data_8JL7
# 
_entry.id   8JL7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8JL7         pdb_00008jl7 10.2210/pdb8jl7/pdb 
WWPDB D_1300038184 ?            ?                   
# 
_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       2024-12-04 
# 
_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                        8JL7 
_pdbx_database_status.recvd_initial_deposition_date   2023-06-02 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              scshin84@kist.re.kr 
_pdbx_contact_author.name_first         Sangchul 
_pdbx_contact_author.name_last          Shin 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0156-680X 
# 
_audit_author.name               'Shin, S.C.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   0000-0003-0156-680X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of the Green fluorescent protein SEA227D variant at pH 8.0' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Shin, S.C.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0003-0156-680X 
# 
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 'Green fluorescent protein' 27002.430 2   ? F64L,Q80R,S147D,N149Q,V163A,S175G,S202F,Q204T,A206T,A227D ? ? 
2 water   nat water                       18.015    263 ? ?                                                         ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTL(CRO)VQCFSRYPDHM
KRHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNDHQVYIMADKQK
NGIKANFKIRHNIEDGGVQLADHYQQNTPIGDGPVLLPDNHYLFTTSTLSKDPNEKRDHMVLLEFVTADGITHGMDELYK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKR
HDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNDHQVYIMADKQKNG
IKANFKIRHNIEDGGVQLADHYQQNTPIGDGPVLLPDNHYLFTTSTLSKDPNEKRDHMVLLEFVTADGITHGMDELYK
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LYS n 
1 4   GLY n 
1 5   GLU n 
1 6   GLU n 
1 7   LEU n 
1 8   PHE n 
1 9   THR n 
1 10  GLY n 
1 11  VAL n 
1 12  VAL n 
1 13  PRO n 
1 14  ILE n 
1 15  LEU n 
1 16  VAL n 
1 17  GLU n 
1 18  LEU n 
1 19  ASP n 
1 20  GLY n 
1 21  ASP n 
1 22  VAL n 
1 23  ASN n 
1 24  GLY n 
1 25  HIS n 
1 26  LYS n 
1 27  PHE n 
1 28  SER n 
1 29  VAL n 
1 30  SER n 
1 31  GLY n 
1 32  GLU n 
1 33  GLY n 
1 34  GLU n 
1 35  GLY n 
1 36  ASP n 
1 37  ALA n 
1 38  THR n 
1 39  TYR n 
1 40  GLY n 
1 41  LYS n 
1 42  LEU n 
1 43  THR n 
1 44  LEU n 
1 45  LYS n 
1 46  PHE n 
1 47  ILE n 
1 48  CYS n 
1 49  THR n 
1 50  THR n 
1 51  GLY n 
1 52  LYS n 
1 53  LEU n 
1 54  PRO n 
1 55  VAL n 
1 56  PRO n 
1 57  TRP n 
1 58  PRO n 
1 59  THR n 
1 60  LEU n 
1 61  VAL n 
1 62  THR n 
1 63  THR n 
1 64  LEU n 
1 65  CRO n 
1 66  VAL n 
1 67  GLN n 
1 68  CYS n 
1 69  PHE n 
1 70  SER n 
1 71  ARG n 
1 72  TYR n 
1 73  PRO n 
1 74  ASP n 
1 75  HIS n 
1 76  MET n 
1 77  LYS n 
1 78  ARG n 
1 79  HIS n 
1 80  ASP n 
1 81  PHE n 
1 82  PHE n 
1 83  LYS n 
1 84  SER n 
1 85  ALA n 
1 86  MET n 
1 87  PRO n 
1 88  GLU n 
1 89  GLY n 
1 90  TYR n 
1 91  VAL n 
1 92  GLN n 
1 93  GLU n 
1 94  ARG n 
1 95  THR n 
1 96  ILE n 
1 97  PHE n 
1 98  PHE n 
1 99  LYS n 
1 100 ASP n 
1 101 ASP n 
1 102 GLY n 
1 103 ASN n 
1 104 TYR n 
1 105 LYS n 
1 106 THR n 
1 107 ARG n 
1 108 ALA n 
1 109 GLU n 
1 110 VAL n 
1 111 LYS n 
1 112 PHE n 
1 113 GLU n 
1 114 GLY n 
1 115 ASP n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 ASN n 
1 120 ARG n 
1 121 ILE n 
1 122 GLU n 
1 123 LEU n 
1 124 LYS n 
1 125 GLY n 
1 126 ILE n 
1 127 ASP n 
1 128 PHE n 
1 129 LYS n 
1 130 GLU n 
1 131 ASP n 
1 132 GLY n 
1 133 ASN n 
1 134 ILE n 
1 135 LEU n 
1 136 GLY n 
1 137 HIS n 
1 138 LYS n 
1 139 LEU n 
1 140 GLU n 
1 141 TYR n 
1 142 ASN n 
1 143 TYR n 
1 144 ASN n 
1 145 ASP n 
1 146 HIS n 
1 147 GLN n 
1 148 VAL n 
1 149 TYR n 
1 150 ILE n 
1 151 MET n 
1 152 ALA n 
1 153 ASP n 
1 154 LYS n 
1 155 GLN n 
1 156 LYS n 
1 157 ASN n 
1 158 GLY n 
1 159 ILE n 
1 160 LYS n 
1 161 ALA n 
1 162 ASN n 
1 163 PHE n 
1 164 LYS n 
1 165 ILE n 
1 166 ARG n 
1 167 HIS n 
1 168 ASN n 
1 169 ILE n 
1 170 GLU n 
1 171 ASP n 
1 172 GLY n 
1 173 GLY n 
1 174 VAL n 
1 175 GLN n 
1 176 LEU n 
1 177 ALA n 
1 178 ASP n 
1 179 HIS n 
1 180 TYR n 
1 181 GLN n 
1 182 GLN n 
1 183 ASN n 
1 184 THR n 
1 185 PRO n 
1 186 ILE n 
1 187 GLY n 
1 188 ASP n 
1 189 GLY n 
1 190 PRO n 
1 191 VAL n 
1 192 LEU n 
1 193 LEU n 
1 194 PRO n 
1 195 ASP n 
1 196 ASN n 
1 197 HIS n 
1 198 TYR n 
1 199 LEU n 
1 200 PHE n 
1 201 THR n 
1 202 THR n 
1 203 SER n 
1 204 THR n 
1 205 LEU n 
1 206 SER n 
1 207 LYS n 
1 208 ASP n 
1 209 PRO n 
1 210 ASN n 
1 211 GLU n 
1 212 LYS n 
1 213 ARG n 
1 214 ASP n 
1 215 HIS n 
1 216 MET n 
1 217 VAL n 
1 218 LEU n 
1 219 LEU n 
1 220 GLU n 
1 221 PHE n 
1 222 VAL n 
1 223 THR n 
1 224 ALA n 
1 225 ASP n 
1 226 GLY n 
1 227 ILE n 
1 228 THR n 
1 229 HIS n 
1 230 GLY n 
1 231 MET n 
1 232 ASP n 
1 233 GLU n 
1 234 LEU n 
1 235 TYR n 
1 236 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   236 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 GFP 
_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      'Aequorea victoria' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     6100 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CRO 'L-peptide linking' n 
'{2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid' 
'PEPTIDE DERIVED CHROMOPHORE' 'C15 H17 N3 O5'  319.313 
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  
HIS 'L-peptide linking' y HISTIDINE ?                             'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER ?                             'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                             'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE ?                             'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE ?                             'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE ?                             'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE ?                             'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE ?                             'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE ?                             'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE ?                             'C4 H9 N O3'     119.119 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   GLY 4   4   4   GLY GLY A . n 
A 1 5   GLU 5   5   5   GLU GLU A . n 
A 1 6   GLU 6   6   6   GLU GLU A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   THR 9   9   9   THR THR A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  VAL 11  11  11  VAL VAL A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  ILE 14  14  14  ILE ILE A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  VAL 22  22  22  VAL VAL A . n 
A 1 23  ASN 23  23  23  ASN ASN A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  HIS 25  25  25  HIS HIS A . n 
A 1 26  LYS 26  26  26  LYS LYS A . n 
A 1 27  PHE 27  27  27  PHE PHE A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  SER 30  30  30  SER SER A . n 
A 1 31  GLY 31  31  31  GLY GLY A . n 
A 1 32  GLU 32  32  32  GLU GLU A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  GLU 34  34  34  GLU GLU A . n 
A 1 35  GLY 35  35  35  GLY GLY A . n 
A 1 36  ASP 36  36  36  ASP ASP A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  THR 38  38  38  THR THR A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  GLY 40  40  40  GLY GLY A . n 
A 1 41  LYS 41  41  41  LYS LYS A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PHE 46  46  46  PHE PHE A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  CYS 48  48  48  CYS CYS A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  LYS 52  52  52  LYS LYS A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  PRO 56  56  56  PRO PRO A . n 
A 1 57  TRP 57  57  57  TRP TRP A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  VAL 61  61  61  VAL VAL A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  CRO 65  66  66  CRO CRO A . n 
A 1 66  VAL 66  68  68  VAL VAL A . n 
A 1 67  GLN 67  69  69  GLN GLN A . n 
A 1 68  CYS 68  70  70  CYS CYS A . n 
A 1 69  PHE 69  71  71  PHE PHE A . n 
A 1 70  SER 70  72  72  SER SER A . n 
A 1 71  ARG 71  73  73  ARG ARG A . n 
A 1 72  TYR 72  74  74  TYR TYR A . n 
A 1 73  PRO 73  75  75  PRO PRO A . n 
A 1 74  ASP 74  76  76  ASP ASP A . n 
A 1 75  HIS 75  77  77  HIS HIS A . n 
A 1 76  MET 76  78  78  MET MET A . n 
A 1 77  LYS 77  79  79  LYS LYS A . n 
A 1 78  ARG 78  80  80  ARG ARG A . n 
A 1 79  HIS 79  81  81  HIS HIS A . n 
A 1 80  ASP 80  82  82  ASP ASP A . n 
A 1 81  PHE 81  83  83  PHE PHE A . n 
A 1 82  PHE 82  84  84  PHE PHE A . n 
A 1 83  LYS 83  85  85  LYS LYS A . n 
A 1 84  SER 84  86  86  SER SER A . n 
A 1 85  ALA 85  87  87  ALA ALA A . n 
A 1 86  MET 86  88  88  MET MET A . n 
A 1 87  PRO 87  89  89  PRO PRO A . n 
A 1 88  GLU 88  90  90  GLU GLU A . n 
A 1 89  GLY 89  91  91  GLY GLY A . n 
A 1 90  TYR 90  92  92  TYR TYR A . n 
A 1 91  VAL 91  93  93  VAL VAL A . n 
A 1 92  GLN 92  94  94  GLN GLN A . n 
A 1 93  GLU 93  95  95  GLU GLU A . n 
A 1 94  ARG 94  96  96  ARG ARG A . n 
A 1 95  THR 95  97  97  THR THR A . n 
A 1 96  ILE 96  98  98  ILE ILE A . n 
A 1 97  PHE 97  99  99  PHE PHE A . n 
A 1 98  PHE 98  100 100 PHE PHE A . n 
A 1 99  LYS 99  101 101 LYS LYS A . n 
A 1 100 ASP 100 102 102 ASP ASP A . n 
A 1 101 ASP 101 103 103 ASP ASP A . n 
A 1 102 GLY 102 104 104 GLY GLY A . n 
A 1 103 ASN 103 105 105 ASN ASN A . n 
A 1 104 TYR 104 106 106 TYR TYR A . n 
A 1 105 LYS 105 107 107 LYS LYS A . n 
A 1 106 THR 106 108 108 THR THR A . n 
A 1 107 ARG 107 109 109 ARG ARG A . n 
A 1 108 ALA 108 110 110 ALA ALA A . n 
A 1 109 GLU 109 111 111 GLU GLU A . n 
A 1 110 VAL 110 112 112 VAL VAL A . n 
A 1 111 LYS 111 113 113 LYS LYS A . n 
A 1 112 PHE 112 114 114 PHE PHE A . n 
A 1 113 GLU 113 115 115 GLU GLU A . n 
A 1 114 GLY 114 116 116 GLY GLY A . n 
A 1 115 ASP 115 117 117 ASP ASP A . n 
A 1 116 THR 116 118 118 THR THR A . n 
A 1 117 LEU 117 119 119 LEU LEU A . n 
A 1 118 VAL 118 120 120 VAL VAL A . n 
A 1 119 ASN 119 121 121 ASN ASN A . n 
A 1 120 ARG 120 122 122 ARG ARG A . n 
A 1 121 ILE 121 123 123 ILE ILE A . n 
A 1 122 GLU 122 124 124 GLU GLU A . n 
A 1 123 LEU 123 125 125 LEU LEU A . n 
A 1 124 LYS 124 126 126 LYS LYS A . n 
A 1 125 GLY 125 127 127 GLY GLY A . n 
A 1 126 ILE 126 128 128 ILE ILE A . n 
A 1 127 ASP 127 129 129 ASP ASP A . n 
A 1 128 PHE 128 130 130 PHE PHE A . n 
A 1 129 LYS 129 131 131 LYS LYS A . n 
A 1 130 GLU 130 132 132 GLU GLU A . n 
A 1 131 ASP 131 133 133 ASP ASP A . n 
A 1 132 GLY 132 134 134 GLY GLY A . n 
A 1 133 ASN 133 135 135 ASN ASN A . n 
A 1 134 ILE 134 136 136 ILE ILE A . n 
A 1 135 LEU 135 137 137 LEU LEU A . n 
A 1 136 GLY 136 138 138 GLY GLY A . n 
A 1 137 HIS 137 139 139 HIS HIS A . n 
A 1 138 LYS 138 140 140 LYS LYS A . n 
A 1 139 LEU 139 141 141 LEU LEU A . n 
A 1 140 GLU 140 142 142 GLU GLU A . n 
A 1 141 TYR 141 143 143 TYR TYR A . n 
A 1 142 ASN 142 144 144 ASN ASN A . n 
A 1 143 TYR 143 145 145 TYR TYR A . n 
A 1 144 ASN 144 146 146 ASN ASN A . n 
A 1 145 ASP 145 147 147 ASP ASP A . n 
A 1 146 HIS 146 148 148 HIS HIS A . n 
A 1 147 GLN 147 149 149 GLN GLN A . n 
A 1 148 VAL 148 150 150 VAL VAL A . n 
A 1 149 TYR 149 151 151 TYR TYR A . n 
A 1 150 ILE 150 152 152 ILE ILE A . n 
A 1 151 MET 151 153 153 MET MET A . n 
A 1 152 ALA 152 154 154 ALA ALA A . n 
A 1 153 ASP 153 155 155 ASP ASP A . n 
A 1 154 LYS 154 156 156 LYS LYS A . n 
A 1 155 GLN 155 157 157 GLN GLN A . n 
A 1 156 LYS 156 158 158 LYS LYS A . n 
A 1 157 ASN 157 159 159 ASN ASN A . n 
A 1 158 GLY 158 160 160 GLY GLY A . n 
A 1 159 ILE 159 161 161 ILE ILE A . n 
A 1 160 LYS 160 162 162 LYS LYS A . n 
A 1 161 ALA 161 163 163 ALA ALA A . n 
A 1 162 ASN 162 164 164 ASN ASN A . n 
A 1 163 PHE 163 165 165 PHE PHE A . n 
A 1 164 LYS 164 166 166 LYS LYS A . n 
A 1 165 ILE 165 167 167 ILE ILE A . n 
A 1 166 ARG 166 168 168 ARG ARG A . n 
A 1 167 HIS 167 169 169 HIS HIS A . n 
A 1 168 ASN 168 170 170 ASN ASN A . n 
A 1 169 ILE 169 171 171 ILE ILE A . n 
A 1 170 GLU 170 172 172 GLU GLU A . n 
A 1 171 ASP 171 173 173 ASP ASP A . n 
A 1 172 GLY 172 174 174 GLY GLY A . n 
A 1 173 GLY 173 175 175 GLY GLY A . n 
A 1 174 VAL 174 176 176 VAL VAL A . n 
A 1 175 GLN 175 177 177 GLN GLN A . n 
A 1 176 LEU 176 178 178 LEU LEU A . n 
A 1 177 ALA 177 179 179 ALA ALA A . n 
A 1 178 ASP 178 180 180 ASP ASP A . n 
A 1 179 HIS 179 181 181 HIS HIS A . n 
A 1 180 TYR 180 182 182 TYR TYR A . n 
A 1 181 GLN 181 183 183 GLN GLN A . n 
A 1 182 GLN 182 184 184 GLN GLN A . n 
A 1 183 ASN 183 185 185 ASN ASN A . n 
A 1 184 THR 184 186 186 THR THR A . n 
A 1 185 PRO 185 187 187 PRO PRO A . n 
A 1 186 ILE 186 188 188 ILE ILE A . n 
A 1 187 GLY 187 189 189 GLY GLY A . n 
A 1 188 ASP 188 190 190 ASP ASP A . n 
A 1 189 GLY 189 191 191 GLY GLY A . n 
A 1 190 PRO 190 192 192 PRO PRO A . n 
A 1 191 VAL 191 193 193 VAL VAL A . n 
A 1 192 LEU 192 194 194 LEU LEU A . n 
A 1 193 LEU 193 195 195 LEU LEU A . n 
A 1 194 PRO 194 196 196 PRO PRO A . n 
A 1 195 ASP 195 197 197 ASP ASP A . n 
A 1 196 ASN 196 198 198 ASN ASN A . n 
A 1 197 HIS 197 199 199 HIS HIS A . n 
A 1 198 TYR 198 200 200 TYR TYR A . n 
A 1 199 LEU 199 201 201 LEU LEU A . n 
A 1 200 PHE 200 202 202 PHE PHE A . n 
A 1 201 THR 201 203 203 THR THR A . n 
A 1 202 THR 202 204 204 THR THR A . n 
A 1 203 SER 203 205 205 SER SER A . n 
A 1 204 THR 204 206 206 THR THR A . n 
A 1 205 LEU 205 207 207 LEU LEU A . n 
A 1 206 SER 206 208 208 SER SER A . n 
A 1 207 LYS 207 209 209 LYS LYS A . n 
A 1 208 ASP 208 210 210 ASP ASP A . n 
A 1 209 PRO 209 211 211 PRO PRO A . n 
A 1 210 ASN 210 212 212 ASN ASN A . n 
A 1 211 GLU 211 213 213 GLU GLU A . n 
A 1 212 LYS 212 214 214 LYS LYS A . n 
A 1 213 ARG 213 215 215 ARG ARG A . n 
A 1 214 ASP 214 216 216 ASP ASP A . n 
A 1 215 HIS 215 217 217 HIS HIS A . n 
A 1 216 MET 216 218 218 MET MET A . n 
A 1 217 VAL 217 219 219 VAL VAL A . n 
A 1 218 LEU 218 220 220 LEU LEU A . n 
A 1 219 LEU 219 221 221 LEU LEU A . n 
A 1 220 GLU 220 222 222 GLU GLU A . n 
A 1 221 PHE 221 223 223 PHE PHE A . n 
A 1 222 VAL 222 224 224 VAL VAL A . n 
A 1 223 THR 223 225 225 THR THR A . n 
A 1 224 ALA 224 226 226 ALA ALA A . n 
A 1 225 ASP 225 227 227 ASP ASP A . n 
A 1 226 GLY 226 228 ?   ?   ?   A . n 
A 1 227 ILE 227 229 ?   ?   ?   A . n 
A 1 228 THR 228 230 ?   ?   ?   A . n 
A 1 229 HIS 229 231 ?   ?   ?   A . n 
A 1 230 GLY 230 232 ?   ?   ?   A . n 
A 1 231 MET 231 233 ?   ?   ?   A . n 
A 1 232 ASP 232 234 ?   ?   ?   A . n 
A 1 233 GLU 233 235 ?   ?   ?   A . n 
A 1 234 LEU 234 236 ?   ?   ?   A . n 
A 1 235 TYR 235 237 ?   ?   ?   A . n 
A 1 236 LYS 236 238 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   GLY 4   4   4   GLY GLY B . n 
B 1 5   GLU 5   5   5   GLU GLU B . n 
B 1 6   GLU 6   6   6   GLU GLU B . n 
B 1 7   LEU 7   7   7   LEU LEU B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   THR 9   9   9   THR THR B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  VAL 11  11  11  VAL VAL B . n 
B 1 12  VAL 12  12  12  VAL VAL B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  ILE 14  14  14  ILE ILE B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  GLU 17  17  17  GLU GLU B . n 
B 1 18  LEU 18  18  18  LEU LEU B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  GLY 20  20  20  GLY GLY B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  VAL 22  22  22  VAL VAL B . n 
B 1 23  ASN 23  23  23  ASN ASN B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  HIS 25  25  25  HIS HIS B . n 
B 1 26  LYS 26  26  26  LYS LYS B . n 
B 1 27  PHE 27  27  27  PHE PHE B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  SER 30  30  30  SER SER B . n 
B 1 31  GLY 31  31  31  GLY GLY B . n 
B 1 32  GLU 32  32  32  GLU GLU B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  GLU 34  34  34  GLU GLU B . n 
B 1 35  GLY 35  35  35  GLY GLY B . n 
B 1 36  ASP 36  36  36  ASP ASP B . n 
B 1 37  ALA 37  37  37  ALA ALA B . n 
B 1 38  THR 38  38  38  THR THR B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  GLY 40  40  40  GLY GLY B . n 
B 1 41  LYS 41  41  41  LYS LYS B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  THR 43  43  43  THR THR B . n 
B 1 44  LEU 44  44  44  LEU LEU B . n 
B 1 45  LYS 45  45  45  LYS LYS B . n 
B 1 46  PHE 46  46  46  PHE PHE B . n 
B 1 47  ILE 47  47  47  ILE ILE B . n 
B 1 48  CYS 48  48  48  CYS CYS B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  LYS 52  52  52  LYS LYS B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  PRO 54  54  54  PRO PRO B . n 
B 1 55  VAL 55  55  55  VAL VAL B . n 
B 1 56  PRO 56  56  56  PRO PRO B . n 
B 1 57  TRP 57  57  57  TRP TRP B . n 
B 1 58  PRO 58  58  58  PRO PRO B . n 
B 1 59  THR 59  59  59  THR THR B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  VAL 61  61  61  VAL VAL B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  THR 63  63  63  THR THR B . n 
B 1 64  LEU 64  64  64  LEU LEU B . n 
B 1 65  CRO 65  66  66  CRO CRO B . n 
B 1 66  VAL 66  68  68  VAL VAL B . n 
B 1 67  GLN 67  69  69  GLN GLN B . n 
B 1 68  CYS 68  70  70  CYS CYS B . n 
B 1 69  PHE 69  71  71  PHE PHE B . n 
B 1 70  SER 70  72  72  SER SER B . n 
B 1 71  ARG 71  73  73  ARG ARG B . n 
B 1 72  TYR 72  74  74  TYR TYR B . n 
B 1 73  PRO 73  75  75  PRO PRO B . n 
B 1 74  ASP 74  76  76  ASP ASP B . n 
B 1 75  HIS 75  77  77  HIS HIS B . n 
B 1 76  MET 76  78  78  MET MET B . n 
B 1 77  LYS 77  79  79  LYS LYS B . n 
B 1 78  ARG 78  80  80  ARG ARG B . n 
B 1 79  HIS 79  81  81  HIS HIS B . n 
B 1 80  ASP 80  82  82  ASP ASP B . n 
B 1 81  PHE 81  83  83  PHE PHE B . n 
B 1 82  PHE 82  84  84  PHE PHE B . n 
B 1 83  LYS 83  85  85  LYS LYS B . n 
B 1 84  SER 84  86  86  SER SER B . n 
B 1 85  ALA 85  87  87  ALA ALA B . n 
B 1 86  MET 86  88  88  MET MET B . n 
B 1 87  PRO 87  89  89  PRO PRO B . n 
B 1 88  GLU 88  90  90  GLU GLU B . n 
B 1 89  GLY 89  91  91  GLY GLY B . n 
B 1 90  TYR 90  92  92  TYR TYR B . n 
B 1 91  VAL 91  93  93  VAL VAL B . n 
B 1 92  GLN 92  94  94  GLN GLN B . n 
B 1 93  GLU 93  95  95  GLU GLU B . n 
B 1 94  ARG 94  96  96  ARG ARG B . n 
B 1 95  THR 95  97  97  THR THR B . n 
B 1 96  ILE 96  98  98  ILE ILE B . n 
B 1 97  PHE 97  99  99  PHE PHE B . n 
B 1 98  PHE 98  100 100 PHE PHE B . n 
B 1 99  LYS 99  101 101 LYS LYS B . n 
B 1 100 ASP 100 102 102 ASP ASP B . n 
B 1 101 ASP 101 103 103 ASP ASP B . n 
B 1 102 GLY 102 104 104 GLY GLY B . n 
B 1 103 ASN 103 105 105 ASN ASN B . n 
B 1 104 TYR 104 106 106 TYR TYR B . n 
B 1 105 LYS 105 107 107 LYS LYS B . n 
B 1 106 THR 106 108 108 THR THR B . n 
B 1 107 ARG 107 109 109 ARG ARG B . n 
B 1 108 ALA 108 110 110 ALA ALA B . n 
B 1 109 GLU 109 111 111 GLU GLU B . n 
B 1 110 VAL 110 112 112 VAL VAL B . n 
B 1 111 LYS 111 113 113 LYS LYS B . n 
B 1 112 PHE 112 114 114 PHE PHE B . n 
B 1 113 GLU 113 115 115 GLU GLU B . n 
B 1 114 GLY 114 116 116 GLY GLY B . n 
B 1 115 ASP 115 117 117 ASP ASP B . n 
B 1 116 THR 116 118 118 THR THR B . n 
B 1 117 LEU 117 119 119 LEU LEU B . n 
B 1 118 VAL 118 120 120 VAL VAL B . n 
B 1 119 ASN 119 121 121 ASN ASN B . n 
B 1 120 ARG 120 122 122 ARG ARG B . n 
B 1 121 ILE 121 123 123 ILE ILE B . n 
B 1 122 GLU 122 124 124 GLU GLU B . n 
B 1 123 LEU 123 125 125 LEU LEU B . n 
B 1 124 LYS 124 126 126 LYS LYS B . n 
B 1 125 GLY 125 127 127 GLY GLY B . n 
B 1 126 ILE 126 128 128 ILE ILE B . n 
B 1 127 ASP 127 129 129 ASP ASP B . n 
B 1 128 PHE 128 130 130 PHE PHE B . n 
B 1 129 LYS 129 131 131 LYS LYS B . n 
B 1 130 GLU 130 132 132 GLU GLU B . n 
B 1 131 ASP 131 133 133 ASP ASP B . n 
B 1 132 GLY 132 134 134 GLY GLY B . n 
B 1 133 ASN 133 135 135 ASN ASN B . n 
B 1 134 ILE 134 136 136 ILE ILE B . n 
B 1 135 LEU 135 137 137 LEU LEU B . n 
B 1 136 GLY 136 138 138 GLY GLY B . n 
B 1 137 HIS 137 139 139 HIS HIS B . n 
B 1 138 LYS 138 140 140 LYS LYS B . n 
B 1 139 LEU 139 141 141 LEU LEU B . n 
B 1 140 GLU 140 142 142 GLU GLU B . n 
B 1 141 TYR 141 143 143 TYR TYR B . n 
B 1 142 ASN 142 144 144 ASN ASN B . n 
B 1 143 TYR 143 145 145 TYR TYR B . n 
B 1 144 ASN 144 146 146 ASN ASN B . n 
B 1 145 ASP 145 147 147 ASP ASP B . n 
B 1 146 HIS 146 148 148 HIS HIS B . n 
B 1 147 GLN 147 149 149 GLN GLN B . n 
B 1 148 VAL 148 150 150 VAL VAL B . n 
B 1 149 TYR 149 151 151 TYR TYR B . n 
B 1 150 ILE 150 152 152 ILE ILE B . n 
B 1 151 MET 151 153 153 MET MET B . n 
B 1 152 ALA 152 154 154 ALA ALA B . n 
B 1 153 ASP 153 155 155 ASP ASP B . n 
B 1 154 LYS 154 156 156 LYS LYS B . n 
B 1 155 GLN 155 157 157 GLN GLN B . n 
B 1 156 LYS 156 158 158 LYS LYS B . n 
B 1 157 ASN 157 159 159 ASN ASN B . n 
B 1 158 GLY 158 160 160 GLY GLY B . n 
B 1 159 ILE 159 161 161 ILE ILE B . n 
B 1 160 LYS 160 162 162 LYS LYS B . n 
B 1 161 ALA 161 163 163 ALA ALA B . n 
B 1 162 ASN 162 164 164 ASN ASN B . n 
B 1 163 PHE 163 165 165 PHE PHE B . n 
B 1 164 LYS 164 166 166 LYS LYS B . n 
B 1 165 ILE 165 167 167 ILE ILE B . n 
B 1 166 ARG 166 168 168 ARG ARG B . n 
B 1 167 HIS 167 169 169 HIS HIS B . n 
B 1 168 ASN 168 170 170 ASN ASN B . n 
B 1 169 ILE 169 171 171 ILE ILE B . n 
B 1 170 GLU 170 172 172 GLU GLU B . n 
B 1 171 ASP 171 173 173 ASP ASP B . n 
B 1 172 GLY 172 174 174 GLY GLY B . n 
B 1 173 GLY 173 175 175 GLY GLY B . n 
B 1 174 VAL 174 176 176 VAL VAL B . n 
B 1 175 GLN 175 177 177 GLN GLN B . n 
B 1 176 LEU 176 178 178 LEU LEU B . n 
B 1 177 ALA 177 179 179 ALA ALA B . n 
B 1 178 ASP 178 180 180 ASP ASP B . n 
B 1 179 HIS 179 181 181 HIS HIS B . n 
B 1 180 TYR 180 182 182 TYR TYR B . n 
B 1 181 GLN 181 183 183 GLN GLN B . n 
B 1 182 GLN 182 184 184 GLN GLN B . n 
B 1 183 ASN 183 185 185 ASN ASN B . n 
B 1 184 THR 184 186 186 THR THR B . n 
B 1 185 PRO 185 187 187 PRO PRO B . n 
B 1 186 ILE 186 188 188 ILE ILE B . n 
B 1 187 GLY 187 189 189 GLY GLY B . n 
B 1 188 ASP 188 190 190 ASP ASP B . n 
B 1 189 GLY 189 191 191 GLY GLY B . n 
B 1 190 PRO 190 192 192 PRO PRO B . n 
B 1 191 VAL 191 193 193 VAL VAL B . n 
B 1 192 LEU 192 194 194 LEU LEU B . n 
B 1 193 LEU 193 195 195 LEU LEU B . n 
B 1 194 PRO 194 196 196 PRO PRO B . n 
B 1 195 ASP 195 197 197 ASP ASP B . n 
B 1 196 ASN 196 198 198 ASN ASN B . n 
B 1 197 HIS 197 199 199 HIS HIS B . n 
B 1 198 TYR 198 200 200 TYR TYR B . n 
B 1 199 LEU 199 201 201 LEU LEU B . n 
B 1 200 PHE 200 202 202 PHE PHE B . n 
B 1 201 THR 201 203 203 THR THR B . n 
B 1 202 THR 202 204 204 THR THR B . n 
B 1 203 SER 203 205 205 SER SER B . n 
B 1 204 THR 204 206 206 THR THR B . n 
B 1 205 LEU 205 207 207 LEU LEU B . n 
B 1 206 SER 206 208 208 SER SER B . n 
B 1 207 LYS 207 209 209 LYS LYS B . n 
B 1 208 ASP 208 210 210 ASP ASP B . n 
B 1 209 PRO 209 211 211 PRO PRO B . n 
B 1 210 ASN 210 212 212 ASN ASN B . n 
B 1 211 GLU 211 213 213 GLU GLU B . n 
B 1 212 LYS 212 214 214 LYS LYS B . n 
B 1 213 ARG 213 215 215 ARG ARG B . n 
B 1 214 ASP 214 216 216 ASP ASP B . n 
B 1 215 HIS 215 217 217 HIS HIS B . n 
B 1 216 MET 216 218 218 MET MET B . n 
B 1 217 VAL 217 219 219 VAL VAL B . n 
B 1 218 LEU 218 220 220 LEU LEU B . n 
B 1 219 LEU 219 221 221 LEU LEU B . n 
B 1 220 GLU 220 222 222 GLU GLU B . n 
B 1 221 PHE 221 223 223 PHE PHE B . n 
B 1 222 VAL 222 224 224 VAL VAL B . n 
B 1 223 THR 223 225 225 THR THR B . n 
B 1 224 ALA 224 226 226 ALA ALA B . n 
B 1 225 ASP 225 227 227 ASP ASP B . n 
B 1 226 GLY 226 228 ?   ?   ?   B . n 
B 1 227 ILE 227 229 ?   ?   ?   B . n 
B 1 228 THR 228 230 ?   ?   ?   B . n 
B 1 229 HIS 229 231 ?   ?   ?   B . n 
B 1 230 GLY 230 232 ?   ?   ?   B . n 
B 1 231 MET 231 233 ?   ?   ?   B . n 
B 1 232 ASP 232 234 ?   ?   ?   B . n 
B 1 233 GLU 233 235 ?   ?   ?   B . n 
B 1 234 LEU 234 236 ?   ?   ?   B . n 
B 1 235 TYR 235 237 ?   ?   ?   B . n 
B 1 236 LYS 236 238 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        CRO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   CRO 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HOH 1   301 47  HOH HOH A . 
C 2 HOH 2   302 145 HOH HOH A . 
C 2 HOH 3   303 180 HOH HOH A . 
C 2 HOH 4   304 106 HOH HOH A . 
C 2 HOH 5   305 229 HOH HOH A . 
C 2 HOH 6   306 82  HOH HOH A . 
C 2 HOH 7   307 62  HOH HOH A . 
C 2 HOH 8   308 159 HOH HOH A . 
C 2 HOH 9   309 93  HOH HOH A . 
C 2 HOH 10  310 108 HOH HOH A . 
C 2 HOH 11  311 12  HOH HOH A . 
C 2 HOH 12  312 250 HOH HOH A . 
C 2 HOH 13  313 5   HOH HOH A . 
C 2 HOH 14  314 135 HOH HOH A . 
C 2 HOH 15  315 243 HOH HOH A . 
C 2 HOH 16  316 116 HOH HOH A . 
C 2 HOH 17  317 120 HOH HOH A . 
C 2 HOH 18  318 164 HOH HOH A . 
C 2 HOH 19  319 197 HOH HOH A . 
C 2 HOH 20  320 134 HOH HOH A . 
C 2 HOH 21  321 110 HOH HOH A . 
C 2 HOH 22  322 10  HOH HOH A . 
C 2 HOH 23  323 25  HOH HOH A . 
C 2 HOH 24  324 127 HOH HOH A . 
C 2 HOH 25  325 75  HOH HOH A . 
C 2 HOH 26  326 27  HOH HOH A . 
C 2 HOH 27  327 65  HOH HOH A . 
C 2 HOH 28  328 97  HOH HOH A . 
C 2 HOH 29  329 233 HOH HOH A . 
C 2 HOH 30  330 73  HOH HOH A . 
C 2 HOH 31  331 78  HOH HOH A . 
C 2 HOH 32  332 219 HOH HOH A . 
C 2 HOH 33  333 49  HOH HOH A . 
C 2 HOH 34  334 7   HOH HOH A . 
C 2 HOH 35  335 33  HOH HOH A . 
C 2 HOH 36  336 29  HOH HOH A . 
C 2 HOH 37  337 181 HOH HOH A . 
C 2 HOH 38  338 215 HOH HOH A . 
C 2 HOH 39  339 187 HOH HOH A . 
C 2 HOH 40  340 23  HOH HOH A . 
C 2 HOH 41  341 13  HOH HOH A . 
C 2 HOH 42  342 90  HOH HOH A . 
C 2 HOH 43  343 146 HOH HOH A . 
C 2 HOH 44  344 16  HOH HOH A . 
C 2 HOH 45  345 52  HOH HOH A . 
C 2 HOH 46  346 155 HOH HOH A . 
C 2 HOH 47  347 64  HOH HOH A . 
C 2 HOH 48  348 68  HOH HOH A . 
C 2 HOH 49  349 67  HOH HOH A . 
C 2 HOH 50  350 30  HOH HOH A . 
C 2 HOH 51  351 42  HOH HOH A . 
C 2 HOH 52  352 254 HOH HOH A . 
C 2 HOH 53  353 37  HOH HOH A . 
C 2 HOH 54  354 212 HOH HOH A . 
C 2 HOH 55  355 128 HOH HOH A . 
C 2 HOH 56  356 210 HOH HOH A . 
C 2 HOH 57  357 32  HOH HOH A . 
C 2 HOH 58  358 149 HOH HOH A . 
C 2 HOH 59  359 251 HOH HOH A . 
C 2 HOH 60  360 11  HOH HOH A . 
C 2 HOH 61  361 72  HOH HOH A . 
C 2 HOH 62  362 227 HOH HOH A . 
C 2 HOH 63  363 174 HOH HOH A . 
C 2 HOH 64  364 81  HOH HOH A . 
C 2 HOH 65  365 163 HOH HOH A . 
C 2 HOH 66  366 156 HOH HOH A . 
C 2 HOH 67  367 57  HOH HOH A . 
C 2 HOH 68  368 85  HOH HOH A . 
C 2 HOH 69  369 179 HOH HOH A . 
C 2 HOH 70  370 235 HOH HOH A . 
C 2 HOH 71  371 225 HOH HOH A . 
C 2 HOH 72  372 22  HOH HOH A . 
C 2 HOH 73  373 39  HOH HOH A . 
C 2 HOH 74  374 154 HOH HOH A . 
C 2 HOH 75  375 263 HOH HOH A . 
C 2 HOH 76  376 176 HOH HOH A . 
C 2 HOH 77  377 43  HOH HOH A . 
C 2 HOH 78  378 140 HOH HOH A . 
C 2 HOH 79  379 161 HOH HOH A . 
C 2 HOH 80  380 191 HOH HOH A . 
C 2 HOH 81  381 160 HOH HOH A . 
C 2 HOH 82  382 165 HOH HOH A . 
C 2 HOH 83  383 123 HOH HOH A . 
C 2 HOH 84  384 148 HOH HOH A . 
C 2 HOH 85  385 213 HOH HOH A . 
C 2 HOH 86  386 226 HOH HOH A . 
C 2 HOH 87  387 92  HOH HOH A . 
C 2 HOH 88  388 104 HOH HOH A . 
C 2 HOH 89  389 2   HOH HOH A . 
C 2 HOH 90  390 122 HOH HOH A . 
C 2 HOH 91  391 167 HOH HOH A . 
C 2 HOH 92  392 205 HOH HOH A . 
C 2 HOH 93  393 261 HOH HOH A . 
C 2 HOH 94  394 79  HOH HOH A . 
C 2 HOH 95  395 216 HOH HOH A . 
C 2 HOH 96  396 55  HOH HOH A . 
C 2 HOH 97  397 239 HOH HOH A . 
C 2 HOH 98  398 194 HOH HOH A . 
C 2 HOH 99  399 252 HOH HOH A . 
C 2 HOH 100 400 222 HOH HOH A . 
C 2 HOH 101 401 175 HOH HOH A . 
C 2 HOH 102 402 193 HOH HOH A . 
C 2 HOH 103 403 248 HOH HOH A . 
C 2 HOH 104 404 166 HOH HOH A . 
C 2 HOH 105 405 236 HOH HOH A . 
C 2 HOH 106 406 206 HOH HOH A . 
C 2 HOH 107 407 168 HOH HOH A . 
C 2 HOH 108 408 113 HOH HOH A . 
C 2 HOH 109 409 244 HOH HOH A . 
C 2 HOH 110 410 125 HOH HOH A . 
C 2 HOH 111 411 262 HOH HOH A . 
C 2 HOH 112 412 253 HOH HOH A . 
C 2 HOH 113 413 208 HOH HOH A . 
C 2 HOH 114 414 150 HOH HOH A . 
C 2 HOH 115 415 199 HOH HOH A . 
C 2 HOH 116 416 133 HOH HOH A . 
C 2 HOH 117 417 169 HOH HOH A . 
C 2 HOH 118 418 223 HOH HOH A . 
C 2 HOH 119 419 257 HOH HOH A . 
C 2 HOH 120 420 96  HOH HOH A . 
D 2 HOH 1   301 40  HOH HOH B . 
D 2 HOH 2   302 63  HOH HOH B . 
D 2 HOH 3   303 260 HOH HOH B . 
D 2 HOH 4   304 173 HOH HOH B . 
D 2 HOH 5   305 170 HOH HOH B . 
D 2 HOH 6   306 198 HOH HOH B . 
D 2 HOH 7   307 132 HOH HOH B . 
D 2 HOH 8   308 177 HOH HOH B . 
D 2 HOH 9   309 111 HOH HOH B . 
D 2 HOH 10  310 126 HOH HOH B . 
D 2 HOH 11  311 237 HOH HOH B . 
D 2 HOH 12  312 54  HOH HOH B . 
D 2 HOH 13  313 178 HOH HOH B . 
D 2 HOH 14  314 91  HOH HOH B . 
D 2 HOH 15  315 20  HOH HOH B . 
D 2 HOH 16  316 86  HOH HOH B . 
D 2 HOH 17  317 224 HOH HOH B . 
D 2 HOH 18  318 185 HOH HOH B . 
D 2 HOH 19  319 31  HOH HOH B . 
D 2 HOH 20  320 66  HOH HOH B . 
D 2 HOH 21  321 45  HOH HOH B . 
D 2 HOH 22  322 153 HOH HOH B . 
D 2 HOH 23  323 46  HOH HOH B . 
D 2 HOH 24  324 56  HOH HOH B . 
D 2 HOH 25  325 115 HOH HOH B . 
D 2 HOH 26  326 15  HOH HOH B . 
D 2 HOH 27  327 6   HOH HOH B . 
D 2 HOH 28  328 119 HOH HOH B . 
D 2 HOH 29  329 18  HOH HOH B . 
D 2 HOH 30  330 41  HOH HOH B . 
D 2 HOH 31  331 35  HOH HOH B . 
D 2 HOH 32  332 58  HOH HOH B . 
D 2 HOH 33  333 95  HOH HOH B . 
D 2 HOH 34  334 137 HOH HOH B . 
D 2 HOH 35  335 61  HOH HOH B . 
D 2 HOH 36  336 4   HOH HOH B . 
D 2 HOH 37  337 214 HOH HOH B . 
D 2 HOH 38  338 3   HOH HOH B . 
D 2 HOH 39  339 230 HOH HOH B . 
D 2 HOH 40  340 255 HOH HOH B . 
D 2 HOH 41  341 77  HOH HOH B . 
D 2 HOH 42  342 48  HOH HOH B . 
D 2 HOH 43  343 221 HOH HOH B . 
D 2 HOH 44  344 136 HOH HOH B . 
D 2 HOH 45  345 94  HOH HOH B . 
D 2 HOH 46  346 107 HOH HOH B . 
D 2 HOH 47  347 17  HOH HOH B . 
D 2 HOH 48  348 50  HOH HOH B . 
D 2 HOH 49  349 19  HOH HOH B . 
D 2 HOH 50  350 44  HOH HOH B . 
D 2 HOH 51  351 8   HOH HOH B . 
D 2 HOH 52  352 99  HOH HOH B . 
D 2 HOH 53  353 190 HOH HOH B . 
D 2 HOH 54  354 36  HOH HOH B . 
D 2 HOH 55  355 100 HOH HOH B . 
D 2 HOH 56  356 256 HOH HOH B . 
D 2 HOH 57  357 217 HOH HOH B . 
D 2 HOH 58  358 51  HOH HOH B . 
D 2 HOH 59  359 9   HOH HOH B . 
D 2 HOH 60  360 121 HOH HOH B . 
D 2 HOH 61  361 195 HOH HOH B . 
D 2 HOH 62  362 112 HOH HOH B . 
D 2 HOH 63  363 182 HOH HOH B . 
D 2 HOH 64  364 103 HOH HOH B . 
D 2 HOH 65  365 53  HOH HOH B . 
D 2 HOH 66  366 28  HOH HOH B . 
D 2 HOH 67  367 38  HOH HOH B . 
D 2 HOH 68  368 14  HOH HOH B . 
D 2 HOH 69  369 157 HOH HOH B . 
D 2 HOH 70  370 89  HOH HOH B . 
D 2 HOH 71  371 34  HOH HOH B . 
D 2 HOH 72  372 220 HOH HOH B . 
D 2 HOH 73  373 60  HOH HOH B . 
D 2 HOH 74  374 207 HOH HOH B . 
D 2 HOH 75  375 201 HOH HOH B . 
D 2 HOH 76  376 21  HOH HOH B . 
D 2 HOH 77  377 129 HOH HOH B . 
D 2 HOH 78  378 196 HOH HOH B . 
D 2 HOH 79  379 241 HOH HOH B . 
D 2 HOH 80  380 118 HOH HOH B . 
D 2 HOH 81  381 258 HOH HOH B . 
D 2 HOH 82  382 101 HOH HOH B . 
D 2 HOH 83  383 26  HOH HOH B . 
D 2 HOH 84  384 24  HOH HOH B . 
D 2 HOH 85  385 80  HOH HOH B . 
D 2 HOH 86  386 76  HOH HOH B . 
D 2 HOH 87  387 59  HOH HOH B . 
D 2 HOH 88  388 69  HOH HOH B . 
D 2 HOH 89  389 234 HOH HOH B . 
D 2 HOH 90  390 74  HOH HOH B . 
D 2 HOH 91  391 105 HOH HOH B . 
D 2 HOH 92  392 84  HOH HOH B . 
D 2 HOH 93  393 98  HOH HOH B . 
D 2 HOH 94  394 162 HOH HOH B . 
D 2 HOH 95  395 246 HOH HOH B . 
D 2 HOH 96  396 144 HOH HOH B . 
D 2 HOH 97  397 83  HOH HOH B . 
D 2 HOH 98  398 114 HOH HOH B . 
D 2 HOH 99  399 188 HOH HOH B . 
D 2 HOH 100 400 87  HOH HOH B . 
D 2 HOH 101 401 211 HOH HOH B . 
D 2 HOH 102 402 141 HOH HOH B . 
D 2 HOH 103 403 147 HOH HOH B . 
D 2 HOH 104 404 70  HOH HOH B . 
D 2 HOH 105 405 152 HOH HOH B . 
D 2 HOH 106 406 109 HOH HOH B . 
D 2 HOH 107 407 142 HOH HOH B . 
D 2 HOH 108 408 238 HOH HOH B . 
D 2 HOH 109 409 143 HOH HOH B . 
D 2 HOH 110 410 184 HOH HOH B . 
D 2 HOH 111 411 192 HOH HOH B . 
D 2 HOH 112 412 131 HOH HOH B . 
D 2 HOH 113 413 183 HOH HOH B . 
D 2 HOH 114 414 124 HOH HOH B . 
D 2 HOH 115 415 1   HOH HOH B . 
D 2 HOH 116 416 203 HOH HOH B . 
D 2 HOH 117 417 139 HOH HOH B . 
D 2 HOH 118 418 186 HOH HOH B . 
D 2 HOH 119 419 209 HOH HOH B . 
D 2 HOH 120 420 247 HOH HOH B . 
D 2 HOH 121 421 138 HOH HOH B . 
D 2 HOH 122 422 228 HOH HOH B . 
D 2 HOH 123 423 117 HOH HOH B . 
D 2 HOH 124 424 158 HOH HOH B . 
D 2 HOH 125 425 204 HOH HOH B . 
D 2 HOH 126 426 242 HOH HOH B . 
D 2 HOH 127 427 218 HOH HOH B . 
D 2 HOH 128 428 172 HOH HOH B . 
D 2 HOH 129 429 245 HOH HOH B . 
D 2 HOH 130 430 259 HOH HOH B . 
D 2 HOH 131 431 151 HOH HOH B . 
D 2 HOH 132 432 189 HOH HOH B . 
D 2 HOH 133 433 202 HOH HOH B . 
D 2 HOH 134 434 232 HOH HOH B . 
D 2 HOH 135 435 240 HOH HOH B . 
D 2 HOH 136 436 102 HOH HOH B . 
D 2 HOH 137 437 249 HOH HOH B . 
D 2 HOH 138 438 231 HOH HOH B . 
D 2 HOH 139 439 200 HOH HOH B . 
D 2 HOH 140 440 130 HOH HOH B . 
D 2 HOH 141 441 88  HOH HOH B . 
D 2 HOH 142 442 171 HOH HOH B . 
D 2 HOH 143 443 71  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A LYS 131 ? NZ  ? A LYS 129 NZ  
2 1 Y 1 A ILE 171 ? CD1 ? A ILE 169 CD1 
3 1 Y 1 B LYS 131 ? NZ  ? B LYS 129 NZ  
4 1 Y 1 B ILE 171 ? CD1 ? B ILE 169 CD1 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   91.18 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8JL7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.681 
_cell.length_a_esd                 ? 
_cell.length_b                     53.479 
_cell.length_b_esd                 ? 
_cell.length_c                     98.187 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         8JL7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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                   8JL7 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.14 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.58 
_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, HANGING DROP' 
_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    '0.1M Tris pH 8.0, 0.2M lithium chloride, 20% PEG 6000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     193 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 225 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-06-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00000 
_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                        'PAL/PLS BEAMLINE 5C (4A)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   '5C (4A)' 
_diffrn_source.pdbx_synchrotron_site       PAL/PLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8JL7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.76 
_reflns.d_resolution_low                               50.00 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     41907 
_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                           97.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.265 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.093 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       218715 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   0.999 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.086 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.76 1.82  ? ? ? ? ? ? 3839 ? ? ? ? ? ? ? ? ? ? ? 3.4 0.552 ? ? 0.397 0.193 ? 1  1 0.730 0.918 ? 89.0 ? 0.344 ? ? ? ? ? ? ? ? ? 
1.82 1.90  ? ? ? ? ? ? 4119 ? ? ? ? ? ? ? ? ? ? ? 4.0 0.672 ? ? 0.350 0.161 ? 2  1 0.876 0.966 ? 95.7 ? 0.309 ? ? ? ? ? ? ? ? ? 
1.90 1.98  ? ? ? ? ? ? 4093 ? ? ? ? ? ? ? ? ? ? ? 4.4 0.849 ? ? 0.285 0.126 ? 3  1 0.938 0.984 ? 95.5 ? 0.254 ? ? ? ? ? ? ? ? ? 
1.98 2.09  ? ? ? ? ? ? 4141 ? ? ? ? ? ? ? ? ? ? ? 4.7 1.024 ? ? 0.233 0.100 ? 4  1 0.966 0.991 ? 96.9 ? 0.210 ? ? ? ? ? ? ? ? ? 
2.09 2.22  ? ? ? ? ? ? 4182 ? ? ? ? ? ? ? ? ? ? ? 5.0 1.194 ? ? 0.195 0.081 ? 5  1 0.973 0.993 ? 97.8 ? 0.176 ? ? ? ? ? ? ? ? ? 
2.22 2.39  ? ? ? ? ? ? 4226 ? ? ? ? ? ? ? ? ? ? ? 5.3 1.280 ? ? 0.165 0.067 ? 6  1 0.986 0.996 ? 98.5 ? 0.150 ? ? ? ? ? ? ? ? ? 
2.39 2.63  ? ? ? ? ? ? 4290 ? ? ? ? ? ? ? ? ? ? ? 5.7 1.394 ? ? 0.135 0.054 ? 7  1 0.991 0.998 ? 99.1 ? 0.124 ? ? ? ? ? ? ? ? ? 
2.63 3.01  ? ? ? ? ? ? 4302 ? ? ? ? ? ? ? ? ? ? ? 6.1 1.478 ? ? 0.106 0.041 ? 8  1 0.995 0.999 ? 99.5 ? 0.098 ? ? ? ? ? ? ? ? ? 
3.01 3.79  ? ? ? ? ? ? 4336 ? ? ? ? ? ? ? ? ? ? ? 6.6 1.649 ? ? 0.074 0.028 ? 9  1 0.997 0.999 ? 99.6 ? 0.069 ? ? ? ? ? ? ? ? ? 
3.79 50.00 ? ? ? ? ? ? 4379 ? ? ? ? ? ? ? ? ? ? ? 6.8 1.578 ? ? 0.065 0.025 ? 10 1 0.997 0.999 ? 98.9 ? 0.060 ? ? ? ? ? ? ? ? ? 
# 
_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                                 8JL7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.76 
_refine.ls_d_res_low                             38.65 
_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                     41863 
_refine.ls_number_reflns_R_free                  2010 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.84 
_refine.ls_percent_reflns_R_free                 4.80 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2138 
_refine.ls_R_factor_R_free                       0.2494 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2120 
_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                          1.47 
_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                 27.72 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.19 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.76 
_refine_hist.d_res_low                        38.65 
_refine_hist.number_atoms_solvent             263 
_refine_hist.number_atoms_total               3859 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3596 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 3680 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.094 ? 4974 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.744 ? 480  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.070 ? 530  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 650  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.76 1.80  . . 125 2489 85.00  . . . . 0.2919 . . . . . . . . . . . 0.2819 
'X-RAY DIFFRACTION' 1.80 1.85  . . 135 2754 94.00  . . . . 0.2797 . . . . . . . . . . . 0.3083 
'X-RAY DIFFRACTION' 1.85 1.91  . . 145 2807 96.00  . . . . 0.2592 . . . . . . . . . . . 0.2890 
'X-RAY DIFFRACTION' 1.91 1.97  . . 139 2810 96.00  . . . . 0.2443 . . . . . . . . . . . 0.2784 
'X-RAY DIFFRACTION' 1.97 2.04  . . 138 2793 96.00  . . . . 0.2139 . . . . . . . . . . . 0.2699 
'X-RAY DIFFRACTION' 2.04 2.12  . . 140 2881 97.00  . . . . 0.2124 . . . . . . . . . . . 0.2025 
'X-RAY DIFFRACTION' 2.12 2.21  . . 141 2841 98.00  . . . . 0.2123 . . . . . . . . . . . 0.2736 
'X-RAY DIFFRACTION' 2.22 2.33  . . 146 2899 98.00  . . . . 0.2166 . . . . . . . . . . . 0.2295 
'X-RAY DIFFRACTION' 2.33 2.48  . . 151 2876 99.00  . . . . 0.2120 . . . . . . . . . . . 0.2803 
'X-RAY DIFFRACTION' 2.48 2.67  . . 149 2915 99.00  . . . . 0.2244 . . . . . . . . . . . 0.2522 
'X-RAY DIFFRACTION' 2.67 2.94  . . 148 2927 99.00  . . . . 0.2233 . . . . . . . . . . . 0.2496 
'X-RAY DIFFRACTION' 2.94 3.36  . . 150 2938 100.00 . . . . 0.2067 . . . . . . . . . . . 0.2524 
'X-RAY DIFFRACTION' 3.36 4.23  . . 151 2952 100.00 . . . . 0.1887 . . . . . . . . . . . 0.2181 
'X-RAY DIFFRACTION' 4.24 38.65 . . 152 2971 98.00  . . . . 0.1885 . . . . . . . . . . . 0.2489 
# 
_struct.entry_id                     8JL7 
_struct.title                        'Crystal structure of the Green fluorescent protein SEA227D variant at pH 8.0' 
_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        8JL7 
_struct_keywords.text            'bioimaging, Sensor. GFP, FLUORESCENT PROTEIN' 
_struct_keywords.pdbx_keywords   'FLUORESCENT PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    GFP_AEQVI 
_struct_ref.pdbx_db_accession          P42212 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFSYGVQCFSRYPDHMKQ
HDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNG
IKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITHGMDELYK
;
_struct_ref.pdbx_align_begin           1 
# 
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 8JL7 A 1 ? 236 ? P42212 1 ? 238 ? 1 238 
2 1 8JL7 B 1 ? 236 ? P42212 1 ? 238 ? 1 238 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8JL7 LEU A 64  ? UNP P42212 PHE 64  'engineered mutation' 64  1  
1 8JL7 CRO A 65  ? UNP P42212 SER 65  chromophore           66  2  
1 8JL7 CRO A 65  ? UNP P42212 TYR 66  chromophore           66  3  
1 8JL7 CRO A 65  ? UNP P42212 GLY 67  chromophore           66  4  
1 8JL7 ARG A 78  ? UNP P42212 GLN 80  'engineered mutation' 80  5  
1 8JL7 ASP A 145 ? UNP P42212 SER 147 'engineered mutation' 147 6  
1 8JL7 GLN A 147 ? UNP P42212 ASN 149 'engineered mutation' 149 7  
1 8JL7 ALA A 161 ? UNP P42212 VAL 163 'engineered mutation' 163 8  
1 8JL7 GLY A 173 ? UNP P42212 SER 175 'engineered mutation' 175 9  
1 8JL7 PHE A 200 ? UNP P42212 SER 202 'engineered mutation' 202 10 
1 8JL7 THR A 202 ? UNP P42212 GLN 204 'engineered mutation' 204 11 
1 8JL7 THR A 204 ? UNP P42212 ALA 206 'engineered mutation' 206 12 
1 8JL7 ASP A 225 ? UNP P42212 ALA 227 'engineered mutation' 227 13 
2 8JL7 LEU B 64  ? UNP P42212 PHE 64  'engineered mutation' 64  14 
2 8JL7 CRO B 65  ? UNP P42212 SER 65  chromophore           66  15 
2 8JL7 CRO B 65  ? UNP P42212 TYR 66  chromophore           66  16 
2 8JL7 CRO B 65  ? UNP P42212 GLY 67  chromophore           66  17 
2 8JL7 ARG B 78  ? UNP P42212 GLN 80  'engineered mutation' 80  18 
2 8JL7 ASP B 145 ? UNP P42212 SER 147 'engineered mutation' 147 19 
2 8JL7 GLN B 147 ? UNP P42212 ASN 149 'engineered mutation' 149 20 
2 8JL7 ALA B 161 ? UNP P42212 VAL 163 'engineered mutation' 163 21 
2 8JL7 GLY B 173 ? UNP P42212 SER 175 'engineered mutation' 175 22 
2 8JL7 PHE B 200 ? UNP P42212 SER 202 'engineered mutation' 202 23 
2 8JL7 THR B 202 ? UNP P42212 GLN 204 'engineered mutation' 204 24 
2 8JL7 THR B 204 ? UNP P42212 ALA 206 'engineered mutation' 206 25 
2 8JL7 ASP B 225 ? UNP P42212 ALA 227 'engineered mutation' 227 26 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C 
2 1 B,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 4   ? THR A 9   ? GLY A 4   THR A 9   5 ? 6 
HELX_P HELX_P2  AA2 PRO A 56  ? VAL A 61  ? PRO A 56  VAL A 61  5 ? 6 
HELX_P HELX_P3  AA3 VAL A 66  ? SER A 70  ? VAL A 68  SER A 72  5 ? 5 
HELX_P HELX_P4  AA4 PRO A 73  ? HIS A 79  ? PRO A 75  HIS A 81  5 ? 7 
HELX_P HELX_P5  AA5 ASP A 80  ? ALA A 85  ? ASP A 82  ALA A 87  1 ? 6 
HELX_P HELX_P6  AA6 LYS A 154 ? ASN A 157 ? LYS A 156 ASN A 159 5 ? 4 
HELX_P HELX_P7  AA7 LYS B 3   ? THR B 9   ? LYS B 3   THR B 9   5 ? 7 
HELX_P HELX_P8  AA8 PRO B 56  ? VAL B 61  ? PRO B 56  VAL B 61  5 ? 6 
HELX_P HELX_P9  AA9 VAL B 66  ? SER B 70  ? VAL B 68  SER B 72  5 ? 5 
HELX_P HELX_P10 AB1 PRO B 73  ? LYS B 77  ? PRO B 75  LYS B 79  5 ? 5 
HELX_P HELX_P11 AB2 ASP B 80  ? ALA B 85  ? ASP B 82  ALA B 87  1 ? 6 
HELX_P HELX_P12 AB3 LYS B 154 ? ASN B 157 ? LYS B 156 ASN B 159 5 ? 4 
# 
_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 
covale1 covale both ? A LEU 64 C  ? ? ? 1_555 A CRO 65 N1 ? ? A LEU 64 A CRO 66 1_555 ? ? ? ? ? ? ? 1.377 ? ? 
covale2 covale both ? A CRO 65 C3 ? ? ? 1_555 A VAL 66 N  ? ? A CRO 66 A VAL 68 1_555 ? ? ? ? ? ? ? 1.320 ? ? 
covale3 covale both ? B LEU 64 C  ? ? ? 1_555 B CRO 65 N1 ? ? B LEU 64 B CRO 66 1_555 ? ? ? ? ? ? ? 1.429 ? ? 
covale4 covale both ? B CRO 65 C3 ? ? ? 1_555 B VAL 66 N  ? ? B CRO 66 B VAL 68 1_555 ? ? ? ? ? ? ? 1.397 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CRO A 65 ? . . . . CRO A 66 ? 1_555 . . . . . . . 'THR, TYR, GLY' 1 CRO None Chromophore/chromophore-like 
2 CRO B 65 ? . . . . CRO B 66 ? 1_555 . . . . . . . 'THR, TYR, GLY' 1 CRO None Chromophore/chromophore-like 
# 
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 MET 86 A . ? MET 88 A PRO 87 A ? PRO 89 A 1 -0.69 
