data_8ZN8
# 
_entry.id   8ZN8 
# 
_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   8ZN8         pdb_00008zn8 10.2210/pdb8zn8/pdb 
WWPDB D_1300048186 ?            ?                   
# 
_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                        8ZN8 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-26 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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              zhangtuo@cau.edu.cn 
_pdbx_contact_author.name_first         Tuo 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0900-9285 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Duan, M.P.' 1 ? 
'Zhang, T.'  2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Construction of an artificial photosynthesis system by incorporation of CdS quantum dots into the intrasubunit interface of a four-helix-bundle-structure enzyme
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Duan, M.P.' 1 ? 
primary 'Zhang, T.'  2 ? 
# 
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 Ferritin             19249.656 6   1.16.3.1 ? ? ? 
2 non-polymer syn 'CADMIUM ION'        112.411   24  ?        ? ? ? 
3 non-polymer syn 'HYDROSULFURIC ACID' 34.081    35  ?        ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'      24.305    6   ?        ? ? ? 
5 non-polymer syn 'SULFATE ION'        96.063    7   ?        ? ? ? 
6 water       nat water                18.015    530 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ASQVRQNYHEDAEASINKQINMCLYASYVYLSMAYYFERDDVALPGFAKFFKESSDCCREHAQTFMKYQNKRGGRIVLQQ
IAAPSMQEWGTGLEALQAALDLEKQVNQSLLELHSTASGNNDPHLTKLLEDEYLEEQVDSIKKIGDMITKLKRAGPTGLG
EYMFDKELN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ASQVRQNYHEDAEASINKQINMCLYASYVYLSMAYYFERDDVALPGFAKFFKESSDCCREHAQTFMKYQNKRGGRIVLQQ
IAAPSMQEWGTGLEALQAALDLEKQVNQSLLELHSTASGNNDPHLTKLLEDEYLEEQVDSIKKIGDMITKLKRAGPTGLG
EYMFDKELN
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CADMIUM ION'        CD  
3 'HYDROSULFURIC ACID' H2S 
4 'MAGNESIUM ION'      MG  
5 'SULFATE ION'        SO4 
6 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   SER n 
1 3   GLN n 
1 4   VAL n 
1 5   ARG n 
1 6   GLN n 
1 7   ASN n 
1 8   TYR n 
1 9   HIS n 
1 10  GLU n 
1 11  ASP n 
1 12  ALA n 
1 13  GLU n 
1 14  ALA n 
1 15  SER n 
1 16  ILE n 
1 17  ASN n 
1 18  LYS n 
1 19  GLN n 
1 20  ILE n 
1 21  ASN n 
1 22  MET n 
1 23  CYS n 
1 24  LEU n 
1 25  TYR n 
1 26  ALA n 
1 27  SER n 
1 28  TYR n 
1 29  VAL n 
1 30  TYR n 
1 31  LEU n 
1 32  SER n 
1 33  MET n 
1 34  ALA n 
1 35  TYR n 
1 36  TYR n 
1 37  PHE n 
1 38  GLU n 
1 39  ARG n 
1 40  ASP n 
1 41  ASP n 
1 42  VAL n 
1 43  ALA n 
1 44  LEU n 
1 45  PRO n 
1 46  GLY n 
1 47  PHE n 
1 48  ALA n 
1 49  LYS n 
1 50  PHE n 
1 51  PHE n 
1 52  LYS n 
1 53  GLU n 
1 54  SER n 
1 55  SER n 
1 56  ASP n 
1 57  CYS n 
1 58  CYS n 
1 59  ARG n 
1 60  GLU n 
1 61  HIS n 
1 62  ALA n 
1 63  GLN n 
1 64  THR n 
1 65  PHE n 
1 66  MET n 
1 67  LYS n 
1 68  TYR n 
1 69  GLN n 
1 70  ASN n 
1 71  LYS n 
1 72  ARG n 
1 73  GLY n 
1 74  GLY n 
1 75  ARG n 
1 76  ILE n 
1 77  VAL n 
1 78  LEU n 
1 79  GLN n 
1 80  GLN n 
1 81  ILE n 
1 82  ALA n 
1 83  ALA n 
1 84  PRO n 
1 85  SER n 
1 86  MET n 
1 87  GLN n 
1 88  GLU n 
1 89  TRP n 
1 90  GLY n 
1 91  THR n 
1 92  GLY n 
1 93  LEU n 
1 94  GLU n 
1 95  ALA n 
1 96  LEU n 
1 97  GLN n 
1 98  ALA n 
1 99  ALA n 
1 100 LEU n 
1 101 ASP n 
1 102 LEU n 
1 103 GLU n 
1 104 LYS n 
1 105 GLN n 
1 106 VAL n 
1 107 ASN n 
1 108 GLN n 
1 109 SER n 
1 110 LEU n 
1 111 LEU n 
1 112 GLU n 
1 113 LEU n 
1 114 HIS n 
1 115 SER n 
1 116 THR n 
1 117 ALA n 
1 118 SER n 
1 119 GLY n 
1 120 ASN n 
1 121 ASN n 
1 122 ASP n 
1 123 PRO n 
1 124 HIS n 
1 125 LEU n 
1 126 THR n 
1 127 LYS n 
1 128 LEU n 
1 129 LEU n 
1 130 GLU n 
1 131 ASP n 
1 132 GLU n 
1 133 TYR n 
1 134 LEU n 
1 135 GLU n 
1 136 GLU n 
1 137 GLN n 
1 138 VAL n 
1 139 ASP n 
1 140 SER n 
1 141 ILE n 
1 142 LYS n 
1 143 LYS n 
1 144 ILE n 
1 145 GLY n 
1 146 ASP n 
1 147 MET n 
1 148 ILE n 
1 149 THR n 
1 150 LYS n 
1 151 LEU n 
1 152 LYS n 
1 153 ARG n 
1 154 ALA n 
1 155 GLY n 
1 156 PRO n 
1 157 THR n 
1 158 GLY n 
1 159 LEU n 
1 160 GLY n 
1 161 GLU n 
1 162 TYR n 
1 163 MET n 
1 164 PHE n 
1 165 ASP n 
1 166 LYS n 
1 167 GLU n 
1 168 LEU n 
1 169 ASN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               'Kuruma prawn, Marsupenaeus japonicus' 
_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      'Penaeus japonicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     27405 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia phage EcSzw-2' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     2419741 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CD  non-polymer         . 'CADMIUM ION'        ?                  'Cd 2'           112.411 
CYS 'L-peptide linking' y CYSTEINE             ?                  'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE            ?                  'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'      ?                  'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE              ?                  'C2 H5 N O2'     75.067  
H2S non-polymer         . 'HYDROSULFURIC ACID' 'HYDROGEN SULFIDE' 'H2 S'           34.081  
HIS 'L-peptide linking' y HISTIDINE            ?                  'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                ?                  'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE           ?                  'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE              ?                  'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE               ?                  'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE           ?                  'C5 H11 N O2 S'  149.211 
MG  non-polymer         . 'MAGNESIUM ION'      ?                  'Mg 2'           24.305  
PHE 'L-peptide linking' y PHENYLALANINE        ?                  'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE              ?                  'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE               ?                  'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'        ?                  'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE            ?                  'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN           ?                  'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE             ?                  'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE               ?                  'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   2   2   ALA ALA A . n 
A 1 2   SER 2   3   3   SER SER A . n 
A 1 3   GLN 3   4   4   GLN GLN A . n 
A 1 4   VAL 4   5   5   VAL VAL A . n 
A 1 5   ARG 5   6   6   ARG ARG A . n 
A 1 6   GLN 6   7   7   GLN GLN A . n 
A 1 7   ASN 7   8   8   ASN ASN A . n 
A 1 8   TYR 8   9   9   TYR TYR A . n 
A 1 9   HIS 9   10  10  HIS HIS A . n 
A 1 10  GLU 10  11  11  GLU GLU A . n 
A 1 11  ASP 11  12  12  ASP ASP A . n 
A 1 12  ALA 12  13  13  ALA ALA A . n 
A 1 13  GLU 13  14  14  GLU GLU A . n 
A 1 14  ALA 14  15  15  ALA ALA A . n 
A 1 15  SER 15  16  16  SER SER A . n 
A 1 16  ILE 16  17  17  ILE ILE A . n 
A 1 17  ASN 17  18  18  ASN ASN A . n 
A 1 18  LYS 18  19  19  LYS LYS A . n 
A 1 19  GLN 19  20  20  GLN GLN A . n 
A 1 20  ILE 20  21  21  ILE ILE A . n 
A 1 21  ASN 21  22  22  ASN ASN A . n 
A 1 22  MET 22  23  23  MET MET A . n 
A 1 23  CYS 23  24  24  CYS CYS A . n 
A 1 24  LEU 24  25  25  LEU LEU A . n 
A 1 25  TYR 25  26  26  TYR TYR A . n 
A 1 26  ALA 26  27  27  ALA ALA A . n 
A 1 27  SER 27  28  28  SER SER A . n 
A 1 28  TYR 28  29  29  TYR TYR A . n 
A 1 29  VAL 29  30  30  VAL VAL A . n 
A 1 30  TYR 30  31  31  TYR TYR A . n 
A 1 31  LEU 31  32  32  LEU LEU A . n 
A 1 32  SER 32  33  33  SER SER A . n 
A 1 33  MET 33  34  34  MET MET A . n 
A 1 34  ALA 34  35  35  ALA ALA A . n 
A 1 35  TYR 35  36  36  TYR TYR A . n 
A 1 36  TYR 36  37  37  TYR TYR A . n 
A 1 37  PHE 37  38  38  PHE PHE A . n 
A 1 38  GLU 38  39  39  GLU GLU A . n 
A 1 39  ARG 39  40  40  ARG ARG A . n 
A 1 40  ASP 40  41  41  ASP ASP A . n 
A 1 41  ASP 41  42  42  ASP ASP A . n 
A 1 42  VAL 42  43  43  VAL VAL A . n 
A 1 43  ALA 43  44  44  ALA ALA A . n 
A 1 44  LEU 44  45  45  LEU LEU A . n 
A 1 45  PRO 45  46  46  PRO PRO A . n 
A 1 46  GLY 46  47  47  GLY GLY A . n 
A 1 47  PHE 47  48  48  PHE PHE A . n 
A 1 48  ALA 48  49  49  ALA ALA A . n 
A 1 49  LYS 49  50  50  LYS LYS A . n 
A 1 50  PHE 50  51  51  PHE PHE A . n 
A 1 51  PHE 51  52  52  PHE PHE A . n 
A 1 52  LYS 52  53  53  LYS LYS A . n 
A 1 53  GLU 53  54  54  GLU GLU A . n 
A 1 54  SER 54  55  55  SER SER A . n 
A 1 55  SER 55  56  56  SER SER A . n 
A 1 56  ASP 56  57  57  ASP ASP A . n 
A 1 57  CYS 57  58  58  CYS CYS A . n 
A 1 58  CYS 58  59  59  CYS CYS A . n 
A 1 59  ARG 59  60  60  ARG ARG A . n 
A 1 60  GLU 60  61  61  GLU GLU A . n 
A 1 61  HIS 61  62  62  HIS HIS A . n 
A 1 62  ALA 62  63  63  ALA ALA A . n 
A 1 63  GLN 63  64  64  GLN GLN A . n 
A 1 64  THR 64  65  65  THR THR A . n 
A 1 65  PHE 65  66  66  PHE PHE A . n 
A 1 66  MET 66  67  67  MET MET A . n 
A 1 67  LYS 67  68  68  LYS LYS A . n 
A 1 68  TYR 68  69  69  TYR TYR A . n 
A 1 69  GLN 69  70  70  GLN GLN A . n 
A 1 70  ASN 70  71  71  ASN ASN A . n 
A 1 71  LYS 71  72  72  LYS LYS A . n 
A 1 72  ARG 72  73  73  ARG ARG A . n 
A 1 73  GLY 73  74  74  GLY GLY A . n 
A 1 74  GLY 74  75  75  GLY GLY A . n 
A 1 75  ARG 75  76  76  ARG ARG A . n 
A 1 76  ILE 76  77  77  ILE ILE A . n 
A 1 77  VAL 77  78  78  VAL VAL A . n 
A 1 78  LEU 78  79  79  LEU LEU A . n 
A 1 79  GLN 79  80  80  GLN GLN A . n 
A 1 80  GLN 80  81  81  GLN GLN A . n 
A 1 81  ILE 81  82  82  ILE ILE A . n 
A 1 82  ALA 82  83  83  ALA ALA A . n 
A 1 83  ALA 83  84  84  ALA ALA A . n 
A 1 84  PRO 84  85  85  PRO PRO A . n 
A 1 85  SER 85  86  86  SER SER A . n 
A 1 86  MET 86  87  87  MET MET A . n 
A 1 87  GLN 87  88  88  GLN GLN A . n 
A 1 88  GLU 88  89  89  GLU GLU A . n 
A 1 89  TRP 89  90  90  TRP TRP A . n 
A 1 90  GLY 90  91  91  GLY GLY A . n 
A 1 91  THR 91  92  92  THR THR A . n 
A 1 92  GLY 92  93  93  GLY GLY A . n 
A 1 93  LEU 93  94  94  LEU LEU A . n 
A 1 94  GLU 94  95  95  GLU GLU A . n 
A 1 95  ALA 95  96  96  ALA ALA A . n 
A 1 96  LEU 96  97  97  LEU LEU A . n 
A 1 97  GLN 97  98  98  GLN GLN A . n 
A 1 98  ALA 98  99  99  ALA ALA A . n 
A 1 99  ALA 99  100 100 ALA ALA A . n 
A 1 100 LEU 100 101 101 LEU LEU A . n 
A 1 101 ASP 101 102 102 ASP ASP A . n 
A 1 102 LEU 102 103 103 LEU LEU A . n 
A 1 103 GLU 103 104 104 GLU GLU A . n 
A 1 104 LYS 104 105 105 LYS LYS A . n 
A 1 105 GLN 105 106 106 GLN GLN A . n 
A 1 106 VAL 106 107 107 VAL VAL A . n 
A 1 107 ASN 107 108 108 ASN ASN A . n 
A 1 108 GLN 108 109 109 GLN GLN A . n 
A 1 109 SER 109 110 110 SER SER A . n 
A 1 110 LEU 110 111 111 LEU LEU A . n 
A 1 111 LEU 111 112 112 LEU LEU A . n 
A 1 112 GLU 112 113 113 GLU GLU A . n 
A 1 113 LEU 113 114 114 LEU LEU A . n 
A 1 114 HIS 114 115 115 HIS HIS A . n 
A 1 115 SER 115 116 116 SER SER A . n 
A 1 116 THR 116 117 117 THR THR A . n 
A 1 117 ALA 117 118 118 ALA ALA A . n 
A 1 118 SER 118 119 119 SER SER A . n 
A 1 119 GLY 119 120 120 GLY GLY A . n 
A 1 120 ASN 120 121 121 ASN ASN A . n 
A 1 121 ASN 121 122 122 ASN ASN A . n 
A 1 122 ASP 122 123 123 ASP ASP A . n 
A 1 123 PRO 123 124 124 PRO PRO A . n 
A 1 124 HIS 124 125 125 HIS HIS A . n 
A 1 125 LEU 125 126 126 LEU LEU A . n 
A 1 126 THR 126 127 127 THR THR A . n 
A 1 127 LYS 127 128 128 LYS LYS A . n 
A 1 128 LEU 128 129 129 LEU LEU A . n 
A 1 129 LEU 129 130 130 LEU LEU A . n 
A 1 130 GLU 130 131 131 GLU GLU A . n 
A 1 131 ASP 131 132 132 ASP ASP A . n 
A 1 132 GLU 132 133 133 GLU GLU A . n 
A 1 133 TYR 133 134 134 TYR TYR A . n 
A 1 134 LEU 134 135 135 LEU LEU A . n 
A 1 135 GLU 135 136 136 GLU GLU A . n 
A 1 136 GLU 136 137 137 GLU GLU A . n 
A 1 137 GLN 137 138 138 GLN GLN A . n 
A 1 138 VAL 138 139 139 VAL VAL A . n 
A 1 139 ASP 139 140 140 ASP ASP A . n 
A 1 140 SER 140 141 141 SER SER A . n 
A 1 141 ILE 141 142 142 ILE ILE A . n 
A 1 142 LYS 142 143 143 LYS LYS A . n 
A 1 143 LYS 143 144 144 LYS LYS A . n 
A 1 144 ILE 144 145 145 ILE ILE A . n 
A 1 145 GLY 145 146 146 GLY GLY A . n 
A 1 146 ASP 146 147 147 ASP ASP A . n 
A 1 147 MET 147 148 148 MET MET A . n 
A 1 148 ILE 148 149 149 ILE ILE A . n 
A 1 149 THR 149 150 150 THR THR A . n 
A 1 150 LYS 150 151 151 LYS LYS A . n 
A 1 151 LEU 151 152 152 LEU LEU A . n 
A 1 152 LYS 152 153 153 LYS LYS A . n 
A 1 153 ARG 153 154 154 ARG ARG A . n 
A 1 154 ALA 154 155 155 ALA ALA A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 PRO 156 157 157 PRO PRO A . n 
A 1 157 THR 157 158 158 THR THR A . n 
A 1 158 GLY 158 159 159 GLY GLY A . n 
A 1 159 LEU 159 160 160 LEU LEU A . n 
A 1 160 GLY 160 161 161 GLY GLY A . n 
A 1 161 GLU 161 162 162 GLU GLU A . n 
A 1 162 TYR 162 163 163 TYR TYR A . n 
A 1 163 MET 163 164 164 MET MET A . n 
A 1 164 PHE 164 165 165 PHE PHE A . n 
A 1 165 ASP 165 166 166 ASP ASP A . n 
A 1 166 LYS 166 167 167 LYS LYS A . n 
A 1 167 GLU 167 168 168 GLU GLU A . n 
A 1 168 LEU 168 169 169 LEU LEU A . n 
A 1 169 ASN 169 170 170 ASN ASN A . n 
B 1 1   ALA 1   2   2   ALA ALA B . n 
B 1 2   SER 2   3   3   SER SER B . n 
B 1 3   GLN 3   4   4   GLN GLN B . n 
B 1 4   VAL 4   5   5   VAL VAL B . n 
B 1 5   ARG 5   6   6   ARG ARG B . n 
B 1 6   GLN 6   7   7   GLN GLN B . n 
B 1 7   ASN 7   8   8   ASN ASN B . n 
B 1 8   TYR 8   9   9   TYR TYR B . n 
B 1 9   HIS 9   10  10  HIS HIS B . n 
B 1 10  GLU 10  11  11  GLU GLU B . n 
B 1 11  ASP 11  12  12  ASP ASP B . n 
B 1 12  ALA 12  13  13  ALA ALA B . n 
B 1 13  GLU 13  14  14  GLU GLU B . n 
B 1 14  ALA 14  15  15  ALA ALA B . n 
B 1 15  SER 15  16  16  SER SER B . n 
B 1 16  ILE 16  17  17  ILE ILE B . n 
B 1 17  ASN 17  18  18  ASN ASN B . n 
B 1 18  LYS 18  19  19  LYS LYS B . n 
B 1 19  GLN 19  20  20  GLN GLN B . n 
B 1 20  ILE 20  21  21  ILE ILE B . n 
B 1 21  ASN 21  22  22  ASN ASN B . n 
B 1 22  MET 22  23  23  MET MET B . n 
B 1 23  CYS 23  24  24  CYS CYS B . n 
B 1 24  LEU 24  25  25  LEU LEU B . n 
B 1 25  TYR 25  26  26  TYR TYR B . n 
B 1 26  ALA 26  27  27  ALA ALA B . n 
B 1 27  SER 27  28  28  SER SER B . n 
B 1 28  TYR 28  29  29  TYR TYR B . n 
B 1 29  VAL 29  30  30  VAL VAL B . n 
B 1 30  TYR 30  31  31  TYR TYR B . n 
B 1 31  LEU 31  32  32  LEU LEU B . n 
B 1 32  SER 32  33  33  SER SER B . n 
B 1 33  MET 33  34  34  MET MET B . n 
B 1 34  ALA 34  35  35  ALA ALA B . n 
B 1 35  TYR 35  36  36  TYR TYR B . n 
B 1 36  TYR 36  37  37  TYR TYR B . n 
B 1 37  PHE 37  38  38  PHE PHE B . n 
B 1 38  GLU 38  39  39  GLU GLU B . n 
B 1 39  ARG 39  40  40  ARG ARG B . n 
B 1 40  ASP 40  41  41  ASP ASP B . n 
B 1 41  ASP 41  42  42  ASP ASP B . n 
B 1 42  VAL 42  43  43  VAL VAL B . n 
B 1 43  ALA 43  44  44  ALA ALA B . n 
B 1 44  LEU 44  45  45  LEU LEU B . n 
B 1 45  PRO 45  46  46  PRO PRO B . n 
B 1 46  GLY 46  47  47  GLY GLY B . n 
B 1 47  PHE 47  48  48  PHE PHE B . n 
B 1 48  ALA 48  49  49  ALA ALA B . n 
B 1 49  LYS 49  50  50  LYS LYS B . n 
B 1 50  PHE 50  51  51  PHE PHE B . n 
B 1 51  PHE 51  52  52  PHE PHE B . n 
B 1 52  LYS 52  53  53  LYS LYS B . n 
B 1 53  GLU 53  54  54  GLU GLU B . n 
B 1 54  SER 54  55  55  SER SER B . n 
B 1 55  SER 55  56  56  SER SER B . n 
B 1 56  ASP 56  57  57  ASP ASP B . n 
B 1 57  CYS 57  58  58  CYS CYS B . n 
B 1 58  CYS 58  59  59  CYS CYS B . n 
B 1 59  ARG 59  60  60  ARG ARG B . n 
B 1 60  GLU 60  61  61  GLU GLU B . n 
B 1 61  HIS 61  62  62  HIS HIS B . n 
B 1 62  ALA 62  63  63  ALA ALA B . n 
B 1 63  GLN 63  64  64  GLN GLN B . n 
B 1 64  THR 64  65  65  THR THR B . n 
B 1 65  PHE 65  66  66  PHE PHE B . n 
B 1 66  MET 66  67  67  MET MET B . n 
B 1 67  LYS 67  68  68  LYS LYS B . n 
B 1 68  TYR 68  69  69  TYR TYR B . n 
B 1 69  GLN 69  70  70  GLN GLN B . n 
B 1 70  ASN 70  71  71  ASN ASN B . n 
B 1 71  LYS 71  72  72  LYS LYS B . n 
B 1 72  ARG 72  73  73  ARG ARG B . n 
B 1 73  GLY 73  74  74  GLY GLY B . n 
B 1 74  GLY 74  75  75  GLY GLY B . n 
B 1 75  ARG 75  76  76  ARG ARG B . n 
B 1 76  ILE 76  77  77  ILE ILE B . n 
B 1 77  VAL 77  78  78  VAL VAL B . n 
B 1 78  LEU 78  79  79  LEU LEU B . n 
B 1 79  GLN 79  80  80  GLN GLN B . n 
B 1 80  GLN 80  81  81  GLN GLN B . n 
B 1 81  ILE 81  82  82  ILE ILE B . n 
B 1 82  ALA 82  83  83  ALA ALA B . n 
B 1 83  ALA 83  84  84  ALA ALA B . n 
B 1 84  PRO 84  85  85  PRO PRO B . n 
B 1 85  SER 85  86  86  SER SER B . n 
B 1 86  MET 86  87  87  MET MET B . n 
B 1 87  GLN 87  88  88  GLN GLN B . n 
B 1 88  GLU 88  89  89  GLU GLU B . n 
B 1 89  TRP 89  90  90  TRP TRP B . n 
B 1 90  GLY 90  91  91  GLY GLY B . n 
B 1 91  THR 91  92  92  THR THR B . n 
B 1 92  GLY 92  93  93  GLY GLY B . n 
B 1 93  LEU 93  94  94  LEU LEU B . n 
B 1 94  GLU 94  95  95  GLU GLU B . n 
B 1 95  ALA 95  96  96  ALA ALA B . n 
B 1 96  LEU 96  97  97  LEU LEU B . n 
B 1 97  GLN 97  98  98  GLN GLN B . n 
B 1 98  ALA 98  99  99  ALA ALA B . n 
B 1 99  ALA 99  100 100 ALA ALA B . n 
B 1 100 LEU 100 101 101 LEU LEU B . n 
B 1 101 ASP 101 102 102 ASP ASP B . n 
B 1 102 LEU 102 103 103 LEU LEU B . n 
B 1 103 GLU 103 104 104 GLU GLU B . n 
B 1 104 LYS 104 105 105 LYS LYS B . n 
B 1 105 GLN 105 106 106 GLN GLN B . n 
B 1 106 VAL 106 107 107 VAL VAL B . n 
B 1 107 ASN 107 108 108 ASN ASN B . n 
B 1 108 GLN 108 109 109 GLN GLN B . n 
B 1 109 SER 109 110 110 SER SER B . n 
B 1 110 LEU 110 111 111 LEU LEU B . n 
B 1 111 LEU 111 112 112 LEU LEU B . n 
B 1 112 GLU 112 113 113 GLU GLU B . n 
B 1 113 LEU 113 114 114 LEU LEU B . n 
B 1 114 HIS 114 115 115 HIS HIS B . n 
B 1 115 SER 115 116 116 SER SER B . n 
B 1 116 THR 116 117 117 THR THR B . n 
B 1 117 ALA 117 118 118 ALA ALA B . n 
B 1 118 SER 118 119 119 SER SER B . n 
B 1 119 GLY 119 120 120 GLY GLY B . n 
B 1 120 ASN 120 121 121 ASN ASN B . n 
B 1 121 ASN 121 122 122 ASN ASN B . n 
B 1 122 ASP 122 123 123 ASP ASP B . n 
B 1 123 PRO 123 124 124 PRO PRO B . n 
B 1 124 HIS 124 125 125 HIS HIS B . n 
B 1 125 LEU 125 126 126 LEU LEU B . n 
B 1 126 THR 126 127 127 THR THR B . n 
B 1 127 LYS 127 128 128 LYS LYS B . n 
B 1 128 LEU 128 129 129 LEU LEU B . n 
B 1 129 LEU 129 130 130 LEU LEU B . n 
B 1 130 GLU 130 131 131 GLU GLU B . n 
B 1 131 ASP 131 132 132 ASP ASP B . n 
B 1 132 GLU 132 133 133 GLU GLU B . n 
B 1 133 TYR 133 134 134 TYR TYR B . n 
B 1 134 LEU 134 135 135 LEU LEU B . n 
B 1 135 GLU 135 136 136 GLU GLU B . n 
B 1 136 GLU 136 137 137 GLU GLU B . n 
B 1 137 GLN 137 138 138 GLN GLN B . n 
B 1 138 VAL 138 139 139 VAL VAL B . n 
B 1 139 ASP 139 140 140 ASP ASP B . n 
B 1 140 SER 140 141 141 SER SER B . n 
B 1 141 ILE 141 142 142 ILE ILE B . n 
B 1 142 LYS 142 143 143 LYS LYS B . n 
B 1 143 LYS 143 144 144 LYS LYS B . n 
B 1 144 ILE 144 145 145 ILE ILE B . n 
B 1 145 GLY 145 146 146 GLY GLY B . n 
B 1 146 ASP 146 147 147 ASP ASP B . n 
B 1 147 MET 147 148 148 MET MET B . n 
B 1 148 ILE 148 149 149 ILE ILE B . n 
B 1 149 THR 149 150 150 THR THR B . n 
B 1 150 LYS 150 151 151 LYS LYS B . n 
B 1 151 LEU 151 152 152 LEU LEU B . n 
B 1 152 LYS 152 153 153 LYS LYS B . n 
B 1 153 ARG 153 154 154 ARG ARG B . n 
B 1 154 ALA 154 155 155 ALA ALA B . n 
B 1 155 GLY 155 156 156 GLY GLY B . n 
B 1 156 PRO 156 157 157 PRO PRO B . n 
B 1 157 THR 157 158 158 THR THR B . n 
B 1 158 GLY 158 159 159 GLY GLY B . n 
B 1 159 LEU 159 160 160 LEU LEU B . n 
B 1 160 GLY 160 161 161 GLY GLY B . n 
B 1 161 GLU 161 162 162 GLU GLU B . n 
B 1 162 TYR 162 163 163 TYR TYR B . n 
B 1 163 MET 163 164 164 MET MET B . n 
B 1 164 PHE 164 165 165 PHE PHE B . n 
B 1 165 ASP 165 166 166 ASP ASP B . n 
B 1 166 LYS 166 167 167 LYS LYS B . n 
B 1 167 GLU 167 168 168 GLU GLU B . n 
B 1 168 LEU 168 169 169 LEU LEU B . n 
B 1 169 ASN 169 170 170 ASN ASN B . n 
C 1 1   ALA 1   2   2   ALA ALA C . n 
C 1 2   SER 2   3   3   SER SER C . n 
C 1 3   GLN 3   4   4   GLN GLN C . n 
C 1 4   VAL 4   5   5   VAL VAL C . n 
C 1 5   ARG 5   6   6   ARG ARG C . n 
C 1 6   GLN 6   7   7   GLN GLN C . n 
C 1 7   ASN 7   8   8   ASN ASN C . n 
C 1 8   TYR 8   9   9   TYR TYR C . n 
C 1 9   HIS 9   10  10  HIS HIS C . n 
C 1 10  GLU 10  11  11  GLU GLU C . n 
C 1 11  ASP 11  12  12  ASP ASP C . n 
C 1 12  ALA 12  13  13  ALA ALA C . n 
C 1 13  GLU 13  14  14  GLU GLU C . n 
C 1 14  ALA 14  15  15  ALA ALA C . n 
C 1 15  SER 15  16  16  SER SER C . n 
C 1 16  ILE 16  17  17  ILE ILE C . n 
C 1 17  ASN 17  18  18  ASN ASN C . n 
C 1 18  LYS 18  19  19  LYS LYS C . n 
C 1 19  GLN 19  20  20  GLN GLN C . n 
C 1 20  ILE 20  21  21  ILE ILE C . n 
C 1 21  ASN 21  22  22  ASN ASN C . n 
C 1 22  MET 22  23  23  MET MET C . n 
C 1 23  CYS 23  24  24  CYS CYS C . n 
C 1 24  LEU 24  25  25  LEU LEU C . n 
C 1 25  TYR 25  26  26  TYR TYR C . n 
C 1 26  ALA 26  27  27  ALA ALA C . n 
C 1 27  SER 27  28  28  SER SER C . n 
C 1 28  TYR 28  29  29  TYR TYR C . n 
C 1 29  VAL 29  30  30  VAL VAL C . n 
C 1 30  TYR 30  31  31  TYR TYR C . n 
C 1 31  LEU 31  32  32  LEU LEU C . n 
C 1 32  SER 32  33  33  SER SER C . n 
C 1 33  MET 33  34  34  MET MET C . n 
C 1 34  ALA 34  35  35  ALA ALA C . n 
C 1 35  TYR 35  36  36  TYR TYR C . n 
C 1 36  TYR 36  37  37  TYR TYR C . n 
C 1 37  PHE 37  38  38  PHE PHE C . n 
C 1 38  GLU 38  39  39  GLU GLU C . n 
C 1 39  ARG 39  40  40  ARG ARG C . n 
C 1 40  ASP 40  41  41  ASP ASP C . n 
C 1 41  ASP 41  42  42  ASP ASP C . n 
C 1 42  VAL 42  43  43  VAL VAL C . n 
C 1 43  ALA 43  44  44  ALA ALA C . n 
C 1 44  LEU 44  45  45  LEU LEU C . n 
C 1 45  PRO 45  46  46  PRO PRO C . n 
C 1 46  GLY 46  47  47  GLY GLY C . n 
C 1 47  PHE 47  48  48  PHE PHE C . n 
C 1 48  ALA 48  49  49  ALA ALA C . n 
C 1 49  LYS 49  50  50  LYS LYS C . n 
C 1 50  PHE 50  51  51  PHE PHE C . n 
C 1 51  PHE 51  52  52  PHE PHE C . n 
C 1 52  LYS 52  53  53  LYS LYS C . n 
C 1 53  GLU 53  54  54  GLU GLU C . n 
C 1 54  SER 54  55  55  SER SER C . n 
C 1 55  SER 55  56  56  SER SER C . n 
C 1 56  ASP 56  57  57  ASP ASP C . n 
C 1 57  CYS 57  58  58  CYS CYS C . n 
C 1 58  CYS 58  59  59  CYS CYS C . n 
C 1 59  ARG 59  60  60  ARG ARG C . n 
C 1 60  GLU 60  61  61  GLU GLU C . n 
C 1 61  HIS 61  62  62  HIS HIS C . n 
C 1 62  ALA 62  63  63  ALA ALA C . n 
C 1 63  GLN 63  64  64  GLN GLN C . n 
C 1 64  THR 64  65  65  THR THR C . n 
C 1 65  PHE 65  66  66  PHE PHE C . n 
C 1 66  MET 66  67  67  MET MET C . n 
C 1 67  LYS 67  68  68  LYS LYS C . n 
C 1 68  TYR 68  69  69  TYR TYR C . n 
C 1 69  GLN 69  70  70  GLN GLN C . n 
C 1 70  ASN 70  71  71  ASN ASN C . n 
C 1 71  LYS 71  72  72  LYS LYS C . n 
C 1 72  ARG 72  73  73  ARG ARG C . n 
C 1 73  GLY 73  74  74  GLY GLY C . n 
C 1 74  GLY 74  75  75  GLY GLY C . n 
C 1 75  ARG 75  76  76  ARG ARG C . n 
C 1 76  ILE 76  77  77  ILE ILE C . n 
C 1 77  VAL 77  78  78  VAL VAL C . n 
C 1 78  LEU 78  79  79  LEU LEU C . n 
C 1 79  GLN 79  80  80  GLN GLN C . n 
C 1 80  GLN 80  81  81  GLN GLN C . n 
C 1 81  ILE 81  82  82  ILE ILE C . n 
C 1 82  ALA 82  83  83  ALA ALA C . n 
C 1 83  ALA 83  84  84  ALA ALA C . n 
C 1 84  PRO 84  85  85  PRO PRO C . n 
C 1 85  SER 85  86  86  SER SER C . n 
C 1 86  MET 86  87  87  MET MET C . n 
C 1 87  GLN 87  88  88  GLN GLN C . n 
C 1 88  GLU 88  89  89  GLU GLU C . n 
C 1 89  TRP 89  90  90  TRP TRP C . n 
C 1 90  GLY 90  91  91  GLY GLY C . n 
C 1 91  THR 91  92  92  THR THR C . n 
C 1 92  GLY 92  93  93  GLY GLY C . n 
C 1 93  LEU 93  94  94  LEU LEU C . n 
C 1 94  GLU 94  95  95  GLU GLU C . n 
C 1 95  ALA 95  96  96  ALA ALA C . n 
C 1 96  LEU 96  97  97  LEU LEU C . n 
C 1 97  GLN 97  98  98  GLN GLN C . n 
C 1 98  ALA 98  99  99  ALA ALA C . n 
C 1 99  ALA 99  100 100 ALA ALA C . n 
C 1 100 LEU 100 101 101 LEU LEU C . n 
C 1 101 ASP 101 102 102 ASP ASP C . n 
C 1 102 LEU 102 103 103 LEU LEU C . n 
C 1 103 GLU 103 104 104 GLU GLU C . n 
C 1 104 LYS 104 105 105 LYS LYS C . n 
C 1 105 GLN 105 106 106 GLN GLN C . n 
C 1 106 VAL 106 107 107 VAL VAL C . n 
C 1 107 ASN 107 108 108 ASN ASN C . n 
C 1 108 GLN 108 109 109 GLN GLN C . n 
C 1 109 SER 109 110 110 SER SER C . n 
C 1 110 LEU 110 111 111 LEU LEU C . n 
C 1 111 LEU 111 112 112 LEU LEU C . n 
C 1 112 GLU 112 113 113 GLU GLU C . n 
C 1 113 LEU 113 114 114 LEU LEU C . n 
C 1 114 HIS 114 115 115 HIS HIS C . n 
C 1 115 SER 115 116 116 SER SER C . n 
C 1 116 THR 116 117 117 THR THR C . n 
C 1 117 ALA 117 118 118 ALA ALA C . n 
C 1 118 SER 118 119 119 SER SER C . n 
C 1 119 GLY 119 120 120 GLY GLY C . n 
C 1 120 ASN 120 121 121 ASN ASN C . n 
C 1 121 ASN 121 122 122 ASN ASN C . n 
C 1 122 ASP 122 123 123 ASP ASP C . n 
C 1 123 PRO 123 124 124 PRO PRO C . n 
C 1 124 HIS 124 125 125 HIS HIS C . n 
C 1 125 LEU 125 126 126 LEU LEU C . n 
C 1 126 THR 126 127 127 THR THR C . n 
C 1 127 LYS 127 128 128 LYS LYS C . n 
C 1 128 LEU 128 129 129 LEU LEU C . n 
C 1 129 LEU 129 130 130 LEU LEU C . n 
C 1 130 GLU 130 131 131 GLU GLU C . n 
C 1 131 ASP 131 132 132 ASP ASP C . n 
C 1 132 GLU 132 133 133 GLU GLU C . n 
C 1 133 TYR 133 134 134 TYR TYR C . n 
C 1 134 LEU 134 135 135 LEU LEU C . n 
C 1 135 GLU 135 136 136 GLU GLU C . n 
C 1 136 GLU 136 137 137 GLU GLU C . n 
C 1 137 GLN 137 138 138 GLN GLN C . n 
C 1 138 VAL 138 139 139 VAL VAL C . n 
C 1 139 ASP 139 140 140 ASP ASP C . n 
C 1 140 SER 140 141 141 SER SER C . n 
C 1 141 ILE 141 142 142 ILE ILE C . n 
C 1 142 LYS 142 143 143 LYS LYS C . n 
C 1 143 LYS 143 144 144 LYS LYS C . n 
C 1 144 ILE 144 145 145 ILE ILE C . n 
C 1 145 GLY 145 146 146 GLY GLY C . n 
C 1 146 ASP 146 147 147 ASP ASP C . n 
C 1 147 MET 147 148 148 MET MET C . n 
C 1 148 ILE 148 149 149 ILE ILE C . n 
C 1 149 THR 149 150 150 THR THR C . n 
C 1 150 LYS 150 151 151 LYS LYS C . n 
C 1 151 LEU 151 152 152 LEU LEU C . n 
C 1 152 LYS 152 153 153 LYS LYS C . n 
C 1 153 ARG 153 154 154 ARG ARG C . n 
C 1 154 ALA 154 155 155 ALA ALA C . n 
C 1 155 GLY 155 156 156 GLY GLY C . n 
C 1 156 PRO 156 157 157 PRO PRO C . n 
C 1 157 THR 157 158 158 THR THR C . n 
C 1 158 GLY 158 159 159 GLY GLY C . n 
C 1 159 LEU 159 160 160 LEU LEU C . n 
C 1 160 GLY 160 161 161 GLY GLY C . n 
C 1 161 GLU 161 162 162 GLU GLU C . n 
C 1 162 TYR 162 163 163 TYR TYR C . n 
C 1 163 MET 163 164 164 MET MET C . n 
C 1 164 PHE 164 165 165 PHE PHE C . n 
C 1 165 ASP 165 166 166 ASP ASP C . n 
C 1 166 LYS 166 167 167 LYS LYS C . n 
C 1 167 GLU 167 168 168 GLU GLU C . n 
C 1 168 LEU 168 169 169 LEU LEU C . n 
C 1 169 ASN 169 170 170 ASN ASN C . n 
D 1 1   ALA 1   2   2   ALA ALA D . n 
D 1 2   SER 2   3   3   SER SER D . n 
D 1 3   GLN 3   4   4   GLN GLN D . n 
D 1 4   VAL 4   5   5   VAL VAL D . n 
D 1 5   ARG 5   6   6   ARG ARG D . n 
D 1 6   GLN 6   7   7   GLN GLN D . n 
D 1 7   ASN 7   8   8   ASN ASN D . n 
D 1 8   TYR 8   9   9   TYR TYR D . n 
D 1 9   HIS 9   10  10  HIS HIS D . n 
D 1 10  GLU 10  11  11  GLU GLU D . n 
D 1 11  ASP 11  12  12  ASP ASP D . n 
D 1 12  ALA 12  13  13  ALA ALA D . n 
D 1 13  GLU 13  14  14  GLU GLU D . n 
D 1 14  ALA 14  15  15  ALA ALA D . n 
D 1 15  SER 15  16  16  SER SER D . n 
D 1 16  ILE 16  17  17  ILE ILE D . n 
D 1 17  ASN 17  18  18  ASN ASN D . n 
D 1 18  LYS 18  19  19  LYS LYS D . n 
D 1 19  GLN 19  20  20  GLN GLN D . n 
D 1 20  ILE 20  21  21  ILE ILE D . n 
D 1 21  ASN 21  22  22  ASN ASN D . n 
D 1 22  MET 22  23  23  MET MET D . n 
D 1 23  CYS 23  24  24  CYS CYS D . n 
D 1 24  LEU 24  25  25  LEU LEU D . n 
D 1 25  TYR 25  26  26  TYR TYR D . n 
D 1 26  ALA 26  27  27  ALA ALA D . n 
D 1 27  SER 27  28  28  SER SER D . n 
D 1 28  TYR 28  29  29  TYR TYR D . n 
D 1 29  VAL 29  30  30  VAL VAL D . n 
D 1 30  TYR 30  31  31  TYR TYR D . n 
D 1 31  LEU 31  32  32  LEU LEU D . n 
D 1 32  SER 32  33  33  SER SER D . n 
D 1 33  MET 33  34  34  MET MET D . n 
D 1 34  ALA 34  35  35  ALA ALA D . n 
D 1 35  TYR 35  36  36  TYR TYR D . n 
D 1 36  TYR 36  37  37  TYR TYR D . n 
D 1 37  PHE 37  38  38  PHE PHE D . n 
D 1 38  GLU 38  39  39  GLU GLU D . n 
D 1 39  ARG 39  40  40  ARG ARG D . n 
D 1 40  ASP 40  41  41  ASP ASP D . n 
D 1 41  ASP 41  42  42  ASP ASP D . n 
D 1 42  VAL 42  43  43  VAL VAL D . n 
D 1 43  ALA 43  44  44  ALA ALA D . n 
D 1 44  LEU 44  45  45  LEU LEU D . n 
D 1 45  PRO 45  46  46  PRO PRO D . n 
D 1 46  GLY 46  47  47  GLY GLY D . n 
D 1 47  PHE 47  48  48  PHE PHE D . n 
D 1 48  ALA 48  49  49  ALA ALA D . n 
D 1 49  LYS 49  50  50  LYS LYS D . n 
D 1 50  PHE 50  51  51  PHE PHE D . n 
D 1 51  PHE 51  52  52  PHE PHE D . n 
D 1 52  LYS 52  53  53  LYS LYS D . n 
D 1 53  GLU 53  54  54  GLU GLU D . n 
D 1 54  SER 54  55  55  SER SER D . n 
D 1 55  SER 55  56  56  SER SER D . n 
D 1 56  ASP 56  57  57  ASP ASP D . n 
D 1 57  CYS 57  58  58  CYS CYS D . n 
D 1 58  CYS 58  59  59  CYS CYS D . n 
D 1 59  ARG 59  60  60  ARG ARG D . n 
D 1 60  GLU 60  61  61  GLU GLU D . n 
D 1 61  HIS 61  62  62  HIS HIS D . n 
D 1 62  ALA 62  63  63  ALA ALA D . n 
D 1 63  GLN 63  64  64  GLN GLN D . n 
D 1 64  THR 64  65  65  THR THR D . n 
D 1 65  PHE 65  66  66  PHE PHE D . n 
D 1 66  MET 66  67  67  MET MET D . n 
D 1 67  LYS 67  68  68  LYS LYS D . n 
D 1 68  TYR 68  69  69  TYR TYR D . n 
D 1 69  GLN 69  70  70  GLN GLN D . n 
D 1 70  ASN 70  71  71  ASN ASN D . n 
D 1 71  LYS 71  72  72  LYS LYS D . n 
D 1 72  ARG 72  73  73  ARG ARG D . n 
D 1 73  GLY 73  74  74  GLY GLY D . n 
D 1 74  GLY 74  75  75  GLY GLY D . n 
D 1 75  ARG 75  76  76  ARG ARG D . n 
D 1 76  ILE 76  77  77  ILE ILE D . n 
D 1 77  VAL 77  78  78  VAL VAL D . n 
D 1 78  LEU 78  79  79  LEU LEU D . n 
D 1 79  GLN 79  80  80  GLN GLN D . n 
D 1 80  GLN 80  81  81  GLN GLN D . n 
D 1 81  ILE 81  82  82  ILE ILE D . n 
D 1 82  ALA 82  83  83  ALA ALA D . n 
D 1 83  ALA 83  84  84  ALA ALA D . n 
D 1 84  PRO 84  85  85  PRO PRO D . n 
D 1 85  SER 85  86  86  SER SER D . n 
D 1 86  MET 86  87  87  MET MET D . n 
D 1 87  GLN 87  88  88  GLN GLN D . n 
D 1 88  GLU 88  89  89  GLU GLU D . n 
D 1 89  TRP 89  90  90  TRP TRP D . n 
D 1 90  GLY 90  91  91  GLY GLY D . n 
D 1 91  THR 91  92  92  THR THR D . n 
D 1 92  GLY 92  93  93  GLY GLY D . n 
D 1 93  LEU 93  94  94  LEU LEU D . n 
D 1 94  GLU 94  95  95  GLU GLU D . n 
D 1 95  ALA 95  96  96  ALA ALA D . n 
D 1 96  LEU 96  97  97  LEU LEU D . n 
D 1 97  GLN 97  98  98  GLN GLN D . n 
D 1 98  ALA 98  99  99  ALA ALA D . n 
D 1 99  ALA 99  100 100 ALA ALA D . n 
D 1 100 LEU 100 101 101 LEU LEU D . n 
D 1 101 ASP 101 102 102 ASP ASP D . n 
D 1 102 LEU 102 103 103 LEU LEU D . n 
D 1 103 GLU 103 104 104 GLU GLU D . n 
D 1 104 LYS 104 105 105 LYS LYS D . n 
D 1 105 GLN 105 106 106 GLN GLN D . n 
D 1 106 VAL 106 107 107 VAL VAL D . n 
D 1 107 ASN 107 108 108 ASN ASN D . n 
D 1 108 GLN 108 109 109 GLN GLN D . n 
D 1 109 SER 109 110 110 SER SER D . n 
D 1 110 LEU 110 111 111 LEU LEU D . n 
D 1 111 LEU 111 112 112 LEU LEU D . n 
D 1 112 GLU 112 113 113 GLU GLU D . n 
D 1 113 LEU 113 114 114 LEU LEU D . n 
D 1 114 HIS 114 115 115 HIS HIS D . n 
D 1 115 SER 115 116 116 SER SER D . n 
D 1 116 THR 116 117 117 THR THR D . n 
D 1 117 ALA 117 118 118 ALA ALA D . n 
D 1 118 SER 118 119 119 SER SER D . n 
D 1 119 GLY 119 120 120 GLY GLY D . n 
D 1 120 ASN 120 121 121 ASN ASN D . n 
D 1 121 ASN 121 122 122 ASN ASN D . n 
D 1 122 ASP 122 123 123 ASP ASP D . n 
D 1 123 PRO 123 124 124 PRO PRO D . n 
D 1 124 HIS 124 125 125 HIS HIS D . n 
D 1 125 LEU 125 126 126 LEU LEU D . n 
D 1 126 THR 126 127 127 THR THR D . n 
D 1 127 LYS 127 128 128 LYS LYS D . n 
D 1 128 LEU 128 129 129 LEU LEU D . n 
D 1 129 LEU 129 130 130 LEU LEU D . n 
D 1 130 GLU 130 131 131 GLU GLU D . n 
D 1 131 ASP 131 132 132 ASP ASP D . n 
D 1 132 GLU 132 133 133 GLU GLU D . n 
D 1 133 TYR 133 134 134 TYR TYR D . n 
D 1 134 LEU 134 135 135 LEU LEU D . n 
D 1 135 GLU 135 136 136 GLU GLU D . n 
D 1 136 GLU 136 137 137 GLU GLU D . n 
D 1 137 GLN 137 138 138 GLN GLN D . n 
D 1 138 VAL 138 139 139 VAL VAL D . n 
D 1 139 ASP 139 140 140 ASP ASP D . n 
D 1 140 SER 140 141 141 SER SER D . n 
D 1 141 ILE 141 142 142 ILE ILE D . n 
D 1 142 LYS 142 143 143 LYS LYS D . n 
D 1 143 LYS 143 144 144 LYS LYS D . n 
D 1 144 ILE 144 145 145 ILE ILE D . n 
D 1 145 GLY 145 146 146 GLY GLY D . n 
D 1 146 ASP 146 147 147 ASP ASP D . n 
D 1 147 MET 147 148 148 MET MET D . n 
D 1 148 ILE 148 149 149 ILE ILE D . n 
D 1 149 THR 149 150 150 THR THR D . n 
D 1 150 LYS 150 151 151 LYS LYS D . n 
D 1 151 LEU 151 152 152 LEU LEU D . n 
D 1 152 LYS 152 153 153 LYS LYS D . n 
D 1 153 ARG 153 154 154 ARG ARG D . n 
D 1 154 ALA 154 155 155 ALA ALA D . n 
D 1 155 GLY 155 156 156 GLY GLY D . n 
D 1 156 PRO 156 157 157 PRO PRO D . n 
D 1 157 THR 157 158 158 THR THR D . n 
D 1 158 GLY 158 159 159 GLY GLY D . n 
D 1 159 LEU 159 160 160 LEU LEU D . n 
D 1 160 GLY 160 161 161 GLY GLY D . n 
D 1 161 GLU 161 162 162 GLU GLU D . n 
D 1 162 TYR 162 163 163 TYR TYR D . n 
D 1 163 MET 163 164 164 MET MET D . n 
D 1 164 PHE 164 165 165 PHE PHE D . n 
D 1 165 ASP 165 166 166 ASP ASP D . n 
D 1 166 LYS 166 167 167 LYS LYS D . n 
D 1 167 GLU 167 168 168 GLU GLU D . n 
D 1 168 LEU 168 169 169 LEU LEU D . n 
D 1 169 ASN 169 170 170 ASN ASN D . n 
E 1 1   ALA 1   2   2   ALA ALA E . n 
E 1 2   SER 2   3   3   SER SER E . n 
E 1 3   GLN 3   4   4   GLN GLN E . n 
E 1 4   VAL 4   5   5   VAL VAL E . n 
E 1 5   ARG 5   6   6   ARG ARG E . n 
E 1 6   GLN 6   7   7   GLN GLN E . n 
E 1 7   ASN 7   8   8   ASN ASN E . n 
E 1 8   TYR 8   9   9   TYR TYR E . n 
E 1 9   HIS 9   10  10  HIS HIS E . n 
E 1 10  GLU 10  11  11  GLU GLU E . n 
E 1 11  ASP 11  12  12  ASP ASP E . n 
E 1 12  ALA 12  13  13  ALA ALA E . n 
E 1 13  GLU 13  14  14  GLU GLU E . n 
E 1 14  ALA 14  15  15  ALA ALA E . n 
E 1 15  SER 15  16  16  SER SER E . n 
E 1 16  ILE 16  17  17  ILE ILE E . n 
E 1 17  ASN 17  18  18  ASN ASN E . n 
E 1 18  LYS 18  19  19  LYS LYS E . n 
E 1 19  GLN 19  20  20  GLN GLN E . n 
E 1 20  ILE 20  21  21  ILE ILE E . n 
E 1 21  ASN 21  22  22  ASN ASN E . n 
E 1 22  MET 22  23  23  MET MET E . n 
E 1 23  CYS 23  24  24  CYS CYS E . n 
E 1 24  LEU 24  25  25  LEU LEU E . n 
E 1 25  TYR 25  26  26  TYR TYR E . n 
E 1 26  ALA 26  27  27  ALA ALA E . n 
E 1 27  SER 27  28  28  SER SER E . n 
E 1 28  TYR 28  29  29  TYR TYR E . n 
E 1 29  VAL 29  30  30  VAL VAL E . n 
E 1 30  TYR 30  31  31  TYR TYR E . n 
E 1 31  LEU 31  32  32  LEU LEU E . n 
E 1 32  SER 32  33  33  SER SER E . n 
E 1 33  MET 33  34  34  MET MET E . n 
E 1 34  ALA 34  35  35  ALA ALA E . n 
E 1 35  TYR 35  36  36  TYR TYR E . n 
E 1 36  TYR 36  37  37  TYR TYR E . n 
E 1 37  PHE 37  38  38  PHE PHE E . n 
E 1 38  GLU 38  39  39  GLU GLU E . n 
E 1 39  ARG 39  40  40  ARG ARG E . n 
E 1 40  ASP 40  41  41  ASP ASP E . n 
E 1 41  ASP 41  42  42  ASP ASP E . n 
E 1 42  VAL 42  43  43  VAL VAL E . n 
E 1 43  ALA 43  44  44  ALA ALA E . n 
E 1 44  LEU 44  45  45  LEU LEU E . n 
E 1 45  PRO 45  46  46  PRO PRO E . n 
E 1 46  GLY 46  47  47  GLY GLY E . n 
E 1 47  PHE 47  48  48  PHE PHE E . n 
E 1 48  ALA 48  49  49  ALA ALA E . n 
E 1 49  LYS 49  50  50  LYS LYS E . n 
E 1 50  PHE 50  51  51  PHE PHE E . n 
E 1 51  PHE 51  52  52  PHE PHE E . n 
E 1 52  LYS 52  53  53  LYS LYS E . n 
E 1 53  GLU 53  54  54  GLU GLU E . n 
E 1 54  SER 54  55  55  SER SER E . n 
E 1 55  SER 55  56  56  SER SER E . n 
E 1 56  ASP 56  57  57  ASP ASP E . n 
E 1 57  CYS 57  58  58  CYS CYS E . n 
E 1 58  CYS 58  59  59  CYS CYS E . n 
E 1 59  ARG 59  60  60  ARG ARG E . n 
E 1 60  GLU 60  61  61  GLU GLU E . n 
E 1 61  HIS 61  62  62  HIS HIS E . n 
E 1 62  ALA 62  63  63  ALA ALA E . n 
E 1 63  GLN 63  64  64  GLN GLN E . n 
E 1 64  THR 64  65  65  THR THR E . n 
E 1 65  PHE 65  66  66  PHE PHE E . n 
E 1 66  MET 66  67  67  MET MET E . n 
E 1 67  LYS 67  68  68  LYS LYS E . n 
E 1 68  TYR 68  69  69  TYR TYR E . n 
E 1 69  GLN 69  70  70  GLN GLN E . n 
E 1 70  ASN 70  71  71  ASN ASN E . n 
E 1 71  LYS 71  72  72  LYS LYS E . n 
E 1 72  ARG 72  73  73  ARG ARG E . n 
E 1 73  GLY 73  74  74  GLY GLY E . n 
E 1 74  GLY 74  75  75  GLY GLY E . n 
E 1 75  ARG 75  76  76  ARG ARG E . n 
E 1 76  ILE 76  77  77  ILE ILE E . n 
E 1 77  VAL 77  78  78  VAL VAL E . n 
E 1 78  LEU 78  79  79  LEU LEU E . n 
E 1 79  GLN 79  80  80  GLN GLN E . n 
E 1 80  GLN 80  81  81  GLN GLN E . n 
E 1 81  ILE 81  82  82  ILE ILE E . n 
E 1 82  ALA 82  83  83  ALA ALA E . n 
E 1 83  ALA 83  84  84  ALA ALA E . n 
E 1 84  PRO 84  85  85  PRO PRO E . n 
E 1 85  SER 85  86  86  SER SER E . n 
E 1 86  MET 86  87  87  MET MET E . n 
E 1 87  GLN 87  88  88  GLN GLN E . n 
E 1 88  GLU 88  89  89  GLU GLU E . n 
E 1 89  TRP 89  90  90  TRP TRP E . n 
E 1 90  GLY 90  91  91  GLY GLY E . n 
E 1 91  THR 91  92  92  THR THR E . n 
E 1 92  GLY 92  93  93  GLY GLY E . n 
E 1 93  LEU 93  94  94  LEU LEU E . n 
E 1 94  GLU 94  95  95  GLU GLU E . n 
E 1 95  ALA 95  96  96  ALA ALA E . n 
E 1 96  LEU 96  97  97  LEU LEU E . n 
E 1 97  GLN 97  98  98  GLN GLN E . n 
E 1 98  ALA 98  99  99  ALA ALA E . n 
E 1 99  ALA 99  100 100 ALA ALA E . n 
E 1 100 LEU 100 101 101 LEU LEU E . n 
E 1 101 ASP 101 102 102 ASP ASP E . n 
E 1 102 LEU 102 103 103 LEU LEU E . n 
E 1 103 GLU 103 104 104 GLU GLU E . n 
E 1 104 LYS 104 105 105 LYS LYS E . n 
E 1 105 GLN 105 106 106 GLN GLN E . n 
E 1 106 VAL 106 107 107 VAL VAL E . n 
E 1 107 ASN 107 108 108 ASN ASN E . n 
E 1 108 GLN 108 109 109 GLN GLN E . n 
E 1 109 SER 109 110 110 SER SER E . n 
E 1 110 LEU 110 111 111 LEU LEU E . n 
E 1 111 LEU 111 112 112 LEU LEU E . n 
E 1 112 GLU 112 113 113 GLU GLU E . n 
E 1 113 LEU 113 114 114 LEU LEU E . n 
E 1 114 HIS 114 115 115 HIS HIS E . n 
E 1 115 SER 115 116 116 SER SER E . n 
E 1 116 THR 116 117 117 THR THR E . n 
E 1 117 ALA 117 118 118 ALA ALA E . n 
E 1 118 SER 118 119 119 SER SER E . n 
E 1 119 GLY 119 120 120 GLY GLY E . n 
E 1 120 ASN 120 121 121 ASN ASN E . n 
E 1 121 ASN 121 122 122 ASN ASN E . n 
E 1 122 ASP 122 123 123 ASP ASP E . n 
E 1 123 PRO 123 124 124 PRO PRO E . n 
E 1 124 HIS 124 125 125 HIS HIS E . n 
E 1 125 LEU 125 126 126 LEU LEU E . n 
E 1 126 THR 126 127 127 THR THR E . n 
E 1 127 LYS 127 128 128 LYS LYS E . n 
E 1 128 LEU 128 129 129 LEU LEU E . n 
E 1 129 LEU 129 130 130 LEU LEU E . n 
E 1 130 GLU 130 131 131 GLU GLU E . n 
E 1 131 ASP 131 132 132 ASP ASP E . n 
E 1 132 GLU 132 133 133 GLU GLU E . n 
E 1 133 TYR 133 134 134 TYR TYR E . n 
E 1 134 LEU 134 135 135 LEU LEU E . n 
E 1 135 GLU 135 136 136 GLU GLU E . n 
E 1 136 GLU 136 137 137 GLU GLU E . n 
E 1 137 GLN 137 138 138 GLN GLN E . n 
E 1 138 VAL 138 139 139 VAL VAL E . n 
E 1 139 ASP 139 140 140 ASP ASP E . n 
E 1 140 SER 140 141 141 SER SER E . n 
E 1 141 ILE 141 142 142 ILE ILE E . n 
E 1 142 LYS 142 143 143 LYS LYS E . n 
E 1 143 LYS 143 144 144 LYS LYS E . n 
E 1 144 ILE 144 145 145 ILE ILE E . n 
E 1 145 GLY 145 146 146 GLY GLY E . n 
E 1 146 ASP 146 147 147 ASP ASP E . n 
E 1 147 MET 147 148 148 MET MET E . n 
E 1 148 ILE 148 149 149 ILE ILE E . n 
E 1 149 THR 149 150 150 THR THR E . n 
E 1 150 LYS 150 151 151 LYS LYS E . n 
E 1 151 LEU 151 152 152 LEU LEU E . n 
E 1 152 LYS 152 153 153 LYS LYS E . n 
E 1 153 ARG 153 154 154 ARG ARG E . n 
E 1 154 ALA 154 155 155 ALA ALA E . n 
E 1 155 GLY 155 156 156 GLY GLY E . n 
E 1 156 PRO 156 157 157 PRO PRO E . n 
E 1 157 THR 157 158 158 THR THR E . n 
E 1 158 GLY 158 159 159 GLY GLY E . n 
E 1 159 LEU 159 160 160 LEU LEU E . n 
E 1 160 GLY 160 161 161 GLY GLY E . n 
E 1 161 GLU 161 162 162 GLU GLU E . n 
E 1 162 TYR 162 163 163 TYR TYR E . n 
E 1 163 MET 163 164 164 MET MET E . n 
E 1 164 PHE 164 165 165 PHE PHE E . n 
E 1 165 ASP 165 166 166 ASP ASP E . n 
E 1 166 LYS 166 167 167 LYS LYS E . n 
E 1 167 GLU 167 168 168 GLU GLU E . n 
E 1 168 LEU 168 169 169 LEU LEU E . n 
E 1 169 ASN 169 170 170 ASN ASN E . n 
F 1 1   ALA 1   2   2   ALA ALA F . n 
F 1 2   SER 2   3   3   SER SER F . n 
F 1 3   GLN 3   4   4   GLN GLN F . n 
F 1 4   VAL 4   5   5   VAL VAL F . n 
F 1 5   ARG 5   6   6   ARG ARG F . n 
F 1 6   GLN 6   7   7   GLN GLN F . n 
F 1 7   ASN 7   8   8   ASN ASN F . n 
F 1 8   TYR 8   9   9   TYR TYR F . n 
F 1 9   HIS 9   10  10  HIS HIS F . n 
F 1 10  GLU 10  11  11  GLU GLU F . n 
F 1 11  ASP 11  12  12  ASP ASP F . n 
F 1 12  ALA 12  13  13  ALA ALA F . n 
F 1 13  GLU 13  14  14  GLU GLU F . n 
F 1 14  ALA 14  15  15  ALA ALA F . n 
F 1 15  SER 15  16  16  SER SER F . n 
F 1 16  ILE 16  17  17  ILE ILE F . n 
F 1 17  ASN 17  18  18  ASN ASN F . n 
F 1 18  LYS 18  19  19  LYS LYS F . n 
F 1 19  GLN 19  20  20  GLN GLN F . n 
F 1 20  ILE 20  21  21  ILE ILE F . n 
F 1 21  ASN 21  22  22  ASN ASN F . n 
F 1 22  MET 22  23  23  MET MET F . n 
F 1 23  CYS 23  24  24  CYS CYS F . n 
F 1 24  LEU 24  25  25  LEU LEU F . n 
F 1 25  TYR 25  26  26  TYR TYR F . n 
F 1 26  ALA 26  27  27  ALA ALA F . n 
F 1 27  SER 27  28  28  SER SER F . n 
F 1 28  TYR 28  29  29  TYR TYR F . n 
F 1 29  VAL 29  30  30  VAL VAL F . n 
F 1 30  TYR 30  31  31  TYR TYR F . n 
F 1 31  LEU 31  32  32  LEU LEU F . n 
F 1 32  SER 32  33  33  SER SER F . n 
F 1 33  MET 33  34  34  MET MET F . n 
F 1 34  ALA 34  35  35  ALA ALA F . n 
F 1 35  TYR 35  36  36  TYR TYR F . n 
F 1 36  TYR 36  37  37  TYR TYR F . n 
F 1 37  PHE 37  38  38  PHE PHE F . n 
F 1 38  GLU 38  39  39  GLU GLU F . n 
F 1 39  ARG 39  40  40  ARG ARG F . n 
F 1 40  ASP 40  41  41  ASP ASP F . n 
F 1 41  ASP 41  42  42  ASP ASP F . n 
F 1 42  VAL 42  43  43  VAL VAL F . n 
F 1 43  ALA 43  44  44  ALA ALA F . n 
F 1 44  LEU 44  45  45  LEU LEU F . n 
F 1 45  PRO 45  46  46  PRO PRO F . n 
F 1 46  GLY 46  47  47  GLY GLY F . n 
F 1 47  PHE 47  48  48  PHE PHE F . n 
F 1 48  ALA 48  49  49  ALA ALA F . n 
F 1 49  LYS 49  50  50  LYS LYS F . n 
F 1 50  PHE 50  51  51  PHE PHE F . n 
F 1 51  PHE 51  52  52  PHE PHE F . n 
F 1 52  LYS 52  53  53  LYS LYS F . n 
F 1 53  GLU 53  54  54  GLU GLU F . n 
F 1 54  SER 54  55  55  SER SER F . n 
F 1 55  SER 55  56  56  SER SER F . n 
F 1 56  ASP 56  57  57  ASP ASP F . n 
F 1 57  CYS 57  58  58  CYS CYS F . n 
F 1 58  CYS 58  59  59  CYS CYS F . n 
F 1 59  ARG 59  60  60  ARG ARG F . n 
F 1 60  GLU 60  61  61  GLU GLU F . n 
F 1 61  HIS 61  62  62  HIS HIS F . n 
F 1 62  ALA 62  63  63  ALA ALA F . n 
F 1 63  GLN 63  64  64  GLN GLN F . n 
F 1 64  THR 64  65  65  THR THR F . n 
F 1 65  PHE 65  66  66  PHE PHE F . n 
F 1 66  MET 66  67  67  MET MET F . n 
F 1 67  LYS 67  68  68  LYS LYS F . n 
F 1 68  TYR 68  69  69  TYR TYR F . n 
F 1 69  GLN 69  70  70  GLN GLN F . n 
F 1 70  ASN 70  71  71  ASN ASN F . n 
F 1 71  LYS 71  72  72  LYS LYS F . n 
F 1 72  ARG 72  73  73  ARG ARG F . n 
F 1 73  GLY 73  74  74  GLY GLY F . n 
F 1 74  GLY 74  75  75  GLY GLY F . n 
F 1 75  ARG 75  76  76  ARG ARG F . n 
F 1 76  ILE 76  77  77  ILE ILE F . n 
F 1 77  VAL 77  78  78  VAL VAL F . n 
F 1 78  LEU 78  79  79  LEU LEU F . n 
F 1 79  GLN 79  80  80  GLN GLN F . n 
F 1 80  GLN 80  81  81  GLN GLN F . n 
F 1 81  ILE 81  82  82  ILE ILE F . n 
F 1 82  ALA 82  83  83  ALA ALA F . n 
F 1 83  ALA 83  84  84  ALA ALA F . n 
F 1 84  PRO 84  85  85  PRO PRO F . n 
F 1 85  SER 85  86  86  SER SER F . n 
F 1 86  MET 86  87  87  MET MET F . n 
F 1 87  GLN 87  88  88  GLN GLN F . n 
F 1 88  GLU 88  89  89  GLU GLU F . n 
F 1 89  TRP 89  90  90  TRP TRP F . n 
F 1 90  GLY 90  91  91  GLY GLY F . n 
F 1 91  THR 91  92  92  THR THR F . n 
F 1 92  GLY 92  93  93  GLY GLY F . n 
F 1 93  LEU 93  94  94  LEU LEU F . n 
F 1 94  GLU 94  95  95  GLU GLU F . n 
F 1 95  ALA 95  96  96  ALA ALA F . n 
F 1 96  LEU 96  97  97  LEU LEU F . n 
F 1 97  GLN 97  98  98  GLN GLN F . n 
F 1 98  ALA 98  99  99  ALA ALA F . n 
F 1 99  ALA 99  100 100 ALA ALA F . n 
F 1 100 LEU 100 101 101 LEU LEU F . n 
F 1 101 ASP 101 102 102 ASP ASP F . n 
F 1 102 LEU 102 103 103 LEU LEU F . n 
F 1 103 GLU 103 104 104 GLU GLU F . n 
F 1 104 LYS 104 105 105 LYS LYS F . n 
F 1 105 GLN 105 106 106 GLN GLN F . n 
F 1 106 VAL 106 107 107 VAL VAL F . n 
F 1 107 ASN 107 108 108 ASN ASN F . n 
F 1 108 GLN 108 109 109 GLN GLN F . n 
F 1 109 SER 109 110 110 SER SER F . n 
F 1 110 LEU 110 111 111 LEU LEU F . n 
F 1 111 LEU 111 112 112 LEU LEU F . n 
F 1 112 GLU 112 113 113 GLU GLU F . n 
F 1 113 LEU 113 114 114 LEU LEU F . n 
F 1 114 HIS 114 115 115 HIS HIS F . n 
F 1 115 SER 115 116 116 SER SER F . n 
F 1 116 THR 116 117 117 THR THR F . n 
F 1 117 ALA 117 118 118 ALA ALA F . n 
F 1 118 SER 118 119 119 SER SER F . n 
F 1 119 GLY 119 120 120 GLY GLY F . n 
F 1 120 ASN 120 121 121 ASN ASN F . n 
F 1 121 ASN 121 122 122 ASN ASN F . n 
F 1 122 ASP 122 123 123 ASP ASP F . n 
F 1 123 PRO 123 124 124 PRO PRO F . n 
F 1 124 HIS 124 125 125 HIS HIS F . n 
F 1 125 LEU 125 126 126 LEU LEU F . n 
F 1 126 THR 126 127 127 THR THR F . n 
F 1 127 LYS 127 128 128 LYS LYS F . n 
F 1 128 LEU 128 129 129 LEU LEU F . n 
F 1 129 LEU 129 130 130 LEU LEU F . n 
F 1 130 GLU 130 131 131 GLU GLU F . n 
F 1 131 ASP 131 132 132 ASP ASP F . n 
F 1 132 GLU 132 133 133 GLU GLU F . n 
F 1 133 TYR 133 134 134 TYR TYR F . n 
F 1 134 LEU 134 135 135 LEU LEU F . n 
F 1 135 GLU 135 136 136 GLU GLU F . n 
F 1 136 GLU 136 137 137 GLU GLU F . n 
F 1 137 GLN 137 138 138 GLN GLN F . n 
F 1 138 VAL 138 139 139 VAL VAL F . n 
F 1 139 ASP 139 140 140 ASP ASP F . n 
F 1 140 SER 140 141 141 SER SER F . n 
F 1 141 ILE 141 142 142 ILE ILE F . n 
F 1 142 LYS 142 143 143 LYS LYS F . n 
F 1 143 LYS 143 144 144 LYS LYS F . n 
F 1 144 ILE 144 145 145 ILE ILE F . n 
F 1 145 GLY 145 146 146 GLY GLY F . n 
F 1 146 ASP 146 147 147 ASP ASP F . n 
F 1 147 MET 147 148 148 MET MET F . n 
F 1 148 ILE 148 149 149 ILE ILE F . n 
F 1 149 THR 149 150 150 THR THR F . n 
F 1 150 LYS 150 151 151 LYS LYS F . n 
F 1 151 LEU 151 152 152 LEU LEU F . n 
F 1 152 LYS 152 153 153 LYS LYS F . n 
F 1 153 ARG 153 154 154 ARG ARG F . n 
F 1 154 ALA 154 155 155 ALA ALA F . n 
F 1 155 GLY 155 156 156 GLY GLY F . n 
F 1 156 PRO 156 157 157 PRO PRO F . n 
F 1 157 THR 157 158 158 THR THR F . n 
F 1 158 GLY 158 159 159 GLY GLY F . n 
F 1 159 LEU 159 160 160 LEU LEU F . n 
F 1 160 GLY 160 161 161 GLY GLY F . n 
F 1 161 GLU 161 162 162 GLU GLU F . n 
F 1 162 TYR 162 163 163 TYR TYR F . n 
F 1 163 MET 163 164 164 MET MET F . n 
F 1 164 PHE 164 165 165 PHE PHE F . n 
F 1 165 ASP 165 166 166 ASP ASP F . n 
F 1 166 LYS 166 167 167 LYS LYS F . n 
F 1 167 GLU 167 168 168 GLU GLU F . n 
F 1 168 LEU 168 169 169 LEU LEU F . n 
F 1 169 ASN 169 170 170 ASN ASN F . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 H2S ? ? H2S ? ? 'SUBJECT OF INVESTIGATION' ? 
2 CD  ? ? CD  ? ? 'SUBJECT OF INVESTIGATION' ? 
3 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
4 SO4 ? ? SO4 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 
G  2 CD  1  201 6   CD  CD  A . 
H  2 CD  1  202 12  CD  CD  A . 
I  2 CD  1  203 17  CD  CD  A . 
J  2 CD  1  204 24  CD  CD  A . 
K  3 H2S 1  205 15  H2S S   A . 
L  3 H2S 1  206 25  H2S S   A . 
M  3 H2S 1  207 33  H2S S   A . 
N  3 H2S 1  208 34  H2S S   A . 
O  3 H2S 1  209 35  H2S S   A . 
P  3 H2S 1  210 80  H2S S   A . 
Q  4 MG  1  211 3   MG  MG  A . 
R  5 SO4 1  212 3   SO4 SO4 A . 
S  5 SO4 1  213 7   SO4 SO4 A . 
T  2 CD  1  201 3   CD  CD  B . 
U  2 CD  1  202 7   CD  CD  B . 
V  2 CD  1  203 16  CD  CD  B . 
W  2 CD  1  204 20  CD  CD  B . 
X  3 H2S 1  205 1   H2S S   B . 
Y  3 H2S 1  206 5   H2S S   B . 
Z  3 H2S 1  207 6   H2S S   B . 
AA 3 H2S 1  208 28  H2S S   B . 
BA 3 H2S 1  209 53  H2S S   B . 
CA 5 SO4 1  210 6   SO4 SO4 B . 
DA 2 CD  1  201 1   CD  CD  C . 
EA 2 CD  1  202 11  CD  CD  C . 
FA 2 CD  1  203 13  CD  CD  C . 
GA 2 CD  1  204 22  CD  CD  C . 
HA 3 H2S 1  205 4   H2S S   C . 
IA 3 H2S 1  206 26  H2S S   C . 
JA 3 H2S 1  207 27  H2S S   C . 
KA 3 H2S 1  208 45  H2S S   C . 
LA 3 H2S 1  209 46  H2S S   C . 
MA 3 H2S 1  210 47  H2S S   C . 
NA 4 MG  1  211 5   MG  MG  C . 
OA 5 SO4 1  212 5   SO4 SO4 C . 
PA 2 CD  1  201 2   CD  CD  D . 
QA 2 CD  1  202 9   CD  CD  D . 
RA 2 CD  1  203 14  CD  CD  D . 
SA 2 CD  1  204 21  CD  CD  D . 
TA 3 H2S 1  205 13  H2S S   D . 
UA 3 H2S 1  206 14  H2S S   D . 
VA 3 H2S 1  207 16  H2S S   D . 
WA 3 H2S 1  208 18  H2S S   D . 
XA 3 H2S 1  209 50  H2S S   D . 
YA 3 H2S 1  210 63  H2S S   D . 
ZA 3 H2S 1  211 81  H2S S   D . 
AB 4 MG  1  212 1   MG  MG  D . 
BB 4 MG  1  213 4   MG  MG  D . 
CB 5 SO4 1  214 2   SO4 SO4 D . 
DB 2 CD  1  201 5   CD  CD  E . 
EB 2 CD  1  202 10  CD  CD  E . 
FB 2 CD  1  203 15  CD  CD  E . 
GB 2 CD  1  204 23  CD  CD  E . 
HB 3 H2S 1  205 23  H2S S   E . 
IB 3 H2S 1  206 58  H2S S   E . 
JB 3 H2S 1  207 59  H2S S   E . 
KB 3 H2S 1  208 75  H2S S   E . 
LB 3 H2S 1  209 83  H2S S   E . 
MB 3 H2S 1  210 84  H2S S   E . 
NB 4 MG  1  211 2   MG  MG  E . 
OB 5 SO4 1  212 1   SO4 SO4 E . 
PB 2 CD  1  201 4   CD  CD  F . 
QB 2 CD  1  202 8   CD  CD  F . 
RB 2 CD  1  203 18  CD  CD  F . 
SB 2 CD  1  204 19  CD  CD  F . 
TB 3 H2S 1  205 12  H2S S   F . 
UB 3 H2S 1  206 20  H2S S   F . 
VB 3 H2S 1  207 21  H2S S   F . 
WB 3 H2S 1  208 40  H2S S   F . 
XB 3 H2S 1  209 78  H2S S   F . 
YB 4 MG  1  210 7   MG  MG  F . 
ZB 5 SO4 1  211 4   SO4 SO4 F . 
AC 6 HOH 1  301 162 HOH HOH A . 
AC 6 HOH 2  302 374 HOH HOH A . 
AC 6 HOH 3  303 367 HOH HOH A . 
AC 6 HOH 4  304 482 HOH HOH A . 
AC 6 HOH 5  305 314 HOH HOH A . 
AC 6 HOH 6  306 164 HOH HOH A . 
AC 6 HOH 7  307 35  HOH HOH A . 
AC 6 HOH 8  308 290 HOH HOH A . 
AC 6 HOH 9  309 73  HOH HOH A . 
AC 6 HOH 10 310 281 HOH HOH A . 
AC 6 HOH 11 311 22  HOH HOH A . 
AC 6 HOH 12 312 92  HOH HOH A . 
AC 6 HOH 13 313 422 HOH HOH A . 
AC 6 HOH 14 314 402 HOH HOH A . 
AC 6 HOH 15 315 238 HOH HOH A . 
AC 6 HOH 16 316 29  HOH HOH A . 
AC 6 HOH 17 317 114 HOH HOH A . 
AC 6 HOH 18 318 393 HOH HOH A . 
AC 6 HOH 19 319 219 HOH HOH A . 
AC 6 HOH 20 320 473 HOH HOH A . 
AC 6 HOH 21 321 325 HOH HOH A . 
AC 6 HOH 22 322 33  HOH HOH A . 
AC 6 HOH 23 323 51  HOH HOH A . 
AC 6 HOH 24 324 520 HOH HOH A . 
AC 6 HOH 25 325 98  HOH HOH A . 
AC 6 HOH 26 326 1   HOH HOH A . 
AC 6 HOH 27 327 270 HOH HOH A . 
AC 6 HOH 28 328 245 HOH HOH A . 
AC 6 HOH 29 329 148 HOH HOH A . 
AC 6 HOH 30 330 183 HOH HOH A . 
AC 6 HOH 31 331 2   HOH HOH A . 
AC 6 HOH 32 332 103 HOH HOH A . 
AC 6 HOH 33 333 203 HOH HOH A . 
AC 6 HOH 34 334 77  HOH HOH A . 
AC 6 HOH 35 335 160 HOH HOH A . 
AC 6 HOH 36 336 236 HOH HOH A . 
AC 6 HOH 37 337 27  HOH HOH A . 
AC 6 HOH 38 338 217 HOH HOH A . 
AC 6 HOH 39 339 79  HOH HOH A . 
AC 6 HOH 40 340 381 HOH HOH A . 
AC 6 HOH 41 341 145 HOH HOH A . 
AC 6 HOH 42 342 126 HOH HOH A . 
AC 6 HOH 43 343 184 HOH HOH A . 
AC 6 HOH 44 344 354 HOH HOH A . 
AC 6 HOH 45 345 147 HOH HOH A . 
AC 6 HOH 46 346 368 HOH HOH A . 
AC 6 HOH 47 347 431 HOH HOH A . 
AC 6 HOH 48 348 130 HOH HOH A . 
AC 6 HOH 49 349 250 HOH HOH A . 
AC 6 HOH 50 350 417 HOH HOH A . 
AC 6 HOH 51 351 138 HOH HOH A . 
AC 6 HOH 52 352 95  HOH HOH A . 
AC 6 HOH 53 353 441 HOH HOH A . 
AC 6 HOH 54 354 275 HOH HOH A . 
AC 6 HOH 55 355 412 HOH HOH A . 
AC 6 HOH 56 356 382 HOH HOH A . 
AC 6 HOH 57 357 16  HOH HOH A . 
AC 6 HOH 58 358 156 HOH HOH A . 
AC 6 HOH 59 359 502 HOH HOH A . 
AC 6 HOH 60 360 315 HOH HOH A . 
AC 6 HOH 61 361 350 HOH HOH A . 
AC 6 HOH 62 362 428 HOH HOH A . 
AC 6 HOH 63 363 450 HOH HOH A . 
AC 6 HOH 64 364 277 HOH HOH A . 
AC 6 HOH 65 365 463 HOH HOH A . 
AC 6 HOH 66 366 312 HOH HOH A . 
AC 6 HOH 67 367 67  HOH HOH A . 
AC 6 HOH 68 368 46  HOH HOH A . 
AC 6 HOH 69 369 378 HOH HOH A . 
AC 6 HOH 70 370 336 HOH HOH A . 
AC 6 HOH 71 371 358 HOH HOH A . 
AC 6 HOH 72 372 274 HOH HOH A . 
AC 6 HOH 73 373 505 HOH HOH A . 
AC 6 HOH 74 374 426 HOH HOH A . 
AC 6 HOH 75 375 529 HOH HOH A . 
AC 6 HOH 76 376 226 HOH HOH A . 
AC 6 HOH 77 377 120 HOH HOH A . 
AC 6 HOH 78 378 492 HOH HOH A . 
AC 6 HOH 79 379 70  HOH HOH A . 
AC 6 HOH 80 380 298 HOH HOH A . 
AC 6 HOH 81 381 389 HOH HOH A . 
AC 6 HOH 82 382 508 HOH HOH A . 
AC 6 HOH 83 383 459 HOH HOH A . 
AC 6 HOH 84 384 499 HOH HOH A . 
AC 6 HOH 85 385 304 HOH HOH A . 
AC 6 HOH 86 386 108 HOH HOH A . 
AC 6 HOH 87 387 458 HOH HOH A . 
AC 6 HOH 88 388 525 HOH HOH A . 
BC 6 HOH 1  301 85  HOH HOH B . 
BC 6 HOH 2  302 299 HOH HOH B . 
BC 6 HOH 3  303 141 HOH HOH B . 
BC 6 HOH 4  304 391 HOH HOH B . 
BC 6 HOH 5  305 18  HOH HOH B . 
BC 6 HOH 6  306 521 HOH HOH B . 
BC 6 HOH 7  307 268 HOH HOH B . 
BC 6 HOH 8  308 516 HOH HOH B . 
BC 6 HOH 9  309 28  HOH HOH B . 
BC 6 HOH 10 310 192 HOH HOH B . 
BC 6 HOH 11 311 376 HOH HOH B . 
BC 6 HOH 12 312 284 HOH HOH B . 
BC 6 HOH 13 313 37  HOH HOH B . 
BC 6 HOH 14 314 353 HOH HOH B . 
BC 6 HOH 15 315 193 HOH HOH B . 
BC 6 HOH 16 316 373 HOH HOH B . 
BC 6 HOH 17 317 286 HOH HOH B . 
BC 6 HOH 18 318 385 HOH HOH B . 
BC 6 HOH 19 319 112 HOH HOH B . 
BC 6 HOH 20 320 215 HOH HOH B . 
BC 6 HOH 21 321 111 HOH HOH B . 
BC 6 HOH 22 322 62  HOH HOH B . 
BC 6 HOH 23 323 68  HOH HOH B . 
BC 6 HOH 24 324 259 HOH HOH B . 
BC 6 HOH 25 325 248 HOH HOH B . 
BC 6 HOH 26 326 204 HOH HOH B . 
BC 6 HOH 27 327 52  HOH HOH B . 
BC 6 HOH 28 328 334 HOH HOH B . 
BC 6 HOH 29 329 9   HOH HOH B . 
BC 6 HOH 30 330 17  HOH HOH B . 
BC 6 HOH 31 331 488 HOH HOH B . 
BC 6 HOH 32 332 195 HOH HOH B . 
BC 6 HOH 33 333 149 HOH HOH B . 
BC 6 HOH 34 334 50  HOH HOH B . 
BC 6 HOH 35 335 246 HOH HOH B . 
BC 6 HOH 36 336 276 HOH HOH B . 
BC 6 HOH 37 337 351 HOH HOH B . 
BC 6 HOH 38 338 21  HOH HOH B . 
BC 6 HOH 39 339 200 HOH HOH B . 
BC 6 HOH 40 340 139 HOH HOH B . 
BC 6 HOH 41 341 498 HOH HOH B . 
BC 6 HOH 42 342 82  HOH HOH B . 
BC 6 HOH 43 343 93  HOH HOH B . 
BC 6 HOH 44 344 396 HOH HOH B . 
BC 6 HOH 45 345 174 HOH HOH B . 
BC 6 HOH 46 346 285 HOH HOH B . 
BC 6 HOH 47 347 237 HOH HOH B . 
BC 6 HOH 48 348 40  HOH HOH B . 
BC 6 HOH 49 349 134 HOH HOH B . 
BC 6 HOH 50 350 500 HOH HOH B . 
BC 6 HOH 51 351 265 HOH HOH B . 
BC 6 HOH 52 352 151 HOH HOH B . 
BC 6 HOH 53 353 161 HOH HOH B . 
BC 6 HOH 54 354 366 HOH HOH B . 
BC 6 HOH 55 355 416 HOH HOH B . 
BC 6 HOH 56 356 242 HOH HOH B . 
BC 6 HOH 57 357 359 HOH HOH B . 
BC 6 HOH 58 358 199 HOH HOH B . 
BC 6 HOH 59 359 106 HOH HOH B . 
BC 6 HOH 60 360 347 HOH HOH B . 
BC 6 HOH 61 361 297 HOH HOH B . 
BC 6 HOH 62 362 455 HOH HOH B . 
BC 6 HOH 63 363 470 HOH HOH B . 
BC 6 HOH 64 364 208 HOH HOH B . 
BC 6 HOH 65 365 317 HOH HOH B . 
BC 6 HOH 66 366 345 HOH HOH B . 
BC 6 HOH 67 367 490 HOH HOH B . 
BC 6 HOH 68 368 75  HOH HOH B . 
BC 6 HOH 69 369 517 HOH HOH B . 
BC 6 HOH 70 370 481 HOH HOH B . 
BC 6 HOH 71 371 178 HOH HOH B . 
BC 6 HOH 72 372 295 HOH HOH B . 
BC 6 HOH 73 373 308 HOH HOH B . 
BC 6 HOH 74 374 328 HOH HOH B . 
BC 6 HOH 75 375 501 HOH HOH B . 
BC 6 HOH 76 376 119 HOH HOH B . 
BC 6 HOH 77 377 511 HOH HOH B . 
BC 6 HOH 78 378 495 HOH HOH B . 
BC 6 HOH 79 379 465 HOH HOH B . 
BC 6 HOH 80 380 340 HOH HOH B . 
BC 6 HOH 81 381 485 HOH HOH B . 
BC 6 HOH 82 382 483 HOH HOH B . 
BC 6 HOH 83 383 379 HOH HOH B . 
BC 6 HOH 84 384 445 HOH HOH B . 
BC 6 HOH 85 385 437 HOH HOH B . 
BC 6 HOH 86 386 493 HOH HOH B . 
BC 6 HOH 87 387 418 HOH HOH B . 
BC 6 HOH 88 388 172 HOH HOH B . 
BC 6 HOH 89 389 122 HOH HOH B . 
BC 6 HOH 90 390 510 HOH HOH B . 
BC 6 HOH 91 391 310 HOH HOH B . 
BC 6 HOH 92 392 451 HOH HOH B . 
BC 6 HOH 93 393 167 HOH HOH B . 
BC 6 HOH 94 394 390 HOH HOH B . 
BC 6 HOH 95 395 272 HOH HOH B . 
CC 6 HOH 1  301 91  HOH HOH C . 
CC 6 HOH 2  302 405 HOH HOH C . 
CC 6 HOH 3  303 471 HOH HOH C . 
CC 6 HOH 4  304 96  HOH HOH C . 
CC 6 HOH 5  305 59  HOH HOH C . 
CC 6 HOH 6  306 320 HOH HOH C . 
CC 6 HOH 7  307 34  HOH HOH C . 
CC 6 HOH 8  308 432 HOH HOH C . 
CC 6 HOH 9  309 339 HOH HOH C . 
CC 6 HOH 10 310 31  HOH HOH C . 
CC 6 HOH 11 311 507 HOH HOH C . 
CC 6 HOH 12 312 78  HOH HOH C . 
CC 6 HOH 13 313 41  HOH HOH C . 
CC 6 HOH 14 314 329 HOH HOH C . 
CC 6 HOH 15 315 232 HOH HOH C . 
CC 6 HOH 16 316 127 HOH HOH C . 
CC 6 HOH 17 317 53  HOH HOH C . 
CC 6 HOH 18 318 446 HOH HOH C . 
CC 6 HOH 19 319 133 HOH HOH C . 
CC 6 HOH 20 320 137 HOH HOH C . 
CC 6 HOH 21 321 302 HOH HOH C . 
CC 6 HOH 22 322 166 HOH HOH C . 
CC 6 HOH 23 323 8   HOH HOH C . 
CC 6 HOH 24 324 159 HOH HOH C . 
CC 6 HOH 25 325 352 HOH HOH C . 
CC 6 HOH 26 326 305 HOH HOH C . 
CC 6 HOH 27 327 56  HOH HOH C . 
CC 6 HOH 28 328 224 HOH HOH C . 
CC 6 HOH 29 329 225 HOH HOH C . 
CC 6 HOH 30 330 409 HOH HOH C . 
CC 6 HOH 31 331 5   HOH HOH C . 
CC 6 HOH 32 332 14  HOH HOH C . 
CC 6 HOH 33 333 323 HOH HOH C . 
CC 6 HOH 34 334 480 HOH HOH C . 
CC 6 HOH 35 335 262 HOH HOH C . 
CC 6 HOH 36 336 369 HOH HOH C . 
CC 6 HOH 37 337 332 HOH HOH C . 
CC 6 HOH 38 338 287 HOH HOH C . 
CC 6 HOH 39 339 251 HOH HOH C . 
CC 6 HOH 40 340 154 HOH HOH C . 
CC 6 HOH 41 341 216 HOH HOH C . 
CC 6 HOH 42 342 513 HOH HOH C . 
CC 6 HOH 43 343 460 HOH HOH C . 
CC 6 HOH 44 344 527 HOH HOH C . 
CC 6 HOH 45 345 87  HOH HOH C . 
CC 6 HOH 46 346 469 HOH HOH C . 
CC 6 HOH 47 347 211 HOH HOH C . 
CC 6 HOH 48 348 476 HOH HOH C . 
CC 6 HOH 49 349 414 HOH HOH C . 
CC 6 HOH 50 350 380 HOH HOH C . 
CC 6 HOH 51 351 423 HOH HOH C . 
CC 6 HOH 52 352 253 HOH HOH C . 
CC 6 HOH 53 353 258 HOH HOH C . 
CC 6 HOH 54 354 362 HOH HOH C . 
CC 6 HOH 55 355 168 HOH HOH C . 
CC 6 HOH 56 356 135 HOH HOH C . 
CC 6 HOH 57 357 180 HOH HOH C . 
CC 6 HOH 58 358 472 HOH HOH C . 
CC 6 HOH 59 359 515 HOH HOH C . 
CC 6 HOH 60 360 227 HOH HOH C . 
CC 6 HOH 61 361 401 HOH HOH C . 
CC 6 HOH 62 362 479 HOH HOH C . 
CC 6 HOH 63 363 48  HOH HOH C . 
CC 6 HOH 64 364 448 HOH HOH C . 
CC 6 HOH 65 365 424 HOH HOH C . 
CC 6 HOH 66 366 504 HOH HOH C . 
CC 6 HOH 67 367 355 HOH HOH C . 
CC 6 HOH 68 368 509 HOH HOH C . 
CC 6 HOH 69 369 3   HOH HOH C . 
CC 6 HOH 70 370 333 HOH HOH C . 
CC 6 HOH 71 371 202 HOH HOH C . 
CC 6 HOH 72 372 331 HOH HOH C . 
CC 6 HOH 73 373 491 HOH HOH C . 
CC 6 HOH 74 374 497 HOH HOH C . 
CC 6 HOH 75 375 81  HOH HOH C . 
CC 6 HOH 76 376 406 HOH HOH C . 
CC 6 HOH 77 377 293 HOH HOH C . 
CC 6 HOH 78 378 477 HOH HOH C . 
CC 6 HOH 79 379 269 HOH HOH C . 
CC 6 HOH 80 380 86  HOH HOH C . 
CC 6 HOH 81 381 150 HOH HOH C . 
CC 6 HOH 82 382 313 HOH HOH C . 
DC 6 HOH 1  301 296 HOH HOH D . 
DC 6 HOH 2  302 439 HOH HOH D . 
DC 6 HOH 3  303 360 HOH HOH D . 
DC 6 HOH 4  304 244 HOH HOH D . 
DC 6 HOH 5  305 49  HOH HOH D . 
DC 6 HOH 6  306 124 HOH HOH D . 
DC 6 HOH 7  307 524 HOH HOH D . 
DC 6 HOH 8  308 83  HOH HOH D . 
DC 6 HOH 9  309 97  HOH HOH D . 
DC 6 HOH 10 310 256 HOH HOH D . 
DC 6 HOH 11 311 101 HOH HOH D . 
DC 6 HOH 12 312 318 HOH HOH D . 
DC 6 HOH 13 313 348 HOH HOH D . 
DC 6 HOH 14 314 110 HOH HOH D . 
DC 6 HOH 15 315 12  HOH HOH D . 
DC 6 HOH 16 316 370 HOH HOH D . 
DC 6 HOH 17 317 260 HOH HOH D . 
DC 6 HOH 18 318 453 HOH HOH D . 
DC 6 HOH 19 319 155 HOH HOH D . 
DC 6 HOH 20 320 140 HOH HOH D . 
DC 6 HOH 21 321 283 HOH HOH D . 
DC 6 HOH 22 322 254 HOH HOH D . 
DC 6 HOH 23 323 13  HOH HOH D . 
DC 6 HOH 24 324 25  HOH HOH D . 
DC 6 HOH 25 325 128 HOH HOH D . 
DC 6 HOH 26 326 123 HOH HOH D . 
DC 6 HOH 27 327 278 HOH HOH D . 
DC 6 HOH 28 328 194 HOH HOH D . 
DC 6 HOH 29 329 10  HOH HOH D . 
DC 6 HOH 30 330 462 HOH HOH D . 
DC 6 HOH 31 331 186 HOH HOH D . 
DC 6 HOH 32 332 90  HOH HOH D . 
DC 6 HOH 33 333 19  HOH HOH D . 
DC 6 HOH 34 334 113 HOH HOH D . 
DC 6 HOH 35 335 54  HOH HOH D . 
DC 6 HOH 36 336 99  HOH HOH D . 
DC 6 HOH 37 337 397 HOH HOH D . 
DC 6 HOH 38 338 58  HOH HOH D . 
DC 6 HOH 39 339 255 HOH HOH D . 
DC 6 HOH 40 340 447 HOH HOH D . 
DC 6 HOH 41 341 387 HOH HOH D . 
DC 6 HOH 42 342 228 HOH HOH D . 
DC 6 HOH 43 343 191 HOH HOH D . 
DC 6 HOH 44 344 163 HOH HOH D . 
DC 6 HOH 45 345 152 HOH HOH D . 
DC 6 HOH 46 346 165 HOH HOH D . 
DC 6 HOH 47 347 519 HOH HOH D . 
DC 6 HOH 48 348 209 HOH HOH D . 
DC 6 HOH 49 349 344 HOH HOH D . 
DC 6 HOH 50 350 64  HOH HOH D . 
DC 6 HOH 51 351 330 HOH HOH D . 
DC 6 HOH 52 352 413 HOH HOH D . 
DC 6 HOH 53 353 234 HOH HOH D . 
DC 6 HOH 54 354 375 HOH HOH D . 
DC 6 HOH 55 355 153 HOH HOH D . 
DC 6 HOH 56 356 522 HOH HOH D . 
DC 6 HOH 57 357 487 HOH HOH D . 
DC 6 HOH 58 358 243 HOH HOH D . 
DC 6 HOH 59 359 435 HOH HOH D . 
DC 6 HOH 60 360 206 HOH HOH D . 
DC 6 HOH 61 361 468 HOH HOH D . 
DC 6 HOH 62 362 346 HOH HOH D . 
DC 6 HOH 63 363 6   HOH HOH D . 
DC 6 HOH 64 364 433 HOH HOH D . 
DC 6 HOH 65 365 233 HOH HOH D . 
DC 6 HOH 66 366 494 HOH HOH D . 
DC 6 HOH 67 367 408 HOH HOH D . 
DC 6 HOH 68 368 252 HOH HOH D . 
DC 6 HOH 69 369 364 HOH HOH D . 
DC 6 HOH 70 370 442 HOH HOH D . 
DC 6 HOH 71 371 461 HOH HOH D . 
DC 6 HOH 72 372 456 HOH HOH D . 
DC 6 HOH 73 373 66  HOH HOH D . 
DC 6 HOH 74 374 288 HOH HOH D . 
DC 6 HOH 75 375 399 HOH HOH D . 
DC 6 HOH 76 376 486 HOH HOH D . 
DC 6 HOH 77 377 341 HOH HOH D . 
DC 6 HOH 78 378 104 HOH HOH D . 
DC 6 HOH 79 379 484 HOH HOH D . 
DC 6 HOH 80 380 512 HOH HOH D . 
DC 6 HOH 81 381 530 HOH HOH D . 
DC 6 HOH 82 382 309 HOH HOH D . 
DC 6 HOH 83 383 474 HOH HOH D . 
DC 6 HOH 84 384 372 HOH HOH D . 
DC 6 HOH 85 385 427 HOH HOH D . 
DC 6 HOH 86 386 322 HOH HOH D . 
DC 6 HOH 87 387 421 HOH HOH D . 
DC 6 HOH 88 388 198 HOH HOH D . 
DC 6 HOH 89 389 185 HOH HOH D . 
DC 6 HOH 90 390 173 HOH HOH D . 
DC 6 HOH 91 391 440 HOH HOH D . 
EC 6 HOH 1  301 383 HOH HOH E . 
EC 6 HOH 2  302 223 HOH HOH E . 
EC 6 HOH 3  303 326 HOH HOH E . 
EC 6 HOH 4  304 177 HOH HOH E . 
EC 6 HOH 5  305 518 HOH HOH E . 
EC 6 HOH 6  306 89  HOH HOH E . 
EC 6 HOH 7  307 205 HOH HOH E . 
EC 6 HOH 8  308 300 HOH HOH E . 
EC 6 HOH 9  309 39  HOH HOH E . 
EC 6 HOH 10 310 327 HOH HOH E . 
EC 6 HOH 11 311 222 HOH HOH E . 
EC 6 HOH 12 312 363 HOH HOH E . 
EC 6 HOH 13 313 23  HOH HOH E . 
EC 6 HOH 14 314 496 HOH HOH E . 
EC 6 HOH 15 315 282 HOH HOH E . 
EC 6 HOH 16 316 170 HOH HOH E . 
EC 6 HOH 17 317 171 HOH HOH E . 
EC 6 HOH 18 318 60  HOH HOH E . 
EC 6 HOH 19 319 466 HOH HOH E . 
EC 6 HOH 20 320 292 HOH HOH E . 
EC 6 HOH 21 321 410 HOH HOH E . 
EC 6 HOH 22 322 80  HOH HOH E . 
EC 6 HOH 23 323 365 HOH HOH E . 
EC 6 HOH 24 324 181 HOH HOH E . 
EC 6 HOH 25 325 109 HOH HOH E . 
EC 6 HOH 26 326 84  HOH HOH E . 
EC 6 HOH 27 327 210 HOH HOH E . 
EC 6 HOH 28 328 273 HOH HOH E . 
EC 6 HOH 29 329 105 HOH HOH E . 
EC 6 HOH 30 330 65  HOH HOH E . 
EC 6 HOH 31 331 11  HOH HOH E . 
EC 6 HOH 32 332 20  HOH HOH E . 
EC 6 HOH 33 333 443 HOH HOH E . 
EC 6 HOH 34 334 69  HOH HOH E . 
EC 6 HOH 35 335 356 HOH HOH E . 
EC 6 HOH 36 336 212 HOH HOH E . 
EC 6 HOH 37 337 132 HOH HOH E . 
EC 6 HOH 38 338 478 HOH HOH E . 
EC 6 HOH 39 339 129 HOH HOH E . 
EC 6 HOH 40 340 15  HOH HOH E . 
EC 6 HOH 41 341 230 HOH HOH E . 
EC 6 HOH 42 342 121 HOH HOH E . 
EC 6 HOH 43 343 229 HOH HOH E . 
EC 6 HOH 44 344 388 HOH HOH E . 
EC 6 HOH 45 345 32  HOH HOH E . 
EC 6 HOH 46 346 136 HOH HOH E . 
EC 6 HOH 47 347 425 HOH HOH E . 
EC 6 HOH 48 348 319 HOH HOH E . 
EC 6 HOH 49 349 457 HOH HOH E . 
EC 6 HOH 50 350 349 HOH HOH E . 
EC 6 HOH 51 351 528 HOH HOH E . 
EC 6 HOH 52 352 125 HOH HOH E . 
EC 6 HOH 53 353 454 HOH HOH E . 
EC 6 HOH 54 354 464 HOH HOH E . 
EC 6 HOH 55 355 197 HOH HOH E . 
EC 6 HOH 56 356 523 HOH HOH E . 
EC 6 HOH 57 357 257 HOH HOH E . 
EC 6 HOH 58 358 266 HOH HOH E . 
EC 6 HOH 59 359 449 HOH HOH E . 
EC 6 HOH 60 360 307 HOH HOH E . 
EC 6 HOH 61 361 398 HOH HOH E . 
EC 6 HOH 62 362 146 HOH HOH E . 
EC 6 HOH 63 363 321 HOH HOH E . 
EC 6 HOH 64 364 316 HOH HOH E . 
EC 6 HOH 65 365 175 HOH HOH E . 
EC 6 HOH 66 366 214 HOH HOH E . 
EC 6 HOH 67 367 361 HOH HOH E . 
EC 6 HOH 68 368 43  HOH HOH E . 
EC 6 HOH 69 369 187 HOH HOH E . 
EC 6 HOH 70 370 377 HOH HOH E . 
EC 6 HOH 71 371 342 HOH HOH E . 
EC 6 HOH 72 372 240 HOH HOH E . 
EC 6 HOH 73 373 301 HOH HOH E . 
EC 6 HOH 74 374 395 HOH HOH E . 
EC 6 HOH 75 375 384 HOH HOH E . 
EC 6 HOH 76 376 436 HOH HOH E . 
EC 6 HOH 77 377 420 HOH HOH E . 
EC 6 HOH 78 378 241 HOH HOH E . 
EC 6 HOH 79 379 249 HOH HOH E . 
EC 6 HOH 80 380 467 HOH HOH E . 
EC 6 HOH 81 381 239 HOH HOH E . 
EC 6 HOH 82 382 76  HOH HOH E . 
EC 6 HOH 83 383 94  HOH HOH E . 
EC 6 HOH 84 384 411 HOH HOH E . 
EC 6 HOH 85 385 526 HOH HOH E . 
EC 6 HOH 86 386 267 HOH HOH E . 
EC 6 HOH 87 387 294 HOH HOH E . 
EC 6 HOH 88 388 452 HOH HOH E . 
FC 6 HOH 1  301 231 HOH HOH F . 
FC 6 HOH 2  302 403 HOH HOH F . 
FC 6 HOH 3  303 24  HOH HOH F . 
FC 6 HOH 4  304 30  HOH HOH F . 
FC 6 HOH 5  305 429 HOH HOH F . 
FC 6 HOH 6  306 72  HOH HOH F . 
FC 6 HOH 7  307 306 HOH HOH F . 
FC 6 HOH 8  308 115 HOH HOH F . 
FC 6 HOH 9  309 394 HOH HOH F . 
FC 6 HOH 10 310 36  HOH HOH F . 
FC 6 HOH 11 311 143 HOH HOH F . 
FC 6 HOH 12 312 182 HOH HOH F . 
FC 6 HOH 13 313 142 HOH HOH F . 
FC 6 HOH 14 314 47  HOH HOH F . 
FC 6 HOH 15 315 303 HOH HOH F . 
FC 6 HOH 16 316 57  HOH HOH F . 
FC 6 HOH 17 317 489 HOH HOH F . 
FC 6 HOH 18 318 190 HOH HOH F . 
FC 6 HOH 19 319 261 HOH HOH F . 
FC 6 HOH 20 320 44  HOH HOH F . 
FC 6 HOH 21 321 107 HOH HOH F . 
FC 6 HOH 22 322 7   HOH HOH F . 
FC 6 HOH 23 323 503 HOH HOH F . 
FC 6 HOH 24 324 264 HOH HOH F . 
FC 6 HOH 25 325 117 HOH HOH F . 
FC 6 HOH 26 326 207 HOH HOH F . 
FC 6 HOH 27 327 179 HOH HOH F . 
FC 6 HOH 28 328 392 HOH HOH F . 
FC 6 HOH 29 329 188 HOH HOH F . 
FC 6 HOH 30 330 335 HOH HOH F . 
FC 6 HOH 31 331 371 HOH HOH F . 
FC 6 HOH 32 332 71  HOH HOH F . 
FC 6 HOH 33 333 144 HOH HOH F . 
FC 6 HOH 34 334 280 HOH HOH F . 
FC 6 HOH 35 335 116 HOH HOH F . 
FC 6 HOH 36 336 45  HOH HOH F . 
FC 6 HOH 37 337 218 HOH HOH F . 
FC 6 HOH 38 338 4   HOH HOH F . 
FC 6 HOH 39 339 26  HOH HOH F . 
FC 6 HOH 40 340 221 HOH HOH F . 
FC 6 HOH 41 341 131 HOH HOH F . 
FC 6 HOH 42 342 63  HOH HOH F . 
FC 6 HOH 43 343 42  HOH HOH F . 
FC 6 HOH 44 344 61  HOH HOH F . 
FC 6 HOH 45 345 55  HOH HOH F . 
FC 6 HOH 46 346 506 HOH HOH F . 
FC 6 HOH 47 347 74  HOH HOH F . 
FC 6 HOH 48 348 220 HOH HOH F . 
FC 6 HOH 49 349 430 HOH HOH F . 
FC 6 HOH 50 350 118 HOH HOH F . 
FC 6 HOH 51 351 386 HOH HOH F . 
FC 6 HOH 52 352 263 HOH HOH F . 
FC 6 HOH 53 353 158 HOH HOH F . 
FC 6 HOH 54 354 357 HOH HOH F . 
FC 6 HOH 55 355 407 HOH HOH F . 
FC 6 HOH 56 356 189 HOH HOH F . 
FC 6 HOH 57 357 102 HOH HOH F . 
FC 6 HOH 58 358 415 HOH HOH F . 
FC 6 HOH 59 359 271 HOH HOH F . 
FC 6 HOH 60 360 311 HOH HOH F . 
FC 6 HOH 61 361 434 HOH HOH F . 
FC 6 HOH 62 362 291 HOH HOH F . 
FC 6 HOH 63 363 324 HOH HOH F . 
FC 6 HOH 64 364 196 HOH HOH F . 
FC 6 HOH 65 365 338 HOH HOH F . 
FC 6 HOH 66 366 169 HOH HOH F . 
FC 6 HOH 67 367 279 HOH HOH F . 
FC 6 HOH 68 368 100 HOH HOH F . 
FC 6 HOH 69 369 404 HOH HOH F . 
FC 6 HOH 70 370 337 HOH HOH F . 
FC 6 HOH 71 371 444 HOH HOH F . 
FC 6 HOH 72 372 201 HOH HOH F . 
FC 6 HOH 73 373 400 HOH HOH F . 
FC 6 HOH 74 374 176 HOH HOH F . 
FC 6 HOH 75 375 247 HOH HOH F . 
FC 6 HOH 76 376 88  HOH HOH F . 
FC 6 HOH 77 377 438 HOH HOH F . 
FC 6 HOH 78 378 289 HOH HOH F . 
FC 6 HOH 79 379 343 HOH HOH F . 
FC 6 HOH 80 380 235 HOH HOH F . 
FC 6 HOH 81 381 38  HOH HOH F . 
FC 6 HOH 82 382 157 HOH HOH F . 
FC 6 HOH 83 383 475 HOH HOH F . 
FC 6 HOH 84 384 514 HOH HOH F . 
FC 6 HOH 85 385 419 HOH HOH F . 
FC 6 HOH 86 386 213 HOH HOH F . 
# 
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   ? ? ? '(1.19.2_4158: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZN8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     126.748 
_cell.length_a_esd                 ? 
_cell.length_b                     126.748 
_cell.length_b_esd                 ? 
_cell.length_c                     177.949 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        48 
_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                         8ZN8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                79 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'I 4' 
_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                   8ZN8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.09 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          60.25 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '2.5 M NaCl, 100 mM MgCl2 and 100 mM Tris (pH 7.0)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     300 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER R 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-05-20 
_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   0.987 
_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                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZN8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.25 
_reflns.d_resolution_low                               44.81 
_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                                     129055 
_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                           98 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.34 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_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                                    2.25 
_reflns_shell.d_res_low                                     2.28 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3530 
_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                                  0.998 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8ZN8 
_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                            2.25 
_refine.ls_d_res_low                             44.81 
_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                     129055 
_refine.ls_number_reflns_R_free                  6356 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.66 
_refine.ls_percent_reflns_R_free                 4.93 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1680 
_refine.ls_R_factor_R_free                       0.2074 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1660 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 21.66 
_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                            0.26 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8094 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         100 
_refine_hist.number_atoms_solvent             530 
_refine_hist.number_atoms_total               8724 
_refine_hist.d_res_high                       2.25 
_refine_hist.d_res_low                        44.81 
# 
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' ? 0.008 ? 8283  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.812 ? 11156 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.334 ? 1108  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.043 ? 1178  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 1469  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.25 2.28 . . 251 3530 87.00  . . . . 0.2898 . . . . . . . . . . . 0.3374 
'X-RAY DIFFRACTION' 2.28 2.31 . . 255 4008 97.00  . . . . 0.2676 . . . . . . . . . . . 0.2862 
'X-RAY DIFFRACTION' 2.31 2.33 . . 98  4219 99.00  . . . . 0.2422 . . . . . . . . . . . 0.2696 
'X-RAY DIFFRACTION' 2.33 2.36 . . 135 4101 99.00  . . . . 0.2233 . . . . . . . . . . . 0.2837 
'X-RAY DIFFRACTION' 2.36 2.39 . . 194 4154 99.00  . . . . 0.2185 . . . . . . . . . . . 0.2730 
'X-RAY DIFFRACTION' 2.39 2.43 . . 276 4089 99.00  . . . . 0.2183 . . . . . . . . . . . 0.2454 
'X-RAY DIFFRACTION' 2.43 2.46 . . 217 4018 99.00  . . . . 0.2050 . . . . . . . . . . . 0.2936 
'X-RAY DIFFRACTION' 2.46 2.50 . . 187 4110 99.00  . . . . 0.2136 . . . . . . . . . . . 0.2683 
'X-RAY DIFFRACTION' 2.50 2.54 . . 199 4151 99.00  . . . . 0.2101 . . . . . . . . . . . 0.2447 
'X-RAY DIFFRACTION' 2.54 2.58 . . 233 4123 99.00  . . . . 0.1981 . . . . . . . . . . . 0.2766 
'X-RAY DIFFRACTION' 2.58 2.62 . . 260 4020 99.00  . . . . 0.2029 . . . . . . . . . . . 0.2693 
'X-RAY DIFFRACTION' 2.62 2.67 . . 172 4169 99.00  . . . . 0.1874 . . . . . . . . . . . 0.2684 
'X-RAY DIFFRACTION' 2.67 2.72 . . 301 3975 99.00  . . . . 0.1892 . . . . . . . . . . . 0.2502 
'X-RAY DIFFRACTION' 2.72 2.78 . . 200 4139 99.00  . . . . 0.1991 . . . . . . . . . . . 0.2122 
'X-RAY DIFFRACTION' 2.78 2.84 . . 187 4137 99.00  . . . . 0.1901 . . . . . . . . . . . 0.2788 
'X-RAY DIFFRACTION' 2.84 2.91 . . 198 4120 99.00  . . . . 0.1841 . . . . . . . . . . . 0.2383 
'X-RAY DIFFRACTION' 2.91 2.98 . . 173 4159 99.00  . . . . 0.1854 . . . . . . . . . . . 0.2197 
'X-RAY DIFFRACTION' 2.98 3.06 . . 253 4054 99.00  . . . . 0.1901 . . . . . . . . . . . 0.2545 
'X-RAY DIFFRACTION' 3.06 3.15 . . 220 4153 99.00  . . . . 0.1865 . . . . . . . . . . . 0.2484 
'X-RAY DIFFRACTION' 3.15 3.25 . . 266 4089 99.00  . . . . 0.1690 . . . . . . . . . . . 0.2238 
'X-RAY DIFFRACTION' 3.25 3.37 . . 220 4077 100.00 . . . . 0.1642 . . . . . . . . . . . 0.2148 
'X-RAY DIFFRACTION' 3.37 3.50 . . 141 4181 99.00  . . . . 0.1476 . . . . . . . . . . . 0.2036 
'X-RAY DIFFRACTION' 3.50 3.66 . . 269 4058 99.00  . . . . 0.1468 . . . . . . . . . . . 0.1602 
'X-RAY DIFFRACTION' 3.66 3.85 . . 266 4098 99.00  . . . . 0.1401 . . . . . . . . . . . 0.1762 
'X-RAY DIFFRACTION' 3.85 4.09 . . 197 4106 99.00  . . . . 0.1325 . . . . . . . . . . . 0.2055 
'X-RAY DIFFRACTION' 4.09 4.41 . . 133 4205 99.00  . . . . 0.1274 . . . . . . . . . . . 0.1620 
'X-RAY DIFFRACTION' 4.41 4.85 . . 199 4174 99.00  . . . . 0.1225 . . . . . . . . . . . 0.1553 
'X-RAY DIFFRACTION' 4.85 5.55 . . 254 4004 99.00  . . . . 0.1487 . . . . . . . . . . . 0.1706 
'X-RAY DIFFRACTION' 5.56 6.99 . . 204 4141 99.00  . . . . 0.1760 . . . . . . . . . . . 0.2060 
'X-RAY DIFFRACTION' 6.99 7    . . 198 4137 99.00  . . . . 0.13   . . . . . . . . . . . 0.1337 
# 
_struct.entry_id                     8ZN8 
_struct.title                        'MjF-3C-CdS QDs' 
_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        8ZN8 
_struct_keywords.text            'ferritin, quantum dots, Cds, catalysis, photosynthesis, METAL BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'METAL BINDING 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 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 1 ? 
G  N N 2 ? 
H  N N 2 ? 
I  N N 2 ? 
J  N N 2 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 4 ? 
R  N N 5 ? 
S  N N 5 ? 
T  N N 2 ? 
U  N N 2 ? 
V  N N 2 ? 
W  N N 2 ? 
X  N N 3 ? 
Y  N N 3 ? 
Z  N N 3 ? 
AA N N 3 ? 
BA N N 3 ? 
CA N N 5 ? 
DA N N 2 ? 
EA N N 2 ? 
FA N N 2 ? 
GA N N 2 ? 
HA N N 3 ? 
IA N N 3 ? 
JA N N 3 ? 
KA N N 3 ? 
LA N N 3 ? 
MA N N 3 ? 
NA N N 4 ? 
OA N N 5 ? 
PA N N 2 ? 
QA N N 2 ? 
RA N N 2 ? 
SA N N 2 ? 
TA N N 3 ? 
UA N N 3 ? 
VA N N 3 ? 
WA N N 3 ? 
XA N N 3 ? 
YA N N 3 ? 
ZA N N 3 ? 
AB N N 4 ? 
BB N N 4 ? 
CB N N 5 ? 
DB N N 2 ? 
EB N N 2 ? 
FB N N 2 ? 
GB N N 2 ? 
HB N N 3 ? 
IB N N 3 ? 
JB N N 3 ? 
KB N N 3 ? 
LB N N 3 ? 
MB N N 3 ? 
NB N N 4 ? 
OB N N 5 ? 
PB N N 2 ? 
QB N N 2 ? 
RB N N 2 ? 
SB N N 2 ? 
TB N N 3 ? 
UB N N 3 ? 
VB N N 3 ? 
WB N N 3 ? 
XB N N 3 ? 
YB N N 4 ? 
ZB N N 5 ? 
AC N N 6 ? 
BC N N 6 ? 
CC N N 6 ? 
DC N N 6 ? 
EC N N 6 ? 
FC N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    T2B7E1_PENJP 
_struct_ref.pdbx_db_accession          T2B7E1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ASQVRQNYHEDCEASINKQINMELYASYVYLSMAYYFERDDVALPGFAKFFKESSDEEREHAQTFMKYQNKRGGRIVLQQ
IAAPSMQEWGTGLEALQAALDLEKQVNQSLLELHSTASGNNDPHLTKLLEDEYLEEQVDSIKKIGDMITKLKRAGPTGLG
EYMFDKELN
;
_struct_ref.pdbx_align_begin           2 
# 
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 8ZN8 A 1 ? 169 ? T2B7E1 2 ? 170 ? 2 170 
2 1 8ZN8 B 1 ? 169 ? T2B7E1 2 ? 170 ? 2 170 
3 1 8ZN8 C 1 ? 169 ? T2B7E1 2 ? 170 ? 2 170 
4 1 8ZN8 D 1 ? 169 ? T2B7E1 2 ? 170 ? 2 170 
5 1 8ZN8 E 1 ? 169 ? T2B7E1 2 ? 170 ? 2 170 
6 1 8ZN8 F 1 ? 169 ? T2B7E1 2 ? 170 ? 2 170 
# 
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 8ZN8 ALA A 12 ? UNP T2B7E1 CYS 13 conflict 13 1  
1 8ZN8 CYS A 23 ? UNP T2B7E1 GLU 24 conflict 24 2  
1 8ZN8 CYS A 57 ? UNP T2B7E1 GLU 58 conflict 58 3  
1 8ZN8 CYS A 58 ? UNP T2B7E1 GLU 59 conflict 59 4  
2 8ZN8 ALA B 12 ? UNP T2B7E1 CYS 13 conflict 13 5  
2 8ZN8 CYS B 23 ? UNP T2B7E1 GLU 24 conflict 24 6  
2 8ZN8 CYS B 57 ? UNP T2B7E1 GLU 58 conflict 58 7  
2 8ZN8 CYS B 58 ? UNP T2B7E1 GLU 59 conflict 59 8  
3 8ZN8 ALA C 12 ? UNP T2B7E1 CYS 13 conflict 13 9  
3 8ZN8 CYS C 23 ? UNP T2B7E1 GLU 24 conflict 24 10 
3 8ZN8 CYS C 57 ? UNP T2B7E1 GLU 58 conflict 58 11 
3 8ZN8 CYS C 58 ? UNP T2B7E1 GLU 59 conflict 59 12 
4 8ZN8 ALA D 12 ? UNP T2B7E1 CYS 13 conflict 13 13 
4 8ZN8 CYS D 23 ? UNP T2B7E1 GLU 24 conflict 24 14 
4 8ZN8 CYS D 57 ? UNP T2B7E1 GLU 58 conflict 58 15 
4 8ZN8 CYS D 58 ? UNP T2B7E1 GLU 59 conflict 59 16 
5 8ZN8 ALA E 12 ? UNP T2B7E1 CYS 13 conflict 13 17 
5 8ZN8 CYS E 23 ? UNP T2B7E1 GLU 24 conflict 24 18 
5 8ZN8 CYS E 57 ? UNP T2B7E1 GLU 58 conflict 58 19 
5 8ZN8 CYS E 58 ? UNP T2B7E1 GLU 59 conflict 59 20 
6 8ZN8 ALA F 12 ? UNP T2B7E1 CYS 13 conflict 13 21 
6 8ZN8 CYS F 23 ? UNP T2B7E1 GLU 24 conflict 24 22 
6 8ZN8 CYS F 57 ? UNP T2B7E1 GLU 58 conflict 58 23 
6 8ZN8 CYS F 58 ? UNP T2B7E1 GLU 59 conflict 59 24 
# 
_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   24-meric 
_pdbx_struct_assembly.oligomeric_count     24 
# 
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)' 107430 ? 
1 MORE         -1524  ? 
1 'SSA (A^2)'  134410 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1,2,3,4 
;B,D,E,F,T,U,V,W,X,Y,Z,AA,BA,CA,PA,QA,RA,SA,TA,UA,VA,WA,XA,YA,ZA,AB,BB,CB,DB,EB,FB,GB,HB,IB,JB,KB,LB,MB,NB,OB,PB,QB,RB,SB,TB,UB,VB,WB,XB,YB,ZB,BC,DC,EC,FC
;
1 5,6,7,8 A,C,G,H,I,J,K,L,M,N,O,P,Q,R,S,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,AC,CC 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z               1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
1.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000  
2 'crystal symmetry operation' 2_555 -x,-y,z             -1.0000000000 0.0000000000  0.0000000000 0.0000000000   0.0000000000  
-1.0000000000 0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000  
3 'crystal symmetry operation' 3_555 -y,x,z              0.0000000000  -1.0000000000 0.0000000000 0.0000000000   1.0000000000  
0.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000  
4 'crystal symmetry operation' 4_555 y,-x,z              0.0000000000  1.0000000000  0.0000000000 0.0000000000   -1.0000000000 
0.0000000000  0.0000000000 0.0000000000   0.0000000000 0.0000000000 1.0000000000 0.0000000000  
5 'crystal symmetry operation' 5_445 x-1/2,y-1/2,z+1/2   1.0000000000  0.0000000000  0.0000000000 -63.3740000000 0.0000000000  
1.0000000000  0.0000000000 -63.3740000000 0.0000000000 0.0000000000 1.0000000000 88.9745000000 
6 'crystal symmetry operation' 6_555 -x+1/2,-y+1/2,z+1/2 -1.0000000000 0.0000000000  0.0000000000 63.3740000000  0.0000000000  
-1.0000000000 0.0000000000 63.3740000000  0.0000000000 0.0000000000 1.0000000000 88.9745000000 
7 'crystal symmetry operation' 7_545 -y+1/2,x-1/2,z+1/2  0.0000000000  -1.0000000000 0.0000000000 63.3740000000  1.0000000000  
0.0000000000  0.0000000000 -63.3740000000 0.0000000000 0.0000000000 1.0000000000 88.9745000000 
8 'crystal symmetry operation' 8_455 y-1/2,-x+1/2,z+1/2  0.0000000000  1.0000000000  0.0000000000 -63.3740000000 -1.0000000000 
0.0000000000  0.0000000000 63.3740000000  0.0000000000 0.0000000000 1.0000000000 88.9745000000 
# 
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 HIS A 9   ? PHE A 37  ? HIS A 10  PHE A 38  1 ? 29 
HELX_P HELX_P2  AA2 LEU A 44  ? GLY A 73  ? LEU A 45  GLY A 74  1 ? 30 
HELX_P HELX_P3  AA3 THR A 91  ? ASN A 120 ? THR A 92  ASN A 121 1 ? 30 
HELX_P HELX_P4  AA4 ASP A 122 ? TYR A 133 ? ASP A 123 TYR A 134 1 ? 12 
HELX_P HELX_P5  AA5 TYR A 133 ? GLY A 155 ? TYR A 134 GLY A 156 1 ? 23 
HELX_P HELX_P6  AA6 THR A 157 ? ASN A 169 ? THR A 158 ASN A 170 1 ? 13 
HELX_P HELX_P7  AA7 HIS B 9   ? PHE B 37  ? HIS B 10  PHE B 38  1 ? 29 
HELX_P HELX_P8  AA8 LEU B 44  ? GLY B 73  ? LEU B 45  GLY B 74  1 ? 30 
HELX_P HELX_P9  AA9 THR B 91  ? ASN B 120 ? THR B 92  ASN B 121 1 ? 30 
HELX_P HELX_P10 AB1 ASP B 122 ? TYR B 133 ? ASP B 123 TYR B 134 1 ? 12 
HELX_P HELX_P11 AB2 TYR B 133 ? GLY B 155 ? TYR B 134 GLY B 156 1 ? 23 
HELX_P HELX_P12 AB3 THR B 157 ? ASN B 169 ? THR B 158 ASN B 170 1 ? 13 
HELX_P HELX_P13 AB4 HIS C 9   ? PHE C 37  ? HIS C 10  PHE C 38  1 ? 29 
HELX_P HELX_P14 AB5 LEU C 44  ? GLY C 73  ? LEU C 45  GLY C 74  1 ? 30 
HELX_P HELX_P15 AB6 THR C 91  ? ASN C 120 ? THR C 92  ASN C 121 1 ? 30 
HELX_P HELX_P16 AB7 ASP C 122 ? TYR C 133 ? ASP C 123 TYR C 134 1 ? 12 
HELX_P HELX_P17 AB8 TYR C 133 ? GLY C 155 ? TYR C 134 GLY C 156 1 ? 23 
HELX_P HELX_P18 AB9 GLY C 158 ? ASN C 169 ? GLY C 159 ASN C 170 1 ? 12 
HELX_P HELX_P19 AC1 HIS D 9   ? PHE D 37  ? HIS D 10  PHE D 38  1 ? 29 
HELX_P HELX_P20 AC2 LEU D 44  ? GLY D 73  ? LEU D 45  GLY D 74  1 ? 30 
HELX_P HELX_P21 AC3 THR D 91  ? ASN D 120 ? THR D 92  ASN D 121 1 ? 30 
HELX_P HELX_P22 AC4 ASP D 122 ? TYR D 133 ? ASP D 123 TYR D 134 1 ? 12 
HELX_P HELX_P23 AC5 TYR D 133 ? GLY D 155 ? TYR D 134 GLY D 156 1 ? 23 
HELX_P HELX_P24 AC6 GLY D 158 ? ASN D 169 ? GLY D 159 ASN D 170 1 ? 12 
HELX_P HELX_P25 AC7 HIS E 9   ? PHE E 37  ? HIS E 10  PHE E 38  1 ? 29 
HELX_P HELX_P26 AC8 LEU E 44  ? GLY E 73  ? LEU E 45  GLY E 74  1 ? 30 
HELX_P HELX_P27 AC9 THR E 91  ? ASN E 120 ? THR E 92  ASN E 121 1 ? 30 
HELX_P HELX_P28 AD1 ASP E 122 ? TYR E 133 ? ASP E 123 TYR E 134 1 ? 12 
HELX_P HELX_P29 AD2 TYR E 133 ? GLY E 155 ? TYR E 134 GLY E 156 1 ? 23 
HELX_P HELX_P30 AD3 GLY E 158 ? ASN E 169 ? GLY E 159 ASN E 170 1 ? 12 
HELX_P HELX_P31 AD4 HIS F 9   ? PHE F 37  ? HIS F 10  PHE F 38  1 ? 29 
HELX_P HELX_P32 AD5 LEU F 44  ? GLY F 73  ? LEU F 45  GLY F 74  1 ? 30 
HELX_P HELX_P33 AD6 THR F 91  ? ASN F 120 ? THR F 92  ASN F 121 1 ? 30 
HELX_P HELX_P34 AD7 ASP F 122 ? TYR F 133 ? ASP F 123 TYR F 134 1 ? 12 
HELX_P HELX_P35 AD8 TYR F 133 ? GLY F 155 ? TYR F 134 GLY F 156 1 ? 23 
HELX_P HELX_P36 AD9 THR F 157 ? ASN F 169 ? THR F 158 ASN F 170 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A  CYS 23  SG  ? ? ? 1_555 G  CD  . CD ? ? A CYS 24  A CD  201 1_555 ? ? ? ? ? ? ? 2.844 ? ? 
metalc2  metalc ? ? A  CYS 57  SG  ? ? ? 1_555 H  CD  . CD ? ? A CYS 58  A CD  202 1_555 ? ? ? ? ? ? ? 2.990 ? ? 
metalc3  metalc ? ? A  CYS 57  SG  ? ? ? 1_555 I  CD  . CD ? ? A CYS 58  A CD  203 1_555 ? ? ? ? ? ? ? 2.838 ? ? 
metalc4  metalc ? ? A  CYS 57  SG  ? ? ? 1_555 J  CD  . CD ? ? A CYS 58  A CD  204 1_555 ? ? ? ? ? ? ? 3.060 ? ? 
metalc5  metalc ? ? A  CYS 58  SG  ? ? ? 1_555 G  CD  . CD ? ? A CYS 59  A CD  201 1_555 ? ? ? ? ? ? ? 2.864 ? ? 
metalc6  metalc ? ? A  CYS 58  SG  ? ? ? 1_555 J  CD  . CD ? ? A CYS 59  A CD  204 1_555 ? ? ? ? ? ? ? 3.009 ? ? 
metalc7  metalc ? ? G  CD  .   CD  ? ? ? 1_555 L  H2S . S  ? ? A CD  201 A H2S 206 1_555 ? ? ? ? ? ? ? 2.588 ? ? 
metalc8  metalc ? ? H  CD  .   CD  ? ? ? 1_555 K  H2S . S  ? ? A CD  202 A H2S 205 1_555 ? ? ? ? ? ? ? 2.770 ? ? 
metalc9  metalc ? ? H  CD  .   CD  ? ? ? 1_555 M  H2S . S  ? ? A CD  202 A H2S 207 1_555 ? ? ? ? ? ? ? 2.665 ? ? 
metalc10 metalc ? ? H  CD  .   CD  ? ? ? 1_555 O  H2S . S  ? ? A CD  202 A H2S 209 1_555 ? ? ? ? ? ? ? 2.776 ? ? 
metalc11 metalc ? ? I  CD  .   CD  ? ? ? 1_555 K  H2S . S  ? ? A CD  203 A H2S 205 1_555 ? ? ? ? ? ? ? 2.901 ? ? 
metalc12 metalc ? ? I  CD  .   CD  ? ? ? 1_555 N  H2S . S  ? ? A CD  203 A H2S 208 1_555 ? ? ? ? ? ? ? 2.546 ? ? 
metalc13 metalc ? ? J  CD  .   CD  ? ? ? 1_555 L  H2S . S  ? ? A CD  204 A H2S 206 1_555 ? ? ? ? ? ? ? 2.832 ? ? 
metalc14 metalc ? ? B  CYS 23  SG  ? ? ? 1_555 T  CD  . CD ? ? B CYS 24  B CD  201 1_555 ? ? ? ? ? ? ? 2.860 ? ? 
metalc15 metalc ? ? B  CYS 57  SG  ? ? ? 1_555 U  CD  . CD ? ? B CYS 58  B CD  202 1_555 ? ? ? ? ? ? ? 3.002 ? ? 
metalc16 metalc ? ? B  CYS 57  SG  ? ? ? 1_555 V  CD  . CD ? ? B CYS 58  B CD  203 1_555 ? ? ? ? ? ? ? 2.974 ? ? 
metalc17 metalc ? ? B  CYS 58  SG  ? ? ? 1_555 T  CD  . CD ? ? B CYS 59  B CD  201 1_555 ? ? ? ? ? ? ? 2.850 ? ? 
metalc18 metalc ? ? B  GLU 136 OE2 ? ? ? 1_555 V  CD  . CD ? ? B GLU 137 B CD  203 1_555 ? ? ? ? ? ? ? 2.557 ? ? 
metalc19 metalc ? ? T  CD  .   CD  ? ? ? 1_555 X  H2S . S  ? ? B CD  201 B H2S 205 1_555 ? ? ? ? ? ? ? 2.591 ? ? 
metalc20 metalc ? ? U  CD  .   CD  ? ? ? 1_555 Y  H2S . S  ? ? B CD  202 B H2S 206 1_555 ? ? ? ? ? ? ? 3.011 ? ? 
metalc21 metalc ? ? U  CD  .   CD  ? ? ? 1_555 AA H2S . S  ? ? B CD  202 B H2S 208 1_555 ? ? ? ? ? ? ? 2.234 ? ? 
metalc22 metalc ? ? V  CD  .   CD  ? ? ? 1_555 Y  H2S . S  ? ? B CD  203 B H2S 206 1_555 ? ? ? ? ? ? ? 3.057 ? ? 
metalc23 metalc ? ? V  CD  .   CD  ? ? ? 1_555 BA H2S . S  ? ? B CD  203 B H2S 209 1_555 ? ? ? ? ? ? ? 3.018 ? ? 
metalc24 metalc ? ? W  CD  .   CD  ? ? ? 1_555 AA H2S . S  ? ? B CD  204 B H2S 208 1_555 ? ? ? ? ? ? ? 2.375 ? ? 
metalc25 metalc ? ? W  CD  .   CD  ? ? ? 1_555 BC HOH . O  ? ? B CD  204 B HOH 331 1_555 ? ? ? ? ? ? ? 2.605 ? ? 
metalc26 metalc ? ? C  CYS 23  SG  ? ? ? 1_555 DA CD  . CD ? ? C CYS 24  C CD  201 1_555 ? ? ? ? ? ? ? 2.872 ? ? 
metalc27 metalc ? ? C  CYS 57  SG  ? ? ? 1_555 EA CD  . CD ? ? C CYS 58  C CD  202 1_555 ? ? ? ? ? ? ? 2.998 ? ? 
metalc28 metalc ? ? C  CYS 57  SG  ? ? ? 1_555 FA CD  . CD ? ? C CYS 58  C CD  203 1_555 ? ? ? ? ? ? ? 2.989 ? ? 
metalc29 metalc ? ? C  CYS 57  SG  ? ? ? 1_555 GA CD  . CD ? ? C CYS 58  C CD  204 1_555 ? ? ? ? ? ? ? 3.020 ? ? 
metalc30 metalc ? ? C  CYS 58  SG  ? ? ? 1_555 DA CD  . CD ? ? C CYS 59  C CD  201 1_555 ? ? ? ? ? ? ? 2.860 ? ? 
metalc31 metalc ? ? C  CYS 58  SG  ? ? ? 1_555 GA CD  . CD ? ? C CYS 59  C CD  204 1_555 ? ? ? ? ? ? ? 2.924 ? ? 
metalc32 metalc ? ? DA CD  .   CD  ? ? ? 1_555 JA H2S . S  ? ? C CD  201 C H2S 207 1_555 ? ? ? ? ? ? ? 2.512 ? ? 
metalc33 metalc ? ? EA CD  .   CD  ? ? ? 1_555 KA H2S . S  ? ? C CD  202 C H2S 208 1_555 ? ? ? ? ? ? ? 2.840 ? ? 
metalc34 metalc ? ? EA CD  .   CD  ? ? ? 1_555 LA H2S . S  ? ? C CD  202 C H2S 209 1_555 ? ? ? ? ? ? ? 2.900 ? ? 
metalc35 metalc ? ? FA CD  .   CD  ? ? ? 1_555 MA H2S . S  ? ? C CD  203 C H2S 210 1_555 ? ? ? ? ? ? ? 2.676 ? ? 
metalc36 metalc ? ? GA CD  .   CD  ? ? ? 1_555 IA H2S . S  ? ? C CD  204 C H2S 206 1_555 ? ? ? ? ? ? ? 3.006 ? ? 
metalc37 metalc ? ? GA CD  .   CD  ? ? ? 1_555 KA H2S . S  ? ? C CD  204 C H2S 208 1_555 ? ? ? ? ? ? ? 2.786 ? ? 
metalc38 metalc ? ? D  GLU 10  N   ? ? ? 1_555 BB MG  . MG ? ? D GLU 11  D MG  213 1_555 ? ? ? ? ? ? ? 2.978 ? ? 
metalc39 metalc ? ? D  CYS 23  SG  ? ? ? 1_555 PA CD  . CD ? ? D CYS 24  D CD  201 1_555 ? ? ? ? ? ? ? 2.845 ? ? 
metalc40 metalc ? ? D  CYS 57  SG  ? ? ? 1_555 QA CD  . CD ? ? D CYS 58  D CD  202 1_555 ? ? ? ? ? ? ? 2.884 ? ? 
metalc41 metalc ? ? D  CYS 57  SG  ? ? ? 1_555 RA CD  . CD ? ? D CYS 58  D CD  203 1_555 ? ? ? ? ? ? ? 2.825 ? ? 
metalc42 metalc ? ? D  CYS 58  SG  ? ? ? 1_555 PA CD  . CD ? ? D CYS 59  D CD  201 1_555 ? ? ? ? ? ? ? 2.885 ? ? 
metalc43 metalc ? ? D  CYS 58  SG  ? ? ? 1_555 SA CD  . CD ? ? D CYS 59  D CD  204 1_555 ? ? ? ? ? ? ? 2.921 ? ? 
metalc44 metalc ? ? PA CD  .   CD  ? ? ? 1_555 WA H2S . S  ? ? D CD  201 D H2S 208 1_555 ? ? ? ? ? ? ? 2.197 ? ? 
metalc45 metalc ? ? QA CD  .   CD  ? ? ? 1_555 TA H2S . S  ? ? D CD  202 D H2S 205 1_555 ? ? ? ? ? ? ? 2.709 ? ? 
metalc46 metalc ? ? QA CD  .   CD  ? ? ? 1_555 VA H2S . S  ? ? D CD  202 D H2S 207 1_555 ? ? ? ? ? ? ? 2.519 ? ? 
metalc47 metalc ? ? QA CD  .   CD  ? ? ? 1_555 XA H2S . S  ? ? D CD  202 D H2S 209 1_555 ? ? ? ? ? ? ? 2.519 ? ? 
metalc48 metalc ? ? RA CD  .   CD  ? ? ? 1_555 TA H2S . S  ? ? D CD  203 D H2S 205 1_555 ? ? ? ? ? ? ? 2.987 ? ? 
metalc49 metalc ? ? RA CD  .   CD  ? ? ? 1_555 UA H2S . S  ? ? D CD  203 D H2S 206 1_555 ? ? ? ? ? ? ? 2.722 ? ? 
metalc50 metalc ? ? RA CD  .   CD  ? ? ? 1_555 YA H2S . S  ? ? D CD  203 D H2S 210 1_555 ? ? ? ? ? ? ? 2.585 ? ? 
metalc51 metalc ? ? SA CD  .   CD  ? ? ? 1_555 VA H2S . S  ? ? D CD  204 D H2S 207 1_555 ? ? ? ? ? ? ? 2.834 ? ? 
metalc52 metalc ? ? SA CD  .   CD  ? ? ? 1_555 WA H2S . S  ? ? D CD  204 D H2S 208 1_555 ? ? ? ? ? ? ? 2.891 ? ? 
metalc53 metalc ? ? SA CD  .   CD  ? ? ? 1_555 ZA H2S . S  ? ? D CD  204 D H2S 211 1_555 ? ? ? ? ? ? ? 2.999 ? ? 
metalc54 metalc ? ? E  CYS 23  SG  ? ? ? 1_555 DB CD  . CD ? ? E CYS 24  E CD  201 1_555 ? ? ? ? ? ? ? 2.961 ? ? 
metalc55 metalc ? ? E  CYS 57  SG  ? ? ? 1_555 EB CD  . CD ? ? E CYS 58  E CD  202 1_555 ? ? ? ? ? ? ? 2.954 ? ? 
metalc56 metalc ? ? E  CYS 57  SG  ? ? ? 1_555 FB CD  . CD ? ? E CYS 58  E CD  203 1_555 ? ? ? ? ? ? ? 2.934 ? ? 
metalc57 metalc ? ? E  CYS 58  SG  ? ? ? 1_555 DB CD  . CD ? ? E CYS 59  E CD  201 1_555 ? ? ? ? ? ? ? 2.896 ? ? 
metalc58 metalc ? ? E  CYS 58  SG  ? ? ? 1_555 GB CD  . CD ? ? E CYS 59  E CD  204 1_555 ? ? ? ? ? ? ? 2.965 ? ? 
metalc59 metalc ? ? DB CD  .   CD  ? ? ? 1_555 HB H2S . S  ? ? E CD  201 E H2S 205 1_555 ? ? ? ? ? ? ? 2.197 ? ? 
metalc60 metalc ? ? EB CD  .   CD  ? ? ? 1_555 IB H2S . S  ? ? E CD  202 E H2S 206 1_555 ? ? ? ? ? ? ? 2.834 ? ? 
metalc61 metalc ? ? EB CD  .   CD  ? ? ? 1_555 JB H2S . S  ? ? E CD  202 E H2S 207 1_555 ? ? ? ? ? ? ? 3.022 ? ? 
metalc62 metalc ? ? FB CD  .   CD  ? ? ? 1_555 KB H2S . S  ? ? E CD  203 E H2S 208 1_555 ? ? ? ? ? ? ? 2.493 ? ? 
metalc63 metalc ? ? FB CD  .   CD  ? ? ? 1_555 MB H2S . S  ? ? E CD  203 E H2S 210 1_555 ? ? ? ? ? ? ? 2.838 ? ? 
metalc64 metalc ? ? GB CD  .   CD  ? ? ? 1_555 JB H2S . S  ? ? E CD  204 E H2S 207 1_555 ? ? ? ? ? ? ? 2.974 ? ? 
metalc65 metalc ? ? F  CYS 23  SG  ? ? ? 1_555 PB CD  . CD ? ? F CYS 24  F CD  201 1_555 ? ? ? ? ? ? ? 2.845 ? ? 
metalc66 metalc ? ? F  CYS 57  SG  ? ? ? 1_555 QB CD  . CD ? ? F CYS 58  F CD  202 1_555 ? ? ? ? ? ? ? 2.990 ? ? 
metalc67 metalc ? ? F  CYS 57  SG  ? ? ? 1_555 RB CD  . CD ? ? F CYS 58  F CD  203 1_555 ? ? ? ? ? ? ? 2.946 ? ? 
metalc68 metalc ? ? F  CYS 58  SG  ? ? ? 1_555 PB CD  . CD ? ? F CYS 59  F CD  201 1_555 ? ? ? ? ? ? ? 2.906 ? ? 
metalc69 metalc ? ? F  CYS 58  SG  ? ? ? 1_555 SB CD  . CD ? ? F CYS 59  F CD  204 1_555 ? ? ? ? ? ? ? 3.017 ? ? 
metalc70 metalc ? ? PB CD  .   CD  ? ? ? 1_555 UB H2S . S  ? ? F CD  201 F H2S 206 1_555 ? ? ? ? ? ? ? 2.698 ? ? 
metalc71 metalc ? ? QB CD  .   CD  ? ? ? 1_555 TB H2S . S  ? ? F CD  202 F H2S 205 1_555 ? ? ? ? ? ? ? 2.425 ? ? 
metalc72 metalc ? ? QB CD  .   CD  ? ? ? 1_555 WB H2S . S  ? ? F CD  202 F H2S 208 1_555 ? ? ? ? ? ? ? 2.673 ? ? 
metalc73 metalc ? ? QB CD  .   CD  ? ? ? 1_555 XB H2S . S  ? ? F CD  202 F H2S 209 1_555 ? ? ? ? ? ? ? 3.022 ? ? 
metalc74 metalc ? ? RB CD  .   CD  ? ? ? 1_555 TB H2S . S  ? ? F CD  203 F H2S 205 1_555 ? ? ? ? ? ? ? 2.333 ? ? 
metalc75 metalc ? ? SB CD  .   CD  ? ? ? 1_555 VB H2S . S  ? ? F CD  204 F H2S 207 1_555 ? ? ? ? ? ? ? 3.083 ? ? 
metalc76 metalc ? ? SB CD  .   CD  ? ? ? 1_555 XB H2S . S  ? ? F CD  204 F H2S 209 1_555 ? ? ? ? ? ? ? 2.833 ? ? 
metalc77 metalc ? ? SB CD  .   CD  ? ? ? 1_555 FC HOH . O  ? ? F CD  204 F HOH 317 1_555 ? ? ? ? ? ? ? 2.579 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A  CYS 23  ? A CYS 24  ? 1_555 CD ? G  CD . ? A CD 201 ? 1_555 SG  ? A  CYS 58  ? A CYS 59  ? 1_555 130.1 ? 
2  SG  ? A  CYS 23  ? A CYS 24  ? 1_555 CD ? G  CD . ? A CD 201 ? 1_555 S   ? L  H2S .   ? A H2S 206 ? 1_555 131.0 ? 
3  SG  ? A  CYS 58  ? A CYS 59  ? 1_555 CD ? G  CD . ? A CD 201 ? 1_555 S   ? L  H2S .   ? A H2S 206 ? 1_555 80.4  ? 
4  SG  ? A  CYS 57  ? A CYS 58  ? 1_555 CD ? H  CD . ? A CD 202 ? 1_555 S   ? K  H2S .   ? A H2S 205 ? 1_555 101.5 ? 
5  SG  ? A  CYS 57  ? A CYS 58  ? 1_555 CD ? H  CD . ? A CD 202 ? 1_555 S   ? M  H2S .   ? A H2S 207 ? 1_555 87.3  ? 
6  S   ? K  H2S .   ? A H2S 205 ? 1_555 CD ? H  CD . ? A CD 202 ? 1_555 S   ? M  H2S .   ? A H2S 207 ? 1_555 156.6 ? 
7  SG  ? A  CYS 57  ? A CYS 58  ? 1_555 CD ? H  CD . ? A CD 202 ? 1_555 S   ? O  H2S .   ? A H2S 209 ? 1_555 101.8 ? 
8  S   ? K  H2S .   ? A H2S 205 ? 1_555 CD ? H  CD . ? A CD 202 ? 1_555 S   ? O  H2S .   ? A H2S 209 ? 1_555 83.4  ? 
9  S   ? M  H2S .   ? A H2S 207 ? 1_555 CD ? H  CD . ? A CD 202 ? 1_555 S   ? O  H2S .   ? A H2S 209 ? 1_555 73.5  ? 
10 SG  ? A  CYS 57  ? A CYS 58  ? 1_555 CD ? I  CD . ? A CD 203 ? 1_555 S   ? K  H2S .   ? A H2S 205 ? 1_555 102.1 ? 
11 SG  ? A  CYS 57  ? A CYS 58  ? 1_555 CD ? I  CD . ? A CD 203 ? 1_555 S   ? N  H2S .   ? A H2S 208 ? 1_555 100.5 ? 
12 S   ? K  H2S .   ? A H2S 205 ? 1_555 CD ? I  CD . ? A CD 203 ? 1_555 S   ? N  H2S .   ? A H2S 208 ? 1_555 83.9  ? 
13 SG  ? A  CYS 57  ? A CYS 58  ? 1_555 CD ? J  CD . ? A CD 204 ? 1_555 SG  ? A  CYS 58  ? A CYS 59  ? 1_555 117.1 ? 
14 SG  ? A  CYS 57  ? A CYS 58  ? 1_555 CD ? J  CD . ? A CD 204 ? 1_555 S   ? L  H2S .   ? A H2S 206 ? 1_555 152.7 ? 
15 SG  ? A  CYS 58  ? A CYS 59  ? 1_555 CD ? J  CD . ? A CD 204 ? 1_555 S   ? L  H2S .   ? A H2S 206 ? 1_555 74.1  ? 
16 SG  ? B  CYS 23  ? B CYS 24  ? 1_555 CD ? T  CD . ? B CD 201 ? 1_555 SG  ? B  CYS 58  ? B CYS 59  ? 1_555 134.5 ? 
17 SG  ? B  CYS 23  ? B CYS 24  ? 1_555 CD ? T  CD . ? B CD 201 ? 1_555 S   ? X  H2S .   ? B H2S 205 ? 1_555 133.3 ? 
18 SG  ? B  CYS 58  ? B CYS 59  ? 1_555 CD ? T  CD . ? B CD 201 ? 1_555 S   ? X  H2S .   ? B H2S 205 ? 1_555 80.8  ? 
19 SG  ? B  CYS 57  ? B CYS 58  ? 1_555 CD ? U  CD . ? B CD 202 ? 1_555 S   ? Y  H2S .   ? B H2S 206 ? 1_555 108.9 ? 
20 SG  ? B  CYS 57  ? B CYS 58  ? 1_555 CD ? U  CD . ? B CD 202 ? 1_555 S   ? AA H2S .   ? B H2S 208 ? 1_555 81.2  ? 
21 S   ? Y  H2S .   ? B H2S 206 ? 1_555 CD ? U  CD . ? B CD 202 ? 1_555 S   ? AA H2S .   ? B H2S 208 ? 1_555 166.2 ? 
22 SG  ? B  CYS 57  ? B CYS 58  ? 1_555 CD ? V  CD . ? B CD 203 ? 1_555 OE2 ? B  GLU 136 ? B GLU 137 ? 1_555 81.7  ? 
23 SG  ? B  CYS 57  ? B CYS 58  ? 1_555 CD ? V  CD . ? B CD 203 ? 1_555 S   ? Y  H2S .   ? B H2S 206 ? 1_555 108.4 ? 
24 OE2 ? B  GLU 136 ? B GLU 137 ? 1_555 CD ? V  CD . ? B CD 203 ? 1_555 S   ? Y  H2S .   ? B H2S 206 ? 1_555 90.0  ? 
25 SG  ? B  CYS 57  ? B CYS 58  ? 1_555 CD ? V  CD . ? B CD 203 ? 1_555 S   ? BA H2S .   ? B H2S 209 ? 1_555 100.2 ? 
26 OE2 ? B  GLU 136 ? B GLU 137 ? 1_555 CD ? V  CD . ? B CD 203 ? 1_555 S   ? BA H2S .   ? B H2S 209 ? 1_555 163.9 ? 
27 S   ? Y  H2S .   ? B H2S 206 ? 1_555 CD ? V  CD . ? B CD 203 ? 1_555 S   ? BA H2S .   ? B H2S 209 ? 1_555 104.4 ? 
28 S   ? AA H2S .   ? B H2S 208 ? 1_555 CD ? W  CD . ? B CD 204 ? 1_555 O   ? BC HOH .   ? B HOH 331 ? 1_555 106.0 ? 
29 SG  ? C  CYS 23  ? C CYS 24  ? 1_555 CD ? DA CD . ? C CD 201 ? 1_555 SG  ? C  CYS 58  ? C CYS 59  ? 1_555 134.1 ? 
30 SG  ? C  CYS 23  ? C CYS 24  ? 1_555 CD ? DA CD . ? C CD 201 ? 1_555 S   ? JA H2S .   ? C H2S 207 ? 1_555 131.6 ? 
31 SG  ? C  CYS 58  ? C CYS 59  ? 1_555 CD ? DA CD . ? C CD 201 ? 1_555 S   ? JA H2S .   ? C H2S 207 ? 1_555 83.9  ? 
32 SG  ? C  CYS 57  ? C CYS 58  ? 1_555 CD ? EA CD . ? C CD 202 ? 1_555 S   ? KA H2S .   ? C H2S 208 ? 1_555 86.7  ? 
33 SG  ? C  CYS 57  ? C CYS 58  ? 1_555 CD ? EA CD . ? C CD 202 ? 1_555 S   ? LA H2S .   ? C H2S 209 ? 1_555 103.5 ? 
34 S   ? KA H2S .   ? C H2S 208 ? 1_555 CD ? EA CD . ? C CD 202 ? 1_555 S   ? LA H2S .   ? C H2S 209 ? 1_555 87.7  ? 
35 SG  ? C  CYS 57  ? C CYS 58  ? 1_555 CD ? FA CD . ? C CD 203 ? 1_555 S   ? MA H2S .   ? C H2S 210 ? 1_555 107.0 ? 
36 SG  ? C  CYS 57  ? C CYS 58  ? 1_555 CD ? GA CD . ? C CD 204 ? 1_555 SG  ? C  CYS 58  ? C CYS 59  ? 1_555 113.9 ? 
37 SG  ? C  CYS 57  ? C CYS 58  ? 1_555 CD ? GA CD . ? C CD 204 ? 1_555 S   ? IA H2S .   ? C H2S 206 ? 1_555 87.4  ? 
38 SG  ? C  CYS 58  ? C CYS 59  ? 1_555 CD ? GA CD . ? C CD 204 ? 1_555 S   ? IA H2S .   ? C H2S 206 ? 1_555 136.0 ? 
39 SG  ? C  CYS 57  ? C CYS 58  ? 1_555 CD ? GA CD . ? C CD 204 ? 1_555 S   ? KA H2S .   ? C H2S 208 ? 1_555 87.3  ? 
40 SG  ? C  CYS 58  ? C CYS 59  ? 1_555 CD ? GA CD . ? C CD 204 ? 1_555 S   ? KA H2S .   ? C H2S 208 ? 1_555 138.3 ? 
41 S   ? IA H2S .   ? C H2S 206 ? 1_555 CD ? GA CD . ? C CD 204 ? 1_555 S   ? KA H2S .   ? C H2S 208 ? 1_555 77.0  ? 
42 SG  ? D  CYS 23  ? D CYS 24  ? 1_555 CD ? PA CD . ? D CD 201 ? 1_555 SG  ? D  CYS 58  ? D CYS 59  ? 1_555 133.1 ? 
43 SG  ? D  CYS 23  ? D CYS 24  ? 1_555 CD ? PA CD . ? D CD 201 ? 1_555 S   ? WA H2S .   ? D H2S 208 ? 1_555 143.9 ? 
44 SG  ? D  CYS 58  ? D CYS 59  ? 1_555 CD ? PA CD . ? D CD 201 ? 1_555 S   ? WA H2S .   ? D H2S 208 ? 1_555 74.9  ? 
45 SG  ? D  CYS 57  ? D CYS 58  ? 1_555 CD ? QA CD . ? D CD 202 ? 1_555 S   ? TA H2S .   ? D H2S 205 ? 1_555 107.5 ? 
46 SG  ? D  CYS 57  ? D CYS 58  ? 1_555 CD ? QA CD . ? D CD 202 ? 1_555 S   ? VA H2S .   ? D H2S 207 ? 1_555 93.0  ? 
47 S   ? TA H2S .   ? D H2S 205 ? 1_555 CD ? QA CD . ? D CD 202 ? 1_555 S   ? VA H2S .   ? D H2S 207 ? 1_555 154.5 ? 
48 SG  ? D  CYS 57  ? D CYS 58  ? 1_555 CD ? QA CD . ? D CD 202 ? 1_555 S   ? XA H2S .   ? D H2S 209 ? 1_555 101.0 ? 
49 S   ? TA H2S .   ? D H2S 205 ? 1_555 CD ? QA CD . ? D CD 202 ? 1_555 S   ? XA H2S .   ? D H2S 209 ? 1_555 72.7  ? 
50 S   ? VA H2S .   ? D H2S 207 ? 1_555 CD ? QA CD . ? D CD 202 ? 1_555 S   ? XA H2S .   ? D H2S 209 ? 1_555 88.9  ? 
51 SG  ? D  CYS 57  ? D CYS 58  ? 1_555 CD ? RA CD . ? D CD 203 ? 1_555 S   ? TA H2S .   ? D H2S 205 ? 1_555 101.8 ? 
52 SG  ? D  CYS 57  ? D CYS 58  ? 1_555 CD ? RA CD . ? D CD 203 ? 1_555 S   ? UA H2S .   ? D H2S 206 ? 1_555 107.7 ? 
53 S   ? TA H2S .   ? D H2S 205 ? 1_555 CD ? RA CD . ? D CD 203 ? 1_555 S   ? UA H2S .   ? D H2S 206 ? 1_555 90.1  ? 
54 SG  ? D  CYS 57  ? D CYS 58  ? 1_555 CD ? RA CD . ? D CD 203 ? 1_555 S   ? YA H2S .   ? D H2S 210 ? 1_555 74.9  ? 
55 S   ? TA H2S .   ? D H2S 205 ? 1_555 CD ? RA CD . ? D CD 203 ? 1_555 S   ? YA H2S .   ? D H2S 210 ? 1_555 95.0  ? 
56 S   ? UA H2S .   ? D H2S 206 ? 1_555 CD ? RA CD . ? D CD 203 ? 1_555 S   ? YA H2S .   ? D H2S 210 ? 1_555 173.7 ? 
57 SG  ? D  CYS 58  ? D CYS 59  ? 1_555 CD ? SA CD . ? D CD 204 ? 1_555 S   ? VA H2S .   ? D H2S 207 ? 1_555 144.4 ? 
58 SG  ? D  CYS 58  ? D CYS 59  ? 1_555 CD ? SA CD . ? D CD 204 ? 1_555 S   ? WA H2S .   ? D H2S 208 ? 1_555 65.3  ? 
59 S   ? VA H2S .   ? D H2S 207 ? 1_555 CD ? SA CD . ? D CD 204 ? 1_555 S   ? WA H2S .   ? D H2S 208 ? 1_555 128.2 ? 
60 SG  ? D  CYS 58  ? D CYS 59  ? 1_555 CD ? SA CD . ? D CD 204 ? 1_555 S   ? ZA H2S .   ? D H2S 211 ? 1_555 132.6 ? 
61 S   ? VA H2S .   ? D H2S 207 ? 1_555 CD ? SA CD . ? D CD 204 ? 1_555 S   ? ZA H2S .   ? D H2S 211 ? 1_555 67.4  ? 
62 S   ? WA H2S .   ? D H2S 208 ? 1_555 CD ? SA CD . ? D CD 204 ? 1_555 S   ? ZA H2S .   ? D H2S 211 ? 1_555 67.8  ? 
63 SG  ? E  CYS 23  ? E CYS 24  ? 1_555 CD ? DB CD . ? E CD 201 ? 1_555 SG  ? E  CYS 58  ? E CYS 59  ? 1_555 132.2 ? 
64 SG  ? E  CYS 23  ? E CYS 24  ? 1_555 CD ? DB CD . ? E CD 201 ? 1_555 S   ? HB H2S .   ? E H2S 205 ? 1_555 130.0 ? 
65 SG  ? E  CYS 58  ? E CYS 59  ? 1_555 CD ? DB CD . ? E CD 201 ? 1_555 S   ? HB H2S .   ? E H2S 205 ? 1_555 84.5  ? 
66 SG  ? E  CYS 57  ? E CYS 58  ? 1_555 CD ? EB CD . ? E CD 202 ? 1_555 S   ? IB H2S .   ? E H2S 206 ? 1_555 105.2 ? 
67 SG  ? E  CYS 57  ? E CYS 58  ? 1_555 CD ? EB CD . ? E CD 202 ? 1_555 S   ? JB H2S .   ? E H2S 207 ? 1_555 94.4  ? 
68 S   ? IB H2S .   ? E H2S 206 ? 1_555 CD ? EB CD . ? E CD 202 ? 1_555 S   ? JB H2S .   ? E H2S 207 ? 1_555 81.5  ? 
69 SG  ? E  CYS 57  ? E CYS 58  ? 1_555 CD ? FB CD . ? E CD 203 ? 1_555 S   ? KB H2S .   ? E H2S 208 ? 1_555 95.2  ? 
70 SG  ? E  CYS 57  ? E CYS 58  ? 1_555 CD ? FB CD . ? E CD 203 ? 1_555 S   ? MB H2S .   ? E H2S 210 ? 1_555 103.2 ? 
71 S   ? KB H2S .   ? E H2S 208 ? 1_555 CD ? FB CD . ? E CD 203 ? 1_555 S   ? MB H2S .   ? E H2S 210 ? 1_555 158.5 ? 
72 SG  ? E  CYS 58  ? E CYS 59  ? 1_555 CD ? GB CD . ? E CD 204 ? 1_555 S   ? JB H2S .   ? E H2S 207 ? 1_555 158.2 ? 
73 SG  ? F  CYS 23  ? F CYS 24  ? 1_555 CD ? PB CD . ? F CD 201 ? 1_555 SG  ? F  CYS 58  ? F CYS 59  ? 1_555 132.3 ? 
74 SG  ? F  CYS 23  ? F CYS 24  ? 1_555 CD ? PB CD . ? F CD 201 ? 1_555 S   ? UB H2S .   ? F H2S 206 ? 1_555 127.5 ? 
75 SG  ? F  CYS 58  ? F CYS 59  ? 1_555 CD ? PB CD . ? F CD 201 ? 1_555 S   ? UB H2S .   ? F H2S 206 ? 1_555 83.3  ? 
76 SG  ? F  CYS 57  ? F CYS 58  ? 1_555 CD ? QB CD . ? F CD 202 ? 1_555 S   ? TB H2S .   ? F H2S 205 ? 1_555 88.7  ? 
77 SG  ? F  CYS 57  ? F CYS 58  ? 1_555 CD ? QB CD . ? F CD 202 ? 1_555 S   ? WB H2S .   ? F H2S 208 ? 1_555 111.6 ? 
78 S   ? TB H2S .   ? F H2S 205 ? 1_555 CD ? QB CD . ? F CD 202 ? 1_555 S   ? WB H2S .   ? F H2S 208 ? 1_555 80.2  ? 
79 SG  ? F  CYS 57  ? F CYS 58  ? 1_555 CD ? QB CD . ? F CD 202 ? 1_555 S   ? XB H2S .   ? F H2S 209 ? 1_555 95.3  ? 
80 S   ? TB H2S .   ? F H2S 205 ? 1_555 CD ? QB CD . ? F CD 202 ? 1_555 S   ? XB H2S .   ? F H2S 209 ? 1_555 164.4 ? 
81 S   ? WB H2S .   ? F H2S 208 ? 1_555 CD ? QB CD . ? F CD 202 ? 1_555 S   ? XB H2S .   ? F H2S 209 ? 1_555 84.3  ? 
82 SG  ? F  CYS 57  ? F CYS 58  ? 1_555 CD ? RB CD . ? F CD 203 ? 1_555 S   ? TB H2S .   ? F H2S 205 ? 1_555 91.5  ? 
83 SG  ? F  CYS 58  ? F CYS 59  ? 1_555 CD ? SB CD . ? F CD 204 ? 1_555 S   ? VB H2S .   ? F H2S 207 ? 1_555 125.8 ? 
84 SG  ? F  CYS 58  ? F CYS 59  ? 1_555 CD ? SB CD . ? F CD 204 ? 1_555 S   ? XB H2S .   ? F H2S 209 ? 1_555 152.1 ? 
85 S   ? VB H2S .   ? F H2S 207 ? 1_555 CD ? SB CD . ? F CD 204 ? 1_555 S   ? XB H2S .   ? F H2S 209 ? 1_555 68.9  ? 
86 SG  ? F  CYS 58  ? F CYS 59  ? 1_555 CD ? SB CD . ? F CD 204 ? 1_555 O   ? FC HOH .   ? F HOH 317 ? 1_555 75.5  ? 
87 S   ? VB H2S .   ? F H2S 207 ? 1_555 CD ? SB CD . ? F CD 204 ? 1_555 O   ? FC HOH .   ? F HOH 317 ? 1_555 53.2  ? 
88 S   ? XB H2S .   ? F H2S 209 ? 1_555 CD ? SB CD . ? F CD 204 ? 1_555 O   ? FC HOH .   ? F HOH 317 ? 1_555 121.9 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 155 A . ? GLY 156 A PRO 156 A ? PRO 157 A 1 7.50  
2 GLY 155 B . ? GLY 156 B PRO 156 B ? PRO 157 B 1 3.65  
3 GLY 155 C . ? GLY 156 C PRO 156 C ? PRO 157 C 1 6.03  
4 GLY 155 D . ? GLY 156 D PRO 156 D ? PRO 157 D 1 -0.99 
5 GLY 155 E . ? GLY 156 E PRO 156 E ? PRO 157 E 1 7.59  
6 GLY 155 F . ? GLY 156 F PRO 156 F ? PRO 157 F 1 6.04  
# 
_pdbx_entry_details.entry_id                   8ZN8 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OE1 A GLU 137 ? ? S   A H2S 210 ? ? 1.47 
2  1 O   E HOH 360 ? ? O   E HOH 369 ? ? 1.83 
3  1 OD1 C ASP 102 ? ? O   C HOH 301 ? ? 1.91 
4  1 OG  E SER 3   ? ? O   E HOH 301 ? ? 2.02 
5  1 S   E H2S 209 ? ? O   E HOH 354 ? ? 2.05 
6  1 O   A HOH 340 ? ? O   A HOH 346 ? ? 2.06 
7  1 O   A HOH 378 ? ? O   A HOH 388 ? ? 2.08 
8  1 O   A HOH 366 ? ? O   A HOH 372 ? ? 2.09 
9  1 O   E HOH 370 ? ? O   E HOH 374 ? ? 2.09 
10 1 O   B HOH 337 ? ? O   B HOH 378 ? ? 2.16 
11 1 NZ  C LYS 128 ? ? OD2 C ASP 132 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OH  F TYR 163 ? ? 1_555 OE1 F GLU 168 ? ? 3_555 2.15 
2 1 OE2 C GLU 136 ? ? 1_555 NZ  D LYS 128 ? ? 6_554 2.18 
3 1 NZ  A LYS 128 ? ? 1_555 OD1 D ASP 132 ? ? 8_554 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 TYR A 134 ? ? -129.26 -52.62 
2  1 TYR B 134 ? ? -126.27 -50.01 
3  1 VAL C 43  ? ? -121.51 -60.51 
4  1 TYR C 134 ? ? -132.12 -54.74 
5  1 VAL D 43  ? ? -125.86 -59.67 
6  1 ASP D 123 ? ? -113.89 79.31  
7  1 TYR D 134 ? ? -133.27 -49.77 
8  1 VAL E 43  ? ? -120.63 -63.03 
9  1 LEU E 45  ? ? -118.45 79.58  
10 1 TYR E 134 ? ? -132.45 -51.95 
11 1 VAL F 43  ? ? -121.67 -61.70 
12 1 ASP F 123 ? ? -110.14 79.98  
13 1 TYR F 134 ? ? -132.55 -53.77 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 D MG  212 ? AB MG  . 
2 1 B HOH 301 ? BC HOH . 
