data_9DQ1
# 
_entry.id   9DQ1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DQ1         pdb_00009dq1 10.2210/pdb9dq1/pdb 
WWPDB D_1000288595 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-12 ? 
2 'Structure model' 1 1 2025-03-05 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DQ1 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              wchang6@ncsu.edu 
_pdbx_contact_author.name_first         Wei-chen 
_pdbx_contact_author.name_last          Chang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2341-9846 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zheng, Y.-C.' 1 ? 
'Swartz, P.'   2 ? 
'Chang, W.-C.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Am.Chem.Soc. 
_citation.journal_id_ASTM           JACSAT 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1520-5126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            147 
_citation.language                  ? 
_citation.page_first                6162 
_citation.page_last                 6170 
_citation.title                     
;Comparison of a Nonheme Iron Cyclopropanase with a Homologous Hydroxylase Reveals Mechanistic Features Associated with Distinct Reaction Outcomes.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/jacs.4c17741 
_citation.pdbx_database_id_PubMed   39901767 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zheng, Y.C.'   1  ? 
primary 'Li, X.'        2  ? 
primary 'Cha, L.'       3  ? 
primary 'Paris, J.C.'   4  ? 
primary 'Michael, C.'   5  ? 
primary 'Ushimaru, R.'  6  ? 
primary 'Ogasawara, Y.' 7  ? 
primary 'Abe, I.'       8  ? 
primary 'Guo, Y.'       9  ? 
primary 'Chang, W.C.'   10 ? 
# 
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 'BsmA domain containing protein' 26498.471 2   ? ? ? ? 
2 non-polymer syn 'MANGANESE (II) ION'             54.938    2   ? ? ? ? 
3 non-polymer syn '2-OXOGLUTARIC ACID'             146.098   2   ? ? ? ? 
4 non-polymer syn 6-nitro-L-norleucine             176.170   3   ? ? ? ? 
5 non-polymer syn 'IODIDE ION'                     126.904   7   ? ? ? ? 
6 non-polymer syn 1,2-ETHANEDIOL                   62.068    1   ? ? ? ? 
7 non-polymer syn GLYCEROL                         92.094    2   ? ? ? ? 
8 water       nat water                            18.015    534 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MPLGTEGFTVIDLPEVAPDILPSYDRCPVDDYMGNGTRFKRFSQYKLTPAEDDTWSFKRLPHRDYTTYKKFNPVGGGIRR
VYEPIEVDFTPLISEGIRELGLDRSEPWQINVHQNRTRADGGRPGPLTPEGVHHDGHEFVMIAILNKVNVAGGTTRLWKP
GADAPFWSGTLEAGQAVLLDDRGLAHDVTDVLSADGGPGHRDIVIIAFSRWAEKWYGDEHDAAALEEQEAHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPLGTEGFTVIDLPEVAPDILPSYDRCPVDDYMGNGTRFKRFSQYKLTPAEDDTWSFKRLPHRDYTTYKKFNPVGGGIRR
VYEPIEVDFTPLISEGIRELGLDRSEPWQINVHQNRTRADGGRPGPLTPEGVHHDGHEFVMIAILNKVNVAGGTTRLWKP
GADAPFWSGTLEAGQAVLLDDRGLAHDVTDVLSADGGPGHRDIVIIAFSRWAEKWYGDEHDAAALEEQEAHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MANGANESE (II) ION' MN  
3 '2-OXOGLUTARIC ACID' AKG 
4 6-nitro-L-norleucine 6HN 
5 'IODIDE ION'         IOD 
6 1,2-ETHANEDIOL       EDO 
7 GLYCEROL             GOL 
8 water                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   PRO n 
1 3   LEU n 
1 4   GLY n 
1 5   THR n 
1 6   GLU n 
1 7   GLY n 
1 8   PHE n 
1 9   THR n 
1 10  VAL n 
1 11  ILE n 
1 12  ASP n 
1 13  LEU n 
1 14  PRO n 
1 15  GLU n 
1 16  VAL n 
1 17  ALA n 
1 18  PRO n 
1 19  ASP n 
1 20  ILE n 
1 21  LEU n 
1 22  PRO n 
1 23  SER n 
1 24  TYR n 
1 25  ASP n 
1 26  ARG n 
1 27  CYS n 
1 28  PRO n 
1 29  VAL n 
1 30  ASP n 
1 31  ASP n 
1 32  TYR n 
1 33  MET n 
1 34  GLY n 
1 35  ASN n 
1 36  GLY n 
1 37  THR n 
1 38  ARG n 
1 39  PHE n 
1 40  LYS n 
1 41  ARG n 
1 42  PHE n 
1 43  SER n 
1 44  GLN n 
1 45  TYR n 
1 46  LYS n 
1 47  LEU n 
1 48  THR n 
1 49  PRO n 
1 50  ALA n 
1 51  GLU n 
1 52  ASP n 
1 53  ASP n 
1 54  THR n 
1 55  TRP n 
1 56  SER n 
1 57  PHE n 
1 58  LYS n 
1 59  ARG n 
1 60  LEU n 
1 61  PRO n 
1 62  HIS n 
1 63  ARG n 
1 64  ASP n 
1 65  TYR n 
1 66  THR n 
1 67  THR n 
1 68  TYR n 
1 69  LYS n 
1 70  LYS n 
1 71  PHE n 
1 72  ASN n 
1 73  PRO n 
1 74  VAL n 
1 75  GLY n 
1 76  GLY n 
1 77  GLY n 
1 78  ILE n 
1 79  ARG n 
1 80  ARG n 
1 81  VAL n 
1 82  TYR n 
1 83  GLU n 
1 84  PRO n 
1 85  ILE n 
1 86  GLU n 
1 87  VAL n 
1 88  ASP n 
1 89  PHE n 
1 90  THR n 
1 91  PRO n 
1 92  LEU n 
1 93  ILE n 
1 94  SER n 
1 95  GLU n 
1 96  GLY n 
1 97  ILE n 
1 98  ARG n 
1 99  GLU n 
1 100 LEU n 
1 101 GLY n 
1 102 LEU n 
1 103 ASP n 
1 104 ARG n 
1 105 SER n 
1 106 GLU n 
1 107 PRO n 
1 108 TRP n 
1 109 GLN n 
1 110 ILE n 
1 111 ASN n 
1 112 VAL n 
1 113 HIS n 
1 114 GLN n 
1 115 ASN n 
1 116 ARG n 
1 117 THR n 
1 118 ARG n 
1 119 ALA n 
1 120 ASP n 
1 121 GLY n 
1 122 GLY n 
1 123 ARG n 
1 124 PRO n 
1 125 GLY n 
1 126 PRO n 
1 127 LEU n 
1 128 THR n 
1 129 PRO n 
1 130 GLU n 
1 131 GLY n 
1 132 VAL n 
1 133 HIS n 
1 134 HIS n 
1 135 ASP n 
1 136 GLY n 
1 137 HIS n 
1 138 GLU n 
1 139 PHE n 
1 140 VAL n 
1 141 MET n 
1 142 ILE n 
1 143 ALA n 
1 144 ILE n 
1 145 LEU n 
1 146 ASN n 
1 147 LYS n 
1 148 VAL n 
1 149 ASN n 
1 150 VAL n 
1 151 ALA n 
1 152 GLY n 
1 153 GLY n 
1 154 THR n 
1 155 THR n 
1 156 ARG n 
1 157 LEU n 
1 158 TRP n 
1 159 LYS n 
1 160 PRO n 
1 161 GLY n 
1 162 ALA n 
1 163 ASP n 
1 164 ALA n 
1 165 PRO n 
1 166 PHE n 
1 167 TRP n 
1 168 SER n 
1 169 GLY n 
1 170 THR n 
1 171 LEU n 
1 172 GLU n 
1 173 ALA n 
1 174 GLY n 
1 175 GLN n 
1 176 ALA n 
1 177 VAL n 
1 178 LEU n 
1 179 LEU n 
1 180 ASP n 
1 181 ASP n 
1 182 ARG n 
1 183 GLY n 
1 184 LEU n 
1 185 ALA n 
1 186 HIS n 
1 187 ASP n 
1 188 VAL n 
1 189 THR n 
1 190 ASP n 
1 191 VAL n 
1 192 LEU n 
1 193 SER n 
1 194 ALA n 
1 195 ASP n 
1 196 GLY n 
1 197 GLY n 
1 198 PRO n 
1 199 GLY n 
1 200 HIS n 
1 201 ARG n 
1 202 ASP n 
1 203 ILE n 
1 204 VAL n 
1 205 ILE n 
1 206 ILE n 
1 207 ALA n 
1 208 PHE n 
1 209 SER n 
1 210 ARG n 
1 211 TRP n 
1 212 ALA n 
1 213 GLU n 
1 214 LYS n 
1 215 TRP n 
1 216 TYR n 
1 217 GLY n 
1 218 ASP n 
1 219 GLU n 
1 220 HIS n 
1 221 ASP n 
1 222 ALA n 
1 223 ALA n 
1 224 ALA n 
1 225 LEU n 
1 226 GLU n 
1 227 GLU n 
1 228 GLN n 
1 229 GLU n 
1 230 ALA n 
1 231 HIS n 
1 232 HIS n 
1 233 HIS n 
1 234 HIS n 
1 235 HIS n 
1 236 HIS 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                 ABE83_05625 
_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      'Streptomyces sp. CFMR 7' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1649184 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_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 
6HN 'L-peptide linking' n 6-nitro-L-norleucine ?                               'C6 H12 N2 O4'   176.170 
AKG non-polymer         . '2-OXOGLUTARIC ACID' ?                               'C5 H6 O5'       146.098 
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 
CYS 'L-peptide linking' y CYSTEINE             ?                               'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL       'ETHYLENE GLYCOL'               'C2 H6 O2'       62.068  
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  
GOL non-polymer         . GLYCEROL             'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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 
IOD non-polymer         . 'IODIDE ION'         ?                               'I -1'           126.904 
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 
MN  non-polymer         . 'MANGANESE (II) ION' ?                               'Mn 2'           54.938  
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   PRO 2   2   2   PRO PRO A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   GLY 4   4   4   GLY GLY A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   GLU 6   6   6   GLU GLU A . n 
A 1 7   GLY 7   7   7   GLY GLY 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  VAL 10  10  10  VAL VAL A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  PRO 18  18  18  PRO PRO A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  ILE 20  20  20  ILE ILE A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  PRO 22  22  22  PRO PRO A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  ARG 26  26  26  ARG ARG A . n 
A 1 27  CYS 27  27  27  CYS CYS A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  ASP 30  30  30  ASP ASP A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  TYR 32  32  32  TYR TYR A . n 
A 1 33  MET 33  33  33  MET MET A . n 
A 1 34  GLY 34  34  34  GLY GLY A . n 
A 1 35  ASN 35  35  35  ASN ASN A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  ARG 41  41  41  ARG ARG A . n 
A 1 42  PHE 42  42  42  PHE PHE A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  GLN 44  44  44  GLN GLN A . n 
A 1 45  TYR 45  45  45  TYR TYR A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  THR 48  48  48  THR THR A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  TRP 55  55  55  TRP TRP A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  ARG 59  59  59  ARG ARG A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  HIS 62  62  62  HIS HIS A . n 
A 1 63  ARG 63  63  63  ARG ARG A . n 
A 1 64  ASP 64  64  64  ASP ASP A . n 
A 1 65  TYR 65  65  65  TYR TYR A . n 
A 1 66  THR 66  66  66  THR THR A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  PHE 71  71  71  PHE PHE A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  VAL 74  74  74  VAL VAL A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  ARG 80  80  80  ARG ARG A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  TYR 82  82  82  TYR TYR A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  ASP 88  88  88  ASP ASP A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  ILE 97  97  97  ILE ILE A . n 
A 1 98  ARG 98  98  98  ARG ARG A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 PRO 107 107 107 PRO PRO A . n 
A 1 108 TRP 108 108 108 TRP TRP A . n 
A 1 109 GLN 109 109 109 GLN GLN A . n 
A 1 110 ILE 110 110 110 ILE ILE A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 HIS 113 113 113 HIS HIS A . n 
A 1 114 GLN 114 114 114 GLN GLN A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 PRO 126 126 126 PRO PRO A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 GLU 130 130 130 GLU GLU A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 HIS 133 133 133 HIS HIS A . n 
A 1 134 HIS 134 134 134 HIS HIS A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 HIS 137 137 137 HIS HIS A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 PHE 139 139 139 PHE PHE A . n 
A 1 140 VAL 140 140 140 VAL VAL A . n 
A 1 141 MET 141 141 141 MET MET A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ASN 146 146 146 ASN ASN A . n 
A 1 147 LYS 147 147 147 LYS LYS A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ASN 149 149 149 ASN ASN A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 GLY 152 152 152 GLY GLY A . n 
A 1 153 GLY 153 153 153 GLY GLY A . n 
A 1 154 THR 154 154 154 THR THR A . n 
A 1 155 THR 155 155 155 THR THR A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 TRP 158 158 158 TRP TRP A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 PRO 160 160 160 PRO PRO A . n 
A 1 161 GLY 161 161 161 GLY GLY A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 ASP 163 163 163 ASP ASP A . n 
A 1 164 ALA 164 164 164 ALA ALA A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 PHE 166 166 166 PHE PHE A . n 
A 1 167 TRP 167 167 167 TRP TRP A . n 
A 1 168 SER 168 168 168 SER SER A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 GLU 172 172 172 GLU GLU A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 GLN 175 175 175 GLN GLN A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 ASP 180 180 180 ASP ASP A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 ARG 182 182 182 ARG ARG A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 HIS 186 186 186 HIS HIS A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 ASP 190 190 190 ASP ASP A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 LEU 192 192 192 LEU LEU A . n 
A 1 193 SER 193 193 193 SER SER A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 GLY 197 197 197 GLY GLY A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 HIS 200 200 200 HIS HIS A . n 
A 1 201 ARG 201 201 201 ARG ARG A . n 
A 1 202 ASP 202 202 202 ASP ASP A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 ILE 205 205 205 ILE ILE A . n 
A 1 206 ILE 206 206 206 ILE ILE A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 PHE 208 208 208 PHE PHE A . n 
A 1 209 SER 209 209 209 SER SER A . n 
A 1 210 ARG 210 210 210 ARG ARG A . n 
A 1 211 TRP 211 211 211 TRP TRP A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 LYS 214 214 214 LYS LYS A . n 
A 1 215 TRP 215 215 215 TRP TRP A . n 
A 1 216 TYR 216 216 216 TYR TYR A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 HIS 220 220 220 HIS HIS A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 ALA 222 222 222 ALA ALA A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 GLU 227 227 227 GLU GLU A . n 
A 1 228 GLN 228 228 ?   ?   ?   A . n 
A 1 229 GLU 229 229 ?   ?   ?   A . n 
A 1 230 ALA 230 230 ?   ?   ?   A . n 
A 1 231 HIS 231 231 ?   ?   ?   A . n 
A 1 232 HIS 232 232 ?   ?   ?   A . n 
A 1 233 HIS 233 233 ?   ?   ?   A . n 
A 1 234 HIS 234 234 ?   ?   ?   A . n 
A 1 235 HIS 235 235 ?   ?   ?   A . n 
A 1 236 HIS 236 236 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   2   PRO PRO B . n 
B 1 3   LEU 3   3   3   LEU LEU B . n 
B 1 4   GLY 4   4   4   GLY GLY B . n 
B 1 5   THR 5   5   5   THR THR B . n 
B 1 6   GLU 6   6   6   GLU GLU B . n 
B 1 7   GLY 7   7   7   GLY GLY 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  VAL 10  10  10  VAL VAL B . n 
B 1 11  ILE 11  11  11  ILE ILE B . n 
B 1 12  ASP 12  12  12  ASP ASP B . n 
B 1 13  LEU 13  13  13  LEU LEU B . n 
B 1 14  PRO 14  14  14  PRO PRO B . n 
B 1 15  GLU 15  15  15  GLU GLU B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  PRO 18  18  18  PRO PRO B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  ILE 20  20  20  ILE ILE B . n 
B 1 21  LEU 21  21  21  LEU LEU B . n 
B 1 22  PRO 22  22  22  PRO PRO B . n 
B 1 23  SER 23  23  23  SER SER B . n 
B 1 24  TYR 24  24  24  TYR TYR B . n 
B 1 25  ASP 25  25  25  ASP ASP B . n 
B 1 26  ARG 26  26  26  ARG ARG B . n 
B 1 27  CYS 27  27  27  CYS CYS B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  ASP 30  30  30  ASP ASP B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  TYR 32  32  32  TYR TYR B . n 
B 1 33  MET 33  33  33  MET MET B . n 
B 1 34  GLY 34  34  34  GLY GLY B . n 
B 1 35  ASN 35  35  35  ASN ASN B . n 
B 1 36  GLY 36  36  36  GLY GLY B . n 
B 1 37  THR 37  37  37  THR THR B . n 
B 1 38  ARG 38  38  38  ARG ARG B . n 
B 1 39  PHE 39  39  39  PHE PHE B . n 
B 1 40  LYS 40  40  40  LYS LYS B . n 
B 1 41  ARG 41  41  41  ARG ARG B . n 
B 1 42  PHE 42  42  42  PHE PHE B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  GLN 44  44  44  GLN GLN B . n 
B 1 45  TYR 45  45  45  TYR TYR B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  LEU 47  47  47  LEU LEU B . n 
B 1 48  THR 48  48  48  THR THR B . n 
B 1 49  PRO 49  49  49  PRO PRO B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ASP 53  53  53  ASP ASP B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  TRP 55  55  55  TRP TRP B . n 
B 1 56  SER 56  56  56  SER SER B . n 
B 1 57  PHE 57  57  57  PHE PHE B . n 
B 1 58  LYS 58  58  58  LYS LYS B . n 
B 1 59  ARG 59  59  59  ARG ARG B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  PRO 61  61  61  PRO PRO B . n 
B 1 62  HIS 62  62  62  HIS HIS B . n 
B 1 63  ARG 63  63  63  ARG ARG B . n 
B 1 64  ASP 64  64  64  ASP ASP B . n 
B 1 65  TYR 65  65  65  TYR TYR B . n 
B 1 66  THR 66  66  66  THR THR B . n 
B 1 67  THR 67  67  67  THR THR B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  PHE 71  71  71  PHE PHE B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  VAL 74  74  74  VAL VAL B . n 
B 1 75  GLY 75  75  75  GLY GLY B . n 
B 1 76  GLY 76  76  76  GLY GLY B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  ARG 80  80  80  ARG ARG B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  TYR 82  82  82  TYR TYR B . n 
B 1 83  GLU 83  83  83  GLU GLU B . n 
B 1 84  PRO 84  84  84  PRO PRO B . n 
B 1 85  ILE 85  85  85  ILE ILE B . n 
B 1 86  GLU 86  86  86  GLU GLU B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  ASP 88  88  88  ASP ASP B . n 
B 1 89  PHE 89  89  89  PHE PHE B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  PRO 91  91  91  PRO PRO B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  ILE 93  93  93  ILE ILE B . n 
B 1 94  SER 94  94  94  SER SER B . n 
B 1 95  GLU 95  95  95  GLU GLU B . n 
B 1 96  GLY 96  96  96  GLY GLY B . n 
B 1 97  ILE 97  97  97  ILE ILE B . n 
B 1 98  ARG 98  98  98  ARG ARG B . n 
B 1 99  GLU 99  99  99  GLU GLU B . n 
B 1 100 LEU 100 100 100 LEU LEU B . n 
B 1 101 GLY 101 101 101 GLY GLY B . n 
B 1 102 LEU 102 102 102 LEU LEU B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 GLU 106 106 106 GLU GLU B . n 
B 1 107 PRO 107 107 107 PRO PRO B . n 
B 1 108 TRP 108 108 108 TRP TRP B . n 
B 1 109 GLN 109 109 109 GLN GLN B . n 
B 1 110 ILE 110 110 110 ILE ILE B . n 
B 1 111 ASN 111 111 111 ASN ASN B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 HIS 113 113 113 HIS HIS B . n 
B 1 114 GLN 114 114 114 GLN GLN B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 ARG 116 116 116 ARG ARG B . n 
B 1 117 THR 117 117 117 THR THR B . n 
B 1 118 ARG 118 118 118 ARG ARG B . n 
B 1 119 ALA 119 119 119 ALA ALA B . n 
B 1 120 ASP 120 120 120 ASP ASP B . n 
B 1 121 GLY 121 121 121 GLY GLY B . n 
B 1 122 GLY 122 122 122 GLY GLY B . n 
B 1 123 ARG 123 123 123 ARG ARG B . n 
B 1 124 PRO 124 124 124 PRO PRO B . n 
B 1 125 GLY 125 125 125 GLY GLY B . n 
B 1 126 PRO 126 126 126 PRO PRO B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 THR 128 128 128 THR THR B . n 
B 1 129 PRO 129 129 129 PRO PRO B . n 
B 1 130 GLU 130 130 130 GLU GLU B . n 
B 1 131 GLY 131 131 131 GLY GLY B . n 
B 1 132 VAL 132 132 132 VAL VAL B . n 
B 1 133 HIS 133 133 133 HIS HIS B . n 
B 1 134 HIS 134 134 134 HIS HIS B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 GLY 136 136 136 GLY GLY B . n 
B 1 137 HIS 137 137 137 HIS HIS B . n 
B 1 138 GLU 138 138 138 GLU GLU B . n 
B 1 139 PHE 139 139 139 PHE PHE B . n 
B 1 140 VAL 140 140 140 VAL VAL B . n 
B 1 141 MET 141 141 141 MET MET B . n 
B 1 142 ILE 142 142 142 ILE ILE B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 ILE 144 144 144 ILE ILE B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 ASN 146 146 146 ASN ASN B . n 
B 1 147 LYS 147 147 147 LYS LYS B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 ASN 149 149 149 ASN ASN B . n 
B 1 150 VAL 150 150 150 VAL VAL B . n 
B 1 151 ALA 151 151 151 ALA ALA B . n 
B 1 152 GLY 152 152 152 GLY GLY B . n 
B 1 153 GLY 153 153 153 GLY GLY B . n 
B 1 154 THR 154 154 154 THR THR B . n 
B 1 155 THR 155 155 155 THR THR B . n 
B 1 156 ARG 156 156 156 ARG ARG B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 TRP 158 158 158 TRP TRP B . n 
B 1 159 LYS 159 159 159 LYS LYS B . n 
B 1 160 PRO 160 160 160 PRO PRO B . n 
B 1 161 GLY 161 161 161 GLY GLY B . n 
B 1 162 ALA 162 162 162 ALA ALA B . n 
B 1 163 ASP 163 163 163 ASP ASP B . n 
B 1 164 ALA 164 164 164 ALA ALA B . n 
B 1 165 PRO 165 165 165 PRO PRO B . n 
B 1 166 PHE 166 166 166 PHE PHE B . n 
B 1 167 TRP 167 167 167 TRP TRP B . n 
B 1 168 SER 168 168 168 SER SER B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 THR 170 170 170 THR THR B . n 
B 1 171 LEU 171 171 171 LEU LEU B . n 
B 1 172 GLU 172 172 172 GLU GLU B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 GLN 175 175 175 GLN GLN B . n 
B 1 176 ALA 176 176 176 ALA ALA B . n 
B 1 177 VAL 177 177 177 VAL VAL B . n 
B 1 178 LEU 178 178 178 LEU LEU B . n 
B 1 179 LEU 179 179 179 LEU LEU B . n 
B 1 180 ASP 180 180 180 ASP ASP B . n 
B 1 181 ASP 181 181 181 ASP ASP B . n 
B 1 182 ARG 182 182 182 ARG ARG B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 LEU 184 184 184 LEU LEU B . n 
B 1 185 ALA 185 185 185 ALA ALA B . n 
B 1 186 HIS 186 186 186 HIS HIS B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 VAL 188 188 188 VAL VAL B . n 
B 1 189 THR 189 189 189 THR THR B . n 
B 1 190 ASP 190 190 190 ASP ASP B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 LEU 192 192 192 LEU LEU B . n 
B 1 193 SER 193 193 193 SER SER B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 ASP 195 195 195 ASP ASP B . n 
B 1 196 GLY 196 196 196 GLY GLY B . n 
B 1 197 GLY 197 197 197 GLY GLY B . n 
B 1 198 PRO 198 198 198 PRO PRO B . n 
B 1 199 GLY 199 199 199 GLY GLY B . n 
B 1 200 HIS 200 200 200 HIS HIS B . n 
B 1 201 ARG 201 201 201 ARG ARG B . n 
B 1 202 ASP 202 202 202 ASP ASP B . n 
B 1 203 ILE 203 203 203 ILE ILE B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 ILE 205 205 205 ILE ILE B . n 
B 1 206 ILE 206 206 206 ILE ILE B . n 
B 1 207 ALA 207 207 207 ALA ALA B . n 
B 1 208 PHE 208 208 208 PHE PHE B . n 
B 1 209 SER 209 209 209 SER SER B . n 
B 1 210 ARG 210 210 210 ARG ARG B . n 
B 1 211 TRP 211 211 211 TRP TRP B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 GLU 213 213 213 GLU GLU B . n 
B 1 214 LYS 214 214 214 LYS LYS B . n 
B 1 215 TRP 215 215 215 TRP TRP B . n 
B 1 216 TYR 216 216 216 TYR TYR B . n 
B 1 217 GLY 217 217 217 GLY GLY B . n 
B 1 218 ASP 218 218 218 ASP ASP B . n 
B 1 219 GLU 219 219 219 GLU GLU B . n 
B 1 220 HIS 220 220 220 HIS HIS B . n 
B 1 221 ASP 221 221 221 ASP ASP B . n 
B 1 222 ALA 222 222 222 ALA ALA B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 GLU 226 226 226 GLU GLU B . n 
B 1 227 GLU 227 227 227 GLU GLU B . n 
B 1 228 GLN 228 228 ?   ?   ?   B . n 
B 1 229 GLU 229 229 ?   ?   ?   B . n 
B 1 230 ALA 230 230 ?   ?   ?   B . n 
B 1 231 HIS 231 231 ?   ?   ?   B . n 
B 1 232 HIS 232 232 ?   ?   ?   B . n 
B 1 233 HIS 233 233 ?   ?   ?   B . n 
B 1 234 HIS 234 234 ?   ?   ?   B . n 
B 1 235 HIS 235 235 ?   ?   ?   B . n 
B 1 236 HIS 236 236 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        6HN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   6HN 
_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 MN  1   301 301 MN  MN  A . 
D 3 AKG 1   302 302 AKG AKG A . 
E 4 6HN 1   303 303 6HN 6NK A . 
F 5 IOD 1   304 304 IOD IOD A . 
G 5 IOD 1   305 305 IOD IOD A . 
H 5 IOD 1   306 306 IOD IOD A . 
I 4 6HN 1   307 307 6HN 6NK A . 
J 2 MN  1   301 301 MN  MN  B . 
K 3 AKG 1   302 302 AKG AKG B . 
L 4 6HN 1   303 303 6HN 6NK B . 
M 5 IOD 1   304 304 IOD IOD B . 
N 5 IOD 1   305 305 IOD IOD B . 
O 5 IOD 1   306 306 IOD IOD B . 
P 5 IOD 1   307 308 IOD IOD B . 
Q 6 EDO 1   308 309 EDO EDO B . 
R 7 GOL 1   309 310 GOL GOL B . 
S 7 GOL 1   310 311 GOL GOL B . 
T 8 HOH 1   401 313 HOH HOH A . 
T 8 HOH 2   402 516 HOH HOH A . 
T 8 HOH 3   403 113 HOH HOH A . 
T 8 HOH 4   404 239 HOH HOH A . 
T 8 HOH 5   405 593 HOH HOH A . 
T 8 HOH 6   406 379 HOH HOH A . 
T 8 HOH 7   407 634 HOH HOH A . 
T 8 HOH 8   408 663 HOH HOH A . 
T 8 HOH 9   409 165 HOH HOH A . 
T 8 HOH 10  410 317 HOH HOH A . 
T 8 HOH 11  411 679 HOH HOH A . 
T 8 HOH 12  412 401 HOH HOH A . 
T 8 HOH 13  413 70  HOH HOH A . 
T 8 HOH 14  414 590 HOH HOH A . 
T 8 HOH 15  415 485 HOH HOH A . 
T 8 HOH 16  416 715 HOH HOH A . 
T 8 HOH 17  417 212 HOH HOH A . 
T 8 HOH 18  418 260 HOH HOH A . 
T 8 HOH 19  419 285 HOH HOH A . 
T 8 HOH 20  420 220 HOH HOH A . 
T 8 HOH 21  421 294 HOH HOH A . 
T 8 HOH 22  422 63  HOH HOH A . 
T 8 HOH 23  423 218 HOH HOH A . 
T 8 HOH 24  424 454 HOH HOH A . 
T 8 HOH 25  425 399 HOH HOH A . 
T 8 HOH 26  426 194 HOH HOH A . 
T 8 HOH 27  427 99  HOH HOH A . 
T 8 HOH 28  428 232 HOH HOH A . 
T 8 HOH 29  429 128 HOH HOH A . 
T 8 HOH 30  430 30  HOH HOH A . 
T 8 HOH 31  431 119 HOH HOH A . 
T 8 HOH 32  432 111 HOH HOH A . 
T 8 HOH 33  433 337 HOH HOH A . 
T 8 HOH 34  434 36  HOH HOH A . 
T 8 HOH 35  435 489 HOH HOH A . 
T 8 HOH 36  436 335 HOH HOH A . 
T 8 HOH 37  437 266 HOH HOH A . 
T 8 HOH 38  438 252 HOH HOH A . 
T 8 HOH 39  439 179 HOH HOH A . 
T 8 HOH 40  440 276 HOH HOH A . 
T 8 HOH 41  441 7   HOH HOH A . 
T 8 HOH 42  442 579 HOH HOH A . 
T 8 HOH 43  443 303 HOH HOH A . 
T 8 HOH 44  444 188 HOH HOH A . 
T 8 HOH 45  445 42  HOH HOH A . 
T 8 HOH 46  446 258 HOH HOH A . 
T 8 HOH 47  447 376 HOH HOH A . 
T 8 HOH 48  448 35  HOH HOH A . 
T 8 HOH 49  449 369 HOH HOH A . 
T 8 HOH 50  450 73  HOH HOH A . 
T 8 HOH 51  451 81  HOH HOH A . 
T 8 HOH 52  452 105 HOH HOH A . 
T 8 HOH 53  453 10  HOH HOH A . 
T 8 HOH 54  454 47  HOH HOH A . 
T 8 HOH 55  455 21  HOH HOH A . 
T 8 HOH 56  456 57  HOH HOH A . 
T 8 HOH 57  457 4   HOH HOH A . 
T 8 HOH 58  458 350 HOH HOH A . 
T 8 HOH 59  459 5   HOH HOH A . 
T 8 HOH 60  460 190 HOH HOH A . 
T 8 HOH 61  461 41  HOH HOH A . 
T 8 HOH 62  462 256 HOH HOH A . 
T 8 HOH 63  463 205 HOH HOH A . 
T 8 HOH 64  464 79  HOH HOH A . 
T 8 HOH 65  465 214 HOH HOH A . 
T 8 HOH 66  466 157 HOH HOH A . 
T 8 HOH 67  467 271 HOH HOH A . 
T 8 HOH 68  468 17  HOH HOH A . 
T 8 HOH 69  469 66  HOH HOH A . 
T 8 HOH 70  470 231 HOH HOH A . 
T 8 HOH 71  471 38  HOH HOH A . 
T 8 HOH 72  472 22  HOH HOH A . 
T 8 HOH 73  473 82  HOH HOH A . 
T 8 HOH 74  474 16  HOH HOH A . 
T 8 HOH 75  475 390 HOH HOH A . 
T 8 HOH 76  476 549 HOH HOH A . 
T 8 HOH 77  477 3   HOH HOH A . 
T 8 HOH 78  478 439 HOH HOH A . 
T 8 HOH 79  479 84  HOH HOH A . 
T 8 HOH 80  480 67  HOH HOH A . 
T 8 HOH 81  481 26  HOH HOH A . 
T 8 HOH 82  482 299 HOH HOH A . 
T 8 HOH 83  483 667 HOH HOH A . 
T 8 HOH 84  484 19  HOH HOH A . 
T 8 HOH 85  485 203 HOH HOH A . 
T 8 HOH 86  486 187 HOH HOH A . 
T 8 HOH 87  487 213 HOH HOH A . 
T 8 HOH 88  488 520 HOH HOH A . 
T 8 HOH 89  489 408 HOH HOH A . 
T 8 HOH 90  490 246 HOH HOH A . 
T 8 HOH 91  491 206 HOH HOH A . 
T 8 HOH 92  492 74  HOH HOH A . 
T 8 HOH 93  493 141 HOH HOH A . 
T 8 HOH 94  494 75  HOH HOH A . 
T 8 HOH 95  495 87  HOH HOH A . 
T 8 HOH 96  496 486 HOH HOH A . 
T 8 HOH 97  497 88  HOH HOH A . 
T 8 HOH 98  498 368 HOH HOH A . 
T 8 HOH 99  499 283 HOH HOH A . 
T 8 HOH 100 500 307 HOH HOH A . 
T 8 HOH 101 501 45  HOH HOH A . 
T 8 HOH 102 502 59  HOH HOH A . 
T 8 HOH 103 503 183 HOH HOH A . 
T 8 HOH 104 504 149 HOH HOH A . 
T 8 HOH 105 505 91  HOH HOH A . 
T 8 HOH 106 506 680 HOH HOH A . 
T 8 HOH 107 507 173 HOH HOH A . 
T 8 HOH 108 508 452 HOH HOH A . 
T 8 HOH 109 509 365 HOH HOH A . 
T 8 HOH 110 510 14  HOH HOH A . 
T 8 HOH 111 511 467 HOH HOH A . 
T 8 HOH 112 512 233 HOH HOH A . 
T 8 HOH 113 513 225 HOH HOH A . 
T 8 HOH 114 514 320 HOH HOH A . 
T 8 HOH 115 515 364 HOH HOH A . 
T 8 HOH 116 516 130 HOH HOH A . 
T 8 HOH 117 517 336 HOH HOH A . 
T 8 HOH 118 518 43  HOH HOH A . 
T 8 HOH 119 519 145 HOH HOH A . 
T 8 HOH 120 520 402 HOH HOH A . 
T 8 HOH 121 521 420 HOH HOH A . 
T 8 HOH 122 522 519 HOH HOH A . 
T 8 HOH 123 523 109 HOH HOH A . 
T 8 HOH 124 524 143 HOH HOH A . 
T 8 HOH 125 525 326 HOH HOH A . 
T 8 HOH 126 526 669 HOH HOH A . 
T 8 HOH 127 527 415 HOH HOH A . 
T 8 HOH 128 528 13  HOH HOH A . 
T 8 HOH 129 529 121 HOH HOH A . 
T 8 HOH 130 530 23  HOH HOH A . 
T 8 HOH 131 531 102 HOH HOH A . 
T 8 HOH 132 532 162 HOH HOH A . 
T 8 HOH 133 533 51  HOH HOH A . 
T 8 HOH 134 534 29  HOH HOH A . 
T 8 HOH 135 535 312 HOH HOH A . 
T 8 HOH 136 536 97  HOH HOH A . 
T 8 HOH 137 537 612 HOH HOH A . 
T 8 HOH 138 538 39  HOH HOH A . 
T 8 HOH 139 539 115 HOH HOH A . 
T 8 HOH 140 540 1   HOH HOH A . 
T 8 HOH 141 541 124 HOH HOH A . 
T 8 HOH 142 542 352 HOH HOH A . 
T 8 HOH 143 543 189 HOH HOH A . 
T 8 HOH 144 544 54  HOH HOH A . 
T 8 HOH 145 545 259 HOH HOH A . 
T 8 HOH 146 546 242 HOH HOH A . 
T 8 HOH 147 547 93  HOH HOH A . 
T 8 HOH 148 548 78  HOH HOH A . 
T 8 HOH 149 549 393 HOH HOH A . 
T 8 HOH 150 550 77  HOH HOH A . 
T 8 HOH 151 551 262 HOH HOH A . 
T 8 HOH 152 552 89  HOH HOH A . 
T 8 HOH 153 553 293 HOH HOH A . 
T 8 HOH 154 554 133 HOH HOH A . 
T 8 HOH 155 555 328 HOH HOH A . 
T 8 HOH 156 556 316 HOH HOH A . 
T 8 HOH 157 557 104 HOH HOH A . 
T 8 HOH 158 558 236 HOH HOH A . 
T 8 HOH 159 559 334 HOH HOH A . 
T 8 HOH 160 560 58  HOH HOH A . 
T 8 HOH 161 561 665 HOH HOH A . 
T 8 HOH 162 562 154 HOH HOH A . 
T 8 HOH 163 563 281 HOH HOH A . 
T 8 HOH 164 564 123 HOH HOH A . 
T 8 HOH 165 565 184 HOH HOH A . 
T 8 HOH 166 566 192 HOH HOH A . 
T 8 HOH 167 567 272 HOH HOH A . 
T 8 HOH 168 568 129 HOH HOH A . 
T 8 HOH 169 569 127 HOH HOH A . 
T 8 HOH 170 570 257 HOH HOH A . 
T 8 HOH 171 571 152 HOH HOH A . 
T 8 HOH 172 572 418 HOH HOH A . 
T 8 HOH 173 573 108 HOH HOH A . 
T 8 HOH 174 574 391 HOH HOH A . 
T 8 HOH 175 575 247 HOH HOH A . 
T 8 HOH 176 576 50  HOH HOH A . 
T 8 HOH 177 577 177 HOH HOH A . 
T 8 HOH 178 578 167 HOH HOH A . 
T 8 HOH 179 579 329 HOH HOH A . 
T 8 HOH 180 580 120 HOH HOH A . 
T 8 HOH 181 581 481 HOH HOH A . 
T 8 HOH 182 582 175 HOH HOH A . 
T 8 HOH 183 583 345 HOH HOH A . 
T 8 HOH 184 584 178 HOH HOH A . 
T 8 HOH 185 585 468 HOH HOH A . 
T 8 HOH 186 586 455 HOH HOH A . 
T 8 HOH 187 587 547 HOH HOH A . 
T 8 HOH 188 588 69  HOH HOH A . 
T 8 HOH 189 589 221 HOH HOH A . 
T 8 HOH 190 590 315 HOH HOH A . 
T 8 HOH 191 591 305 HOH HOH A . 
T 8 HOH 192 592 131 HOH HOH A . 
T 8 HOH 193 593 374 HOH HOH A . 
T 8 HOH 194 594 441 HOH HOH A . 
T 8 HOH 195 595 139 HOH HOH A . 
T 8 HOH 196 596 215 HOH HOH A . 
T 8 HOH 197 597 357 HOH HOH A . 
T 8 HOH 198 598 284 HOH HOH A . 
T 8 HOH 199 599 171 HOH HOH A . 
T 8 HOH 200 600 353 HOH HOH A . 
T 8 HOH 201 601 90  HOH HOH A . 
T 8 HOH 202 602 461 HOH HOH A . 
T 8 HOH 203 603 359 HOH HOH A . 
T 8 HOH 204 604 367 HOH HOH A . 
T 8 HOH 205 605 355 HOH HOH A . 
T 8 HOH 206 606 735 HOH HOH A . 
T 8 HOH 207 607 382 HOH HOH A . 
T 8 HOH 208 608 292 HOH HOH A . 
T 8 HOH 209 609 624 HOH HOH A . 
T 8 HOH 210 610 372 HOH HOH A . 
T 8 HOH 211 611 546 HOH HOH A . 
T 8 HOH 212 612 459 HOH HOH A . 
T 8 HOH 213 613 412 HOH HOH A . 
T 8 HOH 214 614 521 HOH HOH A . 
T 8 HOH 215 615 290 HOH HOH A . 
T 8 HOH 216 616 277 HOH HOH A . 
T 8 HOH 217 617 346 HOH HOH A . 
T 8 HOH 218 618 471 HOH HOH A . 
T 8 HOH 219 619 587 HOH HOH A . 
T 8 HOH 220 620 477 HOH HOH A . 
T 8 HOH 221 621 652 HOH HOH A . 
T 8 HOH 222 622 164 HOH HOH A . 
T 8 HOH 223 623 414 HOH HOH A . 
T 8 HOH 224 624 297 HOH HOH A . 
T 8 HOH 225 625 298 HOH HOH A . 
T 8 HOH 226 626 409 HOH HOH A . 
T 8 HOH 227 627 603 HOH HOH A . 
T 8 HOH 228 628 606 HOH HOH A . 
T 8 HOH 229 629 375 HOH HOH A . 
T 8 HOH 230 630 395 HOH HOH A . 
T 8 HOH 231 631 388 HOH HOH A . 
T 8 HOH 232 632 333 HOH HOH A . 
T 8 HOH 233 633 32  HOH HOH A . 
T 8 HOH 234 634 649 HOH HOH A . 
T 8 HOH 235 635 440 HOH HOH A . 
T 8 HOH 236 636 619 HOH HOH A . 
T 8 HOH 237 637 635 HOH HOH A . 
T 8 HOH 238 638 597 HOH HOH A . 
T 8 HOH 239 639 92  HOH HOH A . 
T 8 HOH 240 640 198 HOH HOH A . 
T 8 HOH 241 641 243 HOH HOH A . 
T 8 HOH 242 642 387 HOH HOH A . 
T 8 HOH 243 643 344 HOH HOH A . 
T 8 HOH 244 644 638 HOH HOH A . 
T 8 HOH 245 645 565 HOH HOH A . 
T 8 HOH 246 646 561 HOH HOH A . 
T 8 HOH 247 647 698 HOH HOH A . 
T 8 HOH 248 648 209 HOH HOH A . 
T 8 HOH 249 649 381 HOH HOH A . 
T 8 HOH 250 650 311 HOH HOH A . 
T 8 HOH 251 651 564 HOH HOH A . 
T 8 HOH 252 652 558 HOH HOH A . 
T 8 HOH 253 653 616 HOH HOH A . 
T 8 HOH 254 654 424 HOH HOH A . 
T 8 HOH 255 655 478 HOH HOH A . 
T 8 HOH 256 656 174 HOH HOH A . 
T 8 HOH 257 657 500 HOH HOH A . 
T 8 HOH 258 658 601 HOH HOH A . 
T 8 HOH 259 659 466 HOH HOH A . 
T 8 HOH 260 660 526 HOH HOH A . 
T 8 HOH 261 661 309 HOH HOH A . 
T 8 HOH 262 662 464 HOH HOH A . 
T 8 HOH 263 663 492 HOH HOH A . 
T 8 HOH 264 664 245 HOH HOH A . 
T 8 HOH 265 665 251 HOH HOH A . 
T 8 HOH 266 666 46  HOH HOH A . 
T 8 HOH 267 667 330 HOH HOH A . 
T 8 HOH 268 668 416 HOH HOH A . 
T 8 HOH 269 669 712 HOH HOH A . 
T 8 HOH 270 670 327 HOH HOH A . 
T 8 HOH 271 671 609 HOH HOH A . 
T 8 HOH 272 672 195 HOH HOH A . 
T 8 HOH 273 673 411 HOH HOH A . 
T 8 HOH 274 674 227 HOH HOH A . 
T 8 HOH 275 675 398 HOH HOH A . 
T 8 HOH 276 676 449 HOH HOH A . 
T 8 HOH 277 677 241 HOH HOH A . 
T 8 HOH 278 678 706 HOH HOH A . 
T 8 HOH 279 679 404 HOH HOH A . 
T 8 HOH 280 680 261 HOH HOH A . 
T 8 HOH 281 681 718 HOH HOH A . 
T 8 HOH 282 682 640 HOH HOH A . 
T 8 HOH 283 683 421 HOH HOH A . 
U 8 HOH 1   401 15  HOH HOH B . 
U 8 HOH 2   402 160 HOH HOH B . 
U 8 HOH 3   403 371 HOH HOH B . 
U 8 HOH 4   404 295 HOH HOH B . 
U 8 HOH 5   405 318 HOH HOH B . 
U 8 HOH 6   406 253 HOH HOH B . 
U 8 HOH 7   407 433 HOH HOH B . 
U 8 HOH 8   408 363 HOH HOH B . 
U 8 HOH 9   409 339 HOH HOH B . 
U 8 HOH 10  410 585 HOH HOH B . 
U 8 HOH 11  411 642 HOH HOH B . 
U 8 HOH 12  412 117 HOH HOH B . 
U 8 HOH 13  413 126 HOH HOH B . 
U 8 HOH 14  414 18  HOH HOH B . 
U 8 HOH 15  415 573 HOH HOH B . 
U 8 HOH 16  416 94  HOH HOH B . 
U 8 HOH 17  417 44  HOH HOH B . 
U 8 HOH 18  418 443 HOH HOH B . 
U 8 HOH 19  419 574 HOH HOH B . 
U 8 HOH 20  420 249 HOH HOH B . 
U 8 HOH 21  421 103 HOH HOH B . 
U 8 HOH 22  422 349 HOH HOH B . 
U 8 HOH 23  423 101 HOH HOH B . 
U 8 HOH 24  424 172 HOH HOH B . 
U 8 HOH 25  425 60  HOH HOH B . 
U 8 HOH 26  426 106 HOH HOH B . 
U 8 HOH 27  427 410 HOH HOH B . 
U 8 HOH 28  428 453 HOH HOH B . 
U 8 HOH 29  429 62  HOH HOH B . 
U 8 HOH 30  430 618 HOH HOH B . 
U 8 HOH 31  431 400 HOH HOH B . 
U 8 HOH 32  432 153 HOH HOH B . 
U 8 HOH 33  433 65  HOH HOH B . 
U 8 HOH 34  434 599 HOH HOH B . 
U 8 HOH 35  435 24  HOH HOH B . 
U 8 HOH 36  436 144 HOH HOH B . 
U 8 HOH 37  437 136 HOH HOH B . 
U 8 HOH 38  438 34  HOH HOH B . 
U 8 HOH 39  439 85  HOH HOH B . 
U 8 HOH 40  440 287 HOH HOH B . 
U 8 HOH 41  441 341 HOH HOH B . 
U 8 HOH 42  442 255 HOH HOH B . 
U 8 HOH 43  443 180 HOH HOH B . 
U 8 HOH 44  444 650 HOH HOH B . 
U 8 HOH 45  445 40  HOH HOH B . 
U 8 HOH 46  446 219 HOH HOH B . 
U 8 HOH 47  447 169 HOH HOH B . 
U 8 HOH 48  448 48  HOH HOH B . 
U 8 HOH 49  449 197 HOH HOH B . 
U 8 HOH 50  450 135 HOH HOH B . 
U 8 HOH 51  451 168 HOH HOH B . 
U 8 HOH 52  452 392 HOH HOH B . 
U 8 HOH 53  453 53  HOH HOH B . 
U 8 HOH 54  454 11  HOH HOH B . 
U 8 HOH 55  455 80  HOH HOH B . 
U 8 HOH 56  456 291 HOH HOH B . 
U 8 HOH 57  457 600 HOH HOH B . 
U 8 HOH 58  458 61  HOH HOH B . 
U 8 HOH 59  459 314 HOH HOH B . 
U 8 HOH 60  460 33  HOH HOH B . 
U 8 HOH 61  461 289 HOH HOH B . 
U 8 HOH 62  462 122 HOH HOH B . 
U 8 HOH 63  463 118 HOH HOH B . 
U 8 HOH 64  464 268 HOH HOH B . 
U 8 HOH 65  465 31  HOH HOH B . 
U 8 HOH 66  466 140 HOH HOH B . 
U 8 HOH 67  467 224 HOH HOH B . 
U 8 HOH 68  468 527 HOH HOH B . 
U 8 HOH 69  469 49  HOH HOH B . 
U 8 HOH 70  470 25  HOH HOH B . 
U 8 HOH 71  471 138 HOH HOH B . 
U 8 HOH 72  472 8   HOH HOH B . 
U 8 HOH 73  473 156 HOH HOH B . 
U 8 HOH 74  474 76  HOH HOH B . 
U 8 HOH 75  475 147 HOH HOH B . 
U 8 HOH 76  476 2   HOH HOH B . 
U 8 HOH 77  477 193 HOH HOH B . 
U 8 HOH 78  478 199 HOH HOH B . 
U 8 HOH 79  479 159 HOH HOH B . 
U 8 HOH 80  480 332 HOH HOH B . 
U 8 HOH 81  481 125 HOH HOH B . 
U 8 HOH 82  482 56  HOH HOH B . 
U 8 HOH 83  483 28  HOH HOH B . 
U 8 HOH 84  484 9   HOH HOH B . 
U 8 HOH 85  485 377 HOH HOH B . 
U 8 HOH 86  486 280 HOH HOH B . 
U 8 HOH 87  487 72  HOH HOH B . 
U 8 HOH 88  488 55  HOH HOH B . 
U 8 HOH 89  489 550 HOH HOH B . 
U 8 HOH 90  490 176 HOH HOH B . 
U 8 HOH 91  491 274 HOH HOH B . 
U 8 HOH 92  492 204 HOH HOH B . 
U 8 HOH 93  493 52  HOH HOH B . 
U 8 HOH 94  494 6   HOH HOH B . 
U 8 HOH 95  495 132 HOH HOH B . 
U 8 HOH 96  496 71  HOH HOH B . 
U 8 HOH 97  497 155 HOH HOH B . 
U 8 HOH 98  498 304 HOH HOH B . 
U 8 HOH 99  499 437 HOH HOH B . 
U 8 HOH 100 500 479 HOH HOH B . 
U 8 HOH 101 501 646 HOH HOH B . 
U 8 HOH 102 502 458 HOH HOH B . 
U 8 HOH 103 503 265 HOH HOH B . 
U 8 HOH 104 504 158 HOH HOH B . 
U 8 HOH 105 505 340 HOH HOH B . 
U 8 HOH 106 506 110 HOH HOH B . 
U 8 HOH 107 507 191 HOH HOH B . 
U 8 HOH 108 508 378 HOH HOH B . 
U 8 HOH 109 509 324 HOH HOH B . 
U 8 HOH 110 510 554 HOH HOH B . 
U 8 HOH 111 511 279 HOH HOH B . 
U 8 HOH 112 512 95  HOH HOH B . 
U 8 HOH 113 513 385 HOH HOH B . 
U 8 HOH 114 514 182 HOH HOH B . 
U 8 HOH 115 515 100 HOH HOH B . 
U 8 HOH 116 516 86  HOH HOH B . 
U 8 HOH 117 517 736 HOH HOH B . 
U 8 HOH 118 518 484 HOH HOH B . 
U 8 HOH 119 519 116 HOH HOH B . 
U 8 HOH 120 520 226 HOH HOH B . 
U 8 HOH 121 521 254 HOH HOH B . 
U 8 HOH 122 522 264 HOH HOH B . 
U 8 HOH 123 523 325 HOH HOH B . 
U 8 HOH 124 524 278 HOH HOH B . 
U 8 HOH 125 525 185 HOH HOH B . 
U 8 HOH 126 526 64  HOH HOH B . 
U 8 HOH 127 527 487 HOH HOH B . 
U 8 HOH 128 528 267 HOH HOH B . 
U 8 HOH 129 529 68  HOH HOH B . 
U 8 HOH 130 530 457 HOH HOH B . 
U 8 HOH 131 531 142 HOH HOH B . 
U 8 HOH 132 532 269 HOH HOH B . 
U 8 HOH 133 533 98  HOH HOH B . 
U 8 HOH 134 534 306 HOH HOH B . 
U 8 HOH 135 535 522 HOH HOH B . 
U 8 HOH 136 536 426 HOH HOH B . 
U 8 HOH 137 537 282 HOH HOH B . 
U 8 HOH 138 538 322 HOH HOH B . 
U 8 HOH 139 539 196 HOH HOH B . 
U 8 HOH 140 540 237 HOH HOH B . 
U 8 HOH 141 541 210 HOH HOH B . 
U 8 HOH 142 542 134 HOH HOH B . 
U 8 HOH 143 543 235 HOH HOH B . 
U 8 HOH 144 544 137 HOH HOH B . 
U 8 HOH 145 545 456 HOH HOH B . 
U 8 HOH 146 546 240 HOH HOH B . 
U 8 HOH 147 547 286 HOH HOH B . 
U 8 HOH 148 548 20  HOH HOH B . 
U 8 HOH 149 549 146 HOH HOH B . 
U 8 HOH 150 550 107 HOH HOH B . 
U 8 HOH 151 551 83  HOH HOH B . 
U 8 HOH 152 552 112 HOH HOH B . 
U 8 HOH 153 553 222 HOH HOH B . 
U 8 HOH 154 554 244 HOH HOH B . 
U 8 HOH 155 555 230 HOH HOH B . 
U 8 HOH 156 556 300 HOH HOH B . 
U 8 HOH 157 557 451 HOH HOH B . 
U 8 HOH 158 558 460 HOH HOH B . 
U 8 HOH 159 559 96  HOH HOH B . 
U 8 HOH 160 560 681 HOH HOH B . 
U 8 HOH 161 561 148 HOH HOH B . 
U 8 HOH 162 562 216 HOH HOH B . 
U 8 HOH 163 563 163 HOH HOH B . 
U 8 HOH 164 564 343 HOH HOH B . 
U 8 HOH 165 565 150 HOH HOH B . 
U 8 HOH 166 566 533 HOH HOH B . 
U 8 HOH 167 567 200 HOH HOH B . 
U 8 HOH 168 568 575 HOH HOH B . 
U 8 HOH 169 569 370 HOH HOH B . 
U 8 HOH 170 570 351 HOH HOH B . 
U 8 HOH 171 571 360 HOH HOH B . 
U 8 HOH 172 572 535 HOH HOH B . 
U 8 HOH 173 573 462 HOH HOH B . 
U 8 HOH 174 574 27  HOH HOH B . 
U 8 HOH 175 575 405 HOH HOH B . 
U 8 HOH 176 576 596 HOH HOH B . 
U 8 HOH 177 577 362 HOH HOH B . 
U 8 HOH 178 578 166 HOH HOH B . 
U 8 HOH 179 579 610 HOH HOH B . 
U 8 HOH 180 580 623 HOH HOH B . 
U 8 HOH 181 581 250 HOH HOH B . 
U 8 HOH 182 582 12  HOH HOH B . 
U 8 HOH 183 583 114 HOH HOH B . 
U 8 HOH 184 584 229 HOH HOH B . 
U 8 HOH 185 585 429 HOH HOH B . 
U 8 HOH 186 586 436 HOH HOH B . 
U 8 HOH 187 587 361 HOH HOH B . 
U 8 HOH 188 588 373 HOH HOH B . 
U 8 HOH 189 589 37  HOH HOH B . 
U 8 HOH 190 590 217 HOH HOH B . 
U 8 HOH 191 591 170 HOH HOH B . 
U 8 HOH 192 592 511 HOH HOH B . 
U 8 HOH 193 593 386 HOH HOH B . 
U 8 HOH 194 594 394 HOH HOH B . 
U 8 HOH 195 595 186 HOH HOH B . 
U 8 HOH 196 596 419 HOH HOH B . 
U 8 HOH 197 597 321 HOH HOH B . 
U 8 HOH 198 598 721 HOH HOH B . 
U 8 HOH 199 599 498 HOH HOH B . 
U 8 HOH 200 600 510 HOH HOH B . 
U 8 HOH 201 601 544 HOH HOH B . 
U 8 HOH 202 602 518 HOH HOH B . 
U 8 HOH 203 603 560 HOH HOH B . 
U 8 HOH 204 604 545 HOH HOH B . 
U 8 HOH 205 605 625 HOH HOH B . 
U 8 HOH 206 606 296 HOH HOH B . 
U 8 HOH 207 607 366 HOH HOH B . 
U 8 HOH 208 608 627 HOH HOH B . 
U 8 HOH 209 609 447 HOH HOH B . 
U 8 HOH 210 610 531 HOH HOH B . 
U 8 HOH 211 611 613 HOH HOH B . 
U 8 HOH 212 612 211 HOH HOH B . 
U 8 HOH 213 613 201 HOH HOH B . 
U 8 HOH 214 614 358 HOH HOH B . 
U 8 HOH 215 615 431 HOH HOH B . 
U 8 HOH 216 616 208 HOH HOH B . 
U 8 HOH 217 617 207 HOH HOH B . 
U 8 HOH 218 618 536 HOH HOH B . 
U 8 HOH 219 619 611 HOH HOH B . 
U 8 HOH 220 620 348 HOH HOH B . 
U 8 HOH 221 621 496 HOH HOH B . 
U 8 HOH 222 622 161 HOH HOH B . 
U 8 HOH 223 623 475 HOH HOH B . 
U 8 HOH 224 624 552 HOH HOH B . 
U 8 HOH 225 625 181 HOH HOH B . 
U 8 HOH 226 626 248 HOH HOH B . 
U 8 HOH 227 627 435 HOH HOH B . 
U 8 HOH 228 628 517 HOH HOH B . 
U 8 HOH 229 629 557 HOH HOH B . 
U 8 HOH 230 630 389 HOH HOH B . 
U 8 HOH 231 631 263 HOH HOH B . 
U 8 HOH 232 632 422 HOH HOH B . 
U 8 HOH 233 633 228 HOH HOH B . 
U 8 HOH 234 634 383 HOH HOH B . 
U 8 HOH 235 635 275 HOH HOH B . 
U 8 HOH 236 636 503 HOH HOH B . 
U 8 HOH 237 637 507 HOH HOH B . 
U 8 HOH 238 638 396 HOH HOH B . 
U 8 HOH 239 639 483 HOH HOH B . 
U 8 HOH 240 640 310 HOH HOH B . 
U 8 HOH 241 641 581 HOH HOH B . 
U 8 HOH 242 642 223 HOH HOH B . 
U 8 HOH 243 643 425 HOH HOH B . 
U 8 HOH 244 644 524 HOH HOH B . 
U 8 HOH 245 645 568 HOH HOH B . 
U 8 HOH 246 646 658 HOH HOH B . 
U 8 HOH 247 647 508 HOH HOH B . 
U 8 HOH 248 648 555 HOH HOH B . 
U 8 HOH 249 649 442 HOH HOH B . 
U 8 HOH 250 650 678 HOH HOH B . 
U 8 HOH 251 651 566 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.21 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrysalisPro ? ? ? .    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .    4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.032 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DQ1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     44.342 
_cell.length_a_esd                 ? 
_cell.length_b                     74.971 
_cell.length_b_esd                 ? 
_cell.length_c                     87.295 
_cell.length_c_esd                 ? 
_cell.volume                       290195.774 
_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                         9DQ1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_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                   9DQ1 
_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             2.74 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.08 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '0.2 M NaI; 0.1 M bis-tris propane, pH 6.5; 20% (w/v) PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER R 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-02-14 
_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   1.54184 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54184 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          13.09 
_reflns.entry_id                                       9DQ1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.90 
_reflns.d_resolution_low                               17.73 
_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                                     45410 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.077 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.90 
_reflns_shell.d_res_low                                     1.94 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           5.1 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3010 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.955 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               17.36 
_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                                 9DQ1 
_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                            1.90 
_refine.ls_d_res_low                             17.49 
_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                     44729 
_refine.ls_number_reflns_R_free                  2326 
_refine.ls_number_reflns_R_work                  42403 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.16 
_refine.ls_percent_reflns_R_free                 5.20 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1760 
_refine.ls_R_factor_R_free                       0.2039 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1745 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.6584 
_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                            0.1650 
_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                       1.90 
_refine_hist.d_res_low                        17.49 
_refine_hist.number_atoms_solvent             534 
_refine_hist.number_atoms_total               4179 
_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        3564 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         81 
_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' ? 0.0075  ? 3741 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0458  ? 5082 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0619  ? 524  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0106  ? 680  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.5561 ? 1366 ? f_dihedral_angle_d ? ? 
# 
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' 1.90 1.94  . . 149 2457 97.64 . . . . 0.2194 . . . . . . . . . . . 0.2888 
'X-RAY DIFFRACTION' 1.94 1.98  . . 124 2452 98.21 . . . . 0.1832 . . . . . . . . . . . 0.2289 
'X-RAY DIFFRACTION' 1.98 2.03  . . 152 2453 98.30 . . . . 0.1818 . . . . . . . . . . . 0.2351 
'X-RAY DIFFRACTION' 2.03 2.08  . . 147 2442 98.40 . . . . 0.1715 . . . . . . . . . . . 0.2307 
'X-RAY DIFFRACTION' 2.08 2.13  . . 121 2477 98.71 . . . . 0.1794 . . . . . . . . . . . 0.2180 
'X-RAY DIFFRACTION' 2.13 2.20  . . 122 2489 99.05 . . . . 0.1762 . . . . . . . . . . . 0.2050 
'X-RAY DIFFRACTION' 2.20 2.27  . . 128 2479 99.20 . . . . 0.1744 . . . . . . . . . . . 0.1954 
'X-RAY DIFFRACTION' 2.27 2.35  . . 137 2531 99.26 . . . . 0.1632 . . . . . . . . . . . 0.1991 
'X-RAY DIFFRACTION' 2.35 2.44  . . 127 2490 99.47 . . . . 0.1701 . . . . . . . . . . . 0.1907 
'X-RAY DIFFRACTION' 2.44 2.55  . . 149 2464 99.62 . . . . 0.1771 . . . . . . . . . . . 0.1964 
'X-RAY DIFFRACTION' 2.55 2.69  . . 145 2492 99.55 . . . . 0.1760 . . . . . . . . . . . 0.2232 
'X-RAY DIFFRACTION' 2.69 2.85  . . 131 2511 99.77 . . . . 0.1844 . . . . . . . . . . . 0.2263 
'X-RAY DIFFRACTION' 2.85 3.07  . . 155 2488 99.96 . . . . 0.1871 . . . . . . . . . . . 0.2199 
'X-RAY DIFFRACTION' 3.07 3.38  . . 123 2569 99.85 . . . . 0.1729 . . . . . . . . . . . 0.2121 
'X-RAY DIFFRACTION' 3.38 3.87  . . 137 2492 99.70 . . . . 0.1567 . . . . . . . . . . . 0.1914 
'X-RAY DIFFRACTION' 3.87 4.85  . . 142 2557 99.85 . . . . 0.1497 . . . . . . . . . . . 0.1543 
'X-RAY DIFFRACTION' 4.85 17.49 . . 137 2560 99.37 . . . . 0.1977 . . . . . . . . . . . 0.1866 
# 
_struct.entry_id                     9DQ1 
_struct.title                        
;Crystal structure of HrmJ from Streptomyces sp. CFMR 7 (HrmJ-ssc) complexed with manganese (II), 2-oxoglutarate and 6-nitronorleucine
;
_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        9DQ1 
_struct_keywords.text            'cyclopropanase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 4 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
P N N 5 ? 
Q N N 6 ? 
R N N 7 ? 
S N N 7 ? 
T N N 8 ? 
U N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0M5J3M0_9ACTN 
_struct_ref.pdbx_db_accession          A0A0M5J3M0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPLGTEGFTVIDLPEVAPDILPSYDRCPVDDYMGNGTRFKRFSQYKLTPAEDDTWSFKRLPHRDYTTYKKFNPVGGGIRR
VYEPIEVDFTPLISEGIRELGLDRSEPWQINVHQNRTRADGGRPGPLTPEGVHHDGHEFVMIAILNKVNVAGGTTRLWKP
GADAPFWSGTLEAGQAVLLDDRGLAHDVTDVLSADGGPGHRDIVIIAFSRWAEKWYGDEHDAAALEEQEA
;
_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 9DQ1 A 1 ? 230 ? A0A0M5J3M0 1 ? 230 ? 1 230 
2 1 9DQ1 B 1 ? 230 ? A0A0M5J3M0 1 ? 230 ? 1 230 
# 
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 9DQ1 HIS A 231 ? UNP A0A0M5J3M0 ? ? 'expression tag' 231 1  
1 9DQ1 HIS A 232 ? UNP A0A0M5J3M0 ? ? 'expression tag' 232 2  
1 9DQ1 HIS A 233 ? UNP A0A0M5J3M0 ? ? 'expression tag' 233 3  
1 9DQ1 HIS A 234 ? UNP A0A0M5J3M0 ? ? 'expression tag' 234 4  
1 9DQ1 HIS A 235 ? UNP A0A0M5J3M0 ? ? 'expression tag' 235 5  
1 9DQ1 HIS A 236 ? UNP A0A0M5J3M0 ? ? 'expression tag' 236 6  
2 9DQ1 HIS B 231 ? UNP A0A0M5J3M0 ? ? 'expression tag' 231 7  
2 9DQ1 HIS B 232 ? UNP A0A0M5J3M0 ? ? 'expression tag' 232 8  
2 9DQ1 HIS B 233 ? UNP A0A0M5J3M0 ? ? 'expression tag' 233 9  
2 9DQ1 HIS B 234 ? UNP A0A0M5J3M0 ? ? 'expression tag' 234 10 
2 9DQ1 HIS B 235 ? UNP A0A0M5J3M0 ? ? 'expression tag' 235 11 
2 9DQ1 HIS B 236 ? UNP A0A0M5J3M0 ? ? 'expression tag' 236 12 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 19  ? TYR A 24  ? ASP A 19  TYR A 24  1 ? 6  
HELX_P HELX_P2  AA2 ASP A 25  ? CYS A 27  ? ASP A 25  CYS A 27  5 ? 3  
HELX_P HELX_P3  AA3 PHE A 89  ? GLY A 101 ? PHE A 89  GLY A 101 1 ? 13 
HELX_P HELX_P4  AA4 ALA A 212 ? LYS A 214 ? ALA A 212 LYS A 214 5 ? 3  
HELX_P HELX_P5  AA5 GLY A 217 ? GLU A 226 ? GLY A 217 GLU A 226 1 ? 10 
HELX_P HELX_P6  AA6 ASP B 19  ? TYR B 24  ? ASP B 19  TYR B 24  1 ? 6  
HELX_P HELX_P7  AA7 ASP B 25  ? CYS B 27  ? ASP B 25  CYS B 27  5 ? 3  
HELX_P HELX_P8  AA8 PHE B 89  ? GLY B 101 ? PHE B 89  GLY B 101 1 ? 13 
HELX_P HELX_P9  AA9 ALA B 212 ? LYS B 214 ? ALA B 212 LYS B 214 5 ? 3  
HELX_P HELX_P10 AB1 GLY B 217 ? LEU B 225 ? GLY B 217 LEU B 225 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A HIS 133 NE2 ? ? ? 1_555 C MN  . MN ? ? A HIS 133 A MN  301 1_555 ? ? ? ? ? ? ? 2.294 ? ? 
metalc2  metalc ? ? A ASP 135 OD1 ? ? ? 1_555 C MN  . MN ? ? A ASP 135 A MN  301 1_555 ? ? ? ? ? ? ? 2.197 ? ? 
metalc3  metalc ? ? A ASP 135 OD2 ? ? ? 1_555 C MN  . MN ? ? A ASP 135 A MN  301 1_555 ? ? ? ? ? ? ? 2.477 ? ? 
metalc4  metalc ? ? A HIS 186 NE2 ? ? ? 1_555 C MN  . MN ? ? A HIS 186 A MN  301 1_555 ? ? ? ? ? ? ? 2.224 ? ? 
metalc5  metalc ? ? C MN  .   MN  ? ? ? 1_555 D AKG . O5 ? ? A MN  301 A AKG 302 1_555 ? ? ? ? ? ? ? 2.165 ? ? 
metalc6  metalc ? ? C MN  .   MN  ? ? ? 1_555 T HOH . O  ? ? A MN  301 A HOH 403 1_555 ? ? ? ? ? ? ? 2.395 ? ? 
metalc7  metalc ? ? B HIS 133 NE2 ? ? ? 1_555 J MN  . MN ? ? B HIS 133 B MN  301 1_555 ? ? ? ? ? ? ? 2.256 ? ? 
metalc8  metalc ? ? B ASP 135 OD1 ? ? ? 1_555 J MN  . MN ? ? B ASP 135 B MN  301 1_555 ? ? ? ? ? ? ? 2.200 ? ? 
metalc9  metalc ? ? B ASP 135 OD2 ? ? ? 1_555 J MN  . MN ? ? B ASP 135 B MN  301 1_555 ? ? ? ? ? ? ? 2.410 ? ? 
metalc10 metalc ? ? B HIS 186 NE2 ? ? ? 1_555 J MN  . MN ? ? B HIS 186 B MN  301 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc11 metalc ? ? J MN  .   MN  ? ? ? 1_555 K AKG . O5 ? ? B MN  301 B AKG 302 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc12 metalc ? ? J MN  .   MN  ? ? ? 1_555 K AKG . O2 ? ? B MN  301 B AKG 302 1_555 ? ? ? ? ? ? ? 2.103 ? ? 
metalc13 metalc ? ? J MN  .   MN  ? ? ? 1_555 U HOH . O  ? ? B MN  301 B HOH 402 1_555 ? ? ? ? ? ? ? 2.450 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 133 ? A HIS 133 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 OD1 ? A ASP 135 ? A ASP 135 ? 1_555 79.8  ? 
2  NE2 ? A HIS 133 ? A HIS 133 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 OD2 ? A ASP 135 ? A ASP 135 ? 1_555 128.8 ? 
3  OD1 ? A ASP 135 ? A ASP 135 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 OD2 ? A ASP 135 ? A ASP 135 ? 1_555 53.0  ? 
4  NE2 ? A HIS 133 ? A HIS 133 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 NE2 ? A HIS 186 ? A HIS 186 ? 1_555 83.6  ? 
5  OD1 ? A ASP 135 ? A ASP 135 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 NE2 ? A HIS 186 ? A HIS 186 ? 1_555 109.7 ? 
6  OD2 ? A ASP 135 ? A ASP 135 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 NE2 ? A HIS 186 ? A HIS 186 ? 1_555 94.0  ? 
7  NE2 ? A HIS 133 ? A HIS 133 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O5  ? D AKG .   ? A AKG 302 ? 1_555 103.5 ? 
8  OD1 ? A ASP 135 ? A ASP 135 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O5  ? D AKG .   ? A AKG 302 ? 1_555 174.8 ? 
9  OD2 ? A ASP 135 ? A ASP 135 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O5  ? D AKG .   ? A AKG 302 ? 1_555 125.3 ? 
10 NE2 ? A HIS 186 ? A HIS 186 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O5  ? D AKG .   ? A AKG 302 ? 1_555 74.8  ? 
11 NE2 ? A HIS 133 ? A HIS 133 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? T HOH .   ? A HOH 403 ? 1_555 178.7 ? 
12 OD1 ? A ASP 135 ? A ASP 135 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? T HOH .   ? A HOH 403 ? 1_555 99.1  ? 
13 OD2 ? A ASP 135 ? A ASP 135 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? T HOH .   ? A HOH 403 ? 1_555 50.4  ? 
14 NE2 ? A HIS 186 ? A HIS 186 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? T HOH .   ? A HOH 403 ? 1_555 97.4  ? 
15 O5  ? D AKG .   ? A AKG 302 ? 1_555 MN ? C MN . ? A MN 301 ? 1_555 O   ? T HOH .   ? A HOH 403 ? 1_555 77.6  ? 
16 NE2 ? B HIS 133 ? B HIS 133 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 OD1 ? B ASP 135 ? B ASP 135 ? 1_555 76.0  ? 
17 NE2 ? B HIS 133 ? B HIS 133 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 OD2 ? B ASP 135 ? B ASP 135 ? 1_555 128.8 ? 
18 OD1 ? B ASP 135 ? B ASP 135 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 OD2 ? B ASP 135 ? B ASP 135 ? 1_555 54.3  ? 
19 NE2 ? B HIS 133 ? B HIS 133 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 NE2 ? B HIS 186 ? B HIS 186 ? 1_555 85.7  ? 
20 OD1 ? B ASP 135 ? B ASP 135 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 NE2 ? B HIS 186 ? B HIS 186 ? 1_555 104.0 ? 
21 OD2 ? B ASP 135 ? B ASP 135 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 NE2 ? B HIS 186 ? B HIS 186 ? 1_555 94.3  ? 
22 NE2 ? B HIS 133 ? B HIS 133 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O5  ? K AKG .   ? B AKG 302 ? 1_555 107.8 ? 
23 OD1 ? B ASP 135 ? B ASP 135 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O5  ? K AKG .   ? B AKG 302 ? 1_555 172.9 ? 
24 OD2 ? B ASP 135 ? B ASP 135 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O5  ? K AKG .   ? B AKG 302 ? 1_555 122.9 ? 
25 NE2 ? B HIS 186 ? B HIS 186 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O5  ? K AKG .   ? B AKG 302 ? 1_555 82.5  ? 
26 NE2 ? B HIS 133 ? B HIS 133 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O2  ? K AKG .   ? B AKG 302 ? 1_555 95.9  ? 
27 OD1 ? B ASP 135 ? B ASP 135 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O2  ? K AKG .   ? B AKG 302 ? 1_555 100.6 ? 
28 OD2 ? B ASP 135 ? B ASP 135 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O2  ? K AKG .   ? B AKG 302 ? 1_555 103.8 ? 
29 NE2 ? B HIS 186 ? B HIS 186 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O2  ? K AKG .   ? B AKG 302 ? 1_555 154.9 ? 
30 O5  ? K AKG .   ? B AKG 302 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O2  ? K AKG .   ? B AKG 302 ? 1_555 73.2  ? 
31 NE2 ? B HIS 133 ? B HIS 133 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O   ? U HOH .   ? B HOH 402 ? 1_555 177.0 ? 
32 OD1 ? B ASP 135 ? B ASP 135 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O   ? U HOH .   ? B HOH 402 ? 1_555 104.1 ? 
33 OD2 ? B ASP 135 ? B ASP 135 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O   ? U HOH .   ? B HOH 402 ? 1_555 52.0  ? 
34 NE2 ? B HIS 186 ? B HIS 186 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O   ? U HOH .   ? B HOH 402 ? 1_555 97.2  ? 
35 O5  ? K AKG .   ? B AKG 302 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O   ? U HOH .   ? B HOH 402 ? 1_555 71.8  ? 
