  1 
ATOM   220  N  N   . ILE A 1 30  ? -9.57819  16.00912  6.37018   1.000 50.61041  ? 62   ILE A N   1 
ATOM   221  C  CA  . ILE A 1 30  ? -9.80907  14.65960  5.85947   1.000 51.72556  ? 62   ILE A CA  1 
ATOM   222  C  C   . ILE A 1 30  ? -8.88923  13.65151  6.53779   1.000 45.09398  ? 62   ILE A C   1 
ATOM   223  O  O   . ILE A 1 30  ? -9.30617  12.52836  6.86299   1.000 47.35488  ? 62   ILE A O   1 
ATOM   224  C  CB  . ILE A 1 30  ? -9.63716  14.65686  4.33169   1.000 52.59216  ? 62   ILE A CB  1 
ATOM   225  C  CG1 . ILE A 1 30  ? -10.74026 15.51177  3.70677   1.000 53.64411  ? 62   ILE A CG1 1 
ATOM   226  C  CG2 . ILE A 1 30  ? -9.53277  13.22574  3.76548   1.000 49.45641  ? 62   ILE A CG2 1 
ATOM   227  C  CD1 . ILE A 1 30  ? -10.63139 15.67097  2.22088   1.000 59.38859  ? 62   ILE A CD1 1 
ATOM   228  N  N   . MET A 1 31  ? -7.61832  14.01882  6.73606   1.000 45.63225  ? 63   MET A N   1 
ATOM   229  C  CA  . MET A 1 31  ? -6.70580  13.14113  7.46849   1.000 43.24285  ? 63   MET A CA  1 
ATOM   230  C  C   . MET A 1 31  ? -7.22825  12.87120  8.86791   1.000 44.20346  ? 63   MET A C   1 
ATOM   231  O  O   . MET A 1 31  ? -7.19713  11.73055  9.34711   1.000 43.81437  ? 63   MET A O   1 
ATOM   232  C  CB  . MET A 1 31  ? -5.31367  13.76635  7.56867   1.000 47.92851  ? 63   MET A CB  1 
ATOM   233  C  CG  . MET A 1 31  ? -4.37107  13.56777  6.38838   1.000 48.18682  ? 63   MET A CG  1 
ATOM   234  S  SD  . MET A 1 31  ? -4.50016  11.94449  5.66468   1.000 51.19599  ? 63   MET A SD  1 
ATOM   235  C  CE  . MET A 1 31  ? -3.51364  10.98745  6.82653   1.000 43.67595  ? 63   MET A CE  1 
ATOM   236  N  N   . ASN A 1 32  ? -7.69959  13.92030  9.54704   1.000 46.88686  ? 64   ASN A N   1 
ATOM   237  C  CA  . ASN A 1 32  ? -8.19017  13.75129  10.90903  1.000 48.51963  ? 64   ASN A CA  1 
ATOM   238  C  C   . ASN A 1 32  ? -9.40640  12.83753  10.94418  1.000 44.20599  ? 64   ASN A C   1 
ATOM   239  O  O   . ASN A 1 32  ? -9.54525  12.01009  11.84987  1.000 43.15312  ? 64   ASN A O   1 
ATOM   240  C  CB  . ASN A 1 32  ? -8.52000  15.11155  11.52547  1.000 47.08936  ? 64   ASN A CB  1 
ATOM   241  C  CG  . ASN A 1 32  ? -8.90464  15.00238  12.98935  1.000 56.59268  ? 64   ASN A CG  1 
ATOM   242  O  OD1 . ASN A 1 32  ? -8.07563  14.65844  13.82862  1.000 53.50346  ? 64   ASN A OD1 1 
ATOM   243  N  ND2 . ASN A 1 32  ? -10.16538 15.29493  13.30254  1.000 54.72803  ? 64   ASN A ND2 1 
ATOM   244  N  N   . SER A 1 33  ? -10.31144 12.98562  9.97650   1.000 50.44013  ? 65   SER A N   1 
ATOM   245  C  CA  A SER A 1 33  ? -11.49258 12.13201  9.94980   0.691 50.10785  ? 65   SER A CA  1 
ATOM   246  C  CA  B SER A 1 33  ? -11.49551 12.13368  9.94306   0.309 50.05136  ? 65   SER A CA  1 
ATOM   247  C  C   . SER A 1 33  ? -11.11767 10.68387  9.68166   1.000 46.10544  ? 65   SER A C   1 
ATOM   248  O  O   . SER A 1 33  ? -11.72167 9.76547   10.24669  1.000 46.93503  ? 65   SER A O   1 
ATOM   249  C  CB  A SER A 1 33  ? -12.48402 12.64264  8.90767   0.691 50.59192  ? 65   SER A CB  1 
ATOM   250  C  CB  B SER A 1 33  ? -12.48448 12.63389  8.88876   0.309 50.61518  ? 65   SER A CB  1 
ATOM   251  O  OG  A SER A 1 33  ? -12.84285 13.98124  9.19345   0.691 51.23262  ? 65   SER A OG  1 
ATOM   252  O  OG  B SER A 1 33  ? -11.99199 12.43209  7.57563   0.309 52.06065  ? 65   SER A OG  1 
ATOM   253  N  N   . PHE A 1 34  ? -10.12736 10.45239  8.82263   1.000 44.14981  ? 66   PHE A N   1 
ATOM   254  C  CA  . PHE A 1 34  ? -9.69752  9.07910   8.60248   1.000 43.55654  ? 66   PHE A CA  1 
ATOM   255  C  C   . PHE A 1 34  ? -9.15815  8.45758   9.88682   1.000 39.55536  ? 66   PHE A C   1 
ATOM   256  O  O   . PHE A 1 34  ? -9.47734  7.30631   10.20248  1.000 40.94815  ? 66   PHE A O   1 
ATOM   257  C  CB  . PHE A 1 34  ? -8.65216  9.00069   7.49873   1.000 44.08419  ? 66   PHE A CB  1 
ATOM   258  C  CG  . PHE A 1 34  ? -8.17800  7.61082   7.25879   1.000 49.97548  ? 66   PHE A CG  1 
ATOM   259  C  CD1 . PHE A 1 34  ? -8.95505  6.71957   6.52863   1.000 53.06013  ? 66   PHE A CD1 1 
ATOM   260  C  CD2 . PHE A 1 34  ? -6.98666  7.16727   7.80472   1.000 51.46885  ? 66   PHE A CD2 1 
ATOM   261  C  CE1 . PHE A 1 34  ? -8.53601  5.41663   6.31937   1.000 46.60014  ? 66   PHE A CE1 1 
ATOM   262  C  CE2 . PHE A 1 34  ? -6.57057  5.86638   7.60885   1.000 47.78171  ? 66   PHE A CE2 1 
ATOM   263  C  CZ  . PHE A 1 34  ? -7.34383  4.99796   6.84781   1.000 53.38631  ? 66   PHE A CZ  1 
ATOM   264  N  N   . VAL A 1 35  ? -8.32392  9.19140   10.63027  1.000 38.28731  ? 67   VAL A N   1 
ATOM   265  C  CA  . VAL A 1 35  ? -7.76733  8.64338   11.86645  1.000 37.73430  ? 67   VAL A CA  1 
ATOM   266  C  C   . VAL A 1 35  ? -8.88065  8.30737   12.84822  1.000 35.29587  ? 67   VAL A C   1 
ATOM   267  O  O   . VAL A 1 35  ? -8.85796  7.24890   13.49077  1.000 36.95564  ? 67   VAL A O   1 
ATOM   268  C  CB  . VAL A 1 35  ? -6.74645  9.61171   12.49511  1.000 40.10026  ? 67   VAL A CB  1 
ATOM   269  C  CG1 . VAL A 1 35  ? -6.24011  9.03938   13.80881  1.000 39.07976  ? 67   VAL A CG1 1 
ATOM   270  C  CG2 . VAL A 1 35  ? -5.58977  9.83688   11.55871  1.000 38.89407  ? 67   VAL A CG2 1 
ATOM   271  N  N   . ASN A 1 36  ? -9.86091  9.20547   12.99614  1.000 38.00155  ? 68   ASN A N   1 
ATOM   272  C  CA  . ASN A 1 36  ? -10.98362 8.93403   13.88980  1.000 38.26737  ? 68   ASN A CA  1 
ATOM   273  C  C   . ASN A 1 36  ? -11.79268 7.73409   13.41532  1.000 37.91666  ? 68   ASN A C   1 
ATOM   274  O  O   . ASN A 1 36  ? -12.24706 6.92619   14.22987  1.000 38.44652  ? 68   ASN A O   1 
ATOM   275  C  CB  . ASN A 1 36  ? -11.89260 10.15800  14.00855  1.000 37.12231  ? 68   ASN A CB  1 
ATOM   276  C  CG  . ASN A 1 36  ? -11.36036 11.19766  14.98005  1.000 50.18009  ? 68   ASN A CG  1 
ATOM   277  O  OD1 . ASN A 1 36  ? -11.50612 11.05808  16.18975  1.000 55.55800  ? 68   ASN A OD1 1 
ATOM   278  N  ND2 . ASN A 1 36  ? -10.76645 12.26378  14.44921  1.000 57.65397  ? 68   ASN A ND2 1 
ATOM   279  N  N   . ASP A 1 37  ? -12.01144 7.61978   12.10311  1.000 38.13823  ? 69   ASP A N   1 
ATOM   280  C  CA  . ASP A 1 37  ? -12.77944 6.49511   11.57648  1.000 39.31655  ? 69   ASP A CA  1 
ATOM   281  C  C   . ASP A 1 37  ? -12.07247 5.16980   11.84279  1.000 36.36810  ? 69   ASP A C   1 
ATOM   282  O  O   . ASP A 1 37  ? -12.71507 4.18482   12.22504  1.000 33.17505  ? 69   ASP A O   1 
ATOM   283  C  CB  . ASP A 1 37  ? -13.02944 6.68087   10.07536  1.000 41.41775  ? 69   ASP A CB  1 
ATOM   284  C  CG  . ASP A 1 37  ? -14.03270 7.79648   9.76722   1.000 52.47457  ? 69   ASP A CG  1 
ATOM   285  O  OD1 . ASP A 1 37  ? -14.70934 8.29695   10.68911  1.000 46.61379  ? 69   ASP A OD1 1 
ATOM   286  O  OD2 . ASP A 1 37  ? -14.14492 8.19019   8.58326   1.000 55.94211  ? 69   ASP A OD2 1 
ATOM   287  N  N   . VAL A 1 38  ? -10.75426 5.11925   11.63278  1.000 32.59989  ? 70   VAL A N   1 
ATOM   288  C  CA  . VAL A 1 38  ? -10.00988 3.88793   11.90699  1.000 27.41524  ? 70   VAL A CA  1 
ATOM   289  C  C   . VAL A 1 38  ? -10.00547 3.58144   13.39520  1.000 29.74914  ? 70   VAL A C   1 
ATOM   290  O  O   . VAL A 1 38  ? -10.16249 2.42475   13.80441  1.000 30.15279  ? 70   VAL A O   1 
ATOM   291  C  CB  . VAL A 1 38  ? -8.57571  3.98745   11.37072  1.000 31.95453  ? 70   VAL A CB  1 
ATOM   292  C  CG1 . VAL A 1 38  ? -7.78565  2.72361   11.77668  1.000 32.29759  ? 70   VAL A CG1 1 
ATOM   293  C  CG2 . VAL A 1 38  ? -8.59873  4.14632   9.86232   1.000 36.48404  ? 70   VAL A CG2 1 
ATOM   294  N  N   . PHE A 1 39  ? -9.79770  4.60536   14.22333  1.000 31.22008  ? 71   PHE A N   1 
ATOM   295  C  CA  . PHE A 1 39  ? -9.85598  4.41509   15.66603  1.000 32.71793  ? 71   PHE A CA  1 
ATOM   296  C  C   . PHE A 1 39  ? -11.17517 3.76895   16.06073  1.000 30.27890  ? 71   PHE A C   1 
ATOM   297  O  O   . PHE A 1 39  ? -11.19397 2.75947   16.77387  1.000 32.28112  ? 71   PHE A O   1 
ATOM   298  C  CB  . PHE A 1 39  ? -9.69534  5.76061   16.38476  1.000 31.67345  ? 71   PHE A CB  1 
ATOM   299  C  CG  . PHE A 1 39  ? -9.89294  5.67275   17.87443  1.000 34.35761  ? 71   PHE A CG  1 
ATOM   300  C  CD1 . PHE A 1 39  ? -11.17118 5.65319   18.42882  1.000 38.21748  ? 71   PHE A CD1 1 
ATOM   301  C  CD2 . PHE A 1 39  ? -8.80430  5.67500   18.72647  1.000 39.05970  ? 71   PHE A CD2 1 
ATOM   302  C  CE1 . PHE A 1 39  ? -11.35047 5.57484   19.79915  1.000 39.99726  ? 71   PHE A CE1 1 
ATOM   303  C  CE2 . PHE A 1 39  ? -8.98119  5.60805   20.11210  1.000 42.08934  ? 71   PHE A CE2 1 
ATOM   304  C  CZ  . PHE A 1 39  ? -10.24756 5.55193   20.64054  1.000 38.84434  ? 71   PHE A CZ  1 
ATOM   305  N  N   . GLU A 1 40  ? -12.29477 4.33709   15.59400  1.000 33.14132  ? 72   GLU A N   1 
ATOM   306  C  CA  A GLU A 1 40  ? -13.60370 3.83192   16.00031  0.483 33.75552  ? 72   GLU A CA  1 
ATOM   307  C  CA  B GLU A 1 40  ? -13.60046 3.83113   16.00782  0.517 33.63268  ? 72   GLU A CA  1 
ATOM   308  C  C   . GLU A 1 40  ? -13.83498 2.41125   15.50443  1.000 32.72489  ? 72   GLU A C   1 
ATOM   309  O  O   . GLU A 1 40  ? -14.41119 1.58369   16.22034  1.000 33.12051  ? 72   GLU A O   1 
ATOM   310  C  CB  A GLU A 1 40  ? -14.71564 4.75008   15.49749  0.483 36.38151  ? 72   GLU A CB  1 
ATOM   311  C  CB  B GLU A 1 40  ? -14.70941 4.76855   15.53043  0.517 36.48157  ? 72   GLU A CB  1 
ATOM   312  C  CG  A GLU A 1 40  ? -14.91545 6.00386   16.33398  0.483 39.30527  ? 72   GLU A CG  1 
ATOM   313  C  CG  B GLU A 1 40  ? -14.75266 6.08182   16.30553  0.517 39.33141  ? 72   GLU A CG  1 
ATOM   314  C  CD  A GLU A 1 40  ? -15.29702 5.70525   17.77689  0.483 41.39645  ? 72   GLU A CD  1 
ATOM   315  C  CD  B GLU A 1 40  ? -15.88221 7.00652   15.88099  0.517 43.39023  ? 72   GLU A CD  1 
ATOM   316  O  OE1 A GLU A 1 40  ? -15.80681 4.59593   18.05412  0.483 43.92075  ? 72   GLU A OE1 1 
ATOM   317  O  OE1 B GLU A 1 40  ? -16.54545 6.72327   14.85954  0.517 46.31463  ? 72   GLU A OE1 1 
ATOM   318  O  OE2 A GLU A 1 40  ? -15.08510 6.58731   18.63686  0.483 49.32975  ? 72   GLU A OE2 1 
ATOM   319  O  OE2 B GLU A 1 40  ? -16.10300 8.02317   16.57256  0.517 49.08301  ? 72   GLU A OE2 1 
ATOM   320  N  N   . ARG A 1 41  ? -13.40647 2.10462   14.28107  1.000 29.96991  ? 73   ARG A N   1 
ATOM   321  C  CA  . ARG A 1 41  ? -13.65444 0.74524   13.79104  1.000 27.01940  ? 73   ARG A CA  1 
ATOM   322  C  C   . ARG A 1 41  ? -12.82238 -0.28054  14.55129  1.000 29.53361  ? 73   ARG A C   1 
ATOM   323  O  O   . ARG A 1 41  ? -13.33699 -1.33512  14.94494  1.000 28.73509  ? 73   ARG A O   1 
ATOM   324  C  CB  . ARG A 1 41  ? -13.36954 0.64535   12.28749  1.000 33.07627  ? 73   ARG A CB  1 
ATOM   325  C  CG  . ARG A 1 41  ? -13.83107 -0.67632  11.65686  1.000 37.38127  ? 73   ARG A CG  1 
ATOM   326  C  CD  . ARG A 1 41  ? -15.34957 -0.76852  11.51957  1.000 37.57343  ? 73   ARG A CD  1 
ATOM   327  N  NE  . ARG A 1 41  ? -15.79385 -2.16144  11.52667  1.000 35.03074  ? 73   ARG A NE  1 
ATOM   328  C  CZ  . ARG A 1 41  ? -15.73173 -2.98565  10.48794  1.000 38.53665  ? 73   ARG A CZ  1 
ATOM   329  N  NH1 . ARG A 1 41  ? -15.28249 -2.58602  9.31185   1.000 35.79733  ? 73   ARG A NH1 1 
ATOM   330  N  NH2 . ARG A 1 41  ? -16.10308 -4.25258  10.64062  1.000 34.49290  ? 73   ARG A NH2 1 
ATOM   331  N  N   . ILE A 1 42  ? -11.54071 0.00914   14.78722  1.000 28.08516  ? 74   ILE A N   1 
ATOM   332  C  CA  . ILE A 1 42  ? -10.70641 -0.94104  15.52707  1.000 27.39359  ? 74   ILE A CA  1 
ATOM   333  C  C   . ILE A 1 42  ? -11.22145 -1.10740  16.95058  1.000 28.31001  ? 74   ILE A C   1 
ATOM   334  O  O   . ILE A 1 42  ? -11.29908 -2.22814  17.46946  1.000 28.39489  ? 74   ILE A O   1 
ATOM   335  C  CB  . ILE A 1 42  ? -9.23388  -0.49765  15.51960  1.000 28.34922  ? 74   ILE A CB  1 
ATOM   336  C  CG1 . ILE A 1 42  ? -8.68865  -0.52887  14.09161  1.000 29.63488  ? 74   ILE A CG1 1 
ATOM   337  C  CG2 . ILE A 1 42  ? -8.40158  -1.41112  16.44823  1.000 28.21221  ? 74   ILE A CG2 1 
ATOM   338  C  CD1 . ILE A 1 42  ? -7.26456  0.04418   13.98561  1.000 31.03686  ? 74   ILE A CD1 1 
ATOM   339  N  N   . ALA A 1 43  ? -11.55449 0.00163   17.61484  1.000 29.53446  ? 75   ALA A N   1 
ATOM   340  C  CA  . ALA A 1 43  ? -11.97571 -0.09372  19.00918  1.000 29.95796  ? 75   ALA A CA  1 
ATOM   341  C  C   . ALA A 1 43  ? -13.28179 -0.86729  19.12473  1.000 31.86361  ? 75   ALA A C   1 
ATOM   342  O  O   . ALA A 1 43  ? -13.45534 -1.67770  20.04424  1.000 30.31075  ? 75   ALA A O   1 
ATOM   343  C  CB  . ALA A 1 43  ? -12.10144 1.30731   19.62027  1.000 28.68023  ? 75   ALA A CB  1 
ATOM   344  N  N   . GLY A 1 44  ? -14.19579 -0.65166  18.17580  1.000 28.11205  ? 76   GLY A N   1 
ATOM   345  C  CA  . GLY A 1 44  ? -15.46173 -1.35724  18.19162  1.000 30.89681  ? 76   GLY A CA  1 
ATOM   346  C  C   . GLY A 1 44  ? -15.31336 -2.85958  18.02621  1.000 30.45747  ? 76   GLY A C   1 
ATOM   347  O  O   . GLY A 1 44  ? -16.01964 -3.63245  18.68228  1.000 30.87882  ? 76   GLY A O   1 
ATOM   348  N  N   . GLU A 1 45  ? -14.43874 -3.29910  17.10806  1.000 27.44094  ? 77   GLU A N   1 
ATOM   349  C  CA  . GLU A 1 45  ? -14.23129 -4.73414  16.94501  1.000 25.67997  ? 77   GLU A CA  1 
ATOM   350  C  C   . GLU A 1 45  ? -13.51247 -5.30261  18.16704  1.000 25.27236  ? 77   GLU A C   1 
ATOM   351  O  O   . GLU A 1 45  ? -13.85421 -6.38964  18.64582  1.000 26.23416  ? 77   GLU A O   1 
ATOM   352  C  CB  . GLU A 1 45  ? -13.46208 -5.04014  15.65470  1.000 28.07353  ? 77   GLU A CB  1 
ATOM   353  C  CG  . GLU A 1 45  ? -14.19180 -4.47669  14.40990  1.000 29.35416  ? 77   GLU A CG  1 
ATOM   354  C  CD  . GLU A 1 45  ? -15.62169 -4.98130  14.20215  1.000 32.75444  ? 77   GLU A CD  1 
ATOM   355  O  OE1 . GLU A 1 45  ? -16.04266 -6.04223  14.72900  1.000 28.54162  ? 77   GLU A OE1 1 
ATOM   356  O  OE2 . GLU A 1 45  ? -16.39166 -4.23873  13.56625  1.000 33.37774  ? 77   GLU A OE2 1 
ATOM   357  N  N   . ALA A 1 46  ? -12.55435 -4.54488  18.72180  1.000 26.31269  ? 78   ALA A N   1 
ATOM   358  C  CA  . ALA A 1 46  ? -11.86078 -4.99206  19.93362  1.000 28.94920  ? 78   ALA A CA  1 
ATOM   359  C  C   . ALA A 1 46  ? -12.82797 -5.17142  21.09922  1.000 29.27196  ? 78   ALA A C   1 
ATOM   360  O  O   . ALA A 1 46  ? -12.68007 -6.10714  21.89824  1.000 28.03644  ? 78   ALA A O   1 
ATOM   361  C  CB  . ALA A 1 46  ? -10.75692 -3.99648  20.30500  1.000 28.13470  ? 78   ALA A CB  1 
ATOM   362  N  N   . SER A 1 47  ? -13.82343 -4.28607  21.20821  1.000 26.69542  ? 79   SER A N   1 
ATOM   363  C  CA  . SER A 1 47  ? -14.84093 -4.39871  22.24978  1.000 28.41464  ? 79   SER A CA  1 
ATOM   364  C  C   . SER A 1 47  ? -15.63190 -5.69699  22.11243  1.000 30.22483  ? 79   SER A C   1 
ATOM   365  O  O   . SER A 1 47  ? -15.92067 -6.37538  23.11456  1.000 27.22917  ? 79   SER A O   1 
ATOM   366  C  CB  . SER A 1 47  ? -15.78702 -3.20330  22.16686  1.000 30.43629  ? 79   SER A CB  1 
ATOM   367  O  OG  . SER A 1 47  ? -16.85611 -3.32046  23.09545  1.000 33.60153  ? 79   SER A OG  1 
ATOM   368  N  N   . ARG A 1 48  ? -16.00519 -6.04771  20.87630  1.000 27.79230  ? 80   ARG A N   1 
ATOM   369  C  CA  . ARG A 1 48  ? -16.73403 -7.28649  20.64587  1.000 24.41151  ? 80   ARG A CA  1 
ATOM   370  C  C   . ARG A 1 48  ? -15.87606 -8.48378  20.99107  1.000 23.89786  ? 80   ARG A C   1 
ATOM   371  O  O   . ARG A 1 48  ? -16.36183 -9.45780  21.58220  1.000 25.31469  ? 80   ARG A O   1 
ATOM   372  C  CB  . ARG A 1 48  ? -17.21078 -7.36493  19.18701  1.000 23.91380  ? 80   ARG A CB  1 
ATOM   373  C  CG  . ARG A 1 48  ? -18.21190 -6.27504  18.87265  1.000 26.76327  ? 80   ARG A CG  1 
ATOM   374  C  CD  . ARG A 1 48  ? -18.65774 -6.27450  17.39659  1.000 27.34695  ? 80   ARG A CD  1 
ATOM   375  N  NE  . ARG A 1 48  ? -19.52511 -5.11956  17.19993  1.000 28.29164  ? 80   ARG A NE  1 
ATOM   376  C  CZ  . ARG A 1 48  ? -20.84568 -5.10637  17.31571  1.000 31.61669  ? 80   ARG A CZ  1 
ATOM   377  N  NH1 . ARG A 1 48  ? -21.55080 -6.21691  17.50053  1.000 31.17899  ? 80   ARG A NH1 1 
ATOM   378  N  NH2 . ARG A 1 48  ? -21.48731 -3.94167  17.24528  1.000 34.92582  ? 80   ARG A NH2 1 
ATOM   379  N  N   . LEU A 1 49  ? -14.60199 -8.43758  20.61907  1.000 23.62731  ? 81   LEU A N   1 
ATOM   380  C  CA  . LEU A 1 49  ? -13.71456 -9.55619  20.91207  1.000 23.94105  ? 81   LEU A CA  1 
ATOM   381  C  C   . LEU A 1 49  ? -13.58871 -9.76071  22.40877  1.000 26.08661  ? 81   LEU A C   1 
ATOM   382  O  O   . LEU A 1 49  ? -13.67045 -10.89108 22.90065  1.000 26.22644  ? 81   LEU A O   1 
ATOM   383  C  CB  . LEU A 1 49  ? -12.34365 -9.29699  20.30165  1.000 25.76123  ? 81   LEU A CB  1 
ATOM   384  C  CG  . LEU A 1 49  ? -12.38077 -9.41190  18.79390  1.000 25.07349  ? 81   LEU A CG  1 
ATOM   385  C  CD1 . LEU A 1 49  ? -11.18397 -8.64764  18.21573  1.000 33.44053  ? 81   LEU A CD1 1 
ATOM   386  C  CD2 . LEU A 1 49  ? -12.31666 -10.90657 18.41167  1.000 29.34576  ? 81   LEU A CD2 1 
ATOM   387  N  N   . ALA A 1 50  ? -13.42285 -8.67760  23.15969  1.000 29.62431  ? 82   ALA A N   1 
ATOM   388  C  CA  . ALA A 1 50  ? -13.32728 -8.85899  24.60324  1.000 29.72843  ? 82   ALA A CA  1 
ATOM   389  C  C   . ALA A 1 50  ? -14.62964 -9.39995  25.16823  1.000 28.37448  ? 82   ALA A C   1 
ATOM   390  O  O   . ALA A 1 50  ? -14.62082 -10.29159 26.02719  1.000 29.40697  ? 82   ALA A O   1 
ATOM   391  C  CB  . ALA A 1 50  ? -12.95590 -7.53696  25.27937  1.000 30.28957  ? 82   ALA A CB  1 
ATOM   392  N  N   . HIS A 1 51  ? -15.76668 -8.93750  24.64004  1.000 26.57304  ? 83   HIS A N   1 
ATOM   393  C  CA  . HIS A 1 51  ? -17.04026 -9.40071  25.16386  1.000 26.94448  ? 83   HIS A CA  1 
ATOM   394  C  C   . HIS A 1 51  ? -17.23799 -10.88659 24.91430  1.000 26.83001  ? 83   HIS A C   1 
ATOM   395  O  O   . HIS A 1 51  ? -17.60940 -11.63228 25.83347  1.000 27.93167  ? 83   HIS A O   1 
ATOM   396  C  CB  . HIS A 1 51  ? -18.18263 -8.61541  24.51785  1.000 30.34915  ? 83   HIS A CB  1 
ATOM   397  C  CG  . HIS A 1 51  ? -19.53161 -9.00424  25.01898  1.000 32.55838  ? 83   HIS A CG  1 
ATOM   398  N  ND1 . HIS A 1 51  ? -20.24522 -10.06469 24.50441  1.000 35.86573  ? 83   HIS A ND1 1 
ATOM   399  C  CD2 . HIS A 1 51  ? -20.29516 -8.47783  26.00503  1.000 35.27556  ? 83   HIS A CD2 1 
ATOM   400  C  CE1 . HIS A 1 51  ? -21.38937 -10.17715 25.15257  1.000 31.25712  ? 83   HIS A CE1 1 
ATOM   401  N  NE2 . HIS A 1 51  ? -21.44828 -9.22112  26.06351  1.000 45.14587  ? 83   HIS A NE2 1 
ATOM   402  N  N   . TYR A 1 52  ? -16.93118 -11.35059 23.69724  1.000 26.92997  ? 84   TYR A N   1 
ATOM   403  C  CA  . TYR A 1 52  ? -17.18041 -12.74709 23.39480  1.000 26.61687  ? 84   TYR A CA  1 
ATOM   404  C  C   . TYR A 1 52  ? -16.16096 -13.65563 24.05139  1.000 25.79660  ? 84   TYR A C   1 
ATOM   405  O  O   . TYR A 1 52  ? -16.44442 -14.83595 24.25473  1.000 29.20229  ? 84   TYR A O   1 
ATOM   406  C  CB  . TYR A 1 52  ? -17.17363 -12.97660 21.87792  1.000 25.65764  ? 84   TYR A CB  1 
ATOM   407  C  CG  . TYR A 1 52  ? -18.34195 -12.32865 21.16832  1.000 24.70096  ? 84   TYR A CG  1 
ATOM   408  C  CD1 . TYR A 1 52  ? -19.63439 -12.58549 21.57267  1.000 29.00030  ? 84   TYR A CD1 1 
ATOM   409  C  CD2 . TYR A 1 52  ? -18.13861 -11.53727 20.01838  1.000 25.64249  ? 84   TYR A CD2 1 
ATOM   410  C  CE1 . TYR A 1 52  ? -20.73151 -12.03638 20.90456  1.000 30.21601  ? 84   TYR A CE1 1 
ATOM   411  C  CE2 . TYR A 1 52  ? -19.23328 -10.99203 19.33385  1.000 26.20810  ? 84   TYR A CE2 1 
ATOM   412  C  CZ  . TYR A 1 52  ? -20.51629 -11.23444 19.80119  1.000 26.71335  ? 84   TYR A CZ  1 
ATOM   413  O  OH  . TYR A 1 52  ? -21.63182 -10.73359 19.15903  1.000 28.44993  ? 84   TYR A OH  1 
ATOM   414  N  N   . ASN A 1 53  ? -15.00273 -13.12171 24.41757  1.000 27.46676  ? 85   ASN A N   1 
ATOM   415  C  CA  . ASN A 1 53  ? -14.01443 -13.89765 25.16230  1.000 30.33820  ? 85   ASN A CA  1 
ATOM   416  C  C   . ASN A 1 53  ? -14.09919 -13.69323 26.67007  1.000 33.98762  ? 85   ASN A C   1 
ATOM   417  O  O   . ASN A 1 53  ? -13.25059 -14.21578 27.41102  1.000 32.70639  ? 85   ASN A O   1 
ATOM   418  C  CB  . ASN A 1 53  ? -12.61403 -13.61680 24.62077  1.000 27.33535  ? 85   ASN A CB  1 
ATOM   419  C  CG  . ASN A 1 53  ? -12.39932 -14.25162 23.26631  1.000 32.39742  ? 85   ASN A CG  1 
ATOM   420  O  OD1 . ASN A 1 53  ? -11.96730 -15.40909 23.18749  1.000 30.66511  ? 85   ASN A OD1 1 
ATOM   421  N  ND2 . ASN A 1 53  ? -12.74433 -13.53571 22.19453  1.000 32.28876  ? 85   ASN A ND2 1 
ATOM   422  N  N   . LYS A 1 54  ? -15.12849 -12.98719 27.14146  1.000 27.56504  ? 86   LYS A N   1 
ATOM   423  C  CA  . LYS A 1 54  ? -15.39675 -12.82049 28.57693  1.000 29.23179  ? 86   LYS A CA  1 
ATOM   424  C  C   . LYS A 1 54  ? -14.21995 -12.16952 29.28487  1.000 31.93843  ? 86   LYS A C   1 
ATOM   425  O  O   . LYS A 1 54  ? -13.82532 -12.57296 30.39136  1.000 35.49056  ? 86   LYS A O   1 
ATOM   426  C  CB  . LYS A 1 54  ? -15.75284 -14.15774 29.22966  1.000 33.18549  ? 86   LYS A CB  1 
ATOM   427  C  CG  . LYS A 1 54  ? -16.96233 -14.83122 28.58573  1.000 36.78748  ? 86   LYS A CG  1 
ATOM   428  C  CD  . LYS A 1 54  ? -18.16789 -13.92284 28.62572  1.000 47.23540  ? 86   LYS A CD  1 
ATOM   429  C  CE  . LYS A 1 54  ? -19.29177 -14.49514 27.78024  1.000 50.05051  ? 86   LYS A CE  1 
ATOM   430  N  NZ  . LYS A 1 54  ? -20.36479 -15.10671 28.59679  1.000 57.40213  ? 86   LYS A NZ  1 
ATOM   431  N  N   . ARG A 1 55  ? -13.65882 -11.15427 28.64239  1.000 32.26033  ? 87   ARG A N   1 
ATOM   432  C  CA  . ARG A 1 55  ? -12.54048 -10.39490 29.18344  1.000 37.98830  ? 87   ARG A CA  1 
ATOM   433  C  C   . ARG A 1 55  ? -13.01997 -9.00811  29.58133  1.000 39.64296  ? 87   ARG A C   1 
ATOM   434  O  O   . ARG A 1 55  ? -13.54080 -8.26427  28.74353  1.000 38.29861  ? 87   ARG A O   1 
ATOM   435  C  CB  . ARG A 1 55  ? -11.43582 -10.28069 28.14174  1.000 34.20204  ? 87   ARG A CB  1 
ATOM   436  C  CG  . ARG A 1 55  ? -10.84382 -11.60774 27.74432  1.000 37.03680  ? 87   ARG A CG  1 
ATOM   437  C  CD  . ARG A 1 55  ? -9.99294  -11.43475 26.53568  1.000 41.98149  ? 87   ARG A CD  1 
ATOM   438  N  NE  . ARG A 1 55  ? -9.58044  -12.71186 25.97621  1.000 43.97039  ? 87   ARG A NE  1 
ATOM   439  C  CZ  . ARG A 1 55  ? -9.24920  -12.87934 24.70508  1.000 45.99180  ? 87   ARG A CZ  1 
ATOM   440  N  NH1 . ARG A 1 55  ? -9.31192  -11.87809 23.83901  1.000 42.17260  ? 87   ARG A NH1 1 
ATOM   441  N  NH2 . ARG A 1 55  ? -8.86216  -14.07967 24.28967  1.000 44.40217  ? 87   ARG A NH2 1 
ATOM   442  N  N   . SER A 1 56  ? -12.78249 -8.63468  30.83500  1.000 34.95880  ? 88   SER A N   1 
ATOM   443  C  CA  . SER A 1 56  ? -13.18374 -7.32284  31.31586  1.000 38.70941  ? 88   SER A CA  1 
ATOM   444  C  C   . SER A 1 56  ? -12.23840 -6.20701  30.89153  1.000 39.13072  ? 88   SER A C   1 
ATOM   445  O  O   . SER A 1 56  ? -12.60678 -5.03226  31.00680  1.000 41.34823  ? 88   SER A O   1 
ATOM   446  C  CB  . SER A 1 56  ? -13.28188 -7.33482  32.84929  1.000 42.06606  ? 88   SER A CB  1 
ATOM   447  O  OG  . SER A 1 56  ? -11.99284 -7.50025  33.42726  1.000 49.28934  ? 88   SER A OG  1 
ATOM   448  N  N   . THR A 1 57  ? -11.05351 -6.53731  30.39020  1.000 34.26952  ? 89   THR A N   1 
ATOM   449  C  CA  . THR A 1 57  ? -10.03505 -5.55056  30.06601  1.000 36.12670  ? 89   THR A CA  1 
ATOM   450  C  C   . THR A 1 57  ? -9.62211  -5.72050  28.61810  1.000 36.40428  ? 89   THR A C   1 
ATOM   451  O  O   . THR A 1 57  ? -9.24100  -6.81902  28.21301  1.000 37.40619  ? 89   THR A O   1 
ATOM   452  C  CB  . THR A 1 57  ? -8.79145  -5.72636  30.94558  1.000 43.50615  ? 89   THR A CB  1 
ATOM   453  O  OG1 . THR A 1 57  ? -9.17580  -5.73710  32.32126  1.000 47.37042  ? 89   THR A OG1 1 
ATOM   454  C  CG2 . THR A 1 57  ? -7.78238  -4.60476  30.69807  1.000 41.87055  ? 89   THR A CG2 1 
ATOM   455  N  N   . ILE A 1 58  ? -9.65030  -4.62777  27.86171  1.000 31.90166  ? 90   ILE A N   1 
ATOM   456  C  CA  . ILE A 1 58  ? -9.06877  -4.60082  26.52014  1.000 30.59501  ? 90   ILE A CA  1 
ATOM   457  C  C   . ILE A 1 58  ? -7.57533  -4.33948  26.63370  1.000 34.77536  ? 90   ILE A C   1 
ATOM   458  O  O   . ILE A 1 58  ? -7.15737  -3.35540  27.24923  1.000 33.47024  ? 90   ILE A O   1 
ATOM   459  C  CB  . ILE A 1 58  ? -9.75648  -3.55523  25.63190  1.000 35.33994  ? 90   ILE A CB  1 
ATOM   460  C  CG1 . ILE A 1 58  ? -11.18792 -4.00789  25.31004  1.000 37.50139  ? 90   ILE A CG1 1 
ATOM   461  C  CG2 . ILE A 1 58  ? -8.92752  -3.24158  24.38660  1.000 33.50885  ? 90   ILE A CG2 1 
ATOM   462  C  CD1 . ILE A 1 58  ? -11.98762 -2.99673  24.51161  1.000 38.31323  ? 90   ILE A CD1 1 
ATOM   463  N  N   . THR A 1 59  ? -6.77180  -5.26337  26.10666  1.000 29.54941  ? 91   THR A N   1 
ATOM   464  C  CA  . THR A 1 59  ? -5.32058  -5.16976  26.04314  1.000 32.83994  ? 91   THR A CA  1 
ATOM   465  C  C   . THR A 1 59  ? -4.89228  -5.08975  24.58814  1.000 32.81386  ? 91   THR A C   1 
ATOM   466  O  O   . THR A 1 59  ? -5.72345  -5.00987  23.67845  1.000 30.82500  ? 91   THR A O   1 
ATOM   467  C  CB  . THR A 1 59  ? -4.65630  -6.35841  26.74686  1.000 34.48473  ? 91   THR A CB  1 
ATOM   468  O  OG1 . THR A 1 59  ? -4.84512  -7.54390  25.97302  1.000 36.55111  ? 91   THR A OG1 1 
ATOM   469  C  CG2 . THR A 1 59  ? -5.24678  -6.56447  28.15239  1.000 39.01641  ? 91   THR A CG2 1 
ATOM   470  N  N   . SER A 1 60  ? -3.57918  -5.14546  24.36226  1.000 30.22931  ? 92   SER A N   1 
ATOM   471  C  CA  . SER A 1 60  ? -3.08985  -5.13740  22.99303  1.000 27.84504  ? 92   SER A CA  1 
ATOM   472  C  C   . SER A 1 60  ? -3.53516  -6.37698  22.22673  1.000 31.28660  ? 92   SER A C   1 
ATOM   473  O  O   . SER A 1 60  ? -3.56603  -6.35242  20.98746  1.000 29.52314  ? 92   SER A O   1 
ATOM   474  C  CB  . SER A 1 60  ? -1.55992  -5.01126  22.97684  1.000 33.99721  ? 92   SER A CB  1 
ATOM   475  O  OG  . SER A 1 60  ? -0.92007  -6.24697  23.25967  1.000 35.30652  ? 92   SER A OG  1 
ATOM   476  N  N   . ARG A 1 61  ? -3.91413  -7.44716  22.93307  1.000 29.22317  ? 93   ARG A N   1 
ATOM   477  C  CA  . ARG A 1 61  ? -4.35941  -8.66585  22.25729  1.000 30.92461  ? 93   ARG A CA  1 
ATOM   478  C  C   . ARG A 1 61  ? -5.60411  -8.43087  21.40450  1.000 29.82027  ? 93   ARG A C   1 
ATOM   479  O  O   . ARG A 1 61  ? -5.65961  -8.87712  20.24870  1.000 30.14020  ? 93   ARG A O   1 
ATOM   480  C  CB  . ARG A 1 61  ? -4.59111  -9.76607  23.30211  1.000 34.25831  ? 93   ARG A CB  1 
ATOM   481  C  CG  . ARG A 1 61  ? -5.24207  -11.03592 22.78224  1.000 38.06440  ? 93   ARG A CG  1 
ATOM   482  C  CD  . ARG A 1 61  ? -5.25465  -12.14800 23.85309  1.000 48.13831  ? 93   ARG A CD  1 
ATOM   483  N  NE  . ARG A 1 61  ? -5.86338  -11.74117 25.11460  1.000 52.91648  ? 93   ARG A NE  1 
ATOM   484  C  CZ  . ARG A 1 61  ? -5.83226  -12.46467 26.22999  1.000 61.94637  ? 93   ARG A CZ  1 
ATOM   485  N  NH1 . ARG A 1 61  ? -5.29327  -13.67573 26.25652  1.000 50.99888  ? 93   ARG A NH1 1 
ATOM   486  N  NH2 . ARG A 1 61  ? -6.33739  -11.95289 27.35107  1.000 58.86846  ? 93   ARG A NH2 1 
ATOM   487  N  N   . GLU A 1 62  ? -6.60614  -7.72893  21.94311  1.000 28.02783  ? 94   GLU A N   1 
ATOM   488  C  CA  . GLU A 1 62  ? -7.82733  -7.47095  21.18216  1.000 31.30630  ? 94   GLU A CA  1 
ATOM   489  C  C   . GLU A 1 62  ? -7.59099  -6.42920  20.10699  1.000 27.92062  ? 94   GLU A C   1 
ATOM   490  O  O   . GLU A 1 62  ? -8.20002  -6.49236  19.03044  1.000 28.72176  ? 94   GLU A O   1 
ATOM   491  C  CB  . GLU A 1 62  ? -8.95086  -6.99308  22.10139  1.000 29.35857  ? 94   GLU A CB  1 
ATOM   492  C  CG  . GLU A 1 62  ? -9.46651  -8.02286  23.08948  1.000 33.41334  ? 94   GLU A CG  1 
ATOM   493  C  CD  . GLU A 1 62  ? -8.47769  -8.28594  24.21340  1.000 36.66404  ? 94   GLU A CD  1 
ATOM   494  O  OE1 . GLU A 1 62  ? -7.84845  -7.32114  24.68007  1.000 42.52667  ? 94   GLU A OE1 1 
ATOM   495  O  OE2 . GLU A 1 62  ? -8.38549  -9.43154  24.69318  1.000 40.36925  ? 94   GLU A OE2 1 
ATOM   496  N  N   . ILE A 1 63  ? -6.73281  -5.45047  20.38145  1.000 27.23484  ? 95   ILE A N   1 
ATOM   497  C  CA  . ILE A 1 63  ? -6.39492  -4.49980  19.32906  1.000 25.97975  ? 95   ILE A CA  1 
ATOM   498  C  C   . ILE A 1 63  ? -5.72800  -5.22290  18.16976  1.000 26.69874  ? 95   ILE A C   1 
ATOM   499  O  O   . ILE A 1 63  ? -6.05073  -4.98403  16.99885  1.000 26.64246  ? 95   ILE A O   1 
ATOM   500  C  CB  . ILE A 1 63  ? -5.49629  -3.37700  19.87736  1.000 26.92021  ? 95   ILE A CB  1 
ATOM   501  C  CG1 . ILE A 1 63  ? -6.16111  -2.65641  21.04197  1.000 28.26864  ? 95   ILE A CG1 1 
ATOM   502  C  CG2 . ILE A 1 63  ? -5.16854  -2.37941  18.74285  1.000 29.14792  ? 95   ILE A CG2 1 
ATOM   503  C  CD1 . ILE A 1 63  ? -7.51939  -2.07405  20.74663  1.000 30.27518  ? 95   ILE A CD1 1 
ATOM   504  N  N   . GLN A 1 64  ? -4.77903  -6.11540  18.46968  1.000 27.10437  ? 96   GLN A N   1 
ATOM   505  C  CA  . GLN A 1 64  ? -4.08900  -6.83522  17.40225  1.000 26.43878  ? 96   GLN A CA  1 
ATOM   506  C  C   . GLN A 1 64  ? -5.05816  -7.68240  16.58978  1.000 25.56182  ? 96   GLN A C   1 
ATOM   507  O  O   . GLN A 1 64  ? -4.99759  -7.69914  15.35376  1.000 26.38006  ? 96   GLN A O   1 
ATOM   508  C  CB  . GLN A 1 64  ? -2.98258  -7.71450  17.98438  1.000 27.74673  ? 96   GLN A CB  1 
ATOM   509  C  CG  . GLN A 1 64  ? -2.36000  -8.64668  16.94400  1.000 27.35134  ? 96   GLN A CG  1 
ATOM   510  C  CD  . GLN A 1 64  ? -1.00994  -9.19173  17.38453  1.000 33.06117  ? 96   GLN A CD  1 
ATOM   511  O  OE1 . GLN A 1 64  ? -0.88384  -10.35914 17.76560  1.000 46.42321  ? 96   GLN A OE1 1 
ATOM   512  N  NE2 . GLN A 1 64  ? 0.00370   -8.35619  17.32554  1.000 28.67486  ? 96   GLN A NE2 1 
ATOM   513  N  N   . THR A 1 65  ? -5.95169  -8.41447  17.26543  1.000 25.47781  ? 97   THR A N   1 
ATOM   514  C  CA  . THR A 1 65  ? -6.89872  -9.24639  16.52855  1.000 25.01183  ? 97   THR A CA  1 
ATOM   515  C  C   . THR A 1 65  ? -7.82774  -8.40438  15.67100  1.000 27.26091  ? 97   THR A C   1 
ATOM   516  O  O   . THR A 1 65  ? -8.09435  -8.75200  14.51463  1.000 27.73275  ? 97   THR A O   1 
ATOM   517  C  CB  . THR A 1 65  ? -7.69623  -10.12336 17.49251  1.000 28.58904  ? 97   THR A CB  1 
ATOM   518  O  OG1 . THR A 1 65  ? -6.78459  -10.99134 18.16772  1.000 29.24134  ? 97   THR A OG1 1 
ATOM   519  C  CG2 . THR A 1 65  ? -8.71509  -10.96624 16.73001  1.000 29.59739  ? 97   THR A CG2 1 
ATOM   520  N  N   . ALA A 1 66  ? -8.30436  -7.27775  16.20653  1.000 25.47785  ? 98   ALA A N   1 
ATOM   521  C  CA  . ALA A 1 66  ? -9.14325  -6.38646  15.40693  1.000 25.83241  ? 98   ALA A CA  1 
ATOM   522  C  C   . ALA A 1 66  ? -8.39976  -5.88176  14.17702  1.000 27.45600  ? 98   ALA A C   1 
ATOM   523  O  O   . ALA A 1 66  ? -8.98565  -5.77041  13.09714  1.000 28.53266  ? 98   ALA A O   1 
ATOM   524  C  CB  . ALA A 1 66  ? -9.61395  -5.19766  16.24791  1.000 26.16042  ? 98   ALA A CB  1 
ATOM   525  N  N   . VAL A 1 67  ? -7.12309  -5.53654  14.33714  1.000 25.92047  ? 99   VAL A N   1 
ATOM   526  C  CA  . VAL A 1 67  ? -6.31717  -5.07530  13.20659  1.000 27.52150  ? 99   VAL A CA  1 
ATOM   527  C  C   . VAL A 1 67  ? -6.23675  -6.16091  12.14360  1.000 28.73942  ? 99   VAL A C   1 
ATOM   528  O  O   . VAL A 1 67  ? -6.35752  -5.88857  10.94007  1.000 28.73059  ? 99   VAL A O   1 
ATOM   529  C  CB  . VAL A 1 67  ? -4.92073  -4.63822  13.70036  1.000 27.69754  ? 99   VAL A CB  1 
ATOM   530  C  CG1 . VAL A 1 67  ? -3.92684  -4.52690  12.52813  1.000 30.02711  ? 99   VAL A CG1 1 
ATOM   531  C  CG2 . VAL A 1 67  ? -5.01482  -3.30670  14.47368  1.000 28.70115  ? 99   VAL A CG2 1 
ATOM   532  N  N   . ARG A 1 68  ? -6.05557  -7.41747  12.56040  1.000 26.41018  ? 100  ARG A N   1 
ATOM   533  C  CA  . ARG A 1 68  ? -5.98558  -8.50539  11.58627  1.000 27.01056  ? 100  ARG A CA  1 
ATOM   534  C  C   . ARG A 1 68  ? -7.31139  -8.73400  10.86755  1.000 32.45685  ? 100  ARG A C   1 
ATOM   535  O  O   . ARG A 1 68  ? -7.32258  -9.15386  9.70184   1.000 30.76817  ? 100  ARG A O   1 
ATOM   536  C  CB  . ARG A 1 68  ? -5.54009  -9.78711  12.28619  1.000 32.51875  ? 100  ARG A CB  1 
ATOM   537  C  CG  . ARG A 1 68  ? -4.09378  -9.79193  12.74796  1.000 33.88528  ? 100  ARG A CG  1 
ATOM   538  C  CD  . ARG A 1 68  ? -3.80504  -11.06352 13.57221  1.000 42.97715  ? 100  ARG A CD  1 
ATOM   539  N  NE  . ARG A 1 68  ? -2.37619  -11.25689 13.77706  1.000 48.29715  ? 100  ARG A NE  1 
ATOM   540  C  CZ  . ARG A 1 68  ? -1.82046  -11.85974 14.81869  1.000 53.67007  ? 100  ARG A CZ  1 
ATOM   541  N  NH1 . ARG A 1 68  ? -2.54854  -12.33562 15.81861  1.000 54.87568  ? 100  ARG A NH1 1 
ATOM   542  N  NH2 . ARG A 1 68  ? -0.49726  -11.99064 14.85723  1.000 52.88968  ? 100  ARG A NH2 1 
ATOM   543  N  N   . LEU A 1 69  ? -8.43360  -8.48940  11.53866  1.000 27.92081  ? 101  LEU A N   1 
ATOM   544  C  CA  . LEU A 1 69  ? -9.72694  -8.66727  10.89340  1.000 28.76376  ? 101  LEU A CA  1 
ATOM   545  C  C   . LEU A 1 69  ? -10.02673 -7.54102  9.91486   1.000 28.92329  ? 101  LEU A C   1 
ATOM   546  O  O   . LEU A 1 69  ? -10.78004 -7.73906  8.94948   1.000 31.99773  ? 101  LEU A O   1 
ATOM   547  C  CB  . LEU A 1 69  ? -10.82081 -8.73991  11.94957  1.000 33.51543  ? 101  LEU A CB  1 
ATOM   548  C  CG  . LEU A 1 69  ? -10.74685 -9.95927  12.85017  1.000 36.88674  ? 101  LEU A CG  1 
ATOM   549  C  CD1 . LEU A 1 69  ? -11.72781 -9.78147  13.99406  1.000 34.12694  ? 101  LEU A CD1 1 
ATOM   550  C  CD2 . LEU A 1 69  ? -11.04749 -11.19509 12.03419  1.000 33.72264  ? 101  LEU A CD2 1 
ATOM   551  N  N   . LEU A 1 70  ? -9.42908  -6.36538  10.12712  1.000 27.45774  ? 102  LEU A N   1 
ATOM   552  C  CA  . LEU A 1 70  ? -9.81283  -5.16094  9.39841   1.000 28.25982  ? 102  LEU A CA  1 
ATOM   553  C  C   . LEU A 1 70  ? -8.84440  -4.77350  8.29320   1.000 31.56362  ? 102  LEU A C   1 
ATOM   554  O  O   . LEU A 1 70  ? -9.27880  -4.30545  7.23419   1.000 36.19869  ? 102  LEU A O   1 
ATOM   555  C  CB  . LEU A 1 70  ? -9.94523  -3.98265  10.36675  1.000 27.97702  ? 102  LEU A CB  1 
ATOM   556  C  CG  . LEU A 1 70  ? -11.12994 -4.12646  11.31658  1.000 30.26392  ? 102  LEU A CG  1 
ATOM   557  C  CD1 . LEU A 1 70  ? -11.06138 -3.03334  12.38172  1.000 30.19147  ? 102  LEU A CD1 1 
ATOM   558  C  CD2 . LEU A 1 70  ? -12.43748 -4.04903  10.54782  1.000 34.69465  ? 102  LEU A CD2 1 
ATOM   559  N  N   . LEU A 1 71  ? -7.55481  -4.93356  8.52040   1.000 30.38386  ? 103  LEU A N   1 
ATOM   560  C  CA  . LEU A 1 71  ? -6.56418  -4.47824  7.54170   1.000 30.75977  ? 103  LEU A CA  1 
ATOM   561  C  C   . LEU A 1 71  ? -6.15812  -5.61647  6.60762   1.000 31.19943  ? 103  LEU A C   1 
ATOM   562  O  O   . LEU A 1 71  ? -6.03406  -6.76687  7.04550   1.000 34.42764  ? 103  LEU A O   1 
ATOM   563  C  CB  . LEU A 1 71  ? -5.32496  -3.94703  8.24033   1.000 32.78716  ? 103  LEU A CB  1 
ATOM   564  C  CG  . LEU A 1 71  ? -5.33759  -2.48065  8.67261   1.000 30.38233  ? 103  LEU A CG  1 
ATOM   565  C  CD1 . LEU A 1 71  ? -6.38927  -2.20398  9.75481   1.000 32.32245  ? 103  LEU A CD1 1 
ATOM   566  C  CD2 . LEU A 1 71  ? -3.95292  -2.09415  9.15719   1.000 30.98984  ? 103  LEU A CD2 1 
ATOM   567  N  N   . PRO A 1 72  ? -6.04514  -5.34722  5.30783   1.000 32.90927  ? 104  PRO A N   1 
ATOM   568  C  CA  . PRO A 1 72  ? -5.63929  -6.37738  4.34951   1.000 34.66600  ? 104  PRO A CA  1 
ATOM   569  C  C   . PRO A 1 72  ? -4.14381  -6.44154  4.07509   1.000 36.17098  ? 104  PRO A C   1 
ATOM   570  O  O   . PRO A 1 72  ? -3.42176  -5.44887  4.15291   1.000 33.56345  ? 104  PRO A O   1 
ATOM   571  C  CB  . PRO A 1 72  ? -6.38240  -5.95515  3.07517   1.000 38.65456  ? 104  PRO A CB  1 
ATOM   572  C  CG  . PRO A 1 72  ? -6.38859  -4.47131  3.15733   1.000 35.55524  ? 104  PRO A CG  1 
ATOM   573  C  CD  . PRO A 1 72  ? -6.55036  -4.14014  4.63809   1.000 30.84462  ? 104  PRO A CD  1 
ATOM   574  N  N   . GLY A 1 73  ? -3.69195  -7.64557  3.72891   1.000 36.00792  ? 105  GLY A N   1 
ATOM   575  C  CA  . GLY A 1 73  ? -2.41054  -7.81047  3.03702   1.000 35.27361  ? 105  GLY A CA  1 
ATOM   576  C  C   . GLY A 1 73  ? -1.20512  -7.25800  3.77349   1.000 34.72789  ? 105  GLY A C   1 
ATOM   577  O  O   . GLY A 1 73  ? -1.02525  -7.47076  4.97380   1.000 35.46736  ? 105  GLY A O   1 
ATOM   578  N  N   . GLU A 1 74  ? -0.33774  -6.56614  3.02378   1.000 34.85012  ? 106  GLU A N   1 
ATOM   579  C  CA  . GLU A 1 74  ? 0.90945   -6.05762  3.58992   1.000 33.11654  ? 106  GLU A CA  1 
ATOM   580  C  C   . GLU A 1 74  ? 0.64752   -4.97783  4.62756   1.000 34.24527  ? 106  GLU A C   1 
ATOM   581  O  O   . GLU A 1 74  ? 1.39795   -4.85988  5.60667   1.000 34.46203  ? 106  GLU A O   1 
ATOM   582  C  CB  . GLU A 1 74  ? 1.80026   -5.50168  2.47405   1.000 33.38349  ? 106  GLU A CB  1 
ATOM   583  C  CG  . GLU A 1 74  ? 2.28624   -6.54742  1.48569   1.000 38.55422  ? 106  GLU A CG  1 
ATOM   584  C  CD  . GLU A 1 74  ? 3.18820   -7.56830  2.14032   1.000 45.84498  ? 106  GLU A CD  1 
ATOM   585  O  OE1 . GLU A 1 74  ? 4.23952   -7.17377  2.69230   1.000 42.63310  ? 106  GLU A OE1 1 
ATOM   586  O  OE2 . GLU A 1 74  ? 2.83500   -8.76172  2.11721   1.000 46.50918  ? 106  GLU A OE2 1 
ATOM   587  N  N   . LEU A 1 75  ? -0.41770  -4.20001  4.44475   1.000 32.32929  ? 107  LEU A N   1 
ATOM   588  C  CA  A LEU A 1 75  ? -0.79171  -3.19951  5.44373   0.440 33.20342  ? 107  LEU A CA  1 
ATOM   589  C  CA  B LEU A 1 75  ? -0.78734  -3.19925  5.43907   0.560 33.17504  ? 107  LEU A CA  1 
ATOM   590  C  C   . LEU A 1 75  ? -0.96638  -3.83398  6.81212   1.000 34.46823  ? 107  LEU A C   1 
ATOM   591  O  O   . LEU A 1 75  ? -0.49359  -3.30071  7.82760   1.000 29.89470  ? 107  LEU A O   1 
ATOM   592  C  CB  A LEU A 1 75  ? -2.09145  -2.50444  5.04410   0.440 37.49675  ? 107  LEU A CB  1 
ATOM   593  C  CB  B LEU A 1 75  ? -2.07392  -2.50714  4.99660   0.560 36.13775  ? 107  LEU A CB  1 
ATOM   594  C  CG  A LEU A 1 75  ? -2.12087  -1.30420  4.10894   0.440 32.58627  ? 107  LEU A CG  1 
ATOM   595  C  CG  B LEU A 1 75  ? -2.36996  -1.10912  5.51416   0.560 31.76858  ? 107  LEU A CG  1 
ATOM   596  C  CD1 A LEU A 1 75  ? -3.55932  -0.82323  4.01824   0.440 30.69266  ? 107  LEU A CD1 1 
ATOM   597  C  CD1 B LEU A 1 75  ? -1.40062  -0.10721  4.89843   0.560 33.07197  ? 107  LEU A CD1 1 
ATOM   598  C  CD2 A LEU A 1 75  ? -1.20771  -0.19525  4.61200   0.440 32.89405  ? 107  LEU A CD2 1 
ATOM   599  C  CD2 B LEU A 1 75  ? -3.81885  -0.74299  5.20115   0.560 30.25854  ? 107  LEU A CD2 1 
ATOM   600  N  N   . ALA A 1 76  ? -1.67137  -4.96798  6.86355   1.000 29.28410  ? 108  ALA A N   1 
ATOM   601  C  CA  . ALA A 1 76  ? -1.89987  -5.63469  8.13779   1.000 30.78198  ? 108  ALA A CA  1 
ATOM   602  C  C   . ALA A 1 76  ? -0.58916  -6.13000  8.74035   1.000 31.29915  ? 108  ALA A C   1 
ATOM   603  O  O   . ALA A 1 76  ? -0.36299  -5.99122  9.94723   1.000 31.23547  ? 108  ALA A O   1 
ATOM   604  C  CB  . ALA A 1 76  ? -2.89088  -6.79159  7.95080   1.000 30.71996  ? 108  ALA A CB  1 
ATOM   605  N  N   . LYS A 1 77  ? 0.28427   -6.72129  7.92115   1.000 28.87569  ? 109  LYS A N   1 
ATOM   606  C  CA  . LYS A 1 77  ? 1.57830   -7.17698  8.42275   1.000 33.12155  ? 109  LYS A CA  1 
ATOM   607  C  C   . LYS A 1 77  ? 2.36712   -6.02662  9.04489   1.000 36.34224  ? 109  LYS A C   1 
ATOM   608  O  O   . LYS A 1 77  ? 2.91781   -6.16056  10.14554  1.000 32.85562  ? 109  LYS A O   1 
ATOM   609  C  CB  . LYS A 1 77  ? 2.38563   -7.83317  7.29857   1.000 36.18745  ? 109  LYS A CB  1 
ATOM   610  C  CG  . LYS A 1 77  ? 1.99982   -9.28085  7.01337   1.000 42.05978  ? 109  LYS A CG  1 
ATOM   611  C  CD  . LYS A 1 77  ? 3.14192   -10.06504 6.31362   1.000 47.20183  ? 109  LYS A CD  1 
ATOM   612  C  CE  . LYS A 1 77  ? 3.16808   -9.85734  4.84564   1.000 55.57713  ? 109  LYS A CE  1 
ATOM   613  N  NZ  . LYS A 1 77  ? 4.01941   -10.80237 4.07143   1.000 44.62242  ? 109  LYS A NZ  1 
ATOM   614  N  N   . HIS A 1 78  ? 2.44378   -4.88909  8.34644   1.000 33.20318  ? 110  HIS A N   1 
ATOM   615  C  CA  . HIS A 1 78  ? 3.18622   -3.75611  8.88186   1.000 36.02295  ? 110  HIS A CA  1 
ATOM   616  C  C   . HIS A 1 78  ? 2.54417   -3.19988  10.13867  1.000 30.88249  ? 110  HIS A C   1 
ATOM   617  O  O   . HIS A 1 78  ? 3.24626   -2.87450  11.09897  1.000 33.57331  ? 110  HIS A O   1 
ATOM   618  C  CB  . HIS A 1 78  ? 3.28185   -2.64456  7.84760   1.000 35.88920  ? 110  HIS A CB  1 
ATOM   619  C  CG  . HIS A 1 78  ? 4.33933   -2.86243  6.82331   1.000 32.77803  ? 110  HIS A CG  1 
ATOM   620  N  ND1 . HIS A 1 78  ? 5.45080   -2.05072  6.73516   1.000 42.16609  ? 110  HIS A ND1 1 
ATOM   621  C  CD2 . HIS A 1 78  ? 4.47078   -3.79340  5.84861   1.000 38.85515  ? 110  HIS A CD2 1 
ATOM   622  C  CE1 . HIS A 1 78  ? 6.22314   -2.47510  5.75051   1.000 49.05819  ? 110  HIS A CE1 1 
ATOM   623  N  NE2 . HIS A 1 78  ? 5.65151   -3.53135  5.19656   1.000 41.92282  ? 110  HIS A NE2 1 
ATOM   624  N  N   . ALA A 1 79  ? 1.21519   -3.07814  10.14511  1.000 29.15357  ? 111  ALA A N   1 
ATOM   625  C  CA  . ALA A 1 79  ? 0.52284   -2.55442  11.31837  1.000 29.12481  ? 111  ALA A CA  1 
ATOM   626  C  C   . ALA A 1 79  ? 0.74733   -3.43083  12.53419  1.000 33.65957  ? 111  ALA A C   1 
ATOM   627  O  O   . ALA A 1 79  ? 0.97585   -2.92347  13.64093  1.000 31.19068  ? 111  ALA A O   1 
ATOM   628  C  CB  . ALA A 1 79  ? -0.96810  -2.43225  11.03855  1.000 29.94997  ? 111  ALA A CB  1 
ATOM   629  N  N   . VAL A 1 80  ? 0.66120   -4.74729  12.35633  1.000 30.58350  ? 112  VAL A N   1 
ATOM   630  C  CA  . VAL A 1 80  ? 0.89625   -5.65986  13.47134  1.000 29.86524  ? 112  VAL A CA  1 
ATOM   631  C  C   . VAL A 1 80  ? 2.33380   -5.54077  13.95605  1.000 33.36466  ? 112  VAL A C   1 
ATOM   632  O  O   . VAL A 1 80  ? 2.60493   -5.53536  15.16532  1.000 33.53715  ? 112  VAL A O   1 
ATOM   633  C  CB  . VAL A 1 80  ? 0.53902   -7.09755  13.05115  1.000 30.70534  ? 112  VAL A CB  1 
ATOM   634  C  CG1 . VAL A 1 80  ? 1.11504   -8.12013  14.03480  1.000 34.39557  ? 112  VAL A CG1 1 
ATOM   635  C  CG2 . VAL A 1 80  ? -0.96078  -7.22108  12.94630  1.000 29.48212  ? 112  VAL A CG2 1 
ATOM   636  N  N   . SER A 1 81  ? 3.27784   -5.43288  13.02534  1.000 31.35862  ? 113  SER A N   1 
ATOM   637  C  CA  . SER A 1 81  ? 4.67275   -5.27222  13.41200  1.000 33.74976  ? 113  SER A CA  1 
ATOM   638  C  C   . SER A 1 81  ? 4.87805   -3.98112  14.19190  1.000 36.50853  ? 113  SER A C   1 
ATOM   639  O  O   . SER A 1 81  ? 5.59036   -3.96237  15.20241  1.000 37.07483  ? 113  SER A O   1 
ATOM   640  C  CB  . SER A 1 81  ? 5.56556   -5.29363  12.17114  1.000 41.46259  ? 113  SER A CB  1 
ATOM   641  O  OG  . SER A 1 81  ? 6.91598   -5.04991  12.52246  1.000 48.68267  ? 113  SER A OG  1 
ATOM   642  N  N   . GLU A 1 82  ? 4.25664   -2.89308  13.73557  1.000 32.22166  ? 114  GLU A N   1 
ATOM   643  C  CA  . GLU A 1 82  ? 4.42436   -1.60284  14.39799  1.000 37.00979  ? 114  GLU A CA  1 
ATOM   644  C  C   . GLU A 1 82  ? 3.81767   -1.61496  15.79363  1.000 35.11102  ? 114  GLU A C   1 
ATOM   645  O  O   . GLU A 1 82  ? 4.41920   -1.09684  16.74424  1.000 33.80136  ? 114  GLU A O   1 
ATOM   646  C  CB  . GLU A 1 82  ? 3.77996   -0.50296  13.56432  1.000 35.68858  ? 114  GLU A CB  1 
ATOM   647  C  CG  . GLU A 1 82  ? 4.56986   -0.10494  12.31868  1.000 37.58846  ? 114  GLU A CG  1 
ATOM   648  C  CD  . GLU A 1 82  ? 5.91693   0.51487   12.63979  1.000 54.52559  ? 114  GLU A CD  1 
ATOM   649  O  OE1 . GLU A 1 82  ? 5.97942   1.42939   13.49590  1.000 49.51429  ? 114  GLU A OE1 1 
ATOM   650  O  OE2 . GLU A 1 82  ? 6.91447   0.09363   12.01845  1.000 60.39161  ? 114  GLU A OE2 1 
ATOM   651  N  N   . GLY A 1 83  ? 2.61390   -2.17260  15.93154  1.000 31.72687  ? 115  GLY A N   1 
ATOM   652  C  CA  . GLY A 1 83  ? 1.98079   -2.20758  17.24409  1.000 27.86342  ? 115  GLY A CA  1 
ATOM   653  C  C   . GLY A 1 83  ? 2.73332   -3.09477  18.21210  1.000 31.89356  ? 115  GLY A C   1 
ATOM   654  O  O   . GLY A 1 83  ? 2.94019   -2.73303  19.37463  1.000 31.56864  ? 115  GLY A O   1 
ATOM   655  N  N   . THR A 1 84  ? 3.14758   -4.27390  17.74763  1.000 30.13257  ? 116  THR A N   1 
ATOM   656  C  CA  . THR A 1 84  ? 3.84833   -5.20644  18.62294  1.000 34.17362  ? 116  THR A CA  1 
ATOM   657  C  C   . THR A 1 84  ? 5.15930   -4.59995  19.10987  1.000 35.54332  ? 116  THR A C   1 
ATOM   658  O  O   . THR A 1 84  ? 5.49266   -4.68083  20.30380  1.000 35.48752  ? 116  THR A O   1 
ATOM   659  C  CB  . THR A 1 84  ? 4.07239   -6.52932  17.87736  1.000 34.26513  ? 116  THR A CB  1 
ATOM   660  O  OG1 . THR A 1 84  ? 2.79455   -7.06961  17.49204  1.000 34.23296  ? 116  THR A OG1 1 
ATOM   661  C  CG2 . THR A 1 84  ? 4.77509   -7.54455  18.76201  1.000 36.23252  ? 116  THR A CG2 1 
ATOM   662  N  N   . LYS A 1 85  ? 5.88918   -3.94637  18.20381  1.000 32.65751  ? 117  LYS A N   1 
ATOM   663  C  CA  . LYS A 1 85  ? 7.15082   -3.29578  18.55008  1.000 37.93671  ? 117  LYS A CA  1 
ATOM   664  C  C   . LYS A 1 85  ? 6.95095   -2.19799  19.58336  1.000 40.87995  ? 117  LYS A C   1 
ATOM   665  O  O   . LYS A 1 85  ? 7.71743   -2.09712  20.54927  1.000 39.55584  ? 117  LYS A O   1 
ATOM   666  C  CB  . LYS A 1 85  ? 7.77541   -2.68053  17.30061  1.000 41.47186  ? 117  LYS A CB  1 
ATOM   667  C  CG  . LYS A 1 85  ? 8.94517   -1.75817  17.61389  1.000 50.38791  ? 117  LYS A CG  1 
ATOM   668  C  CD  . LYS A 1 85  ? 9.42168   -0.94332  16.40755  1.000 60.76057  ? 117  LYS A CD  1 
ATOM   669  C  CE  . LYS A 1 85  ? 9.32018   -1.69738  15.09349  1.000 61.91419  ? 117  LYS A CE  1 
ATOM   670  N  NZ  . LYS A 1 85  ? 9.55370   -0.76426  13.94959  1.000 66.93992  ? 117  LYS A NZ  1 
ATOM   671  N  N   . ALA A 1 86  ? 5.91468   -1.37484  19.40504  1.000 36.16854  ? 118  ALA A N   1 
ATOM   672  C  CA  . ALA A 1 86  ? 5.68907   -0.27637  20.33557  1.000 33.32583  ? 118  ALA A CA  1 
ATOM   673  C  C   . ALA A 1 86  ? 5.34675   -0.79261  21.72390  1.000 35.77038  ? 118  ALA A C   1 
ATOM   674  O  O   . ALA A 1 86  ? 5.87675   -0.28617  22.71646  1.000 37.06641  ? 118  ALA A O   1 
ATOM   675  C  CB  . ALA A 1 86  ? 4.58620   0.64708   19.81710  1.000 32.99245  ? 118  ALA A CB  1 
ATOM   676  N  N   . VAL A 1 87  ? 4.48493   -1.81416  21.81520  1.000 31.89360  ? 119  VAL A N   1 
ATOM   677  C  CA  . VAL A 1 87  ? 4.10975   -2.34722  23.12456  1.000 34.77848  ? 119  VAL A CA  1 
ATOM   678  C  C   . VAL A 1 87  ? 5.30521   -2.99263  23.81152  1.000 39.46761  ? 119  VAL A C   1 
ATOM   679  O  O   . VAL A 1 87  ? 5.50634   -2.81660  25.01748  1.000 37.37726  ? 119  VAL A O   1 
ATOM   680  C  CB  . VAL A 1 87  ? 2.93146   -3.33163  22.99889  1.000 31.69229  ? 119  VAL A CB  1 
ATOM   681  C  CG1 . VAL A 1 87  ? 2.67421   -4.03048  24.33823  1.000 35.20390  ? 119  VAL A CG1 1 
ATOM   682  C  CG2 . VAL A 1 87  ? 1.69526   -2.60169  22.54688  1.000 30.64558  ? 119  VAL A CG2 1 
ATOM   683  N  N   . THR A 1 88  ? 6.11727   -3.74618  23.06615  1.000 35.37009  ? 120  THR A N   1 
ATOM   684  C  CA  . THR A 1 88  ? 7.29109   -4.37385  23.67281  1.000 38.17651  ? 120  THR A CA  1 
ATOM   685  C  C   . THR A 1 88  ? 8.24357   -3.32437  24.23319  1.000 42.51277  ? 120  THR A C   1 
ATOM   686  O  O   . THR A 1 88  ? 8.72722   -3.44815  25.36474  1.000 46.51036  ? 120  THR A O   1 
ATOM   687  C  CB  . THR A 1 88  ? 7.99675   -5.26543  22.65047  1.000 38.88095  ? 120  THR A CB  1 
ATOM   688  O  OG1 . THR A 1 88  ? 7.09600   -6.30553  22.24430  1.000 43.23748  ? 120  THR A OG1 1 
ATOM   689  C  CG2 . THR A 1 88  ? 9.23034   -5.91107  23.26674  1.000 45.67126  ? 120  THR A CG2 1 
ATOM   690  N  N   . LYS A 1 89  ? 8.51324   -2.27292  23.45527  1.000 39.56784  ? 121  LYS A N   1 
ATOM   691  C  CA  . LYS A 1 89  ? 9.38041   -1.19601  23.92710  1.000 45.25577  ? 121  LYS A CA  1 
ATOM   692  C  C   . LYS A 1 89  ? 8.77373   -0.47779  25.12888  1.000 47.51845  ? 121  LYS A C   1 
ATOM   693  O  O   . LYS A 1 89  ? 9.47961   -0.14727  26.08964  1.000 51.40141  ? 121  LYS A O   1 
ATOM   694  C  CB  . LYS A 1 89  ? 9.64244   -0.20595  22.78801  1.000 49.10603  ? 121  LYS A CB  1 
ATOM   695  C  CG  . LYS A 1 89  ? 10.80272  -0.60338  21.87498  1.000 56.89460  ? 121  LYS A CG  1 
ATOM   696  C  CD  . LYS A 1 89  ? 10.56070  -0.21943  20.41991  1.000 53.97442  ? 121  LYS A CD  1 
ATOM   697  C  CE  . LYS A 1 89  ? 10.43784  1.28143   20.22564  1.000 49.84779  ? 121  LYS A CE  1 
ATOM   698  N  NZ  . LYS A 1 89  ? 11.73935  1.96911   20.44417  1.000 60.09698  ? 121  LYS A NZ  1 
ATOM   699  N  N   . TYR A 1 90  ? 7.46911   -0.20910  25.08350  1.000 42.60683  ? 122  TYR A N   1 
ATOM   700  C  CA  . TYR A 1 90  ? 6.80550   0.52310   26.16198  1.000 41.05889  ? 122  TYR A CA  1 
ATOM   701  C  C   . TYR A 1 90  ? 6.76679   -0.26903  27.45790  1.000 42.45427  ? 122  TYR A C   1 
ATOM   702  O  O   . TYR A 1 90  ? 6.87288   0.31145   28.54256  1.000 47.12526  ? 122  TYR A O   1 
ATOM   703  C  CB  . TYR A 1 90  ? 5.39029   0.88890   25.72643  1.000 34.83179  ? 122  TYR A CB  1 
ATOM   704  C  CG  . TYR A 1 90  ? 4.56704   1.62736   26.74273  1.000 37.45498  ? 122  TYR A CG  1 
ATOM   705  C  CD1 . TYR A 1 90  ? 4.61565   3.01019   26.82939  1.000 39.34258  ? 122  TYR A CD1 1 
ATOM   706  C  CD2 . TYR A 1 90  ? 3.69806   0.94144   27.58615  1.000 38.26816  ? 122  TYR A CD2 1 
ATOM   707  C  CE1 . TYR A 1 90  ? 3.84755   3.68986   27.73596  1.000 39.15315  ? 122  TYR A CE1 1 
ATOM   708  C  CE2 . TYR A 1 90  ? 2.92143   1.61448   28.50210  1.000 37.26672  ? 122  TYR A CE2 1 
ATOM   709  C  CZ  . TYR A 1 90  ? 2.99998   2.98932   28.56611  1.000 42.52909  ? 122  TYR A CZ  1 
ATOM   710  O  OH  . TYR A 1 90  ? 2.23591   3.67591   29.47477  1.000 44.30043  ? 122  TYR A OH  1 
ATOM   711  N  N   . THR A 1 91  ? 6.64266   -1.58558  27.37881  1.000 44.51779  ? 123  THR A N   1 
ATOM   712  C  CA  . THR A 1 91  ? 6.45855   -2.38489  28.58424  1.000 50.95718  ? 123  THR A CA  1 
ATOM   713  C  C   . THR A 1 91  ? 7.81527   -2.56819  29.25246  1.000 56.73787  ? 123  THR A C   1 
ATOM   714  O  O   . THR A 1 91  ? 8.59608   -3.45538  28.91199  1.000 59.47092  ? 123  THR A O   1 
ATOM   715  C  CB  . THR A 1 91  ? 5.81056   -3.72162  28.24748  1.000 55.64820  ? 123  THR A CB  1 
ATOM   716  O  OG1 . THR A 1 91  ? 4.58946   -3.48977  27.53777  1.000 47.45784  ? 123  THR A OG1 1 
ATOM   717  C  CG2 . THR A 1 91  ? 5.50609   -4.49759  29.52213  1.000 65.46918  ? 123  THR A CG2 1 
ATOM   718  N  N   . SER A 1 92  ? 8.13624   -1.64138  30.15198  1.000 69.59639  ? 124  SER A N   1 
ATOM   719  C  CA  . SER A 1 92  ? 9.36261   -1.72599  30.92605  1.000 70.02570  ? 124  SER A CA  1 
ATOM   720  C  C   . SER A 1 92  ? 9.19630   -2.77422  32.01620  1.000 88.62339  ? 124  SER A C   1 
ATOM   721  O  O   . SER A 1 92  ? 8.09782   -2.98284  32.54041  1.000 88.28631  ? 124  SER A O   1 
ATOM   722  C  CB  . SER A 1 92  ? 9.73005   -0.37086  31.53255  1.000 70.70679  ? 124  SER A CB  1 
ATOM   723  O  OG  . SER A 1 92  ? 8.81093   0.02095   32.53278  1.000 70.84698  ? 124  SER A OG  1 
ATOM   724  N  N   . ALA A 1 93  ? 10.29991  -3.44151  32.35526  1.000 107.33118 ? 125  ALA A N   1 
ATOM   725  C  CA  . ALA A 1 93  ? 10.22734  -4.47802  33.37877  1.000 119.99029 ? 125  ALA A CA  1 
ATOM   726  C  C   . ALA A 1 93  ? 9.80570   -3.90175  34.72088  1.000 118.83290 ? 125  ALA A C   1 
ATOM   727  O  O   . ALA A 1 93  ? 9.11963   -4.57327  35.49994  1.000 119.27595 ? 125  ALA A O   1 
ATOM   728  C  CB  . ALA A 1 93  ? 11.57298  -5.19017  33.50930  1.000 121.08751 ? 125  ALA A CB  1 
ATOM   729  N  N   . LYS A 1 94  ? 10.21504  -2.67380  35.01320  1.000 107.15641 ? 126  LYS A N   1 
ATOM   730  C  CA  . LYS A 1 94  ? 9.84431   -2.00369  36.25102  1.000 98.41209  ? 126  LYS A CA  1 
ATOM   731  C  C   . LYS A 1 94  ? 8.51298   -1.27615  36.07324  1.000 90.08455  ? 126  LYS A C   1 
ATOM   732  O  O   . LYS A 1 94  ? 8.43626   -0.26449  35.36574  1.000 82.86116  ? 126  LYS A O   1 
ATOM   733  C  CB  . LYS A 1 94  ? 10.93820  -1.03576  36.67690  1.000 87.24007  ? 126  LYS A CB  1 
ATOM   734  C  CG  . LYS A 1 94  ? 10.71662  -0.54285  38.06578  1.000 96.79966  ? 126  LYS A CG  1 
ATOM   735  C  CD  . LYS A 1 94  ? 11.92127  -0.66070  38.93170  1.000 97.70512  ? 126  LYS A CD  1 
ATOM   736  C  CE  . LYS A 1 94  ? 11.66047  0.05806   40.24009  1.000 91.00841  ? 126  LYS A CE  1 
ATOM   737  N  NZ  . LYS A 1 94  ? 12.89782  0.40334   40.97389  1.000 85.10010  ? 126  LYS A NZ  1 
ATOM   738  N  N   . LYS A 1 95  ? 7.46390   -1.78700  36.71120  1.000 93.35411  ? 1014 LYS A N   1 
ATOM   739  C  CA  . LYS A 1 95  ? 6.15859   -1.14432  36.62941  1.000 94.78987  ? 1014 LYS A CA  1 
ATOM   740  C  C   . LYS A 1 95  ? 6.14947   0.14472   37.44829  1.000 86.81488  ? 1014 LYS A C   1 
ATOM   741  O  O   . LYS A 1 95  ? 6.85044   0.26561   38.45654  1.000 86.39598  ? 1014 LYS A O   1 
ATOM   742  C  CB  . LYS A 1 95  ? 5.05544   -2.08978  37.10074  1.000 97.40231  ? 1014 LYS A CB  1 
ATOM   743  C  CG  . LYS A 1 95  ? 3.65301   -1.57420  36.80429  1.000 89.78527  ? 1014 LYS A CG  1 
ATOM   744  C  CD  . LYS A 1 95  ? 3.54043   -1.07108  35.36764  1.000 86.07752  ? 1014 LYS A CD  1 
ATOM   745  C  CE  . LYS A 1 95  ? 2.29737   -0.21186  35.18026  1.000 93.77011  ? 1014 LYS A CE  1 
ATOM   746  N  NZ  . LYS A 1 95  ? 2.09001   0.21886   33.76278  1.000 92.35684  ? 1014 LYS A NZ  1 
ATOM   747  N  N   . ALA A 1 96  ? 5.35908   1.11622   36.98124  1.000 79.52513  ? 1015 ALA A N   1 
ATOM   748  C  CA  . ALA A 1 96  ? 5.14630   2.46297   37.52078  1.000 77.73437  ? 1015 ALA A CA  1 
ATOM   749  C  C   . ALA A 1 96  ? 6.26461   3.37507   37.03462  1.000 68.98750  ? 1015 ALA A C   1 
ATOM   750  O  O   . ALA A 1 96  ? 6.29457   4.56976   37.39350  1.000 61.78276  ? 1015 ALA A O   1 
ATOM   751  C  CB  . ALA A 1 96  ? 5.06452   2.53087   39.05478  1.000 82.96213  ? 1015 ALA A CB  1 
ATOM   752  N  N   . LYS A 1 97  ? 7.21870   2.83222   36.27831  1.000 57.21167  ? 1016 LYS A N   1 
ATOM   753  C  CA  . LYS A 1 97  ? 8.28868   3.56885   35.61977  1.000 53.60666  ? 1016 LYS A CA  1 
ATOM   754  C  C   . LYS A 1 97  ? 8.02820   3.74548   34.12341  1.000 48.69314  ? 1016 LYS A C   1 
ATOM   755  O  O   . LYS A 1 97  ? 8.94776   4.09999   33.38099  1.000 45.14893  ? 1016 LYS A O   1 
ATOM   756  C  CB  . LYS A 1 97  ? 9.63670   2.89643   35.86961  1.000 57.64713  ? 1016 LYS A CB  1 
ATOM   757  C  CG  . LYS A 1 97  ? 10.00313  2.96964   37.34493  1.000 56.82679  ? 1016 LYS A CG  1 
ATOM   758  C  CD  . LYS A 1 97  ? 10.25331  4.42136   37.76593  1.000 56.87965  ? 1016 LYS A CD  1 
ATOM   759  C  CE  . LYS A 1 97  ? 10.48557  4.52621   39.27112  1.000 57.64531  ? 1016 LYS A CE  1 
ATOM   760  N  NZ  . LYS A 1 97  ? 11.37973  3.43302   39.76954  1.000 68.75379  ? 1016 LYS A NZ  1 
ATOM   761  N  N   . THR A 1 98  ? 6.82772   3.42939   33.64484  1.000 45.13869  ? 1017 THR A N   1 
ATOM   762  C  CA  . THR A 1 98  ? 6.57295   3.59525   32.22155  1.000 36.97411  ? 1017 THR A CA  1 
ATOM   763  C  C   . THR A 1 98  ? 6.69767   5.06396   31.81458  1.000 37.75767  ? 1017 THR A C   1 
ATOM   764  O  O   . THR A 1 98  ? 6.42593   5.98050   32.59368  1.000 44.66401  ? 1017 THR A O   1 
ATOM   765  C  CB  . THR A 1 98  ? 5.18217   3.06363   31.85222  1.000 51.53303  ? 1017 THR A CB  1 
ATOM   766  O  OG1 . THR A 1 98  ? 4.18848   4.00681   32.25377  1.000 56.80152  ? 1017 THR A OG1 1 
ATOM   767  C  CG2 . THR A 1 98  ? 4.91824   1.72619   32.53708  1.000 54.00981  ? 1017 THR A CG2 1 
ATOM   768  N  N   . ARG A 1 99  ? 7.13332   5.27315   30.57326  1.000 43.82826  ? 1018 ARG A N   1 
ATOM   769  C  CA  . ARG A 1 99  ? 7.18259   6.58036   29.92992  1.000 38.74551  ? 1018 ARG A CA  1 
ATOM   770  C  C   . ARG A 1 99  ? 6.62721   6.40220   28.52718  1.000 39.42625  ? 1018 ARG A C   1 
ATOM   771  O  O   . ARG A 1 99  ? 7.02451   5.47164   27.82283  1.000 36.14949  ? 1018 ARG A O   1 
ATOM   772  C  CB  . ARG A 1 99  ? 8.61043   7.16436   29.83319  1.000 36.91423  ? 1018 ARG A CB  1 
ATOM   773  C  CG  . ARG A 1 99  ? 9.33748   7.36185   31.17200  1.000 39.55113  ? 1018 ARG A CG  1 
ATOM   774  C  CD  . ARG A 1 99  ? 10.83131  7.84326   31.05481  1.000 41.79586  ? 1018 ARG A CD  1 
ATOM   775  N  NE  . ARG A 1 99  ? 11.68686  6.84589   30.41823  1.000 46.23599  ? 1018 ARG A NE  1 
ATOM   776  C  CZ  . ARG A 1 99  ? 12.21929  6.96583   29.20638  1.000 47.08492  ? 1018 ARG A CZ  1 
ATOM   777  N  NH1 . ARG A 1 99  ? 12.02930  8.04964   28.46519  1.000 40.80656  ? 1018 ARG A NH1 1 
ATOM   778  N  NH2 . ARG A 1 99  ? 12.96031  5.97119   28.72362  1.000 41.98936  ? 1018 ARG A NH2 1 
ATOM   779  N  N   . SER A 1 100 ? 5.73312   7.30246   28.10817  1.000 41.43634  ? 1019 SER A N   1 
ATOM   780  C  CA  . SER A 1 100 ? 5.19064   7.21040   26.75211  1.000 38.81111  ? 1019 SER A CA  1 
ATOM   781  C  C   . SER A 1 100 ? 6.30107   7.27836   25.71856  1.000 40.64022  ? 1019 SER A C   1 
ATOM   782  O  O   . SER A 1 100 ? 6.23515   6.59392   24.69019  1.000 37.89194  ? 1019 SER A O   1 
ATOM   783  C  CB  . SER A 1 100 ? 4.17032   8.32145   26.50862  1.000 49.35116  ? 1019 SER A CB  1 
ATOM   784  O  OG  . SER A 1 100 ? 3.03769   8.11746   27.33348  1.000 49.29707  ? 1019 SER A OG  1 
ATOM   785  N  N   . SER A 1 101 ? 7.36670   8.02559   26.02117  1.000 37.81116  ? 1020 SER A N   1 
ATOM   786  C  CA  . SER A 1 101 ? 8.46655   8.21348   25.08380  1.000 38.28115  ? 1020 SER A CA  1 
ATOM   787  C  C   . SER A 1 101 ? 9.13408   6.89366   24.71749  1.000 42.31798  ? 1020 SER A C   1 
ATOM   788  O  O   . SER A 1 101 ? 9.70052   6.77192   23.62311  1.000 40.88804  ? 1020 SER A O   1 
ATOM   789  C  CB  . SER A 1 101 ? 9.47850   9.17535   25.72136  1.000 40.81641  ? 1020 SER A CB  1 
ATOM   790  O  OG  . SER A 1 101 ? 10.71117  9.23608   25.02224  1.000 46.28960  ? 1020 SER A OG  1 
ATOM   791  N  N   . ARG A 1 102 ? 8.98938   5.87130   25.55370  1.000 35.99337  ? 1021 ARG A N   1 
ATOM   792  C  CA  . ARG A 1 102 ? 9.58642   4.57913   25.24465  1.000 39.10323  ? 1021 ARG A CA  1 
ATOM   793  C  C   . ARG A 1 102 ? 8.90769   3.91608   24.05528  1.000 45.03427  ? 1021 ARG A C   1 
ATOM   794  O  O   . ARG A 1 102 ? 9.52669   3.08878   23.37745  1.000 43.09293  ? 1021 ARG A O   1 
ATOM   795  C  CB  . ARG A 1 102 ? 9.54176   3.66717   26.46153  1.000 41.79211  ? 1021 ARG A CB  1 
ATOM   796  C  CG  . ARG A 1 102 ? 10.59297  4.02378   27.49035  1.000 39.26506  ? 1021 ARG A CG  1 
ATOM   797  C  CD  . ARG A 1 102 ? 10.47152  3.13227   28.70452  1.000 47.74824  ? 1021 ARG A CD  1 
ATOM   798  N  NE  . ARG A 1 102 ? 10.65700  1.72707   28.36400  1.000 48.73186  ? 1021 ARG A NE  1 
ATOM   799  C  CZ  . ARG A 1 102 ? 11.55526  0.93588   28.93524  1.000 50.80432  ? 1021 ARG A CZ  1 
ATOM   800  N  NH1 . ARG A 1 102 ? 12.33968  1.37045   29.90524  1.000 49.24266  ? 1021 ARG A NH1 1 
ATOM   801  N  NH2 . ARG A 1 102 ? 11.65453  -0.32864  28.53546  1.000 56.84291  ? 1021 ARG A NH2 1 
ATOM   802  N  N   . ALA A 1 103 ? 7.63769   4.23393   23.80571  1.000 38.59832  ? 1022 ALA A N   1 
ATOM   803  C  CA  . ALA A 1 103 ? 6.94111   3.60120   22.69166  1.000 39.55813  ? 1022 ALA A CA  1 
ATOM   804  C  C   . ALA A 1 103 ? 7.48110   4.04768   21.34022  1.000 42.49720  ? 1022 ALA A C   1 
ATOM   805  O  O   . ALA A 1 103 ? 7.16766   3.40991   20.32723  1.000 41.21043  ? 1022 ALA A O   1 
ATOM   806  C  CB  . ALA A 1 103 ? 5.44991   3.90591   22.76911  1.000 35.92236  ? 1022 ALA A CB  1 
ATOM   807  N  N   . GLY A 1 104 ? 8.28863   5.10423   21.30808  1.000 41.35118  ? 1023 GLY A N   1 
ATOM   808  C  CA  . GLY A 1 104 ? 8.90989   5.58070   20.08506  1.000 41.82297  ? 1023 GLY A CA  1 
ATOM   809  C  C   . GLY A 1 104 ? 7.98966   6.23962   19.08027  1.000 41.11758  ? 1023 GLY A C   1 
ATOM   810  O  O   . GLY A 1 104 ? 8.32857   6.27578   17.89161  1.000 46.16919  ? 1023 GLY A O   1 
ATOM   811  N  N   . LEU A 1 105 ? 6.85086   6.78328   19.51029  1.000 39.24613  ? 1024 LEU A N   1 
ATOM   812  C  CA  . LEU A 1 105 ? 5.80508   7.25623   18.60864  1.000 41.35923  ? 1024 LEU A CA  1 
ATOM   813  C  C   . LEU A 1 105 ? 5.65592   8.77298   18.61843  1.000 43.61676  ? 1024 LEU A C   1 
ATOM   814  O  O   . LEU A 1 105 ? 6.06039   9.45974   19.55598  1.000 45.75181  ? 1024 LEU A O   1 
ATOM   815  C  CB  . LEU A 1 105 ? 4.45124   6.65662   18.98706  1.000 38.15131  ? 1024 LEU A CB  1 
ATOM   816  C  CG  . LEU A 1 105 ? 4.31453   5.13849   19.10547  1.000 36.65775  ? 1024 LEU A CG  1 
ATOM   817  C  CD1 . LEU A 1 105 ? 2.91466   4.78465   19.56115  1.000 37.74682  ? 1024 LEU A CD1 1 
ATOM   818  C  CD2 . LEU A 1 105 ? 4.63349   4.44736   17.78525  1.000 36.31419  ? 1024 LEU A CD2 1 
ATOM   819  N  N   . GLN A 1 106 ? 5.01293   9.28369   17.56228  1.000 43.71082  ? 1025 GLN A N   1 
ATOM   820  C  CA  . GLN A 1 106 ? 4.55417   10.66946  17.47174  1.000 45.60896  ? 1025 GLN A CA  1 
ATOM   821  C  C   . GLN A 1 106 ? 3.11313   10.81683  17.94674  1.000 44.94250  ? 1025 GLN A C   1 
ATOM   822  O  O   . GLN A 1 106 ? 2.75618   11.83893  18.53962  1.000 46.03410  ? 1025 GLN A O   1 
ATOM   823  C  CB  . GLN A 1 106 ? 4.63152   11.18146  16.02686  1.000 47.79598  ? 1025 GLN A CB  1 
ATOM   824  C  CG  . GLN A 1 106 ? 5.97637   11.04500  15.34187  1.000 50.86143  ? 1025 GLN A CG  1 
ATOM   825  C  CD  . GLN A 1 106 ? 7.09166   11.75580  16.05567  1.000 56.08757  ? 1025 GLN A CD  1 
ATOM   826  O  OE1 . GLN A 1 106 ? 6.98574   12.94009  16.38143  1.000 58.50853  ? 1025 GLN A OE1 1 
ATOM   827  N  NE2 . GLN A 1 106 ? 8.17474   11.03416  16.31357  1.000 58.36667  ? 1025 GLN A NE2 1 
ATOM   828  N  N   . PHE A 1 107 ? 2.27347   9.81698   17.68004  1.000 43.57982  ? 1026 PHE A N   1 
ATOM   829  C  CA  . PHE A 1 107 ? 0.88785   9.85172   18.11879  1.000 40.15016  ? 1026 PHE A CA  1 
ATOM   830  C  C   . PHE A 1 107 ? 0.79665   9.70909   19.63725  1.000 43.45131  ? 1026 PHE A C   1 
ATOM   831  O  O   . PHE A 1 107 ? 1.64686   9.06977   20.26155  1.000 45.64420  ? 1026 PHE A O   1 
ATOM   832  C  CB  . PHE A 1 107 ? 0.07951   8.76717   17.40036  1.000 35.92914  ? 1026 PHE A CB  1 
ATOM   833  C  CG  . PHE A 1 107 ? -0.49923  9.24935   16.08953  1.000 39.78424  ? 1026 PHE A CG  1 
ATOM   834  C  CD1 . PHE A 1 107 ? 0.32030   9.81514   15.12840  1.000 40.34617  ? 1026 PHE A CD1 1 
ATOM   835  C  CD2 . PHE A 1 107 ? -1.85856  9.15312   15.83084  1.000 41.98842  ? 1026 PHE A CD2 1 
ATOM   836  C  CE1 . PHE A 1 107 ? -0.20814  10.28765  13.93408  1.000 42.64578  ? 1026 PHE A CE1 1 
ATOM   837  C  CE2 . PHE A 1 107 ? -2.39075  9.60666   14.62927  1.000 41.25442  ? 1026 PHE A CE2 1 
ATOM   838  C  CZ  . PHE A 1 107 ? -1.56415  10.17434  13.68408  1.000 38.04185  ? 1026 PHE A CZ  1 
ATOM   839  N  N   . PRO A 1 108 ? -0.17835  10.36657  20.26671  1.000 41.58928  ? 1027 PRO A N   1 
ATOM   840  C  CA  . PRO A 1 108 ? -0.18901  10.47415  21.73377  1.000 44.84788  ? 1027 PRO A CA  1 
ATOM   841  C  C   . PRO A 1 108 ? -0.78719  9.25303   22.40301  1.000 44.17462  ? 1027 PRO A C   1 
ATOM   842  O  O   . PRO A 1 108 ? -2.01009  9.03349   22.35929  1.000 44.36844  ? 1027 PRO A O   1 
ATOM   843  C  CB  . PRO A 1 108 ? -1.03806  11.72579  21.97676  1.000 48.24603  ? 1027 PRO A CB  1 
ATOM   844  C  CG  . PRO A 1 108 ? -1.98469  11.74136  20.81467  1.000 46.98111  ? 1027 PRO A CG  1 
ATOM   845  C  CD  . PRO A 1 108 ? -1.25259  11.16006  19.64266  1.000 44.92094  ? 1027 PRO A CD  1 
ATOM   846  N  N   . VAL A 1 109 ? 0.04218   8.51644   23.14022  1.000 41.70487  ? 1028 VAL A N   1 
ATOM   847  C  CA  . VAL A 1 109 ? -0.41217  7.33032   23.85570  1.000 40.93968  ? 1028 VAL A CA  1 
ATOM   848  C  C   . VAL A 1 109 ? -1.46435  7.69860   24.90023  1.000 39.19468  ? 1028 VAL A C   1 
ATOM   849  O  O   . VAL A 1 109 ? -2.51711  7.05398   25.00289  1.000 37.17931  ? 1028 VAL A O   1 
ATOM   850  C  CB  . VAL A 1 109 ? 0.79266   6.61748   24.49566  1.000 39.87586  ? 1028 VAL A CB  1 
ATOM   851  C  CG1 . VAL A 1 109 ? 0.33692   5.53730   25.45070  1.000 42.85321  ? 1028 VAL A CG1 1 
ATOM   852  C  CG2 . VAL A 1 109 ? 1.70719   6.05070   23.40375  1.000 40.59372  ? 1028 VAL A CG2 1 
ATOM   853  N  N   . GLY A 1 110 ? -1.20423  8.75419   25.67812  1.000 39.65606  ? 1029 GLY A N   1 
ATOM   854  C  CA  . GLY A 1 110 ? -2.12231  9.11531   26.74883  1.000 41.12203  ? 1029 GLY A CA  1 
ATOM   855  C  C   . GLY A 1 110 ? -3.47582  9.56950   26.23595  1.000 46.95360  ? 1029 GLY A C   1 
ATOM   856  O  O   . GLY A 1 110 ? -4.51369  9.21500   26.80161  1.000 43.95819  ? 1029 GLY A O   1 
ATOM   857  N  N   . ARG A 1 111 ? -3.48205  10.33141  25.13840  1.000 36.81994  ? 1030 ARG A N   1 
ATOM   858  C  CA  . ARG A 1 111 ? -4.72703  10.76981  24.52239  1.000 42.61835  ? 1030 ARG A CA  1 
ATOM   859  C  C   . ARG A 1 111 ? -5.53772  9.57476   24.02917  1.000 40.95534  ? 1030 ARG A C   1 
ATOM   860  O  O   . ARG A 1 111 ? -6.74897  9.48888   24.26256  1.000 41.48261  ? 1030 ARG A O   1 
ATOM   861  C  CB  . ARG A 1 111 ? -4.39229  11.71581  23.36805  1.000 49.68665  ? 1030 ARG A CB  1 
ATOM   862  C  CG  . ARG A 1 111 ? -5.49608  12.01724  22.38251  1.000 61.50207  ? 1030 ARG A CG  1 
ATOM   863  C  CD  . ARG A 1 111 ? -6.18643  13.31589  22.73907  1.000 69.72179  ? 1030 ARG A CD  1 
ATOM   864  N  NE  . ARG A 1 111 ? -5.22824  14.41480  22.82020  1.000 78.30490  ? 1030 ARG A NE  1 
ATOM   865  C  CZ  . ARG A 1 111 ? -5.04147  15.32352  21.87117  1.000 78.40897  ? 1030 ARG A CZ  1 
ATOM   866  N  NH1 . ARG A 1 111 ? -5.70452  15.27384  20.72561  1.000 71.86803  ? 1030 ARG A NH1 1 
ATOM   867  N  NH2 . ARG A 1 111 ? -4.15885  16.30076  22.07218  1.000 69.88663  ? 1030 ARG A NH2 1 
ATOM   868  N  N   . VAL A 1 112 ? -4.87430  8.62637   23.37274  1.000 38.18802  ? 1031 VAL A N   1 
ATOM   869  C  CA  . VAL A 1 112 ? -5.56784  7.43906   22.87756  1.000 35.38180  ? 1031 VAL A CA  1 
ATOM   870  C  C   . VAL A 1 112 ? -6.11510  6.61992   24.03968  1.000 40.46631  ? 1031 VAL A C   1 
ATOM   871  O  O   . VAL A 1 112 ? -7.21548  6.05938   23.95890  1.000 36.39430  ? 1031 VAL A O   1 
ATOM   872  C  CB  . VAL A 1 112 ? -4.63328  6.62490   21.96853  1.000 33.80391  ? 1031 VAL A CB  1 
ATOM   873  C  CG1 . VAL A 1 112 ? -5.27429  5.30840   21.56217  1.000 32.18100  ? 1031 VAL A CG1 1 
ATOM   874  C  CG2 . VAL A 1 112 ? -4.31481  7.45398   20.71669  1.000 40.20439  ? 1031 VAL A CG2 1 
ATOM   875  N  N   . HIS A 1 113 ? -5.36753  6.55149   25.14545  1.000 37.00921  ? 1032 HIS A N   1 
ATOM   876  C  CA  . HIS A 1 113 ? -5.86581  5.84159   26.31914  1.000 40.04289  ? 1032 HIS A CA  1 
ATOM   877  C  C   . HIS A 1 113 ? -7.14641  6.48314   26.84282  1.000 40.50752  ? 1032 HIS A C   1 
ATOM   878  O  O   . HIS A 1 113 ? -8.12568  5.78675   27.13913  1.000 39.55803  ? 1032 HIS A O   1 
ATOM   879  C  CB  . HIS A 1 113 ? -4.79590  5.80170   27.41390  1.000 36.18913  ? 1032 HIS A CB  1 
ATOM   880  C  CG  . HIS A 1 113 ? -4.96859  4.66654   28.37088  1.000 36.67818  ? 1032 HIS A CG  1 
ATOM   881  N  ND1 . HIS A 1 113 ? -4.07437  4.39949   29.38510  1.000 40.15366  ? 1032 HIS A ND1 1 
ATOM   882  C  CD2 . HIS A 1 113 ? -5.92322  3.70703   28.44764  1.000 39.52746  ? 1032 HIS A CD2 1 
ATOM   883  C  CE1 . HIS A 1 113 ? -4.47248  3.32816   30.04850  1.000 47.12749  ? 1032 HIS A CE1 1 
ATOM   884  N  NE2 . HIS A 1 113 ? -5.59019  2.88621   29.49702  1.000 41.77860  ? 1032 HIS A NE2 1 
ATOM   885  N  N   . ARG A 1 114 ? -7.15552  7.81736   26.96329  1.000 41.36589  ? 1033 ARG A N   1 
ATOM   886  C  CA  . ARG A 1 114 ? -8.33237  8.51236   27.47128  1.000 41.24613  ? 1033 ARG A CA  1 
ATOM   887  C  C   . ARG A 1 114 ? -9.53503  8.30438   26.55923  1.000 40.89619  ? 1033 ARG A C   1 
ATOM   888  O  O   . ARG A 1 114 ? -10.65697 8.12741   27.03981  1.000 43.48927  ? 1033 ARG A O   1 
ATOM   889  C  CB  . ARG A 1 114 ? -8.03655  10.00747  27.61672  1.000 46.40101  ? 1033 ARG A CB  1 
ATOM   890  C  CG  . ARG A 1 114 ? -9.17946  10.80943  28.19739  1.000 60.45031  ? 1033 ARG A CG  1 
ATOM   891  C  CD  . ARG A 1 114 ? -8.79075  12.27543  28.36371  1.000 69.38390  ? 1033 ARG A CD  1 
ATOM   892  N  NE  . ARG A 1 114 ? -8.47630  12.88389  27.07585  1.000 75.22568  ? 1033 ARG A NE  1 
ATOM   893  C  CZ  . ARG A 1 114 ? -9.38895  13.36443  26.24126  1.000 88.98453  ? 1033 ARG A CZ  1 
ATOM   894  N  NH1 . ARG A 1 114 ? -10.67998 13.31536  26.52947  1.000 86.33782  ? 1033 ARG A NH1 1 
ATOM   895  N  NH2 . ARG A 1 114 ? -8.99781  13.89205  25.08292  1.000 80.75782  ? 1033 ARG A NH2 1 
ATOM   896  N  N   . LEU A 1 115 ? -9.32357  8.32635   25.24053  1.000 40.84551  ? 1034 LEU A N   1 
ATOM   897  C  CA  . LEU A 1 115 ? -10.43539 8.11107   24.31672  1.000 43.80721  ? 1034 LEU A CA  1 
ATOM   898  C  C   . LEU A 1 115 ? -10.95430 6.67573   24.37874  1.000 44.10444  ? 1034 LEU A C   1 
ATOM   899  O  O   . LEU A 1 115 ? -12.16453 6.44318   24.25781  1.000 39.99090  ? 1034 LEU A O   1 
ATOM   900  C  CB  . LEU A 1 115 ? -10.02344 8.46698   22.89015  1.000 45.89331  ? 1034 LEU A CB  1 
ATOM   901  C  CG  . LEU A 1 115 ? -9.71110  9.94634   22.65623  1.000 56.99038  ? 1034 LEU A CG  1 
ATOM   902  C  CD1 . LEU A 1 115 ? -9.05742  10.14724  21.30455  1.000 53.27583  ? 1034 LEU A CD1 1 
ATOM   903  C  CD2 . LEU A 1 115 ? -10.96638 10.80472  22.80954  1.000 59.61490  ? 1034 LEU A CD2 1 
ATOM   904  N  N   . LEU A 1 116 ? -10.05851 5.69578   24.53247  1.000 39.91184  ? 1035 LEU A N   1 
ATOM   905  C  CA  . LEU A 1 116 ? -10.51736 4.32088   24.69916  1.000 38.02900  ? 1035 LEU A CA  1 
ATOM   906  C  C   . LEU A 1 116 ? -11.33203 4.18037   25.96982  1.000 38.44137  ? 1035 LEU A C   1 
ATOM   907  O  O   . LEU A 1 116 ? -12.38110 3.53056   25.98153  1.000 37.86117  ? 1035 LEU A O   1 
ATOM   908  C  CB  . LEU A 1 116 ? -9.33059  3.35860   24.72741  1.000 33.82970  ? 1035 LEU A CB  1 
ATOM   909  C  CG  . LEU A 1 116 ? -8.68860  3.03564   23.37290  1.000 34.75305  ? 1035 LEU A CG  1 
ATOM   910  C  CD1 . LEU A 1 116 ? -7.39424  2.28074   23.57158  1.000 34.46123  ? 1035 LEU A CD1 1 
ATOM   911  C  CD2 . LEU A 1 116 ? -9.64703  2.25919   22.48543  1.000 32.48909  ? 1035 LEU A CD2 1 
ATOM   912  N  N   . ARG A 1 117 ? -10.87025 4.80337   27.05201  1.000 38.09048  ? 1036 ARG A N   1 
ATOM   913  C  CA  . ARG A 1 117 ? -11.62632 4.76660   28.29267  1.000 43.03047  ? 1036 ARG A CA  1 
ATOM   914  C  C   . ARG A 1 117 ? -12.97540 5.47022   28.13999  1.000 47.02388  ? 1036 ARG A C   1 
ATOM   915  O  O   . ARG A 1 117 ? -13.99157 4.98243   28.64594  1.000 50.72655  ? 1036 ARG A O   1 
ATOM   916  C  CB  . ARG A 1 117 ? -10.76370 5.37423   29.40420  1.000 43.94111  ? 1036 ARG A CB  1 
ATOM   917  C  CG  . ARG A 1 117 ? -9.99483  4.30218   30.19365  1.000 45.67920  ? 1036 ARG A CG  1 
ATOM   918  C  CD  . ARG A 1 117 ? -8.88955  4.86635   31.10366  1.000 51.69166  ? 1036 ARG A CD  1 
ATOM   919  N  NE  . ARG A 1 117 ? -7.96815  3.79688   31.48218  1.000 54.27739  ? 1036 ARG A NE  1 
ATOM   920  C  CZ  . ARG A 1 117 ? -6.88686  3.94502   32.23814  1.000 53.59249  ? 1036 ARG A CZ  1 
ATOM   921  N  NH1 . ARG A 1 117 ? -6.45237  5.13685   32.59672  1.000 51.60801  ? 1036 ARG A NH1 1 
ATOM   922  N  NH2 . ARG A 1 117 ? -6.22220  2.86468   32.64040  1.000 55.62628  ? 1036 ARG A NH2 1 
ATOM   923  N  N   . LYS A 1 118 ? -13.01105 6.60276   27.42037  1.000 47.08405  ? 1037 LYS A N   1 
ATOM   924  C  CA  . LYS A 1 118 ? -14.25313 7.36561   27.25847  1.000 51.21159  ? 1037 LYS A CA  1 
ATOM   925  C  C   . LYS A 1 118 ? -15.29848 6.58762   26.46999  1.000 52.27878  ? 1037 LYS A C   1 
ATOM   926  O  O   . LYS A 1 118 ? -16.50173 6.77095   26.68087  1.000 46.68732  ? 1037 LYS A O   1 
ATOM   927  C  CB  . LYS A 1 118 ? -13.99419 8.69915   26.54516  1.000 52.95031  ? 1037 LYS A CB  1 
ATOM   928  C  CG  . LYS A 1 118 ? -15.15946 9.71107   26.60447  1.000 60.71203  ? 1037 LYS A CG  1 
ATOM   929  C  CD  . LYS A 1 118 ? -14.81854 11.04481  25.93695  1.000 64.82197  ? 1037 LYS A CD  1 
ATOM   930  C  CE  . LYS A 1 118 ? -14.23427 10.82573  24.53944  1.000 67.23495  ? 1037 LYS A CE  1 
ATOM   931  N  NZ  . LYS A 1 118 ? -15.17172 10.27477  23.51275  1.000 67.18001  ? 1037 LYS A NZ  1 
ATOM   932  N  N   . GLY A 1 119 ? -14.86523 5.71255   25.56515  1.000 47.00454  ? 1038 GLY A N   1 
ATOM   933  C  CA  . GLY A 1 119 ? -15.78231 5.02264   24.67623  1.000 46.07995  ? 1038 GLY A CA  1 
ATOM   934  C  C   . GLY A 1 119 ? -16.51309 3.85458   25.26742  1.000 44.35933  ? 1038 GLY A C   1 
ATOM   935  O  O   . GLY A 1 119 ? -17.37044 3.27913   24.58999  1.000 47.59129  ? 1038 GLY A O   1 
ATOM   936  N  N   . ASN A 1 120 ? -16.18693 3.48261   26.50762  1.000 45.37829  ? 1039 ASN A N   1 
ATOM   937  C  CA  . ASN A 1 120 ? -16.84899 2.37941   27.22011  1.000 43.83377  ? 1039 ASN A CA  1 
ATOM   938  C  C   . ASN A 1 120 ? -16.87027 1.11064   26.36860  1.000 44.82990  ? 1039 ASN A C   1 
ATOM   939  O  O   . ASN A 1 120 ? -17.88696 0.42661   26.23934  1.000 46.53955  ? 1039 ASN A O   1 
ATOM   940  C  CB  . ASN A 1 120 ? -18.26066 2.77382   27.65223  1.000 54.02018  ? 1039 ASN A CB  1 
ATOM   941  C  CG  . ASN A 1 120 ? -18.26752 3.99224   28.55301  1.000 60.80828  ? 1039 ASN A CG  1 
ATOM   942  O  OD1 . ASN A 1 120 ? -17.48006 4.08172   29.50287  1.000 64.98871  ? 1039 ASN A OD1 1 
ATOM   943  N  ND2 . ASN A 1 120 ? -19.17139 4.92263   28.28408  1.000 65.57031  ? 1039 ASN A ND2 1 
ATOM   944  N  N   . TYR A 1 121 ? -15.72527 0.81670   25.76487  1.000 38.93539  ? 1040 TYR A N   1 
ATOM   945  C  CA  . TYR A 1 121 ? -15.55811 -0.40327  24.98204  1.000 33.08727  ? 1040 TYR A CA  1 
ATOM   946  C  C   . TYR A 1 121 ? -15.40898 -1.63835  25.85917  1.000 37.61771  ? 1040 TYR A C   1 
ATOM   947  O  O   . TYR A 1 121 ? -15.66321 -2.75676  25.39491  1.000 35.59733  ? 1040 TYR A O   1 
ATOM   948  C  CB  . TYR A 1 121 ? -14.33262 -0.25028  24.09115  1.000 35.83347  ? 1040 TYR A CB  1 
ATOM   949  C  CG  . TYR A 1 121 ? -14.44096 0.90574   23.11901  1.000 33.09314  ? 1040 TYR A CG  1 
ATOM   950  C  CD1 . TYR A 1 121 ? -15.30167 0.84918   22.03437  1.000 34.98919  ? 1040 TYR A CD1 1 