# 
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  
CD  CD   CD N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
H2S S    S  N N 138 
H2S HS1  H  N N 139 
H2S HS2  H  N N 140 
HIS N    N  N N 141 
HIS CA   C  N S 142 
HIS C    C  N N 143 
HIS O    O  N N 144 
HIS CB   C  N N 145 
HIS CG   C  Y N 146 
HIS ND1  N  Y N 147 
HIS CD2  C  Y N 148 
HIS CE1  C  Y N 149 
HIS NE2  N  Y N 150 
HIS OXT  O  N N 151 
HIS H    H  N N 152 
HIS H2   H  N N 153 
HIS HA   H  N N 154 
HIS HB2  H  N N 155 
HIS HB3  H  N N 156 
HIS HD1  H  N N 157 
HIS HD2  H  N N 158 
HIS HE1  H  N N 159 
HIS HE2  H  N N 160 
HIS HXT  H  N N 161 
HOH O    O  N N 162 
HOH H1   H  N N 163 
HOH H2   H  N N 164 
ILE N    N  N N 165 
ILE CA   C  N S 166 
ILE C    C  N N 167 
ILE O    O  N N 168 
ILE CB   C  N S 169 
ILE CG1  C  N N 170 
ILE CG2  C  N N 171 
ILE CD1  C  N N 172 
ILE OXT  O  N N 173 
ILE H    H  N N 174 
ILE H2   H  N N 175 
ILE HA   H  N N 176 
ILE HB   H  N N 177 
ILE HG12 H  N N 178 
ILE HG13 H  N N 179 
ILE HG21 H  N N 180 
ILE HG22 H  N N 181 
ILE HG23 H  N N 182 
ILE HD11 H  N N 183 
ILE HD12 H  N N 184 
ILE HD13 H  N N 185 
ILE HXT  H  N N 186 
LEU N    N  N N 187 
LEU CA   C  N S 188 
LEU C    C  N N 189 
LEU O    O  N N 190 
LEU CB   C  N N 191 
LEU CG   C  N N 192 
LEU CD1  C  N N 193 
LEU CD2  C  N N 194 
LEU OXT  O  N N 195 
LEU H    H  N N 196 
LEU H2   H  N N 197 
LEU HA   H  N N 198 
LEU HB2  H  N N 199 
LEU HB3  H  N N 200 
LEU HG   H  N N 201 
LEU HD11 H  N N 202 
LEU HD12 H  N N 203 
LEU HD13 H  N N 204 
LEU HD21 H  N N 205 
LEU HD22 H  N N 206 
LEU HD23 H  N N 207 
LEU HXT  H  N N 208 
LYS N    N  N N 209 
LYS CA   C  N S 210 
LYS C    C  N N 211 
LYS O    O  N N 212 
LYS CB   C  N N 213 
LYS CG   C  N N 214 
LYS CD   C  N N 215 
LYS CE   C  N N 216 
LYS NZ   N  N N 217 
LYS OXT  O  N N 218 
LYS H    H  N N 219 
LYS H2   H  N N 220 
LYS HA   H  N N 221 
LYS HB2  H  N N 222 
LYS HB3  H  N N 223 
LYS HG2  H  N N 224 
LYS HG3  H  N N 225 
LYS HD2  H  N N 226 
LYS HD3  H  N N 227 
LYS HE2  H  N N 228 
LYS HE3  H  N N 229 
LYS HZ1  H  N N 230 
LYS HZ2  H  N N 231 
LYS HZ3  H  N N 232 
LYS HXT  H  N N 233 
MET N    N  N N 234 
MET CA   C  N S 235 
MET C    C  N N 236 
MET O    O  N N 237 
MET CB   C  N N 238 
MET CG   C  N N 239 
MET SD   S  N N 240 
MET CE   C  N N 241 
MET OXT  O  N N 242 
MET H    H  N N 243 
MET H2   H  N N 244 
MET HA   H  N N 245 
MET HB2  H  N N 246 
MET HB3  H  N N 247 
MET HG2  H  N N 248 
MET HG3  H  N N 249 
MET HE1  H  N N 250 
MET HE2  H  N N 251 
MET HE3  H  N N 252 
MET HXT  H  N N 253 
MG  MG   MG N N 254 
PHE N    N  N N 255 
PHE CA   C  N S 256 
PHE C    C  N N 257 
PHE O    O  N N 258 
PHE CB   C  N N 259 
PHE CG   C  Y N 260 
PHE CD1  C  Y N 261 
PHE CD2  C  Y N 262 
PHE CE1  C  Y N 263 
PHE CE2  C  Y N 264 
PHE CZ   C  Y N 265 
PHE OXT  O  N N 266 
PHE H    H  N N 267 
PHE H2   H  N N 268 
PHE HA   H  N N 269 
PHE HB2  H  N N 270 
PHE HB3  H  N N 271 
PHE HD1  H  N N 272 
PHE HD2  H  N N 273 
PHE HE1  H  N N 274 
PHE HE2  H  N N 275 
PHE HZ   H  N N 276 
PHE HXT  H  N N 277 
PRO N    N  N N 278 
PRO CA   C  N S 279 
PRO C    C  N N 280 
PRO O    O  N N 281 
PRO CB   C  N N 282 
PRO CG   C  N N 283 
PRO CD   C  N N 284 
PRO OXT  O  N N 285 
PRO H    H  N N 286 
PRO HA   H  N N 287 
PRO HB2  H  N N 288 
PRO HB3  H  N N 289 
PRO HG2  H  N N 290 
PRO HG3  H  N N 291 
PRO HD2  H  N N 292 
PRO HD3  H  N N 293 
PRO HXT  H  N N 294 
SER N    N  N N 295 
SER CA   C  N S 296 
SER C    C  N N 297 
SER O    O  N N 298 
SER CB   C  N N 299 
SER OG   O  N N 300 
SER OXT  O  N N 301 
SER H    H  N N 302 
SER H2   H  N N 303 
SER HA   H  N N 304 
SER HB2  H  N N 305 
SER HB3  H  N N 306 
SER HG   H  N N 307 
SER HXT  H  N N 308 
SO4 S    S  N N 309 
SO4 O1   O  N N 310 
SO4 O2   O  N N 311 
SO4 O3   O  N N 312 
SO4 O4   O  N N 313 
THR N    N  N N 314 
THR CA   C  N S 315 
THR C    C  N N 316 
THR O    O  N N 317 
THR CB   C  N R 318 
THR OG1  O  N N 319 
THR CG2  C  N N 320 
THR OXT  O  N N 321 
THR H    H  N N 322 
THR H2   H  N N 323 
THR HA   H  N N 324 
THR HB   H  N N 325 
THR HG1  H  N N 326 
THR HG21 H  N N 327 
THR HG22 H  N N 328 
THR HG23 H  N N 329 
THR HXT  H  N N 330 
TRP N    N  N N 331 
TRP CA   C  N S 332 
TRP C    C  N N 333 
TRP O    O  N N 334 
TRP CB   C  N N 335 
TRP CG   C  Y N 336 
TRP CD1  C  Y N 337 
TRP CD2  C  Y N 338 
TRP NE1  N  Y N 339 
TRP CE2  C  Y N 340 
TRP CE3  C  Y N 341 
TRP CZ2  C  Y N 342 
TRP CZ3  C  Y N 343 
TRP CH2  C  Y N 344 
TRP OXT  O  N N 345 
TRP H    H  N N 346 
TRP H2   H  N N 347 
TRP HA   H  N N 348 
TRP HB2  H  N N 349 
TRP HB3  H  N N 350 
TRP HD1  H  N N 351 
TRP HE1  H  N N 352 
TRP HE3  H  N N 353 
TRP HZ2  H  N N 354 
TRP HZ3  H  N N 355 
TRP HH2  H  N N 356 
TRP HXT  H  N N 357 
TYR N    N  N N 358 
TYR CA   C  N S 359 
TYR C    C  N N 360 
TYR O    O  N N 361 
TYR CB   C  N N 362 
TYR CG   C  Y N 363 
TYR CD1  C  Y N 364 
TYR CD2  C  Y N 365 
TYR CE1  C  Y N 366 
TYR CE2  C  Y N 367 
TYR CZ   C  Y N 368 
TYR OH   O  N N 369 
TYR OXT  O  N N 370 
TYR H    H  N N 371 
TYR H2   H  N N 372 
TYR HA   H  N N 373 
TYR HB2  H  N N 374 
TYR HB3  H  N N 375 
TYR HD1  H  N N 376 
TYR HD2  H  N N 377 
TYR HE1  H  N N 378 
TYR HE2  H  N N 379 
TYR HH   H  N N 380 
TYR HXT  H  N N 381 
VAL N    N  N N 382 
VAL CA   C  N S 383 
VAL C    C  N N 384 
VAL O    O  N N 385 
VAL CB   C  N N 386 
VAL CG1  C  N N 387 
VAL CG2  C  N N 388 
VAL OXT  O  N N 389 
VAL H    H  N N 390 
VAL H2   H  N N 391 
VAL HA   H  N N 392 
VAL HB   H  N N 393 
VAL HG11 H  N N 394 
VAL HG12 H  N N 395 
VAL HG13 H  N N 396 
VAL HG21 H  N N 397 
VAL HG22 H  N N 398 
VAL HG23 H  N N 399 
VAL HXT  H  N N 400 
# 
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  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
H2S S   HS1  sing N N 129 
H2S S   HS2  sing N N 130 
HIS N   CA   sing N N 131 
HIS N   H    sing N N 132 
HIS N   H2   sing N N 133 
HIS CA  C    sing N N 134 
HIS CA  CB   sing N N 135 
HIS CA  HA   sing N N 136 
HIS C   O    doub N N 137 
HIS C   OXT  sing N N 138 
HIS CB  CG   sing N N 139 
HIS CB  HB2  sing N N 140 
HIS CB  HB3  sing N N 141 
HIS CG  ND1  sing Y N 142 
HIS CG  CD2  doub Y N 143 
HIS ND1 CE1  doub Y N 144 
HIS ND1 HD1  sing N N 145 
HIS CD2 NE2  sing Y N 146 
HIS CD2 HD2  sing N N 147 
HIS CE1 NE2  sing Y N 148 
HIS CE1 HE1  sing N N 149 
HIS NE2 HE2  sing N N 150 
HIS OXT HXT  sing N N 151 
HOH O   H1   sing N N 152 
HOH O   H2   sing N N 153 
ILE N   CA   sing N N 154 
ILE N   H    sing N N 155 
ILE N   H2   sing N N 156 
ILE CA  C    sing N N 157 
ILE CA  CB   sing N N 158 
ILE CA  HA   sing N N 159 
ILE C   O    doub N N 160 
ILE C   OXT  sing N N 161 
ILE CB  CG1  sing N N 162 
ILE CB  CG2  sing N N 163 
ILE CB  HB   sing N N 164 
ILE CG1 CD1  sing N N 165 
ILE CG1 HG12 sing N N 166 
ILE CG1 HG13 sing N N 167 
ILE CG2 HG21 sing N N 168 
ILE CG2 HG22 sing N N 169 
ILE CG2 HG23 sing N N 170 
ILE CD1 HD11 sing N N 171 
ILE CD1 HD12 sing N N 172 
ILE CD1 HD13 sing N N 173 
ILE OXT HXT  sing N N 174 
LEU N   CA   sing N N 175 
LEU N   H    sing N N 176 
LEU N   H2   sing N N 177 
LEU CA  C    sing N N 178 
LEU CA  CB   sing N N 179 
LEU CA  HA   sing N N 180 
LEU C   O    doub N N 181 
LEU C   OXT  sing N N 182 
LEU CB  CG   sing N N 183 
LEU CB  HB2  sing N N 184 
LEU CB  HB3  sing N N 185 
LEU CG  CD1  sing N N 186 
LEU CG  CD2  sing N N 187 
LEU CG  HG   sing N N 188 
LEU CD1 HD11 sing N N 189 
LEU CD1 HD12 sing N N 190 
LEU CD1 HD13 sing N N 191 
LEU CD2 HD21 sing N N 192 
LEU CD2 HD22 sing N N 193 
LEU CD2 HD23 sing N N 194 
LEU OXT HXT  sing N N 195 
LYS N   CA   sing N N 196 
LYS N   H    sing N N 197 
LYS N   H2   sing N N 198 
LYS CA  C    sing N N 199 
LYS CA  CB   sing N N 200 
LYS CA  HA   sing N N 201 
LYS C   O    doub N N 202 
LYS C   OXT  sing N N 203 
LYS CB  CG   sing N N 204 
LYS CB  HB2  sing N N 205 
LYS CB  HB3  sing N N 206 
LYS CG  CD   sing N N 207 
LYS CG  HG2  sing N N 208 
LYS CG  HG3  sing N N 209 
LYS CD  CE   sing N N 210 
LYS CD  HD2  sing N N 211 
LYS CD  HD3  sing N N 212 
LYS CE  NZ   sing N N 213 
LYS CE  HE2  sing N N 214 
LYS CE  HE3  sing N N 215 
LYS NZ  HZ1  sing N N 216 
LYS NZ  HZ2  sing N N 217 
LYS NZ  HZ3  sing N N 218 
LYS OXT HXT  sing N N 219 
MET N   CA   sing N N 220 
MET N   H    sing N N 221 
MET N   H2   sing N N 222 
MET CA  C    sing N N 223 
MET CA  CB   sing N N 224 
MET CA  HA   sing N N 225 
MET C   O    doub N N 226 
MET C   OXT  sing N N 227 
MET CB  CG   sing N N 228 
MET CB  HB2  sing N N 229 
MET CB  HB3  sing N N 230 
MET CG  SD   sing N N 231 
MET CG  HG2  sing N N 232 
MET CG  HG3  sing N N 233 
MET SD  CE   sing N N 234 
MET CE  HE1  sing N N 235 
MET CE  HE2  sing N N 236 
MET CE  HE3  sing N N 237 
MET OXT HXT  sing N N 238 
PHE N   CA   sing N N 239 
PHE N   H    sing N N 240 
PHE N   H2   sing N N 241 
PHE CA  C    sing N N 242 
PHE CA  CB   sing N N 243 
PHE CA  HA   sing N N 244 
PHE C   O    doub N N 245 
PHE C   OXT  sing N N 246 
PHE CB  CG   sing N N 247 
PHE CB  HB2  sing N N 248 
PHE CB  HB3  sing N N 249 
PHE CG  CD1  doub Y N 250 
PHE CG  CD2  sing Y N 251 
PHE CD1 CE1  sing Y N 252 
PHE CD1 HD1  sing N N 253 
PHE CD2 CE2  doub Y N 254 
PHE CD2 HD2  sing N N 255 
PHE CE1 CZ   doub Y N 256 
PHE CE1 HE1  sing N N 257 
PHE CE2 CZ   sing Y N 258 
PHE CE2 HE2  sing N N 259 
PHE CZ  HZ   sing N N 260 
PHE OXT HXT  sing N N 261 
PRO N   CA   sing N N 262 
PRO N   CD   sing N N 263 
PRO N   H    sing N N 264 
PRO CA  C    sing N N 265 
PRO CA  CB   sing N N 266 
PRO CA  HA   sing N N 267 
PRO C   O    doub N N 268 
PRO C   OXT  sing N N 269 
PRO CB  CG   sing N N 270 
PRO CB  HB2  sing N N 271 
PRO CB  HB3  sing N N 272 
PRO CG  CD   sing N N 273 
PRO CG  HG2  sing N N 274 
PRO CG  HG3  sing N N 275 
PRO CD  HD2  sing N N 276 
PRO CD  HD3  sing N N 277 
PRO OXT HXT  sing N N 278 
SER N   CA   sing N N 279 
SER N   H    sing N N 280 
SER N   H2   sing N N 281 
SER CA  C    sing N N 282 
SER CA  CB   sing N N 283 
SER CA  HA   sing N N 284 
SER C   O    doub N N 285 
SER C   OXT  sing N N 286 
SER CB  OG   sing N N 287 
SER CB  HB2  sing N N 288 
SER CB  HB3  sing N N 289 
SER OG  HG   sing N N 290 
SER OXT HXT  sing N N 291 
SO4 S   O1   doub N N 292 
SO4 S   O2   doub N N 293 
SO4 S   O3   sing N N 294 
SO4 S   O4   sing N N 295 
THR N   CA   sing N N 296 
THR N   H    sing N N 297 
THR N   H2   sing N N 298 
THR CA  C    sing N N 299 
THR CA  CB   sing N N 300 
THR CA  HA   sing N N 301 
THR C   O    doub N N 302 
THR C   OXT  sing N N 303 
THR CB  OG1  sing N N 304 
THR CB  CG2  sing N N 305 
THR CB  HB   sing N N 306 
THR OG1 HG1  sing N N 307 
THR CG2 HG21 sing N N 308 
THR CG2 HG22 sing N N 309 
THR CG2 HG23 sing N N 310 
THR OXT HXT  sing N N 311 
TRP N   CA   sing N N 312 
TRP N   H    sing N N 313 
TRP N   H2   sing N N 314 
TRP CA  C    sing N N 315 
TRP CA  CB   sing N N 316 
TRP CA  HA   sing N N 317 
TRP C   O    doub N N 318 
TRP C   OXT  sing N N 319 
TRP CB  CG   sing N N 320 
TRP CB  HB2  sing N N 321 
TRP CB  HB3  sing N N 322 
TRP CG  CD1  doub Y N 323 
TRP CG  CD2  sing Y N 324 
TRP CD1 NE1  sing Y N 325 
TRP CD1 HD1  sing N N 326 
TRP CD2 CE2  doub Y N 327 
TRP CD2 CE3  sing Y N 328 
TRP NE1 CE2  sing Y N 329 
TRP NE1 HE1  sing N N 330 
TRP CE2 CZ2  sing Y N 331 
TRP CE3 CZ3  doub Y N 332 
TRP CE3 HE3  sing N N 333 
TRP CZ2 CH2  doub Y N 334 
TRP CZ2 HZ2  sing N N 335 
TRP CZ3 CH2  sing Y N 336 
TRP CZ3 HZ3  sing N N 337 
TRP CH2 HH2  sing N N 338 
TRP OXT HXT  sing N N 339 
TYR N   CA   sing N N 340 
TYR N   H    sing N N 341 
TYR N   H2   sing N N 342 
TYR CA  C    sing N N 343 
TYR CA  CB   sing N N 344 
TYR CA  HA   sing N N 345 
TYR C   O    doub N N 346 
TYR C   OXT  sing N N 347 
TYR CB  CG   sing N N 348 
TYR CB  HB2  sing N N 349 
TYR CB  HB3  sing N N 350 
TYR CG  CD1  doub Y N 351 
TYR CG  CD2  sing Y N 352 
TYR CD1 CE1  sing Y N 353 
TYR CD1 HD1  sing N N 354 
TYR CD2 CE2  doub Y N 355 
TYR CD2 HD2  sing N N 356 
TYR CE1 CZ   doub Y N 357 
TYR CE1 HE1  sing N N 358 
TYR CE2 CZ   sing Y N 359 
TYR CE2 HE2  sing N N 360 
TYR CZ  OH   sing N N 361 
TYR OH  HH   sing N N 362 
TYR OXT HXT  sing N N 363 
VAL N   CA   sing N N 364 
VAL N   H    sing N N 365 
VAL N   H2   sing N N 366 
VAL CA  C    sing N N 367 
VAL CA  CB   sing N N 368 
VAL CA  HA   sing N N 369 
VAL C   O    doub N N 370 
VAL C   OXT  sing N N 371 
VAL CB  CG1  sing N N 372 
VAL CB  CG2  sing N N 373 
VAL CB  HB   sing N N 374 
VAL CG1 HG11 sing N N 375 
VAL CG1 HG12 sing N N 376 
VAL CG1 HG13 sing N N 377 
VAL CG2 HG21 sing N N 378 
VAL CG2 HG22 sing N N 379 
VAL CG2 HG23 sing N N 380 
VAL OXT HXT  sing N N 381 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6a4u 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZN8 
_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]   0.007890 
_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]   0.007890 
_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]   0.005620 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CD 
MG 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A  1 1   ? 41.486 7.461   -16.917 1.00 58.13 ? 2   ALA A N   1 
ATOM   2    C  CA  . ALA A  1 1   ? 42.139 8.660   -16.405 1.00 70.44 ? 2   ALA A CA  1 
ATOM   3    C  C   . ALA A  1 1   ? 42.356 9.702   -17.511 1.00 66.51 ? 2   ALA A C   1 
ATOM   4    O  O   . ALA A  1 1   ? 41.705 9.678   -18.565 1.00 63.26 ? 2   ALA A O   1 
ATOM   5    C  CB  . ALA A  1 1   ? 43.498 8.299   -15.736 1.00 69.51 ? 2   ALA A CB  1 
ATOM   6    N  N   . SER A  1 2   ? 43.284 10.618  -17.249 1.00 53.98 ? 3   SER A N   1 
ATOM   7    C  CA  . SER A  1 2   ? 43.614 11.646  -18.217 1.00 50.42 ? 3   SER A CA  1 
ATOM   8    C  C   . SER A  1 2   ? 44.410 11.036  -19.360 1.00 48.91 ? 3   SER A C   1 
ATOM   9    O  O   . SER A  1 2   ? 45.194 10.105  -19.163 1.00 48.73 ? 3   SER A O   1 
ATOM   10   C  CB  . SER A  1 2   ? 44.413 12.767  -17.551 1.00 45.07 ? 3   SER A CB  1 
ATOM   11   O  OG  . SER A  1 2   ? 44.101 14.032  -18.121 1.00 50.66 ? 3   SER A OG  1 
ATOM   12   N  N   . GLN A  1 3   ? 44.173 11.540  -20.569 1.00 39.62 ? 4   GLN A N   1 
ATOM   13   C  CA  . GLN A  1 3   ? 45.011 11.181  -21.697 1.00 39.67 ? 4   GLN A CA  1 
ATOM   14   C  C   . GLN A  1 3   ? 46.401 11.802  -21.603 1.00 36.47 ? 4   GLN A C   1 
ATOM   15   O  O   . GLN A  1 3   ? 47.284 11.402  -22.358 1.00 34.92 ? 4   GLN A O   1 
ATOM   16   C  CB  . GLN A  1 3   ? 44.326 11.598  -23.009 1.00 41.18 ? 4   GLN A CB  1 
ATOM   17   C  CG  . GLN A  1 3   ? 44.345 13.116  -23.254 1.00 44.15 ? 4   GLN A CG  1 
ATOM   18   C  CD  . GLN A  1 3   ? 43.393 13.582  -24.373 1.00 44.92 ? 4   GLN A CD  1 
ATOM   19   O  OE1 . GLN A  1 3   ? 43.096 12.840  -25.315 1.00 44.75 ? 4   GLN A OE1 1 
ATOM   20   N  NE2 . GLN A  1 3   ? 42.931 14.826  -24.270 1.00 39.92 ? 4   GLN A NE2 1 
ATOM   21   N  N   . VAL A  1 4   ? 46.624 12.762  -20.706 1.00 35.59 ? 5   VAL A N   1 
ATOM   22   C  CA  . VAL A  1 4   ? 47.925 13.416  -20.594 1.00 34.39 ? 5   VAL A CA  1 
ATOM   23   C  C   . VAL A  1 4   ? 48.679 13.028  -19.332 1.00 36.51 ? 5   VAL A C   1 
ATOM   24   O  O   . VAL A  1 4   ? 49.888 13.290  -19.259 1.00 37.84 ? 5   VAL A O   1 
ATOM   25   C  CB  . VAL A  1 4   ? 47.806 14.956  -20.673 1.00 37.04 ? 5   VAL A CB  1 
ATOM   26   C  CG1 . VAL A  1 4   ? 46.900 15.379  -21.813 1.00 35.80 ? 5   VAL A CG1 1 
ATOM   27   C  CG2 . VAL A  1 4   ? 47.320 15.541  -19.346 1.00 35.12 ? 5   VAL A CG2 1 
ATOM   28   N  N   . ARG A  1 5   ? 48.019 12.422  -18.343 1.00 33.63 ? 6   ARG A N   1 
ATOM   29   C  CA  . ARG A  1 5   ? 48.653 12.166  -17.054 1.00 35.47 ? 6   ARG A CA  1 
ATOM   30   C  C   . ARG A  1 5   ? 49.781 11.140  -17.180 1.00 35.40 ? 6   ARG A C   1 
ATOM   31   O  O   . ARG A  1 5   ? 49.594 10.070  -17.766 1.00 30.66 ? 6   ARG A O   1 
ATOM   32   C  CB  . ARG A  1 5   ? 47.613 11.680  -16.047 1.00 36.27 ? 6   ARG A CB  1 
ATOM   33   C  CG  . ARG A  1 5   ? 48.075 11.800  -14.605 1.00 33.43 ? 6   ARG A CG  1 
ATOM   34   C  CD  . ARG A  1 5   ? 47.237 10.957  -13.663 1.00 32.77 ? 6   ARG A CD  1 
ATOM   35   N  NE  . ARG A  1 5   ? 47.625 11.197  -12.278 1.00 40.22 ? 6   ARG A NE  1 
ATOM   36   C  CZ  . ARG A  1 5   ? 46.893 11.885  -11.408 1.00 46.23 ? 6   ARG A CZ  1 
ATOM   37   N  NH1 . ARG A  1 5   ? 45.698 12.354  -11.732 1.00 40.89 ? 6   ARG A NH1 1 
ATOM   38   N  NH2 . ARG A  1 5   ? 47.371 12.109  -10.184 1.00 40.58 ? 6   ARG A NH2 1 
ATOM   39   N  N   . GLN A  1 6   ? 50.949 11.463  -16.610 1.00 30.51 ? 7   GLN A N   1 
ATOM   40   C  CA  . GLN A  1 6   ? 52.097 10.552  -16.628 1.00 32.87 ? 7   GLN A CA  1 
ATOM   41   C  C   . GLN A  1 6   ? 53.031 10.901  -15.473 1.00 32.67 ? 7   GLN A C   1 
ATOM   42   O  O   . GLN A  1 6   ? 53.464 12.059  -15.341 1.00 30.40 ? 7   GLN A O   1 
ATOM   43   C  CB  . GLN A  1 6   ? 52.823 10.636  -17.981 1.00 32.58 ? 7   GLN A CB  1 
ATOM   44   C  CG  . GLN A  1 6   ? 53.860 9.545   -18.238 1.00 36.46 ? 7   GLN A CG  1 
ATOM   45   C  CD  . GLN A  1 6   ? 54.526 9.672   -19.612 1.00 42.87 ? 7   GLN A CD  1 
ATOM   46   O  OE1 . GLN A  1 6   ? 54.422 10.706  -20.273 1.00 41.40 ? 7   GLN A OE1 1 
ATOM   47   N  NE2 . GLN A  1 6   ? 55.224 8.624   -20.033 1.00 42.79 ? 7   GLN A NE2 1 
ATOM   48   N  N   . ASN A  1 7   ? 53.329 9.912   -14.628 1.00 30.56 ? 8   ASN A N   1 
ATOM   49   C  CA  . ASN A  1 7   ? 54.252 10.086  -13.496 1.00 34.72 ? 8   ASN A CA  1 
ATOM   50   C  C   . ASN A  1 7   ? 53.790 11.171  -12.514 1.00 32.20 ? 8   ASN A C   1 
ATOM   51   O  O   . ASN A  1 7   ? 54.600 11.930  -11.977 1.00 34.18 ? 8   ASN A O   1 
ATOM   52   C  CB  . ASN A  1 7   ? 55.680 10.383  -13.982 1.00 31.00 ? 8   ASN A CB  1 
ATOM   53   C  CG  . ASN A  1 7   ? 56.716 10.200  -12.866 1.00 35.57 ? 8   ASN A CG  1 
ATOM   54   O  OD1 . ASN A  1 7   ? 56.660 9.213   -12.132 1.00 36.73 ? 8   ASN A OD1 1 
ATOM   55   N  ND2 . ASN A  1 7   ? 57.642 11.159  -12.721 1.00 29.25 ? 8   ASN A ND2 1 
ATOM   56   N  N   . TYR A  1 8   ? 52.486 11.249  -12.262 1.00 32.41 ? 9   TYR A N   1 
ATOM   57   C  CA  . TYR A  1 8   ? 51.907 12.304  -11.425 1.00 35.87 ? 9   TYR A CA  1 
ATOM   58   C  C   . TYR A  1 8   ? 51.117 11.636  -10.301 1.00 39.34 ? 9   TYR A C   1 
ATOM   59   O  O   . TYR A  1 8   ? 49.983 11.192  -10.505 1.00 32.75 ? 9   TYR A O   1 
ATOM   60   C  CB  . TYR A  1 8   ? 51.024 13.229  -12.259 1.00 34.70 ? 9   TYR A CB  1 
ATOM   61   C  CG  . TYR A  1 8   ? 50.620 14.504  -11.551 1.00 38.24 ? 9   TYR A CG  1 
ATOM   62   C  CD1 . TYR A  1 8   ? 51.569 15.333  -10.951 1.00 33.46 ? 9   TYR A CD1 1 
ATOM   63   C  CD2 . TYR A  1 8   ? 49.287 14.886  -11.491 1.00 35.90 ? 9   TYR A CD2 1 
ATOM   64   C  CE1 . TYR A  1 8   ? 51.187 16.500  -10.294 1.00 35.01 ? 9   TYR A CE1 1 
ATOM   65   C  CE2 . TYR A  1 8   ? 48.898 16.053  -10.844 1.00 36.51 ? 9   TYR A CE2 1 
ATOM   66   C  CZ  . TYR A  1 8   ? 49.841 16.850  -10.253 1.00 35.98 ? 9   TYR A CZ  1 
ATOM   67   O  OH  . TYR A  1 8   ? 49.426 17.998  -9.625  1.00 36.91 ? 9   TYR A OH  1 
ATOM   68   N  N   . HIS A  1 9   ? 51.718 11.561  -9.121  1.00 40.81 ? 10  HIS A N   1 
ATOM   69   C  CA  . HIS A  1 9   ? 51.163 10.756  -8.049  1.00 41.23 ? 10  HIS A CA  1 
ATOM   70   C  C   . HIS A  1 9   ? 49.965 11.475  -7.435  1.00 43.92 ? 10  HIS A C   1 
ATOM   71   O  O   . HIS A  1 9   ? 49.876 12.707  -7.438  1.00 36.73 ? 10  HIS A O   1 
ATOM   72   C  CB  . HIS A  1 9   ? 52.241 10.469  -6.996  1.00 44.34 ? 10  HIS A CB  1 
ATOM   73   C  CG  . HIS A  1 9   ? 51.840 9.468   -5.944  1.00 57.42 ? 10  HIS A CG  1 
ATOM   74   N  ND1 . HIS A  1 9   ? 52.590 8.342   -5.669  1.00 57.87 ? 10  HIS A ND1 1 
ATOM   75   C  CD2 . HIS A  1 9   ? 50.798 9.442   -5.075  1.00 54.51 ? 10  HIS A CD2 1 
ATOM   76   C  CE1 . HIS A  1 9   ? 52.019 7.660   -4.691  1.00 54.12 ? 10  HIS A CE1 1 
ATOM   77   N  NE2 . HIS A  1 9   ? 50.928 8.304   -4.316  1.00 54.31 ? 10  HIS A NE2 1 
ATOM   78   N  N   . GLU A  1 10  ? 49.029 10.685  -6.915  1.00 45.10 ? 11  GLU A N   1 
ATOM   79   C  CA  . GLU A  1 10  ? 47.821 11.266  -6.349  1.00 44.48 ? 11  GLU A CA  1 
ATOM   80   C  C   . GLU A  1 10  ? 48.125 12.168  -5.158  1.00 43.05 ? 11  GLU A C   1 
ATOM   81   O  O   . GLU A  1 10  ? 47.437 13.175  -4.963  1.00 40.34 ? 11  GLU A O   1 
ATOM   82   C  CB  . GLU A  1 10  ? 46.851 10.153  -5.973  1.00 49.73 ? 11  GLU A CB  1 
ATOM   83   C  CG  . GLU A  1 10  ? 45.619 10.134  -6.874  1.00 60.43 ? 11  GLU A CG  1 
ATOM   84   C  CD  . GLU A  1 10  ? 44.781 8.877   -6.706  1.00 77.29 ? 11  GLU A CD  1 
ATOM   85   O  OE1 . GLU A  1 10  ? 45.163 7.832   -7.281  1.00 81.65 ? 11  GLU A OE1 1 
ATOM   86   O  OE2 . GLU A  1 10  ? 43.742 8.935   -6.006  1.00 82.49 ? 11  GLU A OE2 1 
ATOM   87   N  N   . ASP A  1 11  ? 49.165 11.864  -4.371  1.00 37.49 ? 12  ASP A N   1 
ATOM   88   C  CA  . ASP A  1 11  ? 49.426 12.731  -3.230  1.00 43.96 ? 12  ASP A CA  1 
ATOM   89   C  C   . ASP A  1 11  ? 50.053 14.059  -3.647  1.00 43.79 ? 12  ASP A C   1 
ATOM   90   O  O   . ASP A  1 11  ? 49.901 15.050  -2.926  1.00 43.21 ? 12  ASP A O   1 
ATOM   91   C  CB  . ASP A  1 11  ? 50.289 12.019  -2.174  1.00 48.87 ? 12  ASP A CB  1 
ATOM   92   C  CG  . ASP A  1 11  ? 51.619 11.532  -2.711  1.00 64.39 ? 12  ASP A CG  1 
ATOM   93   O  OD1 . ASP A  1 11  ? 52.288 10.739  -2.000  1.00 66.34 ? 12  ASP A OD1 1 
ATOM   94   O  OD2 . ASP A  1 11  ? 52.018 11.958  -3.822  1.00 63.90 ? 12  ASP A OD2 1 
ATOM   95   N  N   . ALA A  1 12  ? 50.737 14.111  -4.795  1.00 38.04 ? 13  ALA A N   1 
ATOM   96   C  CA  . ALA A  1 12  ? 51.140 15.402  -5.339  1.00 39.16 ? 13  ALA A CA  1 
ATOM   97   C  C   . ALA A  1 12  ? 49.923 16.191  -5.802  1.00 38.33 ? 13  ALA A C   1 
ATOM   98   O  O   . ALA A  1 12  ? 49.827 17.397  -5.547  1.00 35.63 ? 13  ALA A O   1 
ATOM   99   C  CB  . ALA A  1 12  ? 52.128 15.217  -6.490  1.00 39.44 ? 13  ALA A CB  1 
ATOM   100  N  N   . GLU A  1 13  ? 48.973 15.518  -6.460  1.00 37.60 ? 14  GLU A N   1 
ATOM   101  C  CA  . GLU A  1 13  ? 47.753 16.184  -6.902  1.00 34.97 ? 14  GLU A CA  1 
ATOM   102  C  C   . GLU A  1 13  ? 47.036 16.856  -5.729  1.00 36.10 ? 14  GLU A C   1 
ATOM   103  O  O   . GLU A  1 13  ? 46.687 18.043  -5.797  1.00 31.72 ? 14  GLU A O   1 
ATOM   104  C  CB  . GLU A  1 13  ? 46.852 15.167  -7.602  1.00 35.71 ? 14  GLU A CB  1 
ATOM   105  C  CG  . GLU A  1 13  ? 45.589 15.747  -8.220  1.00 39.24 ? 14  GLU A CG  1 
ATOM   106  C  CD  . GLU A  1 13  ? 44.733 14.688  -8.918  1.00 45.14 ? 14  GLU A CD  1 
ATOM   107  O  OE1 . GLU A  1 13  ? 45.111 13.492  -8.903  1.00 46.33 ? 14  GLU A OE1 1 
ATOM   108  O  OE2 . GLU A  1 13  ? 43.667 15.050  -9.472  1.00 43.76 ? 14  GLU A OE2 1 
ATOM   109  N  N   . ALA A  1 14  ? 46.840 16.118  -4.627  1.00 36.32 ? 15  ALA A N   1 
ATOM   110  C  CA  . ALA A  1 14  ? 46.142 16.673  -3.467  1.00 37.91 ? 15  ALA A CA  1 
ATOM   111  C  C   . ALA A  1 14  ? 46.959 17.776  -2.810  1.00 36.59 ? 15  ALA A C   1 
ATOM   112  O  O   . ALA A  1 14  ? 46.405 18.789  -2.369  1.00 39.05 ? 15  ALA A O   1 
ATOM   113  C  CB  . ALA A  1 14  ? 45.817 15.569  -2.455  1.00 33.10 ? 15  ALA A CB  1 
ATOM   114  N  N   . SER A  1 15  ? 48.282 17.617  -2.762  1.00 35.53 ? 16  SER A N   1 
ATOM   115  C  CA  . SER A  1 15  ? 49.120 18.649  -2.161  1.00 39.51 ? 16  SER A CA  1 
ATOM   116  C  C   . SER A  1 15  ? 49.067 19.949  -2.959  1.00 36.28 ? 16  SER A C   1 
ATOM   117  O  O   . SER A  1 15  ? 49.092 21.038  -2.374  1.00 39.35 ? 16  SER A O   1 
ATOM   118  C  CB  . SER A  1 15  ? 50.564 18.156  -2.034  1.00 43.25 ? 16  SER A CB  1 
ATOM   119  O  OG  . SER A  1 15  ? 50.738 17.390  -0.857  1.00 52.17 ? 16  SER A OG  1 
ATOM   120  N  N   . ILE A  1 16  ? 49.019 19.860  -4.291  1.00 38.44 ? 17  ILE A N   1 
ATOM   121  C  CA  . ILE A  1 16  ? 48.867 21.069  -5.095  1.00 34.07 ? 17  ILE A CA  1 
ATOM   122  C  C   . ILE A  1 16  ? 47.567 21.774  -4.726  1.00 32.99 ? 17  ILE A C   1 
ATOM   123  O  O   . ILE A  1 16  ? 47.540 22.995  -4.544  1.00 35.30 ? 17  ILE A O   1 
ATOM   124  C  CB  . ILE A  1 16  ? 48.931 20.741  -6.604  1.00 33.60 ? 17  ILE A CB  1 
ATOM   125  C  CG1 . ILE A  1 16  ? 50.266 20.085  -7.002  1.00 37.86 ? 17  ILE A CG1 1 
ATOM   126  C  CG2 . ILE A  1 16  ? 48.669 22.005  -7.467  1.00 28.33 ? 17  ILE A CG2 1 
ATOM   127  C  CD1 . ILE A  1 16  ? 51.474 20.947  -6.823  1.00 36.08 ? 17  ILE A CD1 1 
ATOM   128  N  N   . ASN A  1 17  ? 46.472 21.017  -4.583  1.00 30.53 ? 18  ASN A N   1 
ATOM   129  C  CA  . ASN A  1 17  ? 45.191 21.648  -4.265  1.00 31.53 ? 18  ASN A CA  1 
ATOM   130  C  C   . ASN A  1 17  ? 45.227 22.332  -2.902  1.00 33.21 ? 18  ASN A C   1 
ATOM   131  O  O   . ASN A  1 17  ? 44.663 23.422  -2.742  1.00 34.01 ? 18  ASN A O   1 
ATOM   132  C  CB  . ASN A  1 17  ? 44.055 20.628  -4.341  1.00 29.60 ? 18  ASN A CB  1 
ATOM   133  C  CG  . ASN A  1 17  ? 43.650 20.334  -5.777  1.00 36.58 ? 18  ASN A CG  1 
ATOM   134  O  OD1 . ASN A  1 17  ? 43.762 21.199  -6.649  1.00 31.91 ? 18  ASN A OD1 1 
ATOM   135  N  ND2 . ASN A  1 17  ? 43.203 19.109  -6.038  1.00 35.23 ? 18  ASN A ND2 1 
ATOM   136  N  N   . LYS A  1 18  ? 45.921 21.745  -1.913  1.00 29.62 ? 19  LYS A N   1 
ATOM   137  C  CA  . LYS A  1 18  ? 46.064 22.468  -0.645  1.00 33.52 ? 19  LYS A CA  1 
ATOM   138  C  C   . LYS A  1 18  ? 46.954 23.697  -0.804  1.00 32.99 ? 19  LYS A C   1 
ATOM   139  O  O   . LYS A  1 18  ? 46.695 24.734  -0.189  1.00 31.42 ? 19  LYS A O   1 
ATOM   140  C  CB  . LYS A  1 18  ? 46.616 21.587  0.488   1.00 34.87 ? 19  LYS A CB  1 
ATOM   141  C  CG  . LYS A  1 18  ? 46.111 20.143  0.608   1.00 43.89 ? 19  LYS A CG  1 
ATOM   142  C  CD  . LYS A  1 18  ? 44.652 19.920  0.190   1.00 53.69 ? 19  LYS A CD  1 
ATOM   143  C  CE  . LYS A  1 18  ? 44.456 18.446  -0.251  1.00 50.86 ? 19  LYS A CE  1 
ATOM   144  N  NZ  . LYS A  1 18  ? 43.512 18.288  -1.398  1.00 44.84 ? 19  LYS A NZ  1 
ATOM   145  N  N   . GLN A  1 19  ? 48.014 23.606  -1.612  1.00 29.55 ? 20  GLN A N   1 
ATOM   146  C  CA  . GLN A  1 19  ? 48.868 24.772  -1.801  1.00 32.88 ? 20  GLN A CA  1 
ATOM   147  C  C   . GLN A  1 19  ? 48.110 25.902  -2.493  1.00 35.26 ? 20  GLN A C   1 
ATOM   148  O  O   . GLN A  1 19  ? 48.302 27.074  -2.160  1.00 30.81 ? 20  GLN A O   1 
ATOM   149  C  CB  . GLN A  1 19  ? 50.123 24.403  -2.591  1.00 38.18 ? 20  GLN A CB  1 
ATOM   150  C  CG  . GLN A  1 19  ? 51.342 25.289  -2.309  1.00 44.08 ? 20  GLN A CG  1 
ATOM   151  C  CD  . GLN A  1 19  ? 51.737 25.341  -0.842  1.00 46.52 ? 20  GLN A CD  1 
ATOM   152  O  OE1 . GLN A  1 19  ? 51.943 24.302  -0.209  1.00 42.18 ? 20  GLN A OE1 1 
ATOM   153  N  NE2 . GLN A  1 19  ? 51.866 26.556  -0.299  1.00 46.92 ? 20  GLN A NE2 1 
ATOM   154  N  N   . ILE A  1 20  ? 47.241 25.571  -3.454  1.00 30.67 ? 21  ILE A N   1 
ATOM   155  C  CA  . ILE A  1 20  ? 46.417 26.597  -4.093  1.00 30.73 ? 21  ILE A CA  1 
ATOM   156  C  C   . ILE A  1 20  ? 45.602 27.352  -3.050  1.00 33.29 ? 21  ILE A C   1 
ATOM   157  O  O   . ILE A  1 20  ? 45.533 28.584  -3.064  1.00 35.57 ? 21  ILE A O   1 
ATOM   158  C  CB  . ILE A  1 20  ? 45.504 25.969  -5.159  1.00 30.18 ? 21  ILE A CB  1 
ATOM   159  C  CG1 . ILE A  1 20  ? 46.306 25.619  -6.411  1.00 29.68 ? 21  ILE A CG1 1 
ATOM   160  C  CG2 . ILE A  1 20  ? 44.393 26.928  -5.523  1.00 27.69 ? 21  ILE A CG2 1 
ATOM   161  C  CD1 . ILE A  1 20  ? 45.659 24.538  -7.260  1.00 29.93 ? 21  ILE A CD1 1 
ATOM   162  N  N   . ASN A  1 21  ? 44.983 26.623  -2.119  1.00 32.05 ? 22  ASN A N   1 
ATOM   163  C  CA  . ASN A  1 21  ? 44.191 27.271  -1.085  1.00 28.87 ? 22  ASN A CA  1 
ATOM   164  C  C   . ASN A  1 21  ? 45.055 28.129  -0.174  1.00 31.09 ? 22  ASN A C   1 
ATOM   165  O  O   . ASN A  1 21  ? 44.667 29.242  0.192   1.00 30.32 ? 22  ASN A O   1 
ATOM   166  C  CB  . ASN A  1 21  ? 43.440 26.236  -0.258  1.00 30.92 ? 22  ASN A CB  1 
ATOM   167  C  CG  . ASN A  1 21  ? 42.382 26.869  0.612   1.00 35.30 ? 22  ASN A CG  1 
ATOM   168  O  OD1 . ASN A  1 21  ? 42.608 27.151  1.800   1.00 28.75 ? 22  ASN A OD1 1 
ATOM   169  N  ND2 . ASN A  1 21  ? 41.221 27.141  0.011   1.00 31.43 ? 22  ASN A ND2 1 
ATOM   170  N  N   . MET A  1 22  ? 46.230 27.635  0.198   1.00 30.77 ? 23  MET A N   1 
ATOM   171  C  CA  . MET A  1 22  ? 47.095 28.413  1.075   1.00 30.83 ? 23  MET A CA  1 
ATOM   172  C  C   . MET A  1 22  ? 47.479 29.746  0.444   1.00 32.25 ? 23  MET A C   1 
ATOM   173  O  O   . MET A  1 22  ? 47.520 30.774  1.125   1.00 26.71 ? 23  MET A O   1 
ATOM   174  C  CB  . MET A  1 22  ? 48.351 27.624  1.417   1.00 34.82 ? 23  MET A CB  1 
ATOM   175  C  CG  . MET A  1 22  ? 49.053 28.167  2.631   1.00 40.71 ? 23  MET A CG  1 
ATOM   176  S  SD  . MET A  1 22  ? 50.421 27.119  3.197   1.00 52.20 ? 23  MET A SD  1 
ATOM   177  C  CE  . MET A  1 22  ? 51.070 28.227  4.455   1.00 49.16 ? 23  MET A CE  1 
ATOM   178  N  N   . CYS A  1 23  ? 47.781 29.755  -0.854  1.00 27.83 ? 24  CYS A N   1 
ATOM   179  C  CA  . CYS A  1 23  ? 48.171 31.030  -1.440  1.00 32.23 ? 24  CYS A CA  1 
ATOM   180  C  C   . CYS A  1 23  ? 46.976 31.961  -1.637  1.00 31.54 ? 24  CYS A C   1 
ATOM   181  O  O   . CYS A  1 23  ? 47.120 33.175  -1.487  1.00 30.90 ? 24  CYS A O   1 
ATOM   182  C  CB  . CYS A  1 23  ? 48.935 30.786  -2.738  1.00 35.59 ? 24  CYS A CB  1 
ATOM   183  S  SG  . CYS A  1 23  ? 50.701 30.383  -2.356  1.00 52.68 ? 24  CYS A SG  1 
ATOM   184  N  N   . LEU A  1 24  ? 45.791 31.414  -1.926  1.00 31.34 ? 25  LEU A N   1 
ATOM   185  C  CA  . LEU A  1 24  ? 44.597 32.246  -1.960  1.00 31.08 ? 25  LEU A CA  1 
ATOM   186  C  C   . LEU A  1 24  ? 44.346 32.873  -0.598  1.00 30.39 ? 25  LEU A C   1 
ATOM   187  O  O   . LEU A  1 24  ? 44.028 34.062  -0.504  1.00 28.84 ? 25  LEU A O   1 
ATOM   188  C  CB  . LEU A  1 24  ? 43.393 31.418  -2.406  1.00 27.19 ? 25  LEU A CB  1 
ATOM   189  C  CG  . LEU A  1 24  ? 43.437 30.958  -3.865  1.00 31.66 ? 25  LEU A CG  1 
ATOM   190  C  CD1 . LEU A  1 24  ? 42.263 30.039  -4.152  1.00 32.70 ? 25  LEU A CD1 1 
ATOM   191  C  CD2 . LEU A  1 24  ? 43.449 32.147  -4.826  1.00 29.13 ? 25  LEU A CD2 1 
ATOM   192  N  N   . TYR A  1 25  ? 44.523 32.095  0.472   1.00 28.01 ? 26  TYR A N   1 
ATOM   193  C  CA  . TYR A  1 25  ? 44.336 32.631  1.810   1.00 28.40 ? 26  TYR A CA  1 
ATOM   194  C  C   . TYR A  1 25  ? 45.339 33.744  2.104   1.00 31.05 ? 26  TYR A C   1 
ATOM   195  O  O   . TYR A  1 25  ? 44.964 34.826  2.574   1.00 28.80 ? 26  TYR A O   1 
ATOM   196  C  CB  . TYR A  1 25  ? 44.443 31.512  2.846   1.00 29.94 ? 26  TYR A CB  1 
ATOM   197  C  CG  . TYR A  1 25  ? 44.446 32.050  4.262   1.00 31.52 ? 26  TYR A CG  1 
ATOM   198  C  CD1 . TYR A  1 25  ? 43.277 32.539  4.845   1.00 33.32 ? 26  TYR A CD1 1 
ATOM   199  C  CD2 . TYR A  1 25  ? 45.623 32.121  4.991   1.00 30.88 ? 26  TYR A CD2 1 
ATOM   200  C  CE1 . TYR A  1 25  ? 43.281 33.058  6.145   1.00 36.42 ? 26  TYR A CE1 1 
ATOM   201  C  CE2 . TYR A  1 25  ? 45.639 32.628  6.289   1.00 35.34 ? 26  TYR A CE2 1 
ATOM   202  C  CZ  . TYR A  1 25  ? 44.472 33.090  6.861   1.00 38.80 ? 26  TYR A CZ  1 
ATOM   203  O  OH  . TYR A  1 25  ? 44.507 33.598  8.135   1.00 39.71 ? 26  TYR A OH  1 
ATOM   204  N  N   . ALA A  1 26  ? 46.627 33.493  1.846   1.00 27.22 ? 27  ALA A N   1 
ATOM   205  C  CA  . ALA A  1 26  ? 47.636 34.536  2.031   1.00 29.76 ? 27  ALA A CA  1 
ATOM   206  C  C   . ALA A  1 26  ? 47.287 35.784  1.239   1.00 30.23 ? 27  ALA A C   1 
ATOM   207  O  O   . ALA A  1 26  ? 47.442 36.909  1.731   1.00 32.78 ? 27  ALA A O   1 
ATOM   208  C  CB  . ALA A  1 26  ? 49.016 34.025  1.619   1.00 29.78 ? 27  ALA A CB  1 
ATOM   209  N  N   . SER A  1 27  ? 46.799 35.607  0.011   1.00 29.09 ? 28  SER A N   1 
ATOM   210  C  CA  . SER A  1 27  ? 46.373 36.754  -0.783  1.00 31.62 ? 28  SER A CA  1 
ATOM   211  C  C   . SER A  1 27  ? 45.267 37.536  -0.079  1.00 30.37 ? 28  SER A C   1 
ATOM   212  O  O   . SER A  1 27  ? 45.309 38.769  -0.012  1.00 28.63 ? 28  SER A O   1 
ATOM   213  C  CB  . SER A  1 27  ? 45.909 36.290  -2.157  1.00 29.77 ? 28  SER A CB  1 
ATOM   214  O  OG  . SER A  1 27  ? 45.404 37.395  -2.864  1.00 36.31 ? 28  SER A OG  1 
ATOM   215  N  N   . TYR A  1 28  ? 44.265 36.825  0.448   1.00 29.38 ? 29  TYR A N   1 
ATOM   216  C  CA  . TYR A  1 28  ? 43.185 37.460  1.205   1.00 31.71 ? 29  TYR A CA  1 
ATOM   217  C  C   . TYR A  1 28  ? 43.727 38.231  2.402   1.00 29.75 ? 29  TYR A C   1 
ATOM   218  O  O   . TYR A  1 28  ? 43.302 39.361  2.668   1.00 30.20 ? 29  TYR A O   1 
ATOM   219  C  CB  . TYR A  1 28  ? 42.190 36.394  1.676   1.00 29.91 ? 29  TYR A CB  1 
ATOM   220  C  CG  . TYR A  1 28  ? 40.744 36.834  1.823   1.00 31.36 ? 29  TYR A CG  1 
ATOM   221  C  CD1 . TYR A  1 28  ? 40.276 38.019  1.261   1.00 29.26 ? 29  TYR A CD1 1 
ATOM   222  C  CD2 . TYR A  1 28  ? 39.839 36.041  2.533   1.00 29.46 ? 29  TYR A CD2 1 
ATOM   223  C  CE1 . TYR A  1 28  ? 38.926 38.393  1.393   1.00 25.82 ? 29  TYR A CE1 1 
ATOM   224  C  CE2 . TYR A  1 28  ? 38.497 36.393  2.662   1.00 27.96 ? 29  TYR A CE2 1 
ATOM   225  C  CZ  . TYR A  1 28  ? 38.042 37.565  2.093   1.00 29.13 ? 29  TYR A CZ  1 
ATOM   226  O  OH  . TYR A  1 28  ? 36.709 37.902  2.253   1.00 24.21 ? 29  TYR A OH  1 
ATOM   227  N  N   . VAL A  1 29  ? 44.640 37.615  3.153   1.00 26.61 ? 30  VAL A N   1 
ATOM   228  C  CA  . VAL A  1 29  ? 45.239 38.266  4.313   1.00 30.79 ? 30  VAL A CA  1 
ATOM   229  C  C   . VAL A  1 29  ? 45.935 39.562  3.903   1.00 35.00 ? 30  VAL A C   1 
ATOM   230  O  O   . VAL A  1 29  ? 45.829 40.587  4.588   1.00 34.40 ? 30  VAL A O   1 
ATOM   231  C  CB  . VAL A  1 29  ? 46.220 37.298  4.999   1.00 32.13 ? 30  VAL A CB  1 
ATOM   232  C  CG1 . VAL A  1 29  ? 47.160 38.068  5.918   1.00 32.48 ? 30  VAL A CG1 1 
ATOM   233  C  CG2 . VAL A  1 29  ? 45.464 36.206  5.752   1.00 31.15 ? 30  VAL A CG2 1 
ATOM   234  N  N   . TYR A  1 30  ? 46.669 39.530  2.785   1.00 31.57 ? 31  TYR A N   1 
ATOM   235  C  CA  . TYR A  1 30  ? 47.347 40.730  2.309   1.00 31.83 ? 31  TYR A CA  1 
ATOM   236  C  C   . TYR A  1 30  ? 46.353 41.788  1.860   1.00 32.17 ? 31  TYR A C   1 
ATOM   237  O  O   . TYR A  1 30  ? 46.579 42.983  2.079   1.00 33.52 ? 31  TYR A O   1 
ATOM   238  C  CB  . TYR A  1 30  ? 48.293 40.375  1.166   1.00 33.99 ? 31  TYR A CB  1 
ATOM   239  C  CG  . TYR A  1 30  ? 49.558 39.739  1.649   1.00 33.88 ? 31  TYR A CG  1 
ATOM   240  C  CD1 . TYR A  1 30  ? 50.279 40.311  2.681   1.00 35.07 ? 31  TYR A CD1 1 
ATOM   241  C  CD2 . TYR A  1 30  ? 50.021 38.554  1.101   1.00 34.99 ? 31  TYR A CD2 1 
ATOM   242  C  CE1 . TYR A  1 30  ? 51.430 39.739  3.148   1.00 41.99 ? 31  TYR A CE1 1 
ATOM   243  C  CE2 . TYR A  1 30  ? 51.189 37.964  1.565   1.00 36.17 ? 31  TYR A CE2 1 
ATOM   244  C  CZ  . TYR A  1 30  ? 51.885 38.566  2.589   1.00 43.03 ? 31  TYR A CZ  1 
ATOM   245  O  OH  . TYR A  1 30  ? 53.045 38.015  3.073   1.00 50.68 ? 31  TYR A OH  1 
ATOM   246  N  N   . LEU A  1 31  ? 45.260 41.369  1.213   1.00 29.77 ? 32  LEU A N   1 
ATOM   247  C  CA  . LEU A  1 31  ? 44.227 42.318  0.805   1.00 31.03 ? 32  LEU A CA  1 
ATOM   248  C  C   . LEU A  1 31  ? 43.618 43.002  2.014   1.00 31.10 ? 32  LEU A C   1 
ATOM   249  O  O   . LEU A  1 31  ? 43.348 44.208  1.990   1.00 33.79 ? 32  LEU A O   1 
ATOM   250  C  CB  . LEU A  1 31  ? 43.138 41.611  0.000   1.00 31.00 ? 32  LEU A CB  1 
ATOM   251  C  CG  . LEU A  1 31  ? 42.079 42.518  -0.635  1.00 35.08 ? 32  LEU A CG  1 
ATOM   252  C  CD1 . LEU A  1 31  ? 42.620 43.210  -1.881  1.00 35.85 ? 32  LEU A CD1 1 
ATOM   253  C  CD2 . LEU A  1 31  ? 40.823 41.726  -0.976  1.00 40.20 ? 32  LEU A CD2 1 
ATOM   254  N  N   . SER A  1 32  ? 43.400 42.242  3.084   1.00 32.90 ? 33  SER A N   1 
ATOM   255  C  CA  . SER A  1 32  ? 42.880 42.822  4.309   1.00 32.79 ? 33  SER A CA  1 
ATOM   256  C  C   . SER A  1 32  ? 43.837 43.867  4.862   1.00 33.48 ? 33  SER A C   1 
ATOM   257  O  O   . SER A  1 32  ? 43.419 44.971  5.217   1.00 32.05 ? 33  SER A O   1 
ATOM   258  C  CB  . SER A  1 32  ? 42.630 41.727  5.335   1.00 28.86 ? 33  SER A CB  1 
ATOM   259  O  OG  . SER A  1 32  ? 42.221 42.317  6.545   1.00 36.48 ? 33  SER A OG  1 
ATOM   260  N  N   . MET A  1 33  ? 45.133 43.535  4.927   1.00 33.30 ? 34  MET A N   1 
ATOM   261  C  CA  . MET A  1 33  ? 46.142 44.499  5.368   1.00 34.24 ? 34  MET A CA  1 
ATOM   262  C  C   . MET A  1 33  ? 46.143 45.742  4.496   1.00 32.97 ? 34  MET A C   1 
ATOM   263  O  O   . MET A  1 33  ? 46.212 46.865  5.009   1.00 33.99 ? 34  MET A O   1 
ATOM   264  C  CB  . MET A  1 33  ? 47.533 43.865  5.344   1.00 33.82 ? 34  MET A CB  1 
ATOM   265  C  CG  . MET A  1 33  ? 47.815 42.892  6.480   1.00 36.74 ? 34  MET A CG  1 
ATOM   266  S  SD  . MET A  1 33  ? 49.513 42.240  6.380   1.00 43.74 ? 34  MET A SD  1 
ATOM   267  C  CE  . MET A  1 33  ? 49.472 40.887  7.566   1.00 40.71 ? 34  MET A CE  1 
ATOM   268  N  N   . ALA A  1 34  ? 46.061 45.564  3.171   1.00 31.54 ? 35  ALA A N   1 
ATOM   269  C  CA  . ALA A  1 34  ? 46.194 46.701  2.265   1.00 31.32 ? 35  ALA A CA  1 
ATOM   270  C  C   . ALA A  1 34  ? 45.129 47.754  2.529   1.00 33.54 ? 35  ALA A C   1 
ATOM   271  O  O   . ALA A  1 34  ? 45.429 48.952  2.548   1.00 36.56 ? 35  ALA A O   1 
ATOM   272  C  CB  . ALA A  1 34  ? 46.121 46.237  0.813   1.00 32.29 ? 35  ALA A CB  1 
ATOM   273  N  N   . TYR A  1 35  ? 43.877 47.330  2.727   1.00 31.37 ? 36  TYR A N   1 
ATOM   274  C  CA  . TYR A  1 35  ? 42.793 48.290  2.921   1.00 34.62 ? 36  TYR A CA  1 
ATOM   275  C  C   . TYR A  1 35  ? 42.708 48.784  4.352   1.00 34.67 ? 36  TYR A C   1 
ATOM   276  O  O   . TYR A  1 35  ? 42.136 49.847  4.592   1.00 35.40 ? 36  TYR A O   1 
ATOM   277  C  CB  . TYR A  1 35  ? 41.457 47.689  2.478   1.00 30.88 ? 36  TYR A CB  1 
ATOM   278  C  CG  . TYR A  1 35  ? 41.360 47.759  0.981   1.00 35.89 ? 36  TYR A CG  1 
ATOM   279  C  CD1 . TYR A  1 35  ? 41.853 46.736  0.188   1.00 34.99 ? 36  TYR A CD1 1 
ATOM   280  C  CD2 . TYR A  1 35  ? 40.876 48.902  0.356   1.00 37.56 ? 36  TYR A CD2 1 
ATOM   281  C  CE1 . TYR A  1 35  ? 41.807 46.816  -1.181  1.00 40.32 ? 36  TYR A CE1 1 
ATOM   282  C  CE2 . TYR A  1 35  ? 40.832 49.001  -1.014  1.00 40.58 ? 36  TYR A CE2 1 
ATOM   283  C  CZ  . TYR A  1 35  ? 41.299 47.955  -1.783  1.00 43.72 ? 36  TYR A CZ  1 
ATOM   284  O  OH  . TYR A  1 35  ? 41.251 48.039  -3.156  1.00 45.91 ? 36  TYR A OH  1 
ATOM   285  N  N   . TYR A  1 36  ? 43.267 48.043  5.303   1.00 32.04 ? 37  TYR A N   1 
ATOM   286  C  CA  . TYR A  1 36  ? 43.420 48.579  6.644   1.00 30.82 ? 37  TYR A CA  1 
ATOM   287  C  C   . TYR A  1 36  ? 44.320 49.818  6.626   1.00 35.18 ? 37  TYR A C   1 
ATOM   288  O  O   . TYR A  1 36  ? 43.953 50.875  7.152   1.00 28.23 ? 37  TYR A O   1 
ATOM   289  C  CB  . TYR A  1 36  ? 43.970 47.491  7.561   1.00 31.69 ? 37  TYR A CB  1 
ATOM   290  C  CG  . TYR A  1 36  ? 44.319 47.988  8.930   1.00 34.91 ? 37  TYR A CG  1 
ATOM   291  C  CD1 . TYR A  1 36  ? 43.330 48.196  9.889   1.00 36.19 ? 37  TYR A CD1 1 
ATOM   292  C  CD2 . TYR A  1 36  ? 45.634 48.252  9.271   1.00 33.95 ? 37  TYR A CD2 1 
ATOM   293  C  CE1 . TYR A  1 36  ? 43.649 48.664  11.155  1.00 37.39 ? 37  TYR A CE1 1 
ATOM   294  C  CE2 . TYR A  1 36  ? 45.962 48.720  10.531  1.00 38.01 ? 37  TYR A CE2 1 
ATOM   295  C  CZ  . TYR A  1 36  ? 44.966 48.924  11.465  1.00 39.31 ? 37  TYR A CZ  1 
ATOM   296  O  OH  . TYR A  1 36  ? 45.296 49.381  12.708  1.00 45.39 ? 37  TYR A OH  1 
ATOM   297  N  N   . PHE A  1 37  ? 45.482 49.725  5.970   1.00 31.29 ? 38  PHE A N   1 
ATOM   298  C  CA  . PHE A  1 37  ? 46.430 50.837  5.949   1.00 33.17 ? 38  PHE A CA  1 
ATOM   299  C  C   . PHE A  1 37  ? 45.962 52.016  5.105   1.00 33.01 ? 38  PHE A C   1 
ATOM   300  O  O   . PHE A  1 37  ? 46.616 53.062  5.128   1.00 33.77 ? 38  PHE A O   1 
ATOM   301  C  CB  . PHE A  1 37  ? 47.798 50.341  5.474   1.00 31.17 ? 38  PHE A CB  1 
ATOM   302  C  CG  . PHE A  1 37  ? 48.488 49.517  6.502   1.00 35.24 ? 38  PHE A CG  1 
ATOM   303  C  CD1 . PHE A  1 37  ? 48.943 50.102  7.673   1.00 33.61 ? 38  PHE A CD1 1 
ATOM   304  C  CD2 . PHE A  1 37  ? 48.604 48.145  6.351   1.00 35.94 ? 38  PHE A CD2 1 
ATOM   305  C  CE1 . PHE A  1 37  ? 49.549 49.345  8.653   1.00 37.06 ? 38  PHE A CE1 1 
ATOM   306  C  CE2 . PHE A  1 37  ? 49.210 47.379  7.330   1.00 32.87 ? 38  PHE A CE2 1 
ATOM   307  C  CZ  . PHE A  1 37  ? 49.690 47.984  8.480   1.00 35.62 ? 38  PHE A CZ  1 
ATOM   308  N  N   . GLU A  1 38  ? 44.849 51.886  4.387   1.00 34.53 ? 39  GLU A N   1 
ATOM   309  C  CA  . GLU A  1 38  ? 44.210 53.002  3.700   1.00 35.77 ? 39  GLU A CA  1 
ATOM   310  C  C   . GLU A  1 38  ? 43.058 53.613  4.501   1.00 35.22 ? 39  GLU A C   1 
ATOM   311  O  O   . GLU A  1 38  ? 42.391 54.525  4.004   1.00 35.06 ? 39  GLU A O   1 
ATOM   312  C  CB  . GLU A  1 38  ? 43.693 52.541  2.340   1.00 35.53 ? 39  GLU A CB  1 
ATOM   313  C  CG  . GLU A  1 38  ? 44.593 52.872  1.189   1.00 44.89 ? 39  GLU A CG  1 
ATOM   314  C  CD  . GLU A  1 38  ? 44.055 52.350  -0.148  1.00 62.10 ? 39  GLU A CD  1 
ATOM   315  O  OE1 . GLU A  1 38  ? 44.870 51.901  -0.988  1.00 71.67 ? 39  GLU A OE1 1 
ATOM   316  O  OE2 . GLU A  1 38  ? 42.818 52.380  -0.363  1.00 60.86 ? 39  GLU A OE2 1 
ATOM   317  N  N   . ARG A  1 39  ? 42.781 53.107  5.703   1.00 34.82 ? 40  ARG A N   1 
ATOM   318  C  CA  . ARG A  1 39  ? 41.801 53.736  6.583   1.00 37.00 ? 40  ARG A CA  1 
ATOM   319  C  C   . ARG A  1 39  ? 42.219 55.171  6.895   1.00 35.78 ? 40  ARG A C   1 
ATOM   320  O  O   . ARG A  1 39  ? 43.407 55.476  7.009   1.00 31.69 ? 40  ARG A O   1 
ATOM   321  C  CB  . ARG A  1 39  ? 41.668 52.935  7.877   1.00 32.09 ? 40  ARG A CB  1 
ATOM   322  C  CG  . ARG A  1 39  ? 40.870 51.645  7.718   1.00 33.15 ? 40  ARG A CG  1 
ATOM   323  C  CD  . ARG A  1 39  ? 40.673 50.917  9.063   1.00 41.25 ? 40  ARG A CD  1 
ATOM   324  N  NE  . ARG A  1 39  ? 40.051 51.761  10.081  1.00 45.83 ? 40  ARG A NE  1 
ATOM   325  C  CZ  . ARG A  1 39  ? 38.738 51.877  10.268  1.00 55.39 ? 40  ARG A CZ  1 
ATOM   326  N  NH1 . ARG A  1 39  ? 37.861 51.229  9.506   1.00 46.73 ? 40  ARG A NH1 1 
ATOM   327  N  NH2 . ARG A  1 39  ? 38.288 52.672  11.238  1.00 49.98 ? 40  ARG A NH2 1 
ATOM   328  N  N   . ASP A  1 40  ? 41.226 56.063  7.033   1.00 34.96 ? 41  ASP A N   1 
ATOM   329  C  CA  . ASP A  1 40  ? 41.537 57.473  7.273   1.00 36.01 ? 41  ASP A CA  1 
ATOM   330  C  C   . ASP A  1 40  ? 42.236 57.679  8.609   1.00 35.87 ? 41  ASP A C   1 
ATOM   331  O  O   . ASP A  1 40  ? 43.026 58.620  8.743   1.00 38.78 ? 41  ASP A O   1 
ATOM   332  C  CB  . ASP A  1 40  ? 40.272 58.335  7.201   1.00 37.99 ? 41  ASP A CB  1 
ATOM   333  C  CG  . ASP A  1 40  ? 39.409 58.225  8.465   1.00 45.95 ? 41  ASP A CG  1 
ATOM   334  O  OD1 . ASP A  1 40  ? 39.695 58.926  9.475   1.00 42.72 ? 41  ASP A OD1 1 
ATOM   335  O  OD2 . ASP A  1 40  ? 38.439 57.423  8.444   1.00 49.19 ? 41  ASP A OD2 1 
ATOM   336  N  N   . ASP A  1 41  ? 41.979 56.811  9.595   1.00 33.07 ? 42  ASP A N   1 
ATOM   337  C  CA  . ASP A  1 41  ? 42.634 56.881  10.897  1.00 32.84 ? 42  ASP A CA  1 
ATOM   338  C  C   . ASP A  1 41  ? 43.917 56.054  10.968  1.00 35.78 ? 42  ASP A C   1 
ATOM   339  O  O   . ASP A  1 41  ? 44.483 55.912  12.058  1.00 34.27 ? 42  ASP A O   1 
ATOM   340  C  CB  . ASP A  1 41  ? 41.654 56.460  12.001  1.00 34.92 ? 42  ASP A CB  1 
ATOM   341  C  CG  . ASP A  1 41  ? 41.105 55.039  11.810  1.00 44.37 ? 42  ASP A CG  1 
ATOM   342  O  OD1 . ASP A  1 41  ? 41.265 54.455  10.712  1.00 42.85 ? 42  ASP A OD1 1 
ATOM   343  O  OD2 . ASP A  1 41  ? 40.451 54.527  12.746  1.00 45.46 ? 42  ASP A OD2 1 
ATOM   344  N  N   . VAL A  1 42  ? 44.399 55.532  9.834   1.00 33.09 ? 43  VAL A N   1 
ATOM   345  C  CA  . VAL A  1 42  ? 45.692 54.852  9.754   1.00 33.29 ? 43  VAL A CA  1 
ATOM   346  C  C   . VAL A  1 42  ? 46.597 55.589  8.769   1.00 30.14 ? 43  VAL A C   1 
ATOM   347  O  O   . VAL A  1 42  ? 47.650 56.099  9.152   1.00 33.97 ? 43  VAL A O   1 
ATOM   348  C  CB  . VAL A  1 42  ? 45.518 53.373  9.352   1.00 29.86 ? 43  VAL A CB  1 
ATOM   349  C  CG1 . VAL A  1 42  ? 46.874 52.692  9.155   1.00 32.41 ? 43  VAL A CG1 1 
ATOM   350  C  CG2 . VAL A  1 42  ? 44.717 52.651  10.399  1.00 32.69 ? 43  VAL A CG2 1 
ATOM   351  N  N   . ALA A  1 43  ? 46.197 55.624  7.493   1.00 34.26 ? 44  ALA A N   1 
ATOM   352  C  CA  . ALA A  1 43  ? 46.796 56.473  6.451   1.00 32.78 ? 44  ALA A CA  1 
ATOM   353  C  C   . ALA A  1 43  ? 48.299 56.228  6.303   1.00 34.10 ? 44  ALA A C   1 
ATOM   354  O  O   . ALA A  1 43  ? 49.132 57.109  6.512   1.00 36.62 ? 44  ALA A O   1 
ATOM   355  C  CB  . ALA A  1 43  ? 46.509 57.953  6.722   1.00 31.55 ? 44  ALA A CB  1 
ATOM   356  N  N   . LEU A  1 44  ? 48.638 55.001  5.930   1.00 35.07 ? 45  LEU A N   1 
ATOM   357  C  CA  . LEU A  1 44  ? 50.014 54.612  5.645   1.00 34.29 ? 45  LEU A CA  1 
ATOM   358  C  C   . LEU A  1 44  ? 50.024 54.103  4.211   1.00 35.65 ? 45  LEU A C   1 
ATOM   359  O  O   . LEU A  1 44  ? 50.021 52.887  3.978   1.00 37.04 ? 45  LEU A O   1 
ATOM   360  C  CB  . LEU A  1 44  ? 50.518 53.560  6.629   1.00 30.70 ? 45  LEU A CB  1 
ATOM   361  C  CG  . LEU A  1 44  ? 50.844 54.099  8.026   1.00 36.88 ? 45  LEU A CG  1 
ATOM   362  C  CD1 . LEU A  1 44  ? 50.903 52.982  9.075   1.00 37.23 ? 45  LEU A CD1 1 
ATOM   363  C  CD2 . LEU A  1 44  ? 52.160 54.881  8.007   1.00 36.41 ? 45  LEU A CD2 1 
ATOM   364  N  N   . PRO A  1 45  ? 49.998 55.005  3.227   1.00 35.75 ? 46  PRO A N   1 
ATOM   365  C  CA  . PRO A  1 45  ? 49.906 54.559  1.823   1.00 35.74 ? 46  PRO A CA  1 
ATOM   366  C  C   . PRO A  1 45  ? 51.061 53.678  1.370   1.00 40.71 ? 46  PRO A C   1 
ATOM   367  O  O   . PRO A  1 45  ? 50.848 52.795  0.526   1.00 41.18 ? 46  PRO A O   1 
ATOM   368  C  CB  . PRO A  1 45  ? 49.869 55.880  1.038   1.00 40.29 ? 46  PRO A CB  1 
ATOM   369  C  CG  . PRO A  1 45  ? 50.457 56.914  1.993   1.00 38.25 ? 46  PRO A CG  1 
ATOM   370  C  CD  . PRO A  1 45  ? 50.002 56.472  3.347   1.00 35.65 ? 46  PRO A CD  1 
ATOM   371  N  N   . GLY A  1 46  ? 52.279 53.890  1.882   1.00 33.64 ? 47  GLY A N   1 
ATOM   372  C  CA  . GLY A  1 46  ? 53.377 53.003  1.523   1.00 39.87 ? 47  GLY A CA  1 
ATOM   373  C  C   . GLY A  1 46  ? 53.122 51.566  1.946   1.00 35.83 ? 47  GLY A C   1 
ATOM   374  O  O   . GLY A  1 46  ? 53.285 50.627  1.163   1.00 32.55 ? 47  GLY A O   1 
ATOM   375  N  N   . PHE A  1 47  ? 52.703 51.377  3.192   1.00 32.70 ? 48  PHE A N   1 
ATOM   376  C  CA  . PHE A  1 47  ? 52.339 50.044  3.637   1.00 35.45 ? 48  PHE A CA  1 
ATOM   377  C  C   . PHE A  1 47  ? 51.185 49.491  2.819   1.00 36.10 ? 48  PHE A C   1 
ATOM   378  O  O   . PHE A  1 47  ? 51.186 48.311  2.460   1.00 35.17 ? 48  PHE A O   1 
ATOM   379  C  CB  . PHE A  1 47  ? 52.005 50.074  5.123   1.00 33.16 ? 48  PHE A CB  1 
ATOM   380  C  CG  . PHE A  1 47  ? 53.224 50.127  5.985   1.00 37.77 ? 48  PHE A CG  1 
ATOM   381  C  CD1 . PHE A  1 47  ? 54.009 48.995  6.158   1.00 35.81 ? 48  PHE A CD1 1 
ATOM   382  C  CD2 . PHE A  1 47  ? 53.619 51.312  6.580   1.00 37.75 ? 48  PHE A CD2 1 
ATOM   383  C  CE1 . PHE A  1 47  ? 55.150 49.042  6.941   1.00 39.53 ? 48  PHE A CE1 1 
ATOM   384  C  CE2 . PHE A  1 47  ? 54.758 51.364  7.371   1.00 39.46 ? 48  PHE A CE2 1 
ATOM   385  C  CZ  . PHE A  1 47  ? 55.522 50.235  7.551   1.00 39.75 ? 48  PHE A CZ  1 
ATOM   386  N  N   . ALA A  1 48  ? 50.216 50.335  2.471   1.00 30.76 ? 49  ALA A N   1 
ATOM   387  C  CA  . ALA A  1 48  ? 49.057 49.838  1.737   1.00 33.43 ? 49  ALA A CA  1 
ATOM   388  C  C   . ALA A  1 48  ? 49.469 49.302  0.372   1.00 35.45 ? 49  ALA A C   1 
ATOM   389  O  O   . ALA A  1 48  ? 49.051 48.208  -0.030  1.00 34.77 ? 49  ALA A O   1 
ATOM   390  C  CB  . ALA A  1 48  ? 47.997 50.937  1.598   1.00 32.67 ? 49  ALA A CB  1 
ATOM   391  N  N   . LYS A  1 49  ? 50.304 50.057  -0.349  1.00 33.76 ? 50  LYS A N   1 
ATOM   392  C  CA  . LYS A  1 49  ? 50.765 49.620  -1.662  1.00 35.17 ? 50  LYS A CA  1 
ATOM   393  C  C   . LYS A  1 49  ? 51.639 48.366  -1.563  1.00 35.62 ? 50  LYS A C   1 
ATOM   394  O  O   . LYS A  1 49  ? 51.544 47.466  -2.406  1.00 32.80 ? 50  LYS A O   1 
ATOM   395  C  CB  . LYS A  1 49  ? 51.510 50.766  -2.351  1.00 39.27 ? 50  LYS A CB  1 
ATOM   396  C  CG  . LYS A  1 49  ? 51.975 50.452  -3.773  1.00 49.71 ? 50  LYS A CG  1 
ATOM   397  C  CD  . LYS A  1 49  ? 52.870 51.545  -4.359  1.00 53.43 ? 50  LYS A CD  1 
ATOM   398  C  CE  . LYS A  1 49  ? 54.009 51.968  -3.421  1.00 62.20 ? 50  LYS A CE  1 
ATOM   399  N  NZ  . LYS A  1 49  ? 54.645 50.870  -2.599  1.00 61.24 ? 50  LYS A NZ  1 
ATOM   400  N  N   . PHE A  1 50  ? 52.466 48.265  -0.524  1.00 34.72 ? 51  PHE A N   1 
ATOM   401  C  CA  . PHE A  1 50  ? 53.316 47.087  -0.393  1.00 34.61 ? 51  PHE A CA  1 
ATOM   402  C  C   . PHE A  1 50  ? 52.478 45.824  -0.208  1.00 35.54 ? 51  PHE A C   1 
ATOM   403  O  O   . PHE A  1 50  ? 52.740 44.797  -0.842  1.00 31.98 ? 51  PHE A O   1 
ATOM   404  C  CB  . PHE A  1 50  ? 54.284 47.268  0.772   1.00 34.34 ? 51  PHE A CB  1 
ATOM   405  C  CG  . PHE A  1 50  ? 55.089 46.046  1.077   1.00 39.42 ? 51  PHE A CG  1 
ATOM   406  C  CD1 . PHE A  1 50  ? 56.180 45.703  0.283   1.00 38.59 ? 51  PHE A CD1 1 
ATOM   407  C  CD2 . PHE A  1 50  ? 54.760 45.229  2.157   1.00 35.03 ? 51  PHE A CD2 1 
ATOM   408  C  CE1 . PHE A  1 50  ? 56.926 44.555  0.555   1.00 39.19 ? 51  PHE A CE1 1 
ATOM   409  C  CE2 . PHE A  1 50  ? 55.493 44.083  2.435   1.00 34.13 ? 51  PHE A CE2 1 
ATOM   410  C  CZ  . PHE A  1 50  ? 56.581 43.745  1.638   1.00 36.84 ? 51  PHE A CZ  1 
ATOM   411  N  N   . PHE A  1 51  ? 51.448 45.886  0.641   1.00 31.93 ? 52  PHE A N   1 
ATOM   412  C  CA  . PHE A  1 51  ? 50.625 44.706  0.888   1.00 34.31 ? 52  PHE A CA  1 
ATOM   413  C  C   . PHE A  1 51  ? 49.677 44.407  -0.268  1.00 35.59 ? 52  PHE A C   1 
ATOM   414  O  O   . PHE A  1 51  ? 49.350 43.242  -0.505  1.00 33.40 ? 52  PHE A O   1 
ATOM   415  C  CB  . PHE A  1 51  ? 49.852 44.877  2.195   1.00 31.38 ? 52  PHE A CB  1 
ATOM   416  C  CG  . PHE A  1 51  ? 50.729 44.805  3.410   1.00 33.09 ? 52  PHE A CG  1 
ATOM   417  C  CD1 . PHE A  1 51  ? 51.503 43.688  3.643   1.00 32.37 ? 52  PHE A CD1 1 
ATOM   418  C  CD2 . PHE A  1 51  ? 50.793 45.858  4.304   1.00 35.31 ? 52  PHE A CD2 1 
ATOM   419  C  CE1 . PHE A  1 51  ? 52.325 43.611  4.747   1.00 34.37 ? 52  PHE A CE1 1 
ATOM   420  C  CE2 . PHE A  1 51  ? 51.612 45.792  5.406   1.00 36.24 ? 52  PHE A CE2 1 
ATOM   421  C  CZ  . PHE A  1 51  ? 52.381 44.664  5.629   1.00 34.58 ? 52  PHE A CZ  1 
ATOM   422  N  N   . LYS A  1 52  ? 49.222 45.432  -0.993  1.00 33.51 ? 53  LYS A N   1 
ATOM   423  C  CA  . LYS A  1 52  ? 48.415 45.171  -2.175  1.00 34.36 ? 53  LYS A CA  1 
ATOM   424  C  C   . LYS A  1 52  ? 49.231 44.446  -3.236  1.00 37.83 ? 53  LYS A C   1 
ATOM   425  O  O   . LYS A  1 52  ? 48.713 43.550  -3.914  1.00 37.10 ? 53  LYS A O   1 
ATOM   426  C  CB  . LYS A  1 52  ? 47.837 46.474  -2.733  1.00 36.09 ? 53  LYS A CB  1 
ATOM   427  C  CG  . LYS A  1 52  ? 46.854 46.250  -3.865  1.00 40.89 ? 53  LYS A CG  1 
ATOM   428  C  CD  . LYS A  1 52  ? 45.568 47.053  -3.664  1.00 58.50 ? 53  LYS A CD  1 
ATOM   429  C  CE  . LYS A  1 52  ? 45.787 48.556  -3.922  1.00 63.30 ? 53  LYS A CE  1 
ATOM   430  N  NZ  . LYS A  1 52  ? 44.616 49.423  -3.558  1.00 55.78 ? 53  LYS A NZ  1 
ATOM   431  N  N   . GLU A  1 53  ? 50.512 44.815  -3.389  1.00 34.87 ? 54  GLU A N   1 
ATOM   432  C  CA  . GLU A  1 53  ? 51.391 44.083  -4.298  1.00 36.49 ? 54  GLU A CA  1 
ATOM   433  C  C   . GLU A  1 53  ? 51.555 42.638  -3.845  1.00 35.66 ? 54  GLU A C   1 
ATOM   434  O  O   . GLU A  1 53  ? 51.506 41.715  -4.668  1.00 34.78 ? 54  GLU A O   1 
ATOM   435  C  CB  . GLU A  1 53  ? 52.759 44.772  -4.408  1.00 37.84 ? 54  GLU A CB  1 
ATOM   436  C  CG  . GLU A  1 53  ? 52.717 46.199  -4.998  1.00 48.77 ? 54  GLU A CG  1 
ATOM   437  C  CD  . GLU A  1 53  ? 54.046 46.992  -4.858  1.00 62.45 ? 54  GLU A CD  1 
ATOM   438  O  OE1 . GLU A  1 53  ? 54.796 46.794  -3.863  1.00 57.92 ? 54  GLU A OE1 1 
ATOM   439  O  OE2 . GLU A  1 53  ? 54.340 47.824  -5.756  1.00 70.24 ? 54  GLU A OE2 1 
ATOM   440  N  N   . SER A  1 54  ? 51.734 42.417  -2.536  1.00 31.23 ? 55  SER A N   1 
ATOM   441  C  CA  . SER A  1 54  ? 51.866 41.051  -2.035  1.00 34.81 ? 55  SER A CA  1 
ATOM   442  C  C   . SER A  1 54  ? 50.583 40.248  -2.237  1.00 34.44 ? 55  SER A C   1 
ATOM   443  O  O   . SER A  1 54  ? 50.641 39.039  -2.499  1.00 36.13 ? 55  SER A O   1 
ATOM   444  C  CB  . SER A  1 54  ? 52.253 41.068  -0.561  1.00 34.70 ? 55  SER A CB  1 
ATOM   445  O  OG  . SER A  1 54  ? 53.489 41.725  -0.377  1.00 41.35 ? 55  SER A OG  1 
ATOM   446  N  N   . SER A  1 55  ? 49.421 40.901  -2.148  1.00 31.88 ? 56  SER A N   1 
ATOM   447  C  CA  . SER A  1 55  ? 48.166 40.195  -2.386  1.00 34.97 ? 56  SER A CA  1 
ATOM   448  C  C   . SER A  1 55  ? 48.088 39.694  -3.827  1.00 34.64 ? 56  SER A C   1 
ATOM   449  O  O   . SER A  1 55  ? 47.730 38.533  -4.072  1.00 32.52 ? 56  SER A O   1 
ATOM   450  C  CB  . SER A  1 55  ? 46.982 41.108  -2.051  1.00 33.10 ? 56  SER A CB  1 
ATOM   451  O  OG  . SER A  1 55  ? 45.741 40.499  -2.372  1.00 32.03 ? 56  SER A OG  1 
ATOM   452  N  N   . ASP A  1 56  ? 48.429 40.558  -4.794  1.00 30.90 ? 57  ASP A N   1 
ATOM   453  C  CA  . ASP A  1 56  ? 48.416 40.152  -6.204  1.00 35.11 ? 57  ASP A CA  1 
ATOM   454  C  C   . ASP A  1 56  ? 49.423 39.052  -6.475  1.00 35.81 ? 57  ASP A C   1 
ATOM   455  O  O   . ASP A  1 56  ? 49.140 38.110  -7.223  1.00 35.87 ? 57  ASP A O   1 
ATOM   456  C  CB  . ASP A  1 56  ? 48.728 41.336  -7.114  1.00 35.39 ? 57  ASP A CB  1 
ATOM   457  C  CG  . ASP A  1 56  ? 47.669 42.416  -7.052  1.00 46.93 ? 57  ASP A CG  1 
ATOM   458  O  OD1 . ASP A  1 56  ? 46.494 42.086  -6.753  1.00 47.45 ? 57  ASP A OD1 1 
ATOM   459  O  OD2 . ASP A  1 56  ? 48.020 43.594  -7.318  1.00 50.80 ? 57  ASP A OD2 1 
ATOM   460  N  N   . CYS A  1 57  ? 50.615 39.170  -5.888  1.00 31.31 ? 58  CYS A N   1 
ATOM   461  C  CA  . CYS A  1 57  ? 51.630 38.144  -6.050  1.00 39.55 ? 58  CYS A CA  1 
ATOM   462  C  C   . CYS A  1 57  ? 51.125 36.782  -5.584  1.00 37.60 ? 58  CYS A C   1 
ATOM   463  O  O   . CYS A  1 57  ? 51.300 35.779  -6.283  1.00 36.48 ? 58  CYS A O   1 
ATOM   464  C  CB  . CYS A  1 57  ? 52.890 38.550  -5.288  1.00 39.78 ? 58  CYS A CB  1 
ATOM   465  S  SG  . CYS A  1 57  ? 53.993 37.167  -5.032  1.00 67.71 ? 58  CYS A SG  1 
ATOM   466  N  N   . CYS A  1 58  ? 50.490 36.726  -4.408  1.00 33.99 ? 59  CYS A N   1 
ATOM   467  C  CA  . CYS A  1 58  ? 49.986 35.448  -3.914  1.00 35.71 ? 59  CYS A CA  1 
ATOM   468  C  C   . CYS A  1 58  ? 48.851 34.915  -4.786  1.00 39.17 ? 59  CYS A C   1 
ATOM   469  O  O   . CYS A  1 58  ? 48.734 33.695  -4.983  1.00 35.52 ? 59  CYS A O   1 
ATOM   470  C  CB  . CYS A  1 58  ? 49.536 35.589  -2.460  1.00 34.37 ? 59  CYS A CB  1 
ATOM   471  S  SG  . CYS A  1 58  ? 50.899 35.436  -1.257  1.00 47.11 ? 59  CYS A SG  1 
ATOM   472  N  N   . ARG A  1 59  ? 48.029 35.804  -5.345  1.00 31.87 ? 60  ARG A N   1 
ATOM   473  C  CA  . ARG A  1 59  ? 46.986 35.331  -6.238  1.00 36.59 ? 60  ARG A CA  1 
ATOM   474  C  C   . ARG A  1 59  ? 47.582 34.716  -7.503  1.00 37.47 ? 60  ARG A C   1 
ATOM   475  O  O   . ARG A  1 59  ? 47.075 33.695  -7.990  1.00 35.12 ? 60  ARG A O   1 
ATOM   476  C  CB  . ARG A  1 59  ? 46.013 36.458  -6.581  1.00 33.80 ? 60  ARG A CB  1 
ATOM   477  C  CG  . ARG A  1 59  ? 44.816 35.949  -7.374  1.00 39.26 ? 60  ARG A CG  1 
ATOM   478  C  CD  . ARG A  1 59  ? 43.825 37.057  -7.649  1.00 47.24 ? 60  ARG A CD  1 
ATOM   479  N  NE  . ARG A  1 59  ? 44.466 38.167  -8.342  1.00 45.28 ? 60  ARG A NE  1 
ATOM   480  C  CZ  . ARG A  1 59  ? 44.590 39.385  -7.832  1.00 48.37 ? 60  ARG A CZ  1 
ATOM   481  N  NH1 . ARG A  1 59  ? 44.192 39.660  -6.597  1.00 51.72 ? 60  ARG A NH1 1 
ATOM   482  N  NH2 . ARG A  1 59  ? 45.126 40.348  -8.577  1.00 46.80 ? 60  ARG A NH2 1 
ATOM   483  N  N   . GLU A  1 60  ? 48.666 35.300  -8.046  1.00 34.21 ? 61  GLU A N   1 
ATOM   484  C  CA  . GLU A  1 60  ? 49.314 34.656  -9.193  1.00 40.64 ? 61  GLU A CA  1 
ATOM   485  C  C   . GLU A  1 60  ? 49.977 33.337  -8.805  1.00 38.00 ? 61  GLU A C   1 
ATOM   486  O  O   . GLU A  1 60  ? 50.003 32.404  -9.613  1.00 35.99 ? 61  GLU A O   1 
ATOM   487  C  CB  . GLU A  1 60  ? 50.346 35.562  -9.872  1.00 35.47 ? 61  GLU A CB  1 
ATOM   488  C  CG  . GLU A  1 60  ? 49.945 36.010  -11.308 1.00 54.74 ? 61  GLU A CG  1 
ATOM   489  C  CD  . GLU A  1 60  ? 49.337 34.875  -12.226 1.00 71.00 ? 61  GLU A CD  1 
ATOM   490  O  OE1 . GLU A  1 60  ? 50.024 33.868  -12.581 1.00 60.90 ? 61  GLU A OE1 1 
ATOM   491  O  OE2 . GLU A  1 60  ? 48.162 35.029  -12.653 1.00 61.81 ? 61  GLU A OE2 1 
ATOM   492  N  N   . HIS A  1 61  ? 50.542 33.239  -7.593  1.00 35.42 ? 62  HIS A N   1 
ATOM   493  C  CA  . HIS A  1 61  ? 51.091 31.952  -7.158  1.00 35.66 ? 62  HIS A CA  1 
ATOM   494  C  C   . HIS A  1 61  ? 50.027 30.864  -7.227  1.00 35.02 ? 62  HIS A C   1 
ATOM   495  O  O   . HIS A  1 61  ? 50.299 29.742  -7.667  1.00 32.80 ? 62  HIS A O   1 
ATOM   496  C  CB  . HIS A  1 61  ? 51.635 32.034  -5.731  1.00 38.63 ? 62  HIS A CB  1 
ATOM   497  C  CG  . HIS A  1 61  ? 52.872 32.859  -5.586  1.00 46.87 ? 62  HIS A CG  1 
ATOM   498  N  ND1 . HIS A  1 61  ? 53.620 33.277  -6.666  1.00 47.08 ? 62  HIS A ND1 1 
ATOM   499  C  CD2 . HIS A  1 61  ? 53.488 33.350  -4.481  1.00 46.36 ? 62  HIS A CD2 1 
ATOM   500  C  CE1 . HIS A  1 61  ? 54.646 33.990  -6.235  1.00 50.60 ? 62  HIS A CE1 1 
ATOM   501  N  NE2 . HIS A  1 61  ? 54.584 34.055  -4.914  1.00 56.75 ? 62  HIS A NE2 1 
ATOM   502  N  N   . ALA A  1 62  ? 48.799 31.191  -6.807  1.00 32.05 ? 63  ALA A N   1 
ATOM   503  C  CA  . ALA A  1 62  ? 47.716 30.217  -6.825  1.00 33.37 ? 63  ALA A CA  1 
ATOM   504  C  C   . ALA A  1 62  ? 47.288 29.896  -8.250  1.00 33.40 ? 63  ALA A C   1 
ATOM   505  O  O   . ALA A  1 62  ? 47.015 28.737  -8.576  1.00 33.61 ? 63  ALA A O   1 
ATOM   506  C  CB  . ALA A  1 62  ? 46.524 30.736  -6.011  1.00 30.33 ? 63  ALA A CB  1 
ATOM   507  N  N   . GLN A  1 63  ? 47.202 30.906  -9.110  1.00 32.11 ? 64  GLN A N   1 
ATOM   508  C  CA  . GLN A  1 63  ? 46.816 30.635  -10.486 1.00 35.04 ? 64  GLN A CA  1 
ATOM   509  C  C   . GLN A  1 63  ? 47.881 29.824  -11.228 1.00 36.05 ? 64  GLN A C   1 
ATOM   510  O  O   . GLN A  1 63  ? 47.537 29.022  -12.103 1.00 33.51 ? 64  GLN A O   1 
ATOM   511  C  CB  . GLN A  1 63  ? 46.514 31.949  -11.196 1.00 41.59 ? 64  GLN A CB  1 
ATOM   512  C  CG  . GLN A  1 63  ? 45.054 32.394  -11.023 1.00 45.39 ? 64  GLN A CG  1 
ATOM   513  C  CD  . GLN A  1 63  ? 44.831 33.858  -11.374 1.00 51.67 ? 64  GLN A CD  1 
ATOM   514  O  OE1 . GLN A  1 63  ? 45.780 34.601  -11.596 1.00 54.95 ? 64  GLN A OE1 1 
ATOM   515  N  NE2 . GLN A  1 63  ? 43.573 34.277  -11.420 1.00 53.53 ? 64  GLN A NE2 1 
ATOM   516  N  N   . THR A  1 64  ? 49.166 29.988  -10.878 1.00 32.57 ? 65  THR A N   1 
ATOM   517  C  CA  . THR A  1 64  ? 50.213 29.177  -11.497 1.00 31.49 ? 65  THR A CA  1 
ATOM   518  C  C   . THR A  1 64  ? 50.060 27.703  -11.123 1.00 31.86 ? 65  THR A C   1 
ATOM   519  O  O   . THR A  1 64  ? 50.227 26.823  -11.975 1.00 33.77 ? 65  THR A O   1 
ATOM   520  C  CB  . THR A  1 64  ? 51.603 29.699  -11.103 1.00 33.74 ? 65  THR A CB  1 
ATOM   521  O  OG1 . THR A  1 64  ? 51.726 31.072  -11.475 1.00 39.58 ? 65  THR A OG1 1 
ATOM   522  C  CG2 . THR A  1 64  ? 52.714 28.915  -11.818 1.00 38.09 ? 65  THR A CG2 1 
ATOM   523  N  N   . PHE A  1 65  ? 49.718 27.418  -9.863  1.00 27.94 ? 66  PHE A N   1 
ATOM   524  C  CA  . PHE A  1 65  ? 49.464 26.040  -9.446  1.00 27.64 ? 66  PHE A CA  1 
ATOM   525  C  C   . PHE A  1 65  ? 48.235 25.456  -10.129 1.00 32.54 ? 66  PHE A C   1 
ATOM   526  O  O   . PHE A  1 65  ? 48.206 24.257  -10.439 1.00 26.85 ? 66  PHE A O   1 
ATOM   527  C  CB  . PHE A  1 65  ? 49.277 25.969  -7.936  1.00 31.33 ? 66  PHE A CB  1 
ATOM   528  C  CG  . PHE A  1 65  ? 50.546 25.830  -7.164  1.00 34.02 ? 66  PHE A CG  1 
ATOM   529  C  CD1 . PHE A  1 65  ? 51.456 24.824  -7.467  1.00 37.70 ? 66  PHE A CD1 1 
ATOM   530  C  CD2 . PHE A  1 65  ? 50.822 26.698  -6.111  1.00 37.20 ? 66  PHE A CD2 1 
ATOM   531  C  CE1 . PHE A  1 65  ? 52.635 24.690  -6.743  1.00 39.51 ? 66  PHE A CE1 1 
ATOM   532  C  CE2 . PHE A  1 65  ? 51.993 26.570  -5.374  1.00 37.41 ? 66  PHE A CE2 1 
ATOM   533  C  CZ  . PHE A  1 65  ? 52.907 25.567  -5.694  1.00 36.60 ? 66  PHE A CZ  1 
ATOM   534  N  N   . MET A  1 66  ? 47.193 26.268  -10.348 1.00 32.23 ? 67  MET A N   1 
ATOM   535  C  CA  . MET A  1 66  ? 46.014 25.750  -11.040 1.00 31.73 ? 67  MET A CA  1 
ATOM   536  C  C   . MET A  1 66  ? 46.361 25.346  -12.467 1.00 31.37 ? 67  MET A C   1 
ATOM   537  O  O   . MET A  1 66  ? 45.994 24.256  -12.925 1.00 30.89 ? 67  MET A O   1 
ATOM   538  C  CB  . MET A  1 66  ? 44.872 26.772  -11.047 1.00 30.40 ? 67  MET A CB  1 
ATOM   539  C  CG  . MET A  1 66  ? 44.166 26.942  -9.712  1.00 32.23 ? 67  MET A CG  1 
ATOM   540  S  SD  . MET A  1 66  ? 43.230 28.482  -9.570  1.00 38.48 ? 67  MET A SD  1 
ATOM   541  C  CE  . MET A  1 66  ? 41.652 27.883  -10.194 1.00 39.47 ? 67  MET A CE  1 
ATOM   542  N  N   . LYS A  1 67  ? 47.074 26.220  -13.182 1.00 32.57 ? 68  LYS A N   1 
ATOM   543  C  CA  . LYS A  1 67  ? 47.566 25.886  -14.514 1.00 33.07 ? 68  LYS A CA  1 
ATOM   544  C  C   . LYS A  1 67  ? 48.389 24.607  -14.481 1.00 34.27 ? 68  LYS A C   1 
ATOM   545  O  O   . LYS A  1 67  ? 48.224 23.725  -15.331 1.00 31.54 ? 68  LYS A O   1 
ATOM   546  C  CB  . LYS A  1 67  ? 48.403 27.043  -15.063 1.00 33.74 ? 68  LYS A CB  1 
ATOM   547  C  CG  . LYS A  1 67  ? 47.663 27.956  -16.041 1.00 45.14 ? 68  LYS A CG  1 
ATOM   548  C  CD  . LYS A  1 67  ? 48.296 29.353  -16.114 1.00 51.92 ? 68  LYS A CD  1 
ATOM   549  C  CE  . LYS A  1 67  ? 47.638 30.327  -15.131 1.00 44.94 ? 68  LYS A CE  1 
ATOM   550  N  NZ  . LYS A  1 67  ? 48.430 31.571  -14.896 1.00 52.97 ? 68  LYS A NZ  1 
ATOM   551  N  N   . TYR A  1 68  ? 49.262 24.477  -13.482 1.00 31.75 ? 69  TYR A N   1 
ATOM   552  C  CA  . TYR A  1 68  ? 50.109 23.296  -13.391 1.00 32.87 ? 69  TYR A CA  1 
ATOM   553  C  C   . TYR A  1 68  ? 49.279 22.027  -13.228 1.00 30.61 ? 69  TYR A C   1 
ATOM   554  O  O   . TYR A  1 68  ? 49.521 21.021  -13.900 1.00 33.33 ? 69  TYR A O   1 
ATOM   555  C  CB  . TYR A  1 68  ? 51.085 23.446  -12.227 1.00 31.30 ? 69  TYR A CB  1 
ATOM   556  C  CG  . TYR A  1 68  ? 52.093 22.324  -12.199 1.00 34.49 ? 69  TYR A CG  1 
ATOM   557  C  CD1 . TYR A  1 68  ? 53.196 22.347  -13.039 1.00 33.30 ? 69  TYR A CD1 1 
ATOM   558  C  CD2 . TYR A  1 68  ? 51.928 21.231  -11.356 1.00 29.78 ? 69  TYR A CD2 1 
ATOM   559  C  CE1 . TYR A  1 68  ? 54.111 21.322  -13.038 1.00 35.14 ? 69  TYR A CE1 1 
ATOM   560  C  CE2 . TYR A  1 68  ? 52.849 20.196  -11.338 1.00 34.47 ? 69  TYR A CE2 1 
ATOM   561  C  CZ  . TYR A  1 68  ? 53.939 20.247  -12.185 1.00 33.57 ? 69  TYR A CZ  1 
ATOM   562  O  OH  . TYR A  1 68  ? 54.869 19.228  -12.185 1.00 34.32 ? 69  TYR A OH  1 
ATOM   563  N  N   . GLN A  1 69  ? 48.313 22.057  -12.313 1.00 29.75 ? 70  GLN A N   1 
ATOM   564  C  CA  . GLN A  1 69  ? 47.381 20.952  -12.135 1.00 29.74 ? 70  GLN A CA  1 
ATOM   565  C  C   . GLN A  1 69  ? 46.767 20.531  -13.468 1.00 35.04 ? 70  GLN A C   1 
ATOM   566  O  O   . GLN A  1 69  ? 46.698 19.335  -13.788 1.00 32.39 ? 70  GLN A O   1 
ATOM   567  C  CB  . GLN A  1 69  ? 46.293 21.371  -11.140 1.00 31.55 ? 70  GLN A CB  1 
ATOM   568  C  CG  . GLN A  1 69  ? 45.425 20.233  -10.631 1.00 34.49 ? 70  GLN A CG  1 
ATOM   569  C  CD  . GLN A  1 69  ? 46.130 19.418  -9.565  1.00 38.26 ? 70  GLN A CD  1 
ATOM   570  O  OE1 . GLN A  1 69  ? 46.959 18.565  -9.880  1.00 40.55 ? 70  GLN A OE1 1 
ATOM   571  N  NE2 . GLN A  1 69  ? 45.829 19.697  -8.294  1.00 34.15 ? 70  GLN A NE2 1 
ATOM   572  N  N   . ASN A  1 70  ? 46.337 21.509  -14.276 1.00 28.28 ? 71  ASN A N   1 
ATOM   573  C  CA  . ASN A  1 70  ? 45.743 21.170  -15.568 1.00 36.21 ? 71  ASN A CA  1 
ATOM   574  C  C   . ASN A  1 70  ? 46.793 20.631  -16.528 1.00 32.43 ? 71  ASN A C   1 
ATOM   575  O  O   . ASN A  1 70  ? 46.503 19.736  -17.329 1.00 32.09 ? 71  ASN A O   1 
ATOM   576  C  CB  . ASN A  1 70  ? 45.034 22.385  -16.173 1.00 29.84 ? 71  ASN A CB  1 
ATOM   577  C  CG  . ASN A  1 70  ? 43.609 22.496  -15.713 1.00 34.26 ? 71  ASN A CG  1 
ATOM   578  O  OD1 . ASN A  1 70  ? 43.074 21.559  -15.112 1.00 35.46 ? 71  ASN A OD1 1 
ATOM   579  N  ND2 . ASN A  1 70  ? 42.976 23.633  -15.988 1.00 33.51 ? 71  ASN A ND2 1 
ATOM   580  N  N   . LYS A  1 71  ? 48.016 21.160  -16.452 1.00 31.65 ? 72  LYS A N   1 
ATOM   581  C  CA  . LYS A  1 71  ? 49.077 20.729  -17.358 1.00 35.76 ? 72  LYS A CA  1 
ATOM   582  C  C   . LYS A  1 71  ? 49.434 19.260  -17.141 1.00 32.96 ? 72  LYS A C   1 
ATOM   583  O  O   . LYS A  1 71  ? 49.662 18.525  -18.106 1.00 31.53 ? 72  LYS A O   1 
ATOM   584  C  CB  . LYS A  1 71  ? 50.298 21.628  -17.173 1.00 35.09 ? 72  LYS A CB  1 
ATOM   585  C  CG  . LYS A  1 71  ? 51.206 21.663  -18.371 1.00 41.44 ? 72  LYS A CG  1 
ATOM   586  C  CD  . LYS A  1 71  ? 52.501 22.419  -18.080 1.00 49.61 ? 72  LYS A CD  1 
ATOM   587  C  CE  . LYS A  1 71  ? 52.288 23.934  -17.991 1.00 49.06 ? 72  LYS A CE  1 
ATOM   588  N  NZ  . LYS A  1 71  ? 52.311 24.446  -16.576 1.00 51.34 ? 72  LYS A NZ  1 
ATOM   589  N  N   . ARG A  1 72  ? 49.454 18.807  -15.882 1.00 31.72 ? 73  ARG A N   1 
ATOM   590  C  CA  . ARG A  1 72  ? 49.813 17.434  -15.540 1.00 32.49 ? 73  ARG A CA  1 
ATOM   591  C  C   . ARG A  1 72  ? 48.631 16.475  -15.607 1.00 32.68 ? 73  ARG A C   1 
ATOM   592  O  O   . ARG A  1 72  ? 48.824 15.268  -15.431 1.00 29.41 ? 73  ARG A O   1 
ATOM   593  C  CB  . ARG A  1 72  ? 50.417 17.365  -14.125 1.00 33.11 ? 73  ARG A CB  1 
ATOM   594  C  CG  . ARG A  1 72  ? 51.751 18.113  -13.937 1.00 36.03 ? 73  ARG A CG  1 
ATOM   595  C  CD  . ARG A  1 72  ? 52.851 17.604  -14.867 1.00 32.94 ? 73  ARG A CD  1 
ATOM   596  N  NE  . ARG A  1 72  ? 53.132 16.185  -14.669 1.00 32.34 ? 73  ARG A NE  1 
ATOM   597  C  CZ  . ARG A  1 72  ? 53.830 15.684  -13.657 1.00 32.64 ? 73  ARG A CZ  1 
ATOM   598  N  NH1 . ARG A  1 72  ? 54.349 16.463  -12.717 1.00 32.57 ? 73  ARG A NH1 1 
ATOM   599  N  NH2 . ARG A  1 72  ? 54.014 14.370  -13.585 1.00 28.19 ? 73  ARG A NH2 1 
ATOM   600  N  N   . GLY A  1 73  ? 47.422 16.976  -15.835 1.00 30.19 ? 74  GLY A N   1 
ATOM   601  C  CA  . GLY A  1 73  ? 46.267 16.117  -15.950 1.00 31.81 ? 74  GLY A CA  1 
ATOM   602  C  C   . GLY A  1 73  ? 45.585 15.783  -14.648 1.00 36.08 ? 74  GLY A C   1 
ATOM   603  O  O   . GLY A  1 73  ? 44.788 14.843  -14.614 1.00 41.55 ? 74  GLY A O   1 
ATOM   604  N  N   . GLY A  1 74  ? 45.901 16.490  -13.568 1.00 37.78 ? 75  GLY A N   1 
ATOM   605  C  CA  . GLY A  1 74  ? 45.137 16.379  -12.345 1.00 39.14 ? 75  GLY A CA  1 
ATOM   606  C  C   . GLY A  1 74  ? 43.916 17.286  -12.369 1.00 39.93 ? 75  GLY A C   1 
ATOM   607  O  O   . GLY A  1 74  ? 43.683 18.049  -13.304 1.00 43.16 ? 75  GLY A O   1 
ATOM   608  N  N   . ARG A  1 75  ? 43.115 17.208  -11.315 1.00 36.83 ? 76  ARG A N   1 
ATOM   609  C  CA  . ARG A  1 75  ? 41.880 17.972  -11.254 1.00 37.09 ? 76  ARG A CA  1 
ATOM   610  C  C   . ARG A  1 75  ? 41.934 19.005  -10.140 1.00 36.70 ? 76  ARG A C   1 
ATOM   611  O  O   . ARG A  1 75  ? 42.241 18.676  -8.990  1.00 36.97 ? 76  ARG A O   1 
ATOM   612  C  CB  . ARG A  1 75  ? 40.677 17.043  -11.097 1.00 36.52 ? 76  ARG A CB  1 
ATOM   613  C  CG  . ARG A  1 75  ? 40.337 16.380  -12.444 1.00 51.33 ? 76  ARG A CG  1 
ATOM   614  C  CD  . ARG A  1 75  ? 40.165 17.454  -13.564 1.00 50.63 ? 76  ARG A CD  1 
ATOM   615  N  NE  . ARG A  1 75  ? 40.216 16.887  -14.910 1.00 51.42 ? 76  ARG A NE  1 
ATOM   616  C  CZ  . ARG A  1 75  ? 41.199 17.085  -15.783 1.00 56.60 ? 76  ARG A CZ  1 
ATOM   617  N  NH1 . ARG A  1 75  ? 42.217 17.902  -15.516 1.00 48.25 ? 76  ARG A NH1 1 
ATOM   618  N  NH2 . ARG A  1 75  ? 41.162 16.452  -16.955 1.00 53.81 ? 76  ARG A NH2 1 
ATOM   619  N  N   . ILE A  1 76  ? 41.655 20.260  -10.503 1.00 35.52 ? 77  ILE A N   1 
ATOM   620  C  CA  . ILE A  1 76  ? 41.584 21.343  -9.531  1.00 35.24 ? 77  ILE A CA  1 
ATOM   621  C  C   . ILE A  1 76  ? 40.368 21.151  -8.634  1.00 36.10 ? 77  ILE A C   1 
ATOM   622  O  O   . ILE A  1 76  ? 39.268 20.822  -9.098  1.00 37.22 ? 77  ILE A O   1 
ATOM   623  C  CB  . ILE A  1 76  ? 41.526 22.702  -10.250 1.00 36.31 ? 77  ILE A CB  1 
ATOM   624  C  CG1 . ILE A  1 76  ? 42.736 22.859  -11.181 1.00 32.21 ? 77  ILE A CG1 1 
ATOM   625  C  CG2 . ILE A  1 76  ? 41.440 23.843  -9.225  1.00 34.15 ? 77  ILE A CG2 1 
ATOM   626  C  CD1 . ILE A  1 76  ? 42.545 23.914  -12.263 1.00 29.98 ? 77  ILE A CD1 1 
ATOM   627  N  N   . VAL A  1 77  ? 40.565 21.341  -7.335  1.00 34.64 ? 78  VAL A N   1 
ATOM   628  C  CA  . VAL A  1 77  ? 39.476 21.291  -6.369  1.00 39.88 ? 78  VAL A CA  1 
ATOM   629  C  C   . VAL A  1 77  ? 39.626 22.525  -5.494  1.00 36.57 ? 78  VAL A C   1 
ATOM   630  O  O   . VAL A  1 77  ? 40.565 22.617  -4.689  1.00 33.84 ? 78  VAL A O   1 
ATOM   631  C  CB  . VAL A  1 77  ? 39.485 20.005  -5.527  1.00 42.44 ? 78  VAL A CB  1 
ATOM   632  C  CG1 . VAL A  1 77  ? 38.273 19.971  -4.583  1.00 32.77 ? 78  VAL A CG1 1 
ATOM   633  C  CG2 . VAL A  1 77  ? 39.521 18.759  -6.437  1.00 37.34 ? 78  VAL A CG2 1 
ATOM   634  N  N   . LEU A  1 78  ? 38.731 23.483  -5.668  1.00 35.21 ? 79  LEU A N   1 
ATOM   635  C  CA  . LEU A  1 78  ? 38.780 24.698  -4.875  1.00 36.41 ? 79  LEU A CA  1 
ATOM   636  C  C   . LEU A  1 78  ? 38.013 24.492  -3.579  1.00 37.42 ? 79  LEU A C   1 
ATOM   637  O  O   . LEU A  1 78  ? 36.968 23.833  -3.555  1.00 41.12 ? 79  LEU A O   1 
ATOM   638  C  CB  . LEU A  1 78  ? 38.219 25.877  -5.662  1.00 33.67 ? 79  LEU A CB  1 
ATOM   639  C  CG  . LEU A  1 78  ? 38.981 26.075  -6.981  1.00 37.71 ? 79  LEU A CG  1 
ATOM   640  C  CD1 . LEU A  1 78  ? 38.220 27.010  -7.901  1.00 35.15 ? 79  LEU A CD1 1 
ATOM   641  C  CD2 . LEU A  1 78  ? 40.392 26.593  -6.729  1.00 31.03 ? 79  LEU A CD2 1 
ATOM   642  N  N   . GLN A  1 79  ? 38.561 25.036  -2.501  1.00 37.56 ? 80  GLN A N   1 
ATOM   643  C  CA  . GLN A  1 79  ? 37.978 24.994  -1.170  1.00 40.24 ? 80  GLN A CA  1 
ATOM   644  C  C   . GLN A  1 79  ? 37.650 26.410  -0.724  1.00 38.17 ? 80  GLN A C   1 
ATOM   645  O  O   . GLN A  1 79  ? 38.135 27.389  -1.302  1.00 32.04 ? 80  GLN A O   1 
ATOM   646  C  CB  . GLN A  1 79  ? 38.943 24.340  -0.167  1.00 40.41 ? 80  GLN A CB  1 
ATOM   647  C  CG  . GLN A  1 79  ? 39.387 22.923  -0.517  1.00 45.99 ? 80  GLN A CG  1 
ATOM   648  C  CD  . GLN A  1 79  ? 38.359 21.855  -0.113  1.00 60.11 ? 80  GLN A CD  1 
ATOM   649  O  OE1 . GLN A  1 79  ? 37.182 21.915  -0.493  1.00 57.48 ? 80  GLN A OE1 1 
ATOM   650  N  NE2 . GLN A  1 79  ? 38.806 20.878  0.674   1.00 67.72 ? 80  GLN A NE2 1 
ATOM   651  N  N   . GLN A  1 80  ? 36.842 26.510  0.337   1.00 33.06 ? 81  GLN A N   1 
ATOM   652  C  CA  . GLN A  1 80  ? 36.565 27.803  0.950   1.00 31.65 ? 81  GLN A CA  1 
ATOM   653  C  C   . GLN A  1 80  ? 37.862 28.521  1.327   1.00 29.84 ? 81  GLN A C   1 
ATOM   654  O  O   . GLN A  1 80  ? 38.882 27.898  1.643   1.00 31.15 ? 81  GLN A O   1 
ATOM   655  C  CB  . GLN A  1 80  ? 35.688 27.626  2.190   1.00 34.49 ? 81  GLN A CB  1 
ATOM   656  C  CG  . GLN A  1 80  ? 36.299 26.728  3.266   1.00 39.56 ? 81  GLN A CG  1 
ATOM   657  C  CD  . GLN A  1 80  ? 35.256 26.190  4.235   1.00 44.82 ? 81  GLN A CD  1 
ATOM   658  O  OE1 . GLN A  1 80  ? 34.087 26.024  3.871   1.00 43.58 ? 81  GLN A OE1 1 
ATOM   659  N  NE2 . GLN A  1 80  ? 35.670 25.928  5.482   1.00 41.52 ? 81  GLN A NE2 1 
ATOM   660  N  N   . ILE A  1 81  ? 37.817 29.845  1.291   1.00 28.08 ? 82  ILE A N   1 
ATOM   661  C  CA  . ILE A  1 81  ? 38.950 30.692  1.653   1.00 28.19 ? 82  ILE A CA  1 
ATOM   662  C  C   . ILE A  1 81  ? 38.585 31.378  2.958   1.00 27.92 ? 82  ILE A C   1 
ATOM   663  O  O   . ILE A  1 81  ? 37.796 32.327  2.965   1.00 29.24 ? 82  ILE A O   1 
ATOM   664  C  CB  . ILE A  1 81  ? 39.280 31.720  0.565   1.00 26.70 ? 82  ILE A CB  1 
ATOM   665  C  CG1 . ILE A  1 81  ? 39.582 31.024  -0.771  1.00 29.04 ? 82  ILE A CG1 1 
ATOM   666  C  CG2 . ILE A  1 81  ? 40.450 32.582  0.993   1.00 23.21 ? 82  ILE A CG2 1 
ATOM   667  C  CD1 . ILE A  1 81  ? 39.497 31.970  -1.964  1.00 27.87 ? 82  ILE A CD1 1 
ATOM   668  N  N   . ALA A  1 82  ? 39.152 30.901  4.064   1.00 29.56 ? 83  ALA A N   1 
ATOM   669  C  CA  . ALA A  1 82  ? 38.867 31.479  5.372   1.00 27.89 ? 83  ALA A CA  1 
ATOM   670  C  C   . ALA A  1 82  ? 39.191 32.967  5.399   1.00 31.41 ? 83  ALA A C   1 
ATOM   671  O  O   . ALA A  1 82  ? 40.147 33.431  4.772   1.00 31.29 ? 83  ALA A O   1 
ATOM   672  C  CB  . ALA A  1 82  ? 39.675 30.765  6.458   1.00 27.61 ? 83  ALA A CB  1 
ATOM   673  N  N   . ALA A  1 83  ? 38.388 33.722  6.149   1.00 28.34 ? 84  ALA A N   1 
ATOM   674  C  CA  . ALA A  1 83  ? 38.709 35.120  6.386   1.00 28.42 ? 84  ALA A CA  1 
ATOM   675  C  C   . ALA A  1 83  ? 39.896 35.226  7.342   1.00 33.04 ? 84  ALA A C   1 
ATOM   676  O  O   . ALA A  1 83  ? 40.094 34.352  8.198   1.00 35.40 ? 84  ALA A O   1 
ATOM   677  C  CB  . ALA A  1 83  ? 37.508 35.865  6.971   1.00 29.79 ? 84  ALA A CB  1 
ATOM   678  N  N   . PRO A  1 84  ? 40.706 36.279  7.214   1.00 40.65 ? 85  PRO A N   1 
ATOM   679  C  CA  . PRO A  1 84  ? 41.741 36.538  8.231   1.00 39.36 ? 85  PRO A CA  1 
ATOM   680  C  C   . PRO A  1 84  ? 41.096 36.646  9.602   1.00 40.77 ? 85  PRO A C   1 
ATOM   681  O  O   . PRO A  1 84  ? 40.045 37.267  9.765   1.00 37.63 ? 85  PRO A O   1 
ATOM   682  C  CB  . PRO A  1 84  ? 42.357 37.871  7.795   1.00 39.49 ? 85  PRO A CB  1 
ATOM   683  C  CG  . PRO A  1 84  ? 41.938 38.061  6.356   1.00 36.36 ? 85  PRO A CG  1 
ATOM   684  C  CD  . PRO A  1 84  ? 40.626 37.346  6.198   1.00 34.75 ? 85  PRO A CD  1 
ATOM   685  N  N   . SER A  1 85  ? 41.724 36.013  10.590  1.00 50.33 ? 86  SER A N   1 
ATOM   686  C  CA  . SER A  1 85  ? 41.115 35.942  11.915  1.00 50.74 ? 86  SER A CA  1 
ATOM   687  C  C   . SER A  1 85  ? 41.107 37.309  12.597  1.00 50.60 ? 86  SER A C   1 
ATOM   688  O  O   . SER A  1 85  ? 40.076 37.740  13.127  1.00 53.37 ? 86  SER A O   1 
ATOM   689  C  CB  . SER A  1 85  ? 41.844 34.907  12.767  1.00 50.53 ? 86  SER A CB  1 
ATOM   690  O  OG  . SER A  1 85  ? 41.252 34.839  14.045  1.00 52.21 ? 86  SER A OG  1 
ATOM   691  N  N   . MET A  1 86  ? 42.241 38.005  12.593  1.00 51.33 ? 87  MET A N   1 
ATOM   692  C  CA  . MET A  1 86  ? 42.323 39.385  13.066  1.00 57.83 ? 87  MET A CA  1 
ATOM   693  C  C   . MET A  1 86  ? 42.453 40.297  11.853  1.00 52.86 ? 87  MET A C   1 
ATOM   694  O  O   . MET A  1 86  ? 43.379 40.133  11.054  1.00 54.54 ? 87  MET A O   1 
ATOM   695  C  CB  . MET A  1 86  ? 43.510 39.585  14.018  1.00 60.12 ? 87  MET A CB  1 
ATOM   696  C  CG  . MET A  1 86  ? 43.629 41.011  14.605  1.00 66.47 ? 87  MET A CG  1 
ATOM   697  S  SD  . MET A  1 86  ? 42.352 41.511  15.818  1.00 99.47 ? 87  MET A SD  1 
ATOM   698  C  CE  . MET A  1 86  ? 41.101 42.345  14.819  1.00 52.66 ? 87  MET A CE  1 
ATOM   699  N  N   . GLN A  1 87  ? 41.539 41.259  11.723  1.00 50.76 ? 88  GLN A N   1 
ATOM   700  C  CA  . GLN A  1 87  ? 41.548 42.188  10.601  1.00 49.73 ? 88  GLN A CA  1 
ATOM   701  C  C   . GLN A  1 87  ? 41.921 43.619  10.988  1.00 52.35 ? 88  GLN A C   1 
ATOM   702  O  O   . GLN A  1 87  ? 41.932 44.502  10.121  1.00 48.17 ? 88  GLN A O   1 
ATOM   703  C  CB  . GLN A  1 87  ? 40.187 42.180  9.910   1.00 45.44 ? 88  GLN A CB  1 
ATOM   704  C  CG  . GLN A  1 87  ? 39.885 40.867  9.203   1.00 44.75 ? 88  GLN A CG  1 
ATOM   705  C  CD  . GLN A  1 87  ? 38.469 40.826  8.673   1.00 42.45 ? 88  GLN A CD  1 
ATOM   706  O  OE1 . GLN A  1 87  ? 37.975 41.813  8.091   1.00 38.07 ? 88  GLN A OE1 1 
ATOM   707  N  NE2 . GLN A  1 87  ? 37.792 39.690  8.873   1.00 38.92 ? 88  GLN A NE2 1 
ATOM   708  N  N   . GLU A  1 88  ? 42.206 43.881  12.258  1.00 54.23 ? 89  GLU A N   1 
ATOM   709  C  CA  . GLU A  1 88  ? 42.806 45.139  12.683  1.00 54.47 ? 89  GLU A CA  1 
ATOM   710  C  C   . GLU A  1 88  ? 44.271 44.856  12.976  1.00 49.36 ? 89  GLU A C   1 
ATOM   711  O  O   . GLU A  1 88  ? 44.600 44.247  13.997  1.00 50.52 ? 89  GLU A O   1 
ATOM   712  C  CB  . GLU A  1 88  ? 42.099 45.718  13.904  1.00 59.93 ? 89  GLU A CB  1 
ATOM   713  C  CG  . GLU A  1 88  ? 41.041 46.751  13.548  1.00 64.78 ? 89  GLU A CG  1 
ATOM   714  C  CD  . GLU A  1 88  ? 39.897 46.775  14.541  1.00 78.57 ? 89  GLU A CD  1 
ATOM   715  O  OE1 . GLU A  1 88  ? 39.039 45.861  14.492  1.00 78.31 ? 89  GLU A OE1 1 
ATOM   716  O  OE2 . GLU A  1 88  ? 39.858 47.711  15.371  1.00 83.00 ? 89  GLU A OE2 1 
ATOM   717  N  N   . TRP A  1 89  ? 45.145 45.295  12.083  1.00 42.27 ? 90  TRP A N   1 
ATOM   718  C  CA  . TRP A  1 89  ? 46.517 44.822  12.091  1.00 47.38 ? 90  TRP A CA  1 
ATOM   719  C  C   . TRP A  1 89  ? 47.442 45.629  12.988  1.00 46.49 ? 90  TRP A C   1 
ATOM   720  O  O   . TRP A  1 89  ? 48.592 45.221  13.178  1.00 47.19 ? 90  TRP A O   1 
ATOM   721  C  CB  . TRP A  1 89  ? 47.039 44.791  10.659  1.00 38.72 ? 90  TRP A CB  1 
ATOM   722  C  CG  . TRP A  1 89  ? 46.234 43.854  9.864   1.00 39.84 ? 90  TRP A CG  1 
ATOM   723  C  CD1 . TRP A  1 89  ? 45.192 44.161  9.033   1.00 40.43 ? 90  TRP A CD1 1 
ATOM   724  C  CD2 . TRP A  1 89  ? 46.353 42.429  9.854   1.00 41.61 ? 90  TRP A CD2 1 
ATOM   725  N  NE1 . TRP A  1 89  ? 44.670 43.013  8.484   1.00 38.57 ? 90  TRP A NE1 1 
ATOM   726  C  CE2 . TRP A  1 89  ? 45.366 41.934  8.971   1.00 41.14 ? 90  TRP A CE2 1 
ATOM   727  C  CE3 . TRP A  1 89  ? 47.213 41.523  10.489  1.00 37.95 ? 90  TRP A CE3 1 
ATOM   728  C  CZ2 . TRP A  1 89  ? 45.210 40.570  8.713   1.00 38.00 ? 90  TRP A CZ2 1 
ATOM   729  C  CZ3 . TRP A  1 89  ? 47.061 40.172  10.231  1.00 39.77 ? 90  TRP A CZ3 1 
ATOM   730  C  CH2 . TRP A  1 89  ? 46.062 39.706  9.350   1.00 40.60 ? 90  TRP A CH2 1 
ATOM   731  N  N   . GLY A  1 90  ? 46.979 46.736  13.558  1.00 45.45 ? 91  GLY A N   1 
ATOM   732  C  CA  . GLY A  1 90  ? 47.814 47.479  14.493  1.00 43.33 ? 91  GLY A CA  1 
ATOM   733  C  C   . GLY A  1 90  ? 48.790 48.379  13.772  1.00 45.26 ? 91  GLY A C   1 
ATOM   734  O  O   . GLY A  1 90  ? 48.421 49.089  12.837  1.00 45.47 ? 91  GLY A O   1 
ATOM   735  N  N   . THR A  1 91  ? 50.046 48.360  14.207  1.00 47.35 ? 92  THR A N   1 
ATOM   736  C  CA  . THR A  1 91  ? 51.070 49.212  13.616  1.00 42.99 ? 92  THR A CA  1 
ATOM   737  C  C   . THR A  1 91  ? 51.659 48.566  12.362  1.00 41.68 ? 92  THR A C   1 
ATOM   738  O  O   . THR A  1 91  ? 51.480 47.374  12.105  1.00 41.94 ? 92  THR A O   1 
ATOM   739  C  CB  . THR A  1 91  ? 52.176 49.486  14.631  1.00 46.20 ? 92  THR A CB  1 
ATOM   740  O  OG1 . THR A  1 91  ? 52.922 48.277  14.855  1.00 44.54 ? 92  THR A OG1 1 
ATOM   741  C  CG2 . THR A  1 91  ? 51.569 49.953  15.954  1.00 42.81 ? 92  THR A CG2 1 
ATOM   742  N  N   . GLY A  1 92  ? 52.372 49.377  11.571  1.00 44.68 ? 93  GLY A N   1 
ATOM   743  C  CA  . GLY A  1 92  ? 53.038 48.843  10.390  1.00 40.97 ? 93  GLY A CA  1 
ATOM   744  C  C   . GLY A  1 92  ? 54.082 47.794  10.731  1.00 40.00 ? 93  GLY A C   1 
ATOM   745  O  O   . GLY A  1 92  ? 54.297 46.848  9.962   1.00 37.02 ? 93  GLY A O   1 
ATOM   746  N  N   . LEU A  1 93  ? 54.731 47.935  11.889  1.00 36.25 ? 94  LEU A N   1 
ATOM   747  C  CA  . LEU A  1 93  ? 55.678 46.921  12.335  1.00 40.73 ? 94  LEU A CA  1 
ATOM   748  C  C   . LEU A  1 93  ? 54.968 45.596  12.608  1.00 41.13 ? 94  LEU A C   1 
ATOM   749  O  O   . LEU A  1 93  ? 55.431 44.539  12.166  1.00 36.63 ? 94  LEU A O   1 
ATOM   750  C  CB  . LEU A  1 93  ? 56.432 47.403  13.576  1.00 34.57 ? 94  LEU A CB  1 
ATOM   751  C  CG  . LEU A  1 93  ? 57.459 46.428  14.165  1.00 43.15 ? 94  LEU A CG  1 
ATOM   752  C  CD1 . LEU A  1 93  ? 58.410 45.919  13.091  1.00 39.23 ? 94  LEU A CD1 1 
ATOM   753  C  CD2 . LEU A  1 93  ? 58.244 47.070  15.306  1.00 39.90 ? 94  LEU A CD2 1 
ATOM   754  N  N   . GLU A  1 94  ? 53.831 45.637  13.321  1.00 36.85 ? 95  GLU A N   1 
ATOM   755  C  CA  . GLU A  1 94  ? 53.111 44.407  13.652  1.00 38.54 ? 95  GLU A CA  1 
ATOM   756  C  C   . GLU A  1 94  ? 52.627 43.694  12.400  1.00 36.32 ? 95  GLU A C   1 
ATOM   757  O  O   . GLU A  1 94  ? 52.596 42.456  12.362  1.00 38.48 ? 95  GLU A O   1 
ATOM   758  C  CB  . GLU A  1 94  ? 51.923 44.704  14.579  1.00 41.55 ? 95  GLU A CB  1 
ATOM   759  C  CG  . GLU A  1 94  ? 52.330 45.142  15.987  1.00 49.49 ? 95  GLU A CG  1 
ATOM   760  C  CD  . GLU A  1 94  ? 51.210 45.826  16.781  1.00 55.05 ? 95  GLU A CD  1 
ATOM   761  O  OE1 . GLU A  1 94  ? 50.270 46.393  16.175  1.00 56.64 ? 95  GLU A OE1 1 
ATOM   762  O  OE2 . GLU A  1 94  ? 51.285 45.805  18.030  1.00 66.61 ? 95  GLU A OE2 1 
ATOM   763  N  N   . ALA A  1 95  ? 52.257 44.456  11.367  1.00 31.45 ? 96  ALA A N   1 
ATOM   764  C  CA  . ALA A  1 95  ? 51.827 43.849  10.116  1.00 36.28 ? 96  ALA A CA  1 
ATOM   765  C  C   . ALA A  1 95  ? 52.998 43.189  9.391   1.00 36.16 ? 96  ALA A C   1 
ATOM   766  O  O   . ALA A  1 95  ? 52.838 42.123  8.782   1.00 36.84 ? 96  ALA A O   1 
ATOM   767  C  CB  . ALA A  1 95  ? 51.154 44.901  9.233   1.00 35.81 ? 96  ALA A CB  1 
ATOM   768  N  N   . LEU A  1 96  ? 54.183 43.807  9.441   1.00 34.53 ? 97  LEU A N   1 
ATOM   769  C  CA  . LEU A  1 96  ? 55.362 43.192  8.838   1.00 34.79 ? 97  LEU A CA  1 
ATOM   770  C  C   . LEU A  1 96  ? 55.739 41.900  9.555   1.00 35.17 ? 97  LEU A C   1 
ATOM   771  O  O   . LEU A  1 96  ? 56.073 40.900  8.907   1.00 33.82 ? 97  LEU A O   1 
ATOM   772  C  CB  . LEU A  1 96  ? 56.526 44.175  8.853   1.00 36.09 ? 97  LEU A CB  1 
ATOM   773  C  CG  . LEU A  1 96  ? 56.400 45.333  7.868   1.00 39.87 ? 97  LEU A CG  1 
ATOM   774  C  CD1 . LEU A  1 96  ? 57.617 46.252  7.971   1.00 38.52 ? 97  LEU A CD1 1 
ATOM   775  C  CD2 . LEU A  1 96  ? 56.217 44.808  6.453   1.00 35.19 ? 97  LEU A CD2 1 
ATOM   776  N  N   . GLN A  1 97  ? 55.658 41.891  10.891  1.00 33.92 ? 98  GLN A N   1 
ATOM   777  C  CA  . GLN A  1 97  ? 55.951 40.672  11.640  1.00 35.96 ? 98  GLN A CA  1 
ATOM   778  C  C   . GLN A  1 97  ? 54.978 39.551  11.287  1.00 37.35 ? 98  GLN A C   1 
ATOM   779  O  O   . GLN A  1 97  ? 55.395 38.407  11.077  1.00 36.16 ? 98  GLN A O   1 
ATOM   780  C  CB  . GLN A  1 97  ? 55.927 40.959  13.139  1.00 37.89 ? 98  GLN A CB  1 
ATOM   781  C  CG  . GLN A  1 97  ? 57.176 41.682  13.607  1.00 43.77 ? 98  GLN A CG  1 
ATOM   782  C  CD  . GLN A  1 97  ? 56.995 42.436  14.924  1.00 49.08 ? 98  GLN A CD  1 
ATOM   783  O  OE1 . GLN A  1 97  ? 55.874 42.791  15.317  1.00 45.06 ? 98  GLN A OE1 1 
ATOM   784  N  NE2 . GLN A  1 97  ? 58.112 42.682  15.612  1.00 45.17 ? 98  GLN A NE2 1 
ATOM   785  N  N   . ALA A  1 98  ? 53.678 39.861  11.212  1.00 38.09 ? 99  ALA A N   1 
ATOM   786  C  CA  . ALA A  1 98  ? 52.705 38.871  10.760  1.00 34.77 ? 99  ALA A CA  1 
ATOM   787  C  C   . ALA A  1 98  ? 53.020 38.391  9.348   1.00 35.07 ? 99  ALA A C   1 
ATOM   788  O  O   . ALA A  1 98  ? 52.984 37.187  9.074   1.00 36.27 ? 99  ALA A O   1 
ATOM   789  C  CB  . ALA A  1 98  ? 51.295 39.453  10.816  1.00 32.07 ? 99  ALA A CB  1 
ATOM   790  N  N   . ALA A  1 99  ? 53.325 39.320  8.434   1.00 35.53 ? 100 ALA A N   1 
ATOM   791  C  CA  . ALA A  1 99  ? 53.658 38.926  7.067   1.00 33.39 ? 100 ALA A CA  1 
ATOM   792  C  C   . ALA A  1 99  ? 54.895 38.038  7.027   1.00 35.04 ? 100 ALA A C   1 
ATOM   793  O  O   . ALA A  1 99  ? 54.946 37.072  6.258   1.00 39.64 ? 100 ALA A O   1 
ATOM   794  C  CB  . ALA A  1 99  ? 53.870 40.158  6.193   1.00 32.66 ? 100 ALA A CB  1 
ATOM   795  N  N   . LEU A  1 100 ? 55.913 38.354  7.832   1.00 34.53 ? 101 LEU A N   1 
ATOM   796  C  CA  . LEU A  1 100 ? 57.093 37.496  7.871   1.00 35.56 ? 101 LEU A CA  1 
ATOM   797  C  C   . LEU A  1 100 ? 56.727 36.081  8.318   1.00 36.37 ? 101 LEU A C   1 
ATOM   798  O  O   . LEU A  1 100 ? 57.182 35.101  7.723   1.00 33.57 ? 101 LEU A O   1 
ATOM   799  C  CB  . LEU A  1 100 ? 58.154 38.096  8.787   1.00 32.04 ? 101 LEU A CB  1 
ATOM   800  C  CG  . LEU A  1 100 ? 59.455 37.289  8.949   1.00 40.28 ? 101 LEU A CG  1 
ATOM   801  C  CD1 . LEU A  1 100 ? 60.264 37.244  7.633   1.00 32.79 ? 101 LEU A CD1 1 
ATOM   802  C  CD2 . LEU A  1 100 ? 60.313 37.831  10.104  1.00 34.11 ? 101 LEU A CD2 1 
ATOM   803  N  N   . ASP A  1 101 ? 55.880 35.953  9.343   1.00 35.05 ? 102 ASP A N   1 
ATOM   804  C  CA  . ASP A  1 101 ? 55.451 34.625  9.780   1.00 35.67 ? 102 ASP A CA  1 
ATOM   805  C  C   . ASP A  1 101 ? 54.612 33.920  8.712   1.00 38.15 ? 102 ASP A C   1 
ATOM   806  O  O   . ASP A  1 101 ? 54.764 32.714  8.496   1.00 35.70 ? 102 ASP A O   1 
ATOM   807  C  CB  . ASP A  1 101 ? 54.673 34.724  11.094  1.00 41.97 ? 102 ASP A CB  1 
ATOM   808  C  CG  . ASP A  1 101 ? 53.766 33.503  11.340  1.00 57.70 ? 102 ASP A CG  1 
ATOM   809  O  OD1 . ASP A  1 101 ? 52.595 33.510  10.867  1.00 60.83 ? 102 ASP A OD1 1 
ATOM   810  O  OD2 . ASP A  1 101 ? 54.227 32.531  12.001  1.00 60.11 ? 102 ASP A OD2 1 
ATOM   811  N  N   . LEU A  1 102 ? 53.711 34.646  8.042   1.00 34.60 ? 103 LEU A N   1 
ATOM   812  C  CA  . LEU A  1 102 ? 52.936 34.039  6.963   1.00 37.36 ? 103 LEU A CA  1 
ATOM   813  C  C   . LEU A  1 102 ? 53.842 33.505  5.849   1.00 37.86 ? 103 LEU A C   1 
ATOM   814  O  O   . LEU A  1 102 ? 53.637 32.389  5.354   1.00 38.69 ? 103 LEU A O   1 
ATOM   815  C  CB  . LEU A  1 102 ? 51.937 35.057  6.416   1.00 35.39 ? 103 LEU A CB  1 
ATOM   816  C  CG  . LEU A  1 102 ? 50.935 34.664  5.332   1.00 40.06 ? 103 LEU A CG  1 
ATOM   817  C  CD1 . LEU A  1 102 ? 50.143 33.456  5.748   1.00 38.49 ? 103 LEU A CD1 1 
ATOM   818  C  CD2 . LEU A  1 102 ? 49.993 35.840  5.061   1.00 38.82 ? 103 LEU A CD2 1 
ATOM   819  N  N   . GLU A  1 103 ? 54.858 34.276  5.451   1.00 35.84 ? 104 GLU A N   1 
ATOM   820  C  CA  . GLU A  1 103 ? 55.734 33.836  4.364   1.00 38.08 ? 104 GLU A CA  1 
ATOM   821  C  C   . GLU A  1 103 ? 56.594 32.635  4.769   1.00 36.91 ? 104 GLU A C   1 
ATOM   822  O  O   . GLU A  1 103 ? 56.847 31.742  3.948   1.00 34.48 ? 104 GLU A O   1 
ATOM   823  C  CB  . GLU A  1 103 ? 56.607 34.998  3.896   1.00 38.08 ? 104 GLU A CB  1 
ATOM   824  C  CG  . GLU A  1 103 ? 55.822 36.177  3.316   1.00 47.12 ? 104 GLU A CG  1 
ATOM   825  C  CD  . GLU A  1 103 ? 55.292 35.879  1.924   1.00 51.92 ? 104 GLU A CD  1 
ATOM   826  O  OE1 . GLU A  1 103 ? 55.902 35.033  1.243   1.00 61.94 ? 104 GLU A OE1 1 
ATOM   827  O  OE2 . GLU A  1 103 ? 54.303 36.502  1.489   1.00 52.63 ? 104 GLU A OE2 1 
ATOM   828  N  N   . LYS A  1 104 ? 57.041 32.584  6.029   1.00 35.12 ? 105 LYS A N   1 
ATOM   829  C  CA  . LYS A  1 104 ? 57.784 31.414  6.496   1.00 36.09 ? 105 LYS A CA  1 
ATOM   830  C  C   . LYS A  1 104 ? 56.906 30.169  6.509   1.00 33.63 ? 105 LYS A C   1 
ATOM   831  O  O   . LYS A  1 104 ? 57.371 29.068  6.190   1.00 33.94 ? 105 LYS A O   1 
ATOM   832  C  CB  . LYS A  1 104 ? 58.364 31.685  7.882   1.00 36.29 ? 105 LYS A CB  1 
ATOM   833  C  CG  . LYS A  1 104 ? 59.747 32.316  7.821   1.00 40.01 ? 105 LYS A CG  1 
ATOM   834  C  CD  . LYS A  1 104 ? 59.983 33.262  8.959   1.00 38.50 ? 105 LYS A CD  1 
ATOM   835  C  CE  . LYS A  1 104 ? 61.374 33.108  9.526   1.00 42.93 ? 105 LYS A CE  1 
ATOM   836  N  NZ  . LYS A  1 104 ? 61.385 33.636  10.923  1.00 46.76 ? 105 LYS A NZ  1 
ATOM   837  N  N   . GLN A  1 105 ? 55.632 30.332  6.875   1.00 34.23 ? 106 GLN A N   1 
ATOM   838  C  CA  . GLN A  1 105 ? 54.671 29.233  6.864   1.00 38.75 ? 106 GLN A CA  1 
ATOM   839  C  C   . GLN A  1 105 ? 54.478 28.684  5.451   1.00 35.21 ? 106 GLN A C   1 
ATOM   840  O  O   . GLN A  1 105 ? 54.451 27.466  5.245   1.00 34.51 ? 106 GLN A O   1 
ATOM   841  C  CB  . GLN A  1 105 ? 53.348 29.743  7.448   1.00 40.44 ? 106 GLN A CB  1 
ATOM   842  C  CG  . GLN A  1 105 ? 52.294 28.709  7.797   1.00 54.53 ? 106 GLN A CG  1 
ATOM   843  C  CD  . GLN A  1 105 ? 50.928 29.355  8.134   1.00 65.15 ? 106 GLN A CD  1 
ATOM   844  O  OE1 . GLN A  1 105 ? 50.861 30.419  8.760   1.00 65.52 ? 106 GLN A OE1 1 
ATOM   845  N  NE2 . GLN A  1 105 ? 49.841 28.704  7.712   1.00 62.95 ? 106 GLN A NE2 1 
ATOM   846  N  N   . VAL A  1 106 ? 54.350 29.574  4.465   1.00 33.58 ? 107 VAL A N   1 
ATOM   847  C  CA  . VAL A  1 106 ? 54.229 29.163  3.068   1.00 32.53 ? 107 VAL A CA  1 
ATOM   848  C  C   . VAL A  1 106 ? 55.500 28.461  2.602   1.00 35.04 ? 107 VAL A C   1 
ATOM   849  O  O   . VAL A  1 106 ? 55.445 27.428  1.921   1.00 34.25 ? 107 VAL A O   1 
ATOM   850  C  CB  . VAL A  1 106 ? 53.905 30.387  2.192   1.00 38.08 ? 107 VAL A CB  1 
ATOM   851  C  CG1 . VAL A  1 106 ? 54.037 30.049  0.702   1.00 41.74 ? 107 VAL A CG1 1 
ATOM   852  C  CG2 . VAL A  1 106 ? 52.513 30.925  2.518   1.00 34.70 ? 107 VAL A CG2 1 
ATOM   853  N  N   . ASN A  1 107 ? 56.664 29.009  2.956   1.00 33.21 ? 108 ASN A N   1 
ATOM   854  C  CA  . ASN A  1 107 ? 57.926 28.371  2.600   1.00 35.07 ? 108 ASN A CA  1 
ATOM   855  C  C   . ASN A  1 107 ? 58.005 26.955  3.164   1.00 33.94 ? 108 ASN A C   1 
ATOM   856  O  O   . ASN A  1 107 ? 58.352 26.011  2.447   1.00 34.87 ? 108 ASN A O   1 
ATOM   857  C  CB  . ASN A  1 107 ? 59.106 29.218  3.093   1.00 32.28 ? 108 ASN A CB  1 
ATOM   858  C  CG  . ASN A  1 107 ? 60.429 28.848  2.418   1.00 31.64 ? 108 ASN A CG  1 
ATOM   859  O  OD1 . ASN A  1 107 ? 61.483 28.831  3.057   1.00 42.71 ? 108 ASN A OD1 1 
ATOM   860  N  ND2 . ASN A  1 107 ? 60.378 28.568  1.124   1.00 31.69 ? 108 ASN A ND2 1 
ATOM   861  N  N   . GLN A  1 108 ? 57.686 26.784  4.449   1.00 33.08 ? 109 GLN A N   1 
ATOM   862  C  CA  . GLN A  1 108 ? 57.757 25.452  5.045   1.00 33.73 ? 109 GLN A CA  1 
ATOM   863  C  C   . GLN A  1 108 ? 56.845 24.477  4.306   1.00 39.02 ? 109 GLN A C   1 
ATOM   864  O  O   . GLN A  1 108 ? 57.239 23.343  4.001   1.00 38.80 ? 109 GLN A O   1 
ATOM   865  C  CB  . GLN A  1 108 ? 57.396 25.514  6.534   1.00 35.70 ? 109 GLN A CB  1 
ATOM   866  C  CG  . GLN A  1 108 ? 57.653 24.200  7.289   1.00 47.54 ? 109 GLN A CG  1 
ATOM   867  C  CD  . GLN A  1 108 ? 59.088 23.640  7.085   1.00 60.66 ? 109 GLN A CD  1 
ATOM   868  O  OE1 . GLN A  1 108 ? 60.097 24.330  7.329   1.00 57.67 ? 109 GLN A OE1 1 
ATOM   869  N  NE2 . GLN A  1 108 ? 59.172 22.392  6.610   1.00 54.30 ? 109 GLN A NE2 1 
ATOM   870  N  N   . SER A  1 109 ? 55.629 24.912  3.991   1.00 32.30 ? 110 SER A N   1 
ATOM   871  C  CA  . SER A  1 109 ? 54.708 24.073  3.228   1.00 38.37 ? 110 SER A CA  1 
ATOM   872  C  C   . SER A  1 109 ? 55.247 23.775  1.822   1.00 35.95 ? 110 SER A C   1 
ATOM   873  O  O   . SER A  1 109 ? 55.131 22.647  1.329   1.00 33.67 ? 110 SER A O   1 
ATOM   874  C  CB  . SER A  1 109 ? 53.345 24.767  3.180   1.00 33.70 ? 110 SER A CB  1 
ATOM   875  O  OG  . SER A  1 109 ? 52.464 24.114  2.307   1.00 40.89 ? 110 SER A OG  1 
ATOM   876  N  N   . LEU A  1 110 ? 55.870 24.765  1.169   1.00 34.06 ? 111 LEU A N   1 
ATOM   877  C  CA  . LEU A  1 110 ? 56.483 24.502  -0.133  1.00 31.74 ? 111 LEU A CA  1 
ATOM   878  C  C   . LEU A  1 110 ? 57.640 23.509  -0.024  1.00 33.95 ? 111 LEU A C   1 
ATOM   879  O  O   . LEU A  1 110 ? 57.819 22.661  -0.909  1.00 31.83 ? 111 LEU A O   1 
ATOM   880  C  CB  . LEU A  1 110 ? 56.951 25.811  -0.770  1.00 35.15 ? 111 LEU A CB  1 
ATOM   881  C  CG  . LEU A  1 110 ? 55.808 26.673  -1.300  1.00 40.60 ? 111 LEU A CG  1 
ATOM   882  C  CD1 . LEU A  1 110 ? 56.310 28.060  -1.634  1.00 41.24 ? 111 LEU A CD1 1 
ATOM   883  C  CD2 . LEU A  1 110 ? 55.155 26.012  -2.523  1.00 35.13 ? 111 LEU A CD2 1 
ATOM   884  N  N   . LEU A  1 111 ? 58.440 23.594  1.051   1.00 32.22 ? 112 LEU A N   1 
ATOM   885  C  CA  . LEU A  1 111 ? 59.539 22.643  1.220   1.00 33.95 ? 112 LEU A CA  1 
ATOM   886  C  C   . LEU A  1 111 ? 59.019 21.236  1.503   1.00 37.05 ? 112 LEU A C   1 
ATOM   887  O  O   . LEU A  1 111 ? 59.607 20.252  1.035   1.00 37.79 ? 112 LEU A O   1 
ATOM   888  C  CB  . LEU A  1 111 ? 60.482 23.098  2.332   1.00 32.72 ? 112 LEU A CB  1 
ATOM   889  C  CG  . LEU A  1 111 ? 61.286 24.372  2.052   1.00 37.64 ? 112 LEU A CG  1 
ATOM   890  C  CD1 . LEU A  1 111 ? 62.024 24.831  3.303   1.00 36.26 ? 112 LEU A CD1 1 
ATOM   891  C  CD2 . LEU A  1 111 ? 62.254 24.131  0.907   1.00 36.99 ? 112 LEU A CD2 1 
ATOM   892  N  N   . GLU A  1 112 ? 57.917 21.121  2.257   1.00 34.73 ? 113 GLU A N   1 
ATOM   893  C  CA  . GLU A  1 112 ? 57.275 19.820  2.462   1.00 37.93 ? 113 GLU A CA  1 
ATOM   894  C  C   . GLU A  1 112 ? 56.878 19.194  1.134   1.00 39.37 ? 113 GLU A C   1 
ATOM   895  O  O   . GLU A  1 112 ? 57.106 18.002  0.906   1.00 39.92 ? 113 GLU A O   1 
ATOM   896  C  CB  . GLU A  1 112 ? 56.033 19.967  3.344   1.00 34.88 ? 113 GLU A CB  1 
ATOM   897  C  CG  . GLU A  1 112 ? 56.254 19.730  4.844   1.00 50.86 ? 113 GLU A CG  1 
ATOM   898  C  CD  . GLU A  1 112 ? 55.105 20.280  5.729   1.00 60.19 ? 113 GLU A CD  1 
ATOM   899  O  OE1 . GLU A  1 112 ? 53.915 20.139  5.353   1.00 65.00 ? 113 GLU A OE1 1 
ATOM   900  O  OE2 . GLU A  1 112 ? 55.391 20.862  6.803   1.00 62.00 ? 113 GLU A OE2 1 
ATOM   901  N  N   . LEU A  1 113 ? 56.283 19.996  0.246   1.00 38.07 ? 114 LEU A N   1 
ATOM   902  C  CA  . LEU A  1 113 ? 55.810 19.509  -1.049  1.00 37.73 ? 114 LEU A CA  1 
ATOM   903  C  C   . LEU A  1 113 ? 56.967 19.108  -1.958  1.00 40.13 ? 114 LEU A C   1 
ATOM   904  O  O   . LEU A  1 113 ? 56.843 18.151  -2.735  1.00 37.38 ? 114 LEU A O   1 
ATOM   905  C  CB  . LEU A  1 113 ? 54.943 20.592  -1.701  1.00 38.69 ? 114 LEU A CB  1 
ATOM   906  C  CG  . LEU A  1 113 ? 54.490 20.485  -3.155  1.00 46.09 ? 114 LEU A CG  1 
ATOM   907  C  CD1 . LEU A  1 113 ? 53.738 19.182  -3.407  1.00 46.95 ? 114 LEU A CD1 1 
ATOM   908  C  CD2 . LEU A  1 113 ? 53.631 21.693  -3.515  1.00 42.40 ? 114 LEU A CD2 1 
ATOM   909  N  N   . HIS A  1 114 ? 58.101 19.814  -1.871  1.00 37.44 ? 115 HIS A N   1 
ATOM   910  C  CA  . HIS A  1 114 ? 59.277 19.389  -2.627  1.00 40.52 ? 115 HIS A CA  1 
ATOM   911  C  C   . HIS A  1 114 ? 59.769 18.025  -2.155  1.00 38.16 ? 115 HIS A C   1 
ATOM   912  O  O   . HIS A  1 114 ? 60.152 17.179  -2.972  1.00 36.64 ? 115 HIS A O   1 
ATOM   913  C  CB  . HIS A  1 114 ? 60.382 20.436  -2.515  1.00 33.18 ? 115 HIS A CB  1 
ATOM   914  C  CG  . HIS A  1 114 ? 61.558 20.175  -3.399  1.00 35.31 ? 115 HIS A CG  1 
ATOM   915  N  ND1 . HIS A  1 114 ? 62.539 19.261  -3.079  1.00 34.25 ? 115 HIS A ND1 1 
ATOM   916  C  CD2 . HIS A  1 114 ? 61.925 20.727  -4.581  1.00 34.88 ? 115 HIS A CD2 1 
ATOM   917  C  CE1 . HIS A  1 114 ? 63.453 19.251  -4.034  1.00 35.38 ? 115 HIS A CE1 1 
ATOM   918  N  NE2 . HIS A  1 114 ? 63.104 20.133  -4.956  1.00 35.44 ? 115 HIS A NE2 1 
ATOM   919  N  N   . SER A  1 115 ? 59.752 17.791  -0.842  1.00 37.60 ? 116 SER A N   1 
ATOM   920  C  CA  . SER A  1 115 ? 60.136 16.485  -0.317  1.00 42.39 ? 116 SER A CA  1 
ATOM   921  C  C   . SER A  1 115 ? 59.168 15.391  -0.768  1.00 37.43 ? 116 SER A C   1 
ATOM   922  O  O   . SER A  1 115 ? 59.594 14.293  -1.142  1.00 42.85 ? 116 SER A O   1 
ATOM   923  C  CB  . SER A  1 115 ? 60.223 16.551  1.208   1.00 39.81 ? 116 SER A CB  1 
ATOM   924  O  OG  . SER A  1 115 ? 59.879 15.306  1.785   1.00 48.67 ? 116 SER A OG  1 
ATOM   925  N  N   . THR A  1 116 ? 57.865 15.669  -0.734  1.00 40.04 ? 117 THR A N   1 
ATOM   926  C  CA  . THR A  1 116 ? 56.857 14.762  -1.284  1.00 43.18 ? 117 THR A CA  1 
ATOM   927  C  C   . THR A  1 116 ? 57.159 14.409  -2.742  1.00 45.59 ? 117 THR A C   1 
ATOM   928  O  O   . THR A  1 116 ? 57.253 13.233  -3.112  1.00 45.66 ? 117 THR A O   1 
ATOM   929  C  CB  . THR A  1 116 ? 55.473 15.418  -1.172  1.00 44.20 ? 117 THR A CB  1 
ATOM   930  O  OG1 . THR A  1 116 ? 55.049 15.439  0.200   1.00 48.50 ? 117 THR A OG1 1 
ATOM   931  C  CG2 . THR A  1 116 ? 54.429 14.694  -2.026  1.00 47.00 ? 117 THR A CG2 1 
ATOM   932  N  N   . ALA A  1 117 ? 57.315 15.431  -3.587  1.00 42.97 ? 118 ALA A N   1 
ATOM   933  C  CA  . ALA A  1 117 ? 57.571 15.195  -5.006  1.00 38.73 ? 118 ALA A CA  1 
ATOM   934  C  C   . ALA A  1 117 ? 58.889 14.457  -5.220  1.00 41.92 ? 118 ALA A C   1 
ATOM   935  O  O   . ALA A  1 117 ? 59.004 13.611  -6.116  1.00 39.53 ? 118 ALA A O   1 
ATOM   936  C  CB  . ALA A  1 117 ? 57.592 16.522  -5.758  1.00 36.60 ? 118 ALA A CB  1 
ATOM   937  N  N   . SER A  1 118 ? 59.905 14.786  -4.430  1.00 37.54 ? 119 SER A N   1 
ATOM   938  C  CA  . SER A  1 118 ? 61.175 14.096  -4.579  1.00 43.65 ? 119 SER A CA  1 
ATOM   939  C  C   . SER A  1 118 ? 61.059 12.629  -4.159  1.00 45.50 ? 119 SER A C   1 
ATOM   940  O  O   . SER A  1 118 ? 61.714 11.761  -4.753  1.00 45.57 ? 119 SER A O   1 
ATOM   941  C  CB  . SER A  1 118 ? 62.250 14.839  -3.782  1.00 40.68 ? 119 SER A CB  1 
ATOM   942  O  OG  . SER A  1 118 ? 63.312 13.971  -3.441  1.00 57.98 ? 119 SER A OG  1 
ATOM   943  N  N   . GLY A  1 119 ? 60.207 12.331  -3.171  1.00 44.42 ? 120 GLY A N   1 
ATOM   944  C  CA  . GLY A  1 119 ? 60.041 10.951  -2.735  1.00 45.42 ? 120 GLY A CA  1 
ATOM   945  C  C   . GLY A  1 119 ? 59.395 10.071  -3.792  1.00 46.89 ? 120 GLY A C   1 
ATOM   946  O  O   . GLY A  1 119 ? 59.774 8.909   -3.962  1.00 47.43 ? 120 GLY A O   1 
ATOM   947  N  N   . ASN A  1 120 ? 58.421 10.610  -4.518  1.00 43.25 ? 121 ASN A N   1 
ATOM   948  C  CA  . ASN A  1 120 ? 57.785 9.896   -5.618  1.00 46.60 ? 121 ASN A CA  1 
ATOM   949  C  C   . ASN A  1 120 ? 58.530 10.061  -6.948  1.00 43.90 ? 121 ASN A C   1 
ATOM   950  O  O   . ASN A  1 120 ? 57.978 9.711   -7.992  1.00 45.63 ? 121 ASN A O   1 
ATOM   951  C  CB  . ASN A  1 120 ? 56.331 10.363  -5.759  1.00 49.65 ? 121 ASN A CB  1 
ATOM   952  C  CG  . ASN A  1 120 ? 55.506 10.112  -4.499  1.00 50.72 ? 121 ASN A CG  1 
ATOM   953  O  OD1 . ASN A  1 120 ? 55.512 9.012   -3.939  1.00 54.71 ? 121 ASN A OD1 1 
ATOM   954  N  ND2 . ASN A  1 120 ? 54.789 11.135  -4.053  1.00 53.89 ? 121 ASN A ND2 1 
ATOM   955  N  N   . ASN A  1 121 ? 59.756 10.590  -6.924  1.00 42.07 ? 122 ASN A N   1 
ATOM   956  C  CA  . ASN A  1 121 ? 60.574 10.875  -8.111  1.00 44.19 ? 122 ASN A CA  1 
ATOM   957  C  C   . ASN A  1 121 ? 59.769 11.581  -9.216  1.00 40.56 ? 122 ASN A C   1 
ATOM   958  O  O   . ASN A  1 121 ? 59.596 11.081  -10.329 1.00 38.08 ? 122 ASN A O   1 
ATOM   959  C  CB  . ASN A  1 121 ? 61.239 9.597   -8.635  1.00 44.71 ? 122 ASN A CB  1 
ATOM   960  C  CG  . ASN A  1 121 ? 62.070 8.883   -7.560  1.00 48.49 ? 122 ASN A CG  1 
ATOM   961  O  OD1 . ASN A  1 121 ? 63.195 9.294   -7.242  1.00 47.71 ? 122 ASN A OD1 1 
ATOM   962  N  ND2 . ASN A  1 121 ? 61.504 7.825   -6.982  1.00 41.70 ? 122 ASN A ND2 1 
ATOM   963  N  N   . ASP A  1 122 ? 59.303 12.787  -8.889  1.00 38.15 ? 123 ASP A N   1 
ATOM   964  C  CA  . ASP A  1 122 ? 58.654 13.671  -9.852  1.00 36.38 ? 123 ASP A CA  1 
ATOM   965  C  C   . ASP A  1 122 ? 59.561 14.870  -10.124 1.00 34.37 ? 123 ASP A C   1 
ATOM   966  O  O   . ASP A  1 122 ? 59.402 15.931  -9.502  1.00 34.81 ? 123 ASP A O   1 
ATOM   967  C  CB  . ASP A  1 122 ? 57.287 14.124  -9.334  1.00 37.56 ? 123 ASP A CB  1 
ATOM   968  C  CG  . ASP A  1 122 ? 56.399 14.712  -10.441 1.00 44.86 ? 123 ASP A CG  1 
ATOM   969  O  OD1 . ASP A  1 122 ? 56.943 15.180  -11.479 1.00 43.12 ? 123 ASP A OD1 1 
ATOM   970  O  OD2 . ASP A  1 122 ? 55.156 14.732  -10.256 1.00 44.83 ? 123 ASP A OD2 1 
ATOM   971  N  N   . PRO A  1 123 ? 60.538 14.735  -11.027 1.00 37.20 ? 124 PRO A N   1 
ATOM   972  C  CA  . PRO A  1 123 ? 61.463 15.851  -11.266 1.00 33.29 ? 124 PRO A CA  1 
ATOM   973  C  C   . PRO A  1 123 ? 60.806 17.049  -11.923 1.00 35.70 ? 124 PRO A C   1 
ATOM   974  O  O   . PRO A  1 123 ? 61.321 18.166  -11.787 1.00 35.98 ? 124 PRO A O   1 
ATOM   975  C  CB  . PRO A  1 123 ? 62.537 15.232  -12.171 1.00 38.35 ? 124 PRO A CB  1 
ATOM   976  C  CG  . PRO A  1 123 ? 61.863 14.080  -12.832 1.00 34.80 ? 124 PRO A CG  1 
ATOM   977  C  CD  . PRO A  1 123 ? 60.889 13.543  -11.821 1.00 34.32 ? 124 PRO A CD  1 
ATOM   978  N  N   . HIS A  1 124 ? 59.696 16.857  -12.634 1.00 33.12 ? 125 HIS A N   1 
ATOM   979  C  CA  . HIS A  1 124 ? 58.999 17.999  -13.215 1.00 36.71 ? 125 HIS A CA  1 
ATOM   980  C  C   . HIS A  1 124 ? 58.390 18.873  -12.123 1.00 38.37 ? 125 HIS A C   1 
ATOM   981  O  O   . HIS A  1 124 ? 58.450 20.105  -12.202 1.00 34.34 ? 125 HIS A O   1 
ATOM   982  C  CB  . HIS A  1 124 ? 57.934 17.510  -14.193 1.00 34.64 ? 125 HIS A CB  1 
ATOM   983  C  CG  . HIS A  1 124 ? 57.345 18.592  -15.039 1.00 42.30 ? 125 HIS A CG  1 
ATOM   984  N  ND1 . HIS A  1 124 ? 56.237 19.318  -14.653 1.00 40.29 ? 125 HIS A ND1 1 
ATOM   985  C  CD2 . HIS A  1 124 ? 57.698 19.063  -16.259 1.00 41.65 ? 125 HIS A CD2 1 
ATOM   986  C  CE1 . HIS A  1 124 ? 55.942 20.197  -15.593 1.00 37.01 ? 125 HIS A CE1 1 
ATOM   987  N  NE2 . HIS A  1 124 ? 56.813 20.063  -16.577 1.00 39.74 ? 125 HIS A NE2 1 
ATOM   988  N  N   . LEU A  1 125 ? 57.825 18.251  -11.079 1.00 35.50 ? 126 LEU A N   1 
ATOM   989  C  CA  . LEU A  1 125 ? 57.264 19.029  -9.978  1.00 35.01 ? 126 LEU A CA  1 
ATOM   990  C  C   . LEU A  1 125 ? 58.360 19.677  -9.134  1.00 35.66 ? 126 LEU A C   1 
ATOM   991  O  O   . LEU A  1 125 ? 58.222 20.833  -8.715  1.00 33.75 ? 126 LEU A O   1 
ATOM   992  C  CB  . LEU A  1 125 ? 56.368 18.147  -9.110  1.00 37.77 ? 126 LEU A CB  1 
ATOM   993  C  CG  . LEU A  1 125 ? 55.707 18.779  -7.875  1.00 37.14 ? 126 LEU A CG  1 
ATOM   994  C  CD1 . LEU A  1 125 ? 54.961 20.078  -8.207  1.00 30.60 ? 126 LEU A CD1 1 
ATOM   995  C  CD2 . LEU A  1 125 ? 54.742 17.782  -7.247  1.00 38.72 ? 126 LEU A CD2 1 
ATOM   996  N  N   . THR A  1 126 ? 59.445 18.955  -8.847  1.00 33.87 ? 127 THR A N   1 
ATOM   997  C  CA  . THR A  1 126 ? 60.506 19.564  -8.046  1.00 38.12 ? 127 THR A CA  1 
ATOM   998  C  C   . THR A  1 126 ? 61.105 20.761  -8.770  1.00 36.32 ? 127 THR A C   1 
ATOM   999  O  O   . THR A  1 126 ? 61.446 21.769  -8.140  1.00 38.94 ? 127 THR A O   1 
ATOM   1000 C  CB  . THR A  1 126 ? 61.594 18.543  -7.696  1.00 34.31 ? 127 THR A CB  1 
ATOM   1001 O  OG1 . THR A  1 126 ? 62.097 17.943  -8.894  1.00 37.61 ? 127 THR A OG1 1 
ATOM   1002 C  CG2 . THR A  1 126 ? 61.031 17.457  -6.803  1.00 37.76 ? 127 THR A CG2 1 
ATOM   1003 N  N   . LYS A  1 127 ? 61.207 20.680  -10.098 1.00 33.46 ? 128 LYS A N   1 
ATOM   1004 C  CA  . LYS A  1 127 ? 61.720 21.802  -10.877 1.00 36.97 ? 128 LYS A CA  1 
ATOM   1005 C  C   . LYS A  1 127 ? 60.783 23.004  -10.817 1.00 36.91 ? 128 LYS A C   1 
ATOM   1006 O  O   . LYS A  1 127 ? 61.229 24.142  -10.622 1.00 38.81 ? 128 LYS A O   1 
ATOM   1007 C  CB  . LYS A  1 127 ? 61.941 21.385  -12.332 1.00 42.24 ? 128 LYS A CB  1 
ATOM   1008 C  CG  . LYS A  1 127 ? 61.893 22.583  -13.244 1.00 46.67 ? 128 LYS A CG  1 
ATOM   1009 C  CD  . LYS A  1 127 ? 61.908 22.236  -14.704 1.00 52.57 ? 128 LYS A CD  1 
ATOM   1010 C  CE  . LYS A  1 127 ? 62.331 23.478  -15.475 1.00 57.33 ? 128 LYS A CE  1 
ATOM   1011 N  NZ  . LYS A  1 127 ? 63.816 23.571  -15.552 1.00 66.44 ? 128 LYS A NZ  1 
ATOM   1012 N  N   . LEU A  1 128 ? 59.485 22.781  -11.029 1.00 35.04 ? 129 LEU A N   1 
ATOM   1013 C  CA  . LEU A  1 128 ? 58.519 23.864  -10.860 1.00 34.86 ? 129 LEU A CA  1 
ATOM   1014 C  C   . LEU A  1 128 ? 58.675 24.540  -9.502  1.00 38.62 ? 129 LEU A C   1 
ATOM   1015 O  O   . LEU A  1 128 ? 58.682 25.773  -9.409  1.00 37.41 ? 129 LEU A O   1 
ATOM   1016 C  CB  . LEU A  1 128 ? 57.094 23.339  -11.017 1.00 32.40 ? 129 LEU A CB  1 
ATOM   1017 C  CG  . LEU A  1 128 ? 56.026 24.352  -10.578 1.00 36.88 ? 129 LEU A CG  1 
ATOM   1018 C  CD1 . LEU A  1 128 ? 55.684 25.290  -11.739 1.00 31.15 ? 129 LEU A CD1 1 
ATOM   1019 C  CD2 . LEU A  1 128 ? 54.780 23.679  -10.027 1.00 32.28 ? 129 LEU A CD2 1 
ATOM   1020 N  N   . LEU A  1 129 ? 58.807 23.751  -8.433  1.00 32.54 ? 130 LEU A N   1 
ATOM   1021 C  CA  . LEU A  1 129 ? 58.900 24.353  -7.108  1.00 37.18 ? 130 LEU A CA  1 
ATOM   1022 C  C   . LEU A  1 129 ? 60.175 25.178  -6.962  1.00 39.86 ? 130 LEU A C   1 
ATOM   1023 O  O   . LEU A  1 129 ? 60.143 26.267  -6.379  1.00 40.37 ? 130 LEU A O   1 
ATOM   1024 C  CB  . LEU A  1 129 ? 58.809 23.276  -6.026  1.00 30.92 ? 130 LEU A CB  1 
ATOM   1025 C  CG  . LEU A  1 129 ? 57.479 22.511  -5.965  1.00 38.36 ? 130 LEU A CG  1 
ATOM   1026 C  CD1 . LEU A  1 129 ? 57.562 21.346  -4.990  1.00 33.90 ? 130 LEU A CD1 1 
ATOM   1027 C  CD2 . LEU A  1 129 ? 56.313 23.425  -5.610  1.00 37.74 ? 130 LEU A CD2 1 
ATOM   1028 N  N   . GLU A  1 130 ? 61.300 24.698  -7.516  1.00 39.58 ? 131 GLU A N   1 
ATOM   1029 C  CA  . GLU A  1 130 ? 62.564 25.424  -7.386  1.00 43.82 ? 131 GLU A CA  1 
ATOM   1030 C  C   . GLU A  1 130 ? 62.560 26.718  -8.197  1.00 43.16 ? 131 GLU A C   1 
ATOM   1031 O  O   . GLU A  1 130 ? 63.049 27.757  -7.730  1.00 47.80 ? 131 GLU A O   1 
ATOM   1032 C  CB  . GLU A  1 130 ? 63.739 24.540  -7.824  1.00 40.13 ? 131 GLU A CB  1 
ATOM   1033 C  CG  . GLU A  1 130 ? 64.138 23.475  -6.821  1.00 43.17 ? 131 GLU A CG  1 
ATOM   1034 C  CD  . GLU A  1 130 ? 64.942 22.334  -7.447  1.00 51.22 ? 131 GLU A CD  1 
ATOM   1035 O  OE1 . GLU A  1 130 ? 65.671 22.584  -8.440  1.00 57.40 ? 131 GLU A OE1 1 
ATOM   1036 O  OE2 . GLU A  1 130 ? 64.842 21.186  -6.945  1.00 43.53 ? 131 GLU A OE2 1 
ATOM   1037 N  N   . ASP A  1 131 ? 62.025 26.675  -9.416  1.00 42.68 ? 132 ASP A N   1 
ATOM   1038 C  CA  . ASP A  1 131 ? 62.124 27.824  -10.312 1.00 49.58 ? 132 ASP A CA  1 
ATOM   1039 C  C   . ASP A  1 131 ? 61.110 28.915  -9.977  1.00 47.69 ? 132 ASP A C   1 
ATOM   1040 O  O   . ASP A  1 131 ? 61.432 30.103  -10.071 1.00 49.99 ? 132 ASP A O   1 
ATOM   1041 C  CB  . ASP A  1 131 ? 61.957 27.373  -11.767 1.00 46.87 ? 132 ASP A CB  1 
ATOM   1042 C  CG  . ASP A  1 131 ? 63.260 26.893  -12.383 1.00 63.96 ? 132 ASP A CG  1 
ATOM   1043 O  OD1 . ASP A  1 131 ? 63.623 27.380  -13.480 1.00 72.43 ? 132 ASP A OD1 1 
ATOM   1044 O  OD2 . ASP A  1 131 ? 63.934 26.046  -11.760 1.00 64.85 ? 132 ASP A OD2 1 
ATOM   1045 N  N   . GLU A  1 132 ? 59.893 28.537  -9.574  1.00 45.23 ? 133 GLU A N   1 
ATOM   1046 C  CA  . GLU A  1 132 ? 58.768 29.465  -9.493  1.00 44.36 ? 133 GLU A CA  1 
ATOM   1047 C  C   . GLU A  1 132 ? 58.334 29.802  -8.076  1.00 48.59 ? 133 GLU A C   1 
ATOM   1048 O  O   . GLU A  1 132 ? 57.556 30.746  -7.899  1.00 49.98 ? 133 GLU A O   1 
ATOM   1049 C  CB  . GLU A  1 132 ? 57.547 28.900  -10.241 1.00 43.62 ? 133 GLU A CB  1 
ATOM   1050 C  CG  . GLU A  1 132 ? 57.849 28.398  -11.647 1.00 53.85 ? 133 GLU A CG  1 
ATOM   1051 C  CD  . GLU A  1 132 ? 57.605 29.466  -12.697 1.00 65.86 ? 133 GLU A CD  1 
ATOM   1052 O  OE1 . GLU A  1 132 ? 58.060 29.281  -13.848 1.00 73.46 ? 133 GLU A OE1 1 
ATOM   1053 O  OE2 . GLU A  1 132 ? 56.957 30.491  -12.365 1.00 70.50 ? 133 GLU A OE2 1 
ATOM   1054 N  N   . TYR A  1 133 ? 58.779 29.052  -7.071  1.00 42.26 ? 134 TYR A N   1 
ATOM   1055 C  CA  . TYR A  1 133 ? 58.272 29.292  -5.727  1.00 41.99 ? 134 TYR A CA  1 
ATOM   1056 C  C   . TYR A  1 133 ? 59.388 29.444  -4.705  1.00 41.19 ? 134 TYR A C   1 
ATOM   1057 O  O   . TYR A  1 133 ? 59.434 30.443  -3.980  1.00 44.65 ? 134 TYR A O   1 
ATOM   1058 C  CB  . TYR A  1 133 ? 57.318 28.171  -5.330  1.00 40.75 ? 134 TYR A CB  1 
ATOM   1059 C  CG  . TYR A  1 133 ? 56.057 28.192  -6.162  1.00 38.83 ? 134 TYR A CG  1 
ATOM   1060 C  CD1 . TYR A  1 133 ? 54.985 28.988  -5.803  1.00 38.21 ? 134 TYR A CD1 1 
ATOM   1061 C  CD2 . TYR A  1 133 ? 55.956 27.442  -7.327  1.00 36.13 ? 134 TYR A CD2 1 
ATOM   1062 C  CE1 . TYR A  1 133 ? 53.836 29.028  -6.578  1.00 41.94 ? 134 TYR A CE1 1 
ATOM   1063 C  CE2 . TYR A  1 133 ? 54.820 27.467  -8.104  1.00 36.37 ? 134 TYR A CE2 1 
ATOM   1064 C  CZ  . TYR A  1 133 ? 53.763 28.262  -7.726  1.00 38.98 ? 134 TYR A CZ  1 
ATOM   1065 O  OH  . TYR A  1 133 ? 52.635 28.283  -8.489  1.00 33.61 ? 134 TYR A OH  1 
ATOM   1066 N  N   . LEU A  1 134 ? 60.305 28.479  -4.655  1.00 40.51 ? 135 LEU A N   1 
ATOM   1067 C  CA  . LEU A  1 134 ? 61.275 28.462  -3.569  1.00 40.81 ? 135 LEU A CA  1 
ATOM   1068 C  C   . LEU A  1 134 ? 62.158 29.697  -3.597  1.00 40.19 ? 135 LEU A C   1 
ATOM   1069 O  O   . LEU A  1 134 ? 62.401 30.309  -2.552  1.00 39.77 ? 135 LEU A O   1 
ATOM   1070 C  CB  . LEU A  1 134 ? 62.110 27.193  -3.634  1.00 36.32 ? 135 LEU A CB  1 
ATOM   1071 C  CG  . LEU A  1 134 ? 61.285 25.972  -3.228  1.00 38.69 ? 135 LEU A CG  1 
ATOM   1072 C  CD1 . LEU A  1 134 ? 62.159 24.724  -3.214  1.00 41.09 ? 135 LEU A CD1 1 
ATOM   1073 C  CD2 . LEU A  1 134 ? 60.651 26.199  -1.861  1.00 40.59 ? 135 LEU A CD2 1 
ATOM   1074 N  N   . GLU A  1 135 ? 62.623 30.098  -4.786  1.00 40.31 ? 136 GLU A N   1 
ATOM   1075 C  CA  . GLU A  1 135 ? 63.525 31.245  -4.876  1.00 43.34 ? 136 GLU A CA  1 
ATOM   1076 C  C   . GLU A  1 135 ? 62.826 32.543  -4.477  1.00 48.35 ? 136 GLU A C   1 
ATOM   1077 O  O   . GLU A  1 135 ? 63.412 33.381  -3.776  1.00 41.70 ? 136 GLU A O   1 
ATOM   1078 C  CB  . GLU A  1 135 ? 64.104 31.351  -6.283  1.00 47.88 ? 136 GLU A CB  1 
ATOM   1079 C  CG  . GLU A  1 135 ? 65.622 31.515  -6.286  1.00 62.51 ? 136 GLU A CG  1 
ATOM   1080 C  CD  . GLU A  1 135 ? 66.154 32.154  -7.564  1.00 70.84 ? 136 GLU A CD  1 
ATOM   1081 O  OE1 . GLU A  1 135 ? 65.477 32.039  -8.612  1.00 74.43 ? 136 GLU A OE1 1 
ATOM   1082 O  OE2 . GLU A  1 135 ? 67.242 32.780  -7.514  1.00 73.17 ? 136 GLU A OE2 1 
ATOM   1083 N  N   . GLU A  1 136 ? 61.562 32.723  -4.880  1.00 46.85 ? 137 GLU A N   1 
ATOM   1084 C  CA  . GLU A  1 136 ? 60.888 33.961  -4.512  1.00 49.26 ? 137 GLU A CA  1 
ATOM   1085 C  C   . GLU A  1 136 ? 60.425 33.958  -3.059  1.00 43.86 ? 137 GLU A C   1 
ATOM   1086 O  O   . GLU A  1 136 ? 60.317 35.033  -2.463  1.00 43.52 ? 137 GLU A O   1 
ATOM   1087 C  CB  . GLU A  1 136 ? 59.711 34.244  -5.445  1.00 52.09 ? 137 GLU A CB  1 
ATOM   1088 C  CG  . GLU A  1 136 ? 58.598 33.240  -5.359  1.00 57.12 ? 137 GLU A CG  1 
ATOM   1089 C  CD  . GLU A  1 136 ? 57.573 33.560  -4.265  1.00 62.32 ? 137 GLU A CD  1 
ATOM   1090 O  OE1 . GLU A  1 136 ? 57.451 34.750  -3.842  1.00 66.33 ? 137 GLU A OE1 1 
ATOM   1091 O  OE2 . GLU A  1 136 ? 56.892 32.595  -3.823  1.00 61.92 ? 137 GLU A OE2 1 
ATOM   1092 N  N   . GLN A  1 137 ? 60.156 32.795  -2.461  1.00 38.43 ? 138 GLN A N   1 
ATOM   1093 C  CA  . GLN A  1 137 ? 59.844 32.805  -1.033  1.00 41.43 ? 138 GLN A CA  1 
ATOM   1094 C  C   . GLN A  1 137 ? 61.032 33.309  -0.229  1.00 38.36 ? 138 GLN A C   1 
ATOM   1095 O  O   . GLN A  1 137 ? 60.878 34.152  0.659   1.00 35.84 ? 138 GLN A O   1 
ATOM   1096 C  CB  . GLN A  1 137 ? 59.427 31.419  -0.543  1.00 39.02 ? 138 GLN A CB  1 
ATOM   1097 C  CG  . GLN A  1 137 ? 58.003 31.053  -0.888  1.00 47.30 ? 138 GLN A CG  1 
ATOM   1098 C  CD  . GLN A  1 137 ? 56.983 32.075  -0.416  1.00 45.04 ? 138 GLN A CD  1 
ATOM   1099 O  OE1 . GLN A  1 137 ? 56.903 32.399  0.776   1.00 40.56 ? 138 GLN A OE1 1 
ATOM   1100 N  NE2 . GLN A  1 137 ? 56.206 32.603  -1.356  1.00 48.43 ? 138 GLN A NE2 1 
ATOM   1101 N  N   . VAL A  1 138 ? 62.232 32.830  -0.557  1.00 36.49 ? 139 VAL A N   1 
ATOM   1102 C  CA  . VAL A  1 138 ? 63.426 33.232  0.171   1.00 35.34 ? 139 VAL A CA  1 
ATOM   1103 C  C   . VAL A  1 138 ? 63.693 34.716  -0.027  1.00 37.74 ? 139 VAL A C   1 
ATOM   1104 O  O   . VAL A  1 138 ? 64.202 35.388  0.881   1.00 35.43 ? 139 VAL A O   1 
ATOM   1105 C  CB  . VAL A  1 138 ? 64.625 32.370  -0.277  1.00 39.17 ? 139 VAL A CB  1 
ATOM   1106 C  CG1 . VAL A  1 138 ? 65.975 33.032  0.079   1.00 33.93 ? 139 VAL A CG1 1 
ATOM   1107 C  CG2 . VAL A  1 138 ? 64.528 30.974  0.303   1.00 41.85 ? 139 VAL A CG2 1 
ATOM   1108 N  N   . ASP A  1 139 ? 63.340 35.258  -1.196  1.00 36.51 ? 140 ASP A N   1 
ATOM   1109 C  CA  . ASP A  1 139 ? 63.572 36.678  -1.449  1.00 39.80 ? 140 ASP A CA  1 
ATOM   1110 C  C   . ASP A  1 139 ? 62.555 37.540  -0.716  1.00 37.70 ? 140 ASP A C   1 
ATOM   1111 O  O   . ASP A  1 139 ? 62.896 38.618  -0.220  1.00 34.20 ? 140 ASP A O   1 
ATOM   1112 C  CB  . ASP A  1 139 ? 63.538 36.964  -2.954  1.00 41.53 ? 140 ASP A CB  1 
ATOM   1113 C  CG  . ASP A  1 139 ? 64.823 36.525  -3.661  1.00 52.18 ? 140 ASP A CG  1 
ATOM   1114 O  OD1 . ASP A  1 139 ? 65.881 36.448  -2.992  1.00 59.37 ? 140 ASP A OD1 1 
ATOM   1115 O  OD2 . ASP A  1 139 ? 64.777 36.249  -4.881  1.00 53.82 ? 140 ASP A OD2 1 
ATOM   1116 N  N   . SER A  1 140 ? 61.302 37.079  -0.634  1.00 35.36 ? 141 SER A N   1 
ATOM   1117 C  CA  . SER A  1 140 ? 60.297 37.784  0.155   1.00 38.51 ? 141 SER A CA  1 
ATOM   1118 C  C   . SER A  1 140 ? 60.699 37.839  1.622   1.00 35.36 ? 141 SER A C   1 
ATOM   1119 O  O   . SER A  1 140 ? 60.656 38.899  2.254   1.00 36.10 ? 141 SER A O   1 
ATOM   1120 C  CB  . SER A  1 140 ? 58.941 37.096  0.009   1.00 39.96 ? 141 SER A CB  1 
ATOM   1121 O  OG  . SER A  1 140 ? 58.312 37.498  -1.186  1.00 50.03 ? 141 SER A OG  1 
ATOM   1122 N  N   . ILE A  1 141 ? 61.095 36.696  2.177   1.00 36.17 ? 142 ILE A N   1 
ATOM   1123 C  CA  . ILE A  1 141 ? 61.458 36.617  3.589   1.00 32.89 ? 142 ILE A CA  1 