36 O2  ? K AKG .   ? B AKG 302 ? 1_555 MN ? J MN . ? B MN 301 ? 1_555 O   ? U HOH .   ? B HOH 402 ? 1_555 81.1  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 2 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 8   ? ASP A 12  ? PHE A 8   ASP A 12  
AA1 2 GLN A 175 ? ASP A 180 ? GLN A 175 ASP A 180 
AA1 3 PHE A 139 ? VAL A 148 ? PHE A 139 VAL A 148 
AA1 4 GLY A 199 ? ARG A 210 ? GLY A 199 ARG A 210 
AA1 5 TRP A 108 ? ALA A 119 ? TRP A 108 ALA A 119 
AA1 6 ARG A 38  ? ALA A 50  ? ARG A 38  ALA A 50  
AA1 7 THR A 54  ? ARG A 59  ? THR A 54  ARG A 59  
AA2 1 VAL A 150 ? GLY A 152 ? VAL A 150 GLY A 152 
AA2 2 VAL A 191 ? SER A 193 ? VAL A 191 SER A 193 
AA3 1 TRP A 167 ? THR A 170 ? TRP A 167 THR A 170 
AA3 2 THR A 154 ? TRP A 158 ? THR A 154 TRP A 158 
AA3 3 ALA A 185 ? VAL A 188 ? ALA A 185 VAL A 188 
AA4 1 PHE B 8   ? ASP B 12  ? PHE B 8   ASP B 12  
AA4 2 GLN B 175 ? ASP B 180 ? GLN B 175 ASP B 180 
AA4 3 PHE B 139 ? VAL B 148 ? PHE B 139 VAL B 148 
AA4 4 GLY B 199 ? ARG B 210 ? GLY B 199 ARG B 210 
AA4 5 TRP B 108 ? ALA B 119 ? TRP B 108 ALA B 119 
AA4 6 ARG B 38  ? PRO B 49  ? ARG B 38  PRO B 49  
AA4 7 TRP B 55  ? ARG B 59  ? TRP B 55  ARG B 59  
AA5 1 VAL B 150 ? GLY B 152 ? VAL B 150 GLY B 152 
AA5 2 VAL B 191 ? SER B 193 ? VAL B 191 SER B 193 
AA6 1 TRP B 167 ? THR B 170 ? TRP B 167 THR B 170 
AA6 2 THR B 154 ? TRP B 158 ? THR B 154 TRP B 158 
AA6 3 ALA B 185 ? VAL B 188 ? ALA B 185 VAL B 188 
# 
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 THR A 9   ? N THR A 9   O LEU A 178 ? O LEU A 178 
AA1 2 3 O GLN A 175 ? O GLN A 175 N ILE A 144 ? N ILE A 144 
AA1 3 4 N ASN A 146 ? N ASN A 146 O ASP A 202 ? O ASP A 202 
AA1 4 5 O SER A 209 ? O SER A 209 N GLN A 109 ? N GLN A 109 
AA1 5 6 O TRP A 108 ? O TRP A 108 N LEU A 47  ? N LEU A 47  
AA1 6 7 N THR A 48  ? N THR A 48  O SER A 56  ? O SER A 56  
AA2 1 2 N ALA A 151 ? N ALA A 151 O LEU A 192 ? O LEU A 192 
AA3 1 2 O TRP A 167 ? O TRP A 167 N LEU A 157 ? N LEU A 157 
AA3 2 3 N TRP A 158 ? N TRP A 158 O ALA A 185 ? O ALA A 185 
AA4 1 2 N THR B 9   ? N THR B 9   O LEU B 178 ? O LEU B 178 
AA4 2 3 O GLN B 175 ? O GLN B 175 N ILE B 144 ? N ILE B 144 
AA4 3 4 N PHE B 139 ? N PHE B 139 O PHE B 208 ? O PHE B 208 
AA4 4 5 O SER B 209 ? O SER B 209 N GLN B 109 ? N GLN B 109 
AA4 5 6 O TRP B 108 ? O TRP B 108 N LEU B 47  ? N LEU B 47  
AA4 6 7 N LYS B 46  ? N LYS B 46  O LYS B 58  ? O LYS B 58  
AA5 1 2 N ALA B 151 ? N ALA B 151 O LEU B 192 ? O LEU B 192 
AA6 1 2 O TRP B 167 ? O TRP B 167 N LEU B 157 ? N LEU B 157 
AA6 2 3 N TRP B 158 ? N TRP B 158 O ALA B 185 ? O ALA B 185 
# 
_pdbx_entry_details.entry_id                   9DQ1 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 587 ? ? O  A HOH 612 ? ? 1.52 
2  1 O   A HOH 404 ? ? O  A HOH 606 ? ? 1.56 
3  1 MN  A MN  301 ? ? O2 A AKG 302 ? ? 1.60 
4  1 O   B HOH 485 ? ? O  B HOH 501 ? ? 1.75 
5  1 NZ  B LYS 40  ? ? O  B HOH 401 ? ? 1.84 
6  1 O   B HOH 430 ? ? O  B HOH 602 ? ? 1.90 
7  1 O   A HOH 428 ? ? O  A HOH 537 ? ? 1.92 
8  1 O   A HOH 407 ? ? O  A HOH 476 ? ? 1.92 
9  1 O   A HOH 407 ? ? O  A HOH 559 ? ? 1.95 
10 1 O   A HOH 483 ? ? O  A HOH 594 ? ? 1.95 
11 1 O   A HOH 571 ? ? O  A HOH 614 ? ? 1.96 
12 1 NH2 A ARG 79  ? ? O  A HOH 401 ? ? 1.99 
13 1 O   A HOH 624 ? ? O  B HOH 599 ? ? 2.00 
14 1 O   B HOH 639 ? ? O  B HOH 644 ? ? 2.01 
15 1 NH1 A ARG 118 ? ? O  A HOH 402 ? ? 2.07 
16 1 OD2 A ASP 135 ? ? O  A HOH 403 ? ? 2.08 
17 1 NH2 A ARG 118 ? ? O  A HOH 404 ? ? 2.09 
18 1 O   A HOH 488 ? ? O  A HOH 660 ? ? 2.12 
19 1 O   A HOH 423 ? ? O  A HOH 658 ? ? 2.12 
20 1 O   A HOH 629 ? ? O  A HOH 657 ? ? 2.12 
21 1 O   A HOH 651 ? ? O  A HOH 660 ? ? 2.12 
22 1 OD2 B ASP 135 ? ? O  B HOH 402 ? ? 2.13 
23 1 O   B HOH 441 ? ? O  B HOH 581 ? ? 2.13 
24 1 O   A HOH 584 ? ? O  A HOH 642 ? ? 2.16 
25 1 O   A HOH 549 ? ? O  A HOH 650 ? ? 2.16 
26 1 O   A HOH 645 ? ? O  A HOH 652 ? ? 2.16 
27 1 O   A PRO 2   ? ? O  A HOH 405 ? ? 2.17 
28 1 O   A HOH 402 ? ? O  A HOH 574 ? ? 2.18 
29 1 O   B HOH 461 ? ? O  B HOH 596 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O  B HOH 580 ? ? 1_555 O  B HOH 593 ? ? 2_555 1.62 
2 1 O  A HOH 620 ? ? 1_555 O  A HOH 654 ? ? 1_455 1.78 
3 1 O  A HOH 522 ? ? 1_555 O  A HOH 644 ? ? 2_646 1.94 
4 1 O  B HOH 586 ? ? 1_555 O  B HOH 591 ? ? 1_455 2.03 
5 1 O3 B GOL 309 ? ? 1_555 O1 B GOL 310 ? ? 2_545 2.10 
6 1 O  A HOH 418 ? ? 1_555 O  A HOH 602 ? ? 2_656 2.13 
7 1 O  A HOH 408 ? ? 1_555 O  A HOH 443 ? ? 2_646 2.15 
8 1 O  A HOH 506 ? ? 1_555 O  A HOH 644 ? ? 2_646 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 51  ? ? -48.15  153.22  
2 1 HIS A 137 ? ? -102.96 -165.74 
3 1 TRP A 215 ? ? -96.72  52.64   
4 1 ASP B 52  ? ? 70.59   -167.87 
5 1 ASP B 53  ? ? -95.48  44.44   
6 1 TRP B 215 ? ? -91.38  52.96   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
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 GLN 228 ? A GLN 228 
3  1 Y 1 A GLU 229 ? A GLU 229 
4  1 Y 1 A ALA 230 ? A ALA 230 
5  1 Y 1 A HIS 231 ? A HIS 231 
6  1 Y 1 A HIS 232 ? A HIS 232 
7  1 Y 1 A HIS 233 ? A HIS 233 
8  1 Y 1 A HIS 234 ? A HIS 234 
9  1 Y 1 A HIS 235 ? A HIS 235 
10 1 Y 1 A HIS 236 ? A HIS 236 
11 1 Y 1 B MET 1   ? B MET 1   
12 1 Y 1 B GLN 228 ? B GLN 228 
13 1 Y 1 B GLU 229 ? B GLU 229 
14 1 Y 1 B ALA 230 ? B ALA 230 
15 1 Y 1 B HIS 231 ? B HIS 231 
16 1 Y 1 B HIS 232 ? B HIS 232 
17 1 Y 1 B HIS 233 ? B HIS 233 
18 1 Y 1 B HIS 234 ? B HIS 234 
19 1 Y 1 B HIS 235 ? B HIS 235 
20 1 Y 1 B HIS 236 ? B HIS 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 
6HN N1   N  N N 1   
6HN N    N  N N 2   
6HN CA   C  N S 3   
6HN C    C  N N 4   
6HN OXT  O  N N 5   
6HN O    O  N N 6   
6HN CB   C  N N 7   
6HN CG   C  N N 8   
6HN CD   C  N N 9   
6HN CE   C  N N 10  
6HN O2   O  N N 11  
6HN O1   O  N N 12  
6HN H    H  N N 13  
6HN HN2  H  N N 14  
6HN HA   H  N N 15  
6HN HB   H  N N 16  
6HN HBA  H  N N 17  
6HN HG   H  N N 18  
6HN HGA  H  N N 19  
6HN HD   H  N N 20  
6HN HDA  H  N N 21  
6HN HE   H  N N 22  
6HN HEA  H  N N 23  
6HN HXT  H  N N 24  
AKG C1   C  N N 25  
AKG O1   O  N N 26  
AKG O2   O  N N 27  
AKG C2   C  N N 28  
AKG O5   O  N N 29  
AKG C3   C  N N 30  
AKG C4   C  N N 31  
AKG C5   C  N N 32  
AKG O3   O  N N 33  
AKG O4   O  N N 34  
AKG HO2  H  N N 35  
AKG H31  H  N N 36  
AKG H32  H  N N 37  
AKG H41  H  N N 38  
AKG H42  H  N N 39  
AKG HO4  H  N N 40  
ALA N    N  N N 41  
ALA CA   C  N S 42  
ALA C    C  N N 43  
ALA O    O  N N 44  
ALA CB   C  N N 45  
ALA OXT  O  N N 46  
ALA H    H  N N 47  
ALA H2   H  N N 48  
ALA HA   H  N N 49  
ALA HB1  H  N N 50  
ALA HB2  H  N N 51  
ALA HB3  H  N N 52  
ALA HXT  H  N N 53  
ARG N    N  N N 54  
ARG CA   C  N S 55  
ARG C    C  N N 56  
ARG O    O  N N 57  
ARG CB   C  N N 58  
ARG CG   C  N N 59  
ARG CD   C  N N 60  
ARG NE   N  N N 61  
ARG CZ   C  N N 62  
ARG NH1  N  N N 63  
ARG NH2  N  N N 64  
ARG OXT  O  N N 65  
ARG H    H  N N 66  
ARG H2   H  N N 67  
ARG HA   H  N N 68  
ARG HB2  H  N N 69  
ARG HB3  H  N N 70  
ARG HG2  H  N N 71  
ARG HG3  H  N N 72  
ARG HD2  H  N N 73  
ARG HD3  H  N N 74  
ARG HE   H  N N 75  
ARG HH11 H  N N 76  
ARG HH12 H  N N 77  
ARG HH21 H  N N 78  
ARG HH22 H  N N 79  
ARG HXT  H  N N 80  
ASN N    N  N N 81  
ASN CA   C  N S 82  
ASN C    C  N N 83  
ASN O    O  N N 84  
ASN CB   C  N N 85  
ASN CG   C  N N 86  
ASN OD1  O  N N 87  
ASN ND2  N  N N 88  
ASN OXT  O  N N 89  
ASN H    H  N N 90  
ASN H2   H  N N 91  
ASN HA   H  N N 92  
ASN HB2  H  N N 93  
ASN HB3  H  N N 94  
ASN HD21 H  N N 95  
ASN HD22 H  N N 96  
ASN HXT  H  N N 97  
ASP N    N  N N 98  
ASP CA   C  N S 99  
ASP C    C  N N 100 
ASP O    O  N N 101 
ASP CB   C  N N 102 
ASP CG   C  N N 103 
ASP OD1  O  N N 104 
ASP OD2  O  N N 105 
ASP OXT  O  N N 106 
ASP H    H  N N 107 
ASP H2   H  N N 108 
ASP HA   H  N N 109 
ASP HB2  H  N N 110 
ASP HB3  H  N N 111 
ASP HD2  H  N N 112 
ASP HXT  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 
EDO C1   C  N N 128 
EDO O1   O  N N 129 
EDO C2   C  N N 130 
EDO O2   O  N N 131 
EDO H11  H  N N 132 
EDO H12  H  N N 133 
EDO HO1  H  N N 134 
EDO H21  H  N N 135 
EDO H22  H  N N 136 
EDO HO2  H  N N 137 
GLN N    N  N N 138 
GLN CA   C  N S 139 
GLN C    C  N N 140 
GLN O    O  N N 141 
GLN CB   C  N N 142 
GLN CG   C  N N 143 
GLN CD   C  N N 144 
GLN OE1  O  N N 145 
GLN NE2  N  N N 146 
GLN OXT  O  N N 147 
GLN H    H  N N 148 
GLN H2   H  N N 149 
GLN HA   H  N N 150 
GLN HB2  H  N N 151 
GLN HB3  H  N N 152 
GLN HG2  H  N N 153 
GLN HG3  H  N N 154 
GLN HE21 H  N N 155 
GLN HE22 H  N N 156 
GLN HXT  H  N N 157 
GLU N    N  N N 158 
GLU CA   C  N S 159 
GLU C    C  N N 160 
GLU O    O  N N 161 
GLU CB   C  N N 162 
GLU CG   C  N N 163 
GLU CD   C  N N 164 
GLU OE1  O  N N 165 
GLU OE2  O  N N 166 
GLU OXT  O  N N 167 
GLU H    H  N N 168 
GLU H2   H  N N 169 
GLU HA   H  N N 170 
GLU HB2  H  N N 171 
GLU HB3  H  N N 172 
GLU HG2  H  N N 173 
GLU HG3  H  N N 174 
GLU HE2  H  N N 175 
GLU HXT  H  N N 176 
GLY N    N  N N 177 
GLY CA   C  N N 178 
GLY C    C  N N 179 
GLY O    O  N N 180 
GLY OXT  O  N N 181 
GLY H    H  N N 182 
GLY H2   H  N N 183 
GLY HA2  H  N N 184 
GLY HA3  H  N N 185 
GLY HXT  H  N N 186 
GOL C1   C  N N 187 
GOL O1   O  N N 188 
GOL C2   C  N N 189 
GOL O2   O  N N 190 
GOL C3   C  N N 191 
GOL O3   O  N N 192 
GOL H11  H  N N 193 
GOL H12  H  N N 194 
GOL HO1  H  N N 195 
GOL H2   H  N N 196 
GOL HO2  H  N N 197 
GOL H31  H  N N 198 
GOL H32  H  N N 199 
GOL HO3  H  N N 200 
HIS N    N  N N 201 
HIS CA   C  N S 202 
HIS C    C  N N 203 
HIS O    O  N N 204 
HIS CB   C  N N 205 
HIS CG   C  Y N 206 
HIS ND1  N  Y N 207 
HIS CD2  C  Y N 208 
HIS CE1  C  Y N 209 
HIS NE2  N  Y N 210 
HIS OXT  O  N N 211 
HIS H    H  N N 212 
HIS H2   H  N N 213 
HIS HA   H  N N 214 
HIS HB2  H  N N 215 
HIS HB3  H  N N 216 
HIS HD1  H  N N 217 
HIS HD2  H  N N 218 
HIS HE1  H  N N 219 
HIS HE2  H  N N 220 
HIS HXT  H  N N 221 
HOH O    O  N N 222 
HOH H1   H  N N 223 
HOH H2   H  N N 224 
ILE N    N  N N 225 
ILE CA   C  N S 226 
ILE C    C  N N 227 
ILE O    O  N N 228 
ILE CB   C  N S 229 
ILE CG1  C  N N 230 
ILE CG2  C  N N 231 
ILE CD1  C  N N 232 
ILE OXT  O  N N 233 
ILE H    H  N N 234 
ILE H2   H  N N 235 
ILE HA   H  N N 236 
ILE HB   H  N N 237 
ILE HG12 H  N N 238 
ILE HG13 H  N N 239 
ILE HG21 H  N N 240 
ILE HG22 H  N N 241 
ILE HG23 H  N N 242 
ILE HD11 H  N N 243 
ILE HD12 H  N N 244 
ILE HD13 H  N N 245 
ILE HXT  H  N N 246 
IOD I    I  N N 247 
LEU N    N  N N 248 
LEU CA   C  N S 249 
LEU C    C  N N 250 
LEU O    O  N N 251 
LEU CB   C  N N 252 
LEU CG   C  N N 253 
LEU CD1  C  N N 254 
LEU CD2  C  N N 255 
LEU OXT  O  N N 256 
LEU H    H  N N 257 
LEU H2   H  N N 258 
LEU HA   H  N N 259 
LEU HB2  H  N N 260 
LEU HB3  H  N N 261 
LEU HG   H  N N 262 
LEU HD11 H  N N 263 
LEU HD12 H  N N 264 
LEU HD13 H  N N 265 
LEU HD21 H  N N 266 
LEU HD22 H  N N 267 
LEU HD23 H  N N 268 
LEU HXT  H  N N 269 
LYS N    N  N N 270 
LYS CA   C  N S 271 
LYS C    C  N N 272 
LYS O    O  N N 273 
LYS CB   C  N N 274 
LYS CG   C  N N 275 
LYS CD   C  N N 276 
LYS CE   C  N N 277 
LYS NZ   N  N N 278 
LYS OXT  O  N N 279 
LYS H    H  N N 280 
LYS H2   H  N N 281 
LYS HA   H  N N 282 
LYS HB2  H  N N 283 
LYS HB3  H  N N 284 
LYS HG2  H  N N 285 
LYS HG3  H  N N 286 
LYS HD2  H  N N 287 
LYS HD3  H  N N 288 
LYS HE2  H  N N 289 
LYS HE3  H  N N 290 
LYS HZ1  H  N N 291 
LYS HZ2  H  N N 292 
LYS HZ3  H  N N 293 
LYS HXT  H  N N 294 
MET N    N  N N 295 
MET CA   C  N S 296 
MET C    C  N N 297 
MET O    O  N N 298 
MET CB   C  N N 299 
MET CG   C  N N 300 
MET SD   S  N N 301 
MET CE   C  N N 302 
MET OXT  O  N N 303 
MET H    H  N N 304 
MET H2   H  N N 305 
MET HA   H  N N 306 
MET HB2  H  N N 307 
MET HB3  H  N N 308 
MET HG2  H  N N 309 
MET HG3  H  N N 310 
MET HE1  H  N N 311 
MET HE2  H  N N 312 
MET HE3  H  N N 313 
MET HXT  H  N N 314 
MN  MN   MN N N 315 
PHE N    N  N N 316 
PHE CA   C  N S 317 
PHE C    C  N N 318 
PHE O    O  N N 319 
PHE CB   C  N N 320 
PHE CG   C  Y N 321 
PHE CD1  C  Y N 322 
PHE CD2  C  Y N 323 
PHE CE1  C  Y N 324 
PHE CE2  C  Y N 325 
PHE CZ   C  Y N 326 
PHE OXT  O  N N 327 
PHE H    H  N N 328 
PHE H2   H  N N 329 
PHE HA   H  N N 330 
PHE HB2  H  N N 331 
PHE HB3  H  N N 332 
PHE HD1  H  N N 333 
PHE HD2  H  N N 334 
PHE HE1  H  N N 335 
PHE HE2  H  N N 336 
PHE HZ   H  N N 337 
PHE HXT  H  N N 338 
PRO N    N  N N 339 
PRO CA   C  N S 340 
PRO C    C  N N 341 
PRO O    O  N N 342 
PRO CB   C  N N 343 
PRO CG   C  N N 344 
PRO CD   C  N N 345 
PRO OXT  O  N N 346 
PRO H    H  N N 347 
PRO HA   H  N N 348 
PRO HB2  H  N N 349 
PRO HB3  H  N N 350 
PRO HG2  H  N N 351 
PRO HG3  H  N N 352 
PRO HD2  H  N N 353 
PRO HD3  H  N N 354 
PRO HXT  H  N N 355 
SER N    N  N N 356 
SER CA   C  N S 357 
SER C    C  N N 358 
SER O    O  N N 359 
SER CB   C  N N 360 
SER OG   O  N N 361 
SER OXT  O  N N 362 
SER H    H  N N 363 
SER H2   H  N N 364 
SER HA   H  N N 365 
SER HB2  H  N N 366 
SER HB3  H  N N 367 
SER HG   H  N N 368 
SER HXT  H  N N 369 
THR N    N  N N 370 
THR CA   C  N S 371 
THR C    C  N N 372 
THR O    O  N N 373 
THR CB   C  N R 374 
THR OG1  O  N N 375 
THR CG2  C  N N 376 
THR OXT  O  N N 377 
THR H    H  N N 378 
THR H2   H  N N 379 
THR HA   H  N N 380 
THR HB   H  N N 381 
THR HG1  H  N N 382 
THR HG21 H  N N 383 
THR HG22 H  N N 384 
THR HG23 H  N N 385 
THR HXT  H  N N 386 
TRP N    N  N N 387 
TRP CA   C  N S 388 
TRP C    C  N N 389 
TRP O    O  N N 390 
TRP CB   C  N N 391 
TRP CG   C  Y N 392 
TRP CD1  C  Y N 393 
TRP CD2  C  Y N 394 
TRP NE1  N  Y N 395 
TRP CE2  C  Y N 396 
TRP CE3  C  Y N 397 
TRP CZ2  C  Y N 398 
TRP CZ3  C  Y N 399 
TRP CH2  C  Y N 400 
TRP OXT  O  N N 401 
TRP H    H  N N 402 
TRP H2   H  N N 403 
TRP HA   H  N N 404 
TRP HB2  H  N N 405 
TRP HB3  H  N N 406 
TRP HD1  H  N N 407 
TRP HE1  H  N N 408 
TRP HE3  H  N N 409 
TRP HZ2  H  N N 410 
TRP HZ3  H  N N 411 
TRP HH2  H  N N 412 
TRP HXT  H  N N 413 
TYR N    N  N N 414 
TYR CA   C  N S 415 
TYR C    C  N N 416 
TYR O    O  N N 417 
TYR CB   C  N N 418 
TYR CG   C  Y N 419 
TYR CD1  C  Y N 420 
TYR CD2  C  Y N 421 
TYR CE1  C  Y N 422 
TYR CE2  C  Y N 423 
TYR CZ   C  Y N 424 
TYR OH   O  N N 425 
TYR OXT  O  N N 426 
TYR H    H  N N 427 
TYR H2   H  N N 428 
TYR HA   H  N N 429 
TYR HB2  H  N N 430 
TYR HB3  H  N N 431 
TYR HD1  H  N N 432 
TYR HD2  H  N N 433 
TYR HE1  H  N N 434 
TYR HE2  H  N N 435 
TYR HH   H  N N 436 
TYR HXT  H  N N 437 
VAL N    N  N N 438 
VAL CA   C  N S 439 
VAL C    C  N N 440 
VAL O    O  N N 441 
VAL CB   C  N N 442 
VAL CG1  C  N N 443 
VAL CG2  C  N N 444 
VAL OXT  O  N N 445 
VAL H    H  N N 446 
VAL H2   H  N N 447 
VAL HA   H  N N 448 
VAL HB   H  N N 449 
VAL HG11 H  N N 450 
VAL HG12 H  N N 451 
VAL HG13 H  N N 452 
VAL HG21 H  N N 453 
VAL HG22 H  N N 454 
VAL HG23 H  N N 455 
VAL HXT  H  N N 456 
# 
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 
6HN N1  CE   sing N N 1   
6HN N1  O2   doub N N 2   
6HN N1  O1   sing N N 3   
6HN N   CA   sing N N 4   
6HN N   H    sing N N 5   
6HN N   HN2  sing N N 6   
6HN CA  C    sing N N 7   
6HN CA  CB   sing N N 8   
6HN CA  HA   sing N N 9   
6HN C   OXT  sing N N 10  
6HN C   O    doub N N 11  
6HN CB  CG   sing N N 12  
6HN CB  HB   sing N N 13  
6HN CB  HBA  sing N N 14  
6HN CG  CD   sing N N 15  
6HN CG  HG   sing N N 16  
6HN CG  HGA  sing N N 17  
6HN CD  CE   sing N N 18  
6HN CD  HD   sing N N 19  
6HN CD  HDA  sing N N 20  
6HN CE  HE   sing N N 21  
6HN CE  HEA  sing N N 22  
6HN OXT HXT  sing N N 23  
AKG C1  O1   doub N N 24  
AKG C1  O2   sing N N 25  
AKG C1  C2   sing N N 26  
AKG O2  HO2  sing N N 27  
AKG C2  O5   doub N N 28  
AKG C2  C3   sing N N 29  
AKG C3  C4   sing N N 30  
AKG C3  H31  sing N N 31  
AKG C3  H32  sing N N 32  
AKG C4  C5   sing N N 33  
AKG C4  H41  sing N N 34  
AKG C4  H42  sing N N 35  
AKG C5  O3   doub N N 36  
AKG C5  O4   sing N N 37  
AKG O4  HO4  sing N N 38  
ALA N   CA   sing N N 39  
ALA N   H    sing N N 40  
ALA N   H2   sing N N 41  
ALA CA  C    sing N N 42  
ALA CA  CB   sing N N 43  
ALA CA  HA   sing N N 44  
ALA C   O    doub N N 45  
ALA C   OXT  sing N N 46  
ALA CB  HB1  sing N N 47  
ALA CB  HB2  sing N N 48  
ALA CB  HB3  sing N N 49  
ALA OXT HXT  sing N N 50  
ARG N   CA   sing N N 51  
ARG N   H    sing N N 52  
ARG N   H2   sing N N 53  
ARG CA  C    sing N N 54  
ARG CA  CB   sing N N 55  
ARG CA  HA   sing N N 56  
ARG C   O    doub N N 57  
ARG C   OXT  sing N N 58  
ARG CB  CG   sing N N 59  
ARG CB  HB2  sing N N 60  
ARG CB  HB3  sing N N 61  
ARG CG  CD   sing N N 62  
ARG CG  HG2  sing N N 63  
ARG CG  HG3  sing N N 64  
ARG CD  NE   sing N N 65  
ARG CD  HD2  sing N N 66  
ARG CD  HD3  sing N N 67  
ARG NE  CZ   sing N N 68  
ARG NE  HE   sing N N 69  
ARG CZ  NH1  sing N N 70  
ARG CZ  NH2  doub N N 71  
ARG NH1 HH11 sing N N 72  
ARG NH1 HH12 sing N N 73  
ARG NH2 HH21 sing N N 74  
ARG NH2 HH22 sing N N 75  
ARG OXT HXT  sing N N 76  
ASN N   CA   sing N N 77  
ASN N   H    sing N N 78  
ASN N   H2   sing N N 79  
ASN CA  C    sing N N 80  
ASN CA  CB   sing N N 81  
ASN CA  HA   sing N N 82  
ASN C   O    doub N N 83  
ASN C   OXT  sing N N 84  
ASN CB  CG   sing N N 85  
ASN CB  HB2  sing N N 86  
ASN CB  HB3  sing N N 87  
ASN CG  OD1  doub N N 88  
ASN CG  ND2  sing N N 89  
ASN ND2 HD21 sing N N 90  
ASN ND2 HD22 sing N N 91  
ASN OXT HXT  sing N N 92  
ASP N   CA   sing N N 93  
ASP N   H    sing N N 94  
ASP N   H2   sing N N 95  
ASP CA  C    sing N N 96  
ASP CA  CB   sing N N 97  
ASP CA  HA   sing N N 98  
ASP C   O    doub N N 99  
ASP C   OXT  sing N N 100 
ASP CB  CG   sing N N 101 
ASP CB  HB2  sing N N 102 
ASP CB  HB3  sing N N 103 
ASP CG  OD1  doub N N 104 
ASP CG  OD2  sing N N 105 
ASP OD2 HD2  sing N N 106 
ASP OXT HXT  sing N N 107 
CYS N   CA   sing N N 108 
CYS N   H    sing N N 109 
CYS N   H2   sing N N 110 
CYS CA  C    sing N N 111 
CYS CA  CB   sing N N 112 
CYS CA  HA   sing N N 113 
CYS C   O    doub N N 114 
CYS C   OXT  sing N N 115 
CYS CB  SG   sing N N 116 
CYS CB  HB2  sing N N 117 
CYS CB  HB3  sing N N 118 
CYS SG  HG   sing N N 119 
CYS OXT HXT  sing N N 120 
EDO C1  O1   sing N N 121 
EDO C1  C2   sing N N 122 
EDO C1  H11  sing N N 123 
EDO C1  H12  sing N N 124 
EDO O1  HO1  sing N N 125 
EDO C2  O2   sing N N 126 
EDO C2  H21  sing N N 127 
EDO C2  H22  sing N N 128 
EDO O2  HO2  sing N N 129 
GLN N   CA   sing N N 130 
GLN N   H    sing N N 131 
GLN N   H2   sing N N 132 
GLN CA  C    sing N N 133 
GLN CA  CB   sing N N 134 
GLN CA  HA   sing N N 135 
GLN C   O    doub N N 136 
GLN C   OXT  sing N N 137 
GLN CB  CG   sing N N 138 
GLN CB  HB2  sing N N 139 
GLN CB  HB3  sing N N 140 
GLN CG  CD   sing N N 141 
GLN CG  HG2  sing N N 142 
GLN CG  HG3  sing N N 143 
GLN CD  OE1  doub N N 144 
GLN CD  NE2  sing N N 145 
GLN NE2 HE21 sing N N 146 
GLN NE2 HE22 sing N N 147 
GLN OXT HXT  sing N N 148 
GLU N   CA   sing N N 149 
GLU N   H    sing N N 150 
GLU N   H2   sing N N 151 
GLU CA  C    sing N N 152 
GLU CA  CB   sing N N 153 
GLU CA  HA   sing N N 154 
GLU C   O    doub N N 155 
GLU C   OXT  sing N N 156 
GLU CB  CG   sing N N 157 
GLU CB  HB2  sing N N 158 
GLU CB  HB3  sing N N 159 
GLU CG  CD   sing N N 160 
GLU CG  HG2  sing N N 161 
GLU CG  HG3  sing N N 162 
GLU CD  OE1  doub N N 163 
GLU CD  OE2  sing N N 164 
GLU OE2 HE2  sing N N 165 
GLU OXT HXT  sing N N 166 
GLY N   CA   sing N N 167 
GLY N   H    sing N N 168 
GLY N   H2   sing N N 169 
GLY CA  C    sing N N 170 
GLY CA  HA2  sing N N 171 
GLY CA  HA3  sing N N 172 
GLY C   O    doub N N 173 
GLY C   OXT  sing N N 174 
GLY OXT HXT  sing N N 175 
GOL C1  O1   sing N N 176 
GOL C1  C2   sing N N 177 
GOL C1  H11  sing N N 178 
GOL C1  H12  sing N N 179 
GOL O1  HO1  sing N N 180 
GOL C2  O2   sing N N 181 
GOL C2  C3   sing N N 182 
GOL C2  H2   sing N N 183 
GOL O2  HO2  sing N N 184 
GOL C3  O3   sing N N 185 
GOL C3  H31  sing N N 186 
GOL C3  H32  sing N N 187 
GOL O3  HO3  sing N N 188 
HIS N   CA   sing N N 189 
HIS N   H    sing N N 190 
HIS N   H2   sing N N 191 
HIS CA  C    sing N N 192 
HIS CA  CB   sing N N 193 
HIS CA  HA   sing N N 194 
HIS C   O    doub N N 195 
HIS C   OXT  sing N N 196 
HIS CB  CG   sing N N 197 
HIS CB  HB2  sing N N 198 
HIS CB  HB3  sing N N 199 
HIS CG  ND1  sing Y N 200 
HIS CG  CD2  doub Y N 201 
HIS ND1 CE1  doub Y N 202 
HIS ND1 HD1  sing N N 203 
HIS CD2 NE2  sing Y N 204 
HIS CD2 HD2  sing N N 205 
HIS CE1 NE2  sing Y N 206 
HIS CE1 HE1  sing N N 207 
HIS NE2 HE2  sing N N 208 
HIS OXT HXT  sing N N 209 
HOH O   H1   sing N N 210 
HOH O   H2   sing N N 211 
ILE N   CA   sing N N 212 
ILE N   H    sing N N 213 
ILE N   H2   sing N N 214 
ILE CA  C    sing N N 215 
ILE CA  CB   sing N N 216 
ILE CA  HA   sing N N 217 
ILE C   O    doub N N 218 
ILE C   OXT  sing N N 219 
ILE CB  CG1  sing N N 220 
ILE CB  CG2  sing N N 221 
ILE CB  HB   sing N N 222 
ILE CG1 CD1  sing N N 223 
ILE CG1 HG12 sing N N 224 
ILE CG1 HG13 sing N N 225 
ILE CG2 HG21 sing N N 226 
ILE CG2 HG22 sing N N 227 
ILE CG2 HG23 sing N N 228 
ILE CD1 HD11 sing N N 229 
ILE CD1 HD12 sing N N 230 
ILE CD1 HD13 sing N N 231 
ILE OXT HXT  sing N N 232 
LEU N   CA   sing N N 233 
LEU N   H    sing N N 234 
LEU N   H2   sing N N 235 
LEU CA  C    sing N N 236 
LEU CA  CB   sing N N 237 
LEU CA  HA   sing N N 238 
LEU C   O    doub N N 239 
LEU C   OXT  sing N N 240 
LEU CB  CG   sing N N 241 
LEU CB  HB2  sing N N 242 
LEU CB  HB3  sing N N 243 
LEU CG  CD1  sing N N 244 
LEU CG  CD2  sing N N 245 
LEU CG  HG   sing N N 246 
LEU CD1 HD11 sing N N 247 
LEU CD1 HD12 sing N N 248 
LEU CD1 HD13 sing N N 249 
LEU CD2 HD21 sing N N 250 
LEU CD2 HD22 sing N N 251 
LEU CD2 HD23 sing N N 252 
LEU OXT HXT  sing N N 253 
LYS N   CA   sing N N 254 
LYS N   H    sing N N 255 
LYS N   H2   sing N N 256 
LYS CA  C    sing N N 257 
LYS CA  CB   sing N N 258 
LYS CA  HA   sing N N 259 
LYS C   O    doub N N 260 
LYS C   OXT  sing N N 261 
LYS CB  CG   sing N N 262 
LYS CB  HB2  sing N N 263 
LYS CB  HB3  sing N N 264 
LYS CG  CD   sing N N 265 
LYS CG  HG2  sing N N 266 
LYS CG  HG3  sing N N 267 
LYS CD  CE   sing N N 268 
LYS CD  HD2  sing N N 269 
LYS CD  HD3  sing N N 270 
LYS CE  NZ   sing N N 271 
LYS CE  HE2  sing N N 272 
LYS CE  HE3  sing N N 273 
LYS NZ  HZ1  sing N N 274 
LYS NZ  HZ2  sing N N 275 
LYS NZ  HZ3  sing N N 276 
LYS OXT HXT  sing N N 277 
MET N   CA   sing N N 278 
MET N   H    sing N N 279 
MET N   H2   sing N N 280 
MET CA  C    sing N N 281 
MET CA  CB   sing N N 282 
MET CA  HA   sing N N 283 
MET C   O    doub N N 284 
MET C   OXT  sing N N 285 
MET CB  CG   sing N N 286 
MET CB  HB2  sing N N 287 
MET CB  HB3  sing N N 288 
MET CG  SD   sing N N 289 
MET CG  HG2  sing N N 290 
MET CG  HG3  sing N N 291 
MET SD  CE   sing N N 292 
MET CE  HE1  sing N N 293 
MET CE  HE2  sing N N 294 
MET CE  HE3  sing N N 295 
MET OXT HXT  sing N N 296 
PHE N   CA   sing N N 297 
PHE N   H    sing N N 298 
PHE N   H2   sing N N 299 
PHE CA  C    sing N N 300 
PHE CA  CB   sing N N 301 
PHE CA  HA   sing N N 302 
PHE C   O    doub N N 303 
PHE C   OXT  sing N N 304 
PHE CB  CG   sing N N 305 
PHE CB  HB2  sing N N 306 
PHE CB  HB3  sing N N 307 
PHE CG  CD1  doub Y N 308 
PHE CG  CD2  sing Y N 309 
PHE CD1 CE1  sing Y N 310 
PHE CD1 HD1  sing N N 311 
PHE CD2 CE2  doub Y N 312 
PHE CD2 HD2  sing N N 313 
PHE CE1 CZ   doub Y N 314 
PHE CE1 HE1  sing N N 315 
PHE CE2 CZ   sing Y N 316 
PHE CE2 HE2  sing N N 317 
PHE CZ  HZ   sing N N 318 
PHE OXT HXT  sing N N 319 
PRO N   CA   sing N N 320 
PRO N   CD   sing N N 321 
PRO N   H    sing N N 322 
PRO CA  C    sing N N 323 
PRO CA  CB   sing N N 324 
PRO CA  HA   sing N N 325 
PRO C   O    doub N N 326 
PRO C   OXT  sing N N 327 
PRO CB  CG   sing N N 328 
PRO CB  HB2  sing N N 329 
PRO CB  HB3  sing N N 330 
PRO CG  CD   sing N N 331 
PRO CG  HG2  sing N N 332 
PRO CG  HG3  sing N N 333 
PRO CD  HD2  sing N N 334 
PRO CD  HD3  sing N N 335 
PRO OXT HXT  sing N N 336 
SER N   CA   sing N N 337 
SER N   H    sing N N 338 
SER N   H2   sing N N 339 
SER CA  C    sing N N 340 
SER CA  CB   sing N N 341 
SER CA  HA   sing N N 342 
SER C   O    doub N N 343 
SER C   OXT  sing N N 344 
SER CB  OG   sing N N 345 
SER CB  HB2  sing N N 346 
SER CB  HB3  sing N N 347 
SER OG  HG   sing N N 348 
SER OXT HXT  sing N N 349 
THR N   CA   sing N N 350 
THR N   H    sing N N 351 
THR N   H2   sing N N 352 
THR CA  C    sing N N 353 
THR CA  CB   sing N N 354 
THR CA  HA   sing N N 355 
THR C   O    doub N N 356 
THR C   OXT  sing N N 357 
THR CB  OG1  sing N N 358 
THR CB  CG2  sing N N 359 
THR CB  HB   sing N N 360 
THR OG1 HG1  sing N N 361 
THR CG2 HG21 sing N N 362 
THR CG2 HG22 sing N N 363 
THR CG2 HG23 sing N N 364 
THR OXT HXT  sing N N 365 
TRP N   CA   sing N N 366 
TRP N   H    sing N N 367 
TRP N   H2   sing N N 368 
TRP CA  C    sing N N 369 
TRP CA  CB   sing N N 370 
TRP CA  HA   sing N N 371 
TRP C   O    doub N N 372 
TRP C   OXT  sing N N 373 
TRP CB  CG   sing N N 374 
TRP CB  HB2  sing N N 375 
TRP CB  HB3  sing N N 376 
TRP CG  CD1  doub Y N 377 
TRP CG  CD2  sing Y N 378 
TRP CD1 NE1  sing Y N 379 
TRP CD1 HD1  sing N N 380 
TRP CD2 CE2  doub Y N 381 
TRP CD2 CE3  sing Y N 382 
TRP NE1 CE2  sing Y N 383 
TRP NE1 HE1  sing N N 384 
TRP CE2 CZ2  sing Y N 385 
TRP CE3 CZ3  doub Y N 386 
TRP CE3 HE3  sing N N 387 
TRP CZ2 CH2  doub Y N 388 
TRP CZ2 HZ2  sing N N 389 
TRP CZ3 CH2  sing Y N 390 
TRP CZ3 HZ3  sing N N 391 
TRP CH2 HH2  sing N N 392 
TRP OXT HXT  sing N N 393 
TYR N   CA   sing N N 394 
TYR N   H    sing N N 395 
TYR N   H2   sing N N 396 
TYR CA  C    sing N N 397 
TYR CA  CB   sing N N 398 
TYR CA  HA   sing N N 399 
TYR C   O    doub N N 400 
TYR C   OXT  sing N N 401 
TYR CB  CG   sing N N 402 
TYR CB  HB2  sing N N 403 
TYR CB  HB3  sing N N 404 
TYR CG  CD1  doub Y N 405 
TYR CG  CD2  sing Y N 406 
TYR CD1 CE1  sing Y N 407 
TYR CD1 HD1  sing N N 408 
TYR CD2 CE2  doub Y N 409 
TYR CD2 HD2  sing N N 410 
TYR CE1 CZ   doub Y N 411 
TYR CE1 HE1  sing N N 412 
TYR CE2 CZ   sing Y N 413 
TYR CE2 HE2  sing N N 414 
TYR CZ  OH   sing N N 415 
TYR OH  HH   sing N N 416 
TYR OXT HXT  sing N N 417 
VAL N   CA   sing N N 418 
VAL N   H    sing N N 419 
VAL N   H2   sing N N 420 
VAL CA  C    sing N N 421 
VAL CA  CB   sing N N 422 
VAL CA  HA   sing N N 423 
VAL C   O    doub N N 424 
VAL C   OXT  sing N N 425 
VAL CB  CG1  sing N N 426 
VAL CB  CG2  sing N N 427 
VAL CB  HB   sing N N 428 
VAL CG1 HG11 sing N N 429 
VAL CG1 HG12 sing N N 430 
VAL CG1 HG13 sing N N 431 
VAL CG2 HG21 sing N N 432 
VAL CG2 HG22 sing N N 433 
VAL CG2 HG23 sing N N 434 
VAL OXT HXT  sing N N 435 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of Environmental Health Sciences (NIH/NIEHS)' 
_pdbx_audit_support.country                'United States' 
_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   9DQ0 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.crystal_system   monoclinic 
_space_group.IT_number        4 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.id               1 
# 
_atom_sites.entry_id                    9DQ1 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.022552 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000013 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013338 
_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]   0.011455 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C   ? ? 3.54356  2.42580  ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
I   ? ? 40.26819 12.56501 ? ? 1.42647  27.02115 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MN  ? ? 20.23591 4.67902  ? ? 2.76514  44.01191 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N   ? ? 4.01032  2.96436  ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O   ? ? 4.49882  3.47563  ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O1- ? ? 5.12366  3.84317  ? ? 3.49406  27.47979 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S   ? ? 9.55732  6.39887  ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . PRO A 1 2   ? 15.12777  -1.07125  56.10448  1.000 45.80701  ?  2   PRO A N   1 
ATOM   2    C  CA  . PRO A 1 2   ? 14.25997  -1.47306  54.98881  1.000 40.94468  ?  2   PRO A CA  1 
ATOM   3    C  C   . PRO A 1 2   ? 13.78953  -0.26482  54.16495  1.000 23.98011  ?  2   PRO A C   1 
ATOM   4    O  O   . PRO A 1 2   ? 14.16544  0.86290   54.46015  1.000 35.63165  ?  2   PRO A O   1 
ATOM   5    C  CB  . PRO A 1 2   ? 13.09675  -2.18338  55.70179  1.000 41.86706  ?  2   PRO A CB  1 
ATOM   6    C  CG  . PRO A 1 2   ? 13.79485  -2.88408  56.85676  1.000 39.96536  ?  2   PRO A CG  1 
ATOM   7    C  CD  . PRO A 1 2   ? 14.97069  -1.96563  57.26709  1.000 41.23056  ?  2   PRO A CD  1 
ATOM   8    N  N   . LEU A 1 3   ? 13.01235  -0.51900  53.11214  1.000 26.20570  ?  3   LEU A N   1 
ATOM   9    C  CA  . LEU A 1 3   ? 12.55648  0.53748   52.21520  1.000 25.76084  ?  3   LEU A CA  1 
ATOM   10   C  C   . LEU A 1 3   ? 11.51739  1.43434   52.89490  1.000 27.13786  ?  3   LEU A C   1 
ATOM   11   O  O   . LEU A 1 3   ? 10.85953  1.04420   53.86194  1.000 27.23242  ?  3   LEU A O   1 
ATOM   12   C  CB  . LEU A 1 3   ? 11.94183  -0.06148  50.94826  1.000 27.92274  ?  3   LEU A CB  1 
ATOM   13   C  CG  . LEU A 1 3   ? 12.86197  -0.77058  49.95476  1.000 21.37679  ?  3   LEU A CG  1 
ATOM   14   C  CD1 . LEU A 1 3   ? 12.06138  -1.34534  48.81140  1.000 27.64006  ?  3   LEU A CD1 1 
ATOM   15   C  CD2 . LEU A 1 3   ? 13.88894  0.20993   49.45196  1.000 22.26586  ?  3   LEU A CD2 1 
ATOM   16   N  N   . GLY A 1 4   ? 11.35763  2.64281   52.35160  1.000 28.05741  ?  4   GLY A N   1 
ATOM   17   C  CA  . GLY A 1 4   ? 10.34244  3.56640   52.83802  1.000 28.29109  ?  4   GLY A CA  1 
ATOM   18   C  C   . GLY A 1 4   ? 8.93428   3.01744   52.65187  1.000 30.93545  ?  4   GLY A C   1 
ATOM   19   O  O   . GLY A 1 4   ? 8.69381   2.02821   51.95468  1.000 28.54089  ?  4   GLY A O   1 
ATOM   20   N  N   . THR A 1 5   ? 7.97239   3.68234   53.30113  1.000 27.18367  ?  5   THR A N   1 
ATOM   21   C  CA  . THR A 1 5   ? 6.60263   3.16423   53.27461  1.000 29.48436  ?  5   THR A CA  1 
ATOM   22   C  C   . THR A 1 5   ? 5.99941   3.22514   51.87727  1.000 25.23810  ?  5   THR A C   1 
ATOM   23   O  O   . THR A 1 5   ? 5.03199   2.51453   51.59381  1.000 22.57755  ?  5   THR A O   1 
ATOM   24   C  CB  . THR A 1 5   ? 5.70669   3.93087   54.25763  1.000 40.03422  ?  5   THR A CB  1 
ATOM   25   O  OG1 . THR A 1 5   ? 6.39065   4.09183   55.50713  1.000 45.76747  ?  5   THR A OG1 1 
ATOM   26   C  CG2 . THR A 1 5   ? 4.40576   3.15990   54.50735  1.000 35.28824  ?  5   THR A CG2 1 
ATOM   27   N  N   . GLU A 1 6   ? 6.56320   4.03831   50.99426  1.000 20.36151  ?  6   GLU A N   1 
ATOM   28   C  CA  . GLU A 1 6   ? 6.08758   4.15595   49.62734  1.000 25.25504  ?  6   GLU A CA  1 
ATOM   29   C  C   . GLU A 1 6   ? 6.79630   3.21959   48.66266  1.000 21.69083  ?  6   GLU A C   1 
ATOM   30   O  O   . GLU A 1 6   ? 6.52812   3.28017   47.45577  1.000 17.57563  ?  6   GLU A O   1 
ATOM   31   C  CB  . GLU A 1 6   ? 6.24079   5.59187   49.14917  1.000 27.95739  ?  6   GLU A CB  1 
ATOM   32   C  CG  . GLU A 1 6   ? 5.37796   6.54295   49.93477  1.000 33.57446  ?  6   GLU A CG  1 
ATOM   33   C  CD  . GLU A 1 6   ? 5.08947   7.78503   49.15302  1.000 48.45521  ?  6   GLU A CD  1 
ATOM   34   O  OE1 . GLU A 1 6   ? 6.04177   8.56754   48.98342  1.000 43.53771  ?  6   GLU A OE1 1 
ATOM   35   O  OE2 . GLU A 1 6   ? 3.94094   7.97390   48.68741  1.000 66.35329  -1 6   GLU A OE2 1 
ATOM   36   N  N   . GLY A 1 7   ? 7.67650   2.35398   49.15360  1.000 16.00752  ?  7   GLY A N   1 
ATOM   37   C  CA  . GLY A 1 7   ? 8.27881   1.34514   48.30317  1.000 20.63797  ?  7   GLY A CA  1 
ATOM   38   C  C   . GLY A 1 7   ? 9.55158   1.76913   47.61042  1.000 10.00074  ?  7   GLY A C   1 
ATOM   39   O  O   . GLY A 1 7   ? 9.96065   1.12040   46.64226  1.000 13.87869  ?  7   GLY A O   1 
ATOM   40   N  N   . PHE A 1 8   ? 10.19452  2.83033   48.07412  1.000 9.54025   ?  8   PHE A N   1 
ATOM   41   C  CA  . PHE A 1 8   ? 11.44983  3.24848   47.48968  1.000 10.55065  ?  8   PHE A CA  1 
ATOM   42   C  C   . PHE A 1 8   ? 12.23425  4.03688   48.52525  1.000 13.83300  ?  8   PHE A C   1 
ATOM   43   O  O   . PHE A 1 8   ? 11.67095  4.58129   49.48138  1.000 11.50487  ?  8   PHE A O   1 
ATOM   44   C  CB  . PHE A 1 8   ? 11.22247  4.09796   46.23573  1.000 9.17184   ?  8   PHE A CB  1 
ATOM   45   C  CG  . PHE A 1 8   ? 10.83304  5.51304   46.53816  1.000 10.79380  ?  8   PHE A CG  1 
ATOM   46   C  CD1 . PHE A 1 8   ? 9.52009   5.83444   46.85376  1.000 10.24453  ?  8   PHE A CD1 1 
ATOM   47   C  CD2 . PHE A 1 8   ? 11.77504  6.52756   46.49454  1.000 11.26630  ?  8   PHE A CD2 1 
ATOM   48   C  CE1 . PHE A 1 8   ? 9.16240   7.14160   47.12379  1.000 12.30336  ?  8   PHE A CE1 1 
ATOM   49   C  CE2 . PHE A 1 8   ? 11.42584  7.83153   46.76511  1.000 13.99321  ?  8   PHE A CE2 1 
ATOM   50   C  CZ  . PHE A 1 8   ? 10.11456  8.14181   47.08176  1.000 17.86208  ?  8   PHE A CZ  1 
ATOM   51   N  N   . THR A 1 9   ? 13.54106  4.11286   48.30309  1.000 9.37388   ?  9   THR A N   1 
ATOM   52   C  CA  . THR A 1 9   ? 14.41891  4.96320   49.09720  1.000 14.02516  ?  9   THR A CA  1 
ATOM   53   C  C   . THR A 1 9   ? 15.52942  5.47624   48.19830  1.000 11.70180  ?  9   THR A C   1 
ATOM   54   O  O   . THR A 1 9   ? 16.00691  4.74390   47.33250  1.000 12.19631  ?  9   THR A O   1 
ATOM   55   C  CB  . THR A 1 9   ? 15.05318  4.22205   50.28253  1.000 15.24049  ?  9   THR A CB  1 
ATOM   56   O  OG1 . THR A 1 9   ? 14.04003  3.51619   51.01200  1.000 21.18885  ?  9   THR A OG1 1 
ATOM   57   C  CG2 . THR A 1 9   ? 15.71361  5.22500   51.20426  1.000 15.44075  ?  9   THR A CG2 1 
ATOM   58   N  N   . VAL A 1 10  ? 15.94065  6.72709   48.40039  1.000 8.57602   ?  10  VAL A N   1 
ATOM   59   C  CA  . VAL A 1 10  ? 17.08649  7.28887   47.69802  1.000 7.99243   ?  10  VAL A CA  1 
ATOM   60   C  C   . VAL A 1 10  ? 18.23499  7.35366   48.69292  1.000 15.81381  ?  10  VAL A C   1 
ATOM   61   O  O   . VAL A 1 10  ? 18.04934  7.82087   49.82029  1.000 10.29515  ?  10  VAL A O   1 
ATOM   62   C  CB  . VAL A 1 10  ? 16.75590  8.67420   47.11174  1.000 10.83700  ?  10  VAL A CB  1 
ATOM   63   C  CG1 . VAL A 1 10  ? 17.98556  9.29768   46.47323  1.000 8.77585   ?  10  VAL A CG1 1 
ATOM   64   C  CG2 . VAL A 1 10  ? 15.60559  8.56287   46.09129  1.000 15.04051  ?  10  VAL A CG2 1 
ATOM   65   N  N   . ILE A 1 11  ? 19.41519  6.87488   48.29310  1.000 10.02123  ?  11  ILE A N   1 
ATOM   66   C  CA  . ILE A 1 11  ? 20.56016  6.85879   49.19554  1.000 10.02023  ?  11  ILE A CA  1 
ATOM   67   C  C   . ILE A 1 11  ? 21.76540  7.52230   48.53854  1.000 17.17451  ?  11  ILE A C   1 
ATOM   68   O  O   . ILE A 1 11  ? 21.87133  7.60574   47.31443  1.000 11.62522  ?  11  ILE A O   1 
ATOM   69   C  CB  . ILE A 1 11  ? 20.94130  5.43133   49.64859  1.000 10.76167  ?  11  ILE A CB  1 
ATOM   70   C  CG1 . ILE A 1 11  ? 21.39355  4.59499   48.44473  1.000 11.85767  ?  11  ILE A CG1 1 
ATOM   71   C  CG2 . ILE A 1 11  ? 19.79354  4.78389   50.41784  1.000 18.44817  ?  11  ILE A CG2 1 
ATOM   72   C  CD1 . ILE A 1 11  ? 22.05736  3.26778   48.81275  1.000 12.18354  ?  11  ILE A CD1 1 
ATOM   73   N  N   . ASP A 1 12  ? 22.67978  8.00086   49.38459  1.000 12.73925  ?  12  ASP A N   1 
ATOM   74   C  CA  . ASP A 1 12  ? 23.99517  8.46032   48.94662  1.000 15.37256  ?  12  ASP A CA  1 
ATOM   75   C  C   . ASP A 1 12  ? 24.98434  7.30364   48.98054  1.000 19.50462  ?  12  ASP A C   1 
ATOM   76   O  O   . ASP A 1 12  ? 24.97277  6.49284   49.90649  1.000 23.24092  ?  12  ASP A O   1 
ATOM   77   C  CB  . ASP A 1 12  ? 24.52284  9.58335   49.84243  1.000 23.16738  ?  12  ASP A CB  1 
ATOM   78   C  CG  . ASP A 1 12  ? 23.68242  10.82596  49.78230  1.000 20.83977  ?  12  ASP A CG  1 
ATOM   79   O  OD1 . ASP A 1 12  ? 23.21101  11.19196  48.68246  1.000 26.82403  ?  12  ASP A OD1 1 
ATOM   80   O  OD2 . ASP A 1 12  ? 23.49308  11.44769  50.84226  1.000 37.52301  -1 12  ASP A OD2 1 
ATOM   81   N  N   . LEU A 1 13  ? 25.84283  7.24175   47.98821  1.000 14.39760  ?  13  LEU A N   1 
ATOM   82   C  CA  . LEU A 1 13  ? 26.81274  6.15594   47.92226  1.000 17.12579  ?  13  LEU A CA  1 
ATOM   83   C  C   . LEU A 1 13  ? 28.16701  6.63082   48.42730  1.000 13.08407  ?  13  LEU A C   1 
ATOM   84   O  O   . LEU A 1 13  ? 28.49157  7.81332   48.31696  1.000 15.76934  ?  13  LEU A O   1 
ATOM   85   C  CB  . LEU A 1 13  ? 26.97193  5.66586   46.48511  1.000 19.08679  ?  13  LEU A CB  1 
ATOM   86   C  CG  . LEU A 1 13  ? 25.64243  5.18213   45.92889  1.000 25.27529  ?  13  LEU A CG  1 
ATOM   87   C  CD1 . LEU A 1 13  ? 25.79630  4.96998   44.44689  1.000 16.78246  ?  13  LEU A CD1 1 
ATOM   88   C  CD2 . LEU A 1 13  ? 25.24063  3.90904   46.66190  1.000 19.68083  ?  13  LEU A CD2 1 
ATOM   89   N  N   . PRO A 1 14  ? 28.98706  5.74564   48.97183  1.000 19.50846  ?  14  PRO A N   1 
ATOM   90   C  CA  . PRO A 1 14  ? 30.34652  6.14481   49.34770  1.000 23.57785  ?  14  PRO A CA  1 
ATOM   91   C  C   . PRO A 1 14  ? 31.20507  6.30897   48.10874  1.000 22.50946  ?  14  PRO A C   1 
ATOM   92   O  O   . PRO A 1 14  ? 30.79247  6.00259   46.99014  1.000 16.30822  ?  14  PRO A O   1 
ATOM   93   C  CB  . PRO A 1 14  ? 30.82900  4.98534   50.21769  1.000 30.66434  ?  14  PRO A CB  1 
ATOM   94   C  CG  . PRO A 1 14  ? 30.07745  3.80692   49.68551  1.000 28.51843  ?  14  PRO A CG  1 
ATOM   95   C  CD  . PRO A 1 14  ? 28.71913  4.33486   49.28521  1.000 16.70628  ?  14  PRO A CD  1 
ATOM   96   N  N   . GLU A 1 15  ? 32.41567  6.81260   48.32581  1.000 18.22412  ?  15  GLU A N   1 
ATOM   97   C  CA  . GLU A 1 15  ? 33.38220  6.93029   47.24529  1.000 21.90358  ?  15  GLU A CA  1 
ATOM   98   C  C   . GLU A 1 15  ? 33.60379  5.57433   46.59566  1.000 14.65988  ?  15  GLU A C   1 
ATOM   99   O  O   . GLU A 1 15  ? 33.59738  4.53492   47.25994  1.000 16.15304  ?  15  GLU A O   1 
ATOM   100  C  CB  . GLU A 1 15  ? 34.71682  7.48462   47.77402  1.000 27.81111  ?  15  GLU A CB  1 
ATOM   101  C  CG  . GLU A 1 15  ? 35.00961  8.94273   47.35910  1.000 42.06965  ?  15  GLU A CG  1 
ATOM   102  C  CD  . GLU A 1 15  ? 36.36081  9.46063   47.85716  1.000 60.35251  ?  15  GLU A CD  1 
ATOM   103  O  OE1 . GLU A 1 15  ? 37.38013  8.74504   47.71596  1.000 58.29073  ?  15  GLU A OE1 1 
ATOM   104  O  OE2 . GLU A 1 15  ? 36.39875  10.59154  48.39359  1.000 72.57013  -1 15  GLU A OE2 1 
ATOM   105  N  N   . VAL A 1 16  ? 33.76374  5.58189   45.28801  1.000 12.66842  ?  16  VAL A N   1 
ATOM   106  C  CA  . VAL A 1 16  ? 33.98910  4.35630   44.55346  1.000 23.42605  ?  16  VAL A CA  1 
ATOM   107  C  C   . VAL A 1 16  ? 35.46566  4.25223   44.18825  1.000 16.08208  ?  16  VAL A C   1 
ATOM   108  O  O   . VAL A 1 16  ? 36.19263  5.25257   44.11677  1.000 17.94760  ?  16  VAL A O   1 
ATOM   109  C  CB  . VAL A 1 16  ? 33.08186  4.26659   43.29957  1.000 24.43784  ?  16  VAL A CB  1 
ATOM   110  C  CG1 . VAL A 1 16  ? 31.60525  4.43030   43.70141  1.000 28.50606  ?  16  VAL A CG1 1 
ATOM   111  C  CG2 . VAL A 1 16  ? 33.47633  5.29533   42.27975  1.000 18.45484  ?  16  VAL A CG2 1 
ATOM   112  N  N   . ALA A 1 17  ? 35.91069  3.00568   43.96327  1.000 20.00361  ?  17  ALA A N   1 
ATOM   113  C  CA  . ALA A 1 17  ? 37.29317  2.71221   43.62679  1.000 12.16193  ?  17  ALA A CA  1 
ATOM   114  C  C   . ALA A 1 17  ? 37.70481  3.47665   42.36764  1.000 17.70553  ?  17  ALA A C   1 
ATOM   115  O  O   . ALA A 1 17  ? 36.86564  3.78739   41.51481  1.000 15.82574  ?  17  ALA A O   1 
ATOM   116  C  CB  . ALA A 1 17  ? 37.46822  1.20580   43.41716  1.000 17.28357  ?  17  ALA A CB  1 
ATOM   117  N  N   . PRO A 1 18  ? 38.99669  3.79510   42.22476  1.000 19.23739  ?  18  PRO A N   1 
ATOM   118  C  CA  . PRO A 1 18  ? 39.40940  4.67835   41.11917  1.000 21.32789  ?  18  PRO A CA  1 
ATOM   119  C  C   . PRO A 1 18  ? 39.22181  4.08238   39.73471  1.000 12.91196  ?  18  PRO A C   1 
ATOM   120  O  O   . PRO A 1 18  ? 39.31581  4.83628   38.75635  1.000 11.65667  ?  18  PRO A O   1 
ATOM   121  C  CB  . PRO A 1 18  ? 40.89679  4.95068   41.40199  1.000 24.36532  ?  18  PRO A CB  1 
ATOM   122  C  CG  . PRO A 1 18  ? 41.30850  4.00211   42.44800  1.000 23.52381  ?  18  PRO A CG  1 
ATOM   123  C  CD  . PRO A 1 18  ? 40.08333  3.56421   43.19514  1.000 24.08659  ?  18  PRO A CD  1 
ATOM   124  N  N   . ASP A 1 19  ? 38.97923  2.77618   39.60829  1.000 9.54556   ?  19  ASP A N   1 
ATOM   125  C  CA  . ASP A 1 19  ? 38.82085  2.18472   38.28721  1.000 10.25365  ?  19  ASP A CA  1 
ATOM   126  C  C   . ASP A 1 19  ? 37.38130  2.21063   37.78198  1.000 12.51388  ?  19  ASP A C   1 
ATOM   127  O  O   . ASP A 1 19  ? 37.15389  1.92345   36.60116  1.000 11.74757  ?  19  ASP A O   1 
ATOM   128  C  CB  . ASP A 1 19  ? 39.34350  0.73892   38.27020  1.000 13.29827  ?  19  ASP A CB  1 
ATOM   129  C  CG  . ASP A 1 19  ? 38.57661  -0.18648  39.20891  1.000 22.09982  ?  19  ASP A CG  1 
ATOM   130  O  OD1 . ASP A 1 19  ? 37.99697  0.30151   40.19760  1.000 20.73196  ?  19  ASP A OD1 1 
ATOM   131  O  OD2 . ASP A 1 19  ? 38.57917  -1.41258  38.97516  1.000 21.57647  -1 19  ASP A OD2 1 
ATOM   132  N  N   . ILE A 1 20  ? 36.42242  2.58489   38.62594  1.000 8.66111   ?  20  ILE A N   1 
ATOM   133  C  CA  . ILE A 1 20  ? 35.00461  2.45666   38.26479  1.000 7.65848   ?  20  ILE A CA  1 
ATOM   134  C  C   . ILE A 1 20  ? 34.62468  3.43931   37.16042  1.000 6.90177   ?  20  ILE A C   1 
ATOM   135  O  O   . ILE A 1 20  ? 34.12098  3.04413   36.10077  1.000 11.59280  ?  20  ILE A O   1 
ATOM   136  C  CB  . ILE A 1 20  ? 34.11675  2.65687   39.50032  1.000 12.95888  ?  20  ILE A CB  1 
ATOM   137  C  CG1 . ILE A 1 20  ? 34.47557  1.62285   40.55808  1.000 15.67862  ?  20  ILE A CG1 1 
ATOM   138  C  CG2 . ILE A 1 20  ? 32.64285  2.51061   39.11717  1.000 12.61825  ?  20  ILE A CG2 1 
ATOM   139  C  CD1 . ILE A 1 20  ? 34.09048  0.23114   40.14195  1.000 12.45984  ?  20  ILE A CD1 1 
ATOM   140  N  N   . LEU A 1 21  ? 34.82241  4.73334   37.40206  1.000 5.45307   ?  21  LEU A N   1 
ATOM   141  C  CA  . LEU A 1 21  ? 34.38937  5.71700   36.41557  1.000 5.75345   ?  21  LEU A CA  1 
ATOM   142  C  C   . LEU A 1 21  ? 35.09496  5.56839   35.08077  1.000 12.27156  ?  21  LEU A C   1 
ATOM   143  O  O   . LEU A 1 21  ? 34.41393  5.66616   34.04222  1.000 9.91911   ?  21  LEU A O   1 
ATOM   144  C  CB  . LEU A 1 21  ? 34.57062  7.14108   36.95645  1.000 8.92760   ?  21  LEU A CB  1 
ATOM   145  C  CG  . LEU A 1 21  ? 33.32915  7.78822   37.56867  1.000 16.09234  ?  21  LEU A CG  1 
ATOM   146  C  CD1 . LEU A 1 21  ? 32.77566  6.93366   38.67177  1.000 19.01998  ?  21  LEU A CD1 1 
ATOM   147  C  CD2 . LEU A 1 21  ? 33.65463  9.19692   38.07321  1.000 17.59930  ?  21  LEU A CD2 1 
ATOM   148  N  N   . PRO A 1 22  ? 36.41497  5.35752   35.01796  1.000 9.78656   ?  22  PRO A N   1 
ATOM   149  C  CA  . PRO A 1 22  ? 37.05925  5.18906   33.71160  1.000 11.82661  ?  22  PRO A CA  1 
ATOM   150  C  C   . PRO A 1 22  ? 36.56419  3.98350   32.94467  1.000 13.30300  ?  22  PRO A C   1 
ATOM   151  O  O   . PRO A 1 22  ? 36.65392  3.97818   31.70590  1.000 9.12603   ?  22  PRO A O   1 
ATOM   152  C  CB  . PRO A 1 22  ? 38.54692  5.04923   34.07327  1.000 12.83239  ?  22  PRO A CB  1 
ATOM   153  C  CG  . PRO A 1 22  ? 38.67868  5.73686   35.35445  1.000 12.61849  ?  22  PRO A CG  1 
ATOM   154  C  CD  . PRO A 1 22  ? 37.41455  5.42904   36.10099  1.000 12.19936  ?  22  PRO A CD  1 
ATOM   155  N  N   . SER A 1 23  ? 36.04329  2.96421   33.63166  1.000 9.39730   ?  23  SER A N   1 
ATOM   156  C  CA  . SER A 1 23  ? 35.64645  1.74631   32.93650  1.000 8.58731   ?  23  SER A CA  1 
ATOM   157  C  C   . SER A 1 23  ? 34.48051  1.97145   31.98422  1.000 8.86542   ?  23  SER A C   1 
ATOM   158  O  O   . SER A 1 23  ? 34.31052  1.17114   31.05373  1.000 8.90109   ?  23  SER A O   1 
ATOM   159  C  CB  . SER A 1 23  ? 35.27325  0.64830   33.93071  1.000 10.18085  ?  23  SER A CB  1 
ATOM   160  O  OG  . SER A 1 23  ? 34.05314  0.95164   34.61498  1.000 10.12803  ?  23  SER A OG  1 
ATOM   161  N  N   . TYR A 1 24  ? 33.69609  3.04381   32.18187  1.000 8.76046   ?  24  TYR A N   1 
ATOM   162  C  CA  . TYR A 1 24  ? 32.57749  3.33087   31.28242  1.000 11.24132  ?  24  TYR A CA  1 
ATOM   163  C  C   . TYR A 1 24  ? 33.06421  3.69941   29.88699  1.000 13.37844  ?  24  TYR A C   1 
ATOM   164  O  O   . TYR A 1 24  ? 32.33930  3.50263   28.90083  1.000 10.18997  ?  24  TYR A O   1 
ATOM   165  C  CB  . TYR A 1 24  ? 31.70656  4.44524   31.86922  1.000 11.43679  ?  24  TYR A CB  1 
ATOM   166  C  CG  . TYR A 1 24  ? 30.82089  3.94082   32.98272  1.000 8.91890   ?  24  TYR A CG  1 
ATOM   167  C  CD1 . TYR A 1 24  ? 31.27461  3.91227   34.30681  1.000 5.72806   ?  24  TYR A CD1 1 
ATOM   168  C  CD2 . TYR A 1 24  ? 29.53695  3.45962   32.71452  1.000 6.78025   ?  24  TYR A CD2 1 
ATOM   169  C  CE1 . TYR A 1 24  ? 30.47212  3.43245   35.31552  1.000 11.07873  ?  24  TYR A CE1 1 
ATOM   170  C  CE2 . TYR A 1 24  ? 28.73051  2.98212   33.72889  1.000 6.55314   ?  24  TYR A CE2 1 
ATOM   171  C  CZ  . TYR A 1 24  ? 29.20940  2.95884   35.02283  1.000 9.36224   ?  24  TYR A CZ  1 
ATOM   172  O  OH  . TYR A 1 24  ? 28.42768  2.48882   36.04970  1.000 9.22269   ?  24  TYR A OH  1 
ATOM   173  N  N   . ASP A 1 25  ? 34.28885  4.21584   29.77725  1.000 9.57808   ?  25  ASP A N   1 
ATOM   174  C  CA  . ASP A 1 25  ? 34.86883  4.50392   28.46973  1.000 9.91833   ?  25  ASP A CA  1 
ATOM   175  C  C   . ASP A 1 25  ? 35.13582  3.24605   27.65628  1.000 13.67694  ?  25  ASP A C   1 
ATOM   176  O  O   . ASP A 1 25  ? 35.38011  3.34915   26.45176  1.000 15.43826  ?  25  ASP A O   1 
ATOM   177  C  CB  . ASP A 1 25  ? 36.17515  5.28200   28.64275  1.000 16.76767  ?  25  ASP A CB  1 
ATOM   178  C  CG  . ASP A 1 25  ? 35.94488  6.68933   29.12831  1.000 25.74638  ?  25  ASP A CG  1 
ATOM   179  O  OD1 . ASP A 1 25  ? 34.92001  7.28782   28.72931  1.000 21.86974  ?  25  ASP A OD1 1 
ATOM   180  O  OD2 . ASP A 1 25  ? 36.78025  7.19349   29.90767  1.000 21.89391  -1 25  ASP A OD2 1 
ATOM   181  N  N   . ARG A 1 26  ? 35.11190  2.06967   28.27864  1.000 11.30721  ?  26  ARG A N   1 
ATOM   182  C  CA  . ARG A 1 26  ? 35.46680  0.82528   27.61046  1.000 11.27249  ?  26  ARG A CA  1 
ATOM   183  C  C   . ARG A 1 26  ? 34.27851  -0.11885  27.49341  1.000 17.78504  ?  26  ARG A C   1 
ATOM   184  O  O   . ARG A 1 26  ? 34.46839  -1.33005  27.32598  1.000 14.41869  ?  26  ARG A O   1 
ATOM   185  C  CB  . ARG A 1 26  ? 36.61727  0.12821   28.34303  1.000 11.08898  ?  26  ARG A CB  1 
ATOM   186  C  CG  . ARG A 1 26  ? 37.82293  1.02670   28.60496  1.000 22.27736  ?  26  ARG A CG  1 
ATOM   187  C  CD  . ARG A 1 26  ? 39.03630  0.25125   29.14669  1.000 13.62140  ?  26  ARG A CD  1 
ATOM   188  N  NE  . ARG A 1 26  ? 38.78408  -0.45745  30.39951  1.000 16.76425  ?  26  ARG A NE  1 
ATOM   189  C  CZ  . ARG A 1 26  ? 38.88803  0.07768   31.61235  1.000 21.32478  ?  26  ARG A CZ  1 
ATOM   190  N  NH1 . ARG A 1 26  ? 39.22315  1.34844   31.78458  1.000 20.68453  ?  26  ARG A NH1 1 
ATOM   191  N  NH2 . ARG A 1 26  ? 38.62795  -0.67592  32.67794  1.000 21.78112  ?  26  ARG A NH2 1 
ATOM   192  N  N   . CYS A 1 27  ? 33.06131  0.40752   27.61265  1.000 11.31696  ?  27  CYS A N   1 
ATOM   193  C  CA  . CYS A 1 27  ? 31.86581  -0.39219  27.37170  1.000 7.44398   ?  27  CYS A CA  1 
ATOM   194  C  C   . CYS A 1 27  ? 31.49796  -0.30134  25.89885  1.000 9.62049   ?  27  CYS A C   1 
ATOM   195  O  O   . CYS A 1 27  ? 31.33943  0.80969   25.37846  1.000 11.46399  ?  27  CYS A O   1 
ATOM   196  C  CB  . CYS A 1 27  ? 30.70709  0.10040   28.23419  1.000 8.82922   ?  27  CYS A CB  1 
ATOM   197  S  SG  . CYS A 1 27  ? 30.95870  -0.21662  30.01484  1.000 11.44343  ?  27  CYS A SG  1 
ATOM   198  N  N   . PRO A 1 28  ? 31.34395  -1.43261  25.21917  1.000 10.21596  ?  28  PRO A N   1 
ATOM   199  C  CA  . PRO A 1 28  ? 30.98692  -1.41908  23.79902  1.000 11.60253  ?  28  PRO A CA  1 
ATOM   200  C  C   . PRO A 1 28  ? 29.51957  -1.08156  23.60924  1.000 8.24999   ?  28  PRO A C   1 
ATOM   201  O  O   . PRO A 1 28  ? 28.71576  -1.14533  24.53495  1.000 8.40569   ?  28  PRO A O   1 
ATOM   202  C  CB  . PRO A 1 28  ? 31.27399  -2.85604  23.34766  1.000 15.08419  ?  28  PRO A CB  1 
ATOM   203  C  CG  . PRO A 1 28  ? 31.11187  -3.67382  24.56804  1.000 13.21428  ?  28  PRO A CG  1 
ATOM   204  C  CD  . PRO A 1 28  ? 31.50061  -2.79955  25.74580  1.000 16.21303  ?  28  PRO A CD  1 
ATOM   205  N  N   . VAL A 1 29  ? 29.16907  -0.75474  22.36629  1.000 10.04146  ?  29  VAL A N   1 
ATOM   206  C  CA  . VAL A 1 29  ? 27.79199  -0.36176  22.08752  1.000 11.43641  ?  29  VAL A CA  1 
ATOM   207  C  C   . VAL A 1 29  ? 26.84781  -1.50928  22.43661  1.000 9.93028   ?  29  VAL A C   1 
ATOM   208  O  O   . VAL A 1 29  ? 27.18522  -2.69051  22.28713  1.000 8.96810   ?  29  VAL A O   1 
ATOM   209  C  CB  . VAL A 1 29  ? 27.65077  0.09028   20.61999  1.000 15.63890  ?  29  VAL A CB  1 
ATOM   210  C  CG1 . VAL A 1 29  ? 27.87384  -1.06995  19.66063  1.000 18.16619  ?  29  VAL A CG1 1 
ATOM   211  C  CG2 . VAL A 1 29  ? 26.28168  0.76331   20.37481  1.000 16.56423  ?  29  VAL A CG2 1 
ATOM   212  N  N   . ASP A 1 30  ? 25.68142  -1.15796  22.97941  1.000 9.11948   ?  30  ASP A N   1 
ATOM   213  C  CA  . ASP A 1 30  ? 24.57171  -2.08723  23.18319  1.000 10.29262  ?  30  ASP A CA  1 
ATOM   214  C  C   . ASP A 1 30  ? 23.92849  -2.35191  21.82562  1.000 10.86419  ?  30  ASP A C   1 
ATOM   215  O  O   . ASP A 1 30  ? 23.28915  -1.46273  21.26353  1.000 6.58258   ?  30  ASP A O   1 
ATOM   216  C  CB  . ASP A 1 30  ? 23.56803  -1.46916  24.16002  1.000 10.45099  ?  30  ASP A CB  1 
ATOM   217  C  CG  . ASP A 1 30  ? 22.49351  -2.46429  24.64990  1.000 13.55182  ?  30  ASP A CG  1 
ATOM   218  O  OD1 . ASP A 1 30  ? 22.18292  -3.45727  23.95442  1.000 5.24565   ?  30  ASP A OD1 1 
ATOM   219  O  OD2 . ASP A 1 30  ? 21.95133  -2.23307  25.75239  1.000 9.74185   -1 30  ASP A OD2 1 
ATOM   220  N  N   . ASP A 1 31  ? 24.09021  -3.56931  21.29611  1.000 11.64181  ?  31  ASP A N   1 
ATOM   221  C  CA  . ASP A 1 31  ? 23.55827  -3.88384  19.97066  1.000 13.47444  ?  31  ASP A CA  1 
ATOM   222  C  C   . ASP A 1 31  ? 22.03765  -3.96502  19.93123  1.000 14.58783  ?  31  ASP A C   1 
ATOM   223  O  O   . ASP A 1 31  ? 21.46305  -4.02406  18.83244  1.000 11.42494  ?  31  ASP A O   1 
ATOM   224  C  CB  . ASP A 1 31  ? 24.13136  -5.21433  19.48143  1.000 14.73936  ?  31  ASP A CB  1 