2 MET 86 B . ? MET 88 B PRO 87 B ? PRO 89 B 1 5.12  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 12 ? 
AA2 ? 12 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA1 5  6  ? anti-parallel 
AA1 6  7  ? anti-parallel 
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? anti-parallel 
AA1 11 12 ? parallel      
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? anti-parallel 
AA2 5  6  ? anti-parallel 
AA2 6  7  ? anti-parallel 
AA2 7  8  ? anti-parallel 
AA2 8  9  ? anti-parallel 
AA2 9  10 ? anti-parallel 
AA2 10 11 ? anti-parallel 
AA2 11 12 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  VAL A 12  ? VAL A 22  ? VAL A 12  VAL A 22  
AA1 2  HIS A 25  ? ASP A 36  ? HIS A 25  ASP A 36  
AA1 3  LYS A 41  ? CYS A 48  ? LYS A 41  CYS A 48  
AA1 4  HIS A 215 ? ASP A 225 ? HIS A 217 ASP A 227 
AA1 5  HIS A 197 ? SER A 206 ? HIS A 199 SER A 208 
AA1 6  VAL A 148 ? ASP A 153 ? VAL A 150 ASP A 155 
AA1 7  GLY A 158 ? ASN A 168 ? GLY A 160 ASN A 170 
AA1 8  VAL A 174 ? PRO A 185 ? VAL A 176 PRO A 187 
AA1 9  TYR A 90  ? PHE A 98  ? TYR A 92  PHE A 100 
AA1 10 ASN A 103 ? GLU A 113 ? ASN A 105 GLU A 115 
AA1 11 THR A 116 ? ILE A 126 ? THR A 118 ILE A 128 
AA1 12 VAL A 12  ? VAL A 22  ? VAL A 12  VAL A 22  
AA2 1  VAL B 12  ? VAL B 22  ? VAL B 12  VAL B 22  
AA2 2  HIS B 25  ? ASP B 36  ? HIS B 25  ASP B 36  
AA2 3  LYS B 41  ? CYS B 48  ? LYS B 41  CYS B 48  
AA2 4  HIS B 215 ? ASP B 225 ? HIS B 217 ASP B 227 
AA2 5  HIS B 197 ? SER B 206 ? HIS B 199 SER B 208 
AA2 6  VAL B 148 ? ASP B 153 ? VAL B 150 ASP B 155 
AA2 7  GLY B 158 ? ASN B 168 ? GLY B 160 ASN B 170 
AA2 8  VAL B 174 ? PRO B 185 ? VAL B 176 PRO B 187 
AA2 9  TYR B 90  ? PHE B 98  ? TYR B 92  PHE B 100 
AA2 10 ASN B 103 ? GLU B 113 ? ASN B 105 GLU B 115 
AA2 11 THR B 116 ? ILE B 126 ? THR B 118 ILE B 128 
AA2 12 VAL B 12  ? VAL B 22  ? VAL B 12  VAL B 22  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N LEU A 18  ? N LEU A 18  O VAL A 29  ? O VAL A 29  
AA1 2  3  N SER A 30  ? N SER A 30  O ILE A 47  ? O ILE A 47  
AA1 3  4  N PHE A 46  ? N PHE A 46  O MET A 216 ? O MET A 218 
AA1 4  5  O LEU A 219 ? O LEU A 221 N THR A 204 ? N THR A 206 
AA1 5  6  O HIS A 197 ? O HIS A 199 N ILE A 150 ? N ILE A 152 
AA1 6  7  N ASP A 153 ? N ASP A 155 O GLY A 158 ? O GLY A 160 
AA1 7  8  N PHE A 163 ? N PHE A 165 O HIS A 179 ? O HIS A 181 
AA1 8  9  O GLN A 182 ? O GLN A 184 N GLU A 93  ? N GLU A 95  
AA1 9  10 N ARG A 94  ? N ARG A 96  O THR A 106 ? O THR A 108 
AA1 10 11 N LYS A 111 ? N LYS A 113 O VAL A 118 ? O VAL A 120 
AA1 11 12 O GLY A 125 ? O GLY A 127 N ASP A 21  ? N ASP A 21  
AA2 1  2  N VAL B 12  ? N VAL B 12  O GLY B 35  ? O GLY B 35  
AA2 2  3  N SER B 30  ? N SER B 30  O ILE B 47  ? O ILE B 47  
AA2 3  4  N LEU B 44  ? N LEU B 44  O LEU B 218 ? O LEU B 220 
AA2 4  5  O THR B 223 ? O THR B 225 N PHE B 200 ? N PHE B 202 
AA2 5  6  O HIS B 197 ? O HIS B 199 N ILE B 150 ? N ILE B 152 
AA2 6  7  N ASP B 153 ? N ASP B 155 O GLY B 158 ? O GLY B 160 
AA2 7  8  N PHE B 163 ? N PHE B 165 O HIS B 179 ? O HIS B 181 
AA2 8  9  O THR B 184 ? O THR B 186 N VAL B 91  ? N VAL B 93  
AA2 9  10 N ILE B 96  ? N ILE B 98  O TYR B 104 ? O TYR B 106 
AA2 10 11 N LYS B 111 ? N LYS B 113 O VAL B 118 ? O VAL B 120 
AA2 11 12 O GLY B 125 ? O GLY B 127 N ASP B 21  ? N ASP B 21  
# 
_pdbx_entry_details.entry_id                   8JL7 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 N  A ASP 82  ? ? CA A ASP 82  ? ? C A ASP 82  ? ? 87.97  111.00 -23.03 2.70 N 
2 1 CB A ASP 173 ? ? CA A ASP 173 ? ? C A ASP 173 ? ? 85.81  110.40 -24.59 2.00 N 
3 1 N  A GLY 174 ? ? CA A GLY 174 ? ? C A GLY 174 ? ? 136.48 113.10 23.38  2.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 77  ? ? -69.20  3.55    
2 1 LYS A 79  ? ? -49.42  -10.15  
3 1 ASP A 103 ? ? -157.71 -159.17 
4 1 ILE A 136 ? ? -93.50  -62.52  
5 1 ILE B 136 ? ? -94.06  -62.04  
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A CRO 65 A CRO 66 ? SER chromophore 
2 A CRO 65 A CRO 66 ? TYR chromophore 
3 A CRO 65 A CRO 66 ? GLY chromophore 
4 B CRO 65 B CRO 66 ? SER chromophore 
5 B CRO 65 B CRO 66 ? TYR chromophore 
6 B CRO 65 B CRO 66 ? GLY chromophore 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       420 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.29 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A SER 2   ? A SER 2   
3  1 Y 1 A GLY 228 ? A GLY 226 
4  1 Y 1 A ILE 229 ? A ILE 227 
5  1 Y 1 A THR 230 ? A THR 228 
6  1 Y 1 A HIS 231 ? A HIS 229 
7  1 Y 1 A GLY 232 ? A GLY 230 
8  1 Y 1 A MET 233 ? A MET 231 
9  1 Y 1 A ASP 234 ? A ASP 232 
10 1 Y 1 A GLU 235 ? A GLU 233 
11 1 Y 1 A LEU 236 ? A LEU 234 
12 1 Y 1 A TYR 237 ? A TYR 235 
13 1 Y 1 A LYS 238 ? A LYS 236 
14 1 Y 1 B MET 1   ? B MET 1   
15 1 Y 1 B SER 2   ? B SER 2   
16 1 Y 1 B GLY 228 ? B GLY 226 
17 1 Y 1 B ILE 229 ? B ILE 227 
18 1 Y 1 B THR 230 ? B THR 228 
19 1 Y 1 B HIS 231 ? B HIS 229 
20 1 Y 1 B GLY 232 ? B GLY 230 
21 1 Y 1 B MET 233 ? B MET 231 
22 1 Y 1 B ASP 234 ? B ASP 232 
23 1 Y 1 B GLU 235 ? B GLU 233 
24 1 Y 1 B LEU 236 ? B LEU 234 
25 1 Y 1 B TYR 237 ? B TYR 235 
26 1 Y 1 B LYS 238 ? B LYS 236 
# 
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  
CRO N1   N N N 74  
CRO CA1  C N R 75  
CRO CB1  C N R 76  
CRO CG1  C N N 77  
CRO OG1  O N N 78  
CRO C1   C N N 79  
CRO N2   N N N 80  
CRO N3   N N N 81  
CRO C2   C N N 82  
CRO O2   O N N 83  
CRO CA2  C N N 84  
CRO CA3  C N N 85  
CRO C3   C N N 86  
CRO O3   O N N 87  
CRO CB2  C N N 88  
CRO CG2  C Y N 89  
CRO CD1  C Y N 90  
CRO CD2  C Y N 91  
CRO CE1  C Y N 92  
CRO CE2  C Y N 93  
CRO CZ   C Y N 94  
CRO OH   O N N 95  
CRO OXT  O N N 96  
CRO H    H N N 97  
CRO H2   H N N 98  
CRO HA1  H N N 99  
CRO HB1  H N N 100 
CRO HG11 H N N 101 
CRO HG12 H N N 102 
CRO HG13 H N N 103 
CRO HOG1 H N N 104 
CRO HA31 H N N 105 
CRO HA32 H N N 106 
CRO HXT  H N N 107 
CRO HB2  H N N 108 
CRO HD1  H N N 109 
CRO HD2  H N N 110 
CRO HE1  H N N 111 
CRO HE2  H N N 112 
CRO HOH  H N N 113 
CYS N    N N N 114 
CYS CA   C N R 115 
CYS C    C N N 116 
CYS O    O N N 117 
CYS CB   C N N 118 
CYS SG   S N N 119 
CYS OXT  O N N 120 
CYS H    H N N 121 
CYS H2   H N N 122 
CYS HA   H N N 123 
CYS HB2  H N N 124 
CYS HB3  H N N 125 
CYS HG   H N N 126 
CYS HXT  H N N 127 
GLN N    N N N 128 
GLN CA   C N S 129 
GLN C    C N N 130 
GLN O    O N N 131 
GLN CB   C N N 132 
GLN CG   C N N 133 
GLN CD   C N N 134 
GLN OE1  O N N 135 
GLN NE2  N N N 136 
GLN OXT  O N N 137 
GLN H    H N N 138 
GLN H2   H N N 139 
GLN HA   H N N 140 
GLN HB2  H N N 141 
GLN HB3  H N N 142 
GLN HG2  H N N 143 
GLN HG3  H N N 144 
GLN HE21 H N N 145 
GLN HE22 H N N 146 
GLN HXT  H N N 147 
GLU N    N N N 148 
GLU CA   C N S 149 
GLU C    C N N 150 
GLU O    O N N 151 
GLU CB   C N N 152 
GLU CG   C N N 153 
GLU CD   C N N 154 
GLU OE1  O N N 155 
GLU OE2  O N N 156 
GLU OXT  O N N 157 
GLU H    H N N 158 
GLU H2   H N N 159 
GLU HA   H N N 160 
GLU HB2  H N N 161 
GLU HB3  H N N 162 
GLU HG2  H N N 163 
GLU HG3  H N N 164 
GLU HE2  H N N 165 
GLU HXT  H N N 166 
GLY N    N N N 167 
GLY CA   C N N 168 
GLY C    C N N 169 
GLY O    O N N 170 
GLY OXT  O N N 171 
GLY H    H N N 172 
GLY H2   H N N 173 
GLY HA2  H N N 174 
GLY HA3  H N N 175 
GLY HXT  H N N 176 
HIS N    N N N 177 
HIS CA   C N S 178 
HIS C    C N N 179 
HIS O    O N N 180 
HIS CB   C N N 181 
HIS CG   C Y N 182 
HIS ND1  N Y N 183 
HIS CD2  C Y N 184 
HIS CE1  C Y N 185 
HIS NE2  N Y N 186 
HIS OXT  O N N 187 
HIS H    H N N 188 
HIS H2   H N N 189 
HIS HA   H N N 190 
HIS HB2  H N N 191 
HIS HB3  H N N 192 
HIS HD1  H N N 193 
HIS HD2  H N N 194 
HIS HE1  H N N 195 
HIS HE2  H N N 196 
HIS HXT  H N N 197 
HOH O    O N N 198 
HOH H1   H N N 199 
HOH H2   H N N 200 
ILE N    N N N 201 
ILE CA   C N S 202 
ILE C    C N N 203 
ILE O    O N N 204 
ILE CB   C N S 205 
ILE CG1  C N N 206 
ILE CG2  C N N 207 
ILE CD1  C N N 208 
ILE OXT  O N N 209 
ILE H    H N N 210 
ILE H2   H N N 211 
ILE HA   H N N 212 
ILE HB   H N N 213 
ILE HG12 H N N 214 
ILE HG13 H N N 215 
ILE HG21 H N N 216 
ILE HG22 H N N 217 
ILE HG23 H N N 218 
ILE HD11 H N N 219 
ILE HD12 H N N 220 
ILE HD13 H N N 221 
ILE HXT  H N N 222 
LEU N    N N N 223 
LEU CA   C N S 224 
LEU C    C N N 225 
LEU O    O N N 226 
LEU CB   C N N 227 
LEU CG   C N N 228 
LEU CD1  C N N 229 
LEU CD2  C N N 230 
LEU OXT  O N N 231 
LEU H    H N N 232 
LEU H2   H N N 233 
LEU HA   H N N 234 
LEU HB2  H N N 235 
LEU HB3  H N N 236 
LEU HG   H N N 237 
LEU HD11 H N N 238 
LEU HD12 H N N 239 
LEU HD13 H N N 240 
LEU HD21 H N N 241 
LEU HD22 H N N 242 
LEU HD23 H N N 243 
LEU HXT  H N N 244 
LYS N    N N N 245 
LYS CA   C N S 246 
LYS C    C N N 247 
LYS O    O N N 248 
LYS CB   C N N 249 
LYS CG   C N N 250 
LYS CD   C N N 251 
LYS CE   C N N 252 
LYS NZ   N N N 253 
LYS OXT  O N N 254 
LYS H    H N N 255 
LYS H2   H N N 256 
LYS HA   H N N 257 
LYS HB2  H N N 258 
LYS HB3  H N N 259 
LYS HG2  H N N 260 
LYS HG3  H N N 261 
LYS HD2  H N N 262 
LYS HD3  H N N 263 
LYS HE2  H N N 264 
LYS HE3  H N N 265 
LYS HZ1  H N N 266 
LYS HZ2  H N N 267 
LYS HZ3  H N N 268 
LYS HXT  H N N 269 
MET N    N N N 270 
MET CA   C N S 271 
MET C    C N N 272 
MET O    O N N 273 
MET CB   C N N 274 
MET CG   C N N 275 
MET SD   S N N 276 
MET CE   C N N 277 
MET OXT  O N N 278 
MET H    H N N 279 
MET H2   H N N 280 
MET HA   H N N 281 
MET HB2  H N N 282 
MET HB3  H N N 283 
MET HG2  H N N 284 
MET HG3  H N N 285 
MET HE1  H N N 286 
MET HE2  H N N 287 
MET HE3  H N N 288 
MET HXT  H N N 289 
PHE N    N N N 290 
PHE CA   C N S 291 
PHE C    C N N 292 
PHE O    O N N 293 
PHE CB   C N N 294 
PHE CG   C Y N 295 
PHE CD1  C Y N 296 
PHE CD2  C Y N 297 
PHE CE1  C Y N 298 
PHE CE2  C Y N 299 
PHE CZ   C Y N 300 
PHE OXT  O N N 301 
PHE H    H N N 302 
PHE H2   H N N 303 
PHE HA   H N N 304 
PHE HB2  H N N 305 
PHE HB3  H N N 306 
PHE HD1  H N N 307 
PHE HD2  H N N 308 
PHE HE1  H N N 309 
PHE HE2  H N N 310 
PHE HZ   H N N 311 
PHE HXT  H N N 312 
PRO N    N N N 313 
PRO CA   C N S 314 
PRO C    C N N 315 
PRO O    O N N 316 
PRO CB   C N N 317 
PRO CG   C N N 318 
PRO CD   C N N 319 
PRO OXT  O N N 320 
PRO H    H N N 321 
PRO HA   H N N 322 
PRO HB2  H N N 323 
PRO HB3  H N N 324 
PRO HG2  H N N 325 
PRO HG3  H N N 326 
PRO HD2  H N N 327 
PRO HD3  H N N 328 
PRO HXT  H N N 329 
SER N    N N N 330 
SER CA   C N S 331 
SER C    C N N 332 
SER O    O N N 333 
SER CB   C N N 334 
SER OG   O N N 335 
SER OXT  O N N 336 
SER H    H N N 337 
SER H2   H N N 338 
SER HA   H N N 339 
SER HB2  H N N 340 
SER HB3  H N N 341 
SER HG   H N N 342 
SER HXT  H N N 343 
THR N    N N N 344 
THR CA   C N S 345 
THR C    C N N 346 
THR O    O N N 347 
THR CB   C N R 348 
THR OG1  O N N 349 
THR CG2  C N N 350 
THR OXT  O N N 351 
THR H    H N N 352 
THR H2   H N N 353 
THR HA   H N N 354 
THR HB   H N N 355 
THR HG1  H N N 356 
THR HG21 H N N 357 
THR HG22 H N N 358 
THR HG23 H N N 359 
THR HXT  H N N 360 
TRP N    N N N 361 
TRP CA   C N S 362 
TRP C    C N N 363 
TRP O    O N N 364 
TRP CB   C N N 365 
TRP CG   C Y N 366 
TRP CD1  C Y N 367 
TRP CD2  C Y N 368 
TRP NE1  N Y N 369 
TRP CE2  C Y N 370 
TRP CE3  C Y N 371 
TRP CZ2  C Y N 372 
TRP CZ3  C Y N 373 
TRP CH2  C Y N 374 
TRP OXT  O N N 375 
TRP H    H N N 376 
TRP H2   H N N 377 
TRP HA   H N N 378 
TRP HB2  H N N 379 
TRP HB3  H N N 380 
TRP HD1  H N N 381 
TRP HE1  H N N 382 
TRP HE3  H N N 383 
TRP HZ2  H N N 384 
TRP HZ3  H N N 385 
TRP HH2  H N N 386 
TRP HXT  H N N 387 
TYR N    N N N 388 
TYR CA   C N S 389 
TYR C    C N N 390 
TYR O    O N N 391 
TYR CB   C N N 392 
TYR CG   C Y N 393 
TYR CD1  C Y N 394 
TYR CD2  C Y N 395 
TYR CE1  C Y N 396 
TYR CE2  C Y N 397 
TYR CZ   C Y N 398 
TYR OH   O N N 399 
TYR OXT  O N N 400 
TYR H    H N N 401 
TYR H2   H N N 402 
TYR HA   H N N 403 
TYR HB2  H N N 404 
TYR HB3  H N N 405 
TYR HD1  H N N 406 
TYR HD2  H N N 407 
TYR HE1  H N N 408 
TYR HE2  H N N 409 
TYR HH   H N N 410 
TYR HXT  H N N 411 
VAL N    N N N 412 
VAL CA   C N S 413 
VAL C    C N N 414 
VAL O    O N N 415 
VAL CB   C N N 416 
VAL CG1  C N N 417 
VAL CG2  C N N 418 
VAL OXT  O N N 419 
VAL H    H N N 420 
VAL H2   H N N 421 
VAL HA   H N N 422 
VAL HB   H N N 423 
VAL HG11 H N N 424 
VAL HG12 H N N 425 
VAL HG13 H N N 426 
VAL HG21 H N N 427 
VAL HG22 H N N 428 
VAL HG23 H N N 429 
VAL HXT  H N N 430 
# 
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  
CRO CG1 CB1  sing N N 70  
CRO OG1 CB1  sing N N 71  
CRO CB1 CA1  sing N N 72  
CRO N1  CA1  sing N N 73  
CRO OH  CZ   sing N N 74  
CRO CE1 CZ   doub Y N 75  
CRO CE1 CD1  sing Y N 76  
CRO CA1 C1   sing N N 77  
CRO CZ  CE2  sing Y N 78  
CRO CD1 CG2  doub Y N 79  
CRO N2  C1   doub N N 80  
CRO N2  CA2  sing N N 81  
CRO C1  N3   sing N N 82  
CRO CE2 CD2  doub Y N 83  
CRO CG2 CD2  sing Y N 84  
CRO CG2 CB2  sing N N 85  
CRO N3  CA3  sing N N 86  
CRO N3  C2   sing N N 87  
CRO CA2 CB2  doub N Z 88  
CRO CA2 C2   sing N N 89  
CRO CA3 C3   sing N N 90  
CRO OXT C3   sing N N 91  
CRO C3  O3   doub N N 92  
CRO C2  O2   doub N N 93  
CRO N1  H    sing N N 94  
CRO N1  H2   sing N N 95  
CRO CA1 HA1  sing N N 96  
CRO CB1 HB1  sing N N 97  
CRO CG1 HG11 sing N N 98  
CRO CG1 HG12 sing N N 99  
CRO CG1 HG13 sing N N 100 
CRO OG1 HOG1 sing N N 101 
CRO CA3 HA31 sing N N 102 
CRO CA3 HA32 sing N N 103 
CRO OXT HXT  sing N N 104 
CRO CB2 HB2  sing N N 105 
CRO CD1 HD1  sing N N 106 
CRO CD2 HD2  sing N N 107 
CRO CE1 HE1  sing N N 108 
CRO CE2 HE2  sing N N 109 
CRO OH  HOH  sing N N 110 
CYS N   CA   sing N N 111 
CYS N   H    sing N N 112 
CYS N   H2   sing N N 113 
CYS CA  C    sing N N 114 
CYS CA  CB   sing N N 115 
CYS CA  HA   sing N N 116 
CYS C   O    doub N N 117 
CYS C   OXT  sing N N 118 
CYS CB  SG   sing N N 119 
CYS CB  HB2  sing N N 120 
CYS CB  HB3  sing N N 121 
CYS SG  HG   sing N N 122 
CYS OXT HXT  sing N N 123 
GLN N   CA   sing N N 124 
GLN N   H    sing N N 125 
GLN N   H2   sing N N 126 
GLN CA  C    sing N N 127 
GLN CA  CB   sing N N 128 
GLN CA  HA   sing N N 129 
GLN C   O    doub N N 130 
GLN C   OXT  sing N N 131 
GLN CB  CG   sing N N 132 
GLN CB  HB2  sing N N 133 
GLN CB  HB3  sing N N 134 
GLN CG  CD   sing N N 135 
GLN CG  HG2  sing N N 136 
GLN CG  HG3  sing N N 137 
GLN CD  OE1  doub N N 138 
GLN CD  NE2  sing N N 139 
GLN NE2 HE21 sing N N 140 
GLN NE2 HE22 sing N N 141 
GLN OXT HXT  sing N N 142 
GLU N   CA   sing N N 143 
GLU N   H    sing N N 144 
GLU N   H2   sing N N 145 
GLU CA  C    sing N N 146 
GLU CA  CB   sing N N 147 
GLU CA  HA   sing N N 148 
GLU C   O    doub N N 149 
GLU C   OXT  sing N N 150 
GLU CB  CG   sing N N 151 
GLU CB  HB2  sing N N 152 
GLU CB  HB3  sing N N 153 
GLU CG  CD   sing N N 154 
GLU CG  HG2  sing N N 155 
GLU CG  HG3  sing N N 156 
GLU CD  OE1  doub N N 157 
GLU CD  OE2  sing N N 158 
GLU OE2 HE2  sing N N 159 
GLU OXT HXT  sing N N 160 
GLY N   CA   sing N N 161 
GLY N   H    sing N N 162 
GLY N   H2   sing N N 163 
GLY CA  C    sing N N 164 
GLY CA  HA2  sing N N 165 
GLY CA  HA3  sing N N 166 
GLY C   O    doub N N 167 
GLY C   OXT  sing N N 168 
GLY OXT HXT  sing N N 169 
HIS N   CA   sing N N 170 
HIS N   H    sing N N 171 
HIS N   H2   sing N N 172 
HIS CA  C    sing N N 173 
HIS CA  CB   sing N N 174 
HIS CA  HA   sing N N 175 
HIS C   O    doub N N 176 
HIS C   OXT  sing N N 177 
HIS CB  CG   sing N N 178 
HIS CB  HB2  sing N N 179 
HIS CB  HB3  sing N N 180 
HIS CG  ND1  sing Y N 181 
HIS CG  CD2  doub Y N 182 
HIS ND1 CE1  doub Y N 183 
HIS ND1 HD1  sing N N 184 
HIS CD2 NE2  sing Y N 185 
HIS CD2 HD2  sing N N 186 
HIS CE1 NE2  sing Y N 187 
HIS CE1 HE1  sing N N 188 
HIS NE2 HE2  sing N N 189 
HIS OXT HXT  sing N N 190 
HOH O   H1   sing N N 191 
HOH O   H2   sing N N 192 
ILE N   CA   sing N N 193 
ILE N   H    sing N N 194 
ILE N   H2   sing N N 195 
ILE CA  C    sing N N 196 
ILE CA  CB   sing N N 197 
ILE CA  HA   sing N N 198 
ILE C   O    doub N N 199 
ILE C   OXT  sing N N 200 
ILE CB  CG1  sing N N 201 
ILE CB  CG2  sing N N 202 
ILE CB  HB   sing N N 203 
ILE CG1 CD1  sing N N 204 
ILE CG1 HG12 sing N N 205 
ILE CG1 HG13 sing N N 206 
ILE CG2 HG21 sing N N 207 
ILE CG2 HG22 sing N N 208 
ILE CG2 HG23 sing N N 209 
ILE CD1 HD11 sing N N 210 
ILE CD1 HD12 sing N N 211 
ILE CD1 HD13 sing N N 212 
ILE OXT HXT  sing N N 213 
LEU N   CA   sing N N 214 
LEU N   H    sing N N 215 
LEU N   H2   sing N N 216 
LEU CA  C    sing N N 217 
LEU CA  CB   sing N N 218 
LEU CA  HA   sing N N 219 
LEU C   O    doub N N 220 
LEU C   OXT  sing N N 221 
LEU CB  CG   sing N N 222 
LEU CB  HB2  sing N N 223 
LEU CB  HB3  sing N N 224 
LEU CG  CD1  sing N N 225 
LEU CG  CD2  sing N N 226 
LEU CG  HG   sing N N 227 
LEU CD1 HD11 sing N N 228 
LEU CD1 HD12 sing N N 229 
LEU CD1 HD13 sing N N 230 
LEU CD2 HD21 sing N N 231 
LEU CD2 HD22 sing N N 232 
LEU CD2 HD23 sing N N 233 
LEU OXT HXT  sing N N 234 
LYS N   CA   sing N N 235 
LYS N   H    sing N N 236 
LYS N   H2   sing N N 237 
LYS CA  C    sing N N 238 
LYS CA  CB   sing N N 239 
LYS CA  HA   sing N N 240 
LYS C   O    doub N N 241 
LYS C   OXT  sing N N 242 
LYS CB  CG   sing N N 243 
LYS CB  HB2  sing N N 244 
LYS CB  HB3  sing N N 245 
LYS CG  CD   sing N N 246 
LYS CG  HG2  sing N N 247 
LYS CG  HG3  sing N N 248 
LYS CD  CE   sing N N 249 
LYS CD  HD2  sing N N 250 
LYS CD  HD3  sing N N 251 
LYS CE  NZ   sing N N 252 
LYS CE  HE2  sing N N 253 
LYS CE  HE3  sing N N 254 
LYS NZ  HZ1  sing N N 255 
LYS NZ  HZ2  sing N N 256 
LYS NZ  HZ3  sing N N 257 
LYS OXT HXT  sing N N 258 
MET N   CA   sing N N 259 
MET N   H    sing N N 260 
MET N   H2   sing N N 261 
MET CA  C    sing N N 262 
MET CA  CB   sing N N 263 
MET CA  HA   sing N N 264 
MET C   O    doub N N 265 
MET C   OXT  sing N N 266 
MET CB  CG   sing N N 267 
MET CB  HB2  sing N N 268 
MET CB  HB3  sing N N 269 
MET CG  SD   sing N N 270 
MET CG  HG2  sing N N 271 
MET CG  HG3  sing N N 272 
MET SD  CE   sing N N 273 
MET CE  HE1  sing N N 274 
MET CE  HE2  sing N N 275 
MET CE  HE3  sing N N 276 
MET OXT HXT  sing N N 277 
PHE N   CA   sing N N 278 
PHE N   H    sing N N 279 
PHE N   H2   sing N N 280 
PHE CA  C    sing N N 281 
PHE CA  CB   sing N N 282 
PHE CA  HA   sing N N 283 
PHE C   O    doub N N 284 
PHE C   OXT  sing N N 285 
PHE CB  CG   sing N N 286 
PHE CB  HB2  sing N N 287 
PHE CB  HB3  sing N N 288 
PHE CG  CD1  doub Y N 289 
PHE CG  CD2  sing Y N 290 
PHE CD1 CE1  sing Y N 291 
PHE CD1 HD1  sing N N 292 
PHE CD2 CE2  doub Y N 293 
PHE CD2 HD2  sing N N 294 
PHE CE1 CZ   doub Y N 295 
PHE CE1 HE1  sing N N 296 
PHE CE2 CZ   sing Y N 297 
PHE CE2 HE2  sing N N 298 
PHE CZ  HZ   sing N N 299 
PHE OXT HXT  sing N N 300 
PRO N   CA   sing N N 301 
PRO N   CD   sing N N 302 
PRO N   H    sing N N 303 
PRO CA  C    sing N N 304 
PRO CA  CB   sing N N 305 
PRO CA  HA   sing N N 306 
PRO C   O    doub N N 307 
PRO C   OXT  sing N N 308 
PRO CB  CG   sing N N 309 
PRO CB  HB2  sing N N 310 
PRO CB  HB3  sing N N 311 
PRO CG  CD   sing N N 312 
PRO CG  HG2  sing N N 313 
PRO CG  HG3  sing N N 314 
PRO CD  HD2  sing N N 315 
PRO CD  HD3  sing N N 316 
PRO OXT HXT  sing N N 317 
SER N   CA   sing N N 318 
SER N   H    sing N N 319 
SER N   H2   sing N N 320 
SER CA  C    sing N N 321 
SER CA  CB   sing N N 322 
SER CA  HA   sing N N 323 
SER C   O    doub N N 324 
SER C   OXT  sing N N 325 
SER CB  OG   sing N N 326 
SER CB  HB2  sing N N 327 
SER CB  HB3  sing N N 328 
SER OG  HG   sing N N 329 
SER OXT HXT  sing N N 330 
THR N   CA   sing N N 331 
THR N   H    sing N N 332 
THR N   H2   sing N N 333 
THR CA  C    sing N N 334 
THR CA  CB   sing N N 335 
THR CA  HA   sing N N 336 
THR C   O    doub N N 337 
THR C   OXT  sing N N 338 
THR CB  OG1  sing N N 339 
THR CB  CG2  sing N N 340 
THR CB  HB   sing N N 341 
THR OG1 HG1  sing N N 342 
THR CG2 HG21 sing N N 343 
THR CG2 HG22 sing N N 344 
THR CG2 HG23 sing N N 345 
THR OXT HXT  sing N N 346 
TRP N   CA   sing N N 347 
TRP N   H    sing N N 348 
TRP N   H2   sing N N 349 
TRP CA  C    sing N N 350 
TRP CA  CB   sing N N 351 
TRP CA  HA   sing N N 352 
TRP C   O    doub N N 353 
TRP C   OXT  sing N N 354 
TRP CB  CG   sing N N 355 
TRP CB  HB2  sing N N 356 
TRP CB  HB3  sing N N 357 
TRP CG  CD1  doub Y N 358 
TRP CG  CD2  sing Y N 359 
TRP CD1 NE1  sing Y N 360 
TRP CD1 HD1  sing N N 361 
TRP CD2 CE2  doub Y N 362 
TRP CD2 CE3  sing Y N 363 
TRP NE1 CE2  sing Y N 364 
TRP NE1 HE1  sing N N 365 
TRP CE2 CZ2  sing Y N 366 
TRP CE3 CZ3  doub Y N 367 
TRP CE3 HE3  sing N N 368 
TRP CZ2 CH2  doub Y N 369 
TRP CZ2 HZ2  sing N N 370 
TRP CZ3 CH2  sing Y N 371 
TRP CZ3 HZ3  sing N N 372 
TRP CH2 HH2  sing N N 373 
TRP OXT HXT  sing N N 374 
TYR N   CA   sing N N 375 
TYR N   H    sing N N 376 
TYR N   H2   sing N N 377 
TYR CA  C    sing N N 378 
TYR CA  CB   sing N N 379 
TYR CA  HA   sing N N 380 
TYR C   O    doub N N 381 
TYR C   OXT  sing N N 382 
TYR CB  CG   sing N N 383 
TYR CB  HB2  sing N N 384 
TYR CB  HB3  sing N N 385 
TYR CG  CD1  doub Y N 386 
TYR CG  CD2  sing Y N 387 
TYR CD1 CE1  sing Y N 388 
TYR CD1 HD1  sing N N 389 
TYR CD2 CE2  doub Y N 390 
TYR CD2 HD2  sing N N 391 
TYR CE1 CZ   doub Y N 392 
TYR CE1 HE1  sing N N 393 
TYR CE2 CZ   sing Y N 394 
TYR CE2 HE2  sing N N 395 
TYR CZ  OH   sing N N 396 
TYR OH  HH   sing N N 397 
TYR OXT HXT  sing N N 398 
VAL N   CA   sing N N 399 
VAL N   H    sing N N 400 
VAL N   H2   sing N N 401 
VAL CA  C    sing N N 402 
VAL CA  CB   sing N N 403 
VAL CA  HA   sing N N 404 
VAL C   O    doub N N 405 
VAL C   OXT  sing N N 406 
VAL CB  CG1  sing N N 407 
VAL CB  CG2  sing N N 408 
VAL CB  HB   sing N N 409 
VAL CG1 HG11 sing N N 410 
VAL CG1 HG12 sing N N 411 
VAL CG1 HG13 sing N N 412 
VAL CG2 HG21 sing N N 413 
VAL CG2 HG22 sing N N 414 
VAL CG2 HG23 sing N N 415 
VAL OXT HXT  sing N N 416 
# 
_pdbx_audit_support.funding_organization   'National Research Foundation (NRF, Korea)' 
_pdbx_audit_support.country                'Korea, Republic Of' 
_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   5WWK 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8JL7 
_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.fract_transf_matrix[1][1]   0.023992 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000494 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018699 
_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]   0.010187 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
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   . LYS A 1 3   ? -17.385 27.833  -16.319 1.00 51.81 ? 3   LYS A N   1 
ATOM   2    C CA  . LYS A 1 3   ? -16.146 27.277  -15.788 1.00 51.18 ? 3   LYS A CA  1 
ATOM   3    C C   . LYS A 1 3   ? -16.405 26.636  -14.420 1.00 50.65 ? 3   LYS A C   1 
ATOM   4    O O   . LYS A 1 3   ? -17.521 26.186  -14.132 1.00 48.29 ? 3   LYS A O   1 
ATOM   5    C CB  . LYS A 1 3   ? -15.085 28.377  -15.685 1.00 53.07 ? 3   LYS A CB  1 
ATOM   6    C CG  . LYS A 1 3   ? -13.983 28.291  -16.733 1.00 56.99 ? 3   LYS A CG  1 
ATOM   7    C CD  . LYS A 1 3   ? -12.747 29.090  -16.327 1.00 54.79 ? 3   LYS A CD  1 
ATOM   8    C CE  . LYS A 1 3   ? -11.747 28.249  -15.549 1.00 52.06 ? 3   LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 3   ? -11.375 26.977  -16.244 1.00 50.86 ? 3   LYS A NZ  1 
ATOM   10   N N   . GLY A 1 4   ? -15.370 26.575  -13.579 1.00 45.12 ? 4   GLY A N   1 
ATOM   11   C CA  . GLY A 1 4   ? -15.610 26.326  -12.167 1.00 39.26 ? 4   GLY A CA  1 
ATOM   12   C C   . GLY A 1 4   ? -16.461 27.412  -11.543 1.00 41.19 ? 4   GLY A C   1 
ATOM   13   O O   . GLY A 1 4   ? -17.232 27.150  -10.614 1.00 36.21 ? 4   GLY A O   1 
ATOM   14   N N   . GLU A 1 5   ? -16.354 28.641  -12.068 1.00 42.92 ? 5   GLU A N   1 
ATOM   15   C CA  . GLU A 1 5   ? -17.188 29.748  -11.611 1.00 43.48 ? 5   GLU A CA  1 
ATOM   16   C C   . GLU A 1 5   ? -18.668 29.412  -11.754 1.00 43.42 ? 5   GLU A C   1 
ATOM   17   O O   . GLU A 1 5   ? -19.488 29.860  -10.946 1.00 43.02 ? 5   GLU A O   1 
ATOM   18   C CB  . GLU A 1 5   ? -16.820 31.010  -12.406 1.00 47.22 ? 5   GLU A CB  1 
ATOM   19   C CG  . GLU A 1 5   ? -17.322 32.385  -11.901 1.00 52.92 ? 5   GLU A CG  1 
ATOM   20   C CD  . GLU A 1 5   ? -18.816 32.484  -11.636 1.00 56.58 ? 5   GLU A CD  1 
ATOM   21   O OE1 . GLU A 1 5   ? -19.597 32.525  -12.619 1.00 59.23 ? 5   GLU A OE1 1 
ATOM   22   O OE2 . GLU A 1 5   ? -19.207 32.549  -10.444 1.00 54.58 ? 5   GLU A OE2 1 
ATOM   23   N N   . GLU A 1 6   ? -19.029 28.603  -12.755 1.00 45.82 ? 6   GLU A N   1 
ATOM   24   C CA  . GLU A 1 6   ? -20.432 28.262  -12.958 1.00 45.75 ? 6   GLU A CA  1 
ATOM   25   C C   . GLU A 1 6   ? -20.984 27.430  -11.808 1.00 39.70 ? 6   GLU A C   1 
ATOM   26   O O   . GLU A 1 6   ? -22.199 27.405  -11.593 1.00 38.95 ? 6   GLU A O   1 
ATOM   27   C CB  . GLU A 1 6   ? -20.595 27.513  -14.287 1.00 48.20 ? 6   GLU A CB  1 
ATOM   28   C CG  . GLU A 1 6   ? -20.754 28.397  -15.556 1.00 50.82 ? 6   GLU A CG  1 
ATOM   29   C CD  . GLU A 1 6   ? -21.652 29.643  -15.422 1.00 57.13 ? 6   GLU A CD  1 
ATOM   30   O OE1 . GLU A 1 6   ? -21.720 30.418  -16.401 1.00 62.87 ? 6   GLU A OE1 1 
ATOM   31   O OE2 . GLU A 1 6   ? -22.373 29.813  -14.417 1.00 57.12 ? 6   GLU A OE2 1 
ATOM   32   N N   . LEU A 1 7   ? -20.120 26.760  -11.055 1.00 36.96 ? 7   LEU A N   1 
ATOM   33   C CA  . LEU A 1 7   ? -20.577 26.019  -9.892  1.00 35.75 ? 7   LEU A CA  1 
ATOM   34   C C   . LEU A 1 7   ? -20.940 26.930  -8.727  1.00 35.92 ? 7   LEU A C   1 
ATOM   35   O O   . LEU A 1 7   ? -21.459 26.431  -7.723  1.00 32.89 ? 7   LEU A O   1 
ATOM   36   C CB  . LEU A 1 7   ? -19.498 25.025  -9.469  1.00 35.97 ? 7   LEU A CB  1 
ATOM   37   C CG  . LEU A 1 7   ? -19.162 23.880  -10.429 1.00 35.64 ? 7   LEU A CG  1 
ATOM   38   C CD1 . LEU A 1 7   ? -18.177 22.941  -9.778  1.00 33.69 ? 7   LEU A CD1 1 
ATOM   39   C CD2 . LEU A 1 7   ? -20.409 23.114  -10.847 1.00 36.84 ? 7   LEU A CD2 1 
ATOM   40   N N   . PHE A 1 8   ? -20.714 28.244  -8.845  1.00 35.19 ? 8   PHE A N   1 
ATOM   41   C CA  . PHE A 1 8   ? -20.907 29.175  -7.735  1.00 34.28 ? 8   PHE A CA  1 
ATOM   42   C C   . PHE A 1 8   ? -21.962 30.244  -8.000  1.00 39.25 ? 8   PHE A C   1 
ATOM   43   O O   . PHE A 1 8   ? -22.073 31.190  -7.213  1.00 37.58 ? 8   PHE A O   1 
ATOM   44   C CB  . PHE A 1 8   ? -19.583 29.867  -7.374  1.00 32.97 ? 8   PHE A CB  1 
ATOM   45   C CG  . PHE A 1 8   ? -18.542 28.940  -6.800  1.00 32.46 ? 8   PHE A CG  1 
ATOM   46   C CD1 . PHE A 1 8   ? -17.745 28.175  -7.627  1.00 30.50 ? 8   PHE A CD1 1 
ATOM   47   C CD2 . PHE A 1 8   ? -18.375 28.824  -5.427  1.00 29.90 ? 8   PHE A CD2 1 
ATOM   48   C CE1 . PHE A 1 8   ? -16.793 27.329  -7.109  1.00 30.54 ? 8   PHE A CE1 1 
ATOM   49   C CE2 . PHE A 1 8   ? -17.421 27.972  -4.903  1.00 27.44 ? 8   PHE A CE2 1 
ATOM   50   C CZ  . PHE A 1 8   ? -16.631 27.221  -5.750  1.00 26.32 ? 8   PHE A CZ  1 
ATOM   51   N N   . THR A 1 9   ? -22.745 30.139  -9.076  1.00 40.91 ? 9   THR A N   1 
ATOM   52   C CA  . THR A 1 9   ? -23.738 31.180  -9.323  1.00 40.30 ? 9   THR A CA  1 
ATOM   53   C C   . THR A 1 9   ? -24.862 31.171  -8.296  1.00 40.92 ? 9   THR A C   1 
ATOM   54   O O   . THR A 1 9   ? -25.550 32.189  -8.136  1.00 42.49 ? 9   THR A O   1 
ATOM   55   C CB  . THR A 1 9   ? -24.330 31.044  -10.727 1.00 42.91 ? 9   THR A CB  1 
ATOM   56   O OG1 . THR A 1 9   ? -24.970 29.764  -10.862 1.00 41.49 ? 9   THR A OG1 1 
ATOM   57   C CG2 . THR A 1 9   ? -23.243 31.208  -11.777 1.00 43.99 ? 9   THR A CG2 1 
ATOM   58   N N   . GLY A 1 10  ? -25.056 30.065  -7.590  1.00 38.07 ? 10  GLY A N   1 
ATOM   59   C CA  . GLY A 1 10  ? -26.102 30.009  -6.595  1.00 40.19 ? 10  GLY A CA  1 
ATOM   60   C C   . GLY A 1 10  ? -25.595 29.791  -5.186  1.00 40.92 ? 10  GLY A C   1 
ATOM   61   O O   . GLY A 1 10  ? -24.400 29.944  -4.905  1.00 35.07 ? 10  GLY A O   1 
ATOM   62   N N   . VAL A 1 11  ? -26.515 29.454  -4.289  1.00 36.84 ? 11  VAL A N   1 
ATOM   63   C CA  . VAL A 1 11  ? -26.179 29.158  -2.903  1.00 37.71 ? 11  VAL A CA  1 
ATOM   64   C C   . VAL A 1 11  ? -25.609 27.748  -2.855  1.00 37.01 ? 11  VAL A C   1 
ATOM   65   O O   . VAL A 1 11  ? -26.203 26.813  -3.404  1.00 37.09 ? 11  VAL A O   1 
ATOM   66   C CB  . VAL A 1 11  ? -27.423 29.286  -2.011  1.00 39.44 ? 11  VAL A CB  1 
ATOM   67   C CG1 . VAL A 1 11  ? -27.251 28.490  -0.728  1.00 38.85 ? 11  VAL A CG1 1 
ATOM   68   C CG2 . VAL A 1 11  ? -27.744 30.742  -1.736  1.00 40.36 ? 11  VAL A CG2 1 
ATOM   69   N N   . VAL A 1 12  ? -24.455 27.588  -2.216  1.00 31.68 ? 12  VAL A N   1 
ATOM   70   C CA  . VAL A 1 12  ? -23.736 26.322  -2.200  1.00 29.72 ? 12  VAL A CA  1 
ATOM   71   C C   . VAL A 1 12  ? -23.607 25.863  -0.752  1.00 29.84 ? 12  VAL A C   1 
ATOM   72   O O   . VAL A 1 12  ? -23.050 26.586  0.078   1.00 28.63 ? 12  VAL A O   1 
ATOM   73   C CB  . VAL A 1 12  ? -22.352 26.434  -2.864  1.00 30.68 ? 12  VAL A CB  1 
ATOM   74   C CG1 . VAL A 1 12  ? -21.642 25.089  -2.872  1.00 30.71 ? 12  VAL A CG1 1 
ATOM   75   C CG2 . VAL A 1 12  ? -22.493 26.975  -4.279  1.00 32.11 ? 12  VAL A CG2 1 
ATOM   76   N N   . PRO A 1 13  ? -24.111 24.685  -0.397  1.00 30.29 ? 13  PRO A N   1 
ATOM   77   C CA  . PRO A 1 13  ? -23.855 24.155  0.949   1.00 27.91 ? 13  PRO A CA  1 
ATOM   78   C C   . PRO A 1 13  ? -22.372 23.894  1.156   1.00 27.81 ? 13  PRO A C   1 
ATOM   79   O O   . PRO A 1 13  ? -21.652 23.500  0.235   1.00 24.44 ? 13  PRO A O   1 
ATOM   80   C CB  . PRO A 1 13  ? -24.663 22.852  0.997   1.00 32.28 ? 13  PRO A CB  1 
ATOM   81   C CG  . PRO A 1 13  ? -25.177 22.614  -0.383  1.00 30.92 ? 13  PRO A CG  1 
ATOM   82   C CD  . PRO A 1 13  ? -24.732 23.703  -1.298  1.00 28.55 ? 13  PRO A CD  1 
ATOM   83   N N   . ILE A 1 14  ? -21.919 24.129  2.387   1.00 27.27 ? 14  ILE A N   1 
ATOM   84   C CA  . ILE A 1 14  ? -20.520 23.967  2.760   1.00 23.83 ? 14  ILE A CA  1 
ATOM   85   C C   . ILE A 1 14  ? -20.428 22.955  3.890   1.00 21.16 ? 14  ILE A C   1 
ATOM   86   O O   . ILE A 1 14  ? -21.221 22.986  4.840   1.00 23.92 ? 14  ILE A O   1 
ATOM   87   C CB  . ILE A 1 14  ? -19.880 25.311  3.175   1.00 22.02 ? 14  ILE A CB  1 
ATOM   88   C CG1 . ILE A 1 14  ? -19.900 26.301  2.004   1.00 26.12 ? 14  ILE A CG1 1 
ATOM   89   C CG2 . ILE A 1 14  ? -18.476 25.107  3.693   1.00 22.55 ? 14  ILE A CG2 1 
ATOM   90   C CD1 . ILE A 1 14  ? -19.664 27.746  2.421   1.00 23.02 ? 14  ILE A CD1 1 
ATOM   91   N N   . LEU A 1 15  ? -19.463 22.052  3.782   1.00 22.83 ? 15  LEU A N   1 
ATOM   92   C CA  . LEU A 1 15  ? -19.117 21.158  4.878   1.00 24.54 ? 15  LEU A CA  1 
ATOM   93   C C   . LEU A 1 15  ? -17.655 21.393  5.232   1.00 21.79 ? 15  LEU A C   1 
ATOM   94   O O   . LEU A 1 15  ? -16.801 21.426  4.347   1.00 22.57 ? 15  LEU A O   1 
ATOM   95   C CB  . LEU A 1 15  ? -19.364 19.691  4.493   1.00 26.11 ? 15  LEU A CB  1 
ATOM   96   C CG  . LEU A 1 15  ? -18.917 18.588  5.459   1.00 31.63 ? 15  LEU A CG  1 
ATOM   97   C CD1 . LEU A 1 15  ? -19.664 18.672  6.784   1.00 28.97 ? 15  LEU A CD1 1 
ATOM   98   C CD2 . LEU A 1 15  ? -19.114 17.219  4.821   1.00 32.33 ? 15  LEU A CD2 1 
ATOM   99   N N   . VAL A 1 16  ? -17.362 21.548  6.523   1.00 24.27 ? 16  VAL A N   1 
ATOM   100  C CA  . VAL A 1 16  ? -15.991 21.717  6.993   1.00 21.12 ? 16  VAL A CA  1 
ATOM   101  C C   . VAL A 1 16  ? -15.697 20.641  8.027   1.00 23.75 ? 16  VAL A C   1 
ATOM   102  O O   . VAL A 1 16  ? -16.503 20.412  8.936   1.00 25.66 ? 16  VAL A O   1 
ATOM   103  C CB  . VAL A 1 16  ? -15.753 23.119  7.586   1.00 23.10 ? 16  VAL A CB  1 
ATOM   104  C CG1 . VAL A 1 16  ? -14.285 23.288  7.983   1.00 20.63 ? 16  VAL A CG1 1 
ATOM   105  C CG2 . VAL A 1 16  ? -16.141 24.174  6.567   1.00 19.00 ? 16  VAL A CG2 1 
ATOM   106  N N   . GLU A 1 17  ? -14.549 19.984  7.883   1.00 21.33 ? 17  GLU A N   1 
ATOM   107  C CA  . GLU A 1 17  ? -14.113 18.953  8.815   1.00 23.52 ? 17  GLU A CA  1 
ATOM   108  C C   . GLU A 1 17  ? -12.653 19.209  9.143   1.00 22.47 ? 17  GLU A C   1 
ATOM   109  O O   . GLU A 1 17  ? -11.819 19.263  8.237   1.00 21.77 ? 17  GLU A O   1 
ATOM   110  C CB  . GLU A 1 17  ? -14.241 17.558  8.208   1.00 26.03 ? 17  GLU A CB  1 
ATOM   111  C CG  . GLU A 1 17  ? -15.658 17.056  7.994   1.00 30.72 ? 17  GLU A CG  1 
ATOM   112  C CD  . GLU A 1 17  ? -16.481 17.004  9.260   1.00 31.90 ? 17  GLU A CD  1 
ATOM   113  O OE1 . GLU A 1 17  ? -15.905 16.784  10.352  1.00 37.83 ? 17  GLU A OE1 1 
ATOM   114  O OE2 . GLU A 1 17  ? -17.717 17.158  9.147   1.00 38.02 ? 17  GLU A OE2 1 
ATOM   115  N N   . LEU A 1 18  ? -12.334 19.341  10.426  1.00 21.53 ? 18  LEU A N   1 
ATOM   116  C CA  . LEU A 1 18  ? -10.965 19.584  10.858  1.00 20.33 ? 18  LEU A CA  1 
ATOM   117  C C   . LEU A 1 18  ? -10.570 18.520  11.867  1.00 20.46 ? 18  LEU A C   1 
ATOM   118  O O   . LEU A 1 18  ? -11.308 18.272  12.822  1.00 21.59 ? 18  LEU A O   1 
ATOM   119  C CB  . LEU A 1 18  ? -10.806 20.964  11.501  1.00 19.95 ? 18  LEU A CB  1 
ATOM   120  C CG  . LEU A 1 18  ? -9.380  21.285  11.981  1.00 20.49 ? 18  LEU A CG  1 
ATOM   121  C CD1 . LEU A 1 18  ? -9.066  22.743  11.734  1.00 20.31 ? 18  LEU A CD1 1 
ATOM   122  C CD2 . LEU A 1 18  ? -9.142  20.906  13.433  1.00 19.59 ? 18  LEU A CD2 1 
ATOM   123  N N   . ASP A 1 19  ? -9.395  17.926  11.663  1.00 21.35 ? 19  ASP A N   1 
ATOM   124  C CA  . ASP A 1 19  ? -8.750  17.018  12.608  1.00 24.51 ? 19  ASP A CA  1 
ATOM   125  C C   . ASP A 1 19  ? -7.483  17.692  13.129  1.00 20.91 ? 19  ASP A C   1 
ATOM   126  O O   . ASP A 1 19  ? -6.574  17.999  12.353  1.00 20.24 ? 19  ASP A O   1 
ATOM   127  C CB  . ASP A 1 19  ? -8.417  15.684  11.934  1.00 26.50 ? 19  ASP A CB  1 
ATOM   128  C CG  . ASP A 1 19  ? -7.660  14.749  12.844  1.00 33.07 ? 19  ASP A CG  1 
ATOM   129  O OD1 . ASP A 1 19  ? -8.109  14.572  13.992  1.00 36.51 ? 19  ASP A OD1 1 
ATOM   130  O OD2 . ASP A 1 19  ? -6.606  14.206  12.431  1.00 42.01 ? 19  ASP A OD2 1 
ATOM   131  N N   . GLY A 1 20  ? -7.400  17.875  14.440  1.00 22.23 ? 20  GLY A N   1 
ATOM   132  C CA  . GLY A 1 20  ? -6.371  18.712  15.021  1.00 20.99 ? 20  GLY A CA  1 
ATOM   133  C C   . GLY A 1 20  ? -5.639  18.046  16.167  1.00 23.59 ? 20  GLY A C   1 
ATOM   134  O O   . GLY A 1 20  ? -6.168  17.179  16.858  1.00 21.54 ? 20  GLY A O   1 
ATOM   135  N N   . ASP A 1 21  ? -4.390  18.462  16.341  1.00 17.63 ? 21  ASP A N   1 
ATOM   136  C CA  . ASP A 1 21  ? -3.554  18.092  17.475  1.00 21.21 ? 21  ASP A CA  1 
ATOM   137  C C   . ASP A 1 21  ? -2.736  19.332  17.785  1.00 20.13 ? 21  ASP A C   1 
ATOM   138  O O   . ASP A 1 21  ? -1.853  19.682  17.002  1.00 21.82 ? 21  ASP A O   1 
ATOM   139  C CB  . ASP A 1 21  ? -2.613  16.942  17.139  1.00 24.28 ? 21  ASP A CB  1 
ATOM   140  C CG  . ASP A 1 21  ? -1.815  16.464  18.340  1.00 23.49 ? 21  ASP A CG  1 
ATOM   141  O OD1 . ASP A 1 21  ? -1.671  17.208  19.320  1.00 25.67 ? 21  ASP A OD1 1 
ATOM   142  O OD2 . ASP A 1 21  ? -1.135  15.440  18.217  1.00 27.85 ? 21  ASP A OD2 1 
ATOM   143  N N   . VAL A 1 22  ? -3.008  19.984  18.909  1.00 20.07 ? 22  VAL A N   1 
ATOM   144  C CA  . VAL A 1 22  ? -2.207  21.109  19.373  1.00 18.18 ? 22  VAL A CA  1 
ATOM   145  C C   . VAL A 1 22  ? -1.605  20.713  20.713  1.00 21.67 ? 22  VAL A C   1 
ATOM   146  O O   . VAL A 1 22  ? -2.332  20.523  21.693  1.00 19.20 ? 22  VAL A O   1 
ATOM   147  C CB  . VAL A 1 22  ? -3.030  22.400  19.496  1.00 21.87 ? 22  VAL A CB  1 
ATOM   148  C CG1 . VAL A 1 22  ? -2.169  23.513  20.047  1.00 16.99 ? 22  VAL A CG1 1 
ATOM   149  C CG2 . VAL A 1 22  ? -3.598  22.812  18.114  1.00 17.43 ? 22  VAL A CG2 1 
ATOM   150  N N   . ASN A 1 23  ? -0.277  20.617  20.768  1.00 20.62 ? 23  ASN A N   1 
ATOM   151  C CA  . ASN A 1 23  ? 0.404   20.230  22.006  1.00 22.32 ? 23  ASN A CA  1 
ATOM   152  C C   . ASN A 1 23  ? -0.194  18.951  22.595  1.00 25.76 ? 23  ASN A C   1 
ATOM   153  O O   . ASN A 1 23  ? -0.336  18.809  23.812  1.00 25.92 ? 23  ASN A O   1 
ATOM   154  C CB  . ASN A 1 23  ? 0.355   21.346  23.056  1.00 21.78 ? 23  ASN A CB  1 
ATOM   155  C CG  . ASN A 1 23  ? 1.514   22.338  22.948  1.00 24.03 ? 23  ASN A CG  1 
ATOM   156  O OD1 . ASN A 1 23  ? 2.131   22.499  21.898  1.00 22.91 ? 23  ASN A OD1 1 
ATOM   157  N ND2 . ASN A 1 23  ? 1.864   22.943  24.076  1.00 23.65 ? 23  ASN A ND2 1 
ATOM   158  N N   . GLY A 1 24  ? -0.559  18.005  21.737  1.00 22.14 ? 24  GLY A N   1 
ATOM   159  C CA  . GLY A 1 24  ? -1.107  16.759  22.227  1.00 26.38 ? 24  GLY A CA  1 
ATOM   160  C C   . GLY A 1 24  ? -2.580  16.787  22.546  1.00 27.00 ? 24  GLY A C   1 
ATOM   161  O O   . GLY A 1 24  ? -3.162  15.719  22.792  1.00 27.44 ? 24  GLY A O   1 
ATOM   162  N N   . HIS A 1 25  ? -3.215  17.959  22.555  1.00 23.92 ? 25  HIS A N   1 
ATOM   163  C CA  . HIS A 1 25  ? -4.662  18.024  22.713  1.00 24.89 ? 25  HIS A CA  1 
ATOM   164  C C   . HIS A 1 25  ? -5.270  17.694  21.356  1.00 27.46 ? 25  HIS A C   1 
ATOM   165  O O   . HIS A 1 25  ? -5.202  18.511  20.433  1.00 22.92 ? 25  HIS A O   1 
ATOM   166  C CB  . HIS A 1 25  ? -5.102  19.411  23.175  1.00 25.24 ? 25  HIS A CB  1 
ATOM   167  C CG  . HIS A 1 25  ? -4.609  19.782  24.540  1.00 29.38 ? 25  HIS A CG  1 
ATOM   168  N ND1 . HIS A 1 25  ? -5.326  19.530  25.689  1.00 31.35 ? 25  HIS A ND1 1 
ATOM   169  C CD2 . HIS A 1 25  ? -3.478  20.414  24.933  1.00 31.88 ? 25  HIS A CD2 1 
ATOM   170  C CE1 . HIS A 1 25  ? -4.643  19.962  26.735  1.00 33.65 ? 25  HIS A CE1 1 
ATOM   171  N NE2 . HIS A 1 25  ? -3.521  20.511  26.303  1.00 35.33 ? 25  HIS A NE2 1 
ATOM   172  N N   . LYS A 1 26  ? -5.845  16.499  21.213  1.00 24.77 ? 26  LYS A N   1 
ATOM   173  C CA  . LYS A 1 26  ? -6.447  16.101  19.950  1.00 23.37 ? 26  LYS A CA  1 
ATOM   174  C C   . LYS A 1 26  ? -7.921  16.469  19.946  1.00 27.08 ? 26  LYS A C   1 
ATOM   175  O O   . LYS A 1 26  ? -8.650  16.189  20.903  1.00 27.50 ? 26  LYS A O   1 
ATOM   176  C CB  . LYS A 1 26  ? -6.261  14.607  19.680  1.00 28.13 ? 26  LYS A CB  1 
ATOM   177  C CG  . LYS A 1 26  ? -4.861  14.103  19.986  1.00 32.76 ? 26  LYS A CG  1 
ATOM   178  C CD  . LYS A 1 26  ? -4.297  13.315  18.824  1.00 35.49 ? 26  LYS A CD  1 
ATOM   179  C CE  . LYS A 1 26  ? -2.898  12.784  19.137  1.00 38.59 ? 26  LYS A CE  1 
ATOM   180  N NZ  . LYS A 1 26  ? -2.612  11.545  18.359  1.00 43.28 ? 26  LYS A NZ  1 
ATOM   181  N N   . PHE A 1 27  ? -8.355  17.103  18.866  1.00 20.91 ? 27  PHE A N   1 
ATOM   182  C CA  . PHE A 1 27  ? -9.702  17.628  18.803  1.00 22.72 ? 27  PHE A CA  1 
ATOM   183  C C   . PHE A 1 27  ? -10.186 17.541  17.366  1.00 24.85 ? 27  PHE A C   1 
ATOM   184  O O   . PHE A 1 27  ? -9.403  17.320  16.435  1.00 23.41 ? 27  PHE A O   1 
ATOM   185  C CB  . PHE A 1 27  ? -9.761  19.066  19.341  1.00 25.53 ? 27  PHE A CB  1 
ATOM   186  C CG  . PHE A 1 27  ? -9.033  20.067  18.489  1.00 24.49 ? 27  PHE A CG  1 
ATOM   187  C CD1 . PHE A 1 27  ? -7.664  20.229  18.608  1.00 23.59 ? 27  PHE A CD1 1 
ATOM   188  C CD2 . PHE A 1 27  ? -9.723  20.853  17.578  1.00 23.87 ? 27  PHE A CD2 1 
ATOM   189  C CE1 . PHE A 1 27  ? -6.994  21.155  17.820  1.00 24.99 ? 27  PHE A CE1 1 
ATOM   190  C CE2 . PHE A 1 27  ? -9.061  21.773  16.795  1.00 21.37 ? 27  PHE A CE2 1 
ATOM   191  C CZ  . PHE A 1 27  ? -7.701  21.924  16.913  1.00 21.72 ? 27  PHE A CZ  1 
ATOM   192  N N   . SER A 1 28  ? -11.496 17.688  17.209  1.00 26.18 ? 28  SER A N   1 
ATOM   193  C CA  . SER A 1 28  ? -12.154 17.603  15.917  1.00 25.10 ? 28  SER A CA  1 
ATOM   194  C C   . SER A 1 28  ? -13.199 18.704  15.854  1.00 24.15 ? 28  SER A C   1 
ATOM   195  O O   . SER A 1 28  ? -13.897 18.970  16.836  1.00 25.23 ? 28  SER A O   1 
ATOM   196  C CB  . SER A 1 28  ? -12.802 16.224  15.712  1.00 24.48 ? 28  SER A CB  1 
ATOM   197  O OG  . SER A 1 28  ? -11.815 15.276  15.334  1.00 27.83 ? 28  SER A OG  1 
ATOM   198  N N   . VAL A 1 29  ? -13.276 19.366  14.707  1.00 22.01 ? 29  VAL A N   1 
ATOM   199  C CA  . VAL A 1 29  ? -14.263 20.404  14.450  1.00 20.07 ? 29  VAL A CA  1 
ATOM   200  C C   . VAL A 1 29  ? -15.017 20.005  13.197  1.00 24.02 ? 29  VAL A C   1 
ATOM   201  O O   . VAL A 1 29  ? -14.399 19.607  12.204  1.00 21.25 ? 29  VAL A O   1 
ATOM   202  C CB  . VAL A 1 29  ? -13.603 21.783  14.266  1.00 19.80 ? 29  VAL A CB  1 
ATOM   203  C CG1 . VAL A 1 29  ? -14.646 22.839  13.794  1.00 19.01 ? 29  VAL A CG1 1 
ATOM   204  C CG2 . VAL A 1 29  ? -12.891 22.205  15.553  1.00 20.74 ? 29  VAL A CG2 1 
ATOM   205  N N   . SER A 1 30  ? -16.348 20.090  13.249  1.00 26.01 ? 30  SER A N   1 
ATOM   206  C CA  . SER A 1 30  ? -17.174 19.948  12.065  1.00 23.62 ? 30  SER A CA  1 
ATOM   207  C C   . SER A 1 30  ? -17.978 21.227  11.899  1.00 23.47 ? 30  SER A C   1 
ATOM   208  O O   . SER A 1 30  ? -18.431 21.830  12.880  1.00 24.20 ? 30  SER A O   1 
ATOM   209  C CB  . SER A 1 30  ? -18.123 18.761  12.158  1.00 30.73 ? 30  SER A CB  1 
ATOM   210  O OG  . SER A 1 30  ? -19.010 18.964  13.232  1.00 33.04 ? 30  SER A OG  1 
ATOM   211  N N   . GLY A 1 31  ? -18.122 21.658  10.663  1.00 24.73 ? 31  GLY A N   1 
ATOM   212  C CA  . GLY A 1 31  ? -18.830 22.887  10.383  1.00 22.44 ? 31  GLY A CA  1 
ATOM   213  C C   . GLY A 1 31  ? -19.762 22.678  9.217   1.00 22.78 ? 31  GLY A C   1 
ATOM   214  O O   . GLY A 1 31  ? -19.469 21.928  8.284   1.00 25.18 ? 31  GLY A O   1 
ATOM   215  N N   . GLU A 1 32  ? -20.899 23.353  9.280   1.00 26.55 ? 32  GLU A N   1 
ATOM   216  C CA  . GLU A 1 32  ? -21.812 23.342  8.154   1.00 26.96 ? 32  GLU A CA  1 
ATOM   217  C C   . GLU A 1 32  ? -22.416 24.721  7.974   1.00 26.83 ? 32  GLU A C   1 
ATOM   218  O O   . GLU A 1 32  ? -22.532 25.506  8.920   1.00 25.63 ? 32  GLU A O   1 
ATOM   219  C CB  . GLU A 1 32  ? -22.900 22.273  8.321   1.00 31.06 ? 32  GLU A CB  1 
ATOM   220  C CG  . GLU A 1 32  ? -23.600 22.270  9.651   1.00 35.41 ? 32  GLU A CG  1 
ATOM   221  C CD  . GLU A 1 32  ? -24.579 21.103  9.765   1.00 49.30 ? 32  GLU A CD  1 
ATOM   222  O OE1 . GLU A 1 32  ? -24.152 19.945  9.524   1.00 48.96 ? 32  GLU A OE1 1 
ATOM   223  O OE2 . GLU A 1 32  ? -25.763 21.342  10.095  1.00 49.66 ? 32  GLU A OE2 1 
ATOM   224  N N   . GLY A 1 33  ? -22.794 25.000  6.735   1.00 25.78 ? 33  GLY A N   1 
ATOM   225  C CA  . GLY A 1 33  ? -23.413 26.266  6.393   1.00 27.30 ? 33  GLY A CA  1 
ATOM   226  C C   . GLY A 1 33  ? -23.596 26.354  4.900   1.00 25.83 ? 33  GLY A C   1 
ATOM   227  O O   . GLY A 1 33  ? -23.746 25.333  4.214   1.00 27.81 ? 33  GLY A O   1 
ATOM   228  N N   . GLU A 1 34  ? -23.556 27.576  4.396   1.00 26.53 ? 34  GLU A N   1 
ATOM   229  C CA  . GLU A 1 34  ? -23.681 27.758  2.964   1.00 27.99 ? 34  GLU A CA  1 
ATOM   230  C C   . GLU A 1 34  ? -22.882 28.979  2.566   1.00 28.04 ? 34  GLU A C   1 
ATOM   231  O O   . GLU A 1 34  ? -22.580 29.841  3.395   1.00 27.81 ? 34  GLU A O   1 
ATOM   232  C CB  . GLU A 1 34  ? -25.137 27.932  2.543   1.00 31.85 ? 34  GLU A CB  1 
ATOM   233  C CG  . GLU A 1 34  ? -25.952 28.734  3.524   1.00 36.03 ? 34  GLU A CG  1 
ATOM   234  C CD  . GLU A 1 34  ? -27.416 28.793  3.130   1.00 46.27 ? 34  GLU A CD  1 
ATOM   235  O OE1 . GLU A 1 34  ? -27.869 27.861  2.429   1.00 46.23 ? 34  GLU A OE1 1 
ATOM   236  O OE2 . GLU A 1 34  ? -28.108 29.767  3.516   1.00 50.46 ? 34  GLU A OE2 1 
ATOM   237  N N   . GLY A 1 35  ? -22.550 29.044  1.285   1.00 25.98 ? 35  GLY A N   1 
ATOM   238  C CA  . GLY A 1 35  ? -21.899 30.211  0.729   1.00 26.37 ? 35  GLY A CA  1 
ATOM   239  C C   . GLY A 1 35  ? -22.588 30.671  -0.536  1.00 30.07 ? 35  GLY A C   1 
ATOM   240  O O   . GLY A 1 35  ? -23.193 29.881  -1.267  1.00 31.80 ? 35  GLY A O   1 
ATOM   241  N N   . ASP A 1 36  ? -22.500 31.979  -0.782  1.00 30.02 ? 36  ASP A N   1 
ATOM   242  C CA  . ASP A 1 36  ? -23.015 32.587  -2.014  1.00 32.30 ? 36  ASP A CA  1 
ATOM   243  C C   . ASP A 1 36  ? -21.969 33.567  -2.539  1.00 30.64 ? 36  ASP A C   1 
ATOM   244  O O   . ASP A 1 36  ? -21.858 34.698  -2.052  1.00 30.61 ? 36  ASP A O   1 
ATOM   245  C CB  . ASP A 1 36  ? -24.360 33.261  -1.779  1.00 36.99 ? 36  ASP A CB  1 
ATOM   246  C CG  . ASP A 1 36  ? -25.221 33.316  -3.043  1.00 41.89 ? 36  ASP A CG  1 
ATOM   247  O OD1 . ASP A 1 36  ? -24.676 33.234  -4.172  1.00 40.98 ? 36  ASP A OD1 1 
ATOM   248  O OD2 . ASP A 1 36  ? -26.456 33.403  -2.900  1.00 45.45 ? 36  ASP A OD2 1 
ATOM   249  N N   . ALA A 1 37  ? -21.204 33.119  -3.537  1.00 28.53 ? 37  ALA A N   1 
ATOM   250  C CA  . ALA A 1 37  ? -20.123 33.923  -4.086  1.00 26.77 ? 37  ALA A CA  1 
ATOM   251  C C   . ALA A 1 37  ? -20.632 35.165  -4.801  1.00 32.24 ? 37  ALA A C   1 
ATOM   252  O O   . ALA A 1 37  ? -19.877 36.131  -4.956  1.00 31.58 ? 37  ALA A O   1 
ATOM   253  C CB  . ALA A 1 37  ? -19.281 33.069  -5.036  1.00 30.38 ? 37  ALA A CB  1 
ATOM   254  N N   . THR A 1 38  ? -21.891 35.157  -5.239  1.00 34.12 ? 38  THR A N   1 
ATOM   255  C CA  . THR A 1 38  ? -22.466 36.343  -5.865  1.00 36.69 ? 38  THR A CA  1 
ATOM   256  C C   . THR A 1 38  ? -22.387 37.536  -4.924  1.00 32.54 ? 38  THR A C   1 
ATOM   257  O O   . THR A 1 38  ? -22.125 38.666  -5.352  1.00 33.98 ? 38  THR A O   1 
ATOM   258  C CB  . THR A 1 38  ? -23.913 36.056  -6.266  1.00 37.77 ? 38  THR A CB  1 
ATOM   259  O OG1 . THR A 1 38  ? -23.927 35.080  -7.320  1.00 43.92 ? 38  THR A OG1 1 
ATOM   260  C CG2 . THR A 1 38  ? -24.609 37.334  -6.739  1.00 38.60 ? 38  THR A CG2 1 
ATOM   261  N N   . TYR A 1 39  ? -22.542 37.279  -3.628  1.00 34.82 ? 39  TYR A N   1 
ATOM   262  C CA  . TYR A 1 39  ? -22.480 38.273  -2.571  1.00 33.05 ? 39  TYR A CA  1 
ATOM   263  C C   . TYR A 1 39  ? -21.190 38.191  -1.770  1.00 33.93 ? 39  TYR A C   1 
ATOM   264  O O   . TYR A 1 39  ? -20.989 39.005  -0.865  1.00 33.91 ? 39  TYR A O   1 
ATOM   265  C CB  . TYR A 1 39  ? -23.665 38.080  -1.614  1.00 37.49 ? 39  TYR A CB  1 
ATOM   266  C CG  . TYR A 1 39  ? -24.980 37.800  -2.310  1.00 41.41 ? 39  TYR A CG  1 
ATOM   267  C CD1 . TYR A 1 39  ? -25.609 38.767  -3.075  1.00 40.72 ? 39  TYR A CD1 1 
ATOM   268  C CD2 . TYR A 1 39  ? -25.577 36.549  -2.221  1.00 44.11 ? 39  TYR A CD2 1 
ATOM   269  C CE1 . TYR A 1 39  ? -26.810 38.506  -3.718  1.00 48.62 ? 39  TYR A CE1 1 
ATOM   270  C CE2 . TYR A 1 39  ? -26.776 36.278  -2.860  1.00 46.84 ? 39  TYR A CE2 1 
ATOM   271  C CZ  . TYR A 1 39  ? -27.388 37.255  -3.610  1.00 48.18 ? 39  TYR A CZ  1 
ATOM   272  O OH  . TYR A 1 39  ? -28.578 36.978  -4.245  1.00 49.74 ? 39  TYR A OH  1 
ATOM   273  N N   . GLY A 1 40  ? -20.333 37.209  -2.053  1.00 31.43 ? 40  GLY A N   1 
ATOM   274  C CA  . GLY A 1 40  ? -19.185 36.941  -1.201  1.00 27.31 ? 40  GLY A CA  1 
ATOM   275  C C   . GLY A 1 40  ? -19.548 36.565  0.218   1.00 29.26 ? 40  GLY A C   1 
ATOM   276  O O   . GLY A 1 40  ? -18.777 36.844  1.141   1.00 32.38 ? 40  GLY A O   1 
ATOM   277  N N   . LYS A 1 41  ? -20.686 35.903  0.421   1.00 26.46 ? 41  LYS A N   1 
ATOM   278  C CA  . LYS A 1 41  ? -21.271 35.736  1.745   1.00 28.96 ? 41  LYS A CA  1 
ATOM   279  C C   . LYS A 1 41  ? -21.144 34.292  2.214   1.00 27.33 ? 41  LYS A C   1 
ATOM   280  O O   . LYS A 1 41  ? -21.410 33.355  1.454   1.00 24.26 ? 41  LYS A O   1 
ATOM   281  C CB  . LYS A 1 41  ? -22.744 36.156  1.723   1.00 26.92 ? 41  LYS A CB  1 
ATOM   282  C CG  . LYS A 1 41  ? -23.599 35.711  2.888   1.00 29.92 ? 41  LYS A CG  1 
ATOM   283  C CD  . LYS A 1 41  ? -24.705 36.744  3.152   1.00 30.09 ? 41  LYS A CD  1 
ATOM   284  C CE  . LYS A 1 41  ? -25.776 36.190  4.079   1.00 33.72 ? 41  LYS A CE  1 
ATOM   285  N NZ  . LYS A 1 41  ? -26.721 37.223  4.618   1.00 36.65 ? 41  LYS A NZ  1 
ATOM   286  N N   . LEU A 1 42  ? -20.757 34.126  3.482   1.00 25.10 ? 42  LEU A N   1 
ATOM   287  C CA  . LEU A 1 42  ? -20.580 32.830  4.124   1.00 27.83 ? 42  LEU A CA  1 
ATOM   288  C C   . LEU A 1 42  ? -21.289 32.856  5.466   1.00 25.16 ? 42  LEU A C   1 
ATOM   289  O O   . LEU A 1 42  ? -21.099 33.796  6.239   1.00 25.90 ? 42  LEU A O   1 
ATOM   290  C CB  . LEU A 1 42  ? -19.090 32.527  4.368   1.00 29.36 ? 42  LEU A CB  1 
ATOM   291  C CG  . LEU A 1 42  ? -18.162 32.335  3.182   1.00 31.88 ? 42  LEU A CG  1 
ATOM   292  C CD1 . LEU A 1 42  ? -16.721 32.202  3.653   1.00 32.83 ? 42  LEU A CD1 1 
ATOM   293  C CD2 . LEU A 1 42  ? -18.599 31.104  2.446   1.00 29.87 ? 42  LEU A CD2 1 
ATOM   294  N N   . THR A 1 43  ? -22.073 31.820  5.761   1.00 26.56 ? 43  THR A N   1 
ATOM   295  C CA  . THR A 1 43  ? -22.595 31.615  7.110   1.00 30.08 ? 43  THR A CA  1 
ATOM   296  C C   . THR A 1 43  ? -22.343 30.174  7.506   1.00 26.92 ? 43  THR A C   1 
ATOM   297  O O   . THR A 1 43  ? -22.659 29.255  6.744   1.00 27.57 ? 43  THR A O   1 
ATOM   298  C CB  . THR A 1 43  ? -24.095 31.951  7.211   1.00 30.25 ? 43  THR A CB  1 
ATOM   299  O OG1 . THR A 1 43  ? -24.864 30.933  6.557   1.00 38.14 ? 43  THR A OG1 1 
ATOM   300  C CG2 . THR A 1 43  ? -24.389 33.266  6.558   1.00 25.47 ? 43  THR A CG2 1 
ATOM   301  N N   . LEU A 1 44  ? -21.793 29.971  8.702   1.00 22.49 ? 44  LEU A N   1 
ATOM   302  C CA  . LEU A 1 44  ? -21.278 28.671  9.082   1.00 23.77 ? 44  LEU A CA  1 
ATOM   303  C C   . LEU A 1 44  ? -21.355 28.510  10.594  1.00 26.77 ? 44  LEU A C   1 
ATOM   304  O O   . LEU A 1 44  ? -21.078 29.450  11.341  1.00 25.85 ? 44  LEU A O   1 
ATOM   305  C CB  . LEU A 1 44  ? -19.829 28.534  8.599   1.00 30.31 ? 44  LEU A CB  1 
ATOM   306  C CG  . LEU A 1 44  ? -19.666 28.217  7.106   1.00 30.12 ? 44  LEU A CG  1 
ATOM   307  C CD1 . LEU A 1 44  ? -18.377 28.780  6.594   1.00 28.76 ? 44  LEU A CD1 1 
ATOM   308  C CD2 . LEU A 1 44  ? -19.695 26.722  6.892   1.00 29.41 ? 44  LEU A CD2 1 
ATOM   309  N N   . LYS A 1 45  ? -21.736 27.316  11.031  1.00 24.07 ? 45  LYS A N   1 
ATOM   310  C CA  . LYS A 1 45  ? -21.728 26.917  12.433  1.00 24.81 ? 45  LYS A CA  1 
ATOM   311  C C   . LYS A 1 45  ? -20.689 25.827  12.627  1.00 22.04 ? 45  LYS A C   1 
ATOM   312  O O   . LYS A 1 45  ? -20.761 24.778  11.985  1.00 21.62 ? 45  LYS A O   1 
ATOM   313  C CB  . LYS A 1 45  ? -23.102 26.405  12.869  1.00 27.75 ? 45  LYS A CB  1 
ATOM   314  C CG  . LYS A 1 45  ? -23.369 26.493  14.362  1.00 31.07 ? 45  LYS A CG  1 
ATOM   315  C CD  . LYS A 1 45  ? -24.356 25.397  14.762  1.00 32.18 ? 45  LYS A CD  1 
ATOM   316  C CE  . LYS A 1 45  ? -24.484 25.273  16.267  1.00 33.13 ? 45  LYS A CE  1 
ATOM   317  N NZ  . LYS A 1 45  ? -25.890 24.903  16.636  1.00 36.02 ? 45  LYS A NZ  1 
ATOM   318  N N   . PHE A 1 46  ? -19.739 26.057  13.523  1.00 22.46 ? 46  PHE A N   1 
ATOM   319  C CA  . PHE A 1 46  ? -18.728 25.053  13.823  1.00 21.39 ? 46  PHE A CA  1 
ATOM   320  C C   . PHE A 1 46  ? -18.966 24.473  15.206  1.00 23.84 ? 46  PHE A C   1 
ATOM   321  O O   . PHE A 1 46  ? -19.337 25.197  16.134  1.00 23.21 ? 46  PHE A O   1 
ATOM   322  C CB  . PHE A 1 46  ? -17.329 25.656  13.738  1.00 24.70 ? 46  PHE A CB  1 
ATOM   323  C CG  . PHE A 1 46  ? -17.018 26.229  12.400  1.00 20.37 ? 46  PHE A CG  1 
ATOM   324  C CD1 . PHE A 1 46  ? -16.624 25.411  11.358  1.00 18.82 ? 46  PHE A CD1 1 
ATOM   325  C CD2 . PHE A 1 46  ? -17.202 27.570  12.163  1.00 20.12 ? 46  PHE A CD2 1 
ATOM   326  C CE1 . PHE A 1 46  ? -16.351 25.939  10.106  1.00 20.40 ? 46  PHE A CE1 1 
ATOM   327  C CE2 . PHE A 1 46  ? -16.941 28.109  10.911  1.00 20.56 ? 46  PHE A CE2 1 
ATOM   328  C CZ  . PHE A 1 46  ? -16.517 27.291  9.883   1.00 22.40 ? 46  PHE A CZ  1 
ATOM   329  N N   . ILE A 1 47  ? -18.717 23.170  15.335  1.00 21.58 ? 47  ILE A N   1 
ATOM   330  C CA  . ILE A 1 47  ? -18.912 22.424  16.571  1.00 26.27 ? 47  ILE A CA  1 
ATOM   331  C C   . ILE A 1 47  ? -17.603 21.733  16.897  1.00 24.25 ? 47  ILE A C   1 
ATOM   332  O O   . ILE A 1 47  ? -17.013 21.091  16.029  1.00 23.65 ? 47  ILE A O   1 
ATOM   333  C CB  . ILE A 1 47  ? -20.025 21.363  16.433  1.00 25.02 ? 47  ILE A CB  1 