ATOM   1124 C  C   . ILE A  1 141 ? 62.627 37.547  3.901   1.00 33.60 ? 142 ILE A C   1 
ATOM   1125 O  O   . ILE A  1 141 ? 62.611 38.265  4.906   1.00 33.32 ? 142 ILE A O   1 
ATOM   1126 C  CB  . ILE A  1 141 ? 61.764 35.151  3.951   1.00 31.07 ? 142 ILE A CB  1 
ATOM   1127 C  CG1 . ILE A  1 141 ? 60.464 34.345  3.947   1.00 31.52 ? 142 ILE A CG1 1 
ATOM   1128 C  CG2 . ILE A  1 141 ? 62.424 35.039  5.303   1.00 28.93 ? 142 ILE A CG2 1 
ATOM   1129 C  CD1 . ILE A  1 141 ? 60.685 32.866  4.007   1.00 31.34 ? 142 ILE A CD1 1 
ATOM   1130 N  N   . LYS A  1 142 ? 63.641 37.575  3.027   1.00 31.86 ? 143 LYS A N   1 
ATOM   1131 C  CA  . LYS A  1 142 ? 64.776 38.477  3.206   1.00 32.32 ? 143 LYS A CA  1 
ATOM   1132 C  C   . LYS A  1 142 ? 64.354 39.937  3.081   1.00 35.15 ? 143 LYS A C   1 
ATOM   1133 O  O   . LYS A  1 142 ? 64.810 40.788  3.855   1.00 31.18 ? 143 LYS A O   1 
ATOM   1134 C  CB  . LYS A  1 142 ? 65.875 38.155  2.186   1.00 34.70 ? 143 LYS A CB  1 
ATOM   1135 C  CG  . LYS A  1 142 ? 66.999 39.179  2.146   1.00 30.96 ? 143 LYS A CG  1 
ATOM   1136 C  CD  . LYS A  1 142 ? 67.722 39.177  3.486   1.00 38.09 ? 143 LYS A CD  1 
ATOM   1137 C  CE  . LYS A  1 142 ? 69.123 39.776  3.397   1.00 37.98 ? 143 LYS A CE  1 
ATOM   1138 N  NZ  . LYS A  1 142 ? 69.124 41.091  2.695   1.00 47.20 ? 143 LYS A NZ  1 
ATOM   1139 N  N   . LYS A  1 143 ? 63.489 40.247  2.113   1.00 29.93 ? 144 LYS A N   1 
ATOM   1140 C  CA  . LYS A  1 143 ? 63.003 41.613  1.964   1.00 36.20 ? 144 LYS A CA  1 
ATOM   1141 C  C   . LYS A  1 143 ? 62.254 42.079  3.213   1.00 34.33 ? 144 LYS A C   1 
ATOM   1142 O  O   . LYS A  1 143 ? 62.481 43.190  3.705   1.00 32.98 ? 144 LYS A O   1 
ATOM   1143 C  CB  . LYS A  1 143 ? 62.106 41.719  0.729   1.00 35.01 ? 144 LYS A CB  1 
ATOM   1144 C  CG  . LYS A  1 143 ? 61.471 43.109  0.530   1.00 39.69 ? 144 LYS A CG  1 
ATOM   1145 C  CD  . LYS A  1 143 ? 60.673 43.167  -0.771  1.00 50.53 ? 144 LYS A CD  1 
ATOM   1146 C  CE  . LYS A  1 143 ? 60.974 44.433  -1.581  1.00 62.10 ? 144 LYS A CE  1 
ATOM   1147 N  NZ  . LYS A  1 143 ? 59.743 45.023  -2.222  1.00 64.13 ? 144 LYS A NZ  1 
ATOM   1148 N  N   . ILE A  1 144 ? 61.353 41.244  3.740   1.00 32.28 ? 145 ILE A N   1 
ATOM   1149 C  CA  . ILE A  1 144 ? 60.600 41.645  4.931   1.00 33.97 ? 145 ILE A CA  1 
ATOM   1150 C  C   . ILE A  1 144 ? 61.537 41.805  6.126   1.00 35.55 ? 145 ILE A C   1 
ATOM   1151 O  O   . ILE A  1 144 ? 61.438 42.780  6.878   1.00 34.22 ? 145 ILE A O   1 
ATOM   1152 C  CB  . ILE A  1 144 ? 59.472 40.639  5.226   1.00 35.25 ? 145 ILE A CB  1 
ATOM   1153 C  CG1 . ILE A  1 144 ? 58.448 40.631  4.092   1.00 35.93 ? 145 ILE A CG1 1 
ATOM   1154 C  CG2 . ILE A  1 144 ? 58.775 40.962  6.551   1.00 32.09 ? 145 ILE A CG2 1 
ATOM   1155 C  CD1 . ILE A  1 144 ? 57.392 39.541  4.244   1.00 38.41 ? 145 ILE A CD1 1 
ATOM   1156 N  N   . GLY A  1 145 ? 62.467 40.859  6.311   1.00 32.55 ? 146 GLY A N   1 
ATOM   1157 C  CA  . GLY A  1 145 ? 63.479 41.014  7.346   1.00 36.44 ? 146 GLY A CA  1 
ATOM   1158 C  C   . GLY A  1 145 ? 64.206 42.346  7.269   1.00 37.82 ? 146 GLY A C   1 
ATOM   1159 O  O   . GLY A  1 145 ? 64.329 43.061  8.268   1.00 35.35 ? 146 GLY A O   1 
ATOM   1160 N  N   . ASP A  1 146 ? 64.690 42.702  6.075   1.00 37.27 ? 147 ASP A N   1 
ATOM   1161 C  CA  . ASP A  1 146 ? 65.340 44.001  5.881   1.00 38.45 ? 147 ASP A CA  1 
ATOM   1162 C  C   . ASP A  1 146 ? 64.430 45.140  6.321   1.00 37.30 ? 147 ASP A C   1 
ATOM   1163 O  O   . ASP A  1 146 ? 64.870 46.074  7.000   1.00 33.15 ? 147 ASP A O   1 
ATOM   1164 C  CB  . ASP A  1 146 ? 65.719 44.208  4.406   1.00 38.11 ? 147 ASP A CB  1 
ATOM   1165 C  CG  . ASP A  1 146 ? 66.866 43.307  3.936   1.00 46.75 ? 147 ASP A CG  1 
ATOM   1166 O  OD1 . ASP A  1 146 ? 67.035 43.149  2.695   1.00 54.39 ? 147 ASP A OD1 1 
ATOM   1167 O  OD2 . ASP A  1 146 ? 67.603 42.760  4.785   1.00 45.34 ? 147 ASP A OD2 1 
ATOM   1168 N  N   . MET A  1 147 ? 63.151 45.073  5.932   1.00 36.60 ? 148 MET A N   1 
ATOM   1169 C  CA  . MET A  1 147 ? 62.198 46.140  6.237   1.00 38.52 ? 148 MET A CA  1 
ATOM   1170 C  C   . MET A  1 147 ? 61.980 46.276  7.737   1.00 34.76 ? 148 MET A C   1 
ATOM   1171 O  O   . MET A  1 147 ? 61.949 47.390  8.267   1.00 32.94 ? 148 MET A O   1 
ATOM   1172 C  CB  . MET A  1 147 ? 60.868 45.863  5.528   1.00 36.77 ? 148 MET A CB  1 
ATOM   1173 C  CG  . MET A  1 147 ? 60.920 46.089  4.009   1.00 37.68 ? 148 MET A CG  1 
ATOM   1174 S  SD  . MET A  1 147 ? 59.447 45.487  3.123   1.00 44.13 ? 148 MET A SD  1 
ATOM   1175 C  CE  . MET A  1 147 ? 58.157 46.540  3.806   1.00 43.87 ? 148 MET A CE  1 
ATOM   1176 N  N   . ILE A  1 148 ? 61.832 45.149  8.440   1.00 34.08 ? 149 ILE A N   1 
ATOM   1177 C  CA  . ILE A  1 148 ? 61.637 45.196  9.888   1.00 33.14 ? 149 ILE A CA  1 
ATOM   1178 C  C   . ILE A  1 148 ? 62.813 45.886  10.567  1.00 34.94 ? 149 ILE A C   1 
ATOM   1179 O  O   . ILE A  1 148 ? 62.625 46.743  11.439  1.00 35.17 ? 149 ILE A O   1 
ATOM   1180 C  CB  . ILE A  1 148 ? 61.409 43.778  10.442  1.00 37.64 ? 149 ILE A CB  1 
ATOM   1181 C  CG1 . ILE A  1 148 ? 60.005 43.281  10.067  1.00 36.54 ? 149 ILE A CG1 1 
ATOM   1182 C  CG2 . ILE A  1 148 ? 61.627 43.757  11.944  1.00 35.49 ? 149 ILE A CG2 1 
ATOM   1183 C  CD1 . ILE A  1 148 ? 59.745 41.846  10.418  1.00 34.99 ? 149 ILE A CD1 1 
ATOM   1184 N  N   . THR A  1 149 ? 64.044 45.543  10.165  1.00 33.91 ? 150 THR A N   1 
ATOM   1185 C  CA  . THR A  1 149 ? 65.231 46.178  10.741  1.00 36.08 ? 150 THR A CA  1 
ATOM   1186 C  C   . THR A  1 149 ? 65.262 47.679  10.447  1.00 32.76 ? 150 THR A C   1 
ATOM   1187 O  O   . THR A  1 149 ? 65.599 48.487  11.322  1.00 29.80 ? 150 THR A O   1 
ATOM   1188 C  CB  . THR A  1 149 ? 66.503 45.516  10.196  1.00 35.22 ? 150 THR A CB  1 
ATOM   1189 O  OG1 . THR A  1 149 ? 66.524 44.135  10.556  1.00 34.34 ? 150 THR A OG1 1 
ATOM   1190 C  CG2 . THR A  1 149 ? 67.748 46.189  10.751  1.00 31.93 ? 150 THR A CG2 1 
ATOM   1191 N  N   . LYS A  1 150 ? 64.948 48.064  9.208   1.00 32.43 ? 151 LYS A N   1 
ATOM   1192 C  CA  . LYS A  1 150 ? 64.929 49.479  8.858   1.00 36.31 ? 151 LYS A CA  1 
ATOM   1193 C  C   . LYS A  1 150 ? 63.855 50.220  9.642   1.00 35.98 ? 151 LYS A C   1 
ATOM   1194 O  O   . LYS A  1 150 ? 64.082 51.338  10.116  1.00 36.21 ? 151 LYS A O   1 
ATOM   1195 C  CB  . LYS A  1 150 ? 64.717 49.650  7.355   1.00 31.60 ? 151 LYS A CB  1 
ATOM   1196 C  CG  . LYS A  1 150 ? 65.840 49.064  6.512   1.00 39.20 ? 151 LYS A CG  1 
ATOM   1197 C  CD  . LYS A  1 150 ? 65.917 49.729  5.135   1.00 41.37 ? 151 LYS A CD  1 
ATOM   1198 C  CE  . LYS A  1 150 ? 66.004 48.713  4.017   1.00 43.93 ? 151 LYS A CE  1 
ATOM   1199 N  NZ  . LYS A  1 150 ? 66.431 49.353  2.719   1.00 53.15 ? 151 LYS A NZ  1 
ATOM   1200 N  N   . LEU A  1 151 ? 62.685 49.605  9.811   1.00 33.68 ? 152 LEU A N   1 
ATOM   1201 C  CA  . LEU A  1 151 ? 61.605 50.280  10.516  1.00 31.86 ? 152 LEU A CA  1 
ATOM   1202 C  C   . LEU A  1 151 ? 61.936 50.459  11.995  1.00 35.83 ? 152 LEU A C   1 
ATOM   1203 O  O   . LEU A  1 151 ? 61.628 51.506  12.577  1.00 36.31 ? 152 LEU A O   1 
ATOM   1204 C  CB  . LEU A  1 151 ? 60.302 49.511  10.328  1.00 30.87 ? 152 LEU A CB  1 
ATOM   1205 C  CG  . LEU A  1 151 ? 59.048 50.096  10.976  1.00 36.32 ? 152 LEU A CG  1 
ATOM   1206 C  CD1 . LEU A  1 151 ? 58.930 51.616  10.711  1.00 32.13 ? 152 LEU A CD1 1 
ATOM   1207 C  CD2 . LEU A  1 151 ? 57.798 49.345  10.504  1.00 32.46 ? 152 LEU A CD2 1 
ATOM   1208 N  N   . LYS A  1 152 ? 62.580 49.462  12.614  1.00 33.50 ? 153 LYS A N   1 
ATOM   1209 C  CA  . LYS A  1 152 ? 63.010 49.597  14.006  1.00 37.36 ? 153 LYS A CA  1 
ATOM   1210 C  C   . LYS A  1 152 ? 64.077 50.674  14.176  1.00 37.02 ? 153 LYS A C   1 
ATOM   1211 O  O   . LYS A  1 152 ? 64.109 51.355  15.207  1.00 36.63 ? 153 LYS A O   1 
ATOM   1212 C  CB  . LYS A  1 152 ? 63.534 48.263  14.533  1.00 35.45 ? 153 LYS A CB  1 
ATOM   1213 C  CG  . LYS A  1 152 ? 62.438 47.275  14.855  1.00 33.20 ? 153 LYS A CG  1 
ATOM   1214 C  CD  . LYS A  1 152 ? 62.991 45.870  14.954  1.00 40.55 ? 153 LYS A CD  1 
ATOM   1215 C  CE  . LYS A  1 152 ? 61.978 44.945  15.627  1.00 43.71 ? 153 LYS A CE  1 
ATOM   1216 N  NZ  . LYS A  1 152 ? 62.468 43.532  15.726  1.00 47.96 ? 153 LYS A NZ  1 
ATOM   1217 N  N   . ARG A  1 153 ? 64.961 50.832  13.190  1.00 32.96 ? 154 ARG A N   1 
ATOM   1218 C  CA  . ARG A  1 153 ? 65.943 51.908  13.250  1.00 33.75 ? 154 ARG A CA  1 
ATOM   1219 C  C   . ARG A  1 153 ? 65.259 53.265  13.111  1.00 38.52 ? 154 ARG A C   1 
ATOM   1220 O  O   . ARG A  1 153 ? 65.445 54.153  13.950  1.00 37.39 ? 154 ARG A O   1 
ATOM   1221 C  CB  . ARG A  1 153 ? 67.001 51.715  12.157  1.00 35.38 ? 154 ARG A CB  1 
ATOM   1222 C  CG  . ARG A  1 153 ? 67.998 52.852  12.028  1.00 33.65 ? 154 ARG A CG  1 
ATOM   1223 C  CD  . ARG A  1 153 ? 69.041 52.593  10.939  1.00 39.13 ? 154 ARG A CD  1 
ATOM   1224 N  NE  . ARG A  1 153 ? 69.921 51.482  11.289  1.00 36.56 ? 154 ARG A NE  1 
ATOM   1225 C  CZ  . ARG A  1 153 ? 69.951 50.323  10.648  1.00 34.27 ? 154 ARG A CZ  1 
ATOM   1226 N  NH1 . ARG A  1 153 ? 69.217 50.114  9.566   1.00 30.63 ? 154 ARG A NH1 1 
ATOM   1227 N  NH2 . ARG A  1 153 ? 70.727 49.346  11.110  1.00 34.40 ? 154 ARG A NH2 1 
ATOM   1228 N  N   . ALA A  1 154 ? 64.447 53.435  12.061  1.00 37.10 ? 155 ALA A N   1 
ATOM   1229 C  CA  . ALA A  1 154 ? 63.771 54.710  11.836  1.00 38.44 ? 155 ALA A CA  1 
ATOM   1230 C  C   . ALA A  1 154 ? 62.807 55.043  12.968  1.00 39.00 ? 155 ALA A C   1 
ATOM   1231 O  O   . ALA A  1 154 ? 62.776 56.182  13.445  1.00 38.39 ? 155 ALA A O   1 
ATOM   1232 C  CB  . ALA A  1 154 ? 63.035 54.694  10.495  1.00 33.28 ? 155 ALA A CB  1 
ATOM   1233 N  N   . GLY A  1 155 ? 62.026 54.067  13.424  1.00 42.48 ? 156 GLY A N   1 
ATOM   1234 C  CA  . GLY A  1 155 ? 60.943 54.336  14.345  1.00 39.68 ? 156 GLY A CA  1 
ATOM   1235 C  C   . GLY A  1 155 ? 61.032 53.510  15.613  1.00 45.43 ? 156 GLY A C   1 
ATOM   1236 O  O   . GLY A  1 155 ? 61.942 53.684  16.436  1.00 49.58 ? 156 GLY A O   1 
ATOM   1237 N  N   . PRO A  1 156 ? 60.100 52.555  15.779  1.00 41.24 ? 157 PRO A N   1 
ATOM   1238 C  CA  . PRO A  1 156 ? 59.121 52.172  14.745  1.00 36.87 ? 157 PRO A CA  1 
ATOM   1239 C  C   . PRO A  1 156 ? 57.768 52.907  14.751  1.00 43.56 ? 157 PRO A C   1 
ATOM   1240 O  O   . PRO A  1 156 ? 56.888 52.532  13.984  1.00 42.59 ? 157 PRO A O   1 
ATOM   1241 C  CB  . PRO A  1 156 ? 58.904 50.684  15.024  1.00 39.96 ? 157 PRO A CB  1 
ATOM   1242 C  CG  . PRO A  1 156 ? 59.155 50.534  16.514  1.00 41.15 ? 157 PRO A CG  1 
ATOM   1243 C  CD  . PRO A  1 156 ? 60.155 51.597  16.904  1.00 40.58 ? 157 PRO A CD  1 
ATOM   1244 N  N   . THR A  1 157 ? 57.603 53.932  15.578  1.00 43.85 ? 158 THR A N   1 
ATOM   1245 C  CA  . THR A  1 157 ? 56.376 54.717  15.633  1.00 44.14 ? 158 THR A CA  1 
ATOM   1246 C  C   . THR A  1 157 ? 56.680 56.175  15.292  1.00 42.94 ? 158 THR A C   1 
ATOM   1247 O  O   . THR A  1 157 ? 57.838 56.586  15.187  1.00 43.80 ? 158 THR A O   1 
ATOM   1248 C  CB  . THR A  1 157 ? 55.724 54.628  17.023  1.00 43.32 ? 158 THR A CB  1 
ATOM   1249 O  OG1 . THR A  1 157 ? 56.499 55.386  17.966  1.00 47.84 ? 158 THR A OG1 1 
ATOM   1250 C  CG2 . THR A  1 157 ? 55.649 53.182  17.498  1.00 48.72 ? 158 THR A CG2 1 
ATOM   1251 N  N   . GLY A  1 158 ? 55.621 56.960  15.100  1.00 41.06 ? 159 GLY A N   1 
ATOM   1252 C  CA  . GLY A  1 158 ? 55.767 58.410  14.996  1.00 32.93 ? 159 GLY A CA  1 
ATOM   1253 C  C   . GLY A  1 158 ? 56.433 58.863  13.707  1.00 40.73 ? 159 GLY A C   1 
ATOM   1254 O  O   . GLY A  1 158 ? 56.163 58.347  12.614  1.00 36.45 ? 159 GLY A O   1 
ATOM   1255 N  N   . LEU A  1 159 ? 57.322 59.856  13.845  1.00 39.38 ? 160 LEU A N   1 
ATOM   1256 C  CA  . LEU A  1 159 ? 57.973 60.453  12.683  1.00 38.83 ? 160 LEU A CA  1 
ATOM   1257 C  C   . LEU A  1 159 ? 58.794 59.419  11.908  1.00 39.75 ? 160 LEU A C   1 
ATOM   1258 O  O   . LEU A  1 159 ? 58.825 59.441  10.668  1.00 39.17 ? 160 LEU A O   1 
ATOM   1259 C  CB  . LEU A  1 159 ? 58.849 61.633  13.124  1.00 33.00 ? 160 LEU A CB  1 
ATOM   1260 C  CG  . LEU A  1 159 ? 59.669 62.269  11.993  1.00 34.01 ? 160 LEU A CG  1 
ATOM   1261 C  CD1 . LEU A  1 159 ? 58.765 62.873  10.917  1.00 38.04 ? 160 LEU A CD1 1 
ATOM   1262 C  CD2 . LEU A  1 159 ? 60.628 63.308  12.520  1.00 41.06 ? 160 LEU A CD2 1 
ATOM   1263 N  N   . GLY A  1 160 ? 59.455 58.501  12.619  1.00 35.69 ? 161 GLY A N   1 
ATOM   1264 C  CA  . GLY A  1 160 ? 60.174 57.434  11.947  1.00 35.41 ? 161 GLY A CA  1 
ATOM   1265 C  C   . GLY A  1 160 ? 59.281 56.584  11.061  1.00 38.31 ? 161 GLY A C   1 
ATOM   1266 O  O   . GLY A  1 160 ? 59.629 56.286  9.915   1.00 33.99 ? 161 GLY A O   1 
ATOM   1267 N  N   . GLU A  1 161 ? 58.121 56.174  11.579  1.00 39.84 ? 162 GLU A N   1 
ATOM   1268 C  CA  . GLU A  1 161 ? 57.205 55.383  10.764  1.00 39.47 ? 162 GLU A CA  1 
ATOM   1269 C  C   . GLU A  1 161 ? 56.722 56.181  9.562   1.00 38.28 ? 162 GLU A C   1 
ATOM   1270 O  O   . GLU A  1 161 ? 56.583 55.639  8.459   1.00 34.66 ? 162 GLU A O   1 
ATOM   1271 C  CB  . GLU A  1 161 ? 56.016 54.919  11.604  1.00 40.17 ? 162 GLU A CB  1 
ATOM   1272 C  CG  . GLU A  1 161 ? 55.081 53.935  10.902  1.00 39.50 ? 162 GLU A CG  1 
ATOM   1273 C  CD  . GLU A  1 161 ? 53.907 53.539  11.790  1.00 49.31 ? 162 GLU A CD  1 
ATOM   1274 O  OE1 . GLU A  1 161 ? 53.369 54.432  12.499  1.00 47.16 ? 162 GLU A OE1 1 
ATOM   1275 O  OE2 . GLU A  1 161 ? 53.522 52.346  11.781  1.00 48.67 ? 162 GLU A OE2 1 
ATOM   1276 N  N   . TYR A  1 162 ? 56.470 57.477  9.759   1.00 38.01 ? 163 TYR A N   1 
ATOM   1277 C  CA  . TYR A  1 162 ? 55.992 58.317  8.668   1.00 36.00 ? 163 TYR A CA  1 
ATOM   1278 C  C   . TYR A  1 162 ? 57.031 58.402  7.559   1.00 39.91 ? 163 TYR A C   1 
ATOM   1279 O  O   . TYR A  1 162 ? 56.682 58.377  6.372   1.00 37.23 ? 163 TYR A O   1 
ATOM   1280 C  CB  . TYR A  1 162 ? 55.638 59.708  9.205   1.00 37.98 ? 163 TYR A CB  1 
ATOM   1281 C  CG  . TYR A  1 162 ? 55.408 60.755  8.146   1.00 39.83 ? 163 TYR A CG  1 
ATOM   1282 C  CD1 . TYR A  1 162 ? 54.165 60.899  7.555   1.00 43.38 ? 163 TYR A CD1 1 
ATOM   1283 C  CD2 . TYR A  1 162 ? 56.429 61.601  7.740   1.00 41.79 ? 163 TYR A CD2 1 
ATOM   1284 C  CE1 . TYR A  1 162 ? 53.942 61.847  6.582   1.00 42.64 ? 163 TYR A CE1 1 
ATOM   1285 C  CE2 . TYR A  1 162 ? 56.214 62.562  6.765   1.00 46.60 ? 163 TYR A CE2 1 
ATOM   1286 C  CZ  . TYR A  1 162 ? 54.963 62.679  6.191   1.00 44.31 ? 163 TYR A CZ  1 
ATOM   1287 O  OH  . TYR A  1 162 ? 54.723 63.623  5.216   1.00 44.62 ? 163 TYR A OH  1 
ATOM   1288 N  N   . MET A  1 163 ? 58.319 58.486  7.930   1.00 39.86 ? 164 MET A N   1 
ATOM   1289 C  CA  . MET A  1 163 ? 59.379 58.554  6.925   1.00 44.20 ? 164 MET A CA  1 
ATOM   1290 C  C   . MET A  1 163 ? 59.638 57.200  6.281   1.00 41.75 ? 164 MET A C   1 
ATOM   1291 O  O   . MET A  1 163 ? 59.862 57.132  5.068   1.00 43.26 ? 164 MET A O   1 
ATOM   1292 C  CB  . MET A  1 163 ? 60.677 59.111  7.526   1.00 40.46 ? 164 MET A CB  1 
ATOM   1293 C  CG  . MET A  1 163 ? 60.504 60.460  8.218   1.00 46.26 ? 164 MET A CG  1 
ATOM   1294 S  SD  . MET A  1 163 ? 60.295 61.810  7.031   1.00 53.43 ? 164 MET A SD  1 
ATOM   1295 C  CE  . MET A  1 163 ? 61.507 61.362  5.787   1.00 53.58 ? 164 MET A CE  1 
ATOM   1296 N  N   . PHE A  1 164 ? 59.620 56.115  7.064   1.00 40.58 ? 165 PHE A N   1 
ATOM   1297 C  CA  . PHE A  1 164 ? 59.759 54.792  6.463   1.00 37.20 ? 165 PHE A CA  1 
ATOM   1298 C  C   . PHE A  1 164 ? 58.639 54.535  5.465   1.00 38.72 ? 165 PHE A C   1 
ATOM   1299 O  O   . PHE A  1 164 ? 58.878 54.017  4.372   1.00 40.63 ? 165 PHE A O   1 
ATOM   1300 C  CB  . PHE A  1 164 ? 59.776 53.702  7.541   1.00 36.37 ? 165 PHE A CB  1 
ATOM   1301 C  CG  . PHE A  1 164 ? 59.938 52.306  6.980   1.00 37.96 ? 165 PHE A CG  1 
ATOM   1302 C  CD1 . PHE A  1 164 ? 61.194 51.828  6.616   1.00 37.27 ? 165 PHE A CD1 1 
ATOM   1303 C  CD2 . PHE A  1 164 ? 58.835 51.490  6.787   1.00 36.04 ? 165 PHE A CD2 1 
ATOM   1304 C  CE1 . PHE A  1 164 ? 61.342 50.560  6.083   1.00 42.57 ? 165 PHE A CE1 1 
ATOM   1305 C  CE2 . PHE A  1 164 ? 58.977 50.211  6.254   1.00 39.45 ? 165 PHE A CE2 1 
ATOM   1306 C  CZ  . PHE A  1 164 ? 60.228 49.743  5.902   1.00 38.06 ? 165 PHE A CZ  1 
ATOM   1307 N  N   . ASP A  1 165 ? 57.407 54.918  5.817   1.00 41.00 ? 166 ASP A N   1 
ATOM   1308 C  CA  . ASP A  1 165 ? 56.278 54.737  4.912   1.00 40.21 ? 166 ASP A CA  1 
ATOM   1309 C  C   . ASP A  1 165 ? 56.482 55.468  3.589   1.00 45.47 ? 166 ASP A C   1 
ATOM   1310 O  O   . ASP A  1 165 ? 56.025 54.991  2.542   1.00 43.13 ? 166 ASP A O   1 
ATOM   1311 C  CB  . ASP A  1 165 ? 54.994 55.223  5.576   1.00 38.63 ? 166 ASP A CB  1 
ATOM   1312 C  CG  . ASP A  1 165 ? 53.784 55.077  4.669   1.00 41.26 ? 166 ASP A CG  1 
ATOM   1313 O  OD1 . ASP A  1 165 ? 53.261 53.949  4.551   1.00 40.88 ? 166 ASP A OD1 1 
ATOM   1314 O  OD2 . ASP A  1 165 ? 53.350 56.089  4.078   1.00 45.39 ? 166 ASP A OD2 1 
ATOM   1315 N  N   . LYS A  1 166 ? 57.160 56.620  3.612   1.00 43.63 ? 167 LYS A N   1 
ATOM   1316 C  CA  . LYS A  1 166 ? 57.389 57.370  2.381   1.00 46.87 ? 167 LYS A CA  1 
ATOM   1317 C  C   . LYS A  1 166 ? 58.374 56.663  1.462   1.00 49.86 ? 167 LYS A C   1 
ATOM   1318 O  O   . LYS A  1 166 ? 58.252 56.765  0.238   1.00 53.16 ? 167 LYS A O   1 
ATOM   1319 C  CB  . LYS A  1 166 ? 57.871 58.781  2.711   1.00 49.37 ? 167 LYS A CB  1 
ATOM   1320 C  CG  . LYS A  1 166 ? 56.751 59.798  2.780   1.00 52.86 ? 167 LYS A CG  1 
ATOM   1321 C  CD  . LYS A  1 166 ? 57.079 60.863  3.793   1.00 58.43 ? 167 LYS A CD  1 
ATOM   1322 C  CE  . LYS A  1 166 ? 58.339 61.633  3.404   1.00 64.00 ? 167 LYS A CE  1 
ATOM   1323 N  NZ  . LYS A  1 166 ? 58.169 63.107  3.570   1.00 65.07 ? 167 LYS A NZ  1 
ATOM   1324 N  N   . GLU A  1 167 ? 59.344 55.934  2.020   1.00 50.35 ? 168 GLU A N   1 
ATOM   1325 C  CA  . GLU A  1 167 ? 60.235 55.155  1.168   1.00 51.31 ? 168 GLU A CA  1 
ATOM   1326 C  C   . GLU A  1 167 ? 59.516 53.995  0.513   1.00 50.82 ? 168 GLU A C   1 
ATOM   1327 O  O   . GLU A  1 167 ? 59.856 53.616  -0.612  1.00 54.60 ? 168 GLU A O   1 
ATOM   1328 C  CB  . GLU A  1 167 ? 61.426 54.628  1.961   1.00 51.89 ? 168 GLU A CB  1 
ATOM   1329 C  CG  . GLU A  1 167 ? 62.471 55.676  2.178   1.00 64.33 ? 168 GLU A CG  1 
ATOM   1330 C  CD  . GLU A  1 167 ? 62.533 56.678  1.024   1.00 72.63 ? 168 GLU A CD  1 
ATOM   1331 O  OE1 . GLU A  1 167 ? 62.034 57.817  1.194   1.00 74.69 ? 168 GLU A OE1 1 
ATOM   1332 O  OE2 . GLU A  1 167 ? 63.076 56.325  -0.051  1.00 68.60 ? 168 GLU A OE2 1 
ATOM   1333 N  N   . LEU A  1 168 ? 58.546 53.405  1.206   1.00 47.51 ? 169 LEU A N   1 
ATOM   1334 C  CA  . LEU A  1 168 ? 57.784 52.297  0.648   1.00 47.76 ? 169 LEU A CA  1 
ATOM   1335 C  C   . LEU A  1 168 ? 56.881 52.738  -0.496  1.00 49.14 ? 169 LEU A C   1 
ATOM   1336 O  O   . LEU A  1 168 ? 56.450 51.899  -1.294  1.00 54.97 ? 169 LEU A O   1 
ATOM   1337 C  CB  . LEU A  1 168 ? 56.946 51.660  1.757   1.00 49.62 ? 169 LEU A CB  1 
ATOM   1338 C  CG  . LEU A  1 168 ? 56.979 50.160  1.993   1.00 47.25 ? 169 LEU A CG  1 
ATOM   1339 C  CD1 . LEU A  1 168 ? 58.400 49.654  1.952   1.00 48.34 ? 169 LEU A CD1 1 
ATOM   1340 C  CD2 . LEU A  1 168 ? 56.360 49.885  3.347   1.00 38.98 ? 169 LEU A CD2 1 
ATOM   1341 N  N   . ASN A  1 169 ? 56.580 54.031  -0.585  1.00 54.69 ? 170 ASN A N   1 
ATOM   1342 C  CA  . ASN A  1 169 ? 55.628 54.551  -1.560  1.00 56.87 ? 170 ASN A CA  1 
ATOM   1343 C  C   . ASN A  1 169 ? 56.320 55.063  -2.828  1.00 65.12 ? 170 ASN A C   1 
ATOM   1344 O  O   . ASN A  1 169 ? 57.351 55.757  -2.784  1.00 63.78 ? 170 ASN A O   1 
ATOM   1345 C  CB  . ASN A  1 169 ? 54.789 55.665  -0.922  1.00 56.82 ? 170 ASN A CB  1 
ATOM   1346 C  CG  . ASN A  1 169 ? 53.433 55.832  -1.590  1.00 62.41 ? 170 ASN A CG  1 
ATOM   1347 O  OD1 . ASN A  1 169 ? 52.857 54.866  -2.104  1.00 65.10 ? 170 ASN A OD1 1 
ATOM   1348 N  ND2 . ASN A  1 169 ? 52.906 57.055  -1.568  1.00 57.94 ? 170 ASN A ND2 1 
ATOM   1349 O  OXT . ASN A  1 169 ? 55.849 54.778  -3.937  1.00 70.04 ? 170 ASN A OXT 1 
ATOM   1350 N  N   . ALA B  1 1   ? 57.913 -19.010 29.561  1.00 63.58 ? 2   ALA B N   1 
ATOM   1351 C  CA  . ALA B  1 1   ? 57.479 -18.095 30.617  1.00 67.61 ? 2   ALA B CA  1 
ATOM   1352 C  C   . ALA B  1 1   ? 55.966 -18.197 30.849  1.00 67.12 ? 2   ALA B C   1 
ATOM   1353 O  O   . ALA B  1 1   ? 55.463 -19.231 31.313  1.00 72.39 ? 2   ALA B O   1 
ATOM   1354 C  CB  . ALA B  1 1   ? 57.871 -16.660 30.274  1.00 69.04 ? 2   ALA B CB  1 
ATOM   1355 N  N   . SER B  1 2   ? 55.248 -17.127 30.504  1.00 56.72 ? 3   SER B N   1 
ATOM   1356 C  CA  . SER B  1 2   ? 53.819 -17.036 30.781  1.00 48.65 ? 3   SER B CA  1 
ATOM   1357 C  C   . SER B  1 2   ? 53.000 -17.736 29.701  1.00 45.55 ? 3   SER B C   1 
ATOM   1358 O  O   . SER B  1 2   ? 53.136 -17.440 28.509  1.00 43.43 ? 3   SER B O   1 
ATOM   1359 C  CB  . SER B  1 2   ? 53.396 -15.572 30.886  1.00 46.04 ? 3   SER B CB  1 
ATOM   1360 O  OG  . SER B  1 2   ? 52.132 -15.465 31.508  1.00 45.21 ? 3   SER B OG  1 
ATOM   1361 N  N   . GLN B  1 3   ? 52.132 -18.654 30.128  1.00 41.27 ? 4   GLN B N   1 
ATOM   1362 C  CA  . GLN B  1 3   ? 51.258 -19.349 29.191  1.00 38.19 ? 4   GLN B CA  1 
ATOM   1363 C  C   . GLN B  1 3   ? 50.264 -18.410 28.506  1.00 37.45 ? 4   GLN B C   1 
ATOM   1364 O  O   . GLN B  1 3   ? 49.694 -18.784 27.478  1.00 36.24 ? 4   GLN B O   1 
ATOM   1365 C  CB  . GLN B  1 3   ? 50.510 -20.478 29.914  1.00 33.62 ? 4   GLN B CB  1 
ATOM   1366 C  CG  . GLN B  1 3   ? 49.276 -19.996 30.696  1.00 42.34 ? 4   GLN B CG  1 
ATOM   1367 C  CD  . GLN B  1 3   ? 48.795 -21.000 31.738  1.00 41.88 ? 4   GLN B CD  1 
ATOM   1368 O  OE1 . GLN B  1 3   ? 48.688 -22.195 31.451  1.00 41.74 ? 4   GLN B OE1 1 
ATOM   1369 N  NE2 . GLN B  1 3   ? 48.529 -20.518 32.965  1.00 33.69 ? 4   GLN B NE2 1 
ATOM   1370 N  N   . VAL B  1 4   ? 50.034 -17.209 29.044  1.00 34.12 ? 5   VAL B N   1 
ATOM   1371 C  CA  . VAL B  1 4   ? 49.078 -16.292 28.437  1.00 33.83 ? 5   VAL B CA  1 
ATOM   1372 C  C   . VAL B  1 4   ? 49.745 -15.275 27.518  1.00 38.54 ? 5   VAL B C   1 
ATOM   1373 O  O   . VAL B  1 4   ? 49.046 -14.665 26.692  1.00 33.87 ? 5   VAL B O   1 
ATOM   1374 C  CB  . VAL B  1 4   ? 48.229 -15.547 29.495  1.00 35.46 ? 5   VAL B CB  1 
ATOM   1375 C  CG1 . VAL B  1 4   ? 47.641 -16.507 30.524  1.00 34.82 ? 5   VAL B CG1 1 
ATOM   1376 C  CG2 . VAL B  1 4   ? 49.038 -14.434 30.169  1.00 32.64 ? 5   VAL B CG2 1 
ATOM   1377 N  N   . ARG B  1 5   ? 51.066 -15.088 27.618  1.00 36.43 ? 6   ARG B N   1 
ATOM   1378 C  CA  . ARG B  1 5   ? 51.735 -13.954 26.984  1.00 33.22 ? 6   ARG B CA  1 
ATOM   1379 C  C   . ARG B  1 5   ? 51.715 -14.066 25.463  1.00 36.12 ? 6   ARG B C   1 
ATOM   1380 O  O   . ARG B  1 5   ? 52.093 -15.096 24.909  1.00 33.38 ? 6   ARG B O   1 
ATOM   1381 C  CB  . ARG B  1 5   ? 53.182 -13.857 27.466  1.00 37.00 ? 6   ARG B CB  1 
ATOM   1382 C  CG  . ARG B  1 5   ? 53.799 -12.479 27.240  1.00 32.15 ? 6   ARG B CG  1 
ATOM   1383 C  CD  . ARG B  1 5   ? 55.285 -12.452 27.584  1.00 35.13 ? 6   ARG B CD  1 
ATOM   1384 N  NE  . ARG B  1 5   ? 55.831 -11.130 27.307  1.00 36.24 ? 6   ARG B NE  1 
ATOM   1385 C  CZ  . ARG B  1 5   ? 56.470 -10.375 28.189  1.00 39.23 ? 6   ARG B CZ  1 
ATOM   1386 N  NH1 . ARG B  1 5   ? 56.740 -10.817 29.411  1.00 30.85 ? 6   ARG B NH1 1 
ATOM   1387 N  NH2 . ARG B  1 5   ? 56.861 -9.151  27.830  1.00 35.65 ? 6   ARG B NH2 1 
ATOM   1388 N  N   . GLN B  1 6   ? 51.316 -12.988 24.785  1.00 32.47 ? 7   GLN B N   1 
ATOM   1389 C  CA  . GLN B  1 6   ? 51.302 -12.994 23.323  1.00 36.26 ? 7   GLN B CA  1 
ATOM   1390 C  C   . GLN B  1 6   ? 51.383 -11.564 22.806  1.00 30.59 ? 7   GLN B C   1 
ATOM   1391 O  O   . GLN B  1 6   ? 50.545 -10.728 23.160  1.00 37.44 ? 7   GLN B O   1 
ATOM   1392 C  CB  . GLN B  1 6   ? 50.045 -13.706 22.802  1.00 32.93 ? 7   GLN B CB  1 
ATOM   1393 C  CG  . GLN B  1 6   ? 49.929 -13.739 21.285  1.00 32.07 ? 7   GLN B CG  1 
ATOM   1394 C  CD  . GLN B  1 6   ? 48.730 -14.555 20.819  1.00 37.87 ? 7   GLN B CD  1 
ATOM   1395 O  OE1 . GLN B  1 6   ? 47.739 -14.695 21.540  1.00 40.34 ? 7   GLN B OE1 1 
ATOM   1396 N  NE2 . GLN B  1 6   ? 48.808 -15.083 19.607  1.00 32.88 ? 7   GLN B NE2 1 
ATOM   1397 N  N   . ASN B  1 7   ? 52.386 -11.284 21.968  1.00 29.16 ? 8   ASN B N   1 
ATOM   1398 C  CA  . ASN B  1 7   ? 52.580 -9.963  21.369  1.00 29.82 ? 8   ASN B CA  1 
ATOM   1399 C  C   . ASN B  1 7   ? 52.798 -8.874  22.421  1.00 35.16 ? 8   ASN B C   1 
ATOM   1400 O  O   . ASN B  1 7   ? 52.378 -7.725  22.239  1.00 33.23 ? 8   ASN B O   1 
ATOM   1401 C  CB  . ASN B  1 7   ? 51.408 -9.581  20.457  1.00 28.32 ? 8   ASN B CB  1 
ATOM   1402 C  CG  . ASN B  1 7   ? 51.767 -8.433  19.510  1.00 40.96 ? 8   ASN B CG  1 
ATOM   1403 O  OD1 . ASN B  1 7   ? 52.904 -8.355  19.024  1.00 38.65 ? 8   ASN B OD1 1 
ATOM   1404 N  ND2 . ASN B  1 7   ? 50.814 -7.524  19.267  1.00 33.74 ? 8   ASN B ND2 1 
ATOM   1405 N  N   . TYR B  1 8   ? 53.450 -9.217  23.531  1.00 32.37 ? 9   TYR B N   1 
ATOM   1406 C  CA  . TYR B  1 8   ? 53.664 -8.293  24.647  1.00 34.97 ? 9   TYR B CA  1 
ATOM   1407 C  C   . TYR B  1 8   ? 55.163 -8.075  24.799  1.00 32.37 ? 9   TYR B C   1 
ATOM   1408 O  O   . TYR B  1 8   ? 55.868 -8.937  25.325  1.00 31.32 ? 9   TYR B O   1 
ATOM   1409 C  CB  . TYR B  1 8   ? 53.059 -8.837  25.944  1.00 32.46 ? 9   TYR B CB  1 
ATOM   1410 C  CG  . TYR B  1 8   ? 52.980 -7.810  27.059  1.00 30.14 ? 9   TYR B CG  1 
ATOM   1411 C  CD1 . TYR B  1 8   ? 52.396 -6.564  26.841  1.00 31.14 ? 9   TYR B CD1 1 
ATOM   1412 C  CD2 . TYR B  1 8   ? 53.476 -8.089  28.325  1.00 28.15 ? 9   TYR B CD2 1 
ATOM   1413 C  CE1 . TYR B  1 8   ? 52.322 -5.611  27.866  1.00 32.72 ? 9   TYR B CE1 1 
ATOM   1414 C  CE2 . TYR B  1 8   ? 53.405 -7.151  29.359  1.00 30.76 ? 9   TYR B CE2 1 
ATOM   1415 C  CZ  . TYR B  1 8   ? 52.823 -5.914  29.119  1.00 34.67 ? 9   TYR B CZ  1 
ATOM   1416 O  OH  . TYR B  1 8   ? 52.741 -4.982  30.127  1.00 35.24 ? 9   TYR B OH  1 
ATOM   1417 N  N   . HIS B  1 9   ? 55.647 -6.924  24.360  1.00 35.02 ? 10  HIS B N   1 
ATOM   1418 C  CA  . HIS B  1 9   ? 57.083 -6.696  24.287  1.00 38.18 ? 10  HIS B CA  1 
ATOM   1419 C  C   . HIS B  1 9   ? 57.627 -6.313  25.666  1.00 36.19 ? 10  HIS B C   1 
ATOM   1420 O  O   . HIS B  1 9   ? 56.957 -5.649  26.459  1.00 36.96 ? 10  HIS B O   1 
ATOM   1421 C  CB  . HIS B  1 9   ? 57.365 -5.613  23.237  1.00 41.26 ? 10  HIS B CB  1 
ATOM   1422 C  CG  . HIS B  1 9   ? 58.808 -5.473  22.848  1.00 51.54 ? 10  HIS B CG  1 
ATOM   1423 N  ND1 . HIS B  1 9   ? 59.253 -5.695  21.560  1.00 53.11 ? 10  HIS B ND1 1 
ATOM   1424 C  CD2 . HIS B  1 9   ? 59.897 -5.085  23.558  1.00 48.98 ? 10  HIS B CD2 1 
ATOM   1425 C  CE1 . HIS B  1 9   ? 60.557 -5.477  21.501  1.00 51.85 ? 10  HIS B CE1 1 
ATOM   1426 N  NE2 . HIS B  1 9   ? 60.971 -5.101  22.699  1.00 51.07 ? 10  HIS B NE2 1 
ATOM   1427 N  N   . GLU B  1 10  ? 58.847 -6.764  25.963  1.00 37.03 ? 11  GLU B N   1 
ATOM   1428 C  CA  . GLU B  1 10  ? 59.456 -6.434  27.251  1.00 39.11 ? 11  GLU B CA  1 
ATOM   1429 C  C   . GLU B  1 10  ? 59.624 -4.926  27.445  1.00 41.02 ? 11  GLU B C   1 
ATOM   1430 O  O   . GLU B  1 10  ? 59.662 -4.453  28.590  1.00 38.53 ? 11  GLU B O   1 
ATOM   1431 C  CB  . GLU B  1 10  ? 60.800 -7.144  27.386  1.00 43.01 ? 11  GLU B CB  1 
ATOM   1432 C  CG  . GLU B  1 10  ? 61.555 -7.320  26.078  1.00 55.90 ? 11  GLU B CG  1 
ATOM   1433 C  CD  . GLU B  1 10  ? 62.844 -8.129  26.257  1.00 77.90 ? 11  GLU B CD  1 
ATOM   1434 O  OE1 . GLU B  1 10  ? 62.865 -9.017  27.145  1.00 75.54 ? 11  GLU B OE1 1 
ATOM   1435 O  OE2 . GLU B  1 10  ? 63.826 -7.880  25.514  1.00 78.82 ? 11  GLU B OE2 1 
ATOM   1436 N  N   . ASP B  1 11  ? 59.739 -4.166  26.346  1.00 35.36 ? 12  ASP B N   1 
ATOM   1437 C  CA  . ASP B  1 11  ? 59.721 -2.703  26.394  1.00 38.23 ? 12  ASP B CA  1 
ATOM   1438 C  C   . ASP B  1 11  ? 58.460 -2.200  27.085  1.00 40.94 ? 12  ASP B C   1 
ATOM   1439 O  O   . ASP B  1 11  ? 58.514 -1.381  28.010  1.00 40.19 ? 12  ASP B O   1 
ATOM   1440 C  CB  . ASP B  1 11  ? 59.760 -2.141  24.966  1.00 48.13 ? 12  ASP B CB  1 
ATOM   1441 C  CG  . ASP B  1 11  ? 61.155 -1.748  24.511  1.00 57.62 ? 12  ASP B CG  1 
ATOM   1442 O  OD1 . ASP B  1 11  ? 62.126 -2.011  25.247  1.00 63.01 ? 12  ASP B OD1 1 
ATOM   1443 O  OD2 . ASP B  1 11  ? 61.277 -1.188  23.394  1.00 67.52 ? 12  ASP B OD2 1 
ATOM   1444 N  N   . ALA B  1 12  ? 57.302 -2.656  26.604  1.00 38.37 ? 13  ALA B N   1 
ATOM   1445 C  CA  . ALA B  1 12  ? 56.037 -2.265  27.207  1.00 35.27 ? 13  ALA B CA  1 
ATOM   1446 C  C   . ALA B  1 12  ? 55.990 -2.681  28.665  1.00 36.91 ? 13  ALA B C   1 
ATOM   1447 O  O   . ALA B  1 12  ? 55.617 -1.883  29.536  1.00 36.75 ? 13  ALA B O   1 
ATOM   1448 C  CB  . ALA B  1 12  ? 54.876 -2.891  26.435  1.00 33.52 ? 13  ALA B CB  1 
ATOM   1449 N  N   . GLU B  1 13  ? 56.413 -3.918  28.951  1.00 33.23 ? 14  GLU B N   1 
ATOM   1450 C  CA  . GLU B  1 13  ? 56.297 -4.441  30.308  1.00 35.52 ? 14  GLU B CA  1 
ATOM   1451 C  C   . GLU B  1 13  ? 57.090 -3.581  31.293  1.00 32.49 ? 14  GLU B C   1 
ATOM   1452 O  O   . GLU B  1 13  ? 56.595 -3.249  32.376  1.00 29.76 ? 14  GLU B O   1 
ATOM   1453 C  CB  . GLU B  1 13  ? 56.741 -5.906  30.325  1.00 31.21 ? 14  GLU B CB  1 
ATOM   1454 C  CG  . GLU B  1 13  ? 56.862 -6.568  31.696  1.00 34.54 ? 14  GLU B CG  1 
ATOM   1455 C  CD  . GLU B  1 13  ? 57.401 -8.016  31.623  1.00 40.39 ? 14  GLU B CD  1 
ATOM   1456 O  OE1 . GLU B  1 13  ? 57.368 -8.731  32.659  1.00 39.56 ? 14  GLU B OE1 1 
ATOM   1457 O  OE2 . GLU B  1 13  ? 57.860 -8.443  30.532  1.00 42.10 ? 14  GLU B OE2 1 
ATOM   1458 N  N   . ALA B  1 14  ? 58.290 -3.149  30.899  1.00 30.93 ? 15  ALA B N   1 
ATOM   1459 C  CA  . ALA B  1 14  ? 59.102 -2.305  31.768  1.00 35.35 ? 15  ALA B CA  1 
ATOM   1460 C  C   . ALA B  1 14  ? 58.502 -0.908  31.907  1.00 35.98 ? 15  ALA B C   1 
ATOM   1461 O  O   . ALA B  1 14  ? 58.497 -0.336  33.002  1.00 34.39 ? 15  ALA B O   1 
ATOM   1462 C  CB  . ALA B  1 14  ? 60.533 -2.223  31.233  1.00 35.08 ? 15  ALA B CB  1 
ATOM   1463 N  N   . SER B  1 15  ? 57.991 -0.343  30.810  1.00 34.77 ? 16  SER B N   1 
ATOM   1464 C  CA  . SER B  1 15  ? 57.368 0.975   30.881  1.00 37.53 ? 16  SER B CA  1 
ATOM   1465 C  C   . SER B  1 15  ? 56.135 0.955   31.772  1.00 33.49 ? 16  SER B C   1 
ATOM   1466 O  O   . SER B  1 15  ? 55.900 1.896   32.539  1.00 35.64 ? 16  SER B O   1 
ATOM   1467 C  CB  . SER B  1 15  ? 56.995 1.462   29.482  1.00 37.18 ? 16  SER B CB  1 
ATOM   1468 O  OG  . SER B  1 15  ? 58.103 2.044   28.837  1.00 42.90 ? 16  SER B OG  1 
ATOM   1469 N  N   . ILE B  1 16  ? 55.334 -0.105  31.683  1.00 34.80 ? 17  ILE B N   1 
ATOM   1470 C  CA  . ILE B  1 16  ? 54.178 -0.229  32.566  1.00 30.59 ? 17  ILE B CA  1 
ATOM   1471 C  C   . ILE B  1 16  ? 54.620 -0.219  34.024  1.00 30.98 ? 17  ILE B C   1 
ATOM   1472 O  O   . ILE B  1 16  ? 53.982 0.424   34.866  1.00 30.84 ? 17  ILE B O   1 
ATOM   1473 C  CB  . ILE B  1 16  ? 53.372 -1.493  32.220  1.00 33.67 ? 17  ILE B CB  1 
ATOM   1474 C  CG1 . ILE B  1 16  ? 52.861 -1.416  30.766  1.00 34.66 ? 17  ILE B CG1 1 
ATOM   1475 C  CG2 . ILE B  1 16  ? 52.264 -1.754  33.262  1.00 28.17 ? 17  ILE B CG2 1 
ATOM   1476 C  CD1 . ILE B  1 16  ? 51.470 -0.948  30.618  1.00 38.89 ? 17  ILE B CD1 1 
ATOM   1477 N  N   . ASN B  1 17  ? 55.739 -0.900  34.343  1.00 27.74 ? 18  ASN B N   1 
ATOM   1478 C  CA  . ASN B  1 17  ? 56.207 -0.924  35.730  1.00 29.57 ? 18  ASN B CA  1 
ATOM   1479 C  C   . ASN B  1 17  ? 56.645 0.463   36.199  1.00 30.44 ? 18  ASN B C   1 
ATOM   1480 O  O   . ASN B  1 17  ? 56.369 0.841   37.344  1.00 27.75 ? 18  ASN B O   1 
ATOM   1481 C  CB  . ASN B  1 17  ? 57.336 -1.948  35.911  1.00 29.18 ? 18  ASN B CB  1 
ATOM   1482 C  CG  . ASN B  1 17  ? 56.804 -3.380  36.110  1.00 31.36 ? 18  ASN B CG  1 
ATOM   1483 O  OD1 . ASN B  1 17  ? 55.687 -3.579  36.573  1.00 31.97 ? 18  ASN B OD1 1 
ATOM   1484 N  ND2 . ASN B  1 17  ? 57.604 -4.372  35.736  1.00 31.46 ? 18  ASN B ND2 1 
ATOM   1485 N  N   . LYS B  1 18  ? 57.315 1.249   35.335  1.00 27.74 ? 19  LYS B N   1 
ATOM   1486 C  CA  . LYS B  1 18  ? 57.654 2.618   35.744  1.00 33.31 ? 19  LYS B CA  1 
ATOM   1487 C  C   . LYS B  1 18  ? 56.404 3.482   35.901  1.00 29.38 ? 19  LYS B C   1 
ATOM   1488 O  O   . LYS B  1 18  ? 56.321 4.294   36.824  1.00 33.61 ? 19  LYS B O   1 
ATOM   1489 C  CB  . LYS B  1 18  ? 58.622 3.276   34.757  1.00 32.85 ? 19  LYS B CB  1 
ATOM   1490 C  CG  . LYS B  1 18  ? 59.851 2.445   34.456  1.00 41.46 ? 19  LYS B CG  1 
ATOM   1491 C  CD  . LYS B  1 18  ? 61.046 2.872   35.291  1.00 49.45 ? 19  LYS B CD  1 
ATOM   1492 C  CE  . LYS B  1 18  ? 61.745 4.081   34.668  1.00 71.16 ? 19  LYS B CE  1 
ATOM   1493 N  NZ  . LYS B  1 18  ? 63.246 3.942   34.662  1.00 67.81 ? 19  LYS B NZ  1 
ATOM   1494 N  N   . GLN B  1 19  ? 55.423 3.324   35.015  1.00 28.69 ? 20  GLN B N   1 
ATOM   1495 C  CA  . GLN B  1 19  ? 54.217 4.134   35.121  1.00 32.69 ? 20  GLN B CA  1 
ATOM   1496 C  C   . GLN B  1 19  ? 53.443 3.828   36.401  1.00 31.41 ? 20  GLN B C   1 
ATOM   1497 O  O   . GLN B  1 19  ? 52.821 4.727   36.979  1.00 30.43 ? 20  GLN B O   1 
ATOM   1498 C  CB  . GLN B  1 19  ? 53.330 3.917   33.893  1.00 37.07 ? 20  GLN B CB  1 
ATOM   1499 C  CG  . GLN B  1 19  ? 52.249 4.981   33.744  1.00 38.39 ? 20  GLN B CG  1 
ATOM   1500 C  CD  . GLN B  1 19  ? 52.825 6.341   33.398  1.00 40.88 ? 20  GLN B CD  1 
ATOM   1501 O  OE1 . GLN B  1 19  ? 53.769 6.447   32.602  1.00 40.31 ? 20  GLN B OE1 1 
ATOM   1502 N  NE2 . GLN B  1 19  ? 52.276 7.390   34.012  1.00 43.70 ? 20  GLN B NE2 1 
ATOM   1503 N  N   . ILE B  1 20  ? 53.482 2.575   36.869  1.00 29.92 ? 21  ILE B N   1 
ATOM   1504 C  CA  . ILE B  1 20  ? 52.853 2.236   38.148  1.00 31.52 ? 21  ILE B CA  1 
ATOM   1505 C  C   . ILE B  1 20  ? 53.491 3.027   39.282  1.00 31.50 ? 21  ILE B C   1 
ATOM   1506 O  O   . ILE B  1 20  ? 52.798 3.566   40.156  1.00 31.42 ? 21  ILE B O   1 
ATOM   1507 C  CB  . ILE B  1 20  ? 52.947 0.722   38.410  1.00 29.20 ? 21  ILE B CB  1 
ATOM   1508 C  CG1 . ILE B  1 20  ? 51.948 -0.031  37.538  1.00 29.60 ? 21  ILE B CG1 1 
ATOM   1509 C  CG2 . ILE B  1 20  ? 52.758 0.425   39.902  1.00 27.00 ? 21  ILE B CG2 1 
ATOM   1510 C  CD1 . ILE B  1 20  ? 52.375 -1.472  37.222  1.00 31.37 ? 21  ILE B CD1 1 
ATOM   1511 N  N   . ASN B  1 21  ? 54.825 3.103   39.289  1.00 28.08 ? 22  ASN B N   1 
ATOM   1512 C  CA  . ASN B  1 21  ? 55.505 3.855   40.329  1.00 30.12 ? 22  ASN B CA  1 
ATOM   1513 C  C   . ASN B  1 21  ? 55.208 5.344   40.204  1.00 32.39 ? 22  ASN B C   1 
ATOM   1514 O  O   . ASN B  1 21  ? 55.080 6.047   41.211  1.00 32.45 ? 22  ASN B O   1 
ATOM   1515 C  CB  . ASN B  1 21  ? 57.009 3.601   40.270  1.00 29.35 ? 22  ASN B CB  1 
ATOM   1516 C  CG  . ASN B  1 21  ? 57.742 4.211   41.455  1.00 36.06 ? 22  ASN B CG  1 
ATOM   1517 O  OD1 . ASN B  1 21  ? 58.307 5.313   41.352  1.00 32.81 ? 22  ASN B OD1 1 
ATOM   1518 N  ND2 . ASN B  1 21  ? 57.719 3.505   42.602  1.00 28.74 ? 22  ASN B ND2 1 
ATOM   1519 N  N   . MET B  1 22  ? 55.091 5.843   38.980  1.00 32.38 ? 23  MET B N   1 
ATOM   1520 C  CA  . MET B  1 22  ? 54.817 7.265   38.801  1.00 33.76 ? 23  MET B CA  1 
ATOM   1521 C  C   . MET B  1 22  ? 53.439 7.626   39.353  1.00 32.24 ? 23  MET B C   1 
ATOM   1522 O  O   . MET B  1 22  ? 53.274 8.652   40.022  1.00 29.12 ? 23  MET B O   1 
ATOM   1523 C  CB  . MET B  1 22  ? 54.950 7.620   37.319  1.00 32.92 ? 23  MET B CB  1 
ATOM   1524 C  CG  . MET B  1 22  ? 54.671 9.073   36.974  1.00 46.37 ? 23  MET B CG  1 
ATOM   1525 S  SD  . MET B  1 22  ? 55.242 9.478   35.294  1.00 50.31 ? 23  MET B SD  1 
ATOM   1526 C  CE  . MET B  1 22  ? 55.823 11.169  35.539  1.00 40.59 ? 23  MET B CE  1 
ATOM   1527 N  N   . CYS B  1 23  ? 52.444 6.765   39.140  1.00 31.75 ? 24  CYS B N   1 
ATOM   1528 C  CA  . CYS B  1 23  ? 51.121 7.071   39.671  1.00 29.45 ? 24  CYS B CA  1 
ATOM   1529 C  C   . CYS B  1 23  ? 51.035 6.827   41.179  1.00 32.47 ? 24  CYS B C   1 
ATOM   1530 O  O   . CYS B  1 23  ? 50.284 7.525   41.870  1.00 32.07 ? 24  CYS B O   1 
ATOM   1531 C  CB  . CYS B  1 23  ? 50.059 6.274   38.907  1.00 36.84 ? 24  CYS B CB  1 
ATOM   1532 S  SG  . CYS B  1 23  ? 49.616 7.046   37.294  1.00 52.03 ? 24  CYS B SG  1 
ATOM   1533 N  N   . LEU B  1 24  ? 51.801 5.875   41.723  1.00 29.35 ? 25  LEU B N   1 
ATOM   1534 C  CA  . LEU B  1 24  ? 51.865 5.763   43.179  1.00 31.35 ? 25  LEU B CA  1 
ATOM   1535 C  C   . LEU B  1 24  ? 52.497 7.005   43.792  1.00 29.54 ? 25  LEU B C   1 
ATOM   1536 O  O   . LEU B  1 24  ? 52.022 7.515   44.813  1.00 28.99 ? 25  LEU B O   1 
ATOM   1537 C  CB  . LEU B  1 24  ? 52.634 4.510   43.592  1.00 29.45 ? 25  LEU B CB  1 
ATOM   1538 C  CG  . LEU B  1 24  ? 51.881 3.204   43.306  1.00 28.57 ? 25  LEU B CG  1 
ATOM   1539 C  CD1 . LEU B  1 24  ? 52.735 1.999   43.617  1.00 25.72 ? 25  LEU B CD1 1 
ATOM   1540 C  CD2 . LEU B  1 24  ? 50.596 3.159   44.095  1.00 27.27 ? 25  LEU B CD2 1 
ATOM   1541 N  N   . TYR B  1 25  ? 53.555 7.522   43.167  1.00 30.24 ? 26  TYR B N   1 
ATOM   1542 C  CA  . TYR B  1 25  ? 54.206 8.719   43.691  1.00 32.60 ? 26  TYR B CA  1 
ATOM   1543 C  C   . TYR B  1 25  ? 53.270 9.920   43.655  1.00 30.68 ? 26  TYR B C   1 
ATOM   1544 O  O   . TYR B  1 25  ? 53.154 10.653  44.641  1.00 32.64 ? 26  TYR B O   1 
ATOM   1545 C  CB  . TYR B  1 25  ? 55.485 9.015   42.909  1.00 32.14 ? 26  TYR B CB  1 
ATOM   1546 C  CG  . TYR B  1 25  ? 56.101 10.335  43.305  1.00 33.05 ? 26  TYR B CG  1 
ATOM   1547 C  CD1 . TYR B  1 25  ? 56.788 10.461  44.502  1.00 36.26 ? 26  TYR B CD1 1 
ATOM   1548 C  CD2 . TYR B  1 25  ? 55.991 11.454  42.494  1.00 31.70 ? 26  TYR B CD2 1 
ATOM   1549 C  CE1 . TYR B  1 25  ? 57.353 11.661  44.880  1.00 33.55 ? 26  TYR B CE1 1 
ATOM   1550 C  CE2 . TYR B  1 25  ? 56.558 12.666  42.866  1.00 33.59 ? 26  TYR B CE2 1 
ATOM   1551 C  CZ  . TYR B  1 25  ? 57.237 12.757  44.062  1.00 32.36 ? 26  TYR B CZ  1 
ATOM   1552 O  OH  . TYR B  1 25  ? 57.802 13.943  44.454  1.00 40.09 ? 26  TYR B OH  1 
ATOM   1553 N  N   . ALA B  1 26  ? 52.607 10.149  42.515  1.00 31.09 ? 27  ALA B N   1 
ATOM   1554 C  CA  . ALA B  1 26  ? 51.631 11.235  42.408  1.00 32.09 ? 27  ALA B CA  1 
ATOM   1555 C  C   . ALA B  1 26  ? 50.519 11.090  43.445  1.00 32.38 ? 27  ALA B C   1 
ATOM   1556 O  O   . ALA B  1 26  ? 50.085 12.075  44.053  1.00 31.63 ? 27  ALA B O   1 
ATOM   1557 C  CB  . ALA B  1 26  ? 51.039 11.262  40.998  1.00 29.39 ? 27  ALA B CB  1 
ATOM   1558 N  N   . SER B  1 27  ? 50.048 9.866   43.656  1.00 30.93 ? 28  SER B N   1 
ATOM   1559 C  CA  . SER B  1 27  ? 49.064 9.624   44.701  1.00 34.47 ? 28  SER B CA  1 
ATOM   1560 C  C   . SER B  1 27  ? 49.582 10.087  46.057  1.00 33.99 ? 28  SER B C   1 
ATOM   1561 O  O   . SER B  1 27  ? 48.857 10.734  46.826  1.00 31.36 ? 28  SER B O   1 
ATOM   1562 C  CB  . SER B  1 27  ? 48.722 8.137   44.737  1.00 30.62 ? 28  SER B CB  1 
ATOM   1563 O  OG  . SER B  1 27  ? 47.756 7.900   45.718  1.00 35.40 ? 28  SER B OG  1 
ATOM   1564 N  N   . TYR B  1 28  ? 50.838 9.759   46.359  1.00 29.05 ? 29  TYR B N   1 
ATOM   1565 C  CA  . TYR B  1 28  ? 51.462 10.149  47.617  1.00 29.04 ? 29  TYR B CA  1 
ATOM   1566 C  C   . TYR B  1 28  ? 51.597 11.669  47.722  1.00 29.98 ? 29  TYR B C   1 
ATOM   1567 O  O   . TYR B  1 28  ? 51.363 12.250  48.792  1.00 30.65 ? 29  TYR B O   1 
ATOM   1568 C  CB  . TYR B  1 28  ? 52.821 9.462   47.711  1.00 29.39 ? 29  TYR B CB  1 
ATOM   1569 C  CG  . TYR B  1 28  ? 53.399 9.270   49.088  1.00 30.96 ? 29  TYR B CG  1 
ATOM   1570 C  CD1 . TYR B  1 28  ? 52.604 9.343   50.236  1.00 27.41 ? 29  TYR B CD1 1 
ATOM   1571 C  CD2 . TYR B  1 28  ? 54.759 8.995   49.239  1.00 25.68 ? 29  TYR B CD2 1 
ATOM   1572 C  CE1 . TYR B  1 28  ? 53.174 9.153   51.518  1.00 29.15 ? 29  TYR B CE1 1 
ATOM   1573 C  CE2 . TYR B  1 28  ? 55.325 8.804   50.485  1.00 27.72 ? 29  TYR B CE2 1 
ATOM   1574 C  CZ  . TYR B  1 28  ? 54.537 8.885   51.625  1.00 27.47 ? 29  TYR B CZ  1 
ATOM   1575 O  OH  . TYR B  1 28  ? 55.128 8.695   52.855  1.00 30.21 ? 29  TYR B OH  1 
ATOM   1576 N  N   . VAL B  1 29  ? 51.973 12.330  46.624  1.00 27.45 ? 30  VAL B N   1 
ATOM   1577 C  CA  . VAL B  1 29  ? 52.066 13.791  46.631  1.00 32.04 ? 30  VAL B CA  1 
ATOM   1578 C  C   . VAL B  1 29  ? 50.702 14.421  46.924  1.00 32.26 ? 30  VAL B C   1 
ATOM   1579 O  O   . VAL B  1 29  ? 50.589 15.353  47.733  1.00 31.18 ? 30  VAL B O   1 
ATOM   1580 C  CB  . VAL B  1 29  ? 52.654 14.283  45.295  1.00 35.01 ? 30  VAL B CB  1 
ATOM   1581 C  CG1 . VAL B  1 29  ? 52.429 15.768  45.121  1.00 29.82 ? 30  VAL B CG1 1 
ATOM   1582 C  CG2 . VAL B  1 29  ? 54.152 13.935  45.218  1.00 31.48 ? 30  VAL B CG2 1 
ATOM   1583 N  N   . TYR B  1 30  ? 49.643 13.900  46.299  1.00 31.86 ? 31  TYR B N   1 
ATOM   1584 C  CA  . TYR B  1 30  ? 48.304 14.422  46.550  1.00 31.00 ? 31  TYR B CA  1 
ATOM   1585 C  C   . TYR B  1 30  ? 47.875 14.198  47.996  1.00 34.17 ? 31  TYR B C   1 
ATOM   1586 O  O   . TYR B  1 30  ? 47.235 15.070  48.603  1.00 31.79 ? 31  TYR B O   1 
ATOM   1587 C  CB  . TYR B  1 30  ? 47.316 13.774  45.591  1.00 31.23 ? 31  TYR B CB  1 
ATOM   1588 C  CG  . TYR B  1 30  ? 47.466 14.316  44.196  1.00 35.19 ? 31  TYR B CG  1 
ATOM   1589 C  CD1 . TYR B  1 30  ? 47.672 15.674  43.997  1.00 36.09 ? 31  TYR B CD1 1 
ATOM   1590 C  CD2 . TYR B  1 30  ? 47.427 13.478  43.079  1.00 33.28 ? 31  TYR B CD2 1 
ATOM   1591 C  CE1 . TYR B  1 30  ? 47.822 16.200  42.735  1.00 41.97 ? 31  TYR B CE1 1 
ATOM   1592 C  CE2 . TYR B  1 30  ? 47.580 14.000  41.790  1.00 36.63 ? 31  TYR B CE2 1 
ATOM   1593 C  CZ  . TYR B  1 30  ? 47.772 15.367  41.635  1.00 42.40 ? 31  TYR B CZ  1 
ATOM   1594 O  OH  . TYR B  1 30  ? 47.924 15.931  40.396  1.00 46.82 ? 31  TYR B OH  1 
ATOM   1595 N  N   . LEU B  1 31  ? 48.218 13.036  48.563  1.00 28.81 ? 32  LEU B N   1 
ATOM   1596 C  CA  . LEU B  1 31  ? 47.918 12.777  49.968  1.00 32.14 ? 32  LEU B CA  1 
ATOM   1597 C  C   . LEU B  1 31  ? 48.584 13.804  50.876  1.00 32.73 ? 32  LEU B C   1 
ATOM   1598 O  O   . LEU B  1 31  ? 47.959 14.308  51.819  1.00 32.19 ? 32  LEU B O   1 
ATOM   1599 C  CB  . LEU B  1 31  ? 48.365 11.371  50.349  1.00 30.55 ? 32  LEU B CB  1 
ATOM   1600 C  CG  . LEU B  1 31  ? 47.904 10.970  51.753  1.00 42.08 ? 32  LEU B CG  1 
ATOM   1601 C  CD1 . LEU B  1 31  ? 46.398 10.767  51.753  1.00 38.86 ? 32  LEU B CD1 1 
ATOM   1602 C  CD2 . LEU B  1 31  ? 48.623 9.707   52.244  1.00 39.44 ? 32  LEU B CD2 1 
ATOM   1603 N  N   . SER B  1 32  ? 49.856 14.111  50.613  1.00 28.03 ? 33  SER B N   1 
ATOM   1604 C  CA  . SER B  1 32  ? 50.569 15.136  51.376  1.00 31.39 ? 33  SER B CA  1 
ATOM   1605 C  C   . SER B  1 32  ? 49.868 16.489  51.283  1.00 35.13 ? 33  SER B C   1 
ATOM   1606 O  O   . SER B  1 32  ? 49.690 17.179  52.292  1.00 35.06 ? 33  SER B O   1 
ATOM   1607 C  CB  . SER B  1 32  ? 52.010 15.253  50.867  1.00 30.34 ? 33  SER B CB  1 
ATOM   1608 O  OG  . SER B  1 32  ? 52.663 16.379  51.425  1.00 38.84 ? 33  SER B OG  1 
ATOM   1609 N  N   . MET B  1 33  ? 49.479 16.889  50.068  1.00 32.96 ? 34  MET B N   1 
ATOM   1610 C  CA  . MET B  1 33  ? 48.722 18.125  49.878  1.00 34.88 ? 34  MET B CA  1 
ATOM   1611 C  C   . MET B  1 33  ? 47.412 18.100  50.659  1.00 32.70 ? 34  MET B C   1 
ATOM   1612 O  O   . MET B  1 33  ? 47.059 19.072  51.342  1.00 31.02 ? 34  MET B O   1 
ATOM   1613 C  CB  . MET B  1 33  ? 48.442 18.325  48.391  1.00 32.69 ? 34  MET B CB  1 
ATOM   1614 C  CG  . MET B  1 33  ? 49.590 18.923  47.588  1.00 33.40 ? 34  MET B CG  1 
ATOM   1615 S  SD  . MET B  1 33  ? 49.089 19.110  45.836  1.00 43.26 ? 34  MET B SD  1 
ATOM   1616 C  CE  . MET B  1 33  ? 50.673 19.153  44.999  1.00 38.71 ? 34  MET B CE  1 
ATOM   1617 N  N   . ALA B  1 34  ? 46.682 16.984  50.578  1.00 28.42 ? 35  ALA B N   1 
ATOM   1618 C  CA  . ALA B  1 34  ? 45.375 16.898  51.223  1.00 32.20 ? 35  ALA B CA  1 
ATOM   1619 C  C   . ALA B  1 34  ? 45.473 17.193  52.716  1.00 35.31 ? 35  ALA B C   1 
ATOM   1620 O  O   . ALA B  1 34  ? 44.718 18.010  53.249  1.00 34.79 ? 35  ALA B O   1 
ATOM   1621 C  CB  . ALA B  1 34  ? 44.757 15.521  50.985  1.00 27.50 ? 35  ALA B CB  1 
ATOM   1622 N  N   . TYR B  1 35  ? 46.403 16.543  53.413  1.00 33.20 ? 36  TYR B N   1 
ATOM   1623 C  CA  . TYR B  1 35  ? 46.486 16.783  54.845  1.00 34.15 ? 36  TYR B CA  1 
ATOM   1624 C  C   . TYR B  1 35  ? 47.191 18.093  55.180  1.00 32.71 ? 36  TYR B C   1 
ATOM   1625 O  O   . TYR B  1 35  ? 46.964 18.633  56.266  1.00 37.64 ? 36  TYR B O   1 
ATOM   1626 C  CB  . TYR B  1 35  ? 47.147 15.585  55.539  1.00 32.16 ? 36  TYR B CB  1 
ATOM   1627 C  CG  . TYR B  1 35  ? 46.178 14.417  55.612  1.00 33.30 ? 36  TYR B CG  1 
ATOM   1628 C  CD1 . TYR B  1 35  ? 45.229 14.328  56.631  1.00 36.67 ? 36  TYR B CD1 1 
ATOM   1629 C  CD2 . TYR B  1 35  ? 46.166 13.441  54.624  1.00 37.04 ? 36  TYR B CD2 1 
ATOM   1630 C  CE1 . TYR B  1 35  ? 44.316 13.271  56.682  1.00 37.16 ? 36  TYR B CE1 1 
ATOM   1631 C  CE2 . TYR B  1 35  ? 45.257 12.387  54.659  1.00 38.81 ? 36  TYR B CE2 1 
ATOM   1632 C  CZ  . TYR B  1 35  ? 44.337 12.306  55.686  1.00 39.57 ? 36  TYR B CZ  1 
ATOM   1633 O  OH  . TYR B  1 35  ? 43.460 11.248  55.707  1.00 50.29 ? 36  TYR B OH  1 
ATOM   1634 N  N   . TYR B  1 36  ? 48.000 18.645  54.269  1.00 29.80 ? 37  TYR B N   1 
ATOM   1635 C  CA  . TYR B  1 36  ? 48.511 19.998  54.487  1.00 32.23 ? 37  TYR B CA  1 
ATOM   1636 C  C   . TYR B  1 36  ? 47.375 21.019  54.596  1.00 36.12 ? 37  TYR B C   1 
ATOM   1637 O  O   . TYR B  1 36  ? 47.416 21.910  55.453  1.00 31.92 ? 37  TYR B O   1 
ATOM   1638 C  CB  . TYR B  1 36  ? 49.464 20.400  53.371  1.00 32.18 ? 37  TYR B CB  1 
ATOM   1639 C  CG  . TYR B  1 36  ? 49.838 21.867  53.406  1.00 37.90 ? 37  TYR B CG  1 
ATOM   1640 C  CD1 . TYR B  1 36  ? 50.792 22.353  54.300  1.00 38.26 ? 37  TYR B CD1 1 
ATOM   1641 C  CD2 . TYR B  1 36  ? 49.232 22.774  52.541  1.00 37.92 ? 37  TYR B CD2 1 
ATOM   1642 C  CE1 . TYR B  1 36  ? 51.127 23.710  54.327  1.00 39.08 ? 37  TYR B CE1 1 
ATOM   1643 C  CE2 . TYR B  1 36  ? 49.556 24.116  52.569  1.00 36.52 ? 37  TYR B CE2 1 
ATOM   1644 C  CZ  . TYR B  1 36  ? 50.499 24.579  53.453  1.00 37.27 ? 37  TYR B CZ  1 
ATOM   1645 O  OH  . TYR B  1 36  ? 50.792 25.925  53.449  1.00 44.47 ? 37  TYR B OH  1 
ATOM   1646 N  N   . PHE B  1 37  ? 46.349 20.902  53.747  1.00 32.73 ? 38  PHE B N   1 
ATOM   1647 C  CA  . PHE B  1 37  ? 45.239 21.850  53.774  1.00 34.23 ? 38  PHE B CA  1 
ATOM   1648 C  C   . PHE B  1 37  ? 44.240 21.585  54.899  1.00 34.74 ? 38  PHE B C   1 
ATOM   1649 O  O   . PHE B  1 37  ? 43.318 22.389  55.085  1.00 35.04 ? 38  PHE B O   1 
ATOM   1650 C  CB  . PHE B  1 37  ? 44.536 21.863  52.412  1.00 30.31 ? 38  PHE B CB  1 
ATOM   1651 C  CG  . PHE B  1 37  ? 45.368 22.510  51.344  1.00 34.08 ? 38  PHE B CG  1 
ATOM   1652 C  CD1 . PHE B  1 37  ? 45.621 23.876  51.386  1.00 31.19 ? 38  PHE B CD1 1 
ATOM   1653 C  CD2 . PHE B  1 37  ? 45.942 21.758  50.339  1.00 32.70 ? 38  PHE B CD2 1 
ATOM   1654 C  CE1 . PHE B  1 37  ? 46.409 24.481  50.431  1.00 37.88 ? 38  PHE B CE1 1 
ATOM   1655 C  CE2 . PHE B  1 37  ? 46.751 22.364  49.378  1.00 35.56 ? 38  PHE B CE2 1 
ATOM   1656 C  CZ  . PHE B  1 37  ? 46.980 23.727  49.425  1.00 36.58 ? 38  PHE B CZ  1 
ATOM   1657 N  N   . GLU B  1 38  ? 44.410 20.503  55.658  1.00 33.16 ? 39  GLU B N   1 
ATOM   1658 C  CA  . GLU B  1 38  ? 43.609 20.230  56.848  1.00 34.16 ? 39  GLU B CA  1 
ATOM   1659 C  C   . GLU B  1 38  ? 44.296 20.695  58.131  1.00 34.74 ? 39  GLU B C   1 
ATOM   1660 O  O   . GLU B  1 38  ? 43.732 20.527  59.219  1.00 36.96 ? 39  GLU B O   1 
ATOM   1661 C  CB  . GLU B  1 38  ? 43.308 18.729  56.937  1.00 34.60 ? 39  GLU B CB  1 
ATOM   1662 C  CG  . GLU B  1 38  ? 42.107 18.283  56.121  1.00 43.83 ? 39  GLU B CG  1 
ATOM   1663 C  CD  . GLU B  1 38  ? 41.737 16.791  56.298  1.00 54.89 ? 39  GLU B CD  1 
ATOM   1664 O  OE1 . GLU B  1 38  ? 42.172 16.135  57.279  1.00 49.45 ? 39  GLU B OE1 1 
ATOM   1665 O  OE2 . GLU B  1 38  ? 41.001 16.268  55.426  1.00 65.79 ? 39  GLU B OE2 1 
ATOM   1666 N  N   . ARG B  1 39  ? 45.513 21.239  58.034  1.00 34.93 ? 40  ARG B N   1 
ATOM   1667 C  CA  . ARG B  1 39  ? 46.210 21.756  59.203  1.00 33.14 ? 40  ARG B CA  1 
ATOM   1668 C  C   . ARG B  1 39  ? 45.409 22.898  59.811  1.00 34.29 ? 40  ARG B C   1 
ATOM   1669 O  O   . ARG B  1 39  ? 44.721 23.642  59.108  1.00 32.99 ? 40  ARG B O   1 
ATOM   1670 C  CB  . ARG B  1 39  ? 47.614 22.241  58.829  1.00 32.72 ? 40  ARG B CB  1 
ATOM   1671 C  CG  . ARG B  1 39  ? 48.646 21.129  58.663  1.00 35.66 ? 40  ARG B CG  1 
ATOM   1672 C  CD  . ARG B  1 39  ? 49.925 21.623  57.995  1.00 38.26 ? 40  ARG B CD  1 
ATOM   1673 N  NE  . ARG B  1 39  ? 50.368 22.921  58.487  1.00 41.44 ? 40  ARG B NE  1 
ATOM   1674 C  CZ  . ARG B  1 39  ? 51.607 23.387  58.388  1.00 49.14 ? 40  ARG B CZ  1 
ATOM   1675 N  NH1 . ARG B  1 39  ? 52.577 22.666  57.841  1.00 47.81 ? 40  ARG B NH1 1 
ATOM   1676 N  NH2 . ARG B  1 39  ? 51.880 24.610  58.846  1.00 48.51 ? 40  ARG B NH2 1 
ATOM   1677 N  N   . ASP B  1 40  ? 45.507 23.037  61.136  1.00 37.09 ? 41  ASP B N   1 
ATOM   1678 C  CA  . ASP B  1 40  ? 44.744 24.080  61.825  1.00 36.97 ? 41  ASP B CA  1 
ATOM   1679 C  C   . ASP B  1 40  ? 45.143 25.489  61.377  1.00 36.45 ? 41  ASP B C   1 
ATOM   1680 O  O   . ASP B  1 40  ? 44.307 26.400  61.408  1.00 37.08 ? 41  ASP B O   1 
ATOM   1681 C  CB  . ASP B  1 40  ? 44.905 23.944  63.339  1.00 37.24 ? 41  ASP B CB  1 
ATOM   1682 C  CG  . ASP B  1 40  ? 46.269 24.415  63.821  1.00 42.40 ? 41  ASP B CG  1 
ATOM   1683 O  OD1 . ASP B  1 40  ? 47.198 23.578  63.873  1.00 46.58 ? 41  ASP B OD1 1 
ATOM   1684 O  OD2 . ASP B  1 40  ? 46.427 25.628  64.111  1.00 42.14 ? 41  ASP B OD2 1 
ATOM   1685 N  N   . ASP B  1 41  ? 46.396 25.699  60.965  1.00 33.59 ? 42  ASP B N   1 
ATOM   1686 C  CA  . ASP B  1 41  ? 46.837 27.015  60.510  1.00 35.69 ? 42  ASP B CA  1 
ATOM   1687 C  C   . ASP B  1 41  ? 46.685 27.213  58.995  1.00 36.66 ? 42  ASP B C   1 
ATOM   1688 O  O   . ASP B  1 41  ? 47.162 28.225  58.458  1.00 35.61 ? 42  ASP B O   1 
ATOM   1689 C  CB  . ASP B  1 41  ? 48.290 27.273  60.938  1.00 36.40 ? 42  ASP B CB  1 
ATOM   1690 C  CG  . ASP B  1 41  ? 49.259 26.183  60.469  1.00 42.35 ? 42  ASP B CG  1 
ATOM   1691 O  OD1 . ASP B  1 41  ? 48.821 25.236  59.783  1.00 42.91 ? 42  ASP B OD1 1 
ATOM   1692 O  OD2 . ASP B  1 41  ? 50.473 26.280  60.771  1.00 44.15 ? 42  ASP B OD2 1 
ATOM   1693 N  N   . VAL B  1 42  ? 46.025 26.283  58.302  1.00 33.36 ? 43  VAL B N   1 
ATOM   1694 C  CA  . VAL B  1 42  ? 45.726 26.430  56.879  1.00 34.27 ? 43  VAL B CA  1 
ATOM   1695 C  C   . VAL B  1 42  ? 44.213 26.434  56.671  1.00 33.10 ? 43  VAL B C   1 
ATOM   1696 O  O   . VAL B  1 42  ? 43.646 27.421  56.197  1.00 34.28 ? 43  VAL B O   1 
ATOM   1697 C  CB  . VAL B  1 42  ? 46.389 25.309  56.057  1.00 38.05 ? 43  VAL B CB  1 
ATOM   1698 C  CG1 . VAL B  1 42  ? 46.004 25.434  54.587  1.00 32.34 ? 43  VAL B CG1 1 
ATOM   1699 C  CG2 . VAL B  1 42  ? 47.917 25.308  56.259  1.00 30.74 ? 43  VAL B CG2 1 
ATOM   1700 N  N   . ALA B  1 43  ? 43.563 25.315  56.999  1.00 33.52 ? 44  ALA B N   1 
ATOM   1701 C  CA  . ALA B  1 43  ? 42.105 25.208  57.115  1.00 34.95 ? 44  ALA B CA  1 
ATOM   1702 C  C   . ALA B  1 43  ? 41.392 25.602  55.817  1.00 37.33 ? 44  ALA B C   1 
ATOM   1703 O  O   . ALA B  1 43  ? 40.570 26.525  55.764  1.00 35.07 ? 44  ALA B O   1 
ATOM   1704 C  CB  . ALA B  1 43  ? 41.600 26.031  58.303  1.00 34.47 ? 44  ALA B CB  1 
ATOM   1705 N  N   . LEU B  1 44  ? 41.722 24.871  54.755  1.00 33.07 ? 45  LEU B N   1 
ATOM   1706 C  CA  . LEU B  1 44  ? 41.097 25.036  53.448  1.00 35.55 ? 45  LEU B CA  1 
ATOM   1707 C  C   . LEU B  1 44  ? 40.455 23.699  53.091  1.00 36.71 ? 45  LEU B C   1 
ATOM   1708 O  O   . LEU B  1 44  ? 40.988 22.938  52.269  1.00 36.56 ? 45  LEU B O   1 
ATOM   1709 C  CB  . LEU B  1 44  ? 42.119 25.489  52.409  1.00 36.44 ? 45  LEU B CB  1 
ATOM   1710 C  CG  . LEU B  1 44  ? 42.481 26.973  52.510  1.00 39.63 ? 45  LEU B CG  1 
ATOM   1711 C  CD1 . LEU B  1 44  ? 43.850 27.266  51.883  1.00 34.94 ? 45  LEU B CD1 1 
ATOM   1712 C  CD2 . LEU B  1 44  ? 41.364 27.848  51.892  1.00 32.80 ? 45  LEU B CD2 1 
ATOM   1713 N  N   . PRO B  1 45  ? 39.305 23.384  53.689  1.00 38.58 ? 46  PRO B N   1 
ATOM   1714 C  CA  . PRO B  1 45  ? 38.723 22.037  53.508  1.00 42.60 ? 46  PRO B CA  1 
ATOM   1715 C  C   . PRO B  1 45  ? 38.342 21.709  52.073  1.00 37.17 ? 46  PRO B C   1 
ATOM   1716 O  O   . PRO B  1 45  ? 38.314 20.524  51.711  1.00 39.93 ? 46  PRO B O   1 
ATOM   1717 C  CB  . PRO B  1 45  ? 37.489 22.069  54.418  1.00 40.20 ? 46  PRO B CB  1 
ATOM   1718 C  CG  . PRO B  1 45  ? 37.139 23.545  54.513  1.00 41.79 ? 46  PRO B CG  1 
ATOM   1719 C  CD  . PRO B  1 45  ? 38.447 24.270  54.490  1.00 37.28 ? 46  PRO B CD  1 
ATOM   1720 N  N   . GLY B  1 46  ? 38.040 22.714  51.249  1.00 39.38 ? 47  GLY B N   1 
ATOM   1721 C  CA  . GLY B  1 46  ? 37.774 22.455  49.839  1.00 38.39 ? 47  GLY B CA  1 
ATOM   1722 C  C   . GLY B  1 46  ? 38.989 21.915  49.104  1.00 36.40 ? 47  GLY B C   1 
ATOM   1723 O  O   . GLY B  1 46  ? 38.913 20.882  48.431  1.00 35.32 ? 47  GLY B O   1 
ATOM   1724 N  N   . PHE B  1 47  ? 40.129 22.606  49.220  1.00 35.10 ? 48  PHE B N   1 
ATOM   1725 C  CA  . PHE B  1 47  ? 41.366 22.087  48.631  1.00 37.04 ? 48  PHE B CA  1 
ATOM   1726 C  C   . PHE B  1 47  ? 41.705 20.700  49.175  1.00 37.14 ? 48  PHE B C   1 
ATOM   1727 O  O   . PHE B  1 47  ? 42.134 19.819  48.420  1.00 35.44 ? 48  PHE B O   1 
ATOM   1728 C  CB  . PHE B  1 47  ? 42.522 23.050  48.890  1.00 33.49 ? 48  PHE B CB  1 
ATOM   1729 C  CG  . PHE B  1 47  ? 42.461 24.300  48.063  1.00 38.06 ? 48  PHE B CG  1 
ATOM   1730 C  CD1 . PHE B  1 47  ? 43.032 24.343  46.805  1.00 39.70 ? 48  PHE B CD1 1 
ATOM   1731 C  CD2 . PHE B  1 47  ? 41.824 25.435  48.544  1.00 39.54 ? 48  PHE B CD2 1 
ATOM   1732 C  CE1 . PHE B  1 47  ? 42.977 25.499  46.042  1.00 36.58 ? 48  PHE B CE1 1 
ATOM   1733 C  CE2 . PHE B  1 47  ? 41.767 26.594  47.785  1.00 41.00 ? 48  PHE B CE2 1 
ATOM   1734 C  CZ  . PHE B  1 47  ? 42.348 26.622  46.532  1.00 38.70 ? 48  PHE B CZ  1 
ATOM   1735 N  N   . ALA B  1 48  ? 41.484 20.476  50.474  1.00 32.58 ? 49  ALA B N   1 
ATOM   1736 C  CA  . ALA B  1 48  ? 41.804 19.175  51.058  1.00 37.86 ? 49  ALA B CA  1 
ATOM   1737 C  C   . ALA B  1 48  ? 41.002 18.064  50.388  1.00 36.17 ? 49  ALA B C   1 
ATOM   1738 O  O   . ALA B  1 48  ? 41.562 17.041  49.981  1.00 33.85 ? 49  ALA B O   1 
ATOM   1739 C  CB  . ALA B  1 48  ? 41.554 19.188  52.567  1.00 29.77 ? 49  ALA B CB  1 
ATOM   1740 N  N   . LYS B  1 49  ? 39.682 18.255  50.267  1.00 36.49 ? 50  LYS B N   1 
ATOM   1741 C  CA  . LYS B  1 49  ? 38.833 17.292  49.571  1.00 33.74 ? 50  LYS B CA  1 
ATOM   1742 C  C   . LYS B  1 49  ? 39.303 17.080  48.132  1.00 34.18 ? 50  LYS B C   1 
ATOM   1743 O  O   . LYS B  1 49  ? 39.426 15.943  47.668  1.00 34.22 ? 50  LYS B O   1 
ATOM   1744 C  CB  . LYS B  1 49  ? 37.377 17.775  49.607  1.00 39.85 ? 50  LYS B CB  1 
ATOM   1745 C  CG  . LYS B  1 49  ? 36.389 16.901  48.824  1.00 46.35 ? 50  LYS B CG  1 
ATOM   1746 C  CD  . LYS B  1 49  ? 34.967 17.484  48.832  1.00 58.39 ? 50  LYS B CD  1 
ATOM   1747 C  CE  . LYS B  1 49  ? 33.953 16.576  49.545  1.00 69.17 ? 50  LYS B CE  1 
ATOM   1748 N  NZ  . LYS B  1 49  ? 34.457 15.989  50.827  1.00 76.14 ? 50  LYS B NZ  1 
ATOM   1749 N  N   . PHE B  1 50  ? 39.604 18.165  47.419  1.00 34.89 ? 51  PHE B N   1 
ATOM   1750 C  CA  . PHE B  1 50  ? 40.024 18.036  46.028  1.00 32.92 ? 51  PHE B CA  1 
ATOM   1751 C  C   . PHE B  1 50  ? 41.274 17.166  45.888  1.00 34.77 ? 51  PHE B C   1 
ATOM   1752 O  O   . PHE B  1 50  ? 41.334 16.282  45.027  1.00 33.90 ? 51  PHE B O   1 
ATOM   1753 C  CB  . PHE B  1 50  ? 40.268 19.411  45.419  1.00 31.12 ? 51  PHE B CB  1 
ATOM   1754 C  CG  . PHE B  1 50  ? 40.704 19.345  43.986  1.00 40.06 ? 51  PHE B CG  1 
ATOM   1755 C  CD1 . PHE B  1 50  ? 39.787 19.058  42.983  1.00 40.16 ? 51  PHE B CD1 1 
ATOM   1756 C  CD2 . PHE B  1 50  ? 42.027 19.526  43.643  1.00 36.31 ? 51  PHE B CD2 1 
ATOM   1757 C  CE1 . PHE B  1 50  ? 40.183 18.978  41.659  1.00 41.56 ? 51  PHE B CE1 1 
ATOM   1758 C  CE2 . PHE B  1 50  ? 42.427 19.450  42.322  1.00 43.26 ? 51  PHE B CE2 1 
ATOM   1759 C  CZ  . PHE B  1 50  ? 41.502 19.169  41.328  1.00 40.37 ? 51  PHE B CZ  1 
ATOM   1760 N  N   . PHE B  1 51  ? 42.293 17.401  46.719  1.00 33.98 ? 52  PHE B N   1 
ATOM   1761 C  CA  . PHE B  1 51  ? 43.530 16.632  46.585  1.00 33.52 ? 52  PHE B CA  1 
ATOM   1762 C  C   . PHE B  1 51  ? 43.387 15.211  47.119  1.00 32.91 ? 52  PHE B C   1 
ATOM   1763 O  O   . PHE B  1 51  ? 44.025 14.291  46.601  1.00 32.63 ? 52  PHE B O   1 
ATOM   1764 C  CB  . PHE B  1 51  ? 44.675 17.372  47.277  1.00 29.66 ? 52  PHE B CB  1 
ATOM   1765 C  CG  . PHE B  1 51  ? 45.086 18.616  46.545  1.00 35.51 ? 52  PHE B CG  1 
ATOM   1766 C  CD1 . PHE B  1 51  ? 45.609 18.535  45.266  1.00 33.35 ? 52  PHE B CD1 1 
ATOM   1767 C  CD2 . PHE B  1 51  ? 44.881 19.864  47.097  1.00 33.81 ? 52  PHE B CD2 1 
ATOM   1768 C  CE1 . PHE B  1 51  ? 45.957 19.675  44.572  1.00 34.81 ? 52  PHE B CE1 1 
ATOM   1769 C  CE2 . PHE B  1 51  ? 45.233 21.002  46.405  1.00 35.32 ? 52  PHE B CE2 1 
ATOM   1770 C  CZ  . PHE B  1 51  ? 45.780 20.903  45.139  1.00 30.05 ? 52  PHE B CZ  1 
ATOM   1771 N  N   . LYS B  1 52  ? 42.534 14.997  48.117  1.00 32.58 ? 53  LYS B N   1 
ATOM   1772 C  CA  . LYS B  1 52  ? 42.289 13.632  48.556  1.00 35.76 ? 53  LYS B CA  1 
ATOM   1773 C  C   . LYS B  1 52  ? 41.609 12.820  47.456  1.00 37.73 ? 53  LYS B C   1 
ATOM   1774 O  O   . LYS B  1 52  ? 41.947 11.650  47.240  1.00 34.10 ? 53  LYS B O   1 
ATOM   1775 C  CB  . LYS B  1 52  ? 41.468 13.635  49.846  1.00 33.61 ? 53  LYS B CB  1 
ATOM   1776 C  CG  . LYS B  1 52  ? 41.265 12.259  50.373  1.00 45.49 ? 53  LYS B CG  1 
ATOM   1777 C  CD  . LYS B  1 52  ? 41.177 12.215  51.884  1.00 60.50 ? 53  LYS B CD  1 
ATOM   1778 C  CE  . LYS B  1 52  ? 41.229 10.753  52.376  1.00 64.43 ? 53  LYS B CE  1 
ATOM   1779 N  NZ  . LYS B  1 52  ? 41.655 9.781   51.303  1.00 59.72 ? 53  LYS B NZ  1 
ATOM   1780 N  N   . GLU B  1 53  ? 40.673 13.436  46.729  1.00 31.46 ? 54  GLU B N   1 
ATOM   1781 C  CA  . GLU B  1 53  ? 40.084 12.779  45.568  1.00 36.62 ? 54  GLU B CA  1 
ATOM   1782 C  C   . GLU B  1 53  ? 41.137 12.521  44.488  1.00 33.58 ? 54  GLU B C   1 
ATOM   1783 O  O   . GLU B  1 53  ? 41.153 11.450  43.876  1.00 33.18 ? 54  GLU B O   1 
ATOM   1784 C  CB  . GLU B  1 53  ? 38.917 13.630  45.043  1.00 38.76 ? 54  GLU B CB  1 
ATOM   1785 C  CG  . GLU B  1 53  ? 37.527 13.102  45.495  1.00 51.76 ? 54  GLU B CG  1 
ATOM   1786 C  CD  . GLU B  1 53  ? 36.472 14.204  45.829  1.00 64.38 ? 54  GLU B CD  1 
ATOM   1787 O  OE1 . GLU B  1 53  ? 36.419 15.268  45.156  1.00 61.57 ? 54  GLU B OE1 1 
ATOM   1788 O  OE2 . GLU B  1 53  ? 35.667 13.983  46.772  1.00 65.45 ? 54  GLU B OE2 1 
ATOM   1789 N  N   . SER B  1 54  ? 42.042 13.477  44.263  1.00 30.55 ? 55  SER B N   1 
ATOM   1790 C  CA  . SER B  1 54  ? 43.135 13.266  43.316  1.00 35.76 ? 55  SER B CA  1 
ATOM   1791 C  C   . SER B  1 54  ? 44.062 12.137  43.770  1.00 34.55 ? 55  SER B C   1 
ATOM   1792 O  O   . SER B  1 54  ? 44.596 11.388  42.941  1.00 33.27 ? 55  SER B O   1 
ATOM   1793 C  CB  . SER B  1 54  ? 43.931 14.557  43.151  1.00 34.41 ? 55  SER B CB  1 
ATOM   1794 O  OG  . SER B  1 54  ? 43.156 15.556  42.520  1.00 37.38 ? 55  SER B OG  1 
ATOM   1795 N  N   . SER B  1 55  ? 44.256 11.992  45.085  1.00 32.83 ? 56  SER B N   1 
ATOM   1796 C  CA  . SER B  1 55  ? 45.075 10.896  45.595  1.00 34.29 ? 56  SER B CA  1 
ATOM   1797 C  C   . SER B  1 55  ? 44.443 9.539   45.290  1.00 33.61 ? 56  SER B C   1 
ATOM   1798 O  O   . SER B  1 55  ? 45.113 8.625   44.798  1.00 33.75 ? 56  SER B O   1 
ATOM   1799 C  CB  . SER B  1 55  ? 45.303 11.063  47.097  1.00 30.00 ? 56  SER B CB  1 
ATOM   1800 O  OG  . SER B  1 55  ? 46.192 10.075  47.573  1.00 32.18 ? 56  SER B OG  1 
ATOM   1801 N  N   . ASP B  1 56  ? 43.150 9.389   45.576  1.00 34.56 ? 57  ASP B N   1 
ATOM   1802 C  CA  . ASP B  1 56  ? 42.472 8.124   45.299  1.00 34.85 ? 57  ASP B CA  1 
ATOM   1803 C  C   . ASP B  1 56  ? 42.478 7.807   43.815  1.00 38.66 ? 57  ASP B C   1 
ATOM   1804 O  O   . ASP B  1 56  ? 42.607 6.641   43.420  1.00 35.46 ? 57  ASP B O   1 
ATOM   1805 C  CB  . ASP B  1 56  ? 41.030 8.177   45.804  1.00 41.41 ? 57  ASP B CB  1 
ATOM   1806 C  CG  . ASP B  1 56  ? 40.937 8.367   47.300  1.00 50.35 ? 57  ASP B CG  1 
ATOM   1807 O  OD1 . ASP B  1 56  ? 39.796 8.487   47.807  1.00 57.90 ? 57  ASP B OD1 1 
ATOM   1808 O  OD2 . ASP B  1 56  ? 41.995 8.354   47.974  1.00 54.30 ? 57  ASP B OD2 1 
ATOM   1809 N  N   . CYS B  1 57  ? 42.338 8.837   42.977  1.00 34.52 ? 58  CYS B N   1 
ATOM   1810 C  CA  . CYS B  1 57  ? 42.275 8.622   41.537  1.00 36.05 ? 58  CYS B CA  1 
ATOM   1811 C  C   . CYS B  1 57  ? 43.597 8.080   40.991  1.00 34.84 ? 58  CYS B C   1 
ATOM   1812 O  O   . CYS B  1 57  ? 43.608 7.127   40.210  1.00 32.94 ? 58  CYS B O   1 
ATOM   1813 C  CB  . CYS B  1 57  ? 41.884 9.926   40.847  1.00 32.85 ? 58  CYS B CB  1 
ATOM   1814 S  SG  . CYS B  1 57  ? 42.432 9.999   39.159  1.00 60.13 ? 58  CYS B SG  1 
ATOM   1815 N  N   . CYS B  1 58  ? 44.725 8.678   41.387  1.00 34.66 ? 59  CYS B N   1 
ATOM   1816 C  CA  . CYS B  1 58  ? 46.023 8.178   40.930  1.00 34.48 ? 59  CYS B CA  1 
ATOM   1817 C  C   . CYS B  1 58  ? 46.325 6.771   41.462  1.00 36.16 ? 59  CYS B C   1 
ATOM   1818 O  O   . CYS B  1 58  ? 46.982 5.978   40.773  1.00 35.77 ? 59  CYS B O   1 
ATOM   1819 C  CB  . CYS B  1 58  ? 47.133 9.144   41.345  1.00 31.60 ? 59  CYS B CB  1 
ATOM   1820 S  SG  . CYS B  1 58  ? 47.235 10.651  40.304  1.00 47.52 ? 59  CYS B SG  1 
ATOM   1821 N  N   . ARG B  1 59  ? 45.867 6.437   42.674  1.00 30.58 ? 60  ARG B N   1 
ATOM   1822 C  CA  . ARG B  1 59  ? 46.084 5.079   43.159  1.00 32.63 ? 60  ARG B CA  1 
ATOM   1823 C  C   . ARG B  1 59  ? 45.307 4.072   42.321  1.00 36.25 ? 60  ARG B C   1 
ATOM   1824 O  O   . ARG B  1 59  ? 45.800 2.967   42.052  1.00 35.83 ? 60  ARG B O   1 
ATOM   1825 C  CB  . ARG B  1 59  ? 45.700 4.955   44.632  1.00 33.91 ? 60  ARG B CB  1 
ATOM   1826 C  CG  . ARG B  1 59  ? 45.929 3.542   45.172  1.00 37.35 ? 60  ARG B CG  1 
ATOM   1827 C  CD  . ARG B  1 59  ? 45.622 3.456   46.654  1.00 46.06 ? 60  ARG B CD  1 
ATOM   1828 N  NE  . ARG B  1 59  ? 44.247 3.858   46.923  1.00 49.51 ? 60  ARG B NE  1 
ATOM   1829 C  CZ  . ARG B  1 59  ? 43.912 4.923   47.636  1.00 50.91 ? 60  ARG B CZ  1 
ATOM   1830 N  NH1 . ARG B  1 59  ? 44.833 5.753   48.109  1.00 50.62 ? 60  ARG B NH1 1 
ATOM   1831 N  NH2 . ARG B  1 59  ? 42.622 5.180   47.851  1.00 49.33 ? 60  ARG B NH2 1 
ATOM   1832 N  N   . GLU B  1 60  ? 44.099 4.437   41.880  1.00 33.25 ? 61  GLU B N   1 
ATOM   1833 C  CA  . GLU B  1 60  ? 43.355 3.521   41.026  1.00 38.37 ? 61  GLU B CA  1 
ATOM   1834 C  C   . GLU B  1 60  ? 44.008 3.391   39.658  1.00 36.10 ? 61  GLU B C   1 
ATOM   1835 O  O   . GLU B  1 60  ? 43.972 2.311   39.066  1.00 35.46 ? 61  GLU B O   1 
ATOM   1836 C  CB  . GLU B  1 60  ? 41.895 3.960   40.899  1.00 36.76 ? 61  GLU B CB  1 
ATOM   1837 C  CG  . GLU B  1 60  ? 41.082 3.626   42.158  1.00 52.69 ? 61  GLU B CG  1 
ATOM   1838 C  CD  . GLU B  1 60  ? 40.710 2.133   42.273  1.00 73.64 ? 61  GLU B CD  1 
ATOM   1839 O  OE1 . GLU B  1 60  ? 39.493 1.825   42.355  1.00 75.66 ? 61  GLU B OE1 1 
ATOM   1840 O  OE2 . GLU B  1 60  ? 41.627 1.267   42.271  1.00 65.46 ? 61  GLU B OE2 1 
ATOM   1841 N  N   . HIS B  1 61  ? 44.630 4.464   39.157  1.00 32.59 ? 62  HIS B N   1 
ATOM   1842 C  CA  . HIS B  1 61  ? 45.410 4.355   37.931  1.00 36.72 ? 62  HIS B CA  1 
ATOM   1843 C  C   . HIS B  1 61  ? 46.516 3.322   38.065  1.00 36.13 ? 62  HIS B C   1 
ATOM   1844 O  O   . HIS B  1 61  ? 46.776 2.557   37.129  1.00 33.46 ? 62  HIS B O   1 
ATOM   1845 C  CB  . HIS B  1 61  ? 46.012 5.708   37.563  1.00 41.11 ? 62  HIS B CB  1 
ATOM   1846 C  CG  . HIS B  1 61  ? 45.002 6.692   37.091  1.00 45.93 ? 62  HIS B CG  1 
ATOM   1847 N  ND1 . HIS B  1 61  ? 45.272 8.039   36.959  1.00 47.83 ? 62  HIS B ND1 1 
ATOM   1848 C  CD2 . HIS B  1 61  ? 43.705 6.524   36.743  1.00 44.39 ? 62  HIS B CD2 1 
ATOM   1849 C  CE1 . HIS B  1 61  ? 44.184 8.652   36.523  1.00 58.64 ? 62  HIS B CE1 1 
ATOM   1850 N  NE2 . HIS B  1 61  ? 43.220 7.757   36.390  1.00 58.64 ? 62  HIS B NE2 1 
ATOM   1851 N  N   . ALA B  1 62  ? 47.198 3.303   39.216  1.00 33.19 ? 63  ALA B N   1 
ATOM   1852 C  CA  . ALA B  1 62  ? 48.304 2.368   39.398  1.00 34.82 ? 63  ALA B CA  1 
ATOM   1853 C  C   . ALA B  1 62  ? 47.803 0.929   39.463  1.00 32.99 ? 63  ALA B C   1 
ATOM   1854 O  O   . ALA B  1 62  ? 48.417 0.028   38.882  1.00 32.98 ? 63  ALA B O   1 
ATOM   1855 C  CB  . ALA B  1 62  ? 49.094 2.728   40.659  1.00 28.15 ? 63  ALA B CB  1 
ATOM   1856 N  N   . GLN B  1 63  ? 46.679 0.697   40.149  1.00 32.69 ? 64  GLN B N   1 
ATOM   1857 C  CA  . GLN B  1 63  ? 46.129 -0.650  40.258  1.00 35.27 ? 64  GLN B CA  1 
ATOM   1858 C  C   . GLN B  1 63  ? 45.595 -1.147  38.916  1.00 32.26 ? 64  GLN B C   1 
ATOM   1859 O  O   . GLN B  1 63  ? 45.730 -2.329  38.587  1.00 29.82 ? 64  GLN B O   1 
ATOM   1860 C  CB  . GLN B  1 63  ? 45.032 -0.666  41.315  1.00 33.80 ? 64  GLN B CB  1 
ATOM   1861 C  CG  . GLN B  1 63  ? 45.530 -0.237  42.678  1.00 40.16 ? 64  GLN B CG  1 
ATOM   1862 C  CD  . GLN B  1 63  ? 44.610 -0.670  43.801  1.00 48.29 ? 64  GLN B CD  1 
ATOM   1863 O  OE1 . GLN B  1 63  ? 44.022 -1.759  43.760  1.00 58.99 ? 64  GLN B OE1 1 
ATOM   1864 N  NE2 . GLN B  1 63  ? 44.479 0.179   44.813  1.00 47.98 ? 64  GLN B NE2 1 
ATOM   1865 N  N   . THR B  1 64  ? 44.981 -0.261  38.134  1.00 26.58 ? 65  THR B N   1 
ATOM   1866 C  CA  . THR B  1 64  ? 44.556 -0.639  36.796  1.00 34.12 ? 65  THR B CA  1 
ATOM   1867 C  C   . THR B  1 64  ? 45.754 -1.059  35.950  1.00 33.43 ? 65  THR B C   1 
ATOM   1868 O  O   . THR B  1 64  ? 45.660 -2.006  35.161  1.00 33.10 ? 65  THR B O   1 
ATOM   1869 C  CB  . THR B  1 64  ? 43.784 0.515   36.148  1.00 33.85 ? 65  THR B CB  1 
ATOM   1870 O  OG1 . THR B  1 64  ? 42.561 0.721   36.858  1.00 38.00 ? 65  THR B OG1 1 
ATOM   1871 C  CG2 . THR B  1 64  ? 43.443 0.213   34.684  1.00 39.19 ? 65  THR B CG2 1 
ATOM   1872 N  N   . PHE B  1 65  ? 46.903 -0.396  36.132  1.00 27.51 ? 66  PHE B N   1 
ATOM   1873 C  CA  . PHE B  1 65  ? 48.116 -0.826  35.435  1.00 30.81 ? 66  PHE B CA  1 
ATOM   1874 C  C   . PHE B  1 65  ? 48.634 -2.159  35.966  1.00 30.36 ? 66  PHE B C   1 
ATOM   1875 O  O   . PHE B  1 65  ? 49.148 -2.975  35.192  1.00 28.36 ? 66  PHE B O   1 
ATOM   1876 C  CB  . PHE B  1 65  ? 49.211 0.223   35.555  1.00 31.20 ? 66  PHE B CB  1 
ATOM   1877 C  CG  . PHE B  1 65  ? 49.215 1.225   34.451  1.00 34.60 ? 66  PHE B CG  1 
ATOM   1878 C  CD1 . PHE B  1 65  ? 49.145 0.820   33.125  1.00 35.68 ? 66  PHE B CD1 1 
ATOM   1879 C  CD2 . PHE B  1 65  ? 49.293 2.583   34.736  1.00 36.46 ? 66  PHE B CD2 1 
ATOM   1880 C  CE1 . PHE B  1 65  ? 49.147 1.757   32.097  1.00 36.54 ? 66  PHE B CE1 1 
ATOM   1881 C  CE2 . PHE B  1 65  ? 49.294 3.523   33.718  1.00 36.02 ? 66  PHE B CE2 1 
ATOM   1882 C  CZ  . PHE B  1 65  ? 49.224 3.111   32.399  1.00 39.30 ? 66  PHE B CZ  1 
ATOM   1883 N  N   . MET B  1 66  ? 48.528 -2.402  37.281  1.00 28.84 ? 67  MET B N   1 
ATOM   1884 C  CA  . MET B  1 66  ? 48.965 -3.701  37.792  1.00 30.83 ? 67  MET B CA  1 
ATOM   1885 C  C   . MET B  1 66  ? 48.068 -4.829  37.290  1.00 34.52 ? 67  MET B C   1 
ATOM   1886 O  O   . MET B  1 66  ? 48.560 -5.918  36.964  1.00 32.09 ? 67  MET B O   1 
ATOM   1887 C  CB  . MET B  1 66  ? 49.029 -3.716  39.322  1.00 31.48 ? 67  MET B CB  1 
ATOM   1888 C  CG  . MET B  1 66  ? 49.911 -2.634  39.927  1.00 27.12 ? 67  MET B CG  1 
ATOM   1889 S  SD  . MET B  1 66  ? 49.681 -2.392  41.692  1.00 36.57 ? 67  MET B SD  1 
ATOM   1890 C  CE  . MET B  1 66  ? 50.305 -3.929  42.340  1.00 33.31 ? 67  MET B CE  1 
ATOM   1891 N  N   . LYS B  1 67  ? 46.753 -4.587  37.222  1.00 26.81 ? 68  LYS B N   1 
ATOM   1892 C  CA  . LYS B  1 67  ? 45.847 -5.573  36.646  1.00 31.94 ? 68  LYS B CA  1 
ATOM   1893 C  C   . LYS B  1 67  ? 46.243 -5.881  35.212  1.00 30.74 ? 68  LYS B C   1 
ATOM   1894 O  O   . LYS B  1 67  ? 46.328 -7.047  34.813  1.00 31.22 ? 68  LYS B O   1 
ATOM   1895 C  CB  . LYS B  1 67  ? 44.400 -5.058  36.700  1.00 31.50 ? 68  LYS B CB  1 
ATOM   1896 C  CG  . LYS B  1 67  ? 43.588 -5.580  37.881  1.00 40.24 ? 68  LYS B CG  1 
ATOM   1897 C  CD  . LYS B  1 67  ? 42.283 -4.799  38.048  1.00 48.09 ? 68  LYS B CD  1 
ATOM   1898 C  CE  . LYS B  1 67  ? 42.398 -3.749  39.155  1.00 48.28 ? 68  LYS B CE  1 
ATOM   1899 N  NZ  . LYS B  1 67  ? 42.494 -4.406  40.492  1.00 51.65 ? 68  LYS B NZ  1 
ATOM   1900 N  N   . TYR B  1 68  ? 46.492 -4.829  34.424  1.00 30.55 ? 69  TYR B N   1 
ATOM   1901 C  CA  . TYR B  1 68  ? 46.846 -4.993  33.019  1.00 32.75 ? 69  TYR B CA  1 
ATOM   1902 C  C   . TYR B  1 68  ? 48.121 -5.809  32.858  1.00 30.86 ? 69  TYR B C   1 
ATOM   1903 O  O   . TYR B  1 68  ? 48.216 -6.654  31.962  1.00 33.79 ? 69  TYR B O   1 
ATOM   1904 C  CB  . TYR B  1 68  ? 47.009 -3.619  32.361  1.00 31.61 ? 69  TYR B CB  1 
ATOM   1905 C  CG  . TYR B  1 68  ? 47.171 -3.719  30.868  1.00 31.89 ? 69  TYR B CG  1 
ATOM   1906 C  CD1 . TYR B  1 68  ? 46.062 -3.837  30.049  1.00 32.70 ? 69  TYR B CD1 1 
ATOM   1907 C  CD2 . TYR B  1 68  ? 48.430 -3.735  30.284  1.00 28.46 ? 69  TYR B CD2 1 
ATOM   1908 C  CE1 . TYR B  1 68  ? 46.196 -3.949  28.694  1.00 32.93 ? 69  TYR B CE1 1 
ATOM   1909 C  CE2 . TYR B  1 68  ? 48.576 -3.846  28.929  1.00 31.38 ? 69  TYR B CE2 1 
ATOM   1910 C  CZ  . TYR B  1 68  ? 47.451 -3.957  28.134  1.00 34.09 ? 69  TYR B CZ  1 
ATOM   1911 O  OH  . TYR B  1 68  ? 47.570 -4.084  26.761  1.00 34.62 ? 69  TYR B OH  1 
ATOM   1912 N  N   . GLN B  1 69  ? 49.117 -5.554  33.708  1.00 29.92 ? 70  GLN B N   1 
ATOM   1913 C  CA  . GLN B  1 69  ? 50.363 -6.316  33.658  1.00 33.83 ? 70  GLN B CA  1 
ATOM   1914 C  C   . GLN B  1 69  ? 50.098 -7.812  33.819  1.00 33.04 ? 70  GLN B C   1 
ATOM   1915 O  O   . GLN B  1 69  ? 50.646 -8.629  33.072  1.00 33.08 ? 70  GLN B O   1 
ATOM   1916 C  CB  . GLN B  1 69  ? 51.318 -5.788  34.737  1.00 32.01 ? 70  GLN B CB  1 
ATOM   1917 C  CG  . GLN B  1 69  ? 52.754 -6.293  34.683  1.00 37.52 ? 70  GLN B CG  1 
ATOM   1918 C  CD  . GLN B  1 69  ? 53.596 -5.576  33.638  1.00 36.79 ? 70  GLN B CD  1 
ATOM   1919 O  OE1 . GLN B  1 69  ? 53.477 -5.857  32.447  1.00 37.85 ? 70  GLN B OE1 1 
ATOM   1920 N  NE2 . GLN B  1 69  ? 54.446 -4.644  34.077  1.00 32.04 ? 70  GLN B NE2 1 
ATOM   1921 N  N   . ASN B  1 70  ? 49.228 -8.185  34.766  1.00 32.16 ? 71  ASN B N   1 
ATOM   1922 C  CA  . ASN B  1 70  ? 48.884 -9.593  34.963  1.00 34.84 ? 71  ASN B CA  1 
ATOM   1923 C  C   . ASN B  1 70  ? 48.062 -10.139 33.797  1.00 35.07 ? 71  ASN B C   1 
ATOM   1924 O  O   . ASN B  1 70  ? 48.272 -11.283 33.367  1.00 31.90 ? 71  ASN B O   1 
ATOM   1925 C  CB  . ASN B  1 70  ? 48.115 -9.777  36.278  1.00 31.92 ? 71  ASN B CB  1 
ATOM   1926 C  CG  . ASN B  1 70  ? 49.038 -9.904  37.479  1.00 38.26 ? 71  ASN B CG  1 
ATOM   1927 O  OD1 . ASN B  1 70  ? 50.260 -10.038 37.323  1.00 34.81 ? 71  ASN B OD1 1 
ATOM   1928 N  ND2 . ASN B  1 70  ? 48.465 -9.842  38.685  1.00 35.20 ? 71  ASN B ND2 1 
ATOM   1929 N  N   . LYS B  1 71  ? 47.109 -9.343  33.292  1.00 32.02 ? 72  LYS B N   1 
ATOM   1930 C  CA  . LYS B  1 71  ? 46.293 -9.762  32.154  1.00 32.49 ? 72  LYS B CA  1 
ATOM   1931 C  C   . LYS B  1 71  ? 47.160 -10.176 30.970  1.00 31.06 ? 72  LYS B C   1 
ATOM   1932 O  O   . LYS B  1 71  ? 46.901 -11.206 30.337  1.00 32.62 ? 72  LYS B O   1 
ATOM   1933 C  CB  . LYS B  1 71  ? 45.350 -8.624  31.758  1.00 32.81 ? 72  LYS B CB  1 
ATOM   1934 C  CG  . LYS B  1 71  ? 43.975 -9.037  31.320  1.00 42.16 ? 72  LYS B CG  1 
ATOM   1935 C  CD  . LYS B  1 71  ? 43.126 -7.777  31.129  1.00 52.51 ? 72  LYS B CD  1 
ATOM   1936 C  CE  . LYS B  1 71  ? 42.806 -7.142  32.494  1.00 49.98 ? 72  LYS B CE  1 
ATOM   1937 N  NZ  . LYS B  1 71  ? 42.823 -5.634  32.552  1.00 39.84 ? 72  LYS B NZ  1 
ATOM   1938 N  N   . ARG B  1 72  ? 48.194 -9.390  30.657  1.00 28.12 ? 73  ARG B N   1 
ATOM   1939 C  CA  . ARG B  1 72  ? 49.055 -9.671  29.513  1.00 28.86 ? 73  ARG B CA  1 
ATOM   1940 C  C   . ARG B  1 72  ? 50.139 -10.692 29.824  1.00 30.02 ? 73  ARG B C   1 
ATOM   1941 O  O   . ARG B  1 72  ? 50.868 -11.090 28.911  1.00 31.11 ? 73  ARG B O   1 
ATOM   1942 C  CB  . ARG B  1 72  ? 49.735 -8.391  28.999  1.00 29.24 ? 73  ARG B CB  1 
ATOM   1943 C  CG  . ARG B  1 72  ? 48.806 -7.310  28.454  1.00 31.26 ? 73  ARG B CG  1 
ATOM   1944 C  CD  . ARG B  1 72  ? 47.931 -7.818  27.297  1.00 32.40 ? 73  ARG B CD  1 
ATOM   1945 N  NE  . ARG B  1 72  ? 48.708 -8.211  26.127  1.00 33.04 ? 73  ARG B NE  1 
ATOM   1946 C  CZ  . ARG B  1 72  ? 49.277 -7.358  25.284  1.00 35.37 ? 73  ARG B CZ  1 
ATOM   1947 N  NH1 . ARG B  1 72  ? 49.190 -6.044  25.462  1.00 32.59 ? 73  ARG B NH1 1 
ATOM   1948 N  NH2 . ARG B  1 72  ? 49.936 -7.832  24.227  1.00 32.41 ? 73  ARG B NH2 1 
ATOM   1949 N  N   . GLY B  1 73  ? 50.286 -11.106 31.076  1.00 30.79 ? 74  GLY B N   1 
ATOM   1950 C  CA  . GLY B  1 73  ? 51.317 -12.061 31.427  1.00 29.16 ? 74  GLY B CA  1 
ATOM   1951 C  C   . GLY B  1 73  ? 52.682 -11.474 31.722  1.00 36.13 ? 74  GLY B C   1 
ATOM   1952 O  O   . GLY B  1 73  ? 53.651 -12.235 31.825  1.00 36.76 ? 74  GLY B O   1 
ATOM   1953 N  N   . GLY B  1 74  ? 52.799 -10.135 31.839  1.00 35.63 ? 75  GLY B N   1 
ATOM   1954 C  CA  . GLY B  1 74  ? 53.999 -9.529  32.374  1.00 35.72 ? 75  GLY B CA  1 
ATOM   1955 C  C   . GLY B  1 74  ? 54.060 -9.680  33.889  1.00 38.57 ? 75  GLY B C   1 
ATOM   1956 O  O   . GLY B  1 74  ? 53.139 -10.177 34.540  1.00 39.75 ? 75  GLY B O   1 
ATOM   1957 N  N   . ARG B  1 75  ? 55.169 -9.242  34.473  1.00 32.30 ? 76  ARG B N   1 
ATOM   1958 C  CA  . ARG B  1 75  ? 55.362 -9.377  35.909  1.00 34.30 ? 76  ARG B CA  1 
ATOM   1959 C  C   . ARG B  1 75  ? 55.533 -8.011  36.558  1.00 37.52 ? 76  ARG B C   1 
ATOM   1960 O  O   . ARG B  1 75  ? 56.404 -7.226  36.160  1.00 33.19 ? 76  ARG B O   1 
ATOM   1961 C  CB  . ARG B  1 75  ? 56.553 -10.281 36.219  1.00 35.97 ? 76  ARG B CB  1 
ATOM   1962 C  CG  . ARG B  1 75  ? 56.276 -11.747 35.866  1.00 33.25 ? 76  ARG B CG  1 
ATOM   1963 C  CD  . ARG B  1 75  ? 55.086 -12.311 36.688  1.00 38.24 ? 76  ARG B CD  1 
ATOM   1964 N  NE  . ARG B  1 75  ? 54.496 -13.505 36.076  1.00 43.90 ? 76  ARG B NE  1 
ATOM   1965 C  CZ  . ARG B  1 75  ? 53.283 -13.572 35.532  1.00 44.58 ? 76  ARG B CZ  1 
ATOM   1966 N  NH1 . ARG B  1 75  ? 52.464 -12.523 35.513  1.00 37.27 ? 76  ARG B NH1 1 
ATOM   1967 N  NH2 . ARG B  1 75  ? 52.871 -14.728 35.012  1.00 46.10 ? 76  ARG B NH2 1 
ATOM   1968 N  N   . ILE B  1 76  ? 54.700 -7.743  37.568  1.00 34.00 ? 77  ILE B N   1 
ATOM   1969 C  CA  . ILE B  1 76  ? 54.763 -6.491  38.306  1.00 34.07 ? 77  ILE B CA  1 
ATOM   1970 C  C   . ILE B  1 76  ? 56.046 -6.451  39.117  1.00 36.62 ? 77  ILE B C   1 
ATOM   1971 O  O   . ILE B  1 76  ? 56.406 -7.424  39.798  1.00 35.81 ? 77  ILE B O   1 
ATOM   1972 C  CB  . ILE B  1 76  ? 53.537 -6.347  39.217  1.00 34.03 ? 77  ILE B CB  1 
ATOM   1973 C  CG1 . ILE B  1 76  ? 52.256 -6.371  38.394  1.00 31.09 ? 77  ILE B CG1 1 
ATOM   1974 C  CG2 . ILE B  1 76  ? 53.617 -5.072  40.048  1.00 29.70 ? 77  ILE B CG2 1 
ATOM   1975 C  CD1 . ILE B  1 76  ? 51.054 -6.815  39.210  1.00 32.49 ? 77  ILE B CD1 1 
ATOM   1976 N  N   . VAL B  1 77  ? 56.747 -5.327  39.052  1.00 34.28 ? 78  VAL B N   1 
ATOM   1977 C  CA  . VAL B  1 77  ? 57.955 -5.111  39.834  1.00 31.70 ? 78  VAL B CA  1 
ATOM   1978 C  C   . VAL B  1 77  ? 57.767 -3.773  40.533  1.00 36.07 ? 78  VAL B C   1 
ATOM   1979 O  O   . VAL B  1 77  ? 57.698 -2.729  39.867  1.00 37.37 ? 78  VAL B O   1 
ATOM   1980 C  CB  . VAL B  1 77  ? 59.223 -5.119  38.965  1.00 40.20 ? 78  VAL B CB  1 
ATOM   1981 C  CG1 . VAL B  1 77  ? 60.446 -4.692  39.778  1.00 33.18 ? 78  VAL B CG1 1 
ATOM   1982 C  CG2 . VAL B  1 77  ? 59.439 -6.505  38.358  1.00 39.19 ? 78  VAL B CG2 1 
ATOM   1983 N  N   . LEU B  1 78  ? 57.642 -3.803  41.862  1.00 34.55 ? 79  LEU B N   1 
ATOM   1984 C  CA  . LEU B  1 78  ? 57.393 -2.612  42.664  1.00 33.24 ? 79  LEU B CA  1 
ATOM   1985 C  C   . LEU B  1 78  ? 58.705 -2.066  43.209  1.00 34.29 ? 79  LEU B C   1 
ATOM   1986 O  O   . LEU B  1 78  ? 59.571 -2.823  43.661  1.00 35.61 ? 79  LEU B O   1 
ATOM   1987 C  CB  . LEU B  1 78  ? 56.429 -2.909  43.820  1.00 29.55 ? 79  LEU B CB  1 
ATOM   1988 C  CG  . LEU B  1 78  ? 55.070 -3.471  43.379  1.00 33.37 ? 79  LEU B CG  1 
ATOM   1989 C  CD1 . LEU B  1 78  ? 54.218 -3.861  44.586  1.00 31.84 ? 79  LEU B CD1 1 
ATOM   1990 C  CD2 . LEU B  1 78  ? 54.332 -2.461  42.484  1.00 29.28 ? 79  LEU B CD2 1 
ATOM   1991 N  N   . GLN B  1 79  ? 58.854 -0.748  43.144  1.00 34.89 ? 80  GLN B N   1 
ATOM   1992 C  CA  . GLN B  1 79  ? 60.021 -0.043  43.657  1.00 32.87 ? 80  GLN B CA  1 
ATOM   1993 C  C   . GLN B  1 79  ? 59.596 0.866   44.807  1.00 33.50 ? 80  GLN B C   1 
ATOM   1994 O  O   . GLN B  1 79  ? 58.402 1.008   45.105  1.00 28.45 ? 80  GLN B O   1 
ATOM   1995 C  CB  . GLN B  1 79  ? 60.704 0.821   42.581  1.00 34.12 ? 80  GLN B CB  1 
ATOM   1996 C  CG  . GLN B  1 79  ? 60.823 0.307   41.153  1.00 38.74 ? 80  GLN B CG  1 
ATOM   1997 C  CD  . GLN B  1 79  ? 60.435 1.397   40.108  1.00 50.21 ? 80  GLN B CD  1 
ATOM   1998 O  OE1 . GLN B  1 79  ? 60.770 2.596   40.257  1.00 43.09 ? 80  GLN B OE1 1 
ATOM   1999 N  NE2 . GLN B  1 79  ? 59.759 0.971   39.031  1.00 45.16 ? 80  GLN B NE2 1 
ATOM   2000 N  N   A GLN B  1 80  ? 60.595 1.512   45.431  0.59 29.93 ? 81  GLN B N   1 
ATOM   2001 N  N   B GLN B  1 80  ? 60.585 1.500   45.431  0.41 30.43 ? 81  GLN B N   1 
ATOM   2002 C  CA  A GLN B  1 80  ? 60.345 2.529   46.448  0.59 30.17 ? 81  GLN B CA  1 
ATOM   2003 C  CA  B GLN B  1 80  ? 60.310 2.480   46.468  0.41 30.19 ? 81  GLN B CA  1 
ATOM   2004 C  C   A GLN B  1 80  ? 59.417 3.607   45.905  0.59 30.08 ? 81  GLN B C   1 
ATOM   2005 C  C   B GLN B  1 80  ? 59.439 3.609   45.922  0.41 30.35 ? 81  GLN B C   1 
ATOM   2006 O  O   A GLN B  1 80  ? 59.458 3.963   44.724  0.59 30.16 ? 81  GLN B O   1 
ATOM   2007 O  O   B GLN B  1 80  ? 59.528 3.988   44.750  0.41 30.20 ? 81  GLN B O   1 
ATOM   2008 C  CB  A GLN B  1 80  ? 61.665 3.181   46.915  0.59 30.27 ? 81  GLN B CB  1 
ATOM   2009 C  CB  B GLN B  1 80  ? 61.623 3.042   47.022  0.41 30.33 ? 81  GLN B CB  1 
ATOM   2010 C  CG  A GLN B  1 80  ? 61.526 4.235   48.055  0.59 30.49 ? 81  GLN B CG  1 
ATOM   2011 C  CG  B GLN B  1 80  ? 62.380 3.953   46.060  0.41 30.14 ? 81  GLN B CG  1 
ATOM   2012 C  CD  A GLN B  1 80  ? 62.678 5.270   48.107  0.59 34.85 ? 81  GLN B CD  1 
ATOM   2013 C  CD  B GLN B  1 80  ? 63.325 3.200   45.128  0.41 31.94 ? 81  GLN B CD  1 
ATOM   2014 O  OE1 A GLN B  1 80  ? 63.566 5.200   48.959  0.59 29.44 ? 81  GLN B OE1 1 
ATOM   2015 O  OE1 B GLN B  1 80  ? 63.106 2.031   44.801  0.41 29.03 ? 81  GLN B OE1 1 
ATOM   2016 N  NE2 A GLN B  1 80  ? 62.639 6.239   47.205  0.59 34.47 ? 81  GLN B NE2 1 
ATOM   2017 N  NE2 B GLN B  1 80  ? 64.377 3.878   44.687  0.41 32.12 ? 81  GLN B NE2 1 
ATOM   2018 N  N   . ILE B  1 81  ? 58.576 4.136   46.782  1.00 28.98 ? 82  ILE B N   1 
ATOM   2019 C  CA  . ILE B  1 81  ? 57.815 5.337   46.493  1.00 28.94 ? 82  ILE B CA  1 
ATOM   2020 C  C   . ILE B  1 81  ? 58.541 6.480   47.189  1.00 29.60 ? 82  ILE B C   1 
ATOM   2021 O  O   . ILE B  1 81  ? 58.613 6.527   48.422  1.00 30.40 ? 82  ILE B O   1 
ATOM   2022 C  CB  . ILE B  1 81  ? 56.356 5.220   46.945  1.00 25.17 ? 82  ILE B CB  1 
ATOM   2023 C  CG1 . ILE B  1 81  ? 55.753 3.899   46.442  1.00 30.18 ? 82  ILE B CG1 1 
ATOM   2024 C  CG2 . ILE B  1 81  ? 55.548 6.386   46.389  1.00 27.00 ? 82  ILE B CG2 1 
ATOM   2025 C  CD1 . ILE B  1 81  ? 54.353 3.607   46.996  1.00 30.21 ? 82  ILE B CD1 1 
ATOM   2026 N  N   . ALA B  1 82  ? 59.108 7.382   46.393  1.00 28.74 ? 83  ALA B N   1 
ATOM   2027 C  CA  . ALA B  1 82  ? 59.850 8.519   46.928  1.00 33.00 ? 83  ALA B CA  1 
ATOM   2028 C  C   . ALA B  1 82  ? 58.952 9.380   47.800  1.00 32.93 ? 83  ALA B C   1 
ATOM   2029 O  O   . ALA B  1 82  ? 57.746 9.508   47.552  1.00 32.38 ? 83  ALA B O   1 
ATOM   2030 C  CB  . ALA B  1 82  ? 60.423 9.382   45.788  1.00 25.42 ? 83  ALA B CB  1 
ATOM   2031 N  N   . ALA B  1 83  ? 59.557 9.978   48.824  1.00 31.51 ? 84  ALA B N   1 
ATOM   2032 C  CA  . ALA B  1 83  ? 58.860 10.983  49.620  1.00 36.17 ? 84  ALA B CA  1 
ATOM   2033 C  C   . ALA B  1 83  ? 58.456 12.154  48.730  1.00 36.22 ? 84  ALA B C   1 
ATOM   2034 O  O   . ALA B  1 83  ? 59.179 12.491  47.785  1.00 34.75 ? 84  ALA B O   1 
ATOM   2035 C  CB  . ALA B  1 83  ? 59.750 11.489  50.756  1.00 33.64 ? 84  ALA B CB  1 
ATOM   2036 N  N   . PRO B  1 84  ? 57.313 12.784  48.983  1.00 35.65 ? 85  PRO B N   1 
ATOM   2037 C  CA  . PRO B  1 84  ? 56.964 14.000  48.236  1.00 36.47 ? 85  PRO B CA  1 
ATOM   2038 C  C   . PRO B  1 84  ? 58.090 15.024  48.312  1.00 40.75 ? 85  PRO B C   1 
ATOM   2039 O  O   . PRO B  1 84  ? 58.740 15.181  49.348  1.00 38.13 ? 85  PRO B O   1 
ATOM   2040 C  CB  . PRO B  1 84  ? 55.701 14.496  48.941  1.00 36.48 ? 85  PRO B CB  1 
ATOM   2041 C  CG  . PRO B  1 84  ? 55.098 13.249  49.532  1.00 35.26 ? 85  PRO B CG  1 
ATOM   2042 C  CD  . PRO B  1 84  ? 56.278 12.407  49.961  1.00 32.80 ? 85  PRO B CD  1 
ATOM   2043 N  N   . SER B  1 85  ? 58.327 15.716  47.193  1.00 46.48 ? 86  SER B N   1 
ATOM   2044 C  CA  . SER B  1 85  ? 59.413 16.695  47.137  1.00 49.86 ? 86  SER B CA  1 
ATOM   2045 C  C   . SER B  1 85  ? 59.237 17.791  48.178  1.00 45.35 ? 86  SER B C   1 
ATOM   2046 O  O   . SER B  1 85  ? 60.229 18.325  48.679  1.00 45.10 ? 86  SER B O   1 
ATOM   2047 C  CB  . SER B  1 85  ? 59.502 17.318  45.740  1.00 53.25 ? 86  SER B CB  1 
ATOM   2048 O  OG  . SER B  1 85  ? 58.218 17.709  45.264  1.00 60.18 ? 86  SER B OG  1 
ATOM   2049 N  N   . MET B  1 86  ? 57.988 18.125  48.520  1.00 49.93 ? 87  MET B N   1 
ATOM   2050 C  CA  . MET B  1 86  ? 57.639 19.109  49.540  1.00 48.62 ? 87  MET B CA  1 
ATOM   2051 C  C   . MET B  1 86  ? 56.840 18.473  50.665  1.00 48.60 ? 87  MET B C   1 
ATOM   2052 O  O   . MET B  1 86  ? 56.150 17.470  50.470  1.00 54.13 ? 87  MET B O   1 
ATOM   2053 C  CB  . MET B  1 86  ? 56.786 20.250  48.967  1.00 53.31 ? 87  MET B CB  1 
ATOM   2054 C  CG  . MET B  1 86  ? 57.253 20.802  47.648  1.00 59.02 ? 87  MET B CG  1 
ATOM   2055 S  SD  . MET B  1 86  ? 58.494 22.054  47.971  1.00 76.26 ? 87  MET B SD  1 
ATOM   2056 C  CE  . MET B  1 86  ? 57.445 23.512  47.909  1.00 62.51 ? 87  MET B CE  1 
ATOM   2057 N  N   . GLN B  1 87  ? 56.917 19.087  51.844  1.00 48.70 ? 88  GLN B N   1 
ATOM   2058 C  CA  . GLN B  1 87  ? 55.991 18.800  52.926  1.00 47.17 ? 88  GLN B CA  1 
ATOM   2059 C  C   . GLN B  1 87  ? 54.990 19.926  53.152  1.00 51.52 ? 88  GLN B C   1 
ATOM   2060 O  O   . GLN B  1 87  ? 53.914 19.671  53.709  1.00 48.01 ? 88  GLN B O   1 
ATOM   2061 C  CB  . GLN B  1 87  ? 56.746 18.537  54.241  1.00 50.18 ? 88  GLN B CB  1 
ATOM   2062 C  CG  . GLN B  1 87  ? 57.832 17.455  54.179  1.00 49.89 ? 88  GLN B CG  1 
ATOM   2063 C  CD  . GLN B  1 87  ? 57.277 16.049  53.944  1.00 47.82 ? 88  GLN B CD  1 
ATOM   2064 O  OE1 . GLN B  1 87  ? 56.174 15.711  54.393  1.00 39.24 ? 88  GLN B OE1 1 
ATOM   2065 N  NE2 . GLN B  1 87  ? 58.061 15.214  53.263  1.00 43.68 ? 88  GLN B NE2 1 
ATOM   2066 N  N   . GLU B  1 88  ? 55.322 21.152  52.742  1.00 49.28 ? 89  GLU B N   1 
ATOM   2067 C  CA  . GLU B  1 88  ? 54.442 22.309  52.849  1.00 49.24 ? 89  GLU B CA  1 
ATOM   2068 C  C   . GLU B  1 88  ? 54.204 22.865  51.455  1.00 48.46 ? 89  GLU B C   1 
ATOM   2069 O  O   . GLU B  1 88  ? 55.155 23.052  50.691  1.00 49.07 ? 89  GLU B O   1 
ATOM   2070 C  CB  . GLU B  1 88  ? 55.047 23.396  53.729  1.00 51.81 ? 89  GLU B CB  1 
ATOM   2071 C  CG  . GLU B  1 88  ? 55.229 23.015  55.170  1.00 58.92 ? 89  GLU B CG  1 
ATOM   2072 C  CD  . GLU B  1 88  ? 55.712 24.193  56.000  1.00 71.02 ? 89  GLU B CD  1 
ATOM   2073 O  OE1 . GLU B  1 88  ? 54.881 25.076  56.322  1.00 73.91 ? 89  GLU B OE1 1 
ATOM   2074 O  OE2 . GLU B  1 88  ? 56.924 24.245  56.309  1.00 71.49 ? 89  GLU B OE2 1 
ATOM   2075 N  N   . TRP B  1 89  ? 52.945 23.148  51.133  1.00 45.16 ? 90  TRP B N   1 
ATOM   2076 C  CA  . TRP B  1 89  ? 52.566 23.438  49.758  1.00 45.28 ? 90  TRP B CA  1 
ATOM   2077 C  C   . TRP B  1 89  ? 52.199 24.897  49.535  1.00 44.29 ? 90  TRP B C   1 
ATOM   2078 O  O   . TRP B  1 89  ? 51.720 25.247  48.450  1.00 44.36 ? 90  TRP B O   1 
ATOM   2079 C  CB  . TRP B  1 89  ? 51.438 22.496  49.343  1.00 38.35 ? 90  TRP B CB  1 
ATOM   2080 C  CG  . TRP B  1 89  ? 51.970 21.104  49.362  1.00 41.20 ? 90  TRP B CG  1 
ATOM   2081 C  CD1 . TRP B  1 89  ? 51.859 20.190  50.370  1.00 40.66 ? 90  TRP B CD1 1 
ATOM   2082 C  CD2 . TRP B  1 89  ? 52.765 20.489  48.346  1.00 44.24 ? 90  TRP B CD2 1 
ATOM   2083 N  NE1 . TRP B  1 89  ? 52.525 19.030  50.036  1.00 39.73 ? 90  TRP B NE1 1 
ATOM   2084 C  CE2 . TRP B  1 89  ? 53.082 19.187  48.792  1.00 44.54 ? 90  TRP B CE2 1 
ATOM   2085 C  CE3 . TRP B  1 89  ? 53.219 20.906  47.083  1.00 46.51 ? 90  TRP B CE3 1 
ATOM   2086 C  CZ2 . TRP B  1 89  ? 53.846 18.302  48.028  1.00 47.46 ? 90  TRP B CZ2 1 
ATOM   2087 C  CZ3 . TRP B  1 89  ? 53.970 20.024  46.322  1.00 44.41 ? 90  TRP B CZ3 1 
ATOM   2088 C  CH2 . TRP B  1 89  ? 54.281 18.737  46.800  1.00 45.57 ? 90  TRP B CH2 1 
ATOM   2089 N  N   . GLY B  1 90  ? 52.435 25.758  50.522  1.00 43.44 ? 91  GLY B N   1 
ATOM   2090 C  CA  . GLY B  1 90  ? 52.218 27.182  50.319  1.00 40.88 ? 91  GLY B CA  1 
ATOM   2091 C  C   . GLY B  1 90  ? 50.744 27.536  50.270  1.00 44.10 ? 91  GLY B C   1 
ATOM   2092 O  O   . GLY B  1 90  ? 49.936 27.057  51.075  1.00 49.55 ? 91  GLY B O   1 
ATOM   2093 N  N   . THR B  1 91  ? 50.387 28.394  49.316  1.00 43.48 ? 92  THR B N   1 
ATOM   2094 C  CA  . THR B  1 91  ? 49.010 28.831  49.129  1.00 44.64 ? 92  THR B CA  1 
ATOM   2095 C  C   . THR B  1 91  ? 48.234 27.834  48.280  1.00 40.96 ? 92  THR B C   1 
ATOM   2096 O  O   . THR B  1 91  ? 48.799 26.941  47.645  1.00 41.30 ? 92  THR B O   1 
ATOM   2097 C  CB  . THR B  1 91  ? 48.972 30.182  48.443  1.00 43.06 ? 92  THR B CB  1 
ATOM   2098 O  OG1 . THR B  1 91  ? 49.574 30.040  47.151  1.00 40.85 ? 92  THR B OG1 1 
ATOM   2099 C  CG2 . THR B  1 91  ? 49.740 31.222  49.262  1.00 40.90 ? 92  THR B CG2 1 
ATOM   2100 N  N   . GLY B  1 92  ? 46.919 28.026  48.237  1.00 39.56 ? 93  GLY B N   1 
ATOM   2101 C  CA  . GLY B  1 92  ? 46.091 27.170  47.403  1.00 38.77 ? 93  GLY B CA  1 
ATOM   2102 C  C   . GLY B  1 92  ? 46.466 27.258  45.936  1.00 40.74 ? 93  GLY B C   1 
ATOM   2103 O  O   . GLY B  1 92  ? 46.470 26.251  45.221  1.00 41.83 ? 93  GLY B O   1 
ATOM   2104 N  N   . LEU B  1 93  ? 46.810 28.460  45.474  1.00 38.73 ? 94  LEU B N   1 
ATOM   2105 C  CA  . LEU B  1 93  ? 47.231 28.631  44.090  1.00 36.43 ? 94  LEU B CA  1 
ATOM   2106 C  C   . LEU B  1 93  ? 48.526 27.875  43.806  1.00 41.64 ? 94  LEU B C   1 
ATOM   2107 O  O   . LEU B  1 93  ? 48.637 27.197  42.777  1.00 40.17 ? 94  LEU B O   1 
ATOM   2108 C  CB  . LEU B  1 93  ? 47.387 30.122  43.777  1.00 35.96 ? 94  LEU B CB  1 
ATOM   2109 C  CG  . LEU B  1 93  ? 47.813 30.489  42.355  1.00 39.80 ? 94  LEU B CG  1 
ATOM   2110 C  CD1 . LEU B  1 93  ? 46.815 29.949  41.339  1.00 35.62 ? 94  LEU B CD1 1 
ATOM   2111 C  CD2 . LEU B  1 93  ? 47.939 31.992  42.235  1.00 33.72 ? 94  LEU B CD2 1 
ATOM   2112 N  N   . GLU B  1 94  ? 49.510 27.971  44.710  1.00 39.08 ? 95  GLU B N   1 
ATOM   2113 C  CA  . GLU B  1 94  ? 50.774 27.264  44.508  1.00 40.82 ? 95  GLU B CA  1 
ATOM   2114 C  C   . GLU B  1 94  ? 50.571 25.753  44.449  1.00 34.04 ? 95  GLU B C   1 
ATOM   2115 O  O   . GLU B  1 94  ? 51.219 25.067  43.650  1.00 33.04 ? 95  GLU B O   1 
ATOM   2116 C  CB  . GLU B  1 94  ? 51.767 27.639  45.607  1.00 37.53 ? 95  GLU B CB  1 
ATOM   2117 C  CG  . GLU B  1 94  ? 52.357 29.021  45.402  1.00 47.51 ? 95  GLU B CG  1 
ATOM   2118 C  CD  . GLU B  1 94  ? 52.919 29.655  46.676  1.00 56.06 ? 95  GLU B CD  1 
ATOM   2119 O  OE1 . GLU B  1 94  ? 52.763 29.067  47.771  1.00 54.26 ? 95  GLU B OE1 1 
ATOM   2120 O  OE2 . GLU B  1 94  ? 53.530 30.747  46.570  1.00 62.99 ? 95  GLU B OE2 1 
ATOM   2121 N  N   . ALA B  1 95  ? 49.675 25.215  45.278  1.00 30.32 ? 96  ALA B N   1 
ATOM   2122 C  CA  . ALA B  1 95  ? 49.374 23.791  45.203  1.00 34.77 ? 96  ALA B CA  1 
ATOM   2123 C  C   . ALA B  1 95  ? 48.808 23.420  43.834  1.00 37.31 ? 96  ALA B C   1 
ATOM   2124 O  O   . ALA B  1 95  ? 49.208 22.411  43.235  1.00 34.84 ? 96  ALA B O   1 
ATOM   2125 C  CB  . ALA B  1 95  ? 48.397 23.401  46.310  1.00 32.32 ? 96  ALA B CB  1 
ATOM   2126 N  N   . LEU B  1 96  ? 47.861 24.221  43.328  1.00 28.99 ? 97  LEU B N   1 
ATOM   2127 C  CA  . LEU B  1 96  ? 47.247 23.921  42.040  1.00 33.35 ? 97  LEU B CA  1 
ATOM   2128 C  C   . LEU B  1 96  ? 48.267 23.997  40.905  1.00 36.38 ? 97  LEU B C   1 
ATOM   2129 O  O   . LEU B  1 96  ? 48.213 23.194  39.963  1.00 32.97 ? 97  LEU B O   1 
ATOM   2130 C  CB  . LEU B  1 96  ? 46.078 24.873  41.775  1.00 34.20 ? 97  LEU B CB  1 
ATOM   2131 C  CG  . LEU B  1 96  ? 44.781 24.648  42.555  1.00 34.60 ? 97  LEU B CG  1 
ATOM   2132 C  CD1 . LEU B  1 96  ? 43.777 25.728  42.170  1.00 36.48 ? 97  LEU B CD1 1 
ATOM   2133 C  CD2 . LEU B  1 96  ? 44.218 23.268  42.281  1.00 35.18 ? 97  LEU B CD2 1 
ATOM   2134 N  N   . GLN B  1 97  ? 49.208 24.950  40.974  1.00 33.17 ? 98  GLN B N   1 
ATOM   2135 C  CA  . GLN B  1 97  ? 50.207 25.037  39.912  1.00 36.45 ? 98  GLN B CA  1 
ATOM   2136 C  C   . GLN B  1 97  ? 51.145 23.833  39.935  1.00 36.60 ? 98  GLN B C   1 
ATOM   2137 O  O   . GLN B  1 97  ? 51.527 23.322  38.873  1.00 33.04 ? 98  GLN B O   1 
ATOM   2138 C  CB  . GLN B  1 97  ? 50.984 26.357  39.995  1.00 37.42 ? 98  GLN B CB  1 
ATOM   2139 C  CG  . GLN B  1 97  ? 50.069 27.588  39.997  1.00 39.91 ? 98  GLN B CG  1 
ATOM   2140 C  CD  . GLN B  1 97  ? 50.764 28.902  40.392  1.00 45.57 ? 98  GLN B CD  1 
ATOM   2141 O  OE1 . GLN B  1 97  ? 50.669 29.905  39.664  1.00 51.00 ? 98  GLN B OE1 1 
ATOM   2142 N  NE2 . GLN B  1 97  ? 51.487 28.893  41.508  1.00 41.30 ? 98  GLN B NE2 1 
ATOM   2143 N  N   . ALA B  1 98  ? 51.501 23.350  41.133  1.00 35.36 ? 99  ALA B N   1 
ATOM   2144 C  CA  . ALA B  1 98  ? 52.280 22.118  41.245  1.00 34.26 ? 99  ALA B CA  1 
ATOM   2145 C  C   . ALA B  1 98  ? 51.492 20.915  40.736  1.00 34.27 ? 99  ALA B C   1 
ATOM   2146 O  O   . ALA B  1 98  ? 52.062 20.030  40.095  1.00 31.45 ? 99  ALA B O   1 
ATOM   2147 C  CB  . ALA B  1 98  ? 52.711 21.893  42.698  1.00 32.65 ? 99  ALA B CB  1 
ATOM   2148 N  N   . ALA B  1 99  ? 50.183 20.849  41.031  1.00 31.58 ? 100 ALA B N   1 
ATOM   2149 C  CA  . ALA B  1 99  ? 49.361 19.769  40.486  1.00 30.53 ? 100 ALA B CA  1 
ATOM   2150 C  C   . ALA B  1 99  ? 49.300 19.835  38.971  1.00 33.28 ? 100 ALA B C   1 
ATOM   2151 O  O   . ALA B  1 99  ? 49.386 18.805  38.295  1.00 36.20 ? 100 ALA B O   1 
ATOM   2152 C  CB  . ALA B  1 99  ? 47.946 19.819  41.058  1.00 33.35 ? 100 ALA B CB  1 
ATOM   2153 N  N   . LEU B  1 100 ? 49.136 21.040  38.415  1.00 37.60 ? 101 LEU B N   1 
ATOM   2154 C  CA  . LEU B  1 100 ? 49.087 21.168  36.964  1.00 35.55 ? 101 LEU B CA  1 
ATOM   2155 C  C   . LEU B  1 100 ? 50.368 20.631  36.328  1.00 38.01 ? 101 LEU B C   1 
ATOM   2156 O  O   . LEU B  1 100 ? 50.316 19.864  35.358  1.00 36.20 ? 101 LEU B O   1 
ATOM   2157 C  CB  . LEU B  1 100 ? 48.846 22.628  36.579  1.00 29.55 ? 101 LEU B CB  1 
ATOM   2158 C  CG  . LEU B  1 100 ? 48.864 22.908  35.075  1.00 37.55 ? 101 LEU B CG  1 
ATOM   2159 C  CD1 . LEU B  1 100 ? 47.778 22.089  34.403  1.00 32.81 ? 101 LEU B CD1 1 
ATOM   2160 C  CD2 . LEU B  1 100 ? 48.699 24.393  34.760  1.00 34.26 ? 101 LEU B CD2 1 
ATOM   2161 N  N   . ASP B  1 101 ? 51.528 20.994  36.892  1.00 35.17 ? 102 ASP B N   1 
ATOM   2162 C  CA  . ASP B  1 101 ? 52.809 20.519  36.368  1.00 38.38 ? 102 ASP B CA  1 
ATOM   2163 C  C   . ASP B  1 101 ? 52.941 19.000  36.509  1.00 39.63 ? 102 ASP B C   1 
ATOM   2164 O  O   . ASP B  1 101 ? 53.450 18.317  35.610  1.00 37.22 ? 102 ASP B O   1 
ATOM   2165 C  CB  . ASP B  1 101 ? 53.948 21.246  37.091  1.00 38.35 ? 102 ASP B CB  1 
ATOM   2166 C  CG  . ASP B  1 101 ? 55.298 20.555  36.922  1.00 58.53 ? 102 ASP B CG  1 
ATOM   2167 O  OD1 . ASP B  1 101 ? 55.540 19.512  37.582  1.00 62.18 ? 102 ASP B OD1 1 
ATOM   2168 O  OD2 . ASP B  1 101 ? 56.132 21.063  36.136  1.00 68.68 ? 102 ASP B OD2 1 
ATOM   2169 N  N   . LEU B  1 102 ? 52.485 18.455  37.637  1.00 35.71 ? 103 LEU B N   1 
ATOM   2170 C  CA  . LEU B  1 102 ? 52.540 17.015  37.846  1.00 39.35 ? 103 LEU B CA  1 
ATOM   2171 C  C   . LEU B  1 102 ? 51.625 16.273  36.870  1.00 36.36 ? 103 LEU B C   1 
ATOM   2172 O  O   . LEU B  1 102 ? 52.011 15.234  36.325  1.00 34.64 ? 103 LEU B O   1 
ATOM   2173 C  CB  . LEU B  1 102 ? 52.179 16.711  39.295  1.00 37.51 ? 103 LEU B CB  1 
ATOM   2174 C  CG  . LEU B  1 102 ? 52.148 15.269  39.762  1.00 43.75 ? 103 LEU B CG  1 
ATOM   2175 C  CD1 . LEU B  1 102 ? 53.543 14.660  39.647  1.00 43.43 ? 103 LEU B CD1 1 
ATOM   2176 C  CD2 . LEU B  1 102 ? 51.654 15.243  41.213  1.00 36.47 ? 103 LEU B CD2 1 
ATOM   2177 N  N   . GLU B  1 103 ? 50.421 16.799  36.613  1.00 34.40 ? 104 GLU B N   1 
ATOM   2178 C  CA  . GLU B  1 103 ? 49.531 16.124  35.669  1.00 37.85 ? 104 GLU B CA  1 
ATOM   2179 C  C   . GLU B  1 103 ? 50.067 16.185  34.239  1.00 33.22 ? 104 GLU B C   1 
ATOM   2180 O  O   . GLU B  1 103 ? 49.849 15.250  33.464  1.00 33.70 ? 104 GLU B O   1 
ATOM   2181 C  CB  . GLU B  1 103 ? 48.115 16.709  35.749  1.00 36.33 ? 104 GLU B CB  1 
ATOM   2182 C  CG  . GLU B  1 103 ? 47.332 16.378  37.055  1.00 41.75 ? 104 GLU B CG  1 
ATOM   2183 C  CD  . GLU B  1 103 ? 47.179 14.869  37.385  1.00 52.22 ? 104 GLU B CD  1 
ATOM   2184 O  OE1 . GLU B  1 103 ? 48.117 14.065  37.194  1.00 53.09 ? 104 GLU B OE1 1 
ATOM   2185 O  OE2 . GLU B  1 103 ? 46.099 14.480  37.879  1.00 61.42 ? 104 GLU B OE2 1 
ATOM   2186 N  N   . LYS B  1 104 ? 50.787 17.252  33.878  1.00 32.98 ? 105 LYS B N   1 
ATOM   2187 C  CA  . LYS B  1 104 ? 51.385 17.320  32.547  1.00 36.52 ? 105 LYS B CA  1 
ATOM   2188 C  C   . LYS B  1 104 ? 52.574 16.376  32.422  1.00 36.62 ? 105 LYS B C   1 
ATOM   2189 O  O   . LYS B  1 104 ? 52.804 15.814  31.345  1.00 34.76 ? 105 LYS B O   1 
ATOM   2190 C  CB  . LYS B  1 104 ? 51.834 18.745  32.226  1.00 32.68 ? 105 LYS B CB  1 
ATOM   2191 C  CG  . LYS B  1 104 ? 50.780 19.633  31.633  1.00 36.35 ? 105 LYS B CG  1 
ATOM   2192 C  CD  . LYS B  1 104 ? 51.116 21.071  31.972  1.00 39.62 ? 105 LYS B CD  1 
ATOM   2193 C  CE  . LYS B  1 104 ? 50.844 22.014  30.828  1.00 41.01 ? 105 LYS B CE  1 
ATOM   2194 N  NZ  . LYS B  1 104 ? 51.116 23.433  31.257  1.00 46.09 ? 105 LYS B NZ  1 
ATOM   2195 N  N   . GLN B  1 105 ? 53.339 16.203  33.501  1.00 33.05 ? 106 GLN B N   1 
ATOM   2196 C  CA  . GLN B  1 105 ? 54.418 15.219  33.508  1.00 37.60 ? 106 GLN B CA  1 
ATOM   2197 C  C   . GLN B  1 105 ? 53.889 13.810  33.302  1.00 34.87 ? 106 GLN B C   1 
ATOM   2198 O  O   . GLN B  1 105 ? 54.482 13.025  32.554  1.00 35.82 ? 106 GLN B O   1 
ATOM   2199 C  CB  . GLN B  1 105 ? 55.179 15.277  34.825  1.00 37.46 ? 106 GLN B CB  1 
ATOM   2200 C  CG  . GLN B  1 105 ? 56.413 16.121  34.786  1.00 50.02 ? 106 GLN B CG  1 
ATOM   2201 C  CD  . GLN B  1 105 ? 56.937 16.381  36.180  1.00 62.33 ? 106 GLN B CD  1 
ATOM   2202 O  OE1 . GLN B  1 105 ? 57.343 17.500  36.500  1.00 61.54 ? 106 GLN B OE1 1 
ATOM   2203 N  NE2 . GLN B  1 105 ? 56.923 15.342  37.030  1.00 57.05 ? 106 GLN B NE2 1 
ATOM   2204 N  N   . VAL B  1 106 ? 52.789 13.461  33.977  1.00 29.63 ? 107 VAL B N   1 
ATOM   2205 C  CA  . VAL B  1 106 ? 52.216 12.129  33.798  1.00 33.58 ? 107 VAL B CA  1 
ATOM   2206 C  C   . VAL B  1 106 ? 51.691 11.963  32.373  1.00 34.76 ? 107 VAL B C   1 
ATOM   2207 O  O   . VAL B  1 106 ? 51.843 10.899  31.756  1.00 32.21 ? 107 VAL B O   1 
ATOM   2208 C  CB  . VAL B  1 106 ? 51.111 11.867  34.838  1.00 33.25 ? 107 VAL B CB  1 
ATOM   2209 C  CG1 . VAL B  1 106 ? 50.337 10.567  34.495  1.00 34.79 ? 107 VAL B CG1 1 
ATOM   2210 C  CG2 . VAL B  1 106 ? 51.712 11.791  36.232  1.00 35.10 ? 107 VAL B CG2 1 
ATOM   2211 N  N   . ASN B  1 107 ? 51.065 13.013  31.829  1.00 33.44 ? 108 ASN B N   1 
ATOM   2212 C  CA  . ASN B  1 107 ? 50.532 12.929  30.473  1.00 35.42 ? 108 ASN B CA  1 
ATOM   2213 C  C   . ASN B  1 107 ? 51.651 12.696  29.464  1.00 32.64 ? 108 ASN B C   1 
ATOM   2214 O  O   . ASN B  1 107 ? 51.549 11.826  28.589  1.00 29.02 ? 108 ASN B O   1 
ATOM   2215 C  CB  . ASN B  1 107 ? 49.748 14.199  30.136  1.00 33.15 ? 108 ASN B CB  1 
ATOM   2216 C  CG  . ASN B  1 107 ? 48.915 14.049  28.878  1.00 35.97 ? 108 ASN B CG  1 
ATOM   2217 O  OD1 . ASN B  1 107 ? 48.324 12.997  28.648  1.00 37.60 ? 108 ASN B OD1 1 
ATOM   2218 N  ND2 . ASN B  1 107 ? 48.859 15.101  28.058  1.00 36.68 ? 108 ASN B ND2 1 
ATOM   2219 N  N   . GLN B  1 108 ? 52.742 13.449  29.590  1.00 30.73 ? 109 GLN B N   1 
ATOM   2220 C  CA  . GLN B  1 108 ? 53.874 13.259  28.685  1.00 37.13 ? 109 GLN B CA  1 
ATOM   2221 C  C   . GLN B  1 108 ? 54.423 11.836  28.768  1.00 34.56 ? 109 GLN B C   1 
ATOM   2222 O  O   . GLN B  1 108 ? 54.746 11.226  27.743  1.00 35.55 ? 109 GLN B O   1 
ATOM   2223 C  CB  . GLN B  1 108 ? 54.963 14.289  28.995  1.00 37.58 ? 109 GLN B CB  1 
ATOM   2224 C  CG  . GLN B  1 108 ? 56.169 14.168  28.095  1.00 42.94 ? 109 GLN B CG  1 
ATOM   2225 C  CD  . GLN B  1 108 ? 55.878 14.670  26.672  1.00 53.09 ? 109 GLN B CD  1 
ATOM   2226 O  OE1 . GLN B  1 108 ? 56.306 14.056  25.692  1.00 57.98 ? 109 GLN B OE1 1 
ATOM   2227 N  NE2 . GLN B  1 108 ? 55.129 15.779  26.559  1.00 54.08 ? 109 GLN B NE2 1 
ATOM   2228 N  N   . SER B  1 109 ? 54.508 11.284  29.981  1.00 31.20 ? 110 SER B N   1 
ATOM   2229 C  CA  . SER B  1 109 ? 54.953 9.904   30.161  1.00 33.76 ? 110 SER B CA  1 
ATOM   2230 C  C   . SER B  1 109 ? 53.970 8.910   29.540  1.00 33.44 ? 110 SER B C   1 
ATOM   2231 O  O   . SER B  1 109 ? 54.381 7.910   28.938  1.00 33.56 ? 110 SER B O   1 
ATOM   2232 C  CB  . SER B  1 109 ? 55.144 9.629   31.655  1.00 32.64 ? 110 SER B CB  1 
ATOM   2233 O  OG  . SER B  1 109 ? 55.609 8.318   31.878  1.00 41.56 ? 110 SER B OG  1 
ATOM   2234 N  N   . LEU B  1 110 ? 52.667 9.161   29.671  1.00 34.22 ? 111 LEU B N   1 
ATOM   2235 C  CA  . LEU B  1 110 ? 51.690 8.286   29.024  1.00 33.26 ? 111 LEU B CA  1 
ATOM   2236 C  C   . LEU B  1 110 ? 51.832 8.335   27.508  1.00 33.02 ? 111 LEU B C   1 
ATOM   2237 O  O   . LEU B  1 110 ? 51.735 7.302   26.838  1.00 33.06 ? 111 LEU B O   1 
ATOM   2238 C  CB  . LEU B  1 110 ? 50.268 8.675   29.446  1.00 33.27 ? 111 LEU B CB  1 
ATOM   2239 C  CG  . LEU B  1 110 ? 49.865 8.327   30.882  1.00 38.75 ? 111 LEU B CG  1 
ATOM   2240 C  CD1 . LEU B  1 110 ? 48.500 8.906   31.221  1.00 35.40 ? 111 LEU B CD1 1 
ATOM   2241 C  CD2 . LEU B  1 110 ? 49.873 6.808   31.094  1.00 37.02 ? 111 LEU B CD2 1 
ATOM   2242 N  N   . LEU B  1 111 ? 52.062 9.532   26.947  1.00 32.97 ? 112 LEU B N   1 
ATOM   2243 C  CA  . LEU B  1 111 ? 52.198 9.652   25.498  1.00 33.77 ? 112 LEU B CA  1 
ATOM   2244 C  C   . LEU B  1 111 ? 53.438 8.929   24.980  1.00 35.84 ? 112 LEU B C   1 
ATOM   2245 O  O   . LEU B  1 111 ? 53.411 8.386   23.875  1.00 36.35 ? 112 LEU B O   1 
ATOM   2246 C  CB  . LEU B  1 111 ? 52.247 11.116  25.088  1.00 31.95 ? 112 LEU B CB  1 
ATOM   2247 C  CG  . LEU B  1 111 ? 50.940 11.890  25.233  1.00 37.53 ? 112 LEU B CG  1 
ATOM   2248 C  CD1 . LEU B  1 111 ? 51.203 13.397  25.111  1.00 29.25 ? 112 LEU B CD1 1 
ATOM   2249 C  CD2 . LEU B  1 111 ? 49.930 11.419  24.197  1.00 34.06 ? 112 LEU B CD2 1 
ATOM   2250 N  N   . GLU B  1 112 ? 54.529 8.920   25.754  1.00 34.96 ? 113 GLU B N   1 
ATOM   2251 C  CA  . GLU B  1 112 ? 55.693 8.120   25.386  1.00 37.30 ? 113 GLU B CA  1 
ATOM   2252 C  C   . GLU B  1 112 ? 55.378 6.634   25.450  1.00 36.45 ? 113 GLU B C   1 
ATOM   2253 O  O   . GLU B  1 112 ? 55.829 5.866   24.599  1.00 34.83 ? 113 GLU B O   1 
ATOM   2254 C  CB  . GLU B  1 112 ? 56.874 8.439   26.302  1.00 37.90 ? 113 GLU B CB  1 
ATOM   2255 C  CG  . GLU B  1 112 ? 57.442 9.829   26.119  1.00 46.63 ? 113 GLU B CG  1 
ATOM   2256 C  CD  . GLU B  1 112 ? 58.585 10.127  27.081  1.00 56.37 ? 113 GLU B CD  1 
ATOM   2257 O  OE1 . GLU B  1 112 ? 59.477 9.262   27.268  1.00 69.42 ? 113 GLU B OE1 1 
ATOM   2258 O  OE2 . GLU B  1 112 ? 58.596 11.240  27.645  1.00 61.04 ? 113 GLU B OE2 1 
ATOM   2259 N  N   . LEU B  1 113 ? 54.622 6.209   26.465  1.00 35.51 ? 114 LEU B N   1 
ATOM   2260 C  CA  . LEU B  1 113 ? 54.180 4.819   26.533  1.00 37.17 ? 114 LEU B CA  1 
ATOM   2261 C  C   . LEU B  1 113 ? 53.353 4.449   25.308  1.00 36.43 ? 114 LEU B C   1 
ATOM   2262 O  O   . LEU B  1 113 ? 53.482 3.342   24.777  1.00 34.51 ? 114 LEU B O   1 
ATOM   2263 C  CB  . LEU B  1 113 ? 53.381 4.588   27.816  1.00 37.56 ? 114 LEU B CB  1 
ATOM   2264 C  CG  . LEU B  1 113 ? 53.046 3.171   28.305  1.00 44.10 ? 114 LEU B CG  1 
ATOM   2265 C  CD1 . LEU B  1 113 ? 54.007 2.110   27.800  1.00 39.01 ? 114 LEU B CD1 1 
ATOM   2266 C  CD2 . LEU B  1 113 ? 53.016 3.166   29.819  1.00 42.74 ? 114 LEU B CD2 1 
ATOM   2267 N  N   . HIS B  1 114 ? 52.517 5.374   24.831  1.00 34.17 ? 115 HIS B N   1 
ATOM   2268 C  CA  . HIS B  1 114 ? 51.742 5.112   23.625  1.00 33.17 ? 115 HIS B CA  1 
ATOM   2269 C  C   . HIS B  1 114 ? 52.650 4.968   22.415  1.00 35.03 ? 115 HIS B C   1 
ATOM   2270 O  O   . HIS B  1 114 ? 52.430 4.095   21.567  1.00 33.85 ? 115 HIS B O   1 
ATOM   2271 C  CB  . HIS B  1 114 ? 50.720 6.223   23.394  1.00 31.56 ? 115 HIS B CB  1 
ATOM   2272 C  CG  . HIS B  1 114 ? 49.725 5.900   22.325  1.00 33.30 ? 115 HIS B CG  1 
ATOM   2273 N  ND1 . HIS B  1 114 ? 50.025 5.983   20.983  1.00 35.82 ? 115 HIS B ND1 1 
ATOM   2274 C  CD2 . HIS B  1 114 ? 48.440 5.472   22.399  1.00 34.37 ? 115 HIS B CD2 1 
ATOM   2275 C  CE1 . HIS B  1 114 ? 48.966 5.623   20.276  1.00 40.60 ? 115 HIS B CE1 1 
ATOM   2276 N  NE2 . HIS B  1 114 ? 47.990 5.310   21.112  1.00 35.76 ? 115 HIS B NE2 1 
ATOM   2277 N  N   . SER B  1 115 ? 53.680 5.812   22.333  1.00 35.67 ? 116 SER B N   1 
ATOM   2278 C  CA  . SER B  1 115 ? 54.667 5.718   21.261  1.00 37.04 ? 116 SER B CA  1 
ATOM   2279 C  C   . SER B  1 115 ? 55.381 4.364   21.259  1.00 35.16 ? 116 SER B C   1 
ATOM   2280 O  O   . SER B  1 115 ? 55.538 3.741   20.207  1.00 38.55 ? 116 SER B O   1 
ATOM   2281 C  CB  . SER B  1 115 ? 55.677 6.851   21.407  1.00 35.92 ? 116 SER B CB  1 
ATOM   2282 O  OG  . SER B  1 115 ? 56.228 7.166   20.153  1.00 55.09 ? 116 SER B OG  1 
ATOM   2283 N  N   . THR B  1 116 ? 55.861 3.918   22.428  1.00 35.25 ? 117 THR B N   1 
ATOM   2284 C  CA  . THR B  1 116 ? 56.451 2.582   22.568  1.00 42.97 ? 117 THR B CA  1 
ATOM   2285 C  C   . THR B  1 116 ? 55.515 1.497   22.041  1.00 41.30 ? 117 THR B C   1 
ATOM   2286 O  O   . THR B  1 116 ? 55.928 0.621   21.272  1.00 43.43 ? 117 THR B O   1 
ATOM   2287 C  CB  . THR B  1 116 ? 56.788 2.288   24.044  1.00 41.80 ? 117 THR B CB  1 
ATOM   2288 O  OG1 . THR B  1 116 ? 57.458 3.399   24.643  1.00 41.64 ? 117 THR B OG1 1 
ATOM   2289 C  CG2 . THR B  1 116 ? 57.663 1.049   24.171  1.00 47.49 ? 117 THR B CG2 1 
ATOM   2290 N  N   . ALA B  1 117 ? 54.249 1.526   22.472  1.00 38.13 ? 118 ALA B N   1 
ATOM   2291 C  CA  . ALA B  1 117 ? 53.303 0.491   22.065  1.00 35.39 ? 118 ALA B CA  1 
ATOM   2292 C  C   . ALA B  1 117 ? 53.068 0.516   20.563  1.00 38.95 ? 118 ALA B C   1 
ATOM   2293 O  O   . ALA B  1 117 ? 52.967 -0.542  19.927  1.00 35.92 ? 118 ALA B O   1 
ATOM   2294 C  CB  . ALA B  1 117 ? 51.983 0.661   22.807  1.00 35.95 ? 118 ALA B CB  1 
ATOM   2295 N  N   . SER B  1 118 ? 52.969 1.717   19.980  1.00 39.08 ? 119 SER B N   1 
ATOM   2296 C  CA  . SER B  1 118 ? 52.822 1.844   18.532  1.00 41.86 ? 119 SER B CA  1 
ATOM   2297 C  C   . SER B  1 118 ? 54.048 1.315   17.804  1.00 42.56 ? 119 SER B C   1 
ATOM   2298 O  O   . SER B  1 118 ? 53.921 0.665   16.758  1.00 43.57 ? 119 SER B O   1 
ATOM   2299 C  CB  . SER B  1 118 ? 52.582 3.304   18.149  1.00 39.14 ? 119 SER B CB  1 
ATOM   2300 O  OG  . SER B  1 118 ? 51.254 3.672   18.439  1.00 52.08 ? 119 SER B OG  1 
ATOM   2301 N  N   . GLY B  1 119 ? 55.245 1.591   18.343  1.00 41.56 ? 120 GLY B N   1 
ATOM   2302 C  CA  . GLY B  1 119 ? 56.465 1.102   17.717  1.00 40.10 ? 120 GLY B CA  1 
ATOM   2303 C  C   . GLY B  1 119 ? 56.520 -0.414  17.626  1.00 42.92 ? 120 GLY B C   1 
ATOM   2304 O  O   . GLY B  1 119 ? 57.012 -0.967  16.642  1.00 44.87 ? 120 GLY B O   1 
ATOM   2305 N  N   . ASN B  1 120 ? 56.017 -1.109  18.647  1.00 40.62 ? 121 ASN B N   1 
ATOM   2306 C  CA  . ASN B  1 120 ? 56.015 -2.567  18.651  1.00 43.23 ? 121 ASN B CA  1 
ATOM   2307 C  C   . ASN B  1 120 ? 54.707 -3.170  18.149  1.00 41.80 ? 121 ASN B C   1 
ATOM   2308 O  O   . ASN B  1 120 ? 54.511 -4.381  18.277  1.00 46.25 ? 121 ASN B O   1 
ATOM   2309 C  CB  . ASN B  1 120 ? 56.325 -3.092  20.053  1.00 44.33 ? 121 ASN B CB  1 
ATOM   2310 C  CG  . ASN B  1 120 ? 57.674 -2.621  20.565  1.00 48.33 ? 121 ASN B CG  1 
ATOM   2311 O  OD1 . ASN B  1 120 ? 57.817 -2.277  21.737  1.00 47.66 ? 121 ASN B OD1 1 
ATOM   2312 N  ND2 . ASN B  1 120 ? 58.670 -2.591  19.679  1.00 53.93 ? 121 ASN B ND2 1 
ATOM   2313 N  N   . ASN B  1 121 ? 53.819 -2.362  17.577  1.00 39.61 ? 122 ASN B N   1 
ATOM   2314 C  CA  . ASN B  1 121 ? 52.532 -2.824  17.065  1.00 38.62 ? 122 ASN B CA  1 
ATOM   2315 C  C   . ASN B  1 121 ? 51.781 -3.645  18.113  1.00 40.11 ? 122 ASN B C   1 
ATOM   2316 O  O   . ASN B  1 121 ? 51.445 -4.814  17.911  1.00 43.03 ? 122 ASN B O   1 
ATOM   2317 C  CB  . ASN B  1 121 ? 52.720 -3.609  15.764  1.00 44.79 ? 122 ASN B CB  1 
ATOM   2318 C  CG  . ASN B  1 121 ? 53.427 -2.785  14.687  1.00 47.75 ? 122 ASN B CG  1 
ATOM   2319 O  OD1 . ASN B  1 121 ? 54.521 -3.128  14.261  1.00 47.04 ? 122 ASN B OD1 1 
ATOM   2320 N  ND2 . ASN B  1 121 ? 52.807 -1.685  14.264  1.00 50.11 ? 122 ASN B ND2 1 
ATOM   2321 N  N   . ASP B  1 122 ? 51.516 -2.999  19.254  1.00 38.83 ? 123 ASP B N   1 
ATOM   2322 C  CA  . ASP B  1 122 ? 50.704 -3.592  20.308  1.00 35.01 ? 123 ASP B CA  1 
ATOM   2323 C  C   . ASP B  1 122 ? 49.369 -2.851  20.400  1.00 34.08 ? 123 ASP B C   1 
ATOM   2324 O  O   . ASP B  1 122 ? 49.195 -1.966  21.253  1.00 36.07 ? 123 ASP B O   1 
ATOM   2325 C  CB  . ASP B  1 122 ? 51.446 -3.550  21.648  1.00 33.17 ? 123 ASP B CB  1 
ATOM   2326 C  CG  . ASP B  1 122 ? 50.730 -4.359  22.750  1.00 40.02 ? 123 ASP B CG  1 
ATOM   2327 O  OD1 . ASP B  1 122 ? 49.498 -4.592  22.620  1.00 38.97 ? 123 ASP B OD1 1 
ATOM   2328 O  OD2 . ASP B  1 122 ? 51.392 -4.731  23.756  1.00 36.70 ? 123 ASP B OD2 1 
ATOM   2329 N  N   . PRO B  1 123 ? 48.396 -3.190  19.557  1.00 33.52 ? 124 PRO B N   1 
ATOM   2330 C  CA  . PRO B  1 123 ? 47.146 -2.409  19.550  1.00 35.07 ? 124 PRO B CA  1 
ATOM   2331 C  C   . PRO B  1 123 ? 46.331 -2.567  20.821  1.00 31.00 ? 124 PRO B C   1 
ATOM   2332 O  O   . PRO B  1 123 ? 45.578 -1.651  21.177  1.00 33.38 ? 124 PRO B O   1 
ATOM   2333 C  CB  . PRO B  1 123 ? 46.394 -2.948  18.324  1.00 32.33 ? 124 PRO B CB  1 
ATOM   2334 C  CG  . PRO B  1 123 ? 46.919 -4.344  18.156  1.00 32.45 ? 124 PRO B CG  1 
ATOM   2335 C  CD  . PRO B  1 123 ? 48.372 -4.305  18.596  1.00 31.98 ? 124 PRO B CD  1 
ATOM   2336 N  N   . HIS B  1 124 ? 46.450 -3.696  21.520  1.00 35.06 ? 125 HIS B N   1 
ATOM   2337 C  CA  . HIS B  1 124 ? 45.737 -3.836  22.784  1.00 32.07 ? 125 HIS B CA  1 
ATOM   2338 C  C   . HIS B  1 124 ? 46.208 -2.796  23.792  1.00 35.28 ? 125 HIS B C   1 
ATOM   2339 O  O   . HIS B  1 124 ? 45.404 -2.252  24.558  1.00 29.23 ? 125 HIS B O   1 
ATOM   2340 C  CB  . HIS B  1 124 ? 45.918 -5.239  23.353  1.00 34.32 ? 125 HIS B CB  1 
ATOM   2341 C  CG  . HIS B  1 124 ? 45.030 -5.521  24.527  1.00 40.37 ? 125 HIS B CG  1 
ATOM   2342 N  ND1 . HIS B  1 124 ? 45.417 -5.286  25.830  1.00 38.12 ? 125 HIS B ND1 1 
ATOM   2343 C  CD2 . HIS B  1 124 ? 43.766 -6.006  24.592  1.00 37.12 ? 125 HIS B CD2 1 
ATOM   2344 C  CE1 . HIS B  1 124 ? 44.431 -5.618  26.646  1.00 36.55 ? 125 HIS B CE1 1 
ATOM   2345 N  NE2 . HIS B  1 124 ? 43.419 -6.058  25.920  1.00 39.97 ? 125 HIS B NE2 1 
ATOM   2346 N  N   . LEU B  1 125 ? 47.511 -2.497  23.801  1.00 34.67 ? 126 LEU B N   1 
ATOM   2347 C  CA  . LEU B  1 125 ? 48.020 -1.547  24.781  1.00 30.66 ? 126 LEU B CA  1 
ATOM   2348 C  C   . LEU B  1 125 ? 47.713 -0.105  24.373  1.00 34.75 ? 126 LEU B C   1 
ATOM   2349 O  O   . LEU B  1 125 ? 47.336 0.702   25.230  1.00 32.82 ? 126 LEU B O   1 
ATOM   2350 C  CB  . LEU B  1 125 ? 49.519 -1.770  25.001  1.00 31.59 ? 126 LEU B CB  1 
ATOM   2351 C  CG  . LEU B  1 125 ? 50.275 -0.749  25.870  1.00 35.47 ? 126 LEU B CG  1 
ATOM   2352 C  CD1 . LEU B  1 125 ? 49.637 -0.607  27.239  1.00 31.11 ? 126 LEU B CD1 1 
ATOM   2353 C  CD2 . LEU B  1 125 ? 51.744 -1.115  26.010  1.00 28.58 ? 126 LEU B CD2 1 
ATOM   2354 N  N   . THR B  1 126 ? 47.846 0.241   23.076  1.00 32.25 ? 127 THR B N   1 
ATOM   2355 C  CA  . THR B  1 126 ? 47.426 1.577   22.643  1.00 39.47 ? 127 THR B CA  1 
ATOM   2356 C  C   . THR B  1 126 ? 45.952 1.810   22.941  1.00 36.48 ? 127 THR B C   1 
ATOM   2357 O  O   . THR B  1 126 ? 45.561 2.933   23.270  1.00 35.24 ? 127 THR B O   1 
ATOM   2358 C  CB  . THR B  1 126 ? 47.677 1.821   21.140  1.00 36.19 ? 127 THR B CB  1 
ATOM   2359 O  OG1 . THR B  1 126 ? 46.937 0.880   20.346  1.00 37.04 ? 127 THR B OG1 1 
ATOM   2360 C  CG2 . THR B  1 126 ? 49.150 1.756   20.793  1.00 34.99 ? 127 THR B CG2 1 
ATOM   2361 N  N   . LYS B  1 127 ? 45.126 0.763   22.835  1.00 35.91 ? 128 LYS B N   1 
ATOM   2362 C  CA  . LYS B  1 127 ? 43.709 0.893   23.168  1.00 38.28 ? 128 LYS B CA  1 
ATOM   2363 C  C   . LYS B  1 127 ? 43.511 1.173   24.655  1.00 38.48 ? 128 LYS B C   1 
ATOM   2364 O  O   . LYS B  1 127 ? 42.710 2.037   25.033  1.00 35.93 ? 128 LYS B O   1 
ATOM   2365 C  CB  . LYS B  1 127 ? 42.956 -0.369  22.755  1.00 38.73 ? 128 LYS B CB  1 
ATOM   2366 C  CG  . LYS B  1 127 ? 41.448 -0.229  22.804  1.00 45.65 ? 128 LYS B CG  1 
ATOM   2367 C  CD  . LYS B  1 127 ? 40.813 -1.152  23.818  1.00 47.80 ? 128 LYS B CD  1 
ATOM   2368 C  CE  . LYS B  1 127 ? 39.285 -1.199  23.623  1.00 56.58 ? 128 LYS B CE  1 
ATOM   2369 N  NZ  . LYS B  1 127 ? 38.531 -0.145  24.366  1.00 53.95 ? 128 LYS B NZ  1 
ATOM   2370 N  N   . LEU B  1 128 ? 44.232 0.454   25.515  1.00 35.43 ? 129 LEU B N   1 
ATOM   2371 C  CA  . LEU B  1 128 ? 44.152 0.730   26.941  1.00 35.17 ? 129 LEU B CA  1 
ATOM   2372 C  C   . LEU B  1 128 ? 44.538 2.181   27.250  1.00 40.07 ? 129 LEU B C   1 
ATOM   2373 O  O   . LEU B  1 128 ? 43.833 2.879   27.988  1.00 35.69 ? 129 LEU B O   1 
ATOM   2374 C  CB  . LEU B  1 128 ? 45.045 -0.238  27.708  1.00 32.97 ? 129 LEU B CB  1 
ATOM   2375 C  CG  . LEU B  1 128 ? 45.137 0.171   29.185  1.00 39.35 ? 129 LEU B CG  1 
ATOM   2376 C  CD1 . LEU B  1 128 ? 43.985 -0.468  29.976  1.00 37.96 ? 129 LEU B CD1 1 
ATOM   2377 C  CD2 . LEU B  1 128 ? 46.504 -0.135  29.805  1.00 33.91 ? 129 LEU B CD2 1 
ATOM   2378 N  N   . LEU B  1 129 ? 45.660 2.653   26.700  1.00 32.04 ? 130 LEU B N   1 
ATOM   2379 C  CA  . LEU B  1 129 ? 46.106 4.007   27.018  1.00 38.54 ? 130 LEU B CA  1 
ATOM   2380 C  C   . LEU B  1 129 ? 45.099 5.053   26.547  1.00 40.67 ? 130 LEU B C   1 
ATOM   2381 O  O   . LEU B  1 129 ? 44.803 6.009   27.271  1.00 43.64 ? 130 LEU B O   1 
ATOM   2382 C  CB  . LEU B  1 129 ? 47.482 4.271   26.412  1.00 30.64 ? 130 LEU B CB  1 
ATOM   2383 C  CG  . LEU B  1 129 ? 48.595 3.398   26.990  1.00 37.62 ? 130 LEU B CG  1 
ATOM   2384 C  CD1 . LEU B  1 129 ? 49.861 3.525   26.158  1.00 34.48 ? 130 LEU B CD1 1 
ATOM   2385 C  CD2 . LEU B  1 129 ? 48.870 3.740   28.457  1.00 35.79 ? 130 LEU B CD2 1 
ATOM   2386 N  N   . GLU B  1 130 ? 44.551 4.884   25.346  1.00 38.01 ? 131 GLU B N   1 
ATOM   2387 C  CA  . GLU B  1 130 ? 43.572 5.845   24.848  1.00 45.28 ? 131 GLU B CA  1 
ATOM   2388 C  C   . GLU B  1 130 ? 42.314 5.870   25.718  1.00 47.56 ? 131 GLU B C   1 
ATOM   2389 O  O   . GLU B  1 130 ? 41.885 6.935   26.184  1.00 50.73 ? 131 GLU B O   1 
ATOM   2390 C  CB  . GLU B  1 130 ? 43.227 5.520   23.393  1.00 40.61 ? 131 GLU B CB  1 
ATOM   2391 C  CG  . GLU B  1 130 ? 44.296 5.965   22.395  1.00 41.83 ? 131 GLU B CG  1 
ATOM   2392 C  CD  . GLU B  1 130 ? 44.173 5.267   21.034  1.00 48.87 ? 131 GLU B CD  1 
ATOM   2393 O  OE1 . GLU B  1 130 ? 43.035 4.947   20.607  1.00 57.92 ? 131 GLU B OE1 1 