ATOM   225  C  CG  . ASP A 1 31  ? 25.58884  -5.10706  19.08528  1.000 25.43435  ?  31  ASP A CG  1 
ATOM   226  O  OD1 . ASP A 1 31  ? 25.98078  -4.04187  18.56786  1.000 25.15339  ?  31  ASP A OD1 1 
ATOM   227  O  OD2 . ASP A 1 31  ? 26.34649  -6.07699  19.29866  1.000 37.78450  -1 31  ASP A OD2 1 
ATOM   228  N  N   . TYR A 1 32  ? 21.37650  -4.00133  21.08725  1.000 7.61736   ?  32  TYR A N   1 
ATOM   229  C  CA  . TYR A 1 32  ? 19.96574  -4.36638  21.15122  1.000 8.64962   ?  32  TYR A CA  1 
ATOM   230  C  C   . TYR A 1 32  ? 19.05099  -3.24719  21.60402  1.000 9.27111   ?  32  TYR A C   1 
ATOM   231  O  O   . TYR A 1 32  ? 17.83547  -3.33030  21.36981  1.000 8.57025   ?  32  TYR A O   1 
ATOM   232  C  CB  . TYR A 1 32  ? 19.77486  -5.55077  22.10560  1.000 6.34170   ?  32  TYR A CB  1 
ATOM   233  C  CG  . TYR A 1 32  ? 20.66992  -6.72122  21.78008  1.000 10.93858  ?  32  TYR A CG  1 
ATOM   234  C  CD1 . TYR A 1 32  ? 20.27515  -7.68832  20.86406  1.000 9.37798   ?  32  TYR A CD1 1 
ATOM   235  C  CD2 . TYR A 1 32  ? 21.91671  -6.85628  22.38246  1.000 7.93595   ?  32  TYR A CD2 1 
ATOM   236  C  CE1 . TYR A 1 32  ? 21.09647  -8.77697  20.56404  1.000 13.03361  ?  32  TYR A CE1 1 
ATOM   237  C  CE2 . TYR A 1 32  ? 22.74830  -7.93396  22.07855  1.000 8.21723   ?  32  TYR A CE2 1 
ATOM   238  C  CZ  . TYR A 1 32  ? 22.33710  -8.88377  21.17350  1.000 13.64828  ?  32  TYR A CZ  1 
ATOM   239  O  OH  . TYR A 1 32  ? 23.17164  -9.94922  20.90534  1.000 8.99495   ?  32  TYR A OH  1 
ATOM   240  N  N   . MET A 1 33  ? 19.57941  -2.23262  22.28285  1.000 6.06952   ?  33  MET A N   1 
ATOM   241  C  CA  . MET A 1 33  ? 18.72798  -1.18719  22.83104  1.000 8.62313   ?  33  MET A CA  1 
ATOM   242  C  C   . MET A 1 33  ? 19.41258  0.15722   22.70920  1.000 6.34570   ?  33  MET A C   1 
ATOM   243  O  O   . MET A 1 33  ? 20.64276  0.25339   22.76104  1.000 7.86294   ?  33  MET A O   1 
ATOM   244  C  CB  . MET A 1 33  ? 18.36768  -1.45781  24.28361  1.000 8.82955   ?  33  MET A CB  1 
ATOM   245  C  CG  . MET A 1 33  ? 17.35085  -2.58835  24.41582  1.000 16.17684  ?  33  MET A CG  1 
ATOM   246  S  SD  . MET A 1 33  ? 16.73226  -2.75284  26.07185  1.000 27.35131  ?  33  MET A SD  1 
ATOM   247  C  CE  . MET A 1 33  ? 15.63261  -1.35030  26.22573  1.000 13.33120  ?  33  MET A CE  1 
ATOM   248  N  N   . GLY A 1 34  ? 18.59529  1.19750   22.52068  1.000 8.76163   ?  34  GLY A N   1 
ATOM   249  C  CA  . GLY A 1 34  ? 19.09300  2.55640   22.50348  1.000 7.21591   ?  34  GLY A CA  1 
ATOM   250  C  C   . GLY A 1 34  ? 19.48111  3.08498   21.14195  1.000 10.40720  ?  34  GLY A C   1 
ATOM   251  O  O   . GLY A 1 34  ? 19.87781  4.25551   21.04747  1.000 10.52690  ?  34  GLY A O   1 
ATOM   252  N  N   . ASN A 1 35  ? 19.38970  2.26284   20.09884  1.000 4.60179   ?  35  ASN A N   1 
ATOM   253  C  CA  . ASN A 1 35  ? 19.69762  2.64560   18.72267  1.000 8.31541   ?  35  ASN A CA  1 
ATOM   254  C  C   . ASN A 1 35  ? 20.99390  3.44088   18.63622  1.000 7.21546   ?  35  ASN A C   1 
ATOM   255  O  O   . ASN A 1 35  ? 21.04934  4.55997   18.12041  1.000 8.48771   ?  35  ASN A O   1 
ATOM   256  C  CB  . ASN A 1 35  ? 18.52342  3.38735   18.09017  1.000 7.93181   ?  35  ASN A CB  1 
ATOM   257  C  CG  . ASN A 1 35  ? 17.37031  2.45639   17.81585  1.000 8.11625   ?  35  ASN A CG  1 
ATOM   258  O  OD1 . ASN A 1 35  ? 17.37478  1.74433   16.81062  1.000 9.54873   ?  35  ASN A OD1 1 
ATOM   259  N  ND2 . ASN A 1 35  ? 16.38837  2.43125   18.71567  1.000 6.19029   ?  35  ASN A ND2 1 
ATOM   260  N  N   . GLY A 1 36  ? 22.05377  2.82118   19.13991  1.000 10.77702  ?  36  GLY A N   1 
ATOM   261  C  CA  . GLY A 1 36  ? 23.38112  3.38622   19.08287  1.000 8.71761   ?  36  GLY A CA  1 
ATOM   262  C  C   . GLY A 1 36  ? 23.71520  4.40057   20.16177  1.000 10.96758  ?  36  GLY A C   1 
ATOM   263  O  O   . GLY A 1 36  ? 24.86978  4.85044   20.21975  1.000 11.08417  ?  36  GLY A O   1 
ATOM   264  N  N   . THR A 1 37  ? 22.75339  4.79631   21.00391  1.000 5.69186   ?  37  THR A N   1 
ATOM   265  C  CA  . THR A 1 37  ? 23.03374  5.74592   22.08139  1.000 9.70845   ?  37  THR A CA  1 
ATOM   266  C  C   . THR A 1 37  ? 23.49043  5.07679   23.37871  1.000 7.33244   ?  37  THR A C   1 
ATOM   267  O  O   . THR A 1 37  ? 23.82581  5.79033   24.33943  1.000 6.09967   ?  37  THR A O   1 
ATOM   268  C  CB  . THR A 1 37  ? 21.80725  6.60771   22.42055  1.000 6.87043   ?  37  THR A CB  1 
ATOM   269  O  OG1 . THR A 1 37  ? 20.79817  5.79270   23.03434  1.000 7.77292   ?  37  THR A OG1 1 
ATOM   270  C  CG2 . THR A 1 37  ? 21.21375  7.33473   21.17013  1.000 9.63608   ?  37  THR A CG2 1 
ATOM   271  N  N   . ARG A 1 38  ? 23.51073  3.74715   23.44648  1.000 7.93723   ?  38  ARG A N   1 
ATOM   272  C  CA  . ARG A 1 38  ? 23.73925  3.05108   24.70809  1.000 7.58661   ?  38  ARG A CA  1 
ATOM   273  C  C   . ARG A 1 38  ? 24.94503  2.12619   24.60903  1.000 7.75758   ?  38  ARG A C   1 
ATOM   274  O  O   . ARG A 1 38  ? 25.18426  1.49451   23.57337  1.000 7.50338   ?  38  ARG A O   1 
ATOM   275  C  CB  . ARG A 1 38  ? 22.50670  2.23676   25.12230  1.000 6.55904   ?  38  ARG A CB  1 
ATOM   276  C  CG  . ARG A 1 38  ? 22.58602  1.68566   26.53427  1.000 7.92638   ?  38  ARG A CG  1 
ATOM   277  C  CD  . ARG A 1 38  ? 21.30477  0.96459   26.92231  1.000 7.41034   ?  38  ARG A CD  1 
ATOM   278  N  NE  . ARG A 1 38  ? 20.16735  1.87599   26.96444  1.000 8.80327   ?  38  ARG A NE  1 
ATOM   279  C  CZ  . ARG A 1 38  ? 18.99750  1.56699   27.50278  1.000 10.24841  ?  38  ARG A CZ  1 
ATOM   280  N  NH1 . ARG A 1 38  ? 18.75804  0.35410   27.96930  1.000 7.34505   ?  38  ARG A NH1 1 
ATOM   281  N  NH2 . ARG A 1 38  ? 18.04023  2.49482   27.56391  1.000 5.67109   ?  38  ARG A NH2 1 
ATOM   282  N  N   . PHE A 1 39  ? 25.67829  2.02206   25.72044  1.000 4.60727   ?  39  PHE A N   1 
ATOM   283  C  CA  . PHE A 1 39  ? 26.87090  1.19352   25.81130  1.000 4.97698   ?  39  PHE A CA  1 
ATOM   284  C  C   . PHE A 1 39  ? 26.80113  0.39325   27.10238  1.000 7.32183   ?  39  PHE A C   1 
ATOM   285  O  O   . PHE A 1 39  ? 26.31393  0.89853   28.11484  1.000 8.30020   ?  39  PHE A O   1 
ATOM   286  C  CB  . PHE A 1 39  ? 28.13304  2.06722   25.76881  1.000 5.96269   ?  39  PHE A CB  1 
ATOM   287  C  CG  . PHE A 1 39  ? 28.17328  2.97069   24.58224  1.000 11.30942  ?  39  PHE A CG  1 
ATOM   288  C  CD1 . PHE A 1 39  ? 27.47486  4.16732   24.58622  1.000 11.39927  ?  39  PHE A CD1 1 
ATOM   289  C  CD2 . PHE A 1 39  ? 28.86398  2.60083   23.43711  1.000 11.66422  ?  39  PHE A CD2 1 
ATOM   290  C  CE1 . PHE A 1 39  ? 27.48901  5.00093   23.48015  1.000 13.22743  ?  39  PHE A CE1 1 
ATOM   291  C  CE2 . PHE A 1 39  ? 28.87986  3.42351   22.31763  1.000 13.50892  ?  39  PHE A CE2 1 
ATOM   292  C  CZ  . PHE A 1 39  ? 28.18125  4.62113   22.33750  1.000 14.06384  ?  39  PHE A CZ  1 
ATOM   293  N  N   . LYS A 1 40  ? 27.29357  -0.85286  27.07795  1.000 7.65086   ?  40  LYS A N   1 
ATOM   294  C  CA  . LYS A 1 40  ? 26.85693  -1.78052  28.11784  1.000 10.84974  ?  40  LYS A CA  1 
ATOM   295  C  C   . LYS A 1 40  ? 27.88652  -2.87641  28.40425  1.000 10.30774  ?  40  LYS A C   1 
ATOM   296  O  O   . LYS A 1 40  ? 28.54139  -3.37678  27.48449  1.000 8.65366   ?  40  LYS A O   1 
ATOM   297  C  CB  . LYS A 1 40  ? 25.51994  -2.41045  27.69525  1.000 14.40241  ?  40  LYS A CB  1 
ATOM   298  C  CG  . LYS A 1 40  ? 25.25710  -3.77206  28.25776  1.000 16.34486  ?  40  LYS A CG  1 
ATOM   299  C  CD  . LYS A 1 40  ? 24.32275  -3.68679  29.42860  1.000 13.61481  ?  40  LYS A CD  1 
ATOM   300  C  CE  . LYS A 1 40  ? 22.93994  -3.41575  28.92630  1.000 14.26777  ?  40  LYS A CE  1 
ATOM   301  N  NZ  . LYS A 1 40  ? 21.97028  -3.25553  30.04649  1.000 17.50083  ?  40  LYS A NZ  1 
ATOM   302  N  N   . ARG A 1 41  ? 28.01682  -3.24338  29.69184  1.000 7.55369   ?  41  ARG A N   1 
ATOM   303  C  CA  . ARG A 1 41  ? 28.55700  -4.53928  30.09636  1.000 5.68700   ?  41  ARG A CA  1 
ATOM   304  C  C   . ARG A 1 41  ? 27.60758  -5.18108  31.10317  1.000 7.44886   ?  41  ARG A C   1 
ATOM   305  O  O   . ARG A 1 41  ? 26.77466  -4.50575  31.70184  1.000 7.60778   ?  41  ARG A O   1 
ATOM   306  C  CB  . ARG A 1 41  ? 29.97526  -4.42131  30.67502  1.000 5.47176   ?  41  ARG A CB  1 
ATOM   307  C  CG  . ARG A 1 41  ? 31.01561  -4.07272  29.62303  1.000 5.10933   ?  41  ARG A CG  1 
ATOM   308  C  CD  . ARG A 1 41  ? 32.41433  -3.88016  30.24659  1.000 6.05462   ?  41  ARG A CD  1 
ATOM   309  N  NE  . ARG A 1 41  ? 33.40279  -3.57401  29.21499  1.000 11.30412  ?  41  ARG A NE  1 
ATOM   310  C  CZ  . ARG A 1 41  ? 34.00966  -4.49421  28.47394  1.000 14.25490  ?  41  ARG A CZ  1 
ATOM   311  N  NH1 . ARG A 1 41  ? 33.80090  -5.78678  28.67547  1.000 12.66512  ?  41  ARG A NH1 1 
ATOM   312  N  NH2 . ARG A 1 41  ? 34.84971  -4.10956  27.51231  1.000 12.09884  ?  41  ARG A NH2 1 
ATOM   313  N  N   . PHE A 1 42  ? 27.69937  -6.50575  31.25490  1.000 8.15470   ?  42  PHE A N   1 
ATOM   314  C  CA  . PHE A 1 42  ? 26.66896  -7.25909  31.97039  1.000 6.40354   ?  42  PHE A CA  1 
ATOM   315  C  C   . PHE A 1 42  ? 27.32090  -8.42234  32.70189  1.000 8.29645   ?  42  PHE A C   1 
ATOM   316  O  O   . PHE A 1 42  ? 28.11900  -9.16662  32.12044  1.000 8.60158   ?  42  PHE A O   1 
ATOM   317  C  CB  . PHE A 1 42  ? 25.57634  -7.75012  30.99030  1.000 8.56032   ?  42  PHE A CB  1 
ATOM   318  C  CG  . PHE A 1 42  ? 24.56265  -8.71409  31.58892  1.000 8.49379   ?  42  PHE A CG  1 
ATOM   319  C  CD1 . PHE A 1 42  ? 23.50923  -8.25558  32.39268  1.000 6.57062   ?  42  PHE A CD1 1 
ATOM   320  C  CD2 . PHE A 1 42  ? 24.63775  -10.07076 31.29901  1.000 9.06890   ?  42  PHE A CD2 1 
ATOM   321  C  CE1 . PHE A 1 42  ? 22.56077  -9.14142  32.91924  1.000 7.83437   ?  42  PHE A CE1 1 
ATOM   322  C  CE2 . PHE A 1 42  ? 23.70252  -10.96585 31.81047  1.000 9.84696   ?  42  PHE A CE2 1 
ATOM   323  C  CZ  . PHE A 1 42  ? 22.65449  -10.50161 32.62268  1.000 8.77776   ?  42  PHE A CZ  1 
ATOM   324  N  N   . SER A 1 43  ? 27.01414  -8.55944  33.98870  1.000 7.52696   ?  43  SER A N   1 
ATOM   325  C  CA  . SER A 1 43  ? 27.45947  -9.72905  34.72828  1.000 9.74521   ?  43  SER A CA  1 
ATOM   326  C  C   . SER A 1 43  ? 26.38635  -10.12734 35.72791  1.000 9.97034   ?  43  SER A C   1 
ATOM   327  O  O   . SER A 1 43  ? 25.46955  -9.35712  36.02388  1.000 6.38933   ?  43  SER A O   1 
ATOM   328  C  CB  . SER A 1 43  ? 28.79085  -9.47850  35.45211  1.000 10.01556  ?  43  SER A CB  1 
ATOM   329  O  OG  . SER A 1 43  ? 29.87317  -9.40959  34.53600  1.000 9.00921   ?  43  SER A OG  1 
ATOM   330  N  N   . GLN A 1 44  ? 26.49753  -11.35987 36.23399  1.000 9.07939   ?  44  GLN A N   1 
ATOM   331  C  CA  . GLN A 1 44  ? 25.50055  -11.90704 37.14166  1.000 8.02141   ?  44  GLN A CA  1 
ATOM   332  C  C   . GLN A 1 44  ? 26.20161  -12.54445 38.33600  1.000 10.69773  ?  44  GLN A C   1 
ATOM   333  O  O   . GLN A 1 44  ? 27.28140  -13.12380 38.19204  1.000 9.97044   ?  44  GLN A O   1 
ATOM   334  C  CB  . GLN A 1 44  ? 24.59743  -12.93287 36.40683  1.000 6.49833   ?  44  GLN A CB  1 
ATOM   335  C  CG  . GLN A 1 44  ? 23.68561  -12.28466 35.34622  1.000 9.20092   ?  44  GLN A CG  1 
ATOM   336  C  CD  . GLN A 1 44  ? 23.04123  -13.31665 34.43322  1.000 12.91366  ?  44  GLN A CD  1 
ATOM   337  O  OE1 . GLN A 1 44  ? 23.72461  -13.97571 33.64538  1.000 10.00295  ?  44  GLN A OE1 1 
ATOM   338  N  NE2 . GLN A 1 44  ? 21.72094  -13.47681 34.55461  1.000 9.56886   ?  44  GLN A NE2 1 
ATOM   339  N  N   . TYR A 1 45  ? 25.57919  -12.43762 39.51568  1.000 5.97916   ?  45  TYR A N   1 
ATOM   340  C  CA  . TYR A 1 45  ? 26.18311  -12.94101 40.74356  1.000 9.14701   ?  45  TYR A CA  1 
ATOM   341  C  C   . TYR A 1 45  ? 25.17489  -13.71720 41.56969  1.000 13.19591  ?  45  TYR A C   1 
ATOM   342  O  O   . TYR A 1 45  ? 23.97619  -13.41917 41.56246  1.000 8.00060   ?  45  TYR A O   1 
ATOM   343  C  CB  . TYR A 1 45  ? 26.72660  -11.82104 41.65107  1.000 8.01485   ?  45  TYR A CB  1 
ATOM   344  C  CG  . TYR A 1 45  ? 27.83721  -10.97801 41.08195  1.000 9.47865   ?  45  TYR A CG  1 
ATOM   345  C  CD1 . TYR A 1 45  ? 27.56875  -9.94980  40.18216  1.000 13.48442  ?  45  TYR A CD1 1 
ATOM   346  C  CD2 . TYR A 1 45  ? 29.15160  -11.16606 41.48476  1.000 12.13365  ?  45  TYR A CD2 1 
ATOM   347  C  CE1 . TYR A 1 45  ? 28.59226  -9.15625  39.67883  1.000 11.11322  ?  45  TYR A CE1 1 
ATOM   348  C  CE2 . TYR A 1 45  ? 30.17406  -10.38800 40.98739  1.000 14.18503  ?  45  TYR A CE2 1 
ATOM   349  C  CZ  . TYR A 1 45  ? 29.89249  -9.38189  40.08776  1.000 18.09362  ?  45  TYR A CZ  1 
ATOM   350  O  OH  . TYR A 1 45  ? 30.91402  -8.60319  39.60388  1.000 17.89375  ?  45  TYR A OH  1 
ATOM   351  N  N   . LYS A 1 46  ? 25.68790  -14.68764 42.32883  1.000 8.88928   ?  46  LYS A N   1 
ATOM   352  C  CA  . LYS A 1 46  ? 24.94926  -15.23541 43.45075  1.000 9.01841   ?  46  LYS A CA  1 
ATOM   353  C  C   . LYS A 1 46  ? 25.30068  -14.46762 44.72123  1.000 10.38264  ?  46  LYS A C   1 
ATOM   354  O  O   . LYS A 1 46  ? 26.47168  -14.14172 44.96505  1.000 14.13776  ?  46  LYS A O   1 
ATOM   355  C  CB  . LYS A 1 46  ? 25.24977  -16.73127 43.63827  1.000 14.53324  ?  46  LYS A CB  1 
ATOM   356  C  CG  . LYS A 1 46  ? 24.59903  -17.29411 44.88822  1.000 13.35474  ?  46  LYS A CG  1 
ATOM   357  C  CD  . LYS A 1 46  ? 24.40353  -18.82759 44.84301  1.000 28.35773  ?  46  LYS A CD  1 
ATOM   358  C  CE  . LYS A 1 46  ? 25.63013  -19.57307 45.28368  1.000 25.80000  ?  46  LYS A CE  1 
ATOM   359  N  NZ  . LYS A 1 46  ? 25.30595  -20.92955 45.83735  1.000 19.29346  ?  46  LYS A NZ  1 
ATOM   360  N  N   . LEU A 1 47  ? 24.27304  -14.16977 45.52406  1.000 10.74607  ?  47  LEU A N   1 
ATOM   361  C  CA  . LEU A 1 47  ? 24.42417  -13.54799 46.83510  1.000 14.49316  ?  47  LEU A CA  1 
ATOM   362  C  C   . LEU A 1 47  ? 24.01981  -14.56763 47.88377  1.000 16.97480  ?  47  LEU A C   1 
ATOM   363  O  O   . LEU A 1 47  ? 22.85410  -14.97941 47.92419  1.000 15.98851  ?  47  LEU A O   1 
ATOM   364  C  CB  . LEU A 1 47  ? 23.53255  -12.31889 47.01315  1.000 13.96397  ?  47  LEU A CB  1 
ATOM   365  C  CG  . LEU A 1 47  ? 23.57294  -11.12286 46.10334  1.000 23.56965  ?  47  LEU A CG  1 
ATOM   366  C  CD1 . LEU A 1 47  ? 22.69427  -10.00200 46.71140  1.000 16.10586  ?  47  LEU A CD1 1 
ATOM   367  C  CD2 . LEU A 1 47  ? 25.00684  -10.70845 45.98931  1.000 22.39637  ?  47  LEU A CD2 1 
ATOM   368  N  N   . THR A 1 48  ? 24.95441  -14.92222 48.76385  1.000 18.85942  ?  48  THR A N   1 
ATOM   369  C  CA  . THR A 1 48  ? 24.64819  -15.86445 49.82152  1.000 16.94864  ?  48  THR A CA  1 
ATOM   370  C  C   . THR A 1 48  ? 24.84515  -15.20438 51.17826  1.000 24.15677  ?  48  THR A C   1 
ATOM   371  O  O   . THR A 1 48  ? 25.83138  -14.48570 51.38005  1.000 19.93898  ?  48  THR A O   1 
ATOM   372  C  CB  . THR A 1 48  ? 25.54057  -17.11508 49.73454  1.000 22.56659  ?  48  THR A CB  1 
ATOM   373  O  OG1 . THR A 1 48  ? 26.90377  -16.75139 49.98902  1.000 34.17957  ?  48  THR A OG1 1 
ATOM   374  C  CG2 . THR A 1 48  ? 25.45213  -17.72661 48.36982  1.000 24.12669  ?  48  THR A CG2 1 
ATOM   375  N  N   . PRO A 1 49  ? 23.92068  -15.41028 52.11590  1.000 24.46097  ?  49  PRO A N   1 
ATOM   376  C  CA  . PRO A 1 49  ? 24.17389  -14.99480 53.49827  1.000 20.63742  ?  49  PRO A CA  1 
ATOM   377  C  C   . PRO A 1 49  ? 25.42971  -15.67756 54.02011  1.000 16.00640  ?  49  PRO A C   1 
ATOM   378  O  O   . PRO A 1 49  ? 25.67322  -16.85826 53.74514  1.000 20.72818  ?  49  PRO A O   1 
ATOM   379  C  CB  . PRO A 1 49  ? 22.92609  -15.46764 54.25238  1.000 21.71294  ?  49  PRO A CB  1 
ATOM   380  C  CG  . PRO A 1 49  ? 21.91043  -15.74705 53.20802  1.000 25.78721  ?  49  PRO A CG  1 
ATOM   381  C  CD  . PRO A 1 49  ? 22.64723  -16.12728 51.96888  1.000 22.36853  ?  49  PRO A CD  1 
ATOM   382  N  N   . ALA A 1 50  ? 26.23601  -14.91132 54.75084  1.000 18.21124  ?  50  ALA A N   1 
ATOM   383  C  CA  . ALA A 1 50  ? 27.51432  -15.36177 55.28743  1.000 26.30901  ?  50  ALA A CA  1 
ATOM   384  C  C   . ALA A 1 50  ? 27.58520  -15.05215 56.77857  1.000 28.72278  ?  50  ALA A C   1 
ATOM   385  O  O   . ALA A 1 50  ? 26.77254  -14.28608 57.31096  1.000 25.36546  ?  50  ALA A O   1 
ATOM   386  C  CB  . ALA A 1 50  ? 28.69171  -14.69989 54.54723  1.000 20.24286  ?  50  ALA A CB  1 
ATOM   387  N  N   . GLU A 1 51  ? 28.59151  -15.65357 57.43555  1.000 31.25457  ?  51  GLU A N   1 
ATOM   388  C  CA  . GLU A 1 51  ? 28.83687  -15.48100 58.86745  1.000 41.67869  ?  51  GLU A CA  1 
ATOM   389  C  C   . GLU A 1 51  ? 28.81455  -14.01253 59.26749  1.000 34.38204  ?  51  GLU A C   1 
ATOM   390  O  O   . GLU A 1 51  ? 29.10912  -13.12427 58.46311  1.000 27.64758  ?  51  GLU A O   1 
ATOM   391  C  CB  . GLU A 1 51  ? 30.20161  -16.07314 59.26109  1.000 38.81722  ?  51  GLU A CB  1 
ATOM   392  C  CG  . GLU A 1 51  ? 30.14189  -17.48050 59.80386  1.000 51.40474  ?  51  GLU A CG  1 
ATOM   393  C  CD  . GLU A 1 51  ? 31.17923  -17.77698 60.87595  1.000 55.68446  ?  51  GLU A CD  1 
ATOM   394  O  OE1 . GLU A 1 51  ? 32.34442  -18.04822 60.51524  1.000 47.56492  ?  51  GLU A OE1 1 
ATOM   395  O  OE2 . GLU A 1 51  ? 30.81741  -17.75315 62.07558  1.000 55.43736  -1 51  GLU A OE2 1 
ATOM   396  N  N   . ASP A 1 52  ? 28.47243  -13.76773 60.53681  1.000 40.89158  ?  52  ASP A N   1 
ATOM   397  C  CA  . ASP A 1 52  ? 28.62144  -12.45069 61.16398  1.000 36.53869  ?  52  ASP A CA  1 
ATOM   398  C  C   . ASP A 1 52  ? 27.83471  -11.37736 60.40955  1.000 36.98556  ?  52  ASP A C   1 
ATOM   399  O  O   . ASP A 1 52  ? 28.28962  -10.24379 60.25731  1.000 32.58218  ?  52  ASP A O   1 
ATOM   400  C  CB  . ASP A 1 52  ? 30.10307  -12.06146 61.28859  1.000 47.61128  ?  52  ASP A CB  1 
ATOM   401  C  CG  . ASP A 1 52  ? 30.67696  -12.33063 62.68465  1.000 54.41179  ?  52  ASP A CG  1 
ATOM   402  O  OD1 . ASP A 1 52  ? 29.92689  -12.20812 63.68302  1.000 60.58520  ?  52  ASP A OD1 1 
ATOM   403  O  OD2 . ASP A 1 52  ? 31.89167  -12.63161 62.77764  1.000 58.10920  -1 52  ASP A OD2 1 
ATOM   404  N  N   . ASP A 1 53  ? 26.65160  -11.75006 59.90734  1.000 35.40116  ?  53  ASP A N   1 
ATOM   405  C  CA  . ASP A 1 53  ? 25.69197  -10.80515 59.32216  1.000 24.96563  ?  53  ASP A CA  1 
ATOM   406  C  C   . ASP A 1 53  ? 26.19298  -10.19402 58.00698  1.000 27.82613  ?  53  ASP A C   1 
ATOM   407  O  O   . ASP A 1 53  ? 25.87389  -9.04852  57.67817  1.000 28.31175  ?  53  ASP A O   1 
ATOM   408  C  CB  . ASP A 1 53  ? 25.33333  -9.70101  60.32651  1.000 36.39644  ?  53  ASP A CB  1 
ATOM   409  C  CG  . ASP A 1 53  ? 24.10623  -8.89124  59.90961  1.000 41.84664  ?  53  ASP A CG  1 
ATOM   410  O  OD1 . ASP A 1 53  ? 22.99050  -9.45349  59.88621  1.000 45.09781  ?  53  ASP A OD1 1 
ATOM   411  O  OD2 . ASP A 1 53  ? 24.25924  -7.68561  59.60893  1.000 56.79718  -1 53  ASP A OD2 1 
ATOM   412  N  N   . THR A 1 54  ? 26.95877  -10.94681 57.22203  1.000 20.57787  ?  54  THR A N   1 
ATOM   413  C  CA  . THR A 1 54  ? 27.53739  -10.45118 55.97835  1.000 24.94037  ?  54  THR A CA  1 
ATOM   414  C  C   . THR A 1 54  ? 26.90212  -11.14854 54.77988  1.000 21.82495  ?  54  THR A C   1 
ATOM   415  O  O   . THR A 1 54  ? 26.11740  -12.09234 54.92244  1.000 24.30219  ?  54  THR A O   1 
ATOM   416  C  CB  . THR A 1 54  ? 29.05825  -10.66130 55.97163  1.000 21.44564  ?  54  THR A CB  1 
ATOM   417  O  OG1 . THR A 1 54  ? 29.34006  -12.06206 55.92507  1.000 27.70003  ?  54  THR A OG1 1 
ATOM   418  C  CG2 . THR A 1 54  ? 29.67905  -10.07807 57.23842  1.000 33.65838  ?  54  THR A CG2 1 
ATOM   419  N  N   . TRP A 1 55  ? 27.25803  -10.68044 53.57889  1.000 20.23265  ?  55  TRP A N   1 
ATOM   420  C  CA  . TRP A 1 55  ? 26.83017  -11.31758 52.33724  1.000 22.36976  ?  55  TRP A CA  1 
ATOM   421  C  C   . TRP A 1 55  ? 28.03821  -11.62590 51.46609  1.000 16.51408  ?  55  TRP A C   1 
ATOM   422  O  O   . TRP A 1 55  ? 28.95025  -10.81205 51.33834  1.000 17.36341  ?  55  TRP A O   1 
ATOM   423  C  CB  . TRP A 1 55  ? 25.85259  -10.44283 51.53371  1.000 24.46264  ?  55  TRP A CB  1 
ATOM   424  C  CG  . TRP A 1 55  ? 24.49626  -10.32977 52.14930  1.000 15.23694  ?  55  TRP A CG  1 
ATOM   425  C  CD1 . TRP A 1 55  ? 24.11836  -9.44983  53.11123  1.000 18.36799  ?  55  TRP A CD1 1 
ATOM   426  C  CD2 . TRP A 1 55  ? 23.33998  -11.11002 51.84057  1.000 13.63175  ?  55  TRP A CD2 1 
ATOM   427  N  NE1 . TRP A 1 55  ? 22.79368  -9.62315  53.41799  1.000 17.46003  ?  55  TRP A NE1 1 
ATOM   428  C  CE2 . TRP A 1 55  ? 22.29364  -10.64500 52.66038  1.000 13.47219  ?  55  TRP A CE2 1 
ATOM   429  C  CE3 . TRP A 1 55  ? 23.08218  -12.15371 50.94431  1.000 16.87098  ?  55  TRP A CE3 1 
ATOM   430  C  CZ2 . TRP A 1 55  ? 21.00896  -11.18878 52.62030  1.000 13.35297  ?  55  TRP A CZ2 1 
ATOM   431  C  CZ3 . TRP A 1 55  ? 21.80694  -12.69440 50.90414  1.000 24.06684  ?  55  TRP A CZ3 1 
ATOM   432  C  CH2 . TRP A 1 55  ? 20.78434  -12.20737 51.73944  1.000 16.13919  ?  55  TRP A CH2 1 
ATOM   433  N  N   . SER A 1 56  ? 28.02554  -12.78788 50.83914  1.000 16.48066  ?  56  SER A N   1 
ATOM   434  C  CA  . SER A 1 56  ? 29.11240  -13.19960 49.96428  1.000 22.56374  ?  56  SER A CA  1 
ATOM   435  C  C   . SER A 1 56  ? 28.65555  -13.11134 48.50988  1.000 21.10134  ?  56  SER A C   1 
ATOM   436  O  O   . SER A 1 56  ? 27.52280  -13.48340 48.19245  1.000 18.19692  ?  56  SER A O   1 
ATOM   437  C  CB  . SER A 1 56  ? 29.56567  -14.61894 50.32054  1.000 26.55443  ?  56  SER A CB  1 
ATOM   438  O  OG  . SER A 1 56  ? 30.28054  -15.20791 49.25273  1.000 34.98554  ?  56  SER A OG  1 
ATOM   439  N  N   . PHE A 1 57  ? 29.51882  -12.57544 47.64007  1.000 17.60874  ?  57  PHE A N   1 
ATOM   440  C  CA  . PHE A 1 57  ? 29.23673  -12.44151 46.21088  1.000 15.53776  ?  57  PHE A CA  1 
ATOM   441  C  C   . PHE A 1 57  ? 30.02354  -13.47377 45.41728  1.000 16.40225  ?  57  PHE A C   1 
ATOM   442  O  O   . PHE A 1 57  ? 31.23067  -13.62880 45.61852  1.000 19.45511  ?  57  PHE A O   1 
ATOM   443  C  CB  . PHE A 1 57  ? 29.62458  -11.05971 45.66494  1.000 12.37884  ?  57  PHE A CB  1 
ATOM   444  C  CG  . PHE A 1 57  ? 28.88362  -9.91207  46.27934  1.000 16.86736  ?  57  PHE A CG  1 
ATOM   445  C  CD1 . PHE A 1 57  ? 29.20695  -9.46134  47.54700  1.000 25.00448  ?  57  PHE A CD1 1 
ATOM   446  C  CD2 . PHE A 1 57  ? 27.90571  -9.24682  45.56616  1.000 21.02278  ?  57  PHE A CD2 1 
ATOM   447  C  CE1 . PHE A 1 57  ? 28.54180  -8.39633  48.11230  1.000 20.81851  ?  57  PHE A CE1 1 
ATOM   448  C  CE2 . PHE A 1 57  ? 27.23800  -8.16732  46.12174  1.000 20.34588  ?  57  PHE A CE2 1 
ATOM   449  C  CZ  . PHE A 1 57  ? 27.55167  -7.75274  47.40336  1.000 19.50487  ?  57  PHE A CZ  1 
ATOM   450  N  N   . LYS A 1 58  ? 29.36414  -14.13659 44.47053  1.000 10.36985  ?  58  LYS A N   1 
ATOM   451  C  CA  . LYS A 1 58  ? 30.05907  -15.03240 43.55238  1.000 13.45098  ?  58  LYS A CA  1 
ATOM   452  C  C   . LYS A 1 58  ? 29.66214  -14.71892 42.12552  1.000 9.21691   ?  58  LYS A C   1 
ATOM   453  O  O   . LYS A 1 58  ? 28.48645  -14.83980 41.76696  1.000 13.46026  ?  58  LYS A O   1 
ATOM   454  C  CB  . LYS A 1 58  ? 29.76160  -16.49741 43.83984  1.000 14.77782  ?  58  LYS A CB  1 
ATOM   455  C  CG  . LYS A 1 58  ? 30.53784  -17.39909 42.89469  1.000 24.12887  ?  58  LYS A CG  1 
ATOM   456  C  CD  . LYS A 1 58  ? 30.37951  -18.85036 43.25522  1.000 27.76624  ?  58  LYS A CD  1 
ATOM   457  C  CE  . LYS A 1 58  ? 31.48473  -19.67991 42.63122  1.000 40.23296  ?  58  LYS A CE  1 
ATOM   458  N  NZ  . LYS A 1 58  ? 32.73738  -19.71122 43.44378  1.000 42.19046  ?  58  LYS A NZ  1 
ATOM   459  N  N   . ARG A 1 59  ? 30.63830  -14.34035 41.31336  1.000 13.68976  ?  59  ARG A N   1 
ATOM   460  C  CA  . ARG A 1 59  ? 30.36729  -14.06041 39.90899  1.000 15.72579  ?  59  ARG A CA  1 
ATOM   461  C  C   . ARG A 1 59  ? 30.04560  -15.35683 39.17852  1.000 17.98285  ?  59  ARG A C   1 
ATOM   462  O  O   . ARG A 1 59  ? 30.81540  -16.32203 39.23449  1.000 14.92270  ?  59  ARG A O   1 
ATOM   463  C  CB  . ARG A 1 59  ? 31.56406  -13.36545 39.26659  1.000 14.40111  ?  59  ARG A CB  1 
ATOM   464  C  CG  . ARG A 1 59  ? 31.29659  -12.79542 37.88338  1.000 20.67781  ?  59  ARG A CG  1 
ATOM   465  C  CD  . ARG A 1 59  ? 32.60146  -12.26183 37.29193  1.000 24.64853  ?  59  ARG A CD  1 
ATOM   466  N  NE  . ARG A 1 59  ? 33.01453  -10.98902 37.87895  1.000 38.01849  ?  59  ARG A NE  1 
ATOM   467  C  CZ  . ARG A 1 59  ? 32.98655  -9.83169  37.22881  1.000 30.84669  ?  59  ARG A CZ  1 
ATOM   468  N  NH1 . ARG A 1 59  ? 32.55992  -9.75621  35.97864  1.000 19.47752  ?  59  ARG A NH1 1 
ATOM   469  N  NH2 . ARG A 1 59  ? 33.40927  -8.72638  37.84318  1.000 32.24292  ?  59  ARG A NH2 1 
ATOM   470  N  N   . LEU A 1 60  ? 28.89957  -15.38711 38.51046  1.000 10.14103  ?  60  LEU A N   1 
ATOM   471  C  CA  . LEU A 1 60  ? 28.47045  -16.60820 37.84664  1.000 11.90478  ?  60  LEU A CA  1 
ATOM   472  C  C   . LEU A 1 60  ? 29.09754  -16.71302 36.46439  1.000 12.57788  ?  60  LEU A C   1 
ATOM   473  O  O   . LEU A 1 60  ? 29.49533  -15.70173 35.87645  1.000 10.66479  ?  60  LEU A O   1 
ATOM   474  C  CB  . LEU A 1 60  ? 26.94130  -16.63025 37.74119  1.000 8.70550   ?  60  LEU A CB  1 
ATOM   475  C  CG  . LEU A 1 60  ? 26.21542  -16.67706 39.08634  1.000 12.85327  ?  60  LEU A CG  1 
ATOM   476  C  CD1 . LEU A 1 60  ? 24.73227  -16.30097 38.96989  1.000 10.24545  ?  60  LEU A CD1 1 
ATOM   477  C  CD2 . LEU A 1 60  ? 26.37509  -18.07536 39.68708  1.000 15.70739  ?  60  LEU A CD2 1 
ATOM   478  N  N   . PRO A 1 61  ? 29.21463  -17.93346 35.92367  1.000 11.48114  ?  61  PRO A N   1 
ATOM   479  C  CA  . PRO A 1 61  ? 29.65871  -18.08767 34.53092  1.000 12.87017  ?  61  PRO A CA  1 
ATOM   480  C  C   . PRO A 1 61  ? 28.86880  -17.18882 33.58762  1.000 13.53766  ?  61  PRO A C   1 
ATOM   481  O  O   . PRO A 1 61  ? 27.64708  -17.05549 33.69522  1.000 11.87373  ?  61  PRO A O   1 
ATOM   482  C  CB  . PRO A 1 61  ? 29.40928  -19.57400 34.24317  1.000 17.18921  ?  61  PRO A CB  1 
ATOM   483  C  CG  . PRO A 1 61  ? 29.61082  -20.23477 35.58958  1.000 14.38783  ?  61  PRO A CG  1 
ATOM   484  C  CD  . PRO A 1 61  ? 29.02846  -19.23797 36.59406  1.000 12.09389  ?  61  PRO A CD  1 
ATOM   485  N  N   . HIS A 1 62  ? 29.58852  -16.56480 32.66302  1.000 11.87004  ?  62  HIS A N   1 
ATOM   486  C  CA  . HIS A 1 62  ? 29.01337  -15.50446 31.84465  1.000 14.13748  ?  62  HIS A CA  1 
ATOM   487  C  C   . HIS A 1 62  ? 28.01868  -16.06879 30.83903  1.000 15.37189  ?  62  HIS A C   1 
ATOM   488  O  O   . HIS A 1 62  ? 28.33545  -16.99285 30.09008  1.000 14.09543  ?  62  HIS A O   1 
ATOM   489  C  CB  . HIS A 1 62  ? 30.12277  -14.76307 31.11877  1.000 15.39315  ?  62  HIS A CB  1 
ATOM   490  C  CG  . HIS A 1 62  ? 29.64761  -13.54901 30.39301  1.000 13.84131  ?  62  HIS A CG  1 
ATOM   491  N  ND1 . HIS A 1 62  ? 29.19588  -12.42401 31.05041  1.000 10.47706  ?  62  HIS A ND1 1 
ATOM   492  C  CD2 . HIS A 1 62  ? 29.53532  -13.28796 29.06945  1.000 15.73991  ?  62  HIS A CD2 1 
ATOM   493  C  CE1 . HIS A 1 62  ? 28.83130  -11.51741 30.15684  1.000 15.65065  ?  62  HIS A CE1 1 
ATOM   494  N  NE2 . HIS A 1 62  ? 29.02960  -12.01627 28.94858  1.000 14.13897  ?  62  HIS A NE2 1 
ATOM   495  N  N   . ARG A 1 63  ? 26.82059  -15.49383 30.80652  1.000 12.36321  ?  63  ARG A N   1 
ATOM   496  C  CA  . ARG A 1 63  ? 25.75847  -15.94771 29.92078  1.000 12.36222  ?  63  ARG A CA  1 
ATOM   497  C  C   . ARG A 1 63  ? 25.06615  -14.74981 29.28476  1.000 14.32288  ?  63  ARG A C   1 
ATOM   498  O  O   . ARG A 1 63  ? 25.11301  -13.62910 29.80740  1.000 9.81035   ?  63  ARG A O   1 
ATOM   499  C  CB  . ARG A 1 63  ? 24.72533  -16.77954 30.67033  1.000 9.78140   ?  63  ARG A CB  1 
ATOM   500  C  CG  . ARG A 1 63  ? 25.24513  -18.11934 31.18823  1.000 13.20639  ?  63  ARG A CG  1 
ATOM   501  C  CD  . ARG A 1 63  ? 24.18099  -18.79598 32.01218  1.000 14.13299  ?  63  ARG A CD  1 
ATOM   502  N  NE  . ARG A 1 63  ? 23.04020  -19.22544 31.20806  1.000 14.72982  ?  63  ARG A NE  1 
ATOM   503  C  CZ  . ARG A 1 63  ? 22.91745  -20.44022 30.68265  1.000 18.61847  ?  63  ARG A CZ  1 
ATOM   504  N  NH1 . ARG A 1 63  ? 23.86486  -21.35465 30.82343  1.000 13.55465  ?  63  ARG A NH1 1 
ATOM   505  N  NH2 . ARG A 1 63  ? 21.81642  -20.74691 30.00779  1.000 17.83015  ?  63  ARG A NH2 1 
ATOM   506  N  N   . ASP A 1 64  ? 24.41894  -15.00796 28.14289  1.000 8.83584   ?  64  ASP A N   1 
ATOM   507  C  CA  . ASP A 1 64  ? 23.59566  -13.99567 27.49328  1.000 11.85429  ?  64  ASP A CA  1 
ATOM   508  C  C   . ASP A 1 64  ? 22.50704  -13.51978 28.44163  1.000 8.28126   ?  64  ASP A C   1 
ATOM   509  O  O   . ASP A 1 64  ? 21.95255  -14.29979 29.22183  1.000 10.78615  ?  64  ASP A O   1 
ATOM   510  C  CB  . ASP A 1 64  ? 22.91005  -14.54377 26.23267  1.000 7.69191   ?  64  ASP A CB  1 
ATOM   511  C  CG  . ASP A 1 64  ? 23.88456  -15.04608 25.17887  1.000 15.84356  ?  64  ASP A CG  1 
ATOM   512  O  OD1 . ASP A 1 64  ? 25.06063  -14.64699 25.16928  1.000 14.37670  ?  64  ASP A OD1 1 
ATOM   513  O  OD2 . ASP A 1 64  ? 23.44521  -15.84426 24.32976  1.000 15.80043  -1 64  ASP A OD2 1 
ATOM   514  N  N   . TYR A 1 65  ? 22.17858  -12.24008 28.34559  1.000 5.87576   ?  65  TYR A N   1 
ATOM   515  C  CA  . TYR A 1 65  ? 21.06109  -11.69737 29.09880  1.000 8.82454   ?  65  TYR A CA  1 
ATOM   516  C  C   . TYR A 1 65  ? 19.76344  -12.06446 28.39063  1.000 11.09843  ?  65  TYR A C   1 
ATOM   517  O  O   . TYR A 1 65  ? 19.66053  -11.94287 27.16621  1.000 9.53467   ?  65  TYR A O   1 
ATOM   518  C  CB  . TYR A 1 65  ? 21.20378  -10.17363 29.22983  1.000 8.13374   ?  65  TYR A CB  1 
ATOM   519  C  CG  . TYR A 1 65  ? 20.02026  -9.50205  29.88342  1.000 6.55962   ?  65  TYR A CG  1 
ATOM   520  C  CD1 . TYR A 1 65  ? 19.57019  -9.90657  31.13707  1.000 8.57966   ?  65  TYR A CD1 1 
ATOM   521  C  CD2 . TYR A 1 65  ? 19.35255  -8.45551  29.24600  1.000 11.55020  ?  65  TYR A CD2 1 
ATOM   522  C  CE1 . TYR A 1 65  ? 18.48077  -9.30365  31.73085  1.000 9.16819   ?  65  TYR A CE1 1 
ATOM   523  C  CE2 . TYR A 1 65  ? 18.26848  -7.84066  29.82984  1.000 11.11247  ?  65  TYR A CE2 1 
ATOM   524  C  CZ  . TYR A 1 65  ? 17.83926  -8.26165  31.07210  1.000 7.59377   ?  65  TYR A CZ  1 
ATOM   525  O  OH  . TYR A 1 65  ? 16.75912  -7.63959  31.64644  1.000 9.53187   ?  65  TYR A OH  1 
ATOM   526  N  N   . THR A 1 66  ? 18.78616  -12.54988 29.14881  1.000 9.29768   ?  66  THR A N   1 
ATOM   527  C  CA  . THR A 1 66  ? 17.45499  -12.76885 28.58914  1.000 8.63971   ?  66  THR A CA  1 
ATOM   528  C  C   . THR A 1 66  ? 16.42763  -12.20367 29.55442  1.000 9.03267   ?  66  THR A C   1 
ATOM   529  O  O   . THR A 1 66  ? 16.53778  -12.38210 30.77545  1.000 9.57513   ?  66  THR A O   1 
ATOM   530  C  CB  . THR A 1 66  ? 17.16238  -14.26033 28.35669  1.000 9.23068   ?  66  THR A CB  1 
ATOM   531  O  OG1 . THR A 1 66  ? 17.38876  -14.96166 29.57847  1.000 13.89988  ?  66  THR A OG1 1 
ATOM   532  C  CG2 . THR A 1 66  ? 18.06998  -14.83885 27.28085  1.000 15.34170  ?  66  THR A CG2 1 
ATOM   533  N  N   . THR A 1 67  ? 15.43400  -11.51661 29.00875  1.000 6.90198   ?  67  THR A N   1 
ATOM   534  C  CA  . THR A 1 67  ? 14.31788  -11.05920 29.81256  1.000 7.59967   ?  67  THR A CA  1 
ATOM   535  C  C   . THR A 1 67  ? 13.04113  -11.34192 29.03572  1.000 9.37650   ?  67  THR A C   1 
ATOM   536  O  O   . THR A 1 67  ? 13.08055  -11.81503 27.89697  1.000 10.08288  ?  67  THR A O   1 
ATOM   537  C  CB  . THR A 1 67  ? 14.46929  -9.58122  30.21441  1.000 8.18662   ?  67  THR A CB  1 
ATOM   538  O  OG1 . THR A 1 67  ? 13.38434  -9.22976  31.06741  1.000 8.40014   ?  67  THR A OG1 1 
ATOM   539  C  CG2 . THR A 1 67  ? 14.51145  -8.64610  29.01589  1.000 9.26619   ?  67  THR A CG2 1 
ATOM   540  N  N   . TYR A 1 68  ? 11.90213  -11.09424 29.68365  1.000 10.49731  ?  68  TYR A N   1 
ATOM   541  C  CA  . TYR A 1 68  ? 10.60001  -11.45375 29.13394  1.000 12.65307  ?  68  TYR A CA  1 
ATOM   542  C  C   . TYR A 1 68  ? 10.01200  -10.29508 28.35326  1.000 13.03411  ?  68  TYR A C   1 
ATOM   543  O  O   . TYR A 1 68  ? 10.06948  -9.14536  28.79567  1.000 8.33480   ?  68  TYR A O   1 
ATOM   544  C  CB  . TYR A 1 68  ? 9.60972   -11.82444 30.23997  1.000 13.08035  ?  68  TYR A CB  1 
ATOM   545  C  CG  . TYR A 1 68  ? 9.93030   -13.04954 31.07498  1.000 11.59415  ?  68  TYR A CG  1 
ATOM   546  C  CD1 . TYR A 1 68  ? 10.87382  -13.00153 32.10018  1.000 11.88731  ?  68  TYR A CD1 1 
ATOM   547  C  CD2 . TYR A 1 68  ? 9.24127   -14.23605 30.87144  1.000 11.69368  ?  68  TYR A CD2 1 
ATOM   548  C  CE1 . TYR A 1 68  ? 11.13940  -14.11798 32.88693  1.000 10.02916  ?  68  TYR A CE1 1 
ATOM   549  C  CE2 . TYR A 1 68  ? 9.50333   -15.36091 31.63857  1.000 15.21415  ?  68  TYR A CE2 1 
ATOM   550  C  CZ  . TYR A 1 68  ? 10.44791  -15.29253 32.65059  1.000 16.52856  ?  68  TYR A CZ  1 
ATOM   551  O  OH  . TYR A 1 68  ? 10.69477  -16.40502 33.41198  1.000 13.53901  ?  68  TYR A OH  1 
ATOM   552  N  N   . LYS A 1 69  ? 9.39363   -10.61342 27.21282  1.000 11.44331  ?  69  LYS A N   1 
ATOM   553  C  CA  . LYS A 1 69  ? 8.65413   -9.59251  26.47580  1.000 14.36807  ?  69  LYS A CA  1 
ATOM   554  C  C   . LYS A 1 69  ? 7.54482   -8.97726  27.32332  1.000 9.26662   ?  69  LYS A C   1 
ATOM   555  O  O   . LYS A 1 69  ? 7.22399   -7.78939  27.16450  1.000 12.30257  ?  69  LYS A O   1 
ATOM   556  C  CB  . LYS A 1 69  ? 8.08100   -10.18539 25.18823  1.000 18.05841  ?  69  LYS A CB  1 
ATOM   557  C  CG  . LYS A 1 69  ? 8.74678   -9.62655  23.95830  1.000 32.48997  ?  69  LYS A CG  1 
ATOM   558  C  CD  . LYS A 1 69  ? 8.17529   -10.21938 22.69366  1.000 33.90372  ?  69  LYS A CD  1 
ATOM   559  C  CE  . LYS A 1 69  ? 9.28323   -10.79157 21.82449  1.000 35.48869  ?  69  LYS A CE  1 
ATOM   560  N  NZ  . LYS A 1 69  ? 8.87728   -10.83818 20.38971  1.000 36.44131  ?  69  LYS A NZ  1 
ATOM   561  N  N   . LYS A 1 70  ? 6.97780   -9.74674  28.25535  1.000 10.76593  ?  70  LYS A N   1 
ATOM   562  C  CA  . LYS A 1 70  ? 5.88960   -9.21530  29.06374  1.000 17.66322  ?  70  LYS A CA  1 
ATOM   563  C  C   . LYS A 1 70  ? 6.35218   -8.05776  29.93145  1.000 16.59088  ?  70  LYS A C   1 
ATOM   564  O  O   . LYS A 1 70  ? 5.53820   -7.20165  30.28133  1.000 14.94212  ?  70  LYS A O   1 
ATOM   565  C  CB  . LYS A 1 70  ? 5.25682   -10.31660 29.93075  1.000 14.63665  ?  70  LYS A CB  1 
ATOM   566  C  CG  . LYS A 1 70  ? 6.01863   -10.66630 31.19213  1.000 19.81583  ?  70  LYS A CG  1 
ATOM   567  C  CD  . LYS A 1 70  ? 5.28971   -11.69050 32.07549  1.000 28.61921  ?  70  LYS A CD  1 
ATOM   568  C  CE  . LYS A 1 70  ? 5.63050   -13.12015 31.68771  1.000 35.49364  ?  70  LYS A CE  1 
ATOM   569  N  NZ  . LYS A 1 70  ? 5.45961   -14.08608 32.81740  1.000 32.30321  ?  70  LYS A NZ  1 
ATOM   570  N  N   . PHE A 1 71  ? 7.64179   -7.99786  30.26554  1.000 13.64651  ?  71  PHE A N   1 
ATOM   571  C  CA  . PHE A 1 71  ? 8.19112   -6.89539  31.04912  1.000 9.82784   ?  71  PHE A CA  1 
ATOM   572  C  C   . PHE A 1 71  ? 8.89034   -5.86172  30.19337  1.000 14.11928  ?  71  PHE A C   1 
ATOM   573  O  O   . PHE A 1 71  ? 8.83699   -4.66954  30.49737  1.000 14.74550  ?  71  PHE A O   1 
ATOM   574  C  CB  . PHE A 1 71  ? 9.19916   -7.41080  32.08287  1.000 12.30023  ?  71  PHE A CB  1 
ATOM   575  C  CG  . PHE A 1 71  ? 8.62722   -8.40215  33.05501  1.000 11.84117  ?  71  PHE A CG  1 
ATOM   576  C  CD1 . PHE A 1 71  ? 7.55978   -8.06200  33.86600  1.000 16.78501  ?  71  PHE A CD1 1 
ATOM   577  C  CD2 . PHE A 1 71  ? 9.19234   -9.65824  33.19022  1.000 15.32149  ?  71  PHE A CD2 1 
ATOM   578  C  CE1 . PHE A 1 71  ? 7.04639   -8.97262  34.77243  1.000 20.18012  ?  71  PHE A CE1 1 
ATOM   579  C  CE2 . PHE A 1 71  ? 8.67957   -10.57269 34.09494  1.000 14.20212  ?  71  PHE A CE2 1 
ATOM   580  C  CZ  . PHE A 1 71  ? 7.60971   -10.22592 34.87846  1.000 12.16273  ?  71  PHE A CZ  1 
ATOM   581  N  N   . ASN A 1 72  ? 9.57687   -6.30489  29.14646  1.000 12.98457  ?  72  ASN A N   1 
ATOM   582  C  CA  . ASN A 1 72  ? 10.37689  -5.43044  28.29625  1.000 9.97223   ?  72  ASN A CA  1 
ATOM   583  C  C   . ASN A 1 72  ? 9.90100   -5.59748  26.86165  1.000 8.65771   ?  72  ASN A C   1 
ATOM   584  O  O   . ASN A 1 72  ? 10.33210  -6.53112  26.17180  1.000 9.85817   ?  72  ASN A O   1 
ATOM   585  C  CB  . ASN A 1 72  ? 11.85469  -5.76040  28.41564  1.000 9.74663   ?  72  ASN A CB  1 
ATOM   586  C  CG  . ASN A 1 72  ? 12.73823  -4.73962  27.71835  1.000 14.51541  ?  72  ASN A CG  1 
ATOM   587  O  OD1 . ASN A 1 72  ? 12.33914  -4.10920  26.73930  1.000 10.75430  ?  72  ASN A OD1 1 
ATOM   588  N  ND2 . ASN A 1 72  ? 13.94230  -4.56667  28.23103  1.000 14.97582  ?  72  ASN A ND2 1 
ATOM   589  N  N   . PRO A 1 73  ? 9.05153   -4.69511  26.36713  1.000 13.69298  ?  73  PRO A N   1 
ATOM   590  C  CA  . PRO A 1 73  ? 8.49283   -4.86922  25.02358  1.000 14.35213  ?  73  PRO A CA  1 
ATOM   591  C  C   . PRO A 1 73  ? 9.50614   -4.67786  23.91221  1.000 18.57017  ?  73  PRO A C   1 
ATOM   592  O  O   . PRO A 1 73  ? 9.26982   -5.16741  22.80478  1.000 17.51733  ?  73  PRO A O   1 
ATOM   593  C  CB  . PRO A 1 73  ? 7.39217   -3.79498  24.96416  1.000 26.19159  ?  73  PRO A CB  1 
ATOM   594  C  CG  . PRO A 1 73  ? 7.84708   -2.74905  25.92951  1.000 23.61587  ?  73  PRO A CG  1 
ATOM   595  C  CD  . PRO A 1 73  ? 8.52241   -3.50264  27.04254  1.000 15.52602  ?  73  PRO A CD  1 
ATOM   596  N  N   . VAL A 1 74  ? 10.61534  -3.98035  24.16090  1.000 12.98723  ?  74  VAL A N   1 
ATOM   597  C  CA  . VAL A 1 74  ? 11.55711  -3.66079  23.09812  1.000 11.52129  ?  74  VAL A CA  1 
ATOM   598  C  C   . VAL A 1 74  ? 12.84045  -4.49766  23.14298  1.000 15.45681  ?  74  VAL A C   1 
ATOM   599  O  O   . VAL A 1 74  ? 13.53128  -4.61125  22.11573  1.000 13.47513  ?  74  VAL A O   1 
ATOM   600  C  CB  . VAL A 1 74  ? 11.88109  -2.14790  23.11042  1.000 11.89412  ?  74  VAL A CB  1 
ATOM   601  C  CG1 . VAL A 1 74  ? 10.63828  -1.33359  22.68560  1.000 13.37859  ?  74  VAL A CG1 1 
ATOM   602  C  CG2 . VAL A 1 74  ? 12.37584  -1.67939  24.47093  1.000 14.75742  ?  74  VAL A CG2 1 
ATOM   603  N  N   . GLY A 1 75  ? 13.16485  -5.10242  24.27627  1.000 12.37576  ?  75  GLY A N   1 
ATOM   604  C  CA  . GLY A 1 75  ? 14.38655  -5.87317  24.36222  1.000 10.99553  ?  75  GLY A CA  1 
ATOM   605  C  C   . GLY A 1 75  ? 14.19755  -7.21403  25.03316  1.000 9.60277   ?  75  GLY A C   1 
ATOM   606  O  O   . GLY A 1 75  ? 15.17241  -7.82645  25.48118  1.000 9.85579   ?  75  GLY A O   1 
ATOM   607  N  N   . GLY A 1 76  ? 12.94649  -7.67908  25.10279  1.000 7.59807   ?  76  GLY A N   1 
ATOM   608  C  CA  . GLY A 1 76  ? 12.62043  -8.94170  25.72575  1.000 9.04495   ?  76  GLY A CA  1 
ATOM   609  C  C   . GLY A 1 76  ? 12.45430  -10.06558 24.71388  1.000 9.80890   ?  76  GLY A C   1 
ATOM   610  O  O   . GLY A 1 76  ? 12.25454  -9.84083  23.51681  1.000 11.03016  ?  76  GLY A O   1 
ATOM   611  N  N   . GLY A 1 77  ? 12.55660  -11.29322 25.21383  1.000 11.09981  ?  77  GLY A N   1 
ATOM   612  C  CA  . GLY A 1 77  ? 12.31529  -12.46371 24.38220  1.000 13.06366  ?  77  GLY A CA  1 
ATOM   613  C  C   . GLY A 1 77  ? 13.44091  -12.83426 23.45249  1.000 14.02799  ?  77  GLY A C   1 
ATOM   614  O  O   . GLY A 1 77  ? 13.22961  -13.65478 22.55272  1.000 15.71689  ?  77  GLY A O   1 
ATOM   615  N  N   . ILE A 1 78  ? 14.63608  -12.27095 23.63733  1.000 8.98988   ?  78  ILE A N   1 
ATOM   616  C  CA  . ILE A 1 78  ? 15.77347  -12.55158 22.77043  1.000 9.76393   ?  78  ILE A CA  1 
ATOM   617  C  C   . ILE A 1 78  ? 17.04546  -12.68672 23.60860  1.000 14.33553  ?  78  ILE A C   1 
ATOM   618  O  O   . ILE A 1 78  ? 17.16066  -12.13031 24.70962  1.000 10.88043  ?  78  ILE A O   1 
ATOM   619  C  CB  . ILE A 1 78  ? 15.96790  -11.46159 21.69450  1.000 11.50638  ?  78  ILE A CB  1 
ATOM   620  C  CG1 . ILE A 1 78  ? 16.13718  -10.10225 22.35993  1.000 14.45397  ?  78  ILE A CG1 1 
ATOM   621  C  CG2 . ILE A 1 78  ? 14.77961  -11.42358 20.69331  1.000 13.55863  ?  78  ILE A CG2 1 
ATOM   622  C  CD1 . ILE A 1 78  ? 16.75466  -9.05922  21.44241  1.000 19.05112  ?  78  ILE A CD1 1 
ATOM   623  N  N   . ARG A 1 79  ? 18.00742  -13.42844 23.06324  1.000 11.35048  ?  79  ARG A N   1 
ATOM   624  C  CA  . ARG A 1 79  ? 19.34066  -13.53718 23.64383  1.000 11.20667  ?  79  ARG A CA  1 
ATOM   625  C  C   . ARG A 1 79  ? 20.12187  -12.26521 23.35281  1.000 13.64297  ?  79  ARG A C   1 
ATOM   626  O  O   . ARG A 1 79  ? 20.28654  -11.88652 22.18733  1.000 10.04595  ?  79  ARG A O   1 
ATOM   627  C  CB  . ARG A 1 79  ? 20.07338  -14.75009 23.07284  1.000 11.78676  ?  79  ARG A CB  1 
ATOM   628  C  CG  . ARG A 1 79  ? 19.43730  -16.07670 23.46044  1.000 15.61778  ?  79  ARG A CG  1 
ATOM   629  C  CD  . ARG A 1 79  ? 20.38125  -17.24857 23.16656  1.000 21.55718  ?  79  ARG A CD  1 
ATOM   630  N  NE  . ARG A 1 79  ? 20.02366  -18.41176 23.97177  1.000 23.49353  ?  79  ARG A NE  1 
ATOM   631  C  CZ  . ARG A 1 79  ? 20.39366  -18.58529 25.23396  1.000 32.30449  ?  79  ARG A CZ  1 
ATOM   632  N  NH1 . ARG A 1 79  ? 21.18512  -17.71429 25.85219  1.000 30.50342  ?  79  ARG A NH1 1 
ATOM   633  N  NH2 . ARG A 1 79  ? 19.95508  -19.65470 25.89790  1.000 41.01576  ?  79  ARG A NH2 1 
ATOM   634  N  N   . ARG A 1 80  ? 20.59597  -11.60123 24.40349  1.000 9.11232   ?  80  ARG A N   1 
ATOM   635  C  CA  . ARG A 1 80  ? 21.35156  -10.37214 24.25668  1.000 10.91332  ?  80  ARG A CA  1 
ATOM   636  C  C   . ARG A 1 80  ? 22.78183  -10.65621 24.70162  1.000 9.82431   ?  80  ARG A C   1 
ATOM   637  O  O   . ARG A 1 80  ? 23.04438  -10.87027 25.89305  1.000 12.68932  ?  80  ARG A O   1 
ATOM   638  C  CB  . ARG A 1 80  ? 20.67241  -9.23877  25.03443  1.000 5.70422   ?  80  ARG A CB  1 
ATOM   639  C  CG  . ARG A 1 80  ? 19.28238  -8.92691  24.42126  1.000 7.76923   ?  80  ARG A CG  1 
ATOM   640  C  CD  . ARG A 1 80  ? 18.36487  -8.06577  25.30385  1.000 10.18399  ?  80  ARG A CD  1 
ATOM   641  N  NE  . ARG A 1 80  ? 19.01027  -6.85691  25.81260  1.000 8.69940   ?  80  ARG A NE  1 
ATOM   642  C  CZ  . ARG A 1 80  ? 18.44436  -6.03500  26.68786  1.000 11.66241  ?  80  ARG A CZ  1 
ATOM   643  N  NH1 . ARG A 1 80  ? 17.19724  -6.21883  27.09544  1.000 8.13281   ?  80  ARG A NH1 1 
ATOM   644  N  NH2 . ARG A 1 80  ? 19.15158  -5.01604  27.18050  1.000 7.90566   ?  80  ARG A NH2 1 
ATOM   645  N  N   . VAL A 1 81  ? 23.68820  -10.69769 23.73099  1.000 6.98273   ?  81  VAL A N   1 
ATOM   646  C  CA  . VAL A 1 81  ? 25.07839  -11.09086 23.94529  1.000 14.95167  ?  81  VAL A CA  1 
ATOM   647  C  C   . VAL A 1 81  ? 25.86808  -9.85230  24.36063  1.000 17.33088  ?  81  VAL A C   1 
ATOM   648  O  O   . VAL A 1 81  ? 26.12874  -8.95314  23.55308  1.000 12.46545  ?  81  VAL A O   1 
ATOM   649  C  CB  . VAL A 1 81  ? 25.67079  -11.74538 22.68821  1.000 14.25812  ?  81  VAL A CB  1 
ATOM   650  C  CG1 . VAL A 1 81  ? 27.07874  -12.28225 22.96106  1.000 19.10788  ?  81  VAL A CG1 1 
ATOM   651  C  CG2 . VAL A 1 81  ? 24.75334  -12.86210 22.20575  1.000 11.04919  ?  81  VAL A CG2 1 
ATOM   652  N  N   . TYR A 1 82  ? 26.24212  -9.79672  25.63304  1.000 11.82249  ?  82  TYR A N   1 
ATOM   653  C  CA  . TYR A 1 82  ? 27.00535  -8.68544  26.17059  1.000 10.64606  ?  82  TYR A CA  1 
ATOM   654  C  C   . TYR A 1 82  ? 28.36015  -9.18579  26.65612  1.000 16.03153  ?  82  TYR A C   1 
ATOM   655  O  O   . TYR A 1 82  ? 28.59338  -10.38988 26.78886  1.000 14.29054  ?  82  TYR A O   1 
ATOM   656  C  CB  . TYR A 1 82  ? 26.24269  -8.01212  27.31683  1.000 7.67104   ?  82  TYR A CB  1 
ATOM   657  C  CG  . TYR A 1 82  ? 24.99062  -7.30917  26.83862  1.000 7.55346   ?  82  TYR A CG  1 
ATOM   658  C  CD1 . TYR A 1 82  ? 25.04442  -6.42476  25.77085  1.000 9.20011   ?  82  TYR A CD1 1 
ATOM   659  C  CD2 . TYR A 1 82  ? 23.76591  -7.53575  27.45041  1.000 8.44597   ?  82  TYR A CD2 1 
ATOM   660  C  CE1 . TYR A 1 82  ? 23.90425  -5.77139  25.32498  1.000 7.87988   ?  82  TYR A CE1 1 
ATOM   661  C  CE2 . TYR A 1 82  ? 22.63543  -6.90086  27.02490  1.000 8.59293   ?  82  TYR A CE2 1 
ATOM   662  C  CZ  . TYR A 1 82  ? 22.70976  -6.01744  25.95975  1.000 9.56757   ?  82  TYR A CZ  1 
ATOM   663  O  OH  . TYR A 1 82  ? 21.57765  -5.38148  25.51051  1.000 9.84938   ?  82  TYR A OH  1 
ATOM   664  N  N   . GLU A 1 83  ? 29.23322  -8.26504  26.90443  1.000 12.62663  ?  83  GLU A N   1 
ATOM   665  C  CA  . GLU A 1 83  ? 30.52451  -8.60698  27.47028  1.000 15.82735  ?  83  GLU A CA  1 
ATOM   666  C  C   . GLU A 1 83  ? 30.51388  -8.40842  28.98345  1.000 15.49136  ?  83  GLU A C   1 
ATOM   667  O  O   . GLU A 1 83  ? 29.77610  -7.56291  29.50700  1.000 10.34027  ?  83  GLU A O   1 
ATOM   668  C  CB  . GLU A 1 83  ? 31.62354  -7.75369  26.83505  1.000 13.75474  ?  83  GLU A CB  1 
ATOM   669  C  CG  . GLU A 1 83  ? 31.63210  -7.90605  25.31629  1.000 19.20772  ?  83  GLU A CG  1 
ATOM   670  C  CD  . GLU A 1 83  ? 32.73377  -7.13095  24.61912  1.000 27.03727  ?  83  GLU A CD  1 
ATOM   671  O  OE1 . GLU A 1 83  ? 33.62696  -6.56880  25.28814  1.000 27.28184  ?  83  GLU A OE1 1 
ATOM   672  O  OE2 . GLU A 1 83  ? 32.69435  -7.07656  23.37462  1.000 32.81053  -1 83  GLU A OE2 1 
ATOM   673  N  N   . PRO A 1 84  ? 31.30949  -9.17383  29.72310  1.000 11.49958  ?  84  PRO A N   1 
ATOM   674  C  CA  . PRO A 1 84  ? 31.26687  -9.07779  31.18567  1.000 10.27677  ?  84  PRO A CA  1 
ATOM   675  C  C   . PRO A 1 84  ? 31.75613  -7.72905  31.67909  1.000 9.28442   ?  84  PRO A C   1 
ATOM   676  O  O   . PRO A 1 84  ? 32.51874  -7.02444  31.02388  1.000 10.75543  ?  84  PRO A O   1 
ATOM   677  C  CB  . PRO A 1 84  ? 32.20386  -10.20058 31.65537  1.000 12.92711  ?  84  PRO A CB  1 
ATOM   678  C  CG  . PRO A 1 84  ? 33.08245  -10.47031 30.49942  1.000 19.43910  ?  84  PRO A CG  1 
ATOM   679  C  CD  . PRO A 1 84  ? 32.28106  -10.17970 29.26106  1.000 12.49628  ?  84  PRO A CD  1 
ATOM   680  N  N   . ILE A 1 85  ? 31.29007  -7.37555  32.86789  1.000 7.87820   ?  85  ILE A N   1 
ATOM   681  C  CA  . ILE A 1 85  ? 31.79240  -6.19195  33.54416  1.000 8.57382   ?  85  ILE A CA  1 
ATOM   682  C  C   . ILE A 1 85  ? 33.22758  -6.44739  33.99047  1.000 11.20579  ?  85  ILE A C   1 
ATOM   683  O  O   . ILE A 1 85  ? 33.56150  -7.53336  34.48155  1.000 12.39828  ?  85  ILE A O   1 
ATOM   684  C  CB  . ILE A 1 85  ? 30.87394  -5.85303  34.72814  1.000 6.96825   ?  85  ILE A CB  1 
ATOM   685  C  CG1 . ILE A 1 85  ? 29.48971  -5.41109  34.20743  1.000 7.22604   ?  85  ILE A CG1 1 
ATOM   686  C  CG2 . ILE A 1 85  ? 31.50935  -4.82453  35.63949  1.000 8.65258   ?  85  ILE A CG2 1 
ATOM   687  C  CD1 . ILE A 1 85  ? 28.45161  -5.28291  35.29976  1.000 7.80055   ?  85  ILE A CD1 1 
ATOM   688  N  N   . GLU A 1 86  ? 34.09307  -5.45752  33.80250  1.000 13.30356  ?  86  GLU A N   1 
ATOM   689  C  CA  . GLU A 1 86  ? 35.49134  -5.64171  34.18696  1.000 15.78073  ?  86  GLU A CA  1 
ATOM   690  C  C   . GLU A 1 86  ? 35.71813  -5.31549  35.65496  1.000 15.44324  ?  86  GLU A C   1 
ATOM   691  O  O   . GLU A 1 86  ? 36.48405  -6.00064  36.33614  1.000 16.86250  ?  86  GLU A O   1 
ATOM   692  C  CB  . GLU A 1 86  ? 36.39602  -4.77288  33.31775  1.000 15.41956  ?  86  GLU A CB  1 
ATOM   693  C  CG  . GLU A 1 86  ? 36.22431  -5.03589  31.83524  1.000 21.79571  ?  86  GLU A CG  1 
ATOM   694  C  CD  . GLU A 1 86  ? 37.08242  -4.13048  30.96314  1.000 30.88356  ?  86  GLU A CD  1 
ATOM   695  O  OE1 . GLU A 1 86  ? 36.84032  -2.89983  30.91271  1.000 22.53662  ?  86  GLU A OE1 1 
ATOM   696  O  OE2 . GLU A 1 86  ? 38.00599  -4.66130  30.31205  1.000 37.01365  -1 86  GLU A OE2 1 
ATOM   697  N  N   . VAL A 1 87  ? 35.06788  -4.27379  36.15770  1.000 9.44283   ?  87  VAL A N   1 
ATOM   698  C  CA  . VAL A 1 87  ? 35.32318  -3.79548  37.51164  1.000 10.79769  ?  87  VAL A CA  1 
ATOM   699  C  C   . VAL A 1 87  ? 34.42630  -4.50269  38.51778  1.000 14.93288  ?  87  VAL A C   1 
ATOM   700  O  O   . VAL A 1 87  ? 33.62425  -5.36780  38.15087  1.000 11.35206  ?  87  VAL A O   1 
ATOM   701  C  CB  . VAL A 1 87  ? 35.14574  -2.26785  37.57550  1.000 12.86157  ?  87  VAL A CB  1 
ATOM   702  C  CG1 . VAL A 1 87  ? 36.12862  -1.61344  36.61157  1.000 10.99433  ?  87  VAL A CG1 1 
ATOM   703  C  CG2 . VAL A 1 87  ? 33.71918  -1.87624  37.19939  1.000 12.55752  ?  87  VAL A CG2 1 
ATOM   704  N  N   . ASP A 1 88  ? 34.55071  -4.12150  39.79234  1.000 9.78686   ?  88  ASP A N   1 
ATOM   705  C  CA  . ASP A 1 88  ? 33.88058  -4.77791  40.91047  1.000 14.53483  ?  88  ASP A CA  1 
ATOM   706  C  C   . ASP A 1 88  ? 32.87579  -3.80723  41.52828  1.000 10.37546  ?  88  ASP A C   1 
ATOM   707  O  O   . ASP A 1 88  ? 33.25543  -2.91750  42.29364  1.000 9.92057   ?  88  ASP A O   1 
ATOM   708  C  CB  . ASP A 1 88  ? 34.91458  -5.22704  41.93547  1.000 12.83393  ?  88  ASP A CB  1 
ATOM   709  C  CG  . ASP A 1 88  ? 34.29171  -5.82781  43.17529  1.000 20.55123  ?  88  ASP A CG  1 
ATOM   710  O  OD1 . ASP A 1 88  ? 33.08739  -6.18275  43.16651  1.000 13.80078  ?  88  ASP A OD1 1 
ATOM   711  O  OD2 . ASP A 1 88  ? 35.03168  -5.94385  44.17112  1.000 16.01277  -1 88  ASP A OD2 1 
ATOM   712  N  N   . PHE A 1 89  ? 31.60038  -3.96151  41.18885  1.000 12.95224  ?  89  PHE A N   1 
ATOM   713  C  CA  . PHE A 1 89  ? 30.56025  -3.10662  41.75602  1.000 14.93224  ?  89  PHE A CA  1 
ATOM   714  C  C   . PHE A 1 89  ? 30.07253  -3.59098  43.11665  1.000 13.73001  ?  89  PHE A C   1 
ATOM   715  O  O   . PHE A 1 89  ? 29.19446  -2.94684  43.70398  1.000 11.04103  ?  89  PHE A O   1 
ATOM   716  C  CB  . PHE A 1 89  ? 29.35490  -3.00831  40.78940  1.000 6.76027   ?  89  PHE A CB  1 
ATOM   717  C  CG  . PHE A 1 89  ? 29.58934  -2.08742  39.62444  1.000 3.30917   ?  89  PHE A CG  1 
ATOM   718  C  CD1 . PHE A 1 89  ? 29.54993  -0.71170  39.80465  1.000 8.30518   ?  89  PHE A CD1 1 
ATOM   719  C  CD2 . PHE A 1 89  ? 29.84970  -2.58407  38.35947  1.000 9.99527   ?  89  PHE A CD2 1 
ATOM   720  C  CE1 . PHE A 1 89  ? 29.76770  0.16083   38.73708  1.000 11.06652  ?  89  PHE A CE1 1 
ATOM   721  C  CE2 . PHE A 1 89  ? 30.06678  -1.71109  37.28097  1.000 10.77947  ?  89  PHE A CE2 1 
ATOM   722  C  CZ  . PHE A 1 89  ? 30.03242  -0.34209  37.48498  1.000 7.56482   ?  89  PHE A CZ  1 
ATOM   723  N  N   . THR A 1 90  ? 30.58527  -4.71839  43.62171  1.000 13.21489  ?  90  THR A N   1 
ATOM   724  C  CA  . THR A 1 90  ? 29.97531  -5.31942  44.80370  1.000 9.97312   ?  90  THR A CA  1 
ATOM   725  C  C   . THR A 1 90  ? 30.02852  -4.44831  46.06413  1.000 13.60460  ?  90  THR A C   1 