ATOM   334  C CG1 . ILE A 1 47  ? -21.383 22.014  16.134  1.00 28.49 ? 47  ILE A CG1 1 
ATOM   335  C CG2 . ILE A 1 47  ? -20.125 20.533  17.709  1.00 28.18 ? 47  ILE A CG2 1 
ATOM   336  C CD1 . ILE A 1 47  ? -22.007 22.680  17.299  1.00 32.34 ? 47  ILE A CD1 1 
ATOM   337  N N   . CYS A 1 48  ? -17.154 21.838  18.144  1.00 25.29 ? 48  CYS A N   1 
ATOM   338  C CA  . CYS A 1 48  ? -16.085 20.951  18.593  1.00 24.34 ? 48  CYS A CA  1 
ATOM   339  C C   . CYS A 1 48  ? -16.712 19.636  19.039  1.00 27.07 ? 48  CYS A C   1 
ATOM   340  O O   . CYS A 1 48  ? -17.278 19.547  20.126  1.00 29.47 ? 48  CYS A O   1 
ATOM   341  C CB  . CYS A 1 48  ? -15.272 21.582  19.716  1.00 26.24 ? 48  CYS A CB  1 
ATOM   342  S SG  . CYS A 1 48  ? -13.904 20.493  20.202  1.00 26.46 ? 48  CYS A SG  1 
ATOM   343  N N   . THR A 1 49  ? -16.607 18.608  18.193  1.00 30.17 ? 49  THR A N   1 
ATOM   344  C CA  . THR A 1 49  ? -17.282 17.330  18.405  1.00 30.67 ? 49  THR A CA  1 
ATOM   345  C C   . THR A 1 49  ? -16.585 16.433  19.429  1.00 33.76 ? 49  THR A C   1 
ATOM   346  O O   . THR A 1 49  ? -17.130 15.380  19.781  1.00 35.24 ? 49  THR A O   1 
ATOM   347  C CB  . THR A 1 49  ? -17.405 16.588  17.072  1.00 29.92 ? 49  THR A CB  1 
ATOM   348  O OG1 . THR A 1 49  ? -16.109 16.191  16.621  1.00 28.39 ? 49  THR A OG1 1 
ATOM   349  C CG2 . THR A 1 49  ? -18.053 17.463  16.013  1.00 29.63 ? 49  THR A CG2 1 
ATOM   350  N N   . THR A 1 50  ? -15.416 16.819  19.924  1.00 28.07 ? 50  THR A N   1 
ATOM   351  C CA  . THR A 1 50  ? -14.666 16.021  20.880  1.00 31.51 ? 50  THR A CA  1 
ATOM   352  C C   . THR A 1 50  ? -14.720 16.588  22.294  1.00 31.72 ? 50  THR A C   1 
ATOM   353  O O   . THR A 1 50  ? -14.035 16.072  23.184  1.00 36.31 ? 50  THR A O   1 
ATOM   354  C CB  . THR A 1 50  ? -13.212 15.882  20.420  1.00 29.76 ? 50  THR A CB  1 
ATOM   355  O OG1 . THR A 1 50  ? -12.673 17.180  20.113  1.00 28.34 ? 50  THR A OG1 1 
ATOM   356  C CG2 . THR A 1 50  ? -13.126 14.979  19.189  1.00 26.41 ? 50  THR A CG2 1 
ATOM   357  N N   . GLY A 1 51  ? -15.514 17.634  22.526  1.00 30.82 ? 51  GLY A N   1 
ATOM   358  C CA  . GLY A 1 51  ? -15.608 18.262  23.829  1.00 30.56 ? 51  GLY A CA  1 
ATOM   359  C C   . GLY A 1 51  ? -15.270 19.741  23.748  1.00 31.25 ? 51  GLY A C   1 
ATOM   360  O O   . GLY A 1 51  ? -15.727 20.445  22.842  1.00 33.34 ? 51  GLY A O   1 
ATOM   361  N N   . LYS A 1 52  ? -14.478 20.208  24.709  1.00 30.64 ? 52  LYS A N   1 
ATOM   362  C CA  . LYS A 1 52  ? -14.097 21.612  24.749  1.00 30.18 ? 52  LYS A CA  1 
ATOM   363  C C   . LYS A 1 52  ? -12.948 21.853  23.775  1.00 30.35 ? 52  LYS A C   1 
ATOM   364  O O   . LYS A 1 52  ? -12.021 21.044  23.677  1.00 30.74 ? 52  LYS A O   1 
ATOM   365  C CB  . LYS A 1 52  ? -13.688 22.018  26.167  1.00 31.03 ? 52  LYS A CB  1 
ATOM   366  C CG  . LYS A 1 52  ? -13.630 23.529  26.401  1.00 36.25 ? 52  LYS A CG  1 
ATOM   367  C CD  . LYS A 1 52  ? -12.206 24.033  26.599  1.00 38.23 ? 52  LYS A CD  1 
ATOM   368  C CE  . LYS A 1 52  ? -12.200 25.484  27.045  1.00 36.12 ? 52  LYS A CE  1 
ATOM   369  N NZ  . LYS A 1 52  ? -13.285 26.268  26.354  1.00 46.69 ? 52  LYS A NZ  1 
ATOM   370  N N   . LEU A 1 53  ? -13.023 22.950  23.039  1.00 27.16 ? 53  LEU A N   1 
ATOM   371  C CA  . LEU A 1 53  ? -11.947 23.288  22.108  1.00 25.43 ? 53  LEU A CA  1 
ATOM   372  C C   . LEU A 1 53  ? -10.702 23.703  22.887  1.00 23.01 ? 53  LEU A C   1 
ATOM   373  O O   . LEU A 1 53  ? -10.778 24.624  23.706  1.00 24.17 ? 53  LEU A O   1 
ATOM   374  C CB  . LEU A 1 53  ? -12.387 24.427  21.186  1.00 24.32 ? 53  LEU A CB  1 
ATOM   375  C CG  . LEU A 1 53  ? -11.501 24.667  19.964  1.00 22.60 ? 53  LEU A CG  1 
ATOM   376  C CD1 . LEU A 1 53  ? -11.582 23.465  19.023  1.00 24.33 ? 53  LEU A CD1 1 
ATOM   377  C CD2 . LEU A 1 53  ? -11.880 25.947  19.252  1.00 22.63 ? 53  LEU A CD2 1 
ATOM   378  N N   . PRO A 1 54  ? -9.540  23.085  22.640  1.00 21.25 ? 54  PRO A N   1 
ATOM   379  C CA  . PRO A 1 54  ? -8.334  23.404  23.421  1.00 22.32 ? 54  PRO A CA  1 
ATOM   380  C C   . PRO A 1 54  ? -7.605  24.673  22.996  1.00 20.17 ? 54  PRO A C   1 
ATOM   381  O O   . PRO A 1 54  ? -6.603  25.022  23.626  1.00 23.97 ? 54  PRO A O   1 
ATOM   382  C CB  . PRO A 1 54  ? -7.441  22.177  23.197  1.00 23.21 ? 54  PRO A CB  1 
ATOM   383  C CG  . PRO A 1 54  ? -7.906  21.581  21.899  1.00 24.20 ? 54  PRO A CG  1 
ATOM   384  C CD  . PRO A 1 54  ? -9.343  21.954  21.717  1.00 22.05 ? 54  PRO A CD  1 
ATOM   385  N N   . VAL A 1 55  ? -8.063  25.373  21.963  1.00 19.35 ? 55  VAL A N   1 
ATOM   386  C CA  . VAL A 1 55  ? -7.476  26.644  21.541  1.00 19.26 ? 55  VAL A CA  1 
ATOM   387  C C   . VAL A 1 55  ? -8.639  27.613  21.416  1.00 21.14 ? 55  VAL A C   1 
ATOM   388  O O   . VAL A 1 55  ? -9.793  27.165  21.385  1.00 23.88 ? 55  VAL A O   1 
ATOM   389  C CB  . VAL A 1 55  ? -6.731  26.522  20.204  1.00 19.42 ? 55  VAL A CB  1 
ATOM   390  C CG1 . VAL A 1 55  ? -5.627  25.481  20.287  1.00 19.27 ? 55  VAL A CG1 1 
ATOM   391  C CG2 . VAL A 1 55  ? -7.723  26.164  19.108  1.00 18.13 ? 55  VAL A CG2 1 
ATOM   392  N N   . PRO A 1 56  ? -8.408  28.916  21.331  1.00 20.23 ? 56  PRO A N   1 
ATOM   393  C CA  . PRO A 1 56  ? -9.538  29.826  21.119  1.00 20.27 ? 56  PRO A CA  1 
ATOM   394  C C   . PRO A 1 56  ? -10.065 29.713  19.698  1.00 21.91 ? 56  PRO A C   1 
ATOM   395  O O   . PRO A 1 56  ? -9.302  29.578  18.732  1.00 20.48 ? 56  PRO A O   1 
ATOM   396  C CB  . PRO A 1 56  ? -8.954  31.221  21.396  1.00 19.99 ? 56  PRO A CB  1 
ATOM   397  C CG  . PRO A 1 56  ? -7.618  30.995  22.004  1.00 19.36 ? 56  PRO A CG  1 
ATOM   398  C CD  . PRO A 1 56  ? -7.149  29.647  21.546  1.00 22.00 ? 56  PRO A CD  1 
ATOM   399  N N   . TRP A 1 57  ? -11.389 29.767  19.589  1.00 21.00 ? 57  TRP A N   1 
ATOM   400  C CA  . TRP A 1 57  ? -12.045 29.760  18.285  1.00 21.74 ? 57  TRP A CA  1 
ATOM   401  C C   . TRP A 1 57  ? -11.472 30.765  17.284  1.00 19.41 ? 57  TRP A C   1 
ATOM   402  O O   . TRP A 1 57  ? -11.290 30.379  16.111  1.00 18.60 ? 57  TRP A O   1 
ATOM   403  C CB  . TRP A 1 57  ? -13.554 29.993  18.481  1.00 21.05 ? 57  TRP A CB  1 
ATOM   404  C CG  . TRP A 1 57  ? -14.284 28.776  18.946  1.00 25.07 ? 57  TRP A CG  1 
ATOM   405  C CD1 . TRP A 1 57  ? -14.784 28.529  20.201  1.00 22.04 ? 57  TRP A CD1 1 
ATOM   406  C CD2 . TRP A 1 57  ? -14.574 27.613  18.164  1.00 22.08 ? 57  TRP A CD2 1 
ATOM   407  N NE1 . TRP A 1 57  ? -15.369 27.289  20.238  1.00 22.30 ? 57  TRP A NE1 1 
ATOM   408  C CE2 . TRP A 1 57  ? -15.261 26.708  18.999  1.00 24.22 ? 57  TRP A CE2 1 
ATOM   409  C CE3 . TRP A 1 57  ? -14.322 27.253  16.837  1.00 21.71 ? 57  TRP A CE3 1 
ATOM   410  C CZ2 . TRP A 1 57  ? -15.702 25.470  18.546  1.00 24.08 ? 57  TRP A CZ2 1 
ATOM   411  C CZ3 . TRP A 1 57  ? -14.761 26.028  16.391  1.00 20.88 ? 57  TRP A CZ3 1 
ATOM   412  C CH2 . TRP A 1 57  ? -15.445 25.150  17.241  1.00 24.21 ? 57  TRP A CH2 1 
ATOM   413  N N   . PRO A 1 58  ? -11.178 32.029  17.643  1.00 20.11 ? 58  PRO A N   1 
ATOM   414  C CA  . PRO A 1 58  ? -10.634 32.961  16.638  1.00 18.80 ? 58  PRO A CA  1 
ATOM   415  C C   . PRO A 1 58  ? -9.355  32.486  15.987  1.00 17.08 ? 58  PRO A C   1 
ATOM   416  O O   . PRO A 1 58  ? -9.099  32.859  14.834  1.00 17.01 ? 58  PRO A O   1 
ATOM   417  C CB  . PRO A 1 58  ? -10.402 34.251  17.440  1.00 18.86 ? 58  PRO A CB  1 
ATOM   418  C CG  . PRO A 1 58  ? -11.356 34.163  18.551  1.00 20.62 ? 58  PRO A CG  1 
ATOM   419  C CD  . PRO A 1 58  ? -11.413 32.725  18.929  1.00 18.97 ? 58  PRO A CD  1 
ATOM   420  N N   . THR A 1 59  ? -8.549  31.668  16.666  1.00 16.41 ? 59  THR A N   1 
ATOM   421  C CA  . THR A 1 59  ? -7.318  31.216  16.031  1.00 17.50 ? 59  THR A CA  1 
ATOM   422  C C   . THR A 1 59  ? -7.563  30.230  14.907  1.00 16.52 ? 59  THR A C   1 
ATOM   423  O O   . THR A 1 59  ? -6.626  29.983  14.137  1.00 16.61 ? 59  THR A O   1 
ATOM   424  C CB  . THR A 1 59  ? -6.339  30.569  17.032  1.00 15.51 ? 59  THR A CB  1 
ATOM   425  O OG1 . THR A 1 59  ? -6.842  29.302  17.470  1.00 18.30 ? 59  THR A OG1 1 
ATOM   426  C CG2 . THR A 1 59  ? -6.042  31.470  18.227  1.00 17.02 ? 59  THR A CG2 1 
ATOM   427  N N   . LEU A 1 60  ? -8.765  29.652  14.797  1.00 15.19 ? 60  LEU A N   1 
ATOM   428  C CA  . LEU A 1 60  ? -9.050  28.711  13.713  1.00 16.19 ? 60  LEU A CA  1 
ATOM   429  C C   . LEU A 1 60  ? -9.776  29.330  12.527  1.00 16.51 ? 60  LEU A C   1 
ATOM   430  O O   . LEU A 1 60  ? -10.034 28.618  11.551  1.00 14.69 ? 60  LEU A O   1 
ATOM   431  C CB  . LEU A 1 60  ? -9.881  27.520  14.207  1.00 15.12 ? 60  LEU A CB  1 
ATOM   432  C CG  . LEU A 1 60  ? -9.189  26.711  15.316  1.00 16.38 ? 60  LEU A CG  1 
ATOM   433  C CD1 . LEU A 1 60  ? -10.128 25.661  15.880  1.00 18.28 ? 60  LEU A CD1 1 
ATOM   434  C CD2 . LEU A 1 60  ? -7.829  26.155  14.882  1.00 13.61 ? 60  LEU A CD2 1 
ATOM   435  N N   . VAL A 1 61  ? -10.140 30.613  12.581  1.00 16.62 ? 61  VAL A N   1 
ATOM   436  C CA  . VAL A 1 61  ? -10.986 31.180  11.523  1.00 16.18 ? 61  VAL A CA  1 
ATOM   437  C C   . VAL A 1 61  ? -10.327 31.035  10.152  1.00 16.12 ? 61  VAL A C   1 
ATOM   438  O O   . VAL A 1 61  ? -10.946 30.556  9.192   1.00 16.89 ? 61  VAL A O   1 
ATOM   439  C CB  . VAL A 1 61  ? -11.324 32.647  11.847  1.00 17.19 ? 61  VAL A CB  1 
ATOM   440  C CG1 . VAL A 1 61  ? -11.912 33.349  10.635  1.00 17.36 ? 61  VAL A CG1 1 
ATOM   441  C CG2 . VAL A 1 61  ? -12.320 32.691  12.976  1.00 18.93 ? 61  VAL A CG2 1 
ATOM   442  N N   . THR A 1 62  ? -9.059  31.459  10.030  1.00 17.36 ? 62  THR A N   1 
ATOM   443  C CA  . THR A 1 62  ? -8.425  31.441  8.712   1.00 14.18 ? 62  THR A CA  1 
ATOM   444  C C   . THR A 1 62  ? -8.315  30.022  8.170   1.00 17.45 ? 62  THR A C   1 
ATOM   445  O O   . THR A 1 62  ? -8.378  29.821  6.957   1.00 16.03 ? 62  THR A O   1 
ATOM   446  C CB  . THR A 1 62  ? -7.040  32.100  8.754   1.00 13.75 ? 62  THR A CB  1 
ATOM   447  O OG1 . THR A 1 62  ? -6.285  31.590  9.866   1.00 14.32 ? 62  THR A OG1 1 
ATOM   448  C CG2 . THR A 1 62  ? -7.180  33.589  8.924   1.00 14.39 ? 62  THR A CG2 1 
ATOM   449  N N   . THR A 1 63  ? -8.136  29.029  9.052   1.00 15.86 ? 63  THR A N   1 
ATOM   450  C CA  . THR A 1 63  ? -8.014  27.640  8.600   1.00 14.00 ? 63  THR A CA  1 
ATOM   451  C C   . THR A 1 63  ? -9.363  27.071  8.172   1.00 17.24 ? 63  THR A C   1 
ATOM   452  O O   . THR A 1 63  ? -9.472  26.409  7.131   1.00 15.14 ? 63  THR A O   1 
ATOM   453  C CB  . THR A 1 63  ? -7.410  26.789  9.721   1.00 16.08 ? 63  THR A CB  1 
ATOM   454  O OG1 . THR A 1 63  ? -6.159  27.346  10.119  1.00 15.43 ? 63  THR A OG1 1 
ATOM   455  C CG2 . THR A 1 63  ? -7.208  25.339  9.264   1.00 16.99 ? 63  THR A CG2 1 
ATOM   456  N N   . LEU A 1 64  ? -10.404 27.330  8.952   1.00 17.33 ? 64  LEU A N   1 
ATOM   457  C CA  . LEU A 1 64  ? -11.745 26.847  8.636   1.00 16.93 ? 64  LEU A CA  1 
ATOM   458  C C   . LEU A 1 64  ? -12.343 27.572  7.447   1.00 17.35 ? 64  LEU A C   1 
ATOM   459  O O   . LEU A 1 64  ? -13.042 26.969  6.647   1.00 16.08 ? 64  LEU A O   1 
ATOM   460  C CB  . LEU A 1 64  ? -12.669 27.012  9.842   1.00 15.21 ? 64  LEU A CB  1 
ATOM   461  C CG  . LEU A 1 64  ? -12.275 26.247  11.101  1.00 15.72 ? 64  LEU A CG  1 
ATOM   462  C CD1 . LEU A 1 64  ? -13.111 26.768  12.297  1.00 17.54 ? 64  LEU A CD1 1 
ATOM   463  C CD2 . LEU A 1 64  ? -12.458 24.745  10.894  1.00 19.22 ? 64  LEU A CD2 1 
HETATM 464  N N1  . CRO A 1 65  ? -12.119 28.930  7.488   1.00 17.99 ? 66  CRO A N1  1 
HETATM 465  C CA1 . CRO A 1 65  ? -12.511 29.738  6.371   1.00 20.90 ? 66  CRO A CA1 1 
HETATM 466  C CB1 . CRO A 1 65  ? -13.676 30.677  6.658   1.00 23.20 ? 66  CRO A CB1 1 
HETATM 467  C CG1 . CRO A 1 65  ? -14.944 29.910  6.921   1.00 24.40 ? 66  CRO A CG1 1 
HETATM 468  O OG1 . CRO A 1 65  ? -13.480 31.485  7.428   1.00 24.62 ? 66  CRO A OG1 1 
HETATM 469  C C1  . CRO A 1 65  ? -11.406 30.395  5.557   1.00 21.76 ? 66  CRO A C1  1 
HETATM 470  N N2  . CRO A 1 65  ? -11.063 31.621  5.714   1.00 22.47 ? 66  CRO A N2  1 
HETATM 471  N N3  . CRO A 1 65  ? -10.555 29.825  4.772   1.00 23.25 ? 66  CRO A N3  1 
HETATM 472  C C2  . CRO A 1 65  ? -9.657  30.692  4.464   1.00 21.79 ? 66  CRO A C2  1 
HETATM 473  O O2  . CRO A 1 65  ? -8.573  30.462  3.677   1.00 18.00 ? 66  CRO A O2  1 
HETATM 474  C CA2 . CRO A 1 65  ? -9.985  31.860  5.068   1.00 21.45 ? 66  CRO A CA2 1 
HETATM 475  C CA3 . CRO A 1 65  ? -10.519 28.475  4.328   1.00 20.45 ? 66  CRO A CA3 1 
HETATM 476  C C3  . CRO A 1 65  ? -11.168 28.238  2.958   1.00 23.06 ? 66  CRO A C3  1 
HETATM 477  O O3  . CRO A 1 65  ? -10.900 27.230  2.450   1.00 21.42 ? 66  CRO A O3  1 
HETATM 478  C CB2 . CRO A 1 65  ? -9.196  33.146  4.878   1.00 22.13 ? 66  CRO A CB2 1 
HETATM 479  C CG2 . CRO A 1 65  ? -9.445  34.399  5.689   1.00 23.78 ? 66  CRO A CG2 1 
HETATM 480  C CD1 . CRO A 1 65  ? -10.489 34.635  6.553   1.00 24.17 ? 66  CRO A CD1 1 
HETATM 481  C CD2 . CRO A 1 65  ? -8.516  35.384  5.527   1.00 25.01 ? 66  CRO A CD2 1 
HETATM 482  C CE1 . CRO A 1 65  ? -10.575 35.827  7.211   1.00 18.44 ? 66  CRO A CE1 1 
HETATM 483  C CE2 . CRO A 1 65  ? -8.576  36.564  6.188   1.00 21.78 ? 66  CRO A CE2 1 
HETATM 484  C CZ  . CRO A 1 65  ? -9.617  36.793  7.028   1.00 24.82 ? 66  CRO A CZ  1 
HETATM 485  O OH  . CRO A 1 65  ? -9.658  37.991  7.673   1.00 24.68 ? 66  CRO A OH  1 
ATOM   486  N N   . VAL A 1 66  ? -12.146 29.076  2.671   1.00 15.46 ? 68  VAL A N   1 
ATOM   487  C CA  . VAL A 1 66  ? -12.834 28.720  1.438   1.00 17.45 ? 68  VAL A CA  1 
ATOM   488  C C   . VAL A 1 66  ? -12.891 29.974  0.571   1.00 19.93 ? 68  VAL A C   1 
ATOM   489  O O   . VAL A 1 66  ? -13.962 30.510  0.289   1.00 20.78 ? 68  VAL A O   1 
ATOM   490  C CB  . VAL A 1 66  ? -14.247 28.128  1.737   1.00 18.88 ? 68  VAL A CB  1 
ATOM   491  C CG1 . VAL A 1 66  ? -14.104 26.747  2.411   1.00 16.27 ? 68  VAL A CG1 1 
ATOM   492  C CG2 . VAL A 1 66  ? -15.048 29.049  2.641   1.00 21.25 ? 68  VAL A CG2 1 
ATOM   493  N N   . GLN A 1 67  ? -11.714 30.461  0.169   1.00 19.66 ? 69  GLN A N   1 
ATOM   494  C CA  . GLN A 1 67  ? -11.634 31.721  -0.565  1.00 19.60 ? 69  GLN A CA  1 
ATOM   495  C C   . GLN A 1 67  ? -12.305 31.632  -1.925  1.00 22.69 ? 69  GLN A C   1 
ATOM   496  O O   . GLN A 1 67  ? -12.492 32.666  -2.575  1.00 24.82 ? 69  GLN A O   1 
ATOM   497  C CB  . GLN A 1 67  ? -10.163 32.166  -0.684  1.00 20.00 ? 69  GLN A CB  1 
ATOM   498  C CG  . GLN A 1 67  ? -9.524  32.420  0.704   1.00 17.08 ? 69  GLN A CG  1 
ATOM   499  C CD  . GLN A 1 67  ? -7.990  32.462  0.703   1.00 18.22 ? 69  GLN A CD  1 
ATOM   500  O OE1 . GLN A 1 67  ? -7.341  31.513  0.265   1.00 22.32 ? 69  GLN A OE1 1 
ATOM   501  N NE2 . GLN A 1 67  ? -7.413  33.501  1.318   1.00 20.19 ? 69  GLN A NE2 1 
ATOM   502  N N   . CYS A 1 68  ? -12.716 30.433  -2.342  1.00 20.82 ? 70  CYS A N   1 
ATOM   503  C CA  . CYS A 1 68  ? -13.513 30.296  -3.551  1.00 25.57 ? 70  CYS A CA  1 
ATOM   504  C C   . CYS A 1 68  ? -14.847 31.028  -3.455  1.00 25.24 ? 70  CYS A C   1 
ATOM   505  O O   . CYS A 1 68  ? -15.543 31.142  -4.472  1.00 28.75 ? 70  CYS A O   1 
ATOM   506  C CB  . CYS A 1 68  ? -13.756 28.808  -3.857  1.00 24.42 ? 70  CYS A CB  1 
ATOM   507  S SG  . CYS A 1 68  ? -14.364 27.814  -2.467  1.00 24.16 ? 70  CYS A SG  1 
ATOM   508  N N   . PHE A 1 69  ? -15.230 31.517  -2.273  1.00 22.17 ? 71  PHE A N   1 
ATOM   509  C CA  . PHE A 1 69  ? -16.526 32.162  -2.093  1.00 24.20 ? 71  PHE A CA  1 
ATOM   510  C C   . PHE A 1 69  ? -16.439 33.673  -2.147  1.00 24.50 ? 71  PHE A C   1 
ATOM   511  O O   . PHE A 1 69  ? -17.407 34.359  -1.802  1.00 26.28 ? 71  PHE A O   1 
ATOM   512  C CB  . PHE A 1 69  ? -17.171 31.711  -0.787  1.00 23.28 ? 71  PHE A CB  1 
ATOM   513  C CG  . PHE A 1 69  ? -17.858 30.392  -0.916  1.00 24.71 ? 71  PHE A CG  1 
ATOM   514  C CD1 . PHE A 1 69  ? -19.036 30.288  -1.639  1.00 25.02 ? 71  PHE A CD1 1 
ATOM   515  C CD2 . PHE A 1 69  ? -17.273 29.237  -0.414  1.00 25.62 ? 71  PHE A CD2 1 
ATOM   516  C CE1 . PHE A 1 69  ? -19.659 29.057  -1.807  1.00 27.16 ? 71  PHE A CE1 1 
ATOM   517  C CE2 . PHE A 1 69  ? -17.887 27.996  -0.576  1.00 26.28 ? 71  PHE A CE2 1 
ATOM   518  C CZ  . PHE A 1 69  ? -19.086 27.908  -1.269  1.00 27.96 ? 71  PHE A CZ  1 
ATOM   519  N N   . SER A 1 70  ? -15.321 34.212  -2.599  1.00 25.16 ? 72  SER A N   1 
ATOM   520  C CA  . SER A 1 70  ? -15.186 35.652  -2.654  1.00 24.20 ? 72  SER A CA  1 
ATOM   521  C C   . SER A 1 70  ? -15.900 36.191  -3.881  1.00 28.66 ? 72  SER A C   1 
ATOM   522  O O   . SER A 1 70  ? -15.936 35.547  -4.932  1.00 25.06 ? 72  SER A O   1 
ATOM   523  C CB  . SER A 1 70  ? -13.719 36.040  -2.678  1.00 30.36 ? 72  SER A CB  1 
ATOM   524  O OG  . SER A 1 70  ? -13.337 36.334  -3.987  1.00 37.25 ? 72  SER A OG  1 
ATOM   525  N N   . ARG A 1 71  ? -16.515 37.356  -3.719  1.00 26.21 ? 73  ARG A N   1 
ATOM   526  C CA  . ARG A 1 71  ? -17.105 38.102  -4.823  1.00 30.90 ? 73  ARG A CA  1 
ATOM   527  C C   . ARG A 1 71  ? -15.988 38.691  -5.671  1.00 33.44 ? 73  ARG A C   1 
ATOM   528  O O   . ARG A 1 71  ? -15.349 39.669  -5.276  1.00 30.79 ? 73  ARG A O   1 
ATOM   529  C CB  . ARG A 1 71  ? -17.989 39.215  -4.274  1.00 29.06 ? 73  ARG A CB  1 
ATOM   530  C CG  . ARG A 1 71  ? -18.683 40.059  -5.320  1.00 32.81 ? 73  ARG A CG  1 
ATOM   531  C CD  . ARG A 1 71  ? -19.850 40.780  -4.668  1.00 30.31 ? 73  ARG A CD  1 
ATOM   532  N NE  . ARG A 1 71  ? -19.395 42.029  -4.057  1.00 34.72 ? 73  ARG A NE  1 
ATOM   533  C CZ  . ARG A 1 71  ? -18.726 42.994  -4.679  1.00 32.27 ? 73  ARG A CZ  1 
ATOM   534  N NH1 . ARG A 1 71  ? -18.618 43.029  -5.997  1.00 37.16 ? 73  ARG A NH1 1 
ATOM   535  N NH2 . ARG A 1 71  ? -18.193 43.978  -3.963  1.00 36.54 ? 73  ARG A NH2 1 
ATOM   536  N N   . TYR A 1 72  ? -15.731 38.102  -6.838  1.00 33.03 ? 74  TYR A N   1 
ATOM   537  C CA  . TYR A 1 72  ? -14.858 38.753  -7.804  1.00 40.96 ? 74  TYR A CA  1 
ATOM   538  C C   . TYR A 1 72  ? -15.730 39.597  -8.721  1.00 44.39 ? 74  TYR A C   1 
ATOM   539  O O   . TYR A 1 72  ? -16.592 39.039  -9.413  1.00 46.53 ? 74  TYR A O   1 
ATOM   540  C CB  . TYR A 1 72  ? -14.062 37.742  -8.631  1.00 36.53 ? 74  TYR A CB  1 
ATOM   541  C CG  . TYR A 1 72  ? -12.781 37.229  -7.994  1.00 34.74 ? 74  TYR A CG  1 
ATOM   542  C CD1 . TYR A 1 72  ? -12.826 36.476  -6.840  1.00 33.29 ? 74  TYR A CD1 1 
ATOM   543  C CD2 . TYR A 1 72  ? -11.530 37.492  -8.552  1.00 35.65 ? 74  TYR A CD2 1 
ATOM   544  C CE1 . TYR A 1 72  ? -11.674 35.992  -6.247  1.00 32.17 ? 74  TYR A CE1 1 
ATOM   545  C CE2 . TYR A 1 72  ? -10.356 37.011  -7.956  1.00 32.26 ? 74  TYR A CE2 1 
ATOM   546  C CZ  . TYR A 1 72  ? -10.442 36.264  -6.792  1.00 34.28 ? 74  TYR A CZ  1 
ATOM   547  O OH  . TYR A 1 72  ? -9.326  35.758  -6.146  1.00 27.67 ? 74  TYR A OH  1 
ATOM   548  N N   . PRO A 1 73  ? -15.582 40.922  -8.738  1.00 45.25 ? 75  PRO A N   1 
ATOM   549  C CA  . PRO A 1 73  ? -16.316 41.721  -9.727  1.00 46.59 ? 75  PRO A CA  1 
ATOM   550  C C   . PRO A 1 73  ? -15.973 41.294  -11.150 1.00 53.49 ? 75  PRO A C   1 
ATOM   551  O O   . PRO A 1 73  ? -14.962 40.634  -11.404 1.00 52.41 ? 75  PRO A O   1 
ATOM   552  C CB  . PRO A 1 73  ? -15.874 43.162  -9.430  1.00 47.87 ? 75  PRO A CB  1 
ATOM   553  C CG  . PRO A 1 73  ? -14.597 43.039  -8.648  1.00 49.71 ? 75  PRO A CG  1 
ATOM   554  C CD  . PRO A 1 73  ? -14.683 41.737  -7.903  1.00 41.87 ? 75  PRO A CD  1 
ATOM   555  N N   . ASP A 1 74  ? -16.857 41.659  -12.086 1.00 52.85 ? 76  ASP A N   1 
ATOM   556  C CA  . ASP A 1 74  ? -16.790 41.104  -13.438 1.00 57.18 ? 76  ASP A CA  1 
ATOM   557  C C   . ASP A 1 74  ? -15.417 41.311  -14.074 1.00 55.43 ? 76  ASP A C   1 
ATOM   558  O O   . ASP A 1 74  ? -14.876 40.395  -14.707 1.00 56.36 ? 76  ASP A O   1 
ATOM   559  C CB  . ASP A 1 74  ? -17.883 41.716  -14.316 1.00 56.08 ? 76  ASP A CB  1 
ATOM   560  C CG  . ASP A 1 74  ? -19.084 40.801  -14.472 1.00 61.57 ? 76  ASP A CG  1 
ATOM   561  O OD1 . ASP A 1 74  ? -18.895 39.645  -14.907 1.00 63.74 ? 76  ASP A OD1 1 
ATOM   562  O OD2 . ASP A 1 74  ? -20.219 41.242  -14.180 1.00 60.21 ? 76  ASP A OD2 1 
ATOM   563  N N   . HIS A 1 75  ? -14.830 42.498  -13.910 1.00 53.26 ? 77  HIS A N   1 
ATOM   564  C CA  . HIS A 1 75  ? -13.530 42.782  -14.514 1.00 57.64 ? 77  HIS A CA  1 
ATOM   565  C C   . HIS A 1 75  ? -12.392 41.990  -13.871 1.00 57.79 ? 77  HIS A C   1 
ATOM   566  O O   . HIS A 1 75  ? -11.236 42.144  -14.282 1.00 55.39 ? 77  HIS A O   1 
ATOM   567  C CB  . HIS A 1 75  ? -13.256 44.291  -14.454 1.00 60.01 ? 77  HIS A CB  1 
ATOM   568  C CG  . HIS A 1 75  ? -12.423 44.722  -13.286 1.00 59.89 ? 77  HIS A CG  1 
ATOM   569  N ND1 . HIS A 1 75  ? -12.970 45.053  -12.064 1.00 59.83 ? 77  HIS A ND1 1 
ATOM   570  C CD2 . HIS A 1 75  ? -11.089 44.921  -13.166 1.00 59.88 ? 77  HIS A CD2 1 
ATOM   571  C CE1 . HIS A 1 75  ? -12.006 45.411  -11.235 1.00 60.54 ? 77  HIS A CE1 1 
ATOM   572  N NE2 . HIS A 1 75  ? -10.855 45.340  -11.878 1.00 59.58 ? 77  HIS A NE2 1 
ATOM   573  N N   . MET A 1 76  ? -12.695 41.110  -12.924 1.00 56.02 ? 78  MET A N   1 
ATOM   574  C CA  . MET A 1 76  ? -11.670 40.354  -12.204 1.00 56.90 ? 78  MET A CA  1 
ATOM   575  C C   . MET A 1 76  ? -11.851 38.849  -12.339 1.00 54.65 ? 78  MET A C   1 
ATOM   576  O O   . MET A 1 76  ? -10.969 38.088  -12.034 1.00 52.04 ? 78  MET A O   1 
ATOM   577  C CB  . MET A 1 76  ? -11.669 40.698  -10.710 1.00 50.42 ? 78  MET A CB  1 
ATOM   578  C CG  . MET A 1 76  ? -11.325 42.114  -10.369 1.00 54.36 ? 78  MET A CG  1 
ATOM   579  S SD  . MET A 1 76  ? -9.570  42.300  -10.241 1.00 59.53 ? 78  MET A SD  1 
ATOM   580  C CE  . MET A 1 76  ? -9.357  41.512  -8.681  1.00 39.98 ? 78  MET A CE  1 
ATOM   581  N N   . LYS A 1 77  ? -13.021 38.438  -12.776 1.00 56.08 ? 79  LYS A N   1 
ATOM   582  C CA  . LYS A 1 77  ? -13.352 37.038  -12.841 1.00 53.19 ? 79  LYS A CA  1 
ATOM   583  C C   . LYS A 1 77  ? -12.276 36.230  -13.526 1.00 57.71 ? 79  LYS A C   1 
ATOM   584  O O   . LYS A 1 77  ? -12.242 35.032  -13.453 1.00 62.47 ? 79  LYS A O   1 
ATOM   585  C CB  . LYS A 1 77  ? -14.696 36.870  -13.521 1.00 57.60 ? 79  LYS A CB  1 
ATOM   586  C CG  . LYS A 1 77  ? -15.857 36.968  -12.539 1.00 59.11 ? 79  LYS A CG  1 
ATOM   587  C CD  . LYS A 1 77  ? -17.215 37.165  -13.192 1.00 61.14 ? 79  LYS A CD  1 
ATOM   588  C CE  . LYS A 1 77  ? -18.259 37.226  -12.138 1.00 64.67 ? 79  LYS A CE  1 
ATOM   589  N NZ  . LYS A 1 77  ? -19.282 36.204  -12.349 1.00 72.42 ? 79  LYS A NZ  1 
ATOM   590  N N   . ARG A 1 78  ? -11.347 36.920  -14.120 1.00 50.92 ? 80  ARG A N   1 
ATOM   591  C CA  . ARG A 1 78  ? -10.337 36.284  -14.876 1.00 51.54 ? 80  ARG A CA  1 
ATOM   592  C C   . ARG A 1 78  ? -9.226  35.755  -14.015 1.00 46.96 ? 80  ARG A C   1 
ATOM   593  O O   . ARG A 1 78  ? -8.354  35.071  -14.464 1.00 48.18 ? 80  ARG A O   1 
ATOM   594  C CB  . ARG A 1 78  ? -9.821  37.315  -15.858 1.00 53.67 ? 80  ARG A CB  1 
ATOM   595  C CG  . ARG A 1 78  ? -9.142  36.769  -17.030 1.00 53.76 ? 80  ARG A CG  1 
ATOM   596  C CD  . ARG A 1 78  ? -8.784  37.882  -17.952 1.00 53.46 ? 80  ARG A CD  1 
ATOM   597  N NE  . ARG A 1 78  ? -9.850  38.876  -18.115 1.00 53.82 ? 80  ARG A NE  1 
ATOM   598  C CZ  . ARG A 1 78  ? -9.709  40.180  -17.894 1.00 54.95 ? 80  ARG A CZ  1 
ATOM   599  N NH1 . ARG A 1 78  ? -8.558  40.658  -17.450 1.00 50.92 ? 80  ARG A NH1 1 
ATOM   600  N NH2 . ARG A 1 78  ? -10.728 41.005  -18.086 1.00 53.09 ? 80  ARG A NH2 1 
ATOM   601  N N   . HIS A 1 79  ? -9.274  36.108  -12.754 1.00 47.47 ? 81  HIS A N   1 
ATOM   602  C CA  . HIS A 1 79  ? -8.202  35.793  -11.848 1.00 41.97 ? 81  HIS A CA  1 
ATOM   603  C C   . HIS A 1 79  ? -8.719  35.075  -10.648 1.00 38.52 ? 81  HIS A C   1 
ATOM   604  O O   . HIS A 1 79  ? -8.348  35.485  -9.583  1.00 40.04 ? 81  HIS A O   1 
ATOM   605  C CB  . HIS A 1 79  ? -7.595  37.118  -11.322 1.00 42.36 ? 81  HIS A CB  1 
ATOM   606  C CG  . HIS A 1 79  ? -7.277  38.104  -12.397 1.00 44.84 ? 81  HIS A CG  1 
ATOM   607  N ND1 . HIS A 1 79  ? -6.228  37.935  -13.269 1.00 40.11 ? 81  HIS A ND1 1 
ATOM   608  C CD2 . HIS A 1 79  ? -7.899  39.238  -12.772 1.00 49.93 ? 81  HIS A CD2 1 
ATOM   609  C CE1 . HIS A 1 79  ? -6.226  38.914  -14.141 1.00 45.37 ? 81  HIS A CE1 1 
ATOM   610  N NE2 . HIS A 1 79  ? -7.227  39.721  -13.860 1.00 48.50 ? 81  HIS A NE2 1 
ATOM   611  N N   . ASP A 1 80  ? -9.532  34.025  -10.780 1.00 38.03 ? 82  ASP A N   1 
ATOM   612  C CA  . ASP A 1 80  ? -10.277 33.613  -9.591  1.00 32.19 ? 82  ASP A CA  1 
ATOM   613  C C   . ASP A 1 80  ? -9.731  32.213  -9.800  1.00 32.11 ? 82  ASP A C   1 
ATOM   614  O O   . ASP A 1 80  ? -10.399 31.336  -10.291 1.00 26.60 ? 82  ASP A O   1 
ATOM   615  C CB  . ASP A 1 80  ? -11.780 33.656  -9.744  1.00 32.32 ? 82  ASP A CB  1 
ATOM   616  C CG  . ASP A 1 80  ? -12.450 33.328  -8.464  1.00 31.78 ? 82  ASP A CG  1 
ATOM   617  O OD1 . ASP A 1 80  ? -11.717 32.873  -7.616  1.00 30.38 ? 82  ASP A OD1 1 
ATOM   618  O OD2 . ASP A 1 80  ? -13.649 33.506  -8.315  1.00 28.88 ? 82  ASP A OD2 1 
ATOM   619  N N   . PHE A 1 81  ? -8.513  32.030  -9.340  1.00 29.18 ? 83  PHE A N   1 
ATOM   620  C CA  . PHE A 1 81  ? -7.889  30.710  -9.264  1.00 30.31 ? 83  PHE A CA  1 
ATOM   621  C C   . PHE A 1 81  ? -8.745  29.737  -8.462  1.00 28.55 ? 83  PHE A C   1 
ATOM   622  O O   . PHE A 1 81  ? -8.889  28.567  -8.837  1.00 26.94 ? 83  PHE A O   1 
ATOM   623  C CB  . PHE A 1 81  ? -6.503  30.840  -8.622  1.00 29.40 ? 83  PHE A CB  1 
ATOM   624  C CG  . PHE A 1 81  ? -5.913  29.533  -8.158  1.00 30.73 ? 83  PHE A CG  1 
ATOM   625  C CD1 . PHE A 1 81  ? -5.218  28.716  -9.037  1.00 33.42 ? 83  PHE A CD1 1 
ATOM   626  C CD2 . PHE A 1 81  ? -6.069  29.112  -6.844  1.00 27.88 ? 83  PHE A CD2 1 
ATOM   627  C CE1 . PHE A 1 81  ? -4.670  27.510  -8.609  1.00 34.39 ? 83  PHE A CE1 1 
ATOM   628  C CE2 . PHE A 1 81  ? -5.541  27.901  -6.417  1.00 27.77 ? 83  PHE A CE2 1 
ATOM   629  C CZ  . PHE A 1 81  ? -4.836  27.101  -7.305  1.00 29.45 ? 83  PHE A CZ  1 
ATOM   630  N N   . PHE A 1 82  ? -9.312  30.211  -7.350  1.00 24.87 ? 84  PHE A N   1 
ATOM   631  C CA  . PHE A 1 82  ? -9.999  29.332  -6.411  1.00 24.69 ? 84  PHE A CA  1 
ATOM   632  C C   . PHE A 1 82  ? -11.227 28.688  -7.032  1.00 25.53 ? 84  PHE A C   1 
ATOM   633  O O   . PHE A 1 82  ? -11.528 27.519  -6.766  1.00 23.74 ? 84  PHE A O   1 
ATOM   634  C CB  . PHE A 1 82  ? -10.396 30.126  -5.171  1.00 26.81 ? 84  PHE A CB  1 
ATOM   635  C CG  . PHE A 1 82  ? -9.255  30.831  -4.530  1.00 25.21 ? 84  PHE A CG  1 
ATOM   636  C CD1 . PHE A 1 82  ? -8.408  30.160  -3.674  1.00 23.96 ? 84  PHE A CD1 1 
ATOM   637  C CD2 . PHE A 1 82  ? -9.023  32.169  -4.790  1.00 27.31 ? 84  PHE A CD2 1 
ATOM   638  C CE1 . PHE A 1 82  ? -7.347  30.809  -3.071  1.00 27.07 ? 84  PHE A CE1 1 
ATOM   639  C CE2 . PHE A 1 82  ? -7.964  32.821  -4.196  1.00 24.81 ? 84  PHE A CE2 1 
ATOM   640  C CZ  . PHE A 1 82  ? -7.124  32.143  -3.338  1.00 25.10 ? 84  PHE A CZ  1 
ATOM   641  N N   . LYS A 1 83  ? -11.972 29.441  -7.841  1.00 25.75 ? 85  LYS A N   1 
ATOM   642  C CA  . LYS A 1 83  ? -13.113 28.836  -8.506  1.00 29.37 ? 85  LYS A CA  1 
ATOM   643  C C   . LYS A 1 83  ? -12.679 28.043  -9.722  1.00 28.25 ? 85  LYS A C   1 
ATOM   644  O O   . LYS A 1 83  ? -13.274 27.003  -10.027 1.00 27.04 ? 85  LYS A O   1 
ATOM   645  C CB  . LYS A 1 83  ? -14.132 29.902  -8.901  1.00 31.49 ? 85  LYS A CB  1 
ATOM   646  C CG  . LYS A 1 83  ? -14.767 30.612  -7.731  1.00 28.62 ? 85  LYS A CG  1 
ATOM   647  C CD  . LYS A 1 83  ? -15.946 31.460  -8.223  1.00 31.92 ? 85  LYS A CD  1 
ATOM   648  C CE  . LYS A 1 83  ? -16.457 32.368  -7.134  1.00 31.19 ? 85  LYS A CE  1 
ATOM   649  N NZ  . LYS A 1 83  ? -15.361 33.291  -6.703  1.00 28.13 ? 85  LYS A NZ  1 
ATOM   650  N N   . SER A 1 84  ? -11.644 28.504  -10.423 1.00 25.89 ? 86  SER A N   1 
ATOM   651  C CA  . SER A 1 84  ? -11.268 27.827  -11.655 1.00 30.33 ? 86  SER A CA  1 
ATOM   652  C C   . SER A 1 84  ? -10.800 26.405  -11.398 1.00 31.94 ? 86  SER A C   1 
ATOM   653  O O   . SER A 1 84  ? -10.930 25.551  -12.285 1.00 27.18 ? 86  SER A O   1 
ATOM   654  C CB  . SER A 1 84  ? -10.199 28.633  -12.395 1.00 34.55 ? 86  SER A CB  1 
ATOM   655  O OG  . SER A 1 84  ? -8.905  28.112  -12.161 1.00 41.19 ? 86  SER A OG  1 
ATOM   656  N N   . ALA A 1 85  ? -10.299 26.125  -10.191 1.00 27.11 ? 87  ALA A N   1 
ATOM   657  C CA  . ALA A 1 85  ? -9.832  24.796  -9.820  1.00 28.32 ? 87  ALA A CA  1 
ATOM   658  C C   . ALA A 1 85  ? -10.968 23.829  -9.534  1.00 25.45 ? 87  ALA A C   1 
ATOM   659  O O   . ALA A 1 85  ? -10.726 22.624  -9.418  1.00 31.30 ? 87  ALA A O   1 
ATOM   660  C CB  . ALA A 1 85  ? -8.922  24.892  -8.590  1.00 24.72 ? 87  ALA A CB  1 
ATOM   661  N N   . MET A 1 86  ? -12.176 24.321  -9.373  1.00 27.70 ? 88  MET A N   1 
ATOM   662  C CA  . MET A 1 86  ? -13.313 23.477  -9.097  1.00 27.97 ? 88  MET A CA  1 
ATOM   663  C C   . MET A 1 86  ? -13.733 22.739  -10.370 1.00 32.16 ? 88  MET A C   1 
ATOM   664  O O   . MET A 1 86  ? -13.443 23.191  -11.483 1.00 29.72 ? 88  MET A O   1 
ATOM   665  C CB  . MET A 1 86  ? -14.450 24.338  -8.562  1.00 26.78 ? 88  MET A CB  1 
ATOM   666  C CG  . MET A 1 86  ? -14.366 24.747  -7.092  1.00 26.70 ? 88  MET A CG  1 
ATOM   667  S SD  . MET A 1 86  ? -13.463 23.644  -5.996  1.00 24.34 ? 88  MET A SD  1 
ATOM   668  C CE  . MET A 1 86  ? -12.498 24.750  -4.949  1.00 21.50 ? 88  MET A CE  1 
ATOM   669  N N   . PRO A 1 87  ? -14.406 21.581  -10.235 1.00 30.32 ? 89  PRO A N   1 
ATOM   670  C CA  . PRO A 1 87  ? -14.775 20.931  -8.971  1.00 29.25 ? 89  PRO A CA  1 
ATOM   671  C C   . PRO A 1 87  ? -13.666 20.071  -8.375  1.00 29.15 ? 89  PRO A C   1 
ATOM   672  O O   . PRO A 1 87  ? -13.812 19.644  -7.233  1.00 29.78 ? 89  PRO A O   1 
ATOM   673  C CB  . PRO A 1 87  ? -15.973 20.054  -9.358  1.00 29.01 ? 89  PRO A CB  1 
ATOM   674  C CG  . PRO A 1 87  ? -15.756 19.734  -10.811 1.00 30.27 ? 89  PRO A CG  1 
ATOM   675  C CD  . PRO A 1 87  ? -14.918 20.845  -11.411 1.00 30.15 ? 89  PRO A CD  1 
ATOM   676  N N   . GLU A 1 88  ? -12.583 19.806  -9.113  1.00 28.30 ? 90  GLU A N   1 
ATOM   677  C CA  . GLU A 1 88  ? -11.531 18.961  -8.555  1.00 28.01 ? 90  GLU A CA  1 
ATOM   678  C C   . GLU A 1 88  ? -10.899 19.600  -7.328  1.00 29.13 ? 90  GLU A C   1 
ATOM   679  O O   . GLU A 1 88  ? -10.493 18.893  -6.402  1.00 30.68 ? 90  GLU A O   1 
ATOM   680  C CB  . GLU A 1 88  ? -10.453 18.644  -9.593  1.00 29.98 ? 90  GLU A CB  1 
ATOM   681  C CG  . GLU A 1 88  ? -10.945 17.900  -10.826 1.00 36.13 ? 90  GLU A CG  1 
ATOM   682  C CD  . GLU A 1 88  ? -11.616 18.790  -11.848 1.00 38.07 ? 90  GLU A CD  1 
ATOM   683  O OE1 . GLU A 1 88  ? -11.651 20.029  -11.658 1.00 33.35 ? 90  GLU A OE1 1 
ATOM   684  O OE2 . GLU A 1 88  ? -12.134 18.230  -12.840 1.00 46.68 ? 90  GLU A OE2 1 
ATOM   685  N N   . GLY A 1 89  ? -10.813 20.917  -7.296  1.00 26.39 ? 91  GLY A N   1 
ATOM   686  C CA  . GLY A 1 89  ? -10.418 21.590  -6.077  1.00 23.96 ? 91  GLY A CA  1 
ATOM   687  C C   . GLY A 1 89  ? -8.937  21.888  -5.993  1.00 23.28 ? 91  GLY A C   1 
ATOM   688  O O   . GLY A 1 89  ? -8.188  21.792  -6.968  1.00 20.89 ? 91  GLY A O   1 
ATOM   689  N N   . TYR A 1 90  ? -8.509  22.266  -4.778  1.00 19.49 ? 92  TYR A N   1 
ATOM   690  C CA  . TYR A 1 90  ? -7.131  22.679  -4.562  1.00 18.61 ? 92  TYR A CA  1 
ATOM   691  C C   . TYR A 1 90  ? -6.712  22.260  -3.159  1.00 20.13 ? 92  TYR A C   1 
ATOM   692  O O   . TYR A 1 90  ? -7.552  22.103  -2.267  1.00 18.60 ? 92  TYR A O   1 
ATOM   693  C CB  . TYR A 1 90  ? -6.931  24.199  -4.769  1.00 19.92 ? 92  TYR A CB  1 
ATOM   694  C CG  . TYR A 1 90  ? -7.840  25.126  -3.975  1.00 20.13 ? 92  TYR A CG  1 
ATOM   695  C CD1 . TYR A 1 90  ? -7.586  25.420  -2.627  1.00 18.14 ? 92  TYR A CD1 1 
ATOM   696  C CD2 . TYR A 1 90  ? -8.947  25.720  -4.571  1.00 22.02 ? 92  TYR A CD2 1 
ATOM   697  C CE1 . TYR A 1 90  ? -8.431  26.276  -1.917  1.00 19.12 ? 92  TYR A CE1 1 
ATOM   698  C CE2 . TYR A 1 90  ? -9.787  26.559  -3.865  1.00 21.57 ? 92  TYR A CE2 1 
ATOM   699  C CZ  . TYR A 1 90  ? -9.522  26.841  -2.544  1.00 19.23 ? 92  TYR A CZ  1 
ATOM   700  O OH  . TYR A 1 90  ? -10.377 27.693  -1.863  1.00 20.42 ? 92  TYR A OH  1 
ATOM   701  N N   . VAL A 1 91  ? -5.424  22.030  -2.998  1.00 18.16 ? 93  VAL A N   1 
ATOM   702  C CA  . VAL A 1 91  ? -4.817  21.837  -1.691  1.00 19.24 ? 93  VAL A CA  1 
ATOM   703  C C   . VAL A 1 91  ? -4.474  23.221  -1.157  1.00 21.97 ? 93  VAL A C   1 
ATOM   704  O O   . VAL A 1 91  ? -3.939  24.062  -1.889  1.00 22.30 ? 93  VAL A O   1 
ATOM   705  C CB  . VAL A 1 91  ? -3.560  20.949  -1.802  1.00 20.31 ? 93  VAL A CB  1 
ATOM   706  C CG1 . VAL A 1 91  ? -2.817  20.884  -0.468  1.00 22.02 ? 93  VAL A CG1 1 
ATOM   707  C CG2 . VAL A 1 91  ? -3.933  19.560  -2.269  1.00 21.78 ? 93  VAL A CG2 1 
ATOM   708  N N   . GLN A 1 92  ? -4.787  23.483  0.111   1.00 18.14 ? 94  GLN A N   1 
ATOM   709  C CA  . GLN A 1 92  ? -4.419  24.738  0.754   1.00 18.14 ? 94  GLN A CA  1 
ATOM   710  C C   . GLN A 1 92  ? -3.538  24.410  1.945   1.00 19.26 ? 94  GLN A C   1 
ATOM   711  O O   . GLN A 1 92  ? -3.967  23.693  2.852   1.00 16.66 ? 94  GLN A O   1 
ATOM   712  C CB  . GLN A 1 92  ? -5.651  25.522  1.212   1.00 16.71 ? 94  GLN A CB  1 
ATOM   713  C CG  . GLN A 1 92  ? -5.288  26.871  1.840   1.00 18.29 ? 94  GLN A CG  1 
ATOM   714  C CD  . GLN A 1 92  ? -6.453  27.847  1.889   1.00 19.14 ? 94  GLN A CD  1 
ATOM   715  O OE1 . GLN A 1 92  ? -6.920  28.307  0.855   1.00 19.50 ? 94  GLN A OE1 1 
ATOM   716  N NE2 . GLN A 1 92  ? -6.894  28.202  3.093   1.00 16.51 ? 94  GLN A NE2 1 
ATOM   717  N N   . GLU A 1 93  ? -2.323  24.930  1.957   1.00 15.88 ? 95  GLU A N   1 
ATOM   718  C CA  . GLU A 1 93  ? -1.411  24.652  3.059   1.00 20.98 ? 95  GLU A CA  1 
ATOM   719  C C   . GLU A 1 93  ? -0.956  25.943  3.705   1.00 20.13 ? 95  GLU A C   1 
ATOM   720  O O   . GLU A 1 93  ? -0.682  26.931  3.014   1.00 19.49 ? 95  GLU A O   1 
ATOM   721  C CB  . GLU A 1 93  ? -0.179  23.870  2.600   1.00 24.79 ? 95  GLU A CB  1 
ATOM   722  C CG  . GLU A 1 93  ? -0.470  22.408  2.441   1.00 21.09 ? 95  GLU A CG  1 
ATOM   723  C CD  . GLU A 1 93  ? 0.538   21.691  1.580   1.00 27.76 ? 95  GLU A CD  1 
ATOM   724  O OE1 . GLU A 1 93  ? 0.999   22.254  0.563   1.00 30.57 ? 95  GLU A OE1 1 
ATOM   725  O OE2 . GLU A 1 93  ? 0.871   20.545  1.955   1.00 31.11 ? 95  GLU A OE2 1 
ATOM   726  N N   . ARG A 1 94  ? -0.838  25.921  5.026   1.00 18.31 ? 96  ARG A N   1 
ATOM   727  C CA  . ARG A 1 94  ? -0.386  27.089  5.748   1.00 16.47 ? 96  ARG A CA  1 
ATOM   728  C C   . ARG A 1 94  ? 0.537   26.659  6.874   1.00 21.38 ? 96  ARG A C   1 
ATOM   729  O O   . ARG A 1 94  ? 0.384   25.575  7.441   1.00 20.30 ? 96  ARG A O   1 
ATOM   730  C CB  . ARG A 1 94  ? -1.558  27.880  6.335   1.00 16.64 ? 96  ARG A CB  1 
ATOM   731  C CG  . ARG A 1 94  ? -2.391  28.654  5.310   1.00 16.12 ? 96  ARG A CG  1 
ATOM   732  C CD  . ARG A 1 94  ? -2.918  29.908  5.941   1.00 16.42 ? 96  ARG A CD  1 
ATOM   733  N NE  . ARG A 1 94  ? -3.873  30.624  5.094   1.00 17.34 ? 96  ARG A NE  1 
ATOM   734  C CZ  . ARG A 1 94  ? -5.192  30.476  5.156   1.00 17.20 ? 96  ARG A CZ  1 
ATOM   735  N NH1 . ARG A 1 94  ? -5.753  29.599  5.976   1.00 14.06 ? 96  ARG A NH1 1 
ATOM   736  N NH2 . ARG A 1 94  ? -5.967  31.258  4.408   1.00 14.95 ? 96  ARG A NH2 1 
ATOM   737  N N   . THR A 1 95  ? 1.501   27.517  7.184   1.00 18.21 ? 97  THR A N   1 
ATOM   738  C CA  . THR A 1 95  ? 2.065   27.571  8.521   1.00 21.21 ? 97  THR A CA  1 
ATOM   739  C C   . THR A 1 95  ? 1.647   28.896  9.134   1.00 20.06 ? 97  THR A C   1 
ATOM   740  O O   . THR A 1 95  ? 1.678   29.936  8.461   1.00 19.10 ? 97  THR A O   1 
ATOM   741  C CB  . THR A 1 95  ? 3.589   27.440  8.539   1.00 22.59 ? 97  THR A CB  1 
ATOM   742  O OG1 . THR A 1 95  ? 3.975   26.255  7.841   1.00 20.93 ? 97  THR A OG1 1 
ATOM   743  C CG2 . THR A 1 95  ? 4.071   27.296  9.973   1.00 20.67 ? 97  THR A CG2 1 
ATOM   744  N N   . ILE A 1 96  ? 1.223   28.847  10.395  1.00 16.84 ? 98  ILE A N   1 
ATOM   745  C CA  . ILE A 1 96  ? 0.761   30.030  11.129  1.00 16.20 ? 98  ILE A CA  1 
ATOM   746  C C   . ILE A 1 96  ? 1.610   30.128  12.388  1.00 19.34 ? 98  ILE A C   1 
ATOM   747  O O   . ILE A 1 96  ? 1.471   29.299  13.293  1.00 18.42 ? 98  ILE A O   1 
ATOM   748  C CB  . ILE A 1 96  ? -0.739  29.956  11.474  1.00 19.27 ? 98  ILE A CB  1 
ATOM   749  C CG1 . ILE A 1 96  ? -1.604  29.778  10.207  1.00 14.88 ? 98  ILE A CG1 1 
ATOM   750  C CG2 . ILE A 1 96  ? -1.185  31.196  12.266  1.00 16.45 ? 98  ILE A CG2 1 
ATOM   751  C CD1 . ILE A 1 96  ? -3.092  29.399  10.509  1.00 15.68 ? 98  ILE A CD1 1 
ATOM   752  N N   . PHE A 1 97  ? 2.485   31.130  12.457  1.00 20.14 ? 99  PHE A N   1 
ATOM   753  C CA  . PHE A 1 97  ? 3.386   31.307  13.602  1.00 20.77 ? 99  PHE A CA  1 
ATOM   754  C C   . PHE A 1 97  ? 2.774   32.283  14.591  1.00 20.40 ? 99  PHE A C   1 
ATOM   755  O O   . PHE A 1 97  ? 2.587   33.458  14.264  1.00 21.01 ? 99  PHE A O   1 
ATOM   756  C CB  . PHE A 1 97  ? 4.740   31.854  13.156  1.00 22.15 ? 99  PHE A CB  1 
ATOM   757  C CG  . PHE A 1 97  ? 5.469   30.967  12.210  1.00 22.86 ? 99  PHE A CG  1 
ATOM   758  C CD1 . PHE A 1 97  ? 6.235   29.914  12.678  1.00 21.00 ? 99  PHE A CD1 1 
ATOM   759  C CD2 . PHE A 1 97  ? 5.350   31.154  10.837  1.00 24.57 ? 99  PHE A CD2 1 
ATOM   760  C CE1 . PHE A 1 97  ? 6.909   29.086  11.803  1.00 25.47 ? 99  PHE A CE1 1 
ATOM   761  C CE2 . PHE A 1 97  ? 6.021   30.321  9.951   1.00 23.56 ? 99  PHE A CE2 1 
ATOM   762  C CZ  . PHE A 1 97  ? 6.802   29.289  10.438  1.00 26.10 ? 99  PHE A CZ  1 
ATOM   763  N N   . PHE A 1 98  ? 2.477   31.820  15.800  1.00 19.58 ? 100 PHE A N   1 
ATOM   764  C CA  . PHE A 1 98  ? 1.948   32.712  16.822  1.00 17.64 ? 100 PHE A CA  1 
ATOM   765  C C   . PHE A 1 98  ? 3.125   33.349  17.544  1.00 22.96 ? 100 PHE A C   1 
ATOM   766  O O   . PHE A 1 98  ? 3.971   32.650  18.109  1.00 22.73 ? 100 PHE A O   1 
ATOM   767  C CB  . PHE A 1 98  ? 1.014   31.967  17.779  1.00 18.44 ? 100 PHE A CB  1 
ATOM   768  C CG  . PHE A 1 98  ? -0.270  31.554  17.128  1.00 17.26 ? 100 PHE A CG  1 
ATOM   769  C CD1 . PHE A 1 98  ? -1.340  32.443  17.039  1.00 17.34 ? 100 PHE A CD1 1 
ATOM   770  C CD2 . PHE A 1 98  ? -0.378  30.310  16.531  1.00 19.91 ? 100 PHE A CD2 1 
ATOM   771  C CE1 . PHE A 1 98  ? -2.505  32.068  16.409  1.00 17.72 ? 100 PHE A CE1 1 
ATOM   772  C CE2 . PHE A 1 98  ? -1.530  29.931  15.891  1.00 17.56 ? 100 PHE A CE2 1 
ATOM   773  C CZ  . PHE A 1 98  ? -2.603  30.813  15.830  1.00 19.67 ? 100 PHE A CZ  1 
ATOM   774  N N   . LYS A 1 99  ? 3.192   34.669  17.491  1.00 21.04 ? 101 LYS A N   1 
ATOM   775  C CA  . LYS A 1 99  ? 4.324   35.394  18.054  1.00 28.56 ? 101 LYS A CA  1 
ATOM   776  C C   . LYS A 1 99  ? 4.537   35.048  19.525  1.00 26.68 ? 101 LYS A C   1 
ATOM   777  O O   . LYS A 1 99  ? 3.600   35.070  20.336  1.00 21.19 ? 101 LYS A O   1 
ATOM   778  C CB  . LYS A 1 99  ? 4.101   36.887  17.859  1.00 25.46 ? 101 LYS A CB  1 
ATOM   779  C CG  . LYS A 1 99  ? 5.101   37.836  18.463  1.00 32.15 ? 101 LYS A CG  1 
ATOM   780  C CD  . LYS A 1 99  ? 4.270   39.040  18.864  1.00 36.11 ? 101 LYS A CD  1 
ATOM   781  C CE  . LYS A 1 99  ? 3.105   38.562  19.771  1.00 35.13 ? 101 LYS A CE  1 
ATOM   782  N NZ  . LYS A 1 99  ? 1.849   39.346  19.590  1.00 22.91 ? 101 LYS A NZ  1 
ATOM   783  N N   . ASP A 1 100 ? 5.782   34.700  19.847  1.00 24.64 ? 102 ASP A N   1 
ATOM   784  C CA  . ASP A 1 100 ? 6.180   34.311  21.198  1.00 26.02 ? 102 ASP A CA  1 
ATOM   785  C C   . ASP A 1 100 ? 5.413   33.087  21.680  1.00 27.73 ? 102 ASP A C   1 
ATOM   786  O O   . ASP A 1 100 ? 5.173   32.928  22.880  1.00 28.18 ? 102 ASP A O   1 
ATOM   787  C CB  . ASP A 1 100 ? 6.016   35.472  22.185  1.00 28.43 ? 102 ASP A CB  1 
ATOM   788  C CG  . ASP A 1 100 ? 6.850   36.693  21.799  1.00 33.27 ? 102 ASP A CG  1 
ATOM   789  O OD1 . ASP A 1 100 ? 7.995   36.525  21.334  1.00 32.36 ? 102 ASP A OD1 1 
ATOM   790  O OD2 . ASP A 1 100 ? 6.361   37.823  21.965  1.00 35.51 ? 102 ASP A OD2 1 
ATOM   791  N N   . ASP A 1 101 ? 5.043   32.202  20.757  1.00 22.70 ? 103 ASP A N   1 
ATOM   792  C CA  . ASP A 1 101 ? 4.289   30.996  21.096  1.00 23.39 ? 103 ASP A CA  1 
ATOM   793  C C   . ASP A 1 101 ? 4.505   29.961  19.986  1.00 22.14 ? 103 ASP A C   1 
ATOM   794  O O   . ASP A 1 101 ? 5.491   30.029  19.242  1.00 24.38 ? 103 ASP A O   1 
ATOM   795  C CB  . ASP A 1 101 ? 2.808   31.342  21.316  1.00 25.79 ? 103 ASP A CB  1 
ATOM   796  C CG  . ASP A 1 101 ? 2.150   30.453  22.353  1.00 24.25 ? 103 ASP A CG  1 
ATOM   797  O OD1 . ASP A 1 101 ? 2.591   29.297  22.487  1.00 23.55 ? 103 ASP A OD1 1 
ATOM   798  O OD2 . ASP A 1 101 ? 1.175   30.893  22.997  1.00 25.48 ? 103 ASP A OD2 1 
ATOM   799  N N   . GLY A 1 102 ? 3.597   28.992  19.885  1.00 22.53 ? 104 GLY A N   1 
ATOM   800  C CA  . GLY A 1 102 ? 3.763   27.889  18.966  1.00 20.95 ? 104 GLY A CA  1 
ATOM   801  C C   . GLY A 1 102 ? 3.307   28.237  17.560  1.00 19.99 ? 104 GLY A C   1 
ATOM   802  O O   . GLY A 1 102 ? 3.064   29.393  17.219  1.00 20.85 ? 104 GLY A O   1 
ATOM   803  N N   . ASN A 1 103 ? 3.194   27.202  16.725  1.00 18.92 ? 105 ASN A N   1 
ATOM   804  C CA  . ASN A 1 103 ? 2.731   27.387  15.355  1.00 20.27 ? 105 ASN A CA  1 
ATOM   805  C C   . ASN A 1 103 ? 1.789   26.262  14.954  1.00 21.60 ? 105 ASN A C   1 
ATOM   806  O O   . ASN A 1 103 ? 1.877   25.141  15.459  1.00 17.09 ? 105 ASN A O   1 
ATOM   807  C CB  . ASN A 1 103 ? 3.910   27.503  14.370  1.00 17.34 ? 105 ASN A CB  1 
ATOM   808  C CG  . ASN A 1 103 ? 4.745   26.216  14.260  1.00 20.12 ? 105 ASN A CG  1 
ATOM   809  O OD1 . ASN A 1 103 ? 4.378   25.259  13.572  1.00 22.59 ? 105 ASN A OD1 1 
ATOM   810  N ND2 . ASN A 1 103 ? 5.861   26.194  14.969  1.00 24.55 ? 105 ASN A ND2 1 
ATOM   811  N N   . TYR A 1 104 ? 0.851   26.594  14.065  1.00 14.86 ? 106 TYR A N   1 
ATOM   812  C CA  . TYR A 1 104 ? -0.008  25.611  13.417  1.00 17.95 ? 106 TYR A CA  1 
ATOM   813  C C   . TYR A 1 104 ? 0.579   25.287  12.052  1.00 20.22 ? 106 TYR A C   1 
ATOM   814  O O   . TYR A 1 104 ? 1.054   26.181  11.348  1.00 17.60 ? 106 TYR A O   1 
ATOM   815  C CB  . TYR A 1 104 ? -1.430  26.139  13.181  1.00 16.18 ? 106 TYR A CB  1 
ATOM   816  C CG  . TYR A 1 104 ? -2.297  26.463  14.390  1.00 16.10 ? 106 TYR A CG  1 
ATOM   817  C CD1 . TYR A 1 104 ? -1.974  26.015  15.667  1.00 17.00 ? 106 TYR A CD1 1 
ATOM   818  C CD2 . TYR A 1 104 ? -3.413  27.272  14.237  1.00 15.65 ? 106 TYR A CD2 1 
ATOM   819  C CE1 . TYR A 1 104 ? -2.776  26.326  16.766  1.00 15.60 ? 106 TYR A CE1 1 
ATOM   820  C CE2 . TYR A 1 104 ? -4.214  27.603  15.309  1.00 16.88 ? 106 TYR A CE2 1 
ATOM   821  C CZ  . TYR A 1 104 ? -3.894  27.138  16.571  1.00 17.02 ? 106 TYR A CZ  1 
ATOM   822  O OH  . TYR A 1 104 ? -4.683  27.455  17.632  1.00 19.66 ? 106 TYR A OH  1 
ATOM   823  N N   . LYS A 1 105 ? 0.489   24.025  11.653  1.00 20.01 ? 107 LYS A N   1 
ATOM   824  C CA  . LYS A 1 105 ? 0.728   23.633  10.273  1.00 17.68 ? 107 LYS A CA  1 
ATOM   825  C C   . LYS A 1 105 ? -0.569  23.021  9.780   1.00 19.86 ? 107 LYS A C   1 
ATOM   826  O O   . LYS A 1 105 ? -1.121  22.132  10.438  1.00 16.74 ? 107 LYS A O   1 
ATOM   827  C CB  . LYS A 1 105 ? 1.873   22.623  10.179  1.00 19.22 ? 107 LYS A CB  1 
ATOM   828  C CG  . LYS A 1 105 ? 3.212   23.230  10.458  1.00 26.07 ? 107 LYS A CG  1 
ATOM   829  C CD  . LYS A 1 105 ? 4.142   22.180  11.078  1.00 34.52 ? 107 LYS A CD  1 
ATOM   830  C CE  . LYS A 1 105 ? 3.613   21.638  12.447  1.00 33.35 ? 107 LYS A CE  1 
ATOM   831  N NZ  . LYS A 1 105 ? 3.125   22.632  13.493  1.00 19.07 ? 107 LYS A NZ  1 
ATOM   832  N N   . THR A 1 106 ? -1.090  23.512  8.655   1.00 16.08 ? 108 THR A N   1 
ATOM   833  C CA  . THR A 1 106 ? -2.376  23.017  8.193   1.00 14.93 ? 108 THR A CA  1 
ATOM   834  C C   . THR A 1 106 ? -2.254  22.547  6.758   1.00 16.82 ? 108 THR A C   1 
ATOM   835  O O   . THR A 1 106 ? -1.511  23.134  5.970   1.00 17.04 ? 108 THR A O   1 
ATOM   836  C CB  . THR A 1 106 ? -3.481  24.088  8.285   1.00 16.89 ? 108 THR A CB  1 
ATOM   837  O OG1 . THR A 1 106 ? -3.198  25.162  7.384   1.00 15.70 ? 108 THR A OG1 1 
ATOM   838  C CG2 . THR A 1 106 ? -3.538  24.658  9.672   1.00 14.61 ? 108 THR A CG2 1 
ATOM   839  N N   . ARG A 1 107 ? -2.989  21.487  6.435   1.00 18.03 ? 109 ARG A N   1 
ATOM   840  C CA  . ARG A 1 107 ? -3.127  20.989  5.071   1.00 18.86 ? 109 ARG A CA  1 
ATOM   841  C C   . ARG A 1 107 ? -4.596  20.693  4.842   1.00 20.53 ? 109 ARG A C   1 
ATOM   842  O O   . ARG A 1 107 ? -5.216  19.980  5.637   1.00 20.33 ? 109 ARG A O   1 
ATOM   843  C CB  . ARG A 1 107 ? -2.278  19.726  4.831   1.00 18.51 ? 109 ARG A CB  1 
ATOM   844  C CG  . ARG A 1 107 ? -2.161  19.376  3.342   1.00 22.40 ? 109 ARG A CG  1 
ATOM   845  C CD  . ARG A 1 107 ? -1.241  18.180  3.113   1.00 26.07 ? 109 ARG A CD  1 
ATOM   846  N NE  . ARG A 1 107 ? -1.163  17.805  1.706   1.00 23.47 ? 109 ARG A NE  1 
ATOM   847  C CZ  . ARG A 1 107 ? -2.088  17.126  1.044   1.00 25.57 ? 109 ARG A CZ  1 
ATOM   848  N NH1 . ARG A 1 107 ? -3.209  16.735  1.623   1.00 26.30 ? 109 ARG A NH1 1 
ATOM   849  N NH2 . ARG A 1 107 ? -1.887  16.848  -0.240  1.00 29.42 ? 109 ARG A NH2 1 
ATOM   850  N N   . ALA A 1 108 ? -5.162  21.245  3.774   1.00 16.87 ? 110 ALA A N   1 
ATOM   851  C CA  . ALA A 1 108 ? -6.585  21.088  3.524   1.00 18.65 ? 110 ALA A CA  1 
ATOM   852  C C   . ALA A 1 108 ? -6.808  20.799  2.052   1.00 19.29 ? 110 ALA A C   1 
ATOM   853  O O   . ALA A 1 108 ? -6.053  21.263  1.201   1.00 18.10 ? 110 ALA A O   1 
ATOM   854  C CB  . ALA A 1 108 ? -7.378  22.343  3.926   1.00 17.39 ? 110 ALA A CB  1 
ATOM   855  N N   . GLU A 1 109 ? -7.845  20.019  1.758   1.00 21.31 ? 111 GLU A N   1 
ATOM   856  C CA  . GLU A 1 109 ? -8.357  19.890  0.401   1.00 24.62 ? 111 GLU A CA  1 
ATOM   857  C C   . GLU A 1 109 ? -9.703  20.584  0.342   1.00 21.61 ? 111 GLU A C   1 
ATOM   858  O O   . GLU A 1 109 ? -10.584 20.320  1.173   1.00 22.93 ? 111 GLU A O   1 
ATOM   859  C CB  . GLU A 1 109 ? -8.487  18.428  -0.027  1.00 26.85 ? 111 GLU A CB  1 
ATOM   860  C CG  . GLU A 1 109 ? -7.321  17.577  0.372   1.00 28.86 ? 111 GLU A CG  1 
ATOM   861  C CD  . GLU A 1 109 ? -7.082  16.446  -0.586  1.00 34.12 ? 111 GLU A CD  1 
ATOM   862  O OE1 . GLU A 1 109 ? -8.081  15.893  -1.088  1.00 32.77 ? 111 GLU A OE1 1 
ATOM   863  O OE2 . GLU A 1 109 ? -5.905  16.081  -0.791  1.00 39.35 ? 111 GLU A OE2 1 
ATOM   864  N N   . VAL A 1 110 ? -9.845  21.494  -0.613  1.00 21.27 ? 112 VAL A N   1 
ATOM   865  C CA  . VAL A 1 110 ? -11.087 22.202  -0.868  1.00 20.21 ? 112 VAL A CA  1 
ATOM   866  C C   . VAL A 1 110 ? -11.574 21.732  -2.233  1.00 20.63 ? 112 VAL A C   1 
ATOM   867  O O   . VAL A 1 110 ? -10.864 21.893  -3.226  1.00 20.17 ? 112 VAL A O   1 
ATOM   868  C CB  . VAL A 1 110 ? -10.891 23.727  -0.844  1.00 20.86 ? 112 VAL A CB  1 
ATOM   869  C CG1 . VAL A 1 110 ? -12.233 24.441  -1.052  1.00 21.08 ? 112 VAL A CG1 1 
ATOM   870  C CG2 . VAL A 1 110 ? -10.229 24.176  0.479   1.00 18.59 ? 112 VAL A CG2 1 
ATOM   871  N N   . LYS A 1 111 ? -12.751 21.121  -2.276  1.00 24.48 ? 113 LYS A N   1 
ATOM   872  C CA  . LYS A 1 111 ? -13.236 20.510  -3.512  1.00 23.61 ? 113 LYS A CA  1 
ATOM   873  C C   . LYS A 1 111 ? -14.722 20.264  -3.373  1.00 25.58 ? 113 LYS A C   1 
ATOM   874  O O   . LYS A 1 111 ? -15.267 20.251  -2.270  1.00 26.07 ? 113 LYS A O   1 
ATOM   875  C CB  . LYS A 1 111 ? -12.533 19.185  -3.836  1.00 26.35 ? 113 LYS A CB  1 
ATOM   876  C CG  . LYS A 1 111 ? -12.329 18.255  -2.642  1.00 30.90 ? 113 LYS A CG  1 
ATOM   877  C CD  . LYS A 1 111 ? -11.711 16.920  -3.102  1.00 35.27 ? 113 LYS A CD  1 
ATOM   878  C CE  . LYS A 1 111 ? -12.059 15.759  -2.172  1.00 40.07 ? 113 LYS A CE  1 
ATOM   879  N NZ  . LYS A 1 111 ? -11.815 16.087  -0.735  1.00 40.87 ? 113 LYS A NZ  1 
ATOM   880  N N   . PHE A 1 112 ? -15.372 20.061  -4.510  1.00 23.80 ? 114 PHE A N   1 
ATOM   881  C CA  . PHE A 1 112 ? -16.776 19.712  -4.503  1.00 25.67 ? 114 PHE A CA  1 
ATOM   882  C C   . PHE A 1 112 ? -16.923 18.214  -4.268  1.00 26.56 ? 114 PHE A C   1 
ATOM   883  O O   . PHE A 1 112 ? -16.209 17.408  -4.872  1.00 29.52 ? 114 PHE A O   1 
ATOM   884  C CB  . PHE A 1 112 ? -17.422 20.131  -5.824  1.00 27.43 ? 114 PHE A CB  1 
ATOM   885  C CG  . PHE A 1 112 ? -17.964 21.531  -5.801  1.00 25.11 ? 114 PHE A CG  1 
ATOM   886  C CD1 . PHE A 1 112 ? -19.230 21.788  -5.298  1.00 26.50 ? 114 PHE A CD1 1 
ATOM   887  C CD2 . PHE A 1 112 ? -17.200 22.596  -6.256  1.00 25.84 ? 114 PHE A CD2 1 
ATOM   888  C CE1 . PHE A 1 112 ? -19.739 23.071  -5.268  1.00 22.99 ? 114 PHE A CE1 1 
ATOM   889  C CE2 . PHE A 1 112 ? -17.705 23.894  -6.222  1.00 23.50 ? 114 PHE A CE2 1 
ATOM   890  C CZ  . PHE A 1 112 ? -18.971 24.128  -5.728  1.00 25.77 ? 114 PHE A CZ  1 
ATOM   891  N N   . GLU A 1 113 ? -17.810 17.853  -3.347  1.00 27.83 ? 115 GLU A N   1 
ATOM   892  C CA  . GLU A 1 113 ? -18.275 16.484  -3.150  1.00 28.50 ? 115 GLU A CA  1 
ATOM   893  C C   . GLU A 1 113 ? -19.753 16.544  -3.519  1.00 29.93 ? 115 GLU A C   1 
ATOM   894  O O   . GLU A 1 113 ? -20.605 16.904  -2.705  1.00 28.12 ? 115 GLU A O   1 
ATOM   895  C CB  . GLU A 1 113 ? -18.033 15.992  -1.709  1.00 29.72 ? 115 GLU A CB  1 
ATOM   896  C CG  . GLU A 1 113 ? -16.646 15.393  -1.502  1.00 32.88 ? 115 GLU A CG  1 
ATOM   897  C CD  . GLU A 1 113 ? -16.221 15.331  -0.039  1.00 38.79 ? 115 GLU A CD  1 
ATOM   898  O OE1 . GLU A 1 113 ? -17.107 15.263  0.847   1.00 42.36 ? 115 GLU A OE1 1 
ATOM   899  O OE2 . GLU A 1 113 ? -14.997 15.348  0.230   1.00 42.33 ? 115 GLU A OE2 1 
ATOM   900  N N   . GLY A 1 114 ? -20.057 16.253  -4.776  1.00 33.64 ? 116 GLY A N   1 
ATOM   901  C CA  . GLY A 1 114 ? -21.418 16.462  -5.231  1.00 30.84 ? 116 GLY A CA  1 
ATOM   902  C C   . GLY A 1 114 ? -21.701 17.941  -5.319  1.00 29.55 ? 116 GLY A C   1 
ATOM   903  O O   . GLY A 1 114 ? -20.923 18.712  -5.889  1.00 34.03 ? 116 GLY A O   1 
ATOM   904  N N   . ASP A 1 115 ? -22.820 18.355  -4.742  1.00 28.59 ? 117 ASP A N   1 
ATOM   905  C CA  . ASP A 1 115 ? -23.203 19.758  -4.760  1.00 33.33 ? 117 ASP A CA  1 
ATOM   906  C C   . ASP A 1 115 ? -22.660 20.531  -3.567  1.00 29.15 ? 117 ASP A C   1 
ATOM   907  O O   . ASP A 1 115 ? -22.978 21.715  -3.423  1.00 28.01 ? 117 ASP A O   1 
ATOM   908  C CB  . ASP A 1 115 ? -24.725 19.874  -4.786  1.00 32.74 ? 117 ASP A CB  1 
ATOM   909  C CG  . ASP A 1 115 ? -25.306 19.598  -6.163  1.00 36.53 ? 117 ASP A CG  1 
ATOM   910  O OD1 . ASP A 1 115 ? -24.527 19.432  -7.131  1.00 38.15 ? 117 ASP A OD1 1 
ATOM   911  O OD2 . ASP A 1 115 ? -26.547 19.517  -6.263  1.00 41.49 ? 117 ASP A OD2 1 
ATOM   912  N N   . THR A 1 116 ? -21.874 19.887  -2.710  1.00 30.39 ? 118 THR A N   1 
ATOM   913  C CA  . THR A 1 116 ? -21.373 20.485  -1.474  1.00 27.67 ? 118 THR A CA  1 
ATOM   914  C C   . THR A 1 116 ? -19.914 20.881  -1.667  1.00 26.20 ? 118 THR A C   1 
ATOM   915  O O   . THR A 1 116 ? -19.116 20.091  -2.180  1.00 23.06 ? 118 THR A O   1 
ATOM   916  C CB  . THR A 1 116 ? -21.484 19.502  -0.304  1.00 30.32 ? 118 THR A CB  1 
ATOM   917  O OG1 . THR A 1 116 ? -22.854 19.138  -0.083  1.00 31.42 ? 118 THR A OG1 1 
ATOM   918  C CG2 . THR A 1 116 ? -20.930 20.130  0.985   1.00 27.83 ? 118 THR A CG2 1 
ATOM   919  N N   . LEU A 1 117 ? -19.567 22.102  -1.255  1.00 26.31 ? 119 LEU A N   1 
ATOM   920  C CA  . LEU A 1 117 ? -18.174 22.534  -1.210  1.00 23.98 ? 119 LEU A CA  1 
ATOM   921  C C   . LEU A 1 117 ? -17.588 22.089  0.128   1.00 23.51 ? 119 LEU A C   1 