ATOM   2394 O  OE2 . GLU B  1 130 ? 45.218 5.032   20.389  1.00 44.32 ? 131 GLU B OE2 1 
ATOM   2395 N  N   . ASP B  1 131 ? 41.724 4.700   25.975  1.00 42.73 ? 132 ASP B N   1 
ATOM   2396 C  CA  . ASP B  1 131 ? 40.389 4.646   26.560  1.00 51.76 ? 132 ASP B CA  1 
ATOM   2397 C  C   . ASP B  1 131 ? 40.367 4.825   28.075  1.00 48.98 ? 132 ASP B C   1 
ATOM   2398 O  O   . ASP B  1 131 ? 39.334 5.229   28.613  1.00 54.31 ? 132 ASP B O   1 
ATOM   2399 C  CB  . ASP B  1 131 ? 39.702 3.329   26.176  1.00 47.87 ? 132 ASP B CB  1 
ATOM   2400 C  CG  . ASP B  1 131 ? 39.566 3.167   24.665  1.00 62.80 ? 132 ASP B CG  1 
ATOM   2401 O  OD1 . ASP B  1 131 ? 39.817 4.165   23.938  1.00 64.10 ? 132 ASP B OD1 1 
ATOM   2402 O  OD2 . ASP B  1 131 ? 39.209 2.055   24.198  1.00 67.44 ? 132 ASP B OD2 1 
ATOM   2403 N  N   . GLU B  1 132 ? 41.466 4.556   28.778  1.00 49.44 ? 133 GLU B N   1 
ATOM   2404 C  CA  . GLU B  1 132 ? 41.455 4.619   30.234  1.00 51.00 ? 133 GLU B CA  1 
ATOM   2405 C  C   . GLU B  1 132 ? 42.364 5.677   30.832  1.00 50.47 ? 133 GLU B C   1 
ATOM   2406 O  O   . GLU B  1 132 ? 42.207 5.986   32.018  1.00 56.26 ? 133 GLU B O   1 
ATOM   2407 C  CB  . GLU B  1 132 ? 41.842 3.258   30.845  1.00 47.43 ? 133 GLU B CB  1 
ATOM   2408 C  CG  . GLU B  1 132 ? 41.288 2.062   30.082  1.00 58.42 ? 133 GLU B CG  1 
ATOM   2409 C  CD  . GLU B  1 132 ? 39.957 1.555   30.635  1.00 71.52 ? 133 GLU B CD  1 
ATOM   2410 O  OE1 . GLU B  1 132 ? 39.217 2.355   31.261  1.00 70.41 ? 133 GLU B OE1 1 
ATOM   2411 O  OE2 . GLU B  1 132 ? 39.656 0.350   30.438  1.00 74.80 ? 133 GLU B OE2 1 
ATOM   2412 N  N   . TYR B  1 133 ? 43.307 6.234   30.071  1.00 41.68 ? 134 TYR B N   1 
ATOM   2413 C  CA  . TYR B  1 133 ? 44.277 7.136   30.683  1.00 38.64 ? 134 TYR B CA  1 
ATOM   2414 C  C   . TYR B  1 133 ? 44.354 8.491   29.990  1.00 43.15 ? 134 TYR B C   1 
ATOM   2415 O  O   . TYR B  1 133 ? 44.280 9.526   30.660  1.00 41.70 ? 134 TYR B O   1 
ATOM   2416 C  CB  . TYR B  1 133 ? 45.656 6.481   30.709  1.00 39.30 ? 134 TYR B CB  1 
ATOM   2417 C  CG  . TYR B  1 133 ? 45.750 5.346   31.708  1.00 44.04 ? 134 TYR B CG  1 
ATOM   2418 C  CD1 . TYR B  1 133 ? 46.106 5.586   33.037  1.00 40.14 ? 134 TYR B CD1 1 
ATOM   2419 C  CD2 . TYR B  1 133 ? 45.457 4.034   31.328  1.00 38.67 ? 134 TYR B CD2 1 
ATOM   2420 C  CE1 . TYR B  1 133 ? 46.169 4.554   33.959  1.00 41.95 ? 134 TYR B CE1 1 
ATOM   2421 C  CE2 . TYR B  1 133 ? 45.523 2.991   32.241  1.00 42.74 ? 134 TYR B CE2 1 
ATOM   2422 C  CZ  . TYR B  1 133 ? 45.879 3.258   33.552  1.00 43.55 ? 134 TYR B CZ  1 
ATOM   2423 O  OH  . TYR B  1 133 ? 45.951 2.223   34.448  1.00 41.68 ? 134 TYR B OH  1 
ATOM   2424 N  N   . LEU B  1 134 ? 44.497 8.500   28.659  1.00 37.70 ? 135 LEU B N   1 
ATOM   2425 C  CA  . LEU B  1 134 ? 44.790 9.743   27.951  1.00 41.99 ? 135 LEU B CA  1 
ATOM   2426 C  C   . LEU B  1 134 ? 43.624 10.720  28.028  1.00 41.32 ? 135 LEU B C   1 
ATOM   2427 O  O   . LEU B  1 134 ? 43.827 11.911  28.287  1.00 36.31 ? 135 LEU B O   1 
ATOM   2428 C  CB  . LEU B  1 134 ? 45.149 9.454   26.495  1.00 40.47 ? 135 LEU B CB  1 
ATOM   2429 C  CG  . LEU B  1 134 ? 46.470 8.703   26.288  1.00 42.96 ? 135 LEU B CG  1 
ATOM   2430 C  CD1 . LEU B  1 134 ? 46.707 8.469   24.811  1.00 42.03 ? 135 LEU B CD1 1 
ATOM   2431 C  CD2 . LEU B  1 134 ? 47.636 9.461   26.904  1.00 40.00 ? 135 LEU B CD2 1 
ATOM   2432 N  N   . GLU B  1 135 ? 42.396 10.238  27.799  1.00 40.04 ? 136 GLU B N   1 
ATOM   2433 C  CA  . GLU B  1 135 ? 41.237 11.128  27.833  1.00 48.77 ? 136 GLU B CA  1 
ATOM   2434 C  C   . GLU B  1 135 ? 41.061 11.739  29.221  1.00 46.43 ? 136 GLU B C   1 
ATOM   2435 O  O   . GLU B  1 135 ? 40.864 12.952  29.363  1.00 42.73 ? 136 GLU B O   1 
ATOM   2436 C  CB  . GLU B  1 135 ? 39.976 10.374  27.396  1.00 51.15 ? 136 GLU B CB  1 
ATOM   2437 C  CG  . GLU B  1 135 ? 39.800 9.017   28.078  1.00 62.92 ? 136 GLU B CG  1 
ATOM   2438 C  CD  . GLU B  1 135 ? 38.332 8.612   28.267  1.00 79.94 ? 136 GLU B CD  1 
ATOM   2439 O  OE1 . GLU B  1 135 ? 37.774 7.933   27.368  1.00 80.03 ? 136 GLU B OE1 1 
ATOM   2440 O  OE2 . GLU B  1 135 ? 37.745 8.951   29.325  1.00 82.42 ? 136 GLU B OE2 1 
ATOM   2441 N  N   . GLU B  1 136 ? 41.164 10.916  30.260  1.00 44.10 ? 137 GLU B N   1 
ATOM   2442 C  CA  . GLU B  1 136 ? 41.007 11.418  31.615  1.00 45.26 ? 137 GLU B CA  1 
ATOM   2443 C  C   . GLU B  1 136 ? 42.187 12.301  32.031  1.00 42.15 ? 137 GLU B C   1 
ATOM   2444 O  O   . GLU B  1 136 ? 42.010 13.249  32.801  1.00 37.92 ? 137 GLU B O   1 
ATOM   2445 C  CB  . GLU B  1 136 ? 40.803 10.227  32.547  1.00 54.40 ? 137 GLU B CB  1 
ATOM   2446 C  CG  . GLU B  1 136 ? 41.452 10.310  33.903  1.00 61.48 ? 137 GLU B CG  1 
ATOM   2447 C  CD  . GLU B  1 136 ? 40.759 9.389   34.895  1.00 69.97 ? 137 GLU B CD  1 
ATOM   2448 O  OE1 . GLU B  1 136 ? 40.398 8.248   34.517  1.00 70.38 ? 137 GLU B OE1 1 
ATOM   2449 O  OE2 . GLU B  1 136 ? 40.569 9.815   36.049  1.00 69.31 ? 137 GLU B OE2 1 
ATOM   2450 N  N   . GLN B  1 137 ? 43.382 12.035  31.503  1.00 39.17 ? 138 GLN B N   1 
ATOM   2451 C  CA  . GLN B  1 137 ? 44.515 12.926  31.732  1.00 38.41 ? 138 GLN B CA  1 
ATOM   2452 C  C   . GLN B  1 137 ? 44.259 14.319  31.149  1.00 37.00 ? 138 GLN B C   1 
ATOM   2453 O  O   . GLN B  1 137 ? 44.567 15.337  31.783  1.00 32.77 ? 138 GLN B O   1 
ATOM   2454 C  CB  . GLN B  1 137 ? 45.772 12.296  31.126  1.00 36.47 ? 138 GLN B CB  1 
ATOM   2455 C  CG  . GLN B  1 137 ? 47.090 12.596  31.818  1.00 38.67 ? 138 GLN B CG  1 
ATOM   2456 C  CD  . GLN B  1 137 ? 47.034 12.481  33.335  1.00 40.08 ? 138 GLN B CD  1 
ATOM   2457 O  OE1 . GLN B  1 137 ? 46.332 11.645  33.886  1.00 45.91 ? 138 GLN B OE1 1 
ATOM   2458 N  NE2 . GLN B  1 137 ? 47.784 13.328  34.010  1.00 39.88 ? 138 GLN B NE2 1 
ATOM   2459 N  N   . VAL B  1 138 ? 43.677 14.385  29.949  1.00 31.60 ? 139 VAL B N   1 
ATOM   2460 C  CA  . VAL B  1 138 ? 43.455 15.681  29.315  1.00 34.76 ? 139 VAL B CA  1 
ATOM   2461 C  C   . VAL B  1 138 ? 42.337 16.435  30.034  1.00 36.52 ? 139 VAL B C   1 
ATOM   2462 O  O   . VAL B  1 138 ? 42.364 17.671  30.113  1.00 30.76 ? 139 VAL B O   1 
ATOM   2463 C  CB  . VAL B  1 138 ? 43.174 15.494  27.806  1.00 32.99 ? 139 VAL B CB  1 
ATOM   2464 C  CG1 . VAL B  1 138 ? 42.328 16.617  27.248  1.00 33.72 ? 139 VAL B CG1 1 
ATOM   2465 C  CG2 . VAL B  1 138 ? 44.482 15.416  27.026  1.00 36.03 ? 139 VAL B CG2 1 
ATOM   2466 N  N   . ASP B  1 139 ? 41.374 15.707  30.611  1.00 35.93 ? 140 ASP B N   1 
ATOM   2467 C  CA  . ASP B  1 139 ? 40.293 16.330  31.377  1.00 36.92 ? 140 ASP B CA  1 
ATOM   2468 C  C   . ASP B  1 139 ? 40.794 16.904  32.697  1.00 34.11 ? 140 ASP B C   1 
ATOM   2469 O  O   . ASP B  1 139 ? 40.373 17.997  33.101  1.00 32.23 ? 140 ASP B O   1 
ATOM   2470 C  CB  . ASP B  1 139 ? 39.184 15.313  31.635  1.00 37.21 ? 140 ASP B CB  1 
ATOM   2471 C  CG  . ASP B  1 139 ? 38.422 14.952  30.364  1.00 47.30 ? 140 ASP B CG  1 
ATOM   2472 O  OD1 . ASP B  1 139 ? 38.476 15.744  29.394  1.00 50.28 ? 140 ASP B OD1 1 
ATOM   2473 O  OD2 . ASP B  1 139 ? 37.796 13.866  30.323  1.00 52.31 ? 140 ASP B OD2 1 
ATOM   2474 N  N   . SER B  1 140 ? 41.682 16.183  33.388  1.00 33.33 ? 141 SER B N   1 
ATOM   2475 C  CA  . SER B  1 140 ? 42.255 16.706  34.625  1.00 33.86 ? 141 SER B CA  1 
ATOM   2476 C  C   . SER B  1 140 ? 43.045 17.984  34.376  1.00 36.52 ? 141 SER B C   1 
ATOM   2477 O  O   . SER B  1 140 ? 42.975 18.930  35.167  1.00 38.89 ? 141 SER B O   1 
ATOM   2478 C  CB  . SER B  1 140 ? 43.159 15.664  35.282  1.00 40.23 ? 141 SER B CB  1 
ATOM   2479 O  OG  . SER B  1 140 ? 42.408 14.536  35.692  1.00 52.36 ? 141 SER B OG  1 
ATOM   2480 N  N   . ILE B  1 141 ? 43.830 18.022  33.302  1.00 36.66 ? 142 ILE B N   1 
ATOM   2481 C  CA  . ILE B  1 141 ? 44.647 19.201  33.053  1.00 33.01 ? 142 ILE B CA  1 
ATOM   2482 C  C   . ILE B  1 141 ? 43.754 20.400  32.761  1.00 31.32 ? 142 ILE B C   1 
ATOM   2483 O  O   . ILE B  1 141 ? 44.024 21.513  33.221  1.00 32.21 ? 142 ILE B O   1 
ATOM   2484 C  CB  . ILE B  1 141 ? 45.653 18.921  31.918  1.00 32.22 ? 142 ILE B CB  1 
ATOM   2485 C  CG1 . ILE B  1 141 ? 46.722 17.929  32.406  1.00 35.30 ? 142 ILE B CG1 1 
ATOM   2486 C  CG2 . ILE B  1 141 ? 46.331 20.204  31.432  1.00 29.56 ? 142 ILE B CG2 1 
ATOM   2487 C  CD1 . ILE B  1 141 ? 47.440 17.199  31.281  1.00 32.62 ? 142 ILE B CD1 1 
ATOM   2488 N  N   . LYS B  1 142 ? 42.660 20.182  32.023  1.00 30.73 ? 143 LYS B N   1 
ATOM   2489 C  CA  . LYS B  1 142 ? 41.734 21.261  31.695  1.00 31.57 ? 143 LYS B CA  1 
ATOM   2490 C  C   . LYS B  1 142 ? 41.015 21.762  32.939  1.00 34.82 ? 143 LYS B C   1 
ATOM   2491 O  O   . LYS B  1 142 ? 40.860 22.973  33.130  1.00 36.64 ? 143 LYS B O   1 
ATOM   2492 C  CB  . LYS B  1 142 ? 40.726 20.781  30.648  1.00 35.26 ? 143 LYS B CB  1 
ATOM   2493 C  CG  . LYS B  1 142 ? 39.567 21.760  30.377  1.00 34.34 ? 143 LYS B CG  1 
ATOM   2494 C  CD  . LYS B  1 142 ? 40.095 23.095  29.858  1.00 36.95 ? 143 LYS B CD  1 
ATOM   2495 C  CE  . LYS B  1 142 ? 39.061 23.840  29.011  1.00 36.25 ? 143 LYS B CE  1 
ATOM   2496 N  NZ  . LYS B  1 142 ? 37.798 24.168  29.744  1.00 38.47 ? 143 LYS B NZ  1 
ATOM   2497 N  N   . LYS B  1 143 ? 40.584 20.842  33.802  1.00 32.36 ? 144 LYS B N   1 
ATOM   2498 C  CA  . LYS B  1 143 ? 39.917 21.218  35.041  1.00 35.27 ? 144 LYS B CA  1 
ATOM   2499 C  C   . LYS B  1 143 ? 40.840 22.026  35.950  1.00 38.10 ? 144 LYS B C   1 
ATOM   2500 O  O   . LYS B  1 143 ? 40.433 23.046  36.515  1.00 38.12 ? 144 LYS B O   1 
ATOM   2501 C  CB  . LYS B  1 143 ? 39.413 19.957  35.753  1.00 40.04 ? 144 LYS B CB  1 
ATOM   2502 C  CG  . LYS B  1 143 ? 38.880 20.184  37.161  1.00 46.43 ? 144 LYS B CG  1 
ATOM   2503 C  CD  . LYS B  1 143 ? 38.873 18.871  37.955  1.00 52.13 ? 144 LYS B CD  1 
ATOM   2504 C  CE  . LYS B  1 143 ? 37.746 18.843  39.001  1.00 61.99 ? 144 LYS B CE  1 
ATOM   2505 N  NZ  . LYS B  1 143 ? 37.343 20.206  39.484  1.00 64.43 ? 144 LYS B NZ  1 
ATOM   2506 N  N   . ILE B  1 144 ? 42.089 21.588  36.114  1.00 33.46 ? 145 ILE B N   1 
ATOM   2507 C  CA  . ILE B  1 144 ? 43.006 22.349  36.960  1.00 35.81 ? 145 ILE B CA  1 
ATOM   2508 C  C   . ILE B  1 144 ? 43.286 23.720  36.344  1.00 35.67 ? 145 ILE B C   1 
ATOM   2509 O  O   . ILE B  1 144 ? 43.380 24.734  37.052  1.00 30.94 ? 145 ILE B O   1 
ATOM   2510 C  CB  . ILE B  1 144 ? 44.299 21.551  37.196  1.00 35.54 ? 145 ILE B CB  1 
ATOM   2511 C  CG1 . ILE B  1 144 ? 43.990 20.288  38.003  1.00 38.33 ? 145 ILE B CG1 1 
ATOM   2512 C  CG2 . ILE B  1 144 ? 45.354 22.420  37.903  1.00 32.76 ? 145 ILE B CG2 1 
ATOM   2513 C  CD1 . ILE B  1 144 ? 45.087 19.223  37.917  1.00 37.36 ? 145 ILE B CD1 1 
ATOM   2514 N  N   . GLY B  1 145 ? 43.420 23.771  35.016  1.00 33.53 ? 146 GLY B N   1 
ATOM   2515 C  CA  . GLY B  1 145 ? 43.571 25.053  34.345  1.00 37.45 ? 146 GLY B CA  1 
ATOM   2516 C  C   . GLY B  1 145 ? 42.399 25.982  34.598  1.00 36.36 ? 146 GLY B C   1 
ATOM   2517 O  O   . GLY B  1 145 ? 42.586 27.167  34.881  1.00 32.68 ? 146 GLY B O   1 
ATOM   2518 N  N   . ASP B  1 146 ? 41.172 25.450  34.500  1.00 34.57 ? 147 ASP B N   1 
ATOM   2519 C  CA  . ASP B  1 146 ? 39.975 26.207  34.878  1.00 36.85 ? 147 ASP B CA  1 
ATOM   2520 C  C   . ASP B  1 146 ? 40.093 26.745  36.298  1.00 37.60 ? 147 ASP B C   1 
ATOM   2521 O  O   . ASP B  1 146 ? 39.833 27.929  36.549  1.00 33.00 ? 147 ASP B O   1 
ATOM   2522 C  CB  . ASP B  1 146 ? 38.714 25.333  34.781  1.00 37.45 ? 147 ASP B CB  1 
ATOM   2523 C  CG  . ASP B  1 146 ? 38.275 25.040  33.341  1.00 45.86 ? 147 ASP B CG  1 
ATOM   2524 O  OD1 . ASP B  1 146 ? 38.851 25.606  32.384  1.00 45.76 ? 147 ASP B OD1 1 
ATOM   2525 O  OD2 . ASP B  1 146 ? 37.346 24.215  33.170  1.00 49.15 ? 147 ASP B OD2 1 
ATOM   2526 N  N   . MET B  1 147 ? 40.467 25.874  37.247  1.00 32.78 ? 148 MET B N   1 
ATOM   2527 C  CA  . MET B  1 147 ? 40.502 26.272  38.653  1.00 36.07 ? 148 MET B CA  1 
ATOM   2528 C  C   . MET B  1 147 ? 41.509 27.390  38.877  1.00 34.32 ? 148 MET B C   1 
ATOM   2529 O  O   . MET B  1 147 ? 41.223 28.368  39.576  1.00 31.76 ? 148 MET B O   1 
ATOM   2530 C  CB  . MET B  1 147 ? 40.845 25.087  39.552  1.00 30.58 ? 148 MET B CB  1 
ATOM   2531 C  CG  . MET B  1 147 ? 39.644 24.245  39.946  1.00 42.75 ? 148 MET B CG  1 
ATOM   2532 S  SD  . MET B  1 147 ? 40.061 22.502  40.158  1.00 49.97 ? 148 MET B SD  1 
ATOM   2533 C  CE  . MET B  1 147 ? 40.478 22.581  41.892  1.00 44.20 ? 148 MET B CE  1 
ATOM   2534 N  N   . ILE B  1 148 ? 42.700 27.256  38.295  1.00 30.25 ? 149 ILE B N   1 
ATOM   2535 C  CA  . ILE B  1 148 ? 43.708 28.303  38.420  1.00 34.14 ? 149 ILE B CA  1 
ATOM   2536 C  C   . ILE B  1 148 ? 43.153 29.637  37.937  1.00 32.46 ? 149 ILE B C   1 
ATOM   2537 O  O   . ILE B  1 148 ? 43.320 30.669  38.596  1.00 30.33 ? 149 ILE B O   1 
ATOM   2538 C  CB  . ILE B  1 148 ? 44.974 27.891  37.650  1.00 38.39 ? 149 ILE B CB  1 
ATOM   2539 C  CG1 . ILE B  1 148 ? 45.570 26.631  38.298  1.00 36.25 ? 149 ILE B CG1 1 
ATOM   2540 C  CG2 . ILE B  1 148 ? 45.979 29.039  37.610  1.00 34.43 ? 149 ILE B CG2 1 
ATOM   2541 C  CD1 . ILE B  1 148 ? 46.922 26.230  37.749  1.00 33.63 ? 149 ILE B CD1 1 
ATOM   2542 N  N   . THR B  1 149 ? 42.444 29.628  36.803  1.00 31.78 ? 150 THR B N   1 
ATOM   2543 C  CA  . THR B  1 149 ? 41.870 30.866  36.288  1.00 33.89 ? 150 THR B CA  1 
ATOM   2544 C  C   . THR B  1 149 ? 40.814 31.416  37.243  1.00 29.85 ? 150 THR B C   1 
ATOM   2545 O  O   . THR B  1 149 ? 40.798 32.621  37.533  1.00 29.96 ? 150 THR B O   1 
ATOM   2546 C  CB  . THR B  1 149 ? 41.282 30.629  34.891  1.00 32.14 ? 150 THR B CB  1 
ATOM   2547 O  OG1 . THR B  1 149 ? 42.332 30.242  34.002  1.00 33.54 ? 150 THR B OG1 1 
ATOM   2548 C  CG2 . THR B  1 149 ? 40.616 31.903  34.325  1.00 28.01 ? 150 THR B CG2 1 
ATOM   2549 N  N   . LYS B  1 150 ? 39.938 30.543  37.754  1.00 30.03 ? 151 LYS B N   1 
ATOM   2550 C  CA  . LYS B  1 150 ? 38.897 30.978  38.682  1.00 33.03 ? 151 LYS B CA  1 
ATOM   2551 C  C   . LYS B  1 150 ? 39.498 31.514  39.977  1.00 36.48 ? 151 LYS B C   1 
ATOM   2552 O  O   . LYS B  1 150 ? 39.000 32.494  40.548  1.00 36.99 ? 151 LYS B O   1 
ATOM   2553 C  CB  . LYS B  1 150 ? 37.937 29.828  38.982  1.00 31.57 ? 151 LYS B CB  1 
ATOM   2554 C  CG  . LYS B  1 150 ? 37.120 29.362  37.789  1.00 38.94 ? 151 LYS B CG  1 
ATOM   2555 C  CD  . LYS B  1 150 ? 35.791 28.782  38.238  1.00 44.26 ? 151 LYS B CD  1 
ATOM   2556 C  CE  . LYS B  1 150 ? 35.672 27.306  37.904  1.00 50.35 ? 151 LYS B CE  1 
ATOM   2557 N  NZ  . LYS B  1 150 ? 34.248 26.837  37.832  1.00 50.96 ? 151 LYS B NZ  1 
ATOM   2558 N  N   . LEU B  1 151 ? 40.571 30.889  40.458  1.00 33.11 ? 152 LEU B N   1 
ATOM   2559 C  CA  . LEU B  1 151 ? 41.141 31.321  41.726  1.00 34.76 ? 152 LEU B CA  1 
ATOM   2560 C  C   . LEU B  1 151 ? 41.894 32.634  41.570  1.00 36.67 ? 152 LEU B C   1 
ATOM   2561 O  O   . LEU B  1 151 ? 41.912 33.447  42.504  1.00 33.80 ? 152 LEU B O   1 
ATOM   2562 C  CB  . LEU B  1 151 ? 42.050 30.229  42.303  1.00 37.53 ? 152 LEU B CB  1 
ATOM   2563 C  CG  . LEU B  1 151 ? 42.808 30.593  43.590  1.00 40.68 ? 152 LEU B CG  1 
ATOM   2564 C  CD1 . LEU B  1 151 ? 41.838 31.007  44.691  1.00 37.55 ? 152 LEU B CD1 1 
ATOM   2565 C  CD2 . LEU B  1 151 ? 43.701 29.450  44.064  1.00 36.42 ? 152 LEU B CD2 1 
ATOM   2566 N  N   . LYS B  1 152 ? 42.511 32.866  40.405  1.00 33.39 ? 153 LYS B N   1 
ATOM   2567 C  CA  . LYS B  1 152 ? 43.172 34.148  40.176  1.00 35.88 ? 153 LYS B CA  1 
ATOM   2568 C  C   . LYS B  1 152 ? 42.165 35.287  40.069  1.00 38.29 ? 153 LYS B C   1 
ATOM   2569 O  O   . LYS B  1 152 ? 42.456 36.404  40.509  1.00 40.71 ? 153 LYS B O   1 
ATOM   2570 C  CB  . LYS B  1 152 ? 44.030 34.091  38.920  1.00 33.89 ? 153 LYS B CB  1 
ATOM   2571 C  CG  . LYS B  1 152 ? 45.342 33.379  39.127  1.00 37.48 ? 153 LYS B CG  1 
ATOM   2572 C  CD  . LYS B  1 152 ? 46.044 33.194  37.811  1.00 36.96 ? 153 LYS B CD  1 
ATOM   2573 C  CE  . LYS B  1 152 ? 47.482 32.793  38.021  1.00 37.15 ? 153 LYS B CE  1 
ATOM   2574 N  NZ  . LYS B  1 152 ? 48.035 32.289  36.717  1.00 46.11 ? 153 LYS B NZ  1 
ATOM   2575 N  N   . ARG B  1 153 ? 40.988 35.021  39.485  1.00 33.53 ? 154 ARG B N   1 
ATOM   2576 C  CA  . ARG B  1 153 ? 39.923 36.020  39.434  1.00 35.83 ? 154 ARG B CA  1 
ATOM   2577 C  C   . ARG B  1 153 ? 39.380 36.303  40.829  1.00 38.09 ? 154 ARG B C   1 
ATOM   2578 O  O   . ARG B  1 153 ? 39.340 37.463  41.268  1.00 36.68 ? 154 ARG B O   1 
ATOM   2579 C  CB  . ARG B  1 153 ? 38.792 35.548  38.502  1.00 35.42 ? 154 ARG B CB  1 
ATOM   2580 C  CG  . ARG B  1 153 ? 37.562 36.479  38.469  1.00 36.98 ? 154 ARG B CG  1 
ATOM   2581 C  CD  . ARG B  1 153 ? 36.483 36.022  37.480  1.00 35.46 ? 154 ARG B CD  1 
ATOM   2582 N  NE  . ARG B  1 153 ? 36.976 35.959  36.107  1.00 39.71 ? 154 ARG B NE  1 
ATOM   2583 C  CZ  . ARG B  1 153 ? 37.092 34.845  35.395  1.00 34.23 ? 154 ARG B CZ  1 
ATOM   2584 N  NH1 . ARG B  1 153 ? 36.747 33.665  35.891  1.00 31.41 ? 154 ARG B NH1 1 
ATOM   2585 N  NH2 . ARG B  1 153 ? 37.568 34.915  34.154  1.00 35.96 ? 154 ARG B NH2 1 
ATOM   2586 N  N   . ALA B  1 154 ? 38.967 35.244  41.543  1.00 33.19 ? 155 ALA B N   1 
ATOM   2587 C  CA  . ALA B  1 154 ? 38.385 35.401  42.872  1.00 38.63 ? 155 ALA B CA  1 
ATOM   2588 C  C   . ALA B  1 154 ? 39.376 36.030  43.841  1.00 40.29 ? 155 ALA B C   1 
ATOM   2589 O  O   . ALA B  1 154 ? 39.034 36.959  44.583  1.00 37.03 ? 155 ALA B O   1 
ATOM   2590 C  CB  . ALA B  1 154 ? 37.915 34.050  43.409  1.00 35.36 ? 155 ALA B CB  1 
ATOM   2591 N  N   . GLY B  1 155 ? 40.608 35.529  43.850  1.00 43.17 ? 156 GLY B N   1 
ATOM   2592 C  CA  . GLY B  1 155 ? 41.575 35.872  44.865  1.00 43.12 ? 156 GLY B CA  1 
ATOM   2593 C  C   . GLY B  1 155 ? 42.795 36.523  44.255  1.00 43.59 ? 156 GLY B C   1 
ATOM   2594 O  O   . GLY B  1 155 ? 42.716 37.625  43.703  1.00 51.80 ? 156 GLY B O   1 
ATOM   2595 N  N   . PRO B  1 156 ? 43.949 35.832  44.297  1.00 46.86 ? 157 PRO B N   1 
ATOM   2596 C  CA  . PRO B  1 156 ? 44.132 34.462  44.815  1.00 43.39 ? 157 PRO B CA  1 
ATOM   2597 C  C   . PRO B  1 156 ? 44.237 34.284  46.338  1.00 48.72 ? 157 PRO B C   1 
ATOM   2598 O  O   . PRO B  1 156 ? 44.322 33.133  46.763  1.00 46.69 ? 157 PRO B O   1 
ATOM   2599 C  CB  . PRO B  1 156 ? 45.451 34.024  44.168  1.00 45.08 ? 157 PRO B CB  1 
ATOM   2600 C  CG  . PRO B  1 156 ? 46.187 35.326  43.895  1.00 39.52 ? 157 PRO B CG  1 
ATOM   2601 C  CD  . PRO B  1 156 ? 45.115 36.291  43.515  1.00 42.16 ? 157 PRO B CD  1 
ATOM   2602 N  N   . THR B  1 157 ? 44.230 35.352  47.137  1.00 49.17 ? 158 THR B N   1 
ATOM   2603 C  CA  . THR B  1 157 ? 44.353 35.231  48.592  1.00 46.97 ? 158 THR B CA  1 
ATOM   2604 C  C   . THR B  1 157 ? 43.146 35.858  49.294  1.00 43.85 ? 158 THR B C   1 
ATOM   2605 O  O   . THR B  1 157 ? 42.231 36.391  48.661  1.00 46.55 ? 158 THR B O   1 
ATOM   2606 C  CB  . THR B  1 157 ? 45.650 35.876  49.090  1.00 48.78 ? 158 THR B CB  1 
ATOM   2607 O  OG1 . THR B  1 157 ? 45.561 37.299  48.951  1.00 51.93 ? 158 THR B OG1 1 
ATOM   2608 C  CG2 . THR B  1 157 ? 46.836 35.372  48.275  1.00 52.83 ? 158 THR B CG2 1 
ATOM   2609 N  N   . GLY B  1 158 ? 43.155 35.776  50.626  1.00 45.67 ? 159 GLY B N   1 
ATOM   2610 C  CA  . GLY B  1 158 ? 42.145 36.431  51.448  1.00 40.99 ? 159 GLY B CA  1 
ATOM   2611 C  C   . GLY B  1 158 ? 40.740 35.900  51.209  1.00 37.43 ? 159 GLY B C   1 
ATOM   2612 O  O   . GLY B  1 158 ? 40.510 34.692  51.046  1.00 36.55 ? 159 GLY B O   1 
ATOM   2613 N  N   . LEU B  1 159 ? 39.780 36.826  51.196  1.00 33.22 ? 160 LEU B N   1 
ATOM   2614 C  CA  . LEU B  1 159 ? 38.376 36.455  51.075  1.00 34.30 ? 160 LEU B CA  1 
ATOM   2615 C  C   . LEU B  1 159 ? 38.097 35.728  49.762  1.00 36.92 ? 160 LEU B C   1 
ATOM   2616 O  O   . LEU B  1 159 ? 37.266 34.814  49.725  1.00 35.70 ? 160 LEU B O   1 
ATOM   2617 C  CB  . LEU B  1 159 ? 37.510 37.712  51.208  1.00 33.46 ? 160 LEU B CB  1 
ATOM   2618 C  CG  . LEU B  1 159 ? 36.002 37.609  50.966  1.00 34.20 ? 160 LEU B CG  1 
ATOM   2619 C  CD1 . LEU B  1 159 ? 35.325 36.652  51.963  1.00 32.71 ? 160 LEU B CD1 1 
ATOM   2620 C  CD2 . LEU B  1 159 ? 35.366 38.997  51.012  1.00 34.95 ? 160 LEU B CD2 1 
ATOM   2621 N  N   . GLY B  1 160 ? 38.786 36.104  48.683  1.00 35.69 ? 161 GLY B N   1 
ATOM   2622 C  CA  . GLY B  1 160 ? 38.606 35.396  47.430  1.00 33.89 ? 161 GLY B CA  1 
ATOM   2623 C  C   . GLY B  1 160 ? 38.991 33.934  47.531  1.00 38.40 ? 161 GLY B C   1 
ATOM   2624 O  O   . GLY B  1 160 ? 38.277 33.056  47.037  1.00 36.76 ? 161 GLY B O   1 
ATOM   2625 N  N   . GLU B  1 161 ? 40.124 33.648  48.182  1.00 39.50 ? 162 GLU B N   1 
ATOM   2626 C  CA  . GLU B  1 161 ? 40.517 32.257  48.372  1.00 38.34 ? 162 GLU B CA  1 
ATOM   2627 C  C   . GLU B  1 161 ? 39.550 31.557  49.320  1.00 40.09 ? 162 GLU B C   1 
ATOM   2628 O  O   . GLU B  1 161 ? 39.196 30.389  49.113  1.00 39.62 ? 162 GLU B O   1 
ATOM   2629 C  CB  . GLU B  1 161 ? 41.968 32.187  48.872  1.00 42.61 ? 162 GLU B CB  1 
ATOM   2630 C  CG  . GLU B  1 161 ? 42.444 30.830  49.420  1.00 45.82 ? 162 GLU B CG  1 
ATOM   2631 C  CD  . GLU B  1 161 ? 43.856 30.892  50.048  1.00 53.24 ? 162 GLU B CD  1 
ATOM   2632 O  OE1 . GLU B  1 161 ? 44.825 30.371  49.435  1.00 52.66 ? 162 GLU B OE1 1 
ATOM   2633 O  OE2 . GLU B  1 161 ? 44.003 31.480  51.148  1.00 54.73 ? 162 GLU B OE2 1 
ATOM   2634 N  N   . TYR B  1 162 ? 39.069 32.271  50.336  1.00 38.34 ? 163 TYR B N   1 
ATOM   2635 C  CA  . TYR B  1 162 ? 38.090 31.672  51.232  1.00 38.49 ? 163 TYR B CA  1 
ATOM   2636 C  C   . TYR B  1 162 ? 36.808 31.331  50.481  1.00 41.37 ? 163 TYR B C   1 
ATOM   2637 O  O   . TYR B  1 162 ? 36.221 30.262  50.697  1.00 37.11 ? 163 TYR B O   1 
ATOM   2638 C  CB  . TYR B  1 162 ? 37.808 32.612  52.404  1.00 33.55 ? 163 TYR B CB  1 
ATOM   2639 C  CG  . TYR B  1 162 ? 36.628 32.191  53.247  1.00 37.75 ? 163 TYR B CG  1 
ATOM   2640 C  CD1 . TYR B  1 162 ? 36.773 31.265  54.281  1.00 34.58 ? 163 TYR B CD1 1 
ATOM   2641 C  CD2 . TYR B  1 162 ? 35.360 32.708  52.999  1.00 38.20 ? 163 TYR B CD2 1 
ATOM   2642 C  CE1 . TYR B  1 162 ? 35.693 30.884  55.049  1.00 37.57 ? 163 TYR B CE1 1 
ATOM   2643 C  CE2 . TYR B  1 162 ? 34.272 32.329  53.754  1.00 42.88 ? 163 TYR B CE2 1 
ATOM   2644 C  CZ  . TYR B  1 162 ? 34.441 31.421  54.782  1.00 42.84 ? 163 TYR B CZ  1 
ATOM   2645 O  OH  . TYR B  1 162 ? 33.343 31.056  55.531  1.00 39.68 ? 163 TYR B OH  1 
ATOM   2646 N  N   . MET B  1 163 ? 36.362 32.225  49.587  1.00 38.13 ? 164 MET B N   1 
ATOM   2647 C  CA  . MET B  1 163 ? 35.149 31.961  48.817  1.00 39.39 ? 164 MET B CA  1 
ATOM   2648 C  C   . MET B  1 163 ? 35.378 30.875  47.769  1.00 42.82 ? 164 MET B C   1 
ATOM   2649 O  O   . MET B  1 163 ? 34.514 30.012  47.566  1.00 40.79 ? 164 MET B O   1 
ATOM   2650 C  CB  . MET B  1 163 ? 34.649 33.244  48.147  1.00 37.94 ? 164 MET B CB  1 
ATOM   2651 C  CG  . MET B  1 163 ? 34.106 34.323  49.112  1.00 44.03 ? 164 MET B CG  1 
ATOM   2652 S  SD  . MET B  1 163 ? 32.749 33.782  50.198  1.00 46.10 ? 164 MET B SD  1 
ATOM   2653 C  CE  . MET B  1 163 ? 31.544 33.137  49.022  1.00 48.87 ? 164 MET B CE  1 
ATOM   2654 N  N   . PHE B  1 164 ? 36.534 30.900  47.087  1.00 38.29 ? 165 PHE B N   1 
ATOM   2655 C  CA  . PHE B  1 164 ? 36.812 29.861  46.093  1.00 41.56 ? 165 PHE B CA  1 
ATOM   2656 C  C   . PHE B  1 164 ? 36.851 28.479  46.737  1.00 40.60 ? 165 PHE B C   1 
ATOM   2657 O  O   . PHE B  1 164 ? 36.354 27.500  46.163  1.00 43.21 ? 165 PHE B O   1 
ATOM   2658 C  CB  . PHE B  1 164 ? 38.128 30.137  45.367  1.00 38.17 ? 165 PHE B CB  1 
ATOM   2659 C  CG  . PHE B  1 164 ? 38.518 29.048  44.417  1.00 39.96 ? 165 PHE B CG  1 
ATOM   2660 C  CD1 . PHE B  1 164 ? 37.925 28.961  43.162  1.00 38.90 ? 165 PHE B CD1 1 
ATOM   2661 C  CD2 . PHE B  1 164 ? 39.452 28.084  44.786  1.00 39.74 ? 165 PHE B CD2 1 
ATOM   2662 C  CE1 . PHE B  1 164 ? 38.265 27.935  42.277  1.00 39.79 ? 165 PHE B CE1 1 
ATOM   2663 C  CE2 . PHE B  1 164 ? 39.804 27.062  43.908  1.00 40.62 ? 165 PHE B CE2 1 
ATOM   2664 C  CZ  . PHE B  1 164 ? 39.203 26.990  42.648  1.00 40.68 ? 165 PHE B CZ  1 
ATOM   2665 N  N   . ASP B  1 165 ? 37.432 28.387  47.935  1.00 36.18 ? 166 ASP B N   1 
ATOM   2666 C  CA  . ASP B  1 165 ? 37.520 27.118  48.645  1.00 38.35 ? 166 ASP B CA  1 
ATOM   2667 C  C   . ASP B  1 165 ? 36.146 26.501  48.871  1.00 45.05 ? 166 ASP B C   1 
ATOM   2668 O  O   . ASP B  1 165 ? 36.007 25.272  48.842  1.00 42.78 ? 166 ASP B O   1 
ATOM   2669 C  CB  . ASP B  1 165 ? 38.233 27.338  49.979  1.00 43.39 ? 166 ASP B CB  1 
ATOM   2670 C  CG  . ASP B  1 165 ? 38.238 26.102  50.850  1.00 41.63 ? 166 ASP B CG  1 
ATOM   2671 O  OD1 . ASP B  1 165 ? 39.034 25.189  50.548  1.00 40.68 ? 166 ASP B OD1 1 
ATOM   2672 O  OD2 . ASP B  1 165 ? 37.450 26.040  51.825  1.00 43.97 ? 166 ASP B OD2 1 
ATOM   2673 N  N   . LYS B  1 166 ? 35.116 27.335  49.075  1.00 45.85 ? 167 LYS B N   1 
ATOM   2674 C  CA  . LYS B  1 166 ? 33.781 26.813  49.364  1.00 47.87 ? 167 LYS B CA  1 
ATOM   2675 C  C   . LYS B  1 166 ? 33.143 26.168  48.141  1.00 49.98 ? 167 LYS B C   1 
ATOM   2676 O  O   . LYS B  1 166 ? 32.350 25.231  48.285  1.00 52.32 ? 167 LYS B O   1 
ATOM   2677 C  CB  . LYS B  1 166 ? 32.883 27.924  49.917  1.00 52.37 ? 167 LYS B CB  1 
ATOM   2678 C  CG  . LYS B  1 166 ? 33.502 28.693  51.071  1.00 50.81 ? 167 LYS B CG  1 
ATOM   2679 C  CD  . LYS B  1 166 ? 32.548 28.750  52.257  1.00 62.75 ? 167 LYS B CD  1 
ATOM   2680 C  CE  . LYS B  1 166 ? 31.276 29.498  51.895  1.00 63.30 ? 167 LYS B CE  1 
ATOM   2681 N  NZ  . LYS B  1 166 ? 31.396 30.963  52.153  1.00 63.98 ? 167 LYS B NZ  1 
ATOM   2682 N  N   . GLU B  1 167 ? 33.468 26.637  46.935  1.00 49.82 ? 168 GLU B N   1 
ATOM   2683 C  CA  . GLU B  1 167 ? 32.952 25.963  45.748  1.00 51.46 ? 168 GLU B CA  1 
ATOM   2684 C  C   . GLU B  1 167 ? 33.601 24.603  45.548  1.00 52.70 ? 168 GLU B C   1 
ATOM   2685 O  O   . GLU B  1 167 ? 33.002 23.735  44.908  1.00 58.68 ? 168 GLU B O   1 
ATOM   2686 C  CB  . GLU B  1 167 ? 33.137 26.832  44.489  1.00 55.17 ? 168 GLU B CB  1 
ATOM   2687 C  CG  . GLU B  1 167 ? 34.384 26.510  43.627  1.00 56.22 ? 168 GLU B CG  1 
ATOM   2688 C  CD  . GLU B  1 167 ? 34.286 27.044  42.182  1.00 64.49 ? 168 GLU B CD  1 
ATOM   2689 O  OE1 . GLU B  1 167 ? 34.412 28.277  41.970  1.00 61.05 ? 168 GLU B OE1 1 
ATOM   2690 O  OE2 . GLU B  1 167 ? 34.096 26.229  41.248  1.00 69.60 ? 168 GLU B OE2 1 
ATOM   2691 N  N   . LEU B  1 168 ? 34.802 24.388  46.086  1.00 51.32 ? 169 LEU B N   1 
ATOM   2692 C  CA  . LEU B  1 168 ? 35.431 23.074  45.986  1.00 51.98 ? 169 LEU B CA  1 
ATOM   2693 C  C   . LEU B  1 168 ? 34.852 22.055  46.962  1.00 55.45 ? 169 LEU B C   1 
ATOM   2694 O  O   . LEU B  1 168 ? 34.952 20.847  46.707  1.00 53.69 ? 169 LEU B O   1 
ATOM   2695 C  CB  . LEU B  1 168 ? 36.935 23.188  46.224  1.00 48.11 ? 169 LEU B CB  1 
ATOM   2696 C  CG  . LEU B  1 168 ? 37.773 23.527  44.997  1.00 48.12 ? 169 LEU B CG  1 
ATOM   2697 C  CD1 . LEU B  1 168 ? 39.248 23.534  45.381  1.00 41.03 ? 169 LEU B CD1 1 
ATOM   2698 C  CD2 . LEU B  1 168 ? 37.480 22.516  43.907  1.00 45.70 ? 169 LEU B CD2 1 
ATOM   2699 N  N   . ASN B  1 169 ? 34.254 22.507  48.064  1.00 53.72 ? 170 ASN B N   1 
ATOM   2700 C  CA  . ASN B  1 169 ? 33.807 21.608  49.126  1.00 59.07 ? 170 ASN B CA  1 
ATOM   2701 C  C   . ASN B  1 169 ? 32.409 21.042  48.880  1.00 67.51 ? 170 ASN B C   1 
ATOM   2702 O  O   . ASN B  1 169 ? 31.438 21.788  48.679  1.00 70.36 ? 170 ASN B O   1 
ATOM   2703 C  CB  . ASN B  1 169 ? 33.844 22.331  50.481  1.00 55.26 ? 170 ASN B CB  1 
ATOM   2704 C  CG  . ASN B  1 169 ? 33.982 21.365  51.658  1.00 64.10 ? 170 ASN B CG  1 
ATOM   2705 O  OD1 . ASN B  1 169 ? 34.166 20.154  51.472  1.00 67.13 ? 170 ASN B OD1 1 
ATOM   2706 N  ND2 . ASN B  1 169 ? 33.885 21.899  52.879  1.00 63.49 ? 170 ASN B ND2 1 
ATOM   2707 O  OXT . ASN B  1 169 ? 32.232 19.816  48.901  1.00 70.40 ? 170 ASN B OXT 1 
ATOM   2708 N  N   . ALA C  1 1   ? 34.388 58.073  17.198  1.00 63.09 ? 2   ALA C N   1 
ATOM   2709 C  CA  . ALA C  1 1   ? 34.421 57.267  15.980  1.00 65.90 ? 2   ALA C CA  1 
ATOM   2710 C  C   . ALA C  1 1   ? 35.139 58.001  14.847  1.00 58.61 ? 2   ALA C C   1 
ATOM   2711 O  O   . ALA C  1 1   ? 36.145 58.676  15.073  1.00 60.75 ? 2   ALA C O   1 
ATOM   2712 C  CB  . ALA C  1 1   ? 33.001 56.880  15.545  1.00 59.44 ? 2   ALA C CB  1 
ATOM   2713 N  N   . SER C  1 2   ? 34.603 57.870  13.633  1.00 49.71 ? 3   SER C N   1 
ATOM   2714 C  CA  . SER C  1 2   ? 35.308 58.307  12.437  1.00 47.37 ? 3   SER C CA  1 
ATOM   2715 C  C   . SER C  1 2   ? 35.200 59.814  12.259  1.00 43.56 ? 3   SER C C   1 
ATOM   2716 O  O   . SER C  1 2   ? 34.105 60.377  12.311  1.00 43.41 ? 3   SER C O   1 
ATOM   2717 C  CB  . SER C  1 2   ? 34.749 57.604  11.204  1.00 46.15 ? 3   SER C CB  1 
ATOM   2718 O  OG  . SER C  1 2   ? 35.452 58.006  10.038  1.00 48.83 ? 3   SER C OG  1 
ATOM   2719 N  N   . GLN C  1 3   ? 36.339 60.463  12.021  1.00 41.76 ? 4   GLN C N   1 
ATOM   2720 C  CA  . GLN C  1 3   ? 36.352 61.897  11.763  1.00 35.76 ? 4   GLN C CA  1 
ATOM   2721 C  C   . GLN C  1 3   ? 35.814 62.260  10.380  1.00 38.15 ? 4   GLN C C   1 
ATOM   2722 O  O   . GLN C  1 3   ? 35.574 63.442  10.132  1.00 33.76 ? 4   GLN C O   1 
ATOM   2723 C  CB  . GLN C  1 3   ? 37.774 62.449  11.912  1.00 36.61 ? 4   GLN C CB  1 
ATOM   2724 C  CG  . GLN C  1 3   ? 38.691 62.048  10.750  1.00 39.75 ? 4   GLN C CG  1 
ATOM   2725 C  CD  . GLN C  1 3   ? 40.172 62.391  10.972  1.00 43.38 ? 4   GLN C CD  1 
ATOM   2726 O  OE1 . GLN C  1 3   ? 40.511 63.426  11.555  1.00 42.45 ? 4   GLN C OE1 1 
ATOM   2727 N  NE2 . GLN C  1 3   ? 41.055 61.519  10.493  1.00 41.88 ? 4   GLN C NE2 1 
ATOM   2728 N  N   . VAL C  1 4   ? 35.625 61.298  9.471   1.00 35.74 ? 5   VAL C N   1 
ATOM   2729 C  CA  . VAL C  1 4   ? 35.116 61.609  8.142   1.00 34.26 ? 5   VAL C CA  1 
ATOM   2730 C  C   . VAL C  1 4   ? 33.670 61.176  7.936   1.00 38.51 ? 5   VAL C C   1 
ATOM   2731 O  O   . VAL C  1 4   ? 33.016 61.709  7.027   1.00 35.78 ? 5   VAL C O   1 
ATOM   2732 C  CB  . VAL C  1 4   ? 35.997 61.013  7.019   1.00 36.54 ? 5   VAL C CB  1 
ATOM   2733 C  CG1 . VAL C  1 4   ? 37.479 61.253  7.283   1.00 37.17 ? 5   VAL C CG1 1 
ATOM   2734 C  CG2 . VAL C  1 4   ? 35.678 59.532  6.806   1.00 33.54 ? 5   VAL C CG2 1 
ATOM   2735 N  N   . ARG C  1 5   ? 33.153 60.236  8.732   1.00 36.20 ? 6   ARG C N   1 
ATOM   2736 C  CA  . ARG C  1 5   ? 31.828 59.670  8.482   1.00 35.42 ? 6   ARG C CA  1 
ATOM   2737 C  C   . ARG C  1 5   ? 30.735 60.736  8.567   1.00 39.03 ? 6   ARG C C   1 
ATOM   2738 O  O   . ARG C  1 5   ? 30.641 61.470  9.554   1.00 37.35 ? 6   ARG C O   1 
ATOM   2739 C  CB  . ARG C  1 5   ? 31.549 58.558  9.491   1.00 36.38 ? 6   ARG C CB  1 
ATOM   2740 C  CG  . ARG C  1 5   ? 30.368 57.666  9.138   1.00 36.05 ? 6   ARG C CG  1 
ATOM   2741 C  CD  . ARG C  1 5   ? 29.961 56.831  10.338  1.00 36.98 ? 6   ARG C CD  1 
ATOM   2742 N  NE  . ARG C  1 5   ? 28.944 55.852  9.981   1.00 39.43 ? 6   ARG C NE  1 
ATOM   2743 C  CZ  . ARG C  1 5   ? 29.152 54.546  9.895   1.00 41.94 ? 6   ARG C CZ  1 
ATOM   2744 N  NH1 . ARG C  1 5   ? 30.333 54.013  10.172  1.00 41.67 ? 6   ARG C NH1 1 
ATOM   2745 N  NH2 . ARG C  1 5   ? 28.148 53.752  9.524   1.00 39.73 ? 6   ARG C NH2 1 
ATOM   2746 N  N   . GLN C  1 6   ? 29.886 60.803  7.541   1.00 31.38 ? 7   GLN C N   1 
ATOM   2747 C  CA  . GLN C  1 6   ? 28.774 61.745  7.570   1.00 35.92 ? 7   GLN C CA  1 
ATOM   2748 C  C   . GLN C  1 6   ? 27.630 61.203  6.719   1.00 36.27 ? 7   GLN C C   1 
ATOM   2749 O  O   . GLN C  1 6   ? 27.834 60.865  5.547   1.00 33.86 ? 7   GLN C O   1 
ATOM   2750 C  CB  . GLN C  1 6   ? 29.234 63.125  7.069   1.00 34.66 ? 7   GLN C CB  1 
ATOM   2751 C  CG  . GLN C  1 6   ? 28.220 64.245  7.200   1.00 33.17 ? 7   GLN C CG  1 
ATOM   2752 C  CD  . GLN C  1 6   ? 28.816 65.601  6.816   1.00 44.84 ? 7   GLN C CD  1 
ATOM   2753 O  OE1 . GLN C  1 6   ? 29.833 65.675  6.109   1.00 41.61 ? 7   GLN C OE1 1 
ATOM   2754 N  NE2 . GLN C  1 6   ? 28.172 66.677  7.254   1.00 38.72 ? 7   GLN C NE2 1 
ATOM   2755 N  N   . ASN C  1 7   ? 26.433 61.110  7.314   1.00 34.90 ? 8   ASN C N   1 
ATOM   2756 C  CA  . ASN C  1 7   ? 25.230 60.655  6.611   1.00 37.66 ? 8   ASN C CA  1 
ATOM   2757 C  C   . ASN C  1 7   ? 25.396 59.230  6.051   1.00 38.16 ? 8   ASN C C   1 
ATOM   2758 O  O   . ASN C  1 7   ? 24.853 58.886  4.993   1.00 35.25 ? 8   ASN C O   1 
ATOM   2759 C  CB  . ASN C  1 7   ? 24.851 61.645  5.500   1.00 37.15 ? 8   ASN C CB  1 
ATOM   2760 C  CG  . ASN C  1 7   ? 23.424 61.453  5.001   1.00 40.06 ? 8   ASN C CG  1 
ATOM   2761 O  OD1 . ASN C  1 7   ? 22.514 61.167  5.784   1.00 46.49 ? 8   ASN C OD1 1 
ATOM   2762 N  ND2 . ASN C  1 7   ? 23.231 61.579  3.690   1.00 36.47 ? 8   ASN C ND2 1 
ATOM   2763 N  N   . TYR C  1 8   ? 26.152 58.385  6.751   1.00 32.82 ? 9   TYR C N   1 
ATOM   2764 C  CA  . TYR C  1 8   ? 26.451 57.022  6.310   1.00 34.02 ? 9   TYR C CA  1 
ATOM   2765 C  C   . TYR C  1 8   ? 25.830 56.056  7.311   1.00 36.34 ? 9   TYR C C   1 
ATOM   2766 O  O   . TYR C  1 8   ? 26.344 55.891  8.421   1.00 33.86 ? 9   TYR C O   1 
ATOM   2767 C  CB  . TYR C  1 8   ? 27.961 56.803  6.206   1.00 32.69 ? 9   TYR C CB  1 
ATOM   2768 C  CG  . TYR C  1 8   ? 28.385 55.530  5.493   1.00 34.57 ? 9   TYR C CG  1 
ATOM   2769 C  CD1 . TYR C  1 8   ? 27.878 55.199  4.237   1.00 35.18 ? 9   TYR C CD1 1 
ATOM   2770 C  CD2 . TYR C  1 8   ? 29.303 54.668  6.074   1.00 35.17 ? 9   TYR C CD2 1 
ATOM   2771 C  CE1 . TYR C  1 8   ? 28.279 54.045  3.587   1.00 35.93 ? 9   TYR C CE1 1 
ATOM   2772 C  CE2 . TYR C  1 8   ? 29.706 53.514  5.437   1.00 35.28 ? 9   TYR C CE2 1 
ATOM   2773 C  CZ  . TYR C  1 8   ? 29.199 53.205  4.200   1.00 36.16 ? 9   TYR C CZ  1 
ATOM   2774 O  OH  . TYR C  1 8   ? 29.607 52.045  3.581   1.00 38.68 ? 9   TYR C OH  1 
ATOM   2775 N  N   . HIS C  1 9   ? 24.737 55.414  6.923   1.00 36.21 ? 10  HIS C N   1 
ATOM   2776 C  CA  . HIS C  1 9   ? 23.946 54.649  7.874   1.00 41.33 ? 10  HIS C CA  1 
ATOM   2777 C  C   . HIS C  1 9   ? 24.565 53.271  8.093   1.00 39.23 ? 10  HIS C C   1 
ATOM   2778 O  O   . HIS C  1 9   ? 25.162 52.689  7.187   1.00 39.19 ? 10  HIS C O   1 
ATOM   2779 C  CB  . HIS C  1 9   ? 22.506 54.528  7.367   1.00 38.81 ? 10  HIS C CB  1 
ATOM   2780 C  CG  . HIS C  1 9   ? 21.532 54.043  8.397   1.00 52.94 ? 10  HIS C CG  1 
ATOM   2781 N  ND1 . HIS C  1 9   ? 20.528 54.842  8.908   1.00 52.66 ? 10  HIS C ND1 1 
ATOM   2782 C  CD2 . HIS C  1 9   ? 21.393 52.835  8.999   1.00 49.49 ? 10  HIS C CD2 1 
ATOM   2783 C  CE1 . HIS C  1 9   ? 19.824 54.150  9.788   1.00 52.58 ? 10  HIS C CE1 1 
ATOM   2784 N  NE2 . HIS C  1 9   ? 20.328 52.929  9.861   1.00 52.43 ? 10  HIS C NE2 1 
ATOM   2785 N  N   . GLU C  1 10  ? 24.411 52.745  9.314   1.00 42.85 ? 11  GLU C N   1 
ATOM   2786 C  CA  . GLU C  1 10  ? 24.926 51.407  9.624   1.00 45.28 ? 11  GLU C CA  1 
ATOM   2787 C  C   . GLU C  1 10  ? 24.292 50.331  8.743   1.00 44.22 ? 11  GLU C C   1 
ATOM   2788 O  O   . GLU C  1 10  ? 24.936 49.316  8.450   1.00 40.35 ? 11  GLU C O   1 
ATOM   2789 C  CB  . GLU C  1 10  ? 24.701 51.087  11.105  1.00 50.47 ? 11  GLU C CB  1 
ATOM   2790 C  CG  . GLU C  1 10  ? 25.772 51.693  12.044  1.00 65.62 ? 11  GLU C CG  1 
ATOM   2791 C  CD  . GLU C  1 10  ? 27.038 50.821  12.206  1.00 77.08 ? 11  GLU C CD  1 
ATOM   2792 O  OE1 . GLU C  1 10  ? 28.159 51.391  12.283  1.00 74.42 ? 11  GLU C OE1 1 
ATOM   2793 O  OE2 . GLU C  1 10  ? 26.915 49.574  12.282  1.00 77.86 ? 11  GLU C OE2 1 
ATOM   2794 N  N   . ASP C  1 11  ? 23.032 50.531  8.332   1.00 41.61 ? 12  ASP C N   1 
ATOM   2795 C  CA  . ASP C  1 11  ? 22.400 49.733  7.282   1.00 43.11 ? 12  ASP C CA  1 
ATOM   2796 C  C   . ASP C  1 11  ? 23.318 49.581  6.078   1.00 39.80 ? 12  ASP C C   1 
ATOM   2797 O  O   . ASP C  1 11  ? 23.589 48.471  5.607   1.00 39.19 ? 12  ASP C O   1 
ATOM   2798 C  CB  . ASP C  1 11  ? 21.104 50.415  6.815   1.00 49.08 ? 12  ASP C CB  1 
ATOM   2799 C  CG  . ASP C  1 11  ? 19.881 49.986  7.590   1.00 58.99 ? 12  ASP C CG  1 
ATOM   2800 O  OD1 . ASP C  1 11  ? 20.023 49.181  8.539   1.00 55.19 ? 12  ASP C OD1 1 
ATOM   2801 O  OD2 . ASP C  1 11  ? 18.772 50.456  7.227   1.00 62.22 ? 12  ASP C OD2 1 
ATOM   2802 N  N   . ALA C  1 12  ? 23.756 50.713  5.533   1.00 37.49 ? 13  ALA C N   1 
ATOM   2803 C  CA  . ALA C  1 12  ? 24.559 50.696  4.322   1.00 36.66 ? 13  ALA C CA  1 
ATOM   2804 C  C   . ALA C  1 12  ? 25.910 50.045  4.573   1.00 36.11 ? 13  ALA C C   1 
ATOM   2805 O  O   . ALA C  1 12  ? 26.370 49.229  3.765   1.00 35.87 ? 13  ALA C O   1 
ATOM   2806 C  CB  . ALA C  1 12  ? 24.738 52.118  3.803   1.00 34.63 ? 13  ALA C CB  1 
ATOM   2807 N  N   . GLU C  1 13  ? 26.557 50.391  5.695   1.00 37.62 ? 14  GLU C N   1 
ATOM   2808 C  CA  . GLU C  1 13  ? 27.850 49.795  6.021   1.00 36.50 ? 14  GLU C CA  1 
ATOM   2809 C  C   . GLU C  1 13  ? 27.783 48.281  5.983   1.00 35.41 ? 14  GLU C C   1 
ATOM   2810 O  O   . GLU C  1 13  ? 28.679 47.630  5.437   1.00 35.19 ? 14  GLU C O   1 
ATOM   2811 C  CB  . GLU C  1 13  ? 28.317 50.249  7.398   1.00 35.40 ? 14  GLU C CB  1 
ATOM   2812 C  CG  . GLU C  1 13  ? 29.801 50.058  7.655   1.00 39.45 ? 14  GLU C CG  1 
ATOM   2813 C  CD  . GLU C  1 13  ? 30.205 50.487  9.070   1.00 47.66 ? 14  GLU C CD  1 
ATOM   2814 O  OE1 . GLU C  1 13  ? 29.424 51.238  9.708   1.00 52.59 ? 14  GLU C OE1 1 
ATOM   2815 O  OE2 . GLU C  1 13  ? 31.305 50.112  9.533   1.00 46.96 ? 14  GLU C OE2 1 
ATOM   2816 N  N   . ALA C  1 14  ? 26.718 47.700  6.549   1.00 33.09 ? 15  ALA C N   1 
ATOM   2817 C  CA  . ALA C  1 14  ? 26.643 46.248  6.628   1.00 33.17 ? 15  ALA C CA  1 
ATOM   2818 C  C   . ALA C  1 14  ? 26.313 45.636  5.277   1.00 33.56 ? 15  ALA C C   1 
ATOM   2819 O  O   . ALA C  1 14  ? 26.831 44.564  4.938   1.00 32.80 ? 15  ALA C O   1 
ATOM   2820 C  CB  . ALA C  1 14  ? 25.613 45.815  7.677   1.00 30.12 ? 15  ALA C CB  1 
ATOM   2821 N  N   . SER C  1 15  ? 25.456 46.290  4.486   1.00 32.40 ? 16  SER C N   1 
ATOM   2822 C  CA  . SER C  1 15  ? 25.160 45.721  3.175   1.00 37.37 ? 16  SER C CA  1 
ATOM   2823 C  C   . SER C  1 15  ? 26.355 45.817  2.235   1.00 32.45 ? 16  SER C C   1 
ATOM   2824 O  O   . SER C  1 15  ? 26.536 44.936  1.397   1.00 33.59 ? 16  SER C O   1 
ATOM   2825 C  CB  . SER C  1 15  ? 23.943 46.388  2.546   1.00 36.51 ? 16  SER C CB  1 
ATOM   2826 O  OG  . SER C  1 15  ? 22.806 46.229  3.368   1.00 52.71 ? 16  SER C OG  1 
ATOM   2827 N  N   . ILE C  1 16  ? 27.180 46.860  2.365   1.00 32.12 ? 17  ILE C N   1 
ATOM   2828 C  CA  . ILE C  1 16  ? 28.390 46.948  1.551   1.00 32.03 ? 17  ILE C CA  1 
ATOM   2829 C  C   . ILE C  1 16  ? 29.340 45.795  1.878   1.00 33.42 ? 17  ILE C C   1 
ATOM   2830 O  O   . ILE C  1 16  ? 29.940 45.194  0.975   1.00 32.62 ? 17  ILE C O   1 
ATOM   2831 C  CB  . ILE C  1 16  ? 29.078 48.313  1.744   1.00 32.11 ? 17  ILE C CB  1 
ATOM   2832 C  CG1 . ILE C  1 16  ? 28.200 49.465  1.221   1.00 34.66 ? 17  ILE C CG1 1 
ATOM   2833 C  CG2 . ILE C  1 16  ? 30.435 48.321  1.051   1.00 28.06 ? 17  ILE C CG2 1 
ATOM   2834 C  CD1 . ILE C  1 16  ? 28.150 49.560  -0.263  1.00 36.81 ? 17  ILE C CD1 1 
ATOM   2835 N  N   . ASN C  1 17  ? 29.496 45.463  3.168   1.00 28.78 ? 18  ASN C N   1 
ATOM   2836 C  CA  . ASN C  1 17  ? 30.375 44.344  3.515   1.00 30.35 ? 18  ASN C CA  1 
ATOM   2837 C  C   . ASN C  1 17  ? 29.840 43.039  2.945   1.00 29.82 ? 18  ASN C C   1 
ATOM   2838 O  O   . ASN C  1 17  ? 30.616 42.191  2.499   1.00 30.37 ? 18  ASN C O   1 
ATOM   2839 C  CB  . ASN C  1 17  ? 30.548 44.225  5.026   1.00 30.85 ? 18  ASN C CB  1 
ATOM   2840 C  CG  . ASN C  1 17  ? 31.563 45.212  5.572   1.00 35.54 ? 18  ASN C CG  1 
ATOM   2841 O  OD1 . ASN C  1 17  ? 32.489 45.618  4.865   1.00 33.19 ? 18  ASN C OD1 1 
ATOM   2842 N  ND2 . ASN C  1 17  ? 31.388 45.613  6.832   1.00 28.10 ? 18  ASN C ND2 1 
ATOM   2843 N  N   . LYS C  1 18  ? 28.510 42.876  2.920   1.00 29.44 ? 19  LYS C N   1 
ATOM   2844 C  CA  . LYS C  1 18  ? 27.922 41.676  2.330   1.00 35.23 ? 19  LYS C CA  1 
ATOM   2845 C  C   . LYS C  1 18  ? 28.115 41.653  0.816   1.00 35.52 ? 19  LYS C C   1 
ATOM   2846 O  O   . LYS C  1 18  ? 28.328 40.587  0.224   1.00 32.04 ? 19  LYS C O   1 
ATOM   2847 C  CB  . LYS C  1 18  ? 26.431 41.581  2.678   1.00 36.47 ? 19  LYS C CB  1 
ATOM   2848 C  CG  . LYS C  1 18  ? 25.784 40.233  2.333   1.00 45.92 ? 19  LYS C CG  1 
ATOM   2849 C  CD  . LYS C  1 18  ? 24.244 40.312  2.264   1.00 57.39 ? 19  LYS C CD  1 
ATOM   2850 C  CE  . LYS C  1 18  ? 23.578 38.918  2.196   1.00 61.05 ? 19  LYS C CE  1 
ATOM   2851 N  NZ  . LYS C  1 18  ? 23.631 38.240  0.855   1.00 63.91 ? 19  LYS C NZ  1 
ATOM   2852 N  N   . GLN C  1 19  ? 28.046 42.815  0.171   1.00 31.09 ? 20  GLN C N   1 
ATOM   2853 C  CA  . GLN C  1 19  ? 28.229 42.847  -1.273  1.00 33.91 ? 20  GLN C CA  1 
ATOM   2854 C  C   . GLN C  1 19  ? 29.687 42.588  -1.659  1.00 31.39 ? 20  GLN C C   1 
ATOM   2855 O  O   . GLN C  1 19  ? 29.960 41.942  -2.681  1.00 31.20 ? 20  GLN C O   1 
ATOM   2856 C  CB  . GLN C  1 19  ? 27.744 44.181  -1.825  1.00 35.43 ? 20  GLN C CB  1 
ATOM   2857 C  CG  . GLN C  1 19  ? 27.588 44.161  -3.313  1.00 39.48 ? 20  GLN C CG  1 
ATOM   2858 C  CD  . GLN C  1 19  ? 26.393 43.343  -3.729  1.00 45.21 ? 20  GLN C CD  1 
ATOM   2859 O  OE1 . GLN C  1 19  ? 25.341 43.392  -3.083  1.00 46.14 ? 20  GLN C OE1 1 
ATOM   2860 N  NE2 . GLN C  1 19  ? 26.545 42.572  -4.804  1.00 46.11 ? 20  GLN C NE2 1 
ATOM   2861 N  N   . ILE C  1 20  ? 30.636 43.082  -0.859  1.00 29.23 ? 21  ILE C N   1 
ATOM   2862 C  CA  . ILE C  1 20  ? 32.042 42.736  -1.078  1.00 30.96 ? 21  ILE C CA  1 
ATOM   2863 C  C   . ILE C  1 20  ? 32.207 41.226  -1.105  1.00 30.98 ? 21  ILE C C   1 
ATOM   2864 O  O   . ILE C  1 20  ? 32.790 40.660  -2.035  1.00 32.14 ? 21  ILE C O   1 
ATOM   2865 C  CB  . ILE C  1 20  ? 32.936 43.355  0.011   1.00 27.97 ? 21  ILE C CB  1 
ATOM   2866 C  CG1 . ILE C  1 20  ? 33.058 44.858  -0.180  1.00 30.40 ? 21  ILE C CG1 1 
ATOM   2867 C  CG2 . ILE C  1 20  ? 34.313 42.720  -0.026  1.00 24.07 ? 21  ILE C CG2 1 
ATOM   2868 C  CD1 . ILE C  1 20  ? 33.570 45.568  1.061   1.00 29.82 ? 21  ILE C CD1 1 
ATOM   2869 N  N   . ASN C  1 21  ? 31.675 40.550  -0.086  1.00 29.22 ? 22  ASN C N   1 
ATOM   2870 C  CA  . ASN C  1 21  ? 31.800 39.100  -0.034  1.00 29.42 ? 22  ASN C CA  1 
ATOM   2871 C  C   . ASN C  1 21  ? 31.127 38.435  -1.228  1.00 30.15 ? 22  ASN C C   1 
ATOM   2872 O  O   . ASN C  1 21  ? 31.619 37.428  -1.750  1.00 29.96 ? 22  ASN C O   1 
ATOM   2873 C  CB  . ASN C  1 21  ? 31.207 38.558  1.262   1.00 25.25 ? 22  ASN C CB  1 
ATOM   2874 C  CG  . ASN C  1 21  ? 31.425 37.063  1.394   1.00 32.62 ? 22  ASN C CG  1 
ATOM   2875 O  OD1 . ASN C  1 21  ? 30.528 36.271  1.107   1.00 28.78 ? 22  ASN C OD1 1 
ATOM   2876 N  ND2 . ASN C  1 21  ? 32.649 36.667  1.794   1.00 25.82 ? 22  ASN C ND2 1 
ATOM   2877 N  N   . MET C  1 22  ? 29.992 38.974  -1.668  1.00 30.24 ? 23  MET C N   1 
ATOM   2878 C  CA  . MET C  1 22  ? 29.258 38.370  -2.779  1.00 31.68 ? 23  MET C CA  1 
ATOM   2879 C  C   . MET C  1 22  ? 30.053 38.459  -4.083  1.00 33.75 ? 23  MET C C   1 
ATOM   2880 O  O   . MET C  1 22  ? 30.148 37.484  -4.840  1.00 30.47 ? 23  MET C O   1 
ATOM   2881 C  CB  . MET C  1 22  ? 27.905 39.064  -2.939  1.00 33.00 ? 23  MET C CB  1 
ATOM   2882 C  CG  . MET C  1 22  ? 26.924 38.287  -3.787  1.00 38.93 ? 23  MET C CG  1 
ATOM   2883 S  SD  . MET C  1 22  ? 25.368 39.197  -4.048  1.00 58.39 ? 23  MET C SD  1 
ATOM   2884 C  CE  . MET C  1 22  ? 24.412 37.950  -4.929  1.00 43.52 ? 23  MET C CE  1 
ATOM   2885 N  N   . CYS C  1 23  ? 30.612 39.631  -4.377  1.00 29.32 ? 24  CYS C N   1 
ATOM   2886 C  CA  . CYS C  1 23  ? 31.408 39.757  -5.591  1.00 32.84 ? 24  CYS C CA  1 
ATOM   2887 C  C   . CYS C  1 23  ? 32.676 38.899  -5.528  1.00 34.24 ? 24  CYS C C   1 
ATOM   2888 O  O   . CYS C  1 23  ? 33.093 38.342  -6.550  1.00 32.15 ? 24  CYS C O   1 
ATOM   2889 C  CB  . CYS C  1 23  ? 31.720 41.236  -5.842  1.00 31.99 ? 24  CYS C CB  1 
ATOM   2890 S  SG  . CYS C  1 23  ? 30.276 42.089  -6.625  1.00 50.20 ? 24  CYS C SG  1 
ATOM   2891 N  N   . LEU C  1 24  ? 33.269 38.734  -4.340  1.00 29.71 ? 25  LEU C N   1 
ATOM   2892 C  CA  . LEU C  1 24  ? 34.439 37.870  -4.232  1.00 29.21 ? 25  LEU C CA  1 
ATOM   2893 C  C   . LEU C  1 24  ? 34.061 36.425  -4.505  1.00 27.77 ? 25  LEU C C   1 
ATOM   2894 O  O   . LEU C  1 24  ? 34.818 35.692  -5.148  1.00 29.46 ? 25  LEU C O   1 
ATOM   2895 C  CB  . LEU C  1 24  ? 35.080 38.001  -2.848  1.00 26.39 ? 25  LEU C CB  1 
ATOM   2896 C  CG  . LEU C  1 24  ? 35.793 39.316  -2.539  1.00 28.50 ? 25  LEU C CG  1 
ATOM   2897 C  CD1 . LEU C  1 24  ? 36.241 39.338  -1.084  1.00 29.70 ? 25  LEU C CD1 1 
ATOM   2898 C  CD2 . LEU C  1 24  ? 36.980 39.478  -3.472  1.00 30.70 ? 25  LEU C CD2 1 
ATOM   2899 N  N   . TYR C  1 25  ? 32.882 36.005  -4.045  1.00 25.14 ? 26  TYR C N   1 
ATOM   2900 C  CA  . TYR C  1 25  ? 32.412 34.657  -4.344  1.00 30.15 ? 26  TYR C CA  1 
ATOM   2901 C  C   . TYR C  1 25  ? 32.184 34.484  -5.838  1.00 31.96 ? 26  TYR C C   1 
ATOM   2902 O  O   . TYR C  1 25  ? 32.637 33.500  -6.437  1.00 28.25 ? 26  TYR C O   1 
ATOM   2903 C  CB  . TYR C  1 25  ? 31.128 34.344  -3.564  1.00 32.22 ? 26  TYR C CB  1 
ATOM   2904 C  CG  . TYR C  1 25  ? 30.517 33.014  -3.948  1.00 31.39 ? 26  TYR C CG  1 
ATOM   2905 C  CD1 . TYR C  1 25  ? 31.111 31.822  -3.557  1.00 32.23 ? 26  TYR C CD1 1 
ATOM   2906 C  CD2 . TYR C  1 25  ? 29.360 32.949  -4.720  1.00 31.94 ? 26  TYR C CD2 1 
ATOM   2907 C  CE1 . TYR C  1 25  ? 30.574 30.599  -3.908  1.00 32.04 ? 26  TYR C CE1 1 
ATOM   2908 C  CE2 . TYR C  1 25  ? 28.803 31.721  -5.081  1.00 34.86 ? 26  TYR C CE2 1 
ATOM   2909 C  CZ  . TYR C  1 25  ? 29.417 30.549  -4.670  1.00 38.85 ? 26  TYR C CZ  1 
ATOM   2910 O  OH  . TYR C  1 25  ? 28.885 29.322  -5.019  1.00 42.14 ? 26  TYR C OH  1 
ATOM   2911 N  N   . ALA C  1 26  ? 31.482 35.440  -6.461  1.00 30.67 ? 27  ALA C N   1 
ATOM   2912 C  CA  . ALA C  1 26  ? 31.254 35.377  -7.904  1.00 32.16 ? 27  ALA C CA  1 
ATOM   2913 C  C   . ALA C  1 26  ? 32.576 35.290  -8.664  1.00 32.32 ? 27  ALA C C   1 
ATOM   2914 O  O   . ALA C  1 26  ? 32.706 34.518  -9.620  1.00 29.87 ? 27  ALA C O   1 
ATOM   2915 C  CB  . ALA C  1 26  ? 30.452 36.600  -8.368  1.00 32.93 ? 27  ALA C CB  1 
ATOM   2916 N  N   . SER C  1 27  ? 33.574 36.066  -8.235  1.00 29.21 ? 28  SER C N   1 
ATOM   2917 C  CA  . SER C  1 27  ? 34.887 36.001  -8.866  1.00 32.28 ? 28  SER C CA  1 
ATOM   2918 C  C   . SER C  1 27  ? 35.503 34.611  -8.710  1.00 32.26 ? 28  SER C C   1 
ATOM   2919 O  O   . SER C  1 27  ? 36.089 34.072  -9.659  1.00 32.25 ? 28  SER C O   1 
ATOM   2920 C  CB  . SER C  1 27  ? 35.792 37.081  -8.269  1.00 30.55 ? 28  SER C CB  1 
ATOM   2921 O  OG  . SER C  1 27  ? 37.151 36.760  -8.439  1.00 35.46 ? 28  SER C OG  1 
ATOM   2922 N  N   . TYR C  1 28  ? 35.368 34.013  -7.520  1.00 29.01 ? 29  TYR C N   1 
ATOM   2923 C  CA  . TYR C  1 28  ? 35.843 32.651  -7.292  1.00 28.57 ? 29  TYR C CA  1 
ATOM   2924 C  C   . TYR C  1 28  ? 35.125 31.659  -8.208  1.00 30.50 ? 29  TYR C C   1 
ATOM   2925 O  O   . TYR C  1 28  ? 35.754 30.764  -8.787  1.00 27.81 ? 29  TYR C O   1 
ATOM   2926 C  CB  . TYR C  1 28  ? 35.633 32.285  -5.820  1.00 31.24 ? 29  TYR C CB  1 
ATOM   2927 C  CG  . TYR C  1 28  ? 36.562 31.241  -5.238  1.00 30.10 ? 29  TYR C CG  1 
ATOM   2928 C  CD1 . TYR C  1 28  ? 37.788 30.948  -5.836  1.00 26.78 ? 29  TYR C CD1 1 
ATOM   2929 C  CD2 . TYR C  1 28  ? 36.212 30.550  -4.070  1.00 28.39 ? 29  TYR C CD2 1 
ATOM   2930 C  CE1 . TYR C  1 28  ? 38.641 29.999  -5.294  1.00 26.92 ? 29  TYR C CE1 1 
ATOM   2931 C  CE2 . TYR C  1 28  ? 37.058 29.598  -3.513  1.00 28.61 ? 29  TYR C CE2 1 
ATOM   2932 C  CZ  . TYR C  1 28  ? 38.274 29.331  -4.129  1.00 30.28 ? 29  TYR C CZ  1 
ATOM   2933 O  OH  . TYR C  1 28  ? 39.120 28.391  -3.589  1.00 29.85 ? 29  TYR C OH  1 
ATOM   2934 N  N   . VAL C  1 29  ? 33.806 31.815  -8.361  1.00 30.63 ? 30  VAL C N   1 
ATOM   2935 C  CA  . VAL C  1 29  ? 33.028 30.940  -9.239  1.00 28.08 ? 30  VAL C CA  1 
ATOM   2936 C  C   . VAL C  1 29  ? 33.501 31.064  -10.683 1.00 32.42 ? 30  VAL C C   1 
ATOM   2937 O  O   . VAL C  1 29  ? 33.698 30.062  -11.379 1.00 33.65 ? 30  VAL C O   1 
ATOM   2938 C  CB  . VAL C  1 29  ? 31.528 31.251  -9.108  1.00 31.97 ? 30  VAL C CB  1 
ATOM   2939 C  CG1 . VAL C  1 29  ? 30.736 30.490  -10.160 1.00 36.95 ? 30  VAL C CG1 1 
ATOM   2940 C  CG2 . VAL C  1 29  ? 31.032 30.839  -7.728  1.00 30.59 ? 30  VAL C CG2 1 
ATOM   2941 N  N   . TYR C  1 30  ? 33.713 32.299  -11.145 1.00 33.61 ? 31  TYR C N   1 
ATOM   2942 C  CA  . TYR C  1 30  ? 34.217 32.519  -12.495 1.00 31.86 ? 31  TYR C CA  1 
ATOM   2943 C  C   . TYR C  1 30  ? 35.612 31.934  -12.677 1.00 31.13 ? 31  TYR C C   1 
ATOM   2944 O  O   . TYR C  1 30  ? 35.925 31.386  -13.740 1.00 30.00 ? 31  TYR C O   1 
ATOM   2945 C  CB  . TYR C  1 30  ? 34.206 34.015  -12.798 1.00 33.61 ? 31  TYR C CB  1 
ATOM   2946 C  CG  . TYR C  1 30  ? 32.816 34.511  -13.108 1.00 37.26 ? 31  TYR C CG  1 
ATOM   2947 C  CD1 . TYR C  1 30  ? 31.966 33.748  -13.904 1.00 37.87 ? 31  TYR C CD1 1 
ATOM   2948 C  CD2 . TYR C  1 30  ? 32.336 35.722  -12.594 1.00 35.51 ? 31  TYR C CD2 1 
ATOM   2949 C  CE1 . TYR C  1 30  ? 30.688 34.165  -14.195 1.00 42.77 ? 31  TYR C CE1 1 
ATOM   2950 C  CE2 . TYR C  1 30  ? 31.045 36.148  -12.877 1.00 37.23 ? 31  TYR C CE2 1 
ATOM   2951 C  CZ  . TYR C  1 30  ? 30.232 35.357  -13.686 1.00 44.43 ? 31  TYR C CZ  1 
ATOM   2952 O  OH  . TYR C  1 30  ? 28.954 35.730  -14.007 1.00 48.46 ? 31  TYR C OH  1 
ATOM   2953 N  N   . LEU C  1 31  ? 36.464 32.032  -11.650 1.00 29.11 ? 32  LEU C N   1 
ATOM   2954 C  CA  . LEU C  1 31  ? 37.792 31.432  -11.734 1.00 26.77 ? 32  LEU C CA  1 
ATOM   2955 C  C   . LEU C  1 31  ? 37.703 29.920  -11.894 1.00 30.35 ? 32  LEU C C   1 
ATOM   2956 O  O   . LEU C  1 31  ? 38.461 29.319  -12.673 1.00 33.45 ? 32  LEU C O   1 
ATOM   2957 C  CB  . LEU C  1 31  ? 38.600 31.797  -10.492 1.00 27.79 ? 32  LEU C CB  1 
ATOM   2958 C  CG  . LEU C  1 31  ? 40.050 31.320  -10.493 1.00 36.23 ? 32  LEU C CG  1 
ATOM   2959 C  CD1 . LEU C  1 31  ? 40.902 32.131  -11.470 1.00 31.59 ? 32  LEU C CD1 1 
ATOM   2960 C  CD2 . LEU C  1 31  ? 40.615 31.384  -9.072  1.00 33.35 ? 32  LEU C CD2 1 
ATOM   2961 N  N   . SER C  1 32  ? 36.766 29.289  -11.180 1.00 25.14 ? 33  SER C N   1 
ATOM   2962 C  CA  . SER C  1 32  ? 36.602 27.848  -11.281 1.00 29.94 ? 33  SER C CA  1 
ATOM   2963 C  C   . SER C  1 32  ? 36.176 27.438  -12.687 1.00 33.16 ? 33  SER C C   1 
ATOM   2964 O  O   . SER C  1 32  ? 36.721 26.488  -13.256 1.00 33.60 ? 33  SER C O   1 
ATOM   2965 C  CB  . SER C  1 32  ? 35.582 27.366  -10.252 1.00 30.88 ? 33  SER C CB  1 
ATOM   2966 O  OG  . SER C  1 32  ? 35.253 26.006  -10.501 1.00 37.65 ? 33  SER C OG  1 
ATOM   2967 N  N   . MET C  1 33  ? 35.201 28.145  -13.260 1.00 34.13 ? 34  MET C N   1 
ATOM   2968 C  CA  . MET C  1 33  ? 34.814 27.902  -14.650 1.00 36.56 ? 34  MET C CA  1 
ATOM   2969 C  C   . MET C  1 33  ? 35.981 28.096  -15.622 1.00 31.97 ? 34  MET C C   1 
ATOM   2970 O  O   . MET C  1 33  ? 36.167 27.294  -16.542 1.00 34.47 ? 34  MET C O   1 
ATOM   2971 C  CB  . MET C  1 33  ? 33.658 28.825  -15.045 1.00 30.62 ? 34  MET C CB  1 
ATOM   2972 C  CG  . MET C  1 33  ? 32.342 28.612  -14.323 1.00 30.86 ? 34  MET C CG  1 
ATOM   2973 S  SD  . MET C  1 33  ? 31.185 29.827  -15.031 1.00 42.01 ? 34  MET C SD  1 
ATOM   2974 C  CE  . MET C  1 33  ? 29.716 29.676  -14.018 1.00 37.19 ? 34  MET C CE  1 
ATOM   2975 N  N   . ALA C  1 34  ? 36.755 29.171  -15.460 1.00 31.61 ? 35  ALA C N   1 
ATOM   2976 C  CA  . ALA C  1 34  ? 37.839 29.455  -16.399 1.00 33.12 ? 35  ALA C CA  1 
ATOM   2977 C  C   . ALA C  1 34  ? 38.811 28.286  -16.496 1.00 34.84 ? 35  ALA C C   1 
ATOM   2978 O  O   . ALA C  1 34  ? 39.201 27.875  -17.594 1.00 35.97 ? 35  ALA C O   1 
ATOM   2979 C  CB  . ALA C  1 34  ? 38.587 30.723  -15.979 1.00 28.16 ? 35  ALA C CB  1 
ATOM   2980 N  N   . TYR C  1 35  ? 39.235 27.755  -15.354 1.00 33.72 ? 36  TYR C N   1 
ATOM   2981 C  CA  . TYR C  1 35  ? 40.209 26.676  -15.369 1.00 32.70 ? 36  TYR C CA  1 
ATOM   2982 C  C   . TYR C  1 35  ? 39.574 25.340  -15.692 1.00 34.99 ? 36  TYR C C   1 
ATOM   2983 O  O   . TYR C  1 35  ? 40.282 24.433  -16.136 1.00 33.80 ? 36  TYR C O   1 
ATOM   2984 C  CB  . TYR C  1 35  ? 40.951 26.618  -14.034 1.00 30.86 ? 36  TYR C CB  1 
ATOM   2985 C  CG  . TYR C  1 35  ? 42.029 27.661  -14.014 1.00 33.04 ? 36  TYR C CG  1 
ATOM   2986 C  CD1 . TYR C  1 35  ? 43.243 27.447  -14.661 1.00 39.14 ? 36  TYR C CD1 1 
ATOM   2987 C  CD2 . TYR C  1 35  ? 41.807 28.894  -13.428 1.00 32.71 ? 36  TYR C CD2 1 
ATOM   2988 C  CE1 . TYR C  1 35  ? 44.225 28.431  -14.687 1.00 38.89 ? 36  TYR C CE1 1 
ATOM   2989 C  CE2 . TYR C  1 35  ? 42.772 29.875  -13.442 1.00 41.01 ? 36  TYR C CE2 1 
ATOM   2990 C  CZ  . TYR C  1 35  ? 43.978 29.640  -14.074 1.00 43.54 ? 36  TYR C CZ  1 
ATOM   2991 O  OH  . TYR C  1 35  ? 44.922 30.631  -14.081 1.00 47.26 ? 36  TYR C OH  1 
ATOM   2992 N  N   . TYR C  1 36  ? 38.260 25.204  -15.493 1.00 28.30 ? 37  TYR C N   1 
ATOM   2993 C  CA  . TYR C  1 36  ? 37.583 24.014  -15.981 1.00 31.31 ? 37  TYR C CA  1 
ATOM   2994 C  C   . TYR C  1 36  ? 37.680 23.923  -17.501 1.00 33.67 ? 37  TYR C C   1 
ATOM   2995 O  O   . TYR C  1 36  ? 37.962 22.855  -18.051 1.00 30.45 ? 37  TYR C O   1 
ATOM   2996 C  CB  . TYR C  1 36  ? 36.130 24.030  -15.533 1.00 29.70 ? 37  TYR C CB  1 
ATOM   2997 C  CG  . TYR C  1 36  ? 35.271 22.983  -16.207 1.00 36.40 ? 37  TYR C CG  1 
ATOM   2998 C  CD1 . TYR C  1 36  ? 35.287 21.661  -15.778 1.00 35.46 ? 37  TYR C CD1 1 
ATOM   2999 C  CD2 . TYR C  1 36  ? 34.437 23.321  -17.264 1.00 32.50 ? 37  TYR C CD2 1 
ATOM   3000 C  CE1 . TYR C  1 36  ? 34.493 20.697  -16.389 1.00 41.10 ? 37  TYR C CE1 1 
ATOM   3001 C  CE2 . TYR C  1 36  ? 33.643 22.372  -17.877 1.00 39.06 ? 37  TYR C CE2 1 
ATOM   3002 C  CZ  . TYR C  1 36  ? 33.677 21.061  -17.436 1.00 43.43 ? 37  TYR C CZ  1 
ATOM   3003 O  OH  . TYR C  1 36  ? 32.887 20.124  -18.046 1.00 47.18 ? 37  TYR C OH  1 
ATOM   3004 N  N   . PHE C  1 37  ? 37.461 25.043  -18.194 1.00 33.19 ? 38  PHE C N   1 
ATOM   3005 C  CA  . PHE C  1 37  ? 37.467 25.069  -19.649 1.00 32.71 ? 38  PHE C CA  1 
ATOM   3006 C  C   . PHE C  1 37  ? 38.872 25.010  -20.243 1.00 36.33 ? 38  PHE C C   1 
ATOM   3007 O  O   . PHE C  1 37  ? 39.010 24.880  -21.468 1.00 33.88 ? 38  PHE C O   1 
ATOM   3008 C  CB  . PHE C  1 37  ? 36.709 26.314  -20.134 1.00 32.37 ? 38  PHE C CB  1 
ATOM   3009 C  CG  . PHE C  1 37  ? 35.222 26.187  -19.993 1.00 33.04 ? 38  PHE C CG  1 
ATOM   3010 C  CD1 . PHE C  1 37  ? 34.532 25.224  -20.716 1.00 30.56 ? 38  PHE C CD1 1 
ATOM   3011 C  CD2 . PHE C  1 37  ? 34.517 26.997  -19.116 1.00 33.14 ? 38  PHE C CD2 1 
ATOM   3012 C  CE1 . PHE C  1 37  ? 33.154 25.072  -20.581 1.00 34.86 ? 38  PHE C CE1 1 
ATOM   3013 C  CE2 . PHE C  1 37  ? 33.140 26.862  -18.975 1.00 35.04 ? 38  PHE C CE2 1 
ATOM   3014 C  CZ  . PHE C  1 37  ? 32.454 25.897  -19.709 1.00 37.88 ? 38  PHE C CZ  1 
ATOM   3015 N  N   . GLU C  1 38  ? 39.910 25.065  -19.412 1.00 35.94 ? 39  GLU C N   1 
ATOM   3016 C  CA  . GLU C  1 38  ? 41.284 24.839  -19.851 1.00 36.07 ? 39  GLU C CA  1 
ATOM   3017 C  C   . GLU C  1 38  ? 41.754 23.404  -19.631 1.00 34.26 ? 39  GLU C C   1 
ATOM   3018 O  O   . GLU C  1 38  ? 42.905 23.088  -19.945 1.00 37.80 ? 39  GLU C O   1 
ATOM   3019 C  CB  . GLU C  1 38  ? 42.211 25.804  -19.121 1.00 38.29 ? 39  GLU C CB  1 
ATOM   3020 C  CG  . GLU C  1 38  ? 42.264 27.174  -19.754 1.00 47.75 ? 39  GLU C CG  1 
ATOM   3021 C  CD  . GLU C  1 38  ? 43.294 28.084  -19.099 1.00 59.26 ? 39  GLU C CD  1 
ATOM   3022 O  OE1 . GLU C  1 38  ? 44.418 27.612  -18.800 1.00 54.00 ? 39  GLU C OE1 1 
ATOM   3023 O  OE2 . GLU C  1 38  ? 42.976 29.284  -18.910 1.00 63.99 ? 39  GLU C OE2 1 
ATOM   3024 N  N   . ARG C  1 39  ? 40.915 22.548  -19.052 1.00 34.84 ? 40  ARG C N   1 
ATOM   3025 C  CA  . ARG C  1 39  ? 41.256 21.138  -18.921 1.00 32.58 ? 40  ARG C CA  1 
ATOM   3026 C  C   . ARG C  1 39  ? 41.467 20.517  -20.298 1.00 37.81 ? 40  ARG C C   1 
ATOM   3027 O  O   . ARG C  1 39  ? 40.799 20.867  -21.281 1.00 33.48 ? 40  ARG C O   1 
ATOM   3028 C  CB  . ARG C  1 39  ? 40.150 20.384  -18.178 1.00 32.30 ? 40  ARG C CB  1 
ATOM   3029 C  CG  . ARG C  1 39  ? 40.122 20.655  -16.681 1.00 36.24 ? 40  ARG C CG  1 
ATOM   3030 C  CD  . ARG C  1 39  ? 38.848 20.130  -16.012 1.00 39.14 ? 40  ARG C CD  1 
ATOM   3031 N  NE  . ARG C  1 39  ? 38.383 18.832  -16.493 1.00 40.98 ? 40  ARG C NE  1 
ATOM   3032 C  CZ  . ARG C  1 39  ? 37.533 18.047  -15.834 1.00 52.62 ? 40  ARG C CZ  1 
ATOM   3033 N  NH1 . ARG C  1 39  ? 37.066 18.380  -14.636 1.00 50.18 ? 40  ARG C NH1 1 
ATOM   3034 N  NH2 . ARG C  1 39  ? 37.128 16.905  -16.395 1.00 48.28 ? 40  ARG C NH2 1 
ATOM   3035 N  N   . ASP C  1 40  ? 42.407 19.574  -20.355 1.00 38.03 ? 41  ASP C N   1 
ATOM   3036 C  CA  . ASP C  1 40  ? 42.758 18.948  -21.622 1.00 37.20 ? 41  ASP C CA  1 
ATOM   3037 C  C   . ASP C  1 40  ? 41.572 18.213  -22.232 1.00 38.45 ? 41  ASP C C   1 
ATOM   3038 O  O   . ASP C  1 40  ? 41.495 18.092  -23.459 1.00 37.58 ? 41  ASP C O   1 
ATOM   3039 C  CB  . ASP C  1 40  ? 43.945 17.996  -21.424 1.00 39.70 ? 41  ASP C CB  1 
ATOM   3040 C  CG  . ASP C  1 40  ? 43.545 16.690  -20.731 1.00 42.84 ? 41  ASP C CG  1 
ATOM   3041 O  OD1 . ASP C  1 40  ? 43.424 16.665  -19.477 1.00 42.95 ? 41  ASP C OD1 1 
ATOM   3042 O  OD2 . ASP C  1 40  ? 43.337 15.686  -21.453 1.00 47.90 ? 41  ASP C OD2 1 
ATOM   3043 N  N   . ASP C  1 41  ? 40.636 17.728  -21.408 1.00 34.15 ? 42  ASP C N   1 
ATOM   3044 C  CA  . ASP C  1 41  ? 39.468 17.012  -21.909 1.00 36.23 ? 42  ASP C CA  1 
ATOM   3045 C  C   . ASP C  1 41  ? 38.238 17.907  -22.037 1.00 36.23 ? 42  ASP C C   1 
ATOM   3046 O  O   . ASP C  1 41  ? 37.121 17.396  -22.193 1.00 33.75 ? 42  ASP C O   1 
ATOM   3047 C  CB  . ASP C  1 41  ? 39.156 15.791  -21.026 1.00 36.22 ? 42  ASP C CB  1 
ATOM   3048 C  CG  . ASP C  1 41  ? 38.855 16.157  -19.572 1.00 43.00 ? 42  ASP C CG  1 
ATOM   3049 O  OD1 . ASP C  1 41  ? 39.021 17.332  -19.193 1.00 41.54 ? 42  ASP C OD1 1 
ATOM   3050 O  OD2 . ASP C  1 41  ? 38.458 15.256  -18.796 1.00 44.93 ? 42  ASP C OD2 1 
ATOM   3051 N  N   . VAL C  1 42  ? 38.421 19.227  -21.975 1.00 35.13 ? 43  VAL C N   1 
ATOM   3052 C  CA  . VAL C  1 42  ? 37.363 20.184  -22.284 1.00 31.01 ? 43  VAL C CA  1 
ATOM   3053 C  C   . VAL C  1 42  ? 37.844 21.078  -23.427 1.00 32.66 ? 43  VAL C C   1 
ATOM   3054 O  O   . VAL C  1 42  ? 37.243 21.094  -24.505 1.00 33.35 ? 43  VAL C O   1 
ATOM   3055 C  CB  . VAL C  1 42  ? 36.965 20.991  -21.034 1.00 35.29 ? 43  VAL C CB  1 
ATOM   3056 C  CG1 . VAL C  1 42  ? 35.985 22.122  -21.403 1.00 33.36 ? 43  VAL C CG1 1 
ATOM   3057 C  CG2 . VAL C  1 42  ? 36.356 20.063  -19.991 1.00 28.43 ? 43  VAL C CG2 1 
ATOM   3058 N  N   . ALA C  1 43  ? 38.941 21.804  -23.207 1.00 33.04 ? 44  ALA C N   1 
ATOM   3059 C  CA  . ALA C  1 43  ? 39.661 22.540  -24.254 1.00 34.30 ? 44  ALA C CA  1 
ATOM   3060 C  C   . ALA C  1 43  ? 38.732 23.490  -25.016 1.00 35.58 ? 44  ALA C C   1 
ATOM   3061 O  O   . ALA C  1 43  ? 38.487 23.351  -26.220 1.00 35.11 ? 44  ALA C O   1 
ATOM   3062 C  CB  . ALA C  1 43  ? 40.372 21.581  -25.219 1.00 29.75 ? 44  ALA C CB  1 
ATOM   3063 N  N   . LEU C  1 44  ? 38.218 24.467  -24.278 1.00 32.32 ? 45  LEU C N   1 
ATOM   3064 C  CA  . LEU C  1 44  ? 37.370 25.529  -24.808 1.00 36.12 ? 45  LEU C CA  1 
ATOM   3065 C  C   . LEU C  1 44  ? 38.016 26.864  -24.449 1.00 36.18 ? 45  LEU C C   1 
ATOM   3066 O  O   . LEU C  1 44  ? 37.561 27.556  -23.530 1.00 37.34 ? 45  LEU C O   1 
ATOM   3067 C  CB  . LEU C  1 44  ? 35.956 25.418  -24.239 1.00 34.91 ? 45  LEU C CB  1 
ATOM   3068 C  CG  . LEU C  1 44  ? 35.130 24.306  -24.897 1.00 35.36 ? 45  LEU C CG  1 
ATOM   3069 C  CD1 . LEU C  1 44  ? 33.821 24.060  -24.140 1.00 35.55 ? 45  LEU C CD1 1 
ATOM   3070 C  CD2 . LEU C  1 44  ? 34.857 24.656  -26.361 1.00 36.25 ? 45  LEU C CD2 1 
ATOM   3071 N  N   . PRO C  1 45  ? 39.084 27.251  -25.155 1.00 40.63 ? 46  PRO C N   1 
ATOM   3072 C  CA  . PRO C  1 45  ? 39.860 28.438  -24.734 1.00 41.35 ? 46  PRO C CA  1 
ATOM   3073 C  C   . PRO C  1 45  ? 39.094 29.754  -24.791 1.00 38.16 ? 46  PRO C C   1 
ATOM   3074 O  O   . PRO C  1 45  ? 39.427 30.678  -24.036 1.00 40.27 ? 46  PRO C O   1 
ATOM   3075 C  CB  . PRO C  1 45  ? 41.044 28.439  -25.713 1.00 39.80 ? 46  PRO C CB  1 
ATOM   3076 C  CG  . PRO C  1 45  ? 40.535 27.688  -26.916 1.00 42.54 ? 46  PRO C CG  1 
ATOM   3077 C  CD  . PRO C  1 45  ? 39.655 26.611  -26.352 1.00 39.68 ? 46  PRO C CD  1 
ATOM   3078 N  N   . GLY C  1 46  ? 38.096 29.882  -25.665 1.00 36.87 ? 47  GLY C N   1 
ATOM   3079 C  CA  . GLY C  1 46  ? 37.310 31.108  -25.694 1.00 41.32 ? 47  GLY C CA  1 
ATOM   3080 C  C   . GLY C  1 46  ? 36.454 31.268  -24.450 1.00 39.59 ? 47  GLY C C   1 
ATOM   3081 O  O   . GLY C  1 46  ? 36.402 32.349  -23.846 1.00 34.56 ? 47  GLY C O   1 
ATOM   3082 N  N   . PHE C  1 47  ? 35.773 30.190  -24.052 1.00 35.68 ? 48  PHE C N   1 
ATOM   3083 C  CA  . PHE C  1 47  ? 35.038 30.194  -22.790 1.00 37.75 ? 48  PHE C CA  1 
ATOM   3084 C  C   . PHE C  1 47  ? 35.966 30.479  -21.616 1.00 35.18 ? 48  PHE C C   1 
ATOM   3085 O  O   . PHE C  1 47  ? 35.655 31.302  -20.751 1.00 31.38 ? 48  PHE C O   1 
ATOM   3086 C  CB  . PHE C  1 47  ? 34.327 28.863  -22.594 1.00 33.78 ? 48  PHE C CB  1 
ATOM   3087 C  CG  . PHE C  1 47  ? 33.075 28.732  -23.390 1.00 36.87 ? 48  PHE C CG  1 
ATOM   3088 C  CD1 . PHE C  1 47  ? 31.874 29.206  -22.893 1.00 36.63 ? 48  PHE C CD1 1 
ATOM   3089 C  CD2 . PHE C  1 47  ? 33.092 28.129  -24.636 1.00 40.27 ? 48  PHE C CD2 1 
ATOM   3090 C  CE1 . PHE C  1 47  ? 30.707 29.077  -23.618 1.00 38.58 ? 48  PHE C CE1 1 
ATOM   3091 C  CE2 . PHE C  1 47  ? 31.928 28.001  -25.373 1.00 38.86 ? 48  PHE C CE2 1 
ATOM   3092 C  CZ  . PHE C  1 47  ? 30.726 28.484  -24.857 1.00 38.79 ? 48  PHE C CZ  1 
ATOM   3093 N  N   . ALA C  1 48  ? 37.126 29.822  -21.585 1.00 36.95 ? 49  ALA C N   1 
ATOM   3094 C  CA  . ALA C  1 48  ? 38.064 30.033  -20.488 1.00 37.18 ? 49  ALA C CA  1 
ATOM   3095 C  C   . ALA C  1 48  ? 38.471 31.502  -20.384 1.00 38.35 ? 49  ALA C C   1 
ATOM   3096 O  O   . ALA C  1 48  ? 38.483 32.081  -19.285 1.00 34.74 ? 49  ALA C O   1 
ATOM   3097 C  CB  . ALA C  1 48  ? 39.286 29.134  -20.671 1.00 34.60 ? 49  ALA C CB  1 
ATOM   3098 N  N   . LYS C  1 49  ? 38.792 32.131  -21.524 1.00 36.93 ? 50  LYS C N   1 
ATOM   3099 C  CA  . LYS C  1 49  ? 39.172 33.543  -21.506 1.00 38.47 ? 50  LYS C CA  1 
ATOM   3100 C  C   . LYS C  1 49  ? 38.011 34.423  -21.057 1.00 38.78 ? 50  LYS C C   1 
ATOM   3101 O  O   . LYS C  1 49  ? 38.196 35.355  -20.263 1.00 39.54 ? 50  LYS C O   1 
ATOM   3102 C  CB  . LYS C  1 49  ? 39.655 33.981  -22.890 1.00 44.47 ? 50  LYS C CB  1 
ATOM   3103 C  CG  . LYS C  1 49  ? 40.102 35.437  -22.953 1.00 48.66 ? 50  LYS C CG  1 
ATOM   3104 C  CD  . LYS C  1 49  ? 40.515 35.847  -24.362 1.00 57.74 ? 50  LYS C CD  1 
ATOM   3105 C  CE  . LYS C  1 49  ? 39.290 36.222  -25.207 1.00 67.68 ? 50  LYS C CE  1 
ATOM   3106 N  NZ  . LYS C  1 49  ? 39.147 37.697  -25.485 1.00 72.62 ? 50  LYS C NZ  1 
ATOM   3107 N  N   . PHE C  1 50  ? 36.806 34.140  -21.554 1.00 35.05 ? 51  PHE C N   1 
ATOM   3108 C  CA  . PHE C  1 50  ? 35.635 34.909  -21.158 1.00 33.85 ? 51  PHE C CA  1 
ATOM   3109 C  C   . PHE C  1 50  ? 35.439 34.857  -19.649 1.00 35.04 ? 51  PHE C C   1 
ATOM   3110 O  O   . PHE C  1 50  ? 35.284 35.892  -18.995 1.00 33.22 ? 51  PHE C O   1 
ATOM   3111 C  CB  . PHE C  1 50  ? 34.398 34.387  -21.888 1.00 33.63 ? 51  PHE C CB  1 
ATOM   3112 C  CG  . PHE C  1 50  ? 33.131 35.097  -21.511 1.00 35.12 ? 51  PHE C CG  1 
ATOM   3113 C  CD1 . PHE C  1 50  ? 32.875 36.380  -21.979 1.00 37.81 ? 51  PHE C CD1 1 
ATOM   3114 C  CD2 . PHE C  1 50  ? 32.203 34.494  -20.675 1.00 34.16 ? 51  PHE C CD2 1 
ATOM   3115 C  CE1 . PHE C  1 50  ? 31.709 37.044  -21.628 1.00 41.03 ? 51  PHE C CE1 1 
ATOM   3116 C  CE2 . PHE C  1 50  ? 31.034 35.145  -20.319 1.00 35.45 ? 51  PHE C CE2 1 
ATOM   3117 C  CZ  . PHE C  1 50  ? 30.787 36.424  -20.788 1.00 42.01 ? 51  PHE C CZ  1 
ATOM   3118 N  N   . PHE C  1 51  ? 35.476 33.655  -19.071 1.00 30.71 ? 52  PHE C N   1 
ATOM   3119 C  CA  . PHE C  1 51  ? 35.251 33.543  -17.635 1.00 34.09 ? 52  PHE C CA  1 
ATOM   3120 C  C   . PHE C  1 51  ? 36.430 34.073  -16.826 1.00 30.65 ? 52  PHE C C   1 
ATOM   3121 O  O   . PHE C  1 51  ? 36.224 34.609  -15.738 1.00 34.96 ? 52  PHE C O   1 
ATOM   3122 C  CB  . PHE C  1 51  ? 34.913 32.095  -17.284 1.00 30.90 ? 52  PHE C CB  1 
ATOM   3123 C  CG  . PHE C  1 51  ? 33.559 31.677  -17.799 1.00 32.77 ? 52  PHE C CG  1 
ATOM   3124 C  CD1 . PHE C  1 51  ? 32.436 32.409  -17.470 1.00 32.31 ? 52  PHE C CD1 1 
ATOM   3125 C  CD2 . PHE C  1 51  ? 33.417 30.596  -18.653 1.00 31.46 ? 52  PHE C CD2 1 
ATOM   3126 C  CE1 . PHE C  1 51  ? 31.185 32.056  -17.959 1.00 36.36 ? 52  PHE C CE1 1 
ATOM   3127 C  CE2 . PHE C  1 51  ? 32.173 30.241  -19.143 1.00 34.28 ? 52  PHE C CE2 1 
ATOM   3128 C  CZ  . PHE C  1 51  ? 31.053 30.974  -18.792 1.00 31.36 ? 52  PHE C CZ  1 
ATOM   3129 N  N   . LYS C  1 52  ? 37.657 33.968  -17.340 1.00 29.28 ? 53  LYS C N   1 
ATOM   3130 C  CA  . LYS C  1 52  ? 38.780 34.667  -16.719 1.00 33.55 ? 53  LYS C CA  1 
ATOM   3131 C  C   . LYS C  1 52  ? 38.510 36.165  -16.599 1.00 37.46 ? 53  LYS C C   1 
ATOM   3132 O  O   . LYS C  1 52  ? 38.725 36.759  -15.534 1.00 34.24 ? 53  LYS C O   1 
ATOM   3133 C  CB  . LYS C  1 52  ? 40.061 34.432  -17.512 1.00 35.39 ? 53  LYS C CB  1 
ATOM   3134 C  CG  . LYS C  1 52  ? 41.310 34.641  -16.713 1.00 43.46 ? 53  LYS C CG  1 
ATOM   3135 C  CD  . LYS C  1 52  ? 41.783 33.315  -16.138 1.00 59.27 ? 53  LYS C CD  1 
ATOM   3136 C  CE  . LYS C  1 52  ? 42.767 32.594  -17.075 1.00 62.52 ? 53  LYS C CE  1 
ATOM   3137 N  NZ  . LYS C  1 52  ? 42.994 31.161  -16.659 1.00 53.90 ? 53  LYS C NZ  1 
ATOM   3138 N  N   . GLU C  1 53  ? 38.040 36.800  -17.687 1.00 36.17 ? 54  GLU C N   1 
ATOM   3139 C  CA  . GLU C  1 53  ? 37.755 38.235  -17.623 1.00 36.62 ? 54  GLU C CA  1 
ATOM   3140 C  C   . GLU C  1 53  ? 36.615 38.534  -16.652 1.00 35.94 ? 54  GLU C C   1 
ATOM   3141 O  O   . GLU C  1 53  ? 36.677 39.522  -15.910 1.00 34.70 ? 54  GLU C O   1 
ATOM   3142 C  CB  . GLU C  1 53  ? 37.450 38.803  -19.012 1.00 37.67 ? 54  GLU C CB  1 
ATOM   3143 C  CG  . GLU C  1 53  ? 38.683 38.916  -19.926 1.00 49.83 ? 54  GLU C CG  1 
ATOM   3144 C  CD  . GLU C  1 53  ? 38.357 38.936  -21.430 1.00 61.17 ? 54  GLU C CD  1 
ATOM   3145 O  OE1 . GLU C  1 53  ? 37.160 38.907  -21.810 1.00 63.61 ? 54  GLU C OE1 1 
ATOM   3146 O  OE2 . GLU C  1 53  ? 39.310 38.992  -22.240 1.00 61.86 ? 54  GLU C OE2 1 
ATOM   3147 N  N   . SER C  1 54  ? 35.578 37.683  -16.614 1.00 28.34 ? 55  SER C N   1 
ATOM   3148 C  CA  . SER C  1 54  ? 34.516 37.912  -15.635 1.00 35.74 ? 55  SER C CA  1 
ATOM   3149 C  C   . SER C  1 54  ? 35.022 37.758  -14.202 1.00 37.14 ? 55  SER C C   1 
ATOM   3150 O  O   . SER C  1 54  ? 34.564 38.479  -13.303 1.00 38.68 ? 55  SER C O   1 
ATOM   3151 C  CB  . SER C  1 54  ? 33.335 36.973  -15.873 1.00 35.74 ? 55  SER C CB  1 
ATOM   3152 O  OG  . SER C  1 54  ? 32.921 37.009  -17.222 1.00 37.47 ? 55  SER C OG  1 
ATOM   3153 N  N   . SER C  1 55  ? 35.966 36.839  -13.971 1.00 34.28 ? 56  SER C N   1 
ATOM   3154 C  CA  . SER C  1 55  ? 36.551 36.700  -12.642 1.00 33.99 ? 56  SER C CA  1 
ATOM   3155 C  C   . SER C  1 55  ? 37.306 37.960  -12.236 1.00 36.13 ? 56  SER C C   1 
ATOM   3156 O  O   . SER C  1 55  ? 37.226 38.395  -11.079 1.00 36.92 ? 56  SER C O   1 
ATOM   3157 C  CB  . SER C  1 55  ? 37.471 35.483  -12.591 1.00 30.76 ? 56  SER C CB  1 
ATOM   3158 O  OG  . SER C  1 55  ? 38.078 35.380  -11.313 1.00 30.62 ? 56  SER C OG  1 
ATOM   3159 N  N   . ASP C  1 56  ? 38.029 38.568  -13.177 1.00 32.57 ? 57  ASP C N   1 
ATOM   3160 C  CA  . ASP C  1 56  ? 38.778 39.782  -12.868 1.00 35.76 ? 57  ASP C CA  1 
ATOM   3161 C  C   . ASP C  1 56  ? 37.838 40.949  -12.615 1.00 38.36 ? 57  ASP C C   1 
ATOM   3162 O  O   . ASP C  1 56  ? 38.050 41.740  -11.687 1.00 37.08 ? 57  ASP C O   1 
ATOM   3163 C  CB  . ASP C  1 56  ? 39.728 40.117  -14.019 1.00 38.01 ? 57  ASP C CB  1 
ATOM   3164 C  CG  . ASP C  1 56  ? 41.004 39.310  -13.969 1.00 47.79 ? 57  ASP C CG  1 
ATOM   3165 O  OD1 . ASP C  1 56  ? 41.335 38.794  -12.879 1.00 56.59 ? 57  ASP C OD1 1 
ATOM   3166 O  OD2 . ASP C  1 56  ? 41.659 39.155  -15.027 1.00 55.13 ? 57  ASP C OD2 1 
ATOM   3167 N  N   . CYS C  1 57  ? 36.799 41.072  -13.441 1.00 35.22 ? 58  CYS C N   1 
ATOM   3168 C  CA  . CYS C  1 57  ? 35.830 42.149  -13.276 1.00 42.74 ? 58  CYS C CA  1 
ATOM   3169 C  C   . CYS C  1 57  ? 35.175 42.108  -11.894 1.00 40.71 ? 58  CYS C C   1 
ATOM   3170 O  O   . CYS C  1 57  ? 35.063 43.137  -11.221 1.00 35.34 ? 58  CYS C O   1 
ATOM   3171 C  CB  . CYS C  1 57  ? 34.775 42.071  -14.383 1.00 34.83 ? 58  CYS C CB  1 
ATOM   3172 S  SG  . CYS C  1 57  ? 33.200 42.811  -13.886 1.00 64.71 ? 58  CYS C SG  1 
ATOM   3173 N  N   . CYS C  1 58  ? 34.735 40.922  -11.450 1.00 38.39 ? 59  CYS C N   1 
ATOM   3174 C  CA  . CYS C  1 58  ? 34.081 40.837  -10.147 1.00 37.16 ? 59  CYS C CA  1 
ATOM   3175 C  C   . CYS C  1 58  ? 35.041 41.171  -9.006  1.00 39.23 ? 59  CYS C C   1 
ATOM   3176 O  O   . CYS C  1 58  ? 34.615 41.705  -7.968  1.00 36.56 ? 59  CYS C O   1 
ATOM   3177 C  CB  . CYS C  1 58  ? 33.475 39.444  -9.941  1.00 35.16 ? 59  CYS C CB  1 
ATOM   3178 S  SG  . CYS C  1 58  ? 31.860 39.187  -10.740 1.00 43.16 ? 59  CYS C SG  1 
ATOM   3179 N  N   . ARG C  1 59  ? 36.334 40.879  -9.172  1.00 34.80 ? 60  ARG C N   1 
ATOM   3180 C  CA  . ARG C  1 59  ? 37.278 41.234  -8.121  1.00 38.50 ? 60  ARG C CA  1 
ATOM   3181 C  C   . ARG C  1 59  ? 37.479 42.747  -8.048  1.00 39.05 ? 60  ARG C C   1 
ATOM   3182 O  O   . ARG C  1 59  ? 37.594 43.303  -6.950  1.00 38.45 ? 60  ARG C O   1 
ATOM   3183 C  CB  . ARG C  1 59  ? 38.609 40.509  -8.316  1.00 34.77 ? 60  ARG C CB  1 
ATOM   3184 C  CG  . ARG C  1 59  ? 39.564 40.762  -7.176  1.00 40.49 ? 60  ARG C CG  1 
ATOM   3185 C  CD  . ARG C  1 59  ? 40.855 39.992  -7.334  1.00 51.56 ? 60  ARG C CD  1 
ATOM   3186 N  NE  . ARG C  1 59  ? 41.545 40.350  -8.567  1.00 52.86 ? 60  ARG C NE  1 
ATOM   3187 C  CZ  . ARG C  1 59  ? 41.658 39.539  -9.609  1.00 49.88 ? 60  ARG C CZ  1 
ATOM   3188 N  NH1 . ARG C  1 59  ? 41.144 38.318  -9.588  1.00 49.26 ? 60  ARG C NH1 1 
ATOM   3189 N  NH2 . ARG C  1 59  ? 42.294 39.965  -10.698 1.00 50.09 ? 60  ARG C NH2 1 
ATOM   3190 N  N   . GLU C  1 60  ? 37.522 43.434  -9.197  1.00 36.19 ? 61  GLU C N   1 
ATOM   3191 C  CA  . GLU C  1 60  ? 37.522 44.896  -9.169  1.00 39.53 ? 61  GLU C CA  1 
ATOM   3192 C  C   . GLU C  1 60  ? 36.257 45.431  -8.502  1.00 37.88 ? 61  GLU C C   1 
ATOM   3193 O  O   . GLU C  1 60  ? 36.329 46.359  -7.691  1.00 40.57 ? 61  GLU C O   1 
ATOM   3194 C  CB  . GLU C  1 60  ? 37.645 45.493  -10.576 1.00 35.44 ? 61  GLU C CB  1 
ATOM   3195 C  CG  . GLU C  1 60  ? 38.685 44.876  -11.524 1.00 51.94 ? 61  GLU C CG  1 
ATOM   3196 C  CD  . GLU C  1 60  ? 39.965 44.380  -10.840 1.00 61.63 ? 61  GLU C CD  1 
ATOM   3197 O  OE1 . GLU C  1 60  ? 40.572 45.127  -10.029 1.00 62.91 ? 61  GLU C OE1 1 
ATOM   3198 O  OE2 . GLU C  1 60  ? 40.380 43.231  -11.146 1.00 64.20 ? 61  GLU C OE2 1 
ATOM   3199 N  N   . HIS C  1 61  ? 35.087 44.869  -8.846  1.00 32.02 ? 62  HIS C N   1 
ATOM   3200 C  CA  . HIS C  1 61  ? 33.844 45.256  -8.185  1.00 35.63 ? 62  HIS C CA  1 
ATOM   3201 C  C   . HIS C  1 61  ? 33.985 45.201  -6.671  1.00 33.41 ? 62  HIS C C   1 
ATOM   3202 O  O   . HIS C  1 61  ? 33.516 46.098  -5.963  1.00 31.66 ? 62  HIS C O   1 
ATOM   3203 C  CB  . HIS C  1 61  ? 32.688 44.345  -8.619  1.00 38.26 ? 62  HIS C CB  1 
ATOM   3204 C  CG  . HIS C  1 61  ? 32.190 44.606  -10.003 1.00 48.33 ? 62  HIS C CG  1 
ATOM   3205 N  ND1 . HIS C  1 61  ? 32.464 45.777  -10.679 1.00 49.53 ? 62  HIS C ND1 1 
ATOM   3206 C  CD2 . HIS C  1 61  ? 31.434 43.851  -10.838 1.00 41.63 ? 62  HIS C CD2 1 
ATOM   3207 C  CE1 . HIS C  1 61  ? 31.903 45.732  -11.874 1.00 53.93 ? 62  HIS C CE1 1 
ATOM   3208 N  NE2 . HIS C  1 61  ? 31.276 44.574  -11.995 1.00 55.13 ? 62  HIS C NE2 1 
ATOM   3209 N  N   . ALA C  1 62  ? 34.620 44.143  -6.152  1.00 31.33 ? 63  ALA C N   1 
ATOM   3210 C  CA  . ALA C  1 62  ? 34.745 44.015  -4.705  1.00 34.30 ? 63  ALA C CA  1 
ATOM   3211 C  C   . ALA C  1 62  ? 35.706 45.055  -4.152  1.00 32.45 ? 63  ALA C C   1 
ATOM   3212 O  O   . ALA C  1 62  ? 35.461 45.626  -3.084  1.00 30.54 ? 63  ALA C O   1 
ATOM   3213 C  CB  . ALA C  1 62  ? 35.191 42.600  -4.326  1.00 30.17 ? 63  ALA C CB  1 
ATOM   3214 N  N   . GLN C  1 63  ? 36.785 45.344  -4.884  1.00 33.13 ? 64  GLN C N   1 
ATOM   3215 C  CA  . GLN C  1 63  ? 37.770 46.301  -4.390  1.00 35.34 ? 64  GLN C CA  1 
ATOM   3216 C  C   . GLN C  1 63  ? 37.237 47.723  -4.424  1.00 33.05 ? 64  GLN C C   1 
ATOM   3217 O  O   . GLN C  1 63  ? 37.583 48.531  -3.556  1.00 32.85 ? 64  GLN C O   1 
ATOM   3218 C  CB  . GLN C  1 63  ? 39.061 46.191  -5.198  1.00 36.30 ? 64  GLN C CB  1 
ATOM   3219 C  CG  . GLN C  1 63  ? 39.667 44.799  -5.143  1.00 38.74 ? 64  GLN C CG  1 
ATOM   3220 C  CD  . GLN C  1 63  ? 41.170 44.803  -5.295  1.00 50.23 ? 64  GLN C CD  1 
ATOM   3221 O  OE1 . GLN C  1 63  ? 41.850 45.763  -4.914  1.00 58.36 ? 64  GLN C OE1 1 
ATOM   3222 N  NE2 . GLN C  1 63  ? 41.704 43.722  -5.845  1.00 49.29 ? 64  GLN C NE2 1 
ATOM   3223 N  N   . THR C  1 64  ? 36.403 48.049  -5.417  1.00 32.52 ? 65  THR C N   1 
ATOM   3224 C  CA  . THR C  1 64  ? 35.783 49.368  -5.445  1.00 31.24 ? 65  THR C CA  1 
ATOM   3225 C  C   . THR C  1 64  ? 34.870 49.555  -4.235  1.00 28.03 ? 65  THR C C   1 
ATOM   3226 O  O   . THR C  1 64  ? 34.799 50.649  -3.667  1.00 29.47 ? 65  THR C O   1 
ATOM   3227 C  CB  . THR C  1 64  ? 35.013 49.555  -6.750  1.00 31.25 ? 65  THR C CB  1 
ATOM   3228 O  OG1 . THR C  1 64  ? 35.908 49.400  -7.852  1.00 35.68 ? 65  THR C OG1 1 
ATOM   3229 C  CG2 . THR C  1 64  ? 34.411 50.947  -6.813  1.00 37.79 ? 65  THR C CG2 1 
ATOM   3230 N  N   . PHE C  1 65  ? 34.197 48.482  -3.804  1.00 31.30 ? 66  PHE C N   1 
ATOM   3231 C  CA  . PHE C  1 65  ? 33.385 48.555  -2.591  1.00 30.29 ? 66  PHE C CA  1 
ATOM   3232 C  C   . PHE C  1 65  ? 34.247 48.722  -1.345  1.00 29.85 ? 66  PHE C C   1 
ATOM   3233 O  O   . PHE C  1 65  ? 33.865 49.450  -0.426  1.00 30.17 ? 66  PHE C O   1 
ATOM   3234 C  CB  . PHE C  1 65  ? 32.512 47.317  -2.464  1.00 29.58 ? 66  PHE C CB  1 
ATOM   3235 C  CG  . PHE C  1 65  ? 31.186 47.432  -3.151  1.00 34.88 ? 66  PHE C CG  1 
ATOM   3236 C  CD1 . PHE C  1 65  ? 30.361 48.518  -2.924  1.00 34.91 ? 66  PHE C CD1 1 
ATOM   3237 C  CD2 . PHE C  1 65  ? 30.759 46.441  -4.020  1.00 35.58 ? 66  PHE C CD2 1 
ATOM   3238 C  CE1 . PHE C  1 65  ? 29.132 48.612  -3.553  1.00 40.08 ? 66  PHE C CE1 1 
ATOM   3239 C  CE2 . PHE C  1 65  ? 29.537 46.536  -4.653  1.00 37.17 ? 66  PHE C CE2 1 
ATOM   3240 C  CZ  . PHE C  1 65  ? 28.720 47.620  -4.413  1.00 39.91 ? 66  PHE C CZ  1 
ATOM   3241 N  N   . MET C  1 66  ? 35.414 48.067  -1.284  1.00 29.41 ? 67  MET C N   1 
ATOM   3242 C  CA  . MET C  1 66  ? 36.240 48.225  -0.089  1.00 31.88 ? 67  MET C CA  1 
ATOM   3243 C  C   . MET C  1 66  ? 36.780 49.644  0.005   1.00 33.87 ? 67  MET C C   1 
ATOM   3244 O  O   . MET C  1 66  ? 36.787 50.233  1.092   1.00 28.67 ? 67  MET C O   1 
ATOM   3245 C  CB  . MET C  1 66  ? 37.393 47.219  -0.058  1.00 29.93 ? 67  MET C CB  1 
ATOM   3246 C  CG  . MET C  1 66  ? 36.918 45.773  -0.124  1.00 34.68 ? 67  MET C CG  1 
ATOM   3247 S  SD  . MET C  1 66  ? 38.187 44.535  -0.435  1.00 37.95 ? 67  MET C SD  1 
ATOM   3248 C  CE  . MET C  1 66  ? 39.278 44.817  0.949   1.00 40.11 ? 67  MET C CE  1 
ATOM   3249 N  N   . LYS C  1 67  ? 37.228 50.199  -1.135  1.00 33.53 ? 68  LYS C N   1 
ATOM   3250 C  CA  . LYS C  1 67  ? 37.623 51.603  -1.215  1.00 33.53 ? 68  LYS C CA  1 
ATOM   3251 C  C   . LYS C  1 67  ? 36.488 52.525  -0.804  1.00 32.14 ? 68  LYS C C   1 
ATOM   3252 O  O   . LYS C  1 67  ? 36.707 53.512  -0.098  1.00 31.08 ? 68  LYS C O   1 
ATOM   3253 C  CB  . LYS C  1 67  ? 38.053 51.950  -2.642  1.00 38.21 ? 68  LYS C CB  1 
ATOM   3254 C  CG  . LYS C  1 67  ? 39.524 51.830  -2.877  1.00 49.82 ? 68  LYS C CG  1 
ATOM   3255 C  CD  . LYS C  1 67  ? 39.882 52.027  -4.338  1.00 56.98 ? 68  LYS C CD  1 
ATOM   3256 C  CE  . LYS C  1 67  ? 40.035 50.660  -5.024  1.00 53.43 ? 68  LYS C CE  1 
ATOM   3257 N  NZ  . LYS C  1 67  ? 41.453 50.202  -5.082  1.00 59.82 ? 68  LYS C NZ  1 
ATOM   3258 N  N   . TYR C  1 68  ? 35.270 52.233  -1.267  1.00 30.83 ? 69  TYR C N   1 
ATOM   3259 C  CA  . TYR C  1 68  ? 34.118 53.049  -0.904  1.00 28.63 ? 69  TYR C CA  1 
ATOM   3260 C  C   . TYR C  1 68  ? 33.871 53.030  0.599   1.00 30.48 ? 69  TYR C C   1 
ATOM   3261 O  O   . TYR C  1 68  ? 33.631 54.079  1.204   1.00 33.25 ? 69  TYR C O   1 
ATOM   3262 C  CB  . TYR C  1 68  ? 32.877 52.557  -1.639  1.00 31.58 ? 69  TYR C CB  1 
ATOM   3263 C  CG  . TYR C  1 68  ? 31.725 53.501  -1.475  1.00 33.08 ? 69  TYR C CG  1 
ATOM   3264 C  CD1 . TYR C  1 68  ? 31.645 54.642  -2.247  1.00 34.17 ? 69  TYR C CD1 1 
ATOM   3265 C  CD2 . TYR C  1 68  ? 30.734 53.271  -0.528  1.00 32.19 ? 69  TYR C CD2 1 
ATOM   3266 C  CE1 . TYR C  1 68  ? 30.608 55.523  -2.099  1.00 35.65 ? 69  TYR C CE1 1 
ATOM   3267 C  CE2 . TYR C  1 68  ? 29.688 54.147  -0.370  1.00 31.53 ? 69  TYR C CE2 1 
ATOM   3268 C  CZ  . TYR C  1 68  ? 29.634 55.272  -1.163  1.00 34.36 ? 69  TYR C CZ  1 
ATOM   3269 O  OH  . TYR C  1 68  ? 28.608 56.168  -1.025  1.00 35.61 ? 69  TYR C OH  1 
ATOM   3270 N  N   . GLN C  1 69  ? 33.919 51.845  1.213   1.00 29.02 ? 70  GLN C N   1 
ATOM   3271 C  CA  . GLN C  1 69  ? 33.731 51.714  2.656   1.00 28.20 ? 70  GLN C CA  1 
ATOM   3272 C  C   . GLN C  1 69  ? 34.703 52.614  3.404   1.00 32.64 ? 70  GLN C C   1 
ATOM   3273 O  O   . GLN C  1 69  ? 34.307 53.362  4.305   1.00 32.50 ? 70  GLN C O   1 
ATOM   3274 C  CB  . GLN C  1 69  ? 33.915 50.248  3.067   1.00 30.20 ? 70  GLN C CB  1 
ATOM   3275 C  CG  . GLN C  1 69  ? 33.540 49.901  4.493   1.00 32.16 ? 70  GLN C CG  1 
ATOM   3276 C  CD  . GLN C  1 69  ? 32.038 49.691  4.640   1.00 38.68 ? 70  GLN C CD  1 
ATOM   3277 O  OE1 . GLN C  1 69  ? 31.291 50.655  4.758   1.00 40.20 ? 70  GLN C OE1 1 
ATOM   3278 N  NE2 . GLN C  1 69  ? 31.591 48.437  4.604   1.00 31.27 ? 70  GLN C NE2 1 
ATOM   3279 N  N   . ASN C  1 70  ? 35.982 52.581  3.017   1.00 30.97 ? 71  ASN C N   1 
ATOM   3280 C  CA  . ASN C  1 70  ? 36.967 53.448  3.657   1.00 33.26 ? 71  ASN C CA  1 
ATOM   3281 C  C   . ASN C  1 70  ? 36.699 54.925  3.361   1.00 33.97 ? 71  ASN C C   1 
ATOM   3282 O  O   . ASN C  1 70  ? 36.880 55.777  4.240   1.00 32.08 ? 71  ASN C O   1 
ATOM   3283 C  CB  . ASN C  1 70  ? 38.377 53.049  3.221   1.00 31.60 ? 71  ASN C CB  1 
ATOM   3284 C  CG  . ASN C  1 70  ? 38.924 51.898  4.051   1.00 35.85 ? 71  ASN C CG  1 
ATOM   3285 O  OD1 . ASN C  1 70  ? 38.381 51.580  5.120   1.00 37.18 ? 71  ASN C OD1 1 
ATOM   3286 N  ND2 . ASN C  1 70  ? 39.987 51.265  3.570   1.00 31.22 ? 71  ASN C ND2 1 
ATOM   3287 N  N   . LYS C  1 71  ? 36.260 55.245  2.136   1.00 31.20 ? 72  LYS C N   1 
ATOM   3288 C  CA  . LYS C  1 71  ? 35.962 56.633  1.774   1.00 32.85 ? 72  LYS C CA  1 
ATOM   3289 C  C   . LYS C  1 71  ? 34.894 57.234  2.683   1.00 33.80 ? 72  LYS C C   1 
ATOM   3290 O  O   . LYS C  1 71  ? 35.039 58.367  3.159   1.00 34.59 ? 72  LYS C O   1 
ATOM   3291 C  CB  . LYS C  1 71  ? 35.505 56.705  0.319   1.00 37.63 ? 72  LYS C CB  1 
ATOM   3292 C  CG  . LYS C  1 71  ? 35.992 57.902  -0.468  1.00 45.35 ? 72  LYS C CG  1 
ATOM   3293 C  CD  . LYS C  1 71  ? 35.388 57.824  -1.860  1.00 53.17 ? 72  LYS C CD  1 
ATOM   3294 C  CE  . LYS C  1 71  ? 36.378 57.216  -2.859  1.00 56.51 ? 72  LYS C CE  1 
ATOM   3295 N  NZ  . LYS C  1 71  ? 35.677 56.338  -3.858  1.00 56.91 ? 72  LYS C NZ  1 
ATOM   3296 N  N   . ARG C  1 72  ? 33.826 56.484  2.951   1.00 29.46 ? 73  ARG C N   1 
ATOM   3297 C  CA  . ARG C  1 72  ? 32.722 56.977  3.768   1.00 30.65 ? 73  ARG C CA  1 
ATOM   3298 C  C   . ARG C  1 72  ? 32.999 56.890  5.265   1.00 33.57 ? 73  ARG C C   1 
ATOM   3299 O  O   . ARG C  1 72  ? 32.224 57.438  6.060   1.00 35.69 ? 73  ARG C O   1 
ATOM   3300 C  CB  . ARG C  1 72  ? 31.446 56.198  3.442   1.00 29.33 ? 73  ARG C CB  1 
ATOM   3301 C  CG  . ARG C  1 72  ? 30.881 56.449  2.047   1.00 33.89 ? 73  ARG C CG  1 
ATOM   3302 C  CD  . ARG C  1 72  ? 30.620 57.938  1.767   1.00 31.69 ? 73  ARG C CD  1 
ATOM   3303 N  NE  . ARG C  1 72  ? 29.576 58.507  2.615   1.00 31.90 ? 73  ARG C NE  1 
ATOM   3304 C  CZ  . ARG C  1 72  ? 28.271 58.290  2.475   1.00 32.10 ? 73  ARG C CZ  1 
ATOM   3305 N  NH1 . ARG C  1 72  ? 27.788 57.515  1.515   1.00 31.44 ? 73  ARG C NH1 1 
ATOM   3306 N  NH2 . ARG C  1 72  ? 27.428 58.854  3.329   1.00 34.02 ? 73  ARG C NH2 1 
ATOM   3307 N  N   . GLY C  1 73  ? 34.064 56.214  5.676   1.00 31.62 ? 74  GLY C N   1 
ATOM   3308 C  CA  . GLY C  1 73  ? 34.362 56.079  7.085   1.00 34.49 ? 74  GLY C CA  1 
ATOM   3309 C  C   . GLY C  1 73  ? 33.793 54.847  7.760   1.00 38.39 ? 74  GLY C C   1 
ATOM   3310 O  O   . GLY C  1 73  ? 33.784 54.793  8.992   1.00 39.83 ? 74  GLY C O   1 
ATOM   3311 N  N   . GLY C  1 74  ? 33.283 53.877  7.003   1.00 30.31 ? 75  GLY C N   1 
ATOM   3312 C  CA  . GLY C  1 74  ? 32.900 52.605  7.569   1.00 37.00 ? 75  GLY C CA  1 
ATOM   3313 C  C   . GLY C  1 74  ? 34.096 51.683  7.754   1.00 37.46 ? 75  GLY C C   1 
ATOM   3314 O  O   . GLY C  1 74  ? 35.247 52.015  7.463   1.00 38.88 ? 75  GLY C O   1 
ATOM   3315 N  N   . ARG C  1 75  ? 33.816 50.489  8.250   1.00 33.58 ? 76  ARG C N   1 
ATOM   3316 C  CA  . ARG C  1 75  ? 34.867 49.515  8.502   1.00 37.57 ? 76  ARG C CA  1 
ATOM   3317 C  C   . ARG C  1 75  ? 34.626 48.281  7.655   1.00 34.84 ? 76  ARG C C   1 
ATOM   3318 O  O   . ARG C  1 75  ? 33.520 47.730  7.665   1.00 33.55 ? 76  ARG C O   1 
ATOM   3319 C  CB  . ARG C  1 75  ? 34.943 49.130  9.980   1.00 39.65 ? 76  ARG C CB  1 
ATOM   3320 C  CG  . ARG C  1 75  ? 36.277 48.458  10.326  1.00 51.51 ? 76  ARG C CG  1 
ATOM   3321 C  CD  . ARG C  1 75  ? 36.310 47.903  11.744  1.00 58.31 ? 76  ARG C CD  1 
ATOM   3322 N  NE  . ARG C  1 75  ? 36.902 48.825  12.715  1.00 65.03 ? 76  ARG C NE  1 
ATOM   3323 C  CZ  . ARG C  1 75  ? 38.124 49.349  12.656  1.00 65.65 ? 76  ARG C CZ  1 
ATOM   3324 N  NH1 . ARG C  1 75  ? 38.971 49.064  11.668  1.00 61.20 ? 76  ARG C NH1 1 
ATOM   3325 N  NH2 . ARG C  1 75  ? 38.517 50.171  13.624  1.00 68.38 ? 76  ARG C NH2 1 
ATOM   3326 N  N   . ILE C  1 76  ? 35.663 47.863  6.921   1.00 35.53 ? 77  ILE C N   1 
ATOM   3327 C  CA  . ILE C  1 76  ? 35.603 46.645  6.118   1.00 34.64 ? 77  ILE C CA  1 
ATOM   3328 C  C   . ILE C  1 76  ? 35.690 45.435  7.037   1.00 33.50 ? 77  ILE C C   1 
ATOM   3329 O  O   . ILE C  1 76  ? 36.570 45.356  7.903   1.00 39.27 ? 77  ILE C O   1 
ATOM   3330 C  CB  . ILE C  1 76  ? 36.743 46.620  5.089   1.00 32.59 ? 77  ILE C CB  1 
ATOM   3331 C  CG1 . ILE C  1 76  ? 36.616 47.756  4.070   1.00 30.46 ? 77  ILE C CG1 1 
ATOM   3332 C  CG2 . ILE C  1 76  ? 36.808 45.285  4.393   1.00 30.31 ? 77  ILE C CG2 1 
ATOM   3333 C  CD1 . ILE C  1 76  ? 37.957 48.112  3.475   1.00 29.45 ? 77  ILE C CD1 1 
ATOM   3334 N  N   . VAL C  1 77  ? 34.787 44.481  6.851   1.00 31.24 ? 78  VAL C N   1 
ATOM   3335 C  CA  . VAL C  1 77  ? 34.831 43.215  7.573   1.00 30.06 ? 78  VAL C CA  1 
ATOM   3336 C  C   . VAL C  1 77  ? 34.755 42.110  6.536   1.00 26.40 ? 78  VAL C C   1 
ATOM   3337 O  O   . VAL C  1 77  ? 33.704 41.904  5.915   1.00 30.53 ? 78  VAL C O   1 
ATOM   3338 C  CB  . VAL C  1 77  ? 33.704 43.083  8.610   1.00 35.48 ? 78  VAL C CB  1 
ATOM   3339 C  CG1 . VAL C  1 77  ? 33.811 41.755  9.345   1.00 31.10 ? 78  VAL C CG1 1 
ATOM   3340 C  CG2 . VAL C  1 77  ? 33.763 44.239  9.611   1.00 35.19 ? 78  VAL C CG2 1 
ATOM   3341 N  N   . LEU C  1 78  ? 35.866 41.415  6.329   1.00 31.71 ? 79  LEU C N   1 
ATOM   3342 C  CA  . LEU C  1 78  ? 35.908 40.318  5.368   1.00 31.56 ? 79  LEU C CA  1 
ATOM   3343 C  C   . LEU C  1 78  ? 35.335 39.046  5.974   1.00 28.85 ? 79  LEU C C   1 
ATOM   3344 O  O   . LEU C  1 78  ? 35.500 38.784  7.166   1.00 31.57 ? 79  LEU C O   1 
ATOM   3345 C  CB  . LEU C  1 78  ? 37.341 40.073  4.901   1.00 29.43 ? 79  LEU C CB  1 
ATOM   3346 C  CG  . LEU C  1 78  ? 37.867 41.354  4.251   1.00 33.42 ? 79  LEU C CG  1 
ATOM   3347 C  CD1 . LEU C  1 78  ? 39.351 41.251  3.954   1.00 35.78 ? 79  LEU C CD1 1 
ATOM   3348 C  CD2 . LEU C  1 78  ? 37.067 41.678  2.996   1.00 23.57 ? 79  LEU C CD2 1 
ATOM   3349 N  N   . GLN C  1 79  ? 34.654 38.261  5.142   1.00 27.68 ? 80  GLN C N   1 
ATOM   3350 C  CA  . GLN C  1 79  ? 34.106 36.975  5.534   1.00 27.12 ? 80  GLN C CA  1 
ATOM   3351 C  C   . GLN C  1 79  ? 34.697 35.892  4.651   1.00 29.59 ? 80  GLN C C   1 
ATOM   3352 O  O   . GLN C  1 79  ? 35.157 36.157  3.542   1.00 25.62 ? 80  GLN C O   1 
ATOM   3353 C  CB  . GLN C  1 79  ? 32.575 36.947  5.419   1.00 25.83 ? 80  GLN C CB  1 
ATOM   3354 C  CG  . GLN C  1 79  ? 31.847 37.968  6.307   1.00 27.29 ? 80  GLN C CG  1 
ATOM   3355 C  CD  . GLN C  1 79  ? 31.745 37.538  7.784   1.00 31.84 ? 80  GLN C CD  1 
ATOM   3356 O  OE1 . GLN C  1 79  ? 31.748 36.339  8.108   1.00 30.65 ? 80  GLN C OE1 1 
ATOM   3357 N  NE2 . GLN C  1 79  ? 31.639 38.527  8.681   1.00 28.58 ? 80  GLN C NE2 1 
ATOM   3358 N  N   . GLN C  1 80  ? 34.662 34.659  5.154   1.00 29.04 ? 81  GLN C N   1 
ATOM   3359 C  CA  . GLN C  1 80  ? 35.072 33.508  4.364   1.00 25.54 ? 81  GLN C CA  1 
ATOM   3360 C  C   . GLN C  1 80  ? 34.438 33.544  2.974   1.00 27.49 ? 81  GLN C C   1 
ATOM   3361 O  O   . GLN C  1 80  ? 33.265 33.892  2.813   1.00 26.09 ? 81  GLN C O   1 
ATOM   3362 C  CB  . GLN C  1 80  ? 34.678 32.228  5.099   1.00 26.16 ? 81  GLN C CB  1 
ATOM   3363 C  CG  . GLN C  1 80  ? 34.828 30.959  4.287   1.00 29.08 ? 81  GLN C CG  1 
ATOM   3364 C  CD  . GLN C  1 80  ? 34.969 29.746  5.181   1.00 35.50 ? 81  GLN C CD  1 
ATOM   3365 O  OE1 . GLN C  1 80  ? 36.021 29.542  5.804   1.00 34.10 ? 81  GLN C OE1 1 
ATOM   3366 N  NE2 . GLN C  1 80  ? 33.910 28.938  5.268   1.00 28.37 ? 81  GLN C NE2 1 
ATOM   3367 N  N   . ILE C  1 81  ? 35.228 33.212  1.959   1.00 29.01 ? 82  ILE C N   1 
ATOM   3368 C  CA  . ILE C  1 81  ? 34.703 33.031  0.609   1.00 27.77 ? 82  ILE C CA  1 
ATOM   3369 C  C   . ILE C  1 81  ? 34.402 31.549  0.419   1.00 33.21 ? 82  ILE C C   1 
ATOM   3370 O  O   . ILE C  1 81  ? 35.300 30.705  0.526   1.00 29.34 ? 82  ILE C O   1 
ATOM   3371 C  CB  . ILE C  1 81  ? 35.688 33.529  -0.454  1.00 26.83 ? 82  ILE C CB  1 
ATOM   3372 C  CG1 . ILE C  1 81  ? 36.121 34.963  -0.160  1.00 29.27 ? 82  ILE C CG1 1 
ATOM   3373 C  CG2 . ILE C  1 81  ? 35.053 33.439  -1.834  1.00 27.30 ? 82  ILE C CG2 1 
ATOM   3374 C  CD1 . ILE C  1 81  ? 37.347 35.377  -0.974  1.00 30.67 ? 82  ILE C CD1 1 
ATOM   3375 N  N   . ALA C  1 82  ? 33.141 31.240  0.138   1.00 30.11 ? 83  ALA C N   1 
ATOM   3376 C  CA  . ALA C  1 82  ? 32.694 29.864  0.007   1.00 31.42 ? 83  ALA C CA  1 
ATOM   3377 C  C   . ALA C  1 82  ? 33.279 29.227  -1.252  1.00 32.92 ? 83  ALA C C   1 
ATOM   3378 O  O   . ALA C  1 82  ? 33.524 29.900  -2.262  1.00 32.92 ? 83  ALA C O   1 
ATOM   3379 C  CB  . ALA C  1 82  ? 31.163 29.823  -0.041  1.00 28.05 ? 83  ALA C CB  1 
ATOM   3380 N  N   . ALA C  1 83  ? 33.512 27.918  -1.189  1.00 33.93 ? 84  ALA C N   1 
ATOM   3381 C  CA  . ALA C  1 83  ? 33.931 27.200  -2.387  1.00 35.42 ? 84  ALA C CA  1 
ATOM   3382 C  C   . ALA C  1 83  ? 32.795 27.222  -3.404  1.00 33.32 ? 84  ALA C C   1 
ATOM   3383 O  O   . ALA C  1 83  ? 31.625 27.184  -3.013  1.00 30.29 ? 84  ALA C O   1 
ATOM   3384 C  CB  . ALA C  1 83  ? 34.302 25.755  -2.051  1.00 37.02 ? 84  ALA C CB  1 
ATOM   3385 N  N   . PRO C  1 84  ? 33.089 27.307  -4.701  1.00 37.56 ? 85  PRO C N   1 
ATOM   3386 C  CA  . PRO C  1 84  ? 32.010 27.242  -5.700  1.00 38.68 ? 85  PRO C CA  1 
ATOM   3387 C  C   . PRO C  1 84  ? 31.146 26.004  -5.487  1.00 42.04 ? 85  PRO C C   1 
ATOM   3388 O  O   . PRO C  1 84  ? 31.632 24.944  -5.080  1.00 38.64 ? 85  PRO C O   1 
ATOM   3389 C  CB  . PRO C  1 84  ? 32.757 27.185  -7.036  1.00 35.19 ? 85  PRO C CB  1 
ATOM   3390 C  CG  . PRO C  1 84  ? 34.073 27.807  -6.748  1.00 37.81 ? 85  PRO C CG  1 
ATOM   3391 C  CD  . PRO C  1 84  ? 34.417 27.447  -5.326  1.00 32.26 ? 85  PRO C CD  1 
ATOM   3392 N  N   . SER C  1 85  ? 29.847 26.162  -5.749  1.00 45.19 ? 86  SER C N   1 
ATOM   3393 C  CA  . SER C  1 85  ? 28.886 25.087  -5.509  1.00 52.70 ? 86  SER C CA  1 
ATOM   3394 C  C   . SER C  1 85  ? 29.267 23.817  -6.267  1.00 48.86 ? 86  SER C C   1 
ATOM   3395 O  O   . SER C  1 85  ? 29.115 22.706  -5.746  1.00 54.84 ? 86  SER C O   1 
ATOM   3396 C  CB  . SER C  1 85  ? 27.483 25.549  -5.906  1.00 52.74 ? 86  SER C CB  1 
ATOM   3397 O  OG  . SER C  1 85  ? 27.528 26.329  -7.102  1.00 56.42 ? 86  SER C OG  1 
ATOM   3398 N  N   . MET C  1 86  ? 29.768 23.954  -7.492  1.00 50.36 ? 87  MET C N   1 
ATOM   3399 C  CA  . MET C  1 86  ? 30.311 22.799  -8.191  1.00 52.91 ? 87  MET C CA  1 
ATOM   3400 C  C   . MET C  1 86  ? 31.634 23.158  -8.841  1.00 51.93 ? 87  MET C C   1 
ATOM   3401 O  O   . MET C  1 86  ? 31.894 24.320  -9.155  1.00 52.88 ? 87  MET C O   1 
ATOM   3402 C  CB  . MET C  1 86  ? 29.352 22.259  -9.243  1.00 57.89 ? 87  MET C CB  1 
ATOM   3403 C  CG  . MET C  1 86  ? 28.960 23.269  -10.300 1.00 52.58 ? 87  MET C CG  1 
ATOM   3404 S  SD  . MET C  1 86  ? 27.480 22.696  -11.149 1.00 80.65 ? 87  MET C SD  1 
ATOM   3405 C  CE  . MET C  1 86  ? 27.545 20.927  -10.794 1.00 64.17 ? 87  MET C CE  1 
ATOM   3406 N  N   . GLN C  1 87  ? 32.474 22.135  -9.014  1.00 55.05 ? 88  GLN C N   1 
ATOM   3407 C  CA  . GLN C  1 87  ? 33.773 22.259  -9.660  1.00 53.99 ? 88  GLN C CA  1 
ATOM   3408 C  C   . GLN C  1 87  ? 33.715 21.952  -11.149 1.00 52.95 ? 88  GLN C C   1 
ATOM   3409 O  O   . GLN C  1 87  ? 34.662 22.282  -11.874 1.00 51.66 ? 88  GLN C O   1 
ATOM   3410 C  CB  . GLN C  1 87  ? 34.797 21.310  -9.011  1.00 53.35 ? 88  GLN C CB  1 
ATOM   3411 C  CG  . GLN C  1 87  ? 34.902 21.355  -7.460  1.00 55.81 ? 88  GLN C CG  1 
ATOM   3412 C  CD  . GLN C  1 87  ? 35.524 22.656  -6.922  1.00 50.05 ? 88  GLN C CD  1 
ATOM   3413 O  OE1 . GLN C  1 87  ? 36.508 23.167  -7.468  1.00 45.37 ? 88  GLN C OE1 1 
ATOM   3414 N  NE2 . GLN C  1 87  ? 34.949 23.185  -5.844  1.00 48.18 ? 88  GLN C NE2 1 
ATOM   3415 N  N   . GLU C  1 88  ? 32.631 21.332  -11.615 1.00 48.05 ? 89  GLU C N   1 
ATOM   3416 C  CA  . GLU C  1 88  ? 32.556 20.756  -12.954 1.00 50.10 ? 89  GLU C CA  1 
ATOM   3417 C  C   . GLU C  1 88  ? 31.327 21.304  -13.662 1.00 50.39 ? 89  GLU C C   1 
ATOM   3418 O  O   . GLU C  1 88  ? 30.195 20.936  -13.330 1.00 50.90 ? 89  GLU C O   1 
ATOM   3419 C  CB  . GLU C  1 88  ? 32.507 19.231  -12.889 1.00 54.97 ? 89  GLU C CB  1 
ATOM   3420 C  CG  . GLU C  1 88  ? 33.342 18.563  -13.960 1.00 61.10 ? 89  GLU C CG  1 
ATOM   3421 C  CD  . GLU C  1 88  ? 33.245 17.050  -13.920 1.00 74.47 ? 89  GLU C CD  1 
ATOM   3422 O  OE1 . GLU C  1 88  ? 33.225 16.425  -15.012 1.00 74.89 ? 89  GLU C OE1 1 
ATOM   3423 O  OE2 . GLU C  1 88  ? 33.196 16.495  -12.795 1.00 73.92 ? 89  GLU C OE2 1 
ATOM   3424 N  N   . TRP C  1 89  ? 31.549 22.141  -14.666 1.00 47.38 ? 90  TRP C N   1 
ATOM   3425 C  CA  . TRP C  1 89  ? 30.492 22.982  -15.200 1.00 46.00 ? 90  TRP C CA  1 
ATOM   3426 C  C   . TRP C  1 89  ? 29.799 22.424  -16.431 1.00 47.12 ? 90  TRP C C   1 
ATOM   3427 O  O   . TRP C  1 89  ? 28.878 23.069  -16.935 1.00 50.64 ? 90  TRP C O   1 
ATOM   3428 C  CB  . TRP C  1 89  ? 31.062 24.363  -15.491 1.00 43.13 ? 90  TRP C CB  1 
ATOM   3429 C  CG  . TRP C  1 89  ? 31.542 24.935  -14.241 1.00 42.14 ? 90  TRP C CG  1 
ATOM   3430 C  CD1 . TRP C  1 89  ? 32.816 24.911  -13.761 1.00 42.13 ? 90  TRP C CD1 1 
ATOM   3431 C  CD2 . TRP C  1 89  ? 30.741 25.568  -13.245 1.00 40.69 ? 90  TRP C CD2 1 
ATOM   3432 N  NE1 . TRP C  1 89  ? 32.862 25.524  -12.530 1.00 42.33 ? 90  TRP C NE1 1 
ATOM   3433 C  CE2 . TRP C  1 89  ? 31.599 25.936  -12.193 1.00 40.88 ? 90  TRP C CE2 1 
ATOM   3434 C  CE3 . TRP C  1 89  ? 29.378 25.874  -13.148 1.00 44.53 ? 90  TRP C CE3 1 
ATOM   3435 C  CZ2 . TRP C  1 89  ? 31.139 26.591  -11.050 1.00 44.98 ? 90  TRP C CZ2 1 
ATOM   3436 C  CZ3 . TRP C  1 89  ? 28.920 26.530  -12.013 1.00 42.06 ? 90  TRP C CZ3 1 
ATOM   3437 C  CH2 . TRP C  1 89  ? 29.799 26.878  -10.978 1.00 46.19 ? 90  TRP C CH2 1 
ATOM   3438 N  N   . GLY C  1 90  ? 30.196 21.254  -16.926 1.00 49.50 ? 91  GLY C N   1 
ATOM   3439 C  CA  . GLY C  1 90  ? 29.470 20.646  -18.041 1.00 45.14 ? 91  GLY C CA  1 
ATOM   3440 C  C   . GLY C  1 90  ? 29.833 21.283  -19.372 1.00 46.74 ? 91  GLY C C   1 
ATOM   3441 O  O   . GLY C  1 90  ? 31.008 21.487  -19.675 1.00 48.86 ? 91  GLY C O   1 
ATOM   3442 N  N   . THR C  1 91  ? 28.819 21.595  -20.176 1.00 43.38 ? 92  THR C N   1 
ATOM   3443 C  CA  . THR C  1 91  ? 29.032 22.185  -21.491 1.00 45.07 ? 92  THR C CA  1 
ATOM   3444 C  C   . THR C  1 91  ? 29.197 23.700  -21.388 1.00 41.92 ? 92  THR C C   1 
ATOM   3445 O  O   . THR C  1 91  ? 28.941 24.319  -20.352 1.00 40.34 ? 92  THR C O   1 
ATOM   3446 C  CB  . THR C  1 91  ? 27.862 21.878  -22.428 1.00 45.12 ? 92  THR C CB  1 
ATOM   3447 O  OG1 . THR C  1 91  ? 26.687 22.551  -21.949 1.00 45.15 ? 92  THR C OG1 1 
ATOM   3448 C  CG2 . THR C  1 91  ? 27.590 20.380  -22.486 1.00 44.38 ? 92  THR C CG2 1 
ATOM   3449 N  N   . GLY C  1 92  ? 29.624 24.304  -22.498 1.00 40.93 ? 93  GLY C N   1 
ATOM   3450 C  CA  . GLY C  1 92  ? 29.695 25.753  -22.550 1.00 41.12 ? 93  GLY C CA  1 
ATOM   3451 C  C   . GLY C  1 92  ? 28.352 26.406  -22.294 1.00 39.85 ? 93  GLY C C   1 
ATOM   3452 O  O   . GLY C  1 92  ? 28.282 27.452  -21.644 1.00 38.35 ? 93  GLY C O   1 
ATOM   3453 N  N   . LEU C  1 93  ? 27.271 25.786  -22.774 1.00 39.20 ? 94  LEU C N   1 
ATOM   3454 C  CA  . LEU C  1 93  ? 25.947 26.371  -22.618 1.00 40.55 ? 94  LEU C CA  1 
ATOM   3455 C  C   . LEU C  1 93  ? 25.516 26.369  -21.158 1.00 45.59 ? 94  LEU C C   1 
ATOM   3456 O  O   . LEU C  1 93  ? 25.007 27.384  -20.653 1.00 39.81 ? 94  LEU C O   1 
ATOM   3457 C  CB  . LEU C  1 93  ? 24.935 25.621  -23.484 1.00 37.87 ? 94  LEU C CB  1 
ATOM   3458 C  CG  . LEU C  1 93  ? 23.485 26.089  -23.319 1.00 41.49 ? 94  LEU C CG  1 
ATOM   3459 C  CD1 . LEU C  1 93  ? 23.361 27.568  -23.624 1.00 39.56 ? 94  LEU C CD1 1 
ATOM   3460 C  CD2 . LEU C  1 93  ? 22.559 25.291  -24.210 1.00 45.74 ? 94  LEU C CD2 1 
ATOM   3461 N  N   . GLU C  1 94  ? 25.733 25.247  -20.458 1.00 42.04 ? 95  GLU C N   1 
ATOM   3462 C  CA  . GLU C  1 94  ? 25.341 25.167  -19.055 1.00 43.55 ? 95  GLU C CA  1 
ATOM   3463 C  C   . GLU C  1 94  ? 26.116 26.153  -18.194 1.00 37.23 ? 95  GLU C C   1 
ATOM   3464 O  O   . GLU C  1 94  ? 25.568 26.667  -17.211 1.00 39.21 ? 95  GLU C O   1 
ATOM   3465 C  CB  . GLU C  1 94  ? 25.514 23.739  -18.530 1.00 44.92 ? 95  GLU C CB  1 
ATOM   3466 C  CG  . GLU C  1 94  ? 24.844 22.675  -19.411 1.00 49.12 ? 95  GLU C CG  1 
ATOM   3467 C  CD  . GLU C  1 94  ? 25.181 21.228  -19.006 1.00 61.62 ? 95  GLU C CD  1 
ATOM   3468 O  OE1 . GLU C  1 94  ? 24.241 20.460  -18.691 1.00 67.14 ? 95  GLU C OE1 1 
ATOM   3469 O  OE2 . GLU C  1 94  ? 26.380 20.849  -19.031 1.00 61.03 ? 95  GLU C OE2 1 
ATOM   3470 N  N   . ALA C  1 95  ? 27.373 26.452  -18.548 1.00 33.72 ? 96  ALA C N   1 
ATOM   3471 C  CA  . ALA C  1 95  ? 28.119 27.444  -17.782 1.00 33.64 ? 96  ALA C CA  1 
ATOM   3472 C  C   . ALA C  1 95  ? 27.568 28.851  -18.008 1.00 35.35 ? 96  ALA C C   1 
ATOM   3473 O  O   . ALA C  1 95  ? 27.476 29.646  -17.060 1.00 36.08 ? 96  ALA C O   1 
ATOM   3474 C  CB  . ALA C  1 95  ? 29.603 27.391  -18.132 1.00 35.54 ? 96  ALA C CB  1 
ATOM   3475 N  N   . LEU C  1 96  ? 27.208 29.180  -19.255 1.00 33.91 ? 97  LEU C N   1 
ATOM   3476 C  CA  . LEU C  1 96  ? 26.614 30.487  -19.537 1.00 37.42 ? 97  LEU C CA  1 
ATOM   3477 C  C   . LEU C  1 96  ? 25.290 30.667  -18.797 1.00 35.94 ? 97  LEU C C   1 
ATOM   3478 O  O   . LEU C  1 96  ? 25.006 31.754  -18.274 1.00 35.90 ? 97  LEU C O   1 
ATOM   3479 C  CB  . LEU C  1 96  ? 26.406 30.660  -21.043 1.00 33.27 ? 97  LEU C CB  1 
ATOM   3480 C  CG  . LEU C  1 96  ? 27.644 30.871  -21.916 1.00 36.93 ? 97  LEU C CG  1 
ATOM   3481 C  CD1 . LEU C  1 96  ? 27.221 31.110  -23.364 1.00 34.60 ? 97  LEU C CD1 1 
ATOM   3482 C  CD2 . LEU C  1 96  ? 28.457 32.025  -21.408 1.00 33.25 ? 97  LEU C CD2 1 
ATOM   3483 N  N   . GLN C  1 97  ? 24.460 29.616  -18.754 1.00 35.22 ? 98  GLN C N   1 
ATOM   3484 C  CA  . GLN C  1 97  ? 23.186 29.714  -18.047 1.00 36.73 ? 98  GLN C CA  1 
ATOM   3485 C  C   . GLN C  1 97  ? 23.406 29.919  -16.552 1.00 39.80 ? 98  GLN C C   1 
ATOM   3486 O  O   . GLN C  1 97  ? 22.642 30.639  -15.902 1.00 38.15 ? 98  GLN C O   1 
ATOM   3487 C  CB  . GLN C  1 97  ? 22.332 28.472  -18.305 1.00 39.89 ? 98  GLN C CB  1 
ATOM   3488 C  CG  . GLN C  1 97  ? 21.728 28.449  -19.713 1.00 47.17 ? 98  GLN C CG  1 
ATOM   3489 C  CD  . GLN C  1 97  ? 21.245 27.074  -20.138 1.00 50.04 ? 98  GLN C CD  1 
ATOM   3490 O  OE1 . GLN C  1 97  ? 21.804 26.049  -19.733 1.00 49.54 ? 98  GLN C OE1 1 
ATOM   3491 N  NE2 . GLN C  1 97  ? 20.194 27.046  -20.956 1.00 47.97 ? 98  GLN C NE2 1 
ATOM   3492 N  N   . ALA C  1 98  ? 24.456 29.311  -15.995 1.00 35.46 ? 99  ALA C N   1 
ATOM   3493 C  CA  . ALA C  1 98  ? 24.772 29.542  -14.590 1.00 35.97 ? 99  ALA C CA  1 
ATOM   3494 C  C   . ALA C  1 98  ? 25.276 30.963  -14.356 1.00 33.00 ? 99  ALA C C   1 
ATOM   3495 O  O   . ALA C  1 98  ? 24.878 31.603  -13.384 1.00 38.83 ? 99  ALA C O   1 
ATOM   3496 C  CB  . ALA C  1 98  ? 25.789 28.519  -14.102 1.00 30.23 ? 99  ALA C CB  1 
ATOM   3497 N  N   . ALA C  1 99  ? 26.131 31.486  -15.244 1.00 30.31 ? 100 ALA C N   1 
ATOM   3498 C  CA  . ALA C  1 99  ? 26.584 32.871  -15.107 1.00 31.52 ? 100 ALA C CA  1 
ATOM   3499 C  C   . ALA C  1 99  ? 25.432 33.867  -15.239 1.00 35.53 ? 100 ALA C C   1 
ATOM   3500 O  O   . ALA C  1 99  ? 25.388 34.874  -14.523 1.00 36.51 ? 100 ALA C O   1 
ATOM   3501 C  CB  . ALA C  1 99  ? 27.662 33.184  -16.142 1.00 31.45 ? 100 ALA C CB  1 
ATOM   3502 N  N   . LEU C  1 100 ? 24.507 33.628  -16.165 1.00 34.98 ? 101 LEU C N   1 
ATOM   3503 C  CA  . LEU C  1 100 ? 23.354 34.515  -16.285 1.00 34.73 ? 101 LEU C CA  1 
ATOM   3504 C  C   . LEU C  1 100 ? 22.577 34.568  -14.977 1.00 36.73 ? 101 LEU C C   1 
ATOM   3505 O  O   . LEU C  1 100 ? 22.217 35.648  -14.501 1.00 40.04 ? 101 LEU C O   1 
ATOM   3506 C  CB  . LEU C  1 100 ? 22.446 34.056  -17.427 1.00 32.56 ? 101 LEU C CB  1 
ATOM   3507 C  CG  . LEU C  1 100 ? 21.160 34.861  -17.575 1.00 38.00 ? 101 LEU C CG  1 
ATOM   3508 C  CD1 . LEU C  1 100 ? 21.477 36.204  -18.186 1.00 36.28 ? 101 LEU C CD1 1 
ATOM   3509 C  CD2 . LEU C  1 100 ? 20.160 34.125  -18.430 1.00 39.55 ? 101 LEU C CD2 1 
ATOM   3510 N  N   . ASP C  1 101 ? 22.324 33.407  -14.371 1.00 38.78 ? 102 ASP C N   1 
ATOM   3511 C  CA  . ASP C  1 101 ? 21.611 33.380  -13.098 1.00 39.79 ? 102 ASP C CA  1 
ATOM   3512 C  C   . ASP C  1 101 ? 22.435 33.997  -11.976 1.00 38.91 ? 102 ASP C C   1 
ATOM   3513 O  O   . ASP C  1 101 ? 21.870 34.602  -11.056 1.00 37.12 ? 102 ASP C O   1 
ATOM   3514 C  CB  . ASP C  1 101 ? 21.219 31.949  -12.753 1.00 42.33 ? 102 ASP C CB  1 
ATOM   3515 C  CG  . ASP C  1 101 ? 19.996 31.489  -13.540 1.00 65.63 ? 102 ASP C CG  1 
ATOM   3516 O  OD1 . ASP C  1 101 ? 19.161 32.356  -13.897 1.00 72.44 ? 102 ASP C OD1 1 
ATOM   3517 O  OD2 . ASP C  1 101 ? 19.874 30.271  -13.827 1.00 75.58 ? 102 ASP C OD2 1 
ATOM   3518 N  N   . LEU C  1 102 ? 23.761 33.886  -12.049 1.00 33.21 ? 103 LEU C N   1 
ATOM   3519 C  CA  . LEU C  1 102 ? 24.609 34.526  -11.047 1.00 38.19 ? 103 LEU C CA  1 
ATOM   3520 C  C   . LEU C  1 102 ? 24.576 36.050  -11.173 1.00 38.06 ? 103 LEU C C   1 
ATOM   3521 O  O   . LEU C  1 102 ? 24.500 36.755  -10.161 1.00 36.62 ? 103 LEU C O   1 
ATOM   3522 C  CB  . LEU C  1 102 ? 26.037 34.006  -11.175 1.00 36.00 ? 103 LEU C CB  1 
ATOM   3523 C  CG  . LEU C  1 102 ? 27.016 34.361  -10.061 1.00 43.74 ? 103 LEU C CG  1 
ATOM   3524 C  CD1 . LEU C  1 102 ? 26.460 33.939  -8.693  1.00 46.10 ? 103 LEU C CD1 1 
ATOM   3525 C  CD2 . LEU C  1 102 ? 28.357 33.675  -10.308 1.00 37.50 ? 103 LEU C CD2 1 
ATOM   3526 N  N   . GLU C  1 103 ? 24.632 36.579  -12.403 1.00 36.85 ? 104 GLU C N   1 
ATOM   3527 C  CA  . GLU C  1 103 ? 24.602 38.032  -12.585 1.00 39.76 ? 104 GLU C CA  1 
ATOM   3528 C  C   . GLU C  1 103 ? 23.228 38.619  -12.251 1.00 36.85 ? 104 GLU C C   1 
ATOM   3529 O  O   . GLU C  1 103 ? 23.142 39.728  -11.709 1.00 35.07 ? 104 GLU C O   1 
ATOM   3530 C  CB  . GLU C  1 103 ? 25.016 38.410  -14.015 1.00 36.70 ? 104 GLU C CB  1 
ATOM   3531 C  CG  . GLU C  1 103 ? 26.398 37.873  -14.471 1.00 41.62 ? 104 GLU C CG  1 
ATOM   3532 C  CD  . GLU C  1 103 ? 27.615 38.561  -13.801 1.00 51.58 ? 104 GLU C CD  1 
ATOM   3533 O  OE1 . GLU C  1 103 ? 28.713 38.555  -14.407 1.00 58.03 ? 104 GLU C OE1 1 
ATOM   3534 O  OE2 . GLU C  1 103 ? 27.498 39.097  -12.671 1.00 53.24 ? 104 GLU C OE2 1 
ATOM   3535 N  N   . LYS C  1 104 ? 22.148 37.890  -12.559 1.00 33.82 ? 105 LYS C N   1 
ATOM   3536 C  CA  . LYS C  1 104 ? 20.810 38.346  -12.189 1.00 37.50 ? 105 LYS C CA  1 
ATOM   3537 C  C   . LYS C  1 104 ? 20.644 38.398  -10.681 1.00 38.08 ? 105 LYS C C   1 
ATOM   3538 O  O   . LYS C  1 104 ? 19.983 39.297  -10.156 1.00 36.87 ? 105 LYS C O   1 
ATOM   3539 C  CB  . LYS C  1 104 ? 19.743 37.436  -12.788 1.00 32.93 ? 105 LYS C CB  1 
ATOM   3540 C  CG  . LYS C  1 104 ? 19.514 37.649  -14.265 1.00 39.71 ? 105 LYS C CG  1 
ATOM   3541 C  CD  . LYS C  1 104 ? 18.582 36.604  -14.799 1.00 41.52 ? 105 LYS C CD  1 
ATOM   3542 C  CE  . LYS C  1 104 ? 17.470 37.208  -15.611 1.00 45.27 ? 105 LYS C CE  1 
ATOM   3543 N  NZ  . LYS C  1 104 ? 16.775 36.096  -16.323 1.00 50.62 ? 105 LYS C NZ  1 
ATOM   3544 N  N   . GLN C  1 105 ? 21.234 37.433  -9.973  1.00 35.55 ? 106 GLN C N   1 
ATOM   3545 C  CA  . GLN C  1 105 ? 21.170 37.426  -8.517  1.00 38.84 ? 106 GLN C CA  1 
ATOM   3546 C  C   . GLN C  1 105 ? 22.005 38.558  -7.922  1.00 40.66 ? 106 GLN C C   1 
ATOM   3547 O  O   . GLN C  1 105 ? 21.565 39.227  -6.977  1.00 36.53 ? 106 GLN C O   1 
ATOM   3548 C  CB  . GLN C  1 105 ? 21.614 36.059  -7.995  1.00 39.87 ? 106 GLN C CB  1 
ATOM   3549 C  CG  . GLN C  1 105 ? 21.960 36.020  -6.524  1.00 50.41 ? 106 GLN C CG  1 
ATOM   3550 C  CD  . GLN C  1 105 ? 22.455 34.647  -6.075  1.00 64.09 ? 106 GLN C CD  1 
ATOM   3551 O  OE1 . GLN C  1 105 ? 22.737 33.769  -6.901  1.00 60.18 ? 106 GLN C OE1 1 
ATOM   3552 N  NE2 . GLN C  1 105 ? 22.548 34.454  -4.758  1.00 64.00 ? 106 GLN C NE2 1 
ATOM   3553 N  N   . VAL C  1 106 ? 23.200 38.809  -8.475  1.00 37.73 ? 107 VAL C N   1 
ATOM   3554 C  CA  . VAL C  1 106 ? 23.964 39.983  -8.058  1.00 37.27 ? 107 VAL C CA  1 
ATOM   3555 C  C   . VAL C  1 106 ? 23.175 41.257  -8.346  1.00 37.36 ? 107 VAL C C   1 
ATOM   3556 O  O   . VAL C  1 106 ? 23.139 42.180  -7.524  1.00 33.57 ? 107 VAL C O   1 
ATOM   3557 C  CB  . VAL C  1 106 ? 25.350 40.011  -8.734  1.00 40.92 ? 107 VAL C CB  1 
ATOM   3558 C  CG1 . VAL C  1 106 ? 26.013 41.375  -8.536  1.00 36.76 ? 107 VAL C CG1 1 
ATOM   3559 C  CG2 . VAL C  1 106 ? 26.248 38.910  -8.162  1.00 38.40 ? 107 VAL C CG2 1 
ATOM   3560 N  N   . ASN C  1 107 ? 22.504 41.315  -9.500  1.00 36.93 ? 108 ASN C N   1 
ATOM   3561 C  CA  . ASN C  1 107 ? 21.742 42.512  -9.843  1.00 35.91 ? 108 ASN C CA  1 
ATOM   3562 C  C   . ASN C  1 107 ? 20.607 42.753  -8.849  1.00 34.46 ? 108 ASN C C   1 
ATOM   3563 O  O   . ASN C  1 107 ? 20.413 43.878  -8.382  1.00 33.13 ? 108 ASN C O   1 
ATOM   3564 C  CB  . ASN C  1 107 ? 21.205 42.408  -11.270 1.00 33.32 ? 108 ASN C CB  1 
ATOM   3565 C  CG  . ASN C  1 107 ? 20.719 43.732  -11.799 1.00 36.17 ? 108 ASN C CG  1 
ATOM   3566 O  OD1 . ASN C  1 107 ? 21.282 44.782  -11.482 1.00 37.71 ? 108 ASN C OD1 1 
ATOM   3567 N  ND2 . ASN C  1 107 ? 19.672 43.695  -12.622 1.00 37.82 ? 108 ASN C ND2 1 
ATOM   3568 N  N   . GLN C  1 108 ? 19.846 41.707  -8.506  1.00 35.50 ? 109 GLN C N   1 
ATOM   3569 C  CA  . GLN C  1 108 ? 18.786 41.872  -7.509  1.00 37.11 ? 109 GLN C CA  1 
ATOM   3570 C  C   . GLN C  1 108 ? 19.348 42.373  -6.179  1.00 38.17 ? 109 GLN C C   1 
ATOM   3571 O  O   . GLN C  1 108 ? 18.742 43.222  -5.518  1.00 37.15 ? 109 GLN C O   1 
ATOM   3572 C  CB  . GLN C  1 108 ? 18.030 40.555  -7.306  1.00 41.43 ? 109 GLN C CB  1 
ATOM   3573 C  CG  . GLN C  1 108 ? 16.542 40.721  -6.918  1.00 51.07 ? 109 GLN C CG  1 
ATOM   3574 C  CD  . GLN C  1 108 ? 15.622 41.076  -8.123  1.00 64.13 ? 109 GLN C CD  1 
ATOM   3575 O  OE1 . GLN C  1 108 ? 15.269 42.250  -8.332  1.00 57.09 ? 109 GLN C OE1 1 
ATOM   3576 N  NE2 . GLN C  1 108 ? 15.235 40.055  -8.911  1.00 55.33 ? 109 GLN C NE2 1 
ATOM   3577 N  N   . SER C  1 109 ? 20.509 41.859  -5.772  1.00 35.14 ? 110 SER C N   1 
ATOM   3578 C  CA  . SER C  1 109 ? 21.125 42.303  -4.529  1.00 35.29 ? 110 SER C CA  1 
ATOM   3579 C  C   . SER C  1 109 ? 21.516 43.783  -4.593  1.00 40.23 ? 110 SER C C   1 
ATOM   3580 O  O   . SER C  1 109 ? 21.345 44.521  -3.613  1.00 39.25 ? 110 SER C O   1 
ATOM   3581 C  CB  . SER C  1 109 ? 22.336 41.420  -4.224  1.00 34.41 ? 110 SER C CB  1 
ATOM   3582 O  OG  . SER C  1 109 ? 23.031 41.903  -3.098  1.00 41.96 ? 110 SER C OG  1 
ATOM   3583 N  N   . LEU C  1 110 ? 22.036 44.241  -5.741  1.00 37.01 ? 111 LEU C N   1 
ATOM   3584 C  CA  . LEU C  1 110 ? 22.380 45.656  -5.875  1.00 37.45 ? 111 LEU C CA  1 
ATOM   3585 C  C   . LEU C  1 110 ? 21.136 46.539  -5.869  1.00 38.16 ? 111 LEU C C   1 
ATOM   3586 O  O   . LEU C  1 110 ? 21.158 47.643  -5.314  1.00 35.42 ? 111 LEU C O   1 
ATOM   3587 C  CB  . LEU C  1 110 ? 23.183 45.894  -7.154  1.00 35.22 ? 111 LEU C CB  1 
ATOM   3588 C  CG  . LEU C  1 110 ? 24.594 45.307  -7.135  1.00 44.46 ? 111 LEU C CG  1 
ATOM   3589 C  CD1 . LEU C  1 110 ? 25.174 45.243  -8.540  1.00 39.81 ? 111 LEU C CD1 1 
ATOM   3590 C  CD2 . LEU C  1 110 ? 25.492 46.099  -6.210  1.00 37.41 ? 111 LEU C CD2 1 
ATOM   3591 N  N   . LEU C  1 111 ? 20.055 46.094  -6.513  1.00 35.76 ? 112 LEU C N   1 
ATOM   3592 C  CA  . LEU C  1 111 ? 18.821 46.874  -6.483  1.00 32.68 ? 112 LEU C CA  1 
ATOM   3593 C  C   . LEU C  1 111 ? 18.306 47.016  -5.053  1.00 36.68 ? 112 LEU C C   1 
ATOM   3594 O  O   . LEU C  1 111 ? 17.823 48.087  -4.668  1.00 37.95 ? 112 LEU C O   1 
ATOM   3595 C  CB  . LEU C  1 111 ? 17.764 46.236  -7.391  1.00 33.77 ? 112 LEU C CB  1 
ATOM   3596 C  CG  . LEU C  1 111 ? 18.035 46.343  -8.903  1.00 36.05 ? 112 LEU C CG  1 
ATOM   3597 C  CD1 . LEU C  1 111 ? 17.178 45.389  -9.739  1.00 37.47 ? 112 LEU C CD1 1 
ATOM   3598 C  CD2 . LEU C  1 111 ? 17.859 47.771  -9.379  1.00 39.23 ? 112 LEU C CD2 1 
ATOM   3599 N  N   . GLU C  1 112 ? 18.440 45.960  -4.236  1.00 35.03 ? 113 GLU C N   1 
ATOM   3600 C  CA  . GLU C  1 112 ? 18.062 46.068  -2.826  1.00 38.43 ? 113 GLU C CA  1 
ATOM   3601 C  C   . GLU C  1 112 ? 18.946 47.070  -2.094  1.00 36.93 ? 113 GLU C C   1 
ATOM   3602 O  O   . GLU C  1 112 ? 18.461 47.841  -1.262  1.00 36.13 ? 113 GLU C O   1 
ATOM   3603 C  CB  . GLU C  1 112 ? 18.132 44.704  -2.132  1.00 40.79 ? 113 GLU C CB  1 
ATOM   3604 C  CG  . GLU C  1 112 ? 17.122 43.666  -2.634  1.00 48.08 ? 113 GLU C CG  1 
ATOM   3605 C  CD  . GLU C  1 112 ? 17.316 42.287  -1.976  1.00 68.55 ? 113 GLU C CD  1 
ATOM   3606 O  OE1 . GLU C  1 112 ? 17.381 41.272  -2.711  1.00 74.25 ? 113 GLU C OE1 1 
ATOM   3607 O  OE2 . GLU C  1 112 ? 17.404 42.215  -0.727  1.00 72.25 ? 113 GLU C OE2 1 
ATOM   3608 N  N   . LEU C  1 113 ? 20.245 47.078  -2.395  1.00 36.97 ? 114 LEU C N   1 
ATOM   3609 C  CA  . LEU C  1 113 ? 21.143 48.041  -1.771  1.00 39.19 ? 114 LEU C CA  1 
ATOM   3610 C  C   . LEU C  1 113 ? 20.776 49.463  -2.175  1.00 40.91 ? 114 LEU C C   1 
ATOM   3611 O  O   . LEU C  1 113 ? 20.837 50.384  -1.351  1.00 41.80 ? 114 LEU C O   1 
ATOM   3612 C  CB  . LEU C  1 113 ? 22.588 47.718  -2.147  1.00 38.31 ? 114 LEU C CB  1 
ATOM   3613 C  CG  . LEU C  1 113 ? 23.739 48.464  -1.478  1.00 41.55 ? 114 LEU C CG  1 
ATOM   3614 C  CD1 . LEU C  1 113 ? 23.424 48.762  -0.029  1.00 47.62 ? 114 LEU C CD1 1 
ATOM   3615 C  CD2 . LEU C  1 113 ? 25.004 47.612  -1.574  1.00 42.24 ? 114 LEU C CD2 1 
ATOM   3616 N  N   . HIS C  1 114 ? 20.378 49.658  -3.436  1.00 35.34 ? 115 HIS C N   1 
ATOM   3617 C  CA  . HIS C  1 114 ? 19.951 50.980  -3.877  1.00 33.77 ? 115 HIS C CA  1 
ATOM   3618 C  C   . HIS C  1 114 ? 18.702 51.419  -3.136  1.00 38.67 ? 115 HIS C C   1 
ATOM   3619 O  O   . HIS C  1 114 ? 18.578 52.587  -2.749  1.00 34.00 ? 115 HIS C O   1 
ATOM   3620 C  CB  . HIS C  1 114 ? 19.690 50.990  -5.381  1.00 32.24 ? 115 HIS C CB  1 
ATOM   3621 C  CG  . HIS C  1 114 ? 19.464 52.359  -5.940  1.00 38.28 ? 115 HIS C CG  1 
ATOM   3622 N  ND1 . HIS C  1 114 ? 18.250 53.006  -5.852  1.00 39.22 ? 115 HIS C ND1 1 
ATOM   3623 C  CD2 . HIS C  1 114 ? 20.296 53.206  -6.592  1.00 33.56 ? 115 HIS C CD2 1 
ATOM   3624 C  CE1 . HIS C  1 114 ? 18.342 54.191  -6.429  1.00 38.19 ? 115 HIS C CE1 1 
ATOM   3625 N  NE2 . HIS C  1 114 ? 19.572 54.335  -6.888  1.00 37.79 ? 115 HIS C NE2 1 
ATOM   3626 N  N   . SER C  1 115 ? 17.773 50.486  -2.914  1.00 37.66 ? 116 SER C N   1 
ATOM   3627 C  CA  . SER C  1 115 ? 16.515 50.836  -2.262  1.00 39.43 ? 116 SER C CA  1 
ATOM   3628 C  C   . SER C  1 115 ? 16.730 51.255  -0.810  1.00 37.05 ? 116 SER C C   1 
ATOM   3629 O  O   . SER C  1 115 ? 16.121 52.226  -0.349  1.00 40.54 ? 116 SER C O   1 
ATOM   3630 C  CB  . SER C  1 115 ? 15.535 49.666  -2.341  1.00 39.41 ? 116 SER C CB  1 
ATOM   3631 O  OG  . SER C  1 115 ? 14.664 49.686  -1.227  1.00 50.76 ? 116 SER C OG  1 
ATOM   3632 N  N   . THR C  1 116 ? 17.604 50.554  -0.077  1.00 38.78 ? 117 THR C N   1 
ATOM   3633 C  CA  . THR C  1 116 ? 17.878 50.942  1.308   1.00 42.92 ? 117 THR C CA  1 
ATOM   3634 C  C   . THR C  1 116 ? 18.673 52.249  1.397   1.00 44.23 ? 117 THR C C   1 
ATOM   3635 O  O   . THR C  1 116 ? 18.489 53.013  2.351   1.00 45.00 ? 117 THR C O   1 
ATOM   3636 C  CB  . THR C  1 116 ? 18.613 49.820  2.056   1.00 44.33 ? 117 THR C CB  1 
ATOM   3637 O  OG1 . THR C  1 116 ? 19.981 49.767  1.633   1.00 52.24 ? 117 THR C OG1 1 
ATOM   3638 C  CG2 . THR C  1 116 ? 17.944 48.452  1.834   1.00 43.40 ? 117 THR C CG2 1 
ATOM   3639 N  N   . ALA C  1 117 ? 19.551 52.529  0.427   1.00 37.63 ? 118 ALA C N   1 
ATOM   3640 C  CA  . ALA C  1 117 ? 20.209 53.835  0.390   1.00 41.35 ? 118 ALA C CA  1 
ATOM   3641 C  C   . ALA C  1 117 ? 19.214 54.963  0.122   1.00 42.55 ? 118 ALA C C   1 
ATOM   3642 O  O   . ALA C  1 117 ? 19.310 56.036  0.734   1.00 41.08 ? 118 ALA C O   1 
ATOM   3643 C  CB  . ALA C  1 117 ? 21.310 53.853  -0.668  1.00 38.69 ? 118 ALA C CB  1 
ATOM   3644 N  N   . SER C  1 118 ? 18.268 54.753  -0.804  1.00 36.47 ? 119 SER C N   1 
ATOM   3645 C  CA  . SER C  1 118 ? 17.233 55.759  -1.051  1.00 41.71 ? 119 SER C CA  1 
ATOM   3646 C  C   . SER C  1 118 ? 16.369 55.985  0.186   1.00 40.04 ? 119 SER C C   1 
ATOM   3647 O  O   . SER C  1 118 ? 16.001 57.125  0.491   1.00 37.54 ? 119 SER C O   1 
ATOM   3648 C  CB  . SER C  1 118 ? 16.347 55.352  -2.230  1.00 37.86 ? 119 SER C CB  1 
ATOM   3649 O  OG  . SER C  1 118 ? 17.094 54.704  -3.243  1.00 49.17 ? 119 SER C OG  1 
ATOM   3650 N  N   . GLY C  1 119 ? 16.015 54.907  0.891   1.00 39.42 ? 120 GLY C N   1 
ATOM   3651 C  CA  . GLY C  1 119 ? 15.234 55.053  2.107   1.00 42.08 ? 120 GLY C CA  1 
ATOM   3652 C  C   . GLY C  1 119 ? 15.957 55.857  3.174   1.00 48.69 ? 120 GLY C C   1 
ATOM   3653 O  O   . GLY C  1 119 ? 15.338 56.629  3.911   1.00 52.69 ? 120 GLY C O   1 
ATOM   3654 N  N   . ASN C  1 120 ? 17.278 55.706  3.258   1.00 41.91 ? 121 ASN C N   1 
ATOM   3655 C  CA  . ASN C  1 120 ? 18.090 56.452  4.213   1.00 42.65 ? 121 ASN C CA  1 
ATOM   3656 C  C   . ASN C  1 120 ? 18.544 57.809  3.675   1.00 43.10 ? 121 ASN C C   1 
ATOM   3657 O  O   . ASN C  1 120 ? 19.303 58.503  4.358   1.00 45.72 ? 121 ASN C O   1 
ATOM   3658 C  CB  . ASN C  1 120 ? 19.293 55.605  4.640   1.00 42.66 ? 121 ASN C CB  1 
ATOM   3659 C  CG  . ASN C  1 120 ? 18.874 54.385  5.469   1.00 52.07 ? 121 ASN C CG  1 
ATOM   3660 O  OD1 . ASN C  1 120 ? 17.855 54.424  6.163   1.00 54.03 ? 121 ASN C OD1 1 
ATOM   3661 N  ND2 . ASN C  1 120 ? 19.644 53.299  5.385   1.00 46.98 ? 121 ASN C ND2 1 
ATOM   3662 N  N   . ASN C  1 121 ? 18.079 58.200  2.482   1.00 40.54 ? 122 ASN C N   1 