ATOM   726  O  O   . THR A 1 90  ? 29.06819  -4.51055  46.84906  1.000 13.42957  ?  90  THR A O   1 
ATOM   727  C  CB  . THR A 1 90  ? 30.57624  -6.71951  45.07112  1.000 14.93665  ?  90  THR A CB  1 
ATOM   728  O  OG1 . THR A 1 90  ? 31.98193  -6.65226  45.33395  1.000 16.46914  ?  90  THR A OG1 1 
ATOM   729  C  CG2 . THR A 1 90  ? 30.34379  -7.61853  43.87200  1.000 15.16316  ?  90  THR A CG2 1 
ATOM   730  N  N   . PRO A 1 91  ? 31.04990  -3.62270  46.31672  1.000 14.95617  ?  91  PRO A N   1 
ATOM   731  C  CA  . PRO A 1 91  ? 30.93608  -2.73396  47.48961  1.000 13.42041  ?  91  PRO A CA  1 
ATOM   732  C  C   . PRO A 1 91  ? 29.79917  -1.73938  47.36398  1.000 13.42583  ?  91  PRO A C   1 
ATOM   733  O  O   . PRO A 1 91  ? 29.10998  -1.42907  48.34505  1.000 11.23453  ?  91  PRO A O   1 
ATOM   734  C  CB  . PRO A 1 91  ? 32.30549  -2.04513  47.56468  1.000 25.55033  ?  91  PRO A CB  1 
ATOM   735  C  CG  . PRO A 1 91  ? 33.01255  -2.35872  46.32529  1.000 26.96721  ?  91  PRO A CG  1 
ATOM   736  C  CD  . PRO A 1 91  ? 32.39512  -3.57890  45.71241  1.000 15.92034  ?  91  PRO A CD  1 
ATOM   737  N  N   . LEU A 1 92  ? 29.54143  -1.25919  46.15826  1.000 14.28529  ?  92  LEU A N   1 
ATOM   738  C  CA  . LEU A 1 92  ? 28.41969  -0.35512  45.99470  1.000 16.29135  ?  92  LEU A CA  1 
ATOM   739  C  C   . LEU A 1 92  ? 27.10194  -1.11452  46.11979  1.000 10.88183  ?  92  LEU A C   1 
ATOM   740  O  O   . LEU A 1 92  ? 26.14183  -0.61702  46.72136  1.000 14.21869  ?  92  LEU A O   1 
ATOM   741  C  CB  . LEU A 1 92  ? 28.56963  0.35605   44.65053  1.000 21.39075  ?  92  LEU A CB  1 
ATOM   742  C  CG  . LEU A 1 92  ? 27.51439  1.23084   44.00431  1.000 23.08539  ?  92  LEU A CG  1 
ATOM   743  C  CD1 . LEU A 1 92  ? 28.21278  2.04536   42.92851  1.000 16.40532  ?  92  LEU A CD1 1 
ATOM   744  C  CD2 . LEU A 1 92  ? 26.41545  0.37634   43.38659  1.000 21.47802  ?  92  LEU A CD2 1 
ATOM   745  N  N   . ILE A 1 93  ? 27.04184  -2.32614  45.56623  1.000 9.24189   ?  93  ILE A N   1 
ATOM   746  C  CA  . ILE A 1 93  ? 25.84399  -3.14956  45.70455  1.000 10.99816  ?  93  ILE A CA  1 
ATOM   747  C  C   . ILE A 1 93  ? 25.56305  -3.44538  47.17473  1.000 15.61364  ?  93  ILE A C   1 
ATOM   748  O  O   . ILE A 1 93  ? 24.40783  -3.44811  47.61164  1.000 13.13043  ?  93  ILE A O   1 
ATOM   749  C  CB  . ILE A 1 93  ? 25.98531  -4.44562  44.88058  1.000 8.00431   ?  93  ILE A CB  1 
ATOM   750  C  CG1 . ILE A 1 93  ? 26.08157  -4.10838  43.38764  1.000 8.26170   ?  93  ILE A CG1 1 
ATOM   751  C  CG2 . ILE A 1 93  ? 24.80113  -5.39795  45.17233  1.000 9.06290   ?  93  ILE A CG2 1 
ATOM   752  C  CD1 . ILE A 1 93  ? 26.54021  -5.28671  42.51333  1.000 11.82224  ?  93  ILE A CD1 1 
ATOM   753  N  N   . SER A 1 94  ? 26.61637  -3.68509  47.96384  1.000 11.37469  ?  94  SER A N   1 
ATOM   754  C  CA  . SER A 1 94  ? 26.44074  -3.96231  49.38823  1.000 14.04105  ?  94  SER A CA  1 
ATOM   755  C  C   . SER A 1 94  ? 25.69052  -2.84601  50.09339  1.000 13.00031  ?  94  SER A C   1 
ATOM   756  O  O   . SER A 1 94  ? 24.92628  -3.09770  51.02907  1.000 12.49478  ?  94  SER A O   1 
ATOM   757  C  CB  . SER A 1 94  ? 27.80165  -4.16089  50.05569  1.000 14.58564  ?  94  SER A CB  1 
ATOM   758  O  OG  . SER A 1 94  ? 28.31740  -5.41104  49.67802  1.000 21.90781  ?  94  SER A OG  1 
ATOM   759  N  N   . GLU A 1 95  ? 25.93428  -1.60210  49.69001  1.000 10.23007  ?  95  GLU A N   1 
ATOM   760  C  CA  . GLU A 1 95  ? 25.21001  -0.48290  50.27509  1.000 14.07099  ?  95  GLU A CA  1 
ATOM   761  C  C   . GLU A 1 95  ? 23.71949  -0.60410  49.99998  1.000 16.98543  ?  95  GLU A C   1 
ATOM   762  O  O   . GLU A 1 95  ? 22.89243  -0.28545  50.86267  1.000 14.06481  ?  95  GLU A O   1 
ATOM   763  C  CB  . GLU A 1 95  ? 25.75881  0.82821   49.72430  1.000 18.23184  ?  95  GLU A CB  1 
ATOM   764  C  CG  . GLU A 1 95  ? 25.65773  1.99070   50.69226  1.000 28.39375  ?  95  GLU A CG  1 
ATOM   765  C  CD  . GLU A 1 95  ? 26.60575  1.87814   51.87767  1.000 29.57785  ?  95  GLU A CD  1 
ATOM   766  O  OE1 . GLU A 1 95  ? 27.73935  1.36463   51.71842  1.000 33.87264  ?  95  GLU A OE1 1 
ATOM   767  O  OE2 . GLU A 1 95  ? 26.20120  2.30391   52.98018  1.000 37.34283  -1 95  GLU A OE2 1 
ATOM   768  N  N   . GLY A 1 96  ? 23.36075  -1.08915  48.80727  1.000 18.88123  ?  96  GLY A N   1 
ATOM   769  C  CA  . GLY A 1 96  ? 21.96392  -1.37128  48.52071  1.000 16.14873  ?  96  GLY A CA  1 
ATOM   770  C  C   . GLY A 1 96  ? 21.40384  -2.50683  49.35684  1.000 17.18977  ?  96  GLY A C   1 
ATOM   771  O  O   . GLY A 1 96  ? 20.27810  -2.41946  49.85915  1.000 17.97745  ?  96  GLY A O   1 
ATOM   772  N  N   . ILE A 1 97  ? 22.16487  -3.59672  49.50727  1.000 15.30236  ?  97  ILE A N   1 
ATOM   773  C  CA  . ILE A 1 97  ? 21.69961  -4.71870  50.32919  1.000 13.50868  ?  97  ILE A CA  1 
ATOM   774  C  C   . ILE A 1 97  ? 21.38848  -4.25400  51.74590  1.000 11.89079  ?  97  ILE A C   1 
ATOM   775  O  O   . ILE A 1 97  ? 20.34456  -4.59854  52.32108  1.000 11.58462  ?  97  ILE A O   1 
ATOM   776  C  CB  . ILE A 1 97  ? 22.74606  -5.84745  50.35058  1.000 19.20631  ?  97  ILE A CB  1 
ATOM   777  C  CG1 . ILE A 1 97  ? 22.94165  -6.44444  48.96978  1.000 11.78587  ?  97  ILE A CG1 1 
ATOM   778  C  CG2 . ILE A 1 97  ? 22.33887  -6.93272  51.34540  1.000 15.47483  ?  97  ILE A CG2 1 
ATOM   779  C  CD1 . ILE A 1 97  ? 24.14178  -7.35356  48.92439  1.000 15.37635  ?  97  ILE A CD1 1 
ATOM   780  N  N   . ARG A 1 98  ? 22.30158  -3.47999  52.32717  1.000 12.79597  ?  98  ARG A N   1 
ATOM   781  C  CA  . ARG A 1 98  ? 22.14875  -2.95921  53.68453  1.000 21.44475  ?  98  ARG A CA  1 
ATOM   782  C  C   . ARG A 1 98  ? 20.86365  -2.14499  53.82425  1.000 18.06866  ?  98  ARG A C   1 
ATOM   783  O  O   . ARG A 1 98  ? 20.10629  -2.31096  54.78638  1.000 13.35342  ?  98  ARG A O   1 
ATOM   784  C  CB  . ARG A 1 98  ? 23.39292  -2.11876  54.01182  1.000 20.90977  ?  98  ARG A CB  1 
ATOM   785  C  CG  . ARG A 1 98  ? 23.70388  -1.81153  55.47078  1.000 31.04405  ?  98  ARG A CG  1 
ATOM   786  C  CD  . ARG A 1 98  ? 25.23813  -1.56871  55.69612  1.000 42.69020  ?  98  ARG A CD  1 
ATOM   787  N  NE  . ARG A 1 98  ? 25.97086  -1.16896  54.49248  1.000 43.23598  ?  98  ARG A NE  1 
ATOM   788  C  CZ  . ARG A 1 98  ? 27.02390  -1.80980  53.99134  1.000 37.34258  ?  98  ARG A CZ  1 
ATOM   789  N  NH1 . ARG A 1 98  ? 27.54075  -2.87067  54.58910  1.000 35.78326  ?  98  ARG A NH1 1 
ATOM   790  N  NH2 . ARG A 1 98  ? 27.57293  -1.37400  52.85872  1.000 36.35533  ?  98  ARG A NH2 1 
ATOM   791  N  N   . GLU A 1 99  ? 20.58503  -1.27885  52.85716  1.000 17.61250  ?  99  GLU A N   1 
ATOM   792  C  CA  . GLU A 1 99  ? 19.42076  -0.41371  52.97886  1.000 16.81594  ?  99  GLU A CA  1 
ATOM   793  C  C   . GLU A 1 99  ? 18.12773  -1.16630  52.68451  1.000 18.15044  ?  99  GLU A C   1 
ATOM   794  O  O   . GLU A 1 99  ? 17.08244  -0.82723  53.24694  1.000 17.12273  ?  99  GLU A O   1 
ATOM   795  C  CB  . GLU A 1 99  ? 19.59666  0.80360   52.06251  1.000 20.03269  ?  99  GLU A CB  1 
ATOM   796  C  CG  . GLU A 1 99  ? 18.58108  1.91598   52.25608  1.000 20.32342  ?  99  GLU A CG  1 
ATOM   797  C  CD  . GLU A 1 99  ? 18.65975  2.57880   53.60968  1.000 29.03756  ?  99  GLU A CD  1 
ATOM   798  O  OE1 . GLU A 1 99  ? 19.77221  2.65670   54.17738  1.000 36.71241  ?  99  GLU A OE1 1 
ATOM   799  O  OE2 . GLU A 1 99  ? 17.59607  3.00726   54.10720  1.000 28.41658  -1 99  GLU A OE2 1 
ATOM   800  N  N   . LEU A 1 100 ? 18.17648  -2.19340  51.82363  1.000 9.99892   ?  100 LEU A N   1 
ATOM   801  C  CA  . LEU A 1 100 ? 17.00630  -3.04338  51.60761  1.000 13.23255  ?  100 LEU A CA  1 
ATOM   802  C  C   . LEU A 1 100 ? 16.71005  -3.93063  52.81432  1.000 17.26405  ?  100 LEU A C   1 
ATOM   803  O  O   . LEU A 1 100 ? 15.56034  -4.33226  53.01450  1.000 18.25197  ?  100 LEU A O   1 
ATOM   804  C  CB  . LEU A 1 100 ? 17.21246  -3.92751  50.38141  1.000 9.52212   ?  100 LEU A CB  1 
ATOM   805  C  CG  . LEU A 1 100 ? 17.21116  -3.26368  49.00707  1.000 16.52100  ?  100 LEU A CG  1 
ATOM   806  C  CD1 . LEU A 1 100 ? 17.68973  -4.28796  47.97358  1.000 14.22261  ?  100 LEU A CD1 1 
ATOM   807  C  CD2 . LEU A 1 100 ? 15.82009  -2.73520  48.68171  1.000 12.28757  ?  100 LEU A CD2 1 
ATOM   808  N  N   . GLY A 1 101 ? 17.72845  -4.26997  53.60618  1.000 15.96301  ?  101 GLY A N   1 
ATOM   809  C  CA  . GLY A 1 101 ? 17.55638  -5.28864  54.62342  1.000 16.05426  ?  101 GLY A CA  1 
ATOM   810  C  C   . GLY A 1 101 ? 17.17850  -6.59618  53.96562  1.000 18.61271  ?  101 GLY A C   1 
ATOM   811  O  O   . GLY A 1 101 ? 16.16615  -7.21669  54.30878  1.000 17.39639  ?  101 GLY A O   1 
ATOM   812  N  N   . LEU A 1 102 ? 17.97628  -7.00109  52.98063  1.000 15.81755  ?  102 LEU A N   1 
ATOM   813  C  CA  . LEU A 1 102 ? 17.66056  -8.17512  52.18022  1.000 14.10373  ?  102 LEU A CA  1 
ATOM   814  C  C   . LEU A 1 102 ? 17.44735  -9.40755  53.06164  1.000 17.41016  ?  102 LEU A C   1 
ATOM   815  O  O   . LEU A 1 102 ? 18.22030  -9.67601  53.98505  1.000 16.98966  ?  102 LEU A O   1 
ATOM   816  C  CB  . LEU A 1 102 ? 18.79588  -8.41966  51.18951  1.000 22.99746  ?  102 LEU A CB  1 
ATOM   817  C  CG  . LEU A 1 102 ? 18.48063  -9.08839  49.86133  1.000 13.02353  ?  102 LEU A CG  1 
ATOM   818  C  CD1 . LEU A 1 102 ? 17.39256  -8.32805  49.11786  1.000 16.47259  ?  102 LEU A CD1 1 
ATOM   819  C  CD2 . LEU A 1 102 ? 19.75520  -9.13941  49.03936  1.000 13.22362  ?  102 LEU A CD2 1 
ATOM   820  N  N   . ASP A 1 103 ? 16.37158  -10.13810 52.76928  1.000 16.98440  ?  103 ASP A N   1 
ATOM   821  C  CA  . ASP A 1 103 ? 15.96597  -11.31614 53.53465  1.000 19.42296  ?  103 ASP A CA  1 
ATOM   822  C  C   . ASP A 1 103 ? 17.07738  -12.36302 53.55649  1.000 17.63068  ?  103 ASP A C   1 
ATOM   823  O  O   . ASP A 1 103 ? 17.49557  -12.86625 52.50602  1.000 15.98060  ?  103 ASP A O   1 
ATOM   824  C  CB  . ASP A 1 103 ? 14.69361  -11.88534 52.90236  1.000 16.87319  ?  103 ASP A CB  1 
ATOM   825  C  CG  . ASP A 1 103 ? 14.14622  -13.12029 53.62071  1.000 14.55934  ?  103 ASP A CG  1 
ATOM   826  O  OD1 . ASP A 1 103 ? 14.69815  -13.55844 54.66016  1.000 16.97604  ?  103 ASP A OD1 1 
ATOM   827  O  OD2 . ASP A 1 103 ? 13.13231  -13.65465 53.11707  1.000 20.50431  -1 103 ASP A OD2 1 
ATOM   828  N  N   . ARG A 1 104 ? 17.54436  -12.70337 54.75376  1.000 20.35183  ?  104 ARG A N   1 
ATOM   829  C  CA  . ARG A 1 104 ? 18.64636  -13.64791 54.89762  1.000 18.17916  ?  104 ARG A CA  1 
ATOM   830  C  C   . ARG A 1 104 ? 18.20257  -15.10441 54.86933  1.000 16.52825  ?  104 ARG A C   1 
ATOM   831  O  O   . ARG A 1 104 ? 19.05886  -15.99547 54.92540  1.000 17.01686  ?  104 ARG A O   1 
ATOM   832  C  CB  . ARG A 1 104 ? 19.39836  -13.35873 56.19553  1.000 21.09202  ?  104 ARG A CB  1 
ATOM   833  C  CG  . ARG A 1 104 ? 20.14730  -12.04230 56.16165  1.000 16.68367  ?  104 ARG A CG  1 
ATOM   834  C  CD  . ARG A 1 104 ? 20.96521  -11.81140 57.42446  1.000 23.26953  ?  104 ARG A CD  1 
ATOM   835  N  NE  . ARG A 1 104 ? 21.97483  -12.83983 57.64047  1.000 20.18907  ?  104 ARG A NE  1 
ATOM   836  C  CZ  . ARG A 1 104 ? 23.19666  -12.82022 57.12664  1.000 18.47319  ?  104 ARG A CZ  1 
ATOM   837  N  NH1 . ARG A 1 104 ? 23.58820  -11.85926 56.30700  1.000 22.78343  ?  104 ARG A NH1 1 
ATOM   838  N  NH2 . ARG A 1 104 ? 24.04686  -13.79232 57.44074  1.000 19.67233  ?  104 ARG A NH2 1 
ATOM   839  N  N   . SER A 1 105 ? 16.90249  -15.37445 54.76622  1.000 15.73497  ?  105 SER A N   1 
ATOM   840  C  CA  . SER A 1 105 ? 16.42131  -16.73811 54.92803  1.000 17.18174  ?  105 SER A CA  1 
ATOM   841  C  C   . SER A 1 105 ? 16.65001  -17.59191 53.68853  1.000 21.54443  ?  105 SER A C   1 
ATOM   842  O  O   . SER A 1 105 ? 16.43207  -18.80942 53.74240  1.000 15.55546  ?  105 SER A O   1 
ATOM   843  C  CB  . SER A 1 105 ? 14.93619  -16.73806 55.30492  1.000 17.31190  ?  105 SER A CB  1 
ATOM   844  O  OG  . SER A 1 105 ? 14.08560  -16.64007 54.16477  1.000 20.58798  ?  105 SER A OG  1 
ATOM   845  N  N   . GLU A 1 106 ? 17.09246  -16.99787 52.58374  1.000 16.57591  ?  106 GLU A N   1 
ATOM   846  C  CA  . GLU A 1 106 ? 17.45479  -17.75617 51.40258  1.000 11.19794  ?  106 GLU A CA  1 
ATOM   847  C  C   . GLU A 1 106 ? 18.42373  -16.93669 50.57958  1.000 11.54965  ?  106 GLU A C   1 
ATOM   848  O  O   . GLU A 1 106 ? 18.55517  -15.71138 50.78848  1.000 10.70176  ?  106 GLU A O   1 
ATOM   849  C  CB  . GLU A 1 106 ? 16.21729  -18.15037 50.58784  1.000 12.46398  ?  106 GLU A CB  1 
ATOM   850  C  CG  . GLU A 1 106 ? 15.50752  -16.96479 49.93848  1.000 10.68470  ?  106 GLU A CG  1 
ATOM   851  C  CD  . GLU A 1 106 ? 14.19478  -17.40199 49.33776  1.000 12.79072  ?  106 GLU A CD  1 
ATOM   852  O  OE1 . GLU A 1 106 ? 14.20974  -18.16819 48.35393  1.000 12.51436  ?  106 GLU A OE1 1 
ATOM   853  O  OE2 . GLU A 1 106 ? 13.14992  -17.00850 49.87968  1.000 19.15030  -1 106 GLU A OE2 1 
ATOM   854  N  N   . PRO A 1 107 ? 19.18160  -17.55912 49.68399  1.000 11.45913  ?  107 PRO A N   1 
ATOM   855  C  CA  . PRO A 1 107 ? 20.15457  -16.83938 48.87315  1.000 9.47909   ?  107 PRO A CA  1 
ATOM   856  C  C   . PRO A 1 107 ? 19.46495  -16.11206 47.72633  1.000 10.43733  ?  107 PRO A C   1 
ATOM   857  O  O   . PRO A 1 107 ? 18.29653  -16.34993 47.42004  1.000 13.46575  ?  107 PRO A O   1 
ATOM   858  C  CB  . PRO A 1 107 ? 21.09510  -17.93336 48.36180  1.000 14.42277  ?  107 PRO A CB  1 
ATOM   859  C  CG  . PRO A 1 107 ? 20.27735  -19.18073 48.38977  1.000 16.13102  ?  107 PRO A CG  1 
ATOM   860  C  CD  . PRO A 1 107 ? 19.33980  -19.02698 49.57769  1.000 9.83460   ?  107 PRO A CD  1 
ATOM   861  N  N   . TRP A 1 108 ? 20.21958  -15.20497 47.10026  1.000 12.07539  ?  108 TRP A N   1 
ATOM   862  C  CA  . TRP A 1 108 ? 19.70266  -14.33165 46.05943  1.000 10.89806  ?  108 TRP A CA  1 
ATOM   863  C  C   . TRP A 1 108 ? 20.57135  -14.45284 44.81292  1.000 11.11350  ?  108 TRP A C   1 
ATOM   864  O  O   . TRP A 1 108 ? 21.65355  -15.04407 44.83496  1.000 10.54966  ?  108 TRP A O   1 
ATOM   865  C  CB  . TRP A 1 108 ? 19.64215  -12.87728 46.56311  1.000 11.31628  ?  108 TRP A CB  1 
ATOM   866  C  CG  . TRP A 1 108 ? 18.60266  -12.68440 47.63729  1.000 12.81229  ?  108 TRP A CG  1 
ATOM   867  C  CD1 . TRP A 1 108 ? 18.66402  -13.11030 48.94542  1.000 10.21091  ?  108 TRP A CD1 1 
ATOM   868  C  CD2 . TRP A 1 108 ? 17.35437  -12.00577 47.49596  1.000 10.71387  ?  108 TRP A CD2 1 
ATOM   869  N  NE1 . TRP A 1 108 ? 17.51350  -12.74743 49.61133  1.000 12.49481  ?  108 TRP A NE1 1 
ATOM   870  C  CE2 . TRP A 1 108 ? 16.69786  -12.06240 48.74605  1.000 11.62251  ?  108 TRP A CE2 1 
ATOM   871  C  CE3 . TRP A 1 108 ? 16.73107  -11.34211 46.43253  1.000 11.98066  ?  108 TRP A CE3 1 
ATOM   872  C  CZ2 . TRP A 1 108 ? 15.44901  -11.49156 48.95816  1.000 11.39050  ?  108 TRP A CZ2 1 
ATOM   873  C  CZ3 . TRP A 1 108 ? 15.48177  -10.77215 46.64499  1.000 13.32408  ?  108 TRP A CZ3 1 
ATOM   874  C  CH2 . TRP A 1 108 ? 14.85522  -10.85456 47.90048  1.000 11.72800  ?  108 TRP A CH2 1 
ATOM   875  N  N   . GLN A 1 109 ? 20.07571  -13.88976 43.71453  1.000 7.98226   ?  109 GLN A N   1 
ATOM   876  C  CA  . GLN A 1 109 ? 20.79044  -13.79372 42.44763  1.000 5.07265   ?  109 GLN A CA  1 
ATOM   877  C  C   . GLN A 1 109 ? 20.57987  -12.37630 41.90875  1.000 9.03555   ?  109 GLN A C   1 
ATOM   878  O  O   . GLN A 1 109 ? 19.46231  -11.85076 41.96418  1.000 8.51662   ?  109 GLN A O   1 
ATOM   879  C  CB  . GLN A 1 109 ? 20.26613  -14.85057 41.45372  1.000 7.97295   ?  109 GLN A CB  1 
ATOM   880  C  CG  . GLN A 1 109 ? 20.93917  -14.86828 40.10110  1.000 10.37190  ?  109 GLN A CG  1 
ATOM   881  C  CD  . GLN A 1 109 ? 20.26805  -13.93441 39.12267  1.000 9.80189   ?  109 GLN A CD  1 
ATOM   882  O  OE1 . GLN A 1 109 ? 19.03977  -13.84218 39.07999  1.000 9.35951   ?  109 GLN A OE1 1 
ATOM   883  N  NE2 . GLN A 1 109 ? 21.07420  -13.21754 38.34965  1.000 8.12630   ?  109 GLN A NE2 1 
ATOM   884  N  N   . ILE A 1 110 ? 21.64171  -11.73693 41.42311  1.000 6.65541   ?  110 ILE A N   1 
ATOM   885  C  CA  . ILE A 1 110 ? 21.51299  -10.38437 40.88345  1.000 8.46368   ?  110 ILE A CA  1 
ATOM   886  C  C   . ILE A 1 110 ? 22.00188  -10.34088 39.44536  1.000 7.70688   ?  110 ILE A C   1 
ATOM   887  O  O   . ILE A 1 110 ? 23.01985  -10.95584 39.09441  1.000 8.11395   ?  110 ILE A O   1 
ATOM   888  C  CB  . ILE A 1 110 ? 22.26395  -9.33414  41.72517  1.000 8.72479   ?  110 ILE A CB  1 
ATOM   889  C  CG1 . ILE A 1 110 ? 23.73686  -9.71118  41.87101  1.000 8.78551   ?  110 ILE A CG1 1 
ATOM   890  C  CG2 . ILE A 1 110 ? 21.61792  -9.16891  43.09288  1.000 8.89561   ?  110 ILE A CG2 1 
ATOM   891  C  CD1 . ILE A 1 110 ? 24.55342  -8.66877  42.61600  1.000 10.24618  ?  110 ILE A CD1 1 
ATOM   892  N  N   . ASN A 1 111 ? 21.27794  -9.57157  38.62554  1.000 8.39057   ?  111 ASN A N   1 
ATOM   893  C  CA  . ASN A 1 111 ? 21.73920  -9.09258  37.33089  1.000 5.95596   ?  111 ASN A CA  1 
ATOM   894  C  C   . ASN A 1 111 ? 22.36563  -7.71480  37.52399  1.000 5.21306   ?  111 ASN A C   1 
ATOM   895  O  O   . ASN A 1 111 ? 21.78714  -6.85804  38.19383  1.000 4.83046   ?  111 ASN A O   1 
ATOM   896  C  CB  . ASN A 1 111 ? 20.57729  -8.99313  36.33071  1.000 6.34923   ?  111 ASN A CB  1 
ATOM   897  C  CG  . ASN A 1 111 ? 20.07797  -10.35341 35.85836  1.000 11.49195  ?  111 ASN A CG  1 
ATOM   898  O  OD1 . ASN A 1 111 ? 20.67984  -11.39204 36.16224  1.000 9.86428   ?  111 ASN A OD1 1 
ATOM   899  N  ND2 . ASN A 1 111 ? 18.98345  -10.34892 35.09782  1.000 10.00827  ?  111 ASN A ND2 1 
ATOM   900  N  N   . VAL A 1 112 ? 23.53665  -7.49720  36.93528  1.000 6.72678   ?  112 VAL A N   1 
ATOM   901  C  CA  . VAL A 1 112 ? 24.25093  -6.22847  37.04999  1.000 5.97845   ?  112 VAL A CA  1 
ATOM   902  C  C   . VAL A 1 112 ? 24.46014  -5.67039  35.65572  1.000 6.65028   ?  112 VAL A C   1 
ATOM   903  O  O   . VAL A 1 112 ? 25.16444  -6.28069  34.84729  1.000 4.95233   ?  112 VAL A O   1 
ATOM   904  C  CB  . VAL A 1 112 ? 25.60138  -6.39327  37.77157  1.000 7.40659   ?  112 VAL A CB  1 
ATOM   905  C  CG1 . VAL A 1 112 ? 26.23388  -5.00450  38.02590  1.000 8.62136   ?  112 VAL A CG1 1 
ATOM   906  C  CG2 . VAL A 1 112 ? 25.39470  -7.11859  39.09553  1.000 9.68977   ?  112 VAL A CG2 1 
ATOM   907  N  N   . HIS A 1 113 ? 23.87977  -4.49446  35.38935  1.000 6.74786   ?  113 HIS A N   1 
ATOM   908  C  CA  . HIS A 1 113 ? 23.95866  -3.83222  34.09536  1.000 8.58945   ?  113 HIS A CA  1 
ATOM   909  C  C   . HIS A 1 113 ? 24.78354  -2.57063  34.24253  1.000 6.96194   ?  113 HIS A C   1 
ATOM   910  O  O   . HIS A 1 113 ? 24.37784  -1.65508  34.96402  1.000 9.61953   ?  113 HIS A O   1 
ATOM   911  C  CB  . HIS A 1 113 ? 22.57434  -3.45312  33.58595  1.000 7.22376   ?  113 HIS A CB  1 
ATOM   912  C  CG  . HIS A 1 113 ? 21.66175  -4.61684  33.39860  1.000 7.21181   ?  113 HIS A CG  1 
ATOM   913  N  ND1 . HIS A 1 113 ? 21.35059  -5.12031  32.15482  1.000 7.68681   ?  113 HIS A ND1 1 
ATOM   914  C  CD2 . HIS A 1 113 ? 20.97896  -5.36661  34.29421  1.000 8.26639   ?  113 HIS A CD2 1 
ATOM   915  C  CE1 . HIS A 1 113 ? 20.50931  -6.13014  32.29201  1.000 8.34323   ?  113 HIS A CE1 1 
ATOM   916  N  NE2 . HIS A 1 113 ? 20.27972  -6.30890  33.58083  1.000 10.08016  ?  113 HIS A NE2 1 
ATOM   917  N  N   . GLN A 1 114 ? 25.91227  -2.51406  33.56211  1.000 4.49153   ?  114 GLN A N   1 
ATOM   918  C  CA  . GLN A 1 114 ? 26.73661  -1.30857  33.52851  1.000 5.48046   ?  114 GLN A CA  1 
ATOM   919  C  C   . GLN A 1 114 ? 26.41326  -0.56241  32.23624  1.000 7.60959   ?  114 GLN A C   1 
ATOM   920  O  O   . GLN A 1 114 ? 26.76317  -1.03435  31.14910  1.000 7.39690   ?  114 GLN A O   1 
ATOM   921  C  CB  . GLN A 1 114 ? 28.22419  -1.65908  33.61956  1.000 4.70503   ?  114 GLN A CB  1 
ATOM   922  C  CG  . GLN A 1 114 ? 29.11199  -0.44027  33.60752  1.000 6.35805   ?  114 GLN A CG  1 
ATOM   923  C  CD  . GLN A 1 114 ? 30.58417  -0.77887  33.65067  1.000 6.45858   ?  114 GLN A CD  1 
ATOM   924  O  OE1 . GLN A 1 114 ? 30.97797  -1.95990  33.60826  1.000 7.10738   ?  114 GLN A OE1 1 
ATOM   925  N  NE2 . GLN A 1 114 ? 31.41677  0.25326   33.75860  1.000 6.74569   ?  114 GLN A NE2 1 
ATOM   926  N  N   . ASN A 1 115 ? 25.73590  0.59002   32.35967  1.000 8.86518   ?  115 ASN A N   1 
ATOM   927  C  CA  . ASN A 1 115 ? 25.18484  1.33496   31.23040  1.000 6.44092   ?  115 ASN A CA  1 
ATOM   928  C  C   . ASN A 1 115 ? 25.79831  2.72446   31.11777  1.000 5.53509   ?  115 ASN A C   1 
ATOM   929  O  O   . ASN A 1 115 ? 25.87170  3.46175   32.10291  1.000 6.76560   ?  115 ASN A O   1 
ATOM   930  C  CB  . ASN A 1 115 ? 23.65212  1.56287   31.35464  1.000 7.04003   ?  115 ASN A CB  1 
ATOM   931  C  CG  . ASN A 1 115 ? 22.82767  0.36346   31.01505  1.000 11.19883  ?  115 ASN A CG  1 
ATOM   932  O  OD1 . ASN A 1 115 ? 23.29092  -0.77105  31.05756  1.000 13.06498  ?  115 ASN A OD1 1 
ATOM   933  N  ND2 . ASN A 1 115 ? 21.55352  0.61835   30.68434  1.000 9.58268   ?  115 ASN A ND2 1 
ATOM   934  N  N   . ARG A 1 116 ? 26.15216  3.10874   29.89710  1.000 4.71428   ?  116 ARG A N   1 
ATOM   935  C  CA  . ARG A 1 116 ? 26.37153  4.50135   29.53492  1.000 5.57276   ?  116 ARG A CA  1 
ATOM   936  C  C   . ARG A 1 116 ? 25.39823  4.85536   28.43022  1.000 6.32110   ?  116 ARG A C   1 
ATOM   937  O  O   . ARG A 1 116 ? 25.31861  4.14314   27.42486  1.000 5.91674   ?  116 ARG A O   1 
ATOM   938  C  CB  . ARG A 1 116 ? 27.79723  4.75179   29.03875  1.000 7.41872   ?  116 ARG A CB  1 
ATOM   939  C  CG  . ARG A 1 116 ? 27.93202  6.09167   28.28698  1.000 11.07264  ?  116 ARG A CG  1 
ATOM   940  C  CD  . ARG A 1 116 ? 29.38798  6.37659   27.98511  1.000 12.15322  ?  116 ARG A CD  1 
ATOM   941  N  NE  . ARG A 1 116 ? 30.14065  6.73450   29.18126  1.000 7.60123   ?  116 ARG A NE  1 
ATOM   942  C  CZ  . ARG A 1 116 ? 31.42673  7.06628   29.16192  1.000 14.31424  ?  116 ARG A CZ  1 
ATOM   943  N  NH1 . ARG A 1 116 ? 32.13442  7.02306   28.04272  1.000 10.66657  ?  116 ARG A NH1 1 
ATOM   944  N  NH2 . ARG A 1 116 ? 32.01389  7.46276   30.28607  1.000 9.43674   ?  116 ARG A NH2 1 
ATOM   945  N  N   . THR A 1 117 ? 24.66955  5.95331   28.61644  1.000 7.57011   ?  117 THR A N   1 
ATOM   946  C  CA  . THR A 1 117 ? 23.80405  6.49549   27.57852  1.000 7.05520   ?  117 THR A CA  1 
ATOM   947  C  C   . THR A 1 117 ? 24.32726  7.87151   27.20433  1.000 7.61098   ?  117 THR A C   1 
ATOM   948  O  O   . THR A 1 117 ? 24.60876  8.69727   28.08232  1.000 7.50628   ?  117 THR A O   1 
ATOM   949  C  CB  . THR A 1 117 ? 22.34263  6.56723   28.04114  1.000 4.18047   ?  117 THR A CB  1 
ATOM   950  O  OG1 . THR A 1 117 ? 21.79053  5.24156   28.04932  1.000 7.39506   ?  117 THR A OG1 1 
ATOM   951  C  CG2 . THR A 1 117 ? 21.51238  7.45564   27.09992  1.000 4.39420   ?  117 THR A CG2 1 
ATOM   952  N  N   . ARG A 1 118 ? 24.47567  8.10797   25.91782  1.000 6.62227   ?  118 ARG A N   1 
ATOM   953  C  CA  . ARG A 1 118 ? 24.95602  9.37688   25.40351  1.000 6.12756   ?  118 ARG A CA  1 
ATOM   954  C  C   . ARG A 1 118 ? 23.80415  10.19605  24.85149  1.000 8.81079   ?  118 ARG A C   1 
ATOM   955  O  O   . ARG A 1 118 ? 22.85298  9.65886   24.27857  1.000 7.66807   ?  118 ARG A O   1 
ATOM   956  C  CB  . ARG A 1 118 ? 25.99323  9.15334   24.30284  1.000 12.69730  ?  118 ARG A CB  1 
ATOM   957  C  CG  . ARG A 1 118 ? 27.29592  8.53801   24.79208  1.000 16.86212  ?  118 ARG A CG  1 
ATOM   958  C  CD  . ARG A 1 118 ? 28.36693  8.65015   23.70747  1.000 22.82855  ?  118 ARG A CD  1 
ATOM   959  N  NE  . ARG A 1 118 ? 29.67190  8.16475   24.14242  1.000 32.14602  ?  118 ARG A NE  1 
ATOM   960  C  CZ  . ARG A 1 118 ? 30.49255  8.83608   24.93850  1.000 20.78622  ?  118 ARG A CZ  1 
ATOM   961  N  NH1 . ARG A 1 118 ? 30.15985  10.00138  25.44473  1.000 18.48923  ?  118 ARG A NH1 1 
ATOM   962  N  NH2 . ARG A 1 118 ? 31.67803  8.31657   25.23584  1.000 35.17730  ?  118 ARG A NH2 1 
ATOM   963  N  N   . ALA A 1 119 ? 23.90170  11.51198  25.03013  1.000 9.18380   ?  119 ALA A N   1 
ATOM   964  C  CA  . ALA A 1 119 ? 23.01969  12.44911  24.35623  1.000 9.13010   ?  119 ALA A CA  1 
ATOM   965  C  C   . ALA A 1 119 ? 23.85439  13.44438  23.56644  1.000 11.69709  ?  119 ALA A C   1 
ATOM   966  O  O   . ALA A 1 119 ? 25.03652  13.65558  23.84496  1.000 11.69179  ?  119 ALA A O   1 
ATOM   967  C  CB  . ALA A 1 119 ? 22.12164  13.20059  25.34425  1.000 10.29269  ?  119 ALA A CB  1 
ATOM   968  N  N   . ASP A 1 120 ? 23.22545  14.06212  22.57443  1.000 10.27570  ?  120 ASP A N   1 
ATOM   969  C  CA  . ASP A 1 120 ? 23.89782  15.06989  21.77185  1.000 10.51258  ?  120 ASP A CA  1 
ATOM   970  C  C   . ASP A 1 120 ? 22.83711  16.04021  21.29438  1.000 10.95544  ?  120 ASP A C   1 
ATOM   971  O  O   . ASP A 1 120 ? 21.64159  15.77338  21.40506  1.000 10.29337  ?  120 ASP A O   1 
ATOM   972  C  CB  . ASP A 1 120 ? 24.63663  14.44408  20.58568  1.000 16.25650  ?  120 ASP A CB  1 
ATOM   973  C  CG  . ASP A 1 120 ? 25.79953  15.28768  20.10568  1.000 25.75941  ?  120 ASP A CG  1 
ATOM   974  O  OD1 . ASP A 1 120 ? 25.87962  16.49447  20.45838  1.000 18.94010  ?  120 ASP A OD1 1 
ATOM   975  O  OD2 . ASP A 1 120 ? 26.64500  14.72994  19.37524  1.000 23.56334  -1 120 ASP A OD2 1 
ATOM   976  N  N   . GLY A 1 121 ? 23.28723  17.17853  20.77165  1.000 12.12318  ?  121 GLY A N   1 
ATOM   977  C  CA  . GLY A 1 121 ? 22.37036  18.12769  20.16680  1.000 12.83449  ?  121 GLY A CA  1 
ATOM   978  C  C   . GLY A 1 121 ? 21.43921  17.44661  19.18177  1.000 15.94660  ?  121 GLY A C   1 
ATOM   979  O  O   . GLY A 1 121 ? 21.89995  16.76387  18.26183  1.000 15.81316  ?  121 GLY A O   1 
ATOM   980  N  N   . GLY A 1 122 ? 20.13096  17.58260  19.39949  1.000 15.72530  ?  122 GLY A N   1 
ATOM   981  C  CA  . GLY A 1 122 ? 19.13321  16.99282  18.52716  1.000 17.76815  ?  122 GLY A CA  1 
ATOM   982  C  C   . GLY A 1 122 ? 18.90320  15.49758  18.68457  1.000 18.16795  ?  122 GLY A C   1 
ATOM   983  O  O   . GLY A 1 122 ? 17.98011  14.96744  18.04937  1.000 17.90525  ?  122 GLY A O   1 
ATOM   984  N  N   . ARG A 1 123 ? 19.69408  14.79791  19.50307  1.000 10.42019  ?  123 ARG A N   1 
ATOM   985  C  CA  . ARG A 1 123 ? 19.54125  13.35278  19.70451  1.000 9.32844   ?  123 ARG A CA  1 
ATOM   986  C  C   . ARG A 1 123 ? 19.56253  13.01818  21.19340  1.000 6.97977   ?  123 ARG A C   1 
ATOM   987  O  O   . ARG A 1 123 ? 20.62750  12.76142  21.77580  1.000 7.89346   ?  123 ARG A O   1 
ATOM   988  C  CB  . ARG A 1 123 ? 20.63054  12.57323  18.97358  1.000 9.33038   ?  123 ARG A CB  1 
ATOM   989  C  CG  . ARG A 1 123 ? 20.43094  11.03044  19.03084  1.000 11.89778  ?  123 ARG A CG  1 
ATOM   990  C  CD  . ARG A 1 123 ? 19.30714  10.58422  18.06210  1.000 10.00838  ?  123 ARG A CD  1 
ATOM   991  N  NE  . ARG A 1 123 ? 18.95590  9.18338   18.25942  1.000 11.07005  ?  123 ARG A NE  1 
ATOM   992  C  CZ  . ARG A 1 123 ? 19.57088  8.15990   17.68269  1.000 10.87336  ?  123 ARG A CZ  1 
ATOM   993  N  NH1 . ARG A 1 123 ? 20.57339  8.34299   16.83790  1.000 12.65514  ?  123 ARG A NH1 1 
ATOM   994  N  NH2 . ARG A 1 123 ? 19.19408  6.91987   17.99284  1.000 7.99273   ?  123 ARG A NH2 1 
ATOM   995  N  N   . PRO A 1 124 ? 18.40150  12.97969  21.83196  1.000 8.10641   ?  124 PRO A N   1 
ATOM   996  C  CA  . PRO A 1 124 ? 18.33339  12.55388  23.23485  1.000 9.12919   ?  124 PRO A CA  1 
ATOM   997  C  C   . PRO A 1 124 ? 18.78741  11.10866  23.40285  1.000 6.62809   ?  124 PRO A C   1 
ATOM   998  O  O   . PRO A 1 124 ? 18.82629  10.32214  22.45450  1.000 9.18247   ?  124 PRO A O   1 
ATOM   999  C  CB  . PRO A 1 124 ? 16.84411  12.69503  23.57702  1.000 12.36950  ?  124 PRO A CB  1 
ATOM   1000 C  CG  . PRO A 1 124 ? 16.25813  13.56518  22.48997  1.000 15.10101  ?  124 PRO A CG  1 
ATOM   1001 C  CD  . PRO A 1 124 ? 17.07703  13.28939  21.26977  1.000 9.96815   ?  124 PRO A CD  1 
ATOM   1002 N  N   . GLY A 1 125 ? 19.12887  10.75648  24.64141  1.000 5.56338   ?  125 GLY A N   1 
ATOM   1003 C  CA  . GLY A 1 125 ? 19.46184  9.38394   24.95204  1.000 4.65200   ?  125 GLY A CA  1 
ATOM   1004 C  C   . GLY A 1 125 ? 18.35440  8.71102   25.74042  1.000 7.09739   ?  125 GLY A C   1 
ATOM   1005 O  O   . GLY A 1 125 ? 18.10571  9.04257   26.90656  1.000 8.31923   ?  125 GLY A O   1 
ATOM   1006 N  N   . PRO A 1 126 ? 17.66209  7.75388   25.12350  1.000 8.84912   ?  126 PRO A N   1 
ATOM   1007 C  CA  . PRO A 1 126 ? 16.53635  7.09938   25.81056  1.000 6.99638   ?  126 PRO A CA  1 
ATOM   1008 C  C   . PRO A 1 126 ? 17.04413  6.21727   26.94440  1.000 4.80979   ?  126 PRO A C   1 
ATOM   1009 O  O   . PRO A 1 126 ? 17.95595  5.41055   26.76206  1.000 7.44307   ?  126 PRO A O   1 
ATOM   1010 C  CB  . PRO A 1 126 ? 15.87270  6.26307   24.70885  1.000 7.12112   ?  126 PRO A CB  1 
ATOM   1011 C  CG  . PRO A 1 126 ? 16.53298  6.68482   23.40720  1.000 12.99037  ?  126 PRO A CG  1 
ATOM   1012 C  CD  . PRO A 1 126 ? 17.88267  7.21150   23.77361  1.000 9.82092   ?  126 PRO A CD  1 
ATOM   1013 N  N   . LEU A 1 127 ? 16.45324  6.38789   28.12156  1.000 6.37969   ?  127 LEU A N   1 
ATOM   1014 C  CA  . LEU A 1 127 ? 16.81353  5.59772   29.29456  1.000 6.94188   ?  127 LEU A CA  1 
ATOM   1015 C  C   . LEU A 1 127 ? 15.84212  4.45677   29.56486  1.000 8.18201   ?  127 LEU A C   1 
ATOM   1016 O  O   . LEU A 1 127 ? 16.26051  3.37652   29.96847  1.000 9.70025   ?  127 LEU A O   1 
ATOM   1017 C  CB  . LEU A 1 127 ? 16.89668  6.50416   30.52820  1.000 6.12439   ?  127 LEU A CB  1 
ATOM   1018 C  CG  . LEU A 1 127 ? 18.00347  7.55314   30.41653  1.000 8.38168   ?  127 LEU A CG  1 
ATOM   1019 C  CD1 . LEU A 1 127 ? 18.00070  8.47149   31.62845  1.000 10.26731  ?  127 LEU A CD1 1 
ATOM   1020 C  CD2 . LEU A 1 127 ? 19.38459  6.90770   30.23843  1.000 6.49816   ?  127 LEU A CD2 1 
ATOM   1021 N  N   . THR A 1 128 ? 14.54315  4.65470   29.36165  1.000 7.67580   ?  128 THR A N   1 
ATOM   1022 C  CA  . THR A 1 128 ? 13.55762  3.58630   29.51635  1.000 7.70547   ?  128 THR A CA  1 
ATOM   1023 C  C   . THR A 1 128 ? 12.65283  3.54549   28.28392  1.000 9.76602   ?  128 THR A C   1 
ATOM   1024 O  O   . THR A 1 128 ? 11.46874  3.87327   28.36289  1.000 6.66274   ?  128 THR A O   1 
ATOM   1025 C  CB  . THR A 1 128 ? 12.74832  3.77213   30.80752  1.000 10.03083  ?  128 THR A CB  1 
ATOM   1026 O  OG1 . THR A 1 128 ? 12.08745  5.03730   30.78743  1.000 6.74274   ?  128 THR A OG1 1 
ATOM   1027 C  CG2 . THR A 1 128 ? 13.67685  3.76425   32.02121  1.000 5.86737   ?  128 THR A CG2 1 
ATOM   1028 N  N   . PRO A 1 129 ? 13.17036  3.09683   27.13498  1.000 8.50387   ?  129 PRO A N   1 
ATOM   1029 C  CA  . PRO A 1 129 ? 12.30241  2.93573   25.95441  1.000 9.60564   ?  129 PRO A CA  1 
ATOM   1030 C  C   . PRO A 1 129 ? 11.19298  1.92913   26.17763  1.000 14.67951  ?  129 PRO A C   1 
ATOM   1031 O  O   . PRO A 1 129 ? 10.23609  1.89572   25.38943  1.000 13.31527  ?  129 PRO A O   1 
ATOM   1032 C  CB  . PRO A 1 129 ? 13.27296  2.47056   24.85905  1.000 8.74529   ?  129 PRO A CB  1 
ATOM   1033 C  CG  . PRO A 1 129 ? 14.39479  1.83458   25.60828  1.000 14.19342  ?  129 PRO A CG  1 
ATOM   1034 C  CD  . PRO A 1 129 ? 14.54581  2.64947   26.86398  1.000 9.99164   ?  129 PRO A CD  1 
ATOM   1035 N  N   . GLU A 1 130 ? 11.30454  1.09823   27.21776  1.000 9.43044   ?  130 GLU A N   1 
ATOM   1036 C  CA  . GLU A 1 130 ? 10.19715  0.25721   27.64881  1.000 11.10995  ?  130 GLU A CA  1 
ATOM   1037 C  C   . GLU A 1 130 ? 8.96326   1.06082   28.03505  1.000 12.08052  ?  130 GLU A C   1 
ATOM   1038 O  O   . GLU A 1 130 ? 7.86919   0.48608   28.12957  1.000 11.18810  ?  130 GLU A O   1 
ATOM   1039 C  CB  . GLU A 1 130 ? 10.61998  -0.59608  28.84935  1.000 8.98343   ?  130 GLU A CB  1 
ATOM   1040 C  CG  . GLU A 1 130 ? 11.89475  -1.41332  28.64220  1.000 14.04323  ?  130 GLU A CG  1 
ATOM   1041 C  CD  . GLU A 1 130 ? 13.17738  -0.65012  28.95817  1.000 14.86312  ?  130 GLU A CD  1 
ATOM   1042 O  OE1 . GLU A 1 130 ? 13.17038  0.60491   29.01058  1.000 10.86473  ?  130 GLU A OE1 1 
ATOM   1043 O  OE2 . GLU A 1 130 ? 14.21644  -1.31150  29.13878  1.000 17.26562  -1 130 GLU A OE2 1 
ATOM   1044 N  N   . GLY A 1 131 ? 9.10703   2.36724   28.28179  1.000 12.30102  ?  131 GLY A N   1 
ATOM   1045 C  CA  . GLY A 1 131 ? 8.00311   3.10122   28.88448  1.000 13.66478  ?  131 GLY A CA  1 
ATOM   1046 C  C   . GLY A 1 131 ? 7.92984   2.78810   30.37551  1.000 10.27006  ?  131 GLY A C   1 
ATOM   1047 O  O   . GLY A 1 131 ? 8.89231   2.30846   30.98287  1.000 8.92766   ?  131 GLY A O   1 
ATOM   1048 N  N   . VAL A 1 132 ? 6.77361   3.08973   30.97433  1.000 9.21089   ?  132 VAL A N   1 
ATOM   1049 C  CA  . VAL A 1 132 ? 6.56420   2.76619   32.38330  1.000 8.93668   ?  132 VAL A CA  1 
ATOM   1050 C  C   . VAL A 1 132 ? 6.53735   1.25425   32.51130  1.000 11.53150  ?  132 VAL A C   1 
ATOM   1051 O  O   . VAL A 1 132 ? 5.78910   0.57694   31.79548  1.000 7.60424   ?  132 VAL A O   1 
ATOM   1052 C  CB  . VAL A 1 132 ? 5.24986   3.37209   32.90726  1.000 10.19790  ?  132 VAL A CB  1 
ATOM   1053 C  CG1 . VAL A 1 132 ? 5.05522   3.02360   34.37247  1.000 12.44082  ?  132 VAL A CG1 1 
ATOM   1054 C  CG2 . VAL A 1 132 ? 5.20290   4.86641   32.71829  1.000 8.94060   ?  132 VAL A CG2 1 
ATOM   1055 N  N   . HIS A 1 133 ? 7.34822   0.70572   33.41120  1.000 5.53871   ?  133 HIS A N   1 
ATOM   1056 C  CA  . HIS A 1 133 ? 7.52048   -0.74235  33.38752  1.000 6.60264   ?  133 HIS A CA  1 
ATOM   1057 C  C   . HIS A 1 133 ? 7.92064   -1.25462  34.76117  1.000 13.62254  ?  133 HIS A C   1 
ATOM   1058 O  O   . HIS A 1 133 ? 8.30461   -0.49109  35.65335  1.000 7.76479   ?  133 HIS A O   1 
ATOM   1059 C  CB  . HIS A 1 133 ? 8.58132   -1.15189  32.35169  1.000 7.93508   ?  133 HIS A CB  1 
ATOM   1060 C  CG  . HIS A 1 133 ? 9.96063   -0.67339  32.69837  1.000 7.68269   ?  133 HIS A CG  1 
ATOM   1061 N  ND1 . HIS A 1 133 ? 10.38287  0.62077   32.46024  1.000 8.08253   ?  133 HIS A ND1 1 
ATOM   1062 C  CD2 . HIS A 1 133 ? 10.99566  -1.30303  33.30732  1.000 9.92076   ?  133 HIS A CD2 1 
ATOM   1063 C  CE1 . HIS A 1 133 ? 11.62863  0.75657   32.88648  1.000 7.76719   ?  133 HIS A CE1 1 
ATOM   1064 N  NE2 . HIS A 1 133 ? 12.01901  -0.39369  33.41750  1.000 9.04865   ?  133 HIS A NE2 1 
ATOM   1065 N  N   . HIS A 1 134 ? 7.80496   -2.57256  34.92171  1.000 7.03245   ?  134 HIS A N   1 
ATOM   1066 C  CA  . HIS A 1 134 ? 8.47836   -3.31579  35.97686  1.000 7.43560   ?  134 HIS A CA  1 
ATOM   1067 C  C   . HIS A 1 134 ? 9.63098   -4.07601  35.34453  1.000 9.67580   ?  134 HIS A C   1 
ATOM   1068 O  O   . HIS A 1 134 ? 9.51108   -4.57303  34.21881  1.000 9.63546   ?  134 HIS A O   1 
ATOM   1069 C  CB  . HIS A 1 134 ? 7.56179   -4.33431  36.65871  1.000 9.26572   ?  134 HIS A CB  1 
ATOM   1070 C  CG  . HIS A 1 134 ? 6.29576   -3.76136  37.21659  1.000 9.91644   ?  134 HIS A CG  1 
ATOM   1071 N  ND1 . HIS A 1 134 ? 6.18511   -3.34079  38.52333  1.000 9.10567   ?  134 HIS A ND1 1 
ATOM   1072 C  CD2 . HIS A 1 134 ? 5.07230   -3.58705  36.66194  1.000 15.69717  ?  134 HIS A CD2 1 
ATOM   1073 C  CE1 . HIS A 1 134 ? 4.95554   -2.90912  38.74509  1.000 15.03218  ?  134 HIS A CE1 1 
ATOM   1074 N  NE2 . HIS A 1 134 ? 4.25896   -3.04982  37.63044  1.000 11.87184  ?  134 HIS A NE2 1 
ATOM   1075 N  N   . ASP A 1 135 ? 10.74464  -4.18855  36.05389  1.000 7.08373   ?  135 ASP A N   1 
ATOM   1076 C  CA  . ASP A 1 135 ? 11.82200  -4.94567  35.44618  1.000 9.68793   ?  135 ASP A CA  1 
ATOM   1077 C  C   . ASP A 1 135 ? 11.54512  -6.44068  35.53619  1.000 10.52991  ?  135 ASP A C   1 
ATOM   1078 O  O   . ASP A 1 135 ? 12.08855  -7.21879  34.75317  1.000 10.85672  ?  135 ASP A O   1 
ATOM   1079 C  CB  . ASP A 1 135 ? 13.15647  -4.55085  36.08815  1.000 9.05031   ?  135 ASP A CB  1 
ATOM   1080 C  CG  . ASP A 1 135 ? 13.67351  -3.19400  35.56737  1.000 13.50318  ?  135 ASP A CG  1 
ATOM   1081 O  OD1 . ASP A 1 135 ? 13.26585  -2.75128  34.50558  1.000 14.66960  ?  135 ASP A OD1 1 
ATOM   1082 O  OD2 . ASP A 1 135 ? 14.52594  -2.55036  36.17199  1.000 35.17299  -1 135 ASP A OD2 1 
ATOM   1083 N  N   . GLY A 1 136 ? 10.67982  -6.84729  36.46292  1.000 9.15431   ?  136 GLY A N   1 
ATOM   1084 C  CA  . GLY A 1 136 ? 10.25306  -8.22448  36.60210  1.000 8.65914   ?  136 GLY A CA  1 
ATOM   1085 C  C   . GLY A 1 136 ? 10.80164  -8.91238  37.82903  1.000 11.84944  ?  136 GLY A C   1 
ATOM   1086 O  O   . GLY A 1 136 ? 10.47354  -10.07987 38.07025  1.000 9.19626   ?  136 GLY A O   1 
ATOM   1087 N  N   . HIS A 1 137 ? 11.61859  -8.23214  38.60511  1.000 8.26732   ?  137 HIS A N   1 
ATOM   1088 C  CA  . HIS A 1 137 ? 12.28137  -8.84230  39.73999  1.000 9.04385   ?  137 HIS A CA  1 
ATOM   1089 C  C   . HIS A 1 137 ? 11.58437  -8.42261  41.03616  1.000 9.07458   ?  137 HIS A C   1 
ATOM   1090 O  O   . HIS A 1 137 ? 10.47958  -7.87951  41.03228  1.000 10.87793  ?  137 HIS A O   1 
ATOM   1091 C  CB  . HIS A 1 137 ? 13.76346  -8.44818  39.74595  1.000 6.49060   ?  137 HIS A CB  1 
ATOM   1092 C  CG  . HIS A 1 137 ? 14.50058  -8.82059  38.49888  1.000 14.36899  ?  137 HIS A CG  1 
ATOM   1093 N  ND1 . HIS A 1 137 ? 15.42688  -9.83609  38.46590  1.000 9.44242   ?  137 HIS A ND1 1 
ATOM   1094 C  CD2 . HIS A 1 137 ? 14.46595  -8.30301  37.24527  1.000 7.49324   ?  137 HIS A CD2 1 
ATOM   1095 C  CE1 . HIS A 1 137 ? 15.93611  -9.92972  37.24999  1.000 9.00959   ?  137 HIS A CE1 1 
ATOM   1096 N  NE2 . HIS A 1 137 ? 15.37975  -8.99954  36.49413  1.000 9.76578   ?  137 HIS A NE2 1 
ATOM   1097 N  N   . GLU A 1 138 ? 12.24359  -8.65901  42.16566  1.000 7.55422   ?  138 GLU A N   1 
ATOM   1098 C  CA  . GLU A 1 138 ? 11.64047  -8.28678  43.43214  1.000 10.76630  ?  138 GLU A CA  1 
ATOM   1099 C  C   . GLU A 1 138 ? 12.10658  -6.91741  43.89896  1.000 8.94343   ?  138 GLU A C   1 
ATOM   1100 O  O   . GLU A 1 138 ? 11.28768  -6.11197  44.35757  1.000 9.51008   ?  138 GLU A O   1 
ATOM   1101 C  CB  . GLU A 1 138 ? 11.94185  -9.35034  44.49410  1.000 9.94682   ?  138 GLU A CB  1 
ATOM   1102 C  CG  . GLU A 1 138 ? 11.27712  -9.07288  45.83163  1.000 10.15470  ?  138 GLU A CG  1 
ATOM   1103 C  CD  . GLU A 1 138 ? 11.27354  -10.28470 46.76478  1.000 15.81141  ?  138 GLU A CD  1 
ATOM   1104 O  OE1 . GLU A 1 138 ? 11.62255  -11.39706 46.31991  1.000 14.55384  ?  138 GLU A OE1 1 
ATOM   1105 O  OE2 . GLU A 1 138 ? 10.91438  -10.11448 47.94558  1.000 14.29969  -1 138 GLU A OE2 1 
ATOM   1106 N  N   . PHE A 1 139 ? 13.40305  -6.62549  43.78316  1.000 9.72145   ?  139 PHE A N   1 
ATOM   1107 C  CA  . PHE A 1 139 ? 13.93961  -5.29959  44.07789  1.000 9.24786   ?  139 PHE A CA  1 
ATOM   1108 C  C   . PHE A 1 139 ? 14.86155  -4.85135  42.95676  1.000 9.37284   ?  139 PHE A C   1 
ATOM   1109 O  O   . PHE A 1 139 ? 15.51336  -5.67842  42.31529  1.000 10.82149  ?  139 PHE A O   1 
ATOM   1110 C  CB  . PHE A 1 139 ? 14.74062  -5.28662  45.37753  1.000 7.04477   ?  139 PHE A CB  1 
ATOM   1111 C  CG  . PHE A 1 139 ? 13.95807  -5.71518  46.56681  1.000 12.26291  ?  139 PHE A CG  1 
ATOM   1112 C  CD1 . PHE A 1 139 ? 12.95042  -4.90259  47.06404  1.000 15.54317  ?  139 PHE A CD1 1 
ATOM   1113 C  CD2 . PHE A 1 139 ? 14.21762  -6.92883  47.19085  1.000 10.91931  ?  139 PHE A CD2 1 
ATOM   1114 C  CE1 . PHE A 1 139 ? 12.20229  -5.29631  48.16843  1.000 18.84889  ?  139 PHE A CE1 1 
ATOM   1115 C  CE2 . PHE A 1 139 ? 13.47901  -7.32076  48.29365  1.000 15.43124  ?  139 PHE A CE2 1 
ATOM   1116 C  CZ  . PHE A 1 139 ? 12.47572  -6.50033  48.78135  1.000 16.26555  ?  139 PHE A CZ  1 
ATOM   1117 N  N   . VAL A 1 140 ? 14.96605  -3.53444  42.76420  1.000 7.67674   ?  140 VAL A N   1 
ATOM   1118 C  CA  . VAL A 1 140 ? 15.89793  -2.96697  41.79263  1.000 4.87913   ?  140 VAL A CA  1 
ATOM   1119 C  C   . VAL A 1 140 ? 16.65021  -1.81697  42.46018  1.000 6.31917   ?  140 VAL A C   1 
ATOM   1120 O  O   . VAL A 1 140 ? 16.06716  -1.02855  43.21105  1.000 8.17916   ?  140 VAL A O   1 
ATOM   1121 C  CB  . VAL A 1 140 ? 15.16067  -2.52611  40.50446  1.000 10.06406  ?  140 VAL A CB  1 
ATOM   1122 C  CG1 . VAL A 1 140 ? 16.05755  -1.67738  39.60382  1.000 12.34407  ?  140 VAL A CG1 1 
ATOM   1123 C  CG2 . VAL A 1 140 ? 14.68257  -3.75797  39.73997  1.000 7.63651   ?  140 VAL A CG2 1 
ATOM   1124 N  N   . MET A 1 141 ? 17.95978  -1.75114  42.21783  1.000 4.44303   ?  141 MET A N   1 
ATOM   1125 C  CA  . MET A 1 141 ? 18.80672  -0.63807  42.62364  1.000 6.51771   ?  141 MET A CA  1 
ATOM   1126 C  C   . MET A 1 141 ? 19.38063  0.01538   41.37878  1.000 6.93562   ?  141 MET A C   1 
ATOM   1127 O  O   . MET A 1 141 ? 19.95699  -0.67549  40.53474  1.000 6.43995   ?  141 MET A O   1 
ATOM   1128 C  CB  . MET A 1 141 ? 19.94521  -1.13481  43.51969  1.000 4.57964   ?  141 MET A CB  1 
ATOM   1129 C  CG  . MET A 1 141 ? 20.99164  -0.05243  43.86854  1.000 6.89391   ?  141 MET A CG  1 
ATOM   1130 S  SD  . MET A 1 141 ? 22.32592  -0.72512  44.87804  1.000 9.12811   ?  141 MET A SD  1 
ATOM   1131 C  CE  . MET A 1 141 ? 23.31964  0.74202   45.18253  1.000 11.94648  ?  141 MET A CE  1 
ATOM   1132 N  N   . ILE A 1 142 ? 19.19399  1.32818   41.23818  1.000 7.03837   ?  142 ILE A N   1 
ATOM   1133 C  CA  . ILE A 1 142 ? 19.76827  2.06375   40.11498  1.000 4.30114   ?  142 ILE A CA  1 
ATOM   1134 C  C   . ILE A 1 142 ? 20.68590  3.12791   40.67996  1.000 6.22332   ?  142 ILE A C   1 
ATOM   1135 O  O   . ILE A 1 142 ? 20.22316  4.04788   41.36355  1.000 6.95405   ?  142 ILE A O   1 
ATOM   1136 C  CB  . ILE A 1 142 ? 18.70419  2.70488   39.21965  1.000 5.24052   ?  142 ILE A CB  1 
ATOM   1137 C  CG1 . ILE A 1 142 ? 17.82076  1.61484   38.59610  1.000 9.00562   ?  142 ILE A CG1 1 
ATOM   1138 C  CG2 . ILE A 1 142 ? 19.40123  3.58489   38.17238  1.000 6.11454   ?  142 ILE A CG2 1 
ATOM   1139 C  CD1 . ILE A 1 142 ? 16.32998  1.93168   38.59788  1.000 13.53430  ?  142 ILE A CD1 1 
ATOM   1140 N  N   . ALA A 1 143 ? 21.97180  3.02718   40.36191  1.000 6.38938   ?  143 ALA A N   1 
ATOM   1141 C  CA  . ALA A 1 143 ? 22.97924  3.92358   40.90343  1.000 9.17874   ?  143 ALA A CA  1 
ATOM   1142 C  C   . ALA A 1 143 ? 23.56001  4.78028   39.78992  1.000 7.86357   ?  143 ALA A C   1 
ATOM   1143 O  O   . ALA A 1 143 ? 23.90029  4.26569   38.72255  1.000 6.37113   ?  143 ALA A O   1 
ATOM   1144 C  CB  . ALA A 1 143 ? 24.09115  3.12577   41.59940  1.000 3.36191   ?  143 ALA A CB  1 
ATOM   1145 N  N   . ILE A 1 144 ? 23.66866  6.08345   40.04449  1.000 7.18827   ?  144 ILE A N   1 
ATOM   1146 C  CA  . ILE A 1 144 ? 24.27950  7.02045   39.10874  1.000 10.39892  ?  144 ILE A CA  1 
ATOM   1147 C  C   . ILE A 1 144 ? 25.75075  7.17105   39.46473  1.000 12.77749  ?  144 ILE A C   1 
ATOM   1148 O  O   . ILE A 1 144 ? 26.09698  7.60682   40.57643  1.000 9.91177   ?  144 ILE A O   1 
ATOM   1149 C  CB  . ILE A 1 144 ? 23.58921  8.39285   39.13406  1.000 9.23536   ?  144 ILE A CB  1 
ATOM   1150 C  CG1 . ILE A 1 144 ? 22.06673  8.25891   39.20883  1.000 7.25402   ?  144 ILE A CG1 1 
ATOM   1151 C  CG2 . ILE A 1 144 ? 24.03345  9.22172   37.96371  1.000 5.09283   ?  144 ILE A CG2 1 
ATOM   1152 C  CD1 . ILE A 1 144 ? 21.43800  7.43726   38.12097  1.000 6.35939   ?  144 ILE A CD1 1 
ATOM   1153 N  N   . LEU A 1 145 ? 26.62207  6.85421   38.51809  1.000 6.56003   ?  145 LEU A N   1 
ATOM   1154 C  CA  . LEU A 1 145 ? 28.05356  6.94133   38.78076  1.000 8.94457   ?  145 LEU A CA  1 
ATOM   1155 C  C   . LEU A 1 145 ? 28.68313  8.21133   38.23607  1.000 10.61950  ?  145 LEU A C   1 
ATOM   1156 O  O   . LEU A 1 145 ? 29.65688  8.69663   38.81798  1.000 10.63592  ?  145 LEU A O   1 
ATOM   1157 C  CB  . LEU A 1 145 ? 28.79306  5.72918   38.19261  1.000 7.35331   ?  145 LEU A CB  1 
ATOM   1158 C  CG  . LEU A 1 145 ? 28.94373  4.45571   39.03687  1.000 11.84312  ?  145 LEU A CG  1 
ATOM   1159 C  CD1 . LEU A 1 145 ? 29.71999  4.77570   40.30993  1.000 17.99124  ?  145 LEU A CD1 1 
ATOM   1160 C  CD2 . LEU A 1 145 ? 27.60864  3.85702   39.37503  1.000 12.65123  ?  145 LEU A CD2 1 
ATOM   1161 N  N   . ASN A 1 146 ? 28.14880  8.77432   37.15501  1.000 9.56950   ?  146 ASN A N   1 
ATOM   1162 C  CA  . ASN A 1 146 ? 28.73731  9.95455   36.53582  1.000 6.16605   ?  146 ASN A CA  1 
ATOM   1163 C  C   . ASN A 1 146 ? 27.73870  10.55025  35.55598  1.000 10.92440  ?  146 ASN A C   1 
ATOM   1164 O  O   . ASN A 1 146 ? 27.03261  9.81384   34.86559  1.000 6.73240   ?  146 ASN A O   1 
ATOM   1165 C  CB  . ASN A 1 146 ? 30.04057  9.60611   35.79881  1.000 7.25609   ?  146 ASN A CB  1 
ATOM   1166 C  CG  . ASN A 1 146 ? 30.87694  10.84160  35.46849  1.000 17.74633  ?  146 ASN A CG  1 
ATOM   1167 O  OD1 . ASN A 1 146 ? 30.65908  11.92040  36.02168  1.000 22.97721  ?  146 ASN A OD1 1 
ATOM   1168 N  ND2 . ASN A 1 146 ? 31.83745  10.68503  34.56338  1.000 27.08375  ?  146 ASN A ND2 1 
ATOM   1169 N  N   . LYS A 1 147 ? 27.68940  11.88245  35.50365  1.000 9.06145   ?  147 LYS A N   1 
ATOM   1170 C  CA  . LYS A 1 147 ? 26.86439  12.61108  34.54061  1.000 10.48333  ?  147 LYS A CA  1 
ATOM   1171 C  C   . LYS A 1 147 ? 27.68173  13.78417  34.03539  1.000 10.96191  ?  147 LYS A C   1 
ATOM   1172 O  O   . LYS A 1 147 ? 28.22626  14.54175  34.84348  1.000 8.71539   ?  147 LYS A O   1 
ATOM   1173 C  CB  . LYS A 1 147 ? 25.55752  13.12933  35.16849  1.000 11.30473  ?  147 LYS A CB  1 
ATOM   1174 C  CG  . LYS A 1 147 ? 24.56213  12.01646  35.50913  1.000 7.15876   ?  147 LYS A CG  1 
ATOM   1175 C  CD  . LYS A 1 147 ? 23.31743  12.54929  36.24856  1.000 7.83705   ?  147 LYS A CD  1 
ATOM   1176 C  CE  . LYS A 1 147 ? 22.58439  13.60967  35.45239  1.000 13.62799  ?  147 LYS A CE  1 
ATOM   1177 N  NZ  . LYS A 1 147 ? 21.35949  14.06016  36.19298  1.000 10.11567  ?  147 LYS A NZ  1 
ATOM   1178 N  N   . VAL A 1 148 ? 27.76828  13.93783  32.71689  1.000 9.87253   ?  148 VAL A N   1 
ATOM   1179 C  CA  . VAL A 1 148 ? 28.53530  15.01390  32.10312  1.000 9.93373   ?  148 VAL A CA  1 
ATOM   1180 C  C   . VAL A 1 148 ? 27.66272  15.66924  31.05149  1.000 9.79492   ?  148 VAL A C   1 
ATOM   1181 O  O   . VAL A 1 148 ? 27.29610  15.02551  30.06422  1.000 10.83548  ?  148 VAL A O   1 
ATOM   1182 C  CB  . VAL A 1 148 ? 29.84117  14.50493  31.46625  1.000 10.22797  ?  148 VAL A CB  1 
ATOM   1183 C  CG1 . VAL A 1 148 ? 30.56406  15.66704  30.77740  1.000 17.57653  ?  148 VAL A CG1 1 
ATOM   1184 C  CG2 . VAL A 1 148 ? 30.73636  13.85849  32.51490  1.000 12.73976  ?  148 VAL A CG2 1 
ATOM   1185 N  N   . ASN A 1 149 ? 27.30952  16.93676  31.27256  1.000 9.20681   ?  149 ASN A N   1 
ATOM   1186 C  CA  . ASN A 1 149 ? 26.70405  17.77501  30.23512  1.000 9.27348   ?  149 ASN A CA  1 
ATOM   1187 C  C   . ASN A 1 149 ? 25.34684  17.24009  29.78716  1.000 10.44604  ?  149 ASN A C   1 
ATOM   1188 O  O   . ASN A 1 149 ? 25.01984  17.22097  28.59638  1.000 8.63861   ?  149 ASN A O   1 
ATOM   1189 C  CB  . ASN A 1 149 ? 27.64729  17.91801  29.03736  1.000 9.95847   ?  149 ASN A CB  1 
ATOM   1190 C  CG  . ASN A 1 149 ? 27.28119  19.09008  28.14901  1.000 23.08123  ?  149 ASN A CG  1 
ATOM   1191 O  OD1 . ASN A 1 149 ? 26.86946  20.15255  28.64505  1.000 15.47215  ?  149 ASN A OD1 1 
ATOM   1192 N  ND2 . ASN A 1 149 ? 27.40423  18.90700  26.83656  1.000 12.88167  ?  149 ASN A ND2 1 
ATOM   1193 N  N   . VAL A 1 150 ? 24.52573  16.84446  30.75096  1.000 10.66644  ?  150 VAL A N   1 
ATOM   1194 C  CA  . VAL A 1 150 ? 23.20444  16.32326  30.43097  1.000 9.69765   ?  150 VAL A CA  1 
ATOM   1195 C  C   . VAL A 1 150 ? 22.13795  17.06748  31.22061  1.000 12.46323  ?  150 VAL A C   1 
ATOM   1196 O  O   . VAL A 1 150 ? 22.39296  17.61310  32.30226  1.000 10.49310  ?  150 VAL A O   1 
ATOM   1197 C  CB  . VAL A 1 150 ? 23.12707  14.79943  30.67960  1.000 10.73274  ?  150 VAL A CB  1 
ATOM   1198 C  CG1 . VAL A 1 150 ? 24.09527  14.07227  29.72288  1.000 9.52838   ?  150 VAL A CG1 1 
ATOM   1199 C  CG2 . VAL A 1 150 ? 23.47737  14.46628  32.11384  1.000 14.09481  ?  150 VAL A CG2 1 
ATOM   1200 N  N   . ALA A 1 151 ? 20.94597  17.12892  30.63881  1.000 8.76664   ?  151 ALA A N   1 
ATOM   1201 C  CA  . ALA A 1 151 ? 19.71088  17.54441  31.28813  1.000 10.13171  ?  151 ALA A CA  1 
ATOM   1202 C  C   . ALA A 1 151 ? 18.72636  16.38591  31.17461  1.000 9.66001   ?  151 ALA A C   1 
ATOM   1203 O  O   . ALA A 1 151 ? 19.03107  15.35145  30.57615  1.000 12.96146  ?  151 ALA A O   1 
ATOM   1204 C  CB  . ALA A 1 151 ? 19.14108  18.82346  30.64617  1.000 10.70500  ?  151 ALA A CB  1 
ATOM   1205 N  N   . GLY A 1 152 ? 17.54095  16.55443  31.75443  1.000 10.63166  ?  152 GLY A N   1 
ATOM   1206 C  CA  . GLY A 1 152 ? 16.60506  15.43759  31.72022  1.000 9.62009   ?  152 GLY A CA  1 
ATOM   1207 C  C   . GLY A 1 152 ? 17.08452  14.30423  32.60938  1.000 8.63950   ?  152 GLY A C   1 
ATOM   1208 O  O   . GLY A 1 152 ? 17.75578  14.51080  33.62078  1.000 8.50805   ?  152 GLY A O   1 
ATOM   1209 N  N   . GLY A 1 153 ? 16.75627  13.08127  32.21341  1.000 8.77916   ?  153 GLY A N   1 
ATOM   1210 C  CA  . GLY A 1 153 ? 17.16106  11.93783  33.02616  1.000 8.47544   ?  153 GLY A CA  1 
ATOM   1211 C  C   . GLY A 1 153 ? 16.46716  11.89805  34.37232  1.000 9.57620   ?  153 GLY A C   1 
ATOM   1212 O  O   . GLY A 1 153 ? 17.09883  11.57872  35.38776  1.000 9.09619   ?  153 GLY A O   1 
ATOM   1213 N  N   . THR A 1 154 ? 15.17947  12.20928  34.40464  1.000 7.17480   ?  154 THR A N   1 
ATOM   1214 C  CA  . THR A 1 154 ? 14.41541  12.29333  35.64006  1.000 6.74331   ?  154 THR A CA  1 
ATOM   1215 C  C   . THR A 1 154 ? 13.67953  10.97938  35.86719  1.000 7.67576   ?  154 THR A C   1 
ATOM   1216 O  O   . THR A 1 154 ? 12.90350  10.53582  35.00702  1.000 7.25284   ?  154 THR A O   1 
ATOM   1217 C  CB  . THR A 1 154 ? 13.43182  13.46191  35.58862  1.000 9.33486   ?  154 THR A CB  1 
ATOM   1218 O  OG1 . THR A 1 154 ? 14.17297  14.67689  35.42899  1.000 9.40478   ?  154 THR A OG1 1 
ATOM   1219 C  CG2 . THR A 1 154 ? 12.64842  13.53811  36.88031  1.000 9.20261   ?  154 THR A CG2 1 
ATOM   1220 N  N   . THR A 1 155 ? 13.95160  10.35755  37.01328  1.000 4.96667   ?  155 THR A N   1 
ATOM   1221 C  CA  . THR A 1 155 ? 13.28911  9.12637   37.42706  1.000 6.46548   ?  155 THR A CA  1 
ATOM   1222 C  C   . THR A 1 155 ? 11.88383  9.43833   37.90544  1.000 8.62310   ?  155 THR A C   1 
ATOM   1223 O  O   . THR A 1 155 ? 11.66848  10.40093  38.64554  1.000 7.63888   ?  155 THR A O   1 
ATOM   1224 C  CB  . THR A 1 155 ? 14.06523  8.46278   38.56537  1.000 6.50893   ?  155 THR A CB  1 
ATOM   1225 O  OG1 . THR A 1 155 ? 15.39909  8.19933   38.12127  1.000 6.84079   ?  155 THR A OG1 1 