ATOM   922  O O   . LEU A 1 117 ? -18.056 22.523  1.182   1.00 23.08 ? 119 LEU A O   1 
ATOM   923  C CB  . LEU A 1 117 ? -18.072 24.053  -1.393  1.00 23.60 ? 119 LEU A CB  1 
ATOM   924  C CG  . LEU A 1 117 ? -16.685 24.700  -1.593  1.00 21.44 ? 119 LEU A CG  1 
ATOM   925  C CD1 . LEU A 1 117 ? -15.959 24.886  -0.239  1.00 19.50 ? 119 LEU A CD1 1 
ATOM   926  C CD2 . LEU A 1 117 ? -15.828 23.884  -2.555  1.00 20.68 ? 119 LEU A CD2 1 
ATOM   927  N N   . VAL A 1 118 ? -16.571 21.223  0.084   1.00 23.74 ? 120 VAL A N   1 
ATOM   928  C CA  . VAL A 1 118 ? -16.006 20.594  1.274   1.00 22.78 ? 120 VAL A CA  1 
ATOM   929  C C   . VAL A 1 118 ? -14.589 21.103  1.500   1.00 23.44 ? 120 VAL A C   1 
ATOM   930  O O   . VAL A 1 118 ? -13.788 21.175  0.562   1.00 23.01 ? 120 VAL A O   1 
ATOM   931  C CB  . VAL A 1 118 ? -16.013 19.060  1.145   1.00 27.96 ? 120 VAL A CB  1 
ATOM   932  C CG1 . VAL A 1 118 ? -15.541 18.427  2.425   1.00 29.97 ? 120 VAL A CG1 1 
ATOM   933  C CG2 . VAL A 1 118 ? -17.433 18.586  0.865   1.00 26.16 ? 120 VAL A CG2 1 
ATOM   934  N N   . ASN A 1 119 ? -14.286 21.437  2.755   1.00 21.96 ? 121 ASN A N   1 
ATOM   935  C CA  . ASN A 1 119 ? -12.965 21.876  3.197   1.00 17.31 ? 121 ASN A CA  1 
ATOM   936  C C   . ASN A 1 119 ? -12.551 20.874  4.270   1.00 19.23 ? 121 ASN A C   1 
ATOM   937  O O   . ASN A 1 119 ? -13.090 20.891  5.379   1.00 19.20 ? 121 ASN A O   1 
ATOM   938  C CB  . ASN A 1 119 ? -13.023 23.312  3.740   1.00 20.30 ? 121 ASN A CB  1 
ATOM   939  C CG  . ASN A 1 119 ? -11.667 23.835  4.208   1.00 16.10 ? 121 ASN A CG  1 
ATOM   940  O OD1 . ASN A 1 119 ? -10.621 23.319  3.825   1.00 17.95 ? 121 ASN A OD1 1 
ATOM   941  N ND2 . ASN A 1 119 ? -11.688 24.896  5.014   1.00 14.57 ? 121 ASN A ND2 1 
ATOM   942  N N   . ARG A 1 120 ? -11.623 19.986  3.940   1.00 19.63 ? 122 ARG A N   1 
ATOM   943  C CA  . ARG A 1 120 ? -11.177 18.938  4.854   1.00 23.91 ? 122 ARG A CA  1 
ATOM   944  C C   . ARG A 1 120 ? -9.740  19.217  5.255   1.00 20.83 ? 122 ARG A C   1 
ATOM   945  O O   . ARG A 1 120 ? -8.853  19.243  4.395   1.00 20.84 ? 122 ARG A O   1 
ATOM   946  C CB  . ARG A 1 120 ? -11.296 17.554  4.213   1.00 23.78 ? 122 ARG A CB  1 
ATOM   947  C CG  . ARG A 1 120 ? -12.734 17.154  4.029   1.00 27.84 ? 122 ARG A CG  1 
ATOM   948  C CD  . ARG A 1 120 ? -12.908 15.730  3.526   1.00 36.52 ? 122 ARG A CD  1 
ATOM   949  N NE  . ARG A 1 120 ? -14.297 15.521  3.145   1.00 38.59 ? 122 ARG A NE  1 
ATOM   950  C CZ  . ARG A 1 120 ? -15.245 15.123  3.983   1.00 41.01 ? 122 ARG A CZ  1 
ATOM   951  N NH1 . ARG A 1 120 ? -14.987 14.904  5.263   1.00 38.45 ? 122 ARG A NH1 1 
ATOM   952  N NH2 . ARG A 1 120 ? -16.491 14.979  3.535   1.00 40.25 ? 122 ARG A NH2 1 
ATOM   953  N N   . ILE A 1 121 ? -9.514  19.389  6.558   1.00 22.34 ? 123 ILE A N   1 
ATOM   954  C CA  . ILE A 1 121 ? -8.296  19.985  7.089   1.00 21.26 ? 123 ILE A CA  1 
ATOM   955  C C   . ILE A 1 121 ? -7.653  19.043  8.088   1.00 19.40 ? 123 ILE A C   1 
ATOM   956  O O   . ILE A 1 121 ? -8.346  18.453  8.922   1.00 18.51 ? 123 ILE A O   1 
ATOM   957  C CB  . ILE A 1 121 ? -8.582  21.326  7.798   1.00 19.90 ? 123 ILE A CB  1 
ATOM   958  C CG1 . ILE A 1 121 ? -9.487  22.241  6.962   1.00 17.09 ? 123 ILE A CG1 1 
ATOM   959  C CG2 . ILE A 1 121 ? -7.271  22.004  8.235   1.00 17.29 ? 123 ILE A CG2 1 
ATOM   960  C CD1 . ILE A 1 121 ? -10.474 22.979  7.819   1.00 19.05 ? 123 ILE A CD1 1 
ATOM   961  N N   . GLU A 1 122 ? -6.324  18.948  8.034   1.00 18.78 ? 124 GLU A N   1 
ATOM   962  C CA  . GLU A 1 122 ? -5.512  18.469  9.146   1.00 20.31 ? 124 GLU A CA  1 
ATOM   963  C C   . GLU A 1 122 ? -4.744  19.641  9.733   1.00 17.69 ? 124 GLU A C   1 
ATOM   964  O O   . GLU A 1 122 ? -4.154  20.431  8.996   1.00 20.26 ? 124 GLU A O   1 
ATOM   965  C CB  . GLU A 1 122 ? -4.495  17.417  8.703   1.00 23.68 ? 124 GLU A CB  1 
ATOM   966  C CG  . GLU A 1 122 ? -4.842  16.675  7.450   1.00 29.57 ? 124 GLU A CG  1 
ATOM   967  C CD  . GLU A 1 122 ? -3.872  15.545  7.200   1.00 35.19 ? 124 GLU A CD  1 
ATOM   968  O OE1 . GLU A 1 122 ? -4.321  14.465  6.759   1.00 46.28 ? 124 GLU A OE1 1 
ATOM   969  O OE2 . GLU A 1 122 ? -2.662  15.742  7.441   1.00 37.87 ? 124 GLU A OE2 1 
ATOM   970  N N   . LEU A 1 123 ? -4.690  19.716  11.055  1.00 17.05 ? 125 LEU A N   1 
ATOM   971  C CA  . LEU A 1 123 ? -3.987  20.787  11.744  1.00 14.97 ? 125 LEU A CA  1 
ATOM   972  C C   . LEU A 1 123 ? -3.103  20.201  12.833  1.00 19.55 ? 125 LEU A C   1 
ATOM   973  O O   . LEU A 1 123 ? -3.562  19.391  13.646  1.00 17.49 ? 125 LEU A O   1 
ATOM   974  C CB  . LEU A 1 123 ? -4.971  21.790  12.353  1.00 13.98 ? 125 LEU A CB  1 
ATOM   975  C CG  . LEU A 1 123 ? -4.339  22.965  13.110  1.00 14.76 ? 125 LEU A CG  1 
ATOM   976  C CD1 . LEU A 1 123 ? -5.239  24.179  13.035  1.00 16.92 ? 125 LEU A CD1 1 
ATOM   977  C CD2 . LEU A 1 123 ? -4.114  22.634  14.578  1.00 16.11 ? 125 LEU A CD2 1 
ATOM   978  N N   . LYS A 1 124 ? -1.848  20.637  12.861  1.00 16.81 ? 126 LYS A N   1 
ATOM   979  C CA  . LYS A 1 124 ? -0.849  20.164  13.812  1.00 18.68 ? 126 LYS A CA  1 
ATOM   980  C C   . LYS A 1 124 ? -0.224  21.392  14.448  1.00 18.94 ? 126 LYS A C   1 
ATOM   981  O O   . LYS A 1 124 ? 0.388   22.203  13.746  1.00 18.20 ? 126 LYS A O   1 
ATOM   982  C CB  . LYS A 1 124 ? 0.217   19.317  13.104  1.00 22.44 ? 126 LYS A CB  1 
ATOM   983  C CG  . LYS A 1 124 ? 1.402   18.927  13.989  1.00 24.77 ? 126 LYS A CG  1 
ATOM   984  C CD  . LYS A 1 124 ? 0.981   17.920  15.036  1.00 24.54 ? 126 LYS A CD  1 
ATOM   985  C CE  . LYS A 1 124 ? 2.153   17.077  15.477  1.00 26.65 ? 126 LYS A CE  1 
ATOM   986  N NZ  . LYS A 1 124 ? 1.834   16.385  16.736  1.00 25.07 ? 126 LYS A NZ  1 
ATOM   987  N N   . GLY A 1 125 ? -0.389  21.542  15.761  1.00 18.32 ? 127 GLY A N   1 
ATOM   988  C CA  . GLY A 1 125 ? 0.174   22.658  16.491  1.00 17.31 ? 127 GLY A CA  1 
ATOM   989  C C   . GLY A 1 125 ? 1.259   22.160  17.435  1.00 20.93 ? 127 GLY A C   1 
ATOM   990  O O   . GLY A 1 125 ? 1.043   21.214  18.198  1.00 19.99 ? 127 GLY A O   1 
ATOM   991  N N   . ILE A 1 126 ? 2.423   22.804  17.365  1.00 18.29 ? 128 ILE A N   1 
ATOM   992  C CA  . ILE A 1 126 ? 3.562   22.386  18.170  1.00 21.08 ? 128 ILE A CA  1 
ATOM   993  C C   . ILE A 1 126 ? 4.145   23.583  18.900  1.00 20.65 ? 128 ILE A C   1 
ATOM   994  O O   . ILE A 1 126 ? 3.960   24.736  18.507  1.00 21.57 ? 128 ILE A O   1 
ATOM   995  C CB  . ILE A 1 126 ? 4.662   21.698  17.332  1.00 22.88 ? 128 ILE A CB  1 
ATOM   996  C CG1 . ILE A 1 126 ? 5.435   22.725  16.492  1.00 24.79 ? 128 ILE A CG1 1 
ATOM   997  C CG2 . ILE A 1 126 ? 4.061   20.613  16.454  1.00 21.50 ? 128 ILE A CG2 1 
ATOM   998  C CD1 . ILE A 1 126 ? 6.390   22.106  15.503  1.00 26.94 ? 128 ILE A CD1 1 
ATOM   999  N N   . ASP A 1 127 ? 4.829   23.280  20.009  1.00 23.12 ? 129 ASP A N   1 
ATOM   1000 C CA  . ASP A 1 127 ? 5.659   24.230  20.762  1.00 23.63 ? 129 ASP A CA  1 
ATOM   1001 C C   . ASP A 1 127 ? 4.866   25.387  21.352  1.00 23.74 ? 129 ASP A C   1 
ATOM   1002 O O   . ASP A 1 127 ? 5.355   26.512  21.442  1.00 25.11 ? 129 ASP A O   1 
ATOM   1003 C CB  . ASP A 1 127 ? 6.814   24.759  19.914  1.00 29.62 ? 129 ASP A CB  1 
ATOM   1004 C CG  . ASP A 1 127 ? 7.723   23.656  19.427  1.00 34.45 ? 129 ASP A CG  1 
ATOM   1005 O OD1 . ASP A 1 127 ? 7.819   22.630  20.131  1.00 33.59 ? 129 ASP A OD1 1 
ATOM   1006 O OD2 . ASP A 1 127 ? 8.355   23.824  18.368  1.00 40.48 ? 129 ASP A OD2 1 
ATOM   1007 N N   . PHE A 1 128 ? 3.650   25.113  21.794  1.00 23.07 ? 130 PHE A N   1 
ATOM   1008 C CA  . PHE A 1 128 ? 2.869   26.160  22.423  1.00 23.10 ? 130 PHE A CA  1 
ATOM   1009 C C   . PHE A 1 128 ? 3.189   26.229  23.905  1.00 24.86 ? 130 PHE A C   1 
ATOM   1010 O O   . PHE A 1 128 ? 3.558   25.228  24.526  1.00 27.07 ? 130 PHE A O   1 
ATOM   1011 C CB  . PHE A 1 128 ? 1.375   25.919  22.220  1.00 22.48 ? 130 PHE A CB  1 
ATOM   1012 C CG  . PHE A 1 128 ? 0.900   26.341  20.864  1.00 21.03 ? 130 PHE A CG  1 
ATOM   1013 C CD1 . PHE A 1 128 ? 0.469   27.638  20.629  1.00 19.53 ? 130 PHE A CD1 1 
ATOM   1014 C CD2 . PHE A 1 128 ? 0.963   25.456  19.814  1.00 16.62 ? 130 PHE A CD2 1 
ATOM   1015 C CE1 . PHE A 1 128 ? 0.073   28.031  19.368  1.00 19.08 ? 130 PHE A CE1 1 
ATOM   1016 C CE2 . PHE A 1 128 ? 0.561   25.841  18.538  1.00 19.61 ? 130 PHE A CE2 1 
ATOM   1017 C CZ  . PHE A 1 128 ? 0.105   27.141  18.331  1.00 18.78 ? 130 PHE A CZ  1 
ATOM   1018 N N   . LYS A 1 129 ? 3.058   27.426  24.458  1.00 25.83 ? 131 LYS A N   1 
ATOM   1019 C CA  . LYS A 1 129 ? 3.144   27.616  25.900  1.00 26.32 ? 131 LYS A CA  1 
ATOM   1020 C C   . LYS A 1 129 ? 1.825   27.194  26.535  1.00 29.12 ? 131 LYS A C   1 
ATOM   1021 O O   . LYS A 1 129 ? 0.755   27.690  26.158  1.00 26.05 ? 131 LYS A O   1 
ATOM   1022 C CB  . LYS A 1 129 ? 3.481   29.067  26.235  1.00 27.96 ? 131 LYS A CB  1 
ATOM   1023 C CG  . LYS A 1 129 ? 4.821   29.556  25.643  1.00 29.45 ? 131 LYS A CG  1 
ATOM   1024 C CD  . LYS A 1 129 ? 5.008   31.066  25.777  1.00 29.72 ? 131 LYS A CD  1 
ATOM   1025 C CE  . LYS A 1 129 ? 6.429   31.493  25.365  1.00 32.05 ? 131 LYS A CE  1 
ATOM   1026 N N   . GLU A 1 130 ? 1.896   26.268  27.491  1.00 26.90 ? 132 GLU A N   1 
ATOM   1027 C CA  . GLU A 1 130 ? 0.678   25.805  28.144  1.00 29.56 ? 132 GLU A CA  1 
ATOM   1028 C C   . GLU A 1 130 ? -0.086  26.937  28.822  1.00 28.44 ? 132 GLU A C   1 
ATOM   1029 O O   . GLU A 1 130 ? -1.313  26.860  28.933  1.00 31.80 ? 132 GLU A O   1 
ATOM   1030 C CB  . GLU A 1 130 ? 1.011   24.686  29.129  1.00 32.15 ? 132 GLU A CB  1 
ATOM   1031 C CG  . GLU A 1 130 ? -0.007  23.559  29.091  1.00 38.27 ? 132 GLU A CG  1 
ATOM   1032 C CD  . GLU A 1 130 ? 0.144   22.671  27.879  1.00 32.48 ? 132 GLU A CD  1 
ATOM   1033 O OE1 . GLU A 1 130 ? 1.282   22.365  27.496  1.00 34.97 ? 132 GLU A OE1 1 
ATOM   1034 O OE2 . GLU A 1 130 ? -0.895  22.270  27.302  1.00 41.34 ? 132 GLU A OE2 1 
ATOM   1035 N N   . ASP A 1 131 ? 0.601   28.006  29.237  1.00 29.83 ? 133 ASP A N   1 
ATOM   1036 C CA  . ASP A 1 131 ? -0.048  29.139  29.884  1.00 30.76 ? 133 ASP A CA  1 
ATOM   1037 C C   . ASP A 1 131 ? -0.021  30.408  29.027  1.00 31.67 ? 133 ASP A C   1 
ATOM   1038 O O   . ASP A 1 131 ? -0.163  31.515  29.557  1.00 31.73 ? 133 ASP A O   1 
ATOM   1039 C CB  . ASP A 1 131 ? 0.592   29.400  31.253  1.00 32.73 ? 133 ASP A CB  1 
ATOM   1040 C CG  . ASP A 1 131 ? 2.107   29.578  31.186  1.00 41.16 ? 133 ASP A CG  1 
ATOM   1041 O OD1 . ASP A 1 131 ? 2.717   29.383  30.108  1.00 37.25 ? 133 ASP A OD1 1 
ATOM   1042 O OD2 . ASP A 1 131 ? 2.698   29.919  32.237  1.00 46.94 ? 133 ASP A OD2 1 
ATOM   1043 N N   . GLY A 1 132 ? 0.165   30.271  27.715  1.00 30.24 ? 134 GLY A N   1 
ATOM   1044 C CA  . GLY A 1 132 ? 0.218   31.405  26.817  1.00 26.14 ? 134 GLY A CA  1 
ATOM   1045 C C   . GLY A 1 132 ? -1.172  31.828  26.375  1.00 26.46 ? 134 GLY A C   1 
ATOM   1046 O O   . GLY A 1 132 ? -2.195  31.327  26.844  1.00 29.03 ? 134 GLY A O   1 
ATOM   1047 N N   . ASN A 1 133 ? -1.200  32.765  25.425  1.00 27.35 ? 135 ASN A N   1 
ATOM   1048 C CA  . ASN A 1 133 ? -2.472  33.344  25.024  1.00 27.06 ? 135 ASN A CA  1 
ATOM   1049 C C   . ASN A 1 133 ? -3.370  32.345  24.313  1.00 22.96 ? 135 ASN A C   1 
ATOM   1050 O O   . ASN A 1 133 ? -4.587  32.552  24.267  1.00 22.46 ? 135 ASN A O   1 
ATOM   1051 C CB  . ASN A 1 133 ? -2.218  34.553  24.134  1.00 26.65 ? 135 ASN A CB  1 
ATOM   1052 C CG  . ASN A 1 133 ? -1.603  35.699  24.901  1.00 32.42 ? 135 ASN A CG  1 
ATOM   1053 O OD1 . ASN A 1 133 ? -1.848  35.863  26.103  1.00 31.16 ? 135 ASN A OD1 1 
ATOM   1054 N ND2 . ASN A 1 133 ? -0.748  36.456  24.234  1.00 26.76 ? 135 ASN A ND2 1 
ATOM   1055 N N   . ILE A 1 134 ? -2.809  31.272  23.765  1.00 24.92 ? 136 ILE A N   1 
ATOM   1056 C CA  . ILE A 1 134 ? -3.603  30.366  22.939  1.00 22.28 ? 136 ILE A CA  1 
ATOM   1057 C C   . ILE A 1 134 ? -4.131  29.242  23.820  1.00 24.85 ? 136 ILE A C   1 
ATOM   1058 O O   . ILE A 1 134 ? -5.344  29.074  23.995  1.00 23.43 ? 136 ILE A O   1 
ATOM   1059 C CB  . ILE A 1 134 ? -2.783  29.798  21.762  1.00 22.57 ? 136 ILE A CB  1 
ATOM   1060 C CG1 . ILE A 1 134 ? -2.595  30.840  20.646  1.00 24.01 ? 136 ILE A CG1 1 
ATOM   1061 C CG2 . ILE A 1 134 ? -3.536  28.632  21.127  1.00 21.85 ? 136 ILE A CG2 1 
ATOM   1062 C CD1 . ILE A 1 134 ? -1.547  31.874  20.917  1.00 22.12 ? 136 ILE A CD1 1 
ATOM   1063 N N   . LEU A 1 135 ? -3.210  28.466  24.384  1.00 25.73 ? 137 LEU A N   1 
ATOM   1064 C CA  . LEU A 1 135 ? -3.569  27.339  25.233  1.00 26.84 ? 137 LEU A CA  1 
ATOM   1065 C C   . LEU A 1 135 ? -4.188  27.793  26.549  1.00 29.21 ? 137 LEU A C   1 
ATOM   1066 O O   . LEU A 1 135 ? -4.906  27.014  27.185  1.00 29.47 ? 137 LEU A O   1 
ATOM   1067 C CB  . LEU A 1 135 ? -2.315  26.501  25.472  1.00 25.86 ? 137 LEU A CB  1 
ATOM   1068 C CG  . LEU A 1 135 ? -1.990  25.477  24.383  1.00 27.07 ? 137 LEU A CG  1 
ATOM   1069 C CD1 . LEU A 1 135 ? -1.057  24.403  24.893  1.00 27.38 ? 137 LEU A CD1 1 
ATOM   1070 C CD2 . LEU A 1 135 ? -3.265  24.831  23.859  1.00 27.09 ? 137 LEU A CD2 1 
ATOM   1071 N N   . GLY A 1 136 ? -3.934  29.030  26.968  1.00 26.81 ? 138 GLY A N   1 
ATOM   1072 C CA  . GLY A 1 136 ? -4.539  29.591  28.157  1.00 30.59 ? 138 GLY A CA  1 
ATOM   1073 C C   . GLY A 1 136 ? -5.825  30.355  27.929  1.00 32.38 ? 138 GLY A C   1 
ATOM   1074 O O   . GLY A 1 136 ? -6.351  30.940  28.884  1.00 30.61 ? 138 GLY A O   1 
ATOM   1075 N N   . HIS A 1 137 ? -6.342  30.373  26.693  1.00 27.90 ? 139 HIS A N   1 
ATOM   1076 C CA  . HIS A 1 137 ? -7.643  30.961  26.373  1.00 28.12 ? 139 HIS A CA  1 
ATOM   1077 C C   . HIS A 1 137 ? -7.713  32.417  26.823  1.00 30.81 ? 139 HIS A C   1 
ATOM   1078 O O   . HIS A 1 137 ? -8.635  32.825  27.528  1.00 31.62 ? 139 HIS A O   1 
ATOM   1079 C CB  . HIS A 1 137 ? -8.779  30.151  27.005  1.00 30.72 ? 139 HIS A CB  1 
ATOM   1080 C CG  . HIS A 1 137 ? -8.967  28.786  26.418  1.00 32.93 ? 139 HIS A CG  1 
ATOM   1081 N ND1 . HIS A 1 137 ? -9.753  28.556  25.308  1.00 29.91 ? 139 HIS A ND1 1 
ATOM   1082 C CD2 . HIS A 1 137 ? -8.453  27.584  26.771  1.00 29.81 ? 139 HIS A CD2 1 
ATOM   1083 C CE1 . HIS A 1 137 ? -9.732  27.267  25.017  1.00 27.49 ? 139 HIS A CE1 1 
ATOM   1084 N NE2 . HIS A 1 137 ? -8.947  26.657  25.885  1.00 28.74 ? 139 HIS A NE2 1 
ATOM   1085 N N   . LYS A 1 138 ? -6.730  33.210  26.389  1.00 29.05 ? 140 LYS A N   1 
ATOM   1086 C CA  . LYS A 1 138 ? -6.606  34.602  26.802  1.00 25.46 ? 140 LYS A CA  1 
ATOM   1087 C C   . LYS A 1 138 ? -6.991  35.571  25.689  1.00 33.21 ? 140 LYS A C   1 
ATOM   1088 O O   . LYS A 1 138 ? -6.797  36.785  25.833  1.00 31.98 ? 140 LYS A O   1 
ATOM   1089 C CB  . LYS A 1 138 ? -5.184  34.870  27.274  1.00 28.35 ? 140 LYS A CB  1 
ATOM   1090 C CG  . LYS A 1 138 ? -4.929  34.374  28.687  1.00 28.55 ? 140 LYS A CG  1 
ATOM   1091 C CD  . LYS A 1 138 ? -3.582  34.851  29.222  1.00 33.24 ? 140 LYS A CD  1 
ATOM   1092 C CE  . LYS A 1 138 ? -2.473  33.845  29.024  1.00 37.33 ? 140 LYS A CE  1 
ATOM   1093 N NZ  . LYS A 1 138 ? -1.979  33.271  30.325  1.00 40.09 ? 140 LYS A NZ  1 
ATOM   1094 N N   . LEU A 1 139 ? -7.523  35.056  24.583  1.00 26.02 ? 141 LEU A N   1 
ATOM   1095 C CA  . LEU A 1 139 ? -7.896  35.836  23.412  1.00 28.75 ? 141 LEU A CA  1 
ATOM   1096 C C   . LEU A 1 139 ? -9.377  36.188  23.492  1.00 26.73 ? 141 LEU A C   1 
ATOM   1097 O O   . LEU A 1 139 ? -10.187 35.376  23.941  1.00 29.39 ? 141 LEU A O   1 
ATOM   1098 C CB  . LEU A 1 139 ? -7.612  35.040  22.131  1.00 23.15 ? 141 LEU A CB  1 
ATOM   1099 C CG  . LEU A 1 139 ? -6.126  34.781  21.874  1.00 23.23 ? 141 LEU A CG  1 
ATOM   1100 C CD1 . LEU A 1 139 ? -5.911  34.079  20.541  1.00 22.13 ? 141 LEU A CD1 1 
ATOM   1101 C CD2 . LEU A 1 139 ? -5.307  36.055  21.958  1.00 19.88 ? 141 LEU A CD2 1 
ATOM   1102 N N   . GLU A 1 140 ? -9.725  37.405  23.071  1.00 29.54 ? 142 GLU A N   1 
ATOM   1103 C CA  . GLU A 1 140 ? -11.122 37.815  23.068  1.00 28.39 ? 142 GLU A CA  1 
ATOM   1104 C C   . GLU A 1 140 ? -11.878 37.095  21.961  1.00 29.49 ? 142 GLU A C   1 
ATOM   1105 O O   . GLU A 1 140 ? -11.307 36.724  20.933  1.00 26.11 ? 142 GLU A O   1 
ATOM   1106 C CB  . GLU A 1 140 ? -11.260 39.321  22.856  1.00 31.54 ? 142 GLU A CB  1 
ATOM   1107 C CG  . GLU A 1 140 ? -10.759 40.205  23.992  1.00 30.37 ? 142 GLU A CG  1 
ATOM   1108 C CD  . GLU A 1 140 ? -10.971 41.681  23.693  1.00 33.86 ? 142 GLU A CD  1 
ATOM   1109 O OE1 . GLU A 1 140 ? -11.540 42.007  22.626  1.00 34.84 ? 142 GLU A OE1 1 
ATOM   1110 O OE2 . GLU A 1 140 ? -10.608 42.519  24.546  1.00 43.11 ? 142 GLU A OE2 1 
ATOM   1111 N N   . TYR A 1 141 ? -13.181 36.906  22.173  1.00 27.57 ? 143 TYR A N   1 
ATOM   1112 C CA  . TYR A 1 141 ? -14.036 36.242  21.181  1.00 27.63 ? 143 TYR A CA  1 
ATOM   1113 C C   . TYR A 1 141 ? -14.557 37.282  20.189  1.00 27.80 ? 143 TYR A C   1 
ATOM   1114 O O   . TYR A 1 141 ? -15.724 37.675  20.194  1.00 30.47 ? 143 TYR A O   1 
ATOM   1115 C CB  . TYR A 1 141 ? -15.175 35.493  21.867  1.00 28.76 ? 143 TYR A CB  1 
ATOM   1116 C CG  . TYR A 1 141 ? -15.992 34.609  20.938  1.00 27.83 ? 143 TYR A CG  1 
ATOM   1117 C CD1 . TYR A 1 141 ? -15.484 33.398  20.486  1.00 25.70 ? 143 TYR A CD1 1 
ATOM   1118 C CD2 . TYR A 1 141 ? -17.273 34.979  20.522  1.00 29.32 ? 143 TYR A CD2 1 
ATOM   1119 C CE1 . TYR A 1 141 ? -16.225 32.572  19.639  1.00 25.88 ? 143 TYR A CE1 1 
ATOM   1120 C CE2 . TYR A 1 141 ? -18.023 34.169  19.674  1.00 28.45 ? 143 TYR A CE2 1 
ATOM   1121 C CZ  . TYR A 1 141 ? -17.487 32.960  19.238  1.00 27.25 ? 143 TYR A CZ  1 
ATOM   1122 O OH  . TYR A 1 141 ? -18.205 32.139  18.398  1.00 26.17 ? 143 TYR A OH  1 
ATOM   1123 N N   . ASN A 1 142 ? -13.643 37.725  19.327  1.00 30.96 ? 144 ASN A N   1 
ATOM   1124 C CA  . ASN A 1 142 ? -13.923 38.651  18.235  1.00 31.21 ? 144 ASN A CA  1 
ATOM   1125 C C   . ASN A 1 142 ? -12.831 38.477  17.180  1.00 28.76 ? 144 ASN A C   1 
ATOM   1126 O O   . ASN A 1 142 ? -12.041 37.527  17.238  1.00 30.89 ? 144 ASN A O   1 
ATOM   1127 C CB  . ASN A 1 142 ? -14.042 40.089  18.758  1.00 31.86 ? 144 ASN A CB  1 
ATOM   1128 C CG  . ASN A 1 142 ? -12.859 40.506  19.623  1.00 33.70 ? 144 ASN A CG  1 
ATOM   1129 O OD1 . ASN A 1 142 ? -11.709 40.116  19.382  1.00 29.39 ? 144 ASN A OD1 1 
ATOM   1130 N ND2 . ASN A 1 142 ? -13.142 41.308  20.646  1.00 35.51 ? 144 ASN A ND2 1 
ATOM   1131 N N   . TYR A 1 143 ? -12.789 39.383  16.201  1.00 29.70 ? 145 TYR A N   1 
ATOM   1132 C CA  . TYR A 1 143 ? -11.880 39.198  15.075  1.00 28.00 ? 145 TYR A CA  1 
ATOM   1133 C C   . TYR A 1 143 ? -11.475 40.528  14.454  1.00 27.25 ? 145 TYR A C   1 
ATOM   1134 O O   . TYR A 1 143 ? -12.290 41.441  14.290  1.00 28.02 ? 145 TYR A O   1 
ATOM   1135 C CB  . TYR A 1 143 ? -12.497 38.297  13.995  1.00 24.92 ? 145 TYR A CB  1 
ATOM   1136 C CG  . TYR A 1 143 ? -11.463 37.479  13.238  1.00 23.39 ? 145 TYR A CG  1 
ATOM   1137 C CD1 . TYR A 1 143 ? -10.856 36.372  13.821  1.00 21.93 ? 145 TYR A CD1 1 
ATOM   1138 C CD2 . TYR A 1 143 ? -11.093 37.827  11.949  1.00 22.07 ? 145 TYR A CD2 1 
ATOM   1139 C CE1 . TYR A 1 143 ? -9.901  35.622  13.122  1.00 20.06 ? 145 TYR A CE1 1 
ATOM   1140 C CE2 . TYR A 1 143 ? -10.153 37.104  11.251  1.00 22.99 ? 145 TYR A CE2 1 
ATOM   1141 C CZ  . TYR A 1 143 ? -9.558  36.002  11.841  1.00 22.57 ? 145 TYR A CZ  1 
ATOM   1142 O OH  . TYR A 1 143 ? -8.608  35.287  11.140  1.00 19.61 ? 145 TYR A OH  1 
ATOM   1143 N N   . ASN A 1 144 ? -10.202 40.627  14.126  1.00 25.59 ? 146 ASN A N   1 
ATOM   1144 C CA  . ASN A 1 144 ? -9.672  41.700  13.303  1.00 26.49 ? 146 ASN A CA  1 
ATOM   1145 C C   . ASN A 1 144 ? -9.269  41.053  11.988  1.00 27.67 ? 146 ASN A C   1 
ATOM   1146 O O   . ASN A 1 144 ? -8.299  40.287  11.941  1.00 23.52 ? 146 ASN A O   1 
ATOM   1147 C CB  . ASN A 1 144 ? -8.471  42.372  13.960  1.00 27.04 ? 146 ASN A CB  1 
ATOM   1148 C CG  . ASN A 1 144 ? -8.821  43.030  15.265  1.00 32.18 ? 146 ASN A CG  1 
ATOM   1149 O OD1 . ASN A 1 144 ? -9.638  43.947  15.300  1.00 35.08 ? 146 ASN A OD1 1 
ATOM   1150 N ND2 . ASN A 1 144 ? -8.181  42.586  16.352  1.00 32.18 ? 146 ASN A ND2 1 
ATOM   1151 N N   . ASP A 1 145 ? -10.019 41.328  10.928  1.00 24.23 ? 147 ASP A N   1 
ATOM   1152 C CA  . ASP A 1 145 ? -9.612  40.761  9.654   1.00 23.65 ? 147 ASP A CA  1 
ATOM   1153 C C   . ASP A 1 145 ? -8.402  41.501  9.091   1.00 25.99 ? 147 ASP A C   1 
ATOM   1154 O O   . ASP A 1 145 ? -8.046  42.596  9.526   1.00 25.71 ? 147 ASP A O   1 
ATOM   1155 C CB  . ASP A 1 145 ? -10.747 40.804  8.645   1.00 22.72 ? 147 ASP A CB  1 
ATOM   1156 C CG  . ASP A 1 145 ? -11.936 39.975  9.079   1.00 25.39 ? 147 ASP A CG  1 
ATOM   1157 O OD1 . ASP A 1 145 ? -11.944 38.748  8.779   1.00 21.18 ? 147 ASP A OD1 1 
ATOM   1158 O OD2 . ASP A 1 145 ? -12.866 40.549  9.684   1.00 25.00 ? 147 ASP A OD2 1 
ATOM   1159 N N   . HIS A 1 146 ? -7.782  40.892  8.083   1.00 21.18 ? 148 HIS A N   1 
ATOM   1160 C CA  . HIS A 1 146 ? -6.700  41.528  7.352   1.00 25.98 ? 148 HIS A CA  1 
ATOM   1161 C C   . HIS A 1 146 ? -6.815  41.127  5.890   1.00 27.02 ? 148 HIS A C   1 
ATOM   1162 O O   . HIS A 1 146 ? -7.217  39.998  5.581   1.00 21.06 ? 148 HIS A O   1 
ATOM   1163 C CB  . HIS A 1 146 ? -5.322  41.117  7.878   1.00 26.61 ? 148 HIS A CB  1 
ATOM   1164 C CG  . HIS A 1 146 ? -4.214  42.029  7.441   1.00 26.31 ? 148 HIS A CG  1 
ATOM   1165 N ND1 . HIS A 1 146 ? -3.474  41.814  6.298   1.00 26.56 ? 148 HIS A ND1 1 
ATOM   1166 C CD2 . HIS A 1 146 ? -3.676  43.121  8.033   1.00 30.63 ? 148 HIS A CD2 1 
ATOM   1167 C CE1 . HIS A 1 146 ? -2.562  42.764  6.177   1.00 27.59 ? 148 HIS A CE1 1 
ATOM   1168 N NE2 . HIS A 1 146 ? -2.657  43.563  7.224   1.00 28.61 ? 148 HIS A NE2 1 
ATOM   1169 N N   . GLN A 1 147 ? -6.433  42.049  4.997   1.00 23.83 ? 149 GLN A N   1 
ATOM   1170 C CA  . GLN A 1 147 ? -6.395  41.749  3.571   1.00 20.83 ? 149 GLN A CA  1 
ATOM   1171 C C   . GLN A 1 147 ? -5.303  40.722  3.277   1.00 23.81 ? 149 GLN A C   1 
ATOM   1172 O O   . GLN A 1 147 ? -4.318  40.593  4.007   1.00 24.93 ? 149 GLN A O   1 
ATOM   1173 C CB  . GLN A 1 147 ? -6.124  43.011  2.743   1.00 23.49 ? 149 GLN A CB  1 
ATOM   1174 C CG  . GLN A 1 147 ? -4.822  43.736  3.135   1.00 30.42 ? 149 GLN A CG  1 
ATOM   1175 C CD  . GLN A 1 147 ? -4.734  45.157  2.609   1.00 32.11 ? 149 GLN A CD  1 
ATOM   1176 O OE1 . GLN A 1 147 ? -5.721  45.882  2.596   1.00 35.32 ? 149 GLN A OE1 1 
ATOM   1177 N NE2 . GLN A 1 147 ? -3.540  45.561  2.171   1.00 31.91 ? 149 GLN A NE2 1 
ATOM   1178 N N   . VAL A 1 148 ? -5.492  39.980  2.187   1.00 22.76 ? 150 VAL A N   1 
ATOM   1179 C CA  . VAL A 1 148 ? -4.598  38.901  1.779   1.00 21.38 ? 150 VAL A CA  1 
ATOM   1180 C C   . VAL A 1 148 ? -4.175  39.161  0.342   1.00 20.09 ? 150 VAL A C   1 
ATOM   1181 O O   . VAL A 1 148 ? -5.018  39.167  -0.564  1.00 21.34 ? 150 VAL A O   1 
ATOM   1182 C CB  . VAL A 1 148 ? -5.266  37.521  1.908   1.00 22.34 ? 150 VAL A CB  1 
ATOM   1183 C CG1 . VAL A 1 148 ? -4.311  36.420  1.482   1.00 21.71 ? 150 VAL A CG1 1 
ATOM   1184 C CG2 . VAL A 1 148 ? -5.746  37.295  3.340   1.00 19.29 ? 150 VAL A CG2 1 
ATOM   1185 N N   . TYR A 1 149 ? -2.878  39.379  0.133   1.00 18.80 ? 151 TYR A N   1 
ATOM   1186 C CA  . TYR A 1 149 ? -2.338  39.640  -1.195  1.00 20.07 ? 151 TYR A CA  1 
ATOM   1187 C C   . TYR A 1 149 ? -2.032  38.313  -1.868  1.00 20.60 ? 151 TYR A C   1 
ATOM   1188 O O   . TYR A 1 149 ? -0.991  37.700  -1.616  1.00 18.67 ? 151 TYR A O   1 
ATOM   1189 C CB  . TYR A 1 149 ? -1.095  40.511  -1.099  1.00 22.31 ? 151 TYR A CB  1 
ATOM   1190 C CG  . TYR A 1 149 ? -0.650  41.089  -2.426  1.00 23.59 ? 151 TYR A CG  1 
ATOM   1191 C CD1 . TYR A 1 149 ? -1.512  41.858  -3.200  1.00 25.29 ? 151 TYR A CD1 1 
ATOM   1192 C CD2 . TYR A 1 149 ? 0.643   40.890  -2.888  1.00 24.20 ? 151 TYR A CD2 1 
ATOM   1193 C CE1 . TYR A 1 149 ? -1.088  42.393  -4.409  1.00 23.99 ? 151 TYR A CE1 1 
ATOM   1194 C CE2 . TYR A 1 149 ? 1.072   41.423  -4.088  1.00 26.35 ? 151 TYR A CE2 1 
ATOM   1195 C CZ  . TYR A 1 149 ? 0.205   42.175  -4.835  1.00 25.40 ? 151 TYR A CZ  1 
ATOM   1196 O OH  . TYR A 1 149 ? 0.654   42.704  -6.025  1.00 29.05 ? 151 TYR A OH  1 
ATOM   1197 N N   . ILE A 1 150 ? -2.935  37.876  -2.739  1.00 22.48 ? 152 ILE A N   1 
ATOM   1198 C CA  . ILE A 1 150 ? -2.760  36.621  -3.461  1.00 20.09 ? 152 ILE A CA  1 
ATOM   1199 C C   . ILE A 1 150 ? -1.772  36.836  -4.598  1.00 23.87 ? 152 ILE A C   1 
ATOM   1200 O O   . ILE A 1 150 ? -1.977  37.707  -5.452  1.00 23.39 ? 152 ILE A O   1 
ATOM   1201 C CB  . ILE A 1 150 ? -4.107  36.118  -3.995  1.00 21.61 ? 152 ILE A CB  1 
ATOM   1202 C CG1 . ILE A 1 150 ? -5.111  35.986  -2.831  1.00 22.59 ? 152 ILE A CG1 1 
ATOM   1203 C CG2 . ILE A 1 150 ? -3.921  34.870  -4.819  1.00 22.49 ? 152 ILE A CG2 1 
ATOM   1204 C CD1 . ILE A 1 150 ? -4.827  34.826  -1.894  1.00 20.96 ? 152 ILE A CD1 1 
ATOM   1205 N N   . MET A 1 151 ? -0.724  36.020  -4.644  1.00 23.45 ? 153 MET A N   1 
ATOM   1206 C CA  . MET A 1 151 ? 0.290   36.137  -5.681  1.00 26.24 ? 153 MET A CA  1 
ATOM   1207 C C   . MET A 1 151 ? 0.379   34.825  -6.433  1.00 28.65 ? 153 MET A C   1 
ATOM   1208 O O   . MET A 1 151 ? 0.342   33.751  -5.826  1.00 25.42 ? 153 MET A O   1 
ATOM   1209 C CB  . MET A 1 151 ? 1.676   36.440  -5.114  1.00 25.95 ? 153 MET A CB  1 
ATOM   1210 C CG  . MET A 1 151 ? 1.945   37.896  -4.840  1.00 32.30 ? 153 MET A CG  1 
ATOM   1211 S SD  . MET A 1 151 ? 3.181   38.069  -3.549  1.00 33.54 ? 153 MET A SD  1 
ATOM   1212 C CE  . MET A 1 151 ? 4.601   38.559  -4.534  1.00 40.07 ? 153 MET A CE  1 
ATOM   1213 N N   . ALA A 1 152 ? 0.534   34.913  -7.751  1.00 27.96 ? 154 ALA A N   1 
ATOM   1214 C CA  . ALA A 1 152 ? 0.797   33.726  -8.545  1.00 29.15 ? 154 ALA A CA  1 
ATOM   1215 C C   . ALA A 1 152 ? 2.148   33.120  -8.180  1.00 33.80 ? 154 ALA A C   1 
ATOM   1216 O O   . ALA A 1 152 ? 3.124   33.831  -7.927  1.00 35.55 ? 154 ALA A O   1 
ATOM   1217 C CB  . ALA A 1 152 ? 0.759   34.075  -10.037 1.00 35.01 ? 154 ALA A CB  1 
ATOM   1218 N N   . ASP A 1 153 ? 2.192   31.792  -8.158  1.00 36.39 ? 155 ASP A N   1 
ATOM   1219 C CA  . ASP A 1 153 ? 3.401   30.987  -7.964  1.00 40.35 ? 155 ASP A CA  1 
ATOM   1220 C C   . ASP A 1 153 ? 3.495   30.077  -9.182  1.00 45.21 ? 155 ASP A C   1 
ATOM   1221 O O   . ASP A 1 153 ? 3.028   28.936  -9.143  1.00 47.24 ? 155 ASP A O   1 
ATOM   1222 C CB  . ASP A 1 153 ? 3.306   30.196  -6.667  1.00 39.97 ? 155 ASP A CB  1 
ATOM   1223 C CG  . ASP A 1 153 ? 4.578   29.440  -6.336  1.00 48.20 ? 155 ASP A CG  1 
ATOM   1224 O OD1 . ASP A 1 153 ? 5.325   29.051  -7.260  1.00 52.99 ? 155 ASP A OD1 1 
ATOM   1225 O OD2 . ASP A 1 153 ? 4.824   29.218  -5.133  1.00 49.94 ? 155 ASP A OD2 1 
ATOM   1226 N N   . LYS A 1 154 ? 4.084   30.594  -10.268 1.00 46.55 ? 156 LYS A N   1 
ATOM   1227 C CA  . LYS A 1 154 ? 4.003   29.903  -11.554 1.00 49.98 ? 156 LYS A CA  1 
ATOM   1228 C C   . LYS A 1 154 ? 4.566   28.491  -11.464 1.00 54.34 ? 156 LYS A C   1 
ATOM   1229 O O   . LYS A 1 154 ? 4.026   27.558  -12.073 1.00 55.36 ? 156 LYS A O   1 
ATOM   1230 C CB  . LYS A 1 154 ? 4.734   30.696  -12.643 1.00 51.02 ? 156 LYS A CB  1 
ATOM   1231 C CG  . LYS A 1 154 ? 5.610   29.827  -13.553 1.00 54.42 ? 156 LYS A CG  1 
ATOM   1232 C CD  . LYS A 1 154 ? 6.301   30.617  -14.650 1.00 52.58 ? 156 LYS A CD  1 
ATOM   1233 C CE  . LYS A 1 154 ? 6.746   29.690  -15.778 1.00 53.55 ? 156 LYS A CE  1 
ATOM   1234 N NZ  . LYS A 1 154 ? 7.715   30.330  -16.714 1.00 53.43 ? 156 LYS A NZ  1 
ATOM   1235 N N   . GLN A 1 155 ? 5.637   28.315  -10.689 1.00 54.28 ? 157 GLN A N   1 
ATOM   1236 C CA  . GLN A 1 155 ? 6.318   27.027  -10.644 1.00 55.86 ? 157 GLN A CA  1 
ATOM   1237 C C   . GLN A 1 155 ? 5.409   25.926  -10.113 1.00 54.35 ? 157 GLN A C   1 
ATOM   1238 O O   . GLN A 1 155 ? 5.432   24.798  -10.618 1.00 56.98 ? 157 GLN A O   1 
ATOM   1239 C CB  . GLN A 1 155 ? 7.578   27.150  -9.797  1.00 58.12 ? 157 GLN A CB  1 
ATOM   1240 C CG  . GLN A 1 155 ? 8.179   28.546  -9.832  1.00 60.68 ? 157 GLN A CG  1 
ATOM   1241 C CD  . GLN A 1 155 ? 9.105   28.805  -8.666  1.00 63.28 ? 157 GLN A CD  1 
ATOM   1242 O OE1 . GLN A 1 155 ? 9.409   27.899  -7.888  1.00 64.18 ? 157 GLN A OE1 1 
ATOM   1243 N NE2 . GLN A 1 155 ? 9.565   30.046  -8.539  1.00 66.69 ? 157 GLN A NE2 1 
ATOM   1244 N N   . LYS A 1 156 ? 4.599   26.230  -9.105  1.00 51.37 ? 158 LYS A N   1 
ATOM   1245 C CA  . LYS A 1 156 ? 3.677   25.252  -8.546  1.00 49.41 ? 158 LYS A CA  1 
ATOM   1246 C C   . LYS A 1 156 ? 2.303   25.297  -9.209  1.00 49.61 ? 158 LYS A C   1 
ATOM   1247 O O   . LYS A 1 156 ? 1.372   24.649  -8.721  1.00 48.95 ? 158 LYS A O   1 
ATOM   1248 C CB  . LYS A 1 156 ? 3.547   25.465  -7.036  1.00 49.53 ? 158 LYS A CB  1 
ATOM   1249 C CG  . LYS A 1 156 ? 4.888   25.721  -6.340  1.00 51.27 ? 158 LYS A CG  1 
ATOM   1250 C CD  . LYS A 1 156 ? 4.877   25.289  -4.875  1.00 47.35 ? 158 LYS A CD  1 
ATOM   1251 C CE  . LYS A 1 156 ? 5.875   24.165  -4.607  1.00 49.16 ? 158 LYS A CE  1 
ATOM   1252 N NZ  . LYS A 1 156 ? 5.494   23.308  -3.436  1.00 49.13 ? 158 LYS A NZ  1 
ATOM   1253 N N   . ASN A 1 157 ? 2.163   26.039  -10.313 1.00 47.87 ? 159 ASN A N   1 
ATOM   1254 C CA  . ASN A 1 157 ? 0.878   26.215  -10.996 1.00 46.68 ? 159 ASN A CA  1 
ATOM   1255 C C   . ASN A 1 157 ? -0.213  26.620  -10.002 1.00 44.91 ? 159 ASN A C   1 
ATOM   1256 O O   . ASN A 1 157 ? -1.376  26.229  -10.124 1.00 44.91 ? 159 ASN A O   1 
ATOM   1257 C CB  . ASN A 1 157 ? 0.487   24.951  -11.774 1.00 46.71 ? 159 ASN A CB  1 
ATOM   1258 C CG  . ASN A 1 157 ? -0.732  25.160  -12.674 1.00 46.91 ? 159 ASN A CG  1 
ATOM   1259 O OD1 . ASN A 1 157 ? -1.685  24.377  -12.643 1.00 44.13 ? 159 ASN A OD1 1 
ATOM   1260 N ND2 . ASN A 1 157 ? -0.706  26.224  -13.475 1.00 45.51 ? 159 ASN A ND2 1 
ATOM   1261 N N   . GLY A 1 158 ? 0.170   27.420  -9.005  1.00 39.34 ? 160 GLY A N   1 
ATOM   1262 C CA  . GLY A 1 158 ? -0.752  27.821  -7.963  1.00 34.81 ? 160 GLY A CA  1 
ATOM   1263 C C   . GLY A 1 158 ? -0.538  29.238  -7.472  1.00 33.37 ? 160 GLY A C   1 
ATOM   1264 O O   . GLY A 1 158 ? -0.047  30.091  -8.217  1.00 34.47 ? 160 GLY A O   1 
ATOM   1265 N N   . ILE A 1 159 ? -0.927  29.508  -6.223  1.00 27.74 ? 161 ILE A N   1 
ATOM   1266 C CA  . ILE A 1 159 ? -0.825  30.832  -5.624  1.00 26.64 ? 161 ILE A CA  1 
ATOM   1267 C C   . ILE A 1 159 ? -0.154  30.716  -4.266  1.00 26.49 ? 161 ILE A C   1 
ATOM   1268 O O   . ILE A 1 159 ? -0.111  29.648  -3.649  1.00 25.87 ? 161 ILE A O   1 
ATOM   1269 C CB  . ILE A 1 159 ? -2.194  31.538  -5.486  1.00 22.19 ? 161 ILE A CB  1 
ATOM   1270 C CG1 . ILE A 1 159 ? -3.101  30.805  -4.475  1.00 25.91 ? 161 ILE A CG1 1 
ATOM   1271 C CG2 . ILE A 1 159 ? -2.870  31.712  -6.864  1.00 24.63 ? 161 ILE A CG2 1 
ATOM   1272 C CD1 . ILE A 1 159 ? -3.025  31.325  -3.011  1.00 20.07 ? 161 ILE A CD1 1 
ATOM   1273 N N   . LYS A 1 160 ? 0.381   31.842  -3.806  1.00 25.63 ? 162 LYS A N   1 
ATOM   1274 C CA  . LYS A 1 160 ? 0.938   31.931  -2.467  1.00 21.67 ? 162 LYS A CA  1 
ATOM   1275 C C   . LYS A 1 160 ? 0.456   33.222  -1.834  1.00 24.21 ? 162 LYS A C   1 
ATOM   1276 O O   . LYS A 1 160 ? -0.045  34.123  -2.519  1.00 24.07 ? 162 LYS A O   1 
ATOM   1277 C CB  . LYS A 1 160 ? 2.462   31.866  -2.500  1.00 28.98 ? 162 LYS A CB  1 
ATOM   1278 C CG  . LYS A 1 160 ? 3.111   33.006  -3.275  1.00 31.99 ? 162 LYS A CG  1 
ATOM   1279 C CD  . LYS A 1 160 ? 4.466   32.574  -3.846  1.00 33.39 ? 162 LYS A CD  1 
ATOM   1280 C CE  . LYS A 1 160 ? 5.315   33.782  -4.205  1.00 42.04 ? 162 LYS A CE  1 
ATOM   1281 N NZ  . LYS A 1 160 ? 5.006   34.275  -5.578  1.00 42.47 ? 162 LYS A NZ  1 
ATOM   1282 N N   . ALA A 1 161 ? 0.607   33.305  -0.516  1.00 20.72 ? 163 ALA A N   1 
ATOM   1283 C CA  . ALA A 1 161 ? 0.303   34.545  0.178   1.00 19.52 ? 163 ALA A CA  1 
ATOM   1284 C C   . ALA A 1 161 ? 0.959   34.523  1.542   1.00 21.81 ? 163 ALA A C   1 
ATOM   1285 O O   . ALA A 1 161 ? 1.244   33.459  2.101   1.00 22.62 ? 163 ALA A O   1 
ATOM   1286 C CB  . ALA A 1 161 ? -1.205  34.771  0.319   1.00 20.73 ? 163 ALA A CB  1 
ATOM   1287 N N   . ASN A 1 162 ? 1.211   35.717  2.061   1.00 22.51 ? 164 ASN A N   1 
ATOM   1288 C CA  . ASN A 1 162 ? 1.728   35.892  3.402   1.00 23.97 ? 164 ASN A CA  1 
ATOM   1289 C C   . ASN A 1 162 ? 1.015   37.089  4.023   1.00 27.70 ? 164 ASN A C   1 
ATOM   1290 O O   . ASN A 1 162 ? 0.925   38.149  3.392   1.00 26.58 ? 164 ASN A O   1 
ATOM   1291 C CB  . ASN A 1 162 ? 3.248   36.093  3.353   1.00 27.15 ? 164 ASN A CB  1 
ATOM   1292 C CG  . ASN A 1 162 ? 3.769   36.796  4.559   1.00 34.79 ? 164 ASN A CG  1 
ATOM   1293 O OD1 . ASN A 1 162 ? 3.735   36.240  5.664   1.00 34.47 ? 164 ASN A OD1 1 
ATOM   1294 N ND2 . ASN A 1 162 ? 4.264   38.018  4.377   1.00 33.99 ? 164 ASN A ND2 1 
ATOM   1295 N N   . PHE A 1 163 ? 0.471   36.916  5.233   1.00 18.50 ? 165 PHE A N   1 
ATOM   1296 C CA  . PHE A 1 163 ? -0.294  37.984  5.868   1.00 21.36 ? 165 PHE A CA  1 
ATOM   1297 C C   . PHE A 1 163 ? -0.307  37.772  7.375   1.00 21.82 ? 165 PHE A C   1 
ATOM   1298 O O   . PHE A 1 163 ? -0.085  36.665  7.871   1.00 19.35 ? 165 PHE A O   1 
ATOM   1299 C CB  . PHE A 1 163 ? -1.728  38.075  5.318   1.00 23.27 ? 165 PHE A CB  1 
ATOM   1300 C CG  . PHE A 1 163 ? -2.553  36.818  5.509   1.00 21.63 ? 165 PHE A CG  1 
ATOM   1301 C CD1 . PHE A 1 163 ? -2.487  35.779  4.584   1.00 18.00 ? 165 PHE A CD1 1 
ATOM   1302 C CD2 . PHE A 1 163 ? -3.418  36.692  6.580   1.00 18.29 ? 165 PHE A CD2 1 
ATOM   1303 C CE1 . PHE A 1 163 ? -3.246  34.637  4.746   1.00 16.98 ? 165 PHE A CE1 1 
ATOM   1304 C CE2 . PHE A 1 163 ? -4.185  35.538  6.744   1.00 19.75 ? 165 PHE A CE2 1 
ATOM   1305 C CZ  . PHE A 1 163 ? -4.104  34.523  5.808   1.00 18.08 ? 165 PHE A CZ  1 
ATOM   1306 N N   . LYS A 1 164 ? -0.561  38.859  8.094   1.00 19.21 ? 166 LYS A N   1 
ATOM   1307 C CA  . LYS A 1 164 ? -0.605  38.859  9.543   1.00 20.89 ? 166 LYS A CA  1 
ATOM   1308 C C   . LYS A 1 164 ? -2.051  38.980  9.999   1.00 22.69 ? 166 LYS A C   1 
ATOM   1309 O O   . LYS A 1 164 ? -2.830  39.735  9.418   1.00 24.09 ? 166 LYS A O   1 
ATOM   1310 C CB  . LYS A 1 164 ? 0.204   40.033  10.097  1.00 25.11 ? 166 LYS A CB  1 
ATOM   1311 C CG  . LYS A 1 164 ? 1.683   39.878  9.867   1.00 28.58 ? 166 LYS A CG  1 
ATOM   1312 C CD  . LYS A 1 164 ? 2.457   40.828  10.753  1.00 36.03 ? 166 LYS A CD  1 
ATOM   1313 C CE  . LYS A 1 164 ? 3.856   40.312  11.001  1.00 35.70 ? 166 LYS A CE  1 
ATOM   1314 N NZ  . LYS A 1 164 ? 4.851   41.335  10.558  1.00 39.79 ? 166 LYS A NZ  1 
ATOM   1315 N N   . ILE A 1 165 ? -2.420  38.223  11.017  1.00 15.41 ? 167 ILE A N   1 
ATOM   1316 C CA  . ILE A 1 165 ? -3.675  38.428  11.716  1.00 17.10 ? 167 ILE A CA  1 
ATOM   1317 C C   . ILE A 1 165 ? -3.335  38.846  13.142  1.00 22.47 ? 167 ILE A C   1 
ATOM   1318 O O   . ILE A 1 165 ? -2.427  38.278  13.768  1.00 19.53 ? 167 ILE A O   1 
ATOM   1319 C CB  . ILE A 1 165 ? -4.546  37.158  11.705  1.00 18.68 ? 167 ILE A CB  1 
ATOM   1320 C CG1 . ILE A 1 165 ? -4.894  36.782  10.261  1.00 16.99 ? 167 ILE A CG1 1 
ATOM   1321 C CG2 . ILE A 1 165 ? -5.840  37.378  12.499  1.00 19.82 ? 167 ILE A CG2 1 
ATOM   1322 C CD1 . ILE A 1 165 ? -5.927  37.705  9.615   1.00 18.55 ? 167 ILE A CD1 1 
ATOM   1323 N N   . ARG A 1 166 ? -4.053  39.849  13.641  1.00 22.42 ? 168 ARG A N   1 
ATOM   1324 C CA  . ARG A 1 166 ? -3.926  40.348  15.008  1.00 22.86 ? 168 ARG A CA  1 
ATOM   1325 C C   . ARG A 1 166 ? -5.124  39.878  15.830  1.00 24.73 ? 168 ARG A C   1 
ATOM   1326 O O   . ARG A 1 166 ? -6.267  40.214  15.509  1.00 24.99 ? 168 ARG A O   1 
ATOM   1327 C CB  . ARG A 1 166 ? -3.862  41.878  15.000  1.00 24.96 ? 168 ARG A CB  1 
ATOM   1328 C CG  . ARG A 1 166 ? -3.008  42.424  13.869  1.00 31.51 ? 168 ARG A CG  1 
ATOM   1329 C CD  . ARG A 1 166 ? -2.369  43.745  14.188  1.00 32.66 ? 168 ARG A CD  1 
ATOM   1330 N NE  . ARG A 1 166 ? -1.155  43.907  13.396  1.00 36.88 ? 168 ARG A NE  1 
ATOM   1331 C CZ  . ARG A 1 166 ? -0.026  44.423  13.859  1.00 42.92 ? 168 ARG A CZ  1 
ATOM   1332 N NH1 . ARG A 1 166 ? 0.059   44.911  15.090  1.00 43.95 ? 168 ARG A NH1 1 
ATOM   1333 N NH2 . ARG A 1 166 ? 1.050   44.442  13.073  1.00 45.91 ? 168 ARG A NH2 1 
ATOM   1334 N N   . HIS A 1 167 ? -4.864  39.138  16.902  1.00 19.11 ? 169 HIS A N   1 
ATOM   1335 C CA  . HIS A 1 167 ? -5.912  38.593  17.764  1.00 21.92 ? 169 HIS A CA  1 
ATOM   1336 C C   . HIS A 1 167 ? -5.927  39.399  19.063  1.00 25.74 ? 169 HIS A C   1 
ATOM   1337 O O   . HIS A 1 167 ? -4.923  39.428  19.780  1.00 25.63 ? 169 HIS A O   1 
ATOM   1338 C CB  . HIS A 1 167 ? -5.646  37.113  18.074  1.00 23.29 ? 169 HIS A CB  1 
ATOM   1339 C CG  . HIS A 1 167 ? -5.834  36.175  16.909  1.00 23.09 ? 169 HIS A CG  1 
ATOM   1340 N ND1 . HIS A 1 167 ? -7.015  36.062  16.203  1.00 18.35 ? 169 HIS A ND1 1 
ATOM   1341 C CD2 . HIS A 1 167 ? -4.962  35.325  16.312  1.00 20.00 ? 169 HIS A CD2 1 
ATOM   1342 C CE1 . HIS A 1 167 ? -6.868  35.171  15.235  1.00 19.16 ? 169 HIS A CE1 1 
ATOM   1343 N NE2 . HIS A 1 167 ? -5.635  34.707  15.279  1.00 19.35 ? 169 HIS A NE2 1 
ATOM   1344 N N   . ASN A 1 168 ? -7.060  40.025  19.381  1.00 26.12 ? 170 ASN A N   1 
ATOM   1345 C CA  . ASN A 1 168 ? -7.158  40.807  20.620  1.00 30.05 ? 170 ASN A CA  1 
ATOM   1346 C C   . ASN A 1 168 ? -6.939  39.912  21.843  1.00 26.27 ? 170 ASN A C   1 
ATOM   1347 O O   . ASN A 1 168 ? -7.614  38.891  22.009  1.00 26.31 ? 170 ASN A O   1 
ATOM   1348 C CB  . ASN A 1 168 ? -8.535  41.478  20.752  1.00 25.98 ? 170 ASN A CB  1 
ATOM   1349 C CG  . ASN A 1 168 ? -8.694  42.705  19.884  1.00 27.10 ? 170 ASN A CG  1 
ATOM   1350 O OD1 . ASN A 1 168 ? -7.759  43.151  19.220  1.00 28.73 ? 170 ASN A OD1 1 
ATOM   1351 N ND2 . ASN A 1 168 ? -9.878  43.301  19.938  1.00 33.45 ? 170 ASN A ND2 1 
ATOM   1352 N N   . ILE A 1 169 ? -6.003  40.311  22.717  1.00 29.95 ? 171 ILE A N   1 
ATOM   1353 C CA  . ILE A 1 169 ? -5.813  39.674  24.023  1.00 30.73 ? 171 ILE A CA  1 
ATOM   1354 C C   . ILE A 1 169 ? -6.732  40.346  25.035  1.00 33.09 ? 171 ILE A C   1 
ATOM   1355 O O   . ILE A 1 169 ? -6.858  41.576  25.050  1.00 33.85 ? 171 ILE A O   1 
ATOM   1356 C CB  . ILE A 1 169 ? -4.341  39.764  24.491  1.00 31.48 ? 171 ILE A CB  1 
ATOM   1357 C CG1 . ILE A 1 169 ? -3.355  39.258  23.433  1.00 29.54 ? 171 ILE A CG1 1 
ATOM   1358 C CG2 . ILE A 1 169 ? -4.132  39.033  25.828  1.00 31.97 ? 171 ILE A CG2 1 
ATOM   1359 N N   . GLU A 1 170 ? -7.347  39.565  25.901  1.00 31.90 ? 172 GLU A N   1 
ATOM   1360 C CA  . GLU A 1 170 ? -8.200  40.083  26.957  1.00 37.87 ? 172 GLU A CA  1 
ATOM   1361 C C   . GLU A 1 170 ? -7.446  41.075  27.815  1.00 41.87 ? 172 GLU A C   1 
ATOM   1362 O O   . GLU A 1 170 ? -6.263  40.956  28.040  1.00 41.87 ? 172 GLU A O   1 
ATOM   1363 C CB  . GLU A 1 170 ? -8.759  38.954  27.831  1.00 41.41 ? 172 GLU A CB  1 
ATOM   1364 C CG  . GLU A 1 170 ? -10.075 38.429  27.364  1.00 39.65 ? 172 GLU A CG  1 
ATOM   1365 C CD  . GLU A 1 170 ? -10.401 37.059  27.852  1.00 47.28 ? 172 GLU A CD  1 
ATOM   1366 O OE1 . GLU A 1 170 ? -9.631  36.513  28.636  1.00 51.48 ? 172 GLU A OE1 1 
ATOM   1367 O OE2 . GLU A 1 170 ? -11.450 36.518  27.472  1.00 49.35 ? 172 GLU A OE2 1 
ATOM   1368 N N   . ASP A 1 171 ? -8.143  42.067  28.291  1.00 43.71 ? 173 ASP A N   1 
ATOM   1369 C CA  . ASP A 1 171 ? -7.441  43.205  28.770  1.00 44.58 ? 173 ASP A CA  1 
ATOM   1370 C C   . ASP A 1 171 ? -6.363  43.863  27.991  1.00 43.11 ? 173 ASP A C   1 
ATOM   1371 O O   . ASP A 1 171 ? -5.324  44.161  28.552  1.00 44.42 ? 173 ASP A O   1 
ATOM   1372 C CB  . ASP A 1 171 ? -6.345  42.768  29.708  1.00 46.92 ? 173 ASP A CB  1 
ATOM   1373 C CG  . ASP A 1 171 ? -6.903  42.131  30.952  1.00 57.63 ? 173 ASP A CG  1 
ATOM   1374 O OD1 . ASP A 1 171 ? -6.148  41.421  31.663  1.00 59.19 ? 173 ASP A OD1 1 
ATOM   1375 O OD2 . ASP A 1 171 ? -8.118  42.322  31.208  1.00 56.16 ? 173 ASP A OD2 1 
ATOM   1376 N N   . GLY A 1 172 ? -6.549  44.141  26.741  1.00 39.84 ? 174 GLY A N   1 
ATOM   1377 C CA  . GLY A 1 172 ? -5.417  44.594  26.011  1.00 35.24 ? 174 GLY A CA  1 
ATOM   1378 C C   . GLY A 1 172 ? -4.265  43.980  25.352  1.00 30.74 ? 174 GLY A C   1 
ATOM   1379 O O   . GLY A 1 172 ? -3.720  43.029  25.794  1.00 34.39 ? 174 GLY A O   1 
ATOM   1380 N N   . GLY A 1 173 ? -3.873  44.585  24.273  1.00 31.32 ? 175 GLY A N   1 
ATOM   1381 C CA  . GLY A 1 173 ? -2.779  44.042  23.503  1.00 28.82 ? 175 GLY A CA  1 
ATOM   1382 C C   . GLY A 1 173 ? -3.281  43.138  22.389  1.00 28.21 ? 175 GLY A C   1 
ATOM   1383 O O   . GLY A 1 173 ? -4.468  42.843  22.262  1.00 28.79 ? 175 GLY A O   1 
ATOM   1384 N N   . VAL A 1 174 ? -2.338  42.677  21.581  1.00 29.23 ? 176 VAL A N   1 
ATOM   1385 C CA  . VAL A 1 174 ? -2.631  41.934  20.366  1.00 25.19 ? 176 VAL A CA  1 
ATOM   1386 C C   . VAL A 1 174 ? -1.682  40.751  20.266  1.00 27.19 ? 176 VAL A C   1 
ATOM   1387 O O   . VAL A 1 174 ? -0.477  40.890  20.510  1.00 28.37 ? 176 VAL A O   1 
ATOM   1388 C CB  . VAL A 1 174 ? -2.527  42.864  19.142  1.00 30.28 ? 176 VAL A CB  1 
ATOM   1389 C CG1 . VAL A 1 174 ? -2.151  42.112  17.930  1.00 30.74 ? 176 VAL A CG1 1 
ATOM   1390 C CG2 . VAL A 1 174 ? -3.863  43.580  18.939  1.00 27.22 ? 176 VAL A CG2 1 
ATOM   1391 N N   . GLN A 1 175 ? -2.235  39.582  19.957  1.00 24.98 ? 177 GLN A N   1 
ATOM   1392 C CA  . GLN A 1 175 ? -1.465  38.376  19.685  1.00 23.66 ? 177 GLN A CA  1 
ATOM   1393 C C   . GLN A 1 175 ? -1.369  38.214  18.178  1.00 25.07 ? 177 GLN A C   1 
ATOM   1394 O O   . GLN A 1 175 ? -2.395  38.112  17.497  1.00 20.34 ? 177 GLN A O   1 
ATOM   1395 C CB  . GLN A 1 175 ? -2.126  37.150  20.322  1.00 25.84 ? 177 GLN A CB  1 
ATOM   1396 C CG  . GLN A 1 175 ? -1.575  35.800  19.842  1.00 24.54 ? 177 GLN A CG  1 
ATOM   1397 C CD  . GLN A 1 175 ? -0.188  35.497  20.375  1.00 26.12 ? 177 GLN A CD  1 
ATOM   1398 O OE1 . GLN A 1 175 ? -0.004  35.337  21.583  1.00 23.46 ? 177 GLN A OE1 1 
ATOM   1399 N NE2 . GLN A 1 175 ? 0.798   35.405  19.475  1.00 21.99 ? 177 GLN A NE2 1 
ATOM   1400 N N   . LEU A 1 176 ? -0.148  38.199  17.663  1.00 20.80 ? 178 LEU A N   1 
ATOM   1401 C CA  . LEU A 1 176 ? 0.081   38.160  16.229  1.00 22.25 ? 178 LEU A CA  1 
ATOM   1402 C C   . LEU A 1 176 ? 0.150   36.730  15.716  1.00 22.40 ? 178 LEU A C   1 
ATOM   1403 O O   . LEU A 1 176 ? 0.728   35.845  16.362  1.00 20.27 ? 178 LEU A O   1 
ATOM   1404 C CB  . LEU A 1 176 ? 1.375   38.895  15.896  1.00 24.18 ? 178 LEU A CB  1 
ATOM   1405 C CG  . LEU A 1 176 ? 1.325   40.391  16.184  1.00 28.30 ? 178 LEU A CG  1 
ATOM   1406 C CD1 . LEU A 1 176 ? 2.608   40.982  15.750  1.00 35.42 ? 178 LEU A CD1 1 
ATOM   1407 C CD2 . LEU A 1 176 ? 0.196   41.046  15.440  1.00 31.40 ? 178 LEU A CD2 1 
ATOM   1408 N N   . ALA A 1 177 ? -0.425  36.516  14.533  1.00 17.58 ? 179 ALA A N   1 
ATOM   1409 C CA  . ALA A 1 177 ? -0.444  35.214  13.878  1.00 18.07 ? 179 ALA A CA  1 
ATOM   1410 C C   . ALA A 1 177 ? 0.043   35.430  12.454  1.00 17.93 ? 179 ALA A C   1 
ATOM   1411 O O   . ALA A 1 177 ? -0.702  35.955  11.621  1.00 18.49 ? 179 ALA A O   1 
ATOM   1412 C CB  . ALA A 1 177 ? -1.842  34.599  13.899  1.00 17.67 ? 179 ALA A CB  1 
ATOM   1413 N N   . ASP A 1 178 ? 1.289   35.045  12.188  1.00 20.42 ? 180 ASP A N   1 
ATOM   1414 C CA  . ASP A 1 178 ? 1.923   35.273  10.898  1.00 21.88 ? 180 ASP A CA  1 
ATOM   1415 C C   . ASP A 1 178 ? 1.626   34.085  9.985   1.00 17.51 ? 180 ASP A C   1 
ATOM   1416 O O   . ASP A 1 178 ? 2.063   32.961  10.256  1.00 17.97 ? 180 ASP A O   1 
ATOM   1417 C CB  . ASP A 1 178 ? 3.428   35.450  11.086  1.00 22.05 ? 180 ASP A CB  1 
ATOM   1418 C CG  . ASP A 1 178 ? 4.114   36.164  9.917   1.00 33.05 ? 180 ASP A CG  1 
ATOM   1419 O OD1 . ASP A 1 178 ? 3.488   36.408  8.847   1.00 31.21 ? 180 ASP A OD1 1 
ATOM   1420 O OD2 . ASP A 1 178 ? 5.335   36.436  10.057  1.00 35.21 ? 180 ASP A OD2 1 
ATOM   1421 N N   . HIS A 1 179 ? 0.932   34.343  8.884   1.00 15.75 ? 181 HIS A N   1 
ATOM   1422 C CA  . HIS A 1 179 ? 0.397   33.296  8.020   1.00 15.73 ? 181 HIS A CA  1 
ATOM   1423 C C   . HIS A 1 179 ? 1.264   33.181  6.771   1.00 19.59 ? 181 HIS A C   1 
ATOM   1424 O O   . HIS A 1 179 ? 1.492   34.181  6.077   1.00 19.20 ? 181 HIS A O   1 
ATOM   1425 C CB  . HIS A 1 179 ? -1.042  33.614  7.584   1.00 18.57 ? 181 HIS A CB  1 
ATOM   1426 C CG  . HIS A 1 179 ? -2.083  33.388  8.640   1.00 16.46 ? 181 HIS A CG  1 
ATOM   1427 N ND1 . HIS A 1 179 ? -2.119  34.118  9.812   1.00 17.29 ? 181 HIS A ND1 1 
ATOM   1428 C CD2 . HIS A 1 179 ? -3.182  32.593  8.657   1.00 16.25 ? 181 HIS A CD2 1 
ATOM   1429 C CE1 . HIS A 1 179 ? -3.165  33.745  10.531  1.00 17.58 ? 181 HIS A CE1 1 
ATOM   1430 N NE2 . HIS A 1 179 ? -3.831  32.828  9.850   1.00 15.42 ? 181 HIS A NE2 1 
ATOM   1431 N N   . TYR A 1 180 ? 1.709   31.968  6.465   1.00 18.76 ? 182 TYR A N   1 
ATOM   1432 C CA  . TYR A 1 180 ? 2.314   31.657  5.173   1.00 20.99 ? 182 TYR A CA  1 
ATOM   1433 C C   . TYR A 1 180 ? 1.432   30.637  4.474   1.00 20.58 ? 182 TYR A C   1 
ATOM   1434 O O   . TYR A 1 180 ? 1.052   29.637  5.080   1.00 18.39 ? 182 TYR A O   1 
ATOM   1435 C CB  . TYR A 1 180 ? 3.753   31.136  5.341   1.00 21.57 ? 182 TYR A CB  1 
ATOM   1436 C CG  . TYR A 1 180 ? 4.660   32.183  5.929   1.00 21.24 ? 182 TYR A CG  1 
ATOM   1437 C CD1 . TYR A 1 180 ? 4.695   32.420  7.299   1.00 22.73 ? 182 TYR A CD1 1 
ATOM   1438 C CD2 . TYR A 1 180 ? 5.424   32.998  5.099   1.00 25.08 ? 182 TYR A CD2 1 
ATOM   1439 C CE1 . TYR A 1 180 ? 5.505   33.407  7.825   1.00 22.46 ? 182 TYR A CE1 1 
ATOM   1440 C CE2 . TYR A 1 180 ? 6.242   33.973  5.609   1.00 25.47 ? 182 TYR A CE2 1 
ATOM   1441 C CZ  . TYR A 1 180 ? 6.278   34.180  6.968   1.00 26.70 ? 182 TYR A CZ  1 
ATOM   1442 O OH  . TYR A 1 180 ? 7.089   35.167  7.462   1.00 33.42 ? 182 TYR A OH  1 
ATOM   1443 N N   . GLN A 1 181 ? 1.085   30.893  3.211   1.00 18.05 ? 183 GLN A N   1 
ATOM   1444 C CA  . GLN A 1 181 ? 0.050   30.110  2.551   1.00 20.44 ? 183 GLN A CA  1 
ATOM   1445 C C   . GLN A 1 181 ? 0.511   29.728  1.152   1.00 21.42 ? 183 GLN A C   1 
ATOM   1446 O O   . GLN A 1 181 ? 1.153   30.529  0.468   1.00 19.31 ? 183 GLN A O   1 
ATOM   1447 C CB  . GLN A 1 181 ? -1.275  30.896  2.486   1.00 17.25 ? 183 GLN A CB  1 
ATOM   1448 C CG  . GLN A 1 181 ? -2.363  30.203  1.685   1.00 15.89 ? 183 GLN A CG  1 
ATOM   1449 C CD  . GLN A 1 181 ? -3.677  30.983  1.660   1.00 19.51 ? 183 GLN A CD  1 
ATOM   1450 O OE1 . GLN A 1 181 ? -3.905  31.894  2.461   1.00 15.17 ? 183 GLN A OE1 1 
ATOM   1451 N NE2 . GLN A 1 181 ? -4.517  30.655  0.705   1.00 19.75 ? 183 GLN A NE2 1 
ATOM   1452 N N   . GLN A 1 182 ? 0.197   28.501  0.731   1.00 22.89 ? 184 GLN A N   1 
ATOM   1453 C CA  . GLN A 1 182 ? 0.305   28.162  -0.685  1.00 22.42 ? 184 GLN A CA  1 
ATOM   1454 C C   . GLN A 1 182 ? -0.796  27.191  -1.058  1.00 25.31 ? 184 GLN A C   1 
ATOM   1455 O O   . GLN A 1 182 ? -1.215  26.362  -0.243  1.00 23.46 ? 184 GLN A O   1 
ATOM   1456 C CB  . GLN A 1 182 ? 1.668   27.579  -1.073  1.00 26.43 ? 184 GLN A CB  1 
ATOM   1457 C CG  . GLN A 1 182 ? 2.363   26.750  -0.045  1.00 30.94 ? 184 GLN A CG  1 
ATOM   1458 C CD  . GLN A 1 182 ? 3.705   26.233  -0.566  1.00 38.40 ? 184 GLN A CD  1 
ATOM   1459 O OE1 . GLN A 1 182 ? 4.760   26.573  -0.030  1.00 39.19 ? 184 GLN A OE1 1 
ATOM   1460 N NE2 . GLN A 1 182 ? 3.665   25.436  -1.631  1.00 38.42 ? 184 GLN A NE2 1 
ATOM   1461 N N   . ASN A 1 183 ? -1.291  27.337  -2.289  1.00 23.66 ? 185 ASN A N   1 
ATOM   1462 C CA  . ASN A 1 183 ? -2.405  26.572  -2.820  1.00 23.12 ? 185 ASN A CA  1 
ATOM   1463 C C   . ASN A 1 183 ? -1.991  26.019  -4.171  1.00 25.03 ? 185 ASN A C   1 
ATOM   1464 O O   . ASN A 1 183 ? -1.348  26.719  -4.958  1.00 26.37 ? 185 ASN A O   1 
ATOM   1465 C CB  . ASN A 1 183 ? -3.665  27.436  -2.991  1.00 23.31 ? 185 ASN A CB  1 
ATOM   1466 C CG  . ASN A 1 183 ? -4.270  27.855  -1.672  1.00 19.84 ? 185 ASN A CG  1 
ATOM   1467 O OD1 . ASN A 1 183 ? -3.547  28.262  -0.767  1.00 24.98 ? 185 ASN A OD1 1 
ATOM   1468 N ND2 . ASN A 1 183 ? -5.604  27.857  -1.588  1.00 21.80 ? 185 ASN A ND2 1 
ATOM   1469 N N   . THR A 1 184 ? -2.334  24.755  -4.423  1.00 25.62 ? 186 THR A N   1 
ATOM   1470 C CA  . THR A 1 184 ? -1.988  24.105  -5.676  1.00 25.31 ? 186 THR A CA  1 
ATOM   1471 C C   . THR A 1 184 ? -3.211  23.333  -6.142  1.00 24.36 ? 186 THR A C   1 
ATOM   1472 O O   . THR A 1 184 ? -3.915  22.732  -5.325  1.00 20.09 ? 186 THR A O   1 
ATOM   1473 C CB  . THR A 1 184 ? -0.795  23.148  -5.538  1.00 28.08 ? 186 THR A CB  1 
ATOM   1474 O OG1 . THR A 1 184 ? -1.188  22.030  -4.744  1.00 31.10 ? 186 THR A OG1 1 
ATOM   1475 C CG2 . THR A 1 184 ? 0.372   23.822  -4.852  1.00 30.61 ? 186 THR A CG2 1 
ATOM   1476 N N   . PRO A 1 185 ? -3.493  23.329  -7.436  1.00 25.64 ? 187 PRO A N   1 
ATOM   1477 C CA  . PRO A 1 185 ? -4.677  22.616  -7.914  1.00 23.26 ? 187 PRO A CA  1 
ATOM   1478 C C   . PRO A 1 185 ? -4.526  21.111  -7.752  1.00 27.31 ? 187 PRO A C   1 
ATOM   1479 O O   . PRO A 1 185 ? -3.431  20.558  -7.848  1.00 28.10 ? 187 PRO A O   1 
ATOM   1480 C CB  . PRO A 1 185 ? -4.774  23.011  -9.391  1.00 28.93 ? 187 PRO A CB  1 
ATOM   1481 C CG  . PRO A 1 185 ? -3.470  23.618  -9.752  1.00 31.33 ? 187 PRO A CG  1 
ATOM   1482 C CD  . PRO A 1 185 ? -2.723  23.980  -8.503  1.00 31.11 ? 187 PRO A CD  1 
ATOM   1483 N N   . ILE A 1 186 ? -5.655  20.462  -7.473  1.00 26.98 ? 188 ILE A N   1 
ATOM   1484 C CA  . ILE A 1 186 ? -5.706  19.005  -7.389  1.00 28.92 ? 188 ILE A CA  1 
ATOM   1485 C C   . ILE A 1 186 ? -5.848  18.390  -8.774  1.00 31.83 ? 188 ILE A C   1 
ATOM   1486 O O   . ILE A 1 186 ? -5.166  17.414  -9.105  1.00 33.32 ? 188 ILE A O   1 
ATOM   1487 C CB  . ILE A 1 186 ? -6.858  18.575  -6.466  1.00 28.22 ? 188 ILE A CB  1 
ATOM   1488 C CG1 . ILE A 1 186 ? -6.615  19.064  -5.037  1.00 25.49 ? 188 ILE A CG1 1 
ATOM   1489 C CG2 . ILE A 1 186 ? -7.072  17.068  -6.520  1.00 30.47 ? 188 ILE A CG2 1 
ATOM   1490 C CD1 . ILE A 1 186 ? -7.760  18.735  -4.090  1.00 22.47 ? 188 ILE A CD1 1 
ATOM   1491 N N   . GLY A 1 187 ? -6.731  18.950  -9.597  1.00 31.89 ? 189 GLY A N   1 
ATOM   1492 C CA  . GLY A 1 187 ? -7.002  18.400  -10.904 1.00 34.31 ? 189 GLY A CA  1 
ATOM   1493 C C   . GLY A 1 187 ? -5.857  18.617  -11.869 1.00 39.72 ? 189 GLY A C   1 
ATOM   1494 O O   . GLY A 1 187 ? -4.815  19.190  -11.553 1.00 34.56 ? 189 GLY A O   1 
ATOM   1495 N N   . ASP A 1 188 ? -6.063  18.124  -13.088 1.00 39.52 ? 190 ASP A N   1 
ATOM   1496 C CA  . ASP A 1 188 ? -5.132  18.338  -14.185 1.00 43.22 ? 190 ASP A CA  1 
ATOM   1497 C C   . ASP A 1 188 ? -5.616  19.403  -15.160 1.00 47.14 ? 190 ASP A C   1 
ATOM   1498 O O   . ASP A 1 188 ? -4.939  19.661  -16.158 1.00 51.84 ? 190 ASP A O   1 
ATOM   1499 C CB  . ASP A 1 188 ? -4.894  17.026  -14.939 1.00 46.38 ? 190 ASP A CB  1 
ATOM   1500 C CG  . ASP A 1 188 ? -4.736  15.839  -14.009 1.00 46.57 ? 190 ASP A CG  1 
ATOM   1501 O OD1 . ASP A 1 188 ? -3.876  15.907  -13.110 1.00 44.99 ? 190 ASP A OD1 1 
ATOM   1502 O OD2 . ASP A 1 188 ? -5.456  14.830  -14.192 1.00 46.63 ? 190 ASP A OD2 1 
ATOM   1503 N N   . GLY A 1 189 ? -6.802  19.917  -14.914 1.00 47.10 ? 191 GLY A N   1 
ATOM   1504 C CA  . GLY A 1 189 ? -7.415  20.833  -15.825 1.00 52.50 ? 191 GLY A CA  1 
ATOM   1505 C C   . GLY A 1 189 ? -6.590  22.050  -16.092 1.00 55.16 ? 191 GLY A C   1 
ATOM   1506 O O   . GLY A 1 189 ? -5.473  22.222  -15.628 1.00 56.74 ? 191 GLY A O   1 
ATOM   1507 N N   . PRO A 1 190 ? -7.185  22.917  -16.867 1.00 56.43 ? 192 PRO A N   1 
ATOM   1508 C CA  . PRO A 1 190 ? -6.624  24.225  -17.097 1.00 55.27 ? 192 PRO A CA  1 