ATOM   3663 C  CA  . ASN C  1 121 ? 18.455 59.445  1.811   1.00 37.63 ? 122 ASN C CA  1 
ATOM   3664 C  C   . ASN C  1 121 ? 19.975 59.637  1.784   1.00 40.77 ? 122 ASN C C   1 
ATOM   3665 O  O   . ASN C  1 121 ? 20.532 60.571  2.369   1.00 41.57 ? 122 ASN C O   1 
ATOM   3666 C  CB  . ASN C  1 121 ? 17.746 60.636  2.460   1.00 42.64 ? 122 ASN C CB  1 
ATOM   3667 C  CG  . ASN C  1 121 ? 16.230 60.464  2.475   1.00 43.72 ? 122 ASN C CG  1 
ATOM   3668 O  OD1 . ASN C  1 121 ? 15.640 60.157  3.508   1.00 47.63 ? 122 ASN C OD1 1 
ATOM   3669 N  ND2 . ASN C  1 121 ? 15.603 60.625  1.316   1.00 43.97 ? 122 ASN C ND2 1 
ATOM   3670 N  N   . ASP C  1 122 ? 20.647 58.723  1.078   1.00 36.72 ? 123 ASP C N   1 
ATOM   3671 C  CA  . ASP C  1 122 ? 22.103 58.714  0.954   1.00 36.04 ? 123 ASP C CA  1 
ATOM   3672 C  C   . ASP C  1 122 ? 22.386 58.842  -0.534  1.00 37.44 ? 123 ASP C C   1 
ATOM   3673 O  O   . ASP C  1 122 ? 22.640 57.835  -1.221  1.00 37.09 ? 123 ASP C O   1 
ATOM   3674 C  CB  . ASP C  1 122 ? 22.713 57.442  1.549   1.00 36.14 ? 123 ASP C CB  1 
ATOM   3675 C  CG  . ASP C  1 122 ? 24.264 57.444  1.528   1.00 47.82 ? 123 ASP C CG  1 
ATOM   3676 O  OD1 . ASP C  1 122 ? 24.875 58.209  0.728   1.00 45.74 ? 123 ASP C OD1 1 
ATOM   3677 O  OD2 . ASP C  1 122 ? 24.875 56.636  2.289   1.00 43.10 ? 123 ASP C OD2 1 
ATOM   3678 N  N   . PRO C  1 123 ? 22.331 60.055  -1.091  1.00 38.16 ? 124 PRO C N   1 
ATOM   3679 C  CA  . PRO C  1 123 ? 22.518 60.203  -2.542  1.00 36.34 ? 124 PRO C CA  1 
ATOM   3680 C  C   . PRO C  1 123 ? 23.932 59.883  -3.004  1.00 35.56 ? 124 PRO C C   1 
ATOM   3681 O  O   . PRO C  1 123 ? 24.119 59.520  -4.173  1.00 34.74 ? 124 PRO C O   1 
ATOM   3682 C  CB  . PRO C  1 123 ? 22.149 61.675  -2.809  1.00 38.55 ? 124 PRO C CB  1 
ATOM   3683 C  CG  . PRO C  1 123 ? 22.350 62.377  -1.482  1.00 34.11 ? 124 PRO C CG  1 
ATOM   3684 C  CD  . PRO C  1 123 ? 22.092 61.349  -0.406  1.00 35.39 ? 124 PRO C CD  1 
ATOM   3685 N  N   . HIS C  1 124 ? 24.938 59.994  -2.136  1.00 35.45 ? 125 HIS C N   1 
ATOM   3686 C  CA  . HIS C  1 124 ? 26.270 59.586  -2.557  1.00 32.93 ? 125 HIS C CA  1 
ATOM   3687 C  C   . HIS C  1 124 ? 26.309 58.093  -2.856  1.00 36.39 ? 125 HIS C C   1 
ATOM   3688 O  O   . HIS C  1 124 ? 26.877 57.666  -3.868  1.00 33.84 ? 125 HIS C O   1 
ATOM   3689 C  CB  . HIS C  1 124 ? 27.302 59.946  -1.498  1.00 33.47 ? 125 HIS C CB  1 
ATOM   3690 C  CG  . HIS C  1 124 ? 28.715 59.815  -1.979  1.00 40.02 ? 125 HIS C CG  1 
ATOM   3691 N  ND1 . HIS C  1 124 ? 29.470 58.678  -1.779  1.00 36.90 ? 125 HIS C ND1 1 
ATOM   3692 C  CD2 . HIS C  1 124 ? 29.505 60.675  -2.666  1.00 40.44 ? 125 HIS C CD2 1 
ATOM   3693 C  CE1 . HIS C  1 124 ? 30.668 58.849  -2.309  1.00 40.83 ? 125 HIS C CE1 1 
ATOM   3694 N  NE2 . HIS C  1 124 ? 30.714 60.051  -2.857  1.00 42.60 ? 125 HIS C NE2 1 
ATOM   3695 N  N   . LEU C  1 125 ? 25.686 57.285  -2.000  1.00 32.83 ? 126 LEU C N   1 
ATOM   3696 C  CA  . LEU C  1 125 ? 25.681 55.847  -2.241  1.00 35.78 ? 126 LEU C CA  1 
ATOM   3697 C  C   . LEU C  1 125 ? 24.823 55.486  -3.453  1.00 33.42 ? 126 LEU C C   1 
ATOM   3698 O  O   . LEU C  1 125 ? 25.217 54.623  -4.245  1.00 30.30 ? 126 LEU C O   1 
ATOM   3699 C  CB  . LEU C  1 125 ? 25.219 55.105  -0.981  1.00 33.74 ? 126 LEU C CB  1 
ATOM   3700 C  CG  . LEU C  1 125 ? 25.020 53.581  -1.036  1.00 37.43 ? 126 LEU C CG  1 
ATOM   3701 C  CD1 . LEU C  1 125 ? 26.181 52.853  -1.711  1.00 33.36 ? 126 LEU C CD1 1 
ATOM   3702 C  CD2 . LEU C  1 125 ? 24.763 53.008  0.363   1.00 33.82 ? 126 LEU C CD2 1 
ATOM   3703 N  N   . THR C  1 126 ? 23.658 56.132  -3.635  1.00 29.52 ? 127 THR C N   1 
ATOM   3704 C  CA  . THR C  1 126 ? 22.855 55.764  -4.804  1.00 37.34 ? 127 THR C CA  1 
ATOM   3705 C  C   . THR C  1 126 ? 23.568 56.143  -6.093  1.00 35.74 ? 127 THR C C   1 
ATOM   3706 O  O   . THR C  1 126 ? 23.448 55.432  -7.094  1.00 34.93 ? 127 THR C O   1 
ATOM   3707 C  CB  . THR C  1 126 ? 21.448 56.394  -4.788  1.00 35.53 ? 127 THR C CB  1 
ATOM   3708 O  OG1 . THR C  1 126 ? 21.533 57.819  -4.681  1.00 38.50 ? 127 THR C OG1 1 
ATOM   3709 C  CG2 . THR C  1 126 ? 20.583 55.835  -3.652  1.00 37.42 ? 127 THR C CG2 1 
ATOM   3710 N  N   . LYS C  1 127 ? 24.313 57.250  -6.085  1.00 37.19 ? 128 LYS C N   1 
ATOM   3711 C  CA  . LYS C  1 127 ? 25.131 57.615  -7.240  1.00 39.23 ? 128 LYS C CA  1 
ATOM   3712 C  C   . LYS C  1 127 ? 26.155 56.527  -7.547  1.00 38.69 ? 128 LYS C C   1 
ATOM   3713 O  O   . LYS C  1 127 ? 26.296 56.100  -8.698  1.00 34.16 ? 128 LYS C O   1 
ATOM   3714 C  CB  . LYS C  1 127 ? 25.826 58.953  -6.979  1.00 41.27 ? 128 LYS C CB  1 
ATOM   3715 C  CG  . LYS C  1 127 ? 26.374 59.669  -8.207  1.00 46.89 ? 128 LYS C CG  1 
ATOM   3716 C  CD  . LYS C  1 127 ? 27.891 59.784  -8.149  1.00 53.98 ? 128 LYS C CD  1 
ATOM   3717 C  CE  . LYS C  1 127 ? 28.440 60.702  -9.249  1.00 60.89 ? 128 LYS C CE  1 
ATOM   3718 N  NZ  . LYS C  1 127 ? 28.712 60.023  -10.542 1.00 58.74 ? 128 LYS C NZ  1 
ATOM   3719 N  N   . LEU C  1 128 ? 26.872 56.059  -6.519  1.00 34.30 ? 129 LEU C N   1 
ATOM   3720 C  CA  . LEU C  1 128 ? 27.850 54.997  -6.726  1.00 35.81 ? 129 LEU C CA  1 
ATOM   3721 C  C   . LEU C  1 128 ? 27.197 53.755  -7.328  1.00 38.83 ? 129 LEU C C   1 
ATOM   3722 O  O   . LEU C  1 128 ? 27.724 53.168  -8.279  1.00 38.65 ? 129 LEU C O   1 
ATOM   3723 C  CB  . LEU C  1 128 ? 28.554 54.645  -5.416  1.00 33.20 ? 129 LEU C CB  1 
ATOM   3724 C  CG  . LEU C  1 128 ? 29.425 53.396  -5.605  1.00 37.10 ? 129 LEU C CG  1 
ATOM   3725 C  CD1 . LEU C  1 128 ? 30.854 53.779  -6.025  1.00 29.20 ? 129 LEU C CD1 1 
ATOM   3726 C  CD2 . LEU C  1 128 ? 29.424 52.507  -4.362  1.00 34.22 ? 129 LEU C CD2 1 
ATOM   3727 N  N   . LEU C  1 129 ? 26.035 53.347  -6.797  1.00 34.95 ? 130 LEU C N   1 
ATOM   3728 C  CA  . LEU C  1 129 ? 25.402 52.131  -7.299  1.00 36.41 ? 130 LEU C CA  1 
ATOM   3729 C  C   . LEU C  1 129 ? 24.948 52.307  -8.740  1.00 40.43 ? 130 LEU C C   1 
ATOM   3730 O  O   . LEU C  1 129 ? 25.109 51.398  -9.558  1.00 39.77 ? 130 LEU C O   1 
ATOM   3731 C  CB  . LEU C  1 129 ? 24.232 51.723  -6.408  1.00 32.49 ? 130 LEU C CB  1 
ATOM   3732 C  CG  . LEU C  1 129 ? 24.689 51.298  -5.011  1.00 35.08 ? 130 LEU C CG  1 
ATOM   3733 C  CD1 . LEU C  1 129 ? 23.505 51.186  -4.074  1.00 33.45 ? 130 LEU C CD1 1 
ATOM   3734 C  CD2 . LEU C  1 129 ? 25.483 49.982  -5.040  1.00 34.70 ? 130 LEU C CD2 1 
ATOM   3735 N  N   . GLU C  1 130 ? 24.435 53.487  -9.080  1.00 38.54 ? 131 GLU C N   1 
ATOM   3736 C  CA  . GLU C  1 130 ? 24.004 53.728  -10.450 1.00 42.29 ? 131 GLU C CA  1 
ATOM   3737 C  C   . GLU C  1 130 ? 25.183 53.711  -11.430 1.00 49.20 ? 131 GLU C C   1 
ATOM   3738 O  O   . GLU C  1 130 ? 25.122 53.038  -12.468 1.00 51.94 ? 131 GLU C O   1 
ATOM   3739 C  CB  . GLU C  1 130 ? 23.234 55.048  -10.515 1.00 43.97 ? 131 GLU C CB  1 
ATOM   3740 C  CG  . GLU C  1 130 ? 21.850 54.949  -9.882  1.00 42.72 ? 131 GLU C CG  1 
ATOM   3741 C  CD  . GLU C  1 130 ? 21.151 56.297  -9.702  1.00 51.17 ? 131 GLU C CD  1 
ATOM   3742 O  OE1 . GLU C  1 130 ? 21.471 57.266  -10.441 1.00 60.02 ? 131 GLU C OE1 1 
ATOM   3743 O  OE2 . GLU C  1 130 ? 20.267 56.378  -8.814  1.00 47.75 ? 131 GLU C OE2 1 
ATOM   3744 N  N   . ASP C  1 131 ? 26.277 54.422  -11.114 1.00 43.40 ? 132 ASP C N   1 
ATOM   3745 C  CA  . ASP C  1 131 ? 27.321 54.648  -12.120 1.00 51.04 ? 132 ASP C CA  1 
ATOM   3746 C  C   . ASP C  1 131 ? 28.278 53.472  -12.283 1.00 49.58 ? 132 ASP C C   1 
ATOM   3747 O  O   . ASP C  1 131 ? 28.748 53.217  -13.394 1.00 52.42 ? 132 ASP C O   1 
ATOM   3748 C  CB  . ASP C  1 131 ? 28.140 55.894  -11.792 1.00 49.49 ? 132 ASP C CB  1 
ATOM   3749 C  CG  . ASP C  1 131 ? 27.298 57.143  -11.745 1.00 61.66 ? 132 ASP C CG  1 
ATOM   3750 O  OD1 . ASP C  1 131 ? 26.128 57.095  -12.183 1.00 65.47 ? 132 ASP C OD1 1 
ATOM   3751 O  OD2 . ASP C  1 131 ? 27.817 58.185  -11.294 1.00 69.05 ? 132 ASP C OD2 1 
ATOM   3752 N  N   . GLU C  1 132 ? 28.620 52.773  -11.198 1.00 51.58 ? 133 GLU C N   1 
ATOM   3753 C  CA  . GLU C  1 132 ? 29.670 51.761  -11.242 1.00 46.44 ? 133 GLU C CA  1 
ATOM   3754 C  C   . GLU C  1 132 ? 29.164 50.327  -11.168 1.00 46.75 ? 133 GLU C C   1 
ATOM   3755 O  O   . GLU C  1 132 ? 29.972 49.406  -11.315 1.00 54.30 ? 133 GLU C O   1 
ATOM   3756 C  CB  . GLU C  1 132 ? 30.685 51.992  -10.105 1.00 51.57 ? 133 GLU C CB  1 
ATOM   3757 C  CG  . GLU C  1 132 ? 32.122 52.402  -10.569 1.00 66.13 ? 133 GLU C CG  1 
ATOM   3758 C  CD  . GLU C  1 132 ? 32.982 51.243  -11.151 1.00 76.31 ? 133 GLU C CD  1 
ATOM   3759 O  OE1 . GLU C  1 132 ? 32.595 50.052  -11.035 1.00 70.29 ? 133 GLU C OE1 1 
ATOM   3760 O  OE2 . GLU C  1 132 ? 34.061 51.530  -11.730 1.00 76.74 ? 133 GLU C OE2 1 
ATOM   3761 N  N   . TYR C  1 133 ? 27.868 50.099  -10.950 1.00 42.51 ? 134 TYR C N   1 
ATOM   3762 C  CA  . TYR C  1 133 ? 27.423 48.717  -10.795 1.00 45.08 ? 134 TYR C CA  1 
ATOM   3763 C  C   . TYR C  1 133 ? 26.197 48.380  -11.633 1.00 40.27 ? 134 TYR C C   1 
ATOM   3764 O  O   . TYR C  1 133 ? 26.231 47.431  -12.421 1.00 43.63 ? 134 TYR C O   1 
ATOM   3765 C  CB  . TYR C  1 133 ? 27.156 48.414  -9.322  1.00 38.68 ? 134 TYR C CB  1 
ATOM   3766 C  CG  . TYR C  1 133 ? 28.425 48.397  -8.511  1.00 42.62 ? 134 TYR C CG  1 
ATOM   3767 C  CD1 . TYR C  1 133 ? 29.171 47.229  -8.387  1.00 37.57 ? 134 TYR C CD1 1 
ATOM   3768 C  CD2 . TYR C  1 133 ? 28.899 49.557  -7.894  1.00 39.76 ? 134 TYR C CD2 1 
ATOM   3769 C  CE1 . TYR C  1 133 ? 30.346 47.206  -7.667  1.00 40.30 ? 134 TYR C CE1 1 
ATOM   3770 C  CE2 . TYR C  1 133 ? 30.080 49.546  -7.159  1.00 39.09 ? 134 TYR C CE2 1 
ATOM   3771 C  CZ  . TYR C  1 133 ? 30.792 48.362  -7.053  1.00 41.10 ? 134 TYR C CZ  1 
ATOM   3772 O  OH  . TYR C  1 133 ? 31.941 48.325  -6.322  1.00 34.23 ? 134 TYR C OH  1 
ATOM   3773 N  N   . LEU C  1 134 ? 25.120 49.153  -11.478 1.00 41.49 ? 135 LEU C N   1 
ATOM   3774 C  CA  . LEU C  1 134 ? 23.853 48.801  -12.114 1.00 43.73 ? 135 LEU C CA  1 
ATOM   3775 C  C   . LEU C  1 134 ? 23.960 48.827  -13.632 1.00 37.75 ? 135 LEU C C   1 
ATOM   3776 O  O   . LEU C  1 134 ? 23.429 47.934  -14.300 1.00 37.74 ? 135 LEU C O   1 
ATOM   3777 C  CB  . LEU C  1 134 ? 22.736 49.725  -11.627 1.00 37.75 ? 135 LEU C CB  1 
ATOM   3778 C  CG  . LEU C  1 134 ? 22.392 49.496  -10.152 1.00 42.18 ? 135 LEU C CG  1 
ATOM   3779 C  CD1 . LEU C  1 134 ? 21.300 50.453  -9.670  1.00 42.11 ? 135 LEU C CD1 1 
ATOM   3780 C  CD2 . LEU C  1 134 ? 21.964 48.054  -9.969  1.00 43.13 ? 135 LEU C CD2 1 
ATOM   3781 N  N   . GLU C  1 135 ? 24.652 49.831  -14.190 1.00 37.98 ? 136 GLU C N   1 
ATOM   3782 C  CA  . GLU C  1 135 ? 24.985 49.835  -15.615 1.00 44.13 ? 136 GLU C CA  1 
ATOM   3783 C  C   . GLU C  1 135 ? 25.699 48.565  -16.043 1.00 44.50 ? 136 GLU C C   1 
ATOM   3784 O  O   . GLU C  1 135 ? 25.255 47.858  -16.957 1.00 42.15 ? 136 GLU C O   1 
ATOM   3785 C  CB  . GLU C  1 135 ? 25.876 51.018  -15.976 1.00 49.91 ? 136 GLU C CB  1 
ATOM   3786 C  CG  . GLU C  1 135 ? 25.256 52.056  -16.862 1.00 61.00 ? 136 GLU C CG  1 
ATOM   3787 C  CD  . GLU C  1 135 ? 25.899 53.417  -16.685 1.00 76.66 ? 136 GLU C CD  1 
ATOM   3788 O  OE1 . GLU C  1 135 ? 27.122 53.488  -16.388 1.00 72.77 ? 136 GLU C OE1 1 
ATOM   3789 O  OE2 . GLU C  1 135 ? 25.198 54.418  -16.926 1.00 78.96 ? 136 GLU C OE2 1 
ATOM   3790 N  N   . GLU C  1 136 ? 26.857 48.306  -15.433 1.00 44.11 ? 137 GLU C N   1 
ATOM   3791 C  CA  . GLU C  1 136 ? 27.665 47.159  -15.819 1.00 47.21 ? 137 GLU C CA  1 
ATOM   3792 C  C   . GLU C  1 136 ? 26.863 45.880  -15.709 1.00 43.96 ? 137 GLU C C   1 
ATOM   3793 O  O   . GLU C  1 136 ? 26.949 45.005  -16.578 1.00 41.82 ? 137 GLU C O   1 
ATOM   3794 C  CB  . GLU C  1 136 ? 28.911 47.090  -14.936 1.00 53.31 ? 137 GLU C CB  1 
ATOM   3795 C  CG  . GLU C  1 136 ? 30.134 47.790  -15.528 1.00 66.70 ? 137 GLU C CG  1 
ATOM   3796 C  CD  . GLU C  1 136 ? 31.407 46.962  -15.373 1.00 78.00 ? 137 GLU C CD  1 
ATOM   3797 O  OE1 . GLU C  1 136 ? 31.338 45.716  -15.536 1.00 76.34 ? 137 GLU C OE1 1 
ATOM   3798 O  OE2 . GLU C  1 136 ? 32.469 47.563  -15.077 1.00 82.06 ? 137 GLU C OE2 1 
ATOM   3799 N  N   . GLN C  1 137 ? 26.056 45.772  -14.654 1.00 38.21 ? 138 GLN C N   1 
ATOM   3800 C  CA  . GLN C  1 137 ? 25.270 44.571  -14.427 1.00 38.51 ? 138 GLN C CA  1 
ATOM   3801 C  C   . GLN C  1 137 ? 24.281 44.342  -15.566 1.00 37.44 ? 138 GLN C C   1 
ATOM   3802 O  O   . GLN C  1 137 ? 24.170 43.232  -16.092 1.00 34.77 ? 138 GLN C O   1 
ATOM   3803 C  CB  . GLN C  1 137 ? 24.569 44.694  -13.071 1.00 37.50 ? 138 GLN C CB  1 
ATOM   3804 C  CG  . GLN C  1 137 ? 24.492 43.421  -12.247 1.00 41.97 ? 138 GLN C CG  1 
ATOM   3805 C  CD  . GLN C  1 137 ? 25.794 42.637  -12.198 1.00 40.99 ? 138 GLN C CD  1 
ATOM   3806 O  OE1 . GLN C  1 137 ? 26.882 43.198  -12.129 1.00 38.04 ? 138 GLN C OE1 1 
ATOM   3807 N  NE2 . GLN C  1 137 ? 25.674 41.321  -12.256 1.00 42.39 ? 138 GLN C NE2 1 
ATOM   3808 N  N   . VAL C  1 138 ? 23.578 45.394  -15.989 1.00 36.03 ? 139 VAL C N   1 
ATOM   3809 C  CA  . VAL C  1 138 ? 22.622 45.236  -17.078 1.00 35.71 ? 139 VAL C CA  1 
ATOM   3810 C  C   . VAL C  1 138 ? 23.345 44.906  -18.385 1.00 37.55 ? 139 VAL C C   1 
ATOM   3811 O  O   . VAL C  1 138 ? 22.853 44.104  -19.191 1.00 32.12 ? 139 VAL C O   1 
ATOM   3812 C  CB  . VAL C  1 138 ? 21.743 46.497  -17.194 1.00 35.54 ? 139 VAL C CB  1 
ATOM   3813 C  CG1 . VAL C  1 138 ? 21.198 46.672  -18.602 1.00 34.42 ? 139 VAL C CG1 1 
ATOM   3814 C  CG2 . VAL C  1 138 ? 20.610 46.436  -16.190 1.00 36.47 ? 139 VAL C CG2 1 
ATOM   3815 N  N   . ASP C  1 139 ? 24.534 45.495  -18.602 1.00 35.64 ? 140 ASP C N   1 
ATOM   3816 C  CA  . ASP C  1 139 ? 25.342 45.176  -19.786 1.00 38.02 ? 140 ASP C CA  1 
ATOM   3817 C  C   . ASP C  1 139 ? 25.792 43.719  -19.788 1.00 38.06 ? 140 ASP C C   1 
ATOM   3818 O  O   . ASP C  1 139 ? 25.752 43.049  -20.827 1.00 36.48 ? 140 ASP C O   1 
ATOM   3819 C  CB  . ASP C  1 139 ? 26.575 46.083  -19.861 1.00 36.62 ? 140 ASP C CB  1 
ATOM   3820 C  CG  . ASP C  1 139 ? 26.238 47.537  -20.185 1.00 49.81 ? 140 ASP C CG  1 
ATOM   3821 O  OD1 . ASP C  1 139 ? 25.092 47.833  -20.613 1.00 56.65 ? 140 ASP C OD1 1 
ATOM   3822 O  OD2 . ASP C  1 139 ? 27.137 48.390  -20.000 1.00 54.32 ? 140 ASP C OD2 1 
ATOM   3823 N  N   A SER C  1 140 ? 26.258 43.222  -18.637 0.58 38.11 ? 141 SER C N   1 
ATOM   3824 N  N   B SER C  1 140 ? 26.228 43.214  -18.631 0.42 38.29 ? 141 SER C N   1 
ATOM   3825 C  CA  A SER C  1 140 ? 26.677 41.828  -18.532 0.58 37.88 ? 141 SER C CA  1 
ATOM   3826 C  CA  B SER C  1 140 ? 26.683 41.832  -18.528 0.42 37.84 ? 141 SER C CA  1 
ATOM   3827 C  C   A SER C  1 140 ? 25.518 40.880  -18.811 0.58 37.60 ? 141 SER C C   1 
ATOM   3828 C  C   B SER C  1 140 ? 25.538 40.847  -18.747 0.42 37.71 ? 141 SER C C   1 
ATOM   3829 O  O   A SER C  1 140 ? 25.674 39.891  -19.534 0.58 36.03 ? 141 SER C O   1 
ATOM   3830 O  O   B SER C  1 140 ? 25.728 39.795  -19.369 0.42 36.08 ? 141 SER C O   1 
ATOM   3831 C  CB  A SER C  1 140 ? 27.258 41.560  -17.140 0.58 38.98 ? 141 SER C CB  1 
ATOM   3832 C  CB  B SER C  1 140 ? 27.339 41.613  -17.162 0.42 39.06 ? 141 SER C CB  1 
ATOM   3833 O  OG  A SER C  1 140 ? 28.527 42.173  -16.988 0.58 42.59 ? 141 SER C OG  1 
ATOM   3834 O  OG  B SER C  1 140 ? 27.090 40.314  -16.668 0.42 38.89 ? 141 SER C OG  1 
ATOM   3835 N  N   . ILE C  1 141 ? 24.345 41.163  -18.238 1.00 38.46 ? 142 ILE C N   1 
ATOM   3836 C  CA  . ILE C  1 141 ? 23.202 40.276  -18.422 1.00 35.80 ? 142 ILE C CA  1 
ATOM   3837 C  C   . ILE C  1 141 ? 22.788 40.237  -19.889 1.00 36.19 ? 142 ILE C C   1 
ATOM   3838 O  O   . ILE C  1 141 ? 22.470 39.171  -20.432 1.00 34.37 ? 142 ILE C O   1 
ATOM   3839 C  CB  . ILE C  1 141 ? 22.044 40.711  -17.506 1.00 30.49 ? 142 ILE C CB  1 
ATOM   3840 C  CG1 . ILE C  1 141 ? 22.347 40.313  -16.064 1.00 35.60 ? 142 ILE C CG1 1 
ATOM   3841 C  CG2 . ILE C  1 141 ? 20.732 40.092  -17.948 1.00 29.58 ? 142 ILE C CG2 1 
ATOM   3842 C  CD1 . ILE C  1 141 ? 21.554 41.117  -15.040 1.00 37.76 ? 142 ILE C CD1 1 
ATOM   3843 N  N   . LYS C  1 142 ? 22.793 41.396  -20.556 1.00 35.05 ? 143 LYS C N   1 
ATOM   3844 C  CA  . LYS C  1 142 ? 22.446 41.431  -21.971 1.00 34.78 ? 143 LYS C CA  1 
ATOM   3845 C  C   . LYS C  1 142 ? 23.459 40.652  -22.795 1.00 37.64 ? 143 LYS C C   1 
ATOM   3846 O  O   . LYS C  1 142 ? 23.081 39.886  -23.690 1.00 34.90 ? 143 LYS C O   1 
ATOM   3847 C  CB  . LYS C  1 142 ? 22.362 42.875  -22.469 1.00 37.79 ? 143 LYS C CB  1 
ATOM   3848 C  CG  . LYS C  1 142 ? 22.174 43.006  -23.988 1.00 36.05 ? 143 LYS C CG  1 
ATOM   3849 C  CD  . LYS C  1 142 ? 20.846 42.367  -24.419 1.00 41.38 ? 143 LYS C CD  1 
ATOM   3850 C  CE  . LYS C  1 142 ? 20.352 42.897  -25.764 1.00 38.26 ? 143 LYS C CE  1 
ATOM   3851 N  NZ  . LYS C  1 142 ? 21.450 43.078  -26.755 1.00 42.60 ? 143 LYS C NZ  1 
ATOM   3852 N  N   . LYS C  1 143 ? 24.751 40.839  -22.507 1.00 34.31 ? 144 LYS C N   1 
ATOM   3853 C  CA  . LYS C  1 143 ? 25.790 40.147  -23.264 1.00 39.37 ? 144 LYS C CA  1 
ATOM   3854 C  C   . LYS C  1 143 ? 25.657 38.632  -23.129 1.00 37.67 ? 144 LYS C C   1 
ATOM   3855 O  O   . LYS C  1 143 ? 25.765 37.895  -24.116 1.00 36.66 ? 144 LYS C O   1 
ATOM   3856 C  CB  . LYS C  1 143 ? 27.172 40.622  -22.801 1.00 36.83 ? 144 LYS C CB  1 
ATOM   3857 C  CG  . LYS C  1 143 ? 28.385 40.026  -23.562 1.00 45.28 ? 144 LYS C CG  1 
ATOM   3858 C  CD  . LYS C  1 143 ? 28.281 40.049  -25.120 1.00 52.36 ? 144 LYS C CD  1 
ATOM   3859 C  CE  . LYS C  1 143 ? 27.674 41.344  -25.761 1.00 60.86 ? 144 LYS C CE  1 
ATOM   3860 N  NZ  . LYS C  1 143 ? 27.100 41.120  -27.160 1.00 57.98 ? 144 LYS C NZ  1 
ATOM   3861 N  N   . ILE C  1 144 ? 25.415 38.147  -21.911 1.00 31.88 ? 145 ILE C N   1 
ATOM   3862 C  CA  . ILE C  1 144 ? 25.302 36.706  -21.723 1.00 38.51 ? 145 ILE C CA  1 
ATOM   3863 C  C   . ILE C  1 144 ? 24.054 36.178  -22.412 1.00 35.66 ? 145 ILE C C   1 
ATOM   3864 O  O   . ILE C  1 144 ? 24.080 35.109  -23.033 1.00 33.11 ? 145 ILE C O   1 
ATOM   3865 C  CB  . ILE C  1 144 ? 25.325 36.361  -20.224 1.00 40.75 ? 145 ILE C CB  1 
ATOM   3866 C  CG1 . ILE C  1 144 ? 26.721 36.644  -19.670 1.00 35.86 ? 145 ILE C CG1 1 
ATOM   3867 C  CG2 . ILE C  1 144 ? 24.898 34.898  -19.982 1.00 32.71 ? 145 ILE C CG2 1 
ATOM   3868 C  CD1 . ILE C  1 144 ? 26.787 36.632  -18.170 1.00 36.53 ? 145 ILE C CD1 1 
ATOM   3869 N  N   . GLY C  1 145 ? 22.949 36.926  -22.326 1.00 37.05 ? 146 GLY C N   1 
ATOM   3870 C  CA  . GLY C  1 145 ? 21.758 36.564  -23.075 1.00 35.55 ? 146 GLY C CA  1 
ATOM   3871 C  C   . GLY C  1 145 ? 22.029 36.415  -24.561 1.00 35.49 ? 146 GLY C C   1 
ATOM   3872 O  O   . GLY C  1 145 ? 21.626 35.426  -25.178 1.00 32.00 ? 146 GLY C O   1 
ATOM   3873 N  N   . ASP C  1 146 ? 22.744 37.386  -25.148 1.00 33.52 ? 147 ASP C N   1 
ATOM   3874 C  CA  . ASP C  1 146 ? 23.106 37.312  -26.561 1.00 36.79 ? 147 ASP C CA  1 
ATOM   3875 C  C   . ASP C  1 146 ? 23.896 36.043  -26.859 1.00 37.46 ? 147 ASP C C   1 
ATOM   3876 O  O   . ASP C  1 146 ? 23.642 35.373  -27.865 1.00 33.13 ? 147 ASP C O   1 
ATOM   3877 C  CB  . ASP C  1 146 ? 23.942 38.527  -26.996 1.00 40.77 ? 147 ASP C CB  1 
ATOM   3878 C  CG  . ASP C  1 146 ? 23.170 39.868  -26.975 1.00 50.26 ? 147 ASP C CG  1 
ATOM   3879 O  OD1 . ASP C  1 146 ? 21.954 39.896  -27.285 1.00 48.31 ? 147 ASP C OD1 1 
ATOM   3880 O  OD2 . ASP C  1 146 ? 23.819 40.916  -26.702 1.00 52.15 ? 147 ASP C OD2 1 
ATOM   3881 N  N   . MET C  1 147 ? 24.871 35.708  -26.003 1.00 34.80 ? 148 MET C N   1 
ATOM   3882 C  CA  . MET C  1 147 ? 25.731 34.564  -26.294 1.00 36.79 ? 148 MET C CA  1 
ATOM   3883 C  C   . MET C  1 147 ? 24.949 33.268  -26.249 1.00 33.30 ? 148 MET C C   1 
ATOM   3884 O  O   . MET C  1 147 ? 25.143 32.398  -27.098 1.00 33.72 ? 148 MET C O   1 
ATOM   3885 C  CB  . MET C  1 147 ? 26.914 34.481  -25.326 1.00 31.83 ? 148 MET C CB  1 
ATOM   3886 C  CG  . MET C  1 147 ? 27.953 35.575  -25.499 1.00 36.29 ? 148 MET C CG  1 
ATOM   3887 S  SD  . MET C  1 147 ? 28.815 35.947  -23.964 1.00 45.80 ? 148 MET C SD  1 
ATOM   3888 C  CE  . MET C  1 147 ? 29.920 34.544  -23.903 1.00 43.39 ? 148 MET C CE  1 
ATOM   3889 N  N   . ILE C  1 148 ? 24.053 33.128  -25.271 1.00 30.82 ? 149 ILE C N   1 
ATOM   3890 C  CA  . ILE C  1 148 ? 23.249 31.915  -25.172 1.00 34.12 ? 149 ILE C CA  1 
ATOM   3891 C  C   . ILE C  1 148 ? 22.424 31.725  -26.441 1.00 34.57 ? 149 ILE C C   1 
ATOM   3892 O  O   . ILE C  1 148 ? 22.321 30.613  -26.976 1.00 32.33 ? 149 ILE C O   1 
ATOM   3893 C  CB  . ILE C  1 148 ? 22.368 31.972  -23.910 1.00 35.22 ? 149 ILE C CB  1 
ATOM   3894 C  CG1 . ILE C  1 148 ? 23.226 31.819  -22.652 1.00 33.77 ? 149 ILE C CG1 1 
ATOM   3895 C  CG2 . ILE C  1 148 ? 21.270 30.906  -23.953 1.00 35.78 ? 149 ILE C CG2 1 
ATOM   3896 C  CD1 . ILE C  1 148 ? 22.426 32.009  -21.360 1.00 32.73 ? 149 ILE C CD1 1 
ATOM   3897 N  N   . THR C  1 149 ? 21.847 32.813  -26.959 1.00 35.68 ? 150 THR C N   1 
ATOM   3898 C  CA  . THR C  1 149 ? 21.080 32.719  -28.196 1.00 35.43 ? 150 THR C CA  1 
ATOM   3899 C  C   . THR C  1 149 ? 21.978 32.321  -29.363 1.00 34.43 ? 150 THR C C   1 
ATOM   3900 O  O   . THR C  1 149 ? 21.620 31.448  -30.167 1.00 30.56 ? 150 THR C O   1 
ATOM   3901 C  CB  . THR C  1 149 ? 20.382 34.051  -28.479 1.00 37.41 ? 150 THR C CB  1 
ATOM   3902 O  OG1 . THR C  1 149 ? 19.522 34.393  -27.386 1.00 35.02 ? 150 THR C OG1 1 
ATOM   3903 C  CG2 . THR C  1 149 ? 19.549 33.970  -29.755 1.00 37.48 ? 150 THR C CG2 1 
ATOM   3904 N  N   . LYS C  1 150 ? 23.160 32.937  -29.459 1.00 29.00 ? 151 LYS C N   1 
ATOM   3905 C  CA  . LYS C  1 150 ? 24.094 32.600  -30.534 1.00 37.05 ? 151 LYS C CA  1 
ATOM   3906 C  C   . LYS C  1 150 ? 24.585 31.160  -30.408 1.00 34.63 ? 151 LYS C C   1 
ATOM   3907 O  O   . LYS C  1 150 ? 24.666 30.433  -31.404 1.00 32.60 ? 151 LYS C O   1 
ATOM   3908 C  CB  . LYS C  1 150 ? 25.277 33.578  -30.534 1.00 32.34 ? 151 LYS C CB  1 
ATOM   3909 C  CG  . LYS C  1 150 ? 24.929 34.984  -31.015 1.00 35.30 ? 151 LYS C CG  1 
ATOM   3910 C  CD  . LYS C  1 150 ? 26.197 35.761  -31.392 1.00 40.54 ? 151 LYS C CD  1 
ATOM   3911 C  CE  . LYS C  1 150 ? 26.441 36.929  -30.445 1.00 40.79 ? 151 LYS C CE  1 
ATOM   3912 N  NZ  . LYS C  1 150 ? 26.595 38.234  -31.166 1.00 54.68 ? 151 LYS C NZ  1 
ATOM   3913 N  N   . LEU C  1 151 ? 24.910 30.729  -29.190 1.00 29.65 ? 152 LEU C N   1 
ATOM   3914 C  CA  . LEU C  1 151 ? 25.375 29.363  -29.005 1.00 34.10 ? 152 LEU C CA  1 
ATOM   3915 C  C   . LEU C  1 151 ? 24.292 28.358  -29.383 1.00 35.30 ? 152 LEU C C   1 
ATOM   3916 O  O   . LEU C  1 151 ? 24.577 27.330  -30.012 1.00 35.06 ? 152 LEU C O   1 
ATOM   3917 C  CB  . LEU C  1 151 ? 25.824 29.162  -27.559 1.00 33.12 ? 152 LEU C CB  1 
ATOM   3918 C  CG  . LEU C  1 151 ? 26.372 27.778  -27.228 1.00 34.80 ? 152 LEU C CG  1 
ATOM   3919 C  CD1 . LEU C  1 151 ? 27.389 27.333  -28.273 1.00 31.55 ? 152 LEU C CD1 1 
ATOM   3920 C  CD2 . LEU C  1 151 ? 26.971 27.757  -25.823 1.00 30.34 ? 152 LEU C CD2 1 
ATOM   3921 N  N   . LYS C  1 152 ? 23.039 28.641  -29.023 1.00 33.57 ? 153 LYS C N   1 
ATOM   3922 C  CA  . LYS C  1 152 ? 21.961 27.714  -29.352 1.00 36.02 ? 153 LYS C CA  1 
ATOM   3923 C  C   . LYS C  1 152 ? 21.730 27.630  -30.856 1.00 35.04 ? 153 LYS C C   1 
ATOM   3924 O  O   . LYS C  1 152 ? 21.343 26.573  -31.366 1.00 39.10 ? 153 LYS C O   1 
ATOM   3925 C  CB  . LYS C  1 152 ? 20.677 28.138  -28.648 1.00 39.40 ? 153 LYS C CB  1 
ATOM   3926 C  CG  . LYS C  1 152 ? 20.604 27.751  -27.180 1.00 41.66 ? 153 LYS C CG  1 
ATOM   3927 C  CD  . LYS C  1 152 ? 19.285 28.241  -26.591 1.00 44.06 ? 153 LYS C CD  1 
ATOM   3928 C  CE  . LYS C  1 152 ? 19.094 27.772  -25.168 1.00 48.44 ? 153 LYS C CE  1 
ATOM   3929 N  NZ  . LYS C  1 152 ? 17.974 28.521  -24.518 1.00 51.59 ? 153 LYS C NZ  1 
ATOM   3930 N  N   . ARG C  1 153 ? 21.933 28.738  -31.570 1.00 34.16 ? 154 ARG C N   1 
ATOM   3931 C  CA  . ARG C  1 153 ? 21.826 28.721  -33.023 1.00 39.74 ? 154 ARG C CA  1 
ATOM   3932 C  C   . ARG C  1 153 ? 22.957 27.899  -33.632 1.00 39.95 ? 154 ARG C C   1 
ATOM   3933 O  O   . ARG C  1 153 ? 22.712 26.963  -34.403 1.00 39.06 ? 154 ARG C O   1 
ATOM   3934 C  CB  . ARG C  1 153 ? 21.842 30.156  -33.567 1.00 35.20 ? 154 ARG C CB  1 
ATOM   3935 C  CG  . ARG C  1 153 ? 22.101 30.249  -35.077 1.00 39.65 ? 154 ARG C CG  1 
ATOM   3936 C  CD  . ARG C  1 153 ? 22.005 31.682  -35.609 1.00 38.81 ? 154 ARG C CD  1 
ATOM   3937 N  NE  . ARG C  1 153 ? 20.701 32.277  -35.336 1.00 43.18 ? 154 ARG C NE  1 
ATOM   3938 C  CZ  . ARG C  1 153 ? 20.495 33.280  -34.491 1.00 40.72 ? 154 ARG C CZ  1 
ATOM   3939 N  NH1 . ARG C  1 153 ? 21.494 33.842  -33.826 1.00 38.16 ? 154 ARG C NH1 1 
ATOM   3940 N  NH2 . ARG C  1 153 ? 19.258 33.729  -34.308 1.00 38.48 ? 154 ARG C NH2 1 
ATOM   3941 N  N   . ALA C  1 154 ? 24.207 28.237  -33.281 1.00 36.65 ? 155 ALA C N   1 
ATOM   3942 C  CA  . ALA C  1 154 ? 25.366 27.552  -33.850 1.00 38.61 ? 155 ALA C CA  1 
ATOM   3943 C  C   . ALA C  1 154 ? 25.379 26.076  -33.467 1.00 38.76 ? 155 ALA C C   1 
ATOM   3944 O  O   . ALA C  1 154 ? 25.600 25.203  -34.315 1.00 35.30 ? 155 ALA C O   1 
ATOM   3945 C  CB  . ALA C  1 154 ? 26.662 28.232  -33.393 1.00 32.24 ? 155 ALA C CB  1 
ATOM   3946 N  N   . GLY C  1 155 ? 25.159 25.783  -32.186 1.00 40.84 ? 156 GLY C N   1 
ATOM   3947 C  CA  . GLY C  1 155 ? 25.318 24.445  -31.662 1.00 39.17 ? 156 GLY C CA  1 
ATOM   3948 C  C   . GLY C  1 155 ? 24.019 23.945  -31.079 1.00 42.82 ? 156 GLY C C   1 
ATOM   3949 O  O   . GLY C  1 155 ? 23.028 23.773  -31.797 1.00 42.86 ? 156 GLY C O   1 
ATOM   3950 N  N   . PRO C  1 156 ? 23.970 23.766  -29.740 1.00 39.37 ? 157 PRO C N   1 
ATOM   3951 C  CA  . PRO C  1 156 ? 25.022 24.128  -28.770 1.00 37.98 ? 157 PRO C CA  1 
ATOM   3952 C  C   . PRO C  1 156 ? 26.158 23.107  -28.539 1.00 38.85 ? 157 PRO C C   1 
ATOM   3953 O  O   . PRO C  1 156 ? 27.037 23.378  -27.724 1.00 42.56 ? 157 PRO C O   1 
ATOM   3954 C  CB  . PRO C  1 156 ? 24.234 24.315  -27.470 1.00 38.19 ? 157 PRO C CB  1 
ATOM   3955 C  CG  . PRO C  1 156 ? 23.088 23.322  -27.603 1.00 46.05 ? 157 PRO C CG  1 
ATOM   3956 C  CD  . PRO C  1 156 ? 22.724 23.327  -29.077 1.00 42.66 ? 157 PRO C CD  1 
ATOM   3957 N  N   . THR C  1 157 ? 26.160 21.972  -29.225 1.00 37.80 ? 158 THR C N   1 
ATOM   3958 C  CA  . THR C  1 157 ? 27.255 21.017  -29.115 1.00 42.48 ? 158 THR C CA  1 
ATOM   3959 C  C   . THR C  1 157 ? 27.934 20.812  -30.470 1.00 44.87 ? 158 THR C C   1 
ATOM   3960 O  O   . THR C  1 157 ? 27.471 21.291  -31.512 1.00 44.93 ? 158 THR C O   1 
ATOM   3961 C  CB  . THR C  1 157 ? 26.758 19.679  -28.548 1.00 43.11 ? 158 THR C CB  1 
ATOM   3962 O  OG1 . THR C  1 157 ? 25.892 19.042  -29.503 1.00 47.16 ? 158 THR C OG1 1 
ATOM   3963 C  CG2 . THR C  1 157 ? 26.005 19.893  -27.224 1.00 44.26 ? 158 THR C CG2 1 
ATOM   3964 N  N   . GLY C  1 158 ? 29.071 20.115  -30.438 1.00 38.46 ? 159 GLY C N   1 
ATOM   3965 C  CA  . GLY C  1 158 ? 29.745 19.711  -31.667 1.00 32.01 ? 159 GLY C CA  1 
ATOM   3966 C  C   . GLY C  1 158 ? 30.457 20.859  -32.359 1.00 36.74 ? 159 GLY C C   1 
ATOM   3967 O  O   . GLY C  1 158 ? 31.043 21.748  -31.725 1.00 33.61 ? 159 GLY C O   1 
ATOM   3968 N  N   . LEU C  1 159 ? 30.412 20.820  -33.694 1.00 36.86 ? 160 LEU C N   1 
ATOM   3969 C  CA  . LEU C  1 159 ? 31.089 21.816  -34.520 1.00 37.22 ? 160 LEU C CA  1 
ATOM   3970 C  C   . LEU C  1 159 ? 30.600 23.232  -34.209 1.00 36.67 ? 160 LEU C C   1 
ATOM   3971 O  O   . LEU C  1 159 ? 31.389 24.186  -34.219 1.00 36.79 ? 160 LEU C O   1 
ATOM   3972 C  CB  . LEU C  1 159 ? 30.884 21.471  -36.002 1.00 34.24 ? 160 LEU C CB  1 
ATOM   3973 C  CG  . LEU C  1 159 ? 31.398 22.437  -37.081 1.00 36.18 ? 160 LEU C CG  1 
ATOM   3974 C  CD1 . LEU C  1 159 ? 32.912 22.674  -36.976 1.00 37.85 ? 160 LEU C CD1 1 
ATOM   3975 C  CD2 . LEU C  1 159 ? 31.024 21.934  -38.470 1.00 36.91 ? 160 LEU C CD2 1 
ATOM   3976 N  N   . GLY C  1 160 ? 29.310 23.386  -33.911 1.00 33.66 ? 161 GLY C N   1 
ATOM   3977 C  CA  . GLY C  1 160 ? 28.803 24.697  -33.539 1.00 33.02 ? 161 GLY C CA  1 
ATOM   3978 C  C   . GLY C  1 160 ? 29.463 25.250  -32.287 1.00 37.59 ? 161 GLY C C   1 
ATOM   3979 O  O   . GLY C  1 160 ? 29.828 26.425  -32.229 1.00 36.68 ? 161 GLY C O   1 
ATOM   3980 N  N   . GLU C  1 161 ? 29.624 24.409  -31.266 1.00 35.43 ? 162 GLU C N   1 
ATOM   3981 C  CA  . GLU C  1 161 ? 30.277 24.864  -30.046 1.00 36.43 ? 162 GLU C CA  1 
ATOM   3982 C  C   . GLU C  1 161 ? 31.746 25.182  -30.309 1.00 36.06 ? 162 GLU C C   1 
ATOM   3983 O  O   . GLU C  1 161 ? 32.294 26.152  -29.764 1.00 32.48 ? 162 GLU C O   1 
ATOM   3984 C  CB  . GLU C  1 161 ? 30.124 23.798  -28.951 1.00 38.23 ? 162 GLU C CB  1 
ATOM   3985 C  CG  . GLU C  1 161 ? 30.919 24.088  -27.665 1.00 41.01 ? 162 GLU C CG  1 
ATOM   3986 C  CD  . GLU C  1 161 ? 30.725 23.017  -26.580 1.00 50.56 ? 162 GLU C CD  1 
ATOM   3987 O  OE1 . GLU C  1 161 ? 30.975 21.821  -26.876 1.00 48.66 ? 162 GLU C OE1 1 
ATOM   3988 O  OE2 . GLU C  1 161 ? 30.334 23.368  -25.435 1.00 46.20 ? 162 GLU C OE2 1 
ATOM   3989 N  N   . TYR C  1 162 ? 32.397 24.381  -31.156 1.00 36.20 ? 163 TYR C N   1 
ATOM   3990 C  CA  . TYR C  1 162 ? 33.777 24.665  -31.529 1.00 35.11 ? 163 TYR C CA  1 
ATOM   3991 C  C   . TYR C  1 162 ? 33.885 26.021  -32.233 1.00 35.82 ? 163 TYR C C   1 
ATOM   3992 O  O   . TYR C  1 162 ? 34.749 26.837  -31.895 1.00 36.54 ? 163 TYR C O   1 
ATOM   3993 C  CB  . TYR C  1 162 ? 34.326 23.516  -32.393 1.00 34.32 ? 163 TYR C CB  1 
ATOM   3994 C  CG  . TYR C  1 162 ? 35.653 23.825  -33.051 1.00 38.44 ? 163 TYR C CG  1 
ATOM   3995 C  CD1 . TYR C  1 162 ? 36.841 23.721  -32.344 1.00 36.59 ? 163 TYR C CD1 1 
ATOM   3996 C  CD2 . TYR C  1 162 ? 35.714 24.244  -34.371 1.00 37.80 ? 163 TYR C CD2 1 
ATOM   3997 C  CE1 . TYR C  1 162 ? 38.051 24.023  -32.927 1.00 35.19 ? 163 TYR C CE1 1 
ATOM   3998 C  CE2 . TYR C  1 162 ? 36.928 24.544  -34.969 1.00 40.54 ? 163 TYR C CE2 1 
ATOM   3999 C  CZ  . TYR C  1 162 ? 38.096 24.432  -34.237 1.00 40.82 ? 163 TYR C CZ  1 
ATOM   4000 O  OH  . TYR C  1 162 ? 39.314 24.740  -34.821 1.00 40.45 ? 163 TYR C OH  1 
ATOM   4001 N  N   . MET C  1 163 ? 32.984 26.295  -33.190 1.00 38.53 ? 164 MET C N   1 
ATOM   4002 C  CA  . MET C  1 163 ? 33.002 27.569  -33.920 1.00 36.76 ? 164 MET C CA  1 
ATOM   4003 C  C   . MET C  1 163 ? 32.685 28.749  -33.013 1.00 39.50 ? 164 MET C C   1 
ATOM   4004 O  O   . MET C  1 163 ? 33.364 29.780  -33.070 1.00 37.57 ? 164 MET C O   1 
ATOM   4005 C  CB  . MET C  1 163 ? 32.014 27.531  -35.091 1.00 36.07 ? 164 MET C CB  1 
ATOM   4006 C  CG  . MET C  1 163 ? 32.345 26.520  -36.181 1.00 43.56 ? 164 MET C CG  1 
ATOM   4007 S  SD  . MET C  1 163 ? 34.043 26.749  -36.779 1.00 48.38 ? 164 MET C SD  1 
ATOM   4008 C  CE  . MET C  1 163 ? 33.968 28.457  -37.339 1.00 43.67 ? 164 MET C CE  1 
ATOM   4009 N  N   . PHE C  1 164 ? 31.634 28.629  -32.189 1.00 38.29 ? 165 PHE C N   1 
ATOM   4010 C  CA  . PHE C  1 164 ? 31.261 29.724  -31.300 1.00 36.76 ? 165 PHE C CA  1 
ATOM   4011 C  C   . PHE C  1 164 ? 32.387 30.044  -30.323 1.00 37.00 ? 165 PHE C C   1 
ATOM   4012 O  O   . PHE C  1 164 ? 32.633 31.215  -30.008 1.00 40.24 ? 165 PHE C O   1 
ATOM   4013 C  CB  . PHE C  1 164 ? 29.976 29.379  -30.544 1.00 35.65 ? 165 PHE C CB  1 
ATOM   4014 C  CG  . PHE C  1 164 ? 29.595 30.407  -29.520 1.00 34.06 ? 165 PHE C CG  1 
ATOM   4015 C  CD1 . PHE C  1 164 ? 28.909 31.546  -29.890 1.00 35.77 ? 165 PHE C CD1 1 
ATOM   4016 C  CD2 . PHE C  1 164 ? 29.960 30.253  -28.192 1.00 34.43 ? 165 PHE C CD2 1 
ATOM   4017 C  CE1 . PHE C  1 164 ? 28.563 32.515  -28.944 1.00 36.48 ? 165 PHE C CE1 1 
ATOM   4018 C  CE2 . PHE C  1 164 ? 29.623 31.211  -27.247 1.00 37.40 ? 165 PHE C CE2 1 
ATOM   4019 C  CZ  . PHE C  1 164 ? 28.922 32.349  -27.628 1.00 35.39 ? 165 PHE C CZ  1 
ATOM   4020 N  N   . ASP C  1 165 ? 33.090 29.011  -29.850 1.00 36.90 ? 166 ASP C N   1 
ATOM   4021 C  CA  . ASP C  1 165 ? 34.252 29.207  -28.981 1.00 38.96 ? 166 ASP C CA  1 
ATOM   4022 C  C   . ASP C  1 165 ? 35.359 30.007  -29.661 1.00 40.48 ? 166 ASP C C   1 
ATOM   4023 O  O   . ASP C  1 165 ? 36.036 30.805  -29.005 1.00 42.64 ? 166 ASP C O   1 
ATOM   4024 C  CB  . ASP C  1 165 ? 34.784 27.851  -28.510 1.00 36.61 ? 166 ASP C CB  1 
ATOM   4025 C  CG  . ASP C  1 165 ? 35.951 27.984  -27.547 1.00 42.49 ? 166 ASP C CG  1 
ATOM   4026 O  OD1 . ASP C  1 165 ? 35.722 28.215  -26.337 1.00 43.04 ? 166 ASP C OD1 1 
ATOM   4027 O  OD2 . ASP C  1 165 ? 37.111 27.831  -28.006 1.00 44.25 ? 166 ASP C OD2 1 
ATOM   4028 N  N   . LYS C  1 166 ? 35.578 29.799  -30.967 1.00 46.26 ? 167 LYS C N   1 
ATOM   4029 C  CA  . LYS C  1 166 ? 36.626 30.554  -31.659 1.00 46.22 ? 167 LYS C CA  1 
ATOM   4030 C  C   . LYS C  1 166 ? 36.291 32.034  -31.731 1.00 49.72 ? 167 LYS C C   1 
ATOM   4031 O  O   . LYS C  1 166 ? 37.198 32.873  -31.699 1.00 54.07 ? 167 LYS C O   1 
ATOM   4032 C  CB  . LYS C  1 166 ? 36.860 30.005  -33.069 1.00 45.85 ? 167 LYS C CB  1 
ATOM   4033 C  CG  . LYS C  1 166 ? 37.221 28.529  -33.104 1.00 49.35 ? 167 LYS C CG  1 
ATOM   4034 C  CD  . LYS C  1 166 ? 37.342 28.015  -34.542 1.00 52.40 ? 167 LYS C CD  1 
ATOM   4035 C  CE  . LYS C  1 166 ? 38.785 28.054  -35.047 1.00 53.37 ? 167 LYS C CE  1 
ATOM   4036 N  NZ  . LYS C  1 166 ? 39.056 29.277  -35.859 1.00 59.82 ? 167 LYS C NZ  1 
ATOM   4037 N  N   . GLU C  1 167 ? 34.999 32.371  -31.813 1.00 51.16 ? 168 GLU C N   1 
ATOM   4038 C  CA  . GLU C  1 167 ? 34.586 33.772  -31.797 1.00 52.75 ? 168 GLU C CA  1 
ATOM   4039 C  C   . GLU C  1 167 ? 34.840 34.417  -30.442 1.00 50.21 ? 168 GLU C C   1 
ATOM   4040 O  O   . GLU C  1 167 ? 35.211 35.591  -30.375 1.00 57.61 ? 168 GLU C O   1 
ATOM   4041 C  CB  . GLU C  1 167 ? 33.106 33.890  -32.167 1.00 58.84 ? 168 GLU C CB  1 
ATOM   4042 C  CG  . GLU C  1 167 ? 32.827 34.027  -33.670 1.00 67.90 ? 168 GLU C CG  1 
ATOM   4043 C  CD  . GLU C  1 167 ? 33.854 34.888  -34.429 1.00 75.24 ? 168 GLU C CD  1 
ATOM   4044 O  OE1 . GLU C  1 167 ? 33.692 36.132  -34.444 1.00 79.77 ? 168 GLU C OE1 1 
ATOM   4045 O  OE2 . GLU C  1 167 ? 34.797 34.324  -35.041 1.00 70.07 ? 168 GLU C OE2 1 
ATOM   4046 N  N   . LEU C  1 168 ? 34.630 33.679  -29.349 1.00 45.16 ? 169 LEU C N   1 
ATOM   4047 C  CA  . LEU C  1 168 ? 34.911 34.241  -28.028 1.00 48.32 ? 169 LEU C CA  1 
ATOM   4048 C  C   . LEU C  1 168 ? 36.396 34.509  -27.834 1.00 53.41 ? 169 LEU C C   1 
ATOM   4049 O  O   . LEU C  1 168 ? 36.771 35.363  -27.022 1.00 59.23 ? 169 LEU C O   1 
ATOM   4050 C  CB  . LEU C  1 168 ? 34.435 33.296  -26.927 1.00 44.43 ? 169 LEU C CB  1 
ATOM   4051 C  CG  . LEU C  1 168 ? 32.955 33.227  -26.610 1.00 48.67 ? 169 LEU C CG  1 
ATOM   4052 C  CD1 . LEU C  1 168 ? 32.770 32.469  -25.300 1.00 42.77 ? 169 LEU C CD1 1 
ATOM   4053 C  CD2 . LEU C  1 168 ? 32.393 34.635  -26.516 1.00 42.97 ? 169 LEU C CD2 1 
ATOM   4054 N  N   . ASN C  1 169 ? 37.250 33.779  -28.547 1.00 55.78 ? 170 ASN C N   1 
ATOM   4055 C  CA  . ASN C  1 169 ? 38.686 33.826  -28.302 1.00 58.59 ? 170 ASN C CA  1 
ATOM   4056 C  C   . ASN C  1 169 ? 39.366 34.943  -29.095 1.00 69.64 ? 170 ASN C C   1 
ATOM   4057 O  O   . ASN C  1 169 ? 39.517 34.867  -30.326 1.00 70.89 ? 170 ASN C O   1 
ATOM   4058 C  CB  . ASN C  1 169 ? 39.330 32.476  -28.639 1.00 55.86 ? 170 ASN C CB  1 
ATOM   4059 C  CG  . ASN C  1 169 ? 40.646 32.259  -27.898 1.00 61.39 ? 170 ASN C CG  1 
ATOM   4060 O  OD1 . ASN C  1 169 ? 40.870 32.829  -26.821 1.00 65.85 ? 170 ASN C OD1 1 
ATOM   4061 N  ND2 . ASN C  1 169 ? 41.527 31.445  -28.475 1.00 57.55 ? 170 ASN C ND2 1 
ATOM   4062 O  OXT . ASN C  1 169 ? 39.780 35.947  -28.497 1.00 71.97 ? 170 ASN C OXT 1 
ATOM   4063 N  N   . ALA D  1 1   ? 54.009 28.792  68.295  1.00 65.94 ? 2   ALA D N   1 
ATOM   4064 C  CA  . ALA D  1 1   ? 53.922 27.650  67.389  1.00 67.00 ? 2   ALA D CA  1 
ATOM   4065 C  C   . ALA D  1 1   ? 52.471 27.399  66.976  1.00 64.56 ? 2   ALA D C   1 
ATOM   4066 O  O   . ALA D  1 1   ? 51.860 28.222  66.287  1.00 66.20 ? 2   ALA D O   1 
ATOM   4067 C  CB  . ALA D  1 1   ? 54.522 26.397  68.040  1.00 64.72 ? 2   ALA D CB  1 
ATOM   4068 N  N   . SER D  1 2   ? 51.929 26.259  67.403  1.00 53.15 ? 3   SER D N   1 
ATOM   4069 C  CA  . SER D  1 2   ? 50.569 25.867  67.059  1.00 51.76 ? 3   SER D CA  1 
ATOM   4070 C  C   . SER D  1 2   ? 49.587 26.367  68.115  1.00 46.88 ? 3   SER D C   1 
ATOM   4071 O  O   . SER D  1 2   ? 49.796 26.165  69.315  1.00 44.14 ? 3   SER D O   1 
ATOM   4072 C  CB  . SER D  1 2   ? 50.471 24.346  66.923  1.00 49.87 ? 3   SER D CB  1 
ATOM   4073 O  OG  . SER D  1 2   ? 49.226 23.964  66.362  1.00 51.16 ? 3   SER D OG  1 
ATOM   4074 N  N   . GLN D  1 3   ? 48.513 27.015  67.661  1.00 42.18 ? 4   GLN D N   1 
ATOM   4075 C  CA  . GLN D  1 3   ? 47.485 27.513  68.560  1.00 38.50 ? 4   GLN D CA  1 
ATOM   4076 C  C   . GLN D  1 3   ? 46.671 26.404  69.208  1.00 39.17 ? 4   GLN D C   1 
ATOM   4077 O  O   . GLN D  1 3   ? 45.945 26.681  70.167  1.00 39.58 ? 4   GLN D O   1 
ATOM   4078 C  CB  . GLN D  1 3   ? 46.540 28.454  67.809  1.00 39.94 ? 4   GLN D CB  1 
ATOM   4079 C  CG  . GLN D  1 3   ? 45.502 27.716  66.954  1.00 42.74 ? 4   GLN D CG  1 
ATOM   4080 C  CD  . GLN D  1 3   ? 44.789 28.632  65.956  1.00 43.70 ? 4   GLN D CD  1 
ATOM   4081 O  OE1 . GLN D  1 3   ? 44.435 29.760  66.293  1.00 40.18 ? 4   GLN D OE1 1 
ATOM   4082 N  NE2 . GLN D  1 3   ? 44.584 28.146  64.721  1.00 37.68 ? 4   GLN D NE2 1 
ATOM   4083 N  N   . VAL D  1 4   ? 46.741 25.173  68.703  1.00 36.72 ? 5   VAL D N   1 
ATOM   4084 C  CA  . VAL D  1 4   ? 45.977 24.086  69.299  1.00 34.43 ? 5   VAL D CA  1 
ATOM   4085 C  C   . VAL D  1 4   ? 46.824 23.164  70.177  1.00 37.40 ? 5   VAL D C   1 
ATOM   4086 O  O   . VAL D  1 4   ? 46.254 22.401  70.969  1.00 38.03 ? 5   VAL D O   1 
ATOM   4087 C  CB  . VAL D  1 4   ? 45.245 23.253  68.224  1.00 40.32 ? 5   VAL D CB  1 
ATOM   4088 C  CG1 . VAL D  1 4   ? 44.432 24.143  67.299  1.00 36.10 ? 5   VAL D CG1 1 
ATOM   4089 C  CG2 . VAL D  1 4   ? 46.238 22.403  67.427  1.00 40.11 ? 5   VAL D CG2 1 
ATOM   4090 N  N   . ARG D  1 5   ? 48.153 23.220  70.079  1.00 35.67 ? 6   ARG D N   1 
ATOM   4091 C  CA  . ARG D  1 5   ? 48.992 22.188  70.682  1.00 37.18 ? 6   ARG D CA  1 
ATOM   4092 C  C   . ARG D  1 5   ? 48.975 22.269  72.206  1.00 36.53 ? 6   ARG D C   1 
ATOM   4093 O  O   . ARG D  1 5   ? 49.218 23.328  72.793  1.00 35.74 ? 6   ARG D O   1 
ATOM   4094 C  CB  . ARG D  1 5   ? 50.427 22.298  70.174  1.00 35.57 ? 6   ARG D CB  1 
ATOM   4095 C  CG  . ARG D  1 5   ? 51.247 21.031  70.379  1.00 35.52 ? 6   ARG D CG  1 
ATOM   4096 C  CD  . ARG D  1 5   ? 52.713 21.302  70.109  1.00 39.89 ? 6   ARG D CD  1 
ATOM   4097 N  NE  . ARG D  1 5   ? 53.533 20.122  70.345  1.00 41.48 ? 6   ARG D NE  1 
ATOM   4098 C  CZ  . ARG D  1 5   ? 54.256 19.513  69.417  1.00 41.66 ? 6   ARG D CZ  1 
ATOM   4099 N  NH1 . ARG D  1 5   ? 54.306 19.959  68.170  1.00 35.27 ? 6   ARG D NH1 1 
ATOM   4100 N  NH2 . ARG D  1 5   ? 54.950 18.429  69.747  1.00 40.15 ? 6   ARG D NH2 1 
ATOM   4101 N  N   . GLN D  1 6   ? 48.717 21.137  72.850  1.00 31.61 ? 7   GLN D N   1 
ATOM   4102 C  CA  . GLN D  1 6   ? 48.690 21.111  74.308  1.00 36.71 ? 7   GLN D CA  1 
ATOM   4103 C  C   . GLN D  1 6   ? 49.054 19.715  74.781  1.00 33.51 ? 7   GLN D C   1 
ATOM   4104 O  O   . GLN D  1 6   ? 48.439 18.732  74.348  1.00 32.99 ? 7   GLN D O   1 
ATOM   4105 C  CB  . GLN D  1 6   ? 47.309 21.528  74.848  1.00 37.30 ? 7   GLN D CB  1 
ATOM   4106 C  CG  . GLN D  1 6   ? 47.302 21.924  76.324  1.00 36.72 ? 7   GLN D CG  1 
ATOM   4107 C  CD  . GLN D  1 6   ? 45.938 22.443  76.798  1.00 45.04 ? 7   GLN D CD  1 
ATOM   4108 O  OE1 . GLN D  1 6   ? 44.914 22.242  76.138  1.00 41.96 ? 7   GLN D OE1 1 
ATOM   4109 N  NE2 . GLN D  1 6   ? 45.921 23.095  77.955  1.00 43.14 ? 7   GLN D NE2 1 
ATOM   4110 N  N   . ASN D  1 7   ? 50.062 19.630  75.650  1.00 32.82 ? 8   ASN D N   1 
ATOM   4111 C  CA  . ASN D  1 7   ? 50.452 18.361  76.265  1.00 35.16 ? 8   ASN D CA  1 
ATOM   4112 C  C   . ASN D  1 7   ? 50.892 17.334  75.223  1.00 34.55 ? 8   ASN D C   1 
ATOM   4113 O  O   . ASN D  1 7   ? 50.678 16.134  75.402  1.00 35.27 ? 8   ASN D O   1 
ATOM   4114 C  CB  . ASN D  1 7   ? 49.318 17.782  77.125  1.00 32.90 ? 8   ASN D CB  1 
ATOM   4115 C  CG  . ASN D  1 7   ? 49.799 16.689  78.074  1.00 35.72 ? 8   ASN D CG  1 
ATOM   4116 O  OD1 . ASN D  1 7   ? 50.861 16.815  78.686  1.00 34.64 ? 8   ASN D OD1 1 
ATOM   4117 N  ND2 . ASN D  1 7   ? 49.028 15.601  78.183  1.00 32.33 ? 8   ASN D ND2 1 
ATOM   4118 N  N   . TYR D  1 8   ? 51.510 17.791  74.129  1.00 34.64 ? 9   TYR D N   1 
ATOM   4119 C  CA  . TYR D  1 8   ? 51.899 16.923  73.015  1.00 35.58 ? 9   TYR D CA  1 
ATOM   4120 C  C   . TYR D  1 8   ? 53.416 16.974  72.876  1.00 36.76 ? 9   TYR D C   1 
ATOM   4121 O  O   . TYR D  1 8   ? 53.964 17.951  72.360  1.00 38.92 ? 9   TYR D O   1 
ATOM   4122 C  CB  . TYR D  1 8   ? 51.202 17.354  71.729  1.00 37.76 ? 9   TYR D CB  1 
ATOM   4123 C  CG  . TYR D  1 8   ? 51.235 16.335  70.619  1.00 32.98 ? 9   TYR D CG  1 
ATOM   4124 C  CD1 . TYR D  1 8   ? 50.883 15.017  70.846  1.00 33.77 ? 9   TYR D CD1 1 
ATOM   4125 C  CD2 . TYR D  1 8   ? 51.625 16.695  69.340  1.00 34.79 ? 9   TYR D CD2 1 
ATOM   4126 C  CE1 . TYR D  1 8   ? 50.910 14.086  69.821  1.00 35.56 ? 9   TYR D CE1 1 
ATOM   4127 C  CE2 . TYR D  1 8   ? 51.658 15.771  68.312  1.00 31.27 ? 9   TYR D CE2 1 
ATOM   4128 C  CZ  . TYR D  1 8   ? 51.301 14.471  68.558  1.00 35.05 ? 9   TYR D CZ  1 
ATOM   4129 O  OH  . TYR D  1 8   ? 51.333 13.545  67.533  1.00 37.73 ? 9   TYR D OH  1 
ATOM   4130 N  N   . HIS D  1 9   ? 54.084 15.913  73.326  1.00 38.67 ? 10  HIS D N   1 
ATOM   4131 C  CA  . HIS D  1 9   ? 55.540 15.861  73.384  1.00 40.86 ? 10  HIS D CA  1 
ATOM   4132 C  C   . HIS D  1 9   ? 56.133 15.637  71.990  1.00 42.54 ? 10  HIS D C   1 
ATOM   4133 O  O   . HIS D  1 9   ? 55.568 14.915  71.164  1.00 40.27 ? 10  HIS D O   1 
ATOM   4134 C  CB  . HIS D  1 9   ? 55.963 14.746  74.354  1.00 44.48 ? 10  HIS D CB  1 
ATOM   4135 C  CG  . HIS D  1 9   ? 57.403 14.803  74.778  1.00 53.35 ? 10  HIS D CG  1 
ATOM   4136 N  ND1 . HIS D  1 9   ? 58.455 14.651  73.897  1.00 53.23 ? 10  HIS D ND1 1 
ATOM   4137 C  CD2 . HIS D  1 9   ? 57.961 15.002  75.996  1.00 50.41 ? 10  HIS D CD2 1 
ATOM   4138 C  CE1 . HIS D  1 9   ? 59.598 14.751  74.551  1.00 53.34 ? 10  HIS D CE1 1 
ATOM   4139 N  NE2 . HIS D  1 9   ? 59.327 14.965  75.826  1.00 58.96 ? 10  HIS D NE2 1 
ATOM   4140 N  N   . GLU D  1 10  ? 57.282 16.269  71.731  1.00 42.01 ? 11  GLU D N   1 
ATOM   4141 C  CA  . GLU D  1 10  ? 57.956 16.115  70.441  1.00 46.99 ? 11  GLU D CA  1 
ATOM   4142 C  C   . GLU D  1 10  ? 58.295 14.653  70.144  1.00 44.83 ? 11  GLU D C   1 
ATOM   4143 O  O   . GLU D  1 10  ? 58.365 14.253  68.974  1.00 39.90 ? 11  GLU D O   1 
ATOM   4144 C  CB  . GLU D  1 10  ? 59.222 16.977  70.423  1.00 48.71 ? 11  GLU D CB  1 
ATOM   4145 C  CG  . GLU D  1 10  ? 60.016 16.874  71.742  1.00 60.79 ? 11  GLU D CG  1 
ATOM   4146 C  CD  . GLU D  1 10  ? 61.535 17.046  71.583  1.00 68.93 ? 11  GLU D CD  1 
ATOM   4147 O  OE1 . GLU D  1 10  ? 61.979 17.680  70.595  1.00 63.77 ? 11  GLU D OE1 1 
ATOM   4148 O  OE2 . GLU D  1 10  ? 62.279 16.531  72.463  1.00 68.15 ? 11  GLU D OE2 1 
ATOM   4149 N  N   . ASP D  1 11  ? 58.503 13.841  71.183  1.00 38.81 ? 12  ASP D N   1 
ATOM   4150 C  CA  . ASP D  1 11  ? 58.796 12.427  70.978  1.00 47.91 ? 12  ASP D CA  1 
ATOM   4151 C  C   . ASP D  1 11  ? 57.579 11.679  70.443  1.00 43.41 ? 12  ASP D C   1 
ATOM   4152 O  O   . ASP D  1 11  ? 57.713 10.797  69.586  1.00 41.17 ? 12  ASP D O   1 
ATOM   4153 C  CB  . ASP D  1 11  ? 59.287 11.800  72.285  1.00 50.11 ? 12  ASP D CB  1 
ATOM   4154 C  CG  . ASP D  1 11  ? 60.722 12.213  72.633  1.00 61.15 ? 12  ASP D CG  1 
ATOM   4155 O  OD1 . ASP D  1 11  ? 61.356 12.960  71.840  1.00 58.35 ? 12  ASP D OD1 1 
ATOM   4156 O  OD2 . ASP D  1 11  ? 61.212 11.789  73.706  1.00 63.89 ? 12  ASP D OD2 1 
ATOM   4157 N  N   . ALA D  1 12  ? 56.384 12.012  70.939  1.00 41.66 ? 13  ALA D N   1 
ATOM   4158 C  CA  . ALA D  1 12  ? 55.169 11.406  70.404  1.00 38.61 ? 13  ALA D CA  1 
ATOM   4159 C  C   . ALA D  1 12  ? 54.943 11.830  68.959  1.00 37.44 ? 13  ALA D C   1 
ATOM   4160 O  O   . ALA D  1 12  ? 54.563 11.010  68.112  1.00 34.91 ? 13  ALA D O   1 
ATOM   4161 C  CB  . ALA D  1 12  ? 53.962 11.781  71.264  1.00 34.25 ? 13  ALA D CB  1 
ATOM   4162 N  N   . GLU D  1 13  ? 55.191 13.105  68.655  1.00 34.78 ? 14  GLU D N   1 
ATOM   4163 C  CA  . GLU D  1 13  ? 54.983 13.585  67.295  1.00 35.40 ? 14  GLU D CA  1 
ATOM   4164 C  C   . GLU D  1 13  ? 55.888 12.848  66.310  1.00 37.73 ? 14  GLU D C   1 
ATOM   4165 O  O   . GLU D  1 13  ? 55.436 12.443  65.230  1.00 32.48 ? 14  GLU D O   1 
ATOM   4166 C  CB  . GLU D  1 13  ? 55.195 15.096  67.249  1.00 33.09 ? 14  GLU D CB  1 
ATOM   4167 C  CG  . GLU D  1 13  ? 55.263 15.705  65.863  1.00 37.99 ? 14  GLU D CG  1 
ATOM   4168 C  CD  . GLU D  1 13  ? 55.641 17.189  65.879  1.00 42.71 ? 14  GLU D CD  1 
ATOM   4169 O  OE1 . GLU D  1 13  ? 56.071 17.698  66.950  1.00 42.69 ? 14  GLU D OE1 1 
ATOM   4170 O  OE2 . GLU D  1 13  ? 55.494 17.851  64.817  1.00 41.64 ? 14  GLU D OE2 1 
ATOM   4171 N  N   . ALA D  1 14  ? 57.152 12.605  66.693  1.00 34.86 ? 15  ALA D N   1 
ATOM   4172 C  CA  . ALA D  1 14  ? 58.073 11.877  65.819  1.00 36.08 ? 15  ALA D CA  1 
ATOM   4173 C  C   . ALA D  1 14  ? 57.681 10.414  65.694  1.00 34.55 ? 15  ALA D C   1 
ATOM   4174 O  O   . ALA D  1 14  ? 57.827 9.817   64.625  1.00 36.28 ? 15  ALA D O   1 
ATOM   4175 C  CB  . ALA D  1 14  ? 59.507 11.974  66.340  1.00 34.98 ? 15  ALA D CB  1 
ATOM   4176 N  N   . SER D  1 15  ? 57.217 9.810   66.785  1.00 35.60 ? 16  SER D N   1 
ATOM   4177 C  CA  . SER D  1 15  ? 56.832 8.406   66.733  1.00 36.21 ? 16  SER D CA  1 
ATOM   4178 C  C   . SER D  1 15  ? 55.597 8.208   65.863  1.00 35.37 ? 16  SER D C   1 
ATOM   4179 O  O   . SER D  1 15  ? 55.485 7.196   65.164  1.00 35.51 ? 16  SER D O   1 
ATOM   4180 C  CB  . SER D  1 15  ? 56.589 7.879   68.143  1.00 37.17 ? 16  SER D CB  1 
ATOM   4181 O  OG  . SER D  1 15  ? 57.799 7.784   68.873  1.00 48.41 ? 16  SER D OG  1 
ATOM   4182 N  N   . ILE D  1 16  ? 54.660 9.165   65.895  1.00 35.00 ? 17  ILE D N   1 
ATOM   4183 C  CA  . ILE D  1 16  ? 53.496 9.102   65.013  1.00 34.72 ? 17  ILE D CA  1 
ATOM   4184 C  C   . ILE D  1 16  ? 53.919 9.159   63.543  1.00 33.00 ? 17  ILE D C   1 
ATOM   4185 O  O   . ILE D  1 16  ? 53.399 8.402   62.711  1.00 34.20 ? 17  ILE D O   1 
ATOM   4186 C  CB  . ILE D  1 16  ? 52.495 10.218  65.350  1.00 29.99 ? 17  ILE D CB  1 
ATOM   4187 C  CG1 . ILE D  1 16  ? 51.903 10.015  66.748  1.00 36.50 ? 17  ILE D CG1 1 
ATOM   4188 C  CG2 . ILE D  1 16  ? 51.380 10.258  64.304  1.00 31.08 ? 17  ILE D CG2 1 
ATOM   4189 C  CD1 . ILE D  1 16  ? 50.900 8.913   66.826  1.00 39.88 ? 17  ILE D CD1 1 
ATOM   4190 N  N   . ASN D  1 17  ? 54.858 10.048  63.192  1.00 26.28 ? 18  ASN D N   1 
ATOM   4191 C  CA  . ASN D  1 17  ? 55.332 10.087  61.807  1.00 32.78 ? 18  ASN D CA  1 
ATOM   4192 C  C   . ASN D  1 17  ? 55.926 8.744   61.388  1.00 33.28 ? 18  ASN D C   1 
ATOM   4193 O  O   . ASN D  1 17  ? 55.712 8.290   60.257  1.00 28.84 ? 18  ASN D O   1 
ATOM   4194 C  CB  . ASN D  1 17  ? 56.352 11.212  61.608  1.00 27.92 ? 18  ASN D CB  1 
ATOM   4195 C  CG  . ASN D  1 17  ? 55.694 12.578  61.505  1.00 34.50 ? 18  ASN D CG  1 
ATOM   4196 O  OD1 . ASN D  1 17  ? 54.599 12.699  60.981  1.00 34.69 ? 18  ASN D OD1 1 
ATOM   4197 N  ND2 . ASN D  1 17  ? 56.345 13.605  62.037  1.00 35.45 ? 18  ASN D ND2 1 
ATOM   4198 N  N   . LYS D  1 18  ? 56.646 8.078   62.300  1.00 29.61 ? 19  LYS D N   1 
ATOM   4199 C  CA  . LYS D  1 18  ? 57.224 6.777   61.986  1.00 32.26 ? 19  LYS D CA  1 
ATOM   4200 C  C   . LYS D  1 18  ? 56.148 5.706   61.864  1.00 33.67 ? 19  LYS D C   1 
ATOM   4201 O  O   . LYS D  1 18  ? 56.254 4.801   61.032  1.00 36.21 ? 19  LYS D O   1 
ATOM   4202 C  CB  . LYS D  1 18  ? 58.253 6.390   63.053  1.00 39.66 ? 19  LYS D CB  1 
ATOM   4203 C  CG  . LYS D  1 18  ? 59.058 5.147   62.715  1.00 46.17 ? 19  LYS D CG  1 
ATOM   4204 C  CD  . LYS D  1 18  ? 59.494 5.134   61.229  1.00 57.12 ? 19  LYS D CD  1 
ATOM   4205 C  CE  . LYS D  1 18  ? 60.473 3.995   60.908  1.00 60.27 ? 19  LYS D CE  1 
ATOM   4206 N  NZ  . LYS D  1 18  ? 61.828 4.505   60.467  1.00 59.34 ? 19  LYS D NZ  1 
ATOM   4207 N  N   . GLN D  1 19  ? 55.109 5.786   62.689  1.00 33.14 ? 20  GLN D N   1 
ATOM   4208 C  CA  . GLN D  1 19  ? 54.031 4.808   62.618  1.00 33.25 ? 20  GLN D CA  1 
ATOM   4209 C  C   . GLN D  1 19  ? 53.218 4.968   61.327  1.00 33.48 ? 20  GLN D C   1 
ATOM   4210 O  O   . GLN D  1 19  ? 52.775 3.972   60.747  1.00 30.70 ? 20  GLN D O   1 
ATOM   4211 C  CB  . GLN D  1 19  ? 53.160 4.951   63.872  1.00 34.54 ? 20  GLN D CB  1 
ATOM   4212 C  CG  . GLN D  1 19  ? 52.451 3.690   64.309  1.00 39.39 ? 20  GLN D CG  1 
ATOM   4213 C  CD  . GLN D  1 19  ? 53.404 2.552   64.587  1.00 41.30 ? 20  GLN D CD  1 
ATOM   4214 O  OE1 . GLN D  1 19  ? 53.143 1.413   64.200  1.00 47.98 ? 20  GLN D OE1 1 
ATOM   4215 N  NE2 . GLN D  1 19  ? 54.526 2.851   65.243  1.00 38.79 ? 20  GLN D NE2 1 
ATOM   4216 N  N   . ILE D  1 20  ? 53.048 6.210   60.852  1.00 31.76 ? 21  ILE D N   1 
ATOM   4217 C  CA  . ILE D  1 20  ? 52.413 6.460   59.555  1.00 30.44 ? 21  ILE D CA  1 
ATOM   4218 C  C   . ILE D  1 20  ? 53.169 5.744   58.443  1.00 32.43 ? 21  ILE D C   1 
ATOM   4219 O  O   . ILE D  1 20  ? 52.571 5.084   57.584  1.00 30.96 ? 21  ILE D O   1 
ATOM   4220 C  CB  . ILE D  1 20  ? 52.336 7.974   59.279  1.00 30.79 ? 21  ILE D CB  1 
ATOM   4221 C  CG1 . ILE D  1 20  ? 51.165 8.623   60.038  1.00 30.06 ? 21  ILE D CG1 1 
ATOM   4222 C  CG2 . ILE D  1 20  ? 52.226 8.253   57.787  1.00 26.63 ? 21  ILE D CG2 1 
ATOM   4223 C  CD1 . ILE D  1 20  ? 51.412 10.088  60.368  1.00 27.61 ? 21  ILE D CD1 1 
ATOM   4224 N  N   . ASN D  1 21  ? 54.502 5.869   58.441  1.00 31.50 ? 22  ASN D N   1 
ATOM   4225 C  CA  . ASN D  1 21  ? 55.300 5.196   57.422  1.00 31.15 ? 22  ASN D CA  1 
ATOM   4226 C  C   . ASN D  1 21  ? 55.139 3.684   57.496  1.00 33.12 ? 22  ASN D C   1 
ATOM   4227 O  O   . ASN D  1 21  ? 55.054 3.012   56.463  1.00 33.68 ? 22  ASN D O   1 
ATOM   4228 C  CB  . ASN D  1 21  ? 56.771 5.569   57.566  1.00 33.27 ? 22  ASN D CB  1 
ATOM   4229 C  CG  . ASN D  1 21  ? 57.565 5.229   56.330  1.00 32.80 ? 22  ASN D CG  1 
ATOM   4230 O  OD1 . ASN D  1 21  ? 58.222 4.198   56.266  1.00 33.22 ? 22  ASN D OD1 1 
ATOM   4231 N  ND2 . ASN D  1 21  ? 57.480 6.084   55.322  1.00 31.00 ? 22  ASN D ND2 1 
ATOM   4232 N  N   . MET D  1 22  ? 55.093 3.133   58.712  1.00 31.33 ? 23  MET D N   1 
ATOM   4233 C  CA  . MET D  1 22  ? 55.031 1.683   58.883  1.00 33.46 ? 23  MET D CA  1 
ATOM   4234 C  C   . MET D  1 22  ? 53.750 1.097   58.295  1.00 32.67 ? 23  MET D C   1 
ATOM   4235 O  O   . MET D  1 22  ? 53.782 0.043   57.651  1.00 27.83 ? 23  MET D O   1 
ATOM   4236 C  CB  . MET D  1 22  ? 55.123 1.338   60.367  1.00 38.78 ? 23  MET D CB  1 
ATOM   4237 C  CG  . MET D  1 22  ? 55.697 -0.018  60.647  1.00 47.86 ? 23  MET D CG  1 
ATOM   4238 S  SD  . MET D  1 22  ? 56.226 -0.148  62.369  1.00 59.53 ? 23  MET D SD  1 
ATOM   4239 C  CE  . MET D  1 22  ? 56.898 -1.819  62.325  1.00 43.30 ? 23  MET D CE  1 
ATOM   4240 N  N   . CYS D  1 23  ? 52.609 1.759   58.524  1.00 28.88 ? 24  CYS D N   1 
ATOM   4241 C  CA  . CYS D  1 23  ? 51.350 1.272   57.971  1.00 32.66 ? 24  CYS D CA  1 
ATOM   4242 C  C   . CYS D  1 23  ? 51.261 1.508   56.463  1.00 30.97 ? 24  CYS D C   1 
ATOM   4243 O  O   . CYS D  1 23  ? 50.669 0.693   55.744  1.00 31.70 ? 24  CYS D O   1 
ATOM   4244 C  CB  . CYS D  1 23  ? 50.177 1.919   58.716  1.00 35.06 ? 24  CYS D CB  1 
ATOM   4245 S  SG  . CYS D  1 23  ? 49.893 1.165   60.382  1.00 48.59 ? 24  CYS D SG  1 
ATOM   4246 N  N   . LEU D  1 24  ? 51.855 2.588   55.953  1.00 28.16 ? 25  LEU D N   1 
ATOM   4247 C  CA  . LEU D  1 24  ? 51.918 2.736   54.506  1.00 29.60 ? 25  LEU D CA  1 
ATOM   4248 C  C   . LEU D  1 24  ? 52.731 1.606   53.900  1.00 27.94 ? 25  LEU D C   1 
ATOM   4249 O  O   . LEU D  1 24  ? 52.334 1.020   52.890  1.00 28.31 ? 25  LEU D O   1 
ATOM   4250 C  CB  . LEU D  1 24  ? 52.514 4.086   54.121  1.00 27.98 ? 25  LEU D CB  1 
ATOM   4251 C  CG  . LEU D  1 24  ? 51.639 5.304   54.395  1.00 31.49 ? 25  LEU D CG  1 
ATOM   4252 C  CD1 . LEU D  1 24  ? 52.395 6.585   54.084  1.00 29.99 ? 25  LEU D CD1 1 
ATOM   4253 C  CD2 . LEU D  1 24  ? 50.388 5.227   53.572  1.00 32.73 ? 25  LEU D CD2 1 
ATOM   4254 N  N   . TYR D  1 25  ? 53.848 1.251   54.541  1.00 27.62 ? 26  TYR D N   1 
ATOM   4255 C  CA  . TYR D  1 25  ? 54.674 0.161   54.039  1.00 30.71 ? 26  TYR D CA  1 
ATOM   4256 C  C   . TYR D  1 25  ? 53.908 -1.159  54.053  1.00 28.93 ? 26  TYR D C   1 
ATOM   4257 O  O   . TYR D  1 25  ? 53.916 -1.899  53.063  1.00 26.65 ? 26  TYR D O   1 
ATOM   4258 C  CB  . TYR D  1 25  ? 55.962 0.052   54.856  1.00 29.23 ? 26  TYR D CB  1 
ATOM   4259 C  CG  . TYR D  1 25  ? 56.729 -1.200  54.540  1.00 30.97 ? 26  TYR D CG  1 
ATOM   4260 C  CD1 . TYR D  1 25  ? 57.417 -1.325  53.341  1.00 27.19 ? 26  TYR D CD1 1 
ATOM   4261 C  CD2 . TYR D  1 25  ? 56.758 -2.267  55.438  1.00 32.42 ? 26  TYR D CD2 1 
ATOM   4262 C  CE1 . TYR D  1 25  ? 58.107 -2.477  53.037  1.00 30.12 ? 26  TYR D CE1 1 
ATOM   4263 C  CE2 . TYR D  1 25  ? 57.459 -3.428  55.151  1.00 31.38 ? 26  TYR D CE2 1 
ATOM   4264 C  CZ  . TYR D  1 25  ? 58.130 -3.526  53.948  1.00 34.86 ? 26  TYR D CZ  1 
ATOM   4265 O  OH  . TYR D  1 25  ? 58.817 -4.677  53.641  1.00 37.46 ? 26  TYR D OH  1 
ATOM   4266 N  N   . ALA D  1 26  ? 53.224 -1.459  55.167  1.00 27.68 ? 27  ALA D N   1 
ATOM   4267 C  CA  . ALA D  1 26  ? 52.436 -2.688  55.256  1.00 29.43 ? 27  ALA D CA  1 
ATOM   4268 C  C   . ALA D  1 26  ? 51.315 -2.705  54.223  1.00 26.48 ? 27  ALA D C   1 
ATOM   4269 O  O   . ALA D  1 26  ? 51.021 -3.747  53.634  1.00 30.51 ? 27  ALA D O   1 
ATOM   4270 C  CB  . ALA D  1 26  ? 51.857 -2.845  56.664  1.00 30.77 ? 27  ALA D CB  1 
ATOM   4271 N  N   . SER D  1 27  ? 50.676 -1.560  53.997  1.00 28.51 ? 28  SER D N   1 
ATOM   4272 C  CA  . SER D  1 27  ? 49.698 -1.458  52.922  1.00 29.52 ? 28  SER D CA  1 
ATOM   4273 C  C   . SER D  1 27  ? 50.323 -1.818  51.581  1.00 32.08 ? 28  SER D C   1 
ATOM   4274 O  O   . SER D  1 27  ? 49.704 -2.491  50.748  1.00 28.52 ? 28  SER D O   1 
ATOM   4275 C  CB  . SER D  1 27  ? 49.137 -0.037  52.886  1.00 31.67 ? 28  SER D CB  1 
ATOM   4276 O  OG  . SER D  1 27  ? 48.121 0.086   51.920  1.00 34.26 ? 28  SER D OG  1 
ATOM   4277 N  N   . TYR D  1 28  ? 51.550 -1.354  51.351  1.00 29.08 ? 29  TYR D N   1 
ATOM   4278 C  CA  . TYR D  1 28  ? 52.231 -1.625  50.096  1.00 27.90 ? 29  TYR D CA  1 
ATOM   4279 C  C   . TYR D  1 28  ? 52.539 -3.111  49.967  1.00 28.31 ? 29  TYR D C   1 
ATOM   4280 O  O   . TYR D  1 28  ? 52.331 -3.707  48.903  1.00 27.62 ? 29  TYR D O   1 
ATOM   4281 C  CB  . TYR D  1 28  ? 53.495 -0.762  50.032  1.00 30.17 ? 29  TYR D CB  1 
ATOM   4282 C  CG  . TYR D  1 28  ? 54.071 -0.497  48.660  1.00 28.00 ? 29  TYR D CG  1 
ATOM   4283 C  CD1 . TYR D  1 28  ? 53.301 -0.615  47.505  1.00 28.64 ? 29  TYR D CD1 1 
ATOM   4284 C  CD2 . TYR D  1 28  ? 55.394 -0.120  48.526  1.00 24.78 ? 29  TYR D CD2 1 
ATOM   4285 C  CE1 . TYR D  1 28  ? 53.858 -0.365  46.243  1.00 25.32 ? 29  TYR D CE1 1 
ATOM   4286 C  CE2 . TYR D  1 28  ? 55.950 0.137   47.294  1.00 26.78 ? 29  TYR D CE2 1 
ATOM   4287 C  CZ  . TYR D  1 28  ? 55.185 0.014   46.152  1.00 29.38 ? 29  TYR D CZ  1 
ATOM   4288 O  OH  . TYR D  1 28  ? 55.777 0.260   44.927  1.00 27.79 ? 29  TYR D OH  1 
ATOM   4289 N  N   . VAL D  1 29  ? 52.977 -3.736  51.067  1.00 29.10 ? 30  VAL D N   1 
ATOM   4290 C  CA  . VAL D  1 29  ? 53.284 -5.162  51.065  1.00 27.56 ? 30  VAL D CA  1 
ATOM   4291 C  C   . VAL D  1 29  ? 52.044 -5.976  50.713  1.00 30.61 ? 30  VAL D C   1 
ATOM   4292 O  O   . VAL D  1 29  ? 52.102 -6.903  49.901  1.00 30.29 ? 30  VAL D O   1 
ATOM   4293 C  CB  . VAL D  1 29  ? 53.871 -5.574  52.432  1.00 31.48 ? 30  VAL D CB  1 
ATOM   4294 C  CG1 . VAL D  1 29  ? 53.906 -7.079  52.565  1.00 28.94 ? 30  VAL D CG1 1 
ATOM   4295 C  CG2 . VAL D  1 29  ? 55.284 -4.969  52.618  1.00 30.83 ? 30  VAL D CG2 1 
ATOM   4296 N  N   . TYR D  1 30  ? 50.902 -5.632  51.309  1.00 30.57 ? 31  TYR D N   1 
ATOM   4297 C  CA  . TYR D  1 30  ? 49.671 -6.364  51.045  1.00 26.88 ? 31  TYR D CA  1 
ATOM   4298 C  C   . TYR D  1 30  ? 49.223 -6.185  49.608  1.00 29.31 ? 31  TYR D C   1 
ATOM   4299 O  O   . TYR D  1 30  ? 48.682 -7.120  49.001  1.00 33.01 ? 31  TYR D O   1 
ATOM   4300 C  CB  . TYR D  1 30  ? 48.574 -5.888  51.991  1.00 27.48 ? 31  TYR D CB  1 
ATOM   4301 C  CG  . TYR D  1 30  ? 48.781 -6.371  53.387  1.00 33.46 ? 31  TYR D CG  1 
ATOM   4302 C  CD1 . TYR D  1 30  ? 49.145 -7.692  53.621  1.00 36.14 ? 31  TYR D CD1 1 
ATOM   4303 C  CD2 . TYR D  1 30  ? 48.634 -5.521  54.472  1.00 31.87 ? 31  TYR D CD2 1 
ATOM   4304 C  CE1 . TYR D  1 30  ? 49.340 -8.161  54.890  1.00 40.51 ? 31  TYR D CE1 1 
ATOM   4305 C  CE2 . TYR D  1 30  ? 48.844 -5.980  55.758  1.00 38.11 ? 31  TYR D CE2 1 
ATOM   4306 C  CZ  . TYR D  1 30  ? 49.192 -7.304  55.957  1.00 42.10 ? 31  TYR D CZ  1 
ATOM   4307 O  OH  . TYR D  1 30  ? 49.394 -7.794  57.221  1.00 47.24 ? 31  TYR D OH  1 
ATOM   4308 N  N   . LEU D  1 31  ? 49.400 -4.979  49.062  1.00 26.71 ? 32  LEU D N   1 
ATOM   4309 C  CA  . LEU D  1 31  ? 49.087 -4.747  47.655  1.00 28.24 ? 32  LEU D CA  1 
ATOM   4310 C  C   . LEU D  1 31  ? 49.913 -5.664  46.766  1.00 26.82 ? 32  LEU D C   1 
ATOM   4311 O  O   . LEU D  1 31  ? 49.393 -6.289  45.836  1.00 30.43 ? 32  LEU D O   1 
ATOM   4312 C  CB  . LEU D  1 31  ? 49.325 -3.278  47.300  1.00 25.80 ? 32  LEU D CB  1 
ATOM   4313 C  CG  . LEU D  1 31  ? 48.819 -2.854  45.915  1.00 36.37 ? 32  LEU D CG  1 
ATOM   4314 C  CD1 . LEU D  1 31  ? 47.287 -2.857  45.865  1.00 41.17 ? 32  LEU D CD1 1 
ATOM   4315 C  CD2 . LEU D  1 31  ? 49.351 -1.478  45.563  1.00 36.14 ? 32  LEU D CD2 1 
ATOM   4316 N  N   . SER D  1 32  ? 51.208 -5.766  47.059  1.00 28.36 ? 33  SER D N   1 
ATOM   4317 C  CA  . SER D  1 32  ? 52.079 -6.680  46.333  1.00 32.36 ? 33  SER D CA  1 
ATOM   4318 C  C   . SER D  1 32  ? 51.549 -8.110  46.379  1.00 31.67 ? 33  SER D C   1 
ATOM   4319 O  O   . SER D  1 32  ? 51.422 -8.767  45.340  1.00 28.95 ? 33  SER D O   1 
ATOM   4320 C  CB  . SER D  1 32  ? 53.488 -6.621  46.918  1.00 30.06 ? 33  SER D CB  1 
ATOM   4321 O  OG  . SER D  1 32  ? 54.292 -7.602  46.302  1.00 35.69 ? 33  SER D OG  1 
ATOM   4322 N  N   . MET D  1 33  ? 51.235 -8.609  47.585  1.00 30.32 ? 34  MET D N   1 
ATOM   4323 C  CA  . MET D  1 33  ? 50.738 -9.977  47.722  1.00 31.74 ? 34  MET D CA  1 
ATOM   4324 C  C   . MET D  1 33  ? 49.437 -10.176 46.958  1.00 30.77 ? 34  MET D C   1 
ATOM   4325 O  O   . MET D  1 33  ? 49.243 -11.211 46.313  1.00 30.14 ? 34  MET D O   1 
ATOM   4326 C  CB  . MET D  1 33  ? 50.530 -10.332 49.195  1.00 29.24 ? 34  MET D CB  1 
ATOM   4327 C  CG  . MET D  1 33  ? 51.764 -10.222 50.076  1.00 31.52 ? 34  MET D CG  1 
ATOM   4328 S  SD  . MET D  1 33  ? 51.337 -10.768 51.764  1.00 40.27 ? 34  MET D SD  1 
ATOM   4329 C  CE  . MET D  1 33  ? 52.935 -10.831 52.587  1.00 36.54 ? 34  MET D CE  1 
ATOM   4330 N  N   . ALA D  1 34  ? 48.534 -9.195  47.026  1.00 28.92 ? 35  ALA D N   1 
ATOM   4331 C  CA  . ALA D  1 34  ? 47.241 -9.319  46.363  1.00 29.45 ? 35  ALA D CA  1 
ATOM   4332 C  C   . ALA D  1 34  ? 47.417 -9.516  44.866  1.00 33.53 ? 35  ALA D C   1 
ATOM   4333 O  O   . ALA D  1 34  ? 46.808 -10.410 44.266  1.00 34.94 ? 35  ALA D O   1 
ATOM   4334 C  CB  . ALA D  1 34  ? 46.385 -8.083  46.641  1.00 26.35 ? 35  ALA D CB  1 
ATOM   4335 N  N   . TYR D  1 35  ? 48.257 -8.700  44.241  1.00 32.77 ? 36  TYR D N   1 
ATOM   4336 C  CA  . TYR D  1 35  ? 48.413 -8.849  42.803  1.00 30.18 ? 36  TYR D CA  1 
ATOM   4337 C  C   . TYR D  1 35  ? 49.281 -10.040 42.440  1.00 29.17 ? 36  TYR D C   1 
ATOM   4338 O  O   . TYR D  1 35  ? 49.166 -10.549 41.323  1.00 34.78 ? 36  TYR D O   1 
ATOM   4339 C  CB  . TYR D  1 35  ? 48.943 -7.551  42.194  1.00 30.60 ? 36  TYR D CB  1 
ATOM   4340 C  CG  . TYR D  1 35  ? 47.800 -6.584  42.008  1.00 31.21 ? 36  TYR D CG  1 
ATOM   4341 C  CD1 . TYR D  1 35  ? 47.439 -5.719  43.023  1.00 32.19 ? 36  TYR D CD1 1 
ATOM   4342 C  CD2 . TYR D  1 35  ? 47.028 -6.600  40.852  1.00 34.49 ? 36  TYR D CD2 1 
ATOM   4343 C  CE1 . TYR D  1 35  ? 46.380 -4.856  42.882  1.00 38.58 ? 36  TYR D CE1 1 
ATOM   4344 C  CE2 . TYR D  1 35  ? 45.957 -5.743  40.700  1.00 36.21 ? 36  TYR D CE2 1 
ATOM   4345 C  CZ  . TYR D  1 35  ? 45.640 -4.870  41.724  1.00 37.05 ? 36  TYR D CZ  1 
ATOM   4346 O  OH  . TYR D  1 35  ? 44.577 -4.005  41.604  1.00 45.92 ? 36  TYR D OH  1 
ATOM   4347 N  N   . TYR D  1 36  ? 50.112 -10.520 43.366  1.00 30.86 ? 37  TYR D N   1 
ATOM   4348 C  CA  . TYR D  1 36  ? 50.859 -11.740 43.100  1.00 29.17 ? 37  TYR D CA  1 
ATOM   4349 C  C   . TYR D  1 36  ? 49.917 -12.934 42.998  1.00 33.81 ? 37  TYR D C   1 
ATOM   4350 O  O   . TYR D  1 36  ? 50.090 -13.792 42.130  1.00 31.18 ? 37  TYR D O   1 
ATOM   4351 C  CB  . TYR D  1 36  ? 51.901 -11.961 44.188  1.00 28.20 ? 37  TYR D CB  1 
ATOM   4352 C  CG  . TYR D  1 36  ? 52.476 -13.362 44.213  1.00 32.38 ? 37  TYR D CG  1 
ATOM   4353 C  CD1 . TYR D  1 36  ? 53.483 -13.739 43.329  1.00 34.34 ? 37  TYR D CD1 1 
ATOM   4354 C  CD2 . TYR D  1 36  ? 52.015 -14.308 45.120  1.00 28.40 ? 37  TYR D CD2 1 
ATOM   4355 C  CE1 . TYR D  1 36  ? 54.003 -15.022 43.342  1.00 33.59 ? 37  TYR D CE1 1 
ATOM   4356 C  CE2 . TYR D  1 36  ? 52.533 -15.581 45.147  1.00 31.56 ? 37  TYR D CE2 1 
ATOM   4357 C  CZ  . TYR D  1 36  ? 53.527 -15.933 44.256  1.00 32.90 ? 37  TYR D CZ  1 
ATOM   4358 O  OH  . TYR D  1 36  ? 54.041 -17.205 44.274  1.00 38.04 ? 37  TYR D OH  1 
ATOM   4359 N  N   . PHE D  1 37  ? 48.899 -12.990 43.856  1.00 28.82 ? 38  PHE D N   1 
ATOM   4360 C  CA  . PHE D  1 37  ? 47.955 -14.097 43.852  1.00 32.91 ? 38  PHE D CA  1 
ATOM   4361 C  C   . PHE D  1 37  ? 46.937 -14.022 42.717  1.00 33.17 ? 38  PHE D C   1 
ATOM   4362 O  O   . PHE D  1 37  ? 46.153 -14.966 42.572  1.00 33.16 ? 38  PHE D O   1 
ATOM   4363 C  CB  . PHE D  1 37  ? 47.240 -14.182 45.206  1.00 28.30 ? 38  PHE D CB  1 
ATOM   4364 C  CG  . PHE D  1 37  ? 48.116 -14.722 46.283  1.00 30.68 ? 38  PHE D CG  1 
ATOM   4365 C  CD1 . PHE D  1 37  ? 48.521 -16.050 46.249  1.00 28.09 ? 38  PHE D CD1 1 
ATOM   4366 C  CD2 . PHE D  1 37  ? 48.589 -13.899 47.291  1.00 29.80 ? 38  PHE D CD2 1 
ATOM   4367 C  CE1 . PHE D  1 37  ? 49.357 -16.559 47.214  1.00 33.89 ? 38  PHE D CE1 1 
ATOM   4368 C  CE2 . PHE D  1 37  ? 49.433 -14.402 48.266  1.00 35.09 ? 38  PHE D CE2 1 
ATOM   4369 C  CZ  . PHE D  1 37  ? 49.819 -15.733 48.228  1.00 32.45 ? 38  PHE D CZ  1 
ATOM   4370 N  N   . GLU D  1 38  ? 46.940 -12.947 41.921  1.00 30.39 ? 39  GLU D N   1 
ATOM   4371 C  CA  . GLU D  1 38  ? 46.128 -12.829 40.707  1.00 36.73 ? 39  GLU D CA  1 
ATOM   4372 C  C   . GLU D  1 38  ? 46.916 -13.114 39.428  1.00 36.81 ? 39  GLU D C   1 
ATOM   4373 O  O   . GLU D  1 38  ? 46.350 -13.006 38.333  1.00 32.41 ? 39  GLU D O   1 
ATOM   4374 C  CB  . GLU D  1 38  ? 45.515 -11.423 40.602  1.00 34.72 ? 39  GLU D CB  1 
ATOM   4375 C  CG  . GLU D  1 38  ? 44.554 -11.054 41.712  1.00 41.24 ? 39  GLU D CG  1 
ATOM   4376 C  CD  . GLU D  1 38  ? 43.700 -9.825  41.386  1.00 57.01 ? 39  GLU D CD  1 
ATOM   4377 O  OE1 . GLU D  1 38  ? 43.967 -9.131  40.367  1.00 53.47 ? 39  GLU D OE1 1 
ATOM   4378 O  OE2 . GLU D  1 38  ? 42.763 -9.542  42.171  1.00 65.77 ? 39  GLU D OE2 1 
ATOM   4379 N  N   . ARG D  1 39  ? 48.209 -13.423 39.529  1.00 31.92 ? 40  ARG D N   1 
ATOM   4380 C  CA  . ARG D  1 39  ? 48.958 -13.879 38.368  1.00 30.72 ? 40  ARG D CA  1 
ATOM   4381 C  C   . ARG D  1 39  ? 48.301 -15.120 37.776  1.00 34.55 ? 40  ARG D C   1 
ATOM   4382 O  O   . ARG D  1 39  ? 47.700 -15.932 38.487  1.00 32.51 ? 40  ARG D O   1 
ATOM   4383 C  CB  . ARG D  1 39  ? 50.408 -14.188 38.751  1.00 31.30 ? 40  ARG D CB  1 
ATOM   4384 C  CG  . ARG D  1 39  ? 51.259 -12.946 38.970  1.00 32.50 ? 40  ARG D CG  1 
ATOM   4385 C  CD  . ARG D  1 39  ? 52.528 -13.276 39.723  1.00 32.57 ? 40  ARG D CD  1 
ATOM   4386 N  NE  . ARG D  1 39  ? 53.273 -14.365 39.100  1.00 35.14 ? 40  ARG D NE  1 
ATOM   4387 C  CZ  . ARG D  1 39  ? 54.570 -14.589 39.274  1.00 43.29 ? 40  ARG D CZ  1 
ATOM   4388 N  NH1 . ARG D  1 39  ? 55.322 -13.782 40.012  1.00 41.79 ? 40  ARG D NH1 1 
ATOM   4389 N  NH2 . ARG D  1 39  ? 55.129 -15.649 38.694  1.00 44.93 ? 40  ARG D NH2 1 
ATOM   4390 N  N   . ASP D  1 40  ? 48.424 -15.266 36.451  1.00 36.52 ? 41  ASP D N   1 
ATOM   4391 C  CA  . ASP D  1 40  ? 47.807 -16.403 35.770  1.00 36.52 ? 41  ASP D CA  1 
ATOM   4392 C  C   . ASP D  1 40  ? 48.384 -17.734 36.243  1.00 38.34 ? 41  ASP D C   1 
ATOM   4393 O  O   . ASP D  1 40  ? 47.675 -18.743 36.234  1.00 41.19 ? 41  ASP D O   1 
ATOM   4394 C  CB  . ASP D  1 40  ? 47.979 -16.275 34.254  1.00 36.75 ? 41  ASP D CB  1 
ATOM   4395 C  CG  . ASP D  1 40  ? 49.407 -16.574 33.804  1.00 40.22 ? 41  ASP D CG  1 
ATOM   4396 O  OD1 . ASP D  1 40  ? 50.250 -15.638 33.798  1.00 40.32 ? 41  ASP D OD1 1 
ATOM   4397 O  OD2 . ASP D  1 40  ? 49.692 -17.757 33.485  1.00 42.56 ? 41  ASP D OD2 1 
ATOM   4398 N  N   . ASP D  1 41  ? 49.657 -17.761 36.645  1.00 32.84 ? 42  ASP D N   1 
ATOM   4399 C  CA  . ASP D  1 41  ? 50.326 -18.968 37.111  1.00 34.32 ? 42  ASP D CA  1 
ATOM   4400 C  C   . ASP D  1 41  ? 50.230 -19.162 38.620  1.00 35.57 ? 42  ASP D C   1 
ATOM   4401 O  O   . ASP D  1 41  ? 50.951 -20.002 39.173  1.00 35.88 ? 42  ASP D O   1 
ATOM   4402 C  CB  . ASP D  1 41  ? 51.805 -18.959 36.682  1.00 36.33 ? 42  ASP D CB  1 
ATOM   4403 C  CG  . ASP D  1 41  ? 52.594 -17.774 37.263  1.00 42.23 ? 42  ASP D CG  1 
ATOM   4404 O  OD1 . ASP D  1 41  ? 51.976 -16.870 37.855  1.00 41.72 ? 42  ASP D OD1 1 
ATOM   4405 O  OD2 . ASP D  1 41  ? 53.842 -17.736 37.120  1.00 47.57 ? 42  ASP D OD2 1 
ATOM   4406 N  N   . VAL D  1 42  ? 49.373 -18.404 39.301  1.00 32.02 ? 43  VAL D N   1 
ATOM   4407 C  CA  . VAL D  1 42  ? 49.178 -18.585 40.739  1.00 36.34 ? 43  VAL D CA  1 
ATOM   4408 C  C   . VAL D  1 42  ? 47.690 -18.791 41.000  1.00 35.17 ? 43  VAL D C   1 
ATOM   4409 O  O   . VAL D  1 42  ? 47.285 -19.817 41.557  1.00 31.47 ? 43  VAL D O   1 
ATOM   4410 C  CB  . VAL D  1 42  ? 49.728 -17.396 41.558  1.00 33.21 ? 43  VAL D CB  1 
ATOM   4411 C  CG1 . VAL D  1 42  ? 49.413 -17.592 43.037  1.00 33.10 ? 43  VAL D CG1 1 
ATOM   4412 C  CG2 . VAL D  1 42  ? 51.231 -17.213 41.353  1.00 26.31 ? 43  VAL D CG2 1 
ATOM   4413 N  N   . ALA D  1 43  ? 46.880 -17.801 40.622  1.00 31.73 ? 44  ALA D N   1 
ATOM   4414 C  CA  . ALA D  1 43  ? 45.427 -17.931 40.528  1.00 30.48 ? 44  ALA D CA  1 
ATOM   4415 C  C   . ALA D  1 43  ? 44.817 -18.433 41.840  1.00 37.95 ? 44  ALA D C   1 
ATOM   4416 O  O   . ALA D  1 43  ? 44.241 -19.524 41.922  1.00 33.13 ? 44  ALA D O   1 
ATOM   4417 C  CB  . ALA D  1 43  ? 45.045 -18.844 39.357  1.00 32.26 ? 44  ALA D CB  1 
ATOM   4418 N  N   . LEU D  1 44  ? 44.960 -17.610 42.884  1.00 34.21 ? 45  LEU D N   1 
ATOM   4419 C  CA  . LEU D  1 44  ? 44.364 -17.874 44.194  1.00 34.78 ? 45  LEU D CA  1 
ATOM   4420 C  C   . LEU D  1 44  ? 43.506 -16.665 44.553  1.00 32.70 ? 45  LEU D C   1 
ATOM   4421 O  O   . LEU D  1 44  ? 43.926 -15.805 45.345  1.00 33.93 ? 45  LEU D O   1 
ATOM   4422 C  CB  . LEU D  1 44  ? 45.433 -18.157 45.253  1.00 29.68 ? 45  LEU D CB  1 
ATOM   4423 C  CG  . LEU D  1 44  ? 46.008 -19.566 45.170  1.00 35.12 ? 45  LEU D CG  1 
ATOM   4424 C  CD1 . LEU D  1 44  ? 47.308 -19.680 45.962  1.00 36.62 ? 45  LEU D CD1 1 
ATOM   4425 C  CD2 . LEU D  1 44  ? 44.981 -20.612 45.628  1.00 30.86 ? 45  LEU D CD2 1 
ATOM   4426 N  N   . PRO D  1 45  ? 42.295 -16.571 43.990  1.00 35.36 ? 46  PRO D N   1 
ATOM   4427 C  CA  . PRO D  1 45  ? 41.475 -15.360 44.192  1.00 34.02 ? 46  PRO D CA  1 
ATOM   4428 C  C   . PRO D  1 45  ? 41.089 -15.093 45.637  1.00 37.84 ? 46  PRO D C   1 
ATOM   4429 O  O   . PRO D  1 45  ? 40.961 -13.922 46.015  1.00 39.19 ? 46  PRO D O   1 
ATOM   4430 C  CB  . PRO D  1 45  ? 40.234 -15.628 43.323  1.00 36.07 ? 46  PRO D CB  1 
ATOM   4431 C  CG  . PRO D  1 45  ? 40.212 -17.132 43.151  1.00 41.93 ? 46  PRO D CG  1 
ATOM   4432 C  CD  . PRO D  1 45  ? 41.659 -17.521 43.060  1.00 31.04 ? 46  PRO D CD  1 
ATOM   4433 N  N   . GLY D  1 46  ? 40.888 -16.125 46.460  1.00 35.85 ? 47  GLY D N   1 
ATOM   4434 C  CA  . GLY D  1 46  ? 40.581 -15.875 47.864  1.00 37.57 ? 47  GLY D CA  1 
ATOM   4435 C  C   . GLY D  1 46  ? 41.714 -15.178 48.601  1.00 36.22 ? 47  GLY D C   1 
ATOM   4436 O  O   . GLY D  1 46  ? 41.495 -14.191 49.308  1.00 33.80 ? 47  GLY D O   1 
ATOM   4437 N  N   . PHE D  1 47  ? 42.943 -15.693 48.457  1.00 31.47 ? 48  PHE D N   1 
ATOM   4438 C  CA  . PHE D  1 47  ? 44.110 -15.019 49.030  1.00 35.06 ? 48  PHE D CA  1 
ATOM   4439 C  C   . PHE D  1 47  ? 44.263 -13.598 48.484  1.00 33.03 ? 48  PHE D C   1 
ATOM   4440 O  O   . PHE D  1 47  ? 44.595 -12.667 49.229  1.00 31.57 ? 48  PHE D O   1 
ATOM   4441 C  CB  . PHE D  1 47  ? 45.374 -15.833 48.748  1.00 33.44 ? 48  PHE D CB  1 
ATOM   4442 C  CG  . PHE D  1 47  ? 45.532 -17.040 49.632  1.00 32.31 ? 48  PHE D CG  1 
ATOM   4443 C  CD1 . PHE D  1 47  ? 46.128 -16.929 50.876  1.00 34.50 ? 48  PHE D CD1 1 
ATOM   4444 C  CD2 . PHE D  1 47  ? 45.106 -18.284 49.211  1.00 34.06 ? 48  PHE D CD2 1 
ATOM   4445 C  CE1 . PHE D  1 47  ? 46.286 -18.038 51.686  1.00 36.15 ? 48  PHE D CE1 1 
ATOM   4446 C  CE2 . PHE D  1 47  ? 45.265 -19.393 50.009  1.00 35.59 ? 48  PHE D CE2 1 
ATOM   4447 C  CZ  . PHE D  1 47  ? 45.855 -19.271 51.252  1.00 35.83 ? 48  PHE D CZ  1 
ATOM   4448 N  N   . ALA D  1 48  ? 44.022 -13.410 47.185  1.00 30.70 ? 49  ALA D N   1 
ATOM   4449 C  CA  . ALA D  1 48  ? 44.125 -12.076 46.607  1.00 33.90 ? 49  ALA D CA  1 
ATOM   4450 C  C   . ALA D  1 48  ? 43.154 -11.125 47.286  1.00 34.97 ? 49  ALA D C   1 
ATOM   4451 O  O   . ALA D  1 48  ? 43.532 -10.020 47.702  1.00 32.87 ? 49  ALA D O   1 
ATOM   4452 C  CB  . ALA D  1 48  ? 43.865 -12.120 45.099  1.00 33.25 ? 49  ALA D CB  1 
ATOM   4453 N  N   . LYS D  1 49  ? 41.897 -11.555 47.432  1.00 33.47 ? 50  LYS D N   1 
ATOM   4454 C  CA  . LYS D  1 49  ? 40.884 -10.723 48.074  1.00 38.36 ? 50  LYS D CA  1 
ATOM   4455 C  C   . LYS D  1 49  ? 41.251 -10.417 49.525  1.00 35.16 ? 50  LYS D C   1 
ATOM   4456 O  O   . LYS D  1 49  ? 41.133 -9.273  49.975  1.00 36.25 ? 50  LYS D O   1 
ATOM   4457 C  CB  . LYS D  1 49  ? 39.518 -11.416 47.991  1.00 39.40 ? 50  LYS D CB  1 
ATOM   4458 C  CG  . LYS D  1 49  ? 38.396 -10.657 48.695  1.00 47.49 ? 50  LYS D CG  1 
ATOM   4459 C  CD  . LYS D  1 49  ? 37.031 -11.324 48.479  1.00 56.62 ? 50  LYS D CD  1 
ATOM   4460 C  CE  . LYS D  1 49  ? 36.385 -10.865 47.176  1.00 61.95 ? 50  LYS D CE  1 
ATOM   4461 N  NZ  . LYS D  1 49  ? 36.490 -11.911 46.103  1.00 65.13 ? 50  LYS D NZ  1 
ATOM   4462 N  N   . PHE D  1 50  ? 41.711 -11.426 50.266  1.00 30.68 ? 51  PHE D N   1 
ATOM   4463 C  CA  . PHE D  1 50  ? 42.102 -11.212 51.653  1.00 31.22 ? 51  PHE D CA  1 
ATOM   4464 C  C   . PHE D  1 50  ? 43.233 -10.185 51.766  1.00 33.48 ? 51  PHE D C   1 
ATOM   4465 O  O   . PHE D  1 50  ? 43.218 -9.328  52.659  1.00 32.00 ? 51  PHE D O   1 
ATOM   4466 C  CB  . PHE D  1 50  ? 42.510 -12.546 52.283  1.00 33.18 ? 51  PHE D CB  1 
ATOM   4467 C  CG  . PHE D  1 50  ? 43.109 -12.407 53.658  1.00 34.52 ? 51  PHE D CG  1 
ATOM   4468 C  CD1 . PHE D  1 50  ? 42.292 -12.216 54.774  1.00 35.67 ? 51  PHE D CD1 1 
ATOM   4469 C  CD2 . PHE D  1 50  ? 44.486 -12.454 53.836  1.00 31.83 ? 51  PHE D CD2 1 
ATOM   4470 C  CE1 . PHE D  1 50  ? 42.850 -12.082 56.052  1.00 40.68 ? 51  PHE D CE1 1 
ATOM   4471 C  CE2 . PHE D  1 50  ? 45.055 -12.318 55.101  1.00 34.84 ? 51  PHE D CE2 1 
ATOM   4472 C  CZ  . PHE D  1 50  ? 44.239 -12.131 56.214  1.00 36.71 ? 51  PHE D CZ  1 
ATOM   4473 N  N   . PHE D  1 51  ? 44.226 -10.248 50.881  1.00 31.11 ? 52  PHE D N   1 
ATOM   4474 C  CA  . PHE D  1 51  ? 45.336 -9.311  51.036  1.00 34.69 ? 52  PHE D CA  1 
ATOM   4475 C  C   . PHE D  1 51  ? 44.984 -7.916  50.520  1.00 33.27 ? 52  PHE D C   1 
ATOM   4476 O  O   . PHE D  1 51  ? 45.466 -6.919  51.068  1.00 30.65 ? 52  PHE D O   1 
ATOM   4477 C  CB  . PHE D  1 51  ? 46.594 -9.865  50.363  1.00 30.35 ? 52  PHE D CB  1 
ATOM   4478 C  CG  . PHE D  1 51  ? 47.214 -11.039 51.113  1.00 32.92 ? 52  PHE D CG  1 
ATOM   4479 C  CD1 . PHE D  1 51  ? 47.647 -10.892 52.418  1.00 31.23 ? 52  PHE D CD1 1 
ATOM   4480 C  CD2 . PHE D  1 51  ? 47.346 -12.282 50.511  1.00 31.12 ? 52  PHE D CD2 1 
ATOM   4481 C  CE1 . PHE D  1 51  ? 48.214 -11.960 53.113  1.00 32.24 ? 52  PHE D CE1 1 
ATOM   4482 C  CE2 . PHE D  1 51  ? 47.914 -13.347 51.192  1.00 35.63 ? 52  PHE D CE2 1 
ATOM   4483 C  CZ  . PHE D  1 51  ? 48.353 -13.185 52.502  1.00 30.79 ? 52  PHE D CZ  1 
ATOM   4484 N  N   . LYS D  1 52  ? 44.136 -7.822  49.496  1.00 29.48 ? 53  LYS D N   1 
ATOM   4485 C  CA  . LYS D  1 52  ? 43.621 -6.524  49.070  1.00 35.07 ? 53  LYS D CA  1 
ATOM   4486 C  C   . LYS D  1 52  ? 42.903 -5.814  50.221  1.00 37.95 ? 53  LYS D C   1 
ATOM   4487 O  O   . LYS D  1 52  ? 43.131 -4.623  50.472  1.00 35.36 ? 53  LYS D O   1 
ATOM   4488 C  CB  . LYS D  1 52  ? 42.686 -6.716  47.875  1.00 33.09 ? 53  LYS D CB  1 
ATOM   4489 C  CG  . LYS D  1 52  ? 42.244 -5.443  47.221  1.00 45.62 ? 53  LYS D CG  1 
ATOM   4490 C  CD  . LYS D  1 52  ? 43.439 -4.665  46.665  1.00 57.43 ? 53  LYS D CD  1 
ATOM   4491 C  CE  . LYS D  1 52  ? 43.192 -3.148  46.704  1.00 56.10 ? 53  LYS D CE  1 
ATOM   4492 N  NZ  . LYS D  1 52  ? 41.831 -2.757  46.206  1.00 62.06 ? 53  LYS D NZ  1 
ATOM   4493 N  N   . GLU D  1 53  ? 42.035 -6.543  50.937  1.00 31.91 ? 54  GLU D N   1 
ATOM   4494 C  CA  . GLU D  1 53  ? 41.359 -5.998  52.112  1.00 36.03 ? 54  GLU D CA  1 
ATOM   4495 C  C   . GLU D  1 53  ? 42.362 -5.551  53.173  1.00 36.43 ? 54  GLU D C   1 
ATOM   4496 O  O   . GLU D  1 53  ? 42.225 -4.463  53.749  1.00 34.21 ? 54  GLU D O   1 
ATOM   4497 C  CB  . GLU D  1 53  ? 40.398 -7.045  52.693  1.00 38.19 ? 54  GLU D CB  1 
ATOM   4498 C  CG  . GLU D  1 53  ? 39.200 -7.381  51.782  1.00 47.50 ? 54  GLU D CG  1 
ATOM   4499 C  CD  . GLU D  1 53  ? 38.336 -8.577  52.276  1.00 63.60 ? 54  GLU D CD  1 
ATOM   4500 O  OE1 . GLU D  1 53  ? 38.669 -9.202  53.324  1.00 56.80 ? 54  GLU D OE1 1 
ATOM   4501 O  OE2 . GLU D  1 53  ? 37.320 -8.891  51.593  1.00 58.88 ? 54  GLU D OE2 1 
ATOM   4502 N  N   . SER D  1 54  ? 43.377 -6.379  53.447  1.00 32.54 ? 55  SER D N   1 
ATOM   4503 C  CA  . SER D  1 54  ? 44.403 -5.994  54.411  1.00 33.45 ? 55  SER D CA  1 
ATOM   4504 C  C   . SER D  1 54  ? 45.121 -4.725  53.965  1.00 33.83 ? 55  SER D C   1 
ATOM   4505 O  O   . SER D  1 54  ? 45.464 -3.874  54.794  1.00 31.71 ? 55  SER D O   1 
ATOM   4506 C  CB  . SER D  1 54  ? 45.398 -7.137  54.611  1.00 35.23 ? 55  SER D CB  1 
ATOM   4507 O  OG  . SER D  1 54  ? 44.749 -8.333  55.038  1.00 39.67 ? 55  SER D OG  1 
ATOM   4508 N  N   . SER D  1 55  ? 45.311 -4.560  52.654  1.00 30.60 ? 56  SER D N   1 
ATOM   4509 C  CA  . SER D  1 55  ? 45.993 -3.379  52.146  1.00 29.18 ? 56  SER D CA  1 
ATOM   4510 C  C   . SER D  1 55  ? 45.190 -2.116  52.430  1.00 33.62 ? 56  SER D C   1 
ATOM   4511 O  O   . SER D  1 55  ? 45.739 -1.118  52.911  1.00 31.47 ? 56  SER D O   1 
ATOM   4512 C  CB  . SER D  1 55  ? 46.266 -3.537  50.649  1.00 27.11 ? 56  SER D CB  1 
ATOM   4513 O  OG  . SER D  1 55  ? 47.053 -2.464  50.161  1.00 30.93 ? 56  SER D OG  1 
ATOM   4514 N  N   . ASP D  1 56  ? 43.882 -2.143  52.139  1.00 31.56 ? 57  ASP D N   1 
ATOM   4515 C  CA  . ASP D  1 56  ? 43.023 -0.989  52.395  1.00 34.75 ? 57  ASP D CA  1 
ATOM   4516 C  C   . ASP D  1 56  ? 43.008 -0.640  53.876  1.00 33.72 ? 57  ASP D C   1 
ATOM   4517 O  O   . ASP D  1 56  ? 43.098 0.535   54.249  1.00 33.12 ? 57  ASP D O   1 
ATOM   4518 C  CB  . ASP D  1 56  ? 41.598 -1.288  51.913  1.00 35.30 ? 57  ASP D CB  1 
ATOM   4519 C  CG  . ASP D  1 56  ? 41.498 -1.386  50.390  1.00 46.04 ? 57  ASP D CG  1 
ATOM   4520 O  OD1 . ASP D  1 56  ? 42.509 -1.120  49.695  1.00 48.97 ? 57  ASP D OD1 1 
ATOM   4521 O  OD2 . ASP D  1 56  ? 40.417 -1.769  49.884  1.00 56.60 ? 57  ASP D OD2 1 
ATOM   4522 N  N   . CYS D  1 57  ? 42.898 -1.660  54.729  1.00 35.39 ? 58  CYS D N   1 
ATOM   4523 C  CA  . CYS D  1 57  ? 42.903 -1.478  56.181  1.00 38.07 ? 58  CYS D CA  1 
ATOM   4524 C  C   . CYS D  1 57  ? 44.129 -0.705  56.668  1.00 38.26 ? 58  CYS D C   1 
ATOM   4525 O  O   . CYS D  1 57  ? 44.001 0.271   57.416  1.00 38.12 ? 58  CYS D O   1 
ATOM   4526 C  CB  . CYS D  1 57  ? 42.843 -2.845  56.853  1.00 42.85 ? 58  CYS D CB  1 
ATOM   4527 S  SG  . CYS D  1 57  ? 43.110 -2.722  58.599  1.00 59.87 ? 58  CYS D SG  1 
ATOM   4528 N  N   . CYS D  1 58  ? 45.331 -1.148  56.275  1.00 33.11 ? 59  CYS D N   1 
ATOM   4529 C  CA  . CYS D  1 58  ? 46.557 -0.452  56.670  1.00 34.25 ? 59  CYS D CA  1 
ATOM   4530 C  C   . CYS D  1 58  ? 46.604 0.980   56.131  1.00 35.73 ? 59  CYS D C   1 
ATOM   4531 O  O   . CYS D  1 58  ? 47.107 1.888   56.805  1.00 31.98 ? 59  CYS D O   1 
ATOM   4532 C  CB  . CYS D  1 58  ? 47.774 -1.239  56.190  1.00 31.60 ? 59  CYS D CB  1 
ATOM   4533 S  SG  . CYS D  1 58  ? 48.179 -2.672  57.226  1.00 42.40 ? 59  CYS D SG  1 
ATOM   4534 N  N   . ARG D  1 59  ? 46.119 1.205   54.906  1.00 33.44 ? 60  ARG D N   1 
ATOM   4535 C  CA  . ARG D  1 59  ? 46.097 2.572   54.395  1.00 35.97 ? 60  ARG D CA  1 
ATOM   4536 C  C   . ARG D  1 59  ? 45.176 3.451   55.238  1.00 37.21 ? 60  ARG D C   1 
ATOM   4537 O  O   . ARG D  1 59  ? 45.485 4.621   55.501  1.00 31.88 ? 60  ARG D O   1 
ATOM   4538 C  CB  . ARG D  1 59  ? 45.673 2.593   52.924  1.00 34.82 ? 60  ARG D CB  1 
ATOM   4539 C  CG  . ARG D  1 59  ? 46.041 3.891   52.232  1.00 38.82 ? 60  ARG D CG  1 
ATOM   4540 C  CD  . ARG D  1 59  ? 45.525 3.973   50.798  1.00 46.67 ? 60  ARG D CD  1 
ATOM   4541 N  NE  . ARG D  1 59  ? 44.122 3.587   50.675  1.00 50.75 ? 60  ARG D NE  1 
ATOM   4542 C  CZ  . ARG D  1 59  ? 43.711 2.458   50.114  1.00 51.71 ? 60  ARG D CZ  1 
ATOM   4543 N  NH1 . ARG D  1 59  ? 44.575 1.576   49.624  1.00 49.15 ? 60  ARG D NH1 1 
ATOM   4544 N  NH2 . ARG D  1 59  ? 42.404 2.199   50.054  1.00 46.09 ? 60  ARG D NH2 1 
ATOM   4545 N  N   . GLU D  1 60  ? 44.047 2.894   55.689  1.00 36.78 ? 61  GLU D N   1 
ATOM   4546 C  CA  . GLU D  1 60  ? 43.173 3.647   56.581  1.00 39.84 ? 61  GLU D CA  1 
ATOM   4547 C  C   . GLU D  1 60  ? 43.821 3.846   57.960  1.00 37.40 ? 61  GLU D C   1 
ATOM   4548 O  O   . GLU D  1 60  ? 43.633 4.903   58.573  1.00 35.33 ? 61  GLU D O   1 
ATOM   4549 C  CB  . GLU D  1 60  ? 41.803 2.956   56.659  1.00 37.31 ? 61  GLU D CB  1 
ATOM   4550 C  CG  . GLU D  1 60  ? 40.979 3.286   57.913  1.00 59.92 ? 61  GLU D CG  1 
ATOM   4551 C  CD  . GLU D  1 60  ? 40.066 2.134   58.393  1.00 72.69 ? 61  GLU D CD  1 
ATOM   4552 O  OE1 . GLU D  1 60  ? 40.425 0.935   58.228  1.00 66.11 ? 61  GLU D OE1 1 
ATOM   4553 O  OE2 . GLU D  1 60  ? 38.991 2.441   58.966  1.00 77.62 ? 61  GLU D OE2 1 
ATOM   4554 N  N   . HIS D  1 61  ? 44.624 2.877   58.439  1.00 34.91 ? 62  HIS D N   1 
ATOM   4555 C  CA  . HIS D  1 61  ? 45.406 3.092   59.661  1.00 36.35 ? 62  HIS D CA  1 
ATOM   4556 C  C   . HIS D  1 61  ? 46.360 4.271   59.509  1.00 33.80 ? 62  HIS D C   1 
ATOM   4557 O  O   . HIS D  1 61  ? 46.499 5.086   60.423  1.00 32.35 ? 62  HIS D O   1 
ATOM   4558 C  CB  . HIS D  1 61  ? 46.221 1.849   60.038  1.00 39.02 ? 62  HIS D CB  1 
ATOM   4559 C  CG  . HIS D  1 61  ? 45.399 0.691   60.506  1.00 45.72 ? 62  HIS D CG  1 
ATOM   4560 N  ND1 . HIS D  1 61  ? 45.892 -0.599  60.548  1.00 46.88 ? 62  HIS D ND1 1 
ATOM   4561 C  CD2 . HIS D  1 61  ? 44.120 0.623   60.947  1.00 45.57 ? 62  HIS D CD2 1 
ATOM   4562 C  CE1 . HIS D  1 61  ? 44.949 -1.411  60.992  1.00 53.67 ? 62  HIS D CE1 1 
ATOM   4563 N  NE2 . HIS D  1 61  ? 43.864 -0.695  61.241  1.00 51.30 ? 62  HIS D NE2 1 
ATOM   4564 N  N   . ALA D  1 62  ? 47.047 4.369   58.369  1.00 33.57 ? 63  ALA D N   1 
ATOM   4565 C  CA  . ALA D  1 62  ? 47.964 5.484   58.165  1.00 30.86 ? 63  ALA D CA  1 
ATOM   4566 C  C   . ALA D  1 62  ? 47.225 6.818   58.190  1.00 32.07 ? 63  ALA D C   1 
ATOM   4567 O  O   . ALA D  1 62  ? 47.691 7.784   58.799  1.00 30.74 ? 63  ALA D O   1 
ATOM   4568 C  CB  . ALA D  1 62  ? 48.720 5.302   56.843  1.00 29.10 ? 63  ALA D CB  1 
ATOM   4569 N  N   . GLN D  1 63  ? 46.062 6.889   57.544  1.00 33.93 ? 64  GLN D N   1 
ATOM   4570 C  CA  . GLN D  1 63  ? 45.362 8.163   57.420  1.00 35.62 ? 64  GLN D CA  1 
ATOM   4571 C  C   . GLN D  1 63  ? 44.750 8.626   58.746  1.00 34.22 ? 64  GLN D C   1 
ATOM   4572 O  O   . GLN D  1 63  ? 44.676 9.831   59.009  1.00 29.18 ? 64  GLN D O   1 
ATOM   4573 C  CB  . GLN D  1 63  ? 44.312 8.034   56.327  1.00 36.88 ? 64  GLN D CB  1 
ATOM   4574 C  CG  . GLN D  1 63  ? 44.953 7.880   54.947  1.00 38.06 ? 64  GLN D CG  1 
ATOM   4575 C  CD  . GLN D  1 63  ? 43.930 7.782   53.849  1.00 49.03 ? 64  GLN D CD  1 
ATOM   4576 O  OE1 . GLN D  1 63  ? 42.733 7.701   54.121  1.00 61.09 ? 64  GLN D OE1 1 
ATOM   4577 N  NE2 . GLN D  1 63  ? 44.387 7.777   52.600  1.00 54.72 ? 64  GLN D NE2 1 
ATOM   4578 N  N   . THR D  1 64  ? 44.319 7.697   59.591  1.00 27.38 ? 65  THR D N   1 
ATOM   4579 C  CA  . THR D  1 64  ? 43.864 8.070   60.923  1.00 33.08 ? 65  THR D CA  1 
ATOM   4580 C  C   . THR D  1 64  ? 45.011 8.680   61.737  1.00 33.81 ? 65  THR D C   1 
ATOM   4581 O  O   . THR D  1 64  ? 44.815 9.670   62.457  1.00 29.79 ? 65  THR D O   1 
ATOM   4582 C  CB  . THR D  1 64  ? 43.261 6.834   61.616  1.00 37.98 ? 65  THR D CB  1 
ATOM   4583 O  OG1 . THR D  1 64  ? 42.094 6.401   60.900  1.00 39.56 ? 65  THR D OG1 1 
ATOM   4584 C  CG2 . THR D  1 64  ? 42.872 7.127   63.071  1.00 36.90 ? 65  THR D CG2 1 
ATOM   4585 N  N   . PHE D  1 65  ? 46.226 8.126   61.611  1.00 27.31 ? 66  PHE D N   1 
ATOM   4586 C  CA  . PHE D  1 65  ? 47.378 8.740   62.266  1.00 28.69 ? 66  PHE D CA  1 
ATOM   4587 C  C   . PHE D  1 65  ? 47.692 10.124  61.700  1.00 30.16 ? 66  PHE D C   1 
ATOM   4588 O  O   . PHE D  1 65  ? 48.127 10.999  62.449  1.00 30.30 ? 66  PHE D O   1 
ATOM   4589 C  CB  . PHE D  1 65  ? 48.613 7.857   62.140  1.00 32.07 ? 66  PHE D CB  1 
ATOM   4590 C  CG  . PHE D  1 65  ? 48.739 6.803   63.204  1.00 36.17 ? 66  PHE D CG  1 
ATOM   4591 C  CD1 . PHE D  1 65  ? 48.651 7.123   64.547  1.00 35.23 ? 66  PHE D CD1 1 
ATOM   4592 C  CD2 . PHE D  1 65  ? 48.990 5.477   62.848  1.00 39.26 ? 66  PHE D CD2 1 
ATOM   4593 C  CE1 . PHE D  1 65  ? 48.784 6.135   65.531  1.00 37.13 ? 66  PHE D CE1 1 
ATOM   4594 C  CE2 . PHE D  1 65  ? 49.130 4.485   63.823  1.00 40.51 ? 66  PHE D CE2 1 
ATOM   4595 C  CZ  . PHE D  1 65  ? 49.024 4.819   65.167  1.00 38.15 ? 66  PHE D CZ  1 
ATOM   4596 N  N   . MET D  1 66  ? 47.491 10.357  60.396  1.00 28.15 ? 67  MET D N   1 
ATOM   4597 C  CA  . MET D  1 66  ? 47.763 11.698  59.878  1.00 30.79 ? 67  MET D CA  1 
ATOM   4598 C  C   . MET D  1 66  ? 46.743 12.701  60.386  1.00 31.18 ? 67  MET D C   1 
ATOM   4599 O  O   . MET D  1 66  ? 47.095 13.835  60.734  1.00 31.54 ? 67  MET D O   1 
ATOM   4600 C  CB  . MET D  1 66  ? 47.806 11.716  58.350  1.00 28.85 ? 67  MET D CB  1 
ATOM   4601 C  CG  . MET D  1 66  ? 48.894 10.823  57.740  1.00 31.26 ? 67  MET D CG  1 
ATOM   4602 S  SD  . MET D  1 66  ? 48.650 10.475  55.983  1.00 39.01 ? 67  MET D SD  1 
ATOM   4603 C  CE  . MET D  1 66  ? 49.229 12.014  55.287  1.00 37.04 ? 67  MET D CE  1 
ATOM   4604 N  N   . LYS D  1 67  ? 45.478 12.298  60.428  1.00 32.04 ? 68  LYS D N   1 
ATOM   4605 C  CA  . LYS D  1 67  ? 44.448 13.145  61.003  1.00 31.65 ? 68  LYS D CA  1 
ATOM   4606 C  C   . LYS D  1 67  ? 44.764 13.443  62.458  1.00 33.21 ? 68  LYS D C   1 
ATOM   4607 O  O   . LYS D  1 67  ? 44.650 14.589  62.909  1.00 32.71 ? 68  LYS D O   1 
ATOM   4608 C  CB  . LYS D  1 67  ? 43.096 12.448  60.878  1.00 34.82 ? 68  LYS D CB  1 
ATOM   4609 C  CG  . LYS D  1 67  ? 41.884 13.348  60.998  1.00 50.25 ? 68  LYS D CG  1 
ATOM   4610 C  CD  . LYS D  1 67  ? 40.604 12.623  60.531  1.00 60.88 ? 68  LYS D CD  1 
ATOM   4611 C  CE  . LYS D  1 67  ? 40.833 11.543  59.425  1.00 58.33 ? 68  LYS D CE  1 
ATOM   4612 N  NZ  . LYS D  1 67  ? 41.608 11.928  58.193  1.00 57.81 ? 68  LYS D NZ  1 
ATOM   4613 N  N   . TYR D  1 68  ? 45.182 12.419  63.201  1.00 32.54 ? 69  TYR D N   1 
ATOM   4614 C  CA  . TYR D  1 68  ? 45.513 12.606  64.606  1.00 32.55 ? 69  TYR D CA  1 
ATOM   4615 C  C   . TYR D  1 68  ? 46.631 13.625  64.764  1.00 29.20 ? 69  TYR D C   1 
ATOM   4616 O  O   . TYR D  1 68  ? 46.546 14.526  65.599  1.00 30.10 ? 69  TYR D O   1 
ATOM   4617 C  CB  . TYR D  1 68  ? 45.916 11.272  65.237  1.00 27.22 ? 69  TYR D CB  1 
ATOM   4618 C  CG  . TYR D  1 68  ? 46.104 11.401  66.724  1.00 30.87 ? 69  TYR D CG  1 
ATOM   4619 C  CD1 . TYR D  1 68  ? 45.003 11.365  67.574  1.00 37.26 ? 69  TYR D CD1 1 
ATOM   4620 C  CD2 . TYR D  1 68  ? 47.367 11.592  67.282  1.00 27.05 ? 69  TYR D CD2 1 
ATOM   4621 C  CE1 . TYR D  1 68  ? 45.143 11.510  68.933  1.00 34.29 ? 69  TYR D CE1 1 
ATOM   4622 C  CE2 . TYR D  1 68  ? 47.527 11.738  68.661  1.00 31.25 ? 69  TYR D CE2 1 
ATOM   4623 C  CZ  . TYR D  1 68  ? 46.399 11.696  69.477  1.00 34.21 ? 69  TYR D CZ  1 
ATOM   4624 O  OH  . TYR D  1 68  ? 46.488 11.840  70.838  1.00 34.52 ? 69  TYR D OH  1 
ATOM   4625 N  N   . GLN D  1 69  ? 47.683 13.496  63.951  1.00 29.18 ? 70  GLN D N   1 
ATOM   4626 C  CA  . GLN D  1 69  ? 48.798 14.435  63.983  1.00 31.15 ? 70  GLN D CA  1 
ATOM   4627 C  C   . GLN D  1 69  ? 48.306 15.875  63.834  1.00 32.58 ? 70  GLN D C   1 
ATOM   4628 O  O   . GLN D  1 69  ? 48.665 16.749  64.630  1.00 31.71 ? 70  GLN D O   1 
ATOM   4629 C  CB  . GLN D  1 69  ? 49.797 14.059  62.885  1.00 30.34 ? 70  GLN D CB  1 
ATOM   4630 C  CG  . GLN D  1 69  ? 51.090 14.820  62.880  1.00 37.93 ? 70  GLN D CG  1 
ATOM   4631 C  CD  . GLN D  1 69  ? 52.061 14.299  63.925  1.00 39.60 ? 70  GLN D CD  1 
ATOM   4632 O  OE1 . GLN D  1 69  ? 51.945 14.616  65.107  1.00 38.77 ? 70  GLN D OE1 1 
ATOM   4633 N  NE2 . GLN D  1 69  ? 53.009 13.480  63.494  1.00 35.08 ? 70  GLN D NE2 1 
ATOM   4634 N  N   . ASN D  1 70  ? 47.440 16.128  62.842  1.00 32.86 ? 71  ASN D N   1 
ATOM   4635 C  CA  . ASN D  1 70  ? 46.894 17.472  62.655  1.00 33.95 ? 71  ASN D CA  1 
ATOM   4636 C  C   . ASN D  1 70  ? 45.994 17.876  63.824  1.00 37.07 ? 71  ASN D C   1 
ATOM   4637 O  O   . ASN D  1 70  ? 45.978 19.049  64.230  1.00 33.43 ? 71  ASN D O   1 
ATOM   4638 C  CB  . ASN D  1 70  ? 46.119 17.551  61.333  1.00 32.66 ? 71  ASN D CB  1 
ATOM   4639 C  CG  . ASN D  1 70  ? 47.023 17.845  60.148  1.00 34.60 ? 71  ASN D CG  1 
ATOM   4640 O  OD1 . ASN D  1 70  ? 48.169 18.265  60.326  1.00 35.86 ? 71  ASN D OD1 1 
ATOM   4641 N  ND2 . ASN D  1 70  ? 46.512 17.632  58.932  1.00 28.63 ? 71  ASN D ND2 1 
ATOM   4642 N  N   . LYS D  1 71  ? 45.237 16.918  64.374  1.00 31.56 ? 72  LYS D N   1 
ATOM   4643 C  CA  . LYS D  1 71  ? 44.305 17.235  65.454  1.00 34.32 ? 72  LYS D CA  1 
ATOM   4644 C  C   . LYS D  1 71  ? 45.039 17.725  66.699  1.00 34.76 ? 72  LYS D C   1 
ATOM   4645 O  O   . LYS D  1 71  ? 44.564 18.642  67.378  1.00 32.13 ? 72  LYS D O   1 
ATOM   4646 C  CB  . LYS D  1 71  ? 43.446 16.015  65.790  1.00 37.55 ? 72  LYS D CB  1 
ATOM   4647 C  CG  . LYS D  1 71  ? 42.142 16.364  66.489  1.00 45.15 ? 72  LYS D CG  1 
ATOM   4648 C  CD  . LYS D  1 71  ? 41.359 15.114  66.867  1.00 56.63 ? 72  LYS D CD  1 
ATOM   4649 C  CE  . LYS D  1 71  ? 41.011 14.273  65.645  1.00 50.30 ? 72  LYS D CE  1 
ATOM   4650 N  NZ  . LYS D  1 71  ? 41.197 12.813  65.921  1.00 56.87 ? 72  LYS D NZ  1 
ATOM   4651 N  N   . ARG D  1 72  ? 46.200 17.129  67.015  1.00 28.98 ? 73  ARG D N   1 
ATOM   4652 C  CA  . ARG D  1 72  ? 46.975 17.543  68.175  1.00 29.82 ? 73  ARG D CA  1 
ATOM   4653 C  C   . ARG D  1 72  ? 47.891 18.726  67.878  1.00 33.30 ? 73  ARG D C   1 
ATOM   4654 O  O   . ARG D  1 72  ? 48.495 19.274  68.810  1.00 31.38 ? 73  ARG D O   1 
ATOM   4655 C  CB  . ARG D  1 72  ? 47.820 16.378  68.713  1.00 30.58 ? 73  ARG D CB  1 
ATOM   4656 C  CG  . ARG D  1 72  ? 47.030 15.203  69.267  1.00 34.53 ? 73  ARG D CG  1 
ATOM   4657 C  CD  . ARG D  1 72  ? 46.146 15.594  70.461  1.00 31.80 ? 73  ARG D CD  1 
ATOM   4658 N  NE  . ARG D  1 72  ? 46.914 16.093  71.598  1.00 32.42 ? 73  ARG D NE  1 
ATOM   4659 C  CZ  . ARG D  1 72  ? 47.608 15.331  72.437  1.00 35.80 ? 73  ARG D CZ  1 
ATOM   4660 N  NH1 . ARG D  1 72  ? 47.668 14.016  72.293  1.00 36.40 ? 73  ARG D NH1 1 
ATOM   4661 N  NH2 . ARG D  1 72  ? 48.254 15.902  73.450  1.00 33.18 ? 73  ARG D NH2 1 
ATOM   4662 N  N   . GLY D  1 73  ? 48.016 19.130  66.619  1.00 30.72 ? 74  GLY D N   1 
ATOM   4663 C  CA  . GLY D  1 73  ? 48.843 20.265  66.279  1.00 29.86 ? 74  GLY D CA  1 
ATOM   4664 C  C   . GLY D  1 73  ? 50.283 19.951  65.957  1.00 35.91 ? 74  GLY D C   1 
ATOM   4665 O  O   . GLY D  1 73  ? 51.108 20.872  65.937  1.00 38.34 ? 74  GLY D O   1 
ATOM   4666 N  N   . GLY D  1 74  ? 50.623 18.684  65.726  1.00 36.38 ? 75  GLY D N   1 
ATOM   4667 C  CA  . GLY D  1 74  ? 51.923 18.342  65.192  1.00 36.56 ? 75  GLY D CA  1 
ATOM   4668 C  C   . GLY D  1 74  ? 51.940 18.448  63.677  1.00 40.22 ? 75  GLY D C   1 
ATOM   4669 O  O   . GLY D  1 74  ? 50.949 18.774  63.023  1.00 37.31 ? 75  GLY D O   1 
ATOM   4670 N  N   . ARG D  1 75  ? 53.097 18.157  63.103  1.00 37.41 ? 76  ARG D N   1 
ATOM   4671 C  CA  . ARG D  1 75  ? 53.295 18.334  61.675  1.00 35.26 ? 76  ARG D CA  1 
ATOM   4672 C  C   . ARG D  1 75  ? 53.606 16.991  61.023  1.00 33.89 ? 76  ARG D C   1 
ATOM   4673 O  O   . ARG D  1 75  ? 54.548 16.299  61.425  1.00 32.58 ? 76  ARG D O   1 
ATOM   4674 C  CB  . ARG D  1 75  ? 54.387 19.375  61.428  1.00 37.57 ? 76  ARG D CB  1 
ATOM   4675 C  CG  . ARG D  1 75  ? 53.906 20.791  61.820  1.00 43.35 ? 76  ARG D CG  1 
ATOM   4676 C  CD  . ARG D  1 75  ? 52.796 21.274  60.830  1.00 47.34 ? 76  ARG D CD  1 
ATOM   4677 N  NE  . ARG D  1 75  ? 51.881 22.276  61.379  1.00 51.61 ? 76  ARG D NE  1 
ATOM   4678 C  CZ  . ARG D  1 75  ? 50.653 22.030  61.832  1.00 53.90 ? 76  ARG D CZ  1 
ATOM   4679 N  NH1 . ARG D  1 75  ? 50.127 20.812  61.802  1.00 47.75 ? 76  ARG D NH1 1 
ATOM   4680 N  NH2 . ARG D  1 75  ? 49.930 23.034  62.330  1.00 49.37 ? 76  ARG D NH2 1 
ATOM   4681 N  N   . ILE D  1 76  ? 52.796 16.619  60.031  1.00 35.21 ? 77  ILE D N   1 
ATOM   4682 C  CA  . ILE D  1 76  ? 53.013 15.377  59.296  1.00 33.32 ? 77  ILE D CA  1 
ATOM   4683 C  C   . ILE D  1 76  ? 54.269 15.495  58.445  1.00 34.68 ? 77  ILE D C   1 
ATOM   4684 O  O   . ILE D  1 76  ? 54.410 16.440  57.657  1.00 40.22 ? 77  ILE D O   1 
ATOM   4685 C  CB  . ILE D  1 76  ? 51.809 15.065  58.404  1.00 31.20 ? 77  ILE D CB  1 
ATOM   4686 C  CG1 . ILE D  1 76  ? 50.536 14.896  59.234  1.00 31.15 ? 77  ILE D CG1 1 
ATOM   4687 C  CG2 . ILE D  1 76  ? 52.121 13.849  57.534  1.00 28.96 ? 77  ILE D CG2 1 
ATOM   4688 C  CD1 . ILE D  1 76  ? 49.290 14.999  58.384  1.00 31.10 ? 77  ILE D CD1 1 
ATOM   4689 N  N   . VAL D  1 77  ? 55.170 14.520  58.568  1.00 31.71 ? 78  VAL D N   1 
ATOM   4690 C  CA  . VAL D  1 77  ? 56.390 14.454  57.759  1.00 33.85 ? 78  VAL D CA  1 
ATOM   4691 C  C   . VAL D  1 77  ? 56.394 13.101  57.058  1.00 32.78 ? 78  VAL D C   1 
ATOM   4692 O  O   . VAL D  1 77  ? 56.604 12.063  57.702  1.00 34.99 ? 78  VAL D O   1 
ATOM   4693 C  CB  . VAL D  1 77  ? 57.662 14.648  58.603  1.00 35.53 ? 78  VAL D CB  1 
ATOM   4694 C  CG1 . VAL D  1 77  ? 58.920 14.443  57.752  1.00 30.59 ? 78  VAL D CG1 1 
ATOM   4695 C  CG2 . VAL D  1 77  ? 57.669 16.033  59.254  1.00 36.04 ? 78  VAL D CG2 1 
ATOM   4696 N  N   . LEU D  1 78  ? 56.150 13.104  55.747  1.00 33.52 ? 79  LEU D N   1 
ATOM   4697 C  CA  . LEU D  1 78  ? 56.055 11.869  54.979  1.00 32.30 ? 79  LEU D CA  1 
ATOM   4698 C  C   . LEU D  1 78  ? 57.434 11.443  54.482  1.00 37.44 ? 79  LEU D C   1 
ATOM   4699 O  O   . LEU D  1 78  ? 58.226 12.272  54.031  1.00 37.35 ? 79  LEU D O   1 
ATOM   4700 C  CB  . LEU D  1 78  ? 55.084 12.048  53.808  1.00 33.30 ? 79  LEU D CB  1 
ATOM   4701 C  CG  . LEU D  1 78  ? 53.662 12.384  54.279  1.00 32.76 ? 79  LEU D CG  1 
ATOM   4702 C  CD1 . LEU D  1 78  ? 52.719 12.557  53.105  1.00 35.45 ? 79  LEU D CD1 1 
ATOM   4703 C  CD2 . LEU D  1 78  ? 53.142 11.285  55.214  1.00 32.07 ? 79  LEU D CD2 1 
ATOM   4704 N  N   . GLN D  1 79  ? 57.722 10.148  54.598  1.00 37.22 ? 80  GLN D N   1 
ATOM   4705 C  CA  . GLN D  1 79  ? 59.001 9.554   54.221  1.00 35.79 ? 80  GLN D CA  1 
ATOM   4706 C  C   . GLN D  1 79  ? 58.808 8.619   53.027  1.00 34.39 ? 80  GLN D C   1 
ATOM   4707 O  O   . GLN D  1 79  ? 57.686 8.260   52.666  1.00 27.86 ? 80  GLN D O   1 
ATOM   4708 C  CB  . GLN D  1 79  ? 59.602 8.782   55.403  1.00 37.34 ? 80  GLN D CB  1 
ATOM   4709 C  CG  . GLN D  1 79  ? 60.382 9.621   56.443  1.00 43.79 ? 80  GLN D CG  1 
ATOM   4710 C  CD  . GLN D  1 79  ? 61.397 10.579  55.825  1.00 56.45 ? 80  GLN D CD  1 
ATOM   4711 O  OE1 . GLN D  1 79  ? 61.042 11.661  55.349  1.00 61.72 ? 80  GLN D OE1 1 
ATOM   4712 N  NE2 . GLN D  1 79  ? 62.672 10.177  55.820  1.00 62.01 ? 80  GLN D NE2 1 
ATOM   4713 N  N   . GLN D  1 80  ? 59.922 8.216   52.413  1.00 34.39 ? 81  GLN D N   1 
ATOM   4714 C  CA  . GLN D  1 80  ? 59.851 7.213   51.355  1.00 34.64 ? 81  GLN D CA  1 
ATOM   4715 C  C   . GLN D  1 80  ? 59.220 5.926   51.881  1.00 30.96 ? 81  GLN D C   1 
ATOM   4716 O  O   . GLN D  1 80  ? 59.352 5.568   53.058  1.00 27.39 ? 81  GLN D O   1 
ATOM   4717 C  CB  . GLN D  1 80  ? 61.240 6.914   50.771  1.00 31.98 ? 81  GLN D CB  1 
ATOM   4718 C  CG  . GLN D  1 80  ? 62.198 6.163   51.691  1.00 42.30 ? 81  GLN D CG  1 
ATOM   4719 C  CD  . GLN D  1 80  ? 62.812 7.042   52.790  1.00 50.81 ? 81  GLN D CD  1 
ATOM   4720 O  OE1 . GLN D  1 80  ? 62.576 8.262   52.856  1.00 51.52 ? 81  GLN D OE1 1 
ATOM   4721 N  NE2 . GLN D  1 80  ? 63.608 6.418   53.659  1.00 50.26 ? 81  GLN D NE2 1 
ATOM   4722 N  N   . ILE D  1 81  ? 58.492 5.253   51.000  1.00 24.82 ? 82  ILE D N   1 
ATOM   4723 C  CA  . ILE D  1 81  ? 57.899 3.961   51.299  1.00 31.13 ? 82  ILE D CA  1 
ATOM   4724 C  C   . ILE D  1 81  ? 58.746 2.904   50.609  1.00 28.16 ? 82  ILE D C   1 
ATOM   4725 O  O   . ILE D  1 81  ? 58.823 2.875   49.377  1.00 27.48 ? 82  ILE D O   1 
ATOM   4726 C  CB  . ILE D  1 81  ? 56.433 3.888   50.849  1.00 27.61 ? 82  ILE D CB  1 
ATOM   4727 C  CG1 . ILE D  1 81  ? 55.626 5.033   51.460  1.00 25.14 ? 82  ILE D CG1 1 
ATOM   4728 C  CG2 . ILE D  1 81  ? 55.828 2.508   51.216  1.00 28.63 ? 82  ILE D CG2 1 
ATOM   4729 C  CD1 . ILE D  1 81  ? 54.298 5.330   50.696  1.00 25.16 ? 82  ILE D CD1 1 
ATOM   4730 N  N   . ALA D  1 82  ? 59.382 2.050   51.409  1.00 28.75 ? 83  ALA D N   1 
ATOM   4731 C  CA  . ALA D  1 82  ? 60.272 1.018   50.895  1.00 29.64 ? 83  ALA D CA  1 
ATOM   4732 C  C   . ALA D  1 82  ? 59.513 0.039   50.006  1.00 27.14 ? 83  ALA D C   1 
ATOM   4733 O  O   . ALA D  1 82  ? 58.345 -0.271  50.256  1.00 30.65 ? 83  ALA D O   1 
ATOM   4734 C  CB  . ALA D  1 82  ? 60.925 0.262   52.065  1.00 23.49 ? 83  ALA D CB  1 
ATOM   4735 N  N   . ALA D  1 83  ? 60.182 -0.439  48.957  1.00 27.50 ? 84  ALA D N   1 
ATOM   4736 C  CA  . ALA D  1 83  ? 59.666 -1.565  48.192  1.00 27.72 ? 84  ALA D CA  1 
ATOM   4737 C  C   . ALA D  1 83  ? 59.391 -2.754  49.114  1.00 28.49 ? 84  ALA D C   1 
ATOM   4738 O  O   . ALA D  1 83  ? 60.104 -2.963  50.104  1.00 30.24 ? 84  ALA D O   1 
ATOM   4739 C  CB  . ALA D  1 83  ? 60.656 -1.987  47.109  1.00 26.19 ? 84  ALA D CB  1 
ATOM   4740 N  N   . PRO D  1 84  ? 58.363 -3.546  48.816  1.00 28.81 ? 85  PRO D N   1 
ATOM   4741 C  CA  . PRO D  1 84  ? 58.115 -4.765  49.610  1.00 30.56 ? 85  PRO D CA  1 
ATOM   4742 C  C   . PRO D  1 84  ? 59.328 -5.668  49.588  1.00 34.18 ? 85  PRO D C   1 
ATOM   4743 O  O   . PRO D  1 84  ? 60.090 -5.672  48.621  1.00 33.60 ? 85  PRO D O   1 
ATOM   4744 C  CB  . PRO D  1 84  ? 56.927 -5.433  48.900  1.00 27.31 ? 85  PRO D CB  1 
ATOM   4745 C  CG  . PRO D  1 84  ? 56.237 -4.302  48.163  1.00 32.37 ? 85  PRO D CG  1 
ATOM   4746 C  CD  . PRO D  1 84  ? 57.342 -3.329  47.773  1.00 27.24 ? 85  PRO D CD  1 
ATOM   4747 N  N   . SER D  1 85  ? 59.472 -6.466  50.657  1.00 35.44 ? 86  SER D N   1 
ATOM   4748 C  CA  . SER D  1 85  ? 60.640 -7.330  50.823  1.00 42.35 ? 86  SER D CA  1 
ATOM   4749 C  C   . SER D  1 85  ? 60.763 -8.382  49.730  1.00 39.18 ? 86  SER D C   1 
ATOM   4750 O  O   . SER D  1 85  ? 61.869 -8.869  49.494  1.00 44.92 ? 86  SER D O   1 
ATOM   4751 C  CB  . SER D  1 85  ? 60.612 -8.021  52.191  1.00 39.50 ? 86  SER D CB  1 
ATOM   4752 O  OG  . SER D  1 85  ? 59.458 -8.836  52.335  1.00 45.89 ? 86  SER D OG  1 
ATOM   4753 N  N   . MET D  1 86  ? 59.669 -8.735  49.056  1.00 39.20 ? 87  MET D N   1 
ATOM   4754 C  CA  . MET D  1 86  ? 59.678 -9.708  47.967  1.00 39.64 ? 87  MET D CA  1 
ATOM   4755 C  C   . MET D  1 86  ? 58.853 -9.165  46.811  1.00 37.59 ? 87  MET D C   1 
ATOM   4756 O  O   . MET D  1 86  ? 57.936 -8.364  47.004  1.00 37.87 ? 87  MET D O   1 
ATOM   4757 C  CB  . MET D  1 86  ? 59.068 -11.072 48.371  1.00 41.05 ? 87  MET D CB  1 
ATOM   4758 C  CG  . MET D  1 86  ? 59.717 -11.802 49.545  1.00 42.83 ? 87  MET D CG  1 
ATOM   4759 S  SD  . MET D  1 86  ? 61.348 -12.472 49.155  1.00 59.79 ? 87  MET D SD  1 
ATOM   4760 C  CE  . MET D  1 86  ? 60.922 -14.091 48.486  1.00 43.30 ? 87  MET D CE  1 
ATOM   4761 N  N   . GLN D  1 87  ? 59.172 -9.621  45.605  1.00 37.18 ? 88  GLN D N   1 
ATOM   4762 C  CA  . GLN D  1 87  ? 58.254 -9.466  44.487  1.00 40.29 ? 88  GLN D CA  1 
ATOM   4763 C  C   . GLN D  1 87  ? 57.315 -10.667 44.353  1.00 43.67 ? 88  GLN D C   1 
ATOM   4764 O  O   . GLN D  1 87  ? 56.163 -10.501 43.936  1.00 38.61 ? 88  GLN D O   1 
ATOM   4765 C  CB  . GLN D  1 87  ? 59.035 -9.268  43.180  1.00 41.44 ? 88  GLN D CB  1 
ATOM   4766 C  CG  . GLN D  1 87  ? 60.055 -8.132  43.180  1.00 37.31 ? 88  GLN D CG  1 
ATOM   4767 C  CD  . GLN D  1 87  ? 59.414 -6.736  43.258  1.00 44.24 ? 88  GLN D CD  1 
ATOM   4768 O  OE1 . GLN D  1 87  ? 58.217 -6.552  42.994  1.00 40.61 ? 88  GLN D OE1 1 
ATOM   4769 N  NE2 . GLN D  1 87  ? 60.225 -5.745  43.602  1.00 40.22 ? 88  GLN D NE2 1 
ATOM   4770 N  N   . GLU D  1 88  ? 57.787 -11.866 44.706  1.00 35.69 ? 89  GLU D N   1 
ATOM   4771 C  CA  . GLU D  1 88  ? 57.009 -13.097 44.651  1.00 39.93 ? 89  GLU D CA  1 
ATOM   4772 C  C   . GLU D  1 88  ? 56.942 -13.728 46.034  1.00 38.95 ? 89  GLU D C   1 
ATOM   4773 O  O   . GLU D  1 88  ? 57.964 -13.837 46.719  1.00 39.34 ? 89  GLU D O   1 
ATOM   4774 C  CB  . GLU D  1 88  ? 57.626 -14.099 43.673  1.00 41.59 ? 89  GLU D CB  1 
ATOM   4775 C  CG  . GLU D  1 88  ? 57.997 -13.510 42.325  1.00 45.76 ? 89  GLU D CG  1 
ATOM   4776 C  CD  . GLU D  1 88  ? 58.521 -14.566 41.366  1.00 62.89 ? 89  GLU D CD  1 
ATOM   4777 O  OE1 . GLU D  1 88  ? 58.942 -15.647 41.853  1.00 66.49 ? 89  GLU D OE1 1 
ATOM   4778 O  OE2 . GLU D  1 88  ? 58.498 -14.323 40.134  1.00 64.12 ? 89  GLU D OE2 1 
ATOM   4779 N  N   . TRP D  1 89  ? 55.750 -14.180 46.432  1.00 36.04 ? 90  TRP D N   1 
ATOM   4780 C  CA  . TRP D  1 89  ? 55.513 -14.622 47.805  1.00 37.85 ? 90  TRP D CA  1 
ATOM   4781 C  C   . TRP D  1 89  ? 55.338 -16.131 47.948  1.00 39.88 ? 90  TRP D C   1 
ATOM   4782 O  O   . TRP D  1 89  ? 54.907 -16.591 49.011  1.00 42.78 ? 90  TRP D O   1 
ATOM   4783 C  CB  . TRP D  1 89  ? 54.305 -13.885 48.381  1.00 30.41 ? 90  TRP D CB  1 
ATOM   4784 C  CG  . TRP D  1 89  ? 54.550 -12.425 48.358  1.00 35.56 ? 90  TRP D CG  1 
ATOM   4785 C  CD1 . TRP D  1 89  ? 54.202 -11.543 47.363  1.00 34.88 ? 90  TRP D CD1 1 
ATOM   4786 C  CD2 . TRP D  1 89  ? 55.235 -11.658 49.357  1.00 35.14 ? 90  TRP D CD2 1 
ATOM   4787 N  NE1 . TRP D  1 89  ? 54.621 -10.274 47.692  1.00 32.66 ? 90  TRP D NE1 1 
ATOM   4788 C  CE2 . TRP D  1 89  ? 55.258 -10.316 48.910  1.00 36.42 ? 90  TRP D CE2 1 
ATOM   4789 C  CE3 . TRP D  1 89  ? 55.824 -11.973 50.591  1.00 31.72 ? 90  TRP D CE3 1 
ATOM   4790 C  CZ2 . TRP D  1 89  ? 55.859 -9.292  49.651  1.00 32.33 ? 90  TRP D CZ2 1 
ATOM   4791 C  CZ3 . TRP D  1 89  ? 56.416 -10.956 51.328  1.00 33.86 ? 90  TRP D CZ3 1 
ATOM   4792 C  CH2 . TRP D  1 89  ? 56.432 -9.631  50.853  1.00 35.27 ? 90  TRP D CH2 1 
ATOM   4793 N  N   . GLY D  1 90  ? 55.676 -16.913 46.927  1.00 40.93 ? 91  GLY D N   1 
ATOM   4794 C  CA  . GLY D  1 90  ? 55.673 -18.366 47.092  1.00 37.81 ? 91  GLY D CA  1 
ATOM   4795 C  C   . GLY D  1 90  ? 54.270 -18.926 47.276  1.00 43.45 ? 91  GLY D C   1 
ATOM   4796 O  O   . GLY D  1 90  ? 53.358 -18.633 46.495  1.00 43.64 ? 91  GLY D O   1 
ATOM   4797 N  N   . THR D  1 91  ? 54.080 -19.753 48.303  1.00 38.93 ? 92  THR D N   1 
ATOM   4798 C  CA  . THR D  1 91  ? 52.776 -20.371 48.516  1.00 41.60 ? 92  THR D CA  1 
ATOM   4799 C  C   . THR D  1 91  ? 51.864 -19.463 49.338  1.00 39.92 ? 92  THR D C   1 
ATOM   4800 O  O   . THR D  1 91  ? 52.286 -18.448 49.897  1.00 38.16 ? 92  THR D O   1 
ATOM   4801 C  CB  . THR D  1 91  ? 52.912 -21.720 49.221  1.00 41.10 ? 92  THR D CB  1 
ATOM   4802 O  OG1 . THR D  1 91  ? 53.479 -21.529 50.530  1.00 39.44 ? 92  THR D OG1 1 
ATOM   4803 C  CG2 . THR D  1 91  ? 53.786 -22.669 48.397  1.00 39.29 ? 92  THR D CG2 1 
ATOM   4804 N  N   . GLY D  1 92  ? 50.588 -19.852 49.404  1.00 41.57 ? 93  GLY D N   1 
ATOM   4805 C  CA  . GLY D  1 92  ? 49.657 -19.170 50.292  1.00 38.00 ? 93  GLY D CA  1 
ATOM   4806 C  C   . GLY D  1 92  ? 50.087 -19.246 51.745  1.00 35.55 ? 93  GLY D C   1 
ATOM   4807 O  O   . GLY D  1 92  ? 49.950 -18.273 52.497  1.00 34.78 ? 93  GLY D O   1 
ATOM   4808 N  N   . LEU D  1 93  ? 50.635 -20.395 52.155  1.00 33.10 ? 94  LEU D N   1 
ATOM   4809 C  CA  . LEU D  1 93  ? 51.129 -20.530 53.520  1.00 34.29 ? 94  LEU D CA  1 
ATOM   4810 C  C   . LEU D  1 93  ? 52.238 -19.524 53.798  1.00 34.65 ? 94  LEU D C   1 
ATOM   4811 O  O   . LEU D  1 93  ? 52.189 -18.796 54.795  1.00 32.97 ? 94  LEU D O   1 
ATOM   4812 C  CB  . LEU D  1 93  ? 51.615 -21.954 53.774  1.00 32.41 ? 94  LEU D CB  1 
ATOM   4813 C  CG  . LEU D  1 93  ? 52.173 -22.214 55.182  1.00 36.92 ? 94  LEU D CG  1 
ATOM   4814 C  CD1 . LEU D  1 93  ? 51.260 -21.658 56.272  1.00 32.10 ? 94  LEU D CD1 1 
ATOM   4815 C  CD2 . LEU D  1 93  ? 52.427 -23.701 55.421  1.00 32.31 ? 94  LEU D CD2 1 
ATOM   4816 N  N   . GLU D  1 94  ? 53.224 -19.442 52.896  1.00 36.69 ? 95  GLU D N   1 
ATOM   4817 C  CA  . GLU D  1 94  ? 54.364 -18.543 53.083  1.00 40.68 ? 95  GLU D CA  1 
ATOM   4818 C  C   . GLU D  1 94  ? 53.930 -17.083 53.135  1.00 34.34 ? 95  GLU D C   1 
ATOM   4819 O  O   . GLU D  1 94  ? 54.475 -16.295 53.918  1.00 36.64 ? 95  GLU D O   1 
ATOM   4820 C  CB  . GLU D  1 94  ? 55.389 -18.763 51.964  1.00 39.80 ? 95  GLU D CB  1 
ATOM   4821 C  CG  . GLU D  1 94  ? 55.990 -20.167 51.985  1.00 45.08 ? 95  GLU D CG  1 
ATOM   4822 C  CD  . GLU D  1 94  ? 56.879 -20.481 50.780  1.00 52.85 ? 95  GLU D CD  1 
ATOM   4823 O  OE1 . GLU D  1 94  ? 56.416 -20.332 49.624  1.00 52.85 ? 95  GLU D OE1 1 
ATOM   4824 O  OE2 . GLU D  1 94  ? 58.037 -20.906 50.992  1.00 60.26 ? 95  GLU D OE2 1 
ATOM   4825 N  N   . ALA D  1 95  ? 52.945 -16.704 52.319  1.00 30.97 ? 96  ALA D N   1 
ATOM   4826 C  CA  . ALA D  1 95  ? 52.435 -15.341 52.374  1.00 32.85 ? 96  ALA D CA  1 
ATOM   4827 C  C   . ALA D  1 95  ? 51.799 -15.044 53.727  1.00 33.86 ? 96  ALA D C   1 
ATOM   4828 O  O   . ALA D  1 95  ? 51.964 -13.943 54.272  1.00 32.62 ? 96  ALA D O   1 
ATOM   4829 C  CB  . ALA D  1 95  ? 51.426 -15.105 51.251  1.00 31.90 ? 96  ALA D CB  1 
ATOM   4830 N  N   . LEU D  1 96  ? 51.045 -16.009 54.271  1.00 33.28 ? 97  LEU D N   1 
ATOM   4831 C  CA  . LEU D  1 96  ? 50.400 -15.816 55.566  1.00 33.29 ? 97  LEU D CA  1 
ATOM   4832 C  C   . LEU D  1 96  ? 51.429 -15.750 56.682  1.00 31.85 ? 97  LEU D C   1 
ATOM   4833 O  O   . LEU D  1 96  ? 51.287 -14.960 57.620  1.00 32.84 ? 97  LEU D O   1 
ATOM   4834 C  CB  . LEU D  1 96  ? 49.400 -16.940 55.838  1.00 32.20 ? 97  LEU D CB  1 
ATOM   4835 C  CG  . LEU D  1 96  ? 48.076 -16.925 55.083  1.00 33.91 ? 97  LEU D CG  1 
ATOM   4836 C  CD1 . LEU D  1 96  ? 47.283 -18.186 55.404  1.00 31.10 ? 97  LEU D CD1 1 
ATOM   4837 C  CD2 . LEU D  1 96  ? 47.290 -15.670 55.431  1.00 31.60 ? 97  LEU D CD2 1 
ATOM   4838 N  N   . GLN D  1 97  ? 52.483 -16.560 56.596  1.00 31.51 ? 98  GLN D N   1 
ATOM   4839 C  CA  . GLN D  1 97  ? 53.545 -16.459 57.592  1.00 34.38 ? 98  GLN D CA  1 
ATOM   4840 C  C   . GLN D  1 97  ? 54.241 -15.102 57.520  1.00 34.47 ? 98  GLN D C   1 
ATOM   4841 O  O   . GLN D  1 97  ? 54.546 -14.499 58.556  1.00 33.46 ? 98  GLN D O   1 
ATOM   4842 C  CB  . GLN D  1 97  ? 54.534 -17.606 57.416  1.00 31.20 ? 98  GLN D CB  1 
ATOM   4843 C  CG  . GLN D  1 97  ? 53.917 -18.969 57.773  1.00 35.58 ? 98  GLN D CG  1 
ATOM   4844 C  CD  . GLN D  1 97  ? 54.723 -20.142 57.227  1.00 40.78 ? 98  GLN D CD  1 
ATOM   4845 O  OE1 . GLN D  1 97  ? 55.316 -20.051 56.150  1.00 43.55 ? 98  GLN D OE1 1 
ATOM   4846 N  NE2 . GLN D  1 97  ? 54.765 -21.245 57.983  1.00 44.01 ? 98  GLN D NE2 1 
ATOM   4847 N  N   . ALA D  1 98  ? 54.466 -14.588 56.305  1.00 32.47 ? 99  ALA D N   1 
ATOM   4848 C  CA  . ALA D  1 98  ? 54.999 -13.235 56.170  1.00 32.79 ? 99  ALA D CA  1 
ATOM   4849 C  C   . ALA D  1 98  ? 54.067 -12.196 56.792  1.00 33.43 ? 99  ALA D C   1 
ATOM   4850 O  O   . ALA D  1 98  ? 54.528 -11.283 57.482  1.00 34.68 ? 99  ALA D O   1 
ATOM   4851 C  CB  . ALA D  1 98  ? 55.254 -12.908 54.699  1.00 35.57 ? 99  ALA D CB  1 
ATOM   4852 N  N   . ALA D  1 99  ? 52.754 -12.315 56.565  1.00 31.72 ? 100 ALA D N   1 
ATOM   4853 C  CA  . ALA D  1 99  ? 51.825 -11.331 57.109  1.00 30.27 ? 100 ALA D CA  1 
ATOM   4854 C  C   . ALA D  1 99  ? 51.782 -11.393 58.632  1.00 34.28 ? 100 ALA D C   1 
ATOM   4855 O  O   . ALA D  1 99  ? 51.710 -10.354 59.300  1.00 34.41 ? 100 ALA D O   1 
ATOM   4856 C  CB  . ALA D  1 99  ? 50.427 -11.539 56.516  1.00 29.95 ? 100 ALA D CB  1 
ATOM   4857 N  N   . LEU D  1 100 ? 51.828 -12.600 59.202  1.00 34.50 ? 101 LEU D N   1 
ATOM   4858 C  CA  . LEU D  1 100 ? 51.852 -12.719 60.657  1.00 38.87 ? 101 LEU D CA  1 
ATOM   4859 C  C   . LEU D  1 100 ? 53.070 -12.017 61.253  1.00 33.45 ? 101 LEU D C   1 
ATOM   4860 O  O   . LEU D  1 100 ? 52.951 -11.304 62.252  1.00 38.80 ? 101 LEU D O   1 
ATOM   4861 C  CB  . LEU D  1 100 ? 51.821 -14.193 61.073  1.00 34.33 ? 101 LEU D CB  1 
ATOM   4862 C  CG  . LEU D  1 100 ? 51.963 -14.429 62.577  1.00 36.92 ? 101 LEU D CG  1 
ATOM   4863 C  CD1 . LEU D  1 100 ? 50.731 -13.916 63.322  1.00 34.74 ? 101 LEU D CD1 1 
ATOM   4864 C  CD2 . LEU D  1 100 ? 52.198 -15.901 62.873  1.00 38.76 ? 101 LEU D CD2 1 
ATOM   4865 N  N   . ASP D  1 101 ? 54.251 -12.200 60.656  1.00 33.28 ? 102 ASP D N   1 
ATOM   4866 C  CA  . ASP D  1 101 ? 55.440 -11.518 61.174  1.00 39.05 ? 102 ASP D CA  1 
ATOM   4867 C  C   . ASP D  1 101 ? 55.334 -10.003 61.005  1.00 41.40 ? 102 ASP D C   1 
ATOM   4868 O  O   . ASP D  1 101 ? 55.755 -9.240  61.887  1.00 36.43 ? 102 ASP D O   1 
ATOM   4869 C  CB  . ASP D  1 101 ? 56.702 -12.056 60.492  1.00 41.41 ? 102 ASP D CB  1 
ATOM   4870 C  CG  . ASP D  1 101 ? 57.042 -13.485 60.933  1.00 64.45 ? 102 ASP D CG  1 
ATOM   4871 O  OD1 . ASP D  1 101 ? 56.308 -14.031 61.799  1.00 70.65 ? 102 ASP D OD1 1 
ATOM   4872 O  OD2 . ASP D  1 101 ? 58.025 -14.074 60.411  1.00 74.18 ? 102 ASP D OD2 1 
ATOM   4873 N  N   . LEU D  1 102 ? 54.754 -9.554  59.888  1.00 35.40 ? 103 LEU D N   1 
ATOM   4874 C  CA  . LEU D  1 102 ? 54.538 -8.129  59.665  1.00 33.18 ? 103 LEU D CA  1 
ATOM   4875 C  C   . LEU D  1 102 ? 53.604 -7.533  60.716  1.00 35.67 ? 103 LEU D C   1 
ATOM   4876 O  O   . LEU D  1 102 ? 53.884 -6.462  61.277  1.00 28.51 ? 103 LEU D O   1 
ATOM   4877 C  CB  . LEU D  1 102 ? 53.981 -7.912  58.263  1.00 34.43 ? 103 LEU D CB  1 
ATOM   4878 C  CG  . LEU D  1 102 ? 53.895 -6.471  57.785  1.00 37.90 ? 103 LEU D CG  1 
ATOM   4879 C  CD1 . LEU D  1 102 ? 55.281 -5.853  57.742  1.00 41.58 ? 103 LEU D CD1 1 
ATOM   4880 C  CD2 . LEU D  1 102 ? 53.258 -6.450  56.411  1.00 39.85 ? 103 LEU D CD2 1 
ATOM   4881 N  N   . GLU D  1 103 ? 52.481 -8.213  61.001  1.00 32.71 ? 104 GLU D N   1 
ATOM   4882 C  CA  . GLU D  1 103 ? 51.543 -7.657  61.980  1.00 36.38 ? 104 GLU D CA  1 
ATOM   4883 C  C   . GLU D  1 103 ? 52.120 -7.695  63.390  1.00 34.09 ? 104 GLU D C   1 
ATOM   4884 O  O   . GLU D  1 103 ? 51.826 -6.809  64.199  1.00 32.14 ? 104 GLU D O   1 
ATOM   4885 C  CB  . GLU D  1 103 ? 50.197 -8.386  61.937  1.00 36.06 ? 104 GLU D CB  1 
ATOM   4886 C  CG  . GLU D  1 103 ? 49.540 -8.445  60.554  1.00 41.08 ? 104 GLU D CG  1 
ATOM   4887 C  CD  . GLU D  1 103 ? 48.898 -7.124  60.098  1.00 50.39 ? 104 GLU D CD  1 
ATOM   4888 O  OE1 . GLU D  1 103 ? 49.123 -6.066  60.724  1.00 52.29 ? 104 GLU D OE1 1 
ATOM   4889 O  OE2 . GLU D  1 103 ? 48.172 -7.141  59.078  1.00 60.43 ? 104 GLU D OE2 1 
ATOM   4890 N  N   . LYS D  1 104 ? 52.970 -8.679  63.690  1.00 31.51 ? 105 LYS D N   1 
ATOM   4891 C  CA  . LYS D  1 104 ? 53.605 -8.709  65.002  1.00 33.69 ? 105 LYS D CA  1 
ATOM   4892 C  C   . LYS D  1 104 ? 54.571 -7.545  65.167  1.00 34.48 ? 105 LYS D C   1 
ATOM   4893 O  O   . LYS D  1 104 ? 54.670 -6.960  66.252  1.00 31.37 ? 105 LYS D O   1 
ATOM   4894 C  CB  . LYS D  1 104 ? 54.339 -10.026 65.199  1.00 33.15 ? 105 LYS D CB  1 
ATOM   4895 C  CG  . LYS D  1 104 ? 53.481 -11.142 65.698  1.00 36.31 ? 105 LYS D CG  1 
ATOM   4896 C  CD  . LYS D  1 104 ? 54.358 -12.309 66.071  1.00 41.56 ? 105 LYS D CD  1 
ATOM   4897 C  CE  . LYS D  1 104 ? 53.558 -13.523 66.458  1.00 44.18 ? 105 LYS D CE  1 
ATOM   4898 N  NZ  . LYS D  1 104 ? 54.337 -14.773 66.128  1.00 50.12 ? 105 LYS D NZ  1 
ATOM   4899 N  N   . GLN D  1 105 ? 55.298 -7.203  64.101  1.00 31.97 ? 106 GLN D N   1 
ATOM   4900 C  CA  . GLN D  1 105 ? 56.222 -6.072  64.156  1.00 34.54 ? 106 GLN D CA  1 
ATOM   4901 C  C   . GLN D  1 105 ? 55.477 -4.755  64.316  1.00 30.61 ? 106 GLN D C   1 
ATOM   4902 O  O   . GLN D  1 105 ? 55.941 -3.857  65.025  1.00 36.76 ? 106 GLN D O   1 
ATOM   4903 C  CB  . GLN D  1 105 ? 57.078 -6.033  62.894  1.00 38.68 ? 106 GLN D CB  1 
ATOM   4904 C  CG  . GLN D  1 105 ? 58.207 -7.039  62.870  1.00 51.41 ? 106 GLN D CG  1 
ATOM   4905 C  CD  . GLN D  1 105 ? 59.150 -6.784  61.715  1.00 65.01 ? 106 GLN D CD  1 
ATOM   4906 O  OE1 . GLN D  1 105 ? 58.890 -5.919  60.868  1.00 66.94 ? 106 GLN D OE1 1 
ATOM   4907 N  NE2 . GLN D  1 105 ? 60.250 -7.534  61.667  1.00 68.91 ? 106 GLN D NE2 1 
ATOM   4908 N  N   . VAL D  1 106 ? 54.337 -4.611  63.643  1.00 27.76 ? 107 VAL D N   1 
ATOM   4909 C  CA  . VAL D  1 106 ? 53.521 -3.418  63.821  1.00 33.30 ? 107 VAL D CA  1 
ATOM   4910 C  C   . VAL D  1 106 ? 52.978 -3.346  65.245  1.00 32.16 ? 107 VAL D C   1 
ATOM   4911 O  O   . VAL D  1 106 ? 53.003 -2.283  65.879  1.00 34.67 ? 107 VAL D O   1 
ATOM   4912 C  CB  . VAL D  1 106 ? 52.385 -3.386  62.784  1.00 31.05 ? 107 VAL D CB  1 
ATOM   4913 C  CG1 . VAL D  1 106 ? 51.356 -2.329  63.182  1.00 33.12 ? 107 VAL D CG1 1 
ATOM   4914 C  CG2 . VAL D  1 106 ? 52.942 -3.087  61.396  1.00 27.32 ? 107 VAL D CG2 1 
ATOM   4915 N  N   . ASN D  1 107 ? 52.468 -4.472  65.762  1.00 31.38 ? 108 ASN D N   1 
ATOM   4916 C  CA  . ASN D  1 107 ? 51.990 -4.516  67.139  1.00 33.28 ? 108 ASN D CA  1 
ATOM   4917 C  C   . ASN D  1 107 ? 53.080 -4.075  68.112  1.00 33.54 ? 108 ASN D C   1 
ATOM   4918 O  O   . ASN D  1 107 ? 52.840 -3.269  69.018  1.00 30.77 ? 108 ASN D O   1 
ATOM   4919 C  CB  . ASN D  1 107 ? 51.512 -5.932  67.475  1.00 36.53 ? 108 ASN D CB  1 
ATOM   4920 C  CG  . ASN D  1 107 ? 50.652 -5.979  68.730  1.00 37.20 ? 108 ASN D CG  1 
ATOM   4921 O  OD1 . ASN D  1 107 ? 49.908 -5.045  69.017  1.00 35.60 ? 108 ASN D OD1 1 
ATOM   4922 N  ND2 . ASN D  1 107 ? 50.744 -7.073  69.473  1.00 39.36 ? 108 ASN D ND2 1 
ATOM   4923 N  N   . GLN D  1 108 ? 54.290 -4.596  67.930  1.00 32.35 ? 109 GLN D N   1 
ATOM   4924 C  CA  . GLN D  1 108 ? 55.387 -4.264  68.828  1.00 37.77 ? 109 GLN D CA  1 
ATOM   4925 C  C   . GLN D  1 108 ? 55.670 -2.763  68.797  1.00 39.78 ? 109 GLN D C   1 
ATOM   4926 O  O   . GLN D  1 108 ? 55.796 -2.119  69.843  1.00 37.57 ? 109 GLN D O   1 
ATOM   4927 C  CB  . GLN D  1 108 ? 56.632 -5.074  68.440  1.00 37.72 ? 109 GLN D CB  1 
ATOM   4928 C  CG  . GLN D  1 108 ? 57.835 -4.820  69.314  1.00 43.47 ? 109 GLN D CG  1 
ATOM   4929 C  CD  . GLN D  1 108 ? 57.531 -5.025  70.797  1.00 59.45 ? 109 GLN D CD  1 
ATOM   4930 O  OE1 . GLN D  1 108 ? 56.902 -6.017  71.181  1.00 65.40 ? 109 GLN D OE1 1 
ATOM   4931 N  NE2 . GLN D  1 108 ? 57.975 -4.082  71.637  1.00 57.01 ? 109 GLN D NE2 1 