ATOM   1226 C  CG2 . THR A 1 155 ? 13.39586  7.13241   39.00820  1.000 4.82956   ?  155 THR A CG2 1 
ATOM   1227 N  N   . ARG A 1 156 ? 10.92830  8.61372   37.49289  1.000 7.78092   ?  156 ARG A N   1 
ATOM   1228 C  CA  . ARG A 1 156 ? 9.54338   8.77976   37.90796  1.000 7.40796   ?  156 ARG A CA  1 
ATOM   1229 C  C   . ARG A 1 156 ? 9.01146   7.44025   38.39184  1.000 6.62435   ?  156 ARG A C   1 
ATOM   1230 O  O   . ARG A 1 156 ? 9.17163   6.42812   37.70735  1.000 9.11122   ?  156 ARG A O   1 
ATOM   1231 C  CB  . ARG A 1 156 ? 8.71407   9.33353   36.75034  1.000 9.85791   ?  156 ARG A CB  1 
ATOM   1232 C  CG  . ARG A 1 156 ? 9.37315   10.60594  36.20100  1.000 16.04158  ?  156 ARG A CG  1 
ATOM   1233 C  CD  . ARG A 1 156 ? 8.59285   11.27566  35.16700  1.000 19.92299  ?  156 ARG A CD  1 
ATOM   1234 N  NE  . ARG A 1 156 ? 8.35243   10.41268  34.02240  1.000 13.34523  ?  156 ARG A NE  1 
ATOM   1235 C  CZ  . ARG A 1 156 ? 7.78016   10.85206  32.91274  1.000 20.38476  ?  156 ARG A CZ  1 
ATOM   1236 N  NH1 . ARG A 1 156 ? 7.45365   12.12333  32.77545  1.000 16.12794  ?  156 ARG A NH1 1 
ATOM   1237 N  NH2 . ARG A 1 156 ? 7.52196   9.99476   31.92497  1.000 11.17546  ?  156 ARG A NH2 1 
ATOM   1238 N  N   . LEU A 1 157 ? 8.37620   7.43348   39.56315  1.000 6.04434   ?  157 LEU A N   1 
ATOM   1239 C  CA  . LEU A 1 157 ? 7.83492   6.21457   40.15320  1.000 6.72132   ?  157 LEU A CA  1 
ATOM   1240 C  C   . LEU A 1 157 ? 6.31021   6.25173   40.08474  1.000 9.47037   ?  157 LEU A C   1 
ATOM   1241 O  O   . LEU A 1 157 ? 5.70085   7.29596   40.31238  1.000 9.17054   ?  157 LEU A O   1 
ATOM   1242 C  CB  . LEU A 1 157 ? 8.30415   6.05361   41.59974  1.000 7.23259   ?  157 LEU A CB  1 
ATOM   1243 C  CG  . LEU A 1 157 ? 9.83290   6.07128   41.75578  1.000 8.07522   ?  157 LEU A CG  1 
ATOM   1244 C  CD1 . LEU A 1 157 ? 10.24625  5.88866   43.20540  1.000 8.94355   ?  157 LEU A CD1 1 
ATOM   1245 C  CD2 . LEU A 1 157 ? 10.45605  5.00309   40.89854  1.000 8.96236   ?  157 LEU A CD2 1 
ATOM   1246 N  N   . TRP A 1 158 ? 5.70743   5.11653   39.74648  1.000 8.12587   ?  158 TRP A N   1 
ATOM   1247 C  CA  . TRP A 1 158 ? 4.29142   5.04525   39.42507  1.000 6.19322   ?  158 TRP A CA  1 
ATOM   1248 C  C   . TRP A 1 158 ? 3.62895   3.94284   40.22918  1.000 7.01033   ?  158 TRP A C   1 
ATOM   1249 O  O   . TRP A 1 158 ? 4.15558   2.83067   40.32657  1.000 10.06981  ?  158 TRP A O   1 
ATOM   1250 C  CB  . TRP A 1 158 ? 4.06213   4.74151   37.94046  1.000 7.99805   ?  158 TRP A CB  1 
ATOM   1251 C  CG  . TRP A 1 158 ? 4.74312   5.65512   36.99374  1.000 8.58357   ?  158 TRP A CG  1 
ATOM   1252 C  CD1 . TRP A 1 158 ? 6.09518   5.82687   36.83398  1.000 8.36934   ?  158 TRP A CD1 1 
ATOM   1253 C  CD2 . TRP A 1 158 ? 4.11199   6.49363   36.02186  1.000 9.64004   ?  158 TRP A CD2 1 
ATOM   1254 N  NE1 . TRP A 1 158 ? 6.33684   6.73758   35.82968  1.000 9.12843   ?  158 TRP A NE1 1 
ATOM   1255 C  CE2 . TRP A 1 158 ? 5.13592   7.16566   35.32161  1.000 11.39428  ?  158 TRP A CE2 1 
ATOM   1256 C  CE3 . TRP A 1 158 ? 2.77663   6.74154   35.67462  1.000 11.61129  ?  158 TRP A CE3 1 
ATOM   1257 C  CZ2 . TRP A 1 158 ? 4.87092   8.06404   34.28870  1.000 14.76331  ?  158 TRP A CZ2 1 
ATOM   1258 C  CZ3 . TRP A 1 158 ? 2.51477   7.64730   34.64590  1.000 12.47945  ?  158 TRP A CZ3 1 
ATOM   1259 C  CH2 . TRP A 1 158 ? 3.56218   8.29637   33.96915  1.000 16.80084  ?  158 TRP A CH2 1 
ATOM   1260 N  N   . LYS A 1 159 ? 2.46423   4.23658   40.78232  1.000 9.66222   ?  159 LYS A N   1 
ATOM   1261 C  CA  . LYS A 1 159 ? 1.64022   3.15867   41.29098  1.000 8.21798   ?  159 LYS A CA  1 
ATOM   1262 C  C   . LYS A 1 159 ? 1.11928   2.35021   40.10476  1.000 9.10027   ?  159 LYS A C   1 
ATOM   1263 O  O   . LYS A 1 159 ? 0.86640   2.90723   39.03323  1.000 12.10216  ?  159 LYS A O   1 
ATOM   1264 C  CB  . LYS A 1 159 ? 0.49421   3.71678   42.13479  1.000 12.87935  ?  159 LYS A CB  1 
ATOM   1265 C  CG  . LYS A 1 159 ? 0.99021   4.56651   43.33094  1.000 11.34122  ?  159 LYS A CG  1 
ATOM   1266 C  CD  . LYS A 1 159 ? 1.74879   3.71388   44.34806  1.000 19.62313  ?  159 LYS A CD  1 
ATOM   1267 C  CE  . LYS A 1 159 ? 2.21089   4.53405   45.57350  1.000 28.18898  ?  159 LYS A CE  1 
ATOM   1268 N  NZ  . LYS A 1 159 ? 1.08978   4.93722   46.47812  1.000 28.97126  ?  159 LYS A NZ  1 
ATOM   1269 N  N   . PRO A 1 160 ? 0.99518   1.03459   40.25271  1.000 11.15395  ?  160 PRO A N   1 
ATOM   1270 C  CA  . PRO A 1 160 ? 0.63590   0.19471   39.10045  1.000 13.27314  ?  160 PRO A CA  1 
ATOM   1271 C  C   . PRO A 1 160 ? -0.67332  0.64732   38.46576  1.000 17.62099  ?  160 PRO A C   1 
ATOM   1272 O  O   . PRO A 1 160 ? -1.66520  0.89207   39.15454  1.000 13.04485  ?  160 PRO A O   1 
ATOM   1273 C  CB  . PRO A 1 160 ? 0.52370   -1.20514  39.71231  1.000 20.92658  ?  160 PRO A CB  1 
ATOM   1274 C  CG  . PRO A 1 160 ? 1.44521   -1.15264  40.89848  1.000 20.89034  ?  160 PRO A CG  1 
ATOM   1275 C  CD  . PRO A 1 160 ? 1.24547   0.23237   41.46429  1.000 13.25630  ?  160 PRO A CD  1 
ATOM   1276 N  N   . GLY A 1 161 ? -0.64817  0.81123   37.14143  1.000 16.03136  ?  161 GLY A N   1 
ATOM   1277 C  CA  . GLY A 1 161 ? -1.80581  1.24991   36.39561  1.000 16.35099  ?  161 GLY A CA  1 
ATOM   1278 C  C   . GLY A 1 161 ? -2.12910  2.73261   36.46071  1.000 16.56247  ?  161 GLY A C   1 
ATOM   1279 O  O   . GLY A 1 161 ? -3.06497  3.16711   35.77872  1.000 11.95690  ?  161 GLY A O   1 
ATOM   1280 N  N   . ALA A 1 162 ? -1.40277  3.52731   37.24826  1.000 9.90711   ?  162 ALA A N   1 
ATOM   1281 C  CA  . ALA A 1 162 ? -1.70189  4.95401   37.37271  1.000 9.84870   ?  162 ALA A CA  1 
ATOM   1282 C  C   . ALA A 1 162 ? -1.35272  5.71624   36.09300  1.000 12.27840  ?  162 ALA A C   1 
ATOM   1283 O  O   . ALA A 1 162 ? -0.51736  5.29141   35.29256  1.000 15.16723  ?  162 ALA A O   1 
ATOM   1284 C  CB  . ALA A 1 162 ? -0.93820  5.57151   38.54585  1.000 12.80697  ?  162 ALA A CB  1 
ATOM   1285 N  N   . ASP A 1 163 ? -2.00890  6.86130   35.90289  1.000 14.55370  ?  163 ASP A N   1 
ATOM   1286 C  CA  . ASP A 1 163 ? -1.75617  7.68460   34.72621  1.000 16.51403  ?  163 ASP A CA  1 
ATOM   1287 C  C   . ASP A 1 163 ? -0.80640  8.84655   35.00098  1.000 13.86797  ?  163 ASP A C   1 
ATOM   1288 O  O   . ASP A 1 163 ? -0.54296  9.64339   34.09241  1.000 16.13436  ?  163 ASP A O   1 
ATOM   1289 C  CB  . ASP A 1 163 ? -3.07818  8.20675   34.13233  1.000 20.43444  ?  163 ASP A CB  1 
ATOM   1290 C  CG  . ASP A 1 163 ? -3.82734  9.11859   35.07085  1.000 21.34247  ?  163 ASP A CG  1 
ATOM   1291 O  OD1 . ASP A 1 163 ? -3.37112  9.33292   36.21507  1.000 36.16847  ?  163 ASP A OD1 1 
ATOM   1292 O  OD2 . ASP A 1 163 ? -4.89201  9.62574   34.65396  1.000 40.97865  -1 163 ASP A OD2 1 
ATOM   1293 N  N   . ALA A 1 164 ? -0.28371  8.96021   36.21939  1.000 14.21217  ?  164 ALA A N   1 
ATOM   1294 C  CA  . ALA A 1 164 ? 0.70568   9.97264   36.56973  1.000 17.30615  ?  164 ALA A CA  1 
ATOM   1295 C  C   . ALA A 1 164 ? 1.61948   9.36731   37.62643  1.000 9.94909   ?  164 ALA A C   1 
ATOM   1296 O  O   . ALA A 1 164 ? 1.15461   8.56619   38.43596  1.000 12.77535  ?  164 ALA A O   1 
ATOM   1297 C  CB  . ALA A 1 164 ? 0.05977   11.25117  37.12528  1.000 18.77458  ?  164 ALA A CB  1 
ATOM   1298 N  N   . PRO A 1 165 ? 2.89951   9.73335   37.63339  1.000 10.01508  ?  165 PRO A N   1 
ATOM   1299 C  CA  . PRO A 1 165 ? 3.77449   9.24007   38.70766  1.000 7.23511   ?  165 PRO A CA  1 
ATOM   1300 C  C   . PRO A 1 165 ? 3.44008   9.92881   40.01213  1.000 10.75807  ?  165 PRO A C   1 
ATOM   1301 O  O   . PRO A 1 165 ? 2.89640   11.03334  40.03914  1.000 17.81075  ?  165 PRO A O   1 
ATOM   1302 C  CB  . PRO A 1 165 ? 5.17997   9.61768   38.22628  1.000 9.68811   ?  165 PRO A CB  1 
ATOM   1303 C  CG  . PRO A 1 165 ? 4.95557   10.84974  37.37903  1.000 13.29521  ?  165 PRO A CG  1 
ATOM   1304 C  CD  . PRO A 1 165 ? 3.59849   10.65255  36.72213  1.000 9.45019   ?  165 PRO A CD  1 
ATOM   1305 N  N   . PHE A 1 166 ? 3.74905   9.25308   41.11598  1.000 7.76056   ?  166 PHE A N   1 
ATOM   1306 C  CA  . PHE A 1 166 ? 3.53939   9.86836   42.42434  1.000 15.02584  ?  166 PHE A CA  1 
ATOM   1307 C  C   . PHE A 1 166 ? 4.80359   10.49026  42.99491  1.000 18.95905  ?  166 PHE A C   1 
ATOM   1308 O  O   . PHE A 1 166 ? 4.71690   11.27974  43.94062  1.000 14.14139  ?  166 PHE A O   1 
ATOM   1309 C  CB  . PHE A 1 166 ? 2.96860   8.84850   43.42841  1.000 13.95348  ?  166 PHE A CB  1 
ATOM   1310 C  CG  . PHE A 1 166 ? 3.95119   7.79010   43.87386  1.000 7.82385   ?  166 PHE A CG  1 
ATOM   1311 C  CD1 . PHE A 1 166 ? 4.10857   6.62616   43.14158  1.000 9.14819   ?  166 PHE A CD1 1 
ATOM   1312 C  CD2 . PHE A 1 166 ? 4.68059   7.94575   45.05365  1.000 11.11262  ?  166 PHE A CD2 1 
ATOM   1313 C  CE1 . PHE A 1 166 ? 5.01195   5.64165   43.55822  1.000 9.76291   ?  166 PHE A CE1 1 
ATOM   1314 C  CE2 . PHE A 1 166 ? 5.57905   6.98355   45.47626  1.000 16.41789  ?  166 PHE A CE2 1 
ATOM   1315 C  CZ  . PHE A 1 166 ? 5.73877   5.82063   44.73425  1.000 12.78413  ?  166 PHE A CZ  1 
ATOM   1316 N  N   . TRP A 1 167 ? 5.97102   10.16190  42.44759  1.000 12.27739  ?  167 TRP A N   1 
ATOM   1317 C  CA  . TRP A 1 167 ? 7.22466   10.74846  42.90375  1.000 13.10581  ?  167 TRP A CA  1 
ATOM   1318 C  C   . TRP A 1 167 ? 8.12487   10.94185  41.69719  1.000 13.81862  ?  167 TRP A C   1 
ATOM   1319 O  O   . TRP A 1 167 ? 8.12769   10.10415  40.78700  1.000 10.10393  ?  167 TRP A O   1 
ATOM   1320 C  CB  . TRP A 1 167 ? 7.92479   9.85921   43.95241  1.000 10.61713  ?  167 TRP A CB  1 
ATOM   1321 C  CG  . TRP A 1 167 ? 9.24352   10.42291  44.45063  1.000 12.09945  ?  167 TRP A CG  1 
ATOM   1322 C  CD1 . TRP A 1 167 ? 9.43726   11.23345  45.53940  1.000 15.28875  ?  167 TRP A CD1 1 
ATOM   1323 C  CD2 . TRP A 1 167 ? 10.53947  10.23258  43.86078  1.000 13.59206  ?  167 TRP A CD2 1 
ATOM   1324 N  NE1 . TRP A 1 167 ? 10.77032  11.54266  45.66739  1.000 14.00330  ?  167 TRP A NE1 1 
ATOM   1325 C  CE2 . TRP A 1 167 ? 11.46802  10.94358  44.65328  1.000 12.43469  ?  167 TRP A CE2 1 
ATOM   1326 C  CE3 . TRP A 1 167 ? 11.00178  9.52839   42.74382  1.000 13.20506  ?  167 TRP A CE3 1 
ATOM   1327 C  CZ2 . TRP A 1 167 ? 12.83046  10.97531  44.36389  1.000 9.49513   ?  167 TRP A CZ2 1 
ATOM   1328 C  CZ3 . TRP A 1 167 ? 12.36076  9.55345   42.45612  1.000 12.56348  ?  167 TRP A CZ3 1 
ATOM   1329 C  CH2 . TRP A 1 167 ? 13.26114  10.26744  43.27463  1.000 11.91759  ?  167 TRP A CH2 1 
ATOM   1330 N  N   . SER A 1 168 ? 8.87702   12.05131  41.69098  1.000 10.87041  ?  168 SER A N   1 
ATOM   1331 C  CA  . SER A 1 168 ? 9.81488   12.35456  40.62067  1.000 12.03797  ?  168 SER A CA  1 
ATOM   1332 C  C   . SER A 1 168 ? 11.09041  12.91497  41.21650  1.000 11.57233  ?  168 SER A C   1 
ATOM   1333 O  O   . SER A 1 168 ? 11.05804  13.66245  42.20218  1.000 13.82486  ?  168 SER A O   1 
ATOM   1334 C  CB  . SER A 1 168 ? 9.24652   13.38075  39.60670  1.000 14.05365  ?  168 SER A CB  1 
ATOM   1335 O  OG  . SER A 1 168 ? 8.07555   12.87635  38.98723  1.000 33.77163  ?  168 SER A OG  1 
ATOM   1336 N  N   . GLY A 1 169 ? 12.21438  12.58952  40.57353  1.000 10.61470  ?  169 GLY A N   1 
ATOM   1337 C  CA  . GLY A 1 169 ? 13.49005  13.15145  40.97063  1.000 11.52040  ?  169 GLY A CA  1 
ATOM   1338 C  C   . GLY A 1 169 ? 14.60335  12.83321  40.00064  1.000 10.39912  ?  169 GLY A C   1 
ATOM   1339 O  O   . GLY A 1 169 ? 14.67821  11.71985  39.47489  1.000 10.39400  ?  169 GLY A O   1 
ATOM   1340 N  N   . THR A 1 170 ? 15.48127  13.80047  39.75344  1.000 11.10509  ?  170 THR A N   1 
ATOM   1341 C  CA  . THR A 1 170 ? 16.61361  13.60275  38.85233  1.000 8.00288   ?  170 THR A CA  1 
ATOM   1342 C  C   . THR A 1 170 ? 17.79522  13.13785  39.68878  1.000 11.30783  ?  170 THR A C   1 
ATOM   1343 O  O   . THR A 1 170 ? 18.36091  13.91464  40.46995  1.000 10.01531  ?  170 THR A O   1 
ATOM   1344 C  CB  . THR A 1 170 ? 16.94812  14.88953  38.10451  1.000 11.16306  ?  170 THR A CB  1 
ATOM   1345 O  OG1 . THR A 1 170 ? 15.80195  15.31613  37.36365  1.000 9.71467   ?  170 THR A OG1 1 
ATOM   1346 C  CG2 . THR A 1 170 ? 18.09923  14.66548  37.16210  1.000 8.04303   ?  170 THR A CG2 1 
ATOM   1347 N  N   . LEU A 1 171 ? 18.15460  11.87552  39.55886  1.000 6.82058   ?  171 LEU A N   1 
ATOM   1348 C  CA  . LEU A 1 171 ? 19.21694  11.32146  40.38025  1.000 7.48814   ?  171 LEU A CA  1 
ATOM   1349 C  C   . LEU A 1 171 ? 20.56176  11.76658  39.84063  1.000 7.11837   ?  171 LEU A C   1 
ATOM   1350 O  O   . LEU A 1 171 ? 20.78879  11.75717  38.62747  1.000 6.77600   ?  171 LEU A O   1 
ATOM   1351 C  CB  . LEU A 1 171 ? 19.13822  9.79699   40.39708  1.000 5.93813   ?  171 LEU A CB  1 
ATOM   1352 C  CG  . LEU A 1 171 ? 17.87247  9.18765   40.99545  1.000 10.21676  ?  171 LEU A CG  1 
ATOM   1353 C  CD1 . LEU A 1 171 ? 17.96330  7.69317   40.80246  1.000 9.11252   ?  171 LEU A CD1 1 
ATOM   1354 C  CD2 . LEU A 1 171 ? 17.72597  9.53026   42.48493  1.000 10.49091  ?  171 LEU A CD2 1 
ATOM   1355 N  N   . GLU A 1 172 ? 21.44632  12.17315  40.74970  1.000 8.23686   ?  172 GLU A N   1 
ATOM   1356 C  CA  . GLU A 1 172 ? 22.74500  12.72351  40.38555  1.000 8.40540   ?  172 GLU A CA  1 
ATOM   1357 C  C   . GLU A 1 172 ? 23.86299  11.76003  40.74823  1.000 6.65154   ?  172 GLU A C   1 
ATOM   1358 O  O   . GLU A 1 172 ? 23.65665  10.78200  41.46262  1.000 9.70701   ?  172 GLU A O   1 
ATOM   1359 C  CB  . GLU A 1 172 ? 22.99425  14.07158  41.08062  1.000 10.77777  ?  172 GLU A CB  1 
ATOM   1360 C  CG  . GLU A 1 172 ? 21.89602  15.08872  40.89580  1.000 14.73255  ?  172 GLU A CG  1 
ATOM   1361 C  CD  . GLU A 1 172 ? 21.70503  15.51026  39.46198  1.000 14.39920  ?  172 GLU A CD  1 
ATOM   1362 O  OE1 . GLU A 1 172 ? 22.53170  15.12172  38.61051  1.000 12.29710  ?  172 GLU A OE1 1 
ATOM   1363 O  OE2 . GLU A 1 172 ? 20.72418  16.24876  39.20030  1.000 13.37635  -1 172 GLU A OE2 1 
ATOM   1364 N  N   . ALA A 1 173 ? 25.05475  12.04385  40.21638  1.000 8.86449   ?  173 ALA A N   1 
ATOM   1365 C  CA  . ALA A 1 173 ? 26.20177  11.18925  40.47462  1.000 8.75982   ?  173 ALA A CA  1 
ATOM   1366 C  C   . ALA A 1 173 ? 26.39219  11.06676  41.97788  1.000 9.08143   ?  173 ALA A C   1 
ATOM   1367 O  O   . ALA A 1 173 ? 26.30894  12.05543  42.71049  1.000 10.71855  ?  173 ALA A O   1 
ATOM   1368 C  CB  . ALA A 1 173 ? 27.45769  11.76178  39.81734  1.000 11.39347  ?  173 ALA A CB  1 
ATOM   1369 N  N   . GLY A 1 174 ? 26.55599  9.84542   42.44585  1.000 8.37825   ?  174 GLY A N   1 
ATOM   1370 C  CA  . GLY A 1 174 ? 26.62985  9.60023   43.86862  1.000 14.63432  ?  174 GLY A CA  1 
ATOM   1371 C  C   . GLY A 1 174 ? 25.32415  9.20200   44.52468  1.000 14.56740  ?  174 GLY A C   1 
ATOM   1372 O  O   . GLY A 1 174 ? 25.32356  8.92884   45.72982  1.000 12.13178  ?  174 GLY A O   1 
ATOM   1373 N  N   . GLN A 1 175 ? 24.21884  9.15925   43.78476  1.000 6.44174   ?  175 GLN A N   1 
ATOM   1374 C  CA  . GLN A 1 175 ? 22.92974  8.75037   44.32585  1.000 5.72131   ?  175 GLN A CA  1 
ATOM   1375 C  C   . GLN A 1 175 ? 22.48783  7.42652   43.72260  1.000 9.16931   ?  175 GLN A C   1 
ATOM   1376 O  O   . GLN A 1 175 ? 22.85197  7.08859   42.59603  1.000 7.89984   ?  175 GLN A O   1 
ATOM   1377 C  CB  . GLN A 1 175 ? 21.85559  9.80991   44.05075  1.000 6.26312   ?  175 GLN A CB  1 
ATOM   1378 C  CG  . GLN A 1 175 ? 22.13852  11.18006  44.68504  1.000 10.00998  ?  175 GLN A CG  1 
ATOM   1379 C  CD  . GLN A 1 175 ? 20.95046  12.09796  44.58092  1.000 14.38646  ?  175 GLN A CD  1 
ATOM   1380 O  OE1 . GLN A 1 175 ? 20.62105  12.55400  43.50183  1.000 9.47556   ?  175 GLN A OE1 1 
ATOM   1381 N  NE2 . GLN A 1 175 ? 20.28910  12.36054  45.70304  1.000 14.12755  ?  175 GLN A NE2 1 
ATOM   1382 N  N   . ALA A 1 176 ? 21.68268  6.69110   44.48680  1.000 7.33993   ?  176 ALA A N   1 
ATOM   1383 C  CA  . ALA A 1 176 ? 21.01137  5.49820   43.99219  1.000 7.37325   ?  176 ALA A CA  1 
ATOM   1384 C  C   . ALA A 1 176 ? 19.58247  5.49302   44.51039  1.000 10.47991  ?  176 ALA A C   1 
ATOM   1385 O  O   . ALA A 1 176 ? 19.31382  5.98236   45.61129  1.000 10.67187  ?  176 ALA A O   1 
ATOM   1386 C  CB  . ALA A 1 176 ? 21.72988  4.21196   44.43906  1.000 5.96622   ?  176 ALA A CB  1 
ATOM   1387 N  N   . VAL A 1 177 ? 18.66450  4.94854   43.71409  1.000 10.33596  ?  177 VAL A N   1 
ATOM   1388 C  CA  . VAL A 1 177 ? 17.30996  4.66900   44.17391  1.000 7.85675   ?  177 VAL A CA  1 
ATOM   1389 C  C   . VAL A 1 177 ? 17.16912  3.16345   44.33520  1.000 9.13936   ?  177 VAL A C   1 
ATOM   1390 O  O   . VAL A 1 177 ? 17.67504  2.38502   43.51871  1.000 7.76400   ?  177 VAL A O   1 
ATOM   1391 C  CB  . VAL A 1 177 ? 16.21288  5.24188   43.24891  1.000 9.00374   ?  177 VAL A CB  1 
ATOM   1392 C  CG1 . VAL A 1 177 ? 16.21768  4.59609   41.83861  1.000 8.06991   ?  177 VAL A CG1 1 
ATOM   1393 C  CG2 . VAL A 1 177 ? 14.86520  5.10218   43.93346  1.000 7.73925   ?  177 VAL A CG2 1 
ATOM   1394 N  N   . LEU A 1 178 ? 16.54401  2.76142   45.43476  1.000 9.21871   ?  178 LEU A N   1 
ATOM   1395 C  CA  . LEU A 1 178 ? 16.16325  1.38099   45.70003  1.000 8.97518   ?  178 LEU A CA  1 
ATOM   1396 C  C   . LEU A 1 178 ? 14.64714  1.28328   45.56317  1.000 11.10049  ?  178 LEU A C   1 
ATOM   1397 O  O   . LEU A 1 178 ? 13.93088  2.13672   46.09244  1.000 11.12284  ?  178 LEU A O   1 
ATOM   1398 C  CB  . LEU A 1 178 ? 16.59992  0.97133   47.10696  1.000 7.51977   ?  178 LEU A CB  1 
ATOM   1399 C  CG  . LEU A 1 178 ? 18.09160  1.12393   47.39222  1.000 11.61483  ?  178 LEU A CG  1 
ATOM   1400 C  CD1 . LEU A 1 178 ? 18.37245  1.01142   48.86258  1.000 16.86556  ?  178 LEU A CD1 1 
ATOM   1401 C  CD2 . LEU A 1 178 ? 18.80013  0.01991   46.68169  1.000 16.57115  ?  178 LEU A CD2 1 
ATOM   1402 N  N   . LEU A 1 179 ? 14.16245  0.26147   44.85326  1.000 8.00267   ?  179 LEU A N   1 
ATOM   1403 C  CA  . LEU A 1 179 ? 12.74850  0.15901   44.49834  1.000 14.72411  ?  179 LEU A CA  1 
ATOM   1404 C  C   . LEU A 1 179 ? 12.18078  -1.22891  44.76529  1.000 13.17110  ?  179 LEU A C   1 
ATOM   1405 O  O   . LEU A 1 179 ? 12.80508  -2.24451  44.43640  1.000 8.36301   ?  179 LEU A O   1 
ATOM   1406 C  CB  . LEU A 1 179 ? 12.50449  0.44146   43.01339  1.000 12.94925  ?  179 LEU A CB  1 
ATOM   1407 C  CG  . LEU A 1 179 ? 13.08529  1.66866   42.35726  1.000 20.64265  ?  179 LEU A CG  1 
ATOM   1408 C  CD1 . LEU A 1 179 ? 12.81670  1.54065   40.88990  1.000 16.49280  ?  179 LEU A CD1 1 
ATOM   1409 C  CD2 . LEU A 1 179 ? 12.36022  2.85748   42.92037  1.000 23.09132  ?  179 LEU A CD2 1 
ATOM   1410 N  N   . ASP A 1 180 ? 10.96787  -1.25017  45.31699  1.000 6.46797   ?  180 ASP A N   1 
ATOM   1411 C  CA  . ASP A 1 180 ? 10.07613  -2.40733  45.25449  1.000 10.52071  ?  180 ASP A CA  1 
ATOM   1412 C  C   . ASP A 1 180 ? 9.61178   -2.54755  43.81058  1.000 8.21717   ?  180 ASP A C   1 
ATOM   1413 O  O   . ASP A 1 180 ? 8.70740   -1.83876  43.37244  1.000 13.23372  ?  180 ASP A O   1 
ATOM   1414 C  CB  . ASP A 1 180 ? 8.90264   -2.19926  46.20925  1.000 10.78787  ?  180 ASP A CB  1 
ATOM   1415 C  CG  . ASP A 1 180 ? 7.82979   -3.28228  46.09393  1.000 19.21041  ?  180 ASP A CG  1 
ATOM   1416 O  OD1 . ASP A 1 180 ? 7.99166   -4.27560  45.34124  1.000 12.56097  ?  180 ASP A OD1 1 
ATOM   1417 O  OD2 . ASP A 1 180 ? 6.80392   -3.12308  46.77713  1.000 18.21637  -1 180 ASP A OD2 1 
ATOM   1418 N  N   . ASP A 1 181 ? 10.22500  -3.47179  43.06528  1.000 9.24235   ?  181 ASP A N   1 
ATOM   1419 C  CA  . ASP A 1 181 ? 9.98382   -3.62399  41.63692  1.000 9.51874   ?  181 ASP A CA  1 
ATOM   1420 C  C   . ASP A 1 181 ? 8.65027   -4.30390  41.33652  1.000 12.83080  ?  181 ASP A C   1 
ATOM   1421 O  O   . ASP A 1 181 ? 8.21692   -4.30972  40.18070  1.000 9.25394   ?  181 ASP A O   1 
ATOM   1422 C  CB  . ASP A 1 181 ? 11.15361  -4.40301  41.01449  1.000 10.31049  ?  181 ASP A CB  1 
ATOM   1423 C  CG  . ASP A 1 181 ? 11.12804  -4.42135  39.48716  1.000 7.34089   ?  181 ASP A CG  1 
ATOM   1424 O  OD1 . ASP A 1 181 ? 10.85740  -3.37674  38.85269  1.000 7.90492   ?  181 ASP A OD1 1 
ATOM   1425 O  OD2 . ASP A 1 181 ? 11.43056  -5.48434  38.92235  1.000 9.91858   -1 181 ASP A OD2 1 
ATOM   1426 N  N   . ARG A 1 182 ? 7.97828   -4.85119  42.34512  1.000 9.27234   ?  182 ARG A N   1 
ATOM   1427 C  CA  . ARG A 1 182 ? 6.65144   -5.43933  42.17592  1.000 10.42001  ?  182 ARG A CA  1 
ATOM   1428 C  C   . ARG A 1 182 ? 5.51937   -4.46457  42.49677  1.000 11.67424  ?  182 ARG A C   1 
ATOM   1429 O  O   . ARG A 1 182 ? 4.54966   -4.37597  41.73579  1.000 11.47525  ?  182 ARG A O   1 
ATOM   1430 C  CB  . ARG A 1 182 ? 6.52970   -6.68799  43.05892  1.000 9.17865   ?  182 ARG A CB  1 
ATOM   1431 C  CG  . ARG A 1 182 ? 7.43392   -7.81904  42.58332  1.000 11.22101  ?  182 ARG A CG  1 
ATOM   1432 C  CD  . ARG A 1 182 ? 7.55395   -8.94488  43.59662  1.000 14.67638  ?  182 ARG A CD  1 
ATOM   1433 N  NE  . ARG A 1 182 ? 8.29038   -10.07149 43.02747  1.000 15.33584  ?  182 ARG A NE  1 
ATOM   1434 C  CZ  . ARG A 1 182 ? 8.59440   -11.17956 43.68748  1.000 17.74998  ?  182 ARG A CZ  1 
ATOM   1435 N  NH1 . ARG A 1 182 ? 8.29709   -11.32452 44.97189  1.000 14.71487  ?  182 ARG A NH1 1 
ATOM   1436 N  NH2 . ARG A 1 182 ? 9.20941   -12.16596 43.04208  1.000 13.39474  ?  182 ARG A NH2 1 
ATOM   1437 N  N   . GLY A 1 183 ? 5.63349   -3.72022  43.59969  1.000 10.72048  ?  183 GLY A N   1 
ATOM   1438 C  CA  . GLY A 1 183 ? 4.59004   -2.79728  44.00658  1.000 16.27938  ?  183 GLY A CA  1 
ATOM   1439 C  C   . GLY A 1 183 ? 4.60240   -1.45920  43.29892  1.000 13.28002  ?  183 GLY A C   1 
ATOM   1440 O  O   . GLY A 1 183 ? 3.58797   -0.76393  43.32440  1.000 10.91144  ?  183 GLY A O   1 
ATOM   1441 N  N   . LEU A 1 184 ? 5.72804   -1.06723  42.69565  1.000 10.22537  ?  184 LEU A N   1 
ATOM   1442 C  CA  . LEU A 1 184 ? 5.84105   0.16429   41.91991  1.000 9.59543   ?  184 LEU A CA  1 
ATOM   1443 C  C   . LEU A 1 184 ? 6.31268   -0.15278  40.50698  1.000 8.94693   ?  184 LEU A C   1 
ATOM   1444 O  O   . LEU A 1 184 ? 6.95060   -1.17885  40.26381  1.000 11.12115  ?  184 LEU A O   1 
ATOM   1445 C  CB  . LEU A 1 184 ? 6.84946   1.14565   42.54933  1.000 12.25860  ?  184 LEU A CB  1 
ATOM   1446 C  CG  . LEU A 1 184 ? 6.77181   1.56185   43.99941  1.000 21.52508  ?  184 LEU A CG  1 
ATOM   1447 C  CD1 . LEU A 1 184 ? 7.92757   2.52105   44.28108  1.000 13.02433  ?  184 LEU A CD1 1 
ATOM   1448 C  CD2 . LEU A 1 184 ? 5.42905   2.22535   44.26638  1.000 16.75330  ?  184 LEU A CD2 1 
ATOM   1449 N  N   . ALA A 1 185 ? 6.01515   0.75039   39.57396  1.000 9.41517   ?  185 ALA A N   1 
ATOM   1450 C  CA  . ALA A 1 185 ? 6.60866   0.73860   38.24307  1.000 7.67101   ?  185 ALA A CA  1 
ATOM   1451 C  C   . ALA A 1 185 ? 7.43420   2.01154   38.07945  1.000 8.82024   ?  185 ALA A C   1 
ATOM   1452 O  O   . ALA A 1 185 ? 7.29594   2.96768   38.84473  1.000 8.32326   ?  185 ALA A O   1 
ATOM   1453 C  CB  . ALA A 1 185 ? 5.53531   0.64567   37.14545  1.000 7.25723   ?  185 ALA A CB  1 
ATOM   1454 N  N   . HIS A 1 186 ? 8.31833   2.03092   37.08364  1.000 6.99203   ?  186 HIS A N   1 
ATOM   1455 C  CA  . HIS A 1 186 ? 9.16772   3.19841   36.91048  1.000 7.26950   ?  186 HIS A CA  1 
ATOM   1456 C  C   . HIS A 1 186 ? 9.36571   3.52043   35.43447  1.000 7.29998   ?  186 HIS A C   1 
ATOM   1457 O  O   . HIS A 1 186 ? 9.22011   2.66627   34.55735  1.000 7.33037   ?  186 HIS A O   1 
ATOM   1458 C  CB  . HIS A 1 186 ? 10.52344  3.00947   37.60633  1.000 5.83280   ?  186 HIS A CB  1 
ATOM   1459 C  CG  . HIS A 1 186 ? 11.29280  1.80666   37.14667  1.000 6.25014   ?  186 HIS A CG  1 
ATOM   1460 N  ND1 . HIS A 1 186 ? 11.00329  0.52768   37.58134  1.000 6.32733   ?  186 HIS A ND1 1 
ATOM   1461 C  CD2 . HIS A 1 186 ? 12.35612  1.68997   36.31159  1.000 5.84905   ?  186 HIS A CD2 1 
ATOM   1462 C  CE1 . HIS A 1 186 ? 11.84731  -0.32341  37.02617  1.000 9.12877   ?  186 HIS A CE1 1 
ATOM   1463 N  NE2 . HIS A 1 186 ? 12.68402  0.35638   36.25934  1.000 7.50714   ?  186 HIS A NE2 1 
ATOM   1464 N  N   . ASP A 1 187 ? 9.67762   4.78875   35.16706  1.000 7.29455   ?  187 ASP A N   1 
ATOM   1465 C  CA  . ASP A 1 187 ? 10.34209  5.14866   33.92569  1.000 6.45867   ?  187 ASP A CA  1 
ATOM   1466 C  C   . ASP A 1 187 ? 11.29602  6.29622   34.22496  1.000 6.89609   ?  187 ASP A C   1 
ATOM   1467 O  O   . ASP A 1 187 ? 11.40970  6.75731   35.36642  1.000 9.68346   ?  187 ASP A O   1 
ATOM   1468 C  CB  . ASP A 1 187 ? 9.33225   5.46505   32.79640  1.000 7.45643   ?  187 ASP A CB  1 
ATOM   1469 C  CG  . ASP A 1 187 ? 8.71802   6.85712   32.89746  1.000 13.38911  ?  187 ASP A CG  1 
ATOM   1470 O  OD1 . ASP A 1 187 ? 8.60424   7.42010   34.01729  1.000 9.93972   ?  187 ASP A OD1 1 
ATOM   1471 O  OD2 . ASP A 1 187 ? 8.32954   7.38236   31.82629  1.000 10.21669  -1 187 ASP A OD2 1 
ATOM   1472 N  N   . VAL A 1 188 ? 12.04313  6.71379   33.21122  1.000 5.97687   ?  188 VAL A N   1 
ATOM   1473 C  CA  . VAL A 1 188 ? 12.97291  7.82973   33.35016  1.000 5.44294   ?  188 VAL A CA  1 
ATOM   1474 C  C   . VAL A 1 188 ? 12.89825  8.65606   32.07123  1.000 5.74539   ?  188 VAL A C   1 
ATOM   1475 O  O   . VAL A 1 188 ? 12.85904  8.09783   30.96994  1.000 7.19582   ?  188 VAL A O   1 
ATOM   1476 C  CB  . VAL A 1 188 ? 14.42061  7.34533   33.60497  1.000 9.24499   ?  188 VAL A CB  1 
ATOM   1477 C  CG1 . VAL A 1 188 ? 15.29400  8.53247   33.98513  1.000 9.73544   ?  188 VAL A CG1 1 
ATOM   1478 C  CG2 . VAL A 1 188 ? 14.48659  6.27202   34.71753  1.000 7.87816   ?  188 VAL A CG2 1 
ATOM   1479 N  N   . THR A 1 189 ? 12.87611  9.98140   32.20655  1.000 5.12471   ?  189 THR A N   1 
ATOM   1480 C  CA  . THR A 1 189 ? 12.86015  10.80602  31.01148  1.000 8.87974   ?  189 THR A CA  1 
ATOM   1481 C  C   . THR A 1 189 ? 14.21294  10.72889  30.31122  1.000 6.62071   ?  189 THR A C   1 
ATOM   1482 O  O   . THR A 1 189 ? 15.24882  10.48133  30.94138  1.000 5.62725   ?  189 THR A O   1 
ATOM   1483 C  CB  . THR A 1 189 ? 12.49676  12.25787  31.34482  1.000 4.99581   ?  189 THR A CB  1 
ATOM   1484 O  OG1 . THR A 1 189 ? 13.51774  12.84004  32.16129  1.000 8.00058   ?  189 THR A OG1 1 
ATOM   1485 C  CG2 . THR A 1 189 ? 11.15946  12.31516  32.10456  1.000 6.83441   ?  189 THR A CG2 1 
ATOM   1486 N  N   . ASP A 1 190 ? 14.18836  10.92238  28.99001  1.000 8.07264   ?  190 ASP A N   1 
ATOM   1487 C  CA  . ASP A 1 190 ? 15.39874  10.86458  28.17481  1.000 8.17542   ?  190 ASP A CA  1 
ATOM   1488 C  C   . ASP A 1 190 ? 16.46022  11.81194  28.70828  1.000 8.18810   ?  190 ASP A C   1 
ATOM   1489 O  O   . ASP A 1 190 ? 16.15646  12.88894  29.22045  1.000 8.46182   ?  190 ASP A O   1 
ATOM   1490 C  CB  . ASP A 1 190 ? 15.10870  11.26799  26.73039  1.000 10.25965  ?  190 ASP A CB  1 
ATOM   1491 C  CG  . ASP A 1 190 ? 14.27974  10.24602  25.97730  1.000 13.63598  ?  190 ASP A CG  1 
ATOM   1492 O  OD1 . ASP A 1 190 ? 13.92568  9.19581   26.55807  1.000 8.09315   ?  190 ASP A OD1 1 
ATOM   1493 O  OD2 . ASP A 1 190 ? 13.98579  10.52337  24.79692  1.000 14.38891  -1 190 ASP A OD2 1 
ATOM   1494 N  N   . VAL A 1 191 ? 17.71839  11.43566  28.54868  1.000 8.72696   ?  191 VAL A N   1 
ATOM   1495 C  CA  . VAL A 1 191 ? 18.77860  12.39120  28.81677  1.000 10.08857  ?  191 VAL A CA  1 
ATOM   1496 C  C   . VAL A 1 191 ? 18.95253  13.27903  27.59217  1.000 13.60893  ?  191 VAL A C   1 
ATOM   1497 O  O   . VAL A 1 191 ? 18.85696  12.82468  26.44355  1.000 7.63965   ?  191 VAL A O   1 
ATOM   1498 C  CB  . VAL A 1 191 ? 20.07983  11.68329  29.22779  1.000 17.62905  ?  191 VAL A CB  1 
ATOM   1499 C  CG1 . VAL A 1 191 ? 20.39566  10.56596  28.33061  1.000 13.27213  ?  191 VAL A CG1 1 
ATOM   1500 C  CG2 . VAL A 1 191 ? 21.18965  12.62904  29.16131  1.000 26.39966  ?  191 VAL A CG2 1 
ATOM   1501 N  N   . LEU A 1 192 ? 19.13016  14.56833  27.84560  1.000 10.33644  ?  192 LEU A N   1 
ATOM   1502 C  CA  . LEU A 1 192 ? 19.28319  15.58618  26.82133  1.000 9.51670   ?  192 LEU A CA  1 
ATOM   1503 C  C   . LEU A 1 192 ? 20.64922  16.24174  26.93424  1.000 9.32814   ?  192 LEU A C   1 
ATOM   1504 O  O   . LEU A 1 192 ? 21.23992  16.29458  28.02122  1.000 12.65614  ?  192 LEU A O   1 
ATOM   1505 C  CB  . LEU A 1 192 ? 18.22696  16.66250  26.97215  1.000 9.80225   ?  192 LEU A CB  1 
ATOM   1506 C  CG  . LEU A 1 192 ? 16.82957  16.08694  27.11717  1.000 14.38006  ?  192 LEU A CG  1 
ATOM   1507 C  CD1 . LEU A 1 192 ? 15.91431  17.20150  27.54726  1.000 14.18456  ?  192 LEU A CD1 1 
ATOM   1508 C  CD2 . LEU A 1 192 ? 16.37359  15.47435  25.79264  1.000 11.53414  ?  192 LEU A CD2 1 
ATOM   1509 N  N   . SER A 1 193 ? 21.14354  16.73894  25.80261  1.000 11.30430  ?  193 SER A N   1 
ATOM   1510 C  CA  . SER A 1 193 ? 22.36577  17.52489  25.81457  1.000 12.60074  ?  193 SER A CA  1 
ATOM   1511 C  C   . SER A 1 193 ? 22.11976  18.78442  26.62107  1.000 14.25093  ?  193 SER A C   1 
ATOM   1512 O  O   . SER A 1 193 ? 21.12335  19.47407  26.40163  1.000 9.40085   ?  193 SER A O   1 
ATOM   1513 C  CB  . SER A 1 193 ? 22.78108  17.89517  24.39299  1.000 11.37165  ?  193 SER A CB  1 
ATOM   1514 O  OG  . SER A 1 193 ? 23.85185  18.82188  24.42390  1.000 12.95166  ?  193 SER A OG  1 
ATOM   1515 N  N   . ALA A 1 194 ? 23.01060  19.08423  27.57199  1.000 7.48680   ?  194 ALA A N   1 
ATOM   1516 C  CA  . ALA A 1 194 ? 22.77788  20.28372  28.37988  1.000 12.16750  ?  194 ALA A CA  1 
ATOM   1517 C  C   . ALA A 1 194 ? 23.03893  21.57437  27.60896  1.000 17.61180  ?  194 ALA A C   1 
ATOM   1518 O  O   . ALA A 1 194 ? 22.45261  22.61631  27.94483  1.000 16.55961  ?  194 ALA A O   1 
ATOM   1519 C  CB  . ALA A 1 194 ? 23.64181  20.26127  29.64484  1.000 11.65898  ?  194 ALA A CB  1 
ATOM   1520 N  N   . ASP A 1 195 ? 23.89747  21.53260  26.58747  1.000 14.34374  ?  195 ASP A N   1 
ATOM   1521 C  CA  . ASP A 1 195 ? 24.29629  22.75618  25.90492  1.000 21.58209  ?  195 ASP A CA  1 
ATOM   1522 C  C   . ASP A 1 195 ? 24.32942  22.61306  24.39020  1.000 20.68864  ?  195 ASP A C   1 
ATOM   1523 O  O   . ASP A 1 195 ? 24.80443  23.52840  23.70804  1.000 16.21070  ?  195 ASP A O   1 
ATOM   1524 C  CB  . ASP A 1 195 ? 25.67568  23.23008  26.39904  1.000 18.03760  ?  195 ASP A CB  1 
ATOM   1525 C  CG  . ASP A 1 195 ? 26.81504  22.34197  25.93089  1.000 21.97526  ?  195 ASP A CG  1 
ATOM   1526 O  OD1 . ASP A 1 195 ? 26.57472  21.25363  25.34102  1.000 17.98745  ?  195 ASP A OD1 1 
ATOM   1527 O  OD2 . ASP A 1 195 ? 27.97970  22.74106  26.15936  1.000 23.73770  -1 195 ASP A OD2 1 
ATOM   1528 N  N   . GLY A 1 196 ? 23.87944  21.49865  23.83241  1.000 14.97945  ?  196 GLY A N   1 
ATOM   1529 C  CA  . GLY A 1 196 ? 23.95029  21.28002  22.40413  1.000 13.38676  ?  196 GLY A CA  1 
ATOM   1530 C  C   . GLY A 1 196 ? 25.04638  20.33063  21.96241  1.000 13.35585  ?  196 GLY A C   1 
ATOM   1531 O  O   . GLY A 1 196 ? 24.98080  19.81780  20.83492  1.000 13.59583  ?  196 GLY A O   1 
ATOM   1532 N  N   . GLY A 1 197 ? 26.04868  20.07856  22.80274  1.000 13.78354  ?  197 GLY A N   1 
ATOM   1533 C  CA  . GLY A 1 197 ? 27.10004  19.14503  22.47460  1.000 11.13862  ?  197 GLY A CA  1 
ATOM   1534 C  C   . GLY A 1 197 ? 26.92373  17.80788  23.17517  1.000 14.95628  ?  197 GLY A C   1 
ATOM   1535 O  O   . GLY A 1 197 ? 25.90917  17.55649  23.82978  1.000 12.92584  ?  197 GLY A O   1 
ATOM   1536 N  N   . PRO A 1 198 ? 27.90920  16.92383  23.04084  1.000 14.35249  ?  198 PRO A N   1 
ATOM   1537 C  CA  . PRO A 1 198 ? 27.78709  15.58522  23.63286  1.000 16.02695  ?  198 PRO A CA  1 
ATOM   1538 C  C   . PRO A 1 198 ? 27.77987  15.61153  25.15704  1.000 17.43251  ?  198 PRO A C   1 
ATOM   1539 O  O   . PRO A 1 198 ? 28.41601  16.44901  25.80172  1.000 13.78348  ?  198 PRO A O   1 
ATOM   1540 C  CB  . PRO A 1 198 ? 29.02052  14.84201  23.10312  1.000 13.14555  ?  198 PRO A CB  1 
ATOM   1541 C  CG  . PRO A 1 198 ? 29.95879  15.89385  22.64900  1.000 28.46892  ?  198 PRO A CG  1 
ATOM   1542 C  CD  . PRO A 1 198 ? 29.10544  17.04686  22.19219  1.000 19.10898  ?  198 PRO A CD  1 
ATOM   1543 N  N   . GLY A 1 199 ? 27.03440  14.66834  25.72526  1.000 8.70742   ?  199 GLY A N   1 
ATOM   1544 C  CA  . GLY A 1 199 ? 26.98225  14.44680  27.15741  1.000 8.72463   ?  199 GLY A CA  1 
ATOM   1545 C  C   . GLY A 1 199 ? 26.67261  12.98694  27.39511  1.000 9.49434   ?  199 GLY A C   1 
ATOM   1546 O  O   . GLY A 1 199 ? 26.30228  12.26333  26.47065  1.000 8.79571   ?  199 GLY A O   1 
ATOM   1547 N  N   . HIS A 1 200 ? 26.83901  12.54474  28.64159  1.000 8.09719   ?  200 HIS A N   1 
ATOM   1548 C  CA  . HIS A 1 200 ? 26.60979  11.12621  28.90042  1.000 10.04546  ?  200 HIS A CA  1 
ATOM   1549 C  C   . HIS A 1 200 ? 26.23390  10.91567  30.35984  1.000 11.06716  ?  200 HIS A C   1 
ATOM   1550 O  O   . HIS A 1 200 ? 26.48057  11.76704  31.21920  1.000 8.44503   ?  200 HIS A O   1 
ATOM   1551 C  CB  . HIS A 1 200 ? 27.82714  10.26760  28.52184  1.000 9.49513   ?  200 HIS A CB  1 
ATOM   1552 C  CG  . HIS A 1 200 ? 29.03630  10.51086  29.37445  1.000 12.03915  ?  200 HIS A CG  1 
ATOM   1553 N  ND1 . HIS A 1 200 ? 29.99393  11.45399  29.05730  1.000 17.53075  ?  200 HIS A ND1 1 
ATOM   1554 C  CD2 . HIS A 1 200 ? 29.44569  9.93235   30.52962  1.000 13.08442  ?  200 HIS A CD2 1 
ATOM   1555 C  CE1 . HIS A 1 200 ? 30.93955  11.44440  29.98229  1.000 13.26948  ?  200 HIS A CE1 1 
ATOM   1556 N  NE2 . HIS A 1 200 ? 30.63344  10.52819  30.88333  1.000 16.41009  ?  200 HIS A NE2 1 
ATOM   1557 N  N   . ARG A 1 201 ? 25.62632  9.75728   30.61900  1.000 8.14735   ?  201 ARG A N   1 
ATOM   1558 C  CA  . ARG A 1 201 ? 25.13423  9.39473   31.94204  1.000 7.09533   ?  201 ARG A CA  1 
ATOM   1559 C  C   . ARG A 1 201 ? 25.49328  7.93392   32.16700  1.000 8.19741   ?  201 ARG A C   1 
ATOM   1560 O  O   . ARG A 1 201 ? 25.08298  7.05762   31.39283  1.000 7.44958   ?  201 ARG A O   1 
ATOM   1561 C  CB  . ARG A 1 201 ? 23.62039  9.62935   32.05124  1.000 5.01904   ?  201 ARG A CB  1 
ATOM   1562 C  CG  . ARG A 1 201 ? 22.93438  9.16278   33.35797  1.000 2.29642   ?  201 ARG A CG  1 
ATOM   1563 C  CD  . ARG A 1 201 ? 21.44290  9.55120   33.29967  1.000 6.60701   ?  201 ARG A CD  1 
ATOM   1564 N  NE  . ARG A 1 201 ? 20.63767  9.16239   34.45372  1.000 4.66382   ?  201 ARG A NE  1 
ATOM   1565 C  CZ  . ARG A 1 201 ? 19.99669  8.00658   34.57280  1.000 6.73063   ?  201 ARG A CZ  1 
ATOM   1566 N  NH1 . ARG A 1 201 ? 20.22896  6.99306   33.74800  1.000 4.08136   ?  201 ARG A NH1 1 
ATOM   1567 N  NH2 . ARG A 1 201 ? 19.07020  7.87867   35.51982  1.000 5.65895   ?  201 ARG A NH2 1 
ATOM   1568 N  N   . ASP A 1 202 ? 26.28011  7.68890   33.21303  1.000 5.68721   ?  202 ASP A N   1 
ATOM   1569 C  CA  . ASP A 1 202 ? 26.84120  6.37994   33.52047  1.000 7.68922   ?  202 ASP A CA  1 
ATOM   1570 C  C   . ASP A 1 202 ? 26.21009  5.85497   34.79702  1.000 6.99662   ?  202 ASP A C   1 
ATOM   1571 O  O   . ASP A 1 202 ? 26.27510  6.52121   35.83989  1.000 6.60033   ?  202 ASP A O   1 
ATOM   1572 C  CB  . ASP A 1 202 ? 28.35306  6.46390   33.72201  1.000 7.69925   ?  202 ASP A CB  1 
ATOM   1573 C  CG  . ASP A 1 202 ? 29.08372  6.95591   32.49494  1.000 10.10385  ?  202 ASP A CG  1 
ATOM   1574 O  OD1 . ASP A 1 202 ? 28.53050  6.81669   31.38178  1.000 9.67029   ?  202 ASP A OD1 1 
ATOM   1575 O  OD2 . ASP A 1 202 ? 30.22826  7.46374   32.65057  1.000 8.88222   -1 202 ASP A OD2 1 
ATOM   1576 N  N   . ILE A 1 203 ? 25.65524  4.64735   34.72985  1.000 8.13367   ?  203 ILE A N   1 
ATOM   1577 C  CA  . ILE A 1 203 ? 24.84339  4.08468   35.80290  1.000 5.09145   ?  203 ILE A CA  1 
ATOM   1578 C  C   . ILE A 1 203 ? 25.17441  2.60948   35.94233  1.000 5.16859   ?  203 ILE A C   1 
ATOM   1579 O  O   . ILE A 1 203 ? 25.81385  2.00882   35.08242  1.000 7.21220   ?  203 ILE A O   1 
ATOM   1580 C  CB  . ILE A 1 203 ? 23.32367  4.24200   35.54724  1.000 6.28917   ?  203 ILE A CB  1 
ATOM   1581 C  CG1 . ILE A 1 203 ? 22.85887  3.33349   34.40731  1.000 6.45937   ?  203 ILE A CG1 1 
ATOM   1582 C  CG2 . ILE A 1 203 ? 22.94664  5.71454   35.25937  1.000 4.63076   ?  203 ILE A CG2 1 
ATOM   1583 C  CD1 . ILE A 1 203 ? 21.31849  3.39389   34.17382  1.000 7.55431   ?  203 ILE A CD1 1 
ATOM   1584 N  N   . VAL A 1 204 ? 24.71901  2.01881   37.04279  1.000 6.41149   ?  204 VAL A N   1 
ATOM   1585 C  CA  . VAL A 1 204 ? 24.68312  0.57131   37.16042  1.000 4.99085   ?  204 VAL A CA  1 
ATOM   1586 C  C   . VAL A 1 204 ? 23.32004  0.19524   37.71652  1.000 8.28174   ?  204 VAL A C   1 
ATOM   1587 O  O   . VAL A 1 204 ? 22.80893  0.84740   38.63175  1.000 6.22889   ?  204 VAL A O   1 
ATOM   1588 C  CB  . VAL A 1 204 ? 25.84084  0.03046   38.01647  1.000 8.57175   ?  204 VAL A CB  1 
ATOM   1589 C  CG1 . VAL A 1 204 ? 25.79309  0.61762   39.42179  1.000 7.67576   ?  204 VAL A CG1 1 
ATOM   1590 C  CG2 . VAL A 1 204 ? 25.82200  -1.51637  38.04333  1.000 8.75340   ?  204 VAL A CG2 1 
ATOM   1591 N  N   . ILE A 1 205 ? 22.70036  -0.81076  37.11362  1.000 5.65512   ?  205 ILE A N   1 
ATOM   1592 C  CA  . ILE A 1 205 ? 21.39308  -1.30390  37.52639  1.000 5.86736   ?  205 ILE A CA  1 
ATOM   1593 C  C   . ILE A 1 205 ? 21.59383  -2.70293  38.05983  1.000 9.35179   ?  205 ILE A C   1 
ATOM   1594 O  O   . ILE A 1 205 ? 22.24267  -3.52898  37.40454  1.000 8.47267   ?  205 ILE A O   1 
ATOM   1595 C  CB  . ILE A 1 205 ? 20.39268  -1.32012  36.36150  1.000 7.93772   ?  205 ILE A CB  1 
ATOM   1596 C  CG1 . ILE A 1 205 ? 20.32189  0.06920   35.71439  1.000 8.53995   ?  205 ILE A CG1 1 
ATOM   1597 C  CG2 . ILE A 1 205 ? 19.02347  -1.78878  36.86205  1.000 7.56317   ?  205 ILE A CG2 1 
ATOM   1598 C  CD1 . ILE A 1 205 ? 19.59164  0.08938   34.36879  1.000 10.26069  ?  205 ILE A CD1 1 
ATOM   1599 N  N   . ILE A 1 206 ? 21.04444  -2.96188  39.24504  1.000 7.24095   ?  206 ILE A N   1 
ATOM   1600 C  CA  . ILE A 1 206 ? 21.15345  -4.25302  39.90365  1.000 6.41599   ?  206 ILE A CA  1 
ATOM   1601 C  C   . ILE A 1 206 ? 19.74745  -4.75292  40.19295  1.000 6.13700   ?  206 ILE A C   1 
ATOM   1602 O  O   . ILE A 1 206 ? 19.00621  -4.12692  40.95819  1.000 7.53704   ?  206 ILE A O   1 
ATOM   1603 C  CB  . ILE A 1 206 ? 21.97233  -4.17600  41.19961  1.000 7.14140   ?  206 ILE A CB  1 
ATOM   1604 C  CG1 . ILE A 1 206 ? 23.36741  -3.58215  40.93472  1.000 7.23515   ?  206 ILE A CG1 1 
ATOM   1605 C  CG2 . ILE A 1 206 ? 22.06333  -5.58018  41.80089  1.000 9.73362   ?  206 ILE A CG2 1 
ATOM   1606 C  CD1 . ILE A 1 206 ? 23.48396  -2.10389  41.27263  1.000 6.54691   ?  206 ILE A CD1 1 
ATOM   1607 N  N   . ALA A 1 207 ? 19.37790  -5.86903  39.57053  1.000 6.79975   ?  207 ALA A N   1 
ATOM   1608 C  CA  . ALA A 1 207 ? 18.05423  -6.45355  39.72189  1.000 8.96864   ?  207 ALA A CA  1 
ATOM   1609 C  C   . ALA A 1 207 ? 18.17797  -7.67140  40.62957  1.000 9.82543   ?  207 ALA A C   1 
ATOM   1610 O  O   . ALA A 1 207 ? 18.98188  -8.56671  40.35559  1.000 8.46910   ?  207 ALA A O   1 
ATOM   1611 C  CB  . ALA A 1 207 ? 17.47055  -6.84141  38.36054  1.000 5.05182   ?  207 ALA A CB  1 
ATOM   1612 N  N   . PHE A 1 208 ? 17.38744  -7.69644  41.69962  1.000 7.74462   ?  208 PHE A N   1 
ATOM   1613 C  CA  . PHE A 1 208 ? 17.48187  -8.69227  42.76345  1.000 10.61989  ?  208 PHE A CA  1 
ATOM   1614 C  C   . PHE A 1 208 ? 16.33860  -9.69359  42.67700  1.000 14.35484  ?  208 PHE A C   1 
ATOM   1615 O  O   . PHE A 1 208 ? 15.16854  -9.30194  42.74064  1.000 9.19481   ?  208 PHE A O   1 
ATOM   1616 C  CB  . PHE A 1 208 ? 17.39364  -8.03725  44.14347  1.000 7.05312   ?  208 PHE A CB  1 
ATOM   1617 C  CG  . PHE A 1 208 ? 18.53835  -7.15285  44.50217  1.000 8.07676   ?  208 PHE A CG  1 
ATOM   1618 C  CD1 . PHE A 1 208 ? 18.60712  -5.84143  44.06101  1.000 7.86217   ?  208 PHE A CD1 1 
ATOM   1619 C  CD2 . PHE A 1 208 ? 19.50370  -7.61153  45.38438  1.000 14.07263  ?  208 PHE A CD2 1 
ATOM   1620 C  CE1 . PHE A 1 208 ? 19.65282  -5.01291  44.45130  1.000 8.18306   ?  208 PHE A CE1 1 
ATOM   1621 C  CE2 . PHE A 1 208 ? 20.54667  -6.79754  45.78632  1.000 14.10671  ?  208 PHE A CE2 1 
ATOM   1622 C  CZ  . PHE A 1 208 ? 20.63336  -5.50951  45.31769  1.000 12.24337  ?  208 PHE A CZ  1 
ATOM   1623 N  N   . SER A 1 209 ? 16.67283  -10.97939 42.63275  1.000 8.59392   ?  209 SER A N   1 
ATOM   1624 C  CA  . SER A 1 209 ? 15.67981  -12.03609 42.68817  1.000 8.47514   ?  209 SER A CA  1 
ATOM   1625 C  C   . SER A 1 209 ? 16.19491  -13.12024 43.62179  1.000 13.40100  ?  209 SER A C   1 
ATOM   1626 O  O   . SER A 1 209 ? 17.40443  -13.35647 43.70840  1.000 7.82164   ?  209 SER A O   1 
ATOM   1627 C  CB  . SER A 1 209 ? 15.39209  -12.63858 41.29823  1.000 7.09330   ?  209 SER A CB  1 
ATOM   1628 O  OG  . SER A 1 209 ? 14.88569  -11.64120 40.41130  1.000 9.70174   ?  209 SER A OG  1 
ATOM   1629 N  N   . ARG A 1 210 ? 15.27901  -13.76943 44.33786  1.000 12.31385  ?  210 ARG A N   1 
ATOM   1630 C  CA  . ARG A 1 210 ? 15.70133  -14.89958 45.16368  1.000 12.03598  ?  210 ARG A CA  1 
ATOM   1631 C  C   . ARG A 1 210 ? 16.27025  -15.99801 44.26786  1.000 13.75954  ?  210 ARG A C   1 
ATOM   1632 O  O   . ARG A 1 210 ? 15.86457  -16.16451 43.11267  1.000 10.78282  ?  210 ARG A O   1 
ATOM   1633 C  CB  . ARG A 1 210 ? 14.53423  -15.40519 46.01056  1.000 8.15864   ?  210 ARG A CB  1 
ATOM   1634 C  CG  . ARG A 1 210 ? 14.05766  -14.35403 47.01314  1.000 12.35167  ?  210 ARG A CG  1 
ATOM   1635 C  CD  . ARG A 1 210 ? 12.66757  -14.63520 47.54707  1.000 14.20049  ?  210 ARG A CD  1 
ATOM   1636 N  NE  . ARG A 1 210 ? 12.14498  -13.46874 48.24969  1.000 14.96995  ?  210 ARG A NE  1 
ATOM   1637 C  CZ  . ARG A 1 210 ? 12.28822  -13.23062 49.54735  1.000 16.33892  ?  210 ARG A CZ  1 
ATOM   1638 N  NH1 . ARG A 1 210 ? 12.82718  -14.12751 50.36532  1.000 14.67535  ?  210 ARG A NH1 1 
ATOM   1639 N  NH2 . ARG A 1 210 ? 11.90189  -12.05343 50.03336  1.000 13.62081  ?  210 ARG A NH2 1 
ATOM   1640 N  N   . TRP A 1 211 ? 17.26761  -16.71954 44.79252  1.000 10.73112  ?  211 TRP A N   1 
ATOM   1641 C  CA  . TRP A 1 211 ? 17.94352  -17.74346 43.99636  1.000 8.49900   ?  211 TRP A CA  1 
ATOM   1642 C  C   . TRP A 1 211 ? 16.96309  -18.76947 43.45929  1.000 6.87956   ?  211 TRP A C   1 
ATOM   1643 O  O   . TRP A 1 211 ? 17.14499  -19.28223 42.34777  1.000 10.01684  ?  211 TRP A O   1 
ATOM   1644 C  CB  . TRP A 1 211 ? 19.02216  -18.45618 44.83426  1.000 11.81338  ?  211 TRP A CB  1 
ATOM   1645 C  CG  . TRP A 1 211 ? 19.76406  -19.49520 44.04617  1.000 11.76078  ?  211 TRP A CG  1 
ATOM   1646 C  CD1 . TRP A 1 211 ? 19.53063  -20.84894 44.01816  1.000 9.30767   ?  211 TRP A CD1 1 
ATOM   1647 C  CD2 . TRP A 1 211 ? 20.84022  -19.25822 43.14060  1.000 9.90731   ?  211 TRP A CD2 1 
ATOM   1648 N  NE1 . TRP A 1 211 ? 20.42170  -21.46027 43.16775  1.000 9.78419   ?  211 TRP A NE1 1 
ATOM   1649 C  CE2 . TRP A 1 211 ? 21.22594  -20.50377 42.60708  1.000 11.16842  ?  211 TRP A CE2 1 
ATOM   1650 C  CE3 . TRP A 1 211 ? 21.52466  -18.11010 42.73420  1.000 12.21590  ?  211 TRP A CE3 1 
ATOM   1651 C  CZ2 . TRP A 1 211 ? 22.25513  -20.62844 41.67699  1.000 17.59345  ?  211 TRP A CZ2 1 
ATOM   1652 C  CZ3 . TRP A 1 211 ? 22.54726  -18.23515 41.81335  1.000 14.36179  ?  211 TRP A CZ3 1 
ATOM   1653 C  CH2 . TRP A 1 211 ? 22.89768  -19.48311 41.29034  1.000 20.13623  ?  211 TRP A CH2 1 
ATOM   1654 N  N   . ALA A 1 212 ? 15.93211  -19.09180 44.24770  1.000 8.99242   ?  212 ALA A N   1 
ATOM   1655 C  CA  . ALA A 1 212 ? 14.90604  -20.04852 43.84813  1.000 12.27864  ?  212 ALA A CA  1 
ATOM   1656 C  C   . ALA A 1 212 ? 14.06803  -19.54513 42.67942  1.000 12.75682  ?  212 ALA A C   1 
ATOM   1657 O  O   . ALA A 1 212 ? 13.39838  -20.34948 42.01954  1.000 14.07371  ?  212 ALA A O   1 
ATOM   1658 C  CB  . ALA A 1 212 ? 13.99524  -20.35642 45.04018  1.000 9.28160   ?  212 ALA A CB  1 
ATOM   1659 N  N   . GLU A 1 213 ? 14.09644  -18.23299 42.41064  1.000 13.00241  ?  213 GLU A N   1 
ATOM   1660 C  CA  . GLU A 1 213 ? 13.42939  -17.60363 41.26892  1.000 14.25074  ?  213 GLU A CA  1 
ATOM   1661 C  C   . GLU A 1 213 ? 14.45153  -16.93561 40.35162  1.000 14.10026  ?  213 GLU A C   1 
ATOM   1662 O  O   . GLU A 1 213 ? 14.16221  -15.91235 39.71634  1.000 10.92359  ?  213 GLU A O   1 
ATOM   1663 C  CB  . GLU A 1 213 ? 12.40072  -16.56946 41.73831  1.000 17.50304  ?  213 GLU A CB  1 
ATOM   1664 C  CG  . GLU A 1 213 ? 11.65864  -16.95051 43.00224  1.000 28.48449  ?  213 GLU A CG  1 
ATOM   1665 C  CD  . GLU A 1 213 ? 10.86205  -15.79701 43.59927  1.000 30.39002  ?  213 GLU A CD  1 
ATOM   1666 O  OE1 . GLU A 1 213 ? 10.04538  -16.05802 44.50808  1.000 47.80180  ?  213 GLU A OE1 1 
ATOM   1667 O  OE2 . GLU A 1 213 ? 11.03915  -14.64481 43.16486  1.000 35.82911  -1 213 GLU A OE2 1 
ATOM   1668 N  N   . LYS A 1 214 ? 15.65148  -17.50585 40.26789  1.000 11.56500  ?  214 LYS A N   1 
ATOM   1669 C  CA  . LYS A 1 214 ? 16.76900  -16.78841 39.67137  1.000 12.97558  ?  214 LYS A CA  1 
ATOM   1670 C  C   . LYS A 1 214 ? 16.54468  -16.54686 38.18408  1.000 14.17134  ?  214 LYS A C   1 
ATOM   1671 O  O   . LYS A 1 214 ? 15.85794  -17.30933 37.49844  1.000 12.39010  ?  214 LYS A O   1 
ATOM   1672 C  CB  . LYS A 1 214 ? 18.07585  -17.54884 39.89996  1.000 10.07545  ?  214 LYS A CB  1 
ATOM   1673 C  CG  . LYS A 1 214 ? 18.14846  -18.93289 39.23167  1.000 13.72725  ?  214 LYS A CG  1 
ATOM   1674 C  CD  . LYS A 1 214 ? 19.43418  -19.66595 39.69997  1.000 13.48088  ?  214 LYS A CD  1 
ATOM   1675 C  CE  . LYS A 1 214 ? 19.66287  -20.99379 38.96064  1.000 20.27874  ?  214 LYS A CE  1 
ATOM   1676 N  NZ  . LYS A 1 214 ? 18.46337  -21.87631 38.98889  1.000 14.90828  ?  214 LYS A NZ  1 
ATOM   1677 N  N   . TRP A 1 215 ? 17.11212  -15.44524 37.69875  1.000 10.44475  ?  215 TRP A N   1 
ATOM   1678 C  CA  . TRP A 1 215 ? 17.07419  -15.06968 36.28440  1.000 8.88997   ?  215 TRP A CA  1 
ATOM   1679 C  C   . TRP A 1 215 ? 18.34379  -15.50893 35.58000  1.000 11.71990  ?  215 TRP A C   1 
ATOM   1680 O  O   . TRP A 1 215 ? 19.01628  -14.73003 34.89363  1.000 10.57164  ?  215 TRP A O   1 
ATOM   1681 C  CB  . TRP A 1 215 ? 16.87611  -13.56612 36.15672  1.000 11.93866  ?  215 TRP A CB  1 
ATOM   1682 C  CG  . TRP A 1 215 ? 15.49463  -13.12543 36.40740  1.000 11.16869  ?  215 TRP A CG  1 
ATOM   1683 C  CD1 . TRP A 1 215 ? 14.70702  -13.41266 37.48696  1.000 13.80784  ?  215 TRP A CD1 1 
ATOM   1684 C  CD2 . TRP A 1 215 ? 14.72984  -12.27369 35.56198  1.000 13.16286  ?  215 TRP A CD2 1 
ATOM   1685 N  NE1 . TRP A 1 215 ? 13.48014  -12.79613 37.35180  1.000 11.94635  ?  215 TRP A NE1 1 
ATOM   1686 C  CE2 . TRP A 1 215 ? 13.47199  -12.09147 36.17481  1.000 13.17341  ?  215 TRP A CE2 1 
ATOM   1687 C  CE3 . TRP A 1 215 ? 14.98710  -11.65166 34.33412  1.000 11.22134  ?  215 TRP A CE3 1 
ATOM   1688 C  CZ2 . TRP A 1 215 ? 12.46818  -11.30300 35.60346  1.000 11.53436  ?  215 TRP A CZ2 1 
ATOM   1689 C  CZ3 . TRP A 1 215 ? 13.99098  -10.86768 33.77067  1.000 14.29548  ?  215 TRP A CZ3 1 
ATOM   1690 C  CH2 . TRP A 1 215 ? 12.74603  -10.70289 34.40545  1.000 10.46367  ?  215 TRP A CH2 1 
ATOM   1691 N  N   . TYR A 1 216 ? 18.66594  -16.79279 35.72820  1.000 8.93908   ?  216 TYR A N   1 
ATOM   1692 C  CA  . TYR A 1 216 ? 19.95525  -17.30908 35.30226  1.000 11.37791  ?  216 TYR A CA  1 
ATOM   1693 C  C   . TYR A 1 216 ? 19.81178  -18.80229 35.05468  1.000 11.42205  ?  216 TYR A C   1 
ATOM   1694 O  O   . TYR A 1 216 ? 19.16676  -19.49438 35.84183  1.000 12.87808  ?  216 TYR A O   1 
ATOM   1695 C  CB  . TYR A 1 216 ? 21.01758  -17.05030 36.37603  1.000 8.12185   ?  216 TYR A CB  1 
ATOM   1696 C  CG  . TYR A 1 216 ? 22.40150  -17.53235 35.99306  1.000 11.16769  ?  216 TYR A CG  1 
ATOM   1697 C  CD1 . TYR A 1 216 ? 23.27739  -16.70714 35.30177  1.000 12.90857  ?  216 TYR A CD1 1 
ATOM   1698 C  CD2 . TYR A 1 216 ? 22.83107  -18.81607 36.32087  1.000 15.36058  ?  216 TYR A CD2 1 
ATOM   1699 C  CE1 . TYR A 1 216 ? 24.54937  -17.14514 34.94350  1.000 10.30917  ?  216 TYR A CE1 1 
ATOM   1700 C  CE2 . TYR A 1 216 ? 24.10208  -19.25760 35.97735  1.000 14.74637  ?  216 TYR A CE2 1 
ATOM   1701 C  CZ  . TYR A 1 216 ? 24.95461  -18.42751 35.28968  1.000 13.69947  ?  216 TYR A CZ  1 
ATOM   1702 O  OH  . TYR A 1 216 ? 26.22037  -18.87835 34.94081  1.000 12.39397  ?  216 TYR A OH  1 
ATOM   1703 N  N   . GLY A 1 217 ? 20.37947  -19.28503 33.96691  1.000 12.88517  ?  217 GLY A N   1 
ATOM   1704 C  CA  . GLY A 1 217 ? 20.39123  -20.71086 33.69539  1.000 20.14446  ?  217 GLY A CA  1 
ATOM   1705 C  C   . GLY A 1 217 ? 19.42834  -21.10223 32.58473  1.000 17.90302  ?  217 GLY A C   1 
ATOM   1706 O  O   . GLY A 1 217 ? 18.68919  -20.28549 32.03603  1.000 12.65789  ?  217 GLY A O   1 
ATOM   1707 N  N   . ASP A 1 218 ? 19.45607  -22.39976 32.26180  1.000 15.35401  ?  218 ASP A N   1 
ATOM   1708 C  CA  . ASP A 1 218 ? 18.71423  -22.90671 31.10631  1.000 13.72265  ?  218 ASP A CA  1 
ATOM   1709 C  C   . ASP A 1 218 ? 17.20782  -22.76209 31.28250  1.000 10.14319  ?  218 ASP A C   1 
ATOM   1710 O  O   . ASP A 1 218 ? 16.49146  -22.46002 30.32108  1.000 14.28512  ?  218 ASP A O   1 
ATOM   1711 C  CB  . ASP A 1 218 ? 19.05246  -24.38000 30.87030  1.000 21.71782  ?  218 ASP A CB  1 
ATOM   1712 C  CG  . ASP A 1 218 ? 20.44341  -24.58863 30.33810  1.000 28.28920  ?  218 ASP A CG  1 
ATOM   1713 O  OD1 . ASP A 1 218 ? 21.00375  -23.65334 29.72198  1.000 25.82394  ?  218 ASP A OD1 1 
ATOM   1714 O  OD2 . ASP A 1 218 ? 20.96469  -25.71055 30.52273  1.000 35.48041  -1 218 ASP A OD2 1 
ATOM   1715 N  N   . GLU A 1 219 ? 16.69863  -23.03323 32.48151  1.000 17.46693  ?  219 GLU A N   1 
ATOM   1716 C  CA  . GLU A 1 219 ? 15.25852  -22.94543 32.71154  1.000 13.73529  ?  219 GLU A CA  1 
ATOM   1717 C  C   . GLU A 1 219 ? 14.76748  -21.50943 32.55015  1.000 17.44051  ?  219 GLU A C   1 
ATOM   1718 O  O   . GLU A 1 219 ? 13.75417  -21.25641 31.88039  1.000 14.14517  ?  219 GLU A O   1 
ATOM   1719 C  CB  . GLU A 1 219 ? 14.93949  -23.47560 34.10675  1.000 19.77510  ?  219 GLU A CB  1 
ATOM   1720 C  CG  . GLU A 1 219 ? 13.46485  -23.58633 34.43634  1.000 30.56357  ?  219 GLU A CG  1 
ATOM   1721 C  CD  . GLU A 1 219 ? 13.22062  -23.94300 35.90686  1.000 30.99535  ?  219 GLU A CD  1 
ATOM   1722 O  OE1 . GLU A 1 219 ? 14.19444  -24.27734 36.62145  1.000 40.43942  ?  219 GLU A OE1 1 
ATOM   1723 O  OE2 . GLU A 1 219 ? 12.05345  -23.87014 36.34696  1.000 38.08805  -1 219 GLU A OE2 1 
ATOM   1724 N  N   . HIS A 1 220 ? 15.46530  -20.55244 33.17227  1.000 14.25901  ?  220 HIS A N   1 
ATOM   1725 C  CA  . HIS A 1 220 ? 15.10364  -19.14738 32.98050  1.000 10.73718  ?  220 HIS A CA  1 
ATOM   1726 C  C   . HIS A 1 220 ? 15.12279  -18.77070 31.50842  1.000 10.71255  ?  220 HIS A C   1 