ATOM   951  C  CD2 . TYR A 1 121 ? -13.67460 2.05041   23.28546  1.000 36.07266  ? 1040 TYR A CD2 1 
ATOM   952  C  CE1 . TYR A 1 121 ? -15.39978 1.91242   21.14195  1.000 38.63070  ? 1040 TYR A CE1 1 
ATOM   953  C  CE2 . TYR A 1 121 ? -13.76713 3.11592   22.40117  1.000 37.50872  ? 1040 TYR A CE2 1 
ATOM   954  C  CZ  . TYR A 1 121 ? -14.63016 3.03647   21.33393  1.000 42.55209  ? 1040 TYR A CZ  1 
ATOM   955  O  OH  . TYR A 1 121 ? -14.72461 4.08752   20.45796  1.000 47.31522  ? 1040 TYR A OH  1 
ATOM   956  N  N   . ALA A 1 122 ? -14.99802 -1.45527  27.11195  1.000 38.40097  ? 1041 ALA A N   1 
ATOM   957  C  CA  . ALA A 1 122 ? -14.89398 -2.52211  28.09471  1.000 34.16257  ? 1041 ALA A CA  1 
ATOM   958  C  C   . ALA A 1 122 ? -14.82721 -1.86635  29.46393  1.000 42.24329  ? 1041 ALA A C   1 
ATOM   959  O  O   . ALA A 1 122 ? -14.67762 -0.64595  29.58041  1.000 39.96655  ? 1041 ALA A O   1 
ATOM   960  C  CB  . ALA A 1 122 ? -13.66425 -3.40461  27.87523  1.000 34.85270  ? 1041 ALA A CB  1 
ATOM   961  N  N   . GLU A 1 123 ? -14.91350 -2.69917  30.50259  1.000 39.80436  ? 1042 GLU A N   1 
ATOM   962  C  CA  . GLU A 1 123 ? -14.82726 -2.17387  31.86314  1.000 39.27284  ? 1042 GLU A CA  1 
ATOM   963  C  C   . GLU A 1 123 ? -13.49789 -1.47599  32.10428  1.000 43.51021  ? 1042 GLU A C   1 
ATOM   964  O  O   . GLU A 1 123 ? -13.45602 -0.40518  32.72312  1.000 45.50986  ? 1042 GLU A O   1 
ATOM   965  C  CB  . GLU A 1 123 ? -14.99272 -3.29001  32.88563  1.000 45.20908  ? 1042 GLU A CB  1 
ATOM   966  C  CG  . GLU A 1 123 ? -16.40249 -3.59000  33.29589  1.000 64.19708  ? 1042 GLU A CG  1 
ATOM   967  C  CD  . GLU A 1 123 ? -16.43803 -4.56123  34.45556  1.000 77.14974  ? 1042 GLU A CD  1 
ATOM   968  O  OE1 . GLU A 1 123 ? -15.46564 -4.54245  35.24973  1.000 80.70504  ? 1042 GLU A OE1 1 
ATOM   969  O  OE2 . GLU A 1 123 ? -17.41627 -5.32332  34.57784  1.000 81.82188  ? 1042 GLU A OE2 1 
ATOM   970  N  N   . ARG A 1 124 ? -12.40321 -2.06455  31.62685  1.000 40.16430  ? 1043 ARG A N   1 
ATOM   971  C  CA  . ARG A 1 124 ? -11.07693 -1.50669  31.83223  1.000 42.88410  ? 1043 ARG A CA  1 
ATOM   972  C  C   . ARG A 1 124 ? -10.29686 -1.57823  30.52894  1.000 38.52771  ? 1043 ARG A C   1 
ATOM   973  O  O   . ARG A 1 124 ? -10.58121 -2.40878  29.65751  1.000 35.50818  ? 1043 ARG A O   1 
ATOM   974  C  CB  . ARG A 1 124 ? -10.31984 -2.22994  32.96330  1.000 47.37607  ? 1043 ARG A CB  1 
ATOM   975  C  CG  . ARG A 1 124 ? -10.95697 -2.05007  34.35280  1.000 50.80468  ? 1043 ARG A CG  1 
ATOM   976  C  CD  . ARG A 1 124 ? -10.38164 -3.02282  35.37249  1.000 61.18146  ? 1043 ARG A CD  1 
ATOM   977  N  NE  . ARG A 1 124 ? -9.00018  -3.32946  35.02778  1.000 77.12970  ? 1043 ARG A NE  1 
ATOM   978  C  CZ  . ARG A 1 124 ? -8.52215  -4.55413  34.85807  1.000 73.75394  ? 1043 ARG A CZ  1 
ATOM   979  N  NH1 . ARG A 1 124 ? -9.26160  -5.62524  35.10541  1.000 79.02410  ? 1043 ARG A NH1 1 
ATOM   980  N  NH2 . ARG A 1 124 ? -7.28342  -4.70873  34.39390  1.000 62.01137  ? 1043 ARG A NH2 1 
ATOM   981  N  N   . VAL A 1 125 ? -9.32111  -0.68231  30.39817  1.000 39.54191  ? 1044 VAL A N   1 
ATOM   982  C  CA  . VAL A 1 125 ? -8.42344  -0.64823  29.25102  1.000 34.13438  ? 1044 VAL A CA  1 
ATOM   983  C  C   . VAL A 1 125 ? -6.99463  -0.75633  29.76172  1.000 39.22382  ? 1044 VAL A C   1 
ATOM   984  O  O   . VAL A 1 125 ? -6.52809  0.11554   30.50917  1.000 40.35462  ? 1044 VAL A O   1 
ATOM   985  C  CB  . VAL A 1 125 ? -8.60090  0.63256   28.42375  1.000 36.23842  ? 1044 VAL A CB  1 
ATOM   986  C  CG1 . VAL A 1 125 ? -7.60049  0.65086   27.26794  1.000 39.67981  ? 1044 VAL A CG1 1 
ATOM   987  C  CG2 . VAL A 1 125 ? -10.03111 0.74236   27.90782  1.000 42.58042  ? 1044 VAL A CG2 1 
ATOM   988  N  N   . GLY A 1 126 ? -6.30053  -1.80853  29.35028  1.000 35.00158  ? 1045 GLY A N   1 
ATOM   989  C  CA  . GLY A 1 126 ? -4.92030  -1.97932  29.74572  1.000 37.21181  ? 1045 GLY A CA  1 
ATOM   990  C  C   . GLY A 1 126 ? -4.00396  -1.00305  29.03994  1.000 39.89964  ? 1045 GLY A C   1 
ATOM   991  O  O   . GLY A 1 126 ? -4.30698  -0.49770  27.95825  1.000 37.22937  ? 1045 GLY A O   1 
ATOM   992  N  N   . ALA A 1 127 ? -2.84555  -0.75619  29.66468  1.000 40.44575  ? 1046 ALA A N   1 
ATOM   993  C  CA  . ALA A 1 127 ? -1.91156  0.25139   29.16915  1.000 40.95463  ? 1046 ALA A CA  1 
ATOM   994  C  C   . ALA A 1 127 ? -1.32531  -0.10954  27.81205  1.000 41.03552  ? 1046 ALA A C   1 
ATOM   995  O  O   . ALA A 1 127 ? -0.89185  0.79031   27.08264  1.000 45.81617  ? 1046 ALA A O   1 
ATOM   996  C  CB  . ALA A 1 127 ? -0.78096  0.47274   30.17968  1.000 45.54248  ? 1046 ALA A CB  1 
ATOM   997  N  N   . GLY A 1 128 ? -1.31090  -1.39395  27.44597  1.000 36.16721  ? 1047 GLY A N   1 
ATOM   998  C  CA  . GLY A 1 128 ? -0.77793  -1.77289  26.14818  1.000 36.10879  ? 1047 GLY A CA  1 
ATOM   999  C  C   . GLY A 1 128 ? -1.71035  -1.48136  24.99216  1.000 33.36631  ? 1047 GLY A C   1 
ATOM   1000 O  O   . GLY A 1 128 ? -1.24911  -1.30376  23.86169  1.000 34.81623  ? 1047 GLY A O   1 
ATOM   1001 N  N   . ALA A 1 129 ? -3.02003  -1.42421  25.24494  1.000 32.29488  ? 1048 ALA A N   1 
ATOM   1002 C  CA  . ALA A 1 129 ? -3.96454  -1.20171  24.15078  1.000 32.11104  ? 1048 ALA A CA  1 
ATOM   1003 C  C   . ALA A 1 129 ? -3.76631  0.14877   23.48133  1.000 32.14009  ? 1048 ALA A C   1 
ATOM   1004 O  O   . ALA A 1 129 ? -3.68510  0.18746   22.24103  1.000 29.95040  ? 1048 ALA A O   1 
ATOM   1005 C  CB  . ALA A 1 129 ? -5.40220  -1.35865  24.65052  1.000 32.90267  ? 1048 ALA A CB  1 
ATOM   1006 N  N   . PRO A 1 130 ? -3.67381  1.27860   24.20323  1.000 32.95606  ? 1049 PRO A N   1 
ATOM   1007 C  CA  . PRO A 1 130 ? -3.47044  2.55141   23.49094  1.000 29.14919  ? 1049 PRO A CA  1 
ATOM   1008 C  C   . PRO A 1 130 ? -2.11288  2.65565   22.82402  1.000 33.70691  ? 1049 PRO A C   1 
ATOM   1009 O  O   . PRO A 1 130 ? -1.97470  3.38008   21.83133  1.000 29.92712  ? 1049 PRO A O   1 
ATOM   1010 C  CB  . PRO A 1 130 ? -3.64016  3.61217   24.58895  1.000 31.61216  ? 1049 PRO A CB  1 
ATOM   1011 C  CG  . PRO A 1 130 ? -3.27236  2.89420   25.85784  1.000 32.10059  ? 1049 PRO A CG  1 
ATOM   1012 C  CD  . PRO A 1 130 ? -3.75611  1.48176   25.66523  1.000 34.05369  ? 1049 PRO A CD  1 
ATOM   1013 N  N   . VAL A 1 131 ? -1.08778  1.99310   23.35884  1.000 29.59745  ? 1050 VAL A N   1 
ATOM   1014 C  CA  . VAL A 1 131 ? 0.21664   2.01340   22.70556  1.000 29.00847  ? 1050 VAL A CA  1 
ATOM   1015 C  C   . VAL A 1 131 ? 0.13671   1.33086   21.35000  1.000 31.73205  ? 1050 VAL A C   1 
ATOM   1016 O  O   . VAL A 1 131 ? 0.60083   1.86364   20.33838  1.000 30.21410  ? 1050 VAL A O   1 
ATOM   1017 C  CB  . VAL A 1 131 ? 1.27207   1.34016   23.59507  1.000 30.67912  ? 1050 VAL A CB  1 
ATOM   1018 C  CG1 . VAL A 1 131 ? 2.59400   1.29294   22.86110  1.000 33.42667  ? 1050 VAL A CG1 1 
ATOM   1019 C  CG2 . VAL A 1 131 ? 1.40649   2.11573   24.93253  1.000 33.89740  ? 1050 VAL A CG2 1 
ATOM   1020 N  N   . TYR A 1 132 ? -0.43027  0.12475   21.32336  1.000 28.89893  ? 1051 TYR A N   1 
ATOM   1021 C  CA  . TYR A 1 132 ? -0.58639  -0.60432  20.06575  1.000 28.12471  ? 1051 TYR A CA  1 
ATOM   1022 C  C   . TYR A 1 132 ? -1.44406  0.19254   19.09341  1.000 27.81958  ? 1051 TYR A C   1 
ATOM   1023 O  O   . TYR A 1 132 ? -1.08742  0.36043   17.92101  1.000 28.79386  ? 1051 TYR A O   1 
ATOM   1024 C  CB  . TYR A 1 132 ? -1.22434  -1.96116  20.35613  1.000 25.78125  ? 1051 TYR A CB  1 
ATOM   1025 C  CG  . TYR A 1 132 ? -1.08296  -3.01739  19.27476  1.000 26.01005  ? 1051 TYR A CG  1 
ATOM   1026 C  CD1 . TYR A 1 132 ? -1.76017  -2.90310  18.06238  1.000 29.45383  ? 1051 TYR A CD1 1 
ATOM   1027 C  CD2 . TYR A 1 132 ? -0.27187  -4.12141  19.47160  1.000 27.31866  ? 1051 TYR A CD2 1 
ATOM   1028 C  CE1 . TYR A 1 132 ? -1.65388  -3.88246  17.09706  1.000 29.22850  ? 1051 TYR A CE1 1 
ATOM   1029 C  CE2 . TYR A 1 132 ? -0.14077  -5.10586  18.49771  1.000 28.31064  ? 1051 TYR A CE2 1 
ATOM   1030 C  CZ  . TYR A 1 132 ? -0.83274  -4.97301  17.30726  1.000 27.57492  ? 1051 TYR A CZ  1 
ATOM   1031 O  OH  . TYR A 1 132 ? -0.72075  -5.94754  16.32531  1.000 28.86213  ? 1051 TYR A OH  1 
ATOM   1032 N  N   . LEU A 1 133 ? -2.57273  0.71978   19.57173  1.000 26.88657  ? 1052 LEU A N   1 
ATOM   1033 C  CA  . LEU A 1 133 ? -3.46600  1.43310   18.65645  1.000 26.52246  ? 1052 LEU A CA  1 
ATOM   1034 C  C   . LEU A 1 133 ? -2.83428  2.72250   18.14834  1.000 31.68812  ? 1052 LEU A C   1 
ATOM   1035 O  O   . LEU A 1 133 ? -2.92602  3.03104   16.95490  1.000 27.96733  ? 1052 LEU A O   1 
ATOM   1036 C  CB  . LEU A 1 133 ? -4.79813  1.71643   19.34365  1.000 28.61724  ? 1052 LEU A CB  1 
ATOM   1037 C  CG  . LEU A 1 133 ? -5.86896  2.44756   18.53665  1.000 29.16867  ? 1052 LEU A CG  1 
ATOM   1038 C  CD1 . LEU A 1 133 ? -6.08487  1.72445   17.20411  1.000 30.54734  ? 1052 LEU A CD1 1 
ATOM   1039 C  CD2 . LEU A 1 133 ? -7.16497  2.54284   19.31138  1.000 31.95990  ? 1052 LEU A CD2 1 
ATOM   1040 N  N   . ALA A 1 134 ? -2.16409  3.48223   19.01977  1.000 29.85343  ? 1053 ALA A N   1 
ATOM   1041 C  CA  . ALA A 1 134 ? -1.49692  4.68589   18.52806  1.000 30.17647  ? 1053 ALA A CA  1 
ATOM   1042 C  C   . ALA A 1 134 ? -0.48237  4.34202   17.44662  1.000 30.33883  ? 1053 ALA A C   1 
ATOM   1043 O  O   . ALA A 1 134 ? -0.36771  5.06259   16.45106  1.000 32.40715  ? 1053 ALA A O   1 
ATOM   1044 C  CB  . ALA A 1 134 ? -0.82428  5.45340   19.67588  1.000 31.80008  ? 1053 ALA A CB  1 
ATOM   1045 N  N   . ALA A 1 135 ? 0.24901   3.23140   17.60845  1.000 29.87125  ? 1054 ALA A N   1 
ATOM   1046 C  CA  . ALA A 1 135 ? 1.25336   2.86597   16.61211  1.000 29.77310  ? 1054 ALA A CA  1 
ATOM   1047 C  C   . ALA A 1 135 ? 0.60369   2.53960   15.27528  1.000 30.02084  ? 1054 ALA A C   1 
ATOM   1048 O  O   . ALA A 1 135 ? 1.13719   2.88303   14.21573  1.000 30.92049  ? 1054 ALA A O   1 
ATOM   1049 C  CB  . ALA A 1 135 ? 2.08451   1.67421   17.09675  1.000 28.70335  ? 1054 ALA A CB  1 
ATOM   1050 N  N   . VAL A 1 136 ? -0.54698  1.86810   15.31135  1.000 27.87734  ? 1055 VAL A N   1 
ATOM   1051 C  CA  . VAL A 1 136 ? -1.24410  1.53350   14.07270  1.000 27.51153  ? 1055 VAL A CA  1 
ATOM   1052 C  C   . VAL A 1 136 ? -1.76701  2.79101   13.39557  1.000 28.89823  ? 1055 VAL A C   1 
ATOM   1053 O  O   . VAL A 1 136 ? -1.62732  2.95121   12.17741  1.000 29.81576  ? 1055 VAL A O   1 
ATOM   1054 C  CB  . VAL A 1 136 ? -2.36939  0.51868   14.34869  1.000 28.67587  ? 1055 VAL A CB  1 
ATOM   1055 C  CG1 . VAL A 1 136 ? -3.23626  0.31420   13.08994  1.000 27.60503  ? 1055 VAL A CG1 1 
ATOM   1056 C  CG2 . VAL A 1 136 ? -1.76778  -0.83399  14.73522  1.000 29.93857  ? 1055 VAL A CG2 1 
ATOM   1057 N  N   . LEU A 1 137 ? -2.37615  3.69910   14.16739  1.000 29.44636  ? 1056 LEU A N   1 
ATOM   1058 C  CA  . LEU A 1 137 ? -2.87904  4.93926   13.58068  1.000 31.41183  ? 1056 LEU A CA  1 
ATOM   1059 C  C   . LEU A 1 137 ? -1.74539  5.74715   12.97521  1.000 32.34286  ? 1056 LEU A C   1 
ATOM   1060 O  O   . LEU A 1 137 ? -1.89840  6.31568   11.89424  1.000 30.53514  ? 1056 LEU A O   1 
ATOM   1061 C  CB  . LEU A 1 137 ? -3.60543  5.77557   14.63380  1.000 32.17165  ? 1056 LEU A CB  1 
ATOM   1062 C  CG  . LEU A 1 137 ? -4.82984  5.10707   15.25207  1.000 31.25745  ? 1056 LEU A CG  1 
ATOM   1063 C  CD1 . LEU A 1 137 ? -5.38826  5.96383   16.37819  1.000 30.88871  ? 1056 LEU A CD1 1 
ATOM   1064 C  CD2 . LEU A 1 137 ? -5.90821  4.79342   14.20864  1.000 31.55460  ? 1056 LEU A CD2 1 
ATOM   1065 N  N   . GLU A 1 138 ? -0.59563  5.80034   13.65406  1.000 33.50319  ? 1057 GLU A N   1 
ATOM   1066 C  CA  . GLU A 1 138 ? 0.55492   6.51693   13.10526  1.000 36.57591  ? 1057 GLU A CA  1 
ATOM   1067 C  C   . GLU A 1 138 ? 1.06591   5.85221   11.83171  1.000 34.98171  ? 1057 GLU A C   1 
ATOM   1068 O  O   . GLU A 1 138 ? 1.37928   6.53382   10.84944  1.000 33.89665  ? 1057 GLU A O   1 
ATOM   1069 C  CB  . GLU A 1 138 ? 1.67312   6.58686   14.14891  1.000 34.57119  ? 1057 GLU A CB  1 
ATOM   1070 C  CG  . GLU A 1 138 ? 2.97577   7.19091   13.63561  1.000 37.65145  ? 1057 GLU A CG  1 
ATOM   1071 C  CD  . GLU A 1 138 ? 3.92365   7.57370   14.75727  1.000 43.38938  ? 1057 GLU A CD  1 
ATOM   1072 O  OE1 . GLU A 1 138 ? 3.44782   7.76945   15.89303  1.000 47.30726  ? 1057 GLU A OE1 1 
ATOM   1073 O  OE2 . GLU A 1 138 ? 5.14243   7.66587   14.50601  1.000 46.10384  ? 1057 GLU A OE2 1 
ATOM   1074 N  N   . TYR A 1 139 ? 1.14504   4.51890   11.82159  1.000 33.79067  ? 1058 TYR A N   1 
ATOM   1075 C  CA  . TYR A 1 139 ? 1.64012   3.82473   10.63924  1.000 33.75313  ? 1058 TYR A CA  1 
ATOM   1076 C  C   . TYR A 1 139 ? 0.75202   4.08748   9.42543   1.000 34.10129  ? 1058 TYR A C   1 
ATOM   1077 O  O   . TYR A 1 139 ? 1.25196   4.36465   8.32519   1.000 32.17388  ? 1058 TYR A O   1 
ATOM   1078 C  CB  . TYR A 1 139 ? 1.75040   2.31588   10.91042  1.000 32.94142  ? 1058 TYR A CB  1 
ATOM   1079 C  CG  . TYR A 1 139 ? 1.78134   1.53819   9.62273   1.000 35.32708  ? 1058 TYR A CG  1 
ATOM   1080 C  CD1 . TYR A 1 139 ? 2.87285   1.62778   8.77141   1.000 38.14597  ? 1058 TYR A CD1 1 
ATOM   1081 C  CD2 . TYR A 1 139 ? 0.70971   0.73313   9.24311   1.000 32.67041  ? 1058 TYR A CD2 1 
ATOM   1082 C  CE1 . TYR A 1 139 ? 2.89961   0.94538   7.56219   1.000 38.31197  ? 1058 TYR A CE1 1 
ATOM   1083 C  CE2 . TYR A 1 139 ? 0.72868   0.03433   8.03998   1.000 31.30495  ? 1058 TYR A CE2 1 
ATOM   1084 C  CZ  . TYR A 1 139 ? 1.81897   0.14849   7.20425   1.000 33.04072  ? 1058 TYR A CZ  1 
ATOM   1085 O  OH  . TYR A 1 139 ? 1.84748   -0.52189  5.99236   1.000 36.33276  ? 1058 TYR A OH  1 
ATOM   1086 N  N   . LEU A 1 140 ? -0.56655  4.01277   9.60631   1.000 31.33324  ? 1059 LEU A N   1 
ATOM   1087 C  CA  . LEU A 1 140 ? -1.47605  4.26781   8.49659   1.000 31.24276  ? 1059 LEU A CA  1 
ATOM   1088 C  C   . LEU A 1 140 ? -1.34767  5.70771   8.03164   1.000 34.22878  ? 1059 LEU A C   1 
ATOM   1089 O  O   . LEU A 1 140 ? -1.39539  5.99190   6.83051   1.000 34.19220  ? 1059 LEU A O   1 
ATOM   1090 C  CB  . LEU A 1 140 ? -2.91436  3.96576   8.91347   1.000 29.80071  ? 1059 LEU A CB  1 
ATOM   1091 C  CG  . LEU A 1 140 ? -3.22406  2.48685   9.17341   1.000 32.65613  ? 1059 LEU A CG  1 
ATOM   1092 C  CD1 . LEU A 1 140 ? -4.61469  2.34738   9.77313   1.000 34.38150  ? 1059 LEU A CD1 1 
ATOM   1093 C  CD2 . LEU A 1 140 ? -3.11638  1.67277   7.87258   1.000 31.19051  ? 1059 LEU A CD2 1 
ATOM   1094 N  N   . THR A 1 141 ? -1.18448  6.63305   8.97721   1.000 35.60487  ? 1060 THR A N   1 
ATOM   1095 C  CA  . THR A 1 141 ? -0.97380  8.02223   8.60573   1.000 34.01940  ? 1060 THR A CA  1 
ATOM   1096 C  C   . THR A 1 141 ? 0.28627   8.16489   7.76698   1.000 38.53695  ? 1060 THR A C   1 
ATOM   1097 O  O   . THR A 1 141 ? 0.28758   8.86748   6.75137   1.000 40.42667  ? 1060 THR A O   1 
ATOM   1098 C  CB  . THR A 1 141 ? -0.89671  8.89079   9.86659   1.000 36.61940  ? 1060 THR A CB  1 
ATOM   1099 O  OG1 . THR A 1 141 ? -2.16106  8.85577   10.53369  1.000 37.81989  ? 1060 THR A OG1 1 
ATOM   1100 C  CG2 . THR A 1 141 ? -0.53716  10.32405  9.52712   1.000 40.60399  ? 1060 THR A CG2 1 
ATOM   1101 N  N   . ALA A 1 142 ? 1.36396   7.48304   8.16475   1.000 33.76016  ? 1061 ALA A N   1 
ATOM   1102 C  CA  . ALA A 1 142 ? 2.60698   7.57144   7.41051   1.000 40.68508  ? 1061 ALA A CA  1 
ATOM   1103 C  C   . ALA A 1 142 ? 2.42738   7.02731   5.99751   1.000 39.03523  ? 1061 ALA A C   1 
ATOM   1104 O  O   . ALA A 1 142 ? 2.91933   7.62119   5.03270   1.000 42.74352  ? 1061 ALA A O   1 
ATOM   1105 C  CB  . ALA A 1 142 ? 3.72664   6.83731   8.15270   1.000 37.37017  ? 1061 ALA A CB  1 
ATOM   1106 N  N   . GLU A 1 143 ? 1.68541   5.92370   5.84810   1.000 40.24204  ? 1062 GLU A N   1 
ATOM   1107 C  CA  . GLU A 1 143 ? 1.46250   5.36973   4.51430   1.000 42.31664  ? 1062 GLU A CA  1 
ATOM   1108 C  C   . GLU A 1 143 ? 0.68571   6.34942   3.64030   1.000 43.19574  ? 1062 GLU A C   1 
ATOM   1109 O  O   . GLU A 1 143 ? 1.07681   6.62858   2.50005   1.000 39.37262  ? 1062 GLU A O   1 
ATOM   1110 C  CB  . GLU A 1 143 ? 0.70917   4.03693   4.60792   1.000 36.20124  ? 1062 GLU A CB  1 
ATOM   1111 C  CG  . GLU A 1 143 ? 1.54359   2.84816   5.06700   1.000 36.92094  ? 1062 GLU A CG  1 
ATOM   1112 C  CD  . GLU A 1 143 ? 2.33650   2.20999   3.93250   1.000 40.92252  ? 1062 GLU A CD  1 
ATOM   1113 O  OE1 . GLU A 1 143 ? 2.23700   2.69440   2.78729   1.000 40.08300  ? 1062 GLU A OE1 1 
ATOM   1114 O  OE2 . GLU A 1 143 ? 3.05320   1.21901   4.18590   1.000 40.54854  ? 1062 GLU A OE2 1 
ATOM   1115 N  N   . ILE A 1 144 ? -0.41812  6.88899   4.16214   1.000 39.97268  ? 1063 ILE A N   1 
ATOM   1116 C  CA  . ILE A 1 144 ? -1.23710  7.79820   3.36224   1.000 39.00939  ? 1063 ILE A CA  1 
ATOM   1117 C  C   . ILE A 1 144 ? -0.46763  9.06825   3.02856   1.000 40.77026  ? 1063 ILE A C   1 
ATOM   1118 O  O   . ILE A 1 144 ? -0.46298  9.52475   1.87888   1.000 45.28136  ? 1063 ILE A O   1 
ATOM   1119 C  CB  . ILE A 1 144 ? -2.56482  8.10136   4.07502   1.000 35.47751  ? 1063 ILE A CB  1 
ATOM   1120 C  CG1 . ILE A 1 144 ? -3.38358  6.80946   4.17319   1.000 37.93163  ? 1063 ILE A CG1 1 
ATOM   1121 C  CG2 . ILE A 1 144 ? -3.33724  9.18270   3.32272   1.000 39.07088  ? 1063 ILE A CG2 1 
ATOM   1122 C  CD1 . ILE A 1 144 ? -4.47277  6.85924   5.18962   1.000 44.61075  ? 1063 ILE A CD1 1 
ATOM   1123 N  N   . LEU A 1 145 ? 0.21099   9.64687   4.01741   1.000 40.95938  ? 1064 LEU A N   1 
ATOM   1124 C  CA  . LEU A 1 145 ? 0.92977   10.88964  3.75620   1.000 43.57375  ? 1064 LEU A CA  1 
ATOM   1125 C  C   . LEU A 1 145 ? 2.08451   10.66847  2.79122   1.000 46.77795  ? 1064 LEU A C   1 
ATOM   1126 O  O   . LEU A 1 145 ? 2.38518   11.54953  1.97957   1.000 50.11993  ? 1064 LEU A O   1 
ATOM   1127 C  CB  . LEU A 1 145 ? 1.42811   11.51017  5.06373   1.000 45.57006  ? 1064 LEU A CB  1 
ATOM   1128 C  CG  . LEU A 1 145 ? 0.33774   12.07435  5.98057   1.000 48.28122  ? 1064 LEU A CG  1 
ATOM   1129 C  CD1 . LEU A 1 145 ? 0.94211   12.67253  7.26293   1.000 45.83474  ? 1064 LEU A CD1 1 
ATOM   1130 C  CD2 . LEU A 1 145 ? -0.51035  13.09478  5.25458   1.000 48.21656  ? 1064 LEU A CD2 1 
ATOM   1131 N  N   . GLU A 1 146 ? 2.74447   9.51007   2.85858   1.000 48.61754  ? 1065 GLU A N   1 
ATOM   1132 C  CA  . GLU A 1 146 ? 3.78677   9.21015   1.87959   1.000 53.03434  ? 1065 GLU A CA  1 
ATOM   1133 C  C   . GLU A 1 146 ? 3.23019   9.22728   0.46369   1.000 53.43376  ? 1065 GLU A C   1 
ATOM   1134 O  O   . GLU A 1 146 ? 3.77105   9.89515   -0.42577  1.000 56.20615  ? 1065 GLU A O   1 
ATOM   1135 C  CB  . GLU A 1 146 ? 4.40624   7.84230   2.15750   1.000 50.34684  ? 1065 GLU A CB  1 
ATOM   1136 C  CG  . GLU A 1 146 ? 5.39665   7.42586   1.07644   1.000 57.12135  ? 1065 GLU A CG  1 
ATOM   1137 C  CD  . GLU A 1 146 ? 5.99771   6.05713   1.31459   1.000 63.36353  ? 1065 GLU A CD  1 
ATOM   1138 O  OE1 . GLU A 1 146 ? 6.92819   5.92684   2.13764   1.000 62.25258  ? 1065 GLU A OE1 1 
ATOM   1139 O  OE2 . GLU A 1 146 ? 5.51863   5.10467   0.66891   1.000 57.23971  ? 1065 GLU A OE2 1 
ATOM   1140 N  N   . LEU A 1 147 ? 2.15111   8.47795   0.23345   1.000 52.32025  ? 1066 LEU A N   1 
ATOM   1141 C  CA  . LEU A 1 147 ? 1.60112   8.35422   -1.11283  1.000 48.25308  ? 1066 LEU A CA  1 
ATOM   1142 C  C   . LEU A 1 147 ? 0.98407   9.66594   -1.58435  1.000 53.61524  ? 1066 LEU A C   1 
ATOM   1143 O  O   . LEU A 1 147 ? 1.15379   10.05645  -2.74317  1.000 52.78263  ? 1066 LEU A O   1 
ATOM   1144 C  CB  . LEU A 1 147 ? 0.58281   7.21832   -1.14342  1.000 48.46033  ? 1066 LEU A CB  1 
ATOM   1145 C  CG  . LEU A 1 147 ? 1.22137   5.86278   -0.82209  1.000 46.90681  ? 1066 LEU A CG  1 
ATOM   1146 C  CD1 . LEU A 1 147 ? 0.14915   4.81394   -0.59754  1.000 49.71109  ? 1066 LEU A CD1 1 
ATOM   1147 C  CD2 . LEU A 1 147 ? 2.16506   5.43976   -1.94225  1.000 57.16052  ? 1066 LEU A CD2 1 
ATOM   1148 N  N   . ALA A 1 148 ? 0.27217   10.36052  -0.69781  1.000 51.92906  ? 1067 ALA A N   1 
ATOM   1149 C  CA  . ALA A 1 148 ? -0.30953  11.64706  -1.05656  1.000 54.95360  ? 1067 ALA A CA  1 
ATOM   1150 C  C   . ALA A 1 148 ? 0.77887   12.66639  -1.36984  1.000 57.97745  ? 1067 ALA A C   1 
ATOM   1151 O  O   . ALA A 1 148 ? 0.65309   13.45597  -2.31663  1.000 60.55072  ? 1067 ALA A O   1 
ATOM   1152 C  CB  . ALA A 1 148 ? -1.20894  12.13723  0.07713   1.000 50.47705  ? 1067 ALA A CB  1 
ATOM   1153 N  N   . GLY A 1 149 ? 1.86114   12.65764  -0.58946  1.000 57.87636  ? 1068 GLY A N   1 
ATOM   1154 C  CA  . GLY A 1 149 ? 2.97321   13.54629  -0.87607  1.000 60.81289  ? 1068 GLY A CA  1 
ATOM   1155 C  C   . GLY A 1 149 ? 3.65944   13.21473  -2.18710  1.000 62.92707  ? 1068 GLY A C   1 
ATOM   1156 O  O   . GLY A 1 149 ? 4.12756   14.11088  -2.89738  1.000 67.47028  ? 1068 GLY A O   1 
ATOM   1157 N  N   . ASN A 1 150 ? 3.74547   11.92487  -2.52141  1.000 62.12909  ? 1069 ASN A N   1 
ATOM   1158 C  CA  . ASN A 1 150 ? 4.24713   11.54595  -3.83857  1.000 68.06833  ? 1069 ASN A CA  1 
ATOM   1159 C  C   . ASN A 1 150 ? 3.33195   12.07091  -4.93288  1.000 70.83795  ? 1069 ASN A C   1 
ATOM   1160 O  O   . ASN A 1 150 ? 3.80074   12.54941  -5.97211  1.000 75.38647  ? 1069 ASN A O   1 
ATOM   1161 C  CB  . ASN A 1 150 ? 4.38756   10.02671  -3.95090  1.000 65.86652  ? 1069 ASN A CB  1 
ATOM   1162 C  CG  . ASN A 1 150 ? 5.42928   9.46290   -3.01093  1.000 65.16774  ? 1069 ASN A CG  1 
ATOM   1163 O  OD1 . ASN A 1 150 ? 6.22437   10.19963  -2.42885  1.000 69.28830  ? 1069 ASN A OD1 1 
ATOM   1164 N  ND2 . ASN A 1 150 ? 5.45010   8.14200   -2.87881  1.000 61.90434  ? 1069 ASN A ND2 1 
ATOM   1165 N  N   . ALA A 1 151 ? 2.01806   11.97690  -4.71905  1.000 67.01602  ? 1070 ALA A N   1 
ATOM   1166 C  CA  . ALA A 1 151 ? 1.06832   12.48680  -5.70003  1.000 67.58218  ? 1070 ALA A CA  1 
ATOM   1167 C  C   . ALA A 1 151 ? 1.20408   13.99560  -5.86479  1.000 72.55579  ? 1070 ALA A C   1 
ATOM   1168 O  O   . ALA A 1 151 ? 1.09063   14.51826  -6.98022  1.000 70.90899  ? 1070 ALA A O   1 
ATOM   1169 C  CB  . ALA A 1 151 ? -0.35539  12.10762  -5.29370  1.000 68.82953  ? 1070 ALA A CB  1 
ATOM   1170 N  N   . ALA A 1 152 ? 1.41817   14.71648  -4.76108  1.000 66.11188  ? 1071 ALA A N   1 
ATOM   1171 C  CA  . ALA A 1 152 ? 1.65665   16.15350  -4.85583  1.000 71.40293  ? 1071 ALA A CA  1 
ATOM   1172 C  C   . ALA A 1 152 ? 2.94271   16.45074  -5.61916  1.000 78.05467  ? 1071 ALA A C   1 
ATOM   1173 O  O   . ALA A 1 152 ? 2.97339   17.33969  -6.47977  1.000 78.15308  ? 1071 ALA A O   1 
ATOM   1174 C  CB  . ALA A 1 152 ? 1.70287   16.77259  -3.45962  1.000 71.11834  ? 1071 ALA A CB  1 
ATOM   1175 N  N   . ARG A 1 153 ? 4.01940   15.72210  -5.30925  1.000 77.98743  ? 1072 ARG A N   1 
ATOM   1176 C  CA  . ARG A 1 153 ? 5.29397   15.94324  -5.98765  1.000 82.19999  ? 1072 ARG A CA  1 
ATOM   1177 C  C   . ARG A 1 153 ? 5.18461   15.65364  -7.47920  1.000 85.46851  ? 1072 ARG A C   1 
ATOM   1178 O  O   . ARG A 1 153 ? 5.71102   16.40838  -8.30664  1.000 91.29695  ? 1072 ARG A O   1 
ATOM   1179 C  CB  . ARG A 1 153 ? 6.37738   15.07011  -5.35820  1.000 84.30398  ? 1072 ARG A CB  1 
ATOM   1180 C  CG  . ARG A 1 153 ? 7.75930   15.28272  -5.94310  1.000 86.79385  ? 1072 ARG A CG  1 
ATOM   1181 C  CD  . ARG A 1 153 ? 8.67551   14.14442  -5.54313  1.000 85.31269  ? 1072 ARG A CD  1 
ATOM   1182 N  NE  . ARG A 1 153 ? 8.11388   12.86861  -5.97260  1.000 89.76095  ? 1072 ARG A NE  1 
ATOM   1183 C  CZ  . ARG A 1 153 ? 8.24564   11.72719  -5.31198  1.000 85.27497  ? 1072 ARG A CZ  1 
ATOM   1184 N  NH1 . ARG A 1 153 ? 8.93301   11.65804  -4.18416  1.000 81.28858  ? 1072 ARG A NH1 1 
ATOM   1185 N  NH2 . ARG A 1 153 ? 7.66512   10.62971  -5.79102  1.000 82.58030  ? 1072 ARG A NH2 1 
ATOM   1186 N  N   . ASP A 1 154 ? 4.49933   14.56396  -7.84179  1.000 85.38683  ? 1073 ASP A N   1 
ATOM   1187 C  CA  . ASP A 1 154 ? 4.29659   14.25042  -9.25123  1.000 91.07931  ? 1073 ASP A CA  1 
ATOM   1188 C  C   . ASP A 1 154 ? 3.46776   15.32692  -9.93691  1.000 91.43095  ? 1073 ASP A C   1 
ATOM   1189 O  O   . ASP A 1 154 ? 3.59107   15.53153  -11.14930 1.000 91.29922  ? 1073 ASP A O   1 
ATOM   1190 C  CB  . ASP A 1 154 ? 3.60959   12.89234  -9.39808  1.000 90.87815  ? 1073 ASP A CB  1 
ATOM   1191 C  CG  . ASP A 1 154 ? 4.58067   11.73012  -9.33496  1.000 95.21611  ? 1073 ASP A CG  1 
ATOM   1192 O  OD1 . ASP A 1 154 ? 5.11746   11.44602  -8.23882  1.000 93.66040  ? 1073 ASP A OD1 1 
ATOM   1193 O  OD2 . ASP A 1 154 ? 4.81420   11.08846  -10.37399 1.000 99.39313  ? 1073 ASP A OD2 1 
ATOM   1194 N  N   . ASN A 1 155 ? 2.62242   16.01936  -9.17640  1.000 88.66297  ? 1074 ASN A N   1 
ATOM   1195 C  CA  . ASN A 1 155 ? 1.79402   17.11105  -9.66418  1.000 88.39553  ? 1074 ASN A CA  1 
ATOM   1196 C  C   . ASN A 1 155 ? 2.50030   18.46524  -9.58287  1.000 87.60908  ? 1074 ASN A C   1 
ATOM   1197 O  O   . ASN A 1 155 ? 1.86873   19.49791  -9.82740  1.000 84.77522  ? 1074 ASN A O   1 
ATOM   1198 C  CB  . ASN A 1 155 ? 0.48671   17.14117  -8.86642  1.000 85.36003  ? 1074 ASN A CB  1 
ATOM   1199 C  CG  . ASN A 1 155 ? -0.58496  17.97361  -9.52648  1.000 86.50560  ? 1074 ASN A CG  1 
ATOM   1200 O  OD1 . ASN A 1 155 ? -0.46355  18.35468  -10.68957 1.000 84.52388  ? 1074 ASN A OD1 1 
ATOM   1201 N  ND2 . ASN A 1 155 ? -1.65352  18.24834  -8.78993  1.000 82.65422  ? 1074 ASN A ND2 1 
ATOM   1202 N  N   . LYS A 1 156 ? 3.78812   18.48079  -9.22637  1.000 90.54949  ? 1075 LYS A N   1 
ATOM   1203 C  CA  . LYS A 1 156 ? 4.56041   19.71787  -9.08115  1.000 91.68103  ? 1075 LYS A CA  1 
ATOM   1204 C  C   . LYS A 1 156 ? 3.89673   20.69075  -8.10876  1.000 91.15406  ? 1075 LYS A C   1 
ATOM   1205 O  O   . LYS A 1 156 ? 3.83404   21.89689  -8.35384  1.000 92.43652  ? 1075 LYS A O   1 
ATOM   1206 C  CB  . LYS A 1 156 ? 4.84548   20.38461  -10.43054 1.000 97.90620  ? 1075 LYS A CB  1 
ATOM   1207 C  CG  . LYS A 1 156 ? 5.64146   19.50008  -11.36143 1.000 101.37224 ? 1075 LYS A CG  1 
ATOM   1208 C  CD  . LYS A 1 156 ? 7.06511   19.45481  -10.80214 1.000 116.61822 ? 1075 LYS A CD  1 
ATOM   1209 C  CE  . LYS A 1 156 ? 8.09019   18.81892  -11.70699 1.000 120.29285 ? 1075 LYS A CE  1 
ATOM   1210 N  NZ  . LYS A 1 156 ? 8.65478   19.79627  -12.69672 1.000 119.93655 ? 1075 LYS A NZ  1 
ATOM   1211 N  N   . LYS A 1 157 ? 3.39951   20.15228  -6.99570  1.000 85.50763  ? 1076 LYS A N   1 
ATOM   1212 C  CA  . LYS A 1 157 ? 2.85529   20.92362  -5.89007  1.000 81.32247  ? 1076 LYS A CA  1 
ATOM   1213 C  C   . LYS A 1 157 ? 3.70034   20.69261  -4.64809  1.000 80.83080  ? 1076 LYS A C   1 
ATOM   1214 O  O   . LYS A 1 157 ? 4.20221   19.58749  -4.40816  1.000 84.57865  ? 1076 LYS A O   1 
ATOM   1215 C  CB  . LYS A 1 157 ? 1.41346   20.54676  -5.58016  1.000 78.73954  ? 1076 LYS A CB  1 
ATOM   1216 C  CG  . LYS A 1 157 ? 0.40479   21.05409  -6.57340  1.000 86.33609  ? 1076 LYS A CG  1 
ATOM   1217 C  CD  . LYS A 1 157 ? 0.26564   22.57802  -6.43612  1.000 82.76695  ? 1076 LYS A CD  1 
ATOM   1218 C  CE  . LYS A 1 157 ? 0.11105   22.98457  -4.95388  1.000 94.03206  ? 1076 LYS A CE  1 
ATOM   1219 N  NZ  . LYS A 1 157 ? -0.89455  22.14753  -4.22676  1.000 80.51673  ? 1076 LYS A NZ  1 
ATOM   1220 N  N   . THR A 1 158 ? 3.81627   21.73733  -3.83512  1.000 80.04242  ? 1077 THR A N   1 
ATOM   1221 C  CA  . THR A 1 158 ? 4.55319   21.66961  -2.58273  1.000 79.11018  ? 1077 THR A CA  1 
ATOM   1222 C  C   . THR A 1 158 ? 3.65436   21.48184  -1.37213  1.000 76.10139  ? 1077 THR A C   1 
ATOM   1223 O  O   . THR A 1 158 ? 4.15429   21.44964  -0.24343  1.000 77.76945  ? 1077 THR A O   1 
ATOM   1224 C  CB  . THR A 1 158 ? 5.39617   22.93818  -2.41685  1.000 77.46749  ? 1077 THR A CB  1 
ATOM   1225 O  OG1 . THR A 1 158 ? 4.53192   24.07710  -2.26544  1.000 77.80251  ? 1077 THR A OG1 1 
ATOM   1226 C  CG2 . THR A 1 158 ? 6.31540   23.12797  -3.62122  1.000 83.84742  ? 1077 THR A CG2 1 
ATOM   1227 N  N   . ARG A 1 159 ? 2.35213   21.31951  -1.57822  1.000 75.22621  ? 1078 ARG A N   1 
ATOM   1228 C  CA  . ARG A 1 159 ? 1.43694   21.05026  -0.48274  1.000 73.27704  ? 1078 ARG A CA  1 
ATOM   1229 C  C   . ARG A 1 159 ? 0.41535   20.02109  -0.93994  1.000 72.03474  ? 1078 ARG A C   1 
ATOM   1230 O  O   . ARG A 1 159 ? 0.02751   19.98549  -2.11060  1.000 71.02702  ? 1078 ARG A O   1 
ATOM   1231 C  CB  . ARG A 1 159 ? 0.74462   22.34141  -0.00952  1.000 73.09379  ? 1078 ARG A CB  1 
ATOM   1232 C  CG  . ARG A 1 159 ? -0.64016  22.52905  -0.57144  1.000 81.90379  ? 1078 ARG A CG  1 
ATOM   1233 C  CD  . ARG A 1 159 ? -1.14462  23.93317  -0.34515  1.000 97.63103  ? 1078 ARG A CD  1 
ATOM   1234 N  NE  . ARG A 1 159 ? -1.30752  24.26869  1.06193   1.000 100.31589 ? 1078 ARG A NE  1 
ATOM   1235 C  CZ  . ARG A 1 159 ? -1.45280  25.50688  1.51125   1.000 104.84457 ? 1078 ARG A CZ  1 
ATOM   1236 N  NH1 . ARG A 1 159 ? -1.40661  26.54830  0.69779   1.000 98.51384  ? 1078 ARG A NH1 1 
ATOM   1237 N  NH2 . ARG A 1 159 ? -1.63527  25.70739  2.80877   1.000 103.91587 ? 1078 ARG A NH2 1 
ATOM   1238 N  N   . ILE A 1 160 ? 0.00806   19.16957  -0.00569  1.000 63.48732  ? 1079 ILE A N   1 
ATOM   1239 C  CA  . ILE A 1 160 ? -1.00771  18.15296  -0.25379  1.000 62.63700  ? 1079 ILE A CA  1 
ATOM   1240 C  C   . ILE A 1 160 ? -2.38664  18.78939  -0.16323  1.000 60.20135  ? 1079 ILE A C   1 
ATOM   1241 O  O   . ILE A 1 160 ? -2.69257  19.50190  0.79935   1.000 62.85540  ? 1079 ILE A O   1 
ATOM   1242 C  CB  . ILE A 1 160 ? -0.86532  16.98800  0.74090   1.000 57.19857  ? 1079 ILE A CB  1 
ATOM   1243 C  CG1 . ILE A 1 160 ? 0.42746   16.20022  0.50607   1.000 61.08229  ? 1079 ILE A CG1 1 
ATOM   1244 C  CG2 . ILE A 1 160 ? -2.04287  16.04001  0.65215   1.000 57.91097  ? 1079 ILE A CG2 1 
ATOM   1245 C  CD1 . ILE A 1 160 ? 0.97778   15.57485  1.79717   1.000 60.67771  ? 1079 ILE A CD1 1 
ATOM   1246 N  N   . ILE A 1 161 ? -3.21003  18.55916  -1.17924  1.000 62.80094  ? 1080 ILE A N   1 
ATOM   1247 C  CA  . ILE A 1 161 ? -4.57892  19.05904  -1.18948  1.000 64.93949  ? 1080 ILE A CA  1 
ATOM   1248 C  C   . ILE A 1 161 ? -5.49547  17.84041  -1.18736  1.000 62.44216  ? 1080 ILE A C   1 
ATOM   1249 O  O   . ILE A 1 161 ? -5.00116  16.71078  -1.31749  1.000 64.13157  ? 1080 ILE A O   1 
ATOM   1250 C  CB  . ILE A 1 161 ? -4.81676  19.99511  -2.38851  1.000 69.44695  ? 1080 ILE A CB  1 
ATOM   1251 C  CG1 . ILE A 1 161 ? -4.83128  19.22793  -3.70344  1.000 68.21228  ? 1080 ILE A CG1 1 
ATOM   1252 C  CG2 . ILE A 1 161 ? -3.72927  21.04597  -2.47375  1.000 76.11559  ? 1080 ILE A CG2 1 
ATOM   1253 C  CD1 . ILE A 1 161 ? -5.25658  20.09836  -4.89248  1.000 75.58410  ? 1080 ILE A CD1 1 
ATOM   1254 N  N   . PRO A 1 162 ? -6.81005  17.99938  -0.98837  1.000 67.30877  ? 1081 PRO A N   1 
ATOM   1255 C  CA  . PRO A 1 162 ? -7.66825  16.80838  -0.86492  1.000 62.81178  ? 1081 PRO A CA  1 
ATOM   1256 C  C   . PRO A 1 162 ? -7.58225  15.83864  -2.03612  1.000 67.36417  ? 1081 PRO A C   1 
ATOM   1257 O  O   . PRO A 1 162 ? -7.61024  14.62322  -1.81040  1.000 68.43350  ? 1081 PRO A O   1 
ATOM   1258 C  CB  . PRO A 1 162 ? -9.06943  17.41733  -0.73276  1.000 67.81093  ? 1081 PRO A CB  1 
ATOM   1259 C  CG  . PRO A 1 162 ? -8.83018  18.70835  -0.04345  1.000 69.02487  ? 1081 PRO A CG  1 
ATOM   1260 C  CD  . PRO A 1 162 ? -7.52906  19.22593  -0.59305  1.000 68.54894  ? 1081 PRO A CD  1 
ATOM   1261 N  N   . ARG A 1 163 ? -7.48290  16.31839  -3.28201  1.000 68.88779  ? 1082 ARG A N   1 
ATOM   1262 C  CA  . ARG A 1 163 ? -7.48552  15.36355  -4.38910  1.000 70.74120  ? 1082 ARG A CA  1 
ATOM   1263 C  C   . ARG A 1 163 ? -6.21805  14.51385  -4.42874  1.000 70.24353  ? 1082 ARG A C   1 
ATOM   1264 O  O   . ARG A 1 163 ? -6.24559  13.42051  -5.00226  1.000 74.15571  ? 1082 ARG A O   1 
ATOM   1265 C  CB  . ARG A 1 163 ? -7.71374  16.06156  -5.73397  1.000 79.20163  ? 1082 ARG A CB  1 
ATOM   1266 C  CG  . ARG A 1 163 ? -6.57130  16.89355  -6.25827  1.000 81.10148  ? 1082 ARG A CG  1 
ATOM   1267 C  CD  . ARG A 1 163 ? -6.80237  17.25022  -7.72533  1.000 86.59021  ? 1082 ARG A CD  1 
ATOM   1268 N  NE  . ARG A 1 163 ? -5.71954  18.07021  -8.24962  1.000 75.63473  ? 1082 ARG A NE  1 
ATOM   1269 C  CZ  . ARG A 1 163 ? -5.82067  19.37088  -8.47694  1.000 90.66909  ? 1082 ARG A CZ  1 
ATOM   1270 N  NH1 . ARG A 1 163 ? -6.94906  20.02349  -8.25282  1.000 99.92223  ? 1082 ARG A NH1 1 
ATOM   1271 N  NH2 . ARG A 1 163 ? -4.76445  20.03405  -8.93989  1.000 95.69543  ? 1082 ARG A NH2 1 
ATOM   1272 N  N   . HIS A 1 164 ? -5.11427  14.97935  -3.83352  1.000 70.36562  ? 1083 HIS A N   1 
ATOM   1273 C  CA  . HIS A 1 164 ? -3.94076  14.11873  -3.68600  1.000 69.76716  ? 1083 HIS A CA  1 
ATOM   1274 C  C   . HIS A 1 164 ? -4.22480  12.95358  -2.74489  1.000 66.40315  ? 1083 HIS A C   1 
ATOM   1275 O  O   . HIS A 1 164 ? -3.82590  11.81287  -3.01496  1.000 65.36451  ? 1083 HIS A O   1 
ATOM   1276 C  CB  . HIS A 1 164 ? -2.74716  14.92044  -3.16287  1.000 66.25900  ? 1083 HIS A CB  1 
ATOM   1277 C  CG  . HIS A 1 164 ? -2.29532  16.02351  -4.07006  1.000 70.95349  ? 1083 HIS A CG  1 
ATOM   1278 N  ND1 . HIS A 1 164 ? -1.72698  17.18551  -3.59492  1.000 71.43578  ? 1083 HIS A ND1 1 
ATOM   1279 C  CD2 . HIS A 1 164 ? -2.28513  16.12535  -5.42033  1.000 75.14543  ? 1083 HIS A CD2 1 
ATOM   1280 C  CE1 . HIS A 1 164 ? -1.40751  17.96556  -4.61285  1.000 77.21989  ? 1083 HIS A CE1 1 
ATOM   1281 N  NE2 . HIS A 1 164 ? -1.73468  17.34515  -5.73236  1.000 74.70198  ? 1083 HIS A NE2 1 
ATOM   1282 N  N   . LEU A 1 165 ? -4.90288  13.22548  -1.62714  1.000 62.06161  ? 1084 LEU A N   1 
ATOM   1283 C  CA  . LEU A 1 165 ? -5.23542  12.16731  -0.67986  1.000 59.64157  ? 1084 LEU A CA  1 
ATOM   1284 C  C   . LEU A 1 165 ? -6.15282  11.13899  -1.32290  1.000 63.34959  ? 1084 LEU A C   1 
ATOM   1285 O  O   . LEU A 1 165 ? -5.91379  9.92984   -1.23318  1.000 59.25168  ? 1084 LEU A O   1 
ATOM   1286 C  CB  . LEU A 1 165 ? -5.90839  12.77448  0.54894   1.000 58.89780  ? 1084 LEU A CB  1 
ATOM   1287 C  CG  . LEU A 1 165 ? -5.05625  13.59165  1.51246   1.000 59.95016  ? 1084 LEU A CG  1 
ATOM   1288 C  CD1 . LEU A 1 165 ? -5.94945  14.20703  2.57417   1.000 59.92741  ? 1084 LEU A CD1 1 
ATOM   1289 C  CD2 . LEU A 1 165 ? -3.99330  12.73648  2.14041   1.000 58.49923  ? 1084 LEU A CD2 1 
ATOM   1290 N  N   . GLN A 1 166 ? -7.19652  11.61268  -2.00751  1.000 65.15612  ? 1085 GLN A N   1 
ATOM   1291 C  CA  . GLN A 1 166 ? -8.17899  10.71572  -2.61052  1.000 70.07493  ? 1085 GLN A CA  1 
ATOM   1292 C  C   . GLN A 1 166 ? -7.54114  9.84133   -3.67884  1.000 65.35855  ? 1085 GLN A C   1 
ATOM   1293 O  O   . GLN A 1 166 ? -7.82974  8.64090   -3.77231  1.000 62.84604  ? 1085 GLN A O   1 
ATOM   1294 C  CB  . GLN A 1 166 ? -9.31822  11.54310  -3.20490  1.000 70.29664  ? 1085 GLN A CB  1 
ATOM   1295 C  CG  . GLN A 1 166 ? -10.09178 12.32429  -2.16193  1.000 80.47102  ? 1085 GLN A CG  1 
ATOM   1296 C  CD  . GLN A 1 166 ? -10.66783 13.62097  -2.70359  1.000 91.31055  ? 1085 GLN A CD  1 
ATOM   1297 O  OE1 . GLN A 1 166 ? -11.02622 14.51573  -1.93502  1.000 86.39100  ? 1085 GLN A OE1 1 
ATOM   1298 N  NE2 . GLN A 1 166 ? -10.74551 13.73715  -4.02900  1.000 89.79503  ? 1085 GLN A NE2 1 
ATOM   1299 N  N   . LEU A 1 167 ? -6.67892  10.43482  -4.50134  1.000 66.00974  ? 1086 LEU A N   1 
ATOM   1300 C  CA  . LEU A 1 167 ? -5.99326  9.68244   -5.54173  1.000 66.77234  ? 1086 LEU A CA  1 
ATOM   1301 C  C   . LEU A 1 167 ? -5.05073  8.65036   -4.92605  1.000 64.82468  ? 1086 LEU A C   1 
ATOM   1302 O  O   . LEU A 1 167 ? -5.00551  7.49693   -5.37122  1.000 63.27849  ? 1086 LEU A O   1 
ATOM   1303 C  CB  . LEU A 1 167 ? -5.26074  10.66662  -6.45657  1.000 66.30209  ? 1086 LEU A CB  1 
ATOM   1304 C  CG  . LEU A 1 167 ? -4.90986  10.36121  -7.91566  1.000 71.13832  ? 1086 LEU A CG  1 
ATOM   1305 C  CD1 . LEU A 1 167 ? -4.14714  11.53299  -8.50131  1.000 70.34933  ? 1086 LEU A CD1 1 
ATOM   1306 C  CD2 . LEU A 1 167 ? -4.11063  9.10188   -8.05119  1.000 73.71118  ? 1086 LEU A CD2 1 
ATOM   1307 N  N   . ALA A 1 168 ? -4.31134  9.03985   -3.88075  1.000 60.99658  ? 1087 ALA A N   1 
ATOM   1308 C  CA  . ALA A 1 168 ? -3.36684  8.12015   -3.24851  1.000 60.30070  ? 1087 ALA A CA  1 
ATOM   1309 C  C   . ALA A 1 168 ? -4.07297  6.90783   -2.64829  1.000 55.49371  ? 1087 ALA A C   1 
ATOM   1310 O  O   . ALA A 1 168 ? -3.58450  5.77811   -2.75921  1.000 52.36918  ? 1087 ALA A O   1 
ATOM   1311 C  CB  . ALA A 1 168 ? -2.56221  8.84969   -2.17425  1.000 63.03462  ? 1087 ALA A CB  1 
ATOM   1312 N  N   . VAL A 1 169 ? -5.21061  7.12096   -1.98849  1.000 51.74074  ? 1088 VAL A N   1 
ATOM   1313 C  CA  . VAL A 1 169 ? -5.95542  5.99776   -1.42669  1.000 53.67497  ? 1088 VAL A CA  1 
ATOM   1314 C  C   . VAL A 1 169 ? -6.55982  5.14047   -2.53542  1.000 54.35186  ? 1088 VAL A C   1 
ATOM   1315 O  O   . VAL A 1 169 ? -6.54286  3.90464   -2.46274  1.000 52.36215  ? 1088 VAL A O   1 
ATOM   1316 C  CB  . VAL A 1 169 ? -7.02973  6.50774   -0.44742  1.000 49.46352  ? 1088 VAL A CB  1 
ATOM   1317 C  CG1 . VAL A 1 169 ? -7.98192  5.38939   -0.06075  1.000 50.91670  ? 1088 VAL A CG1 1 
ATOM   1318 C  CG2 . VAL A 1 169 ? -6.37574  7.09278   0.78733   1.000 47.55530  ? 1088 VAL A CG2 1 
ATOM   1319 N  N   . ARG A 1 170 ? -7.09977  5.77897   -3.57645  1.000 56.30344  ? 1089 ARG A N   1 
ATOM   1320 C  CA  . ARG A 1 170 ? -7.79648  5.04582   -4.63148  1.000 64.25113  ? 1089 ARG A CA  1 
ATOM   1321 C  C   . ARG A 1 170 ? -6.86463  4.09627   -5.37373  1.000 61.24234  ? 1089 ARG A C   1 
ATOM   1322 O  O   . ARG A 1 170 ? -7.26365  2.98333   -5.73640  1.000 62.05421  ? 1089 ARG A O   1 
ATOM   1323 C  CB  . ARG A 1 170 ? -8.42102  6.03168   -5.61961  1.000 69.67824  ? 1089 ARG A CB  1 
ATOM   1324 C  CG  . ARG A 1 170 ? -8.71076  5.43972   -6.99676  1.000 84.18847  ? 1089 ARG A CG  1 
ATOM   1325 C  CD  . ARG A 1 170 ? -10.04846 4.71984   -7.06640  1.000 95.04191  ? 1089 ARG A CD  1 
ATOM   1326 N  NE  . ARG A 1 170 ? -11.11927 5.49378   -6.44980  1.000 103.91255 ? 1089 ARG A NE  1 
ATOM   1327 C  CZ  . ARG A 1 170 ? -12.07859 6.10647   -7.13061  1.000 107.82454 ? 1089 ARG A CZ  1 
ATOM   1328 N  NH1 . ARG A 1 170 ? -12.12702 6.05556   -8.45072  1.000 100.69802 ? 1089 ARG A NH1 1 
ATOM   1329 N  NH2 . ARG A 1 170 ? -13.00800 6.79190   -6.47059  1.000 112.70791 ? 1089 ARG A NH2 1 
ATOM   1330 N  N   . ASN A 1 171 ? -5.62735  4.51494   -5.61540  1.000 54.92398  ? 1090 ASN A N   1 
ATOM   1331 C  CA  . ASN A 1 171 ? -4.67946  3.72036   -6.38323  1.000 54.16674  ? 1090 ASN A CA  1 
ATOM   1332 C  C   . ASN A 1 171 ? -3.89294  2.72823   -5.54618  1.000 55.06007  ? 1090 ASN A C   1 
ATOM   1333 O  O   . ASN A 1 171 ? -3.02200  2.04183   -6.09066  1.000 55.96669  ? 1090 ASN A O   1 
ATOM   1334 C  CB  . ASN A 1 171 ? -3.70191  4.61259   -7.14119  1.000 58.98878  ? 1090 ASN A CB  1 
ATOM   1335 C  CG  . ASN A 1 171 ? -4.32460  5.24082   -8.36047  1.000 60.73144  ? 1090 ASN A CG  1 
ATOM   1336 O  OD1 . ASN A 1 171 ? -5.39017  4.82478   -8.81579  1.000 67.17749  ? 1090 ASN A OD1 1 
ATOM   1337 N  ND2 . ASN A 1 171 ? -3.62769  6.19507   -8.94324  1.000 68.98224  ? 1090 ASN A ND2 1 
ATOM   1338 N  N   . ASP A 1 172 ? -4.13555  2.66162   -4.24506  1.000 46.47041  ? 1091 ASP A N   1 
ATOM   1339 C  CA  . ASP A 1 172 ? -3.48404  1.68545   -3.38790  1.000 47.74861  ? 1091 ASP A CA  1 
ATOM   1340 C  C   . ASP A 1 172 ? -4.53883  0.65466   -3.01409  1.000 51.04004  ? 1091 ASP A C   1 
ATOM   1341 O  O   . ASP A 1 172 ? -5.46373  0.95305   -2.25288  1.000 42.82553  ? 1091 ASP A O   1 
ATOM   1342 C  CB  . ASP A 1 172 ? -2.87308  2.35996   -2.16052  1.000 49.39285  ? 1091 ASP A CB  1 
ATOM   1343 C  CG  . ASP A 1 172 ? -2.02837  1.41174   -1.32011  1.000 48.31334  ? 1091 ASP A CG  1 
ATOM   1344 O  OD1 . ASP A 1 172 ? -2.60038  0.58191   -0.57772  1.000 44.87944  ? 1091 ASP A OD1 1 
ATOM   1345 O  OD2 . ASP A 1 172 ? -0.78349  1.47657   -1.42638  1.000 51.19058  ? 1091 ASP A OD2 1 
ATOM   1346 N  N   . GLU A 1 173 ? -4.39123  -0.55722  -3.55193  1.000 43.99347  ? 1092 GLU A N   1 
ATOM   1347 C  CA  . GLU A 1 173 ? -5.41432  -1.58005  -3.37045  1.000 43.80944  ? 1092 GLU A CA  1 
ATOM   1348 C  C   . GLU A 1 173 ? -5.72151  -1.81838  -1.89930  1.000 44.03188  ? 1092 GLU A C   1 
ATOM   1349 O  O   . GLU A 1 173 ? -6.89072  -1.92741  -1.51563  1.000 42.90775  ? 1092 GLU A O   1 
ATOM   1350 C  CB  . GLU A 1 173 ? -4.96688  -2.88089  -4.03368  1.000 50.07685  ? 1092 GLU A CB  1 
ATOM   1351 C  CG  . GLU A 1 173 ? -5.86869  -4.05995  -3.74337  1.000 52.14531  ? 1092 GLU A CG  1 
ATOM   1352 C  CD  . GLU A 1 173 ? -5.68523  -5.20216  -4.71785  1.000 64.03196  ? 1092 GLU A CD  1 
ATOM   1353 O  OE1 . GLU A 1 173 ? -6.51023  -6.11651  -4.72794  1.000 76.62957  ? 1092 GLU A OE1 1 
ATOM   1354 O  OE2 . GLU A 1 173 ? -4.69290  -5.23959  -5.44757  1.000 61.68522  ? 1092 GLU A OE2 1 
ATOM   1355 N  N   . GLU A 1 174 ? -4.68872  -1.89008  -1.05986  1.000 41.10644  ? 1093 GLU A N   1 
ATOM   1356 C  CA  . GLU A 1 174 ? -4.91999  -2.18881  0.34812   1.000 37.14901  ? 1093 GLU A CA  1 
ATOM   1357 C  C   . GLU A 1 174 ? -5.52977  -1.00231  1.09365   1.000 36.99716  ? 1093 GLU A C   1 
ATOM   1358 O  O   . GLU A 1 174 ? -6.49486  -1.18077  1.84107   1.000 36.35481  ? 1093 GLU A O   1 
ATOM   1359 C  CB  . GLU A 1 174 ? -3.62407  -2.67333  0.99549   1.000 37.77476  ? 1093 GLU A CB  1 
ATOM   1360 C  CG  . GLU A 1 174 ? -3.21718  -4.06887  0.48050   1.000 36.82102  ? 1093 GLU A CG  1 
ATOM   1361 C  CD  . GLU A 1 174 ? -1.80945  -4.48087  0.87905   1.000 41.59645  ? 1093 GLU A CD  1 
ATOM   1362 O  OE1 . GLU A 1 174 ? -1.36991  -5.58368  0.52735   1.000 37.96536  ? 1093 GLU A OE1 1 
ATOM   1363 O  OE2 . GLU A 1 174 ? -1.10158  -3.71539  1.55300   1.000 37.88317  ? 1093 GLU A OE2 1 
ATOM   1364 N  N   . LEU A 1 175 ? -5.02125  0.21683   0.87805   1.000 38.48670  ? 1094 LEU A N   1 
ATOM   1365 C  CA  . LEU A 1 175 ? -5.61372  1.37528   1.55082   1.000 38.54157  ? 1094 LEU A CA  1 
ATOM   1366 C  C   . LEU A 1 175 ? -7.04032  1.62895   1.08268   1.000 40.55373  ? 1094 LEU A C   1 
ATOM   1367 O  O   . LEU A 1 175 ? -7.90054  2.01040   1.88224   1.000 40.70493  ? 1094 LEU A O   1 
ATOM   1368 C  CB  . LEU A 1 175 ? -4.76901  2.63063   1.31915   1.000 42.12169  ? 1094 LEU A CB  1 
ATOM   1369 C  CG  . LEU A 1 175 ? -3.50913  2.75011   2.17645   1.000 37.46382  ? 1094 LEU A CG  1 
ATOM   1370 C  CD1 . LEU A 1 175 ? -2.64491  3.90609   1.64483   1.000 39.31517  ? 1094 LEU A CD1 1 
ATOM   1371 C  CD2 . LEU A 1 175 ? -3.87084  2.96272   3.64015   1.000 38.68284  ? 1094 LEU A CD2 1 
ATOM   1372 N  N   . ASN A 1 176 ? -7.30925  1.43069   -0.20719  1.000 39.78428  ? 1095 ASN A N   1 
ATOM   1373 C  CA  . ASN A 1 176 ? -8.66113  1.62713   -0.71810  1.000 44.28437  ? 1095 ASN A CA  1 
ATOM   1374 C  C   . ASN A 1 176 ? -9.63074  0.64786   -0.06754  1.000 44.69781  ? 1095 ASN A C   1 
ATOM   1375 O  O   . ASN A 1 176 ? -10.75528 1.01928   0.29168   1.000 43.44239  ? 1095 ASN A O   1 
ATOM   1376 C  CB  . ASN A 1 176 ? -8.67169  1.46732   -2.23674  1.000 49.83170  ? 1095 ASN A CB  1 
ATOM   1377 C  CG  . ASN A 1 176 ? -9.97042  1.92903   -2.86222  1.000 56.44553  ? 1095 ASN A CG  1 
ATOM   1378 O  OD1 . ASN A 1 176 ? -10.44848 3.03136   -2.58714  1.000 57.86334  ? 1095 ASN A OD1 1 
ATOM   1379 N  ND2 . ASN A 1 176 ? -10.55231 1.08769   -3.70045  1.000 59.50988  ? 1095 ASN A ND2 1 
ATOM   1380 N  N   . LYS A 1 177 ? -9.21065  -0.61356  0.08489   1.000 39.67522  ? 1096 LYS A N   1 
ATOM   1381 C  CA  . LYS A 1 177 ? -10.03845 -1.59433  0.77958   1.000 42.86080  ? 1096 LYS A CA  1 
ATOM   1382 C  C   . LYS A 1 177 ? -10.27938 -1.17864  2.22114   1.000 40.55972  ? 1096 LYS A C   1 
ATOM   1383 O  O   . LYS A 1 177 ? -11.41468 -1.23341  2.70524   1.000 39.17703  ? 1096 LYS A O   1 
ATOM   1384 C  CB  . LYS A 1 177 ? -9.38508  -2.97431  0.71583   1.000 40.67524  ? 1096 LYS A CB  1 
ATOM   1385 C  CG  . LYS A 1 177 ? -10.11367 -4.05073  1.51191   1.000 48.96272  ? 1096 LYS A CG  1 
ATOM   1386 C  CD  . LYS A 1 177 ? -9.48974  -5.43204  1.27751   1.000 55.93524  ? 1096 LYS A CD  1 
ATOM   1387 C  CE  . LYS A 1 177 ? -10.12675 -6.18509  0.11403   1.000 58.82889  ? 1096 LYS A CE  1 
ATOM   1388 N  NZ  . LYS A 1 177 ? -9.97157  -5.50402  -1.21042  1.000 64.69159  ? 1096 LYS A NZ  1 
ATOM   1389 N  N   . LEU A 1 178 ? -9.23651  -0.70640  2.90665   1.000 35.37855  ? 1097 LEU A N   1 
ATOM   1390 C  CA  . LEU A 1 178 ? -9.40860  -0.31951  4.30675   1.000 32.98590  ? 1097 LEU A CA  1 
ATOM   1391 C  C   . LEU A 1 178 ? -10.36302 0.85654   4.43061   1.000 37.55953  ? 1097 LEU A C   1 
ATOM   1392 O  O   . LEU A 1 178 ? -11.23157 0.87216   5.31217   1.000 36.59106  ? 1097 LEU A O   1 
ATOM   1393 C  CB  . LEU A 1 178 ? -8.06391  0.02525   4.93524   1.000 34.82668  ? 1097 LEU A CB  1 
ATOM   1394 C  CG  . LEU A 1 178 ? -8.18192  0.56699   6.36226   1.000 34.91005  ? 1097 LEU A CG  1 
ATOM   1395 C  CD1 . LEU A 1 178 ? -8.74026  -0.50509  7.30247   1.000 32.70452  ? 1097 LEU A CD1 1 
ATOM   1396 C  CD2 . LEU A 1 178 ? -6.82865  1.05403   6.83540   1.000 37.04344  ? 1097 LEU A CD2 1 
ATOM   1397 N  N   . LEU A 1 179 ? -10.23081 1.84518   3.54958   1.000 34.57246  ? 1098 LEU A N   1 
ATOM   1398 C  CA  . LEU A 1 179 ? -11.07085 3.02318   3.68370   1.000 43.22918  ? 1098 LEU A CA  1 
ATOM   1399 C  C   . LEU A 1 179 ? -12.53640 2.64753   3.52772   1.000 48.84709  ? 1098 LEU A C   1 
ATOM   1400 O  O   . LEU A 1 179 ? -13.40222 3.21290   4.20860   1.000 52.28494  ? 1098 LEU A O   1 
ATOM   1401 C  CB  . LEU A 1 179 ? -10.68293 4.05904   2.63227   1.000 47.88570  ? 1098 LEU A CB  1 
ATOM   1402 C  CG  . LEU A 1 179 ? -11.79107 5.06711   2.30856   1.000 49.55478  ? 1098 LEU A CG  1 
ATOM   1403 C  CD1 . LEU A 1 179 ? -11.91344 6.07268   3.45500   1.000 57.21644  ? 1098 LEU A CD1 1 
ATOM   1404 C  CD2 . LEU A 1 179 ? -11.60223 5.77295   0.95212   1.000 54.71102  ? 1098 LEU A CD2 1 
ATOM   1405 N  N   . GLY A 1 180 ? -12.82229 1.64375   2.69353   1.000 44.54437  ? 1099 GLY A N   1 
ATOM   1406 C  CA  . GLY A 1 180 ? -14.19090 1.21195   2.50036   1.000 53.06614  ? 1099 GLY A CA  1 
ATOM   1407 C  C   . GLY A 1 180 ? -14.77424 0.53333   3.71844   1.000 51.32937  ? 1099 GLY A C   1 
ATOM   1408 O  O   . GLY A 1 180 ? -15.99736 0.44936   3.84703   1.000 62.82375  ? 1099 GLY A O   1 
ATOM   1409 N  N   . GLY A 1 181 ? -13.93067 0.05240   4.61862   1.000 43.36025  ? 1100 GLY A N   1 
ATOM   1410 C  CA  . GLY A 1 181 ? -14.41299 -0.59645  5.81197   1.000 43.17182  ? 1100 GLY A CA  1 
ATOM   1411 C  C   . GLY A 1 181 ? -14.47933 0.24506   7.06186   1.000 50.50555  ? 1100 GLY A C   1 
ATOM   1412 O  O   . GLY A 1 181 ? -14.89489 -0.26745  8.10392   1.000 45.83835  ? 1100 GLY A O   1 
ATOM   1413 N  N   . VAL A 1 182 ? -14.04562 1.50747   7.02401   1.000 46.91925  ? 1101 VAL A N   1 
ATOM   1414 C  CA  . VAL A 1 182 ? -14.14577 2.34722   8.21336   1.000 44.56416  ? 1101 VAL A CA  1 
ATOM   1415 C  C   . VAL A 1 182 ? -15.39744 3.22676   8.21850   1.000 58.35079  ? 1101 VAL A C   1 
ATOM   1416 O  O   . VAL A 1 182 ? -15.61727 3.96635   9.18753   1.000 56.28140  ? 1101 VAL A O   1 
ATOM   1417 C  CB  . VAL A 1 182 ? -12.86082 3.17174   8.41871   1.000 44.08287  ? 1101 VAL A CB  1 
ATOM   1418 C  CG1 . VAL A 1 182 ? -11.67120 2.21928   8.59606   1.000 48.56037  ? 1101 VAL A CG1 1 
ATOM   1419 C  CG2 . VAL A 1 182 ? -12.63418 4.12362   7.26951   1.000 48.18305  ? 1101 VAL A CG2 1 
ATOM   1420 N  N   . THR A 1 183 ? -16.20766 3.19130   7.15927   1.000 54.40572  ? 1102 THR A N   1 
ATOM   1421 C  CA  . THR A 1 183 ? -17.44486 3.96034   7.07978   1.000 67.35060  ? 1102 THR A CA  1 
ATOM   1422 C  C   . THR A 1 183 ? -18.58105 3.04986   6.62829   1.000 67.70393  ? 1102 THR A C   1 
ATOM   1423 O  O   . THR A 1 183 ? -18.35051 2.04645   5.95169   1.000 70.06064  ? 1102 THR A O   1 
ATOM   1424 C  CB  . THR A 1 183 ? -17.32086 5.14923   6.10856   1.000 70.27273  ? 1102 THR A CB  1 
ATOM   1425 O  OG1 . THR A 1 183 ? -16.86763 4.68098   4.82945   1.000 70.86502  ? 1102 THR A OG1 1 
ATOM   1426 C  CG2 . THR A 1 183 ? -16.34082 6.19041   6.65130   1.000 66.34391  ? 1102 THR A CG2 1 
ATOM   1427 N  N   . ILE A 1 184 ? -19.81265 3.39910   6.99866   1.000 71.38830  ? 1103 ILE A N   1 
ATOM   1428 C  CA  . ILE A 1 184 ? -20.97569 2.68644   6.45597   1.000 72.34025  ? 1103 ILE A CA  1 
ATOM   1429 C  C   . ILE A 1 184 ? -21.64997 3.52942   5.37795   1.000 73.30997  ? 1103 ILE A C   1 
ATOM   1430 O  O   . ILE A 1 184 ? -21.94408 4.70679   5.59098   1.000 80.56475  ? 1103 ILE A O   1 
ATOM   1431 C  CB  . ILE A 1 184 ? -21.99411 2.30324   7.55252   1.000 69.81948  ? 1103 ILE A CB  1 
ATOM   1432 C  CG1 . ILE A 1 184 ? -21.55913 1.02606   8.27814   1.000 59.31115  ? 1103 ILE A CG1 1 
ATOM   1433 C  CG2 . ILE A 1 184 ? -23.37336 2.10407   6.93679   1.000 67.98688  ? 1103 ILE A CG2 1 
ATOM   1434 C  CD1 . ILE A 1 184 ? -22.37273 0.71625   9.54727   1.000 43.88733  ? 1103 ILE A CD1 1 
ATOM   1435 N  N   . GLU B 1 4   ? -5.92517  -10.16115 -15.02400 1.000 85.55115  ? 36   GLU B N   1 
ATOM   1436 C  CA  . GLU B 1 4   ? -5.35067  -9.24761  -14.04099 1.000 91.11711  ? 36   GLU B CA  1 
ATOM   1437 C  C   . GLU B 1 4   ? -4.67635  -8.07100  -14.73243 1.000 82.37596  ? 36   GLU B C   1 
ATOM   1438 O  O   . GLU B 1 4   ? -4.01064  -8.25343  -15.74823 1.000 76.71501  ? 36   GLU B O   1 
ATOM   1439 C  CB  . GLU B 1 4   ? -4.33949  -9.97484  -13.15150 1.000 82.09835  ? 36   GLU B CB  1 
ATOM   1440 C  CG  . GLU B 1 4   ? -4.33072  -9.47804  -11.71833 1.000 86.46760  ? 36   GLU B CG  1 
ATOM   1441 C  CD  . GLU B 1 4   ? -5.59900  -9.85129  -10.97543 1.000 89.54043  ? 36   GLU B CD  1 
ATOM   1442 O  OE1 . GLU B 1 4   ? -6.15866  -10.92954 -11.27068 1.000 88.85343  ? 36   GLU B OE1 1 
ATOM   1443 O  OE2 . GLU B 1 4   ? -6.03691  -9.06863  -10.10318 1.000 93.48589  ? 36   GLU B OE2 1 
ATOM   1444 N  N   . SER B 1 5   ? -4.83978  -6.86915  -14.18076 1.000 68.92490  ? 37   SER B N   1 
ATOM   1445 C  CA  . SER B 1 5   ? -4.24223  -5.66002  -14.73822 1.000 57.88741  ? 37   SER B CA  1 
ATOM   1446 C  C   . SER B 1 5   ? -3.14667  -5.14071  -13.81785 1.000 51.70918  ? 37   SER B C   1 
ATOM   1447 O  O   . SER B 1 5   ? -3.40036  -4.83763  -12.64659 1.000 47.86147  ? 37   SER B O   1 
ATOM   1448 C  CB  . SER B 1 5   ? -5.27836  -4.56654  -14.97828 1.000 52.56832  ? 37   SER B CB  1 
ATOM   1449 O  OG  . SER B 1 5   ? -4.62706  -3.40188  -15.45978 1.000 48.29284  ? 37   SER B OG  1 
ATOM   1450 N  N   . TYR B 1 6   ? -1.93916  -5.01850  -14.36693 1.000 46.12550  ? 38   TYR B N   1 
ATOM   1451 C  CA  . TYR B 1 6   ? -0.80622  -4.37686  -13.71754 1.000 43.33785  ? 38   TYR B CA  1 
ATOM   1452 C  C   . TYR B 1 6   ? -0.65752  -2.91470  -14.11379 1.000 45.45551  ? 38   TYR B C   1 
ATOM   1453 O  O   . TYR B 1 6   ? 0.39384   -2.31517  -13.85685 1.000 42.92433  ? 38   TYR B O   1 
ATOM   1454 C  CB  . TYR B 1 6   ? 0.47659   -5.12202  -14.05807 1.000 46.34527  ? 38   TYR B CB  1 
ATOM   1455 C  CG  . TYR B 1 6   ? 0.49350   -6.56488  -13.62744 1.000 51.21744  ? 38   TYR B CG  1 
ATOM   1456 C  CD1 . TYR B 1 6   ? 0.99389   -6.92356  -12.38279 1.000 49.87365  ? 38   TYR B CD1 1 
ATOM   1457 C  CD2 . TYR B 1 6   ? 0.02816   -7.57392  -14.46760 1.000 43.55719  ? 38   TYR B CD2 1 
ATOM   1458 C  CE1 . TYR B 1 6   ? 1.03018   -8.24463  -11.97786 1.000 47.86194  ? 38   TYR B CE1 1 
ATOM   1459 C  CE2 . TYR B 1 6   ? 0.06093   -8.90553  -14.06487 1.000 49.20524  ? 38   TYR B CE2 1 
ATOM   1460 C  CZ  . TYR B 1 6   ? 0.56866   -9.22824  -12.81783 1.000 52.26782  ? 38   TYR B CZ  1 
ATOM   1461 O  OH  . TYR B 1 6   ? 0.62643   -10.54038 -12.39236 1.000 55.06876  ? 38   TYR B OH  1 
ATOM   1462 N  N   . ALA B 1 7   ? -1.69999  -2.32679  -14.70858 1.000 46.75848  ? 39   ALA B N   1 
ATOM   1463 C  CA  . ALA B 1 7   ? -1.55909  -1.04117  -15.38288 1.000 41.77288  ? 39   ALA B CA  1 
ATOM   1464 C  C   . ALA B 1 7   ? -1.03908  0.04025   -14.44961 1.000 47.77288  ? 39   ALA B C   1 
ATOM   1465 O  O   . ALA B 1 7   ? -0.13706  0.79656   -14.81998 1.000 44.10311  ? 39   ALA B O   1 
ATOM   1466 C  CB  . ALA B 1 7   ? -2.89858  -0.61983  -15.98271 1.000 49.27511  ? 39   ALA B CB  1 
ATOM   1467 N  N   . ILE B 1 8   ? -1.57454  0.12410   -13.22776 1.000 42.82630  ? 40   ILE B N   1 
ATOM   1468 C  CA  . ILE B 1 8   ? -1.11467  1.16304   -12.31003 1.000 44.01376  ? 40   ILE B CA  1 
ATOM   1469 C  C   . ILE B 1 8   ? 0.38613   1.03358   -12.05649 1.000 37.58968  ? 40   ILE B C   1 
ATOM   1470 O  O   . ILE B 1 8   ? 1.10094   2.03926   -11.98167 1.000 46.36539  ? 40   ILE B O   1 
ATOM   1471 C  CB  . ILE B 1 8   ? -1.94257  1.15782   -11.00309 1.000 45.61340  ? 40   ILE B CB  1 
ATOM   1472 C  CG1 . ILE B 1 8   ? -3.33019  1.79189   -11.21736 1.000 53.83598  ? 40   ILE B CG1 1 
ATOM   1473 C  CG2 . ILE B 1 8   ? -1.21966  1.90573   -9.87823  1.000 52.30239  ? 40   ILE B CG2 1 
ATOM   1474 C  CD1 . ILE B 1 8   ? -4.37289  0.93359   -11.90979 1.000 59.21128  ? 40   ILE B CD1 1 
ATOM   1475 N  N   . TYR B 1 9   ? 0.89267   -0.19628  -11.93551 1.000 40.17233  ? 41   TYR B N   1 
ATOM   1476 C  CA  . TYR B 1 9   ? 2.31423   -0.38723  -11.64837 1.000 41.11735  ? 41   TYR B CA  1 
ATOM   1477 C  C   . TYR B 1 9   ? 3.17073   -0.21216  -12.89192 1.000 39.82319  ? 41   TYR B C   1 
ATOM   1478 O  O   . TYR B 1 9   ? 4.27469   0.33654   -12.80889 1.000 40.28654  ? 41   TYR B O   1 
ATOM   1479 C  CB  . TYR B 1 9   ? 2.54519   -1.76787  -11.03012 1.000 37.55036  ? 41   TYR B CB  1 
ATOM   1480 C  CG  . TYR B 1 9   ? 1.44128   -2.04360  -10.05230 1.000 42.95054  ? 41   TYR B CG  1 
ATOM   1481 C  CD1 . TYR B 1 9   ? 0.55656   -3.06618  -10.23649 1.000 48.30515  ? 41   TYR B CD1 1 
ATOM   1482 C  CD2 . TYR B 1 9   ? 1.27087   -1.25169  -8.96188  1.000 46.63409  ? 41   TYR B CD2 1 
ATOM   1483 C  CE1 . TYR B 1 9   ? -0.47013  -3.28615  -9.34283  1.000 53.99748  ? 41   TYR B CE1 1 
ATOM   1484 C  CE2 . TYR B 1 9   ? 0.25204   -1.46203  -8.08116  1.000 49.63964  ? 41   TYR B CE2 1 
ATOM   1485 C  CZ  . TYR B 1 9   ? -0.61142  -2.47861  -8.27002  1.000 52.59413  ? 41   TYR B CZ  1 
ATOM   1486 O  OH  . TYR B 1 9   ? -1.62079  -2.66669  -7.36455  1.000 60.63829  ? 41   TYR B OH  1 
ATOM   1487 N  N   . VAL B 1 10  ? 2.67140   -0.65335  -14.05126 1.000 42.33355  ? 42   VAL B N   1 
ATOM   1488 C  CA  . VAL B 1 10  ? 3.36151   -0.34750  -15.30468 1.000 38.36353  ? 42   VAL B CA  1 
ATOM   1489 C  C   . VAL B 1 10  ? 3.52062   1.15726   -15.44722 1.000 40.85694  ? 42   VAL B C   1 
ATOM   1490 O  O   . VAL B 1 10  ? 4.60497   1.65369   -15.78154 1.000 39.31599  ? 42   VAL B O   1 
ATOM   1491 C  CB  . VAL B 1 10  ? 2.61318   -0.95573  -16.51031 1.000 38.45145  ? 42   VAL B CB  1 
ATOM   1492 C  CG1 . VAL B 1 10  ? 3.28749   -0.53063  -17.83970 1.000 37.61401  ? 42   VAL B CG1 1 
ATOM   1493 C  CG2 . VAL B 1 10  ? 2.57217   -2.45965  -16.41350 1.000 40.89537  ? 42   VAL B CG2 1 
ATOM   1494 N  N   . TYR B 1 11  ? 2.45293   1.90698   -15.14491 1.000 41.22274  ? 43   TYR B N   1 
ATOM   1495 C  CA  . TYR B 1 11  ? 2.47817   3.35899   -15.25861 1.000 43.61985  ? 43   TYR B CA  1 
ATOM   1496 C  C   . TYR B 1 11  ? 3.49562   3.97417   -14.29539 1.000 42.70399  ? 43   TYR B C   1 
ATOM   1497 O  O   . TYR B 1 11  ? 4.24137   4.88842   -14.67289 1.000 45.32370  ? 43   TYR B O   1 
ATOM   1498 C  CB  . TYR B 1 11  ? 1.06843   3.89603   -15.01352 1.000 49.46351  ? 43   TYR B CB  1 
ATOM   1499 C  CG  . TYR B 1 11  ? 0.69639   5.13288   -15.78770 1.000 61.91342  ? 43   TYR B CG  1 
ATOM   1500 C  CD1 . TYR B 1 11  ? 0.06157   5.02127   -17.02363 1.000 62.82132  ? 43   TYR B CD1 1 
ATOM   1501 C  CD2 . TYR B 1 11  ? 0.94094   6.40527   -15.28637 1.000 71.32065  ? 43   TYR B CD2 1 
ATOM   1502 C  CE1 . TYR B 1 11  ? -0.30359  6.13943   -17.74864 1.000 81.75752  ? 43   TYR B CE1 1 
ATOM   1503 C  CE2 . TYR B 1 11  ? 0.57718   7.53864   -16.00507 1.000 80.30915  ? 43   TYR B CE2 1 
ATOM   1504 C  CZ  . TYR B 1 11  ? -0.04475  7.39741   -17.23653 1.000 91.85590  ? 43   TYR B CZ  1 
ATOM   1505 O  OH  . TYR B 1 11  ? -0.40762  8.51459   -17.95774 1.000 97.68325  ? 43   TYR B OH  1 
ATOM   1506 N  N   . LYS B 1 12  ? 3.55849   3.47873   -13.05031 1.000 44.48856  ? 44   LYS B N   1 
ATOM   1507 C  CA  . LYS B 1 12  ? 4.58208   3.96382   -12.12159 1.000 45.18800  ? 44   LYS B CA  1 
ATOM   1508 C  C   . LYS B 1 12  ? 5.98680   3.68897   -12.64845 1.000 36.35378  ? 44   LYS B C   1 
ATOM   1509 O  O   . LYS B 1 12  ? 6.85653   4.56741   -12.60769 1.000 43.19365  ? 44   LYS B O   1 
ATOM   1510 C  CB  . LYS B 1 12  ? 4.42794   3.33651   -10.72622 1.000 45.59409  ? 44   LYS B CB  1 
ATOM   1511 C  CG  . LYS B 1 12  ? 3.30360   3.83380   -9.79917  1.000 50.92058  ? 44   LYS B CG  1 
ATOM   1512 C  CD  . LYS B 1 12  ? 2.91105   2.69030   -8.84479  1.000 53.25377  ? 44   LYS B CD  1 
ATOM   1513 C  CE  . LYS B 1 12  ? 2.20824   3.19192   -7.59265  1.000 56.19116  ? 44   LYS B CE  1 
ATOM   1514 N  NZ  . LYS B 1 12  ? 3.23705   3.28368   -6.48849  1.000 71.06453  ? 44   LYS B NZ  1 
ATOM   1515 N  N   . VAL B 1 13  ? 6.22805   2.47688   -13.15836 1.000 36.02354  ? 45   VAL B N   1 
ATOM   1516 C  CA  . VAL B 1 13  ? 7.55149   2.16309   -13.68877 1.000 34.18701  ? 45   VAL B CA  1 
ATOM   1517 C  C   . VAL B 1 13  ? 7.86559   3.05646   -14.87775 1.000 38.57926  ? 45   VAL B C   1 
ATOM   1518 O  O   . VAL B 1 13  ? 8.98019   3.57672   -15.00258 1.000 37.81369  ? 45   VAL B O   1 
ATOM   1519 C  CB  . VAL B 1 13  ? 7.65988   0.67251   -14.05609 1.000 32.40404  ? 45   VAL B CB  1 
ATOM   1520 C  CG1 . VAL B 1 13  ? 8.97091   0.40845   -14.76517 1.000 34.37330  ? 45   VAL B CG1 1 
ATOM   1521 C  CG2 . VAL B 1 13  ? 7.58776   -0.20156  -12.79529 1.000 37.48488  ? 45   VAL B CG2 1 
ATOM   1522 N  N   . LEU B 1 14  ? 6.88103   3.26850   -15.75521 1.000 35.50289  ? 46   LEU B N   1 
ATOM   1523 C  CA  . LEU B 1 14  ? 7.10553   4.12982   -16.90936 1.000 39.26960  ? 46   LEU B CA  1 
ATOM   1524 C  C   . LEU B 1 14  ? 7.51725   5.52594   -16.46441 1.000 40.95873  ? 46   LEU B C   1 
ATOM   1525 O  O   . LEU B 1 14  ? 8.39805   6.14382   -17.07090 1.000 43.81775  ? 46   LEU B O   1 
ATOM   1526 C  CB  . LEU B 1 14  ? 5.84764   4.18292   -17.77625 1.000 36.33487  ? 46   LEU B CB  1 
ATOM   1527 C  CG  . LEU B 1 14  ? 5.88509   5.12399   -18.97675 1.000 37.03447  ? 46   LEU B CG  1 
ATOM   1528 C  CD1 . LEU B 1 14  ? 7.02443   4.75939   -19.91204 1.000 36.10973  ? 46   LEU B CD1 1 
ATOM   1529 C  CD2 . LEU B 1 14  ? 4.56423   5.06144   -19.69249 1.000 37.72983  ? 46   LEU B CD2 1 
ATOM   1530 N  N   . LYS B 1 15  ? 6.92844   6.02556   -15.37573 1.000 45.66789  ? 47   LYS B N   1 
ATOM   1531 C  CA  . LYS B 1 15  ? 7.27595   7.38116   -14.96797 1.000 47.59448  ? 47   LYS B CA  1 
ATOM   1532 C  C   . LYS B 1 15  ? 8.69717   7.45648   -14.42279 1.000 46.60688  ? 47   LYS B C   1 
ATOM   1533 O  O   . LYS B 1 15  ? 9.30064   8.53321   -14.45054 1.000 48.73015  ? 47   LYS B O   1 
ATOM   1534 C  CB  . LYS B 1 15  ? 6.30992   7.91552   -13.90921 1.000 55.57291  ? 47   LYS B CB  1 
ATOM   1535 C  CG  . LYS B 1 15  ? 4.83432   8.10962   -14.34428 1.000 64.91054  ? 47   LYS B CG  1 
ATOM   1536 C  CD  . LYS B 1 15  ? 4.57337   8.15367   -15.85535 1.000 63.28248  ? 47   LYS B CD  1 
ATOM   1537 C  CE  . LYS B 1 15  ? 5.06063   9.39193   -16.57713 1.000 66.20724  ? 47   LYS B CE  1 
ATOM   1538 N  NZ  . LYS B 1 15  ? 5.33245   8.98418   -17.99238 1.000 50.50730  ? 47   LYS B NZ  1 
ATOM   1539 N  N   . GLN B 1 16  ? 9.25240   6.33705   -13.94529 1.000 49.37688  ? 48   GLN B N   1 
ATOM   1540 C  CA  . GLN B 1 16  ? 10.64590  6.32378   -13.50519 1.000 48.15467  ? 48   GLN B CA  1 
ATOM   1541 C  C   . GLN B 1 16  ? 11.60471  6.35123   -14.68621 1.000 50.09714  ? 48   GLN B C   1 
ATOM   1542 O  O   . GLN B 1 16  ? 12.59236  7.09236   -14.67552 1.000 50.79505  ? 48   GLN B O   1 
ATOM   1543 C  CB  . GLN B 1 16  ? 10.92840  5.08212   -12.65756 1.000 51.57113  ? 48   GLN B CB  1 
ATOM   1544 C  CG  . GLN B 1 16  ? 10.25488  5.02589   -11.31204 1.000 54.28270  ? 48   GLN B CG  1 
ATOM   1545 C  CD  . GLN B 1 16  ? 10.54369  3.70542   -10.61500 1.000 61.17138  ? 48   GLN B CD  1 
ATOM   1546 O  OE1 . GLN B 1 16  ? 10.77808  2.68572   -11.27114 1.000 58.59377  ? 48   GLN B OE1 1 
ATOM   1547 N  NE2 . GLN B 1 16  ? 10.53207  3.71607   -9.28950  1.000 64.39417  ? 48   GLN B NE2 1 
ATOM   1548 N  N   . VAL B 1 17  ? 11.35212  5.52087   -15.69944 1.000 45.72900  ? 49   VAL B N   1 
ATOM   1549 C  CA  . VAL B 1 17  ? 12.31837  5.37003   -16.78409 1.000 48.28103  ? 49   VAL B CA  1 
ATOM   1550 C  C   . VAL B 1 17  ? 12.12571  6.40419   -17.88991 1.000 41.43994  ? 49   VAL B C   1 
ATOM   1551 O  O   . VAL B 1 17  ? 13.08891  6.74406   -18.58253 1.000 43.29548  ? 49   VAL B O   1 
ATOM   1552 C  CB  . VAL B 1 17  ? 12.28259  3.94409   -17.36341 1.000 46.79164  ? 49   VAL B CB  1 
ATOM   1553 C  CG1 . VAL B 1 17  ? 12.54852  2.90231   -16.26657 1.000 45.90022  ? 49   VAL B CG1 1 
ATOM   1554 C  CG2 . VAL B 1 17  ? 10.96444  3.66565   -18.06263 1.000 42.40157  ? 49   VAL B CG2 1 
ATOM   1555 N  N   . HIS B 1 18  ? 10.90333  6.90003   -18.09322 1.000 42.46178  ? 50   HIS B N   1 
ATOM   1556 C  CA  . HIS B 1 18  ? 10.62110  7.92427   -19.10513 1.000 43.26654  ? 50   HIS B CA  1 
ATOM   1557 C  C   . HIS B 1 18  ? 9.56875   8.87328   -18.55298 1.000 48.74919  ? 50   HIS B C   1 
ATOM   1558 O  O   . HIS B 1 18  ? 8.37301   8.74702   -18.84915 1.000 45.22104  ? 50   HIS B O   1 
ATOM   1559 C  CB  . HIS B 1 18  ? 10.15149  7.30065   -20.42744 1.000 44.09361  ? 50   HIS B CB  1 
ATOM   1560 C  CG  . HIS B 1 18  ? 11.22920  6.59992   -21.19590 1.000 41.29260  ? 50   HIS B CG  1 
ATOM   1561 N  ND1 . HIS B 1 18  ? 12.28088  7.27142   -21.78533 1.000 49.29645  ? 50   HIS B ND1 1 
ATOM   1562 C  CD2 . HIS B 1 18  ? 11.38762  5.29299   -21.52005 1.000 36.04985  ? 50   HIS B CD2 1 
ATOM   1563 C  CE1 . HIS B 1 18  ? 13.05764  6.40334   -22.41079 1.000 42.16458  ? 50   HIS B CE1 1 
ATOM   1564 N  NE2 . HIS B 1 18  ? 12.54162  5.19597   -22.25965 1.000 35.51873  ? 50   HIS B NE2 1 
ATOM   1565 N  N   . PRO B 1 19  ? 9.98674   9.86039   -17.75399 1.000 49.85541  ? 51   PRO B N   1 
ATOM   1566 C  CA  . PRO B 1 19  ? 9.01120   10.68037  -17.01055 1.000 47.18566  ? 51   PRO B CA  1 
ATOM   1567 C  C   . PRO B 1 19  ? 8.00425   11.42469  -17.87120 1.000 54.22946  ? 51   PRO B C   1 
ATOM   1568 O  O   . PRO B 1 19  ? 6.89466   11.69815  -17.39874 1.000 52.38137  ? 51   PRO B O   1 
ATOM   1569 C  CB  . PRO B 1 19  ? 9.90851   11.65033  -16.22761 1.000 51.91701  ? 51   PRO B CB  1 
ATOM   1570 C  CG  . PRO B 1 19  ? 11.20188  10.91423  -16.07619 1.000 52.38144  ? 51   PRO B CG  1 
ATOM   1571 C  CD  . PRO B 1 19  ? 11.37316  10.13588  -17.34551 1.000 53.69812  ? 51   PRO B CD  1 
ATOM   1572 N  N   . ASP B 1 20  ? 8.34291   11.76760  -19.11169 1.000 51.10178  ? 52   ASP B N   1 
ATOM   1573 C  CA  . ASP B 1 20  ? 7.47356   12.58538  -19.94764 1.000 49.77656  ? 52   ASP B CA  1 
ATOM   1574 C  C   . ASP B 1 20  ? 6.84065   11.80039  -21.09563 1.000 49.41000  ? 52   ASP B C   1 
ATOM   1575 O  O   . ASP B 1 20  ? 6.36521   12.40422  -22.06349 1.000 49.02609  ? 52   ASP B O   1 
ATOM   1576 C  CB  . ASP B 1 20  ? 8.25735   13.78254  -20.48402 1.000 59.11080  ? 52   ASP B CB  1 
ATOM   1577 C  CG  . ASP B 1 20  ? 8.75397   14.69293  -19.37295 1.000 61.91328  ? 52   ASP B CG  1 
ATOM   1578 O  OD1 . ASP B 1 20  ? 7.99321   14.90578  -18.40625 1.000 64.90854  ? 52   ASP B OD1 1 
ATOM   1579 O  OD2 . ASP B 1 20  ? 9.89910   15.18618  -19.45670 1.000 69.65736  ? 52   ASP B OD2 1 
ATOM   1580 N  N   . THR B 1 21  ? 6.80818   10.47370  -21.00632 1.000 46.41734  ? 53   THR B N   1 
ATOM   1581 C  CA  . THR B 1 21  ? 6.29682   9.63075   -22.08063 1.000 42.71709  ? 53   THR B CA  1 
ATOM   1582 C  C   . THR B 1 21  ? 5.02462   8.92164   -21.64032 1.000 39.34268  ? 53   THR B C   1 
ATOM   1583 O  O   . THR B 1 21  ? 4.99916   8.28864   -20.57930 1.000 44.02872  ? 53   THR B O   1 
ATOM   1584 C  CB  . THR B 1 21  ? 7.33983   8.60238   -22.49797 1.000 45.22101  ? 53   THR B CB  1 
ATOM   1585 O  OG1 . THR B 1 21  ? 8.50939   9.29228   -22.94625 1.000 44.35605  ? 53   THR B OG1 1 
ATOM   1586 C  CG2 . THR B 1 21  ? 6.79520   7.72246   -23.62563 1.000 41.39557  ? 53   THR B CG2 1 
ATOM   1587 N  N   . GLY B 1 22  ? 3.97158   9.02913   -22.45948 1.000 42.61216  ? 54   GLY B N   1 
ATOM   1588 C  CA  . GLY B 1 22  ? 2.73810   8.31381   -22.21180 1.000 39.61986  ? 54   GLY B CA  1 
ATOM   1589 C  C   . GLY B 1 22  ? 2.76266   6.90848   -22.78955 1.000 37.20941  ? 54   GLY B C   1 
ATOM   1590 O  O   . GLY B 1 22  ? 3.75445   6.44184   -23.34925 1.000 34.15245  ? 54   GLY B O   1 
ATOM   1591 N  N   . ILE B 1 23  ? 1.63683   6.21670   -22.63496 1.000 36.56537  ? 55   ILE B N   1 
ATOM   1592 C  CA  . ILE B 1 23  ? 1.46753   4.89364   -23.23581 1.000 33.32140  ? 55   ILE B CA  1 
ATOM   1593 C  C   . ILE B 1 23  ? 0.00420   4.71817   -23.62945 1.000 38.30162  ? 55   ILE B C   1 
ATOM   1594 O  O   . ILE B 1 23  ? -0.90121  5.01192   -22.84359 1.000 37.60212  ? 55   ILE B O   1 
ATOM   1595 C  CB  . ILE B 1 23  ? 1.98110   3.78642   -22.28974 1.000 35.28613  ? 55   ILE B CB  1 
ATOM   1596 C  CG1 . ILE B 1 23  ? 1.91371   2.41882   -22.97770 1.000 29.00283  ? 55   ILE B CG1 1 
ATOM   1597 C  CG2 . ILE B 1 23  ? 1.30110   3.85518   -20.90190 1.000 37.65591  ? 55   ILE B CG2 1 
ATOM   1598 C  CD1 . ILE B 1 23  ? 2.60087   1.28455   -22.16703 1.000 29.25273  ? 55   ILE B CD1 1 
ATOM   1599 N  N   . SER B 1 24  ? -0.22787  4.25308   -24.85656 1.000 33.17164  ? 56   SER B N   1 
ATOM   1600 C  CA  . SER B 1 24  ? -1.59225  4.14678   -25.35703 1.000 35.38306  ? 56   SER B CA  1 
ATOM   1601 C  C   . SER B 1 24  ? -2.31892  2.98520   -24.69061 1.000 36.98157  ? 56   SER B C   1 
ATOM   1602 O  O   . SER B 1 24  ? -1.70395  2.08978   -24.10558 1.000 36.32600  ? 56   SER B O   1 
ATOM   1603 C  CB  . SER B 1 24  ? -1.61677  3.95394   -26.87927 1.000 38.07822  ? 56   SER B CB  1 
ATOM   1604 O  OG  . SER B 1 24  ? -1.26450  2.61278   -27.20332 1.000 36.34604  ? 56   SER B OG  1 
ATOM   1605 N  N   . SER B 1 25  ? -3.65278  3.00321   -24.79586 1.000 38.71761  ? 57   SER B N   1 
ATOM   1606 C  CA  A SER B 1 25  ? -4.44408  1.93715   -24.18913 0.500 40.38787  ? 57   SER B CA  1 
ATOM   1607 C  CA  B SER B 1 25  ? -4.44743  1.93437   -24.19361 0.500 40.38829  ? 57   SER B CA  1 
ATOM   1608 C  C   . SER B 1 25  ? -4.04852  0.57444   -24.74872 1.000 38.03236  ? 57   SER B C   1 
ATOM   1609 O  O   . SER B 1 25  ? -3.87594  -0.38837  -23.99399 1.000 36.18604  ? 57   SER B O   1 
ATOM   1610 C  CB  A SER B 1 25  ? -5.93465  2.20448   -24.40865 0.500 44.24930  ? 57   SER B CB  1 
ATOM   1611 C  CB  B SER B 1 25  ? -5.93611  2.18812   -24.42862 0.500 44.24761  ? 57   SER B CB  1 
ATOM   1612 O  OG  A SER B 1 25  ? -6.71996  1.17138   -23.84130 0.500 44.97644  ? 57   SER B OG  1 
ATOM   1613 O  OG  B SER B 1 25  ? -6.35533  3.34845   -23.74632 0.500 45.67210  ? 57   SER B OG  1 
ATOM   1614 N  N   . LYS B 1 26  ? -3.87410  0.47577   -26.06802 1.000 40.31504  ? 58   LYS B N   1 
ATOM   1615 C  CA  . LYS B 1 26  ? -3.51435  -0.81802  -26.64372 1.000 38.28300  ? 58   LYS B CA  1 
ATOM   1616 C  C   . LYS B 1 26  ? -2.09496  -1.22548  -26.29244 1.000 37.89385  ? 58   LYS B C   1 
ATOM   1617 O  O   . LYS B 1 26  ? -1.81834  -2.42277  -26.17352 1.000 34.82910  ? 58   LYS B O   1 
ATOM   1618 C  CB  . LYS B 1 26  ? -3.72486  -0.80115  -28.15739 1.000 35.97105  ? 58   LYS B CB  1 
ATOM   1619 C  CG  . LYS B 1 26  ? -5.19432  -0.68502  -28.53609 1.000 36.83462  ? 58   LYS B CG  1 
ATOM   1620 C  CD  . LYS B 1 26  ? -5.43473  -1.13649  -29.97188 1.000 44.54098  ? 58   LYS B CD  1 
ATOM   1621 C  CE  . LYS B 1 26  ? -6.82542  -0.75973  -30.41775 1.000 50.48697  ? 58   LYS B CE  1 
ATOM   1622 N  NZ  . LYS B 1 26  ? -7.03875  -0.89356  -31.88934 1.000 66.13414  ? 58   LYS B NZ  1 
ATOM   1623 N  N   . ALA B 1 27  ? -1.17156  -0.26787  -26.15631 1.000 33.57624  ? 59   ALA B N   1 
ATOM   1624 C  CA  . ALA B 1 27  ? 0.16916   -0.62713  -25.70156 1.000 35.56609  ? 59   ALA B CA  1 
ATOM   1625 C  C   . ALA B 1 27  ? 0.15132   -1.10616  -24.25126 1.000 30.85861  ? 59   ALA B C   1 
ATOM   1626 O  O   . ALA B 1 27  ? 0.88590   -2.03241  -23.89191 1.000 30.33673  ? 59   ALA B O   1 
ATOM   1627 C  CB  . ALA B 1 27  ? 1.13019   0.55295   -25.86993 1.000 36.56712  ? 59   ALA B CB  1 
ATOM   1628 N  N   . MET B 1 28  ? -0.68015  -0.49644  -23.40209 1.000 31.83701  ? 60   MET B N   1 
ATOM   1629 C  CA  . MET B 1 28  ? -0.77477  -0.96411  -22.01815 1.000 32.15815  ? 60   MET B CA  1 
ATOM   1630 C  C   . MET B 1 28  ? -1.32115  -2.38583  -21.96257 1.000 32.62308  ? 60   MET B C   1 
ATOM   1631 O  O   . MET B 1 28  ? -0.87345  -3.19900  -21.14081 1.000 33.51909  ? 60   MET B O   1 
ATOM   1632 C  CB  . MET B 1 28  ? -1.64757  -0.02563  -21.17875 1.000 32.77553  ? 60   MET B CB  1 
ATOM   1633 C  CG  . MET B 1 28  ? -1.82552  -0.57825  -19.75907 1.000 34.76116  ? 60   MET B CG  1 
ATOM   1634 S  SD  . MET B 1 28  ? -0.27961  -0.47101  -18.82716 1.000 36.83586  ? 60   MET B SD  1 
ATOM   1635 C  CE  . MET B 1 28  ? -0.19710  1.27731   -18.42518 1.000 37.58141  ? 60   MET B CE  1 
ATOM   1636 N  N   . SER B 1 29  ? -2.27038  -2.70637  -22.83322 1.000 34.26247  ? 61   SER B N   1 
ATOM   1637 C  CA  A SER B 1 29  ? -2.81130  -4.06186  -22.87807 0.368 37.45696  ? 61   SER B CA  1 
ATOM   1638 C  CA  B SER B 1 29  ? -2.80728  -4.06331  -22.86712 0.632 37.60204  ? 61   SER B CA  1 
ATOM   1639 C  C   . SER B 1 29  ? -1.72236  -5.07239  -23.21818 1.000 35.85661  ? 61   SER B C   1 
ATOM   1640 O  O   . SER B 1 29  ? -1.66244  -6.16025  -22.62994 1.000 32.31266  ? 61   SER B O   1 
ATOM   1641 C  CB  A SER B 1 29  ? -3.95789  -4.12887  -23.89017 0.368 38.99010  ? 61   SER B CB  1 
ATOM   1642 C  CB  B SER B 1 29  ? -3.96457  -4.14856  -23.86003 0.632 38.81152  ? 61   SER B CB  1 
ATOM   1643 O  OG  A SER B 1 29  ? -4.50651  -5.43198  -23.97050 0.368 36.07520  ? 61   SER B OG  1 
ATOM   1644 O  OG  B SER B 1 29  ? -5.06535  -3.37563  -23.42941 0.632 39.14638  ? 61   SER B OG  1 
ATOM   1645 N  N   . ILE B 1 30  ? -0.85369  -4.73316  -24.16896 1.000 30.74929  ? 62   ILE B N   1 
ATOM   1646 C  CA  . ILE B 1 30  ? 0.27972   -5.60573  -24.49224 1.000 29.39635  ? 62   ILE B CA  1 
ATOM   1647 C  C   . ILE B 1 30  ? 1.21291   -5.75392  -23.29703 1.000 32.24466  ? 62   ILE B C   1 
ATOM   1648 O  O   . ILE B 1 30  ? 1.66429   -6.86618  -22.97263 1.000 31.15443  ? 62   ILE B O   1 
ATOM   1649 C  CB  . ILE B 1 30  ? 1.00836   -5.07395  -25.74875 1.000 31.53577  ? 62   ILE B CB  1 
ATOM   1650 C  CG1 . ILE B 1 30  ? 0.10893   -5.23279  -26.95643 1.000 33.72870  ? 62   ILE B CG1 1 
ATOM   1651 C  CG2 . ILE B 1 30  ? 2.35459   -5.80719  -25.93662 1.000 30.79221  ? 62   ILE B CG2 1 
ATOM   1652 C  CD1 . ILE B 1 30  ? 0.61603   -4.55034  -28.24522 1.000 36.68384  ? 62   ILE B CD1 1 
ATOM   1653 N  N   . MET B 1 31  ? 1.49364   -4.65180  -22.59416 1.000 28.54997  ? 63   MET B N   1 
ATOM   1654 C  CA  . MET B 1 31  ? 2.32495   -4.72621  -21.39329 1.000 28.96515  ? 63   MET B CA  1 
ATOM   1655 C  C   . MET B 1 31  ? 1.72345   -5.66953  -20.36056 1.000 33.67475  ? 63   MET B C   1 
ATOM   1656 O  O   . MET B 1 31  ? 2.43275   -6.49045  -19.75541 1.000 29.48575  ? 63   MET B O   1 
ATOM   1657 C  CB  . MET B 1 31  ? 2.47350   -3.32840  -20.79833 1.000 29.10624  ? 63   MET B CB  1 
ATOM   1658 C  CG  . MET B 1 31  ? 3.59151   -2.42633  -21.37121 1.000 30.63588  ? 63   MET B CG  1 
ATOM   1659 S  SD  . MET B 1 31  ? 5.17046   -3.17851  -21.75570 1.000 30.60338  ? 63   MET B SD  1 
ATOM   1660 C  CE  . MET B 1 31  ? 5.75894   -3.34973  -20.05651 1.000 29.15850  ? 63   MET B CE  1 
ATOM   1661 N  N   . ASN B 1 32  ? 0.41732   -5.54990  -20.14004 1.000 32.24425  ? 64   ASN B N   1 
ATOM   1662 C  CA  A ASN B 1 32  ? -0.26311  -6.43591  -19.19764 0.490 32.92598  ? 64   ASN B CA  1 
ATOM   1663 C  CA  B ASN B 1 32  ? -0.26885  -6.42993  -19.20238 0.510 33.24590  ? 64   ASN B CA  1 
ATOM   1664 C  C   . ASN B 1 32  ? -0.13265  -7.89087  -19.61999 1.000 35.47669  ? 64   ASN B C   1 
ATOM   1665 O  O   . ASN B 1 32  ? 0.10058   -8.77126  -18.77880 1.000 33.76918  ? 64   ASN B O   1 
ATOM   1666 C  CB  A ASN B 1 32  ? -1.73773  -6.06108  -19.08191 0.490 37.24208  ? 64   ASN B CB  1 
ATOM   1667 C  CB  B ASN B 1 32  ? -1.73625  -6.02414  -19.12168 0.510 37.82475  ? 64   ASN B CB  1 
ATOM   1668 C  CG  A ASN B 1 32  ? -1.99644  -5.02247  -18.01460 0.490 37.76949  ? 64   ASN B CG  1 
ATOM   1669 C  CG  B ASN B 1 32  ? -2.46680  -6.70899  -18.00001 0.510 40.24379  ? 64   ASN B CG  1 
ATOM   1670 O  OD1 A ASN B 1 32  ? -1.25439  -4.90812  -17.03915 0.490 41.32505  ? 64   ASN B OD1 1 
ATOM   1671 O  OD1 B ASN B 1 32  ? -1.96770  -6.79339  -16.87455 0.510 42.83174  ? 64   ASN B OD1 1 
ATOM   1672 N  ND2 A ASN B 1 32  ? -3.06836  -4.26647  -18.18567 0.490 39.14123  ? 64   ASN B ND2 1 
ATOM   1673 N  ND2 B ASN B 1 32  ? -3.66034  -7.20470  -18.29606 0.510 43.06395  ? 64   ASN B ND2 1 
ATOM   1674 N  N   . SER B 1 33  ? -0.27033  -8.16446  -20.91825 1.000 29.42671  ? 65   SER B N   1 
ATOM   1675 C  CA  A SER B 1 33  ? -0.12444  -9.53760  -21.39843 0.570 32.80174  ? 65   SER B CA  1 
ATOM   1676 C  CA  B SER B 1 33  ? -0.12578  -9.53724  -21.40143 0.430 33.70009  ? 65   SER B CA  1 
ATOM   1677 C  C   . SER B 1 33  ? 1.29404   -10.05387 -21.19925 1.000 32.33373  ? 65   SER B C   1 
ATOM   1678 O  O   . SER B 1 33  ? 1.48647   -11.23771 -20.88739 1.000 32.77409  ? 65   SER B O   1 
ATOM   1679 C  CB  A SER B 1 33  ? -0.52072  -9.62684  -22.86865 0.570 32.88377  ? 65   SER B CB  1 
ATOM   1680 C  CB  B SER B 1 33  ? -0.52205  -9.63120  -22.87579 0.430 32.77042  ? 65   SER B CB  1 
ATOM   1681 O  OG  A SER B 1 33  ? -1.87897  -9.26688  -23.03109 0.570 32.55571  ? 65   SER B OG  1 