ATOM   4932 N  N   . SER D  1 109 ? 55.742 -2.187  67.598  1.00 35.35 ? 110 SER D N   1 
ATOM   4933 C  CA  . SER D  1 109 ? 55.984 -0.755  67.484  1.00 37.27 ? 110 SER D CA  1 
ATOM   4934 C  C   . SER D  1 109 ? 54.864 0.054   68.146  1.00 39.35 ? 110 SER D C   1 
ATOM   4935 O  O   . SER D  1 109 ? 55.133 1.077   68.792  1.00 35.95 ? 110 SER D O   1 
ATOM   4936 C  CB  . SER D  1 109 ? 56.155 -0.387  66.006  1.00 35.58 ? 110 SER D CB  1 
ATOM   4937 O  OG  . SER D  1 109 ? 56.025 1.004   65.803  1.00 48.94 ? 110 SER D OG  1 
ATOM   4938 N  N   . LEU D  1 110 ? 53.603 -0.401  68.026  1.00 35.60 ? 111 LEU D N   1 
ATOM   4939 C  CA  . LEU D  1 110 ? 52.497 0.299   68.691  1.00 35.96 ? 111 LEU D CA  1 
ATOM   4940 C  C   . LEU D  1 110 ? 52.613 0.242   70.214  1.00 36.33 ? 111 LEU D C   1 
ATOM   4941 O  O   . LEU D  1 110 ? 52.326 1.228   70.901  1.00 34.70 ? 111 LEU D O   1 
ATOM   4942 C  CB  . LEU D  1 110 ? 51.153 -0.283  68.264  1.00 36.97 ? 111 LEU D CB  1 
ATOM   4943 C  CG  . LEU D  1 110 ? 50.723 -0.074  66.813  1.00 40.14 ? 111 LEU D CG  1 
ATOM   4944 C  CD1 . LEU D  1 110 ? 49.476 -0.885  66.545  1.00 39.64 ? 111 LEU D CD1 1 
ATOM   4945 C  CD2 . LEU D  1 110 ? 50.485 1.398   66.519  1.00 39.53 ? 111 LEU D CD2 1 
ATOM   4946 N  N   . LEU D  1 111 ? 52.994 -0.914  70.764  1.00 39.14 ? 112 LEU D N   1 
ATOM   4947 C  CA  . LEU D  1 111 ? 53.158 -1.029  72.211  1.00 39.49 ? 112 LEU D CA  1 
ATOM   4948 C  C   . LEU D  1 111 ? 54.268 -0.108  72.715  1.00 36.56 ? 112 LEU D C   1 
ATOM   4949 O  O   . LEU D  1 111 ? 54.159 0.463   73.805  1.00 37.83 ? 112 LEU D O   1 
ATOM   4950 C  CB  . LEU D  1 111 ? 53.445 -2.485  72.593  1.00 34.32 ? 112 LEU D CB  1 
ATOM   4951 C  CG  . LEU D  1 111 ? 52.273 -3.456  72.406  1.00 37.64 ? 112 LEU D CG  1 
ATOM   4952 C  CD1 . LEU D  1 111 ? 52.748 -4.911  72.470  1.00 35.46 ? 112 LEU D CD1 1 
ATOM   4953 C  CD2 . LEU D  1 111 ? 51.207 -3.185  73.445  1.00 36.54 ? 112 LEU D CD2 1 
ATOM   4954 N  N   . GLU D  1 112 ? 55.343 0.049   71.930  1.00 35.86 ? 113 GLU D N   1 
ATOM   4955 C  CA  . GLU D  1 112 ? 56.401 0.988   72.295  1.00 39.88 ? 113 GLU D CA  1 
ATOM   4956 C  C   . GLU D  1 112 ? 55.895 2.432   72.277  1.00 41.06 ? 113 GLU D C   1 
ATOM   4957 O  O   . GLU D  1 112 ? 56.224 3.227   73.167  1.00 39.79 ? 113 GLU D O   1 
ATOM   4958 C  CB  . GLU D  1 112 ? 57.594 0.820   71.351  1.00 42.06 ? 113 GLU D CB  1 
ATOM   4959 C  CG  . GLU D  1 112 ? 58.727 -0.039  71.922  1.00 54.23 ? 113 GLU D CG  1 
ATOM   4960 C  CD  . GLU D  1 112 ? 59.414 -0.933  70.880  1.00 63.58 ? 113 GLU D CD  1 
ATOM   4961 O  OE1 . GLU D  1 112 ? 59.683 -0.452  69.748  1.00 58.50 ? 113 GLU D OE1 1 
ATOM   4962 O  OE2 . GLU D  1 112 ? 59.703 -2.114  71.205  1.00 64.30 ? 113 GLU D OE2 1 
ATOM   4963 N  N   . LEU D  1 113 ? 55.084 2.782   71.275  1.00 38.40 ? 114 LEU D N   1 
ATOM   4964 C  CA  . LEU D  1 113 ? 54.467 4.103   71.235  1.00 38.73 ? 114 LEU D CA  1 
ATOM   4965 C  C   . LEU D  1 113 ? 53.542 4.319   72.429  1.00 40.90 ? 114 LEU D C   1 
ATOM   4966 O  O   . LEU D  1 113 ? 53.492 5.422   72.995  1.00 35.48 ? 114 LEU D O   1 
ATOM   4967 C  CB  . LEU D  1 113 ? 53.708 4.274   69.921  1.00 38.30 ? 114 LEU D CB  1 
ATOM   4968 C  CG  . LEU D  1 113 ? 53.070 5.632   69.659  1.00 46.91 ? 114 LEU D CG  1 
ATOM   4969 C  CD1 . LEU D  1 113 ? 54.019 6.752   70.057  1.00 43.01 ? 114 LEU D CD1 1 
ATOM   4970 C  CD2 . LEU D  1 113 ? 52.681 5.732   68.207  1.00 43.58 ? 114 LEU D CD2 1 
ATOM   4971 N  N   . HIS D  1 114 ? 52.804 3.277   72.835  1.00 33.97 ? 115 HIS D N   1 
ATOM   4972 C  CA  . HIS D  1 114 ? 51.956 3.422   74.010  1.00 36.47 ? 115 HIS D CA  1 
ATOM   4973 C  C   . HIS D  1 114 ? 52.788 3.718   75.250  1.00 38.80 ? 115 HIS D C   1 
ATOM   4974 O  O   . HIS D  1 114 ? 52.449 4.612   76.034  1.00 39.39 ? 115 HIS D O   1 
ATOM   4975 C  CB  . HIS D  1 114 ? 51.117 2.171   74.227  1.00 36.40 ? 115 HIS D CB  1 
ATOM   4976 C  CG  . HIS D  1 114 ? 50.102 2.320   75.316  1.00 39.58 ? 115 HIS D CG  1 
ATOM   4977 N  ND1 . HIS D  1 114 ? 50.427 2.240   76.654  1.00 40.48 ? 115 HIS D ND1 1 
ATOM   4978 C  CD2 . HIS D  1 114 ? 48.771 2.566   75.266  1.00 37.48 ? 115 HIS D CD2 1 
ATOM   4979 C  CE1 . HIS D  1 114 ? 49.338 2.421   77.379  1.00 38.91 ? 115 HIS D CE1 1 
ATOM   4980 N  NE2 . HIS D  1 114 ? 48.320 2.617   76.561  1.00 37.84 ? 115 HIS D NE2 1 
ATOM   4981 N  N   . SER D  1 115 ? 53.890 2.987   75.432  1.00 37.22 ? 116 SER D N   1 
ATOM   4982 C  CA  . SER D  1 115 ? 54.743 3.196   76.599  1.00 43.08 ? 116 SER D CA  1 
ATOM   4983 C  C   . SER D  1 115 ? 55.354 4.602   76.599  1.00 40.25 ? 116 SER D C   1 
ATOM   4984 O  O   . SER D  1 115 ? 55.445 5.246   77.647  1.00 45.58 ? 116 SER D O   1 
ATOM   4985 C  CB  . SER D  1 115 ? 55.825 2.116   76.635  1.00 42.71 ? 116 SER D CB  1 
ATOM   4986 O  OG  . SER D  1 115 ? 56.901 2.490   77.462  1.00 48.53 ? 116 SER D OG  1 
ATOM   4987 N  N   . THR D  1 116 ? 55.752 5.098   75.428  1.00 42.07 ? 117 THR D N   1 
ATOM   4988 C  CA  . THR D  1 116 ? 56.229 6.472   75.298  1.00 43.12 ? 117 THR D CA  1 
ATOM   4989 C  C   . THR D  1 116 ? 55.162 7.466   75.747  1.00 42.67 ? 117 THR D C   1 
ATOM   4990 O  O   . THR D  1 116 ? 55.424 8.359   76.559  1.00 40.21 ? 117 THR D O   1 
ATOM   4991 C  CB  . THR D  1 116 ? 56.610 6.729   73.839  1.00 44.98 ? 117 THR D CB  1 
ATOM   4992 O  OG1 . THR D  1 116 ? 57.876 6.118   73.564  1.00 54.84 ? 117 THR D OG1 1 
ATOM   4993 C  CG2 . THR D  1 116 ? 56.694 8.227   73.542  1.00 48.41 ? 117 THR D CG2 1 
ATOM   4994 N  N   . ALA D  1 117 ? 53.946 7.322   75.216  1.00 40.09 ? 118 ALA D N   1 
ATOM   4995 C  CA  . ALA D  1 117 ? 52.843 8.191   75.602  1.00 39.62 ? 118 ALA D CA  1 
ATOM   4996 C  C   . ALA D  1 117 ? 52.583 8.146   77.108  1.00 41.51 ? 118 ALA D C   1 
ATOM   4997 O  O   . ALA D  1 117 ? 52.323 9.186   77.722  1.00 40.15 ? 118 ALA D O   1 
ATOM   4998 C  CB  . ALA D  1 117 ? 51.585 7.795   74.834  1.00 37.70 ? 118 ALA D CB  1 
ATOM   4999 N  N   . SER D  1 118 ? 52.629 6.951   77.716  1.00 38.35 ? 119 SER D N   1 
ATOM   5000 C  CA  . SER D  1 118 ? 52.429 6.841   79.164  1.00 43.07 ? 119 SER D CA  1 
ATOM   5001 C  C   . SER D  1 118 ? 53.516 7.574   79.938  1.00 43.62 ? 119 SER D C   1 
ATOM   5002 O  O   . SER D  1 118 ? 53.229 8.249   80.934  1.00 42.67 ? 119 SER D O   1 
ATOM   5003 C  CB  . SER D  1 118 ? 52.399 5.372   79.602  1.00 39.91 ? 119 SER D CB  1 
ATOM   5004 O  OG  . SER D  1 118 ? 51.311 4.682   79.020  1.00 50.89 ? 119 SER D OG  1 
ATOM   5005 N  N   . GLY D  1 119 ? 54.776 7.431   79.509  1.00 44.72 ? 120 GLY D N   1 
ATOM   5006 C  CA  . GLY D  1 119 ? 55.871 8.088   80.207  1.00 47.36 ? 120 GLY D CA  1 
ATOM   5007 C  C   . GLY D  1 119 ? 55.778 9.602   80.176  1.00 47.39 ? 120 GLY D C   1 
ATOM   5008 O  O   . GLY D  1 119 ? 56.198 10.273  81.120  1.00 47.76 ? 120 GLY D O   1 
ATOM   5009 N  N   . ASN D  1 120 ? 55.229 10.157  79.101  1.00 43.06 ? 121 ASN D N   1 
ATOM   5010 C  CA  . ASN D  1 120 ? 54.989 11.588  78.999  1.00 45.21 ? 121 ASN D CA  1 
ATOM   5011 C  C   . ASN D  1 120 ? 53.607 11.995  79.513  1.00 42.31 ? 121 ASN D C   1 
ATOM   5012 O  O   . ASN D  1 120 ? 53.224 13.157  79.361  1.00 44.81 ? 121 ASN D O   1 
ATOM   5013 C  CB  . ASN D  1 120 ? 55.178 12.033  77.545  1.00 44.06 ? 121 ASN D CB  1 
ATOM   5014 C  CG  . ASN D  1 120 ? 56.588 11.759  77.044  1.00 50.91 ? 121 ASN D CG  1 
ATOM   5015 O  OD1 . ASN D  1 120 ? 57.550 11.846  77.810  1.00 54.70 ? 121 ASN D OD1 1 
ATOM   5016 N  ND2 . ASN D  1 120 ? 56.717 11.413  75.767  1.00 45.10 ? 121 ASN D ND2 1 
ATOM   5017 N  N   . ASN D  1 121 ? 52.864 11.069  80.123  1.00 40.27 ? 122 ASN D N   1 
ATOM   5018 C  CA  . ASN D  1 121 ? 51.503 11.303  80.609  1.00 41.53 ? 122 ASN D CA  1 
ATOM   5019 C  C   . ASN D  1 121 ? 50.643 11.982  79.541  1.00 41.61 ? 122 ASN D C   1 
ATOM   5020 O  O   . ASN D  1 121 ? 50.176 13.111  79.702  1.00 41.42 ? 122 ASN D O   1 
ATOM   5021 C  CB  . ASN D  1 121 ? 51.503 12.127  81.903  1.00 46.21 ? 122 ASN D CB  1 
ATOM   5022 C  CG  . ASN D  1 121 ? 52.207 11.417  83.061  1.00 47.39 ? 122 ASN D CG  1 
ATOM   5023 O  OD1 . ASN D  1 121 ? 53.294 11.821  83.470  1.00 49.35 ? 122 ASN D OD1 1 
ATOM   5024 N  ND2 . ASN D  1 121 ? 51.595 10.355  83.582  1.00 43.86 ? 122 ASN D ND2 1 
ATOM   5025 N  N   . ASP D  1 122 ? 50.441 11.265  78.428  1.00 43.20 ? 123 ASP D N   1 
ATOM   5026 C  CA  . ASP D  1 122 ? 49.604 11.737  77.330  1.00 35.83 ? 123 ASP D CA  1 
ATOM   5027 C  C   . ASP D  1 122 ? 48.376 10.834  77.220  1.00 38.60 ? 123 ASP D C   1 
ATOM   5028 O  O   . ASP D  1 122 ? 48.321 9.947   76.355  1.00 39.35 ? 123 ASP D O   1 
ATOM   5029 C  CB  . ASP D  1 122 ? 50.404 11.780  76.019  1.00 37.34 ? 123 ASP D CB  1 
ATOM   5030 C  CG  . ASP D  1 122 ? 49.683 12.584  74.899  1.00 44.97 ? 123 ASP D CG  1 
ATOM   5031 O  OD1 . ASP D  1 122 ? 48.452 12.853  75.009  1.00 40.01 ? 123 ASP D OD1 1 
ATOM   5032 O  OD2 . ASP D  1 122 ? 50.361 12.966  73.913  1.00 42.27 ? 123 ASP D OD2 1 
ATOM   5033 N  N   . PRO D  1 123 ? 47.369 11.032  78.076  1.00 40.07 ? 124 PRO D N   1 
ATOM   5034 C  CA  . PRO D  1 123 ? 46.228 10.102  78.079  1.00 39.56 ? 124 PRO D CA  1 
ATOM   5035 C  C   . PRO D  1 123 ? 45.433 10.130  76.791  1.00 40.01 ? 124 PRO D C   1 
ATOM   5036 O  O   . PRO D  1 123 ? 44.806 9.118   76.446  1.00 39.98 ? 124 PRO D O   1 
ATOM   5037 C  CB  . PRO D  1 123 ? 45.385 10.579  79.270  1.00 39.70 ? 124 PRO D CB  1 
ATOM   5038 C  CG  . PRO D  1 123 ? 45.726 12.014  79.420  1.00 39.12 ? 124 PRO D CG  1 
ATOM   5039 C  CD  . PRO D  1 123 ? 47.167 12.168  78.994  1.00 36.97 ? 124 PRO D CD  1 
ATOM   5040 N  N   . HIS D  1 124 ? 45.434 11.258  76.068  1.00 38.14 ? 125 HIS D N   1 
ATOM   5041 C  CA  . HIS D  1 124 ? 44.708 11.307  74.805  1.00 34.08 ? 125 HIS D CA  1 
ATOM   5042 C  C   . HIS D  1 124 ? 45.345 10.387  73.770  1.00 36.62 ? 125 HIS D C   1 
ATOM   5043 O  O   . HIS D  1 124 ? 44.638 9.682   73.040  1.00 35.61 ? 125 HIS D O   1 
ATOM   5044 C  CB  . HIS D  1 124 ? 44.641 12.737  74.290  1.00 33.51 ? 125 HIS D CB  1 
ATOM   5045 C  CG  . HIS D  1 124 ? 43.685 12.913  73.151  1.00 37.33 ? 125 HIS D CG  1 
ATOM   5046 N  ND1 . HIS D  1 124 ? 44.051 12.717  71.834  1.00 36.65 ? 125 HIS D ND1 1 
ATOM   5047 C  CD2 . HIS D  1 124 ? 42.373 13.252  73.132  1.00 36.68 ? 125 HIS D CD2 1 
ATOM   5048 C  CE1 . HIS D  1 124 ? 43.009 12.940  71.052  1.00 34.38 ? 125 HIS D CE1 1 
ATOM   5049 N  NE2 . HIS D  1 124 ? 41.978 13.262  71.815  1.00 40.59 ? 125 HIS D NE2 1 
ATOM   5050 N  N   . LEU D  1 125 ? 46.679 10.347  73.719  1.00 35.22 ? 126 LEU D N   1 
ATOM   5051 C  CA  . LEU D  1 125 ? 47.355 9.443   72.790  1.00 35.36 ? 126 LEU D CA  1 
ATOM   5052 C  C   . LEU D  1 125 ? 47.235 7.975   73.222  1.00 34.74 ? 126 LEU D C   1 
ATOM   5053 O  O   . LEU D  1 125 ? 47.004 7.105   72.375  1.00 31.96 ? 126 LEU D O   1 
ATOM   5054 C  CB  . LEU D  1 125 ? 48.819 9.854   72.637  1.00 32.39 ? 126 LEU D CB  1 
ATOM   5055 C  CG  . LEU D  1 125 ? 49.731 8.931   71.822  1.00 37.16 ? 126 LEU D CG  1 
ATOM   5056 C  CD1 . LEU D  1 125 ? 49.149 8.671   70.448  1.00 33.92 ? 126 LEU D CD1 1 
ATOM   5057 C  CD2 . LEU D  1 125 ? 51.137 9.526   71.701  1.00 33.77 ? 126 LEU D CD2 1 
ATOM   5058 N  N   . THR D  1 126 ? 47.408 7.662   74.518  1.00 33.70 ? 127 THR D N   1 
ATOM   5059 C  CA  . THR D  1 126 ? 47.225 6.268   74.941  1.00 37.97 ? 127 THR D CA  1 
ATOM   5060 C  C   . THR D  1 126 ? 45.807 5.799   74.645  1.00 36.86 ? 127 THR D C   1 
ATOM   5061 O  O   . THR D  1 126 ? 45.591 4.648   74.250  1.00 38.46 ? 127 THR D O   1 
ATOM   5062 C  CB  . THR D  1 126 ? 47.527 6.061   76.438  1.00 41.44 ? 127 THR D CB  1 
ATOM   5063 O  OG1 . THR D  1 126 ? 46.629 6.837   77.246  1.00 41.55 ? 127 THR D OG1 1 
ATOM   5064 C  CG2 . THR D  1 126 ? 48.969 6.404   76.787  1.00 38.60 ? 127 THR D CG2 1 
ATOM   5065 N  N   . LYS D  1 127 ? 44.831 6.688   74.815  1.00 35.90 ? 128 LYS D N   1 
ATOM   5066 C  CA  . LYS D  1 127 ? 43.450 6.345   74.499  1.00 40.81 ? 128 LYS D CA  1 
ATOM   5067 C  C   . LYS D  1 127 ? 43.294 5.974   73.029  1.00 42.18 ? 128 LYS D C   1 
ATOM   5068 O  O   . LYS D  1 127 ? 42.736 4.918   72.698  1.00 35.59 ? 128 LYS D O   1 
ATOM   5069 C  CB  . LYS D  1 127 ? 42.542 7.518   74.831  1.00 45.11 ? 128 LYS D CB  1 
ATOM   5070 C  CG  . LYS D  1 127 ? 41.142 7.091   75.040  1.00 52.94 ? 128 LYS D CG  1 
ATOM   5071 C  CD  . LYS D  1 127 ? 40.237 7.661   74.020  1.00 53.92 ? 128 LYS D CD  1 
ATOM   5072 C  CE  . LYS D  1 127 ? 38.817 7.276   74.401  1.00 68.24 ? 128 LYS D CE  1 
ATOM   5073 N  NZ  . LYS D  1 127 ? 37.912 7.135   73.225  1.00 65.75 ? 128 LYS D NZ  1 
ATOM   5074 N  N   . LEU D  1 128 ? 43.771 6.852   72.134  1.00 36.55 ? 129 LEU D N   1 
ATOM   5075 C  CA  . LEU D  1 128 ? 43.728 6.587   70.698  1.00 35.64 ? 129 LEU D CA  1 
ATOM   5076 C  C   . LEU D  1 128 ? 44.364 5.241   70.361  1.00 39.47 ? 129 LEU D C   1 
ATOM   5077 O  O   . LEU D  1 128 ? 43.818 4.460   69.574  1.00 37.76 ? 129 LEU D O   1 
ATOM   5078 C  CB  . LEU D  1 128 ? 44.444 7.702   69.936  1.00 31.66 ? 129 LEU D CB  1 
ATOM   5079 C  CG  . LEU D  1 128 ? 44.756 7.293   68.486  1.00 39.68 ? 129 LEU D CG  1 
ATOM   5080 C  CD1 . LEU D  1 128 ? 43.552 7.605   67.600  1.00 33.50 ? 129 LEU D CD1 1 
ATOM   5081 C  CD2 . LEU D  1 128 ? 46.045 7.931   67.925  1.00 34.98 ? 129 LEU D CD2 1 
ATOM   5082 N  N   . LEU D  1 129 ? 45.536 4.962   70.939  1.00 35.26 ? 130 LEU D N   1 
ATOM   5083 C  CA  . LEU D  1 129 ? 46.211 3.702   70.652  1.00 40.50 ? 130 LEU D CA  1 
ATOM   5084 C  C   . LEU D  1 129 ? 45.398 2.518   71.161  1.00 43.14 ? 130 LEU D C   1 
ATOM   5085 O  O   . LEU D  1 129 ? 45.311 1.481   70.494  1.00 41.34 ? 130 LEU D O   1 
ATOM   5086 C  CB  . LEU D  1 129 ? 47.605 3.703   71.275  1.00 32.72 ? 130 LEU D CB  1 
ATOM   5087 C  CG  . LEU D  1 129 ? 48.583 4.664   70.606  1.00 38.00 ? 130 LEU D CG  1 
ATOM   5088 C  CD1 . LEU D  1 129 ? 49.862 4.767   71.451  1.00 41.50 ? 130 LEU D CD1 1 
ATOM   5089 C  CD2 . LEU D  1 129 ? 48.897 4.205   69.187  1.00 38.02 ? 130 LEU D CD2 1 
ATOM   5090 N  N   . GLU D  1 130 ? 44.776 2.664   72.335  1.00 41.85 ? 131 GLU D N   1 
ATOM   5091 C  CA  . GLU D  1 130 ? 43.963 1.583   72.871  1.00 46.06 ? 131 GLU D CA  1 
ATOM   5092 C  C   . GLU D  1 130 ? 42.695 1.367   72.053  1.00 50.52 ? 131 GLU D C   1 
ATOM   5093 O  O   . GLU D  1 130 ? 42.269 0.224   71.887  1.00 56.25 ? 131 GLU D O   1 
ATOM   5094 C  CB  . GLU D  1 130 ? 43.615 1.853   74.339  1.00 47.02 ? 131 GLU D CB  1 
ATOM   5095 C  CG  . GLU D  1 130 ? 44.746 1.521   75.303  1.00 43.25 ? 131 GLU D CG  1 
ATOM   5096 C  CD  . GLU D  1 130 ? 44.504 2.064   76.704  1.00 53.76 ? 131 GLU D CD  1 
ATOM   5097 O  OE1 . GLU D  1 130 ? 43.350 1.964   77.178  1.00 60.97 ? 131 GLU D OE1 1 
ATOM   5098 O  OE2 . GLU D  1 130 ? 45.464 2.584   77.332  1.00 48.25 ? 131 GLU D OE2 1 
ATOM   5099 N  N   . ASP D  1 131 ? 42.082 2.427   71.523  1.00 46.31 ? 132 ASP D N   1 
ATOM   5100 C  CA  . ASP D  1 131 ? 40.790 2.255   70.868  1.00 48.31 ? 132 ASP D CA  1 
ATOM   5101 C  C   . ASP D  1 131 ? 40.875 1.973   69.374  1.00 51.29 ? 132 ASP D C   1 
ATOM   5102 O  O   . ASP D  1 131 ? 40.010 1.267   68.846  1.00 57.63 ? 132 ASP D O   1 
ATOM   5103 C  CB  . ASP D  1 131 ? 39.903 3.481   71.072  1.00 52.43 ? 132 ASP D CB  1 
ATOM   5104 C  CG  . ASP D  1 131 ? 39.378 3.589   72.486  1.00 69.19 ? 132 ASP D CG  1 
ATOM   5105 O  OD1 . ASP D  1 131 ? 39.496 2.600   73.248  1.00 70.14 ? 132 ASP D OD1 1 
ATOM   5106 O  OD2 . ASP D  1 131 ? 38.795 4.646   72.819  1.00 73.97 ? 132 ASP D OD2 1 
ATOM   5107 N  N   . GLU D  1 132 ? 41.869 2.506   68.669  1.00 48.21 ? 133 GLU D N   1 
ATOM   5108 C  CA  . GLU D  1 132 ? 41.896 2.417   67.214  1.00 50.14 ? 133 GLU D CA  1 
ATOM   5109 C  C   . GLU D  1 132 ? 42.924 1.442   66.662  1.00 51.81 ? 133 GLU D C   1 
ATOM   5110 O  O   . GLU D  1 132 ? 42.887 1.154   65.457  1.00 50.59 ? 133 GLU D O   1 
ATOM   5111 C  CB  . GLU D  1 132 ? 42.169 3.797   66.593  1.00 51.30 ? 133 GLU D CB  1 
ATOM   5112 C  CG  . GLU D  1 132 ? 41.195 4.888   67.003  1.00 61.20 ? 133 GLU D CG  1 
ATOM   5113 C  CD  . GLU D  1 132 ? 39.941 4.906   66.145  1.00 68.80 ? 133 GLU D CD  1 
ATOM   5114 O  OE1 . GLU D  1 132 ? 39.988 5.483   65.032  1.00 68.66 ? 133 GLU D OE1 1 
ATOM   5115 O  OE2 . GLU D  1 132 ? 38.910 4.350   66.593  1.00 72.67 ? 133 GLU D OE2 1 
ATOM   5116 N  N   . TYR D  1 133 ? 43.844 0.940   67.489  1.00 44.30 ? 134 TYR D N   1 
ATOM   5117 C  CA  . TYR D  1 133 ? 44.962 0.187   66.936  1.00 45.37 ? 134 TYR D CA  1 
ATOM   5118 C  C   . TYR D  1 133 ? 45.237 -1.123  67.665  1.00 43.23 ? 134 TYR D C   1 
ATOM   5119 O  O   . TYR D  1 133 ? 45.355 -2.167  67.016  1.00 42.82 ? 134 TYR D O   1 
ATOM   5120 C  CB  . TYR D  1 133 ? 46.216 1.059   66.925  1.00 42.72 ? 134 TYR D CB  1 
ATOM   5121 C  CG  . TYR D  1 133 ? 46.099 2.210   65.964  1.00 41.02 ? 134 TYR D CG  1 
ATOM   5122 C  CD1 . TYR D  1 133 ? 46.358 2.037   64.615  1.00 39.74 ? 134 TYR D CD1 1 
ATOM   5123 C  CD2 . TYR D  1 133 ? 45.692 3.463   66.403  1.00 38.92 ? 134 TYR D CD2 1 
ATOM   5124 C  CE1 . TYR D  1 133 ? 46.229 3.080   63.725  1.00 40.77 ? 134 TYR D CE1 1 
ATOM   5125 C  CE2 . TYR D  1 133 ? 45.564 4.519   65.530  1.00 38.78 ? 134 TYR D CE2 1 
ATOM   5126 C  CZ  . TYR D  1 133 ? 45.836 4.327   64.190  1.00 43.10 ? 134 TYR D CZ  1 
ATOM   5127 O  OH  . TYR D  1 133 ? 45.713 5.380   63.310  1.00 35.67 ? 134 TYR D OH  1 
ATOM   5128 N  N   . LEU D  1 134 ? 45.337 -1.097  68.997  1.00 39.93 ? 135 LEU D N   1 
ATOM   5129 C  CA  . LEU D  1 134 ? 45.827 -2.287  69.691  1.00 43.64 ? 135 LEU D CA  1 
ATOM   5130 C  C   . LEU D  1 134 ? 44.844 -3.443  69.585  1.00 42.35 ? 135 LEU D C   1 
ATOM   5131 O  O   . LEU D  1 134 ? 45.260 -4.590  69.380  1.00 39.58 ? 135 LEU D O   1 
ATOM   5132 C  CB  . LEU D  1 134 ? 46.142 -1.977  71.149  1.00 41.74 ? 135 LEU D CB  1 
ATOM   5133 C  CG  . LEU D  1 134 ? 47.329 -1.027  71.316  1.00 44.06 ? 135 LEU D CG  1 
ATOM   5134 C  CD1 . LEU D  1 134 ? 47.339 -0.479  72.736  1.00 47.39 ? 135 LEU D CD1 1 
ATOM   5135 C  CD2 . LEU D  1 134 ? 48.662 -1.699  70.963  1.00 37.81 ? 135 LEU D CD2 1 
ATOM   5136 N  N   . GLU D  1 135 ? 43.540 -3.166  69.690  1.00 41.28 ? 136 GLU D N   1 
ATOM   5137 C  CA  . GLU D  1 135 ? 42.557 -4.247  69.602  1.00 44.74 ? 136 GLU D CA  1 
ATOM   5138 C  C   . GLU D  1 135 ? 42.515 -4.846  68.196  1.00 46.02 ? 136 GLU D C   1 
ATOM   5139 O  O   . GLU D  1 135 ? 42.514 -6.073  68.040  1.00 43.98 ? 136 GLU D O   1 
ATOM   5140 C  CB  . GLU D  1 135 ? 41.171 -3.753  70.042  1.00 44.60 ? 136 GLU D CB  1 
ATOM   5141 C  CG  . GLU D  1 135 ? 40.495 -2.752  69.104  1.00 59.33 ? 136 GLU D CG  1 
ATOM   5142 C  CD  . GLU D  1 135 ? 41.387 -1.540  68.771  1.00 64.32 ? 136 GLU D CD  1 
ATOM   5143 O  OE1 . GLU D  1 135 ? 41.593 -1.230  67.570  1.00 56.97 ? 136 GLU D OE1 1 
ATOM   5144 O  OE2 . GLU D  1 135 ? 41.928 -0.925  69.717  1.00 63.76 ? 136 GLU D OE2 1 
ATOM   5145 N  N   . GLU D  1 136 ? 42.513 -4.006  67.157  1.00 47.02 ? 137 GLU D N   1 
ATOM   5146 C  CA  . GLU D  1 136 ? 42.489 -4.528  65.795  1.00 48.16 ? 137 GLU D CA  1 
ATOM   5147 C  C   . GLU D  1 136 ? 43.758 -5.302  65.481  1.00 45.26 ? 137 GLU D C   1 
ATOM   5148 O  O   . GLU D  1 136 ? 43.713 -6.300  64.752  1.00 40.12 ? 137 GLU D O   1 
ATOM   5149 C  CB  . GLU D  1 136 ? 42.283 -3.392  64.790  1.00 51.60 ? 137 GLU D CB  1 
ATOM   5150 C  CG  . GLU D  1 136 ? 40.975 -2.622  65.010  1.00 64.57 ? 137 GLU D CG  1 
ATOM   5151 C  CD  . GLU D  1 136 ? 40.615 -1.687  63.864  1.00 72.67 ? 137 GLU D CD  1 
ATOM   5152 O  OE1 . GLU D  1 136 ? 40.976 -0.487  63.937  1.00 73.28 ? 137 GLU D OE1 1 
ATOM   5153 O  OE2 . GLU D  1 136 ? 39.956 -2.145  62.901  1.00 77.45 ? 137 GLU D OE2 1 
ATOM   5154 N  N   . GLN D  1 137 ? 44.882 -4.886  66.061  1.00 40.77 ? 138 GLN D N   1 
ATOM   5155 C  CA  . GLN D  1 137 ? 46.130 -5.603  65.853  1.00 39.32 ? 138 GLN D CA  1 
ATOM   5156 C  C   . GLN D  1 137 ? 46.080 -6.999  66.474  1.00 39.41 ? 138 GLN D C   1 
ATOM   5157 O  O   . GLN D  1 137 ? 46.548 -7.970  65.871  1.00 34.44 ? 138 GLN D O   1 
ATOM   5158 C  CB  . GLN D  1 137 ? 47.279 -4.775  66.425  1.00 39.33 ? 138 GLN D CB  1 
ATOM   5159 C  CG  . GLN D  1 137 ? 48.584 -4.952  65.688  1.00 43.74 ? 138 GLN D CG  1 
ATOM   5160 C  CD  . GLN D  1 137 ? 48.465 -4.669  64.197  1.00 41.73 ? 138 GLN D CD  1 
ATOM   5161 O  OE1 . GLN D  1 137 ? 47.717 -3.786  63.764  1.00 43.52 ? 138 GLN D OE1 1 
ATOM   5162 N  NE2 . GLN D  1 137 ? 49.197 -5.433  63.405  1.00 43.14 ? 138 GLN D NE2 1 
ATOM   5163 N  N   . VAL D  1 138 ? 45.503 -7.121  67.672  1.00 35.81 ? 139 VAL D N   1 
ATOM   5164 C  CA  . VAL D  1 138 ? 45.418 -8.422  68.325  1.00 39.25 ? 139 VAL D CA  1 
ATOM   5165 C  C   . VAL D  1 138 ? 44.428 -9.327  67.591  1.00 39.06 ? 139 VAL D C   1 
ATOM   5166 O  O   . VAL D  1 138 ? 44.675 -10.528 67.417  1.00 34.10 ? 139 VAL D O   1 
ATOM   5167 C  CB  . VAL D  1 138 ? 45.052 -8.234  69.812  1.00 38.07 ? 139 VAL D CB  1 
ATOM   5168 C  CG1 . VAL D  1 138 ? 44.514 -9.522  70.404  1.00 35.53 ? 139 VAL D CG1 1 
ATOM   5169 C  CG2 . VAL D  1 138 ? 46.272 -7.748  70.600  1.00 37.54 ? 139 VAL D CG2 1 
ATOM   5170 N  N   . ASP D  1 139 ? 43.302 -8.761  67.134  1.00 39.95 ? 140 ASP D N   1 
ATOM   5171 C  CA  . ASP D  1 139 ? 42.355 -9.511  66.307  1.00 40.29 ? 140 ASP D CA  1 
ATOM   5172 C  C   . ASP D  1 139 ? 42.991 -9.949  64.997  1.00 36.80 ? 140 ASP D C   1 
ATOM   5173 O  O   . ASP D  1 139 ? 42.785 -11.081 64.540  1.00 35.22 ? 140 ASP D O   1 
ATOM   5174 C  CB  . ASP D  1 139 ? 41.115 -8.657  66.018  1.00 41.20 ? 140 ASP D CB  1 
ATOM   5175 C  CG  . ASP D  1 139 ? 40.290 -8.371  67.270  1.00 53.10 ? 140 ASP D CG  1 
ATOM   5176 O  OD1 . ASP D  1 139 ? 40.502 -9.063  68.295  1.00 55.79 ? 140 ASP D OD1 1 
ATOM   5177 O  OD2 . ASP D  1 139 ? 39.443 -7.445  67.237  1.00 58.83 ? 140 ASP D OD2 1 
ATOM   5178 N  N   . SER D  1 140 ? 43.739 -9.049  64.363  1.00 34.20 ? 141 SER D N   1 
ATOM   5179 C  CA  . SER D  1 140 ? 44.381 -9.371  63.097  1.00 34.77 ? 141 SER D CA  1 
ATOM   5180 C  C   . SER D  1 140 ? 45.380 -10.516 63.261  1.00 34.05 ? 141 SER D C   1 
ATOM   5181 O  O   . SER D  1 140 ? 45.414 -11.442 62.443  1.00 35.22 ? 141 SER D O   1 
ATOM   5182 C  CB  . SER D  1 140 ? 45.053 -8.108  62.539  1.00 34.95 ? 141 SER D CB  1 
ATOM   5183 O  OG  . SER D  1 140 ? 45.738 -8.371  61.333  1.00 51.78 ? 141 SER D OG  1 
ATOM   5184 N  N   . ILE D  1 141 ? 46.186 -10.482 64.325  1.00 34.03 ? 142 ILE D N   1 
ATOM   5185 C  CA  . ILE D  1 141 ? 47.178 -11.535 64.549  1.00 34.55 ? 142 ILE D CA  1 
ATOM   5186 C  C   . ILE D  1 141 ? 46.487 -12.872 64.812  1.00 34.28 ? 142 ILE D C   1 
ATOM   5187 O  O   . ILE D  1 141 ? 46.916 -13.921 64.308  1.00 31.70 ? 142 ILE D O   1 
ATOM   5188 C  CB  . ILE D  1 141 ? 48.124 -11.137 65.704  1.00 30.92 ? 142 ILE D CB  1 
ATOM   5189 C  CG1 . ILE D  1 141 ? 49.161 -10.117 65.213  1.00 33.95 ? 142 ILE D CG1 1 
ATOM   5190 C  CG2 . ILE D  1 141 ? 48.842 -12.351 66.279  1.00 28.07 ? 142 ILE D CG2 1 
ATOM   5191 C  CD1 . ILE D  1 141 ? 49.773 -9.283  66.307  1.00 32.02 ? 142 ILE D CD1 1 
ATOM   5192 N  N   . LYS D  1 142 ? 45.402 -12.850 65.596  1.00 29.42 ? 143 LYS D N   1 
ATOM   5193 C  CA  . LYS D  1 142 ? 44.661 -14.069 65.903  1.00 33.23 ? 143 LYS D CA  1 
ATOM   5194 C  C   . LYS D  1 142 ? 44.020 -14.657 64.648  1.00 34.90 ? 143 LYS D C   1 
ATOM   5195 O  O   . LYS D  1 142 ? 44.030 -15.878 64.452  1.00 32.03 ? 143 LYS D O   1 
ATOM   5196 C  CB  . LYS D  1 142 ? 43.598 -13.777 66.970  1.00 31.43 ? 143 LYS D CB  1 
ATOM   5197 C  CG  . LYS D  1 142 ? 42.621 -14.938 67.257  1.00 31.49 ? 143 LYS D CG  1 
ATOM   5198 C  CD  . LYS D  1 142 ? 43.352 -16.156 67.806  1.00 33.51 ? 143 LYS D CD  1 
ATOM   5199 C  CE  . LYS D  1 142 ? 42.461 -17.033 68.710  1.00 36.68 ? 143 LYS D CE  1 
ATOM   5200 N  NZ  . LYS D  1 142 ? 41.317 -17.640 67.966  1.00 43.25 ? 143 LYS D NZ  1 
ATOM   5201 N  N   . LYS D  1 143 ? 43.467 -13.800 63.786  1.00 32.61 ? 144 LYS D N   1 
ATOM   5202 C  CA  . LYS D  1 143 ? 42.859 -14.272 62.546  1.00 36.87 ? 144 LYS D CA  1 
ATOM   5203 C  C   . LYS D  1 143 ? 43.887 -14.982 61.662  1.00 34.21 ? 144 LYS D C   1 
ATOM   5204 O  O   . LYS D  1 143 ? 43.642 -16.095 61.182  1.00 38.33 ? 144 LYS D O   1 
ATOM   5205 C  CB  . LYS D  1 143 ? 42.205 -13.094 61.808  1.00 38.38 ? 144 LYS D CB  1 
ATOM   5206 C  CG  . LYS D  1 143 ? 41.622 -13.419 60.429  1.00 42.94 ? 144 LYS D CG  1 
ATOM   5207 C  CD  . LYS D  1 143 ? 40.471 -14.423 60.532  1.00 50.79 ? 144 LYS D CD  1 
ATOM   5208 C  CE  . LYS D  1 143 ? 39.094 -13.753 60.408  1.00 58.39 ? 144 LYS D CE  1 
ATOM   5209 N  NZ  . LYS D  1 143 ? 38.030 -14.411 61.246  1.00 60.79 ? 144 LYS D NZ  1 
ATOM   5210 N  N   . ILE D  1 144 ? 45.054 -14.363 61.448  1.00 33.34 ? 145 ILE D N   1 
ATOM   5211 C  CA  . ILE D  1 144 ? 46.076 -14.976 60.595  1.00 32.55 ? 145 ILE D CA  1 
ATOM   5212 C  C   . ILE D  1 144 ? 46.554 -16.297 61.191  1.00 31.58 ? 145 ILE D C   1 
ATOM   5213 O  O   . ILE D  1 144 ? 46.774 -17.273 60.467  1.00 28.91 ? 145 ILE D O   1 
ATOM   5214 C  CB  . ILE D  1 144 ? 47.245 -13.999 60.364  1.00 32.80 ? 145 ILE D CB  1 
ATOM   5215 C  CG1 . ILE D  1 144 ? 46.820 -12.886 59.415  1.00 34.90 ? 145 ILE D CG1 1 
ATOM   5216 C  CG2 . ILE D  1 144 ? 48.462 -14.721 59.760  1.00 29.92 ? 145 ILE D CG2 1 
ATOM   5217 C  CD1 . ILE D  1 144 ? 47.584 -11.601 59.652  1.00 38.50 ? 145 ILE D CD1 1 
ATOM   5218 N  N   . GLY D  1 145 ? 46.709 -16.353 62.518  1.00 33.38 ? 146 GLY D N   1 
ATOM   5219 C  CA  . GLY D  1 145 ? 47.075 -17.607 63.165  1.00 32.35 ? 146 GLY D CA  1 
ATOM   5220 C  C   . GLY D  1 145 ? 46.058 -18.717 62.930  1.00 34.07 ? 146 GLY D C   1 
ATOM   5221 O  O   . GLY D  1 145 ? 46.424 -19.848 62.582  1.00 33.69 ? 146 GLY D O   1 
ATOM   5222 N  N   . ASP D  1 146 ? 44.768 -18.415 63.144  1.00 35.19 ? 147 ASP D N   1 
ATOM   5223 C  CA  . ASP D  1 146 ? 43.708 -19.361 62.785  1.00 34.70 ? 147 ASP D CA  1 
ATOM   5224 C  C   . ASP D  1 146 ? 43.856 -19.845 61.347  1.00 31.63 ? 147 ASP D C   1 
ATOM   5225 O  O   . ASP D  1 146 ? 43.701 -21.040 61.070  1.00 35.57 ? 147 ASP D O   1 
ATOM   5226 C  CB  . ASP D  1 146 ? 42.304 -18.747 62.968  1.00 34.63 ? 147 ASP D CB  1 
ATOM   5227 C  CG  . ASP D  1 146 ? 41.991 -18.311 64.415  1.00 46.92 ? 147 ASP D CG  1 
ATOM   5228 O  OD1 . ASP D  1 146 ? 42.624 -18.840 65.362  1.00 45.57 ? 147 ASP D OD1 1 
ATOM   5229 O  OD2 . ASP D  1 146 ? 41.075 -17.460 64.609  1.00 48.77 ? 147 ASP D OD2 1 
ATOM   5230 N  N   . MET D  1 147 ? 44.144 -18.929 60.412  1.00 34.61 ? 148 MET D N   1 
ATOM   5231 C  CA  . MET D  1 147 ? 44.191 -19.307 58.999  1.00 32.02 ? 148 MET D CA  1 
ATOM   5232 C  C   . MET D  1 147 ? 45.357 -20.239 58.727  1.00 34.90 ? 148 MET D C   1 
ATOM   5233 O  O   . MET D  1 147 ? 45.227 -21.204 57.964  1.00 32.68 ? 148 MET D O   1 
ATOM   5234 C  CB  . MET D  1 147 ? 44.292 -18.062 58.122  1.00 31.85 ? 148 MET D CB  1 
ATOM   5235 C  CG  . MET D  1 147 ? 43.031 -17.188 58.152  1.00 35.69 ? 148 MET D CG  1 
ATOM   5236 S  SD  . MET D  1 147 ? 43.204 -15.551 57.367  1.00 42.12 ? 148 MET D SD  1 
ATOM   5237 C  CE  . MET D  1 147 ? 43.695 -15.981 55.697  1.00 36.50 ? 148 MET D CE  1 
ATOM   5238 N  N   . ILE D  1 148 ? 46.505 -19.972 59.351  1.00 30.71 ? 149 ILE D N   1 
ATOM   5239 C  CA  . ILE D  1 148 ? 47.668 -20.818 59.119  1.00 31.85 ? 149 ILE D CA  1 
ATOM   5240 C  C   . ILE D  1 148 ? 47.386 -22.236 59.606  1.00 32.24 ? 149 ILE D C   1 
ATOM   5241 O  O   . ILE D  1 148 ? 47.761 -23.217 58.955  1.00 33.99 ? 149 ILE D O   1 
ATOM   5242 C  CB  . ILE D  1 148 ? 48.913 -20.203 59.788  1.00 31.78 ? 149 ILE D CB  1 
ATOM   5243 C  CG1 . ILE D  1 148 ? 49.380 -18.959 59.026  1.00 32.14 ? 149 ILE D CG1 1 
ATOM   5244 C  CG2 . ILE D  1 148 ? 50.037 -21.223 59.916  1.00 27.03 ? 149 ILE D CG2 1 
ATOM   5245 C  CD1 . ILE D  1 148 ? 50.290 -18.052 59.858  1.00 31.19 ? 149 ILE D CD1 1 
ATOM   5246 N  N   . THR D  1 149 ? 46.695 -22.364 60.739  1.00 31.74 ? 150 THR D N   1 
ATOM   5247 C  CA  . THR D  1 149 ? 46.360 -23.687 61.255  1.00 32.07 ? 150 THR D CA  1 
ATOM   5248 C  C   . THR D  1 149 ? 45.382 -24.403 60.330  1.00 33.81 ? 150 THR D C   1 
ATOM   5249 O  O   . THR D  1 149 ? 45.558 -25.592 60.036  1.00 34.28 ? 150 THR D O   1 
ATOM   5250 C  CB  . THR D  1 149 ? 45.776 -23.561 62.665  1.00 29.79 ? 150 THR D CB  1 
ATOM   5251 O  OG1 . THR D  1 149 ? 46.733 -22.921 63.502  1.00 33.81 ? 150 THR D OG1 1 
ATOM   5252 C  CG2 . THR D  1 149 ? 45.451 -24.933 63.251  1.00 31.03 ? 150 THR D CG2 1 
ATOM   5253 N  N   . LYS D  1 150 ? 44.342 -23.689 59.872  1.00 31.21 ? 151 LYS D N   1 
ATOM   5254 C  CA  . LYS D  1 150 ? 43.372 -24.271 58.948  1.00 32.89 ? 151 LYS D CA  1 
ATOM   5255 C  C   . LYS D  1 150 ? 44.034 -24.690 57.650  1.00 32.40 ? 151 LYS D C   1 
ATOM   5256 O  O   . LYS D  1 150 ? 43.741 -25.761 57.115  1.00 32.47 ? 151 LYS D O   1 
ATOM   5257 C  CB  . LYS D  1 150 ? 42.249 -23.280 58.653  1.00 31.93 ? 151 LYS D CB  1 
ATOM   5258 C  CG  . LYS D  1 150 ? 41.292 -23.013 59.809  1.00 33.65 ? 151 LYS D CG  1 
ATOM   5259 C  CD  . LYS D  1 150 ? 40.437 -21.792 59.502  1.00 39.82 ? 151 LYS D CD  1 
ATOM   5260 C  CE  . LYS D  1 150 ? 39.202 -21.723 60.374  1.00 49.34 ? 151 LYS D CE  1 
ATOM   5261 N  NZ  . LYS D  1 150 ? 38.301 -20.592 59.979  1.00 55.71 ? 151 LYS D NZ  1 
ATOM   5262 N  N   . LEU D  1 151 ? 44.926 -23.855 57.121  1.00 30.24 ? 152 LEU D N   1 
ATOM   5263 C  CA  . LEU D  1 151 ? 45.561 -24.190 55.858  1.00 31.11 ? 152 LEU D CA  1 
ATOM   5264 C  C   . LEU D  1 151 ? 46.558 -25.328 56.022  1.00 32.98 ? 152 LEU D C   1 
ATOM   5265 O  O   . LEU D  1 151 ? 46.698 -26.156 55.117  1.00 33.25 ? 152 LEU D O   1 
ATOM   5266 C  CB  . LEU D  1 151 ? 46.228 -22.950 55.264  1.00 31.84 ? 152 LEU D CB  1 
ATOM   5267 C  CG  . LEU D  1 151 ? 47.076 -23.166 54.014  1.00 35.99 ? 152 LEU D CG  1 
ATOM   5268 C  CD1 . LEU D  1 151 ? 46.216 -23.678 52.863  1.00 28.84 ? 152 LEU D CD1 1 
ATOM   5269 C  CD2 . LEU D  1 151 ? 47.776 -21.876 53.626  1.00 31.84 ? 152 LEU D CD2 1 
ATOM   5270 N  N   . LYS D  1 152 ? 47.232 -25.422 57.171  1.00 29.50 ? 153 LYS D N   1 
ATOM   5271 C  CA  . LYS D  1 152 ? 48.092 -26.589 57.393  1.00 36.97 ? 153 LYS D CA  1 
ATOM   5272 C  C   . LYS D  1 152 ? 47.281 -27.879 57.510  1.00 37.91 ? 153 LYS D C   1 
ATOM   5273 O  O   . LYS D  1 152 ? 47.729 -28.938 57.046  1.00 37.73 ? 153 LYS D O   1 
ATOM   5274 C  CB  . LYS D  1 152 ? 48.947 -26.400 58.643  1.00 35.62 ? 153 LYS D CB  1 
ATOM   5275 C  CG  . LYS D  1 152 ? 50.228 -25.631 58.417  1.00 34.66 ? 153 LYS D CG  1 
ATOM   5276 C  CD  . LYS D  1 152 ? 50.827 -25.157 59.745  1.00 39.44 ? 153 LYS D CD  1 
ATOM   5277 C  CE  . LYS D  1 152 ? 52.235 -24.591 59.562  1.00 36.05 ? 153 LYS D CE  1 
ATOM   5278 N  NZ  . LYS D  1 152 ? 52.756 -23.979 60.826  1.00 42.07 ? 153 LYS D NZ  1 
ATOM   5279 N  N   . ARG D  1 153 ? 46.091 -27.813 58.122  1.00 30.63 ? 154 ARG D N   1 
ATOM   5280 C  CA  . ARG D  1 153 ? 45.235 -28.992 58.187  1.00 32.56 ? 154 ARG D CA  1 
ATOM   5281 C  C   . ARG D  1 153 ? 44.703 -29.360 56.803  1.00 39.26 ? 154 ARG D C   1 
ATOM   5282 O  O   . ARG D  1 153 ? 44.749 -30.530 56.402  1.00 36.42 ? 154 ARG D O   1 
ATOM   5283 C  CB  . ARG D  1 153 ? 44.081 -28.750 59.160  1.00 34.65 ? 154 ARG D CB  1 
ATOM   5284 C  CG  . ARG D  1 153 ? 43.000 -29.824 59.125  1.00 35.04 ? 154 ARG D CG  1 
ATOM   5285 C  CD  . ARG D  1 153 ? 41.931 -29.565 60.172  1.00 39.88 ? 154 ARG D CD  1 
ATOM   5286 N  NE  . ARG D  1 153 ? 42.498 -29.567 61.516  1.00 37.64 ? 154 ARG D NE  1 
ATOM   5287 C  CZ  . ARG D  1 153 ? 42.533 -28.507 62.310  1.00 36.67 ? 154 ARG D CZ  1 
ATOM   5288 N  NH1 . ARG D  1 153 ? 41.996 -27.349 61.943  1.00 30.88 ? 154 ARG D NH1 1 
ATOM   5289 N  NH2 . ARG D  1 153 ? 43.121 -28.608 63.499  1.00 34.69 ? 154 ARG D NH2 1 
ATOM   5290 N  N   . ALA D  1 154 ? 44.212 -28.371 56.052  1.00 34.40 ? 155 ALA D N   1 
ATOM   5291 C  CA  . ALA D  1 154 ? 43.633 -28.653 54.745  1.00 37.37 ? 155 ALA D CA  1 
ATOM   5292 C  C   . ALA D  1 154 ? 44.698 -29.072 53.736  1.00 38.96 ? 155 ALA D C   1 
ATOM   5293 O  O   . ALA D  1 154 ? 44.497 -30.030 52.984  1.00 37.86 ? 155 ALA D O   1 
ATOM   5294 C  CB  . ALA D  1 154 ? 42.860 -27.438 54.227  1.00 30.20 ? 155 ALA D CB  1 
ATOM   5295 N  N   . GLY D  1 155 ? 45.834 -28.379 53.708  1.00 41.46 ? 156 GLY D N   1 
ATOM   5296 C  CA  . GLY D  1 155 ? 46.799 -28.551 52.645  1.00 38.48 ? 156 GLY D CA  1 
ATOM   5297 C  C   . GLY D  1 155 ? 48.141 -29.002 53.167  1.00 42.93 ? 156 GLY D C   1 
ATOM   5298 O  O   . GLY D  1 155 ? 48.320 -30.166 53.549  1.00 48.06 ? 156 GLY D O   1 
ATOM   5299 N  N   . PRO D  1 156 ? 49.125 -28.081 53.203  1.00 44.39 ? 157 PRO D N   1 
ATOM   5300 C  CA  . PRO D  1 156 ? 48.989 -26.683 52.753  1.00 39.94 ? 157 PRO D CA  1 
ATOM   5301 C  C   . PRO D  1 156 ? 49.119 -26.460 51.231  1.00 43.42 ? 157 PRO D C   1 
ATOM   5302 O  O   . PRO D  1 156 ? 48.999 -25.326 50.769  1.00 42.47 ? 157 PRO D O   1 
ATOM   5303 C  CB  . PRO D  1 156 ? 50.130 -25.977 53.482  1.00 41.67 ? 157 PRO D CB  1 
ATOM   5304 C  CG  . PRO D  1 156 ? 51.176 -27.057 53.669  1.00 40.43 ? 157 PRO D CG  1 
ATOM   5305 C  CD  . PRO D  1 156 ? 50.403 -28.322 53.908  1.00 38.43 ? 157 PRO D CD  1 
ATOM   5306 N  N   . THR D  1 157 ? 49.336 -27.520 50.461  1.00 42.99 ? 158 THR D N   1 
ATOM   5307 C  CA  . THR D  1 157 ? 49.452 -27.433 49.011  1.00 42.71 ? 158 THR D CA  1 
ATOM   5308 C  C   . THR D  1 157 ? 48.395 -28.307 48.320  1.00 43.45 ? 158 THR D C   1 
ATOM   5309 O  O   . THR D  1 157 ? 47.686 -29.097 48.952  1.00 41.13 ? 158 THR D O   1 
ATOM   5310 C  CB  . THR D  1 157 ? 50.863 -27.844 48.567  1.00 45.94 ? 158 THR D CB  1 
ATOM   5311 O  OG1 . THR D  1 157 ? 51.133 -29.179 49.021  1.00 48.87 ? 158 THR D OG1 1 
ATOM   5312 C  CG2 . THR D  1 157 ? 51.912 -26.888 49.147  1.00 46.57 ? 158 THR D CG2 1 
ATOM   5313 N  N   . GLY D  1 158 ? 48.274 -28.139 47.000  1.00 38.86 ? 159 GLY D N   1 
ATOM   5314 C  CA  . GLY D  1 158 ? 47.409 -29.014 46.212  1.00 34.21 ? 159 GLY D CA  1 
ATOM   5315 C  C   . GLY D  1 158 ? 45.927 -28.738 46.417  1.00 35.51 ? 159 GLY D C   1 
ATOM   5316 O  O   . GLY D  1 158 ? 45.487 -27.590 46.563  1.00 34.83 ? 159 GLY D O   1 
ATOM   5317 N  N   . LEU D  1 159 ? 45.146 -29.822 46.414  1.00 33.46 ? 160 LEU D N   1 
ATOM   5318 C  CA  . LEU D  1 159 ? 43.699 -29.723 46.571  1.00 37.87 ? 160 LEU D CA  1 
ATOM   5319 C  C   . LEU D  1 159 ? 43.315 -29.011 47.868  1.00 35.77 ? 160 LEU D C   1 
ATOM   5320 O  O   . LEU D  1 159 ? 42.360 -28.224 47.891  1.00 30.52 ? 160 LEU D O   1 
ATOM   5321 C  CB  . LEU D  1 159 ? 43.077 -31.123 46.514  1.00 36.30 ? 160 LEU D CB  1 
ATOM   5322 C  CG  . LEU D  1 159 ? 41.564 -31.255 46.745  1.00 37.51 ? 160 LEU D CG  1 
ATOM   5323 C  CD1 . LEU D  1 159 ? 40.749 -30.440 45.735  1.00 36.72 ? 160 LEU D CD1 1 
ATOM   5324 C  CD2 . LEU D  1 159 ? 41.164 -32.715 46.684  1.00 37.18 ? 160 LEU D CD2 1 
ATOM   5325 N  N   . GLY D  1 160 ? 44.044 -29.270 48.954  1.00 32.94 ? 161 GLY D N   1 
ATOM   5326 C  CA  . GLY D  1 160 ? 43.746 -28.591 50.203  1.00 34.89 ? 161 GLY D CA  1 
ATOM   5327 C  C   . GLY D  1 160 ? 43.888 -27.086 50.100  1.00 35.88 ? 161 GLY D C   1 
ATOM   5328 O  O   . GLY D  1 160 ? 43.057 -26.338 50.620  1.00 36.82 ? 161 GLY D O   1 
ATOM   5329 N  N   . GLU D  1 161 ? 44.936 -26.619 49.426  1.00 32.36 ? 162 GLU D N   1 
ATOM   5330 C  CA  . GLU D  1 161 ? 45.089 -25.179 49.248  1.00 34.69 ? 162 GLU D CA  1 
ATOM   5331 C  C   . GLU D  1 161 ? 43.990 -24.621 48.362  1.00 35.57 ? 162 GLU D C   1 
ATOM   5332 O  O   . GLU D  1 161 ? 43.499 -23.514 48.597  1.00 33.38 ? 162 GLU D O   1 
ATOM   5333 C  CB  . GLU D  1 161 ? 46.455 -24.848 48.646  1.00 36.28 ? 162 GLU D CB  1 
ATOM   5334 C  CG  . GLU D  1 161 ? 46.681 -23.346 48.461  1.00 39.38 ? 162 GLU D CG  1 
ATOM   5335 C  CD  . GLU D  1 161 ? 48.056 -23.023 47.897  1.00 46.62 ? 162 GLU D CD  1 
ATOM   5336 O  OE1 . GLU D  1 161 ? 48.410 -23.577 46.826  1.00 48.90 ? 162 GLU D OE1 1 
ATOM   5337 O  OE2 . GLU D  1 161 ? 48.780 -22.209 48.517  1.00 48.32 ? 162 GLU D OE2 1 
ATOM   5338 N  N   . TYR D  1 162 ? 43.609 -25.370 47.325  1.00 36.83 ? 163 TYR D N   1 
ATOM   5339 C  CA  . TYR D  1 162 ? 42.519 -24.944 46.456  1.00 34.48 ? 163 TYR D CA  1 
ATOM   5340 C  C   . TYR D  1 162 ? 41.226 -24.792 47.249  1.00 35.85 ? 163 TYR D C   1 
ATOM   5341 O  O   . TYR D  1 162 ? 40.512 -23.792 47.101  1.00 37.12 ? 163 TYR D O   1 
ATOM   5342 C  CB  . TYR D  1 162 ? 42.360 -25.948 45.308  1.00 34.04 ? 163 TYR D CB  1 
ATOM   5343 C  CG  . TYR D  1 162 ? 41.132 -25.748 44.461  1.00 38.78 ? 163 TYR D CG  1 
ATOM   5344 C  CD1 . TYR D  1 162 ? 41.127 -24.820 43.427  1.00 40.26 ? 163 TYR D CD1 1 
ATOM   5345 C  CD2 . TYR D  1 162 ? 39.971 -26.481 44.694  1.00 36.80 ? 163 TYR D CD2 1 
ATOM   5346 C  CE1 . TYR D  1 162 ? 40.006 -24.626 42.645  1.00 41.27 ? 163 TYR D CE1 1 
ATOM   5347 C  CE2 . TYR D  1 162 ? 38.842 -26.296 43.917  1.00 42.45 ? 163 TYR D CE2 1 
ATOM   5348 C  CZ  . TYR D  1 162 ? 38.864 -25.364 42.892  1.00 43.83 ? 163 TYR D CZ  1 
ATOM   5349 O  OH  . TYR D  1 162 ? 37.742 -25.165 42.116  1.00 44.16 ? 163 TYR D OH  1 
ATOM   5350 N  N   . MET D  1 163 ? 40.934 -25.753 48.134  1.00 37.78 ? 164 MET D N   1 
ATOM   5351 C  CA  . MET D  1 163 ? 39.690 -25.711 48.904  1.00 36.96 ? 164 MET D CA  1 
ATOM   5352 C  C   . MET D  1 163 ? 39.721 -24.605 49.949  1.00 36.01 ? 164 MET D C   1 
ATOM   5353 O  O   . MET D  1 163 ? 38.725 -23.897 50.146  1.00 36.33 ? 164 MET D O   1 
ATOM   5354 C  CB  . MET D  1 163 ? 39.438 -27.062 49.577  1.00 34.92 ? 164 MET D CB  1 
ATOM   5355 C  CG  . MET D  1 163 ? 39.316 -28.225 48.604  1.00 42.16 ? 164 MET D CG  1 
ATOM   5356 S  SD  . MET D  1 163 ? 37.846 -28.119 47.557  1.00 45.51 ? 164 MET D SD  1 
ATOM   5357 C  CE  . MET D  1 163 ? 36.608 -27.535 48.730  1.00 49.16 ? 164 MET D CE  1 
ATOM   5358 N  N   . PHE D  1 164 ? 40.853 -24.446 50.634  1.00 34.81 ? 165 PHE D N   1 
ATOM   5359 C  CA  . PHE D  1 164 ? 40.980 -23.360 51.600  1.00 33.04 ? 165 PHE D CA  1 
ATOM   5360 C  C   . PHE D  1 164 ? 40.787 -22.006 50.924  1.00 36.97 ? 165 PHE D C   1 
ATOM   5361 O  O   . PHE D  1 164 ? 40.189 -21.094 51.504  1.00 42.27 ? 165 PHE D O   1 
ATOM   5362 C  CB  . PHE D  1 164 ? 42.342 -23.443 52.300  1.00 34.44 ? 165 PHE D CB  1 
ATOM   5363 C  CG  . PHE D  1 164 ? 42.579 -22.331 53.272  1.00 39.04 ? 165 PHE D CG  1 
ATOM   5364 C  CD1 . PHE D  1 164 ? 42.047 -22.390 54.555  1.00 31.51 ? 165 PHE D CD1 1 
ATOM   5365 C  CD2 . PHE D  1 164 ? 43.300 -21.200 52.890  1.00 34.79 ? 165 PHE D CD2 1 
ATOM   5366 C  CE1 . PHE D  1 164 ? 42.239 -21.358 55.442  1.00 35.71 ? 165 PHE D CE1 1 
ATOM   5367 C  CE2 . PHE D  1 164 ? 43.502 -20.153 53.781  1.00 37.58 ? 165 PHE D CE2 1 
ATOM   5368 C  CZ  . PHE D  1 164 ? 42.972 -20.228 55.061  1.00 39.43 ? 165 PHE D CZ  1 
ATOM   5369 N  N   . ASP D  1 165 ? 41.265 -21.865 49.682  1.00 36.47 ? 166 ASP D N   1 
ATOM   5370 C  CA  . ASP D  1 165 ? 41.156 -20.590 48.982  1.00 37.71 ? 166 ASP D CA  1 
ATOM   5371 C  C   . ASP D  1 165 ? 39.706 -20.199 48.722  1.00 43.63 ? 166 ASP D C   1 
ATOM   5372 O  O   . ASP D  1 165 ? 39.397 -19.001 48.680  1.00 40.69 ? 166 ASP D O   1 
ATOM   5373 C  CB  . ASP D  1 165 ? 41.937 -20.641 47.665  1.00 39.97 ? 166 ASP D CB  1 
ATOM   5374 C  CG  . ASP D  1 165 ? 41.813 -19.352 46.857  1.00 40.05 ? 166 ASP D CG  1 
ATOM   5375 O  OD1 . ASP D  1 165 ? 42.498 -18.357 47.195  1.00 39.66 ? 166 ASP D OD1 1 
ATOM   5376 O  OD2 . ASP D  1 165 ? 41.031 -19.337 45.880  1.00 47.03 ? 166 ASP D OD2 1 
ATOM   5377 N  N   . LYS D  1 166 ? 38.806 -21.184 48.539  1.00 43.51 ? 167 LYS D N   1 
ATOM   5378 C  CA  . LYS D  1 166 ? 37.379 -20.884 48.395  1.00 43.53 ? 167 LYS D CA  1 
ATOM   5379 C  C   . LYS D  1 166 ? 36.775 -20.351 49.690  1.00 48.26 ? 167 LYS D C   1 
ATOM   5380 O  O   . LYS D  1 166 ? 35.814 -19.571 49.649  1.00 53.13 ? 167 LYS D O   1 
ATOM   5381 C  CB  . LYS D  1 166 ? 36.615 -22.127 47.942  1.00 50.48 ? 167 LYS D CB  1 
ATOM   5382 C  CG  . LYS D  1 166 ? 37.136 -22.738 46.664  1.00 47.52 ? 167 LYS D CG  1 
ATOM   5383 C  CD  . LYS D  1 166 ? 36.404 -24.034 46.340  1.00 54.36 ? 167 LYS D CD  1 
ATOM   5384 C  CE  . LYS D  1 166 ? 35.907 -24.034 44.898  1.00 55.63 ? 167 LYS D CE  1 
ATOM   5385 N  NZ  . LYS D  1 166 ? 36.613 -23.002 44.059  1.00 57.61 ? 167 LYS D NZ  1 
ATOM   5386 N  N   . GLU D  1 167 ? 37.318 -20.755 50.840  1.00 44.32 ? 168 GLU D N   1 
ATOM   5387 C  CA  . GLU D  1 167 ? 36.853 -20.219 52.116  1.00 47.55 ? 168 GLU D CA  1 
ATOM   5388 C  C   . GLU D  1 167 ? 36.979 -18.701 52.159  1.00 49.16 ? 168 GLU D C   1 
ATOM   5389 O  O   . GLU D  1 167 ? 36.064 -18.007 52.614  1.00 60.17 ? 168 GLU D O   1 
ATOM   5390 C  CB  . GLU D  1 167 ? 37.638 -20.860 53.270  1.00 54.44 ? 168 GLU D CB  1 
ATOM   5391 C  CG  . GLU D  1 167 ? 36.909 -20.886 54.620  1.00 61.31 ? 168 GLU D CG  1 
ATOM   5392 C  CD  . GLU D  1 167 ? 37.859 -21.091 55.821  1.00 62.20 ? 168 GLU D CD  1 
ATOM   5393 O  OE1 . GLU D  1 167 ? 38.597 -22.107 55.850  1.00 55.35 ? 168 GLU D OE1 1 
ATOM   5394 O  OE2 . GLU D  1 167 ? 37.869 -20.234 56.736  1.00 57.62 ? 168 GLU D OE2 1 
ATOM   5395 N  N   . LEU D  1 168 ? 38.110 -18.164 51.688  1.00 47.10 ? 169 LEU D N   1 
ATOM   5396 C  CA  . LEU D  1 168 ? 38.351 -16.724 51.749  1.00 46.12 ? 169 LEU D CA  1 
ATOM   5397 C  C   . LEU D  1 168 ? 37.761 -15.964 50.572  1.00 52.99 ? 169 LEU D C   1 
ATOM   5398 O  O   . LEU D  1 168 ? 37.834 -14.728 50.561  1.00 50.29 ? 169 LEU D O   1 
ATOM   5399 C  CB  . LEU D  1 168 ? 39.849 -16.414 51.802  1.00 37.55 ? 169 LEU D CB  1 
ATOM   5400 C  CG  . LEU D  1 168 ? 40.826 -17.369 52.469  1.00 45.32 ? 169 LEU D CG  1 
ATOM   5401 C  CD1 . LEU D  1 168 ? 42.267 -16.867 52.282  1.00 40.02 ? 169 LEU D CD1 1 
ATOM   5402 C  CD2 . LEU D  1 168 ? 40.496 -17.518 53.945  1.00 49.36 ? 169 LEU D CD2 1 
ATOM   5403 N  N   . ASN D  1 169 ? 37.236 -16.664 49.567  1.00 53.22 ? 170 ASN D N   1 
ATOM   5404 C  CA  . ASN D  1 169 ? 36.656 -16.010 48.402  1.00 53.22 ? 170 ASN D CA  1 
ATOM   5405 C  C   . ASN D  1 169 ? 35.394 -15.270 48.831  1.00 67.25 ? 170 ASN D C   1 
ATOM   5406 O  O   . ASN D  1 169 ? 34.416 -15.888 49.276  1.00 68.67 ? 170 ASN D O   1 
ATOM   5407 C  CB  . ASN D  1 169 ? 36.334 -17.026 47.302  1.00 57.90 ? 170 ASN D CB  1 
ATOM   5408 C  CG  . ASN D  1 169 ? 36.667 -16.510 45.903  1.00 64.22 ? 170 ASN D CG  1 
ATOM   5409 O  OD1 . ASN D  1 169 ? 37.320 -15.477 45.746  1.00 62.48 ? 170 ASN D OD1 1 
ATOM   5410 N  ND2 . ASN D  1 169 ? 36.199 -17.225 44.879  1.00 69.09 ? 170 ASN D ND2 1 
ATOM   5411 O  OXT . ASN D  1 169 ? 35.334 -14.040 48.750  1.00 73.61 ? 170 ASN D OXT 1 
ATOM   5412 N  N   . ALA E  1 1   ? 1.229  28.842  -8.866  1.00 61.12 ? 2   ALA E N   1 
ATOM   5413 C  CA  . ALA E  1 1   ? 0.619  29.608  -7.777  1.00 67.23 ? 2   ALA E CA  1 
ATOM   5414 C  C   . ALA E  1 1   ? 0.377  28.735  -6.527  1.00 66.05 ? 2   ALA E C   1 
ATOM   5415 O  O   . ALA E  1 1   ? 0.210  27.509  -6.635  1.00 65.53 ? 2   ALA E O   1 
ATOM   5416 C  CB  . ALA E  1 1   ? -0.692 30.245  -8.253  1.00 58.82 ? 2   ALA E CB  1 
ATOM   5417 N  N   . SER E  1 2   ? 0.353  29.372  -5.349  1.00 53.46 ? 3   SER E N   1 
ATOM   5418 C  CA  . SER E  1 2   ? 0.161  28.659  -4.086  1.00 50.12 ? 3   SER E CA  1 
ATOM   5419 C  C   . SER E  1 2   ? -1.322 28.424  -3.805  1.00 46.89 ? 3   SER E C   1 
ATOM   5420 O  O   . SER E  1 2   ? -2.139 29.343  -3.919  1.00 50.41 ? 3   SER E O   1 
ATOM   5421 C  CB  . SER E  1 2   ? 0.789  29.441  -2.931  1.00 48.27 ? 3   SER E CB  1 
ATOM   5422 O  OG  . SER E  1 2   ? 0.539  28.805  -1.678  1.00 46.48 ? 3   SER E OG  1 
ATOM   5423 N  N   . GLN E  1 3   ? -1.666 27.194  -3.410  1.00 42.50 ? 4   GLN E N   1 
ATOM   5424 C  CA  . GLN E  1 3   ? -3.054 26.860  -3.113  1.00 38.14 ? 4   GLN E CA  1 
ATOM   5425 C  C   . GLN E  1 3   ? -3.500 27.350  -1.734  1.00 37.05 ? 4   GLN E C   1 
ATOM   5426 O  O   . GLN E  1 3   ? -4.707 27.453  -1.494  1.00 38.85 ? 4   GLN E O   1 
ATOM   5427 C  CB  . GLN E  1 3   ? -3.267 25.340  -3.230  1.00 36.50 ? 4   GLN E CB  1 
ATOM   5428 C  CG  . GLN E  1 3   ? -2.612 24.534  -2.092  1.00 42.82 ? 4   GLN E CG  1 
ATOM   5429 C  CD  . GLN E  1 3   ? -2.729 23.014  -2.251  1.00 42.25 ? 4   GLN E CD  1 
ATOM   5430 O  OE1 . GLN E  1 3   ? -3.698 22.496  -2.815  1.00 41.60 ? 4   GLN E OE1 1 
ATOM   5431 N  NE2 . GLN E  1 3   ? -1.717 22.298  -1.764  1.00 38.15 ? 4   GLN E NE2 1 
ATOM   5432 N  N   . VAL E  1 4   ? -2.568 27.650  -0.824  1.00 29.93 ? 5   VAL E N   1 
ATOM   5433 C  CA  . VAL E  1 4   ? -2.931 28.113  0.513   1.00 34.85 ? 5   VAL E CA  1 
ATOM   5434 C  C   . VAL E  1 4   ? -2.770 29.617  0.696   1.00 34.86 ? 5   VAL E C   1 
ATOM   5435 O  O   . VAL E  1 4   ? -3.287 30.160  1.687   1.00 38.04 ? 5   VAL E O   1 
ATOM   5436 C  CB  . VAL E  1 4   ? -2.119 27.404  1.622   1.00 36.28 ? 5   VAL E CB  1 
ATOM   5437 C  CG1 . VAL E  1 4   ? -2.267 25.897  1.546   1.00 36.08 ? 5   VAL E CG1 1 
ATOM   5438 C  CG2 . VAL E  1 4   ? -0.652 27.806  1.568   1.00 35.95 ? 5   VAL E CG2 1 
ATOM   5439 N  N   . ARG E  1 5   ? -2.072 30.306  -0.204  1.00 33.32 ? 6   ARG E N   1 
ATOM   5440 C  CA  . ARG E  1 5   ? -1.695 31.692  0.051   1.00 35.26 ? 6   ARG E CA  1 
ATOM   5441 C  C   . ARG E  1 5   ? -2.910 32.616  0.007   1.00 34.15 ? 6   ARG E C   1 
ATOM   5442 O  O   . ARG E  1 5   ? -3.708 32.550  -0.928  1.00 35.09 ? 6   ARG E O   1 
ATOM   5443 C  CB  . ARG E  1 5   ? -0.655 32.145  -0.965  1.00 33.61 ? 6   ARG E CB  1 
ATOM   5444 C  CG  . ARG E  1 5   ? -0.065 33.501  -0.657  1.00 35.18 ? 6   ARG E CG  1 
ATOM   5445 C  CD  . ARG E  1 5   ? 1.168  33.716  -1.500  1.00 39.62 ? 6   ARG E CD  1 
ATOM   5446 N  NE  . ARG E  1 5   ? 1.718  35.043  -1.284  1.00 37.65 ? 6   ARG E NE  1 
ATOM   5447 C  CZ  . ARG E  1 5   ? 3.008  35.330  -1.330  1.00 41.06 ? 6   ARG E CZ  1 
ATOM   5448 N  NH1 . ARG E  1 5   ? 3.909  34.409  -1.626  1.00 39.32 ? 6   ARG E NH1 1 
ATOM   5449 N  NH2 . ARG E  1 5   ? 3.403  36.572  -1.068  1.00 41.27 ? 6   ARG E NH2 1 
ATOM   5450 N  N   . GLN E  1 6   ? -3.045 33.484  1.015   1.00 31.95 ? 7   GLN E N   1 
ATOM   5451 C  CA  . GLN E  1 6   ? -4.170 34.427  1.063   1.00 36.91 ? 7   GLN E CA  1 
ATOM   5452 C  C   . GLN E  1 6   ? -3.794 35.632  1.911   1.00 33.77 ? 7   GLN E C   1 
ATOM   5453 O  O   . GLN E  1 6   ? -3.459 35.476  3.094   1.00 32.09 ? 7   GLN E O   1 
ATOM   5454 C  CB  . GLN E  1 6   ? -5.438 33.749  1.629   1.00 33.60 ? 7   GLN E CB  1 
ATOM   5455 C  CG  . GLN E  1 6   ? -6.737 34.545  1.434   1.00 33.57 ? 7   GLN E CG  1 
ATOM   5456 C  CD  . GLN E  1 6   ? -7.974 33.775  1.919   1.00 40.88 ? 7   GLN E CD  1 
ATOM   5457 O  OE1 . GLN E  1 6   ? -7.869 32.879  2.750   1.00 38.92 ? 7   GLN E OE1 1 
ATOM   5458 N  NE2 . GLN E  1 6   ? -9.143 34.127  1.398   1.00 37.99 ? 7   GLN E NE2 1 
ATOM   5459 N  N   . ASN E  1 7   ? -3.885 36.833  1.326   1.00 36.02 ? 8   ASN E N   1 
ATOM   5460 C  CA  . ASN E  1 7   ? -3.639 38.085  2.054   1.00 32.53 ? 8   ASN E CA  1 
ATOM   5461 C  C   . ASN E  1 7   ? -2.205 38.154  2.596   1.00 36.81 ? 8   ASN E C   1 
ATOM   5462 O  O   . ASN E  1 7   ? -1.947 38.721  3.666   1.00 33.53 ? 8   ASN E O   1 
ATOM   5463 C  CB  . ASN E  1 7   ? -4.660 38.271  3.187   1.00 32.56 ? 8   ASN E CB  1 
ATOM   5464 C  CG  . ASN E  1 7   ? -4.685 39.696  3.723   1.00 33.80 ? 8   ASN E CG  1 
ATOM   5465 O  OD1 . ASN E  1 7   ? -4.619 40.649  2.952   1.00 31.69 ? 8   ASN E OD1 1 
ATOM   5466 N  ND2 . ASN E  1 7   ? -4.754 39.844  5.053   1.00 30.48 ? 8   ASN E ND2 1 
ATOM   5467 N  N   . TYR E  1 8   ? -1.254 37.568  1.870   1.00 34.55 ? 9   TYR E N   1 
ATOM   5468 C  CA  . TYR E  1 8   ? 0.151  37.524  2.281   1.00 33.73 ? 9   TYR E CA  1 
ATOM   5469 C  C   . TYR E  1 8   ? 0.960  38.287  1.230   1.00 34.14 ? 9   TYR E C   1 
ATOM   5470 O  O   . TYR E  1 8   ? 1.253  37.755  0.156   1.00 33.89 ? 9   TYR E O   1 
ATOM   5471 C  CB  . TYR E  1 8   ? 0.614  36.074  2.427   1.00 33.33 ? 9   TYR E CB  1 
ATOM   5472 C  CG  . TYR E  1 8   ? 1.918  35.879  3.153   1.00 35.24 ? 9   TYR E CG  1 
ATOM   5473 C  CD1 . TYR E  1 8   ? 2.142  36.466  4.403   1.00 33.75 ? 9   TYR E CD1 1 
ATOM   5474 C  CD2 . TYR E  1 8   ? 2.930  35.096  2.596   1.00 28.69 ? 9   TYR E CD2 1 
ATOM   5475 C  CE1 . TYR E  1 8   ? 3.359  36.279  5.077   1.00 35.33 ? 9   TYR E CE1 1 
ATOM   5476 C  CE2 . TYR E  1 8   ? 4.144  34.909  3.252   1.00 31.26 ? 9   TYR E CE2 1 
ATOM   5477 C  CZ  . TYR E  1 8   ? 4.349  35.491  4.494   1.00 36.51 ? 9   TYR E CZ  1 
ATOM   5478 O  OH  . TYR E  1 8   ? 5.544  35.298  5.147   1.00 37.08 ? 9   TYR E OH  1 
ATOM   5479 N  N   . HIS E  1 9   ? 1.298  39.533  1.543   1.00 34.95 ? 10  HIS E N   1 
ATOM   5480 C  CA  . HIS E  1 9   ? 2.004  40.422  0.628   1.00 39.54 ? 10  HIS E CA  1 
ATOM   5481 C  C   . HIS E  1 9   ? 3.466  39.994  0.446   1.00 38.03 ? 10  HIS E C   1 
ATOM   5482 O  O   . HIS E  1 9   ? 4.099  39.464  1.358   1.00 37.52 ? 10  HIS E O   1 
ATOM   5483 C  CB  . HIS E  1 9   ? 1.932  41.848  1.176   1.00 41.20 ? 10  HIS E CB  1 
ATOM   5484 C  CG  . HIS E  1 9   ? 2.230  42.920  0.172   1.00 53.02 ? 10  HIS E CG  1 
ATOM   5485 N  ND1 . HIS E  1 9   ? 3.512  43.357  -0.098  1.00 50.12 ? 10  HIS E ND1 1 
ATOM   5486 C  CD2 . HIS E  1 9   ? 1.406  43.678  -0.593  1.00 54.13 ? 10  HIS E CD2 1 
ATOM   5487 C  CE1 . HIS E  1 9   ? 3.466  44.319  -1.003  1.00 52.50 ? 10  HIS E CE1 1 
ATOM   5488 N  NE2 . HIS E  1 9   ? 2.200  44.536  -1.318  1.00 55.06 ? 10  HIS E NE2 1 
ATOM   5489 N  N   . GLU E  1 10  ? 4.010  40.246  -0.749  1.00 38.50 ? 11  GLU E N   1 
ATOM   5490 C  CA  . GLU E  1 10  ? 5.409  39.895  -1.022  1.00 42.31 ? 11  GLU E CA  1 
ATOM   5491 C  C   . GLU E  1 10  ? 6.387  40.638  -0.107  1.00 41.79 ? 11  GLU E C   1 
ATOM   5492 O  O   . GLU E  1 10  ? 7.479  40.124  0.170   1.00 40.33 ? 11  GLU E O   1 
ATOM   5493 C  CB  . GLU E  1 10  ? 5.747  40.168  -2.494  1.00 45.51 ? 11  GLU E CB  1 
ATOM   5494 C  CG  . GLU E  1 10  ? 5.236  41.522  -3.000  1.00 56.65 ? 11  GLU E CG  1 
ATOM   5495 C  CD  . GLU E  1 10  ? 6.086  42.124  -4.114  1.00 68.63 ? 11  GLU E CD  1 
ATOM   5496 O  OE1 . GLU E  1 10  ? 6.141  41.531  -5.217  1.00 68.29 ? 11  GLU E OE1 1 
ATOM   5497 O  OE2 . GLU E  1 10  ? 6.692  43.199  -3.881  1.00 67.64 ? 11  GLU E OE2 1 
ATOM   5498 N  N   . ASP E  1 11  ? 6.027  41.844  0.354   1.00 36.68 ? 12  ASP E N   1 
ATOM   5499 C  CA  . ASP E  1 11  ? 6.870  42.577  1.300   1.00 43.45 ? 12  ASP E CA  1 
ATOM   5500 C  C   . ASP E  1 11  ? 7.051  41.805  2.596   1.00 40.86 ? 12  ASP E C   1 
ATOM   5501 O  O   . ASP E  1 11  ? 8.157  41.758  3.152   1.00 38.87 ? 12  ASP E O   1 
ATOM   5502 C  CB  . ASP E  1 11  ? 6.262  43.945  1.628   1.00 47.36 ? 12  ASP E CB  1 
ATOM   5503 C  CG  . ASP E  1 11  ? 6.281  44.891  0.458   1.00 52.94 ? 12  ASP E CG  1 
ATOM   5504 O  OD1 . ASP E  1 11  ? 7.040  44.622  -0.504  1.00 55.64 ? 12  ASP E OD1 1 
ATOM   5505 O  OD2 . ASP E  1 11  ? 5.534  45.899  0.512   1.00 57.09 ? 12  ASP E OD2 1 
ATOM   5506 N  N   . ALA E  1 12  ? 5.957  41.243  3.120   1.00 38.48 ? 13  ALA E N   1 
ATOM   5507 C  CA  . ALA E  1 12  ? 6.046  40.446  4.332   1.00 37.22 ? 13  ALA E CA  1 
ATOM   5508 C  C   . ALA E  1 12  ? 6.891  39.208  4.096   1.00 33.25 ? 13  ALA E C   1 
ATOM   5509 O  O   . ALA E  1 12  ? 7.758  38.878  4.908   1.00 32.98 ? 13  ALA E O   1 
ATOM   5510 C  CB  . ALA E  1 12  ? 4.650  40.063  4.815   1.00 32.41 ? 13  ALA E CB  1 
ATOM   5511 N  N   . GLU E  1 13  ? 6.681  38.530  2.969   1.00 36.05 ? 14  GLU E N   1 
ATOM   5512 C  CA  . GLU E  1 13  ? 7.437  37.308  2.711   1.00 36.49 ? 14  GLU E CA  1 
ATOM   5513 C  C   . GLU E  1 13  ? 8.934  37.602  2.645   1.00 37.34 ? 14  GLU E C   1 
ATOM   5514 O  O   . GLU E  1 13  ? 9.738  36.903  3.274   1.00 31.54 ? 14  GLU E O   1 
ATOM   5515 C  CB  . GLU E  1 13  ? 6.930  36.655  1.434   1.00 33.01 ? 14  GLU E CB  1 
ATOM   5516 C  CG  . GLU E  1 13  ? 7.717  35.458  0.949   1.00 36.49 ? 14  GLU E CG  1 
ATOM   5517 C  CD  . GLU E  1 13  ? 7.280  35.025  -0.447  1.00 44.45 ? 14  GLU E CD  1 
ATOM   5518 O  OE1 . GLU E  1 13  ? 6.506  35.782  -1.090  1.00 43.44 ? 14  GLU E OE1 1 
ATOM   5519 O  OE2 . GLU E  1 13  ? 7.705  33.938  -0.907  1.00 44.75 ? 14  GLU E OE2 1 
ATOM   5520 N  N   . ALA E  1 14  ? 9.320  38.684  1.949   1.00 34.81 ? 15  ALA E N   1 
ATOM   5521 C  CA  . ALA E  1 14  ? 10.737 39.033  1.853   1.00 34.35 ? 15  ALA E CA  1 
ATOM   5522 C  C   . ALA E  1 14  ? 11.298 39.441  3.204   1.00 37.86 ? 15  ALA E C   1 
ATOM   5523 O  O   . ALA E  1 14  ? 12.458 39.141  3.522   1.00 35.38 ? 15  ALA E O   1 
ATOM   5524 C  CB  . ALA E  1 14  ? 10.956 40.158  0.840   1.00 34.53 ? 15  ALA E CB  1 
ATOM   5525 N  N   . SER E  1 15  ? 10.496 40.112  4.023   1.00 34.86 ? 16  SER E N   1 
ATOM   5526 C  CA  . SER E  1 15  ? 11.057 40.596  5.273   1.00 37.97 ? 16  SER E CA  1 
ATOM   5527 C  C   . SER E  1 15  ? 11.100 39.497  6.339   1.00 36.69 ? 16  SER E C   1 
ATOM   5528 O  O   . SER E  1 15  ? 11.963 39.538  7.222   1.00 37.39 ? 16  SER E O   1 
ATOM   5529 C  CB  . SER E  1 15  ? 10.286 41.836  5.733   1.00 36.31 ? 16  SER E CB  1 
ATOM   5530 O  OG  . SER E  1 15  ? 10.291 41.929  7.135   1.00 51.57 ? 16  SER E OG  1 
ATOM   5531 N  N   . ILE E  1 16  ? 10.231 38.482  6.247   1.00 34.73 ? 17  ILE E N   1 
ATOM   5532 C  CA  . ILE E  1 16  ? 10.380 37.303  7.099   1.00 31.58 ? 17  ILE E CA  1 
ATOM   5533 C  C   . ILE E  1 16  ? 11.675 36.559  6.779   1.00 33.89 ? 17  ILE E C   1 
ATOM   5534 O  O   . ILE E  1 16  ? 12.374 36.093  7.686   1.00 33.16 ? 17  ILE E O   1 
ATOM   5535 C  CB  . ILE E  1 16  ? 9.148  36.383  6.977   1.00 31.97 ? 17  ILE E CB  1 
ATOM   5536 C  CG1 . ILE E  1 16  ? 7.882  37.095  7.460   1.00 32.52 ? 17  ILE E CG1 1 
ATOM   5537 C  CG2 . ILE E  1 16  ? 9.375  35.034  7.683   1.00 29.30 ? 17  ILE E CG2 1 
ATOM   5538 C  CD1 . ILE E  1 16  ? 7.677  36.994  8.935   1.00 41.57 ? 17  ILE E CD1 1 
ATOM   5539 N  N   . ASN E  1 17  ? 12.010 36.416  5.490   1.00 30.68 ? 18  ASN E N   1 
ATOM   5540 C  CA  . ASN E  1 17  ? 13.272 35.768  5.126   1.00 32.54 ? 18  ASN E CA  1 
ATOM   5541 C  C   . ASN E  1 17  ? 14.475 36.531  5.687   1.00 31.33 ? 18  ASN E C   1 
ATOM   5542 O  O   . ASN E  1 17  ? 15.442 35.921  6.162   1.00 32.50 ? 18  ASN E O   1 
ATOM   5543 C  CB  . ASN E  1 17  ? 13.382 35.635  3.604   1.00 32.81 ? 18  ASN E CB  1 
ATOM   5544 C  CG  . ASN E  1 17  ? 12.638 34.416  3.061   1.00 35.79 ? 18  ASN E CG  1 
ATOM   5545 O  OD1 . ASN E  1 17  ? 12.471 33.405  3.740   1.00 35.42 ? 18  ASN E OD1 1 
ATOM   5546 N  ND2 . ASN E  1 17  ? 12.189 34.516  1.826   1.00 34.73 ? 18  ASN E ND2 1 
ATOM   5547 N  N   . LYS E  1 18  ? 14.430 37.864  5.676   1.00 30.31 ? 19  LYS E N   1 
ATOM   5548 C  CA  . LYS E  1 18  ? 15.532 38.607  6.279   1.00 32.41 ? 19  LYS E CA  1 
ATOM   5549 C  C   . LYS E  1 18  ? 15.553 38.457  7.806   1.00 33.83 ? 19  LYS E C   1 
ATOM   5550 O  O   . LYS E  1 18  ? 16.631 38.429  8.411   1.00 34.23 ? 19  LYS E O   1 
ATOM   5551 C  CB  . LYS E  1 18  ? 15.454 40.078  5.862   1.00 38.06 ? 19  LYS E CB  1 
ATOM   5552 C  CG  . LYS E  1 18  ? 16.449 41.001  6.577   1.00 52.67 ? 19  LYS E CG  1 
ATOM   5553 C  CD  . LYS E  1 18  ? 17.929 40.579  6.334   1.00 58.71 ? 19  LYS E CD  1 
ATOM   5554 C  CE  . LYS E  1 18  ? 18.427 41.022  4.943   1.00 60.62 ? 19  LYS E CE  1 
ATOM   5555 N  NZ  . LYS E  1 18  ? 19.101 42.351  4.939   1.00 58.39 ? 19  LYS E NZ  1 
ATOM   5556 N  N   . GLN E  1 19  ? 14.387 38.333  8.443   1.00 30.39 ? 20  GLN E N   1 
ATOM   5557 C  CA  . GLN E  1 19  ? 14.350 38.132  9.888   1.00 33.08 ? 20  GLN E CA  1 
ATOM   5558 C  C   . GLN E  1 19  ? 14.844 36.749  10.289  1.00 31.87 ? 20  GLN E C   1 
ATOM   5559 O  O   . GLN E  1 19  ? 15.439 36.594  11.361  1.00 30.80 ? 20  GLN E O   1 
ATOM   5560 C  CB  . GLN E  1 19  ? 12.936 38.334  10.424  1.00 35.58 ? 20  GLN E CB  1 
ATOM   5561 C  CG  . GLN E  1 19  ? 12.908 38.579  11.921  1.00 36.28 ? 20  GLN E CG  1 
ATOM   5562 C  CD  . GLN E  1 19  ? 13.585 39.878  12.297  1.00 39.44 ? 20  GLN E CD  1 
ATOM   5563 O  OE1 . GLN E  1 19  ? 13.397 40.904  11.638  1.00 45.61 ? 20  GLN E OE1 1 
ATOM   5564 N  NE2 . GLN E  1 19  ? 14.397 39.838  13.343  1.00 40.26 ? 20  GLN E NE2 1 
ATOM   5565 N  N   . ILE E  1 20  ? 14.593 35.732  9.461   1.00 31.42 ? 21  ILE E N   1 
ATOM   5566 C  CA  . ILE E  1 20  ? 15.181 34.419  9.713   1.00 27.96 ? 21  ILE E CA  1 
ATOM   5567 C  C   . ILE E  1 20  ? 16.703 34.533  9.771   1.00 34.13 ? 21  ILE E C   1 
ATOM   5568 O  O   . ILE E  1 20  ? 17.345 34.005  10.687  1.00 29.69 ? 21  ILE E O   1 
ATOM   5569 C  CB  . ILE E  1 20  ? 14.729 33.411  8.643   1.00 29.03 ? 21  ILE E CB  1 
ATOM   5570 C  CG1 . ILE E  1 20  ? 13.254 33.035  8.847   1.00 29.36 ? 21  ILE E CG1 1 
ATOM   5571 C  CG2 . ILE E  1 20  ? 15.594 32.166  8.699   1.00 31.62 ? 21  ILE E CG2 1 
ATOM   5572 C  CD1 . ILE E  1 20  ? 12.573 32.548  7.583   1.00 29.74 ? 21  ILE E CD1 1 
ATOM   5573 N  N   . ASN E  1 21  ? 17.303 35.254  8.808   1.00 26.92 ? 22  ASN E N   1 
ATOM   5574 C  CA  . ASN E  1 21  ? 18.755 35.376  8.798   1.00 29.64 ? 22  ASN E CA  1 
ATOM   5575 C  C   . ASN E  1 21  ? 19.241 36.136  10.020  1.00 28.75 ? 22  ASN E C   1 
ATOM   5576 O  O   . ASN E  1 21  ? 20.277 35.801  10.595  1.00 29.20 ? 22  ASN E O   1 
ATOM   5577 C  CB  . ASN E  1 21  ? 19.254 36.062  7.514   1.00 28.53 ? 22  ASN E CB  1 
ATOM   5578 C  CG  . ASN E  1 21  ? 20.765 35.952  7.357   1.00 36.69 ? 22  ASN E CG  1 
ATOM   5579 O  OD1 . ASN E  1 21  ? 21.516 36.817  7.825   1.00 30.95 ? 22  ASN E OD1 1 
ATOM   5580 N  ND2 . ASN E  1 21  ? 21.223 34.855  6.740   1.00 32.93 ? 22  ASN E ND2 1 
ATOM   5581 N  N   . MET E  1 22  ? 18.493 37.137  10.459  1.00 30.72 ? 23  MET E N   1 
ATOM   5582 C  CA  . MET E  1 22  ? 18.968 37.932  11.585  1.00 34.12 ? 23  MET E CA  1 
ATOM   5583 C  C   . MET E  1 22  ? 18.973 37.113  12.874  1.00 34.19 ? 23  MET E C   1 
ATOM   5584 O  O   . MET E  1 22  ? 19.904 37.216  13.683  1.00 33.14 ? 23  MET E O   1 
ATOM   5585 C  CB  . MET E  1 22  ? 18.111 39.192  11.721  1.00 37.12 ? 23  MET E CB  1 
ATOM   5586 C  CG  . MET E  1 22  ? 18.644 40.194  12.727  1.00 39.53 ? 23  MET E CG  1 
ATOM   5587 S  SD  . MET E  1 22  ? 17.667 41.705  12.673  1.00 56.25 ? 23  MET E SD  1 
ATOM   5588 C  CE  . MET E  1 22  ? 18.922 42.889  13.158  1.00 43.11 ? 23  MET E CE  1 
ATOM   5589 N  N   . CYS E  1 23  ? 17.968 36.256  13.064  1.00 29.01 ? 24  CYS E N   1 
ATOM   5590 C  CA  . CYS E  1 23  ? 17.957 35.429  14.265  1.00 29.40 ? 24  CYS E CA  1 
ATOM   5591 C  C   . CYS E  1 23  ? 18.993 34.313  14.186  1.00 30.60 ? 24  CYS E C   1 
ATOM   5592 O  O   . CYS E  1 23  ? 19.557 33.930  15.217  1.00 30.90 ? 24  CYS E O   1 
ATOM   5593 C  CB  . CYS E  1 23  ? 16.549 34.871  14.505  1.00 36.46 ? 24  CYS E CB  1 
ATOM   5594 S  SG  . CYS E  1 23  ? 15.403 36.100  15.286  1.00 54.87 ? 24  CYS E SG  1 
ATOM   5595 N  N   . LEU E  1 24  ? 19.266 33.790  12.983  1.00 27.99 ? 25  LEU E N   1 
ATOM   5596 C  CA  . LEU E  1 24  ? 20.333 32.803  12.832  1.00 30.25 ? 25  LEU E CA  1 
ATOM   5597 C  C   . LEU E  1 24  ? 21.694 33.415  13.140  1.00 31.13 ? 25  LEU E C   1 
ATOM   5598 O  O   . LEU E  1 24  ? 22.520 32.791  13.819  1.00 31.21 ? 25  LEU E O   1 
ATOM   5599 C  CB  . LEU E  1 24  ? 20.325 32.220  11.423  1.00 27.08 ? 25  LEU E CB  1 
ATOM   5600 C  CG  . LEU E  1 24  ? 19.173 31.251  11.190  1.00 31.93 ? 25  LEU E CG  1 
ATOM   5601 C  CD1 . LEU E  1 24  ? 19.217 30.708  9.786   1.00 29.57 ? 25  LEU E CD1 1 
ATOM   5602 C  CD2 . LEU E  1 24  ? 19.267 30.141  12.186  1.00 28.15 ? 25  LEU E CD2 1 
ATOM   5603 N  N   . TYR E  1 25  ? 21.931 34.648  12.668  1.00 24.94 ? 26  TYR E N   1 
ATOM   5604 C  CA  . TYR E  1 25  ? 23.157 35.365  13.008  1.00 27.60 ? 26  TYR E CA  1 
ATOM   5605 C  C   . TYR E  1 25  ? 23.275 35.602  14.514  1.00 29.10 ? 26  TYR E C   1 
ATOM   5606 O  O   . TYR E  1 25  ? 24.333 35.361  15.109  1.00 27.71 ? 26  TYR E O   1 
ATOM   5607 C  CB  . TYR E  1 25  ? 23.224 36.696  12.251  1.00 30.58 ? 26  TYR E CB  1 
ATOM   5608 C  CG  . TYR E  1 25  ? 24.376 37.558  12.695  1.00 32.33 ? 26  TYR E CG  1 
ATOM   5609 C  CD1 . TYR E  1 25  ? 25.671 37.279  12.272  1.00 30.29 ? 26  TYR E CD1 1 
ATOM   5610 C  CD2 . TYR E  1 25  ? 24.177 38.641  13.543  1.00 32.43 ? 26  TYR E CD2 1 
ATOM   5611 C  CE1 . TYR E  1 25  ? 26.737 38.051  12.675  1.00 34.45 ? 26  TYR E CE1 1 
ATOM   5612 C  CE2 . TYR E  1 25  ? 25.245 39.429  13.957  1.00 33.95 ? 26  TYR E CE2 1 
ATOM   5613 C  CZ  . TYR E  1 25  ? 26.520 39.123  13.518  1.00 37.86 ? 26  TYR E CZ  1 
ATOM   5614 O  OH  . TYR E  1 25  ? 27.585 39.883  13.916  1.00 38.00 ? 26  TYR E OH  1 
ATOM   5615 N  N   . ALA E  1 26  ? 22.205 36.096  15.148  1.00 29.25 ? 27  ALA E N   1 
ATOM   5616 C  CA  . ALA E  1 26  ? 22.230 36.285  16.596  1.00 26.73 ? 27  ALA E CA  1 
ATOM   5617 C  C   . ALA E  1 26  ? 22.521 34.974  17.314  1.00 30.07 ? 27  ALA E C   1 
ATOM   5618 O  O   . ALA E  1 26  ? 23.334 34.933  18.243  1.00 30.03 ? 27  ALA E O   1 
ATOM   5619 C  CB  . ALA E  1 26  ? 20.904 36.872  17.088  1.00 30.22 ? 27  ALA E CB  1 
ATOM   5620 N  N   . SER E  1 27  ? 21.883 33.887  16.880  1.00 27.93 ? 28  SER E N   1 
ATOM   5621 C  CA  . SER E  1 27  ? 22.190 32.571  17.439  1.00 28.93 ? 28  SER E CA  1 
ATOM   5622 C  C   . SER E  1 27  ? 23.679 32.244  17.345  1.00 32.46 ? 28  SER E C   1 
ATOM   5623 O  O   . SER E  1 27  ? 24.252 31.627  18.255  1.00 31.06 ? 28  SER E O   1 
ATOM   5624 C  CB  . SER E  1 27  ? 21.385 31.508  16.704  1.00 29.47 ? 28  SER E CB  1 
ATOM   5625 O  OG  . SER E  1 27  ? 21.825 30.231  17.091  1.00 34.80 ? 28  SER E OG  1 
ATOM   5626 N  N   . TYR E  1 28  ? 24.311 32.620  16.229  1.00 29.73 ? 29  TYR E N   1 
ATOM   5627 C  CA  . TYR E  1 28  ? 25.726 32.350  16.013  1.00 27.42 ? 29  TYR E CA  1 
ATOM   5628 C  C   . TYR E  1 28  ? 26.599 33.228  16.904  1.00 25.93 ? 29  TYR E C   1 
ATOM   5629 O  O   . TYR E  1 28  ? 27.623 32.770  17.430  1.00 30.55 ? 29  TYR E O   1 
ATOM   5630 C  CB  . TYR E  1 28  ? 26.036 32.573  14.534  1.00 26.95 ? 29  TYR E CB  1 
ATOM   5631 C  CG  . TYR E  1 28  ? 27.195 31.817  13.959  1.00 27.00 ? 29  TYR E CG  1 
ATOM   5632 C  CD1 . TYR E  1 28  ? 27.650 30.629  14.517  1.00 26.46 ? 29  TYR E CD1 1 
ATOM   5633 C  CD2 . TYR E  1 28  ? 27.837 32.296  12.823  1.00 28.40 ? 29  TYR E CD2 1 
ATOM   5634 C  CE1 . TYR E  1 28  ? 28.729 29.935  13.927  1.00 29.65 ? 29  TYR E CE1 1 
ATOM   5635 C  CE2 . TYR E  1 28  ? 28.903 31.619  12.237  1.00 28.72 ? 29  TYR E CE2 1 
ATOM   5636 C  CZ  . TYR E  1 28  ? 29.341 30.450  12.783  1.00 25.71 ? 29  TYR E CZ  1 
ATOM   5637 O  OH  . TYR E  1 28  ? 30.414 29.826  12.180  1.00 25.87 ? 29  TYR E OH  1 
ATOM   5638 N  N   . VAL E  1 29  ? 26.214 34.490  17.089  1.00 26.09 ? 30  VAL E N   1 
ATOM   5639 C  CA  . VAL E  1 29  ? 26.954 35.367  17.999  1.00 28.88 ? 30  VAL E CA  1 
ATOM   5640 C  C   . VAL E  1 29  ? 26.942 34.792  19.418  1.00 31.44 ? 30  VAL E C   1 
ATOM   5641 O  O   . VAL E  1 29  ? 27.964 34.752  20.106  1.00 32.44 ? 30  VAL E O   1 
ATOM   5642 C  CB  . VAL E  1 29  ? 26.366 36.792  17.962  1.00 31.10 ? 30  VAL E CB  1 
ATOM   5643 C  CG1 . VAL E  1 29  ? 26.900 37.624  19.135  1.00 28.34 ? 30  VAL E CG1 1 
ATOM   5644 C  CG2 . VAL E  1 29  ? 26.678 37.476  16.627  1.00 33.34 ? 30  VAL E CG2 1 
ATOM   5645 N  N   . TYR E  1 30  ? 25.776 34.339  19.872  1.00 30.61 ? 31  TYR E N   1 
ATOM   5646 C  CA  . TYR E  1 30  ? 25.651 33.756  21.202  1.00 27.57 ? 31  TYR E CA  1 
ATOM   5647 C  C   . TYR E  1 30  ? 26.444 32.461  21.325  1.00 31.30 ? 31  TYR E C   1 
ATOM   5648 O  O   . TYR E  1 30  ? 27.044 32.188  22.369  1.00 32.02 ? 31  TYR E O   1 
ATOM   5649 C  CB  . TYR E  1 30  ? 24.177 33.506  21.502  1.00 28.41 ? 31  TYR E CB  1 
ATOM   5650 C  CG  . TYR E  1 30  ? 23.416 34.758  21.854  1.00 31.84 ? 31  TYR E CG  1 
ATOM   5651 C  CD1 . TYR E  1 30  ? 23.960 35.686  22.733  1.00 35.22 ? 31  TYR E CD1 1 
ATOM   5652 C  CD2 . TYR E  1 30  ? 22.173 35.023  21.305  1.00 31.62 ? 31  TYR E CD2 1 
ATOM   5653 C  CE1 . TYR E  1 30  ? 23.285 36.832  23.076  1.00 41.74 ? 31  TYR E CE1 1 
ATOM   5654 C  CE2 . TYR E  1 30  ? 21.478 36.186  21.636  1.00 39.05 ? 31  TYR E CE2 1 
ATOM   5655 C  CZ  . TYR E  1 30  ? 22.043 37.082  22.530  1.00 45.31 ? 31  TYR E CZ  1 
ATOM   5656 O  OH  . TYR E  1 30  ? 21.385 38.239  22.891  1.00 48.62 ? 31  TYR E OH  1 
ATOM   5657 N  N   . LEU E  1 31  ? 26.432 31.632  20.282  1.00 28.76 ? 32  LEU E N   1 
ATOM   5658 C  CA  . LEU E  1 31  ? 27.260 30.431  20.302  1.00 33.41 ? 32  LEU E CA  1 
ATOM   5659 C  C   . LEU E  1 31  ? 28.736 30.791  20.475  1.00 30.26 ? 32  LEU E C   1 
ATOM   5660 O  O   . LEU E  1 31  ? 29.458 30.158  21.260  1.00 26.36 ? 32  LEU E O   1 
ATOM   5661 C  CB  . LEU E  1 31  ? 27.031 29.628  19.022  1.00 27.88 ? 32  LEU E CB  1 
ATOM   5662 C  CG  . LEU E  1 31  ? 27.677 28.247  18.961  1.00 38.56 ? 32  LEU E CG  1 
ATOM   5663 C  CD1 . LEU E  1 31  ? 26.918 27.288  19.865  1.00 37.53 ? 32  LEU E CD1 1 
ATOM   5664 C  CD2 . LEU E  1 31  ? 27.744 27.737  17.507  1.00 35.19 ? 32  LEU E CD2 1 
ATOM   5665 N  N   . SER E  1 32  ? 29.186 31.838  19.787  1.00 28.10 ? 33  SER E N   1 
ATOM   5666 C  CA  . SER E  1 32  ? 30.573 32.260  19.910  1.00 29.59 ? 33  SER E CA  1 
ATOM   5667 C  C   . SER E  1 32  ? 30.893 32.686  21.340  1.00 33.28 ? 33  SER E C   1 
ATOM   5668 O  O   . SER E  1 32  ? 31.916 32.276  21.907  1.00 31.81 ? 33  SER E O   1 
ATOM   5669 C  CB  . SER E  1 32  ? 30.849 33.389  18.929  1.00 27.61 ? 33  SER E CB  1 
ATOM   5670 O  OG  . SER E  1 32  ? 32.116 33.932  19.159  1.00 32.25 ? 33  SER E OG  1 
ATOM   5671 N  N   . MET E  1 33  ? 30.009 33.486  21.957  1.00 32.55 ? 34  MET E N   1 
ATOM   5672 C  CA  . MET E  1 33  ? 30.228 33.892  23.351  1.00 37.65 ? 34  MET E CA  1 
ATOM   5673 C  C   . MET E  1 33  ? 30.180 32.696  24.294  1.00 33.11 ? 34  MET E C   1 
ATOM   5674 O  O   . MET E  1 33  ? 30.938 32.639  25.264  1.00 34.52 ? 34  MET E O   1 
ATOM   5675 C  CB  . MET E  1 33  ? 29.195 34.925  23.807  1.00 31.29 ? 34  MET E CB  1 
ATOM   5676 C  CG  . MET E  1 33  ? 29.029 36.149  22.930  1.00 33.82 ? 34  MET E CG  1 
ATOM   5677 S  SD  . MET E  1 33  ? 27.693 37.189  23.627  1.00 39.09 ? 34  MET E SD  1 
ATOM   5678 C  CE  . MET E  1 33  ? 28.017 38.759  22.814  1.00 37.82 ? 34  MET E CE  1 
ATOM   5679 N  N   . ALA E  1 34  ? 29.284 31.741  24.036  1.00 27.12 ? 35  ALA E N   1 
ATOM   5680 C  CA  . ALA E  1 34  ? 29.114 30.622  24.959  1.00 30.83 ? 35  ALA E CA  1 
ATOM   5681 C  C   . ALA E  1 34  ? 30.405 29.831  25.107  1.00 36.74 ? 35  ALA E C   1 
ATOM   5682 O  O   . ALA E  1 34  ? 30.767 29.422  26.217  1.00 36.47 ? 35  ALA E O   1 
ATOM   5683 C  CB  . ALA E  1 34  ? 27.983 29.702  24.487  1.00 26.31 ? 35  ALA E CB  1 
ATOM   5684 N  N   . TYR E  1 35  ? 31.117 29.612  23.999  1.00 33.19 ? 36  TYR E N   1 
ATOM   5685 C  CA  . TYR E  1 35  ? 32.343 28.834  24.057  1.00 33.06 ? 36  TYR E CA  1 
ATOM   5686 C  C   . TYR E  1 35  ? 33.556 29.680  24.404  1.00 31.07 ? 36  TYR E C   1 
ATOM   5687 O  O   . TYR E  1 35  ? 34.534 29.146  24.936  1.00 35.30 ? 36  TYR E O   1 
ATOM   5688 C  CB  . TYR E  1 35  ? 32.543 28.072  22.739  1.00 30.44 ? 36  TYR E CB  1 
ATOM   5689 C  CG  . TYR E  1 35  ? 31.651 26.842  22.695  1.00 32.22 ? 36  TYR E CG  1 
ATOM   5690 C  CD1 . TYR E  1 35  ? 32.063 25.644  23.255  1.00 37.39 ? 36  TYR E CD1 1 
ATOM   5691 C  CD2 . TYR E  1 35  ? 30.369 26.906  22.164  1.00 32.81 ? 36  TYR E CD2 1 
ATOM   5692 C  CE1 . TYR E  1 35  ? 31.241 24.519  23.257  1.00 36.53 ? 36  TYR E CE1 1 
ATOM   5693 C  CE2 . TYR E  1 35  ? 29.538 25.798  22.157  1.00 40.56 ? 36  TYR E CE2 1 
ATOM   5694 C  CZ  . TYR E  1 35  ? 29.981 24.604  22.707  1.00 42.87 ? 36  TYR E CZ  1 
ATOM   5695 O  OH  . TYR E  1 35  ? 29.165 23.503  22.700  1.00 45.00 ? 36  TYR E OH  1 
ATOM   5696 N  N   . TYR E  1 36  ? 33.510 30.989  24.162  1.00 31.54 ? 37  TYR E N   1 
ATOM   5697 C  CA  . TYR E  1 36  ? 34.585 31.845  24.651  1.00 32.25 ? 37  TYR E CA  1 
ATOM   5698 C  C   . TYR E  1 36  ? 34.654 31.812  26.179  1.00 34.77 ? 37  TYR E C   1 
ATOM   5699 O  O   . TYR E  1 36  ? 35.745 31.755  26.757  1.00 28.60 ? 37  TYR E O   1 
ATOM   5700 C  CB  . TYR E  1 36  ? 34.391 33.269  24.137  1.00 32.60 ? 37  TYR E CB  1 
ATOM   5701 C  CG  . TYR E  1 36  ? 35.278 34.292  24.787  1.00 34.53 ? 37  TYR E CG  1 
ATOM   5702 C  CD1 . TYR E  1 36  ? 36.579 34.507  24.331  1.00 37.44 ? 37  TYR E CD1 1 
ATOM   5703 C  CD2 . TYR E  1 36  ? 34.819 35.051  25.861  1.00 35.12 ? 37  TYR E CD2 1 
ATOM   5704 C  CE1 . TYR E  1 36  ? 37.400 35.447  24.924  1.00 39.93 ? 37  TYR E CE1 1 
ATOM   5705 C  CE2 . TYR E  1 36  ? 35.634 35.998  26.462  1.00 40.08 ? 37  TYR E CE2 1 
ATOM   5706 C  CZ  . TYR E  1 36  ? 36.922 36.192  25.990  1.00 43.52 ? 37  TYR E CZ  1 
ATOM   5707 O  OH  . TYR E  1 36  ? 37.731 37.132  26.583  1.00 46.45 ? 37  TYR E OH  1 
ATOM   5708 N  N   . PHE E  1 37  ? 33.502 31.804  26.851  1.00 31.16 ? 38  PHE E N   1 
ATOM   5709 C  CA  . PHE E  1 37  ? 33.509 31.801  28.313  1.00 35.26 ? 38  PHE E CA  1 
ATOM   5710 C  C   . PHE E  1 37  ? 33.803 30.432  28.916  1.00 33.08 ? 38  PHE E C   1 
ATOM   5711 O  O   . PHE E  1 37  ? 33.930 30.333  30.136  1.00 38.01 ? 38  PHE E O   1 
ATOM   5712 C  CB  . PHE E  1 37  ? 32.185 32.356  28.848  1.00 30.51 ? 38  PHE E CB  1 
ATOM   5713 C  CG  . PHE E  1 37  ? 32.062 33.837  28.653  1.00 32.72 ? 38  PHE E CG  1 
ATOM   5714 C  CD1 . PHE E  1 37  ? 32.838 34.710  29.404  1.00 29.85 ? 38  PHE E CD1 1 
ATOM   5715 C  CD2 . PHE E  1 37  ? 31.220 34.362  27.682  1.00 32.04 ? 38  PHE E CD2 1 
ATOM   5716 C  CE1 . PHE E  1 37  ? 32.760 36.083  29.213  1.00 34.71 ? 38  PHE E CE1 1 
ATOM   5717 C  CE2 . PHE E  1 37  ? 31.142 35.740  27.478  1.00 32.41 ? 38  PHE E CE2 1 
ATOM   5718 C  CZ  . PHE E  1 37  ? 31.913 36.604  28.246  1.00 33.77 ? 38  PHE E CZ  1 
ATOM   5719 N  N   . GLU E  1 38  ? 33.953 29.392  28.103  1.00 32.75 ? 39  GLU E N   1 
ATOM   5720 C  CA  . GLU E  1 38  ? 34.438 28.095  28.564  1.00 34.08 ? 39  GLU E CA  1 
ATOM   5721 C  C   . GLU E  1 38  ? 35.923 27.882  28.288  1.00 32.40 ? 39  GLU E C   1 
ATOM   5722 O  O   . GLU E  1 38  ? 36.442 26.807  28.583  1.00 32.14 ? 39  GLU E O   1 
ATOM   5723 C  CB  . GLU E  1 38  ? 33.632 26.979  27.906  1.00 36.25 ? 39  GLU E CB  1 
ATOM   5724 C  CG  . GLU E  1 38  ? 32.188 27.003  28.348  1.00 43.93 ? 39  GLU E CG  1 
ATOM   5725 C  CD  . GLU E  1 38  ? 31.342 25.899  27.740  1.00 57.67 ? 39  GLU E CD  1 
ATOM   5726 O  OE1 . GLU E  1 38  ? 31.902 24.883  27.309  1.00 64.01 ? 39  GLU E OE1 1 
ATOM   5727 O  OE2 . GLU E  1 38  ? 30.094 26.078  27.658  1.00 66.39 ? 39  GLU E OE2 1 
ATOM   5728 N  N   . ARG E  1 39  ? 36.612 28.862  27.708  1.00 35.05 ? 40  ARG E N   1 
ATOM   5729 C  CA  . ARG E  1 39  ? 38.056 28.754  27.559  1.00 32.70 ? 40  ARG E CA  1 
ATOM   5730 C  C   . ARG E  1 39  ? 38.691 28.616  28.938  1.00 35.51 ? 40  ARG E C   1 
ATOM   5731 O  O   . ARG E  1 39  ? 38.223 29.196  29.925  1.00 32.16 ? 40  ARG E O   1 
ATOM   5732 C  CB  . ARG E  1 39  ? 38.620 29.987  26.847  1.00 31.16 ? 40  ARG E CB  1 
ATOM   5733 C  CG  . ARG E  1 39  ? 38.272 30.086  25.363  1.00 33.41 ? 40  ARG E CG  1 
ATOM   5734 C  CD  . ARG E  1 39  ? 38.836 31.362  24.706  1.00 35.78 ? 40  ARG E CD  1 
ATOM   5735 N  NE  . ARG E  1 39  ? 40.261 31.517  24.982  1.00 48.17 ? 40  ARG E NE  1 
ATOM   5736 C  CZ  . ARG E  1 39  ? 41.230 30.897  24.311  1.00 57.81 ? 40  ARG E CZ  1 
ATOM   5737 N  NH1 . ARG E  1 39  ? 40.965 30.111  23.275  1.00 50.89 ? 40  ARG E NH1 1 
ATOM   5738 N  NH2 . ARG E  1 39  ? 42.498 31.064  24.691  1.00 57.16 ? 40  ARG E NH2 1 
ATOM   5739 N  N   . ASP E  1 40  ? 39.768 27.838  29.004  1.00 31.94 ? 41  ASP E N   1 
ATOM   5740 C  CA  . ASP E  1 40  ? 40.437 27.632  30.284  1.00 34.21 ? 41  ASP E CA  1 
ATOM   5741 C  C   . ASP E  1 40  ? 40.997 28.929  30.859  1.00 36.23 ? 41  ASP E C   1 
ATOM   5742 O  O   . ASP E  1 40  ? 41.143 29.035  32.080  1.00 40.04 ? 41  ASP E O   1 
ATOM   5743 C  CB  . ASP E  1 40  ? 41.560 26.610  30.140  1.00 37.75 ? 41  ASP E CB  1 
ATOM   5744 C  CG  . ASP E  1 40  ? 42.777 27.194  29.439  1.00 43.85 ? 41  ASP E CG  1 
ATOM   5745 O  OD1 . ASP E  1 40  ? 42.770 27.193  28.186  1.00 44.73 ? 41  ASP E OD1 1 
ATOM   5746 O  OD2 . ASP E  1 40  ? 43.712 27.685  30.131  1.00 43.08 ? 41  ASP E OD2 1 
ATOM   5747 N  N   . ASP E  1 41  ? 41.334 29.913  30.016  1.00 31.85 ? 42  ASP E N   1 
ATOM   5748 C  CA  . ASP E  1 41  ? 41.803 31.204  30.508  1.00 33.90 ? 42  ASP E CA  1 
ATOM   5749 C  C   . ASP E  1 41  ? 40.681 32.224  30.653  1.00 35.30 ? 42  ASP E C   1 
ATOM   5750 O  O   . ASP E  1 41  ? 40.961 33.417  30.833  1.00 36.41 ? 42  ASP E O   1 
ATOM   5751 C  CB  . ASP E  1 41  ? 42.902 31.776  29.607  1.00 35.06 ? 42  ASP E CB  1 
ATOM   5752 C  CG  . ASP E  1 41  ? 42.461 31.934  28.160  1.00 43.28 ? 42  ASP E CG  1 
ATOM   5753 O  OD1 . ASP E  1 41  ? 41.373 31.435  27.804  1.00 43.19 ? 42  ASP E OD1 1 
ATOM   5754 O  OD2 . ASP E  1 41  ? 43.202 32.574  27.376  1.00 49.33 ? 42  ASP E OD2 1 
ATOM   5755 N  N   . VAL E  1 42  ? 39.427 31.789  30.585  1.00 32.11 ? 43  VAL E N   1 
ATOM   5756 C  CA  . VAL E  1 42  ? 38.299 32.672  30.872  1.00 37.21 ? 43  VAL E CA  1 
ATOM   5757 C  C   . VAL E  1 42  ? 37.511 32.078  32.034  1.00 32.62 ? 43  VAL E C   1 
ATOM   5758 O  O   . VAL E  1 42  ? 37.409 32.688  33.100  1.00 34.41 ? 43  VAL E O   1 
ATOM   5759 C  CB  . VAL E  1 42  ? 37.421 32.872  29.622  1.00 36.20 ? 43  VAL E CB  1 
ATOM   5760 C  CG1 . VAL E  1 42  ? 36.261 33.810  29.920  1.00 32.79 ? 43  VAL E CG1 1 
ATOM   5761 C  CG2 . VAL E  1 42  ? 38.281 33.390  28.456  1.00 33.55 ? 43  VAL E CG2 1 
ATOM   5762 N  N   . ALA E  1 43  ? 36.948 30.884  31.825  1.00 35.40 ? 44  ALA E N   1 
ATOM   5763 C  CA  . ALA E  1 43  ? 36.372 30.042  32.877  1.00 35.61 ? 44  ALA E CA  1 
ATOM   5764 C  C   . ALA E  1 43  ? 35.256 30.756  33.647  1.00 34.32 ? 44  ALA E C   1 
ATOM   5765 O  O   . ALA E  1 43  ? 35.300 30.909  34.869  1.00 34.33 ? 44  ALA E O   1 
ATOM   5766 C  CB  . ALA E  1 43  ? 37.469 29.537  33.826  1.00 32.89 ? 44  ALA E CB  1 
ATOM   5767 N  N   . LEU E  1 44  ? 34.238 31.195  32.907  1.00 35.97 ? 45  LEU E N   1 
ATOM   5768 C  CA  . LEU E  1 44  ? 33.032 31.781  33.493  1.00 35.85 ? 45  LEU E CA  1 
ATOM   5769 C  C   . LEU E  1 44  ? 31.865 30.892  33.088  1.00 35.97 ? 45  LEU E C   1 
ATOM   5770 O  O   . LEU E  1 44  ? 31.121 31.213  32.150  1.00 38.37 ? 45  LEU E O   1 
ATOM   5771 C  CB  . LEU E  1 44  ? 32.815 33.223  33.046  1.00 32.67 ? 45  LEU E CB  1 
ATOM   5772 C  CG  . LEU E  1 44  ? 33.837 34.188  33.642  1.00 38.88 ? 45  LEU E CG  1 
ATOM   5773 C  CD1 . LEU E  1 44  ? 33.856 35.526  32.878  1.00 37.79 ? 45  LEU E CD1 1 
ATOM   5774 C  CD2 . LEU E  1 44  ? 33.553 34.396  35.121  1.00 34.30 ? 45  LEU E CD2 1 
ATOM   5775 N  N   . PRO E  1 45  ? 31.678 29.765  33.772  1.00 35.47 ? 46  PRO E N   1 
ATOM   5776 C  CA  . PRO E  1 45  ? 30.638 28.819  33.346  1.00 34.89 ? 46  PRO E CA  1 
ATOM   5777 C  C   . PRO E  1 45  ? 29.229 29.379  33.417  1.00 37.34 ? 46  PRO E C   1 
ATOM   5778 O  O   . PRO E  1 45  ? 28.373 28.953  32.633  1.00 41.10 ? 46  PRO E O   1 
ATOM   5779 C  CB  . PRO E  1 45  ? 30.836 27.632  34.304  1.00 38.52 ? 46  PRO E CB  1 
ATOM   5780 C  CG  . PRO E  1 45  ? 31.574 28.195  35.485  1.00 38.27 ? 46  PRO E CG  1 
ATOM   5781 C  CD  . PRO E  1 45  ? 32.450 29.273  34.928  1.00 41.79 ? 46  PRO E CD  1 
ATOM   5782 N  N   . GLY E  1 46  ? 28.947 30.311  34.330  1.00 37.12 ? 47  GLY E N   1 
ATOM   5783 C  CA  . GLY E  1 46  ? 27.610 30.890  34.373  1.00 38.96 ? 47  GLY E CA  1 
ATOM   5784 C  C   . GLY E  1 46  ? 27.284 31.676  33.115  1.00 35.35 ? 47  GLY E C   1 
ATOM   5785 O  O   . GLY E  1 46  ? 26.221 31.499  32.516  1.00 34.19 ? 47  GLY E O   1 
ATOM   5786 N  N   . PHE E  1 47  ? 28.207 32.548  32.694  1.00 31.12 ? 48  PHE E N   1 
ATOM   5787 C  CA  . PHE E  1 47  ? 28.061 33.264  31.425  1.00 37.06 ? 48  PHE E CA  1 
ATOM   5788 C  C   . PHE E  1 47  ? 27.953 32.304  30.245  1.00 34.50 ? 48  PHE E C   1 
ATOM   5789 O  O   . PHE E  1 47  ? 27.142 32.512  29.334  1.00 34.29 ? 48  PHE E O   1 
ATOM   5790 C  CB  . PHE E  1 47  ? 29.249 34.208  31.221  1.00 34.04 ? 48  PHE E CB  1 
ATOM   5791 C  CG  . PHE E  1 47  ? 29.153 35.468  32.015  1.00 36.28 ? 48  PHE E CG  1 
ATOM   5792 C  CD1 . PHE E  1 47  ? 28.429 36.557  31.526  1.00 37.30 ? 48  PHE E CD1 1 
ATOM   5793 C  CD2 . PHE E  1 47  ? 29.753 35.566  33.263  1.00 35.13 ? 48  PHE E CD2 1 
ATOM   5794 C  CE1 . PHE E  1 47  ? 28.325 37.730  32.271  1.00 37.68 ? 48  PHE E CE1 1 
ATOM   5795 C  CE2 . PHE E  1 47  ? 29.652 36.729  34.011  1.00 36.35 ? 48  PHE E CE2 1 
ATOM   5796 C  CZ  . PHE E  1 47  ? 28.941 37.816  33.516  1.00 37.96 ? 48  PHE E CZ  1 
ATOM   5797 N  N   . ALA E  1 48  ? 28.772 31.254  30.237  1.00 32.33 ? 49  ALA E N   1 
ATOM   5798 C  CA  . ALA E  1 48  ? 28.711 30.272  29.157  1.00 37.70 ? 49  ALA E CA  1 
ATOM   5799 C  C   . ALA E  1 48  ? 27.317 29.679  29.035  1.00 36.81 ? 49  ALA E C   1 
ATOM   5800 O  O   . ALA E  1 48  ? 26.735 29.647  27.943  1.00 33.13 ? 49  ALA E O   1 
ATOM   5801 C  CB  . ALA E  1 48  ? 29.731 29.162  29.394  1.00 32.86 ? 49  ALA E CB  1 
ATOM   5802 N  N   . LYS E  1 49  ? 26.775 29.191  30.153  1.00 35.74 ? 50  LYS E N   1 
ATOM   5803 C  CA  . LYS E  1 49  ? 25.436 28.613  30.158  1.00 40.39 ? 50  LYS E CA  1 
ATOM   5804 C  C   . LYS E  1 49  ? 24.393 29.638  29.718  1.00 35.38 ? 50  LYS E C   1 
ATOM   5805 O  O   . LYS E  1 49  ? 23.543 29.346  28.874  1.00 36.74 ? 50  LYS E O   1 
ATOM   5806 C  CB  . LYS E  1 49  ? 25.120 28.072  31.551  1.00 38.84 ? 50  LYS E CB  1 
ATOM   5807 C  CG  . LYS E  1 49  ? 24.061 27.016  31.574  1.00 46.37 ? 50  LYS E CG  1 
ATOM   5808 C  CD  . LYS E  1 49  ? 23.943 26.438  32.971  1.00 62.80 ? 50  LYS E CD  1 
ATOM   5809 C  CE  . LYS E  1 49  ? 22.492 26.298  33.372  1.00 67.30 ? 50  LYS E CE  1 
ATOM   5810 N  NZ  . LYS E  1 49  ? 21.932 27.629  33.734  1.00 66.57 ? 50  LYS E NZ  1 
ATOM   5811 N  N   . PHE E  1 50  ? 24.471 30.856  30.253  1.00 30.81 ? 51  PHE E N   1 
ATOM   5812 C  CA  . PHE E  1 50  ? 23.515 31.893  29.877  1.00 37.06 ? 51  PHE E CA  1 
ATOM   5813 C  C   . PHE E  1 50  ? 23.506 32.130  28.368  1.00 33.86 ? 51  PHE E C   1 
ATOM   5814 O  O   . PHE E  1 50  ? 22.441 32.151  27.742  1.00 35.65 ? 51  PHE E O   1 
ATOM   5815 C  CB  . PHE E  1 50  ? 23.818 33.200  30.611  1.00 32.28 ? 51  PHE E CB  1 
ATOM   5816 C  CG  . PHE E  1 50  ? 22.891 34.313  30.226  1.00 37.74 ? 51  PHE E CG  1 
ATOM   5817 C  CD1 . PHE E  1 50  ? 21.594 34.360  30.732  1.00 34.29 ? 51  PHE E CD1 1 
ATOM   5818 C  CD2 . PHE E  1 50  ? 23.293 35.289  29.324  1.00 34.89 ? 51  PHE E CD2 1 
ATOM   5819 C  CE1 . PHE E  1 50  ? 20.723 35.383  30.368  1.00 37.94 ? 51  PHE E CE1 1 
ATOM   5820 C  CE2 . PHE E  1 50  ? 22.431 36.316  28.949  1.00 37.74 ? 51  PHE E CE2 1 
ATOM   5821 C  CZ  . PHE E  1 50  ? 21.141 36.363  29.468  1.00 39.86 ? 51  PHE E CZ  1 
ATOM   5822 N  N   . PHE E  1 51  ? 24.685 32.320  27.765  1.00 30.57 ? 52  PHE E N   1 
ATOM   5823 C  CA  . PHE E  1 51  ? 24.737 32.582  26.327  1.00 36.40 ? 52  PHE E CA  1 
ATOM   5824 C  C   . PHE E  1 51  ? 24.398 31.345  25.500  1.00 34.18 ? 52  PHE E C   1 
ATOM   5825 O  O   . PHE E  1 51  ? 23.819 31.478  24.416  1.00 31.72 ? 52  PHE E O   1 
ATOM   5826 C  CB  . PHE E  1 51  ? 26.108 33.132  25.938  1.00 28.28 ? 52  PHE E CB  1 
ATOM   5827 C  CG  . PHE E  1 51  ? 26.349 34.522  26.443  1.00 30.39 ? 52  PHE E CG  1 
ATOM   5828 C  CD1 . PHE E  1 51  ? 25.481 35.545  26.122  1.00 28.89 ? 52  PHE E CD1 1 
ATOM   5829 C  CD2 . PHE E  1 51  ? 27.428 34.806  27.253  1.00 33.35 ? 52  PHE E CD2 1 
ATOM   5830 C  CE1 . PHE E  1 51  ? 25.696 36.832  26.585  1.00 29.61 ? 52  PHE E CE1 1 
ATOM   5831 C  CE2 . PHE E  1 51  ? 27.639 36.085  27.720  1.00 31.05 ? 52  PHE E CE2 1 
ATOM   5832 C  CZ  . PHE E  1 51  ? 26.770 37.098  27.379  1.00 28.90 ? 52  PHE E CZ  1 
ATOM   5833 N  N   . LYS E  1 52  ? 24.725 30.143  25.979  1.00 26.95 ? 53  LYS E N   1 
ATOM   5834 C  CA  . LYS E  1 52  ? 24.306 28.954  25.240  1.00 33.89 ? 53  LYS E CA  1 
ATOM   5835 C  C   . LYS E  1 52  ? 22.789 28.889  25.137  1.00 38.32 ? 53  LYS E C   1 
ATOM   5836 O  O   . LYS E  1 52  ? 22.242 28.587  24.068  1.00 36.59 ? 53  LYS E O   1 
ATOM   5837 C  CB  . LYS E  1 52  ? 24.844 27.682  25.892  1.00 36.61 ? 53  LYS E CB  1 
ATOM   5838 C  CG  . LYS E  1 52  ? 24.307 26.421  25.260  1.00 44.83 ? 53  LYS E CG  1 
ATOM   5839 C  CD  . LYS E  1 52  ? 25.129 26.042  24.023  1.00 52.99 ? 53  LYS E CD  1 
ATOM   5840 C  CE  . LYS E  1 52  ? 24.855 24.607  23.560  1.00 56.74 ? 53  LYS E CE  1 
ATOM   5841 N  NZ  . LYS E  1 52  ? 26.055 24.005  22.875  1.00 59.69 ? 53  LYS E NZ  1 
ATOM   5842 N  N   . GLU E  1 53  ? 22.090 29.205  26.231  1.00 36.22 ? 54  GLU E N   1 
ATOM   5843 C  CA  . GLU E  1 53  ? 20.634 29.204  26.192  1.00 40.07 ? 54  GLU E CA  1 
ATOM   5844 C  C   . GLU E  1 53  ? 20.111 30.295  25.265  1.00 34.43 ? 54  GLU E C   1 
ATOM   5845 O  O   . GLU E  1 53  ? 19.157 30.069  24.516  1.00 34.13 ? 54  GLU E O   1 
ATOM   5846 C  CB  . GLU E  1 53  ? 20.075 29.346  27.612  1.00 41.79 ? 54  GLU E CB  1 
ATOM   5847 C  CG  . GLU E  1 53  ? 20.281 28.047  28.408  1.00 51.13 ? 54  GLU E CG  1 
ATOM   5848 C  CD  . GLU E  1 53  ? 20.032 28.151  29.921  1.00 66.76 ? 54  GLU E CD  1 
ATOM   5849 O  OE1 . GLU E  1 53  ? 20.139 29.260  30.504  1.00 57.88 ? 54  GLU E OE1 1 
ATOM   5850 O  OE2 . GLU E  1 53  ? 19.761 27.089  30.534  1.00 72.08 ? 54  GLU E OE2 1 
ATOM   5851 N  N   . SER E  1 54  ? 20.745 31.468  25.267  1.00 29.62 ? 55  SER E N   1 
ATOM   5852 C  CA  . SER E  1 54  ? 20.346 32.504  24.319  1.00 34.91 ? 55  SER E CA  1 
ATOM   5853 C  C   . SER E  1 54  ? 20.538 32.043  22.878  1.00 36.02 ? 55  SER E C   1 
ATOM   5854 O  O   . SER E  1 54  ? 19.737 32.384  21.996  1.00 34.94 ? 55  SER E O   1 
ATOM   5855 C  CB  . SER E  1 54  ? 21.128 33.790  24.572  1.00 30.92 ? 55  SER E CB  1 
ATOM   5856 O  OG  . SER E  1 54  ? 20.868 34.280  25.872  1.00 36.32 ? 55  SER E OG  1 
ATOM   5857 N  N   . SER E  1 55  ? 21.591 31.265  22.616  1.00 30.88 ? 56  SER E N   1 
ATOM   5858 C  CA  . SER E  1 55  ? 21.810 30.775  21.263  1.00 33.57 ? 56  SER E CA  1 
ATOM   5859 C  C   . SER E  1 55  ? 20.681 29.846  20.837  1.00 32.37 ? 56  SER E C   1 
ATOM   5860 O  O   . SER E  1 55  ? 20.104 30.009  19.758  1.00 34.77 ? 56  SER E O   1 
ATOM   5861 C  CB  . SER E  1 55  ? 23.166 30.068  21.168  1.00 30.60 ? 56  SER E CB  1 
ATOM   5862 O  OG  . SER E  1 55  ? 23.344 29.526  19.872  1.00 29.14 ? 56  SER E OG  1 
ATOM   5863 N  N   . ASP E  1 56  ? 20.345 28.874  21.686  1.00 31.49 ? 57  ASP E N   1 
ATOM   5864 C  CA  . ASP E  1 56  ? 19.252 27.952  21.397  1.00 37.10 ? 57  ASP E CA  1 
ATOM   5865 C  C   . ASP E  1 56  ? 17.947 28.694  21.149  1.00 37.86 ? 57  ASP E C   1 
ATOM   5866 O  O   . ASP E  1 56  ? 17.196 28.360  20.226  1.00 35.48 ? 57  ASP E O   1 
ATOM   5867 C  CB  . ASP E  1 56  ? 19.080 26.978  22.563  1.00 37.40 ? 57  ASP E CB  1 
ATOM   5868 C  CG  . ASP E  1 56  ? 20.213 25.973  22.656  1.00 47.54 ? 57  ASP E CG  1 
ATOM   5869 O  OD1 . ASP E  1 56  ? 21.003 25.860  21.682  1.00 46.83 ? 57  ASP E OD1 1 
ATOM   5870 O  OD2 . ASP E  1 56  ? 20.324 25.310  23.717  1.00 52.35 ? 57  ASP E OD2 1 
ATOM   5871 N  N   . CYS E  1 57  ? 17.671 29.711  21.964  1.00 34.21 ? 58  CYS E N   1 
ATOM   5872 C  CA  . CYS E  1 57  ? 16.420 30.455  21.853  1.00 39.56 ? 58  CYS E CA  1 
ATOM   5873 C  C   . CYS E  1 57  ? 16.317 31.189  20.510  1.00 38.39 ? 58  CYS E C   1 
ATOM   5874 O  O   . CYS E  1 57  ? 15.274 31.147  19.850  1.00 35.09 ? 58  CYS E O   1 
ATOM   5875 C  CB  . CYS E  1 57  ? 16.312 31.413  23.047  1.00 36.97 ? 58  CYS E CB  1 
ATOM   5876 S  SG  . CYS E  1 57  ? 15.326 32.855  22.781  1.00 59.82 ? 58  CYS E SG  1 
ATOM   5877 N  N   . CYS E  1 58  ? 17.398 31.853  20.075  1.00 37.11 ? 59  CYS E N   1 
ATOM   5878 C  CA  . CYS E  1 58  ? 17.381 32.501  18.762  1.00 36.83 ? 59  CYS E CA  1 
ATOM   5879 C  C   . CYS E  1 58  ? 17.236 31.491  17.623  1.00 36.39 ? 59  CYS E C   1 
ATOM   5880 O  O   . CYS E  1 58  ? 16.619 31.803  16.594  1.00 34.68 ? 59  CYS E O   1 
ATOM   5881 C  CB  . CYS E  1 58  ? 18.647 33.337  18.556  1.00 34.57 ? 59  CYS E CB  1 
ATOM   5882 S  SG  . CYS E  1 58  ? 18.597 34.916  19.417  1.00 45.77 ? 59  CYS E SG  1 
ATOM   5883 N  N   . ARG E  1 59  ? 17.792 30.284  17.771  1.00 34.17 ? 60  ARG E N   1 
ATOM   5884 C  CA  . ARG E  1 59  ? 17.589 29.295  16.722  1.00 38.30 ? 60  ARG E CA  1 
ATOM   5885 C  C   . ARG E  1 59  ? 16.121 28.876  16.641  1.00 37.27 ? 60  ARG E C   1 
ATOM   5886 O  O   . ARG E  1 59  ? 15.578 28.704  15.542  1.00 34.33 ? 60  ARG E O   1 
ATOM   5887 C  CB  . ARG E  1 59  ? 18.491 28.079  16.933  1.00 34.89 ? 60  ARG E CB  1 
ATOM   5888 C  CG  . ARG E  1 59  ? 18.481 27.161  15.715  1.00 42.37 ? 60  ARG E CG  1 
ATOM   5889 C  CD  . ARG E  1 59  ? 19.314 25.891  15.888  1.00 45.54 ? 60  ARG E CD  1 
ATOM   5890 N  NE  . ARG E  1 59  ? 19.037 25.225  17.155  1.00 47.41 ? 60  ARG E NE  1 
ATOM   5891 C  CZ  . ARG E  1 59  ? 19.828 25.283  18.219  1.00 46.43 ? 60  ARG E CZ  1 
ATOM   5892 N  NH1 . ARG E  1 59  ? 20.968 25.967  18.196  1.00 42.47 ? 60  ARG E NH1 1 
ATOM   5893 N  NH2 . ARG E  1 59  ? 19.462 24.650  19.335  1.00 47.20 ? 60  ARG E NH2 1 
ATOM   5894 N  N   . GLU E  1 60  ? 15.454 28.713  17.789  1.00 36.45 ? 61  GLU E N   1 
ATOM   5895 C  CA  . GLU E  1 60  ? 14.030 28.388  17.744  1.00 39.81 ? 61  GLU E CA  1 
ATOM   5896 C  C   . GLU E  1 60  ? 13.214 29.546  17.177  1.00 39.01 ? 61  GLU E C   1 
ATOM   5897 O  O   . GLU E  1 60  ? 12.216 29.312  16.487  1.00 36.43 ? 61  GLU E O   1 
ATOM   5898 C  CB  . GLU E  1 60  ? 13.517 27.999  19.130  1.00 38.86 ? 61  GLU E CB  1 
ATOM   5899 C  CG  . GLU E  1 60  ? 13.889 26.564  19.542  1.00 53.57 ? 61  GLU E CG  1 
ATOM   5900 C  CD  . GLU E  1 60  ? 14.464 26.461  20.964  1.00 70.11 ? 61  GLU E CD  1 
ATOM   5901 O  OE1 . GLU E  1 60  ? 15.447 25.696  21.166  1.00 69.54 ? 61  GLU E OE1 1 
ATOM   5902 O  OE2 . GLU E  1 60  ? 13.931 27.141  21.879  1.00 72.10 ? 61  GLU E OE2 1 
ATOM   5903 N  N   . HIS E  1 61  ? 13.627 30.794  17.444  1.00 33.69 ? 62  HIS E N   1 
ATOM   5904 C  CA  . HIS E  1 61  ? 12.984 31.941  16.807  1.00 37.34 ? 62  HIS E CA  1 
ATOM   5905 C  C   . HIS E  1 61  ? 13.076 31.854  15.294  1.00 36.05 ? 62  HIS E C   1 
ATOM   5906 O  O   . HIS E  1 61  ? 12.091 32.116  14.592  1.00 33.49 ? 62  HIS E O   1 
ATOM   5907 C  CB  . HIS E  1 61  ? 13.616 33.248  17.286  1.00 39.67 ? 62  HIS E CB  1 
ATOM   5908 C  CG  . HIS E  1 61  ? 13.188 33.637  18.659  1.00 50.00 ? 62  HIS E CG  1 
ATOM   5909 N  ND1 . HIS E  1 61  ? 13.806 34.633  19.389  1.00 47.12 ? 62  HIS E ND1 1 
ATOM   5910 C  CD2 . HIS E  1 61  ? 12.196 33.146  19.440  1.00 48.08 ? 62  HIS E CD2 1 
ATOM   5911 C  CE1 . HIS E  1 61  ? 13.198 34.743  20.559  1.00 58.78 ? 62  HIS E CE1 1 
ATOM   5912 N  NE2 . HIS E  1 61  ? 12.225 33.850  20.617  1.00 57.58 ? 62  HIS E NE2 1 
ATOM   5913 N  N   . ALA E  1 62  ? 14.261 31.508  14.769  1.00 30.41 ? 63  ALA E N   1 
ATOM   5914 C  CA  . ALA E  1 62  ? 14.406 31.417  13.321  1.00 36.76 ? 63  ALA E CA  1 
ATOM   5915 C  C   . ALA E  1 62  ? 13.531 30.301  12.760  1.00 35.74 ? 63  ALA E C   1 
ATOM   5916 O  O   . ALA E  1 62  ? 12.875 30.479  11.726  1.00 32.49 ? 63  ALA E O   1 
ATOM   5917 C  CB  . ALA E  1 62  ? 15.874 31.214  12.937  1.00 32.61 ? 63  ALA E CB  1 
ATOM   5918 N  N   . GLN E  1 63  ? 13.472 29.162  13.455  1.00 35.18 ? 64  GLN E N   1 
ATOM   5919 C  CA  . GLN E  1 63  ? 12.690 28.032  12.963  1.00 35.92 ? 64  GLN E CA  1 
ATOM   5920 C  C   . GLN E  1 63  ? 11.192 28.330  12.984  1.00 37.72 ? 64  GLN E C   1 
ATOM   5921 O  O   . GLN E  1 63  ? 10.451 27.884  12.098  1.00 31.88 ? 64  GLN E O   1 
ATOM   5922 C  CB  . GLN E  1 63  ? 13.005 26.799  13.791  1.00 35.35 ? 64  GLN E CB  1 
ATOM   5923 C  CG  . GLN E  1 63  ? 14.303 26.119  13.393  1.00 41.92 ? 64  GLN E CG  1 
ATOM   5924 C  CD  . GLN E  1 63  ? 14.675 25.038  14.388  1.00 50.97 ? 64  GLN E CD  1 
ATOM   5925 O  OE1 . GLN E  1 63  ? 13.859 24.669  15.241  1.00 59.51 ? 64  GLN E OE1 1 
ATOM   5926 N  NE2 . GLN E  1 63  ? 15.904 24.529  14.296  1.00 45.94 ? 64  GLN E NE2 1 
ATOM   5927 N  N   . THR E  1 64  ? 10.734 29.084  13.980  1.00 30.24 ? 65  THR E N   1 
ATOM   5928 C  CA  . THR E  1 64  ? 9.331  29.469  14.021  1.00 33.79 ? 65  THR E CA  1 
ATOM   5929 C  C   . THR E  1 64  ? 8.969  30.343  12.825  1.00 32.81 ? 65  THR E C   1 
ATOM   5930 O  O   . THR E  1 64  ? 7.893  30.184  12.242  1.00 31.06 ? 65  THR E O   1 
ATOM   5931 C  CB  . THR E  1 64  ? 9.029  30.175  15.344  1.00 32.28 ? 65  THR E CB  1 
ATOM   5932 O  OG1 . THR E  1 64  ? 9.274  29.266  16.418  1.00 35.07 ? 65  THR E OG1 1 
ATOM   5933 C  CG2 . THR E  1 64  ? 7.580  30.651  15.415  1.00 35.40 ? 65  THR E CG2 1 
ATOM   5934 N  N   . PHE E  1 65  ? 9.865  31.253  12.428  1.00 31.89 ? 66  PHE E N   1 
ATOM   5935 C  CA  . PHE E  1 65  ? 9.628  32.043  11.221  1.00 27.01 ? 66  PHE E CA  1 
ATOM   5936 C  C   . PHE E  1 65  ? 9.601  31.166  9.969   1.00 30.90 ? 66  PHE E C   1 
ATOM   5937 O  O   . PHE E  1 65  ? 8.801  31.404  9.058   1.00 30.57 ? 66  PHE E O   1 
ATOM   5938 C  CB  . PHE E  1 65  ? 10.700 33.114  11.080  1.00 32.28 ? 66  PHE E CB  1 
ATOM   5939 C  CG  . PHE E  1 65  ? 10.377 34.410  11.765  1.00 35.93 ? 66  PHE E CG  1 
ATOM   5940 C  CD1 . PHE E  1 65  ? 9.167  35.060  11.533  1.00 37.54 ? 66  PHE E CD1 1 
ATOM   5941 C  CD2 . PHE E  1 65  ? 11.295 34.995  12.631  1.00 37.54 ? 66  PHE E CD2 1 
ATOM   5942 C  CE1 . PHE E  1 65  ? 8.873  36.278  12.153  1.00 36.46 ? 66  PHE E CE1 1 
ATOM   5943 C  CE2 . PHE E  1 65  ? 11.011 36.209  13.259  1.00 35.47 ? 66  PHE E CE2 1 
ATOM   5944 C  CZ  . PHE E  1 65  ? 9.792  36.850  13.015  1.00 38.74 ? 66  PHE E CZ  1 
ATOM   5945 N  N   . MET E  1 66  ? 10.468 30.149  9.896   1.00 30.42 ? 67  MET E N   1 
ATOM   5946 C  CA  . MET E  1 66  ? 10.450 29.261  8.736   1.00 29.99 ? 67  MET E CA  1 
ATOM   5947 C  C   . MET E  1 66  ? 9.125  28.502  8.642   1.00 33.25 ? 67  MET E C   1 
ATOM   5948 O  O   . MET E  1 66  ? 8.550  28.380  7.553   1.00 32.29 ? 67  MET E O   1 
ATOM   5949 C  CB  . MET E  1 66  ? 11.623 28.288  8.802   1.00 28.44 ? 67  MET E CB  1 
ATOM   5950 C  CG  . MET E  1 66  ? 12.956 28.978  8.940   1.00 31.03 ? 67  MET E CG  1 
ATOM   5951 S  SD  . MET E  1 66  ? 14.408 27.887  9.024   1.00 38.71 ? 67  MET E SD  1 
ATOM   5952 C  CE  . MET E  1 66  ? 14.392 27.161  7.371   1.00 39.08 ? 67  MET E CE  1 
ATOM   5953 N  N   . LYS E  1 67  ? 8.629  27.980  9.771   1.00 32.92 ? 68  LYS E N   1 
ATOM   5954 C  CA  . LYS E  1 67  ? 7.320  27.329  9.771   1.00 37.22 ? 68  LYS E CA  1 
ATOM   5955 C  C   . LYS E  1 67  ? 6.237  28.302  9.348   1.00 33.57 ? 68  LYS E C   1 
ATOM   5956 O  O   . LYS E  1 67  ? 5.308  27.930  8.621   1.00 31.21 ? 68  LYS E O   1 
ATOM   5957 C  CB  . LYS E  1 67  ? 6.971  26.770  11.151  1.00 31.80 ? 68  LYS E CB  1 
ATOM   5958 C  CG  . LYS E  1 67  ? 7.857  25.663  11.631  1.00 42.90 ? 68  LYS E CG  1 
ATOM   5959 C  CD  . LYS E  1 67  ? 7.640  25.383  13.119  1.00 52.41 ? 68  LYS E CD  1 
ATOM   5960 C  CE  . LYS E  1 67  ? 8.978  25.297  13.859  1.00 45.26 ? 68  LYS E CE  1 
ATOM   5961 N  NZ  . LYS E  1 67  ? 9.554  23.937  13.777  1.00 46.43 ? 68  LYS E NZ  1 
ATOM   5962 N  N   . TYR E  1 68  ? 6.328  29.548  9.822   1.00 28.48 ? 69  TYR E N   1 
ATOM   5963 C  CA  . TYR E  1 68  ? 5.312  30.536  9.496   1.00 30.27 ? 69  TYR E CA  1 
ATOM   5964 C  C   . TYR E  1 68  ? 5.281  30.785  8.000   1.00 29.52 ? 69  TYR E C   1 
ATOM   5965 O  O   . TYR E  1 68  ? 4.211  30.811  7.385   1.00 29.95 ? 69  TYR E O   1 
ATOM   5966 C  CB  . TYR E  1 68  ? 5.570  31.840  10.244  1.00 31.63 ? 69  TYR E CB  1 
ATOM   5967 C  CG  . TYR E  1 68  ? 4.438  32.823  10.052  1.00 32.74 ? 69  TYR E CG  1 
ATOM   5968 C  CD1 . TYR E  1 68  ? 3.284  32.724  10.816  1.00 32.16 ? 69  TYR E CD1 1 
ATOM   5969 C  CD2 . TYR E  1 68  ? 4.511  33.829  9.090   1.00 30.65 ? 69  TYR E CD2 1 
ATOM   5970 C  CE1 . TYR E  1 68  ? 2.239  33.601  10.643  1.00 33.91 ? 69  TYR E CE1 1 
ATOM   5971 C  CE2 . TYR E  1 68  ? 3.453  34.721  8.901   1.00 30.74 ? 69  TYR E CE2 1 
ATOM   5972 C  CZ  . TYR E  1 68  ? 2.324  34.595  9.692   1.00 32.04 ? 69  TYR E CZ  1 
ATOM   5973 O  OH  . TYR E  1 68  ? 1.260  35.450  9.543   1.00 34.13 ? 69  TYR E OH  1 
ATOM   5974 N  N   . GLN E  1 69  ? 6.460  30.953  7.404   1.00 28.32 ? 70  GLN E N   1 
ATOM   5975 C  CA  . GLN E  1 69  ? 6.575  31.163  5.970   1.00 32.06 ? 70  GLN E CA  1 
ATOM   5976 C  C   . GLN E  1 69  ? 5.838  30.063  5.208   1.00 32.22 ? 70  GLN E C   1 
ATOM   5977 O  O   . GLN E  1 69  ? 5.023  30.344  4.321   1.00 31.66 ? 70  GLN E O   1 
ATOM   5978 C  CB  . GLN E  1 69  ? 8.068  31.233  5.609   1.00 31.57 ? 70  GLN E CB  1 
ATOM   5979 C  CG  . GLN E  1 69  ? 8.387  31.618  4.183   1.00 38.30 ? 70  GLN E CG  1 
ATOM   5980 C  CD  . GLN E  1 69  ? 8.299  33.123  3.954   1.00 39.81 ? 70  GLN E CD  1 
ATOM   5981 O  OE1 . GLN E  1 69  ? 7.202  33.680  3.837   1.00 37.42 ? 70  GLN E OE1 1 
ATOM   5982 N  NE2 . GLN E  1 69  ? 9.448  33.785  3.900   1.00 32.97 ? 70  GLN E NE2 1 
ATOM   5983 N  N   . ASN E  1 70  ? 6.062  28.800  5.597   1.00 30.86 ? 71  ASN E N   1 
ATOM   5984 C  CA  . ASN E  1 70  ? 5.370  27.673  4.968   1.00 31.70 ? 71  ASN E CA  1 
ATOM   5985 C  C   . ASN E  1 70  ? 3.871  27.689  5.260   1.00 34.19 ? 71  ASN E C   1 
ATOM   5986 O  O   . ASN E  1 70  ? 3.064  27.301  4.403   1.00 32.01 ? 71  ASN E O   1 
ATOM   5987 C  CB  . ASN E  1 70  ? 5.974  26.347  5.446   1.00 32.98 ? 71  ASN E CB  1 
ATOM   5988 C  CG  . ASN E  1 70  ? 7.175  25.916  4.617   1.00 37.02 ? 71  ASN E CG  1 
ATOM   5989 O  OD1 . ASN E  1 70  ? 7.495  26.527  3.590   1.00 34.26 ? 71  ASN E OD1 1 
ATOM   5990 N  ND2 . ASN E  1 70  ? 7.847  24.855  5.063   1.00 33.93 ? 71  ASN E ND2 1 
ATOM   5991 N  N   . LYS E  1 71  ? 3.482  28.107  6.470   1.00 31.71 ? 72  LYS E N   1 
ATOM   5992 C  CA  . LYS E  1 71  ? 2.066  28.157  6.828   1.00 35.39 ? 72  LYS E CA  1 
ATOM   5993 C  C   . LYS E  1 71  ? 1.302  29.131  5.936   1.00 36.04 ? 72  LYS E C   1 
ATOM   5994 O  O   . LYS E  1 71  ? 0.161  28.859  5.544   1.00 31.28 ? 72  LYS E O   1 
ATOM   5995 C  CB  . LYS E  1 71  ? 1.913  28.539  8.301   1.00 34.08 ? 72  LYS E CB  1 
ATOM   5996 C  CG  . LYS E  1 71  ? 0.585  28.182  8.916   1.00 42.06 ? 72  LYS E CG  1 
ATOM   5997 C  CD  . LYS E  1 71  ? 0.591  28.462  10.431  1.00 47.47 ? 72  LYS E CD  1 
ATOM   5998 C  CE  . LYS E  1 71  ? 1.604  27.575  11.178  1.00 53.60 ? 72  LYS E CE  1 
ATOM   5999 N  NZ  . LYS E  1 71  ? 2.622  28.346  11.981  1.00 50.35 ? 72  LYS E NZ  1 
ATOM   6000 N  N   . ARG E  1 72  ? 1.923  30.261  5.581   1.00 31.05 ? 73  ARG E N   1 
ATOM   6001 C  CA  . ARG E  1 72  ? 1.251  31.269  4.773   1.00 31.47 ? 73  ARG E CA  1 
ATOM   6002 C  C   . ARG E  1 72  ? 1.412  31.036  3.280   1.00 31.93 ? 73  ARG E C   1 
ATOM   6003 O  O   . ARG E  1 72  ? 0.811  31.768  2.489   1.00 30.77 ? 73  ARG E O   1 
ATOM   6004 C  CB  . ARG E  1 72  ? 1.769  32.667  5.117   1.00 30.98 ? 73  ARG E CB  1 
ATOM   6005 C  CG  . ARG E  1 72  ? 1.503  33.071  6.552   1.00 31.52 ? 73  ARG E CG  1 
ATOM   6006 C  CD  . ARG E  1 72  ? -0.003 33.095  6.884   1.00 32.56 ? 73  ARG E CD  1 
ATOM   6007 N  NE  . ARG E  1 72  ? -0.738 34.040  6.050   1.00 32.26 ? 73  ARG E NE  1 
ATOM   6008 C  CZ  . ARG E  1 72  ? -0.745 35.359  6.203   1.00 33.19 ? 73  ARG E CZ  1 
ATOM   6009 N  NH1 . ARG E  1 72  ? -0.065 35.956  7.171   1.00 33.28 ? 73  ARG E NH1 1 
ATOM   6010 N  NH2 . ARG E  1 72  ? -1.469 36.099  5.374   1.00 30.30 ? 73  ARG E NH2 1 
ATOM   6011 N  N   . GLY E  1 73  ? 2.196  30.041  2.877   1.00 32.17 ? 74  GLY E N   1 
ATOM   6012 C  CA  . GLY E  1 73  ? 2.425  29.792  1.468   1.00 34.51 ? 74  GLY E CA  1 
ATOM   6013 C  C   . GLY E  1 73  ? 3.528  30.609  0.834   1.00 36.28 ? 74  GLY E C   1 
ATOM   6014 O  O   . GLY E  1 73  ? 3.576  30.703  -0.398  1.00 40.82 ? 74  GLY E O   1 
ATOM   6015 N  N   . GLY E  1 74  ? 4.399  31.230  1.629   1.00 33.33 ? 75  GLY E N   1 
ATOM   6016 C  CA  . GLY E  1 74  ? 5.581  31.878  1.102   1.00 36.57 ? 75  GLY E CA  1 
ATOM   6017 C  C   . GLY E  1 74  ? 6.719  30.883  0.920   1.00 38.76 ? 75  GLY E C   1 
ATOM   6018 O  O   . GLY E  1 74  ? 6.610  29.694  1.203   1.00 37.06 ? 75  GLY E O   1 
ATOM   6019 N  N   . ARG E  1 75  ? 7.847  31.382  0.439   1.00 39.09 ? 76  ARG E N   1 
ATOM   6020 C  CA  . ARG E  1 75  ? 8.967  30.514  0.106   1.00 40.07 ? 76  ARG E CA  1 
ATOM   6021 C  C   . ARG E  1 75  ? 10.169 30.898  0.952   1.00 36.13 ? 76  ARG E C   1 
ATOM   6022 O  O   . ARG E  1 75  ? 10.606 32.053  0.924   1.00 37.84 ? 76  ARG E O   1 
ATOM   6023 C  CB  . ARG E  1 75  ? 9.267  30.595  -1.388  1.00 41.60 ? 76  ARG E CB  1 
ATOM   6024 C  CG  . ARG E  1 75  ? 8.222  29.841  -2.221  1.00 50.95 ? 76  ARG E CG  1 
ATOM   6025 C  CD  . ARG E  1 75  ? 8.131  28.337  -1.871  1.00 55.45 ? 76  ARG E CD  1 
ATOM   6026 N  NE  . ARG E  1 75  ? 7.308  28.018  -0.700  1.00 54.44 ? 76  ARG E NE  1 
ATOM   6027 C  CZ  . ARG E  1 75  ? 6.003  27.753  -0.736  1.00 59.50 ? 76  ARG E CZ  1 
ATOM   6028 N  NH1 . ARG E  1 75  ? 5.324  27.766  -1.877  1.00 58.53 ? 76  ARG E NH1 1 
ATOM   6029 N  NH2 . ARG E  1 75  ? 5.367  27.439  0.398   1.00 48.96 ? 76  ARG E NH2 1 
ATOM   6030 N  N   . ILE E  1 76  ? 10.670 29.938  1.732   1.00 32.65 ? 77  ILE E N   1 
ATOM   6031 C  CA  . ILE E  1 76  ? 11.857 30.167  2.543   1.00 32.16 ? 77  ILE E CA  1 
ATOM   6032 C  C   . ILE E  1 76  ? 13.061 30.338  1.629   1.00 34.65 ? 77  ILE E C   1 
ATOM   6033 O  O   . ILE E  1 76  ? 13.297 29.525  0.727   1.00 34.49 ? 77  ILE E O   1 
ATOM   6034 C  CB  . ILE E  1 76  ? 12.085 29.004  3.517   1.00 33.22 ? 77  ILE E CB  1 
ATOM   6035 C  CG1 . ILE E  1 76  ? 10.914 28.860  4.492   1.00 30.91 ? 77  ILE E CG1 1 
ATOM   6036 C  CG2 . ILE E  1 76  ? 13.370 29.229  4.279   1.00 30.29 ? 77  ILE E CG2 1 
ATOM   6037 C  CD1 . ILE E  1 76  ? 10.827 27.480  5.088   1.00 28.24 ? 77  ILE E CD1 1 
ATOM   6038 N  N   . VAL E  1 77  ? 13.836 31.392  1.863   1.00 34.12 ? 78  VAL E N   1 
ATOM   6039 C  CA  . VAL E  1 77  ? 15.073 31.632  1.131   1.00 37.02 ? 78  VAL E CA  1 
ATOM   6040 C  C   . VAL E  1 77  ? 16.168 31.858  2.169   1.00 37.25 ? 78  VAL E C   1 
ATOM   6041 O  O   . VAL E  1 77  ? 16.161 32.876  2.870   1.00 35.45 ? 78  VAL E O   1 
ATOM   6042 C  CB  . VAL E  1 77  ? 14.965 32.823  0.165   1.00 39.98 ? 78  VAL E CB  1 
ATOM   6043 C  CG1 . VAL E  1 77  ? 16.313 33.116  -0.465  1.00 36.10 ? 78  VAL E CG1 1 
ATOM   6044 C  CG2 . VAL E  1 77  ? 13.930 32.533  -0.925  1.00 38.41 ? 78  VAL E CG2 1 
ATOM   6045 N  N   . LEU E  1 78  ? 17.096 30.905  2.284   1.00 37.09 ? 79  LEU E N   1 
ATOM   6046 C  CA  . LEU E  1 78  ? 18.160 30.994  3.278   1.00 38.10 ? 79  LEU E CA  1 
ATOM   6047 C  C   . LEU E  1 78  ? 19.406 31.644  2.688   1.00 34.64 ? 79  LEU E C   1 
ATOM   6048 O  O   . LEU E  1 78  ? 19.821 31.322  1.575   1.00 36.27 ? 79  LEU E O   1 
ATOM   6049 C  CB  . LEU E  1 78  ? 18.501 29.611  3.822   1.00 30.92 ? 79  LEU E CB  1 
ATOM   6050 C  CG  . LEU E  1 78  ? 17.316 28.872  4.452   1.00 38.56 ? 79  LEU E CG  1 
ATOM   6051 C  CD1 . LEU E  1 78  ? 17.675 27.403  4.648   1.00 33.34 ? 79  LEU E CD1 1 
ATOM   6052 C  CD2 . LEU E  1 78  ? 16.851 29.529  5.783   1.00 32.28 ? 79  LEU E CD2 1 
ATOM   6053 N  N   . GLN E  1 79  ? 19.996 32.555  3.449   1.00 36.99 ? 80  GLN E N   1 
ATOM   6054 C  CA  . GLN E  1 79  ? 21.190 33.298  3.065   1.00 38.19 ? 80  GLN E CA  1 
ATOM   6055 C  C   . GLN E  1 79  ? 22.353 32.897  3.961   1.00 36.91 ? 80  GLN E C   1 
ATOM   6056 O  O   . GLN E  1 79  ? 22.170 32.279  5.018   1.00 30.22 ? 80  GLN E O   1 
ATOM   6057 C  CB  . GLN E  1 79  ? 20.955 34.813  3.181   1.00 41.20 ? 80  GLN E CB  1 
ATOM   6058 C  CG  . GLN E  1 79  ? 19.775 35.368  2.377   1.00 50.47 ? 80  GLN E CG  1 
ATOM   6059 C  CD  . GLN E  1 79  ? 20.074 35.486  0.886   1.00 62.38 ? 80  GLN E CD  1 
ATOM   6060 O  OE1 . GLN E  1 79  ? 19.154 35.515  0.062   1.00 63.51 ? 80  GLN E OE1 1 
ATOM   6061 N  NE2 . GLN E  1 79  ? 21.363 35.572  0.535   1.00 60.47 ? 80  GLN E NE2 1 
ATOM   6062 N  N   . GLN E  1 80  ? 23.556 33.300  3.546   1.00 32.02 ? 81  GLN E N   1 
ATOM   6063 C  CA  . GLN E  1 80  ? 24.746 33.049  4.349   1.00 32.30 ? 81  GLN E CA  1 
ATOM   6064 C  C   . GLN E  1 80  ? 24.594 33.630  5.755   1.00 29.01 ? 81  GLN E C   1 
ATOM   6065 O  O   . GLN E  1 80  ? 23.912 34.633  5.970   1.00 27.11 ? 81  GLN E O   1 
ATOM   6066 C  CB  . GLN E  1 80  ? 25.981 33.638  3.665   1.00 33.87 ? 81  GLN E CB  1 
ATOM   6067 C  CG  . GLN E  1 80  ? 25.872 35.128  3.377   1.00 39.70 ? 81  GLN E CG  1 
ATOM   6068 C  CD  . GLN E  1 80  ? 26.855 35.584  2.318   1.00 46.31 ? 81  GLN E CD  1 
ATOM   6069 O  OE1 . GLN E  1 80  ? 27.245 34.804  1.440   1.00 45.09 ? 81  GLN E OE1 1 
ATOM   6070 N  NE2 . GLN E  1 80  ? 27.277 36.848  2.401   1.00 44.35 ? 81  GLN E NE2 1 
ATOM   6071 N  N   . ILE E  1 81  ? 25.227 32.979  6.724   1.00 28.76 ? 82  ILE E N   1 
ATOM   6072 C  CA  . ILE E  1 81  ? 25.222 33.431  8.114   1.00 28.17 ? 82  ILE E CA  1 
ATOM   6073 C  C   . ILE E  1 81  ? 26.611 33.972  8.424   1.00 28.82 ? 82  ILE E C   1 
ATOM   6074 O  O   . ILE E  1 81  ? 27.557 33.195  8.598   1.00 31.41 ? 82  ILE E O   1 
ATOM   6075 C  CB  . ILE E  1 81  ? 24.845 32.302  9.083   1.00 28.49 ? 82  ILE E CB  1 
ATOM   6076 C  CG1 . ILE E  1 81  ? 23.530 31.638  8.675   1.00 29.09 ? 82  ILE E CG1 1 
ATOM   6077 C  CG2 . ILE E  1 81  ? 24.728 32.843  10.507  1.00 26.40 ? 82  ILE E CG2 1 
ATOM   6078 C  CD1 . ILE E  1 81  ? 23.199 30.397  9.508   1.00 26.94 ? 82  ILE E CD1 1 
ATOM   6079 N  N   . ALA E  1 82  ? 26.735 35.296  8.496   1.00 29.07 ? 83  ALA E N   1 
ATOM   6080 C  CA  . ALA E  1 82  ? 28.008 35.943  8.792   1.00 30.67 ? 83  ALA E CA  1 
ATOM   6081 C  C   . ALA E  1 82  ? 28.574 35.475  10.135  1.00 32.20 ? 83  ALA E C   1 
ATOM   6082 O  O   . ALA E  1 82  ? 27.842 35.189  11.084  1.00 30.07 ? 83  ALA E O   1 
ATOM   6083 C  CB  . ALA E  1 82  ? 27.833 37.471  8.806   1.00 27.79 ? 83  ALA E CB  1 
ATOM   6084 N  N   . ALA E  1 83  ? 29.888 35.402  10.209  1.00 28.56 ? 84  ALA E N   1 
ATOM   6085 C  CA  . ALA E  1 83  ? 30.521 35.117  11.485  1.00 31.73 ? 84  ALA E CA  1 
ATOM   6086 C  C   . ALA E  1 83  ? 30.543 36.389  12.318  1.00 34.97 ? 84  ALA E C   1 
ATOM   6087 O  O   . ALA E  1 83  ? 30.543 37.487  11.764  1.00 32.57 ? 84  ALA E O   1 
ATOM   6088 C  CB  . ALA E  1 83  ? 31.952 34.608  11.283  1.00 29.67 ? 84  ALA E CB  1 
ATOM   6089 N  N   . PRO E  1 84  ? 30.548 36.272  13.648  1.00 34.74 ? 85  PRO E N   1 
ATOM   6090 C  CA  . PRO E  1 84  ? 30.733 37.469  14.478  1.00 37.43 ? 85  PRO E CA  1 
ATOM   6091 C  C   . PRO E  1 84  ? 32.052 38.135  14.121  1.00 42.44 ? 85  PRO E C   1 
ATOM   6092 O  O   . PRO E  1 84  ? 33.075 37.469  13.950  1.00 44.56 ? 85  PRO E O   1 
ATOM   6093 C  CB  . PRO E  1 84  ? 30.741 36.924  15.911  1.00 35.99 ? 85  PRO E CB  1 
ATOM   6094 C  CG  . PRO E  1 84  ? 30.132 35.571  15.831  1.00 34.44 ? 85  PRO E CG  1 
ATOM   6095 C  CD  . PRO E  1 84  ? 30.440 35.046  14.451  1.00 34.01 ? 85  PRO E CD  1 
ATOM   6096 N  N   . SER E  1 85  ? 32.019 39.460  13.984  1.00 49.91 ? 86  SER E N   1 
ATOM   6097 C  CA  . SER E  1 85  ? 33.212 40.183  13.548  1.00 50.88 ? 86  SER E CA  1 
ATOM   6098 C  C   . SER E  1 85  ? 34.318 40.131  14.607  1.00 55.21 ? 86  SER E C   1 
ATOM   6099 O  O   . SER E  1 85  ? 35.486 39.873  14.289  1.00 58.65 ? 86  SER E O   1 
ATOM   6100 C  CB  . SER E  1 85  ? 32.840 41.627  13.204  1.00 53.57 ? 86  SER E CB  1 
ATOM   6101 O  OG  . SER E  1 85  ? 33.963 42.478  13.309  1.00 60.90 ? 86  SER E OG  1 
ATOM   6102 N  N   . MET E  1 86  ? 33.973 40.363  15.872  1.00 46.80 ? 87  MET E N   1 
ATOM   6103 C  CA  . MET E  1 86  ? 34.920 40.273  16.982  1.00 56.11 ? 87  MET E CA  1 
ATOM   6104 C  C   . MET E  1 86  ? 34.550 39.060  17.833  1.00 49.47 ? 87  MET E C   1 
ATOM   6105 O  O   . MET E  1 86  ? 33.493 39.051  18.468  1.00 51.98 ? 87  MET E O   1 
ATOM   6106 C  CB  . MET E  1 86  ? 34.905 41.558  17.817  1.00 58.46 ? 87  MET E CB  1 
ATOM   6107 C  CG  . MET E  1 86  ? 36.104 41.720  18.759  1.00 64.88 ? 87  MET E CG  1 
ATOM   6108 S  SD  . MET E  1 86  ? 37.710 41.433  17.960  1.00 99.42 ? 87  MET E SD  1 
ATOM   6109 C  CE  . MET E  1 86  ? 38.335 40.012  18.860  1.00 58.22 ? 87  MET E CE  1 
ATOM   6110 N  N   . GLN E  1 87  ? 35.426 38.053  17.868  1.00 49.12 ? 88  GLN E N   1 
ATOM   6111 C  CA  . GLN E  1 87  ? 35.156 36.798  18.565  1.00 45.01 ? 88  GLN E CA  1 
ATOM   6112 C  C   . GLN E  1 87  ? 35.867 36.668  19.909  1.00 47.39 ? 88  GLN E C   1 
ATOM   6113 O  O   . GLN E  1 87  ? 35.699 35.651  20.590  1.00 45.70 ? 88  GLN E O   1 
ATOM   6114 C  CB  . GLN E  1 87  ? 35.541 35.617  17.688  1.00 37.71 ? 88  GLN E CB  1 
ATOM   6115 C  CG  . GLN E  1 87  ? 34.608 35.430  16.537  1.00 46.23 ? 88  GLN E CG  1 
ATOM   6116 C  CD  . GLN E  1 87  ? 35.004 34.273  15.660  1.00 43.79 ? 88  GLN E CD  1 
ATOM   6117 O  OE1 . GLN E  1 87  ? 35.313 33.171  16.146  1.00 38.43 ? 88  GLN E OE1 1 
ATOM   6118 N  NE2 . GLN E  1 87  ? 34.994 34.507  14.351  1.00 38.62 ? 88  GLN E NE2 1 
ATOM   6119 N  N   . GLU E  1 88  ? 36.673 37.644  20.302  1.00 53.84 ? 89  GLU E N   1 
ATOM   6120 C  CA  . GLU E  1 88  ? 37.203 37.699  21.663  1.00 54.20 ? 89  GLU E CA  1 
ATOM   6121 C  C   . GLU E  1 88  ? 36.384 38.749  22.401  1.00 47.53 ? 89  GLU E C   1 
ATOM   6122 O  O   . GLU E  1 88  ? 36.565 39.952  22.209  1.00 48.39 ? 89  GLU E O   1 
ATOM   6123 C  CB  . GLU E  1 88  ? 38.692 38.012  21.677  1.00 53.61 ? 89  GLU E CB  1 
ATOM   6124 C  CG  . GLU E  1 88  ? 39.525 36.813  21.311  1.00 62.71 ? 89  GLU E CG  1 
ATOM   6125 C  CD  . GLU E  1 88  ? 40.705 36.636  22.235  1.00 71.23 ? 89  GLU E CD  1 
ATOM   6126 O  OE1 . GLU E  1 88  ? 41.836 36.524  21.718  1.00 81.07 ? 89  GLU E OE1 1 
ATOM   6127 O  OE2 . GLU E  1 88  ? 40.503 36.614  23.474  1.00 74.08 ? 89  GLU E OE2 1 
ATOM   6128 N  N   . TRP E  1 89  ? 35.477 38.278  23.239  1.00 44.43 ? 90  TRP E N   1 
ATOM   6129 C  CA  . TRP E  1 89  ? 34.466 39.135  23.825  1.00 46.63 ? 90  TRP E CA  1 
ATOM   6130 C  C   . TRP E  1 89  ? 34.950 39.893  25.049  1.00 45.71 ? 90  TRP E C   1 
ATOM   6131 O  O   . TRP E  1 89  ? 34.260 40.823  25.474  1.00 49.42 ? 90  TRP E O   1 
ATOM   6132 C  CB  . TRP E  1 89  ? 33.247 38.280  24.149  1.00 40.70 ? 90  TRP E CB  1 
ATOM   6133 C  CG  . TRP E  1 89  ? 32.772 37.656  22.909  1.00 39.75 ? 90  TRP E CG  1 
ATOM   6134 C  CD1 . TRP E  1 89  ? 33.064 36.401  22.443  1.00 40.98 ? 90  TRP E CD1 1 
ATOM   6135 C  CD2 . TRP E  1 89  ? 31.971 38.283  21.910  1.00 40.47 ? 90  TRP E CD2 1 
ATOM   6136 N  NE1 . TRP E  1 89  ? 32.458 36.198  21.225  1.00 39.55 ? 90  TRP E NE1 1 
ATOM   6137 C  CE2 . TRP E  1 89  ? 31.781 37.340  20.874  1.00 41.43 ? 90  TRP E CE2 1 
ATOM   6138 C  CE3 . TRP E  1 89  ? 31.378 39.548  21.797  1.00 41.40 ? 90  TRP E CE3 1 
ATOM   6139 C  CZ2 . TRP E  1 89  ? 31.018 37.622  19.736  1.00 40.19 ? 90  TRP E CZ2 1 
ATOM   6140 C  CZ3 . TRP E  1 89  ? 30.625 39.830  20.672  1.00 41.80 ? 90  TRP E CZ3 1 
ATOM   6141 C  CH2 . TRP E  1 89  ? 30.454 38.868  19.650  1.00 43.97 ? 90  TRP E CH2 1 
ATOM   6142 N  N   . GLY E  1 90  ? 36.107 39.546  25.608  1.00 41.63 ? 91  GLY E N   1 
ATOM   6143 C  CA  . GLY E  1 90  ? 36.623 40.295  26.749  1.00 41.50 ? 91  GLY E CA  1 
ATOM   6144 C  C   . GLY E  1 90  ? 35.997 39.821  28.043  1.00 45.73 ? 91  GLY E C   1 
ATOM   6145 O  O   . GLY E  1 90  ? 35.932 38.617  28.307  1.00 50.00 ? 91  GLY E O   1 
ATOM   6146 N  N   . THR E  1 91  ? 35.528 40.767  28.856  1.00 39.91 ? 92  THR E N   1 
ATOM   6147 C  CA  . THR E  1 91  ? 34.951 40.476  30.163  1.00 40.95 ? 92  THR E CA  1 
ATOM   6148 C  C   . THR E  1 91  ? 33.465 40.122  30.050  1.00 41.67 ? 92  THR E C   1 
ATOM   6149 O  O   . THR E  1 91  ? 32.816 40.341  29.022  1.00 40.24 ? 92  THR E O   1 
ATOM   6150 C  CB  . THR E  1 91  ? 35.096 41.678  31.089  1.00 40.89 ? 92  THR E CB  1 
ATOM   6151 O  OG1 . THR E  1 91  ? 34.235 42.727  30.617  1.00 39.39 ? 92  THR E OG1 1 
ATOM   6152 C  CG2 . THR E  1 91  ? 36.538 42.174  31.111  1.00 40.77 ? 92  THR E CG2 1 
ATOM   6153 N  N   . GLY E  1 92  ? 32.916 39.597  31.149  1.00 37.30 ? 93  GLY E N   1 
ATOM   6154 C  CA  . GLY E  1 92  ? 31.489 39.306  31.188  1.00 38.13 ? 93  GLY E CA  1 
ATOM   6155 C  C   . GLY E  1 92  ? 30.619 40.525  30.921  1.00 36.28 ? 93  GLY E C   1 
ATOM   6156 O  O   . GLY E  1 92  ? 29.584 40.426  30.254  1.00 39.51 ? 93  GLY E O   1 
ATOM   6157 N  N   . LEU E  1 93  ? 31.033 41.692  31.422  1.00 30.68 ? 94  LEU E N   1 
ATOM   6158 C  CA  . LEU E  1 93  ? 30.261 42.912  31.205  1.00 36.33 ? 94  LEU E CA  1 
ATOM   6159 C  C   . LEU E  1 93  ? 30.287 43.340  29.738  1.00 39.20 ? 94  LEU E C   1 
ATOM   6160 O  O   . LEU E  1 93  ? 29.261 43.759  29.194  1.00 40.09 ? 94  LEU E O   1 
ATOM   6161 C  CB  . LEU E  1 93  ? 30.784 44.034  32.099  1.00 30.20 ? 94  LEU E CB  1 
ATOM   6162 C  CG  . LEU E  1 93  ? 30.031 45.364  32.015  1.00 38.61 ? 94  LEU E CG  1 
ATOM   6163 C  CD1 . LEU E  1 93  ? 28.561 45.175  32.321  1.00 36.05 ? 94  LEU E CD1 1 
ATOM   6164 C  CD2 . LEU E  1 93  ? 30.621 46.369  32.971  1.00 34.67 ? 94  LEU E CD2 1 
ATOM   6165 N  N   . GLU E  1 94  ? 31.444 43.245  29.079  1.00 39.27 ? 95  GLU E N   1 
ATOM   6166 C  CA  . GLU E  1 94  ? 31.510 43.616  27.669  1.00 40.92 ? 95  GLU E CA  1 
ATOM   6167 C  C   . GLU E  1 94  ? 30.607 42.728  26.820  1.00 36.62 ? 95  GLU E C   1 
ATOM   6168 O  O   . GLU E  1 94  ? 29.979 43.200  25.862  1.00 35.42 ? 95  GLU E O   1 
ATOM   6169 C  CB  . GLU E  1 94  ? 32.956 43.559  27.180  1.00 41.11 ? 95  GLU E CB  1 
ATOM   6170 C  CG  . GLU E  1 94  ? 33.794 44.720  27.683  1.00 45.49 ? 95  GLU E CG  1 
ATOM   6171 C  CD  . GLU E  1 94  ? 35.288 44.410  27.751  1.00 54.12 ? 95  GLU E CD  1 
ATOM   6172 O  OE1 . GLU E  1 94  ? 35.670 43.342  28.285  1.00 58.21 ? 95  GLU E OE1 1 
ATOM   6173 O  OE2 . GLU E  1 94  ? 36.089 45.249  27.287  1.00 59.78 ? 95  GLU E OE2 1 
ATOM   6174 N  N   . ALA E  1 95  ? 30.503 41.446  27.172  1.00 34.45 ? 96  ALA E N   1 
ATOM   6175 C  CA  . ALA E  1 95  ? 29.636 40.546  26.420  1.00 34.07 ? 96  ALA E CA  1 
ATOM   6176 C  C   . ALA E  1 95  ? 28.158 40.856  26.660  1.00 33.69 ? 96  ALA E C   1 
ATOM   6177 O  O   . ALA E  1 95  ? 27.357 40.807  25.721  1.00 33.08 ? 96  ALA E O   1 
ATOM   6178 C  CB  . ALA E  1 95  ? 29.950 39.096  26.780  1.00 32.15 ? 96  ALA E CB  1 
ATOM   6179 N  N   . LEU E  1 96  ? 27.775 41.154  27.911  1.00 33.54 ? 97  LEU E N   1 
ATOM   6180 C  CA  . LEU E  1 96  ? 26.388 41.534  28.197  1.00 37.00 ? 97  LEU E CA  1 
ATOM   6181 C  C   . LEU E  1 96  ? 26.001 42.804  27.457  1.00 32.68 ? 97  LEU E C   1 
ATOM   6182 O  O   . LEU E  1 96  ? 24.859 42.941  26.999  1.00 32.75 ? 97  LEU E O   1 
ATOM   6183 C  CB  . LEU E  1 96  ? 26.172 41.744  29.696  1.00 31.59 ? 97  LEU E CB  1 
ATOM   6184 C  CG  . LEU E  1 96  ? 26.183 40.499  30.575  1.00 36.95 ? 97  LEU E CG  1 
ATOM   6185 C  CD1 . LEU E  1 96  ? 25.976 40.909  32.012  1.00 29.28 ? 97  LEU E CD1 1 
ATOM   6186 C  CD2 . LEU E  1 96  ? 25.131 39.514  30.113  1.00 27.12 ? 97  LEU E CD2 1 
ATOM   6187 N  N   . GLN E  1 97  ? 26.940 43.748  27.335  1.00 30.03 ? 98  GLN E N   1 
ATOM   6188 C  CA  . GLN E  1 97  ? 26.653 44.993  26.634  1.00 34.20 ? 98  GLN E CA  1 
ATOM   6189 C  C   . GLN E  1 97  ? 26.482 44.758  25.138  1.00 36.84 ? 98  GLN E C   1 
ATOM   6190 O  O   . GLN E  1 97  ? 25.631 45.389  24.502  1.00 35.96 ? 98  GLN E O   1 
ATOM   6191 C  CB  . GLN E  1 97  ? 27.760 46.015  26.904  1.00 35.68 ? 98  GLN E CB  1 
ATOM   6192 C  CG  . GLN E  1 97  ? 27.640 46.671  28.274  1.00 36.47 ? 98  GLN E CG  1 
ATOM   6193 C  CD  . GLN E  1 97  ? 28.922 47.347  28.729  1.00 43.96 ? 98  GLN E CD  1 
ATOM   6194 O  OE1 . GLN E  1 97  ? 30.029 46.950  28.344  1.00 42.07 ? 98  GLN E OE1 1 
ATOM   6195 N  NE2 . GLN E  1 97  ? 28.777 48.378  29.556  1.00 41.68 ? 98  GLN E NE2 1 
ATOM   6196 N  N   . ALA E  1 98  ? 27.284 43.856  24.561  1.00 32.81 ? 99  ALA E N   1 
ATOM   6197 C  CA  . ALA E  1 98  ? 27.101 43.477  23.165  1.00 33.36 ? 99  ALA E CA  1 
ATOM   6198 C  C   . ALA E  1 98  ? 25.760 42.786  22.952  1.00 34.70 ? 99  ALA E C   1 
ATOM   6199 O  O   . ALA E  1 98  ? 25.057 43.081  21.977  1.00 33.70 ? 99  ALA E O   1 
ATOM   6200 C  CB  . ALA E  1 98  ? 28.247 42.572  22.712  1.00 32.22 ? 99  ALA E CB  1 