ATOM   1509 C C   . PRO A 1 190 ? -6.987  25.061  -15.911 1.00 54.06 ? 192 PRO A C   1 
ATOM   1510 O O   . PRO A 1 190 ? -8.136  25.051  -15.511 1.00 54.84 ? 192 PRO A O   1 
ATOM   1511 C CB  . PRO A 1 190 ? -7.417  24.716  -18.299 1.00 55.13 ? 192 PRO A CB  1 
ATOM   1512 C CG  . PRO A 1 190 ? -8.484  23.651  -18.586 1.00 54.94 ? 192 PRO A CG  1 
ATOM   1513 C CD  . PRO A 1 190 ? -8.544  22.793  -17.408 1.00 56.75 ? 192 PRO A CD  1 
ATOM   1514 N N   . VAL A 1 191 ? -6.040  25.794  -15.384 1.00 52.74 ? 193 VAL A N   1 
ATOM   1515 C CA  . VAL A 1 191 ? -6.321  26.646  -14.247 1.00 49.76 ? 193 VAL A CA  1 
ATOM   1516 C C   . VAL A 1 191 ? -5.832  28.075  -14.462 1.00 47.61 ? 193 VAL A C   1 
ATOM   1517 O O   . VAL A 1 191 ? -4.726  28.271  -14.876 1.00 50.22 ? 193 VAL A O   1 
ATOM   1518 C CB  . VAL A 1 191 ? -5.657  26.037  -12.993 1.00 49.43 ? 193 VAL A CB  1 
ATOM   1519 C CG1 . VAL A 1 191 ? -5.119  27.064  -12.127 1.00 45.76 ? 193 VAL A CG1 1 
ATOM   1520 C CG2 . VAL A 1 191 ? -6.596  25.110  -12.265 1.00 43.63 ? 193 VAL A CG2 1 
ATOM   1521 N N   . LEU A 1 192 ? -6.640  29.064  -14.125 1.00 50.40 ? 194 LEU A N   1 
ATOM   1522 C CA  . LEU A 1 192 ? -6.267  30.458  -14.361 1.00 49.18 ? 194 LEU A CA  1 
ATOM   1523 C C   . LEU A 1 192 ? -5.311  30.913  -13.264 1.00 46.09 ? 194 LEU A C   1 
ATOM   1524 O O   . LEU A 1 192 ? -5.726  31.148  -12.126 1.00 46.16 ? 194 LEU A O   1 
ATOM   1525 C CB  . LEU A 1 192 ? -7.511  31.345  -14.379 1.00 49.44 ? 194 LEU A CB  1 
ATOM   1526 C CG  . LEU A 1 192 ? -8.692  31.068  -15.321 1.00 51.33 ? 194 LEU A CG  1 
ATOM   1527 C CD1 . LEU A 1 192 ? -9.998  31.480  -14.658 1.00 49.35 ? 194 LEU A CD1 1 
ATOM   1528 C CD2 . LEU A 1 192 ? -8.530  31.805  -16.642 1.00 53.64 ? 194 LEU A CD2 1 
ATOM   1529 N N   . LEU A 1 193 ? -4.035  31.059  -13.600 1.00 40.42 ? 195 LEU A N   1 
ATOM   1530 C CA  . LEU A 1 193 ? -3.090  31.682  -12.677 1.00 40.47 ? 195 LEU A CA  1 
ATOM   1531 C C   . LEU A 1 193 ? -3.343  33.187  -12.683 1.00 35.92 ? 195 LEU A C   1 
ATOM   1532 O O   . LEU A 1 193 ? -3.272  33.808  -13.753 1.00 35.68 ? 195 LEU A O   1 
ATOM   1533 C CB  . LEU A 1 193 ? -1.654  31.374  -13.089 1.00 38.85 ? 195 LEU A CB  1 
ATOM   1534 C CG  . LEU A 1 193 ? -0.646  30.939  -12.028 1.00 43.82 ? 195 LEU A CG  1 
ATOM   1535 C CD1 . LEU A 1 193 ? -1.028  29.589  -11.457 1.00 44.49 ? 195 LEU A CD1 1 
ATOM   1536 C CD2 . LEU A 1 193 ? 0.763   30.910  -12.588 1.00 46.89 ? 195 LEU A CD2 1 
ATOM   1537 N N   . PRO A 1 194 ? -3.643  33.812  -11.546 1.00 32.45 ? 196 PRO A N   1 
ATOM   1538 C CA  . PRO A 1 194 ? -4.129  35.197  -11.555 1.00 31.80 ? 196 PRO A CA  1 
ATOM   1539 C C   . PRO A 1 194 ? -3.010  36.235  -11.559 1.00 29.37 ? 196 PRO A C   1 
ATOM   1540 O O   . PRO A 1 194 ? -1.861  35.960  -11.218 1.00 29.64 ? 196 PRO A O   1 
ATOM   1541 C CB  . PRO A 1 194 ? -4.912  35.287  -10.237 1.00 30.12 ? 196 PRO A CB  1 
ATOM   1542 C CG  . PRO A 1 194 ? -4.125  34.373  -9.317  1.00 31.01 ? 196 PRO A CG  1 
ATOM   1543 C CD  . PRO A 1 194 ? -3.768  33.195  -10.209 1.00 32.74 ? 196 PRO A CD  1 
ATOM   1544 N N   . ASP A 1 195 ? -3.376  37.449  -11.963 1.00 28.61 ? 197 ASP A N   1 
ATOM   1545 C CA  . ASP A 1 195 ? -2.605  38.627  -11.599 1.00 31.73 ? 197 ASP A CA  1 
ATOM   1546 C C   . ASP A 1 195 ? -2.702  38.840  -10.093 1.00 26.07 ? 197 ASP A C   1 
ATOM   1547 O O   . ASP A 1 195 ? -3.704  38.498  -9.463  1.00 26.14 ? 197 ASP A O   1 
ATOM   1548 C CB  . ASP A 1 195 ? -3.128  39.860  -12.339 1.00 33.09 ? 197 ASP A CB  1 
ATOM   1549 C CG  . ASP A 1 195 ? -2.740  39.878  -13.818 1.00 32.99 ? 197 ASP A CG  1 
ATOM   1550 O OD1 . ASP A 1 195 ? -1.852  39.103  -14.217 1.00 32.78 ? 197 ASP A OD1 1 
ATOM   1551 O OD2 . ASP A 1 195 ? -3.362  40.639  -14.590 1.00 36.73 ? 197 ASP A OD2 1 
ATOM   1552 N N   . ASN A 1 196 ? -1.655  39.405  -9.512  1.00 27.10 ? 198 ASN A N   1 
ATOM   1553 C CA  . ASN A 1 196 ? -1.656  39.627  -8.071  1.00 24.70 ? 198 ASN A CA  1 
ATOM   1554 C C   . ASN A 1 196 ? -2.771  40.601  -7.696  1.00 25.75 ? 198 ASN A C   1 
ATOM   1555 O O   . ASN A 1 196 ? -3.056  41.555  -8.425  1.00 25.54 ? 198 ASN A O   1 
ATOM   1556 C CB  . ASN A 1 196 ? -0.287  40.146  -7.625  1.00 26.25 ? 198 ASN A CB  1 
ATOM   1557 C CG  . ASN A 1 196 ? 0.841   39.164  -7.919  1.00 23.09 ? 198 ASN A CG  1 
ATOM   1558 O OD1 . ASN A 1 196 ? 0.610   38.050  -8.380  1.00 26.45 ? 198 ASN A OD1 1 
ATOM   1559 N ND2 . ASN A 1 196 ? 2.069   39.585  -7.667  1.00 29.57 ? 198 ASN A ND2 1 
ATOM   1560 N N   . HIS A 1 197 ? -3.436  40.334  -6.574  1.00 23.55 ? 199 HIS A N   1 
ATOM   1561 C CA  . HIS A 1 197 ? -4.606  41.104  -6.153  1.00 20.58 ? 199 HIS A CA  1 
ATOM   1562 C C   . HIS A 1 197 ? -4.896  40.770  -4.697  1.00 22.13 ? 199 HIS A C   1 
ATOM   1563 O O   . HIS A 1 197 ? -4.349  39.812  -4.146  1.00 19.61 ? 199 HIS A O   1 
ATOM   1564 C CB  . HIS A 1 197 ? -5.833  40.805  -7.021  1.00 23.66 ? 199 HIS A CB  1 
ATOM   1565 C CG  . HIS A 1 197 ? -6.329  39.397  -6.885  1.00 24.03 ? 199 HIS A CG  1 
ATOM   1566 N ND1 . HIS A 1 197 ? -5.738  38.334  -7.536  1.00 23.73 ? 199 HIS A ND1 1 
ATOM   1567 C CD2 . HIS A 1 197 ? -7.312  38.870  -6.119  1.00 23.59 ? 199 HIS A CD2 1 
ATOM   1568 C CE1 . HIS A 1 197 ? -6.370  37.220  -7.215  1.00 26.11 ? 199 HIS A CE1 1 
ATOM   1569 N NE2 . HIS A 1 197 ? -7.324  37.517  -6.351  1.00 20.70 ? 199 HIS A NE2 1 
ATOM   1570 N N   . TYR A 1 198 ? -5.785  41.556  -4.086  1.00 22.24 ? 200 TYR A N   1 
ATOM   1571 C CA  . TYR A 1 198 ? -6.148  41.368  -2.687  1.00 21.66 ? 200 TYR A CA  1 
ATOM   1572 C C   . TYR A 1 198 ? -7.496  40.674  -2.558  1.00 24.34 ? 200 TYR A C   1 
ATOM   1573 O O   . TYR A 1 198 ? -8.392  40.855  -3.383  1.00 24.75 ? 200 TYR A O   1 
ATOM   1574 C CB  . TYR A 1 198 ? -6.238  42.696  -1.926  1.00 22.97 ? 200 TYR A CB  1 
ATOM   1575 C CG  . TYR A 1 198 ? -4.925  43.384  -1.647  1.00 24.39 ? 200 TYR A CG  1 
ATOM   1576 C CD1 . TYR A 1 198 ? -4.185  43.064  -0.519  1.00 21.97 ? 200 TYR A CD1 1 
ATOM   1577 C CD2 . TYR A 1 198 ? -4.456  44.397  -2.478  1.00 25.54 ? 200 TYR A CD2 1 
ATOM   1578 C CE1 . TYR A 1 198 ? -2.988  43.697  -0.243  1.00 24.23 ? 200 TYR A CE1 1 
ATOM   1579 C CE2 . TYR A 1 198 ? -3.256  45.041  -2.210  1.00 23.80 ? 200 TYR A CE2 1 
ATOM   1580 C CZ  . TYR A 1 198 ? -2.528  44.678  -1.092  1.00 27.50 ? 200 TYR A CZ  1 
ATOM   1581 O OH  . TYR A 1 198 ? -1.344  45.303  -0.810  1.00 26.85 ? 200 TYR A OH  1 
ATOM   1582 N N   . LEU A 1 199 ? -7.634  39.897  -1.493  1.00 20.43 ? 201 LEU A N   1 
ATOM   1583 C CA  . LEU A 1 199 ? -8.931  39.505  -0.954  1.00 20.49 ? 201 LEU A CA  1 
ATOM   1584 C C   . LEU A 1 199 ? -9.171  40.274  0.340   1.00 24.39 ? 201 LEU A C   1 
ATOM   1585 O O   . LEU A 1 199 ? -8.302  40.304  1.220   1.00 23.50 ? 201 LEU A O   1 
ATOM   1586 C CB  . LEU A 1 199 ? -8.996  38.001  -0.681  1.00 20.37 ? 201 LEU A CB  1 
ATOM   1587 C CG  . LEU A 1 199 ? -8.909  37.108  -1.905  1.00 24.28 ? 201 LEU A CG  1 
ATOM   1588 C CD1 . LEU A 1 199 ? -8.989  35.626  -1.513  1.00 22.36 ? 201 LEU A CD1 1 
ATOM   1589 C CD2 . LEU A 1 199 ? -10.038 37.485  -2.828  1.00 21.65 ? 201 LEU A CD2 1 
ATOM   1590 N N   . PHE A 1 200 ? -10.346 40.883  0.456   1.00 22.38 ? 202 PHE A N   1 
ATOM   1591 C CA  . PHE A 1 200 ? -10.741 41.618  1.648   1.00 23.02 ? 202 PHE A CA  1 
ATOM   1592 C C   . PHE A 1 200 ? -11.864 40.851  2.326   1.00 24.96 ? 202 PHE A C   1 
ATOM   1593 O O   . PHE A 1 200 ? -12.795 40.388  1.660   1.00 23.94 ? 202 PHE A O   1 
ATOM   1594 C CB  . PHE A 1 200 ? -11.187 43.048  1.298   1.00 25.80 ? 202 PHE A CB  1 
ATOM   1595 C CG  . PHE A 1 200 ? -10.122 43.857  0.603   1.00 25.04 ? 202 PHE A CG  1 
ATOM   1596 C CD1 . PHE A 1 200 ? -10.028 43.863  -0.776  1.00 30.30 ? 202 PHE A CD1 1 
ATOM   1597 C CD2 . PHE A 1 200 ? -9.182  44.557  1.330   1.00 26.16 ? 202 PHE A CD2 1 
ATOM   1598 C CE1 . PHE A 1 200 ? -9.031  44.593  -1.416  1.00 31.37 ? 202 PHE A CE1 1 
ATOM   1599 C CE2 . PHE A 1 200 ? -8.189  45.274  0.706   1.00 27.06 ? 202 PHE A CE2 1 
ATOM   1600 C CZ  . PHE A 1 200 ? -8.112  45.298  -0.672  1.00 29.78 ? 202 PHE A CZ  1 
ATOM   1601 N N   . THR A 1 201 ? -11.764 40.703  3.639   1.00 23.35 ? 203 THR A N   1 
ATOM   1602 C CA  . THR A 1 201 ? -12.682 39.881  4.409   1.00 23.60 ? 203 THR A CA  1 
ATOM   1603 C C   . THR A 1 201 ? -13.179 40.661  5.616   1.00 25.01 ? 203 THR A C   1 
ATOM   1604 O O   . THR A 1 201 ? -12.426 41.427  6.215   1.00 24.01 ? 203 THR A O   1 
ATOM   1605 C CB  . THR A 1 201 ? -11.990 38.578  4.856   1.00 20.34 ? 203 THR A CB  1 
ATOM   1606 O OG1 . THR A 1 201 ? -11.459 37.928  3.698   1.00 20.80 ? 203 THR A OG1 1 
ATOM   1607 C CG2 . THR A 1 201 ? -12.987 37.651  5.532   1.00 20.33 ? 203 THR A CG2 1 
ATOM   1608 N N   . THR A 1 202 ? -14.457 40.491  5.943   1.00 23.10 ? 204 THR A N   1 
ATOM   1609 C CA  . THR A 1 202 ? -15.015 40.979  7.198   1.00 25.03 ? 204 THR A CA  1 
ATOM   1610 C C   . THR A 1 202 ? -15.744 39.819  7.858   1.00 24.92 ? 204 THR A C   1 
ATOM   1611 O O   . THR A 1 202 ? -16.682 39.264  7.272   1.00 25.18 ? 204 THR A O   1 
ATOM   1612 C CB  . THR A 1 202 ? -15.964 42.161  6.973   1.00 26.64 ? 204 THR A CB  1 
ATOM   1613 O OG1 . THR A 1 202 ? -17.147 41.698  6.326   1.00 37.40 ? 204 THR A OG1 1 
ATOM   1614 C CG2 . THR A 1 202 ? -15.312 43.180  6.055   1.00 26.33 ? 204 THR A CG2 1 
ATOM   1615 N N   . SER A 1 203 ? -15.316 39.457  9.072   1.00 24.19 ? 205 SER A N   1 
ATOM   1616 C CA  . SER A 1 203 ? -15.832 38.301  9.797   1.00 23.49 ? 205 SER A CA  1 
ATOM   1617 C C   . SER A 1 203 ? -16.536 38.736  11.075  1.00 24.82 ? 205 SER A C   1 
ATOM   1618 O O   . SER A 1 203 ? -16.086 39.657  11.765  1.00 28.82 ? 205 SER A O   1 
ATOM   1619 C CB  . SER A 1 203 ? -14.700 37.318  10.165  1.00 23.48 ? 205 SER A CB  1 
ATOM   1620 O OG  . SER A 1 203 ? -13.822 37.107  9.072   1.00 21.65 ? 205 SER A OG  1 
ATOM   1621 N N   . THR A 1 204 ? -17.626 38.055  11.412  1.00 26.32 ? 206 THR A N   1 
ATOM   1622 C CA  . THR A 1 204 ? -18.325 38.318  12.661  1.00 28.75 ? 206 THR A CA  1 
ATOM   1623 C C   . THR A 1 204 ? -18.564 37.002  13.383  1.00 28.05 ? 206 THR A C   1 
ATOM   1624 O O   . THR A 1 204 ? -19.129 36.067  12.807  1.00 28.57 ? 206 THR A O   1 
ATOM   1625 C CB  . THR A 1 204 ? -19.652 39.052  12.422  1.00 30.13 ? 206 THR A CB  1 
ATOM   1626 O OG1 . THR A 1 204 ? -19.377 40.426  12.126  1.00 34.30 ? 206 THR A OG1 1 
ATOM   1627 C CG2 . THR A 1 204 ? -20.516 39.003  13.684  1.00 27.28 ? 206 THR A CG2 1 
ATOM   1628 N N   . LEU A 1 205 ? -18.137 36.938  14.641  1.00 25.55 ? 207 LEU A N   1 
ATOM   1629 C CA  . LEU A 1 205 ? -18.258 35.739  15.451  1.00 26.42 ? 207 LEU A CA  1 
ATOM   1630 C C   . LEU A 1 205 ? -19.396 35.908  16.453  1.00 31.56 ? 207 LEU A C   1 
ATOM   1631 O O   . LEU A 1 205 ? -19.544 36.973  17.063  1.00 32.67 ? 207 LEU A O   1 
ATOM   1632 C CB  . LEU A 1 205 ? -16.958 35.457  16.208  1.00 26.33 ? 207 LEU A CB  1 
ATOM   1633 C CG  . LEU A 1 205 ? -15.621 35.350  15.462  1.00 23.83 ? 207 LEU A CG  1 
ATOM   1634 C CD1 . LEU A 1 205 ? -14.587 34.759  16.383  1.00 26.97 ? 207 LEU A CD1 1 
ATOM   1635 C CD2 . LEU A 1 205 ? -15.719 34.556  14.227  1.00 31.35 ? 207 LEU A CD2 1 
ATOM   1636 N N   . SER A 1 206 ? -20.169 34.842  16.655  1.00 29.08 ? 208 SER A N   1 
ATOM   1637 C CA  . SER A 1 206 ? -21.306 34.880  17.568  1.00 31.77 ? 208 SER A CA  1 
ATOM   1638 C C   . SER A 1 206 ? -21.517 33.493  18.163  1.00 32.05 ? 208 SER A C   1 
ATOM   1639 O O   . SER A 1 206 ? -20.781 32.548  17.867  1.00 30.74 ? 208 SER A O   1 
ATOM   1640 C CB  . SER A 1 206 ? -22.554 35.389  16.843  1.00 32.84 ? 208 SER A CB  1 
ATOM   1641 O OG  . SER A 1 206 ? -22.889 34.519  15.784  1.00 28.61 ? 208 SER A OG  1 
ATOM   1642 N N   . LYS A 1 207 ? -22.523 33.377  19.035  1.00 31.08 ? 209 LYS A N   1 
ATOM   1643 C CA  . LYS A 1 207 ? -22.909 32.089  19.585  1.00 30.45 ? 209 LYS A CA  1 
ATOM   1644 C C   . LYS A 1 207 ? -24.373 31.827  19.273  1.00 34.29 ? 209 LYS A C   1 
ATOM   1645 O O   . LYS A 1 207 ? -25.159 32.750  19.046  1.00 33.48 ? 209 LYS A O   1 
ATOM   1646 C CB  . LYS A 1 207 ? -22.701 32.011  21.104  1.00 32.52 ? 209 LYS A CB  1 
ATOM   1647 C CG  . LYS A 1 207 ? -21.283 32.259  21.532  1.00 35.18 ? 209 LYS A CG  1 
ATOM   1648 C CD  . LYS A 1 207 ? -20.376 31.088  21.228  1.00 28.05 ? 209 LYS A CD  1 
ATOM   1649 C CE  . LYS A 1 207 ? -19.026 31.303  21.906  1.00 30.19 ? 209 LYS A CE  1 
ATOM   1650 N NZ  . LYS A 1 207 ? -18.078 30.201  21.592  1.00 27.49 ? 209 LYS A NZ  1 
ATOM   1651 N N   . ASP A 1 208 ? -24.721 30.548  19.263  1.00 32.67 ? 210 ASP A N   1 
ATOM   1652 C CA  . ASP A 1 208 ? -26.090 30.094  19.094  1.00 35.71 ? 210 ASP A CA  1 
ATOM   1653 C C   . ASP A 1 208 ? -26.669 29.813  20.474  1.00 37.77 ? 210 ASP A C   1 
ATOM   1654 O O   . ASP A 1 208 ? -26.175 28.911  21.171  1.00 34.74 ? 210 ASP A O   1 
ATOM   1655 C CB  . ASP A 1 208 ? -26.115 28.842  18.212  1.00 33.45 ? 210 ASP A CB  1 
ATOM   1656 C CG  . ASP A 1 208 ? -27.442 28.109  18.231  1.00 38.06 ? 210 ASP A CG  1 
ATOM   1657 O OD1 . ASP A 1 208 ? -28.483 28.681  18.619  1.00 39.76 ? 210 ASP A OD1 1 
ATOM   1658 O OD2 . ASP A 1 208 ? -27.440 26.942  17.789  1.00 37.76 ? 210 ASP A OD2 1 
ATOM   1659 N N   . PRO A 1 209 ? -27.696 30.548  20.916  1.00 38.20 ? 211 PRO A N   1 
ATOM   1660 C CA  . PRO A 1 209 ? -28.187 30.372  22.294  1.00 39.32 ? 211 PRO A CA  1 
ATOM   1661 C C   . PRO A 1 209 ? -28.772 29.000  22.562  1.00 40.49 ? 211 PRO A C   1 
ATOM   1662 O O   . PRO A 1 209 ? -28.941 28.636  23.734  1.00 43.13 ? 211 PRO A O   1 
ATOM   1663 C CB  . PRO A 1 209 ? -29.246 31.471  22.451  1.00 41.58 ? 211 PRO A CB  1 
ATOM   1664 C CG  . PRO A 1 209 ? -29.425 32.094  21.123  1.00 39.00 ? 211 PRO A CG  1 
ATOM   1665 C CD  . PRO A 1 209 ? -28.549 31.434  20.113  1.00 40.15 ? 211 PRO A CD  1 
ATOM   1666 N N   . ASN A 1 210 ? -29.058 28.219  21.527  1.00 39.08 ? 212 ASN A N   1 
ATOM   1667 C CA  . ASN A 1 210 ? -29.628 26.892  21.686  1.00 40.81 ? 212 ASN A CA  1 
ATOM   1668 C C   . ASN A 1 210 ? -28.577 25.783  21.642  1.00 42.53 ? 212 ASN A C   1 
ATOM   1669 O O   . ASN A 1 210 ? -28.944 24.603  21.701  1.00 44.03 ? 212 ASN A O   1 
ATOM   1670 C CB  . ASN A 1 210 ? -30.688 26.666  20.596  1.00 42.48 ? 212 ASN A CB  1 
ATOM   1671 C CG  . ASN A 1 210 ? -32.053 27.217  20.988  1.00 42.18 ? 212 ASN A CG  1 
ATOM   1672 O OD1 . ASN A 1 210 ? -32.531 26.996  22.101  1.00 41.98 ? 212 ASN A OD1 1 
ATOM   1673 N ND2 . ASN A 1 210 ? -32.664 27.976  20.087  1.00 42.61 ? 212 ASN A ND2 1 
ATOM   1674 N N   . GLU A 1 211 ? -27.284 26.120  21.550  1.00 38.31 ? 213 GLU A N   1 
ATOM   1675 C CA  . GLU A 1 211 ? -26.228 25.129  21.347  1.00 37.27 ? 213 GLU A CA  1 
ATOM   1676 C C   . GLU A 1 211 ? -25.435 24.974  22.637  1.00 37.55 ? 213 GLU A C   1 
ATOM   1677 O O   . GLU A 1 211 ? -24.864 25.949  23.142  1.00 40.53 ? 213 GLU A O   1 
ATOM   1678 C CB  . GLU A 1 211 ? -25.285 25.539  20.215  1.00 36.15 ? 213 GLU A CB  1 
ATOM   1679 C CG  . GLU A 1 211 ? -24.142 24.559  19.970  1.00 34.77 ? 213 GLU A CG  1 
ATOM   1680 C CD  . GLU A 1 211 ? -24.639 23.162  19.614  1.00 35.08 ? 213 GLU A CD  1 
ATOM   1681 O OE1 . GLU A 1 211 ? -25.172 22.988  18.499  1.00 33.67 ? 213 GLU A OE1 1 
ATOM   1682 O OE2 . GLU A 1 211 ? -24.485 22.233  20.429  1.00 37.26 ? 213 GLU A OE2 1 
ATOM   1683 N N   . LYS A 1 212 ? -25.386 23.754  23.154  1.00 36.89 ? 214 LYS A N   1 
ATOM   1684 C CA  . LYS A 1 212 ? -24.684 23.481  24.401  1.00 39.78 ? 214 LYS A CA  1 
ATOM   1685 C C   . LYS A 1 212 ? -23.259 22.996  24.185  1.00 38.84 ? 214 LYS A C   1 
ATOM   1686 O O   . LYS A 1 212 ? -22.481 22.951  25.146  1.00 37.27 ? 214 LYS A O   1 
ATOM   1687 C CB  . LYS A 1 212 ? -25.453 22.435  25.222  1.00 42.56 ? 214 LYS A CB  1 
ATOM   1688 C CG  . LYS A 1 212 ? -25.532 21.070  24.530  1.00 45.53 ? 214 LYS A CG  1 
ATOM   1689 C CD  . LYS A 1 212 ? -26.635 20.174  25.097  1.00 45.50 ? 214 LYS A CD  1 
ATOM   1690 C CE  . LYS A 1 212 ? -26.808 20.366  26.596  1.00 47.31 ? 214 LYS A CE  1 
ATOM   1691 N NZ  . LYS A 1 212 ? -28.193 20.047  27.051  1.00 48.58 ? 214 LYS A NZ  1 
ATOM   1692 N N   . ARG A 1 213 ? -22.903 22.610  22.967  1.00 37.05 ? 215 ARG A N   1 
ATOM   1693 C CA  . ARG A 1 213 ? -21.530 22.199  22.728  1.00 34.57 ? 215 ARG A CA  1 
ATOM   1694 C C   . ARG A 1 213 ? -20.662 23.427  22.480  1.00 33.77 ? 215 ARG A C   1 
ATOM   1695 O O   . ARG A 1 213 ? -21.150 24.517  22.157  1.00 31.60 ? 215 ARG A O   1 
ATOM   1696 C CB  . ARG A 1 213 ? -21.449 21.227  21.547  1.00 35.28 ? 215 ARG A CB  1 
ATOM   1697 C CG  . ARG A 1 213 ? -22.456 20.072  21.638  1.00 34.68 ? 215 ARG A CG  1 
ATOM   1698 C CD  . ARG A 1 213 ? -22.474 19.193  20.387  1.00 38.10 ? 215 ARG A CD  1 
ATOM   1699 N NE  . ARG A 1 213 ? -23.401 19.719  19.389  1.00 38.74 ? 215 ARG A NE  1 
ATOM   1700 C CZ  . ARG A 1 213 ? -23.657 19.150  18.217  1.00 37.90 ? 215 ARG A CZ  1 
ATOM   1701 N NH1 . ARG A 1 213 ? -23.109 17.992  17.873  1.00 35.42 ? 215 ARG A NH1 1 
ATOM   1702 N NH2 . ARG A 1 213 ? -24.488 19.756  17.370  1.00 35.45 ? 215 ARG A NH2 1 
ATOM   1703 N N   . ASP A 1 214 ? -19.363 23.250  22.698  1.00 33.57 ? 216 ASP A N   1 
ATOM   1704 C CA  . ASP A 1 214 ? -18.397 24.291  22.384  1.00 29.83 ? 216 ASP A CA  1 
ATOM   1705 C C   . ASP A 1 214 ? -18.465 24.596  20.901  1.00 27.44 ? 216 ASP A C   1 
ATOM   1706 O O   . ASP A 1 214 ? -18.270 23.701  20.079  1.00 26.93 ? 216 ASP A O   1 
ATOM   1707 C CB  . ASP A 1 214 ? -16.999 23.827  22.775  1.00 28.16 ? 216 ASP A CB  1 
ATOM   1708 C CG  . ASP A 1 214 ? -16.044 24.972  22.985  1.00 27.75 ? 216 ASP A CG  1 
ATOM   1709 O OD1 . ASP A 1 214 ? -16.459 26.135  22.783  1.00 34.94 ? 216 ASP A OD1 1 
ATOM   1710 O OD2 . ASP A 1 214 ? -14.887 24.711  23.376  1.00 28.49 ? 216 ASP A OD2 1 
ATOM   1711 N N   . HIS A 1 215 ? -18.741 25.847  20.550  1.00 26.32 ? 217 HIS A N   1 
ATOM   1712 C CA  . HIS A 1 215 ? -19.067 26.112  19.156  1.00 27.33 ? 217 HIS A CA  1 
ATOM   1713 C C   . HIS A 1 215 ? -18.760 27.558  18.785  1.00 27.80 ? 217 HIS A C   1 
ATOM   1714 O O   . HIS A 1 215 ? -18.474 28.406  19.639  1.00 26.30 ? 217 HIS A O   1 
ATOM   1715 C CB  . HIS A 1 215 ? -20.535 25.777  18.885  1.00 27.43 ? 217 HIS A CB  1 
ATOM   1716 C CG  . HIS A 1 215 ? -21.482 26.796  19.434  1.00 28.87 ? 217 HIS A CG  1 
ATOM   1717 N ND1 . HIS A 1 215 ? -21.761 26.895  20.779  1.00 30.09 ? 217 HIS A ND1 1 
ATOM   1718 C CD2 . HIS A 1 215 ? -22.186 27.782  18.829  1.00 29.08 ? 217 HIS A CD2 1 
ATOM   1719 C CE1 . HIS A 1 215 ? -22.604 27.892  20.980  1.00 28.93 ? 217 HIS A CE1 1 
ATOM   1720 N NE2 . HIS A 1 215 ? -22.878 28.446  19.813  1.00 30.50 ? 217 HIS A NE2 1 
ATOM   1721 N N   . MET A 1 216 ? -18.829 27.810  17.475  1.00 24.38 ? 218 MET A N   1 
ATOM   1722 C CA  . MET A 1 216 ? -18.622 29.111  16.838  1.00 23.34 ? 218 MET A CA  1 
ATOM   1723 C C   . MET A 1 216 ? -19.587 29.276  15.682  1.00 23.04 ? 218 MET A C   1 
ATOM   1724 O O   . MET A 1 216 ? -19.543 28.484  14.738  1.00 23.23 ? 218 MET A O   1 
ATOM   1725 C CB  . MET A 1 216 ? -17.194 29.273  16.300  1.00 22.66 ? 218 MET A CB  1 
ATOM   1726 C CG  . MET A 1 216 ? -16.967 30.643  15.671  1.00 23.47 ? 218 MET A CG  1 
ATOM   1727 S SD  . MET A 1 216 ? -15.252 31.014  15.217  1.00 22.17 ? 218 MET A SD  1 
ATOM   1728 C CE  . MET A 1 216 ? -14.962 29.750  13.981  1.00 19.25 ? 218 MET A CE  1 
ATOM   1729 N N   . VAL A 1 217 ? -20.414 30.320  15.731  1.00 25.94 ? 219 VAL A N   1 
ATOM   1730 C CA  . VAL A 1 217 ? -21.156 30.778  14.559  1.00 26.90 ? 219 VAL A CA  1 
ATOM   1731 C C   . VAL A 1 217 ? -20.361 31.896  13.898  1.00 27.60 ? 219 VAL A C   1 
ATOM   1732 O O   . VAL A 1 217 ? -19.840 32.798  14.568  1.00 27.37 ? 219 VAL A O   1 
ATOM   1733 C CB  . VAL A 1 217 ? -22.573 31.256  14.934  1.00 27.99 ? 219 VAL A CB  1 
ATOM   1734 C CG1 . VAL A 1 217 ? -23.281 31.837  13.704  1.00 26.62 ? 219 VAL A CG1 1 
ATOM   1735 C CG2 . VAL A 1 217 ? -23.378 30.117  15.535  1.00 26.09 ? 219 VAL A CG2 1 
ATOM   1736 N N   . LEU A 1 218 ? -20.264 31.839  12.573  1.00 25.30 ? 220 LEU A N   1 
ATOM   1737 C CA  . LEU A 1 218 ? -19.366 32.719  11.840  1.00 25.41 ? 220 LEU A CA  1 
ATOM   1738 C C   . LEU A 1 218 ? -20.085 33.259  10.618  1.00 26.90 ? 220 LEU A C   1 
ATOM   1739 O O   . LEU A 1 218 ? -20.598 32.488  9.800   1.00 28.63 ? 220 LEU A O   1 
ATOM   1740 C CB  . LEU A 1 218 ? -18.087 31.978  11.433  1.00 20.62 ? 220 LEU A CB  1 
ATOM   1741 C CG  . LEU A 1 218 ? -17.220 32.672  10.389  1.00 24.63 ? 220 LEU A CG  1 
ATOM   1742 C CD1 . LEU A 1 218 ? -16.638 33.959  10.966  1.00 27.14 ? 220 LEU A CD1 1 
ATOM   1743 C CD2 . LEU A 1 218 ? -16.087 31.743  9.973   1.00 24.27 ? 220 LEU A CD2 1 
ATOM   1744 N N   . LEU A 1 219 ? -20.119 34.578  10.507  1.00 27.82 ? 221 LEU A N   1 
ATOM   1745 C CA  . LEU A 1 219 ? -20.609 35.264  9.326   1.00 26.83 ? 221 LEU A CA  1 
ATOM   1746 C C   . LEU A 1 219 ? -19.433 35.960  8.665   1.00 29.11 ? 221 LEU A C   1 
ATOM   1747 O O   . LEU A 1 219 ? -18.656 36.652  9.337   1.00 28.98 ? 221 LEU A O   1 
ATOM   1748 C CB  . LEU A 1 219 ? -21.711 36.270  9.684   1.00 27.66 ? 221 LEU A CB  1 
ATOM   1749 C CG  . LEU A 1 219 ? -22.189 37.125  8.508   1.00 25.19 ? 221 LEU A CG  1 
ATOM   1750 C CD1 . LEU A 1 219 ? -23.088 36.358  7.576   1.00 29.37 ? 221 LEU A CD1 1 
ATOM   1751 C CD2 . LEU A 1 219 ? -22.948 38.299  9.050   1.00 24.70 ? 221 LEU A CD2 1 
ATOM   1752 N N   . GLU A 1 220 ? -19.307 35.787  7.353   1.00 23.16 ? 222 GLU A N   1 
ATOM   1753 C CA  . GLU A 1 220 ? -18.147 36.299  6.654   1.00 26.60 ? 222 GLU A CA  1 
ATOM   1754 C C   . GLU A 1 220 ? -18.562 36.842  5.293   1.00 27.52 ? 222 GLU A C   1 
ATOM   1755 O O   . GLU A 1 220 ? -19.373 36.231  4.589   1.00 27.33 ? 222 GLU A O   1 
ATOM   1756 C CB  . GLU A 1 220 ? -17.107 35.182  6.494   1.00 27.63 ? 222 GLU A CB  1 
ATOM   1757 C CG  . GLU A 1 220 ? -15.724 35.641  6.232   1.00 30.31 ? 222 GLU A CG  1 
ATOM   1758 C CD  . GLU A 1 220 ? -14.685 34.560  6.544   1.00 26.05 ? 222 GLU A CD  1 
ATOM   1759 O OE1 . GLU A 1 220 ? -14.092 34.565  7.638   1.00 28.50 ? 222 GLU A OE1 1 
ATOM   1760 O OE2 . GLU A 1 220 ? -14.437 33.731  5.660   1.00 31.87 ? 222 GLU A OE2 1 
ATOM   1761 N N   . PHE A 1 221 ? -17.992 37.985  4.928   1.00 27.36 ? 223 PHE A N   1 
ATOM   1762 C CA  . PHE A 1 221 ? -18.088 38.536  3.582   1.00 26.38 ? 223 PHE A CA  1 
ATOM   1763 C C   . PHE A 1 221 ? -16.690 38.691  3.012   1.00 26.58 ? 223 PHE A C   1 
ATOM   1764 O O   . PHE A 1 221 ? -15.783 39.133  3.711   1.00 26.20 ? 223 PHE A O   1 
ATOM   1765 C CB  . PHE A 1 221 ? -18.801 39.887  3.587   1.00 30.11 ? 223 PHE A CB  1 
ATOM   1766 C CG  . PHE A 1 221 ? -20.201 39.826  4.114   1.00 28.86 ? 223 PHE A CG  1 
ATOM   1767 C CD1 . PHE A 1 221 ? -21.258 39.557  3.257   1.00 32.52 ? 223 PHE A CD1 1 
ATOM   1768 C CD2 . PHE A 1 221 ? -20.450 39.954  5.470   1.00 30.91 ? 223 PHE A CD2 1 
ATOM   1769 C CE1 . PHE A 1 221 ? -22.552 39.481  3.732   1.00 31.43 ? 223 PHE A CE1 1 
ATOM   1770 C CE2 . PHE A 1 221 ? -21.739 39.871  5.952   1.00 32.65 ? 223 PHE A CE2 1 
ATOM   1771 C CZ  . PHE A 1 221 ? -22.788 39.638  5.078   1.00 32.33 ? 223 PHE A CZ  1 
ATOM   1772 N N   . VAL A 1 222 ? -16.498 38.308  1.756   1.00 23.91 ? 224 VAL A N   1 
ATOM   1773 C CA  . VAL A 1 222 ? -15.180 38.407  1.142   1.00 25.99 ? 224 VAL A CA  1 
ATOM   1774 C C   . VAL A 1 222 ? -15.329 38.849  -0.307  1.00 26.59 ? 224 VAL A C   1 
ATOM   1775 O O   . VAL A 1 222 ? -16.224 38.393  -1.024  1.00 27.14 ? 224 VAL A O   1 
ATOM   1776 C CB  . VAL A 1 222 ? -14.407 37.080  1.262   1.00 27.50 ? 224 VAL A CB  1 
ATOM   1777 C CG1 . VAL A 1 222 ? -15.292 35.935  0.872   1.00 29.76 ? 224 VAL A CG1 1 
ATOM   1778 C CG2 . VAL A 1 222 ? -13.106 37.118  0.442   1.00 22.58 ? 224 VAL A CG2 1 
ATOM   1779 N N   . THR A 1 223 ? -14.446 39.748  -0.731  1.00 26.07 ? 225 THR A N   1 
ATOM   1780 C CA  . THR A 1 223 ? -14.533 40.342  -2.054  1.00 25.27 ? 225 THR A CA  1 
ATOM   1781 C C   . THR A 1 223 ? -13.120 40.583  -2.563  1.00 27.10 ? 225 THR A C   1 
ATOM   1782 O O   . THR A 1 223 ? -12.219 40.885  -1.780  1.00 29.87 ? 225 THR A O   1 
ATOM   1783 C CB  . THR A 1 223 ? -15.348 41.646  -2.010  1.00 30.71 ? 225 THR A CB  1 
ATOM   1784 O OG1 . THR A 1 223 ? -15.164 42.378  -3.227  1.00 37.08 ? 225 THR A OG1 1 
ATOM   1785 C CG2 . THR A 1 223 ? -14.925 42.520  -0.845  1.00 31.76 ? 225 THR A CG2 1 
ATOM   1786 N N   . ALA A 1 224 ? -12.922 40.414  -3.862  1.00 25.72 ? 226 ALA A N   1 
ATOM   1787 C CA  . ALA A 1 224 ? -11.637 40.699  -4.478  1.00 27.96 ? 226 ALA A CA  1 
ATOM   1788 C C   . ALA A 1 224 ? -11.606 42.138  -4.981  1.00 36.86 ? 226 ALA A C   1 
ATOM   1789 O O   . ALA A 1 224 ? -12.648 42.741  -5.255  1.00 40.20 ? 226 ALA A O   1 
ATOM   1790 C CB  . ALA A 1 224 ? -11.356 39.730  -5.631  1.00 30.57 ? 226 ALA A CB  1 
ATOM   1791 N N   . ASP A 1 225 ? -10.400 42.693  -5.062  1.00 38.94 ? 227 ASP A N   1 
ATOM   1792 C CA  . ASP A 1 225 ? -10.180 44.034  -5.608  1.00 39.54 ? 227 ASP A CA  1 
ATOM   1793 C C   . ASP A 1 225 ? -8.674  44.327  -5.649  1.00 41.84 ? 227 ASP A C   1 
ATOM   1794 O O   . ASP A 1 225 ? -7.834  43.437  -5.423  1.00 36.11 ? 227 ASP A O   1 
ATOM   1795 C CB  . ASP A 1 225 ? -10.922 45.104  -4.782  1.00 43.47 ? 227 ASP A CB  1 
ATOM   1796 C CG  . ASP A 1 225 ? -10.542 46.531  -5.178  1.00 49.23 ? 227 ASP A CG  1 
ATOM   1797 O OD1 . ASP A 1 225 ? -10.290 46.777  -6.379  1.00 58.18 ? 227 ASP A OD1 1 
ATOM   1798 O OD2 . ASP A 1 225 ? -10.493 47.410  -4.290  1.00 47.66 ? 227 ASP A OD2 1 
ATOM   1799 N N   . LYS B 1 3   ? 15.282  1.495   65.999  1.00 53.11 ? 3   LYS B N   1 
ATOM   1800 C CA  . LYS B 1 3   ? 14.559  2.151   64.919  1.00 47.63 ? 3   LYS B CA  1 
ATOM   1801 C C   . LYS B 1 3   ? 15.010  1.650   63.550  1.00 45.80 ? 3   LYS B C   1 
ATOM   1802 O O   . LYS B 1 3   ? 16.187  1.347   63.339  1.00 46.13 ? 3   LYS B O   1 
ATOM   1803 C CB  . LYS B 1 3   ? 14.737  3.673   64.994  1.00 47.24 ? 3   LYS B CB  1 
ATOM   1804 C CG  . LYS B 1 3   ? 13.716  4.436   65.861  1.00 48.95 ? 3   LYS B CG  1 
ATOM   1805 C CD  . LYS B 1 3   ? 12.326  3.775   65.959  1.00 48.01 ? 3   LYS B CD  1 
ATOM   1806 C CE  . LYS B 1 3   ? 11.589  3.722   64.606  1.00 48.06 ? 3   LYS B CE  1 
ATOM   1807 N NZ  . LYS B 1 3   ? 10.326  2.921   64.673  1.00 50.74 ? 3   LYS B NZ  1 
ATOM   1808 N N   . GLY B 1 4   ? 14.059  1.536   62.621  1.00 38.26 ? 4   GLY B N   1 
ATOM   1809 C CA  . GLY B 1 4   ? 14.426  1.358   61.226  1.00 33.79 ? 4   GLY B CA  1 
ATOM   1810 C C   . GLY B 1 4   ? 15.237  2.508   60.673  1.00 31.50 ? 4   GLY B C   1 
ATOM   1811 O O   . GLY B 1 4   ? 15.990  2.324   59.714  1.00 29.03 ? 4   GLY B O   1 
ATOM   1812 N N   . GLU B 1 5   ? 15.124  3.687   61.285  1.00 35.41 ? 5   GLU B N   1 
ATOM   1813 C CA  . GLU B 1 5   ? 15.901  4.835   60.836  1.00 36.65 ? 5   GLU B CA  1 
ATOM   1814 C C   . GLU B 1 5   ? 17.392  4.536   60.887  1.00 38.08 ? 5   GLU B C   1 
ATOM   1815 O O   . GLU B 1 5   ? 18.155  5.036   60.056  1.00 37.93 ? 5   GLU B O   1 
ATOM   1816 C CB  . GLU B 1 5   ? 15.552  6.052   61.702  1.00 40.62 ? 5   GLU B CB  1 
ATOM   1817 C CG  . GLU B 1 5   ? 15.954  7.439   61.153  1.00 49.19 ? 5   GLU B CG  1 
ATOM   1818 C CD  . GLU B 1 5   ? 17.453  7.633   60.948  1.00 52.59 ? 5   GLU B CD  1 
ATOM   1819 O OE1 . GLU B 1 5   ? 18.190  7.720   61.960  1.00 55.93 ? 5   GLU B OE1 1 
ATOM   1820 O OE2 . GLU B 1 5   ? 17.893  7.717   59.770  1.00 48.61 ? 5   GLU B OE2 1 
ATOM   1821 N N   . GLU B 1 6   ? 17.827  3.709   61.840  1.00 41.07 ? 6   GLU B N   1 
ATOM   1822 C CA  . GLU B 1 6   ? 19.250  3.439   61.993  1.00 39.75 ? 6   GLU B CA  1 
ATOM   1823 C C   . GLU B 1 6   ? 19.793  2.584   60.858  1.00 34.32 ? 6   GLU B C   1 
ATOM   1824 O O   . GLU B 1 6   ? 21.010  2.524   60.666  1.00 33.77 ? 6   GLU B O   1 
ATOM   1825 C CB  . GLU B 1 6   ? 19.505  2.773   63.352  1.00 45.77 ? 6   GLU B CB  1 
ATOM   1826 C CG  . GLU B 1 6   ? 19.246  3.707   64.547  1.00 47.35 ? 6   GLU B CG  1 
ATOM   1827 C CD  . GLU B 1 6   ? 20.057  5.002   64.503  1.00 54.94 ? 6   GLU B CD  1 
ATOM   1828 O OE1 . GLU B 1 6   ? 21.178  5.010   63.941  1.00 52.93 ? 6   GLU B OE1 1 
ATOM   1829 O OE2 . GLU B 1 6   ? 19.556  6.026   65.019  1.00 59.50 ? 6   GLU B OE2 1 
ATOM   1830 N N   . LEU B 1 7   ? 18.913  1.949   60.089  1.00 32.77 ? 7   LEU B N   1 
ATOM   1831 C CA  . LEU B 1 7   ? 19.304  1.195   58.908  1.00 33.09 ? 7   LEU B CA  1 
ATOM   1832 C C   . LEU B 1 7   ? 19.700  2.103   57.749  1.00 30.86 ? 7   LEU B C   1 
ATOM   1833 O O   . LEU B 1 7   ? 20.203  1.599   56.740  1.00 29.73 ? 7   LEU B O   1 
ATOM   1834 C CB  . LEU B 1 7   ? 18.145  0.276   58.511  1.00 31.95 ? 7   LEU B CB  1 
ATOM   1835 C CG  . LEU B 1 7   ? 17.847  -0.904  59.446  1.00 31.79 ? 7   LEU B CG  1 
ATOM   1836 C CD1 . LEU B 1 7   ? 16.833  -1.857  58.838  1.00 26.09 ? 7   LEU B CD1 1 
ATOM   1837 C CD2 . LEU B 1 7   ? 19.124  -1.672  59.780  1.00 30.95 ? 7   LEU B CD2 1 
ATOM   1838 N N   . PHE B 1 8   ? 19.527  3.423   57.878  1.00 30.19 ? 8   PHE B N   1 
ATOM   1839 C CA  . PHE B 1 8   ? 19.781  4.344   56.772  1.00 33.33 ? 8   PHE B CA  1 
ATOM   1840 C C   . PHE B 1 8   ? 20.863  5.383   57.049  1.00 35.60 ? 8   PHE B C   1 
ATOM   1841 O O   . PHE B 1 8   ? 21.035  6.304   56.238  1.00 35.34 ? 8   PHE B O   1 
ATOM   1842 C CB  . PHE B 1 8   ? 18.500  5.082   56.379  1.00 30.40 ? 8   PHE B CB  1 
ATOM   1843 C CG  . PHE B 1 8   ? 17.460  4.200   55.772  1.00 27.59 ? 8   PHE B CG  1 
ATOM   1844 C CD1 . PHE B 1 8   ? 16.594  3.480   56.571  1.00 26.45 ? 8   PHE B CD1 1 
ATOM   1845 C CD2 . PHE B 1 8   ? 17.361  4.079   54.397  1.00 25.60 ? 8   PHE B CD2 1 
ATOM   1846 C CE1 . PHE B 1 8   ? 15.640  2.680   56.021  1.00 23.35 ? 8   PHE B CE1 1 
ATOM   1847 C CE2 . PHE B 1 8   ? 16.396  3.256   53.832  1.00 22.37 ? 8   PHE B CE2 1 
ATOM   1848 C CZ  . PHE B 1 8   ? 15.548  2.555   54.644  1.00 24.05 ? 8   PHE B CZ  1 
ATOM   1849 N N   . THR B 1 9   ? 21.595  5.285   58.158  1.00 34.63 ? 9   THR B N   1 
ATOM   1850 C CA  . THR B 1 9   ? 22.604  6.307   58.408  1.00 35.94 ? 9   THR B CA  1 
ATOM   1851 C C   . THR B 1 9   ? 23.756  6.254   57.413  1.00 35.02 ? 9   THR B C   1 
ATOM   1852 O O   . THR B 1 9   ? 24.544  7.204   57.359  1.00 36.87 ? 9   THR B O   1 
ATOM   1853 C CB  . THR B 1 9   ? 23.155  6.197   59.833  1.00 38.51 ? 9   THR B CB  1 
ATOM   1854 O OG1 . THR B 1 9   ? 23.489  4.831   60.126  1.00 39.06 ? 9   THR B OG1 1 
ATOM   1855 C CG2 . THR B 1 9   ? 22.120  6.712   60.843  1.00 40.19 ? 9   THR B CG2 1 
ATOM   1856 N N   . GLY B 1 10  ? 23.864  5.199   56.610  1.00 34.38 ? 10  GLY B N   1 
ATOM   1857 C CA  . GLY B 1 10  ? 24.922  5.144   55.622  1.00 33.51 ? 10  GLY B CA  1 
ATOM   1858 C C   . GLY B 1 10  ? 24.441  4.932   54.197  1.00 32.83 ? 10  GLY B C   1 
ATOM   1859 O O   . GLY B 1 10  ? 23.264  5.145   53.882  1.00 28.12 ? 10  GLY B O   1 
ATOM   1860 N N   . VAL B 1 11  ? 25.352  4.520   53.324  1.00 28.03 ? 11  VAL B N   1 
ATOM   1861 C CA  . VAL B 1 11  ? 25.001  4.214   51.941  1.00 29.42 ? 11  VAL B CA  1 
ATOM   1862 C C   . VAL B 1 11  ? 24.387  2.820   51.897  1.00 29.24 ? 11  VAL B C   1 
ATOM   1863 O O   . VAL B 1 11  ? 24.942  1.867   52.452  1.00 25.88 ? 11  VAL B O   1 
ATOM   1864 C CB  . VAL B 1 11  ? 26.239  4.317   51.038  1.00 31.33 ? 11  VAL B CB  1 
ATOM   1865 C CG1 . VAL B 1 11  ? 25.961  3.723   49.669  1.00 33.13 ? 11  VAL B CG1 1 
ATOM   1866 C CG2 . VAL B 1 11  ? 26.694  5.763   50.935  1.00 34.87 ? 11  VAL B CG2 1 
ATOM   1867 N N   . VAL B 1 12  ? 23.227  2.699   51.261  1.00 23.65 ? 12  VAL B N   1 
ATOM   1868 C CA  . VAL B 1 12  ? 22.447  1.469   51.255  1.00 23.59 ? 12  VAL B CA  1 
ATOM   1869 C C   . VAL B 1 12  ? 22.355  0.980   49.818  1.00 24.55 ? 12  VAL B C   1 
ATOM   1870 O O   . VAL B 1 12  ? 21.846  1.698   48.953  1.00 22.49 ? 12  VAL B O   1 
ATOM   1871 C CB  . VAL B 1 12  ? 21.039  1.676   51.837  1.00 24.99 ? 12  VAL B CB  1 
ATOM   1872 C CG1 . VAL B 1 12  ? 20.231  0.386   51.805  1.00 22.50 ? 12  VAL B CG1 1 
ATOM   1873 C CG2 . VAL B 1 12  ? 21.135  2.214   53.249  1.00 24.56 ? 12  VAL B CG2 1 
ATOM   1874 N N   . PRO B 1 13  ? 22.806  -0.232  49.516  1.00 25.75 ? 13  PRO B N   1 
ATOM   1875 C CA  . PRO B 1 13  ? 22.592  -0.769  48.171  1.00 21.99 ? 13  PRO B CA  1 
ATOM   1876 C C   . PRO B 1 13  ? 21.113  -1.015  47.933  1.00 22.48 ? 13  PRO B C   1 
ATOM   1877 O O   . PRO B 1 13  ? 20.365  -1.385  48.843  1.00 19.97 ? 13  PRO B O   1 
ATOM   1878 C CB  . PRO B 1 13  ? 23.379  -2.082  48.169  1.00 25.04 ? 13  PRO B CB  1 
ATOM   1879 C CG  . PRO B 1 13  ? 23.714  -2.378  49.608  1.00 21.77 ? 13  PRO B CG  1 
ATOM   1880 C CD  . PRO B 1 13  ? 23.337  -1.225  50.467  1.00 22.25 ? 13  PRO B CD  1 
ATOM   1881 N N   . ILE B 1 14  ? 20.691  -0.809  46.688  1.00 20.56 ? 14  ILE B N   1 
ATOM   1882 C CA  . ILE B 1 14  ? 19.288  -0.917  46.300  1.00 16.51 ? 14  ILE B CA  1 
ATOM   1883 C C   . ILE B 1 14  ? 19.177  -1.925  45.168  1.00 18.00 ? 14  ILE B C   1 
ATOM   1884 O O   . ILE B 1 14  ? 20.020  -1.945  44.262  1.00 19.82 ? 14  ILE B O   1 
ATOM   1885 C CB  . ILE B 1 14  ? 18.708  0.443   45.853  1.00 15.80 ? 14  ILE B CB  1 
ATOM   1886 C CG1 . ILE B 1 14  ? 18.765  1.453   46.992  1.00 18.96 ? 14  ILE B CG1 1 
ATOM   1887 C CG2 . ILE B 1 14  ? 17.266  0.277   45.389  1.00 19.70 ? 14  ILE B CG2 1 
ATOM   1888 C CD1 . ILE B 1 14  ? 18.483  2.881   46.541  1.00 19.62 ? 14  ILE B CD1 1 
ATOM   1889 N N   . LEU B 1 15  ? 18.137  -2.762  45.220  1.00 17.98 ? 15  LEU B N   1 
ATOM   1890 C CA  . LEU B 1 15  ? 17.778  -3.635  44.112  1.00 17.45 ? 15  LEU B CA  1 
ATOM   1891 C C   . LEU B 1 15  ? 16.304  -3.413  43.784  1.00 18.37 ? 15  LEU B C   1 
ATOM   1892 O O   . LEU B 1 15  ? 15.467  -3.357  44.686  1.00 17.55 ? 15  LEU B O   1 
ATOM   1893 C CB  . LEU B 1 15  ? 18.072  -5.108  44.460  1.00 22.97 ? 15  LEU B CB  1 
ATOM   1894 C CG  . LEU B 1 15  ? 17.424  -6.224  43.632  1.00 25.69 ? 15  LEU B CG  1 
ATOM   1895 C CD1 . LEU B 1 15  ? 18.196  -6.424  42.333  1.00 26.81 ? 15  LEU B CD1 1 
ATOM   1896 C CD2 . LEU B 1 15  ? 17.402  -7.527  44.411  1.00 27.16 ? 15  LEU B CD2 1 
ATOM   1897 N N   . VAL B 1 16  ? 15.984  -3.286  42.497  1.00 18.46 ? 16  VAL B N   1 
ATOM   1898 C CA  . VAL B 1 16  ? 14.606  -3.118  42.063  1.00 18.45 ? 16  VAL B CA  1 
ATOM   1899 C C   . VAL B 1 16  ? 14.288  -4.199  41.043  1.00 19.37 ? 16  VAL B C   1 
ATOM   1900 O O   . VAL B 1 16  ? 15.113  -4.498  40.173  1.00 19.39 ? 16  VAL B O   1 
ATOM   1901 C CB  . VAL B 1 16  ? 14.368  -1.709  41.471  1.00 17.17 ? 16  VAL B CB  1 
ATOM   1902 C CG1 . VAL B 1 16  ? 12.884  -1.516  41.119  1.00 19.70 ? 16  VAL B CG1 1 
ATOM   1903 C CG2 . VAL B 1 16  ? 14.815  -0.646  42.464  1.00 15.57 ? 16  VAL B CG2 1 
ATOM   1904 N N   . GLU B 1 17  ? 13.095  -4.784  41.149  1.00 15.85 ? 17  GLU B N   1 
ATOM   1905 C CA  . GLU B 1 17  ? 12.622  -5.762  40.177  1.00 17.89 ? 17  GLU B CA  1 
ATOM   1906 C C   . GLU B 1 17  ? 11.166  -5.464  39.856  1.00 18.24 ? 17  GLU B C   1 
ATOM   1907 O O   . GLU B 1 17  ? 10.342  -5.322  40.764  1.00 18.56 ? 17  GLU B O   1 
ATOM   1908 C CB  . GLU B 1 17  ? 12.762  -7.197  40.700  1.00 21.04 ? 17  GLU B CB  1 
ATOM   1909 C CG  . GLU B 1 17  ? 14.202  -7.592  41.067  1.00 28.13 ? 17  GLU B CG  1 
ATOM   1910 C CD  . GLU B 1 17  ? 15.129  -7.758  39.861  1.00 31.73 ? 17  GLU B CD  1 
ATOM   1911 O OE1 . GLU B 1 17  ? 14.661  -7.655  38.698  1.00 32.80 ? 17  GLU B OE1 1 
ATOM   1912 O OE2 . GLU B 1 17  ? 16.339  -7.995  40.080  1.00 31.78 ? 17  GLU B OE2 1 
ATOM   1913 N N   . LEU B 1 18  ? 10.847  -5.384  38.570  1.00 17.46 ? 18  LEU B N   1 
ATOM   1914 C CA  . LEU B 1 18  ? 9.491   -5.093  38.137  1.00 20.13 ? 18  LEU B CA  1 
ATOM   1915 C C   . LEU B 1 18  ? 9.076   -6.152  37.130  1.00 17.73 ? 18  LEU B C   1 
ATOM   1916 O O   . LEU B 1 18  ? 9.795   -6.395  36.157  1.00 18.36 ? 18  LEU B O   1 
ATOM   1917 C CB  . LEU B 1 18  ? 9.382   -3.699  37.501  1.00 19.91 ? 18  LEU B CB  1 
ATOM   1918 C CG  . LEU B 1 18  ? 7.970   -3.337  37.021  1.00 18.93 ? 18  LEU B CG  1 
ATOM   1919 C CD1 . LEU B 1 18  ? 7.624   -1.884  37.368  1.00 21.32 ? 18  LEU B CD1 1 
ATOM   1920 C CD2 . LEU B 1 18  ? 7.782   -3.618  35.549  1.00 20.25 ? 18  LEU B CD2 1 
ATOM   1921 N N   . ASP B 1 19  ? 7.913   -6.757  37.360  1.00 19.96 ? 19  ASP B N   1 
ATOM   1922 C CA  . ASP B 1 19  ? 7.247   -7.646  36.410  1.00 22.39 ? 19  ASP B CA  1 
ATOM   1923 C C   . ASP B 1 19  ? 6.021   -6.928  35.860  1.00 21.95 ? 19  ASP B C   1 
ATOM   1924 O O   . ASP B 1 19  ? 5.093   -6.628  36.622  1.00 19.62 ? 19  ASP B O   1 
ATOM   1925 C CB  . ASP B 1 19  ? 6.835   -8.941  37.118  1.00 27.05 ? 19  ASP B CB  1 
ATOM   1926 C CG  . ASP B 1 19  ? 6.325   -10.002 36.174  1.00 32.65 ? 19  ASP B CG  1 
ATOM   1927 O OD1 . ASP B 1 19  ? 5.220   -10.516 36.436  1.00 34.56 ? 19  ASP B OD1 1 
ATOM   1928 O OD2 . ASP B 1 19  ? 7.032   -10.349 35.198  1.00 37.75 ? 19  ASP B OD2 1 
ATOM   1929 N N   . GLY B 1 20  ? 5.984   -6.709  34.546  1.00 18.31 ? 20  GLY B N   1 
ATOM   1930 C CA  . GLY B 1 20  ? 4.995   -5.837  33.940  1.00 18.18 ? 20  GLY B CA  1 
ATOM   1931 C C   . GLY B 1 20  ? 4.205   -6.486  32.821  1.00 22.55 ? 20  GLY B C   1 
ATOM   1932 O O   . GLY B 1 20  ? 4.699   -7.364  32.113  1.00 20.23 ? 20  GLY B O   1 
ATOM   1933 N N   . ASP B 1 21  ? 2.961   -6.034  32.670  1.00 20.65 ? 21  ASP B N   1 
ATOM   1934 C CA  . ASP B 1 21  ? 2.076   -6.457  31.589  1.00 21.19 ? 21  ASP B CA  1 
ATOM   1935 C C   . ASP B 1 21  ? 1.225   -5.246  31.260  1.00 22.45 ? 21  ASP B C   1 
ATOM   1936 O O   . ASP B 1 21  ? 0.430   -4.823  32.095  1.00 22.95 ? 21  ASP B O   1 
ATOM   1937 C CB  . ASP B 1 21  ? 1.202   -7.640  32.016  1.00 25.75 ? 21  ASP B CB  1 
ATOM   1938 C CG  . ASP B 1 21  ? 0.306   -8.156  30.887  1.00 29.48 ? 21  ASP B CG  1 
ATOM   1939 O OD1 . ASP B 1 21  ? -0.134  -7.366  30.029  1.00 30.47 ? 21  ASP B OD1 1 
ATOM   1940 O OD2 . ASP B 1 21  ? -0.024  -9.346  30.899  1.00 35.91 ? 21  ASP B OD2 1 
ATOM   1941 N N   . VAL B 1 22  ? 1.379   -4.693  30.062  1.00 20.67 ? 22  VAL B N   1 
ATOM   1942 C CA  . VAL B 1 22  ? 0.627   -3.525  29.631  1.00 21.79 ? 22  VAL B CA  1 
ATOM   1943 C C   . VAL B 1 22  ? -0.075  -3.893  28.335  1.00 21.57 ? 22  VAL B C   1 
ATOM   1944 O O   . VAL B 1 22  ? 0.590   -4.149  27.326  1.00 24.48 ? 22  VAL B O   1 
ATOM   1945 C CB  . VAL B 1 22  ? 1.539   -2.299  29.449  1.00 19.26 ? 22  VAL B CB  1 
ATOM   1946 C CG1 . VAL B 1 22  ? 0.785   -1.158  28.843  1.00 17.29 ? 22  VAL B CG1 1 
ATOM   1947 C CG2 . VAL B 1 22  ? 2.082   -1.868  30.823  1.00 18.29 ? 22  VAL B CG2 1 
ATOM   1948 N N   . ASN B 1 23  ? -1.412  -3.936  28.373  1.00 20.41 ? 23  ASN B N   1 
ATOM   1949 C CA  . ASN B 1 23  ? -2.235  -4.351  27.222  1.00 24.18 ? 23  ASN B CA  1 
ATOM   1950 C C   . ASN B 1 23  ? -1.815  -5.711  26.675  1.00 26.07 ? 23  ASN B C   1 
ATOM   1951 O O   . ASN B 1 23  ? -1.921  -5.966  25.473  1.00 27.06 ? 23  ASN B O   1 
ATOM   1952 C CB  . ASN B 1 23  ? -2.184  -3.338  26.082  1.00 19.78 ? 23  ASN B CB  1 
ATOM   1953 C CG  . ASN B 1 23  ? -3.167  -2.201  26.252  1.00 22.61 ? 23  ASN B CG  1 
ATOM   1954 O OD1 . ASN B 1 23  ? -3.603  -1.915  27.361  1.00 22.49 ? 23  ASN B OD1 1 
ATOM   1955 N ND2 . ASN B 1 23  ? -3.577  -1.589  25.128  1.00 21.42 ? 23  ASN B ND2 1 
ATOM   1956 N N   . GLY B 1 24  ? -1.295  -6.587  27.524  1.00 25.95 ? 24  GLY B N   1 
ATOM   1957 C CA  . GLY B 1 24  ? -0.821  -7.874  27.065  1.00 27.12 ? 24  GLY B CA  1 
ATOM   1958 C C   . GLY B 1 24  ? 0.643   -7.920  26.693  1.00 28.47 ? 24  GLY B C   1 
ATOM   1959 O O   . GLY B 1 24  ? 1.173   -9.014  26.470  1.00 30.21 ? 24  GLY B O   1 
ATOM   1960 N N   . HIS B 1 25  ? 1.312   -6.775  26.604  1.00 25.84 ? 25  HIS B N   1 
ATOM   1961 C CA  . HIS B 1 25  ? 2.738   -6.737  26.304  1.00 26.39 ? 25  HIS B CA  1 
ATOM   1962 C C   . HIS B 1 25  ? 3.486   -6.978  27.607  1.00 27.31 ? 25  HIS B C   1 
ATOM   1963 O O   . HIS B 1 25  ? 3.463   -6.127  28.501  1.00 24.50 ? 25  HIS B O   1 
ATOM   1964 C CB  . HIS B 1 25  ? 3.128   -5.388  25.711  1.00 26.62 ? 25  HIS B CB  1 
ATOM   1965 C CG  . HIS B 1 25  ? 2.356   -5.017  24.486  1.00 30.15 ? 25  HIS B CG  1 
ATOM   1966 N ND1 . HIS B 1 25  ? 2.591   -5.592  23.256  1.00 32.65 ? 25  HIS B ND1 1 
ATOM   1967 C CD2 . HIS B 1 25  ? 1.391   -4.086  24.289  1.00 32.20 ? 25  HIS B CD2 1 
ATOM   1968 C CE1 . HIS B 1 25  ? 1.777   -5.060  22.360  1.00 37.83 ? 25  HIS B CE1 1 
ATOM   1969 N NE2 . HIS B 1 25  ? 1.044   -4.136  22.958  1.00 35.64 ? 25  HIS B NE2 1 
ATOM   1970 N N   . LYS B 1 26  ? 4.148   -8.124  27.729  1.00 24.34 ? 26  LYS B N   1 
ATOM   1971 C CA  . LYS B 1 26  ? 4.854   -8.456  28.961  1.00 24.61 ? 26  LYS B CA  1 
ATOM   1972 C C   . LYS B 1 26  ? 6.304   -7.995  28.900  1.00 22.57 ? 26  LYS B C   1 
ATOM   1973 O O   . LYS B 1 26  ? 6.934   -7.992  27.838  1.00 21.88 ? 26  LYS B O   1 
ATOM   1974 C CB  . LYS B 1 26  ? 4.789   -9.957  29.234  1.00 23.62 ? 26  LYS B CB  1 
ATOM   1975 C CG  . LYS B 1 26  ? 3.360   -10.436 29.137  1.00 28.34 ? 26  LYS B CG  1 
ATOM   1976 C CD  . LYS B 1 26  ? 2.999   -11.525 30.095  1.00 30.12 ? 26  LYS B CD  1 
ATOM   1977 C CE  . LYS B 1 26  ? 1.539   -11.904 29.840  1.00 30.44 ? 26  LYS B CE  1 
ATOM   1978 N NZ  . LYS B 1 26  ? 0.956   -12.746 30.909  1.00 40.81 ? 26  LYS B NZ  1 
ATOM   1979 N N   . PHE B 1 27  ? 6.830   -7.601  30.059  1.00 19.54 ? 27  PHE B N   1 
ATOM   1980 C CA  . PHE B 1 27  ? 8.178   -7.059  30.132  1.00 19.04 ? 27  PHE B CA  1 
ATOM   1981 C C   . PHE B 1 27  ? 8.668   -7.125  31.569  1.00 18.06 ? 27  PHE B C   1 
ATOM   1982 O O   . PHE B 1 27  ? 7.879   -7.204  32.510  1.00 16.92 ? 27  PHE B O   1 
ATOM   1983 C CB  . PHE B 1 27  ? 8.239   -5.625  29.593  1.00 20.34 ? 27  PHE B CB  1 
ATOM   1984 C CG  . PHE B 1 27  ? 7.561   -4.611  30.467  1.00 20.39 ? 27  PHE B CG  1 
ATOM   1985 C CD1 . PHE B 1 27  ? 6.188   -4.401  30.362  1.00 21.84 ? 27  PHE B CD1 1 
ATOM   1986 C CD2 . PHE B 1 27  ? 8.280   -3.862  31.385  1.00 19.24 ? 27  PHE B CD2 1 
ATOM   1987 C CE1 . PHE B 1 27  ? 5.553   -3.451  31.170  1.00 22.26 ? 27  PHE B CE1 1 
ATOM   1988 C CE2 . PHE B 1 27  ? 7.650   -2.922  32.184  1.00 17.18 ? 27  PHE B CE2 1 
ATOM   1989 C CZ  . PHE B 1 27  ? 6.285   -2.718  32.073  1.00 20.65 ? 27  PHE B CZ  1 
ATOM   1990 N N   . SER B 1 28  ? 9.983   -7.104  31.719  1.00 19.80 ? 28  SER B N   1 
ATOM   1991 C CA  . SER B 1 28  ? 10.613  -7.182  33.032  1.00 21.90 ? 28  SER B CA  1 
ATOM   1992 C C   . SER B 1 28  ? 11.691  -6.110  33.108  1.00 19.35 ? 28  SER B C   1 
ATOM   1993 O O   . SER B 1 28  ? 12.364  -5.832  32.114  1.00 19.25 ? 28  SER B O   1 
ATOM   1994 C CB  . SER B 1 28  ? 11.221  -8.575  33.271  1.00 23.01 ? 28  SER B CB  1 
ATOM   1995 O OG  . SER B 1 28  ? 10.209  -9.495  33.664  1.00 28.76 ? 28  SER B OG  1 
ATOM   1996 N N   . VAL B 1 29  ? 11.839  -5.493  34.278  1.00 18.75 ? 29  VAL B N   1 
ATOM   1997 C CA  . VAL B 1 29  ? 12.840  -4.453  34.505  1.00 17.96 ? 29  VAL B CA  1 
ATOM   1998 C C   . VAL B 1 29  ? 13.621  -4.820  35.759  1.00 19.43 ? 29  VAL B C   1 
ATOM   1999 O O   . VAL B 1 29  ? 13.021  -5.180  36.777  1.00 17.56 ? 29  VAL B O   1 
ATOM   2000 C CB  . VAL B 1 29  ? 12.202  -3.058  34.655  1.00 19.71 ? 29  VAL B CB  1 
ATOM   2001 C CG1 . VAL B 1 29  ? 13.249  -2.043  35.138  1.00 20.44 ? 29  VAL B CG1 1 
ATOM   2002 C CG2 . VAL B 1 29  ? 11.654  -2.598  33.315  1.00 19.27 ? 29  VAL B CG2 1 
ATOM   2003 N N   . SER B 1 30  ? 14.953  -4.762  35.674  1.00 20.31 ? 30  SER B N   1 
ATOM   2004 C CA  . SER B 1 30  ? 15.839  -4.898  36.824  1.00 20.43 ? 30  SER B CA  1 
ATOM   2005 C C   . SER B 1 30  ? 16.562  -3.584  37.076  1.00 19.92 ? 30  SER B C   1 
ATOM   2006 O O   . SER B 1 30  ? 17.000  -2.915  36.134  1.00 23.26 ? 30  SER B O   1 
ATOM   2007 C CB  . SER B 1 30  ? 16.885  -6.002  36.589  1.00 22.31 ? 30  SER B CB  1 
ATOM   2008 O OG  . SER B 1 30  ? 16.265  -7.210  36.199  1.00 35.53 ? 30  SER B OG  1 
ATOM   2009 N N   . GLY B 1 31  ? 16.740  -3.234  38.339  1.00 17.12 ? 31  GLY B N   1 
ATOM   2010 C CA  . GLY B 1 31  ? 17.463  -2.025  38.675  1.00 18.91 ? 31  GLY B CA  1 
ATOM   2011 C C   . GLY B 1 31  ? 18.439  -2.271  39.808  1.00 20.61 ? 31  GLY B C   1 
ATOM   2012 O O   . GLY B 1 31  ? 18.215  -3.103  40.682  1.00 19.10 ? 31  GLY B O   1 
ATOM   2013 N N   . GLU B 1 32  ? 19.525  -1.511  39.795  1.00 20.56 ? 32  GLU B N   1 
ATOM   2014 C CA  . GLU B 1 32  ? 20.473  -1.580  40.894  1.00 24.33 ? 32  GLU B CA  1 
ATOM   2015 C C   . GLU B 1 32  ? 21.139  -0.223  41.049  1.00 19.31 ? 32  GLU B C   1 
ATOM   2016 O O   . GLU B 1 32  ? 21.218  0.564   40.104  1.00 18.50 ? 32  GLU B O   1 
ATOM   2017 C CB  . GLU B 1 32  ? 21.510  -2.697  40.677  1.00 26.83 ? 32  GLU B CB  1 
ATOM   2018 C CG  . GLU B 1 32  ? 22.224  -2.655  39.338  1.00 34.32 ? 32  GLU B CG  1 
ATOM   2019 C CD  . GLU B 1 32  ? 23.320  -3.715  39.208  1.00 42.47 ? 32  GLU B CD  1 
ATOM   2020 O OE1 . GLU B 1 32  ? 23.085  -4.862  39.666  1.00 43.38 ? 32  GLU B OE1 1 
ATOM   2021 O OE2 . GLU B 1 32  ? 24.391  -3.406  38.623  1.00 36.43 ? 32  GLU B OE2 1 
ATOM   2022 N N   . GLY B 1 33  ? 21.601  0.047   42.263  1.00 18.41 ? 33  GLY B N   1 
ATOM   2023 C CA  . GLY B 1 33  ? 22.205  1.328   42.579  1.00 21.63 ? 33  GLY B CA  1 
ATOM   2024 C C   . GLY B 1 33  ? 22.365  1.448   44.081  1.00 22.70 ? 33  GLY B C   1 
ATOM   2025 O O   . GLY B 1 33  ? 22.514  0.438   44.787  1.00 21.05 ? 33  GLY B O   1 
ATOM   2026 N N   . GLU B 1 34  ? 22.294  2.683   44.570  1.00 19.94 ? 34  GLU B N   1 
ATOM   2027 C CA  . GLU B 1 34  ? 22.404  2.892   46.009  1.00 21.97 ? 34  GLU B CA  1 
ATOM   2028 C C   . GLU B 1 34  ? 21.655  4.141   46.428  1.00 25.83 ? 34  GLU B C   1 
ATOM   2029 O O   . GLU B 1 34  ? 21.361  5.023   45.616  1.00 21.83 ? 34  GLU B O   1 
ATOM   2030 C CB  . GLU B 1 34  ? 23.860  2.995   46.478  1.00 27.61 ? 34  GLU B CB  1 
ATOM   2031 C CG  . GLU B 1 34  ? 24.832  3.522   45.459  1.00 32.11 ? 34  GLU B CG  1 
ATOM   2032 C CD  . GLU B 1 34  ? 26.278  3.416   45.941  1.00 39.13 ? 34  GLU B CD  1 
ATOM   2033 O OE1 . GLU B 1 34  ? 26.964  4.459   46.020  1.00 43.25 ? 34  GLU B OE1 1 
ATOM   2034 O OE2 . GLU B 1 34  ? 26.723  2.288   46.254  1.00 43.11 ? 34  GLU B OE2 1 
ATOM   2035 N N   . GLY B 1 35  ? 21.343  4.188   47.714  1.00 21.10 ? 35  GLY B N   1 
ATOM   2036 C CA  . GLY B 1 35  ? 20.687  5.339   48.300  1.00 22.86 ? 35  GLY B CA  1 
ATOM   2037 C C   . GLY B 1 35  ? 21.404  5.761   49.565  1.00 25.73 ? 35  GLY B C   1 
ATOM   2038 O O   . GLY B 1 35  ? 21.944  4.925   50.299  1.00 23.12 ? 35  GLY B O   1 
ATOM   2039 N N   . ASP B 1 36  ? 21.429  7.072   49.799  1.00 20.11 ? 36  ASP B N   1 
ATOM   2040 C CA  . ASP B 1 36  ? 22.015  7.655   51.011  1.00 26.00 ? 36  ASP B CA  1 
ATOM   2041 C C   . ASP B 1 36  ? 21.032  8.671   51.580  1.00 25.62 ? 36  ASP B C   1 
ATOM   2042 O O   . ASP B 1 36  ? 21.027  9.838   51.179  1.00 26.88 ? 36  ASP B O   1 
ATOM   2043 C CB  . ASP B 1 36  ? 23.373  8.280   50.720  1.00 28.46 ? 36  ASP B CB  1 
ATOM   2044 C CG  . ASP B 1 36  ? 24.172  8.544   51.982  1.00 36.83 ? 36  ASP B CG  1 
ATOM   2045 O OD1 . ASP B 1 36  ? 23.593  8.480   53.090  1.00 34.92 ? 36  ASP B OD1 1 
ATOM   2046 O OD2 . ASP B 1 36  ? 25.386  8.789   51.865  1.00 41.93 ? 36  ASP B OD2 1 
ATOM   2047 N N   . ALA B 1 37  ? 20.199  8.221   52.519  1.00 23.31 ? 37  ALA B N   1 
ATOM   2048 C CA  . ALA B 1 37  ? 19.152  9.085   53.051  1.00 24.53 ? 37  ALA B CA  1 
ATOM   2049 C C   . ALA B 1 37  ? 19.717  10.288  53.802  1.00 28.83 ? 37  ALA B C   1 
ATOM   2050 O O   . ALA B 1 37  ? 19.035  11.314  53.910  1.00 25.22 ? 37  ALA B O   1 
ATOM   2051 C CB  . ALA B 1 37  ? 18.223  8.274   53.954  1.00 23.94 ? 37  ALA B CB  1 
ATOM   2052 N N   . THR B 1 38  ? 20.952  10.197  54.304  1.00 28.22 ? 38  THR B N   1 
ATOM   2053 C CA  . THR B 1 38  ? 21.584  11.369  54.907  1.00 33.63 ? 38  THR B CA  1 
ATOM   2054 C C   . THR B 1 38  ? 21.560  12.563  53.968  1.00 33.28 ? 38  THR B C   1 
ATOM   2055 O O   . THR B 1 38  ? 21.478  13.710  54.417  1.00 32.43 ? 38  THR B O   1 
ATOM   2056 C CB  . THR B 1 38  ? 23.028  11.057  55.302  1.00 34.11 ? 38  THR B CB  1 
ATOM   2057 O OG1 . THR B 1 38  ? 23.088  9.772   55.937  1.00 38.35 ? 38  THR B OG1 1 
ATOM   2058 C CG2 . THR B 1 38  ? 23.567  12.139  56.239  1.00 39.98 ? 38  THR B CG2 1 
ATOM   2059 N N   . TYR B 1 39  ? 21.625  12.311  52.666  1.00 31.65 ? 39  TYR B N   1 
ATOM   2060 C CA  . TYR B 1 39  ? 21.600  13.339  51.642  1.00 27.27 ? 39  TYR B CA  1 
ATOM   2061 C C   . TYR B 1 39  ? 20.333  13.301  50.797  1.00 30.80 ? 39  TYR B C   1 
ATOM   2062 O O   . TYR B 1 39  ? 20.164  14.155  49.920  1.00 29.25 ? 39  TYR B O   1 
ATOM   2063 C CB  . TYR B 1 39  ? 22.830  13.202  50.729  1.00 31.97 ? 39  TYR B CB  1 
ATOM   2064 C CG  . TYR B 1 39  ? 24.157  12.992  51.453  1.00 37.72 ? 39  TYR B CG  1 
ATOM   2065 C CD1 . TYR B 1 39  ? 25.036  14.046  51.652  1.00 40.06 ? 39  TYR B CD1 1 
ATOM   2066 C CD2 . TYR B 1 39  ? 24.512  11.751  51.961  1.00 39.45 ? 39  TYR B CD2 1 
ATOM   2067 C CE1 . TYR B 1 39  ? 26.246  13.863  52.307  1.00 38.51 ? 39  TYR B CE1 1 
ATOM   2068 C CE2 . TYR B 1 39  ? 25.712  11.563  52.632  1.00 41.77 ? 39  TYR B CE2 1 
ATOM   2069 C CZ  . TYR B 1 39  ? 26.573  12.618  52.800  1.00 43.53 ? 39  TYR B CZ  1 
ATOM   2070 O OH  . TYR B 1 39  ? 27.762  12.424  53.465  1.00 49.32 ? 39  TYR B OH  1 
ATOM   2071 N N   . GLY B 1 40  ? 19.439  12.342  51.035  1.00 25.72 ? 40  GLY B N   1 
ATOM   2072 C CA  . GLY B 1 40  ? 18.283  12.183  50.168  1.00 24.68 ? 40  GLY B CA  1 
ATOM   2073 C C   . GLY B 1 40  ? 18.613  11.720  48.766  1.00 26.75 ? 40  GLY B C   1 
ATOM   2074 O O   . GLY B 1 40  ? 17.774  11.854  47.868  1.00 24.46 ? 40  GLY B O   1 
ATOM   2075 N N   . LYS B 1 41  ? 19.796  11.135  48.553  1.00 20.42 ? 41  LYS B N   1 
ATOM   2076 C CA  . LYS B 1 41  ? 20.312  10.857  47.215  1.00 23.00 ? 41  LYS B CA  1 
ATOM   2077 C C   . LYS B 1 41  ? 20.108  9.400   46.796  1.00 21.81 ? 41  LYS B C   1 
ATOM   2078 O O   . LYS B 1 41  ? 20.406  8.473   47.558  1.00 20.32 ? 41  LYS B O   1 
ATOM   2079 C CB  . LYS B 1 41  ? 21.798  11.206  47.155  1.00 21.44 ? 41  LYS B CB  1 
ATOM   2080 C CG  . LYS B 1 41  ? 22.429  11.174  45.776  1.00 27.20 ? 41  LYS B CG  1 
ATOM   2081 C CD  . LYS B 1 41  ? 23.913  11.571  45.902  1.00 27.62 ? 41  LYS B CD  1 
ATOM   2082 C CE  . LYS B 1 41  ? 24.664  11.495  44.591  1.00 31.53 ? 41  LYS B CE  1 
ATOM   2083 N NZ  . LYS B 1 41  ? 25.784  12.488  44.555  1.00 35.39 ? 41  LYS B NZ  1 
ATOM   2084 N N   . LEU B 1 42  ? 19.665  9.218   45.544  1.00 18.33 ? 42  LEU B N   1 
ATOM   2085 C CA  . LEU B 1 42  ? 19.439  7.927   44.896  1.00 22.80 ? 42  LEU B CA  1 
ATOM   2086 C C   . LEU B 1 42  ? 20.162  7.930   43.556  1.00 21.16 ? 42  LEU B C   1 
ATOM   2087 O O   . LEU B 1 42  ? 19.974  8.855   42.765  1.00 20.86 ? 42  LEU B O   1 
ATOM   2088 C CB  . LEU B 1 42  ? 17.933  7.696   44.642  1.00 20.11 ? 42  LEU B CB  1 
ATOM   2089 C CG  . LEU B 1 42  ? 17.001  7.536   45.827  1.00 26.03 ? 42  LEU B CG  1 
ATOM   2090 C CD1 . LEU B 1 42  ? 15.557  7.645   45.392  1.00 25.27 ? 42  LEU B CD1 1 
ATOM   2091 C CD2 . LEU B 1 42  ? 17.230  6.180   46.442  1.00 25.48 ? 42  LEU B CD2 1 
ATOM   2092 N N   . THR B 1 43  ? 20.964  6.898   43.282  1.00 21.35 ? 43  THR B N   1 
ATOM   2093 C CA  . THR B 1 43  ? 21.487  6.670   41.934  1.00 24.32 ? 43  THR B CA  1 
ATOM   2094 C C   . THR B 1 43  ? 21.177  5.240   41.522  1.00 24.23 ? 43  THR B C   1 
ATOM   2095 O O   . THR B 1 43  ? 21.485  4.298   42.256  1.00 24.39 ? 43  THR B O   1 
ATOM   2096 C CB  . THR B 1 43  ? 23.001  6.953   41.841  1.00 25.80 ? 43  THR B CB  1 