ATOM   1682 O  OG  B SER B 1 33  ? 0.50337   -9.14495  -23.72455 0.430 36.42405  ? 65   SER B OG  1 
ATOM   1683 N  N   . PHE B 1 34  ? 2.30579   -9.19617  -21.39919 1.000 26.54411  ? 66   PHE B N   1 
ATOM   1684 C  CA  . PHE B 1 34  ? 3.68563   -9.62681  -21.15967 1.000 27.83937  ? 66   PHE B CA  1 
ATOM   1685 C  C   . PHE B 1 34  ? 3.89418   -10.00468 -19.69466 1.000 31.94178  ? 66   PHE B C   1 
ATOM   1686 O  O   . PHE B 1 34  ? 4.45468   -11.06644 -19.38449 1.000 29.80983  ? 66   PHE B O   1 
ATOM   1687 C  CB  . PHE B 1 34  ? 4.67861   -8.51561  -21.49697 1.000 28.08115  ? 66   PHE B CB  1 
ATOM   1688 C  CG  . PHE B 1 34  ? 4.86397   -8.23900  -22.97003 1.000 26.96676  ? 66   PHE B CG  1 
ATOM   1689 C  CD1 . PHE B 1 34  ? 4.59315   -9.18749  -23.94766 1.000 27.27727  ? 66   PHE B CD1 1 
ATOM   1690 C  CD2 . PHE B 1 34  ? 5.39129   -7.01753  -23.35241 1.000 30.48276  ? 66   PHE B CD2 1 
ATOM   1691 C  CE1 . PHE B 1 34  ? 4.81672   -8.88411  -25.31079 1.000 31.79247  ? 66   PHE B CE1 1 
ATOM   1692 C  CE2 . PHE B 1 34  ? 5.61080   -6.72121  -24.68234 1.000 30.55932  ? 66   PHE B CE2 1 
ATOM   1693 C  CZ  . PHE B 1 34  ? 5.34191   -7.64909  -25.65667 1.000 32.05204  ? 66   PHE B CZ  1 
ATOM   1694 N  N   . VAL B 1 35  ? 3.46453   -9.13049  -18.77195 1.000 26.82097  ? 67   VAL B N   1 
ATOM   1695 C  CA  . VAL B 1 35  ? 3.67801   -9.40905  -17.35291 1.000 26.82402  ? 67   VAL B CA  1 
ATOM   1696 C  C   . VAL B 1 35  ? 2.92562   -10.66786 -16.95273 1.000 28.40226  ? 67   VAL B C   1 
ATOM   1697 O  O   . VAL B 1 35  ? 3.45309   -11.53012 -16.22800 1.000 28.10858  ? 67   VAL B O   1 
ATOM   1698 C  CB  . VAL B 1 35  ? 3.25789   -8.20659  -16.48883 1.000 31.69259  ? 67   VAL B CB  1 
ATOM   1699 C  CG1 . VAL B 1 35  ? 3.44516   -8.55016  -15.02953 1.000 34.23884  ? 67   VAL B CG1 1 
ATOM   1700 C  CG2 . VAL B 1 35  ? 4.08842   -6.98806  -16.83074 1.000 30.13113  ? 67   VAL B CG2 1 
ATOM   1701 N  N   . ASN B 1 36  ? 1.68322   -10.79334 -17.41127 1.000 27.81467  ? 68   ASN B N   1 
ATOM   1702 C  CA  A ASN B 1 36  ? 0.88321   -11.96745 -17.07438 0.510 30.00115  ? 68   ASN B CA  1 
ATOM   1703 C  CA  B ASN B 1 36  ? 0.90072   -11.96802 -17.05123 0.490 30.92383  ? 68   ASN B CA  1 
ATOM   1704 C  C   . ASN B 1 36  ? 1.53618   -13.24297 -17.58844 1.000 31.67878  ? 68   ASN B C   1 
ATOM   1705 O  O   . ASN B 1 36  ? 1.55158   -14.27020 -16.89646 1.000 30.51061  ? 68   ASN B O   1 
ATOM   1706 C  CB  A ASN B 1 36  ? -0.52673  -11.82657 -17.64707 0.510 32.90486  ? 68   ASN B CB  1 
ATOM   1707 C  CB  B ASN B 1 36  ? -0.53040  -11.84588 -17.55601 0.490 32.19189  ? 68   ASN B CB  1 
ATOM   1708 C  CG  A ASN B 1 36  ? -1.44007  -11.02184 -16.74843 0.510 34.65180  ? 68   ASN B CG  1 
ATOM   1709 C  CG  B ASN B 1 36  ? -1.36568  -13.04373 -17.17610 0.490 35.10750  ? 68   ASN B CG  1 
ATOM   1710 O  OD1 A ASN B 1 36  ? -1.40096  -11.16530 -15.53011 0.510 37.04864  ? 68   ASN B OD1 1 
ATOM   1711 O  OD1 B ASN B 1 36  ? -1.82031  -13.16080 -16.03761 0.490 37.27204  ? 68   ASN B OD1 1 
ATOM   1712 N  ND2 A ASN B 1 36  ? -2.25911  -10.16401 -17.34111 0.510 37.68679  ? 68   ASN B ND2 1 
ATOM   1713 N  ND2 B ASN B 1 36  ? -1.55361  -13.95349 -18.11697 0.490 33.92979  ? 68   ASN B ND2 1 
ATOM   1714 N  N   . ASP B 1 37  ? 2.05611   -13.20423 -18.81436 1.000 29.32491  ? 69   ASP B N   1 
ATOM   1715 C  CA  . ASP B 1 37  ? 2.66195   -14.40468 -19.38437 1.000 28.44144  ? 69   ASP B CA  1 
ATOM   1716 C  C   . ASP B 1 37  ? 3.89080   -14.82597 -18.59214 1.000 30.21182  ? 69   ASP B C   1 
ATOM   1717 O  O   . ASP B 1 37  ? 4.08476   -16.01814 -18.31955 1.000 30.91633  ? 69   ASP B O   1 
ATOM   1718 C  CB  . ASP B 1 37  ? 3.03398   -14.17295 -20.84675 1.000 30.25388  ? 69   ASP B CB  1 
ATOM   1719 C  CG  . ASP B 1 37  ? 3.49363   -15.44178 -21.52366 1.000 39.35465  ? 69   ASP B CG  1 
ATOM   1720 O  OD1 . ASP B 1 37  ? 2.63559   -16.29433 -21.82210 1.000 44.17715  ? 69   ASP B OD1 1 
ATOM   1721 O  OD2 . ASP B 1 37  ? 4.70983   -15.58861 -21.74000 1.000 41.55817  ? 69   ASP B OD2 1 
ATOM   1722 N  N   . VAL B 1 38  ? 4.73829   -13.86437 -18.22402 1.000 26.57650  ? 70   VAL B N   1 
ATOM   1723 C  CA  . VAL B 1 38  ? 5.93401   -14.19145 -17.44716 1.000 25.70522  ? 70   VAL B CA  1 
ATOM   1724 C  C   . VAL B 1 38  ? 5.54888   -14.68950 -16.06072 1.000 27.94968  ? 70   VAL B C   1 
ATOM   1725 O  O   . VAL B 1 38  ? 6.15346   -15.63490 -15.53404 1.000 27.92547  ? 70   VAL B O   1 
ATOM   1726 C  CB  . VAL B 1 38  ? 6.88955   -12.98339 -17.37547 1.000 24.90256  ? 70   VAL B CB  1 
ATOM   1727 C  CG1 . VAL B 1 38  ? 8.08534   -13.31348 -16.46569 1.000 26.13509  ? 70   VAL B CG1 1 
ATOM   1728 C  CG2 . VAL B 1 38  ? 7.39778   -12.61893 -18.78799 1.000 28.80224  ? 70   VAL B CG2 1 
ATOM   1729 N  N   . PHE B 1 39  ? 4.57072   -14.04412 -15.42574 1.000 25.15962  ? 71   PHE B N   1 
ATOM   1730 C  CA  . PHE B 1 39  ? 4.10790   -14.53928 -14.13347 1.000 25.31282  ? 71   PHE B CA  1 
ATOM   1731 C  C   . PHE B 1 39  ? 3.66737   -15.99557 -14.23647 1.000 25.38978  ? 71   PHE B C   1 
ATOM   1732 O  O   . PHE B 1 39  ? 4.07688   -16.84130 -13.42640 1.000 27.17507  ? 71   PHE B O   1 
ATOM   1733 C  CB  . PHE B 1 39  ? 2.95244   -13.68235 -13.61387 1.000 25.12928  ? 71   PHE B CB  1 
ATOM   1734 C  CG  . PHE B 1 39  ? 2.30450   -14.25356 -12.37280 1.000 25.63306  ? 71   PHE B CG  1 
ATOM   1735 C  CD1 . PHE B 1 39  ? 1.30957   -15.23028 -12.45951 1.000 29.76396  ? 71   PHE B CD1 1 
ATOM   1736 C  CD2 . PHE B 1 39  ? 2.72812   -13.86313 -11.12561 1.000 27.47744  ? 71   PHE B CD2 1 
ATOM   1737 C  CE1 . PHE B 1 39  ? 0.74364   -15.77867 -11.31848 1.000 34.03030  ? 71   PHE B CE1 1 
ATOM   1738 C  CE2 . PHE B 1 39  ? 2.14328   -14.41296 -9.97281  1.000 29.14924  ? 71   PHE B CE2 1 
ATOM   1739 C  CZ  . PHE B 1 39  ? 1.16182   -15.36635 -10.08307 1.000 32.48591  ? 71   PHE B CZ  1 
ATOM   1740 N  N   . GLU B 1 40  ? 2.83506   -16.30562 -15.23721 1.000 25.37082  ? 72   GLU B N   1 
ATOM   1741 C  CA  . GLU B 1 40  ? 2.25774   -17.64411 -15.35229 1.000 28.89019  ? 72   GLU B CA  1 
ATOM   1742 C  C   . GLU B 1 40  ? 3.33880   -18.69769 -15.56629 1.000 27.77213  ? 72   GLU B C   1 
ATOM   1743 O  O   . GLU B 1 40  ? 3.27524   -19.80121 -14.99830 1.000 26.26534  ? 72   GLU B O   1 
ATOM   1744 C  CB  . GLU B 1 40  ? 1.24284   -17.66959 -16.50063 1.000 34.36920  ? 72   GLU B CB  1 
ATOM   1745 C  CG  . GLU B 1 40  ? -0.06656  -16.97340 -16.13548 1.000 36.41809  ? 72   GLU B CG  1 
ATOM   1746 C  CD  . GLU B 1 40  ? -1.08713  -16.98799 -17.26039 1.000 47.53344  ? 72   GLU B CD  1 
ATOM   1747 O  OE1 . GLU B 1 40  ? -0.75292  -17.43011 -18.38679 1.000 44.12657  ? 72   GLU B OE1 1 
ATOM   1748 O  OE2 . GLU B 1 40  ? -2.22879  -16.54818 -17.01188 1.000 46.47156  ? 72   GLU B OE2 1 
ATOM   1749 N  N   . ARG B 1 41  ? 4.32725   -18.38499 -16.39807 1.000 25.42769  ? 73   ARG B N   1 
ATOM   1750 C  CA  . ARG B 1 41  ? 5.34400   -19.38103 -16.70819 1.000 26.06724  ? 73   ARG B CA  1 
ATOM   1751 C  C   . ARG B 1 41  ? 6.32029   -19.55150 -15.55004 1.000 25.21759  ? 73   ARG B C   1 
ATOM   1752 O  O   . ARG B 1 41  ? 6.71876   -20.68606 -15.23954 1.000 26.90417  ? 73   ARG B O   1 
ATOM   1753 C  CB  . ARG B 1 41  ? 6.01932   -19.02496 -18.03578 1.000 26.28209  ? 73   ARG B CB  1 
ATOM   1754 C  CG  . ARG B 1 41  ? 5.01680   -19.14967 -19.19080 1.000 27.49206  ? 73   ARG B CG  1 
ATOM   1755 C  CD  . ARG B 1 41  ? 5.72743   -19.10480 -20.54944 1.000 30.50688  ? 73   ARG B CD  1 
ATOM   1756 N  NE  . ARG B 1 41  ? 6.13449   -17.73675 -20.80896 1.000 33.62823  ? 73   ARG B NE  1 
ATOM   1757 C  CZ  . ARG B 1 41  ? 7.21299   -17.35883 -21.48315 1.000 41.76753  ? 73   ARG B CZ  1 
ATOM   1758 N  NH1 . ARG B 1 41  ? 8.06120   -18.23893 -21.98527 1.000 43.48494  ? 73   ARG B NH1 1 
ATOM   1759 N  NH2 . ARG B 1 41  ? 7.46146   -16.05896 -21.62472 1.000 36.70297  ? 73   ARG B NH2 1 
ATOM   1760 N  N   . ILE B 1 42  ? 6.70353   -18.45690 -14.87944 1.000 23.89263  ? 74   ILE B N   1 
ATOM   1761 C  CA  . ILE B 1 42  ? 7.53744   -18.59846 -13.68208 1.000 23.85757  ? 74   ILE B CA  1 
ATOM   1762 C  C   . ILE B 1 42  ? 6.80322   -19.39754 -12.61848 1.000 26.61312  ? 74   ILE B C   1 
ATOM   1763 O  O   . ILE B 1 42  ? 7.37659   -20.30072 -11.99572 1.000 25.58381  ? 74   ILE B O   1 
ATOM   1764 C  CB  . ILE B 1 42  ? 7.96401   -17.22928 -13.13019 1.000 23.54230  ? 74   ILE B CB  1 
ATOM   1765 C  CG1 . ILE B 1 42  ? 8.92350   -16.53017 -14.08704 1.000 24.95833  ? 74   ILE B CG1 1 
ATOM   1766 C  CG2 . ILE B 1 42  ? 8.59897   -17.42691 -11.73811 1.000 26.06903  ? 74   ILE B CG2 1 
ATOM   1767 C  CD1 . ILE B 1 42  ? 9.27321   -15.12625 -13.61048 1.000 28.11556  ? 74   ILE B CD1 1 
ATOM   1768 N  N   . ALA B 1 43  ? 5.52291   -19.07776 -12.39103 1.000 23.76366  ? 75   ALA B N   1 
ATOM   1769 C  CA  . ALA B 1 43  ? 4.76401   -19.75948 -11.34422 1.000 24.51500  ? 75   ALA B CA  1 
ATOM   1770 C  C   . ALA B 1 43  ? 4.58758   -21.23881 -11.66778 1.000 26.99518  ? 75   ALA B C   1 
ATOM   1771 O  O   . ALA B 1 43  ? 4.67811   -22.09261 -10.77375 1.000 27.70208  ? 75   ALA B O   1 
ATOM   1772 C  CB  . ALA B 1 43  ? 3.40371   -19.08987 -11.17658 1.000 26.79383  ? 75   ALA B CB  1 
ATOM   1773 N  N   . GLY B 1 44  ? 4.34699   -21.55614 -12.94119 1.000 26.90694  ? 76   GLY B N   1 
ATOM   1774 C  CA  . GLY B 1 44  ? 4.19852   -22.94795 -13.34751 1.000 29.66252  ? 76   GLY B CA  1 
ATOM   1775 C  C   . GLY B 1 44  ? 5.47741   -23.74686 -13.16254 1.000 25.67662  ? 76   GLY B C   1 
ATOM   1776 O  O   . GLY B 1 44  ? 5.44515   -24.87626 -12.67548 1.000 26.84752  ? 76   GLY B O   1 
ATOM   1777 N  N   . GLU B 1 45  ? 6.62279   -23.17136 -13.55179 1.000 24.88551  ? 77   GLU B N   1 
ATOM   1778 C  CA  . GLU B 1 45  ? 7.89231   -23.86525 -13.31915 1.000 24.65500  ? 77   GLU B CA  1 
ATOM   1779 C  C   . GLU B 1 45  ? 8.19705   -23.98355 -11.83370 1.000 25.28954  ? 77   GLU B C   1 
ATOM   1780 O  O   . GLU B 1 45  ? 8.64180   -25.04331 -11.36972 1.000 26.87767  ? 77   GLU B O   1 
ATOM   1781 C  CB  . GLU B 1 45  ? 9.05222   -23.14077 -14.00713 1.000 24.49457  ? 77   GLU B CB  1 
ATOM   1782 C  CG  . GLU B 1 45  ? 9.12264   -23.29601 -15.52756 1.000 26.53915  ? 77   GLU B CG  1 
ATOM   1783 C  CD  . GLU B 1 45  ? 9.40947   -24.72623 -15.97356 1.000 31.09214  ? 77   GLU B CD  1 
ATOM   1784 O  OE1 . GLU B 1 45  ? 9.77228   -25.56514 -15.12974 1.000 29.42070  ? 77   GLU B OE1 1 
ATOM   1785 O  OE2 . GLU B 1 45  ? 9.35299   -24.99120 -17.20312 1.000 29.92335  ? 77   GLU B OE2 1 
ATOM   1786 N  N   . ALA B 1 46  ? 7.95716   -22.91519 -11.07295 1.000 25.96408  ? 78   ALA B N   1 
ATOM   1787 C  CA  . ALA B 1 46  ? 8.19508   -22.99160 -9.63198  1.000 25.88328  ? 78   ALA B CA  1 
ATOM   1788 C  C   . ALA B 1 46  ? 7.31239   -24.04799 -8.98097  1.000 28.62818  ? 78   ALA B C   1 
ATOM   1789 O  O   . ALA B 1 46  ? 7.75133   -24.75963 -8.06647  1.000 28.05799  ? 78   ALA B O   1 
ATOM   1790 C  CB  . ALA B 1 46  ? 7.96085   -21.61684 -8.98821  1.000 24.61246  ? 78   ALA B CB  1 
ATOM   1791 N  N   . SER B 1 47  ? 6.06345   -24.17082 -9.43887  1.000 25.79386  ? 79   SER B N   1 
ATOM   1792 C  CA  . SER B 1 47  ? 5.16670   -25.17349 -8.88721  1.000 28.00271  ? 79   SER B CA  1 
ATOM   1793 C  C   . SER B 1 47  ? 5.66983   -26.58043 -9.18275  1.000 28.54970  ? 79   SER B C   1 
ATOM   1794 O  O   . SER B 1 47  ? 5.66252   -27.45024 -8.30413  1.000 31.37649  ? 79   SER B O   1 
ATOM   1795 C  CB  . SER B 1 47  ? 3.75922   -24.96361 -9.43475  1.000 28.34667  ? 79   SER B CB  1 
ATOM   1796 O  OG  . SER B 1 47  ? 2.88529   -25.96944 -8.96518  1.000 32.30007  ? 79   SER B OG  1 
ATOM   1797 N  N   . ARG B 1 48  ? 6.15019   -26.80378 -10.40748 1.000 27.13503  ? 80   ARG B N   1 
ATOM   1798 C  CA  . ARG B 1 48  ? 6.71545   -28.10530 -10.74451 1.000 27.25752  ? 80   ARG B CA  1 
ATOM   1799 C  C   . ARG B 1 48  ? 7.92209   -28.40899 -9.86152  1.000 27.07763  ? 80   ARG B C   1 
ATOM   1800 O  O   . ARG B 1 48  ? 8.07791   -29.52928 -9.36301  1.000 29.83622  ? 80   ARG B O   1 
ATOM   1801 C  CB  . ARG B 1 48  ? 7.12518   -28.11698 -12.22676 1.000 27.61825  ? 80   ARG B CB  1 
ATOM   1802 C  CG  . ARG B 1 48  ? 7.84121   -29.40287 -12.65368 1.000 30.10452  ? 80   ARG B CG  1 
ATOM   1803 C  CD  . ARG B 1 48  ? 8.45456   -29.29416 -14.04168 1.000 29.37168  ? 80   ARG B CD  1 
ATOM   1804 N  NE  . ARG B 1 48  ? 9.50068   -28.27389 -14.12517 1.000 28.71454  ? 80   ARG B NE  1 
ATOM   1805 C  CZ  . ARG B 1 48  ? 10.79473  -28.51619 -13.95006 1.000 26.31039  ? 80   ARG B CZ  1 
ATOM   1806 N  NH1 . ARG B 1 48  ? 11.23214  -29.71467 -13.59491 1.000 28.48502  ? 80   ARG B NH1 1 
ATOM   1807 N  NH2 . ARG B 1 48  ? 11.66788  -27.52631 -14.11433 1.000 26.73885  ? 80   ARG B NH2 1 
ATOM   1808 N  N   . LEU B 1 49  ? 8.78004   -27.40751 -9.64948  1.000 27.52966  ? 81   LEU B N   1 
ATOM   1809 C  CA  . LEU B 1 49  ? 9.99907   -27.60598 -8.87075  1.000 30.88319  ? 81   LEU B CA  1 
ATOM   1810 C  C   . LEU B 1 49  ? 9.68091   -27.95946 -7.42711  1.000 29.77053  ? 81   LEU B C   1 
ATOM   1811 O  O   . LEU B 1 49  ? 10.40111  -28.73740 -6.79372  1.000 31.42907  ? 81   LEU B O   1 
ATOM   1812 C  CB  . LEU B 1 49  ? 10.87029  -26.35315 -8.94191  1.000 26.45830  ? 81   LEU B CB  1 
ATOM   1813 C  CG  . LEU B 1 49  ? 11.49068  -26.14108 -10.32134 1.000 26.82026  ? 81   LEU B CG  1 
ATOM   1814 C  CD1 . LEU B 1 49  ? 11.95228  -24.70124 -10.52820 1.000 30.28819  ? 81   LEU B CD1 1 
ATOM   1815 C  CD2 . LEU B 1 49  ? 12.63920  -27.11833 -10.49006 1.000 30.51928  ? 81   LEU B CD2 1 
ATOM   1816 N  N   . ALA B 1 50  ? 8.62532   -27.36232 -6.88132  1.000 27.76663  ? 82   ALA B N   1 
ATOM   1817 C  CA  . ALA B 1 50  ? 8.26443   -27.58776 -5.48526  1.000 33.95769  ? 82   ALA B CA  1 
ATOM   1818 C  C   . ALA B 1 50  ? 7.95044   -29.05494 -5.19791  1.000 32.89231  ? 82   ALA B C   1 
ATOM   1819 O  O   . ALA B 1 50  ? 8.04712   -29.48975 -4.04889  1.000 34.77217  ? 82   ALA B O   1 
ATOM   1820 C  CB  . ALA B 1 50  ? 7.09070   -26.68610 -5.10125  1.000 34.98836  ? 82   ALA B CB  1 
ATOM   1821 N  N   . HIS B 1 51  ? 7.52887   -29.82401 -6.20459  1.000 31.84163  ? 83   HIS B N   1 
ATOM   1822 C  CA  . HIS B 1 51  ? 7.21441   -31.23344 -5.96128  1.000 36.79512  ? 83   HIS B CA  1 
ATOM   1823 C  C   . HIS B 1 51  ? 8.44103   -32.02642 -5.52777  1.000 36.71700  ? 83   HIS B C   1 
ATOM   1824 O  O   . HIS B 1 51  ? 8.29937   -33.10730 -4.95395  1.000 40.63956  ? 83   HIS B O   1 
ATOM   1825 C  CB  . HIS B 1 51  ? 6.56700   -31.86277 -7.18958  1.000 36.04221  ? 83   HIS B CB  1 
ATOM   1826 C  CG  . HIS B 1 51  ? 5.13465   -31.47001 -7.36433  1.000 39.28144  ? 83   HIS B CG  1 
ATOM   1827 N  ND1 . HIS B 1 51  ? 4.09066   -32.18098 -6.81128  1.000 43.03000  ? 83   HIS B ND1 1 
ATOM   1828 C  CD2 . HIS B 1 51  ? 4.57547   -30.41902 -8.00530  1.000 38.67781  ? 83   HIS B CD2 1 
ATOM   1829 C  CE1 . HIS B 1 51  ? 2.94932   -31.58593 -7.11450  1.000 40.81500  ? 83   HIS B CE1 1 
ATOM   1830 N  NE2 . HIS B 1 51  ? 3.21713   -30.51823 -7.84268  1.000 38.66090  ? 83   HIS B NE2 1 
ATOM   1831 N  N   . TYR B 1 52  ? 9.64223   -31.57787 -5.90109  1.000 39.15582  ? 84   TYR B N   1 
ATOM   1832 C  CA  . TYR B 1 52  ? 10.87421  -32.25941 -5.50635  1.000 39.59290  ? 84   TYR B CA  1 
ATOM   1833 C  C   . TYR B 1 52  ? 11.22119  -32.03517 -4.04300  1.000 48.26274  ? 84   TYR B C   1 
ATOM   1834 O  O   . TYR B 1 52  ? 12.06826  -32.75580 -3.50673  1.000 47.60862  ? 84   TYR B O   1 
ATOM   1835 C  CB  . TYR B 1 52  ? 12.02787  -31.79444 -6.39732  1.000 40.40722  ? 84   TYR B CB  1 
ATOM   1836 C  CG  . TYR B 1 52  ? 11.93451  -32.31636 -7.80726  1.000 40.87203  ? 84   TYR B CG  1 
ATOM   1837 C  CD1 . TYR B 1 52  ? 12.17709  -33.65262 -8.08871  1.000 46.50431  ? 84   TYR B CD1 1 
ATOM   1838 C  CD2 . TYR B 1 52  ? 11.49654  -31.49992 -8.83669  1.000 37.02823  ? 84   TYR B CD2 1 
ATOM   1839 C  CE1 . TYR B 1 52  ? 12.07171  -34.14211 -9.37620  1.000 43.43625  ? 84   TYR B CE1 1 
ATOM   1840 C  CE2 . TYR B 1 52  ? 11.37568  -31.98657 -10.13915 1.000 39.28935  ? 84   TYR B CE2 1 
ATOM   1841 C  CZ  . TYR B 1 52  ? 11.66526  -33.30749 -10.39427 1.000 42.37765  ? 84   TYR B CZ  1 
ATOM   1842 O  OH  . TYR B 1 52  ? 11.54419  -33.80304 -11.67268 1.000 43.52423  ? 84   TYR B OH  1 
ATOM   1843 N  N   . ASN B 1 53  ? 10.60136  -31.05963 -3.39195  1.000 46.11692  ? 85   ASN B N   1 
ATOM   1844 C  CA  . ASN B 1 53  ? 10.87412  -30.78390 -1.99147  1.000 48.08821  ? 85   ASN B CA  1 
ATOM   1845 C  C   . ASN B 1 53  ? 9.89072   -31.53672 -1.10357  1.000 49.57157  ? 85   ASN B C   1 
ATOM   1846 O  O   . ASN B 1 53  ? 8.83693   -31.99658 -1.55091  1.000 47.93808  ? 85   ASN B O   1 
ATOM   1847 C  CB  . ASN B 1 53  ? 10.77502  -29.28901 -1.74736  1.000 42.44589  ? 85   ASN B CB  1 
ATOM   1848 C  CG  . ASN B 1 53  ? 11.71232  -28.51745 -2.64332  1.000 49.27559  ? 85   ASN B CG  1 
ATOM   1849 O  OD1 . ASN B 1 53  ? 12.72274  -29.05430 -3.13094  1.000 48.38941  ? 85   ASN B OD1 1 
ATOM   1850 N  ND2 . ASN B 1 53  ? 11.36075  -27.26925 -2.91794  1.000 45.13522  ? 85   ASN B ND2 1 
ATOM   1851 N  N   . LYS B 1 54  ? 10.24663  -31.65524 0.17893   1.000 59.44909  ? 86   LYS B N   1 
ATOM   1852 C  CA  . LYS B 1 54  ? 9.36487   -32.35218 1.11259   1.000 69.10390  ? 86   LYS B CA  1 
ATOM   1853 C  C   . LYS B 1 54  ? 8.12409   -31.53951 1.45653   1.000 65.81554  ? 86   LYS B C   1 
ATOM   1854 O  O   . LYS B 1 54  ? 7.07545   -32.11613 1.76427   1.000 63.49178  ? 86   LYS B O   1 
ATOM   1855 C  CB  . LYS B 1 54  ? 10.12317  -32.72041 2.38974   1.000 72.51870  ? 86   LYS B CB  1 
ATOM   1856 C  CG  . LYS B 1 54  ? 11.30100  -33.65216 2.16378   1.000 83.17797  ? 86   LYS B CG  1 
ATOM   1857 C  CD  . LYS B 1 54  ? 10.83919  -34.93946 1.48314   1.000 102.95481 ? 86   LYS B CD  1 
ATOM   1858 C  CE  . LYS B 1 54  ? 11.99651  -35.84303 1.05637   1.000 108.11634 ? 86   LYS B CE  1 
ATOM   1859 N  NZ  . LYS B 1 54  ? 12.12442  -37.02822 1.95992   1.000 97.44916  ? 86   LYS B NZ  1 
ATOM   1860 N  N   . ARG B 1 55  ? 8.20560   -30.21769 1.39348   1.000 60.34252  ? 87   ARG B N   1 
ATOM   1861 C  CA  . ARG B 1 55  ? 7.08784   -29.35440 1.74517   1.000 61.83776  ? 87   ARG B CA  1 
ATOM   1862 C  C   . ARG B 1 55  ? 6.47453   -28.75915 0.49134   1.000 54.15300  ? 87   ARG B C   1 
ATOM   1863 O  O   . ARG B 1 55  ? 7.19697   -28.27964 -0.39114  1.000 56.95354  ? 87   ARG B O   1 
ATOM   1864 C  CB  . ARG B 1 55  ? 7.51524   -28.24338 2.70292   1.000 67.68467  ? 87   ARG B CB  1 
ATOM   1865 C  CG  . ARG B 1 55  ? 7.94066   -28.75374 4.06382   1.000 85.14075  ? 87   ARG B CG  1 
ATOM   1866 C  CD  . ARG B 1 55  ? 8.55481   -27.65376 4.90611   1.000 107.94088 ? 87   ARG B CD  1 
ATOM   1867 N  NE  . ARG B 1 55  ? 9.11287   -28.17757 6.14688   1.000 117.06841 ? 87   ARG B NE  1 
ATOM   1868 C  CZ  . ARG B 1 55  ? 10.04678  -27.56942 6.86454   1.000 115.79765 ? 87   ARG B CZ  1 
ATOM   1869 N  NH1 . ARG B 1 55  ? 10.57283  -26.41730 6.48046   1.000 115.34247 ? 87   ARG B NH1 1 
ATOM   1870 N  NH2 . ARG B 1 55  ? 10.46701  -28.13379 7.99329   1.000 117.82895 ? 87   ARG B NH2 1 
ATOM   1871 N  N   . SER B 1 56  ? 5.14523   -28.83335 0.39908   1.000 47.08208  ? 88   SER B N   1 
ATOM   1872 C  CA  . SER B 1 56  ? 4.41771   -28.25788 -0.73151  1.000 43.04095  ? 88   SER B CA  1 
ATOM   1873 C  C   . SER B 1 56  ? 4.36180   -26.74622 -0.52812  1.000 40.24917  ? 88   SER B C   1 
ATOM   1874 O  O   . SER B 1 56  ? 3.35242   -26.16879 -0.11899  1.000 41.49854  ? 88   SER B O   1 
ATOM   1875 C  CB  . SER B 1 56  ? 3.02652   -28.86411 -0.84740  1.000 43.91367  ? 88   SER B CB  1 
ATOM   1876 O  OG  . SER B 1 56  ? 2.26715   -28.21219 -1.85345  1.000 45.22514  ? 88   SER B OG  1 
ATOM   1877 N  N   . THR B 1 57  ? 5.49967   -26.10436 -0.77476  1.000 38.62768  ? 89   THR B N   1 
ATOM   1878 C  CA  . THR B 1 57  ? 5.65479   -24.67358 -0.55900  1.000 35.43181  ? 89   THR B CA  1 
ATOM   1879 C  C   . THR B 1 57  ? 6.37659   -24.03741 -1.73663  1.000 32.29619  ? 89   THR B C   1 
ATOM   1880 O  O   . THR B 1 57  ? 7.40659   -24.55709 -2.16828  1.000 34.37231  ? 89   THR B O   1 
ATOM   1881 C  CB  . THR B 1 57  ? 6.45036   -24.40220 0.71328   1.000 34.40693  ? 89   THR B CB  1 
ATOM   1882 O  OG1 . THR B 1 57  ? 5.87210   -25.13407 1.79670   1.000 44.50079  ? 89   THR B OG1 1 
ATOM   1883 C  CG2 . THR B 1 57  ? 6.44140   -22.90040 1.01986   1.000 37.15516  ? 89   THR B CG2 1 
ATOM   1884 N  N   . ILE B 1 58  ? 5.86485   -22.92194 -2.24729  1.000 27.30059  ? 90   ILE B N   1 
ATOM   1885 C  CA  . ILE B 1 58  ? 6.62702   -22.11659 -3.20158  1.000 26.24452  ? 90   ILE B CA  1 
ATOM   1886 C  C   . ILE B 1 58  ? 7.50045   -21.18637 -2.36254  1.000 31.62441  ? 90   ILE B C   1 
ATOM   1887 O  O   . ILE B 1 58  ? 6.97317   -20.28560 -1.70750  1.000 34.95331  ? 90   ILE B O   1 
ATOM   1888 C  CB  . ILE B 1 58  ? 5.71931   -21.27802 -4.11404  1.000 31.84667  ? 90   ILE B CB  1 
ATOM   1889 C  CG1 . ILE B 1 58  ? 4.68123   -22.11041 -4.87317  1.000 43.76704  ? 90   ILE B CG1 1 
ATOM   1890 C  CG2 . ILE B 1 58  ? 6.58697   -20.46743 -5.11870  1.000 30.89225  ? 90   ILE B CG2 1 
ATOM   1891 C  CD1 . ILE B 1 58  ? 5.23403   -23.15812 -5.72021  1.000 34.94674  ? 90   ILE B CD1 1 
ATOM   1892 N  N   . THR B 1 59  ? 8.82518   -21.33449 -2.43024  1.000 29.76242  ? 91   THR B N   1 
ATOM   1893 C  CA  . THR B 1 59  ? 9.72565   -20.40061 -1.75183  1.000 25.90781  ? 91   THR B CA  1 
ATOM   1894 C  C   . THR B 1 59  ? 10.51130  -19.60672 -2.78498  1.000 28.37569  ? 91   THR B C   1 
ATOM   1895 O  O   . THR B 1 59  ? 10.43416  -19.85699 -3.99648  1.000 29.64213  ? 91   THR B O   1 
ATOM   1896 C  CB  . THR B 1 59  ? 10.71281  -21.11298 -0.82777  1.000 32.29158  ? 91   THR B CB  1 
ATOM   1897 O  OG1 . THR B 1 59  ? 11.72920  -21.74523 -1.61480  1.000 35.47046  ? 91   THR B OG1 1 
ATOM   1898 C  CG2 . THR B 1 59  ? 10.00859  -22.15955 0.02140   1.000 35.01168  ? 91   THR B CG2 1 
ATOM   1899 N  N   . SER B 1 60  ? 11.30217  -18.64558 -2.30287  1.000 28.67330  ? 92   SER B N   1 
ATOM   1900 C  CA  A SER B 1 60  ? 12.11824  -17.89430 -3.25042  0.619 28.16844  ? 92   SER B CA  1 
ATOM   1901 C  CA  B SER B 1 60  ? 12.16890  -17.88479 -3.20013  0.381 27.92922  ? 92   SER B CA  1 
ATOM   1902 C  C   . SER B 1 60  ? 13.11398  -18.79264 -3.96520  1.000 27.85695  ? 92   SER B C   1 
ATOM   1903 O  O   . SER B 1 60  ? 13.56995  -18.43574 -5.05766  1.000 28.48962  ? 92   SER B O   1 
ATOM   1904 C  CB  A SER B 1 60  ? 12.86682  -16.74359 -2.56182  0.619 31.59690  ? 92   SER B CB  1 
ATOM   1905 C  CB  B SER B 1 60  ? 12.99185  -16.86124 -2.41628  0.381 31.45757  ? 92   SER B CB  1 
ATOM   1906 O  OG  A SER B 1 60  ? 13.70967  -17.21003 -1.53190  0.619 33.77853  ? 92   SER B OG  1 
ATOM   1907 O  OG  B SER B 1 60  ? 12.15785  -15.90559 -1.80255  0.381 31.59549  ? 92   SER B OG  1 
ATOM   1908 N  N   . ARG B 1 61  ? 13.45510  -19.94987 -3.38971  1.000 28.79051  ? 93   ARG B N   1 
ATOM   1909 C  CA  . ARG B 1 61  ? 14.39599  -20.82428 -4.07303  1.000 30.20414  ? 93   ARG B CA  1 
ATOM   1910 C  C   . ARG B 1 61  ? 13.77649  -21.37691 -5.35487  1.000 27.24967  ? 93   ARG B C   1 
ATOM   1911 O  O   . ARG B 1 61  ? 14.43689  -21.41743 -6.39956  1.000 28.37545  ? 93   ARG B O   1 
ATOM   1912 C  CB  . ARG B 1 61  ? 14.89215  -21.92229 -3.12554  1.000 35.30992  ? 93   ARG B CB  1 
ATOM   1913 C  CG  . ARG B 1 61  ? 15.92196  -22.80088 -3.78613  1.000 45.78533  ? 93   ARG B CG  1 
ATOM   1914 C  CD  . ARG B 1 61  ? 16.59440  -23.81444 -2.86855  1.000 69.90133  ? 93   ARG B CD  1 
ATOM   1915 N  NE  . ARG B 1 61  ? 15.93043  -25.10608 -2.76878  1.000 81.80529  ? 93   ARG B NE  1 
ATOM   1916 C  CZ  . ARG B 1 61  ? 16.30221  -26.07242 -1.94549  1.000 82.66181  ? 93   ARG B CZ  1 
ATOM   1917 N  NH1 . ARG B 1 61  ? 17.36271  -25.94606 -1.17118  1.000 82.38928  ? 93   ARG B NH1 1 
ATOM   1918 N  NH2 . ARG B 1 61  ? 15.60887  -27.20251 -1.92411  1.000 82.41938  ? 93   ARG B NH2 1 
ATOM   1919 N  N   . GLU B 1 62  ? 12.49786  -21.76539 -5.30972  1.000 26.47999  ? 94   GLU B N   1 
ATOM   1920 C  CA  . GLU B 1 62  ? 11.85308  -22.25077 -6.53091  1.000 25.16248  ? 94   GLU B CA  1 
ATOM   1921 C  C   . GLU B 1 62  ? 11.60119  -21.12085 -7.52519  1.000 26.43561  ? 94   GLU B C   1 
ATOM   1922 O  O   . GLU B 1 62  ? 11.67546  -21.33509 -8.74128  1.000 26.72025  ? 94   GLU B O   1 
ATOM   1923 C  CB  . GLU B 1 62  ? 10.54496  -22.95722 -6.20127  1.000 27.44915  ? 94   GLU B CB  1 
ATOM   1924 C  CG  . GLU B 1 62  ? 10.73786  -24.30844 -5.48323  1.000 29.77440  ? 94   GLU B CG  1 
ATOM   1925 C  CD  . GLU B 1 62  ? 11.21151  -24.15283 -4.05432  1.000 37.98935  ? 94   GLU B CD  1 
ATOM   1926 O  OE1 . GLU B 1 62  ? 10.63199  -23.33319 -3.31290  1.000 34.15373  ? 94   GLU B OE1 1 
ATOM   1927 O  OE2 . GLU B 1 62  ? 12.21829  -24.78833 -3.69439  1.000 39.60367  ? 94   GLU B OE2 1 
ATOM   1928 N  N   . ILE B 1 63  ? 11.29137  -19.91489 -7.04065  1.000 25.29009  ? 95   ILE B N   1 
ATOM   1929 C  CA  . ILE B 1 63  ? 11.15934  -18.78563 -7.96449  1.000 25.84257  ? 95   ILE B CA  1 
ATOM   1930 C  C   . ILE B 1 63  ? 12.47795  -18.53427 -8.68612  1.000 23.60200  ? 95   ILE B C   1 
ATOM   1931 O  O   . ILE B 1 63  ? 12.50831  -18.34599 -9.91083  1.000 24.77804  ? 95   ILE B O   1 
ATOM   1932 C  CB  . ILE B 1 63  ? 10.69664  -17.51549 -7.21971  1.000 24.87694  ? 95   ILE B CB  1 
ATOM   1933 C  CG1 . ILE B 1 63  ? 9.33838   -17.70156 -6.54938  1.000 26.81297  ? 95   ILE B CG1 1 
ATOM   1934 C  CG2 . ILE B 1 63  ? 10.61806  -16.32039 -8.20833  1.000 26.69536  ? 95   ILE B CG2 1 
ATOM   1935 C  CD1 . ILE B 1 63  ? 8.20392   -18.05703 -7.51330  1.000 25.38174  ? 95   ILE B CD1 1 
ATOM   1936 N  N   . GLN B 1 64  ? 13.58410  -18.50760 -7.93473  1.000 24.95003  ? 96   GLN B N   1 
ATOM   1937 C  CA  . GLN B 1 64  ? 14.89436  -18.24804 -8.52708  1.000 27.52064  ? 96   GLN B CA  1 
ATOM   1938 C  C   . GLN B 1 64  ? 15.25813  -19.30186 -9.55396  1.000 28.82973  ? 96   GLN B C   1 
ATOM   1939 O  O   . GLN B 1 64  ? 15.72944  -18.96731 -10.65360 1.000 24.77293  ? 96   GLN B O   1 
ATOM   1940 C  CB  . GLN B 1 64  ? 15.96861  -18.19429 -7.43328  1.000 27.49039  ? 96   GLN B CB  1 
ATOM   1941 C  CG  . GLN B 1 64  ? 17.40171  -18.15102 -7.98084  1.000 28.08217  ? 96   GLN B CG  1 
ATOM   1942 C  CD  . GLN B 1 64  ? 18.39343  -17.66048 -6.94567  1.000 30.30391  ? 96   GLN B CD  1 
ATOM   1943 O  OE1 . GLN B 1 64  ? 18.28261  -16.54146 -6.46533  1.000 31.62163  ? 96   GLN B OE1 1 
ATOM   1944 N  NE2 . GLN B 1 64  ? 19.38460  -18.49193 -6.61519  1.000 37.60285  ? 96   GLN B NE2 1 
ATOM   1945 N  N   . THR B 1 65  ? 15.03959  -20.58360 -9.22672  1.000 25.42031  ? 97   THR B N   1 
ATOM   1946 C  CA  . THR B 1 65  ? 15.35259  -21.63098 -10.19621 1.000 25.17607  ? 97   THR B CA  1 
ATOM   1947 C  C   . THR B 1 65  ? 14.49160  -21.49565 -11.44308 1.000 25.34992  ? 97   THR B C   1 
ATOM   1948 O  O   . THR B 1 65  ? 14.99596  -21.62182 -12.56957 1.000 25.10593  ? 97   THR B O   1 
ATOM   1949 C  CB  . THR B 1 65  ? 15.18591  -23.00721 -9.54787  1.000 27.22214  ? 97   THR B CB  1 
ATOM   1950 O  OG1 . THR B 1 65  ? 16.08104  -23.07445 -8.43710  1.000 30.02129  ? 97   THR B OG1 1 
ATOM   1951 C  CG2 . THR B 1 65  ? 15.56996  -24.12197 -10.54026 1.000 30.31257  ? 97   THR B CG2 1 
ATOM   1952 N  N   . ALA B 1 66  ? 13.20710  -21.18273 -11.26429 1.000 25.19434  ? 98   ALA B N   1 
ATOM   1953 C  CA  . ALA B 1 66  ? 12.31994  -20.97500 -12.40475 1.000 23.38513  ? 98   ALA B CA  1 
ATOM   1954 C  C   . ALA B 1 66  ? 12.79480  -19.81438 -13.27022 1.000 23.32172  ? 98   ALA B C   1 
ATOM   1955 O  O   . ALA B 1 66  ? 12.74711  -19.88014 -14.49989 1.000 26.20935  ? 98   ALA B O   1 
ATOM   1956 C  CB  . ALA B 1 66  ? 10.89867  -20.72516 -11.91975 1.000 24.59215  ? 98   ALA B CB  1 
ATOM   1957 N  N   . VAL B 1 67  ? 13.22920  -18.72688 -12.64067 1.000 23.99746  ? 99   VAL B N   1 
ATOM   1958 C  CA  . VAL B 1 67  ? 13.73224  -17.57586 -13.38415 1.000 25.20385  ? 99   VAL B CA  1 
ATOM   1959 C  C   . VAL B 1 67  ? 14.97339  -17.94358 -14.19427 1.000 23.56160  ? 99   VAL B C   1 
ATOM   1960 O  O   . VAL B 1 67  ? 15.13903  -17.49427 -15.33203 1.000 26.15705  ? 99   VAL B O   1 
ATOM   1961 C  CB  . VAL B 1 67  ? 14.00819  -16.42754 -12.39512 1.000 23.54141  ? 99   VAL B CB  1 
ATOM   1962 C  CG1 . VAL B 1 67  ? 14.90337  -15.36705 -13.00501 1.000 28.75226  ? 99   VAL B CG1 1 
ATOM   1963 C  CG2 . VAL B 1 67  ? 12.68112  -15.83957 -11.92014 1.000 25.67989  ? 99   VAL B CG2 1 
ATOM   1964 N  N   . ARG B 1 68  ? 15.88679  -18.72992 -13.60832 1.000 22.47970  ? 100  ARG B N   1 
ATOM   1965 C  CA  . ARG B 1 68  ? 17.08873  -19.13577 -14.32902 1.000 24.65440  ? 100  ARG B CA  1 
ATOM   1966 C  C   . ARG B 1 68  ? 16.76161  -20.03752 -15.51294 1.000 24.32319  ? 100  ARG B C   1 
ATOM   1967 O  O   . ARG B 1 68  ? 17.46574  -19.99694 -16.52453 1.000 26.76671  ? 100  ARG B O   1 
ATOM   1968 C  CB  . ARG B 1 68  ? 18.06761  -19.82502 -13.37140 1.000 26.21121  ? 100  ARG B CB  1 
ATOM   1969 C  CG  . ARG B 1 68  ? 18.64951  -18.81375 -12.35762 1.000 28.32903  ? 100  ARG B CG  1 
ATOM   1970 C  CD  . ARG B 1 68  ? 19.57921  -19.44940 -11.30952 1.000 34.79584  ? 100  ARG B CD  1 
ATOM   1971 N  NE  . ARG B 1 68  ? 20.90323  -19.74955 -11.84604 1.000 45.16759  ? 100  ARG B NE  1 
ATOM   1972 C  CZ  . ARG B 1 68  ? 21.85559  -20.39615 -11.18377 1.000 48.71225  ? 100  ARG B CZ  1 
ATOM   1973 N  NH1 . ARG B 1 68  ? 21.66991  -20.82306 -9.94358  1.000 47.17401  ? 100  ARG B NH1 1 
ATOM   1974 N  NH2 . ARG B 1 68  ? 23.02689  -20.61430 -11.77712 1.000 49.42953  ? 100  ARG B NH2 1 
ATOM   1975 N  N   . LEU B 1 69  ? 15.69682  -20.84203 -15.41179 1.000 25.25119  ? 101  LEU B N   1 
ATOM   1976 C  CA  . LEU B 1 69  ? 15.30601  -21.66859 -16.55937 1.000 25.08881  ? 101  LEU B CA  1 
ATOM   1977 C  C   . LEU B 1 69  ? 14.70602  -20.82989 -17.66509 1.000 25.75992  ? 101  LEU B C   1 
ATOM   1978 O  O   . LEU B 1 69  ? 15.03703  -21.02228 -18.84493 1.000 27.41643  ? 101  LEU B O   1 
ATOM   1979 C  CB  . LEU B 1 69  ? 14.27732  -22.71971 -16.14107 1.000 25.46529  ? 101  LEU B CB  1 
ATOM   1980 C  CG  . LEU B 1 69  ? 14.73528  -23.85009 -15.23443 1.000 24.00769  ? 101  LEU B CG  1 
ATOM   1981 C  CD1 . LEU B 1 69  ? 13.52533  -24.59088 -14.71445 1.000 28.24294  ? 101  LEU B CD1 1 
ATOM   1982 C  CD2 . LEU B 1 69  ? 15.64288  -24.80377 -16.01093 1.000 24.26291  ? 101  LEU B CD2 1 
ATOM   1983 N  N   . LEU B 1 70  ? 13.82071  -19.90309 -17.29385 1.000 23.75620  ? 102  LEU B N   1 
ATOM   1984 C  CA  A LEU B 1 70  ? 12.92040  -19.22932 -18.22942 0.663 24.99929  ? 102  LEU B CA  1 
ATOM   1985 C  CA  B LEU B 1 70  ? 12.92565  -19.23191 -18.23214 0.337 25.80747  ? 102  LEU B CA  1 
ATOM   1986 C  C   . LEU B 1 70  ? 13.54013  -18.00689 -18.89219 1.000 24.06790  ? 102  LEU B C   1 
ATOM   1987 O  O   . LEU B 1 70  ? 13.30816  -17.76949 -20.08540 1.000 26.66636  ? 102  LEU B O   1 
ATOM   1988 C  CB  A LEU B 1 70  ? 11.63358  -18.80355 -17.51018 0.663 31.61188  ? 102  LEU B CB  1 
ATOM   1989 C  CB  B LEU B 1 70  ? 11.64188  -18.81090 -17.51583 0.337 26.85152  ? 102  LEU B CB  1 
ATOM   1990 C  CG  A LEU B 1 70  ? 10.67845  -17.94838 -18.35234 0.663 26.01236  ? 102  LEU B CG  1 
ATOM   1991 C  CG  B LEU B 1 70  ? 10.56010  -19.86091 -17.29211 0.337 26.20379  ? 102  LEU B CG  1 
ATOM   1992 C  CD1 A LEU B 1 70  ? 10.07346  -18.80529 -19.43740 0.663 29.66687  ? 102  LEU B CD1 1 
ATOM   1993 C  CD1 B LEU B 1 70  ? 9.88830   -19.56542 -15.99728 0.337 26.84886  ? 102  LEU B CD1 1 
ATOM   1994 C  CD2 A LEU B 1 70  ? 9.59808   -17.28885 -17.52660 0.663 32.13595  ? 102  LEU B CD2 1 
ATOM   1995 C  CD2 B LEU B 1 70  ? 9.55258   -19.80365 -18.42000 0.337 29.05662  ? 102  LEU B CD2 1 
ATOM   1996 N  N   . LEU B 1 71  ? 14.28931  -17.20113 -18.14016 1.000 24.99324  ? 103  LEU B N   1 
ATOM   1997 C  CA  . LEU B 1 71  ? 14.77651  -15.94493 -18.71378 1.000 26.53029  ? 103  LEU B CA  1 
ATOM   1998 C  C   . LEU B 1 71  ? 16.05024  -16.17975 -19.51407 1.000 25.96305  ? 103  LEU B C   1 
ATOM   1999 O  O   . LEU B 1 71  ? 17.01304  -16.75198 -18.99020 1.000 30.78130  ? 103  LEU B O   1 
ATOM   2000 C  CB  . LEU B 1 71  ? 15.00833  -14.91140 -17.59615 1.000 25.47970  ? 103  LEU B CB  1 
ATOM   2001 C  CG  . LEU B 1 71  ? 13.77473  -14.05384 -17.31355 1.000 27.00759  ? 103  LEU B CG  1 
ATOM   2002 C  CD1 . LEU B 1 71  ? 12.59960  -14.86395 -16.85153 1.000 26.06721  ? 103  LEU B CD1 1 
ATOM   2003 C  CD2 . LEU B 1 71  ? 14.08020  -12.95922 -16.28160 1.000 29.88902  ? 103  LEU B CD2 1 
ATOM   2004 N  N   . PRO B 1 72  ? 16.13740  -15.68420 -20.74774 1.000 29.39394  ? 104  PRO B N   1 
ATOM   2005 C  CA  . PRO B 1 72  ? 17.31911  -15.99204 -21.55773 1.000 31.61874  ? 104  PRO B CA  1 
ATOM   2006 C  C   . PRO B 1 72  ? 18.49598  -15.09962 -21.21761 1.000 33.06024  ? 104  PRO B C   1 
ATOM   2007 O  O   . PRO B 1 72  ? 18.34171  -13.90493 -20.96245 1.000 32.18683  ? 104  PRO B O   1 
ATOM   2008 C  CB  . PRO B 1 72  ? 16.85033  -15.71335 -22.99485 1.000 30.70159  ? 104  PRO B CB  1 
ATOM   2009 C  CG  . PRO B 1 72  ? 15.39770  -15.68543 -22.94858 1.000 32.79408  ? 104  PRO B CG  1 
ATOM   2010 C  CD  . PRO B 1 72  ? 14.99628  -15.25084 -21.56591 1.000 28.64555  ? 104  PRO B CD  1 
ATOM   2011 N  N   . GLY B 1 73  ? 19.68709  -15.68850 -21.27584 1.000 34.41328  ? 105  GLY B N   1 
ATOM   2012 C  CA  . GLY B 1 73  ? 20.91810  -14.91570 -21.25294 1.000 37.28525  ? 105  GLY B CA  1 
ATOM   2013 C  C   . GLY B 1 73  ? 21.03342  -14.03680 -20.02543 1.000 38.92783  ? 105  GLY B C   1 
ATOM   2014 O  O   . GLY B 1 73  ? 20.71187  -14.43809 -18.90204 1.000 35.62800  ? 105  GLY B O   1 
ATOM   2015 N  N   . GLU B 1 74  ? 21.51027  -12.81551 -20.23885 1.000 35.95810  ? 106  GLU B N   1 
ATOM   2016 C  CA  . GLU B 1 74  ? 21.76125  -11.90413 -19.12869 1.000 33.18505  ? 106  GLU B CA  1 
ATOM   2017 C  C   . GLU B 1 74  ? 20.49795  -11.39269 -18.46107 1.000 30.69245  ? 106  GLU B C   1 
ATOM   2018 O  O   . GLU B 1 74  ? 20.60039  -10.80281 -17.37835 1.000 34.46994  ? 106  GLU B O   1 
ATOM   2019 C  CB  . GLU B 1 74  ? 22.61962  -10.72808 -19.60322 1.000 33.83735  ? 106  GLU B CB  1 
ATOM   2020 C  CG  . GLU B 1 74  ? 24.03376  -11.12860 -19.95596 1.000 37.95465  ? 106  GLU B CG  1 
ATOM   2021 C  CD  . GLU B 1 74  ? 24.90935  -9.93356  -20.25100 1.000 43.44570  ? 106  GLU B CD  1 
ATOM   2022 O  OE1 . GLU B 1 74  ? 24.93482  -9.49477  -21.41417 1.000 44.25874  ? 106  GLU B OE1 1 
ATOM   2023 O  OE2 . GLU B 1 74  ? 25.56132  -9.41914  -19.31874 1.000 53.93685  ? 106  GLU B OE2 1 
ATOM   2024 N  N   . LEU B 1 75  ? 19.32256  -11.57468 -19.07089 1.000 28.68824  ? 107  LEU B N   1 
ATOM   2025 C  CA  . LEU B 1 75  ? 18.08936  -11.25164 -18.36612 1.000 26.81547  ? 107  LEU B CA  1 
ATOM   2026 C  C   . LEU B 1 75  ? 18.00559  -12.03351 -17.06847 1.000 29.09129  ? 107  LEU B C   1 
ATOM   2027 O  O   . LEU B 1 75  ? 17.60201  -11.48922 -16.03938 1.000 29.57566  ? 107  LEU B O   1 
ATOM   2028 C  CB  . LEU B 1 75  ? 16.85491  -11.55099 -19.21638 1.000 29.97178  ? 107  LEU B CB  1 
ATOM   2029 C  CG  . LEU B 1 75  ? 16.58148  -10.60367 -20.38990 1.000 29.84312  ? 107  LEU B CG  1 
ATOM   2030 C  CD1 . LEU B 1 75  ? 15.41288  -11.15470 -21.20523 1.000 26.70646  ? 107  LEU B CD1 1 
ATOM   2031 C  CD2 . LEU B 1 75  ? 16.26265  -9.19720  -19.85726 1.000 27.92110  ? 107  LEU B CD2 1 
ATOM   2032 N  N   . ALA B 1 76  ? 18.40254  -13.31351 -17.09865 1.000 28.00978  ? 108  ALA B N   1 
ATOM   2033 C  CA  . ALA B 1 76  ? 18.31350  -14.13416 -15.89204 1.000 28.93463  ? 108  ALA B CA  1 
ATOM   2034 C  C   . ALA B 1 76  ? 19.25869  -13.62830 -14.81262 1.000 28.34941  ? 108  ALA B C   1 
ATOM   2035 O  O   . ALA B 1 76  ? 18.86855  -13.53897 -13.64158 1.000 31.44802  ? 108  ALA B O   1 
ATOM   2036 C  CB  . ALA B 1 76  ? 18.62012  -15.59913 -16.21195 1.000 29.24273  ? 108  ALA B CB  1 
ATOM   2037 N  N   . LYS B 1 77  ? 20.49001  -13.26824 -15.19217 1.000 29.32758  ? 109  LYS B N   1 
ATOM   2038 C  CA  . LYS B 1 77  ? 21.46717  -12.76717 -14.22611 1.000 31.65328  ? 109  LYS B CA  1 
ATOM   2039 C  C   . LYS B 1 77  ? 20.93613  -11.54508 -13.48869 1.000 33.56658  ? 109  LYS B C   1 
ATOM   2040 O  O   . LYS B 1 77  ? 21.00830  -11.46578 -12.25550 1.000 32.00919  ? 109  LYS B O   1 
ATOM   2041 C  CB  . LYS B 1 77  ? 22.78396  -12.42748 -14.94132 1.000 34.18441  ? 109  LYS B CB  1 
ATOM   2042 C  CG  . LYS B 1 77  ? 23.82766  -11.71955 -14.05839 1.000 37.30963  ? 109  LYS B CG  1 
ATOM   2043 C  CD  . LYS B 1 77  ? 25.12034  -11.44482 -14.82737 1.000 47.02504  ? 109  LYS B CD  1 
ATOM   2044 C  CE  . LYS B 1 77  ? 24.89264  -10.46521 -15.96467 1.000 48.29820  ? 109  LYS B CE  1 
ATOM   2045 N  NZ  . LYS B 1 77  ? 26.17712  -10.05660 -16.60675 1.000 53.61161  ? 109  LYS B NZ  1 
ATOM   2046 N  N   . HIS B 1 78  ? 20.41511  -10.56815 -14.23232 1.000 30.01605  ? 110  HIS B N   1 
ATOM   2047 C  CA  . HIS B 1 78  ? 19.93979  -9.34388  -13.60063 1.000 30.83291  ? 110  HIS B CA  1 
ATOM   2048 C  C   . HIS B 1 78  ? 18.66743  -9.58956  -12.80908 1.000 30.22631  ? 110  HIS B C   1 
ATOM   2049 O  O   . HIS B 1 78  ? 18.48142  -9.02169  -11.72640 1.000 30.97697  ? 110  HIS B O   1 
ATOM   2050 C  CB  . HIS B 1 78  ? 19.74057  -8.27081  -14.66773 1.000 33.17353  ? 110  HIS B CB  1 
ATOM   2051 C  CG  . HIS B 1 78  ? 21.02786  -7.80426  -15.26175 1.000 35.52383  ? 110  HIS B CG  1 
ATOM   2052 N  ND1 . HIS B 1 78  ? 22.19117  -7.70431  -14.52713 1.000 40.67576  ? 110  HIS B ND1 1 
ATOM   2053 C  CD2 . HIS B 1 78  ? 21.35872  -7.48606  -16.53523 1.000 37.36348  ? 110  HIS B CD2 1 
ATOM   2054 C  CE1 . HIS B 1 78  ? 23.17418  -7.30671  -15.31612 1.000 45.72872  ? 110  HIS B CE1 1 
ATOM   2055 N  NE2 . HIS B 1 78  ? 22.69305  -7.16465  -16.53844 1.000 39.82141  ? 110  HIS B NE2 1 
ATOM   2056 N  N   . ALA B 1 79  ? 17.76199  -10.41586 -13.33154 1.000 26.84641  ? 111  ALA B N   1 
ATOM   2057 C  CA  . ALA B 1 79  ? 16.54606  -10.71113 -12.57298 1.000 27.00563  ? 111  ALA B CA  1 
ATOM   2058 C  C   . ALA B 1 79  ? 16.87663  -11.38627 -11.25112 1.000 27.41943  ? 111  ALA B C   1 
ATOM   2059 O  O   . ALA B 1 79  ? 16.25504  -11.09224 -10.22106 1.000 27.66868  ? 111  ALA B O   1 
ATOM   2060 C  CB  . ALA B 1 79  ? 15.59912  -11.58946 -13.39920 1.000 26.35740  ? 111  ALA B CB  1 
ATOM   2061 N  N   . VAL B 1 80  ? 17.82505  -12.32455 -11.26758 1.000 26.47876  ? 112  VAL B N   1 
ATOM   2062 C  CA  . VAL B 1 80  ? 18.23080  -12.99097 -10.02735 1.000 25.84247  ? 112  VAL B CA  1 
ATOM   2063 C  C   . VAL B 1 80  ? 18.82585  -11.98196 -9.06217  1.000 27.20737  ? 112  VAL B C   1 
ATOM   2064 O  O   . VAL B 1 80  ? 18.54709  -12.01298 -7.85206  1.000 33.44887  ? 112  VAL B O   1 
ATOM   2065 C  CB  . VAL B 1 80  ? 19.20981  -14.13971 -10.33961 1.000 27.67626  ? 112  VAL B CB  1 
ATOM   2066 C  CG1 . VAL B 1 80  ? 19.93211  -14.59386 -9.07427  1.000 30.01510  ? 112  VAL B CG1 1 
ATOM   2067 C  CG2 . VAL B 1 80  ? 18.43861  -15.30384 -10.97607 1.000 32.17328  ? 112  VAL B CG2 1 
ATOM   2068 N  N   . SER B 1 81  ? 19.63953  -11.06246 -9.57452  1.000 27.92349  ? 113  SER B N   1 
ATOM   2069 C  CA  . SER B 1 81  ? 20.21558  -10.04187 -8.70570  1.000 31.14257  ? 113  SER B CA  1 
ATOM   2070 C  C   . SER B 1 81  ? 19.11959  -9.18345  -8.08318  1.000 31.58975  ? 113  SER B C   1 
ATOM   2071 O  O   . SER B 1 81  ? 19.17765  -8.85371  -6.88866  1.000 34.87503  ? 113  SER B O   1 
ATOM   2072 C  CB  . SER B 1 81  ? 21.19702  -9.17366  -9.50260  1.000 32.14558  ? 113  SER B CB  1 
ATOM   2073 O  OG  . SER B 1 81  ? 21.71232  -8.13295  -8.69048  1.000 51.33840  ? 113  SER B OG  1 
ATOM   2074 N  N   . GLU B 1 82  ? 18.12386  -8.79824  -8.88420  1.000 30.40394  ? 114  GLU B N   1 
ATOM   2075 C  CA  . GLU B 1 82  ? 17.02978  -7.97292  -8.37830  1.000 31.13862  ? 114  GLU B CA  1 
ATOM   2076 C  C   . GLU B 1 82  ? 16.17711  -8.72413  -7.36723  1.000 31.86888  ? 114  GLU B C   1 
ATOM   2077 O  O   . GLU B 1 82  ? 15.78569  -8.16145  -6.33842  1.000 29.61012  ? 114  GLU B O   1 
ATOM   2078 C  CB  . GLU B 1 82  ? 16.16459  -7.47762  -9.53364  1.000 30.42359  ? 114  GLU B CB  1 
ATOM   2079 C  CG  . GLU B 1 82  ? 16.79217  -6.30241  -10.27942 1.000 34.06251  ? 114  GLU B CG  1 
ATOM   2080 C  CD  . GLU B 1 82  ? 16.89319  -5.05643  -9.40268  1.000 40.88230  ? 114  GLU B CD  1 
ATOM   2081 O  OE1 . GLU B 1 82  ? 15.88284  -4.63463  -8.78858  1.000 40.65058  ? 114  GLU B OE1 1 
ATOM   2082 O  OE2 . GLU B 1 82  ? 17.99867  -4.52252  -9.28684  1.000 43.33224  ? 114  GLU B OE2 1 
ATOM   2083 N  N   . GLY B 1 83  ? 15.84011  -9.97781  -7.65576  1.000 26.77482  ? 115  GLY B N   1 
ATOM   2084 C  CA  . GLY B 1 83  ? 15.01988  -10.72666 -6.71143  1.000 25.35934  ? 115  GLY B CA  1 
ATOM   2085 C  C   . GLY B 1 83  ? 15.74180  -10.96187 -5.39786  1.000 27.93149  ? 115  GLY B C   1 
ATOM   2086 O  O   . GLY B 1 83  ? 15.15740  -10.81916 -4.31535  1.000 28.96385  ? 115  GLY B O   1 
ATOM   2087 N  N   . THR B 1 84  ? 17.02313  -11.31905 -5.46568  1.000 30.83105  ? 116  THR B N   1 
ATOM   2088 C  CA  A THR B 1 84  ? 17.75762  -11.55437 -4.22660  0.207 32.91760  ? 116  THR B CA  1 
ATOM   2089 C  CA  B THR B 1 84  ? 17.80522  -11.54545 -4.24869  0.793 33.06902  ? 116  THR B CA  1 
ATOM   2090 C  C   . THR B 1 84  ? 17.92023  -10.27049 -3.42360  1.000 33.05894  ? 116  THR B C   1 
ATOM   2091 O  O   . THR B 1 84  ? 17.80898  -10.29296 -2.18863  1.000 33.35954  ? 116  THR B O   1 
ATOM   2092 C  CB  A THR B 1 84  ? 19.11480  -12.18530 -4.52056  0.207 35.29530  ? 116  THR B CB  1 
ATOM   2093 C  CB  B THR B 1 84  ? 19.19769  -12.06314 -4.62359  0.793 35.05948  ? 116  THR B CB  1 
ATOM   2094 O  OG1 A THR B 1 84  ? 19.87113  -11.32534 -5.37899  0.207 35.11821  ? 116  THR B OG1 1 
ATOM   2095 O  OG1 B THR B 1 84  ? 19.06876  -13.25647 -5.41096  0.793 33.19950  ? 116  THR B OG1 1 
ATOM   2096 C  CG2 A THR B 1 84  ? 18.91685  -13.53015 -5.19188  0.207 33.87961  ? 116  THR B CG2 1 
ATOM   2097 C  CG2 B THR B 1 84  ? 20.00274  -12.37279 -3.38996  0.793 39.33893  ? 116  THR B CG2 1 
ATOM   2098 N  N   . LYS B 1 85  ? 18.17700  -9.14585  -4.09123  1.000 29.08356  ? 117  LYS B N   1 
ATOM   2099 C  CA  . LYS B 1 85  ? 18.33011  -7.88546  -3.37457  1.000 34.51197  ? 117  LYS B CA  1 
ATOM   2100 C  C   . LYS B 1 85  ? 17.01925  -7.47431  -2.70507  1.000 35.66964  ? 117  LYS B C   1 
ATOM   2101 O  O   . LYS B 1 85  ? 17.03141  -6.92233  -1.59525  1.000 37.46095  ? 117  LYS B O   1 
ATOM   2102 C  CB  . LYS B 1 85  ? 18.86256  -6.80915  -4.32851  1.000 37.49851  ? 117  LYS B CB  1 
ATOM   2103 C  CG  . LYS B 1 85  ? 18.87543  -5.39085  -3.77655  1.000 47.69065  ? 117  LYS B CG  1 
ATOM   2104 C  CD  . LYS B 1 85  ? 19.39761  -4.38311  -4.81494  1.000 45.98848  ? 117  LYS B CD  1 
ATOM   2105 C  CE  . LYS B 1 85  ? 18.44532  -4.13846  -5.96489  1.000 47.81408  ? 117  LYS B CE  1 
ATOM   2106 N  NZ  . LYS B 1 85  ? 19.07234  -3.21278  -6.96981  1.000 53.09366  ? 117  LYS B NZ  1 
ATOM   2107 N  N   . ALA B 1 86  ? 15.88401  -7.71037  -3.37678  1.000 32.17691  ? 118  ALA B N   1 
ATOM   2108 C  CA  . ALA B 1 86  ? 14.58553  -7.36967  -2.79782  1.000 33.00627  ? 118  ALA B CA  1 
ATOM   2109 C  C   . ALA B 1 86  ? 14.27601  -8.22513  -1.57401  1.000 32.51205  ? 118  ALA B C   1 
ATOM   2110 O  O   . ALA B 1 86  ? 13.77896  -7.70942  -0.56894  1.000 33.69429  ? 118  ALA B O   1 
ATOM   2111 C  CB  . ALA B 1 86  ? 13.47856  -7.51145  -3.84492  1.000 32.39819  ? 118  ALA B CB  1 
ATOM   2112 N  N   . VAL B 1 87  ? 14.54635  -9.53282  -1.63508  1.000 29.36580  ? 119  VAL B N   1 
ATOM   2113 C  CA  . VAL B 1 87  ? 14.28200  -10.39297 -0.47713  1.000 31.08948  ? 119  VAL B CA  1 
ATOM   2114 C  C   . VAL B 1 87  ? 15.17673  -9.99968  0.69524   1.000 34.44371  ? 119  VAL B C   1 
ATOM   2115 O  O   . VAL B 1 87  ? 14.72986  -9.95171  1.84847   1.000 38.05355  ? 119  VAL B O   1 
ATOM   2116 C  CB  . VAL B 1 87  ? 14.45349  -11.87617 -0.84202  1.000 37.22692  ? 119  VAL B CB  1 
ATOM   2117 C  CG1 . VAL B 1 87  ? 14.38905  -12.75231 0.42155   1.000 39.60566  ? 119  VAL B CG1 1 
ATOM   2118 C  CG2 . VAL B 1 87  ? 13.37879  -12.31178 -1.85807  1.000 30.31157  ? 119  VAL B CG2 1 
ATOM   2119 N  N   . THR B 1 88  ? 16.45103  -9.70022  0.42148   1.000 36.97863  ? 120  THR B N   1 
ATOM   2120 C  CA  . THR B 1 88  ? 17.34326  -9.25325  1.48889   1.000 38.99037  ? 120  THR B CA  1 
ATOM   2121 C  C   . THR B 1 88  ? 16.82021  -7.98071  2.14289   1.000 40.64373  ? 120  THR B C   1 
ATOM   2122 O  O   . THR B 1 88  ? 16.77943  -7.87106  3.37388   1.000 44.30260  ? 120  THR B O   1 
ATOM   2123 C  CB  . THR B 1 88  ? 18.75791  -9.02530  0.94495   1.000 39.61634  ? 120  THR B CB  1 
ATOM   2124 O  OG1 . THR B 1 88  ? 19.29692  -10.26504 0.47250   1.000 41.00437  ? 120  THR B OG1 1 
ATOM   2125 C  CG2 . THR B 1 88  ? 19.66599  -8.46386  2.04302   1.000 39.93151  ? 120  THR B CG2 1 
ATOM   2126 N  N   . LYS B 1 89  ? 16.40769  -7.00801  1.33319   1.000 38.05723  ? 121  LYS B N   1 
ATOM   2127 C  CA  . LYS B 1 89  ? 15.88494  -5.76122  1.87521   1.000 38.17557  ? 121  LYS B CA  1 
ATOM   2128 C  C   . LYS B 1 89  ? 14.60052  -5.99172  2.66598   1.000 40.83208  ? 121  LYS B C   1 
ATOM   2129 O  O   . LYS B 1 89  ? 14.42377  -5.43761  3.75885   1.000 44.22505  ? 121  LYS B O   1 
ATOM   2130 C  CB  . LYS B 1 89  ? 15.65821  -4.77331  0.73072   1.000 43.22205  ? 121  LYS B CB  1 
ATOM   2131 C  CG  . LYS B 1 89  ? 15.32787  -3.35433  1.12585   1.000 49.50050  ? 121  LYS B CG  1 
ATOM   2132 C  CD  . LYS B 1 89  ? 15.24460  -2.48292  -0.12287  1.000 54.22571  ? 121  LYS B CD  1 
ATOM   2133 C  CE  . LYS B 1 89  ? 14.67458  -1.10490  0.18562   1.000 60.97686  ? 121  LYS B CE  1 
ATOM   2134 N  NZ  . LYS B 1 89  ? 15.34693  -0.47127  1.34793   1.000 60.98765  ? 121  LYS B NZ  1 
ATOM   2135 N  N   . TYR B 1 90  ? 13.70855  -6.83511  2.14275   1.000 40.06547  ? 122  TYR B N   1 
ATOM   2136 C  CA  . TYR B 1 90  ? 12.40161  -7.03488  2.76126   1.000 37.53979  ? 122  TYR B CA  1 
ATOM   2137 C  C   . TYR B 1 90  ? 12.52963  -7.69195  4.12568   1.000 43.57091  ? 122  TYR B C   1 
ATOM   2138 O  O   . TYR B 1 90  ? 11.73456  -7.41248  5.02741   1.000 43.50815  ? 122  TYR B O   1 
ATOM   2139 C  CB  . TYR B 1 90  ? 11.54363  -7.88580  1.82772   1.000 36.91220  ? 122  TYR B CB  1 
ATOM   2140 C  CG  . TYR B 1 90  ? 10.11760  -8.15444  2.24786   1.000 35.08572  ? 122  TYR B CG  1 
ATOM   2141 C  CD1 . TYR B 1 90  ? 9.08968   -7.28888  1.88010   1.000 39.63780  ? 122  TYR B CD1 1 
ATOM   2142 C  CD2 . TYR B 1 90  ? 9.78780   -9.30631  2.94358   1.000 36.83007  ? 122  TYR B CD2 1 
ATOM   2143 C  CE1 . TYR B 1 90  ? 7.76722   -7.55648  2.22006   1.000 38.41123  ? 122  TYR B CE1 1 
ATOM   2144 C  CE2 . TYR B 1 90  ? 8.47329   -9.57995  3.28947   1.000 39.37164  ? 122  TYR B CE2 1 
ATOM   2145 C  CZ  . TYR B 1 90  ? 7.47288   -8.70400  2.92600   1.000 35.36316  ? 122  TYR B CZ  1 
ATOM   2146 O  OH  . TYR B 1 90  ? 6.17645   -8.99101  3.27349   1.000 41.20559  ? 122  TYR B OH  1 
ATOM   2147 N  N   . THR B 1 91  ? 13.48503  -8.60784  4.27414   1.000 44.15903  ? 123  THR B N   1 
ATOM   2148 C  CA  . THR B 1 91  ? 13.71391  -9.35234  5.50300   1.000 44.23673  ? 123  THR B CA  1 
ATOM   2149 C  C   . THR B 1 91  ? 14.71185  -8.66802  6.44547   1.000 46.00670  ? 123  THR B C   1 
ATOM   2150 O  O   . THR B 1 91  ? 15.10259  -9.26854  7.44877   1.000 52.47750  ? 123  THR B O   1 
ATOM   2151 C  CB  . THR B 1 91  ? 14.19635  -10.77168 5.17113   1.000 45.82387  ? 123  THR B CB  1 
ATOM   2152 O  OG1 . THR B 1 91  ? 15.42750  -10.70328 4.43709   1.000 47.72368  ? 123  THR B OG1 1 
ATOM   2153 C  CG2 . THR B 1 91  ? 13.15713  -11.52616 4.33012   1.000 42.50867  ? 123  THR B CG2 1 
ATOM   2154 N  N   . SER B 1 92  ? 15.08731  -7.41999  6.17775   1.000 49.87273  ? 124  SER B N   1 
ATOM   2155 C  CA  . SER B 1 92  ? 16.12578  -6.75663  6.95940   1.000 47.83788  ? 124  SER B CA  1 
ATOM   2156 C  C   . SER B 1 92  ? 15.66394  -6.46926  8.37798   1.000 57.12499  ? 124  SER B C   1 
ATOM   2157 O  O   . SER B 1 92  ? 14.49093  -6.18598  8.62499   1.000 51.23787  ? 124  SER B O   1 
ATOM   2158 C  CB  . SER B 1 92  ? 16.52331  -5.44417  6.29695   1.000 59.90207  ? 124  SER B CB  1 
ATOM   2159 O  OG  . SER B 1 92  ? 15.45147  -4.51599  6.37786   1.000 60.94817  ? 124  SER B OG  1 
ATOM   2160 N  N   . ALA B 1 93  ? 16.62404  -6.53081  9.31484   1.000 55.13345  ? 125  ALA B N   1 
ATOM   2161 C  CA  . ALA B 1 93  ? 16.33052  -6.31776  10.72799  1.000 61.28737  ? 125  ALA B CA  1 
ATOM   2162 C  C   . ALA B 1 93  ? 15.84315  -4.90422  11.00745  1.000 67.53005  ? 125  ALA B C   1 
ATOM   2163 O  O   . ALA B 1 93  ? 15.00390  -4.70471  11.89183  1.000 70.19154  ? 125  ALA B O   1 
ATOM   2164 C  CB  . ALA B 1 93  ? 17.56576  -6.63033  11.57630  1.000 65.47777  ? 125  ALA B CB  1 
ATOM   2165 N  N   . LYS B 1 94  ? 16.34126  -3.91320  10.27501  1.000 67.61647  ? 126  LYS B N   1 
ATOM   2166 C  CA  . LYS B 1 94  ? 15.88011  -2.54415  10.47198  1.000 76.30954  ? 126  LYS B CA  1 
ATOM   2167 C  C   . LYS B 1 94  ? 14.58678  -2.41625  9.68832   1.000 77.24488  ? 126  LYS B C   1 
ATOM   2168 O  O   . LYS B 1 94  ? 14.59878  -2.43392  8.45358   1.000 70.56322  ? 126  LYS B O   1 
ATOM   2169 C  CB  . LYS B 1 94  ? 16.91528  -1.52148  10.00774  1.000 83.55805  ? 126  LYS B CB  1 
ATOM   2170 C  CG  . LYS B 1 94  ? 16.68157  -0.11400  10.55898  1.000 86.35432  ? 126  LYS B CG  1 
ATOM   2171 C  CD  . LYS B 1 94  ? 15.78366  0.70988   9.64896   1.000 94.04265  ? 126  LYS B CD  1 
ATOM   2172 C  CE  . LYS B 1 94  ? 15.22317  1.91577   10.35672  1.000 98.09394  ? 126  LYS B CE  1 
ATOM   2173 N  NZ  . LYS B 1 94  ? 15.16881  3.04785   9.40445   1.000 111.68286 ? 126  LYS B NZ  1 
ATOM   2174 N  N   . LYS B 1 95  ? 13.47196  -2.29487  10.39993  1.000 75.86476  ? 1014 LYS B N   1 
ATOM   2175 C  CA  . LYS B 1 95  ? 12.18639  -2.24421  9.72497   1.000 75.18066  ? 1014 LYS B CA  1 
ATOM   2176 C  C   . LYS B 1 95  ? 11.99281  -0.92269  8.99373   1.000 71.85238  ? 1014 LYS B C   1 
ATOM   2177 O  O   . LYS B 1 95  ? 12.31121  0.15135   9.51271   1.000 69.47231  ? 1014 LYS B O   1 
ATOM   2178 C  CB  . LYS B 1 95  ? 11.06117  -2.44198  10.74009  1.000 72.14467  ? 1014 LYS B CB  1 
ATOM   2179 C  CG  . LYS B 1 95  ? 11.08910  -3.79062  11.43756  1.000 75.64659  ? 1014 LYS B CG  1 
ATOM   2180 C  CD  . LYS B 1 95  ? 11.22831  -4.91278  10.41776  1.000 69.91375  ? 1014 LYS B CD  1 
ATOM   2181 C  CE  . LYS B 1 95  ? 10.55221  -6.19458  10.88481  1.000 76.03203  ? 1014 LYS B CE  1 
ATOM   2182 N  NZ  . LYS B 1 95  ? 10.59748  -7.25634  9.83435   1.000 73.44609  ? 1014 LYS B NZ  1 
ATOM   2183 N  N   . ALA B 1 96  ? 11.42615  -1.00889  7.79583   1.000 67.07131  ? 1015 ALA B N   1 
ATOM   2184 C  CA  . ALA B 1 96  ? 11.06766  0.17792   7.04883   1.000 58.12616  ? 1015 ALA B CA  1 
ATOM   2185 C  C   . ALA B 1 96  ? 9.78073   0.73773   7.63404   1.000 59.16694  ? 1015 ALA B C   1 
ATOM   2186 O  O   . ALA B 1 96  ? 9.05952   0.05033   8.35480   1.000 64.53790  ? 1015 ALA B O   1 
ATOM   2187 C  CB  . ALA B 1 96  ? 10.89703  -0.15084  5.56844   1.000 54.22707  ? 1015 ALA B CB  1 
ATOM   2188 N  N   . LYS B 1 97  ? 9.46532   1.98043   7.30285   1.000 57.15260  ? 1016 LYS B N   1 
ATOM   2189 C  CA  . LYS B 1 97  ? 8.24040   2.54272   7.84146   1.000 63.65265  ? 1016 LYS B CA  1 
ATOM   2190 C  C   . LYS B 1 97  ? 7.05877   2.43571   6.89822   1.000 52.99035  ? 1016 LYS B C   1 
ATOM   2191 O  O   . LYS B 1 97  ? 5.93465   2.74165   7.30401   1.000 60.12048  ? 1016 LYS B O   1 
ATOM   2192 C  CB  . LYS B 1 97  ? 8.45860   4.02022   8.17271   1.000 65.51961  ? 1016 LYS B CB  1 
ATOM   2193 C  CG  . LYS B 1 97  ? 9.38814   4.32034   9.32721   1.000 71.88349  ? 1016 LYS B CG  1 
ATOM   2194 C  CD  . LYS B 1 97  ? 8.81534   3.89943   10.66380  1.000 77.43573  ? 1016 LYS B CD  1 
ATOM   2195 C  CE  . LYS B 1 97  ? 9.79983   4.18854   11.77145  1.000 82.90482  ? 1016 LYS B CE  1 
ATOM   2196 N  NZ  . LYS B 1 97  ? 10.28160  5.57735   11.61026  1.000 90.44738  ? 1016 LYS B NZ  1 
ATOM   2197 N  N   . THR B 1 98  ? 7.27198   1.96177   5.68346   1.000 54.27245  ? 1017 THR B N   1 
ATOM   2198 C  CA  . THR B 1 98  ? 6.20762   1.84437   4.70031   1.000 53.96446  ? 1017 THR B CA  1 
ATOM   2199 C  C   . THR B 1 98  ? 6.49354   0.63103   3.83115   1.000 53.55510  ? 1017 THR B C   1 
ATOM   2200 O  O   . THR B 1 98  ? 7.62991   0.15889   3.73838   1.000 53.68475  ? 1017 THR B O   1 
ATOM   2201 C  CB  . THR B 1 98  ? 6.03752   3.11335   3.83201   1.000 54.20999  ? 1017 THR B CB  1 
ATOM   2202 O  OG1 . THR B 1 98  ? 7.09554   3.18929   2.86610   1.000 59.46627  ? 1017 THR B OG1 1 
ATOM   2203 C  CG2 . THR B 1 98  ? 5.95985   4.40402   4.66254   1.000 60.76320  ? 1017 THR B CG2 1 
ATOM   2204 N  N   . ARG B 1 99  ? 5.42428   0.09201   3.24099   1.000 48.18949  ? 1018 ARG B N   1 
ATOM   2205 C  CA  . ARG B 1 99  ? 5.55270   -1.00555  2.29711   1.000 45.67003  ? 1018 ARG B CA  1 
ATOM   2206 C  C   . ARG B 1 99  ? 6.48570   -0.65101  1.15109   1.000 53.84727  ? 1018 ARG B C   1 
ATOM   2207 O  O   . ARG B 1 99  ? 7.33224   -1.46257  0.76644   1.000 45.08262  ? 1018 ARG B O   1 
ATOM   2208 C  CB  . ARG B 1 99  ? 4.16813   -1.37324  1.77366   1.000 42.17410  ? 1018 ARG B CB  1 
ATOM   2209 C  CG  . ARG B 1 99  ? 3.22652   -1.86658  2.87395   1.000 42.93395  ? 1018 ARG B CG  1 
ATOM   2210 C  CD  . ARG B 1 99  ? 1.81249   -1.82410  2.36029   1.000 45.92908  ? 1018 ARG B CD  1 
ATOM   2211 N  NE  . ARG B 1 99  ? 1.40923   -0.42998  2.21267   1.000 44.05605  ? 1018 ARG B NE  1 
ATOM   2212 C  CZ  . ARG B 1 99  ? 0.40099   -0.01021  1.46141   1.000 46.50377  ? 1018 ARG B CZ  1 
ATOM   2213 N  NH1 . ARG B 1 99  ? -0.34413  -0.85571  0.76854   1.000 40.02452  ? 1018 ARG B NH1 1 
ATOM   2214 N  NH2 . ARG B 1 99  ? 0.13748   1.29126   1.40094   1.000 45.40569  ? 1018 ARG B NH2 1 
ATOM   2215 N  N   . SER B 1 100 ? 6.35299   0.56032   0.59684   1.000 48.20536  ? 1019 SER B N   1 
ATOM   2216 C  CA  . SER B 1 100 ? 7.18938   0.93602   -0.54168  1.000 57.19214  ? 1019 SER B CA  1 
ATOM   2217 C  C   . SER B 1 100 ? 8.66988   0.92110   -0.18276  1.000 55.55396  ? 1019 SER B C   1 
ATOM   2218 O  O   . SER B 1 100 ? 9.50612   0.48981   -0.98595  1.000 54.17436  ? 1019 SER B O   1 
ATOM   2219 C  CB  . SER B 1 100 ? 6.79306   2.32098   -1.04263  1.000 54.07602  ? 1019 SER B CB  1 
ATOM   2220 O  OG  . SER B 1 100 ? 7.24327   3.31098   -0.13603  1.000 62.54362  ? 1019 SER B OG  1 
ATOM   2221 N  N   . SER B 1 101 ? 9.01336   1.41905   1.00399   1.000 52.43818  ? 1020 SER B N   1 
ATOM   2222 C  CA  . SER B 1 101 ? 10.39938  1.46542   1.45473   1.000 59.16356  ? 1020 SER B CA  1 
ATOM   2223 C  C   . SER B 1 101 ? 10.92644  0.11310   1.91125   1.000 55.97864  ? 1020 SER B C   1 
ATOM   2224 O  O   . SER B 1 101 ? 12.14172  -0.04251  2.06657   1.000 59.26537  ? 1020 SER B O   1 
ATOM   2225 C  CB  . SER B 1 101 ? 10.57406  2.50735   2.56548   1.000 60.24242  ? 1020 SER B CB  1 
ATOM   2226 O  OG  . SER B 1 101 ? 9.76957   2.23750   3.70423   1.000 62.25356  ? 1020 SER B OG  1 
ATOM   2227 N  N   . ARG B 1 102 ? 10.04840  -0.84649  2.19248   1.000 51.25391  ? 1021 ARG B N   1 
ATOM   2228 C  CA  . ARG B 1 102 ? 10.52155  -2.13294  2.69126   1.000 45.01837  ? 1021 ARG B CA  1 
ATOM   2229 C  C   . ARG B 1 102 ? 11.21986  -2.96298  1.62054   1.000 45.92082  ? 1021 ARG B C   1 
ATOM   2230 O  O   . ARG B 1 102 ? 12.20629  -3.64675  1.91017   1.000 44.21293  ? 1021 ARG B O   1 
ATOM   2231 C  CB  . ARG B 1 102 ? 9.35311   -2.91942  3.26061   1.000 44.08394  ? 1021 ARG B CB  1 
ATOM   2232 C  CG  . ARG B 1 102 ? 9.75490   -4.27497  3.73383   1.000 47.93291  ? 1021 ARG B CG  1 
ATOM   2233 C  CD  . ARG B 1 102 ? 8.69080   -4.83836  4.62116   1.000 49.68067  ? 1021 ARG B CD  1 
ATOM   2234 N  NE  . ARG B 1 102 ? 9.09172   -6.11593  5.18676   1.000 43.41385  ? 1021 ARG B NE  1 
ATOM   2235 C  CZ  . ARG B 1 102 ? 8.28846   -6.88237  5.90792   1.000 51.49369  ? 1021 ARG B CZ  1 
ATOM   2236 N  NH1 . ARG B 1 102 ? 7.02748   -6.54071  6.12846   1.000 53.41582  ? 1021 ARG B NH1 1 
ATOM   2237 N  NH2 . ARG B 1 102 ? 8.76305   -8.01309  6.42827   1.000 46.86432  ? 1021 ARG B NH2 1 
ATOM   2238 N  N   . ALA B 1 103 ? 10.72685  -2.93500  0.38761   1.000 43.48587  ? 1022 ALA B N   1 
ATOM   2239 C  CA  . ALA B 1 103 ? 11.31007  -3.74621  -0.67663  1.000 39.90112  ? 1022 ALA B CA  1 
ATOM   2240 C  C   . ALA B 1 103 ? 11.94226  -2.92989  -1.79142  1.000 50.19959  ? 1022 ALA B C   1 
ATOM   2241 O  O   . ALA B 1 103 ? 12.57806  -3.51598  -2.68181  1.000 43.78625  ? 1022 ALA B O   1 
ATOM   2242 C  CB  . ALA B 1 103 ? 10.25290  -4.69550  -1.26966  1.000 41.23562  ? 1022 ALA B CB  1 
ATOM   2243 N  N   . GLY B 1 104 ? 11.74516  -1.61364  -1.79469  1.000 46.53380  ? 1023 GLY B N   1 
ATOM   2244 C  CA  . GLY B 1 104 ? 12.28911  -0.76459  -2.83407  1.000 49.99301  ? 1023 GLY B CA  1 
ATOM   2245 C  C   . GLY B 1 104 ? 11.63424  -0.92032  -4.19046  1.000 43.03720  ? 1023 GLY B C   1 
ATOM   2246 O  O   . GLY B 1 104 ? 12.22602  -0.53004  -5.20014  1.000 46.30671  ? 1023 GLY B O   1 
ATOM   2247 N  N   . LEU B 1 105 ? 10.40815  -1.43831  -4.24182  1.000 39.38232  ? 1024 LEU B N   1 
ATOM   2248 C  CA  . LEU B 1 105 ? 9.74489   -1.78090  -5.49122  1.000 41.86240  ? 1024 LEU B CA  1 
ATOM   2249 C  C   . LEU B 1 105 ? 8.52339   -0.90116  -5.75316  1.000 44.53039  ? 1024 LEU B C   1 
ATOM   2250 O  O   . LEU B 1 105 ? 7.99951   -0.22996  -4.85882  1.000 48.34036  ? 1024 LEU B O   1 
ATOM   2251 C  CB  . LEU B 1 105 ? 9.32474   -3.25471  -5.48467  1.000 35.94171  ? 1024 LEU B CB  1 
ATOM   2252 C  CG  . LEU B 1 105 ? 10.44805  -4.25834  -5.21453  1.000 41.07905  ? 1024 LEU B CG  1 
ATOM   2253 C  CD1 . LEU B 1 105 ? 9.87728   -5.66876  -5.13649  1.000 37.63077  ? 1024 LEU B CD1 1 
ATOM   2254 C  CD2 . LEU B 1 105 ? 11.47261  -4.17353  -6.34964  1.000 42.27199  ? 1024 LEU B CD2 1 
ATOM   2255 N  N   . GLN B 1 106 ? 8.08815   -0.90856  -7.01711  1.000 41.45091  ? 1025 GLN B N   1 
ATOM   2256 C  CA  . GLN B 1 106 ? 6.81553   -0.34535  -7.45886  1.000 46.43855  ? 1025 GLN B CA  1 
ATOM   2257 C  C   . GLN B 1 106 ? 5.70758   -1.38955  -7.50839  1.000 43.96232  ? 1025 GLN B C   1 
ATOM   2258 O  O   . GLN B 1 106 ? 4.55071   -1.07613  -7.19932  1.000 48.45822  ? 1025 GLN B O   1 
ATOM   2259 C  CB  . GLN B 1 106 ? 6.97248   0.27312   -8.84833  1.000 46.56934  ? 1025 GLN B CB  1 
ATOM   2260 C  CG  . GLN B 1 106 ? 8.06572   1.31254   -8.90256  1.000 52.06273  ? 1025 GLN B CG  1 
ATOM   2261 C  CD  . GLN B 1 106 ? 7.81963   2.43465   -7.92588  1.000 50.91446  ? 1025 GLN B CD  1 
ATOM   2262 O  OE1 . GLN B 1 106 ? 6.75409   3.05863   -7.93204  1.000 52.31471  ? 1025 GLN B OE1 1 
ATOM   2263 N  NE2 . GLN B 1 106 ? 8.77278   2.65660   -7.03806  1.000 55.00921  ? 1025 GLN B NE2 1 
ATOM   2264 N  N   . PHE B 1 107 ? 6.04196   -2.62397  -7.91348  1.000 35.63419  ? 1026 PHE B N   1 
ATOM   2265 C  CA  . PHE B 1 107 ? 5.06211   -3.70093  -7.94853  1.000 32.87848  ? 1026 PHE B CA  1 
ATOM   2266 C  C   . PHE B 1 107 ? 4.74992   -4.10578  -6.51284  1.000 39.78521  ? 1026 PHE B C   1 
ATOM   2267 O  O   . PHE B 1 107 ? 5.67864   -4.31326  -5.72431  1.000 43.25462  ? 1026 PHE B O   1 
ATOM   2268 C  CB  . PHE B 1 107 ? 5.61375   -4.91333  -8.70839  1.000 28.58726  ? 1026 PHE B CB  1 
ATOM   2269 C  CG  . PHE B 1 107 ? 5.43486   -4.84108  -10.21595 1.000 32.64357  ? 1026 PHE B CG  1 
ATOM   2270 C  CD1 . PHE B 1 107 ? 5.96032   -3.78335  -10.93737 1.000 37.33123  ? 1026 PHE B CD1 1 
ATOM   2271 C  CD2 . PHE B 1 107 ? 4.73453   -5.82302  -10.88732 1.000 34.20181  ? 1026 PHE B CD2 1 
ATOM   2272 C  CE1 . PHE B 1 107 ? 5.80170   -3.70887  -12.31295 1.000 39.89474  ? 1026 PHE B CE1 1 
ATOM   2273 C  CE2 . PHE B 1 107 ? 4.57174   -5.76102  -12.28105 1.000 36.39695  ? 1026 PHE B CE2 1 
ATOM   2274 C  CZ  . PHE B 1 107 ? 5.10223   -4.69167  -12.98061 1.000 32.83133  ? 1026 PHE B CZ  1 
ATOM   2275 N  N   . PRO B 1 108 ? 3.47942   -4.26670  -6.14695  1.000 35.03387  ? 1027 PRO B N   1 
ATOM   2276 C  CA  . PRO B 1 108 ? 3.13089   -4.49060  -4.73326  1.000 34.33044  ? 1027 PRO B CA  1 
ATOM   2277 C  C   . PRO B 1 108 ? 3.23813   -5.96322  -4.36589  1.000 33.51252  ? 1027 PRO B C   1 
ATOM   2278 O  O   . PRO B 1 108 ? 2.73221   -6.83612  -5.07618  1.000 35.41581  ? 1027 PRO B O   1 
ATOM   2279 C  CB  . PRO B 1 108 ? 1.69037   -3.97834  -4.63276  1.000 41.74476  ? 1027 PRO B CB  1 
ATOM   2280 C  CG  . PRO B 1 108 ? 1.14819   -4.18129  -6.00474  1.000 49.41935  ? 1027 PRO B CG  1 
ATOM   2281 C  CD  . PRO B 1 108 ? 2.28969   -4.00028  -6.97076  1.000 43.44914  ? 1027 PRO B CD  1 
ATOM   2282 N  N   . VAL B 1 109 ? 3.92814   -6.23072  -3.25617  1.000 33.07200  ? 1028 VAL B N   1 
ATOM   2283 C  CA  . VAL B 1 109 ? 4.16136   -7.60347  -2.81995  1.000 30.35878  ? 1028 VAL B CA  1 
ATOM   2284 C  C   . VAL B 1 109 ? 2.84331   -8.33830  -2.59537  1.000 33.72250  ? 1028 VAL B C   1 
ATOM   2285 O  O   . VAL B 1 109 ? 2.69969   -9.51585  -2.95396  1.000 31.91325  ? 1028 VAL B O   1 
ATOM   2286 C  CB  . VAL B 1 109 ? 5.04122   -7.58792  -1.55630  1.000 35.64687  ? 1028 VAL B CB  1 
ATOM   2287 C  CG1 . VAL B 1 109 ? 5.08422   -8.95961  -0.90323  1.000 40.50718  ? 1028 VAL B CG1 1 
ATOM   2288 C  CG2 . VAL B 1 109 ? 6.45208   -7.09512  -1.93343  1.000 36.27996  ? 1028 VAL B CG2 1 
ATOM   2289 N  N   . GLY B 1 110 ? 1.86600   -7.65723  -2.00347  1.000 33.15199  ? 1029 GLY B N   1 
ATOM   2290 C  CA  . GLY B 1 110 ? 0.60668   -8.30314  -1.65847  1.000 37.39862  ? 1029 GLY B CA  1 
ATOM   2291 C  C   . GLY B 1 110 ? -0.17700  -8.76483  -2.87079  1.000 37.07501  ? 1029 GLY B C   1 
ATOM   2292 O  O   . GLY B 1 110 ? -0.86811  -9.78498  -2.82072  1.000 33.71272  ? 1029 GLY B O   1 
ATOM   2293 N  N   . ARG B 1 111 ? -0.13552  -7.99088  -3.95518  1.000 33.18467  ? 1030 ARG B N   1 
ATOM   2294 C  CA  . ARG B 1 111 ? -0.80717  -8.43170  -5.17194  1.000 36.16427  ? 1030 ARG B CA  1 
ATOM   2295 C  C   . ARG B 1 111 ? -0.17769  -9.70941  -5.71497  1.000 33.00768  ? 1030 ARG B C   1 
ATOM   2296 O  O   . ARG B 1 111 ? -0.88573  -10.66935 -6.04892  1.000 35.86525  ? 1030 ARG B O   1 
ATOM   2297 C  CB  . ARG B 1 111 ? -0.79415  -7.33133  -6.22663  1.000 41.96560  ? 1030 ARG B CB  1 
ATOM   2298 C  CG  . ARG B 1 111 ? -0.99812  -7.89748  -7.63430  1.000 46.96425  ? 1030 ARG B CG  1 
ATOM   2299 C  CD  . ARG B 1 111 ? -2.46638  -8.02704  -8.01378  1.000 55.01139  ? 1030 ARG B CD  1 
ATOM   2300 N  NE  . ARG B 1 111 ? -3.20213  -6.77914  -7.86639  1.000 63.48846  ? 1030 ARG B NE  1 
ATOM   2301 C  CZ  . ARG B 1 111 ? -3.51564  -5.97244  -8.87132  1.000 67.01185  ? 1030 ARG B CZ  1 
ATOM   2302 N  NH1 . ARG B 1 111 ? -3.12173  -6.22612  -10.10698 1.000 57.35261  ? 1030 ARG B NH1 1 
ATOM   2303 N  NH2 . ARG B 1 111 ? -4.24360  -4.88380  -8.62825  1.000 67.43228  ? 1030 ARG B NH2 1 
ATOM   2304 N  N   . VAL B 1 112 ? 1.15354   -9.75630  -5.77014  1.000 29.93371  ? 1031 VAL B N   1 
ATOM   2305 C  CA  . VAL B 1 112 ? 1.81703   -10.95934 -6.26527  1.000 26.70789  ? 1031 VAL B CA  1 
ATOM   2306 C  C   . VAL B 1 112 ? 1.52329   -12.13745 -5.34433  1.000 28.85548  ? 1031 VAL B C   1 
ATOM   2307 O  O   . VAL B 1 112 ? 1.28102   -13.25936 -5.80570  1.000 30.57873  ? 1031 VAL B O   1 
ATOM   2308 C  CB  . VAL B 1 112 ? 3.32689   -10.71967 -6.42438  1.000 30.73815  ? 1031 VAL B CB  1 
ATOM   2309 C  CG1 . VAL B 1 112 ? 4.03667   -12.01242 -6.87072  1.000 29.30897  ? 1031 VAL B CG1 1 
ATOM   2310 C  CG2 . VAL B 1 112 ? 3.58664   -9.59216  -7.43933  1.000 31.09593  ? 1031 VAL B CG2 1 
ATOM   2311 N  N   . HIS B 1 113 ? 1.49754   -11.89734 -4.02866  1.000 27.90196  ? 1032 HIS B N   1 
ATOM   2312 C  CA  . HIS B 1 113 ? 1.16754   -12.97367 -3.09623  1.000 28.78032  ? 1032 HIS B CA  1 
ATOM   2313 C  C   . HIS B 1 113 ? -0.22844  -13.52890 -3.36047  1.000 35.96295  ? 1032 HIS B C   1 
ATOM   2314 O  O   . HIS B 1 113 ? -0.43301  -14.74860 -3.42392  1.000 32.05797  ? 1032 HIS B O   1 
ATOM   2315 C  CB  . HIS B 1 113 ? 1.26037   -12.45678 -1.65843  1.000 32.16793  ? 1032 HIS B CB  1 
ATOM   2316 C  CG  . HIS B 1 113 ? 1.38939   -13.54114 -0.63773  1.000 42.81689  ? 1032 HIS B CG  1 
ATOM   2317 N  ND1 . HIS B 1 113 ? 1.50367   -13.28401 0.71028   1.000 52.40274  ? 1032 HIS B ND1 1 
ATOM   2318 C  CD2 . HIS B 1 113 ? 1.42289   -14.88721 -0.76685  1.000 48.41693  ? 1032 HIS B CD2 1 
ATOM   2319 C  CE1 . HIS B 1 113 ? 1.60388   -14.42465 1.36800   1.000 61.84836  ? 1032 HIS B CE1 1 
ATOM   2320 N  NE2 . HIS B 1 113 ? 1.55824   -15.41280 0.49367   1.000 54.53569  ? 1032 HIS B NE2 1 
ATOM   2321 N  N   . ARG B 1 114 ? -1.20835  -12.64306 -3.50378  1.000 34.01538  ? 1033 ARG B N   1 
ATOM   2322 C  CA  . ARG B 1 114 ? -2.57120  -13.08612 -3.74563  1.000 32.13990  ? 1033 ARG B CA  1 
ATOM   2323 C  C   . ARG B 1 114 ? -2.67393  -13.86212 -5.05433  1.000 33.90683  ? 1033 ARG B C   1 
ATOM   2324 O  O   . ARG B 1 114 ? -3.40883  -14.85528 -5.13390  1.000 38.69699  ? 1033 ARG B O   1 
ATOM   2325 C  CB  . ARG B 1 114 ? -3.50549  -11.87992 -3.72123  1.000 38.82942  ? 1033 ARG B CB  1 
ATOM   2326 C  CG  . ARG B 1 114 ? -4.96129  -12.18010 -3.98165  1.000 54.63294  ? 1033 ARG B CG  1 
ATOM   2327 C  CD  . ARG B 1 114 ? -5.81661  -10.95233 -3.67645  1.000 59.88283  ? 1033 ARG B CD  1 
ATOM   2328 N  NE  . ARG B 1 114 ? -5.39533  -9.75785  -4.39900  1.000 64.00599  ? 1033 ARG B NE  1 
ATOM   2329 C  CZ  . ARG B 1 114 ? -5.71125  -9.48018  -5.65564  1.000 70.63028  ? 1033 ARG B CZ  1 
ATOM   2330 N  NH1 . ARG B 1 114 ? -6.43116  -10.31463 -6.38932  1.000 76.16491  ? 1033 ARG B NH1 1 
ATOM   2331 N  NH2 . ARG B 1 114 ? -5.30269  -8.33106  -6.18604  1.000 66.77536  ? 1033 ARG B NH2 1 
ATOM   2332 N  N   . LEU B 1 115 ? -1.94847  -13.42635 -6.08691  1.000 34.03124  ? 1034 LEU B N   1 
ATOM   2333 C  CA  . LEU B 1 115 ? -2.00524  -14.13112 -7.37001  1.000 39.54407  ? 1034 LEU B CA  1 
ATOM   2334 C  C   . LEU B 1 115 ? -1.36840  -15.51321 -7.28013  1.000 36.80548  ? 1034 LEU B C   1 
ATOM   2335 O  O   . LEU B 1 115 ? -1.87975  -16.47263 -7.86968  1.000 36.65438  ? 1034 LEU B O   1 
ATOM   2336 C  CB  . LEU B 1 115 ? -1.33897  -13.30727 -8.46340  1.000 41.08079  ? 1034 LEU B CB  1 
ATOM   2337 C  CG  . LEU B 1 115 ? -2.00943  -11.98135 -8.81671  1.000 46.10901  ? 1034 LEU B CG  1 
ATOM   2338 C  CD1 . LEU B 1 115 ? -1.07736  -11.16982 -9.70207  1.000 43.21245  ? 1034 LEU B CD1 1 
ATOM   2339 C  CD2 . LEU B 1 115 ? -3.37465  -12.19837 -9.47842  1.000 56.39079  ? 1034 LEU B CD2 1 
ATOM   2340 N  N   . LEU B 1 116 ? -0.25990  -15.64130 -6.54718  1.000 30.82253  ? 1035 LEU B N   1 
ATOM   2341 C  CA  . LEU B 1 116 ? 0.32572   -16.96358 -6.33776  1.000 33.23043  ? 1035 LEU B CA  1 
ATOM   2342 C  C   . LEU B 1 116 ? -0.62289  -17.86143 -5.56036  1.000 36.61952  ? 1035 LEU B C   1 
ATOM   2343 O  O   . LEU B 1 116 ? -0.77594  -19.04428 -5.88564  1.000 38.02776  ? 1035 LEU B O   1 
ATOM   2344 C  CB  . LEU B 1 116 ? 1.66495   -16.84439 -5.60742  1.000 30.99625  ? 1035 LEU B CB  1 
ATOM   2345 C  CG  . LEU B 1 116 ? 2.84347   -16.36651 -6.45605  1.000 29.75628  ? 1035 LEU B CG  1 
ATOM   2346 C  CD1 . LEU B 1 116 ? 4.03621   -16.04986 -5.56503  1.000 29.10715  ? 1035 LEU B CD1 1 
ATOM   2347 C  CD2 . LEU B 1 116 ? 3.22439   -17.44123 -7.46973  1.000 28.33660  ? 1035 LEU B CD2 1 
ATOM   2348 N  N   . ARG B 1 117 ? -1.26657  -17.32241 -4.51504  1.000 33.96890  ? 1036 ARG B N   1 
ATOM   2349 C  CA  . ARG B 1 117 ? -2.21144  -18.14051 -3.76532  1.000 35.23152  ? 1036 ARG B CA  1 
ATOM   2350 C  C   . ARG B 1 117 ? -3.42063  -18.51966 -4.61599  1.000 38.74180  ? 1036 ARG B C   1 
ATOM   2351 O  O   . ARG B 1 117 ? -3.86745  -19.67383 -4.58100  1.000 42.24509  ? 1036 ARG B O   1 
ATOM   2352 C  CB  . ARG B 1 117 ? -2.62676  -17.41974 -2.47874  1.000 38.56434  ? 1036 ARG B CB  1 
ATOM   2353 C  CG  . ARG B 1 117 ? -1.75370  -17.85450 -1.30487  1.000 51.91064  ? 1036 ARG B CG  1 
ATOM   2354 C  CD  . ARG B 1 117 ? -1.96929  -17.06339 -0.02726  1.000 69.03746  ? 1036 ARG B CD  1 
ATOM   2355 N  NE  . ARG B 1 117 ? -0.80958  -17.15381 0.85700   1.000 72.44388  ? 1036 ARG B NE  1 
ATOM   2356 C  CZ  . ARG B 1 117 ? -0.77461  -16.70029 2.10405   1.000 85.18959  ? 1036 ARG B CZ  1 
ATOM   2357 N  NH1 . ARG B 1 117 ? -1.77078  -15.98234 2.60636   1.000 90.62797  ? 1036 ARG B NH1 1 
ATOM   2358 N  NH2 . ARG B 1 117 ? 0.30124   -16.94091 2.85349   1.000 78.32677  ? 1036 ARG B NH2 1 
ATOM   2359 N  N   . LYS B 1 118 ? -3.93658  -17.58045 -5.41943  1.000 35.57913  ? 1037 LYS B N   1 
ATOM   2360 C  CA  . LYS B 1 118 ? -5.12398  -17.84951 -6.23536  1.000 47.00195  ? 1037 LYS B CA  1 
ATOM   2361 C  C   . LYS B 1 118 ? -4.88262  -18.96347 -7.25376  1.000 42.94638  ? 1037 LYS B C   1 
ATOM   2362 O  O   . LYS B 1 118 ? -5.82696  -19.65976 -7.64776  1.000 44.73624  ? 1037 LYS B O   1 
ATOM   2363 C  CB  . LYS B 1 118 ? -5.55829  -16.55588 -6.94112  1.000 50.49078  ? 1037 LYS B CB  1 
ATOM   2364 C  CG  . LYS B 1 118 ? -6.98094  -16.54825 -7.48984  1.000 60.19191  ? 1037 LYS B CG  1 
ATOM   2365 C  CD  . LYS B 1 118 ? -7.32191  -15.24663 -8.23137  1.000 69.01011  ? 1037 LYS B CD  1 
ATOM   2366 C  CE  . LYS B 1 118 ? -6.49398  -14.04613 -7.75801  1.000 76.30896  ? 1037 LYS B CE  1 
ATOM   2367 N  NZ  . LYS B 1 118 ? -6.92074  -13.44301 -6.45482  1.000 77.38519  ? 1037 LYS B NZ  1 
ATOM   2368 N  N   . GLY B 1 119 ? -3.65031  -19.12765 -7.70761  1.000 38.10639  ? 1038 GLY B N   1 
ATOM   2369 C  CA  . GLY B 1 119 ? -3.34540  -20.11949 -8.72418  1.000 41.35312  ? 1038 GLY B CA  1 
ATOM   2370 C  C   . GLY B 1 119 ? -3.16188  -21.53732 -8.22036  1.000 41.25084  ? 1038 GLY B C   1 
ATOM   2371 O  O   . GLY B 1 119 ? -3.00309  -22.45412 -9.03704  1.000 40.55300  ? 1038 GLY B O   1 
ATOM   2372 N  N   . ASN B 1 120 ? -3.18482  -21.74030 -6.90200  1.000 39.28921  ? 1039 ASN B N   1 
ATOM   2373 C  CA  . ASN B 1 120 ? -3.03085  -23.06551 -6.29958  1.000 41.80096  ? 1039 ASN B CA  1 
ATOM   2374 C  C   . ASN B 1 120 ? -1.79245  -23.77352 -6.83823  1.000 42.97312  ? 1039 ASN B C   1 
ATOM   2375 O  O   . ASN B 1 120 ? -1.82772  -24.93311 -7.25673  1.000 43.54956  ? 1039 ASN B O   1 
ATOM   2376 C  CB  . ASN B 1 120 ? -4.28634  -23.91202 -6.48518  1.000 42.23981  ? 1039 ASN B CB  1 
ATOM   2377 C  CG  . ASN B 1 120 ? -5.49432  -23.26469 -5.86294  1.000 52.80547  ? 1039 ASN B CG  1 
ATOM   2378 O  OD1 . ASN B 1 120 ? -5.41579  -22.76524 -4.74637  1.000 56.14194  ? 1039 ASN B OD1 1 
ATOM   2379 N  ND2 . ASN B 1 120 ? -6.62356  -23.28005 -6.56758  1.000 62.89813  ? 1039 ASN B ND2 1 
ATOM   2380 N  N   . TYR B 1 121 ? -0.69027  -23.03280 -6.84529  1.000 38.45283  ? 1040 TYR B N   1 
ATOM   2381 C  CA  . TYR B 1 121 ? 0.59774   -23.56979 -7.25375  1.000 33.90745  ? 1040 TYR B CA  1 
ATOM   2382 C  C   . TYR B 1 121 ? 1.21859   -24.47364 -6.20350  1.000 38.66810  ? 1040 TYR B C   1 
ATOM   2383 O  O   . TYR B 1 121 ? 2.07886   -25.29030 -6.54403  1.000 36.88716  ? 1040 TYR B O   1 
ATOM   2384 C  CB  . TYR B 1 121 ? 1.53805   -22.42044 -7.60720  1.000 34.15913  ? 1040 TYR B CB  1 
ATOM   2385 C  CG  . TYR B 1 121 ? 1.06228   -21.62808 -8.79085  1.000 33.27374  ? 1040 TYR B CG  1 
ATOM   2386 C  CD1 . TYR B 1 121 ? 1.10690   -22.17823 -10.07162 1.000 33.18267  ? 1040 TYR B CD1 1 
ATOM   2387 C  CD2 . TYR B 1 121 ? 0.57024   -20.33751 -8.65033  1.000 34.57309  ? 1040 TYR B CD2 1 
ATOM   2388 C  CE1 . TYR B 1 121 ? 0.68080   -21.45879 -11.17185 1.000 36.19241  ? 1040 TYR B CE1 1 
ATOM   2389 C  CE2 . TYR B 1 121 ? 0.12572   -19.61692 -9.75091  1.000 30.90372  ? 1040 TYR B CE2 1 
ATOM   2390 C  CZ  . TYR B 1 121 ? 0.18764   -20.18634 -11.01164 1.000 37.57538  ? 1040 TYR B CZ  1 
ATOM   2391 O  OH  . TYR B 1 121 ? -0.22773  -19.48950 -12.11829 1.000 38.08863  ? 1040 TYR B OH  1 
ATOM   2392 N  N   . ALA B 1 122 ? 0.81895   -24.34750 -4.94011  1.000 39.90453  ? 1041 ALA B N   1 
ATOM   2393 C  CA  . ALA B 1 122 ? 1.30513   -25.23113 -3.89253  1.000 34.98389  ? 1041 ALA B CA  1 
ATOM   2394 C  C   . ALA B 1 122 ? 0.38785   -25.03481 -2.69894  1.000 39.23558  ? 1041 ALA B C   1 
ATOM   2395 O  O   . ALA B 1 122 ? -0.45014  -24.13163 -2.68837  1.000 39.20792  ? 1041 ALA B O   1 
ATOM   2396 C  CB  . ALA B 1 122 ? 2.76426   -24.94090 -3.51764  1.000 38.16620  ? 1041 ALA B CB  1 
ATOM   2397 N  N   . GLU B 1 123 ? 0.55712   -25.89497 -1.69483  1.000 40.82110  ? 1042 GLU B N   1 
ATOM   2398 C  CA  . GLU B 1 123 ? -0.22649  -25.77372 -0.46886  1.000 43.48862  ? 1042 GLU B CA  1 
ATOM   2399 C  C   . GLU B 1 123 ? 0.04957   -24.44349 0.22344   1.000 43.83822  ? 1042 GLU B C   1 
ATOM   2400 O  O   . GLU B 1 123 ? -0.86786  -23.81808 0.76749   1.000 43.79165  ? 1042 GLU B O   1 
ATOM   2401 C  CB  . GLU B 1 123 ? 0.08777   -26.95385 0.44212   1.000 44.17509  ? 1042 GLU B CB  1 
ATOM   2402 C  CG  . GLU B 1 123 ? -0.68031  -28.19872 0.06996   1.000 44.19057  ? 1042 GLU B CG  1 
ATOM   2403 C  CD  . GLU B 1 123 ? -0.38652  -29.34762 1.00534   1.000 62.37920  ? 1042 GLU B CD  1 
ATOM   2404 O  OE1 . GLU B 1 123 ? -0.33488  -30.49304 0.54710   1.000 63.79748  ? 1042 GLU B OE1 1 
ATOM   2405 O  OE2 . GLU B 1 123 ? -0.13872  -29.12696 2.19291   1.000 65.81151  ? 1042 GLU B OE2 1 
ATOM   2406 N  N   . ARG B 1 124 ? 1.30921   -24.00138 0.22943   1.000 39.13352  ? 1043 ARG B N   1 
ATOM   2407 C  CA  . ARG B 1 124 ? 1.68963   -22.75700 0.88812   1.000 39.77473  ? 1043 ARG B CA  1 
ATOM   2408 C  C   . ARG B 1 124 ? 2.62985   -21.94813 0.01101   1.000 37.28253  ? 1043 ARG B C   1 
ATOM   2409 O  O   . ARG B 1 124 ? 3.33167   -22.47583 -0.85614  1.000 35.94282  ? 1043 ARG B O   1 
ATOM   2410 C  CB  . ARG B 1 124 ? 2.36294   -22.97722 2.25605   1.000 37.24431  ? 1043 ARG B CB  1 
ATOM   2411 C  CG  . ARG B 1 124 ? 1.44784   -23.55146 3.32348   1.000 57.45046  ? 1043 ARG B CG  1 
ATOM   2412 C  CD  . ARG B 1 124 ? 2.25623   -24.07613 4.48910   1.000 65.53303  ? 1043 ARG B CD  1 