ATOM   6201 N  N   . ALA E  1 99  ? 25.393 41.863  23.854  1.00 32.94 ? 100 ALA E N   1 
ATOM   6202 C  CA  . ALA E  1 99  ? 24.096 41.193  23.770  1.00 35.99 ? 100 ALA E CA  1 
ATOM   6203 C  C   . ALA E  1 99  ? 22.941 42.187  23.868  1.00 34.00 ? 100 ALA E C   1 
ATOM   6204 O  O   . ALA E  1 99  ? 21.957 42.081  23.127  1.00 31.45 ? 100 ALA E O   1 
ATOM   6205 C  CB  . ALA E  1 99  ? 23.975 40.128  24.866  1.00 31.18 ? 100 ALA E CB  1 
ATOM   6206 N  N   . LEU E  1 100 ? 23.043 43.157  24.776  1.00 32.47 ? 101 LEU E N   1 
ATOM   6207 C  CA  . LEU E  1 100 ? 21.986 44.158  24.908  1.00 31.90 ? 101 LEU E CA  1 
ATOM   6208 C  C   . LEU E  1 100 ? 21.797 44.923  23.599  1.00 36.69 ? 101 LEU E C   1 
ATOM   6209 O  O   . LEU E  1 100 ? 20.667 45.093  23.128  1.00 36.06 ? 101 LEU E O   1 
ATOM   6210 C  CB  . LEU E  1 100 ? 22.308 45.117  26.063  1.00 30.94 ? 101 LEU E CB  1 
ATOM   6211 C  CG  . LEU E  1 100 ? 21.313 46.268  26.264  1.00 32.61 ? 101 LEU E CG  1 
ATOM   6212 C  CD1 . LEU E  1 100 ? 19.933 45.710  26.532  1.00 32.57 ? 101 LEU E CD1 1 
ATOM   6213 C  CD2 . LEU E  1 100 ? 21.748 47.209  27.377  1.00 33.51 ? 101 LEU E CD2 1 
ATOM   6214 N  N   . ASP E  1 101 ? 22.904 45.373  22.989  1.00 35.75 ? 102 ASP E N   1 
ATOM   6215 C  CA  . ASP E  1 101 ? 22.852 46.044  21.687  1.00 31.63 ? 102 ASP E CA  1 
ATOM   6216 C  C   . ASP E  1 101 ? 22.217 45.140  20.638  1.00 36.14 ? 102 ASP E C   1 
ATOM   6217 O  O   . ASP E  1 101 ? 21.360 45.567  19.857  1.00 33.80 ? 102 ASP E O   1 
ATOM   6218 C  CB  . ASP E  1 101 ? 24.265 46.411  21.241  1.00 39.30 ? 102 ASP E CB  1 
ATOM   6219 C  CG  . ASP E  1 101 ? 24.869 47.534  22.050  1.00 55.82 ? 102 ASP E CG  1 
ATOM   6220 O  OD1 . ASP E  1 101 ? 24.229 48.001  23.025  1.00 60.80 ? 102 ASP E OD1 1 
ATOM   6221 O  OD2 . ASP E  1 101 ? 26.016 47.927  21.731  1.00 65.20 ? 102 ASP E OD2 1 
ATOM   6222 N  N   . LEU E  1 102 ? 22.641 43.876  20.608  1.00 33.28 ? 103 LEU E N   1 
ATOM   6223 C  CA  . LEU E  1 102 ? 22.118 42.927  19.633  1.00 36.09 ? 103 LEU E CA  1 
ATOM   6224 C  C   . LEU E  1 102 ? 20.616 42.712  19.801  1.00 38.46 ? 103 LEU E C   1 
ATOM   6225 O  O   . LEU E  1 102 ? 19.877 42.672  18.808  1.00 35.31 ? 103 LEU E O   1 
ATOM   6226 C  CB  . LEU E  1 102 ? 22.865 41.607  19.767  1.00 32.76 ? 103 LEU E CB  1 
ATOM   6227 C  CG  . LEU E  1 102 ? 22.483 40.502  18.811  1.00 34.31 ? 103 LEU E CG  1 
ATOM   6228 C  CD1 . LEU E  1 102 ? 22.957 40.892  17.415  1.00 39.59 ? 103 LEU E CD1 1 
ATOM   6229 C  CD2 . LEU E  1 102 ? 23.129 39.223  19.256  1.00 31.24 ? 103 LEU E CD2 1 
ATOM   6230 N  N   . GLU E  1 103 ? 20.140 42.571  21.047  1.00 35.99 ? 104 GLU E N   1 
ATOM   6231 C  CA  . GLU E  1 103 ? 18.712 42.321  21.248  1.00 37.14 ? 104 GLU E CA  1 
ATOM   6232 C  C   . GLU E  1 103 ? 17.881 43.552  20.887  1.00 35.58 ? 104 GLU E C   1 
ATOM   6233 O  O   . GLU E  1 103 ? 16.774 43.426  20.347  1.00 33.58 ? 104 GLU E O   1 
ATOM   6234 C  CB  . GLU E  1 103 ? 18.432 41.882  22.692  1.00 36.59 ? 104 GLU E CB  1 
ATOM   6235 C  CG  . GLU E  1 103 ? 19.082 40.548  23.139  1.00 44.78 ? 104 GLU E CG  1 
ATOM   6236 C  CD  . GLU E  1 103 ? 18.482 39.278  22.480  1.00 49.75 ? 104 GLU E CD  1 
ATOM   6237 O  OE1 . GLU E  1 103 ? 17.538 39.383  21.671  1.00 55.49 ? 104 GLU E OE1 1 
ATOM   6238 O  OE2 . GLU E  1 103 ? 18.940 38.155  22.794  1.00 48.89 ? 104 GLU E OE2 1 
ATOM   6239 N  N   . LYS E  1 104 ? 18.395 44.751  21.170  1.00 32.43 ? 105 LYS E N   1 
ATOM   6240 C  CA  . LYS E  1 104 ? 17.691 45.962  20.754  1.00 33.21 ? 105 LYS E CA  1 
ATOM   6241 C  C   . LYS E  1 104 ? 17.643 46.083  19.237  1.00 34.43 ? 105 LYS E C   1 
ATOM   6242 O  O   . LYS E  1 104 ? 16.646 46.562  18.687  1.00 31.79 ? 105 LYS E O   1 
ATOM   6243 C  CB  . LYS E  1 104 ? 18.347 47.197  21.369  1.00 32.41 ? 105 LYS E CB  1 
ATOM   6244 C  CG  . LYS E  1 104 ? 17.882 47.505  22.787  1.00 38.74 ? 105 LYS E CG  1 
ATOM   6245 C  CD  . LYS E  1 104 ? 18.993 48.139  23.578  1.00 38.97 ? 105 LYS E CD  1 
ATOM   6246 C  CE  . LYS E  1 104 ? 18.551 49.395  24.322  1.00 42.90 ? 105 LYS E CE  1 
ATOM   6247 N  NZ  . LYS E  1 104 ? 19.734 50.062  25.031  1.00 42.87 ? 105 LYS E NZ  1 
ATOM   6248 N  N   . GLN E  1 105 ? 18.689 45.626  18.546  1.00 33.76 ? 106 GLN E N   1 
ATOM   6249 C  CA  . GLN E  1 105 ? 18.686 45.650  17.088  1.00 38.94 ? 106 GLN E CA  1 
ATOM   6250 C  C   . GLN E  1 105 ? 17.648 44.687  16.523  1.00 36.60 ? 106 GLN E C   1 
ATOM   6251 O  O   . GLN E  1 105 ? 16.941 45.017  15.563  1.00 37.27 ? 106 GLN E O   1 
ATOM   6252 C  CB  . GLN E  1 105 ? 20.081 45.310  16.562  1.00 38.67 ? 106 GLN E CB  1 
ATOM   6253 C  CG  . GLN E  1 105 ? 20.508 46.109  15.351  1.00 50.56 ? 106 GLN E CG  1 
ATOM   6254 C  CD  . GLN E  1 105 ? 20.585 47.615  15.628  1.00 64.79 ? 106 GLN E CD  1 
ATOM   6255 O  OE1 . GLN E  1 105 ? 21.385 48.066  16.456  1.00 63.27 ? 106 GLN E OE1 1 
ATOM   6256 N  NE2 . GLN E  1 105 ? 19.759 48.400  14.917  1.00 60.39 ? 106 GLN E NE2 1 
ATOM   6257 N  N   . VAL E  1 106 ? 17.546 43.489  17.100  1.00 33.00 ? 107 VAL E N   1 
ATOM   6258 C  CA  . VAL E  1 106 ? 16.515 42.552  16.669  1.00 32.29 ? 107 VAL E CA  1 
ATOM   6259 C  C   . VAL E  1 106 ? 15.133 43.122  16.971  1.00 33.92 ? 107 VAL E C   1 
ATOM   6260 O  O   . VAL E  1 106 ? 14.213 43.027  16.147  1.00 32.04 ? 107 VAL E O   1 
ATOM   6261 C  CB  . VAL E  1 106 ? 16.724 41.180  17.335  1.00 36.42 ? 107 VAL E CB  1 
ATOM   6262 C  CG1 . VAL E  1 106 ? 15.521 40.276  17.072  1.00 34.34 ? 107 VAL E CG1 1 
ATOM   6263 C  CG2 . VAL E  1 106 ? 18.028 40.524  16.851  1.00 32.32 ? 107 VAL E CG2 1 
ATOM   6264 N  N   . ASN E  1 107 ? 14.972 43.738  18.150  1.00 32.32 ? 108 ASN E N   1 
ATOM   6265 C  CA  . ASN E  1 107 ? 13.695 44.345  18.506  1.00 32.75 ? 108 ASN E CA  1 
ATOM   6266 C  C   . ASN E  1 107 ? 13.294 45.397  17.477  1.00 34.84 ? 108 ASN E C   1 
ATOM   6267 O  O   . ASN E  1 107 ? 12.162 45.392  16.972  1.00 28.48 ? 108 ASN E O   1 
ATOM   6268 C  CB  . ASN E  1 107 ? 13.768 44.956  19.911  1.00 30.10 ? 108 ASN E CB  1 
ATOM   6269 C  CG  . ASN E  1 107 ? 12.388 45.190  20.521  1.00 33.26 ? 108 ASN E CG  1 
ATOM   6270 O  OD1 . ASN E  1 107 ? 11.425 44.506  20.174  1.00 37.03 ? 108 ASN E OD1 1 
ATOM   6271 N  ND2 . ASN E  1 107 ? 12.285 46.163  21.423  1.00 31.95 ? 108 ASN E ND2 1 
ATOM   6272 N  N   . GLN E  1 108 ? 14.224 46.294  17.138  1.00 32.57 ? 109 GLN E N   1 
ATOM   6273 C  CA  . GLN E  1 108 ? 13.949 47.322  16.142  1.00 33.52 ? 109 GLN E CA  1 
ATOM   6274 C  C   . GLN E  1 108 ? 13.461 46.707  14.832  1.00 37.62 ? 109 GLN E C   1 
ATOM   6275 O  O   . GLN E  1 108 ? 12.467 47.155  14.248  1.00 34.27 ? 109 GLN E O   1 
ATOM   6276 C  CB  . GLN E  1 108 ? 15.205 48.153  15.903  1.00 35.80 ? 109 GLN E CB  1 
ATOM   6277 C  CG  . GLN E  1 108 ? 14.987 49.365  15.015  1.00 43.88 ? 109 GLN E CG  1 
ATOM   6278 C  CD  . GLN E  1 108 ? 16.288 50.105  14.710  1.00 60.24 ? 109 GLN E CD  1 
ATOM   6279 O  OE1 . GLN E  1 108 ? 17.232 50.089  15.508  1.00 65.30 ? 109 GLN E OE1 1 
ATOM   6280 N  NE2 . GLN E  1 108 ? 16.336 50.769  13.558  1.00 62.13 ? 109 GLN E NE2 1 
ATOM   6281 N  N   . SER E  1 109 ? 14.154 45.675  14.358  1.00 31.40 ? 110 SER E N   1 
ATOM   6282 C  CA  . SER E  1 109 ? 13.752 45.015  13.124  1.00 35.27 ? 110 SER E CA  1 
ATOM   6283 C  C   . SER E  1 109 ? 12.352 44.405  13.241  1.00 37.19 ? 110 SER E C   1 
ATOM   6284 O  O   . SER E  1 109 ? 11.544 44.499  12.306  1.00 34.94 ? 110 SER E O   1 
ATOM   6285 C  CB  . SER E  1 109 ? 14.792 43.955  12.769  1.00 29.86 ? 110 SER E CB  1 
ATOM   6286 O  OG  . SER E  1 109 ? 14.400 43.215  11.642  1.00 46.43 ? 110 SER E OG  1 
ATOM   6287 N  N   . LEU E  1 110 ? 12.042 43.775  14.383  1.00 36.68 ? 111 LEU E N   1 
ATOM   6288 C  CA  . LEU E  1 110 ? 10.708 43.202  14.570  1.00 34.87 ? 111 LEU E CA  1 
ATOM   6289 C  C   . LEU E  1 110 ? 9.634  44.283  14.564  1.00 36.01 ? 111 LEU E C   1 
ATOM   6290 O  O   . LEU E  1 110 ? 8.548  44.091  13.996  1.00 32.88 ? 111 LEU E O   1 
ATOM   6291 C  CB  . LEU E  1 110 ? 10.644 42.413  15.873  1.00 35.83 ? 111 LEU E CB  1 
ATOM   6292 C  CG  . LEU E  1 110 ? 11.410 41.099  15.895  1.00 40.94 ? 111 LEU E CG  1 
ATOM   6293 C  CD1 . LEU E  1 110 ? 11.350 40.514  17.289  1.00 43.21 ? 111 LEU E CD1 1 
ATOM   6294 C  CD2 . LEU E  1 110 ? 10.819 40.139  14.876  1.00 39.26 ? 111 LEU E CD2 1 
ATOM   6295 N  N   . LEU E  1 111 ? 9.914  45.426  15.202  1.00 32.67 ? 112 LEU E N   1 
ATOM   6296 C  CA  . LEU E  1 111 ? 8.952  46.523  15.198  1.00 34.62 ? 112 LEU E CA  1 
ATOM   6297 C  C   . LEU E  1 111 ? 8.728  47.069  13.785  1.00 34.50 ? 112 LEU E C   1 
ATOM   6298 O  O   . LEU E  1 111 ? 7.606  47.469  13.461  1.00 35.51 ? 112 LEU E O   1 
ATOM   6299 C  CB  . LEU E  1 111 ? 9.413  47.631  16.147  1.00 31.34 ? 112 LEU E CB  1 
ATOM   6300 C  CG  . LEU E  1 111 ? 9.401  47.269  17.637  1.00 36.65 ? 112 LEU E CG  1 
ATOM   6301 C  CD1 . LEU E  1 111 ? 10.156 48.308  18.469  1.00 31.00 ? 112 LEU E CD1 1 
ATOM   6302 C  CD2 . LEU E  1 111 ? 7.969  47.087  18.151  1.00 35.76 ? 112 LEU E CD2 1 
ATOM   6303 N  N   . GLU E  1 112 ? 9.765  47.078  12.931  1.00 32.55 ? 113 GLU E N   1 
ATOM   6304 C  CA  . GLU E  1 112 ? 9.573  47.493  11.538  1.00 36.61 ? 113 GLU E CA  1 
ATOM   6305 C  C   . GLU E  1 112 ? 8.745  46.466  10.763  1.00 39.80 ? 113 GLU E C   1 
ATOM   6306 O  O   . GLU E  1 112 ? 7.845  46.837  10.001  1.00 39.01 ? 113 GLU E O   1 
ATOM   6307 C  CB  . GLU E  1 112 ? 10.914 47.720  10.828  1.00 35.10 ? 113 GLU E CB  1 
ATOM   6308 C  CG  . GLU E  1 112 ? 11.606 49.054  11.113  1.00 45.83 ? 113 GLU E CG  1 
ATOM   6309 C  CD  . GLU E  1 112 ? 13.140 48.975  11.024  1.00 55.55 ? 113 GLU E CD  1 
ATOM   6310 O  OE1 . GLU E  1 112 ? 13.803 50.038  11.010  1.00 67.76 ? 113 GLU E OE1 1 
ATOM   6311 O  OE2 . GLU E  1 112 ? 13.692 47.857  10.945  1.00 58.72 ? 113 GLU E OE2 1 
ATOM   6312 N  N   . LEU E  1 113 ? 9.034  45.174  10.939  1.00 36.31 ? 114 LEU E N   1 
ATOM   6313 C  CA  . LEU E  1 113 ? 8.190  44.145  10.336  1.00 36.91 ? 114 LEU E CA  1 
ATOM   6314 C  C   . LEU E  1 113 ? 6.736  44.299  10.765  1.00 38.46 ? 114 LEU E C   1 
ATOM   6315 O  O   . LEU E  1 113 ? 5.823  44.094  9.957   1.00 34.50 ? 114 LEU E O   1 
ATOM   6316 C  CB  . LEU E  1 113 ? 8.718  42.758  10.696  1.00 37.24 ? 114 LEU E CB  1 
ATOM   6317 C  CG  . LEU E  1 113 ? 8.099  41.520  10.044  1.00 43.51 ? 114 LEU E CG  1 
ATOM   6318 C  CD1 . LEU E  1 113 ? 7.659  41.753  8.600   1.00 42.89 ? 114 LEU E CD1 1 
ATOM   6319 C  CD2 . LEU E  1 113 ? 9.098  40.373  10.123  1.00 45.20 ? 114 LEU E CD2 1 
ATOM   6320 N  N   . HIS E  1 114 ? 6.496  44.685  12.029  1.00 35.82 ? 115 HIS E N   1 
ATOM   6321 C  CA  . HIS E  1 114 ? 5.118  44.819  12.495  1.00 35.54 ? 115 HIS E CA  1 
ATOM   6322 C  C   . HIS E  1 114 ? 4.413  45.979  11.802  1.00 37.64 ? 115 HIS E C   1 
ATOM   6323 O  O   . HIS E  1 114 ? 3.239  45.868  11.438  1.00 36.03 ? 115 HIS E O   1 
ATOM   6324 C  CB  . HIS E  1 114 ? 5.082  44.997  14.009  1.00 35.14 ? 115 HIS E CB  1 
ATOM   6325 C  CG  . HIS E  1 114 ? 3.699  45.021  14.579  1.00 35.28 ? 115 HIS E CG  1 
ATOM   6326 N  ND1 . HIS E  1 114 ? 2.891  46.140  14.531  1.00 34.83 ? 115 HIS E ND1 1 
ATOM   6327 C  CD2 . HIS E  1 114 ? 2.978  44.062  15.206  1.00 35.29 ? 115 HIS E CD2 1 
ATOM   6328 C  CE1 . HIS E  1 114 ? 1.731  45.867  15.102  1.00 36.27 ? 115 HIS E CE1 1 
ATOM   6329 N  NE2 . HIS E  1 114 ? 1.760  44.614  15.525  1.00 36.58 ? 115 HIS E NE2 1 
ATOM   6330 N  N   . SER E  1 115 ? 5.123  47.091  11.597  1.00 38.45 ? 116 SER E N   1 
ATOM   6331 C  CA  . SER E  1 115 ? 4.558  48.243  10.897  1.00 40.70 ? 116 SER E CA  1 
ATOM   6332 C  C   . SER E  1 115 ? 4.266  47.927  9.425   1.00 39.51 ? 116 SER E C   1 
ATOM   6333 O  O   . SER E  1 115 ? 3.231  48.339  8.891   1.00 37.34 ? 116 SER E O   1 
ATOM   6334 C  CB  . SER E  1 115 ? 5.516  49.429  11.022  1.00 39.07 ? 116 SER E CB  1 
ATOM   6335 O  OG  . SER E  1 115 ? 5.112  50.490  10.180  1.00 51.94 ? 116 SER E OG  1 
ATOM   6336 N  N   . THR E  1 116 ? 5.175  47.216  8.753   1.00 37.36 ? 117 THR E N   1 
ATOM   6337 C  CA  . THR E  1 116 ? 4.917  46.720  7.402   1.00 40.26 ? 117 THR E CA  1 
ATOM   6338 C  C   . THR E  1 116 ? 3.635  45.896  7.351   1.00 43.49 ? 117 THR E C   1 
ATOM   6339 O  O   . THR E  1 116 ? 2.761  46.121  6.506   1.00 42.69 ? 117 THR E O   1 
ATOM   6340 C  CB  . THR E  1 116 ? 6.097  45.859  6.948   1.00 43.82 ? 117 THR E CB  1 
ATOM   6341 O  OG1 . THR E  1 116 ? 7.242  46.689  6.724   1.00 45.11 ? 117 THR E OG1 1 
ATOM   6342 C  CG2 . THR E  1 116 ? 5.754  45.065  5.675   1.00 43.95 ? 117 THR E CG2 1 
ATOM   6343 N  N   . ALA E  1 117 ? 3.523  44.913  8.249   1.00 39.51 ? 118 ALA E N   1 
ATOM   6344 C  CA  . ALA E  1 117 ? 2.344  44.059  8.290   1.00 36.46 ? 118 ALA E CA  1 
ATOM   6345 C  C   . ALA E  1 117 ? 1.080  44.866  8.577   1.00 40.71 ? 118 ALA E C   1 
ATOM   6346 O  O   . ALA E  1 117 ? 0.022  44.598  7.999   1.00 37.23 ? 118 ALA E O   1 
ATOM   6347 C  CB  . ALA E  1 117 ? 2.539  42.969  9.341   1.00 36.19 ? 118 ALA E CB  1 
ATOM   6348 N  N   . SER E  1 118 ? 1.170  45.857  9.468   1.00 37.28 ? 119 SER E N   1 
ATOM   6349 C  CA  . SER E  1 118 ? 0.024  46.726  9.724   1.00 43.10 ? 119 SER E CA  1 
ATOM   6350 C  C   . SER E  1 118 ? -0.348 47.534  8.487   1.00 42.50 ? 119 SER E C   1 
ATOM   6351 O  O   . SER E  1 118 ? -1.537 47.702  8.186   1.00 40.29 ? 119 SER E O   1 
ATOM   6352 C  CB  . SER E  1 118 ? 0.321  47.667  10.893  1.00 41.30 ? 119 SER E CB  1 
ATOM   6353 O  OG  . SER E  1 118 ? 0.127  47.003  12.116  1.00 45.52 ? 119 SER E OG  1 
ATOM   6354 N  N   . GLY E  1 119 ? 0.658  48.056  7.769   1.00 40.11 ? 120 GLY E N   1 
ATOM   6355 C  CA  . GLY E  1 119 ? 0.388  48.803  6.548   1.00 38.95 ? 120 GLY E CA  1 
ATOM   6356 C  C   . GLY E  1 119 ? -0.317 47.988  5.479   1.00 45.31 ? 120 GLY E C   1 
ATOM   6357 O  O   . GLY E  1 119 ? -1.153 48.515  4.741   1.00 51.48 ? 120 GLY E O   1 
ATOM   6358 N  N   . ASN E  1 120 ? -0.006 46.697  5.384   1.00 41.58 ? 121 ASN E N   1 
ATOM   6359 C  CA  . ASN E  1 120 ? -0.637 45.815  4.413   1.00 40.17 ? 121 ASN E CA  1 
ATOM   6360 C  C   . ASN E  1 120 ? -1.893 45.122  4.949   1.00 41.82 ? 121 ASN E C   1 
ATOM   6361 O  O   . ASN E  1 120 ? -2.414 44.218  4.287   1.00 39.23 ? 121 ASN E O   1 
ATOM   6362 C  CB  . ASN E  1 120 ? 0.375  44.769  3.942   1.00 42.28 ? 121 ASN E CB  1 
ATOM   6363 C  CG  . ASN E  1 120 ? 1.509  45.380  3.141   1.00 47.78 ? 121 ASN E CG  1 
ATOM   6364 O  OD1 . ASN E  1 120 ? 1.304  46.329  2.383   1.00 55.90 ? 121 ASN E OD1 1 
ATOM   6365 N  ND2 . ASN E  1 120 ? 2.707  44.833  3.296   1.00 51.00 ? 121 ASN E ND2 1 
ATOM   6366 N  N   . ASN E  1 121 ? -2.365 45.501  6.139   1.00 40.66 ? 122 ASN E N   1 
ATOM   6367 C  CA  . ASN E  1 121 ? -3.553 44.919  6.757   1.00 35.68 ? 122 ASN E CA  1 
ATOM   6368 C  C   . ASN E  1 121 ? -3.470 43.394  6.780   1.00 38.99 ? 122 ASN E C   1 
ATOM   6369 O  O   . ASN E  1 121 ? -4.302 42.676  6.216   1.00 37.14 ? 122 ASN E O   1 
ATOM   6370 C  CB  . ASN E  1 121 ? -4.820 45.409  6.051   1.00 40.96 ? 122 ASN E CB  1 
ATOM   6371 C  CG  . ASN E  1 121 ? -4.907 46.933  6.023   1.00 39.71 ? 122 ASN E CG  1 
ATOM   6372 O  OD1 . ASN E  1 121 ? -5.079 47.577  7.064   1.00 42.01 ? 122 ASN E OD1 1 
ATOM   6373 N  ND2 . ASN E  1 121 ? -4.755 47.514  4.834   1.00 45.54 ? 122 ASN E ND2 1 
ATOM   6374 N  N   . ASP E  1 122 ? -2.422 42.912  7.447   1.00 37.10 ? 123 ASP E N   1 
ATOM   6375 C  CA  . ASP E  1 122 ? -2.167 41.496  7.671   1.00 33.08 ? 123 ASP E CA  1 
ATOM   6376 C  C   . ASP E  1 122 ? -2.291 41.207  9.168   1.00 32.12 ? 123 ASP E C   1 
ATOM   6377 O  O   . ASP E  1 122 ? -1.283 41.183  9.883   1.00 33.40 ? 123 ASP E O   1 
ATOM   6378 C  CB  . ASP E  1 122 ? -0.780 41.130  7.143   1.00 33.92 ? 123 ASP E CB  1 
ATOM   6379 C  CG  . ASP E  1 122 ? -0.565 39.629  7.034   1.00 38.80 ? 123 ASP E CG  1 
ATOM   6380 O  OD1 . ASP E  1 122 ? -1.228 38.866  7.776   1.00 40.71 ? 123 ASP E OD1 1 
ATOM   6381 O  OD2 . ASP E  1 122 ? 0.288  39.212  6.211   1.00 39.72 ? 123 ASP E OD2 1 
ATOM   6382 N  N   . PRO E  1 123 ? -3.505 40.996  9.681   1.00 30.52 ? 124 PRO E N   1 
ATOM   6383 C  CA  . PRO E  1 123 ? -3.662 40.767  11.128  1.00 34.42 ? 124 PRO E CA  1 
ATOM   6384 C  C   . PRO E  1 123 ? -3.122 39.434  11.603  1.00 33.91 ? 124 PRO E C   1 
ATOM   6385 O  O   . PRO E  1 123 ? -2.848 39.291  12.799  1.00 34.90 ? 124 PRO E O   1 
ATOM   6386 C  CB  . PRO E  1 123 ? -5.181 40.852  11.343  1.00 32.90 ? 124 PRO E CB  1 
ATOM   6387 C  CG  . PRO E  1 123 ? -5.756 40.502  10.039  1.00 33.52 ? 124 PRO E CG  1 
ATOM   6388 C  CD  . PRO E  1 123 ? -4.797 41.034  8.986   1.00 32.73 ? 124 PRO E CD  1 
ATOM   6389 N  N   . HIS E  1 124 ? -2.955 38.450  10.721  1.00 34.30 ? 125 HIS E N   1 
ATOM   6390 C  CA  . HIS E  1 124 ? -2.323 37.212  11.157  1.00 33.58 ? 125 HIS E CA  1 
ATOM   6391 C  C   . HIS E  1 124 ? -0.845 37.432  11.466  1.00 36.82 ? 125 HIS E C   1 
ATOM   6392 O  O   . HIS E  1 124 ? -0.314 36.893  12.448  1.00 34.49 ? 125 HIS E O   1 
ATOM   6393 C  CB  . HIS E  1 124 ? -2.503 36.130  10.097  1.00 31.89 ? 125 HIS E CB  1 
ATOM   6394 C  CG  . HIS E  1 124 ? -2.261 34.749  10.614  1.00 38.98 ? 125 HIS E CG  1 
ATOM   6395 N  ND1 . HIS E  1 124 ? -1.068 34.081  10.428  1.00 34.04 ? 125 HIS E ND1 1 
ATOM   6396 C  CD2 . HIS E  1 124 ? -3.053 33.918  11.332  1.00 41.41 ? 125 HIS E CD2 1 
ATOM   6397 C  CE1 . HIS E  1 124 ? -1.144 32.889  10.994  1.00 38.98 ? 125 HIS E CE1 1 
ATOM   6398 N  NE2 . HIS E  1 124 ? -2.336 32.766  11.552  1.00 41.21 ? 125 HIS E NE2 1 
ATOM   6399 N  N   . LEU E  1 125 ? -0.168 38.240  10.652  1.00 32.68 ? 126 LEU E N   1 
ATOM   6400 C  CA  . LEU E  1 125 ? 1.250  38.479  10.873  1.00 36.18 ? 126 LEU E CA  1 
ATOM   6401 C  C   . LEU E  1 125 ? 1.472  39.345  12.114  1.00 36.32 ? 126 LEU E C   1 
ATOM   6402 O  O   . LEU E  1 125 ? 2.337  39.035  12.942  1.00 32.94 ? 126 LEU E O   1 
ATOM   6403 C  CB  . LEU E  1 125 ? 1.870  39.111  9.619   1.00 33.66 ? 126 LEU E CB  1 
ATOM   6404 C  CG  . LEU E  1 125 ? 3.367  39.411  9.698   1.00 39.03 ? 126 LEU E CG  1 
ATOM   6405 C  CD1 . LEU E  1 125 ? 4.169  38.229  10.269  1.00 31.47 ? 126 LEU E CD1 1 
ATOM   6406 C  CD2 . LEU E  1 125 ? 3.895  39.824  8.327   1.00 30.15 ? 126 LEU E CD2 1 
ATOM   6407 N  N   . THR E  1 126 ? 0.689  40.425  12.276  1.00 31.67 ? 127 THR E N   1 
ATOM   6408 C  CA  . THR E  1 126 ? 0.869  41.274  13.454  1.00 36.12 ? 127 THR E CA  1 
ATOM   6409 C  C   . THR E  1 126 ? 0.637  40.473  14.732  1.00 38.81 ? 127 THR E C   1 
ATOM   6410 O  O   . THR E  1 126 ? 1.325  40.674  15.741  1.00 34.54 ? 127 THR E O   1 
ATOM   6411 C  CB  . THR E  1 126 ? -0.061 42.505  13.418  1.00 38.56 ? 127 THR E CB  1 
ATOM   6412 O  OG1 . THR E  1 126 ? -1.429 42.107  13.268  1.00 35.41 ? 127 THR E OG1 1 
ATOM   6413 C  CG2 . THR E  1 126 ? 0.313  43.475  12.278  1.00 36.04 ? 127 THR E CG2 1 
ATOM   6414 N  N   . LYS E  1 127 ? -0.317 39.544  14.696  1.00 36.53 ? 128 LYS E N   1 
ATOM   6415 C  CA  . LYS E  1 127 ? -0.602 38.717  15.862  1.00 38.56 ? 128 LYS E CA  1 
ATOM   6416 C  C   . LYS E  1 127 ? 0.555  37.765  16.160  1.00 41.15 ? 128 LYS E C   1 
ATOM   6417 O  O   . LYS E  1 127 ? 0.973  37.637  17.315  1.00 37.57 ? 128 LYS E O   1 
ATOM   6418 C  CB  . LYS E  1 127 ? -1.906 37.942  15.642  1.00 36.99 ? 128 LYS E CB  1 
ATOM   6419 C  CG  . LYS E  1 127 ? -2.229 36.930  16.731  1.00 43.65 ? 128 LYS E CG  1 
ATOM   6420 C  CD  . LYS E  1 127 ? -2.917 35.704  16.163  1.00 47.36 ? 128 LYS E CD  1 
ATOM   6421 C  CE  . LYS E  1 127 ? -2.930 34.563  17.190  1.00 58.24 ? 128 LYS E CE  1 
ATOM   6422 N  NZ  . LYS E  1 127 ? -3.359 35.010  18.554  1.00 61.61 ? 128 LYS E NZ  1 
ATOM   6423 N  N   . LEU E  1 128 ? 1.081  37.091  15.129  1.00 37.95 ? 129 LEU E N   1 
ATOM   6424 C  CA  . LEU E  1 128 ? 2.287  36.286  15.299  1.00 37.72 ? 129 LEU E CA  1 
ATOM   6425 C  C   . LEU E  1 128 ? 3.406  37.097  15.938  1.00 40.15 ? 129 LEU E C   1 
ATOM   6426 O  O   . LEU E  1 128 ? 4.029  36.657  16.913  1.00 37.40 ? 129 LEU E O   1 
ATOM   6427 C  CB  . LEU E  1 128 ? 2.761  35.723  13.956  1.00 37.02 ? 129 LEU E CB  1 
ATOM   6428 C  CG  . LEU E  1 128 ? 4.169  35.120  14.086  1.00 38.61 ? 129 LEU E CG  1 
ATOM   6429 C  CD1 . LEU E  1 128 ? 4.058  33.746  14.703  1.00 35.32 ? 129 LEU E CD1 1 
ATOM   6430 C  CD2 . LEU E  1 128 ? 4.949  35.068  12.775  1.00 35.10 ? 129 LEU E CD2 1 
ATOM   6431 N  N   . LEU E  1 129 ? 3.683  38.288  15.396  1.00 35.40 ? 130 LEU E N   1 
ATOM   6432 C  CA  . LEU E  1 129 ? 4.785  39.080  15.938  1.00 38.98 ? 130 LEU E CA  1 
ATOM   6433 C  C   . LEU E  1 129 ? 4.523  39.469  17.393  1.00 40.20 ? 130 LEU E C   1 
ATOM   6434 O  O   . LEU E  1 129 ? 5.419  39.368  18.239  1.00 41.39 ? 130 LEU E O   1 
ATOM   6435 C  CB  . LEU E  1 129 ? 5.038  40.315  15.065  1.00 33.81 ? 130 LEU E CB  1 
ATOM   6436 C  CG  . LEU E  1 129 ? 5.548  40.008  13.651  1.00 37.74 ? 130 LEU E CG  1 
ATOM   6437 C  CD1 . LEU E  1 129 ? 5.453  41.240  12.738  1.00 34.32 ? 130 LEU E CD1 1 
ATOM   6438 C  CD2 . LEU E  1 129 ? 6.979  39.475  13.666  1.00 36.14 ? 130 LEU E CD2 1 
ATOM   6439 N  N   . GLU E  1 130 ? 3.292  39.871  17.714  1.00 40.23 ? 131 GLU E N   1 
ATOM   6440 C  CA  . GLU E  1 130 ? 2.975  40.281  19.082  1.00 44.86 ? 131 GLU E CA  1 
ATOM   6441 C  C   . GLU E  1 130 ? 3.106  39.116  20.061  1.00 47.46 ? 131 GLU E C   1 
ATOM   6442 O  O   . GLU E  1 130 ? 3.756  39.238  21.106  1.00 50.17 ? 131 GLU E O   1 
ATOM   6443 C  CB  . GLU E  1 130 ? 1.562  40.870  19.139  1.00 40.36 ? 131 GLU E CB  1 
ATOM   6444 C  CG  . GLU E  1 130 ? 1.457  42.278  18.578  1.00 39.77 ? 131 GLU E CG  1 
ATOM   6445 C  CD  . GLU E  1 130 ? 0.021  42.690  18.280  1.00 47.65 ? 131 GLU E CD  1 
ATOM   6446 O  OE1 . GLU E  1 130 ? -0.910 42.088  18.869  1.00 52.03 ? 131 GLU E OE1 1 
ATOM   6447 O  OE2 . GLU E  1 130 ? -0.172 43.608  17.446  1.00 42.76 ? 131 GLU E OE2 1 
ATOM   6448 N  N   . ASP E  1 131 ? 2.502  37.970  19.732  1.00 43.18 ? 132 ASP E N   1 
ATOM   6449 C  CA  . ASP E  1 131 ? 2.411  36.863  20.676  1.00 46.87 ? 132 ASP E CA  1 
ATOM   6450 C  C   . ASP E  1 131 ? 3.715  36.077  20.799  1.00 51.23 ? 132 ASP E C   1 
ATOM   6451 O  O   . ASP E  1 131 ? 3.999  35.540  21.874  1.00 53.83 ? 132 ASP E O   1 
ATOM   6452 C  CB  . ASP E  1 131 ? 1.272  35.930  20.261  1.00 52.90 ? 132 ASP E CB  1 
ATOM   6453 C  CG  . ASP E  1 131 ? -0.105 36.524  20.543  1.00 63.84 ? 132 ASP E CG  1 
ATOM   6454 O  OD1 . ASP E  1 131 ? -0.191 37.755  20.776  1.00 67.52 ? 132 ASP E OD1 1 
ATOM   6455 O  OD2 . ASP E  1 131 ? -1.108 35.770  20.492  1.00 62.46 ? 132 ASP E OD2 1 
ATOM   6456 N  N   . GLU E  1 132 ? 4.522  36.002  19.734  1.00 49.74 ? 133 GLU E N   1 
ATOM   6457 C  CA  . GLU E  1 132 ? 5.654  35.080  19.683  1.00 48.37 ? 133 GLU E CA  1 
ATOM   6458 C  C   . GLU E  1 132 ? 7.023  35.745  19.741  1.00 46.53 ? 133 GLU E C   1 
ATOM   6459 O  O   . GLU E  1 132 ? 8.010  35.048  19.991  1.00 50.78 ? 133 GLU E O   1 
ATOM   6460 C  CB  . GLU E  1 132 ? 5.599  34.228  18.398  1.00 50.23 ? 133 GLU E CB  1 
ATOM   6461 C  CG  . GLU E  1 132 ? 4.426  33.229  18.290  1.00 54.87 ? 133 GLU E CG  1 
ATOM   6462 C  CD  . GLU E  1 132 ? 4.263  32.336  19.526  1.00 66.72 ? 133 GLU E CD  1 
ATOM   6463 O  OE1 . GLU E  1 132 ? 3.109  32.154  19.979  1.00 69.42 ? 133 GLU E OE1 1 
ATOM   6464 O  OE2 . GLU E  1 132 ? 5.282  31.804  20.032  1.00 69.56 ? 133 GLU E OE2 1 
ATOM   6465 N  N   . TYR E  1 133 ? 7.119  37.058  19.524  1.00 39.58 ? 134 TYR E N   1 
ATOM   6466 C  CA  . TYR E  1 133 ? 8.425  37.697  19.366  1.00 38.50 ? 134 TYR E CA  1 
ATOM   6467 C  C   . TYR E  1 133 ? 8.595  38.967  20.199  1.00 40.26 ? 134 TYR E C   1 
ATOM   6468 O  O   . TYR E  1 133 ? 9.580  39.096  20.928  1.00 43.61 ? 134 TYR E O   1 
ATOM   6469 C  CB  . TYR E  1 133 ? 8.667  38.014  17.890  1.00 40.38 ? 134 TYR E CB  1 
ATOM   6470 C  CG  . TYR E  1 133 ? 8.855  36.776  17.061  1.00 40.33 ? 134 TYR E CG  1 
ATOM   6471 C  CD1 . TYR E  1 133 ? 10.107 36.209  16.930  1.00 38.57 ? 134 TYR E CD1 1 
ATOM   6472 C  CD2 . TYR E  1 133 ? 7.771  36.146  16.444  1.00 37.03 ? 134 TYR E CD2 1 
ATOM   6473 C  CE1 . TYR E  1 133 ? 10.295 35.057  16.203  1.00 39.94 ? 134 TYR E CE1 1 
ATOM   6474 C  CE2 . TYR E  1 133 ? 7.948  34.998  15.695  1.00 36.59 ? 134 TYR E CE2 1 
ATOM   6475 C  CZ  . TYR E  1 133 ? 9.223  34.457  15.582  1.00 39.01 ? 134 TYR E CZ  1 
ATOM   6476 O  OH  . TYR E  1 133 ? 9.452  33.322  14.853  1.00 33.79 ? 134 TYR E OH  1 
ATOM   6477 N  N   . LEU E  1 134 ? 7.656  39.912  20.095  1.00 36.68 ? 135 LEU E N   1 
ATOM   6478 C  CA  . LEU E  1 134 ? 7.839  41.210  20.735  1.00 39.41 ? 135 LEU E CA  1 
ATOM   6479 C  C   . LEU E  1 134 ? 7.876  41.096  22.254  1.00 37.71 ? 135 LEU E C   1 
ATOM   6480 O  O   . LEU E  1 134 ? 8.706  41.738  22.905  1.00 35.78 ? 135 LEU E O   1 
ATOM   6481 C  CB  . LEU E  1 134 ? 6.734  42.167  20.306  1.00 34.62 ? 135 LEU E CB  1 
ATOM   6482 C  CG  . LEU E  1 134 ? 6.782  42.556  18.835  1.00 37.56 ? 135 LEU E CG  1 
ATOM   6483 C  CD1 . LEU E  1 134 ? 5.689  43.582  18.555  1.00 38.98 ? 135 LEU E CD1 1 
ATOM   6484 C  CD2 . LEU E  1 134 ? 8.170  43.090  18.451  1.00 37.20 ? 135 LEU E CD2 1 
ATOM   6485 N  N   . GLU E  1 135 ? 6.986  40.289  22.837  1.00 39.54 ? 136 GLU E N   1 
ATOM   6486 C  CA  . GLU E  1 135 ? 6.988  40.122  24.285  1.00 43.41 ? 136 GLU E CA  1 
ATOM   6487 C  C   . GLU E  1 135 ? 8.304  39.524  24.761  1.00 43.92 ? 136 GLU E C   1 
ATOM   6488 O  O   . GLU E  1 135 ? 8.835  39.910  25.808  1.00 42.31 ? 136 GLU E O   1 
ATOM   6489 C  CB  . GLU E  1 135 ? 5.817  39.241  24.717  1.00 45.19 ? 136 GLU E CB  1 
ATOM   6490 C  CG  . GLU E  1 135 ? 5.567  39.289  26.213  1.00 57.71 ? 136 GLU E CG  1 
ATOM   6491 C  CD  . GLU E  1 135 ? 4.130  38.953  26.584  1.00 70.19 ? 136 GLU E CD  1 
ATOM   6492 O  OE1 . GLU E  1 135 ? 3.228  39.340  25.812  1.00 70.00 ? 136 GLU E OE1 1 
ATOM   6493 O  OE2 . GLU E  1 135 ? 3.900  38.338  27.655  1.00 65.65 ? 136 GLU E OE2 1 
ATOM   6494 N  N   . GLU E  1 136 ? 8.857  38.603  23.980  1.00 43.18 ? 137 GLU E N   1 
ATOM   6495 C  CA  . GLU E  1 136 ? 10.074 37.907  24.375  1.00 50.30 ? 137 GLU E CA  1 
ATOM   6496 C  C   . GLU E  1 136 ? 11.300 38.796  24.219  1.00 42.58 ? 137 GLU E C   1 
ATOM   6497 O  O   . GLU E  1 136 ? 12.236 38.688  25.017  1.00 38.25 ? 137 GLU E O   1 
ATOM   6498 C  CB  . GLU E  1 136 ? 10.218 36.616  23.558  1.00 49.82 ? 137 GLU E CB  1 
ATOM   6499 C  CG  . GLU E  1 136 ? 9.080  35.572  23.791  1.00 59.95 ? 137 GLU E CG  1 
ATOM   6500 C  CD  . GLU E  1 136 ? 7.659  36.073  23.394  1.00 64.51 ? 137 GLU E CD  1 
ATOM   6501 O  OE1 . GLU E  1 136 ? 7.504  36.686  22.313  1.00 60.14 ? 137 GLU E OE1 1 
ATOM   6502 O  OE2 . GLU E  1 136 ? 6.688  35.846  24.157  1.00 67.77 ? 137 GLU E OE2 1 
ATOM   6503 N  N   . GLN E  1 137 ? 11.305 39.690  23.221  1.00 38.51 ? 138 GLN E N   1 
ATOM   6504 C  CA  . GLN E  1 137 ? 12.388 40.662  23.107  1.00 39.84 ? 138 GLN E CA  1 
ATOM   6505 C  C   . GLN E  1 137 ? 12.419 41.597  24.310  1.00 36.22 ? 138 GLN E C   1 
ATOM   6506 O  O   . GLN E  1 137 ? 13.486 41.868  24.865  1.00 36.54 ? 138 GLN E O   1 
ATOM   6507 C  CB  . GLN E  1 137 ? 12.239 41.480  21.823  1.00 40.81 ? 138 GLN E CB  1 
ATOM   6508 C  CG  . GLN E  1 137 ? 12.687 40.779  20.571  1.00 40.52 ? 138 GLN E CG  1 
ATOM   6509 C  CD  . GLN E  1 137 ? 14.035 40.104  20.722  1.00 44.81 ? 138 GLN E CD  1 
ATOM   6510 O  OE1 . GLN E  1 137 ? 15.072 40.761  20.891  1.00 41.78 ? 138 GLN E OE1 1 
ATOM   6511 N  NE2 . GLN E  1 137 ? 14.027 38.780  20.677  1.00 45.76 ? 138 GLN E NE2 1 
ATOM   6512 N  N   . VAL E  1 138 ? 11.250 42.094  24.728  1.00 37.89 ? 139 VAL E N   1 
ATOM   6513 C  CA  . VAL E  1 138 ? 11.182 43.049  25.832  1.00 35.80 ? 139 VAL E CA  1 
ATOM   6514 C  C   . VAL E  1 138 ? 11.649 42.405  27.132  1.00 38.80 ? 139 VAL E C   1 
ATOM   6515 O  O   . VAL E  1 138 ? 12.384 43.019  27.916  1.00 34.01 ? 139 VAL E O   1 
ATOM   6516 C  CB  . VAL E  1 138 ? 9.752  43.611  25.957  1.00 37.96 ? 139 VAL E CB  1 
ATOM   6517 C  CG1 . VAL E  1 138 ? 9.584  44.351  27.259  1.00 37.48 ? 139 VAL E CG1 1 
ATOM   6518 C  CG2 . VAL E  1 138 ? 9.426  44.523  24.774  1.00 36.12 ? 139 VAL E CG2 1 
ATOM   6519 N  N   . ASP E  1 139 ? 11.248 41.148  27.373  1.00 40.44 ? 140 ASP E N   1 
ATOM   6520 C  CA  . ASP E  1 139 ? 11.663 40.449  28.591  1.00 40.92 ? 140 ASP E CA  1 
ATOM   6521 C  C   . ASP E  1 139 ? 13.169 40.209  28.612  1.00 37.60 ? 140 ASP E C   1 
ATOM   6522 O  O   . ASP E  1 139 ? 13.822 40.385  29.648  1.00 34.57 ? 140 ASP E O   1 
ATOM   6523 C  CB  . ASP E  1 139 ? 10.917 39.114  28.727  1.00 41.34 ? 140 ASP E CB  1 
ATOM   6524 C  CG  . ASP E  1 139 ? 9.438  39.296  29.099  1.00 53.22 ? 140 ASP E CG  1 
ATOM   6525 O  OD1 . ASP E  1 139 ? 9.058  40.408  29.536  1.00 56.39 ? 140 ASP E OD1 1 
ATOM   6526 O  OD2 . ASP E  1 139 ? 8.654  38.325  28.957  1.00 59.49 ? 140 ASP E OD2 1 
ATOM   6527 N  N   . SER E  1 140 ? 13.737 39.807  27.485  1.00 32.66 ? 141 SER E N   1 
ATOM   6528 C  CA  . SER E  1 140 ? 15.159 39.528  27.470  1.00 36.50 ? 141 SER E CA  1 
ATOM   6529 C  C   . SER E  1 140 ? 15.979 40.816  27.469  1.00 35.63 ? 141 SER E C   1 
ATOM   6530 O  O   . SER E  1 140 ? 17.068 40.846  28.048  1.00 33.51 ? 141 SER E O   1 
ATOM   6531 C  CB  . SER E  1 140 ? 15.492 38.627  26.279  1.00 41.38 ? 141 SER E CB  1 
ATOM   6532 O  OG  . SER E  1 140 ? 15.930 39.386  25.182  1.00 48.75 ? 141 SER E OG  1 
ATOM   6533 N  N   . ILE E  1 141 ? 15.462 41.900  26.880  1.00 37.39 ? 142 ILE E N   1 
ATOM   6534 C  CA  . ILE E  1 141 ? 16.139 43.191  27.014  1.00 33.53 ? 142 ILE E CA  1 
ATOM   6535 C  C   . ILE E  1 141 ? 16.173 43.611  28.479  1.00 33.83 ? 142 ILE E C   1 
ATOM   6536 O  O   . ILE E  1 141 ? 17.194 44.097  28.982  1.00 32.85 ? 142 ILE E O   1 
ATOM   6537 C  CB  . ILE E  1 141 ? 15.458 44.257  26.129  1.00 32.37 ? 142 ILE E CB  1 
ATOM   6538 C  CG1 . ILE E  1 141 ? 15.786 44.023  24.656  1.00 36.24 ? 142 ILE E CG1 1 
ATOM   6539 C  CG2 . ILE E  1 141 ? 15.927 45.667  26.499  1.00 30.68 ? 142 ILE E CG2 1 
ATOM   6540 C  CD1 . ILE E  1 141 ? 14.913 44.827  23.693  1.00 34.24 ? 142 ILE E CD1 1 
ATOM   6541 N  N   . LYS E  1 142 ? 15.061 43.410  29.191  1.00 32.90 ? 143 LYS E N   1 
ATOM   6542 C  CA  . LYS E  1 142 ? 14.980 43.803  30.591  1.00 34.10 ? 143 LYS E CA  1 
ATOM   6543 C  C   . LYS E  1 142 ? 15.862 42.918  31.466  1.00 33.57 ? 143 LYS E C   1 
ATOM   6544 O  O   . LYS E  1 142 ? 16.492 43.405  32.409  1.00 32.26 ? 143 LYS E O   1 
ATOM   6545 C  CB  . LYS E  1 142 ? 13.520 43.752  31.058  1.00 35.49 ? 143 LYS E CB  1 
ATOM   6546 C  CG  . LYS E  1 142 ? 13.331 43.766  32.575  1.00 28.39 ? 143 LYS E CG  1 
ATOM   6547 C  CD  . LYS E  1 142 ? 13.756 45.103  33.117  1.00 36.85 ? 143 LYS E CD  1 
ATOM   6548 C  CE  . LYS E  1 142 ? 13.019 45.447  34.406  1.00 40.10 ? 143 LYS E CE  1 
ATOM   6549 N  NZ  . LYS E  1 142 ? 13.471 44.627  35.573  1.00 37.57 ? 143 LYS E NZ  1 
ATOM   6550 N  N   . LYS E  1 143 ? 15.910 41.617  31.171  1.00 32.00 ? 144 LYS E N   1 
ATOM   6551 C  CA  . LYS E  1 143 ? 16.769 40.701  31.913  1.00 34.85 ? 144 LYS E CA  1 
ATOM   6552 C  C   . LYS E  1 143 ? 18.245 41.072  31.767  1.00 35.94 ? 144 LYS E C   1 
ATOM   6553 O  O   . LYS E  1 143 ? 18.993 41.047  32.750  1.00 35.00 ? 144 LYS E O   1 
ATOM   6554 C  CB  . LYS E  1 143 ? 16.513 39.261  31.445  1.00 35.24 ? 144 LYS E CB  1 
ATOM   6555 C  CG  . LYS E  1 143 ? 17.551 38.222  31.905  1.00 42.92 ? 144 LYS E CG  1 
ATOM   6556 C  CD  . LYS E  1 143 ? 17.550 38.057  33.442  1.00 50.55 ? 144 LYS E CD  1 
ATOM   6557 C  CE  . LYS E  1 143 ? 17.701 36.585  33.907  1.00 58.43 ? 144 LYS E CE  1 
ATOM   6558 N  NZ  . LYS E  1 143 ? 19.118 36.057  33.938  1.00 61.94 ? 144 LYS E NZ  1 
ATOM   6559 N  N   . ILE E  1 144 ? 18.681 41.436  30.556  1.00 33.18 ? 145 ILE E N   1 
ATOM   6560 C  CA  . ILE E  1 144 ? 20.088 41.784  30.359  1.00 33.76 ? 145 ILE E CA  1 
ATOM   6561 C  C   . ILE E  1 144 ? 20.411 43.093  31.057  1.00 32.52 ? 145 ILE E C   1 
ATOM   6562 O  O   . ILE E  1 144 ? 21.489 43.249  31.644  1.00 32.57 ? 145 ILE E O   1 
ATOM   6563 C  CB  . ILE E  1 144 ? 20.433 41.856  28.861  1.00 32.82 ? 145 ILE E CB  1 
ATOM   6564 C  CG1 . ILE E  1 144 ? 20.263 40.482  28.209  1.00 36.67 ? 145 ILE E CG1 1 
ATOM   6565 C  CG2 . ILE E  1 144 ? 21.859 42.373  28.677  1.00 31.40 ? 145 ILE E CG2 1 
ATOM   6566 C  CD1 . ILE E  1 144 ? 20.144 40.532  26.688  1.00 36.90 ? 145 ILE E CD1 1 
ATOM   6567 N  N   . GLY E  1 145 ? 19.489 44.059  30.996  1.00 31.79 ? 146 GLY E N   1 
ATOM   6568 C  CA  . GLY E  1 145 ? 19.673 45.301  31.736  1.00 31.40 ? 146 GLY E CA  1 
ATOM   6569 C  C   . GLY E  1 145 ? 19.850 45.076  33.228  1.00 35.77 ? 146 GLY E C   1 
ATOM   6570 O  O   . GLY E  1 145 ? 20.771 45.624  33.842  1.00 35.74 ? 146 GLY E O   1 
ATOM   6571 N  N   . ASP E  1 146 ? 18.970 44.261  33.833  1.00 34.10 ? 147 ASP E N   1 
ATOM   6572 C  CA  . ASP E  1 146 ? 19.130 43.896  35.243  1.00 35.55 ? 147 ASP E CA  1 
ATOM   6573 C  C   . ASP E  1 146 ? 20.508 43.308  35.510  1.00 31.86 ? 147 ASP E C   1 
ATOM   6574 O  O   . ASP E  1 146 ? 21.153 43.654  36.501  1.00 30.49 ? 147 ASP E O   1 
ATOM   6575 C  CB  . ASP E  1 146 ? 18.075 42.873  35.705  1.00 39.47 ? 147 ASP E CB  1 
ATOM   6576 C  CG  . ASP E  1 146 ? 16.647 43.408  35.701  1.00 46.56 ? 147 ASP E CG  1 
ATOM   6577 O  OD1 . ASP E  1 146 ? 16.450 44.646  35.715  1.00 44.58 ? 147 ASP E OD1 1 
ATOM   6578 O  OD2 . ASP E  1 146 ? 15.709 42.567  35.748  1.00 49.10 ? 147 ASP E OD2 1 
ATOM   6579 N  N   . MET E  1 147 ? 20.953 42.378  34.654  1.00 32.81 ? 148 MET E N   1 
ATOM   6580 C  CA  . MET E  1 147 ? 22.227 41.694  34.891  1.00 34.77 ? 148 MET E CA  1 
ATOM   6581 C  C   . MET E  1 147 ? 23.401 42.657  34.824  1.00 31.98 ? 148 MET E C   1 
ATOM   6582 O  O   . MET E  1 147 ? 24.351 42.538  35.602  1.00 35.24 ? 148 MET E O   1 
ATOM   6583 C  CB  . MET E  1 147 ? 22.419 40.558  33.886  1.00 33.73 ? 148 MET E CB  1 
ATOM   6584 C  CG  . MET E  1 147 ? 21.387 39.421  34.009  1.00 36.99 ? 148 MET E CG  1 
ATOM   6585 S  SD  . MET E  1 147 ? 21.372 38.298  32.577  1.00 44.53 ? 148 MET E SD  1 
ATOM   6586 C  CE  . MET E  1 147 ? 23.080 37.766  32.529  1.00 40.81 ? 148 MET E CE  1 
ATOM   6587 N  N   . ILE E  1 148 ? 23.360 43.611  33.896  1.00 29.34 ? 149 ILE E N   1 
ATOM   6588 C  CA  . ILE E  1 148 ? 24.419 44.612  33.802  1.00 30.08 ? 149 ILE E CA  1 
ATOM   6589 C  C   . ILE E  1 148 ? 24.494 45.419  35.095  1.00 35.80 ? 149 ILE E C   1 
ATOM   6590 O  O   . ILE E  1 148 ? 25.576 45.629  35.660  1.00 32.23 ? 149 ILE E O   1 
ATOM   6591 C  CB  . ILE E  1 148 ? 24.186 45.511  32.573  1.00 30.84 ? 149 ILE E CB  1 
ATOM   6592 C  CG1 . ILE E  1 148 ? 24.407 44.703  31.286  1.00 27.71 ? 149 ILE E CG1 1 
ATOM   6593 C  CG2 . ILE E  1 148 ? 25.094 46.713  32.609  1.00 33.49 ? 149 ILE E CG2 1 
ATOM   6594 C  CD1 . ILE E  1 148 ? 24.312 45.524  30.042  1.00 30.17 ? 149 ILE E CD1 1 
ATOM   6595 N  N   . THR E  1 149 ? 23.334 45.835  35.609  1.00 30.65 ? 150 THR E N   1 
ATOM   6596 C  CA  . THR E  1 149 ? 23.296 46.588  36.855  1.00 31.39 ? 150 THR E CA  1 
ATOM   6597 C  C   . THR E  1 149 ? 23.843 45.773  38.025  1.00 31.17 ? 150 THR E C   1 
ATOM   6598 O  O   . THR E  1 149 ? 24.609 46.293  38.847  1.00 31.33 ? 150 THR E O   1 
ATOM   6599 C  CB  . THR E  1 149 ? 21.861 47.031  37.137  1.00 33.55 ? 150 THR E CB  1 
ATOM   6600 O  OG1 . THR E  1 149 ? 21.366 47.752  36.004  1.00 32.51 ? 150 THR E OG1 1 
ATOM   6601 C  CG2 . THR E  1 149 ? 21.796 47.930  38.380  1.00 33.88 ? 150 THR E CG2 1 
ATOM   6602 N  N   . LYS E  1 150 ? 23.448 44.498  38.130  1.00 30.64 ? 151 LYS E N   1 
ATOM   6603 C  CA  . LYS E  1 150 ? 23.928 43.657  39.231  1.00 32.89 ? 151 LYS E CA  1 
ATOM   6604 C  C   . LYS E  1 150 ? 25.430 43.415  39.123  1.00 32.89 ? 151 LYS E C   1 
ATOM   6605 O  O   . LYS E  1 150 ? 26.148 43.453  40.129  1.00 33.90 ? 151 LYS E O   1 
ATOM   6606 C  CB  . LYS E  1 150 ? 23.195 42.313  39.247  1.00 32.37 ? 151 LYS E CB  1 
ATOM   6607 C  CG  . LYS E  1 150 ? 21.721 42.341  39.613  1.00 37.52 ? 151 LYS E CG  1 
ATOM   6608 C  CD  . LYS E  1 150 ? 21.225 40.911  39.831  1.00 40.08 ? 151 LYS E CD  1 
ATOM   6609 C  CE  . LYS E  1 150 ? 19.748 40.771  39.549  1.00 44.73 ? 151 LYS E CE  1 
ATOM   6610 N  NZ  . LYS E  1 150 ? 19.246 39.421  39.954  1.00 57.03 ? 151 LYS E NZ  1 
ATOM   6611 N  N   . LEU E  1 151 ? 25.919 43.144  37.911  1.00 31.99 ? 152 LEU E N   1 
ATOM   6612 C  CA  . LEU E  1 151 ? 27.341 42.864  37.734  1.00 33.43 ? 152 LEU E CA  1 
ATOM   6613 C  C   . LEU E  1 151 ? 28.185 44.092  38.047  1.00 34.66 ? 152 LEU E C   1 
ATOM   6614 O  O   . LEU E  1 151 ? 29.273 43.966  38.620  1.00 33.34 ? 152 LEU E O   1 
ATOM   6615 C  CB  . LEU E  1 151 ? 27.607 42.367  36.307  1.00 33.24 ? 152 LEU E CB  1 
ATOM   6616 C  CG  . LEU E  1 151 ? 29.049 42.140  35.828  1.00 33.56 ? 152 LEU E CG  1 
ATOM   6617 C  CD1 . LEU E  1 151 ? 29.852 41.328  36.835  1.00 31.62 ? 152 LEU E CD1 1 
ATOM   6618 C  CD2 . LEU E  1 151 ? 29.026 41.432  34.481  1.00 29.11 ? 152 LEU E CD2 1 
ATOM   6619 N  N   . LYS E  1 152 ? 27.696 45.286  37.678  1.00 32.57 ? 153 LYS E N   1 
ATOM   6620 C  CA  . LYS E  1 152 ? 28.395 46.531  37.996  1.00 35.68 ? 153 LYS E CA  1 
ATOM   6621 C  C   . LYS E  1 152 ? 28.429 46.796  39.490  1.00 33.71 ? 153 LYS E C   1 
ATOM   6622 O  O   . LYS E  1 152 ? 29.379 47.408  39.986  1.00 40.84 ? 153 LYS E O   1 
ATOM   6623 C  CB  . LYS E  1 152 ? 27.730 47.724  37.307  1.00 33.56 ? 153 LYS E CB  1 
ATOM   6624 C  CG  . LYS E  1 152 ? 28.215 48.016  35.914  1.00 34.07 ? 153 LYS E CG  1 
ATOM   6625 C  CD  . LYS E  1 152 ? 27.226 48.943  35.207  1.00 35.38 ? 153 LYS E CD  1 
ATOM   6626 C  CE  . LYS E  1 152 ? 27.723 49.334  33.829  1.00 39.44 ? 153 LYS E CE  1 
ATOM   6627 N  NZ  . LYS E  1 152 ? 26.727 50.199  33.105  1.00 43.31 ? 153 LYS E NZ  1 
ATOM   6628 N  N   . ARG E  1 153 ? 27.387 46.392  40.217  1.00 34.13 ? 154 ARG E N   1 
ATOM   6629 C  CA  . ARG E  1 153 ? 27.389 46.577  41.665  1.00 35.31 ? 154 ARG E CA  1 
ATOM   6630 C  C   . ARG E  1 153 ? 28.344 45.594  42.329  1.00 38.25 ? 154 ARG E C   1 
ATOM   6631 O  O   . ARG E  1 153 ? 29.180 45.986  43.152  1.00 39.92 ? 154 ARG E O   1 
ATOM   6632 C  CB  . ARG E  1 153 ? 25.969 46.418  42.224  1.00 35.02 ? 154 ARG E CB  1 
ATOM   6633 C  CG  . ARG E  1 153 ? 25.905 46.209  43.732  1.00 34.87 ? 154 ARG E CG  1 
ATOM   6634 C  CD  . ARG E  1 153 ? 24.465 46.036  44.220  1.00 34.08 ? 154 ARG E CD  1 
ATOM   6635 N  NE  . ARG E  1 153 ? 23.625 47.166  43.834  1.00 40.17 ? 154 ARG E NE  1 
ATOM   6636 C  CZ  . ARG E  1 153 ? 22.572 47.076  43.028  1.00 36.41 ? 154 ARG E CZ  1 
ATOM   6637 N  NH1 . ARG E  1 153 ? 22.213 45.920  42.488  1.00 32.42 ? 154 ARG E NH1 1 
ATOM   6638 N  NH2 . ARG E  1 153 ? 21.857 48.171  42.764  1.00 33.56 ? 154 ARG E NH2 1 
ATOM   6639 N  N   . ALA E  1 154 ? 28.229 44.307  41.974  1.00 35.84 ? 155 ALA E N   1 
ATOM   6640 C  CA  . ALA E  1 154 ? 29.109 43.285  42.535  1.00 40.13 ? 155 ALA E CA  1 
ATOM   6641 C  C   . ALA E  1 154 ? 30.557 43.533  42.141  1.00 37.93 ? 155 ALA E C   1 
ATOM   6642 O  O   . ALA E  1 154 ? 31.459 43.456  42.982  1.00 37.95 ? 155 ALA E O   1 
ATOM   6643 C  CB  . ALA E  1 154 ? 28.670 41.891  42.065  1.00 31.12 ? 155 ALA E CB  1 
ATOM   6644 N  N   . GLY E  1 155 ? 30.792 43.849  40.871  1.00 42.16 ? 156 GLY E N   1 
ATOM   6645 C  CA  . GLY E  1 155 ? 32.123 43.895  40.314  1.00 41.85 ? 156 GLY E CA  1 
ATOM   6646 C  C   . GLY E  1 155 ? 32.418 45.239  39.687  1.00 43.50 ? 156 GLY E C   1 
ATOM   6647 O  O   . GLY E  1 155 ? 32.464 46.266  40.372  1.00 50.54 ? 156 GLY E O   1 
ATOM   6648 N  N   . PRO E  1 156 ? 32.583 45.271  38.353  1.00 42.20 ? 157 PRO E N   1 
ATOM   6649 C  CA  . PRO E  1 156 ? 32.350 44.152  37.430  1.00 37.39 ? 157 PRO E CA  1 
ATOM   6650 C  C   . PRO E  1 156 ? 33.542 43.225  37.168  1.00 40.97 ? 157 PRO E C   1 
ATOM   6651 O  O   . PRO E  1 156 ? 33.475 42.435  36.236  1.00 39.29 ? 157 PRO E O   1 
ATOM   6652 C  CB  . PRO E  1 156 ? 31.968 44.865  36.138  1.00 38.30 ? 157 PRO E CB  1 
ATOM   6653 C  CG  . PRO E  1 156 ? 32.808 46.153  36.180  1.00 40.88 ? 157 PRO E CG  1 
ATOM   6654 C  CD  . PRO E  1 156 ? 32.971 46.509  37.641  1.00 41.25 ? 157 PRO E CD  1 
ATOM   6655 N  N   . THR E  1 157 ? 34.611 43.308  37.956  1.00 42.53 ? 158 THR E N   1 
ATOM   6656 C  CA  . THR E  1 157 ? 35.761 42.432  37.761  1.00 45.94 ? 158 THR E CA  1 
ATOM   6657 C  C   . THR E  1 157 ? 36.156 41.762  39.077  1.00 42.28 ? 158 THR E C   1 
ATOM   6658 O  O   . THR E  1 157 ? 35.624 42.065  40.149  1.00 43.24 ? 158 THR E O   1 
ATOM   6659 C  CB  . THR E  1 157 ? 36.957 43.205  37.182  1.00 47.90 ? 158 THR E CB  1 
ATOM   6660 O  OG1 . THR E  1 157 ? 37.184 44.392  37.957  1.00 45.29 ? 158 THR E OG1 1 
ATOM   6661 C  CG2 . THR E  1 157 ? 36.681 43.587  35.716  1.00 43.83 ? 158 THR E CG2 1 
ATOM   6662 N  N   . GLY E  1 158 ? 37.107 40.835  38.984  1.00 44.50 ? 159 GLY E N   1 
ATOM   6663 C  CA  . GLY E  1 158 ? 37.655 40.221  40.182  1.00 34.56 ? 159 GLY E CA  1 
ATOM   6664 C  C   . GLY E  1 158 ? 36.620 39.384  40.911  1.00 39.20 ? 159 GLY E C   1 
ATOM   6665 O  O   . GLY E  1 158 ? 35.842 38.633  40.304  1.00 37.33 ? 159 GLY E O   1 
ATOM   6666 N  N   . LEU E  1 159 ? 36.609 39.523  42.241  1.00 33.82 ? 160 LEU E N   1 
ATOM   6667 C  CA  . LEU E  1 159 ? 35.757 38.681  43.075  1.00 37.67 ? 160 LEU E CA  1 
ATOM   6668 C  C   . LEU E  1 159 ? 34.273 38.920  42.800  1.00 35.98 ? 160 LEU E C   1 
ATOM   6669 O  O   . LEU E  1 159 ? 33.474 37.982  42.880  1.00 37.64 ? 160 LEU E O   1 
ATOM   6670 C  CB  . LEU E  1 159 ? 36.077 38.910  44.558  1.00 37.38 ? 160 LEU E CB  1 
ATOM   6671 C  CG  . LEU E  1 159 ? 35.141 38.190  45.544  1.00 37.66 ? 160 LEU E CG  1 
ATOM   6672 C  CD1 . LEU E  1 159 ? 35.181 36.678  45.345  1.00 38.06 ? 160 LEU E CD1 1 
ATOM   6673 C  CD2 . LEU E  1 159 ? 35.437 38.545  46.986  1.00 32.78 ? 160 LEU E CD2 1 
ATOM   6674 N  N   . GLY E  1 160 ? 33.883 40.152  42.461  1.00 38.09 ? 161 GLY E N   1 
ATOM   6675 C  CA  . GLY E  1 160 ? 32.488 40.406  42.120  1.00 35.12 ? 161 GLY E CA  1 
ATOM   6676 C  C   . GLY E  1 160 ? 32.035 39.671  40.868  1.00 35.79 ? 161 GLY E C   1 
ATOM   6677 O  O   . GLY E  1 160 ? 30.941 39.100  40.837  1.00 34.39 ? 161 GLY E O   1 
ATOM   6678 N  N   . GLU E  1 161 ? 32.861 39.677  39.818  1.00 35.22 ? 162 GLU E N   1 
ATOM   6679 C  CA  . GLU E  1 161 ? 32.540 38.891  38.628  1.00 37.63 ? 162 GLU E CA  1 
ATOM   6680 C  C   . GLU E  1 161 ? 32.473 37.403  38.949  1.00 36.28 ? 162 GLU E C   1 
ATOM   6681 O  O   . GLU E  1 161 ? 31.624 36.682  38.413  1.00 34.99 ? 162 GLU E O   1 
ATOM   6682 C  CB  . GLU E  1 161 ? 33.570 39.144  37.525  1.00 40.11 ? 162 GLU E CB  1 
ATOM   6683 C  CG  . GLU E  1 161 ? 33.262 38.437  36.197  1.00 39.76 ? 162 GLU E CG  1 
ATOM   6684 C  CD  . GLU E  1 161 ? 34.276 38.772  35.084  1.00 49.37 ? 162 GLU E CD  1 
ATOM   6685 O  OE1 . GLU E  1 161 ? 35.495 38.586  35.308  1.00 51.54 ? 162 GLU E OE1 1 
ATOM   6686 O  OE2 . GLU E  1 161 ? 33.863 39.202  33.977  1.00 52.40 ? 162 GLU E OE2 1 
ATOM   6687 N  N   . TYR E  1 162 ? 33.363 36.923  39.821  1.00 36.68 ? 163 TYR E N   1 
ATOM   6688 C  CA  . TYR E  1 162 ? 33.348 35.505  40.165  1.00 35.45 ? 163 TYR E CA  1 
ATOM   6689 C  C   . TYR E  1 162 ? 32.057 35.131  40.882  1.00 33.57 ? 163 TYR E C   1 
ATOM   6690 O  O   . TYR E  1 162 ? 31.479 34.081  40.602  1.00 36.83 ? 163 TYR E O   1 
ATOM   6691 C  CB  . TYR E  1 162 ? 34.570 35.153  41.016  1.00 36.19 ? 163 TYR E CB  1 
ATOM   6692 C  CG  . TYR E  1 162 ? 34.498 33.796  41.701  1.00 35.59 ? 163 TYR E CG  1 
ATOM   6693 C  CD1 . TYR E  1 162 ? 34.856 32.637  41.026  1.00 38.54 ? 163 TYR E CD1 1 
ATOM   6694 C  CD2 . TYR E  1 162 ? 34.089 33.680  43.025  1.00 38.79 ? 163 TYR E CD2 1 
ATOM   6695 C  CE1 . TYR E  1 162 ? 34.798 31.397  41.639  1.00 39.54 ? 163 TYR E CE1 1 
ATOM   6696 C  CE2 . TYR E  1 162 ? 34.035 32.437  43.655  1.00 43.16 ? 163 TYR E CE2 1 
ATOM   6697 C  CZ  . TYR E  1 162 ? 34.390 31.299  42.950  1.00 44.83 ? 163 TYR E CZ  1 
ATOM   6698 O  OH  . TYR E  1 162 ? 34.334 30.064  43.554  1.00 44.54 ? 163 TYR E OH  1 
ATOM   6699 N  N   . MET E  1 163 ? 31.583 35.984  41.800  1.00 34.44 ? 164 MET E N   1 
ATOM   6700 C  CA  . MET E  1 163 ? 30.335 35.690  42.510  1.00 35.33 ? 164 MET E CA  1 
ATOM   6701 C  C   . MET E  1 163 ? 29.120 35.868  41.605  1.00 40.85 ? 164 MET E C   1 
ATOM   6702 O  O   . MET E  1 163 ? 28.200 35.039  41.626  1.00 36.11 ? 164 MET E O   1 
ATOM   6703 C  CB  . MET E  1 163 ? 30.198 36.569  43.758  1.00 37.86 ? 164 MET E CB  1 
ATOM   6704 C  CG  . MET E  1 163 ? 31.375 36.468  44.739  1.00 41.59 ? 164 MET E CG  1 
ATOM   6705 S  SD  . MET E  1 163 ? 31.492 34.858  45.583  1.00 51.82 ? 164 MET E SD  1 
ATOM   6706 C  CE  . MET E  1 163 ? 29.770 34.360  45.768  1.00 46.73 ? 164 MET E CE  1 
ATOM   6707 N  N   . PHE E  1 164 ? 29.095 36.935  40.797  1.00 36.05 ? 165 PHE E N   1 
ATOM   6708 C  CA  . PHE E  1 164 ? 27.991 37.086  39.855  1.00 39.80 ? 165 PHE E CA  1 
ATOM   6709 C  C   . PHE E  1 164 ? 27.873 35.865  38.949  1.00 36.85 ? 165 PHE E C   1 
ATOM   6710 O  O   . PHE E  1 164 ? 26.773 35.347  38.731  1.00 34.52 ? 165 PHE E O   1 
ATOM   6711 C  CB  . PHE E  1 164 ? 28.158 38.346  39.014  1.00 34.58 ? 165 PHE E CB  1 
ATOM   6712 C  CG  . PHE E  1 164 ? 27.012 38.576  38.088  1.00 35.31 ? 165 PHE E CG  1 
ATOM   6713 C  CD1 . PHE E  1 164 ? 25.833 39.135  38.559  1.00 36.59 ? 165 PHE E CD1 1 
ATOM   6714 C  CD2 . PHE E  1 164 ? 27.088 38.193  36.755  1.00 34.13 ? 165 PHE E CD2 1 
ATOM   6715 C  CE1 . PHE E  1 164 ? 24.755 39.326  37.708  1.00 39.60 ? 165 PHE E CE1 1 
ATOM   6716 C  CE2 . PHE E  1 164 ? 26.016 38.381  35.899  1.00 38.88 ? 165 PHE E CE2 1 
ATOM   6717 C  CZ  . PHE E  1 164 ? 24.845 38.953  36.374  1.00 37.78 ? 165 PHE E CZ  1 
ATOM   6718 N  N   . ASP E  1 165 ? 29.006 35.375  38.441  1.00 36.70 ? 166 ASP E N   1 
ATOM   6719 C  CA  . ASP E  1 165 ? 29.001 34.193  37.582  1.00 40.57 ? 166 ASP E CA  1 
ATOM   6720 C  C   . ASP E  1 165 ? 28.406 32.975  38.291  1.00 41.20 ? 166 ASP E C   1 
ATOM   6721 O  O   . ASP E  1 165 ? 27.662 32.201  37.679  1.00 37.33 ? 166 ASP E O   1 
ATOM   6722 C  CB  . ASP E  1 165 ? 30.422 33.874  37.117  1.00 37.55 ? 166 ASP E CB  1 
ATOM   6723 C  CG  . ASP E  1 165 ? 30.472 32.651  36.213  1.00 41.72 ? 166 ASP E CG  1 
ATOM   6724 O  OD1 . ASP E  1 165 ? 29.988 32.730  35.061  1.00 36.42 ? 166 ASP E OD1 1 
ATOM   6725 O  OD2 . ASP E  1 165 ? 30.950 31.590  36.679  1.00 49.69 ? 166 ASP E OD2 1 
ATOM   6726 N  N   . LYS E  1 166 ? 28.731 32.787  39.577  1.00 41.42 ? 167 LYS E N   1 
ATOM   6727 C  CA  . LYS E  1 166 ? 28.229 31.626  40.311  1.00 46.57 ? 167 LYS E CA  1 
ATOM   6728 C  C   . LYS E  1 166 ? 26.715 31.677  40.470  1.00 48.09 ? 167 LYS E C   1 
ATOM   6729 O  O   . LYS E  1 166 ? 26.063 30.628  40.524  1.00 51.73 ? 167 LYS E O   1 
ATOM   6730 C  CB  . LYS E  1 166 ? 28.906 31.524  41.686  1.00 44.99 ? 167 LYS E CB  1 
ATOM   6731 C  CG  . LYS E  1 166 ? 30.369 31.076  41.614  1.00 53.04 ? 167 LYS E CG  1 
ATOM   6732 C  CD  . LYS E  1 166 ? 30.885 30.401  42.902  1.00 56.39 ? 167 LYS E CD  1 
ATOM   6733 C  CE  . LYS E  1 166 ? 30.093 30.804  44.141  1.00 60.05 ? 167 LYS E CE  1 
ATOM   6734 N  NZ  . LYS E  1 166 ? 30.958 30.757  45.369  1.00 66.20 ? 167 LYS E NZ  1 
ATOM   6735 N  N   . GLU E  1 167 ? 26.130 32.874  40.537  1.00 44.86 ? 168 GLU E N   1 
ATOM   6736 C  CA  . GLU E  1 167 ? 24.681 32.943  40.648  1.00 53.49 ? 168 GLU E CA  1 
ATOM   6737 C  C   . GLU E  1 167 ? 23.982 32.733  39.312  1.00 53.35 ? 168 GLU E C   1 
ATOM   6738 O  O   . GLU E  1 167 ? 22.820 32.315  39.299  1.00 55.82 ? 168 GLU E O   1 
ATOM   6739 C  CB  . GLU E  1 167 ? 24.245 34.278  41.268  1.00 59.52 ? 168 GLU E CB  1 
ATOM   6740 C  CG  . GLU E  1 167 ? 22.812 34.261  41.859  1.00 71.49 ? 168 GLU E CG  1 
ATOM   6741 C  CD  . GLU E  1 167 ? 22.596 33.216  42.987  1.00 77.89 ? 168 GLU E CD  1 
ATOM   6742 O  OE1 . GLU E  1 167 ? 23.585 32.644  43.508  1.00 75.06 ? 168 GLU E OE1 1 
ATOM   6743 O  OE2 . GLU E  1 167 ? 21.417 32.956  43.339  1.00 75.88 ? 168 GLU E OE2 1 
ATOM   6744 N  N   . LEU E  1 168 ? 24.660 33.004  38.194  1.00 47.02 ? 169 LEU E N   1 
ATOM   6745 C  CA  . LEU E  1 168 ? 24.079 32.695  36.891  1.00 49.01 ? 169 LEU E CA  1 
ATOM   6746 C  C   . LEU E  1 168 ? 24.007 31.191  36.659  1.00 53.79 ? 169 LEU E C   1 
ATOM   6747 O  O   . LEU E  1 168 ? 23.072 30.701  36.015  1.00 56.40 ? 169 LEU E O   1 
ATOM   6748 C  CB  . LEU E  1 168 ? 24.903 33.351  35.782  1.00 46.22 ? 169 LEU E CB  1 
ATOM   6749 C  CG  . LEU E  1 168 ? 24.378 34.649  35.176  1.00 46.33 ? 169 LEU E CG  1 
ATOM   6750 C  CD1 . LEU E  1 168 ? 25.321 35.158  34.071  1.00 44.70 ? 169 LEU E CD1 1 
ATOM   6751 C  CD2 . LEU E  1 168 ? 22.961 34.464  34.660  1.00 50.53 ? 169 LEU E CD2 1 
ATOM   6752 N  N   . ASN E  1 169 ? 24.985 30.452  37.173  1.00 57.12 ? 170 ASN E N   1 
ATOM   6753 C  CA  . ASN E  1 169 ? 25.103 29.023  36.931  1.00 61.14 ? 170 ASN E CA  1 
ATOM   6754 C  C   . ASN E  1 169 ? 23.879 28.252  37.432  1.00 69.22 ? 170 ASN E C   1 
ATOM   6755 O  O   . ASN E  1 169 ? 23.388 28.475  38.544  1.00 75.81 ? 170 ASN E O   1 
ATOM   6756 C  CB  . ASN E  1 169 ? 26.375 28.499  37.596  1.00 60.98 ? 170 ASN E CB  1 
ATOM   6757 C  CG  . ASN E  1 169 ? 27.075 27.439  36.766  1.00 65.06 ? 170 ASN E CG  1 
ATOM   6758 O  OD1 . ASN E  1 169 ? 26.483 26.842  35.857  1.00 66.44 ? 170 ASN E OD1 1 
ATOM   6759 N  ND2 . ASN E  1 169 ? 28.347 27.203  37.070  1.00 60.91 ? 170 ASN E ND2 1 
ATOM   6760 O  OXT . ASN E  1 169 ? 23.353 27.392  36.722  1.00 72.69 ? 170 ASN E OXT 1 
ATOM   6761 N  N   . ALA F  1 1   ? 51.764 30.691  26.006  1.00 62.24 ? 2   ALA F N   1 
ATOM   6762 C  CA  . ALA F  1 1   ? 50.356 30.858  25.677  1.00 65.44 ? 2   ALA F CA  1 
ATOM   6763 C  C   . ALA F  1 1   ? 49.475 30.061  26.639  1.00 57.54 ? 2   ALA F C   1 
ATOM   6764 O  O   . ALA F  1 1   ? 49.228 30.486  27.768  1.00 60.57 ? 2   ALA F O   1 
ATOM   6765 C  CB  . ALA F  1 1   ? 50.087 30.436  24.229  1.00 61.26 ? 2   ALA F CB  1 
ATOM   6766 N  N   . SER F  1 2   ? 49.027 28.893  26.190  1.00 53.17 ? 3   SER F N   1 
ATOM   6767 C  CA  . SER F  1 2   ? 48.009 28.137  26.906  1.00 45.87 ? 3   SER F CA  1 
ATOM   6768 C  C   . SER F  1 2   ? 48.613 27.322  28.043  1.00 46.43 ? 3   SER F C   1 
ATOM   6769 O  O   . SER F  1 2   ? 49.581 26.582  27.849  1.00 45.75 ? 3   SER F O   1 
ATOM   6770 C  CB  . SER F  1 2   ? 47.270 27.212  25.945  1.00 43.48 ? 3   SER F CB  1 
ATOM   6771 O  OG  . SER F  1 2   ? 46.257 26.485  26.621  1.00 48.34 ? 3   SER F OG  1 
ATOM   6772 N  N   . GLN F  1 3   ? 48.012 27.438  29.226  1.00 42.73 ? 4   GLN F N   1 
ATOM   6773 C  CA  . GLN F  1 3   ? 48.455 26.657  30.371  1.00 41.15 ? 4   GLN F CA  1 
ATOM   6774 C  C   . GLN F  1 3   ? 48.042 25.188  30.278  1.00 39.42 ? 4   GLN F C   1 
ATOM   6775 O  O   . GLN F  1 3   ? 48.581 24.371  31.027  1.00 37.53 ? 4   GLN F O   1 
ATOM   6776 C  CB  . GLN F  1 3   ? 47.916 27.280  31.672  1.00 41.26 ? 4   GLN F CB  1 
ATOM   6777 C  CG  . GLN F  1 3   ? 46.431 26.978  31.941  1.00 44.53 ? 4   GLN F CG  1 
ATOM   6778 C  CD  . GLN F  1 3   ? 45.820 27.795  33.092  1.00 44.02 ? 4   GLN F CD  1 
ATOM   6779 O  OE1 . GLN F  1 3   ? 44.646 28.187  33.030  1.00 43.14 ? 4   GLN F OE1 1 
ATOM   6780 N  NE2 . GLN F  1 3   ? 46.601 28.029  34.148  1.00 39.41 ? 4   GLN F NE2 1 
ATOM   6781 N  N   . VAL F  1 4   ? 47.105 24.821  29.397  1.00 34.31 ? 5   VAL F N   1 
ATOM   6782 C  CA  . VAL F  1 4   ? 46.713 23.414  29.284  1.00 35.73 ? 5   VAL F CA  1 
ATOM   6783 C  C   . VAL F  1 4   ? 47.274 22.725  28.038  1.00 40.07 ? 5   VAL F C   1 
ATOM   6784 O  O   . VAL F  1 4   ? 47.268 21.479  27.984  1.00 40.04 ? 5   VAL F O   1 
ATOM   6785 C  CB  . VAL F  1 4   ? 45.176 23.226  29.323  1.00 35.68 ? 5   VAL F CB  1 
ATOM   6786 C  CG1 . VAL F  1 4   ? 44.536 24.037  30.450  1.00 36.29 ? 5   VAL F CG1 1 
ATOM   6787 C  CG2 . VAL F  1 4   ? 44.544 23.558  27.983  1.00 35.00 ? 5   VAL F CG2 1 
ATOM   6788 N  N   . ARG F  1 5   ? 47.764 23.475  27.049  1.00 34.93 ? 6   ARG F N   1 
ATOM   6789 C  CA  . ARG F  1 5   ? 48.090 22.897  25.750  1.00 38.17 ? 6   ARG F CA  1 
ATOM   6790 C  C   . ARG F  1 5   ? 49.296 21.967  25.845  1.00 36.58 ? 6   ARG F C   1 
ATOM   6791 O  O   . ARG F  1 5   ? 50.331 22.337  26.405  1.00 35.16 ? 6   ARG F O   1 
ATOM   6792 C  CB  . ARG F  1 5   ? 48.367 23.999  24.732  1.00 34.37 ? 6   ARG F CB  1 
ATOM   6793 C  CG  . ARG F  1 5   ? 48.416 23.514  23.292  1.00 37.19 ? 6   ARG F CG  1 
ATOM   6794 C  CD  . ARG F  1 5   ? 48.871 24.633  22.348  1.00 39.48 ? 6   ARG F CD  1 
ATOM   6795 N  NE  . ARG F  1 5   ? 48.753 24.246  20.946  1.00 41.06 ? 6   ARG F NE  1 
ATOM   6796 C  CZ  . ARG F  1 5   ? 48.005 24.880  20.049  1.00 40.67 ? 6   ARG F CZ  1 
ATOM   6797 N  NH1 . ARG F  1 5   ? 47.294 25.949  20.371  1.00 36.75 ? 6   ARG F NH1 1 
ATOM   6798 N  NH2 . ARG F  1 5   ? 47.977 24.434  18.794  1.00 33.75 ? 6   ARG F NH2 1 
ATOM   6799 N  N   . GLN F  1 6   ? 49.168 20.770  25.267  1.00 32.05 ? 7   GLN F N   1 
ATOM   6800 C  CA  . GLN F  1 6   ? 50.239 19.771  25.316  1.00 35.71 ? 7   GLN F CA  1 
ATOM   6801 C  C   . GLN F  1 6   ? 50.054 18.804  24.158  1.00 32.82 ? 7   GLN F C   1 
ATOM   6802 O  O   . GLN F  1 6   ? 48.988 18.189  24.035  1.00 33.23 ? 7   GLN F O   1 
ATOM   6803 C  CB  . GLN F  1 6   ? 50.229 19.030  26.659  1.00 32.80 ? 7   GLN F CB  1 
ATOM   6804 C  CG  . GLN F  1 6   ? 51.447 18.157  26.915  1.00 36.03 ? 7   GLN F CG  1 
ATOM   6805 C  CD  . GLN F  1 6   ? 51.432 17.509  28.316  1.00 43.61 ? 7   GLN F CD  1 
ATOM   6806 O  OE1 . GLN F  1 6   ? 50.372 17.362  28.945  1.00 41.38 ? 7   GLN F OE1 1 
ATOM   6807 N  NE2 . GLN F  1 6   ? 52.608 17.114  28.798  1.00 38.05 ? 7   GLN F NE2 1 
ATOM   6808 N  N   . ASN F  1 7   ? 51.075 18.679  23.302  1.00 35.52 ? 8   ASN F N   1 
ATOM   6809 C  CA  . ASN F  1 7   ? 51.041 17.756  22.158  1.00 35.49 ? 8   ASN F CA  1 
ATOM   6810 C  C   . ASN F  1 7   ? 49.887 18.065  21.204  1.00 33.37 ? 8   ASN F C   1 
ATOM   6811 O  O   . ASN F  1 7   ? 49.308 17.157  20.594  1.00 31.06 ? 8   ASN F O   1 
ATOM   6812 C  CB  . ASN F  1 7   ? 50.971 16.288  22.612  1.00 33.36 ? 8   ASN F CB  1 
ATOM   6813 C  CG  . ASN F  1 7   ? 51.345 15.308  21.495  1.00 37.06 ? 8   ASN F CG  1 
ATOM   6814 O  OD1 . ASN F  1 7   ? 52.254 15.575  20.710  1.00 34.70 ? 8   ASN F OD1 1 
ATOM   6815 N  ND2 . ASN F  1 7   ? 50.618 14.184  21.406  1.00 31.51 ? 8   ASN F ND2 1 
ATOM   6816 N  N   . TYR F  1 8   ? 49.534 19.341  21.061  1.00 30.82 ? 9   TYR F N   1 
ATOM   6817 C  CA  . TYR F  1 8   ? 48.441 19.759  20.177  1.00 32.26 ? 9   TYR F CA  1 
ATOM   6818 C  C   . TYR F  1 8   ? 49.053 20.578  19.051  1.00 34.15 ? 9   TYR F C   1 
ATOM   6819 O  O   . TYR F  1 8   ? 49.451 21.726  19.257  1.00 35.19 ? 9   TYR F O   1 
ATOM   6820 C  CB  . TYR F  1 8   ? 47.388 20.558  20.935  1.00 31.09 ? 9   TYR F CB  1 
ATOM   6821 C  CG  . TYR F  1 8   ? 46.067 20.685  20.221  1.00 31.45 ? 9   TYR F CG  1 
ATOM   6822 C  CD1 . TYR F  1 8   ? 45.457 19.581  19.628  1.00 32.97 ? 9   TYR F CD1 1 
ATOM   6823 C  CD2 . TYR F  1 8   ? 45.421 21.909  20.144  1.00 30.79 ? 9   TYR F CD2 1 
ATOM   6824 C  CE1 . TYR F  1 8   ? 44.225 19.701  18.970  1.00 33.39 ? 9   TYR F CE1 1 
ATOM   6825 C  CE2 . TYR F  1 8   ? 44.198 22.043  19.486  1.00 32.31 ? 9   TYR F CE2 1 
ATOM   6826 C  CZ  . TYR F  1 8   ? 43.606 20.939  18.907  1.00 33.50 ? 9   TYR F CZ  1 
ATOM   6827 O  OH  . TYR F  1 8   ? 42.399 21.081  18.258  1.00 35.54 ? 9   TYR F OH  1 
ATOM   6828 N  N   . HIS F  1 9   ? 49.137 19.981  17.865  1.00 34.93 ? 10  HIS F N   1 
ATOM   6829 C  CA  . HIS F  1 9   ? 49.798 20.624  16.742  1.00 41.73 ? 10  HIS F CA  1 
ATOM   6830 C  C   . HIS F  1 9   ? 48.869 21.663  16.106  1.00 42.09 ? 10  HIS F C   1 
ATOM   6831 O  O   . HIS F  1 9   ? 47.643 21.508  16.092  1.00 38.12 ? 10  HIS F O   1 
ATOM   6832 C  CB  . HIS F  1 9   ? 50.229 19.562  15.729  1.00 42.94 ? 10  HIS F CB  1 
ATOM   6833 C  CG  . HIS F  1 9   ? 51.152 20.068  14.660  1.00 52.56 ? 10  HIS F CG  1 
ATOM   6834 N  ND1 . HIS F  1 9   ? 52.447 19.617  14.521  1.00 56.74 ? 10  HIS F ND1 1 
ATOM   6835 C  CD2 . HIS F  1 9   ? 50.962 20.973  13.667  1.00 54.53 ? 10  HIS F CD2 1 
ATOM   6836 C  CE1 . HIS F  1 9   ? 53.015 20.225  13.493  1.00 55.43 ? 10  HIS F CE1 1 
ATOM   6837 N  NE2 . HIS F  1 9   ? 52.137 21.057  12.961  1.00 56.40 ? 10  HIS F NE2 1 
ATOM   6838 N  N   . GLU F  1 10  ? 49.464 22.742  15.590  1.00 37.38 ? 11  GLU F N   1 
ATOM   6839 C  CA  . GLU F  1 10  ? 48.659 23.806  14.990  1.00 44.10 ? 11  GLU F CA  1 
ATOM   6840 C  C   . GLU F  1 10  ? 47.914 23.334  13.741  1.00 42.46 ? 11  GLU F C   1 
ATOM   6841 O  O   . GLU F  1 10  ? 46.860 23.888  13.406  1.00 38.50 ? 11  GLU F O   1 
ATOM   6842 C  CB  . GLU F  1 10  ? 49.542 25.015  14.671  1.00 43.78 ? 11  GLU F CB  1 
ATOM   6843 C  CG  . GLU F  1 10  ? 50.464 24.816  13.478  1.00 56.96 ? 11  GLU F CG  1 
ATOM   6844 C  CD  . GLU F  1 10  ? 51.782 25.576  13.616  1.00 72.39 ? 11  GLU F CD  1 
ATOM   6845 O  OE1 . GLU F  1 10  ? 51.894 26.407  14.554  1.00 80.29 ? 11  GLU F OE1 1 
ATOM   6846 O  OE2 . GLU F  1 10  ? 52.695 25.348  12.788  1.00 79.57 ? 11  GLU F OE2 1 
ATOM   6847 N  N   . ASP F  1 11  ? 48.447 22.329  13.035  1.00 40.38 ? 12  ASP F N   1 
ATOM   6848 C  CA  . ASP F  1 11  ? 47.726 21.713  11.922  1.00 42.59 ? 12  ASP F CA  1 
ATOM   6849 C  C   . ASP F  1 11  ? 46.367 21.204  12.376  1.00 40.58 ? 12  ASP F C   1 
ATOM   6850 O  O   . ASP F  1 11  ? 45.341 21.444  11.728  1.00 40.84 ? 12  ASP F O   1 
ATOM   6851 C  CB  . ASP F  1 11  ? 48.522 20.534  11.361  1.00 47.74 ? 12  ASP F CB  1 
ATOM   6852 C  CG  . ASP F  1 11  ? 49.624 20.949  10.438  1.00 59.70 ? 12  ASP F CG  1 
ATOM   6853 O  OD1 . ASP F  1 11  ? 49.737 22.166  10.150  1.00 64.46 ? 12  ASP F OD1 1 
ATOM   6854 O  OD2 . ASP F  1 11  ? 50.380 20.040  10.005  1.00 66.05 ? 12  ASP F OD2 1 
ATOM   6855 N  N   . ALA F  1 12  ? 46.360 20.443  13.468  1.00 35.15 ? 13  ALA F N   1 
ATOM   6856 C  CA  . ALA F  1 12  ? 45.118 19.905  13.997  1.00 39.67 ? 13  ALA F CA  1 
ATOM   6857 C  C   . ALA F  1 12  ? 44.166 21.025  14.397  1.00 35.56 ? 13  ALA F C   1 
ATOM   6858 O  O   . ALA F  1 12  ? 42.970 20.970  14.087  1.00 33.37 ? 13  ALA F O   1 
ATOM   6859 C  CB  . ALA F  1 12  ? 45.422 18.998  15.192  1.00 34.68 ? 13  ALA F CB  1 
ATOM   6860 N  N   . GLU F  1 13  ? 44.688 22.057  15.072  1.00 34.50 ? 14  GLU F N   1 
ATOM   6861 C  CA  . GLU F  1 13  ? 43.848 23.164  15.532  1.00 37.76 ? 14  GLU F CA  1 
ATOM   6862 C  C   . GLU F  1 13  ? 43.145 23.865  14.372  1.00 34.00 ? 14  GLU F C   1 
ATOM   6863 O  O   . GLU F  1 13  ? 41.953 24.193  14.463  1.00 29.22 ? 14  GLU F O   1 
ATOM   6864 C  CB  . GLU F  1 13  ? 44.692 24.146  16.344  1.00 32.92 ? 14  GLU F CB  1 
ATOM   6865 C  CG  . GLU F  1 13  ? 44.012 25.463  16.705  1.00 38.93 ? 14  GLU F CG  1 
ATOM   6866 C  CD  . GLU F  1 13  ? 44.903 26.398  17.541  1.00 42.35 ? 14  GLU F CD  1 
ATOM   6867 O  OE1 . GLU F  1 13  ? 46.147 26.224  17.558  1.00 44.45 ? 14  GLU F OE1 1 
ATOM   6868 O  OE2 . GLU F  1 13  ? 44.357 27.339  18.158  1.00 42.84 ? 14  GLU F OE2 1 
ATOM   6869 N  N   . ALA F  1 14  ? 43.855 24.080  13.265  1.00 34.32 ? 15  ALA F N   1 
ATOM   6870 C  CA  . ALA F  1 14  ? 43.233 24.707  12.103  1.00 33.95 ? 15  ALA F CA  1 
ATOM   6871 C  C   . ALA F  1 14  ? 42.246 23.767  11.413  1.00 33.97 ? 15  ALA F C   1 
ATOM   6872 O  O   . ALA F  1 14  ? 41.216 24.220  10.896  1.00 33.50 ? 15  ALA F O   1 
ATOM   6873 C  CB  . ALA F  1 14  ? 44.313 25.172  11.120  1.00 31.66 ? 15  ALA F CB  1 
ATOM   6874 N  N   . SER F  1 15  ? 42.533 22.465  11.397  1.00 32.80 ? 16  SER F N   1 
ATOM   6875 C  CA  . SER F  1 15  ? 41.628 21.521  10.745  1.00 35.33 ? 16  SER F CA  1 
ATOM   6876 C  C   . SER F  1 15  ? 40.340 21.347  11.543  1.00 37.65 ? 16  SER F C   1 
ATOM   6877 O  O   . SER F  1 15  ? 39.262 21.169  10.955  1.00 33.97 ? 16  SER F O   1 
ATOM   6878 C  CB  . SER F  1 15  ? 42.319 20.173  10.555  1.00 40.25 ? 16  SER F CB  1 
ATOM   6879 O  OG  . SER F  1 15  ? 42.945 20.098  9.292   1.00 47.20 ? 16  SER F OG  1 
ATOM   6880 N  N   . ILE F  1 16  ? 40.435 21.393  12.880  1.00 32.81 ? 17  ILE F N   1 
ATOM   6881 C  CA  . ILE F  1 16  ? 39.237 21.361  13.720  1.00 32.98 ? 17  ILE F CA  1 
ATOM   6882 C  C   . ILE F  1 16  ? 38.329 22.540  13.394  1.00 32.58 ? 17  ILE F C   1 
ATOM   6883 O  O   . ILE F  1 16  ? 37.108 22.384  13.258  1.00 28.86 ? 17  ILE F O   1 
ATOM   6884 C  CB  . ILE F  1 16  ? 39.606 21.360  15.214  1.00 33.78 ? 17  ILE F CB  1 
ATOM   6885 C  CG1 . ILE F  1 16  ? 40.386 20.102  15.601  1.00 34.49 ? 17  ILE F CG1 1 
ATOM   6886 C  CG2 . ILE F  1 16  ? 38.342 21.526  16.074  1.00 33.40 ? 17  ILE F CG2 1 
ATOM   6887 C  CD1 . ILE F  1 16  ? 39.695 18.844  15.308  1.00 37.66 ? 17  ILE F CD1 1 
ATOM   6888 N  N   . ASN F  1 17  ? 38.908 23.744  13.292  1.00 29.99 ? 18  ASN F N   1 
ATOM   6889 C  CA  . ASN F  1 17  ? 38.105 24.911  12.940  1.00 29.48 ? 18  ASN F CA  1 
ATOM   6890 C  C   . ASN F  1 17  ? 37.441 24.748  11.575  1.00 32.52 ? 18  ASN F C   1 
ATOM   6891 O  O   . ASN F  1 17  ? 36.266 25.100  11.409  1.00 30.70 ? 18  ASN F O   1 
ATOM   6892 C  CB  . ASN F  1 17  ? 38.955 26.177  12.982  1.00 30.57 ? 18  ASN F CB  1 
ATOM   6893 C  CG  . ASN F  1 17  ? 39.206 26.638  14.389  1.00 33.79 ? 18  ASN F CG  1 
ATOM   6894 O  OD1 . ASN F  1 17  ? 38.401 26.373  15.275  1.00 33.98 ? 18  ASN F OD1 1 
ATOM   6895 N  ND2 . ASN F  1 17  ? 40.326 27.315  14.615  1.00 31.66 ? 18  ASN F ND2 1 
ATOM   6896 N  N   . LYS F  1 18  ? 38.153 24.193  10.586  1.00 27.48 ? 19  LYS F N   1 
ATOM   6897 C  CA  . LYS F  1 18  ? 37.499 24.011  9.293   1.00 32.30 ? 19  LYS F CA  1 
ATOM   6898 C  C   . LYS F  1 18  ? 36.379 22.975  9.382   1.00 33.36 ? 19  LYS F C   1 
ATOM   6899 O  O   . LYS F  1 18  ? 35.308 23.148  8.781   1.00 28.37 ? 19  LYS F O   1 
ATOM   6900 C  CB  . LYS F  1 18  ? 38.509 23.618  8.219   1.00 35.19 ? 19  LYS F CB  1 
ATOM   6901 C  CG  . LYS F  1 18  ? 37.881 23.665  6.838   1.00 43.14 ? 19  LYS F CG  1 
ATOM   6902 C  CD  . LYS F  1 18  ? 38.745 23.067  5.732   1.00 53.78 ? 19  LYS F CD  1 
ATOM   6903 C  CE  . LYS F  1 18  ? 37.961 23.055  4.404   1.00 54.32 ? 19  LYS F CE  1 
ATOM   6904 N  NZ  . LYS F  1 18  ? 38.753 22.508  3.260   1.00 61.78 ? 19  LYS F NZ  1 
ATOM   6905 N  N   . GLN F  1 19  ? 36.604 21.899  10.141  1.00 29.96 ? 20  GLN F N   1 
ATOM   6906 C  CA  . GLN F  1 19  ? 35.589 20.864  10.308  1.00 30.81 ? 20  GLN F CA  1 
ATOM   6907 C  C   . GLN F  1 19  ? 34.369 21.366  11.091  1.00 32.02 ? 20  GLN F C   1 
ATOM   6908 O  O   . GLN F  1 19  ? 33.242 20.919  10.833  1.00 29.11 ? 20  GLN F O   1 
ATOM   6909 C  CB  . GLN F  1 19  ? 36.212 19.658  11.001  1.00 35.09 ? 20  GLN F CB  1 
ATOM   6910 C  CG  . GLN F  1 19  ? 35.344 18.420  10.946  1.00 40.88 ? 20  GLN F CG  1 
ATOM   6911 C  CD  . GLN F  1 19  ? 35.168 17.898  9.542   1.00 44.63 ? 20  GLN F CD  1 
ATOM   6912 O  OE1 . GLN F  1 19  ? 36.133 17.819  8.778   1.00 44.76 ? 20  GLN F OE1 1 
ATOM   6913 N  NE2 . GLN F  1 19  ? 33.927 17.551  9.182   1.00 45.42 ? 20  GLN F NE2 1 
ATOM   6914 N  N   . ILE F  1 20  ? 34.563 22.280  12.050  1.00 28.17 ? 21  ILE F N   1 
ATOM   6915 C  CA  . ILE F  1 20  ? 33.418 22.926  12.690  1.00 29.20 ? 21  ILE F CA  1 
ATOM   6916 C  C   . ILE F  1 20  ? 32.555 23.618  11.642  1.00 30.52 ? 21  ILE F C   1 
ATOM   6917 O  O   . ILE F  1 20  ? 31.337 23.411  11.572  1.00 28.89 ? 21  ILE F O   1 
ATOM   6918 C  CB  . ILE F  1 20  ? 33.889 23.922  13.762  1.00 29.77 ? 21  ILE F CB  1 
ATOM   6919 C  CG1 . ILE F  1 20  ? 34.394 23.165  14.997  1.00 28.56 ? 21  ILE F CG1 1 
ATOM   6920 C  CG2 . ILE F  1 20  ? 32.751 24.870  14.123  1.00 27.00 ? 21  ILE F CG2 1 
ATOM   6921 C  CD1 . ILE F  1 20  ? 35.409 23.947  15.837  1.00 29.70 ? 21  ILE F CD1 1 
ATOM   6922 N  N   . ASN F  1 21  ? 33.186 24.426  10.784  1.00 28.44 ? 22  ASN F N   1 
ATOM   6923 C  CA  . ASN F  1 21  ? 32.436 25.133  9.754   1.00 27.31 ? 22  ASN F CA  1 
ATOM   6924 C  C   . ASN F  1 21  ? 31.735 24.159  8.814   1.00 27.61 ? 22  ASN F C   1 
ATOM   6925 O  O   . ASN F  1 21  ? 30.611 24.422  8.375   1.00 28.03 ? 22  ASN F O   1 
ATOM   6926 C  CB  . ASN F  1 21  ? 33.364 26.086  8.980   1.00 26.21 ? 22  ASN F CB  1 
ATOM   6927 C  CG  . ASN F  1 21  ? 32.600 27.019  8.040   1.00 28.59 ? 22  ASN F CG  1 
ATOM   6928 O  OD1 . ASN F  1 21  ? 32.512 26.763  6.845   1.00 31.50 ? 22  ASN F OD1 1 
ATOM   6929 N  ND2 . ASN F  1 21  ? 32.033 28.094  8.584   1.00 25.01 ? 22  ASN F ND2 1 
ATOM   6930 N  N   . MET F  1 22  ? 32.353 23.013  8.533   1.00 27.59 ? 23  MET F N   1 
ATOM   6931 C  CA  . MET F  1 22  ? 31.750 22.066  7.597   1.00 30.14 ? 23  MET F CA  1 
ATOM   6932 C  C   . MET F  1 22  ? 30.500 21.408  8.186   1.00 30.87 ? 23  MET F C   1 
ATOM   6933 O  O   . MET F  1 22  ? 29.487 21.253  7.497   1.00 24.69 ? 23  MET F O   1 
ATOM   6934 C  CB  . MET F  1 22  ? 32.776 21.007  7.202   1.00 30.18 ? 23  MET F CB  1 
ATOM   6935 C  CG  . MET F  1 22  ? 32.311 20.077  6.078   1.00 43.27 ? 23  MET F CG  1 
ATOM   6936 S  SD  . MET F  1 22  ? 33.406 18.638  5.808   1.00 55.53 ? 23  MET F SD  1 
ATOM   6937 C  CE  . MET F  1 22  ? 32.854 18.129  4.169   1.00 46.01 ? 23  MET F CE  1 
ATOM   6938 N  N   . CYS F  1 23  ? 30.546 21.019  9.464   1.00 29.75 ? 24  CYS F N   1 
ATOM   6939 C  CA  . CYS F  1 23  ? 29.357 20.429  10.070  1.00 32.58 ? 24  CYS F CA  1 
ATOM   6940 C  C   . CYS F  1 23  ? 28.254 21.468  10.278  1.00 33.04 ? 24  CYS F C   1 
ATOM   6941 O  O   . CYS F  1 23  ? 27.069 21.137  10.157  1.00 29.36 ? 24  CYS F O   1 
ATOM   6942 C  CB  . CYS F  1 23  ? 29.729 19.720  11.376  1.00 33.00 ? 24  CYS F CB  1 
ATOM   6943 S  SG  . CYS F  1 23  ? 30.500 18.063  11.061  1.00 50.37 ? 24  CYS F SG  1 
ATOM   6944 N  N   . LEU F  1 24  ? 28.607 22.732  10.545  1.00 27.09 ? 25  LEU F N   1 
ATOM   6945 C  CA  . LEU F  1 24  ? 27.556 23.750  10.614  1.00 28.94 ? 25  LEU F CA  1 
ATOM   6946 C  C   . LEU F  1 24  ? 26.901 23.946  9.254   1.00 28.73 ? 25  LEU F C   1 
ATOM   6947 O  O   . LEU F  1 24  ? 25.678 24.089  9.163   1.00 29.33 ? 25  LEU F O   1 
ATOM   6948 C  CB  . LEU F  1 24  ? 28.108 25.075  11.125  1.00 26.99 ? 25  LEU F CB  1 
ATOM   6949 C  CG  . LEU F  1 24  ? 28.613 25.095  12.559  1.00 30.23 ? 25  LEU F CG  1 
ATOM   6950 C  CD1 . LEU F  1 24  ? 29.373 26.401  12.782  1.00 24.08 ? 25  LEU F CD1 1 
ATOM   6951 C  CD2 . LEU F  1 24  ? 27.448 24.943  13.520  1.00 28.97 ? 25  LEU F CD2 1 
ATOM   6952 N  N   . TYR F  1 25  ? 27.696 23.913  8.182   1.00 25.45 ? 26  TYR F N   1 
ATOM   6953 C  CA  . TYR F  1 25  ? 27.122 24.002  6.847   1.00 28.38 ? 26  TYR F CA  1 
ATOM   6954 C  C   . TYR F  1 25  ? 26.223 22.805  6.540   1.00 29.98 ? 26  TYR F C   1 
ATOM   6955 O  O   . TYR F  1 25  ? 25.127 22.976  5.992   1.00 26.98 ? 26  TYR F O   1 
ATOM   6956 C  CB  . TYR F  1 25  ? 28.226 24.127  5.800   1.00 26.13 ? 26  TYR F CB  1 
ATOM   6957 C  CG  . TYR F  1 25  ? 27.675 24.141  4.395   1.00 29.80 ? 26  TYR F CG  1 
ATOM   6958 C  CD1 . TYR F  1 25  ? 27.001 25.248  3.906   1.00 30.86 ? 26  TYR F CD1 1 
ATOM   6959 C  CD2 . TYR F  1 25  ? 27.787 23.024  3.570   1.00 33.55 ? 26  TYR F CD2 1 
ATOM   6960 C  CE1 . TYR F  1 25  ? 26.476 25.264  2.613   1.00 29.39 ? 26  TYR F CE1 1 
ATOM   6961 C  CE2 . TYR F  1 25  ? 27.271 23.029  2.286   1.00 38.44 ? 26  TYR F CE2 1 
ATOM   6962 C  CZ  . TYR F  1 25  ? 26.620 24.155  1.812   1.00 36.31 ? 26  TYR F CZ  1 
ATOM   6963 O  OH  . TYR F  1 25  ? 26.106 24.156  0.530   1.00 45.50 ? 26  TYR F OH  1 
ATOM   6964 N  N   . ALA F  1 26  ? 26.684 21.584  6.861   1.00 26.28 ? 27  ALA F N   1 
ATOM   6965 C  CA  . ALA F  1 26  ? 25.844 20.400  6.693   1.00 33.81 ? 27  ALA F CA  1 
ATOM   6966 C  C   . ALA F  1 26  ? 24.540 20.546  7.463   1.00 31.19 ? 27  ALA F C   1 
ATOM   6967 O  O   . ALA F  1 26  ? 23.467 20.219  6.947   1.00 30.02 ? 27  ALA F O   1 
ATOM   6968 C  CB  . ALA F  1 26  ? 26.580 19.136  7.149   1.00 28.40 ? 27  ALA F CB  1 
ATOM   6969 N  N   . SER F  1 27  ? 24.613 21.069  8.690   1.00 30.37 ? 28  SER F N   1 
ATOM   6970 C  CA  . SER F  1 27  ? 23.407 21.253  9.487   1.00 31.92 ? 28  SER F CA  1 
ATOM   6971 C  C   . SER F  1 27  ? 22.453 22.229  8.820   1.00 32.08 ? 28  SER F C   1 
ATOM   6972 O  O   . SER F  1 27  ? 21.224 22.066  8.898   1.00 29.88 ? 28  SER F O   1 
ATOM   6973 C  CB  . SER F  1 27  ? 23.784 21.741  10.888  1.00 31.24 ? 28  SER F CB  1 
ATOM   6974 O  OG  . SER F  1 27  ? 22.636 22.085  11.623  1.00 34.21 ? 28  SER F OG  1 
ATOM   6975 N  N   . TYR F  1 28  ? 23.011 23.237  8.147   1.00 27.76 ? 29  TYR F N   1 
ATOM   6976 C  CA  . TYR F  1 28  ? 22.212 24.242  7.463   1.00 28.05 ? 29  TYR F CA  1 
ATOM   6977 C  C   . TYR F  1 28  ? 21.552 23.656  6.223   1.00 30.29 ? 29  TYR F C   1 
ATOM   6978 O  O   . TYR F  1 28  ? 20.385 23.948  5.930   1.00 30.15 ? 29  TYR F O   1 
ATOM   6979 C  CB  . TYR F  1 28  ? 23.116 25.422  7.101   1.00 31.37 ? 29  TYR F CB  1 
ATOM   6980 C  CG  . TYR F  1 28  ? 22.441 26.752  6.922   1.00 28.88 ? 29  TYR F CG  1 
ATOM   6981 C  CD1 . TYR F  1 28  ? 21.155 26.986  7.401   1.00 28.86 ? 29  TYR F CD1 1 
ATOM   6982 C  CD2 . TYR F  1 28  ? 23.098 27.784  6.278   1.00 30.55 ? 29  TYR F CD2 1 
ATOM   6983 C  CE1 . TYR F  1 28  ? 20.550 28.198  7.236   1.00 27.96 ? 29  TYR F CE1 1 
ATOM   6984 C  CE2 . TYR F  1 28  ? 22.504 29.011  6.114   1.00 29.42 ? 29  TYR F CE2 1 
ATOM   6985 C  CZ  . TYR F  1 28  ? 21.231 29.215  6.585   1.00 32.48 ? 29  TYR F CZ  1 
ATOM   6986 O  OH  . TYR F  1 28  ? 20.654 30.455  6.399   1.00 32.29 ? 29  TYR F OH  1 
ATOM   6987 N  N   . VAL F  1 29  ? 22.282 22.811  5.493   1.00 31.87 ? 30  VAL F N   1 
ATOM   6988 C  CA  . VAL F  1 29  ? 21.728 22.161  4.310   1.00 32.04 ? 30  VAL F CA  1 
ATOM   6989 C  C   . VAL F  1 29  ? 20.562 21.263  4.697   1.00 34.37 ? 30  VAL F C   1 
ATOM   6990 O  O   . VAL F  1 29  ? 19.508 21.277  4.050   1.00 33.20 ? 30  VAL F O   1 
ATOM   6991 C  CB  . VAL F  1 29  ? 22.827 21.373  3.568   1.00 33.71 ? 30  VAL F CB  1 
ATOM   6992 C  CG1 . VAL F  1 29  ? 22.205 20.482  2.499   1.00 35.01 ? 30  VAL F CG1 1 
ATOM   6993 C  CG2 . VAL F  1 29  ? 23.848 22.320  2.955   1.00 30.16 ? 30  VAL F CG2 1 
ATOM   6994 N  N   . TYR F  1 30  ? 20.729 20.477  5.766   1.00 34.22 ? 31  TYR F N   1 
ATOM   6995 C  CA  . TYR F  1 30  ? 19.662 19.588  6.210   1.00 33.86 ? 31  TYR F CA  1 
ATOM   6996 C  C   . TYR F  1 30  ? 18.452 20.377  6.675   1.00 33.93 ? 31  TYR F C   1 
ATOM   6997 O  O   . TYR F  1 30  ? 17.311 19.940  6.479   1.00 33.98 ? 31  TYR F O   1 
ATOM   6998 C  CB  . TYR F  1 30  ? 20.148 18.683  7.346   1.00 34.76 ? 31  TYR F CB  1 
ATOM   6999 C  CG  . TYR F  1 30  ? 21.048 17.573  6.891   1.00 37.89 ? 31  TYR F CG  1 
ATOM   7000 C  CD1 . TYR F  1 30  ? 20.735 16.819  5.763   1.00 41.72 ? 31  TYR F CD1 1 
ATOM   7001 C  CD2 . TYR F  1 30  ? 22.223 17.285  7.575   1.00 34.26 ? 31  TYR F CD2 1 
ATOM   7002 C  CE1 . TYR F  1 30  ? 21.569 15.802  5.337   1.00 44.27 ? 31  TYR F CE1 1 
ATOM   7003 C  CE2 . TYR F  1 30  ? 23.060 16.277  7.162   1.00 37.84 ? 31  TYR F CE2 1 
ATOM   7004 C  CZ  . TYR F  1 30  ? 22.728 15.540  6.047   1.00 42.91 ? 31  TYR F CZ  1 
ATOM   7005 O  OH  . TYR F  1 30  ? 23.561 14.541  5.636   1.00 49.96 ? 31  TYR F OH  1 
ATOM   7006 N  N   . LEU F  1 31  ? 18.684 21.516  7.341   1.00 30.80 ? 32  LEU F N   1 
ATOM   7007 C  CA  . LEU F  1 31  ? 17.571 22.363  7.767   1.00 33.02 ? 32  LEU F CA  1 
ATOM   7008 C  C   . LEU F  1 31  ? 16.772 22.846  6.565   1.00 31.52 ? 32  LEU F C   1 
ATOM   7009 O  O   . LEU F  1 31  ? 15.536 22.880  6.595   1.00 31.17 ? 32  LEU F O   1 
ATOM   7010 C  CB  . LEU F  1 31  ? 18.089 23.553  8.582   1.00 29.69 ? 32  LEU F CB  1 
ATOM   7011 C  CG  . LEU F  1 31  ? 17.014 24.365  9.306   1.00 35.67 ? 32  LEU F CG  1 
ATOM   7012 C  CD1 . LEU F  1 31  ? 16.366 23.523  10.410  1.00 29.82 ? 32  LEU F CD1 1 
ATOM   7013 C  CD2 . LEU F  1 31  ? 17.601 25.639  9.869   1.00 34.05 ? 32  LEU F CD2 1 
ATOM   7014 N  N   . SER F  1 32  ? 17.471 23.217  5.494   1.00 31.12 ? 33  SER F N   1 
ATOM   7015 C  CA  . SER F  1 32  ? 16.806 23.617  4.266   1.00 31.79 ? 33  SER F CA  1 
ATOM   7016 C  C   . SER F  1 32  ? 15.962 22.481  3.715   1.00 34.85 ? 33  SER F C   1 
ATOM   7017 O  O   . SER F  1 32  ? 14.797 22.677  3.349   1.00 31.82 ? 33  SER F O   1 
ATOM   7018 C  CB  . SER F  1 32  ? 17.853 24.054  3.246   1.00 32.39 ? 33  SER F CB  1 
ATOM   7019 O  OG  . SER F  1 32  ? 17.254 24.262  1.993   1.00 40.41 ? 33  SER F OG  1 
ATOM   7020 N  N   . MET F  1 33  ? 16.543 21.277  3.647   1.00 33.06 ? 34  MET F N   1 
ATOM   7021 C  CA  . MET F  1 33  ? 15.800 20.098  3.203   1.00 37.55 ? 34  MET F CA  1 
ATOM   7022 C  C   . MET F  1 33  ? 14.553 19.879  4.055   1.00 33.59 ? 34  MET F C   1 
ATOM   7023 O  O   . MET F  1 33  ? 13.449 19.689  3.531   1.00 33.02 ? 34  MET F O   1 
ATOM   7024 C  CB  . MET F  1 33  ? 16.698 18.863  3.267   1.00 34.60 ? 34  MET F CB  1 
ATOM   7025 C  CG  . MET F  1 33  ? 17.624 18.669  2.078   1.00 39.30 ? 34  MET F CG  1 
ATOM   7026 S  SD  . MET F  1 33  ? 18.605 17.153  2.259   1.00 44.92 ? 34  MET F SD  1 
ATOM   7027 C  CE  . MET F  1 33  ? 19.960 17.470  1.130   1.00 39.61 ? 34  MET F CE  1 
ATOM   7028 N  N   . ALA F  1 34  ? 14.717 19.910  5.378   1.00 30.17 ? 35  ALA F N   1 
ATOM   7029 C  CA  . ALA F  1 34  ? 13.605 19.621  6.277   1.00 32.09 ? 35  ALA F CA  1 
ATOM   7030 C  C   . ALA F  1 34  ? 12.419 20.535  6.005   1.00 37.06 ? 35  ALA F C   1 
ATOM   7031 O  O   . ALA F  1 34  ? 11.270 20.079  5.956   1.00 37.09 ? 35  ALA F O   1 
ATOM   7032 C  CB  . ALA F  1 34  ? 14.051 19.765  7.730   1.00 31.36 ? 35  ALA F CB  1 
ATOM   7033 N  N   . TYR F  1 35  ? 12.669 21.838  5.858   1.00 30.97 ? 36  TYR F N   1 
ATOM   7034 C  CA  . TYR F  1 35  ? 11.541 22.748  5.701   1.00 32.03 ? 36  TYR F CA  1 
ATOM   7035 C  C   . TYR F  1 35  ? 11.026 22.756  4.272   1.00 34.66 ? 36  TYR F C   1 
ATOM   7036 O  O   . TYR F  1 35  ? 9.857  23.089  4.053   1.00 34.46 ? 36  TYR F O   1 
ATOM   7037 C  CB  . TYR F  1 35  ? 11.921 24.157  6.176   1.00 33.57 ? 36  TYR F CB  1 
ATOM   7038 C  CG  . TYR F  1 35  ? 11.798 24.257  7.674   1.00 32.23 ? 36  TYR F CG  1 
ATOM   7039 C  CD1 . TYR F  1 35  ? 10.558 24.468  8.271   1.00 38.72 ? 36  TYR F CD1 1 
ATOM   7040 C  CD2 . TYR F  1 35  ? 12.898 24.071  8.495   1.00 32.59 ? 36  TYR F CD2 1 
ATOM   7041 C  CE1 . TYR F  1 35  ? 10.415 24.523  9.644   1.00 37.02 ? 36  TYR F CE1 1 
ATOM   7042 C  CE2 . TYR F  1 35  ? 12.769 24.121  9.884   1.00 39.33 ? 36  TYR F CE2 1 
ATOM   7043 C  CZ  . TYR F  1 35  ? 11.518 24.348  10.451  1.00 42.98 ? 36  TYR F CZ  1 
ATOM   7044 O  OH  . TYR F  1 35  ? 11.367 24.408  11.820  1.00 43.00 ? 36  TYR F OH  1 
ATOM   7045 N  N   . TYR F  1 36  ? 11.860 22.362  3.304   1.00 31.06 ? 37  TYR F N   1 
ATOM   7046 C  CA  . TYR F  1 36  ? 11.356 22.141  1.957   1.00 33.94 ? 37  TYR F CA  1 
ATOM   7047 C  C   . TYR F  1 36  ? 10.295 21.050  1.953   1.00 35.98 ? 37  TYR F C   1 
ATOM   7048 O  O   . TYR F  1 36  ? 9.268  21.174  1.278   1.00 32.23 ? 37  TYR F O   1 
ATOM   7049 C  CB  . TYR F  1 36  ? 12.500 21.775  1.013   1.00 32.86 ? 37  TYR F CB  1 
ATOM   7050 C  CG  . TYR F  1 36  ? 12.038 21.273  -0.337  1.00 34.53 ? 37  TYR F CG  1 
ATOM   7051 C  CD1 . TYR F  1 36  ? 11.616 22.157  -1.326  1.00 39.04 ? 37  TYR F CD1 1 
ATOM   7052 C  CD2 . TYR F  1 36  ? 12.022 19.915  -0.627  1.00 32.68 ? 37  TYR F CD2 1 
ATOM   7053 C  CE1 . TYR F  1 36  ? 11.193 21.694  -2.571  1.00 39.87 ? 37  TYR F CE1 1 
ATOM   7054 C  CE2 . TYR F  1 36  ? 11.598 19.451  -1.859  1.00 37.27 ? 37  TYR F CE2 1 
ATOM   7055 C  CZ  . TYR F  1 36  ? 11.184 20.341  -2.827  1.00 38.62 ? 37  TYR F CZ  1 
ATOM   7056 O  OH  . TYR F  1 36  ? 10.767 19.870  -4.051  1.00 44.28 ? 37  TYR F OH  1 
ATOM   7057 N  N   . PHE F  1 37  ? 10.520 19.979  2.712   1.00 34.94 ? 38  PHE F N   1 
ATOM   7058 C  CA  . PHE F  1 37  ? 9.597  18.856  2.701   1.00 34.85 ? 38  PHE F CA  1 
ATOM   7059 C  C   . PHE F  1 37  ? 8.360  19.113  3.550   1.00 36.42 ? 38  PHE F C   1 
ATOM   7060 O  O   . PHE F  1 37  ? 7.440  18.294  3.521   1.00 34.48 ? 38  PHE F O   1 
ATOM   7061 C  CB  . PHE F  1 37  ? 10.321 17.577  3.148   1.00 30.47 ? 38  PHE F CB  1 
ATOM   7062 C  CG  . PHE F  1 37  ? 11.210 16.996  2.077   1.00 36.65 ? 38  PHE F CG  1 
ATOM   7063 C  CD1 . PHE F  1 37  ? 10.660 16.466  0.914   1.00 35.02 ? 38  PHE F CD1 1 
ATOM   7064 C  CD2 . PHE F  1 37  ? 12.593 17.021  2.205   1.00 31.15 ? 38  PHE F CD2 1 
ATOM   7065 C  CE1 . PHE F  1 37  ? 11.461 15.950  -0.092  1.00 35.19 ? 38  PHE F CE1 1 
ATOM   7066 C  CE2 . PHE F  1 37  ? 13.397 16.507  1.198   1.00 36.71 ? 38  PHE F CE2 1 
ATOM   7067 C  CZ  . PHE F  1 37  ? 12.823 15.972  0.041   1.00 36.53 ? 38  PHE F CZ  1 
ATOM   7068 N  N   . GLU F  1 38  ? 8.318  20.222  4.292   1.00 38.17 ? 39  GLU F N   1 
ATOM   7069 C  CA  . GLU F  1 38  ? 7.129  20.668  5.015   1.00 39.17 ? 39  GLU F CA  1 
ATOM   7070 C  C   . GLU F  1 38  ? 6.270  21.629  4.197   1.00 37.10 ? 39  GLU F C   1 
ATOM   7071 O  O   . GLU F  1 38  ? 5.239  22.103  4.692   1.00 36.10 ? 39  GLU F O   1 
ATOM   7072 C  CB  . GLU F  1 38  ? 7.537  21.333  6.342   1.00 36.48 ? 39  GLU F CB  1 
ATOM   7073 C  CG  . GLU F  1 38  ? 7.887  20.314  7.424   1.00 43.60 ? 39  GLU F CG  1 
ATOM   7074 C  CD  . GLU F  1 38  ? 7.934  20.901  8.834   1.00 58.59 ? 39  GLU F CD  1 
ATOM   7075 O  OE1 . GLU F  1 38  ? 7.415  22.023  9.058   1.00 57.54 ? 39  GLU F OE1 1 
ATOM   7076 O  OE2 . GLU F  1 38  ? 8.477  20.216  9.733   1.00 64.84 ? 39  GLU F OE2 1 
ATOM   7077 N  N   . ARG F  1 39  ? 6.684  21.952  2.975   1.00 35.06 ? 40  ARG F N   1 
ATOM   7078 C  CA  . ARG F  1 39  ? 5.892  22.838  2.139   1.00 36.23 ? 40  ARG F CA  1 
ATOM   7079 C  C   . ARG F  1 39  ? 4.548  22.205  1.809   1.00 34.44 ? 40  ARG F C   1 
ATOM   7080 O  O   . ARG F  1 39  ? 4.426  20.989  1.644   1.00 32.67 ? 40  ARG F O   1 
ATOM   7081 C  CB  . ARG F  1 39  ? 6.642  23.170  0.860   1.00 33.78 ? 40  ARG F CB  1 
ATOM   7082 C  CG  . ARG F  1 39  ? 7.449  24.401  0.977   1.00 36.80 ? 40  ARG F CG  1 
ATOM   7083 C  CD  . ARG F  1 39  ? 8.740  24.298  0.224   1.00 39.63 ? 40  ARG F CD  1 
ATOM   7084 N  NE  . ARG F  1 39  ? 8.626  23.908  -1.180  1.00 45.27 ? 40  ARG F NE  1 
ATOM   7085 C  CZ  . ARG F  1 39  ? 7.949  24.542  -2.129  1.00 48.94 ? 40  ARG F CZ  1 
ATOM   7086 N  NH1 . ARG F  1 39  ? 7.128  25.523  -1.841  1.00 50.75 ? 40  ARG F NH1 1 
ATOM   7087 N  NH2 . ARG F  1 39  ? 8.090  24.156  -3.404  1.00 53.99 ? 40  ARG F NH2 1 
ATOM   7088 N  N   . ASP F  1 40  ? 3.531  23.056  1.716   1.00 35.19 ? 41  ASP F N   1 
ATOM   7089 C  CA  . ASP F  1 40  ? 2.182  22.579  1.441   1.00 37.43 ? 41  ASP F CA  1 
ATOM   7090 C  C   . ASP F  1 40  ? 2.087  21.858  0.097   1.00 36.39 ? 41  ASP F C   1 
ATOM   7091 O  O   . ASP F  1 40  ? 1.234  20.981  -0.067  1.00 35.53 ? 41  ASP F O   1 
ATOM   7092 C  CB  . ASP F  1 40  ? 1.212  23.759  1.508   1.00 36.89 ? 41  ASP F CB  1 
ATOM   7093 C  CG  . ASP F  1 40  ? 1.221  24.580  0.232   1.00 43.86 ? 41  ASP F CG  1 
ATOM   7094 O  OD1 . ASP F  1 40  ? 2.137  25.428  0.085   1.00 46.08 ? 41  ASP F OD1 1 
ATOM   7095 O  OD2 . ASP F  1 40  ? 0.343  24.358  -0.635  1.00 43.98 ? 41  ASP F OD2 1 
ATOM   7096 N  N   . ASP F  1 41  ? 2.939  22.204  -0.873  1.00 34.40 ? 42  ASP F N   1 
ATOM   7097 C  CA  . ASP F  1 41  ? 2.922  21.542  -2.175  1.00 36.16 ? 42  ASP F CA  1 
ATOM   7098 C  C   . ASP F  1 41  ? 3.965  20.437  -2.291  1.00 34.81 ? 42  ASP F C   1 
ATOM   7099 O  O   . ASP F  1 41  ? 4.233  19.973  -3.405  1.00 33.40 ? 42  ASP F O   1 
ATOM   7100 C  CB  . ASP F  1 41  ? 3.108  22.555  -3.315  1.00 34.32 ? 42  ASP F CB  1 
ATOM   7101 C  CG  . ASP F  1 41  ? 4.452  23.313  -3.235  1.00 45.77 ? 42  ASP F CG  1 
ATOM   7102 O  OD1 . ASP F  1 41  ? 5.205  23.118  -2.255  1.00 39.38 ? 42  ASP F OD1 1 
ATOM   7103 O  OD2 . ASP F  1 41  ? 4.756  24.115  -4.155  1.00 48.91 ? 42  ASP F OD2 1 
ATOM   7104 N  N   . VAL F  1 42  ? 4.555  20.009  -1.173  1.00 33.64 ? 43  VAL F N   1 
ATOM   7105 C  CA  . VAL F  1 42  ? 5.432  18.841  -1.135  1.00 33.50 ? 43  VAL F CA  1 
ATOM   7106 C  C   . VAL F  1 42  ? 4.853  17.831  -0.135  1.00 34.06 ? 43  VAL F C   1 
ATOM   7107 O  O   . VAL F  1 42  ? 4.513  16.703  -0.506  1.00 34.39 ? 43  VAL F O   1 
ATOM   7108 C  CB  . VAL F  1 42  ? 6.877  19.248  -0.778  1.00 32.61 ? 43  VAL F CB  1 
ATOM   7109 C  CG1 . VAL F  1 42  ? 7.809  18.029  -0.748  1.00 34.13 ? 43  VAL F CG1 1 
ATOM   7110 C  CG2 . VAL F  1 42  ? 7.388  20.313  -1.743  1.00 32.95 ? 43  VAL F CG2 1 
ATOM   7111 N  N   . ALA F  1 43  ? 4.752  18.226  1.140   1.00 33.11 ? 44  ALA F N   1 
ATOM   7112 C  CA  . ALA F  1 43  ? 4.004  17.496  2.171   1.00 37.67 ? 44  ALA F CA  1 
ATOM   7113 C  C   . ALA F  1 43  ? 4.477  16.049  2.317   1.00 36.70 ? 44  ALA F C   1 
ATOM   7114 O  O   . ALA F  1 43  ? 3.702  15.094  2.189   1.00 37.14 ? 44  ALA F O   1 
ATOM   7115 C  CB  . ALA F  1 43  ? 2.493  17.548  1.896   1.00 33.09 ? 44  ALA F CB  1 
ATOM   7116 N  N   . LEU F  1 44  ? 5.772  15.899  2.605   1.00 31.53 ? 45  LEU F N   1 
ATOM   7117 C  CA  . LEU F  1 44  ? 6.380  14.607  2.911   1.00 37.36 ? 45  LEU F CA  1 
ATOM   7118 C  C   . LEU F  1 44  ? 6.883  14.680  4.350   1.00 36.41 ? 45  LEU F C   1 
ATOM   7119 O  O   . LEU F  1 44  ? 8.059  14.991  4.595   1.00 36.26 ? 45  LEU F O   1 
ATOM   7120 C  CB  . LEU F  1 44  ? 7.496  14.260  1.924   1.00 33.89 ? 45  LEU F CB  1 
ATOM   7121 C  CG  . LEU F  1 44  ? 6.992  13.837  0.536   1.00 39.09 ? 45  LEU F CG  1 
ATOM   7122 C  CD1 . LEU F  1 44  ? 8.092  13.883  -0.536  1.00 35.60 ? 45  LEU F CD1 1 
ATOM   7123 C  CD2 . LEU F  1 44  ? 6.347  12.445  0.590   1.00 36.59 ? 45  LEU F CD2 1 
ATOM   7124 N  N   . PRO F  1 45  ? 6.011  14.421  5.332   1.00 40.26 ? 46  PRO F N   1 
ATOM   7125 C  CA  . PRO F  1 45  ? 6.407  14.626  6.738   1.00 41.82 ? 46  PRO F CA  1 
ATOM   7126 C  C   . PRO F  1 45  ? 7.512  13.701  7.222   1.00 40.61 ? 46  PRO F C   1 
ATOM   7127 O  O   . PRO F  1 45  ? 8.290  14.106  8.097   1.00 40.01 ? 46  PRO F O   1 
ATOM   7128 C  CB  . PRO F  1 45  ? 5.094  14.396  7.508   1.00 37.63 ? 46  PRO F CB  1 
ATOM   7129 C  CG  . PRO F  1 45  ? 4.257  13.562  6.584   1.00 40.93 ? 46  PRO F CG  1 
ATOM   7130 C  CD  . PRO F  1 45  ? 4.581  14.083  5.213   1.00 43.23 ? 46  PRO F CD  1 
ATOM   7131 N  N   . GLY F  1 46  ? 7.609  12.477  6.696   1.00 40.90 ? 47  GLY F N   1 
ATOM   7132 C  CA  . GLY F  1 46  ? 8.688  11.589  7.115   1.00 40.46 ? 47  GLY F CA  1 
ATOM   7133 C  C   . GLY F  1 46  ? 10.055 12.087  6.673   1.00 38.34 ? 47  GLY F C   1 
ATOM   7134 O  O   . GLY F  1 46  ? 11.008 12.123  7.461   1.00 33.46 ? 47  GLY F O   1 
ATOM   7135 N  N   . PHE F  1 47  ? 10.173 12.465  5.402   1.00 35.07 ? 48  PHE F N   1 
ATOM   7136 C  CA  . PHE F  1 47  ? 11.413 13.079  4.938   1.00 38.97 ? 48  PHE F CA  1 
ATOM   7137 C  C   . PHE F  1 47  ? 11.754 14.310  5.760   1.00 37.13 ? 48  PHE F C   1 
ATOM   7138 O  O   . PHE F  1 47  ? 12.915 14.510  6.134   1.00 35.02 ? 48  PHE F O   1 
ATOM   7139 C  CB  . PHE F  1 47  ? 11.309 13.445  3.461   1.00 33.62 ? 48  PHE F CB  1 
ATOM   7140 C  CG  . PHE F  1 47  ? 11.456 12.272  2.549   1.00 35.99 ? 48  PHE F CG  1 
ATOM   7141 C  CD1 . PHE F  1 47  ? 10.352 11.530  2.169   1.00 36.55 ? 48  PHE F CD1 1 
ATOM   7142 C  CD2 . PHE F  1 47  ? 12.700 11.886  2.097   1.00 40.24 ? 48  PHE F CD2 1 
ATOM   7143 C  CE1 . PHE F  1 47  ? 10.477 10.436  1.331   1.00 40.83 ? 48  PHE F CE1 1 
ATOM   7144 C  CE2 . PHE F  1 47  ? 12.837 10.783  1.257   1.00 40.53 ? 48  PHE F CE2 1 
ATOM   7145 C  CZ  . PHE F  1 47  ? 11.722 10.061  0.874   1.00 40.44 ? 48  PHE F CZ  1 
ATOM   7146 N  N   . ALA F  1 48  ? 10.751 15.136  6.070   1.00 33.20 ? 49  ALA F N   1 
ATOM   7147 C  CA  . ALA F  1 48  ? 11.018 16.357  6.822   1.00 36.84 ? 49  ALA F CA  1 
ATOM   7148 C  C   . ALA F  1 48  ? 11.590 16.034  8.194   1.00 40.20 ? 49  ALA F C   1 
ATOM   7149 O  O   . ALA F  1 48  ? 12.557 16.667  8.638   1.00 35.16 ? 49  ALA F O   1 
ATOM   7150 C  CB  . ALA F  1 48  ? 9.743  17.190  6.957   1.00 35.26 ? 49  ALA F CB  1 
ATOM   7151 N  N   . LYS F  1 49  ? 11.012 15.040  8.873   1.00 33.48 ? 50  LYS F N   1 
ATOM   7152 C  CA  . LYS F  1 49  ? 11.524 14.647  10.179  1.00 38.48 ? 50  LYS F CA  1 
ATOM   7153 C  C   . LYS F  1 49  ? 12.917 14.036  10.070  1.00 36.57 ? 50  LYS F C   1 
ATOM   7154 O  O   . LYS F  1 49  ? 13.793 14.330  10.885  1.00 37.00 ? 50  LYS F O   1 
ATOM   7155 C  CB  . LYS F  1 49  ? 10.562 13.666  10.842  1.00 43.92 ? 50  LYS F CB  1 
ATOM   7156 C  CG  . LYS F  1 49  ? 10.658 13.656  12.345  1.00 53.08 ? 50  LYS F CG  1 
ATOM   7157 C  CD  . LYS F  1 49  ? 9.609  12.751  12.954  1.00 64.30 ? 50  LYS F CD  1 
ATOM   7158 C  CE  . LYS F  1 49  ? 10.215 11.409  13.336  1.00 66.93 ? 50  LYS F CE  1 
ATOM   7159 N  NZ  . LYS F  1 49  ? 10.232 11.235  14.822  1.00 77.92 ? 50  LYS F NZ  1 
ATOM   7160 N  N   . PHE F  1 50  ? 13.146 13.189  9.069   1.00 32.36 ? 51  PHE F N   1 
ATOM   7161 C  CA  . PHE F  1 50  ? 14.467 12.584  8.927   1.00 36.79 ? 51  PHE F CA  1 
ATOM   7162 C  C   . PHE F  1 50  ? 15.547 13.650  8.750   1.00 35.35 ? 51  PHE F C   1 
ATOM   7163 O  O   . PHE F  1 50  ? 16.599 13.586  9.390   1.00 36.61 ? 51  PHE F O   1 
ATOM   7164 C  CB  . PHE F  1 50  ? 14.487 11.601  7.754   1.00 33.51 ? 51  PHE F CB  1 
ATOM   7165 C  CG  . PHE F  1 50  ? 15.841 10.990  7.514   1.00 37.22 ? 51  PHE F CG  1 
ATOM   7166 C  CD1 . PHE F  1 50  ? 16.289 9.926   8.309   1.00 36.05 ? 51  PHE F CD1 1 
ATOM   7167 C  CD2 . PHE F  1 50  ? 16.678 11.480  6.508   1.00 33.89 ? 51  PHE F CD2 1 
ATOM   7168 C  CE1 . PHE F  1 50  ? 17.563 9.358   8.100   1.00 34.72 ? 51  PHE F CE1 1 
ATOM   7169 C  CE2 . PHE F  1 50  ? 17.936 10.922  6.286   1.00 33.87 ? 51  PHE F CE2 1 
ATOM   7170 C  CZ  . PHE F  1 50  ? 18.386 9.862   7.090   1.00 33.40 ? 51  PHE F CZ  1 
ATOM   7171 N  N   . PHE F  1 51  ? 15.293 14.663  7.916   1.00 34.88 ? 52  PHE F N   1 
ATOM   7172 C  CA  . PHE F  1 51  ? 16.315 15.679  7.683   1.00 36.26 ? 52  PHE F CA  1 
ATOM   7173 C  C   . PHE F  1 51  ? 16.452 16.640  8.859   1.00 36.27 ? 52  PHE F C   1 
ATOM   7174 O  O   . PHE F  1 51  ? 17.556 17.129  9.125   1.00 33.71 ? 52  PHE F O   1 
ATOM   7175 C  CB  . PHE F  1 51  ? 16.019 16.423  6.388   1.00 29.59 ? 52  PHE F CB  1 
ATOM   7176 C  CG  . PHE F  1 51  ? 16.215 15.568  5.177   1.00 34.00 ? 52  PHE F CG  1 
ATOM   7177 C  CD1 . PHE F  1 51  ? 17.395 14.866  5.010   1.00 31.27 ? 52  PHE F CD1 1 
ATOM   7178 C  CD2 . PHE F  1 51  ? 15.212 15.429  4.228   1.00 34.24 ? 52  PHE F CD2 1 
ATOM   7179 C  CE1 . PHE F  1 51  ? 17.588 14.056  3.914   1.00 35.29 ? 52  PHE F CE1 1 
ATOM   7180 C  CE2 . PHE F  1 51  ? 15.399 14.616  3.122   1.00 33.72 ? 52  PHE F CE2 1 
ATOM   7181 C  CZ  . PHE F  1 51  ? 16.591 13.932  2.961   1.00 33.19 ? 52  PHE F CZ  1 
ATOM   7182 N  N   . LYS F  1 52  ? 15.366 16.907  9.588   1.00 32.14 ? 53  LYS F N   1 
ATOM   7183 C  CA  . LYS F  1 52  ? 15.493 17.762  10.764  1.00 39.25 ? 53  LYS F CA  1 
ATOM   7184 C  C   . LYS F  1 52  ? 16.343 17.089  11.834  1.00 40.52 ? 53  LYS F C   1 
ATOM   7185 O  O   . LYS F  1 52  ? 17.188 17.738  12.464  1.00 41.57 ? 53  LYS F O   1 
ATOM   7186 C  CB  . LYS F  1 52  ? 14.113 18.136  11.308  1.00 40.51 ? 53  LYS F CB  1 
ATOM   7187 C  CG  . LYS F  1 52  ? 14.160 18.920  12.615  1.00 44.83 ? 53  LYS F CG  1 
ATOM   7188 C  CD  . LYS F  1 52  ? 14.750 20.321  12.407  1.00 56.81 ? 53  LYS F CD  1 
ATOM   7189 C  CE  . LYS F  1 52  ? 14.401 21.277  13.540  1.00 57.95 ? 53  LYS F CE  1 
ATOM   7190 N  NZ  . LYS F  1 52  ? 12.919 21.448  13.700  1.00 63.35 ? 53  LYS F NZ  1 
ATOM   7191 N  N   . GLU F  1 53  ? 16.152 15.785  12.033  1.00 34.86 ? 54  GLU F N   1 
ATOM   7192 C  CA  . GLU F  1 53  ? 17.040 15.029  12.906  1.00 39.37 ? 54  GLU F CA  1 
ATOM   7193 C  C   . GLU F  1 53  ? 18.494 15.127  12.429  1.00 38.83 ? 54  GLU F C   1 
ATOM   7194 O  O   . GLU F  1 53  ? 19.395 15.422  13.221  1.00 36.05 ? 54  GLU F O   1 
ATOM   7195 C  CB  . GLU F  1 53  ? 16.550 13.574  12.985  1.00 39.73 ? 54  GLU F CB  1 
ATOM   7196 C  CG  . GLU F  1 53  ? 15.321 13.412  13.914  1.00 45.77 ? 54  GLU F CG  1 
ATOM   7197 C  CD  . GLU F  1 53  ? 14.618 12.037  13.843  1.00 63.29 ? 54  GLU F CD  1 
ATOM   7198 O  OE1 . GLU F  1 53  ? 13.514 11.897  14.437  1.00 59.03 ? 54  GLU F OE1 1 
ATOM   7199 O  OE2 . GLU F  1 53  ? 15.140 11.107  13.180  1.00 67.47 ? 54  GLU F OE2 1 
ATOM   7200 N  N   . SER F  1 54  ? 18.737 14.924  11.128  1.00 30.24 ? 55  SER F N   1 
ATOM   7201 C  CA  . SER F  1 54  ? 20.100 15.036  10.609  1.00 38.72 ? 55  SER F CA  1 
ATOM   7202 C  C   . SER F  1 54  ? 20.672 16.440  10.812  1.00 36.94 ? 55  SER F C   1 
ATOM   7203 O  O   . SER F  1 54  ? 21.878 16.597  11.032  1.00 35.57 ? 55  SER F O   1 
ATOM   7204 C  CB  . SER F  1 54  ? 20.148 14.671  9.122   1.00 36.68 ? 55  SER F CB  1 
ATOM   7205 O  OG  . SER F  1 54  ? 19.568 13.404  8.857   1.00 42.64 ? 55  SER F OG  1 
ATOM   7206 N  N   . SER F  1 55  ? 19.831 17.469  10.750  1.00 33.79 ? 56  SER F N   1 
ATOM   7207 C  CA  . SER F  1 55  ? 20.319 18.818  10.998  1.00 35.47 ? 56  SER F CA  1 
ATOM   7208 C  C   . SER F  1 55  ? 20.794 18.981  12.435  1.00 36.60 ? 56  SER F C   1 
ATOM   7209 O  O   . SER F  1 55  ? 21.833 19.608  12.678  1.00 36.57 ? 56  SER F O   1 
ATOM   7210 C  CB  . SER F  1 55  ? 19.234 19.839  10.684  1.00 33.42 ? 56  SER F CB  1 
ATOM   7211 O  OG  . SER F  1 55  ? 19.676 21.113  11.089  1.00 29.76 ? 56  SER F OG  1 
ATOM   7212 N  N   . ASP F  1 56  ? 20.038 18.430  13.393  1.00 35.62 ? 57  ASP F N   1 
ATOM   7213 C  CA  . ASP F  1 56  ? 20.428 18.472  14.799  1.00 35.99 ? 57  ASP F CA  1 
ATOM   7214 C  C   . ASP F  1 56  ? 21.714 17.700  15.040  1.00 39.95 ? 57  ASP F C   1 
ATOM   7215 O  O   . ASP F  1 56  ? 22.556 18.112  15.851  1.00 37.07 ? 57  ASP F O   1 
ATOM   7216 C  CB  . ASP F  1 56  ? 19.324 17.879  15.674  1.00 42.40 ? 57  ASP F CB  1 
ATOM   7217 C  CG  . ASP F  1 56  ? 18.077 18.744  15.724  1.00 49.12 ? 57  ASP F CG  1 
ATOM   7218 O  OD1 . ASP F  1 56  ? 18.155 19.941  15.364  1.00 52.68 ? 57  ASP F OD1 1 
ATOM   7219 O  OD2 . ASP F  1 56  ? 17.013 18.214  16.120  1.00 54.05 ? 57  ASP F OD2 1 
ATOM   7220 N  N   . CYS F  1 57  ? 21.866 16.554  14.371  1.00 36.43 ? 58  CYS F N   1 
ATOM   7221 C  CA  . CYS F  1 57  ? 23.044 15.728  14.603  1.00 37.85 ? 58  CYS F CA  1 
ATOM   7222 C  C   . CYS F  1 57  ? 24.311 16.451  14.162  1.00 38.69 ? 58  CYS F C   1 
ATOM   7223 O  O   . CYS F  1 57  ? 25.325 16.425  14.868  1.00 37.91 ? 58  CYS F O   1 
ATOM   7224 C  CB  . CYS F  1 57  ? 22.895 14.383  13.882  1.00 39.67 ? 58  CYS F CB  1 
ATOM   7225 S  SG  . CYS F  1 57  ? 24.478 13.588  13.455  1.00 64.63 ? 58  CYS F SG  1 
ATOM   7226 N  N   . CYS F  1 58  ? 24.265 17.120  13.002  1.00 35.19 ? 59  CYS F N   1 
ATOM   7227 C  CA  . CYS F  1 58  ? 25.422 17.884  12.537  1.00 36.38 ? 59  CYS F CA  1 
ATOM   7228 C  C   . CYS F  1 58  ? 25.716 19.092  13.427  1.00 37.23 ? 59  CYS F C   1 
ATOM   7229 O  O   . CYS F  1 58  ? 26.884 19.459  13.610  1.00 36.03 ? 59  CYS F O   1 
ATOM   7230 C  CB  . CYS F  1 58  ? 25.205 18.325  11.097  1.00 32.61 ? 59  CYS F CB  1 
ATOM   7231 S  SG  . CYS F  1 58  ? 25.480 16.993  9.911   1.00 49.08 ? 59  CYS F SG  1 
ATOM   7232 N  N   . ARG F  1 59  ? 24.692 19.726  13.994  1.00 30.59 ? 60  ARG F N   1 
ATOM   7233 C  CA  . ARG F  1 59  ? 24.985 20.817  14.910  1.00 36.10 ? 60  ARG F CA  1 
ATOM   7234 C  C   . ARG F  1 59  ? 25.699 20.305  16.155  1.00 36.35 ? 60  ARG F C   1 
ATOM   7235 O  O   . ARG F  1 59  ? 26.632 20.949  16.644  1.00 34.78 ? 60  ARG F O   1 
ATOM   7236 C  CB  . ARG F  1 59  ? 23.712 21.572  15.281  1.00 38.03 ? 60  ARG F CB  1 
ATOM   7237 C  CG  . ARG F  1 59  ? 24.022 22.816  16.085  1.00 41.47 ? 60  ARG F CG  1 
ATOM   7238 C  CD  . ARG F  1 59  ? 22.783 23.616  16.420  1.00 45.71 ? 60  ARG F CD  1 
ATOM   7239 N  NE  . ARG F  1 59  ? 21.795 22.810  17.123  1.00 46.66 ? 60  ARG F NE  1 
ATOM   7240 C  CZ  . ARG F  1 59  ? 20.686 22.345  16.565  1.00 47.26 ? 60  ARG F CZ  1 
ATOM   7241 N  NH1 . ARG F  1 59  ? 20.415 22.562  15.287  1.00 47.37 ? 60  ARG F NH1 1 
ATOM   7242 N  NH2 . ARG F  1 59  ? 19.833 21.638  17.304  1.00 48.00 ? 60  ARG F NH2 1 
ATOM   7243 N  N   . GLU F  1 60  ? 25.297 19.141  16.670  1.00 35.20 ? 61  GLU F N   1 
ATOM   7244 C  CA  . GLU F  1 60  ? 26.000 18.574  17.817  1.00 38.23 ? 61  GLU F CA  1 
ATOM   7245 C  C   . GLU F  1 60  ? 27.442 18.212  17.469  1.00 35.58 ? 61  GLU F C   1 
ATOM   7246 O  O   . GLU F  1 60  ? 28.350 18.474  18.260  1.00 34.68 ? 61  GLU F O   1 
ATOM   7247 C  CB  . GLU F  1 60  ? 25.245 17.363  18.355  1.00 35.86 ? 61  GLU F CB  1 
ATOM   7248 C  CG  . GLU F  1 60  ? 23.882 17.721  18.966  1.00 51.91 ? 61  GLU F CG  1 
ATOM   7249 C  CD  . GLU F  1 60  ? 22.877 16.553  18.952  1.00 66.37 ? 61  GLU F CD  1 
ATOM   7250 O  OE1 . GLU F  1 60  ? 23.229 15.455  19.445  1.00 69.55 ? 61  GLU F OE1 1 
ATOM   7251 O  OE2 . GLU F  1 60  ? 21.727 16.744  18.474  1.00 65.88 ? 61  GLU F OE2 1 
ATOM   7252 N  N   . HIS F  1 61  ? 27.671 17.620  16.287  1.00 30.37 ? 62  HIS F N   1 
ATOM   7253 C  CA  . HIS F  1 61  ? 29.031 17.399  15.795  1.00 35.07 ? 62  HIS F CA  1 
ATOM   7254 C  C   . HIS F  1 61  ? 29.872 18.667  15.871  1.00 34.58 ? 62  HIS F C   1 
ATOM   7255 O  O   . HIS F  1 61  ? 31.032 18.636  16.308  1.00 30.65 ? 62  HIS F O   1 
ATOM   7256 C  CB  . HIS F  1 61  ? 29.017 16.925  14.344  1.00 37.00 ? 62  HIS F CB  1 
ATOM   7257 C  CG  . HIS F  1 61  ? 28.512 15.532  14.157  1.00 46.52 ? 62  HIS F CG  1 
ATOM   7258 N  ND1 . HIS F  1 61  ? 28.308 14.659  15.205  1.00 47.77 ? 62  HIS F ND1 1 
ATOM   7259 C  CD2 . HIS F  1 61  ? 28.166 14.863  13.035  1.00 42.17 ? 62  HIS F CD2 1 
ATOM   7260 C  CE1 . HIS F  1 61  ? 27.853 13.512  14.733  1.00 50.35 ? 62  HIS F CE1 1 
ATOM   7261 N  NE2 . HIS F  1 61  ? 27.753 13.612  13.419  1.00 53.90 ? 62  HIS F NE2 1 
ATOM   7262 N  N   . ALA F  1 62  ? 29.318 19.788  15.401  1.00 29.23 ? 63  ALA F N   1 
ATOM   7263 C  CA  . ALA F  1 62  ? 30.080 21.030  15.438  1.00 32.19 ? 63  ALA F CA  1 
ATOM   7264 C  C   . ALA F  1 62  ? 30.369 21.440  16.873  1.00 32.40 ? 63  ALA F C   1 
ATOM   7265 O  O   . ALA F  1 62  ? 31.462 21.933  17.175  1.00 32.40 ? 63  ALA F O   1 
ATOM   7266 C  CB  . ALA F  1 62  ? 29.337 22.138  14.690  1.00 27.58 ? 63  ALA F CB  1 
ATOM   7267 N  N   . GLN F  1 63  ? 29.415 21.211  17.773  1.00 32.45 ? 64  GLN F N   1 
ATOM   7268 C  CA  . GLN F  1 63  ? 29.564 21.661  19.151  1.00 34.13 ? 64  GLN F CA  1 
ATOM   7269 C  C   . GLN F  1 63  ? 30.573 20.803  19.913  1.00 34.93 ? 64  GLN F C   1 
ATOM   7270 O  O   . GLN F  1 63  ? 31.363 21.324  20.714  1.00 28.85 ? 64  GLN F O   1 
ATOM   7271 C  CB  . GLN F  1 63  ? 28.206 21.640  19.840  1.00 33.93 ? 64  GLN F CB  1 
ATOM   7272 C  CG  . GLN F  1 63  ? 27.511 23.001  19.850  1.00 45.24 ? 64  GLN F CG  1 
ATOM   7273 C  CD  . GLN F  1 63  ? 26.017 22.869  19.981  1.00 49.51 ? 64  GLN F CD  1 
ATOM   7274 O  OE1 . GLN F  1 63  ? 25.533 21.922  20.603  1.00 61.01 ? 64  GLN F OE1 1 
ATOM   7275 N  NE2 . GLN F  1 63  ? 25.278 23.823  19.437  1.00 52.91 ? 64  GLN F NE2 1 
ATOM   7276 N  N   . THR F  1 64  ? 30.544 19.486  19.683  1.00 24.41 ? 65  THR F N   1 
ATOM   7277 C  CA  . THR F  1 64  ? 31.553 18.598  20.242  1.00 32.05 ? 65  THR F CA  1 
ATOM   7278 C  C   . THR F  1 64  ? 32.960 19.008  19.798  1.00 32.92 ? 65  THR F C   1 
ATOM   7279 O  O   . THR F  1 64  ? 33.906 18.976  20.593  1.00 31.99 ? 65  THR F O   1 
ATOM   7280 C  CB  . THR F  1 64  ? 31.236 17.161  19.823  1.00 31.52 ? 65  THR F CB  1 
ATOM   7281 O  OG1 . THR F  1 64  ? 29.919 16.833  20.265  1.00 36.36 ? 65  THR F OG1 1 
ATOM   7282 C  CG2 . THR F  1 64  ? 32.230 16.186  20.419  1.00 33.21 ? 65  THR F CG2 1 
ATOM   7283 N  N   . PHE F  1 65  ? 33.112 19.421  18.537  1.00 27.74 ? 66  PHE F N   1 
ATOM   7284 C  CA  . PHE F  1 65  ? 34.406 19.899  18.069  1.00 29.54 ? 66  PHE F CA  1 
ATOM   7285 C  C   . PHE F  1 65  ? 34.810 21.196  18.757  1.00 30.42 ? 66  PHE F C   1 
ATOM   7286 O  O   . PHE F  1 65  ? 35.989 21.387  19.072  1.00 27.37 ? 66  PHE F O   1 
ATOM   7287 C  CB  . PHE F  1 65  ? 34.375 20.104  16.559  1.00 30.05 ? 66  PHE F CB  1 
ATOM   7288 C  CG  . PHE F  1 65  ? 34.793 18.907  15.781  1.00 31.82 ? 66  PHE F CG  1 
ATOM   7289 C  CD1 . PHE F  1 65  ? 35.939 18.200  16.131  1.00 37.19 ? 66  PHE F CD1 1 
ATOM   7290 C  CD2 . PHE F  1 65  ? 34.043 18.482  14.692  1.00 33.53 ? 66  PHE F CD2 1 
ATOM   7291 C  CE1 . PHE F  1 65  ? 36.336 17.080  15.404  1.00 38.34 ? 66  PHE F CE1 1 
ATOM   7292 C  CE2 . PHE F  1 65  ? 34.426 17.372  13.958  1.00 37.03 ? 66  PHE F CE2 1 
ATOM   7293 C  CZ  . PHE F  1 65  ? 35.583 16.667  14.309  1.00 37.89 ? 66  PHE F CZ  1 
ATOM   7294 N  N   . MET F  1 66  ? 33.868 22.123  18.957  1.00 29.44 ? 67  MET F N   1 
ATOM   7295 C  CA  . MET F  1 66  ? 34.239 23.361  19.635  1.00 32.93 ? 67  MET F CA  1 
ATOM   7296 C  C   . MET F  1 66  ? 34.693 23.082  21.062  1.00 33.06 ? 67  MET F C   1 
ATOM   7297 O  O   . MET F  1 66  ? 35.663 23.686  21.537  1.00 32.59 ? 67  MET F O   1 
ATOM   7298 C  CB  . MET F  1 66  ? 33.089 24.374  19.612  1.00 29.51 ? 67  MET F CB  1 
ATOM   7299 C  CG  . MET F  1 66  ? 32.553 24.693  18.211  1.00 33.35 ? 67  MET F CG  1 
ATOM   7300 S  SD  . MET F  1 66  ? 31.064 25.732  18.162  1.00 36.52 ? 67  MET F SD  1 
ATOM   7301 C  CE  . MET F  1 66  ? 31.643 27.212  18.978  1.00 40.06 ? 67  MET F CE  1 
ATOM   7302 N  N   . LYS F  1 67  ? 34.020 22.148  21.748  1.00 34.68 ? 68  LYS F N   1 
ATOM   7303 C  CA  . LYS F  1 67  ? 34.425 21.764  23.097  1.00 32.29 ? 68  LYS F CA  1 
ATOM   7304 C  C   . LYS F  1 67  ? 35.806 21.120  23.100  1.00 33.45 ? 68  LYS F C   1 
ATOM   7305 O  O   . LYS F  1 67  ? 36.620 21.382  23.992  1.00 31.57 ? 68  LYS F O   1 
ATOM   7306 C  CB  . LYS F  1 67  ? 33.377 20.829  23.717  1.00 31.38 ? 68  LYS F CB  1 
ATOM   7307 C  CG  . LYS F  1 67  ? 33.641 20.404  25.185  1.00 50.86 ? 68  LYS F CG  1 
ATOM   7308 C  CD  . LYS F  1 67  ? 34.229 21.561  26.055  1.00 54.77 ? 68  LYS F CD  1 
ATOM   7309 C  CE  . LYS F  1 67  ? 33.471 22.877  25.848  1.00 57.82 ? 68  LYS F CE  1 
ATOM   7310 N  NZ  . LYS F  1 67  ? 34.315 24.119  25.962  1.00 41.53 ? 68  LYS F NZ  1 
ATOM   7311 N  N   . TYR F  1 68  ? 36.084 20.264  22.118  1.00 30.77 ? 69  TYR F N   1 
ATOM   7312 C  CA  . TYR F  1 68  ? 37.411 19.672  22.010  1.00 31.12 ? 69  TYR F CA  1 
ATOM   7313 C  C   . TYR F  1 68  ? 38.480 20.742  21.868  1.00 29.84 ? 69  TYR F C   1 
ATOM   7314 O  O   . TYR F  1 68  ? 39.510 20.707  22.554  1.00 29.69 ? 69  TYR F O   1 
ATOM   7315 C  CB  . TYR F  1 68  ? 37.456 18.728  20.818  1.00 31.28 ? 69  TYR F CB  1 
ATOM   7316 C  CG  . TYR F  1 68  ? 38.696 17.892  20.831  1.00 32.53 ? 69  TYR F CG  1 
ATOM   7317 C  CD1 . TYR F  1 68  ? 38.769 16.768  21.634  1.00 30.66 ? 69  TYR F CD1 1 
ATOM   7318 C  CD2 . TYR F  1 68  ? 39.799 18.232  20.054  1.00 30.71 ? 69  TYR F CD2 1 
ATOM   7319 C  CE1 . TYR F  1 68  ? 39.897 15.992  21.668  1.00 34.55 ? 69  TYR F CE1 1 
ATOM   7320 C  CE2 . TYR F  1 68  ? 40.941 17.455  20.078  1.00 34.17 ? 69  TYR F CE2 1 
ATOM   7321 C  CZ  . TYR F  1 68  ? 40.980 16.333  20.892  1.00 33.78 ? 69  TYR F CZ  1 
ATOM   7322 O  OH  . TYR F  1 68  ? 42.104 15.549  20.948  1.00 34.75 ? 69  TYR F OH  1 
ATOM   7323 N  N   . GLN F  1 69  ? 38.248 21.705  20.974  1.00 28.23 ? 70  GLN F N   1 
ATOM   7324 C  CA  . GLN F  1 69  ? 39.187 22.804  20.789  1.00 28.55 ? 70  GLN F CA  1 
ATOM   7325 C  C   . GLN F  1 69  ? 39.509 23.479  22.118  1.00 29.53 ? 70  GLN F C   1 
ATOM   7326 O  O   . GLN F  1 69  ? 40.679 23.710  22.435  1.00 31.55 ? 70  GLN F O   1 
ATOM   7327 C  CB  . GLN F  1 69  ? 38.611 23.799  19.772  1.00 31.63 ? 70  GLN F CB  1 
ATOM   7328 C  CG  . GLN F  1 69  ? 39.587 24.836  19.272  1.00 35.08 ? 70  GLN F CG  1 
ATOM   7329 C  CD  . GLN F  1 69  ? 40.403 24.325  18.096  1.00 39.55 ? 70  GLN F CD  1 
ATOM   7330 O  OE1 . GLN F  1 69  ? 41.338 23.547  18.278  1.00 38.15 ? 70  GLN F OE1 1 
ATOM   7331 N  NE2 . GLN F  1 69  ? 40.059 24.767  16.887  1.00 36.45 ? 70  GLN F NE2 1 
ATOM   7332 N  N   . ASN F  1 70  ? 38.486 23.765  22.931  1.00 30.30 ? 71  ASN F N   1 
ATOM   7333 C  CA  . ASN F  1 70  ? 38.741 24.371  24.236  1.00 32.12 ? 71  ASN F CA  1 
ATOM   7334 C  C   . ASN F  1 70  ? 39.479 23.413  25.161  1.00 33.05 ? 71  ASN F C   1 
ATOM   7335 O  O   . ASN F  1 70  ? 40.365 23.837  25.912  1.00 28.17 ? 71  ASN F O   1 
ATOM   7336 C  CB  . ASN F  1 70  ? 37.431 24.826  24.885  1.00 31.43 ? 71  ASN F CB  1 
ATOM   7337 C  CG  . ASN F  1 70  ? 36.967 26.184  24.375  1.00 37.00 ? 71  ASN F CG  1 
ATOM   7338 O  OD1 . ASN F  1 70  ? 37.774 26.984  23.902  1.00 38.60 ? 71  ASN F OD1 1 
ATOM   7339 N  ND2 . ASN F  1 70  ? 35.668 26.454  24.480  1.00 37.23 ? 71  ASN F ND2 1 
ATOM   7340 N  N   . LYS F  1 71  ? 39.129 22.119  25.113  1.00 26.59 ? 72  LYS F N   1 
ATOM   7341 C  CA  . LYS F  1 71  ? 39.724 21.131  26.011  1.00 33.78 ? 72  LYS F CA  1 
ATOM   7342 C  C   . LYS F  1 71  ? 41.229 20.991  25.772  1.00 33.69 ? 72  LYS F C   1 
ATOM   7343 O  O   . LYS F  1 71  ? 42.007 20.849  26.725  1.00 29.61 ? 72  LYS F O   1 
ATOM   7344 C  CB  . LYS F  1 71  ? 39.015 19.786  25.826  1.00 33.64 ? 72  LYS F CB  1 
ATOM   7345 C  CG  . LYS F  1 71  ? 39.022 18.867  27.018  1.00 45.58 ? 72  LYS F CG  1 
ATOM   7346 C  CD  . LYS F  1 71  ? 38.343 17.529  26.673  1.00 50.42 ? 72  LYS F CD  1 
ATOM   7347 C  CE  . LYS F  1 71  ? 36.855 17.710  26.374  1.00 54.82 ? 72  LYS F CE  1 
ATOM   7348 N  NZ  . LYS F  1 71  ? 36.458 17.234  25.005  1.00 46.06 ? 72  LYS F NZ  1 
ATOM   7349 N  N   . ARG F  1 72  ? 41.661 21.045  24.514  1.00 27.81 ? 73  ARG F N   1 
ATOM   7350 C  CA  . ARG F  1 72  ? 43.076 20.915  24.182  1.00 31.08 ? 73  ARG F CA  1 
ATOM   7351 C  C   . ARG F  1 72  ? 43.826 22.239  24.258  1.00 30.98 ? 73  ARG F C   1 
ATOM   7352 O  O   . ARG F  1 72  ? 45.040 22.252  24.058  1.00 27.82 ? 73  ARG F O   1 
ATOM   7353 C  CB  . ARG F  1 72  ? 43.254 20.315  22.774  1.00 25.96 ? 73  ARG F CB  1 
ATOM   7354 C  CG  . ARG F  1 72  ? 42.661 18.931  22.609  1.00 31.41 ? 73  ARG F CG  1 
ATOM   7355 C  CD  . ARG F  1 72  ? 43.362 17.901  23.493  1.00 31.34 ? 73  ARG F CD  1 
ATOM   7356 N  NE  . ARG F  1 72  ? 44.807 17.887  23.294  1.00 35.03 ? 73  ARG F NE  1 
ATOM   7357 C  CZ  . ARG F  1 72  ? 45.427 17.232  22.319  1.00 35.28 ? 73  ARG F CZ  1 
ATOM   7358 N  NH1 . ARG F  1 72  ? 44.758 16.518  21.426  1.00 31.34 ? 73  ARG F NH1 1 
ATOM   7359 N  NH2 . ARG F  1 72  ? 46.751 17.306  22.227  1.00 28.56 ? 73  ARG F NH2 1 
ATOM   7360 N  N   . GLY F  1 73  ? 43.136 23.349  24.507  1.00 32.01 ? 74  GLY F N   1 
ATOM   7361 C  CA  . GLY F  1 73  ? 43.794 24.634  24.589  1.00 31.56 ? 74  GLY F CA  1 
ATOM   7362 C  C   . GLY F  1 73  ? 43.997 25.344  23.272  1.00 33.80 ? 74  GLY F C   1 
ATOM   7363 O  O   . GLY F  1 73  ? 44.867 26.212  23.184  1.00 39.26 ? 74  GLY F O   1 
ATOM   7364 N  N   . GLY F  1 74  ? 43.232 25.001  22.233  1.00 34.95 ? 75  GLY F N   1 
ATOM   7365 C  CA  . GLY F  1 74  ? 43.225 25.793  21.017  1.00 37.50 ? 75  GLY F CA  1 
ATOM   7366 C  C   . GLY F  1 74  ? 42.174 26.909  21.040  1.00 36.31 ? 75  GLY F C   1 
ATOM   7367 O  O   . GLY F  1 74  ? 41.362 27.044  21.955  1.00 37.90 ? 75  GLY F O   1 
ATOM   7368 N  N   . ARG F  1 75  ? 42.183 27.727  19.996  1.00 33.35 ? 76  ARG F N   1 
ATOM   7369 C  CA  . ARG F  1 75  ? 41.214 28.810  19.866  1.00 39.13 ? 76  ARG F CA  1 
ATOM   7370 C  C   . ARG F  1 75  ? 40.194 28.495  18.778  1.00 36.26 ? 76  ARG F C   1 
ATOM   7371 O  O   . ARG F  1 75  ? 40.568 28.154  17.649  1.00 34.09 ? 76  ARG F O   1 
ATOM   7372 C  CB  . ARG F  1 75  ? 41.896 30.152  19.565  1.00 38.26 ? 76  ARG F CB  1 
ATOM   7373 C  CG  . ARG F  1 75  ? 40.997 31.348  19.968  1.00 51.69 ? 76  ARG F CG  1 
ATOM   7374 C  CD  . ARG F  1 75  ? 41.640 32.723  19.727  1.00 58.39 ? 76  ARG F CD  1 
ATOM   7375 N  NE  . ARG F  1 75  ? 42.207 33.295  20.952  1.00 70.06 ? 76  ARG F NE  1 
ATOM   7376 C  CZ  . ARG F  1 75  ? 41.567 33.489  22.104  1.00 69.79 ? 76  ARG F CZ  1 
ATOM   7377 N  NH1 . ARG F  1 75  ? 40.254 33.305  22.223  1.00 58.36 ? 76  ARG F NH1 1 
ATOM   7378 N  NH2 . ARG F  1 75  ? 42.261 33.887  23.170  1.00 72.69 ? 76  ARG F NH2 1 
ATOM   7379 N  N   . ILE F  1 76  ? 38.911 28.625  19.124  1.00 33.94 ? 77  ILE F N   1 
ATOM   7380 C  CA  . ILE F  1 76  ? 37.847 28.525  18.131  1.00 33.94 ? 77  ILE F CA  1 
ATOM   7381 C  C   . ILE F  1 76  ? 37.829 29.794  17.288  1.00 33.60 ? 77  ILE F C   1 
ATOM   7382 O  O   . ILE F  1 76  ? 37.801 30.910  17.821  1.00 36.77 ? 77  ILE F O   1 
ATOM   7383 C  CB  . ILE F  1 76  ? 36.490 28.300  18.820  1.00 31.75 ? 77  ILE F CB  1 
ATOM   7384 C  CG1 . ILE F  1 76  ? 36.518 27.017  19.646  1.00 30.24 ? 77  ILE F CG1 1 
ATOM   7385 C  CG2 . ILE F  1 76  ? 35.359 28.194  17.801  1.00 30.66 ? 77  ILE F CG2 1 
ATOM   7386 C  CD1 . ILE F  1 76  ? 35.601 27.076  20.861  1.00 33.24 ? 77  ILE F CD1 1 
ATOM   7387 N  N   . VAL F  1 77  ? 37.874 29.631  15.970  1.00 31.84 ? 78  VAL F N   1 
ATOM   7388 C  CA  . VAL F  1 77  ? 37.674 30.728  15.032  1.00 28.86 ? 78  VAL F CA  1 
ATOM   7389 C  C   . VAL F  1 77  ? 36.494 30.338  14.153  1.00 32.95 ? 78  VAL F C   1 
ATOM   7390 O  O   . VAL F  1 77  ? 36.602 29.419  13.329  1.00 32.90 ? 78  VAL F O   1 
ATOM   7391 C  CB  . VAL F  1 77  ? 38.922 31.021  14.185  1.00 34.37 ? 78  VAL F CB  1 
ATOM   7392 C  CG1 . VAL F  1 77  ? 38.721 32.302  13.370  1.00 30.18 ? 78  VAL F CG1 1 
ATOM   7393 C  CG2 . VAL F  1 77  ? 40.141 31.167  15.072  1.00 33.35 ? 78  VAL F CG2 1 
ATOM   7394 N  N   . LEU F  1 78  ? 35.368 31.019  14.341  1.00 28.83 ? 79  LEU F N   1 
ATOM   7395 C  CA  . LEU F  1 78  ? 34.172 30.750  13.560  1.00 29.38 ? 79  LEU F CA  1 
ATOM   7396 C  C   . LEU F  1 78  ? 34.240 31.487  12.233  1.00 32.92 ? 79  LEU F C   1 
ATOM   7397 O  O   . LEU F  1 78  ? 34.756 32.606  12.148  1.00 31.99 ? 79  LEU F O   1 
ATOM   7398 C  CB  . LEU F  1 78  ? 32.919 31.163  14.333  1.00 29.56 ? 79  LEU F CB  1 
ATOM   7399 C  CG  . LEU F  1 78  ? 32.763 30.358  15.632  1.00 28.60 ? 79  LEU F CG  1 
ATOM   7400 C  CD1 . LEU F  1 78  ? 31.635 30.914  16.480  1.00 31.79 ? 79  LEU F CD1 1 
ATOM   7401 C  CD2 . LEU F  1 78  ? 32.522 28.879  15.329  1.00 26.80 ? 79  LEU F CD2 1 
ATOM   7402 N  N   . GLN F  1 79  ? 33.744 30.835  11.188  1.00 29.37 ? 80  GLN F N   1 
ATOM   7403 C  CA  . GLN F  1 79  ? 33.692 31.402  9.853   1.00 24.62 ? 80  GLN F CA  1 
ATOM   7404 C  C   . GLN F  1 79  ? 32.243 31.460  9.399   1.00 30.99 ? 80  GLN F C   1 
ATOM   7405 O  O   . GLN F  1 79  ? 31.391 30.716  9.890   1.00 25.68 ? 80  GLN F O   1 
ATOM   7406 C  CB  . GLN F  1 79  ? 34.511 30.565  8.857   1.00 28.56 ? 80  GLN F CB  1 
ATOM   7407 C  CG  . GLN F  1 79  ? 35.990 30.466  9.176   1.00 25.62 ? 80  GLN F CG  1 
ATOM   7408 C  CD  . GLN F  1 79  ? 36.745 31.763  8.855   1.00 32.95 ? 80  GLN F CD  1 
ATOM   7409 O  OE1 . GLN F  1 79  ? 36.334 32.546  7.981   1.00 32.94 ? 80  GLN F OE1 1 
ATOM   7410 N  NE2 . GLN F  1 79  ? 37.854 31.995  9.563   1.00 29.68 ? 80  GLN F NE2 1 
ATOM   7411 N  N   . GLN F  1 80  ? 31.983 32.343  8.438   1.00 29.68 ? 81  GLN F N   1 
ATOM   7412 C  CA  . GLN F  1 80  ? 30.675 32.415  7.807   1.00 25.39 ? 81  GLN F CA  1 
ATOM   7413 C  C   . GLN F  1 80  ? 30.179 31.034  7.386   1.00 27.68 ? 81  GLN F C   1 
ATOM   7414 O  O   . GLN F  1 80  ? 30.951 30.191  6.924   1.00 29.72 ? 81  GLN F O   1 
ATOM   7415 C  CB  . GLN F  1 80  ? 30.750 33.335  6.590   1.00 27.75 ? 81  GLN F CB  1 
ATOM   7416 C  CG  . GLN F  1 80  ? 29.461 33.468  5.776   1.00 28.63 ? 81  GLN F CG  1 
ATOM   7417 C  CD  . GLN F  1 80  ? 29.502 34.736  4.906   1.00 36.82 ? 81  GLN F CD  1 
ATOM   7418 O  OE1 . GLN F  1 80  ? 29.200 35.840  5.384   1.00 31.66 ? 81  GLN F OE1 1 
ATOM   7419 N  NE2 . GLN F  1 80  ? 29.868 34.579  3.632   1.00 28.77 ? 81  GLN F NE2 1 
ATOM   7420 N  N   . ILE F  1 81  ? 28.877 30.813  7.548   1.00 24.12 ? 82  ILE F N   1 
ATOM   7421 C  CA  . ILE F  1 81  ? 28.214 29.607  7.071   1.00 27.21 ? 82  ILE F CA  1 
ATOM   7422 C  C   . ILE F  1 81  ? 27.536 29.950  5.751   1.00 26.57 ? 82  ILE F C   1 
ATOM   7423 O  O   . ILE F  1 81  ? 26.686 30.843  5.694   1.00 25.72 ? 82  ILE F O   1 
ATOM   7424 C  CB  . ILE F  1 81  ? 27.201 29.081  8.101   1.00 28.81 ? 82  ILE F CB  1 
ATOM   7425 C  CG1 . ILE F  1 81  ? 27.847 28.958  9.493   1.00 26.19 ? 82  ILE F CG1 1 
ATOM   7426 C  CG2 . ILE F  1 81  ? 26.621 27.742  7.657   1.00 26.05 ? 82  ILE F CG2 1 
ATOM   7427 C  CD1 . ILE F  1 81  ? 26.782 28.927  10.633  1.00 29.27 ? 82  ILE F CD1 1 
ATOM   7428 N  N   . ALA F  1 82  ? 27.933 29.264  4.687   1.00 31.21 ? 83  ALA F N   1 
ATOM   7429 C  CA  . ALA F  1 82  ? 27.400 29.546  3.361   1.00 31.88 ? 83  ALA F CA  1 
ATOM   7430 C  C   . ALA F  1 82  ? 25.924 29.165  3.287   1.00 36.42 ? 83  ALA F C   1 
ATOM   7431 O  O   . ALA F  1 82  ? 25.460 28.257  3.987   1.00 33.59 ? 83  ALA F O   1 
ATOM   7432 C  CB  . ALA F  1 82  ? 28.182 28.768  2.295   1.00 29.23 ? 83  ALA F CB  1 
ATOM   7433 N  N   . ALA F  1 83  ? 25.187 29.864  2.424   1.00 35.41 ? 84  ALA F N   1 
ATOM   7434 C  CA  . ALA F  1 83  ? 23.821 29.449  2.134   1.00 38.94 ? 84  ALA F CA  1 
ATOM   7435 C  C   . ALA F  1 83  ? 23.852 28.094  1.432   1.00 35.65 ? 84  ALA F C   1 
ATOM   7436 O  O   . ALA F  1 83  ? 24.805 27.805  0.699   1.00 39.82 ? 84  ALA F O   1 
ATOM   7437 C  CB  . ALA F  1 83  ? 23.109 30.488  1.259   1.00 38.54 ? 84  ALA F CB  1 
ATOM   7438 N  N   . PRO F  1 84  ? 22.872 27.224  1.672   1.00 38.18 ? 85  PRO F N   1 
ATOM   7439 C  CA  . PRO F  1 84  ? 22.794 25.971  0.906   1.00 39.31 ? 85  PRO F CA  1 
ATOM   7440 C  C   . PRO F  1 84  ? 22.838 26.251  -0.590  1.00 44.61 ? 85  PRO F C   1 
ATOM   7441 O  O   . PRO F  1 84  ? 22.235 27.214  -1.075  1.00 41.86 ? 85  PRO F O   1 
ATOM   7442 C  CB  . PRO F  1 84  ? 21.444 25.381  1.326   1.00 38.90 ? 85  PRO F CB  1 
ATOM   7443 C  CG  . PRO F  1 84  ? 21.190 25.945  2.677   1.00 37.70 ? 85  PRO F CG  1 
ATOM   7444 C  CD  . PRO F  1 84  ? 21.849 27.300  2.733   1.00 37.47 ? 85  PRO F CD  1 
ATOM   7445 N  N   . SER F  1 85  ? 23.561 25.389  -1.315  1.00 49.19 ? 86  SER F N   1 
ATOM   7446 C  CA  . SER F  1 85  ? 23.794 25.595  -2.746  1.00 55.62 ? 86  SER F CA  1 
ATOM   7447 C  C   . SER F  1 85  ? 22.482 25.669  -3.520  1.00 54.83 ? 86  SER F C   1 
ATOM   7448 O  O   . SER F  1 85  ? 22.287 26.555  -4.361  1.00 58.89 ? 86  SER F O   1 
ATOM   7449 C  CB  . SER F  1 85  ? 24.689 24.475  -3.290  1.00 56.97 ? 86  SER F CB  1 
ATOM   7450 O  OG  . SER F  1 85  ? 23.998 23.231  -3.336  1.00 62.76 ? 86  SER F OG  1 
ATOM   7451 N  N   . MET F  1 86  ? 21.568 24.748  -3.250  1.00 56.45 ? 87  MET F N   1 
ATOM   7452 C  CA  . MET F  1 86  ? 20.225 24.817  -3.801  1.00 59.93 ? 87  MET F CA  1 
ATOM   7453 C  C   . MET F  1 86  ? 19.225 24.728  -2.662  1.00 55.62 ? 87  MET F C   1 
ATOM   7454 O  O   . MET F  1 86  ? 19.568 24.349  -1.539  1.00 56.21 ? 87  MET F O   1 
ATOM   7455 C  CB  . MET F  1 86  ? 19.998 23.717  -4.839  1.00 66.57 ? 87  MET F CB  1 
ATOM   7456 C  CG  . MET F  1 86  ? 19.780 22.327  -4.268  1.00 61.59 ? 87  MET F CG  1 
ATOM   7457 S  SD  . MET F  1 86  ? 19.277 21.224  -5.614  1.00 85.60 ? 87  MET F SD  1 
ATOM   7458 C  CE  . MET F  1 86  ? 20.094 22.022  -7.001  1.00 61.69 ? 87  MET F CE  1 
ATOM   7459 N  N   . GLN F  1 87  ? 17.988 25.127  -2.942  1.00 55.02 ? 88  GLN F N   1 
ATOM   7460 C  CA  . GLN F  1 87  ? 16.982 25.161  -1.890  1.00 53.54 ? 88  GLN F CA  1 
ATOM   7461 C  C   . GLN F  1 87  ? 15.630 24.599  -2.299  1.00 51.40 ? 88  GLN F C   1 
ATOM   7462 O  O   . GLN F  1 87  ? 14.712 24.597  -1.474  1.00 55.29 ? 88  GLN F O   1 
ATOM   7463 C  CB  . GLN F  1 87  ? 16.826 26.589  -1.374  1.00 47.82 ? 88  GLN F CB  1 
ATOM   7464 C  CG  . GLN F  1 87  ? 18.008 26.966  -0.480  1.00 52.22 ? 88  GLN F CG  1 
ATOM   7465 C  CD  . GLN F  1 87  ? 18.020 28.425  -0.097  1.00 48.40 ? 88  GLN F CD  1 
ATOM   7466 O  OE1 . GLN F  1 87  ? 17.034 28.939  0.434   1.00 40.41 ? 88  GLN F OE1 1 
ATOM   7467 N  NE2 . GLN F  1 87  ? 19.138 29.110  -0.374  1.00 43.14 ? 88  GLN F NE2 1 
ATOM   7468 N  N   . GLU F  1 88  ? 15.479 24.139  -3.535  1.00 53.08 ? 89  GLU F N   1 
ATOM   7469 C  CA  . GLU F  1 88  ? 14.370 23.293  -3.960  1.00 52.92 ? 89  GLU F CA  1 
ATOM   7470 C  C   . GLU F  1 88  ? 14.983 21.928  -4.218  1.00 49.23 ? 89  GLU F C   1 