ATOM   2097 O OG1 . THR B 1 43  ? 23.727  5.998   42.627  1.00 32.04 ? 43  THR B OG1 1 
ATOM   2098 C CG2 . THR B 1 43  ? 23.318  8.324   42.343  1.00 21.89 ? 43  THR B CG2 1 
ATOM   2099 N N   . LEU B 1 44  ? 20.559  5.077   40.359  1.00 19.92 ? 44  LEU B N   1 
ATOM   2100 C CA  . LEU B 1 44  ? 20.049  3.780   39.952  1.00 20.92 ? 44  LEU B CA  1 
ATOM   2101 C C   . LEU B 1 44  ? 20.195  3.617   38.453  1.00 20.12 ? 44  LEU B C   1 
ATOM   2102 O O   . LEU B 1 44  ? 20.066  4.588   37.703  1.00 23.23 ? 44  LEU B O   1 
ATOM   2103 C CB  . LEU B 1 44  ? 18.579  3.647   40.342  1.00 21.08 ? 44  LEU B CB  1 
ATOM   2104 C CG  . LEU B 1 44  ? 18.408  3.366   41.843  1.00 22.36 ? 44  LEU B CG  1 
ATOM   2105 C CD1 . LEU B 1 44  ? 17.106  3.985   42.354  1.00 26.55 ? 44  LEU B CD1 1 
ATOM   2106 C CD2 . LEU B 1 44  ? 18.450  1.871   42.106  1.00 24.15 ? 44  LEU B CD2 1 
ATOM   2107 N N   . LYS B 1 45  ? 20.472  2.394   38.021  1.00 20.73 ? 45  LYS B N   1 
ATOM   2108 C CA  . LYS B 1 45  ? 20.435  2.024   36.613  1.00 20.89 ? 45  LYS B CA  1 
ATOM   2109 C C   . LYS B 1 45  ? 19.396  0.928   36.429  1.00 20.68 ? 45  LYS B C   1 
ATOM   2110 O O   . LYS B 1 45  ? 19.434  -0.088  37.127  1.00 17.80 ? 45  LYS B O   1 
ATOM   2111 C CB  . LYS B 1 45  ? 21.791  1.514   36.128  1.00 22.87 ? 45  LYS B CB  1 
ATOM   2112 C CG  . LYS B 1 45  ? 21.821  1.164   34.645  1.00 22.07 ? 45  LYS B CG  1 
ATOM   2113 C CD  . LYS B 1 45  ? 23.237  0.788   34.243  1.00 28.31 ? 45  LYS B CD  1 
ATOM   2114 C CE  . LYS B 1 45  ? 23.294  0.216   32.844  1.00 27.67 ? 45  LYS B CE  1 
ATOM   2115 N NZ  . LYS B 1 45  ? 24.609  0.478   32.156  1.00 30.97 ? 45  LYS B NZ  1 
ATOM   2116 N N   . PHE B 1 46  ? 18.492  1.119   35.473  1.00 17.01 ? 46  PHE B N   1 
ATOM   2117 C CA  . PHE B 1 46  ? 17.442  0.156   35.181  1.00 18.78 ? 46  PHE B CA  1 
ATOM   2118 C C   . PHE B 1 46  ? 17.661  -0.420  33.794  1.00 19.26 ? 46  PHE B C   1 
ATOM   2119 O O   . PHE B 1 46  ? 17.967  0.320   32.857  1.00 19.83 ? 46  PHE B O   1 
ATOM   2120 C CB  . PHE B 1 46  ? 16.052  0.811   35.245  1.00 16.18 ? 46  PHE B CB  1 
ATOM   2121 C CG  . PHE B 1 46  ? 15.730  1.399   36.593  1.00 16.34 ? 46  PHE B CG  1 
ATOM   2122 C CD1 . PHE B 1 46  ? 15.265  0.601   37.624  1.00 15.96 ? 46  PHE B CD1 1 
ATOM   2123 C CD2 . PHE B 1 46  ? 15.956  2.742   36.843  1.00 15.63 ? 46  PHE B CD2 1 
ATOM   2124 C CE1 . PHE B 1 46  ? 14.989  1.137   38.880  1.00 15.58 ? 46  PHE B CE1 1 
ATOM   2125 C CE2 . PHE B 1 46  ? 15.691  3.288   38.111  1.00 14.81 ? 46  PHE B CE2 1 
ATOM   2126 C CZ  . PHE B 1 46  ? 15.205  2.482   39.116  1.00 15.74 ? 46  PHE B CZ  1 
ATOM   2127 N N   . ILE B 1 47  ? 17.410  -1.724  33.661  1.00 17.95 ? 47  ILE B N   1 
ATOM   2128 C CA  . ILE B 1 47  ? 17.561  -2.470  32.414  1.00 20.16 ? 47  ILE B CA  1 
ATOM   2129 C C   . ILE B 1 47  ? 16.218  -3.099  32.096  1.00 18.75 ? 47  ILE B C   1 
ATOM   2130 O O   . ILE B 1 47  ? 15.613  -3.717  32.972  1.00 19.53 ? 47  ILE B O   1 
ATOM   2131 C CB  . ILE B 1 47  ? 18.612  -3.590  32.554  1.00 19.22 ? 47  ILE B CB  1 
ATOM   2132 C CG1 . ILE B 1 47  ? 20.027  -3.046  32.748  1.00 24.27 ? 47  ILE B CG1 1 
ATOM   2133 C CG2 . ILE B 1 47  ? 18.608  -4.478  31.322  1.00 21.50 ? 47  ILE B CG2 1 
ATOM   2134 C CD1 . ILE B 1 47  ? 20.450  -2.042  31.760  1.00 23.78 ? 47  ILE B CD1 1 
ATOM   2135 N N   . CYS B 1 48  ? 15.765  -2.997  30.842  1.00 16.32 ? 48  CYS B N   1 
ATOM   2136 C CA  . CYS B 1 48  ? 14.682  -3.872  30.404  1.00 16.61 ? 48  CYS B CA  1 
ATOM   2137 C C   . CYS B 1 48  ? 15.310  -5.204  30.022  1.00 21.88 ? 48  CYS B C   1 
ATOM   2138 O O   . CYS B 1 48  ? 16.028  -5.300  29.019  1.00 22.86 ? 48  CYS B O   1 
ATOM   2139 C CB  . CYS B 1 48  ? 13.881  -3.279  29.240  1.00 18.52 ? 48  CYS B CB  1 
ATOM   2140 S SG  . CYS B 1 48  ? 12.488  -4.398  28.832  1.00 21.50 ? 48  CYS B SG  1 
ATOM   2141 N N   . THR B 1 49  ? 15.099  -6.218  30.848  1.00 21.52 ? 49  THR B N   1 
ATOM   2142 C CA  . THR B 1 49  ? 15.781  -7.480  30.610  1.00 23.66 ? 49  THR B CA  1 
ATOM   2143 C C   . THR B 1 49  ? 15.077  -8.346  29.579  1.00 26.90 ? 49  THR B C   1 
ATOM   2144 O O   . THR B 1 49  ? 15.646  -9.353  29.145  1.00 25.95 ? 49  THR B O   1 
ATOM   2145 C CB  . THR B 1 49  ? 15.926  -8.242  31.916  1.00 25.11 ? 49  THR B CB  1 
ATOM   2146 O OG1 . THR B 1 49  ? 14.626  -8.557  32.427  1.00 25.35 ? 49  THR B OG1 1 
ATOM   2147 C CG2 . THR B 1 49  ? 16.717  -7.416  32.916  1.00 21.46 ? 49  THR B CG2 1 
ATOM   2148 N N   . THR B 1 50  ? 13.872  -7.977  29.162  1.00 21.60 ? 50  THR B N   1 
ATOM   2149 C CA  . THR B 1 50  ? 13.135  -8.774  28.203  1.00 22.69 ? 50  THR B CA  1 
ATOM   2150 C C   . THR B 1 50  ? 13.274  -8.266  26.773  1.00 26.39 ? 50  THR B C   1 
ATOM   2151 O O   . THR B 1 50  ? 12.685  -8.853  25.863  1.00 28.03 ? 50  THR B O   1 
ATOM   2152 C CB  . THR B 1 50  ? 11.664  -8.828  28.608  1.00 22.80 ? 50  THR B CB  1 
ATOM   2153 O OG1 . THR B 1 50  ? 11.229  -7.508  28.938  1.00 22.16 ? 50  THR B OG1 1 
ATOM   2154 C CG2 . THR B 1 50  ? 11.470  -9.755  29.815  1.00 25.92 ? 50  THR B CG2 1 
ATOM   2155 N N   . GLY B 1 51  ? 14.042  -7.204  26.543  1.00 21.94 ? 51  GLY B N   1 
ATOM   2156 C CA  . GLY B 1 51  ? 14.115  -6.629  25.211  1.00 24.07 ? 51  GLY B CA  1 
ATOM   2157 C C   . GLY B 1 51  ? 13.820  -5.140  25.202  1.00 21.45 ? 51  GLY B C   1 
ATOM   2158 O O   . GLY B 1 51  ? 14.365  -4.387  26.019  1.00 25.66 ? 51  GLY B O   1 
ATOM   2159 N N   . LYS B 1 52  ? 12.969  -4.700  24.283  1.00 27.13 ? 52  LYS B N   1 
ATOM   2160 C CA  . LYS B 1 52  ? 12.577  -3.298  24.235  1.00 21.52 ? 52  LYS B CA  1 
ATOM   2161 C C   . LYS B 1 52  ? 11.435  -3.042  25.212  1.00 22.45 ? 52  LYS B C   1 
ATOM   2162 O O   . LYS B 1 52  ? 10.489  -3.836  25.312  1.00 19.05 ? 52  LYS B O   1 
ATOM   2163 C CB  . LYS B 1 52  ? 12.164  -2.899  22.817  1.00 25.77 ? 52  LYS B CB  1 
ATOM   2164 C CG  . LYS B 1 52  ? 12.153  -1.399  22.636  1.00 29.73 ? 52  LYS B CG  1 
ATOM   2165 C CD  . LYS B 1 52  ? 11.324  -0.946  21.450  1.00 33.04 ? 52  LYS B CD  1 
ATOM   2166 C CE  . LYS B 1 52  ? 11.712  0.471   21.082  1.00 38.54 ? 52  LYS B CE  1 
ATOM   2167 N NZ  . LYS B 1 52  ? 11.333  1.421   22.160  1.00 36.15 ? 52  LYS B NZ  1 
ATOM   2168 N N   . LEU B 1 53  ? 11.550  -1.950  25.963  1.00 19.27 ? 53  LEU B N   1 
ATOM   2169 C CA  . LEU B 1 53  ? 10.510  -1.568  26.916  1.00 19.61 ? 53  LEU B CA  1 
ATOM   2170 C C   . LEU B 1 53  ? 9.287   -1.104  26.142  1.00 19.87 ? 53  LEU B C   1 
ATOM   2171 O O   . LEU B 1 53  ? 9.419   -0.243  25.279  1.00 19.48 ? 53  LEU B O   1 
ATOM   2172 C CB  . LEU B 1 53  ? 11.008  -0.423  27.814  1.00 16.99 ? 53  LEU B CB  1 
ATOM   2173 C CG  . LEU B 1 53  ? 10.162  -0.110  29.056  1.00 16.81 ? 53  LEU B CG  1 
ATOM   2174 C CD1 . LEU B 1 53  ? 10.219  -1.309  30.024  1.00 18.25 ? 53  LEU B CD1 1 
ATOM   2175 C CD2 . LEU B 1 53  ? 10.584  1.163   29.759  1.00 16.02 ? 53  LEU B CD2 1 
ATOM   2176 N N   . PRO B 1 54  ? 8.093   -1.650  26.398  1.00 18.26 ? 54  PRO B N   1 
ATOM   2177 C CA  . PRO B 1 54  ? 6.934   -1.300  25.559  1.00 18.26 ? 54  PRO B CA  1 
ATOM   2178 C C   . PRO B 1 54  ? 6.230   -0.010  25.949  1.00 20.03 ? 54  PRO B C   1 
ATOM   2179 O O   . PRO B 1 54  ? 5.280   0.382   25.251  1.00 19.39 ? 54  PRO B O   1 
ATOM   2180 C CB  . PRO B 1 54  ? 6.001   -2.509  25.730  1.00 19.56 ? 54  PRO B CB  1 
ATOM   2181 C CG  . PRO B 1 54  ? 6.404   -3.140  27.032  1.00 19.29 ? 54  PRO B CG  1 
ATOM   2182 C CD  . PRO B 1 54  ? 7.835   -2.803  27.277  1.00 17.97 ? 54  PRO B CD  1 
ATOM   2183 N N   . VAL B 1 55  ? 6.668   0.644   27.027  1.00 17.68 ? 55  VAL B N   1 
ATOM   2184 C CA  . VAL B 1 55  ? 6.167   1.945   27.467  1.00 17.38 ? 55  VAL B CA  1 
ATOM   2185 C C   . VAL B 1 55  ? 7.364   2.878   27.608  1.00 16.69 ? 55  VAL B C   1 
ATOM   2186 O O   . VAL B 1 55  ? 8.507   2.398   27.612  1.00 16.62 ? 55  VAL B O   1 
ATOM   2187 C CB  . VAL B 1 55  ? 5.425   1.823   28.800  1.00 14.54 ? 55  VAL B CB  1 
ATOM   2188 C CG1 . VAL B 1 55  ? 4.304   0.779   28.689  1.00 19.66 ? 55  VAL B CG1 1 
ATOM   2189 C CG2 . VAL B 1 55  ? 6.424   1.462   29.904  1.00 19.23 ? 55  VAL B CG2 1 
ATOM   2190 N N   . PRO B 1 56  ? 7.179   4.194   27.724  1.00 17.35 ? 56  PRO B N   1 
ATOM   2191 C CA  . PRO B 1 56  ? 8.348   5.066   27.888  1.00 15.24 ? 56  PRO B CA  1 
ATOM   2192 C C   . PRO B 1 56  ? 8.896   4.978   29.303  1.00 16.46 ? 56  PRO B C   1 
ATOM   2193 O O   . PRO B 1 56  ? 8.156   4.825   30.283  1.00 16.04 ? 56  PRO B O   1 
ATOM   2194 C CB  . PRO B 1 56  ? 7.814   6.474   27.560  1.00 16.45 ? 56  PRO B CB  1 
ATOM   2195 C CG  . PRO B 1 56  ? 6.435   6.259   26.975  1.00 16.40 ? 56  PRO B CG  1 
ATOM   2196 C CD  . PRO B 1 56  ? 5.938   4.972   27.510  1.00 18.83 ? 56  PRO B CD  1 
ATOM   2197 N N   . TRP B 1 57  ? 10.225  5.015   29.391  1.00 14.83 ? 57  TRP B N   1 
ATOM   2198 C CA  . TRP B 1 57  ? 10.890  4.955   30.689  1.00 14.04 ? 57  TRP B CA  1 
ATOM   2199 C C   . TRP B 1 57  ? 10.362  5.972   31.691  1.00 13.91 ? 57  TRP B C   1 
ATOM   2200 O O   . TRP B 1 57  ? 10.209  5.604   32.871  1.00 13.72 ? 57  TRP B O   1 
ATOM   2201 C CB  . TRP B 1 57  ? 12.407  5.136   30.509  1.00 14.71 ? 57  TRP B CB  1 
ATOM   2202 C CG  . TRP B 1 57  ? 13.092  3.884   30.082  1.00 15.58 ? 57  TRP B CG  1 
ATOM   2203 C CD1 . TRP B 1 57  ? 13.587  3.609   28.833  1.00 18.25 ? 57  TRP B CD1 1 
ATOM   2204 C CD2 . TRP B 1 57  ? 13.347  2.721   30.881  1.00 16.42 ? 57  TRP B CD2 1 
ATOM   2205 N NE1 . TRP B 1 57  ? 14.138  2.347   28.814  1.00 16.31 ? 57  TRP B NE1 1 
ATOM   2206 C CE2 . TRP B 1 57  ? 14.002  1.781   30.054  1.00 17.73 ? 57  TRP B CE2 1 
ATOM   2207 C CE3 . TRP B 1 57  ? 13.082  2.381   32.206  1.00 15.16 ? 57  TRP B CE3 1 
ATOM   2208 C CZ2 . TRP B 1 57  ? 14.406  0.543   30.513  1.00 16.46 ? 57  TRP B CZ2 1 
ATOM   2209 C CZ3 . TRP B 1 57  ? 13.488  1.133   32.666  1.00 18.50 ? 57  TRP B CZ3 1 
ATOM   2210 C CH2 . TRP B 1 57  ? 14.136  0.231   31.820  1.00 18.09 ? 57  TRP B CH2 1 
ATOM   2211 N N   . PRO B 1 58  ? 10.092  7.234   31.330  1.00 12.83 ? 58  PRO B N   1 
ATOM   2212 C CA  . PRO B 1 58  ? 9.581   8.178   32.341  1.00 13.35 ? 58  PRO B CA  1 
ATOM   2213 C C   . PRO B 1 58  ? 8.294   7.750   32.987  1.00 14.44 ? 58  PRO B C   1 
ATOM   2214 O O   . PRO B 1 58  ? 8.074   8.121   34.146  1.00 15.89 ? 58  PRO B O   1 
ATOM   2215 C CB  . PRO B 1 58  ? 9.399   9.482   31.557  1.00 15.77 ? 58  PRO B CB  1 
ATOM   2216 C CG  . PRO B 1 58  ? 10.389  9.375   30.449  1.00 15.62 ? 58  PRO B CG  1 
ATOM   2217 C CD  . PRO B 1 58  ? 10.393  7.924   30.057  1.00 15.12 ? 58  PRO B CD  1 
ATOM   2218 N N   . THR B 1 59  ? 7.441   6.975   32.300  1.00 12.30 ? 59  THR B N   1 
ATOM   2219 C CA  . THR B 1 59  ? 6.177   6.582   32.909  1.00 13.53 ? 59  THR B CA  1 
ATOM   2220 C C   . THR B 1 59  ? 6.369   5.587   34.033  1.00 13.35 ? 59  THR B C   1 
ATOM   2221 O O   . THR B 1 59  ? 5.423   5.379   34.798  1.00 13.76 ? 59  THR B O   1 
ATOM   2222 C CB  . THR B 1 59  ? 5.203   5.979   31.877  1.00 15.95 ? 59  THR B CB  1 
ATOM   2223 O OG1 . THR B 1 59  ? 5.638   4.663   31.510  1.00 14.81 ? 59  THR B OG1 1 
ATOM   2224 C CG2 . THR B 1 59  ? 5.094   6.839   30.622  1.00 14.55 ? 59  THR B CG2 1 
ATOM   2225 N N   . LEU B 1 60  ? 7.569   4.991   34.164  1.00 11.88 ? 60  LEU B N   1 
ATOM   2226 C CA  . LEU B 1 60  ? 7.855   4.072   35.256  1.00 11.79 ? 60  LEU B CA  1 
ATOM   2227 C C   . LEU B 1 60  ? 8.593   4.690   36.445  1.00 12.37 ? 60  LEU B C   1 
ATOM   2228 O O   . LEU B 1 60  ? 8.775   3.993   37.455  1.00 14.10 ? 60  LEU B O   1 
ATOM   2229 C CB  . LEU B 1 60  ? 8.663   2.874   34.760  1.00 11.96 ? 60  LEU B CB  1 
ATOM   2230 C CG  . LEU B 1 60  ? 7.938   2.000   33.714  1.00 13.23 ? 60  LEU B CG  1 
ATOM   2231 C CD1 . LEU B 1 60  ? 8.911   0.953   33.202  1.00 12.80 ? 60  LEU B CD1 1 
ATOM   2232 C CD2 . LEU B 1 60  ? 6.649   1.431   34.304  1.00 12.94 ? 60  LEU B CD2 1 
ATOM   2233 N N   . VAL B 1 61  ? 9.023   5.953   36.371  1.00 11.85 ? 61  VAL B N   1 
ATOM   2234 C CA  . VAL B 1 61  ? 9.870   6.510   37.431  1.00 12.48 ? 61  VAL B CA  1 
ATOM   2235 C C   . VAL B 1 61  ? 9.197   6.401   38.800  1.00 14.65 ? 61  VAL B C   1 
ATOM   2236 O O   . VAL B 1 61  ? 9.800   5.922   39.771  1.00 14.56 ? 61  VAL B O   1 
ATOM   2237 C CB  . VAL B 1 61  ? 10.260  7.963   37.106  1.00 16.30 ? 61  VAL B CB  1 
ATOM   2238 C CG1 . VAL B 1 61  ? 10.886  8.628   38.306  1.00 16.09 ? 61  VAL B CG1 1 
ATOM   2239 C CG2 . VAL B 1 61  ? 11.210  8.009   35.917  1.00 14.61 ? 61  VAL B CG2 1 
ATOM   2240 N N   . THR B 1 62  ? 7.931   6.829   38.910  1.00 15.44 ? 62  THR B N   1 
ATOM   2241 C CA  . THR B 1 62  ? 7.331   6.831   40.252  1.00 14.71 ? 62  THR B CA  1 
ATOM   2242 C C   . THR B 1 62  ? 7.183   5.414   40.794  1.00 14.31 ? 62  THR B C   1 
ATOM   2243 O O   . THR B 1 62  ? 7.232   5.204   42.015  1.00 15.20 ? 62  THR B O   1 
ATOM   2244 C CB  . THR B 1 62  ? 5.962   7.516   40.251  1.00 12.85 ? 62  THR B CB  1 
ATOM   2245 O OG1 . THR B 1 62  ? 5.160   6.957   39.195  1.00 12.07 ? 62  THR B OG1 1 
ATOM   2246 C CG2 . THR B 1 62  ? 6.131   9.000   39.986  1.00 13.90 ? 62  THR B CG2 1 
ATOM   2247 N N   . THR B 1 63  ? 6.981   4.431   39.917  1.00 15.15 ? 63  THR B N   1 
ATOM   2248 C CA  . THR B 1 63  ? 6.802   3.055   40.387  1.00 12.58 ? 63  THR B CA  1 
ATOM   2249 C C   . THR B 1 63  ? 8.122   2.417   40.810  1.00 15.73 ? 63  THR B C   1 
ATOM   2250 O O   . THR B 1 63  ? 8.205   1.769   41.869  1.00 12.59 ? 63  THR B O   1 
ATOM   2251 C CB  . THR B 1 63  ? 6.148   2.209   39.301  1.00 13.51 ? 63  THR B CB  1 
ATOM   2252 O OG1 . THR B 1 63  ? 4.868   2.771   38.961  1.00 12.44 ? 63  THR B OG1 1 
ATOM   2253 C CG2 . THR B 1 63  ? 6.006   0.759   39.781  1.00 16.71 ? 63  THR B CG2 1 
ATOM   2254 N N   . LEU B 1 64  ? 9.153   2.575   39.993  1.00 14.54 ? 64  LEU B N   1 
ATOM   2255 C CA  . LEU B 1 64  ? 10.505  2.135   40.328  1.00 14.02 ? 64  LEU B CA  1 
ATOM   2256 C C   . LEU B 1 64  ? 11.093  2.829   41.554  1.00 16.00 ? 64  LEU B C   1 
ATOM   2257 O O   . LEU B 1 64  ? 11.856  2.251   42.342  1.00 16.79 ? 64  LEU B O   1 
ATOM   2258 C CB  . LEU B 1 64  ? 11.398  2.360   39.110  1.00 16.64 ? 64  LEU B CB  1 
ATOM   2259 C CG  . LEU B 1 64  ? 10.964  1.601   37.854  1.00 13.30 ? 64  LEU B CG  1 
ATOM   2260 C CD1 . LEU B 1 64  ? 11.702  2.151   36.638  1.00 15.00 ? 64  LEU B CD1 1 
ATOM   2261 C CD2 . LEU B 1 64  ? 11.300  0.103   38.035  1.00 17.77 ? 64  LEU B CD2 1 
HETATM 2262 N N1  . CRO B 1 65  ? 10.990  4.254   41.528  1.00 17.99 ? 66  CRO B N1  1 
HETATM 2263 C CA1 . CRO B 1 65  ? 11.400  5.027   42.629  1.00 20.90 ? 66  CRO B CA1 1 
HETATM 2264 C CB1 . CRO B 1 65  ? 12.587  5.935   42.337  1.00 23.20 ? 66  CRO B CB1 1 
HETATM 2265 C CG1 . CRO B 1 65  ? 13.836  5.136   42.077  1.00 24.40 ? 66  CRO B CG1 1 
HETATM 2266 O OG1 . CRO B 1 65  ? 12.411  6.744   41.563  1.00 24.62 ? 66  CRO B OG1 1 
HETATM 2267 C C1  . CRO B 1 65  ? 10.312  5.715   43.441  1.00 21.76 ? 66  CRO B C1  1 
HETATM 2268 N N2  . CRO B 1 65  ? 10.000  6.948   43.280  1.00 22.47 ? 66  CRO B N2  1 
HETATM 2269 N N3  . CRO B 1 65  ? 9.449   5.169   44.230  1.00 23.25 ? 66  CRO B N3  1 
HETATM 2270 C C2  . CRO B 1 65  ? 8.572   6.060   44.534  1.00 21.79 ? 66  CRO B C2  1 
HETATM 2271 O O2  . CRO B 1 65  ? 7.484   5.860   45.324  1.00 18.00 ? 66  CRO B O2  1 
HETATM 2272 C CA2 . CRO B 1 65  ? 8.929   7.217   43.925  1.00 21.45 ? 66  CRO B CA2 1 
HETATM 2273 C CA3 . CRO B 1 65  ? 9.378   3.822   44.679  1.00 20.45 ? 66  CRO B CA3 1 
HETATM 2274 C C3  . CRO B 1 65  ? 10.023  3.576   46.050  1.00 23.06 ? 66  CRO B C3  1 
HETATM 2275 O O3  . CRO B 1 65  ? 9.730   2.576   46.562  1.00 21.42 ? 66  CRO B O3  1 
HETATM 2276 C CB2 . CRO B 1 65  ? 8.173   8.523   44.110  1.00 22.13 ? 66  CRO B CB2 1 
HETATM 2277 C CG2 . CRO B 1 65  ? 8.452   9.766   43.294  1.00 23.78 ? 66  CRO B CG2 1 
HETATM 2278 C CD1 . CRO B 1 65  ? 9.501   9.972   42.427  1.00 24.17 ? 66  CRO B CD1 1 
HETATM 2279 C CD2 . CRO B 1 65  ? 7.547   10.774  43.452  1.00 25.01 ? 66  CRO B CD2 1 
HETATM 2280 C CE1 . CRO B 1 65  ? 9.615   11.159  41.764  1.00 18.44 ? 66  CRO B CE1 1 
HETATM 2281 C CE2 . CRO B 1 65  ? 7.637   11.949  42.786  1.00 21.78 ? 66  CRO B CE2 1 
HETATM 2282 C CZ  . CRO B 1 65  ? 8.682   12.149  41.944  1.00 24.82 ? 66  CRO B CZ  1 
HETATM 2283 O OH  . CRO B 1 65  ? 8.752   13.343  41.293  1.00 24.68 ? 66  CRO B OH  1 
ATOM   2284 N N   . VAL B 1 66  ? 11.081  4.446   46.322  1.00 16.12 ? 68  VAL B N   1 
ATOM   2285 C CA  . VAL B 1 66  ? 11.639  3.986   47.558  1.00 14.11 ? 68  VAL B CA  1 
ATOM   2286 C C   . VAL B 1 66  ? 11.742  5.240   48.400  1.00 15.86 ? 68  VAL B C   1 
ATOM   2287 O O   . VAL B 1 66  ? 12.831  5.756   48.659  1.00 16.79 ? 68  VAL B O   1 
ATOM   2288 C CB  . VAL B 1 66  ? 13.023  3.371   47.267  1.00 15.80 ? 68  VAL B CB  1 
ATOM   2289 C CG1 . VAL B 1 66  ? 12.843  1.973   46.692  1.00 16.97 ? 68  VAL B CG1 1 
ATOM   2290 C CG2 . VAL B 1 66  ? 13.822  4.224   46.296  1.00 18.81 ? 68  VAL B CG2 1 
ATOM   2291 N N   . GLN B 1 67  ? 10.579  5.749   48.813  1.00 17.23 ? 69  GLN B N   1 
ATOM   2292 C CA  . GLN B 1 67  ? 10.529  7.025   49.512  1.00 18.12 ? 69  GLN B CA  1 
ATOM   2293 C C   . GLN B 1 67  ? 11.155  6.962   50.889  1.00 21.72 ? 69  GLN B C   1 
ATOM   2294 O O   . GLN B 1 67  ? 11.213  7.993   51.569  1.00 21.42 ? 69  GLN B O   1 
ATOM   2295 C CB  . GLN B 1 67  ? 9.076   7.505   49.594  1.00 17.88 ? 69  GLN B CB  1 
ATOM   2296 C CG  . GLN B 1 67  ? 8.449   7.702   48.199  1.00 18.72 ? 69  GLN B CG  1 
ATOM   2297 C CD  . GLN B 1 67  ? 6.945   7.877   48.221  1.00 20.12 ? 69  GLN B CD  1 
ATOM   2298 O OE1 . GLN B 1 67  ? 6.225   6.998   48.702  1.00 18.18 ? 69  GLN B OE1 1 
ATOM   2299 N NE2 . GLN B 1 67  ? 6.445   8.995   47.631  1.00 16.53 ? 69  GLN B NE2 1 
ATOM   2300 N N   . CYS B 1 68  ? 11.627  5.789   51.313  1.00 23.29 ? 70  CYS B N   1 
ATOM   2301 C CA  . CYS B 1 68  ? 12.403  5.684   52.538  1.00 20.59 ? 70  CYS B CA  1 
ATOM   2302 C C   . CYS B 1 68  ? 13.738  6.402   52.450  1.00 24.06 ? 70  CYS B C   1 
ATOM   2303 O O   . CYS B 1 68  ? 14.403  6.570   53.483  1.00 22.33 ? 70  CYS B O   1 
ATOM   2304 C CB  . CYS B 1 68  ? 12.592  4.197   52.892  1.00 22.05 ? 70  CYS B CB  1 
ATOM   2305 S SG  . CYS B 1 68  ? 13.172  3.132   51.523  1.00 20.10 ? 70  CYS B SG  1 
ATOM   2306 N N   . PHE B 1 69  ? 14.150  6.851   51.263  1.00 18.08 ? 71  PHE B N   1 
ATOM   2307 C CA  . PHE B 1 69  ? 15.465  7.461   51.127  1.00 20.06 ? 71  PHE B CA  1 
ATOM   2308 C C   . PHE B 1 69  ? 15.419  8.979   51.186  1.00 23.37 ? 71  PHE B C   1 
ATOM   2309 O O   . PHE B 1 69  ? 16.410  9.638   50.855  1.00 24.22 ? 71  PHE B O   1 
ATOM   2310 C CB  . PHE B 1 69  ? 16.132  6.979   49.842  1.00 20.87 ? 71  PHE B CB  1 
ATOM   2311 C CG  . PHE B 1 69  ? 16.737  5.608   49.978  1.00 20.35 ? 71  PHE B CG  1 
ATOM   2312 C CD1 . PHE B 1 69  ? 17.889  5.415   50.721  1.00 20.52 ? 71  PHE B CD1 1 
ATOM   2313 C CD2 . PHE B 1 69  ? 16.118  4.503   49.393  1.00 17.75 ? 71  PHE B CD2 1 
ATOM   2314 C CE1 . PHE B 1 69  ? 18.444  4.142   50.862  1.00 21.97 ? 71  PHE B CE1 1 
ATOM   2315 C CE2 . PHE B 1 69  ? 16.669  3.212   49.535  1.00 18.48 ? 71  PHE B CE2 1 
ATOM   2316 C CZ  . PHE B 1 69  ? 17.829  3.042   50.268  1.00 22.23 ? 71  PHE B CZ  1 
ATOM   2317 N N   . SER B 1 70  ? 14.325  9.562   51.649  1.00 23.88 ? 72  SER B N   1 
ATOM   2318 C CA  . SER B 1 70  ? 14.288  11.015  51.698  1.00 24.77 ? 72  SER B CA  1 
ATOM   2319 C C   . SER B 1 70  ? 15.050  11.545  52.905  1.00 27.23 ? 72  SER B C   1 
ATOM   2320 O O   . SER B 1 70  ? 15.172  10.891  53.950  1.00 26.50 ? 72  SER B O   1 
ATOM   2321 C CB  . SER B 1 70  ? 12.854  11.531  51.719  1.00 27.37 ? 72  SER B CB  1 
ATOM   2322 O OG  . SER B 1 70  ? 12.263  11.249  52.949  1.00 34.12 ? 72  SER B OG  1 
ATOM   2323 N N   . ARG B 1 71  ? 15.606  12.734  52.730  1.00 24.47 ? 73  ARG B N   1 
ATOM   2324 C CA  . ARG B 1 71  ? 16.258  13.447  53.819  1.00 28.19 ? 73  ARG B CA  1 
ATOM   2325 C C   . ARG B 1 71  ? 15.182  14.135  54.649  1.00 33.59 ? 73  ARG B C   1 
ATOM   2326 O O   . ARG B 1 71  ? 14.619  15.151  54.234  1.00 31.75 ? 73  ARG B O   1 
ATOM   2327 C CB  . ARG B 1 71  ? 17.252  14.451  53.261  1.00 25.41 ? 73  ARG B CB  1 
ATOM   2328 C CG  . ARG B 1 71  ? 17.912  15.294  54.310  1.00 30.23 ? 73  ARG B CG  1 
ATOM   2329 C CD  . ARG B 1 71  ? 19.019  16.093  53.664  1.00 30.54 ? 73  ARG B CD  1 
ATOM   2330 N NE  . ARG B 1 71  ? 18.482  17.269  52.988  1.00 34.82 ? 73  ARG B NE  1 
ATOM   2331 C CZ  . ARG B 1 71  ? 17.986  18.335  53.604  1.00 35.50 ? 73  ARG B CZ  1 
ATOM   2332 N NH1 . ARG B 1 71  ? 17.988  18.437  54.925  1.00 39.73 ? 73  ARG B NH1 1 
ATOM   2333 N NH2 . ARG B 1 71  ? 17.475  19.323  52.876  1.00 36.38 ? 73  ARG B NH2 1 
ATOM   2334 N N   . TYR B 1 72  ? 14.864  13.553  55.811  1.00 36.08 ? 74  TYR B N   1 
ATOM   2335 C CA  . TYR B 1 72  ? 13.974  14.189  56.777  1.00 41.74 ? 74  TYR B CA  1 
ATOM   2336 C C   . TYR B 1 72  ? 14.845  14.975  57.745  1.00 49.11 ? 74  TYR B C   1 
ATOM   2337 O O   . TYR B 1 72  ? 15.658  14.362  58.450  1.00 51.68 ? 74  TYR B O   1 
ATOM   2338 C CB  . TYR B 1 72  ? 13.166  13.148  57.562  1.00 42.94 ? 74  TYR B CB  1 
ATOM   2339 C CG  . TYR B 1 72  ? 11.865  12.639  56.944  1.00 37.97 ? 74  TYR B CG  1 
ATOM   2340 C CD1 . TYR B 1 72  ? 11.889  11.829  55.821  1.00 35.86 ? 74  TYR B CD1 1 
ATOM   2341 C CD2 . TYR B 1 72  ? 10.615  12.927  57.511  1.00 38.86 ? 74  TYR B CD2 1 
ATOM   2342 C CE1 . TYR B 1 72  ? 10.713  11.331  55.253  1.00 33.56 ? 74  TYR B CE1 1 
ATOM   2343 C CE2 . TYR B 1 72  ? 9.419   12.432  56.938  1.00 35.11 ? 74  TYR B CE2 1 
ATOM   2344 C CZ  . TYR B 1 72  ? 9.485   11.636  55.796  1.00 35.90 ? 74  TYR B CZ  1 
ATOM   2345 O OH  . TYR B 1 72  ? 8.357   11.118  55.168  1.00 28.31 ? 74  TYR B OH  1 
ATOM   2346 N N   . PRO B 1 73  ? 14.751  16.306  57.799  1.00 48.69 ? 75  PRO B N   1 
ATOM   2347 C CA  . PRO B 1 73  ? 15.498  17.049  58.826  1.00 51.76 ? 75  PRO B CA  1 
ATOM   2348 C C   . PRO B 1 73  ? 15.119  16.615  60.240  1.00 57.36 ? 75  PRO B C   1 
ATOM   2349 O O   . PRO B 1 73  ? 14.060  16.029  60.478  1.00 57.98 ? 75  PRO B O   1 
ATOM   2350 C CB  . PRO B 1 73  ? 15.127  18.514  58.559  1.00 46.51 ? 75  PRO B CB  1 
ATOM   2351 C CG  . PRO B 1 73  ? 13.890  18.475  57.739  1.00 52.76 ? 75  PRO B CG  1 
ATOM   2352 C CD  . PRO B 1 73  ? 13.928  17.191  56.956  1.00 44.91 ? 75  PRO B CD  1 
ATOM   2353 N N   . ASP B 1 74  ? 16.023  16.909  61.188  1.00 60.30 ? 76  ASP B N   1 
ATOM   2354 C CA  . ASP B 1 74  ? 15.941  16.345  62.538  1.00 61.33 ? 76  ASP B CA  1 
ATOM   2355 C C   . ASP B 1 74  ? 14.579  16.565  63.191  1.00 63.40 ? 76  ASP B C   1 
ATOM   2356 O O   . ASP B 1 74  ? 14.038  15.655  63.833  1.00 64.76 ? 76  ASP B O   1 
ATOM   2357 C CB  . ASP B 1 74  ? 17.044  16.931  63.427  1.00 62.86 ? 76  ASP B CB  1 
ATOM   2358 C CG  . ASP B 1 74  ? 18.439  16.522  62.981  1.00 70.22 ? 76  ASP B CG  1 
ATOM   2359 O OD1 . ASP B 1 74  ? 18.622  15.339  62.618  1.00 74.04 ? 76  ASP B OD1 1 
ATOM   2360 O OD2 . ASP B 1 74  ? 19.355  17.375  63.008  1.00 66.27 ? 76  ASP B OD2 1 
ATOM   2361 N N   . HIS B 1 75  ? 14.009  17.766  63.049  1.00 61.39 ? 77  HIS B N   1 
ATOM   2362 C CA  . HIS B 1 75  ? 12.725  18.048  63.685  1.00 61.66 ? 77  HIS B CA  1 
ATOM   2363 C C   . HIS B 1 75  ? 11.591  17.195  63.117  1.00 60.79 ? 77  HIS B C   1 
ATOM   2364 O O   . HIS B 1 75  ? 10.550  17.052  63.769  1.00 58.79 ? 77  HIS B O   1 
ATOM   2365 C CB  . HIS B 1 75  ? 12.421  19.549  63.576  1.00 63.16 ? 77  HIS B CB  1 
ATOM   2366 C CG  . HIS B 1 75  ? 11.550  19.925  62.415  1.00 61.81 ? 77  HIS B CG  1 
ATOM   2367 N ND1 . HIS B 1 75  ? 12.055  20.167  61.155  1.00 62.62 ? 77  HIS B ND1 1 
ATOM   2368 C CD2 . HIS B 1 75  ? 10.217  20.148  62.334  1.00 61.00 ? 77  HIS B CD2 1 
ATOM   2369 C CE1 . HIS B 1 75  ? 11.068  20.502  60.343  1.00 62.24 ? 77  HIS B CE1 1 
ATOM   2370 N NE2 . HIS B 1 75  ? 9.941   20.497  61.033  1.00 60.58 ? 77  HIS B NE2 1 
ATOM   2371 N N   . MET B 1 76  ? 11.782  16.660  61.916  1.00 59.67 ? 78  MET B N   1 
ATOM   2372 C CA  . MET B 1 76  ? 10.753  15.861  61.262  1.00 60.39 ? 78  MET B CA  1 
ATOM   2373 C C   . MET B 1 76  ? 11.177  14.402  61.154  1.00 61.53 ? 78  MET B C   1 
ATOM   2374 O O   . MET B 1 76  ? 10.844  13.717  60.186  1.00 61.55 ? 78  MET B O   1 
ATOM   2375 C CB  . MET B 1 76  ? 10.441  16.422  59.873  1.00 54.63 ? 78  MET B CB  1 
ATOM   2376 C CG  . MET B 1 76  ? 10.160  17.916  59.857  1.00 55.90 ? 78  MET B CG  1 
ATOM   2377 S SD  . MET B 1 76  ? 8.579   18.317  59.088  1.00 61.38 ? 78  MET B SD  1 
ATOM   2378 C CE  . MET B 1 76  ? 8.670   17.334  57.594  1.00 38.79 ? 78  MET B CE  1 
ATOM   2379 N N   . LYS B 1 77  ? 11.915  13.932  62.154  1.00 61.65 ? 79  LYS B N   1 
ATOM   2380 C CA  . LYS B 1 77  ? 12.387  12.554  62.172  1.00 62.49 ? 79  LYS B CA  1 
ATOM   2381 C C   . LYS B 1 77  ? 11.461  11.665  62.994  1.00 65.51 ? 79  LYS B C   1 
ATOM   2382 O O   . LYS B 1 77  ? 11.810  10.532  63.326  1.00 69.66 ? 79  LYS B O   1 
ATOM   2383 C CB  . LYS B 1 77  ? 13.811  12.483  62.726  1.00 61.82 ? 79  LYS B CB  1 
ATOM   2384 C CG  . LYS B 1 77  ? 14.837  11.958  61.735  1.00 62.41 ? 79  LYS B CG  1 
ATOM   2385 C CD  . LYS B 1 77  ? 16.228  12.483  62.049  1.00 64.37 ? 79  LYS B CD  1 
ATOM   2386 C CE  . LYS B 1 77  ? 16.976  12.861  60.781  1.00 67.24 ? 79  LYS B CE  1 
ATOM   2387 N NZ  . LYS B 1 77  ? 18.451  12.846  60.981  1.00 73.61 ? 79  LYS B NZ  1 
ATOM   2388 N N   . ARG B 1 78  ? 10.304  12.208  63.347  1.00 57.46 ? 80  ARG B N   1 
ATOM   2389 C CA  . ARG B 1 78  ? 9.304   11.460  64.083  1.00 59.90 ? 80  ARG B CA  1 
ATOM   2390 C C   . ARG B 1 78  ? 8.137   11.206  63.149  1.00 57.21 ? 80  ARG B C   1 
ATOM   2391 O O   . ARG B 1 78  ? 7.097   10.693  63.562  1.00 56.32 ? 80  ARG B O   1 
ATOM   2392 C CB  . ARG B 1 78  ? 8.840   12.242  65.311  1.00 64.00 ? 80  ARG B CB  1 
ATOM   2393 C CG  . ARG B 1 78  ? 9.009   11.495  66.624  1.00 62.34 ? 80  ARG B CG  1 
ATOM   2394 C CD  . ARG B 1 78  ? 9.190   12.456  67.787  1.00 59.79 ? 80  ARG B CD  1 
ATOM   2395 N NE  . ARG B 1 78  ? 10.598  12.659  68.115  1.00 64.05 ? 80  ARG B NE  1 
ATOM   2396 C CZ  . ARG B 1 78  ? 11.141  13.843  68.377  1.00 64.19 ? 80  ARG B CZ  1 
ATOM   2397 N NH1 . ARG B 1 78  ? 10.393  14.938  68.351  1.00 59.86 ? 80  ARG B NH1 1 
ATOM   2398 N NH2 . ARG B 1 78  ? 12.432  13.935  68.666  1.00 66.96 ? 80  ARG B NH2 1 
ATOM   2399 N N   . HIS B 1 79  ? 8.314   11.570  61.882  1.00 56.16 ? 81  HIS B N   1 
ATOM   2400 C CA  . HIS B 1 79  ? 7.264   11.395  60.932  1.00 51.17 ? 81  HIS B CA  1 
ATOM   2401 C C   . HIS B 1 79  ? 7.702   10.563  59.799  1.00 45.06 ? 81  HIS B C   1 
ATOM   2402 O O   . HIS B 1 79  ? 7.141   10.676  58.737  1.00 43.98 ? 81  HIS B O   1 
ATOM   2403 C CB  . HIS B 1 79  ? 6.853   12.780  60.440  1.00 49.67 ? 81  HIS B CB  1 
ATOM   2404 C CG  . HIS B 1 79  ? 6.403   13.655  61.558  1.00 55.12 ? 81  HIS B CG  1 
ATOM   2405 N ND1 . HIS B 1 79  ? 5.091   13.738  61.949  1.00 50.95 ? 81  HIS B ND1 1 
ATOM   2406 C CD2 . HIS B 1 79  ? 7.108   14.382  62.447  1.00 59.44 ? 81  HIS B CD2 1 
ATOM   2407 C CE1 . HIS B 1 79  ? 5.000   14.531  62.993  1.00 54.59 ? 81  HIS B CE1 1 
ATOM   2408 N NE2 . HIS B 1 79  ? 6.208   14.940  63.313  1.00 59.54 ? 81  HIS B NE2 1 
ATOM   2409 N N   . ASP B 1 80  ? 8.718   9.741   60.004  1.00 43.60 ? 82  ASP B N   1 
ATOM   2410 C CA  . ASP B 1 80  ? 9.237   8.952   58.899  1.00 35.82 ? 82  ASP B CA  1 
ATOM   2411 C C   . ASP B 1 80  ? 8.671   7.560   58.914  1.00 32.49 ? 82  ASP B C   1 
ATOM   2412 O O   . ASP B 1 80  ? 9.308   6.630   59.287  1.00 28.89 ? 82  ASP B O   1 
ATOM   2413 C CB  . ASP B 1 80  ? 10.760  8.956   58.872  1.00 33.70 ? 82  ASP B CB  1 
ATOM   2414 C CG  . ASP B 1 80  ? 11.319  8.687   57.520  1.00 32.50 ? 82  ASP B CG  1 
ATOM   2415 O OD1 . ASP B 1 80  ? 10.597  8.224   56.665  1.00 28.69 ? 82  ASP B OD1 1 
ATOM   2416 O OD2 . ASP B 1 80  ? 12.511  8.927   57.349  1.00 34.55 ? 82  ASP B OD2 1 
ATOM   2417 N N   . PHE B 1 81  ? 7.443   7.451   58.479  1.00 27.90 ? 83  PHE B N   1 
ATOM   2418 C CA  . PHE B 1 81  ? 6.795   6.149   58.369  1.00 28.44 ? 83  PHE B CA  1 
ATOM   2419 C C   . PHE B 1 81  ? 7.610   5.182   57.519  1.00 26.02 ? 83  PHE B C   1 
ATOM   2420 O O   . PHE B 1 81  ? 7.733   3.998   57.858  1.00 23.46 ? 83  PHE B O   1 
ATOM   2421 C CB  . PHE B 1 81  ? 5.399   6.329   57.761  1.00 27.11 ? 83  PHE B CB  1 
ATOM   2422 C CG  . PHE B 1 81  ? 4.821   5.080   57.173  1.00 26.34 ? 83  PHE B CG  1 
ATOM   2423 C CD1 . PHE B 1 81  ? 4.032   4.250   57.954  1.00 28.01 ? 83  PHE B CD1 1 
ATOM   2424 C CD2 . PHE B 1 81  ? 5.033   4.742   55.841  1.00 24.68 ? 83  PHE B CD2 1 
ATOM   2425 C CE1 . PHE B 1 81  ? 3.487   3.085   57.438  1.00 30.04 ? 83  PHE B CE1 1 
ATOM   2426 C CE2 . PHE B 1 81  ? 4.487   3.574   55.305  1.00 25.40 ? 83  PHE B CE2 1 
ATOM   2427 C CZ  . PHE B 1 81  ? 3.700   2.746   56.111  1.00 26.76 ? 83  PHE B CZ  1 
ATOM   2428 N N   . PHE B 1 82  ? 8.142   5.664   56.392  1.00 22.34 ? 84  PHE B N   1 
ATOM   2429 C CA  . PHE B 1 82  ? 8.810   4.776   55.446  1.00 21.35 ? 84  PHE B CA  1 
ATOM   2430 C C   . PHE B 1 82  ? 10.005  4.080   56.076  1.00 23.48 ? 84  PHE B C   1 
ATOM   2431 O O   . PHE B 1 82  ? 10.207  2.877   55.877  1.00 22.19 ? 84  PHE B O   1 
ATOM   2432 C CB  . PHE B 1 82  ? 9.245   5.563   54.210  1.00 22.60 ? 84  PHE B CB  1 
ATOM   2433 C CG  . PHE B 1 82  ? 8.129   6.280   53.542  1.00 24.53 ? 84  PHE B CG  1 
ATOM   2434 C CD1 . PHE B 1 82  ? 7.204   5.592   52.775  1.00 25.14 ? 84  PHE B CD1 1 
ATOM   2435 C CD2 . PHE B 1 82  ? 7.980   7.644   53.698  1.00 26.65 ? 84  PHE B CD2 1 
ATOM   2436 C CE1 . PHE B 1 82  ? 6.158   6.270   52.147  1.00 24.76 ? 84  PHE B CE1 1 
ATOM   2437 C CE2 . PHE B 1 82  ? 6.942   8.318   53.080  1.00 24.80 ? 84  PHE B CE2 1 
ATOM   2438 C CZ  . PHE B 1 82  ? 6.034   7.631   52.308  1.00 23.12 ? 84  PHE B CZ  1 
ATOM   2439 N N   . LYS B 1 83  ? 10.812  4.814   56.837  1.00 20.66 ? 85  LYS B N   1 
ATOM   2440 C CA  . LYS B 1 83  ? 11.966  4.186   57.460  1.00 20.98 ? 85  LYS B CA  1 
ATOM   2441 C C   . LYS B 1 83  ? 11.560  3.398   58.693  1.00 25.27 ? 85  LYS B C   1 
ATOM   2442 O O   . LYS B 1 83  ? 12.086  2.306   58.933  1.00 21.79 ? 85  LYS B O   1 
ATOM   2443 C CB  . LYS B 1 83  ? 13.009  5.230   57.830  1.00 22.85 ? 85  LYS B CB  1 
ATOM   2444 C CG  . LYS B 1 83  ? 13.663  5.952   56.686  1.00 25.41 ? 85  LYS B CG  1 
ATOM   2445 C CD  . LYS B 1 83  ? 14.871  6.724   57.242  1.00 28.75 ? 85  LYS B CD  1 
ATOM   2446 C CE  . LYS B 1 83  ? 15.467  7.663   56.223  1.00 30.67 ? 85  LYS B CE  1 
ATOM   2447 N NZ  . LYS B 1 83  ? 14.482  8.671   55.821  1.00 26.14 ? 85  LYS B NZ  1 
ATOM   2448 N N   . SER B 1 84  ? 10.609  3.922   59.470  1.00 25.87 ? 86  SER B N   1 
ATOM   2449 C CA  . SER B 1 84  ? 10.217  3.259   60.705  1.00 30.08 ? 86  SER B CA  1 
ATOM   2450 C C   . SER B 1 84  ? 9.615   1.884   60.453  1.00 28.01 ? 86  SER B C   1 
ATOM   2451 O O   . SER B 1 84  ? 9.654   1.027   61.349  1.00 26.11 ? 86  SER B O   1 
ATOM   2452 C CB  . SER B 1 84  ? 9.249   4.150   61.487  1.00 33.45 ? 86  SER B CB  1 
ATOM   2453 O OG  . SER B 1 84  ? 7.903   3.837   61.173  1.00 40.82 ? 86  SER B OG  1 
ATOM   2454 N N   . ALA B 1 85  ? 9.068   1.649   59.262  1.00 22.04 ? 87  ALA B N   1 
ATOM   2455 C CA  . ALA B 1 85  ? 8.588   0.317   58.903  1.00 25.03 ? 87  ALA B CA  1 
ATOM   2456 C C   . ALA B 1 85  ? 9.718   -0.656  58.614  1.00 23.77 ? 87  ALA B C   1 
ATOM   2457 O O   . ALA B 1 85  ? 9.455   -1.851  58.433  1.00 25.02 ? 87  ALA B O   1 
ATOM   2458 C CB  . ALA B 1 85  ? 7.672   0.372   57.677  1.00 24.25 ? 87  ALA B CB  1 
ATOM   2459 N N   . MET B 1 86  ? 10.939  -0.193  58.534  1.00 21.47 ? 88  MET B N   1 
ATOM   2460 C CA  . MET B 1 86  ? 11.949  -1.186  58.214  1.00 24.98 ? 88  MET B CA  1 
ATOM   2461 C C   . MET B 1 86  ? 12.500  -1.857  59.461  1.00 25.28 ? 88  MET B C   1 
ATOM   2462 O O   . MET B 1 86  ? 12.433  -1.305  60.559  1.00 27.24 ? 88  MET B O   1 
ATOM   2463 C CB  . MET B 1 86  ? 13.085  -0.558  57.411  1.00 23.72 ? 88  MET B CB  1 
ATOM   2464 C CG  . MET B 1 86  ? 12.654  0.265   56.223  1.00 19.35 ? 88  MET B CG  1 
ATOM   2465 S SD  . MET B 1 86  ? 12.221  -0.990  54.984  1.00 21.30 ? 88  MET B SD  1 
ATOM   2466 C CE  . MET B 1 86  ? 11.095  -0.076  53.924  1.00 20.05 ? 88  MET B CE  1 
ATOM   2467 N N   . PRO B 1 87  ? 13.093  -3.058  59.318  1.00 24.07 ? 89  PRO B N   1 
ATOM   2468 C CA  . PRO B 1 87  ? 13.378  -3.786  58.071  1.00 25.78 ? 89  PRO B CA  1 
ATOM   2469 C C   . PRO B 1 87  ? 12.240  -4.586  57.476  1.00 26.38 ? 89  PRO B C   1 
ATOM   2470 O O   . PRO B 1 87  ? 12.377  -4.949  56.301  1.00 29.91 ? 89  PRO B O   1 
ATOM   2471 C CB  . PRO B 1 87  ? 14.520  -4.718  58.480  1.00 30.45 ? 89  PRO B CB  1 
ATOM   2472 C CG  . PRO B 1 87  ? 14.209  -5.052  59.914  1.00 26.76 ? 89  PRO B CG  1 
ATOM   2473 C CD  . PRO B 1 87  ? 13.568  -3.801  60.501  1.00 25.45 ? 89  PRO B CD  1 
ATOM   2474 N N   . GLU B 1 88  ? 11.161  -4.868  58.221  1.00 20.69 ? 90  GLU B N   1 
ATOM   2475 C CA  . GLU B 1 88  ? 10.108  -5.710  57.656  1.00 25.27 ? 90  GLU B CA  1 
ATOM   2476 C C   . GLU B 1 88  ? 9.494   -5.079  56.411  1.00 23.39 ? 90  GLU B C   1 
ATOM   2477 O O   . GLU B 1 88  ? 9.106   -5.792  55.477  1.00 23.91 ? 90  GLU B O   1 
ATOM   2478 C CB  . GLU B 1 88  ? 9.034   -5.986  58.703  1.00 26.33 ? 90  GLU B CB  1 
ATOM   2479 C CG  . GLU B 1 88  ? 9.559   -6.791  59.863  1.00 30.14 ? 90  GLU B CG  1 
ATOM   2480 C CD  . GLU B 1 88  ? 10.099  -5.926  60.986  1.00 35.34 ? 90  GLU B CD  1 
ATOM   2481 O OE1 . GLU B 1 88  ? 10.310  -4.701  60.781  1.00 29.25 ? 90  GLU B OE1 1 
ATOM   2482 O OE2 . GLU B 1 88  ? 10.344  -6.485  62.073  1.00 40.07 ? 90  GLU B OE2 1 
ATOM   2483 N N   . GLY B 1 89  ? 9.424   -3.761  56.365  1.00 22.31 ? 91  GLY B N   1 
ATOM   2484 C CA  . GLY B 1 89  ? 9.075   -3.073  55.136  1.00 22.63 ? 91  GLY B CA  1 
ATOM   2485 C C   . GLY B 1 89  ? 7.608   -2.718  55.039  1.00 23.20 ? 91  GLY B C   1 
ATOM   2486 O O   . GLY B 1 89  ? 6.853   -2.755  56.016  1.00 20.50 ? 91  GLY B O   1 
ATOM   2487 N N   . TYR B 1 90  ? 7.199   -2.364  53.813  1.00 17.41 ? 92  TYR B N   1 
ATOM   2488 C CA  . TYR B 1 90  ? 5.835   -1.906  53.602  1.00 20.34 ? 92  TYR B CA  1 
ATOM   2489 C C   . TYR B 1 90  ? 5.396   -2.302  52.207  1.00 21.34 ? 92  TYR B C   1 
ATOM   2490 O O   . TYR B 1 90  ? 6.225   -2.512  51.317  1.00 19.05 ? 92  TYR B O   1 
ATOM   2491 C CB  . TYR B 1 90  ? 5.677   -0.383  53.802  1.00 20.85 ? 92  TYR B CB  1 
ATOM   2492 C CG  . TYR B 1 90  ? 6.593   0.516   52.982  1.00 19.92 ? 92  TYR B CG  1 
ATOM   2493 C CD1 . TYR B 1 90  ? 6.329   0.795   51.639  1.00 16.82 ? 92  TYR B CD1 1 
ATOM   2494 C CD2 . TYR B 1 90  ? 7.687   1.132   53.569  1.00 18.13 ? 92  TYR B CD2 1 
ATOM   2495 C CE1 . TYR B 1 90  ? 7.180   1.628   50.907  1.00 17.29 ? 92  TYR B CE1 1 
ATOM   2496 C CE2 . TYR B 1 90  ? 8.518   1.962   52.859  1.00 18.81 ? 92  TYR B CE2 1 
ATOM   2497 C CZ  . TYR B 1 90  ? 8.263   2.213   51.527  1.00 16.41 ? 92  TYR B CZ  1 
ATOM   2498 O OH  . TYR B 1 90  ? 9.123   3.057   50.828  1.00 17.75 ? 92  TYR B OH  1 
ATOM   2499 N N   . VAL B 1 91  ? 4.092   -2.431  52.038  1.00 19.51 ? 93  VAL B N   1 
ATOM   2500 C CA  . VAL B 1 91  ? 3.511   -2.653  50.725  1.00 18.76 ? 93  VAL B CA  1 
ATOM   2501 C C   . VAL B 1 91  ? 3.132   -1.286  50.174  1.00 21.36 ? 93  VAL B C   1 
ATOM   2502 O O   . VAL B 1 91  ? 2.532   -0.471  50.880  1.00 20.43 ? 93  VAL B O   1 
ATOM   2503 C CB  . VAL B 1 91  ? 2.289   -3.577  50.808  1.00 23.66 ? 93  VAL B CB  1 
ATOM   2504 C CG1 . VAL B 1 91  ? 1.556   -3.597  49.468  1.00 21.74 ? 93  VAL B CG1 1 
ATOM   2505 C CG2 . VAL B 1 91  ? 2.691   -5.000  51.237  1.00 23.45 ? 93  VAL B CG2 1 
ATOM   2506 N N   . GLN B 1 92  ? 3.492   -1.024  48.922  1.00 18.29 ? 94  GLN B N   1 
ATOM   2507 C CA  . GLN B 1 92  ? 3.150   0.226   48.254  1.00 16.73 ? 94  GLN B CA  1 
ATOM   2508 C C   . GLN B 1 92  ? 2.275   -0.103  47.064  1.00 18.34 ? 94  GLN B C   1 
ATOM   2509 O O   . GLN B 1 92  ? 2.695   -0.845  46.171  1.00 19.45 ? 94  GLN B O   1 
ATOM   2510 C CB  . GLN B 1 92  ? 4.400   0.979   47.790  1.00 17.08 ? 94  GLN B CB  1 
ATOM   2511 C CG  . GLN B 1 92  ? 4.038   2.297   47.106  1.00 16.40 ? 94  GLN B CG  1 
ATOM   2512 C CD  . GLN B 1 92  ? 5.203   3.260   47.044  1.00 17.83 ? 94  GLN B CD  1 
ATOM   2513 O OE1 . GLN B 1 92  ? 5.663   3.724   48.078  1.00 17.64 ? 94  GLN B OE1 1 
ATOM   2514 N NE2 . GLN B 1 92  ? 5.626   3.631   45.834  1.00 15.77 ? 94  GLN B NE2 1 
ATOM   2515 N N   . GLU B 1 93  ? 1.067   0.440   47.042  1.00 17.29 ? 95  GLU B N   1 
ATOM   2516 C CA  . GLU B 1 93  ? 0.155   0.177   45.943  1.00 20.18 ? 95  GLU B CA  1 
ATOM   2517 C C   . GLU B 1 93  ? -0.238  1.483   45.287  1.00 19.87 ? 95  GLU B C   1 
ATOM   2518 O O   . GLU B 1 93  ? -0.430  2.488   45.970  1.00 18.29 ? 95  GLU B O   1 
ATOM   2519 C CB  . GLU B 1 93  ? -1.099  -0.565  46.410  1.00 23.66 ? 95  GLU B CB  1 
ATOM   2520 C CG  . GLU B 1 93  ? -0.852  -2.046  46.612  1.00 25.75 ? 95  GLU B CG  1 
ATOM   2521 C CD  . GLU B 1 93  ? -1.831  -2.727  47.572  1.00 29.58 ? 95  GLU B CD  1 
ATOM   2522 O OE1 . GLU B 1 93  ? -2.211  -2.154  48.623  1.00 33.58 ? 95  GLU B OE1 1 
ATOM   2523 O OE2 . GLU B 1 93  ? -2.223  -3.863  47.240  1.00 30.22 ? 95  GLU B OE2 1 
ATOM   2524 N N   . ARG B 1 94  ? -0.394  1.454   43.964  1.00 18.03 ? 96  ARG B N   1 
ATOM   2525 C CA  . ARG B 1 94  ? -0.822  2.634   43.241  1.00 17.15 ? 96  ARG B CA  1 
ATOM   2526 C C   . ARG B 1 94  ? -1.774  2.251   42.122  1.00 20.80 ? 96  ARG B C   1 
ATOM   2527 O O   . ARG B 1 94  ? -1.691  1.159   41.548  1.00 18.83 ? 96  ARG B O   1 
ATOM   2528 C CB  . ARG B 1 94  ? 0.368   3.406   42.645  1.00 17.81 ? 96  ARG B CB  1 
ATOM   2529 C CG  . ARG B 1 94  ? 1.214   4.145   43.674  1.00 15.78 ? 96  ARG B CG  1 
ATOM   2530 C CD  . ARG B 1 94  ? 1.729   5.420   43.056  1.00 15.37 ? 96  ARG B CD  1 
ATOM   2531 N NE  . ARG B 1 94  ? 2.724   6.094   43.886  1.00 14.76 ? 96  ARG B NE  1 
ATOM   2532 C CZ  . ARG B 1 94  ? 4.038   5.915   43.782  1.00 16.66 ? 96  ARG B CZ  1 
ATOM   2533 N NH1 . ARG B 1 94  ? 4.556   5.047   42.927  1.00 15.39 ? 96  ARG B NH1 1 
ATOM   2534 N NH2 . ARG B 1 94  ? 4.853   6.633   44.549  1.00 14.52 ? 96  ARG B NH2 1 
ATOM   2535 N N   . THR B 1 95  ? -2.677  3.176   41.811  1.00 17.59 ? 97  THR B N   1 
ATOM   2536 C CA  . THR B 1 95  ? -3.287  3.230   40.499  1.00 19.66 ? 97  THR B CA  1 
ATOM   2537 C C   . THR B 1 95  ? -2.861  4.535   39.847  1.00 18.92 ? 97  THR B C   1 
ATOM   2538 O O   . THR B 1 95  ? -2.842  5.579   40.500  1.00 17.85 ? 97  THR B O   1 
ATOM   2539 C CB  . THR B 1 95  ? -4.807  3.128   40.568  1.00 21.72 ? 97  THR B CB  1 
ATOM   2540 O OG1 . THR B 1 95  ? -5.152  1.967   41.317  1.00 23.37 ? 97  THR B OG1 1 
ATOM   2541 C CG2 . THR B 1 95  ? -5.354  2.951   39.182  1.00 21.99 ? 97  THR B CG2 1 
ATOM   2542 N N   . ILE B 1 96  ? -2.463  4.470   38.583  1.00 16.41 ? 98  ILE B N   1 
ATOM   2543 C CA  . ILE B 1 96  ? -1.948  5.642   37.868  1.00 16.90 ? 98  ILE B CA  1 
ATOM   2544 C C   . ILE B 1 96  ? -2.778  5.806   36.608  1.00 17.91 ? 98  ILE B C   1 
ATOM   2545 O O   . ILE B 1 96  ? -2.672  4.994   35.677  1.00 15.39 ? 98  ILE B O   1 
ATOM   2546 C CB  . ILE B 1 96  ? -0.454  5.524   37.515  1.00 16.24 ? 98  ILE B CB  1 
ATOM   2547 C CG1 . ILE B 1 96  ? 0.413   5.314   38.769  1.00 15.74 ? 98  ILE B CG1 1 
ATOM   2548 C CG2 . ILE B 1 96  ? 0.002   6.770   36.773  1.00 15.36 ? 98  ILE B CG2 1 
ATOM   2549 C CD1 . ILE B 1 96  ? 1.845   4.893   38.467  1.00 14.12 ? 98  ILE B CD1 1 
ATOM   2550 N N   . PHE B 1 97  ? -3.592  6.858   36.558  1.00 18.64 ? 99  PHE B N   1 
ATOM   2551 C CA  . PHE B 1 97  ? -4.485  7.085   35.422  1.00 19.00 ? 99  PHE B CA  1 
ATOM   2552 C C   . PHE B 1 97  ? -3.814  8.014   34.429  1.00 17.15 ? 99  PHE B C   1 
ATOM   2553 O O   . PHE B 1 97  ? -3.533  9.174   34.752  1.00 15.71 ? 99  PHE B O   1 
ATOM   2554 C CB  . PHE B 1 97  ? -5.810  7.695   35.890  1.00 17.29 ? 99  PHE B CB  1 
ATOM   2555 C CG  . PHE B 1 97  ? -6.588  6.806   36.796  1.00 20.27 ? 99  PHE B CG  1 
ATOM   2556 C CD1 . PHE B 1 97  ? -7.407  5.817   36.270  1.00 23.45 ? 99  PHE B CD1 1 
ATOM   2557 C CD2 . PHE B 1 97  ? -6.492  6.937   38.173  1.00 22.67 ? 99  PHE B CD2 1 
ATOM   2558 C CE1 . PHE B 1 97  ? -8.131  4.981   37.108  1.00 23.87 ? 99  PHE B CE1 1 
ATOM   2559 C CE2 . PHE B 1 97  ? -7.201  6.106   39.010  1.00 23.66 ? 99  PHE B CE2 1 
ATOM   2560 C CZ  . PHE B 1 97  ? -8.029  5.132   38.476  1.00 20.66 ? 99  PHE B CZ  1 
ATOM   2561 N N   . PHE B 1 98  ? -3.584  7.531   33.215  1.00 17.15 ? 100 PHE B N   1 
ATOM   2562 C CA  . PHE B 1 98  ? -3.023  8.383   32.177  1.00 15.30 ? 100 PHE B CA  1 
ATOM   2563 C C   . PHE B 1 98  ? -4.172  9.051   31.437  1.00 19.94 ? 100 PHE B C   1 
ATOM   2564 O O   . PHE B 1 98  ? -5.006  8.364   30.837  1.00 19.31 ? 100 PHE B O   1 
ATOM   2565 C CB  . PHE B 1 98  ? -2.137  7.574   31.240  1.00 19.84 ? 100 PHE B CB  1 
ATOM   2566 C CG  . PHE B 1 98  ? -0.864  7.149   31.888  1.00 17.43 ? 100 PHE B CG  1 
ATOM   2567 C CD1 . PHE B 1 98  ? 0.230   8.003   31.912  1.00 17.47 ? 100 PHE B CD1 1 
ATOM   2568 C CD2 . PHE B 1 98  ? -0.780  5.926   32.529  1.00 19.61 ? 100 PHE B CD2 1 
ATOM   2569 C CE1 . PHE B 1 98  ? 1.413   7.620   32.533  1.00 17.00 ? 100 PHE B CE1 1 
ATOM   2570 C CE2 . PHE B 1 98  ? 0.394   5.530   33.155  1.00 18.15 ? 100 PHE B CE2 1 
ATOM   2571 C CZ  . PHE B 1 98  ? 1.497   6.393   33.157  1.00 18.01 ? 100 PHE B CZ  1 
ATOM   2572 N N   . LYS B 1 99  ? -4.216  10.382  31.497  1.00 18.37 ? 101 LYS B N   1 
ATOM   2573 C CA  . LYS B 1 99  ? -5.349  11.127  30.958  1.00 19.40 ? 101 LYS B CA  1 
ATOM   2574 C C   . LYS B 1 99  ? -5.587  10.729  29.510  1.00 23.93 ? 101 LYS B C   1 
ATOM   2575 O O   . LYS B 1 99  ? -4.649  10.669  28.707  1.00 22.54 ? 101 LYS B O   1 
ATOM   2576 C CB  . LYS B 1 99  ? -5.081  12.627  31.058  1.00 20.83 ? 101 LYS B CB  1 
ATOM   2577 C CG  . LYS B 1 99  ? -6.160  13.532  30.456  1.00 26.00 ? 101 LYS B CG  1 
ATOM   2578 C CD  . LYS B 1 99  ? -6.273  14.801  31.272  1.00 27.05 ? 101 LYS B CD  1 
ATOM   2579 C CE  . LYS B 1 99  ? -7.439  15.666  30.844  1.00 32.42 ? 101 LYS B CE  1 
ATOM   2580 N NZ  . LYS B 1 99  ? -7.310  17.002  31.473  1.00 36.72 ? 101 LYS B NZ  1 
ATOM   2581 N N   . ASP B 1 100 ? -6.847  10.414  29.194  1.00 25.96 ? 102 ASP B N   1 
ATOM   2582 C CA  . ASP B 1 100 ? -7.264  10.043  27.841  1.00 25.53 ? 102 ASP B CA  1 
ATOM   2583 C C   . ASP B 1 100 ? -6.523  8.805   27.344  1.00 21.85 ? 102 ASP B C   1 
ATOM   2584 O O   . ASP B 1 100 ? -6.324  8.629   26.143  1.00 21.22 ? 102 ASP B O   1 
ATOM   2585 C CB  . ASP B 1 100 ? -7.073  11.215  26.874  1.00 25.58 ? 102 ASP B CB  1 
ATOM   2586 C CG  . ASP B 1 100 ? -7.910  12.415  27.257  1.00 28.13 ? 102 ASP B CG  1 
ATOM   2587 O OD1 . ASP B 1 100 ? -9.086  12.215  27.617  1.00 31.53 ? 102 ASP B OD1 1 
ATOM   2588 O OD2 . ASP B 1 100 ? -7.375  13.541  27.249  1.00 32.62 ? 102 ASP B OD2 1 
ATOM   2589 N N   . ASP B 1 101 ? -6.116  7.938   28.261  1.00 21.80 ? 103 ASP B N   1 
ATOM   2590 C CA  . ASP B 1 101 ? -5.384  6.721   27.920  1.00 20.81 ? 103 ASP B CA  1 
ATOM   2591 C C   . ASP B 1 101 ? -5.655  5.694   29.016  1.00 21.50 ? 103 ASP B C   1 
ATOM   2592 O O   . ASP B 1 101 ? -6.641  5.800   29.754  1.00 20.66 ? 103 ASP B O   1 
ATOM   2593 C CB  . ASP B 1 101 ? -3.885  7.021   27.722  1.00 21.26 ? 103 ASP B CB  1 
ATOM   2594 C CG  . ASP B 1 101 ? -3.243  6.137   26.644  1.00 22.54 ? 103 ASP B CG  1 
ATOM   2595 O OD1 . ASP B 1 101 ? -3.674  4.969   26.480  1.00 23.57 ? 103 ASP B OD1 1 
ATOM   2596 O OD2 . ASP B 1 101 ? -2.302  6.605   25.971  1.00 21.40 ? 103 ASP B OD2 1 
ATOM   2597 N N   . GLY B 1 102 ? -4.800  4.682   29.108  1.00 21.99 ? 104 GLY B N   1 
ATOM   2598 C CA  . GLY B 1 102 ? -4.997  3.594   30.042  1.00 22.70 ? 104 GLY B CA  1 
ATOM   2599 C C   . GLY B 1 102 ? -4.478  3.918   31.428  1.00 18.58 ? 104 GLY B C   1 
ATOM   2600 O O   . GLY B 1 102 ? -4.138  5.055   31.752  1.00 15.61 ? 104 GLY B O   1 
ATOM   2601 N N   . ASN B 1 103 ? -4.407  2.883   32.262  1.00 19.54 ? 105 ASN B N   1 
ATOM   2602 C CA  . ASN B 1 103 ? -3.930  3.068   33.622  1.00 18.86 ? 105 ASN B CA  1 
ATOM   2603 C C   . ASN B 1 103 ? -2.998  1.934   34.015  1.00 19.63 ? 105 ASN B C   1 
ATOM   2604 O O   . ASN B 1 103 ? -3.091  0.815   33.497  1.00 17.88 ? 105 ASN B O   1 
ATOM   2605 C CB  . ASN B 1 103 ? -5.102  3.191   34.602  1.00 19.39 ? 105 ASN B CB  1 
ATOM   2606 C CG  . ASN B 1 103 ? -5.938  1.920   34.698  1.00 24.07 ? 105 ASN B CG  1 
ATOM   2607 O OD1 . ASN B 1 103 ? -5.557  0.947   35.354  1.00 23.80 ? 105 ASN B OD1 1 
ATOM   2608 N ND2 . ASN B 1 103 ? -7.066  1.911   33.994  1.00 26.45 ? 105 ASN B ND2 1 
ATOM   2609 N N   . TYR B 1 104 ? -2.077  2.254   34.922  1.00 17.43 ? 106 TYR B N   1 
ATOM   2610 C CA  . TYR B 1 104 ? -1.230  1.276   35.602  1.00 18.07 ? 106 TYR B CA  1 
ATOM   2611 C C   . TYR B 1 104 ? -1.810  0.991   36.978  1.00 19.29 ? 106 TYR B C   1 
ATOM   2612 O O   . TYR B 1 104 ? -2.203  1.910   37.693  1.00 18.56 ? 106 TYR B O   1 
ATOM   2613 C CB  . TYR B 1 104 ? 0.197   1.803   35.828  1.00 16.59 ? 106 TYR B CB  1 
ATOM   2614 C CG  . TYR B 1 104 ? 1.086   2.045   34.616  1.00 17.05 ? 106 TYR B CG  1 
ATOM   2615 C CD1 . TYR B 1 104 ? 0.772   1.539   33.359  1.00 14.46 ? 106 TYR B CD1 1 
ATOM   2616 C CD2 . TYR B 1 104 ? 2.234   2.828   34.742  1.00 16.16 ? 106 TYR B CD2 1 
ATOM   2617 C CE1 . TYR B 1 104 ? 1.598   1.763   32.279  1.00 16.75 ? 106 TYR B CE1 1 
ATOM   2618 C CE2 . TYR B 1 104 ? 3.053   3.078   33.652  1.00 14.63 ? 106 TYR B CE2 1 
ATOM   2619 C CZ  . TYR B 1 104 ? 2.737   2.546   32.429  1.00 15.68 ? 106 TYR B CZ  1 
ATOM   2620 O OH  . TYR B 1 104 ? 3.556   2.796   31.351  1.00 15.50 ? 106 TYR B OH  1 
ATOM   2621 N N   . LYS B 1 105 ? -1.827  -0.275  37.366  1.00 20.53 ? 107 LYS B N   1 
ATOM   2622 C CA  . LYS B 1 105 ? -2.065  -0.662  38.745  1.00 15.72 ? 107 LYS B CA  1 
ATOM   2623 C C   . LYS B 1 105 ? -0.775  -1.313  39.216  1.00 20.55 ? 107 LYS B C   1 
ATOM   2624 O O   . LYS B 1 105 ? -0.243  -2.176  38.521  1.00 19.75 ? 107 LYS B O   1 
ATOM   2625 C CB  . LYS B 1 105 ? -3.235  -1.645  38.850  1.00 23.41 ? 107 LYS B CB  1 
ATOM   2626 C CG  . LYS B 1 105 ? -4.596  -0.969  38.920  1.00 26.94 ? 107 LYS B CG  1 
ATOM   2627 C CD  . LYS B 1 105 ? -5.736  -1.965  38.686  1.00 32.15 ? 107 LYS B CD  1 
ATOM   2628 C CE  . LYS B 1 105 ? -6.664  -1.516  37.523  1.00 35.40 ? 107 LYS B CE  1 
ATOM   2629 N NZ  . LYS B 1 105 ? -7.288  -0.163  37.672  1.00 31.28 ? 107 LYS B NZ  1 
ATOM   2630 N N   . THR B 1 106 ? -0.250  -0.894  40.365  1.00 19.62 ? 108 THR B N   1 
ATOM   2631 C CA  . THR B 1 106 ? 1.032   -1.427  40.809  1.00 16.21 ? 108 THR B CA  1 
ATOM   2632 C C   . THR B 1 106 ? 0.941   -1.889  42.252  1.00 18.57 ? 108 THR B C   1 
ATOM   2633 O O   . THR B 1 106 ? 0.240   -1.285  43.062  1.00 16.89 ? 108 THR B O   1 
ATOM   2634 C CB  . THR B 1 106 ? 2.188   -0.403  40.687  1.00 18.06 ? 108 THR B CB  1 
ATOM   2635 O OG1 . THR B 1 106 ? 1.976   0.695   41.595  1.00 16.23 ? 108 THR B OG1 1 
ATOM   2636 C CG2 . THR B 1 106 ? 2.315   0.117   39.251  1.00 18.52 ? 108 THR B CG2 1 
ATOM   2637 N N   . ARG B 1 107 ? 1.647   -2.974  42.556  1.00 17.54 ? 109 ARG B N   1 
ATOM   2638 C CA  . ARG B 1 107 ? 1.801   -3.460  43.917  1.00 19.26 ? 109 ARG B CA  1 
ATOM   2639 C C   . ARG B 1 107 ? 3.269   -3.757  44.146  1.00 17.73 ? 109 ARG B C   1 
ATOM   2640 O O   . ARG B 1 107 ? 3.885   -4.478  43.355  1.00 18.54 ? 109 ARG B O   1 
ATOM   2641 C CB  . ARG B 1 107 ? 0.990   -4.729  44.176  1.00 17.90 ? 109 ARG B CB  1 
ATOM   2642 C CG  . ARG B 1 107 ? 0.853   -5.038  45.648  1.00 22.16 ? 109 ARG B CG  1 
ATOM   2643 C CD  . ARG B 1 107 ? -0.027  -6.268  45.834  1.00 22.77 ? 109 ARG B CD  1 
ATOM   2644 N NE  . ARG B 1 107 ? -0.170  -6.652  47.227  1.00 21.18 ? 109 ARG B NE  1 
ATOM   2645 C CZ  . ARG B 1 107 ? 0.723   -7.346  47.914  1.00 26.90 ? 109 ARG B CZ  1 
ATOM   2646 N NH1 . ARG B 1 107 ? 1.819   -7.817  47.344  1.00 24.50 ? 109 ARG B NH1 1 
ATOM   2647 N NH2 . ARG B 1 107 ? 0.509   -7.569  49.209  1.00 29.69 ? 109 ARG B NH2 1 
ATOM   2648 N N   . ALA B 1 108 ? 3.817   -3.268  45.258  1.00 17.85 ? 110 ALA B N   1 
ATOM   2649 C CA  . ALA B 1 108 ? 5.230   -3.464  45.515  1.00 18.61 ? 110 ALA B CA  1 
ATOM   2650 C C   . ALA B 1 108 ? 5.457   -3.747  46.991  1.00 20.00 ? 110 ALA B C   1 
ATOM   2651 O O   . ALA B 1 108 ? 4.721   -3.256  47.852  1.00 16.74 ? 110 ALA B O   1 
ATOM   2652 C CB  . ALA B 1 108 ? 6.042   -2.234  45.075  1.00 15.81 ? 110 ALA B CB  1 
ATOM   2653 N N   . GLU B 1 109 ? 6.476   -4.556  47.274  1.00 17.41 ? 111 GLU B N   1 
ATOM   2654 C CA  . GLU B 1 109 ? 7.015   -4.689  48.624  1.00 20.64 ? 111 GLU B CA  1 
ATOM   2655 C C   . GLU B 1 109 ? 8.393   -4.044  48.702  1.00 19.71 ? 111 GLU B C   1 
ATOM   2656 O O   . GLU B 1 109 ? 9.281   -4.357  47.899  1.00 21.05 ? 111 GLU B O   1 
ATOM   2657 C CB  . GLU B 1 109 ? 7.088   -6.156  49.065  1.00 24.40 ? 111 GLU B CB  1 
ATOM   2658 C CG  . GLU B 1 109 ? 5.941   -7.008  48.584  1.00 28.86 ? 111 GLU B CG  1 
ATOM   2659 C CD  . GLU B 1 109 ? 5.679   -8.187  49.495  1.00 32.67 ? 111 GLU B CD  1 
ATOM   2660 O OE1 . GLU B 1 109 ? 6.646   -8.713  50.063  1.00 31.82 ? 111 GLU B OE1 1 
ATOM   2661 O OE2 . GLU B 1 109 ? 4.496   -8.568  49.653  1.00 44.88 ? 111 GLU B OE2 1 
ATOM   2662 N N   . VAL B 1 110 ? 8.564   -3.145  49.666  1.00 18.41 ? 112 VAL B N   1 
ATOM   2663 C CA  . VAL B 1 110 ? 9.819   -2.455  49.910  1.00 19.55 ? 112 VAL B CA  1 
ATOM   2664 C C   . VAL B 1 110 ? 10.303  -2.900  51.281  1.00 20.57 ? 112 VAL B C   1 
ATOM   2665 O O   . VAL B 1 110 ? 9.619   -2.681  52.285  1.00 20.13 ? 112 VAL B O   1 
ATOM   2666 C CB  . VAL B 1 110 ? 9.661   -0.931  49.861  1.00 19.58 ? 112 VAL B CB  1 
ATOM   2667 C CG1 . VAL B 1 110 ? 11.017  -0.254  50.007  1.00 19.10 ? 112 VAL B CG1 1 
ATOM   2668 C CG2 . VAL B 1 110 ? 8.961   -0.491  48.557  1.00 17.30 ? 112 VAL B CG2 1 
ATOM   2669 N N   . LYS B 1 111 ? 11.469  -3.523  51.321  1.00 20.78 ? 113 LYS B N   1 
ATOM   2670 C CA  . LYS B 1 111 ? 11.937  -4.127  52.565  1.00 22.20 ? 113 LYS B CA  1 
ATOM   2671 C C   . LYS B 1 111 ? 13.407  -4.446  52.405  1.00 20.91 ? 113 LYS B C   1 
ATOM   2672 O O   . LYS B 1 111 ? 13.917  -4.530  51.292  1.00 21.75 ? 113 LYS B O   1 
ATOM   2673 C CB  . LYS B 1 111 ? 11.179  -5.417  52.899  1.00 21.20 ? 113 LYS B CB  1 
ATOM   2674 C CG  . LYS B 1 111 ? 11.244  -6.492  51.811  1.00 24.08 ? 113 LYS B CG  1 
ATOM   2675 C CD  . LYS B 1 111 ? 10.370  -7.675  52.207  1.00 30.91 ? 113 LYS B CD  1 
ATOM   2676 C CE  . LYS B 1 111 ? 10.546  -8.866  51.273  1.00 37.67 ? 113 LYS B CE  1 
ATOM   2677 N NZ  . LYS B 1 111 ? 10.914  -8.451  49.906  1.00 40.16 ? 113 LYS B NZ  1 
ATOM   2678 N N   . PHE B 1 112 ? 14.077  -4.668  53.536  1.00 20.07 ? 114 PHE B N   1 
ATOM   2679 C CA  . PHE B 1 112 ? 15.468  -5.089  53.505  1.00 22.17 ? 114 PHE B CA  1 
ATOM   2680 C C   . PHE B 1 112 ? 15.548  -6.593  53.267  1.00 23.92 ? 114 PHE B C   1 
ATOM   2681 O O   . PHE B 1 112 ? 14.762  -7.373  53.823  1.00 21.97 ? 114 PHE B O   1 
ATOM   2682 C CB  . PHE B 1 112 ? 16.161  -4.717  54.817  1.00 21.78 ? 114 PHE B CB  1 
ATOM   2683 C CG  . PHE B 1 112 ? 16.735  -3.321  54.820  1.00 21.02 ? 114 PHE B CG  1 
ATOM   2684 C CD1 . PHE B 1 112 ? 18.020  -3.075  54.353  1.00 21.23 ? 114 PHE B CD1 1 