ATOM   2413 N  NE  . ARG B 1 124 ? 3.21087   -25.06697 4.01553   1.000 68.41337  ? 1043 ARG B NE  1 
ATOM   2414 C  CZ  . ARG B 1 124 ? 2.91806   -26.34035 3.79194   1.000 73.06339  ? 1043 ARG B CZ  1 
ATOM   2415 N  NH1 . ARG B 1 124 ? 1.72217   -26.83727 4.07515   1.000 73.89770  ? 1043 ARG B NH1 1 
ATOM   2416 N  NH2 . ARG B 1 124 ? 3.84813   -27.13613 3.27311   1.000 70.02597  ? 1043 ARG B NH2 1 
ATOM   2417 N  N   . VAL B 1 125 ? 2.63983   -20.64394 0.25879   1.000 33.86838  ? 1044 VAL B N   1 
ATOM   2418 C  CA  . VAL B 1 125 ? 3.53137   -19.71262 -0.42646  1.000 33.04591  ? 1044 VAL B CA  1 
ATOM   2419 C  C   . VAL B 1 125 ? 4.39554   -19.06597 0.64070   1.000 37.67780  ? 1044 VAL B C   1 
ATOM   2420 O  O   . VAL B 1 125 ? 3.86866   -18.45667 1.57854   1.000 40.25933  ? 1044 VAL B O   1 
ATOM   2421 C  CB  . VAL B 1 125 ? 2.75627   -18.65230 -1.22317  1.000 35.41970  ? 1044 VAL B CB  1 
ATOM   2422 C  CG1 . VAL B 1 125 ? 3.71596   -17.64509 -1.83422  1.000 34.71096  ? 1044 VAL B CG1 1 
ATOM   2423 C  CG2 . VAL B 1 125 ? 1.91438   -19.31909 -2.30399  1.000 41.97111  ? 1044 VAL B CG2 1 
ATOM   2424 N  N   . GLY B 1 126 ? 5.71425   -19.22308 0.51565   1.000 31.67325  ? 1045 GLY B N   1 
ATOM   2425 C  CA  . GLY B 1 126 ? 6.62411   -18.64062 1.48282   1.000 36.17678  ? 1045 GLY B CA  1 
ATOM   2426 C  C   . GLY B 1 126 ? 6.67355   -17.12835 1.38133   1.000 33.78283  ? 1045 GLY B C   1 
ATOM   2427 O  O   . GLY B 1 126 ? 6.31485   -16.53773 0.36921   1.000 37.08645  ? 1045 GLY B O   1 
ATOM   2428 N  N   . ALA B 1 127 ? 7.11160   -16.49020 2.47729   1.000 35.48199  ? 1046 ALA B N   1 
ATOM   2429 C  CA  . ALA B 1 127 ? 7.06216   -15.03114 2.55157   1.000 39.88893  ? 1046 ALA B CA  1 
ATOM   2430 C  C   . ALA B 1 127 ? 8.01860   -14.36125 1.57566   1.000 38.29111  ? 1046 ALA B C   1 
ATOM   2431 O  O   . ALA B 1 127 ? 7.77073   -13.22280 1.15919   1.000 38.99086  ? 1046 ALA B O   1 
ATOM   2432 C  CB  . ALA B 1 127 ? 7.36895   -14.56132 3.97339   1.000 44.62556  ? 1046 ALA B CB  1 
ATOM   2433 N  N   . GLY B 1 128 ? 9.11403   -15.03118 1.20110   1.000 33.58440  ? 1047 GLY B N   1 
ATOM   2434 C  CA  . GLY B 1 128 ? 10.04898  -14.43874 0.25334   1.000 33.45396  ? 1047 GLY B CA  1 
ATOM   2435 C  C   . GLY B 1 128 ? 9.64218   -14.55379 -1.20075  1.000 32.51752  ? 1047 GLY B C   1 
ATOM   2436 O  O   . GLY B 1 128 ? 10.05238  -13.73531 -2.03368  1.000 30.62843  ? 1047 GLY B O   1 
ATOM   2437 N  N   . ALA B 1 129 ? 8.83742   -15.55426 -1.53621  1.000 27.85924  ? 1048 ALA B N   1 
ATOM   2438 C  CA  . ALA B 1 129 ? 8.54300   -15.80613 -2.94587  1.000 26.13954  ? 1048 ALA B CA  1 
ATOM   2439 C  C   . ALA B 1 129 ? 7.83863   -14.64595 -3.63635  1.000 27.63373  ? 1048 ALA B C   1 
ATOM   2440 O  O   . ALA B 1 129 ? 8.22991   -14.31088 -4.76656  1.000 27.55602  ? 1048 ALA B O   1 
ATOM   2441 C  CB  . ALA B 1 129 ? 7.72478   -17.09265 -3.08032  1.000 26.90448  ? 1048 ALA B CB  1 
ATOM   2442 N  N   . PRO B 1 130 ? 6.77465   -14.04066 -3.08840  1.000 27.12835  ? 1049 PRO B N   1 
ATOM   2443 C  CA  . PRO B 1 130 ? 6.15940   -12.92757 -3.83743  1.000 24.63195  ? 1049 PRO B CA  1 
ATOM   2444 C  C   . PRO B 1 130 ? 7.05654   -11.70564 -3.92044  1.000 24.64908  ? 1049 PRO B C   1 
ATOM   2445 O  O   . PRO B 1 130 ? 6.93780   -10.93881 -4.88488  1.000 25.42631  ? 1049 PRO B O   1 
ATOM   2446 C  CB  . PRO B 1 130 ? 4.86022   -12.64454 -3.06979  1.000 28.19530  ? 1049 PRO B CB  1 
ATOM   2447 C  CG  . PRO B 1 130 ? 5.08771   -13.16325 -1.71873  1.000 34.99439  ? 1049 PRO B CG  1 
ATOM   2448 C  CD  . PRO B 1 130 ? 5.98773   -14.37429 -1.88825  1.000 30.89663  ? 1049 PRO B CD  1 
ATOM   2449 N  N   . VAL B 1 131 ? 7.92314   -11.47682 -2.92213  1.000 27.10618  ? 1050 VAL B N   1 
ATOM   2450 C  CA  . VAL B 1 131 ? 8.86584   -10.35901 -2.99993  1.000 26.60579  ? 1050 VAL B CA  1 
ATOM   2451 C  C   . VAL B 1 131 ? 9.83290   -10.56258 -4.15695  1.000 27.46536  ? 1050 VAL B C   1 
ATOM   2452 O  O   . VAL B 1 131 ? 10.05376  -9.66417  -4.98055  1.000 27.24445  ? 1050 VAL B O   1 
ATOM   2453 C  CB  . VAL B 1 131 ? 9.62418   -10.20161 -1.67107  1.000 29.85481  ? 1050 VAL B CB  1 
ATOM   2454 C  CG1 . VAL B 1 131 ? 10.60972  -9.07896  -1.78367  1.000 36.79657  ? 1050 VAL B CG1 1 
ATOM   2455 C  CG2 . VAL B 1 131 ? 8.64833   -9.95359  -0.55769  1.000 33.01537  ? 1050 VAL B CG2 1 
ATOM   2456 N  N   . TYR B 1 132 ? 10.42900  -11.75492 -4.23322  1.000 25.60844  ? 1051 TYR B N   1 
ATOM   2457 C  CA  . TYR B 1 132 ? 11.35988  -12.06244 -5.31663  1.000 25.71005  ? 1051 TYR B CA  1 
ATOM   2458 C  C   . TYR B 1 132 ? 10.67249  -11.93416 -6.66520  1.000 26.07061  ? 1051 TYR B C   1 
ATOM   2459 O  O   . TYR B 1 132 ? 11.20084  -11.30770 -7.59479  1.000 26.31190  ? 1051 TYR B O   1 
ATOM   2460 C  CB  . TYR B 1 132 ? 11.90038  -13.48116 -5.11440  1.000 27.29164  ? 1051 TYR B CB  1 
ATOM   2461 C  CG  . TYR B 1 132 ? 13.15156  -13.85328 -5.86835  1.000 26.63885  ? 1051 TYR B CG  1 
ATOM   2462 C  CD1 . TYR B 1 132 ? 13.14220  -13.97331 -7.25773  1.000 25.93472  ? 1051 TYR B CD1 1 
ATOM   2463 C  CD2 . TYR B 1 132 ? 14.32208  -14.16356 -5.18508  1.000 27.47797  ? 1051 TYR B CD2 1 
ATOM   2464 C  CE1 . TYR B 1 132 ? 14.29397  -14.35143 -7.94563  1.000 27.28063  ? 1051 TYR B CE1 1 
ATOM   2465 C  CE2 . TYR B 1 132 ? 15.47046  -14.54780 -5.86219  1.000 31.74549  ? 1051 TYR B CE2 1 
ATOM   2466 C  CZ  . TYR B 1 132 ? 15.44829  -14.63481 -7.23913  1.000 27.42048  ? 1051 TYR B CZ  1 
ATOM   2467 O  OH  . TYR B 1 132 ? 16.59833  -15.00918 -7.89966  1.000 29.44125  ? 1051 TYR B OH  1 
ATOM   2468 N  N   . LEU B 1 133 ? 9.47820   -12.51245 -6.78851  1.000 25.52536  ? 1052 LEU B N   1 
ATOM   2469 C  CA  . LEU B 1 133 ? 8.79174   -12.49381 -8.07596  1.000 24.11557  ? 1052 LEU B CA  1 
ATOM   2470 C  C   . LEU B 1 133 ? 8.36292   -11.07425 -8.45163  1.000 25.58709  ? 1052 LEU B C   1 
ATOM   2471 O  O   . LEU B 1 133 ? 8.48148   -10.67589 -9.61384  1.000 24.78737  ? 1052 LEU B O   1 
ATOM   2472 C  CB  . LEU B 1 133 ? 7.60590   -13.45629 -8.04767  1.000 23.52889  ? 1052 LEU B CB  1 
ATOM   2473 C  CG  . LEU B 1 133 ? 6.77369   -13.58117 -9.32762  1.000 22.31606  ? 1052 LEU B CG  1 
ATOM   2474 C  CD1 . LEU B 1 133 ? 7.66466   -13.87477 -10.53673 1.000 24.05600  ? 1052 LEU B CD1 1 
ATOM   2475 C  CD2 . LEU B 1 133 ? 5.71926   -14.67983 -9.13587  1.000 25.85025  ? 1052 LEU B CD2 1 
ATOM   2476 N  N   . ALA B 1 134 ? 7.88732   -10.28532 -7.48518  1.000 24.63386  ? 1053 ALA B N   1 
ATOM   2477 C  CA  . ALA B 1 134 ? 7.54167   -8.89681  -7.79959  1.000 23.73955  ? 1053 ALA B CA  1 
ATOM   2478 C  C   . ALA B 1 134 ? 8.75681   -8.13320  -8.32947  1.000 28.29296  ? 1053 ALA B C   1 
ATOM   2479 O  O   . ALA B 1 134 ? 8.63822   -7.34464  -9.27392  1.000 26.86034  ? 1053 ALA B O   1 
ATOM   2480 C  CB  . ALA B 1 134 ? 6.96239   -8.20295  -6.56265  1.000 28.06251  ? 1053 ALA B CB  1 
ATOM   2481 N  N   . ALA B 1 135 ? 9.93078   -8.35711  -7.73661  1.000 26.31204  ? 1054 ALA B N   1 
ATOM   2482 C  CA  . ALA B 1 135 ? 11.13694  -7.66567  -8.20051  1.000 26.23030  ? 1054 ALA B CA  1 
ATOM   2483 C  C   . ALA B 1 135 ? 11.50801  -8.08777  -9.61519  1.000 24.99886  ? 1054 ALA B C   1 
ATOM   2484 O  O   . ALA B 1 135 ? 12.03038  -7.27425  -10.39248 1.000 26.86633  ? 1054 ALA B O   1 
ATOM   2485 C  CB  . ALA B 1 135 ? 12.31646  -7.93198  -7.26011  1.000 27.97105  ? 1054 ALA B CB  1 
ATOM   2486 N  N   . VAL B 1 136 ? 11.33314  -9.37340  -9.93079  1.000 24.73041  ? 1055 VAL B N   1 
ATOM   2487 C  CA  . VAL B 1 136 ? 11.62914  -9.87657  -11.27291 1.000 24.20018  ? 1055 VAL B CA  1 
ATOM   2488 C  C   . VAL B 1 136 ? 10.67833  -9.26234  -12.28867 1.000 23.69300  ? 1055 VAL B C   1 
ATOM   2489 O  O   . VAL B 1 136 ? 11.10423  -8.80302  -13.35898 1.000 24.95548  ? 1055 VAL B O   1 
ATOM   2490 C  CB  . VAL B 1 136 ? 11.56464  -11.41703 -11.29915 1.000 22.26585  ? 1055 VAL B CB  1 
ATOM   2491 C  CG1 . VAL B 1 136 ? 11.67173  -11.96202 -12.75431 1.000 22.16462  ? 1055 VAL B CG1 1 
ATOM   2492 C  CG2 . VAL B 1 136 ? 12.73667  -11.98839 -10.50115 1.000 24.35509  ? 1055 VAL B CG2 1 
ATOM   2493 N  N   . LEU B 1 137 ? 9.38632   -9.23331  -11.96662 1.000 22.66489  ? 1056 LEU B N   1 
ATOM   2494 C  CA  . LEU B 1 137 ? 8.41736   -8.64198  -12.88788 1.000 24.16084  ? 1056 LEU B CA  1 
ATOM   2495 C  C   . LEU B 1 137 ? 8.69773   -7.16414  -13.08135 1.000 27.03438  ? 1056 LEU B C   1 
ATOM   2496 O  O   . LEU B 1 137 ? 8.57557   -6.64525  -14.19647 1.000 26.82298  ? 1056 LEU B O   1 
ATOM   2497 C  CB  . LEU B 1 137 ? 6.99595   -8.85860  -12.38829 1.000 26.29855  ? 1056 LEU B CB  1 
ATOM   2498 C  CG  . LEU B 1 137 ? 6.57325   -10.32643 -12.28955 1.000 24.12027  ? 1056 LEU B CG  1 
ATOM   2499 C  CD1 . LEU B 1 137 ? 5.19076   -10.38777 -11.66393 1.000 29.33536  ? 1056 LEU B CD1 1 
ATOM   2500 C  CD2 . LEU B 1 137 ? 6.58018   -10.98294 -13.67205 1.000 25.85513  ? 1056 LEU B CD2 1 
ATOM   2501 N  N   . GLU B 1 138 ? 9.08555   -6.46682  -12.00490 1.000 26.61182  ? 1057 GLU B N   1 
ATOM   2502 C  CA  . GLU B 1 138 ? 9.40889   -5.05511  -12.14487 1.000 31.47347  ? 1057 GLU B CA  1 
ATOM   2503 C  C   . GLU B 1 138 ? 10.64263  -4.83902  -13.01002 1.000 29.80941  ? 1057 GLU B C   1 
ATOM   2504 O  O   . GLU B 1 138 ? 10.69228  -3.89341  -13.80613 1.000 28.26386  ? 1057 GLU B O   1 
ATOM   2505 C  CB  . GLU B 1 138 ? 9.60043   -4.42438  -10.77283 1.000 25.48297  ? 1057 GLU B CB  1 
ATOM   2506 C  CG  . GLU B 1 138 ? 10.10156  -3.00569  -10.88905 1.000 30.97062  ? 1057 GLU B CG  1 
ATOM   2507 C  CD  . GLU B 1 138 ? 9.88555   -2.22464  -9.64204  1.000 40.56747  ? 1057 GLU B CD  1 
ATOM   2508 O  OE1 . GLU B 1 138 ? 9.02332   -2.64544  -8.85239  1.000 43.19837  ? 1057 GLU B OE1 1 
ATOM   2509 O  OE2 . GLU B 1 138 ? 10.54512  -1.17689  -9.46443  1.000 40.35185  ? 1057 GLU B OE2 1 
ATOM   2510 N  N   . TYR B 1 139 ? 11.66646  -5.67918  -12.83994 1.000 26.23236  ? 1058 TYR B N   1 
ATOM   2511 C  CA  . TYR B 1 139 ? 12.87511  -5.52788  -13.63827 1.000 25.59567  ? 1058 TYR B CA  1 
ATOM   2512 C  C   . TYR B 1 139 ? 12.56585  -5.68265  -15.11895 1.000 25.71714  ? 1058 TYR B C   1 
ATOM   2513 O  O   . TYR B 1 139 ? 13.02031  -4.87972  -15.94923 1.000 27.43311  ? 1058 TYR B O   1 
ATOM   2514 C  CB  . TYR B 1 139 ? 13.91860  -6.56149  -13.19804 1.000 24.88143  ? 1058 TYR B CB  1 
ATOM   2515 C  CG  . TYR B 1 139 ? 14.97738  -6.80557  -14.26135 1.000 24.79805  ? 1058 TYR B CG  1 
ATOM   2516 C  CD1 . TYR B 1 139 ? 15.91376  -5.82477  -14.55210 1.000 28.53678  ? 1058 TYR B CD1 1 
ATOM   2517 C  CD2 . TYR B 1 139 ? 15.01167  -8.00419  -14.99198 1.000 26.22057  ? 1058 TYR B CD2 1 
ATOM   2518 C  CE1 . TYR B 1 139 ? 16.87533  -6.00974  -15.53938 1.000 31.09032  ? 1058 TYR B CE1 1 
ATOM   2519 C  CE2 . TYR B 1 139 ? 15.98430  -8.20945  -15.98765 1.000 28.66170  ? 1058 TYR B CE2 1 
ATOM   2520 C  CZ  . TYR B 1 139 ? 16.90386  -7.19958  -16.24712 1.000 28.53405  ? 1058 TYR B CZ  1 
ATOM   2521 O  OH  . TYR B 1 139 ? 17.87728  -7.35222  -17.22690 1.000 31.35584  ? 1058 TYR B OH  1 
ATOM   2522 N  N   . LEU B 1 140 ? 11.77034  -6.69718  -15.46450 1.000 23.70322  ? 1059 LEU B N   1 
ATOM   2523 C  CA  . LEU B 1 140 ? 11.43653  -6.91953  -16.86691 1.000 25.25751  ? 1059 LEU B CA  1 
ATOM   2524 C  C   . LEU B 1 140 ? 10.57591  -5.79377  -17.40496 1.000 28.10972  ? 1059 LEU B C   1 
ATOM   2525 O  O   . LEU B 1 140 ? 10.77073  -5.34273  -18.54557 1.000 27.90538  ? 1059 LEU B O   1 
ATOM   2526 C  CB  . LEU B 1 140 ? 10.72532  -8.26822  -17.03054 1.000 27.64606  ? 1059 LEU B CB  1 
ATOM   2527 C  CG  . LEU B 1 140 ? 11.61433  -9.49431  -16.76984 1.000 25.10456  ? 1059 LEU B CG  1 
ATOM   2528 C  CD1 . LEU B 1 140 ? 10.74388  -10.72584 -16.77310 1.000 24.86871  ? 1059 LEU B CD1 1 
ATOM   2529 C  CD2 . LEU B 1 140 ? 12.68996  -9.62117  -17.84865 1.000 27.59470  ? 1059 LEU B CD2 1 
ATOM   2530 N  N   . THR B 1 141 ? 9.62257   -5.33132  -16.59638 1.000 25.43453  ? 1060 THR B N   1 
ATOM   2531 C  CA  . THR B 1 141 ? 8.75588   -4.22831  -17.00927 1.000 26.29434  ? 1060 THR B CA  1 
ATOM   2532 C  C   . THR B 1 141 ? 9.57385   -2.97922  -17.28215 1.000 28.83286  ? 1060 THR B C   1 
ATOM   2533 O  O   . THR B 1 141 ? 9.37736   -2.30214  -18.29756 1.000 27.60801  ? 1060 THR B O   1 
ATOM   2534 C  CB  . THR B 1 141 ? 7.71523   -3.97641  -15.92245 1.000 28.03345  ? 1060 THR B CB  1 
ATOM   2535 O  OG1 . THR B 1 141 ? 6.88591   -5.13792  -15.81213 1.000 28.70031  ? 1060 THR B OG1 1 
ATOM   2536 C  CG2 . THR B 1 141 ? 6.84043   -2.75460  -16.23769 1.000 29.92645  ? 1060 THR B CG2 1 
ATOM   2537 N  N   . ALA B 1 142 ? 10.51260  -2.66551  -16.38389 1.000 27.57052  ? 1061 ALA B N   1 
ATOM   2538 C  CA  . ALA B 1 142 ? 11.35627  -1.49565  -16.57790 1.000 28.87358  ? 1061 ALA B CA  1 
ATOM   2539 C  C   . ALA B 1 142 ? 12.18889  -1.62723  -17.84329 1.000 29.46588  ? 1061 ALA B C   1 
ATOM   2540 O  O   . ALA B 1 142 ? 12.37257  -0.65327  -18.57361 1.000 33.11285  ? 1061 ALA B O   1 
ATOM   2541 C  CB  . ALA B 1 142 ? 12.26274  -1.29162  -15.35908 1.000 29.68679  ? 1061 ALA B CB  1 
ATOM   2542 N  N   . GLU B 1 143 ? 12.70289  -2.82762  -18.11587 1.000 28.25144  ? 1062 GLU B N   1 
ATOM   2543 C  CA  . GLU B 1 143 ? 13.54026  -3.03271  -19.29413 1.000 28.58579  ? 1062 GLU B CA  1 
ATOM   2544 C  C   . GLU B 1 143 ? 12.74358  -2.82847  -20.57920 1.000 31.44562  ? 1062 GLU B C   1 
ATOM   2545 O  O   . GLU B 1 143 ? 13.18096  -2.12670  -21.50189 1.000 31.55207  ? 1062 GLU B O   1 
ATOM   2546 C  CB  . GLU B 1 143 ? 14.14663  -4.43256  -19.24400 1.000 33.07329  ? 1062 GLU B CB  1 
ATOM   2547 C  CG  . GLU B 1 143 ? 15.26449  -4.63834  -20.21987 1.000 35.50258  ? 1062 GLU B CG  1 
ATOM   2548 C  CD  . GLU B 1 143 ? 16.56694  -3.95875  -19.80408 1.000 36.45669  ? 1062 GLU B CD  1 
ATOM   2549 O  OE1 . GLU B 1 143 ? 16.68393  -3.42791  -18.66826 1.000 37.11784  ? 1062 GLU B OE1 1 
ATOM   2550 O  OE2 . GLU B 1 143 ? 17.49285  -3.96854  -20.62792 1.000 35.43211  ? 1062 GLU B OE2 1 
ATOM   2551 N  N   . ILE B 1 144 ? 11.56604  -3.43398  -20.64836 1.000 29.28512  ? 1063 ILE B N   1 
ATOM   2552 C  CA  . ILE B 1 144 ? 10.72617  -3.30492  -21.83668 1.000 27.67954  ? 1063 ILE B CA  1 
ATOM   2553 C  C   . ILE B 1 144 ? 10.32665  -1.84956  -22.03851 1.000 29.15913  ? 1063 ILE B C   1 
ATOM   2554 O  O   . ILE B 1 144 ? 10.40241  -1.31358  -23.15562 1.000 30.96723  ? 1063 ILE B O   1 
ATOM   2555 C  CB  . ILE B 1 144 ? 9.49278   -4.21481  -21.69024 1.000 28.75328  ? 1063 ILE B CB  1 
ATOM   2556 C  CG1 . ILE B 1 144 ? 9.93113   -5.67702  -21.61667 1.000 29.39018  ? 1063 ILE B CG1 1 
ATOM   2557 C  CG2 . ILE B 1 144 ? 8.52682   -3.98720  -22.84696 1.000 29.10818  ? 1063 ILE B CG2 1 
ATOM   2558 C  CD1 . ILE B 1 144 ? 8.87354   -6.58112  -20.99385 1.000 29.91694  ? 1063 ILE B CD1 1 
ATOM   2559 N  N   . LEU B 1 145 ? 9.90993   -1.17800  -20.95710 1.000 26.92357  ? 1064 LEU B N   1 
ATOM   2560 C  CA  . LEU B 1 145 ? 9.44731   0.20457   -21.08400 1.000 29.29030  ? 1064 LEU B CA  1 
ATOM   2561 C  C   . LEU B 1 145 ? 10.58810  1.14224   -21.43846 1.000 30.97704  ? 1064 LEU B C   1 
ATOM   2562 O  O   . LEU B 1 145 ? 10.39883  2.10083   -22.19929 1.000 31.40397  ? 1064 LEU B O   1 
ATOM   2563 C  CB  . LEU B 1 145 ? 8.77389   0.65371   -19.78695 1.000 29.71422  ? 1064 LEU B CB  1 
ATOM   2564 C  CG  . LEU B 1 145 ? 7.42820   -0.00068  -19.46786 1.000 31.96996  ? 1064 LEU B CG  1 
ATOM   2565 C  CD1 . LEU B 1 145 ? 6.96857   0.44597   -18.07015 1.000 29.62031  ? 1064 LEU B CD1 1 
ATOM   2566 C  CD2 . LEU B 1 145 ? 6.37401   0.40921   -20.48619 1.000 30.57313  ? 1064 LEU B CD2 1 
ATOM   2567 N  N   . GLU B 1 146 ? 11.78263  0.89161   -20.89632 1.000 28.05289  ? 1065 GLU B N   1 
ATOM   2568 C  CA  . GLU B 1 146 ? 12.93359  1.70410   -21.28213 1.000 32.60902  ? 1065 GLU B CA  1 
ATOM   2569 C  C   . GLU B 1 146 ? 13.16100  1.63290   -22.78669 1.000 35.81456  ? 1065 GLU B C   1 
ATOM   2570 O  O   . GLU B 1 146 ? 13.29005  2.66276   -23.46448 1.000 34.55300  ? 1065 GLU B O   1 
ATOM   2571 C  CB  . GLU B 1 146 ? 14.18202  1.22465   -20.54307 1.000 36.98634  ? 1065 GLU B CB  1 
ATOM   2572 C  CG  . GLU B 1 146 ? 15.44432  1.95919   -20.94626 1.000 42.58027  ? 1065 GLU B CG  1 
ATOM   2573 C  CD  . GLU B 1 146 ? 16.67059  1.48193   -20.17215 1.000 60.03868  ? 1065 GLU B CD  1 
ATOM   2574 O  OE1 . GLU B 1 146 ? 16.53213  0.57710   -19.31700 1.000 52.22581  ? 1065 GLU B OE1 1 
ATOM   2575 O  OE2 . GLU B 1 146 ? 17.77510  2.01032   -20.41904 1.000 63.64435  ? 1065 GLU B OE2 1 
ATOM   2576 N  N   . LEU B 1 147 ? 13.22334  0.41378   -23.32269 1.000 32.74955  ? 1066 LEU B N   1 
ATOM   2577 C  CA  . LEU B 1 147 ? 13.47819  0.23869   -24.74772 1.000 33.83850  ? 1066 LEU B CA  1 
ATOM   2578 C  C   . LEU B 1 147 ? 12.31219  0.74255   -25.58379 1.000 35.87793  ? 1066 LEU B C   1 
ATOM   2579 O  O   . LEU B 1 147 ? 12.52298  1.35431   -26.63522 1.000 34.91366  ? 1066 LEU B O   1 
ATOM   2580 C  CB  . LEU B 1 147 ? 13.75841  -1.23657  -25.05184 1.000 35.93452  ? 1066 LEU B CB  1 
ATOM   2581 C  CG  . LEU B 1 147 ? 15.03078  -1.80327  -24.40312 1.000 37.93963  ? 1066 LEU B CG  1 
ATOM   2582 C  CD1 . LEU B 1 147 ? 15.05928  -3.32289  -24.53293 1.000 37.42723  ? 1066 LEU B CD1 1 
ATOM   2583 C  CD2 . LEU B 1 147 ? 16.24916  -1.19767  -25.04403 1.000 41.24184  ? 1066 LEU B CD2 1 
ATOM   2584 N  N   . ALA B 1 148 ? 11.07877  0.48355   -25.14916 1.000 32.96944  ? 1067 ALA B N   1 
ATOM   2585 C  CA  . ALA B 1 148 ? 9.92893   0.94678   -25.92815 1.000 35.79387  ? 1067 ALA B CA  1 
ATOM   2586 C  C   . ALA B 1 148 ? 9.85909   2.46710   -25.96590 1.000 33.95713  ? 1067 ALA B C   1 
ATOM   2587 O  O   . ALA B 1 148 ? 9.50381   3.05602   -26.99770 1.000 33.84586  ? 1067 ALA B O   1 
ATOM   2588 C  CB  . ALA B 1 148 ? 8.63916   0.35613   -25.36637 1.000 31.49215  ? 1067 ALA B CB  1 
ATOM   2589 N  N   . GLY B 1 149 ? 10.16262  3.12275   -24.84306 1.000 33.78130  ? 1068 GLY B N   1 
ATOM   2590 C  CA  . GLY B 1 149 ? 10.16009  4.57576   -24.81328 1.000 32.67751  ? 1068 GLY B CA  1 
ATOM   2591 C  C   . GLY B 1 149 ? 11.23966  5.17426   -25.69314 1.000 38.25005  ? 1068 GLY B C   1 
ATOM   2592 O  O   . GLY B 1 149 ? 11.05293  6.24805   -26.27795 1.000 37.74889  ? 1068 GLY B O   1 
ATOM   2593 N  N   . ASN B 1 150 ? 12.39753  4.50642   -25.76744 1.000 36.71201  ? 1069 ASN B N   1 
ATOM   2594 C  CA  . ASN B 1 150 ? 13.42453  4.90891   -26.72518 1.000 37.98597  ? 1069 ASN B CA  1 
ATOM   2595 C  C   . ASN B 1 150 ? 12.91679  4.78112   -28.15375 1.000 35.15280  ? 1069 ASN B C   1 
ATOM   2596 O  O   . ASN B 1 150 ? 13.16140  5.65547   -28.98793 1.000 43.94394  ? 1069 ASN B O   1 
ATOM   2597 C  CB  . ASN B 1 150 ? 14.67809  4.04620   -26.56140 1.000 41.36775  ? 1069 ASN B CB  1 
ATOM   2598 C  CG  . ASN B 1 150 ? 15.36676  4.24220   -25.23095 1.000 41.04072  ? 1069 ASN B CG  1 
ATOM   2599 O  OD1 . ASN B 1 150 ? 15.09239  5.19385   -24.51048 1.000 43.66693  ? 1069 ASN B OD1 1 
ATOM   2600 N  ND2 . ASN B 1 150 ? 16.28291  3.33368   -24.90377 1.000 46.10378  ? 1069 ASN B ND2 1 
ATOM   2601 N  N   . ALA B 1 151 ? 12.22264  3.68339   -28.45968 1.000 37.23746  ? 1070 ALA B N   1 
ATOM   2602 C  CA  . ALA B 1 151 ? 11.67461  3.51756   -29.80058 1.000 39.85803  ? 1070 ALA B CA  1 
ATOM   2603 C  C   . ALA B 1 151 ? 10.63259  4.59010   -30.10315 1.000 38.02750  ? 1070 ALA B C   1 
ATOM   2604 O  O   . ALA B 1 151 ? 10.59233  5.13412   -31.21638 1.000 42.10903  ? 1070 ALA B O   1 
ATOM   2605 C  CB  . ALA B 1 151 ? 11.08390  2.11370   -29.95132 1.000 36.96472  ? 1070 ALA B CB  1 
ATOM   2606 N  N   . ALA B 1 152 ? 9.80525   4.94462   -29.11257 1.000 34.21219  ? 1071 ALA B N   1 
ATOM   2607 C  CA  . ALA B 1 152 ? 8.82524   6.01098   -29.32853 1.000 35.17907  ? 1071 ALA B CA  1 
ATOM   2608 C  C   . ALA B 1 152 ? 9.50988   7.32777   -29.65707 1.000 41.40681  ? 1071 ALA B C   1 
ATOM   2609 O  O   . ALA B 1 152 ? 9.13291   8.01979   -30.61199 1.000 43.82861  ? 1071 ALA B O   1 
ATOM   2610 C  CB  . ALA B 1 152 ? 7.94768   6.17409   -28.08619 1.000 38.46881  ? 1071 ALA B CB  1 
ATOM   2611 N  N   . ARG B 1 153 ? 10.53779  7.67645   -28.88568 1.000 41.09600  ? 1072 ARG B N   1 
ATOM   2612 C  CA  . ARG B 1 153 ? 11.25603  8.92345   -29.11208 1.000 45.97587  ? 1072 ARG B CA  1 
ATOM   2613 C  C   . ARG B 1 153 ? 11.91049  8.94663   -30.48853 1.000 45.10013  ? 1072 ARG B C   1 
ATOM   2614 O  O   . ARG B 1 153 ? 11.87808  9.96999   -31.18542 1.000 48.87053  ? 1072 ARG B O   1 
ATOM   2615 C  CB  . ARG B 1 153 ? 12.28939  9.10990   -28.00211 1.000 47.24082  ? 1072 ARG B CB  1 
ATOM   2616 C  CG  . ARG B 1 153 ? 13.07443  10.41453  -28.07906 1.000 52.21329  ? 1072 ARG B CG  1 
ATOM   2617 C  CD  . ARG B 1 153 ? 14.26019  10.31638  -27.13867 1.000 59.57140  ? 1072 ARG B CD  1 
ATOM   2618 N  NE  . ARG B 1 153 ? 15.08475  9.16057   -27.46931 1.000 59.62738  ? 1072 ARG B NE  1 
ATOM   2619 C  CZ  . ARG B 1 153 ? 15.70020  8.40142   -26.57440 1.000 60.38741  ? 1072 ARG B CZ  1 
ATOM   2620 N  NH1 . ARG B 1 153 ? 15.60190  8.64504   -25.27619 1.000 65.21165  ? 1072 ARG B NH1 1 
ATOM   2621 N  NH2 . ARG B 1 153 ? 16.41727  7.36333   -26.98991 1.000 60.28538  ? 1072 ARG B NH2 1 
ATOM   2622 N  N   . ASP B 1 154 ? 12.50660  7.82855   -30.90195 1.000 46.82260  ? 1073 ASP B N   1 
ATOM   2623 C  CA  . ASP B 1 154 ? 13.12768  7.75817   -32.22356 1.000 51.41578  ? 1073 ASP B CA  1 
ATOM   2624 C  C   . ASP B 1 154 ? 12.09234  7.88029   -33.33617 1.000 48.65135  ? 1073 ASP B C   1 
ATOM   2625 O  O   . ASP B 1 154 ? 12.41374  8.33242   -34.43957 1.000 55.51186  ? 1073 ASP B O   1 
ATOM   2626 C  CB  . ASP B 1 154 ? 13.89300  6.44371   -32.34423 1.000 55.37476  ? 1073 ASP B CB  1 
ATOM   2627 C  CG  . ASP B 1 154 ? 15.18699  6.45977   -31.55399 1.000 59.49858  ? 1073 ASP B CG  1 
ATOM   2628 O  OD1 . ASP B 1 154 ? 15.57331  7.54890   -31.07108 1.000 61.43441  ? 1073 ASP B OD1 1 
ATOM   2629 O  OD2 . ASP B 1 154 ? 15.77636  5.37386   -31.36603 1.000 60.18792  ? 1073 ASP B OD2 1 
ATOM   2630 N  N   . ASN B 1 155 ? 10.85514  7.47860   -33.06082 1.000 52.07310  ? 1074 ASN B N   1 
ATOM   2631 C  CA  . ASN B 1 155 ? 9.72804   7.57645   -33.98186 1.000 47.30645  ? 1074 ASN B CA  1 
ATOM   2632 C  C   . ASN B 1 155 ? 9.04738   8.93264   -33.89853 1.000 47.69797  ? 1074 ASN B C   1 
ATOM   2633 O  O   . ASN B 1 155 ? 8.00014   9.14118   -34.52936 1.000 50.82483  ? 1074 ASN B O   1 
ATOM   2634 C  CB  . ASN B 1 155 ? 8.73858   6.42797   -33.68853 1.000 45.95322  ? 1074 ASN B CB  1 
ATOM   2635 C  CG  . ASN B 1 155 ? 7.68995   6.24384   -34.78183 1.000 56.30848  ? 1074 ASN B CG  1 
ATOM   2636 O  OD1 . ASN B 1 155 ? 6.53762   5.90445   -34.49890 1.000 43.32545  ? 1074 ASN B OD1 1 
ATOM   2637 N  ND2 . ASN B 1 155 ? 8.08115   6.47819   -36.02832 1.000 51.16155  ? 1074 ASN B ND2 1 
ATOM   2638 N  N   . LYS B 1 156 ? 9.65381   9.87247   -33.16946 1.000 48.83782  ? 1075 LYS B N   1 
ATOM   2639 C  CA  . LYS B 1 156 ? 9.13602   11.22534  -32.99088 1.000 46.80249  ? 1075 LYS B CA  1 
ATOM   2640 C  C   . LYS B 1 156 ? 7.74353   11.24279  -32.36459 1.000 48.41141  ? 1075 LYS B C   1 
ATOM   2641 O  O   . LYS B 1 156 ? 6.88571   12.04881  -32.74164 1.000 50.04569  ? 1075 LYS B O   1 
ATOM   2642 C  CB  . LYS B 1 156 ? 9.12648   11.98251  -34.32323 1.000 51.11663  ? 1075 LYS B CB  1 
ATOM   2643 C  CG  . LYS B 1 156 ? 10.46311  12.05643  -35.03096 1.000 57.22763  ? 1075 LYS B CG  1 
ATOM   2644 C  CD  . LYS B 1 156 ? 11.36303  13.06436  -34.36395 1.000 76.33049  ? 1075 LYS B CD  1 
ATOM   2645 C  CE  . LYS B 1 156 ? 12.54939  13.33184  -35.24117 1.000 84.57425  ? 1075 LYS B CE  1 
ATOM   2646 N  NZ  . LYS B 1 156 ? 12.27413  14.34260  -36.29312 1.000 90.11019  ? 1075 LYS B NZ  1 
ATOM   2647 N  N   . LYS B 1 157 ? 7.53489   10.37398  -31.38019 1.000 47.38306  ? 1076 LYS B N   1 
ATOM   2648 C  CA  . LYS B 1 157 ? 6.28837   10.28699  -30.63939 1.000 47.20131  ? 1076 LYS B CA  1 
ATOM   2649 C  C   . LYS B 1 157 ? 6.54784   10.54100  -29.15627 1.000 45.58273  ? 1076 LYS B C   1 
ATOM   2650 O  O   . LYS B 1 157 ? 7.63884   10.26462  -28.65402 1.000 47.74849  ? 1076 LYS B O   1 
ATOM   2651 C  CB  . LYS B 1 157 ? 5.65924   8.89420   -30.81186 1.000 42.94146  ? 1076 LYS B CB  1 
ATOM   2652 C  CG  . LYS B 1 157 ? 5.30678   8.52532   -32.26041 1.000 42.24555  ? 1076 LYS B CG  1 
ATOM   2653 C  CD  . LYS B 1 157 ? 4.19902   9.36531   -32.88211 1.000 48.42954  ? 1076 LYS B CD  1 
ATOM   2654 C  CE  . LYS B 1 157 ? 3.87189   8.83162   -34.26863 1.000 47.99205  ? 1076 LYS B CE  1 
ATOM   2655 N  NZ  . LYS B 1 157 ? 2.91045   9.68702   -34.99562 1.000 55.28157  ? 1076 LYS B NZ  1 
ATOM   2656 N  N   . THR B 1 158 ? 5.54895   11.08904  -28.45601 1.000 46.14626  ? 1077 THR B N   1 
ATOM   2657 C  CA  . THR B 1 158 ? 5.60687   11.27097  -27.00362 1.000 41.07946  ? 1077 THR B CA  1 
ATOM   2658 C  C   . THR B 1 158 ? 4.81117   10.22705  -26.22401 1.000 42.39809  ? 1077 THR B C   1 
ATOM   2659 O  O   . THR B 1 158 ? 4.65623   10.36052  -25.00668 1.000 43.11257  ? 1077 THR B O   1 
ATOM   2660 C  CB  . THR B 1 158 ? 5.15436   12.67122  -26.61265 1.000 44.65311  ? 1077 THR B CB  1 
ATOM   2661 O  OG1 . THR B 1 158 ? 3.77013   12.85999  -26.94407 1.000 50.45735  ? 1077 THR B OG1 1 
ATOM   2662 C  CG2 . THR B 1 158 ? 6.01039   13.72336  -27.30561 1.000 55.17559  ? 1077 THR B CG2 1 
ATOM   2663 N  N   . ARG B 1 159 ? 4.30896   9.19579   -26.88822 1.000 38.00669  ? 1078 ARG B N   1 
ATOM   2664 C  CA  . ARG B 1 159 ? 3.62663   8.10213   -26.21897 1.000 36.14462  ? 1078 ARG B CA  1 
ATOM   2665 C  C   . ARG B 1 159 ? 4.05257   6.80589   -26.87107 1.000 38.01282  ? 1078 ARG B C   1 
ATOM   2666 O  O   . ARG B 1 159 ? 4.33405   6.76251   -28.07278 1.000 40.09469  ? 1078 ARG B O   1 
ATOM   2667 C  CB  . ARG B 1 159 ? 2.09514   8.27096   -26.27360 1.000 45.43709  ? 1078 ARG B CB  1 
ATOM   2668 C  CG  . ARG B 1 159 ? 1.44367   7.64379   -27.50790 1.000 48.92579  ? 1078 ARG B CG  1 
ATOM   2669 C  CD  . ARG B 1 159 ? -0.03637  8.01892   -27.65717 1.000 39.50894  ? 1078 ARG B CD  1 
ATOM   2670 N  NE  . ARG B 1 159 ? -0.46120  8.04633   -29.04939 1.000 48.48854  ? 1078 ARG B NE  1 
ATOM   2671 C  CZ  . ARG B 1 159 ? -1.71134  7.86311   -29.44671 1.000 48.53761  ? 1078 ARG B CZ  1 
ATOM   2672 N  NH1 . ARG B 1 159 ? -2.67119  7.56097   -28.58479 1.000 47.14156  ? 1078 ARG B NH1 1 
ATOM   2673 N  NH2 . ARG B 1 159 ? -2.00607  7.99811   -30.73374 1.000 48.97192  ? 1078 ARG B NH2 1 
ATOM   2674 N  N   . ILE B 1 160 ? 4.12651   5.76585   -26.05571 1.000 32.58687  ? 1079 ILE B N   1 
ATOM   2675 C  CA  . ILE B 1 160 ? 4.42497   4.42395   -26.53599 1.000 31.17384  ? 1079 ILE B CA  1 
ATOM   2676 C  C   . ILE B 1 160 ? 3.16393   3.83710   -27.14432 1.000 38.91442  ? 1079 ILE B C   1 
ATOM   2677 O  O   . ILE B 1 160 ? 2.11424   3.80657   -26.49140 1.000 34.86717  ? 1079 ILE B O   1 
ATOM   2678 C  CB  . ILE B 1 160 ? 4.94059   3.53864   -25.39041 1.000 33.14205  ? 1079 ILE B CB  1 
ATOM   2679 C  CG1 . ILE B 1 160 ? 6.32391   3.98752   -24.93578 1.000 32.73215  ? 1079 ILE B CG1 1 
ATOM   2680 C  CG2 . ILE B 1 160 ? 4.92903   2.06039   -25.77515 1.000 33.80868  ? 1079 ILE B CG2 1 
ATOM   2681 C  CD1 . ILE B 1 160 ? 6.61990   3.62775   -23.48089 1.000 33.19998  ? 1079 ILE B CD1 1 
ATOM   2682 N  N   . ILE B 1 161 ? 3.25864   3.37587   -28.39402 1.000 32.15199  ? 1080 ILE B N   1 
ATOM   2683 C  CA  . ILE B 1 161 ? 2.14443   2.69693   -29.06435 1.000 32.75696  ? 1080 ILE B CA  1 
ATOM   2684 C  C   . ILE B 1 161 ? 2.56414   1.26497   -29.38225 1.000 36.61217  ? 1080 ILE B C   1 
ATOM   2685 O  O   . ILE B 1 161 ? 3.74492   0.93290   -29.22693 1.000 34.36536  ? 1080 ILE B O   1 
ATOM   2686 C  CB  . ILE B 1 161 ? 1.68598   3.47604   -30.30797 1.000 37.45407  ? 1080 ILE B CB  1 
ATOM   2687 C  CG1 . ILE B 1 161 ? 2.75672   3.45572   -31.41085 1.000 38.28016  ? 1080 ILE B CG1 1 
ATOM   2688 C  CG2 . ILE B 1 161 ? 1.26631   4.88550   -29.91691 1.000 40.13782  ? 1080 ILE B CG2 1 
ATOM   2689 C  CD1 . ILE B 1 161 ? 2.32156   4.14830   -32.68461 1.000 40.53317  ? 1080 ILE B CD1 1 
ATOM   2690 N  N   . PRO B 1 162 ? 1.65505   0.37261   -29.79258 1.000 34.67797  ? 1081 PRO B N   1 
ATOM   2691 C  CA  . PRO B 1 162 ? 2.06928   -1.03920  -29.93275 1.000 35.49832  ? 1081 PRO B CA  1 
ATOM   2692 C  C   . PRO B 1 162 ? 3.27896   -1.26466  -30.83144 1.000 32.61140  ? 1081 PRO B C   1 
ATOM   2693 O  O   . PRO B 1 162 ? 4.14225   -2.07876  -30.47453 1.000 38.24321  ? 1081 PRO B O   1 
ATOM   2694 C  CB  . PRO B 1 162 ? 0.80728   -1.70739  -30.49041 1.000 40.52434  ? 1081 PRO B CB  1 
ATOM   2695 C  CG  . PRO B 1 162 ? -0.30597  -0.91641  -29.86876 1.000 41.11130  ? 1081 PRO B CG  1 
ATOM   2696 C  CD  . PRO B 1 162 ? 0.18518   0.51275   -29.84864 1.000 36.57430  ? 1081 PRO B CD  1 
ATOM   2697 N  N   . ARG B 1 163 ? 3.40763   -0.54534  -31.94527 1.000 37.91647  ? 1082 ARG B N   1 
ATOM   2698 C  CA  . ARG B 1 163 ? 4.54376   -0.82567  -32.81745 1.000 37.09385  ? 1082 ARG B CA  1 
ATOM   2699 C  C   . ARG B 1 163 ? 5.87836   -0.48133  -32.15809 1.000 42.50313  ? 1082 ARG B C   1 
ATOM   2700 O  O   . ARG B 1 163 ? 6.89144   -1.10528  -32.49159 1.000 39.35147  ? 1082 ARG B O   1 
ATOM   2701 C  CB  . ARG B 1 163 ? 4.38356   -0.09654  -34.14818 1.000 43.30343  ? 1082 ARG B CB  1 
ATOM   2702 C  CG  . ARG B 1 163 ? 4.50263   1.41267   -34.08816 1.000 39.96990  ? 1082 ARG B CG  1 
ATOM   2703 C  CD  . ARG B 1 163 ? 4.67760   1.95631   -35.50455 1.000 50.51720  ? 1082 ARG B CD  1 
ATOM   2704 N  NE  . ARG B 1 163 ? 4.80285   3.40690   -35.54553 1.000 48.74262  ? 1082 ARG B NE  1 
ATOM   2705 C  CZ  . ARG B 1 163 ? 3.88919   4.24171   -36.02292 1.000 55.81689  ? 1082 ARG B CZ  1 
ATOM   2706 N  NH1 . ARG B 1 163 ? 2.75671   3.80403   -36.55281 1.000 54.07125  ? 1082 ARG B NH1 1 
ATOM   2707 N  NH2 . ARG B 1 163 ? 4.13055   5.55020   -35.99201 1.000 48.51529  ? 1082 ARG B NH2 1 
ATOM   2708 N  N   . HIS B 1 164 ? 5.89476   0.43669   -31.18130 1.000 34.73845  ? 1083 HIS B N   1 
ATOM   2709 C  CA  . HIS B 1 164 ? 7.12083   0.68360   -30.42651 1.000 34.67750  ? 1083 HIS B CA  1 
ATOM   2710 C  C   . HIS B 1 164 ? 7.48302   -0.51400  -29.55425 1.000 35.17396  ? 1083 HIS B C   1 
ATOM   2711 O  O   . HIS B 1 164 ? 8.65699   -0.89848  -29.45769 1.000 35.81937  ? 1083 HIS B O   1 
ATOM   2712 C  CB  . HIS B 1 164 ? 6.96222   1.92335   -29.55863 1.000 35.40034  ? 1083 HIS B CB  1 
ATOM   2713 C  CG  . HIS B 1 164 ? 6.61356   3.15911   -30.32316 1.000 35.64783  ? 1083 HIS B CG  1 
ATOM   2714 N  ND1 . HIS B 1 164 ? 5.86109   4.17068   -29.76710 1.000 35.44789  ? 1083 HIS B ND1 1 
ATOM   2715 C  CD2 . HIS B 1 164 ? 6.88277   3.54197   -31.59690 1.000 37.18222  ? 1083 HIS B CD2 1 
ATOM   2716 C  CE1 . HIS B 1 164 ? 5.69714   5.13037   -30.65870 1.000 37.46259  ? 1083 HIS B CE1 1 
ATOM   2717 N  NE2 . HIS B 1 164 ? 6.29887   4.77035   -31.78087 1.000 38.29449  ? 1083 HIS B NE2 1 
ATOM   2718 N  N   . LEU B 1 165 ? 6.48958   -1.09518  -28.87930 1.000 32.73506  ? 1084 LEU B N   1 
ATOM   2719 C  CA  . LEU B 1 165 ? 6.72566   -2.28650  -28.06951 1.000 31.90807  ? 1084 LEU B CA  1 
ATOM   2720 C  C   . LEU B 1 165 ? 7.17590   -3.45028  -28.92692 1.000 38.86349  ? 1084 LEU B C   1 
ATOM   2721 O  O   . LEU B 1 165 ? 8.11436   -4.17495  -28.57357 1.000 33.71979  ? 1084 LEU B O   1 
ATOM   2722 C  CB  . LEU B 1 165 ? 5.46184   -2.66475  -27.30563 1.000 41.09174  ? 1084 LEU B CB  1 
ATOM   2723 C  CG  . LEU B 1 165 ? 5.14884   -1.85245  -26.06473 1.000 40.23997  ? 1084 LEU B CG  1 
ATOM   2724 C  CD1 . LEU B 1 165 ? 3.77417   -2.22192  -25.55544 1.000 34.72331  ? 1084 LEU B CD1 1 
ATOM   2725 C  CD2 . LEU B 1 165 ? 6.19148   -2.23203  -25.03424 1.000 36.03757  ? 1084 LEU B CD2 1 
ATOM   2726 N  N   . GLN B 1 166 ? 6.49745   -3.65878  -30.05641 1.000 37.93212  ? 1085 GLN B N   1 
ATOM   2727 C  CA  . GLN B 1 166 ? 6.83744   -4.78831  -30.90867 1.000 40.89510  ? 1085 GLN B CA  1 
ATOM   2728 C  C   . GLN B 1 166 ? 8.25114   -4.65089  -31.45184 1.000 40.07644  ? 1085 GLN B C   1 
ATOM   2729 O  O   . GLN B 1 166 ? 9.02289   -5.61878  -31.43599 1.000 39.81907  ? 1085 GLN B O   1 
ATOM   2730 C  CB  . GLN B 1 166 ? 5.79530   -4.92271  -32.01832 1.000 44.09321  ? 1085 GLN B CB  1 
ATOM   2731 C  CG  . GLN B 1 166 ? 4.42440   -5.30015  -31.42788 1.000 49.08796  ? 1085 GLN B CG  1 
ATOM   2732 C  CD  . GLN B 1 166 ? 3.23712   -4.79602  -32.24394 1.000 57.33915  ? 1085 GLN B CD  1 
ATOM   2733 O  OE1 . GLN B 1 166 ? 3.39854   -4.18567  -33.30197 1.000 57.89166  ? 1085 GLN B OE1 1 
ATOM   2734 N  NE2 . GLN B 1 166 ? 2.03272   -5.04051  -31.73587 1.000 54.34110  ? 1085 GLN B NE2 1 
ATOM   2735 N  N   . LEU B 1 167 ? 8.62776   -3.44408  -31.88015 1.000 36.92532  ? 1086 LEU B N   1 
ATOM   2736 C  CA  . LEU B 1 167 ? 9.98275   -3.21544  -32.37320 1.000 44.29915  ? 1086 LEU B CA  1 
ATOM   2737 C  C   . LEU B 1 167 ? 11.01980  -3.41316  -31.27524 1.000 38.91505  ? 1086 LEU B C   1 
ATOM   2738 O  O   . LEU B 1 167 ? 12.04534  -4.07245  -31.48964 1.000 40.11365  ? 1086 LEU B O   1 
ATOM   2739 C  CB  . LEU B 1 167 ? 10.09186  -1.80416  -32.96343 1.000 40.88405  ? 1086 LEU B CB  1 
ATOM   2740 C  CG  . LEU B 1 167 ? 11.28907  -1.52193  -33.86844 1.000 54.00829  ? 1086 LEU B CG  1 
ATOM   2741 C  CD1 . LEU B 1 167 ? 11.26875  -2.39958  -35.11188 1.000 58.89562  ? 1086 LEU B CD1 1 
ATOM   2742 C  CD2 . LEU B 1 167 ? 11.36888  -0.02439  -34.23050 1.000 55.97412  ? 1086 LEU B CD2 1 
ATOM   2743 N  N   . ALA B 1 168 ? 10.75880  -2.86963  -30.08403 1.000 36.49635  ? 1087 ALA B N   1 
ATOM   2744 C  CA  . ALA B 1 168 ? 11.72325  -2.96175  -28.99721 1.000 33.43988  ? 1087 ALA B CA  1 
ATOM   2745 C  C   . ALA B 1 168 ? 11.96766  -4.40977  -28.58968 1.000 38.77577  ? 1087 ALA B C   1 
ATOM   2746 O  O   . ALA B 1 168 ? 13.11433  -4.81607  -28.38148 1.000 37.90322  ? 1087 ALA B O   1 
ATOM   2747 C  CB  . ALA B 1 168 ? 11.23046  -2.15470  -27.79360 1.000 42.34100  ? 1087 ALA B CB  1 
ATOM   2748 N  N   . VAL B 1 169 ? 10.90445  -5.20474  -28.49147 1.000 32.60030  ? 1088 VAL B N   1 
ATOM   2749 C  CA  . VAL B 1 169 ? 11.05649  -6.61436  -28.12768 1.000 31.35770  ? 1088 VAL B CA  1 
ATOM   2750 C  C   . VAL B 1 169 ? 11.73811  -7.38696  -29.25201 1.000 35.45922  ? 1088 VAL B C   1 
ATOM   2751 O  O   . VAL B 1 169 ? 12.65996  -8.16954  -29.01699 1.000 34.23091  ? 1088 VAL B O   1 
ATOM   2752 C  CB  . VAL B 1 169 ? 9.68449   -7.21661  -27.77429 1.000 34.89324  ? 1088 VAL B CB  1 
ATOM   2753 C  CG1 . VAL B 1 169 ? 9.76274   -8.74919  -27.66635 1.000 40.69898  ? 1088 VAL B CG1 1 
ATOM   2754 C  CG2 . VAL B 1 169 ? 9.16109   -6.62071  -26.47595 1.000 33.84207  ? 1088 VAL B CG2 1 
ATOM   2755 N  N   . ARG B 1 170 ? 11.33338  -7.14591  -30.49560 1.000 36.69751  ? 1089 ARG B N   1 
ATOM   2756 C  CA  . ARG B 1 170 ? 11.88470  -7.92486  -31.59586 1.000 37.73464  ? 1089 ARG B CA  1 
ATOM   2757 C  C   . ARG B 1 170 ? 13.37721  -7.67095  -31.77880 1.000 38.67087  ? 1089 ARG B C   1 
ATOM   2758 O  O   . ARG B 1 170 ? 14.11804  -8.59168  -32.14107 1.000 40.64411  ? 1089 ARG B O   1 
ATOM   2759 C  CB  . ARG B 1 170 ? 11.10870  -7.63783  -32.87883 1.000 41.48544  ? 1089 ARG B CB  1 
ATOM   2760 C  CG  . ARG B 1 170 ? 11.85376  -7.99985  -34.13696 1.000 51.31575  ? 1089 ARG B CG  1 
ATOM   2761 C  CD  . ARG B 1 170 ? 11.75449  -9.49475  -34.42481 1.000 59.91416  ? 1089 ARG B CD  1 
ATOM   2762 N  NE  . ARG B 1 170 ? 10.41641  -10.02259 -34.17380 1.000 69.71885  ? 1089 ARG B NE  1 
ATOM   2763 C  CZ  . ARG B 1 170 ? 9.57138   -10.40243 -35.12941 1.000 76.35696  ? 1089 ARG B CZ  1 
ATOM   2764 N  NH1 . ARG B 1 170 ? 9.88011   -10.29691 -36.41812 1.000 79.83729  ? 1089 ARG B NH1 1 
ATOM   2765 N  NH2 . ARG B 1 170 ? 8.38508   -10.90146 -34.78917 1.000 71.93933  ? 1089 ARG B NH2 1 
ATOM   2766 N  N   . ASN B 1 171 ? 13.84145  -6.44655  -31.51896 1.000 36.36977  ? 1090 ASN B N   1 
ATOM   2767 C  CA  . ASN B 1 171 ? 15.22877  -6.07279  -31.76774 1.000 42.65002  ? 1090 ASN B CA  1 
ATOM   2768 C  C   . ASN B 1 171 ? 16.16682  -6.43227  -30.62938 1.000 38.88892  ? 1090 ASN B C   1 
ATOM   2769 O  O   . ASN B 1 171 ? 17.37746  -6.19204  -30.75101 1.000 39.52808  ? 1090 ASN B O   1 
ATOM   2770 C  CB  . ASN B 1 171 ? 15.33877  -4.56312  -32.00986 1.000 42.10509  ? 1090 ASN B CB  1 
ATOM   2771 C  CG  . ASN B 1 171 ? 14.84378  -4.15016  -33.37380 1.000 50.60363  ? 1090 ASN B CG  1 
ATOM   2772 O  OD1 . ASN B 1 171 ? 14.71355  -4.97504  -34.27874 1.000 52.25187  ? 1090 ASN B OD1 1 
ATOM   2773 N  ND2 . ASN B 1 171 ? 14.56099  -2.85695  -33.53062 1.000 51.96225  ? 1090 ASN B ND2 1 
ATOM   2774 N  N   . ASP B 1 172 ? 15.64745  -6.97216  -29.53769 1.000 35.13180  ? 1091 ASP B N   1 
ATOM   2775 C  CA  . ASP B 1 172 ? 16.45065  -7.39912  -28.40023 1.000 33.13948  ? 1091 ASP B CA  1 
ATOM   2776 C  C   . ASP B 1 172 ? 16.41882  -8.92021  -28.37133 1.000 33.01548  ? 1091 ASP B C   1 
ATOM   2777 O  O   . ASP B 1 172 ? 15.36892  -9.50590  -28.10327 1.000 33.50792  ? 1091 ASP B O   1 
ATOM   2778 C  CB  . ASP B 1 172 ? 15.88776  -6.80993  -27.10903 1.000 34.15353  ? 1091 ASP B CB  1 
ATOM   2779 C  CG  . ASP B 1 172 ? 16.79289  -7.02974  -25.92613 1.000 40.51413  ? 1091 ASP B CG  1 
ATOM   2780 O  OD1 . ASP B 1 172 ? 16.88168  -8.17980  -25.44330 1.000 40.79818  ? 1091 ASP B OD1 1 
ATOM   2781 O  OD2 . ASP B 1 172 ? 17.39677  -6.04124  -25.46276 1.000 37.33583  ? 1091 ASP B OD2 1 
ATOM   2782 N  N   . GLU B 1 173 ? 17.56004  -9.55802  -28.63998 1.000 33.86397  ? 1092 GLU B N   1 
ATOM   2783 C  CA  . GLU B 1 173 ? 17.55691  -11.01019 -28.81459 1.000 35.21592  ? 1092 GLU B CA  1 
ATOM   2784 C  C   . GLU B 1 173 ? 16.99470  -11.72648 -27.59288 1.000 30.48484  ? 1092 GLU B C   1 
ATOM   2785 O  O   . GLU B 1 173 ? 16.23124  -12.68824 -27.72850 1.000 34.01033  ? 1092 GLU B O   1 
ATOM   2786 C  CB  . GLU B 1 173 ? 18.96684  -11.51378 -29.13418 1.000 41.76450  ? 1092 GLU B CB  1 
ATOM   2787 C  CG  . GLU B 1 173 ? 19.06298  -13.02279 -29.27982 1.000 51.77330  ? 1092 GLU B CG  1 
ATOM   2788 C  CD  . GLU B 1 173 ? 20.32141  -13.46441 -30.01797 1.000 72.12311  ? 1092 GLU B CD  1 
ATOM   2789 O  OE1 . GLU B 1 173 ? 21.26641  -12.65242 -30.12348 1.000 74.79920  ? 1092 GLU B OE1 1 
ATOM   2790 O  OE2 . GLU B 1 173 ? 20.34454  -14.60799 -30.52989 1.000 76.72092  ? 1092 GLU B OE2 1 
ATOM   2791 N  N   . GLU B 1 174 ? 17.36850  -11.29450 -26.39272 1.000 31.81740  ? 1093 GLU B N   1 
ATOM   2792 C  CA  . GLU B 1 174 ? 16.89076  -11.99635 -25.19893 1.000 30.84840  ? 1093 GLU B CA  1 
ATOM   2793 C  C   . GLU B 1 174 ? 15.40515  -11.74656 -24.94849 1.000 27.55309  ? 1093 GLU B C   1 
ATOM   2794 O  O   . GLU B 1 174 ? 14.65379  -12.67350 -24.60952 1.000 29.05886  ? 1093 GLU B O   1 
ATOM   2795 C  CB  . GLU B 1 174 ? 17.72851  -11.58701 -23.98749 1.000 35.33025  ? 1093 GLU B CB  1 
ATOM   2796 C  CG  . GLU B 1 174 ? 19.16178  -12.13286 -24.05441 1.000 30.77242  ? 1093 GLU B CG  1 
ATOM   2797 C  CD  . GLU B 1 174 ? 20.11405  -11.52008 -23.02853 1.000 29.51589  ? 1093 GLU B CD  1 
ATOM   2798 O  OE1 . GLU B 1 174 ? 19.70277  -10.61844 -22.27217 1.000 33.39454  ? 1093 GLU B OE1 1 
ATOM   2799 O  OE2 . GLU B 1 174 ? 21.27331  -11.97510 -22.95578 1.000 32.45966  ? 1093 GLU B OE2 1 
ATOM   2800 N  N   . LEU B 1 175 ? 14.94760  -10.50135 -25.08444 1.000 28.24544  ? 1094 LEU B N   1 
ATOM   2801 C  CA  . LEU B 1 175 ? 13.52512  -10.24366 -24.86968 1.000 30.67254  ? 1094 LEU B CA  1 
ATOM   2802 C  C   . LEU B 1 175 ? 12.67249  -10.91429 -25.93985 1.000 27.19444  ? 1094 LEU B C   1 
ATOM   2803 O  O   . LEU B 1 175 ? 11.54098  -11.32038 -25.65897 1.000 29.96490  ? 1094 LEU B O   1 
ATOM   2804 C  CB  . LEU B 1 175 ? 13.26050  -8.73518  -24.83895 1.000 30.95344  ? 1094 LEU B CB  1 
ATOM   2805 C  CG  . LEU B 1 175 ? 13.69465  -8.02166  -23.54680 1.000 31.51783  ? 1094 LEU B CG  1 
ATOM   2806 C  CD1 . LEU B 1 175 ? 13.62901  -6.50231  -23.73053 1.000 34.29349  ? 1094 LEU B CD1 1 
ATOM   2807 C  CD2 . LEU B 1 175 ? 12.86084  -8.46092  -22.35339 1.000 29.90650  ? 1094 LEU B CD2 1 
ATOM   2808 N  N   . ASN B 1 176 ? 13.18123  -10.98704 -27.17769 1.000 27.40311  ? 1095 ASN B N   1 
ATOM   2809 C  CA  . ASN B 1 176 ? 12.44665  -11.65218 -28.24874 1.000 28.94241  ? 1095 ASN B CA  1 
ATOM   2810 C  C   . ASN B 1 176 ? 12.23779  -13.12922 -27.93469 1.000 33.60148  ? 1095 ASN B C   1 
ATOM   2811 O  O   . ASN B 1 176 ? 11.14816  -13.67540 -28.15807 1.000 31.70187  ? 1095 ASN B O   1 
ATOM   2812 C  CB  . ASN B 1 176 ? 13.18947  -11.49317 -29.57213 1.000 32.96127  ? 1095 ASN B CB  1 
ATOM   2813 C  CG  . ASN B 1 176 ? 12.38158  -11.99238 -30.74536 1.000 37.80134  ? 1095 ASN B CG  1 
ATOM   2814 O  OD1 . ASN B 1 176 ? 11.21184  -11.63999 -30.90038 1.000 35.20404  ? 1095 ASN B OD1 1 
ATOM   2815 N  ND2 . ASN B 1 176 ? 12.98700  -12.84650 -31.56021 1.000 44.83952  ? 1095 ASN B ND2 1 
ATOM   2816 N  N   . LYS B 1 177 ? 13.27393  -13.79760 -27.42449 1.000 29.88832  ? 1096 LYS B N   1 
ATOM   2817 C  CA  . LYS B 1 177 ? 13.10125  -15.19042 -27.00801 1.000 30.52247  ? 1096 LYS B CA  1 
ATOM   2818 C  C   . LYS B 1 177 ? 12.05290  -15.31130 -25.90989 1.000 28.42993  ? 1096 LYS B C   1 
ATOM   2819 O  O   . LYS B 1 177 ? 11.21910  -16.22741 -25.92673 1.000 28.72009  ? 1096 LYS B O   1 
ATOM   2820 C  CB  . LYS B 1 177 ? 14.44257  -15.76779 -26.53948 1.000 27.76651  ? 1096 LYS B CB  1 
ATOM   2821 C  CG  . LYS B 1 177 ? 15.43355  -15.95632 -27.69849 1.000 33.66292  ? 1096 LYS B CG  1 
ATOM   2822 C  CD  . LYS B 1 177 ? 16.70953  -16.61780 -27.20539 1.000 34.24639  ? 1096 LYS B CD  1 
ATOM   2823 C  CE  . LYS B 1 177 ? 17.78813  -16.59910 -28.25742 1.000 38.04915  ? 1096 LYS B CE  1 
ATOM   2824 N  NZ  . LYS B 1 177 ? 18.96982  -17.38398 -27.85899 1.000 43.69727  ? 1096 LYS B NZ  1 
ATOM   2825 N  N   . LEU B 1 178 ? 12.07764  -14.39872 -24.94426 1.000 28.36287  ? 1097 LEU B N   1 
ATOM   2826 C  CA  . LEU B 1 178 ? 11.17356  -14.48862 -23.79777 1.000 28.24340  ? 1097 LEU B CA  1 
ATOM   2827 C  C   . LEU B 1 178 ? 9.71977   -14.22234 -24.17918 1.000 28.94511  ? 1097 LEU B C   1 
ATOM   2828 O  O   . LEU B 1 178 ? 8.81257   -14.92033 -23.71484 1.000 30.43419  ? 1097 LEU B O   1 
ATOM   2829 C  CB  . LEU B 1 178 ? 11.61616  -13.49645 -22.72099 1.000 25.34561  ? 1097 LEU B CB  1 
ATOM   2830 C  CG  . LEU B 1 178 ? 10.74845  -13.42009 -21.45779 1.000 27.31627  ? 1097 LEU B CG  1 
ATOM   2831 C  CD1 . LEU B 1 178 ? 10.85434  -14.73115 -20.67894 1.000 30.62988  ? 1097 LEU B CD1 1 
ATOM   2832 C  CD2 . LEU B 1 178 ? 11.17049  -12.23786 -20.56350 1.000 30.60710  ? 1097 LEU B CD2 1 
ATOM   2833 N  N   . LEU B 1 179 ? 9.48361   -13.22497 -25.03272 1.000 28.26912  ? 1098 LEU B N   1 
ATOM   2834 C  CA  . LEU B 1 179 ? 8.16065   -12.64477 -25.26369 1.000 28.67105  ? 1098 LEU B CA  1 
ATOM   2835 C  C   . LEU B 1 179 ? 7.59828   -12.79599 -26.66900 1.000 40.44660  ? 1098 LEU B C   1 
ATOM   2836 O  O   . LEU B 1 179 ? 6.42201   -12.47040 -26.87533 1.000 38.59414  ? 1098 LEU B O   1 
ATOM   2837 C  CB  . LEU B 1 179 ? 8.18480   -11.14964 -24.92779 1.000 29.58688  ? 1098 LEU B CB  1 
ATOM   2838 C  CG  . LEU B 1 179 ? 8.59481   -10.85798 -23.50256 1.000 32.08202  ? 1098 LEU B CG  1 
ATOM   2839 C  CD1 . LEU B 1 179 ? 8.84231   -9.36050  -23.33506 1.000 37.94097  ? 1098 LEU B CD1 1 
ATOM   2840 C  CD2 . LEU B 1 179 ? 7.50796   -11.34013 -22.56964 1.000 30.91058  ? 1098 LEU B CD2 1 
ATOM   2841 N  N   . GLY B 1 180 ? 8.39679   -13.22453 -27.64481 1.000 35.30686  ? 1099 GLY B N   1 
ATOM   2842 C  CA  . GLY B 1 180 ? 7.96879   -13.19354 -29.03809 1.000 40.54318  ? 1099 GLY B CA  1 
ATOM   2843 C  C   . GLY B 1 180 ? 6.75869   -14.04263 -29.36754 1.000 50.67584  ? 1099 GLY B C   1 
ATOM   2844 O  O   . GLY B 1 180 ? 6.16414   -13.86697 -30.44010 1.000 54.17697  ? 1099 GLY B O   1 
ATOM   2845 N  N   . GLY B 1 181 ? 6.39510   -14.97103 -28.49662 1.000 50.74566  ? 1100 GLY B N   1 
ATOM   2846 C  CA  . GLY B 1 181 ? 5.23284   -15.81680 -28.66287 1.000 56.48972  ? 1100 GLY B CA  1 
ATOM   2847 C  C   . GLY B 1 181 ? 3.98032   -15.32054 -27.97579 1.000 61.48789  ? 1100 GLY B C   1 
ATOM   2848 O  O   . GLY B 1 181 ? 2.94347   -15.98763 -28.04626 1.000 66.74252  ? 1100 GLY B O   1 
ATOM   2849 N  N   . VAL B 1 182 ? 4.02948   -14.14873 -27.34044 1.000 53.46274  ? 1101 VAL B N   1 
ATOM   2850 C  CA  . VAL B 1 182 ? 2.87773   -13.61220 -26.61944 1.000 57.20236  ? 1101 VAL B CA  1 
ATOM   2851 C  C   . VAL B 1 182 ? 1.96712   -12.90096 -27.61115 1.000 63.00188  ? 1101 VAL B C   1 
ATOM   2852 O  O   . VAL B 1 182 ? 2.42648   -12.10369 -28.43752 1.000 57.79971  ? 1101 VAL B O   1 
ATOM   2853 C  CB  . VAL B 1 182 ? 3.32917   -12.65104 -25.50286 1.000 51.51382  ? 1101 VAL B CB  1 
ATOM   2854 C  CG1 . VAL B 1 182 ? 2.12166   -11.97701 -24.84691 1.000 45.22471  ? 1101 VAL B CG1 1 
ATOM   2855 C  CG2 . VAL B 1 182 ? 4.17219   -13.37590 -24.45814 1.000 44.12785  ? 1101 VAL B CG2 1 
ATOM   2856 N  N   . THR B 1 183 ? 0.67040   -13.18121 -27.52448 1.000 81.32631  ? 1102 THR B N   1 
ATOM   2857 C  CA  . THR B 1 183 ? -0.30041  -12.61689 -28.45598 1.000 93.62395  ? 1102 THR B CA  1 
ATOM   2858 C  C   . THR B 1 183 ? -1.46200  -11.93714 -27.73397 1.000 96.87853  ? 1102 THR B C   1 
ATOM   2859 O  O   . THR B 1 183 ? -1.28272  -10.92738 -27.05214 1.000 88.97863  ? 1102 THR B O   1 
ATOM   2860 C  CB  . THR B 1 183 ? -0.86996  -13.70926 -29.38303 1.000 105.51252 ? 1102 THR B CB  1 
ATOM   2861 O  OG1 . THR B 1 183 ? -1.40623  -14.77396 -28.58737 1.000 104.93397 ? 1102 THR B OG1 1 
ATOM   2862 C  CG2 . THR B 1 183 ? 0.22102   -14.26920 -30.28939 1.000 96.25649  ? 1102 THR B CG2 1 
ATOM   2863 N  N   . GLU C 2 11  ? -0.63453  26.95757  23.21410  1.000 98.32045  ? 131  GLU C N   1 
ATOM   2864 C  CA  . GLU C 2 11  ? 0.55992   26.37010  22.61423  1.000 90.96939  ? 131  GLU C CA  1 
ATOM   2865 C  C   . GLU C 2 11  ? 0.72142   26.81186  21.16232  1.000 94.09929  ? 131  GLU C C   1 
ATOM   2866 O  O   . GLU C 2 11  ? -0.17816  27.42345  20.58180  1.000 96.94725  ? 131  GLU C O   1 
ATOM   2867 C  CB  . GLU C 2 11  ? 0.51446   24.84099  22.70675  1.000 92.19601  ? 131  GLU C CB  1 
ATOM   2868 C  CG  . GLU C 2 11  ? -0.76671  24.21030  22.19467  0.000 98.65957  ? 131  GLU C CG  1 
ATOM   2869 C  CD  . GLU C 2 11  ? -0.94858  22.78852  22.69217  0.000 100.61843 ? 131  GLU C CD  1 
ATOM   2870 O  OE1 . GLU C 2 11  ? -0.78921  22.55919  23.91002  0.000 100.04529 ? 131  GLU C OE1 1 
ATOM   2871 O  OE2 . GLU C 2 11  ? -1.24243  21.89922  21.86625  0.000 101.99679 ? 131  GLU C OE2 1 
ATOM   2872 N  N   . GLY C 2 12  ? 1.88076   26.50531  20.58638  1.000 83.77351  ? 132  GLY C N   1 
ATOM   2873 C  CA  . GLY C 2 12  ? 2.16524   26.86164  19.21064  1.000 93.33309  ? 132  GLY C CA  1 
ATOM   2874 C  C   . GLY C 2 12  ? 1.57445   25.88637  18.21255  1.000 90.47873  ? 132  GLY C C   1 
ATOM   2875 O  O   . GLY C 2 12  ? 2.28780   25.03308  17.67601  1.000 88.89282  ? 132  GLY C O   1 
ATOM   2876 N  N   . TYR C 2 13  ? 0.26639   25.98201  17.97987  1.000 88.31087  ? 133  TYR C N   1 
ATOM   2877 C  CA  . TYR C 2 13  ? -0.38585  25.10468  17.01794  1.000 91.75033  ? 133  TYR C CA  1 
ATOM   2878 C  C   . TYR C 2 13  ? 0.17089   25.33748  15.62002  1.000 85.65732  ? 133  TYR C C   1 
ATOM   2879 O  O   . TYR C 2 13  ? 0.29559   26.47807  15.16684  1.000 92.84823  ? 133  TYR C O   1 
ATOM   2880 C  CB  . TYR C 2 13  ? -1.89643  25.33339  17.03959  1.000 88.33213  ? 133  TYR C CB  1 
ATOM   2881 C  CG  . TYR C 2 13  ? -2.57009  24.70966  18.23711  0.000 92.92901  ? 133  TYR C CG  1 
ATOM   2882 C  CD1 . TYR C 2 13  ? -2.70840  23.33230  18.33357  0.000 93.29597  ? 133  TYR C CD1 1 
ATOM   2883 C  CD2 . TYR C 2 13  ? -3.06235  25.49274  19.27248  0.000 95.50155  ? 133  TYR C CD2 1 
ATOM   2884 C  CE1 . TYR C 2 13  ? -3.31795  22.75007  19.42458  0.000 96.19231  ? 133  TYR C CE1 1 
ATOM   2885 C  CE2 . TYR C 2 13  ? -3.67696  24.91891  20.36934  0.000 98.31087  ? 133  TYR C CE2 1 
ATOM   2886 C  CZ  . TYR C 2 13  ? -3.80084  23.54653  20.43979  0.000 99.56614  ? 133  TYR C CZ  1 
ATOM   2887 O  OH  . TYR C 2 13  ? -4.41001  22.96647  21.52808  0.000 100.91207 ? 133  TYR C OH  1 
ATOM   2888 N  N   . GLN C 2 14  ? 0.51407   24.25009  14.93891  1.000 93.12253  ? 134  GLN C N   1 
ATOM   2889 C  CA  . GLN C 2 14  ? 1.01738   24.36748  13.58314  1.000 87.45187  ? 134  GLN C CA  1 
ATOM   2890 C  C   . GLN C 2 14  ? -0.11002  24.82044  12.65592  1.000 85.06176  ? 134  GLN C C   1 
ATOM   2891 O  O   . GLN C 2 14  ? -1.29148  24.80107  13.00978  1.000 87.87445  ? 134  GLN C O   1 
ATOM   2892 C  CB  . GLN C 2 14  ? 1.64101   23.04546  13.13900  1.000 87.51333  ? 134  GLN C CB  1 
ATOM   2893 C  CG  . GLN C 2 14  ? 2.94343   22.71382  13.87698  1.000 87.57846  ? 134  GLN C CG  1 
ATOM   2894 C  CD  . GLN C 2 14  ? 2.96707   21.30567  14.45524  1.000 82.50164  ? 134  GLN C CD  1 
ATOM   2895 O  OE1 . GLN C 2 14  ? 1.95448   20.80096  14.93276  1.000 77.23686  ? 134  GLN C OE1 1 
ATOM   2896 N  NE2 . GLN C 2 14  ? 4.13054   20.66698  14.41224  1.000 86.02729  ? 134  GLN C NE2 1 
ATOM   2897 N  N   . ASP C 2 15  ? 0.26200   25.27170  11.46639  1.000 86.01062  ? 135  ASP C N   1 
ATOM   2898 C  CA  . ASP C 2 15  ? -0.69003  25.89344  10.55992  1.000 87.77964  ? 135  ASP C CA  1 
ATOM   2899 C  C   . ASP C 2 15  ? -0.74077  25.14355  9.23883   1.000 88.66614  ? 135  ASP C C   1 
ATOM   2900 O  O   . ASP C 2 15  ? 0.28303   24.67151  8.73586   1.000 87.60928  ? 135  ASP C O   1 
ATOM   2901 C  CB  . ASP C 2 15  ? -0.34011  27.36304  10.32085  1.000 90.69641  ? 135  ASP C CB  1 
ATOM   2902 C  CG  . ASP C 2 15  ? -1.21863  28.30273  11.12054  0.000 92.84365  ? 135  ASP C CG  1 
ATOM   2903 O  OD1 . ASP C 2 15  ? -1.33979  28.10193  12.34738  0.000 91.08890  ? 135  ASP C OD1 1 
ATOM   2904 O  OD2 . ASP C 2 15  ? -1.78948  29.24009  10.52440  0.000 96.97914  ? 135  ASP C OD2 1 
ATOM   2905 N  N   . TYR C 2 16  ? -1.94657  25.01153  8.69310   1.000 91.11823  ? 136  TYR C N   1 
ATOM   2906 C  CA  . TYR C 2 16  ? -2.12659  24.39765  7.38402   1.000 92.96763  ? 136  TYR C CA  1 
ATOM   2907 C  C   . TYR C 2 16  ? -2.69828  25.38966  6.37532   1.000 101.21901 ? 136  TYR C C   1 
ATOM   2908 O  O   . TYR C 2 16  ? -2.01471  25.70683  5.39834   1.000 100.36832 ? 136  TYR C O   1 
ATOM   2909 C  CB  . TYR C 2 16  ? -2.98361  23.13175  7.57564   1.000 92.43555  ? 136  TYR C CB  1 
ATOM   2910 C  CG  . TYR C 2 16  ? -2.76707  22.56445  8.97447   1.000 88.72492  ? 136  TYR C CG  1 
ATOM   2911 C  CD1 . TYR C 2 16  ? -1.53806  22.02433  9.34739   1.000 85.35008  ? 136  TYR C CD1 1 
ATOM   2912 C  CD2 . TYR C 2 16  ? -3.76523  22.63157  9.93929   1.000 89.05557  ? 136  TYR C CD2 1 
ATOM   2913 C  CE1 . TYR C 2 16  ? -1.31861  21.55560  10.63257  1.000 82.17084  ? 136  TYR C CE1 1 
ATOM   2914 C  CE2 . TYR C 2 16  ? -3.55713  22.15382  11.22268  1.000 86.05133  ? 136  TYR C CE2 1 
ATOM   2915 C  CZ  . TYR C 2 16  ? -2.33444  21.61942  11.56347  1.000 82.49211  ? 136  TYR C CZ  1 
ATOM   2916 O  OH  . TYR C 2 16  ? -2.13137  21.15514  12.84115  1.000 79.71416  ? 136  TYR C OH  1 
ATOM   2917 N  N   . GLU C 2 17  ? -3.89119  25.96288  6.62250   1.000 123.57337 ? 137  GLU C N   1 
ATOM   2918 C  CA  . GLU C 2 17  ? -4.49130  27.05888  5.85039   1.000 124.91513 ? 137  GLU C CA  1 
ATOM   2919 C  C   . GLU C 2 17  ? -4.91911  26.64051  4.43908   1.000 122.04672 ? 137  GLU C C   1 
ATOM   2920 O  O   . GLU C 2 17  ? -4.45515  25.61047  3.93425   1.000 116.89149 ? 137  GLU C O   1 
ATOM   2921 C  CB  . GLU C 2 17  ? -3.52224  28.24767  5.79957   1.000 134.67887 ? 137  GLU C CB  1 
ATOM   2922 C  CG  . GLU C 2 17  ? -3.25676  28.90302  7.15329   0.000 135.57241 ? 137  GLU C CG  1 
ATOM   2923 C  CD  . GLU C 2 17  ? -4.46925  29.62904  7.71494   0.000 144.81650 ? 137  GLU C CD  1 
ATOM   2924 O  OE1 . GLU C 2 17  ? -5.38519  28.95918  8.23839   0.000 149.11891 ? 137  GLU C OE1 1 
ATOM   2925 O  OE2 . GLU C 2 17  ? -4.50612  30.87493  7.63028   0.000 150.09238 ? 137  GLU C OE2 1 
ATOM   2926 N  N   . PRO C 2 18  ? -5.79698  27.40710  3.77500   1.000 127.01685 ? 138  PRO C N   1 
ATOM   2927 C  CA  . PRO C 2 18  ? -6.37449  26.96262  2.49283   1.000 129.87952 ? 138  PRO C CA  1 
ATOM   2928 C  C   . PRO C 2 18  ? -5.33449  26.74334  1.40154   1.000 129.69069 ? 138  PRO C C   1 
ATOM   2929 O  O   . PRO C 2 18  ? -4.14488  27.02509  1.55198   1.000 122.32523 ? 138  PRO C O   1 
ATOM   2930 C  CB  . PRO C 2 18  ? -7.33020  28.10218  2.12200   1.000 126.88438 ? 138  PRO C CB  1 
ATOM   2931 C  CG  . PRO C 2 18  ? -7.71549  28.69718  3.42066   1.000 124.61333 ? 138  PRO C CG  1 
ATOM   2932 C  CD  . PRO C 2 18  ? -6.48911  28.60599  4.28687   1.000 124.79311 ? 138  PRO C CD  1 
ATOM   2933 N  N   . GLU C 2 19  ? -5.81789  26.24058  0.26543   1.000 149.30660 ? 139  GLU C N   1 
ATOM   2934 C  CA  . GLU C 2 19  ? -4.95476  25.71778  -0.78604  1.000 153.18838 ? 139  GLU C CA  1 
ATOM   2935 C  C   . GLU C 2 19  ? -5.52718  26.07823  -2.15062  1.000 172.39340 ? 139  GLU C C   1 
ATOM   2936 O  O   . GLU C 2 19  ? -6.49368  26.83778  -2.26921  1.000 179.00571 ? 139  GLU C O   1 
ATOM   2937 C  CB  . GLU C 2 19  ? -4.80715  24.19764  -0.67048  1.000 149.33990 ? 139  GLU C CB  1 
ATOM   2938 C  CG  . GLU C 2 19  ? -6.03474  23.39114  -1.13860  1.000 160.55175 ? 139  GLU C CG  1 
ATOM   2939 C  CD  . GLU C 2 19  ? -7.11933  23.21755  -0.07850  1.000 151.08837 ? 139  GLU C CD  1 
ATOM   2940 O  OE1 . GLU C 2 19  ? -7.10652  23.93349  0.94494   1.000 148.13726 ? 139  GLU C OE1 1 
ATOM   2941 O  OE2 . GLU C 2 19  ? -7.99353  22.34775  -0.27311  1.000 147.14148 ? 139  GLU C OE2 1 
ATOM   2942 N  N   . ALA C 2 20  ? -4.91377  25.50438  -3.18376  1.000 171.86311 ? 140  ALA C N   1 
ATOM   2943 C  CA  . ALA C 2 20  ? -5.38672  25.59473  -4.55748  1.000 178.53353 ? 140  ALA C CA  1 
ATOM   2944 C  C   . ALA C 2 20  ? -4.91536  24.36543  -5.33506  1.000 170.55952 ? 140  ALA C C   1 
ATOM   2945 O  O   . ALA C 2 20  ? -5.39443  24.06912  -6.43119  1.000 176.56012 ? 140  ALA C O   1 
ATOM   2946 C  CB  . ALA C 2 20  ? -4.89179  26.87329  -5.21472  1.000 167.93361 ? 140  ALA C CB  1 
ATOM   2947 O  OXT . ALA C 2 20  ? -4.03657  23.63151  -4.87919  1.000 154.63788 ? 140  ALA C OXT 1 
ATOM   2948 N  N   . PRO D 2 8   ? 4.83484   -5.76195  -39.02969 1.000 117.01216 ? 128  PRO D N   1 
ATOM   2949 C  CA  . PRO D 2 8   ? 4.16743   -4.54649  -38.55068 1.000 119.22017 ? 128  PRO D CA  1 
ATOM   2950 C  C   . PRO D 2 8   ? 4.83033   -3.27417  -39.07483 1.000 117.79794 ? 128  PRO D C   1 
ATOM   2951 O  O   . PRO D 2 8   ? 6.02299   -3.06987  -38.85064 1.000 114.66855 ? 128  PRO D O   1 
ATOM   2952 C  CB  . PRO D 2 8   ? 4.30484   -4.65255  -37.03028 1.000 114.00192 ? 128  PRO D CB  1 
ATOM   2953 C  CG  . PRO D 2 8   ? 4.36088   -6.11867  -36.77144 1.000 110.18208 ? 128  PRO D CG  1 
ATOM   2954 C  CD  . PRO D 2 8   ? 5.10982   -6.71084  -37.93638 1.000 116.61086 ? 128  PRO D CD  1 
ATOM   2955 N  N   . SER D 2 9   ? 4.05981   -2.43798  -39.76975 1.000 114.95537 ? 129  SER D N   1 
ATOM   2956 C  CA  . SER D 2 9   ? 4.60165   -1.20837  -40.33506 1.000 112.87589 ? 129  SER D CA  1 
ATOM   2957 C  C   . SER D 2 9   ? 5.12531   -0.29511  -39.23207 1.000 107.29332 ? 129  SER D C   1 
ATOM   2958 O  O   . SER D 2 9   ? 4.45439   -0.07577  -38.21910 1.000 98.93868  ? 129  SER D O   1 
ATOM   2959 C  CB  . SER D 2 9   ? 3.52758   -0.49139  -41.15576 1.000 109.35959 ? 129  SER D CB  1 
ATOM   2960 O  OG  . SER D 2 9   ? 4.02591   0.70921   -41.71963 1.000 106.30984 ? 129  SER D OG  1 
ATOM   2961 N  N   . GLU D 2 10  ? 6.33515   0.23431   -39.43062 1.000 98.46832  ? 130  GLU D N   1 
ATOM   2962 C  CA  . GLU D 2 10  ? 6.93014   1.15713   -38.47201 1.000 93.50438  ? 130  GLU D CA  1 
ATOM   2963 C  C   . GLU D 2 10  ? 6.38558   2.56981   -38.59741 1.000 88.89856  ? 130  GLU D C   1 
ATOM   2964 O  O   . GLU D 2 10  ? 6.73106   3.42189   -37.77215 1.000 87.88580  ? 130  GLU D O   1 
ATOM   2965 C  CB  . GLU D 2 10  ? 8.45327   1.20439   -38.62912 1.000 100.39045 ? 130  GLU D CB  1 
ATOM   2966 C  CG  . GLU D 2 10  ? 9.19106   -0.02307  -38.12689 1.000 105.21754 ? 130  GLU D CG  1 
ATOM   2967 C  CD  . GLU D 2 10  ? 10.69716  0.18042   -38.09381 1.000 111.96466 ? 130  GLU D CD  1 
ATOM   2968 O  OE1 . GLU D 2 10  ? 11.13684  1.31729   -37.81807 1.000 111.69024 ? 130  GLU D OE1 1 
ATOM   2969 O  OE2 . GLU D 2 10  ? 11.43957  -0.79259  -38.34919 1.000 117.94540 ? 130  GLU D OE2 1 
ATOM   2970 N  N   . GLU D 2 11  ? 5.56699   2.84383   -39.60943 1.000 86.52994  ? 131  GLU D N   1 
ATOM   2971 C  CA  . GLU D 2 11  ? 5.00826   4.16719   -39.83143 1.000 82.35795  ? 131  GLU D CA  1 
ATOM   2972 C  C   . GLU D 2 11  ? 3.52460   4.04302   -40.15062 1.000 77.19388  ? 131  GLU D C   1 
ATOM   2973 O  O   . GLU D 2 11  ? 2.99222   2.94779   -40.35038 1.000 77.42589  ? 131  GLU D O   1 
ATOM   2974 C  CB  . GLU D 2 11  ? 5.73319   4.90563   -40.97050 1.000 89.65915  ? 131  GLU D CB  1 
ATOM   2975 C  CG  . GLU D 2 11  ? 7.26081   4.90991   -40.87856 1.000 95.51656  ? 131  GLU D CG  1 
ATOM   2976 C  CD  . GLU D 2 11  ? 7.79426   5.72639   -39.70995 1.000 93.03701  ? 131  GLU D CD  1 
ATOM   2977 O  OE1 . GLU D 2 11  ? 7.01368   6.48605   -39.09530 1.000 89.66082  ? 131  GLU D OE1 1 
ATOM   2978 O  OE2 . GLU D 2 11  ? 9.00118   5.60414   -39.40556 1.000 97.25765  ? 131  GLU D OE2 1 
ATOM   2979 N  N   . GLY D 2 12  ? 2.85506   5.18489   -40.19227 1.000 72.87483  ? 132  GLY D N   1 
ATOM   2980 C  CA  . GLY D 2 12  ? 1.47374   5.23016   -40.62293 1.000 68.41135  ? 132  GLY D CA  1 
ATOM   2981 C  C   . GLY D 2 12  ? 0.50471   5.40531   -39.47040 1.000 63.41613  ? 132  GLY D C   1 
ATOM   2982 O  O   . GLY D 2 12  ? 0.87297   5.54417   -38.29974 1.000 63.21205  ? 132  GLY D O   1 
ATOM   2983 N  N   . TYR D 2 13  ? -0.77687  5.39853   -39.84140 1.000 59.78252  ? 133  TYR D N   1 
ATOM   2984 C  CA  . TYR D 2 13  ? -1.87276  5.69047   -38.92690 1.000 55.15951  ? 133  TYR D CA  1 
ATOM   2985 C  C   . TYR D 2 13  ? -3.00033  4.67268   -39.05735 1.000 53.83091  ? 133  TYR D C   1 
ATOM   2986 O  O   . TYR D 2 13  ? -4.11185  4.91992   -38.58981 1.000 50.21198  ? 133  TYR D O   1 
ATOM   2987 C  CB  . TYR D 2 13  ? -2.38918  7.11422   -39.16791 1.000 51.84503  ? 133  TYR D CB  1 
ATOM   2988 C  CG  . TYR D 2 13  ? -1.36714  8.16179   -38.79846 1.000 53.13775  ? 133  TYR D CG  1 
ATOM   2989 C  CD1 . TYR D 2 13  ? -0.36126  8.53219   -39.68649 1.000 56.51934  ? 133  TYR D CD1 1 
ATOM   2990 C  CD2 . TYR D 2 13  ? -1.39017  8.76234   -37.54655 1.000 51.62339  ? 133  TYR D CD2 1 
ATOM   2991 C  CE1 . TYR D 2 13  ? 0.58623   9.47663   -39.33682 1.000 58.25783  ? 133  TYR D CE1 1 
ATOM   2992 C  CE2 . TYR D 2 13  ? -0.45154  9.70391   -37.18776 1.000 53.37039  ? 133  TYR D CE2 1 
ATOM   2993 C  CZ  . TYR D 2 13  ? 0.53482   10.05994  -38.08188 1.000 56.64537  ? 133  TYR D CZ  1 
ATOM   2994 O  OH  . TYR D 2 13  ? 1.46645   11.00093  -37.71375 1.000 58.84757  ? 133  TYR D OH  1 
ATOM   2995 N  N   . GLN D 2 14  ? -2.73020  3.51440   -39.66161 1.000 57.22102  ? 134  GLN D N   1 
ATOM   2996 C  CA  . GLN D 2 14  ? -3.79309  2.54086   -39.87510 1.000 56.61075  ? 134  GLN D CA  1 
ATOM   2997 C  C   . GLN D 2 14  ? -4.45484  2.12081   -38.56803 1.000 54.43295  ? 134  GLN D C   1 
ATOM   2998 O  O   . GLN D 2 14  ? -5.66132  1.86157   -38.54557 1.000 52.30001  ? 134  GLN D O   1 
ATOM   2999 C  CB  . GLN D 2 14  ? -3.24337  1.31934   -40.60873 1.000 61.52013  ? 134  GLN D CB  1 
ATOM   3000 C  CG  . GLN D 2 14  ? -4.31911  0.35467   -41.02752 1.000 61.65837  ? 134  GLN D CG  1 
ATOM   3001 C  CD  . GLN D 2 14  ? -3.79614  -0.73129  -41.94648 1.000 67.09931  ? 134  GLN D CD  1 
ATOM   3002 O  OE1 . GLN D 2 14  ? -4.57109  -1.44593  -42.57814 1.000 70.60555  ? 134  GLN D OE1 1 
ATOM   3003 N  NE2 . GLN D 2 14  ? -2.47383  -0.85985  -42.02350 1.000 71.01298  ? 134  GLN D NE2 1 
ATOM   3004 N  N   . ASP D 2 15  ? -3.68878  2.04864   -37.47662 1.000 55.35531  ? 135  ASP D N   1 
ATOM   3005 C  CA  . ASP D 2 15  ? -4.20333  1.69391   -36.15843 1.000 53.86035  ? 135  ASP D CA  1 
ATOM   3006 C  C   . ASP D 2 15  ? -4.17544  2.88227   -35.20268 1.000 51.36886  ? 135  ASP D C   1 
ATOM   3007 O  O   . ASP D 2 15  ? -4.02044  2.70463   -33.99249 1.000 51.63287  ? 135  ASP D O   1 
ATOM   3008 C  CB  . ASP D 2 15  ? -3.40298  0.54027   -35.55601 1.000 57.45442  ? 135  ASP D CB  1 
ATOM   3009 C  CG  . ASP D 2 15  ? -3.28419  -0.64091  -36.49652 1.000 63.27351  ? 135  ASP D CG  1 
ATOM   3010 O  OD1 . ASP D 2 15  ? -4.22412  -0.85955  -37.28935 1.000 64.39312  ? 135  ASP D OD1 1 
ATOM   3011 O  OD2 . ASP D 2 15  ? -2.25109  -1.34659  -36.44258 1.000 66.45475  ? 135  ASP D OD2 1 
ATOM   3012 N  N   . TYR D 2 16  ? -4.30407  4.09717   -35.73516 1.000 49.36357  ? 136  TYR D N   1 
ATOM   3013 C  CA  . TYR D 2 16  ? -4.14567  5.29472   -34.92060 1.000 47.77363  ? 136  TYR D CA  1 
ATOM   3014 C  C   . TYR D 2 16  ? -5.10727  5.27612   -33.74145 1.000 45.67599  ? 136  TYR D C   1 
ATOM   3015 O  O   . TYR D 2 16  ? -6.31475  5.11574   -33.91901 1.000 43.54742  ? 136  TYR D O   1 
ATOM   3016 C  CB  . TYR D 2 16  ? -4.40096  6.53107   -35.77677 1.000 45.76023  ? 136  TYR D CB  1 
ATOM   3017 C  CG  . TYR D 2 16  ? -4.36081  7.84218   -35.02761 1.000 44.25764  ? 136  TYR D CG  1 
ATOM   3018 C  CD1 . TYR D 2 16  ? -3.17202  8.32032   -34.47845 1.000 46.62342  ? 136  TYR D CD1 1 
ATOM   3019 C  CD2 . TYR D 2 16  ? -5.50672  8.62817   -34.90695 1.000 40.97290  ? 136  TYR D CD2 1 
ATOM   3020 C  CE1 . TYR D 2 16  ? -3.12878  9.52865   -33.81548 1.000 45.83224  ? 136  TYR D CE1 1 
ATOM   3021 C  CE2 . TYR D 2 16  ? -5.47093  9.83830   -34.24294 1.000 40.12902  ? 136  TYR D CE2 1 
ATOM   3022 C  CZ  . TYR D 2 16  ? -4.28265  10.28580  -33.70208 1.000 42.59008  ? 136  TYR D CZ  1 
ATOM   3023 O  OH  . TYR D 2 16  ? -4.24926  11.49480  -33.04061 1.000 42.29064  ? 136  TYR D OH  1 
ATOM   3024 N  N   . GLU D 2 17  ? -4.56243  5.43300   -32.52997 1.000 46.79683  ? 137  GLU D N   1 
ATOM   3025 C  CA  . GLU D 2 17  ? -5.40401  5.49442   -31.34120 1.000 45.50784  ? 137  GLU D CA  1 
ATOM   3026 C  C   . GLU D 2 17  ? -5.63081  6.94115   -30.90897 1.000 43.90862  ? 137  GLU D C   1 
ATOM   3027 O  O   . GLU D 2 17  ? -4.69862  7.74541   -30.93749 1.000 45.02665  ? 137  GLU D O   1 
ATOM   3028 C  CB  . GLU D 2 17  ? -4.75744  4.72860   -30.18369 1.000 48.19871  ? 137  GLU D CB  1 
ATOM   3029 C  CG  . GLU D 2 17  ? -4.47024  3.26815   -30.49208 1.000 50.30556  ? 137  GLU D CG  1 
ATOM   3030 C  CD  . GLU D 2 17  ? -3.72851  2.58275   -29.35195 1.000 53.19968  ? 137  GLU D CD  1 
ATOM   3031 O  OE1 . GLU D 2 17  ? -4.31645  2.44087   -28.25847 1.000 52.93173  ? 137  GLU D OE1 1 
ATOM   3032 O  OE2 . GLU D 2 17  ? -2.55490  2.22082   -29.55580 1.000 56.05357  ? 137  GLU D OE2 1 
ATOM   3033 N  N   . PRO D 2 18  ? -6.85260  7.29526   -30.45671 1.000 41.82216  ? 138  PRO D N   1 
ATOM   3034 C  CA  . PRO D 2 18  ? -7.08332  8.64747   -29.91633 1.000 40.94106  ? 138  PRO D CA  1 
ATOM   3035 C  C   . PRO D 2 18  ? -6.23255  8.97468   -28.69664 1.000 44.24490  ? 138  PRO D C   1 
ATOM   3036 O  O   . PRO D 2 18  ? -5.53925  8.09729   -28.17179 1.000 45.81758  ? 138  PRO D O   1 
ATOM   3037 C  CB  . PRO D 2 18  ? -8.56770  8.62915   -29.52940 1.000 39.22841  ? 138  PRO D CB  1 
ATOM   3038 C  CG  . PRO D 2 18  ? -9.16761  7.46095   -30.26898 1.000 38.57601  ? 138  PRO D CG  1 
ATOM   3039 C  CD  . PRO D 2 18  ? -8.06593  6.46053   -30.42873 1.000 40.77535  ? 138  PRO D CD  1 
ATOM   3040 N  N   . GLU D 2 19  ? -6.40498  10.19864  -28.17774 1.000 57.37116  ? 139  GLU D N   1 
ATOM   3041 C  CA  . GLU D 2 19  ? -5.70539  10.88830  -27.06678 1.000 48.74057  ? 139  GLU D CA  1 
ATOM   3042 C  C   . GLU D 2 19  ? -4.44105  11.57596  -27.57473 1.000 65.56231  ? 139  GLU D C   1 
ATOM   3043 O  O   . GLU D 2 19  ? -3.71986  12.17643  -26.77298 1.000 90.98750  ? 139  GLU D O   1 
ATOM   3044 C  CB  . GLU D 2 19  ? -5.35416  9.95366   -25.88854 1.000 65.83349  ? 139  GLU D CB  1 
ATOM   3045 C  CG  . GLU D 2 19  ? -4.87491  10.61982  -24.59644 1.000 73.84143  ? 139  GLU D CG  1 
ATOM   3046 C  CD  . GLU D 2 19  ? -5.84711  11.65021  -24.04750 1.000 85.17216  ? 139  GLU D CD  1 
ATOM   3047 O  OE1 . GLU D 2 19  ? -7.04200  11.32636  -23.89312 1.000 92.11740  ? 139  GLU D OE1 1 
ATOM   3048 O  OE2 . GLU D 2 19  ? -5.41534  12.78852  -23.77084 1.000 92.60103  ? 139  GLU D OE2 1 
ATOM   3049 N  N   . ALA D 2 20  ? -4.19036  11.55843  -28.88075 1.000 59.90739  ? 140  ALA D N   1 
ATOM   3050 C  CA  . ALA D 2 20  ? -3.07336  12.24084  -29.54499 1.000 49.70295  ? 140  ALA D CA  1 
ATOM   3051 C  C   . ALA D 2 20  ? -1.73874  11.55563  -29.30064 1.000 54.02045  ? 140  ALA D C   1 
ATOM   3052 O  O   . ALA D 2 20  ? -0.96892  11.44574  -30.24900 1.000 52.62626  ? 140  ALA D O   1 
ATOM   3053 C  CB  . ALA D 2 20  ? -2.98344  13.71506  -29.12209 1.000 60.51683  ? 140  ALA D CB  1 
ATOM   3054 O  OXT . ALA D 2 20  ? -1.39976  11.12547  -28.18990 1.000 53.74260  ? 140  ALA D OXT 1 
HETATM 3055 CL CL  . CL  E 3 .   ? -2.56084  -3.85992  28.33662  1.000 59.08758  ? 1201 CL  A CL  1 
HETATM 3056 CL CL  . CL  F 3 .   ? 10.16774  -17.97708 0.72425   1.000 34.28299  ? 1201 CL  B CL  1 
HETATM 3057 O  O   . HOH G 4 .   ? -0.95057  -10.99555 11.64217  1.000 56.56421  ? 1301 HOH A O   1 
HETATM 3058 O  O   . HOH G 4 .   ? 10.536    8.322     21.692    1.000 41.95140  ? 1302 HOH A O   1 
HETATM 3059 O  O   . HOH G 4 .   ? -18.46750 1.37758   3.42701   1.000 64.03756  ? 1303 HOH A O   1 
HETATM 3060 O  O   . HOH G 4 .   ? 0.70852   -10.19553 1.60226   1.000 47.02384  ? 1304 HOH A O   1 
HETATM 3061 O  O   . HOH G 4 .   ? 7.23674   2.81366   29.24079  1.000 43.19921  ? 1305 HOH A O   1 
HETATM 3062 O  O   . HOH G 4 .   ? -15.73000 -7.03071  27.97543  1.000 35.78607  ? 1306 HOH A O   1 
HETATM 3063 O  O   . HOH G 4 .   ? -7.15937  -8.82018  26.94125  1.000 47.34988  ? 1307 HOH A O   1 
HETATM 3064 O  O   . HOH G 4 .   ? 11.37640  5.14462   33.16627  1.000 38.81632  ? 1308 HOH A O   1 
HETATM 3065 O  O   . HOH G 4 .   ? -15.48402 3.98893   11.84208  1.000 40.47508  ? 1309 HOH A O   1 
HETATM 3066 O  O   . HOH G 4 .   ? 3.47718   9.02576   22.20311  1.000 48.33854  ? 1310 HOH A O   1 
HETATM 3067 O  O   . HOH G 4 .   ? -16.74285 2.10557   17.80891  1.000 46.04104  ? 1311 HOH A O   1 
HETATM 3068 O  O   . HOH G 4 .   ? -10.59145 9.15760   17.83302  1.000 47.84015  ? 1312 HOH A O   1 
HETATM 3069 O  O   . HOH G 4 .   ? -10.80514 -16.76835 25.18037  1.000 41.28974  ? 1313 HOH A O   1 
HETATM 3070 O  O   . HOH G 4 .   ? 2.55717   6.40985   29.36052  1.000 47.13460  ? 1314 HOH A O   1 
HETATM 3071 O  O   . HOH G 4 .   ? -9.89178  -15.66280 21.48281  1.000 34.87486  ? 1315 HOH A O   1 
HETATM 3072 O  O   . HOH G 4 .   ? 7.90321   2.23594   18.01143  1.000 42.86990  ? 1316 HOH A O   1 
HETATM 3073 O  O   . HOH G 4 .   ? 5.89532   7.52948   22.17049  1.000 38.98539  ? 1317 HOH A O   1 
HETATM 3074 O  O   . HOH G 4 .   ? 6.08244   1.00836   16.35771  1.000 40.86387  ? 1318 HOH A O   1 
HETATM 3075 O  O   . HOH G 4 .   ? -6.66784  0.36124   -6.12069  1.000 52.53165  ? 1319 HOH A O   1 
HETATM 3076 O  O   . HOH G 4 .   ? -5.14953  -9.48965  8.10522   1.000 42.15360  ? 1320 HOH A O   1 
HETATM 3077 O  O   . HOH G 4 .   ? -13.45235 1.42329   27.33815  1.000 38.44433  ? 1321 HOH A O   1 
HETATM 3078 O  O   . HOH G 4 .   ? -18.18091 -2.29699  19.67518  1.000 44.60379  ? 1322 HOH A O   1 
HETATM 3079 O  O   . HOH G 4 .   ? 5.43081   -4.71678  2.69049   1.000 39.60735  ? 1323 HOH A O   1 
HETATM 3080 O  O   . HOH G 4 .   ? -12.45556 8.10914   6.43820   1.000 54.97841  ? 1324 HOH A O   1 
HETATM 3081 O  O   . HOH G 4 .   ? -16.12441 -5.45176  25.67921  1.000 33.85088  ? 1325 HOH A O   1 
HETATM 3082 O  O   . HOH G 4 .   ? -1.84435  -9.89407  5.94953   1.000 39.01234  ? 1326 HOH A O   1 
HETATM 3083 O  O   . HOH G 4 .   ? 7.95688   -2.52609  12.30893  1.000 59.26995  ? 1327 HOH A O   1 
HETATM 3084 O  O   . HOH G 4 .   ? -2.94759  -7.45765  -0.71447  1.000 44.08866  ? 1328 HOH A O   1 
HETATM 3085 O  O   . HOH G 4 .   ? 2.86460   -9.65232  16.54881  1.000 48.58146  ? 1329 HOH A O   1 
HETATM 3086 O  O   . HOH G 4 .   ? -5.23571  -12.50896 16.47373  1.000 51.40688  ? 1330 HOH A O   1 
HETATM 3087 O  O   . HOH G 4 .   ? -1.31590  5.21657   -4.22448  1.000 46.71267  ? 1331 HOH A O   1 
HETATM 3088 O  O   . HOH G 4 .   ? 1.04977   -8.58507  19.87302  1.000 37.66988  ? 1332 HOH A O   1 
HETATM 3089 O  O   . HOH G 4 .   ? -19.26944 -2.28636  17.30575  1.000 52.25172  ? 1333 HOH A O   1 
HETATM 3090 O  O   . HOH G 4 .   ? 0.71295   -5.10658  -1.25326  1.000 36.69657  ? 1334 HOH A O   1 
HETATM 3091 O  O   . HOH G 4 .   ? 4.17599   2.60426   0.76961   1.000 45.26251  ? 1335 HOH A O   1 
HETATM 3092 O  O   . HOH G 4 .   ? 8.104     9.833     21.452    1.000 49.08381  ? 1336 HOH A O   1 
HETATM 3093 O  O   . HOH G 4 .   ? -9.17414  -2.11690  -3.15072  1.000 48.98589  ? 1337 HOH A O   1 
HETATM 3094 O  O   . HOH G 4 .   ? -18.95593 -5.13571  22.62249  1.000 36.48630  ? 1338 HOH A O   1 
HETATM 3095 O  O   . HOH G 4 .   ? -12.90581 1.49970   30.10634  1.000 46.68855  ? 1339 HOH A O   1 
HETATM 3096 O  O   . HOH G 4 .   ? 3.66723   -8.72414  11.14398  1.000 39.83490  ? 1340 HOH A O   1 
HETATM 3097 O  O   . HOH G 4 .   ? -10.20571 -6.05457  5.18182   1.000 46.30090  ? 1341 HOH A O   1 
HETATM 3098 O  O   . HOH G 4 .   ? -16.16269 -1.57888  14.56859  1.000 41.20830  ? 1342 HOH A O   1 
HETATM 3099 O  O   . HOH G 4 .   ? 9.90829   16.81322  1.13967   1.000 71.29035  ? 1343 HOH A O   1 
HETATM 3100 O  O   . HOH G 4 .   ? -13.21120 -6.91659  7.68806   1.000 40.86558  ? 1344 HOH A O   1 
HETATM 3101 O  O   . HOH G 4 .   ? 3.93661   3.41865   13.88510  1.000 38.65666  ? 1345 HOH A O   1 
HETATM 3102 O  O   . HOH G 4 .   ? 1.46515   -6.47159  21.67805  1.000 39.21500  ? 1346 HOH A O   1 
HETATM 3103 O  O   . HOH G 4 .   ? 0.20506   2.87485   -3.75656  1.000 54.15572  ? 1347 HOH A O   1 
HETATM 3104 O  O   . HOH G 4 .   ? -15.37070 -5.20426  7.98474   1.000 36.35441  ? 1348 HOH A O   1 
HETATM 3105 O  O   . HOH G 4 .   ? -9.27155  1.37464   32.47315  1.000 40.23650  ? 1349 HOH A O   1 
HETATM 3106 O  O   . HOH G 4 .   ? 1.53412   22.91073  5.63819   1.000 67.32333  ? 1350 HOH A O   1 
HETATM 3107 O  O   . HOH G 4 .   ? -1.16190  12.14516  25.17682  1.000 47.47655  ? 1351 HOH A O   1 
HETATM 3108 O  O   . HOH G 4 .   ? -4.39500  18.29241  17.37722  1.000 55.13252  ? 1352 HOH A O   1 
HETATM 3109 O  O   . HOH G 4 .   ? -11.591   -14.493   30.029    1.000 51.93271  ? 1353 HOH A O   1 
HETATM 3110 O  O   . HOH G 4 .   ? -16.10280 -5.40460  30.18826  1.000 43.74048  ? 1354 HOH A O   1 
HETATM 3111 O  O   . HOH G 4 .   ? -3.82616  -11.05784 19.37271  1.000 34.84476  ? 1355 HOH A O   1 
HETATM 3112 O  O   . HOH G 4 .   ? -1.84082  -2.22821  -1.89021  1.000 47.33130  ? 1356 HOH A O   1 
HETATM 3113 O  O   . HOH G 4 .   ? -19.08868 -2.26250  25.68411  1.000 56.60807  ? 1357 HOH A O   1 
HETATM 3114 O  O   . HOH G 4 .   ? -3.36467  -6.90381  -3.27847  1.000 50.13411  ? 1358 HOH A O   1 
HETATM 3115 O  O   . HOH G 4 .   ? 1.31908   10.45862  25.60202  1.000 53.32986  ? 1359 HOH A O   1 
HETATM 3116 O  O   . HOH G 4 .   ? 4.094     -6.881    22.250    1.000 40.59932  ? 1360 HOH A O   1 
HETATM 3117 O  O   . HOH G 4 .   ? -23.633   -1.991    18.307    1.000 40.78739  ? 1361 HOH A O   1 
HETATM 3118 O  O   . HOH G 4 .   ? 3.34818   6.84273   -4.75170  1.000 57.87040  ? 1362 HOH A O   1 
HETATM 3119 O  O   . HOH G 4 .   ? -9.79345  -9.43869  31.17187  1.000 50.47321  ? 1363 HOH A O   1 
HETATM 3120 O  O   . HOH G 4 .   ? 6.52699   -11.43319 5.81082   1.000 43.13488  ? 1364 HOH A O   1 
HETATM 3121 O  O   . HOH G 4 .   ? 4.28397   7.96110   -10.58589 1.000 57.80748  ? 1365 HOH A O   1 
HETATM 3122 O  O   . HOH G 4 .   ? -8.74992  -11.38902 20.72577  1.000 26.97953  ? 1366 HOH A O   1 
HETATM 3123 O  O   . HOH G 4 .   ? -2.46951  -2.09829  32.54944  1.000 52.89731  ? 1367 HOH A O   1 
HETATM 3124 O  O   . HOH G 4 .   ? 1.63427   -0.68479  -1.90515  1.000 51.08646  ? 1368 HOH A O   1 
HETATM 3125 O  O   . HOH G 4 .   ? -7.70380  -9.55218  29.30285  1.000 47.59798  ? 1369 HOH A O   1 
HETATM 3126 O  O   . HOH G 4 .   ? -12.98390 -3.16698  5.43138   1.000 56.36590  ? 1370 HOH A O   1 
HETATM 3127 O  O   . HOH G 4 .   ? 7.45833   -3.93528  8.87342   1.000 53.84641  ? 1371 HOH A O   1 
HETATM 3128 O  O   . HOH G 4 .   ? -9.60797  19.03918  11.67372  1.000 58.68561  ? 1372 HOH A O   1 
HETATM 3129 O  O   . HOH G 4 .   ? -20.67972 -13.51769 24.98261  1.000 38.57568  ? 1373 HOH A O   1 
HETATM 3130 O  O   . HOH G 4 .   ? -20.186   -3.928    20.611    1.000 41.43345  ? 1374 HOH A O   1 
HETATM 3131 O  O   . HOH G 4 .   ? -10.197   -13.823   19.589    1.000 39.69367  ? 1375 HOH A O   1 
HETATM 3132 O  O   . HOH G 4 .   ? 0.09458   -0.86745  -4.11968  1.000 61.41667  ? 1376 HOH A O   1 
HETATM 3133 O  O   . HOH G 4 .   ? -22.563   -2.804    20.712    1.000 44.52925  ? 1377 HOH A O   1 
HETATM 3134 O  O   . HOH G 4 .   ? -18.40749 -2.44160  28.88532  1.000 56.80182  ? 1378 HOH A O   1 
HETATM 3135 O  O   . HOH G 4 .   ? 2.71222   -10.60346 20.53912  1.000 50.96903  ? 1379 HOH A O   1 
HETATM 3136 O  O   . HOH G 4 .   ? 1.49340   -10.44954 10.86612  1.000 48.67786  ? 1380 HOH A O   1 
HETATM 3137 O  O   . HOH G 4 .   ? -8.94127  9.42260   3.14881   1.000 55.37076  ? 1381 HOH A O   1 
HETATM 3138 O  O   . HOH H 4 .   ? -2.27640  -4.26460  -5.55231  1.000 56.56154  ? 1301 HOH B O   1 
HETATM 3139 O  O   . HOH H 4 .   ? -0.87840  -12.42203 -13.34459 1.000 45.51000  ? 1302 HOH B O   1 
HETATM 3140 O  O   . HOH H 4 .   ? 23.186    -10.168   -23.241   1.000 42.58130  ? 1303 HOH B O   1 
HETATM 3141 O  O   . HOH H 4 .   ? 6.80090   -4.01864  0.54504   1.000 40.65837  ? 1304 HOH B O   1 
HETATM 3142 O  O   . HOH H 4 .   ? 3.54135   -11.63095 0.77785   1.000 54.33929  ? 1305 HOH B O   1 
HETATM 3143 O  O   . HOH H 4 .   ? 22.32477  -13.68291 -24.65161 1.000 45.30361  ? 1306 HOH B O   1 