ATOM   1727 O  O   . HIS A 1 220 ? 14.17490  -18.15795 31.00413  1.000 16.35543  ?  220 HIS A O   1 
ATOM   1728 C  CB  . HIS A 1 220 ? 16.04045  -18.21418 33.75024  1.000 8.86685   ?  220 HIS A CB  1 
ATOM   1729 C  CG  . HIS A 1 220 ? 15.93261  -16.78630 33.30079  1.000 11.01216  ?  220 HIS A CG  1 
ATOM   1730 N  ND1 . HIS A 1 220 ? 14.89194  -15.96747 33.68352  1.000 10.26583  ?  220 HIS A ND1 1 
ATOM   1731 C  CD2 . HIS A 1 220 ? 16.70603  -16.04816 32.46657  1.000 10.79884  ?  220 HIS A CD2 1 
ATOM   1732 C  CE1 . HIS A 1 220 ? 15.03597  -14.78038 33.11695  1.000 11.36647  ?  220 HIS A CE1 1 
ATOM   1733 N  NE2 . HIS A 1 220 ? 16.12883  -14.80221 32.37353  1.000 8.83838   ?  220 HIS A NE2 1 
ATOM   1734 N  N   . ASP A 1 221 ? 16.21485  -19.08630 30.80725  1.000 11.69240  ?  221 ASP A N   1 
ATOM   1735 C  CA  . ASP A 1 221 ? 16.30533  -18.70240 29.40087  1.000 12.09556  ?  221 ASP A CA  1 
ATOM   1736 C  C   . ASP A 1 221 ? 15.12903  -19.26476 28.60621  1.000 15.70684  ?  221 ASP A C   1 
ATOM   1737 O  O   . ASP A 1 221 ? 14.52788  -18.56438 27.78882  1.000 11.82379  ?  221 ASP A O   1 
ATOM   1738 C  CB  . ASP A 1 221 ? 17.62791  -19.17691 28.79131  1.000 15.56430  ?  221 ASP A CB  1 
ATOM   1739 C  CG  . ASP A 1 221 ? 18.84120  -18.41733 29.30894  1.000 19.44897  ?  221 ASP A CG  1 
ATOM   1740 O  OD1 . ASP A 1 221 ? 18.70627  -17.41280 30.04379  1.000 15.36939  ?  221 ASP A OD1 1 
ATOM   1741 O  OD2 . ASP A 1 221 ? 19.96243  -18.84354 28.97269  1.000 18.06734  -1 221 ASP A OD2 1 
ATOM   1742 N  N   . ALA A 1 222 ? 14.78308  -20.53441 28.83699  1.000 17.88774  ?  222 ALA A N   1 
ATOM   1743 C  CA  . ALA A 1 222 ? 13.67310  -21.13680 28.10247  1.000 19.28447  ?  222 ALA A CA  1 
ATOM   1744 C  C   . ALA A 1 222 ? 12.37538  -20.38175 28.35188  1.000 16.68263  ?  222 ALA A C   1 
ATOM   1745 O  O   . ALA A 1 222 ? 11.60128  -20.13191 27.41858  1.000 21.68982  ?  222 ALA A O   1 
ATOM   1746 C  CB  . ALA A 1 222 ? 13.52149  -22.60919 28.49268  1.000 15.45535  ?  222 ALA A CB  1 
ATOM   1747 N  N   . ALA A 1 223 ? 12.12398  -20.00298 29.60898  1.000 16.80954  ?  223 ALA A N   1 
ATOM   1748 C  CA  . ALA A 1 223 ? 10.92093  -19.24306 29.93563  1.000 21.16499  ?  223 ALA A CA  1 
ATOM   1749 C  C   . ALA A 1 223 ? 10.95055  -17.85689 29.29972  1.000 17.41032  ?  223 ALA A C   1 
ATOM   1750 O  O   . ALA A 1 223 ? 9.96434   -17.42798 28.69582  1.000 15.10105  ?  223 ALA A O   1 
ATOM   1751 C  CB  . ALA A 1 223 ? 10.76553  -19.13820 31.45637  1.000 15.62703  ?  223 ALA A CB  1 
ATOM   1752 N  N   . ALA A 1 224 ? 12.07603  -17.14354 29.41328  1.000 12.89517  ?  224 ALA A N   1 
ATOM   1753 C  CA  . ALA A 1 224 ? 12.14244  -15.78573 28.87068  1.000 10.57266  ?  224 ALA A CA  1 
ATOM   1754 C  C   . ALA A 1 224 ? 12.06205  -15.78000 27.34708  1.000 14.80139  ?  224 ALA A C   1 
ATOM   1755 O  O   . ALA A 1 224 ? 11.43956  -14.88646 26.75792  1.000 15.17520  ?  224 ALA A O   1 
ATOM   1756 C  CB  . ALA A 1 224 ? 13.42233  -15.10296 29.33262  1.000 11.88760  ?  224 ALA A CB  1 
ATOM   1757 N  N   . LEU A 1 225 ? 12.70622  -16.74603 26.68977  1.000 16.85770  ?  225 LEU A N   1 
ATOM   1758 C  CA  . LEU A 1 225 ? 12.63623  -16.86048 25.23605  1.000 15.15769  ?  225 LEU A CA  1 
ATOM   1759 C  C   . LEU A 1 225 ? 11.37058  -17.55849 24.76071  1.000 20.99633  ?  225 LEU A C   1 
ATOM   1760 O  O   . LEU A 1 225 ? 11.14764  -17.63445 23.54541  1.000 18.73558  ?  225 LEU A O   1 
ATOM   1761 C  CB  . LEU A 1 225 ? 13.85312  -17.61128 24.70309  1.000 14.76649  ?  225 LEU A CB  1 
ATOM   1762 C  CG  . LEU A 1 225 ? 15.21449  -17.04163 25.11485  1.000 25.03158  ?  225 LEU A CG  1 
ATOM   1763 C  CD1 . LEU A 1 225 ? 16.33450  -17.93595 24.60580  1.000 22.13213  ?  225 LEU A CD1 1 
ATOM   1764 C  CD2 . LEU A 1 225 ? 15.38460  -15.61990 24.61485  1.000 16.76585  ?  225 LEU A CD2 1 
ATOM   1765 N  N   . GLU A 1 226 ? 10.55156  -18.05900 25.68985  1.000 16.33216  ?  226 GLU A N   1 
ATOM   1766 C  CA  . GLU A 1 226 ? 9.32365   -18.79346 25.38035  1.000 20.61834  ?  226 GLU A CA  1 
ATOM   1767 C  C   . GLU A 1 226 ? 9.60695   -20.02417 24.51882  1.000 28.06055  ?  226 GLU A C   1 
ATOM   1768 O  O   . GLU A 1 226 ? 8.88758   -20.31078 23.56027  1.000 33.77450  ?  226 GLU A O   1 
ATOM   1769 C  CB  . GLU A 1 226 ? 8.28510   -17.88415 24.72102  1.000 26.12739  ?  226 GLU A CB  1 
ATOM   1770 C  CG  . GLU A 1 226 ? 7.74408   -16.82215 25.65842  1.000 27.49715  ?  226 GLU A CG  1 
ATOM   1771 C  CD  . GLU A 1 226 ? 6.59045   -16.05694 25.05577  1.000 43.63934  ?  226 GLU A CD  1 
ATOM   1772 O  OE1 . GLU A 1 226 ? 5.47080   -16.12748 25.60765  1.000 36.60081  ?  226 GLU A OE1 1 
ATOM   1773 O  OE2 . GLU A 1 226 ? 6.80541   -15.39321 24.01972  1.000 37.67332  -1 226 GLU A OE2 1 
ATOM   1774 N  N   . GLU A 1 227 ? 10.65374  -20.77168 24.87629  1.000 29.53003  ?  227 GLU A N   1 
ATOM   1775 C  CA  . GLU A 1 227 ? 10.99647  -21.99501 24.15429  1.000 30.50382  ?  227 GLU A CA  1 
ATOM   1776 C  C   . GLU A 1 227 ? 10.84271  -23.24709 25.02333  1.000 36.59831  ?  227 GLU A C   1 
ATOM   1777 O  O   . GLU A 1 227 ? 9.99331   -23.29672 25.91640  1.000 38.52460  ?  227 GLU A O   1 
ATOM   1778 C  CB  . GLU A 1 227 ? 12.42041  -21.90196 23.61419  1.000 33.44556  ?  227 GLU A CB  1 
ATOM   1779 C  CG  . GLU A 1 227 ? 13.46560  -21.67508 24.67267  1.000 31.84065  ?  227 GLU A CG  1 
ATOM   1780 C  CD  . GLU A 1 227 ? 14.85030  -21.51286 24.08794  1.000 35.34662  ?  227 GLU A CD  1 
ATOM   1781 O  OE1 . GLU A 1 227 ? 14.95800  -20.92283 22.98553  1.000 39.38880  ?  227 GLU A OE1 1 
ATOM   1782 O  OE2 . GLU A 1 227 ? 15.82653  -21.98704 24.72352  1.000 40.57288  -1 227 GLU A OE2 1 
ATOM   1783 N  N   . PRO B 1 2   ? -14.34606 1.79228   -1.70626  1.000 52.48363  ?  2   PRO B N   1 
ATOM   1784 C  CA  . PRO B 1 2   ? -13.28894 2.11964   -0.74159  1.000 44.27085  ?  2   PRO B CA  1 
ATOM   1785 C  C   . PRO B 1 2   ? -13.01976 1.00888   0.26942   1.000 38.50787  ?  2   PRO B C   1 
ATOM   1786 O  O   . PRO B 1 2   ? -13.21410 -0.15932  -0.05267  1.000 45.28702  ?  2   PRO B O   1 
ATOM   1787 C  CB  . PRO B 1 2   ? -13.83401 3.36661   -0.05590  1.000 40.38486  ?  2   PRO B CB  1 
ATOM   1788 C  CG  . PRO B 1 2   ? -14.56896 4.07401   -1.17797  1.000 43.29469  ?  2   PRO B CG  1 
ATOM   1789 C  CD  . PRO B 1 2   ? -15.15984 2.97413   -2.04928  1.000 44.77785  ?  2   PRO B CD  1 
ATOM   1790 N  N   . LEU B 1 3   ? -12.56018 1.37606   1.46538   1.000 28.25640  ?  3   LEU B N   1 
ATOM   1791 C  CA  . LEU B 1 3   ? -12.21579 0.38086   2.47139   1.000 24.72402  ?  3   LEU B CA  1 
ATOM   1792 C  C   . LEU B 1 3   ? -13.42759 -0.47257  2.83185   1.000 25.57291  ?  3   LEU B C   1 
ATOM   1793 O  O   . LEU B 1 3   ? -14.57431 -0.02705  2.75600   1.000 31.13921  ?  3   LEU B O   1 
ATOM   1794 C  CB  . LEU B 1 3   ? -11.67004 1.06397   3.72957   1.000 24.41942  ?  3   LEU B CB  1 
ATOM   1795 C  CG  . LEU B 1 3   ? -10.34305 1.79064   3.52888   1.000 22.03045  ?  3   LEU B CG  1 
ATOM   1796 C  CD1 . LEU B 1 3   ? -9.84754  2.38116   4.82388   1.000 29.02273  ?  3   LEU B CD1 1 
ATOM   1797 C  CD2 . LEU B 1 3   ? -9.33198  0.81180   2.98305   1.000 23.75169  ?  3   LEU B CD2 1 
ATOM   1798 N  N   . GLY B 1 4   ? -13.16121 -1.71068  3.23723   1.000 25.96892  ?  4   GLY B N   1 
ATOM   1799 C  CA  . GLY B 1 4   ? -14.22032 -2.59273  3.68757   1.000 27.57290  ?  4   GLY B CA  1 
ATOM   1800 C  C   . GLY B 1 4   ? -14.91693 -2.07368  4.93489   1.000 31.04704  ?  4   GLY B C   1 
ATOM   1801 O  O   . GLY B 1 4   ? -14.50581 -1.10589  5.57903   1.000 25.54346  ?  4   GLY B O   1 
ATOM   1802 N  N   . THR B 1 5   ? -16.00958 -2.76285  5.27836   1.000 24.46924  ?  5   THR B N   1 
ATOM   1803 C  CA  . THR B 1 5   ? -16.83119 -2.37716  6.42259   1.000 27.35700  ?  5   THR B CA  1 
ATOM   1804 C  C   . THR B 1 5   ? -16.02618 -2.33264  7.71388   1.000 28.96892  ?  5   THR B C   1 
ATOM   1805 O  O   . THR B 1 5   ? -16.30927 -1.51141  8.59546   1.000 26.82934  ?  5   THR B O   1 
ATOM   1806 C  CB  . THR B 1 5   ? -18.00010 -3.35661  6.55611   1.000 35.45390  ?  5   THR B CB  1 
ATOM   1807 O  OG1 . THR B 1 5   ? -18.81339 -3.27842  5.37834   1.000 34.80764  ?  5   THR B OG1 1 
ATOM   1808 C  CG2 . THR B 1 5   ? -18.84437 -3.05008  7.79722   1.000 33.75521  ?  5   THR B CG2 1 
ATOM   1809 N  N   . GLU B 1 6   ? -15.01566 -3.19002  7.84059   1.000 21.03301  ?  6   GLU B N   1 
ATOM   1810 C  CA  . GLU B 1 6   ? -14.21870 -3.25505  9.05316   1.000 30.89914  ?  6   GLU B CA  1 
ATOM   1811 C  C   . GLU B 1 6   ? -13.05674 -2.27589  9.04904   1.000 21.38494  ?  6   GLU B C   1 
ATOM   1812 O  O   . GLU B 1 6   ? -12.28923 -2.25024  10.01655  1.000 23.71712  ?  6   GLU B O   1 
ATOM   1813 C  CB  . GLU B 1 6   ? -13.70628 -4.68178  9.27380   1.000 29.24942  ?  6   GLU B CB  1 
ATOM   1814 C  CG  . GLU B 1 6   ? -14.81602 -5.65339  9.66981   1.000 36.41234  ?  6   GLU B CG  1 
ATOM   1815 C  CD  . GLU B 1 6   ? -15.57230 -5.19221  10.91139  1.000 51.84785  ?  6   GLU B CD  1 
ATOM   1816 O  OE1 . GLU B 1 6   ? -14.91834 -4.85078  11.92752  1.000 56.24850  ?  6   GLU B OE1 1 
ATOM   1817 O  OE2 . GLU B 1 6   ? -16.82139 -5.15402  10.86272  1.000 54.43501  -1 6   GLU B OE2 1 
ATOM   1818 N  N   . GLY B 1 7   ? -12.91791 -1.46328  8.00309   1.000 16.54669  ?  7   GLY B N   1 
ATOM   1819 C  CA  . GLY B 1 7   ? -11.92337 -0.40647  7.99663   1.000 21.57851  ?  7   GLY B CA  1 
ATOM   1820 C  C   . GLY B 1 7   ? -10.58452 -0.77351  7.40331   1.000 18.69493  ?  7   GLY B C   1 
ATOM   1821 O  O   . GLY B 1 7   ? -9.59901  -0.07029  7.65043   1.000 17.00704  ?  7   GLY B O   1 
ATOM   1822 N  N   . PHE B 1 8   ? -10.50977 -1.84883  6.62716   1.000 17.09684  ?  8   PHE B N   1 
ATOM   1823 C  CA  . PHE B 1 8   ? -9.26358  -2.23716  5.98796   1.000 15.96585  ?  8   PHE B CA  1 
ATOM   1824 C  C   . PHE B 1 8   ? -9.59143  -3.02861  4.73557   1.000 16.40012  ?  8   PHE B C   1 
ATOM   1825 O  O   . PHE B 1 8   ? -10.66697 -3.60825  4.61532   1.000 14.07144  ?  8   PHE B O   1 
ATOM   1826 C  CB  . PHE B 1 8   ? -8.37796  -3.07590  6.92071   1.000 13.93235  ?  8   PHE B CB  1 
ATOM   1827 C  CG  . PHE B 1 8   ? -8.83281  -4.50062  7.06055   1.000 14.40095  ?  8   PHE B CG  1 
ATOM   1828 C  CD1 . PHE B 1 8   ? -9.90142  -4.82665  7.88355   1.000 14.04587  ?  8   PHE B CD1 1 
ATOM   1829 C  CD2 . PHE B 1 8   ? -8.18661  -5.51784  6.37206   1.000 14.20320  ?  8   PHE B CD2 1 
ATOM   1830 C  CE1 . PHE B 1 8   ? -10.32526 -6.13571  8.00464   1.000 16.74578  ?  8   PHE B CE1 1 
ATOM   1831 C  CE2 . PHE B 1 8   ? -8.60372  -6.83673  6.49464   1.000 20.30183  ?  8   PHE B CE2 1 
ATOM   1832 C  CZ  . PHE B 1 8   ? -9.67299  -7.14393  7.30932   1.000 24.99041  ?  8   PHE B CZ  1 
ATOM   1833 N  N   . THR B 1 9   ? -8.65079  -3.03774  3.80023   1.000 10.04225  ?  9   THR B N   1 
ATOM   1834 C  CA  . THR B 1 9   ? -8.71461  -3.90699  2.63679   1.000 15.39023  ?  9   THR B CA  1 
ATOM   1835 C  C   . THR B 1 9   ? -7.30591  -4.36582  2.30523   1.000 17.56309  ?  9   THR B C   1 
ATOM   1836 O  O   . THR B 1 9   ? -6.34064  -3.60957  2.45853   1.000 16.61228  ?  9   THR B O   1 
ATOM   1837 C  CB  . THR B 1 9   ? -9.30663  -3.21839  1.39882   1.000 18.16810  ?  9   THR B CB  1 
ATOM   1838 O  OG1 . THR B 1 9   ? -10.52901 -2.56725  1.74896   1.000 24.44735  ?  9   THR B OG1 1 
ATOM   1839 C  CG2 . THR B 1 9   ? -9.60610  -4.25208  0.33640   1.000 16.02188  ?  9   THR B CG2 1 
ATOM   1840 N  N   . VAL B 1 10  ? -7.20060  -5.60939  1.84859   1.000 13.11889  ?  10  VAL B N   1 
ATOM   1841 C  CA  . VAL B 1 10  ? -5.95797  -6.17782  1.34689   1.000 13.14900  ?  10  VAL B CA  1 
ATOM   1842 C  C   . VAL B 1 10  ? -6.08372  -6.28142  -0.16333  1.000 19.92108  ?  10  VAL B C   1 
ATOM   1843 O  O   . VAL B 1 10  ? -7.07872  -6.81431  -0.66270  1.000 13.65137  ?  10  VAL B O   1 
ATOM   1844 C  CB  . VAL B 1 10  ? -5.67523  -7.55910  1.96223   1.000 16.32197  ?  10  VAL B CB  1 
ATOM   1845 C  CG1 . VAL B 1 10  ? -4.40960  -8.14493  1.35167   1.000 11.30396  ?  10  VAL B CG1 1 
ATOM   1846 C  CG2 . VAL B 1 10  ? -5.56432  -7.45494  3.49042   1.000 12.53462  ?  10  VAL B CG2 1 
ATOM   1847 N  N   . ILE B 1 11  ? -5.07158  -5.80260  -0.88670  1.000 16.54881  ?  11  ILE B N   1 
ATOM   1848 C  CA  . ILE B 1 11  ? -5.09230  -5.80387  -2.34449  1.000 17.63611  ?  11  ILE B CA  1 
ATOM   1849 C  C   . ILE B 1 11  ? -3.83740  -6.47678  -2.88845  1.000 25.14540  ?  11  ILE B C   1 
ATOM   1850 O  O   . ILE B 1 11  ? -2.81972  -6.62515  -2.20136  1.000 14.17785  ?  11  ILE B O   1 
ATOM   1851 C  CB  . ILE B 1 11  ? -5.21604  -4.38056  -2.92011  1.000 18.07572  ?  11  ILE B CB  1 
ATOM   1852 C  CG1 . ILE B 1 11  ? -4.02429  -3.52435  -2.47138  1.000 14.90217  ?  11  ILE B CG1 1 
ATOM   1853 C  CG2 . ILE B 1 11  ? -6.51615  -3.74796  -2.47900  1.000 18.37604  ?  11  ILE B CG2 1 
ATOM   1854 C  CD1 . ILE B 1 11  ? -3.85360  -2.24557  -3.26348  1.000 16.23073  ?  11  ILE B CD1 1 
ATOM   1855 N  N   . ASP B 1 12  ? -3.92255  -6.87688  -4.15507  1.000 14.57898  ?  12  ASP B N   1 
ATOM   1856 C  CA  . ASP B 1 12  ? -2.76481  -7.33178  -4.90861  1.000 19.51829  ?  12  ASP B CA  1 
ATOM   1857 C  C   . ASP B 1 12  ? -2.13350  -6.16429  -5.65963  1.000 26.06887  ?  12  ASP B C   1 
ATOM   1858 O  O   . ASP B 1 12  ? -2.81536  -5.23766  -6.10512  1.000 30.02239  ?  12  ASP B O   1 
ATOM   1859 C  CB  . ASP B 1 12  ? -3.15196  -8.44045  -5.88852  1.000 25.27904  ?  12  ASP B CB  1 
ATOM   1860 C  CG  . ASP B 1 12  ? -3.69907  -9.66149  -5.18460  1.000 24.61266  ?  12  ASP B CG  1 
ATOM   1861 O  OD1 . ASP B 1 12  ? -3.08810  -10.09794 -4.18434  1.000 33.09387  ?  12  ASP B OD1 1 
ATOM   1862 O  OD2 . ASP B 1 12  ? -4.74753  -10.17787 -5.61896  1.000 37.30099  -1 12  ASP B OD2 1 
ATOM   1863 N  N   . LEU B 1 13  ? -0.83757  -6.20498  -5.77402  1.000 21.81571  ?  13  LEU B N   1 
ATOM   1864 C  CA  . LEU B 1 13  ? -0.15609  -5.11047  -6.43752  1.000 19.33150  ?  13  LEU B CA  1 
ATOM   1865 C  C   . LEU B 1 13  ? 0.22061   -5.50713  -7.85687  1.000 21.64214  ?  13  LEU B C   1 
ATOM   1866 O  O   . LEU B 1 13  ? 0.49684   -6.67691  -8.12721  1.000 24.43433  ?  13  LEU B O   1 
ATOM   1867 C  CB  . LEU B 1 13  ? 1.11332   -4.73406  -5.66925  1.000 20.30354  ?  13  LEU B CB  1 
ATOM   1868 C  CG  . LEU B 1 13  ? 0.84940   -4.25695  -4.24355  1.000 25.72601  ?  13  LEU B CG  1 
ATOM   1869 C  CD1 . LEU B 1 13  ? 2.16747   -4.04808  -3.52299  1.000 23.49014  ?  13  LEU B CD1 1 
ATOM   1870 C  CD2 . LEU B 1 13  ? 0.02220   -2.98315  -4.29295  1.000 26.00125  ?  13  LEU B CD2 1 
ATOM   1871 N  N   . PRO B 1 14  ? 0.24530   -4.56408  -8.78446  1.000 29.28346  ?  14  PRO B N   1 
ATOM   1872 C  CA  . PRO B 1 14  ? 0.76242   -4.86270  -10.11884 1.000 27.87299  ?  14  PRO B CA  1 
ATOM   1873 C  C   . PRO B 1 14  ? 2.26078   -5.09546  -10.06468 1.000 32.26066  ?  14  PRO B C   1 
ATOM   1874 O  O   . PRO B 1 14  ? 2.91900   -4.85979  -9.05161  1.000 25.56884  ?  14  PRO B O   1 
ATOM   1875 C  CB  . PRO B 1 14  ? 0.41705   -3.60677  -10.91974 1.000 33.15663  ?  14  PRO B CB  1 
ATOM   1876 C  CG  . PRO B 1 14  ? 0.38786   -2.52145  -9.89627  1.000 35.33478  ?  14  PRO B CG  1 
ATOM   1877 C  CD  . PRO B 1 14  ? -0.18597  -3.16351  -8.65934  1.000 25.76118  ?  14  PRO B CD  1 
ATOM   1878 N  N   . GLU B 1 15  ? 2.79153   -5.57305  -11.18745 1.000 31.55465  ?  15  GLU B N   1 
ATOM   1879 C  CA  . GLU B 1 15  ? 4.23072   -5.71103  -11.34644 1.000 30.50805  ?  15  GLU B CA  1 
ATOM   1880 C  C   . GLU B 1 15  ? 4.91027   -4.36144  -11.14209 1.000 24.12684  ?  15  GLU B C   1 
ATOM   1881 O  O   . GLU B 1 15  ? 4.38109   -3.31862  -11.53005 1.000 28.84056  ?  15  GLU B O   1 
ATOM   1882 C  CB  . GLU B 1 15  ? 4.54261   -6.25636  -12.73989 1.000 38.72192  ?  15  GLU B CB  1 
ATOM   1883 C  CG  . GLU B 1 15  ? 5.88649   -6.95714  -12.87267 1.000 56.10903  ?  15  GLU B CG  1 
ATOM   1884 C  CD  . GLU B 1 15  ? 6.59994   -6.59150  -14.17009 1.000 67.93803  ?  15  GLU B CD  1 
ATOM   1885 O  OE1 . GLU B 1 15  ? 7.81160   -6.27421  -14.11283 1.000 73.07178  ?  15  GLU B OE1 1 
ATOM   1886 O  OE2 . GLU B 1 15  ? 5.95052   -6.61034  -15.24349 1.000 70.56743  -1 15  GLU B OE2 1 
ATOM   1887 N  N   . VAL B 1 16  ? 6.08233   -4.38063  -10.51671 1.000 27.49770  ?  16  VAL B N   1 
ATOM   1888 C  CA  . VAL B 1 16  ? 6.82910   -3.16163  -10.24873 1.000 28.28273  ?  16  VAL B CA  1 
ATOM   1889 C  C   . VAL B 1 16  ? 7.95422   -3.03460  -11.26929 1.000 25.74400  ?  16  VAL B C   1 
ATOM   1890 O  O   . VAL B 1 16  ? 8.39066   -4.01153  -11.88427 1.000 23.14136  ?  16  VAL B O   1 
ATOM   1891 C  CB  . VAL B 1 16  ? 7.38055   -3.12471  -8.79694  1.000 31.02271  ?  16  VAL B CB  1 
ATOM   1892 C  CG1 . VAL B 1 16  ? 6.23930   -3.14197  -7.79231  1.000 30.21416  ?  16  VAL B CG1 1 
ATOM   1893 C  CG2 . VAL B 1 16  ? 8.33012   -4.29000  -8.54153  1.000 28.37450  ?  16  VAL B CG2 1 
ATOM   1894 N  N   . ALA B 1 17  ? 8.43203   -1.80474  -11.45263 1.000 25.04068  ?  17  ALA B N   1 
ATOM   1895 C  CA  . ALA B 1 17  ? 9.54332   -1.55644  -12.35507 1.000 26.56209  ?  17  ALA B CA  1 
ATOM   1896 C  C   . ALA B 1 17  ? 10.78045  -2.31971  -11.88139 1.000 24.34213  ?  17  ALA B C   1 
ATOM   1897 O  O   . ALA B 1 17  ? 10.93592  -2.57504  -10.68378 1.000 24.95180  ?  17  ALA B O   1 
ATOM   1898 C  CB  . ALA B 1 17  ? 9.83252   -0.05814  -12.42760 1.000 28.49796  ?  17  ALA B CB  1 
ATOM   1899 N  N   . PRO B 1 18  ? 11.68187  -2.69306  -12.79734 1.000 24.94849  ?  18  PRO B N   1 
ATOM   1900 C  CA  . PRO B 1 18  ? 12.80146  -3.56944  -12.41338 1.000 28.81886  ?  18  PRO B CA  1 
ATOM   1901 C  C   . PRO B 1 18  ? 13.82962  -2.92020  -11.50267 1.000 23.16707  ?  18  PRO B C   1 
ATOM   1902 O  O   . PRO B 1 18  ? 14.66534  -3.64187  -10.94497 1.000 22.81514  ?  18  PRO B O   1 
ATOM   1903 C  CB  . PRO B 1 18  ? 13.42818  -3.95567  -13.76194 1.000 28.95721  ?  18  PRO B CB  1 
ATOM   1904 C  CG  . PRO B 1 18  ? 13.02221  -2.88893  -14.68980 1.000 28.81532  ?  18  PRO B CG  1 
ATOM   1905 C  CD  . PRO B 1 18  ? 11.65589  -2.44780  -14.25000 1.000 33.62407  ?  18  PRO B CD  1 
ATOM   1906 N  N   . ASP B 1 19  ? 13.82036  -1.59965  -11.33733 1.000 24.76696  ?  19  ASP B N   1 
ATOM   1907 C  CA  . ASP B 1 19  ? 14.78726  -0.98019  -10.44403 1.000 23.94058  ?  19  ASP B CA  1 
ATOM   1908 C  C   . ASP B 1 19  ? 14.31366  -0.94541  -8.99299  1.000 20.99504  ?  19  ASP B C   1 
ATOM   1909 O  O   . ASP B 1 19  ? 15.09724  -0.58058  -8.10566  1.000 25.04203  ?  19  ASP B O   1 
ATOM   1910 C  CB  . ASP B 1 19  ? 15.12245  0.44259   -10.92362 1.000 27.58748  ?  19  ASP B CB  1 
ATOM   1911 C  CG  . ASP B 1 19  ? 13.93010  1.37822   -10.84728 1.000 30.67926  ?  19  ASP B CG  1 
ATOM   1912 O  OD1 . ASP B 1 19  ? 12.79090  0.87064   -10.81311 1.000 39.12680  -1 19  ASP B OD1 1 
ATOM   1913 O  OD2 . ASP B 1 19  ? 14.12297  2.61142   -10.81803 1.000 31.77205  -1 19  ASP B OD2 1 
ATOM   1914 N  N   . ILE B 1 20  ? 13.07300  -1.34587  -8.72191  1.000 19.53348  ?  20  ILE B N   1 
ATOM   1915 C  CA  . ILE B 1 20  ? 12.50891  -1.16069  -7.38534  1.000 21.10216  ?  20  ILE B CA  1 
ATOM   1916 C  C   . ILE B 1 20  ? 13.11834  -2.14834  -6.39331  1.000 20.08318  ?  20  ILE B C   1 
ATOM   1917 O  O   . ILE B 1 20  ? 13.65013  -1.75369  -5.34688  1.000 20.02465  ?  20  ILE B O   1 
ATOM   1918 C  CB  . ILE B 1 20  ? 10.97601  -1.26746  -7.43171  1.000 21.18137  ?  20  ILE B CB  1 
ATOM   1919 C  CG1 . ILE B 1 20  ? 10.40692  -0.05926  -8.19114  1.000 22.34729  ?  20  ILE B CG1 1 
ATOM   1920 C  CG2 . ILE B 1 20  ? 10.40728  -1.33054  -6.02160  1.000 17.57274  ?  20  ILE B CG2 1 
ATOM   1921 C  CD1 . ILE B 1 20  ? 8.91046   0.05268   -8.13426  1.000 28.05045  ?  20  ILE B CD1 1 
ATOM   1922 N  N   . LEU B 1 21  ? 13.04907  -3.44631  -6.69651  1.000 16.91144  ?  21  LEU B N   1 
ATOM   1923 C  CA  . LEU B 1 21  ? 13.59354  -4.42992  -5.75992  1.000 15.80180  ?  21  LEU B CA  1 
ATOM   1924 C  C   . LEU B 1 21  ? 15.09287  -4.27213  -5.51305  1.000 17.57098  ?  21  LEU B C   1 
ATOM   1925 O  O   . LEU B 1 21  ? 15.50589  -4.36962  -4.34132  1.000 16.37060  ?  21  LEU B O   1 
ATOM   1926 C  CB  . LEU B 1 21  ? 13.25761  -5.85511  -6.23101  1.000 19.58006  ?  21  LEU B CB  1 
ATOM   1927 C  CG  . LEU B 1 21  ? 12.02735  -6.46766  -5.55146  1.000 22.78452  ?  21  LEU B CG  1 
ATOM   1928 C  CD1 . LEU B 1 21  ? 10.76967  -5.70443  -5.90992  1.000 23.05028  ?  21  LEU B CD1 1 
ATOM   1929 C  CD2 . LEU B 1 21  ? 11.86057  -7.95930  -5.84723  1.000 21.20041  ?  21  LEU B CD2 1 
ATOM   1930 N  N   . PRO B 1 22  ? 15.94969  -4.04801  -6.51796  1.000 17.04441  ?  22  PRO B N   1 
ATOM   1931 C  CA  . PRO B 1 22  ? 17.37481  -3.83873  -6.21431  1.000 20.59325  ?  22  PRO B CA  1 
ATOM   1932 C  C   . PRO B 1 22  ? 17.65063  -2.62489  -5.35400  1.000 18.48611  ?  22  PRO B C   1 
ATOM   1933 O  O   . PRO B 1 22  ? 18.65007  -2.61969  -4.62406  1.000 19.52336  ?  22  PRO B O   1 
ATOM   1934 C  CB  . PRO B 1 22  ? 18.00995  -3.68693  -7.60437  1.000 20.52500  ?  22  PRO B CB  1 
ATOM   1935 C  CG  . PRO B 1 22  ? 17.11129  -4.45558  -8.49265  1.000 18.41207  ?  22  PRO B CG  1 
ATOM   1936 C  CD  . PRO B 1 22  ? 15.73379  -4.20445  -7.97028  1.000 19.26410  ?  22  PRO B CD  1 
ATOM   1937 N  N   . SER B 1 23  ? 16.80350  -1.59390  -5.41151  1.000 16.15381  ?  23  SER B N   1 
ATOM   1938 C  CA  . SER B 1 23  ? 17.06281  -0.38425  -4.63514  1.000 15.91487  ?  23  SER B CA  1 
ATOM   1939 C  C   . SER B 1 23  ? 17.10555  -0.64279  -3.13175  1.000 18.07413  ?  23  SER B C   1 
ATOM   1940 O  O   . SER B 1 23  ? 17.68197  0.16353   -2.38897  1.000 17.55275  ?  23  SER B O   1 
ATOM   1941 C  CB  . SER B 1 23  ? 16.00062  0.66872   -4.93307  1.000 15.33682  ?  23  SER B CB  1 
ATOM   1942 O  OG  . SER B 1 23  ? 14.77171  0.32708   -4.30534  1.000 18.33113  ?  23  SER B OG  1 
ATOM   1943 N  N   . TYR B 1 24  ? 16.49805  -1.73342  -2.65875  1.000 15.64244  ?  24  TYR B N   1 
ATOM   1944 C  CA  . TYR B 1 24  ? 16.52098  -2.00391  -1.22457  1.000 14.27550  ?  24  TYR B CA  1 
ATOM   1945 C  C   . TYR B 1 24  ? 17.92481  -2.33067  -0.73586  1.000 18.21235  ?  24  TYR B C   1 
ATOM   1946 O  O   . TYR B 1 24  ? 18.24029  -2.09610  0.43827   1.000 18.08540  ?  24  TYR B O   1 
ATOM   1947 C  CB  . TYR B 1 24  ? 15.55097  -3.13175  -0.88456  1.000 12.02128  ?  24  TYR B CB  1 
ATOM   1948 C  CG  . TYR B 1 24  ? 14.12715  -2.64531  -0.83614  1.000 11.61884  ?  24  TYR B CG  1 
ATOM   1949 C  CD1 . TYR B 1 24  ? 13.33920  -2.62456  -1.97943  1.000 9.33005   ?  24  TYR B CD1 1 
ATOM   1950 C  CD2 . TYR B 1 24  ? 13.58857  -2.15501  0.34628   1.000 9.80514   ?  24  TYR B CD2 1 
ATOM   1951 C  CE1 . TYR B 1 24  ? 12.04335  -2.16957  -1.93229  1.000 12.18277  ?  24  TYR B CE1 1 
ATOM   1952 C  CE2 . TYR B 1 24  ? 12.29186  -1.69697  0.40221   1.000 9.10728   ?  24  TYR B CE2 1 
ATOM   1953 C  CZ  . TYR B 1 24  ? 11.53078  -1.68820  -0.73962  1.000 10.71225  ?  24  TYR B CZ  1 
ATOM   1954 O  OH  . TYR B 1 24  ? 10.23570  -1.22684  -0.67289  1.000 12.07817  ?  24  TYR B OH  1 
ATOM   1955 N  N   . ASP B 1 25  ? 18.78346  -2.85046  -1.61715  1.000 15.80403  ?  25  ASP B N   1 
ATOM   1956 C  CA  . ASP B 1 25  ? 20.17230  -3.10423  -1.24211  1.000 17.46379  ?  25  ASP B CA  1 
ATOM   1957 C  C   . ASP B 1 25  ? 20.95528  -1.82499  -0.97571  1.000 17.45438  ?  25  ASP B C   1 
ATOM   1958 O  O   . ASP B 1 25  ? 22.04587  -1.89532  -0.40147  1.000 18.22819  ?  25  ASP B O   1 
ATOM   1959 C  CB  . ASP B 1 25  ? 20.89358  -3.89549  -2.33310  1.000 20.98171  ?  25  ASP B CB  1 
ATOM   1960 C  CG  . ASP B 1 25  ? 20.38799  -5.30628  -2.45638  1.000 24.88195  ?  25  ASP B CG  1 
ATOM   1961 O  OD1 . ASP B 1 25  ? 20.10005  -5.92153  -1.41028  1.000 28.04718  ?  25  ASP B OD1 1 
ATOM   1962 O  OD2 . ASP B 1 25  ? 20.27201  -5.79529  -3.59990  1.000 34.17161  -1 25  ASP B OD2 1 
ATOM   1963 N  N   . ARG B 1 26  ? 20.45892  -0.67050  -1.41824  1.000 16.37953  ?  26  ARG B N   1 
ATOM   1964 C  CA  . ARG B 1 26  ? 21.18084  0.58329   -1.26041  1.000 20.97742  ?  26  ARG B CA  1 
ATOM   1965 C  C   . ARG B 1 26  ? 20.51889  1.50410   -0.24548  1.000 21.45787  ?  26  ARG B C   1 
ATOM   1966 O  O   . ARG B 1 26  ? 20.75341  2.71859   -0.26678  1.000 18.50857  ?  26  ARG B O   1 
ATOM   1967 C  CB  . ARG B 1 26  ? 21.32118  1.29842   -2.60392  1.000 25.59112  ?  26  ARG B CB  1 
ATOM   1968 C  CG  . ARG B 1 26  ? 21.77554  0.40720   -3.74184  1.000 26.49145  ?  26  ARG B CG  1 
ATOM   1969 C  CD  . ARG B 1 26  ? 22.02758  1.22431   -5.00180  1.000 23.59533  ?  26  ARG B CD  1 
ATOM   1970 N  NE  . ARG B 1 26  ? 20.85756  1.98538   -5.42600  1.000 27.90141  ?  26  ARG B NE  1 
ATOM   1971 C  CZ  . ARG B 1 26  ? 19.94518  1.54370   -6.28388  1.000 31.90256  ?  26  ARG B CZ  1 
ATOM   1972 N  NH1 . ARG B 1 26  ? 20.01734  0.32832   -6.80287  1.000 25.07500  ?  26  ARG B NH1 1 
ATOM   1973 N  NH2 . ARG B 1 26  ? 18.93258  2.34089   -6.62596  1.000 23.67336  ?  26  ARG B NH2 1 
ATOM   1974 N  N   . CYS B 1 27  ? 19.69381  0.95265   0.63665   1.000 15.19152  ?  27  CYS B N   1 
ATOM   1975 C  CA  . CYS B 1 27  ? 19.12667  1.76705   1.71030   1.000 15.92428  ?  27  CYS B CA  1 
ATOM   1976 C  C   . CYS B 1 27  ? 20.05376  1.75761   2.92441   1.000 13.74532  ?  27  CYS B C   1 
ATOM   1977 O  O   . CYS B 1 27  ? 20.41698  0.68061   3.40577   1.000 13.19805  ?  27  CYS B O   1 
ATOM   1978 C  CB  . CYS B 1 27  ? 17.76110  1.24751   2.11455   1.000 10.20423  ?  27  CYS B CB  1 
ATOM   1979 S  SG  . CYS B 1 27  ? 16.49527  1.50714   0.87944   1.000 15.78702  ?  27  CYS B SG  1 
ATOM   1980 N  N   . PRO B 1 28  ? 20.43686  2.91555   3.45742   1.000 14.40214  ?  28  PRO B N   1 
ATOM   1981 C  CA  . PRO B 1 28  ? 21.36592  2.93558   4.59657   1.000 13.68733  ?  28  PRO B CA  1 
ATOM   1982 C  C   . PRO B 1 28  ? 20.68879  2.51255   5.89014   1.000 10.43296  ?  28  PRO B C   1 
ATOM   1983 O  O   . PRO B 1 28  ? 19.46564  2.47524   5.99773   1.000 13.40088  ?  28  PRO B O   1 
ATOM   1984 C  CB  . PRO B 1 28  ? 21.82027  4.39656   4.66557   1.000 18.40842  ?  28  PRO B CB  1 
ATOM   1985 C  CG  . PRO B 1 28  ? 20.73774  5.16784   4.01099   1.000 21.03309  ?  28  PRO B CG  1 
ATOM   1986 C  CD  . PRO B 1 28  ? 20.14095  4.26586   2.94849   1.000 15.53508  ?  28  PRO B CD  1 
ATOM   1987 N  N   . VAL B 1 29  ? 21.50863  2.17438   6.88883   1.000 12.41891  ?  29  VAL B N   1 
ATOM   1988 C  CA  . VAL B 1 29  ? 20.93442  1.73701   8.15709   1.000 8.87550   ?  29  VAL B CA  1 
ATOM   1989 C  C   . VAL B 1 29  ? 20.07580  2.85271   8.73578   1.000 11.58758  ?  29  VAL B C   1 
ATOM   1990 O  O   . VAL B 1 29  ? 20.37615  4.05007   8.59587   1.000 9.14812   ?  29  VAL B O   1 
ATOM   1991 C  CB  . VAL B 1 29  ? 22.01914  1.27579   9.15059   1.000 14.99585  ?  29  VAL B CB  1 
ATOM   1992 C  CG1 . VAL B 1 29  ? 22.83742  2.44478   9.67316   1.000 17.26758  ?  29  VAL B CG1 1 
ATOM   1993 C  CG2 . VAL B 1 29  ? 21.37796  0.50809   10.32641  1.000 14.03926  ?  29  VAL B CG2 1 
ATOM   1994 N  N   . ASP B 1 30  ? 18.95656  2.45669   9.32638   1.000 8.75434   ?  30  ASP B N   1 
ATOM   1995 C  CA  . ASP B 1 30  ? 18.10070  3.35913   10.08550  1.000 9.86041   ?  30  ASP B CA  1 
ATOM   1996 C  C   . ASP B 1 30  ? 18.77025  3.59624   11.43767  1.000 8.88372   ?  30  ASP B C   1 
ATOM   1997 O  O   . ASP B 1 30  ? 18.85289  2.67974   12.26656  1.000 8.84642   ?  30  ASP B O   1 
ATOM   1998 C  CB  . ASP B 1 30  ? 16.71187  2.74202   10.24492  1.000 12.08280  ?  30  ASP B CB  1 
ATOM   1999 C  CG  . ASP B 1 30  ? 15.69952  3.68250   10.89909  1.000 14.33338  ?  30  ASP B CG  1 
ATOM   2000 O  OD1 . ASP B 1 30  ? 16.07820  4.68947   11.53091  1.000 8.06849   ?  30  ASP B OD1 1 
ATOM   2001 O  OD2 . ASP B 1 30  ? 14.48972  3.39466   10.76601  1.000 12.73738  -1 30  ASP B OD2 1 
ATOM   2002 N  N   . ASP B 1 31  ? 19.26785  4.81358   11.65327  1.000 12.20159  ?  31  ASP B N   1 
ATOM   2003 C  CA  . ASP B 1 31  ? 19.98716  5.12724   12.88741  1.000 14.08590  ?  31  ASP B CA  1 
ATOM   2004 C  C   . ASP B 1 31  ? 19.08655  5.28582   14.10137  1.000 13.90157  ?  31  ASP B C   1 
ATOM   2005 O  O   . ASP B 1 31  ? 19.60745  5.42588   15.21562  1.000 11.47362  ?  31  ASP B O   1 
ATOM   2006 C  CB  . ASP B 1 31  ? 20.79432  6.40828   12.70700  1.000 16.82037  ?  31  ASP B CB  1 
ATOM   2007 C  CG  . ASP B 1 31  ? 21.92844  6.23174   11.72859  1.000 20.05039  ?  31  ASP B CG  1 
ATOM   2008 O  OD1 . ASP B 1 31  ? 22.64314  5.22121   11.85158  1.000 22.33155  ?  31  ASP B OD1 1 
ATOM   2009 O  OD2 . ASP B 1 31  ? 22.08742  7.08642   10.83683  1.000 30.69652  -1 31  ASP B OD2 1 
ATOM   2010 N  N   . TYR B 1 32  ? 17.76531  5.27780   13.92839  1.000 8.36957   ?  32  TYR B N   1 
ATOM   2011 C  CA  . TYR B 1 32  ? 16.85620  5.62673   15.01205  1.000 9.56406   ?  32  TYR B CA  1 
ATOM   2012 C  C   . TYR B 1 32  ? 15.94190  4.50541   15.45439  1.000 10.44577  ?  32  TYR B C   1 
ATOM   2013 O  O   . TYR B 1 32  ? 15.41126  4.57910   16.57507  1.000 10.14148  ?  32  TYR B O   1 
ATOM   2014 C  CB  . TYR B 1 32  ? 15.97393  6.81633   14.60559  1.000 11.05563  ?  32  TYR B CB  1 
ATOM   2015 C  CG  . TYR B 1 32  ? 16.77261  7.99040   14.08030  1.000 8.05524   ?  32  TYR B CG  1 
ATOM   2016 C  CD1 . TYR B 1 32  ? 17.28565  8.94551   14.94337  1.000 10.29079  ?  32  TYR B CD1 1 
ATOM   2017 C  CD2 . TYR B 1 32  ? 17.00328  8.14443   12.71692  1.000 10.96449  ?  32  TYR B CD2 1 
ATOM   2018 C  CE1 . TYR B 1 32  ? 18.01341  10.03041  14.46449  1.000 10.79903  ?  32  TYR B CE1 1 
ATOM   2019 C  CE2 . TYR B 1 32  ? 17.74455  9.21497   12.23012  1.000 10.53169  ?  32  TYR B CE2 1 
ATOM   2020 C  CZ  . TYR B 1 32  ? 18.24125  10.15546  13.10546  1.000 13.41671  ?  32  TYR B CZ  1 
ATOM   2021 O  OH  . TYR B 1 32  ? 18.96293  11.23842  12.62011  1.000 11.49143  ?  32  TYR B OH  1 
ATOM   2022 N  N   A MET B 1 33  ? 15.71277  3.48935   14.61524  0.409 9.61333   ?  33  MET B N   1 
ATOM   2023 N  N   B MET B 1 33  ? 15.73234  3.48616   14.61882  0.591 9.61193   ?  33  MET B N   1 
ATOM   2024 C  CA  A MET B 1 33  ? 14.77338  2.41208   14.90598  0.409 10.05724  ?  33  MET B CA  1 
ATOM   2025 C  CA  B MET B 1 33  ? 14.81704  2.40271   14.93137  0.591 10.04579  ?  33  MET B CA  1 
ATOM   2026 C  C   A MET B 1 33  ? 15.35735  1.07427   14.47974  0.409 8.25605   ?  33  MET B C   1 
ATOM   2027 C  C   B MET B 1 33  ? 15.38460  1.06762   14.49168  0.591 8.25887   ?  33  MET B C   1 
ATOM   2028 O  O   A MET B 1 33  ? 16.10690  0.99347   13.50549  0.409 9.33876   ?  33  MET B O   1 
ATOM   2029 O  O   B MET B 1 33  ? 16.12923  0.98279   13.51417  0.591 9.33449   ?  33  MET B O   1 
ATOM   2030 C  CB  A MET B 1 33  ? 13.44038  2.60654   14.17592  0.409 10.03342  ?  33  MET B CB  1 
ATOM   2031 C  CB  B MET B 1 33  ? 13.47543  2.56848   14.24721  0.591 10.03403  ?  33  MET B CB  1 
ATOM   2032 C  CG  A MET B 1 33  ? 12.82160  3.95686   14.36042  0.409 9.13977   ?  33  MET B CG  1 
ATOM   2033 C  CG  B MET B 1 33  ? 12.39072  2.02914   15.08322  0.591 17.13186  ?  33  MET B CG  1 
ATOM   2034 S  SD  A MET B 1 33  ? 11.61233  3.93167   15.67168  0.409 29.62284  ?  33  MET B SD  1 
ATOM   2035 S  SD  B MET B 1 33  ? 11.72489  3.49927   15.82656  0.591 32.49103  ?  33  MET B SD  1 
ATOM   2036 C  CE  A MET B 1 33  ? 10.50185  2.63479   15.11571  0.409 7.42675   ?  33  MET B CE  1 
ATOM   2037 C  CE  B MET B 1 33  ? 10.89974  4.08513   14.36336  0.591 0.00008   ?  33  MET B CE  1 
ATOM   2038 N  N   . GLY B 1 34  ? 14.99144  0.01848   15.21417  1.000 9.67411   ?  34  GLY B N   1 
ATOM   2039 C  CA  . GLY B 1 34  ? 15.34419  -1.33550  14.85052  1.000 6.89811   ?  34  GLY B CA  1 
ATOM   2040 C  C   . GLY B 1 34  ? 16.70182  -1.80878  15.32196  1.000 7.15896   ?  34  GLY B C   1 
ATOM   2041 O  O   . GLY B 1 34  ? 17.05107  -2.97068  15.06718  1.000 9.87742   ?  34  GLY B O   1 
ATOM   2042 N  N   . ASN B 1 35  ? 17.47354  -0.95396  15.98337  1.000 6.75012   ?  35  ASN B N   1 
ATOM   2043 C  CA  . ASN B 1 35  ? 18.74530  -1.33911  16.60088  1.000 8.80693   ?  35  ASN B CA  1 
ATOM   2044 C  C   . ASN B 1 35  ? 19.62358  -2.14875  15.65513  1.000 10.95557  ?  35  ASN B C   1 
ATOM   2045 O  O   . ASN B 1 35  ? 20.11196  -3.24259  15.98646  1.000 9.67979   ?  35  ASN B O   1 
ATOM   2046 C  CB  . ASN B 1 35  ? 18.49794  -2.09501  17.90387  1.000 7.69174   ?  35  ASN B CB  1 
ATOM   2047 C  CG  . ASN B 1 35  ? 18.05642  -1.16062  19.01015  1.000 6.75569   ?  35  ASN B CG  1 
ATOM   2048 O  OD1 . ASN B 1 35  ? 18.88104  -0.46218  19.59707  1.000 8.39940   ?  35  ASN B OD1 1 
ATOM   2049 N  ND2 . ASN B 1 35  ? 16.76076  -1.11775  19.27530  1.000 7.39558   ?  35  ASN B ND2 1 
ATOM   2050 N  N   . GLY B 1 36  ? 19.82375  -1.59174  14.46259  1.000 10.33595  ?  36  GLY B N   1 
ATOM   2051 C  CA  . GLY B 1 36  ? 20.67261  -2.19908  13.46627  1.000 13.00783  ?  36  GLY B CA  1 
ATOM   2052 C  C   . GLY B 1 36  ? 19.98993  -3.16544  12.51840  1.000 10.15333  ?  36  GLY B C   1 
ATOM   2053 O  O   . GLY B 1 36  ? 20.61627  -3.56632  11.53062  1.000 12.23989  ?  36  GLY B O   1 
ATOM   2054 N  N   . THR B 1 37  ? 18.73283  -3.55177  12.77502  1.000 9.38295   ?  37  THR B N   1 
ATOM   2055 C  CA  . THR B 1 37  ? 18.03241  -4.49166  11.90077  1.000 10.96345  ?  37  THR B CA  1 
ATOM   2056 C  C   . THR B 1 37  ? 17.29527  -3.81108  10.75403  1.000 9.15083   ?  37  THR B C   1 
ATOM   2057 O  O   . THR B 1 37  ? 16.79365  -4.51082  9.86952   1.000 9.61470   ?  37  THR B O   1 
ATOM   2058 C  CB  . THR B 1 37  ? 17.01514  -5.33181  12.67946  1.000 8.21315   ?  37  THR B CB  1 
ATOM   2059 O  OG1 . THR B 1 37  ? 15.95024  -4.49421  13.14447  1.000 8.87131   ?  37  THR B OG1 1 
ATOM   2060 C  CG2 . THR B 1 37  ? 17.67199  -6.03069  13.86447  1.000 11.70282  ?  37  THR B CG2 1 
ATOM   2061 N  N   . ARG B 1 38  ? 17.20854  -2.48226  10.75190  1.000 10.75247  ?  38  ARG B N   1 
ATOM   2062 C  CA  . ARG B 1 38  ? 16.37067  -1.74750  9.81217   1.000 10.39275  ?  38  ARG B CA  1 
ATOM   2063 C  C   . ARG B 1 38  ? 17.21137  -0.85260  8.91288   1.000 9.79698   ?  38  ARG B C   1 
ATOM   2064 O  O   . ARG B 1 38  ? 18.19966  -0.25390  9.35328   1.000 11.27300  ?  38  ARG B O   1 
ATOM   2065 C  CB  . ARG B 1 38  ? 15.34639  -0.87733  10.54264  1.000 9.04960   ?  38  ARG B CB  1 
ATOM   2066 C  CG  . ARG B 1 38  ? 14.25464  -0.35548  9.62642   1.000 7.84951   ?  38  ARG B CG  1 
ATOM   2067 C  CD  . ARG B 1 38  ? 13.14501  0.27883   10.42678  1.000 7.46219   ?  38  ARG B CD  1 
ATOM   2068 N  NE  . ARG B 1 38  ? 12.41437  -0.67226  11.25440  1.000 9.12245   ?  38  ARG B NE  1 
ATOM   2069 C  CZ  . ARG B 1 38  ? 11.29334  -0.36538  11.89029  1.000 10.17823  ?  38  ARG B CZ  1 
ATOM   2070 N  NH1 . ARG B 1 38  ? 10.75477  0.84125   11.78378  1.000 6.21496   ?  38  ARG B NH1 1 
ATOM   2071 N  NH2 . ARG B 1 38  ? 10.69971  -1.28806  12.65044  1.000 6.68963   ?  38  ARG B NH2 1 
ATOM   2072 N  N   . PHE B 1 39  ? 16.77946  -0.73090  7.66132   1.000 9.69686   ?  39  PHE B N   1 
ATOM   2073 C  CA  . PHE B 1 39  ? 17.41543  0.10744   6.66341   1.000 10.67326  ?  39  PHE B CA  1 
ATOM   2074 C  C   . PHE B 1 39  ? 16.31980  0.91521   5.97498   1.000 12.85395  ?  39  PHE B C   1 
ATOM   2075 O  O   . PHE B 1 39  ? 15.21873  0.39925   5.75745   1.000 11.76284  ?  39  PHE B O   1 
ATOM   2076 C  CB  . PHE B 1 39  ? 18.21529  -0.77279  5.68002   1.000 12.92888  ?  39  PHE B CB  1 
ATOM   2077 C  CG  . PHE B 1 39  ? 19.23578  -1.65914  6.36634   1.000 11.74307  ?  39  PHE B CG  1 
ATOM   2078 C  CD1 . PHE B 1 39  ? 18.85310  -2.82582  7.01167   1.000 10.65271  ?  39  PHE B CD1 1 
ATOM   2079 C  CD2 . PHE B 1 39  ? 20.56860  -1.29504  6.40236   1.000 17.46803  ?  39  PHE B CD2 1 
ATOM   2080 C  CE1 . PHE B 1 39  ? 19.78642  -3.62143  7.66373   1.000 13.57532  ?  39  PHE B CE1 1 
ATOM   2081 C  CE2 . PHE B 1 39  ? 21.50458  -2.08148  7.05010   1.000 14.41326  ?  39  PHE B CE2 1 
ATOM   2082 C  CZ  . PHE B 1 39  ? 21.11412  -3.24114  7.68353   1.000 15.48175  ?  39  PHE B CZ  1 
ATOM   2083 N  N   . LYS B 1 40  ? 16.58976  2.18994   5.66466   1.000 12.46832  ?  40  LYS B N   1 
ATOM   2084 C  CA  . LYS B 1 40  ? 15.48003  3.07517   5.31875   1.000 12.82536  ?  40  LYS B CA  1 
ATOM   2085 C  C   . LYS B 1 40  ? 15.87865  4.17903   4.35083   1.000 12.87370  ?  40  LYS B C   1 
ATOM   2086 O  O   . LYS B 1 40  ? 17.00023  4.68946   4.39964   1.000 10.11260  ?  40  LYS B O   1 
ATOM   2087 C  CB  . LYS B 1 40  ? 14.87842  3.74855   6.56369   1.000 17.94629  ?  40  LYS B CB  1 
ATOM   2088 C  CG  . LYS B 1 40  ? 13.77212  4.78299   6.23894   1.000 20.12710  ?  40  LYS B CG  1 
ATOM   2089 C  CD  . LYS B 1 40  ? 12.65560  4.76625   7.25155   1.000 19.11815  ?  40  LYS B CD  1 
ATOM   2090 C  CE  . LYS B 1 40  ? 13.31413  4.60787   8.57565   1.000 29.39452  ?  40  LYS B CE  1 
ATOM   2091 N  NZ  . LYS B 1 40  ? 12.43051  4.63224   9.77320   1.000 45.61092  ?  40  LYS B NZ  1 
ATOM   2092 N  N   . ARG B 1 41  ? 14.93117  4.54206   3.48316   1.000 9.06997   ?  41  ARG B N   1 
ATOM   2093 C  CA  . ARG B 1 41  ? 14.88498  5.84150   2.82424   1.000 11.17695  ?  41  ARG B CA  1 
ATOM   2094 C  C   . ARG B 1 41  ? 13.48899  6.42673   2.99911   1.000 12.37687  ?  41  ARG B C   1 
ATOM   2095 O  O   . ARG B 1 41  ? 12.53158  5.71330   3.30365   1.000 10.98784  ?  41  ARG B O   1 
ATOM   2096 C  CB  . ARG B 1 41  ? 15.24701  5.73809   1.33805   1.000 9.96002   ?  41  ARG B CB  1 
ATOM   2097 C  CG  . ARG B 1 41  ? 16.68569  5.32838   1.11340   1.000 9.74896   ?  41  ARG B CG  1 
ATOM   2098 C  CD  . ARG B 1 41  ? 16.99828  5.19146   -0.37466  1.000 11.28924  ?  41  ARG B CD  1 
ATOM   2099 N  NE  . ARG B 1 41  ? 18.41022  4.89904   -0.57554  1.000 15.98785  ?  41  ARG B NE  1 
ATOM   2100 C  CZ  . ARG B 1 41  ? 19.35157  5.82552   -0.69498  1.000 21.36181  ?  41  ARG B CZ  1 
ATOM   2101 N  NH1 . ARG B 1 41  ? 19.05473  7.11760   -0.67135  1.000 15.08620  ?  41  ARG B NH1 1 
ATOM   2102 N  NH2 . ARG B 1 41  ? 20.62270  5.44424   -0.84581  1.000 17.99353  ?  41  ARG B NH2 1 
ATOM   2103 N  N   . PHE B 1 42  ? 13.38473  7.74297   2.82002   1.000 8.54573   ?  42  PHE B N   1 
ATOM   2104 C  CA  . PHE B 1 42  ? 12.18202  8.48226   3.18075   1.000 6.53214   ?  42  PHE B CA  1 
ATOM   2105 C  C   . PHE B 1 42  ? 11.98462  9.64506   2.21350   1.000 12.54939  ?  42  PHE B C   1 
ATOM   2106 O  O   . PHE B 1 42  ? 12.93824  10.36270  1.91138   1.000 10.66536  ?  42  PHE B O   1 
ATOM   2107 C  CB  . PHE B 1 42  ? 12.31644  8.97611   4.62990   1.000 11.47274  ?  42  PHE B CB  1 
ATOM   2108 C  CG  . PHE B 1 42  ? 11.23311  9.90739   5.07925   1.000 10.30398  ?  42  PHE B CG  1 
ATOM   2109 C  CD1 . PHE B 1 42  ? 9.97923   9.42100   5.42260   1.000 9.85680   ?  42  PHE B CD1 1 
ATOM   2110 C  CD2 . PHE B 1 42  ? 11.48850  11.26633  5.22120   1.000 11.31576  ?  42  PHE B CD2 1 
ATOM   2111 C  CE1 . PHE B 1 42  ? 8.98234   10.27198  5.86543   1.000 8.88036   ?  42  PHE B CE1 1 
ATOM   2112 C  CE2 . PHE B 1 42  ? 10.49002  12.13340  5.65327   1.000 16.50063  ?  42  PHE B CE2 1 
ATOM   2113 C  CZ  . PHE B 1 42  ? 9.23089   11.62675  5.97691   1.000 13.64017  ?  42  PHE B CZ  1 
ATOM   2114 N  N   . SER B 1 43  ? 10.75926  9.81395   1.71792   1.000 11.25108  ?  43  SER B N   1 
ATOM   2115 C  CA  . SER B 1 43  ? 10.40951  10.95327  0.87714   1.000 14.03779  ?  43  SER B CA  1 
ATOM   2116 C  C   . SER B 1 43  ? 8.96886   11.34691  1.17073   1.000 10.07420  ?  43  SER B C   1 
ATOM   2117 O  O   . SER B 1 43  ? 8.19296   10.55847  1.71412   1.000 8.87577   ?  43  SER B O   1 
ATOM   2118 C  CB  . SER B 1 43  ? 10.59730  10.64036  -0.61334  1.000 13.87225  ?  43  SER B CB  1 
ATOM   2119 O  OG  . SER B 1 43  ? 11.96924  10.69680  -0.97325  1.000 14.06549  ?  43  SER B OG  1 
ATOM   2120 N  N   . GLN B 1 44  ? 8.61876   12.58891  0.82208   1.000 9.63392   ?  44  GLN B N   1 
ATOM   2121 C  CA  . GLN B 1 44  ? 7.27983   13.10420  1.05806   1.000 11.54307  ?  44  GLN B CA  1 
ATOM   2122 C  C   . GLN B 1 44  ? 6.74931   13.72081  -0.22629  1.000 13.52847  ?  44  GLN B C   1 
ATOM   2123 O  O   . GLN B 1 44  ? 7.51013   14.28186  -1.01270  1.000 12.00640  ?  44  GLN B O   1 
ATOM   2124 C  CB  . GLN B 1 44  ? 7.26798   14.13264  2.21415   1.000 8.36843   ?  44  GLN B CB  1 
ATOM   2125 C  CG  . GLN B 1 44  ? 7.63968   13.49690  3.55518   1.000 11.40749  ?  44  GLN B CG  1 
ATOM   2126 C  CD  . GLN B 1 44  ? 7.92348   14.51928  4.63310   1.000 10.28257  ?  44  GLN B CD  1 
ATOM   2127 O  OE1 . GLN B 1 44  ? 8.91974   15.24019  4.57276   1.000 11.48494  ?  44  GLN B OE1 1 
ATOM   2128 N  NE2 . GLN B 1 44  ? 7.04228   14.60294  5.61350   1.000 10.47194  ?  44  GLN B NE2 1 
ATOM   2129 N  N   . TYR B 1 45  ? 5.44157   13.59890  -0.44345  1.000 9.92264   ?  45  TYR B N   1 
ATOM   2130 C  CA  . TYR B 1 45  ? 4.83145   14.08953  -1.67249  1.000 12.52890  ?  45  TYR B CA  1 
ATOM   2131 C  C   . TYR B 1 45  ? 3.56297   14.86269  -1.36284  1.000 12.95020  ?  45  TYR B C   1 
ATOM   2132 O  O   . TYR B 1 45  ? 2.89260   14.63575  -0.35421  1.000 10.22629  ?  45  TYR B O   1 
ATOM   2133 C  CB  . TYR B 1 45  ? 4.45817   12.95463  -2.65284  1.000 10.58304  ?  45  TYR B CB  1 
ATOM   2134 C  CG  . TYR B 1 45  ? 5.60387   12.14131  -3.20178  1.000 15.66380  ?  45  TYR B CG  1 
ATOM   2135 C  CD1 . TYR B 1 45  ? 6.20920   11.14510  -2.44005  1.000 18.96646  ?  45  TYR B CD1 1 
ATOM   2136 C  CD2 . TYR B 1 45  ? 6.04645   12.32614  -4.50154  1.000 15.08932  ?  45  TYR B CD2 1 
ATOM   2137 C  CE1 . TYR B 1 45  ? 7.24092   10.37996  -2.95407  1.000 16.45424  ?  45  TYR B CE1 1 
ATOM   2138 C  CE2 . TYR B 1 45  ? 7.07781   11.57171  -5.01800  1.000 24.45591  ?  45  TYR B CE2 1 
ATOM   2139 C  CZ  . TYR B 1 45  ? 7.66990   10.60020  -4.24266  1.000 23.83199  ?  45  TYR B CZ  1 
ATOM   2140 O  OH  . TYR B 1 45  ? 8.69122   9.85253   -4.76389  1.000 23.78035  ?  45  TYR B OH  1 
ATOM   2141 N  N   . LYS B 1 46  ? 3.22198   15.76296  -2.27514  1.000 14.62167  ?  46  LYS B N   1 
ATOM   2142 C  CA  . LYS B 1 46  ? 1.90072   16.35755  -2.31707  1.000 11.42814  ?  46  LYS B CA  1 
ATOM   2143 C  C   . LYS B 1 46  ? 1.05470   15.60008  -3.33365  1.000 11.94278  ?  46  LYS B C   1 
ATOM   2144 O  O   . LYS B 1 46  ? 1.53367   15.26820  -4.42112  1.000 14.08403  ?  46  LYS B O   1 
ATOM   2145 C  CB  . LYS B 1 46  ? 2.00105   17.83590  -2.69902  1.000 17.34160  ?  46  LYS B CB  1 
ATOM   2146 C  CG  . LYS B 1 46  ? 0.67851   18.56280  -2.78047  1.000 19.18312  ?  46  LYS B CG  1 
ATOM   2147 C  CD  . LYS B 1 46  ? 0.92739   20.05456  -3.11476  1.000 19.59835  ?  46  LYS B CD  1 
ATOM   2148 C  CE  . LYS B 1 46  ? -0.36167  20.84562  -3.05867  1.000 20.00397  ?  46  LYS B CE  1 
ATOM   2149 N  NZ  . LYS B 1 46  ? -0.24961  22.15781  -3.76241  1.000 15.68372  ?  46  LYS B NZ  1 
ATOM   2150 N  N   . LEU B 1 47  ? -0.19974  15.31575  -2.96459  1.000 14.04339  ?  47  LEU B N   1 
ATOM   2151 C  CA  . LEU B 1 47  ? -1.16848  14.64766  -3.82601  1.000 18.02953  ?  47  LEU B CA  1 
ATOM   2152 C  C   . LEU B 1 47  ? -2.24391  15.65582  -4.17799  1.000 15.68489  ?  47  LEU B C   1 
ATOM   2153 O  O   . LEU B 1 47  ? -2.99921  16.08178  -3.29869  1.000 19.98560  ?  47  LEU B O   1 
ATOM   2154 C  CB  . LEU B 1 47  ? -1.82735  13.45506  -3.14220  1.000 20.25573  ?  47  LEU B CB  1 
ATOM   2155 C  CG  . LEU B 1 47  ? -0.96013  12.30796  -2.71045  1.000 19.22604  ?  47  LEU B CG  1 
ATOM   2156 C  CD1 . LEU B 1 47  ? -1.84831  11.14657  -2.24947  1.000 18.62985  ?  47  LEU B CD1 1 
ATOM   2157 C  CD2 . LEU B 1 47  ? -0.12906  11.95109  -3.89228  1.000 23.37679  ?  47  LEU B CD2 1 
ATOM   2158 N  N   . THR B 1 48  ? -2.34446  15.99745  -5.45846  1.000 22.95599  ?  48  THR B N   1 
ATOM   2159 C  CA  . THR B 1 48  ? -3.32781  16.96710  -5.90034  1.000 30.28616  ?  48  THR B CA  1 
ATOM   2160 C  C   . THR B 1 48  ? -4.30584  16.28107  -6.83637  1.000 29.79678  ?  48  THR B C   1 
ATOM   2161 O  O   . THR B 1 48  ? -3.87734  15.63751  -7.80457  1.000 30.14977  ?  48  THR B O   1 
ATOM   2162 C  CB  . THR B 1 48  ? -2.67344  18.14862  -6.62404  1.000 30.65043  ?  48  THR B CB  1 
ATOM   2163 O  OG1 . THR B 1 48  ? -1.96397  17.66052  -7.76959  1.000 29.92602  ?  48  THR B OG1 1 
ATOM   2164 C  CG2 . THR B 1 48  ? -1.70778  18.86022  -5.71335  1.000 22.76554  ?  48  THR B CG2 1 
ATOM   2165 N  N   . PRO B 1 49  ? -5.60666  16.35345  -6.57299  1.000 31.77298  ?  49  PRO B N   1 
ATOM   2166 C  CA  . PRO B 1 49  ? -6.56446  15.85618  -7.55883  1.000 32.94308  ?  49  PRO B CA  1 
ATOM   2167 C  C   . PRO B 1 49  ? -6.37921  16.63414  -8.84983  1.000 33.87978  ?  49  PRO B C   1 
ATOM   2168 O  O   . PRO B 1 49  ? -6.31132  17.86787  -8.85146  1.000 38.03788  ?  49  PRO B O   1 
ATOM   2169 C  CB  . PRO B 1 49  ? -7.92658  16.11248  -6.90394  1.000 28.47981  ?  49  PRO B CB  1 
ATOM   2170 C  CG  . PRO B 1 49  ? -7.67153  17.11973  -5.84555  1.000 32.78019  ?  49  PRO B CG  1 
ATOM   2171 C  CD  . PRO B 1 49  ? -6.26962  16.91185  -5.38372  1.000 32.05173  ?  49  PRO B CD  1 
ATOM   2172 N  N   . ALA B 1 50  ? -6.21307  15.90207  -9.93607  1.000 27.81223  ?  50  ALA B N   1 
ATOM   2173 C  CA  . ALA B 1 50  ? -5.92278  16.50199  -11.22572 1.000 45.97652  ?  50  ALA B CA  1 
ATOM   2174 C  C   . ALA B 1 50  ? -7.17420  16.51197  -12.09040 1.000 53.06625  ?  50  ALA B C   1 
ATOM   2175 O  O   . ALA B 1 50  ? -8.20122  15.91549  -11.75173 1.000 47.39085  ?  50  ALA B O   1 
ATOM   2176 C  CB  . ALA B 1 50  ? -4.79065  15.74574  -11.93003 1.000 38.39715  ?  50  ALA B CB  1 
ATOM   2177 N  N   . GLU B 1 51  ? -7.07903  17.21790  -13.21789 1.000 49.27992  ?  51  GLU B N   1 
ATOM   2178 C  CA  . GLU B 1 51  ? -8.06598  17.05503  -14.27353 1.000 55.85239  ?  51  GLU B CA  1 
ATOM   2179 C  C   . GLU B 1 51  ? -8.22489  15.57317  -14.58557 1.000 57.58506  ?  51  GLU B C   1 
ATOM   2180 O  O   . GLU B 1 51  ? -7.28884  14.78315  -14.41229 1.000 50.85657  ?  51  GLU B O   1 
ATOM   2181 C  CB  . GLU B 1 51  ? -7.63880  17.82106  -15.52464 1.000 48.91424  ?  51  GLU B CB  1 
ATOM   2182 C  CG  . GLU B 1 51  ? -8.77724  18.21225  -16.44241 1.000 54.87084  ?  51  GLU B CG  1 
ATOM   2183 C  CD  . GLU B 1 51  ? -8.28757  18.99389  -17.63897 1.000 58.97105  ?  51  GLU B CD  1 
ATOM   2184 O  OE1 . GLU B 1 51  ? -7.06239  18.96987  -17.89831 1.000 65.01792  ?  51  GLU B OE1 1 
ATOM   2185 O  OE2 . GLU B 1 51  ? -9.12204  19.63483  -18.31429 1.000 66.52499  -1 51  GLU B OE2 1 
ATOM   2186 N  N   . ASP B 1 52  ? -9.42745  15.20228  -15.03788 1.000 66.76067  ?  52  ASP B N   1 
ATOM   2187 C  CA  . ASP B 1 52  ? -9.84465  13.80637  -15.12947 1.000 61.18084  ?  52  ASP B CA  1 
ATOM   2188 C  C   . ASP B 1 52  ? -10.04956 13.28683  -13.71033 1.000 60.89236  ?  52  ASP B C   1 
ATOM   2189 O  O   . ASP B 1 52  ? -10.09384 14.07838  -12.76231 1.000 63.69006  ?  52  ASP B O   1 
ATOM   2190 C  CB  . ASP B 1 52  ? -8.81358  12.96973  -15.90045 1.000 61.28516  ?  52  ASP B CB  1 
ATOM   2191 C  CG  . ASP B 1 52  ? -9.40626  11.73729  -16.52558 1.000 67.53077  ?  52  ASP B CG  1 
ATOM   2192 O  OD1 . ASP B 1 52  ? -10.22997 11.88988  -17.45386 1.000 73.93012  -1 52  ASP B OD1 1 
ATOM   2193 O  OD2 . ASP B 1 52  ? -9.03432  10.62058  -16.10000 1.000 65.45916  -1 52  ASP B OD2 1 
ATOM   2194 N  N   . ASP B 1 53  ? -10.19214 11.97473  -13.54234 1.000 63.12955  ?  53  ASP B N   1 
ATOM   2195 C  CA  . ASP B 1 53  ? -10.21017 11.38345  -12.20426 1.000 58.16267  ?  53  ASP B CA  1 
ATOM   2196 C  C   . ASP B 1 53  ? -8.83300  10.87703  -11.80085 1.000 57.17084  ?  53  ASP B C   1 
ATOM   2197 O  O   . ASP B 1 53  ? -8.69071  9.77060   -11.27037 1.000 53.24042  ?  53  ASP B O   1 
ATOM   2198 C  CB  . ASP B 1 53  ? -11.24800 10.26707  -12.13662 1.000 58.84268  ?  53  ASP B CB  1 
ATOM   2199 C  CG  . ASP B 1 53  ? -12.34412 10.55027  -11.12269 1.000 65.26986  ?  53  ASP B CG  1 
ATOM   2200 O  OD1 . ASP B 1 53  ? -12.92183 11.66005  -11.16580 1.000 64.93692  ?  53  ASP B OD1 1 
ATOM   2201 O  OD2 . ASP B 1 53  ? -12.63195 9.66195   -10.28995 1.000 60.55930  -1 53  ASP B OD2 1 
ATOM   2202 N  N   . THR B 1 54  ? -7.80152  11.67675  -12.05609 1.000 49.68987  ?  54  THR B N   1 
ATOM   2203 C  CA  . THR B 1 54  ? -6.41115  11.32122  -11.81951 1.000 48.86688  ?  54  THR B CA  1 
ATOM   2204 C  C   . THR B 1 54  ? -5.86423  12.09304  -10.62828 1.000 37.73304  ?  54  THR B C   1 
ATOM   2205 O  O   . THR B 1 54  ? -6.47981  13.03573  -10.12225 1.000 41.54825  ?  54  THR B O   1 
ATOM   2206 C  CB  . THR B 1 54  ? -5.55898  11.61533  -13.05630 1.000 41.69606  ?  54  THR B CB  1 
ATOM   2207 O  OG1 . THR B 1 54  ? -5.73696  12.98761  -13.43070 1.000 50.07478  ?  54  THR B OG1 1 
ATOM   2208 C  CG2 . THR B 1 54  ? -5.96864  10.71968  -14.20901 1.000 54.91145  ?  54  THR B CG2 1 
ATOM   2209 N  N   . TRP B 1 55  ? -4.67958  11.68583  -10.19256 1.000 33.98290  ?  55  TRP B N   1 
ATOM   2210 C  CA  . TRP B 1 55  ? -3.97898  12.34698  -9.10372  1.000 31.76906  ?  55  TRP B CA  1 
ATOM   2211 C  C   . TRP B 1 55  ? -2.55806  12.63773  -9.54723  1.000 24.81060  ?  55  TRP B C   1 
ATOM   2212 O  O   . TRP B 1 55  ? -1.90817  11.79206  -10.16397 1.000 26.74896  ?  55  TRP B O   1 
ATOM   2213 C  CB  . TRP B 1 55  ? -3.94958  11.48776  -7.82762  1.000 32.92787  ?  55  TRP B CB  1 
ATOM   2214 C  CG  . TRP B 1 55  ? -5.25941  11.37704  -7.12662  1.000 25.31087  ?  55  TRP B CG  1 
ATOM   2215 C  CD1 . TRP B 1 55  ? -6.26801  10.49915  -7.40370  1.000 26.14893  ?  55  TRP B CD1 1 
ATOM   2216 C  CD2 . TRP B 1 55  ? -5.70065  12.15448  -6.01222  1.000 22.32640  ?  55  TRP B CD2 1 
ATOM   2217 N  NE1 . TRP B 1 55  ? -7.31049  10.68602  -6.52966  1.000 23.98636  ?  55  TRP B NE1 1 
ATOM   2218 C  CE2 . TRP B 1 55  ? -6.99003  11.70143  -5.67003  1.000 18.55283  ?  55  TRP B CE2 1 
ATOM   2219 C  CE3 . TRP B 1 55  ? -5.13176  13.19150  -5.26895  1.000 23.33141  ?  55  TRP B CE3 1 
ATOM   2220 C  CZ2 . TRP B 1 55  ? -7.71756  12.24839  -4.61905  1.000 21.29932  ?  55  TRP B CZ2 1 
ATOM   2221 C  CZ3 . TRP B 1 55  ? -5.85427  13.73214  -4.22837  1.000 29.71428  ?  55  TRP B CZ3 1 
ATOM   2222 C  CH2 . TRP B 1 55  ? -7.13495  13.26161  -3.91201  1.000 28.40643  ?  55  TRP B CH2 1 
ATOM   2223 N  N   . SER B 1 56  ? -2.07631  13.82839  -9.23030  1.000 24.28911  ?  56  SER B N   1 
ATOM   2224 C  CA  . SER B 1 56  ? -0.71832  14.21908  -9.56843  1.000 32.12700  ?  56  SER B CA  1 
ATOM   2225 C  C   . SER B 1 56  ? 0.15503   14.16749  -8.31938  1.000 25.73559  ?  56  SER B C   1 
ATOM   2226 O  O   . SER B 1 56  ? -0.27066  14.58857  -7.23923  1.000 26.28538  ?  56  SER B O   1 
ATOM   2227 C  CB  . SER B 1 56  ? -0.69393  15.61748  -10.18244 1.000 30.39917  ?  56  SER B CB  1 