ATOM   2685 C CD2 . PHE B 1 112 ? 15.955  -2.240  55.226  1.00 21.82 ? 114 PHE B CD2 1 
ATOM   2686 C CE1 . PHE B 1 112 ? 18.553  -1.786  54.347  1.00 23.41 ? 114 PHE B CE1 1 
ATOM   2687 C CE2 . PHE B 1 112 ? 16.469  -0.949  55.217  1.00 22.38 ? 114 PHE B CE2 1 
ATOM   2688 C CZ  . PHE B 1 112 ? 17.766  -0.715  54.772  1.00 24.39 ? 114 PHE B CZ  1 
ATOM   2689 N N   . GLU B 1 113 ? 16.459  -6.982  52.378  1.00 21.97 ? 115 GLU B N   1 
ATOM   2690 C CA  . GLU B 1 113 ? 16.914  -8.357  52.192  1.00 22.69 ? 115 GLU B CA  1 
ATOM   2691 C C   . GLU B 1 113 ? 18.392  -8.316  52.535  1.00 22.31 ? 115 GLU B C   1 
ATOM   2692 O O   . GLU B 1 113 ? 19.212  -7.912  51.707  1.00 19.45 ? 115 GLU B O   1 
ATOM   2693 C CB  . GLU B 1 113 ? 16.687  -8.850  50.766  1.00 25.43 ? 115 GLU B CB  1 
ATOM   2694 C CG  . GLU B 1 113 ? 15.263  -9.297  50.506  1.00 27.77 ? 115 GLU B CG  1 
ATOM   2695 C CD  . GLU B 1 113 ? 14.967  -9.467  49.023  1.00 35.01 ? 115 GLU B CD  1 
ATOM   2696 O OE1 . GLU B 1 113 ? 15.925  -9.593  48.226  1.00 34.45 ? 115 GLU B OE1 1 
ATOM   2697 O OE2 . GLU B 1 113 ? 13.772  -9.480  48.656  1.00 39.12 ? 115 GLU B OE2 1 
ATOM   2698 N N   . GLY B 1 114 ? 18.732  -8.697  53.762  1.00 27.59 ? 116 GLY B N   1 
ATOM   2699 C CA  . GLY B 1 114 ? 20.086  -8.444  54.230  1.00 23.20 ? 116 GLY B CA  1 
ATOM   2700 C C   . GLY B 1 114 ? 20.343  -6.955  54.306  1.00 25.84 ? 116 GLY B C   1 
ATOM   2701 O O   . GLY B 1 114 ? 19.516  -6.182  54.799  1.00 24.21 ? 116 GLY B O   1 
ATOM   2702 N N   . ASP B 1 115 ? 21.493  -6.538  53.802  1.00 23.58 ? 117 ASP B N   1 
ATOM   2703 C CA  . ASP B 1 115 ? 21.848  -5.125  53.779  1.00 24.27 ? 117 ASP B CA  1 
ATOM   2704 C C   . ASP B 1 115 ? 21.258  -4.366  52.597  1.00 22.25 ? 117 ASP B C   1 
ATOM   2705 O O   . ASP B 1 115 ? 21.545  -3.174  52.451  1.00 23.34 ? 117 ASP B O   1 
ATOM   2706 C CB  . ASP B 1 115 ? 23.363  -4.980  53.742  1.00 27.45 ? 117 ASP B CB  1 
ATOM   2707 C CG  . ASP B 1 115 ? 23.991  -5.144  55.103  1.00 33.08 ? 117 ASP B CG  1 
ATOM   2708 O OD1 . ASP B 1 115 ? 23.249  -5.222  56.116  1.00 34.04 ? 117 ASP B OD1 1 
ATOM   2709 O OD2 . ASP B 1 115 ? 25.233  -5.231  55.140  1.00 39.58 ? 117 ASP B OD2 1 
ATOM   2710 N N   . THR B 1 116 ? 20.481  -5.016  51.739  1.00 21.50 ? 118 THR B N   1 
ATOM   2711 C CA  . THR B 1 116 ? 19.990  -4.391  50.512  1.00 20.77 ? 118 THR B CA  1 
ATOM   2712 C C   . THR B 1 116 ? 18.536  -3.974  50.689  1.00 20.20 ? 118 THR B C   1 
ATOM   2713 O O   . THR B 1 116 ? 17.714  -4.770  51.145  1.00 20.88 ? 118 THR B O   1 
ATOM   2714 C CB  . THR B 1 116 ? 20.101  -5.344  49.318  1.00 23.41 ? 118 THR B CB  1 
ATOM   2715 O OG1 . THR B 1 116 ? 21.476  -5.657  49.068  1.00 23.51 ? 118 THR B OG1 1 
ATOM   2716 C CG2 . THR B 1 116 ? 19.554  -4.687  48.068  1.00 18.65 ? 118 THR B CG2 1 
ATOM   2717 N N   . LEU B 1 117 ? 18.213  -2.733  50.316  1.00 20.85 ? 119 LEU B N   1 
ATOM   2718 C CA  . LEU B 1 117 ? 16.815  -2.314  50.230  1.00 20.51 ? 119 LEU B CA  1 
ATOM   2719 C C   . LEU B 1 117 ? 16.274  -2.766  48.881  1.00 20.72 ? 119 LEU B C   1 
ATOM   2720 O O   . LEU B 1 117 ? 16.819  -2.381  47.847  1.00 21.92 ? 119 LEU B O   1 
ATOM   2721 C CB  . LEU B 1 117 ? 16.702  -0.795  50.393  1.00 20.81 ? 119 LEU B CB  1 
ATOM   2722 C CG  . LEU B 1 117 ? 15.359  -0.076  50.632  1.00 18.55 ? 119 LEU B CG  1 
ATOM   2723 C CD1 . LEU B 1 117 ? 14.620  0.088   49.313  1.00 18.23 ? 119 LEU B CD1 1 
ATOM   2724 C CD2 . LEU B 1 117 ? 14.459  -0.819  51.641  1.00 19.32 ? 119 LEU B CD2 1 
ATOM   2725 N N   . VAL B 1 118 ? 15.227  -3.595  48.895  1.00 18.86 ? 120 VAL B N   1 
ATOM   2726 C CA  . VAL B 1 118 ? 14.646  -4.183  47.694  1.00 19.30 ? 120 VAL B CA  1 
ATOM   2727 C C   . VAL B 1 118 ? 13.249  -3.616  47.478  1.00 21.05 ? 120 VAL B C   1 
ATOM   2728 O O   . VAL B 1 118 ? 12.453  -3.528  48.420  1.00 19.65 ? 120 VAL B O   1 
ATOM   2729 C CB  . VAL B 1 118 ? 14.608  -5.720  47.814  1.00 23.47 ? 120 VAL B CB  1 
ATOM   2730 C CG1 . VAL B 1 118 ? 14.133  -6.362  46.537  1.00 24.96 ? 120 VAL B CG1 1 
ATOM   2731 C CG2 . VAL B 1 118 ? 16.016  -6.235  48.156  1.00 23.25 ? 120 VAL B CG2 1 
ATOM   2732 N N   . ASN B 1 119 ? 12.954  -3.251  46.229  1.00 19.59 ? 121 ASN B N   1 
ATOM   2733 C CA  . ASN B 1 119 ? 11.629  -2.820  45.786  1.00 16.66 ? 121 ASN B CA  1 
ATOM   2734 C C   . ASN B 1 119 ? 11.178  -3.835  44.732  1.00 15.20 ? 121 ASN B C   1 
ATOM   2735 O O   . ASN B 1 119 ? 11.647  -3.791  43.596  1.00 15.31 ? 121 ASN B O   1 
ATOM   2736 C CB  . ASN B 1 119 ? 11.691  -1.380  45.226  1.00 17.89 ? 121 ASN B CB  1 
ATOM   2737 C CG  . ASN B 1 119 ? 10.329  -0.849  44.779  1.00 17.21 ? 121 ASN B CG  1 
ATOM   2738 O OD1 . ASN B 1 119 ? 9.290   -1.366  45.196  1.00 19.57 ? 121 ASN B OD1 1 
ATOM   2739 N ND2 . ASN B 1 119 ? 10.327  0.225   43.964  1.00 12.46 ? 121 ASN B ND2 1 
ATOM   2740 N N   . ARG B 1 120 ? 10.265  -4.741  45.089  1.00 16.35 ? 122 ARG B N   1 
ATOM   2741 C CA  . ARG B 1 120 ? 9.778   -5.768  44.167  1.00 18.70 ? 122 ARG B CA  1 
ATOM   2742 C C   . ARG B 1 120 ? 8.347   -5.461  43.727  1.00 18.87 ? 122 ARG B C   1 
ATOM   2743 O O   . ARG B 1 120 ? 7.440   -5.413  44.564  1.00 17.91 ? 122 ARG B O   1 
ATOM   2744 C CB  . ARG B 1 120 ? 9.854   -7.138  44.837  1.00 19.18 ? 122 ARG B CB  1 
ATOM   2745 C CG  . ARG B 1 120 ? 11.288  -7.609  44.941  1.00 25.20 ? 122 ARG B CG  1 
ATOM   2746 C CD  . ARG B 1 120 ? 11.393  -9.050  45.405  1.00 31.34 ? 122 ARG B CD  1 
ATOM   2747 N NE  . ARG B 1 120 ? 12.754  -9.369  45.825  1.00 34.76 ? 122 ARG B NE  1 
ATOM   2748 C CZ  . ARG B 1 120 ? 13.788  -9.507  44.999  1.00 36.16 ? 122 ARG B CZ  1 
ATOM   2749 N NH1 . ARG B 1 120 ? 13.651  -9.386  43.685  1.00 33.77 ? 122 ARG B NH1 1 
ATOM   2750 N NH2 . ARG B 1 120 ? 14.987  -9.792  45.503  1.00 37.38 ? 122 ARG B NH2 1 
ATOM   2751 N N   . ILE B 1 121 ? 8.133   -5.308  42.411  1.00 15.95 ? 123 ILE B N   1 
ATOM   2752 C CA  . ILE B 1 121 ? 6.923   -4.685  41.875  1.00 16.19 ? 123 ILE B CA  1 
ATOM   2753 C C   . ILE B 1 121 ? 6.222   -5.612  40.895  1.00 18.83 ? 123 ILE B C   1 
ATOM   2754 O O   . ILE B 1 121 ? 6.872   -6.197  40.027  1.00 16.42 ? 123 ILE B O   1 
ATOM   2755 C CB  . ILE B 1 121 ? 7.240   -3.367  41.137  1.00 16.15 ? 123 ILE B CB  1 
ATOM   2756 C CG1 . ILE B 1 121 ? 8.162   -2.471  41.962  1.00 13.87 ? 123 ILE B CG1 1 
ATOM   2757 C CG2 . ILE B 1 121 ? 5.960   -2.610  40.802  1.00 18.81 ? 123 ILE B CG2 1 
ATOM   2758 C CD1 . ILE B 1 121 ? 9.146   -1.739  41.090  1.00 15.56 ? 123 ILE B CD1 1 
ATOM   2759 N N   . GLU B 1 122 ? 4.885   -5.680  40.987  1.00 18.54 ? 124 GLU B N   1 
ATOM   2760 C CA  . GLU B 1 122 ? 4.022   -6.130  39.898  1.00 17.90 ? 124 GLU B CA  1 
ATOM   2761 C C   . GLU B 1 122 ? 3.318   -4.925  39.287  1.00 17.02 ? 124 GLU B C   1 
ATOM   2762 O O   . GLU B 1 122 ? 2.746   -4.112  40.010  1.00 19.13 ? 124 GLU B O   1 
ATOM   2763 C CB  . GLU B 1 122 ? 2.957   -7.103  40.401  1.00 21.61 ? 124 GLU B CB  1 
ATOM   2764 C CG  . GLU B 1 122 ? 3.474   -8.355  41.025  1.00 29.60 ? 124 GLU B CG  1 
ATOM   2765 C CD  . GLU B 1 122 ? 2.418   -8.956  41.926  1.00 31.43 ? 124 GLU B CD  1 
ATOM   2766 O OE1 . GLU B 1 122 ? 1.248   -8.974  41.507  1.00 36.26 ? 124 GLU B OE1 1 
ATOM   2767 O OE2 . GLU B 1 122 ? 2.742   -9.354  43.058  1.00 38.10 ? 124 GLU B OE2 1 
ATOM   2768 N N   . LEU B 1 123 ? 3.300   -4.839  37.966  1.00 17.42 ? 125 LEU B N   1 
ATOM   2769 C CA  . LEU B 1 123 ? 2.637   -3.746  37.270  1.00 18.49 ? 125 LEU B CA  1 
ATOM   2770 C C   . LEU B 1 123 ? 1.738   -4.323  36.189  1.00 19.47 ? 125 LEU B C   1 
ATOM   2771 O O   . LEU B 1 123 ? 2.167   -5.182  35.415  1.00 20.37 ? 125 LEU B O   1 
ATOM   2772 C CB  . LEU B 1 123 ? 3.652   -2.779  36.648  1.00 19.12 ? 125 LEU B CB  1 
ATOM   2773 C CG  . LEU B 1 123 ? 3.083   -1.579  35.878  1.00 16.83 ? 125 LEU B CG  1 
ATOM   2774 C CD1 . LEU B 1 123 ? 4.089   -0.450  35.920  1.00 15.82 ? 125 LEU B CD1 1 
ATOM   2775 C CD2 . LEU B 1 123 ? 2.745   -1.875  34.421  1.00 16.49 ? 125 LEU B CD2 1 
ATOM   2776 N N   . LYS B 1 124 ? 0.495   -3.854  36.152  1.00 21.43 ? 126 LYS B N   1 
ATOM   2777 C CA  . LYS B 1 124 ? -0.478  -4.300  35.163  1.00 21.98 ? 126 LYS B CA  1 
ATOM   2778 C C   . LYS B 1 124 ? -1.197  -3.098  34.560  1.00 19.58 ? 126 LYS B C   1 
ATOM   2779 O O   . LYS B 1 124 ? -1.879  -2.353  35.263  1.00 16.87 ? 126 LYS B O   1 
ATOM   2780 C CB  . LYS B 1 124 ? -1.489  -5.257  35.795  1.00 26.18 ? 126 LYS B CB  1 
ATOM   2781 C CG  . LYS B 1 124 ? -2.404  -4.607  36.819  1.00 26.09 ? 126 LYS B CG  1 
ATOM   2782 C CD  . LYS B 1 124 ? -3.356  -5.621  37.432  1.00 31.59 ? 126 LYS B CD  1 
ATOM   2783 C CE  . LYS B 1 124 ? -4.182  -5.000  38.547  1.00 36.81 ? 126 LYS B CE  1 
ATOM   2784 N NZ  . LYS B 1 124 ? -4.107  -5.796  39.803  1.00 30.26 ? 126 LYS B NZ  1 
ATOM   2785 N N   . GLY B 1 125 ? -1.034  -2.914  33.255  1.00 17.86 ? 127 GLY B N   1 
ATOM   2786 C CA  . GLY B 1 125 ? -1.610  -1.771  32.560  1.00 19.70 ? 127 GLY B CA  1 
ATOM   2787 C C   . GLY B 1 125 ? -2.697  -2.259  31.625  1.00 22.44 ? 127 GLY B C   1 
ATOM   2788 O O   . GLY B 1 125 ? -2.543  -3.297  30.985  1.00 18.75 ? 127 GLY B O   1 
ATOM   2789 N N   . ILE B 1 126 ? -3.813  -1.528  31.581  1.00 19.11 ? 128 ILE B N   1 
ATOM   2790 C CA  . ILE B 1 126 ? -4.941  -1.906  30.740  1.00 24.04 ? 128 ILE B CA  1 
ATOM   2791 C C   . ILE B 1 126 ? -5.497  -0.662  30.073  1.00 23.94 ? 128 ILE B C   1 
ATOM   2792 O O   . ILE B 1 126 ? -5.288  0.460   30.535  1.00 23.32 ? 128 ILE B O   1 
ATOM   2793 C CB  . ILE B 1 126 ? -6.073  -2.607  31.531  1.00 22.50 ? 128 ILE B CB  1 
ATOM   2794 C CG1 . ILE B 1 126 ? -6.616  -1.672  32.611  1.00 25.53 ? 128 ILE B CG1 1 
ATOM   2795 C CG2 . ILE B 1 126 ? -5.562  -3.866  32.199  1.00 26.90 ? 128 ILE B CG2 1 
ATOM   2796 C CD1 . ILE B 1 126 ? -7.981  -2.062  33.119  1.00 26.79 ? 128 ILE B CD1 1 
ATOM   2797 N N   . ASP B 1 127 ? -6.229  -0.889  28.975  1.00 22.74 ? 129 ASP B N   1 
ATOM   2798 C CA  . ASP B 1 127 ? -6.963  0.147   28.240  1.00 24.10 ? 129 ASP B CA  1 
ATOM   2799 C C   . ASP B 1 127 ? -6.067  1.215   27.631  1.00 23.26 ? 129 ASP B C   1 
ATOM   2800 O O   . ASP B 1 127 ? -6.496  2.354   27.451  1.00 23.97 ? 129 ASP B O   1 
ATOM   2801 C CB  . ASP B 1 127 ? -8.044  0.815   29.100  1.00 26.97 ? 129 ASP B CB  1 
ATOM   2802 C CG  . ASP B 1 127 ? -9.062  -0.174  29.619  1.00 27.98 ? 129 ASP B CG  1 
ATOM   2803 O OD1 . ASP B 1 127 ? -9.496  -1.012  28.809  1.00 32.83 ? 129 ASP B OD1 1 
ATOM   2804 O OD2 . ASP B 1 127 ? -9.506  -0.043  30.774  1.00 27.96 ? 129 ASP B OD2 1 
ATOM   2805 N N   . PHE B 1 128 ? -4.849  0.867   27.250  1.00 19.08 ? 130 PHE B N   1 
ATOM   2806 C CA  . PHE B 1 128 ? -4.011  1.831   26.557  1.00 22.17 ? 130 PHE B CA  1 
ATOM   2807 C C   . PHE B 1 128 ? -4.305  1.831   25.067  1.00 21.93 ? 130 PHE B C   1 
ATOM   2808 O O   . PHE B 1 128 ? -4.641  0.805   24.474  1.00 27.77 ? 130 PHE B O   1 
ATOM   2809 C CB  . PHE B 1 128 ? -2.527  1.545   26.792  1.00 19.49 ? 130 PHE B CB  1 
ATOM   2810 C CG  . PHE B 1 128 ? -2.067  1.983   28.147  1.00 17.56 ? 130 PHE B CG  1 
ATOM   2811 C CD1 . PHE B 1 128 ? -1.585  3.262   28.356  1.00 18.93 ? 130 PHE B CD1 1 
ATOM   2812 C CD2 . PHE B 1 128 ? -2.198  1.131   29.229  1.00 19.02 ? 130 PHE B CD2 1 
ATOM   2813 C CE1 . PHE B 1 128 ? -1.212  3.678   29.628  1.00 15.82 ? 130 PHE B CE1 1 
ATOM   2814 C CE2 . PHE B 1 128 ? -1.824  1.539   30.488  1.00 19.39 ? 130 PHE B CE2 1 
ATOM   2815 C CZ  . PHE B 1 128 ? -1.326  2.815   30.682  1.00 16.06 ? 130 PHE B CZ  1 
ATOM   2816 N N   . LYS B 1 129 ? -4.171  3.005   24.465  1.00 24.10 ? 131 LYS B N   1 
ATOM   2817 C CA  . LYS B 1 129 ? -4.270  3.123   23.022  1.00 23.76 ? 131 LYS B CA  1 
ATOM   2818 C C   . LYS B 1 129 ? -2.942  2.726   22.390  1.00 28.24 ? 131 LYS B C   1 
ATOM   2819 O O   . LYS B 1 129 ? -1.887  3.253   22.752  1.00 23.97 ? 131 LYS B O   1 
ATOM   2820 C CB  . LYS B 1 129 ? -4.672  4.545   22.628  1.00 26.38 ? 131 LYS B CB  1 
ATOM   2821 C CG  . LYS B 1 129 ? -5.989  5.007   23.268  1.00 28.32 ? 131 LYS B CG  1 
ATOM   2822 C CD  . LYS B 1 129 ? -6.215  6.523   23.148  1.00 26.20 ? 131 LYS B CD  1 
ATOM   2823 C CE  . LYS B 1 129 ? -7.602  6.942   23.676  1.00 28.99 ? 131 LYS B CE  1 
ATOM   2824 N N   . GLU B 1 130 ? -2.996  1.802   21.433  1.00 28.24 ? 132 GLU B N   1 
ATOM   2825 C CA  . GLU B 1 130 ? -1.768  1.332   20.812  1.00 29.08 ? 132 GLU B CA  1 
ATOM   2826 C C   . GLU B 1 130 ? -1.037  2.457   20.095  1.00 30.49 ? 132 GLU B C   1 
ATOM   2827 O O   . GLU B 1 130 ? 0.176   2.358   19.896  1.00 31.88 ? 132 GLU B O   1 
ATOM   2828 C CB  . GLU B 1 130 ? -2.072  0.194   19.834  1.00 29.81 ? 132 GLU B CB  1 
ATOM   2829 C CG  . GLU B 1 130 ? -2.278  -1.135  20.526  1.00 29.44 ? 132 GLU B CG  1 
ATOM   2830 C CD  . GLU B 1 130 ? -0.996  -1.809  20.992  1.00 36.69 ? 132 GLU B CD  1 
ATOM   2831 O OE1 . GLU B 1 130 ? 0.131   -1.353  20.660  1.00 38.98 ? 132 GLU B OE1 1 
ATOM   2832 O OE2 . GLU B 1 130 ? -1.136  -2.778  21.753  1.00 34.28 ? 132 GLU B OE2 1 
ATOM   2833 N N   . ASP B 1 131 ? -1.735  3.539   19.728  1.00 27.89 ? 133 ASP B N   1 
ATOM   2834 C CA  . ASP B 1 131 ? -1.098  4.693   19.098  1.00 32.41 ? 133 ASP B CA  1 
ATOM   2835 C C   . ASP B 1 131 ? -1.154  5.942   19.970  1.00 28.98 ? 133 ASP B C   1 
ATOM   2836 O O   . ASP B 1 131 ? -1.093  7.060   19.448  1.00 31.99 ? 133 ASP B O   1 
ATOM   2837 C CB  . ASP B 1 131 ? -1.736  5.003   17.742  1.00 34.85 ? 133 ASP B CB  1 
ATOM   2838 C CG  . ASP B 1 131 ? -3.230  4.744   17.723  1.00 41.64 ? 133 ASP B CG  1 
ATOM   2839 O OD1 . ASP B 1 131 ? -3.850  4.715   18.812  1.00 39.24 ? 133 ASP B OD1 1 
ATOM   2840 O OD2 . ASP B 1 131 ? -3.796  4.586   16.612  1.00 50.33 ? 133 ASP B OD2 1 
ATOM   2841 N N   . GLY B 1 132 ? -1.288  5.782   21.284  1.00 26.05 ? 134 GLY B N   1 
ATOM   2842 C CA  . GLY B 1 132 ? -1.270  6.899   22.201  1.00 25.14 ? 134 GLY B CA  1 
ATOM   2843 C C   . GLY B 1 132 ? 0.144   7.268   22.603  1.00 22.08 ? 134 GLY B C   1 
ATOM   2844 O O   . GLY B 1 132 ? 1.133   6.783   22.053  1.00 23.47 ? 134 GLY B O   1 
ATOM   2845 N N   . ASN B 1 133 ? 0.236   8.146   23.598  1.00 19.57 ? 135 ASN B N   1 
ATOM   2846 C CA  . ASN B 1 133 ? 1.546   8.653   23.958  1.00 21.53 ? 135 ASN B CA  1 
ATOM   2847 C C   . ASN B 1 133 ? 2.396   7.607   24.661  1.00 20.06 ? 135 ASN B C   1 
ATOM   2848 O O   . ASN B 1 133 ? 3.626   7.735   24.675  1.00 18.15 ? 135 ASN B O   1 
ATOM   2849 C CB  . ASN B 1 133 ? 1.382   9.893   24.832  1.00 20.12 ? 135 ASN B CB  1 
ATOM   2850 C CG  . ASN B 1 133 ? 0.827   11.047  24.049  1.00 25.09 ? 135 ASN B CG  1 
ATOM   2851 O OD1 . ASN B 1 133 ? 1.080   11.150  22.846  1.00 20.00 ? 135 ASN B OD1 1 
ATOM   2852 N ND2 . ASN B 1 133 ? 0.039   11.898  24.701  1.00 22.74 ? 135 ASN B ND2 1 
ATOM   2853 N N   . ILE B 1 134 ? 1.776   6.577   25.228  1.00 17.33 ? 136 ILE B N   1 
ATOM   2854 C CA  . ILE B 1 134 ? 2.526   5.625   26.041  1.00 18.44 ? 136 ILE B CA  1 
ATOM   2855 C C   . ILE B 1 134 ? 2.948   4.451   25.155  1.00 20.41 ? 136 ILE B C   1 
ATOM   2856 O O   . ILE B 1 134 ? 4.139   4.190   24.951  1.00 18.48 ? 136 ILE B O   1 
ATOM   2857 C CB  . ILE B 1 134 ? 1.691   5.146   27.249  1.00 20.00 ? 136 ILE B CB  1 
ATOM   2858 C CG1 . ILE B 1 134 ? 1.573   6.223   28.342  1.00 20.45 ? 136 ILE B CG1 1 
ATOM   2859 C CG2 . ILE B 1 134 ? 2.302   3.899   27.863  1.00 16.57 ? 136 ILE B CG2 1 
ATOM   2860 C CD1 . ILE B 1 134 ? 0.519   7.296   28.100  1.00 19.44 ? 136 ILE B CD1 1 
ATOM   2861 N N   . LEU B 1 135 ? 1.973   3.732   24.610  1.00 18.13 ? 137 LEU B N   1 
ATOM   2862 C CA  . LEU B 1 135 ? 2.297   2.596   23.755  1.00 22.44 ? 137 LEU B CA  1 
ATOM   2863 C C   . LEU B 1 135 ? 2.947   3.052   22.449  1.00 21.48 ? 137 LEU B C   1 
ATOM   2864 O O   . LEU B 1 135 ? 3.694   2.285   21.828  1.00 23.34 ? 137 LEU B O   1 
ATOM   2865 C CB  . LEU B 1 135 ? 1.010   1.814   23.503  1.00 23.72 ? 137 LEU B CB  1 
ATOM   2866 C CG  . LEU B 1 135 ? 0.571   0.869   24.633  1.00 22.01 ? 137 LEU B CG  1 
ATOM   2867 C CD1 . LEU B 1 135 ? -0.437  -0.149  24.165  1.00 22.74 ? 137 LEU B CD1 1 
ATOM   2868 C CD2 . LEU B 1 135 ? 1.755   0.122   25.250  1.00 23.26 ? 137 LEU B CD2 1 
ATOM   2869 N N   . GLY B 1 136 ? 2.690   4.288   22.028  1.00 20.19 ? 138 GLY B N   1 
ATOM   2870 C CA  . GLY B 1 136 ? 3.281   4.860   20.839  1.00 21.32 ? 138 GLY B CA  1 
ATOM   2871 C C   . GLY B 1 136 ? 4.561   5.622   21.069  1.00 23.84 ? 138 GLY B C   1 
ATOM   2872 O O   . GLY B 1 136 ? 5.069   6.248   20.129  1.00 24.61 ? 138 GLY B O   1 
ATOM   2873 N N   . HIS B 1 137 ? 5.089   5.616   22.292  1.00 19.96 ? 139 HIS B N   1 
ATOM   2874 C CA  . HIS B 1 137 ? 6.402   6.185   22.595  1.00 20.88 ? 139 HIS B CA  1 
ATOM   2875 C C   . HIS B 1 137 ? 6.510   7.631   22.132  1.00 21.91 ? 139 HIS B C   1 
ATOM   2876 O O   . HIS B 1 137 ? 7.383   7.986   21.343  1.00 21.61 ? 139 HIS B O   1 
ATOM   2877 C CB  . HIS B 1 137 ? 7.521   5.349   21.960  1.00 24.12 ? 139 HIS B CB  1 
ATOM   2878 C CG  . HIS B 1 137 ? 7.680   3.998   22.570  1.00 25.43 ? 139 HIS B CG  1 
ATOM   2879 N ND1 . HIS B 1 137 ? 8.385   3.782   23.736  1.00 22.12 ? 139 HIS B ND1 1 
ATOM   2880 C CD2 . HIS B 1 137 ? 7.214   2.789   22.179  1.00 24.55 ? 139 HIS B CD2 1 
ATOM   2881 C CE1 . HIS B 1 137 ? 8.342   2.496   24.036  1.00 24.75 ? 139 HIS B CE1 1 
ATOM   2882 N NE2 . HIS B 1 137 ? 7.644   1.872   23.106  1.00 22.32 ? 139 HIS B NE2 1 
ATOM   2883 N N   . LYS B 1 138 ? 5.604   8.476   22.631  1.00 21.34 ? 140 LYS B N   1 
ATOM   2884 C CA  . LYS B 1 138 ? 5.565   9.864   22.186  1.00 21.25 ? 140 LYS B CA  1 
ATOM   2885 C C   . LYS B 1 138 ? 5.967   10.828  23.300  1.00 20.88 ? 140 LYS B C   1 
ATOM   2886 O O   . LYS B 1 138 ? 5.665   12.023  23.225  1.00 22.32 ? 140 LYS B O   1 
ATOM   2887 C CB  . LYS B 1 138 ? 4.172   10.205  21.645  1.00 21.81 ? 140 LYS B CB  1 
ATOM   2888 C CG  . LYS B 1 138 ? 3.940   9.675   20.219  1.00 24.25 ? 140 LYS B CG  1 
ATOM   2889 C CD  . LYS B 1 138 ? 2.640   10.208  19.620  1.00 27.32 ? 140 LYS B CD  1 
ATOM   2890 C CE  . LYS B 1 138 ? 1.464   9.282   19.778  1.00 31.68 ? 140 LYS B CE  1 
ATOM   2891 N NZ  . LYS B 1 138 ? 0.984   8.760   18.445  1.00 31.95 ? 140 LYS B NZ  1 
ATOM   2892 N N   . LEU B 1 139 ? 6.598   10.321  24.357  1.00 18.09 ? 141 LEU B N   1 
ATOM   2893 C CA  . LEU B 1 139 ? 6.983   11.128  25.510  1.00 18.80 ? 141 LEU B CA  1 
ATOM   2894 C C   . LEU B 1 139 ? 8.476   11.448  25.485  1.00 18.68 ? 141 LEU B C   1 
ATOM   2895 O O   . LEU B 1 139 ? 9.299   10.596  25.142  1.00 21.09 ? 141 LEU B O   1 
ATOM   2896 C CB  . LEU B 1 139 ? 6.620   10.398  26.810  1.00 16.78 ? 141 LEU B CB  1 
ATOM   2897 C CG  . LEU B 1 139 ? 5.130   10.177  27.067  1.00 16.54 ? 141 LEU B CG  1 
ATOM   2898 C CD1 . LEU B 1 139 ? 4.896   9.561   28.445  1.00 16.20 ? 141 LEU B CD1 1 
ATOM   2899 C CD2 . LEU B 1 139 ? 4.310   11.462  26.887  1.00 15.14 ? 141 LEU B CD2 1 
ATOM   2900 N N   . GLU B 1 140 ? 8.822   12.678  25.853  1.00 18.05 ? 142 GLU B N   1 
ATOM   2901 C CA  . GLU B 1 140 ? 10.224  13.079  25.887  1.00 21.38 ? 142 GLU B CA  1 
ATOM   2902 C C   . GLU B 1 140 ? 10.949  12.310  26.984  1.00 18.81 ? 142 GLU B C   1 
ATOM   2903 O O   . GLU B 1 140 ? 10.341  11.918  27.979  1.00 15.81 ? 142 GLU B O   1 
ATOM   2904 C CB  . GLU B 1 140 ? 10.349  14.587  26.136  1.00 22.01 ? 142 GLU B CB  1 
ATOM   2905 C CG  . GLU B 1 140 ? 9.824   15.445  24.977  1.00 21.08 ? 142 GLU B CG  1 
ATOM   2906 C CD  . GLU B 1 140 ? 10.015  16.929  25.175  1.00 23.71 ? 142 GLU B CD  1 
ATOM   2907 O OE1 . GLU B 1 140 ? 10.415  17.349  26.280  1.00 21.16 ? 142 GLU B OE1 1 
ATOM   2908 O OE2 . GLU B 1 140 ? 9.778   17.685  24.197  1.00 28.04 ? 142 GLU B OE2 1 
ATOM   2909 N N   . TYR B 1 141 ? 12.254  12.077  26.782  1.00 19.75 ? 143 TYR B N   1 
ATOM   2910 C CA  . TYR B 1 141 ? 13.090  11.397  27.780  1.00 19.61 ? 143 TYR B CA  1 
ATOM   2911 C C   . TYR B 1 141 ? 13.615  12.452  28.739  1.00 21.16 ? 143 TYR B C   1 
ATOM   2912 O O   . TYR B 1 141 ? 14.761  12.891  28.672  1.00 19.01 ? 143 TYR B O   1 
ATOM   2913 C CB  . TYR B 1 141 ? 14.226  10.623  27.118  1.00 19.11 ? 143 TYR B CB  1 
ATOM   2914 C CG  . TYR B 1 141 ? 15.007  9.726   28.054  1.00 20.90 ? 143 TYR B CG  1 
ATOM   2915 C CD1 . TYR B 1 141 ? 14.476  8.538   28.502  1.00 18.01 ? 143 TYR B CD1 1 
ATOM   2916 C CD2 . TYR B 1 141 ? 16.297  10.070  28.468  1.00 22.93 ? 143 TYR B CD2 1 
ATOM   2917 C CE1 . TYR B 1 141 ? 15.197  7.698   29.361  1.00 19.89 ? 143 TYR B CE1 1 
ATOM   2918 C CE2 . TYR B 1 141 ? 17.027  9.249   29.326  1.00 20.25 ? 143 TYR B CE2 1 
ATOM   2919 C CZ  . TYR B 1 141 ? 16.467  8.061   29.761  1.00 19.66 ? 143 TYR B CZ  1 
ATOM   2920 O OH  . TYR B 1 141 ? 17.167  7.230   30.599  1.00 21.11 ? 143 TYR B OH  1 
ATOM   2921 N N   . ASN B 1 142 ? 12.727  12.899  29.619  1.00 18.26 ? 144 ASN B N   1 
ATOM   2922 C CA  . ASN B 1 142 ? 13.053  13.829  30.690  1.00 19.84 ? 144 ASN B CA  1 
ATOM   2923 C C   . ASN B 1 142 ? 11.966  13.703  31.748  1.00 18.91 ? 144 ASN B C   1 
ATOM   2924 O O   . ASN B 1 142 ? 11.184  12.748  31.735  1.00 18.25 ? 144 ASN B O   1 
ATOM   2925 C CB  . ASN B 1 142 ? 13.230  15.262  30.163  1.00 22.18 ? 144 ASN B CB  1 
ATOM   2926 C CG  . ASN B 1 142 ? 12.060  15.740  29.313  1.00 24.63 ? 144 ASN B CG  1 
ATOM   2927 O OD1 . ASN B 1 142 ? 10.898  15.385  29.545  1.00 19.10 ? 144 ASN B OD1 1 
ATOM   2928 N ND2 . ASN B 1 142 ? 12.365  16.599  28.346  1.00 19.97 ? 144 ASN B ND2 1 
ATOM   2929 N N   . TYR B 1 143 ? 11.916  14.653  32.678  1.00 18.47 ? 145 TYR B N   1 
ATOM   2930 C CA  . TYR B 1 143 ? 11.003  14.502  33.806  1.00 19.81 ? 145 TYR B CA  1 
ATOM   2931 C C   . TYR B 1 143 ? 10.679  15.840  34.456  1.00 22.06 ? 145 TYR B C   1 
ATOM   2932 O O   . TYR B 1 143 ? 11.570  16.664  34.685  1.00 22.36 ? 145 TYR B O   1 
ATOM   2933 C CB  . TYR B 1 143 ? 11.604  13.579  34.870  1.00 18.56 ? 145 TYR B CB  1 
ATOM   2934 C CG  . TYR B 1 143 ? 10.560  12.830  35.630  1.00 15.29 ? 145 TYR B CG  1 
ATOM   2935 C CD1 . TYR B 1 143 ? 9.953   11.730  35.067  1.00 14.70 ? 145 TYR B CD1 1 
ATOM   2936 C CD2 . TYR B 1 143 ? 10.188  13.219  36.915  1.00 17.27 ? 145 TYR B CD2 1 
ATOM   2937 C CE1 . TYR B 1 143 ? 8.969   11.023  35.744  1.00 15.71 ? 145 TYR B CE1 1 
ATOM   2938 C CE2 . TYR B 1 143 ? 9.225   12.505  37.617  1.00 14.77 ? 145 TYR B CE2 1 
ATOM   2939 C CZ  . TYR B 1 143 ? 8.603   11.414  37.004  1.00 15.93 ? 145 TYR B CZ  1 
ATOM   2940 O OH  . TYR B 1 143 ? 7.617   10.676  37.637  1.00 14.83 ? 145 TYR B OH  1 
ATOM   2941 N N   . ASN B 1 144 ? 9.405   16.014  34.788  1.00 19.52 ? 146 ASN B N   1 
ATOM   2942 C CA  . ASN B 1 144 ? 8.905   17.093  35.633  1.00 18.59 ? 146 ASN B CA  1 
ATOM   2943 C C   . ASN B 1 144 ? 8.470   16.442  36.935  1.00 20.80 ? 146 ASN B C   1 
ATOM   2944 O O   . ASN B 1 144 ? 7.456   15.729  36.964  1.00 19.63 ? 146 ASN B O   1 
ATOM   2945 C CB  . ASN B 1 144 ? 7.708   17.812  35.005  1.00 19.39 ? 146 ASN B CB  1 
ATOM   2946 C CG  . ASN B 1 144 ? 7.984   18.334  33.608  1.00 25.43 ? 146 ASN B CG  1 
ATOM   2947 O OD1 . ASN B 1 144 ? 8.864   19.178  33.410  1.00 23.98 ? 146 ASN B OD1 1 
ATOM   2948 N ND2 . ASN B 1 144 ? 7.212   17.848  32.629  1.00 24.32 ? 146 ASN B ND2 1 
ATOM   2949 N N   . ASP B 1 145 ? 9.221   16.672  38.005  1.00 14.80 ? 147 ASP B N   1 
ATOM   2950 C CA  . ASP B 1 145 ? 8.802   16.114  39.276  1.00 17.09 ? 147 ASP B CA  1 
ATOM   2951 C C   . ASP B 1 145 ? 7.582   16.843  39.829  1.00 20.42 ? 147 ASP B C   1 
ATOM   2952 O O   . ASP B 1 145 ? 7.228   17.941  39.398  1.00 20.10 ? 147 ASP B O   1 
ATOM   2953 C CB  . ASP B 1 145 ? 9.939   16.166  40.278  1.00 18.92 ? 147 ASP B CB  1 
ATOM   2954 C CG  . ASP B 1 145 ? 11.090  15.302  39.852  1.00 17.87 ? 147 ASP B CG  1 
ATOM   2955 O OD1 . ASP B 1 145 ? 11.029  14.085  40.130  1.00 17.32 ? 147 ASP B OD1 1 
ATOM   2956 O OD2 . ASP B 1 145 ? 12.025  15.831  39.224  1.00 17.67 ? 147 ASP B OD2 1 
ATOM   2957 N N   . HIS B 1 146 ? 6.950   16.227  40.830  1.00 16.34 ? 148 HIS B N   1 
ATOM   2958 C CA  . HIS B 1 146 ? 5.892   16.918  41.549  1.00 21.17 ? 148 HIS B CA  1 
ATOM   2959 C C   . HIS B 1 146 ? 5.958   16.545  43.027  1.00 24.21 ? 148 HIS B C   1 
ATOM   2960 O O   . HIS B 1 146 ? 6.268   15.395  43.365  1.00 17.31 ? 148 HIS B O   1 
ATOM   2961 C CB  . HIS B 1 146 ? 4.522   16.565  40.961  1.00 20.88 ? 148 HIS B CB  1 
ATOM   2962 C CG  . HIS B 1 146 ? 3.440   17.501  41.381  1.00 24.31 ? 148 HIS B CG  1 
ATOM   2963 N ND1 . HIS B 1 146 ? 2.856   17.454  42.629  1.00 23.71 ? 148 HIS B ND1 1 
ATOM   2964 C CD2 . HIS B 1 146 ? 2.843   18.520  40.721  1.00 25.70 ? 148 HIS B CD2 1 
ATOM   2965 C CE1 . HIS B 1 146 ? 1.941   18.407  42.717  1.00 27.98 ? 148 HIS B CE1 1 
ATOM   2966 N NE2 . HIS B 1 146 ? 1.918   19.069  41.575  1.00 27.53 ? 148 HIS B NE2 1 
ATOM   2967 N N   . GLN B 1 147 ? 5.675   17.516  43.905  1.00 17.66 ? 149 GLN B N   1 
ATOM   2968 C CA  . GLN B 1 147 ? 5.602   17.212  45.336  1.00 20.43 ? 149 GLN B CA  1 
ATOM   2969 C C   . GLN B 1 147 ? 4.496   16.194  45.618  1.00 18.56 ? 149 GLN B C   1 
ATOM   2970 O O   . GLN B 1 147 ? 3.536   16.055  44.857  1.00 21.58 ? 149 GLN B O   1 
ATOM   2971 C CB  . GLN B 1 147 ? 5.317   18.475  46.141  1.00 24.60 ? 149 GLN B CB  1 
ATOM   2972 C CG  . GLN B 1 147 ? 4.341   19.423  45.425  1.00 29.07 ? 149 GLN B CG  1 
ATOM   2973 C CD  . GLN B 1 147 ? 3.911   20.591  46.286  1.00 32.13 ? 149 GLN B CD  1 
ATOM   2974 O OE1 . GLN B 1 147 ? 4.742   21.346  46.786  1.00 36.18 ? 149 GLN B OE1 1 
ATOM   2975 N NE2 . GLN B 1 147 ? 2.599   20.765  46.436  1.00 34.30 ? 149 GLN B NE2 1 
ATOM   2976 N N   . VAL B 1 148 ? 4.646   15.468  46.719  1.00 18.51 ? 150 VAL B N   1 
ATOM   2977 C CA  . VAL B 1 148 ? 3.728   14.405  47.122  1.00 18.60 ? 150 VAL B CA  1 
ATOM   2978 C C   . VAL B 1 148 ? 3.328   14.680  48.563  1.00 18.55 ? 150 VAL B C   1 
ATOM   2979 O O   . VAL B 1 148 ? 4.182   14.670  49.457  1.00 18.53 ? 150 VAL B O   1 
ATOM   2980 C CB  . VAL B 1 148 ? 4.367   13.010  47.007  1.00 20.08 ? 150 VAL B CB  1 
ATOM   2981 C CG1 . VAL B 1 148 ? 3.399   11.944  47.501  1.00 19.52 ? 150 VAL B CG1 1 
ATOM   2982 C CG2 . VAL B 1 148 ? 4.813   12.724  45.570  1.00 16.45 ? 150 VAL B CG2 1 
ATOM   2983 N N   . TYR B 1 149 ? 2.038   14.910  48.795  1.00 19.34 ? 151 TYR B N   1 
ATOM   2984 C CA  . TYR B 1 149 ? 1.557   15.210  50.137  1.00 21.05 ? 151 TYR B CA  1 
ATOM   2985 C C   . TYR B 1 149 ? 1.207   13.885  50.801  1.00 21.56 ? 151 TYR B C   1 
ATOM   2986 O O   . TYR B 1 149 ? 0.190   13.269  50.492  1.00 18.83 ? 151 TYR B O   1 
ATOM   2987 C CB  . TYR B 1 149 ? 0.368   16.160  50.086  1.00 20.85 ? 151 TYR B CB  1 
ATOM   2988 C CG  . TYR B 1 149 ? -0.041  16.696  51.441  1.00 20.94 ? 151 TYR B CG  1 
ATOM   2989 C CD1 . TYR B 1 149 ? 0.823   17.501  52.172  1.00 22.87 ? 151 TYR B CD1 1 
ATOM   2990 C CD2 . TYR B 1 149 ? -1.295  16.423  51.976  1.00 23.40 ? 151 TYR B CD2 1 
ATOM   2991 C CE1 . TYR B 1 149 ? 0.454   18.010  53.404  1.00 23.58 ? 151 TYR B CE1 1 
ATOM   2992 C CE2 . TYR B 1 149 ? -1.674  16.936  53.214  1.00 26.26 ? 151 TYR B CE2 1 
ATOM   2993 C CZ  . TYR B 1 149 ? -0.794  17.723  53.917  1.00 26.06 ? 151 TYR B CZ  1 
ATOM   2994 O OH  . TYR B 1 149 ? -1.152  18.243  55.146  1.00 30.08 ? 151 TYR B OH  1 
ATOM   2995 N N   . ILE B 1 150 ? 2.076   13.432  51.697  1.00 20.36 ? 152 ILE B N   1 
ATOM   2996 C CA  . ILE B 1 150 ? 1.874   12.180  52.420  1.00 19.56 ? 152 ILE B CA  1 
ATOM   2997 C C   . ILE B 1 150 ? 0.917   12.421  53.576  1.00 23.90 ? 152 ILE B C   1 
ATOM   2998 O O   . ILE B 1 150 ? 1.181   13.257  54.449  1.00 22.17 ? 152 ILE B O   1 
ATOM   2999 C CB  . ILE B 1 150 ? 3.214   11.629  52.923  1.00 22.06 ? 152 ILE B CB  1 
ATOM   3000 C CG1 . ILE B 1 150 ? 4.199   11.555  51.747  1.00 21.36 ? 152 ILE B CG1 1 
ATOM   3001 C CG2 . ILE B 1 150 ? 3.016   10.363  53.723  1.00 22.36 ? 152 ILE B CG2 1 
ATOM   3002 C CD1 . ILE B 1 150 ? 3.977   10.338  50.850  1.00 21.98 ? 152 ILE B CD1 1 
ATOM   3003 N N   . MET B 1 151 ? -0.187  11.680  53.599  1.00 20.98 ? 153 MET B N   1 
ATOM   3004 C CA  . MET B 1 151 ? -1.137  11.768  54.700  1.00 26.90 ? 153 MET B CA  1 
ATOM   3005 C C   . MET B 1 151 ? -1.312  10.448  55.426  1.00 25.61 ? 153 MET B C   1 
ATOM   3006 O O   . MET B 1 151 ? -1.291  9.368   54.820  1.00 22.53 ? 153 MET B O   1 
ATOM   3007 C CB  . MET B 1 151 ? -2.504  12.332  54.259  1.00 24.17 ? 153 MET B CB  1 
ATOM   3008 C CG  . MET B 1 151 ? -2.422  13.294  53.104  1.00 23.20 ? 153 MET B CG  1 
ATOM   3009 S SD  . MET B 1 151 ? -4.040  13.744  52.441  1.00 28.42 ? 153 MET B SD  1 
ATOM   3010 C CE  . MET B 1 151 ? -4.737  14.570  53.858  1.00 28.01 ? 153 MET B CE  1 
ATOM   3011 N N   . ALA B 1 152 ? -1.447  10.565  56.744  1.00 26.08 ? 154 ALA B N   1 
ATOM   3012 C CA  . ALA B 1 152 ? -1.706  9.419   57.590  1.00 27.44 ? 154 ALA B CA  1 
ATOM   3013 C C   . ALA B 1 152 ? -3.051  8.810   57.242  1.00 30.86 ? 154 ALA B C   1 
ATOM   3014 O O   . ALA B 1 152 ? -4.013  9.519   56.934  1.00 31.05 ? 154 ALA B O   1 
ATOM   3015 C CB  . ALA B 1 152 ? -1.674  9.835   59.062  1.00 29.49 ? 154 ALA B CB  1 
ATOM   3016 N N   . ASP B 1 153 ? -3.101  7.482   57.284  1.00 33.76 ? 155 ASP B N   1 
ATOM   3017 C CA  . ASP B 1 153 ? -4.296  6.690   57.015  1.00 36.94 ? 155 ASP B CA  1 
ATOM   3018 C C   . ASP B 1 153 ? -4.516  5.734   58.185  1.00 45.82 ? 155 ASP B C   1 
ATOM   3019 O O   . ASP B 1 153 ? -4.413  4.518   58.029  1.00 49.52 ? 155 ASP B O   1 
ATOM   3020 C CB  . ASP B 1 153 ? -4.125  5.911   55.714  1.00 40.60 ? 155 ASP B CB  1 
ATOM   3021 C CG  . ASP B 1 153 ? -5.424  5.342   55.192  1.00 46.24 ? 155 ASP B CG  1 
ATOM   3022 O OD1 . ASP B 1 153 ? -6.385  5.220   55.983  1.00 50.84 ? 155 ASP B OD1 1 
ATOM   3023 O OD2 . ASP B 1 153 ? -5.466  4.985   53.991  1.00 46.70 ? 155 ASP B OD2 1 
ATOM   3024 N N   . LYS B 1 154 ? -4.822  6.296   59.364  1.00 45.60 ? 156 LYS B N   1 
ATOM   3025 C CA  . LYS B 1 154 ? -4.753  5.533   60.614  1.00 51.55 ? 156 LYS B CA  1 
ATOM   3026 C C   . LYS B 1 154 ? -5.533  4.222   60.542  1.00 52.85 ? 156 LYS B C   1 
ATOM   3027 O O   . LYS B 1 154 ? -5.148  3.235   61.182  1.00 52.13 ? 156 LYS B O   1 
ATOM   3028 C CB  . LYS B 1 154 ? -5.250  6.398   61.782  1.00 53.53 ? 156 LYS B CB  1 
ATOM   3029 C CG  . LYS B 1 154 ? -5.645  5.625   63.047  1.00 59.49 ? 156 LYS B CG  1 
ATOM   3030 C CD  . LYS B 1 154 ? -7.154  5.577   63.251  1.00 56.19 ? 156 LYS B CD  1 
ATOM   3031 C CE  . LYS B 1 154 ? -7.755  6.974   63.201  1.00 59.34 ? 156 LYS B CE  1 
ATOM   3032 N NZ  . LYS B 1 154 ? -9.060  7.046   63.921  1.00 63.40 ? 156 LYS B NZ  1 
ATOM   3033 N N   . GLN B 1 155 ? -6.609  4.191   59.751  1.00 53.48 ? 157 GLN B N   1 
ATOM   3034 C CA  . GLN B 1 155 ? -7.384  2.969   59.545  1.00 55.26 ? 157 GLN B CA  1 
ATOM   3035 C C   . GLN B 1 155 ? -6.490  1.792   59.170  1.00 53.93 ? 157 GLN B C   1 
ATOM   3036 O O   . GLN B 1 155 ? -6.578  0.709   59.759  1.00 51.77 ? 157 GLN B O   1 
ATOM   3037 C CB  . GLN B 1 155 ? -8.417  3.205   58.446  1.00 57.27 ? 157 GLN B CB  1 
ATOM   3038 C CG  . GLN B 1 155 ? -9.535  4.148   58.821  1.00 62.67 ? 157 GLN B CG  1 
ATOM   3039 C CD  . GLN B 1 155 ? -10.886 3.621   58.397  1.00 69.37 ? 157 GLN B CD  1 
ATOM   3040 O OE1 . GLN B 1 155 ? -11.043 3.107   57.287  1.00 69.97 ? 157 GLN B OE1 1 
ATOM   3041 N NE2 . GLN B 1 155 ? -11.874 3.752   59.276  1.00 68.35 ? 157 GLN B NE2 1 
ATOM   3042 N N   . LYS B 1 156 ? -5.628  1.990   58.179  1.00 50.23 ? 158 LYS B N   1 
ATOM   3043 C CA  . LYS B 1 156 ? -4.767  0.942   57.660  1.00 49.16 ? 158 LYS B CA  1 
ATOM   3044 C C   . LYS B 1 156 ? -3.400  0.936   58.328  1.00 49.31 ? 158 LYS B C   1 
ATOM   3045 O O   . LYS B 1 156 ? -2.492  0.249   57.847  1.00 50.08 ? 158 LYS B O   1 
ATOM   3046 C CB  . LYS B 1 156 ? -4.610  1.115   56.147  1.00 49.19 ? 158 LYS B CB  1 
ATOM   3047 C CG  . LYS B 1 156 ? -5.940  1.080   55.396  1.00 50.02 ? 158 LYS B CG  1 
ATOM   3048 C CD  . LYS B 1 156 ? -6.235  -0.280  54.789  1.00 52.64 ? 158 LYS B CD  1 
ATOM   3049 C CE  . LYS B 1 156 ? -7.308  -0.173  53.718  1.00 48.65 ? 158 LYS B CE  1 
ATOM   3050 N NZ  . LYS B 1 156 ? -7.057  -1.082  52.559  1.00 50.16 ? 158 LYS B NZ  1 
ATOM   3051 N N   . ASN B 1 157 ? -3.238  1.686   59.423  1.00 45.80 ? 159 ASN B N   1 
ATOM   3052 C CA  . ASN B 1 157 ? -1.929  1.922   60.039  1.00 44.51 ? 159 ASN B CA  1 
ATOM   3053 C C   . ASN B 1 157 ? -0.888  2.301   58.991  1.00 45.77 ? 159 ASN B C   1 
ATOM   3054 O O   . ASN B 1 157 ? 0.284   1.931   59.085  1.00 45.33 ? 159 ASN B O   1 
ATOM   3055 C CB  . ASN B 1 157 ? -1.462  0.714   60.852  1.00 42.04 ? 159 ASN B CB  1 
ATOM   3056 C CG  . ASN B 1 157 ? -0.330  1.061   61.813  1.00 48.69 ? 159 ASN B CG  1 
ATOM   3057 O OD1 . ASN B 1 157 ? -0.383  2.069   62.524  1.00 50.15 ? 159 ASN B OD1 1 
ATOM   3058 N ND2 . ASN B 1 157 ? 0.708   0.228   61.826  1.00 47.06 ? 159 ASN B ND2 1 
ATOM   3059 N N   . GLY B 1 158 ? -1.319  3.054   57.984  1.00 38.31 ? 160 GLY B N   1 
ATOM   3060 C CA  . GLY B 1 158 ? -0.447  3.362   56.877  1.00 33.33 ? 160 GLY B CA  1 
ATOM   3061 C C   . GLY B 1 158 ? -0.611  4.781   56.391  1.00 34.02 ? 160 GLY B C   1 
ATOM   3062 O O   . GLY B 1 158 ? -1.110  5.639   57.125  1.00 29.16 ? 160 GLY B O   1 
ATOM   3063 N N   . ILE B 1 159 ? -0.175  5.047   55.160  1.00 26.94 ? 161 ILE B N   1 
ATOM   3064 C CA  . ILE B 1 159 ? -0.249  6.385   54.590  1.00 25.45 ? 161 ILE B CA  1 
ATOM   3065 C C   . ILE B 1 159 ? -0.889  6.294   53.216  1.00 25.14 ? 161 ILE B C   1 
ATOM   3066 O O   . ILE B 1 159 ? -0.973  5.227   52.600  1.00 22.22 ? 161 ILE B O   1 
ATOM   3067 C CB  . ILE B 1 159 ? 1.124   7.074   54.483  1.00 23.27 ? 161 ILE B CB  1 
ATOM   3068 C CG1 . ILE B 1 159 ? 2.085   6.229   53.636  1.00 23.10 ? 161 ILE B CG1 1 
ATOM   3069 C CG2 . ILE B 1 159 ? 1.715   7.312   55.869  1.00 25.66 ? 161 ILE B CG2 1 
ATOM   3070 C CD1 . ILE B 1 159 ? 2.377   6.818   52.272  1.00 25.35 ? 161 ILE B CD1 1 
ATOM   3071 N N   . LYS B 1 160 ? -1.337  7.447   52.735  1.00 24.65 ? 162 LYS B N   1 
ATOM   3072 C CA  . LYS B 1 160 ? -1.942  7.551   51.423  1.00 21.12 ? 162 LYS B CA  1 
ATOM   3073 C C   . LYS B 1 160 ? -1.469  8.840   50.785  1.00 20.78 ? 162 LYS B C   1 
ATOM   3074 O O   . LYS B 1 160 ? -1.000  9.748   51.466  1.00 21.30 ? 162 LYS B O   1 
ATOM   3075 C CB  . LYS B 1 160 ? -3.467  7.549   51.501  1.00 25.49 ? 162 LYS B CB  1 
ATOM   3076 C CG  . LYS B 1 160 ? -4.027  8.680   52.347  1.00 25.28 ? 162 LYS B CG  1 
ATOM   3077 C CD  . LYS B 1 160 ? -5.538  8.624   52.437  1.00 35.81 ? 162 LYS B CD  1 
ATOM   3078 C CE  . LYS B 1 160 ? -6.082  9.877   53.126  1.00 35.34 ? 162 LYS B CE  1 
ATOM   3079 N NZ  . LYS B 1 160 ? -5.935  9.791   54.607  1.00 39.12 ? 162 LYS B NZ  1 
ATOM   3080 N N   . ALA B 1 161 ? -1.627  8.928   49.470  1.00 18.44 ? 163 ALA B N   1 
ATOM   3081 C CA  . ALA B 1 161 ? -1.284  10.166  48.791  1.00 17.87 ? 163 ALA B CA  1 
ATOM   3082 C C   . ALA B 1 161 ? -1.932  10.174  47.423  1.00 21.22 ? 163 ALA B C   1 
ATOM   3083 O O   . ALA B 1 161 ? -2.252  9.122   46.851  1.00 20.74 ? 163 ALA B O   1 
ATOM   3084 C CB  . ALA B 1 161 ? 0.238   10.340  48.662  1.00 19.94 ? 163 ALA B CB  1 
ATOM   3085 N N   . ASN B 1 162 ? -2.126  11.377  46.900  1.00 20.39 ? 164 ASN B N   1 
ATOM   3086 C CA  . ASN B 1 162 ? -2.689  11.533  45.571  1.00 25.55 ? 164 ASN B CA  1 
ATOM   3087 C C   . ASN B 1 162 ? -1.992  12.719  44.914  1.00 21.93 ? 164 ASN B C   1 
ATOM   3088 O O   . ASN B 1 162 ? -1.853  13.772  45.546  1.00 21.75 ? 164 ASN B O   1 
ATOM   3089 C CB  . ASN B 1 162 ? -4.209  11.719  45.681  1.00 25.44 ? 164 ASN B CB  1 
ATOM   3090 C CG  . ASN B 1 162 ? -4.782  12.456  44.535  1.00 34.68 ? 164 ASN B CG  1 
ATOM   3091 O OD1 . ASN B 1 162 ? -4.796  11.948  43.402  1.00 37.12 ? 164 ASN B OD1 1 
ATOM   3092 N ND2 . ASN B 1 162 ? -5.268  13.663  44.794  1.00 33.60 ? 164 ASN B ND2 1 
ATOM   3093 N N   . PHE B 1 163 ? -1.487  12.531  43.686  1.00 18.08 ? 165 PHE B N   1 
ATOM   3094 C CA  . PHE B 1 163 ? -0.654  13.554  43.067  1.00 19.33 ? 165 PHE B CA  1 
ATOM   3095 C C   . PHE B 1 163 ? -0.567  13.327  41.568  1.00 18.14 ? 165 PHE B C   1 
ATOM   3096 O O   . PHE B 1 163 ? -0.724  12.208  41.083  1.00 19.13 ? 165 PHE B O   1 
ATOM   3097 C CB  . PHE B 1 163 ? 0.758   13.607  43.673  1.00 16.94 ? 165 PHE B CB  1 
ATOM   3098 C CG  . PHE B 1 163 ? 1.569   12.342  43.489  1.00 15.67 ? 165 PHE B CG  1 
ATOM   3099 C CD1 . PHE B 1 163 ? 1.487   11.303  44.404  1.00 16.45 ? 165 PHE B CD1 1 
ATOM   3100 C CD2 . PHE B 1 163 ? 2.426   12.208  42.408  1.00 17.88 ? 165 PHE B CD2 1 
ATOM   3101 C CE1 . PHE B 1 163 ? 2.243   10.151  44.252  1.00 17.87 ? 165 PHE B CE1 1 
ATOM   3102 C CE2 . PHE B 1 163 ? 3.177   11.047  42.238  1.00 17.78 ? 165 PHE B CE2 1 
ATOM   3103 C CZ  . PHE B 1 163 ? 3.085   10.025  43.174  1.00 14.90 ? 165 PHE B CZ  1 
ATOM   3104 N N   . LYS B 1 164 ? -0.329  14.413  40.836  1.00 18.33 ? 166 LYS B N   1 
ATOM   3105 C CA  . LYS B 1 164 ? -0.251  14.375  39.381  1.00 17.14 ? 166 LYS B CA  1 
ATOM   3106 C C   . LYS B 1 164 ? 1.197   14.507  38.947  1.00 20.05 ? 166 LYS B C   1 
ATOM   3107 O O   . LYS B 1 164 ? 1.951   15.290  39.527  1.00 21.88 ? 166 LYS B O   1 
ATOM   3108 C CB  . LYS B 1 164 ? -1.077  15.506  38.763  1.00 21.42 ? 166 LYS B CB  1 
ATOM   3109 C CG  . LYS B 1 164 ? -2.516  15.454  39.209  1.00 26.52 ? 166 LYS B CG  1 
ATOM   3110 C CD  . LYS B 1 164 ? -3.288  16.733  38.858  1.00 33.87 ? 166 LYS B CD  1 
ATOM   3111 C CE  . LYS B 1 164 ? -4.788  16.427  38.769  1.00 36.99 ? 166 LYS B CE  1 
ATOM   3112 N NZ  . LYS B 1 164 ? -5.404  16.633  37.432  1.00 38.70 ? 166 LYS B NZ  1 
ATOM   3113 N N   . ILE B 1 165 ? 1.582   13.726  37.941  1.00 16.39 ? 167 ILE B N   1 
ATOM   3114 C CA  . ILE B 1 165 ? 2.838   13.906  37.229  1.00 14.66 ? 167 ILE B CA  1 
ATOM   3115 C C   . ILE B 1 165 ? 2.519   14.348  35.804  1.00 18.87 ? 167 ILE B C   1 
ATOM   3116 O O   . ILE B 1 165 ? 1.585   13.829  35.175  1.00 18.06 ? 167 ILE B O   1 
ATOM   3117 C CB  . ILE B 1 165 ? 3.662   12.604  37.230  1.00 16.18 ? 167 ILE B CB  1 
ATOM   3118 C CG1 . ILE B 1 165 ? 4.067   12.230  38.656  1.00 16.25 ? 167 ILE B CG1 1 
ATOM   3119 C CG2 . ILE B 1 165 ? 4.891   12.708  36.346  1.00 18.28 ? 167 ILE B CG2 1 
ATOM   3120 C CD1 . ILE B 1 165 ? 5.130   13.150  39.256  1.00 16.19 ? 167 ILE B CD1 1 
ATOM   3121 N N   . ARG B 1 166 ? 3.296   15.303  35.296  1.00 20.04 ? 168 ARG B N   1 
ATOM   3122 C CA  . ARG B 1 166 ? 3.166   15.818  33.935  1.00 18.47 ? 168 ARG B CA  1 
ATOM   3123 C C   . ARG B 1 166 ? 4.354   15.328  33.113  1.00 20.07 ? 168 ARG B C   1 
ATOM   3124 O O   . ARG B 1 166 ? 5.501   15.681  33.409  1.00 19.45 ? 168 ARG B O   1 
ATOM   3125 C CB  . ARG B 1 166 ? 3.129   17.349  33.941  1.00 22.02 ? 168 ARG B CB  1 
ATOM   3126 C CG  . ARG B 1 166 ? 2.043   17.934  34.845  1.00 25.29 ? 168 ARG B CG  1 
ATOM   3127 C CD  . ARG B 1 166 ? 2.227   19.433  35.057  1.00 34.20 ? 168 ARG B CD  1 
ATOM   3128 N NE  . ARG B 1 166 ? 1.687   20.265  33.986  1.00 42.26 ? 168 ARG B NE  1 
ATOM   3129 C CZ  . ARG B 1 166 ? 2.413   21.097  33.249  1.00 43.35 ? 168 ARG B CZ  1 
ATOM   3130 N NH1 . ARG B 1 166 ? 3.724   21.210  33.419  1.00 42.40 ? 168 ARG B NH1 1 
ATOM   3131 N NH2 . ARG B 1 166 ? 1.810   21.827  32.310  1.00 40.43 ? 168 ARG B NH2 1 
ATOM   3132 N N   . HIS B 1 167 ? 4.077   14.534  32.081  1.00 15.55 ? 169 HIS B N   1 
ATOM   3133 C CA  . HIS B 1 167 ? 5.106   13.971  31.209  1.00 17.68 ? 169 HIS B CA  1 
ATOM   3134 C C   . HIS B 1 167 ? 5.138   14.798  29.923  1.00 18.76 ? 169 HIS B C   1 
ATOM   3135 O O   . HIS B 1 167 ? 4.110   14.910  29.248  1.00 18.23 ? 169 HIS B O   1 
ATOM   3136 C CB  . HIS B 1 167 ? 4.777   12.513  30.887  1.00 15.85 ? 169 HIS B CB  1 
ATOM   3137 C CG  . HIS B 1 167 ? 4.890   11.563  32.048  1.00 19.88 ? 169 HIS B CG  1 
ATOM   3138 N ND1 . HIS B 1 167 ? 6.021   11.452  32.827  1.00 15.52 ? 169 HIS B ND1 1 
ATOM   3139 C CD2 . HIS B 1 167 ? 3.994   10.686  32.565  1.00 16.24 ? 169 HIS B CD2 1 
ATOM   3140 C CE1 . HIS B 1 167 ? 5.825   10.542  33.766  1.00 14.63 ? 169 HIS B CE1 1 
ATOM   3141 N NE2 . HIS B 1 167 ? 4.602   10.061  33.630  1.00 15.59 ? 169 HIS B NE2 1 
ATOM   3142 N N   . ASN B 1 168 ? 6.295   15.374  29.580  1.00 16.43 ? 170 ASN B N   1 
ATOM   3143 C CA  . ASN B 1 168 ? 6.399   16.129  28.323  1.00 18.02 ? 170 ASN B CA  1 
ATOM   3144 C C   . ASN B 1 168 ? 6.141   15.244  27.109  1.00 19.33 ? 170 ASN B C   1 
ATOM   3145 O O   . ASN B 1 168 ? 6.788   14.208  26.931  1.00 19.06 ? 170 ASN B O   1 
ATOM   3146 C CB  . ASN B 1 168 ? 7.781   16.771  28.166  1.00 20.09 ? 170 ASN B CB  1 
ATOM   3147 C CG  . ASN B 1 168 ? 7.956   18.018  28.991  1.00 21.71 ? 170 ASN B CG  1 
ATOM   3148 O OD1 . ASN B 1 168 ? 7.056   18.445  29.697  1.00 20.48 ? 170 ASN B OD1 1 
ATOM   3149 N ND2 . ASN B 1 168 ? 9.140   18.619  28.896  1.00 26.91 ? 170 ASN B ND2 1 
ATOM   3150 N N   . ILE B 1 169 ? 5.232   15.699  26.232  1.00 17.70 ? 171 ILE B N   1 
ATOM   3151 C CA  . ILE B 1 169 ? 4.964   15.057  24.947  1.00 21.30 ? 171 ILE B CA  1 
ATOM   3152 C C   . ILE B 1 169 ? 5.914   15.645  23.909  1.00 22.18 ? 171 ILE B C   1 
ATOM   3153 O O   . ILE B 1 169 ? 6.190   16.850  23.915  1.00 22.32 ? 171 ILE B O   1 
ATOM   3154 C CB  . ILE B 1 169 ? 3.492   15.262  24.529  1.00 20.43 ? 171 ILE B CB  1 
ATOM   3155 C CG1 . ILE B 1 169 ? 2.543   14.798  25.629  1.00 22.21 ? 171 ILE B CG1 1 
ATOM   3156 C CG2 . ILE B 1 169 ? 3.156   14.475  23.268  1.00 16.31 ? 171 ILE B CG2 1 
ATOM   3157 N N   . GLU B 1 170 ? 6.426   14.798  23.019  1.00 22.16 ? 172 GLU B N   1 
ATOM   3158 C CA  . GLU B 1 170 ? 7.264   15.300  21.939  1.00 25.03 ? 172 GLU B CA  1 
ATOM   3159 C C   . GLU B 1 170 ? 6.466   16.300  21.101  1.00 25.60 ? 172 GLU B C   1 
ATOM   3160 O O   . GLU B 1 170 ? 5.301   16.058  20.769  1.00 24.09 ? 172 GLU B O   1 
ATOM   3161 C CB  . GLU B 1 170 ? 7.755   14.130  21.085  1.00 29.56 ? 172 GLU B CB  1 
ATOM   3162 C CG  . GLU B 1 170 ? 8.338   13.028  21.959  1.00 27.68 ? 172 GLU B CG  1 
ATOM   3163 C CD  . GLU B 1 170 ? 9.635   12.422  21.464  1.00 39.92 ? 172 GLU B CD  1 
ATOM   3164 O OE1 . GLU B 1 170 ? 9.571   11.452  20.674  1.00 42.89 ? 172 GLU B OE1 1 
ATOM   3165 O OE2 . GLU B 1 170 ? 10.716  12.888  21.903  1.00 38.57 ? 172 GLU B OE2 1 
ATOM   3166 N N   . ASP B 1 171 ? 7.087   17.434  20.790  1.00 27.63 ? 173 ASP B N   1 
ATOM   3167 C CA  . ASP B 1 171 ? 6.552   18.523  19.972  1.00 26.60 ? 173 ASP B CA  1 
ATOM   3168 C C   . ASP B 1 171 ? 5.589   19.386  20.780  1.00 29.39 ? 173 ASP B C   1 
ATOM   3169 O O   . ASP B 1 171 ? 4.960   20.283  20.208  1.00 28.53 ? 173 ASP B O   1 
ATOM   3170 C CB  . ASP B 1 171 ? 5.850   18.019  18.699  1.00 26.40 ? 173 ASP B CB  1 
ATOM   3171 C CG  . ASP B 1 171 ? 6.822   17.431  17.706  1.00 34.60 ? 173 ASP B CG  1 
ATOM   3172 O OD1 . ASP B 1 171 ? 6.454   16.450  17.027  1.00 41.02 ? 173 ASP B OD1 1 
ATOM   3173 O OD2 . ASP B 1 171 ? 7.954   17.945  17.616  1.00 36.91 ? 173 ASP B OD2 1 
ATOM   3174 N N   . GLY B 1 172 ? 5.438   19.144  22.079  1.00 27.44 ? 174 GLY B N   1 
ATOM   3175 C CA  . GLY B 1 172 ? 4.698   20.051  22.937  1.00 26.12 ? 174 GLY B CA  1 
ATOM   3176 C C   . GLY B 1 172 ? 3.545   19.409  23.680  1.00 21.94 ? 174 GLY B C   1 
ATOM   3177 O O   . GLY B 1 172 ? 2.894   18.482  23.192  1.00 22.95 ? 174 GLY B O   1 
ATOM   3178 N N   . GLY B 1 173 ? 3.271   19.925  24.871  1.00 23.29 ? 175 GLY B N   1 
ATOM   3179 C CA  . GLY B 1 173 ? 2.170   19.462  25.690  1.00 24.89 ? 175 GLY B CA  1 
ATOM   3180 C C   . GLY B 1 173 ? 2.640   18.510  26.774  1.00 22.00 ? 175 GLY B C   1 
ATOM   3181 O O   . GLY B 1 173 ? 3.792   18.071  26.811  1.00 21.56 ? 175 GLY B O   1 
ATOM   3182 N N   . VAL B 1 174 ? 1.713   18.181  27.673  1.00 19.90 ? 176 VAL B N   1 
ATOM   3183 C CA  . VAL B 1 174 ? 1.995   17.263  28.770  1.00 24.31 ? 176 VAL B CA  1 
ATOM   3184 C C   . VAL B 1 174 ? 0.952   16.160  28.771  1.00 21.13 ? 176 VAL B C   1 
ATOM   3185 O O   . VAL B 1 174 ? -0.221  16.390  28.459  1.00 22.87 ? 176 VAL B O   1 
ATOM   3186 C CB  . VAL B 1 174 ? 2.038   17.978  30.141  1.00 21.64 ? 176 VAL B CB  1 
ATOM   3187 C CG1 . VAL B 1 174 ? 3.205   18.950  30.183  1.00 25.70 ? 176 VAL B CG1 1 
ATOM   3188 C CG2 . VAL B 1 174 ? 0.746   18.701  30.403  1.00 26.22 ? 176 VAL B CG2 1 
ATOM   3189 N N   . GLN B 1 175 ? 1.404   14.951  29.075  1.00 19.02 ? 177 GLN B N   1 
ATOM   3190 C CA  . GLN B 1 175 ? 0.542   13.810  29.319  1.00 16.75 ? 177 GLN B CA  1 
ATOM   3191 C C   . GLN B 1 175 ? 0.404   13.691  30.830  1.00 19.70 ? 177 GLN B C   1 
ATOM   3192 O O   . GLN B 1 175 ? 1.406   13.477  31.518  1.00 19.74 ? 177 GLN B O   1 
ATOM   3193 C CB  . GLN B 1 175 ? 1.175   12.547  28.718  1.00 18.72 ? 177 GLN B CB  1 
ATOM   3194 C CG  . GLN B 1 175 ? 0.528   11.237  29.158  1.00 18.74 ? 177 GLN B CG  1 
ATOM   3195 C CD  . GLN B 1 175 ? -0.861  11.068  28.555  1.00 20.86 ? 177 GLN B CD  1 
ATOM   3196 O OE1 . GLN B 1 175 ? -1.009  10.919  27.343  1.00 19.22 ? 177 GLN B OE1 1 
ATOM   3197 N NE2 . GLN B 1 175 ? -1.884  11.082  29.403  1.00 19.66 ? 177 GLN B NE2 1 
ATOM   3198 N N   . LEU B 1 176 ? -0.809  13.854  31.357  1.00 17.51 ? 178 LEU B N   1 
ATOM   3199 C CA  . LEU B 1 176 ? -0.992  13.753  32.806  1.00 17.70 ? 178 LEU B CA  1 
ATOM   3200 C C   . LEU B 1 176 ? -1.064  12.305  33.276  1.00 17.01 ? 178 LEU B C   1 
ATOM   3201 O O   . LEU B 1 176 ? -1.620  11.433  32.601  1.00 18.28 ? 178 LEU B O   1 
ATOM   3202 C CB  . LEU B 1 176 ? -2.252  14.503  33.238  1.00 22.97 ? 178 LEU B CB  1 
ATOM   3203 C CG  . LEU B 1 176 ? -1.977  15.995  33.381  1.00 24.72 ? 178 LEU B CG  1 
ATOM   3204 C CD1 . LEU B 1 176 ? -3.192  16.770  32.980  1.00 35.07 ? 178 LEU B CD1 1 
ATOM   3205 C CD2 . LEU B 1 176 ? -1.626  16.255  34.840  1.00 28.33 ? 178 LEU B CD2 1 
ATOM   3206 N N   . ALA B 1 177 ? -0.482  12.055  34.449  1.00 16.08 ? 179 ALA B N   1 
ATOM   3207 C CA  . ALA B 1 177 ? -0.503  10.749  35.104  1.00 16.49 ? 179 ALA B CA  1 
ATOM   3208 C C   . ALA B 1 177 ? -0.998  10.986  36.527  1.00 17.90 ? 179 ALA B C   1 
ATOM   3209 O O   . ALA B 1 177 ? -0.247  11.491  37.366  1.00 15.67 ? 179 ALA B O   1 
ATOM   3210 C CB  . ALA B 1 177 ? 0.878   10.093  35.099  1.00 14.16 ? 179 ALA B CB  1 
ATOM   3211 N N   . ASP B 1 178 ? -2.260  10.637  36.793  1.00 18.00 ? 180 ASP B N   1 
ATOM   3212 C CA  . ASP B 1 178 ? -2.893  10.894  38.084  1.00 18.29 ? 180 ASP B CA  1 
ATOM   3213 C C   . ASP B 1 178 ? -2.624  9.717   39.012  1.00 18.14 ? 180 ASP B C   1 
ATOM   3214 O O   . ASP B 1 178 ? -3.125  8.618   38.773  1.00 20.34 ? 180 ASP B O   1 
ATOM   3215 C CB  . ASP B 1 178 ? -4.388  11.115  37.879  1.00 17.46 ? 180 ASP B CB  1 
ATOM   3216 C CG  . ASP B 1 178 ? -5.056  11.822  39.048  1.00 32.26 ? 180 ASP B CG  1 
ATOM   3217 O OD1 . ASP B 1 178 ? -4.359  12.205  40.019  1.00 31.31 ? 180 ASP B OD1 1 
ATOM   3218 O OD2 . ASP B 1 178 ? -6.306  11.977  38.996  1.00 38.27 ? 180 ASP B OD2 1 
ATOM   3219 N N   . HIS B 1 179 ? -1.828  9.940   40.059  1.00 14.07 ? 181 HIS B N   1 
ATOM   3220 C CA  . HIS B 1 179 ? -1.354  8.875   40.943  1.00 16.72 ? 181 HIS B CA  1 
ATOM   3221 C C   . HIS B 1 179 ? -2.215  8.821   42.199  1.00 19.03 ? 181 HIS B C   1 
ATOM   3222 O O   . HIS B 1 179 ? -2.405  9.844   42.873  1.00 18.44 ? 181 HIS B O   1 
ATOM   3223 C CB  . HIS B 1 179 ? 0.095   9.121   41.367  1.00 13.97 ? 181 HIS B CB  1 
ATOM   3224 C CG  . HIS B 1 179 ? 1.107   8.880   40.287  1.00 14.14 ? 181 HIS B CG  1 
ATOM   3225 N ND1 . HIS B 1 179 ? 1.189   9.665   39.152  1.00 14.86 ? 181 HIS B ND1 1 
ATOM   3226 C CD2 . HIS B 1 179 ? 2.128   7.995   40.208  1.00 14.86 ? 181 HIS B CD2 1 
ATOM   3227 C CE1 . HIS B 1 179 ? 2.182   9.231   38.389  1.00 13.89 ? 181 HIS B CE1 1 
ATOM   3228 N NE2 . HIS B 1 179 ? 2.780   8.229   39.017  1.00 13.47 ? 181 HIS B NE2 1 
ATOM   3229 N N   . TYR B 1 180 ? -2.690  7.625   42.537  1.00 17.05 ? 182 TYR B N   1 
ATOM   3230 C CA  . TYR B 1 180 ? -3.328  7.357   43.819  1.00 18.37 ? 182 TYR B CA  1 
ATOM   3231 C C   . TYR B 1 180 ? -2.506  6.301   44.529  1.00 19.33 ? 182 TYR B C   1 
ATOM   3232 O O   . TYR B 1 180 ? -2.223  5.254   43.942  1.00 20.47 ? 182 TYR B O   1 
ATOM   3233 C CB  . TYR B 1 180 ? -4.772  6.882   43.642  1.00 16.67 ? 182 TYR B CB  1 
ATOM   3234 C CG  . TYR B 1 180 ? -5.636  7.966   43.052  1.00 20.12 ? 182 TYR B CG  1 
ATOM   3235 C CD1 . TYR B 1 180 ? -5.656  8.192   41.683  1.00 22.66 ? 182 TYR B CD1 1 
ATOM   3236 C CD2 . TYR B 1 180 ? -6.377  8.805   43.873  1.00 25.07 ? 182 TYR B CD2 1 
ATOM   3237 C CE1 . TYR B 1 180 ? -6.415  9.208   41.140  1.00 26.12 ? 182 TYR B CE1 1 
ATOM   3238 C CE2 . TYR B 1 180 ? -7.143  9.822   43.343  1.00 30.13 ? 182 TYR B CE2 1 
ATOM   3239 C CZ  . TYR B 1 180 ? -7.158  10.018  41.973  1.00 31.97 ? 182 TYR B CZ  1 
ATOM   3240 O OH  . TYR B 1 180 ? -7.919  11.032  41.423  1.00 36.70 ? 182 TYR B OH  1 
ATOM   3241 N N   . GLN B 1 181 ? -2.132  6.565   45.782  1.00 16.47 ? 183 GLN B N   1 
ATOM   3242 C CA  . GLN B 1 181 ? -1.155  5.731   46.465  1.00 16.60 ? 183 GLN B CA  1 
ATOM   3243 C C   . GLN B 1 181 ? -1.626  5.353   47.858  1.00 19.58 ? 183 GLN B C   1 
ATOM   3244 O O   . GLN B 1 181 ? -2.204  6.179   48.567  1.00 20.82 ? 183 GLN B O   1 
ATOM   3245 C CB  . GLN B 1 181 ? 0.201   6.461   46.543  1.00 15.90 ? 183 GLN B CB  1 
ATOM   3246 C CG  . GLN B 1 181 ? 1.290   5.728   47.340  1.00 13.05 ? 183 GLN B CG  1 
ATOM   3247 C CD  . GLN B 1 181 ? 2.600   6.506   47.355  1.00 17.46 ? 183 GLN B CD  1 
ATOM   3248 O OE1 . GLN B 1 181 ? 2.781   7.447   46.591  1.00 15.30 ? 183 GLN B OE1 1 
ATOM   3249 N NE2 . GLN B 1 181 ? 3.498   6.142   48.255  1.00 18.55 ? 183 GLN B NE2 1 
ATOM   3250 N N   . GLN B 1 182 ? -1.378  4.103   48.256  1.00 19.60 ? 184 GLN B N   1 
ATOM   3251 C CA  . GLN B 1 182 ? -1.464  3.776   49.672  1.00 18.80 ? 184 GLN B CA  1 
ATOM   3252 C C   . GLN B 1 182 ? -0.378  2.785   50.055  1.00 21.73 ? 184 GLN B C   1 
ATOM   3253 O O   . GLN B 1 182 ? -0.016  1.900   49.269  1.00 21.11 ? 184 GLN B O   1 
ATOM   3254 C CB  . GLN B 1 182 ? -2.837  3.220   50.066  1.00 24.17 ? 184 GLN B CB  1 
ATOM   3255 C CG  . GLN B 1 182 ? -3.407  2.126   49.210  1.00 30.50 ? 184 GLN B CG  1 
ATOM   3256 C CD  . GLN B 1 182 ? -4.778  1.683   49.746  1.00 39.37 ? 184 GLN B CD  1 
ATOM   3257 O OE1 . GLN B 1 182 ? -5.823  2.100   49.242  1.00 38.29 ? 184 GLN B OE1 1 
ATOM   3258 N NE2 . GLN B 1 182 ? -4.765  0.888   50.812  1.00 41.17 ? 184 GLN B NE2 1 
ATOM   3259 N N   . ASN B 1 183 ? 0.140   2.945   51.277  1.00 19.93 ? 185 ASN B N   1 
ATOM   3260 C CA  . ASN B 1 183 ? 1.206   2.113   51.817  1.00 18.86 ? 185 ASN B CA  1 
ATOM   3261 C C   . ASN B 1 183 ? 0.758   1.547   53.151  1.00 23.82 ? 185 ASN B C   1 
ATOM   3262 O O   . ASN B 1 183 ? 0.108   2.242   53.941  1.00 22.33 ? 185 ASN B O   1 
ATOM   3263 C CB  . ASN B 1 183 ? 2.503   2.904   52.026  1.00 18.60 ? 185 ASN B CB  1 
ATOM   3264 C CG  . ASN B 1 183 ? 3.125   3.365   50.722  1.00 19.02 ? 185 ASN B CG  1 
ATOM   3265 O OD1 . ASN B 1 183 ? 2.417   3.801   49.824  1.00 23.00 ? 185 ASN B OD1 1 
ATOM   3266 N ND2 . ASN B 1 183 ? 4.459   3.305   50.628  1.00 19.66 ? 185 ASN B ND2 1 
ATOM   3267 N N   . THR B 1 184 ? 1.102   0.284   53.404  1.00 18.28 ? 186 THR B N   1 
ATOM   3268 C CA  . THR B 1 184 ? 0.750   -0.331  54.677  1.00 23.00 ? 186 THR B CA  1 
ATOM   3269 C C   . THR B 1 184 ? 1.945   -1.153  55.132  1.00 24.47 ? 186 THR B C   1 
ATOM   3270 O O   . THR B 1 184 ? 2.567   -1.844  54.313  1.00 22.73 ? 186 THR B O   1 
ATOM   3271 C CB  . THR B 1 184 ? -0.498  -1.234  54.591  1.00 27.14 ? 186 THR B CB  1 