HETATM 3144 O  O   . HOH H 4 .   ? 16.19801  -24.97081 -6.59148  1.000 40.51447  ? 1307 HOH B O   1 
HETATM 3145 O  O   . HOH H 4 .   ? 9.91829   8.51943   -25.05336 1.000 42.25456  ? 1308 HOH B O   1 
HETATM 3146 O  O   . HOH H 4 .   ? 12.86961  -24.96990 -1.11181  1.000 52.40426  ? 1309 HOH B O   1 
HETATM 3147 O  O   . HOH H 4 .   ? 9.903     -32.337   -13.194   1.000 41.54786  ? 1310 HOH B O   1 
HETATM 3148 O  O   . HOH H 4 .   ? 5.83109   -11.56752 1.96898   1.000 44.01926  ? 1311 HOH B O   1 
HETATM 3149 O  O   . HOH H 4 .   ? 9.21617   -26.36865 -1.36844  1.000 44.55895  ? 1312 HOH B O   1 
HETATM 3150 O  O   . HOH H 4 .   ? 16.54540  -9.75355  -32.08401 1.000 44.48813  ? 1313 HOH B O   1 
HETATM 3151 O  O   . HOH H 4 .   ? 15.21341  -3.12759  -28.42336 1.000 37.05885  ? 1314 HOH B O   1 
HETATM 3152 O  O   . HOH H 4 .   ? 10.507    -18.240   -24.273   1.000 40.96983  ? 1315 HOH B O   1 
HETATM 3153 O  O   . HOH H 4 .   ? 11.32021  0.65540   -7.63600  1.000 47.66968  ? 1316 HOH B O   1 
HETATM 3154 O  O   . HOH H 4 .   ? -4.62796  -2.72484  -19.76440 1.000 50.76150  ? 1317 HOH B O   1 
HETATM 3155 O  O   . HOH H 4 .   ? 12.338    -17.756   -22.611   1.000 33.68526  ? 1318 HOH B O   1 
HETATM 3156 O  O   . HOH H 4 .   ? -1.13383  -21.61988 -1.94099  1.000 39.36903  ? 1319 HOH B O   1 
HETATM 3157 O  O   . HOH H 4 .   ? 20.04773  -19.21919 -16.79261 1.000 35.65989  ? 1320 HOH B O   1 
HETATM 3158 O  O   . HOH H 4 .   ? -0.19825  -21.35001 -4.58328  1.000 40.63339  ? 1321 HOH B O   1 
HETATM 3159 O  O   . HOH H 4 .   ? 12.04349  -6.15626  7.44675   1.000 50.76086  ? 1322 HOH B O   1 
HETATM 3160 O  O   . HOH H 4 .   ? 14.00814  -25.86369 -5.43239  1.000 45.91722  ? 1323 HOH B O   1 
HETATM 3161 O  O   . HOH H 4 .   ? 13.42042  -3.04935  4.59002   1.000 48.92481  ? 1324 HOH B O   1 
HETATM 3162 O  O   . HOH H 4 .   ? -3.51238  -24.45656 0.51920   1.000 56.55348  ? 1325 HOH B O   1 
HETATM 3163 O  O   . HOH H 4 .   ? 21.24927  -16.96042 -17.99103 1.000 42.99536  ? 1326 HOH B O   1 
HETATM 3164 O  O   . HOH H 4 .   ? -3.10812  -16.50861 -10.31466 1.000 37.87254  ? 1327 HOH B O   1 
HETATM 3165 O  O   . HOH H 4 .   ? 14.873    0.230     -17.169   1.000 43.37970  ? 1328 HOH B O   1 
HETATM 3166 O  O   . HOH H 4 .   ? 22.82431  -12.76103 -10.66351 1.000 38.18267  ? 1329 HOH B O   1 
HETATM 3167 O  O   . HOH H 4 .   ? 15.02749  -3.99725  -3.83060  1.000 45.15075  ? 1330 HOH B O   1 
HETATM 3168 O  O   . HOH H 4 .   ? 13.35943  -4.82789  -9.86784  1.000 36.47594  ? 1331 HOH B O   1 
HETATM 3169 O  O   . HOH H 4 .   ? 19.18508  -5.58698  -0.50950  1.000 42.70750  ? 1332 HOH B O   1 
HETATM 3170 O  O   . HOH H 4 .   ? 17.97061  -9.41452  5.32694   1.000 55.12606  ? 1333 HOH B O   1 
HETATM 3171 O  O   . HOH H 4 .   ? 1.172     -18.884   -19.731   1.000 45.36319  ? 1334 HOH B O   1 
HETATM 3172 O  O   . HOH H 4 .   ? 19.00048  -4.46596  -29.32981 1.000 50.71571  ? 1335 HOH B O   1 
HETATM 3173 O  O   . HOH H 4 .   ? 23.07689  -8.13937  -11.94042 1.000 42.98841  ? 1336 HOH B O   1 
HETATM 3174 O  O   . HOH H 4 .   ? -0.66661  -12.96370 -21.11599 1.000 39.06155  ? 1337 HOH B O   1 
HETATM 3175 O  O   . HOH H 4 .   ? 15.35538  -5.41171  -6.18022  1.000 36.27723  ? 1338 HOH B O   1 
HETATM 3176 O  O   . HOH H 4 .   ? 9.38496   10.78441  -26.56273 1.000 45.73991  ? 1339 HOH B O   1 
HETATM 3177 O  O   . HOH H 4 .   ? 13.07708  -28.31393 -6.19541  1.000 39.31891  ? 1340 HOH B O   1 
HETATM 3178 O  O   . HOH H 4 .   ? 18.13849  -16.20142 -3.71415  1.000 45.51044  ? 1341 HOH B O   1 
HETATM 3179 O  O   . HOH H 4 .   ? 3.06649   11.34415  -29.67857 1.000 44.80852  ? 1342 HOH B O   1 
HETATM 3180 O  O   . HOH H 4 .   ? 4.92243   -10.90715 -28.72310 1.000 47.64695  ? 1343 HOH B O   1 
HETATM 3181 O  O   . HOH H 4 .   ? 4.12502   -34.21119 -4.90785  1.000 50.20783  ? 1344 HOH B O   1 
HETATM 3182 O  O   . HOH H 4 .   ? 12.96075  -16.20511 0.95853   1.000 45.87252  ? 1345 HOH B O   1 
HETATM 3183 O  O   . HOH H 4 .   ? 6.38804   -0.55685  8.90468   1.000 53.18821  ? 1346 HOH B O   1 
HETATM 3184 O  O   . HOH H 4 .   ? 3.45278   -29.33233 -4.12466  1.000 42.66582  ? 1347 HOH B O   1 
HETATM 3185 O  O   . HOH H 4 .   ? -3.32633  -26.18158 -9.26858  1.000 54.99136  ? 1348 HOH B O   1 
HETATM 3186 O  O   . HOH H 4 .   ? 5.98641   3.14959   10.07612  1.000 52.35909  ? 1349 HOH B O   1 
HETATM 3187 O  O   . HOH H 4 .   ? -5.42627  -1.05346  -21.75551 1.000 40.66296  ? 1350 HOH B O   1 
HETATM 3188 O  O   . HOH H 4 .   ? 15.43096  -2.98262  -16.19842 1.000 37.38084  ? 1351 HOH B O   1 
HETATM 3189 O  O   . HOH H 4 .   ? 14.78835  1.14473   -28.27776 1.000 46.96528  ? 1352 HOH B O   1 
HETATM 3190 O  O   . HOH H 4 .   ? 0.69199   -20.81647 -14.41377 1.000 45.01721  ? 1353 HOH B O   1 
HETATM 3191 O  O   . HOH H 4 .   ? 17.52805  -19.47225 -19.47237 1.000 29.39969  ? 1354 HOH B O   1 
HETATM 3192 O  O   . HOH H 4 .   ? 17.46217  -3.82682  -27.19215 1.000 39.63755  ? 1355 HOH B O   1 
HETATM 3193 O  O   . HOH H 4 .   ? 10.59444  -10.00365 7.19617   1.000 46.62956  ? 1356 HOH B O   1 
HETATM 3194 O  O   . HOH H 4 .   ? 0.22661   4.66201   -11.46750 1.000 48.37948  ? 1357 HOH B O   1 
HETATM 3195 O  O   . HOH H 4 .   ? 5.95699   -30.59939 -2.52311  1.000 44.22250  ? 1358 HOH B O   1 
HETATM 3196 O  O   . HOH H 4 .   ? 21.401    -18.948   -14.504   1.000 43.93730  ? 1359 HOH B O   1 
HETATM 3197 O  O   . HOH H 4 .   ? 6.25709   -2.70951  -3.46313  1.000 44.74005  ? 1360 HOH B O   1 
HETATM 3198 O  O   . HOH H 4 .   ? -2.98751  7.77129   -25.77022 1.000 41.59503  ? 1361 HOH B O   1 
HETATM 3199 O  O   . HOH H 4 .   ? -3.29186  -4.32299  -27.68865 1.000 43.97595  ? 1362 HOH B O   1 
HETATM 3200 O  O   . HOH H 4 .   ? -4.74461  5.57565   -25.32770 1.000 36.99171  ? 1363 HOH B O   1 
HETATM 3201 O  O   . HOH H 4 .   ? 7.93111   -17.93089 4.79124   1.000 50.57514  ? 1364 HOH B O   1 
HETATM 3202 O  O   . HOH H 4 .   ? -3.85892  -7.64502  -21.59262 1.000 44.30454  ? 1365 HOH B O   1 
HETATM 3203 O  O   . HOH H 4 .   ? 3.85702   -27.56148 -6.10353  1.000 36.95634  ? 1366 HOH B O   1 
HETATM 3204 O  O   . HOH H 4 .   ? 11.81825  0.03538   -11.70779 1.000 51.76708  ? 1367 HOH B O   1 
HETATM 3205 O  O   . HOH H 4 .   ? 7.68771   -8.12437  -31.09680 1.000 49.52323  ? 1368 HOH B O   1 
HETATM 3206 O  O   . HOH H 4 .   ? 21.59654  -8.85460  -5.36291  1.000 46.25234  ? 1369 HOH B O   1 
HETATM 3207 O  O   . HOH H 4 .   ? 23.77501  -20.24233 -14.51382 1.000 48.37603  ? 1370 HOH B O   1 
HETATM 3208 O  O   . HOH H 4 .   ? -2.72230  3.91050   -20.92820 1.000 49.81290  ? 1371 HOH B O   1 
HETATM 3209 O  O   . HOH H 4 .   ? 17.02694  1.46822   -26.94519 1.000 50.36117  ? 1372 HOH B O   1 
HETATM 3210 O  O   . HOH H 4 .   ? 11.60649  3.73992   -33.50539 1.000 46.64889  ? 1373 HOH B O   1 
HETATM 3211 O  O   . HOH H 4 .   ? 2.82974   7.92875   -37.26294 1.000 52.23344  ? 1374 HOH B O   1 
HETATM 3212 O  O   . HOH H 4 .   ? 8.55074   -2.07612  -1.85636  1.000 48.00155  ? 1375 HOH B O   1 
HETATM 3213 O  O   . HOH H 4 .   ? -5.44405  5.81491   -22.56836 1.000 51.85468  ? 1376 HOH B O   1 
HETATM 3214 O  O   . HOH H 4 .   ? 9.81578   1.67239   -3.59624  1.000 55.23823  ? 1377 HOH B O   1 
HETATM 3215 O  O   . HOH H 4 .   ? 7.637     -20.773   -23.302   1.000 39.64860  ? 1378 HOH B O   1 
HETATM 3216 O  O   . HOH H 4 .   ? -3.12894  -1.85619  -11.75571 1.000 51.45603  ? 1379 HOH B O   1 
HETATM 3217 O  O   . HOH H 4 .   ? -0.12104  7.65413   -20.78731 1.000 45.84133  ? 1380 HOH B O   1 
HETATM 3218 O  O   . HOH H 4 .   ? 6.03287   -6.20474  8.86924   1.000 49.07124  ? 1381 HOH B O   1 
HETATM 3219 O  O   . HOH H 4 .   ? 4.89320   -4.03026  -1.56286  1.000 35.73560  ? 1382 HOH B O   1 
HETATM 3220 O  O   . HOH H 4 .   ? -0.53735  -27.57081 -7.05928  1.000 48.05666  ? 1383 HOH B O   1 
HETATM 3221 O  O   . HOH H 4 .   ? 17.36640  -21.23201 -6.05741  1.000 44.92656  ? 1384 HOH B O   1 
HETATM 3222 O  O   . HOH H 4 .   ? 21.71622  -14.42506 -6.01707  1.000 53.14627  ? 1385 HOH B O   1 
HETATM 3223 O  O   . HOH H 4 .   ? 15.66287  -13.81030 -30.40693 1.000 40.44344  ? 1386 HOH B O   1 
HETATM 3224 O  O   . HOH H 4 .   ? 10.33872  10.86209  -21.19010 1.000 51.70060  ? 1387 HOH B O   1 
HETATM 3225 O  O   . HOH H 4 .   ? -7.00031  -6.23937  -12.21139 1.000 68.05096  ? 1388 HOH B O   1 
HETATM 3226 O  O   . HOH H 4 .   ? 6.67638   -15.97336 -25.52971 1.000 49.16362  ? 1389 HOH B O   1 
HETATM 3227 O  O   . HOH H 4 .   ? 1.11419   0.80720   -33.35025 1.000 36.78758  ? 1390 HOH B O   1 
HETATM 3228 O  O   . HOH H 4 .   ? 19.09330  -21.45594 -8.29426  1.000 37.53908  ? 1391 HOH B O   1 
HETATM 3229 O  O   . HOH H 4 .   ? 18.19753  -13.02195 -0.58803  1.000 42.43314  ? 1392 HOH B O   1 
HETATM 3230 O  O   . HOH H 4 .   ? -2.99666  -7.21603  -26.08936 1.000 53.25964  ? 1393 HOH B O   1 
HETATM 3231 O  O   . HOH H 4 .   ? 19.06342  -8.49296  -32.11113 1.000 49.36044  ? 1394 HOH B O   1 
HETATM 3232 O  O   . HOH H 4 .   ? 0.24309   7.74370   -32.97614 1.000 33.93561  ? 1395 HOH B O   1 
HETATM 3233 O  O   . HOH H 4 .   ? 11.75959  3.66945   5.85647   1.000 56.64436  ? 1396 HOH B O   1 
HETATM 3234 O  O   . HOH H 4 .   ? -1.73487  -10.09209 0.24804   1.000 46.10318  ? 1397 HOH B O   1 
HETATM 3235 O  O   . HOH H 4 .   ? -5.53069  -15.10919 -2.71527  1.000 58.60646  ? 1398 HOH B O   1 
HETATM 3236 O  O   . HOH H 4 .   ? 12.55943  5.32254   -35.64379 1.000 59.95403  ? 1399 HOH B O   1 
HETATM 3237 O  O   . HOH H 4 .   ? -0.92884  8.02757   -24.08605 1.000 48.57657  ? 1400 HOH B O   1 
HETATM 3238 O  O   . HOH H 4 .   ? -5.49842  -5.55886  -20.63213 1.000 53.51475  ? 1401 HOH B O   1 
HETATM 3239 O  O   . HOH H 4 .   ? 5.989     -18.850   -24.617   1.000 51.95400  ? 1402 HOH B O   1 
HETATM 3240 O  O   . HOH H 4 .   ? 4.83849   0.15213   -3.61916  1.000 54.09803  ? 1403 HOH B O   1 
HETATM 3241 O  O   . HOH H 4 .   ? -1.29084  -4.80611  -3.16118  1.000 42.97577  ? 1404 HOH B O   1 
HETATM 3242 O  O   . HOH H 4 .   ? -6.00191  -4.24286  -26.92383 1.000 54.15678  ? 1405 HOH B O   1 
HETATM 3243 O  O   . HOH H 4 .   ? -0.65284  -27.84009 -4.36855  1.000 53.52982  ? 1406 HOH B O   1 
HETATM 3244 O  O   . HOH H 4 .   ? 21.39775  -9.24096  -2.23428  1.000 52.50163  ? 1407 HOH B O   1 
HETATM 3245 O  O   . HOH H 4 .   ? 17.831    -28.537   -4.638    1.000 54.61700  ? 1408 HOH B O   1 
HETATM 3246 O  O   . HOH H 4 .   ? 18.49958  -24.07151 -5.33220  1.000 46.60909  ? 1409 HOH B O   1 
HETATM 3247 O  O   . HOH H 4 .   ? 14.02196  -2.87039  -11.82746 1.000 42.93667  ? 1410 HOH B O   1 
HETATM 3248 O  O   . HOH H 4 .   ? 2.45662   -2.97634  -0.68834  1.000 39.57594  ? 1411 HOH B O   1 
HETATM 3249 O  O   . HOH H 4 .   ? 22.94221  -16.11630 -15.98090 1.000 53.67634  ? 1412 HOH B O   1 
HETATM 3250 O  O   . HOH H 4 .   ? 14.83346  -1.05918  -30.09823 1.000 51.69827  ? 1413 HOH B O   1 
HETATM 3251 O  O   . HOH H 4 .   ? 3.23539   1.53094   -1.52805  1.000 52.77057  ? 1414 HOH B O   1 
HETATM 3252 O  O   . HOH H 4 .   ? 16.59743  -14.63590 -2.17678  1.000 42.49855  ? 1415 HOH B O   1 
HETATM 3253 O  O   . HOH H 4 .   ? -4.79504  1.85349   -20.45664 1.000 53.21962  ? 1416 HOH B O   1 
HETATM 3254 O  O   . HOH H 4 .   ? -2.49823  -14.72277 -12.48504 1.000 49.64179  ? 1417 HOH B O   1 
HETATM 3255 O  O   . HOH H 4 .   ? 16.84785  -12.33207 -32.31471 1.000 50.17670  ? 1418 HOH B O   1 
HETATM 3256 O  O   . HOH H 4 .   ? 22.79487  -12.72845 -7.82849  1.000 50.29504  ? 1419 HOH B O   1 
HETATM 3257 O  O   . HOH H 4 .   ? 13.81664  2.13926   -32.75873 1.000 50.44323  ? 1420 HOH B O   1 
HETATM 3258 O  O   . HOH H 4 .   ? -4.34310  -20.03956 -12.43576 1.000 51.93617  ? 1421 HOH B O   1 
HETATM 3259 O  O   . HOH H 4 .   ? 9.29261   -12.15752 5.66274   1.000 43.50852  ? 1422 HOH B O   1 
HETATM 3260 O  O   . HOH H 4 .   ? 20.65648  -14.24110 -0.26076  1.000 52.23602  ? 1423 HOH B O   1 
HETATM 3261 O  O   . HOH H 4 .   ? 22.75786  -15.72801 -11.29043 1.000 49.54774  ? 1424 HOH B O   1 
HETATM 3262 O  O   . HOH H 4 .   ? 21.64632  -6.66325  -1.16660  1.000 45.89366  ? 1425 HOH B O   1 
HETATM 3263 O  O   . HOH I 4 .   ? 1.157     28.821    24.919    1.000 38.75516  ? 201  HOH C O   1 
HETATM 3264 O  O   . HOH J 4 .   ? -1.80077  11.18559  -25.34033 1.000 55.58067  ? 201  HOH D O   1 
HETATM 3265 O  O   . HOH J 4 .   ? -1.76752  12.54630  -32.55110 1.000 35.37880  ? 202  HOH D O   1 
HETATM 3266 O  O   . HOH J 4 .   ? 3.317     11.417    -39.600   1.000 43.80996  ? 203  HOH D O   1 
HETATM 3267 O  O   . HOH J 4 .   ? 1.08543   9.80663   -30.75675 1.000 50.85316  ? 204  HOH D O   1 
HETATM 3268 O  O   . HOH J 4 .   ? 1.12699   11.81995  -27.51830 1.000 49.34442  ? 205  HOH D O   1 
HETATM 3269 O  O   . HOH J 4 .   ? -6.95711  3.06204   -28.02761 1.000 39.98990  ? 206  HOH D O   1 
HETATM 3270 O  O   . HOH J 4 .   ? -1.496    5.778     -42.449   1.000 42.49754  ? 207  HOH D O   1 
HETATM 3271 O  O   . HOH J 4 .   ? 4.67007   8.02288   -39.24663 1.000 63.88943  ? 208  HOH D O   1 
HETATM 3272 O  O   . HOH J 4 .   ? -6.406    11.797    -31.258   1.000 30.38969  ? 209  HOH D O   1 
HETATM 3273 O  O   . HOH J 4 .   ? 10.65464  6.42587   -37.27949 1.000 53.79574  ? 210  HOH D O   1 
HETATM 3274 O  O   . HOH J 4 .   ? -2.81900  0.90391   -32.04506 1.000 52.88197  ? 211  HOH D O   1 
HETATM 3275 O  O   . HOH J 4 .   ? -6.89631  5.87103   -27.04774 1.000 40.15434  ? 212  HOH D O   1 
HETATM 3276 O  O   . HOH J 4 .   ? -7.66523  2.05696   -40.58123 1.000 37.19123  ? 213  HOH D O   1 
HETATM 3277 O  O   . HOH J 4 .   ? -1.68864  5.24486   -32.49603 1.000 41.08820  ? 214  HOH D O   1 
HETATM 3278 O  O   . HOH J 4 .   ? 0.16896   2.30017   -40.21161 1.000 56.32365  ? 215  HOH D O   1 
HETATM 3279 O  O   . HOH J 4 .   ? 7.77938   2.79480   -35.13186 1.000 52.23518  ? 216  HOH D O   1 
HETATM 3280 O  O   . HOH J 4 .   ? -1.24071  2.99420   -35.92244 1.000 50.46673  ? 217  HOH D O   1 
HETATM 3281 O  O   . HOH J 4 .   ? -0.51907  5.50205   -35.53560 1.000 46.26648  ? 218  HOH D O   1 
HETATM 3282 O  O   . HOH J 4 .   ? 0.71340   14.04869  -29.71037 1.000 48.47120  ? 219  HOH D O   1 
HETATM 3283 O  O   . HOH J 4 .   ? -0.90740  2.63230   -32.63225 1.000 52.90188  ? 220  HOH D O   1 
HETATM 3284 O  O   . HOH J 4 .   ? -1.42814  14.95471  -26.46160 1.000 58.56962  ? 221  HOH D 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   . LYS A 3   ? 1.10589 0.85822 1.24470 0.16055  -0.05697 -0.03970 35   LYS A N   
2    C CA  . LYS A 3   ? 1.24851 0.96440 1.39068 0.16615  -0.05690 -0.04325 35   LYS A CA  
3    C C   . LYS A 3   ? 1.23550 0.92301 1.36071 0.14843  -0.05394 -0.05201 35   LYS A C   
4    O O   . LYS A 3   ? 1.21883 0.86911 1.34256 0.14618  -0.05657 -0.04999 35   LYS A O   
5    C CB  . LYS A 3   ? 1.27799 1.00520 1.43618 0.18508  -0.04822 -0.06213 35   LYS A CB  
6    C CG  . LYS A 3   ? 1.28642 0.97426 1.44943 0.19403  -0.04787 -0.06770 35   LYS A CG  
7    C CD  . LYS A 3   ? 1.25451 0.95668 1.43392 0.21416  -0.03794 -0.08692 35   LYS A CD  
8    C CE  . LYS A 3   ? 1.31445 1.04491 1.48471 0.20860  -0.02473 -0.11007 35   LYS A CE  
9    N NZ  . LYS A 3   ? 1.34331 1.08841 1.52759 0.22703  -0.01299 -0.12933 35   LYS A NZ  
10   N N   . GLU A 4   ? 1.13973 0.84570 1.25305 0.13555  -0.04914 -0.06137 36   GLU A N   
11   C CA  A GLU A 4   ? 1.07446 0.76064 1.17347 0.11781  -0.04750 -0.07003 36   GLU A CA  
12   C CA  B GLU A 4   ? 1.07441 0.76095 1.17331 0.11766  -0.04751 -0.06995 36   GLU A CA  
13   C C   . GLU A 4   ? 1.05092 0.71150 1.14448 0.10281  -0.05580 -0.04887 36   GLU A C   
14   O O   . GLU A 4   ? 1.01395 0.68308 1.10698 0.10080  -0.06138 -0.02860 36   GLU A O   
15   C CB  A GLU A 4   ? 1.00829 0.72341 1.09687 0.10864  -0.04197 -0.08198 36   GLU A CB  
16   C CB  B GLU A 4   ? 1.00817 0.72387 1.09671 0.10829  -0.04226 -0.08098 36   GLU A CB  
17   C CG  A GLU A 4   ? 0.99675 0.75085 1.09154 0.12082  -0.03650 -0.08702 36   GLU A CG  
18   C CG  B GLU A 4   ? 0.98851 0.69080 1.06392 0.09032  -0.04175 -0.09118 36   GLU A CG  
19   C CD  A GLU A 4   ? 0.99786 0.76020 1.10068 0.13624  -0.02803 -0.10469 36   GLU A CD  
20   C CD  B GLU A 4   ? 1.03874 0.73073 1.10944 0.09355  -0.03611 -0.11433 36   GLU A CD  
21   O OE1 A GLU A 4   ? 1.02942 0.76856 1.12743 0.13599  -0.02499 -0.11837 36   GLU A OE1 
22   O OE1 B GLU A 4   ? 1.08236 0.74389 1.15769 0.09826  -0.03741 -0.11627 36   GLU A OE1 
23   O OE2 A GLU A 4   ? 0.96342 0.75621 1.07786 0.14809  -0.02414 -0.10529 36   GLU A OE2 
24   O OE2 B GLU A 4   ? 1.04420 0.75767 1.10492 0.09147  -0.03037 -0.13044 36   GLU A OE2 
25   N N   . SER A 5   ? 0.93323 0.56278 1.02172 0.09094  -0.05639 -0.05345 37   SER A N   
26   C CA  . SER A 5   ? 0.85506 0.45968 0.93949 0.07471  -0.06266 -0.03307 37   SER A CA  
27   C C   . SER A 5   ? 0.87256 0.48659 0.94843 0.05267  -0.06166 -0.03452 37   SER A C   
28   O O   . SER A 5   ? 0.83342 0.44416 0.90581 0.04371  -0.05909 -0.05280 37   SER A O   
29   C CB  . SER A 5   ? 0.92865 0.49125 1.01564 0.07374  -0.06465 -0.03411 37   SER A CB  
30   O OG  . SER A 5   ? 0.97646 0.51720 1.05906 0.05553  -0.06951 -0.01304 37   SER A OG  
31   N N   . TYR A 6   ? 0.74557 0.37165 0.81805 0.04378  -0.06417 -0.01487 38   TYR A N   
32   C CA  . TYR A 6   ? 0.68835 0.32149 0.75639 0.02202  -0.06347 -0.01072 38   TYR A CA  
33   C C   . TYR A 6   ? 0.70651 0.31443 0.77333 0.00417  -0.06611 0.00945  38   TYR A C   
34   O O   . TYR A 6   ? 0.73669 0.35384 0.80207 -0.01511 -0.06467 0.01900  38   TYR A O   
35   C CB  . TYR A 6   ? 0.65820 0.32544 0.72116 0.02210  -0.06108 -0.00225 38   TYR A CB  
36   C CG  . TYR A 6   ? 0.65663 0.35516 0.71873 0.03615  -0.05627 -0.01989 38   TYR A CG  
37   C CD1 . TYR A 6   ? 0.68608 0.39290 0.75233 0.05563  -0.05750 -0.01962 38   TYR A CD1 
38   C CD2 . TYR A 6   ? 0.65288 0.37452 0.71089 0.02892  -0.05104 -0.03501 38   TYR A CD2 
39   C CE1 . TYR A 6   ? 0.71989 0.45708 0.78616 0.06567  -0.05190 -0.03438 38   TYR A CE1 
40   C CE2 . TYR A 6   ? 0.66599 0.41468 0.72109 0.03962  -0.04640 -0.04824 38   TYR A CE2 
41   C CZ  . TYR A 6   ? 0.66922 0.42552 0.72835 0.05697  -0.04597 -0.04803 38   TYR A CZ  
42   O OH  . TYR A 6   ? 0.71931 0.50399 0.77625 0.06485  -0.04022 -0.06010 38   TYR A OH  
43   N N   . ALA A 7   ? 0.72937 0.30703 0.79770 0.00997  -0.06915 0.01687  39   ALA A N   
44   C CA  . ALA A 7   ? 0.77193 0.32663 0.83671 -0.00570 -0.07135 0.04095  39   ALA A CA  
45   C C   . ALA A 7   ? 0.78324 0.33330 0.85001 -0.03158 -0.06860 0.03763  39   ALA A C   
46   O O   . ALA A 7   ? 0.78014 0.33528 0.84378 -0.05072 -0.06656 0.05739  39   ALA A O   
47   C CB  . ALA A 7   ? 0.82258 0.34184 0.89009 0.00614  -0.07552 0.04631  39   ALA A CB  
48   N N   . ILE A 8   ? 0.81973 0.36372 0.89140 -0.03335 -0.06812 0.01264  40   ILE A N   
49   C CA  . ILE A 8   ? 0.80593 0.34807 0.88180 -0.05831 -0.06735 0.00766  40   ILE A CA  
50   C C   . ILE A 8   ? 0.75578 0.33489 0.83441 -0.07305 -0.06438 0.01452  40   ILE A C   
51   O O   . ILE A 8   ? 0.76019 0.34373 0.84386 -0.09609 -0.06213 0.02714  40   ILE A O   
52   C CB  . ILE A 8   ? 0.88437 0.41968 0.96128 -0.05585 -0.06854 -0.02262 40   ILE A CB  
53   C CG1 . ILE A 8   ? 0.91481 0.40818 0.99067 -0.04603 -0.07011 -0.02885 40   ILE A CG1 
54   C CG2 . ILE A 8   ? 0.94334 0.48977 1.02563 -0.08135 -0.06951 -0.03008 40   ILE A CG2 
55   C CD1 . ILE A 8   ? 1.09909 0.55830 1.17752 -0.06170 -0.07176 -0.00988 40   ILE A CD1 
56   N N   . TYR A 9   ? 0.74999 0.35739 0.82690 -0.06010 -0.06338 0.00658  41   TYR A N   
57   C CA  . TYR A 9   ? 0.74880 0.39364 0.82918 -0.07097 -0.05939 0.01050  41   TYR A CA  
58   C C   . TYR A 9   ? 0.72120 0.38229 0.79358 -0.07498 -0.05257 0.03686  41   TYR A C   
59   O O   . TYR A 9   ? 0.70257 0.39325 0.77763 -0.09056 -0.04492 0.04469  41   TYR A O   
60   C CB  . TYR A 9   ? 0.65911 0.33490 0.73460 -0.05374 -0.05694 -0.00892 41   TYR A CB  
61   C CG  . TYR A 9   ? 0.74124 0.39706 0.81880 -0.04777 -0.06327 -0.03463 41   TYR A CG  
62   C CD1 . TYR A 9   ? 0.67217 0.32823 0.75447 -0.06441 -0.06635 -0.04718 41   TYR A CD1 
63   C CD2 . TYR A 9   ? 0.70192 0.34874 0.77264 -0.02548 -0.06252 -0.04544 41   TYR A CD2 
64   C CE1 . TYR A 9   ? 0.74854 0.39455 0.82398 -0.05919 -0.06862 -0.07042 41   TYR A CE1 
65   C CE2 . TYR A 9   ? 0.75313 0.39169 0.81935 -0.01989 -0.06273 -0.06848 41   TYR A CE2 
66   C CZ  . TYR A 9   ? 0.79998 0.43657 0.86630 -0.03695 -0.06591 -0.08107 41   TYR A CZ  
67   O OH  . TYR A 9   ? 0.82697 0.45446 0.88472 -0.03265 -0.06616 -0.10432 41   TYR A OH  
68   N N   . VAL A 10  ? 0.71117 0.35592 0.77389 -0.06083 -0.05526 0.04997  42   VAL A N   
69   C CA  . VAL A 10  ? 0.70479 0.35930 0.75520 -0.06704 -0.05066 0.07629  42   VAL A CA  
70   C C   . VAL A 10  ? 0.71386 0.35165 0.76748 -0.09289 -0.04887 0.09465  42   VAL A C   
71   O O   . VAL A 10  ? 0.72134 0.38694 0.76931 -0.10763 -0.03888 0.10839  42   VAL A O   
72   C CB  . VAL A 10  ? 0.70730 0.34215 0.74819 -0.04813 -0.05813 0.08825  42   VAL A CB  
73   C CG1 . VAL A 10  ? 0.69819 0.33952 0.72149 -0.05683 -0.05548 0.11715  42   VAL A CG1 
74   C CG2 . VAL A 10  ? 0.65835 0.31808 0.69820 -0.02568 -0.05798 0.07134  42   VAL A CG2 
75   N N   . TYR A 11  ? 0.73196 0.33332 0.79219 -0.09690 -0.05429 0.09155  43   TYR A N   
76   C CA  . TYR A 11  ? 0.74380 0.33452 0.80630 -0.12102 -0.05003 0.10613  43   TYR A CA  
77   C C   . TYR A 11  ? 0.77815 0.39999 0.85528 -0.14363 -0.04348 0.09983  43   TYR A C   
78   O O   . TYR A 11  ? 0.74826 0.38625 0.82588 -0.16427 -0.03473 0.11781  43   TYR A O   
79   C CB  . TYR A 11  ? 0.80614 0.35455 0.87268 -0.11891 -0.05574 0.09862  43   TYR A CB  
80   C CG  . TYR A 11  ? 0.85142 0.37993 0.91618 -0.13990 -0.05237 0.11989  43   TYR A CG  
81   C CD1 . TYR A 11  ? 0.89432 0.40796 0.94409 -0.13728 -0.05237 0.14677  43   TYR A CD1 
82   C CD2 . TYR A 11  ? 0.88674 0.41396 0.96470 -0.16337 -0.04941 0.11340  43   TYR A CD2 
83   C CE1 . TYR A 11  ? 0.97041 0.46610 1.01735 -0.15729 -0.04854 0.16695  43   TYR A CE1 
84   C CE2 . TYR A 11  ? 0.88165 0.39176 0.95938 -0.18392 -0.04528 0.13269  43   TYR A CE2 
85   C CZ  . TYR A 11  ? 0.98178 0.47535 1.04340 -0.18072 -0.04434 0.15974  43   TYR A CZ  
86   O OH  . TYR A 11  ? 1.04540 0.52142 1.10533 -0.20158 -0.03974 0.18015  43   TYR A OH  
87   N N   . LYS A 12  ? 0.71703 0.35167 0.80661 -0.13974 -0.04714 0.07443  44   LYS A N   
88   C CA  . LYS A 12  ? 0.74315 0.41193 0.85068 -0.15959 -0.04312 0.06787  44   LYS A CA  
89   C C   . LYS A 12  ? 0.69604 0.41381 0.79978 -0.16096 -0.02957 0.07965  44   LYS A C   
90   O O   . LYS A 12  ? 0.69171 0.43598 0.80725 -0.18169 -0.02072 0.08917  44   LYS A O   
91   C CB  . LYS A 12  ? 0.70609 0.38457 0.82197 -0.15028 -0.05030 0.03844  44   LYS A CB  
92   C CG  . LYS A 12  ? 0.88505 0.52595 0.99709 -0.14548 -0.05822 0.02069  44   LYS A CG  
93   C CD  . LYS A 12  ? 0.91340 0.56638 1.03502 -0.15351 -0.06408 -0.00379 44   LYS A CD  
94   C CE  . LYS A 12  ? 0.91625 0.52768 1.03113 -0.15334 -0.06880 -0.01672 44   LYS A CE  
95   N NZ  . LYS A 12  ? 1.09364 0.68994 1.21764 -0.17834 -0.06746 -0.00637 44   LYS A NZ  
96   N N   . VAL A 13  ? 0.72378 0.45596 0.81130 -0.13854 -0.02666 0.07769  45   VAL A N   
97   C CA  . VAL A 13  ? 0.65091 0.42560 0.73059 -0.13742 -0.01326 0.08611  45   VAL A CA  
98   C C   . VAL A 13  ? 0.66395 0.43311 0.73201 -0.15333 -0.00556 0.11348  45   VAL A C   
99   O O   . VAL A 13  ? 0.70730 0.51218 0.77774 -0.16596 0.00826  0.12114  45   VAL A O   
100  C CB  . VAL A 13  ? 0.62158 0.40630 0.68528 -0.11176 -0.01387 0.07770  45   VAL A CB  
101  C CG1 . VAL A 13  ? 0.61707 0.43827 0.66893 -0.11091 -0.00065 0.08576  45   VAL A CG1 
102  C CG2 . VAL A 13  ? 0.61616 0.41204 0.69005 -0.09926 -0.01907 0.05280  45   VAL A CG2 
103  N N   . LEU A 14  ? 0.68775 0.41287 0.74291 -0.15252 -0.01402 0.12913  46   LEU A N   
104  C CA  . LEU A 14  ? 0.71848 0.43555 0.75816 -0.16856 -0.00808 0.15855  46   LEU A CA  
105  C C   . LEU A 14  ? 0.76351 0.49195 0.81993 -0.19890 0.00092  0.16782  46   LEU A C   
106  O O   . LEU A 14  ? 0.83559 0.59000 0.88278 -0.21355 0.01509  0.18499  46   LEU A O   
107  C CB  . LEU A 14  ? 0.79606 0.46102 0.82301 -0.16095 -0.02100 0.17300  46   LEU A CB  
108  C CG  . LEU A 14  ? 0.79659 0.45363 0.80460 -0.17384 -0.01478 0.20076  46   LEU A CG  
109  C CD1 . LEU A 14  ? 0.83589 0.52767 0.81941 -0.17647 -0.00440 0.21624  46   LEU A CD1 
110  C CD2 . LEU A 14  ? 0.81928 0.43031 0.81765 -0.15975 -0.02729 0.20996  46   LEU A CD2 
111  N N   . LYS A 15  ? 0.79767 0.51318 0.87725 -0.20644 -0.00521 0.15277  47   LYS A N   
112  C CA  . LYS A 15  ? 0.81948 0.55172 0.91638 -0.23202 0.00403  0.15700  47   LYS A CA  
113  C C   . LYS A 15  ? 0.80316 0.59485 0.91945 -0.24260 0.01653  0.15181  47   LYS A C   
114  O O   . LYS A 15  ? 0.85081 0.66892 0.97953 -0.26278 0.02914  0.15975  47   LYS A O   
115  C CB  . LYS A 15  ? 0.79874 0.50033 0.91226 -0.23731 -0.00684 0.14101  47   LYS A CB  
116  C CG  . LYS A 15  ? 0.94801 0.59446 1.04627 -0.23280 -0.01396 0.15077  47   LYS A CG  
117  C CD  . LYS A 15  ? 0.94381 0.58784 1.01895 -0.23517 -0.00574 0.18049  47   LYS A CD  
118  C CE  . LYS A 15  ? 1.03759 0.63045 1.10148 -0.23474 -0.01196 0.19445  47   LYS A CE  
119  N NZ  . LYS A 15  ? 1.09708 0.69648 1.14338 -0.24796 -0.00129 0.22428  47   LYS A NZ  
120  N N   . GLN A 16  ? 0.78887 0.60746 0.90665 -0.22205 0.01601  0.13331  48   GLN A N   
121  C CA  . GLN A 16  ? 0.74358 0.62202 0.87705 -0.22269 0.03015  0.12495  48   GLN A CA  
122  C C   . GLN A 16  ? 0.74887 0.65344 0.86229 -0.22390 0.04837  0.14106  48   GLN A C   
123  O O   . GLN A 16  ? 0.81228 0.75759 0.94014 -0.23956 0.06449  0.14663  48   GLN A O   
124  C CB  . GLN A 16  ? 0.77517 0.67097 0.91275 -0.19741 0.02423  0.09997  48   GLN A CB  
125  C CG  . GLN A 16  ? 0.75783 0.64211 0.91534 -0.19766 0.00872  0.08108  48   GLN A CG  
126  C CD  . GLN A 16  ? 0.80499 0.70487 0.96036 -0.17282 0.00344  0.06023  48   GLN A CD  
127  O OE1 . GLN A 16  ? 0.75616 0.65579 0.89078 -0.15319 0.00672  0.05953  48   GLN A OE1 
128  N NE2 . GLN A 16  ? 0.84993 0.76377 1.02608 -0.17510 -0.00561 0.04406  48   GLN A NE2 
129  N N   . VAL A 17  ? 0.78641 0.67054 0.86675 -0.20793 0.04625  0.14796  49   VAL A N   
130  C CA  . VAL A 17  ? 0.76324 0.67426 0.81955 -0.20712 0.06252  0.15895  49   VAL A CA  
131  C C   . VAL A 17  ? 0.79682 0.69319 0.83509 -0.23039 0.06934  0.18893  49   VAL A C   
132  O O   . VAL A 17  ? 0.79359 0.72320 0.81946 -0.24023 0.08790  0.19877  49   VAL A O   
133  C CB  . VAL A 17  ? 0.75470 0.65731 0.78296 -0.18092 0.05682  0.15196  49   VAL A CB  
134  C CG1 . VAL A 17  ? 0.68330 0.60150 0.72774 -0.15992 0.05173  0.12462  49   VAL A CG1 
135  C CG2 . VAL A 17  ? 0.73826 0.58927 0.74627 -0.17521 0.04002  0.16554  49   VAL A CG2 
136  N N   . HIS A 18  ? 0.87092 0.71732 0.90649 -0.23948 0.05525  0.20380  50   HIS A N   
137  C CA  . HIS A 18  ? 0.85860 0.68745 0.87695 -0.25260 0.06055  0.22634  50   HIS A CA  
138  C C   . HIS A 18  ? 0.88649 0.67862 0.92594 -0.26275 0.05053  0.22551  50   HIS A C   
139  O O   . HIS A 18  ? 0.85713 0.59968 0.88680 -0.25365 0.03534  0.23006  50   HIS A O   
140  C CB  . HIS A 18  ? 0.88535 0.68687 0.86419 -0.23888 0.05299  0.24260  50   HIS A CB  
141  C CG  . HIS A 18  ? 0.88447 0.72305 0.83570 -0.23367 0.06533  0.24526  50   HIS A CG  
142  N ND1 . HIS A 18  ? 0.87082 0.74561 0.80920 -0.24713 0.08629  0.25404  50   HIS A ND1 
143  C CD2 . HIS A 18  ? 0.83585 0.68164 0.76948 -0.21468 0.06041  0.23639  50   HIS A CD2 
144  C CE1 . HIS A 18  ? 0.89705 0.79822 0.80884 -0.23755 0.09371  0.25019  50   HIS A CE1 
145  N NE2 . HIS A 18  ? 0.81248 0.69635 0.72080 -0.21831 0.07785  0.23972  50   HIS A NE2 
146  N N   . PRO A 19  ? 0.91662 0.73366 0.98611 -0.28144 0.05925  0.21885  51   PRO A N   
147  C CA  . PRO A 19  ? 0.92379 0.70794 1.01503 -0.29178 0.04863  0.21256  51   PRO A CA  
148  C C   . PRO A 19  ? 0.99701 0.73243 1.07107 -0.29815 0.04422  0.23240  51   PRO A C   
149  O O   . PRO A 19  ? 1.01325 0.70627 1.09645 -0.29806 0.03104  0.22531  51   PRO A O   
150  C CB  . PRO A 19  ? 0.89887 0.73025 1.02320 -0.31278 0.06212  0.20605  51   PRO A CB  
151  C CG  . PRO A 19  ? 0.92112 0.80805 1.04959 -0.30472 0.07413  0.19837  51   PRO A CG  
152  C CD  . PRO A 19  ? 0.89001 0.76938 0.97830 -0.29152 0.07833  0.21283  51   PRO A CD  
153  N N   . ASP A 20  ? 0.97254 0.71254 1.02121 -0.30357 0.05495  0.25641  52   ASP A N   
154  C CA  . ASP A 20  ? 1.11698 0.81317 1.15033 -0.31160 0.05137  0.27827  52   ASP A CA  
155  C C   . ASP A 20  ? 1.10557 0.76957 1.10437 -0.29124 0.04052  0.29269  52   ASP A C   
156  O O   . ASP A 20  ? 1.08401 0.72043 1.06382 -0.29679 0.03968  0.31592  52   ASP A O   
157  C CB  . ASP A 20  ? 1.18009 0.90327 1.21164 -0.33641 0.07102  0.29741  52   ASP A CB  
158  C CG  . ASP A 20  ? 1.17730 0.93082 1.24781 -0.35766 0.08054  0.28492  52   ASP A CG  
159  O OD1 . ASP A 20  ? 1.17473 0.90385 1.26909 -0.36041 0.06827  0.26953  52   ASP A OD1 
160  O OD2 . ASP A 20  ? 1.25166 1.05505 1.32928 -0.37099 0.10033  0.28936  52   ASP A OD2 
161  N N   . THR A 21  ? 1.02296 0.69039 1.01457 -0.26794 0.03142  0.27995  53   THR A N   
162  C CA  . THR A 21  ? 1.03154 0.67619 0.99369 -0.24736 0.02039  0.29195  53   THR A CA  
163  C C   . THR A 21  ? 0.94508 0.54785 0.91786 -0.22561 0.00078  0.27737  53   THR A C   
164  O O   . THR A 21  ? 1.04951 0.66028 1.04137 -0.21672 -0.00346 0.25290  53   THR A O   
165  C CB  . THR A 21  ? 0.99601 0.68237 0.93812 -0.23769 0.02716  0.29024  53   THR A CB  
166  O OG1 . THR A 21  ? 1.01087 0.73605 0.94022 -0.25625 0.04739  0.30262  53   THR A OG1 
167  C CG2 . THR A 21  ? 1.03369 0.69920 0.94781 -0.21613 0.01329  0.30077  53   THR A CG2 
168  N N   . GLY A 22  ? 1.06627 0.62590 1.02690 -0.21623 -0.01058 0.29203  54   GLY A N   
169  C CA  . GLY A 22  ? 1.08222 0.60476 1.05198 -0.19245 -0.02734 0.27850  54   GLY A CA  
170  C C   . GLY A 22  ? 1.01026 0.54363 0.96549 -0.16664 -0.03597 0.27685  54   GLY A C   
171  O O   . GLY A 22  ? 0.97302 0.54110 0.90899 -0.16758 -0.02991 0.28517  54   GLY A O   
172  N N   . ILE A 23  ? 0.98112 0.48560 0.94644 -0.14326 -0.04970 0.26432  55   ILE A N   
173  C CA  . ILE A 23  ? 0.98869 0.50051 0.94512 -0.11701 -0.05973 0.26249  55   ILE A CA  
174  C C   . ILE A 23  ? 1.09196 0.56155 1.05611 -0.09651 -0.07324 0.26278  55   ILE A C   
175  O O   . ILE A 23  ? 1.09619 0.53578 1.07913 -0.09571 -0.07501 0.24824  55   ILE A O   
176  C CB  . ILE A 23  ? 0.93498 0.47551 0.90330 -0.10623 -0.05883 0.23612  55   ILE A CB  
177  C CG1 . ILE A 23  ? 0.88372 0.43791 0.84132 -0.08235 -0.06794 0.23718  55   ILE A CG1 
178  C CG2 . ILE A 23  ? 0.94775 0.46842 0.94231 -0.09966 -0.06197 0.20847  55   ILE A CG2 
179  C CD1 . ILE A 23  ? 0.89143 0.47392 0.85815 -0.07217 -0.06686 0.21400  55   ILE A CD1 
180  N N   . SER A 24  ? 0.99352 0.46158 0.94265 -0.08062 -0.08257 0.27956  56   SER A N   
181  C CA  . SER A 24  ? 1.06735 0.49897 1.02562 -0.05933 -0.09516 0.28145  56   SER A CA  
182  C C   . SER A 24  ? 0.97508 0.40964 0.95572 -0.03466 -0.10005 0.25174  56   SER A C   
183  O O   . SER A 24  ? 0.97474 0.44107 0.96022 -0.03233 -0.09575 0.23300  56   SER A O   
184  C CB  . SER A 24  ? 1.20614 0.64019 1.14367 -0.04890 -0.10496 0.30802  56   SER A CB  
185  O OG  . SER A 24  ? 1.05607 0.52420 0.99059 -0.03122 -0.11048 0.30069  56   SER A OG  
186  N N   . SER A 25  ? 1.13511 0.53591 1.12913 -0.01584 -0.10841 0.24795  57   SER A N   
187  C CA  . SER A 25  ? 1.05857 0.46182 1.07369 0.00886  -0.11144 0.21997  57   SER A CA  
188  C C   . SER A 25  ? 0.91051 0.35144 0.92367 0.02806  -0.11707 0.21951  57   SER A C   
189  O O   . SER A 25  ? 0.88157 0.34705 0.90649 0.03834  -0.11411 0.19536  57   SER A O   
190  C CB  . SER A 25  ? 1.13787 0.49627 1.16648 0.02469  -0.11786 0.21835  57   SER A CB  
191  O OG  . SER A 25  ? 1.24547 0.60340 1.29440 0.04305  -0.11612 0.18665  57   SER A OG  
192  N N   . LYS A 26  ? 1.05141 0.49833 1.04902 0.03225  -0.12553 0.24601  58   LYS A N   
193  C CA  . LYS A 26  ? 1.04323 0.52680 1.03927 0.04940  -0.13253 0.24596  58   LYS A CA  
194  C C   . LYS A 26  ? 0.98224 0.50583 0.96503 0.03569  -0.12532 0.24046  58   LYS A C   
195  O O   . LYS A 26  ? 0.89557 0.44912 0.88648 0.04859  -0.12674 0.22518  58   LYS A O   
196  C CB  . LYS A 26  ? 1.09943 0.57914 1.08016 0.05603  -0.14495 0.27595  58   LYS A CB  
197  C CG  . LYS A 26  ? 1.22502 0.66765 1.22258 0.07557  -0.15388 0.28044  58   LYS A CG  
198  C CD  . LYS A 26  ? 1.33102 0.78014 1.31964 0.08993  -0.16906 0.30524  58   LYS A CD  
199  C CE  . LYS A 26  ? 1.28396 0.68860 1.28653 0.10589  -0.17730 0.31475  58   LYS A CE  
200  N NZ  . LYS A 26  ? 1.38866 0.79276 1.37768 0.11509  -0.19287 0.34533  58   LYS A NZ  
201  N N   . ALA A 27  ? 0.98119 0.50623 0.94486 0.00936  -0.11656 0.25211  59   ALA A N   
202  C CA  . ALA A 27  ? 0.87244 0.43333 0.82472 -0.00390 -0.10788 0.24550  59   ALA A CA  
203  C C   . ALA A 27  ? 0.84049 0.40740 0.81475 -0.00143 -0.10098 0.21488  59   ALA A C   
204  O O   . ALA A 27  ? 0.80219 0.39912 0.77596 0.00146  -0.09869 0.20283  59   ALA A O   
205  C CB  . ALA A 27  ? 0.90019 0.46398 0.82934 -0.03247 -0.09761 0.26420  59   ALA A CB  
206  N N   . MET A 28  ? 0.78899 0.32730 0.78082 -0.00320 -0.09793 0.20166  60   MET A N   
207  C CA  . MET A 28  ? 0.81150 0.35665 0.82176 0.00017  -0.09245 0.17116  60   MET A CA  
208  C C   . MET A 28  ? 0.75169 0.31112 0.77569 0.02715  -0.09770 0.15326  60   MET A C   
209  O O   . MET A 28  ? 0.77400 0.35618 0.80497 0.03070  -0.09339 0.13273  60   MET A O   
210  C CB  . MET A 28  ? 0.84088 0.35253 0.86392 -0.00771 -0.08920 0.15973  60   MET A CB  
211  C CG  . MET A 28  ? 0.85151 0.37002 0.89037 -0.00320 -0.08477 0.12707  60   MET A CG  
212  S SD  . MET A 28  ? 0.80450 0.35784 0.83991 -0.02408 -0.07583 0.11952  60   MET A SD  
213  C CE  . MET A 28  ? 0.86416 0.39900 0.89721 -0.05522 -0.07020 0.13367  60   MET A CE  
214  N N   . SER A 29  ? 0.84638 0.39487 0.87559 0.04630  -0.10659 0.16107  61   SER A N   
215  C CA  . SER A 29  ? 0.82989 0.39832 0.87501 0.07131  -0.11027 0.14502  61   SER A CA  
216  C C   . SER A 29  ? 0.79745 0.40657 0.83396 0.07247  -0.11216 0.14776  61   SER A C   
217  O O   . SER A 29  ? 0.79794 0.43127 0.84682 0.08385  -0.10971 0.12741  61   SER A O   
218  C CB  . SER A 29  ? 0.86739 0.41887 0.92174 0.09113  -0.11981 0.15552  61   SER A CB  
219  O OG  . SER A 29  ? 0.95408 0.46744 1.02008 0.09460  -0.11742 0.14617  61   SER A OG  
220  N N   . ILE A 30  ? 0.76407 0.38144 0.77746 0.05997  -0.11600 0.17255  62   ILE A N   
221  C CA  . ILE A 30  ? 0.77059 0.42424 0.77050 0.05764  -0.11773 0.17553  62   ILE A CA  
222  C C   . ILE A 30  ? 0.68292 0.34939 0.68106 0.04483  -0.10705 0.15937  62   ILE A C   
223  O O   . ILE A 30  ? 0.69922 0.40112 0.69894 0.05055  -0.10249 0.14279  62   ILE A O   
224  C CB  . ILE A 30  ? 0.79007 0.44831 0.75988 0.04507  -0.12280 0.20511  62   ILE A CB  
225  C CG1 . ILE A 30  ? 0.80486 0.45495 0.77842 0.06152  -0.13603 0.21997  62   ILE A CG1 
226  C CG2 . ILE A 30  ? 0.74605 0.43938 0.69369 0.03574  -0.12159 0.20724  62   ILE A CG2 
227  C CD1 . ILE A 30  ? 0.88730 0.53967 0.82953 0.05020  -0.14191 0.24903  62   ILE A CD1 
228  N N   . MET A 31  ? 0.69679 0.34580 0.69122 0.02593  -0.09814 0.15987  63   MET A N   
229  C CA  . MET A 31  ? 0.65822 0.33087 0.65394 0.01470  -0.08338 0.13858  63   MET A CA  
230  C C   . MET A 31  ? 0.66111 0.34010 0.67832 0.03044  -0.08183 0.10971  63   MET A C   
231  O O   . MET A 31  ? 0.64525 0.35775 0.66175 0.03109  -0.07349 0.09261  63   MET A O   
232  C CB  . MET A 31  ? 0.72440 0.37675 0.71992 -0.00714 -0.07641 0.14334  63   MET A CB  
233  C CG  . MET A 31  ? 0.73109 0.39567 0.70412 -0.02939 -0.06858 0.16443  63   MET A CG  
234  S SD  . MET A 31  ? 0.75876 0.47579 0.71066 -0.02940 -0.05939 0.15997  63   MET A SD  
235  C CE  . MET A 31  ? 0.64916 0.39329 0.61703 -0.03468 -0.04462 0.13073  63   MET A CE  
236  N N   . ASN A 32  ? 0.69988 0.34643 0.73517 0.04295  -0.08886 0.10356  64   ASN A N   
237  C CA  . ASN A 32  ? 0.71225 0.36655 0.76473 0.05709  -0.08502 0.07475  64   ASN A CA  
238  C C   . ASN A 32  ? 0.64496 0.33222 0.70244 0.07451  -0.08694 0.06814  64   ASN A C   
239  O O   . ASN A 32  ? 0.62162 0.33467 0.68333 0.07776  -0.07889 0.04706  64   ASN A O   
240  C CB  . ASN A 32  ? 0.69930 0.32599 0.76389 0.06627  -0.08529 0.06603  64   ASN A CB  
241  C CG  . ASN A 32  ? 0.81267 0.44797 0.88962 0.07753  -0.07886 0.03572  64   ASN A CG  
242  O OD1 . ASN A 32  ? 0.77316 0.41189 0.84784 0.06666  -0.07286 0.01986  64   ASN A OD1 
243  N ND2 . ASN A 32  ? 0.78283 0.42419 0.87239 0.09878  -0.07987 0.02810  64   ASN A ND2 
244  N N   . SER A 33  ? 0.72312 0.41377 0.77960 0.08443  -0.09709 0.08629  65   SER A N   
245  C CA  A SER A 33  ? 0.70460 0.43122 0.76806 0.09873  -0.09955 0.08051  65   SER A CA  
246  C CA  B SER A 33  ? 0.70390 0.43050 0.76733 0.09874  -0.09961 0.08064  65   SER A CA  
247  C C   . SER A 33  ? 0.64723 0.41183 0.69274 0.08507  -0.09060 0.07651  65   SER A C   
248  O O   . SER A 33  ? 0.64537 0.44002 0.69793 0.09117  -0.08598 0.06092  65   SER A O   
249  C CB  A SER A 33  ? 0.71011 0.43646 0.77569 0.11006  -0.11322 0.10156  65   SER A CB  
250  C CB  B SER A 33  ? 0.71044 0.43698 0.77573 0.10995  -0.11336 0.10189  65   SER A CB  
251  O OG  A SER A 33  ? 0.72204 0.42335 0.80122 0.12091  -0.11388 0.10092  65   SER A OG  
252  O OG  B SER A 33  ? 0.73783 0.46283 0.77741 0.09526  -0.11959 0.12707  65   SER A OG  
253  N N   . PHE A 34  ? 0.63039 0.39385 0.65325 0.06643  -0.08727 0.09015  66   PHE A N   
254  C CA  . PHE A 34  ? 0.61715 0.41325 0.62456 0.05498  -0.07765 0.08355  66   PHE A CA  
255  C C   . PHE A 34  ? 0.56023 0.36628 0.57642 0.05266  -0.06601 0.06023  66   PHE A C   
256  O O   . PHE A 34  ? 0.56888 0.40247 0.58450 0.05404  -0.06105 0.04839  66   PHE A O   
257  C CB  . PHE A 34  ? 0.63261 0.42676 0.61562 0.03624  -0.07353 0.10000  66   PHE A CB  
258  C CG  . PHE A 34  ? 0.70168 0.52662 0.67054 0.02659  -0.06283 0.09097  66   PHE A CG  
259  C CD1 . PHE A 34  ? 0.73689 0.58577 0.69339 0.02896  -0.06658 0.09220  66   PHE A CD1 
260  C CD2 . PHE A 34  ? 0.71846 0.54850 0.68862 0.01599  -0.05004 0.07986  66   PHE A CD2 
261  C CE1 . PHE A 34  ? 0.65133 0.52395 0.59530 0.02084  -0.05673 0.08170  66   PHE A CE1 
262  C CE2 . PHE A 34  ? 0.66639 0.52244 0.62666 0.00997  -0.04050 0.07075  66   PHE A CE2 
263  C CZ  . PHE A 34  ? 0.73573 0.61067 0.68204 0.01242  -0.04338 0.07131  66   PHE A CZ  
264  N N   . VAL A 35  ? 0.54939 0.33266 0.57269 0.04781  -0.06261 0.05424  67   VAL A N   
265  C CA  . VAL A 35  ? 0.53703 0.33039 0.56631 0.04491  -0.05380 0.03351  67   VAL A CA  
266  C C   . VAL A 35  ? 0.49758 0.30419 0.53931 0.06071  -0.05385 0.01679  67   VAL A C   
267  O O   . VAL A 35  ? 0.51127 0.34150 0.55138 0.05934  -0.04709 0.00449  67   VAL A O   
268  C CB  . VAL A 35  ? 0.57413 0.34024 0.60926 0.03617  -0.05289 0.02945  67   VAL A CB  
269  C CG1 . VAL A 35  ? 0.55539 0.33456 0.59490 0.03380  -0.04640 0.00841  67   VAL A CG1 
270  C CG2 . VAL A 35  ? 0.56435 0.32407 0.58938 0.01784  -0.05041 0.04613  67   VAL A CG2 
271  N N   . ASN A 36  ? 0.53219 0.32407 0.58762 0.07607  -0.06092 0.01650  68   ASN A N   
272  C CA  . ASN A 36  ? 0.52505 0.33415 0.59479 0.09159  -0.05906 0.00052  68   ASN A CA  
273  C C   . ASN A 36  ? 0.50931 0.35439 0.57696 0.09315  -0.05869 0.00358  68   ASN A C   
274  O O   . ASN A 36  ? 0.50664 0.37537 0.57878 0.09574  -0.05206 -0.01015 68   ASN A O   
275  C CB  . ASN A 36  ? 0.51126 0.29920 0.60001 0.11007  -0.06651 -0.00001 68   ASN A CB  
276  C CG  . ASN A 36  ? 0.68575 0.44079 0.78007 0.11153  -0.06442 -0.01418 68   ASN A CG  
277  O OD1 . ASN A 36  ? 0.74954 0.51490 0.84651 0.11483  -0.05581 -0.03525 68   ASN A OD1 
278  N ND2 . ASN A 36  ? 0.79257 0.51497 0.88305 0.10475  -0.06903 -0.00160 68   ASN A ND2 
279  N N   . ASP A 37  ? 0.51342 0.36255 0.57310 0.09046  -0.06628 0.02175  69   ASP A N   
280  C CA  . ASP A 37  ? 0.51849 0.40022 0.57514 0.08985  -0.06772 0.02369  69   ASP A CA  
281  C C   . ASP A 37  ? 0.48024 0.37858 0.52301 0.07619  -0.05741 0.01509  69   ASP A C   
282  O O   . ASP A 37  ? 0.43019 0.35303 0.47728 0.07696  -0.05419 0.00642  69   ASP A O   
283  C CB  . ASP A 37  ? 0.54913 0.43009 0.59447 0.08758  -0.07911 0.04461  69   ASP A CB  
284  C CG  . ASP A 37  ? 0.68663 0.55747 0.74969 0.10451  -0.09252 0.05517  69   ASP A CG  
285  O OD1 . ASP A 37  ? 0.60459 0.47443 0.69209 0.11998  -0.09185 0.04363  69   ASP A OD1 
286  O OD2 . ASP A 37  ? 0.73647 0.60040 0.78868 0.10305  -0.10395 0.07551  69   ASP A OD2 
287  N N   . VAL A 38  ? 0.44161 0.32730 0.46974 0.06355  -0.05228 0.01810  70   VAL A N   
288  C CA  . VAL A 38  ? 0.37447 0.27424 0.39294 0.05314  -0.04304 0.01002  70   VAL A CA  
289  C C   . VAL A 38  ? 0.39911 0.30396 0.42727 0.05642  -0.03688 -0.00604 70   VAL A C   
290  O O   . VAL A 38  ? 0.39899 0.32152 0.42516 0.05380  -0.03213 -0.01306 70   VAL A O   
291  C CB  . VAL A 38  ? 0.43974 0.32877 0.44562 0.04049  -0.03840 0.01657  70   VAL A CB  
292  C CG1 . VAL A 38  ? 0.44073 0.34431 0.44212 0.03325  -0.02922 0.00692  70   VAL A CG1 
293  C CG2 . VAL A 38  ? 0.50262 0.39050 0.49311 0.03535  -0.04266 0.03277  70   VAL A CG2 
294  N N   . PHE A 39  ? 0.42067 0.30829 0.45725 0.06109  -0.03711 -0.01193 71   PHE A N   
295  C CA  . PHE A 39  ? 0.43615 0.32915 0.47784 0.06414  -0.03172 -0.02782 71   PHE A CA  
296  C C   . PHE A 39  ? 0.39486 0.31129 0.44431 0.07228  -0.02980 -0.03380 71   PHE A C   
297  O O   . PHE A 39  ? 0.41612 0.34878 0.46163 0.06817  -0.02389 -0.04056 71   PHE A O   
298  C CB  . PHE A 39  ? 0.42837 0.29760 0.47748 0.06970  -0.03356 -0.03538 71   PHE A CB  
299  C CG  . PHE A 39  ? 0.45965 0.33535 0.51043 0.07366  -0.02802 -0.05348 71   PHE A CG  
300  C CD1 . PHE A 39  ? 0.50039 0.39071 0.56099 0.08616  -0.02496 -0.06239 71   PHE A CD1 
301  C CD2 . PHE A 39  ? 0.52409 0.39324 0.56676 0.06461  -0.02604 -0.06163 71   PHE A CD2 
302  C CE1 . PHE A 39  ? 0.52108 0.41933 0.57930 0.08868  -0.01807 -0.07915 71   PHE A CE1 
303  C CE2 . PHE A 39  ? 0.56149 0.43719 0.60053 0.06718  -0.02165 -0.07807 71   PHE A CE2 
304  C CZ  . PHE A 39  ? 0.51377 0.40348 0.55866 0.07888  -0.01678 -0.08682 71   PHE A CZ  
305  N N   . GLU A 40  ? 0.42582 0.34541 0.48799 0.08349  -0.03526 -0.03000 72   GLU A N   
306  C CA  A GLU A 40  ? 0.42029 0.36674 0.49552 0.09117  -0.03301 -0.03609 72   GLU A CA  
307  C CA  B GLU A 40  ? 0.41875 0.36518 0.49395 0.09115  -0.03296 -0.03617 72   GLU A CA  
308  C C   . GLU A 40  ? 0.40213 0.37098 0.47029 0.08115  -0.03215 -0.03157 72   GLU A C   
309  O O   . GLU A 40  ? 0.39878 0.38857 0.47108 0.07936  -0.02609 -0.03863 72   GLU A O   
310  C CB  A GLU A 40  ? 0.44649 0.39450 0.54134 0.10643  -0.04084 -0.03162 72   GLU A CB  
311  C CB  B GLU A 40  ? 0.44783 0.39550 0.54281 0.10660  -0.04065 -0.03200 72   GLU A CB  
312  C CG  A GLU A 40  ? 0.48463 0.41557 0.59322 0.12064  -0.03912 -0.04250 72   GLU A CG  
313  C CG  B GLU A 40  ? 0.48707 0.41364 0.59370 0.11968  -0.03946 -0.04193 72   GLU A CG  
314  C CD  A GLU A 40  ? 0.50391 0.45183 0.61714 0.12406  -0.02705 -0.06157 72   GLU A CD  
315  C CD  B GLU A 40  ? 0.53026 0.45732 0.66105 0.13844  -0.04741 -0.03806 72   GLU A CD  
316  O OE1 A GLU A 40  ? 0.52584 0.50391 0.63904 0.11856  -0.02131 -0.06345 72   GLU A OE1 
317  O OE1 B GLU A 40  ? 0.55993 0.50296 0.69686 0.14010  -0.05641 -0.02451 72   GLU A OE1 
318  O OE2 A GLU A 40  ? 0.60965 0.53972 0.72494 0.13116  -0.02319 -0.07481 72   GLU A OE2 
319  O OE2 B GLU A 40  ? 0.60325 0.51442 0.74726 0.15209  -0.04540 -0.04924 72   GLU A OE2 
320  N N   . ARG A 41  ? 0.37279 0.33679 0.42914 0.07360  -0.03767 -0.02024 73   ARG A N   
321  C CA  . ARG A 41  ? 0.33191 0.31385 0.38086 0.06405  -0.03715 -0.01885 73   ARG A CA  
322  C C   . ARG A 41  ? 0.36752 0.34840 0.40623 0.05479  -0.02822 -0.02568 73   ARG A C   
323  O O   . ARG A 41  ? 0.35172 0.34802 0.39206 0.05012  -0.02485 -0.02963 73   ARG A O   
324  C CB  . ARG A 41  ? 0.41495 0.39207 0.44973 0.05802  -0.04428 -0.00754 73   ARG A CB  
325  C CG  . ARG A 41  ? 0.46609 0.46065 0.49357 0.04884  -0.04577 -0.00840 73   ARG A CG  
326  C CD  . ARG A 41  ? 0.45467 0.47375 0.49919 0.05332  -0.05336 -0.00785 73   ARG A CD  
327  N NE  . ARG A 41  ? 0.41762 0.45295 0.46043 0.04252  -0.05148 -0.01366 73   ARG A NE  
328  C CZ  . ARG A 41  ? 0.46682 0.50364 0.49376 0.03198  -0.05601 -0.01255 73   ARG A CZ  
329  N NH1 . ARG A 41  ? 0.44121 0.46853 0.45040 0.03057  -0.06218 -0.00514 73   ARG A NH1 
330  N NH2 . ARG A 41  ? 0.41238 0.45887 0.43932 0.02154  -0.05378 -0.01940 73   ARG A NH2 
331  N N   . ILE A 42  ? 0.35802 0.32123 0.38785 0.05161  -0.02511 -0.02610 74   ILE A N   
332  C CA  . ILE A 42  ? 0.35171 0.31485 0.37426 0.04468  -0.01875 -0.03103 74   ILE A CA  
333  C C   . ILE A 42  ? 0.35841 0.33087 0.38638 0.04745  -0.01422 -0.03923 74   ILE A C   
334  O O   . ILE A 42  ? 0.35789 0.33893 0.38205 0.04193  -0.01049 -0.04068 74   ILE A O   
335  C CB  . ILE A 42  ? 0.37103 0.31840 0.38771 0.04109  -0.01754 -0.02966 74   ILE A CB  
336  C CG1 . ILE A 42  ? 0.39157 0.33418 0.40024 0.03622  -0.01890 -0.02134 74   ILE A CG1 
337  C CG2 . ILE A 42  ? 0.36973 0.31940 0.38280 0.03649  -0.01314 -0.03425 74   ILE A CG2 
338  C CD1 . ILE A 42  ? 0.41374 0.34490 0.42063 0.03147  -0.01669 -0.01868 74   ILE A CD1 
339  N N   . ALA A 43  ? 0.37245 0.34181 0.40791 0.05565  -0.01400 -0.04482 75   ALA A N   
340  C CA  . ALA A 43  ? 0.37406 0.35357 0.41064 0.05782  -0.00783 -0.05433 75   ALA A CA  
341  C C   . ALA A 43  ? 0.38727 0.39132 0.43209 0.05762  -0.00433 -0.05443 75   ALA A C   
342  O O   . ALA A 43  ? 0.36555 0.38102 0.40510 0.05211  0.00185  -0.05694 75   ALA A O   
343  C CB  . ALA A 43  ? 0.35913 0.32875 0.40184 0.06767  -0.00753 -0.06347 75   ALA A CB  
344  N N   . GLY A 44  ? 0.33229 0.34573 0.39010 0.06221  -0.00907 -0.05020 76   GLY A N   
345  C CA  . GLY A 44  ? 0.35448 0.39502 0.42444 0.06042  -0.00702 -0.05002 76   GLY A CA  
346  C C   . GLY A 44  ? 0.35084 0.39551 0.41090 0.04608  -0.00591 -0.04549 76   GLY A C   
347  O O   . GLY A 44  ? 0.34864 0.41156 0.41306 0.04001  -0.00012 -0.04679 76   GLY A O   
348  N N   . GLU A 45  ? 0.32245 0.35021 0.36997 0.04022  -0.01087 -0.04024 77   GLU A N   
349  C CA  . GLU A 45  ? 0.30364 0.32985 0.34223 0.02816  -0.00979 -0.03793 77   GLU A CA  
350  C C   . GLU A 45  ? 0.30417 0.32286 0.33320 0.02428  -0.00330 -0.03906 77   GLU A C   
351  O O   . GLU A 45  ? 0.31521 0.33917 0.34240 0.01559  -0.00007 -0.03716 77   GLU A O   
352  C CB  . GLU A 45  ? 0.34273 0.35375 0.37018 0.02459  -0.01499 -0.03474 77   GLU A CB  
353  C CG  . GLU A 45  ? 0.35461 0.37389 0.38682 0.02728  -0.02332 -0.03153 77   GLU A CG  
354  C CD  . GLU A 45  ? 0.38536 0.42854 0.43062 0.02296  -0.02722 -0.03182 77   GLU A CD  
355  O OE1 . GLU A 45  ? 0.32844 0.37955 0.37646 0.01371  -0.02331 -0.03411 77   GLU A OE1 
356  O OE2 . GLU A 45  ? 0.38557 0.44142 0.44120 0.02900  -0.03490 -0.02868 77   GLU A OE2 
357  N N   . ALA A 46  ? 0.32335 0.33004 0.34637 0.02979  -0.00237 -0.04128 78   ALA A N   
358  C CA  . ALA A 46  ? 0.36171 0.36371 0.37452 0.02655  0.00132  -0.04160 78   ALA A CA  
359  C C   . ALA A 46  ? 0.35956 0.37943 0.37320 0.02452  0.00801  -0.04385 78   ALA A C   
360  O O   . ALA A 46  ? 0.34700 0.36724 0.35102 0.01700  0.01084  -0.03954 78   ALA A O   
361  C CB  . ALA A 46  ? 0.35709 0.34669 0.36521 0.03180  -0.00058 -0.04509 78   ALA A CB  
362  N N   . SER A 47  ? 0.31778 0.35320 0.34332 0.03148  0.01099  -0.04991 79   SER A N   
363  C CA  . SER A 47  ? 0.33078 0.38914 0.35971 0.03005  0.02003  -0.05357 79   SER A CA  
364  C C   . SER A 47  ? 0.34754 0.42001 0.38086 0.01780  0.02243  -0.04608 79   SER A C   
365  O O   . SER A 47  ? 0.30877 0.39139 0.33443 0.00929  0.02976  -0.04318 79   SER A O   
366  C CB  . SER A 47  ? 0.34519 0.41881 0.39244 0.04256  0.02251  -0.06239 79   SER A CB  
367  O OG  . SER A 47  ? 0.37356 0.47532 0.42782 0.04183  0.03352  -0.06725 79   SER A OG  
368  N N   . ARG A 48  ? 0.31294 0.38590 0.35715 0.01528  0.01594  -0.04262 80   ARG A N   
369  C CA  . ARG A 48  ? 0.26505 0.34826 0.31422 0.00155  0.01649  -0.03685 80   ARG A CA  
370  C C   . ARG A 48  ? 0.27185 0.33294 0.30322 -0.00894 0.01624  -0.02982 80   ARG A C   
371  O O   . ARG A 48  ? 0.28832 0.35552 0.31800 -0.02132 0.02081  -0.02391 80   ARG A O   
372  C CB  . ARG A 48  ? 0.25377 0.34004 0.31480 0.00061  0.00734  -0.03646 80   ARG A CB  
373  C CG  . ARG A 48  ? 0.27440 0.38555 0.35693 0.01143  0.00575  -0.04064 80   ARG A CG  
374  C CD  . ARG A 48  ? 0.27739 0.39283 0.36884 0.01074  -0.00618 -0.03854 80   ARG A CD  
375  N NE  . ARG A 48  ? 0.27459 0.41224 0.38813 0.02440  -0.00911 -0.04070 80   ARG A NE  
376  C CZ  . ARG A 48  ? 0.29609 0.46950 0.43570 0.02446  -0.00819 -0.04175 80   ARG A CZ  
377  N NH1 . ARG A 48  ? 0.28152 0.47449 0.42865 0.00827  -0.00526 -0.04011 80   ARG A NH1 
378  N NH2 . ARG A 48  ? 0.32508 0.51554 0.48640 0.04121  -0.01040 -0.04430 80   ARG A NH2 
379  N N   . LEU A 49  ? 0.28071 0.31642 0.30060 -0.00421 0.01092  -0.02945 81   LEU A N   
380  C CA  . LEU A 49  ? 0.29621 0.31038 0.30305 -0.01082 0.00953  -0.02279 81   LEU A CA  
381  C C   . LEU A 49  ? 0.32605 0.34370 0.32142 -0.01415 0.01480  -0.01760 81   LEU A C   
382  O O   . LEU A 49  ? 0.33226 0.34319 0.32104 -0.02467 0.01593  -0.00850 81   LEU A O   
383  C CB  . LEU A 49  ? 0.32813 0.32138 0.32930 -0.00288 0.00415  -0.02457 81   LEU A CB  
384  C CG  . LEU A 49  ? 0.31977 0.30711 0.32580 -0.00275 -0.00022 -0.02803 81   LEU A CG  
385  C CD1 . LEU A 49  ? 0.43047 0.40680 0.43331 0.00637  -0.00270 -0.03077 81   LEU A CD1 
386  C CD2 . LEU A 49  ? 0.38022 0.35183 0.38296 -0.01219 -0.00161 -0.02551 81   LEU A CD2 
387  N N   . ALA A 50  ? 0.36917 0.39616 0.36027 -0.00616 0.01779  -0.02313 82   ALA A N   
388  C CA  . ALA A 50  ? 0.37396 0.40639 0.34920 -0.01042 0.02267  -0.01900 82   ALA A CA  
389  C C   . ALA A 50  ? 0.34853 0.40313 0.32645 -0.02131 0.03208  -0.01492 82   ALA A C   
390  O O   . ALA A 50  ? 0.36696 0.41948 0.33089 -0.03205 0.03478  -0.00398 82   ALA A O   
391  C CB  . ALA A 50  ? 0.38137 0.41947 0.35003 -0.00053 0.02421  -0.02935 82   ALA A CB  
392  N N   . HIS A 51  ? 0.31177 0.38854 0.30935 -0.01964 0.03650  -0.02176 83   HIS A N   
393  C CA  . HIS A 51  ? 0.30472 0.40913 0.30992 -0.03067 0.04666  -0.01849 83   HIS A CA  
394  C C   . HIS A 51  ? 0.30700 0.40074 0.31168 -0.04793 0.04425  -0.00540 83   HIS A C   
395  O O   . HIS A 51  ? 0.32177 0.42255 0.31696 -0.06143 0.05140  0.00465  83   HIS A O   
396  C CB  . HIS A 51  ? 0.32935 0.46194 0.36185 -0.02378 0.04952  -0.02826 83   HIS A CB  
397  C CG  . HIS A 51  ? 0.34063 0.50909 0.38735 -0.03459 0.06096  -0.02618 83   HIS A CG  
398  N ND1 . HIS A 51  ? 0.37570 0.55165 0.43538 -0.05082 0.05930  -0.01791 83   HIS A ND1 
399  C CD2 . HIS A 51  ? 0.36292 0.56370 0.41369 -0.03246 0.07523  -0.03215 83   HIS A CD2 
400  C CE1 . HIS A 51  ? 0.30036 0.51375 0.37353 -0.05933 0.07190  -0.01718 83   HIS A CE1 
401  N NE2 . HIS A 51  ? 0.47227 0.70267 0.54040 -0.04758 0.08265  -0.02604 83   HIS A NE2 
402  N N   . TYR A 52  ? 0.31246 0.38620 0.32456 -0.04845 0.03425  -0.00524 84   TYR A N   
403  C CA  . TYR A 52  ? 0.31273 0.37286 0.32574 -0.06498 0.03158  0.00426  84   TYR A CA  
404  C C   . TYR A 52  ? 0.31971 0.34858 0.31186 -0.06922 0.02872  0.01612  84   TYR A C   
405  O O   . TYR A 52  ? 0.36764 0.38466 0.35725 -0.08466 0.02892  0.02723  84   TYR A O   
406  C CB  . TYR A 52  ? 0.30087 0.34868 0.32533 -0.06429 0.02198  -0.00199 84   TYR A CB  
407  C CG  . TYR A 52  ? 0.27064 0.35045 0.31743 -0.06339 0.02181  -0.00992 84   TYR A CG  
408  C CD1 . TYR A 52  ? 0.30913 0.42077 0.37198 -0.07580 0.02855  -0.00723 84   TYR A CD1 
409  C CD2 . TYR A 52  ? 0.28100 0.35952 0.33377 -0.05116 0.01386  -0.01855 84   TYR A CD2 
410  C CE1 . TYR A 52  ? 0.30501 0.44991 0.39315 -0.07426 0.02669  -0.01377 84   TYR A CE1 
411  C CE2 . TYR A 52  ? 0.27123 0.37923 0.34532 -0.04988 0.01092  -0.02349 84   TYR A CE2 
412  C CZ  . TYR A 52  ? 0.25992 0.40189 0.35317 -0.06042 0.01688  -0.02148 84   TYR A CZ  
413  O OH  . TYR A 52  ? 0.26202 0.43783 0.38112 -0.05860 0.01281  -0.02566 84   TYR A OH  
414  N N   . ASN A 53  ? 0.34968 0.36551 0.32842 -0.05633 0.02527  0.01486  85   ASN A N   
415  C CA  . ASN A 53  ? 0.40040 0.39124 0.36107 -0.05823 0.02096  0.02745  85   ASN A CA  
416  C C   . ASN A 53  ? 0.44806 0.45360 0.38971 -0.06217 0.02721  0.03536  85   ASN A C   
417  O O   . ASN A 53  ? 0.44355 0.43145 0.36769 -0.06281 0.02188  0.04739  85   ASN A O   
418  C CB  . ASN A 53  ? 0.37002 0.33919 0.32942 -0.04354 0.01178  0.02271  85   ASN A CB  
419  C CG  . ASN A 53  ? 0.43705 0.38562 0.40829 -0.04283 0.00648  0.01829  85   ASN A CG  
420  O OD1 . ASN A 53  ? 0.42467 0.34683 0.39363 -0.04694 0.00214  0.02616  85   ASN A OD1 
421  N ND2 . ASN A 53  ? 0.42821 0.38756 0.41105 -0.03792 0.00664  0.00579  85   ASN A ND2 
422  N N   . LYS A 54  ? 0.35468 0.39340 0.29927 -0.06478 0.03834  0.02903  86   LYS A N   
423  C CA  . LYS A 54  ? 0.37637 0.43389 0.30042 -0.07066 0.04750  0.03458  86   LYS A CA  
424  C C   . LYS A 54  ? 0.42063 0.46933 0.32356 -0.05957 0.04154  0.03195  86   LYS A C   
425  O O   . LYS A 54  ? 0.47521 0.52057 0.35270 -0.06584 0.04074  0.04415  86   LYS A O   
426  C CB  . LYS A 54  ? 0.43283 0.48323 0.34484 -0.09021 0.05022  0.05545  86   LYS A CB  
427  C CG  . LYS A 54  ? 0.46758 0.52838 0.40180 -0.10491 0.05585  0.05788  86   LYS A CG  
428  C CD  . LYS A 54  ? 0.57933 0.68483 0.53056 -0.10394 0.06919  0.04442  86   LYS A CD  
429  C CE  . LYS A 54  ? 0.60125 0.71988 0.58056 -0.11700 0.07115  0.04470  86   LYS A CE  
430  N NZ  . LYS A 54  ? 0.68516 0.83075 0.66511 -0.13837 0.08488  0.05639  86   LYS A NZ  
431  N N   . ARG A 55  ? 0.42247 0.46783 0.33545 -0.04436 0.03640  0.01691  87   ARG A N   
432  C CA  . ARG A 55  ? 0.50229 0.54093 0.40016 -0.03460 0.02970  0.01147  87   ARG A CA  
433  C C   . ARG A 55  ? 0.51604 0.57704 0.41318 -0.02704 0.03822  -0.00690 87   ARG A C   
434  O O   . ARG A 55  ? 0.48944 0.55751 0.40822 -0.01903 0.04115  -0.01924 87   ARG A O   
435  C CB  . ARG A 55  ? 0.45754 0.47340 0.36859 -0.02440 0.01764  0.00853  87   ARG A CB  
436  C CG  . ARG A 55  ? 0.50082 0.49234 0.41406 -0.02842 0.00946  0.02341  87   ARG A CG  
437  C CD  . ARG A 55  ? 0.56303 0.53890 0.49318 -0.01821 0.00210  0.01683  87   ARG A CD  
438  N NE  . ARG A 55  ? 0.59402 0.54642 0.53023 -0.02035 -0.00342 0.02685  87   ARG A NE  
439  C CZ  . ARG A 55  ? 0.61855 0.55854 0.57039 -0.01496 -0.00579 0.02050  87   ARG A CZ  
440  N NH1 . ARG A 55  ? 0.56375 0.51296 0.52565 -0.00854 -0.00380 0.00728  87   ARG A NH1 
441  N NH2 . ARG A 55  ? 0.60475 0.52138 0.56095 -0.01609 -0.01002 0.02755  87   ARG A NH2 
442  N N   . SER A 56  ? 0.46232 0.53218 0.33377 -0.02866 0.04089  -0.00919 88   SER A N   
443  C CA  . SER A 56  ? 0.50498 0.59264 0.37316 -0.02087 0.04949  -0.02942 88   SER A CA  
444  C C   . SER A 56  ? 0.51355 0.58560 0.38764 -0.00833 0.03969  -0.04347 88   SER A C   
445  O O   . SER A 56  ? 0.53748 0.61767 0.41590 0.00028  0.04572  -0.06207 88   SER A O   
446  C CB  . SER A 56  ? 0.55383 0.65701 0.38747 -0.02870 0.05667  -0.02893 88   SER A CB  
447  O OG  . SER A 56  ? 0.65883 0.74522 0.46872 -0.03037 0.04242  -0.02180 88   SER A OG  
448  N N   . THR A 57  ? 0.45846 0.50852 0.33511 -0.00710 0.02545  -0.03528 89   THR A N   
449  C CA  . THR A 57  ? 0.48476 0.52151 0.36639 0.00132  0.01593  -0.04610 89   THR A CA  
450  C C   . THR A 57  ? 0.48489 0.50646 0.39185 0.00609  0.00958  -0.04179 89   THR A C   
451  O O   . THR A 57  ? 0.49942 0.51189 0.40996 0.00239  0.00458  -0.02771 89   THR A O   
452  C CB  . THR A 57  ? 0.58761 0.61779 0.44763 -0.00255 0.00403  -0.04067 89   THR A CB  
453  O OG1 . THR A 57  ? 0.64162 0.68661 0.47163 -0.00918 0.00954  -0.04230 89   THR A OG1 
454  C CG2 . THR A 57  ? 0.56805 0.58808 0.43477 0.00349  -0.00521 -0.05351 89   THR A CG2 
455  N N   . ILE A 58  ? 0.42407 0.44124 0.34681 0.01432  0.00963  -0.05395 90   ILE A N   
456  C CA  . ILE A 58  ? 0.40586 0.40900 0.34760 0.01818  0.00332  -0.05068 90   ILE A CA  
457  C C   . ILE A 58  ? 0.46349 0.45540 0.40241 0.01825  -0.00721 -0.05014 90   ILE A C   
458  O O   . ILE A 58  ? 0.44964 0.44056 0.38152 0.01920  -0.00998 -0.06057 90   ILE A O   
459  C CB  . ILE A 58  ? 0.46031 0.46331 0.41914 0.02593  0.00691  -0.06036 90   ILE A CB  
460  C CG1 . ILE A 58  ? 0.47940 0.49774 0.44774 0.02555  0.01511  -0.05838 90   ILE A CG1 
461  C CG2 . ILE A 58  ? 0.43781 0.42565 0.40973 0.02877  -0.00002 -0.05780 90   ILE A CG2 
462  C CD1 . ILE A 58  ? 0.48240 0.50413 0.46921 0.03484  0.01709  -0.06633 90   ILE A CD1 
463  N N   . THR A 59  ? 0.39763 0.38231 0.34281 0.01687  -0.01309 -0.03884 91   THR A N   
464  C CA  . THR A 59  ? 0.43959 0.41859 0.38959 0.01753  -0.02280 -0.03665 91   THR A CA  
465  C C   . THR A 59  ? 0.43515 0.40666 0.40497 0.02103  -0.02245 -0.03594 91   THR A C   
466  O O   . THR A 59  ? 0.40847 0.37792 0.38482 0.02276  -0.01637 -0.03754 91   THR A O   
467  C CB  . THR A 59  ? 0.46287 0.44245 0.40494 0.01491  -0.02984 -0.02373 91   THR A CB  
468  O OG1 . THR A 59  ? 0.48851 0.46042 0.43985 0.01590  -0.02753 -0.01402 91   THR A OG1 
469  C CG2 . THR A 59  ? 0.52583 0.51377 0.44284 0.00943  -0.02877 -0.02148 91   THR A CG2 
470  N N   . SER A 60  ? 0.39962 0.36990 0.37905 0.02166  -0.02909 -0.03308 92   SER A N   
471  C CA  . SER A 60  ? 0.36522 0.33135 0.36141 0.02411  -0.02678 -0.03224 92   SER A CA  
472  C C   . SER A 60  ? 0.40954 0.37077 0.40844 0.02597  -0.02223 -0.02635 92   SER A C   
473  O O   . SER A 60  ? 0.38571 0.34355 0.39248 0.02732  -0.01781 -0.02790 92   SER A O   
474  C CB  . SER A 60  ? 0.43705 0.40838 0.44631 0.02407  -0.03337 -0.03059 92   SER A CB  
475  O OG  . SER A 60  ? 0.45117 0.42526 0.46506 0.02726  -0.03775 -0.02207 92   SER A OG  
476  N N   . ARG A 61  ? 0.38682 0.34626 0.37727 0.02481  -0.02337 -0.01967 93   ARG A N   
477  C CA  . ARG A 61  ? 0.41054 0.36100 0.40346 0.02491  -0.01988 -0.01511 93   ARG A CA  
478  C C   . ARG A 61  ? 0.39684 0.34736 0.38884 0.02233  -0.01317 -0.02014 93   ARG A C   
479  O O   . ARG A 61  ? 0.40102 0.34546 0.39871 0.02297  -0.01054 -0.02187 93   ARG A O   
480  C CB  . ARG A 61  ? 0.45764 0.40356 0.44047 0.02196  -0.02311 -0.00491 93   ARG A CB  
481  C CG  . ARG A 61  ? 0.50998 0.44265 0.49365 0.01920  -0.01991 -0.00026 93   ARG A CG  
482  C CD  . ARG A 61  ? 0.64365 0.56752 0.61787 0.01573  -0.02457 0.01342  93   ARG A CD  
483  N NE  . ARG A 61  ? 0.70602 0.64192 0.66264 0.00912  -0.02421 0.01756  93   ARG A NE  
484  C CZ  . ARG A 61  ? 0.82627 0.75850 0.76891 0.00463  -0.02872 0.03122  93   ARG A CZ  
485  N NH1 . ARG A 61  ? 0.69256 0.60618 0.63899 0.00660  -0.03507 0.04357  93   ARG A NH1 
486  N NH2 . ARG A 61  ? 0.78882 0.73560 0.71232 -0.00153 -0.02680 0.03259  93   ARG A NH2 
487  N N   . GLU A 62  ? 0.37349 0.33257 0.35886 0.01991  -0.01060 -0.02336 94   GLU A N   
488  C CA  . GLU A 62  ? 0.41244 0.37601 0.40104 0.01865  -0.00599 -0.02722 94   GLU A CA  
489  C C   . GLU A 62  ? 0.36755 0.33002 0.36329 0.02286  -0.00635 -0.03231 94   GLU A C   
490  O O   . GLU A 62  ? 0.37648 0.33924 0.37558 0.02233  -0.00523 -0.03311 94   GLU A O   
491  C CB  . GLU A 62  ? 0.38502 0.36171 0.36876 0.01695  -0.00208 -0.02988 94   GLU A CB  
492  C CG  . GLU A 62  ? 0.43808 0.41884 0.41264 0.00982  0.00040  -0.02289 94   GLU A CG  
493  C CD  . GLU A 62  ? 0.48484 0.46114 0.44709 0.00922  -0.00406 -0.01746 94   GLU A CD  
494  O OE1 . GLU A 62  ? 0.55941 0.53830 0.51811 0.01315  -0.00687 -0.02333 94   GLU A OE1 
495  O OE2 . GLU A 62  ? 0.53608 0.50622 0.49155 0.00405  -0.00570 -0.00690 94   GLU A OE2 
496  N N   . ILE A 63  ? 0.35888 0.31997 0.35595 0.02564  -0.00876 -0.03502 95   ILE A N   
497  C CA  . ILE A 63  ? 0.34225 0.29947 0.34540 0.02764  -0.00910 -0.03689 95   ILE A CA  
498  C C   . ILE A 63  ? 0.35163 0.30505 0.35774 0.02673  -0.00771 -0.03391 95   ILE A C   
499  O O   . ILE A 63  ? 0.35144 0.30367 0.35718 0.02640  -0.00626 -0.03368 95   ILE A O   
500  C CB  . ILE A 63  ? 0.35436 0.30888 0.35961 0.02800  -0.01227 -0.04010 95   ILE A CB  
501  C CG1 . ILE A 63  ? 0.37259 0.32931 0.37218 0.02948  -0.01265 -0.04669 95   ILE A CG1 
502  C CG2 . ILE A 63  ? 0.38273 0.33082 0.39393 0.02793  -0.01224 -0.03924 95   ILE A CG2 
503  C CD1 . ILE A 63  ? 0.39654 0.35523 0.39855 0.03388  -0.00949 -0.05014 95   ILE A CD1 
504  N N   . GLN A 64  ? 0.35637 0.30845 0.36503 0.02700  -0.00827 -0.03185 96   GLN A N   
505  C CA  . GLN A 64  ? 0.34747 0.29664 0.36044 0.02802  -0.00503 -0.03186 96   GLN A CA  
506  C C   . GLN A 64  ? 0.34015 0.28438 0.34670 0.02602  -0.00250 -0.03350 96   GLN A C   
507  O O   . GLN A 64  ? 0.35170 0.29497 0.35565 0.02528  0.00075  -0.03621 96   GLN A O   
508  C CB  . GLN A 64  ? 0.36152 0.31037 0.38236 0.03140  -0.00686 -0.02957 96   GLN A CB  
509  C CG  . GLN A 64  ? 0.35573 0.30085 0.38265 0.03483  -0.00179 -0.03220 96   GLN A CG  
510  C CD  . GLN A 64  ? 0.42154 0.37081 0.46383 0.04115  -0.00367 -0.03021 96   GLN A CD  
511  O OE1 . GLN A 64  ? 0.59262 0.53312 0.63814 0.04570  -0.00591 -0.02787 96   GLN A OE1 
512  N NE2 . GLN A 64  ? 0.35766 0.32033 0.41153 0.04131  -0.00348 -0.03033 96   GLN A NE2 
513  N N   . THR A 65  ? 0.34113 0.28305 0.34387 0.02350  -0.00399 -0.03188 97   THR A N   
514  C CA  . THR A 65  ? 0.33809 0.27575 0.33649 0.01901  -0.00287 -0.03404 97   THR A CA  
515  C C   . THR A 65  ? 0.36468 0.31074 0.36037 0.01707  -0.00352 -0.03611 97   THR A C   
516  O O   . THR A 65  ? 0.37298 0.31704 0.36370 0.01428  -0.00329 -0.03949 97   THR A O   
517  C CB  . THR A 65  ? 0.38480 0.32001 0.38144 0.01407  -0.00406 -0.03005 97   THR A CB  
518  O OG1 . THR A 65  ? 0.39621 0.32042 0.39441 0.01659  -0.00531 -0.02574 97   THR A OG1 
519  C CG2 . THR A 65  ? 0.39962 0.33099 0.39396 0.00664  -0.00391 -0.03288 97   THR A CG2 
520  N N   . ALA A 66  ? 0.33822 0.29317 0.33666 0.01919  -0.00505 -0.03455 98   ALA A N   
521  C CA  . ALA A 66  ? 0.34016 0.30226 0.33909 0.01994  -0.00742 -0.03464 98   ALA A CA  
522  C C   . ALA A 66  ? 0.36401 0.32133 0.35786 0.02068  -0.00734 -0.03380 98   ALA A C   
523  O O   . ALA A 66  ? 0.37844 0.33886 0.36681 0.01868  -0.00998 -0.03305 98   ALA A O   
524  C CB  . ALA A 66  ? 0.34007 0.30874 0.34517 0.02487  -0.00843 -0.03452 98   ALA A CB  
525  N N   . VAL A 67  ? 0.34570 0.29801 0.34115 0.02253  -0.00464 -0.03313 99   VAL A N   
526  C CA  . VAL A 67  ? 0.36809 0.31858 0.35902 0.02138  -0.00215 -0.03134 99   VAL A CA  
527  C C   . VAL A 67  ? 0.38694 0.33647 0.36856 0.01842  0.00137  -0.03557 99   VAL A C   
528  O O   . VAL A 67  ? 0.38998 0.34122 0.36044 0.01552  0.00181  -0.03448 99   VAL A O   
529  C CB  . VAL A 67  ? 0.36787 0.31757 0.36693 0.02231  0.00068  -0.03042 99   VAL A CB  
530  C CG1 . VAL A 67  ? 0.39759 0.34963 0.39368 0.01950  0.00677  -0.02920 99   VAL A CG1 
531  C CG2 . VAL A 67  ? 0.37956 0.32687 0.38408 0.02337  -0.00356 -0.02800 99   VAL A CG2 
532  N N   . ARG A 68  ? 0.35808 0.30311 0.34228 0.01887  0.00348  -0.04061 100  ARG A N   
533  C CA  . ARG A 68  ? 0.37032 0.31023 0.34573 0.01656  0.00709  -0.04787 100  ARG A CA  
534  C C   . ARG A 68  ? 0.44247 0.38394 0.40680 0.01043  0.00195  -0.04997 100  ARG A C   
535  O O   . ARG A 68  ? 0.42612 0.36606 0.37686 0.00678  0.00367  -0.05611 100  ARG A O   
536  C CB  . ARG A 68  ? 0.44093 0.37067 0.42396 0.01935  0.00901  -0.05187 100  ARG A CB  
537  C CG  . ARG A 68  ? 0.45364 0.38465 0.44920 0.02629  0.01322  -0.05100 100  ARG A CG  
538  C CD  . ARG A 68  ? 0.56993 0.48893 0.57408 0.03047  0.01192  -0.05173 100  ARG A CD  
539  N NE  . ARG A 68  ? 0.63123 0.55363 0.65021 0.03887  0.01532  -0.05212 100  ARG A NE  
540  C CZ  . ARG A 68  ? 0.69668 0.61460 0.72793 0.04472  0.01113  -0.04732 100  ARG A CZ  
541  N NH1 . ARG A 68  ? 0.71655 0.62462 0.74385 0.04190  0.00433  -0.04073 100  ARG A NH1 
542  N NH2 . ARG A 68  ? 0.67848 0.60416 0.72693 0.05329  0.01364  -0.04808 100  ARG A NH2 
543  N N   . LEU A 69  ? 0.38123 0.32823 0.35140 0.00886  -0.00425 -0.04595 101  LEU A N   
544  C CA  . LEU A 69  ? 0.39138 0.34536 0.35615 0.00272  -0.01066 -0.04725 101  LEU A CA  
545  C C   . LEU A 69  ? 0.39301 0.35602 0.34993 0.00340  -0.01538 -0.04206 101  LEU A C   
546  O O   . LEU A 69  ? 0.43333 0.40232 0.38012 -0.00211 -0.02138 -0.04372 101  LEU A O   
547  C CB  . LEU A 69  ? 0.44446 0.40680 0.42217 0.00118  -0.01429 -0.04428 101  LEU A CB  
548  C CG  . LEU A 69  ? 0.48894 0.44154 0.47105 -0.00255 -0.01117 -0.04641 101  LEU A CG  
549  C CD1 . LEU A 69  ? 0.44595 0.41119 0.43953 -0.00425 -0.01221 -0.04159 101  LEU A CD1 
550  C CD2 . LEU A 69  ? 0.45469 0.39759 0.42903 -0.01126 -0.01261 -0.05405 101  LEU A CD2 
551  N N   . LEU A 70  ? 0.37329 0.33612 0.33386 0.00915  -0.01393 -0.03512 102  LEU A N   
552  C CA  . LEU A 70  ? 0.38336 0.35118 0.33921 0.01064  -0.02000 -0.02654 102  LEU A CA  
553  C C   . LEU A 70  ? 0.43212 0.39567 0.37148 0.00795  -0.01588 -0.02313 102  LEU A C   
554  O O   . LEU A 70  ? 0.49413 0.46167 0.41958 0.00518  -0.02177 -0.01689 102  LEU A O   
555  C CB  . LEU A 70  ? 0.37484 0.34203 0.34613 0.01800  -0.02195 -0.02064 102  LEU A CB  
556  C CG  . LEU A 70  ? 0.39541 0.37263 0.38185 0.02107  -0.02547 -0.02311 102  LEU A CG  
557  C CD1 . LEU A 70  ? 0.39121 0.36539 0.39054 0.02906  -0.02458 -0.02159 102  LEU A CD1 
558  C CD2 . LEU A 70  ? 0.44646 0.43761 0.43417 0.02025  -0.03498 -0.02009 102  LEU A CD2 
559  N N   . LEU A 71  ? 0.41842 0.37650 0.35952 0.00837  -0.00617 -0.02597 103  LEU A N   
560  C CA  . LEU A 71  ? 0.42743 0.38559 0.35572 0.00486  0.00034  -0.02201 103  LEU A CA  
561  C C   . LEU A 71  ? 0.43768 0.39797 0.34979 0.00078  0.00791  -0.03272 103  LEU A C   
562  O O   . LEU A 71  ? 0.47772 0.43423 0.39614 0.00274  0.01141  -0.04395 103  LEU A O   
563  C CB  . LEU A 71  ? 0.44906 0.40496 0.39175 0.00678  0.00727  -0.01962 103  LEU A CB  
564  C CG  . LEU A 71  ? 0.41760 0.36804 0.36875 0.00767  0.00211  -0.00850 103  LEU A CG  
565  C CD1 . LEU A 71  ? 0.43909 0.38620 0.40282 0.01401  -0.00659 -0.00937 103  LEU A CD1 
566  C CD2 . LEU A 71  ? 0.42112 0.37167 0.38468 0.00586  0.00929  -0.00786 103  LEU A CD2 
567  N N   . PRO A 72  ? 0.46546 0.43023 0.35471 -0.00501 0.00984  -0.02976 104  PRO A N   
568  C CA  . PRO A 72  ? 0.49328 0.46032 0.36355 -0.00885 0.01861  -0.04283 104  PRO A CA  
569  C C   . PRO A 72  ? 0.51017 0.48221 0.38196 -0.00820 0.03507  -0.04671 104  PRO A C   
570  O O   . PRO A 72  ? 0.47331 0.45012 0.35183 -0.00947 0.03920  -0.03535 104  PRO A O   
571  C CB  . PRO A 72  ? 0.55170 0.52436 0.39264 -0.01644 0.01113  -0.03657 104  PRO A CB  
572  C CG  . PRO A 72  ? 0.51095 0.48398 0.35601 -0.01621 0.00571  -0.01663 104  PRO A CG  
573  C CD  . PRO A 72  ? 0.44275 0.40948 0.31973 -0.00824 0.00158  -0.01428 104  PRO A CD  
574  N N   . GLY A 73  ? 0.50995 0.48111 0.37708 -0.00643 0.04470  -0.06377 105  GLY A N   
575  C CA  . GLY A 73  ? 0.49877 0.48030 0.36117 -0.00635 0.06224  -0.07054 105  GLY A CA  
576  C C   . GLY A 73  ? 0.47959 0.46978 0.37013 -0.00208 0.07017  -0.06366 105  GLY A C   
577  O O   . GLY A 73  ? 0.48169 0.46678 0.39913 0.00509  0.06594  -0.06366 105  GLY A O   
578  N N   . GLU A 74  ? 0.47848 0.48381 0.36185 -0.00797 0.08190  -0.05756 106  GLU A N   
579  C CA  . GLU A 74  ? 0.44280 0.46106 0.35442 -0.00649 0.09044  -0.05200 106  GLU A CA  
580  C C   . GLU A 74  ? 0.45398 0.46447 0.38272 -0.00814 0.07711  -0.03620 106  GLU A C   
581  O O   . GLU A 74  ? 0.44543 0.46066 0.40331 -0.00419 0.07732  -0.03545 106  GLU A O   
582  C CB  . GLU A 74  ? 0.44397 0.48203 0.34242 -0.01578 0.10671  -0.04740 106  GLU A CB  
583  C CG  . GLU A 74  ? 0.51043 0.56033 0.39412 -0.01307 0.12412  -0.06637 106  GLU A CG  
584  C CD  . GLU A 74  ? 0.58930 0.64590 0.50669 0.00082  0.13311  -0.08257 106  GLU A CD  
585  O OE1 . GLU A 74  ? 0.53235 0.60599 0.48152 0.00254  0.13910  -0.07709 106  GLU A OE1 
586  O OE2 . GLU A 74  ? 0.60322 0.64724 0.51668 0.00979  0.13280  -0.10017 106  GLU A OE2 
587  N N   . LEU A 75  ? 0.43930 0.43812 0.35095 -0.01317 0.06472  -0.02459 107  LEU A N   
588  C CA  A LEU A 75  ? 0.44875 0.43691 0.37593 -0.01279 0.05217  -0.01282 107  LEU A CA  
589  C CA  B LEU A 75  ? 0.44838 0.43660 0.37552 -0.01282 0.05224  -0.01281 107  LEU A CA  
590  C C   . LEU A 75  ? 0.45916 0.44151 0.40896 -0.00332 0.04579  -0.02128 107  LEU A C   
591  O O   . LEU A 75  ? 0.39443 0.37612 0.36532 -0.00213 0.04259  -0.01770 107  LEU A O   
592  C CB  A LEU A 75  ? 0.51346 0.48980 0.42144 -0.01537 0.03896  -0.00206 107  LEU A CB  
593  C CB  B LEU A 75  ? 0.49640 0.47309 0.40358 -0.01564 0.03933  -0.00200 107  LEU A CB  
594  C CG  A LEU A 75  ? 0.45810 0.43217 0.34787 -0.02476 0.03750  0.01576  107  LEU A CG  
595  C CG  B LEU A 75  ? 0.44208 0.40678 0.35821 -0.01720 0.02917  0.01315  107  LEU A CG  
596  C CD1 A LEU A 75  ? 0.44150 0.40366 0.32102 -0.02191 0.02060  0.02428  107  LEU A CD1 
597  C CD1 B LEU A 75  ? 0.45887 0.42620 0.37151 -0.02797 0.03672  0.02657  107  LEU A CD1 
598  C CD2 A LEU A 75  ? 0.45676 0.42788 0.36519 -0.02994 0.04021  0.02660  107  LEU A CD2 
599  C CD2 B LEU A 75  ? 0.43069 0.38599 0.33301 -0.01475 0.01481  0.02033  107  LEU A CD2 
600  N N   . ALA A 76  ? 0.39718 0.37446 0.34102 0.00200  0.04312  -0.03210 108  ALA A N   
601  C CA  . ALA A 76  ? 0.41236 0.38311 0.37410 0.00944  0.03720  -0.03772 108  ALA A CA  
602  C C   . ALA A 76  ? 0.40875 0.38754 0.39293 0.01470  0.04459  -0.04279 108  ALA A C   
603  O O   . ALA A 76  ? 0.40234 0.37998 0.40449 0.01815  0.03865  -0.04027 108  ALA A O   
604  C CB  . ALA A 76  ? 0.41808 0.38060 0.36854 0.01129  0.03354  -0.04714 108  ALA A CB  
605  N N   . LYS A 77  ? 0.37481 0.36375 0.35858 0.01594  0.05733  -0.05052 109  LYS A N   
606  C CA  . LYS A 77  ? 0.41573 0.41684 0.42591 0.02275  0.06427  -0.05502 109  LYS A CA  
607  C C   . LYS A 77  ? 0.44623 0.45927 0.47535 0.01806  0.06216  -0.04441 109  LYS A C   
608  O O   . LYS A 77  ? 0.39304 0.41014 0.44519 0.02304  0.05672  -0.04381 109  LYS A O   
609  C CB  . LYS A 77  ? 0.45116 0.46517 0.45863 0.02511  0.08089  -0.06602 109  LYS A CB  
610  C CG  . LYS A 77  ? 0.53264 0.53312 0.53232 0.03332  0.08330  -0.08156 109  LYS A CG  
611  C CD  . LYS A 77  ? 0.58953 0.60420 0.59972 0.04138  0.10082  -0.09591 109  LYS A CD  
612  C CE  . LYS A 77  ? 0.70149 0.72609 0.68410 0.03370  0.11441  -0.10211 109  LYS A CE  
613  N NZ  . LYS A 77  ? 0.55798 0.59302 0.54445 0.04250  0.13288  -0.12129 109  LYS A NZ  
614  N N   . HIS A 78  ? 0.40829 0.42613 0.42715 0.00737  0.06541  -0.03537 110  HIS A N   
615  C CA  . HIS A 78  ? 0.43539 0.46126 0.47206 0.00026  0.06309  -0.02580 110  HIS A CA  
616  C C   . HIS A 78  ? 0.37394 0.38417 0.41529 0.00114  0.04744  -0.02170 110  HIS A C   
617  O O   . HIS A 78  ? 0.39882 0.41553 0.46129 0.00047  0.04270  -0.02073 110  HIS A O   
618  C CB  . HIS A 78  ? 0.43781 0.46609 0.45973 -0.01279 0.06895  -0.01479 110  HIS A CB  
619  C CG  . HIS A 78  ? 0.38968 0.44184 0.41389 -0.01728 0.08694  -0.01683 110  HIS A CG  
620  N ND1 . HIS A 78  ? 0.49644 0.56698 0.53870 -0.02792 0.09429  -0.00895 110  HIS A ND1 
621  C CD2 . HIS A 78  ? 0.46760 0.52986 0.47886 -0.01327 0.10020  -0.02706 110  HIS A CD2 
622  C CE1 . HIS A 78  ? 0.57611 0.67032 0.61755 -0.02987 0.11262  -0.01342 110  HIS A CE1 
623  N NE2 . HIS A 78  ? 0.49417 0.58297 0.51574 -0.02031 0.11676  -0.02542 110  HIS A NE2 
624  N N   . ALA A 79  ? 0.36447 0.35655 0.38668 0.00245  0.03942  -0.02017 111  ALA A N   
625  C CA  . ALA A 79  ? 0.36731 0.34640 0.39290 0.00431  0.02691  -0.01836 111  ALA A CA  
626  C C   . ALA A 79  ? 0.41921 0.40115 0.45854 0.01184  0.02251  -0.02494 111  ALA A C   
627  O O   . ALA A 79  ? 0.38483 0.36586 0.43441 0.01112  0.01510  -0.02417 111  ALA A O   
628  C CB  . ALA A 79  ? 0.38874 0.35383 0.39540 0.00611  0.02074  -0.01665 111  ALA A CB  
629  N N   . VAL A 80  ? 0.38032 0.36363 0.41808 0.01862  0.02613  -0.03131 112  VAL A N   
630  C CA  . VAL A 80  ? 0.36713 0.35067 0.41694 0.02591  0.02119  -0.03459 112  VAL A CA  
631  C C   . VAL A 80  ? 0.39783 0.39824 0.47164 0.02684  0.02164  -0.03368 112  VAL A C   
632  O O   . VAL A 80  ? 0.39605 0.39846 0.47975 0.02867  0.01248  -0.03201 112  VAL A O   
633  C CB  . VAL A 80  ? 0.38198 0.35874 0.42594 0.03239  0.02509  -0.04116 112  VAL A CB  
634  C CG1 . VAL A 80  ? 0.42339 0.40018 0.48330 0.04082  0.02110  -0.04218 112  VAL A CG1 
635  C CG2 . VAL A 80  ? 0.37760 0.34037 0.40222 0.02985  0.02065  -0.04135 112  VAL A CG2 
636  N N   . SER A 81  ? 0.36406 0.37983 0.44760 0.02484  0.03216  -0.03465 113  SER A N   
637  C CA  . SER A 81  ? 0.37764 0.41554 0.48916 0.02476  0.03296  -0.03360 113  SER A CA  
638  C C   . SER A 81  ? 0.41033 0.44945 0.52738 0.01468  0.02365  -0.02782 113  SER A C   
639  O O   . SER A 81  ? 0.40762 0.45784 0.54322 0.01544  0.01508  -0.02730 113  SER A O   
640  C CB  . SER A 81  ? 0.46574 0.52340 0.58625 0.02265  0.04883  -0.03587 113  SER A CB  
641  O OG  . SER A 81  ? 0.53767 0.62210 0.68995 0.02120  0.04993  -0.03434 113  SER A OG  
642  N N   . GLU A 82  ? 0.36568 0.39211 0.46648 0.00525  0.02403  -0.02365 114  GLU A N   
643  C CA  . GLU A 82  ? 0.42634 0.44821 0.53166 -0.00475 0.01566  -0.01994 114  GLU A CA  
644  C C   . GLU A 82  ? 0.40803 0.41801 0.50802 -0.00060 0.00245  -0.02344 114  GLU A C   
645  O O   . GLU A 82  ? 0.38581 0.40121 0.49729 -0.00547 -0.00625 -0.02461 114  GLU A O   
646  C CB  . GLU A 82  ? 0.42073 0.42613 0.50914 -0.01334 0.01832  -0.01378 114  GLU A CB  
647  C CG  . GLU A 82  ? 0.43906 0.45749 0.53164 -0.02304 0.03059  -0.00725 114  GLU A CG  