ATOM   2228 O  OG  . SER B 1 56  ? 0.62738   15.98116  -10.55414 1.000 41.20373  ?  56  SER B OG  1 
ATOM   2229 N  N   . PHE B 1 57  ? 1.36780   13.63676  -8.47385  1.000 19.12613  ?  57  PHE B N   1 
ATOM   2230 C  CA  . PHE B 1 57  ? 2.34563   13.53963  -7.39310  1.000 25.19568  ?  57  PHE B CA  1 
ATOM   2231 C  C   . PHE B 1 57  ? 3.43566   14.58590  -7.57618  1.000 21.34376  ?  57  PHE B C   1 
ATOM   2232 O  O   . PHE B 1 57  ? 4.03615   14.67075  -8.65070  1.000 28.49023  ?  57  PHE B O   1 
ATOM   2233 C  CB  . PHE B 1 57  ? 3.01822   12.17013  -7.37209  1.000 15.71496  ?  57  PHE B CB  1 
ATOM   2234 C  CG  . PHE B 1 57  ? 2.10358   11.02649  -7.06391  1.000 20.56365  ?  57  PHE B CG  1 
ATOM   2235 C  CD1 . PHE B 1 57  ? 1.22826   10.54254  -8.01807  1.000 26.09374  ?  57  PHE B CD1 1 
ATOM   2236 C  CD2 . PHE B 1 57  ? 2.16993   10.39069  -5.83518  1.000 23.65117  ?  57  PHE B CD2 1 
ATOM   2237 C  CE1 . PHE B 1 57  ? 0.40517   9.47033   -7.74407  1.000 26.64569  ?  57  PHE B CE1 1 
ATOM   2238 C  CE2 . PHE B 1 57  ? 1.35194   9.30880   -5.55400  1.000 23.15901  ?  57  PHE B CE2 1 
ATOM   2239 C  CZ  . PHE B 1 57  ? 0.46312   8.85423   -6.50620  1.000 28.00876  ?  57  PHE B CZ  1 
ATOM   2240 N  N   . LYS B 1 58  ? 3.73213   15.33898  -6.51959  1.000 22.11613  ?  58  LYS B N   1 
ATOM   2241 C  CA  . LYS B 1 58  ? 4.87759   16.23831  -6.51609  1.000 17.79962  ?  58  LYS B CA  1 
ATOM   2242 C  C   . LYS B 1 58  ? 5.72972   15.93981  -5.29437  1.000 16.47756  ?  58  LYS B C   1 
ATOM   2243 O  O   . LYS B 1 58  ? 5.25646   16.07759  -4.16189  1.000 16.45289  ?  58  LYS B O   1 
ATOM   2244 C  CB  . LYS B 1 58  ? 4.44551   17.70166  -6.51827  1.000 19.93337  ?  58  LYS B CB  1 
ATOM   2245 C  CG  . LYS B 1 58  ? 5.58498   18.64953  -6.17188  1.000 28.02278  ?  58  LYS B CG  1 
ATOM   2246 C  CD  . LYS B 1 58  ? 5.17425   20.10006  -6.29341  1.000 26.79771  ?  58  LYS B CD  1 
ATOM   2247 C  CE  . LYS B 1 58  ? 5.56488   20.64167  -7.65521  1.000 44.03201  ?  58  LYS B CE  1 
ATOM   2248 N  NZ  . LYS B 1 58  ? 6.96995   20.25208  -7.98888  1.000 49.39789  ?  58  LYS B NZ  1 
ATOM   2249 N  N   . ARG B 1 59  ? 6.97349   15.52233  -5.53257  1.000 15.80868  ?  59  ARG B N   1 
ATOM   2250 C  CA  . ARG B 1 59  ? 7.92697   15.28017  -4.45620  1.000 19.42597  ?  59  ARG B CA  1 
ATOM   2251 C  C   . ARG B 1 59  ? 8.31211   16.60210  -3.80237  1.000 21.17667  ?  59  ARG B C   1 
ATOM   2252 O  O   . ARG B 1 59  ? 8.73840   17.54324  -4.48069  1.000 16.38028  ?  59  ARG B O   1 
ATOM   2253 C  CB  . ARG B 1 59  ? 9.17151   14.56884  -4.99913  1.000 21.03268  ?  59  ARG B CB  1 
ATOM   2254 C  CG  . ARG B 1 59  ? 10.11284  14.01843  -3.92692  1.000 22.05069  ?  59  ARG B CG  1 
ATOM   2255 C  CD  . ARG B 1 59  ? 11.47469  13.59041  -4.51966  1.000 31.46804  ?  59  ARG B CD  1 
ATOM   2256 N  NE  . ARG B 1 59  ? 11.38213  12.39785  -5.35932  1.000 40.84037  ?  59  ARG B NE  1 
ATOM   2257 C  CZ  . ARG B 1 59  ? 11.83996  11.19891  -5.01662  1.000 34.04629  ?  59  ARG B CZ  1 
ATOM   2258 N  NH1 . ARG B 1 59  ? 12.46923  11.00079  -3.87014  1.000 23.15397  ?  59  ARG B NH1 1 
ATOM   2259 N  NH2 . ARG B 1 59  ? 11.67053  10.17290  -5.84940  1.000 31.02357  ?  59  ARG B NH2 1 
ATOM   2260 N  N   . LEU B 1 60  ? 8.15536   16.67316  -2.47312  1.000 16.86727  ?  60  LEU B N   1 
ATOM   2261 C  CA  . LEU B 1 60  ? 8.40384   17.88832  -1.71911  1.000 14.55923  ?  60  LEU B CA  1 
ATOM   2262 C  C   . LEU B 1 60  ? 9.88049   17.99997  -1.37834  1.000 16.11702  ?  60  LEU B C   1 
ATOM   2263 O  O   . LEU B 1 60  ? 10.59352  16.99286  -1.34704  1.000 15.13805  ?  60  LEU B O   1 
ATOM   2264 C  CB  . LEU B 1 60  ? 7.56040   17.88531  -0.44156  1.000 16.02461  ?  60  LEU B CB  1 
ATOM   2265 C  CG  . LEU B 1 60  ? 6.05760   17.78717  -0.71304  1.000 12.03312  ?  60  LEU B CG  1 
ATOM   2266 C  CD1 . LEU B 1 60  ? 5.26336   17.50906  0.54491   1.000 14.91737  ?  60  LEU B CD1 1 
ATOM   2267 C  CD2 . LEU B 1 60  ? 5.58307   19.07499  -1.36722  1.000 25.25194  ?  60  LEU B CD2 1 
ATOM   2268 N  N   . PRO B 1 61  ? 10.38066  19.21256  -1.13116  1.000 13.56802  ?  61  PRO B N   1 
ATOM   2269 C  CA  . PRO B 1 61  ? 11.77684  19.35449  -0.69422  1.000 14.58383  ?  61  PRO B CA  1 
ATOM   2270 C  C   . PRO B 1 61  ? 12.07838  18.46089  0.50183   1.000 12.30086  ?  61  PRO B C   1 
ATOM   2271 O  O   . PRO B 1 61  ? 11.26215  18.30720  1.41217   1.000 12.62639  ?  61  PRO B O   1 
ATOM   2272 C  CB  . PRO B 1 61  ? 11.88617  20.84072  -0.33306  1.000 20.29780  ?  61  PRO B CB  1 
ATOM   2273 C  CG  . PRO B 1 61  ? 10.90183  21.49941  -1.25583  1.000 20.72284  ?  61  PRO B CG  1 
ATOM   2274 C  CD  . PRO B 1 61  ? 9.73546   20.52046  -1.34395  1.000 21.04578  ?  61  PRO B CD  1 
ATOM   2275 N  N   . HIS B 1 62  ? 13.26070  17.85958  0.47757   1.000 12.34895  ?  62  HIS B N   1 
ATOM   2276 C  CA  . HIS B 1 62  ? 13.59668  16.80168  1.41738   1.000 15.75024  ?  62  HIS B CA  1 
ATOM   2277 C  C   . HIS B 1 62  ? 13.75818  17.35969  2.82759   1.000 18.33683  ?  62  HIS B C   1 
ATOM   2278 O  O   . HIS B 1 62  ? 14.51176  18.31457  3.04473   1.000 18.93214  ?  62  HIS B O   1 
ATOM   2279 C  CB  . HIS B 1 62  ? 14.88584  16.12155  0.97133   1.000 17.22066  ?  62  HIS B CB  1 
ATOM   2280 C  CG  . HIS B 1 62  ? 15.23238  14.92053  1.78168   1.000 14.39733  ?  62  HIS B CG  1 
ATOM   2281 N  ND1 . HIS B 1 62  ? 14.44496  13.79041  1.79713   1.000 12.82410  ?  62  HIS B ND1 1 
ATOM   2282 C  CD2 . HIS B 1 62  ? 16.27455  14.67147  2.60957   1.000 20.11325  ?  62  HIS B CD2 1 
ATOM   2283 C  CE1 . HIS B 1 62  ? 14.99297  12.88933  2.59419   1.000 16.72599  ?  62  HIS B CE1 1 
ATOM   2284 N  NE2 . HIS B 1 62  ? 16.10263  13.40152  3.10218   1.000 18.06108  ?  62  HIS B NE2 1 
ATOM   2285 N  N   . ARG B 1 63  ? 13.05826  16.75708  3.79137   1.000 12.29755  ?  63  ARG B N   1 
ATOM   2286 C  CA  . ARG B 1 63  ? 13.13640  17.18531  5.18161   1.000 10.38511  ?  63  ARG B CA  1 
ATOM   2287 C  C   . ARG B 1 63  ? 13.27895  15.97811  6.09592   1.000 16.60817  ?  63  ARG B C   1 
ATOM   2288 O  O   . ARG B 1 63  ? 12.85722  14.86909  5.75524   1.000 11.02185  ?  63  ARG B O   1 
ATOM   2289 C  CB  . ARG B 1 63  ? 11.90319  17.98479  5.60661   1.000 12.06216  ?  63  ARG B CB  1 
ATOM   2290 C  CG  . ARG B 1 63  ? 11.78116  19.33218  4.89886   1.000 17.64018  ?  63  ARG B CG  1 
ATOM   2291 C  CD  . ARG B 1 63  ? 10.48038  20.01420  5.23755   1.000 19.64412  ?  63  ARG B CD  1 
ATOM   2292 N  NE  . ARG B 1 63  ? 10.41263  20.45808  6.62596   1.000 24.09481  ?  63  ARG B NE  1 
ATOM   2293 C  CZ  . ARG B 1 63  ? 10.73257  21.67870  7.03566   1.000 22.26974  ?  63  ARG B CZ  1 
ATOM   2294 N  NH1 . ARG B 1 63  ? 11.23449  22.58008  6.20250   1.000 20.10057  ?  63  ARG B NH1 1 
ATOM   2295 N  NH2 . ARG B 1 63  ? 10.53308  22.00718  8.30779   1.000 20.00146  ?  63  ARG B NH2 1 
ATOM   2296 N  N   . ASP B 1 64  ? 13.88122  16.21160  7.26648   1.000 10.49988  ?  64  ASP B N   1 
ATOM   2297 C  CA  . ASP B 1 64  ? 13.89676  15.20838  8.32506   1.000 11.60683  ?  64  ASP B CA  1 
ATOM   2298 C  C   . ASP B 1 64  ? 12.48573  14.71603  8.61552   1.000 14.43918  ?  64  ASP B C   1 
ATOM   2299 O  O   . ASP B 1 64  ? 11.52470  15.48295  8.56860   1.000 14.67594  ?  64  ASP B O   1 
ATOM   2300 C  CB  . ASP B 1 64  ? 14.47193  15.77561  9.62529   1.000 10.61090  ?  64  ASP B CB  1 
ATOM   2301 C  CG  . ASP B 1 64  ? 15.88678  16.30790  9.48437   1.000 19.96947  ?  64  ASP B CG  1 
ATOM   2302 O  OD1 . ASP B 1 64  ? 16.57836  16.00592  8.49463   1.000 18.14060  ?  64  ASP B OD1 1 
ATOM   2303 O  OD2 . ASP B 1 64  ? 16.31349  17.03388  10.40676  1.000 16.79501  -1 64  ASP B OD2 1 
ATOM   2304 N  N   . TYR B 1 65  ? 12.38000  13.44236  8.97442   1.000 10.56393  ?  65  TYR B N   1 
ATOM   2305 C  CA  . TYR B 1 65  ? 11.11175  12.87041  9.39257   1.000 9.61445   ?  65  TYR B CA  1 
ATOM   2306 C  C   . TYR B 1 65  ? 10.89516  13.21340  10.85961  1.000 10.34328  ?  65  TYR B C   1 
ATOM   2307 O  O   . TYR B 1 65  ? 11.81851  13.09421  11.66948  1.000 8.02078   ?  65  TYR B O   1 
ATOM   2308 C  CB  . TYR B 1 65  ? 11.11706  11.35362  9.16632   1.000 11.45263  ?  65  TYR B CB  1 
ATOM   2309 C  CG  . TYR B 1 65  ? 9.89885   10.65219  9.73758   1.000 10.92050  ?  65  TYR B CG  1 
ATOM   2310 C  CD1 . TYR B 1 65  ? 8.61800   11.05254  9.37730   1.000 9.23852   ?  65  TYR B CD1 1 
ATOM   2311 C  CD2 . TYR B 1 65  ? 10.03171  9.59247   10.63037  1.000 10.76964  ?  65  TYR B CD2 1 
ATOM   2312 C  CE1 . TYR B 1 65  ? 7.50254   10.42914  9.89983   1.000 9.38108   ?  65  TYR B CE1 1 
ATOM   2313 C  CE2 . TYR B 1 65  ? 8.92027   8.95269   11.15603  1.000 12.50438  ?  65  TYR B CE2 1 
ATOM   2314 C  CZ  . TYR B 1 65  ? 7.65694   9.37431   10.78478  1.000 9.94039   ?  65  TYR B CZ  1 
ATOM   2315 O  OH  . TYR B 1 65  ? 6.55938   8.74293   11.30720  1.000 9.85811   ?  65  TYR B OH  1 
ATOM   2316 N  N   . THR B 1 66  ? 9.70469   13.71181  11.19084  1.000 10.78259  ?  66  THR B N   1 
ATOM   2317 C  CA  . THR B 1 66  ? 9.33780   13.95381  12.58268  1.000 10.75794  ?  66  THR B CA  1 
ATOM   2318 C  C   . THR B 1 66  ? 7.95072   13.39574  12.83820  1.000 10.23708  ?  66  THR B C   1 
ATOM   2319 O  O   . THR B 1 66  ? 7.03536   13.58942  12.02899  1.000 11.23963  ?  66  THR B O   1 
ATOM   2320 C  CB  . THR B 1 66  ? 9.33851   15.44025  12.93248  1.000 12.13504  ?  66  THR B CB  1 
ATOM   2321 O  OG1 . THR B 1 66  ? 8.39956   16.10698  12.08247  1.000 12.91802  ?  66  THR B OG1 1 
ATOM   2322 C  CG2 . THR B 1 66  ? 10.71910  16.03744  12.73459  1.000 14.16631  ?  66  THR B CG2 1 
ATOM   2323 N  N   . THR B 1 67  ? 7.79160   12.69953  13.96363  1.000 7.49443   ?  67  THR B N   1 
ATOM   2324 C  CA  . THR B 1 67  ? 6.48071   12.23576  14.38451  1.000 7.82548   ?  67  THR B CA  1 
ATOM   2325 C  C   . THR B 1 67  ? 6.32971   12.53020  15.87149  1.000 11.82548  ?  67  THR B C   1 
ATOM   2326 O  O   . THR B 1 67  ? 7.25421   13.02814  16.52409  1.000 9.11936   ?  67  THR B O   1 
ATOM   2327 C  CB  . THR B 1 67  ? 6.26835   10.75062  14.05291  1.000 10.50029  ?  67  THR B CB  1 
ATOM   2328 O  OG1 . THR B 1 67  ? 4.91980   10.40082  14.35505  1.000 8.90419   ?  67  THR B OG1 1 
ATOM   2329 C  CG2 . THR B 1 67  ? 7.18658   9.86181   14.86740  1.000 10.05992  ?  67  THR B CG2 1 
ATOM   2330 N  N   . TYR B 1 68  ? 5.15124   12.24032  16.40888  1.000 8.96720   ?  68  TYR B N   1 
ATOM   2331 C  CA  . TYR B 1 68  ? 4.83821   12.55712  17.80096  1.000 13.08136  ?  68  TYR B CA  1 
ATOM   2332 C  C   . TYR B 1 68  ? 5.12413   11.38068  18.71950  1.000 12.43094  ?  68  TYR B C   1 
ATOM   2333 O  O   . TYR B 1 68  ? 4.83261   10.23154  18.37266  1.000 11.25538  ?  68  TYR B O   1 
ATOM   2334 C  CB  . TYR B 1 68  ? 3.36234   12.91076  17.96464  1.000 12.92800  ?  68  TYR B CB  1 
ATOM   2335 C  CG  . TYR B 1 68  ? 2.86664   14.11312  17.20684  1.000 11.32471  ?  68  TYR B CG  1 
ATOM   2336 C  CD1 . TYR B 1 68  ? 2.61682   14.05100  15.83531  1.000 13.69641  ?  68  TYR B CD1 1 
ATOM   2337 C  CD2 . TYR B 1 68  ? 2.58992   15.29504  17.87613  1.000 18.00295  ?  68  TYR B CD2 1 
ATOM   2338 C  CE1 . TYR B 1 68  ? 2.13053   15.15391  15.15143  1.000 14.41893  ?  68  TYR B CE1 1 
ATOM   2339 C  CE2 . TYR B 1 68  ? 2.10705   16.40367  17.20099  1.000 14.88235  ?  68  TYR B CE2 1 
ATOM   2340 C  CZ  . TYR B 1 68  ? 1.87730   16.32610  15.84879  1.000 15.19232  ?  68  TYR B CZ  1 
ATOM   2341 O  OH  . TYR B 1 68  ? 1.39488   17.44376  15.20055  1.000 15.48513  ?  68  TYR B OH  1 
ATOM   2342 N  N   . LYS B 1 69  ? 5.62652   11.68667  19.92640  1.000 11.33252  ?  69  LYS B N   1 
ATOM   2343 C  CA  . LYS B 1 69  ? 5.77209   10.66533  20.96735  1.000 13.95148  ?  69  LYS B CA  1 
ATOM   2344 C  C   . LYS B 1 69  ? 4.44571   10.00433  21.30048  1.000 13.73567  ?  69  LYS B C   1 
ATOM   2345 O  O   . LYS B 1 69  ? 4.41231   8.81727   21.62841  1.000 10.53437  ?  69  LYS B O   1 
ATOM   2346 C  CB  . LYS B 1 69  ? 6.35242   11.28062  22.24310  1.000 18.38458  ?  69  LYS B CB  1 
ATOM   2347 C  CG  . LYS B 1 69  ? 7.81992   11.60167  22.18480  1.000 29.36407  ?  69  LYS B CG  1 
ATOM   2348 C  CD  . LYS B 1 69  ? 8.66168   10.34476  22.40302  1.000 34.53914  ?  69  LYS B CD  1 
ATOM   2349 C  CE  . LYS B 1 69  ? 8.69208   9.91036   23.87400  1.000 36.33213  ?  69  LYS B CE  1 
ATOM   2350 N  NZ  . LYS B 1 69  ? 9.37918   8.58455   24.08766  1.000 29.38461  ?  69  LYS B NZ  1 
ATOM   2351 N  N   . LYS B 1 70  ? 3.33979   10.74526  21.21787  1.000 13.50114  ?  70  LYS B N   1 
ATOM   2352 C  CA  . LYS B 1 70  ? 2.06158   10.16480  21.60872  1.000 17.59468  ?  70  LYS B CA  1 
ATOM   2353 C  C   . LYS B 1 70  ? 1.61815   9.05652   20.66425  1.000 15.19229  ?  70  LYS B C   1 
ATOM   2354 O  O   . LYS B 1 70  ? 0.83498   8.19623   21.07352  1.000 17.00366  ?  70  LYS B O   1 
ATOM   2355 C  CB  . LYS B 1 70  ? 0.98429   11.25298  21.71683  1.000 15.30861  ?  70  LYS B CB  1 
ATOM   2356 C  CG  . LYS B 1 70  ? 0.50393   11.83715  20.40009  1.000 16.63500  ?  70  LYS B CG  1 
ATOM   2357 C  CD  . LYS B 1 70  ? -0.34750  13.08934  20.64581  1.000 29.90265  ?  70  LYS B CD  1 
ATOM   2358 C  CE  . LYS B 1 70  ? -0.70987  13.80595  19.35231  1.000 22.05495  ?  70  LYS B CE  1 
ATOM   2359 N  NZ  . LYS B 1 70  ? -0.87493  15.28328  19.54486  1.000 30.27503  ?  70  LYS B NZ  1 
ATOM   2360 N  N   . PHE B 1 71  ? 2.12590   9.03020   19.43125  1.000 13.11972  ?  71  PHE B N   1 
ATOM   2361 C  CA  . PHE B 1 71  ? 1.84259   7.93840   18.51045  1.000 9.66269   ?  71  PHE B CA  1 
ATOM   2362 C  C   . PHE B 1 71  ? 2.95107   6.90176   18.46646  1.000 10.57394  ?  71  PHE B C   1 
ATOM   2363 O  O   . PHE B 1 71  ? 2.67834   5.71803   18.25843  1.000 14.27998  ?  71  PHE B O   1 
ATOM   2364 C  CB  . PHE B 1 71  ? 1.63194   8.47146   17.08884  1.000 16.31101  ?  71  PHE B CB  1 
ATOM   2365 C  CG  . PHE B 1 71  ? 0.50229   9.44593   16.97264  1.000 13.51190  ?  71  PHE B CG  1 
ATOM   2366 C  CD1 . PHE B 1 71  ? -0.77733  9.08080   17.33391  1.000 12.19878  ?  71  PHE B CD1 1 
ATOM   2367 C  CD2 . PHE B 1 71  ? 0.72905   10.73117  16.50619  1.000 15.93622  ?  71  PHE B CD2 1 
ATOM   2368 C  CE1 . PHE B 1 71  ? -1.82570  9.98409   17.23472  1.000 16.54140  ?  71  PHE B CE1 1 
ATOM   2369 C  CE2 . PHE B 1 71  ? -0.30800  11.64566  16.41361  1.000 16.56449  ?  71  PHE B CE2 1 
ATOM   2370 C  CZ  . PHE B 1 71  ? -1.58505  11.26613  16.77422  1.000 18.43258  ?  71  PHE B CZ  1 
ATOM   2371 N  N   . ASN B 1 72  ? 4.19570   7.33024   18.63808  1.000 12.43261  ?  72  ASN B N   1 
ATOM   2372 C  CA  . ASN B 1 72  ? 5.36026   6.46511   18.48222  1.000 11.59073  ?  72  ASN B CA  1 
ATOM   2373 C  C   . ASN B 1 72  ? 6.26551   6.67128   19.69164  1.000 9.81083   ?  72  ASN B C   1 
ATOM   2374 O  O   . ASN B 1 72  ? 7.07175   7.61130   19.70895  1.000 10.84567  ?  72  ASN B O   1 
ATOM   2375 C  CB  . ASN B 1 72  ? 6.08916   6.78027   17.18418  1.000 12.25661  ?  72  ASN B CB  1 
ATOM   2376 C  CG  . ASN B 1 72  ? 7.19783   5.79573   16.88232  1.000 14.52538  ?  72  ASN B CG  1 
ATOM   2377 O  OD1 . ASN B 1 72  ? 7.75529   5.17748   17.78847  1.000 11.44770  ?  72  ASN B OD1 1 
ATOM   2378 N  ND2 . ASN B 1 72  ? 7.51931   5.63773   15.59678  1.000 13.20914  ?  72  ASN B ND2 1 
ATOM   2379 N  N   . PRO B 1 73  ? 6.18260   5.81046   20.70632  1.000 12.27216  ?  73  PRO B N   1 
ATOM   2380 C  CA  . PRO B 1 73  ? 6.95008   6.05689   21.93489  1.000 16.44826  ?  73  PRO B CA  1 
ATOM   2381 C  C   . PRO B 1 73  ? 8.43402   5.79749   21.79378  1.000 16.85584  ?  73  PRO B C   1 
ATOM   2382 O  O   . PRO B 1 73  ? 9.20782   6.24840   22.64665  1.000 16.38858  ?  73  PRO B O   1 
ATOM   2383 C  CB  . PRO B 1 73  ? 6.31738   5.08507   22.94029  1.000 18.36950  ?  73  PRO B CB  1 
ATOM   2384 C  CG  . PRO B 1 73  ? 5.79318   3.98358   22.08893  1.000 20.94607  ?  73  PRO B CG  1 
ATOM   2385 C  CD  . PRO B 1 73  ? 5.29989   4.64460   20.83165  1.000 14.91907  ?  73  PRO B CD  1 
ATOM   2386 N  N   . VAL B 1 74  ? 8.86093   5.08897   20.75388  1.000 9.04710   ?  74  VAL B N   1 
ATOM   2387 C  CA  . VAL B 1 74  ? 10.26726  4.73938   20.60929  1.000 10.33842  ?  74  VAL B CA  1 
ATOM   2388 C  C   . VAL B 1 74  ? 10.98774  5.59217   19.56608  1.000 14.58210  ?  74  VAL B C   1 
ATOM   2389 O  O   . VAL B 1 74  ? 12.21862  5.73412   19.64024  1.000 12.02886  ?  74  VAL B O   1 
ATOM   2390 C  CB  . VAL B 1 74  ? 10.40969  3.23685   20.28743  1.000 15.30902  ?  74  VAL B CB  1 
ATOM   2391 C  CG1 . VAL B 1 74  ? 9.97289   2.40156   21.49739  1.000 15.82244  ?  74  VAL B CG1 1 
ATOM   2392 C  CG2 . VAL B 1 74  ? 9.60776   2.85143   19.02186  1.000 12.32476  ?  74  VAL B CG2 1 
ATOM   2393 N  N   . GLY B 1 75  ? 10.26692  6.18685   18.62704  1.000 8.24858   ?  75  GLY B N   1 
ATOM   2394 C  CA  . GLY B 1 75  ? 10.90149  6.96882   17.59222  1.000 9.76787   ?  75  GLY B CA  1 
ATOM   2395 C  C   . GLY B 1 75  ? 10.24571  8.31118   17.34367  1.000 7.50053   ?  75  GLY B C   1 
ATOM   2396 O  O   . GLY B 1 75  ? 10.48918  8.92231   16.30188  1.000 10.30439  ?  75  GLY B O   1 
ATOM   2397 N  N   . GLY B 1 76  ? 9.42152   8.77917   18.29174  1.000 8.19453   ?  76  GLY B N   1 
ATOM   2398 C  CA  . GLY B 1 76  ? 8.72268   10.03937  18.15649  1.000 10.49937  ?  76  GLY B CA  1 
ATOM   2399 C  C   . GLY B 1 76  ? 9.42566   11.18710  18.86769  1.000 8.65194   ?  76  GLY B C   1 
ATOM   2400 O  O   . GLY B 1 76  ? 10.30371  10.97619  19.71095  1.000 10.87808  ?  76  GLY B O   1 
ATOM   2401 N  N   . GLY B 1 77  ? 9.06666   12.41322  18.47126  1.000 9.48317   ?  77  GLY B N   1 
ATOM   2402 C  CA  . GLY B 1 77  ? 9.57075   13.61407  19.13200  1.000 10.61989  ?  77  GLY B CA  1 
ATOM   2403 C  C   . GLY B 1 77  ? 10.99332  14.02027  18.80667  1.000 15.08596  ?  77  GLY B C   1 
ATOM   2404 O  O   . GLY B 1 77  ? 11.54814  14.87701  19.50218  1.000 15.85352  ?  77  GLY B O   1 
ATOM   2405 N  N   . ILE B 1 78  ? 11.61084  13.43618  17.77890  1.000 11.49190  ?  78  ILE B N   1 
ATOM   2406 C  CA  . ILE B 1 78  ? 13.00488  13.70197  17.43447  1.000 8.37739   ?  78  ILE B CA  1 
ATOM   2407 C  C   . ILE B 1 78  ? 13.12284  13.87601  15.92453  1.000 11.21435  ?  78  ILE B C   1 
ATOM   2408 O  O   . ILE B 1 78  ? 12.34407  13.30518  15.15299  1.000 12.12692  ?  78  ILE B O   1 
ATOM   2409 C  CB  . ILE B 1 78  ? 13.94730  12.56463  17.90554  1.000 13.05766  ?  78  ILE B CB  1 
ATOM   2410 C  CG1 . ILE B 1 78  ? 13.55257  11.23035  17.26926  1.000 14.48345  ?  78  ILE B CG1 1 
ATOM   2411 C  CG2 . ILE B 1 78  ? 13.95806  12.44225  19.44066  1.000 10.68053  ?  78  ILE B CG2 1 
ATOM   2412 C  CD1 . ILE B 1 78  ? 14.65119  10.17677  17.39376  1.000 14.52576  ?  78  ILE B CD1 1 
ATOM   2413 N  N   . ARG B 1 79  ? 14.12116  14.64807  15.50349  1.000 13.15032  ?  79  ARG B N   1 
ATOM   2414 C  CA  . ARG B 1 79  ? 14.41640  14.78448  14.08187  1.000 10.28815  ?  79  ARG B CA  1 
ATOM   2415 C  C   . ARG B 1 79  ? 15.11697  13.52562  13.59618  1.000 15.58447  ?  79  ARG B C   1 
ATOM   2416 O  O   . ARG B 1 79  ? 16.14559  13.12129  14.15242  1.000 9.64286   ?  79  ARG B O   1 
ATOM   2417 C  CB  . ARG B 1 79  ? 15.27603  16.01629  13.81391  1.000 12.08105  ?  79  ARG B CB  1 
ATOM   2418 C  CG  . ARG B 1 79  ? 14.50537  17.29930  14.01384  1.000 16.74743  ?  79  ARG B CG  1 
ATOM   2419 C  CD  . ARG B 1 79  ? 15.29435  18.53545  13.58559  1.000 17.22842  ?  79  ARG B CD  1 
ATOM   2420 N  NE  . ARG B 1 79  ? 14.36429  19.59889  13.21998  1.000 23.72862  ?  79  ARG B NE  1 
ATOM   2421 C  CZ  . ARG B 1 79  ? 13.76790  19.67379  12.03662  1.000 29.58999  ?  79  ARG B CZ  1 
ATOM   2422 N  NH1 . ARG B 1 79  ? 14.05481  18.82197  11.06390  1.000 28.63812  ?  79  ARG B NH1 1 
ATOM   2423 N  NH2 . ARG B 1 79  ? 12.85852  20.62277  11.82397  1.000 41.72575  ?  79  ARG B NH2 1 
ATOM   2424 N  N   . ARG B 1 80  ? 14.55421  12.89764  12.57396  1.000 9.28760   ?  80  ARG B N   1 
ATOM   2425 C  CA  . ARG B 1 80  ? 15.08191  11.65436  12.03767  1.000 11.82603  ?  80  ARG B CA  1 
ATOM   2426 C  C   . ARG B 1 80  ? 15.59349  11.92592  10.62871  1.000 11.92731  ?  80  ARG B C   1 
ATOM   2427 O  O   . ARG B 1 80  ? 14.80650  12.11773  9.69490   1.000 14.27432  ?  80  ARG B O   1 
ATOM   2428 C  CB  . ARG B 1 80  ? 14.01442  10.56346  12.10314  1.000 9.88932   ?  80  ARG B CB  1 
ATOM   2429 C  CG  . ARG B 1 80  ? 13.78795  10.15490  13.56162  1.000 10.67935  ?  80  ARG B CG  1 
ATOM   2430 C  CD  . ARG B 1 80  ? 12.55346  9.28298   13.79368  1.000 8.29378   ?  80  ARG B CD  1 
ATOM   2431 N  NE  . ARG B 1 80  ? 12.54739  8.05559   13.00427  1.000 8.43684   ?  80  ARG B NE  1 
ATOM   2432 C  CZ  . ARG B 1 80  ? 11.50215  7.23974   12.92748  1.000 14.77465  ?  80  ARG B CZ  1 
ATOM   2433 N  NH1 . ARG B 1 80  ? 10.41888  7.43903   13.65579  1.000 11.32039  ?  80  ARG B NH1 1 
ATOM   2434 N  NH2 . ARG B 1 80  ? 11.54218  6.20704   12.09175  1.000 8.17468   ?  80  ARG B NH2 1 
ATOM   2435 N  N   . VAL B 1 81  ? 16.91489  11.97050  10.49866  1.000 10.11198  ?  81  VAL B N   1 
ATOM   2436 C  CA  . VAL B 1 81  ? 17.59362  12.38837  9.27583   1.000 16.75797  ?  81  VAL B CA  1 
ATOM   2437 C  C   . VAL B 1 81  ? 17.75439  11.15983  8.39248   1.000 13.40293  ?  81  VAL B C   1 
ATOM   2438 O  O   . VAL B 1 81  ? 18.52932  10.25289  8.70479   1.000 14.80976  ?  81  VAL B O   1 
ATOM   2439 C  CB  . VAL B 1 81  ? 18.95215  13.03059  9.59136   1.000 17.09897  ?  81  VAL B CB  1 
ATOM   2440 C  CG1 . VAL B 1 81  ? 19.59770  13.59102  8.32227   1.000 14.13653  ?  81  VAL B CG1 1 
ATOM   2441 C  CG2 . VAL B 1 81  ? 18.78524  14.11109  10.65714  1.000 10.76110  ?  81  VAL B CG2 1 
ATOM   2442 N  N   . TYR B 1 82  ? 16.99699  11.11196  7.30575   1.000 12.14463  ?  82  TYR B N   1 
ATOM   2443 C  CA  . TYR B 1 82  ? 17.00736  9.98852   6.38682   1.000 12.57554  ?  82  TYR B CA  1 
ATOM   2444 C  C   . TYR B 1 82  ? 17.41276  10.47660  5.00185   1.000 16.74485  ?  82  TYR B C   1 
ATOM   2445 O  O   . TYR B 1 82  ? 17.28486  11.66026  4.67269   1.000 14.41995  ?  82  TYR B O   1 
ATOM   2446 C  CB  . TYR B 1 82  ? 15.63081  9.30058   6.33991   1.000 8.80156   ?  82  TYR B CB  1 
ATOM   2447 C  CG  . TYR B 1 82  ? 15.29637  8.55765   7.61967   1.000 8.32454   ?  82  TYR B CG  1 
ATOM   2448 C  CD1 . TYR B 1 82  ? 16.17945  7.62710   8.15843   1.000 12.15209  ?  82  TYR B CD1 1 
ATOM   2449 C  CD2 . TYR B 1 82  ? 14.09927  8.79077   8.28816   1.000 11.97670  ?  82  TYR B CD2 1 
ATOM   2450 C  CE1 . TYR B 1 82  ? 15.87277  6.94255   9.32212   1.000 11.95119  ?  82  TYR B CE1 1 
ATOM   2451 C  CE2 . TYR B 1 82  ? 13.78380  8.10599   9.44923   1.000 10.29258  ?  82  TYR B CE2 1 
ATOM   2452 C  CZ  . TYR B 1 82  ? 14.67638  7.19813   9.96617   1.000 7.84056   ?  82  TYR B CZ  1 
ATOM   2453 O  OH  . TYR B 1 82  ? 14.36158  6.53530   11.12822  1.000 9.97178   ?  82  TYR B OH  1 
ATOM   2454 N  N   . GLU B 1 83  ? 17.93921  9.56273   4.21064   1.000 13.53273  ?  83  GLU B N   1 
ATOM   2455 C  CA  . GLU B 1 83  ? 18.21482  9.86350   2.81005   1.000 15.54295  ?  83  GLU B CA  1 
ATOM   2456 C  C   . GLU B 1 83  ? 16.93928  9.72187   1.97833   1.000 16.99850  ?  83  GLU B C   1 
ATOM   2457 O  O   . GLU B 1 83  ? 16.06587  8.90843   2.30223   1.000 11.40764  ?  83  GLU B O   1 
ATOM   2458 C  CB  . GLU B 1 83  ? 19.28261  8.92193   2.26086   1.000 17.73997  ?  83  GLU B CB  1 
ATOM   2459 C  CG  . GLU B 1 83  ? 20.66705  9.10818   2.85745   1.000 24.86191  ?  83  GLU B CG  1 
ATOM   2460 C  CD  . GLU B 1 83  ? 21.24797  10.47882  2.55899   1.000 28.21365  ?  83  GLU B CD  1 
ATOM   2461 O  OE1 . GLU B 1 83  ? 21.12082  10.94889  1.40676   1.000 25.63678  ?  83  GLU B OE1 1 
ATOM   2462 O  OE2 . GLU B 1 83  ? 21.81546  11.09064  3.48277   1.000 37.71081  -1 83  GLU B OE2 1 
ATOM   2463 N  N   . PRO B 1 84  ? 16.81323  10.48657  0.89340   1.000 12.83891  ?  84  PRO B N   1 
ATOM   2464 C  CA  . PRO B 1 84  ? 15.59993  10.39450  0.07326   1.000 12.47913  ?  84  PRO B CA  1 
ATOM   2465 C  C   . PRO B 1 84  ? 15.51278  9.06856   -0.66291  1.000 14.37978  ?  84  PRO B C   1 
ATOM   2466 O  O   . PRO B 1 84  ? 16.51782  8.40414   -0.92721  1.000 12.32072  ?  84  PRO B O   1 
ATOM   2467 C  CB  . PRO B 1 84  ? 15.73676  11.56905  -0.90454  1.000 16.10721  ?  84  PRO B CB  1 
ATOM   2468 C  CG  . PRO B 1 84  ? 17.19377  11.91077  -0.90002  1.000 20.02443  ?  84  PRO B CG  1 
ATOM   2469 C  CD  . PRO B 1 84  ? 17.70379  11.57929  0.45724   1.000 13.11995  ?  84  PRO B CD  1 
ATOM   2470 N  N   . ILE B 1 85  ? 14.27619  8.67877   -0.97316  1.000 11.00943  ?  85  ILE B N   1 
ATOM   2471 C  CA  . ILE B 1 85  ? 14.02597  7.49869   -1.79319  1.000 10.55827  ?  85  ILE B CA  1 
ATOM   2472 C  C   . ILE B 1 85  ? 14.52414  7.75807   -3.21003  1.000 16.63759  ?  85  ILE B C   1 
ATOM   2473 O  O   . ILE B 1 85  ? 14.27662  8.82323   -3.78966  1.000 16.78430  ?  85  ILE B O   1 
ATOM   2474 C  CB  . ILE B 1 85  ? 12.52699  7.15711   -1.77988  1.000 10.54866  ?  85  ILE B CB  1 
ATOM   2475 C  CG1 . ILE B 1 85  ? 12.12240  6.62204   -0.40641  1.000 11.93912  ?  85  ILE B CG1 1 
ATOM   2476 C  CG2 . ILE B 1 85  ? 12.16933  6.15166   -2.88608  1.000 13.47835  ?  85  ILE B CG2 1 
ATOM   2477 C  CD1 . ILE B 1 85  ? 10.64750  6.48042   -0.22205  1.000 10.74535  ?  85  ILE B CD1 1 
ATOM   2478 N  N   . GLU B 1 86  ? 15.23148  6.78541   -3.77173  1.000 18.86520  ?  86  GLU B N   1 
ATOM   2479 C  CA  . GLU B 1 86  ? 15.80246  6.93006   -5.10661  1.000 22.24786  ?  86  GLU B CA  1 
ATOM   2480 C  C   . GLU B 1 86  ? 14.80961  6.56856   -6.19947  1.000 19.93250  ?  86  GLU B C   1 
ATOM   2481 O  O   . GLU B 1 86  ? 14.77725  7.21434   -7.24820  1.000 18.36225  ?  86  GLU B O   1 
ATOM   2482 C  CB  . GLU B 1 86  ? 17.04301  6.04796   -5.25189  1.000 20.36747  ?  86  GLU B CB  1 
ATOM   2483 C  CG  . GLU B 1 86  ? 18.22073  6.49449   -4.41524  1.000 25.86275  ?  86  GLU B CG  1 
ATOM   2484 C  CD  . GLU B 1 86  ? 19.41316  5.56075   -4.53083  1.000 26.44534  ?  86  GLU B CD  1 
ATOM   2485 O  OE1 . GLU B 1 86  ? 19.23306  4.32334   -4.50613  1.000 29.17001  ?  86  GLU B OE1 1 
ATOM   2486 O  OE2 . GLU B 1 86  ? 20.54327  6.06764   -4.64768  1.000 36.02950  -1 86  GLU B OE2 1 
ATOM   2487 N  N   . VAL B 1 87  ? 14.00885  5.53529   -5.97965  1.000 14.61376  ?  87  VAL B N   1 
ATOM   2488 C  CA  . VAL B 1 87  ? 13.13490  5.01994   -7.02531  1.000 18.16918  ?  87  VAL B CA  1 
ATOM   2489 C  C   . VAL B 1 87  ? 11.79432  5.72995   -6.96801  1.000 20.31169  ?  87  VAL B C   1 
ATOM   2490 O  O   . VAL B 1 87  ? 11.58347  6.61053   -6.12804  1.000 15.74952  ?  87  VAL B O   1 
ATOM   2491 C  CB  . VAL B 1 87  ? 12.96633  3.50066   -6.88801  1.000 21.89397  ?  87  VAL B CB  1 
ATOM   2492 C  CG1 . VAL B 1 87  ? 14.31999  2.82356   -7.02460  1.000 18.29939  ?  87  VAL B CG1 1 
ATOM   2493 C  CG2 . VAL B 1 87  ? 12.33174  3.17697   -5.55242  1.000 14.72519  ?  87  VAL B CG2 1 
ATOM   2494 N  N   . ASP B 1 88  ? 10.87034  5.33893   -7.84775  1.000 18.12677  ?  88  ASP B N   1 
ATOM   2495 C  CA  . ASP B 1 88  ? 9.57647   6.00054   -7.97042  1.000 16.52131  ?  88  ASP B CA  1 
ATOM   2496 C  C   . ASP B 1 88  ? 8.47269   5.02269   -7.57897  1.000 18.77850  ?  88  ASP B C   1 
ATOM   2497 O  O   . ASP B 1 88  ? 8.10904   4.13641   -8.35489  1.000 17.03605  ?  88  ASP B O   1 
ATOM   2498 C  CB  . ASP B 1 88  ? 9.38575   6.52181   -9.39051  1.000 18.96394  ?  88  ASP B CB  1 
ATOM   2499 C  CG  . ASP B 1 88  ? 7.99329   7.05492   -9.63514  1.000 24.30139  ?  88  ASP B CG  1 
ATOM   2500 O  OD1 . ASP B 1 88  ? 7.27030   7.35975   -8.66581  1.000 22.47354  ?  88  ASP B OD1 1 
ATOM   2501 O  OD2 . ASP B 1 88  ? 7.61780   7.16963   -10.81522 1.000 21.73873  -1 88  ASP B OD2 1 
ATOM   2502 N  N   . PHE B 1 89  ? 7.92670   5.20227   -6.38193  1.000 17.85609  ?  89  PHE B N   1 
ATOM   2503 C  CA  . PHE B 1 89  ? 6.87824   4.32895   -5.87732  1.000 19.12858  ?  89  PHE B CA  1 
ATOM   2504 C  C   . PHE B 1 89  ? 5.48432   4.77032   -6.29209  1.000 13.15021  ?  89  PHE B C   1 
ATOM   2505 O  O   . PHE B 1 89  ? 4.50970   4.10015   -5.93150  1.000 16.02275  ?  89  PHE B O   1 
ATOM   2506 C  CB  . PHE B 1 89  ? 6.94244   4.24335   -4.33915  1.000 13.25564  ?  89  PHE B CB  1 
ATOM   2507 C  CG  . PHE B 1 89  ? 8.00963   3.31216   -3.82993  1.000 12.77281  ?  89  PHE B CG  1 
ATOM   2508 C  CD1 . PHE B 1 89  ? 7.86275   1.94157   -3.95438  1.000 15.45608  ?  89  PHE B CD1 1 
ATOM   2509 C  CD2 . PHE B 1 89  ? 9.15721   3.80577   -3.23213  1.000 15.53257  ?  89  PHE B CD2 1 
ATOM   2510 C  CE1 . PHE B 1 89  ? 8.84768   1.07280   -3.49308  1.000 11.64404  ?  89  PHE B CE1 1 
ATOM   2511 C  CE2 . PHE B 1 89  ? 10.13838  2.94886   -2.76383  1.000 14.66603  ?  89  PHE B CE2 1 
ATOM   2512 C  CZ  . PHE B 1 89  ? 9.98744   1.57971   -2.90631  1.000 14.60334  ?  89  PHE B CZ  1 
ATOM   2513 N  N   . THR B 1 90  ? 5.35577   5.87962   -7.02632  1.000 14.73156  ?  90  THR B N   1 
ATOM   2514 C  CA  . THR B 1 90  ? 4.02883   6.46131   -7.22059  1.000 13.73864  ?  90  THR B CA  1 
ATOM   2515 C  C   . THR B 1 90  ? 3.06817   5.55927   -8.00046  1.000 19.63440  ?  90  THR B C   1 
ATOM   2516 O  O   . THR B 1 90  ? 1.86002   5.60404   -7.72288  1.000 19.86022  ?  90  THR B O   1 
ATOM   2517 C  CB  . THR B 1 90  ? 4.13380   7.84592   -7.88486  1.000 19.43196  ?  90  THR B CB  1 
ATOM   2518 O  OG1 . THR B 1 90  ? 4.73513   7.73332   -9.17655  1.000 21.59154  ?  90  THR B OG1 1 
ATOM   2519 C  CG2 . THR B 1 90  ? 4.99166   8.75609   -7.03472  1.000 23.46488  ?  90  THR B CG2 1 
ATOM   2520 N  N   . PRO B 1 91  ? 3.51618   4.72911   -8.95959  1.000 22.19280  ?  91  PRO B N   1 
ATOM   2521 C  CA  . PRO B 1 91  ? 2.53995   3.82336   -9.59319  1.000 22.55201  ?  91  PRO B CA  1 
ATOM   2522 C  C   . PRO B 1 91  ? 1.93739   2.84373   -8.60575  1.000 20.44357  ?  91  PRO B C   1 
ATOM   2523 O  O   . PRO B 1 91  ? 0.73176   2.57939   -8.64403  1.000 21.41772  ?  91  PRO B O   1 
ATOM   2524 C  CB  . PRO B 1 91  ? 3.34948   3.12174   -10.69683 1.000 26.03641  ?  91  PRO B CB  1 
ATOM   2525 C  CG  . PRO B 1 91  ? 4.75624   3.40662   -10.42280 1.000 29.44678  ?  91  PRO B CG  1 
ATOM   2526 C  CD  . PRO B 1 91  ? 4.80511   4.70306   -9.67832  1.000 24.74065  ?  91  PRO B CD  1 
ATOM   2527 N  N   . LEU B 1 92  ? 2.74006   2.33328   -7.67917  1.000 20.77707  ?  92  LEU B N   1 
ATOM   2528 C  CA  . LEU B 1 92  ? 2.19691   1.46976   -6.64103  1.000 18.55892  ?  92  LEU B CA  1 
ATOM   2529 C  C   . LEU B 1 92  ? 1.25616   2.24046   -5.71209  1.000 12.04470  ?  92  LEU B C   1 
ATOM   2530 O  O   . LEU B 1 92  ? 0.17901   1.74432   -5.35520  1.000 19.59595  ?  92  LEU B O   1 
ATOM   2531 C  CB  . LEU B 1 92  ? 3.36973   0.84025   -5.88710  1.000 23.91787  ?  92  LEU B CB  1 
ATOM   2532 C  CG  . LEU B 1 92  ? 3.23156   -0.01862  -4.64686  1.000 24.80080  ?  92  LEU B CG  1 
ATOM   2533 C  CD1 . LEU B 1 92  ? 4.45276   -0.91433  -4.59955  1.000 23.08925  ?  92  LEU B CD1 1 
ATOM   2534 C  CD2 . LEU B 1 92  ? 3.16398   0.85395   -3.40036  1.000 29.26571  ?  92  LEU B CD2 1 
ATOM   2535 N  N   . ILE B 1 93  ? 1.63461   3.45977   -5.31902  1.000 16.20466  ?  93  ILE B N   1 
ATOM   2536 C  CA  . ILE B 1 93  ? 0.76719   4.26385   -4.46331  1.000 15.01583  ?  93  ILE B CA  1 
ATOM   2537 C  C   . ILE B 1 93  ? -0.56392  4.54395   -5.15321  1.000 20.92799  ?  93  ILE B C   1 
ATOM   2538 O  O   . ILE B 1 93  ? -1.62292  4.51926   -4.51554  1.000 16.32930  ?  93  ILE B O   1 
ATOM   2539 C  CB  . ILE B 1 93  ? 1.47694   5.56573   -4.04398  1.000 15.07889  ?  93  ILE B CB  1 
ATOM   2540 C  CG1 . ILE B 1 93  ? 2.74518   5.22766   -3.24367  1.000 20.45554  ?  93  ILE B CG1 1 
ATOM   2541 C  CG2 . ILE B 1 93  ? 0.53394   6.43915   -3.23300  1.000 15.75520  ?  93  ILE B CG2 1 
ATOM   2542 C  CD1 . ILE B 1 93  ? 3.76045   6.36497   -3.18631  1.000 16.81063  ?  93  ILE B CD1 1 
ATOM   2543 N  N   . SER B 1 94  ? -0.53693  4.80014   -6.46599  1.000 17.38678  ?  94  SER B N   1 
ATOM   2544 C  CA  . SER B 1 94  ? -1.77944  5.04290   -7.19775  1.000 23.64549  ?  94  SER B CA  1 
ATOM   2545 C  C   . SER B 1 94  ? -2.78505  3.91370   -6.99322  1.000 15.08558  ?  94  SER B C   1 
ATOM   2546 O  O   . SER B 1 94  ? -3.99340  4.15806   -6.88829  1.000 20.48014  ?  94  SER B O   1 
ATOM   2547 C  CB  . SER B 1 94  ? -1.49081  5.22719   -8.69168  1.000 23.05431  ?  94  SER B CB  1 
ATOM   2548 O  OG  . SER B 1 94  ? -0.85343  6.46865   -8.93280  1.000 27.65483  ?  94  SER B OG  1 
ATOM   2549 N  N   . GLU B 1 95  ? -2.30433  2.67088   -6.91787  1.000 19.07346  ?  95  GLU B N   1 
ATOM   2550 C  CA  . GLU B 1 95  ? -3.20434  1.55300   -6.65527  1.000 23.98119  ?  95  GLU B CA  1 
ATOM   2551 C  C   . GLU B 1 95  ? -3.92370  1.72476   -5.32774  1.000 23.69662  ?  95  GLU B C   1 
ATOM   2552 O  O   . GLU B 1 95  ? -5.13513  1.48949   -5.22991  1.000 19.72766  ?  95  GLU B O   1 
ATOM   2553 C  CB  . GLU B 1 95  ? -2.43305  0.23922   -6.65716  1.000 26.89820  ?  95  GLU B CB  1 
ATOM   2554 C  CG  . GLU B 1 95  ? -3.32296  -0.95227  -6.88699  1.000 36.96846  ?  95  GLU B CG  1 
ATOM   2555 C  CD  . GLU B 1 95  ? -3.66253  -1.12570  -8.35198  1.000 43.11436  ?  95  GLU B CD  1 
ATOM   2556 O  OE1 . GLU B 1 95  ? -2.83535  -0.72568  -9.20003  1.000 44.58822  ?  95  GLU B OE1 1 
ATOM   2557 O  OE2 . GLU B 1 95  ? -4.75904  -1.64895  -8.65294  1.000 54.17999  -1 95  GLU B OE2 1 
ATOM   2558 N  N   . GLY B 1 96  ? -3.18957  2.12841   -4.29040  1.000 26.72036  ?  96  GLY B N   1 
ATOM   2559 C  CA  . GLY B 1 96  ? -3.81752  2.37616   -3.00481  1.000 27.87518  ?  96  GLY B CA  1 
ATOM   2560 C  C   . GLY B 1 96  ? -4.78796  3.54111   -3.03942  1.000 18.34700  ?  96  GLY B C   1 
ATOM   2561 O  O   . GLY B 1 96  ? -5.85599  3.48309   -2.42546  1.000 19.69205  ?  96  GLY B O   1 
ATOM   2562 N  N   . ILE B 1 97  ? -4.42649  4.61830   -3.74283  1.000 18.08654  ?  97  ILE B N   1 
ATOM   2563 C  CA  . ILE B 1 97  ? -5.32837  5.76032   -3.86880  1.000 20.50353  ?  97  ILE B CA  1 
ATOM   2564 C  C   . ILE B 1 97  ? -6.64317  5.32967   -4.49949  1.000 21.16692  ?  97  ILE B C   1 
ATOM   2565 O  O   . ILE B 1 97  ? -7.72637  5.74747   -4.06847  1.000 20.80827  ?  97  ILE B O   1 
ATOM   2566 C  CB  . ILE B 1 97  ? -4.66655  6.88460   -4.68363  1.000 24.87891  ?  97  ILE B CB  1 
ATOM   2567 C  CG1 . ILE B 1 97  ? -3.43774  7.41356   -3.95546  1.000 21.49594  ?  97  ILE B CG1 1 
ATOM   2568 C  CG2 . ILE B 1 97  ? -5.67809  8.00304   -4.98102  1.000 20.06694  ?  97  ILE B CG2 1 
ATOM   2569 C  CD1 . ILE B 1 97  ? -2.68628  8.46126   -4.73911  1.000 24.29197  ?  97  ILE B CD1 1 
ATOM   2570 N  N   . ARG B 1 98  ? -6.56836  4.47865   -5.52133  1.000 17.55776  ?  98  ARG B N   1 
ATOM   2571 C  CA  . ARG B 1 98  ? -7.77396  4.04021   -6.21405  1.000 25.20119  ?  98  ARG B CA  1 
ATOM   2572 C  C   . ARG B 1 98  ? -8.64053  3.17609   -5.30908  1.000 22.74785  ?  98  ARG B C   1 
ATOM   2573 O  O   . ARG B 1 98  ? -9.86560  3.33296   -5.27411  1.000 19.53089  ?  98  ARG B O   1 
ATOM   2574 C  CB  . ARG B 1 98  ? -7.37643  3.28832   -7.48223  1.000 26.13934  ?  98  ARG B CB  1 
ATOM   2575 C  CG  . ARG B 1 98  ? -8.44887  2.38141   -8.07432  1.000 32.13500  ?  98  ARG B CG  1 
ATOM   2576 C  CD  . ARG B 1 98  ? -7.83386  1.26215   -8.95286  1.000 44.49891  ?  98  ARG B CD  1 
ATOM   2577 N  NE  . ARG B 1 98  ? -6.48245  1.54944   -9.43389  1.000 49.07571  ?  98  ARG B NE  1 
ATOM   2578 C  CZ  . ARG B 1 98  ? -6.18514  2.45408   -10.36010 1.000 48.64417  ?  98  ARG B CZ  1 
ATOM   2579 N  NH1 . ARG B 1 98  ? -7.11930  3.21057   -10.91062 1.000 60.16812  ?  98  ARG B NH1 1 
ATOM   2580 N  NH2 . ARG B 1 98  ? -4.91638  2.61824   -10.72745 1.000 40.68108  ?  98  ARG B NH2 1 
ATOM   2581 N  N   . GLU B 1 99  ? -8.01602  2.27776   -4.54697  1.000 24.77013  ?  99  GLU B N   1 
ATOM   2582 C  CA  . GLU B 1 99  ? -8.77154  1.41336   -3.65110  1.000 23.70391  ?  99  GLU B CA  1 
ATOM   2583 C  C   . GLU B 1 99  ? -9.38418  2.20261   -2.50362  1.000 27.09219  ?  99  GLU B C   1 
ATOM   2584 O  O   . GLU B 1 99  ? -10.50024 1.89779   -2.06453  1.000 19.99638  ?  99  GLU B O   1 
ATOM   2585 C  CB  . GLU B 1 99  ? -7.86724  0.30120   -3.12088  1.000 19.96889  ?  99  GLU B CB  1 
ATOM   2586 C  CG  . GLU B 1 99  ? -8.60681  -0.82534  -2.42986  1.000 22.92451  ?  99  GLU B CG  1 
ATOM   2587 C  CD  . GLU B 1 99  ? -9.61497  -1.52289  -3.32213  1.000 34.36708  ?  99  GLU B CD  1 
ATOM   2588 O  OE1 . GLU B 1 99  ? -9.40043  -1.56864  -4.55454  1.000 37.08253  ?  99  GLU B OE1 1 
ATOM   2589 O  OE2 . GLU B 1 99  ? -10.63368 -2.01973  -2.78764  1.000 31.62891  -1 99  GLU B OE2 1 
ATOM   2590 N  N   . LEU B 1 100 ? -8.66147  3.21107   -1.99555  1.000 17.23538  ?  100 LEU B N   1 
ATOM   2591 C  CA  . LEU B 1 100 ? -9.17628  4.05198   -0.92164  1.000 16.72766  ?  100 LEU B CA  1 
ATOM   2592 C  C   . LEU B 1 100 ? -10.32373 4.93851   -1.38168  1.000 23.15207  ?  100 LEU B C   1 
ATOM   2593 O  O   . LEU B 1 100 ? -11.18712 5.29685   -0.57083  1.000 20.26240  ?  100 LEU B O   1 
ATOM   2594 C  CB  . LEU B 1 100 ? -8.06348  4.93889   -0.36693  1.000 11.21858  ?  100 LEU B CB  1 
ATOM   2595 C  CG  . LEU B 1 100 ? -7.01381  4.27654   0.51313   1.000 17.49876  ?  100 LEU B CG  1 
ATOM   2596 C  CD1 . LEU B 1 100 ? -5.84567  5.24347   0.68609   1.000 14.97774  ?  100 LEU B CD1 1 
ATOM   2597 C  CD2 . LEU B 1 100 ? -7.62635  3.87539   1.85149   1.000 17.41673  ?  100 LEU B CD2 1 
ATOM   2598 N  N   . GLY B 1 101 ? -10.34095 5.31450   -2.66059  1.000 25.28894  ?  101 GLY B N   1 
ATOM   2599 C  CA  . GLY B 1 101 ? -11.25066 6.34289   -3.12687  1.000 20.96213  ?  101 GLY B CA  1 
ATOM   2600 C  C   . GLY B 1 101 ? -10.99760 7.64686   -2.40457  1.000 27.04631  ?  101 GLY B C   1 
ATOM   2601 O  O   . GLY B 1 101 ? -11.92917 8.24702   -1.85782  1.000 23.81085  ?  101 GLY B O   1 
ATOM   2602 N  N   . LEU B 1 102 ? -9.73019  8.07521   -2.38219  1.000 23.78855  ?  102 LEU B N   1 
ATOM   2603 C  CA  . LEU B 1 102 ? -9.33372  9.27481   -1.65098  1.000 25.05775  ?  102 LEU B CA  1 
ATOM   2604 C  C   . LEU B 1 102 ? -10.21211 10.46381  -2.01584  1.000 25.62891  ?  102 LEU B C   1 
ATOM   2605 O  O   . LEU B 1 102 ? -10.47573 10.72320  -3.19180  1.000 24.34635  ?  102 LEU B O   1 
ATOM   2606 C  CB  . LEU B 1 102 ? -7.87437  9.62258   -1.94912  1.000 29.85607  ?  102 LEU B CB  1 
ATOM   2607 C  CG  . LEU B 1 102 ? -6.75041  9.32259   -0.96011  1.000 24.75248  ?  102 LEU B CG  1 
ATOM   2608 C  CD1 . LEU B 1 102 ? -5.59335  10.26027  -1.24194  1.000 17.97494  ?  102 LEU B CD1 1 
ATOM   2609 C  CD2 . LEU B 1 102 ? -7.18997  9.42750   0.48202   1.000 14.51562  ?  102 LEU B CD2 1 
ATOM   2610 N  N   . ASP B 1 103 ? -10.64656 11.18958  -0.98697  1.000 23.73257  ?  103 ASP B N   1 
ATOM   2611 C  CA  . ASP B 1 103 ? -11.52839 12.34145  -1.15348  1.000 26.22209  ?  103 ASP B CA  1 
ATOM   2612 C  C   . ASP B 1 103 ? -10.88889 13.37513  -2.07553  1.000 26.36553  ?  103 ASP B C   1 
ATOM   2613 O  O   . ASP B 1 103 ? -9.81869  13.91599  -1.77642  1.000 22.86284  ?  103 ASP B O   1 
ATOM   2614 C  CB  . ASP B 1 103 ? -11.82904 12.94297  0.22170   1.000 22.25765  ?  103 ASP B CB  1 
ATOM   2615 C  CG  . ASP B 1 103 ? -12.75909 14.14373  0.16334   1.000 18.20254  ?  103 ASP B CG  1 
ATOM   2616 O  OD1 . ASP B 1 103 ? -13.23920 14.50524  -0.93204  1.000 22.56056  ?  103 ASP B OD1 1 
ATOM   2617 O  OD2 . ASP B 1 103 ? -13.00713 14.72413  1.24046   1.000 24.34804  -1 103 ASP B OD2 1 
ATOM   2618 N  N   . ARG B 1 104 ? -11.54971 13.65759  -3.19531  1.000 29.22473  ?  104 ARG B N   1 
ATOM   2619 C  CA  . ARG B 1 104 ? -11.00052 14.58786  -4.17480  1.000 25.72284  ?  104 ARG B CA  1 
ATOM   2620 C  C   . ARG B 1 104 ? -11.33606 16.04077  -3.87105  1.000 27.54751  ?  104 ARG B C   1 
ATOM   2621 O  O   . ARG B 1 104 ? -10.91667 16.92862  -4.62172  1.000 26.44170  ?  104 ARG B O   1 
ATOM   2622 C  CB  . ARG B 1 104 ? -11.49104 14.21364  -5.57361  1.000 28.26242  ?  104 ARG B CB  1 
ATOM   2623 C  CG  . ARG B 1 104 ? -10.89611 12.91617  -6.09520  1.000 34.83798  ?  104 ARG B CG  1 
ATOM   2624 C  CD  . ARG B 1 104 ? -11.43688 12.57524  -7.46810  1.000 39.16782  ?  104 ARG B CD  1 
ATOM   2625 N  NE  . ARG B 1 104 ? -11.34430 13.71954  -8.36294  1.000 39.17356  ?  104 ARG B NE  1 
ATOM   2626 C  CZ  . ARG B 1 104 ? -10.29865 13.98546  -9.13148  1.000 44.87098  ?  104 ARG B CZ  1 
ATOM   2627 N  NH1 . ARG B 1 104 ? -9.23819  13.19427  -9.14895  1.000 38.53852  ?  104 ARG B NH1 1 
ATOM   2628 N  NH2 . ARG B 1 104 ? -10.31979 15.07177  -9.90289  1.000 40.05915  ?  104 ARG B NH2 1 
ATOM   2629 N  N   . SER B 1 105 ? -12.04725 16.31617  -2.78191  1.000 22.61888  ?  105 SER B N   1 
ATOM   2630 C  CA  . SER B 1 105 ? -12.44193 17.68559  -2.50411  1.000 23.17417  ?  105 SER B CA  1 
ATOM   2631 C  C   . SER B 1 105 ? -11.31614 18.53356  -1.91532  1.000 28.17989  ?  105 SER B C   1 
ATOM   2632 O  O   . SER B 1 105 ? -11.50559 19.74539  -1.75784  1.000 22.87503  ?  105 SER B O   1 
ATOM   2633 C  CB  . SER B 1 105 ? -13.65028 17.71063  -1.56470  1.000 30.93007  ?  105 SER B CB  1 
ATOM   2634 O  OG  . SER B 1 105 ? -13.25468 17.60033  -0.20385  1.000 40.73367  ?  105 SER B OG  1 
ATOM   2635 N  N   . GLU B 1 106 ? -10.15767 17.95373  -1.60236  1.000 23.24828  ?  106 GLU B N   1 
ATOM   2636 C  CA  . GLU B 1 106 ? -9.02238  18.73785  -1.12890  1.000 14.51081  ?  106 GLU B CA  1 
ATOM   2637 C  C   . GLU B 1 106 ? -7.74387  17.94370  -1.38175  1.000 16.79536  ?  106 GLU B C   1 
ATOM   2638 O  O   . GLU B 1 106 ? -7.79323  16.72293  -1.56511  1.000 15.95831  ?  106 GLU B O   1 
ATOM   2639 C  CB  . GLU B 1 106 ? -9.17161  19.09827  0.35889   1.000 17.42749  ?  106 GLU B CB  1 
ATOM   2640 C  CG  . GLU B 1 106 ? -9.12516  17.92116  1.33025   1.000 17.23364  ?  106 GLU B CG  1 
ATOM   2641 C  CD  . GLU B 1 106 ? -9.43067  18.36440  2.73006   1.000 17.23539  ?  106 GLU B CD  1 
ATOM   2642 O  OE1 . GLU B 1 106 ? -8.61945  19.13200  3.29775   1.000 19.05876  ?  106 GLU B OE1 1 
ATOM   2643 O  OE2 . GLU B 1 106 ? -10.49789 17.97796  3.25594   1.000 23.63321  -1 106 GLU B OE2 1 
ATOM   2644 N  N   . PRO B 1 107 ? -6.59356  18.61144  -1.42905  1.000 18.82452  ?  107 PRO B N   1 
ATOM   2645 C  CA  . PRO B 1 107 ? -5.34096  17.90657  -1.71213  1.000 16.10608  ?  107 PRO B CA  1 
ATOM   2646 C  C   . PRO B 1 107 ? -4.82922  17.18638  -0.47310  1.000 13.24123  ?  107 PRO B C   1 
ATOM   2647 O  O   . PRO B 1 107 ? -5.25527  17.43426  0.65520   1.000 15.42061  ?  107 PRO B O   1 
ATOM   2648 C  CB  . PRO B 1 107 ? -4.38937  19.02911  -2.13899  1.000 20.95090  ?  107 PRO B CB  1 
ATOM   2649 C  CG  . PRO B 1 107 ? -4.87232  20.21542  -1.37385  1.000 15.78983  ?  107 PRO B CG  1 
ATOM   2650 C  CD  . PRO B 1 107 ? -6.38985  20.07038  -1.34866  1.000 16.35814  ?  107 PRO B CD  1 
ATOM   2651 N  N   . TRP B 1 108 ? -3.89715  16.26909  -0.71586  1.000 17.27734  ?  108 TRP B N   1 
ATOM   2652 C  CA  . TRP B 1 108 ? -3.38307  15.36871  0.30566   1.000 12.88910  ?  108 TRP B CA  1 
ATOM   2653 C  C   . TRP B 1 108 ? -1.86331  15.47861  0.35976   1.000 16.76928  ?  108 TRP B C   1 
ATOM   2654 O  O   . TRP B 1 108 ? -1.21701  16.01126  -0.55077  1.000 12.03281  ?  108 TRP B O   1 
ATOM   2655 C  CB  . TRP B 1 108 ? -3.82706  13.92182  0.01927   1.000 8.69279   ?  108 TRP B CB  1 
ATOM   2656 C  CG  . TRP B 1 108 ? -5.27809  13.70488  0.22922   1.000 18.58312  ?  108 TRP B CG  1 
ATOM   2657 C  CD1 . TRP B 1 108 ? -6.30477  14.14322  -0.57234  1.000 17.34249  ?  108 TRP B CD1 1 
ATOM   2658 C  CD2 . TRP B 1 108 ? -5.88798  13.00664  1.31645   1.000 14.16135  ?  108 TRP B CD2 1 
ATOM   2659 N  NE1 . TRP B 1 108 ? -7.52004  13.75428  -0.04241  1.000 16.33838  ?  108 TRP B NE1 1 
ATOM   2660 C  CE2 . TRP B 1 108 ? -7.28879  13.05346  1.11638   1.000 20.82931  ?  108 TRP B CE2 1 
ATOM   2661 C  CE3 . TRP B 1 108 ? -5.38739  12.33403  2.43927   1.000 14.15706  ?  108 TRP B CE3 1 
ATOM   2662 C  CZ2 . TRP B 1 108 ? -8.19450  12.45973  2.00622   1.000 15.03461  ?  108 TRP B CZ2 1 
ATOM   2663 C  CZ3 . TRP B 1 108 ? -6.29069  11.74159  3.32142   1.000 13.96094  ?  108 TRP B CZ3 1 
ATOM   2664 C  CH2 . TRP B 1 108 ? -7.67746  11.81628  3.10058   1.000 17.34526  ?  108 TRP B CH2 1 
ATOM   2665 N  N   . GLN B 1 109 ? -1.28933  14.97948  1.45284   1.000 12.47895  ?  109 GLN B N   1 
ATOM   2666 C  CA  . GLN B 1 109 ? 0.15514   14.89085  1.61446   1.000 9.93197   ?  109 GLN B CA  1 
ATOM   2667 C  C   . GLN B 1 109 ? 0.48224   13.48679  2.10384   1.000 8.81373   ?  109 GLN B C   1 
ATOM   2668 O  O   . GLN B 1 109 ? -0.25846  12.93844  2.92620   1.000 10.83921  ?  109 GLN B O   1 
ATOM   2669 C  CB  . GLN B 1 109 ? 0.65865   15.95443  2.61200   1.000 9.67646   ?  109 GLN B CB  1 
ATOM   2670 C  CG  . GLN B 1 109 ? 2.15407   15.95047  2.84583   1.000 11.10544  ?  109 GLN B CG  1 
ATOM   2671 C  CD  . GLN B 1 109 ? 2.54637   15.05369  4.00975   1.000 10.93941  ?  109 GLN B CD  1 
ATOM   2672 O  OE1 . GLN B 1 109 ? 1.83549   14.98040  5.01012   1.000 10.61998  ?  109 GLN B OE1 1 
ATOM   2673 N  NE2 . GLN B 1 109 ? 3.66502   14.35905  3.86868   1.000 9.50487   ?  109 GLN B NE2 1 
ATOM   2674 N  N   . ILE B 1 110 ? 1.56260   12.89052  1.58636   1.000 11.67648  ?  110 ILE B N   1 
ATOM   2675 C  CA  . ILE B 1 110 ? 1.93545   11.52859  1.97088   1.000 9.94809   ?  110 ILE B CA  1 
ATOM   2676 C  C   . ILE B 1 110 ? 3.37522   11.47284  2.45844   1.000 9.33600   ?  110 ILE B C   1 
ATOM   2677 O  O   . ILE B 1 110 ? 4.26678   12.14268  1.92117   1.000 10.03436  ?  110 ILE B O   1 
ATOM   2678 C  CB  . ILE B 1 110 ? 1.73047   10.50715  0.82828   1.000 10.37728  ?  110 ILE B CB  1 
ATOM   2679 C  CG1 . ILE B 1 110 ? 2.44976   10.92549  -0.45193  1.000 10.42546  ?  110 ILE B CG1 1 
ATOM   2680 C  CG2 . ILE B 1 110 ? 0.23753   10.26908  0.58159   1.000 14.96538  ?  110 ILE B CG2 1 
ATOM   2681 C  CD1 . ILE B 1 110 ? 2.49686   9.79974   -1.50528  1.000 8.88900   ?  110 ILE B CD1 1 
ATOM   2682 N  N   . ASN B 1 111 ? 3.59456   10.64214  3.47285   1.000 11.51364  ?  111 ASN B N   1 
ATOM   2683 C  CA  . ASN B 1 111 ? 4.91747   10.21254  3.89688   1.000 9.59898   ?  111 ASN B CA  1 
ATOM   2684 C  C   . ASN B 1 111 ? 5.16238   8.84254   3.28184   1.000 7.38069   ?  111 ASN B C   1 
ATOM   2685 O  O   . ASN B 1 111 ? 4.28338   7.98061   3.33646   1.000 8.81951   ?  111 ASN B O   1 
ATOM   2686 C  CB  . ASN B 1 111 ? 5.00794   10.11335  5.42696   1.000 8.25262   ?  111 ASN B CB  1 
ATOM   2687 C  CG  . ASN B 1 111 ? 5.05444   11.46623  6.10608   1.000 12.65584  ?  111 ASN B CG  1 
ATOM   2688 O  OD1 . ASN B 1 111 ? 5.21227   12.50114  5.45149   1.000 13.10261  ?  111 ASN B OD1 1 
ATOM   2689 N  ND2 . ASN B 1 111 ? 4.92461   11.46696  7.42055   1.000 12.88523  ?  111 ASN B ND2 1 
ATOM   2690 N  N   . VAL B 1 112 ? 6.33141   8.65223   2.68025   1.000 6.77583   ?  112 VAL B N   1 
ATOM   2691 C  CA  . VAL B 1 112 ? 6.68613   7.40176   2.01600   1.000 8.57775   ?  112 VAL B CA  1 
ATOM   2692 C  C   . VAL B 1 112 ? 7.94544   6.85742   2.67404   1.000 8.65006   ?  112 VAL B C   1 
ATOM   2693 O  O   . VAL B 1 112 ? 9.01103   7.48785   2.60353   1.000 7.10366   ?  112 VAL B O   1 
ATOM   2694 C  CB  . VAL B 1 112 ? 6.90227   7.59959   0.50555   1.000 10.94505  ?  112 VAL B CB  1 
ATOM   2695 C  CG1 . VAL B 1 112 ? 7.16964   6.24588   -0.18261  1.000 7.95253   ?  112 VAL B CG1 1 
ATOM   2696 C  CG2 . VAL B 1 112 ? 5.67666   8.27611   -0.11388  1.000 13.89584  ?  112 VAL B CG2 1 
ATOM   2697 N  N   . HIS B 1 113 ? 7.82500   5.68263   3.30107   1.000 10.21853  ?  113 HIS B N   1 
ATOM   2698 C  CA  . HIS B 1 113 ? 8.92379   5.02208   3.99349   1.000 10.02323  ?  113 HIS B CA  1 
ATOM   2699 C  C   . HIS B 1 113 ? 9.31463   3.77745   3.22436   1.000 10.24201  ?  113 HIS B C   1 
ATOM   2700 O  O   . HIS B 1 113 ? 8.49547   2.86606   3.06962   1.000 12.19439  ?  113 HIS B O   1 
ATOM   2701 C  CB  . HIS B 1 113 ? 8.53102   4.60745   5.41056   1.000 9.34507   ?  113 HIS B CB  1 
ATOM   2702 C  CG  . HIS B 1 113 ? 8.15890   5.75299   6.29023   1.000 11.43135  ?  113 HIS B CG  1 
ATOM   2703 N  ND1 . HIS B 1 113 ? 9.00639   6.24646   7.26042   1.000 10.46833  ?  113 HIS B ND1 1 
ATOM   2704 C  CD2 . HIS B 1 113 ? 7.03822   6.50835   6.34303   1.000 10.65988  ?  113 HIS B CD2 1 
ATOM   2705 C  CE1 . HIS B 1 113 ? 8.42022   7.25923   7.87199   1.000 13.90409  ?  113 HIS B CE1 1 
ATOM   2706 N  NE2 . HIS B 1 113 ? 7.22489   7.43914   7.33611   1.000 11.98490  ?  113 HIS B NE2 1 
ATOM   2707 N  N   . GLN B 1 114 ? 10.55850  3.72370   2.77552   1.000 7.56020   ?  114 GLN B N   1 
ATOM   2708 C  CA  . GLN B 1 114 ? 11.09216  2.52349   2.13926   1.000 8.47071   ?  114 GLN B CA  1 
ATOM   2709 C  C   . GLN B 1 114 ? 11.95120  1.79019   3.17062   1.000 12.83768  ?  114 GLN B C   1 
ATOM   2710 O  O   . GLN B 1 114 ? 13.03154  2.26747   3.53616   1.000 8.97862   ?  114 GLN B O   1 
ATOM   2711 C  CB  . GLN B 1 114 ? 11.89173  2.87823   0.88668   1.000 7.06328   ?  114 GLN B CB  1 
ATOM   2712 C  CG  . GLN B 1 114 ? 12.37586  1.66978   0.11671   1.000 8.31601   ?  114 GLN B CG  1 
ATOM   2713 C  CD  . GLN B 1 114 ? 13.27160  2.03945   -1.04579  1.000 9.14967   ?  114 GLN B CD  1 
ATOM   2714 O  OE1 . GLN B 1 114 ? 13.52894  3.21730   -1.29264  1.000 10.07921  ?  114 GLN B OE1 1 
ATOM   2715 N  NE2 . GLN B 1 114 ? 13.75294  1.03358   -1.76523  1.000 9.09682   ?  114 GLN B NE2 1 
ATOM   2716 N  N   . ASN B 1 115 ? 11.47490  0.62691   3.62925   1.000 13.83384  ?  115 ASN B N   1 
ATOM   2717 C  CA  . ASN B 1 115 ? 12.04369  -0.08561  4.77278   1.000 7.83869   ?  115 ASN B CA  1 
ATOM   2718 C  C   . ASN B 1 115 ? 12.49331  -1.47436  4.35828   1.000 9.38213   ?  115 ASN B C   1 
ATOM   2719 O  O   . ASN B 1 115 ? 11.71039  -2.22223  3.76405   1.000 8.73431   ?  115 ASN B O   1 
ATOM   2720 C  CB  . ASN B 1 115 ? 11.01263  -0.28394  5.90425   1.000 8.97192   ?  115 ASN B CB  1 
ATOM   2721 C  CG  . ASN B 1 115 ? 10.75004  0.95993   6.73157   1.000 13.24688  ?  115 ASN B CG  1 
ATOM   2722 O  OD1 . ASN B 1 115 ? 11.01843  2.08800   6.31584   1.000 14.37436  ?  115 ASN B OD1 1 
ATOM   2723 N  ND2 . ASN B 1 115 ? 10.17884  0.74766   7.91822   1.000 13.06338  ?  115 ASN B ND2 1 
ATOM   2724 N  N   . ARG B 1 116 ? 13.71388  -1.84672  4.73927   1.000 7.90048   ?  116 ARG B N   1 
ATOM   2725 C  CA  . ARG B 1 116 ? 14.13353  -3.24261  4.77311   1.000 9.64509   ?  116 ARG B CA  1 
ATOM   2726 C  C   . ARG B 1 116 ? 14.38670  -3.63156  6.21934   1.000 7.85619   ?  116 ARG B C   1 
ATOM   2727 O  O   . ARG B 1 116 ? 15.10844  -2.92407  6.93121   1.000 7.06966   ?  116 ARG B O   1 
ATOM   2728 C  CB  . ARG B 1 116 ? 15.40253  -3.47784  3.95045   1.000 9.18954   ?  116 ARG B CB  1 