ATOM   7471 O  O   . GLU F  1 88  ? 15.795 21.768  -5.134  1.00 51.91 ? 89  GLU F O   1 
ATOM   7472 C  CB  . GLU F  1 88  ? 13.682 23.846  -5.204  1.00 55.13 ? 89  GLU F CB  1 
ATOM   7473 C  CG  . GLU F  1 88  ? 13.153 25.250  -5.019  1.00 59.41 ? 89  GLU F CG  1 
ATOM   7474 C  CD  . GLU F  1 88  ? 11.700 25.366  -5.411  1.00 71.92 ? 89  GLU F CD  1 
ATOM   7475 O  OE1 . GLU F  1 88  ? 11.371 24.987  -6.560  1.00 75.84 ? 89  GLU F OE1 1 
ATOM   7476 O  OE2 . GLU F  1 88  ? 10.889 25.818  -4.565  1.00 76.08 ? 89  GLU F OE2 1 
ATOM   7477 N  N   . TRP F  1 89  ? 14.632 20.956  -3.396  1.00 43.16 ? 90  TRP F N   1 
ATOM   7478 C  CA  . TRP F  1 89  ? 15.383 19.717  -3.368  1.00 46.14 ? 90  TRP F CA  1 
ATOM   7479 C  C   . TRP F  1 89  ? 14.783 18.624  -4.240  1.00 43.70 ? 90  TRP F C   1 
ATOM   7480 O  O   . TRP F  1 89  ? 15.272 17.494  -4.207  1.00 44.74 ? 90  TRP F O   1 
ATOM   7481 C  CB  . TRP F  1 89  ? 15.528 19.259  -1.925  1.00 40.05 ? 90  TRP F CB  1 
ATOM   7482 C  CG  . TRP F  1 89  ? 16.358 20.226  -1.189  1.00 43.35 ? 90  TRP F CG  1 
ATOM   7483 C  CD1 . TRP F  1 89  ? 15.926 21.278  -0.421  1.00 40.53 ? 90  TRP F CD1 1 
ATOM   7484 C  CD2 . TRP F  1 89  ? 17.786 20.287  -1.191  1.00 43.16 ? 90  TRP F CD2 1 
ATOM   7485 N  NE1 . TRP F  1 89  ? 17.007 21.976  0.070   1.00 38.48 ? 90  TRP F NE1 1 
ATOM   7486 C  CE2 . TRP F  1 89  ? 18.159 21.384  -0.385  1.00 44.66 ? 90  TRP F CE2 1 
ATOM   7487 C  CE3 . TRP F  1 89  ? 18.787 19.511  -1.789  1.00 47.73 ? 90  TRP F CE3 1 
ATOM   7488 C  CZ2 . TRP F  1 89  ? 19.497 21.719  -0.154  1.00 45.52 ? 90  TRP F CZ2 1 
ATOM   7489 C  CZ3 . TRP F  1 89  ? 20.115 19.846  -1.560  1.00 46.02 ? 90  TRP F CZ3 1 
ATOM   7490 C  CH2 . TRP F  1 89  ? 20.456 20.944  -0.754  1.00 47.51 ? 90  TRP F CH2 1 
ATOM   7491 N  N   . GLY F  1 90  ? 13.755 18.929  -5.032  1.00 41.48 ? 91  GLY F N   1 
ATOM   7492 C  CA  . GLY F  1 90  ? 13.242 17.924  -5.957  1.00 41.50 ? 91  GLY F CA  1 
ATOM   7493 C  C   . GLY F  1 90  ? 12.490 16.810  -5.252  1.00 45.65 ? 91  GLY F C   1 
ATOM   7494 O  O   . GLY F  1 90  ? 11.700 17.053  -4.334  1.00 49.46 ? 91  GLY F O   1 
ATOM   7495 N  N   . THR F  1 91  ? 12.731 15.569  -5.684  1.00 42.52 ? 92  THR F N   1 
ATOM   7496 C  CA  . THR F  1 91  ? 12.007 14.426  -5.141  1.00 44.63 ? 92  THR F CA  1 
ATOM   7497 C  C   . THR F  1 91  ? 12.620 13.980  -3.819  1.00 42.68 ? 92  THR F C   1 
ATOM   7498 O  O   . THR F  1 91  ? 13.704 14.419  -3.419  1.00 39.61 ? 92  THR F O   1 
ATOM   7499 C  CB  . THR F  1 91  ? 12.026 13.244  -6.109  1.00 42.35 ? 92  THR F CB  1 
ATOM   7500 O  OG1 . THR F  1 91  ? 13.379 12.847  -6.357  1.00 42.42 ? 92  THR F OG1 1 
ATOM   7501 C  CG2 . THR F  1 91  ? 11.406 13.655  -7.442  1.00 42.32 ? 92  THR F CG2 1 
ATOM   7502 N  N   . GLY F  1 92  ? 11.916 13.077  -3.140  1.00 39.03 ? 93  GLY F N   1 
ATOM   7503 C  CA  . GLY F  1 92  ? 12.494 12.463  -1.959  1.00 40.70 ? 93  GLY F CA  1 
ATOM   7504 C  C   . GLY F  1 92  ? 13.757 11.686  -2.288  1.00 42.81 ? 93  GLY F C   1 
ATOM   7505 O  O   . GLY F  1 92  ? 14.704 11.660  -1.497  1.00 36.76 ? 93  GLY F O   1 
ATOM   7506 N  N   . LEU F  1 93  ? 13.789 11.052  -3.469  1.00 38.40 ? 94  LEU F N   1 
ATOM   7507 C  CA  . LEU F  1 93  ? 14.964 10.292  -3.883  1.00 35.32 ? 94  LEU F CA  1 
ATOM   7508 C  C   . LEU F  1 93  ? 16.168 11.204  -4.100  1.00 40.02 ? 94  LEU F C   1 
ATOM   7509 O  O   . LEU F  1 93  ? 17.285 10.881  -3.678  1.00 37.90 ? 94  LEU F O   1 
ATOM   7510 C  CB  . LEU F  1 93  ? 14.651 9.501   -5.150  1.00 34.51 ? 94  LEU F CB  1 
ATOM   7511 C  CG  . LEU F  1 93  ? 15.772 8.609   -5.684  1.00 41.42 ? 94  LEU F CG  1 
ATOM   7512 C  CD1 . LEU F  1 93  ? 16.265 7.669   -4.590  1.00 34.19 ? 94  LEU F CD1 1 
ATOM   7513 C  CD2 . LEU F  1 93  ? 15.268 7.821   -6.889  1.00 37.99 ? 94  LEU F CD2 1 
ATOM   7514 N  N   . GLU F  1 94  ? 15.953 12.358  -4.735  1.00 37.39 ? 95  GLU F N   1 
ATOM   7515 C  CA  . GLU F  1 94  ? 17.058 13.256  -5.048  1.00 41.39 ? 95  GLU F CA  1 
ATOM   7516 C  C   . GLU F  1 94  ? 17.650 13.889  -3.788  1.00 36.98 ? 95  GLU F C   1 
ATOM   7517 O  O   . GLU F  1 94  ? 18.859 14.121  -3.715  1.00 37.31 ? 95  GLU F O   1 
ATOM   7518 C  CB  . GLU F  1 94  ? 16.574 14.330  -6.009  1.00 41.08 ? 95  GLU F CB  1 
ATOM   7519 C  CG  . GLU F  1 94  ? 16.377 13.816  -7.410  1.00 47.23 ? 95  GLU F CG  1 
ATOM   7520 C  CD  . GLU F  1 94  ? 15.710 14.847  -8.314  1.00 58.69 ? 95  GLU F CD  1 
ATOM   7521 O  OE1 . GLU F  1 94  ? 14.592 15.292  -7.968  1.00 55.96 ? 95  GLU F OE1 1 
ATOM   7522 O  OE2 . GLU F  1 94  ? 16.300 15.208  -9.363  1.00 67.14 ? 95  GLU F OE2 1 
ATOM   7523 N  N   . ALA F  1 95  ? 16.816 14.189  -2.795  1.00 30.62 ? 96  ALA F N   1 
ATOM   7524 C  CA  . ALA F  1 95  ? 17.343 14.693  -1.536  1.00 35.44 ? 96  ALA F CA  1 
ATOM   7525 C  C   . ALA F  1 95  ? 18.184 13.636  -0.822  1.00 38.78 ? 96  ALA F C   1 
ATOM   7526 O  O   . ALA F  1 95  ? 19.263 13.950  -0.303  1.00 36.55 ? 96  ALA F O   1 
ATOM   7527 C  CB  . ALA F  1 95  ? 16.203 15.169  -0.647  1.00 33.42 ? 96  ALA F CB  1 
ATOM   7528 N  N   . LEU F  1 96  ? 17.710 12.380  -0.787  1.00 32.98 ? 97  LEU F N   1 
ATOM   7529 C  CA  . LEU F  1 96  ? 18.500 11.299  -0.204  1.00 33.17 ? 97  LEU F CA  1 
ATOM   7530 C  C   . LEU F  1 96  ? 19.824 11.133  -0.933  1.00 35.90 ? 97  LEU F C   1 
ATOM   7531 O  O   . LEU F  1 96  ? 20.865 10.913  -0.300  1.00 38.37 ? 97  LEU F O   1 
ATOM   7532 C  CB  . LEU F  1 96  ? 17.723 9.980   -0.233  1.00 33.84 ? 97  LEU F CB  1 
ATOM   7533 C  CG  . LEU F  1 96  ? 16.629 9.840   0.821   1.00 41.04 ? 97  LEU F CG  1 
ATOM   7534 C  CD1 . LEU F  1 96  ? 15.871 8.523   0.667   1.00 36.03 ? 97  LEU F CD1 1 
ATOM   7535 C  CD2 . LEU F  1 96  ? 17.241 9.976   2.210   1.00 37.68 ? 97  LEU F CD2 1 
ATOM   7536 N  N   . GLN F  1 97  ? 19.808 11.242  -2.263  1.00 36.20 ? 98  GLN F N   1 
ATOM   7537 C  CA  . GLN F  1 97  ? 21.046 11.108  -3.024  1.00 38.43 ? 98  GLN F CA  1 
ATOM   7538 C  C   . GLN F  1 97  ? 21.998 12.267  -2.738  1.00 39.01 ? 98  GLN F C   1 
ATOM   7539 O  O   . GLN F  1 97  ? 23.213 12.063  -2.609  1.00 37.88 ? 98  GLN F O   1 
ATOM   7540 C  CB  . GLN F  1 97  ? 20.735 10.983  -4.520  1.00 42.93 ? 98  GLN F CB  1 
ATOM   7541 C  CG  . GLN F  1 97  ? 20.124 9.613   -4.880  1.00 43.97 ? 98  GLN F CG  1 
ATOM   7542 C  CD  . GLN F  1 97  ? 19.465 9.560   -6.257  1.00 49.29 ? 98  GLN F CD  1 
ATOM   7543 O  OE1 . GLN F  1 97  ? 18.997 10.573  -6.786  1.00 47.66 ? 98  GLN F OE1 1 
ATOM   7544 N  NE2 . GLN F  1 97  ? 19.432 8.365   -6.846  1.00 44.86 ? 98  GLN F NE2 1 
ATOM   7545 N  N   . ALA F  1 98  ? 21.469 13.484  -2.592  1.00 38.49 ? 99  ALA F N   1 
ATOM   7546 C  CA  . ALA F  1 98  ? 22.316 14.606  -2.192  1.00 35.25 ? 99  ALA F CA  1 
ATOM   7547 C  C   . ALA F  1 98  ? 22.861 14.412  -0.782  1.00 36.59 ? 99  ALA F C   1 
ATOM   7548 O  O   . ALA F  1 98  ? 23.998 14.795  -0.497  1.00 40.47 ? 99  ALA F O   1 
ATOM   7549 C  CB  . ALA F  1 98  ? 21.537 15.918  -2.282  1.00 30.49 ? 99  ALA F CB  1 
ATOM   7550 N  N   . ALA F  1 99  ? 22.067 13.817  0.117   1.00 35.64 ? 100 ALA F N   1 
ATOM   7551 C  CA  . ALA F  1 99  ? 22.533 13.612  1.488   1.00 33.76 ? 100 ALA F CA  1 
ATOM   7552 C  C   . ALA F  1 99  ? 23.579 12.503  1.560   1.00 37.46 ? 100 ALA F C   1 
ATOM   7553 O  O   . ALA F  1 99  ? 24.511 12.569  2.368   1.00 36.87 ? 100 ALA F O   1 
ATOM   7554 C  CB  . ALA F  1 99  ? 21.357 13.294  2.408   1.00 34.20 ? 100 ALA F CB  1 
ATOM   7555 N  N   . LEU F  1 100 ? 23.440 11.471  0.728   1.00 38.28 ? 101 LEU F N   1 
ATOM   7556 C  CA  . LEU F  1 100 ? 24.480 10.449  0.654   1.00 40.53 ? 101 LEU F CA  1 
ATOM   7557 C  C   . LEU F  1 100 ? 25.813 11.059  0.225   1.00 38.14 ? 101 LEU F C   1 
ATOM   7558 O  O   . LEU F  1 100 ? 26.857 10.790  0.828   1.00 35.42 ? 101 LEU F O   1 
ATOM   7559 C  CB  . LEU F  1 100 ? 24.054 9.345   -0.311  1.00 34.51 ? 101 LEU F CB  1 
ATOM   7560 C  CG  . LEU F  1 100 ? 25.088 8.247   -0.520  1.00 38.80 ? 101 LEU F CG  1 
ATOM   7561 C  CD1 . LEU F  1 100 ? 25.393 7.548   0.808   1.00 37.04 ? 101 LEU F CD1 1 
ATOM   7562 C  CD2 . LEU F  1 100 ? 24.603 7.254   -1.569  1.00 33.59 ? 101 LEU F CD2 1 
ATOM   7563 N  N   . ASP F  1 101 ? 25.792 11.897  -0.812  1.00 34.83 ? 102 ASP F N   1 
ATOM   7564 C  CA  . ASP F  1 101 ? 27.017 12.539  -1.275  1.00 37.07 ? 102 ASP F CA  1 
ATOM   7565 C  C   . ASP F  1 101 ? 27.610 13.432  -0.189  1.00 38.56 ? 102 ASP F C   1 
ATOM   7566 O  O   . ASP F  1 101 ? 28.823 13.425  0.036   1.00 39.33 ? 102 ASP F O   1 
ATOM   7567 C  CB  . ASP F  1 101 ? 26.722 13.330  -2.553  1.00 41.43 ? 102 ASP F CB  1 
ATOM   7568 C  CG  . ASP F  1 101 ? 27.824 14.336  -2.902  1.00 61.37 ? 102 ASP F CG  1 
ATOM   7569 O  OD1 . ASP F  1 101 ? 28.842 13.925  -3.511  1.00 69.76 ? 102 ASP F OD1 1 
ATOM   7570 O  OD2 . ASP F  1 101 ? 27.672 15.543  -2.581  1.00 68.81 ? 102 ASP F OD2 1 
ATOM   7571 N  N   . LEU F  1 102 ? 26.757 14.169  0.530   1.00 38.62 ? 103 LEU F N   1 
ATOM   7572 C  CA  . LEU F  1 102 ? 27.212 15.033  1.616   1.00 39.14 ? 103 LEU F CA  1 
ATOM   7573 C  C   . LEU F  1 102 ? 27.880 14.229  2.734   1.00 38.67 ? 103 LEU F C   1 
ATOM   7574 O  O   . LEU F  1 102 ? 28.938 14.620  3.250   1.00 33.97 ? 103 LEU F O   1 
ATOM   7575 C  CB  . LEU F  1 102 ? 26.019 15.831  2.147   1.00 37.38 ? 103 LEU F CB  1 
ATOM   7576 C  CG  . LEU F  1 102 ? 26.146 16.946  3.189   1.00 40.35 ? 103 LEU F CG  1 
ATOM   7577 C  CD1 . LEU F  1 102 ? 26.476 16.390  4.570   1.00 48.25 ? 103 LEU F CD1 1 
ATOM   7578 C  CD2 . LEU F  1 102 ? 27.187 17.967  2.759   1.00 44.27 ? 103 LEU F CD2 1 
ATOM   7579 N  N   . GLU F  1 103 ? 27.258 13.120  3.153   1.00 36.00 ? 104 GLU F N   1 
ATOM   7580 C  CA  . GLU F  1 103 ? 27.851 12.329  4.235   1.00 38.85 ? 104 GLU F CA  1 
ATOM   7581 C  C   . GLU F  1 103 ? 29.167 11.685  3.803   1.00 36.86 ? 104 GLU F C   1 
ATOM   7582 O  O   . GLU F  1 103 ? 30.076 11.529  4.623   1.00 33.07 ? 104 GLU F O   1 
ATOM   7583 C  CB  . GLU F  1 103 ? 26.861 11.271  4.725   1.00 37.81 ? 104 GLU F CB  1 
ATOM   7584 C  CG  . GLU F  1 103 ? 25.603 11.874  5.362   1.00 47.47 ? 104 GLU F CG  1 
ATOM   7585 C  CD  . GLU F  1 103 ? 25.856 12.474  6.747   1.00 55.44 ? 104 GLU F CD  1 
ATOM   7586 O  OE1 . GLU F  1 103 ? 26.548 11.827  7.560   1.00 61.22 ? 104 GLU F OE1 1 
ATOM   7587 O  OE2 . GLU F  1 103 ? 25.380 13.598  7.024   1.00 59.92 ? 104 GLU F OE2 1 
ATOM   7588 N  N   . LYS F  1 104 ? 29.305 11.349  2.517   1.00 33.26 ? 105 LYS F N   1 
ATOM   7589 C  CA  . LYS F  1 104 ? 30.573 10.812  2.030   1.00 36.85 ? 105 LYS F CA  1 
ATOM   7590 C  C   . LYS F  1 104 ? 31.664 11.877  2.008   1.00 33.58 ? 105 LYS F C   1 
ATOM   7591 O  O   . LYS F  1 104 ? 32.818 11.578  2.325   1.00 32.13 ? 105 LYS F O   1 
ATOM   7592 C  CB  . LYS F  1 104 ? 30.380 10.196  0.648   1.00 31.48 ? 105 LYS F CB  1 
ATOM   7593 C  CG  . LYS F  1 104 ? 29.718 8.842   0.735   1.00 34.82 ? 105 LYS F CG  1 
ATOM   7594 C  CD  . LYS F  1 104 ? 29.122 8.420   -0.579  1.00 42.55 ? 105 LYS F CD  1 
ATOM   7595 C  CE  . LYS F  1 104 ? 29.627 7.053   -1.001  1.00 39.57 ? 105 LYS F CE  1 
ATOM   7596 N  NZ  . LYS F  1 104 ? 29.145 6.800   -2.402  1.00 48.31 ? 105 LYS F NZ  1 
ATOM   7597 N  N   . GLN F  1 105 ? 31.314 13.122  1.654   1.00 32.85 ? 106 GLN F N   1 
ATOM   7598 C  CA  . GLN F  1 105 ? 32.259 14.239  1.735   1.00 37.14 ? 106 GLN F CA  1 
ATOM   7599 C  C   . GLN F  1 105 ? 32.702 14.487  3.169   1.00 35.77 ? 106 GLN F C   1 
ATOM   7600 O  O   . GLN F  1 105 ? 33.885 14.745  3.431   1.00 35.42 ? 106 GLN F O   1 
ATOM   7601 C  CB  . GLN F  1 105 ? 31.625 15.522  1.199   1.00 39.05 ? 106 GLN F CB  1 
ATOM   7602 C  CG  . GLN F  1 105 ? 31.667 15.751  -0.282  1.00 48.18 ? 106 GLN F CG  1 
ATOM   7603 C  CD  . GLN F  1 105 ? 30.805 16.962  -0.672  1.00 62.20 ? 106 GLN F CD  1 
ATOM   7604 O  OE1 . GLN F  1 105 ? 30.843 18.019  -0.019  1.00 61.48 ? 106 GLN F OE1 1 
ATOM   7605 N  NE2 . GLN F  1 105 ? 30.008 16.801  -1.726  1.00 59.27 ? 106 GLN F NE2 1 
ATOM   7606 N  N   . VAL F  1 106 ? 31.752 14.483  4.109   1.00 32.45 ? 107 VAL F N   1 
ATOM   7607 C  CA  . VAL F  1 106 ? 32.121 14.684  5.508   1.00 33.56 ? 107 VAL F CA  1 
ATOM   7608 C  C   . VAL F  1 106 ? 33.054 13.572  5.962   1.00 35.05 ? 107 VAL F C   1 
ATOM   7609 O  O   . VAL F  1 106 ? 34.073 13.824  6.616   1.00 34.97 ? 107 VAL F O   1 
ATOM   7610 C  CB  . VAL F  1 106 ? 30.870 14.779  6.395   1.00 36.77 ? 107 VAL F CB  1 
ATOM   7611 C  CG1 . VAL F  1 106 ? 31.273 14.856  7.879   1.00 39.51 ? 107 VAL F CG1 1 
ATOM   7612 C  CG2 . VAL F  1 106 ? 30.043 15.995  6.000   1.00 37.72 ? 107 VAL F CG2 1 
ATOM   7613 N  N   . ASN F  1 107 ? 32.748 12.332  5.571   1.00 33.97 ? 108 ASN F N   1 
ATOM   7614 C  CA  . ASN F  1 107 ? 33.578 11.191  5.944   1.00 33.94 ? 108 ASN F CA  1 
ATOM   7615 C  C   . ASN F  1 107 ? 35.007 11.349  5.430   1.00 35.75 ? 108 ASN F C   1 
ATOM   7616 O  O   . ASN F  1 107 ? 35.971 11.152  6.183   1.00 30.44 ? 108 ASN F O   1 
ATOM   7617 C  CB  . ASN F  1 107 ? 32.954 9.901   5.408   1.00 33.20 ? 108 ASN F CB  1 
ATOM   7618 C  CG  . ASN F  1 107 ? 33.525 8.658   6.066   1.00 36.61 ? 108 ASN F CG  1 
ATOM   7619 O  OD1 . ASN F  1 107 ? 33.881 8.681   7.245   1.00 36.03 ? 108 ASN F OD1 1 
ATOM   7620 N  ND2 . ASN F  1 107 ? 33.599 7.559   5.311   1.00 39.86 ? 108 ASN F ND2 1 
ATOM   7621 N  N   . GLN F  1 108 ? 35.164 11.694  4.143   1.00 33.20 ? 109 GLN F N   1 
ATOM   7622 C  CA  . GLN F  1 108 ? 36.501 11.871  3.576   1.00 35.41 ? 109 GLN F CA  1 
ATOM   7623 C  C   . GLN F  1 108 ? 37.287 12.943  4.323   1.00 38.53 ? 109 GLN F C   1 
ATOM   7624 O  O   . GLN F  1 108 ? 38.499 12.811  4.524   1.00 40.67 ? 109 GLN F O   1 
ATOM   7625 C  CB  . GLN F  1 108 ? 36.406 12.233  2.091   1.00 41.48 ? 109 GLN F CB  1 
ATOM   7626 C  CG  . GLN F  1 108 ? 37.682 11.964  1.275   1.00 43.85 ? 109 GLN F CG  1 
ATOM   7627 C  CD  . GLN F  1 108 ? 38.282 10.552  1.509   1.00 59.83 ? 109 GLN F CD  1 
ATOM   7628 O  OE1 . GLN F  1 108 ? 37.708 9.531   1.088   1.00 58.68 ? 109 GLN F OE1 1 
ATOM   7629 N  NE2 . GLN F  1 108 ? 39.462 10.503  2.149   1.00 58.31 ? 109 GLN F NE2 1 
ATOM   7630 N  N   . SER F  1 109 ? 36.621 14.016  4.732   1.00 31.58 ? 110 SER F N   1 
ATOM   7631 C  CA  . SER F  1 109 ? 37.332 15.071  5.433   1.00 35.32 ? 110 SER F CA  1 
ATOM   7632 C  C   . SER F  1 109 ? 37.760 14.615  6.834   1.00 36.13 ? 110 SER F C   1 
ATOM   7633 O  O   . SER F  1 109 ? 38.861 14.946  7.292   1.00 34.00 ? 110 SER F O   1 
ATOM   7634 C  CB  . SER F  1 109 ? 36.457 16.321  5.478   1.00 34.63 ? 110 SER F CB  1 
ATOM   7635 O  OG  . SER F  1 109 ? 36.845 17.168  6.539   1.00 48.12 ? 110 SER F OG  1 
ATOM   7636 N  N   . LEU F  1 110 ? 36.926 13.823  7.517   1.00 34.83 ? 111 LEU F N   1 
ATOM   7637 C  CA  . LEU F  1 110 ? 37.324 13.282  8.819   1.00 34.53 ? 111 LEU F CA  1 
ATOM   7638 C  C   . LEU F  1 110 ? 38.504 12.320  8.688   1.00 31.43 ? 111 LEU F C   1 
ATOM   7639 O  O   . LEU F  1 110 ? 39.359 12.255  9.576   1.00 33.28 ? 111 LEU F O   1 
ATOM   7640 C  CB  . LEU F  1 110 ? 36.142 12.569  9.484   1.00 30.20 ? 111 LEU F CB  1 
ATOM   7641 C  CG  . LEU F  1 110 ? 34.925 13.416  9.846   1.00 38.78 ? 111 LEU F CG  1 
ATOM   7642 C  CD1 . LEU F  1 110 ? 33.761 12.502  10.162  1.00 38.29 ? 111 LEU F CD1 1 
ATOM   7643 C  CD2 . LEU F  1 110 ? 35.217 14.336  11.022  1.00 34.91 ? 111 LEU F CD2 1 
ATOM   7644 N  N   . LEU F  1 111 ? 38.550 11.542  7.603   1.00 31.95 ? 112 LEU F N   1 
ATOM   7645 C  CA  . LEU F  1 111 ? 39.657 10.610  7.413   1.00 36.31 ? 112 LEU F CA  1 
ATOM   7646 C  C   . LEU F  1 111 ? 40.958 11.359  7.140   1.00 31.40 ? 112 LEU F C   1 
ATOM   7647 O  O   . LEU F  1 111 ? 42.026 10.943  7.604   1.00 34.59 ? 112 LEU F O   1 
ATOM   7648 C  CB  . LEU F  1 111 ? 39.344 9.631   6.274   1.00 33.80 ? 112 LEU F CB  1 
ATOM   7649 C  CG  . LEU F  1 111 ? 38.248 8.577   6.467   1.00 36.95 ? 112 LEU F CG  1 
ATOM   7650 C  CD1 . LEU F  1 111 ? 37.927 7.873   5.137   1.00 36.00 ? 112 LEU F CD1 1 
ATOM   7651 C  CD2 . LEU F  1 111 ? 38.677 7.566   7.511   1.00 36.46 ? 112 LEU F CD2 1 
ATOM   7652 N  N   . GLU F  1 112 ? 40.885 12.466  6.391   1.00 33.66 ? 113 GLU F N   1 
ATOM   7653 C  CA  . GLU F  1 112 ? 42.042 13.348  6.251   1.00 36.79 ? 113 GLU F CA  1 
ATOM   7654 C  C   . GLU F  1 112 ? 42.465 13.913  7.598   1.00 35.18 ? 113 GLU F C   1 
ATOM   7655 O  O   . GLU F  1 112 ? 43.657 13.960  7.910   1.00 38.19 ? 113 GLU F O   1 
ATOM   7656 C  CB  . GLU F  1 112 ? 41.737 14.484  5.279   1.00 35.66 ? 113 GLU F CB  1 
ATOM   7657 C  CG  . GLU F  1 112 ? 41.749 14.068  3.818   1.00 48.23 ? 113 GLU F CG  1 
ATOM   7658 C  CD  . GLU F  1 112 ? 41.171 15.151  2.895   1.00 67.80 ? 113 GLU F CD  1 
ATOM   7659 O  OE1 . GLU F  1 112 ? 41.661 16.308  2.930   1.00 69.96 ? 113 GLU F OE1 1 
ATOM   7660 O  OE2 . GLU F  1 112 ? 40.233 14.843  2.123   1.00 69.20 ? 113 GLU F OE2 1 
ATOM   7661 N  N   . LEU F  1 113 ? 41.500 14.350  8.411   1.00 34.60 ? 114 LEU F N   1 
ATOM   7662 C  CA  . LEU F  1 113 ? 41.834 14.819  9.753   1.00 36.26 ? 114 LEU F CA  1 
ATOM   7663 C  C   . LEU F  1 113 ? 42.512 13.719  10.559  1.00 37.02 ? 114 LEU F C   1 
ATOM   7664 O  O   . LEU F  1 113 ? 43.538 13.960  11.210  1.00 36.33 ? 114 LEU F O   1 
ATOM   7665 C  CB  . LEU F  1 113 ? 40.576 15.329  10.464  1.00 34.70 ? 114 LEU F CB  1 
ATOM   7666 C  CG  . LEU F  1 113 ? 40.783 16.075  11.792  1.00 37.69 ? 114 LEU F CG  1 
ATOM   7667 C  CD1 . LEU F  1 113 ? 42.086 16.860  11.800  1.00 37.50 ? 114 LEU F CD1 1 
ATOM   7668 C  CD2 . LEU F  1 113 ? 39.618 17.013  12.064  1.00 39.83 ? 114 LEU F CD2 1 
ATOM   7669 N  N   . HIS F  1 114 ? 41.977 12.494  10.499  1.00 35.97 ? 115 HIS F N   1 
ATOM   7670 C  CA  . HIS F  1 114 ? 42.572 11.397  11.254  1.00 33.94 ? 115 HIS F CA  1 
ATOM   7671 C  C   . HIS F  1 114 ? 44.004 11.158  10.805  1.00 37.97 ? 115 HIS F C   1 
ATOM   7672 O  O   . HIS F  1 114 ? 44.909 10.992  11.631  1.00 37.30 ? 115 HIS F O   1 
ATOM   7673 C  CB  . HIS F  1 114 ? 41.737 10.126  11.090  1.00 32.54 ? 115 HIS F CB  1 
ATOM   7674 C  CG  . HIS F  1 114 ? 42.182 8.991   11.962  1.00 34.87 ? 115 HIS F CG  1 
ATOM   7675 N  ND1 . HIS F  1 114 ? 43.244 8.171   11.638  1.00 34.63 ? 115 HIS F ND1 1 
ATOM   7676 C  CD2 . HIS F  1 114 ? 41.700 8.532   13.142  1.00 31.98 ? 115 HIS F CD2 1 
ATOM   7677 C  CE1 . HIS F  1 114 ? 43.397 7.260   12.583  1.00 35.11 ? 115 HIS F CE1 1 
ATOM   7678 N  NE2 . HIS F  1 114 ? 42.472 7.457   13.508  1.00 31.89 ? 115 HIS F NE2 1 
ATOM   7679 N  N   . SER F  1 115 ? 44.227 11.147  9.490   1.00 35.38 ? 116 SER F N   1 
ATOM   7680 C  CA  . SER F  1 115 ? 45.563 10.880  8.972   1.00 36.77 ? 116 SER F CA  1 
ATOM   7681 C  C   . SER F  1 115 ? 46.538 11.975  9.388   1.00 38.90 ? 116 SER F C   1 
ATOM   7682 O  O   . SER F  1 115 ? 47.701 11.695  9.693   1.00 41.04 ? 116 SER F O   1 
ATOM   7683 C  CB  . SER F  1 115 ? 45.508 10.731  7.449   1.00 38.12 ? 116 SER F CB  1 
ATOM   7684 O  OG  . SER F  1 115 ? 46.733 11.095  6.853   1.00 49.57 ? 116 SER F OG  1 
ATOM   7685 N  N   . THR F  1 116 ? 46.069 13.226  9.433   1.00 41.30 ? 117 THR F N   1 
ATOM   7686 C  CA  . THR F  1 116 ? 46.881 14.332  9.943   1.00 41.70 ? 117 THR F CA  1 
ATOM   7687 C  C   . THR F  1 116 ? 47.273 14.098  11.404  1.00 44.53 ? 117 THR F C   1 
ATOM   7688 O  O   . THR F  1 116 ? 48.449 14.204  11.770  1.00 46.05 ? 117 THR F O   1 
ATOM   7689 C  CB  . THR F  1 116 ? 46.099 15.646  9.817   1.00 47.89 ? 117 THR F CB  1 
ATOM   7690 O  OG1 . THR F  1 116 ? 46.017 16.039  8.443   1.00 45.96 ? 117 THR F OG1 1 
ATOM   7691 C  CG2 . THR F  1 116 ? 46.778 16.772  10.626  1.00 46.48 ? 117 THR F CG2 1 
ATOM   7692 N  N   . ALA F  1 117 ? 46.283 13.801  12.257  1.00 41.46 ? 118 ALA F N   1 
ATOM   7693 C  CA  . ALA F  1 117 ? 46.545 13.549  13.672  1.00 38.20 ? 118 ALA F CA  1 
ATOM   7694 C  C   . ALA F  1 117 ? 47.502 12.380  13.859  1.00 39.87 ? 118 ALA F C   1 
ATOM   7695 O  O   . ALA F  1 117 ? 48.329 12.386  14.774  1.00 37.53 ? 118 ALA F O   1 
ATOM   7696 C  CB  . ALA F  1 117 ? 45.234 13.274  14.404  1.00 29.45 ? 118 ALA F CB  1 
ATOM   7697 N  N   . SER F  1 118 ? 47.391 11.364  13.005  1.00 39.78 ? 119 SER F N   1 
ATOM   7698 C  CA  . SER F  1 118 ? 48.292 10.219  13.076  1.00 42.30 ? 119 SER F CA  1 
ATOM   7699 C  C   . SER F  1 118 ? 49.731 10.636  12.809  1.00 42.89 ? 119 SER F C   1 
ATOM   7700 O  O   . SER F  1 118 ? 50.645 10.262  13.553  1.00 41.45 ? 119 SER F O   1 
ATOM   7701 C  CB  . SER F  1 118 ? 47.850 9.158   12.070  1.00 38.76 ? 119 SER F CB  1 
ATOM   7702 O  OG  . SER F  1 118 ? 46.934 8.263   12.667  1.00 50.26 ? 119 SER F OG  1 
ATOM   7703 N  N   . GLY F  1 119 ? 49.949 11.415  11.739  1.00 45.98 ? 120 GLY F N   1 
ATOM   7704 C  CA  . GLY F  1 119 ? 51.297 11.833  11.382  1.00 44.33 ? 120 GLY F CA  1 
ATOM   7705 C  C   . GLY F  1 119 ? 51.969 12.691  12.439  1.00 45.25 ? 120 GLY F C   1 
ATOM   7706 O  O   . GLY F  1 119 ? 53.193 12.663  12.581  1.00 45.80 ? 120 GLY F O   1 
ATOM   7707 N  N   . ASN F  1 120 ? 51.191 13.460  13.194  1.00 41.12 ? 121 ASN F N   1 
ATOM   7708 C  CA  . ASN F  1 120 ? 51.740 14.256  14.287  1.00 42.96 ? 121 ASN F CA  1 
ATOM   7709 C  C   . ASN F  1 120 ? 51.780 13.503  15.620  1.00 43.58 ? 121 ASN F C   1 
ATOM   7710 O  O   . ASN F  1 120 ? 52.161 14.096  16.638  1.00 49.74 ? 121 ASN F O   1 
ATOM   7711 C  CB  . ASN F  1 120 ? 50.940 15.556  14.436  1.00 44.09 ? 121 ASN F CB  1 
ATOM   7712 C  CG  . ASN F  1 120 ? 51.116 16.486  13.242  1.00 50.05 ? 121 ASN F CG  1 
ATOM   7713 O  OD1 . ASN F  1 120 ? 52.208 16.582  12.673  1.00 50.71 ? 121 ASN F OD1 1 
ATOM   7714 N  ND2 . ASN F  1 120 ? 50.047 17.174  12.859  1.00 48.00 ? 121 ASN F ND2 1 
ATOM   7715 N  N   . ASN F  1 121 ? 51.410 12.218  15.630  1.00 40.47 ? 122 ASN F N   1 
ATOM   7716 C  CA  . ASN F  1 121 ? 51.317 11.390  16.837  1.00 37.12 ? 122 ASN F CA  1 
ATOM   7717 C  C   . ASN F  1 121 ? 50.466 12.061  17.923  1.00 39.04 ? 122 ASN F C   1 
ATOM   7718 O  O   . ASN F  1 121 ? 50.921 12.321  19.035  1.00 36.76 ? 122 ASN F O   1 
ATOM   7719 C  CB  . ASN F  1 121 ? 52.710 11.030  17.370  1.00 41.18 ? 122 ASN F CB  1 
ATOM   7720 C  CG  . ASN F  1 121 ? 53.619 10.462  16.283  1.00 45.03 ? 122 ASN F CG  1 
ATOM   7721 O  OD1 . ASN F  1 121 ? 54.557 11.119  15.831  1.00 48.09 ? 122 ASN F OD1 1 
ATOM   7722 N  ND2 . ASN F  1 121 ? 53.325 9.252   15.844  1.00 36.31 ? 122 ASN F ND2 1 
ATOM   7723 N  N   . ASP F  1 122 ? 49.193 12.320  17.582  1.00 36.31 ? 123 ASP F N   1 
ATOM   7724 C  CA  . ASP F  1 122 ? 48.210 12.837  18.528  1.00 33.63 ? 123 ASP F CA  1 
ATOM   7725 C  C   . ASP F  1 122 ? 47.183 11.749  18.826  1.00 33.75 ? 123 ASP F C   1 
ATOM   7726 O  O   . ASP F  1 122 ? 46.080 11.772  18.264  1.00 35.03 ? 123 ASP F O   1 
ATOM   7727 C  CB  . ASP F  1 122 ? 47.497 14.070  17.967  1.00 34.28 ? 123 ASP F CB  1 
ATOM   7728 C  CG  . ASP F  1 122 ? 46.806 14.909  19.062  1.00 44.65 ? 123 ASP F CG  1 
ATOM   7729 O  OD1 . ASP F  1 122 ? 46.347 14.329  20.084  1.00 39.99 ? 123 ASP F OD1 1 
ATOM   7730 O  OD2 . ASP F  1 122 ? 46.650 16.147  18.860  1.00 40.17 ? 123 ASP F OD2 1 
ATOM   7731 N  N   . PRO F  1 123 ? 47.483 10.788  19.699  1.00 33.51 ? 124 PRO F N   1 
ATOM   7732 C  CA  . PRO F  1 123 ? 46.508 9.716   19.952  1.00 34.33 ? 124 PRO F CA  1 
ATOM   7733 C  C   . PRO F  1 123 ? 45.226 10.200  20.618  1.00 36.70 ? 124 PRO F C   1 
ATOM   7734 O  O   . PRO F  1 123 ? 44.186 9.541   20.455  1.00 34.35 ? 124 PRO F O   1 
ATOM   7735 C  CB  . PRO F  1 123 ? 47.274 8.746   20.862  1.00 34.86 ? 124 PRO F CB  1 
ATOM   7736 C  CG  . PRO F  1 123 ? 48.226 9.637   21.606  1.00 35.02 ? 124 PRO F CG  1 
ATOM   7737 C  CD  . PRO F  1 123 ? 48.629 10.723  20.624  1.00 34.90 ? 124 PRO F CD  1 
ATOM   7738 N  N   . HIS F  1 124 ? 45.256 11.312  21.369  1.00 35.17 ? 125 HIS F N   1 
ATOM   7739 C  CA  . HIS F  1 124 ? 44.005 11.815  21.928  1.00 36.12 ? 125 HIS F CA  1 
ATOM   7740 C  C   . HIS F  1 124 ? 43.053 12.231  20.812  1.00 35.66 ? 125 HIS F C   1 
ATOM   7741 O  O   . HIS F  1 124 ? 41.841 12.003  20.898  1.00 35.15 ? 125 HIS F O   1 
ATOM   7742 C  CB  . HIS F  1 124 ? 44.257 12.984  22.884  1.00 33.25 ? 125 HIS F CB  1 
ATOM   7743 C  CG  . HIS F  1 124 ? 43.055 13.357  23.707  1.00 39.21 ? 125 HIS F CG  1 
ATOM   7744 N  ND1 . HIS F  1 124 ? 42.119 14.283  23.292  1.00 36.22 ? 125 HIS F ND1 1 
ATOM   7745 C  CD2 . HIS F  1 124 ? 42.635 12.924  24.921  1.00 38.97 ? 125 HIS F CD2 1 
ATOM   7746 C  CE1 . HIS F  1 124 ? 41.178 14.403  24.211  1.00 34.11 ? 125 HIS F CE1 1 
ATOM   7747 N  NE2 . HIS F  1 124 ? 41.465 13.589  25.208  1.00 42.00 ? 125 HIS F NE2 1 
ATOM   7748 N  N   . LEU F  1 125 ? 43.588 12.817  19.739  1.00 32.87 ? 126 LEU F N   1 
ATOM   7749 C  CA  . LEU F  1 125 ? 42.724 13.265  18.656  1.00 33.86 ? 126 LEU F CA  1 
ATOM   7750 C  C   . LEU F  1 125 ? 42.265 12.101  17.773  1.00 33.36 ? 126 LEU F C   1 
ATOM   7751 O  O   . LEU F  1 125 ? 41.100 12.066  17.362  1.00 30.72 ? 126 LEU F O   1 
ATOM   7752 C  CB  . LEU F  1 125 ? 43.437 14.344  17.838  1.00 34.51 ? 126 LEU F CB  1 
ATOM   7753 C  CG  . LEU F  1 125 ? 42.748 14.873  16.581  1.00 35.10 ? 126 LEU F CG  1 
ATOM   7754 C  CD1 . LEU F  1 125 ? 41.332 15.363  16.882  1.00 31.66 ? 126 LEU F CD1 1 
ATOM   7755 C  CD2 . LEU F  1 125 ? 43.598 15.982  15.959  1.00 32.90 ? 126 LEU F CD2 1 
ATOM   7756 N  N   . THR F  1 126 ? 43.142 11.132  17.476  1.00 30.17 ? 127 THR F N   1 
ATOM   7757 C  CA  . THR F  1 126 ? 42.680 9.979   16.693  1.00 36.23 ? 127 THR F CA  1 
ATOM   7758 C  C   . THR F  1 126 ? 41.584 9.215   17.435  1.00 36.73 ? 127 THR F C   1 
ATOM   7759 O  O   . THR F  1 126 ? 40.622 8.749   16.817  1.00 35.46 ? 127 THR F O   1 
ATOM   7760 C  CB  . THR F  1 126 ? 43.837 9.029   16.336  1.00 32.53 ? 127 THR F CB  1 
ATOM   7761 O  OG1 . THR F  1 126 ? 44.479 8.555   17.527  1.00 35.10 ? 127 THR F OG1 1 
ATOM   7762 C  CG2 . THR F  1 126 ? 44.864 9.715   15.432  1.00 35.52 ? 127 THR F CG2 1 
ATOM   7763 N  N   . LYS F  1 127 ? 41.698 9.102   18.764  1.00 33.32 ? 128 LYS F N   1 
ATOM   7764 C  CA  . LYS F  1 127 ? 40.659 8.446   19.557  1.00 40.17 ? 128 LYS F CA  1 
ATOM   7765 C  C   . LYS F  1 127 ? 39.315 9.165   19.435  1.00 39.89 ? 128 LYS F C   1 
ATOM   7766 O  O   . LYS F  1 127 ? 38.279 8.525   19.229  1.00 34.50 ? 128 LYS F O   1 
ATOM   7767 C  CB  . LYS F  1 127 ? 41.099 8.367   21.019  1.00 43.60 ? 128 LYS F CB  1 
ATOM   7768 C  CG  . LYS F  1 127 ? 40.052 7.835   21.976  1.00 43.46 ? 128 LYS F CG  1 
ATOM   7769 C  CD  . LYS F  1 127 ? 39.752 8.848   23.057  1.00 49.29 ? 128 LYS F CD  1 
ATOM   7770 C  CE  . LYS F  1 127 ? 39.079 8.211   24.293  1.00 58.36 ? 128 LYS F CE  1 
ATOM   7771 N  NZ  . LYS F  1 127 ? 38.044 7.172   23.959  1.00 58.68 ? 128 LYS F NZ  1 
ATOM   7772 N  N   . LEU F  1 128 ? 39.319 10.500  19.568  1.00 35.10 ? 129 LEU F N   1 
ATOM   7773 C  CA  . LEU F  1 128 ? 38.100 11.294  19.411  1.00 33.53 ? 129 LEU F CA  1 
ATOM   7774 C  C   . LEU F  1 128 ? 37.435 11.051  18.056  1.00 37.84 ? 129 LEU F C   1 
ATOM   7775 O  O   . LEU F  1 128 ? 36.227 10.805  17.983  1.00 35.27 ? 129 LEU F O   1 
ATOM   7776 C  CB  . LEU F  1 128 ? 38.420 12.781  19.571  1.00 36.79 ? 129 LEU F CB  1 
ATOM   7777 C  CG  . LEU F  1 128 ? 37.260 13.705  19.170  1.00 41.32 ? 129 LEU F CG  1 
ATOM   7778 C  CD1 . LEU F  1 128 ? 36.317 13.828  20.349  1.00 34.09 ? 129 LEU F CD1 1 
ATOM   7779 C  CD2 . LEU F  1 128 ? 37.719 15.086  18.672  1.00 35.67 ? 129 LEU F CD2 1 
ATOM   7780 N  N   . LEU F  1 129 ? 38.203 11.143  16.965  1.00 35.41 ? 130 LEU F N   1 
ATOM   7781 C  CA  . LEU F  1 129 ? 37.620 10.958  15.640  1.00 36.53 ? 130 LEU F CA  1 
ATOM   7782 C  C   . LEU F  1 129 ? 37.075 9.545   15.477  1.00 40.19 ? 130 LEU F C   1 
ATOM   7783 O  O   . LEU F  1 129 ? 36.006 9.347   14.890  1.00 40.89 ? 130 LEU F O   1 
ATOM   7784 C  CB  . LEU F  1 129 ? 38.652 11.279  14.556  1.00 31.53 ? 130 LEU F CB  1 
ATOM   7785 C  CG  . LEU F  1 129 ? 39.197 12.714  14.546  1.00 37.85 ? 130 LEU F CG  1 
ATOM   7786 C  CD1 . LEU F  1 129 ? 40.398 12.823  13.608  1.00 34.98 ? 130 LEU F CD1 1 
ATOM   7787 C  CD2 . LEU F  1 129 ? 38.131 13.777  14.180  1.00 32.23 ? 130 LEU F CD2 1 
ATOM   7788 N  N   . GLU F  1 130 ? 37.778 8.555   16.022  1.00 38.20 ? 131 GLU F N   1 
ATOM   7789 C  CA  . GLU F  1 130 ? 37.307 7.177   15.943  1.00 42.86 ? 131 GLU F CA  1 
ATOM   7790 C  C   . GLU F  1 130 ? 36.016 6.987   16.730  1.00 44.93 ? 131 GLU F C   1 
ATOM   7791 O  O   . GLU F  1 130 ? 35.033 6.442   16.210  1.00 47.29 ? 131 GLU F O   1 
ATOM   7792 C  CB  . GLU F  1 130 ? 38.385 6.223   16.455  1.00 38.91 ? 131 GLU F CB  1 
ATOM   7793 C  CG  . GLU F  1 130 ? 39.382 5.816   15.398  1.00 42.31 ? 131 GLU F CG  1 
ATOM   7794 C  CD  . GLU F  1 130 ? 40.626 5.175   15.989  1.00 47.21 ? 131 GLU F CD  1 
ATOM   7795 O  OE1 . GLU F  1 130 ? 40.482 4.313   16.890  1.00 57.38 ? 131 GLU F OE1 1 
ATOM   7796 O  OE2 . GLU F  1 130 ? 41.746 5.520   15.543  1.00 43.68 ? 131 GLU F OE2 1 
ATOM   7797 N  N   . ASP F  1 131 ? 35.997 7.434   17.987  1.00 44.13 ? 132 ASP F N   1 
ATOM   7798 C  CA  . ASP F  1 131 ? 34.874 7.120   18.869  1.00 49.44 ? 132 ASP F CA  1 
ATOM   7799 C  C   . ASP F  1 131 ? 33.639 7.974   18.593  1.00 49.14 ? 132 ASP F C   1 
ATOM   7800 O  O   . ASP F  1 131 ? 32.516 7.483   18.746  1.00 49.42 ? 132 ASP F O   1 
ATOM   7801 C  CB  . ASP F  1 131 ? 35.294 7.272   20.332  1.00 47.45 ? 132 ASP F CB  1 
ATOM   7802 C  CG  . ASP F  1 131 ? 36.270 6.183   20.779  1.00 62.25 ? 132 ASP F CG  1 
ATOM   7803 O  OD1 . ASP F  1 131 ? 36.612 5.299   19.951  1.00 59.89 ? 132 ASP F OD1 1 
ATOM   7804 O  OD2 . ASP F  1 131 ? 36.687 6.208   21.965  1.00 67.15 ? 132 ASP F OD2 1 
ATOM   7805 N  N   . GLU F  1 132 ? 33.815 9.234   18.172  1.00 45.53 ? 133 GLU F N   1 
ATOM   7806 C  CA  . GLU F  1 132 ? 32.718 10.189  18.105  1.00 46.56 ? 133 GLU F CA  1 
ATOM   7807 C  C   . GLU F  1 132 ? 32.309 10.579  16.692  1.00 48.54 ? 133 GLU F C   1 
ATOM   7808 O  O   . GLU F  1 132 ? 31.265 11.226  16.528  1.00 49.14 ? 133 GLU F O   1 
ATOM   7809 C  CB  . GLU F  1 132 ? 33.075 11.468  18.878  1.00 49.73 ? 133 GLU F CB  1 
ATOM   7810 C  CG  . GLU F  1 132 ? 33.248 11.281  20.388  1.00 59.83 ? 133 GLU F CG  1 
ATOM   7811 C  CD  . GLU F  1 132 ? 32.027 11.735  21.188  1.00 71.22 ? 133 GLU F CD  1 
ATOM   7812 O  OE1 . GLU F  1 132 ? 30.896 11.296  20.857  1.00 74.92 ? 133 GLU F OE1 1 
ATOM   7813 O  OE2 . GLU F  1 132 ? 32.200 12.539  22.138  1.00 70.21 ? 133 GLU F OE2 1 
ATOM   7814 N  N   . TYR F  1 133 ? 33.079 10.212  15.670  1.00 41.84 ? 134 TYR F N   1 
ATOM   7815 C  CA  . TYR F  1 133 ? 32.757 10.699  14.333  1.00 40.96 ? 134 TYR F CA  1 
ATOM   7816 C  C   . TYR F  1 133 ? 32.765 9.604   13.272  1.00 39.97 ? 134 TYR F C   1 
ATOM   7817 O  O   . TYR F  1 133 ? 31.782 9.448   12.547  1.00 40.58 ? 134 TYR F O   1 
ATOM   7818 C  CB  . TYR F  1 133 ? 33.724 11.819  13.941  1.00 36.63 ? 134 TYR F CB  1 
ATOM   7819 C  CG  . TYR F  1 133 ? 33.505 13.080  14.736  1.00 43.73 ? 134 TYR F CG  1 
ATOM   7820 C  CD1 . TYR F  1 133 ? 32.492 13.975  14.391  1.00 40.72 ? 134 TYR F CD1 1 
ATOM   7821 C  CD2 . TYR F  1 133 ? 34.283 13.363  15.856  1.00 41.09 ? 134 TYR F CD2 1 
ATOM   7822 C  CE1 . TYR F  1 133 ? 32.267 15.127  15.127  1.00 39.21 ? 134 TYR F CE1 1 
ATOM   7823 C  CE2 . TYR F  1 133 ? 34.066 14.522  16.608  1.00 43.25 ? 134 TYR F CE2 1 
ATOM   7824 C  CZ  . TYR F  1 133 ? 33.055 15.396  16.234  1.00 41.99 ? 134 TYR F CZ  1 
ATOM   7825 O  OH  . TYR F  1 133 ? 32.833 16.542  16.960  1.00 37.83 ? 134 TYR F OH  1 
ATOM   7826 N  N   . LEU F  1 134 ? 33.865 8.852   13.166  1.00 40.09 ? 135 LEU F N   1 
ATOM   7827 C  CA  . LEU F  1 134 ? 34.002 7.885   12.079  1.00 40.46 ? 135 LEU F CA  1 
ATOM   7828 C  C   . LEU F  1 134 ? 32.926 6.815   12.149  1.00 36.53 ? 135 LEU F C   1 
ATOM   7829 O  O   . LEU F  1 134 ? 32.313 6.484   11.128  1.00 39.16 ? 135 LEU F O   1 
ATOM   7830 C  CB  . LEU F  1 134 ? 35.398 7.262   12.095  1.00 36.17 ? 135 LEU F CB  1 
ATOM   7831 C  CG  . LEU F  1 134 ? 36.450 8.302   11.672  1.00 41.66 ? 135 LEU F CG  1 
ATOM   7832 C  CD1 . LEU F  1 134 ? 37.853 7.739   11.698  1.00 43.73 ? 135 LEU F CD1 1 
ATOM   7833 C  CD2 . LEU F  1 134 ? 36.138 8.836   10.286  1.00 38.75 ? 135 LEU F CD2 1 
ATOM   7834 N  N   . GLU F  1 135 ? 32.660 6.280   13.342  1.00 39.35 ? 136 GLU F N   1 
ATOM   7835 C  CA  . GLU F  1 135 ? 31.615 5.270   13.464  1.00 44.03 ? 136 GLU F CA  1 
ATOM   7836 C  C   . GLU F  1 135 ? 30.245 5.811   13.049  1.00 42.99 ? 136 GLU F C   1 
ATOM   7837 O  O   . GLU F  1 135 ? 29.517 5.163   12.281  1.00 40.82 ? 136 GLU F O   1 
ATOM   7838 C  CB  . GLU F  1 135 ? 31.581 4.711   14.881  1.00 46.60 ? 136 GLU F CB  1 
ATOM   7839 C  CG  . GLU F  1 135 ? 30.842 3.379   14.935  1.00 58.04 ? 136 GLU F CG  1 
ATOM   7840 C  CD  . GLU F  1 135 ? 31.487 2.362   15.867  1.00 70.89 ? 136 GLU F CD  1 
ATOM   7841 O  OE1 . GLU F  1 135 ? 31.098 2.301   17.062  1.00 68.59 ? 136 GLU F OE1 1 
ATOM   7842 O  OE2 . GLU F  1 135 ? 32.356 1.593   15.383  1.00 66.89 ? 136 GLU F OE2 1 
ATOM   7843 N  N   . GLU F  1 136 ? 29.868 6.992   13.546  1.00 41.85 ? 137 GLU F N   1 
ATOM   7844 C  CA  . GLU F  1 136 ? 28.563 7.545   13.187  1.00 49.32 ? 137 GLU F CA  1 
ATOM   7845 C  C   . GLU F  1 136 ? 28.474 7.831   11.690  1.00 45.13 ? 137 GLU F C   1 
ATOM   7846 O  O   . GLU F  1 136 ? 27.434 7.591   11.073  1.00 43.17 ? 137 GLU F O   1 
ATOM   7847 C  CB  . GLU F  1 136 ? 28.272 8.813   13.997  1.00 53.01 ? 137 GLU F CB  1 
ATOM   7848 C  CG  . GLU F  1 136 ? 26.797 9.325   13.940  1.00 66.63 ? 137 GLU F CG  1 
ATOM   7849 C  CD  . GLU F  1 136 ? 25.757 8.240   13.543  1.00 72.04 ? 137 GLU F CD  1 
ATOM   7850 O  OE1 . GLU F  1 136 ? 25.513 7.308   14.346  1.00 79.88 ? 137 GLU F OE1 1 
ATOM   7851 O  OE2 . GLU F  1 136 ? 25.145 8.338   12.449  1.00 64.62 ? 137 GLU F OE2 1 
ATOM   7852 N  N   . GLN F  1 137 ? 29.560 8.322   11.087  1.00 38.37 ? 138 GLN F N   1 
ATOM   7853 C  CA  . GLN F  1 137 ? 29.562 8.585   9.651   1.00 38.61 ? 138 GLN F CA  1 
ATOM   7854 C  C   . GLN F  1 137 ? 29.261 7.319   8.856   1.00 39.11 ? 138 GLN F C   1 
ATOM   7855 O  O   . GLN F  1 137 ? 28.432 7.328   7.941   1.00 37.18 ? 138 GLN F O   1 
ATOM   7856 C  CB  . GLN F  1 137 ? 30.912 9.174   9.242   1.00 38.99 ? 138 GLN F CB  1 
ATOM   7857 C  CG  . GLN F  1 137 ? 30.837 10.322  8.254   1.00 46.02 ? 138 GLN F CG  1 
ATOM   7858 C  CD  . GLN F  1 137 ? 29.755 11.357  8.594   1.00 42.93 ? 138 GLN F CD  1 
ATOM   7859 O  OE1 . GLN F  1 137 ? 29.550 11.734  9.756   1.00 40.59 ? 138 GLN F OE1 1 
ATOM   7860 N  NE2 . GLN F  1 137 ? 29.057 11.811  7.568   1.00 44.52 ? 138 GLN F NE2 1 
ATOM   7861 N  N   . VAL F  1 138 ? 29.912 6.207   9.211   1.00 32.42 ? 139 VAL F N   1 
ATOM   7862 C  CA  . VAL F  1 138 ? 29.731 4.975   8.455   1.00 38.11 ? 139 VAL F CA  1 
ATOM   7863 C  C   . VAL F  1 138 ? 28.320 4.429   8.637   1.00 36.05 ? 139 VAL F C   1 
ATOM   7864 O  O   . VAL F  1 138 ? 27.741 3.879   7.694   1.00 35.08 ? 139 VAL F O   1 
ATOM   7865 C  CB  . VAL F  1 138 ? 30.805 3.943   8.853   1.00 39.61 ? 139 VAL F CB  1 
ATOM   7866 C  CG1 . VAL F  1 138 ? 30.350 2.532   8.549   1.00 37.58 ? 139 VAL F CG1 1 
ATOM   7867 C  CG2 . VAL F  1 138 ? 32.096 4.228   8.127   1.00 38.64 ? 139 VAL F CG2 1 
ATOM   7868 N  N   . ASP F  1 139 ? 27.731 4.590   9.822   1.00 36.23 ? 140 ASP F N   1 
ATOM   7869 C  CA  . ASP F  1 139 ? 26.361 4.123   10.024  1.00 42.58 ? 140 ASP F CA  1 
ATOM   7870 C  C   . ASP F  1 139 ? 25.354 4.973   9.261   1.00 38.91 ? 140 ASP F C   1 
ATOM   7871 O  O   . ASP F  1 139 ? 24.391 4.438   8.702   1.00 35.11 ? 140 ASP F O   1 
ATOM   7872 C  CB  . ASP F  1 139 ? 25.997 4.102   11.506  1.00 41.53 ? 140 ASP F CB  1 
ATOM   7873 C  CG  . ASP F  1 139 ? 26.717 2.996   12.261  1.00 55.27 ? 140 ASP F CG  1 
ATOM   7874 O  OD1 . ASP F  1 139 ? 26.927 3.140   13.489  1.00 58.96 ? 140 ASP F OD1 1 
ATOM   7875 O  OD2 . ASP F  1 139 ? 27.125 2.005   11.607  1.00 57.36 ? 140 ASP F OD2 1 
ATOM   7876 N  N   . SER F  1 140 ? 25.537 6.298   9.237   1.00 33.36 ? 141 SER F N   1 
ATOM   7877 C  CA  . SER F  1 140 ? 24.580 7.112   8.497   1.00 35.29 ? 141 SER F CA  1 
ATOM   7878 C  C   . SER F  1 140 ? 24.707 6.893   6.989   1.00 35.02 ? 141 SER F C   1 
ATOM   7879 O  O   . SER F  1 140 ? 23.694 6.908   6.281   1.00 36.58 ? 141 SER F O   1 
ATOM   7880 C  CB  . SER F  1 140 ? 24.721 8.592   8.875   1.00 44.67 ? 141 SER F CB  1 
ATOM   7881 O  OG  . SER F  1 140 ? 25.927 9.156   8.405   1.00 49.12 ? 141 SER F OG  1 
ATOM   7882 N  N   . ILE F  1 141 ? 25.918 6.653   6.474   1.00 34.49 ? 142 ILE F N   1 
ATOM   7883 C  CA  . ILE F  1 141 ? 26.035 6.341   5.053   1.00 31.28 ? 142 ILE F CA  1 
ATOM   7884 C  C   . ILE F  1 141 ? 25.294 5.043   4.741   1.00 34.92 ? 142 ILE F C   1 
ATOM   7885 O  O   . ILE F  1 141 ? 24.541 4.963   3.766   1.00 30.77 ? 142 ILE F O   1 
ATOM   7886 C  CB  . ILE F  1 141 ? 27.514 6.272   4.630   1.00 33.08 ? 142 ILE F CB  1 
ATOM   7887 C  CG1 . ILE F  1 141 ? 28.113 7.684   4.500   1.00 36.80 ? 142 ILE F CG1 1 
ATOM   7888 C  CG2 . ILE F  1 141 ? 27.661 5.521   3.312   1.00 26.37 ? 142 ILE F CG2 1 
ATOM   7889 C  CD1 . ILE F  1 141 ? 29.642 7.733   4.633   1.00 30.58 ? 142 ILE F CD1 1 
ATOM   7890 N  N   . LYS F  1 142 ? 25.465 4.020   5.588   1.00 32.73 ? 143 LYS F N   1 
ATOM   7891 C  CA  . LYS F  1 142 ? 24.761 2.754   5.378   1.00 36.73 ? 143 LYS F CA  1 
ATOM   7892 C  C   . LYS F  1 142 ? 23.249 2.927   5.498   1.00 35.90 ? 143 LYS F C   1 
ATOM   7893 O  O   . LYS F  1 142 ? 22.489 2.331   4.728   1.00 34.31 ? 143 LYS F O   1 
ATOM   7894 C  CB  . LYS F  1 142 ? 25.253 1.701   6.377   1.00 35.50 ? 143 LYS F CB  1 
ATOM   7895 C  CG  . LYS F  1 142 ? 24.401 0.422   6.426   1.00 34.30 ? 143 LYS F CG  1 
ATOM   7896 C  CD  . LYS F  1 142 ? 24.622 -0.403  5.165   1.00 34.04 ? 143 LYS F CD  1 
ATOM   7897 C  CE  . LYS F  1 142 ? 24.403 -1.899  5.404   1.00 41.73 ? 143 LYS F CE  1 
ATOM   7898 N  NZ  . LYS F  1 142 ? 22.964 -2.292  5.386   1.00 36.51 ? 143 LYS F NZ  1 
ATOM   7899 N  N   . LYS F  1 143 ? 22.803 3.723   6.473   1.00 32.28 ? 144 LYS F N   1 
ATOM   7900 C  CA  . LYS F  1 143 ? 21.386 4.029   6.648   1.00 35.33 ? 144 LYS F CA  1 
ATOM   7901 C  C   . LYS F  1 143 ? 20.793 4.664   5.393   1.00 36.36 ? 144 LYS F C   1 
ATOM   7902 O  O   . LYS F  1 143 ? 19.748 4.223   4.893   1.00 34.68 ? 144 LYS F O   1 
ATOM   7903 C  CB  . LYS F  1 143 ? 21.209 4.963   7.856   1.00 36.51 ? 144 LYS F CB  1 
ATOM   7904 C  CG  . LYS F  1 143 ? 19.783 5.449   8.117   1.00 40.59 ? 144 LYS F CG  1 
ATOM   7905 C  CD  . LYS F  1 143 ? 18.780 4.299   8.047   1.00 48.91 ? 144 LYS F CD  1 
ATOM   7906 C  CE  . LYS F  1 143 ? 18.371 3.772   9.436   1.00 60.93 ? 144 LYS F CE  1 
ATOM   7907 N  NZ  . LYS F  1 143 ? 16.926 3.345   9.505   1.00 55.31 ? 144 LYS F NZ  1 
ATOM   7908 N  N   . ILE F  1 144 ? 21.436 5.715   4.880   1.00 28.81 ? 145 ILE F N   1 
ATOM   7909 C  CA  . ILE F  1 144 ? 20.899 6.389   3.702   1.00 36.19 ? 145 ILE F CA  1 
ATOM   7910 C  C   . ILE F  1 144 ? 20.914 5.453   2.502   1.00 36.62 ? 145 ILE F C   1 
ATOM   7911 O  O   . ILE F  1 144 ? 19.973 5.442   1.697   1.00 34.31 ? 145 ILE F O   1 
ATOM   7912 C  CB  . ILE F  1 144 ? 21.672 7.687   3.419   1.00 34.11 ? 145 ILE F CB  1 
ATOM   7913 C  CG1 . ILE F  1 144 ? 21.360 8.718   4.502   1.00 34.25 ? 145 ILE F CG1 1 
ATOM   7914 C  CG2 . ILE F  1 144 ? 21.301 8.238   2.044   1.00 33.96 ? 145 ILE F CG2 1 
ATOM   7915 C  CD1 . ILE F  1 144 ? 22.425 9.779   4.624   1.00 38.57 ? 145 ILE F CD1 1 
ATOM   7916 N  N   . GLY F  1 145 ? 21.979 4.652   2.368   1.00 36.78 ? 146 GLY F N   1 
ATOM   7917 C  CA  . GLY F  1 145 ? 22.037 3.675   1.290   1.00 35.91 ? 146 GLY F CA  1 
ATOM   7918 C  C   . GLY F  1 145 ? 20.871 2.706   1.325   1.00 37.11 ? 146 GLY F C   1 
ATOM   7919 O  O   . GLY F  1 145 ? 20.223 2.460   0.301   1.00 31.21 ? 146 GLY F O   1 
ATOM   7920 N  N   . ASP F  1 146 ? 20.583 2.155   2.515   1.00 35.09 ? 147 ASP F N   1 
ATOM   7921 C  CA  . ASP F  1 146 ? 19.407 1.301   2.712   1.00 38.13 ? 147 ASP F CA  1 
ATOM   7922 C  C   . ASP F  1 146 ? 18.126 2.004   2.269   1.00 36.25 ? 147 ASP F C   1 
ATOM   7923 O  O   . ASP F  1 146 ? 17.283 1.413   1.577   1.00 33.12 ? 147 ASP F O   1 
ATOM   7924 C  CB  . ASP F  1 146 ? 19.278 0.893   4.192   1.00 36.41 ? 147 ASP F CB  1 
ATOM   7925 C  CG  . ASP F  1 146 ? 20.279 -0.196  4.622   1.00 48.17 ? 147 ASP F CG  1 
ATOM   7926 O  OD1 . ASP F  1 146 ? 21.108 -0.658  3.795   1.00 46.62 ? 147 ASP F OD1 1 
ATOM   7927 O  OD2 . ASP F  1 146 ? 20.238 -0.591  5.813   1.00 56.39 ? 147 ASP F OD2 1 
ATOM   7928 N  N   . MET F  1 147 ? 17.953 3.264   2.686   1.00 31.93 ? 148 MET F N   1 
ATOM   7929 C  CA  . MET F  1 147 ? 16.728 3.998   2.378   1.00 34.63 ? 148 MET F CA  1 
ATOM   7930 C  C   . MET F  1 147 ? 16.564 4.192   0.881   1.00 32.10 ? 148 MET F C   1 
ATOM   7931 O  O   . MET F  1 147 ? 15.458 4.065   0.356   1.00 30.88 ? 148 MET F O   1 
ATOM   7932 C  CB  . MET F  1 147 ? 16.734 5.355   3.072   1.00 33.38 ? 148 MET F CB  1 
ATOM   7933 C  CG  . MET F  1 147 ? 16.404 5.297   4.551   1.00 37.41 ? 148 MET F CG  1 
ATOM   7934 S  SD  . MET F  1 147 ? 16.958 6.807   5.401   1.00 43.37 ? 148 MET F SD  1 
ATOM   7935 C  CE  . MET F  1 147 ? 15.596 7.906   5.040   1.00 38.32 ? 148 MET F CE  1 
ATOM   7936 N  N   . ILE F  1 148 ? 17.653 4.521   0.182   1.00 30.70 ? 149 ILE F N   1 
ATOM   7937 C  CA  . ILE F  1 148 ? 17.585 4.715   -1.263  1.00 33.80 ? 149 ILE F CA  1 
ATOM   7938 C  C   . ILE F  1 148 ? 17.134 3.432   -1.955  1.00 36.44 ? 149 ILE F C   1 
ATOM   7939 O  O   . ILE F  1 148 ? 16.301 3.465   -2.867  1.00 34.01 ? 149 ILE F O   1 
ATOM   7940 C  CB  . ILE F  1 148 ? 18.944 5.190   -1.802  1.00 33.19 ? 149 ILE F CB  1 
ATOM   7941 C  CG1 . ILE F  1 148 ? 19.256 6.587   -1.293  1.00 35.77 ? 149 ILE F CG1 1 
ATOM   7942 C  CG2 . ILE F  1 148 ? 18.940 5.188   -3.316  1.00 32.86 ? 149 ILE F CG2 1 
ATOM   7943 C  CD1 . ILE F  1 148 ? 20.641 7.054   -1.674  1.00 33.32 ? 149 ILE F CD1 1 
ATOM   7944 N  N   . THR F  1 149 ? 17.676 2.283   -1.534  1.00 31.12 ? 150 THR F N   1 
ATOM   7945 C  CA  . THR F  1 149 ? 17.251 1.009   -2.104  1.00 31.92 ? 150 THR F CA  1 
ATOM   7946 C  C   . THR F  1 149 ? 15.766 0.756   -1.834  1.00 32.71 ? 150 THR F C   1 
ATOM   7947 O  O   . THR F  1 149 ? 15.007 0.379   -2.736  1.00 33.19 ? 150 THR F O   1 
ATOM   7948 C  CB  . THR F  1 149 ? 18.102 -0.129  -1.528  1.00 35.50 ? 150 THR F CB  1 
ATOM   7949 O  OG1 . THR F  1 149 ? 19.492 0.120   -1.784  1.00 35.45 ? 150 THR F OG1 1 
ATOM   7950 C  CG2 . THR F  1 149 ? 17.710 -1.468  -2.161  1.00 32.56 ? 150 THR F CG2 1 
ATOM   7951 N  N   . LYS F  1 150 ? 15.335 0.961   -0.593  1.00 31.81 ? 151 LYS F N   1 
ATOM   7952 C  CA  . LYS F  1 150 ? 13.940 0.719   -0.257  1.00 37.06 ? 151 LYS F CA  1 
ATOM   7953 C  C   . LYS F  1 150 ? 13.030 1.653   -1.035  1.00 32.80 ? 151 LYS F C   1 
ATOM   7954 O  O   . LYS F  1 150 ? 11.981 1.232   -1.524  1.00 35.72 ? 151 LYS F O   1 
ATOM   7955 C  CB  . LYS F  1 150 ? 13.718 0.883   1.245   1.00 33.62 ? 151 LYS F CB  1 
ATOM   7956 C  CG  . LYS F  1 150 ? 14.254 -0.250  2.080   1.00 34.12 ? 151 LYS F CG  1 
ATOM   7957 C  CD  . LYS F  1 150 ? 14.760 0.298   3.413   1.00 43.84 ? 151 LYS F CD  1 
ATOM   7958 C  CE  . LYS F  1 150 ? 13.813 -0.022  4.561   1.00 48.13 ? 151 LYS F CE  1 
ATOM   7959 N  NZ  . LYS F  1 150 ? 14.563 -0.540  5.753   1.00 52.06 ? 151 LYS F NZ  1 
ATOM   7960 N  N   . LEU F  1 151 ? 13.428 2.917   -1.184  1.00 32.00 ? 152 LEU F N   1 
ATOM   7961 C  CA  . LEU F  1 151 ? 12.589 3.876   -1.898  1.00 34.17 ? 152 LEU F CA  1 
ATOM   7962 C  C   . LEU F  1 151 ? 12.507 3.546   -3.386  1.00 33.96 ? 152 LEU F C   1 
ATOM   7963 O  O   . LEU F  1 151 ? 11.441 3.689   -3.997  1.00 33.77 ? 152 LEU F O   1 
ATOM   7964 C  CB  . LEU F  1 151 ? 13.107 5.307   -1.678  1.00 33.57 ? 152 LEU F CB  1 
ATOM   7965 C  CG  . LEU F  1 151 ? 12.374 6.429   -2.434  1.00 35.90 ? 152 LEU F CG  1 
ATOM   7966 C  CD1 . LEU F  1 151 ? 10.881 6.343   -2.183  1.00 32.90 ? 152 LEU F CD1 1 
ATOM   7967 C  CD2 . LEU F  1 151 ? 12.904 7.841   -2.068  1.00 35.73 ? 152 LEU F CD2 1 
ATOM   7968 N  N   . LYS F  1 152 ? 13.609 3.093   -3.993  1.00 32.22 ? 153 LYS F N   1 
ATOM   7969 C  CA  . LYS F  1 152 ? 13.531 2.681   -5.396  1.00 37.30 ? 153 LYS F CA  1 
ATOM   7970 C  C   . LYS F  1 152 ? 12.621 1.466   -5.567  1.00 34.65 ? 153 LYS F C   1 
ATOM   7971 O  O   . LYS F  1 152 ? 11.904 1.355   -6.568  1.00 37.11 ? 153 LYS F O   1 
ATOM   7972 C  CB  . LYS F  1 152 ? 14.922 2.386   -5.952  1.00 36.73 ? 153 LYS F CB  1 
ATOM   7973 C  CG  . LYS F  1 152 ? 15.678 3.612   -6.419  1.00 34.73 ? 153 LYS F CG  1 
ATOM   7974 C  CD  . LYS F  1 152 ? 17.144 3.283   -6.544  1.00 35.42 ? 153 LYS F CD  1 
ATOM   7975 C  CE  . LYS F  1 152 ? 17.915 4.442   -7.137  1.00 38.26 ? 153 LYS F CE  1 
ATOM   7976 N  NZ  . LYS F  1 152 ? 19.358 4.079   -7.283  1.00 43.73 ? 153 LYS F NZ  1 
ATOM   7977 N  N   . ARG F  1 153 ? 12.633 0.548   -4.599  1.00 32.37 ? 154 ARG F N   1 
ATOM   7978 C  CA  . ARG F  1 153 ? 11.738 -0.604  -4.663  1.00 38.04 ? 154 ARG F CA  1 
ATOM   7979 C  C   . ARG F  1 153 ? 10.282 -0.167  -4.540  1.00 37.99 ? 154 ARG F C   1 
ATOM   7980 O  O   . ARG F  1 153 ? 9.450  -0.485  -5.396  1.00 38.69 ? 154 ARG F O   1 
ATOM   7981 C  CB  . ARG F  1 153 ? 12.089 -1.617  -3.563  1.00 34.38 ? 154 ARG F CB  1 
ATOM   7982 C  CG  . ARG F  1 153 ? 11.081 -2.746  -3.427  1.00 34.40 ? 154 ARG F CG  1 
ATOM   7983 C  CD  . ARG F  1 153 ? 11.512 -3.783  -2.394  1.00 38.08 ? 154 ARG F CD  1 
ATOM   7984 N  NE  . ARG F  1 153 ? 12.755 -4.446  -2.774  1.00 42.28 ? 154 ARG F NE  1 
ATOM   7985 C  CZ  . ARG F  1 153 ? 13.905 -4.290  -2.133  1.00 38.32 ? 154 ARG F CZ  1 
ATOM   7986 N  NH1 . ARG F  1 153 ? 13.992 -3.523  -1.057  1.00 34.15 ? 154 ARG F NH1 1 
ATOM   7987 N  NH2 . ARG F  1 153 ? 14.997 -4.905  -2.594  1.00 31.29 ? 154 ARG F NH2 1 
ATOM   7988 N  N   . ALA F  1 154 ? 9.962  0.577   -3.485  1.00 35.81 ? 155 ALA F N   1 
ATOM   7989 C  CA  . ALA F  1 154 ? 8.577  0.959   -3.248  1.00 39.14 ? 155 ALA F CA  1 
ATOM   7990 C  C   . ALA F  1 154 ? 8.085  1.921   -4.323  1.00 40.70 ? 155 ALA F C   1 
ATOM   7991 O  O   . ALA F  1 154 ? 6.950  1.799   -4.806  1.00 39.53 ? 155 ALA F O   1 
ATOM   7992 C  CB  . ALA F  1 154 ? 8.434  1.563   -1.849  1.00 31.24 ? 155 ALA F CB  1 
ATOM   7993 N  N   . GLY F  1 155 ? 8.934  2.850   -4.740  1.00 43.80 ? 156 GLY F N   1 
ATOM   7994 C  CA  . GLY F  1 155 ? 8.532  3.908   -5.640  1.00 43.48 ? 156 GLY F CA  1 
ATOM   7995 C  C   . GLY F  1 155 ? 9.353  3.900   -6.914  1.00 45.85 ? 156 GLY F C   1 
ATOM   7996 O  O   . GLY F  1 155 ? 9.281  2.951   -7.705  1.00 48.72 ? 156 GLY F O   1 
ATOM   7997 N  N   . PRO F  1 156 ? 10.184 4.954   -7.129  1.00 45.31 ? 157 PRO F N   1 
ATOM   7998 C  CA  . PRO F  1 156 ? 10.462 6.053   -6.183  1.00 39.19 ? 157 PRO F CA  1 
ATOM   7999 C  C   . PRO F  1 156 ? 9.474  7.233   -6.131  1.00 45.57 ? 157 PRO F C   1 
ATOM   8000 O  O   . PRO F  1 156 ? 9.767  8.179   -5.405  1.00 44.85 ? 157 PRO F O   1 
ATOM   8001 C  CB  . PRO F  1 156 ? 11.824 6.567   -6.653  1.00 42.25 ? 157 PRO F CB  1 
ATOM   8002 C  CG  . PRO F  1 156 ? 11.817 6.318   -8.132  1.00 43.90 ? 157 PRO F CG  1 
ATOM   8003 C  CD  . PRO F  1 156 ? 11.018 5.054   -8.347  1.00 43.99 ? 157 PRO F CD  1 
ATOM   8004 N  N   . THR F  1 157 ? 8.355  7.194   -6.862  1.00 44.74 ? 158 THR F N   1 
ATOM   8005 C  CA  . THR F  1 157 ? 7.348  8.253   -6.762  1.00 43.77 ? 158 THR F CA  1 
ATOM   8006 C  C   . THR F  1 157 ? 5.948  7.704   -6.502  1.00 41.98 ? 158 THR F C   1 
ATOM   8007 O  O   . THR F  1 157 ? 5.769  6.497   -6.294  1.00 43.37 ? 158 THR F O   1 
ATOM   8008 C  CB  . THR F  1 157 ? 7.320  9.105   -8.040  1.00 46.29 ? 158 THR F CB  1 
ATOM   8009 O  OG1 . THR F  1 157 ? 7.319  8.241   -9.187  1.00 46.39 ? 158 THR F OG1 1 
ATOM   8010 C  CG2 . THR F  1 157 ? 8.537  10.031  -8.095  1.00 48.25 ? 158 THR F CG2 1 
ATOM   8011 N  N   . GLY F  1 158 ? 4.954  8.593   -6.505  1.00 43.68 ? 159 GLY F N   1 
ATOM   8012 C  CA  . GLY F  1 158 ? 3.558  8.204   -6.370  1.00 35.90 ? 159 GLY F CA  1 
ATOM   8013 C  C   . GLY F  1 158 ? 3.240  7.514   -5.054  1.00 36.41 ? 159 GLY F C   1 
ATOM   8014 O  O   . GLY F  1 158 ? 3.737  7.880   -3.980  1.00 32.86 ? 159 GLY F O   1 
ATOM   8015 N  N   . LEU F  1 159 ? 2.383  6.494   -5.144  1.00 35.88 ? 160 LEU F N   1 
ATOM   8016 C  CA  . LEU F  1 159 ? 1.947  5.761   -3.963  1.00 38.68 ? 160 LEU F CA  1 
ATOM   8017 C  C   . LEU F  1 159 ? 3.120  5.118   -3.224  1.00 34.89 ? 160 LEU F C   1 
ATOM   8018 O  O   . LEU F  1 159 ? 3.096  5.037   -1.996  1.00 35.70 ? 160 LEU F O   1 
ATOM   8019 C  CB  . LEU F  1 159 ? 0.906  4.714   -4.373  1.00 36.10 ? 160 LEU F CB  1 
ATOM   8020 C  CG  . LEU F  1 159 ? 0.354  3.762   -3.308  1.00 39.09 ? 160 LEU F CG  1 
ATOM   8021 C  CD1 . LEU F  1 159 ? -0.352 4.502   -2.174  1.00 40.96 ? 160 LEU F CD1 1 
ATOM   8022 C  CD2 . LEU F  1 159 ? -0.592 2.762   -3.948  1.00 38.94 ? 160 LEU F CD2 1 
ATOM   8023 N  N   . GLY F  1 160 ? 4.155  4.677   -3.944  1.00 36.61 ? 161 GLY F N   1 
ATOM   8024 C  CA  . GLY F  1 160 ? 5.320  4.108   -3.279  1.00 36.54 ? 161 GLY F CA  1 
ATOM   8025 C  C   . GLY F  1 160 ? 6.057  5.118   -2.415  1.00 36.42 ? 161 GLY F C   1 
ATOM   8026 O  O   . GLY F  1 160 ? 6.429  4.828   -1.275  1.00 37.39 ? 161 GLY F O   1 
ATOM   8027 N  N   . GLU F  1 161 ? 6.288  6.317   -2.957  1.00 37.26 ? 162 GLU F N   1 
ATOM   8028 C  CA  . GLU F  1 161 ? 6.893  7.393   -2.181  1.00 37.86 ? 162 GLU F CA  1 
ATOM   8029 C  C   . GLU F  1 161 ? 6.028  7.753   -0.981  1.00 36.98 ? 162 GLU F C   1 
ATOM   8030 O  O   . GLU F  1 161 ? 6.544  7.992   0.116   1.00 33.36 ? 162 GLU F O   1 
ATOM   8031 C  CB  . GLU F  1 161 ? 7.104  8.617   -3.075  1.00 40.44 ? 162 GLU F CB  1 
ATOM   8032 C  CG  . GLU F  1 161 ? 7.675  9.843   -2.361  1.00 45.10 ? 162 GLU F CG  1 
ATOM   8033 C  CD  . GLU F  1 161 ? 8.000  11.004  -3.309  1.00 48.62 ? 162 GLU F CD  1 
ATOM   8034 O  OE1 . GLU F  1 161 ? 7.112  11.405  -4.105  1.00 52.04 ? 162 GLU F OE1 1 
ATOM   8035 O  OE2 . GLU F  1 161 ? 9.142  11.524  -3.246  1.00 47.71 ? 162 GLU F OE2 1 
ATOM   8036 N  N   . TYR F  1 162 ? 4.705  7.800   -1.181  1.00 36.34 ? 163 TYR F N   1 
ATOM   8037 C  CA  . TYR F  1 162 ? 3.777  8.092   -0.090  1.00 33.94 ? 163 TYR F CA  1 
ATOM   8038 C  C   . TYR F  1 162 ? 3.885  7.046   1.017   1.00 37.74 ? 163 TYR F C   1 
ATOM   8039 O  O   . TYR F  1 162 ? 3.932  7.384   2.205   1.00 36.98 ? 163 TYR F O   1 
ATOM   8040 C  CB  . TYR F  1 162 ? 2.354  8.163   -0.644  1.00 36.90 ? 163 TYR F CB  1 
ATOM   8041 C  CG  . TYR F  1 162 ? 1.280  8.208   0.421   1.00 42.32 ? 163 TYR F CG  1 
ATOM   8042 C  CD1 . TYR F  1 162 ? 0.962  9.398   1.061   1.00 39.15 ? 163 TYR F CD1 1 
ATOM   8043 C  CD2 . TYR F  1 162 ? 0.589  7.062   0.783   1.00 38.90 ? 163 TYR F CD2 1 
ATOM   8044 C  CE1 . TYR F  1 162 ? -0.008 9.443   2.031   1.00 38.64 ? 163 TYR F CE1 1 
ATOM   8045 C  CE2 . TYR F  1 162 ? -0.387 7.097   1.755   1.00 41.31 ? 163 TYR F CE2 1 
ATOM   8046 C  CZ  . TYR F  1 162 ? -0.681 8.294   2.374   1.00 43.15 ? 163 TYR F CZ  1 
ATOM   8047 O  OH  . TYR F  1 162 ? -1.654 8.336   3.341   1.00 45.37 ? 163 TYR F OH  1 
ATOM   8048 N  N   . MET F  1 163 ? 3.939  5.763   0.638   1.00 38.10 ? 164 MET F N   1 
ATOM   8049 C  CA  . MET F  1 163 ? 4.060  4.684   1.619   1.00 39.76 ? 164 MET F CA  1 
ATOM   8050 C  C   . MET F  1 163 ? 5.418  4.712   2.318   1.00 38.81 ? 164 MET F C   1 
ATOM   8051 O  O   . MET F  1 163 ? 5.500  4.564   3.542   1.00 35.66 ? 164 MET F O   1 
ATOM   8052 C  CB  . MET F  1 163 ? 3.832  3.325   0.947   1.00 37.55 ? 164 MET F CB  1 
ATOM   8053 C  CG  . MET F  1 163 ? 2.390  3.059   0.473   1.00 42.83 ? 164 MET F CG  1 
ATOM   8054 S  SD  . MET F  1 163 ? 1.155  3.450   1.762   1.00 53.23 ? 164 MET F SD  1 
ATOM   8055 C  CE  . MET F  1 163 ? 1.295  2.023   2.807   1.00 51.63 ? 164 MET F CE  1 
ATOM   8056 N  N   . PHE F  1 164 ? 6.498  4.879   1.549   1.00 38.66 ? 165 PHE F N   1 
ATOM   8057 C  CA  . PHE F  1 164 ? 7.826  4.983   2.147   1.00 40.51 ? 165 PHE F CA  1 
ATOM   8058 C  C   . PHE F  1 164 ? 7.896  6.123   3.152   1.00 39.91 ? 165 PHE F C   1 
ATOM   8059 O  O   . PHE F  1 164 ? 8.503  5.981   4.218   1.00 39.55 ? 165 PHE F O   1 
ATOM   8060 C  CB  . PHE F  1 164 ? 8.879  5.186   1.059   1.00 38.78 ? 165 PHE F CB  1 
ATOM   8061 C  CG  . PHE F  1 164 ? 10.263 5.288   1.592   1.00 39.55 ? 165 PHE F CG  1 
ATOM   8062 C  CD1 . PHE F  1 164 ? 10.972 4.136   1.938   1.00 40.39 ? 165 PHE F CD1 1 
ATOM   8063 C  CD2 . PHE F  1 164 ? 10.863 6.534   1.774   1.00 38.67 ? 165 PHE F CD2 1 
ATOM   8064 C  CE1 . PHE F  1 164 ? 12.272 4.223   2.453   1.00 39.04 ? 165 PHE F CE1 1 
ATOM   8065 C  CE2 . PHE F  1 164 ? 12.158 6.636   2.281   1.00 36.22 ? 165 PHE F CE2 1 
ATOM   8066 C  CZ  . PHE F  1 164 ? 12.867 5.475   2.624   1.00 38.35 ? 165 PHE F CZ  1 
ATOM   8067 N  N   . ASP F  1 165 ? 7.295  7.270   2.814   1.00 39.81 ? 166 ASP F N   1 
ATOM   8068 C  CA  . ASP F  1 165 ? 7.269  8.417   3.717   1.00 41.45 ? 166 ASP F CA  1 
ATOM   8069 C  C   . ASP F  1 165 ? 6.623  8.069   5.049   1.00 42.43 ? 166 ASP F C   1 
ATOM   8070 O  O   . ASP F  1 165 ? 7.086  8.514   6.103   1.00 43.29 ? 166 ASP F O   1 
ATOM   8071 C  CB  . ASP F  1 165 ? 6.506  9.575   3.073   1.00 42.52 ? 166 ASP F CB  1 
ATOM   8072 C  CG  . ASP F  1 165 ? 6.565  10.855  3.909   1.00 47.26 ? 166 ASP F CG  1 
ATOM   8073 O  OD1 . ASP F  1 165 ? 7.634  11.503  3.936   1.00 46.10 ? 166 ASP F OD1 1 
ATOM   8074 O  OD2 . ASP F  1 165 ? 5.545  11.189  4.576   1.00 47.92 ? 166 ASP F OD2 1 
ATOM   8075 N  N   . LYS F  1 166 ? 5.532  7.298   5.018   1.00 42.88 ? 167 LYS F N   1 
ATOM   8076 C  CA  . LYS F  1 166 ? 4.856  6.918   6.255   1.00 50.56 ? 167 LYS F CA  1 
ATOM   8077 C  C   . LYS F  1 166 ? 5.745  6.046   7.138   1.00 50.08 ? 167 LYS F C   1 
ATOM   8078 O  O   . LYS F  1 166 ? 5.632  6.103   8.368   1.00 51.44 ? 167 LYS F O   1 
ATOM   8079 C  CB  . LYS F  1 166 ? 3.534  6.210   5.933   1.00 48.66 ? 167 LYS F CB  1 
ATOM   8080 C  CG  . LYS F  1 166 ? 2.399  7.194   5.669   1.00 53.15 ? 167 LYS F CG  1 
ATOM   8081 C  CD  . LYS F  1 166 ? 1.013  6.626   5.981   1.00 60.10 ? 167 LYS F CD  1 
ATOM   8082 C  CE  . LYS F  1 166 ? 0.590  5.587   4.962   1.00 54.65 ? 167 LYS F CE  1 
ATOM   8083 N  NZ  . LYS F  1 166 ? 0.034  4.362   5.615   1.00 71.94 ? 167 LYS F NZ  1 
ATOM   8084 N  N   . GLU F  1 167 ? 6.657  5.265   6.543   1.00 43.67 ? 168 GLU F N   1 
ATOM   8085 C  CA  . GLU F  1 167 ? 7.562  4.462   7.363   1.00 51.90 ? 168 GLU F CA  1 
ATOM   8086 C  C   . GLU F  1 167 ? 8.618  5.325   8.054   1.00 50.50 ? 168 GLU F C   1 
ATOM   8087 O  O   . GLU F  1 167 ? 9.037  5.000   9.170   1.00 53.20 ? 168 GLU F O   1 
ATOM   8088 C  CB  . GLU F  1 167 ? 8.224  3.346   6.527   1.00 56.83 ? 168 GLU F CB  1 
ATOM   8089 C  CG  . GLU F  1 167 ? 9.709  3.569   6.167   1.00 54.93 ? 168 GLU F CG  1 
ATOM   8090 C  CD  . GLU F  1 167 ? 10.427 2.299   5.662   1.00 66.97 ? 168 GLU F CD  1 
ATOM   8091 O  OE1 . GLU F  1 167 ? 10.101 1.820   4.556   1.00 64.42 ? 168 GLU F OE1 1 
ATOM   8092 O  OE2 . GLU F  1 167 ? 11.351 1.795   6.349   1.00 72.87 ? 168 GLU F OE2 1 
ATOM   8093 N  N   . LEU F  1 168 ? 9.058  6.424   7.427   1.00 48.64 ? 169 LEU F N   1 
ATOM   8094 C  CA  . LEU F  1 168 ? 10.002 7.326   8.090   1.00 47.32 ? 169 LEU F CA  1 
ATOM   8095 C  C   . LEU F  1 168 ? 9.363  8.123   9.210   1.00 51.30 ? 169 LEU F C   1 
ATOM   8096 O  O   . LEU F  1 168 ? 10.080 8.635   10.079  1.00 52.31 ? 169 LEU F O   1 
ATOM   8097 C  CB  . LEU F  1 168 ? 10.591 8.324   7.102   1.00 46.76 ? 169 LEU F CB  1 
ATOM   8098 C  CG  . LEU F  1 168 ? 11.634 7.781   6.157   1.00 48.28 ? 169 LEU F CG  1 
ATOM   8099 C  CD1 . LEU F  1 168 ? 12.070 8.905   5.226   1.00 43.39 ? 169 LEU F CD1 1 
ATOM   8100 C  CD2 . LEU F  1 168 ? 12.786 7.242   6.990   1.00 47.05 ? 169 LEU F CD2 1 
ATOM   8101 N  N   . ASN F  1 169 ? 8.042  8.273   9.181   1.00 56.71 ? 170 ASN F N   1 
ATOM   8102 C  CA  . ASN F  1 169 ? 7.339  9.164   10.090  1.00 61.41 ? 170 ASN F CA  1 
ATOM   8103 C  C   . ASN F  1 169 ? 7.432  8.686   11.516  1.00 66.76 ? 170 ASN F C   1 
ATOM   8104 O  O   . ASN F  1 169 ? 6.839  7.659   11.867  1.00 71.08 ? 170 ASN F O   1 
ATOM   8105 C  CB  . ASN F  1 169 ? 5.873  9.293   9.688   1.00 60.47 ? 170 ASN F CB  1 
ATOM   8106 C  CG  . ASN F  1 169 ? 5.454  10.735  9.488   1.00 63.22 ? 170 ASN F CG  1 
ATOM   8107 O  OD1 . ASN F  1 169 ? 4.595  11.032  8.650   1.00 70.71 ? 170 ASN F OD1 1 
ATOM   8108 N  ND2 . ASN F  1 169 ? 6.065  11.646  10.252  1.00 55.32 ? 170 ASN F ND2 1 
ATOM   8109 O  OXT . ASN F  1 169 ? 8.094  9.341   12.323  1.00 73.45 ? 170 ASN F OXT 1 
HETATM 8110 CD CD  . CD  G  2 .   ? 51.974 32.910  -2.073  0.72 44.82 ? 201 CD  A CD  1 
HETATM 8111 CD CD  . CD  H  2 .   ? 56.351 38.769  -4.130  0.64 71.59 ? 202 CD  A CD  1 
HETATM 8112 CD CD  . CD  I  2 .   ? 55.544 37.605  -7.368  0.40 60.95 ? 203 CD  A CD  1 
HETATM 8113 CD CD  . CD  J  2 .   ? 53.697 35.882  -2.271  0.35 73.24 ? 204 CD  A CD  1 
HETATM 8114 S  S   . H2S K  3 .   ? 57.301 39.758  -6.537  1.00 86.01 ? 205 H2S A S   1 
HETATM 8115 S  S   . H2S L  3 .   ? 53.861 33.691  -0.484  0.66 58.09 ? 206 H2S A S   1 
HETATM 8116 S  S   . H2S M  3 .   ? 55.204 38.869  -1.727  0.74 64.28 ? 207 H2S A S   1 
HETATM 8117 S  S   . H2S N  3 .   ? 54.212 39.478  -8.464  0.92 75.36 ? 208 H2S A S   1 
HETATM 8118 S  S   . H2S O  3 .   ? 55.254 41.307  -3.887  0.65 55.08 ? 209 H2S A S   1 
HETATM 8119 S  S   . H2S P  3 .   ? 56.876 35.526  -2.733  0.38 57.58 ? 210 H2S A S   1 
HETATM 8120 MG MG  . MG  Q  4 .   ? 49.411 7.705   -7.513  1.00 50.20 ? 211 MG  A MG  1 
HETATM 8121 S  S   . SO4 R  5 .   ? 41.792 37.287  -3.610  0.63 57.13 ? 212 SO4 A S   1 
HETATM 8122 O  O1  . SO4 R  5 .   ? 43.022 36.931  -4.329  0.63 41.16 ? 212 SO4 A O1  1 
HETATM 8123 O  O2  . SO4 R  5 .   ? 41.085 36.088  -3.155  0.63 47.48 ? 212 SO4 A O2  1 
HETATM 8124 O  O3  . SO4 R  5 .   ? 42.126 38.093  -2.437  0.63 45.20 ? 212 SO4 A O3  1 
HETATM 8125 O  O4  . SO4 R  5 .   ? 40.941 38.052  -4.514  0.63 49.44 ? 212 SO4 A O4  1 
HETATM 8126 S  S   . SO4 S  5 .   ? 66.543 24.105  -12.261 1.00 95.58 ? 213 SO4 A S   1 
HETATM 8127 O  O1  . SO4 S  5 .   ? 67.440 24.724  -13.241 1.00 75.90 ? 213 SO4 A O1  1 
HETATM 8128 O  O2  . SO4 S  5 .   ? 65.256 23.797  -12.895 1.00 77.11 ? 213 SO4 A O2  1 
HETATM 8129 O  O3  . SO4 S  5 .   ? 67.130 22.868  -11.714 1.00 77.57 ? 213 SO4 A O3  1 
HETATM 8130 O  O4  . SO4 S  5 .   ? 66.343 25.079  -11.188 1.00 76.85 ? 213 SO4 A O4  1 
HETATM 8131 CD CD  . CD  T  2 .   ? 47.817 9.175   37.936  0.80 47.07 ? 201 CD  B CD  1 
HETATM 8132 CD CD  . CD  U  2 .   ? 40.816 12.432  38.464  0.65 79.85 ? 202 CD  B CD  1 
HETATM 8133 CD CD  . CD  V  2 .   ? 39.684 9.185   38.364  0.52 74.63 ? 203 CD  B CD  1 
HETATM 8134 CD CD  . CD  W  2 .   ? 44.735 12.388  39.700  0.25 64.02 ? 204 CD  B CD  1 
HETATM 8135 S  S   . H2S X  3 .   ? 47.356 11.493  36.874  0.67 60.62 ? 205 H2S B S   1 
HETATM 8136 S  S   . H2S Y  3 .   ? 37.905 11.671  38.359  1.00 82.67 ? 206 H2S B S   1 
HETATM 8137 S  S   . H2S Z  3 .   ? 43.954 12.227  35.958  0.94 71.59 ? 207 H2S B S   1 
HETATM 8138 S  S   . H2S AA 3 .   ? 42.789 13.420  38.812  0.80 60.82 ? 208 H2S B S   1 
HETATM 8139 S  S   . H2S BA 3 .   ? 38.840 7.665   40.831  0.92 74.99 ? 209 H2S B S   1 
HETATM 8140 S  S   . SO4 CA 5 .   ? 49.369 5.933   48.458  0.65 61.70 ? 210 SO4 B S   1 
HETATM 8141 O  O1  . SO4 CA 5 .   ? 49.500 7.365   48.192  0.65 48.52 ? 210 SO4 B O1  1 
HETATM 8142 O  O2  . SO4 CA 5 .   ? 48.014 5.514   48.116  0.65 47.86 ? 210 SO4 B O2  1 
HETATM 8143 O  O3  . SO4 CA 5 .   ? 50.337 5.169   47.662  0.65 49.63 ? 210 SO4 B O3  1 
HETATM 8144 O  O4  . SO4 CA 5 .   ? 49.639 5.762   49.885  0.65 52.01 ? 210 SO4 B O4  1 
HETATM 8145 CD CD  . CD  DA 2 .   ? 30.504 41.305  -9.379  0.77 45.69 ? 201 CD  C CD  1 
HETATM 8146 CD CD  . CD  EA 2 .   ? 32.220 42.574  -16.709 0.68 76.60 ? 202 CD  C CD  1 
HETATM 8147 CD CD  . CD  FA 2 .   ? 34.178 45.189  -15.411 0.48 70.78 ? 203 CD  C CD  1 
HETATM 8148 CD CD  . CD  GA 2 .   ? 31.265 40.585  -13.238 0.28 63.75 ? 204 CD  C CD  1 
HETATM 8149 S  S   . H2S HA 3 .   ? 33.984 44.475  -18.682 1.00 92.38 ? 205 H2S C S   1 
HETATM 8150 S  S   . H2S IA 3 .   ? 29.073 42.381  -14.241 0.88 62.61 ? 206 H2S C S   1 
HETATM 8151 S  S   . H2S JA 3 .   ? 28.772 40.987  -11.170 0.69 57.78 ? 207 H2S C S   1 
HETATM 8152 S  S   . H2S KA 3 .   ? 31.198 40.030  -15.967 0.76 63.89 ? 208 H2S C S   1 
HETATM 8153 S  S   . H2S LA 3 .   ? 34.377 41.183  -18.060 0.66 61.42 ? 209 H2S C S   1 
HETATM 8154 S  S   . H2S MA 3 .   ? 36.783 44.800  -15.884 1.00 82.55 ? 210 H2S C S   1 
HETATM 8155 MG MG  . MG  NA 4 .   ? 23.334 54.738  11.474  1.00 50.49 ? 211 MG  C MG  1 
HETATM 8156 S  S   . SO4 OA 5 .   ? 39.419 35.897  -6.172  0.66 57.45 ? 212 SO4 C S   1 
HETATM 8157 O  O1  . SO4 OA 5 .   ? 40.847 35.728  -5.959  0.66 43.60 ? 212 SO4 C O1  1 
HETATM 8158 O  O2  . SO4 OA 5 .   ? 38.982 34.917  -7.169  0.66 47.00 ? 212 SO4 C O2  1 
HETATM 8159 O  O3  . SO4 OA 5 .   ? 38.666 35.666  -4.927  0.66 45.60 ? 212 SO4 C O3  1 
HETATM 8160 O  O4  . SO4 OA 5 .   ? 39.180 37.250  -6.680  0.66 43.07 ? 212 SO4 C O4  1 
HETATM 8161 CD CD  . CD  PA 2 .   ? 48.463 -1.194  59.687  0.69 43.28 ? 201 CD  D CD  1 
HETATM 8162 CD CD  . CD  QA 2 .   ? 42.216 -5.394  59.212  0.53 61.12 ? 202 CD  D CD  1 
HETATM 8163 CD CD  . CD  RA 2 .   ? 40.468 -2.478  59.568  0.40 60.10 ? 203 CD  D CD  1 
HETATM 8164 CD CD  . CD  SA 2 .   ? 45.929 -4.043  58.487  0.25 54.84 ? 204 CD  D CD  1 
HETATM 8165 S  S   . H2S TA 3 .   ? 39.522 -5.310  59.479  1.00 78.29 ? 205 H2S D S   1 
HETATM 8166 S  S   . H2S UA 3 .   ? 38.864 -1.872  57.454  1.00 78.09 ? 206 H2S D S   1 
HETATM 8167 S  S   . H2S VA 3 .   ? 44.399 -6.429  58.500  0.65 55.56 ? 207 H2S D S   1 
HETATM 8168 S  S   . H2S WA 3 .   ? 48.035 -3.258  60.305  0.75 66.83 ? 208 H2S D S   1 
HETATM 8169 S  S   . H2S XA 3 .   ? 41.222 -6.086  57.003  0.66 58.85 ? 209 H2S D S   1 
HETATM 8170 S  S   . H2S YA 3 .   ? 41.931 -2.795  61.675  0.43 55.02 ? 210 H2S D S   1 
HETATM 8171 S  S   . H2S ZA 3 .   ? 45.501 -5.125  61.251  0.70 62.03 ? 211 H2S D S   1 
HETATM 8172 MG MG  . MG  AB 4 .   ? 63.374 0.000   48.823  0.50 28.16 ? 212 MG  D MG  1 
HETATM 8173 MG MG  . MG  BB 4 .   ? 58.116 18.394  73.644  1.00 50.66 ? 213 MG  D MG  1 
HETATM 8174 S  S   . SO4 CB 5 .   ? 49.278 2.448   49.169  0.68 60.07 ? 214 SO4 D S   1 
HETATM 8175 O  O1  . SO4 CB 5 .   ? 50.642 2.450   49.717  0.68 51.30 ? 214 SO4 D O1  1 
HETATM 8176 O  O2  . SO4 CB 5 .   ? 48.497 3.476   49.840  0.68 51.45 ? 214 SO4 D O2  1 
HETATM 8177 O  O3  . SO4 CB 5 .   ? 48.608 1.181   49.424  0.68 45.76 ? 214 SO4 D O3  1 
HETATM 8178 O  O4  . SO4 CB 5 .   ? 49.302 2.673   47.726  0.68 54.11 ? 214 SO4 D O4  1 
HETATM 8179 CD CD  . CD  DB 2 .   ? 16.226 35.966  18.127  0.71 44.15 ? 201 CD  E CD  1 
HETATM 8180 CD CD  . CD  EB 2 .   ? 15.361 33.857  25.560  0.62 71.57 ? 202 CD  E CD  1 
HETATM 8181 CD CD  . CD  FB 2 .   ? 13.077 31.480  24.070  0.41 65.81 ? 203 CD  E CD  1 
HETATM 8182 CD CD  . CD  GB 2 .   ? 17.769 34.894  22.264  0.22 54.30 ? 204 CD  E CD  1 
HETATM 8183 S  S   . H2S HB 3 .   ? 16.367 37.559  19.634  0.53 50.63 ? 205 H2S E S   1 
HETATM 8184 S  S   . H2S IB 3 .   ? 17.220 32.208  26.923  0.67 63.97 ? 206 H2S E S   1 
HETATM 8185 S  S   . H2S JB 3 .   ? 17.833 35.550  25.164  0.76 68.13 ? 207 H2S E S   1 
HETATM 8186 S  S   . H2S KB 3 .   ? 11.514 33.416  23.921  0.79 73.50 ? 208 H2S E S   1 
HETATM 8187 S  S   . H2S LB 3 .   ? 14.490 36.454  23.758  0.74 69.30 ? 209 H2S E S   1 
HETATM 8188 S  S   . H2S MB 3 .   ? 14.267 29.119  25.102  1.00 79.37 ? 210 H2S E S   1 
HETATM 8189 MG MG  . MG  NB 4 .   ? 2.099  40.946  -2.985  1.00 50.31 ? 211 MG  E MG  1 
HETATM 8190 S  S   . SO4 OB 5 .   ? 23.215 28.084  14.757  0.68 62.30 ? 212 SO4 E S   1 
HETATM 8191 O  O1  . SO4 OB 5 .   ? 24.163 28.771  15.635  0.68 50.07 ? 212 SO4 E O1  1 
HETATM 8192 O  O2  . SO4 OB 5 .   ? 21.866 28.124  15.348  0.68 41.38 ? 212 SO4 E O2  1 
HETATM 8193 O  O3  . SO4 OB 5 .   ? 23.181 28.752  13.449  0.68 49.88 ? 212 SO4 E O3  1 
HETATM 8194 O  O4  . SO4 OB 5 .   ? 23.688 26.706  14.639  0.68 46.05 ? 212 SO4 E O4  1 
HETATM 8195 CD CD  . CD  PB 2 .   ? 28.233 16.400  10.629  0.76 47.51 ? 201 CD  F CD  1 
HETATM 8196 CD CD  . CD  QB 2 .   ? 23.111 11.096  12.526  0.55 67.44 ? 202 CD  F CD  1 
HETATM 8197 CD CD  . CD  RB 2 .   ? 24.181 12.003  15.920  0.42 61.40 ? 203 CD  F CD  1 
HETATM 8198 CD CD  . CD  SB 2 .   ? 24.339 14.245  10.411  0.26 63.71 ? 204 CD  F CD  1 
HETATM 8199 S  S   . H2S TB 3 .   ? 22.768 10.487  14.848  1.00 76.40 ? 205 H2S F S   1 
HETATM 8200 S  S   . H2S UB 3 .   ? 27.957 14.445  8.790   0.65 59.04 ? 206 H2S F S   1 
HETATM 8201 S  S   . H2S VB 3 .   ? 25.951 11.620  10.532  0.90 60.46 ? 207 H2S F S   1 
HETATM 8202 S  S   . H2S WB 3 .   ? 20.451 11.319  12.669  1.00 74.37 ? 208 H2S F S   1 
HETATM 8203 S  S   . H2S XB 3 .   ? 22.736 12.028  9.676   0.82 75.78 ? 209 H2S F S   1 
HETATM 8204 MG MG  . MG  YB 4 .   ? 51.313 21.775  21.846  1.00 35.50 ? 210 MG  F MG  1 
HETATM 8205 S  S   . SO4 ZB 5 .   ? 22.343 25.700  12.284  0.76 63.32 ? 211 SO4 F S   1 
HETATM 8206 O  O1  . SO4 ZB 5 .   ? 23.540 26.454  11.895  0.76 51.96 ? 211 SO4 F O1  1 
HETATM 8207 O  O2  . SO4 ZB 5 .   ? 22.734 24.536  13.087  0.76 46.39 ? 211 SO4 F O2  1 
HETATM 8208 O  O3  . SO4 ZB 5 .   ? 21.430 26.524  13.063  0.76 48.96 ? 211 SO4 F O3  1 
HETATM 8209 O  O4  . SO4 ZB 5 .   ? 21.651 25.268  11.066  0.76 54.00 ? 211 SO4 F O4  1 
HETATM 8210 O  O   . HOH AC 6 .   ? 40.742 52.542  0.499   1.00 41.54 ? 301 HOH A O   1 
HETATM 8211 O  O   . HOH AC 6 .   ? 44.484 41.239  -4.855  1.00 46.20 ? 302 HOH A O   1 
HETATM 8212 O  O   . HOH AC 6 .   ? 37.624 53.321  8.323   1.00 48.56 ? 303 HOH A O   1 
HETATM 8213 O  O   . HOH AC 6 .   ? 42.316 13.494  -10.732 1.00 46.68 ? 304 HOH A O   1 
HETATM 8214 O  O   . HOH AC 6 .   ? 42.006 17.771  -3.337  1.00 39.81 ? 305 HOH A O   1 
HETATM 8215 O  O   . HOH AC 6 .   ? 37.185 27.393  6.909   1.00 40.58 ? 306 HOH A O   1 
HETATM 8216 O  O   . HOH AC 6 .   ? 38.664 58.951  11.806  1.00 42.21 ? 307 HOH A O   1 
HETATM 8217 O  O   . HOH AC 6 .   ? 43.661 10.461  -26.136 1.00 41.75 ? 308 HOH A O   1 
HETATM 8218 O  O   . HOH AC 6 .   ? 51.020 35.467  10.258  1.00 36.29 ? 309 HOH A O   1 
HETATM 8219 O  O   . HOH AC 6 .   ? 44.845 13.088  -5.021  1.00 45.20 ? 310 HOH A O   1 
HETATM 8220 O  O   . HOH AC 6 .   ? 57.912 14.171  -13.669 1.00 38.56 ? 311 HOH A O   1 
HETATM 8221 O  O   . HOH AC 6 .   ? 53.835 58.373  5.259   1.00 35.72 ? 312 HOH A O   1 
HETATM 8222 O  O   . HOH AC 6 .   ? 32.168 24.455  4.721   1.00 45.68 ? 313 HOH A O   1 
HETATM 8223 O  O   . HOH AC 6 .   ? 60.261 25.793  9.498   1.00 47.87 ? 314 HOH A O   1 
HETATM 8224 O  O   . HOH AC 6 .   ? 65.311 9.271   -8.795  1.00 46.61 ? 315 HOH A O   1 
HETATM 8225 O  O   . HOH AC 6 .   ? 42.406 24.290  -3.823  1.00 30.21 ? 316 HOH A O   1 
HETATM 8226 O  O   . HOH AC 6 .   ? 62.677 28.263  -0.144  1.00 37.86 ? 317 HOH A O   1 
HETATM 8227 O  O   . HOH AC 6 .   ? 55.347 50.683  12.770  1.00 42.01 ? 318 HOH A O   1 
HETATM 8228 O  O   . HOH AC 6 .   ? 41.657 32.626  9.557   1.00 42.20 ? 319 HOH A O   1 
HETATM 8229 O  O   . HOH AC 6 .   ? 44.813 26.578  3.263   1.00 43.50 ? 320 HOH A O   1 
HETATM 8230 O  O   . HOH AC 6 .   ? 55.099 43.349  -1.845  1.00 45.56 ? 321 HOH A O   1 
HETATM 8231 O  O   . HOH AC 6 .   ? 38.435 55.497  6.526   1.00 36.61 ? 322 HOH A O   1 
HETATM 8232 O  O   . HOH AC 6 .   ? 39.684 43.631  7.011   1.00 39.19 ? 323 HOH A O   1 
HETATM 8233 O  O   . HOH AC 6 .   ? 57.952 7.908   -10.124 1.00 44.66 ? 324 HOH A O   1 
HETATM 8234 O  O   . HOH AC 6 .   ? 54.145 13.110  -8.319  1.00 37.03 ? 325 HOH A O   1 
HETATM 8235 O  O   . HOH AC 6 .   ? 34.259 39.123  2.364   1.00 25.52 ? 326 HOH A O   1 
HETATM 8236 O  O   . HOH AC 6 .   ? 51.970 14.991  -18.713 1.00 34.62 ? 327 HOH A O   1 
HETATM 8237 O  O   . HOH AC 6 .   ? 40.566 11.947  -25.937 1.00 49.13 ? 328 HOH A O   1 
HETATM 8238 O  O   . HOH AC 6 .   ? 63.389 18.129  -0.713  1.00 41.93 ? 329 HOH A O   1 
HETATM 8239 O  O   . HOH AC 6 .   ? 53.385 32.990  -10.350 1.00 44.32 ? 330 HOH A O   1 
HETATM 8240 O  O   . HOH AC 6 .   ? 41.114 20.868  -13.166 1.00 28.43 ? 331 HOH A O   1 
HETATM 8241 O  O   . HOH AC 6 .   ? 65.519 34.668  3.228   1.00 30.02 ? 332 HOH A O   1 
HETATM 8242 O  O   . HOH AC 6 .   ? 41.723 16.247  -7.708  1.00 40.15 ? 333 HOH A O   1 
HETATM 8243 O  O   . HOH AC 6 .   ? 64.792 54.052  16.666  1.00 50.07 ? 334 HOH A O   1 
HETATM 8244 O  O   . HOH AC 6 .   ? 44.598 57.233  14.527  1.00 43.62 ? 335 HOH A O   1 
HETATM 8245 O  O   . HOH AC 6 .   ? 60.617 41.453  15.169  1.00 42.76 ? 336 HOH A O   1 
HETATM 8246 O  O   . HOH AC 6 .   ? 67.206 48.144  13.627  1.00 32.78 ? 337 HOH A O   1 
HETATM 8247 O  O   . HOH AC 6 .   ? 34.931 22.045  -2.240  1.00 52.71 ? 338 HOH A O   1 
HETATM 8248 O  O   . HOH AC 6 .   ? 51.410 14.269  -16.205 1.00 31.25 ? 339 HOH A O   1 
HETATM 8249 O  O   . HOH AC 6 .   ? 64.306 42.435  13.807  1.00 54.10 ? 340 HOH A O   1 
HETATM 8250 O  O   . HOH AC 6 .   ? 51.132 16.891  -19.965 1.00 33.17 ? 341 HOH A O   1 
HETATM 8251 O  O   . HOH AC 6 .   ? 39.619 25.566  3.176   1.00 40.48 ? 342 HOH A O   1 
HETATM 8252 O  O   . HOH AC 6 .   ? 47.415 24.090  -18.079 1.00 36.59 ? 343 HOH A O   1 
HETATM 8253 O  O   . HOH AC 6 .   ? 53.266 25.439  6.928   1.00 43.62 ? 344 HOH A O   1 
HETATM 8254 O  O   . HOH AC 6 .   ? 40.647 45.826  5.212   1.00 38.32 ? 345 HOH A O   1 
HETATM 8255 O  O   . HOH AC 6 .   ? 65.968 43.555  13.344  1.00 52.71 ? 346 HOH A O   1 
HETATM 8256 O  O   . HOH AC 6 .   ? 62.432 19.593  1.127   1.00 41.34 ? 347 HOH A O   1 
HETATM 8257 O  O   . HOH AC 6 .   ? 51.682 58.350  7.175   1.00 39.00 ? 348 HOH A O   1 
HETATM 8258 O  O   . HOH AC 6 .   ? 65.176 40.149  -1.195  1.00 41.97 ? 349 HOH A O   1 
HETATM 8259 O  O   . HOH AC 6 .   ? 66.335 33.712  -3.898  1.00 49.11 ? 350 HOH A O   1 
HETATM 8260 O  O   . HOH AC 6 .   ? 51.963 26.632  -14.327 1.00 39.44 ? 351 HOH A O   1 
HETATM 8261 O  O   . HOH AC 6 .   ? 53.100 17.765  0.853   1.00 36.25 ? 352 HOH A O   1 
HETATM 8262 O  O   . HOH AC 6 .   ? 49.065 53.402  -1.735  1.00 45.80 ? 353 HOH A O   1 
HETATM 8263 O  O   . HOH AC 6 .   ? 51.868 40.626  14.559  1.00 38.27 ? 354 HOH A O   1 
HETATM 8264 O  O   . HOH AC 6 .   ? 52.296 63.222  3.575   1.00 44.38 ? 355 HOH A O   1 
HETATM 8265 O  O   . HOH AC 6 .   ? 59.418 55.355  17.433  1.00 46.19 ? 356 HOH A O   1 
HETATM 8266 O  O   . HOH AC 6 .   ? 41.473 28.765  4.008   1.00 31.10 ? 357 HOH A O   1 
HETATM 8267 O  O   . HOH AC 6 .   ? 54.543 13.936  -17.372 1.00 34.58 ? 358 HOH A O   1 
HETATM 8268 O  O   . HOH AC 6 .   ? 59.727 37.539  -3.942  1.00 51.30 ? 359 HOH A O   1 
HETATM 8269 O  O   . HOH AC 6 .   ? 37.938 56.112  12.656  1.00 44.47 ? 360 HOH A O   1 
HETATM 8270 O  O   . HOH AC 6 .   ? 50.485 21.720  0.174   1.00 44.43 ? 361 HOH A O   1 
HETATM 8271 O  O   . HOH AC 6 .   ? 61.995 55.981  18.363  1.00 51.21 ? 362 HOH A O   1 
HETATM 8272 O  O   . HOH AC 6 .   ? 58.393 22.234  -14.345 1.00 42.36 ? 363 HOH A O   1 
HETATM 8273 O  O   . HOH AC 6 .   ? 55.296 10.533  -9.390  1.00 45.39 ? 364 HOH A O   1 
HETATM 8274 O  O   . HOH AC 6 .   ? 52.930 7.000   -15.342 1.00 45.20 ? 365 HOH A O   1 
HETATM 8275 O  O   . HOH AC 6 .   ? 63.562 11.499  -1.687  1.00 46.25 ? 366 HOH A O   1 
HETATM 8276 O  O   . HOH AC 6 .   ? 58.027 61.085  16.545  1.00 37.06 ? 367 HOH A O   1 
HETATM 8277 O  O   . HOH AC 6 .   ? 35.682 23.725  1.502   1.00 46.98 ? 368 HOH A O   1 
HETATM 8278 O  O   . HOH AC 6 .   ? 32.036 26.409  1.570   1.00 42.50 ? 369 HOH A O   1 
HETATM 8279 O  O   . HOH AC 6 .   ? 48.890 14.752  0.022   1.00 47.47 ? 370 HOH A O   1 
HETATM 8280 O  O   . HOH AC 6 .   ? 63.897 15.411  -8.376  1.00 47.07 ? 371 HOH A O   1 
HETATM 8281 O  O   . HOH AC 6 .   ? 62.289 12.718  -0.569  1.00 49.15 ? 372 HOH A O   1 
HETATM 8282 O  O   . HOH AC 6 .   ? 44.941 36.877  11.361  1.00 57.52 ? 373 HOH A O   1 
HETATM 8283 O  O   . HOH AC 6 .   ? 50.370 25.461  7.365   1.00 51.95 ? 374 HOH A O   1 
HETATM 8284 O  O   . HOH AC 6 .   ? 47.856 16.900  1.134   1.00 53.28 ? 375 HOH A O   1 
HETATM 8285 O  O   . HOH AC 6 .   ? 56.677 14.542  -15.969 1.00 35.74 ? 376 HOH A O   1 
HETATM 8286 O  O   . HOH AC 6 .   ? 40.033 47.931  6.854   1.00 35.76 ? 377 HOH A O   1 
HETATM 8287 O  O   . HOH AC 6 .   ? 40.237 12.719  -22.807 1.00 48.12 ? 378 HOH A O   1 
HETATM 8288 O  O   . HOH AC 6 .   ? 64.566 27.569  1.360   1.00 34.29 ? 379 HOH A O   1 
HETATM 8289 O  O   . HOH AC 6 .   ? 63.134 12.918  -8.930  1.00 39.22 ? 380 HOH A O   1 
HETATM 8290 O  O   . HOH AC 6 .   ? 39.931 27.019  5.271   1.00 39.15 ? 381 HOH A O   1 
HETATM 8291 O  O   . HOH AC 6 .   ? 65.952 43.893  17.396  1.00 58.89 ? 382 HOH A O   1 
HETATM 8292 O  O   . HOH AC 6 .   ? 51.433 14.191  1.512   1.00 55.31 ? 383 HOH A O   1 
HETATM 8293 O  O   . HOH AC 6 .   ? 46.474 28.240  5.382   1.00 44.63 ? 384 HOH A O   1 
HETATM 8294 O  O   . HOH AC 6 .   ? 67.017 45.284  14.778  1.00 44.33 ? 385 HOH A O   1 
HETATM 8295 O  O   . HOH AC 6 .   ? 43.459 28.974  5.720   1.00 39.51 ? 386 HOH A O   1 
HETATM 8296 O  O   . HOH AC 6 .   ? 31.352 22.400  3.342   1.00 45.08 ? 387 HOH A O   1 
HETATM 8297 O  O   . HOH AC 6 .   ? 39.538 10.763  -22.937 1.00 59.57 ? 388 HOH A O   1 
HETATM 8298 O  O   . HOH BC 6 .   ? 63.374 0.000   45.531  0.50 33.49 ? 301 HOH B O   1 
HETATM 8299 O  O   . HOH BC 6 .   ? 60.192 -1.181  38.442  1.00 43.25 ? 302 HOH B O   1 
HETATM 8300 O  O   . HOH BC 6 .   ? 55.930 -2.062  23.224  1.00 41.78 ? 303 HOH B O   1 
HETATM 8301 O  O   . HOH BC 6 .   ? 43.724 16.144  59.197  1.00 34.11 ? 304 HOH B O   1 
HETATM 8302 O  O   . HOH BC 6 .   ? 48.493 -6.395  21.233  1.00 34.58 ? 305 HOH B O   1 
HETATM 8303 O  O   . HOH BC 6 .   ? 44.799 33.792  51.818  1.00 56.87 ? 306 HOH B O   1 
HETATM 8304 O  O   . HOH BC 6 .   ? 49.682 -23.634 29.579  1.00 41.11 ? 307 HOH B O   1 
HETATM 8305 O  O   . HOH BC 6 .   ? 52.689 -17.726 26.001  1.00 51.38 ? 308 HOH B O   1 
HETATM 8306 O  O   . HOH BC 6 .   ? 48.389 27.189  64.733  1.00 41.85 ? 309 HOH B O   1 
HETATM 8307 O  O   . HOH BC 6 .   ? 50.768 -1.718  12.653  1.00 48.63 ? 310 HOH B O   1 
HETATM 8308 O  O   . HOH BC 6 .   ? 36.588 28.215  53.005  1.00 35.70 ? 311 HOH B O   1 
HETATM 8309 O  O   . HOH BC 6 .   ? 43.390 -3.239  33.523  1.00 41.10 ? 312 HOH B O   1 
HETATM 8310 O  O   . HOH BC 6 .   ? 54.018 -4.676  23.402  1.00 37.08 ? 313 HOH B O   1 
HETATM 8311 O  O   . HOH BC 6 .   ? 33.896 21.440  55.490  1.00 47.81 ? 314 HOH B O   1 
HETATM 8312 O  O   . HOH BC 6 .   ? 58.840 -7.591  34.569  1.00 32.85 ? 315 HOH B O   1 
HETATM 8313 O  O   . HOH BC 6 .   ? 44.516 8.514   48.965  1.00 46.68 ? 316 HOH B O   1 
HETATM 8314 O  O   . HOH BC 6 .   ? 56.738 -10.081 39.569  1.00 43.63 ? 317 HOH B O   1 
HETATM 8315 O  O   . HOH BC 6 .   ? 44.691 2.097   19.494  1.00 45.56 ? 318 HOH B O   1 
HETATM 8316 O  O   . HOH BC 6 .   ? 34.984 32.181  37.306  1.00 40.12 ? 319 HOH B O   1 
HETATM 8317 O  O   . HOH BC 6 .   ? 54.720 19.580  40.346  1.00 41.32 ? 320 HOH B O   1 
HETATM 8318 O  O   . HOH BC 6 .   ? 39.320 14.329  27.237  1.00 41.71 ? 321 HOH B O   1 
HETATM 8319 O  O   . HOH BC 6 .   ? 45.874 -12.461 28.152  1.00 35.30 ? 322 HOH B O   1 
HETATM 8320 O  O   . HOH BC 6 .   ? 57.903 4.275   27.275  1.00 35.66 ? 323 HOH B O   1 
HETATM 8321 O  O   . HOH BC 6 .   ? 40.115 39.248  45.622  1.00 43.26 ? 324 HOH B O   1 
HETATM 8322 O  O   . HOH BC 6 .   ? 58.375 -11.283 32.735  1.00 40.95 ? 325 HOH B O   1 
HETATM 8323 O  O   . HOH BC 6 .   ? 53.763 25.713  42.811  1.00 44.20 ? 326 HOH B O   1 
HETATM 8324 O  O   . HOH BC 6 .   ? 43.807 19.455  28.582  1.00 34.28 ? 327 HOH B O   1 
HETATM 8325 O  O   . HOH BC 6 .   ? 35.847 22.969  35.124  1.00 47.07 ? 328 HOH B O   1 
HETATM 8326 O  O   . HOH BC 6 .   ? 55.781 8.339   55.518  1.00 26.14 ? 329 HOH B O   1 
HETATM 8327 O  O   . HOH BC 6 .   ? 52.818 -9.829  38.352  1.00 30.68 ? 330 HOH B O   1 
HETATM 8328 O  O   . HOH BC 6 .   ? 45.484 10.629  37.930  1.00 61.04 ? 331 HOH B O   1 
HETATM 8329 O  O   . HOH BC 6 .   ? 58.501 7.191   39.317  1.00 38.22 ? 332 HOH B O   1 
HETATM 8330 O  O   . HOH BC 6 .   ? 49.806 30.134  36.722  1.00 42.14 ? 333 HOH B O   1 
HETATM 8331 O  O   . HOH BC 6 .   ? 56.144 -0.411  39.993  1.00 26.14 ? 334 HOH B O   1 
HETATM 8332 O  O   . HOH BC 6 .   ? 54.191 28.177  41.529  1.00 49.71 ? 335 HOH B O   1 
HETATM 8333 O  O   . HOH BC 6 .   ? 47.327 -12.560 26.024  1.00 32.60 ? 336 HOH B O   1 
HETATM 8334 O  O   . HOH BC 6 .   ? 61.476 4.544   42.808  1.00 39.48 ? 337 HOH B O   1 
HETATM 8335 O  O   . HOH BC 6 .   ? 49.874 -10.946 26.290  1.00 27.67 ? 338 HOH B O   1 
HETATM 8336 O  O   . HOH BC 6 .   ? 52.752 20.319  56.303  1.00 47.81 ? 339 HOH B O   1 
HETATM 8337 O  O   . HOH BC 6 .   ? 57.244 12.922  32.005  1.00 29.88 ? 340 HOH B O   1 
HETATM 8338 O  O   . HOH BC 6 .   ? 33.487 28.712  57.091  1.00 50.10 ? 341 HOH B O   1 
HETATM 8339 O  O   . HOH BC 6 .   ? 58.991 7.064   43.463  1.00 31.22 ? 342 HOH B O   1 
HETATM 8340 O  O   . HOH BC 6 .   ? 54.441 -7.024  17.057  1.00 42.36 ? 343 HOH B O   1 
HETATM 8341 O  O   . HOH BC 6 .   ? 41.071 39.517  42.244  1.00 52.65 ? 344 HOH B O   1 
HETATM 8342 O  O   . HOH BC 6 .   ? 48.308 30.611  59.549  1.00 45.87 ? 345 HOH B O   1 
HETATM 8343 O  O   . HOH BC 6 .   ? 51.867 7.570   19.441  1.00 40.92 ? 346 HOH B O   1 
HETATM 8344 O  O   . HOH BC 6 .   ? 56.639 6.178   29.378  1.00 32.97 ? 347 HOH B O   1 
HETATM 8345 O  O   . HOH BC 6 .   ? 47.727 -10.925 23.719  1.00 26.92 ? 348 HOH B O   1 
HETATM 8346 O  O   . HOH BC 6 .   ? 46.356 12.680  26.556  1.00 36.23 ? 349 HOH B O   1 
HETATM 8347 O  O   . HOH BC 6 .   ? 53.372 0.557   12.522  1.00 56.71 ? 350 HOH B O   1 
HETATM 8348 O  O   . HOH BC 6 .   ? 54.284 -5.961  20.958  1.00 39.74 ? 351 HOH B O   1 
HETATM 8349 O  O   . HOH BC 6 .   ? 50.768 16.573  54.911  1.00 31.96 ? 352 HOH B O   1 
HETATM 8350 O  O   . HOH BC 6 .   ? 37.745 19.021  32.275  1.00 41.56 ? 353 HOH B O   1 
HETATM 8351 O  O   . HOH BC 6 .   ? 41.925 3.592   36.757  1.00 40.20 ? 354 HOH B O   1 
HETATM 8352 O  O   . HOH BC 6 .   ? 45.008 31.431  34.309  1.00 47.65 ? 355 HOH B O   1 
HETATM 8353 O  O   . HOH BC 6 .   ? 56.665 4.639   31.728  1.00 46.44 ? 356 HOH B O   1 
HETATM 8354 O  O   . HOH BC 6 .   ? 52.255 9.389   21.327  1.00 38.02 ? 357 HOH B O   1 
HETATM 8355 O  O   . HOH BC 6 .   ? 40.572 21.794  56.058  1.00 40.76 ? 358 HOH B O   1 
HETATM 8356 O  O   . HOH BC 6 .   ? 40.679 39.668  51.493  1.00 35.03 ? 359 HOH B O   1 
HETATM 8357 O  O   . HOH BC 6 .   ? 60.704 13.357  45.341  1.00 41.96 ? 360 HOH B O   1 
HETATM 8358 O  O   . HOH BC 6 .   ? 65.943 3.242   35.857  1.00 37.99 ? 361 HOH B O   1 
HETATM 8359 O  O   . HOH BC 6 .   ? 47.941 28.542  52.828  1.00 52.04 ? 362 HOH B O   1 
HETATM 8360 O  O   . HOH BC 6 .   ? 51.025 -6.983  15.795  1.00 45.89 ? 363 HOH B O   1 
HETATM 8361 O  O   . HOH BC 6 .   ? 54.417 16.201  23.610  1.00 56.28 ? 364 HOH B O   1 
HETATM 8362 O  O   . HOH BC 6 .   ? 44.609 -9.444  35.678  1.00 36.66 ? 365 HOH B O   1 
HETATM 8363 O  O   . HOH BC 6 .   ? 43.922 38.339  46.470  1.00 44.09 ? 366 HOH B O   1 
HETATM 8364 O  O   . HOH BC 6 .   ? 56.745 -2.066  12.408  1.00 51.08 ? 367 HOH B O   1 
HETATM 8365 O  O   . HOH BC 6 .   ? 41.967 35.054  36.028  1.00 39.42 ? 368 HOH B O   1 
HETATM 8366 O  O   . HOH BC 6 .   ? 53.173 16.476  54.480  1.00 43.39 ? 369 HOH B O   1 
HETATM 8367 O  O   . HOH BC 6 .   ? 51.107 32.964  39.404  1.00 50.50 ? 370 HOH B O   1 
HETATM 8368 O  O   . HOH BC 6 .   ? 58.653 21.543  52.608  1.00 41.22 ? 371 HOH B O   1 
HETATM 8369 O  O   . HOH BC 6 .   ? 53.945 -13.393 20.306  1.00 33.31 ? 372 HOH B O   1 
HETATM 8370 O  O   . HOH BC 6 .   ? 40.274 38.787  48.071  1.00 44.07 ? 373 HOH B O   1 
HETATM 8371 O  O   . HOH BC 6 .   ? 60.554 -6.017  31.179  1.00 41.81 ? 374 HOH B O   1 
HETATM 8372 O  O   . HOH BC 6 .   ? 45.130 38.812  51.698  1.00 52.35 ? 375 HOH B O   1 
HETATM 8373 O  O   . HOH BC 6 .   ? 47.914 0.849   17.325  1.00 46.95 ? 376 HOH B O   1 
HETATM 8374 O  O   . HOH BC 6 .   ? 36.018 19.419  42.288  1.00 52.85 ? 377 HOH B O   1 
HETATM 8375 O  O   . HOH BC 6 .   ? 62.506 6.277   43.593  1.00 50.95 ? 378 HOH B O   1 
HETATM 8376 O  O   . HOH BC 6 .   ? 51.854 25.622  36.582  1.00 42.99 ? 379 HOH B O   1 
HETATM 8377 O  O   . HOH BC 6 .   ? 60.143 -5.218  33.804  1.00 43.38 ? 380 HOH B O   1 
HETATM 8378 O  O   . HOH BC 6 .   ? 59.680 4.120   30.985  1.00 46.46 ? 381 HOH B O   1 
HETATM 8379 O  O   . HOH BC 6 .   ? 52.503 23.647  34.393  1.00 47.32 ? 382 HOH B O   1 
HETATM 8380 O  O   . HOH BC 6 .   ? 56.442 -7.153  20.205  1.00 47.83 ? 383 HOH B O   1 
HETATM 8381 O  O   . HOH BC 6 .   ? 55.610 10.662  19.451  1.00 46.99 ? 384 HOH B O   1 
HETATM 8382 O  O   . HOH BC 6 .   ? 40.790 36.495  33.327  1.00 52.14 ? 385 HOH B O   1 
HETATM 8383 O  O   . HOH BC 6 .   ? 49.673 -1.202  16.552  1.00 40.45 ? 386 HOH B O   1 
HETATM 8384 O  O   . HOH BC 6 .   ? 42.953 37.677  36.991  1.00 44.76 ? 387 HOH B O   1 
HETATM 8385 O  O   . HOH BC 6 .   ? 46.969 -8.402  21.963  1.00 34.35 ? 388 HOH B O   1 
HETATM 8386 O  O   . HOH BC 6 .   ? 50.714 18.394  57.110  1.00 40.76 ? 389 HOH B O   1 
HETATM 8387 O  O   . HOH BC 6 .   ? 52.636 -6.442  13.366  1.00 51.54 ? 390 HOH B O   1 
HETATM 8388 O  O   . HOH BC 6 .   ? 52.224 -21.558 33.766  1.00 41.62 ? 391 HOH B O   1 
HETATM 8389 O  O   . HOH BC 6 .   ? 48.676 31.984  32.533  1.00 50.94 ? 392 HOH B O   1 
HETATM 8390 O  O   . HOH BC 6 .   ? 59.366 9.454   42.015  1.00 37.88 ? 393 HOH B O   1 
HETATM 8391 O  O   . HOH BC 6 .   ? 57.794 10.053  39.417  1.00 45.50 ? 394 HOH B O   1 
HETATM 8392 O  O   . HOH BC 6 .   ? 44.184 34.628  34.607  1.00 42.60 ? 395 HOH B O   1 
HETATM 8393 O  O   . HOH CC 6 .   ? 18.333 33.130  -15.430 1.00 47.10 ? 301 HOH C O   1 
HETATM 8394 O  O   . HOH CC 6 .   ? 21.451 58.915  -6.689  1.00 47.12 ? 302 HOH C O   1 
HETATM 8395 O  O   . HOH CC 6 .   ? 39.748 64.963  13.108  1.00 42.20 ? 303 HOH C O   1 
HETATM 8396 O  O   . HOH CC 6 .   ? 40.555 36.423  -10.965 1.00 46.72 ? 304 HOH C O   1 
HETATM 8397 O  O   . HOH CC 6 .   ? 23.621 55.572  4.205   1.00 33.18 ? 305 HOH C O   1 
HETATM 8398 O  O   . HOH CC 6 .   ? 33.221 39.005  -18.777 1.00 46.84 ? 306 HOH C O   1 
HETATM 8399 O  O   . HOH CC 6 .   ? 25.112 60.719  1.211   1.00 40.10 ? 307 HOH C O   1 
HETATM 8400 O  O   . HOH CC 6 .   ? 27.207 48.232  10.111  1.00 47.32 ? 308 HOH C O   1 
HETATM 8401 O  O   . HOH CC 6 .   ? 31.534 47.572  9.922   1.00 40.29 ? 309 HOH C O   1 
HETATM 8402 O  O   . HOH CC 6 .   ? 44.087 18.738  -18.082 1.00 37.62 ? 310 HOH C O   1 
HETATM 8403 O  O   . HOH CC 6 .   ? 42.528 31.509  -20.217 1.00 51.73 ? 311 HOH C O   1 
HETATM 8404 O  O   . HOH CC 6 .   ? 44.993 25.560  -17.252 1.00 40.18 ? 312 HOH C O   1 
HETATM 8405 O  O   . HOH CC 6 .   ? 33.062 41.462  3.158   1.00 25.45 ? 313 HOH C O   1 
HETATM 8406 O  O   . HOH CC 6 .   ? 21.654 44.247  -0.986  1.00 37.95 ? 314 HOH C O   1 
HETATM 8407 O  O   . HOH CC 6 .   ? 23.749 25.757  -15.496 1.00 43.17 ? 315 HOH C O   1 
HETATM 8408 O  O   . HOH CC 6 .   ? 37.235 26.286  -30.196 1.00 40.33 ? 316 HOH C O   1 
HETATM 8409 O  O   . HOH CC 6 .   ? 18.464 28.944  -21.738 1.00 39.80 ? 317 HOH C O   1 
HETATM 8410 O  O   . HOH CC 6 .   ? 32.025 51.463  11.753  1.00 48.30 ? 318 HOH C O   1 
HETATM 8411 O  O   . HOH CC 6 .   ? 32.266 61.620  4.419   1.00 35.09 ? 319 HOH C O   1 
HETATM 8412 O  O   . HOH CC 6 .   ? 17.725 31.239  -24.373 1.00 41.99 ? 320 HOH C O   1 
HETATM 8413 O  O   . HOH CC 6 .   ? 27.598 24.372  -25.237 1.00 43.73 ? 321 HOH C O   1 
HETATM 8414 O  O   . HOH CC 6 .   ? 42.017 30.907  -23.162 1.00 44.93 ? 322 HOH C O   1 
HETATM 8415 O  O   . HOH CC 6 .   ? 30.689 59.517  5.126   1.00 27.72 ? 323 HOH C O   1 
HETATM 8416 O  O   . HOH CC 6 .   ? 15.734 51.972  -5.424  1.00 38.38 ? 324 HOH C O   1 
HETATM 8417 O  O   . HOH CC 6 .   ? 22.157 41.016  -29.796 1.00 47.05 ? 325 HOH C O   1 
HETATM 8418 O  O   . HOH CC 6 .   ? 19.967 30.759  -16.657 1.00 48.80 ? 326 HOH C O   1 
HETATM 8419 O  O   . HOH CC 6 .   ? 41.988 13.329  -20.781 1.00 42.29 ? 327 HOH C O   1 
HETATM 8420 O  O   . HOH CC 6 .   ? 34.657 48.330  -10.116 1.00 44.16 ? 328 HOH C O   1 
HETATM 8421 O  O   . HOH CC 6 .   ? 15.452 63.145  0.102   1.00 48.65 ? 329 HOH C O   1 
HETATM 8422 O  O   . HOH CC 6 .   ? 19.743 60.789  5.954   1.00 50.91 ? 330 HOH C O   1 
HETATM 8423 O  O   . HOH CC 6 .   ? 38.062 49.482  6.953   1.00 32.56 ? 331 HOH C O   1 
HETATM 8424 O  O   . HOH CC 6 .   ? 41.061 26.537  -2.766  1.00 27.62 ? 332 HOH C O   1 
HETATM 8425 O  O   . HOH CC 6 .   ? 37.354 23.895  -10.057 1.00 42.07 ? 333 HOH C O   1 
HETATM 8426 O  O   . HOH CC 6 .   ? 34.019 50.288  -14.266 1.00 62.27 ? 334 HOH C O   1 
HETATM 8427 O  O   . HOH CC 6 .   ? 27.102 42.425  6.770   1.00 36.91 ? 335 HOH C O   1 
HETATM 8428 O  O   . HOH CC 6 .   ? 17.637 32.375  -26.722 1.00 52.29 ? 336 HOH C O   1 
HETATM 8429 O  O   . HOH CC 6 .   ? 25.695 44.179  -23.438 1.00 42.75 ? 337 HOH C O   1 
HETATM 8430 O  O   . HOH CC 6 .   ? 35.063 53.335  -4.575  1.00 40.00 ? 338 HOH C O   1 
HETATM 8431 O  O   . HOH CC 6 .   ? 22.190 57.857  5.144   1.00 43.47 ? 339 HOH C O   1 
HETATM 8432 O  O   . HOH CC 6 .   ? 19.008 30.475  -30.824 1.00 35.23 ? 340 HOH C O   1 
HETATM 8433 O  O   . HOH CC 6 .   ? 38.661 24.760  -12.020 1.00 35.57 ? 341 HOH C O   1 
HETATM 8434 O  O   . HOH CC 6 .   ? 22.636 62.314  8.420   1.00 56.87 ? 342 HOH C O   1 
HETATM 8435 O  O   . HOH CC 6 .   ? 29.349 62.126  3.445   1.00 34.70 ? 343 HOH C O   1 
HETATM 8436 O  O   . HOH CC 6 .   ? 32.237 22.318  -4.021  1.00 66.13 ? 344 HOH C O   1 
HETATM 8437 O  O   . HOH CC 6 .   ? 24.255 34.548  -34.406 1.00 35.85 ? 345 HOH C O   1 
HETATM 8438 O  O   . HOH CC 6 .   ? 36.178 37.279  -24.023 1.00 58.04 ? 346 HOH C O   1 
HETATM 8439 O  O   . HOH CC 6 .   ? 37.071 23.580  -28.767 1.00 39.81 ? 347 HOH C O   1 
HETATM 8440 O  O   . HOH CC 6 .   ? 31.129 18.196  -16.021 1.00 52.30 ? 348 HOH C O   1 
HETATM 8441 O  O   . HOH CC 6 .   ? 27.111 21.410  -34.421 1.00 49.86 ? 349 HOH C O   1 
HETATM 8442 O  O   . HOH CC 6 .   ? 27.718 38.309  -27.744 1.00 48.74 ? 350 HOH C O   1 
HETATM 8443 O  O   . HOH CC 6 .   ? 29.150 18.455  -34.927 1.00 46.87 ? 351 HOH C O   1 
HETATM 8444 O  O   . HOH CC 6 .   ? 40.593 13.361  -18.033 1.00 47.13 ? 352 HOH C O   1 
HETATM 8445 O  O   . HOH CC 6 .   ? 25.592 62.708  9.675   1.00 40.12 ? 353 HOH C O   1 
HETATM 8446 O  O   . HOH CC 6 .   ? 20.366 47.299  -12.808 1.00 42.46 ? 354 HOH C O   1 
HETATM 8447 O  O   . HOH CC 6 .   ? 19.024 59.340  -4.098  1.00 41.14 ? 355 HOH C O   1 
HETATM 8448 O  O   . HOH CC 6 .   ? 30.811 33.445  0.161   1.00 34.94 ? 356 HOH C O   1 
HETATM 8449 O  O   . HOH CC 6 .   ? 31.376 29.677  3.821   1.00 35.09 ? 357 HOH C O   1 
HETATM 8450 O  O   . HOH CC 6 .   ? 20.041 23.750  -31.289 1.00 49.50 ? 358 HOH C O   1 
HETATM 8451 O  O   . HOH CC 6 .   ? 29.708 44.954  -17.976 1.00 52.76 ? 359 HOH C O   1 
HETATM 8452 O  O   . HOH CC 6 .   ? 17.888 57.711  -7.489  1.00 51.15 ? 360 HOH C O   1 
HETATM 8453 O  O   . HOH CC 6 .   ? 29.213 58.667  -5.526  1.00 44.77 ? 361 HOH C O   1 
HETATM 8454 O  O   . HOH CC 6 .   ? 40.231 34.823  -33.285 1.00 52.46 ? 362 HOH C O   1 
HETATM 8455 O  O   . HOH CC 6 .   ? 30.995 41.186  7.148   1.00 32.72 ? 363 HOH C O   1 
HETATM 8456 O  O   . HOH CC 6 .   ? 20.286 63.302  3.750   1.00 44.21 ? 364 HOH C O   1 
HETATM 8457 O  O   . HOH CC 6 .   ? 41.352 26.035  -23.131 1.00 44.71 ? 365 HOH C O   1 
HETATM 8458 O  O   . HOH CC 6 .   ? 43.138 43.340  -8.567  1.00 57.88 ? 366 HOH C O   1 
HETATM 8459 O  O   . HOH CC 6 .   ? 16.006 52.256  4.058   1.00 50.17 ? 367 HOH C O   1 
HETATM 8460 O  O   . HOH CC 6 .   ? 12.541 60.188  3.857   1.00 54.47 ? 368 HOH C O   1 
HETATM 8461 O  O   . HOH CC 6 .   ? 26.929 58.972  9.733   1.00 22.16 ? 369 HOH C O   1 
HETATM 8462 O  O   . HOH CC 6 .   ? 15.920 49.754  -6.523  1.00 40.00 ? 370 HOH C O   1 
HETATM 8463 O  O   . HOH CC 6 .   ? 35.138 37.319  10.031  1.00 47.27 ? 371 HOH C O   1 
HETATM 8464 O  O   . HOH CC 6 .   ? 16.985 59.527  6.535   1.00 51.27 ? 372 HOH C O   1 
HETATM 8465 O  O   . HOH CC 6 .   ? 29.445 43.515  8.734   1.00 34.14 ? 373 HOH C O   1 
HETATM 8466 O  O   . HOH CC 6 .   ? 29.098 46.370  9.325   1.00 44.30 ? 374 HOH C O   1 
HETATM 8467 O  O   . HOH CC 6 .   ? 29.206 40.634  5.482   1.00 30.99 ? 375 HOH C O   1 
HETATM 8468 O  O   . HOH CC 6 .   ? 21.424 57.960  7.639   1.00 52.03 ? 376 HOH C O   1 
HETATM 8469 O  O   . HOH CC 6 .   ? 38.809 22.400  -13.342 1.00 37.41 ? 377 HOH C O   1 
HETATM 8470 O  O   . HOH CC 6 .   ? 18.065 28.041  -31.806 1.00 57.15 ? 378 HOH C O   1 
HETATM 8471 O  O   . HOH CC 6 .   ? 23.913 58.802  9.721   1.00 51.72 ? 379 HOH C O   1 
HETATM 8472 O  O   . HOH CC 6 .   ? 18.501 60.440  -1.600  1.00 39.79 ? 380 HOH C O   1 
HETATM 8473 O  O   . HOH CC 6 .   ? 40.605 59.604  13.844  1.00 40.03 ? 381 HOH C O   1 
HETATM 8474 O  O   . HOH CC 6 .   ? 16.909 30.425  -28.731 1.00 42.04 ? 382 HOH C O   1 
HETATM 8475 O  O   . HOH DC 6 .   ? 45.275 -0.554  48.757  1.00 42.77 ? 301 HOH D O   1 
HETATM 8476 O  O   . HOH DC 6 .   ? 45.702 -31.976 52.076  1.00 46.38 ? 302 HOH D O   1 
HETATM 8477 O  O   . HOH DC 6 .   ? 59.436 1.705   68.560  1.00 50.24 ? 303 HOH D O   1 
HETATM 8478 O  O   . HOH DC 6 .   ? 45.569 -8.846  38.492  1.00 40.86 ? 304 HOH D O   1 
HETATM 8479 O  O   . HOH DC 6 .   ? 46.678 21.079  62.935  1.00 35.35 ? 305 HOH D O   1 
HETATM 8480 O  O   . HOH DC 6 .   ? 52.848 13.395  74.223  1.00 34.28 ? 306 HOH D O   1 
HETATM 8481 O  O   . HOH DC 6 .   ? 55.644 -16.277 60.804  1.00 54.89 ? 307 HOH D O   1 
HETATM 8482 O  O   . HOH DC 6 .   ? 46.853 14.255  76.420  1.00 38.70 ? 308 HOH D O   1 
HETATM 8483 O  O   . HOH DC 6 .   ? 56.843 17.062  62.792  1.00 40.68 ? 309 HOH D O   1 
HETATM 8484 O  O   . HOH DC 6 .   ? 45.011 20.238  71.555  1.00 32.84 ? 310 HOH D O   1 
HETATM 8485 O  O   . HOH DC 6 .   ? 58.475 -3.395  65.369  1.00 42.46 ? 311 HOH D O   1 
HETATM 8486 O  O   . HOH DC 6 .   ? 52.294 0.929   77.906  1.00 42.02 ? 312 HOH D O   1 
HETATM 8487 O  O   . HOH DC 6 .   ? 49.088 26.203  71.828  1.00 46.69 ? 313 HOH D O   1 
HETATM 8488 O  O   . HOH DC 6 .   ? 64.184 -9.966  48.965  1.00 38.49 ? 314 HOH D O   1 
HETATM 8489 O  O   . HOH DC 6 .   ? 49.633 -13.261 34.727  1.00 35.58 ? 315 HOH D O   1 
HETATM 8490 O  O   . HOH DC 6 .   ? 49.810 -22.830 50.878  1.00 42.91 ? 316 HOH D O   1 
HETATM 8491 O  O   . HOH DC 6 .   ? 55.902 20.475  64.947  1.00 41.13 ? 317 HOH D O   1 
HETATM 8492 O  O   . HOH DC 6 .   ? 58.681 2.341   58.120  1.00 41.82 ? 318 HOH D O   1 
HETATM 8493 O  O   . HOH DC 6 .   ? 55.452 9.428   57.852  1.00 30.43 ? 319 HOH D O   1 
HETATM 8494 O  O   . HOH DC 6 .   ? 52.062 -18.817 32.826  1.00 41.85 ? 320 HOH D O   1 
HETATM 8495 O  O   . HOH DC 6 .   ? 57.294 -8.621  70.550  1.00 49.44 ? 321 HOH D O   1 
HETATM 8496 O  O   . HOH DC 6 .   ? 56.486 4.605   65.928  1.00 43.65 ? 322 HOH D O   1 
HETATM 8497 O  O   . HOH DC 6 .   ? 50.789 18.351  59.357  1.00 33.63 ? 323 HOH D O   1 
HETATM 8498 O  O   . HOH DC 6 .   ? 59.107 2.311   54.485  1.00 29.57 ? 324 HOH D O   1 
HETATM 8499 O  O   . HOH DC 6 .   ? 40.793 -21.841 44.739  1.00 37.73 ? 325 HOH D O   1 
HETATM 8500 O  O   . HOH DC 6 .   ? 55.205 -11.388 41.403  1.00 41.16 ? 326 HOH D O   1 
HETATM 8501 O  O   . HOH DC 6 .   ? 56.762 3.253   68.231  1.00 42.62 ? 327 HOH D O   1 
HETATM 8502 O  O   . HOH DC 6 .   ? 52.456 15.809  80.725  1.00 48.19 ? 328 HOH D O   1 
HETATM 8503 O  O   . HOH DC 6 .   ? 47.548 19.037  71.418  1.00 29.34 ? 329 HOH D O   1 
HETATM 8504 O  O   . HOH DC 6 .   ? 44.552 5.193   78.151  1.00 52.71 ? 330 HOH D O   1 
HETATM 8505 O  O   . HOH DC 6 .   ? 43.391 19.996  69.536  1.00 29.00 ? 331 HOH D O   1 
HETATM 8506 O  O   . HOH DC 6 .   ? 46.917 -27.560 61.506  1.00 37.85 ? 332 HOH D O   1 
HETATM 8507 O  O   . HOH DC 6 .   ? 56.486 0.798   42.249  1.00 28.88 ? 333 HOH D O   1 
HETATM 8508 O  O   . HOH DC 6 .   ? 61.392 5.411   55.096  1.00 43.16 ? 334 HOH D O   1 
HETATM 8509 O  O   . HOH DC 6 .   ? 49.240 -30.670 50.731  1.00 45.34 ? 335 HOH D O   1 
HETATM 8510 O  O   . HOH DC 6 .   ? 48.012 -4.814  71.134  1.00 38.49 ? 336 HOH D O   1 
HETATM 8511 O  O   . HOH DC 6 .   ? 47.268 -31.908 55.571  1.00 45.62 ? 337 HOH D O   1 
HETATM 8512 O  O   . HOH DC 6 .   ? 43.087 -21.863 43.125  1.00 33.92 ? 338 HOH D O   1 
HETATM 8513 O  O   . HOH DC 6 .   ? 49.228 -24.130 64.255  1.00 49.53 ? 339 HOH D O   1 
HETATM 8514 O  O   . HOH DC 6 .   ? 57.475 -17.048 44.677  1.00 55.78 ? 340 HOH D O   1 
HETATM 8515 O  O   . HOH DC 6 .   ? 52.775 14.690  76.758  1.00 44.65 ? 341 HOH D O   1 
HETATM 8516 O  O   . HOH DC 6 .   ? 57.243 -16.502 54.736  1.00 35.24 ? 342 HOH D O   1 
HETATM 8517 O  O   . HOH DC 6 .   ? 39.929 -11.980 44.123  1.00 44.10 ? 343 HOH D O   1 
HETATM 8518 O  O   . HOH DC 6 .   ? 57.239 -10.397 56.889  1.00 37.59 ? 344 HOH D O   1 
HETATM 8519 O  O   . HOH DC 6 .   ? 54.050 -21.369 60.823  1.00 42.16 ? 345 HOH D O   1 
HETATM 8520 O  O   . HOH DC 6 .   ? 45.529 18.501  74.143  1.00 38.92 ? 346 HOH D O   1 
HETATM 8521 O  O   . HOH DC 6 .   ? 53.229 -1.011  76.157  1.00 50.55 ? 347 HOH D O   1 
HETATM 8522 O  O   . HOH DC 6 .   ? 42.370 10.268  63.957  1.00 38.58 ? 348 HOH D O   1 
HETATM 8523 O  O   . HOH DC 6 .   ? 40.318 -12.592 65.041  1.00 44.00 ? 349 HOH D O   1 
HETATM 8524 O  O   . HOH DC 6 .   ? 52.501 -7.841  42.760  1.00 28.93 ? 350 HOH D O   1 
HETATM 8525 O  O   . HOH DC 6 .   ? 59.103 15.758  66.533  1.00 40.26 ? 351 HOH D O   1 
HETATM 8526 O  O   . HOH DC 6 .   ? 61.490 -4.237  52.390  1.00 43.55 ? 352 HOH D O   1 
HETATM 8527 O  O   . HOH DC 6 .   ? 41.671 3.470   60.916  1.00 45.70 ? 353 HOH D O   1 
HETATM 8528 O  O   . HOH DC 6 .   ? 41.359 11.383  68.554  1.00 40.97 ? 354 HOH D O   1 
HETATM 8529 O  O   . HOH DC 6 .   ? 57.795 -7.772  54.611  1.00 44.05 ? 355 HOH D O   1 
HETATM 8530 O  O   . HOH DC 6 .   ? 47.053 3.463   79.738  1.00 56.89 ? 356 HOH D O   1 
HETATM 8531 O  O   . HOH DC 6 .   ? 51.757 -20.247 44.501  1.00 47.71 ? 357 HOH D O   1 
HETATM 8532 O  O   . HOH DC 6 .   ? 54.143 -17.701 34.108  1.00 46.67 ? 358 HOH D O   1 
HETATM 8533 O  O   . HOH DC 6 .   ? 54.321 19.421  58.215  1.00 45.34 ? 359 HOH D O   1 
HETATM 8534 O  O   . HOH DC 6 .   ? 52.540 -22.447 38.162  1.00 43.80 ? 360 HOH D O   1 
HETATM 8535 O  O   . HOH DC 6 .   ? 47.589 7.114   80.172  1.00 53.62 ? 361 HOH D O   1 
HETATM 8536 O  O   . HOH DC 6 .   ? 53.568 -24.325 51.847  1.00 45.75 ? 362 HOH D O   1 
HETATM 8537 O  O   . HOH DC 6 .   ? 60.974 -12.076 45.014  1.00 28.00 ? 363 HOH D O   1 
HETATM 8538 O  O   . HOH DC 6 .   ? 39.588 -3.160  54.737  1.00 48.44 ? 364 HOH D O   1 
HETATM 8539 O  O   . HOH DC 6 .   ? 42.627 16.782  62.054  1.00 42.31 ? 365 HOH D O   1 
HETATM 8540 O  O   . HOH DC 6 .   ? 37.565 -22.545 40.456  1.00 47.54 ? 366 HOH D O   1 
HETATM 8541 O  O   . HOH DC 6 .   ? 45.863 -31.734 49.563  1.00 44.82 ? 367 HOH D O   1 
HETATM 8542 O  O   . HOH DC 6 .   ? 63.140 -2.606  50.745  1.00 47.11 ? 368 HOH D O   1 
HETATM 8543 O  O   . HOH DC 6 .   ? 46.387 -32.689 46.071  1.00 37.89 ? 369 HOH D O   1 
HETATM 8544 O  O   . HOH DC 6 .   ? 41.086 6.757   57.943  1.00 43.01 ? 370 HOH D O   1 
HETATM 8545 O  O   . HOH DC 6 .   ? 57.866 5.014   70.367  1.00 45.03 ? 371 HOH D O   1 
HETATM 8546 O  O   . HOH DC 6 .   ? 60.638 9.632   69.251  1.00 52.40 ? 372 HOH D O   1 
HETATM 8547 O  O   . HOH DC 6 .   ? 59.488 13.199  61.991  1.00 28.87 ? 373 HOH D O   1 
HETATM 8548 O  O   . HOH DC 6 .   ? 52.710 20.733  73.916  1.00 23.81 ? 374 HOH D O   1 
HETATM 8549 O  O   . HOH DC 6 .   ? 49.560 15.461  81.817  1.00 44.59 ? 375 HOH D O   1 
HETATM 8550 O  O   . HOH DC 6 .   ? 36.450 -23.227 58.052  1.00 49.57 ? 376 HOH D O   1 
HETATM 8551 O  O   . HOH DC 6 .   ? 48.148 -30.185 60.211  1.00 45.37 ? 377 HOH D O   1 
HETATM 8552 O  O   . HOH DC 6 .   ? 52.618 -9.905  41.077  1.00 36.09 ? 378 HOH D O   1 
HETATM 8553 O  O   . HOH DC 6 .   ? 51.832 -21.005 42.422  1.00 49.54 ? 379 HOH D O   1 
HETATM 8554 O  O   . HOH DC 6 .   ? 60.566 8.376   66.508  1.00 47.58 ? 380 HOH D O   1 
HETATM 8555 O  O   . HOH DC 6 .   ? 60.458 7.554   71.466  1.00 54.69 ? 381 HOH D O   1 
HETATM 8556 O  O   . HOH DC 6 .   ? 45.122 16.111  75.526  1.00 37.75 ? 382 HOH D O   1 
HETATM 8557 O  O   . HOH DC 6 .   ? 54.437 16.353  77.431  1.00 49.60 ? 383 HOH D O   1 
HETATM 8558 O  O   . HOH DC 6 .   ? 48.675 9.239   81.368  1.00 42.90 ? 384 HOH D O   1 
HETATM 8559 O  O   . HOH DC 6 .   ? 61.933 15.179  67.367  1.00 53.89 ? 385 HOH D O   1 
HETATM 8560 O  O   . HOH DC 6 .   ? 48.205 29.986  63.722  1.00 41.05 ? 386 HOH D O   1 
HETATM 8561 O  O   . HOH DC 6 .   ? 51.520 26.924  73.517  1.00 46.76 ? 387 HOH D O   1 
HETATM 8562 O  O   . HOH DC 6 .   ? 58.656 18.847  61.680  1.00 44.34 ? 388 HOH D O   1 
HETATM 8563 O  O   . HOH DC 6 .   ? 49.124 -26.822 63.174  1.00 39.01 ? 389 HOH D O   1 
HETATM 8564 O  O   . HOH DC 6 .   ? 59.951 -0.106  55.912  1.00 36.81 ? 390 HOH D O   1 
HETATM 8565 O  O   . HOH DC 6 .   ? 58.365 -0.504  58.380  1.00 44.57 ? 391 HOH D O   1 
HETATM 8566 O  O   . HOH EC 6 .   ? 2.039  27.540  -1.202  1.00 47.11 ? 301 HOH E O   1 
HETATM 8567 O  O   . HOH EC 6 .   ? -3.870 30.570  -3.201  1.00 45.16 ? 302 HOH E O   1 
HETATM 8568 O  O   . HOH EC 6 .   ? 24.978 47.956  25.189  1.00 48.13 ? 303 HOH E O   1 
HETATM 8569 O  O   . HOH EC 6 .   ? 22.438 49.393  23.858  1.00 41.89 ? 304 HOH E O   1 
HETATM 8570 O  O   . HOH EC 6 .   ? 31.267 47.701  41.913  1.00 68.42 ? 305 HOH E O   1 
HETATM 8571 O  O   . HOH EC 6 .   ? -5.376 22.926  -4.571  1.00 37.70 ? 306 HOH E O   1 
HETATM 8572 O  O   . HOH EC 6 .   ? 1.029  40.708  4.369   1.00 37.63 ? 307 HOH E O   1 
HETATM 8573 O  O   . HOH EC 6 .   ? 7.275  41.375  28.046  1.00 44.71 ? 308 HOH E O   1 
HETATM 8574 O  O   . HOH EC 6 .   ? 45.758 28.977  29.415  1.00 41.73 ? 309 HOH E O   1 
HETATM 8575 O  O   . HOH EC 6 .   ? 6.973  33.001  -3.140  1.00 47.31 ? 310 HOH E O   1 
HETATM 8576 O  O   . HOH EC 6 .   ? 33.499 44.809  43.655  1.00 38.23 ? 311 HOH E O   1 
HETATM 8577 O  O   . HOH EC 6 .   ? 41.707 27.981  24.502  1.00 39.97 ? 312 HOH E O   1 
HETATM 8578 O  O   . HOH EC 6 .   ? 3.696  25.902  2.335   1.00 36.16 ? 313 HOH E O   1 
HETATM 8579 O  O   . HOH EC 6 .   ? 22.698 26.798  19.969  1.00 49.21 ? 314 HOH E O   1 
HETATM 8580 O  O   . HOH EC 6 .   ? 30.549 45.401  24.540  1.00 41.43 ? 315 HOH E O   1 
HETATM 8581 O  O   . HOH EC 6 .   ? 12.785 39.960  32.031  1.00 38.15 ? 316 HOH E O   1 
HETATM 8582 O  O   . HOH EC 6 .   ? 31.318 49.199  40.006  1.00 48.09 ? 317 HOH E O   1 
HETATM 8583 O  O   . HOH EC 6 .   ? 10.325 33.687  -1.228  1.00 43.26 ? 318 HOH E O   1 
HETATM 8584 O  O   . HOH EC 6 .   ? 28.258 35.623  -0.919  1.00 41.01 ? 319 HOH E O   1 
HETATM 8585 O  O   . HOH EC 6 .   ? -3.402 31.023  4.239   1.00 29.97 ? 320 HOH E O   1 
HETATM 8586 O  O   . HOH EC 6 .   ? 35.669 45.529  39.908  1.00 46.00 ? 321 HOH E O   1 
HETATM 8587 O  O   . HOH EC 6 .   ? -4.548 33.825  4.966   1.00 40.63 ? 322 HOH E O   1 
HETATM 8588 O  O   . HOH EC 6 .   ? 32.438 31.760  38.957  1.00 37.59 ? 323 HOH E O   1 
HETATM 8589 O  O   . HOH EC 6 .   ? 16.609 33.543  5.478   1.00 29.72 ? 324 HOH E O   1 
HETATM 8590 O  O   . HOH EC 6 .   ? 3.368  48.814  14.229  1.00 39.62 ? 325 HOH E O   1 
HETATM 8591 O  O   . HOH EC 6 .   ? 34.411 32.248  18.563  1.00 34.64 ? 326 HOH E O   1 
HETATM 8592 O  O   . HOH EC 6 .   ? 37.362 38.106  33.329  1.00 48.47 ? 327 HOH E O   1 
HETATM 8593 O  O   . HOH EC 6 .   ? 4.148  31.487  -2.988  1.00 48.84 ? 328 HOH E O   1 
HETATM 8594 O  O   . HOH EC 6 .   ? -2.586 28.694  5.247   1.00 32.90 ? 329 HOH E O   1 
HETATM 8595 O  O   . HOH EC 6 .   ? 26.392 49.645  30.180  1.00 43.52 ? 330 HOH E O   1 
HETATM 8596 O  O   . HOH EC 6 .   ? -1.563 32.826  3.477   1.00 31.27 ? 331 HOH E O   1 
HETATM 8597 O  O   . HOH EC 6 .   ? 24.256 37.003  8.280   1.00 32.82 ? 332 HOH E O   1 
HETATM 8598 O  O   . HOH EC 6 .   ? 10.254 30.396  18.773  1.00 43.59 ? 333 HOH E O   1 
HETATM 8599 O  O   . HOH EC 6 .   ? 25.045 48.973  39.523  1.00 36.06 ? 334 HOH E O   1 
HETATM 8600 O  O   . HOH EC 6 .   ? 28.447 26.205  32.059  1.00 43.05 ? 335 HOH E O   1 
HETATM 8601 O  O   . HOH EC 6 .   ? 5.264  29.582  13.079  1.00 42.57 ? 336 HOH E O   1 
HETATM 8602 O  O   . HOH EC 6 .   ? -3.871 37.999  7.259   1.00 37.79 ? 337 HOH E O   1 
HETATM 8603 O  O   . HOH EC 6 .   ? 29.462 40.089  11.459  1.00 42.79 ? 338 HOH E O   1 
HETATM 8604 O  O   . HOH EC 6 .   ? 26.222 43.642  19.455  1.00 36.11 ? 339 HOH E O   1 
HETATM 8605 O  O   . HOH EC 6 .   ? 32.651 28.183  11.588  1.00 25.54 ? 340 HOH E O   1 
HETATM 8606 O  O   . HOH EC 6 .   ? 33.896 30.648  20.684  1.00 35.34 ? 341 HOH E O   1 
HETATM 8607 O  O   . HOH EC 6 .   ? -1.295 41.473  3.396   1.00 42.31 ? 342 HOH E O   1 
HETATM 8608 O  O   . HOH EC 6 .   ? -6.980 42.670  5.256   1.00 39.60 ? 343 HOH E O   1 
HETATM 8609 O  O   . HOH EC 6 .   ? 19.346 33.472  28.136  1.00 47.80 ? 344 HOH E O   1 
HETATM 8610 O  O   . HOH EC 6 .   ? 9.477  27.345  1.674   1.00 38.23 ? 345 HOH E O   1 
HETATM 8611 O  O   . HOH EC 6 .   ? 17.634 46.544  13.249  1.00 39.96 ? 346 HOH E O   1 
HETATM 8612 O  O   . HOH EC 6 .   ? 12.077 44.449  9.495   1.00 45.12 ? 347 HOH E O   1 
HETATM 8613 O  O   . HOH EC 6 .   ? 5.842  49.039  15.112  1.00 42.67 ? 348 HOH E O   1 
HETATM 8614 O  O   . HOH EC 6 .   ? 16.090 39.901  36.820  1.00 50.65 ? 349 HOH E O   1 
HETATM 8615 O  O   . HOH EC 6 .   ? 13.258 41.772  8.562   1.00 45.81 ? 350 HOH E O   1 
HETATM 8616 O  O   . HOH EC 6 .   ? 19.898 33.253  34.062  1.00 59.32 ? 351 HOH E O   1 
HETATM 8617 O  O   . HOH EC 6 .   ? 8.895  44.468  21.631  1.00 39.21 ? 352 HOH E O   1 
HETATM 8618 O  O   . HOH EC 6 .   ? 45.699 33.929  28.067  1.00 59.23 ? 353 HOH E O   1 
HETATM 8619 O  O   . HOH EC 6 .   ? 15.777 37.064  22.279  1.00 55.07 ? 354 HOH E O   1 
HETATM 8620 O  O   . HOH EC 6 .   ? 29.585 20.749  23.646  1.00 43.60 ? 355 HOH E O   1 
HETATM 8621 O  O   . HOH EC 6 .   ? 28.404 46.787  23.075  1.00 56.72 ? 356 HOH E O   1 
HETATM 8622 O  O   . HOH EC 6 .   ? -5.773 37.332  -0.910  1.00 42.05 ? 357 HOH E O   1 
HETATM 8623 O  O   . HOH EC 6 .   ? 8.930  38.305  -1.720  1.00 47.92 ? 358 HOH E O   1 
HETATM 8624 O  O   . HOH EC 6 .   ? 43.383 34.866  31.859  1.00 49.39 ? 359 HOH E O   1 
HETATM 8625 O  O   . HOH EC 6 .   ? 31.117 41.030  16.620  1.00 52.11 ? 360 HOH E O   1 
HETATM 8626 O  O   . HOH EC 6 .   ? 39.770 36.200  31.001  1.00 45.13 ? 361 HOH E O   1 
HETATM 8627 O  O   . HOH EC 6 .   ? 10.336 43.683  2.146   1.00 40.99 ? 362 HOH E O   1 
HETATM 8628 O  O   . HOH EC 6 .   ? 3.942  25.186  8.316   1.00 39.30 ? 363 HOH E O   1 
HETATM 8629 O  O   . HOH EC 6 .   ? 35.308 42.760  43.382  1.00 43.99 ? 364 HOH E O   1 
HETATM 8630 O  O   . HOH EC 6 .   ? 38.509 41.460  43.804  1.00 39.92 ? 365 HOH E O   1 
HETATM 8631 O  O   . HOH EC 6 .   ? -3.293 44.590  12.708  1.00 40.44 ? 366 HOH E O   1 
HETATM 8632 O  O   . HOH EC 6 .   ? -1.675 36.667  -1.134  1.00 24.40 ? 367 HOH E O   1 
HETATM 8633 O  O   . HOH EC 6 .   ? 9.996  45.237  7.386   1.00 35.87 ? 368 HOH E O   1 
HETATM 8634 O  O   . HOH EC 6 .   ? 29.374 40.471  16.516  1.00 48.34 ? 369 HOH E O   1 
HETATM 8635 O  O   . HOH EC 6 .   ? 13.579 36.794  0.036   1.00 34.97 ? 370 HOH E O   1 
HETATM 8636 O  O   . HOH EC 6 .   ? 37.280 37.150  30.845  1.00 40.23 ? 371 HOH E O   1 
HETATM 8637 O  O   . HOH EC 6 .   ? 20.678 38.849  42.808  1.00 60.48 ? 372 HOH E O   1 
HETATM 8638 O  O   . HOH EC 6 .   ? 35.954 36.955  12.341  1.00 49.79 ? 373 HOH E O   1 
HETATM 8639 O  O   . HOH EC 6 .   ? 11.616 36.684  -0.674  1.00 43.92 ? 374 HOH E O   1 
HETATM 8640 O  O   . HOH EC 6 .   ? 36.165 30.903  21.920  1.00 39.13 ? 375 HOH E O   1 
HETATM 8641 O  O   . HOH EC 6 .   ? 27.461 50.359  40.328  1.00 47.09 ? 376 HOH E O   1 
HETATM 8642 O  O   . HOH EC 6 .   ? 10.473 43.642  -0.633  1.00 51.95 ? 377 HOH E O   1 
HETATM 8643 O  O   . HOH EC 6 .   ? 3.173  30.135  15.124  1.00 43.60 ? 378 HOH E O   1 
HETATM 8644 O  O   . HOH EC 6 .   ? -1.719 42.026  1.084   1.00 54.23 ? 379 HOH E O   1 
HETATM 8645 O  O   . HOH EC 6 .   ? 25.893 38.365  5.521   1.00 44.65 ? 380 HOH E O   1 
HETATM 8646 O  O   . HOH EC 6 .   ? -0.083 23.197  -5.034  1.00 42.56 ? 381 HOH E O   1 
HETATM 8647 O  O   . HOH EC 6 .   ? -4.694 35.470  7.288   1.00 36.18 ? 382 HOH E O   1 
HETATM 8648 O  O   . HOH EC 6 .   ? -4.579 44.756  10.020  1.00 34.36 ? 383 HOH E O   1 
HETATM 8649 O  O   . HOH EC 6 .   ? 13.000 42.978  3.219   1.00 44.28 ? 384 HOH E O   1 
HETATM 8650 O  O   . HOH EC 6 .   ? 24.140 53.292  32.810  1.00 58.81 ? 385 HOH E O   1 
HETATM 8651 O  O   . HOH EC 6 .   ? 24.335 39.446  9.680   1.00 33.88 ? 386 HOH E O   1 
HETATM 8652 O  O   . HOH EC 6 .   ? 24.717 50.660  37.614  1.00 37.70 ? 387 HOH E O   1 
HETATM 8653 O  O   . HOH EC 6 .   ? 10.737 30.184  24.653  1.00 51.98 ? 388 HOH E O   1 
HETATM 8654 O  O   . HOH FC 6 .   ? 48.808 28.033  34.597  1.00 40.56 ? 301 HOH F O   1 
HETATM 8655 O  O   . HOH FC 6 .   ? 44.464 27.944  26.296  1.00 52.01 ? 302 HOH F O   1 
HETATM 8656 O  O   . HOH FC 6 .   ? 47.836 17.258  17.181  1.00 36.18 ? 303 HOH F O   1 
HETATM 8657 O  O   . HOH FC 6 .   ? 6.919  24.127  8.104   1.00 36.29 ? 304 HOH F O   1 
HETATM 8658 O  O   . HOH FC 6 .   ? 30.903 7.133   -3.951  1.00 48.82 ? 305 HOH F O   1 
HETATM 8659 O  O   . HOH FC 6 .   ? 50.692 24.439  28.147  1.00 40.43 ? 306 HOH F O   1 
HETATM 8660 O  O   . HOH FC 6 .   ? 19.039 22.272  13.245  1.00 44.61 ? 307 HOH F O   1 
HETATM 8661 O  O   . HOH FC 6 .   ? 28.182 37.999  4.519   1.00 38.95 ? 308 HOH F O   1 
HETATM 8662 O  O   . HOH FC 6 .   ? 43.440 6.315   18.294  1.00 49.45 ? 309 HOH F O   1 
HETATM 8663 O  O   . HOH FC 6 .   ? 47.615 13.600  22.222  1.00 35.20 ? 310 HOH F O   1 
HETATM 8664 O  O   . HOH FC 6 .   ? 47.846 16.770  14.197  1.00 41.97 ? 311 HOH F O   1 
HETATM 8665 O  O   . HOH FC 6 .   ? 44.450 7.588   9.386   1.00 34.69 ? 312 HOH F O   1 
HETATM 8666 O  O   . HOH FC 6 .   ? 23.252 2.306   9.747   1.00 38.36 ? 313 HOH F O   1 
HETATM 8667 O  O   . HOH FC 6 .   ? 45.857 19.265  27.462  1.00 28.16 ? 314 HOH F O   1 
HETATM 8668 O  O   . HOH FC 6 .   ? 21.114 6.307   -6.504  1.00 47.63 ? 315 HOH F O   1 
HETATM 8669 O  O   . HOH FC 6 .   ? 40.726 26.401  26.620  1.00 37.46 ? 316 HOH F O   1 
HETATM 8670 O  O   . HOH FC 6 .   ? 26.858 14.000  10.906  1.00 57.23 ? 317 HOH F O   1 
HETATM 8671 O  O   . HOH FC 6 .   ? 20.986 2.890   -5.484  1.00 43.25 ? 318 HOH F O   1 
HETATM 8672 O  O   . HOH FC 6 .   ? 29.815 2.149   12.163  1.00 45.96 ? 319 HOH F O   1 
HETATM 8673 O  O   . HOH FC 6 .   ? 34.975 27.326  12.566  1.00 27.01 ? 320 HOH F O   1 
HETATM 8674 O  O   . HOH FC 6 .   ? 25.406 16.897  -1.615  1.00 37.26 ? 321 HOH F O   1 
HETATM 8675 O  O   . HOH FC 6 .   ? 46.243 19.811  24.701  1.00 29.63 ? 322 HOH F O   1 
HETATM 8676 O  O   . HOH FC 6 .   ? 17.091 10.363  -8.811  1.00 47.82 ? 323 HOH F O   1 
HETATM 8677 O  O   . HOH FC 6 .   ? 21.385 12.407  6.990   1.00 49.25 ? 324 HOH F O   1 
HETATM 8678 O  O   . HOH FC 6 .   ? 47.496 16.716  25.888  1.00 36.56 ? 325 HOH F O   1 
HETATM 8679 O  O   . HOH FC 6 .   ? 13.572 25.186  3.080   1.00 36.71 ? 326 HOH F O   1 
HETATM 8680 O  O   . HOH FC 6 .   ? 30.866 32.148  2.648   1.00 33.70 ? 327 HOH F O   1 
HETATM 8681 O  O   . HOH FC 6 .   ? 3.016  26.323  -4.280  1.00 50.07 ? 328 HOH F O   1 
HETATM 8682 O  O   . HOH FC 6 .   ? 41.091 26.706  9.578   1.00 39.30 ? 329 HOH F O   1 
HETATM 8683 O  O   . HOH FC 6 .   ? 49.499 9.707   8.819   1.00 50.24 ? 330 HOH F O   1 
HETATM 8684 O  O   . HOH FC 6 .   ? 42.263 2.312   16.006  1.00 45.84 ? 331 HOH F O   1 
HETATM 8685 O  O   . HOH FC 6 .   ? 38.382 29.059  22.073  1.00 35.62 ? 332 HOH F O   1 
HETATM 8686 O  O   . HOH FC 6 .   ? 54.016 14.236  18.783  1.00 45.36 ? 333 HOH F O   1 
HETATM 8687 O  O   . HOH FC 6 .   ? 34.401 17.008  23.054  1.00 40.51 ? 334 HOH F O   1 
HETATM 8688 O  O   . HOH FC 6 .   ? 43.010 29.199  16.474  1.00 41.62 ? 335 HOH F O   1 
HETATM 8689 O  O   . HOH FC 6 .   ? 19.003 32.775  6.174   1.00 30.98 ? 336 HOH F O   1 
HETATM 8690 O  O   . HOH FC 6 .   ? 12.748 16.830  -9.518  1.00 54.09 ? 337 HOH F O   1 
HETATM 8691 O  O   . HOH FC 6 .   ? 33.957 34.368  8.018   1.00 26.56 ? 338 HOH F O   1 
HETATM 8692 O  O   . HOH FC 6 .   ? 34.526 6.289   8.695   1.00 40.42 ? 339 HOH F O   1 
HETATM 8693 O  O   . HOH FC 6 .   ? 20.546 14.922  -5.896  1.00 41.77 ? 340 HOH F O   1 
HETATM 8694 O  O   . HOH FC 6 .   ? 0.364  25.069  -3.425  1.00 42.38 ? 341 HOH F O   1 
HETATM 8695 O  O   . HOH FC 6 .   ? 43.259 17.605  7.852   1.00 34.25 ? 342 HOH F O   1 
HETATM 8696 O  O   . HOH FC 6 .   ? 15.729 -1.064  -5.145  1.00 34.14 ? 343 HOH F O   1 
HETATM 8697 O  O   . HOH FC 6 .   ? 3.045  12.361  1.471   1.00 33.40 ? 344 HOH F O   1 
HETATM 8698 O  O   . HOH FC 6 .   ? 30.341 27.289  4.991   1.00 29.55 ? 345 HOH F O   1 
HETATM 8699 O  O   . HOH FC 6 .   ? 45.421 21.936  8.865   1.00 44.85 ? 346 HOH F O   1 
HETATM 8700 O  O   . HOH FC 6 .   ? 53.866 19.310  23.815  1.00 35.60 ? 347 HOH F O   1 
HETATM 8701 O  O   . HOH FC 6 .   ? 3.187  10.165  3.184   1.00 44.36 ? 348 HOH F O   1 
HETATM 8702 O  O   . HOH FC 6 .   ? 7.391  15.832  10.292  1.00 46.96 ? 349 HOH F O   1 
HETATM 8703 O  O   . HOH FC 6 .   ? 15.619 26.700  1.821   1.00 43.66 ? 350 HOH F O   1 
HETATM 8704 O  O   . HOH FC 6 .   ? 53.184 11.846  20.857  1.00 39.19 ? 351 HOH F O   1 
HETATM 8705 O  O   . HOH FC 6 .   ? 47.053 7.156   17.102  1.00 42.37 ? 352 HOH F O   1 
HETATM 8706 O  O   . HOH FC 6 .   ? 17.323 25.928  -5.728  1.00 42.56 ? 353 HOH F O   1 
HETATM 8707 O  O   . HOH FC 6 .   ? 11.971 25.765  -1.186  1.00 49.43 ? 354 HOH F O   1 
HETATM 8708 O  O   . HOH FC 6 .   ? 38.791 19.621  8.434   1.00 43.36 ? 355 HOH F O   1 
HETATM 8709 O  O   . HOH FC 6 .   ? 46.061 26.754  13.947  1.00 42.35 ? 356 HOH F O   1 
HETATM 8710 O  O   . HOH FC 6 .   ? 38.769 29.407  11.205  1.00 31.26 ? 357 HOH F O   1 
HETATM 8711 O  O   . HOH FC 6 .   ? 13.376 10.567  -8.369  1.00 46.99 ? 358 HOH F O   1 
HETATM 8712 O  O   . HOH FC 6 .   ? 42.685 7.971   7.712   1.00 38.24 ? 359 HOH F O   1 
HETATM 8713 O  O   . HOH FC 6 .   ? 2.742  19.507  -6.041  1.00 42.72 ? 360 HOH F O   1 
HETATM 8714 O  O   . HOH FC 6 .   ? 19.510 14.024  15.997  1.00 43.47 ? 361 HOH F O   1 
HETATM 8715 O  O   . HOH FC 6 .   ? 52.489 23.092  16.229  1.00 39.90 ? 362 HOH F O   1 
HETATM 8716 O  O   . HOH FC 6 .   ? 1.170  5.554   -7.910  1.00 43.53 ? 363 HOH F O   1 
HETATM 8717 O  O   . HOH FC 6 .   ? 26.898 31.601  0.403   1.00 41.98 ? 364 HOH F O   1 
HETATM 8718 O  O   . HOH FC 6 .   ? 4.124  3.788   -6.993  1.00 40.91 ? 365 HOH F O   1 
HETATM 8719 O  O   . HOH FC 6 .   ? 55.320 14.210  16.276  1.00 52.75 ? 366 HOH F O   1 
HETATM 8720 O  O   . HOH FC 6 .   ? 35.983 35.088  10.571  1.00 44.08 ? 367 HOH F O   1 
HETATM 8721 O  O   . HOH FC 6 .   ? 41.403 28.711  11.908  1.00 39.25 ? 368 HOH F O   1 
HETATM 8722 O  O   . HOH FC 6 .   ? 31.365 -0.839  13.498  1.00 48.00 ? 369 HOH F O   1 
HETATM 8723 O  O   . HOH FC 6 .   ? 34.277 14.658  23.494  1.00 49.98 ? 370 HOH F O   1 
HETATM 8724 O  O   . HOH FC 6 .   ? 13.288 9.409   10.966  1.00 52.47 ? 371 HOH F O   1 
HETATM 8725 O  O   . HOH FC 6 .   ? 6.163  17.992  8.754   1.00 50.35 ? 372 HOH F O   1 
HETATM 8726 O  O   . HOH FC 6 .   ? 27.364 9.463   -3.568  1.00 39.82 ? 373 HOH F O   1 
HETATM 8727 O  O   . HOH FC 6 .   ? 38.214 27.466  9.475   1.00 36.29 ? 374 HOH F O   1 
HETATM 8728 O  O   . HOH FC 6 .   ? 20.949 13.113  -8.095  1.00 49.51 ? 375 HOH F O   1 
HETATM 8729 O  O   . HOH FC 6 .   ? 11.447 25.504  1.631   1.00 35.30 ? 376 HOH F O   1 
HETATM 8730 O  O   . HOH FC 6 .   ? 14.291 0.521   -9.154  1.00 47.39 ? 377 HOH F O   1 
HETATM 8731 O  O   . HOH FC 6 .   ? 51.178 8.324   10.240  1.00 43.03 ? 378 HOH F O   1 
HETATM 8732 O  O   . HOH FC 6 .   ? 14.308 -1.225  -7.658  1.00 44.99 ? 379 HOH F O   1 
HETATM 8733 O  O   . HOH FC 6 .   ? 46.176 31.059  31.214  1.00 40.62 ? 380 HOH F O   1 
HETATM 8734 O  O   . HOH FC 6 .   ? 46.980 14.405  24.734  1.00 31.30 ? 381 HOH F O   1 
HETATM 8735 O  O   . HOH FC 6 .   ? 49.455 8.317   17.491  1.00 38.24 ? 382 HOH F O   1 
HETATM 8736 O  O   . HOH FC 6 .   ? 22.838 11.168  -7.896  1.00 53.50 ? 383 HOH F O   1 
HETATM 8737 O  O   . HOH FC 6 .   ? 15.049 7.150   10.608  1.00 53.28 ? 384 HOH F O   1 
HETATM 8738 O  O   . HOH FC 6 .   ? 43.747 31.560  16.252  1.00 46.41 ? 385 HOH F O   1 
HETATM 8739 O  O   . HOH FC 6 .   ? 18.266 -0.716  -6.585  1.00 41.23 ? 386 HOH F O   1 
# 