648  C CD  . GLU A 82  ? 0.63844 0.67566 0.75763 -0.03404 0.03103  -0.00483 114  GLU A CD  
649  O OE1 . GLU A 82  ? 0.57653 0.60320 0.70158 -0.04123 0.02018  -0.00426 114  GLU A OE1 
650  O OE2 . GLU A 82  ? 0.69854 0.76237 0.83369 -0.03597 0.04264  -0.00460 114  GLU A OE2 
651  N N   . GLY A 83  ? 0.37618 0.37149 0.45780 0.00685  0.00094  -0.02549 115  GLY A N   
652  C CA  . GLY A 83  ? 0.33261 0.31933 0.40675 0.00998  -0.00908 -0.02861 115  GLY A CA  
653  C C   . GLY A 83  ? 0.37540 0.37517 0.46124 0.01467  -0.01515 -0.02924 115  GLY A C   
654  O O   . GLY A 83  ? 0.37056 0.37213 0.45678 0.01213  -0.02501 -0.03083 115  GLY A O   
655  N N   . THR A 84  ? 0.34740 0.35546 0.44203 0.02206  -0.01008 -0.02826 116  THR A N   
656  C CA  . THR A 84  ? 0.39076 0.40930 0.49839 0.02892  -0.01721 -0.02657 116  THR A CA  
657  C C   . THR A 84  ? 0.39351 0.43322 0.52376 0.02394  -0.02383 -0.02557 116  THR A C   
658  O O   . THR A 84  ? 0.38985 0.43565 0.52286 0.02419  -0.03650 -0.02390 116  THR A O   
659  C CB  . THR A 84  ? 0.38872 0.40870 0.50450 0.03919  -0.00940 -0.02716 116  THR A CB  
660  O OG1 . THR A 84  ? 0.40231 0.40204 0.49634 0.04098  -0.00532 -0.02881 116  THR A OG1 
661  C CG2 . THR A 84  ? 0.40599 0.43343 0.53725 0.04863  -0.01809 -0.02335 116  THR A CG2 
662  N N   . LYS A 85  ? 0.34772 0.40008 0.49304 0.01752  -0.01589 -0.02601 117  LYS A N   
663  C CA  . LYS A 85  ? 0.39838 0.47401 0.56903 0.00969  -0.02136 -0.02506 117  LYS A CA  
664  C C   . LYS A 85  ? 0.44193 0.50875 0.60257 -0.00111 -0.03404 -0.02706 117  LYS A C   
665  O O   . LYS A 85  ? 0.41565 0.49791 0.58938 -0.00422 -0.04665 -0.02732 117  LYS A O   
666  C CB  . LYS A 85  ? 0.43442 0.52265 0.61867 0.00137  -0.00802 -0.02405 117  LYS A CB  
667  C CG  . LYS A 85  ? 0.53137 0.64192 0.74123 -0.01190 -0.01333 -0.02264 117  LYS A CG  
668  C CD  . LYS A 85  ? 0.65693 0.77622 0.87548 -0.02467 0.00052  -0.01927 117  LYS A CD  
669  C CE  . LYS A 85  ? 0.67105 0.79555 0.88585 -0.01666 0.01875  -0.01909 117  LYS A CE  
670  N NZ  . LYS A 85  ? 0.73440 0.86204 0.94698 -0.03154 0.03174  -0.01358 117  LYS A NZ  
671  N N   . ALA A 86  ? 0.39818 0.44031 0.53574 -0.00625 -0.03162 -0.02938 118  ALA A N   
672  C CA  . ALA A 86  ? 0.36946 0.39967 0.49710 -0.01545 -0.04201 -0.03442 118  ALA A CA  
673  C C   . ALA A 86  ? 0.40530 0.43444 0.51937 -0.01009 -0.05367 -0.03764 118  ALA A C   
674  O O   . ALA A 86  ? 0.41890 0.45452 0.53494 -0.01732 -0.06583 -0.04185 118  ALA A O   
675  C CB  . ALA A 86  ? 0.38076 0.38366 0.48914 -0.01839 -0.03650 -0.03626 118  ALA A CB  
676  N N   . VAL A 87  ? 0.36367 0.38537 0.46277 0.00095  -0.05050 -0.03533 119  VAL A N   
677  C CA  . VAL A 87  ? 0.40594 0.42665 0.48884 0.00459  -0.06027 -0.03579 119  VAL A CA  
678  C C   . VAL A 87  ? 0.45215 0.49540 0.55204 0.00626  -0.07202 -0.03060 119  VAL A C   
679  O O   . VAL A 87  ? 0.42712 0.47563 0.51741 0.00228  -0.08514 -0.03223 119  VAL A O   
680  C CB  . VAL A 87  ? 0.37684 0.38491 0.44241 0.01365  -0.05350 -0.03250 119  VAL A CB  
681  C CG1 . VAL A 87  ? 0.42622 0.43581 0.47555 0.01608  -0.06280 -0.02931 119  VAL A CG1 
682  C CG2 . VAL A 87  ? 0.37469 0.36497 0.42473 0.01213  -0.04533 -0.03791 119  VAL A CG2 
683  N N   . THR A 88  ? 0.38678 0.44503 0.51209 0.01279  -0.06794 -0.02478 120  THR A N   
684  C CA  . THR A 88  ? 0.40678 0.48935 0.55440 0.01694  -0.08003 -0.01896 120  THR A CA  
685  C C   . THR A 88  ? 0.45092 0.55214 0.61223 0.00409  -0.09176 -0.02294 120  THR A C   
686  O O   . THR A 88  ? 0.49748 0.61154 0.65816 0.00256  -0.10861 -0.02080 120  THR A O   
687  C CB  . THR A 88  ? 0.40141 0.49772 0.57817 0.02771  -0.07080 -0.01488 120  THR A CB  
688  O OG1 . THR A 88  ? 0.46843 0.54414 0.63026 0.03844  -0.06230 -0.01265 120  THR A OG1 
689  C CG2 . THR A 88  ? 0.46851 0.59247 0.67432 0.03472  -0.08411 -0.00837 120  THR A CG2 
690  N N   . LYS A 89  ? 0.40960 0.51177 0.58203 -0.00675 -0.08401 -0.02812 121  LYS A N   
691  C CA  . LYS A 89  ? 0.47227 0.58883 0.65842 -0.02225 -0.09486 -0.03282 121  LYS A CA  
692  C C   . LYS A 89  ? 0.51695 0.61603 0.67251 -0.03028 -0.10692 -0.04129 121  LYS A C   
693  O O   . LYS A 89  ? 0.55962 0.67398 0.71942 -0.03882 -0.12355 -0.04449 121  LYS A O   
694  C CB  . LYS A 89  ? 0.51696 0.63148 0.71737 -0.03377 -0.08243 -0.03477 121  LYS A CB  
695  C CG  . LYS A 89  ? 0.59173 0.73877 0.83123 -0.03259 -0.07431 -0.02876 121  LYS A CG  
696  C CD  . LYS A 89  ? 0.55757 0.69557 0.79764 -0.03616 -0.05429 -0.02691 121  LYS A CD  
697  C CE  . LYS A 89  ? 0.51350 0.63397 0.74653 -0.05537 -0.05396 -0.02942 121  LYS A CE  
698  N NZ  . LYS A 89  ? 0.62333 0.77141 0.88867 -0.07228 -0.06120 -0.02931 121  LYS A NZ  
699  N N   . TYR A 90  ? 0.47488 0.54395 0.60004 -0.02779 -0.09871 -0.04622 122  TYR A N   
700  C CA  . TYR A 90  ? 0.47082 0.52286 0.56637 -0.03399 -0.10653 -0.05721 122  TYR A CA  
701  C C   . TYR A 90  ? 0.49129 0.55332 0.56845 -0.02946 -0.11945 -0.05492 122  TYR A C   
702  O O   . TYR A 90  ? 0.55593 0.61843 0.61619 -0.03826 -0.13188 -0.06406 122  TYR A O   
703  C CB  . TYR A 90  ? 0.40934 0.43177 0.48234 -0.02932 -0.09305 -0.06210 122  TYR A CB  
704  C CG  . TYR A 90  ? 0.45830 0.46287 0.50194 -0.03262 -0.09694 -0.07562 122  TYR A CG  
705  C CD1 . TYR A 90  ? 0.48818 0.47613 0.53053 -0.04331 -0.09927 -0.08841 122  TYR A CD1 
706  C CD2 . TYR A 90  ? 0.47802 0.48098 0.49501 -0.02507 -0.09677 -0.07607 122  TYR A CD2 
707  C CE1 . TYR A 90  ? 0.50039 0.47085 0.51641 -0.04445 -0.10118 -0.10380 122  TYR A CE1 
708  C CE2 . TYR A 90  ? 0.47882 0.46859 0.46856 -0.02737 -0.09751 -0.09027 122  TYR A CE2 
709  C CZ  . TYR A 90  ? 0.55092 0.52438 0.54061 -0.03598 -0.09946 -0.10537 122  TYR A CZ  
710  O OH  . TYR A 90  ? 0.58688 0.54622 0.55011 -0.03668 -0.09901 -0.12260 122  TYR A OH  
711  N N   . THR A 91  ? 0.51470 0.58352 0.59326 -0.01675 -0.11746 -0.04271 123  THR A N   
712  C CA  . THR A 91  ? 0.60196 0.67570 0.65848 -0.01265 -0.12892 -0.03700 123  THR A CA  
713  C C   . THR A 91  ? 0.65933 0.76177 0.73469 -0.01611 -0.14873 -0.03166 123  THR A C   
714  O O   . THR A 91  ? 0.67863 0.79902 0.78198 -0.00713 -0.15224 -0.01971 123  THR A O   
715  C CB  . THR A 91  ? 0.66552 0.73141 0.71745 0.00096  -0.12040 -0.02468 123  THR A CB  
716  O OG1 . THR A 91  ? 0.57350 0.61724 0.61244 0.00279  -0.10325 -0.03012 123  THR A OG1 
717  C CG2 . THR A 91  ? 0.79858 0.86569 0.82325 0.00305  -0.13142 -0.01637 123  THR A CG2 
718  N N   . SER A 92  ? 0.82458 0.93223 0.88754 -0.02944 -0.16198 -0.04233 124  SER A N   
719  C CA  . SER A 92  ? 0.81527 0.95258 0.89281 -0.03502 -0.18420 -0.03835 124  SER A CA  
720  C C   . SER A 92  ? 1.05709 1.20037 1.10982 -0.02767 -0.19726 -0.02589 124  SER A C   
721  O O   . SER A 92  ? 1.07232 1.19604 1.08611 -0.02588 -0.19121 -0.02685 124  SER A O   
722  C CB  . SER A 92  ? 0.82607 0.96484 0.89562 -0.05398 -0.19523 -0.05567 124  SER A CB  
723  O OG  . SER A 92  ? 0.84983 0.96967 0.87236 -0.05861 -0.19697 -0.06720 124  SER A OG  
724  N N   . ALA A 93  ? 1.27640 1.44842 1.35327 -0.02344 -0.21534 -0.01282 125  ALA A N   
725  C CA  . ALA A 93  ? 1.44263 1.61954 1.49692 -0.01620 -0.23019 0.00310  125  ALA A CA  
726  C C   . ALA A 93  ? 1.44546 1.61892 1.45074 -0.02961 -0.24221 -0.00564 125  ALA A C   
727  O O   . ALA A 93  ? 1.46668 1.63065 1.43462 -0.02634 -0.24433 0.00401  125  ALA A O   
728  C CB  . ALA A 93  ? 1.43222 1.64284 1.52571 -0.00833 -0.25023 0.01869  125  ALA A CB  
729  N N   . LYS A 94  ? 1.29569 1.47640 1.29936 -0.04571 -0.24978 -0.02413 126  LYS A N   
730  C CA  . LYS A 94  ? 1.20230 1.37878 1.15813 -0.05943 -0.26008 -0.03779 126  LYS A CA  
731  C C   . LYS A 94  ? 1.11816 1.26146 1.04319 -0.06211 -0.23711 -0.05620 126  LYS A C   
732  O O   . LYS A 94  ? 1.02587 1.15583 0.96664 -0.06790 -0.22624 -0.07255 126  LYS A O   
733  C CB  . LYS A 94  ? 1.04883 1.24713 1.01877 -0.07532 -0.27793 -0.05123 126  LYS A CB  
734  C CG  . LYS A 94  ? 1.18590 1.38362 1.10843 -0.08435 -0.28481 -0.06511 126  LYS A CG  
735  C CD  . LYS A 94  ? 1.18348 1.41323 1.11563 -0.08659 -0.30601 -0.06099 126  LYS A CD  
736  C CE  . LYS A 94  ? 1.11685 1.33952 1.00153 -0.09614 -0.31275 -0.08068 126  LYS A CE  
737  N NZ  . LYS A 94  ? 1.02868 1.27868 0.92606 -0.10342 -0.33461 -0.08567 126  LYS A NZ  
738  N N   . LYS A 95  ? 1.17778 1.30864 1.06061 -0.05790 -0.22974 -0.05248 1014 LYS A N   
739  C CA  . LYS A 95  ? 1.21376 1.31836 1.06946 -0.05875 -0.20810 -0.06995 1014 LYS A CA  
740  C C   . LYS A 95  ? 1.12348 1.22371 0.95137 -0.07357 -0.21433 -0.09694 1014 LYS A C   
741  O O   . LYS A 95  ? 1.11845 1.23626 0.92794 -0.08400 -0.23577 -0.09968 1014 LYS A O   
742  C CB  . LYS A 95  ? 1.26064 1.35819 1.08201 -0.05149 -0.19747 -0.05786 1014 LYS A CB  
743  C CG  . LYS A 95  ? 1.17717 1.25240 0.98187 -0.04899 -0.17242 -0.07324 1014 LYS A CG  
744  C CD  . LYS A 95  ? 1.12196 1.18223 0.96637 -0.04320 -0.15822 -0.07916 1014 LYS A CD  
745  C CE  . LYS A 95  ? 1.23093 1.27076 1.06115 -0.04183 -0.13835 -0.09882 1014 LYS A CE  
746  N NZ  . LYS A 95  ? 1.20652 1.23092 1.07170 -0.03574 -0.12542 -0.10099 1014 LYS A NZ  
747  N N   . ALA A 96  ? 1.04002 1.11567 0.86590 -0.07405 -0.19633 -0.11734 1015 ALA A N   
748  C CA  . ALA A 96  ? 1.02962 1.09039 0.83354 -0.08524 -0.19644 -0.14729 1015 ALA A CA  
749  C C   . ALA A 96  ? 0.90720 0.96810 0.74591 -0.09685 -0.20870 -0.15625 1015 ALA A C   
750  O O   . ALA A 96  ? 0.82552 0.86867 0.65327 -0.10883 -0.20763 -0.17692 1015 ALA A O   
751  C CB  . ALA A 96  ? 1.11046 1.17593 0.86579 -0.09168 -0.20643 -0.15553 1015 ALA A CB  
752  N N   . LYS A 97  ? 0.73783 0.81698 0.61898 -0.09495 -0.21599 -0.13668 1016 LYS A N   
753  C CA  . LYS A 97  ? 0.67687 0.76100 0.59895 -0.10596 -0.22413 -0.14052 1016 LYS A CA  
754  C C   . LYS A 97  ? 0.60845 0.67607 0.56560 -0.09850 -0.20416 -0.13451 1016 LYS A C   
755  O O   . LYS A 97  ? 0.54755 0.62424 0.54367 -0.10598 -0.20769 -0.13079 1016 LYS A O   
756  C CB  . LYS A 97  ? 0.70646 0.82972 0.65415 -0.10988 -0.24618 -0.12388 1016 LYS A CB  
757  C CG  . LYS A 97  ? 0.69979 0.84273 0.61663 -0.11726 -0.25999 -0.13076 1016 LYS A CG  
758  C CD  . LYS A 97  ? 0.70559 0.83911 0.61647 -0.13438 -0.26019 -0.15805 1016 LYS A CD  
759  C CE  . LYS A 97  ? 0.72289 0.86537 0.60200 -0.13364 -0.27668 -0.16986 1016 LYS A CE  
760  N NZ  . LYS A 97  ? 0.84831 1.02769 0.73634 -0.12821 -0.29647 -0.14795 1016 LYS A NZ  
761  N N   . THR A 98  ? 0.57410 0.62181 0.51915 -0.08448 -0.18370 -0.13152 1017 THR A N   
762  C CA  . THR A 98  ? 0.46569 0.49891 0.44025 -0.07812 -0.16664 -0.12526 1017 THR A CA  
763  C C   . THR A 98  ? 0.48005 0.48948 0.46508 -0.09030 -0.16472 -0.14211 1017 THR A C   
764  O O   . THR A 98  ? 0.58126 0.57316 0.54261 -0.09852 -0.16939 -0.16319 1017 THR A O   
765  C CB  . THR A 98  ? 0.66109 0.67794 0.61899 -0.06235 -0.14718 -0.12085 1017 THR A CB  
766  O OG1 . THR A 98  ? 0.74500 0.73620 0.67699 -0.06303 -0.13927 -0.14117 1017 THR A OG1 
767  C CG2 . THR A 98  ? 0.69324 0.72722 0.63167 -0.05370 -0.15013 -0.10692 1017 THR A CG2 
768  N N   . ARG A 99  ? 0.54576 0.55359 0.56593 -0.09187 -0.15756 -0.13254 1018 ARG A N   
769  C CA  . ARG A 99  ? 0.48592 0.46706 0.51917 -0.10257 -0.15311 -0.14231 1018 ARG A CA  
770  C C   . ARG A 99  ? 0.49331 0.46255 0.54216 -0.09181 -0.13448 -0.12870 1018 ARG A C   
771  O O   . ARG A 99  ? 0.43760 0.42954 0.50638 -0.08548 -0.12987 -0.11131 1018 ARG A O   
772  C CB  . ARG A 99  ? 0.44724 0.44434 0.51099 -0.12292 -0.16685 -0.14247 1018 ARG A CB  
773  C CG  . ARG A 99  ? 0.47899 0.49284 0.53093 -0.13674 -0.18922 -0.15554 1018 ARG A CG  
774  C CD  . ARG A 99  ? 0.48758 0.52600 0.57447 -0.15748 -0.20129 -0.15220 1018 ARG A CD  
775  N NE  . ARG A 99  ? 0.51729 0.59638 0.64309 -0.15301 -0.20413 -0.13193 1018 ARG A NE  
776  C CZ  . ARG A 99  ? 0.51277 0.60011 0.67613 -0.15688 -0.19329 -0.11983 1018 ARG A CZ  
777  N NH1 . ARG A 99  ? 0.44152 0.49806 0.61089 -0.16802 -0.18340 -0.12434 1018 ARG A NH1 
778  N NH2 . ARG A 99  ? 0.42440 0.55142 0.61958 -0.14903 -0.19194 -0.10248 1018 ARG A NH2 
779  N N   . SER A 100 ? 0.53350 0.46722 0.57368 -0.08940 -0.12452 -0.13701 1019 SER A N   
780  C CA  . SER A 100 ? 0.49987 0.42229 0.55248 -0.08038 -0.10900 -0.12341 1019 SER A CA  
781  C C   . SER A 100 ? 0.50723 0.44409 0.59282 -0.09136 -0.10814 -0.10907 1019 SER A C   
782  O O   . SER A 100 ? 0.46502 0.41264 0.56206 -0.08340 -0.09718 -0.09367 1019 SER A O   
783  C CB  . SER A 100 ? 0.65062 0.53227 0.69223 -0.07695 -0.10205 -0.13398 1019 SER A CB  
784  O OG  . SER A 100 ? 0.66144 0.53594 0.67568 -0.06383 -0.09858 -0.14618 1019 SER A OG  
785  N N   . SER A 101 ? 0.46480 0.40599 0.56586 -0.11055 -0.11958 -0.11466 1020 SER A N   
786  C CA  . SER A 101 ? 0.45393 0.41180 0.58878 -0.12408 -0.11770 -0.10180 1020 SER A CA  
787  C C   . SER A 101 ? 0.48402 0.48524 0.63864 -0.11621 -0.11467 -0.08699 1020 SER A C   
788  O O   . SER A 101 ? 0.45282 0.46870 0.63205 -0.11982 -0.10495 -0.07395 1020 SER A O   
789  C CB  . SER A 101 ? 0.48132 0.44030 0.62921 -0.14772 -0.13320 -0.11266 1020 SER A CB  
790  O OG  . SER A 101 ? 0.52904 0.51585 0.71390 -0.16312 -0.13302 -0.10048 1020 SER A OG  
791  N N   . ARG A 102 ? 0.40184 0.42142 0.54433 -0.10399 -0.12107 -0.08821 1021 ARG A N   
792  C CA  . ARG A 102 ? 0.42253 0.47851 0.58470 -0.09388 -0.11900 -0.07467 1021 ARG A CA  
793  C C   . ARG A 102 ? 0.50033 0.54947 0.66130 -0.07931 -0.10014 -0.06383 1021 ARG A C   
794  O O   . ARG A 102 ? 0.45942 0.53464 0.64328 -0.07357 -0.09381 -0.05336 1021 ARG A O   
795  C CB  . ARG A 102 ? 0.45649 0.52818 0.60324 -0.08468 -0.13194 -0.07644 1021 ARG A CB  
796  C CG  . ARG A 102 ? 0.41375 0.50777 0.57037 -0.09919 -0.15301 -0.08296 1021 ARG A CG  
797  C CD  . ARG A 102 ? 0.52382 0.63129 0.65911 -0.09015 -0.16672 -0.08237 1021 ARG A CD  
798  N NE  . ARG A 102 ? 0.52414 0.65347 0.67398 -0.07296 -0.16302 -0.06580 1021 ARG A NE  
799  C CZ  . ARG A 102 ? 0.53359 0.69636 0.70039 -0.06934 -0.17844 -0.05710 1021 ARG A CZ  
800  N NH1 . ARG A 102 ? 0.50644 0.68859 0.67597 -0.08249 -0.19984 -0.06269 1021 ARG A NH1 
801  N NH2 . ARG A 102 ? 0.60084 0.77687 0.78206 -0.05176 -0.17342 -0.04275 1021 ARG A NH2 
802  N N   . ALA A 103 ? 0.43839 0.45453 0.57364 -0.07249 -0.09149 -0.06727 1022 ALA A N   
803  C CA  . ALA A 103 ? 0.45352 0.46405 0.58546 -0.05993 -0.07577 -0.05775 1022 ALA A CA  
804  C C   . ALA A 103 ? 0.48298 0.49662 0.63510 -0.06825 -0.06490 -0.04867 1022 ALA A C   
805  O O   . ALA A 103 ? 0.46578 0.48239 0.61764 -0.05940 -0.05224 -0.04047 1022 ALA A O   
806  C CB  . ALA A 103 ? 0.42774 0.40631 0.53084 -0.05140 -0.07088 -0.06339 1022 ALA A CB  
807  N N   . GLY A 104 ? 0.46321 0.47666 0.63129 -0.08641 -0.06948 -0.04998 1023 GLY A N   
808  C CA  . GLY A 104 ? 0.46081 0.48008 0.64819 -0.09791 -0.05887 -0.03955 1023 GLY A CA  
809  C C   . GLY A 104 ? 0.46864 0.45477 0.63887 -0.09753 -0.04841 -0.03341 1023 GLY A C   
810  O O   . GLY A 104 ? 0.52692 0.52112 0.70618 -0.10271 -0.03635 -0.02164 1023 GLY A O   
811  N N   . LEU A 105 ? 0.46469 0.41557 0.61092 -0.09145 -0.05265 -0.04067 1024 LEU A N   
812  C CA  . LEU A 105 ? 0.50685 0.42788 0.63673 -0.08606 -0.04481 -0.03399 1024 LEU A CA  
813  C C   . LEU A 105 ? 0.54847 0.43233 0.67643 -0.09830 -0.05003 -0.03553 1024 LEU A C   
814  O O   . LEU A 105 ? 0.57720 0.45143 0.70973 -0.10842 -0.06070 -0.04722 1024 LEU A O   
815  C CB  . LEU A 105 ? 0.47741 0.38745 0.58471 -0.06631 -0.04443 -0.04019 1024 LEU A CB  
816  C CG  . LEU A 105 ? 0.45057 0.38727 0.55498 -0.05279 -0.04063 -0.03964 1024 LEU A CG  
817  C CD1 . LEU A 105 ? 0.47620 0.39884 0.55916 -0.03771 -0.04082 -0.04582 1024 LEU A CD1 
818  C CD2 . LEU A 105 ? 0.43813 0.39206 0.54959 -0.05135 -0.02856 -0.02730 1024 LEU A CD2 
819  N N   . GLN A 106 ? 0.56030 0.42077 0.67975 -0.09671 -0.04343 -0.02371 1025 GLN A N   
820  C CA  . GLN A 106 ? 0.60063 0.41717 0.71514 -0.10264 -0.04839 -0.02309 1025 GLN A CA  
821  C C   . GLN A 106 ? 0.60694 0.39727 0.70339 -0.08304 -0.05168 -0.03324 1025 GLN A C   
822  O O   . GLN A 106 ? 0.63291 0.38928 0.72689 -0.08381 -0.05900 -0.04383 1025 GLN A O   
823  C CB  . GLN A 106 ? 0.63210 0.43707 0.74687 -0.11133 -0.04070 -0.00127 1025 GLN A CB  
824  C CG  . GLN A 106 ? 0.65520 0.48956 0.78774 -0.13084 -0.03317 0.01108  1025 GLN A CG  
825  C CD  . GLN A 106 ? 0.71398 0.54948 0.86761 -0.15210 -0.04090 0.00433  1025 GLN A CD  
826  O OE1 . GLN A 106 ? 0.75755 0.55440 0.91111 -0.16217 -0.04943 0.00113  1025 GLN A OE1 
827  N NE2 . GLN A 106 ? 0.72145 0.60118 0.89504 -0.15893 -0.03888 0.00144  1025 GLN A NE2 
828  N N   . PHE A 107 ? 0.58814 0.39411 0.67359 -0.06570 -0.04589 -0.03103 1026 PHE A N   
829  C CA  . PHE A 107 ? 0.55458 0.34410 0.62685 -0.04718 -0.04757 -0.04023 1026 PHE A CA  
830  C C   . PHE A 107 ? 0.59662 0.38999 0.66434 -0.04311 -0.05315 -0.06172 1026 PHE A C   
831  O O   . PHE A 107 ? 0.61470 0.43349 0.68608 -0.04987 -0.05537 -0.06655 1026 PHE A O   
832  C CB  . PHE A 107 ? 0.49759 0.30638 0.56118 -0.03329 -0.04035 -0.03161 1026 PHE A CB  
833  C CG  . PHE A 107 ? 0.55332 0.34546 0.61285 -0.03102 -0.03813 -0.01466 1026 PHE A CG  
834  C CD1 . PHE A 107 ? 0.56119 0.34666 0.62512 -0.04637 -0.03611 0.00123  1026 PHE A CD1 
835  C CD2 . PHE A 107 ? 0.58619 0.37146 0.63772 -0.01448 -0.03863 -0.01357 1026 PHE A CD2 
836  C CE1 . PHE A 107 ? 0.59828 0.36757 0.65449 -0.04521 -0.03540 0.01908  1026 PHE A CE1 
837  C CE2 . PHE A 107 ? 0.58305 0.35438 0.63004 -0.01225 -0.03932 0.00354  1026 PHE A CE2 
838  C CZ  . PHE A 107 ? 0.54540 0.30742 0.59260 -0.02758 -0.03806 0.02040  1026 PHE A CZ  
839  N N   . PRO A 108 ? 0.58392 0.35241 0.64387 -0.03247 -0.05590 -0.07505 1027 PRO A N   
840  C CA  . PRO A 108 ? 0.62797 0.39609 0.67995 -0.03161 -0.06091 -0.09744 1027 PRO A CA  
841  C C   . PRO A 108 ? 0.61379 0.41105 0.65360 -0.01947 -0.05681 -0.10301 1027 PRO A C   
842  O O   . PRO A 108 ? 0.61869 0.41495 0.65216 -0.00382 -0.05128 -0.10479 1027 PRO A O   
843  C CB  . PRO A 108 ? 0.68515 0.41300 0.73498 -0.02370 -0.06303 -0.10954 1027 PRO A CB  
844  C CG  . PRO A 108 ? 0.67053 0.39047 0.72407 -0.01080 -0.05792 -0.09324 1027 PRO A CG  
845  C CD  . PRO A 108 ? 0.63638 0.37478 0.69562 -0.02113 -0.05509 -0.07041 1027 PRO A CD  
846  N N   . VAL A 109 ? 0.57494 0.39763 0.61203 -0.02700 -0.06057 -0.10648 1028 VAL A N   
847  C CA  . VAL A 109 ? 0.56105 0.40931 0.58516 -0.01796 -0.05791 -0.10943 1028 VAL A CA  
848  C C   . VAL A 109 ? 0.54808 0.38593 0.55522 -0.00824 -0.05627 -0.12804 1028 VAL A C   
849  O O   . VAL A 109 ? 0.52169 0.37005 0.52090 0.00419  -0.04885 -0.12760 1028 VAL A O   
850  C CB  . VAL A 109 ? 0.53840 0.41261 0.56409 -0.02829 -0.06528 -0.10831 1028 VAL A CB  
851  C CG1 . VAL A 109 ? 0.57510 0.46965 0.58348 -0.02055 -0.06478 -0.11156 1028 VAL A CG1 
852  C CG2 . VAL A 109 ? 0.53536 0.42647 0.58055 -0.03389 -0.06323 -0.09036 1028 VAL A CG2 
853  N N   . GLY A 110 ? 0.56238 0.38003 0.56434 -0.01447 -0.06242 -0.14581 1029 GLY A N   
854  C CA  . GLY A 110 ? 0.58950 0.39931 0.57364 -0.00532 -0.05935 -0.16705 1029 GLY A CA  
855  C C   . GLY A 110 ? 0.66697 0.46051 0.65655 0.01186  -0.05010 -0.16887 1029 GLY A C   
856  O O   . GLY A 110 ? 0.62835 0.43438 0.60748 0.02396  -0.04175 -0.17673 1029 GLY A O   
857  N N   . ARG A 111 ? 0.54079 0.31096 0.54724 0.01242  -0.05073 -0.15777 1030 ARG A N   
858  C CA  . ARG A 111 ? 0.61523 0.37489 0.62918 0.02875  -0.04324 -0.15270 1030 ARG A CA  
859  C C   . ARG A 111 ? 0.58466 0.37016 0.60130 0.03979  -0.03779 -0.14309 1030 ARG A C   
860  O O   . ARG A 111 ? 0.58837 0.38305 0.60474 0.05423  -0.03020 -0.14821 1030 ARG A O   
861  C CB  . ARG A 111 ? 0.70935 0.44051 0.73801 0.02430  -0.04737 -0.13808 1030 ARG A CB  
862  C CG  . ARG A 111 ? 0.85829 0.58099 0.89751 0.03957  -0.04377 -0.12561 1030 ARG A CG  
863  C CD  . ARG A 111 ? 0.97034 0.66786 1.01091 0.04902  -0.04117 -0.13492 1030 ARG A CD  
864  N NE  . ARG A 111 ? 1.08963 0.75605 1.12955 0.03478  -0.04663 -0.13712 1030 ARG A NE  
865  C CZ  . ARG A 111 ? 1.09739 0.73515 1.14664 0.03145  -0.05049 -0.12254 1030 ARG A CZ  
866  N NH1 . ARG A 111 ? 1.01193 0.64822 1.07051 0.04143  -0.05084 -0.10358 1030 ARG A NH1 
867  N NH2 . ARG A 111 ? 0.99900 0.60930 1.04707 0.01659  -0.05468 -0.12628 1030 ARG A NH2 
868  N N   . VAL A 112 ? 0.54257 0.34767 0.56073 0.03099  -0.03877 -0.12496 1031 VAL A N   
869  C CA  . VAL A 112 ? 0.49827 0.32972 0.51635 0.03799  -0.03267 -0.11279 1031 VAL A CA  
870  C C   . VAL A 112 ? 0.55946 0.41424 0.56384 0.04206  -0.02731 -0.12350 1031 VAL A C   
871  O O   . VAL A 112 ? 0.50235 0.37269 0.50778 0.05177  -0.02050 -0.12158 1031 VAL A O   
872  C CB  . VAL A 112 ? 0.47278 0.31701 0.49460 0.02770  -0.03430 -0.09440 1031 VAL A CB  
873  C CG1 . VAL A 112 ? 0.44481 0.31357 0.46434 0.03319  -0.02874 -0.08485 1031 VAL A CG1 
874  C CG2 . VAL A 112 ? 0.55714 0.38045 0.58999 0.02398  -0.03710 -0.08184 1031 VAL A CG2 
875  N N   . HIS A 113 ? 0.51882 0.37767 0.50969 0.03344  -0.03080 -0.13413 1032 HIS A N   
876  C CA  . HIS A 113 ? 0.55616 0.43601 0.52928 0.03572  -0.02582 -0.14312 1032 HIS A CA  
877  C C   . HIS A 113 ? 0.56401 0.44010 0.53499 0.04883  -0.01714 -0.15991 1032 HIS A C   
878  O O   . HIS A 113 ? 0.54601 0.44390 0.51312 0.05549  -0.00809 -0.15954 1032 HIS A O   
879  C CB  . HIS A 113 ? 0.51162 0.39517 0.46823 0.02365  -0.03362 -0.15153 1032 HIS A CB  
880  C CG  . HIS A 113 ? 0.51574 0.42527 0.45259 0.02194  -0.03113 -0.14980 1032 HIS A CG  
881  N ND1 . HIS A 113 ? 0.56264 0.48118 0.48184 0.01166  -0.03973 -0.15344 1032 HIS A ND1 
882  C CD2 . HIS A 113 ? 0.54716 0.47551 0.47919 0.02789  -0.02196 -0.14271 1032 HIS A CD2 
883  C CE1 . HIS A 113 ? 0.64948 0.58925 0.55190 0.01205  -0.03589 -0.14729 1032 HIS A CE1 
884  N NE2 . HIS A 113 ? 0.57719 0.52267 0.48753 0.02104  -0.02446 -0.14086 1032 HIS A NE2 
885  N N   . ARG A 114 ? 0.58257 0.43110 0.55804 0.05261  -0.01932 -0.17519 1033 ARG A N   
886  C CA  . ARG A 114 ? 0.58150 0.42840 0.55727 0.06519  -0.00917 -0.18737 1033 ARG A CA  
887  C C   . ARG A 114 ? 0.56702 0.42375 0.56310 0.07956  -0.00301 -0.17700 1033 ARG A C   
888  O O   . ARG A 114 ? 0.59311 0.46930 0.58998 0.08945  0.00759  -0.18354 1033 ARG A O   
889  C CB  . ARG A 114 ? 0.65713 0.47095 0.63494 0.06402  -0.01219 -0.19626 1033 ARG A CB  
890  C CG  . ARG A 114 ? 0.83638 0.64585 0.81460 0.07773  -0.00162 -0.20989 1033 ARG A CG  
891  C CD  . ARG A 114 ? 0.96210 0.73406 0.94011 0.07582  -0.00531 -0.21974 1033 ARG A CD  
892  N NE  . ARG A 114 ? 1.03769 0.78469 1.03585 0.07551  -0.01310 -0.20374 1033 ARG A NE  
893  C CZ  . ARG A 114 ? 1.20824 0.94690 1.22586 0.09016  -0.01070 -0.19486 1033 ARG A CZ  
894  N NH1 . ARG A 114 ? 1.16714 0.92212 1.19118 0.10687  -0.00074 -0.20108 1033 ARG A NH1 
895  N NH2 . ARG A 114 ? 1.10722 0.82273 1.13847 0.08748  -0.01877 -0.17833 1033 ARG A NH2 
896  N N   . LEU A 115 ? 0.56454 0.41017 0.57723 0.08004  -0.00976 -0.16047 1034 LEU A N   
897  C CA  . LEU A 115 ? 0.59226 0.44879 0.62342 0.09268  -0.00675 -0.14959 1034 LEU A CA  
898  C C   . LEU A 115 ? 0.58526 0.47780 0.61271 0.09119  -0.00073 -0.14246 1034 LEU A C   
899  O O   . LEU A 115 ? 0.52249 0.43482 0.56216 0.10198  0.00571  -0.14254 1034 LEU A O   
900  C CB  . LEU A 115 ? 0.62117 0.45725 0.66531 0.09117  -0.01617 -0.13164 1034 LEU A CB  
901  C CG  . LEU A 115 ? 0.77162 0.57290 0.82086 0.09107  -0.02086 -0.13135 1034 LEU A CG  
902  C CD1 . LEU A 115 ? 0.72841 0.51110 0.78472 0.08457  -0.02995 -0.11157 1034 LEU A CD1 
903  C CD2 . LEU A 115 ? 0.80201 0.60003 0.86306 0.10782  -0.01569 -0.13718 1034 LEU A CD2 
904  N N   . LEU A 116 ? 0.53378 0.43621 0.54648 0.07683  -0.00300 -0.13376 1035 LEU A N   
905  C CA  . LEU A 116 ? 0.50186 0.43415 0.50892 0.07320  0.00270  -0.12555 1035 LEU A CA  
906  C C   . LEU A 116 ? 0.50383 0.45557 0.50120 0.07718  0.01329  -0.14026 1035 LEU A C   
907  O O   . LEU A 116 ? 0.48613 0.46252 0.48990 0.08075  0.02126  -0.13711 1035 LEU A O   
908  C CB  . LEU A 116 ? 0.45203 0.38716 0.44619 0.05910  -0.00250 -0.11453 1035 LEU A CB  
909  C CG  . LEU A 116 ? 0.46304 0.39077 0.46665 0.05453  -0.00872 -0.09777 1035 LEU A CG  
910  C CD1 . LEU A 116 ? 0.46162 0.39163 0.45613 0.04320  -0.01337 -0.09112 1035 LEU A CD1 
911  C CD2 . LEU A 116 ? 0.42645 0.36881 0.43918 0.05820  -0.00556 -0.08710 1035 LEU A CD2 
912  N N   . ARG A 117 ? 0.50788 0.45024 0.48915 0.07540  0.01388  -0.15711 1036 ARG A N   
913  C CA  . ARG A 117 ? 0.56855 0.52989 0.53651 0.07896  0.02563  -0.17327 1036 ARG A CA  
914  C C   . ARG A 117 ? 0.60970 0.57789 0.59911 0.09653  0.03540  -0.18466 1036 ARG A C   
915  O O   . ARG A 117 ? 0.64630 0.64436 0.63672 0.09996  0.04790  -0.18784 1036 ARG A O   
916  C CB  . ARG A 117 ? 0.59291 0.54017 0.53648 0.07261  0.02229  -0.19070 1036 ARG A CB  
917  C CG  . ARG A 117 ? 0.61888 0.58119 0.53553 0.05727  0.01878  -0.18225 1036 ARG A CG  
918  C CD  . ARG A 117 ? 0.70741 0.65555 0.60109 0.04810  0.00973  -0.19582 1036 ARG A CD  
919  N NE  . ARG A 117 ? 0.74184 0.70208 0.61838 0.03451  0.00107  -0.18032 1036 ARG A NE  
920  C CZ  . ARG A 117 ? 0.74111 0.69703 0.59813 0.02387  -0.01021 -0.18559 1036 ARG A CZ  
921  N NH1 . ARG A 117 ? 0.72407 0.66031 0.57649 0.02250  -0.01541 -0.20616 1036 ARG A NH1 
922  N NH2 . ARG A 117 ? 0.76656 0.73755 0.60944 0.01423  -0.01769 -0.16958 1036 ARG A NH2 
923  N N   . LYS A 118 ? 0.61312 0.55514 0.62072 0.10468  0.02955  -0.18345 1037 LYS A N   
924  C CA  . LYS A 118 ? 0.65678 0.60298 0.68605 0.12016  0.03650  -0.18709 1037 LYS A CA  
925  C C   . LYS A 118 ? 0.65273 0.62868 0.70494 0.12709  0.03951  -0.17561 1037 LYS A C   
926  O O   . LYS A 118 ? 0.56944 0.56668 0.63779 0.13784  0.04894  -0.18012 1037 LYS A O   
927  C CB  . LYS A 118 ? 0.68672 0.59597 0.72918 0.12659  0.02761  -0.18467 1037 LYS A CB  
928  C CG  . LYS A 118 ? 0.77927 0.68655 0.84097 0.14399  0.03421  -0.19170 1037 LYS A CG  
929  C CD  . LYS A 118 ? 0.84170 0.70816 0.91308 0.14924  0.02493  -0.18816 1037 LYS A CD  
930  C CE  . LYS A 118 ? 0.87356 0.72760 0.95346 0.14385  0.01147  -0.16660 1037 LYS A CE  
931  N NZ  . LYS A 118 ? 0.85778 0.73500 0.95975 0.15303  0.00914  -0.15142 1037 LYS A NZ  
932  N N   . GLY A 119 ? 0.58402 0.56314 0.63880 0.12067  0.03157  -0.16111 1038 GLY A N   
933  C CA  . GLY A 119 ? 0.55731 0.56122 0.63230 0.12319  0.03137  -0.14618 1038 GLY A CA  
934  C C   . GLY A 119 ? 0.52372 0.56627 0.59546 0.11611  0.04251  -0.14445 1038 GLY A C   
935  O O   . GLY A 119 ? 0.55059 0.61647 0.64120 0.11689  0.04243  -0.13393 1038 GLY A O   
936  N N   . ASN A 120 ? 0.54238 0.59223 0.58956 0.10761  0.05119  -0.15348 1039 ASN A N   
937  C CA  . ASN A 120 ? 0.51345 0.59860 0.55343 0.09848  0.06313  -0.15057 1039 ASN A CA  
938  C C   . ASN A 120 ? 0.52167 0.61577 0.56589 0.08596  0.05708  -0.12861 1039 ASN A C   
939  O O   . ASN A 120 ? 0.52844 0.65244 0.58742 0.08325  0.06349  -0.12296 1039 ASN A O   
940  C CB  . ASN A 120 ? 0.62444 0.74188 0.68620 0.11158  0.07785  -0.16401 1039 ASN A CB  
941  C CG  . ASN A 120 ? 0.71765 0.82109 0.77170 0.12194  0.08412  -0.18403 1039 ASN A CG  
942  O OD1 . ASN A 120 ? 0.78555 0.87553 0.80819 0.11391  0.08563  -0.19224 1039 ASN A OD1 
943  N ND2 . ASN A 120 ? 0.76886 0.87315 0.84937 0.13747  0.08625  -0.18834 1039 ASN A ND2 
944  N N   . TYR A 121 ? 0.45959 0.52763 0.49215 0.07801  0.04480  -0.11743 1040 TYR A N   
945  C CA  . TYR A 121 ? 0.38473 0.45514 0.41730 0.06622  0.03899  -0.09941 1040 TYR A CA  
946  C C   . TYR A 121 ? 0.44499 0.52681 0.45751 0.05160  0.04461  -0.09269 1040 TYR A C   
947  O O   . TYR A 121 ? 0.41583 0.50505 0.43166 0.04188  0.04334  -0.07989 1040 TYR A O   
948  C CB  . TYR A 121 ? 0.43128 0.47162 0.45861 0.06408  0.02622  -0.09181 1040 TYR A CB  
949  C CG  . TYR A 121 ? 0.39560 0.42160 0.44019 0.07600  0.01949  -0.09373 1040 TYR A CG  
950  C CD1 . TYR A 121 ? 0.40943 0.44604 0.47396 0.08066  0.01578  -0.08637 1040 TYR A CD1 
951  C CD2 . TYR A 121 ? 0.44316 0.44402 0.48341 0.08136  0.01552  -0.10177 1040 TYR A CD2 
952  C CE1 . TYR A 121 ? 0.45576 0.47791 0.53412 0.09166  0.00800  -0.08501 1040 TYR A CE1 
953  C CE2 . TYR A 121 ? 0.46211 0.44576 0.51730 0.09134  0.00879  -0.10086 1040 TYR A CE2 
954  C CZ  . TYR A 121 ? 0.51636 0.51062 0.58980 0.09701  0.00495  -0.09143 1040 TYR A CZ  
955  O OH  . TYR A 121 ? 0.57841 0.55460 0.66476 0.10695  -0.00322 -0.08756 1040 TYR A OH  
956  N N   . ALA A 122 ? 0.46242 0.54388 0.45276 0.04925  0.04985  -0.10077 1041 ALA A N   
957  C CA  . ALA A 122 ? 0.41264 0.50500 0.38038 0.03578  0.05502  -0.09311 1041 ALA A CA  
958  C C   . ALA A 122 ? 0.52012 0.61891 0.46603 0.03766  0.06309  -0.10824 1041 ALA A C   
959  O O   . ALA A 122 ? 0.49376 0.58265 0.44213 0.04877  0.06279  -0.12511 1041 ALA A O   
960  C CB  . ALA A 122 ? 0.43324 0.50428 0.38673 0.02611  0.04326  -0.07833 1041 ALA A CB  
961  N N   . GLU A 123 ? 0.49231 0.60555 0.41452 0.02576  0.06981  -0.10188 1042 GLU A N   
962  C CA  . GLU A 123 ? 0.49212 0.61351 0.38656 0.02530  0.07765  -0.11613 1042 GLU A CA  
963  C C   . GLU A 123 ? 0.56050 0.65484 0.43785 0.02726  0.06442  -0.12399 1042 GLU A C   
964  O O   . GLU A 123 ? 0.58992 0.68165 0.45759 0.03404  0.06802  -0.14510 1042 GLU A O   
965  C CB  . GLU A 123 ? 0.57069 0.70954 0.43751 0.00954  0.08457  -0.10289 1042 GLU A CB  
966  C CG  . GLU A 123 ? 0.79689 0.97167 0.67064 0.00613  0.10420  -0.10422 1042 GLU A CG  
967  C CD  . GLU A 123 ? 0.96765 1.15686 0.80683 -0.01126 0.11122  -0.09070 1042 GLU A CD  
968  O OE1 . GLU A 123 ? 1.02873 1.20425 0.83344 -0.01585 0.10318  -0.08976 1042 GLU A OE1 
969  O OE2 . GLU A 123 ? 1.01606 1.23056 0.86223 -0.02123 0.12376  -0.08018 1042 GLU A OE2 
970  N N   . ARG A 124 ? 0.52536 0.60019 0.40051 0.02124  0.04926  -0.10851 1043 ARG A N   
971  C CA  . ARG A 124 ? 0.57090 0.62473 0.43377 0.02081  0.03559  -0.11365 1043 ARG A CA  
972  C C   . ARG A 124 ? 0.51472 0.54833 0.40082 0.02323  0.02324  -0.10356 1043 ARG A C   
973  O O   . ARG A 124 ? 0.47082 0.50558 0.37275 0.02210  0.02324  -0.08915 1043 ARG A O   
974  C CB  . ARG A 124 ? 0.63779 0.69539 0.46690 0.00895  0.02932  -0.10456 1043 ARG A CB  
975  C CG  . ARG A 124 ? 0.68484 0.76272 0.48279 0.00486  0.04161  -0.11605 1043 ARG A CG  
976  C CD  . ARG A 124 ? 0.82574 0.90982 0.58905 -0.00849 0.03510  -0.09980 1043 ARG A CD  
977  N NE  . ARG A 124 ? 1.03287 1.09813 0.79958 -0.01057 0.01463  -0.08759 1043 ARG A NE  
978  C CZ  . ARG A 124 ? 0.99137 1.05236 0.75858 -0.01633 0.00566  -0.06287 1043 ARG A CZ  
979  N NH1 . ARG A 124 ? 1.05749 1.12834 0.81674 -0.02343 0.01390  -0.04606 1043 ARG A NH1 
980  N NH2 . ARG A 124 ? 0.84373 0.88987 0.62254 -0.01481 -0.01148 -0.05493 1043 ARG A NH2 
981  N N   . VAL A 125 ? 0.53310 0.54878 0.42053 0.02545  0.01335  -0.11230 1044 VAL A N   
982  C CA  . VAL A 125 ? 0.46381 0.46251 0.37063 0.02618  0.00266  -0.10361 1044 VAL A CA  
983  C C   . VAL A 125 ? 0.53441 0.52695 0.42897 0.01875  -0.01051 -0.10040 1044 VAL A C   
984  O O   . VAL A 125 ? 0.55448 0.54239 0.43643 0.01674  -0.01489 -0.11465 1044 VAL A O   
985  C CB  . VAL A 125 ? 0.48892 0.47245 0.41553 0.03496  0.00290  -0.11492 1044 VAL A CB  
986  C CG1 . VAL A 125 ? 0.53208 0.50056 0.47501 0.03315  -0.00682 -0.10447 1044 VAL A CG1 
987  C CG2 . VAL A 125 ? 0.56081 0.55395 0.50311 0.04399  0.01375  -0.11699 1044 VAL A CG2 
988  N N   . GLY A 126 ? 0.47904 0.47183 0.37903 0.01503  -0.01740 -0.08289 1045 GLY A N   
989  C CA  . GLY A 126 ? 0.50919 0.50040 0.40429 0.00963  -0.03104 -0.07799 1045 GLY A CA  
990  C C   . GLY A 126 ? 0.54102 0.52047 0.45451 0.01002  -0.03797 -0.08463 1045 GLY A C   
991  O O   . GLY A 126 ? 0.50426 0.47408 0.43621 0.01460  -0.03314 -0.08643 1045 GLY A O   
992  N N   . ALA A 127 ? 0.54897 0.53060 0.45718 0.00378  -0.05040 -0.08676 1046 ALA A N   
993  C CA  . ALA A 127 ? 0.55291 0.52527 0.47791 0.00052  -0.05746 -0.09382 1046 ALA A CA  
994  C C   . ALA A 127 ? 0.54528 0.51585 0.49803 0.00253  -0.05725 -0.08126 1046 ALA A C   
995  O O   . ALA A 127 ? 0.60375 0.56458 0.57248 0.00026  -0.05792 -0.08545 1046 ALA A O   
996  C CB  . ALA A 127 ? 0.61174 0.59201 0.52666 -0.00850 -0.07241 -0.09808 1046 ALA A CB  
997  N N   . GLY A 128 ? 0.47935 0.45771 0.43713 0.00619  -0.05564 -0.06638 1047 GLY A N   
998  C CA  . GLY A 128 ? 0.47095 0.44846 0.45255 0.00876  -0.05353 -0.05724 1047 GLY A CA  
999  C C   . GLY A 128 ? 0.43759 0.40440 0.42578 0.01315  -0.04250 -0.05821 1047 GLY A C   
1000 O O   . GLY A 128 ? 0.45145 0.41533 0.45608 0.01314  -0.04034 -0.05458 1047 GLY A O   
1001 N N   . ALA A 129 ? 0.42917 0.39282 0.40507 0.01662  -0.03553 -0.06258 1048 ALA A N   
1002 C CA  . ALA A 129 ? 0.42650 0.38338 0.41019 0.02140  -0.02737 -0.06216 1048 ALA A CA  
1003 C C   . ALA A 129 ? 0.42786 0.37188 0.42144 0.02114  -0.02802 -0.06784 1048 ALA A C   
1004 O O   . ALA A 129 ? 0.39792 0.33758 0.40248 0.02189  -0.02569 -0.06120 1048 ALA A O   
1005 C CB  . ALA A 129 ? 0.43857 0.39995 0.41163 0.02515  -0.02027 -0.06619 1048 ALA A CB  
1006 N N   . PRO A 130 ? 0.44258 0.37811 0.43149 0.01936  -0.03124 -0.07968 1049 PRO A N   
1007 C CA  . PRO A 130 ? 0.39668 0.31450 0.39636 0.01824  -0.03252 -0.08287 1049 PRO A CA  
1008 C C   . PRO A 130 ? 0.45009 0.36786 0.46277 0.00964  -0.03711 -0.07519 1049 PRO A C   
1009 O O   . PRO A 130 ? 0.40302 0.30853 0.42554 0.00765  -0.03597 -0.07076 1049 PRO A O   
1010 C CB  . PRO A 130 ? 0.43468 0.34149 0.42495 0.01774  -0.03525 -0.09986 1049 PRO A CB  
1011 C CG  . PRO A 130 ? 0.44083 0.36367 0.41518 0.01362  -0.03890 -0.10362 1049 PRO A CG  
1012 C CD  . PRO A 130 ? 0.46094 0.40022 0.43272 0.01753  -0.03387 -0.09116 1049 PRO A CD  
1013 N N   . VAL A 131 ? 0.39266 0.32523 0.40668 0.00423  -0.04251 -0.07271 1050 VAL A N   
1014 C CA  . VAL A 131 ? 0.37715 0.31646 0.40858 -0.00327 -0.04536 -0.06550 1050 VAL A CA  
1015 C C   . VAL A 131 ? 0.40738 0.35106 0.44723 0.00056  -0.03719 -0.05406 1050 VAL A C   
1016 O O   . VAL A 131 ? 0.38589 0.32578 0.43633 -0.00431 -0.03417 -0.04888 1050 VAL A O   
1017 C CB  . VAL A 131 ? 0.39084 0.34945 0.42538 -0.00723 -0.05399 -0.06467 1050 VAL A CB  
1018 C CG1 . VAL A 131 ? 0.41336 0.38509 0.47161 -0.01355 -0.05521 -0.05734 1050 VAL A CG1 
1019 C CG2 . VAL A 131 ? 0.43707 0.39170 0.45917 -0.01341 -0.06356 -0.07770 1050 VAL A CG2 
1020 N N   . TYR A 132 ? 0.37103 0.32237 0.40463 0.00795  -0.03348 -0.05011 1051 TYR A N   
1021 C CA  . TYR A 132 ? 0.35882 0.31289 0.39690 0.01141  -0.02598 -0.04231 1051 TYR A CA  
1022 C C   . TYR A 132 ? 0.36066 0.30127 0.39509 0.01224  -0.02159 -0.04102 1051 TYR A C   
1023 O O   . TYR A 132 ? 0.37148 0.31160 0.41096 0.00936  -0.01739 -0.03482 1051 TYR A O   
1024 C CB  . TYR A 132 ? 0.33008 0.28922 0.36027 0.01781  -0.02415 -0.04019 1051 TYR A CB  
1025 C CG  . TYR A 132 ? 0.33004 0.29296 0.36526 0.02084  -0.01812 -0.03476 1051 TYR A CG  
1026 C CD1 . TYR A 132 ? 0.37683 0.33406 0.40822 0.02139  -0.01209 -0.03334 1051 TYR A CD1 
1027 C CD2 . TYR A 132 ? 0.34105 0.31259 0.38434 0.02372  -0.01926 -0.03175 1051 TYR A CD2 
1028 C CE1 . TYR A 132 ? 0.37283 0.33264 0.40507 0.02342  -0.00650 -0.03136 1051 TYR A CE1 
1029 C CE2 . TYR A 132 ? 0.35193 0.32413 0.39961 0.02762  -0.01289 -0.02994 1051 TYR A CE2 
1030 C CZ  . TYR A 132 ? 0.34697 0.31318 0.38757 0.02669  -0.00604 -0.03091 1051 TYR A CZ  
1031 O OH  . TYR A 132 ? 0.36310 0.32906 0.40447 0.02970  0.00049  -0.03195 1051 TYR A OH  
1032 N N   . LEU A 133 ? 0.35491 0.28594 0.38071 0.01651  -0.02256 -0.04643 1052 LEU A N   
1033 C CA  . LEU A 133 ? 0.35450 0.27388 0.37935 0.01972  -0.02044 -0.04362 1052 LEU A CA  
1034 C C   . LEU A 133 ? 0.42270 0.32737 0.45393 0.01354  -0.02273 -0.04085 1052 LEU A C   
1035 O O   . LEU A 133 ? 0.37731 0.27634 0.40898 0.01216  -0.02069 -0.03167 1052 LEU A O   
1036 C CB  . LEU A 133 ? 0.38396 0.29992 0.40345 0.02758  -0.02053 -0.05097 1052 LEU A CB  
1037 C CG  . LEU A 133 ? 0.39320 0.29968 0.41540 0.03402  -0.02042 -0.04811 1052 LEU A CG  
1038 C CD1 . LEU A 133 ? 0.40875 0.32234 0.42957 0.03327  -0.01849 -0.03730 1052 LEU A CD1 
1039 C CD2 . LEU A 133 ? 0.42719 0.33817 0.44897 0.04317  -0.01881 -0.05675 1052 LEU A CD2 
1040 N N   . ALA A 134 ? 0.40058 0.29832 0.43540 0.00807  -0.02753 -0.04799 1053 ALA A N   
1041 C CA  . ALA A 134 ? 0.40756 0.28908 0.44993 -0.00074 -0.02995 -0.04441 1053 ALA A CA  
1042 C C   . ALA A 134 ? 0.40318 0.29647 0.45309 -0.00932 -0.02552 -0.03248 1053 ALA A C   
1043 O O   . ALA A 134 ? 0.43271 0.31458 0.48403 -0.01476 -0.02373 -0.02280 1053 ALA A O   
1044 C CB  . ALA A 134 ? 0.42972 0.30334 0.47520 -0.00800 -0.03682 -0.05587 1053 ALA A CB  
1045 N N   . ALA A 135 ? 0.38792 0.30439 0.44266 -0.01005 -0.02315 -0.03247 1054 ALA A N   
1046 C CA  . ALA A 135 ? 0.37844 0.31004 0.44277 -0.01664 -0.01669 -0.02376 1054 ALA A CA  
1047 C C   . ALA A 135 ? 0.38565 0.31548 0.43953 -0.01294 -0.00928 -0.01546 1054 ALA A C   
1048 O O   . ALA A 135 ? 0.39583 0.32780 0.45121 -0.02067 -0.00352 -0.00653 1054 ALA A O   
1049 C CB  . ALA A 135 ? 0.35335 0.30954 0.42770 -0.01428 -0.01610 -0.02663 1054 ALA A CB  
1050 N N   . VAL A 136 ? 0.36305 0.29082 0.40534 -0.00262 -0.00946 -0.01813 1055 VAL A N   
1051 C CA  . VAL A 136 ? 0.36246 0.28967 0.39319 0.00009  -0.00485 -0.01156 1055 VAL A CA  
1052 C C   . VAL A 136 ? 0.38812 0.29682 0.41307 -0.00256 -0.00792 -0.00291 1055 VAL A C   
1053 O O   . VAL A 136 ? 0.40221 0.31122 0.41944 -0.00758 -0.00393 0.00728  1055 VAL A O   
1054 C CB  . VAL A 136 ? 0.37867 0.30946 0.40141 0.00966  -0.00581 -0.01684 1055 VAL A CB  
1055 C CG1 . VAL A 136 ? 0.36970 0.29943 0.37974 0.01126  -0.00416 -0.01103 1055 VAL A CG1 
1056 C CG2 . VAL A 136 ? 0.38835 0.33364 0.41554 0.01166  -0.00236 -0.02177 1055 VAL A CG2 
1057 N N   . LEU A 137 ? 0.39988 0.29146 0.42749 0.00121  -0.01502 -0.00670 1056 LEU A N   
1058 C CA  . LEU A 137 ? 0.43300 0.30249 0.45802 0.00081  -0.01949 0.00222  1056 LEU A CA  
1059 C C   . LEU A 137 ? 0.44623 0.30786 0.47479 -0.01338 -0.01745 0.01251  1056 LEU A C   
1060 O O   . LEU A 137 ? 0.42941 0.28068 0.45011 -0.01734 -0.01755 0.02681  1056 LEU A O   
1061 C CB  . LEU A 137 ? 0.44683 0.29816 0.47739 0.00869  -0.02627 -0.00719 1056 LEU A CB  
1062 C CG  . LEU A 137 ? 0.43252 0.29396 0.46116 0.02188  -0.02681 -0.01658 1056 LEU A CG  
1063 C CD1 . LEU A 137 ? 0.43092 0.27736 0.46535 0.02938  -0.03068 -0.02887 1056 LEU A CD1 
1064 C CD2 . LEU A 137 ? 0.43636 0.30327 0.45930 0.02864  -0.02794 -0.00751 1056 LEU A CD2 
1065 N N   . GLU A 138 ? 0.45472 0.32302 0.49522 -0.02232 -0.01612 0.00667  1057 GLU A N   
1066 C CA  . GLU A 138 ? 0.49202 0.35794 0.53976 -0.03852 -0.01310 0.01649  1057 GLU A CA  
1067 C C   . GLU A 138 ? 0.46690 0.35388 0.50837 -0.04409 -0.00232 0.02716  1057 GLU A C   
1068 O O   . GLU A 138 ? 0.45726 0.33715 0.49350 -0.05489 0.00113  0.04182  1057 GLU A O   
1069 C CB  . GLU A 138 ? 0.45765 0.33322 0.52268 -0.04706 -0.01512 0.00661  1057 GLU A CB  
1070 C CG  . GLU A 138 ? 0.49042 0.37175 0.56842 -0.06609 -0.01099 0.01598  1057 GLU A CG  
1071 C CD  . GLU A 138 ? 0.55548 0.44106 0.65206 -0.07604 -0.01753 0.00583  1057 GLU A CD  
1072 O OE1 . GLU A 138 ? 0.61030 0.48268 0.70447 -0.06949 -0.02671 -0.00756 1057 GLU A OE1 
1073 O OE2 . GLU A 138 ? 0.57779 0.48263 0.69132 -0.09092 -0.01336 0.01066  1057 GLU A OE2 
1074 N N   . TYR A 139 ? 0.44398 0.35554 0.48437 -0.03706 0.00356  0.01991  1058 TYR A N   
1075 C CA  . TYR A 139 ? 0.43904 0.37079 0.47264 -0.04097 0.01528  0.02586  1058 TYR A CA  
1076 C C   . TYR A 139 ? 0.45502 0.37554 0.46514 -0.04048 0.01556  0.03768  1058 TYR A C   
1077 O O   . TYR A 139 ? 0.43191 0.35783 0.43272 -0.05101 0.02343  0.04951  1058 TYR A O   
1078 C CB  . TYR A 139 ? 0.42042 0.37399 0.45722 -0.03103 0.02008  0.01385  1058 TYR A CB  
1079 C CG  . TYR A 139 ? 0.45089 0.41812 0.47326 -0.03086 0.03115  0.01624  1058 TYR A CG  
1080 C CD1 . TYR A 139 ? 0.47950 0.46440 0.50547 -0.04117 0.04360  0.02167  1058 TYR A CD1 
1081 C CD2 . TYR A 139 ? 0.42433 0.38809 0.42891 -0.02166 0.02964  0.01213  1058 TYR A CD2 
1082 C CE1 . TYR A 139 ? 0.48304 0.48078 0.49186 -0.04130 0.05522  0.02173  1058 TYR A CE1 
1083 C CE2 . TYR A 139 ? 0.40895 0.38366 0.39683 -0.02264 0.03916  0.01187  1058 TYR A CE2 
1084 C CZ  . TYR A 139 ? 0.42534 0.41636 0.41370 -0.03187 0.05229  0.01603  1058 TYR A CZ  
1085 O OH  . TYR A 139 ? 0.46993 0.47245 0.43809 -0.03309 0.06322  0.01368  1058 TYR A OH  
1086 N N   . LEU A 140 ? 0.42755 0.33506 0.42791 -0.02897 0.00684  0.03540  1059 LEU A N   
1087 C CA  . LEU A 140 ? 0.43615 0.33520 0.41573 -0.02764 0.00374  0.04728  1059 LEU A CA  
1088 C C   . LEU A 140 ? 0.48238 0.35894 0.45922 -0.03668 -0.00061 0.06455  1059 LEU A C   
1089 O O   . LEU A 140 ? 0.48858 0.36369 0.44688 -0.04350 0.00125  0.08008  1059 LEU A O   
1090 C CB  . LEU A 140 ? 0.42072 0.31400 0.39757 -0.01340 -0.00594 0.04102  1059 LEU A CB  
1091 C CG  . LEU A 140 ? 0.45104 0.36326 0.42649 -0.00645 -0.00234 0.02720  1059 LEU A CG  
1092 C CD1 . LEU A 140 ? 0.47341 0.38146 0.45146 0.00515  -0.01150 0.02166  1059 LEU A CD1 
1093 C CD2 . LEU A 140 ? 0.43427 0.36061 0.39022 -0.01077 0.00471  0.02969  1059 LEU A CD2 
1094 N N   . THR A 141 ? 0.50085 0.35775 0.49422 -0.03756 -0.00689 0.06221  1060 THR A N   
1095 C CA  . THR A 141 ? 0.48978 0.31978 0.48303 -0.04745 -0.01138 0.07835  1060 THR A CA  
1096 C C   . THR A 141 ? 0.54401 0.38609 0.53413 -0.06675 -0.00006 0.09063  1060 THR A C   
1097 O O   . THR A 141 ? 0.57694 0.40656 0.55252 -0.07618 -0.00003 0.11086  1060 THR A O   
1098 C CB  . THR A 141 ? 0.52411 0.33070 0.53655 -0.04615 -0.01911 0.06869  1060 THR A CB  
1099 O OG1 . THR A 141 ? 0.54220 0.33870 0.55608 -0.02779 -0.02772 0.05843  1060 THR A OG1 
1100 C CG2 . THR A 141 ? 0.58459 0.35883 0.59935 -0.05868 -0.02362 0.08451  1060 THR A CG2 
1101 N N   . ALA A 142 ? 0.46996 0.33862 0.47414 -0.07269 0.00983  0.07964  1061 ALA A N   
1102 C CA  . ALA A 142 ? 0.55077 0.43802 0.55705 -0.09074 0.02287  0.08952  1061 ALA A CA  
1103 C C   . ALA A 142 ? 0.53360 0.43639 0.51317 -0.09244 0.03258  0.09976  1061 ALA A C   
1104 O O   . ALA A 142 ? 0.58439 0.48716 0.55251 -0.10806 0.03960  0.11773  1061 ALA A O   
1105 C CB  . ALA A 142 ? 0.49042 0.40803 0.52145 -0.09296 0.03048  0.07420  1061 ALA A CB  
1106 N N   . GLU A 143 ? 0.54906 0.46387 0.51609 -0.07787 0.03266  0.08884  1062 GLU A N   
1107 C CA  . GLU A 143 ? 0.58029 0.50910 0.51845 -0.07979 0.04069  0.09541  1062 GLU A CA  
1108 C C   . GLU A 143 ? 0.60760 0.51247 0.52117 -0.08437 0.03138  0.11783  1062 GLU A C   
1109 O O   . GLU A 143 ? 0.56432 0.47538 0.45628 -0.09772 0.03952  0.13390  1062 GLU A O   
1110 C CB  . GLU A 143 ? 0.50132 0.44226 0.43190 -0.06416 0.03962  0.07806  1062 GLU A CB  
1111 C CG  . GLU A 143 ? 0.49609 0.46301 0.44373 -0.05986 0.05133  0.05898  1062 GLU A CG  
1112 C CD  . GLU A 143 ? 0.54257 0.53559 0.47671 -0.06694 0.06959  0.05766  1062 GLU A CD  
1113 O OE1 . GLU A 143 ? 0.54109 0.53319 0.44869 -0.07710 0.07351  0.07217  1062 GLU A OE1 
1114 O OE2 . GLU A 143 ? 0.52554 0.54008 0.47504 -0.06170 0.08010  0.04211  1062 GLU A OE2 
1115 N N   . ILE A 144 ? 0.57454 0.45296 0.49128 -0.07299 0.01436  0.11989  1063 ILE A N   
1116 C CA  . ILE A 144 ? 0.57687 0.43184 0.47346 -0.07390 0.00270  0.14214  1063 ILE A CA  
1117 C C   . ILE A 144 ? 0.60567 0.44042 0.50300 -0.09151 0.00435  0.16378  1063 ILE A C   
1118 O O   . ILE A 144 ? 0.67292 0.50307 0.54449 -0.10228 0.00503  0.18647  1063 ILE A O   
1119 C CB  . ILE A 144 ? 0.53572 0.36963 0.44263 -0.05544 -0.01509 0.13773  1063 ILE A CB  
1120 C CG1 . ILE A 144 ? 0.56085 0.41735 0.46303 -0.04203 -0.01618 0.12037  1063 ILE A CG1 
1121 C CG2 . ILE A 144 ? 0.59497 0.40204 0.48750 -0.05464 -0.02918 0.16268  1063 ILE A CG2 
1122 C CD1 . ILE A 144 ? 0.64253 0.48905 0.56342 -0.02466 -0.02827 0.10923  1063 ILE A CD1 
1123 N N   . LEU A 145 ? 0.60287 0.42531 0.52809 -0.09649 0.00471  0.15767  1064 LEU A N   
1124 C CA  . LEU A 145 ? 0.64247 0.44212 0.57101 -0.11547 0.00525  0.17797  1064 LEU A CA  
1125 C C   . LEU A 145 ? 0.67764 0.50532 0.59438 -0.13658 0.02390  0.18900  1064 LEU A C   
1126 O O   . LEU A 145 ? 0.72964 0.54246 0.63223 -0.15363 0.02535  0.21448  1064 LEU A O   
1127 C CB  . LEU A 145 ? 0.66286 0.44458 0.62401 -0.11788 0.00088  0.16569  1064 LEU A CB  
1128 C CG  . LEU A 145 ? 0.70519 0.45229 0.67699 -0.09963 -0.01649 0.15734  1064 LEU A CG  
1129 C CD1 . LEU A 145 ? 0.67040 0.40097 0.67014 -0.10462 -0.01968 0.14249  1064 LEU A CD1 
1130 C CD2 . LEU A 145 ? 0.72166 0.43165 0.67870 -0.09679 -0.02911 0.18135  1064 LEU A CD2 
1131 N N   . GLU A 146 ? 0.68543 0.55353 0.60828 -0.13565 0.03886  0.17079  1065 GLU A N   
1132 C CA  . GLU A 146 ? 0.73435 0.63452 0.64619 -0.15315 0.05915  0.17864  1065 GLU A CA  
1133 C C   . GLU A 146 ? 0.75391 0.65379 0.62253 -0.15720 0.06082  0.19796  1065 GLU A C   
1134 O O   . GLU A 146 ? 0.79465 0.69425 0.64668 -0.17732 0.06906  0.22111  1065 GLU A O   
1135 C CB  . GLU A 146 ? 0.68175 0.62388 0.60733 -0.14553 0.07365  0.15341  1065 GLU A CB  
1136 C CG  . GLU A 146 ? 0.75915 0.73844 0.67276 -0.16008 0.09694  0.15804  1065 GLU A CG  
1137 C CD  . GLU A 146 ? 0.81976 0.83832 0.74944 -0.14953 0.11122  0.13226  1065 GLU A CD  
1138 O OE1 . GLU A 146 ? 0.78728 0.82358 0.75445 -0.15108 0.11596  0.12145  1065 GLU A OE1 
1139 O OE2 . GLU A 146 ? 0.74651 0.77703 0.65131 -0.13939 0.11645  0.12274  1065 GLU A OE2 
1140 N N   . LEU A 147 ? 0.74584 0.64743 0.59467 -0.13974 0.05278  0.18920  1066 LEU A N   
1141 C CA  . LEU A 147 ? 0.70742 0.61351 0.51247 -0.14328 0.05283  0.20463  1066 LEU A CA  
1142 C C   . LEU A 147 ? 0.79334 0.66208 0.58171 -0.14935 0.03644  0.23619  1066 LEU A C   
1143 O O   . LEU A 147 ? 0.79334 0.66377 0.54840 -0.16462 0.04106  0.26000  1066 LEU A O   
1144 C CB  . LEU A 147 ? 0.71058 0.62768 0.50301 -0.12412 0.04594  0.18548  1066 LEU A CB  
1145 C CG  . LEU A 147 ? 0.67538 0.62612 0.48075 -0.11852 0.06268  0.15626  1066 LEU A CG  
1146 C CD1 . LEU A 147 ? 0.71177 0.66530 0.51172 -0.10007 0.05295  0.13689  1066 LEU A CD1 
1147 C CD2 . LEU A 147 ? 0.80266 0.78450 0.58468 -0.13316 0.08557  0.15787  1066 LEU A CD2 
1148 N N   . ALA A 148 ? 0.77604 0.61037 0.58666 -0.13715 0.01748  0.23701  1067 ALA A N   
1149 C CA  . ALA A 148 ? 0.83113 0.62510 0.63175 -0.13997 0.00059  0.26641  1067 ALA A CA  
1150 C C   . ALA A 148 ? 0.87129 0.65459 0.67700 -0.16103 0.01074  0.28316  1067 ALA A C   
1151 O O   . ALA A 148 ? 0.91471 0.68520 0.70074 -0.16537 0.00788  0.30363  1067 ALA A O   
1152 C CB  . ALA A 148 ? 0.77538 0.53720 0.60531 -0.11978 -0.01862 0.25708  1067 ALA A CB  
1153 N N   . GLY A 149 ? 0.85766 0.64911 0.69227 -0.17301 0.02271  0.27215  1068 GLY A N   
1154 C CA  . GLY A 149 ? 0.89267 0.68126 0.73669 -0.19280 0.03410  0.28323  1068 GLY A CA  
1155 C C   . GLY A 149 ? 0.91732 0.74028 0.73334 -0.20720 0.05371  0.29336  1068 GLY A C   
1156 O O   . GLY A 149 ? 0.98087 0.79402 0.78867 -0.22044 0.05845  0.31195  1068 GLY A O   
1157 N N   . ASN A 150 ? 0.89886 0.76210 0.69966 -0.20462 0.06633  0.27984  1069 ASN A N   
1158 C CA  . ASN A 150 ? 0.97362 0.86922 0.74345 -0.21426 0.08471  0.28560  1069 ASN A CA  
1159 C C   . ASN A 150 ? 1.02844 0.90381 0.75927 -0.20996 0.07197  0.30656  1069 ASN A C   
1160 O O   . ASN A 150 ? 1.09124 0.97203 0.80108 -0.22261 0.08160  0.32290  1069 ASN A O   
1161 C CB  . ASN A 150 ? 0.93442 0.87334 0.69486 -0.20837 0.09959  0.26213  1069 ASN A CB  
1162 C CG  . ASN A 150 ? 0.90321 0.86968 0.70318 -0.21291 0.11484  0.24204  1069 ASN A CG  
1163 O OD1 . ASN A 150 ? 0.94657 0.90663 0.77944 -0.22402 0.11686  0.24624  1069 ASN A OD1 
1164 N ND2 . ASN A 150 ? 0.85121 0.84901 0.65187 -0.20092 0.12464  0.21624  1069 ASN A ND2 
1165 N N   . ALA A 151 ? 0.99010 0.84424 0.71197 -0.19198 0.05001  0.30651  1070 ALA A N   
1166 C CA  . ALA A 151 ? 1.01385 0.85062 0.70334 -0.18587 0.03478  0.32615  1070 ALA A CA  
1167 C C   . ALA A 151 ? 1.08693 0.88642 0.78344 -0.19303 0.02727  0.35076  1070 ALA A C   
1168 O O   . ALA A 151 ? 1.07753 0.87225 0.74444 -0.19899 0.02607  0.37165  1070 ALA A O   
1169 C CB  . ALA A 151 ? 1.03413 0.85866 0.72242 -0.16386 0.01194  0.31933  1070 ALA A CB  
1170 N N   . ALA A 152 ? 1.00225 0.77323 0.73647 -0.19237 0.02150  0.34792  1071 ALA A N   
1171 C CA  . ALA A 152 ? 1.07888 0.81250 0.82161 -0.20062 0.01630  0.36831  1071 ALA A CA  
1172 C C   . ALA A 152 ? 1.16032 0.91158 0.89382 -0.22573 0.03801  0.38033  1071 ALA A C   
1173 O O   . ALA A 152 ? 1.17404 0.90723 0.88819 -0.23438 0.03641  0.40478  1071 ALA A O   
1174 C CB  . ALA A 152 ? 1.07174 0.77364 0.85680 -0.19540 0.00754  0.35678  1071 ALA A CB  
1175 N N   . ARG A 153 ? 1.14214 0.92990 0.89113 -0.23732 0.05873  0.36371  1072 ARG A N   
1176 C CA  . ARG A 153 ? 1.18880 0.99975 0.93467 -0.26038 0.08143  0.37258  1072 ARG A CA  
1177 C C   . ARG A 153 ? 1.23869 1.07084 0.93789 -0.26463 0.09016  0.38647  1072 ARG A C   
1178 O O   . ARG A 153 ? 1.31901 1.14638 1.00348 -0.28081 0.09833  0.40783  1072 ARG A O   
1179 C CB  . ARG A 153 ? 1.19184 1.04459 0.96674 -0.26756 0.10139  0.34897  1072 ARG A CB  
1180 C CG  . ARG A 153 ? 1.21183 1.09347 0.99248 -0.29024 0.12591  0.35541  1072 ARG A CG  
1181 C CD  . ARG A 153 ? 1.16786 1.10111 0.97252 -0.29157 0.14627  0.33007  1072 ARG A CD  
1182 N NE  . ARG A 153 ? 1.22402 1.18461 1.00188 -0.27631 0.15039  0.31523  1072 ARG A NE  
1183 C CZ  . ARG A 153 ? 1.15142 1.14119 0.94745 -0.26594 0.15663  0.28916  1072 ARG A CZ  
1184 N NH1 . ARG A 153 ? 1.08254 1.08179 0.92426 -0.26873 0.15908  0.27540  1072 ARG A NH1 
1185 N NH2 . ARG A 153 ? 1.12026 1.12956 0.88785 -0.25253 0.15958  0.27603  1072 ARG A NH2 
1186 N N   . ASP A 154 ? 1.23832 1.09341 0.91258 -0.25097 0.08836  0.37408  1073 ASP A N   
1187 C CA  . ASP A 154 ? 1.31987 1.19399 0.94674 -0.25375 0.09435  0.38423  1073 ASP A CA  
1188 C C   . ASP A 154 ? 1.34527 1.18139 0.94730 -0.25205 0.07460  0.41365  1073 ASP A C   
1189 O O   . ASP A 154 ? 1.35313 1.19736 0.91846 -0.26173 0.08087  0.43095  1073 ASP A O   
1190 C CB  . ASP A 154 ? 1.31496 1.21605 0.92194 -0.23834 0.09274  0.36223  1073 ASP A CB  
1191 C CG  . ASP A 154 ? 1.35159 1.29953 0.96665 -0.24257 0.11908  0.33634  1073 ASP A CG  
1192 O OD1 . ASP A 154 ? 1.31613 1.27147 0.97106 -0.24167 0.12509  0.31985  1073 ASP A OD1 
1193 O OD2 . ASP A 154 ? 1.40538 1.38313 0.98798 -0.24584 0.13376  0.33126  1073 ASP A OD2 
1194 N N   . ASN A 155 ? 1.31724 1.11229 0.93926 -0.23893 0.05102  0.41910  1074 ASN A N   
1195 C CA  . ASN A 155 ? 1.33210 1.08752 0.93900 -0.23377 0.03047  0.44588  1074 ASN A CA  
1196 C C   . ASN A 155 ? 1.32790 1.05014 0.95071 -0.24962 0.03346  0.46658  1074 ASN A C   
1197 O O   . ASN A 155 ? 1.30718 0.98988 0.92402 -0.24476 0.01617  0.48867  1074 ASN A O   
1198 C CB  . ASN A 155 ? 1.29644 1.02633 0.92052 -0.20863 0.00446  0.43832  1074 ASN A CB  
1199 C CG  . ASN A 155 ? 1.32757 1.02709 0.93216 -0.19780 -0.01800 0.46278  1074 ASN A CG  
1200 O OD1 . ASN A 155 ? 1.31345 1.01419 0.88388 -0.20843 -0.01558 0.48538  1074 ASN A OD1 
1201 N ND2 . ASN A 155 ? 1.27997 0.95375 0.90676 -0.17578 -0.03982 0.45820  1074 ASN A ND2 
1202 N N   . LYS A 156 ? 1.35258 1.09030 0.99759 -0.26813 0.05460  0.45931  1075 LYS A N   
1203 C CA  . LYS A 156 ? 1.37045 1.07904 1.03397 -0.28597 0.05882  0.47625  1075 LYS A CA  
1204 C C   . LYS A 156 ? 1.37209 1.02714 1.06421 -0.27354 0.03649  0.47791  1075 LYS A C   
1205 O O   . LYS A 156 ? 1.40235 1.01710 1.09272 -0.27945 0.02855  0.50063  1075 LYS A O   
1206 C CB  . LYS A 156 ? 1.46275 1.16751 1.08973 -0.30255 0.06558  0.50735  1075 LYS A CB  
1207 C CG  . LYS A 156 ? 1.49756 1.25570 1.09842 -0.31619 0.09106  0.50348  1075 LYS A CG  
1208 C CD  . LYS A 156 ? 1.67091 1.45231 1.30774 -0.33506 0.11445  0.49132  1075 LYS A CD  
1209 C CE  . LYS A 156 ? 1.70625 1.53915 1.32518 -0.35140 0.14369  0.48945  1075 LYS A CE  
1210 N NZ  . LYS A 156 ? 1.71227 1.53494 1.30983 -0.37384 0.15333  0.52076  1075 LYS A NZ  
1211 N N   . LYS A 157 ? 1.29212 0.94646 1.01032 -0.25580 0.02708  0.45287  1076 LYS A N   
1212 C CA  . LYS A 157 ? 1.24355 0.85288 0.99345 -0.24253 0.00915  0.44630  1076 LYS A CA  
1213 C C   . LYS A 157 ? 1.22118 0.83905 1.01098 -0.24952 0.01828  0.42119  1076 LYS A C   
1214 O O   . LYS A 157 ? 1.25249 0.91309 1.04802 -0.25241 0.03147  0.40257  1076 LYS A O   
1215 C CB  . LYS A 157 ? 1.21485 0.81457 0.96232 -0.21333 -0.01183 0.43768  1076 LYS A CB  
1216 C CG  . LYS A 157 ? 1.32736 0.90808 1.04493 -0.20257 -0.02764 0.46234  1076 LYS A CG  
1217 C CD  . LYS A 157 ? 1.29638 0.82193 1.02646 -0.20262 -0.03891 0.48069  1076 LYS A CD  
1218 C CE  . LYS A 157 ? 1.43456 0.93043 1.20780 -0.19074 -0.04651 0.45822  1076 LYS A CE  
1219 N NZ  . LYS A 157 ? 1.25483 0.76396 1.04048 -0.16479 -0.05771 0.43479  1076 LYS A NZ  
1220 N N   . THR A 158 ? 1.21587 0.79211 1.03327 -0.25115 0.01023  0.41963  1077 THR A N   
1221 C CA  . THR A 158 ? 1.19038 0.76939 1.04606 -0.25753 0.01523  0.39537  1077 THR A CA  
1222 C C   . THR A 158 ? 1.15152 0.71184 1.02815 -0.23314 -0.00112 0.37179  1077 THR A C   
1223 O O   . THR A 158 ? 1.16276 0.72240 1.06973 -0.23631 0.00031  0.34991  1077 THR A O   
1224 C CB  . THR A 158 ? 1.17443 0.72167 1.04731 -0.27839 0.01862  0.40537  1077 THR A CB  
1225 O OG1 . THR A 158 ? 1.19778 0.68778 1.07058 -0.26573 0.00021  0.41537  1077 THR A OG1 
1226 C CG2 . THR A 158 ? 1.25493 0.82287 1.10802 -0.30367 0.03644  0.42944  1077 THR A CG2 
1227 N N   . ARG A 159 ? 1.14927 0.69816 1.01082 -0.20905 -0.01628 0.37480  1078 ARG A N   
1228 C CA  . ARG A 159 ? 1.12213 0.65906 1.00301 -0.18450 -0.03007 0.35192  1078 ARG A CA  
1229 C C   . ARG A 159 ? 1.10465 0.66727 0.96507 -0.16560 -0.03644 0.35112  1078 ARG A C   
1230 O O   . ARG A 159 ? 1.09948 0.66954 0.92968 -0.16535 -0.03829 0.37199  1078 ARG A O   
1231 C CB  . ARG A 159 ? 1.13350 0.61584 1.02790 -0.17115 -0.04569 0.35424  1078 ARG A CB  
1232 C CG  . ARG A 159 ? 1.25528 0.72277 1.13393 -0.14717 -0.06175 0.36710  1078 ARG A CG  
1233 C CD  . ARG A 159 ? 1.46876 0.88221 1.35856 -0.13750 -0.07398 0.37484  1078 ARG A CD  
1234 N NE  . ARG A 159 ? 1.49987 0.89053 1.42115 -0.12595 -0.07816 0.34703  1078 ARG A NE  
1235 C CZ  . ARG A 159 ? 1.56856 0.91097 1.50408 -0.12178 -0.08465 0.34667  1078 ARG A CZ  
1236 N NH1 . ARG A 159 ? 1.50343 0.81260 1.42705 -0.12909 -0.08809 0.37398  1078 ARG A NH1 
1237 N NH2 . ARG A 159 ? 1.55373 0.88008 1.51452 -0.11048 -0.08727 0.31797  1078 ARG A NH2 
1238 N N   . ILE A 160 ? 0.98628 0.56336 0.86259 -0.15102 -0.03983 0.32651  1079 ILE A N   
1239 C CA  . ILE A 160 ? 0.97259 0.57302 0.83431 -0.13262 -0.04694 0.32204  1079 ILE A CA  
1240 C C   . ILE A 160 ? 0.95024 0.52111 0.81603 -0.10733 -0.06674 0.32574  1079 ILE A C   
1241 O O   . ILE A 160 ? 0.98535 0.52560 0.87726 -0.09585 -0.07410 0.31356  1079 ILE A O   
1242 C CB  . ILE A 160 ? 0.88937 0.51607 0.76784 -0.12808 -0.04215 0.29512  1079 ILE A CB  
1243 C CG1 . ILE A 160 ? 0.92765 0.59194 0.80126 -0.15098 -0.02176 0.29220  1079 ILE A CG1 
1244 C CG2 . ILE A 160 ? 0.89607 0.54035 0.76393 -0.10741 -0.05194 0.28876  1079 ILE A CG2 
1245 C CD1 . ILE A 160 ? 0.90858 0.58529 0.81161 -0.15225 -0.01677 0.26636  1079 ILE A CD1 
1246 N N   . ILE A 161 ? 0.98804 0.56987 0.82823 -0.09863 -0.07491 0.34161  1080 ILE A N   
1247 C CA  . ILE A 161 ? 1.01986 0.58202 0.86553 -0.07343 -0.09398 0.34587  1080 ILE A CA  
1248 C C   . ILE A 161 ? 0.97855 0.57498 0.81898 -0.05772 -0.10039 0.33401  1080 ILE A C   
1249 O O   . ILE A 161 ? 0.99311 0.62324 0.82035 -0.06845 -0.08973 0.32593  1080 ILE A O   
1250 C CB  . ILE A 161 ? 1.09109 0.63380 0.91378 -0.07653 -0.10125 0.37686  1080 ILE A CB  
1251 C CG1 . ILE A 161 ? 1.07701 0.65459 0.86015 -0.08575 -0.09854 0.39228  1080 ILE A CG1 
1252 C CG2 . ILE A 161 ? 1.18474 0.69800 1.00930 -0.09748 -0.09190 0.38954  1080 ILE A CG2 
1253 C CD1 . ILE A 161 ? 1.18456 0.74437 0.94293 -0.08565 -0.10895 0.42317  1080 ILE A CD1 
1254 N N   . PRO A 162 ? 1.03802 0.62864 0.89076 -0.03255 -0.11670 0.33095  1081 PRO A N   
1255 C CA  . PRO A 162 ? 0.96971 0.59472 0.82214 -0.01879 -0.12257 0.31720  1081 PRO A CA  
1256 C C   . PRO A 162 ? 1.02816 0.68880 0.84257 -0.03068 -0.11990 0.32743  1081 PRO A C   
1257 O O   . PRO A 162 ? 1.03302 0.72386 0.84328 -0.03138 -0.11557 0.31175  1081 PRO A O   
1258 C CB  . PRO A 162 ? 1.03095 0.64372 0.90184 0.00808  -0.14051 0.31882  1081 PRO A CB  
1259 C CG  . PRO A 162 ? 1.05281 0.62269 0.94714 0.01202  -0.13979 0.31753  1081 PRO A CG  
1260 C CD  . PRO A 162 ? 1.05873 0.61199 0.93383 -0.01454 -0.12857 0.33393  1081 PRO A CD  
1261 N N   . ARG A 163 ? 1.05831 0.71623 0.84289 -0.04022 -0.12199 0.35216  1082 ARG A N   
1262 C CA  . ARG A 163 ? 1.08265 0.77656 0.82864 -0.05021 -0.11926 0.35772  1082 ARG A CA  
1263 C C   . ARG A 163 ? 1.07389 0.79058 0.80447 -0.07234 -0.09687 0.34800  1082 ARG A C   
1264 O O   . ARG A 163 ? 1.12079 0.87149 0.82530 -0.07761 -0.09200 0.34117  1082 ARG A O   
1265 C CB  . ARG A 163 ? 1.20236 0.88948 0.91746 -0.05473 -0.12704 0.38586  1082 ARG A CB  
1266 C CG  . ARG A 163 ? 1.23783 0.90554 0.93812 -0.07590 -0.11401 0.40463  1082 ARG A CG  
1267 C CD  . ARG A 163 ? 1.31955 0.99034 0.98015 -0.08221 -0.12040 0.43131  1082 ARG A CD  
1268 N NE  . ARG A 163 ? 1.19160 0.84422 0.83795 -0.10333 -0.10736 0.45086  1082 ARG A NE  
1269 C CZ  . ARG A 163 ? 1.39357 1.00791 1.04353 -0.10210 -0.11599 0.47391  1082 ARG A CZ  
1270 N NH1 . ARG A 163 ? 1.51294 1.10331 1.18034 -0.07942 -0.13725 0.48017  1082 ARG A NH1 
1271 N NH2 . ARG A 163 ? 1.46620 1.06660 1.10319 -0.12398 -0.10241 0.49094  1082 ARG A NH2 
1272 N N   . HIS A 164 ? 1.07533 0.77574 0.82250 -0.08525 -0.08288 0.34555  1083 HIS A N   
1273 C CA  . HIS A 164 ? 1.06107 0.78720 0.80256 -0.10352 -0.06131 0.33293  1083 HIS A CA  
1274 C C   . HIS A 164 ? 1.00700 0.75226 0.76376 -0.09385 -0.06099 0.30745  1083 HIS A C   
1275 O O   . HIS A 164 ? 0.98900 0.76719 0.72737 -0.10225 -0.04854 0.29668  1083 HIS A O   
1276 C CB  . HIS A 164 ? 1.01633 0.72256 0.77866 -0.11898 -0.04857 0.33496  1083 HIS A CB  
1277 C CG  . HIS A 164 ? 1.08708 0.77487 0.83396 -0.13235 -0.04603 0.36035  1083 HIS A CG  
1278 N ND1 . HIS A 164 ? 1.09704 0.75094 0.86625 -0.13967 -0.04481 0.36685  1083 HIS A ND1 
1279 C CD2 . HIS A 164 ? 1.14892 0.84734 0.85892 -0.14110 -0.04387 0.38042  1083 HIS A CD2 
1280 C CE1 . HIS A 164 ? 1.18111 0.82421 0.92868 -0.15232 -0.04225 0.39161  1083 HIS A CE1 
1281 N NE2 . HIS A 164 ? 1.15239 0.82247 0.86347 -0.15322 -0.04155 0.40069  1083 HIS A NE2 
1282 N N   . LEU A 165 ? 0.94775 0.67251 0.73780 -0.07586 -0.07345 0.29633  1084 LEU A N   
1283 C CA  . LEU A 165 ? 0.90689 0.64693 0.71228 -0.06587 -0.07441 0.27334  1084 LEU A CA  
1284 C C   . LEU A 165 ? 0.95074 0.72204 0.73422 -0.05714 -0.08098 0.26772  1084 LEU A C   
1285 O O   . LEU A 165 ? 0.88941 0.69329 0.66859 -0.05852 -0.06829 0.24440  1084 LEU A O   
1286 C CB  . LEU A 165 ? 0.89341 0.60652 0.73792 -0.04596 -0.08639 0.26164  1084 LEU A CB  
1287 C CG  . LEU A 165 ? 0.90668 0.59252 0.77863 -0.05201 -0.07931 0.25436  1084 LEU A CG  
1288 C CD1 . LEU A 165 ? 0.90341 0.56573 0.80783 -0.02909 -0.09116 0.24027  1084 LEU A CD1 
1289 C CD2 . LEU A 165 ? 0.87713 0.58802 0.75756 -0.06320 -0.06074 0.23215  1084 LEU A CD2 
1290 N N   . GLN A 166 ? 0.97867 0.74437 0.75259 -0.04644 -0.09868 0.28318  1085 GLN A N   
1291 C CA  . GLN A 166 ? 1.03776 0.83208 0.79269 -0.03900 -0.10925 0.27928  1085 GLN A CA  
1292 C C   . GLN A 166 ? 0.98272 0.80596 0.69465 -0.05773 -0.09571 0.27909  1085 GLN A C   
1293 O O   . GLN A 166 ? 0.94538 0.79702 0.64546 -0.05702 -0.09355 0.26091  1085 GLN A O   
1294 C CB  . GLN A 166 ? 1.04295 0.82821 0.79979 -0.02442 -0.12914 0.29529  1085 GLN A CB  
1295 C CG  . GLN A 166 ? 1.16497 0.92698 0.96558 -0.00248 -0.14085 0.29052  1085 GLN A CG  
1296 C CD  . GLN A 166 ? 1.30888 1.04755 1.11296 0.00717  -0.15365 0.31142  1085 GLN A CD  
1297 O OE1 . GLN A 166 ? 1.24440 0.95711 1.08095 0.02215  -0.15863 0.30902  1085 GLN A OE1 
1298 N NE2 . GLN A 166 ? 1.29855 1.04553 1.06772 -0.00124 -0.15844 0.33116  1085 GLN A NE2 
1299 N N   . LEU A 167 ? 0.99976 0.81763 0.69068 -0.07343 -0.08438 0.29489  1086 LEU A N   
1300 C CA  . LEU A 167 ? 1.01308 0.85948 0.66449 -0.09042 -0.06804 0.29231  1086 LEU A CA  
1301 C C   . LEU A 167 ? 0.98067 0.84630 0.63608 -0.09964 -0.04688 0.26999  1086 LEU A C   
1302 O O   . LEU A 167 ? 0.95922 0.85397 0.59110 -0.10336 -0.03809 0.25313  1086 LEU A O   
1303 C CB  . LEU A 167 ? 1.01690 0.85199 0.65028 -0.10446 -0.05998 0.31512  1086 LEU A CB  
1304 C CG  . LEU A 167 ? 1.08578 0.94380 0.67335 -0.11813 -0.05004 0.32191  1086 LEU A CG  
1305 C CD1 . LEU A 167 ? 1.08442 0.92407 0.66446 -0.13138 -0.04267 0.34660  1086 LEU A CD1 
1306 C CD2 . LEU A 167 ? 1.11233 1.00402 0.68434 -0.12846 -0.02729 0.29856  1086 LEU A CD2 
1307 N N   . ALA A 168 ? 0.92561 0.77629 0.61569 -0.10085 -0.03784 0.26438  1087 ALA A N   
1308 C CA  . ALA A 168 ? 0.90309 0.77642 0.61164 -0.10337 -0.01574 0.23530  1087 ALA A CA  
1309 C C   . ALA A 168 ? 0.83183 0.72273 0.55395 -0.08660 -0.01892 0.20496  1087 ALA A C   
1310 O O   . ALA A 168 ? 0.78572 0.70259 0.50148 -0.08903 -0.00328 0.18332  1087 ALA A O   
1311 C CB  . ALA A 168 ? 0.93117 0.78532 0.67854 -0.10594 -0.00975 0.23377  1087 ALA A CB  
1312 N N   . VAL A 169 ? 0.78210 0.65889 0.52493 -0.06949 -0.03826 0.20277  1088 VAL A N   
1313 C CA  . VAL A 169 ? 0.79664 0.69035 0.55241 -0.05580 -0.04168 0.17660  1088 VAL A CA  
1314 C C   . VAL A 169 ? 0.81002 0.72577 0.52933 -0.05888 -0.04608 0.17421  1088 VAL A C   
1315 O O   . VAL A 169 ? 0.77903 0.71475 0.49575 -0.05771 -0.03774 0.14993  1088 VAL A O   
1316 C CB  . VAL A 169 ? 0.73800 0.61484 0.52655 -0.03761 -0.05953 0.17546  1088 VAL A CB  
1317 C CG1 . VAL A 169 ? 0.74669 0.64362 0.54429 -0.02609 -0.06496 0.15359  1088 VAL A CG1 
1318 C CG2 . VAL A 169 ? 0.70855 0.56676 0.53158 -0.03486 -0.05280 0.16874  1088 VAL A CG2 
1319 N N   . ARG A 170 ? 0.84623 0.75710 0.53594 -0.06332 -0.06034 0.19943  1089 ARG A N   
1320 C CA  . ARG A 170 ? 0.95217 0.88393 0.60515 -0.06668 -0.06880 0.19777  1089 ARG A CA  
1321 C C   . ARG A 170 ? 0.91781 0.87119 0.53794 -0.08122 -0.04681 0.18291  1089 ARG A C   
1322 O O   . ARG A 170 ? 0.92730 0.89966 0.53081 -0.08123 -0.04681 0.16284  1089 ARG A O   
1323 C CB  . ARG A 170 ? 1.03347 0.95522 0.65876 -0.06980 -0.08911 0.23178  1089 ARG A CB  
1324 C CG  . ARG A 170 ? 1.22400 1.16877 0.80600 -0.07771 -0.09078 0.22949  1089 ARG A CG  
1325 C CD  . ARG A 170 ? 1.35519 1.31667 0.93930 -0.06788 -0.11094 0.21730  1089 ARG A CD  
1326 N NE  . ARG A 170 ? 1.45974 1.40881 1.07965 -0.05064 -0.13372 0.23011  1089 ARG A NE  
1327 C CZ  . ARG A 170 ? 1.50960 1.45962 1.12763 -0.04273 -0.15356 0.24608  1089 ARG A CZ  
1328 N NH1 . ARG A 170 ? 1.42866 1.38958 1.00783 -0.05159 -0.15568 0.25324  1089 ARG A NH1 
1329 N NH2 . ARG A 170 ? 1.56181 1.50219 1.21839 -0.02469 -0.17113 0.25424  1089 ARG A NH2 
1330 N N   . ASN A 171 ? 0.84127 0.79261 0.45298 -0.09398 -0.02753 0.19142  1090 ASN A N   
1331 C CA  . ASN A 171 ? 0.83408 0.80849 0.41552 -0.10718 -0.00417 0.17829  1090 ASN A CA  
1332 C C   . ASN A 171 ? 0.83157 0.81750 0.44296 -0.10193 0.01608  0.14650  1090 ASN A C   
1333 O O   . ASN A 171 ? 0.84247 0.84817 0.43584 -0.11014 0.03768  0.13268  1090 ASN A O   
1334 C CB  . ASN A 171 ? 0.90268 0.87558 0.46305 -0.12392 0.00904  0.20236  1090 ASN A CB  
1335 C CG  . ASN A 171 ? 0.93582 0.90484 0.46686 -0.12533 -0.00502 0.22266  1090 ASN A CG  
1336 O OD1 . ASN A 171 ? 1.02106 0.99564 0.53574 -0.11839 -0.02228 0.21827  1090 ASN A OD1 
1337 N ND2 . ASN A 171 ? 1.04534 1.00700 0.56867 -0.13561 0.00306  0.24412  1090 ASN A ND2 
1338 N N   . ASP A 172 ? 0.71157 0.68630 0.36779 -0.08825 0.01027  0.13532  1091 ASP A N   
1339 C CA  . ASP A 172 ? 0.71504 0.69928 0.39992 -0.08184 0.02575  0.10727  1091 ASP A CA  
1340 C C   . ASP A 172 ? 0.75398 0.74040 0.44492 -0.07014 0.01406  0.08683  1091 ASP A C   
1341 O O   . ASP A 172 ? 0.64631 0.62082 0.36005 -0.05990 -0.00310 0.09001  1091 ASP A O   
1342 C CB  . ASP A 172 ? 0.72576 0.69699 0.45395 -0.07776 0.02857  0.11036  1091 ASP A CB  
1343 C CG  . ASP A 172 ? 0.69853 0.68192 0.45524 -0.07227 0.04442  0.08510  1091 ASP A CG  
1344 O OD1 . ASP A 172 ? 0.64992 0.63210 0.42319 -0.06028 0.03836  0.06697  1091 ASP A OD1 
1345 O OD2 . ASP A 172 ? 0.72871 0.72448 0.49182 -0.08035 0.06289  0.08439  1091 ASP A OD2 
1346 N N   . GLU A 173 ? 0.66619 0.66786 0.33750 -0.07225 0.02429  0.06511  1092 GLU A N   
1347 C CA  . GLU A 173 ? 0.66315 0.66608 0.33533 -0.06516 0.01285  0.04647  1092 GLU A CA  
1348 C C   . GLU A 173 ? 0.65409 0.64732 0.37160 -0.05236 0.00767  0.03699  1092 GLU A C   
1349 O O   . GLU A 173 ? 0.63765 0.62739 0.36526 -0.04627 -0.00961 0.03642  1092 GLU A O   
1350 C CB  . GLU A 173 ? 0.74601 0.76166 0.39502 -0.06921 0.02822  0.02088  1092 GLU A CB  
1351 C CG  . GLU A 173 ? 0.77124 0.78467 0.42537 -0.06371 0.01869  -0.00120 1092 GLU A CG  
1352 C CD  . GLU A 173 ? 0.93046 0.95230 0.55017 -0.07008 0.02887  -0.02460 1092 GLU A CD  
1353 O OE1 . GLU A 173 ? 1.09230 1.11108 0.70819 -0.06961 0.01891  -0.04127 1092 GLU A OE1 
1354 O OE2 . GLU A 173 ? 0.90479 0.93644 0.50253 -0.07586 0.04811  -0.02857 1092 GLU A OE2 
1355 N N   . GLU A 174 ? 0.60835 0.59990 0.35361 -0.04876 0.02225  0.03012  1093 GLU A N   
1356 C CA  . GLU A 174 ? 0.54817 0.53175 0.33157 -0.03770 0.01799  0.02076  1093 GLU A CA  
1357 C C   . GLU A 174 ? 0.54372 0.51451 0.34749 -0.03258 0.00341  0.03800  1093 GLU A C   
1358 O O   . GLU A 174 ? 0.53114 0.49808 0.35209 -0.02437 -0.00836 0.03367  1093 GLU A O   
1359 C CB  . GLU A 174 ? 0.54732 0.53508 0.35287 -0.03515 0.03586  0.00835  1093 GLU A CB  
1360 C CG  . GLU A 174 ? 0.53627 0.53330 0.32946 -0.03490 0.04884  -0.01410 1093 GLU A CG  
1361 C CD  . GLU A 174 ? 0.58672 0.59241 0.40134 -0.03158 0.06758  -0.02432 1093 GLU A CD  
1362 O OE1 . GLU A 174 ? 0.54037 0.55210 0.35004 -0.02872 0.07948  -0.04342 1093 GLU A OE1 
1363 O OE2 . GLU A 174 ? 0.53125 0.53829 0.36985 -0.03142 0.07029  -0.01424 1093 GLU A OE2 
1364 N N   . LEU A 175 ? 0.56553 0.52918 0.36760 -0.03767 0.00427  0.05729  1094 LEU A N   
1365 C CA  . LEU A 175 ? 0.56540 0.51233 0.38667 -0.03162 -0.00975 0.07196  1094 LEU A CA  
1366 C C   . LEU A 175 ? 0.59501 0.54041 0.40543 -0.02687 -0.02922 0.08147  1094 LEU A C   
1367 O O   . LEU A 175 ? 0.59160 0.52974 0.42527 -0.01613 -0.04119 0.08235  1094 LEU A O   
1368 C CB  . LEU A 175 ? 0.61500 0.55022 0.43521 -0.04003 -0.00558 0.09154  1094 LEU A CB  
1369 C CG  . LEU A 175 ? 0.54783 0.48250 0.39312 -0.04289 0.00811  0.08474  1094 LEU A CG  
1370 C CD1 . LEU A 175 ? 0.57621 0.50258 0.41500 -0.05639 0.01349  0.10542  1094 LEU A CD1 
1371 C CD2 . LEU A 175 ? 0.55636 0.47900 0.43440 -0.03162 0.00031  0.07632  1094 LEU A CD2 
1372 N N   . ASN A 176 ? 0.59379 0.54843 0.36941 -0.03460 -0.03273 0.08826  1095 ASN A N   
1373 C CA  . ASN A 176 ? 0.65307 0.61074 0.41879 -0.03059 -0.05358 0.09799  1095 ASN A CA  
1374 C C   . ASN A 176 ? 0.64852 0.61688 0.43291 -0.02252 -0.06041 0.07879  1095 ASN A C   
1375 O O   . ASN A 176 ? 0.62623 0.59560 0.42879 -0.01320 -0.07664 0.08430  1095 ASN A O   
1376 C CB  . ASN A 176 ? 0.73505 0.70338 0.45495 -0.04259 -0.05576 0.10677  1095 ASN A CB  
1377 C CG  . ASN A 176 ? 0.82148 0.79312 0.53008 -0.03934 -0.08048 0.12334  1095 ASN A CG  
1378 O OD1 . ASN A 176 ? 0.83821 0.79641 0.56392 -0.03106 -0.09389 0.14279  1095 ASN A OD1 
1379 N ND2 . ASN A 176 ? 0.86352 0.85289 0.54469 -0.04533 -0.08758 0.11501  1095 ASN A ND2 
1380 N N   . LYS A 177 ? 0.58300 0.55966 0.36482 -0.02603 -0.04783 0.05652  1096 LYS A N   
1381 C CA  . LYS A 177 ? 0.61471 0.59859 0.41522 -0.02087 -0.05262 0.03910  1096 LYS A CA  
1382 C C   . LYS A 177 ? 0.57499 0.55158 0.41451 -0.00956 -0.05382 0.03847  1096 LYS A C   
1383 O O   . LYS A 177 ? 0.54904 0.53257 0.40694 -0.00309 -0.06543 0.03707  1096 LYS A O   
1384 C CB  . LYS A 177 ? 0.58894 0.57619 0.38035 -0.02629 -0.03790 0.01663  1096 LYS A CB  
1385 C CG  . LYS A 177 ? 0.68632 0.67644 0.49760 -0.02310 -0.04120 -0.00030 1096 LYS A CG  
1386 C CD  . LYS A 177 ? 0.77925 0.76751 0.57852 -0.02834 -0.02828 -0.02180 1096 LYS A CD  
1387 C CE  . LYS A 177 ? 0.82360 0.81945 0.59218 -0.03813 -0.03557 -0.03131 1096 LYS A CE  
1388 N NZ  . LYS A 177 ? 0.90758 0.91049 0.63992 -0.04508 -0.03841 -0.01962 1096 LYS A NZ  
1389 N N   . LEU A 178 ? 0.50897 0.47385 0.36140 -0.00770 -0.04211 0.03954  1097 LEU A N   
1390 C CA  . LEU A 178 ? 0.47017 0.42791 0.35524 0.00205  -0.04277 0.03670  1097 LEU A CA  
1391 C C   . LEU A 178 ? 0.52571 0.47817 0.42321 0.01067  -0.05746 0.05097  1097 LEU A C   
1392 O O   . LEU A 178 ? 0.50419 0.46083 0.42527 0.01998  -0.06304 0.04559  1097 LEU A O   
1393 C CB  . LEU A 178 ? 0.49385 0.44110 0.38830 0.00057  -0.02961 0.03539  1097 LEU A CB  
1394 C CG  . LEU A 178 ? 0.48829 0.42673 0.41140 0.00937  -0.03115 0.03234  1097 LEU A CG  
1395 C CD1 . LEU A 178 ? 0.45269 0.40048 0.38945 0.01404  -0.03017 0.01680  1097 LEU A CD1 
1396 C CD2 . LEU A 178 ? 0.51600 0.44507 0.44642 0.00545  -0.02119 0.03298  1097 LEU A CD2 
1397 N N   . LEU A 179 ? 0.49588 0.43941 0.37830 0.00811  -0.06351 0.06969  1098 LEU A N   
1398 C CA  . LEU A 179 ? 0.60377 0.53778 0.50096 0.01863  -0.07803 0.08420  1098 LEU A CA  
1399 C C   . LEU A 179 ? 0.66580 0.61902 0.57115 0.02589  -0.09281 0.08259  1098 LEU A C   
1400 O O   . LEU A 179 ? 0.70012 0.65355 0.63292 0.03919  -0.10112 0.08364  1098 LEU A O   
1401 C CB  . LEU A 179 ? 0.67476 0.59410 0.55057 0.01298  -0.08338 0.10774  1098 LEU A CB  
1402 C CG  . LEU A 179 ? 0.69546 0.60819 0.57920 0.02408  -0.10354 0.12628  1098 LEU A CG  
1403 C CD1 . LEU A 179 ? 0.78838 0.67988 0.70570 0.03750  -0.10482 0.12562  1098 LEU A CD1 
1404 C CD2 . LEU A 179 ? 0.77429 0.67791 0.62658 0.01582  -0.11216 0.15253  1098 LEU A CD2 
1405 N N   . GLY A 180 ? 0.61240 0.58371 0.49638 0.01706  -0.09534 0.07752  1099 GLY A N   
1406 C CA  . GLY A 180 ? 0.71011 0.70335 0.60281 0.02084  -0.11029 0.07533  1099 GLY A CA  
1407 C C   . GLY A 180 ? 0.67390 0.67880 0.59759 0.02655  -0.10586 0.05781  1099 GLY A C   
1408 O O   . GLY A 180 ? 0.80646 0.83094 0.74961 0.03246  -0.11773 0.05739  1099 GLY A O   
1409 N N   . GLY A 181 ? 0.57422 0.56972 0.50356 0.02449  -0.08934 0.04452  1100 GLY A N   
1410 C CA  . GLY A 181 ? 0.56023 0.56536 0.51475 0.02828  -0.08419 0.03006  1100 GLY A CA  
1411 C C   . GLY A 181 ? 0.64664 0.64401 0.62833 0.04071  -0.08037 0.02931  1100 GLY A C   
1412 O O   . GLY A 181 ? 0.57806 0.58526 0.57833 0.04327  -0.07499 0.01794  1100 GLY A O   
1413 N N   . VAL A 182 ? 0.60714 0.58551 0.59006 0.04734  -0.08219 0.04038  1101 VAL A N   
1414 C CA  . VAL A 182 ? 0.57237 0.54093 0.57993 0.05938  -0.07901 0.03665  1101 VAL A CA  
1415 C C   . VAL A 182 ? 0.73682 0.71278 0.76747 0.07465  -0.09179 0.04359  1101 VAL A C   
1416 O O   . VAL A 182 ? 0.70588 0.67427 0.75829 0.08679  -0.08905 0.03824  1101 VAL A O   
1417 C CB  . VAL A 182 ? 0.57818 0.51850 0.57827 0.05709  -0.07203 0.04057  1101 VAL A CB  
1418 C CG1 . VAL A 182 ? 0.63994 0.57963 0.62550 0.04465  -0.05881 0.03147  1101 VAL A CG1 
1419 C CG2 . VAL A 182 ? 0.64009 0.56473 0.62591 0.05557  -0.08092 0.06025  1101 VAL A CG2 
1420 N N   . THR A 183 ? 0.68312 0.67407 0.70998 0.07509  -0.10616 0.05475  1102 THR A N   
1421 C CA  . THR A 183 ? 0.83450 0.83729 0.88723 0.09114  -0.12043 0.06261  1102 THR A CA  
1422 C C   . THR A 183 ? 0.82408 0.86419 0.88417 0.08776  -0.13004 0.06038  1102 THR A C   
1423 O O   . THR A 183 ? 0.85908 0.90780 0.89511 0.07197  -0.13012 0.05812  1102 THR A O   
1424 C CB  . THR A 183 ? 0.88191 0.86321 0.92492 0.09667  -0.13422 0.08495  1102 THR A CB  
1425 O OG1 . THR A 183 ? 0.90105 0.88345 0.90805 0.08104  -0.13926 0.09595  1102 THR A OG1 
1426 C CG2 . THR A 183 ? 0.84494 0.78813 0.88770 0.10025  -0.12612 0.08703  1102 THR A CG2 
1427 N N   . ILE A 184 ? 0.85141 0.91461 0.94641 0.10243  -0.13805 0.05982  1103 ILE A N   
1428 C CA  . ILE A 184 ? 0.84666 0.94886 0.95308 0.09890  -0.15081 0.06048  1103 ILE A CA  
1429 C C   . ILE A 184 ? 0.85548 0.96385 0.96612 0.10899  -0.17400 0.08098  1103 ILE A C   
1430 O O   . ILE A 184 ? 0.94351 1.04115 1.07644 0.12851  -0.17992 0.08976  1103 ILE A O   
1431 C CB  . ILE A 184 ? 0.79066 0.92556 0.93659 0.10577  -0.14414 0.04605  1103 ILE A CB  
1432 C CG1 . ILE A 184 ? 0.66007 0.79823 0.79525 0.08890  -0.12679 0.02942  1103 ILE A CG1 
1433 C CG2 . ILE A 184 ? 0.74525 0.92236 0.91558 0.10853  -0.16241 0.05186  1103 ILE A CG2 
1434 C CD1 . ILE A 184 ? 0.44408 0.60977 0.61367 0.09387  -0.11551 0.01600  1103 ILE A CD1 
1435 N N   . GLU B 4   ? 0.87140 1.23398 1.14517 0.00672  -0.00406 0.01181  36   GLU B N   
1436 C CA  . GLU B 4   ? 0.95565 1.29622 1.21016 0.02064  0.01080  0.00921  36   GLU B CA  
1437 C C   . GLU B 4   ? 0.86151 1.17438 1.09402 0.03459  0.00458  0.00716  36   GLU B C   
1438 O O   . GLU B 4   ? 0.80064 1.09608 1.01811 0.02848  -0.00741 0.00630  36   GLU B O   
1439 C CB  . GLU B 4   ? 0.85781 1.17247 1.08909 0.00865  0.01914  0.00572  36   GLU B CB  
1440 C CG  . GLU B 4   ? 0.91796 1.22708 1.14034 0.01800  0.03687  0.00442  36   GLU B CG  
1441 C CD  . GLU B 4   ? 0.93488 1.28133 1.18592 0.01816  0.04951  0.00977  36   GLU B CD  
1442 O OE1 . GLU B 4   ? 0.91078 1.28075 1.18450 0.00230  0.04533  0.01431  36   GLU B OE1 
1443 O OE2 . GLU B 4   ? 0.98341 1.33470 1.23393 0.03384  0.06428  0.00949  36   GLU B OE2 
1444 N N   . SER B 5   ? 0.69476 1.00080 0.92327 0.05337  0.01392  0.00658  37   SER B N   
1445 C CA  . SER B 5   ? 0.57202 0.84799 0.77945 0.06647  0.00962  0.00557  37   SER B CA  
1446 C C   . SER B 5   ? 0.51621 0.75426 0.69424 0.06722  0.01910  -0.00065 37   SER B C   
1447 O O   . SER B 5   ? 0.46878 0.70572 0.64402 0.07439  0.03216  -0.00384 37   SER B O   
1448 C CB  . SER B 5   ? 0.49408 0.78562 0.71765 0.08893  0.01016  0.00987  37   SER B CB  
1449 O OG  . SER B 5   ? 0.46012 0.71550 0.65930 0.10044  0.00701  0.00950  37   SER B OG  