ATOM   3272 O OG1 . THR B 1 184 ? -0.236  -2.319  53.710  1.00 27.32 ? 186 THR B OG1 1 
ATOM   3273 C CG2 . THR B 1 184 ? -1.703  -0.479  54.059  1.00 31.53 ? 186 THR B CG2 1 
ATOM   3274 N N   . PRO B 1 185 ? 2.293   -1.104  56.419  1.00 23.90 ? 187 PRO B N   1 
ATOM   3275 C CA  . PRO B 1 185 ? 3.451   -1.861  56.894  1.00 20.58 ? 187 PRO B CA  1 
ATOM   3276 C C   . PRO B 1 185 ? 3.235   -3.362  56.785  1.00 25.11 ? 187 PRO B C   1 
ATOM   3277 O O   . PRO B 1 185 ? 2.114   -3.869  56.844  1.00 25.45 ? 187 PRO B O   1 
ATOM   3278 C CB  . PRO B 1 185 ? 3.607   -1.418  58.353  1.00 24.56 ? 187 PRO B CB  1 
ATOM   3279 C CG  . PRO B 1 185 ? 2.355   -0.747  58.723  1.00 29.78 ? 187 PRO B CG  1 
ATOM   3280 C CD  . PRO B 1 185 ? 1.587   -0.390  57.491  1.00 29.70 ? 187 PRO B CD  1 
ATOM   3281 N N   . ILE B 1 186 ? 4.339   -4.062  56.555  1.00 22.61 ? 188 ILE B N   1 
ATOM   3282 C CA  . ILE B 1 186 ? 4.356   -5.520  56.507  1.00 22.32 ? 188 ILE B CA  1 
ATOM   3283 C C   . ILE B 1 186 ? 4.495   -6.117  57.901  1.00 27.35 ? 188 ILE B C   1 
ATOM   3284 O O   . ILE B 1 186 ? 3.901   -7.154  58.195  1.00 28.22 ? 188 ILE B O   1 
ATOM   3285 C CB  . ILE B 1 186 ? 5.513   -5.974  55.594  1.00 25.44 ? 188 ILE B CB  1 
ATOM   3286 C CG1 . ILE B 1 186 ? 5.296   -5.499  54.149  1.00 20.21 ? 188 ILE B CG1 1 
ATOM   3287 C CG2 . ILE B 1 186 ? 5.705   -7.502  55.655  1.00 28.07 ? 188 ILE B CG2 1 
ATOM   3288 C CD1 . ILE B 1 186 ? 6.445   -5.889  53.211  1.00 21.57 ? 188 ILE B CD1 1 
ATOM   3289 N N   . GLY B 1 187 ? 5.284   -5.471  58.770  1.00 26.25 ? 189 GLY B N   1 
ATOM   3290 C CA  . GLY B 1 187 ? 5.594   -6.017  60.077  1.00 31.59 ? 189 GLY B CA  1 
ATOM   3291 C C   . GLY B 1 187 ? 4.569   -5.686  61.153  1.00 33.88 ? 189 GLY B C   1 
ATOM   3292 O O   . GLY B 1 187 ? 3.629   -4.926  60.947  1.00 29.52 ? 189 GLY B O   1 
ATOM   3293 N N   . ASP B 1 188 ? 4.765   -6.294  62.329  1.00 36.70 ? 190 ASP B N   1 
ATOM   3294 C CA  . ASP B 1 188 ? 3.871   -6.087  63.462  1.00 40.37 ? 190 ASP B CA  1 
ATOM   3295 C C   . ASP B 1 188 ? 4.346   -4.990  64.409  1.00 42.27 ? 190 ASP B C   1 
ATOM   3296 O O   . ASP B 1 188 ? 3.545   -4.494  65.211  1.00 45.82 ? 190 ASP B O   1 
ATOM   3297 C CB  . ASP B 1 188 ? 3.713   -7.377  64.279  1.00 40.97 ? 190 ASP B CB  1 
ATOM   3298 C CG  . ASP B 1 188 ? 3.689   -8.624  63.418  1.00 39.70 ? 190 ASP B CG  1 
ATOM   3299 O OD1 . ASP B 1 188 ? 2.871   -8.682  62.475  1.00 38.21 ? 190 ASP B OD1 1 
ATOM   3300 O OD2 . ASP B 1 188 ? 4.444   -9.576  63.726  1.00 40.40 ? 190 ASP B OD2 1 
ATOM   3301 N N   . GLY B 1 189 ? 5.627   -4.622  64.349  1.00 44.95 ? 191 GLY B N   1 
ATOM   3302 C CA  . GLY B 1 189 ? 6.205   -3.664  65.260  1.00 46.53 ? 191 GLY B CA  1 
ATOM   3303 C C   . GLY B 1 189 ? 5.574   -2.294  65.148  1.00 47.89 ? 191 GLY B C   1 
ATOM   3304 O O   . GLY B 1 189 ? 4.841   -1.994  64.202  1.00 45.96 ? 191 GLY B O   1 
ATOM   3305 N N   . PRO B 1 190 ? 5.868   -1.419  66.111  1.00 50.20 ? 192 PRO B N   1 
ATOM   3306 C CA  . PRO B 1 190 ? 5.220   -0.100  66.131  1.00 49.22 ? 192 PRO B CA  1 
ATOM   3307 C C   . PRO B 1 190 ? 5.776   0.788   65.027  1.00 49.78 ? 192 PRO B C   1 
ATOM   3308 O O   . PRO B 1 190 ? 6.994   0.958   64.901  1.00 44.84 ? 192 PRO B O   1 
ATOM   3309 C CB  . PRO B 1 190 ? 5.562   0.444   67.527  1.00 44.09 ? 192 PRO B CB  1 
ATOM   3310 C CG  . PRO B 1 190 ? 6.767   -0.391  68.011  1.00 45.65 ? 192 PRO B CG  1 
ATOM   3311 C CD  . PRO B 1 190 ? 7.074   -1.437  66.963  1.00 49.37 ? 192 PRO B CD  1 
ATOM   3312 N N   . VAL B 1 191 ? 4.876   1.352   64.223  1.00 46.56 ? 193 VAL B N   1 
ATOM   3313 C CA  . VAL B 1 191 ? 5.259   2.160   63.071  1.00 46.34 ? 193 VAL B CA  1 
ATOM   3314 C C   . VAL B 1 191 ? 4.623   3.541   63.193  1.00 46.38 ? 193 VAL B C   1 
ATOM   3315 O O   . VAL B 1 191 ? 3.418   3.663   63.450  1.00 46.68 ? 193 VAL B O   1 
ATOM   3316 C CB  . VAL B 1 191 ? 4.869   1.480   61.747  1.00 43.51 ? 193 VAL B CB  1 
ATOM   3317 C CG1 . VAL B 1 191 ? 5.008   2.453   60.613  1.00 40.35 ? 193 VAL B CG1 1 
ATOM   3318 C CG2 . VAL B 1 191 ? 5.746   0.265   61.505  1.00 40.95 ? 193 VAL B CG2 1 
ATOM   3319 N N   . LEU B 1 192 ? 5.442   4.573   62.986  1.00 47.51 ? 194 LEU B N   1 
ATOM   3320 C CA  . LEU B 1 192 ? 5.091   5.982   63.173  1.00 51.65 ? 194 LEU B CA  1 
ATOM   3321 C C   . LEU B 1 192 ? 4.125   6.443   62.085  1.00 49.07 ? 194 LEU B C   1 
ATOM   3322 O O   . LEU B 1 192 ? 4.537   6.676   60.946  1.00 46.43 ? 194 LEU B O   1 
ATOM   3323 C CB  . LEU B 1 192 ? 6.366   6.821   63.132  1.00 49.58 ? 194 LEU B CB  1 
ATOM   3324 C CG  . LEU B 1 192 ? 7.507   6.557   64.127  1.00 54.64 ? 194 LEU B CG  1 
ATOM   3325 C CD1 . LEU B 1 192 ? 8.812   7.213   63.656  1.00 48.11 ? 194 LEU B CD1 1 
ATOM   3326 C CD2 . LEU B 1 192 ? 7.127   7.068   65.511  1.00 56.18 ? 194 LEU B CD2 1 
ATOM   3327 N N   . LEU B 1 193 ? 2.847   6.617   62.428  1.00 47.66 ? 195 LEU B N   1 
ATOM   3328 C CA  . LEU B 1 193 ? 1.931   7.333   61.528  1.00 45.38 ? 195 LEU B CA  1 
ATOM   3329 C C   . LEU B 1 193 ? 2.259   8.818   61.559  1.00 45.34 ? 195 LEU B C   1 
ATOM   3330 O O   . LEU B 1 193 ? 2.071   9.458   62.603  1.00 50.04 ? 195 LEU B O   1 
ATOM   3331 C CB  . LEU B 1 193 ? 0.461   7.129   61.911  1.00 46.02 ? 195 LEU B CB  1 
ATOM   3332 C CG  . LEU B 1 193 ? -0.265  5.800   61.726  1.00 46.81 ? 195 LEU B CG  1 
ATOM   3333 C CD1 . LEU B 1 193 ? -1.507  5.764   62.601  1.00 53.63 ? 195 LEU B CD1 1 
ATOM   3334 C CD2 . LEU B 1 193 ? -0.662  5.671   60.281  1.00 43.23 ? 195 LEU B CD2 1 
ATOM   3335 N N   . PRO B 1 194 ? 2.718   9.411   60.464  1.00 38.48 ? 196 PRO B N   1 
ATOM   3336 C CA  . PRO B 1 194 ? 3.240   10.779  60.524  1.00 42.96 ? 196 PRO B CA  1 
ATOM   3337 C C   . PRO B 1 194 ? 2.120   11.806  60.535  1.00 34.21 ? 196 PRO B C   1 
ATOM   3338 O O   . PRO B 1 194 ? 1.008   11.553  60.070  1.00 40.81 ? 196 PRO B O   1 
ATOM   3339 C CB  . PRO B 1 194 ? 4.043   10.892  59.224  1.00 39.98 ? 196 PRO B CB  1 
ATOM   3340 C CG  . PRO B 1 194 ? 3.236   10.019  58.272  1.00 33.00 ? 196 PRO B CG  1 
ATOM   3341 C CD  . PRO B 1 194 ? 2.844   8.835   59.111  1.00 37.74 ? 196 PRO B CD  1 
ATOM   3342 N N   . ASP B 1 195 ? 2.438   12.996  61.045  1.00 37.28 ? 197 ASP B N   1 
ATOM   3343 C CA  . ASP B 1 195 ? 1.677   14.151  60.601  1.00 36.45 ? 197 ASP B CA  1 
ATOM   3344 C C   . ASP B 1 195 ? 1.945   14.410  59.128  1.00 31.11 ? 197 ASP B C   1 
ATOM   3345 O O   . ASP B 1 195 ? 3.019   14.108  58.598  1.00 30.57 ? 197 ASP B O   1 
ATOM   3346 C CB  . ASP B 1 195 ? 1.965   15.410  61.432  1.00 41.83 ? 197 ASP B CB  1 
ATOM   3347 C CG  . ASP B 1 195 ? 1.604   15.251  62.901  1.00 45.87 ? 197 ASP B CG  1 
ATOM   3348 O OD1 . ASP B 1 195 ? 0.406   15.413  63.225  1.00 47.41 ? 197 ASP B OD1 1 
ATOM   3349 O OD2 . ASP B 1 195 ? 2.489   15.028  63.740  1.00 52.75 ? 197 ASP B OD2 1 
ATOM   3350 N N   . ASN B 1 196 ? 0.940   14.959  58.469  1.00 28.88 ? 198 ASN B N   1 
ATOM   3351 C CA  . ASN B 1 196 ? 0.976   15.100  57.026  1.00 27.72 ? 198 ASN B CA  1 
ATOM   3352 C C   . ASN B 1 196 ? 2.065   16.081  56.606  1.00 27.40 ? 198 ASN B C   1 
ATOM   3353 O O   . ASN B 1 196 ? 2.298   17.100  57.265  1.00 23.74 ? 198 ASN B O   1 
ATOM   3354 C CB  . ASN B 1 196 ? -0.397  15.542  56.551  1.00 25.15 ? 198 ASN B CB  1 
ATOM   3355 C CG  . ASN B 1 196 ? -1.479  14.563  56.965  1.00 26.99 ? 198 ASN B CG  1 
ATOM   3356 O OD1 . ASN B 1 196 ? -1.182  13.487  57.483  1.00 28.90 ? 198 ASN B OD1 1 
ATOM   3357 N ND2 . ASN B 1 196 ? -2.729  14.944  56.784  1.00 29.51 ? 198 ASN B ND2 1 
ATOM   3358 N N   . HIS B 1 197 ? 2.739   15.762  55.498  1.00 24.03 ? 199 HIS B N   1 
ATOM   3359 C CA  . HIS B 1 197 ? 3.904   16.525  55.072  1.00 22.12 ? 199 HIS B CA  1 
ATOM   3360 C C   . HIS B 1 197 ? 4.195   16.222  53.611  1.00 23.60 ? 199 HIS B C   1 
ATOM   3361 O O   . HIS B 1 197 ? 3.727   15.220  53.063  1.00 20.93 ? 199 HIS B O   1 
ATOM   3362 C CB  . HIS B 1 197 ? 5.129   16.184  55.916  1.00 25.95 ? 199 HIS B CB  1 
ATOM   3363 C CG  . HIS B 1 197 ? 5.588   14.766  55.759  1.00 23.47 ? 199 HIS B CG  1 
ATOM   3364 N ND1 . HIS B 1 197 ? 5.010   13.714  56.436  1.00 27.27 ? 199 HIS B ND1 1 
ATOM   3365 C CD2 . HIS B 1 197 ? 6.557   14.226  54.982  1.00 22.86 ? 199 HIS B CD2 1 
ATOM   3366 C CE1 . HIS B 1 197 ? 5.620   12.589  56.104  1.00 27.16 ? 199 HIS B CE1 1 
ATOM   3367 N NE2 . HIS B 1 197 ? 6.564   12.873  55.224  1.00 24.95 ? 199 HIS B NE2 1 
ATOM   3368 N N   . TYR B 1 198 ? 5.009   17.079  52.998  1.00 20.71 ? 200 TYR B N   1 
ATOM   3369 C CA  . TYR B 1 198 ? 5.393   16.901  51.603  1.00 21.60 ? 200 TYR B CA  1 
ATOM   3370 C C   . TYR B 1 198 ? 6.718   16.164  51.465  1.00 23.76 ? 200 TYR B C   1 
ATOM   3371 O O   . TYR B 1 198 ? 7.641   16.351  52.258  1.00 19.64 ? 200 TYR B O   1 
ATOM   3372 C CB  . TYR B 1 198 ? 5.546   18.239  50.906  1.00 21.27 ? 200 TYR B CB  1 
ATOM   3373 C CG  . TYR B 1 198 ? 4.250   18.941  50.639  1.00 22.59 ? 200 TYR B CG  1 
ATOM   3374 C CD1 . TYR B 1 198 ? 3.447   18.564  49.572  1.00 24.00 ? 200 TYR B CD1 1 
ATOM   3375 C CD2 . TYR B 1 198 ? 3.832   19.985  51.451  1.00 23.84 ? 200 TYR B CD2 1 
ATOM   3376 C CE1 . TYR B 1 198 ? 2.272   19.213  49.305  1.00 21.74 ? 200 TYR B CE1 1 
ATOM   3377 C CE2 . TYR B 1 198 ? 2.648   20.642  51.195  1.00 24.41 ? 200 TYR B CE2 1 
ATOM   3378 C CZ  . TYR B 1 198 ? 1.867   20.246  50.126  1.00 29.79 ? 200 TYR B CZ  1 
ATOM   3379 O OH  . TYR B 1 198 ? 0.676   20.903  49.856  1.00 25.93 ? 200 TYR B OH  1 
ATOM   3380 N N   . LEU B 1 199 ? 6.813   15.350  50.417  1.00 20.51 ? 201 LEU B N   1 
ATOM   3381 C CA  . LEU B 1 199 ? 8.091   14.886  49.887  1.00 20.98 ? 201 LEU B CA  1 
ATOM   3382 C C   . LEU B 1 199 ? 8.366   15.638  48.592  1.00 20.90 ? 201 LEU B C   1 
ATOM   3383 O O   . LEU B 1 199 ? 7.475   15.756  47.742  1.00 17.86 ? 201 LEU B O   1 
ATOM   3384 C CB  . LEU B 1 199 ? 8.069   13.377  49.626  1.00 16.53 ? 201 LEU B CB  1 
ATOM   3385 C CG  . LEU B 1 199 ? 7.897   12.463  50.825  1.00 24.26 ? 201 LEU B CG  1 
ATOM   3386 C CD1 . LEU B 1 199 ? 7.862   10.995  50.393  1.00 19.33 ? 201 LEU B CD1 1 
ATOM   3387 C CD2 . LEU B 1 199 ? 9.031   12.734  51.780  1.00 23.87 ? 201 LEU B CD2 1 
ATOM   3388 N N   . PHE B 1 200 ? 9.583   16.154  48.448  1.00 20.11 ? 202 PHE B N   1 
ATOM   3389 C CA  . PHE B 1 200 ? 9.995   16.910  47.268  1.00 21.38 ? 202 PHE B CA  1 
ATOM   3390 C C   . PHE B 1 200 ? 11.094  16.140  46.555  1.00 24.00 ? 202 PHE B C   1 
ATOM   3391 O O   . PHE B 1 200 ? 12.075  15.743  47.189  1.00 21.06 ? 202 PHE B O   1 
ATOM   3392 C CB  . PHE B 1 200 ? 10.516  18.299  47.648  1.00 22.36 ? 202 PHE B CB  1 
ATOM   3393 C CG  . PHE B 1 200 ? 9.506   19.168  48.332  1.00 22.79 ? 202 PHE B CG  1 
ATOM   3394 C CD1 . PHE B 1 200 ? 8.500   19.781  47.617  1.00 24.13 ? 202 PHE B CD1 1 
ATOM   3395 C CD2 . PHE B 1 200 ? 9.574   19.377  49.704  1.00 30.05 ? 202 PHE B CD2 1 
ATOM   3396 C CE1 . PHE B 1 200 ? 7.565   20.581  48.253  1.00 25.15 ? 202 PHE B CE1 1 
ATOM   3397 C CE2 . PHE B 1 200 ? 8.639   20.175  50.346  1.00 31.70 ? 202 PHE B CE2 1 
ATOM   3398 C CZ  . PHE B 1 200 ? 7.632   20.774  49.616  1.00 28.11 ? 202 PHE B CZ  1 
ATOM   3399 N N   . THR B 1 201 ? 10.946  15.956  45.239  1.00 20.47 ? 203 THR B N   1 
ATOM   3400 C CA  . THR B 1 201 ? 11.851  15.107  44.472  1.00 20.09 ? 203 THR B CA  1 
ATOM   3401 C C   . THR B 1 201 ? 12.407  15.882  43.286  1.00 20.82 ? 203 THR B C   1 
ATOM   3402 O O   . THR B 1 201 ? 11.692  16.666  42.671  1.00 18.41 ? 203 THR B O   1 
ATOM   3403 C CB  . THR B 1 201 ? 11.115  13.854  43.978  1.00 18.70 ? 203 THR B CB  1 
ATOM   3404 O OG1 . THR B 1 201 ? 10.599  13.167  45.117  1.00 19.76 ? 203 THR B OG1 1 
ATOM   3405 C CG2 . THR B 1 201 ? 12.077  12.902  43.250  1.00 20.19 ? 203 THR B CG2 1 
ATOM   3406 N N   . THR B 1 202 ? 13.684  15.676  42.971  1.00 19.67 ? 204 THR B N   1 
ATOM   3407 C CA  . THR B 1 202 ? 14.257  16.164  41.720  1.00 17.09 ? 204 THR B CA  1 
ATOM   3408 C C   . THR B 1 202 ? 14.952  15.006  41.015  1.00 21.67 ? 204 THR B C   1 
ATOM   3409 O O   . THR B 1 202 ? 15.945  14.464  41.524  1.00 19.82 ? 204 THR B O   1 
ATOM   3410 C CB  . THR B 1 202 ? 15.228  17.328  41.955  1.00 23.09 ? 204 THR B CB  1 
ATOM   3411 O OG1 . THR B 1 202 ? 16.506  16.818  42.338  1.00 35.18 ? 204 THR B OG1 1 
ATOM   3412 C CG2 . THR B 1 202 ? 14.734  18.225  43.048  1.00 24.21 ? 204 THR B CG2 1 
ATOM   3413 N N   . SER B 1 203 ? 14.432  14.629  39.845  1.00 19.75 ? 205 SER B N   1 
ATOM   3414 C CA  . SER B 1 203 ? 14.894  13.471  39.094  1.00 19.23 ? 205 SER B CA  1 
ATOM   3415 C C   . SER B 1 203 ? 15.568  13.917  37.804  1.00 21.94 ? 205 SER B C   1 
ATOM   3416 O O   . SER B 1 203 ? 15.062  14.800  37.109  1.00 19.38 ? 205 SER B O   1 
ATOM   3417 C CB  . SER B 1 203 ? 13.726  12.540  38.752  1.00 17.91 ? 205 SER B CB  1 
ATOM   3418 O OG  . SER B 1 203 ? 12.876  12.359  39.874  1.00 17.18 ? 205 SER B OG  1 
ATOM   3419 N N   . THR B 1 204 ? 16.703  13.305  37.474  1.00 16.95 ? 206 THR B N   1 
ATOM   3420 C CA  . THR B 1 204 ? 17.325  13.523  36.173  1.00 20.71 ? 206 THR B CA  1 
ATOM   3421 C C   . THR B 1 204 ? 17.584  12.186  35.502  1.00 19.45 ? 206 THR B C   1 
ATOM   3422 O O   . THR B 1 204 ? 18.144  11.271  36.114  1.00 21.26 ? 206 THR B O   1 
ATOM   3423 C CB  . THR B 1 204 ? 18.630  14.336  36.252  1.00 25.54 ? 206 THR B CB  1 
ATOM   3424 O OG1 . THR B 1 204 ? 19.700  13.495  36.689  1.00 35.97 ? 206 THR B OG1 1 
ATOM   3425 C CG2 . THR B 1 204 ? 18.491  15.516  37.176  1.00 20.40 ? 206 THR B CG2 1 
ATOM   3426 N N   . LEU B 1 205 ? 17.160  12.079  34.252  1.00 19.18 ? 207 LEU B N   1 
ATOM   3427 C CA  . LEU B 1 205 ? 17.258  10.849  33.485  1.00 19.44 ? 207 LEU B CA  1 
ATOM   3428 C C   . LEU B 1 205 ? 18.403  10.986  32.495  1.00 21.77 ? 207 LEU B C   1 
ATOM   3429 O O   . LEU B 1 205 ? 18.596  12.052  31.902  1.00 22.81 ? 207 LEU B O   1 
ATOM   3430 C CB  . LEU B 1 205 ? 15.962  10.562  32.720  1.00 21.16 ? 207 LEU B CB  1 
ATOM   3431 C CG  . LEU B 1 205 ? 14.599  10.574  33.423  1.00 23.31 ? 207 LEU B CG  1 
ATOM   3432 C CD1 . LEU B 1 205 ? 13.531  9.939   32.536  1.00 20.62 ? 207 LEU B CD1 1 
ATOM   3433 C CD2 . LEU B 1 205 ? 14.613  9.966   34.795  1.00 23.18 ? 207 LEU B CD2 1 
ATOM   3434 N N   . SER B 1 206 ? 19.162  9.909   32.308  1.00 21.16 ? 208 SER B N   1 
ATOM   3435 C CA  . SER B 1 206 ? 20.278  9.936   31.371  1.00 20.64 ? 208 SER B CA  1 
ATOM   3436 C C   . SER B 1 206 ? 20.477  8.538   30.822  1.00 21.54 ? 208 SER B C   1 
ATOM   3437 O O   . SER B 1 206 ? 19.744  7.606   31.168  1.00 18.10 ? 208 SER B O   1 
ATOM   3438 C CB  . SER B 1 206 ? 21.551  10.463  32.038  1.00 21.48 ? 208 SER B CB  1 
ATOM   3439 O OG  . SER B 1 206 ? 21.909  9.617   33.112  1.00 23.20 ? 208 SER B OG  1 
ATOM   3440 N N   . LYS B 1 207 ? 21.466  8.399   29.941  1.00 18.48 ? 209 LYS B N   1 
ATOM   3441 C CA  . LYS B 1 207 ? 21.799  7.118   29.346  1.00 18.98 ? 209 LYS B CA  1 
ATOM   3442 C C   . LYS B 1 207 ? 23.249  6.772   29.664  1.00 24.35 ? 209 LYS B C   1 
ATOM   3443 O O   . LYS B 1 207 ? 24.085  7.655   29.885  1.00 24.25 ? 209 LYS B O   1 
ATOM   3444 C CB  . LYS B 1 207 ? 21.580  7.119   27.823  1.00 21.93 ? 209 LYS B CB  1 
ATOM   3445 C CG  . LYS B 1 207 ? 20.128  7.378   27.420  1.00 18.65 ? 209 LYS B CG  1 
ATOM   3446 C CD  . LYS B 1 207 ? 19.255  6.165   27.684  1.00 18.37 ? 209 LYS B CD  1 
ATOM   3447 C CE  . LYS B 1 207 ? 17.837  6.358   27.109  1.00 20.90 ? 209 LYS B CE  1 
ATOM   3448 N NZ  . LYS B 1 207 ? 16.979  5.167   27.424  1.00 18.38 ? 209 LYS B NZ  1 
ATOM   3449 N N   . ASP B 1 208 ? 23.524  5.474   29.690  1.00 21.64 ? 210 ASP B N   1 
ATOM   3450 C CA  . ASP B 1 208 ? 24.871  4.966   29.874  1.00 24.46 ? 210 ASP B CA  1 
ATOM   3451 C C   . ASP B 1 208 ? 25.455  4.686   28.497  1.00 23.89 ? 210 ASP B C   1 
ATOM   3452 O O   . ASP B 1 208 ? 24.936  3.813   27.779  1.00 22.97 ? 210 ASP B O   1 
ATOM   3453 C CB  . ASP B 1 208 ? 24.844  3.725   30.751  1.00 25.74 ? 210 ASP B CB  1 
ATOM   3454 C CG  . ASP B 1 208 ? 26.155  2.974   30.774  1.00 30.72 ? 210 ASP B CG  1 
ATOM   3455 O OD1 . ASP B 1 208 ? 27.209  3.516   30.357  1.00 28.69 ? 210 ASP B OD1 1 
ATOM   3456 O OD2 . ASP B 1 208 ? 26.135  1.862   31.337  1.00 27.27 ? 210 ASP B OD2 1 
ATOM   3457 N N   . PRO B 1 209 ? 26.476  5.428   28.066  1.00 24.74 ? 211 PRO B N   1 
ATOM   3458 C CA  . PRO B 1 209 ? 26.947  5.305   26.674  1.00 28.29 ? 211 PRO B CA  1 
ATOM   3459 C C   . PRO B 1 209 ? 27.491  3.933   26.351  1.00 28.70 ? 211 PRO B C   1 
ATOM   3460 O O   . PRO B 1 209 ? 27.693  3.620   25.172  1.00 29.35 ? 211 PRO B O   1 
ATOM   3461 C CB  . PRO B 1 209 ? 28.061  6.354   26.571  1.00 27.58 ? 211 PRO B CB  1 
ATOM   3462 C CG  . PRO B 1 209 ? 28.099  7.073   27.859  1.00 30.14 ? 211 PRO B CG  1 
ATOM   3463 C CD  . PRO B 1 209 ? 27.054  6.577   28.779  1.00 26.09 ? 211 PRO B CD  1 
ATOM   3464 N N   . ASN B 1 210 ? 27.731  3.093   27.352  1.00 27.88 ? 212 ASN B N   1 
ATOM   3465 C CA  . ASN B 1 210 ? 28.335  1.790   27.135  1.00 28.50 ? 212 ASN B CA  1 
ATOM   3466 C C   . ASN B 1 210 ? 27.327  0.665   27.321  1.00 30.08 ? 212 ASN B C   1 
ATOM   3467 O O   . ASN B 1 210 ? 27.705  -0.513  27.290  1.00 34.85 ? 212 ASN B O   1 
ATOM   3468 C CB  . ASN B 1 210 ? 29.529  1.650   28.077  1.00 31.65 ? 212 ASN B CB  1 
ATOM   3469 C CG  . ASN B 1 210 ? 30.705  2.523   27.643  1.00 30.95 ? 212 ASN B CG  1 
ATOM   3470 O OD1 . ASN B 1 210 ? 31.121  3.428   28.370  1.00 30.34 ? 212 ASN B OD1 1 
ATOM   3471 N ND2 . ASN B 1 210 ? 31.218  2.276   26.447  1.00 35.52 ? 212 ASN B ND2 1 
ATOM   3472 N N   . GLU B 1 211 ? 26.042  1.000   27.488  1.00 26.84 ? 213 GLU B N   1 
ATOM   3473 C CA  . GLU B 1 211 ? 24.984  0.016   27.697  1.00 23.70 ? 213 GLU B CA  1 
ATOM   3474 C C   . GLU B 1 211 ? 24.222  -0.165  26.392  1.00 23.73 ? 213 GLU B C   1 
ATOM   3475 O O   . GLU B 1 211 ? 23.661  0.801   25.867  1.00 26.32 ? 213 GLU B O   1 
ATOM   3476 C CB  . GLU B 1 211 ? 24.015  0.484   28.779  1.00 25.18 ? 213 GLU B CB  1 
ATOM   3477 C CG  . GLU B 1 211 ? 22.867  -0.471  29.001  1.00 24.10 ? 213 GLU B CG  1 
ATOM   3478 C CD  . GLU B 1 211 ? 23.372  -1.852  29.341  1.00 26.97 ? 213 GLU B CD  1 
ATOM   3479 O OE1 . GLU B 1 211 ? 23.904  -2.018  30.453  1.00 27.47 ? 213 GLU B OE1 1 
ATOM   3480 O OE2 . GLU B 1 211 ? 23.230  -2.776  28.523  1.00 25.54 ? 213 GLU B OE2 1 
ATOM   3481 N N   . LYS B 1 212 ? 24.167  -1.393  25.890  1.00 29.08 ? 214 LYS B N   1 
ATOM   3482 C CA  . LYS B 1 212 ? 23.458  -1.656  24.644  1.00 33.24 ? 214 LYS B CA  1 
ATOM   3483 C C   . LYS B 1 212 ? 22.002  -2.064  24.849  1.00 30.31 ? 214 LYS B C   1 
ATOM   3484 O O   . LYS B 1 212 ? 21.202  -1.956  23.907  1.00 29.59 ? 214 LYS B O   1 
ATOM   3485 C CB  . LYS B 1 212 ? 24.185  -2.743  23.846  1.00 35.38 ? 214 LYS B CB  1 
ATOM   3486 C CG  . LYS B 1 212 ? 25.314  -2.195  22.982  1.00 35.19 ? 214 LYS B CG  1 
ATOM   3487 C CD  . LYS B 1 212 ? 25.845  -3.252  22.018  1.00 42.99 ? 214 LYS B CD  1 
ATOM   3488 C CE  . LYS B 1 212 ? 26.637  -4.351  22.730  1.00 42.76 ? 214 LYS B CE  1 
ATOM   3489 N NZ  . LYS B 1 212 ? 28.069  -4.385  22.278  1.00 47.97 ? 214 LYS B NZ  1 
ATOM   3490 N N   . ARG B 1 213 ? 21.638  -2.550  26.031  1.00 29.67 ? 215 ARG B N   1 
ATOM   3491 C CA  . ARG B 1 213 ? 20.238  -2.869  26.258  1.00 25.30 ? 215 ARG B CA  1 
ATOM   3492 C C   . ARG B 1 213 ? 19.438  -1.586  26.478  1.00 23.09 ? 215 ARG B C   1 
ATOM   3493 O O   . ARG B 1 213 ? 19.990  -0.505  26.700  1.00 23.65 ? 215 ARG B O   1 
ATOM   3494 C CB  . ARG B 1 213 ? 20.069  -3.823  27.447  1.00 26.42 ? 215 ARG B CB  1 
ATOM   3495 C CG  . ARG B 1 213 ? 20.977  -5.079  27.411  1.00 30.17 ? 215 ARG B CG  1 
ATOM   3496 C CD  . ARG B 1 213 ? 20.976  -5.780  28.774  1.00 29.16 ? 215 ARG B CD  1 
ATOM   3497 N NE  . ARG B 1 213 ? 21.989  -5.167  29.628  1.00 30.70 ? 215 ARG B NE  1 
ATOM   3498 C CZ  . ARG B 1 213 ? 22.361  -5.608  30.826  1.00 31.99 ? 215 ARG B CZ  1 
ATOM   3499 N NH1 . ARG B 1 213 ? 21.822  -6.687  31.366  1.00 28.22 ? 215 ARG B NH1 1 
ATOM   3500 N NH2 . ARG B 1 213 ? 23.264  -4.916  31.518  1.00 30.99 ? 215 ARG B NH2 1 
ATOM   3501 N N   . ASP B 1 214 ? 18.120  -1.718  26.374  1.00 22.05 ? 216 ASP B N   1 
ATOM   3502 C CA  . ASP B 1 214 ? 17.212  -0.614  26.656  1.00 19.18 ? 216 ASP B CA  1 
ATOM   3503 C C   . ASP B 1 214 ? 17.282  -0.313  28.142  1.00 19.37 ? 216 ASP B C   1 
ATOM   3504 O O   . ASP B 1 214 ? 17.150  -1.225  28.961  1.00 19.12 ? 216 ASP B O   1 
ATOM   3505 C CB  . ASP B 1 214 ? 15.795  -1.016  26.241  1.00 21.08 ? 216 ASP B CB  1 
ATOM   3506 C CG  . ASP B 1 214 ? 14.858  0.171   26.016  1.00 22.93 ? 216 ASP B CG  1 
ATOM   3507 O OD1 . ASP B 1 214 ? 15.246  1.324   26.272  1.00 20.63 ? 216 ASP B OD1 1 
ATOM   3508 O OD2 . ASP B 1 214 ? 13.723  -0.070  25.527  1.00 22.61 ? 216 ASP B OD2 1 
ATOM   3509 N N   . HIS B 1 215 ? 17.496  0.947   28.503  1.00 20.93 ? 217 HIS B N   1 
ATOM   3510 C CA  . HIS B 1 215 ? 17.835  1.221   29.894  1.00 18.14 ? 217 HIS B CA  1 
ATOM   3511 C C   . HIS B 1 215 ? 17.544  2.671   30.275  1.00 18.90 ? 217 HIS B C   1 
ATOM   3512 O O   . HIS B 1 215 ? 17.288  3.526   29.435  1.00 18.45 ? 217 HIS B O   1 
ATOM   3513 C CB  . HIS B 1 215 ? 19.304  0.891   30.141  1.00 18.86 ? 217 HIS B CB  1 
ATOM   3514 C CG  . HIS B 1 215 ? 20.226  1.902   29.556  1.00 19.72 ? 217 HIS B CG  1 
ATOM   3515 N ND1 . HIS B 1 215 ? 20.482  1.965   28.203  1.00 17.95 ? 217 HIS B ND1 1 
ATOM   3516 C CD2 . HIS B 1 215 ? 20.886  2.941   30.117  1.00 20.36 ? 217 HIS B CD2 1 
ATOM   3517 C CE1 . HIS B 1 215 ? 21.303  2.972   27.964  1.00 19.95 ? 217 HIS B CE1 1 
ATOM   3518 N NE2 . HIS B 1 215 ? 21.551  3.586   29.106  1.00 21.27 ? 217 HIS B NE2 1 
ATOM   3519 N N   . MET B 1 216 ? 17.598  2.923   31.578  1.00 16.16 ? 218 MET B N   1 
ATOM   3520 C CA  . MET B 1 216 ? 17.432  4.226   32.218  1.00 16.80 ? 218 MET B CA  1 
ATOM   3521 C C   . MET B 1 216 ? 18.462  4.398   33.309  1.00 16.57 ? 218 MET B C   1 
ATOM   3522 O O   . MET B 1 216 ? 18.462  3.615   34.259  1.00 18.51 ? 218 MET B O   1 
ATOM   3523 C CB  . MET B 1 216 ? 16.056  4.374   32.880  1.00 17.92 ? 218 MET B CB  1 
ATOM   3524 C CG  . MET B 1 216 ? 15.797  5.772   33.446  1.00 17.47 ? 218 MET B CG  1 
ATOM   3525 S SD  . MET B 1 216 ? 14.106  6.228   33.774  1.00 15.95 ? 218 MET B SD  1 
ATOM   3526 C CE  . MET B 1 216 ? 13.665  5.013   35.022  1.00 14.49 ? 218 MET B CE  1 
ATOM   3527 N N   . VAL B 1 217 ? 19.278  5.446   33.236  1.00 15.90 ? 219 VAL B N   1 
ATOM   3528 C CA  . VAL B 1 217 ? 20.054  5.886   34.394  1.00 16.66 ? 219 VAL B CA  1 
ATOM   3529 C C   . VAL B 1 217 ? 19.280  7.000   35.090  1.00 18.06 ? 219 VAL B C   1 
ATOM   3530 O O   . VAL B 1 217 ? 18.777  7.918   34.434  1.00 18.96 ? 219 VAL B O   1 
ATOM   3531 C CB  . VAL B 1 217 ? 21.459  6.370   33.989  1.00 19.81 ? 219 VAL B CB  1 
ATOM   3532 C CG1 . VAL B 1 217 ? 22.242  6.842   35.233  1.00 19.42 ? 219 VAL B CG1 1 
ATOM   3533 C CG2 . VAL B 1 217 ? 22.179  5.291   33.290  1.00 17.68 ? 219 VAL B CG2 1 
ATOM   3534 N N   . LEU B 1 218 ? 19.196  6.933   36.418  1.00 17.55 ? 220 LEU B N   1 
ATOM   3535 C CA  . LEU B 1 218 ? 18.308  7.805   37.167  1.00 12.75 ? 220 LEU B CA  1 
ATOM   3536 C C   . LEU B 1 218 ? 19.069  8.348   38.366  1.00 17.75 ? 220 LEU B C   1 
ATOM   3537 O O   . LEU B 1 218 ? 19.627  7.580   39.157  1.00 19.03 ? 220 LEU B O   1 
ATOM   3538 C CB  . LEU B 1 218 ? 17.047  7.043   37.608  1.00 13.81 ? 220 LEU B CB  1 
ATOM   3539 C CG  . LEU B 1 218 ? 16.224  7.831   38.609  1.00 17.79 ? 220 LEU B CG  1 
ATOM   3540 C CD1 . LEU B 1 218 ? 15.716  9.039   37.880  1.00 19.96 ? 220 LEU B CD1 1 
ATOM   3541 C CD2 . LEU B 1 218 ? 15.039  6.999   39.072  1.00 21.68 ? 220 LEU B CD2 1 
ATOM   3542 N N   . LEU B 1 219 ? 19.103  9.662   38.482  1.00 18.09 ? 221 LEU B N   1 
ATOM   3543 C CA  . LEU B 1 219 ? 19.598  10.357  39.660  1.00 18.93 ? 221 LEU B CA  1 
ATOM   3544 C C   . LEU B 1 219 ? 18.438  11.075  40.326  1.00 19.77 ? 221 LEU B C   1 
ATOM   3545 O O   . LEU B 1 219 ? 17.626  11.717  39.656  1.00 19.65 ? 221 LEU B O   1 
ATOM   3546 C CB  . LEU B 1 219 ? 20.707  11.352  39.291  1.00 21.89 ? 221 LEU B CB  1 
ATOM   3547 C CG  . LEU B 1 219 ? 21.167  12.315  40.394  1.00 21.94 ? 221 LEU B CG  1 
ATOM   3548 C CD1 . LEU B 1 219 ? 22.057  11.610  41.384  1.00 25.24 ? 221 LEU B CD1 1 
ATOM   3549 C CD2 . LEU B 1 219 ? 21.920  13.473  39.761  1.00 26.07 ? 221 LEU B CD2 1 
ATOM   3550 N N   . GLU B 1 220 ? 18.372  10.969  41.646  1.00 17.68 ? 222 GLU B N   1 
ATOM   3551 C CA  . GLU B 1 220 ? 17.267  11.539  42.388  1.00 19.87 ? 222 GLU B CA  1 
ATOM   3552 C C   . GLU B 1 220 ? 17.701  12.073  43.733  1.00 20.13 ? 222 GLU B C   1 
ATOM   3553 O O   . GLU B 1 220 ? 18.496  11.438  44.424  1.00 21.26 ? 222 GLU B O   1 
ATOM   3554 C CB  . GLU B 1 220 ? 16.198  10.471  42.549  1.00 20.50 ? 222 GLU B CB  1 
ATOM   3555 C CG  . GLU B 1 220 ? 14.882  10.906  42.109  1.00 24.28 ? 222 GLU B CG  1 
ATOM   3556 C CD  . GLU B 1 220 ? 13.936  9.747   42.026  1.00 25.08 ? 222 GLU B CD  1 
ATOM   3557 O OE1 . GLU B 1 220 ? 13.441  9.291   43.054  1.00 23.19 ? 222 GLU B OE1 1 
ATOM   3558 O OE2 . GLU B 1 220 ? 13.588  9.404   40.885  1.00 32.90 ? 222 GLU B OE2 1 
ATOM   3559 N N   . PHE B 1 221 ? 17.140  13.230  44.101  1.00 19.42 ? 223 PHE B N   1 
ATOM   3560 C CA  . PHE B 1 221 ? 17.213  13.761  45.458  1.00 19.81 ? 223 PHE B CA  1 
ATOM   3561 C C   . PHE B 1 221 ? 15.810  13.943  46.007  1.00 20.97 ? 223 PHE B C   1 
ATOM   3562 O O   . PHE B 1 221 ? 14.954  14.517  45.335  1.00 20.89 ? 223 PHE B O   1 
ATOM   3563 C CB  . PHE B 1 221 ? 17.981  15.088  45.508  1.00 24.06 ? 223 PHE B CB  1 
ATOM   3564 C CG  . PHE B 1 221 ? 19.416  14.958  45.105  1.00 24.44 ? 223 PHE B CG  1 
ATOM   3565 C CD1 . PHE B 1 221 ? 19.788  15.014  43.780  1.00 27.95 ? 223 PHE B CD1 1 
ATOM   3566 C CD2 . PHE B 1 221 ? 20.391  14.760  46.070  1.00 23.71 ? 223 PHE B CD2 1 
ATOM   3567 C CE1 . PHE B 1 221 ? 21.108  14.889  43.419  1.00 25.00 ? 223 PHE B CE1 1 
ATOM   3568 C CE2 . PHE B 1 221 ? 21.715  14.631  45.714  1.00 26.75 ? 223 PHE B CE2 1 
ATOM   3569 C CZ  . PHE B 1 221 ? 22.069  14.702  44.380  1.00 29.00 ? 223 PHE B CZ  1 
ATOM   3570 N N   . VAL B 1 222 ? 15.574  13.439  47.217  1.00 20.16 ? 224 VAL B N   1 
ATOM   3571 C CA  . VAL B 1 222 ? 14.274  13.515  47.870  1.00 21.42 ? 224 VAL B CA  1 
ATOM   3572 C C   . VAL B 1 222 ? 14.456  14.123  49.249  1.00 23.94 ? 224 VAL B C   1 
ATOM   3573 O O   . VAL B 1 222 ? 15.340  13.701  50.005  1.00 23.39 ? 224 VAL B O   1 
ATOM   3574 C CB  . VAL B 1 222 ? 13.599  12.134  47.988  1.00 21.74 ? 224 VAL B CB  1 
ATOM   3575 C CG1 . VAL B 1 222 ? 12.135  12.315  48.368  1.00 24.32 ? 224 VAL B CG1 1 
ATOM   3576 C CG2 . VAL B 1 222 ? 13.698  11.381  46.655  1.00 21.56 ? 224 VAL B CG2 1 
ATOM   3577 N N   . THR B 1 223 ? 13.606  15.091  49.585  1.00 22.90 ? 225 THR B N   1 
ATOM   3578 C CA  . THR B 1 223 ? 13.659  15.754  50.878  1.00 25.44 ? 225 THR B CA  1 
ATOM   3579 C C   . THR B 1 223 ? 12.233  15.988  51.356  1.00 22.96 ? 225 THR B C   1 
ATOM   3580 O O   . THR B 1 223 ? 11.320  16.159  50.553  1.00 26.84 ? 225 THR B O   1 
ATOM   3581 C CB  . THR B 1 223 ? 14.442  17.076  50.794  1.00 28.32 ? 225 THR B CB  1 
ATOM   3582 O OG1 . THR B 1 223 ? 14.817  17.503  52.110  1.00 38.62 ? 225 THR B OG1 1 
ATOM   3583 C CG2 . THR B 1 223 ? 13.597  18.153  50.150  1.00 28.54 ? 225 THR B CG2 1 
ATOM   3584 N N   . ALA B 1 224 ? 12.041  15.955  52.665  1.00 24.77 ? 226 ALA B N   1 
ATOM   3585 C CA  . ALA B 1 224 ? 10.738  16.187  53.269  1.00 25.22 ? 226 ALA B CA  1 
ATOM   3586 C C   . ALA B 1 224 ? 10.674  17.596  53.845  1.00 32.96 ? 226 ALA B C   1 
ATOM   3587 O O   . ALA B 1 224 ? 11.694  18.161  54.245  1.00 35.26 ? 226 ALA B O   1 
ATOM   3588 C CB  . ALA B 1 224 ? 10.459  15.151  54.364  1.00 30.83 ? 226 ALA B CB  1 
ATOM   3589 N N   . ASP B 1 225 ? 9.470   18.177  53.849  1.00 33.21 ? 227 ASP B N   1 
ATOM   3590 C CA  . ASP B 1 225 ? 9.257   19.464  54.517  1.00 35.47 ? 227 ASP B CA  1 
ATOM   3591 C C   . ASP B 1 225 ? 7.766   19.805  54.665  1.00 39.20 ? 227 ASP B C   1 
ATOM   3592 O O   . ASP B 1 225 ? 6.879   18.997  54.351  1.00 36.24 ? 227 ASP B O   1 
ATOM   3593 C CB  . ASP B 1 225 ? 9.969   20.594  53.761  1.00 40.33 ? 227 ASP B CB  1 
ATOM   3594 C CG  . ASP B 1 225 ? 9.766   21.960  54.413  1.00 48.03 ? 227 ASP B CG  1 
ATOM   3595 O OD1 . ASP B 1 225 ? 9.719   22.034  55.663  1.00 49.45 ? 227 ASP B OD1 1 
ATOM   3596 O OD2 . ASP B 1 225 ? 9.650   22.961  53.675  1.00 53.24 ? 227 ASP B OD2 1 
HETATM 3597 O O   . HOH C 2 .   ? -7.325  14.690  16.113  1.00 26.62 ? 301 HOH A O   1 
HETATM 3598 O O   . HOH C 2 .   ? -11.445 22.607  -12.636 1.00 37.34 ? 302 HOH A O   1 
HETATM 3599 O O   . HOH C 2 .   ? -23.875 23.407  -4.847  1.00 34.61 ? 303 HOH A O   1 
HETATM 3600 O O   . HOH C 2 .   ? -21.393 41.315  -1.508  1.00 36.35 ? 304 HOH A O   1 
HETATM 3601 O O   . HOH C 2 .   ? -4.028  16.491  3.906   1.00 46.37 ? 305 HOH A O   1 
HETATM 3602 O O   . HOH C 2 .   ? -13.163 25.904  -14.398 1.00 46.90 ? 306 HOH A O   1 
HETATM 3603 O O   . HOH C 2 .   ? -22.052 35.343  13.636  1.00 30.89 ? 307 HOH A O   1 
HETATM 3604 O O   . HOH C 2 .   ? -24.906 29.310  23.270  1.00 37.14 ? 308 HOH A O   1 
HETATM 3605 O O   . HOH C 2 .   ? -10.764 14.578  13.186  1.00 40.33 ? 309 HOH A O   1 
HETATM 3606 O O   . HOH C 2 .   ? -7.308  18.004  25.546  1.00 33.73 ? 310 HOH A O   1 
HETATM 3607 O O   . HOH C 2 .   ? -9.310  28.943  0.445   1.00 21.20 ? 311 HOH A O   1 
HETATM 3608 O O   . HOH C 2 .   ? 3.874   38.367  7.328   1.00 47.40 ? 312 HOH A O   1 
HETATM 3609 O O   . HOH C 2 .   ? -6.647  29.436  11.477  1.00 14.54 ? 313 HOH A O   1 
HETATM 3610 O O   . HOH C 2 .   ? -10.417 45.452  13.396  1.00 36.76 ? 314 HOH A O   1 
HETATM 3611 O O   . HOH C 2 .   ? -2.035  13.527  23.505  1.00 37.13 ? 315 HOH A O   1 
HETATM 3612 O O   . HOH C 2 .   ? -17.670 38.643  18.817  1.00 34.16 ? 316 HOH A O   1 
HETATM 3613 O O   . HOH C 2 .   ? -11.290 30.544  24.728  1.00 32.12 ? 317 HOH A O   1 
HETATM 3614 O O   . HOH C 2 .   ? -26.772 26.580  -5.924  1.00 49.07 ? 318 HOH A O   1 
HETATM 3615 O O   . HOH C 2 .   ? -17.300 45.954  -2.527  1.00 38.95 ? 319 HOH A O   1 
HETATM 3616 O O   . HOH C 2 .   ? -13.929 17.159  -6.440  1.00 35.00 ? 320 HOH A O   1 
HETATM 3617 O O   . HOH C 2 .   ? 3.744   36.287  -8.600  1.00 37.72 ? 321 HOH A O   1 
HETATM 3618 O O   . HOH C 2 .   ? -4.824  24.653  5.389   1.00 17.95 ? 322 HOH A O   1 
HETATM 3619 O O   . HOH C 2 .   ? -9.422  37.345  17.188  1.00 22.74 ? 323 HOH A O   1 
HETATM 3620 O O   . HOH C 2 .   ? 0.400   14.437  15.713  1.00 35.27 ? 324 HOH A O   1 
HETATM 3621 O O   . HOH C 2 .   ? -0.826  39.795  2.326   1.00 25.04 ? 325 HOH A O   1 
HETATM 3622 O O   . HOH C 2 .   ? -5.090  32.947  13.401  1.00 19.37 ? 326 HOH A O   1 
HETATM 3623 O O   . HOH C 2 .   ? -8.917  37.381  20.036  1.00 26.50 ? 327 HOH A O   1 
HETATM 3624 O O   . HOH C 2 .   ? -13.026 32.930  -5.317  1.00 27.89 ? 328 HOH A O   1 
HETATM 3625 O O   . HOH C 2 .   ? -21.506 38.718  17.401  1.00 44.90 ? 329 HOH A O   1 
HETATM 3626 O O   . HOH C 2 .   ? 7.911   31.049  19.664  1.00 28.45 ? 330 HOH A O   1 
HETATM 3627 O O   . HOH C 2 .   ? -30.794 28.771  17.298  1.00 40.91 ? 331 HOH A O   1 
HETATM 3628 O O   . HOH C 2 .   ? -10.825 44.751  17.911  1.00 40.42 ? 332 HOH A O   1 
HETATM 3629 O O   . HOH C 2 .   ? -7.180  34.044  -7.665  1.00 31.11 ? 333 HOH A O   1 
HETATM 3630 O O   . HOH C 2 .   ? -0.522  29.239  24.236  1.00 25.45 ? 334 HOH A O   1 
HETATM 3631 O O   . HOH C 2 .   ? 0.811   15.209  20.040  1.00 23.66 ? 335 HOH A O   1 
HETATM 3632 O O   . HOH C 2 .   ? -9.519  40.366  17.863  1.00 26.77 ? 336 HOH A O   1 
HETATM 3633 O O   . HOH C 2 .   ? -9.467  32.841  24.458  1.00 26.68 ? 337 HOH A O   1 
HETATM 3634 O O   . HOH C 2 .   ? -18.401 20.632  23.052  1.00 37.82 ? 338 HOH A O   1 
HETATM 3635 O O   . HOH C 2 .   ? -11.584 18.206  22.349  1.00 34.53 ? 339 HOH A O   1 
HETATM 3636 O O   . HOH C 2 .   ? -8.872  38.644  3.420   1.00 21.65 ? 340 HOH A O   1 
HETATM 3637 O O   . HOH C 2 .   ? -8.861  25.283  3.245   1.00 18.23 ? 341 HOH A O   1 
HETATM 3638 O O   . HOH C 2 .   ? -15.797 30.824  22.896  1.00 28.60 ? 342 HOH A O   1 
HETATM 3639 O O   . HOH C 2 .   ? 1.119   33.407  24.002  1.00 31.26 ? 343 HOH A O   1 
HETATM 3640 O O   . HOH C 2 .   ? -7.576  33.096  12.354  1.00 19.13 ? 344 HOH A O   1 
HETATM 3641 O O   . HOH C 2 .   ? -8.377  38.657  14.578  1.00 24.93 ? 345 HOH A O   1 
HETATM 3642 O O   . HOH C 2 .   ? 6.217   24.862  8.531   1.00 38.94 ? 346 HOH A O   1 
HETATM 3643 O O   . HOH C 2 .   ? -18.926 27.820  22.668  1.00 29.98 ? 347 HOH A O   1 
HETATM 3644 O O   . HOH C 2 .   ? -6.859  44.026  22.936  1.00 36.24 ? 348 HOH A O   1 
HETATM 3645 O O   . HOH C 2 .   ? -11.421 35.251  3.025   1.00 24.66 ? 349 HOH A O   1 
HETATM 3646 O O   . HOH C 2 .   ? -5.708  41.207  11.689  1.00 23.69 ? 350 HOH A O   1 
HETATM 3647 O O   . HOH C 2 .   ? -17.072 39.153  15.920  1.00 31.47 ? 351 HOH A O   1 
HETATM 3648 O O   . HOH C 2 .   ? -15.372 34.704  -10.131 1.00 41.49 ? 352 HOH A O   1 
HETATM 3649 O O   . HOH C 2 .   ? 1.223   37.842  0.052   1.00 24.09 ? 353 HOH A O   1 
HETATM 3650 O O   . HOH C 2 .   ? 4.160   35.717  14.709  1.00 44.07 ? 354 HOH A O   1 
HETATM 3651 O O   . HOH C 2 .   ? -6.227  44.647  6.002   1.00 34.43 ? 355 HOH A O   1 
HETATM 3652 O O   . HOH C 2 .   ? -3.610  16.011  -2.388  1.00 41.69 ? 356 HOH A O   1 
HETATM 3653 O O   . HOH C 2 .   ? 1.528   18.506  18.743  1.00 22.22 ? 357 HOH A O   1 
HETATM 3654 O O   . HOH C 2 .   ? -26.424 33.657  21.382  1.00 44.25 ? 358 HOH A O   1 
HETATM 3655 O O   . HOH C 2 .   ? -2.064  43.106  -10.547 1.00 32.86 ? 359 HOH A O   1 
HETATM 3656 O O   . HOH C 2 .   ? -4.624  27.644  7.779   1.00 17.05 ? 360 HOH A O   1 
HETATM 3657 O O   . HOH C 2 .   ? -7.736  21.575  -9.921  1.00 29.72 ? 361 HOH A O   1 
HETATM 3658 O O   . HOH C 2 .   ? -21.258 16.244  19.125  1.00 43.85 ? 362 HOH A O   1 
HETATM 3659 O O   . HOH C 2 .   ? -1.867  17.792  25.992  1.00 35.35 ? 363 HOH A O   1 
HETATM 3660 O O   . HOH C 2 .   ? 4.020   14.636  17.292  1.00 36.00 ? 364 HOH A O   1 
HETATM 3661 O O   . HOH C 2 .   ? -12.567 42.821  11.397  1.00 34.15 ? 365 HOH A O   1 
HETATM 3662 O O   . HOH C 2 .   ? 1.756   20.731  4.678   1.00 30.55 ? 366 HOH A O   1 
HETATM 3663 O O   . HOH C 2 .   ? -12.718 31.840  3.214   1.00 23.95 ? 367 HOH A O   1 
HETATM 3664 O O   . HOH C 2 .   ? 6.803   28.409  16.550  1.00 30.01 ? 368 HOH A O   1 
HETATM 3665 O O   . HOH C 2 .   ? -3.923  15.730  -7.078  1.00 42.12 ? 369 HOH A O   1 
HETATM 3666 O O   . HOH C 2 .   ? 9.519   38.985  21.730  1.00 46.81 ? 370 HOH A O   1 
HETATM 3667 O O   . HOH C 2 .   ? -12.988 43.604  16.140  1.00 47.95 ? 371 HOH A O   1 
HETATM 3668 O O   . HOH C 2 .   ? -7.254  26.155  5.228   1.00 17.85 ? 372 HOH A O   1 
HETATM 3669 O O   . HOH C 2 .   ? 5.587   30.995  16.244  1.00 26.19 ? 373 HOH A O   1 
HETATM 3670 O O   . HOH C 2 .   ? -9.818  14.361  17.335  1.00 28.20 ? 374 HOH A O   1 
HETATM 3671 O O   . HOH C 2 .   ? -6.861  45.296  9.918   1.00 53.52 ? 375 HOH A O   1 
HETATM 3672 O O   . HOH C 2 .   ? -9.776  42.403  5.063   1.00 31.08 ? 376 HOH A O   1 
HETATM 3673 O O   . HOH C 2 .   ? -8.984  35.793  2.391   1.00 20.94 ? 377 HOH A O   1 
HETATM 3674 O O   . HOH C 2 .   ? -0.618  45.091  -7.281  1.00 35.21 ? 378 HOH A O   1 
HETATM 3675 O O   . HOH C 2 .   ? -16.621 44.628  -12.321 1.00 48.29 ? 379 HOH A O   1 
HETATM 3676 O O   . HOH C 2 .   ? 0.643   40.052  -11.339 1.00 34.74 ? 380 HOH A O   1 
HETATM 3677 O O   . HOH C 2 .   ? 9.293   20.764  18.284  1.00 39.14 ? 381 HOH A O   1 
HETATM 3678 O O   . HOH C 2 .   ? -15.238 28.391  24.367  1.00 40.47 ? 382 HOH A O   1 
HETATM 3679 O O   . HOH C 2 .   ? -18.138 15.939  -7.094  1.00 40.47 ? 383 HOH A O   1 
HETATM 3680 O O   . HOH C 2 .   ? 8.093   34.170  17.964  1.00 33.08 ? 384 HOH A O   1 
HETATM 3681 O O   . HOH C 2 .   ? -27.871 29.630  -9.995  1.00 38.93 ? 385 HOH A O   1 
HETATM 3682 O O   . HOH C 2 .   ? 1.527   23.058  5.805   1.00 31.32 ? 386 HOH A O   1 
HETATM 3683 O O   . HOH C 2 .   ? -16.140 41.851  20.642  1.00 41.06 ? 387 HOH A O   1 
HETATM 3684 O O   . HOH C 2 .   ? -14.776 37.658  24.659  1.00 36.12 ? 388 HOH A O   1 
HETATM 3685 O O   . HOH C 2 .   ? -12.773 30.941  22.042  1.00 14.24 ? 389 HOH A O   1 
HETATM 3686 O O   . HOH C 2 .   ? -23.180 36.048  20.395  1.00 37.87 ? 390 HOH A O   1 
HETATM 3687 O O   . HOH C 2 .   ? -25.286 18.798  -1.929  1.00 37.76 ? 391 HOH A O   1 
HETATM 3688 O O   . HOH C 2 .   ? -0.362  41.522  6.554   1.00 42.07 ? 392 HOH A O   1 
HETATM 3689 O O   . HOH C 2 .   ? -24.249 16.217  -3.035  1.00 44.65 ? 393 HOH A O   1 
HETATM 3690 O O   . HOH C 2 .   ? 3.904   21.300  0.083   1.00 39.36 ? 394 HOH A O   1 
HETATM 3691 O O   . HOH C 2 .   ? -12.396 45.024  14.305  1.00 42.23 ? 395 HOH A O   1 
HETATM 3692 O O   . HOH C 2 .   ? -19.300 39.741  8.941   1.00 27.17 ? 396 HOH A O   1 
HETATM 3693 O O   . HOH C 2 .   ? 8.001   22.097  23.234  1.00 40.49 ? 397 HOH A O   1 
HETATM 3694 O O   . HOH C 2 .   ? 6.966   34.686  12.122  1.00 38.29 ? 398 HOH A O   1 
HETATM 3695 O O   . HOH C 2 .   ? -6.262  14.481  23.622  1.00 36.89 ? 399 HOH A O   1 
HETATM 3696 O O   . HOH C 2 .   ? -6.857  16.670  4.461   1.00 44.48 ? 400 HOH A O   1 
HETATM 3697 O O   . HOH C 2 .   ? -9.868  44.981  10.920  1.00 50.00 ? 401 HOH A O   1 
HETATM 3698 O O   . HOH C 2 .   ? -15.253 42.602  2.198   1.00 45.32 ? 402 HOH A O   1 
HETATM 3699 O O   . HOH C 2 .   ? -3.613  15.819  26.170  1.00 45.39 ? 403 HOH A O   1 
HETATM 3700 O O   . HOH C 2 .   ? 2.817   39.795  0.899   1.00 33.85 ? 404 HOH A O   1 
HETATM 3701 O O   . HOH C 2 .   ? -0.496  18.832  9.213   1.00 46.06 ? 405 HOH A O   1 
HETATM 3702 O O   . HOH C 2 .   ? 10.774  20.496  20.795  1.00 39.60 ? 406 HOH A O   1 
HETATM 3703 O O   . HOH C 2 .   ? -5.236  44.210  11.573  1.00 35.35 ? 407 HOH A O   1 
HETATM 3704 O O   . HOH C 2 .   ? -12.817 30.498  26.639  1.00 44.54 ? 408 HOH A O   1 
HETATM 3705 O O   . HOH C 2 .   ? -25.316 31.804  23.713  1.00 39.74 ? 409 HOH A O   1 
HETATM 3706 O O   . HOH C 2 .   ? 7.102   33.325  15.883  1.00 32.30 ? 410 HOH A O   1 
HETATM 3707 O O   . HOH C 2 .   ? 3.075   36.349  -1.745  1.00 52.55 ? 411 HOH A O   1 
HETATM 3708 O O   . HOH C 2 .   ? -11.092 44.967  8.822   1.00 44.87 ? 412 HOH A O   1 
HETATM 3709 O O   . HOH C 2 .   ? -22.008 16.954  -9.365  1.00 46.04 ? 413 HOH A O   1 
HETATM 3710 O O   . HOH C 2 .   ? -25.680 36.779  18.967  1.00 41.07 ? 414 HOH A O   1 
HETATM 3711 O O   . HOH C 2 .   ? 0.838   15.886  -3.124  1.00 40.03 ? 415 HOH A O   1 
HETATM 3712 O O   . HOH C 2 .   ? 6.438   35.008  14.415  1.00 35.22 ? 416 HOH A O   1 
HETATM 3713 O O   . HOH C 2 .   ? -9.909  12.235  19.255  1.00 41.85 ? 417 HOH A O   1 
HETATM 3714 O O   . HOH C 2 .   ? 5.787   21.768  1.649   1.00 47.20 ? 418 HOH A O   1 
HETATM 3715 O O   . HOH C 2 .   ? -25.859 34.632  11.827  1.00 47.10 ? 419 HOH A O   1 
HETATM 3716 O O   . HOH C 2 .   ? -22.157 39.918  23.198  1.00 44.15 ? 420 HOH A O   1 
HETATM 3717 O O   . HOH D 2 .   ? 12.186  1.396   24.325  1.00 24.74 ? 301 HOH B O   1 
HETATM 3718 O O   . HOH D 2 .   ? 3.304   -7.865  44.776  1.00 30.85 ? 302 HOH B O   1 
HETATM 3719 O O   . HOH D 2 .   ? -0.474  20.021  34.860  1.00 47.87 ? 303 HOH B O   1 
HETATM 3720 O O   . HOH D 2 .   ? 25.997  14.135  46.241  1.00 38.03 ? 304 HOH B O   1 
HETATM 3721 O O   . HOH D 2 .   ? 1.518   0.486   19.282  1.00 43.80 ? 305 HOH B O   1 
HETATM 3722 O O   . HOH D 2 .   ? 14.531  -8.755  35.461  1.00 42.16 ? 306 HOH B O   1 
HETATM 3723 O O   . HOH D 2 .   ? 12.968  -7.583  55.482  1.00 30.99 ? 307 HOH B O   1 
HETATM 3724 O O   . HOH D 2 .   ? -4.764  13.871  41.798  1.00 42.56 ? 308 HOH B O   1 
HETATM 3725 O O   . HOH D 2 .   ? 29.477  3.777   31.331  1.00 32.32 ? 309 HOH B O   1 
HETATM 3726 O O   . HOH D 2 .   ? 16.854  21.390  51.643  1.00 33.49 ? 310 HOH B O   1 
HETATM 3727 O O   . HOH D 2 .   ? -2.209  -10.092 29.943  1.00 38.75 ? 311 HOH B O   1 
HETATM 3728 O O   . HOH D 2 .   ? -1.983  8.946   25.130  1.00 23.56 ? 312 HOH B O   1 
HETATM 3729 O O   . HOH D 2 .   ? 20.798  16.551  50.339  1.00 37.38 ? 313 HOH B O   1 
HETATM 3730 O O   . HOH D 2 .   ? 12.792  -8.659  37.284  1.00 32.98 ? 314 HOH B O   1 
HETATM 3731 O O   . HOH D 2 .   ? 8.281   4.131   48.662  1.00 25.26 ? 315 HOH B O   1 
HETATM 3732 O O   . HOH D 2 .   ? 11.943  8.416   54.488  1.00 33.34 ? 316 HOH B O   1 
HETATM 3733 O O   . HOH D 2 .   ? 13.934  10.164  59.098  1.00 44.06 ? 317 HOH B O   1 
HETATM 3734 O O   . HOH D 2 .   ? 9.390   -10.301 36.229  1.00 37.06 ? 318 HOH B O   1 
HETATM 3735 O O   . HOH D 2 .   ? 16.937  -4.277  26.162  1.00 23.68 ? 319 HOH B O   1 
HETATM 3736 O O   . HOH D 2 .   ? 5.793   -9.934  32.967  1.00 25.35 ? 320 HOH B O   1 
HETATM 3737 O O   . HOH D 2 .   ? 3.510   0.461   43.671  1.00 19.62 ? 321 HOH B O   1 
HETATM 3738 O O   . HOH D 2 .   ? 6.456   -6.726  25.627  1.00 36.87 ? 322 HOH B O   1 
HETATM 3739 O O   . HOH D 2 .   ? 4.502   -0.003  22.754  1.00 26.78 ? 323 HOH B O   1 
HETATM 3740 O O   . HOH D 2 .   ? -0.901  -0.882  50.503  1.00 26.01 ? 324 HOH B O   1 
HETATM 3741 O O   . HOH D 2 .   ? 23.370  -2.485  36.391  1.00 35.03 ? 325 HOH B O   1 
HETATM 3742 O O   . HOH D 2 .   ? 7.988   12.615  28.913  1.00 17.13 ? 326 HOH B O   1 
HETATM 3743 O O   . HOH D 2 .   ? 5.512   4.852   37.492  1.00 13.48 ? 327 HOH B O   1 
HETATM 3744 O O   . HOH D 2 .   ? 10.058  5.784   24.204  1.00 24.98 ? 328 HOH B O   1 
HETATM 3745 O O   . HOH D 2 .   ? -0.784  4.764   24.816  1.00 21.75 ? 329 HOH B O   1 
HETATM 3746 O O   . HOH D 2 .   ? 8.731   15.495  31.096  1.00 19.97 ? 330 HOH B O   1 
HETATM 3747 O O   . HOH D 2 .   ? 20.923  10.496  35.441  1.00 23.04 ? 331 HOH B O   1 
HETATM 3748 O O   . HOH D 2 .   ? 0.070   15.226  46.724  1.00 21.96 ? 332 HOH B O   1 
HETATM 3749 O O   . HOH D 2 .   ? 20.757  -2.325  36.454  1.00 36.05 ? 333 HOH B O   1 
HETATM 3750 O O   . HOH D 2 .   ? 20.580  5.630   53.668  1.00 29.65 ? 334 HOH B O   1 
HETATM 3751 O O   . HOH D 2 .   ? 2.867   17.268  20.784  1.00 21.97 ? 335 HOH B O   1 
HETATM 3752 O O   . HOH D 2 .   ? 6.686   8.398   36.519  1.00 14.26 ? 336 HOH B O   1 
HETATM 3753 O O   . HOH D 2 .   ? 0.913   13.099  20.970  1.00 35.80 ? 337 HOH B O   1 
HETATM 3754 O O   . HOH D 2 .   ? 3.412   3.135   41.220  1.00 14.70 ? 338 HOH B O   1 
HETATM 3755 O O   . HOH D 2 .   ? 12.889  -1.873  63.175  1.00 38.81 ? 339 HOH B O   1 
HETATM 3756 O O   . HOH D 2 .   ? -10.769 10.114  27.258  1.00 43.91 ? 340 HOH B O   1 
HETATM 3757 O O   . HOH D 2 .   ? 2.218   -8.546  56.571  1.00 36.75 ? 341 HOH B O   1 
HETATM 3758 O O   . HOH D 2 .   ? 7.882   11.078  46.628  1.00 21.03 ? 342 HOH B O   1 
HETATM 3759 O O   . HOH D 2 .   ? 22.607  -1.416  54.259  1.00 26.91 ? 343 HOH B O   1 
HETATM 3760 O O   . HOH D 2 .   ? 8.577   20.073  24.808  1.00 33.61 ? 344 HOH B O   1 
HETATM 3761 O O   . HOH D 2 .   ? 10.243  -6.370  26.646  1.00 26.04 ? 345 HOH B O   1 
HETATM 3762 O O   . HOH D 2 .   ? 0.578   20.671  44.584  1.00 43.24 ? 346 HOH B O   1 
HETATM 3763 O O   . HOH D 2 .   ? -4.510  -1.581  35.162  1.00 19.07 ? 347 HOH B O   1 
HETATM 3764 O O   . HOH D 2 .   ? 17.657  2.837   26.145  1.00 23.65 ? 348 HOH B O   1 
HETATM 3765 O O   . HOH D 2 .   ? 7.553   14.016  34.450  1.00 19.78 ? 349 HOH B O   1 
HETATM 3766 O O   . HOH D 2 .   ? -1.971  13.509  48.816  1.00 21.83 ? 350 HOH B O   1 
HETATM 3767 O O   . HOH D 2 .   ? 8.437   12.634  31.641  1.00 14.98 ? 351 HOH B O   1 
HETATM 3768 O O   . HOH D 2 .   ? 16.700  13.930  30.332  1.00 29.07 ? 352 HOH B O   1 
HETATM 3769 O O   . HOH D 2 .   ? 10.346  19.855  31.187  1.00 39.31 ? 353 HOH B O   1 
HETATM 3770 O O   . HOH D 2 .   ? 6.512   -3.002  58.949  1.00 25.35 ? 354 HOH B O   1 
HETATM 3771 O O   . HOH D 2 .   ? -9.250  6.606   29.328  1.00 32.10 ? 355 HOH B O   1 
HETATM 3772 O O   . HOH D 2 .   ? -7.979  16.883  38.444  1.00 37.37 ? 356 HOH B O   1 
HETATM 3773 O O   . HOH D 2 .   ? -6.465  -3.580  28.284  1.00 40.60 ? 357 HOH B O   1 
HETATM 3774 O O   . HOH D 2 .   ? 10.525  10.459  45.792  1.00 23.04 ? 358 HOH B O   1 
HETATM 3775 O O   . HOH D 2 .   ? 7.951   13.992  45.441  1.00 19.11 ? 359 HOH B O   1 
HETATM 3776 O O   . HOH D 2 .   ? 6.351   9.515   56.277  1.00 32.35 ? 360 HOH B O   1 
HETATM 3777 O O   . HOH D 2 .   ? -0.694  19.472  27.068  1.00 45.31 ? 361 HOH B O   1 
HETATM 3778 O O   . HOH D 2 .   ? 19.889  -8.373  30.244  1.00 39.10 ? 362 HOH B O   1 
HETATM 3779 O O   . HOH D 2 .   ? 18.312  15.014  40.129  1.00 22.48 ? 363 HOH B O   1 
HETATM 3780 O O   . HOH D 2 .   ? 13.314  12.932  24.332  1.00 28.03 ? 364 HOH B O   1 
HETATM 3781 O O   . HOH D 2 .   ? 11.580  7.170   45.831  1.00 21.34 ? 365 HOH B O   1 
HETATM 3782 O O   . HOH D 2 .   ? 4.861   16.718  37.429  1.00 19.86 ? 366 HOH B O   1 
HETATM 3783 O O   . HOH D 2 .   ? 4.091   8.338   35.799  1.00 16.78 ? 367 HOH B O   1 
HETATM 3784 O O   . HOH D 2 .   ? 7.561   0.811   45.739  1.00 18.11 ? 368 HOH B O   1 
HETATM 3785 O O   . HOH D 2 .   ? -4.611  12.251  57.423  1.00 30.22 ? 369 HOH B O   1 
HETATM 3786 O O   . HOH D 2 .   ? 22.229  -3.702  44.588  1.00 27.69 ? 370 HOH B O   1 
HETATM 3787 O O   . HOH D 2 .   ? -2.724  14.827  29.497  1.00 22.75 ? 371 HOH B O   1 
HETATM 3788 O O   . HOH D 2 .   ? 5.967   21.082  29.555  1.00 43.63 ? 372 HOH B O   1 
HETATM 3789 O O   . HOH D 2 .   ? 6.286   19.064  25.718  1.00 28.76 ? 373 HOH B O   1 
HETATM 3790 O O   . HOH D 2 .   ? 24.617  8.561   32.550  1.00 41.13 ? 374 HOH B O   1 
HETATM 3791 O O   . HOH D 2 .   ? 4.727   21.820  26.454  1.00 37.13 ? 375 HOH B O   1 
HETATM 3792 O O   . HOH D 2 .   ? 6.047   1.485   43.739  1.00 18.56 ? 376 HOH B O   1 
HETATM 3793 O O   . HOH D 2 .   ? 11.516  18.384  37.744  1.00 29.97 ? 377 HOH B O   1 
HETATM 3794 O O   . HOH D 2 .   ? 4.293   -9.933  25.493  1.00 32.06 ? 378 HOH B O   1 
HETATM 3795 O O   . HOH D 2 .   ? 2.883   -2.252  21.783  1.00 41.27 ? 379 HOH B O   1 
HETATM 3796 O O   . HOH D 2 .   ? 21.105  -1.138  56.619  1.00 32.43 ? 380 HOH B O   1 
HETATM 3797 O O   . HOH D 2 .   ? 7.073   -7.998  62.639  1.00 40.01 ? 381 HOH B O   1 
HETATM 3798 O O   . HOH D 2 .   ? 20.455  14.225  31.473  1.00 33.32 ? 382 HOH B O   1 
HETATM 3799 O O   . HOH D 2 .   ? 14.599  6.028   26.014  1.00 21.06 ? 383 HOH B O   1 
HETATM 3800 O O   . HOH D 2 .   ? 8.470   7.895   24.476  1.00 21.98 ? 384 HOH B O   1 
HETATM 3801 O O   . HOH D 2 .   ? 8.275   -10.444 31.714  1.00 28.45 ? 385 HOH B O   1 
HETATM 3802 O O   . HOH D 2 .   ? 0.069   20.765  55.921  1.00 36.67 ? 386 HOH B O   1 
HETATM 3803 O O   . HOH D 2 .   ? 15.875  14.420  33.080  1.00 23.68 ? 387 HOH B O   1 
HETATM 3804 O O   . HOH D 2 .   ? -9.091  9.948   31.016  1.00 29.33 ? 388 HOH B O   1 
HETATM 3805 O O   . HOH D 2 .   ? 2.465   -8.632  51.762  1.00 44.35 ? 389 HOH B O   1 
HETATM 3806 O O   . HOH D 2 .   ? -2.754  -6.248  30.745  1.00 28.13 ? 390 HOH B O   1 
HETATM 3807 O O   . HOH D 2 .   ? 5.829   -7.766  45.290  1.00 42.32 ? 391 HOH B O   1 
HETATM 3808 O O   . HOH D 2 .   ? -7.963  4.381   32.645  1.00 30.92 ? 392 HOH B O   1 
HETATM 3809 O O   . HOH D 2 .   ? 9.433   -1.837  62.054  1.00 35.43 ? 393 HOH B O   1 
HETATM 3810 O O   . HOH D 2 .   ? 14.265  16.382  33.201  1.00 27.91 ? 394 HOH B O   1 
HETATM 3811 O O   . HOH D 2 .   ? -0.711  11.423  62.486  1.00 43.35 ? 395 HOH B O   1 
HETATM 3812 O O   . HOH D 2 .   ? 22.741  -6.221  34.166  1.00 41.98 ? 396 HOH B O   1 
HETATM 3813 O O   . HOH D 2 .   ? -6.669  6.730   32.704  1.00 22.85 ? 397 HOH B O   1 
HETATM 3814 O O   . HOH D 2 .   ? 24.216  -5.608  50.293  1.00 36.95 ? 398 HOH B O   1 
HETATM 3815 O O   . HOH D 2 .   ? 7.572   -0.932  22.000  1.00 32.67 ? 399 HOH B O   1 
HETATM 3816 O O   . HOH D 2 .   ? 21.088  -8.795  49.514  1.00 31.48 ? 400 HOH B O   1 
HETATM 3817 O O   . HOH D 2 .   ? 17.123  21.279  55.510  1.00 44.27 ? 401 HOH B O   1 
HETATM 3818 O O   . HOH D 2 .   ? 22.574  10.895  28.613  1.00 30.79 ? 402 HOH B O   1 
HETATM 3819 O O   . HOH D 2 .   ? 11.840  -12.034 33.269  1.00 40.07 ? 403 HOH B O   1 
HETATM 3820 O O   . HOH D 2 .   ? 17.080  -9.156  56.280  1.00 30.73 ? 404 HOH B O   1 
HETATM 3821 O O   . HOH D 2 .   ? -8.073  10.480  37.007  1.00 32.83 ? 405 HOH B O   1 
HETATM 3822 O O   . HOH D 2 .   ? 11.259  8.919   26.777  1.00 26.77 ? 406 HOH B O   1 
HETATM 3823 O O   . HOH D 2 .   ? -1.318  15.478  60.461  1.00 35.91 ? 407 HOH B O   1 
HETATM 3824 O O   . HOH D 2 .   ? -0.479  20.939  47.019  1.00 48.51 ? 408 HOH B O   1 
HETATM 3825 O O   . HOH D 2 .   ? 8.904   17.666  43.686  1.00 25.86 ? 409 HOH B O   1 
HETATM 3826 O O   . HOH D 2 .   ? -0.852  16.995  42.448  1.00 20.44 ? 410 HOH B O   1 
HETATM 3827 O O   . HOH D 2 .   ? 1.743   -8.124  36.266  1.00 34.99 ? 411 HOH B O   1 
HETATM 3828 O O   . HOH D 2 .   ? 22.986  -8.445  51.878  1.00 29.49 ? 412 HOH B O   1 
HETATM 3829 O O   . HOH D 2 .   ? 15.325  17.391  27.900  1.00 43.38 ? 413 HOH B O   1 
HETATM 3830 O O   . HOH D 2 .   ? -3.072  -3.892  44.246  1.00 31.03 ? 414 HOH B O   1 
HETATM 3831 O O   . HOH D 2 .   ? 11.676  6.146   26.867  1.00 10.62 ? 415 HOH B O   1 
HETATM 3832 O O   . HOH D 2 .   ? -5.107  -2.943  49.629  1.00 46.10 ? 416 HOH B O   1 
HETATM 3833 O O   . HOH D 2 .   ? 22.639  12.569  35.958  1.00 34.19 ? 417 HOH B O   1 
HETATM 3834 O O   . HOH D 2 .   ? 14.624  17.507  46.517  1.00 33.50 ? 418 HOH B O   1 
HETATM 3835 O O   . HOH D 2 .   ? 3.980   13.431  19.483  1.00 32.18 ? 419 HOH B O   1 
HETATM 3836 O O   . HOH D 2 .   ? 12.148  9.082   24.415  1.00 45.27 ? 420 HOH B O   1 
HETATM 3837 O O   . HOH D 2 .   ? -4.069  13.806  27.357  1.00 31.95 ? 421 HOH B O   1 
HETATM 3838 O O   . HOH D 2 .   ? 20.669  -3.389  57.131  1.00 46.83 ? 422 HOH B O   1 
HETATM 3839 O O   . HOH D 2 .   ? 7.491   -9.687  53.249  1.00 29.36 ? 423 HOH B O   1 
HETATM 3840 O O   . HOH D 2 .   ? 19.723  17.127  40.689  1.00 28.19 ? 424 HOH B O   1 
HETATM 3841 O O   . HOH D 2 .   ? 4.580   19.487  37.397  1.00 35.46 ? 425 HOH B O   1 
HETATM 3842 O O   . HOH D 2 .   ? -3.506  15.597  48.261  1.00 43.70 ? 426 HOH B O   1 
HETATM 3843 O O   . HOH D 2 .   ? 12.126  7.189   61.719  1.00 48.64 ? 427 HOH B O   1 
HETATM 3844 O O   . HOH D 2 .   ? 0.233   17.911  45.909  1.00 38.79 ? 428 HOH B O   1 
HETATM 3845 O O   . HOH D 2 .   ? 13.124  -8.289  58.082  1.00 45.08 ? 429 HOH B O   1 
HETATM 3846 O O   . HOH D 2 .   ? 19.913  2.575   24.260  1.00 46.33 ? 430 HOH B O   1 
HETATM 3847 O O   . HOH D 2 .   ? -8.112  8.889   33.207  1.00 31.64 ? 431 HOH B O   1 
HETATM 3848 O O   . HOH D 2 .   ? -5.723  -3.871  35.975  1.00 32.82 ? 432 HOH B O   1 
HETATM 3849 O O   . HOH D 2 .   ? 20.698  -7.593  58.740  1.00 39.24 ? 433 HOH B O   1 
HETATM 3850 O O   . HOH D 2 .   ? 1.516   19.386  64.816  1.00 39.76 ? 434 HOH B O   1 
HETATM 3851 O O   . HOH D 2 .   ? 15.071  7.838   24.441  1.00 47.13 ? 435 HOH B O   1 
HETATM 3852 O O   . HOH D 2 .   ? 11.919  6.120   22.340  1.00 36.97 ? 436 HOH B O   1 
HETATM 3853 O O   . HOH D 2 .   ? 22.862  -1.415  58.796  1.00 46.61 ? 437 HOH B O   1 
HETATM 3854 O O   . HOH D 2 .   ? 17.454  16.421  29.508  1.00 42.98 ? 438 HOH B O   1 
HETATM 3855 O O   . HOH D 2 .   ? 8.406   -11.991 29.539  1.00 38.56 ? 439 HOH B O   1 
HETATM 3856 O O   . HOH D 2 .   ? 16.325  -8.151  58.101  1.00 37.65 ? 440 HOH B O   1 
HETATM 3857 O O   . HOH D 2 .   ? 25.437  3.792   35.533  1.00 36.08 ? 441 HOH B O   1 
HETATM 3858 O O   . HOH D 2 .   ? 24.244  10.313  37.450  1.00 41.57 ? 442 HOH B O   1 
HETATM 3859 O O   . HOH D 2 .   ? 15.206  -12.911 39.381  1.00 35.00 ? 443 HOH B O   1 
# 