1450 N N   . TYR B 6   ? 0.46299 0.67066 0.61891 0.05993  0.01233  -0.00217 38   TYR B N   
1451 C CA  . TYR B 6   ? 0.44831 0.61970 0.57862 0.05932  0.01687  -0.00727 38   TYR B CA  
1452 C C   . TYR B 6   ? 0.48810 0.63322 0.60579 0.07348  0.01575  -0.00676 38   TYR B C   
1453 O O   . TYR B 6   ? 0.47395 0.58598 0.57099 0.06994  0.01613  -0.01016 38   TYR B O   
1454 C CB  . TYR B 6   ? 0.49508 0.65206 0.61377 0.04233  0.01122  -0.00778 38   TYR B CB  
1455 C CG  . TYR B 6   ? 0.54869 0.72255 0.67479 0.02861  0.01239  -0.00822 38   TYR B CG  
1456 C CD1 . TYR B 6   ? 0.53764 0.70347 0.65386 0.02309  0.01895  -0.01184 38   TYR B CD1 
1457 C CD2 . TYR B 6   ? 0.44036 0.63449 0.58012 0.02087  0.00592  -0.00495 38   TYR B CD2 
1458 C CE1 . TYR B 6   ? 0.50688 0.68412 0.62754 0.01126  0.02037  -0.01072 38   TYR B CE1 
1459 C CE2 . TYR B 6   ? 0.50712 0.71083 0.65162 0.00763  0.00726  -0.00516 38   TYR B CE2 
1460 C CZ  . TYR B 6   ? 0.55192 0.74683 0.68719 0.00344  0.01515  -0.00731 38   TYR B CZ  
1461 O OH  . TYR B 6   ? 0.58480 0.78523 0.72233 -0.00877 0.01693  -0.00604 38   TYR B OH  
1462 N N   . ALA B 7   ? 0.49555 0.65469 0.62636 0.08924  0.01383  -0.00195 39   ALA B N   
1463 C CA  . ALA B 7   ? 0.44560 0.57788 0.56369 0.10240  0.01054  0.00128  39   ALA B CA  
1464 C C   . ALA B 7   ? 0.54178 0.63565 0.63772 0.10910  0.01885  -0.00532 39   ALA B C   
1465 O O   . ALA B 7   ? 0.51357 0.57181 0.59034 0.10625  0.01569  -0.00479 39   ALA B O   
1466 C CB  . ALA B 7   ? 0.52566 0.68289 0.66368 0.12141  0.00730  0.00804  39   ALA B CB  
1467 N N   . ILE B 8   ? 0.47743 0.57600 0.57378 0.11703  0.02982  -0.01168 40   ILE B N   
1468 C CA  . ILE B 8   ? 0.51517 0.57241 0.58474 0.12367  0.03667  -0.01999 40   ILE B CA  
1469 C C   . ILE B 8   ? 0.45034 0.47851 0.49938 0.10295  0.03122  -0.02470 40   ILE B C   
1470 O O   . ILE B 8   ? 0.58214 0.56949 0.61004 0.10266  0.02930  -0.02811 40   ILE B O   
1471 C CB  . ILE B 8   ? 0.53223 0.59968 0.60119 0.13599  0.05102  -0.02659 40   ILE B CB  
1472 C CG1 . ILE B 8   ? 0.62409 0.71022 0.71121 0.16241  0.05822  -0.02206 40   ILE B CG1 
1473 C CG2 . ILE B 8   ? 0.64424 0.66572 0.67730 0.13609  0.05615  -0.03828 40   ILE B CG2 
1474 C CD1 . ILE B 8   ? 0.66021 0.80235 0.78720 0.16369  0.05508  -0.01219 40   ILE B CD1 
1475 N N   . TYR B 9   ? 0.47373 0.52233 0.53031 0.08522  0.02817  -0.02431 41   TYR B N   
1476 C CA  . TYR B 9   ? 0.49753 0.52495 0.53979 0.06693  0.02268  -0.02767 41   TYR B CA  
1477 C C   . TYR B 9   ? 0.48371 0.50106 0.52833 0.05804  0.01454  -0.02063 41   TYR B C   
1478 O O   . TYR B 9   ? 0.50296 0.49246 0.53528 0.04840  0.01093  -0.02227 41   TYR B O   
1479 C CB  . TYR B 9   ? 0.44235 0.49348 0.49092 0.05401  0.02321  -0.02876 41   TYR B CB  
1480 C CG  . TYR B 9   ? 0.50422 0.57285 0.55485 0.06416  0.03378  -0.03199 41   TYR B CG  
1481 C CD1 . TYR B 9   ? 0.55197 0.65823 0.62518 0.06369  0.03720  -0.02679 41   TYR B CD1 
1482 C CD2 . TYR B 9   ? 0.56553 0.61170 0.59465 0.07405  0.04110  -0.04015 41   TYR B CD2 
1483 C CE1 . TYR B 9   ? 0.61616 0.74109 0.69442 0.07249  0.04926  -0.02801 41   TYR B CE1 
1484 C CE2 . TYR B 9   ? 0.59797 0.66037 0.62774 0.08509  0.05392  -0.04228 41   TYR B CE2 
1485 C CZ  . TYR B 9   ? 0.61278 0.71646 0.66909 0.08406  0.05872  -0.03537 41   TYR B CZ  
1486 O OH  . TYR B 9   ? 0.70753 0.82953 0.76692 0.09443  0.07382  -0.03603 41   TYR B OH  
1487 N N   . VAL B 10  ? 0.50309 0.54269 0.56271 0.06075  0.01160  -0.01254 42   VAL B N   
1488 C CA  . VAL B 10  ? 0.45802 0.48499 0.51463 0.05596  0.00625  -0.00493 42   VAL B CA  
1489 C C   . VAL B 10  ? 0.50700 0.49689 0.54849 0.06443  0.00704  -0.00376 42   VAL B C   
1490 O O   . VAL B 10  ? 0.49881 0.46370 0.53132 0.05416  0.00531  -0.00102 42   VAL B O   
1491 C CB  . VAL B 10  ? 0.44633 0.49963 0.51501 0.06048  0.00184  0.00257  42   VAL B CB  
1492 C CG1 . VAL B 10  ? 0.44483 0.48083 0.50351 0.05805  -0.00195 0.01123  42   VAL B CG1 
1493 C CG2 . VAL B 10  ? 0.46349 0.54605 0.54430 0.04934  0.00046  0.00091  42   VAL B CG2 
1494 N N   . TYR B 11  ? 0.51393 0.49897 0.55337 0.08332  0.01060  -0.00553 43   TYR B N   
1495 C CA  . TYR B 11  ? 0.56325 0.50812 0.58599 0.09423  0.01189  -0.00455 43   TYR B CA  
1496 C C   . TYR B 11  ? 0.57049 0.47768 0.57439 0.08292  0.01280  -0.01348 43   TYR B C   
1497 O O   . TYR B 11  ? 0.61994 0.49097 0.61119 0.07735  0.01058  -0.01048 43   TYR B O   
1498 C CB  . TYR B 11  ? 0.63376 0.58517 0.66045 0.11946  0.01682  -0.00528 43   TYR B CB  
1499 C CG  . TYR B 11  ? 0.80396 0.72736 0.82111 0.13687  0.01579  0.00231  43   TYR B CG  
1500 C CD1 . TYR B 11  ? 0.80463 0.74894 0.83335 0.14647  0.00973  0.01436  43   TYR B CD1 
1501 C CD2 . TYR B 11  ? 0.94728 0.82107 0.94151 0.14437  0.01984  -0.00245 43   TYR B CD2 
1502 C CE1 . TYR B 11  ? 1.05665 0.97478 1.07498 0.16417  0.00802  0.02313  43   TYR B CE1 
1503 C CE2 . TYR B 11  ? 1.07441 0.91859 1.05838 0.16168  0.01927  0.00575  43   TYR B CE2 
1504 C CZ  . TYR B 11  ? 1.20871 1.07619 1.20520 0.17222  0.01354  0.01935  43   TYR B CZ  
1505 O OH  . TYR B 11  ? 1.29668 1.13375 1.28109 0.19083  0.01222  0.02916  43   TYR B OH  
1506 N N   . LYS B 12  ? 0.59180 0.50598 0.59258 0.07809  0.01522  -0.02399 44   LYS B N   
1507 C CA  . LYS B 12  ? 0.61833 0.49871 0.59989 0.06503  0.01244  -0.03316 44   LYS B CA  
1508 C C   . LYS B 12  ? 0.50484 0.38326 0.49318 0.04209  0.00496  -0.02776 44   LYS B C   
1509 O O   . LYS B 12  ? 0.60678 0.45030 0.58409 0.03183  0.00090  -0.02883 44   LYS B O   
1510 C CB  . LYS B 12  ? 0.62243 0.51342 0.59651 0.06367  0.01522  -0.04413 44   LYS B CB  
1511 C CG  . LYS B 12  ? 0.69812 0.57960 0.65703 0.08478  0.02529  -0.05279 44   LYS B CG  
1512 C CD  . LYS B 12  ? 0.71565 0.62944 0.67831 0.08355  0.03071  -0.05678 44   LYS B CD  
1513 C CE  . LYS B 12  ? 0.76705 0.66296 0.70500 0.09956  0.04154  -0.06793 44   LYS B CE  
1514 N NZ  . LYS B 12  ? 0.97578 0.84115 0.88319 0.08510  0.03482  -0.07913 44   LYS B NZ  
1515 N N   . VAL B 13  ? 0.48203 0.39724 0.48945 0.03375  0.00366  -0.02166 45   VAL B N   
1516 C CA  . VAL B 13  ? 0.45502 0.37237 0.47156 0.01476  -0.00086 -0.01562 45   VAL B CA  
1517 C C   . VAL B 13  ? 0.51836 0.41445 0.53303 0.01457  0.00005  -0.00542 45   VAL B C   
1518 O O   . VAL B 13  ? 0.51513 0.39182 0.52981 -0.00031 -0.00232 -0.00243 45   VAL B O   
1519 C CB  . VAL B 13  ? 0.41333 0.37047 0.44741 0.00951  -0.00066 -0.01142 45   VAL B CB  
1520 C CG1 . VAL B 13  ? 0.43373 0.39396 0.47834 -0.00581 -0.00235 -0.00371 45   VAL B CG1 
1521 C CG2 . VAL B 13  ? 0.47246 0.44537 0.50642 0.00640  -0.00173 -0.01984 45   VAL B CG2 
1522 N N   . LEU B 14  ? 0.47862 0.37833 0.49200 0.03075  0.00313  0.00103  46   LEU B N   
1523 C CA  . LEU B 14  ? 0.53612 0.41296 0.54298 0.03255  0.00435  0.01238  46   LEU B CA  
1524 C C   . LEU B 14  ? 0.57875 0.40782 0.56967 0.02976  0.00400  0.00973  46   LEU B C   
1525 O O   . LEU B 14  ? 0.62336 0.42971 0.61181 0.01812  0.00457  0.01808  46   LEU B O   
1526 C CB  . LEU B 14  ? 0.49582 0.38351 0.50123 0.05310  0.00503  0.01898  46   LEU B CB  
1527 C CG  . LEU B 14  ? 0.51752 0.37891 0.51071 0.05933  0.00589  0.03209  46   LEU B CG  
1528 C CD1 . LEU B 14  ? 0.50419 0.36847 0.49935 0.04287  0.00800  0.04202  46   LEU B CD1 
1529 C CD2 . LEU B 14  ? 0.52071 0.39880 0.51405 0.08076  0.00328  0.03765  46   LEU B CD2 
1530 N N   . LYS B 15  ? 0.64834 0.45971 0.62712 0.03927  0.00383  -0.00209 47   LYS B N   
1531 C CA  . LYS B 15  ? 0.69689 0.45576 0.65573 0.03708  0.00283  -0.00614 47   LYS B CA  
1532 C C   . LYS B 15  ? 0.68826 0.43368 0.64892 0.01020  -0.00333 -0.01023 47   LYS B C   
1533 O O   . LYS B 15  ? 0.73316 0.43590 0.68247 0.00051  -0.00556 -0.00931 47   LYS B O   
1534 C CB  . LYS B 15  ? 0.81062 0.54960 0.75130 0.05564  0.00541  -0.01923 47   LYS B CB  
1535 C CG  . LYS B 15  ? 0.92545 0.67426 0.86659 0.08519  0.01164  -0.01502 47   LYS B CG  
1536 C CD  . LYS B 15  ? 0.89810 0.65771 0.84864 0.09207  0.01132  0.00201  47   LYS B CD  
1537 C CE  . LYS B 15  ? 0.95705 0.66737 0.89115 0.09051  0.01113  0.01130  47   LYS B CE  
1538 N NZ  . LYS B 15  ? 0.74833 0.47860 0.69212 0.08554  0.01005  0.02789  47   LYS B NZ  
1539 N N   . GLN B 16  ? 0.70637 0.48728 0.68244 -0.00247 -0.00692 -0.01383 48   GLN B N   
1540 C CA  . GLN B 16  ? 0.68969 0.46619 0.67378 -0.02781 -0.01456 -0.01560 48   GLN B CA  
1541 C C   . GLN B 16  ? 0.70566 0.48925 0.70855 -0.04209 -0.01199 0.00004  48   GLN B C   
1542 O O   . GLN B 16  ? 0.72149 0.48120 0.72729 -0.06060 -0.01583 0.00274  48   GLN B O   
1543 C CB  . GLN B 16  ? 0.71706 0.53038 0.71203 -0.03410 -0.01925 -0.02239 48   GLN B CB  
1544 C CG  . GLN B 16  ? 0.76099 0.56617 0.73534 -0.02486 -0.02163 -0.03767 48   GLN B CG  
1545 C CD  . GLN B 16  ? 0.83231 0.67481 0.81711 -0.03074 -0.02541 -0.04078 48   GLN B CD  
1546 O OE1 . GLN B 16  ? 0.78013 0.65876 0.78740 -0.03349 -0.02299 -0.03169 48   GLN B OE1 
1547 N NE2 . GLN B 16  ? 0.88367 0.71425 0.84877 -0.03189 -0.03118 -0.05351 48   GLN B NE2 
1548 N N   . VAL B 17  ? 0.63516 0.45168 0.65065 -0.03474 -0.00523 0.01042  49   VAL B N   
1549 C CA  . VAL B 17  ? 0.65831 0.48598 0.69018 -0.04728 -0.00026 0.02506  49   VAL B CA  
1550 C C   . VAL B 17  ? 0.58620 0.38286 0.60547 -0.04204 0.00640  0.03758  49   VAL B C   
1551 O O   . VAL B 17  ? 0.60883 0.39909 0.63711 -0.05651 0.01116  0.04963  49   VAL B O   
1552 C CB  . VAL B 17  ? 0.61943 0.49248 0.66596 -0.04294 0.00409  0.02961  49   VAL B CB  
1553 C CG1 . VAL B 17  ? 0.59500 0.49570 0.65329 -0.04843 -0.00224 0.01922  49   VAL B CG1 
1554 C CG2 . VAL B 17  ? 0.56541 0.44589 0.59977 -0.02156 0.00769  0.03161  49   VAL B CG2 
1555 N N   . HIS B 18  ? 0.61165 0.39040 0.61130 -0.02091 0.00756  0.03653  50   HIS B N   
1556 C CA  . HIS B 18  ? 0.63823 0.38374 0.62197 -0.01270 0.01267  0.04924  50   HIS B CA  
1557 C C   . HIS B 18  ? 0.72652 0.43670 0.68903 0.00568  0.01002  0.04143  50   HIS B C   
1558 O O   . HIS B 18  ? 0.68079 0.40083 0.63658 0.02890  0.01075  0.04203  50   HIS B O   
1559 C CB  . HIS B 18  ? 0.64078 0.41107 0.62351 -0.00027 0.01801  0.06175  50   HIS B CB  
1560 C CG  . HIS B 18  ? 0.59272 0.38665 0.58956 -0.01560 0.02440  0.07194  50   HIS B CG  
1561 N ND1 . HIS B 18  ? 0.70032 0.47375 0.69897 -0.03121 0.03155  0.08495  50   HIS B ND1 
1562 C CD2 . HIS B 18  ? 0.50861 0.34359 0.51753 -0.01629 0.02637  0.07176  50   HIS B CD2 
1563 C CE1 . HIS B 18  ? 0.59506 0.39915 0.60785 -0.03975 0.03881  0.09230  50   HIS B CE1 
1564 N NE2 . HIS B 18  ? 0.49749 0.33698 0.51509 -0.03035 0.03545  0.08382  50   HIS B NE2 
1565 N N   . PRO B 19  ? 0.75832 0.42596 0.71000 -0.00384 0.00669  0.03399  51   PRO B N   
1566 C CA  . PRO B 19  ? 0.74368 0.37626 0.67290 0.01518  0.00522  0.02292  51   PRO B CA  
1567 C C   . PRO B 19  ? 0.84573 0.45557 0.75917 0.04029  0.00996  0.03334  51   PRO B C   
1568 O O   . PRO B 19  ? 0.82846 0.43079 0.73100 0.06409  0.01066  0.02563  51   PRO B O   
1569 C CB  . PRO B 19  ? 0.82368 0.40759 0.74134 -0.00489 0.00008  0.01502  51   PRO B CB  
1570 C CG  . PRO B 19  ? 0.81118 0.42557 0.75351 -0.03351 -0.00435 0.01601  51   PRO B CG  
1571 C CD  . PRO B 19  ? 0.80820 0.46248 0.76960 -0.03307 0.00292  0.03295  51   PRO B CD  
1572 N N   . ASP B 20  ? 0.81031 0.40953 0.72180 0.03717  0.01377  0.05147  52   ASP B N   
1573 C CA  . ASP B 20  ? 0.80890 0.38046 0.70192 0.06081  0.01664  0.06333  52   ASP B CA  
1574 C C   . ASP B 20  ? 0.78800 0.40162 0.68774 0.07523  0.01725  0.07582  52   ASP B C   
1575 O O   . ASP B 20  ? 0.79483 0.38863 0.67931 0.09079  0.01851  0.09041  52   ASP B O   
1576 C CB  . ASP B 20  ? 0.95129 0.46632 0.82834 0.04801  0.02012  0.07586  52   ASP B CB  
1577 C CG  . ASP B 20  ? 1.00734 0.47206 0.87302 0.03473  0.01709  0.06248  52   ASP B CG  
1578 O OD1 . ASP B 20  ? 1.05305 0.50539 0.90779 0.05102  0.01445  0.04651  52   ASP B OD1 
1579 O OD2 . ASP B 20  ? 1.11382 0.55165 0.98120 0.00768  0.01744  0.06768  52   ASP B OD2 
1580 N N   . THR B 21  ? 0.72526 0.39353 0.64485 0.07064  0.01528  0.07036  53   THR B N   
1581 C CA  . THR B 21  ? 0.66406 0.37085 0.58815 0.08048  0.01404  0.08010  53   THR B CA  
1582 C C   . THR B 21  ? 0.60466 0.34990 0.54028 0.09952  0.00873  0.07051  53   THR B C   
1583 O O   . THR B 21  ? 0.65206 0.41924 0.60159 0.09377  0.00811  0.05612  53   THR B O   
1584 C CB  . THR B 21  ? 0.68138 0.41840 0.61841 0.05870  0.01700  0.08310  53   THR B CB  
1585 O OG1 . THR B 21  ? 0.68307 0.38848 0.61378 0.04092  0.02374  0.09412  53   THR B OG1 
1586 C CG2 . THR B 21  ? 0.62227 0.39309 0.55748 0.06895  0.01498  0.09127  53   THR B CG2 
1587 N N   . GLY B 22  ? 0.64476 0.39912 0.57519 0.12172  0.00456  0.07960  54   GLY B N   
1588 C CA  . GLY B 22  ? 0.58707 0.38443 0.53387 0.13831  -0.00109 0.07337  54   GLY B CA  
1589 C C   . GLY B 22  ? 0.53659 0.38126 0.49594 0.12865  -0.00568 0.07389  54   GLY B C   
1590 O O   . GLY B 22  ? 0.49944 0.34432 0.45387 0.11094  -0.00313 0.07817  54   GLY B O   
1591 N N   . ILE B 23  ? 0.50920 0.39433 0.48578 0.14068  -0.01190 0.06935  55   ILE B N   
1592 C CA  . ILE B 23  ? 0.45087 0.37781 0.43737 0.13307  -0.01845 0.06936  55   ILE B CA  
1593 C C   . ILE B 23  ? 0.49924 0.45807 0.49797 0.15305  -0.02918 0.07269  55   ILE B C   
1594 O O   . ILE B 23  ? 0.48076 0.45178 0.49617 0.16760  -0.02838 0.06786  55   ILE B O   
1595 C CB  . ILE B 23  ? 0.46237 0.41296 0.46538 0.11435  -0.01446 0.05626  55   ILE B CB  
1596 C CG1 . ILE B 23  ? 0.36930 0.35450 0.37818 0.10536  -0.02064 0.05623  55   ILE B CG1 
1597 C CG2 . ILE B 23  ? 0.48322 0.44490 0.50263 0.12155  -0.01109 0.04478  55   ILE B CG2 
1598 C CD1 . ILE B 23  ? 0.36246 0.36509 0.38393 0.08642  -0.01611 0.04555  55   ILE B CD1 
1599 N N   . SER B 24  ? 0.43245 0.40530 0.42262 0.15418  -0.03932 0.08120  56   SER B N   
1600 C CA  . SER B 24  ? 0.44608 0.45002 0.44830 0.17227  -0.05315 0.08603  56   SER B CA  
1601 C C   . SER B 24  ? 0.43902 0.49253 0.47358 0.16623  -0.05717 0.07521  56   SER B C   
1602 O O   . SER B 24  ? 0.42571 0.48788 0.46663 0.14706  -0.05099 0.06536  56   SER B O   
1603 C CB  . SER B 24  ? 0.48854 0.49103 0.46724 0.17390  -0.06536 0.09753  56   SER B CB  
1604 O OG  . SER B 24  ? 0.45925 0.48405 0.43768 0.15498  -0.06900 0.09090  56   SER B OG  
1605 N N   . SER B 25  ? 0.44238 0.52963 0.49908 0.18298  -0.06779 0.07842  57   SER B N   
1606 C CA  A SER B 25  ? 0.43552 0.57231 0.52673 0.17659  -0.07123 0.07017  57   SER B CA  
1607 C CA  B SER B 25  ? 0.43547 0.57240 0.52671 0.17659  -0.07131 0.07020  57   SER B CA  
1608 C C   . SER B 25  ? 0.40216 0.55452 0.48838 0.15387  -0.07904 0.06571  57   SER B C   
1609 O O   . SER B 25  ? 0.36801 0.53760 0.46930 0.13782  -0.07338 0.05590  57   SER B O   
1610 C CB  A SER B 25  ? 0.46256 0.63713 0.58158 0.19796  -0.08318 0.07704  57   SER B CB  
1611 C CB  B SER B 25  ? 0.46246 0.63737 0.58138 0.19774  -0.08350 0.07709  57   SER B CB  
1612 O OG  A SER B 25  ? 0.44264 0.66757 0.59869 0.18964  -0.08578 0.07055  57   SER B OG  
1613 O OG  B SER B 25  ? 0.48226 0.64445 0.60862 0.22066  -0.07342 0.07948  57   SER B OG  
1614 N N   . LYS B 26  ? 0.44277 0.58517 0.50385 0.15294  -0.09136 0.07284  58   LYS B N   
1615 C CA  . LYS B 26  ? 0.41709 0.56916 0.46833 0.13314  -0.09844 0.06736  58   LYS B CA  
1616 C C   . LYS B 26  ? 0.42696 0.55170 0.46114 0.11561  -0.08268 0.06092  58   LYS B C   
1617 O O   . LYS B 26  ? 0.38300 0.51978 0.42057 0.09888  -0.08286 0.05260  58   LYS B O   
1618 C CB  . LYS B 26  ? 0.39925 0.54522 0.42226 0.13834  -0.11578 0.07600  58   LYS B CB  
1619 C CG  . LYS B 26  ? 0.39029 0.57355 0.43571 0.15265  -0.13645 0.08159  58   LYS B CG  
1620 C CD  . LYS B 26  ? 0.49689 0.68120 0.51426 0.15084  -0.15818 0.08591  58   LYS B CD  
1621 C CE  . LYS B 26  ? 0.55376 0.77248 0.59203 0.16826  -0.18073 0.09454  58   LYS B CE  
1622 N NZ  . LYS B 26  ? 0.76616 0.97819 0.76844 0.17106  -0.20395 0.10124  58   LYS B NZ  
1623 N N   . ALA B 27  ? 0.39047 0.47825 0.40703 0.11872  -0.06972 0.06520  59   ALA B N   
1624 C CA  . ALA B 27  ? 0.42486 0.49322 0.43327 0.10198  -0.05535 0.05963  59   ALA B CA  
1625 C C   . ALA B 27  ? 0.35061 0.43584 0.38604 0.09392  -0.04764 0.04858  59   ALA B C   
1626 O O   . ALA B 27  ? 0.34260 0.43054 0.37952 0.07819  -0.04221 0.04179  59   ALA B O   
1627 C CB  . ALA B 27  ? 0.45821 0.48537 0.44580 0.10489  -0.04450 0.06760  59   ALA B CB  
1628 N N   . MET B 28  ? 0.35300 0.44864 0.40802 0.10598  -0.04629 0.04715  60   MET B N   
1629 C CA  . MET B 28  ? 0.34472 0.45607 0.42108 0.09953  -0.03817 0.03725  60   MET B CA  
1630 C C   . MET B 28  ? 0.33245 0.48018 0.42690 0.08829  -0.04443 0.03213  60   MET B C   
1631 O O   . MET B 28  ? 0.33992 0.49274 0.44091 0.07484  -0.03766 0.02484  60   MET B O   
1632 C CB  . MET B 28  ? 0.34647 0.46154 0.43731 0.11744  -0.03366 0.03690  60   MET B CB  
1633 C CG  . MET B 28  ? 0.35974 0.49223 0.46879 0.11146  -0.02425 0.02713  60   MET B CG  
1634 S SD  . MET B 28  ? 0.40427 0.50097 0.49435 0.09635  -0.01291 0.01956  60   MET B SD  
1635 C CE  . MET B 28  ? 0.43248 0.48861 0.50683 0.11311  -0.00650 0.02034  60   MET B CE  
1636 N N   . SER B 29  ? 0.34292 0.51436 0.44454 0.09282  -0.05846 0.03623  61   SER B N   
1637 C CA  A SER B 29  ? 0.36743 0.57034 0.48543 0.07954  -0.06646 0.03140  61   SER B CA  
1638 C CA  B SER B 29  ? 0.36925 0.57213 0.48733 0.07948  -0.06634 0.03135  61   SER B CA  
1639 C C   . SER B 29  ? 0.35981 0.54539 0.45719 0.06156  -0.06460 0.02646  61   SER B C   
1640 O O   . SER B 29  ? 0.30725 0.50484 0.41565 0.04771  -0.06194 0.01986  61   SER B O   
1641 C CB  A SER B 29  ? 0.37540 0.60405 0.50200 0.08664  -0.08546 0.03697  61   SER B CB  
1642 C CB  B SER B 29  ? 0.37270 0.60194 0.50001 0.08637  -0.08526 0.03678  61   SER B CB  
1643 O OG  A SER B 29  ? 0.32362 0.58073 0.46634 0.07118  -0.09512 0.03194  61   SER B OG  
1644 O OG  B SER B 29  ? 0.35965 0.61335 0.51438 0.10383  -0.08618 0.04153  61   SER B OG  
1645 N N   . ILE B 30  ? 0.31495 0.47144 0.38194 0.06256  -0.06464 0.03046  62   ILE B N   
1646 C CA  . ILE B 30  ? 0.31025 0.44910 0.35757 0.04874  -0.05951 0.02649  62   ILE B CA  
1647 C C   . ILE B 30  ? 0.34634 0.47688 0.40193 0.04075  -0.04462 0.02174  62   ILE B C   
1648 O O   . ILE B 30  ? 0.33097 0.46432 0.38843 0.02852  -0.04157 0.01587  62   ILE B O   
1649 C CB  . ILE B 30  ? 0.35807 0.46863 0.37152 0.05363  -0.05937 0.03369  62   ILE B CB  
1650 C CG1 . ILE B 30  ? 0.38760 0.50653 0.38740 0.05922  -0.07703 0.03690  62   ILE B CG1 
1651 C CG2 . ILE B 30  ? 0.36063 0.45248 0.35686 0.04221  -0.04848 0.03062  62   ILE B CG2 
1652 C CD1 . ILE B 30  ? 0.44707 0.53768 0.40906 0.06755  -0.07765 0.04636  62   ILE B CD1 
1653 N N   . MET B 31  ? 0.30223 0.42084 0.36170 0.04773  -0.03636 0.02400  63   MET B N   
1654 C CA  . MET B 31  ? 0.30770 0.41897 0.37387 0.04009  -0.02531 0.01906  63   MET B CA  
1655 C C   . MET B 31  ? 0.35261 0.48810 0.43878 0.03386  -0.02485 0.01228  63   MET B C   
1656 O O   . MET B 31  ? 0.29976 0.43369 0.38687 0.02289  -0.01982 0.00807  63   MET B O   
1657 C CB  . MET B 31  ? 0.31590 0.40901 0.38099 0.04906  -0.01954 0.02111  63   MET B CB  
1658 C CG  . MET B 31  ? 0.35200 0.41336 0.39866 0.04836  -0.01476 0.02741  63   MET B CG  
1659 S SD  . MET B 31  ? 0.35744 0.40957 0.39577 0.03288  -0.00823 0.02836  63   MET B SD  
1660 C CE  . MET B 31  ? 0.33324 0.38764 0.38701 0.02367  -0.00321 0.01992  63   MET B CE  
1661 N N   . ASN B 32  ? 0.32097 0.47980 0.42437 0.04138  -0.02939 0.01247  64   ASN B N   
1662 C CA  A ASN B 32  ? 0.31423 0.49841 0.43839 0.03493  -0.02731 0.00801  64   ASN B CA  
1663 C CA  B ASN B 32  ? 0.31826 0.50249 0.44244 0.03502  -0.02736 0.00804  64   ASN B CA  
1664 C C   . ASN B 32  ? 0.34446 0.53578 0.46771 0.01984  -0.03263 0.00533  64   ASN B C   
1665 O O   . ASN B 32  ? 0.31983 0.51458 0.44866 0.00962  -0.02703 0.00165  64   ASN B O   
1666 C CB  A ASN B 32  ? 0.35145 0.56483 0.49875 0.04603  -0.03106 0.01063  64   ASN B CB  
1667 C CB  B ASN B 32  ? 0.35916 0.57203 0.50598 0.04648  -0.03132 0.01083  64   ASN B CB  
1668 C CG  A ASN B 32  ? 0.35736 0.56742 0.51029 0.05938  -0.02012 0.00995  64   ASN B CG  
1669 C CG  B ASN B 32  ? 0.37303 0.61264 0.54342 0.04144  -0.02484 0.00803  64   ASN B CG  
1670 O OD1 A ASN B 32  ? 0.41155 0.60387 0.55474 0.05588  -0.01018 0.00544  64   ASN B OD1 
1671 O OD1 B ASN B 32  ? 0.41038 0.64038 0.57664 0.03813  -0.01345 0.00427  64   ASN B OD1 
1672 N ND2 A ASN B 32  ? 0.36430 0.59095 0.53194 0.07574  -0.02251 0.01421  64   ASN B ND2 
1673 N ND2 B ASN B 32  ? 0.38898 0.66305 0.58420 0.04020  -0.03243 0.01058  64   ASN B ND2 
1674 N N   . SER B 33  ? 0.27192 0.46176 0.38440 0.01876  -0.04362 0.00706  65   SER B N   
1675 C CA  A SER B 33  ? 0.31700 0.50648 0.42283 0.00492  -0.04914 0.00297  65   SER B CA  
1676 C CA  B SER B 33  ? 0.32839 0.51787 0.43419 0.00493  -0.04918 0.00298  65   SER B CA  
1677 C C   . SER B 33  ? 0.32504 0.48966 0.41384 -0.00178 -0.03944 0.00037  65   SER B C   
1678 O O   . SER B 33  ? 0.33054 0.49446 0.42027 -0.01274 -0.03816 -0.00374 65   SER B O   
1679 C CB  A SER B 33  ? 0.32364 0.51161 0.41418 0.00649  -0.06371 0.00435  65   SER B CB  
1680 C CB  B SER B 33  ? 0.32224 0.51019 0.41269 0.00645  -0.06379 0.00433  65   SER B CB  
1681 O OG  A SER B 33  ? 0.30299 0.51962 0.41436 0.01217  -0.07523 0.00742  65   SER B OG  
1682 O OG  B SER B 33  ? 0.38781 0.54739 0.44875 0.01185  -0.06044 0.00703  65   SER B OG  
1683 N N   . PHE B 34  ? 0.26323 0.40749 0.33784 0.00458  -0.03264 0.00359  66   PHE B N   
1684 C CA  . PHE B 34  ? 0.28865 0.41535 0.35377 -0.00096 -0.02326 0.00251  66   PHE B CA  
1685 C C   . PHE B 34  ? 0.33352 0.46652 0.41360 -0.00640 -0.01691 -0.00039 66   PHE B C   
1686 O O   . PHE B 34  ? 0.30828 0.43743 0.38692 -0.01390 -0.01397 -0.00279 66   PHE B O   
1687 C CB  . PHE B 34  ? 0.30137 0.40987 0.35572 0.00498  -0.01675 0.00788  66   PHE B CB  
1688 C CG  . PHE B 34  ? 0.29893 0.39445 0.33123 0.00983  -0.01904 0.01250  66   PHE B CG  
1689 C CD1 . PHE B 34  ? 0.30861 0.40272 0.32508 0.00752  -0.02524 0.00979  66   PHE B CD1 
1690 C CD2 . PHE B 34  ? 0.35123 0.43183 0.37515 0.01606  -0.01423 0.01972  66   PHE B CD2 
1691 C CE1 . PHE B 34  ? 0.37995 0.45868 0.36935 0.01317  -0.02649 0.01427  66   PHE B CE1 
1692 C CE2 . PHE B 34  ? 0.36480 0.43129 0.36503 0.02096  -0.01433 0.02575  66   PHE B CE2 
1693 C CZ  . PHE B 34  ? 0.39016 0.45594 0.37173 0.02023  -0.02006 0.02304  66   PHE B CZ  
1694 N N   . VAL B 35  ? 0.26264 0.40252 0.35392 -0.00129 -0.01439 -0.00001 67   VAL B N   
1695 C CA  . VAL B 35  ? 0.25905 0.40194 0.35820 -0.00541 -0.00832 -0.00266 67   VAL B CA  
1696 C C   . VAL B 35  ? 0.27052 0.42919 0.37945 -0.01331 -0.00949 -0.00466 67   VAL B C   
1697 O O   . VAL B 35  ? 0.26858 0.42315 0.37627 -0.02039 -0.00565 -0.00572 67   VAL B O   
1698 C CB  . VAL B 35  ? 0.31899 0.46256 0.42262 0.00314  -0.00479 -0.00315 67   VAL B CB  
1699 C CG1 . VAL B 35  ? 0.35024 0.49498 0.45570 -0.00088 0.00106  -0.00630 67   VAL B CG1 
1700 C CG2 . VAL B 35  ? 0.30990 0.43219 0.40276 0.00818  -0.00385 -0.00108 67   VAL B CG2 
1701 N N   . ASN B 36  ? 0.25327 0.43040 0.37316 -0.01270 -0.01541 -0.00424 68   ASN B N   
1702 C CA  A ASN B 36  ? 0.27131 0.46464 0.40395 -0.02296 -0.01691 -0.00522 68   ASN B CA  
1703 C CA  B ASN B 36  ? 0.28311 0.47620 0.41565 -0.02298 -0.01670 -0.00523 68   ASN B CA  
1704 C C   . ASN B 36  ? 0.30199 0.47971 0.42195 -0.03356 -0.01970 -0.00747 68   ASN B C   
1705 O O   . ASN B 36  ? 0.28654 0.46325 0.40947 -0.04276 -0.01621 -0.00795 68   ASN B O   
1706 C CB  A ASN B 36  ? 0.29354 0.51269 0.44401 -0.02153 -0.02544 -0.00371 68   ASN B CB  
1707 C CB  B ASN B 36  ? 0.28415 0.50371 0.43529 -0.02176 -0.02473 -0.00371 68   ASN B CB  
1708 C CG  A ASN B 36  ? 0.30148 0.54298 0.47215 -0.01246 -0.01894 -0.00122 68   ASN B CG  
1709 C CG  B ASN B 36  ? 0.30928 0.54704 0.47760 -0.03541 -0.02600 -0.00378 68   ASN B CG  
1710 O OD1 A ASN B 36  ? 0.32990 0.57343 0.50435 -0.01381 -0.00806 -0.00141 68   ASN B OD1 
1711 O OD1 B ASN B 36  ? 0.32714 0.57900 0.51003 -0.03701 -0.01659 -0.00180 68   ASN B OD1 
1712 N ND2 A ASN B 36  ? 0.33109 0.58822 0.51262 -0.00149 -0.02504 0.00149  68   ASN B ND2 
1713 N ND2 B ASN B 36  ? 0.29671 0.53154 0.46093 -0.04606 -0.03706 -0.00605 68   ASN B ND2 
1714 N N   . ASP B 37  ? 0.28262 0.44566 0.38594 -0.03140 -0.02502 -0.00849 69   ASP B N   
1715 C CA  . ASP B 37  ? 0.28279 0.42748 0.37038 -0.03884 -0.02640 -0.01166 69   ASP B CA  
1716 C C   . ASP B 37  ? 0.31182 0.44170 0.39439 -0.03918 -0.01644 -0.01090 69   ASP B C   
1717 O O   . ASP B 37  ? 0.32506 0.44551 0.40411 -0.04641 -0.01505 -0.01246 69   ASP B O   
1718 C CB  . ASP B 37  ? 0.31777 0.44792 0.38382 -0.03385 -0.03150 -0.01267 69   ASP B CB  
1719 C CG  . ASP B 37  ? 0.44677 0.55570 0.49282 -0.03994 -0.03279 -0.01755 69   ASP B CG  
1720 O OD1 . ASP B 37  ? 0.50737 0.61808 0.55308 -0.04960 -0.04232 -0.02187 69   ASP B OD1 
1721 O OD2 . ASP B 37  ? 0.48566 0.57604 0.51732 -0.03512 -0.02407 -0.01708 69   ASP B OD2 
1722 N N   . VAL B 38  ? 0.26688 0.39362 0.34929 -0.03167 -0.01056 -0.00809 70   VAL B N   
1723 C CA  . VAL B 38  ? 0.25951 0.37661 0.34056 -0.03185 -0.00371 -0.00655 70   VAL B CA  
1724 C C   . VAL B 38  ? 0.28254 0.40693 0.37248 -0.03688 -0.00154 -0.00609 70   VAL B C   
1725 O O   . VAL B 38  ? 0.28631 0.40183 0.37289 -0.04005 0.00116  -0.00498 70   VAL B O   
1726 C CB  . VAL B 38  ? 0.25034 0.36409 0.33175 -0.02542 -0.00018 -0.00360 70   VAL B CB  
1727 C CG1 . VAL B 38  ? 0.26637 0.37567 0.35098 -0.02656 0.00390  -0.00156 70   VAL B CG1 
1728 C CG2 . VAL B 38  ? 0.30668 0.41088 0.37679 -0.02091 0.00062  -0.00194 70   VAL B CG2 
1729 N N   . PHE B 39  ? 0.23880 0.37842 0.33873 -0.03607 -0.00148 -0.00604 71   PHE B N   
1730 C CA  . PHE B 39  ? 0.23658 0.38318 0.34201 -0.04056 0.00286  -0.00475 71   PHE B CA  
1731 C C   . PHE B 39  ? 0.23799 0.38237 0.34434 -0.05095 0.00193  -0.00423 71   PHE B C   
1732 O O   . PHE B 39  ? 0.26535 0.40049 0.36669 -0.05501 0.00577  -0.00171 71   PHE B O   
1733 C CB  . PHE B 39  ? 0.22418 0.38961 0.34101 -0.03661 0.00526  -0.00474 71   PHE B CB  
1734 C CG  . PHE B 39  ? 0.22573 0.40057 0.34764 -0.04137 0.01233  -0.00241 71   PHE B CG  
1735 C CD1 . PHE B 39  ? 0.26955 0.45737 0.40397 -0.05124 0.01258  -0.00022 71   PHE B CD1 
1736 C CD2 . PHE B 39  ? 0.25432 0.42319 0.36651 -0.03731 0.01849  -0.00199 71   PHE B CD2 
1737 C CE1 . PHE B 39  ? 0.31944 0.51531 0.45824 -0.05654 0.02141  0.00386  71   PHE B CE1 
1738 C CE2 . PHE B 39  ? 0.27334 0.44883 0.38537 -0.04102 0.02680  0.00127  71   PHE B CE2 
1739 C CZ  . PHE B 39  ? 0.30627 0.49566 0.43239 -0.05050 0.02939  0.00494  71   PHE B CZ  
1740 N N   . GLU B 40  ? 0.23407 0.38464 0.34526 -0.05578 -0.00440 -0.00636 72   GLU B N   
1741 C CA  . GLU B 40  ? 0.27921 0.42630 0.39219 -0.06852 -0.00692 -0.00670 72   GLU B CA  
1742 C C   . GLU B 40  ? 0.28068 0.39904 0.37550 -0.07023 -0.00585 -0.00771 72   GLU B C   
1743 O O   . GLU B 40  ? 0.26591 0.37354 0.35852 -0.07849 -0.00319 -0.00559 72   GLU B O   
1744 C CB  . GLU B 40  ? 0.34253 0.50087 0.46248 -0.07374 -0.01758 -0.00993 72   GLU B CB  
1745 C CG  . GLU B 40  ? 0.34886 0.54073 0.49413 -0.07366 -0.01821 -0.00712 72   GLU B CG  
1746 C CD  . GLU B 40  ? 0.48096 0.68852 0.63657 -0.07869 -0.03184 -0.00928 72   GLU B CD  
1747 O OE1 . GLU B 40  ? 0.45018 0.63896 0.58747 -0.08164 -0.04140 -0.01411 72   GLU B OE1 
1748 O OE2 . GLU B 40  ? 0.44824 0.68763 0.62983 -0.07881 -0.03310 -0.00601 72   GLU B OE2 
1749 N N   . ARG B 41  ? 0.25979 0.36477 0.34158 -0.06174 -0.00669 -0.01002 73   ARG B N   
1750 C CA  . ARG B 41  ? 0.28186 0.36090 0.34767 -0.06038 -0.00417 -0.01096 73   ARG B CA  
1751 C C   . ARG B 41  ? 0.27224 0.34675 0.33917 -0.05565 0.00263  -0.00550 73   ARG B C   
1752 O O   . ARG B 41  ? 0.30222 0.35859 0.36142 -0.05749 0.00500  -0.00377 73   ARG B O   
1753 C CB  . ARG B 41  ? 0.29276 0.36126 0.34458 -0.05224 -0.00512 -0.01440 73   ARG B CB  
1754 C CG  . ARG B 41  ? 0.31101 0.37857 0.35499 -0.05809 -0.01465 -0.02017 73   ARG B CG  
1755 C CD  . ARG B 41  ? 0.36328 0.41213 0.38371 -0.05011 -0.01419 -0.02386 73   ARG B CD  
1756 N NE  . ARG B 41  ? 0.39727 0.45875 0.42170 -0.04048 -0.01128 -0.01982 73   ARG B NE  
1757 C CZ  . ARG B 41  ? 0.50777 0.55912 0.52009 -0.03072 -0.00385 -0.01800 73   ARG B CZ  
1758 N NH1 . ARG B 41  ? 0.54245 0.57217 0.53761 -0.02646 0.00281  -0.02020 73   ARG B NH1 
1759 N NH2 . ARG B 41  ? 0.43790 0.50044 0.45621 -0.02471 -0.00167 -0.01318 73   ARG B NH2 
1760 N N   . ILE B 42  ? 0.24813 0.33669 0.32300 -0.04959 0.00459  -0.00269 74   ILE B N   
1761 C CA  . ILE B 42  ? 0.24848 0.33456 0.32344 -0.04644 0.00775  0.00235  74   ILE B CA  
1762 C C   . ILE B 42  ? 0.28408 0.36895 0.35815 -0.05406 0.00976  0.00572  74   ILE B C   
1763 O O   . ILE B 42  ? 0.27804 0.34908 0.34494 -0.05362 0.01155  0.01031  74   ILE B O   
1764 C CB  . ILE B 42  ? 0.23827 0.33706 0.31917 -0.04104 0.00726  0.00313  74   ILE B CB  
1765 C CG1 . ILE B 42  ? 0.25596 0.35367 0.33867 -0.03473 0.00696  0.00247  74   ILE B CG1 
1766 C CG2 . ILE B 42  ? 0.27183 0.36878 0.34989 -0.03986 0.00748  0.00772  74   ILE B CG2 
1767 C CD1 . ILE B 42  ? 0.29112 0.39757 0.37957 -0.03215 0.00540  0.00277  74   ILE B CD1 
1768 N N   . ALA B 43  ? 0.24022 0.34030 0.32239 -0.06040 0.01034  0.00482  75   ALA B N   
1769 C CA  . ALA B 43  ? 0.24881 0.35078 0.33187 -0.06839 0.01507  0.00965  75   ALA B CA  
1770 C C   . ALA B 43  ? 0.28843 0.37113 0.36613 -0.07795 0.01467  0.01115  75   ALA B C   
1771 O O   . ALA B 43  ? 0.30397 0.37428 0.37430 -0.08169 0.01903  0.01755  75   ALA B O   
1772 C CB  . ALA B 43  ? 0.26446 0.39123 0.36235 -0.07221 0.01740  0.00891  75   ALA B CB  
1773 N N   . GLY B 44  ? 0.28944 0.36569 0.36721 -0.08189 0.00906  0.00528  76   GLY B N   
1774 C CA  . GLY B 44  ? 0.33562 0.38711 0.40431 -0.09155 0.00741  0.00455  76   GLY B CA  
1775 C C   . GLY B 44  ? 0.30045 0.32300 0.35214 -0.08322 0.01041  0.00726  76   GLY B C   
1776 O O   . GLY B 44  ? 0.32523 0.32624 0.36862 -0.08914 0.01303  0.01177  76   GLY B O   
1777 N N   . GLU B 45  ? 0.29178 0.31400 0.33976 -0.06905 0.01051  0.00564  77   GLU B N   
1778 C CA  . GLU B 45  ? 0.29933 0.30055 0.33689 -0.05856 0.01370  0.00971  77   GLU B CA  
1779 C C   . GLU B 45  ? 0.30612 0.31037 0.34440 -0.05659 0.01604  0.01923  77   GLU B C   
1780 O O   . GLU B 45  ? 0.33723 0.31887 0.36513 -0.05426 0.01805  0.02509  77   GLU B O   
1781 C CB  . GLU B 45  ? 0.29455 0.30190 0.33423 -0.04461 0.01442  0.00765  77   GLU B CB  
1782 C CG  . GLU B 45  ? 0.32819 0.32253 0.35765 -0.04210 0.01451  -0.00034 77   GLU B CG  
1783 C CD  . GLU B 45  ? 0.40400 0.36254 0.41482 -0.04020 0.01719  -0.00249 77   GLU B CD  
1784 O OE1 . GLU B 45  ? 0.38854 0.33263 0.39669 -0.03806 0.01964  0.00384  77   GLU B OE1 
1785 O OE2 . GLU B 45  ? 0.39989 0.34165 0.39541 -0.03901 0.01708  -0.01054 77   GLU B OE2 
1786 N N   . ALA B 46  ? 0.30361 0.33236 0.35055 -0.05660 0.01559  0.02087  78   ALA B N   
1787 C CA  . ALA B 46  ? 0.30410 0.33377 0.34558 -0.05478 0.01700  0.02919  78   ALA B CA  
1788 C C   . ALA B 46  ? 0.34613 0.36200 0.37962 -0.06566 0.02177  0.03522  78   ALA B C   
1789 O O   . ALA B 46  ? 0.34819 0.34863 0.36925 -0.06290 0.02331  0.04406  78   ALA B O   
1790 C CB  . ALA B 46  ? 0.27798 0.33200 0.32518 -0.05335 0.01617  0.02758  78   ALA B CB  
1791 N N   . SER B 47  ? 0.30562 0.32740 0.34703 -0.07860 0.02373  0.03169  79   SER B N   
1792 C CA  . SER B 47  ? 0.33846 0.34895 0.37657 -0.09215 0.02907  0.03826  79   SER B CA  
1793 C C   . SER B 47  ? 0.36279 0.33554 0.38643 -0.09345 0.02842  0.04105  79   SER B C   
1794 O O   . SER B 47  ? 0.40897 0.36241 0.42079 -0.09680 0.03309  0.05106  79   SER B O   
1795 C CB  . SER B 47  ? 0.33033 0.36032 0.38640 -0.10654 0.02933  0.03377  79   SER B CB  
1796 O OG  . SER B 47  ? 0.38316 0.40378 0.44032 -0.12250 0.03479  0.04088  79   SER B OG  
1797 N N   . ARG B 48  ? 0.35031 0.30922 0.37148 -0.08917 0.02351  0.03263  80   ARG B N   
1798 C CA  . ARG B 48  ? 0.37094 0.28954 0.37518 -0.08690 0.02385  0.03381  80   ARG B CA  
1799 C C   . ARG B 48  ? 0.37608 0.28272 0.37003 -0.07091 0.02595  0.04366  80   ARG B C   
1800 O O   . ARG B 48  ? 0.42618 0.30181 0.40564 -0.07130 0.02873  0.05172  80   ARG B O   
1801 C CB  . ARG B 48  ? 0.38073 0.28810 0.38054 -0.08115 0.01984  0.02201  80   ARG B CB  
1802 C CG  . ARG B 48  ? 0.43420 0.29643 0.41320 -0.07423 0.02173  0.02152  80   ARG B CG  
1803 C CD  . ARG B 48  ? 0.43107 0.28323 0.40170 -0.06347 0.02071  0.01035  80   ARG B CD  
1804 N NE  . ARG B 48  ? 0.41008 0.28913 0.39182 -0.04586 0.02265  0.01154  80   ARG B NE  
1805 C CZ  . ARG B 48  ? 0.38252 0.25440 0.36276 -0.02706 0.02716  0.01695  80   ARG B CZ  
1806 N NH1 . ARG B 48  ? 0.42592 0.26392 0.39246 -0.02048 0.03043  0.02243  80   ARG B NH1 
1807 N NH2 . ARG B 48  ? 0.37372 0.27376 0.36847 -0.01467 0.02827  0.01788  80   ARG B NH2 
1808 N N   . LEU B 49  ? 0.37114 0.30193 0.37293 -0.05721 0.02355  0.04378  81   LEU B N   
1809 C CA  . LEU B 49  ? 0.41728 0.34272 0.41342 -0.04161 0.02224  0.05296  81   LEU B CA  
1810 C C   . LEU B 49  ? 0.40871 0.32903 0.39340 -0.04578 0.02389  0.06497  81   LEU B C   
1811 O O   . LEU B 49  ? 0.44065 0.34067 0.41284 -0.03633 0.02312  0.07513  81   LEU B O   
1812 C CB  . LEU B 49  ? 0.34624 0.30234 0.35672 -0.03055 0.01761  0.05012  81   LEU B CB  
1813 C CG  . LEU B 49  ? 0.34765 0.30498 0.36642 -0.02259 0.01823  0.04178  81   LEU B CG  
1814 C CD1 . LEU B 49  ? 0.37509 0.36512 0.41060 -0.01865 0.01493  0.03797  81   LEU B CD1 
1815 C CD2 . LEU B 49  ? 0.40352 0.33893 0.41715 -0.00690 0.02016  0.04705  81   LEU B CD2 
1816 N N   . ALA B 50  ? 0.37599 0.31517 0.36385 -0.05812 0.02680  0.06476  82   ALA B N   
1817 C CA  . ALA B 50  ? 0.46020 0.39614 0.43390 -0.06176 0.03083  0.07633  82   ALA B CA  
1818 C C   . ALA B 50  ? 0.46407 0.36349 0.42220 -0.06882 0.03634  0.08639  82   ALA B C   
1819 O O   . ALA B 50  ? 0.49800 0.38507 0.43811 -0.06693 0.03906  0.09920  82   ALA B O   
1820 C CB  . ALA B 50  ? 0.46145 0.42490 0.44305 -0.07278 0.03629  0.07332  82   ALA B CB  
1821 N N   . HIS B 51  ? 0.45637 0.33534 0.41813 -0.07797 0.03776  0.08097  83   HIS B N   
1822 C CA  . HIS B 51  ? 0.53790 0.37642 0.48372 -0.08663 0.04271  0.09013  83   HIS B CA  
1823 C C   . HIS B 51  ? 0.55358 0.36116 0.48034 -0.06835 0.04034  0.10001  83   HIS B C   
1824 O O   . HIS B 51  ? 0.62095 0.39368 0.52948 -0.07222 0.04482  0.11189  83   HIS B O   
1825 C CB  . HIS B 51  ? 0.53298 0.35236 0.48410 -0.10075 0.04212  0.08004  83   HIS B CB  
1826 C CG  . HIS B 51  ? 0.55961 0.40398 0.52893 -0.12282 0.04463  0.07585  83   HIS B CG  
1827 N ND1 . HIS B 51  ? 0.61049 0.44459 0.57986 -0.14322 0.05181  0.08497  83   HIS B ND1 
1828 C CD2 . HIS B 51  ? 0.53249 0.41415 0.52295 -0.12694 0.04117  0.06498  83   HIS B CD2 
1829 C CE1 . HIS B 51  ? 0.56317 0.43114 0.55648 -0.15881 0.05248  0.07962  83   HIS B CE1 
1830 N NE2 . HIS B 51  ? 0.52254 0.41859 0.52781 -0.14835 0.04550  0.06739  83   HIS B NE2 
1831 N N   . TYR B 52  ? 0.57908 0.39712 0.51154 -0.04853 0.03362  0.09576  84   TYR B N   
1832 C CA  . TYR B 52  ? 0.59606 0.39193 0.51636 -0.02825 0.03032  0.10589  84   TYR B CA  
1833 C C   . TYR B 52  ? 0.70649 0.51214 0.61514 -0.02152 0.02686  0.12012  84   TYR B C   
1834 O O   . TYR B 52  ? 0.70986 0.49399 0.60506 -0.00636 0.02348  0.13221  84   TYR B O   
1835 C CB  . TYR B 52  ? 0.59609 0.40710 0.53210 -0.00994 0.02529  0.09759  84   TYR B CB  
1836 C CG  . TYR B 52  ? 0.60934 0.39772 0.54589 -0.01089 0.02938  0.08573  84   TYR B CG  
1837 C CD1 . TYR B 52  ? 0.70277 0.44289 0.62129 -0.00471 0.03330  0.08903  84   TYR B CD1 
1838 C CD2 . TYR B 52  ? 0.54869 0.35922 0.49900 -0.01894 0.02924  0.07109  84   TYR B CD2 
1839 C CE1 . TYR B 52  ? 0.67451 0.38867 0.58719 -0.00558 0.03677  0.07644  84   TYR B CE1 
1840 C CE2 . TYR B 52  ? 0.58714 0.37399 0.53169 -0.02009 0.03201  0.05954  84   TYR B CE2 
1841 C CZ  . TYR B 52  ? 0.64911 0.38728 0.57376 -0.01365 0.03575  0.06155  84   TYR B CZ  
1842 O OH  . TYR B 52  ? 0.67706 0.38670 0.58996 -0.01452 0.03819  0.04855  84   TYR B OH  
1843 N N   . ASN B 53  ? 0.66840 0.50426 0.57957 -0.03089 0.02728  0.11893  85   ASN B N   
1844 C CA  . ASN B 53  ? 0.69683 0.53977 0.59053 -0.02506 0.02365  0.13074  85   ASN B CA  
1845 C C   . ASN B 53  ? 0.73126 0.55046 0.60178 -0.03822 0.03433  0.14339  85   ASN B C   
1846 O O   . ASN B 53  ? 0.71270 0.52074 0.58799 -0.05573 0.04437  0.14117  85   ASN B O   
1847 C CB  . ASN B 53  ? 0.60827 0.49207 0.51241 -0.02656 0.01939  0.12166  85   ASN B CB  
1848 C CG  . ASN B 53  ? 0.67898 0.58584 0.60742 -0.01621 0.01018  0.11053  85   ASN B CG  
1849 O OD1 . ASN B 53  ? 0.66878 0.56578 0.60401 -0.00278 0.00537  0.11279  85   ASN B OD1 
1850 N ND2 . ASN B 53  ? 0.61189 0.54866 0.55439 -0.02195 0.00937  0.09901  85   ASN B ND2 
1851 N N   . LYS B 54  ? 0.86725 0.67938 0.71217 -0.03037 0.03164  0.15753  86   LYS B N   
1852 C CA  . LYS B 54  ? 1.00581 0.79469 0.82513 -0.04198 0.04375  0.17211  86   LYS B CA  
1853 C C   . LYS B 54  ? 0.95390 0.76962 0.77717 -0.05839 0.05536  0.16744  86   LYS B C   
1854 O O   . LYS B 54  ? 0.93099 0.73378 0.74762 -0.07450 0.06996  0.17582  86   LYS B O   
1855 C CB  . LYS B 54  ? 1.06618 0.83755 0.85165 -0.02719 0.03723  0.18965  86   LYS B CB  
1856 C CG  . LYS B 54  ? 1.21183 0.95516 0.99339 -0.00872 0.02699  0.19785  86   LYS B CG  
1857 C CD  . LYS B 54  ? 1.47644 1.17758 1.25780 -0.01741 0.03750  0.20164  86   LYS B CD  
1858 C CE  . LYS B 54  ? 1.55208 1.22356 1.33229 0.00355  0.02938  0.20694  86   LYS B CE  
1859 N NZ  . LYS B 54  ? 1.44416 1.06873 1.18974 0.00975  0.03195  0.22934  86   LYS B NZ  
1860 N N   . ARG B 55  ? 0.86819 0.72076 0.70379 -0.05467 0.05011  0.15473  87   ARG B N   
1861 C CA  . ARG B 55  ? 0.87723 0.75603 0.71629 -0.06585 0.06152  0.14985  87   ARG B CA  
1862 C C   . ARG B 55  ? 0.75923 0.66321 0.63512 -0.07514 0.06299  0.13349  87   ARG B C   
1863 O O   . ARG B 55  ? 0.78531 0.69984 0.67882 -0.06722 0.05141  0.12185  87   ARG B O   
1864 C CB  . ARG B 55  ? 0.95174 0.84857 0.77140 -0.05458 0.05526  0.14744  87   ARG B CB  
1865 C CG  . ARG B 55  ? 1.19481 1.06816 0.97200 -0.04650 0.05393  0.16414  87   ARG B CG  
1866 C CD  . ARG B 55  ? 1.48590 1.37375 1.24161 -0.03477 0.04229  0.15913  87   ARG B CD  
1867 N NE  . ARG B 55  ? 1.62396 1.48790 1.33621 -0.02527 0.03648  0.17511  87   ARG B NE  
1868 C CZ  . ARG B 55  ? 1.61400 1.48176 1.30402 -0.01277 0.01835  0.17375  87   ARG B CZ  
1869 N NH1 . ARG B 55  ? 1.59363 1.48680 1.30206 -0.00926 0.00472  0.15728  87   ARG B NH1 
1870 N NH2 . ARG B 55  ? 1.66175 1.50601 1.30921 -0.00440 0.01271  0.18981  87   ARG B NH2 
1871 N N   . SER B 56  ? 0.66223 0.57625 0.55043 -0.09198 0.07730  0.13401  88   SER B N   
1872 C CA  . SER B 56  ? 0.59073 0.53116 0.51347 -0.10124 0.07787  0.11992  88   SER B CA  
1873 C C   . SER B 56  ? 0.54236 0.51651 0.47042 -0.09272 0.07645  0.10960  88   SER B C   
1874 O O   . SER B 56  ? 0.54895 0.54522 0.48259 -0.09817 0.08840  0.10938  88   SER B O   
1875 C CB  . SER B 56  ? 0.59571 0.53916 0.53365 -0.12245 0.09189  0.12537  88   SER B CB  
1876 O OG  . SER B 56  ? 0.59096 0.56489 0.56250 -0.13033 0.09064  0.11253  88   SER B OG  
1877 N N   . THR B 57  ? 0.52168 0.49843 0.44757 -0.07849 0.06221  0.10169  89   THR B N   
1878 C CA  . THR B 57  ? 0.47294 0.47373 0.39958 -0.06997 0.05829  0.09170  89   THR B CA  
1879 C C   . THR B 57  ? 0.42237 0.43383 0.37091 -0.06423 0.04557  0.07902  89   THR B C   
1880 O O   . THR B 57  ? 0.45304 0.45065 0.40231 -0.05812 0.03592  0.08023  89   THR B O   
1881 C CB  . THR B 57  ? 0.47430 0.46542 0.36759 -0.05866 0.05280  0.09730  89   THR B CB  
1882 O OG1 . THR B 57  ? 0.61580 0.59181 0.48321 -0.06304 0.06539  0.11139  89   THR B OG1 
1883 C CG2 . THR B 57  ? 0.50357 0.51465 0.39351 -0.05229 0.05005  0.08586  89   THR B CG2 
1884 N N   . ILE B 58  ? 0.34541 0.38075 0.31114 -0.06485 0.04657  0.06802  90   ILE B N   
1885 C CA  . ILE B 58  ? 0.32366 0.36851 0.30500 -0.05828 0.03530  0.05731  90   ILE B CA  
1886 C C   . ILE B 58  ? 0.39653 0.44343 0.36163 -0.04831 0.02697  0.05516  90   ILE B C   
1887 O O   . ILE B 58  ? 0.43898 0.49472 0.39437 -0.04703 0.03146  0.05131  90   ILE B O   
1888 C CB  . ILE B 58  ? 0.37969 0.44631 0.38402 -0.06243 0.03872  0.04753  90   ILE B CB  
1889 C CG1 . ILE B 58  ? 0.52450 0.59291 0.54553 -0.07483 0.04488  0.04894  90   ILE B CG1 
1890 C CG2 . ILE B 58  ? 0.36141 0.43398 0.37838 -0.05565 0.02799  0.03839  90   ILE B CG2 
1891 C CD1 . ILE B 58  ? 0.41873 0.46723 0.44185 -0.07751 0.03922  0.04974  90   ILE B CD1 
1892 N N   . THR B 59  ? 0.37577 0.41558 0.33948 -0.04108 0.01446  0.05674  91   THR B N   
1893 C CA  . THR B 59  ? 0.32914 0.37316 0.28208 -0.03415 0.00281  0.05367  91   THR B CA  
1894 C C   . THR B 59  ? 0.34807 0.40474 0.32534 -0.03166 -0.00601 0.04542  91   THR B C   
1895 O O   . THR B 59  ? 0.35593 0.41619 0.35414 -0.03323 -0.00274 0.04291  91   THR B O   
1896 C CB  . THR B 59  ? 0.42092 0.45148 0.35453 -0.02785 -0.00696 0.06410  91   THR B CB  
1897 O OG1 . THR B 59  ? 0.45510 0.48460 0.40802 -0.02270 -0.01428 0.06751  91   THR B OG1 
1898 C CG2 . THR B 59  ? 0.46927 0.48230 0.37872 -0.03047 0.00331  0.07550  91   THR B CG2 
1899 N N   . SER B 60  ? 0.35165 0.41349 0.32431 -0.02848 -0.01759 0.04143  92   SER B N   
1900 C CA  A SER B 60  ? 0.33302 0.40694 0.33032 -0.02764 -0.02506 0.03565  92   SER B CA  
1901 C CA  B SER B 60  ? 0.33021 0.40406 0.32691 -0.02748 -0.02574 0.03581  92   SER B CA  
1902 C C   . SER B 60  ? 0.32226 0.39781 0.33837 -0.02292 -0.02863 0.04236  92   SER B C   
1903 O O   . SER B 60  ? 0.31942 0.40465 0.35840 -0.02229 -0.02849 0.03896  92   SER B O   
1904 C CB  A SER B 60  ? 0.37753 0.45509 0.36791 -0.02767 -0.03865 0.03073  92   SER B CB  
1905 C CB  B SER B 60  ? 0.37671 0.45347 0.36507 -0.02710 -0.04022 0.03209  92   SER B CB  
1906 O OG  A SER B 60  ? 0.41156 0.48469 0.38717 -0.02429 -0.05109 0.03788  92   SER B OG  
1907 O OG  B SER B 60  ? 0.38702 0.45834 0.35512 -0.02946 -0.03655 0.02393  92   SER B OG  
1908 N N   . ARG B 61  ? 0.34122 0.40594 0.34675 -0.01828 -0.03047 0.05242  93   ARG B N   
1909 C CA  . ARG B 61  ? 0.35343 0.41781 0.37638 -0.01072 -0.03223 0.05876  93   ARG B CA  
1910 C C   . ARG B 61  ? 0.31495 0.37234 0.34807 -0.01264 -0.01946 0.05530  93   ARG B C   
1911 O O   . ARG B 61  ? 0.32085 0.38403 0.37326 -0.00782 -0.01827 0.05382  93   ARG B O   
1912 C CB  . ARG B 61  ? 0.42781 0.47891 0.43490 -0.00333 -0.03772 0.07117  93   ARG B CB  
1913 C CG  . ARG B 61  ? 0.55446 0.60495 0.58023 0.00790  -0.03904 0.07807  93   ARG B CG  
1914 C CD  . ARG B 61  ? 0.86805 0.90681 0.88107 0.01853  -0.04688 0.09185  93   ARG B CD  
1915 N NE  . ARG B 61  ? 1.03556 1.04402 1.02865 0.01960  -0.03657 0.09873  93   ARG B NE  
1916 C CZ  . ARG B 61  ? 1.05806 1.04889 1.03382 0.02847  -0.04113 0.11204  93   ARG B CZ  
1917 N NH1 . ARG B 61  ? 1.05009 1.05321 1.02713 0.03855  -0.05725 0.12013  93   ARG B NH1 
1918 N NH2 . ARG B 61  ? 1.07158 1.03109 1.02889 0.02683  -0.03026 0.11796  93   ARG B NH2 
1919 N N   . GLU B 62  ? 0.31330 0.35923 0.33359 -0.02023 -0.00987 0.05379  94   GLU B N   
1920 C CA  . GLU B 62  ? 0.29618 0.33522 0.32467 -0.02425 -0.00097 0.04925  94   GLU B CA  
1921 C C   . GLU B 62  ? 0.30176 0.35722 0.34546 -0.02717 -0.00003 0.03916  94   GLU B C   
1922 O O   . GLU B 62  ? 0.30328 0.35603 0.35594 -0.02605 0.00327  0.03534  94   GLU B O   
1923 C CB  . GLU B 62  ? 0.33380 0.35986 0.34929 -0.03403 0.00738  0.05125  94   GLU B CB  
1924 C CG  . GLU B 62  ? 0.37687 0.37866 0.37575 -0.03191 0.00878  0.06263  94   GLU B CG  
1925 C CD  . GLU B 62  ? 0.48629 0.48870 0.46843 -0.02677 0.00296  0.07092  94   GLU B CD  
1926 O OE1 . GLU B 62  ? 0.43694 0.45043 0.41031 -0.03125 0.00405  0.06858  94   GLU B OE1 
1927 O OE2 . GLU B 62  ? 0.51183 0.50408 0.48884 -0.01667 -0.00353 0.07935  94   GLU B OE2 
1928 N N   . ILE B 63  ? 0.28287 0.35196 0.32608 -0.03008 -0.00258 0.03477  95   ILE B N   
1929 C CA  . ILE B 63  ? 0.28126 0.36290 0.33773 -0.03129 -0.00234 0.02676  95   ILE B CA  
1930 C C   . ILE B 63  ? 0.24579 0.33341 0.31756 -0.02521 -0.00651 0.02757  95   ILE B C   
1931 O O   . ILE B 63  ? 0.25682 0.34651 0.33813 -0.02438 -0.00251 0.02412  95   ILE B O   
1932 C CB  . ILE B 63  ? 0.26820 0.35820 0.31881 -0.03360 -0.00437 0.02205  95   ILE B CB  
1933 C CG1 . ILE B 63  ? 0.29734 0.38570 0.33573 -0.03802 0.00325  0.02189  95   ILE B CG1 
1934 C CG2 . ILE B 63  ? 0.28399 0.38295 0.34736 -0.03378 -0.00437 0.01511  95   ILE B CG2 
1935 C CD1 . ILE B 63  ? 0.27459 0.36667 0.32313 -0.04311 0.01060  0.01954  95   ILE B CD1 
1936 N N   . GLN B 64  ? 0.26043 0.35254 0.33502 -0.02090 -0.01465 0.03285  96   GLN B N   
1937 C CA  . GLN B 64  ? 0.28217 0.38602 0.37747 -0.01560 -0.01809 0.03545  96   GLN B CA  
1938 C C   . GLN B 64  ? 0.29887 0.39576 0.40077 -0.00815 -0.01000 0.03840  96   GLN B C   
1939 O O   . GLN B 64  ? 0.24061 0.34438 0.35627 -0.00535 -0.00493 0.03688  96   GLN B O   
1940 C CB  . GLN B 64  ? 0.27759 0.39010 0.37682 -0.01268 -0.03066 0.04182  96   GLN B CB  
1941 C CG  . GLN B 64  ? 0.26985 0.39980 0.39735 -0.00649 -0.03379 0.04737  96   GLN B CG  
1942 C CD  . GLN B 64  ? 0.28988 0.43509 0.42644 -0.00773 -0.05029 0.05176  96   GLN B CD  
1943 O OE1 . GLN B 64  ? 0.30682 0.45534 0.43932 -0.01683 -0.05842 0.04616  96   GLN B OE1 
1944 N NE2 . GLN B 64  ? 0.37548 0.52912 0.52414 0.00187  -0.05631 0.06170  96   GLN B NE2 
1945 N N   . THR B 65  ? 0.26555 0.34547 0.35484 -0.00451 -0.00761 0.04273  97   THR B N   
1946 C CA  . THR B 65  ? 0.26662 0.33295 0.35701 0.00356  0.00052  0.04402  97   THR B CA  
1947 C C   . THR B 65  ? 0.27324 0.33175 0.35820 -0.00165 0.00844  0.03516  97   THR B C   
1948 O O   . THR B 65  ? 0.26922 0.32558 0.35911 0.00499  0.01493  0.03334  97   THR B O   
1949 C CB  . THR B 65  ? 0.30554 0.34890 0.37988 0.00717  0.00108  0.05027  97   THR B CB  
1950 O OG1 . THR B 65  ? 0.33659 0.38883 0.41525 0.01388  -0.00818 0.05956  97   THR B OG1 
1951 C CG2 . THR B 65  ? 0.35228 0.37526 0.42420 0.01722  0.00968  0.05055  97   THR B CG2 
1952 N N   . ALA B 66  ? 0.27536 0.33156 0.35036 -0.01271 0.00794  0.02998  98   ALA B N   
1953 C CA  . ALA B 66  ? 0.25503 0.30740 0.32610 -0.01817 0.01206  0.02204  98   ALA B CA  
1954 C C   . ALA B 66  ? 0.24551 0.31286 0.32775 -0.01538 0.01300  0.01913  98   ALA B C   
1955 O O   . ALA B 66  ? 0.28558 0.34652 0.36374 -0.01319 0.01776  0.01517  98   ALA B O   
1956 C CB  . ALA B 66  ? 0.27126 0.32644 0.33668 -0.02951 0.01058  0.01892  98   ALA B CB  
1957 N N   . VAL B 67  ? 0.24462 0.32916 0.33801 -0.01621 0.00833  0.02104  99   VAL B N   
1958 C CA  . VAL B 67  ? 0.25210 0.34869 0.35684 -0.01522 0.00950  0.01993  99   VAL B CA  
1959 C C   . VAL B 67  ? 0.22715 0.32579 0.34229 -0.00611 0.01582  0.02433  99   VAL B C   
1960 O O   . VAL B 67  ? 0.25935 0.35890 0.37560 -0.00407 0.02231  0.02304  99   VAL B O   
1961 C CB  . VAL B 67  ? 0.22395 0.33360 0.33692 -0.01949 0.00182  0.02084  99   VAL B CB  
1962 C CG1 . VAL B 67  ? 0.28085 0.40182 0.40978 -0.01935 0.00249  0.02261  99   VAL B CG1 
1963 C CG2 . VAL B 67  ? 0.25568 0.36292 0.35712 -0.02574 -0.00018 0.01522  99   VAL B CG2 
1964 N N   . ARG B 68  ? 0.21024 0.31064 0.33325 0.00080  0.01476  0.03066  100  ARG B N   
1965 C CA  . ARG B 68  ? 0.23164 0.33710 0.36802 0.01213  0.02272  0.03588  100  ARG B CA  
1966 C C   . ARG B 68  ? 0.24097 0.32418 0.35902 0.01871  0.03371  0.03142  100  ARG B C   
1967 O O   . ARG B 68  ? 0.26952 0.35517 0.39233 0.02705  0.04417  0.03282  100  ARG B O   
1968 C CB  . ARG B 68  ? 0.24430 0.35751 0.39410 0.02006  0.01767  0.04445  100  ARG B CB  
1969 C CG  . ARG B 68  ? 0.25664 0.39401 0.42572 0.01351  0.00514  0.04859  100  ARG B CG  
1970 C CD  . ARG B 68  ? 0.33112 0.47847 0.51249 0.02092  -0.00409 0.05773  100  ARG B CD  
1971 N NE  . ARG B 68  ? 0.44688 0.61280 0.65649 0.03325  0.00168  0.06603  100  ARG B NE  
1972 C CZ  . ARG B 68  ? 0.48218 0.66044 0.70823 0.04385  -0.00479 0.07573  100  ARG B CZ  
1973 N NH1 . ARG B 68  ? 0.46932 0.64053 0.68256 0.04330  -0.01825 0.07870  100  ARG B NH1 
1974 N NH2 . ARG B 68  ? 0.47427 0.67346 0.73037 0.05633  0.00290  0.08365  100  ARG B NH2 
1975 N N   . LEU B 69  ? 0.26762 0.32821 0.36360 0.01433  0.03177  0.02597  101  LEU B N   
1976 C CA  . LEU B 69  ? 0.28123 0.31640 0.35563 0.01805  0.03946  0.01963  101  LEU B CA  
1977 C C   . LEU B 69  ? 0.29224 0.32880 0.35772 0.01295  0.04137  0.01327  101  LEU B C   
1978 O O   . LEU B 69  ? 0.32087 0.34641 0.37442 0.02055  0.05043  0.01063  101  LEU B O   
1979 C CB  . LEU B 69  ? 0.30052 0.31116 0.35588 0.01101  0.03503  0.01576  101  LEU B CB  
1980 C CG  . LEU B 69  ? 0.28694 0.28400 0.34124 0.01730  0.03457  0.02220  101  LEU B CG  
1981 C CD1 . LEU B 69  ? 0.35282 0.32949 0.39079 0.00496  0.02983  0.01963  101  LEU B CD1 
1982 C CD2 . LEU B 69  ? 0.29934 0.27626 0.34628 0.03367  0.04477  0.02268  101  LEU B CD2 
1983 N N   . LEU B 70  ? 0.26175 0.31032 0.33056 0.00171  0.03339  0.01116  102  LEU B N   
1984 C CA  A LEU B 70  ? 0.28182 0.32886 0.33917 -0.00372 0.03195  0.00522  102  LEU B CA  
1985 C CA  B LEU B 70  ? 0.29208 0.33908 0.34941 -0.00367 0.03199  0.00524  102  LEU B CA  
1986 C C   . LEU B 70  ? 0.26267 0.32345 0.32834 -0.00028 0.03668  0.00855  102  LEU B C   
1987 O O   . LEU B 70  ? 0.30349 0.35604 0.35367 0.00183  0.04048  0.00563  102  LEU B O   
1988 C CB  A LEU B 70  ? 0.36238 0.41704 0.42168 -0.01513 0.02243  0.00249  102  LEU B CB  
1989 C CB  B LEU B 70  ? 0.30215 0.35669 0.36139 -0.01506 0.02249  0.00250  102  LEU B CB  
1990 C CG  A LEU B 70  ? 0.29230 0.35100 0.34505 -0.01921 0.01882  -0.00188 102  LEU B CG  
1991 C CG  B LEU B 70  ? 0.30230 0.34299 0.35034 -0.02292 0.01812  -0.00184 102  LEU B CG  
1992 C CD1 A LEU B 70  ? 0.35215 0.39163 0.38343 -0.02058 0.01766  -0.00843 102  LEU B CD1 
1993 C CD1 B LEU B 70  ? 0.30236 0.35652 0.36125 -0.03033 0.01340  0.00060  102  LEU B CD1 
1994 C CD2 A LEU B 70  ? 0.36203 0.43503 0.42396 -0.02680 0.01183  -0.00258 102  LEU B CD2 
1995 C CD2 B LEU B 70  ? 0.34509 0.37940 0.37953 -0.02792 0.01414  -0.00885 102  LEU B CD2 
1996 N N   . LEU B 71  ? 0.26063 0.34048 0.34852 -0.00085 0.03561  0.01480  103  LEU B N   
1997 C CA  . LEU B 71  ? 0.27341 0.36440 0.37021 -0.00096 0.03949  0.01863  103  LEU B CA  
1998 C C   . LEU B 71  ? 0.26303 0.35694 0.36651 0.00862  0.05259  0.02454  103  LEU B C   
1999 O O   . LEU B 71  ? 0.31548 0.41823 0.43584 0.01412  0.05521  0.02953  103  LEU B O   
2000 C CB  . LEU B 71  ? 0.24814 0.35531 0.36466 -0.00794 0.03168  0.02181  103  LEU B CB  
2001 C CG  . LEU B 71  ? 0.27110 0.37584 0.37922 -0.01486 0.02401  0.01678  103  LEU B CG  
2002 C CD1 . LEU B 71  ? 0.26555 0.36334 0.36155 -0.01725 0.01895  0.01108  103  LEU B CD1 
2003 C CD2 . LEU B 71  ? 0.29982 0.41408 0.42174 -0.02070 0.01731  0.01844  103  LEU B CD2 
2004 N N   . PRO B 72  ? 0.31188 0.40085 0.40411 0.01172  0.06163  0.02559  104  PRO B N   
2005 C CA  . PRO B 72  ? 0.33767 0.42936 0.43434 0.02246  0.07778  0.03165  104  PRO B CA  
2006 C C   . PRO B 72  ? 0.33556 0.45355 0.46703 0.02007  0.08208  0.04245  104  PRO B C   
2007 O O   . PRO B 72  ? 0.31864 0.44453 0.45978 0.00990  0.07602  0.04484  104  PRO B O   
2008 C CB  . PRO B 72  ? 0.34202 0.41644 0.40806 0.02561  0.08547  0.02902  104  PRO B CB  
2009 C CG  . PRO B 72  ? 0.37996 0.44101 0.42506 0.01828  0.07146  0.02016  104  PRO B CG  
2010 C CD  . PRO B 72  ? 0.31534 0.39066 0.38240 0.00854  0.05818  0.02005  104  PRO B CD  
2011 N N   . GLY B 73  ? 0.34202 0.47282 0.49271 0.02983  0.09303  0.04922  105  GLY B N   
2012 C CA  . GLY B 73  ? 0.35702 0.51597 0.54368 0.02794  0.10031  0.06104  105  GLY B CA  
2013 C C   . GLY B 73  ? 0.36295 0.53984 0.57629 0.01350  0.08350  0.06334  105  GLY B C   
2014 O O   . GLY B 73  ? 0.32062 0.49737 0.53572 0.01075  0.06881  0.05901  105  GLY B O   
2015 N N   . GLU B 74  ? 0.31497 0.50468 0.54659 0.00377  0.08595  0.07037  106  GLU B N   
2016 C CA  . GLU B 74  ? 0.26695 0.47091 0.52302 -0.01098 0.06996  0.07208  106  GLU B CA  
2017 C C   . GLU B 74  ? 0.25025 0.43383 0.48209 -0.01942 0.05428  0.06167  106  GLU B C   
2018 O O   . GLU B 74  ? 0.29185 0.48160 0.53625 -0.02986 0.03956  0.06031  106  GLU B O   
2019 C CB  . GLU B 74  ? 0.26155 0.48081 0.54331 -0.02091 0.07754  0.08268  106  GLU B CB  
2020 C CG  . GLU B 74  ? 0.29897 0.53890 0.60423 -0.01423 0.08773  0.09072  106  GLU B CG  
2021 C CD  . GLU B 74  ? 0.35921 0.60844 0.68309 -0.02682 0.09008  0.09799  106  GLU B CD  
2022 O OE1 . GLU B 74  ? 0.37573 0.61694 0.68896 -0.02541 0.10691  0.10338  106  GLU B OE1 
2023 O OE2 . GLU B 74  ? 0.47963 0.74278 0.82695 -0.03860 0.07502  0.09846  106  GLU B OE2 
2024 N N   . LEU B 75  ? 0.24393 0.40429 0.44180 -0.01503 0.05676  0.05435  107  LEU B N   
2025 C CA  . LEU B 75  ? 0.23126 0.37719 0.41042 -0.02046 0.04321  0.04512  107  LEU B CA  
2026 C C   . LEU B 75  ? 0.25712 0.40784 0.44037 -0.02047 0.03173  0.04108  107  LEU B C   
2027 O O   . LEU B 75  ? 0.26428 0.41316 0.44630 -0.02782 0.01957  0.03695  107  LEU B O   
2028 C CB  . LEU B 75  ? 0.28848 0.41463 0.43568 -0.01495 0.04637  0.03874  107  LEU B CB  
2029 C CG  . LEU B 75  ? 0.29478 0.41059 0.42853 -0.01505 0.05356  0.04184  107  LEU B CG  
2030 C CD1 . LEU B 75  ? 0.27100 0.37025 0.37348 -0.00866 0.05357  0.03526  107  LEU B CD1 
2031 C CD2 . LEU B 75  ? 0.27003 0.38229 0.40855 -0.02429 0.04513  0.04201  107  LEU B CD2 
2032 N N   . ALA B 76  ? 0.24164 0.39571 0.42689 -0.01120 0.03623  0.04260  108  ALA B N   
2033 C CA  . ALA B 76  ? 0.25281 0.40813 0.43844 -0.01014 0.02596  0.04056  108  ALA B CA  
2034 C C   . ALA B 76  ? 0.23045 0.40516 0.44154 -0.01638 0.01479  0.04554  108  ALA B C   
2035 O O   . ALA B 76  ? 0.27311 0.44467 0.47709 -0.02149 0.00182  0.04175  108  ALA B O   
2036 C CB  . ALA B 76  ? 0.25957 0.41024 0.44128 0.00236  0.03372  0.04225  108  ALA B CB  
2037 N N   . LYS B 77  ? 0.22622 0.42154 0.46655 -0.01668 0.01946  0.05418  109  LYS B N   
2038 C CA  . LYS B 77  ? 0.23897 0.45603 0.50769 -0.02467 0.00633  0.05934  109  LYS B CA  
2039 C C   . LYS B 77  ? 0.26990 0.47681 0.52867 -0.03921 -0.00717 0.05275  109  LYS B C   
2040 O O   . LYS B 77  ? 0.25007 0.45864 0.50749 -0.04441 -0.02337 0.05012  109  LYS B O   
2041 C CB  . LYS B 77  ? 0.24983 0.49329 0.55573 -0.02504 0.01574  0.07053  109  LYS B CB  
2042 C CG  . LYS B 77  ? 0.27609 0.53649 0.60502 -0.03630 0.00027  0.07303  109  LYS B CG  
2043 C CD  . LYS B 77  ? 0.38451 0.66325 0.73898 -0.03580 0.01114  0.08117  109  LYS B CD  
2044 C CE  . LYS B 77  ? 0.40613 0.67429 0.75469 -0.04243 0.02516  0.08237  109  LYS B CE  
2045 N NZ  . LYS B 77  ? 0.45847 0.74550 0.83303 -0.04489 0.03484  0.09118  109  LYS B NZ  
2046 N N   . HIS B 78  ? 0.23261 0.42640 0.48146 -0.04479 -0.00064 0.05013  110  HIS B N   
2047 C CA  . HIS B 78  ? 0.25109 0.43103 0.48939 -0.05673 -0.01176 0.04375  110  HIS B CA  
2048 C C   . HIS B 78  ? 0.26031 0.42116 0.46699 -0.05357 -0.01823 0.03350  110  HIS B C   
2049 O O   . HIS B 78  ? 0.27548 0.42857 0.47294 -0.06031 -0.03105 0.02774  110  HIS B O   
2050 C CB  . HIS B 78  ? 0.28527 0.45415 0.52102 -0.06127 -0.00186 0.04556  110  HIS B CB  
2051 C CG  . HIS B 78  ? 0.29773 0.48558 0.56643 -0.06821 0.00428  0.05672  110  HIS B CG  
2052 N ND1 . HIS B 78  ? 0.34524 0.55542 0.64483 -0.07696 -0.00638 0.06149  110  HIS B ND1 
2053 C CD2 . HIS B 78  ? 0.31798 0.50782 0.59385 -0.06711 0.02082  0.06499  110  HIS B CD2 
2054 C CE1 . HIS B 78  ? 0.39969 0.62028 0.71751 -0.07968 0.00401  0.06944  110  HIS B CE1 
2055 N NE2 . HIS B 78  ? 0.33132 0.54231 0.63940 -0.07487 0.02141  0.07350  110  HIS B NE2 
2056 N N   . ALA B 79  ? 0.22624 0.37868 0.41512 -0.04392 -0.00924 0.03097  111  ALA B N   
2057 C CA  . ALA B 79  ? 0.24106 0.38002 0.40501 -0.04179 -0.01366 0.02301  111  ALA B CA  
2058 C C   . ALA B 79  ? 0.24500 0.38902 0.40780 -0.04183 -0.02423 0.02315  111  ALA B C   
2059 O O   . ALA B 79  ? 0.25732 0.39162 0.40235 -0.04450 -0.03164 0.01724  111  ALA B O   
2060 C CB  . ALA B 79  ? 0.23989 0.37183 0.38974 -0.03388 -0.00366 0.02129  111  ALA B CB  
2061 N N   . VAL B 80  ? 0.22293 0.38097 0.40217 -0.03705 -0.02415 0.03039  112  VAL B N   
2062 C CA  . VAL B 80  ? 0.21376 0.37663 0.39151 -0.03566 -0.03563 0.03263  112  VAL B CA  
2063 C C   . VAL B 80  ? 0.22776 0.39540 0.41059 -0.04579 -0.05157 0.03100  112  VAL B C   
2064 O O   . VAL B 80  ? 0.31600 0.47553 0.47937 -0.04755 -0.06266 0.02731  112  VAL B O   
2065 C CB  . VAL B 80  ? 0.22553 0.40303 0.42302 -0.02607 -0.03211 0.04199  112  VAL B CB  
2066 C CG1 . VAL B 80  ? 0.25032 0.43750 0.45262 -0.02477 -0.04739 0.04694  112  VAL B CG1 
2067 C CG2 . VAL B 80  ? 0.29288 0.45564 0.47392 -0.01667 -0.01943 0.04094  112  VAL B CG2 
2068 N N   . SER B 81  ? 0.22526 0.40390 0.43181 -0.05348 -0.05298 0.03363  113  SER B N   
2069 C CA  . SER B 81  ? 0.26400 0.44403 0.47524 -0.06609 -0.06999 0.03097  113  SER B CA  
2070 C C   . SER B 81  ? 0.29038 0.44265 0.46723 -0.07052 -0.07364 0.01910  113  SER B C   
2071 O O   . SER B 81  ? 0.34031 0.48408 0.50070 -0.07573 -0.08878 0.01366  113  SER B O   
2072 C CB  . SER B 81  ? 0.26060 0.45556 0.50523 -0.07578 -0.06835 0.03676  113  SER B CB  
2073 O OG  . SER B 81  ? 0.50324 0.69577 0.75162 -0.09091 -0.08631 0.03307  113  SER B OG  
2074 N N   . GLU B 82  ? 0.28435 0.42199 0.44888 -0.06735 -0.06007 0.01506  114  GLU B N   
2075 C CA  . GLU B 82  ? 0.31183 0.42476 0.44653 -0.06827 -0.06084 0.00458  114  GLU B CA  
2076 C C   . GLU B 82  ? 0.33251 0.43816 0.44020 -0.06124 -0.06175 0.00025  114  GLU B C   
2077 O O   . GLU B 82  ? 0.31756 0.40693 0.40055 -0.06320 -0.06887 -0.00767 114  GLU B O   
2078 C CB  . GLU B 82  ? 0.30705 0.41036 0.43855 -0.06421 -0.04665 0.00342  114  GLU B CB  
2079 C CG  . GLU B 82  ? 0.34949 0.44852 0.49621 -0.07292 -0.04633 0.00598  114  GLU B CG  
2080 C CD  . GLU B 82  ? 0.44717 0.52522 0.58095 -0.08268 -0.05852 -0.00197 114  GLU B CD  
2081 O OE1 . GLU B 82  ? 0.46083 0.51763 0.56608 -0.07785 -0.05874 -0.01139 114  GLU B OE1 
2082 O OE2 . GLU B 82  ? 0.47047 0.55323 0.62272 -0.09531 -0.06807 0.00097  114  GLU B OE2 
2083 N N   . GLY B 83  ? 0.26451 0.37898 0.37383 -0.05310 -0.05335 0.00524  115  GLY B N   
2084 C CA  . GLY B 83  ? 0.25715 0.36439 0.34200 -0.04795 -0.05243 0.00316  115  GLY B CA  
2085 C C   . GLY B 83  ? 0.29313 0.40047 0.36767 -0.05024 -0.06740 0.00433  115  GLY B C   
2086 O O   . GLY B 83  ? 0.32063 0.41409 0.36578 -0.04949 -0.07050 -0.00096 115  GLY B O   
2087 N N   . THR B 84  ? 0.31657 0.44043 0.41444 -0.05211 -0.07687 0.01177  116  THR B N   
2088 C CA  A THR B 84  ? 0.34514 0.47141 0.43417 -0.05385 -0.09439 0.01393  116  THR B CA  
2089 C CA  B THR B 84  ? 0.34636 0.47338 0.43673 -0.05402 -0.09468 0.01413  116  THR B CA  
2090 C C   . THR B 84  ? 0.35681 0.46990 0.42937 -0.06380 -0.10883 0.00444  116  THR B C   
2091 O O   . THR B 84  ? 0.37492 0.47565 0.41694 -0.06384 -0.11974 0.00072  116  THR B O   
2092 C CB  A THR B 84  ? 0.35536 0.50688 0.47883 -0.05237 -0.10200 0.02501  116  THR B CB  
2093 C CB  B THR B 84  ? 0.35067 0.50364 0.47779 -0.05342 -0.10214 0.02489  116  THR B CB  
2094 O OG1 A THR B 84  ? 0.33785 0.50310 0.49338 -0.06031 -0.10258 0.02583  116  THR B OG1 
2095 O OG1 B THR B 84  ? 0.32108 0.48076 0.45959 -0.04264 -0.08768 0.03243  116  THR B OG1 
2096 C CG2 A THR B 84  ? 0.33307 0.48967 0.46453 -0.04063 -0.08767 0.03294  116  THR B CG2 
2097 C CG2 B THR B 84  ? 0.40469 0.56403 0.52597 -0.05408 -0.12291 0.02884  116  THR B CG2 
2098 N N   . LYS B 85  ? 0.30165 0.41334 0.39005 -0.07235 -0.10902 0.00034  117  LYS B N   
2099 C CA  . LYS B 85  ? 0.38255 0.47546 0.45329 -0.08295 -0.12301 -0.00987 117  LYS B CA  
2100 C C   . LYS B 85  ? 0.42185 0.48515 0.44829 -0.07729 -0.11580 -0.02115 117  LYS B C   
2101 O O   . LYS B 85  ? 0.46166 0.50503 0.45665 -0.08105 -0.12850 -0.02999 117  LYS B O   
2102 C CB  . LYS B 85  ? 0.41052 0.50541 0.50884 -0.09376 -0.12249 -0.01005 117  LYS B CB  
2103 C CG  . LYS B 85  ? 0.55554 0.62269 0.63380 -0.10551 -0.13429 -0.02187 117  LYS B CG  
2104 C CD  . LYS B 85  ? 0.52424 0.59164 0.63147 -0.11702 -0.13162 -0.01946 117  LYS B CD  
2105 C CE  . LYS B 85  ? 0.55050 0.60891 0.65731 -0.10823 -0.10935 -0.01856 117  LYS B CE  
2106 N NZ  . LYS B 85  ? 0.60836 0.66673 0.74222 -0.11969 -0.10663 -0.01352 117  LYS B NZ  
2107 N N   . ALA B 86  ? 0.37951 0.44008 0.40299 -0.06800 -0.09562 -0.02116 118  ALA B N   
2108 C CA  . ALA B 86  ? 0.40916 0.44788 0.39706 -0.06068 -0.08586 -0.03010 118  ALA B CA  
2109 C C   . ALA B 86  ? 0.41404 0.44914 0.37213 -0.05512 -0.08766 -0.02927 118  ALA B C   
2110 O O   . ALA B 86  ? 0.44876 0.46192 0.36955 -0.05282 -0.08900 -0.03822 118  ALA B O   
2111 C CB  . ALA B 86  ? 0.39626 0.43990 0.39483 -0.05264 -0.06582 -0.02830 118  ALA B CB  
2112 N N   . VAL B 87  ? 0.36398 0.41717 0.33462 -0.05195 -0.08649 -0.01833 119  VAL B N   
2113 C CA  . VAL B 87  ? 0.39769 0.44517 0.33841 -0.04681 -0.08771 -0.01515 119  VAL B CA  
2114 C C   . VAL B 87  ? 0.45145 0.48854 0.36872 -0.05197 -0.11004 -0.01884 119  VAL B C   
2115 O O   . VAL B 87  ? 0.51765 0.53582 0.39239 -0.04858 -0.11148 -0.02347 119  VAL B O   
2116 C CB  . VAL B 87  ? 0.46364 0.52809 0.42272 -0.04233 -0.08256 -0.00191 119  VAL B CB  
2117 C CG1 . VAL B 87  ? 0.50730 0.56330 0.43424 -0.03788 -0.08656 0.00373  119  VAL B CG1 
2118 C CG2 . VAL B 87  ? 0.36945 0.43932 0.34293 -0.03839 -0.06168 -0.00011 119  VAL B CG2 
2119 N N   . THR B 88  ? 0.47033 0.52024 0.41445 -0.06059 -0.12797 -0.01668 120  THR B N   
2120 C CA  . THR B 88  ? 0.50478 0.54684 0.42984 -0.06797 -0.15319 -0.02083 120  THR B CA  
2121 C C   . THR B 88  ? 0.54986 0.55907 0.43534 -0.07187 -0.15610 -0.03716 120  THR B C   
2122 O O   . THR B 88  ? 0.61780 0.60671 0.45878 -0.07106 -0.16714 -0.04321 120  THR B O   
2123 C CB  . THR B 88  ? 0.48970 0.55602 0.45952 -0.07861 -0.17078 -0.01542 120  THR B CB  
2124 O OG1 . THR B 88  ? 0.48703 0.58178 0.48917 -0.07175 -0.16805 -0.00035 120  THR B OG1 
2125 C CG2 . THR B 88  ? 0.50196 0.56118 0.45408 -0.08909 -0.20047 -0.02079 120  THR B CG2 
2126 N N   . LYS B 89  ? 0.51602 0.51649 0.41348 -0.07483 -0.14591 -0.04445 121  LYS B N   
2127 C CA  . LYS B 89  ? 0.54191 0.50684 0.40175 -0.07644 -0.14681 -0.06037 121  LYS B CA  
2128 C C   . LYS B 89  ? 0.59717 0.54285 0.41141 -0.06233 -0.12986 -0.06539 121  LYS B C   
2129 O O   . LYS B 89  ? 0.66613 0.58196 0.43225 -0.06113 -0.13655 -0.07679 121  LYS B O   
2130 C CB  . LYS B 89  ? 0.59921 0.55908 0.48395 -0.07999 -0.13706 -0.06419 121  LYS B CB  
2131 C CG  . LYS B 89  ? 0.70296 0.62292 0.55492 -0.08281 -0.14004 -0.08030 121  LYS B CG  
2132 C CD  . LYS B 89  ? 0.75385 0.67092 0.63556 -0.08654 -0.13137 -0.08012 121  LYS B CD  
2133 C CE  . LYS B 89  ? 0.86597 0.73824 0.71264 -0.08485 -0.12929 -0.09563 121  LYS B CE  
2134 N NZ  . LYS B 89  ? 0.88835 0.73014 0.69876 -0.09611 -0.15241 -0.10835 121  LYS B NZ  
2135 N N   . TYR B 90  ? 0.57720 0.53976 0.40535 -0.05204 -0.10778 -0.05678 122  TYR B N   
2136 C CA  . TYR B 90  ? 0.56076 0.51098 0.35460 -0.03938 -0.08793 -0.05962 122  TYR B CA  
2137 C C   . TYR B 90  ? 0.65458 0.59483 0.40608 -0.03648 -0.09483 -0.05768 122  TYR B C   
2138 O O   . TYR B 90  ? 0.67618 0.59411 0.38281 -0.02819 -0.08465 -0.06489 122  TYR B O   
2139 C CB  . TYR B 90  ? 0.53396 0.50902 0.35951 -0.03293 -0.06639 -0.04917 122  TYR B CB  
2140 C CG  . TYR B 90  ? 0.51894 0.49085 0.32332 -0.02136 -0.04316 -0.04927 122  TYR B CG  
2141 C CD1 . TYR B 90  ? 0.57875 0.54412 0.38318 -0.01360 -0.02743 -0.05683 122  TYR B CD1 
2142 C CD2 . TYR B 90  ? 0.54420 0.52218 0.33300 -0.01795 -0.03589 -0.03995 122  TYR B CD2 
2143 C CE1 . TYR B 90  ? 0.56569 0.53522 0.35854 -0.00266 -0.00486 -0.05530 122  TYR B CE1 
2144 C CE2 . TYR B 90  ? 0.58047 0.55989 0.35559 -0.00902 -0.01268 -0.03813 122  TYR B CE2 
2145 C CZ  . TYR B 90  ? 0.52887 0.50655 0.30822 -0.00146 0.00279  -0.04585 122  TYR B CZ  
2146 O OH  . TYR B 90  ? 0.60298 0.58798 0.37466 0.00759  0.02648  -0.04270 122  TYR B OH  
2147 N N   . THR B 91  ? 0.65220 0.60903 0.41661 -0.04134 -0.11027 -0.04678 123  THR B N   
2148 C CA  . THR B 91  ? 0.66867 0.61755 0.39458 -0.03812 -0.11907 -0.04168 123  THR B CA  
2149 C C   . THR B 91  ? 0.70784 0.63776 0.40244 -0.04581 -0.14835 -0.05070 123  THR B C   
2150 O O   . THR B 91  ? 0.80227 0.72659 0.46505 -0.04385 -0.16127 -0.04561 123  THR B O   
2151 C CB  . THR B 91  ? 0.67010 0.64526 0.42574 -0.03705 -0.12074 -0.02375 123  THR B CB  
2152 O OG1 . THR B 91  ? 0.67248 0.66847 0.47233 -0.04546 -0.13919 -0.02013 123  THR B OG1 
2153 C CG2 . THR B 91  ? 0.61522 0.60444 0.39547 -0.03119 -0.09348 -0.01581 123  THR B CG2 
2154 N N   . SER B 92  ? 0.75940 0.67658 0.45896 -0.05483 -0.15956 -0.06390 124  SER B N   
2155 C CA  . SER B 92  ? 0.74682 0.64761 0.42320 -0.06610 -0.19097 -0.07283 124  SER B CA  
2156 C C   . SER B 92  ? 0.90210 0.76467 0.50371 -0.05983 -0.19386 -0.08397 124  SER B C   
2157 O O   . SER B 92  ? 0.84562 0.68678 0.41441 -0.04832 -0.16959 -0.09105 124  SER B O   
2158 C CB  . SER B 92  ? 0.89562 0.78664 0.59374 -0.07876 -0.19958 -0.08457 124  SER B CB  
2159 O OG  . SER B 92  ? 0.93101 0.78844 0.59631 -0.07156 -0.18125 -0.09883 124  SER B OG  
2160 N N   . ALA B 93  ? 0.88242 0.74387 0.46853 -0.06520 -0.21852 -0.08375 125  ALA B N   
2161 C CA  . ALA B 93  ? 0.99020 0.82285 0.51560 -0.05794 -0.21793 -0.09171 125  ALA B CA  
2162 C C   . ALA B 93  ? 1.09172 0.88723 0.58688 -0.05843 -0.21140 -0.11206 125  ALA B C   
2163 O O   . ALA B 93  ? 1.15228 0.92001 0.59467 -0.04675 -0.19609 -0.11951 125  ALA B O   
2164 C CB  . ALA B 93  ? 1.03888 0.88394 0.56504 -0.06401 -0.24576 -0.08643 125  ALA B CB  
2165 N N   . LYS B 94  ? 1.08248 0.87616 0.61047 -0.07098 -0.22097 -0.12026 126  LYS B N   
2166 C CA  . LYS B 94  ? 1.21492 0.96947 0.71503 -0.07081 -0.21447 -0.13884 126  LYS B CA  
2167 C C   . LYS B 94  ? 1.23022 0.97584 0.72890 -0.05838 -0.18490 -0.14123 126  LYS B C   
2168 O O   . LYS B 94  ? 1.12512 0.88808 0.66788 -0.06337 -0.18169 -0.13637 126  LYS B O   
2169 C CB  . LYS B 94  ? 1.29556 1.04901 0.83026 -0.08964 -0.23510 -0.14517 126  LYS B CB  
2170 C CG  . LYS B 94  ? 1.35921 1.06620 0.85566 -0.09097 -0.23508 -0.16446 126  LYS B CG  
2171 C CD  . LYS B 94  ? 1.46176 1.14755 0.96388 -0.08529 -0.21390 -0.17194 126  LYS B CD  
2172 C CE  . LYS B 94  ? 1.54640 1.18190 0.99882 -0.07857 -0.20673 -0.19015 126  LYS B CE  
2173 N NZ  . LYS B 94  ? 1.71714 1.33364 1.19266 -0.08480 -0.20308 -0.19676 126  LYS B NZ  
2174 N N   . LYS B 95  ? 1.23725 0.95808 0.68718 -0.04153 -0.16238 -0.14798 1014 LYS B N   
2175 C CA  . LYS B 95  ? 1.22949 0.94705 0.67998 -0.02696 -0.13182 -0.14893 1014 LYS B CA  
2176 C C   . LYS B 95  ? 1.19082 0.88537 0.65387 -0.02873 -0.12831 -0.16172 1014 LYS B C   
2177 O O   . LYS B 95  ? 1.17781 0.84152 0.62030 -0.03306 -0.13800 -0.17461 1014 LYS B O   
2178 C CB  . LYS B 95  ? 1.21255 0.91502 0.61360 -0.00754 -0.10596 -0.15093 1014 LYS B CB  
2179 C CG  . LYS B 95  ? 1.25506 0.97767 0.64149 -0.00425 -0.10445 -0.13605 1014 LYS B CG  
2180 C CD  . LYS B 95  ? 1.15620 0.91479 0.58541 -0.00873 -0.10450 -0.11953 1014 LYS B CD  
2181 C CE  . LYS B 95  ? 1.23214 1.00790 0.64883 0.00169  -0.08420 -0.10350 1014 LYS B CE  
2182 N NZ  . LYS B 95  ? 1.16204 0.98292 0.64566 -0.00261 -0.07792 -0.08448 1014 LYS B NZ  
2183 N N   . ALA B 96  ? 1.11279 0.82351 0.61211 -0.02438 -0.11250 -0.15656 1015 ALA B N   
2184 C CA  . ALA B 96  ? 1.00251 0.69193 0.51409 -0.02209 -0.10461 -0.16604 1015 ALA B CA  
2185 C C   . ALA B 96  ? 1.04109 0.69999 0.50699 0.00079  -0.07798 -0.17709 1015 ALA B C   
2186 O O   . ALA B 96  ? 1.11426 0.78214 0.55574 0.01452  -0.06028 -0.17281 1015 ALA B O   
2187 C CB  . ALA B 96  ? 0.91571 0.64676 0.49791 -0.02335 -0.09320 -0.15096 1015 ALA B CB  
2188 N N   . LYS B 97  ? 1.02622 0.65530 0.49002 0.00571  -0.07211 -0.18787 1016 LYS B N   
2189 C CA  . LYS B 97  ? 1.12572 0.73420 0.55860 0.02941  -0.04478 -0.19522 1016 LYS B CA  
2190 C C   . LYS B 97  ? 0.97606 0.60256 0.43478 0.04845  -0.01643 -0.18961 1016 LYS B C   
2191 O O   . LYS B 97  ? 1.07309 0.69475 0.51646 0.07014  0.00939  -0.19197 1016 LYS B O   
2192 C CB  . LYS B 97  ? 1.17237 0.73429 0.58279 0.02784  -0.05252 -0.21019 1016 LYS B CB  
2193 C CG  . LYS B 97  ? 1.27223 0.81091 0.64810 0.01395  -0.07600 -0.21850 1016 LYS B CG  
2194 C CD  . LYS B 97  ? 1.35969 0.89366 0.68885 0.02810  -0.06322 -0.22052 1016 LYS B CD  
2195 C CE  . LYS B 97  ? 1.44851 0.95893 0.74256 0.01394  -0.08915 -0.22892 1016 LYS B CE  
2196 N NZ  . LYS B 97  ? 1.55866 1.02964 0.84829 0.00456  -0.10298 -0.24227 1016 LYS B NZ  
2197 N N   . THR B 98  ? 0.95780 0.62511 0.47919 0.03922  -0.01922 -0.17487 1017 THR B N   
2198 C CA  . THR B 98  ? 0.92853 0.62788 0.49399 0.05396  0.00471  -0.16421 1017 THR B CA  
2199 C C   . THR B 98  ? 0.88568 0.64051 0.50866 0.04189  0.00112  -0.14491 1017 THR B C   
2200 O O   . THR B 98  ? 0.87980 0.64422 0.51575 0.02239  -0.02074 -0.14038 1017 THR B O   
2201 C CB  . THR B 98  ? 0.93587 0.60964 0.51422 0.05913  0.00589  -0.17029 1017 THR B CB  
2202 O OG1 . THR B 98  ? 0.98648 0.66945 0.60352 0.03737  -0.01526 -0.16380 1017 THR B OG1 
2203 C CG2 . THR B 98  ? 1.06098 0.66908 0.57866 0.06854  0.00530  -0.19148 1017 THR B CG2 
2204 N N   . ARG B 99  ? 0.79425 0.58596 0.45077 0.05445  0.02307  -0.13365 1018 ARG B N   
2205 C CA  . ARG B 99  ? 0.72862 0.56847 0.43816 0.04464  0.02146  -0.11672 1018 ARG B CA  
2206 C C   . ARG B 99  ? 0.81999 0.66187 0.56408 0.02979  0.00356  -0.11357 1018 ARG B C   
2207 O O   . ARG B 99  ? 0.69288 0.55778 0.46227 0.01460  -0.00936 -0.10439 1018 ARG B O   
2208 C CB  . ARG B 99  ? 0.66340 0.53673 0.40230 0.06025  0.04614  -0.10776 1018 ARG B CB  
2209 C CG  . ARG B 99  ? 0.68013 0.55933 0.39183 0.07358  0.06721  -0.10745 1018 ARG B CG  
2210 C CD  . ARG B 99  ? 0.69851 0.60635 0.44023 0.09083  0.09126  -0.10129 1018 ARG B CD  
2211 N NE  . ARG B 99  ? 0.68903 0.56726 0.41763 0.10728  0.09679  -0.11251 1018 ARG B NE  
2212 C CZ  . ARG B 99  ? 0.70336 0.60037 0.46320 0.12292  0.11066  -0.10845 1018 ARG B CZ  
2213 N NH1 . ARG B 99  ? 0.58864 0.53606 0.39604 0.12277  0.11944  -0.09417 1018 ARG B NH1 
2214 N NH2 . ARG B 99  ? 0.70659 0.56958 0.44904 0.13903  0.11451  -0.11889 1018 ARG B NH2 
2215 N N   . SER B 100 ? 0.75675 0.57341 0.50143 0.03488  0.00387  -0.12028 1019 SER B N   
2216 C CA  . SER B 100 ? 0.85929 0.67735 0.63640 0.02097  -0.01011 -0.11543 1019 SER B CA  
2217 C C   . SER B 100 ? 0.84491 0.65076 0.61513 -0.00105 -0.03458 -0.11826 1019 SER B C   
2218 O O   . SER B 100 ? 0.80754 0.63681 0.61403 -0.01542 -0.04494 -0.10824 1019 SER B O   
2219 C CB  . SER B 100 ? 0.83308 0.61775 0.60381 0.03076  -0.00548 -0.12224 1019 SER B CB  
2220 O OG  . SER B 100 ? 0.97265 0.70574 0.69797 0.02802  -0.01503 -0.13827 1019 SER B OG  
2221 N N   . SER B 101 ? 0.83304 0.60243 0.55694 -0.00352 -0.04431 -0.13196 1020 SER B N   
2222 C CA  . SER B 101 ? 0.92448 0.68268 0.64078 -0.02497 -0.07064 -0.13552 1020 SER B CA  
2223 C C   . SER B 101 ? 0.86988 0.66245 0.59460 -0.03204 -0.07870 -0.12609 1020 SER B C   
2224 O O   . SER B 101 ? 0.90714 0.70421 0.64047 -0.04978 -0.10128 -0.12447 1020 SER B O   
2225 C CB  . SER B 101 ? 0.97562 0.67853 0.63479 -0.02591 -0.08110 -0.15491 1020 SER B CB  
2226 O OG  . SER B 101 ? 1.02092 0.71130 0.63313 -0.00952 -0.06884 -0.16245 1020 SER B OG  
2227 N N   . ARG B 102 ? 0.80345 0.61894 0.52503 -0.01862 -0.06127 -0.11955 1021 ARG B N   
2228 C CA  . ARG B 102 ? 0.71477 0.55656 0.43917 -0.02416 -0.06839 -0.11004 1021 ARG B CA  
2229 C C   . ARG B 102 ? 0.69489 0.57596 0.47393 -0.03460 -0.07436 -0.09486 1021 ARG B C   
2230 O O   . ARG B 102 ? 0.66617 0.56114 0.45258 -0.04491 -0.09091 -0.08887 1021 ARG B O   
2231 C CB  . ARG B 102 ? 0.70522 0.55815 0.41161 -0.00827 -0.04615 -0.10601 1021 ARG B CB  
2232 C CG  . ARG B 102 ? 0.74569 0.62195 0.45359 -0.01288 -0.05139 -0.09449 1021 ARG B CG  
2233 C CD  . ARG B 102 ? 0.77883 0.65422 0.45459 0.00079  -0.03100 -0.09275 1021 ARG B CD  
2234 N NE  . ARG B 102 ? 0.69624 0.58703 0.36625 -0.00341 -0.03645 -0.08110 1021 ARG B NE  
2235 C CZ  . ARG B 102 ? 0.80478 0.69972 0.45202 0.00544  -0.01883 -0.07472 1021 ARG B CZ  
2236 N NH1 . ARG B 102 ? 0.83529 0.72593 0.46834 0.01903  0.00649  -0.07842 1021 ARG B NH1 
2237 N NH2 . ARG B 102 ? 0.74582 0.64968 0.38513 0.00115  -0.02601 -0.06329 1021 ARG B NH2 
2238 N N   . ALA B 103 ? 0.64579 0.54474 0.46174 -0.03071 -0.06120 -0.08829 1022 ALA B N   
2239 C CA  . ALA B 103 ? 0.57333 0.50657 0.43616 -0.03833 -0.06389 -0.07469 1022 ALA B CA  
2240 C C   . ALA B 103 ? 0.69462 0.62590 0.58684 -0.04733 -0.06992 -0.07357 1022 ALA B C   
2241 O O   . ALA B 103 ? 0.59243 0.54990 0.52135 -0.05391 -0.07231 -0.06279 1022 ALA B O   
2242 C CB  . ALA B 103 ? 0.57488 0.53502 0.45686 -0.02780 -0.04403 -0.06536 1022 ALA B CB  
2243 N N   . GLY B 104 ? 0.66442 0.56361 0.54004 -0.04664 -0.07037 -0.08373 1023 GLY B N   
2244 C CA  . GLY B 104 ? 0.70227 0.59485 0.60239 -0.05550 -0.07445 -0.08153 1023 GLY B CA  
2245 C C   . GLY B 104 ? 0.59800 0.50966 0.52756 -0.04719 -0.05862 -0.07198 1023 GLY B C   
2246 O O   . GLY B 104 ? 0.62998 0.54466 0.58480 -0.05535 -0.06100 -0.06570 1023 GLY B O   
2247 N N   . LEU B 105 ? 0.54872 0.47284 0.47478 -0.03159 -0.04270 -0.07045 1024 LEU B N   
2248 C CA  . LEU B 105 ? 0.56350 0.51012 0.51696 -0.02425 -0.03050 -0.06113 1024 LEU B CA  
2249 C C   . LEU B 105 ? 0.60576 0.53704 0.54915 -0.00841 -0.01823 -0.06535 1024 LEU B C   
2250 O O   . LEU B 105 ? 0.67216 0.57845 0.58610 0.00034  -0.01479 -0.07556 1024 LEU B O   
2251 C CB  . LEU B 105 ? 0.47329 0.45318 0.43916 -0.02100 -0.02381 -0.05371 1024 LEU B CB  
2252 C CG  . LEU B 105 ? 0.52972 0.52551 0.50559 -0.03266 -0.03449 -0.04814 1024 LEU B CG  
2253 C CD1 . LEU B 105 ? 0.47570 0.49607 0.45803 -0.02809 -0.02629 -0.04146 1024 LEU B CD1 
2254 C CD2 . LEU B 105 ? 0.53181 0.53711 0.53722 -0.04237 -0.04029 -0.04073 1024 LEU B CD2 
2255 N N   . GLN B 106 ? 0.55398 0.49994 0.52103 -0.00352 -0.01180 -0.05711 1025 GLN B N   
2256 C CA  . GLN B 106 ? 0.61812 0.56165 0.58468 0.01380  -0.00030 -0.05724 1025 GLN B CA  
2257 C C   . GLN B 106 ? 0.57071 0.54904 0.55062 0.02305  0.01010  -0.05256 1025 GLN B C   
2258 O O   . GLN B 106 ? 0.62902 0.60884 0.60333 0.03861  0.02071  -0.05537 1025 GLN B O   
2259 C CB  . GLN B 106 ? 0.61590 0.55487 0.59866 0.01360  -0.00145 -0.04977 1025 GLN B CB  
2260 C CG  . GLN B 106 ? 0.69968 0.60489 0.67357 0.00192  -0.01059 -0.05222 1025 GLN B CG  
2261 C CD  . GLN B 106 ? 0.70916 0.57379 0.65157 0.00820  -0.01094 -0.06470 1025 GLN B CD  
2262 O OE1 . GLN B 106 ? 0.73468 0.58667 0.66637 0.02658  -0.00159 -0.06766 1025 GLN B OE1 
2263 N NE2 . GLN B 106 ? 0.77306 0.61750 0.69953 -0.00590 -0.02205 -0.07253 1025 GLN B NE2 
2264 N N   . PHE B 107 ? 0.44961 0.45576 0.44857 0.01369  0.00764  -0.04512 1026 PHE B N   
2265 C CA  . PHE B 107 ? 0.39997 0.43702 0.41224 0.01835  0.01589  -0.04052 1026 PHE B CA  
2266 C C   . PHE B 107 ? 0.49415 0.53033 0.48718 0.02048  0.02161  -0.04538 1026 PHE B C   
2267 O O   . PHE B 107 ? 0.54766 0.57137 0.52445 0.01167  0.01432  -0.04838 1026 PHE B O   
2268 C CB  . PHE B 107 ? 0.33200 0.39032 0.36387 0.00711  0.01116  -0.03258 1026 PHE B CB  
2269 C CG  . PHE B 107 ? 0.37415 0.44183 0.42433 0.00844  0.00992  -0.02641 1026 PHE B CG  
2270 C CD1 . PHE B 107 ? 0.44043 0.48932 0.48867 0.00895  0.00605  -0.02565 1026 PHE B CD1 
2271 C CD2 . PHE B 107 ? 0.38018 0.47281 0.44652 0.00844  0.01219  -0.02129 1026 PHE B CD2 
2272 C CE1 . PHE B 107 ? 0.46706 0.52218 0.52658 0.01108  0.00527  -0.01911 1026 PHE B CE1 
2273 C CE2 . PHE B 107 ? 0.40227 0.50101 0.47964 0.00990  0.00934  -0.01633 1026 PHE B CE2 
2274 C CZ  . PHE B 107 ? 0.36501 0.44496 0.43746 0.01219  0.00638  -0.01495 1026 PHE B CZ  
2275 N N   . PRO B 108 ? 0.42832 0.47952 0.42329 0.03183  0.03451  -0.04512 1027 PRO B N   
2276 C CA  . PRO B 108 ? 0.42891 0.47541 0.40008 0.03595  0.04327  -0.04950 1027 PRO B CA  
2277 C C   . PRO B 108 ? 0.40981 0.47680 0.38671 0.02565  0.04425  -0.04250 1027 PRO B C   
2278 O O   . PRO B 108 ? 0.41596 0.50998 0.41969 0.02196  0.04695  -0.03455 1027 PRO B O   
2279 C CB  . PRO B 108 ? 0.51742 0.57482 0.49387 0.05386  0.05926  -0.05031 1027 PRO B CB  
2280 C CG  . PRO B 108 ? 0.59360 0.67770 0.60641 0.05448  0.05736  -0.04232 1027 PRO B CG  
2281 C CD  . PRO B 108 ? 0.52119 0.59166 0.53803 0.04358  0.04195  -0.04118 1027 PRO B CD  
2282 N N   . VAL B 109 ? 0.41879 0.46975 0.36805 0.02064  0.04055  -0.04549 1028 VAL B N   
2283 C CA  . VAL B 109 ? 0.37996 0.44392 0.32961 0.01160  0.04041  -0.03794 1028 VAL B CA  
2284 C C   . VAL B 109 ? 0.41077 0.49913 0.37140 0.01595  0.05782  -0.03149 1028 VAL B C   
2285 O O   . VAL B 109 ? 0.37520 0.48248 0.35488 0.00739  0.05872  -0.02266 1028 VAL B O   
2286 C CB  . VAL B 109 ? 0.46719 0.50734 0.37990 0.00838  0.03274  -0.04237 1028 VAL B CB  
2287 C CG1 . VAL B 109 ? 0.52749 0.57761 0.43399 0.00276  0.03560  -0.03343 1028 VAL B CG1 
2288 C CG2 . VAL B 109 ? 0.47994 0.50480 0.39373 -0.00057 0.01290  -0.04589 1028 VAL B CG2 
2289 N N   . GLY B 110 ? 0.40742 0.49516 0.35704 0.02913  0.07249  -0.03560 1029 GLY B N   
2290 C CA  . GLY B 110 ? 0.44825 0.56241 0.41032 0.03306  0.09120  -0.02846 1029 GLY B CA  
2291 C C   . GLY B 110 ? 0.41780 0.56562 0.42526 0.02961  0.09235  -0.02102 1029 GLY B C   
2292 O O   . GLY B 110 ? 0.36095 0.53323 0.38675 0.02295  0.10090  -0.01214 1029 GLY B O   
2293 N N   . ARG B 111 ? 0.36263 0.51101 0.38722 0.03385  0.08370  -0.02427 1030 ARG B N   
2294 C CA  . ARG B 111 ? 0.37742 0.55566 0.44100 0.02999  0.08100  -0.01772 1030 ARG B CA  
2295 C C   . ARG B 111 ? 0.33297 0.51516 0.40601 0.01236  0.07065  -0.01210 1030 ARG B C   
2296 O O   . ARG B 111 ? 0.35331 0.55979 0.44962 0.00432  0.07374  -0.00517 1030 ARG B O   
2297 C CB  . ARG B 111 ? 0.44922 0.62252 0.52276 0.03888  0.07275  -0.02141 1030 ARG B CB  
2298 C CG  . ARG B 111 ? 0.49533 0.68986 0.59925 0.03088  0.06262  -0.01554 1030 ARG B CG  
2299 C CD  . ARG B 111 ? 0.57382 0.80586 0.71050 0.03662  0.06946  -0.00996 1030 ARG B CD  
2300 N NE  . ARG B 111 ? 0.67955 0.91409 0.81863 0.05699  0.07744  -0.01247 1030 ARG B NE  
2301 C CZ  . ARG B 111 ? 0.71862 0.95679 0.87074 0.06722  0.07013  -0.01183 1030 ARG B CZ  
2302 N NH1 . ARG B 111 ? 0.59340 0.83183 0.75391 0.05860  0.05472  -0.00932 1030 ARG B NH1 
2303 N NH2 . ARG B 111 ? 0.72282 0.96235 0.87694 0.08808  0.07917  -0.01339 1030 ARG B NH2 
2304 N N   . VAL B 112 ? 0.30791 0.46595 0.36349 0.00611  0.05864  -0.01489 1031 VAL B N   
2305 C CA  . VAL B 112 ? 0.26442 0.42333 0.32703 -0.00747 0.05027  -0.00978 1031 VAL B CA  
2306 C C   . VAL B 112 ? 0.29195 0.45585 0.34858 -0.01456 0.05864  -0.00338 1031 VAL B C   
2307 O O   . VAL B 112 ? 0.30515 0.47948 0.37722 -0.02476 0.05797  0.00267  1031 VAL B O   
2308 C CB  . VAL B 112 ? 0.32784 0.46377 0.37630 -0.01067 0.03742  -0.01292 1031 VAL B CB  
2309 C CG1 . VAL B 112 ? 0.30761 0.44361 0.36239 -0.02143 0.03101  -0.00731 1031 VAL B CG1 
2310 C CG2 . VAL B 112 ? 0.33180 0.46213 0.38758 -0.00557 0.03074  -0.01712 1031 VAL B CG2 
2311 N N   . HIS B 113 ? 0.29172 0.44543 0.32300 -0.00936 0.06707  -0.00451 1032 HIS B N   
2312 C CA  . HIS B 113 ? 0.30499 0.46161 0.32692 -0.01533 0.07710  0.00337  1032 HIS B CA  
2313 C C   . HIS B 113 ? 0.37631 0.56279 0.42734 -0.01920 0.08997  0.01029  1032 HIS B C   
2314 O O   . HIS B 113 ? 0.32145 0.51412 0.38249 -0.03157 0.09181  0.01855  1032 HIS B O   
2315 C CB  . HIS B 113 ? 0.36577 0.50569 0.35078 -0.00677 0.08531  0.00036  1032 HIS B CB  
2316 C CG  . HIS B 113 ? 0.51020 0.64256 0.47408 -0.01295 0.09129  0.00904  1032 HIS B CG  
2317 N ND1 . HIS B 113 ? 0.65067 0.76563 0.57476 -0.00627 0.09828  0.00786  1032 HIS B ND1 
2318 C CD2 . HIS B 113 ? 0.57671 0.71279 0.55013 -0.02476 0.09124  0.01939  1032 HIS B CD2 
2319 C CE1 . HIS B 113 ? 0.77653 0.88648 0.68695 -0.01340 0.10238  0.01843  1032 HIS B CE1 
2320 N NE2 . HIS B 113 ? 0.66981 0.79160 0.61069 -0.02476 0.09844  0.02572  1032 HIS B NE2 
2321 N N   . ARG B 114 ? 0.34032 0.54555 0.40655 -0.00880 0.09873  0.00749  1033 ARG B N   
2322 C CA  . ARG B 114 ? 0.29360 0.53380 0.39376 -0.01229 0.11017  0.01474  1033 ARG B CA  
2323 C C   . ARG B 114 ? 0.30143 0.55497 0.43191 -0.02601 0.09706  0.01773  1033 ARG B C   
2324 O O   . ARG B 114 ? 0.34846 0.62125 0.50060 -0.03876 0.10188  0.02568  1033 ARG B O   
2325 C CB  . ARG B 114 ? 0.36812 0.62659 0.48063 0.00499  0.12040  0.01105  1033 ARG B CB  
2326 C CG  . ARG B 114 ? 0.53973 0.84182 0.69426 0.00356  0.13181  0.01909  1033 ARG B CG  
2327 C CD  . ARG B 114 ? 0.59871 0.91631 0.76025 0.02548  0.14568  0.01609  1033 ARG B CD  
2328 N NE  . ARG B 114 ? 0.65826 0.95986 0.81382 0.03886  0.13316  0.00687  1033 ARG B NE  
2329 C CZ  . ARG B 114 ? 0.72655 1.04536 0.91172 0.03982  0.12021  0.00734  1033 ARG B CZ  
2330 N NH1 . ARG B 114 ? 0.77242 1.12558 0.99592 0.02720  0.11521  0.01503  1033 ARG B NH1 
2331 N NH2 . ARG B 114 ? 0.68795 0.98710 0.86210 0.05313  0.11135  0.00017  1033 ARG B NH2 
2332 N N   . LEU B 115 ? 0.30695 0.54865 0.43743 -0.02435 0.08080  0.01148  1034 LEU B N   
2333 C CA  . LEU B 115 ? 0.36694 0.61663 0.51893 -0.03595 0.06811  0.01288  1034 LEU B CA  
2334 C C   . LEU B 115 ? 0.34130 0.57389 0.48325 -0.05101 0.06443  0.01699  1034 LEU B C   
2335 O O   . LEU B 115 ? 0.33005 0.57245 0.49020 -0.06433 0.06109  0.02075  1034 LEU B O   
2336 C CB  . LEU B 115 ? 0.39106 0.62954 0.54029 -0.02912 0.05421  0.00620  1034 LEU B CB  
2337 C CG  . LEU B 115 ? 0.44618 0.69872 0.60703 -0.01404 0.05534  0.00318  1034 LEU B CG  
2338 C CD1 . LEU B 115 ? 0.42046 0.65205 0.56937 -0.00825 0.04323  -0.00210 1034 LEU B CD1 
2339 C CD2 . LEU B 115 ? 0.55219 0.84149 0.74891 -0.01629 0.05493  0.00775  1034 LEU B CD2 
2340 N N   . LEU B 116 ? 0.28413 0.48997 0.39701 -0.04906 0.06391  0.01641  1035 LEU B N   
2341 C CA  . LEU B 116 ? 0.32405 0.51230 0.42626 -0.06037 0.06176  0.02184  1035 LEU B CA  
2342 C C   . LEU B 116 ? 0.36141 0.56024 0.46972 -0.07014 0.07512  0.03116  1035 LEU B C   
2343 O O   . LEU B 116 ? 0.37828 0.57244 0.49416 -0.08400 0.07325  0.03630  1035 LEU B O   
2344 C CB  . LEU B 116 ? 0.31456 0.47654 0.38661 -0.05437 0.05769  0.02074  1035 LEU B CB  
2345 C CG  . LEU B 116 ? 0.30400 0.45337 0.37323 -0.04978 0.04393  0.01449  1035 LEU B CG  
2346 C CD1 . LEU B 116 ? 0.31017 0.44106 0.35471 -0.04397 0.03953  0.01373  1035 LEU B CD1 
2347 C CD2 . LEU B 116 ? 0.28590 0.42744 0.36332 -0.05796 0.03682  0.01623  1035 LEU B CD2 
2348 N N   . ARG B 117 ? 0.32550 0.53628 0.42888 -0.06322 0.08991  0.03370  1036 ARG B N   
2349 C CA  . ARG B 117 ? 0.33471 0.55830 0.44562 -0.07280 0.10572  0.04439  1036 ARG B CA  
2350 C C   . ARG B 117 ? 0.35445 0.60992 0.50764 -0.08461 0.10632  0.04758  1036 ARG B C   
2351 O O   . ARG B 117 ? 0.39441 0.65179 0.55892 -0.10160 0.10985  0.05604  1036 ARG B O   
2352 C CB  . ARG B 117 ? 0.38083 0.61012 0.47432 -0.06055 0.12368  0.04610  1036 ARG B CB  
2353 C CG  . ARG B 117 ? 0.57461 0.77254 0.62522 -0.05910 0.12667  0.05027  1036 ARG B CG  
2354 C CD  . ARG B 117 ? 0.80226 0.99715 0.82369 -0.04519 0.14208  0.04938  1036 ARG B CD  
2355 N NE  . ARG B 117 ? 0.87207 1.03267 0.84780 -0.04086 0.13537  0.04878  1036 ARG B NE  
2356 C CZ  . ARG B 117 ? 1.05065 1.19816 0.98801 -0.03062 0.14588  0.04844  1036 ARG B CZ  
2357 N NH1 . ARG B 117 ? 1.11419 1.27784 1.05142 -0.02070 0.16536  0.04689  1036 ARG B NH1 
2358 N NH2 . ARG B 117 ? 0.98725 1.10454 0.88427 -0.02892 0.13606  0.04927  1036 ARG B NH2 
2359 N N   . LYS B 118 ? 0.29866 0.57779 0.47539 -0.07668 0.10105  0.04127  1037 LYS B N   
2360 C CA  . LYS B 118 ? 0.41868 0.73031 0.63687 -0.08642 0.09823  0.04392  1037 LYS B CA  
2361 C C   . LYS B 118 ? 0.37028 0.66728 0.59420 -0.10422 0.08185  0.04302  1037 LYS B C   
2362 O O   . LYS B 118 ? 0.38171 0.68821 0.62985 -0.11613 0.07898  0.04553  1037 LYS B O   
2363 C CB  . LYS B 118 ? 0.45043 0.78222 0.68577 -0.07055 0.09233  0.03697  1037 LYS B CB  
2364 C CG  . LYS B 118 ? 0.55134 0.91070 0.82498 -0.07246 0.09027  0.03851  1037 LYS B CG  
2365 C CD  . LYS B 118 ? 0.65292 1.02903 0.94012 -0.05515 0.08292  0.03296  1037 LYS B CD  
2366 C CE  . LYS B 118 ? 0.75760 1.12299 1.01881 -0.03583 0.08917  0.02825  1037 LYS B CE  
2367 N NZ  . LYS B 118 ? 0.77190 1.14321 1.02518 -0.02188 0.11123  0.03015  1037 LYS B NZ  
2368 N N   . GLY B 119 ? 0.32743 0.59408 0.52637 -0.10341 0.07021  0.03752  1038 GLY B N   
2369 C CA  . GLY B 119 ? 0.37430 0.62341 0.57352 -0.11752 0.05584  0.03510  1038 GLY B CA  
2370 C C   . GLY B 119 ? 0.38468 0.61003 0.57263 -0.13329 0.06020  0.04229  1038 GLY B C   
2371 O O   . GLY B 119 ? 0.38233 0.58936 0.56914 -0.14585 0.04929  0.03990  1038 GLY B O   
2372 N N   . ASN B 120 ? 0.36500 0.58672 0.54109 -0.13232 0.07605  0.05107  1039 ASN B N   
2373 C CA  . ASN B 120 ? 0.40975 0.60624 0.57226 -0.14617 0.08197  0.06043  1039 ASN B CA  
2374 C C   . ASN B 120 ? 0.44694 0.60183 0.58401 -0.14561 0.06928  0.05608  1039 ASN B C   
2375 O O   . ASN B 120 ? 0.46163 0.59517 0.59789 -0.16047 0.06471  0.05815  1039 ASN B O   
2376 C CB  . ASN B 120 ? 0.40108 0.61122 0.59262 -0.16519 0.08501  0.06611  1039 ASN B CB  
2377 C CG  . ASN B 120 ? 0.51519 0.76018 0.73099 -0.15900 0.09908  0.06959  1039 ASN B CG  
2378 O OD1 . ASN B 120 ? 0.56062 0.81048 0.76203 -0.14861 0.11497  0.07492  1039 ASN B OD1 
2379 N ND2 . ASN B 120 ? 0.62346 0.89201 0.87437 -0.16519 0.09359  0.06638  1039 ASN B ND2 
2380 N N   . TYR B 121 ? 0.40009 0.54360 0.51734 -0.12791 0.06385  0.04981  1040 TYR B N   
2381 C CA  . TYR B 121 ? 0.36136 0.47037 0.45659 -0.12307 0.05419  0.04675  1040 TYR B CA  
2382 C C   . TYR B 121 ? 0.43945 0.51998 0.50978 -0.12312 0.06033  0.05693  1040 TYR B C   
2383 O O   . TYR B 121 ? 0.43179 0.48194 0.48781 -0.12207 0.05396  0.05709  1040 TYR B O   
2384 C CB  . TYR B 121 ? 0.36593 0.47776 0.45420 -0.10567 0.04680  0.03821  1040 TYR B CB  
2385 C CG  . TYR B 121 ? 0.34136 0.47372 0.44917 -0.10456 0.03928  0.02922  1040 TYR B CG  
2386 C CD1 . TYR B 121 ? 0.34251 0.46433 0.45395 -0.11106 0.02913  0.02365  1040 TYR B CD1 
2387 C CD2 . TYR B 121 ? 0.34523 0.50414 0.46425 -0.09590 0.04200  0.02627  1040 TYR B CD2 
2388 C CE1 . TYR B 121 ? 0.37039 0.50936 0.49539 -0.10933 0.02094  0.01632  1040 TYR B CE1 
2389 C CE2 . TYR B 121 ? 0.28750 0.46365 0.42304 -0.09353 0.03429  0.01964  1040 TYR B CE2 
2390 C CZ  . TYR B 121 ? 0.37426 0.54111 0.51233 -0.10054 0.02322  0.01514  1040 TYR B CZ  
2391 O OH  . TYR B 121 ? 0.37183 0.55371 0.52166 -0.09757 0.01428  0.00940  1040 TYR B OH  
2392 N N   . ALA B 122 ? 0.45513 0.54334 0.51773 -0.12258 0.07302  0.06586  1041 ALA B N   
2393 C CA  . ALA B 122 ? 0.41090 0.47144 0.44689 -0.12286 0.07899  0.07762  1041 ALA B CA  
2394 C C   . ALA B 122 ? 0.46011 0.53721 0.49345 -0.12620 0.09628  0.08721  1041 ALA B C   
2395 O O   . ALA B 122 ? 0.44275 0.55239 0.49458 -0.12480 0.10296  0.08337  1041 ALA B O   
2396 C CB  . ALA B 122 ? 0.46593 0.50800 0.47621 -0.10552 0.07033  0.07613  1041 ALA B CB  
2397 N N   . GLU B 123 ? 0.49626 0.54968 0.50507 -0.12914 0.10453  0.10054  1042 GLU B N   
2398 C CA  . GLU B 123 ? 0.52939 0.59439 0.52859 -0.13104 0.12359  0.11140  1042 GLU B CA  
2399 C C   . GLU B 123 ? 0.53471 0.61393 0.51701 -0.11276 0.12559  0.10493  1042 GLU B C   
2400 O O   . GLU B 123 ? 0.52400 0.62786 0.51203 -0.11137 0.14108  0.10632  1042 GLU B O   
2401 C CB  . GLU B 123 ? 0.55979 0.58997 0.52869 -0.13572 0.13020  0.12768  1042 GLU B CB  
2402 C CG  . GLU B 123 ? 0.55751 0.57727 0.54426 -0.15826 0.13641  0.13711  1042 GLU B CG  
2403 C CD  . GLU B 123 ? 0.81160 0.79275 0.76577 -0.16235 0.14419  0.15495  1042 GLU B CD  
2404 O OE1 . GLU B 123 ? 0.83856 0.79058 0.79487 -0.17518 0.14043  0.16004  1042 GLU B OE1 
2405 O OE2 . GLU B 123 ? 0.86788 0.84284 0.78981 -0.15170 0.15287  0.16381  1042 GLU B OE2 
2406 N N   . ARG B 124 ? 0.48732 0.55070 0.44887 -0.09863 0.11044  0.09789  1043 ARG B N   
2407 C CA  . ARG B 124 ? 0.49981 0.56998 0.44147 -0.08305 0.10909  0.09051  1043 ARG B CA  
2408 C C   . ARG B 124 ? 0.46446 0.53670 0.41541 -0.07417 0.09033  0.07657  1043 ARG B C   
2409 O O   . ARG B 124 ? 0.44751 0.50917 0.40899 -0.07628 0.07791  0.07481  1043 ARG B O   
2410 C CB  . ARG B 124 ? 0.49123 0.53688 0.38701 -0.07502 0.11022  0.09924  1043 ARG B CB  
2411 C CG  . ARG B 124 ? 0.75398 0.79684 0.63203 -0.08103 0.13208  0.11385  1043 ARG B CG  
2412 C CD  . ARG B 124 ? 0.88280 0.89422 0.71294 -0.07432 0.12928  0.12485  1043 ARG B CD  
2413 N NE  . ARG B 124 ? 0.92691 0.91453 0.75795 -0.07630 0.11350  0.12992  1043 ARG B NE  
2414 C CZ  . ARG B 124 ? 0.98865 0.96026 0.82716 -0.08844 0.11928  0.14216  1043 ARG B CZ  
2415 N NH1 . ARG B 124 ? 0.99470 0.97236 0.84072 -0.10219 0.14005  0.15250  1043 ARG B NH1 
2416 N NH2 . ARG B 124 ? 0.95769 0.90607 0.79691 -0.08680 0.10453  0.14438  1043 ARG B NH2 
2417 N N   . VAL B 125 ? 0.41916 0.50321 0.36447 -0.06379 0.08977  0.06691  1044 VAL B N   
2418 C CA  . VAL B 125 ? 0.40630 0.49149 0.35781 -0.05583 0.07358  0.05464  1044 VAL B CA  
2419 C C   . VAL B 125 ? 0.48164 0.55219 0.39776 -0.04553 0.06674  0.05216  1044 VAL B C   
2420 O O   . VAL B 125 ? 0.52133 0.59261 0.41573 -0.04029 0.07703  0.05082  1044 VAL B O   
2421 C CB  . VAL B 125 ? 0.41956 0.52880 0.39742 -0.05381 0.07664  0.04449  1044 VAL B CB  
2422 C CG1 . VAL B 125 ? 0.41085 0.51712 0.39089 -0.04618 0.06134  0.03348  1044 VAL B CG1 
2423 C CG2 . VAL B 125 ? 0.48595 0.61065 0.49812 -0.06510 0.07964  0.04675  1044 VAL B CG2 
2424 N N   . GLY B 126 ? 0.41205 0.46949 0.32190 -0.04247 0.04945  0.05171  1045 GLY B N   
2425 C CA  . GLY B 126 ? 0.48370 0.52853 0.36232 -0.03471 0.03834  0.04923  1045 GLY B CA  
2426 C C   . GLY B 126 ? 0.45131 0.50241 0.32987 -0.02962 0.03385  0.03509  1045 GLY B C   
2427 O O   . GLY B 126 ? 0.47927 0.54414 0.38570 -0.03061 0.03547  0.02783  1045 GLY B O   
2428 N N   . ALA B 127 ? 0.48926 0.52668 0.33221 -0.02400 0.02755  0.03121  1046 ALA B N   
2429 C CA  . ALA B 127 ? 0.54816 0.58402 0.38342 -0.01927 0.02475  0.01711  1046 ALA B CA  
2430 C C   . ALA B 127 ? 0.51777 0.55831 0.37881 -0.02140 0.00768  0.00959  1046 ALA B C   
2431 O O   . ALA B 127 ? 0.52370 0.56577 0.39201 -0.01930 0.00845  -0.00095 1046 ALA B O   
2432 C CB  . ALA B 127 ? 0.63184 0.64651 0.41722 -0.01386 0.01993  0.01359  1046 ALA B CB  
2433 N N   . GLY B 128 ? 0.45280 0.49521 0.32805 -0.02466 -0.00655 0.01569  1047 GLY B N   
2434 C CA  . GLY B 128 ? 0.43965 0.48941 0.34204 -0.02701 -0.02011 0.01048  1047 GLY B CA  
2435 C C   . GLY B 128 ? 0.41074 0.47501 0.34976 -0.02920 -0.01225 0.01027  1047 GLY B C   
2436 O O   . GLY B 128 ? 0.37881 0.44818 0.33676 -0.03033 -0.01783 0.00428  1047 GLY B O   
2437 N N   . ALA B 129 ? 0.34713 0.41651 0.29489 -0.03072 0.00013  0.01697  1048 ALA B N   
2438 C CA  . ALA B 129 ? 0.31121 0.39194 0.29004 -0.03350 0.00436  0.01672  1048 ALA B CA  
2439 C C   . ALA B 129 ? 0.32320 0.41250 0.31425 -0.03221 0.00897  0.00786  1048 ALA B C   
2440 O O   . ALA B 129 ? 0.31372 0.40830 0.32498 -0.03285 0.00450  0.00526  1048 ALA B O   
2441 C CB  . ALA B 129 ? 0.31923 0.40078 0.30224 -0.03770 0.01523  0.02465  1048 ALA B CB  
2442 N N   . PRO B 130 ? 0.31974 0.41088 0.30013 -0.02906 0.01913  0.00403  1049 PRO B N   
2443 C CA  . PRO B 130 ? 0.28107 0.37968 0.27515 -0.02537 0.02242  -0.00339 1049 PRO B CA  
2444 C C   . PRO B 130 ? 0.28691 0.37414 0.27550 -0.02306 0.01144  -0.01098 1049 PRO B C   
2445 O O   . PRO B 130 ? 0.29044 0.38101 0.29463 -0.02144 0.01063  -0.01472 1049 PRO B O   
2446 C CB  . PRO B 130 ? 0.32806 0.43169 0.31154 -0.02016 0.03738  -0.00451 1049 PRO B CB  
2447 C CG  . PRO B 130 ? 0.42810 0.51973 0.38181 -0.02028 0.03958  -0.00076 1049 PRO B CG  
2448 C CD  . PRO B 130 ? 0.37603 0.46407 0.33384 -0.02741 0.03051  0.00746  1049 PRO B CD  
2449 N N   . VAL B 131 ? 0.33049 0.40324 0.29617 -0.02359 0.00222  -0.01301 1050 VAL B N   
2450 C CA  . VAL B 131 ? 0.32883 0.39023 0.29184 -0.02503 -0.01049 -0.01992 1050 VAL B CA  
2451 C C   . VAL B 131 ? 0.32699 0.39778 0.31878 -0.03031 -0.01860 -0.01570 1050 VAL B C   
2452 O O   . VAL B 131 ? 0.32028 0.38976 0.32513 -0.03127 -0.02080 -0.01914 1050 VAL B O   
2453 C CB  . VAL B 131 ? 0.38543 0.43085 0.31806 -0.02647 -0.02188 -0.02268 1050 VAL B CB  
2454 C CG1 . VAL B 131 ? 0.47675 0.51108 0.41027 -0.03134 -0.03680 -0.02972 1050 VAL B CG1 
2455 C CG2 . VAL B 131 ? 0.44069 0.47408 0.33967 -0.01958 -0.01113 -0.02729 1050 VAL B CG2 
2456 N N   . TYR B 132 ? 0.29791 0.37662 0.29847 -0.03274 -0.02178 -0.00742 1051 TYR B N   
2457 C CA  . TYR B 132 ? 0.28726 0.37549 0.31412 -0.03538 -0.02652 -0.00280 1051 TYR B CA  
2458 C C   . TYR B 132 ? 0.28389 0.37872 0.32795 -0.03416 -0.01721 -0.00354 1051 TYR B C   
2459 O O   . TYR B 132 ? 0.28129 0.37825 0.34019 -0.03542 -0.01938 -0.00414 1051 TYR B O   
2460 C CB  . TYR B 132 ? 0.30490 0.39738 0.33468 -0.03474 -0.02847 0.00621  1051 TYR B CB  
2461 C CG  . TYR B 132 ? 0.28576 0.38744 0.33895 -0.03486 -0.03448 0.01172  1051 TYR B CG  
2462 C CD1 . TYR B 132 ? 0.26829 0.37606 0.34105 -0.03400 -0.02732 0.01253  1051 TYR B CD1 
2463 C CD2 . TYR B 132 ? 0.29459 0.39986 0.34959 -0.03452 -0.04677 0.01694  1051 TYR B CD2 
2464 C CE1 . TYR B 132 ? 0.27557 0.39218 0.36879 -0.03211 -0.02952 0.01814  1051 TYR B CE1 
2465 C CE2 . TYR B 132 ? 0.33581 0.45379 0.41658 -0.03263 -0.05033 0.02330  1051 TYR B CE2 
2466 C CZ  . TYR B 132 ? 0.27304 0.39629 0.37253 -0.03105 -0.04017 0.02376  1051 TYR B CZ  
2467 O OH  . TYR B 132 ? 0.28609 0.42234 0.41020 -0.02739 -0.04077 0.03039  1051 TYR B OH  
2468 N N   . LEU B 133 ? 0.27640 0.37499 0.31846 -0.03236 -0.00719 -0.00279 1052 LEU B N   
2469 C CA  . LEU B 133 ? 0.25101 0.35701 0.30826 -0.03164 -0.00131 -0.00325 1052 LEU B CA  
2470 C C   . LEU B 133 ? 0.27006 0.37392 0.32821 -0.02820 -0.00054 -0.00899 1052 LEU B C   
2471 O O   . LEU B 133 ? 0.25554 0.36116 0.32511 -0.02759 -0.00095 -0.00869 1052 LEU B O   
2472 C CB  . LEU B 133 ? 0.24115 0.35384 0.29900 -0.03286 0.00690  -0.00080 1052 LEU B CB  
2473 C CG  . LEU B 133 ? 0.21789 0.33968 0.29034 -0.03352 0.01009  -0.00142 1052 LEU B CG  
2474 C CD1 . LEU B 133 ? 0.23861 0.35669 0.31872 -0.03419 0.00590  -0.00018 1052 LEU B CD1 
2475 C CD2 . LEU B 133 ? 0.25940 0.38816 0.33463 -0.03850 0.01609  0.00178  1052 LEU B CD2 
2476 N N   . ALA B 134 ? 0.26533 0.36223 0.30841 -0.02477 0.00113  -0.01399 1053 ALA B N   
2477 C CA  . ALA B 134 ? 0.25704 0.34635 0.29860 -0.01978 0.00185  -0.01950 1053 ALA B CA  
2478 C C   . ALA B 134 ? 0.31644 0.39558 0.36299 -0.02411 -0.00689 -0.01989 1053 ALA B C   
2479 O O   . ALA B 134 ? 0.29696 0.37268 0.35093 -0.02192 -0.00593 -0.01998 1053 ALA B O   
2480 C CB  . ALA B 134 ? 0.32288 0.40100 0.34237 -0.01401 0.00577  -0.02593 1053 ALA B CB  
2481 N N   . ALA B 135 ? 0.29350 0.36891 0.33733 -0.03051 -0.01562 -0.01888 1054 ALA B N   
2482 C CA  . ALA B 135 ? 0.29063 0.36104 0.34496 -0.03686 -0.02370 -0.01783 1054 ALA B CA  
2483 C C   . ALA B 135 ? 0.26388 0.34620 0.33977 -0.03758 -0.01981 -0.01077 1054 ALA B C   
2484 O O   . ALA B 135 ? 0.28595 0.36385 0.37100 -0.04039 -0.02047 -0.00907 1054 ALA B O   
2485 C CB  . ALA B 135 ? 0.31348 0.38382 0.36547 -0.04374 -0.03561 -0.01698 1054 ALA B CB  
2486 N N   . VAL B 136 ? 0.25447 0.34900 0.33617 -0.03559 -0.01558 -0.00636 1055 VAL B N   
2487 C CA  . VAL B 136 ? 0.24060 0.34262 0.33627 -0.03472 -0.01089 -0.00108 1055 VAL B CA  
2488 C C   . VAL B 136 ? 0.23579 0.33480 0.32964 -0.03063 -0.00557 -0.00252 1055 VAL B C   
2489 O O   . VAL B 136 ? 0.25039 0.34748 0.35033 -0.03058 -0.00348 0.00078  1055 VAL B O   
2490 C CB  . VAL B 136 ? 0.21338 0.32238 0.31024 -0.03320 -0.00811 0.00227  1055 VAL B CB  
2491 C CG1 . VAL B 136 ? 0.20896 0.32034 0.31285 -0.03078 -0.00218 0.00538  1055 VAL B CG1 
2492 C CG2 . VAL B 136 ? 0.23709 0.34968 0.33861 -0.03504 -0.01423 0.00627  1055 VAL B CG2 
2493 N N   . LEU B 137 ? 0.22511 0.32496 0.31109 -0.02657 -0.00305 -0.00633 1056 LEU B N   
2494 C CA  . LEU B 137 ? 0.24385 0.34400 0.33015 -0.02112 -0.00009 -0.00686 1056 LEU B CA  
2495 C C   . LEU B 137 ? 0.28602 0.37204 0.36912 -0.01922 -0.00146 -0.00767 1056 LEU B C   
2496 O O   . LEU B 137 ? 0.28409 0.36655 0.36851 -0.01614 -0.00014 -0.00447 1056 LEU B O   
2497 C CB  . LEU B 137 ? 0.26866 0.37763 0.35294 -0.01676 0.00304  -0.00975 1056 LEU B CB  
2498 C CG  . LEU B 137 ? 0.23580 0.35667 0.32399 -0.02086 0.00478  -0.00802 1056 LEU B CG  
2499 C CD1 . LEU B 137 ? 0.29725 0.42987 0.38749 -0.01796 0.00939  -0.00958 1056 LEU B CD1 
2500 C CD2 . LEU B 137 ? 0.25510 0.37904 0.34824 -0.02250 0.00341  -0.00554 1056 LEU B CD2 
2501 N N   . GLU B 138 ? 0.28696 0.36143 0.36273 -0.02139 -0.00470 -0.01187 1057 GLU B N   
2502 C CA  . GLU B 138 ? 0.35654 0.41173 0.42757 -0.02151 -0.00670 -0.01318 1057 GLU B CA  
2503 C C   . GLU B 138 ? 0.33245 0.38551 0.41467 -0.02925 -0.00812 -0.00658 1057 GLU B C   
2504 O O   . GLU B 138 ? 0.31735 0.35780 0.39875 -0.02825 -0.00627 -0.00338 1057 GLU B O   
2505 C CB  . GLU B 138 ? 0.29065 0.33010 0.34749 -0.02367 -0.01138 -0.02073 1057 GLU B CB  
2506 C CG  . GLU B 138 ? 0.37047 0.38469 0.42158 -0.02693 -0.01503 -0.02262 1057 GLU B CG  
2507 C CD  . GLU B 138 ? 0.50687 0.49839 0.53612 -0.02536 -0.01855 -0.03273 1057 GLU B CD  
2508 O OE1 . GLU B 138 ? 0.54234 0.53902 0.55998 -0.01729 -0.01430 -0.03749 1057 GLU B OE1 
2509 O OE2 . GLU B 138 ? 0.51474 0.48154 0.53691 -0.03232 -0.02479 -0.03595 1057 GLU B OE2 
2510 N N   . TYR B 139 ? 0.27942 0.34464 0.37265 -0.03632 -0.01050 -0.00339 1058 TYR B N   
2511 C CA  . TYR B 139 ? 0.26528 0.33366 0.37357 -0.04294 -0.00939 0.00411  1058 TYR B CA  
2512 C C   . TYR B 139 ? 0.26590 0.33664 0.37460 -0.03725 -0.00079 0.01004  1058 TYR B C   
2513 O O   . TYR B 139 ? 0.28956 0.35186 0.40091 -0.03953 0.00288  0.01585  1058 TYR B O   
2514 C CB  . TYR B 139 ? 0.24577 0.33133 0.36829 -0.04773 -0.01249 0.00722  1058 TYR B CB  
2515 C CG  . TYR B 139 ? 0.23476 0.33152 0.37593 -0.05003 -0.00622 0.01654  1058 TYR B CG  
2516 C CD1 . TYR B 139 ? 0.27852 0.37254 0.43321 -0.05883 -0.00659 0.02171  1058 TYR B CD1 
2517 C CD2 . TYR B 139 ? 0.24805 0.35619 0.39202 -0.04338 0.00137  0.02019  1058 TYR B CD2 
2518 C CE1 . TYR B 139 ? 0.30054 0.40707 0.47368 -0.06038 0.00230  0.03165  1058 TYR B CE1 
2519 C CE2 . TYR B 139 ? 0.27113 0.38839 0.42949 -0.04308 0.01006  0.02862  1058 TYR B CE2 
2520 C CZ  . TYR B 139 ? 0.26391 0.38236 0.43789 -0.05125 0.01136  0.03489  1058 TYR B CZ  
2521 O OH  . TYR B 139 ? 0.29045 0.42040 0.48053 -0.05079 0.02281  0.04471  1058 TYR B OH  
2522 N N   . LEU B 140 ? 0.23894 0.31900 0.34268 -0.03060 0.00206  0.00882  1059 LEU B N   
2523 C CA  . LEU B 140 ? 0.26015 0.34052 0.35900 -0.02532 0.00786  0.01308  1059 LEU B CA  
2524 C C   . LEU B 140 ? 0.30399 0.37169 0.39236 -0.01977 0.00761  0.01357  1059 LEU B C   
2525 O O   . LEU B 140 ? 0.30561 0.36591 0.38875 -0.01768 0.01181  0.01994  1059 LEU B O   
2526 C CB  . LEU B 140 ? 0.28847 0.37884 0.38311 -0.02169 0.00814  0.01015  1059 LEU B CB  
2527 C CG  . LEU B 140 ? 0.25107 0.34956 0.35324 -0.02438 0.01001  0.01138  1059 LEU B CG  
2528 C CD1 . LEU B 140 ? 0.24922 0.35115 0.34453 -0.02246 0.00920  0.00755  1059 LEU B CD1 
2529 C CD2 . LEU B 140 ? 0.28134 0.37977 0.38737 -0.02341 0.01767  0.01799  1059 LEU B CD2 
2530 N N   . THR B 141 ? 0.27271 0.33709 0.35660 -0.01583 0.00369  0.00770  1060 THR B N   
2531 C CA  . THR B 141 ? 0.29060 0.34267 0.36580 -0.00756 0.00331  0.00844  1060 THR B CA  
2532 C C   . THR B 141 ? 0.33089 0.36128 0.40335 -0.01131 0.00469  0.01316  1060 THR B C   
2533 O O   . THR B 141 ? 0.32177 0.34067 0.38654 -0.00627 0.00694  0.01960  1060 THR B O   
2534 C CB  . THR B 141 ? 0.31301 0.36628 0.38586 -0.00143 0.00130  0.00110  1060 THR B CB  
2535 O OG1 . THR B 141 ? 0.31253 0.38741 0.39054 0.00048  0.00112  -0.00109 1060 THR B OG1 
2536 C CG2 . THR B 141 ? 0.34413 0.38352 0.40941 0.01013  0.00145  0.00197  1060 THR B CG2 
2537 N N   . ALA B 142 ? 0.31526 0.33893 0.39336 -0.02118 0.00244  0.01069  1061 ALA B N   
2538 C CA  . ALA B 142 ? 0.33870 0.34123 0.41714 -0.02864 0.00280  0.01523  1061 ALA B CA  
2539 C C   . ALA B 142 ? 0.34244 0.34937 0.42776 -0.03284 0.00990  0.02661  1061 ALA B C   
2540 O O   . ALA B 142 ? 0.39675 0.38493 0.47645 -0.03362 0.01370  0.03398  1061 ALA B O   
2541 C CB  . ALA B 142 ? 0.34803 0.34654 0.43339 -0.04101 -0.00388 0.00991  1061 ALA B CB  
2542 N N   . GLU B 143 ? 0.31619 0.34555 0.41168 -0.03464 0.01313  0.02869  1062 GLU B N   
2543 C CA  . GLU B 143 ? 0.31713 0.35146 0.41754 -0.03677 0.02271  0.03919  1062 GLU B CA  
2544 C C   . GLU B 143 ? 0.36343 0.38774 0.44362 -0.02623 0.02749  0.04419  1062 GLU B C   
2545 O O   . GLU B 143 ? 0.37083 0.38258 0.44543 -0.02738 0.03487  0.05423  1062 GLU B O   
2546 C CB  . GLU B 143 ? 0.36216 0.41989 0.47458 -0.03733 0.02560  0.03877  1062 GLU B CB  
2547 C CG  . GLU B 143 ? 0.38728 0.45251 0.50915 -0.03968 0.03754  0.04930  1062 GLU B CG  
2548 C CD  . GLU B 143 ? 0.38925 0.45948 0.53646 -0.05305 0.03848  0.05579  1062 GLU B CD  
2549 O OE1 . GLU B 143 ? 0.39589 0.46266 0.55176 -0.06163 0.02731  0.05047  1062 GLU B OE1 
2550 O OE2 . GLU B 143 ? 0.36989 0.44804 0.52833 -0.05540 0.05059  0.06637  1062 GLU B OE2 
2551 N N   . ILE B 144 ? 0.33782 0.36800 0.40688 -0.01655 0.02276  0.03809  1063 ILE B N   
2552 C CA  . ILE B 144 ? 0.32633 0.34960 0.37577 -0.00633 0.02336  0.04219  1063 ILE B CA  
2553 C C   . ILE B 144 ? 0.35588 0.35637 0.39566 -0.00205 0.02206  0.04726  1063 ILE B C   
2554 O O   . ILE B 144 ? 0.38845 0.37501 0.41315 0.00187  0.02672  0.05706  1063 ILE B O   
2555 C CB  . ILE B 144 ? 0.33643 0.37406 0.38201 0.00060  0.01563  0.03403  1063 ILE B CB  
2556 C CG1 . ILE B 144 ? 0.33754 0.39063 0.38852 -0.00364 0.01773  0.03003  1063 ILE B CG1 
2557 C CG2 . ILE B 144 ? 0.34898 0.38139 0.37561 0.01092  0.01192  0.03789  1063 ILE B CG2 
2558 C CD1 . ILE B 144 ? 0.33837 0.40551 0.39283 -0.00219 0.01011  0.02130  1063 ILE B CD1 
2559 N N   . LEU B 145 ? 0.32831 0.32128 0.37339 -0.00178 0.01646  0.04097  1064 LEU B N   
2560 C CA  . LEU B 145 ? 0.37077 0.33745 0.40468 0.00468  0.01525  0.04477  1064 LEU B CA  
2561 C C   . LEU B 145 ? 0.39994 0.34378 0.43326 -0.00565 0.02177  0.05424  1064 LEU B C   
2562 O O   . LEU B 145 ? 0.41822 0.33824 0.43675 -0.00027 0.02431  0.06338  1064 LEU B O   
2563 C CB  . LEU B 145 ? 0.37694 0.33822 0.41385 0.00859  0.00960  0.03435  1064 LEU B CB  
2564 C CG  . LEU B 145 ? 0.39779 0.38033 0.43659 0.02060  0.00495  0.02743  1064 LEU B CG  
2565 C CD1 . LEU B 145 ? 0.36959 0.34574 0.41011 0.02384  0.00328  0.01735  1064 LEU B CD1 
2566 C CD2 . LEU B 145 ? 0.38424 0.36458 0.41282 0.03590  0.00233  0.03394  1064 LEU B CD2 
2567 N N   . GLU B 146 ? 0.35466 0.30591 0.40531 -0.02090 0.02421  0.05339  1065 GLU B N   
2568 C CA  . GLU B 146 ? 0.41584 0.35102 0.47213 -0.03364 0.03104  0.06392  1065 GLU B CA  
2569 C C   . GLU B 146 ? 0.46069 0.39451 0.50559 -0.02962 0.04214  0.07783  1065 GLU B C   
2570 O O   . GLU B 146 ? 0.45736 0.36517 0.49033 -0.03023 0.04747  0.08888  1065 GLU B O   
2571 C CB  . GLU B 146 ? 0.45631 0.41017 0.53883 -0.04999 0.03081  0.06180  1065 GLU B CB  
2572 C CG  . GLU B 146 ? 0.52539 0.47065 0.62182 -0.06577 0.03830  0.07390  1065 GLU B CG  
2573 C CD  . GLU B 146 ? 0.72787 0.69749 0.85583 -0.08162 0.03559  0.07235  1065 GLU B CD  
2574 O OE1 . GLU B 146 ? 0.61996 0.60967 0.75471 -0.07903 0.02771  0.06197  1065 GLU B OE1 
2575 O OE2 . GLU B 146 ? 0.76708 0.73684 0.91428 -0.09683 0.04112  0.08263  1065 GLU B OE2 
2576 N N   . LEU B 147 ? 0.41368 0.37197 0.45868 -0.02523 0.04624  0.07753  1066 LEU B N   
2577 C CA  . LEU B 147 ? 0.43368 0.38962 0.46240 -0.02047 0.05771  0.08940  1066 LEU B CA  
2578 C C   . LEU B 147 ? 0.47594 0.41291 0.47435 -0.00574 0.05350  0.09319  1066 LEU B C   
2579 O O   . LEU B 147 ? 0.47616 0.39459 0.45581 -0.00330 0.06189  0.10652  1066 LEU B O   
2580 C CB  . LEU B 147 ? 0.45059 0.43255 0.48221 -0.01776 0.06217  0.08551  1066 LEU B CB  
2581 C CG  . LEU B 147 ? 0.45854 0.46189 0.52110 -0.02953 0.06785  0.08492  1066 LEU B CG  
2582 C CD1 . LEU B 147 ? 0.44510 0.46949 0.50748 -0.02323 0.06983  0.07847  1066 LEU B CD1 
2583 C CD2 . LEU B 147 ? 0.49808 0.49829 0.57063 -0.03853 0.08316  0.09988  1066 LEU B CD2 
2584 N N   . ALA B 148 ? 0.43861 0.38153 0.43255 0.00456  0.04077  0.08292  1067 ALA B N   
2585 C CA  . ALA B 148 ? 0.48683 0.41687 0.45631 0.01980  0.03441  0.08718  1067 ALA B CA  
2586 C C   . ALA B 148 ? 0.47738 0.37449 0.43834 0.02224  0.03533  0.09609  1067 ALA B C   
2587 O O   . ALA B 148 ? 0.49042 0.36857 0.42701 0.03195  0.03631  0.10762  1067 ALA B O   
2588 C CB  . ALA B 148 ? 0.42432 0.37341 0.39882 0.02916  0.02107  0.07508  1067 ALA B CB  
2589 N N   . GLY B 149 ? 0.47323 0.35972 0.45059 0.01412  0.03409  0.09072  1068 GLY B N   
2590 C CA  . GLY B 149 ? 0.47502 0.32378 0.44280 0.01507  0.03514  0.09798  1068 GLY B CA  
2591 C C   . GLY B 149 ? 0.55491 0.38304 0.51538 0.00431  0.04776  0.11440  1068 GLY B C   
2592 O O   . GLY B 149 ? 0.56630 0.36065 0.50734 0.00973  0.05022  0.12615  1068 GLY B O   
2593 N N   . ASN B 150 ? 0.52318 0.37122 0.50048 -0.01072 0.05692  0.11645  1069 ASN B N   
2594 C CA  . ASN B 150 ? 0.54484 0.38092 0.51753 -0.02023 0.07232  0.13381  1069 ASN B CA  
2595 C C   . ASN B 150 ? 0.52263 0.35153 0.46149 -0.00504 0.07756  0.14535  1069 ASN B C   
2596 O O   . ASN B 150 ? 0.64986 0.45034 0.56947 -0.00505 0.08665  0.16183  1069 ASN B O   
2597 C CB  . ASN B 150 ? 0.56812 0.43513 0.56853 -0.03528 0.08190  0.13360  1069 ASN B CB  
2598 C CG  . ASN B 150 ? 0.55076 0.42451 0.58409 -0.05260 0.07577  0.12492  1069 ASN B CG  
2599 O OD1 . ASN B 150 ? 0.59286 0.44091 0.62537 -0.05656 0.06708  0.12056  1069 ASN B OD1 
2600 N ND2 . ASN B 150 ? 0.59467 0.50169 0.65537 -0.06215 0.07974  0.12228  1069 ASN B ND2 
2601 N N   . ALA B 151 ? 0.54438 0.39696 0.47351 0.00712  0.07139  0.13720  1070 ALA B N   
2602 C CA  . ALA B 151 ? 0.59222 0.43722 0.48498 0.02158  0.07268  0.14624  1070 ALA B CA  
2603 C C   . ALA B 151 ? 0.58631 0.40244 0.45612 0.03592  0.06282  0.15298  1070 ALA B C   
2604 O O   . ALA B 151 ? 0.65634 0.44896 0.49464 0.04325  0.06823  0.16872  1070 ALA B O   
2605 C CB  . ALA B 151 ? 0.54733 0.42160 0.43555 0.02943  0.06457  0.13367  1070 ALA B CB  
2606 N N   . ALA B 152 ? 0.53331 0.34924 0.41736 0.04133  0.04945  0.14228  1071 ALA B N   
2607 C CA  . ALA B 152 ? 0.56089 0.34930 0.42645 0.05755  0.04090  0.14898  1071 ALA B CA  
2608 C C   . ALA B 152 ? 0.65834 0.40341 0.51152 0.05154  0.05190  0.16538  1071 ALA B C   
2609 O O   . ALA B 152 ? 0.70814 0.42626 0.53089 0.06383  0.05224  0.18064  1071 ALA B O   
2610 C CB  . ALA B 152 ? 0.59320 0.38917 0.47927 0.06427  0.02871  0.13409  1071 ALA B CB  
2611 N N   . ARG B 153 ? 0.64939 0.38662 0.52545 0.03165  0.06020  0.16325  1072 ARG B N   
2612 C CA  . ARG B 153 ? 0.72778 0.42282 0.59627 0.02135  0.07052  0.17843  1072 ARG B CA  
2613 C C   . ARG B 153 ? 0.72718 0.41345 0.57296 0.01863  0.08610  0.19895  1072 ARG B C   
2614 O O   . ARG B 153 ? 0.79671 0.44323 0.61692 0.02278  0.09160  0.21643  1072 ARG B O   
2615 C CB  . ARG B 153 ? 0.73251 0.42841 0.63402 -0.00280 0.07394  0.17054  1072 ARG B CB  
2616 C CG  . ARG B 153 ? 0.81115 0.46251 0.71021 -0.01842 0.08287  0.18443  1072 ARG B CG  
2617 C CD  . ARG B 153 ? 0.88769 0.55226 0.82350 -0.04572 0.08525  0.17724  1072 ARG B CD  
2618 N NE  . ARG B 153 ? 0.86631 0.57686 0.82240 -0.05460 0.09476  0.17882  1072 ARG B NE  
2619 C CZ  . ARG B 153 ? 0.85319 0.59853 0.84272 -0.06752 0.09102  0.16611  1072 ARG B CZ  
2620 N NH1 . ARG B 153 ? 0.91096 0.65133 0.91546 -0.07456 0.07734  0.15030  1072 ARG B NH1 
2621 N NH2 . ARG B 153 ? 0.83358 0.61794 0.83905 -0.07179 0.10127  0.16933  1072 ARG B NH2 
2622 N N   . ASP B 154 ? 0.73552 0.45596 0.58756 0.01287  0.09459  0.19768  1073 ASP B N   
2623 C CA  . ASP B 154 ? 0.80434 0.51795 0.63128 0.01224  0.11200  0.21638  1073 ASP B CA  
2624 C C   . ASP B 154 ? 0.79055 0.48715 0.57083 0.03536  0.10517  0.22528  1073 ASP B C   
2625 O O   . ASP B 154 ? 0.89620 0.56856 0.64444 0.03783  0.11808  0.24505  1073 ASP B O   
2626 C CB  . ASP B 154 ? 0.83572 0.58987 0.67840 0.00492  0.12204  0.21010  1073 ASP B CB  
2627 C CG  . ASP B 154 ? 0.86824 0.63761 0.75483 -0.01882 0.13290  0.20914  1073 ASP B CG  
2628 O OD1 . ASP B 154 ? 0.89633 0.64102 0.79688 -0.03227 0.13398  0.21531  1073 ASP B OD1 
2629 O OD2 . ASP B 154 ? 0.85791 0.66337 0.76559 -0.02371 0.13831  0.20136  1073 ASP B OD2 
2630 N N   . ASN B 155 ? 0.83057 0.54095 0.60702 0.05206  0.08479  0.21182  1074 ASN B N   
2631 C CA  . ASN B 155 ? 0.78652 0.48653 0.52438 0.07474  0.07234  0.21829  1074 ASN B CA  
2632 C C   . ASN B 155 ? 0.80819 0.46981 0.53430 0.08678  0.06464  0.22824  1074 ASN B C   
2633 O O   . ASN B 155 ? 0.85952 0.51329 0.55831 0.10802  0.05100  0.23398  1074 ASN B O   
2634 C CB  . ASN B 155 ? 0.75346 0.49246 0.50009 0.08481  0.05356  0.19913  1074 ASN B CB  
2635 C CG  . ASN B 155 ? 0.89808 0.63562 0.60576 0.10528  0.03907  0.20486  1074 ASN B CG  
2636 O OD1 . ASN B 155 ? 0.72406 0.48236 0.43975 0.11736  0.01891  0.19427  1074 ASN B OD1 
2637 N ND2 . ASN B 155 ? 0.85477 0.56875 0.52038 0.10895  0.04900  0.22231  1074 ASN B ND2 
2638 N N   . LYS B 156 ? 0.82508 0.46058 0.56996 0.07368  0.07274  0.23104  1075 LYS B N   
2639 C CA  . LYS B 156 ? 0.81784 0.40891 0.55154 0.08380  0.06776  0.23973  1075 LYS B CA  
2640 C C   . LYS B 156 ? 0.83198 0.43413 0.57330 0.10552  0.04712  0.22632  1075 LYS B C   
2641 O O   . LYS B 156 ? 0.86900 0.44423 0.58828 0.12660  0.03871  0.23631  1075 LYS B O   
2642 C CB  . LYS B 156 ? 0.89371 0.45750 0.59099 0.09068  0.07160  0.25947  1075 LYS B CB  
2643 C CG  . LYS B 156 ? 0.97324 0.53372 0.66742 0.06902  0.09194  0.27100  1075 LYS B CG  
2644 C CD  . LYS B 156 ? 1.21621 0.75007 0.93393 0.04718  0.10131  0.27399  1075 LYS B CD  
2645 C CE  . LYS B 156 ? 1.32310 0.85383 1.03650 0.02872  0.11963  0.28869  1075 LYS B CE  
2646 N NZ  . LYS B 156 ? 1.41510 0.91336 1.09531 0.03761  0.11946  0.30549  1075 LYS B NZ  
2647 N N   . LYS B 157 ? 0.79482 0.43676 0.56876 0.10088  0.04000  0.20480  1076 LYS B N   
2648 C CA  . LYS B 157 ? 0.78181 0.44136 0.57027 0.11877  0.02368  0.19098  1076 LYS B CA  
2649 C C   . LYS B 157 ? 0.75235 0.40874 0.57085 0.10777  0.02540  0.17478  1076 LYS B C   
2650 O O   . LYS B 157 ? 0.77263 0.43355 0.60804 0.08434  0.03466  0.16923  1076 LYS B O   
2651 C CB  . LYS B 157 ? 0.70737 0.41955 0.50466 0.12386  0.01275  0.17965  1076 LYS B CB  
2652 C CG  . LYS B 157 ? 0.70831 0.42502 0.47181 0.13511  0.00729  0.19245  1076 LYS B CG  
2653 C CD  . LYS B 157 ? 0.80080 0.49815 0.54116 0.16127  -0.00583 0.20531  1076 LYS B CD  
2654 C CE  . LYS B 157 ? 0.80409 0.51022 0.50918 0.17045  -0.01425 0.21553  1076 LYS B CE  
2655 N NZ  . LYS B 157 ? 0.91034 0.59822 0.59190 0.19421  -0.02777 0.22972  1076 LYS B NZ  
2656 N N   . THR B 158 ? 0.76034 0.40859 0.58441 0.12571  0.01643  0.16753  1077 THR B N   
2657 C CA  . THR B 158 ? 0.68951 0.33506 0.53626 0.11924  0.01675  0.14991  1077 THR B CA  
2658 C C   . THR B 158 ? 0.68112 0.37705 0.55277 0.12572  0.00833  0.13205  1077 THR B C   
2659 O O   . THR B 158 ? 0.68559 0.38056 0.57194 0.12499  0.00822  0.11740  1077 THR B O   
2660 C CB  . THR B 158 ? 0.75615 0.35076 0.58971 0.13407  0.01649  0.15278  1077 THR B CB  
2661 O OG1 . THR B 158 ? 0.82896 0.43185 0.65634 0.16548  0.00669  0.15668  1077 THR B OG1 
2662 C CG2 . THR B 158 ? 0.91568 0.45558 0.72516 0.12403  0.02576  0.17097  1077 THR B CG2 
2663 N N   . ARG B 159 ? 0.61073 0.34812 0.48523 0.13120  0.00150  0.13295  1078 ARG B N   
2664 C CA  . ARG B 159 ? 0.56262 0.34863 0.46207 0.13331  -0.00563 0.11758  1078 ARG B CA  
2665 C C   . ARG B 159 ? 0.57468 0.39412 0.47552 0.12024  -0.00644 0.11702  1078 ARG B C   
2666 O O   . ARG B 159 ? 0.61126 0.42259 0.48956 0.12036  -0.00570 0.12975  1078 ARG B O   
2667 C CB  . ARG B 159 ? 0.67283 0.47611 0.57747 0.16046  -0.01714 0.11810  1078 ARG B CB  
2668 C CG  . ARG B 159 ? 0.71096 0.54132 0.60667 0.16984  -0.02901 0.12720  1078 ARG B CG  
2669 C CD  . ARG B 159 ? 0.58410 0.43003 0.48703 0.19786  -0.04198 0.13135  1078 ARG B CD  
2670 N NE  . ARG B 159 ? 0.70507 0.55210 0.58517 0.20951  -0.05393 0.14652  1078 ARG B NE  
2671 C CZ  . ARG B 159 ? 0.69187 0.57066 0.58168 0.22868  -0.07060 0.14991  1078 ARG B CZ  
2672 N NH1 . ARG B 159 ? 0.64951 0.56626 0.57540 0.23753  -0.07535 0.13970  1078 ARG B NH1 
2673 N NH2 . ARG B 159 ? 0.70815 0.58147 0.57109 0.23919  -0.08278 0.16466  1078 ARG B NH2 
2674 N N   . ILE B 160 ? 0.48702 0.34007 0.41107 0.10951  -0.00694 0.10233  1079 ILE B N   
2675 C CA  . ILE B 160 ? 0.45782 0.34222 0.38442 0.09874  -0.00819 0.09912  1079 ILE B CA  
2676 C C   . ILE B 160 ? 0.54666 0.45976 0.47215 0.11325  -0.02240 0.09924  1079 ILE B C   
2677 O O   . ILE B 160 ? 0.48212 0.41586 0.42681 0.12403  -0.02993 0.09255  1079 ILE B O   
2678 C CB  . ILE B 160 ? 0.46713 0.37381 0.41831 0.08279  -0.00425 0.08433  1079 ILE B CB  
2679 C CG1 . ILE B 160 ? 0.46895 0.35229 0.42243 0.06556  0.00718  0.08520  1079 ILE B CG1 
2680 C CG2 . ILE B 160 ? 0.46307 0.40316 0.41834 0.07600  -0.00767 0.07909  1079 ILE B CG2 
2681 C CD1 . ILE B 160 ? 0.46346 0.35868 0.43930 0.05505  0.00798  0.07074  1079 ILE B CD1 
2682 N N   . ILE B 161 ? 0.46791 0.38290 0.37081 0.11338  -0.02612 0.10694  1080 ILE B N   
2683 C CA  . ILE B 161 ? 0.46736 0.41019 0.36707 0.12347  -0.04273 0.10622  1080 ILE B CA  
2684 C C   . ILE B 161 ? 0.51037 0.47355 0.40718 0.10877  -0.04304 0.09795  1080 ILE B C   
2685 O O   . ILE B 161 ? 0.48582 0.43939 0.38052 0.09444  -0.02908 0.09582  1080 ILE B O   
2686 C CB  . ILE B 161 ? 0.54396 0.46671 0.41241 0.14011  -0.05105 0.12228  1080 ILE B CB  
2687 C CG1 . ILE B 161 ? 0.57584 0.47143 0.40720 0.13236  -0.04114 0.13260  1080 ILE B CG1 
2688 C CG2 . ILE B 161 ? 0.58476 0.48362 0.45668 0.15628  -0.04995 0.13022  1080 ILE B CG2 
2689 C CD1 . ILE B 161 ? 0.62409 0.49793 0.41806 0.14872  -0.04950 0.14949  1080 ILE B CD1 
2690 N N   . PRO B 162 ? 0.47611 0.46716 0.37433 0.11134  -0.05872 0.09284  1081 PRO B N   
2691 C CA  . PRO B 162 ? 0.48248 0.48797 0.37832 0.09646  -0.05813 0.08263  1081 PRO B CA  
2692 C C   . PRO B 162 ? 0.46542 0.44580 0.32787 0.08965  -0.04571 0.08769  1081 PRO B C   
2693 O O   . PRO B 162 ? 0.53358 0.51701 0.40248 0.07674  -0.03466 0.08021  1081 PRO B O   
2694 C CB  . PRO B 162 ? 0.53754 0.56920 0.43300 0.10153  -0.08012 0.07924  1081 PRO B CB  
2695 C CG  . PRO B 162 ? 0.52968 0.57889 0.45347 0.11519  -0.08867 0.08202  1081 PRO B CG  
2696 C CD  . PRO B 162 ? 0.48728 0.50302 0.39935 0.12585  -0.07739 0.09361  1081 PRO B CD  
2697 N N   . ARG B 163 ? 0.55257 0.50800 0.38008 0.09891  -0.04537 0.10121  1082 ARG B N   
2698 C CA  . ARG B 163 ? 0.56014 0.49400 0.35525 0.09305  -0.03071 0.10646  1082 ARG B CA  
2699 C C   . ARG B 163 ? 0.62698 0.54930 0.43864 0.08183  -0.00808 0.10888  1082 ARG B C   
2700 O O   . ARG B 163 ? 0.59173 0.51006 0.39338 0.07362  0.00613  0.10831  1082 ARG B O   
2701 C CB  . ARG B 163 ? 0.66226 0.57019 0.41289 0.10569  -0.03402 0.12213  1082 ARG B CB  
2702 C CG  . ARG B 163 ? 0.62896 0.51156 0.37815 0.11378  -0.02742 0.13771  1082 ARG B CG  
2703 C CD  . ARG B 163 ? 0.78988 0.64176 0.48778 0.12347  -0.02507 0.15498  1082 ARG B CD  
2704 N NE  . ARG B 163 ? 0.77953 0.60105 0.47141 0.13114  -0.01833 0.17187  1082 ARG B NE  
2705 C CZ  . ARG B 163 ? 0.87912 0.68792 0.55374 0.14906  -0.03277 0.18325  1082 ARG B CZ  
2706 N NH1 . ARG B 163 ? 0.85468 0.68232 0.51746 0.16120  -0.05658 0.18041  1082 ARG B NH1 
2707 N NH2 . ARG B 163 ? 0.79973 0.57504 0.46859 0.15477  -0.02390 0.19854  1082 ARG B NH2 
2708 N N   . HIS B 164 ? 0.52099 0.43950 0.35941 0.08115  -0.00510 0.11043  1083 HIS B N   
2709 C CA  . HIS B 164 ? 0.51575 0.42739 0.37444 0.06767  0.01222  0.11054  1083 HIS B CA  
2710 C C   . HIS B 164 ? 0.50444 0.44248 0.38953 0.05608  0.01400  0.09571  1083 HIS B C   
2711 O O   . HIS B 164 ? 0.51023 0.44877 0.40198 0.04534  0.02818  0.09604  1083 HIS B O   
2712 C CB  . HIS B 164 ? 0.52387 0.42104 0.40014 0.06950  0.01202  0.11331  1083 HIS B CB  
2713 C CG  . HIS B 164 ? 0.54560 0.41217 0.39669 0.08191  0.01066  0.12876  1083 HIS B CG  
2714 N ND1 . HIS B 164 ? 0.54458 0.39872 0.40355 0.09261  0.00351  0.12999  1083 HIS B ND1 
2715 C CD2 . HIS B 164 ? 0.58444 0.42823 0.40009 0.08700  0.01592  0.14422  1083 HIS B CD2 
2716 C CE1 . HIS B 164 ? 0.58944 0.41357 0.42040 0.10369  0.00363  0.14598  1083 HIS B CE1 
2717 N NE2 . HIS B 164 ? 0.61129 0.42891 0.41482 0.10006  0.01084  0.15530  1083 HIS B NE2 
2718 N N   . LEU B 165 ? 0.46009 0.42113 0.36256 0.05844  0.00030  0.08385  1084 LEU B N   
2719 C CA  . LEU B 165 ? 0.43489 0.41849 0.35898 0.04826  0.00108  0.07087  1084 LEU B CA  
2720 C C   . LEU B 165 ? 0.52878 0.51459 0.43326 0.04502  0.00474  0.06842  1084 LEU B C   
2721 O O   . LEU B 165 ? 0.45851 0.44950 0.37319 0.03631  0.01525  0.06426  1084 LEU B O   
2722 C CB  . LEU B 165 ? 0.53687 0.54377 0.48066 0.05163  -0.01334 0.06092  1084 LEU B CB  
2723 C CG  . LEU B 165 ? 0.51737 0.52611 0.48545 0.05342  -0.01333 0.05840  1084 LEU B CG  
2724 C CD1 . LEU B 165 ? 0.43331 0.46770 0.41831 0.05956  -0.02577 0.05126  1084 LEU B CD1 
2725 C CD2 . LEU B 165 ? 0.45739 0.46858 0.44329 0.04016  -0.00335 0.05231  1084 LEU B CD2 
2726 N N   . GLN B 166 ? 0.52858 0.50950 0.40316 0.05305  -0.00474 0.07058  1085 GLN B N   
2727 C CA  . GLN B 166 ? 0.57573 0.55344 0.42466 0.05114  -0.00226 0.06619  1085 GLN B CA  
2728 C C   . GLN B 166 ? 0.57611 0.53651 0.41011 0.04914  0.01971  0.07477  1085 GLN B C   
2729 O O   . GLN B 166 ? 0.57162 0.53515 0.40617 0.04430  0.03016  0.06916  1085 GLN B O   
2730 C CB  . GLN B 166 ? 0.62872 0.60202 0.44461 0.05987  -0.01951 0.06671  1085 GLN B CB  
2731 C CG  . GLN B 166 ? 0.67563 0.67456 0.51493 0.05940  -0.04089 0.05739  1085 GLN B CG  
2732 C CD  . GLN B 166 ? 0.78546 0.78609 0.60708 0.07051  -0.06106 0.06283  1085 GLN B CD  
2733 O OE1 . GLN B 166 ? 0.81160 0.79063 0.59739 0.07938  -0.06049 0.07351  1085 GLN B OE1 
2734 N NE2 . GLN B 166 ? 0.72948 0.75758 0.57765 0.07044  -0.07885 0.05671  1085 GLN B NE2 
2735 N N   . LEU B 167 ? 0.54557 0.48820 0.36922 0.05286  0.02820  0.08924  1086 LEU B N   
2736 C CA  . LEU B 167 ? 0.64633 0.57574 0.46109 0.04955  0.05118  0.09986  1086 LEU B CA  
2737 C C   . LEU B 167 ? 0.55939 0.50390 0.41530 0.03772  0.06315  0.09671  1086 LEU B C   
2738 O O   . LEU B 167 ? 0.57268 0.52142 0.43004 0.03458  0.07901  0.09734  1086 LEU B O   
2739 C CB  . LEU B 167 ? 0.61656 0.52232 0.41452 0.05396  0.05698  0.11737  1086 LEU B CB  
2740 C CG  . LEU B 167 ? 0.79527 0.68423 0.57256 0.05257  0.08102  0.13209  1086 LEU B CG  
2741 C CD1 . LEU B 167 ? 0.87538 0.75589 0.60650 0.06130  0.08488  0.13090  1086 LEU B CD1 
2742 C CD2 . LEU B 167 ? 0.83222 0.69569 0.59884 0.05418  0.08631  0.15046  1086 LEU B CD2 
2743 N N   . ALA B 168 ? 0.51500 0.46803 0.40366 0.03224  0.05529  0.09309  1087 ALA B N   
2744 C CA  . ALA B 168 ? 0.45954 0.42584 0.38519 0.02057  0.06327  0.09042  1087 ALA B CA  
2745 C C   . ALA B 168 ? 0.51675 0.50280 0.45375 0.01815  0.06344  0.07868  1087 ALA B C   
2746 O O   . ALA B 168 ? 0.49704 0.49216 0.45094 0.01251  0.07650  0.08062  1087 ALA B O   
2747 C CB  . ALA B 168 ? 0.56383 0.53122 0.51371 0.01681  0.05242  0.08638  1087 ALA B CB  
2748 N N   . VAL B 169 ? 0.43886 0.43181 0.36800 0.02240  0.04907  0.06742  1088 VAL B N   
2749 C CA  . VAL B 169 ? 0.41634 0.42241 0.35270 0.01997  0.04866  0.05653  1088 VAL B CA  
2750 C C   . VAL B 169 ? 0.48039 0.47696 0.38994 0.02486  0.06167  0.05839  1088 VAL B C   
2751 O O   . VAL B 169 ? 0.45856 0.46216 0.37990 0.02317  0.07292  0.05646  1088 VAL B O   
2752 C CB  . VAL B 169 ? 0.45866 0.47311 0.39402 0.02109  0.03005  0.04519  1088 VAL B CB  
2753 C CG1 . VAL B 169 ? 0.53104 0.55087 0.46446 0.01865  0.02955  0.03476  1088 VAL B CG1 
2754 C CG2 . VAL B 169 ? 0.43156 0.45798 0.39630 0.01728  0.02177  0.04241  1088 VAL B CG2 
2755 N N   . ARG B 170 ? 0.51458 0.49386 0.38590 0.03250  0.06109  0.06283  1089 ARG B N   
2756 C CA  . ARG B 170 ? 0.54326 0.50941 0.38107 0.03884  0.07360  0.06284  1089 ARG B CA  
2757 C C   . ARG B 170 ? 0.55116 0.51854 0.39961 0.03846  0.09905  0.07417  1089 ARG B C   
2758 O O   . ARG B 170 ? 0.57934 0.54566 0.41929 0.04284  0.11318  0.07164  1089 ARG B O   
2759 C CB  . ARG B 170 ? 0.61356 0.55922 0.40348 0.04726  0.06593  0.06572  1089 ARG B CB  
2760 C CG  . ARG B 170 ? 0.75855 0.68449 0.50672 0.05532  0.08400  0.07034  1089 ARG B CG  
2761 C CD  . ARG B 170 ? 0.87721 0.79613 0.60313 0.05814  0.08163  0.05512  1089 ARG B CD  
2762 N NE  . ARG B 170 ? 1.00152 0.92335 0.72413 0.05436  0.05435  0.04190  1089 ARG B NE  
2763 C CZ  . ARG B 170 ? 1.10613 1.01077 0.78432 0.05837  0.03926  0.03544  1089 ARG B CZ  
2764 N NH1 . ARG B 170 ? 1.17578 1.05532 0.80235 0.06785  0.04838  0.04041  1089 ARG B NH1 
2765 N NH2 . ARG B 170 ? 1.04504 0.95825 0.73008 0.05220  0.01416  0.02409  1089 ARG B NH2 
2766 N N   . ASN B 171 ? 0.51448 0.48420 0.38320 0.03319  0.10557  0.08681  1090 ASN B N   
2767 C CA  . ASN B 171 ? 0.58823 0.56169 0.47058 0.03057  0.12961  0.10013  1090 ASN B CA  
2768 C C   . ASN B 171 ? 0.51570 0.51468 0.44722 0.02212  0.13471  0.09808  1090 ASN B C   
2769 O O   . ASN B 171 ? 0.51372 0.52281 0.46535 0.01882  0.15399  0.10937  1090 ASN B O   
2770 C CB  . ASN B 171 ? 0.58512 0.54684 0.46785 0.02602  0.13370  0.11568  1090 ASN B CB  
2771 C CG  . ASN B 171 ? 0.71872 0.65408 0.54990 0.03609  0.13647  0.12397  1090 ASN B CG  
2772 O OD1 . ASN B 171 ? 0.75524 0.68133 0.54876 0.04598  0.14051  0.11979  1090 ASN B OD1 
2773 N ND2 . ASN B 171 ? 0.74294 0.66268 0.56871 0.03415  0.13363  0.13580  1090 ASN B ND2 
2774 N N   . ASP B 172 ? 0.45736 0.46821 0.40928 0.01841  0.11803  0.08537  1091 ASP B N   
2775 C CA  . ASP B 172 ? 0.41025 0.44425 0.40465 0.01160  0.11932  0.08282  1091 ASP B CA  
2776 C C   . ASP B 172 ? 0.41012 0.44755 0.39676 0.01913  0.11940  0.07178  1091 ASP B C   
2777 O O   . ASP B 172 ? 0.42283 0.45426 0.39606 0.02032  0.10360  0.05994  1091 ASP B O   
2778 C CB  . ASP B 172 ? 0.41278 0.45324 0.43166 0.00208  0.10094  0.07751  1091 ASP B CB  
2779 C CG  . ASP B 172 ? 0.47215 0.53477 0.53244 -0.00620 0.10064  0.07690  1091 ASP B CG  
2780 O OD1 . ASP B 172 ? 0.46975 0.54305 0.53734 -0.00288 0.09810  0.06913  1091 ASP B OD1 
2781 O OD2 . ASP B 172 ? 0.42223 0.48977 0.50659 -0.01648 0.10146  0.08427  1091 ASP B OD2 
2782 N N   . GLU B 173 ? 0.41448 0.46130 0.41090 0.02431  0.13766  0.07620  1092 GLU B N   
2783 C CA  . GLU B 173 ? 0.43845 0.48019 0.41941 0.03431  0.14041  0.06619  1092 GLU B CA  
2784 C C   . GLU B 173 ? 0.37036 0.41928 0.36864 0.02965  0.12204  0.05465  1092 GLU B C   
2785 O O   . GLU B 173 ? 0.42798 0.46231 0.40195 0.03360  0.11380  0.04322  1092 GLU B O   
2786 C CB  . GLU B 173 ? 0.51203 0.56638 0.50845 0.04254  0.16437  0.07406  1092 GLU B CB  
2787 C CG  . GLU B 173 ? 0.64735 0.69232 0.62749 0.05506  0.16899  0.06386  1092 GLU B CG  
2788 C CD  . GLU B 173 ? 0.90284 0.95324 0.88427 0.06880  0.19733  0.07201  1092 GLU B CD  
2789 O OE1 . GLU B 173 ? 0.91988 0.99191 0.93024 0.06580  0.21247  0.08698  1092 GLU B OE1 
2790 O OE2 . GLU B 173 ? 0.97704 1.00861 0.92939 0.08262  0.20527  0.06356  1092 GLU B OE2 
2791 N N   . GLU B 174 ? 0.36702 0.43665 0.40525 0.02049  0.11535  0.05760  1093 GLU B N   
2792 C CA  . GLU B 174 ? 0.34829 0.42383 0.39998 0.01684  0.09988  0.04812  1093 GLU B CA  
2793 C C   . GLU B 174 ? 0.31583 0.38052 0.35054 0.01180  0.08178  0.03953  1093 GLU B C   
2794 O O   . GLU B 174 ? 0.33992 0.39895 0.36524 0.01216  0.07232  0.02993  1093 GLU B O   
2795 C CB  . GLU B 174 ? 0.38284 0.48222 0.47733 0.00894  0.09672  0.05360  1093 GLU B CB  
2796 C CG  . GLU B 174 ? 0.31096 0.42818 0.43007 0.01520  0.11206  0.06153  1093 GLU B CG  
2797 C CD  . GLU B 174 ? 0.27111 0.41531 0.43505 0.00555  0.10784  0.06928  1093 GLU B CD  
2798 O OE1 . GLU B 174 ? 0.31748 0.46204 0.48931 -0.00645 0.09375  0.06768  1093 GLU B OE1 
2799 O OE2 . GLU B 174 ? 0.29238 0.45738 0.48356 0.01057  0.11786  0.07656  1093 GLU B OE2 
2800 N N   . LEU B 175 ? 0.32621 0.38824 0.35874 0.00717  0.07706  0.04355  1094 LEU B N   
2801 C CA  . LEU B 175 ? 0.36324 0.41883 0.38335 0.00494  0.06096  0.03650  1094 LEU B CA  
2802 C C   . LEU B 175 ? 0.33607 0.37629 0.32091 0.01108  0.05759  0.03059  1094 LEU B C   
2803 O O   . LEU B 175 ? 0.37303 0.41303 0.35248 0.00892  0.04373  0.02239  1094 LEU B O   
2804 C CB  . LEU B 175 ? 0.36644 0.41931 0.39034 0.00150  0.05764  0.04282  1094 LEU B CB  
2805 C CG  . LEU B 175 ? 0.35982 0.42331 0.41441 -0.00708 0.05373  0.04425  1094 LEU B CG  
2806 C CD1 . LEU B 175 ? 0.39881 0.45168 0.45251 -0.00992 0.05364  0.05144  1094 LEU B CD1 
2807 C CD2 . LEU B 175 ? 0.33431 0.40489 0.39711 -0.00956 0.04064  0.03440  1094 LEU B CD2 
2808 N N   . ASN B 176 ? 0.35123 0.37873 0.31123 0.01813  0.06988  0.03502  1095 ASN B N   
2809 C CA  . ASN B 176 ? 0.39008 0.39914 0.31046 0.02377  0.06541  0.02831  1095 ASN B CA  
2810 C C   . ASN B 176 ? 0.45192 0.45655 0.36824 0.02336  0.06097  0.01666  1095 ASN B C   
2811 O O   . ASN B 176 ? 0.43678 0.43288 0.33487 0.02084  0.04650  0.00755  1095 ASN B O   
2812 C CB  . ASN B 176 ? 0.45595 0.44976 0.34667 0.03259  0.08250  0.03545  1095 ASN B CB  
2813 C CG  . ASN B 176 ? 0.54098 0.51190 0.38340 0.03828  0.07534  0.02845  1095 ASN B CG  
2814 O OD1 . ASN B 176 ? 0.51250 0.48135 0.34375 0.03569  0.05709  0.02544  1095 ASN B OD1 
2815 N ND2 . ASN B 176 ? 0.64557 0.59928 0.45885 0.04663  0.08884  0.02531  1095 ASN B ND2 
2816 N N   . LYS B 177 ? 0.39713 0.40721 0.33127 0.02555  0.07269  0.01750  1096 LYS B N   
2817 C CA  . LYS B 177 ? 0.40869 0.41110 0.33993 0.02543  0.06866  0.00762  1096 LYS B CA  
2818 C C   . LYS B 177 ? 0.37274 0.38540 0.32207 0.01483  0.05079  0.00216  1096 LYS B C   
2819 O O   . LYS B 177 ? 0.38481 0.38618 0.32025 0.01093  0.04068  -0.00708 1096 LYS B O   
2820 C CB  . LYS B 177 ? 0.36438 0.37401 0.31661 0.03166  0.08393  0.01194  1096 LYS B CB  
2821 C CG  . LYS B 177 ? 0.44967 0.44794 0.38143 0.04457  0.10483  0.01610  1096 LYS B CG  
2822 C CD  . LYS B 177 ? 0.44487 0.45419 0.40214 0.05278  0.11942  0.02073  1096 LYS B CD  
2823 C CE  . LYS B 177 ? 0.49780 0.50401 0.44388 0.06631  0.14378  0.02780  1096 LYS B CE  
2824 N NZ  . LYS B 177 ? 0.55727 0.57488 0.52815 0.07744  0.15821  0.03195  1096 LYS B NZ  
2825 N N   . LEU B 178 ? 0.35519 0.38795 0.33452 0.00954  0.04731  0.00774  1097 LEU B N   
2826 C CA  . LEU B 178 ? 0.34425 0.38790 0.34097 0.00114  0.03402  0.00355  1097 LEU B CA  
2827 C C   . LEU B 178 ? 0.35750 0.40033 0.34196 -0.00269 0.02016  -0.00112 1097 LEU B C   
2828 O O   . LEU B 178 ? 0.37462 0.41972 0.36202 -0.00906 0.01039  -0.00730 1097 LEU B O   
2829 C CB  . LEU B 178 ? 0.29193 0.35322 0.31786 -0.00215 0.03446  0.00979  1097 LEU B CB  
2830 C CG  . LEU B 178 ? 0.30806 0.38031 0.34953 -0.00901 0.02363  0.00631  1097 LEU B CG  
2831 C CD1 . LEU B 178 ? 0.34893 0.41988 0.39499 -0.01138 0.02295  0.00275  1097 LEU B CD1 
2832 C CD2 . LEU B 178 ? 0.33942 0.42259 0.40092 -0.01142 0.02347  0.01110  1097 LEU B CD2 
2833 N N   . LEU B 179 ? 0.35381 0.39443 0.32585 0.00113  0.01913  0.00298  1098 LEU B N   
2834 C CA  . LEU B 179 ? 0.35822 0.40461 0.32654 -0.00034 0.00512  0.00164  1098 LEU B CA  
2835 C C   . LEU B 179 ? 0.52323 0.55563 0.45793 0.00326  -0.00178 -0.00070 1098 LEU B C   
2836 O O   . LEU B 179 ? 0.49745 0.53777 0.43119 0.00208  -0.01631 -0.00198 1098 LEU B O   
2837 C CB  . LEU B 179 ? 0.36221 0.41708 0.34488 0.00228  0.00629  0.00953  1098 LEU B CB  
2838 C CG  . LEU B 179 ? 0.38013 0.44698 0.39186 -0.00196 0.00960  0.01049  1098 LEU B CG  
2839 C CD1 . LEU B 179 ? 0.45195 0.51825 0.47138 0.00042  0.01221  0.01764  1098 LEU B CD1 
2840 C CD2 . LEU B 179 ? 0.35631 0.43633 0.38182 -0.00689 -0.00008 0.00430  1098 LEU B CD2 
2841 N N   . GLY B 180 ? 0.47404 0.48680 0.38066 0.00871  0.00810  -0.00077 1099 GLY B N   
2842 C CA  . GLY B 180 ? 0.55909 0.55491 0.42645 0.01359  0.00222  -0.00208 1099 GLY B CA  
2843 C C   . GLY B 180 ? 0.69349 0.68567 0.54629 0.00720  -0.01731 -0.01271 1099 GLY B C   
2844 O O   . GLY B 180 ? 0.75134 0.73355 0.57359 0.01010  -0.02825 -0.01377 1099 GLY B O   
2845 N N   . GLY B 181 ? 0.68546 0.68452 0.55812 -0.00219 -0.02259 -0.01998 1100 GLY B N   
2846 C CA  . GLY B 181 ? 0.76054 0.75881 0.62700 -0.01218 -0.04143 -0.02952 1100 GLY B CA  
2847 C C   . GLY B 181 ? 0.80249 0.83154 0.70223 -0.01903 -0.05636 -0.02741 1100 GLY B C   
2848 O O   . GLY B 181 ? 0.86617 0.90103 0.76871 -0.02947 -0.07276 -0.03395 1100 GLY B O   
2849 N N   . VAL B 182 ? 0.68590 0.73446 0.61098 -0.01339 -0.05103 -0.01842 1101 VAL B N   
2850 C CA  . VAL B 182 ? 0.71257 0.79074 0.67012 -0.01649 -0.06165 -0.01594 1101 VAL B CA  
2851 C C   . VAL B 182 ? 0.78770 0.87261 0.73347 -0.01083 -0.07750 -0.01291 1101 VAL B C   
2852 O O   . VAL B 182 ? 0.73437 0.80543 0.65633 -0.00029 -0.07415 -0.00703 1101 VAL B O   
2853 C CB  . VAL B 182 ? 0.62744 0.71796 0.61189 -0.01140 -0.04915 -0.00898 1101 VAL B CB  
2854 C CG1 . VAL B 182 ? 0.52861 0.64741 0.54231 -0.01054 -0.05768 -0.00627 1101 VAL B CG1 
2855 C CG2 . VAL B 182 ? 0.53116 0.61774 0.52775 -0.01695 -0.03673 -0.01133 1101 VAL B CG2 
2856 N N   . THR B 183 ? 1.00622 1.11378 0.97002 -0.01784 -0.09488 -0.01562 1102 THR B N   
2857 C CA  . THR B 183 ? 1.16097 1.27941 1.11690 -0.01264 -0.11391 -0.01256 1102 THR B CA  
2858 C C   . THR B 183 ? 1.17503 1.33218 1.17374 -0.01012 -0.12163 -0.00702 1102 THR B C   
2859 O O   . THR B 183 ? 1.06665 1.23136 1.08278 0.00018  -0.11022 -0.00011 1102 THR B O   
2860 C CB  . THR B 183 ? 1.32222 1.43194 1.25483 -0.02384 -0.13327 -0.02188 1102 THR B CB  
2861 O OG1 . THR B 183 ? 1.30120 1.42471 1.26110 -0.04060 -0.13714 -0.02866 1102 THR B OG1 
2862 C CG2 . THR B 183 ? 1.23576 1.30345 1.11809 -0.02189 -0.12524 -0.02746 1102 THR B CG2 
2863 N N   . GLU C 11  ? 1.49979 0.88347 1.35247 0.37858  -0.06831 -0.20274 131  GLU C N   
2864 C CA  . GLU C 11  ? 1.41520 0.79326 1.24796 0.29441  -0.06583 -0.22862 131  GLU C CA  
2865 C C   . GLU C 11  ? 1.47822 0.80769 1.28944 0.21886  -0.09685 -0.20720 131  GLU C C   
2866 O O   . GLU C 11  ? 1.51885 0.82686 1.33785 0.22732  -0.12089 -0.16949 131  GLU C O   
2867 C CB  . GLU C 11  ? 1.38335 0.86065 1.25903 0.27755  -0.03412 -0.22194 131  GLU C CB  
2868 C CG  . GLU C 11  ? 1.42217 0.97030 1.35615 0.27699  -0.03641 -0.16486 131  GLU C CG  
2869 C CD  . GLU C 11  ? 1.40219 1.04103 1.37982 0.28159  -0.00710 -0.15744 131  GLU C CD  
2870 O OE1 . GLU C 11  ? 1.38238 1.05132 1.36756 0.33761  0.02152  -0.17917 131  GLU C OE1 
2871 O OE2 . GLU C 11  ? 1.40170 1.07409 1.39963 0.22919  -0.01585 -0.12981 131  GLU C OE2 
2872 N N   . GLY C 12  ? 1.36122 0.67777 1.14403 0.14889  -0.09475 -0.22901 132  GLY C N   
2873 C CA  . GLY C 12  ? 1.50504 0.78115 1.26003 0.07690  -0.11858 -0.20850 132  GLY C CA  
2874 C C   . GLY C 12  ? 1.44432 0.77496 1.21850 0.03976  -0.11661 -0.17394 132  GLY C C   
2875 O O   . GLY C 12  ? 1.42168 0.77804 1.17780 -0.00877 -0.10231 -0.18444 132  GLY C O   
2876 N N   . TYR C 13  ? 1.39970 0.74785 1.20786 0.06560  -0.13299 -0.13200 133  TYR C N   
2877 C CA  . TYR C 13  ? 1.42346 0.81411 1.24852 0.02759  -0.14258 -0.09551 133  TYR C CA  
2878 C C   . TYR C 13  ? 1.38253 0.72106 1.15099 -0.04439 -0.16317 -0.08782 133  TYR C C   
2879 O O   . TYR C 13  ? 1.50533 0.77778 1.24469 -0.05623 -0.18558 -0.07933 133  TYR C O   
2880 C CB  . TYR C 13  ? 1.35123 0.77413 1.23086 0.06843  -0.16196 -0.04562 133  TYR C CB  
2881 C CG  . TYR C 13  ? 1.36057 0.86578 1.30452 0.13173  -0.13638 -0.03871 133  TYR C CG  
2882 C CD1 . TYR C 13  ? 1.33112 0.90662 1.30708 0.11333  -0.12187 -0.03120 133  TYR C CD1 
2883 C CD2 . TYR C 13  ? 1.38474 0.89310 1.35079 0.21248  -0.12732 -0.03797 133  TYR C CD2 
2884 C CE1 . TYR C 13  ? 1.32050 0.97623 1.35814 0.16775  -0.09756 -0.01805 133  TYR C CE1 
2885 C CE2 . TYR C 13  ? 1.37343 0.96572 1.39622 0.27458  -0.09919 -0.02655 133  TYR C CE2 
2886 C CZ  . TYR C 13  ? 1.34986 1.02020 1.41299 0.24896  -0.08361 -0.01412 133  TYR C CZ  
2887 O OH  . TYR C 13  ? 1.31766 1.07622 1.44032 0.30737  -0.05491 0.00395  133  TYR C OH  
2888 N N   . GLN C 14  ? 1.47632 0.83975 1.22217 -0.08962 -0.15600 -0.08988 134  GLN C N   
2889 C CA  . GLN C 14  ? 1.43978 0.75995 1.12303 -0.15127 -0.17140 -0.08028 134  GLN C CA  
2890 C C   . GLN C 14  ? 1.41664 0.71241 1.10290 -0.16299 -0.21260 -0.03111 134  GLN C C   
2891 O O   . GLN C 14  ? 1.42251 0.75027 1.16604 -0.12759 -0.22774 -0.00217 134  GLN C O   
2892 C CB  . GLN C 14  ? 1.44450 0.79079 1.08981 -0.18386 -0.15309 -0.09785 134  GLN C CB  
2893 C CG  . GLN C 14  ? 1.44208 0.80989 1.07562 -0.17764 -0.11301 -0.14482 134  GLN C CG  
2894 C CD  . GLN C 14  ? 1.35634 0.77503 1.00332 -0.16005 -0.09043 -0.16466 134  GLN C CD  
2895 O OE1 . GLN C 14  ? 1.26332 0.71271 0.95862 -0.13364 -0.09880 -0.14729 134  GLN C OE1 
2896 N NE2 . GLN C 14  ? 1.41064 0.84157 1.01644 -0.17409 -0.06190 -0.19713 134  GLN C NE2 
2897 N N   . ASP C 15  ? 1.46591 0.71006 1.09204 -0.21110 -0.23045 -0.01758 135  ASP C N   
2898 C CA  . ASP C 15  ? 1.50149 0.71156 1.12218 -0.22291 -0.27216 0.02818  135  ASP C CA  
2899 C C   . ASP C 15  ? 1.53600 0.73459 1.09832 -0.27379 -0.29073 0.04583  135  ASP C C   
2900 O O   . ASP C 15  ? 1.54751 0.73523 1.04601 -0.30709 -0.27074 0.02356  135  ASP C O   
2901 C CB  . ASP C 15  ? 1.57055 0.71079 1.16471 -0.22912 -0.28581 0.03548  135  ASP C CB  
2902 C CG  . ASP C 15  ? 1.58496 0.71199 1.23068 -0.17038 -0.30161 0.04906  135  ASP C CG  
2903 O OD1 . ASP C 15  ? 1.53425 0.69980 1.22691 -0.11863 -0.27977 0.02698  135  ASP C OD1 
2904 O OD2 . ASP C 15  ? 1.65821 0.73470 1.29185 -0.17101 -0.33522 0.08233  135  ASP C OD2 
2905 N N   . TYR C 16  ? 1.55904 0.76194 1.14110 -0.27585 -0.33024 0.08705  136  TYR C N   
2906 C CA  . TYR C 16  ? 1.61319 0.78926 1.12990 -0.32234 -0.35977 0.10655  136  TYR C CA  
2907 C C   . TYR C 16  ? 1.74320 0.86863 1.23403 -0.34020 -0.40093 0.14856  136  TYR C C   
2908 O O   . TYR C 16  ? 1.77756 0.85082 1.18516 -0.37700 -0.40257 0.14900  136  TYR C O   
2909 C CB  . TYR C 16  ? 1.57773 0.80098 1.13343 -0.31918 -0.37795 0.11825  136  TYR C CB  
2910 C CG  . TYR C 16  ? 1.48899 0.77327 1.10888 -0.28072 -0.33856 0.08883  136  TYR C CG  
2911 C CD1 . TYR C 16  ? 1.45988 0.74401 1.03903 -0.28331 -0.29586 0.04006  136  TYR C CD1 
2912 C CD2 . TYR C 16  ? 1.43872 0.78551 1.15948 -0.23708 -0.34153 0.11249  136  TYR C CD2 
2913 C CE1 . TYR C 16  ? 1.38402 0.72048 1.01762 -0.24660 -0.26106 0.01342  136  TYR C CE1 
2914 C CE2 . TYR C 16  ? 1.36503 0.76659 1.13794 -0.19865 -0.30372 0.08768  136  TYR C CE2 
2915 C CZ  . TYR C 16  ? 1.33833 0.73031 1.06568 -0.20492 -0.26533 0.03692  136  TYR C CZ  
2916 O OH  . TYR C 16  ? 1.26969 0.71367 1.04542 -0.16556 -0.22971 0.01294  136  TYR C OH  
2917 N N   . GLU C 17  ? 1.99739 1.14016 1.55768 -0.31040 -0.43090 0.18610  137  GLU C N   
2918 C CA  . GLU C 17  ? 2.03448 1.13037 1.58135 -0.31526 -0.46951 0.22703  137  GLU C CA  
2919 C C   . GLU C 17  ? 2.02910 1.09435 1.51377 -0.36226 -0.51415 0.25819  137  GLU C C   
2920 O O   . GLU C 17  ? 1.98620 1.04484 1.41031 -0.39545 -0.51078 0.23984  137  GLU C O   
2921 C CB  . GLU C 17  ? 2.19508 1.22643 1.69568 -0.32081 -0.45150 0.21138  137  GLU C CB  
2922 C CG  . GLU C 17  ? 2.18571 1.22539 1.74003 -0.27063 -0.42316 0.18542  137  GLU C CG  
2923 C CD  . GLU C 17  ? 2.27605 1.32722 1.89910 -0.21180 -0.44612 0.21554  137  GLU C CD  
2924 O OE1 . GLU C 17  ? 2.28166 1.40837 1.97580 -0.17872 -0.44780 0.23033  137  GLU C OE1 
2925 O OE2 . GLU C 17  ? 2.37088 1.35604 1.97591 -0.19695 -0.46287 0.22759  137  GLU C OE2 
2926 N N   . PRO C 18  ? 2.09871 1.13880 1.58855 -0.36248 -0.55873 0.30430  138  PRO C N   
2927 C CA  . PRO C 18  ? 2.16148 1.17562 1.59772 -0.40333 -0.60995 0.33736  138  PRO C CA  
2928 C C   . PRO C 18  ? 2.22489 1.17139 1.53137 -0.45093 -0.60249 0.31816  138  PRO C C   
2929 O O   . PRO C 18  ? 2.15293 1.07866 1.41622 -0.45663 -0.55740 0.28599  138  PRO C O   
2930 C CB  . PRO C 18  ? 2.11911 1.11581 1.58611 -0.38610 -0.65100 0.38744  138  PRO C CB  
2931 C CG  . PRO C 18  ? 2.04035 1.08587 1.60852 -0.32413 -0.62810 0.38687  138  PRO C CG  
2932 C CD  . PRO C 18  ? 2.04870 1.09012 1.60274 -0.31560 -0.56941 0.33063  138  PRO C CD  
2933 N N   . GLU C 19  ? 2.50542 1.41976 1.74779 -0.48414 -0.64997 0.34230  139  GLU C N   
2934 C CA  . GLU C 19  ? 2.61867 1.47485 1.72694 -0.52165 -0.64499 0.32376  139  GLU C CA  
2935 C C   . GLU C 19  ? 2.90747 1.70295 1.93974 -0.54910 -0.70153 0.36539  139  GLU C C   
2936 O O   . GLU C 19  ? 2.97209 1.77049 2.05882 -0.54033 -0.74131 0.40798  139  GLU C O   
2937 C CB  . GLU C 19  ? 2.57518 1.44470 1.65436 -0.53033 -0.64358 0.29304  139  GLU C CB  
2938 C CG  . GLU C 19  ? 2.71569 1.58133 1.80322 -0.54777 -0.71478 0.32364  139  GLU C CG  
2939 C CD  . GLU C 19  ? 2.51781 1.46721 1.75566 -0.52461 -0.73136 0.34738  139  GLU C CD  
2940 O OE1 . GLU C 19  ? 2.43064 1.43424 1.76366 -0.48721 -0.69337 0.34578  139  GLU C OE1 
2941 O OE2 . GLU C 19  ? 2.45739 1.41789 1.71542 -0.54346 -0.78467 0.37022  139  GLU C OE2 
2942 N N   . ALA C 20  ? 2.96356 1.70347 1.86298 -0.57747 -0.70437 0.35267  140  ALA C N   
2943 C CA  . ALA C 20  ? 3.10286 1.77655 1.90405 -0.60405 -0.76021 0.38608  140  ALA C CA  
2944 C C   . ALA C 20  ? 3.06345 1.68753 1.72951 -0.62221 -0.76810 0.35842  140  ALA C C   
2945 O O   . ALA C 20  ? 3.19167 1.75386 1.76295 -0.64269 -0.82427 0.37816  140  ALA C O   
2946 C CB  . ALA C 20  ? 2.99992 1.63189 1.74889 -0.61228 -0.74600 0.40976  140  ALA C CB  
2947 O OXT . ALA C 20  ? 2.86497 1.50423 1.50634 -0.61285 -0.72024 0.31435  140  ALA C OXT 
2948 N N   . PRO D 8   ? 1.61650 1.37710 1.45232 0.76321  0.14717  0.03238  128  PRO D N   
2949 C CA  . PRO D 8   ? 1.61234 1.42583 1.49165 0.69131  0.12500  0.03894  128  PRO D CA  
2950 C C   . PRO D 8   ? 1.52539 1.46581 1.48458 0.67800  0.16572  0.05712  128  PRO D C   
2951 O O   . PRO D 8   ? 1.41207 1.46930 1.47552 0.70680  0.18830  0.08666  128  PRO D O   
2952 C CB  . PRO D 8   ? 1.50316 1.36828 1.46012 0.66580  0.07978  0.05844  128  PRO D CB  
2953 C CG  . PRO D 8   ? 1.50225 1.27595 1.40822 0.71634  0.06238  0.05164  128  PRO D CG  
2954 C CD  . PRO D 8   ? 1.60303 1.35608 1.47157 0.77161  0.11041  0.04168  128  PRO D CD  
2955 N N   . SER D 9   ? 1.51109 1.42927 1.42743 0.63337  0.17202  0.04397  129  SER D N   
2956 C CA  . SER D 9   ? 1.42318 1.45468 1.41091 0.61628  0.20758  0.06259  129  SER D CA  
2957 C C   . SER D 9   ? 1.26356 1.42664 1.38645 0.57309  0.18187  0.09257  129  SER D C   
2958 O O   . SER D 9   ? 1.16150 1.30759 1.29013 0.52253  0.13295  0.08746  129  SER D O   
2959 C CB  . SER D 9   ? 1.42302 1.39510 1.33705 0.56766  0.20798  0.04221  129  SER D CB  
2960 O OG  . SER D 9   ? 1.32535 1.40529 1.30865 0.54866  0.23999  0.06210  129  SER D OG  
2961 N N   . GLU D 10  ? 1.07318 1.36507 1.30309 0.59490  0.21381  0.12696  130  GLU D N   
2962 C CA  . GLU D 10  ? 0.92600 1.34023 1.28651 0.55340  0.18356  0.15932  130  GLU D CA  
2963 C C   . GLU D 10  ? 0.84864 1.29804 1.23106 0.48198  0.16880  0.15890  130  GLU D C   
2964 O O   . GLU D 10  ? 0.77778 1.30876 1.25272 0.44020  0.13345  0.18071  130  GLU D O   
2965 C CB  . GLU D 10  ? 0.92891 1.47356 1.41191 0.60034  0.21742  0.20583  130  GLU D CB  
2966 C CG  . GLU D 10  ? 0.98442 1.52537 1.48800 0.66380  0.21932  0.21713  130  GLU D CG  
2967 C CD  . GLU D 10  ? 0.98739 1.65047 1.61629 0.67342  0.23488  0.26306  130  GLU D CD  
2968 O OE1 . GLU D 10  ? 0.91547 1.68065 1.64760 0.62586  0.21609  0.29445  130  GLU D OE1 
2969 O OE2 . GLU D 10  ? 1.07073 1.71982 1.69084 0.72437  0.26190  0.26779  130  GLU D OE2 
2970 N N   . GLU D 11  ? 0.86802 1.25340 1.16632 0.46752  0.19124  0.13546  131  GLU D N   
2971 C CA  . GLU D 11  ? 0.80031 1.21294 1.11599 0.40201  0.17945  0.13455  131  GLU D CA  
2972 C C   . GLU D 11  ? 0.81839 1.10209 1.01253 0.37063  0.16579  0.09595  131  GLU D C   
2973 O O   . GLU D 11  ? 0.88998 1.06494 0.98692 0.40067  0.16753  0.07286  131  GLU D O   
2974 C CB  . GLU D 11  ? 0.84580 1.34670 1.21414 0.41328  0.22836  0.16096  131  GLU D CB  
2975 C CG  . GLU D 11  ? 0.83352 1.46720 1.32848 0.45472  0.25257  0.20928  131  GLU D CG  
2976 C CD  . GLU D 11  ? 0.72719 1.45854 1.34925 0.40905  0.20045  0.23940  131  GLU D CD  
2977 O OE1 . GLU D 11  ? 0.69777 1.40116 1.30777 0.34509  0.15233  0.22206  131  GLU D OE1 
2978 O OE2 . GLU D 11  ? 0.71024 1.54255 1.44255 0.43906  0.20605  0.28200  131  GLU D OE2 
2979 N N   . GLY D 12  ? 0.75630 1.05139 0.96122 0.30872  0.14828  0.09226  132  GLY D N   
2980 C CA  . GLY D 12  ? 0.76827 0.95587 0.87517 0.27512  0.13820  0.06395  132  GLY D CA  
2981 C C   . GLY D 12  ? 0.72234 0.86853 0.81866 0.22921  0.08907  0.05298  132  GLY D C   
2982 O O   . GLY D 12  ? 0.68462 0.87879 0.83836 0.22151  0.06044  0.06341  132  GLY D O   
2983 N N   . TYR D 13  ? 0.73375 0.78609 0.75162 0.19960  0.07971  0.03422  133  TYR D N   
2984 C CA  . TYR D 13  ? 0.69295 0.70547 0.69739 0.15472  0.04191  0.02809  133  TYR D CA  
2985 C C   . TYR D 13  ? 0.74853 0.63719 0.65961 0.15805  0.02953  0.01567  133  TYR D C   
2986 O O   . TYR D 13  ? 0.72277 0.56951 0.61554 0.11974  0.00580  0.01515  133  TYR D O   
2987 C CB  . TYR D 13  ? 0.63009 0.67535 0.66444 0.09934  0.03695  0.02878  133  TYR D CB  
2988 C CG  . TYR D 13  ? 0.57508 0.73627 0.70764 0.08760  0.03352  0.04485  133  TYR D CG  
2989 C CD1 . TYR D 13  ? 0.57656 0.81209 0.75882 0.10314  0.06371  0.05993  133  TYR D CD1 
2990 C CD2 . TYR D 13  ? 0.53147 0.72482 0.70517 0.06265  -0.00220 0.04837  133  TYR D CD2 
2991 C CE1 . TYR D 13  ? 0.52887 0.87235 0.81231 0.08881  0.05367  0.08239  133  TYR D CE1 
2992 C CE2 . TYR D 13  ? 0.49321 0.78083 0.75380 0.04924  -0.01630 0.06462  133  TYR D CE2 
2993 C CZ  . TYR D 13  ? 0.48842 0.85340 0.81045 0.05977  0.00923  0.08377  133  TYR D CZ  
2994 O OH  . TYR D 13  ? 0.45212 0.91247 0.87135 0.04212  -0.01167 0.10719  133  TYR D OH  
2995 N N   . GLN D 14  ? 0.83124 0.65846 0.68444 0.20510  0.04331  0.00874  134  GLN D N   
2996 C CA  . GLN D 14  ? 0.89587 0.59559 0.65949 0.20534  0.02326  -0.00016 134  GLN D CA  
2997 C C   . GLN D 14  ? 0.87316 0.55010 0.64494 0.18923  -0.01287 0.00961  134  GLN D C   
2998 O O   . GLN D 14  ? 0.88732 0.48436 0.61549 0.16143  -0.03599 0.01309  134  GLN D O   
2999 C CB  . GLN D 14  ? 1.00250 0.63540 0.69959 0.26612  0.03899  -0.01070 134  GLN D CB  
3000 C CG  . GLN D 14  ? 1.08632 0.57339 0.68303 0.26405  0.01148  -0.01972 134  GLN D CG  
3001 C CD  . GLN D 14  ? 1.21157 0.61505 0.72285 0.32601  0.02669  -0.03576 134  GLN D CD  
3002 O OE1 . GLN D 14  ? 1.33208 0.60374 0.74687 0.32698  0.00354  -0.04608 134  GLN D OE1 
3003 N NE2 . GLN D 14  ? 1.22537 0.70167 0.77113 0.37977  0.06387  -0.03576 134  GLN D NE2 
3004 N N   . ASP D 15  ? 0.84261 0.58943 0.67121 0.20602  -0.01903 0.01854  135  ASP D N   
3005 C CA  . ASP D 15  ? 0.82579 0.56021 0.66045 0.19478  -0.04999 0.03036  135  ASP D CA  
3006 C C   . ASP D 15  ? 0.74729 0.56326 0.64122 0.16105  -0.05869 0.03741  135  ASP D C   
3007 O O   . ASP D 15  ? 0.73711 0.57553 0.64917 0.16578  -0.07829 0.04712  135  ASP D O   
3008 C CB  . ASP D 15  ? 0.87121 0.60301 0.70878 0.24300  -0.05794 0.03532  135  ASP D CB  
3009 C CG  . ASP D 15  ? 0.99495 0.64072 0.76843 0.28519  -0.05005 0.02509  135  ASP D CG  
3010 O OD1 . ASP D 15  ? 1.06111 0.61617 0.76937 0.26943  -0.05594 0.01823  135  ASP D OD1 
3011 O OD2 . ASP D 15  ? 1.02488 0.68894 0.81116 0.33516  -0.04038 0.02472  135  ASP D OD2 
3012 N N   . TYR D 16  ? 0.70082 0.55550 0.61927 0.12835  -0.04683 0.03231  136  TYR D N   
3013 C CA  . TYR D 16  ? 0.63943 0.56559 0.61016 0.09991  -0.05812 0.03580  136  TYR D CA  
3014 C C   . TYR D 16  ? 0.63170 0.52505 0.57873 0.08236  -0.08097 0.04329  136  TYR D C   
3015 O O   . TYR D 16  ? 0.63859 0.46930 0.54672 0.06316  -0.08194 0.04769  136  TYR D O   
3016 C CB  . TYR D 16  ? 0.59902 0.55044 0.58922 0.06372  -0.04519 0.02983  136  TYR D CB  
3017 C CG  . TYR D 16  ? 0.54604 0.55440 0.58115 0.03168  -0.06175 0.03094  136  TYR D CG  
3018 C CD1 . TYR D 16  ? 0.52961 0.61685 0.62502 0.03952  -0.07403 0.03636  136  TYR D CD1 
3019 C CD2 . TYR D 16  ? 0.51994 0.49904 0.53780 -0.00601 -0.06788 0.02834  136  TYR D CD2 
3020 C CE1 . TYR D 16  ? 0.49679 0.62110 0.62353 0.00994  -0.09734 0.03569  136  TYR D CE1 
3021 C CE2 . TYR D 16  ? 0.48590 0.50475 0.53407 -0.03074 -0.08453 0.02602  136  TYR D CE2 
3022 C CZ  . TYR D 16  ? 0.47826 0.56428 0.57569 -0.02328 -0.10176 0.02789  136  TYR D CZ  
3023 O OH  . TYR D 16  ? 0.45936 0.57015 0.57735 -0.04824 -0.12663 0.02404  136  TYR D OH  
3024 N N   . GLU D 17  ? 0.62401 0.55963 0.59443 0.09029  -0.09986 0.04853  137  GLU D N   
3025 C CA  . GLU D 17  ? 0.62641 0.53546 0.56722 0.07923  -0.11708 0.05707  137  GLU D CA  
3026 C C   . GLU D 17  ? 0.59071 0.53181 0.54581 0.04862  -0.12421 0.05067  137  GLU D C   
3027 O O   . GLU D 17  ? 0.57090 0.57011 0.56979 0.04305  -0.13275 0.04355  137  GLU D O   
3028 C CB  . GLU D 17  ? 0.65766 0.57735 0.59632 0.10882  -0.13734 0.06664  137  GLU D CB  
3029 C CG  . GLU D 17  ? 0.70036 0.58532 0.62571 0.14299  -0.13478 0.07309  137  GLU D CG  
3030 C CD  . GLU D 17  ? 0.72861 0.63170 0.66104 0.17088  -0.15705 0.08412  137  GLU D CD  
3031 O OE1 . GLU D 17  ? 0.74292 0.62442 0.64382 0.16685  -0.17280 0.09635  137  GLU D OE1 
3032 O OE2 . GLU D 17  ? 0.73898 0.68068 0.71012 0.19766  -0.15732 0.08332  137  GLU D OE2 
3033 N N   . PRO D 18  ? 0.58829 0.49163 0.50913 0.03029  -0.12284 0.05628  138  PRO D N   
3034 C CA  . PRO D 18  ? 0.57003 0.49272 0.49282 0.00856  -0.13096 0.04817  138  PRO D CA  
3035 C C   . PRO D 18  ? 0.60324 0.55466 0.52320 0.02209  -0.15919 0.04409  138  PRO D C   
3036 O O   . PRO D 18  ? 0.62093 0.58007 0.53986 0.04780  -0.17150 0.05125  138  PRO D O   
3037 C CB  . PRO D 18  ? 0.57876 0.45123 0.46051 -0.00002 -0.11902 0.06241  138  PRO D CB  
3038 C CG  . PRO D 18  ? 0.58748 0.41711 0.46113 0.00323  -0.10671 0.07838  138  PRO D CG  
3039 C CD  . PRO D 18  ? 0.60871 0.44946 0.49111 0.03066  -0.11476 0.07438  138  PRO D CD  
3040 N N   . GLU D 19  ? 0.77182 0.72686 0.68116 0.00562  -0.17253 0.03374  139  GLU D N   
3041 C CA  . GLU D 19  ? 0.66314 0.63052 0.55825 0.01009  -0.20861 0.02541  139  GLU D CA  
3042 C C   . GLU D 19  ? 0.83377 0.85952 0.79778 -0.00486 -0.23224 0.01869  139  GLU D C   
3043 O O   . GLU D 19  ? 1.15233 1.18898 1.11581 -0.00629 -0.27198 0.01443  139  GLU D O   
3044 C CB  . GLU D 19  ? 0.89733 0.85057 0.75347 0.04092  -0.22588 0.03611  139  GLU D CB  
3045 C CG  . GLU D 19  ? 1.01635 0.95872 0.83057 0.04694  -0.26659 0.02827  139  GLU D CG  
3046 C CD  . GLU D 19  ? 1.19676 1.09328 0.94611 0.04070  -0.26367 0.01665  139  GLU D CD  
3047 O OE1 . GLU D 19  ? 1.31050 1.17253 1.01702 0.05029  -0.22985 0.02711  139  GLU D OE1 
3048 O OE2 . GLU D 19  ? 1.29382 1.18747 1.03712 0.02742  -0.29650 -0.00028 139  GLU D OE2 
3049 N N   . ALA D 20  ? 0.73164 0.79210 0.75247 -0.01694 -0.21081 0.02058  140  ALA D N   
3050 C CA  . ALA D 20  ? 0.55479 0.68097 0.65273 -0.03236 -0.22446 0.02270  140  ALA D CA  
3051 C C   . ALA D 20  ? 0.57720 0.75296 0.72237 -0.00893 -0.24088 0.03763  140  ALA D C   
3052 O O   . ALA D 20  ? 0.51895 0.75033 0.73028 -0.00658 -0.22564 0.04866  140  ALA D O   
3053 C CB  . ALA D 20  ? 0.68824 0.81817 0.79295 -0.06081 -0.26014 0.01301  140  ALA D CB  
3054 O OXT . ALA D 20  ? 0.58606 0.74948 0.70644 0.00905  -0.26797 0.04161  140  ALA D OXT 
# 