ATOM   2729 C  CG  . ARG B 1 116 ? 16.10896  -4.78270  4.29927   1.000 12.66855  ?  116 ARG B CG  1 
ATOM   2730 C  CD  . ARG B 1 116 ? 17.23098  -5.05534  3.32337   1.000 19.33240  ?  116 ARG B CD  1 
ATOM   2731 N  NE  . ARG B 1 116 ? 16.71085  -5.45278  2.01691   1.000 15.63473  ?  116 ARG B NE  1 
ATOM   2732 C  CZ  . ARG B 1 116 ? 17.47529  -5.79433  0.99006   1.000 15.80259  ?  116 ARG B CZ  1 
ATOM   2733 N  NH1 . ARG B 1 116 ? 18.79615  -5.78550  1.08275   1.000 14.60289  ?  116 ARG B NH1 1 
ATOM   2734 N  NH2 . ARG B 1 116 ? 16.90059  -6.17348  -0.15041  1.000 13.66962  ?  116 ARG B NH2 1 
ATOM   2735 N  N   . THR B 1 117 ? 13.77814  -4.72447  6.66826   1.000 7.69198   ?  117 THR B N   1 
ATOM   2736 C  CA  . THR B 1 117 ? 14.10909  -5.28193  7.97449   1.000 9.05899   ?  117 THR B CA  1 
ATOM   2737 C  C   . THR B 1 117 ? 14.77454  -6.63432  7.78256   1.000 9.16867   ?  117 THR B C   1 
ATOM   2738 O  O   . THR B 1 117 ? 14.30306  -7.46838  6.99712   1.000 11.42885  ?  117 THR B O   1 
ATOM   2739 C  CB  . THR B 1 117 ? 12.87402  -5.37291  8.88603   1.000 5.75902   ?  117 THR B CB  1 
ATOM   2740 O  OG1 . THR B 1 117 ? 12.58706  -4.06850  9.40711   1.000 8.61036   ?  117 THR B OG1 1 
ATOM   2741 C  CG2 . THR B 1 117 ? 13.11514  -6.31630  10.07206  1.000 6.51275   ?  117 THR B CG2 1 
ATOM   2742 N  N   . ARG B 1 118 ? 15.89899  -6.82792  8.45761   1.000 8.14936   ?  118 ARG B N   1 
ATOM   2743 C  CA  . ARG B 1 118 ? 16.62951  -8.08010  8.38846   1.000 6.90398   ?  118 ARG B CA  1 
ATOM   2744 C  C   . ARG B 1 118 ? 16.37121  -8.94150  9.61322   1.000 13.10354  ?  118 ARG B C   1 
ATOM   2745 O  O   . ARG B 1 118 ? 16.20276  -8.44099  10.73049  1.000 9.95386   ?  118 ARG B O   1 
ATOM   2746 C  CB  . ARG B 1 118 ? 18.12403  -7.81698  8.26160   1.000 13.26319  ?  118 ARG B CB  1 
ATOM   2747 C  CG  . ARG B 1 118 ? 18.52010  -7.21413  6.94828   1.000 18.54261  ?  118 ARG B CG  1 
ATOM   2748 C  CD  . ARG B 1 118 ? 20.01352  -7.41663  6.72513   1.000 26.73308  ?  118 ARG B CD  1 
ATOM   2749 N  NE  . ARG B 1 118 ? 20.40022  -7.05230  5.36862   1.000 35.16120  ?  118 ARG B NE  1 
ATOM   2750 C  CZ  . ARG B 1 118 ? 20.28077  -7.84813  4.31495   1.000 24.57662  ?  118 ARG B CZ  1 
ATOM   2751 N  NH1 . ARG B 1 118 ? 19.76831  -9.06014  4.41951   1.000 27.53444  ?  118 ARG B NH1 1 
ATOM   2752 N  NH2 . ARG B 1 118 ? 20.69472  -7.41654  3.12804   1.000 41.96221  ?  118 ARG B NH2 1 
ATOM   2753 N  N   . ALA B 1 119 ? 16.36127  -10.25648 9.39673   1.000 13.99820  ?  119 ALA B N   1 
ATOM   2754 C  CA  . ALA B 1 119 ? 16.33649  -11.21540 10.48743  1.000 11.54018  ?  119 ALA B CA  1 
ATOM   2755 C  C   . ALA B 1 119 ? 17.50142  -12.17630 10.31783  1.000 16.61931  ?  119 ALA B C   1 
ATOM   2756 O  O   . ALA B 1 119 ? 18.02425  -12.34882 9.21885   1.000 14.95037  ?  119 ALA B O   1 
ATOM   2757 C  CB  . ALA B 1 119 ? 15.01969  -11.99130 10.54266  1.000 14.72745  ?  119 ALA B CB  1 
ATOM   2758 N  N   . ASP B 1 120 ? 17.91346  -12.79294 11.42355  1.000 13.47231  ?  120 ASP B N   1 
ATOM   2759 C  CA  . ASP B 1 120 ? 18.97202  -13.78974 11.38890  1.000 11.89959  ?  120 ASP B CA  1 
ATOM   2760 C  C   . ASP B 1 120 ? 18.68281  -14.77192 12.50527  1.000 12.96198  ?  120 ASP B C   1 
ATOM   2761 O  O   . ASP B 1 120 ? 17.81618  -14.53425 13.34991  1.000 17.18338  ?  120 ASP B O   1 
ATOM   2762 C  CB  . ASP B 1 120 ? 20.35765  -13.14702 11.53606  1.000 17.70893  ?  120 ASP B CB  1 
ATOM   2763 C  CG  . ASP B 1 120 ? 21.47496  -13.98701 10.90976  1.000 31.72304  ?  120 ASP B CG  1 
ATOM   2764 O  OD1 . ASP B 1 120 ? 21.28919  -15.20701 10.69223  1.000 21.66715  ?  120 ASP B OD1 1 
ATOM   2765 O  OD2 . ASP B 1 120 ? 22.54688  -13.41099 10.62928  1.000 29.25974  -1 120 ASP B OD2 1 
ATOM   2766 N  N   . GLY B 1 121 ? 19.39160  -15.89894 12.49499  1.000 15.97766  ?  121 GLY B N   1 
ATOM   2767 C  CA  . GLY B 1 121 ? 19.21642  -16.83872 13.58488  1.000 13.14238  ?  121 GLY B CA  1 
ATOM   2768 C  C   . GLY B 1 121 ? 19.45936  -16.16403 14.92024  1.000 14.67397  ?  121 GLY B C   1 
ATOM   2769 O  O   . GLY B 1 121 ? 20.45297  -15.45798 15.07919  1.000 13.61079  ?  121 GLY B O   1 
ATOM   2770 N  N   . GLY B 1 122 ? 18.54741  -16.33463 15.87204  1.000 17.20753  ?  122 GLY B N   1 
ATOM   2771 C  CA  . GLY B 1 122 ? 18.69096  -15.74401 17.18833  1.000 22.29102  ?  122 GLY B CA  1 
ATOM   2772 C  C   . GLY B 1 122 ? 18.41143  -14.25537 17.28087  1.000 17.22249  ?  122 GLY B C   1 
ATOM   2773 O  O   . GLY B 1 122 ? 18.37849  -13.71892 18.40047  1.000 17.71532  ?  122 GLY B O   1 
ATOM   2774 N  N   . ARG B 1 123 ? 18.21227  -13.56445 16.15792  1.000 11.01824  ?  123 ARG B N   1 
ATOM   2775 C  CA  . ARG B 1 123 ? 17.96877  -12.12371 16.16130  1.000 11.66722  ?  123 ARG B CA  1 
ATOM   2776 C  C   . ARG B 1 123 ? 16.79921  -11.78453 15.24347  1.000 8.51432   ?  123 ARG B C   1 
ATOM   2777 O  O   . ARG B 1 123 ? 16.98607  -11.52481 14.05126  1.000 8.36462   ?  123 ARG B O   1 
ATOM   2778 C  CB  . ARG B 1 123 ? 19.21537  -11.34736 15.74527  1.000 10.26127  ?  123 ARG B CB  1 
ATOM   2779 C  CG  . ARG B 1 123 ? 19.05480  -9.80828  15.92116  1.000 11.10003  ?  123 ARG B CG  1 
ATOM   2780 C  CD  . ARG B 1 123 ? 19.07722  -9.39333  17.41735  1.000 12.93378  ?  123 ARG B CD  1 
ATOM   2781 N  NE  . ARG B 1 123 ? 18.70656  -7.98963  17.61001  1.000 10.76633  ?  123 ARG B NE  1 
ATOM   2782 C  CZ  . ARG B 1 123 ? 19.50728  -6.96082  17.36627  1.000 14.44275  ?  123 ARG B CZ  1 
ATOM   2783 N  NH1 . ARG B 1 123 ? 20.77006  -7.13869  17.00743  1.000 13.93063  ?  123 ARG B NH1 1 
ATOM   2784 N  NH2 . ARG B 1 123 ? 19.02828  -5.71897  17.48007  1.000 9.90275   ?  123 ARG B NH2 1 
ATOM   2785 N  N   . PRO B 1 124 ? 15.58416  -11.75015 15.77439  1.000 11.05620  ?  124 PRO B N   1 
ATOM   2786 C  CA  . PRO B 1 124 ? 14.43474  -11.33979 14.95867  1.000 11.42616  ?  124 PRO B CA  1 
ATOM   2787 C  C   . PRO B 1 124 ? 14.55296  -9.88645  14.51716  1.000 14.57070  ?  124 PRO B C   1 
ATOM   2788 O  O   . PRO B 1 124 ? 15.30459  -9.08691  15.08380  1.000 10.09735  ?  124 PRO B O   1 
ATOM   2789 C  CB  . PRO B 1 124 ? 13.22953  -11.54125 15.88922  1.000 14.39678  ?  124 PRO B CB  1 
ATOM   2790 C  CG  . PRO B 1 124 ? 13.77864  -11.87109 17.25559  1.000 18.16606  ?  124 PRO B CG  1 
ATOM   2791 C  CD  . PRO B 1 124 ? 15.23270  -12.16002 17.14518  1.000 14.95550  ?  124 PRO B CD  1 
ATOM   2792 N  N   . GLY B 1 125 ? 13.78071  -9.53977  13.48950  1.000 7.84777   ?  125 GLY B N   1 
ATOM   2793 C  CA  . GLY B 1 125 ? 13.71618  -8.16450  13.04250  1.000 8.05973   ?  125 GLY B CA  1 
ATOM   2794 C  C   . GLY B 1 125 ? 12.41131  -7.50809  13.45880  1.000 10.21710  ?  125 GLY B C   1 
ATOM   2795 O  O   . GLY B 1 125 ? 11.33839  -7.85105  12.96138  1.000 9.79195   ?  125 GLY B O   1 
ATOM   2796 N  N   . PRO B 1 126 ? 12.47528  -6.55709  14.39184  1.000 11.78710  ?  126 PRO B N   1 
ATOM   2797 C  CA  . PRO B 1 126 ? 11.24076  -5.91857  14.87708  1.000 11.05458  ?  126 PRO B CA  1 
ATOM   2798 C  C   . PRO B 1 126 ? 10.62360  -5.04579  13.79654  1.000 6.95283   ?  126 PRO B C   1 
ATOM   2799 O  O   . PRO B 1 126 ? 11.30483  -4.23886  13.17069  1.000 11.14729  ?  126 PRO B O   1 
ATOM   2800 C  CB  . PRO B 1 126 ? 11.70679  -5.07500  16.07336  1.000 11.15395  ?  126 PRO B CB  1 
ATOM   2801 C  CG  . PRO B 1 126 ? 13.12355  -5.51285  16.36148  1.000 20.40984  ?  126 PRO B CG  1 
ATOM   2802 C  CD  . PRO B 1 126 ? 13.67551  -6.02854  15.05558  1.000 10.96744  ?  126 PRO B CD  1 
ATOM   2803 N  N   . LEU B 1 127 ? 9.31970   -5.20394  13.59648  1.000 9.70555   ?  127 LEU B N   1 
ATOM   2804 C  CA  . LEU B 1 127 ? 8.58693   -4.40979  12.62034  1.000 5.87186   ?  127 LEU B CA  1 
ATOM   2805 C  C   . LEU B 1 127 ? 7.80890   -3.27243  13.25550  1.000 8.07878   ?  127 LEU B C   1 
ATOM   2806 O  O   . LEU B 1 127 ? 7.76155   -2.17933  12.69576  1.000 10.79629  ?  127 LEU B O   1 
ATOM   2807 C  CB  . LEU B 1 127 ? 7.62685   -5.31241  11.82876  1.000 8.91294   ?  127 LEU B CB  1 
ATOM   2808 C  CG  . LEU B 1 127 ? 8.40014   -6.33892  10.98939  1.000 13.98668  ?  127 LEU B CG  1 
ATOM   2809 C  CD1 . LEU B 1 127 ? 7.44083   -7.31731  10.28970  1.000 12.50504  ?  127 LEU B CD1 1 
ATOM   2810 C  CD2 . LEU B 1 127 ? 9.33395   -5.64341  9.97361   1.000 7.41921   ?  127 LEU B CD2 1 
ATOM   2811 N  N   . THR B 1 128 ? 7.16862   -3.49924  14.39995  1.000 8.08545   ?  128 THR B N   1 
ATOM   2812 C  CA  . THR B 1 128 ? 6.43747   -2.44449  15.10497  1.000 6.53997   ?  128 THR B CA  1 
ATOM   2813 C  C   . THR B 1 128 ? 6.85899   -2.43968  16.56782  1.000 10.41402  ?  128 THR B C   1 
ATOM   2814 O  O   . THR B 1 128 ? 6.08717   -2.82088  17.45755  1.000 9.44610   ?  128 THR B O   1 
ATOM   2815 C  CB  . THR B 1 128 ? 4.92344   -2.61366  14.97029  1.000 9.15758   ?  128 THR B CB  1 
ATOM   2816 O  OG1 . THR B 1 128 ? 4.52554   -3.87887  15.51290  1.000 8.74472   ?  128 THR B OG1 1 
ATOM   2817 C  CG2 . THR B 1 128 ? 4.51430   -2.55730  13.50107  1.000 6.99743   ?  128 THR B CG2 1 
ATOM   2818 N  N   . PRO B 1 129 ? 8.07659   -1.97483  16.85715  1.000 9.41274   ?  129 PRO B N   1 
ATOM   2819 C  CA  . PRO B 1 129 ? 8.47121   -1.81328  18.26313  1.000 9.47895   ?  129 PRO B CA  1 
ATOM   2820 C  C   . PRO B 1 129 ? 7.61854   -0.80236  18.99493  1.000 13.43278  ?  129 PRO B C   1 
ATOM   2821 O  O   . PRO B 1 129 ? 7.67127   -0.74396  20.22987  1.000 13.91427  ?  129 PRO B O   1 
ATOM   2822 C  CB  . PRO B 1 129 ? 9.93659   -1.37222  18.17014  1.000 14.14641  ?  129 PRO B CB  1 
ATOM   2823 C  CG  . PRO B 1 129 ? 10.01615  -0.66778  16.85724  1.000 17.20827  ?  129 PRO B CG  1 
ATOM   2824 C  CD  . PRO B 1 129 ? 9.08661   -1.43596  15.93296  1.000 11.65135  ?  129 PRO B CD  1 
ATOM   2825 N  N   . GLU B 1 130 ? 6.82282   -0.01159  18.26836  1.000 13.07867  ?  130 GLU B N   1 
ATOM   2826 C  CA  . GLU B 1 130 ? 5.82264   0.84644   18.88803  1.000 14.55282  ?  130 GLU B CA  1 
ATOM   2827 C  C   . GLU B 1 130 ? 4.77143   0.05160   19.65108  1.000 14.07693  ?  130 GLU B C   1 
ATOM   2828 O  O   . GLU B 1 130 ? 4.03499   0.63460   20.45928  1.000 13.54055  ?  130 GLU B O   1 
ATOM   2829 C  CB  . GLU B 1 130 ? 5.11692   1.69437   17.82224  1.000 8.84186   ?  130 GLU B CB  1 
ATOM   2830 C  CG  . GLU B 1 130 ? 6.04004   2.52113   16.93468  1.000 12.69537  ?  130 GLU B CG  1 
ATOM   2831 C  CD  . GLU B 1 130 ? 6.60965   1.75966   15.75500  1.000 12.44965  ?  130 GLU B CD  1 
ATOM   2832 O  OE1 . GLU B 1 130 ? 6.58967   0.50419   15.74561  1.000 10.68899  ?  130 GLU B OE1 1 
ATOM   2833 O  OE2 . GLU B 1 130 ? 7.09463   2.42478   14.82416  1.000 18.97673  -1 130 GLU B OE2 1 
ATOM   2834 N  N   . GLY B 1 131 ? 4.67028   -1.25204  19.40542  1.000 14.17213  ?  131 GLY B N   1 
ATOM   2835 C  CA  . GLY B 1 131 ? 3.53877   -2.00963  19.89516  1.000 19.41389  ?  131 GLY B CA  1 
ATOM   2836 C  C   . GLY B 1 131 ? 2.30949   -1.73358  19.04388  1.000 10.73743  ?  131 GLY B C   1 
ATOM   2837 O  O   . GLY B 1 131 ? 2.39345   -1.21545  17.92574  1.000 12.42628  ?  131 GLY B O   1 
ATOM   2838 N  N   . VAL B 1 132 ? 1.14768   -2.08781  19.59265  1.000 9.60752   ?  132 VAL B N   1 
ATOM   2839 C  CA  . VAL B 1 132 ? -0.12229  -1.75843  18.95048  1.000 9.28009   ?  132 VAL B CA  1 
ATOM   2840 C  C   . VAL B 1 132 ? -0.25382  -0.24343  18.92219  1.000 12.16459  ?  132 VAL B C   1 
ATOM   2841 O  O   . VAL B 1 132 ? -0.14622  0.41016   19.96291  1.000 10.33751  ?  132 VAL B O   1 
ATOM   2842 C  CB  . VAL B 1 132 ? -1.29086  -2.40456  19.71149  1.000 11.72099  ?  132 VAL B CB  1 
ATOM   2843 C  CG1 . VAL B 1 132 ? -2.64776  -2.00851  19.08932  1.000 14.08533  ?  132 VAL B CG1 1 
ATOM   2844 C  CG2 . VAL B 1 132 ? -1.12268  -3.93030  19.78764  1.000 11.00684  ?  132 VAL B CG2 1 
ATOM   2845 N  N   . HIS B 1 133 ? -0.46627  0.33069   17.73968  1.000 5.28873   ?  133 HIS B N   1 
ATOM   2846 C  CA  . HIS B 1 133 ? -0.36241  1.78485   17.62534  1.000 10.02322  ?  133 HIS B CA  1 
ATOM   2847 C  C   . HIS B 1 133 ? -1.20785  2.29737   16.47222  1.000 13.25727  ?  133 HIS B C   1 
ATOM   2848 O  O   . HIS B 1 133 ? -1.62685  1.53879   15.59537  1.000 11.22393  ?  133 HIS B O   1 
ATOM   2849 C  CB  . HIS B 1 133 ? 1.09848   2.22381   17.40619  1.000 8.79524   ?  133 HIS B CB  1 
ATOM   2850 C  CG  . HIS B 1 133 ? 1.66399   1.76913   16.09176  1.000 8.31315   ?  133 HIS B CG  1 
ATOM   2851 N  ND1 . HIS B 1 133 ? 2.12214   0.48268   15.88046  1.000 6.69375   ?  133 HIS B ND1 1 
ATOM   2852 C  CD2 . HIS B 1 133 ? 1.79136   2.41555   14.90351  1.000 8.68310   ?  133 HIS B CD2 1 
ATOM   2853 C  CE1 . HIS B 1 133 ? 2.53506   0.36742   14.62607  1.000 8.49606   ?  133 HIS B CE1 1 
ATOM   2854 N  NE2 . HIS B 1 133 ? 2.33608   1.52477   14.01153  1.000 12.30605  ?  133 HIS B NE2 1 
ATOM   2855 N  N   . HIS B 1 134 ? -1.46491  3.60807   16.50185  1.000 8.55097   ?  134 HIS B N   1 
ATOM   2856 C  CA  . HIS B 1 134 ? -1.87264  4.36560   15.33098  1.000 13.97004  ?  134 HIS B CA  1 
ATOM   2857 C  C   . HIS B 1 134 ? -0.65975  5.11984   14.82466  1.000 13.25497  ?  134 HIS B C   1 
ATOM   2858 O  O   . HIS B 1 134 ? 0.19696   5.52557   15.61311  1.000 11.09752  ?  134 HIS B O   1 
ATOM   2859 C  CB  . HIS B 1 134 ? -2.97692  5.37247   15.64552  1.000 10.89635  ?  134 HIS B CB  1 
ATOM   2860 C  CG  . HIS B 1 134 ? -4.15287  4.77976   16.35319  1.000 17.18226  ?  134 HIS B CG  1 
ATOM   2861 N  ND1 . HIS B 1 134 ? -5.25865  4.29732   15.68826  1.000 10.19597  ?  134 HIS B ND1 1 
ATOM   2862 C  CD2 . HIS B 1 134 ? -4.39504  4.59494   17.67310  1.000 20.54414  ?  134 HIS B CD2 1 
ATOM   2863 C  CE1 . HIS B 1 134 ? -6.13433  3.84348   16.56803  1.000 12.38831  ?  134 HIS B CE1 1 
ATOM   2864 N  NE2 . HIS B 1 134 ? -5.63220  4.01054   17.78006  1.000 12.71342  ?  134 HIS B NE2 1 
ATOM   2865 N  N   . ASP B 1 135 ? -0.57604  5.29646   13.51147  1.000 9.48261   ?  135 ASP B N   1 
ATOM   2866 C  CA  . ASP B 1 135 ? 0.52050   6.09954   13.00342  1.000 11.21559  ?  135 ASP B CA  1 
ATOM   2867 C  C   . ASP B 1 135 ? 0.22601   7.58396   13.14361  1.000 14.80000  ?  135 ASP B C   1 
ATOM   2868 O  O   . ASP B 1 135 ? 1.15540   8.39637   13.15312  1.000 13.24562  ?  135 ASP B O   1 
ATOM   2869 C  CB  . ASP B 1 135 ? 0.82460   5.68289   11.56799  1.000 8.73354   ?  135 ASP B CB  1 
ATOM   2870 C  CG  . ASP B 1 135 ? 1.51549   4.30220   11.51612  1.000 11.79529  ?  135 ASP B CG  1 
ATOM   2871 O  OD1 . ASP B 1 135 ? 1.93436   3.81635   12.55704  1.000 21.53838  ?  135 ASP B OD1 1 
ATOM   2872 O  OD2 . ASP B 1 135 ? 1.65834   3.68933   10.46614  1.000 30.54398  -1 135 ASP B OD2 1 
ATOM   2873 N  N   . GLY B 1 136 ? -1.03575  7.93655   13.32523  1.000 12.96632  ?  136 GLY B N   1 
ATOM   2874 C  CA  . GLY B 1 136 ? -1.43199  9.29926   13.57094  1.000 12.98352  ?  136 GLY B CA  1 
ATOM   2875 C  C   . GLY B 1 136 ? -2.02552  9.98891   12.36521  1.000 15.30053  ?  136 GLY B C   1 
ATOM   2876 O  O   . GLY B 1 136 ? -2.40799  11.16921  12.46913  1.000 12.56929  ?  136 GLY B O   1 
ATOM   2877 N  N   . HIS B 1 137 ? -2.12424  9.28683   11.23788  1.000 8.65207   ?  137 HIS B N   1 
ATOM   2878 C  CA  . HIS B 1 137 ? -2.63138  9.82141   9.99005   1.000 11.39037  ?  137 HIS B CA  1 
ATOM   2879 C  C   . HIS B 1 137 ? -4.08701  9.40169   9.78946   1.000 15.40352  ?  137 HIS B C   1 
ATOM   2880 O  O   . HIS B 1 137 ? -4.73399  8.84382   10.68135  1.000 12.76976  ?  137 HIS B O   1 
ATOM   2881 C  CB  . HIS B 1 137 ? -1.73988  9.35884   8.83218   1.000 10.05168  ?  137 HIS B CB  1 
ATOM   2882 C  CG  . HIS B 1 137 ? -0.31865  9.80011   8.96176   1.000 11.42885  ?  137 HIS B CG  1 
ATOM   2883 N  ND1 . HIS B 1 137 ? 0.19882   10.86168  8.25339   1.000 10.56451  ?  137 HIS B ND1 1 
ATOM   2884 C  CD2 . HIS B 1 137 ? 0.69351   9.33102   9.72873   1.000 14.19781  ?  137 HIS B CD2 1 
ATOM   2885 C  CE1 . HIS B 1 137 ? 1.47242   11.01687  8.56239   1.000 12.30134  ?  137 HIS B CE1 1 
ATOM   2886 N  NE2 . HIS B 1 137 ? 1.79784   10.10022  9.45595   1.000 10.53018  ?  137 HIS B NE2 1 
ATOM   2887 N  N   . GLU B 1 138 ? -4.61275  9.66385   8.59305   1.000 9.36850   ?  138 GLU B N   1 
ATOM   2888 C  CA  . GLU B 1 138 ? -5.98811  9.28847   8.30945   1.000 10.01241  ?  138 GLU B CA  1 
ATOM   2889 C  C   . GLU B 1 138 ? -6.06822  7.92277   7.64253   1.000 8.80975   ?  138 GLU B C   1 
ATOM   2890 O  O   . GLU B 1 138 ? -6.91702  7.10731   8.01424   1.000 12.58235  ?  138 GLU B O   1 
ATOM   2891 C  CB  . GLU B 1 138 ? -6.66048  10.36770  7.44252   1.000 10.74199  ?  138 GLU B CB  1 
ATOM   2892 C  CG  . GLU B 1 138 ? -8.15387  10.15739  7.26109   1.000 12.41853  ?  138 GLU B CG  1 
ATOM   2893 C  CD  . GLU B 1 138 ? -8.88856  11.38394  6.68702   1.000 17.63129  ?  138 GLU B CD  1 
ATOM   2894 O  OE1 . GLU B 1 138 ? -8.30247  12.48326  6.58444   1.000 17.81132  ?  138 GLU B OE1 1 
ATOM   2895 O  OE2 . GLU B 1 138 ? -10.07152 11.23367  6.34837   1.000 18.88308  -1 138 GLU B OE2 1 
ATOM   2896 N  N   . PHE B 1 139 ? -5.18420  7.64123   6.68675   1.000 10.77586  ?  139 PHE B N   1 
ATOM   2897 C  CA  . PHE B 1 139 ? -5.10071  6.33141   6.05551   1.000 13.52259  ?  139 PHE B CA  1 
ATOM   2898 C  C   . PHE B 1 139 ? -3.64774  5.90603   5.97842   1.000 13.02801  ?  139 PHE B C   1 
ATOM   2899 O  O   . PHE B 1 139 ? -2.74766  6.74110   5.89010   1.000 11.52147  ?  139 PHE B O   1 
ATOM   2900 C  CB  . PHE B 1 139 ? -5.69765  6.32488   4.64286   1.000 9.35015   ?  139 PHE B CB  1 
ATOM   2901 C  CG  . PHE B 1 139 ? -7.13180  6.74315   4.60242   1.000 14.91501  ?  139 PHE B CG  1 
ATOM   2902 C  CD1 . PHE B 1 139 ? -8.11611  5.91723   5.13521   1.000 14.56106  ?  139 PHE B CD1 1 
ATOM   2903 C  CD2 . PHE B 1 139 ? -7.49720  7.97158   4.05263   1.000 13.54065  ?  139 PHE B CD2 1 
ATOM   2904 C  CE1 . PHE B 1 139 ? -9.46032  6.30408   5.11230   1.000 21.75771  ?  139 PHE B CE1 1 
ATOM   2905 C  CE2 . PHE B 1 139 ? -8.83258  8.35969   4.01782   1.000 16.34435  ?  139 PHE B CE2 1 
ATOM   2906 C  CZ  . PHE B 1 139 ? -9.81022  7.52705   4.54946   1.000 14.93041  ?  139 PHE B CZ  1 
ATOM   2907 N  N   . VAL B 1 140 ? -3.42505  4.59663   6.00390   1.000 11.73315  ?  140 VAL B N   1 
ATOM   2908 C  CA  . VAL B 1 140 ? -2.08162  4.04829   5.88080   1.000 7.96327   ?  140 VAL B CA  1 
ATOM   2909 C  C   . VAL B 1 140 ? -2.12292  2.90321   4.87352   1.000 10.95295  ?  140 VAL B C   1 
ATOM   2910 O  O   . VAL B 1 140 ? -3.06516  2.10744   4.86782   1.000 11.37074  ?  140 VAL B O   1 
ATOM   2911 C  CB  . VAL B 1 140 ? -1.53993  3.59584   7.25768   1.000 10.51153  ?  140 VAL B CB  1 
ATOM   2912 C  CG1 . VAL B 1 140 ? -0.29735  2.73336   7.10294   1.000 14.07433  ?  140 VAL B CG1 1 
ATOM   2913 C  CG2 . VAL B 1 140 ? -1.22080  4.82221   8.13620   1.000 8.71565   ?  140 VAL B CG2 1 
ATOM   2914 N  N   . MET B 1 141 ? -1.12023  2.85407   3.99665   1.000 8.95734   ?  141 MET B N   1 
ATOM   2915 C  CA  . MET B 1 141 ? -0.91496  1.77486   3.04619   1.000 10.30293  ?  141 MET B CA  1 
ATOM   2916 C  C   . MET B 1 141 ? 0.41464   1.12012   3.36719   1.000 10.35811  ?  141 MET B C   1 
ATOM   2917 O  O   . MET B 1 141 ? 1.42675   1.81291   3.47536   1.000 10.72732  ?  141 MET B O   1 
ATOM   2918 C  CB  . MET B 1 141 ? -0.89486  2.30622   1.60649   1.000 7.37737   ?  141 MET B CB  1 
ATOM   2919 C  CG  . MET B 1 141 ? -0.59636  1.22274   0.57258   1.000 15.98115  ?  141 MET B CG  1 
ATOM   2920 S  SD  . MET B 1 141 ? -0.64896  1.86372   -1.10958  1.000 11.45785  ?  141 MET B SD  1 
ATOM   2921 C  CE  . MET B 1 141 ? -0.35157  0.37130   -2.06791  1.000 19.51886  ?  141 MET B CE  1 
ATOM   2922 N  N   . ILE B 1 142 ? 0.42893   -0.20313  3.51797   1.000 10.66441  ?  142 ILE B N   1 
ATOM   2923 C  CA  . ILE B 1 142 ? 1.67794   -0.92452  3.75081   1.000 7.25268   ?  142 ILE B CA  1 
ATOM   2924 C  C   . ILE B 1 142 ? 1.80286   -1.97286  2.66400   1.000 9.02160   ?  142 ILE B C   1 
ATOM   2925 O  O   . ILE B 1 142 ? 0.95873   -2.86662  2.57275   1.000 9.42313   ?  142 ILE B O   1 
ATOM   2926 C  CB  . ILE B 1 142 ? 1.72559   -1.57137  5.13972   1.000 7.79845   ?  142 ILE B CB  1 
ATOM   2927 C  CG1 . ILE B 1 142 ? 1.66545   -0.47672  6.21312   1.000 8.73310   ?  142 ILE B CG1 1 
ATOM   2928 C  CG2 . ILE B 1 142 ? 2.96761   -2.45308  5.27344   1.000 6.49909   ?  142 ILE B CG2 1 
ATOM   2929 C  CD1 . ILE B 1 142 ? 0.86228   -0.88587  7.39336   1.000 13.45397  ?  142 ILE B CD1 1 
ATOM   2930 N  N   . ALA B 1 143 ? 2.84660   -1.86972  1.84603   1.000 10.22132  ?  143 ALA B N   1 
ATOM   2931 C  CA  . ALA B 1 143 ? 3.01551   -2.75855  0.70064   1.000 13.74162  ?  143 ALA B CA  1 
ATOM   2932 C  C   . ALA B 1 143 ? 4.25599   -3.61793  0.88761   1.000 9.37610   ?  143 ALA B C   1 
ATOM   2933 O  O   . ALA B 1 143 ? 5.32181   -3.09759  1.22980   1.000 9.16347   ?  143 ALA B O   1 
ATOM   2934 C  CB  . ALA B 1 143 ? 3.11695   -1.95525  -0.60091  1.000 9.42662   ?  143 ALA B CB  1 
ATOM   2935 N  N   . ILE B 1 144 ? 4.12036   -4.92664  0.65564   1.000 10.62599  ?  144 ILE B N   1 
ATOM   2936 C  CA  . ILE B 1 144 ? 5.22850   -5.87363  0.75363   1.000 10.01787  ?  144 ILE B CA  1 
ATOM   2937 C  C   . ILE B 1 144 ? 5.83438   -6.03551  -0.63193  1.000 10.30521  ?  144 ILE B C   1 
ATOM   2938 O  O   . ILE B 1 144 ? 5.16982   -6.53031  -1.55158  1.000 13.39952  ?  144 ILE B O   1 
ATOM   2939 C  CB  . ILE B 1 144 ? 4.77378   -7.24542  1.28849   1.000 13.34328  ?  144 ILE B CB  1 
ATOM   2940 C  CG1 . ILE B 1 144 ? 3.87225   -7.12515  2.50692   1.000 8.38368   ?  144 ILE B CG1 1 
ATOM   2941 C  CG2 . ILE B 1 144 ? 5.97647   -8.15307  1.56828   1.000 8.43513   ?  144 ILE B CG2 1 
ATOM   2942 C  CD1 . ILE B 1 144 ? 4.35814   -6.19661  3.59434   1.000 9.56008   ?  144 ILE B CD1 1 
ATOM   2943 N  N   . LEU B 1 145 ? 7.09794   -5.66672  -0.78893  1.000 9.40410   ?  145 LEU B N   1 
ATOM   2944 C  CA  . LEU B 1 145 ? 7.72973   -5.75388  -2.10204  1.000 12.99482  ?  145 LEU B CA  1 
ATOM   2945 C  C   . LEU B 1 145 ? 8.53201   -7.02937  -2.29044  1.000 16.84580  ?  145 LEU B C   1 
ATOM   2946 O  O   . LEU B 1 145 ? 8.62011   -7.53429  -3.41670  1.000 11.14055  ?  145 LEU B O   1 
ATOM   2947 C  CB  . LEU B 1 145 ? 8.65124   -4.54978  -2.34663  1.000 11.62771  ?  145 LEU B CB  1 
ATOM   2948 C  CG  . LEU B 1 145 ? 8.02236   -3.23286  -2.82689  1.000 17.25680  ?  145 LEU B CG  1 
ATOM   2949 C  CD1 . LEU B 1 145 ? 7.55498   -3.37294  -4.27294  1.000 21.80008  ?  145 LEU B CD1 1 
ATOM   2950 C  CD2 . LEU B 1 145 ? 6.88180   -2.80064  -1.94101  1.000 13.82384  ?  145 LEU B CD2 1 
ATOM   2951 N  N   . ASN B 1 146 ? 9.10169   -7.57294  -1.21537  1.000 13.34260  ?  146 ASN B N   1 
ATOM   2952 C  CA  . ASN B 1 146 ? 9.97867   -8.72897  -1.32450  1.000 10.18602  ?  146 ASN B CA  1 
ATOM   2953 C  C   . ASN B 1 146 ? 10.16987  -9.33121  0.05717   1.000 10.89591  ?  146 ASN B C   1 
ATOM   2954 O  O   . ASN B 1 146 ? 10.34773  -8.59429  1.03402   1.000 11.71458  ?  146 ASN B O   1 
ATOM   2955 C  CB  . ASN B 1 146 ? 11.33094  -8.32377  -1.92472  1.000 12.26074  ?  146 ASN B CB  1 
ATOM   2956 C  CG  . ASN B 1 146 ? 12.20373  -9.51707  -2.29343  1.000 19.85313  ?  146 ASN B CG  1 
ATOM   2957 O  OD1 . ASN B 1 146 ? 13.42590  -9.45145  -2.18995  1.000 40.11518  ?  146 ASN B OD1 1 
ATOM   2958 N  ND2 . ASN B 1 146 ? 11.58346  -10.60145 -2.71873  1.000 18.28171  ?  146 ASN B ND2 1 
ATOM   2959 N  N   . LYS B 1 147 ? 10.13261  -10.66438 0.13449   1.000 9.59233   ?  147 LYS B N   1 
ATOM   2960 C  CA  . LYS B 1 147 ? 10.48537  -11.37740 1.36464   1.000 10.49561  ?  147 LYS B CA  1 
ATOM   2961 C  C   . LYS B 1 147 ? 11.39912  -12.53249 0.99784   1.000 17.08782  ?  147 LYS B C   1 
ATOM   2962 O  O   . LYS B 1 147 ? 11.12031  -13.25788 0.03656   1.000 10.04003  ?  147 LYS B O   1 
ATOM   2963 C  CB  . LYS B 1 147 ? 9.24406   -11.90129 2.11308   1.000 10.36069  ?  147 LYS B CB  1 
ATOM   2964 C  CG  . LYS B 1 147 ? 8.37165   -10.80401 2.72515   1.000 9.18236   ?  147 LYS B CG  1 
ATOM   2965 C  CD  . LYS B 1 147 ? 7.00573   -11.32182 3.19168   1.000 9.27350   ?  147 LYS B CD  1 
ATOM   2966 C  CE  . LYS B 1 147 ? 7.13932   -12.47453 4.19315   1.000 12.59665  ?  147 LYS B CE  1 
ATOM   2967 N  NZ  . LYS B 1 147 ? 5.82780   -12.83594 4.83083   1.000 12.40624  ?  147 LYS B NZ  1 
ATOM   2968 N  N   . VAL B 1 148 ? 12.48880  -12.69606 1.75249   1.000 13.35691  ?  148 VAL B N   1 
ATOM   2969 C  CA  . VAL B 1 148 ? 13.45275  -13.76668 1.51105   1.000 15.53153  ?  148 VAL B CA  1 
ATOM   2970 C  C   . VAL B 1 148 ? 13.75400  -14.43746 2.83826   1.000 14.49042  ?  148 VAL B C   1 
ATOM   2971 O  O   . VAL B 1 148 ? 14.25417  -13.78335 3.75896   1.000 10.94750  ?  148 VAL B O   1 
ATOM   2972 C  CB  . VAL B 1 148 ? 14.76427  -13.25677 0.88546   1.000 12.24025  ?  148 VAL B CB  1 
ATOM   2973 C  CG1 . VAL B 1 148 ? 15.75445  -14.42052 0.73941   1.000 20.80513  ?  148 VAL B CG1 1 
ATOM   2974 C  CG2 . VAL B 1 148 ? 14.50399  -12.58557 -0.45168  1.000 19.28837  ?  148 VAL B CG2 1 
ATOM   2975 N  N   . ASN B 1 149 ? 13.42109  -15.72732 2.94818   1.000 14.24332  ?  149 ASN B N   1 
ATOM   2976 C  CA  . ASN B 1 149 ? 13.86212  -16.57203 4.05723   1.000 15.01237  ?  149 ASN B CA  1 
ATOM   2977 C  C   . ASN B 1 149 ? 13.39604  -16.05653 5.41832   1.000 19.78860  ?  149 ASN B C   1 
ATOM   2978 O  O   . ASN B 1 149 ? 14.14498  -16.07767 6.40218   1.000 17.43766  ?  149 ASN B O   1 
ATOM   2979 C  CB  . ASN B 1 149 ? 15.38164  -16.73263 4.05675   1.000 12.74352  ?  149 ASN B CB  1 
ATOM   2980 C  CG  . ASN B 1 149 ? 15.82198  -17.91210 4.88461   1.000 19.05777  ?  149 ASN B CG  1 
ATOM   2981 O  OD1 . ASN B 1 149 ? 15.13865  -18.93779 4.91762   1.000 17.74969  ?  149 ASN B OD1 1 
ATOM   2982 N  ND2 . ASN B 1 149 ? 16.93651  -17.76342 5.60127   1.000 19.51025  ?  149 ASN B ND2 1 
ATOM   2983 N  N   . VAL B 1 150 ? 12.14598  -15.62359 5.50303   1.000 15.56157  ?  150 VAL B N   1 
ATOM   2984 C  CA  . VAL B 1 150 ? 11.62994  -15.12656 6.76533   1.000 12.26488  ?  150 VAL B CA  1 
ATOM   2985 C  C   . VAL B 1 150 ? 10.31600  -15.80710 7.10750   1.000 16.48662  ?  150 VAL B C   1 
ATOM   2986 O  O   . VAL B 1 150 ? 9.55353   -16.22335 6.22835   1.000 16.99021  ?  150 VAL B O   1 
ATOM   2987 C  CB  . VAL B 1 150 ? 11.47431  -13.59008 6.73073   1.000 15.86933  ?  150 VAL B CB  1 
ATOM   2988 C  CG1 . VAL B 1 150 ? 12.85278  -12.94154 6.69379   1.000 11.10207  ?  150 VAL B CG1 1 
ATOM   2989 C  CG2 . VAL B 1 150 ? 10.64832  -13.16275 5.52896   1.000 13.87623  ?  150 VAL B CG2 1 
ATOM   2990 N  N   . ALA B 1 151 ? 10.07326  -15.94069 8.40381   1.000 10.61893  ?  151 ALA B N   1 
ATOM   2991 C  CA  . ALA B 1 151 ? 8.77855   -16.30278 8.95635   1.000 14.18009  ?  151 ALA B CA  1 
ATOM   2992 C  C   . ALA B 1 151 ? 8.29057   -15.14392 9.82334   1.000 13.67484  ?  151 ALA B C   1 
ATOM   2993 O  O   . ALA B 1 151 ? 8.90145   -14.07330 9.85885   1.000 14.62226  ?  151 ALA B O   1 
ATOM   2994 C  CB  . ALA B 1 151 ? 8.86891   -17.61205 9.74638   1.000 17.47507  ?  151 ALA B CB  1 
ATOM   2995 N  N   . GLY B 1 152 ? 7.18144   -15.36682 10.52565  1.000 20.04700  ?  152 GLY B N   1 
ATOM   2996 C  CA  . GLY B 1 152 ? 6.59348   -14.28560 11.30198  1.000 15.40117  ?  152 GLY B CA  1 
ATOM   2997 C  C   . GLY B 1 152 ? 6.15637   -13.15165 10.39566  1.000 14.60970  ?  152 GLY B C   1 
ATOM   2998 O  O   . GLY B 1 152 ? 5.72888   -13.35200 9.25482   1.000 13.08876  ?  152 GLY B O   1 
ATOM   2999 N  N   . GLY B 1 153 ? 6.28774   -11.92960 10.90169  1.000 13.53726  ?  153 GLY B N   1 
ATOM   3000 C  CA  . GLY B 1 153 ? 5.85535   -10.78497 10.11148  1.000 11.31348  ?  153 GLY B CA  1 
ATOM   3001 C  C   . GLY B 1 153 ? 4.36144   -10.76483 9.86618   1.000 13.93997  ?  153 GLY B C   1 
ATOM   3002 O  O   . GLY B 1 153 ? 3.91695   -10.42240 8.76242   1.000 11.51868  ?  153 GLY B O   1 
ATOM   3003 N  N   . THR B 1 154 ? 3.57076   -11.11764 10.87213  1.000 8.60353   ?  154 THR B N   1 
ATOM   3004 C  CA  . THR B 1 154 ? 2.12249   -11.19913 10.72343  1.000 10.91571  ?  154 THR B CA  1 
ATOM   3005 C  C   . THR B 1 154 ? 1.48432   -9.88809  11.15199  1.000 11.63137  ?  154 THR B C   1 
ATOM   3006 O  O   . THR B 1 154 ? 1.70738   -9.42249  12.27602  1.000 8.84767   ?  154 THR B O   1 
ATOM   3007 C  CB  . THR B 1 154 ? 1.56899   -12.36296 11.53567  1.000 11.59294  ?  154 THR B CB  1 
ATOM   3008 O  OG1 . THR B 1 154 ? 2.19204   -13.56603 11.07105  1.000 15.15214  ?  154 THR B OG1 1 
ATOM   3009 C  CG2 . THR B 1 154 ? 0.05569   -12.46854 11.37337  1.000 12.02951  ?  154 THR B CG2 1 
ATOM   3010 N  N   . THR B 1 155 ? 0.71685   -9.29017  10.24467  1.000 7.89843   ?  155 THR B N   1 
ATOM   3011 C  CA  . THR B 1 155 ? -0.00987  -8.06490  10.52951  1.000 8.28126   ?  155 THR B CA  1 
ATOM   3012 C  C   . THR B 1 155 ? -1.24691  -8.37080  11.35790  1.000 11.60228  ?  155 THR B C   1 
ATOM   3013 O  O   . THR B 1 155 ? -1.98395  -9.31184  11.06698  1.000 7.95474   ?  155 THR B O   1 
ATOM   3014 C  CB  . THR B 1 155 ? -0.43218  -7.39224  9.22632   1.000 5.76951   ?  155 THR B CB  1 
ATOM   3015 O  OG1 . THR B 1 155 ? 0.73520   -7.05433  8.46923   1.000 10.92386  ?  155 THR B OG1 1 
ATOM   3016 C  CG2 . THR B 1 155 ? -1.24197  -6.12179  9.51930   1.000 8.37045   ?  155 THR B CG2 1 
ATOM   3017 N  N   . ARG B 1 156 ? -1.48602  -7.56503  12.38893  1.000 11.73970  ?  156 ARG B N   1 
ATOM   3018 C  CA  . ARG B 1 156 ? -2.64969  -7.77034  13.23949  1.000 7.69949   ?  156 ARG B CA  1 
ATOM   3019 C  C   . ARG B 1 156 ? -3.37839  -6.45048  13.39606  1.000 9.95764   ?  156 ARG B C   1 
ATOM   3020 O  O   . ARG B 1 156 ? -2.75539  -5.43167  13.70320  1.000 9.01703   ?  156 ARG B O   1 
ATOM   3021 C  CB  . ARG B 1 156 ? -2.22876  -8.33791  14.59128  1.000 11.82633  ?  156 ARG B CB  1 
ATOM   3022 C  CG  . ARG B 1 156 ? -1.37045  -9.58568  14.40968  1.000 14.10693  ?  156 ARG B CG  1 
ATOM   3023 C  CD  . ARG B 1 156 ? -1.03235  -10.23442 15.69290  1.000 21.35956  ?  156 ARG B CD  1 
ATOM   3024 N  NE  . ARG B 1 156 ? -0.28506  -9.36469  16.58840  1.000 12.89874  ?  156 ARG B NE  1 
ATOM   3025 C  CZ  . ARG B 1 156 ? 0.30282   -9.81233  17.68628  1.000 16.44085  ?  156 ARG B CZ  1 
ATOM   3026 N  NH1 . ARG B 1 156 ? 0.26679   -11.08691 18.00672  1.000 19.11077  ?  156 ARG B NH1 1 
ATOM   3027 N  NH2 . ARG B 1 156 ? 0.92841   -8.95924  18.48396  1.000 16.92559  ?  156 ARG B NH2 1 
ATOM   3028 N  N   . LEU B 1 157 ? -4.68391  -6.46550  13.17395  1.000 7.28769   ?  157 LEU B N   1 
ATOM   3029 C  CA  . LEU B 1 157 ? -5.49177  -5.25853  13.23407  1.000 9.05786   ?  157 LEU B CA  1 
ATOM   3030 C  C   . LEU B 1 157 ? -6.32485  -5.27377  14.50825  1.000 13.98630  ?  157 LEU B C   1 
ATOM   3031 O  O   . LEU B 1 157 ? -6.85862  -6.31615  14.89479  1.000 12.09968  ?  157 LEU B O   1 
ATOM   3032 C  CB  . LEU B 1 157 ? -6.38015  -5.14236  11.99341  1.000 11.14387  ?  157 LEU B CB  1 
ATOM   3033 C  CG  . LEU B 1 157 ? -5.56126  -5.09989  10.69905  1.000 11.96555  ?  157 LEU B CG  1 
ATOM   3034 C  CD1 . LEU B 1 157 ? -6.48914  -5.02029  9.44989   1.000 12.56047  ?  157 LEU B CD1 1 
ATOM   3035 C  CD2 . LEU B 1 157 ? -4.59013  -3.91712  10.73338  1.000 12.87154  ?  157 LEU B CD2 1 
ATOM   3036 N  N   . TRP B 1 158 ? -6.41609  -4.12502  15.17544  1.000 12.56191  ?  158 TRP B N   1 
ATOM   3037 C  CA  . TRP B 1 158 ? -6.99535  -4.07541  16.50996  1.000 13.21418  ?  158 TRP B CA  1 
ATOM   3038 C  C   . TRP B 1 158 ? -8.02779  -2.97099  16.61419  1.000 11.27597  ?  158 TRP B C   1 
ATOM   3039 O  O   . TRP B 1 158 ? -7.81920  -1.86357  16.11156  1.000 12.75356  ?  158 TRP B O   1 
ATOM   3040 C  CB  . TRP B 1 158 ? -5.94318  -3.80557  17.58209  1.000 11.43306  ?  158 TRP B CB  1 
ATOM   3041 C  CG  . TRP B 1 158 ? -4.77577  -4.73405  17.64273  1.000 11.15826  ?  158 TRP B CG  1 
ATOM   3042 C  CD1 . TRP B 1 158 ? -3.77045  -4.86359  16.72522  1.000 9.78407   ?  158 TRP B CD1 1 
ATOM   3043 C  CD2 . TRP B 1 158 ? -4.44198  -5.59847  18.73188  1.000 10.57000  ?  158 TRP B CD2 1 
ATOM   3044 N  NE1 . TRP B 1 158 ? -2.83777  -5.77942  17.17346  1.000 10.25323  ?  158 TRP B NE1 1 
ATOM   3045 C  CE2 . TRP B 1 158 ? -3.23000  -6.24418  18.40064  1.000 9.31282   ?  158 TRP B CE2 1 
ATOM   3046 C  CE3 . TRP B 1 158 ? -5.04888  -5.88613  19.95737  1.000 12.52710  ?  158 TRP B CE3 1 
ATOM   3047 C  CZ2 . TRP B 1 158 ? -2.60901  -7.15459  19.25701  1.000 10.94500  ?  158 TRP B CZ2 1 
ATOM   3048 C  CZ3 . TRP B 1 158 ? -4.43282  -6.79593  20.80690  1.000 15.52283  ?  158 TRP B CZ3 1 
ATOM   3049 C  CH2 . TRP B 1 158 ? -3.22991  -7.42535  20.44650  1.000 13.06825  ?  158 TRP B CH2 1 
ATOM   3050 N  N   . LYS B 1 159 ? -9.11114  -3.25625  17.29280  1.000 11.49073  ?  159 LYS B N   1 
ATOM   3051 C  CA  . LYS B 1 159 ? -9.96601  -2.13396  17.61802  1.000 15.80512  ?  159 LYS B CA  1 
ATOM   3052 C  C   . LYS B 1 159 ? -9.47883  -1.49930  18.91758  1.000 11.11680  ?  159 LYS B C   1 
ATOM   3053 O  O   . LYS B 1 159 ? -8.92857  -2.18643  19.77846  1.000 13.38810  ?  159 LYS B O   1 
ATOM   3054 C  CB  . LYS B 1 159 ? -11.41890 -2.58035  17.75367  1.000 18.32974  ?  159 LYS B CB  1 
ATOM   3055 C  CG  . LYS B 1 159 ? -12.03950 -3.06391  16.43625  1.000 20.04754  ?  159 LYS B CG  1 
ATOM   3056 C  CD  . LYS B 1 159 ? -13.55207 -3.13303  16.56794  1.000 40.68637  ?  159 LYS B CD  1 
ATOM   3057 C  CE  . LYS B 1 159 ? -14.26829 -2.40345  15.43651  1.000 52.65343  ?  159 LYS B CE  1 
ATOM   3058 N  NZ  . LYS B 1 159 ? -15.65820 -1.99388  15.83215  1.000 40.86787  ?  159 LYS B NZ  1 
ATOM   3059 N  N   . PRO B 1 160 ? -9.65328  -0.19133  19.07329  1.000 16.11056  ?  160 PRO B N   1 
ATOM   3060 C  CA  . PRO B 1 160 ? -9.14387  0.48400   20.27644  1.000 18.92015  ?  160 PRO B CA  1 
ATOM   3061 C  C   . PRO B 1 160 ? -9.68506  -0.15318  21.54830  1.000 19.79568  ?  160 PRO B C   1 
ATOM   3062 O  O   . PRO B 1 160 ? -10.87735 -0.44384  21.65968  1.000 18.06456  ?  160 PRO B O   1 
ATOM   3063 C  CB  . PRO B 1 160 ? -9.64297  1.92202   20.11304  1.000 20.06343  ?  160 PRO B CB  1 
ATOM   3064 C  CG  . PRO B 1 160 ? -9.80991  2.09432   18.63648  1.000 24.27539  ?  160 PRO B CG  1 
ATOM   3065 C  CD  . PRO B 1 160 ? -10.24961 0.75010   18.10917  1.000 21.76198  ?  160 PRO B CD  1 
ATOM   3066 N  N   . GLY B 1 161 ? -8.78461  -0.39156  22.50430  1.000 20.15192  ?  161 GLY B N   1 
ATOM   3067 C  CA  . GLY B 1 161 ? -9.13528  -0.98222  23.77570  1.000 14.99097  ?  161 GLY B CA  1 
ATOM   3068 C  C   . GLY B 1 161 ? -9.17005  -2.49282  23.79958  1.000 23.23496  ?  161 GLY B C   1 
ATOM   3069 O  O   . GLY B 1 161 ? -9.19705  -3.07554  24.89366  1.000 21.81278  ?  161 GLY B O   1 
ATOM   3070 N  N   . ALA B 1 162 ? -9.15188  -3.15033  22.64126  1.000 14.30374  ?  162 ALA B N   1 
ATOM   3071 C  CA  . ALA B 1 162 ? -9.36847  -4.58933  22.61059  1.000 16.47574  ?  162 ALA B CA  1 
ATOM   3072 C  C   . ALA B 1 162 ? -8.14058  -5.33556  23.10906  1.000 17.55442  ?  162 ALA B C   1 
ATOM   3073 O  O   . ALA B 1 162 ? -6.99572  -4.92785  22.87929  1.000 15.38626  ?  162 ALA B O   1 
ATOM   3074 C  CB  . ALA B 1 162 ? -9.73443  -5.06090  21.19508  1.000 16.06073  ?  162 ALA B CB  1 
ATOM   3075 N  N   . ASP B 1 163 ? -8.39959  -6.44800  23.80885  1.000 19.91959  ?  163 ASP B N   1 
ATOM   3076 C  CA  . ASP B 1 163 ? -7.34818  -7.32892  24.30659  1.000 19.12819  ?  163 ASP B CA  1 
ATOM   3077 C  C   . ASP B 1 163 ? -6.70211  -8.16216  23.21627  1.000 21.53544  ?  163 ASP B C   1 
ATOM   3078 O  O   . ASP B 1 163 ? -5.61140  -8.70108  23.43414  1.000 15.83814  ?  163 ASP B O   1 
ATOM   3079 C  CB  . ASP B 1 163 ? -7.90135  -8.29372  25.35585  1.000 15.19771  ?  163 ASP B CB  1 
ATOM   3080 C  CG  . ASP B 1 163 ? -8.33084  -7.59102  26.61936  1.000 22.06336  ?  163 ASP B CG  1 
ATOM   3081 O  OD1 . ASP B 1 163 ? -7.89917  -6.44492  26.83004  1.000 16.95808  ?  163 ASP B OD1 1 
ATOM   3082 O  OD2 . ASP B 1 163 ? -9.10582  -8.18616  27.39291  1.000 20.81928  -1 163 ASP B OD2 1 
ATOM   3083 N  N   . ALA B 1 164 ? -7.36019  -8.31908  22.07115  1.000 17.44272  ?  164 ALA B N   1 
ATOM   3084 C  CA  . ALA B 1 164 ? -6.85120  -9.19939  21.02977  1.000 13.22285  ?  164 ALA B CA  1 
ATOM   3085 C  C   . ALA B 1 164 ? -7.18312  -8.58469  19.68405  1.000 12.23893  ?  164 ALA B C   1 
ATOM   3086 O  O   . ALA B 1 164 ? -8.15474  -7.83228  19.57876  1.000 14.10827  ?  164 ALA B O   1 
ATOM   3087 C  CB  . ALA B 1 164 ? -7.45821  -10.60675 21.13675  1.000 18.95868  ?  164 ALA B CB  1 
ATOM   3088 N  N   . PRO B 1 165 ? -6.41176  -8.88555  18.64184  1.000 13.76698  ?  165 PRO B N   1 
ATOM   3089 C  CA  . PRO B 1 165 ? -6.74962  -8.37668  17.30758  1.000 12.37513  ?  165 PRO B CA  1 
ATOM   3090 C  C   . PRO B 1 165 ? -7.98584  -9.06748  16.75663  1.000 14.40625  ?  165 PRO B C   1 
ATOM   3091 O  O   . PRO B 1 165 ? -8.27620  -10.22398 17.07925  1.000 14.98284  ?  165 PRO B O   1 
ATOM   3092 C  CB  . PRO B 1 165 ? -5.51001  -8.71449  16.46994  1.000 11.79069  ?  165 PRO B CB  1 
ATOM   3093 C  CG  . PRO B 1 165 ? -4.87394  -9.87323  17.17907  1.000 17.16521  ?  165 PRO B CG  1 
ATOM   3094 C  CD  . PRO B 1 165 ? -5.16944  -9.67793  18.64772  1.000 15.10914  ?  165 PRO B CD  1 
ATOM   3095 N  N   . PHE B 1 166 ? -8.72320  -8.34453  15.91510  1.000 14.11121  ?  166 PHE B N   1 
ATOM   3096 C  CA  . PHE B 1 166 ? -9.88571  -8.94480  15.26908  1.000 15.71853  ?  166 PHE B CA  1 
ATOM   3097 C  C   . PHE B 1 166 ? -9.55956  -9.53312  13.91203  1.000 19.24927  ?  166 PHE B C   1 
ATOM   3098 O  O   . PHE B 1 166 ? -10.38227 -10.26724 13.35863  1.000 15.06543  ?  166 PHE B O   1 
ATOM   3099 C  CB  . PHE B 1 166 ? -11.02531 -7.92354  15.11013  1.000 15.61093  ?  166 PHE B CB  1 
ATOM   3100 C  CG  . PHE B 1 166 ? -10.75251 -6.84748  14.09254  1.000 11.94377  ?  166 PHE B CG  1 
ATOM   3101 C  CD1 . PHE B 1 166 ? -10.06435 -5.70177  14.44678  1.000 13.58721  ?  166 PHE B CD1 1 
ATOM   3102 C  CD2 . PHE B 1 166 ? -11.20518 -6.97582  12.78097  1.000 11.21538  ?  166 PHE B CD2 1 
ATOM   3103 C  CE1 . PHE B 1 166 ? -9.81605  -4.70741  13.50485  1.000 15.39662  ?  166 PHE B CE1 1 
ATOM   3104 C  CE2 . PHE B 1 166 ? -10.96093 -6.00454  11.84288  1.000 18.69801  ?  166 PHE B CE2 1 
ATOM   3105 C  CZ  . PHE B 1 166 ? -10.26787 -4.86214  12.19801  1.000 15.94186  ?  166 PHE B CZ  1 
ATOM   3106 N  N   . TRP B 1 167 ? -8.39651  -9.21303  13.35540  1.000 14.87775  ?  167 TRP B N   1 
ATOM   3107 C  CA  . TRP B 1 167 ? -7.99056  -9.75882  12.07236  1.000 16.00166  ?  167 TRP B CA  1 
ATOM   3108 C  C   . TRP B 1 167 ? -6.48650  -9.91676  12.10078  1.000 13.60349  ?  167 TRP B C   1 
ATOM   3109 O  O   . TRP B 1 167 ? -5.77793  -9.05710  12.63528  1.000 11.06677  ?  167 TRP B O   1 
ATOM   3110 C  CB  . TRP B 1 167 ? -8.39821  -8.85237  10.90049  1.000 17.34852  ?  167 TRP B CB  1 
ATOM   3111 C  CG  . TRP B 1 167 ? -7.99749  -9.38444  9.55099   1.000 18.73109  ?  167 TRP B CG  1 
ATOM   3112 C  CD1 . TRP B 1 167 ? -8.75956  -10.14876 8.71717   1.000 19.17310  ?  167 TRP B CD1 1 
ATOM   3113 C  CD2 . TRP B 1 167 ? -6.73966  -9.18952  8.87966   1.000 13.51154  ?  167 TRP B CD2 1 
ATOM   3114 N  NE1 . TRP B 1 167 ? -8.05810  -10.44391 7.57513   1.000 15.90819  ?  167 TRP B NE1 1 
ATOM   3115 C  CE2 . TRP B 1 167 ? -6.81694  -9.86960  7.64931   1.000 13.60043  ?  167 TRP B CE2 1 
ATOM   3116 C  CE3 . TRP B 1 167 ? -5.56250  -8.50755  9.20212   1.000 14.16239  ?  167 TRP B CE3 1 
ATOM   3117 C  CZ2 . TRP B 1 167 ? -5.76402  -9.88982  6.74156   1.000 17.03867  ?  167 TRP B CZ2 1 
ATOM   3118 C  CZ3 . TRP B 1 167 ? -4.51305  -8.53313  8.30644   1.000 14.98874  ?  167 TRP B CZ3 1 
ATOM   3119 C  CH2 . TRP B 1 167 ? -4.62149  -9.21897  7.08342   1.000 20.04794  ?  167 TRP B CH2 1 
ATOM   3120 N  N   . SER B 1 168 ? -5.99481  -11.00303 11.51576  1.000 12.41555  ?  168 SER B N   1 
ATOM   3121 C  CA  . SER B 1 168 ? -4.55546  -11.15400 11.40022  1.000 12.27334  ?  168 SER B CA  1 
ATOM   3122 C  C   . SER B 1 168 ? -4.23253  -11.81894 10.07601  1.000 22.14052  ?  168 SER B C   1 
ATOM   3123 O  O   . SER B 1 168 ? -5.02548  -12.60495 9.54767   1.000 16.44665  ?  168 SER B O   1 
ATOM   3124 C  CB  . SER B 1 168 ? -3.97204  -11.97086 12.57203  1.000 15.23192  ?  168 SER B CB  1 
ATOM   3125 O  OG  . SER B 1 168 ? -4.11765  -13.35585 12.33340  1.000 27.77581  ?  168 SER B OG  1 
ATOM   3126 N  N   . GLY B 1 169 ? -3.07061  -11.47463 9.53219   1.000 14.94493  ?  169 GLY B N   1 
ATOM   3127 C  CA  . GLY B 1 169 ? -2.62810  -12.10266 8.30803   1.000 18.12254  ?  169 GLY B CA  1 
ATOM   3128 C  C   . GLY B 1 169 ? -1.19246  -11.75759 7.98804   1.000 13.38392  ?  169 GLY B C   1 
ATOM   3129 O  O   . GLY B 1 169 ? -0.74968  -10.62798 8.21465   1.000 11.18718  ?  169 GLY B O   1 
ATOM   3130 N  N   . THR B 1 170 ? -0.45219  -12.72213 7.45882   1.000 10.73437  ?  170 THR B N   1 
ATOM   3131 C  CA  . THR B 1 170 ? 0.91692   -12.48644 7.01592   1.000 13.40617  ?  170 THR B CA  1 
ATOM   3132 C  C   . THR B 1 170 ? 0.88030   -11.99802 5.57609   1.000 14.14594  ?  170 THR B C   1 
ATOM   3133 O  O   . THR B 1 170 ? 0.59435   -12.77766 4.65854   1.000 11.33441  ?  170 THR B O   1 
ATOM   3134 C  CB  . THR B 1 170 ? 1.74470   -13.75995 7.14155   1.000 13.56300  ?  170 THR B CB  1 
ATOM   3135 O  OG1 . THR B 1 170 ? 1.67923   -14.21585 8.49287   1.000 14.03286  ?  170 THR B OG1 1 
ATOM   3136 C  CG2 . THR B 1 170 ? 3.18176   -13.49021 6.77794   1.000 11.62819  ?  170 THR B CG2 1 
ATOM   3137 N  N   . LEU B 1 171 ? 1.14819   -10.70708 5.38270   1.000 8.80313   ?  171 LEU B N   1 
ATOM   3138 C  CA  . LEU B 1 171 ? 1.15819   -10.12311 4.04870   1.000 13.71116  ?  171 LEU B CA  1 
ATOM   3139 C  C   . LEU B 1 171 ? 2.37862   -10.61616 3.28408   1.000 13.93489  ?  171 LEU B C   1 
ATOM   3140 O  O   . LEU B 1 171 ? 3.49169   -10.63493 3.82577   1.000 9.26504   ?  171 LEU B O   1 
ATOM   3141 C  CB  . LEU B 1 171 ? 1.17247   -8.59304  4.14993   1.000 7.20399   ?  171 LEU B CB  1 
ATOM   3142 C  CG  . LEU B 1 171 ? -0.06284  -8.00536  4.82886   1.000 11.49845  ?  171 LEU B CG  1 
ATOM   3143 C  CD1 . LEU B 1 171 ? 0.07988   -6.51441  5.02740   1.000 11.54877  ?  171 LEU B CD1 1 
ATOM   3144 C  CD2 . LEU B 1 171 ? -1.27591  -8.31630  3.95331   1.000 16.30131  ?  171 LEU B CD2 1 
ATOM   3145 N  N   . GLU B 1 172 ? 2.17780   -11.02040 2.03038   1.000 11.11679  ?  172 GLU B N   1 
ATOM   3146 C  CA  . GLU B 1 172 ? 3.26168   -11.57586 1.22952   1.000 11.06125  ?  172 GLU B CA  1 
ATOM   3147 C  C   . GLU B 1 172 ? 3.67757   -10.59997 0.13835   1.000 10.79930  ?  172 GLU B C   1 
ATOM   3148 O  O   . GLU B 1 172 ? 2.99921   -9.60805  -0.13775  1.000 12.39904  ?  172 GLU B O   1 
ATOM   3149 C  CB  . GLU B 1 172 ? 2.86904   -12.92881 0.60940   1.000 12.32734  ?  172 GLU B CB  1 
ATOM   3150 C  CG  . GLU B 1 172 ? 2.36113   -13.97548 1.60198   1.000 9.57883   ?  172 GLU B CG  1 
ATOM   3151 C  CD  . GLU B 1 172 ? 3.34443   -14.31316 2.71396   1.000 14.57626  ?  172 GLU B CD  1 
ATOM   3152 O  OE1 . GLU B 1 172 ? 4.54370   -13.97480 2.60687   1.000 12.59471  ?  172 GLU B OE1 1 
ATOM   3153 O  OE2 . GLU B 1 172 ? 2.90356   -14.94837 3.70199   1.000 14.41414  -1 172 GLU B OE2 1 
ATOM   3154 N  N   . ALA B 1 173 ? 4.84045   -10.87505 -0.45283  1.000 9.03730   ?  173 ALA B N   1 
ATOM   3155 C  CA  . ALA B 1 173 ? 5.33391   -10.05282 -1.55165  1.000 10.91403  ?  173 ALA B CA  1 
ATOM   3156 C  C   . ALA B 1 173 ? 4.24870   -9.90484  -2.60822  1.000 14.30318  ?  173 ALA B C   1 
ATOM   3157 O  O   . ALA B 1 173 ? 3.62809   -10.88561 -3.00976  1.000 12.16395  ?  173 ALA B O   1 
ATOM   3158 C  CB  . ALA B 1 173 ? 6.58826   -10.68356 -2.15519  1.000 13.42267  ?  173 ALA B CB  1 
ATOM   3159 N  N   . GLY B 1 174 ? 3.97146   -8.66808  -3.00328  1.000 12.36115  ?  174 GLY B N   1 
ATOM   3160 C  CA  . GLY B 1 174 ? 2.88368   -8.41187  -3.92337  1.000 13.92973  ?  174 GLY B CA  1 
ATOM   3161 C  C   . GLY B 1 174 ? 1.55009   -8.09516  -3.27993  1.000 17.01055  ?  174 GLY B C   1 
ATOM   3162 O  O   . GLY B 1 174 ? 0.56809   -7.88857  -4.00022  1.000 15.21873  ?  174 GLY B O   1 
ATOM   3163 N  N   . GLN B 1 175 ? 1.46808   -8.05352  -1.95324  1.000 9.74009   ?  175 GLN B N   1 
ATOM   3164 C  CA  . GLN B 1 175 ? 0.24736   -7.63664  -1.27987  1.000 9.08798   ?  175 GLN B CA  1 
ATOM   3165 C  C   . GLN B 1 175 ? 0.46345   -6.31385  -0.56762  1.000 11.90169  ?  175 GLN B C   1 
ATOM   3166 O  O   . GLN B 1 175 ? 1.58300   -5.96012  -0.20369  1.000 12.34340  ?  175 GLN B O   1 
ATOM   3167 C  CB  . GLN B 1 175 ? -0.21860  -8.68403  -0.26385  1.000 10.09439  ?  175 GLN B CB  1 
ATOM   3168 C  CG  . GLN B 1 175 ? -0.50149  -10.05617 -0.85640  1.000 16.64162  ?  175 GLN B CG  1 
ATOM   3169 C  CD  . GLN B 1 175 ? -1.11722  -10.97654 0.16058   1.000 17.47522  ?  175 GLN B CD  1 
ATOM   3170 O  OE1 . GLN B 1 175 ? -0.42433  -11.51085 1.02335   1.000 10.85332  ?  175 GLN B OE1 1 
ATOM   3171 N  NE2 . GLN B 1 175 ? -2.43472  -11.15084 0.08566   1.000 17.32572  ?  175 GLN B NE2 1 
ATOM   3172 N  N   . ALA B 1 176 ? -0.63538  -5.58668  -0.38257  1.000 8.84264   ?  176 ALA B N   1 
ATOM   3173 C  CA  . ALA B 1 176 ? -0.65362  -4.37978  0.41961   1.000 10.92365  ?  176 ALA B CA  1 
ATOM   3174 C  C   . ALA B 1 176 ? -1.91278  -4.39577  1.27011   1.000 13.24964  ?  176 ALA B C   1 
ATOM   3175 O  O   . ALA B 1 176 ? -2.94961  -4.92095  0.85616   1.000 14.86868  ?  176 ALA B O   1 
ATOM   3176 C  CB  . ALA B 1 176 ? -0.61551  -3.11000  -0.45546  1.000 9.88894   ?  176 ALA B CB  1 
ATOM   3177 N  N   . VAL B 1 177 ? -1.82483  -3.82300  2.46496   1.000 9.36356   ?  177 VAL B N   1 
ATOM   3178 C  CA  . VAL B 1 177 ? -3.00668  -3.58342  3.27954   1.000 9.00694   ?  177 VAL B CA  1 
ATOM   3179 C  C   . VAL B 1 177 ? -3.24217  -2.08606  3.30887   1.000 11.67926  ?  177 VAL B C   1 
ATOM   3180 O  O   . VAL B 1 177 ? -2.29312  -1.29700  3.34377   1.000 11.54597  ?  177 VAL B O   1 
ATOM   3181 C  CB  . VAL B 1 177 ? -2.89894  -4.17433  4.70410   1.000 13.86414  ?  177 VAL B CB  1 
ATOM   3182 C  CG1 . VAL B 1 177 ? -1.80372  -3.47931  5.51273   1.000 10.95176  ?  177 VAL B CG1 1 
ATOM   3183 C  CG2 . VAL B 1 177 ? -4.24747  -4.08646  5.40660   1.000 11.75872  ?  177 VAL B CG2 1 
ATOM   3184 N  N   . LEU B 1 178 ? -4.50505  -1.70433  3.19169   1.000 11.82540  ?  178 LEU B N   1 
ATOM   3185 C  CA  . LEU B 1 178 ? -4.95974  -0.32930  3.31775   1.000 16.21549  ?  178 LEU B CA  1 
ATOM   3186 C  C   . LEU B 1 178 ? -5.79192  -0.24132  4.58542   1.000 14.30703  ?  178 LEU B C   1 
ATOM   3187 O  O   . LEU B 1 178 ? -6.64256  -1.10015  4.82808   1.000 15.01076  ?  178 LEU B O   1 
ATOM   3188 C  CB  . LEU B 1 178 ? -5.81584  0.08662   2.10714   1.000 16.87352  ?  178 LEU B CB  1 
ATOM   3189 C  CG  . LEU B 1 178 ? -5.19229  0.37669   0.73313   1.000 15.81600  ?  178 LEU B CG  1 
ATOM   3190 C  CD1 . LEU B 1 178 ? -4.30545  1.58908   0.81461   1.000 17.62644  ?  178 LEU B CD1 1 
ATOM   3191 C  CD2 . LEU B 1 178 ? -4.40257  -0.76524  0.14921   1.000 21.83438  ?  178 LEU B CD2 1 
ATOM   3192 N  N   . LEU B 1 179 ? -5.56454  0.77574   5.40761   1.000 9.86299   ?  179 LEU B N   1 
ATOM   3193 C  CA  . LEU B 1 179 ? -6.33394  0.77059   6.63714   1.000 11.77174  ?  179 LEU B CA  1 
ATOM   3194 C  C   . LEU B 1 179 ? -6.72345  2.17360   7.06969   1.000 16.72267  ?  179 LEU B C   1 
ATOM   3195 O  O   . LEU B 1 179 ? -6.02524  3.15748   6.79678   1.000 9.50971   ?  179 LEU B O   1 
ATOM   3196 C  CB  . LEU B 1 179 ? -5.58602  0.05767   7.76109   1.000 13.94556  ?  179 LEU B CB  1 
ATOM   3197 C  CG  . LEU B 1 179 ? -4.21306  0.54309   8.17158   1.000 17.44973  ?  179 LEU B CG  1 
ATOM   3198 C  CD1 . LEU B 1 179 ? -4.36045  1.42241   9.38165   1.000 20.57657  ?  179 LEU B CD1 1 
ATOM   3199 C  CD2 . LEU B 1 179 ? -3.30108  -0.62755  8.48341   1.000 23.23312  ?  179 LEU B CD2 1 
ATOM   3200 N  N   . ASP B 1 180 ? -7.85622  2.22843   7.76480   1.000 8.23496   ?  180 ASP B N   1 
ATOM   3201 C  CA  . ASP B 1 180 ? -8.31211  3.38797   8.52087   1.000 12.00887  ?  180 ASP B CA  1 
ATOM   3202 C  C   . ASP B 1 180 ? -7.43948  3.51031   9.76459   1.000 10.07794  ?  180 ASP B C   1 
ATOM   3203 O  O   . ASP B 1 180 ? -7.61195  2.77053   10.73647  1.000 14.68745  ?  180 ASP B O   1 
ATOM   3204 C  CB  . ASP B 1 180 ? -9.78820  3.21160   8.86971   1.000 14.51405  ?  180 ASP B CB  1 
ATOM   3205 C  CG  . ASP B 1 180 ? -10.30103 4.24648   9.84843   1.000 19.37036  ?  180 ASP B CG  1 
ATOM   3206 O  OD1 . ASP B 1 180 ? -9.58491  5.21588   10.16703  1.000 15.40518  ?  180 ASP B OD1 1 
ATOM   3207 O  OD2 . ASP B 1 180 ? -11.44829 4.08521   10.31132  1.000 23.41340  -1 180 ASP B OD2 1 
ATOM   3208 N  N   . ASP B 1 181 ? -6.48969  4.44391   9.72198   1.000 11.15853  ?  181 ASP B N   1 
ATOM   3209 C  CA  . ASP B 1 181 ? -5.47457  4.60093   10.75543  1.000 10.63967  ?  181 ASP B CA  1 
ATOM   3210 C  C   . ASP B 1 181 ? -6.01244  5.31328   11.98763  1.000 16.39258  ?  181 ASP B C   1 
ATOM   3211 O  O   . ASP B 1 181 ? -5.30788  5.38650   13.00007  1.000 12.65381  ?  181 ASP B O   1 
ATOM   3212 C  CB  . ASP B 1 181 ? -4.26977  5.35724   10.16448  1.000 11.27745  ?  181 ASP B CB  1 
ATOM   3213 C  CG  . ASP B 1 181 ? -3.05599  5.42526   11.11369  1.000 11.01644  ?  181 ASP B CG  1 
ATOM   3214 O  OD1 . ASP B 1 181 ? -2.67714  4.39093   11.69802  1.000 9.71505   ?  181 ASP B OD1 1 
ATOM   3215 O  OD2 . ASP B 1 181 ? -2.45248  6.51679   11.24291  1.000 14.16413  -1 181 ASP B OD2 1 
ATOM   3216 N  N   . ARG B 1 182 ? -7.24873  5.81293   11.93318  1.000 12.24662  ?  182 ARG B N   1 
ATOM   3217 C  CA  . ARG B 1 182 ? -7.88966  6.45862   13.07560  1.000 15.20906  ?  182 ARG B CA  1 
ATOM   3218 C  C   . ARG B 1 182 ? -8.81995  5.50132   13.81665  1.000 14.02544  ?  182 ARG B C   1 
ATOM   3219 O  O   . ARG B 1 182 ? -8.79940  5.43401   15.05157  1.000 15.00967  ?  182 ARG B O   1 
ATOM   3220 C  CB  . ARG B 1 182 ? -8.65940  7.69847   12.60552  1.000 13.00799  ?  182 ARG B CB  1 
ATOM   3221 C  CG  . ARG B 1 182 ? -7.74853  8.78519   12.04823  1.000 14.74001  ?  182 ARG B CG  1 
ATOM   3222 C  CD  . ARG B 1 182 ? -8.51280  9.98621   11.50387  1.000 13.34213  ?  182 ARG B CD  1 
ATOM   3223 N  NE  . ARG B 1 182 ? -7.61386  11.10524  11.23794  1.000 15.91404  ?  182 ARG B NE  1 
ATOM   3224 C  CZ  . ARG B 1 182 ? -7.95716  12.21861  10.60396  1.000 19.96343  ?  182 ARG B CZ  1 
ATOM   3225 N  NH1 . ARG B 1 182 ? -9.17066  12.38342  10.09936  1.000 20.74050  ?  182 ARG B NH1 1 
ATOM   3226 N  NH2 . ARG B 1 182 ? -7.06022  13.19013  10.47182  1.000 16.48610  ?  182 ARG B NH2 1 
ATOM   3227 N  N   . GLY B 1 183 ? -9.61891  4.74259   13.06444  1.000 14.08052  ?  183 GLY B N   1 
ATOM   3228 C  CA  . GLY B 1 183 ? -10.55017 3.78678   13.63910  1.000 16.57560  ?  183 GLY B CA  1 
ATOM   3229 C  C   . GLY B 1 183 ? -9.93942  2.46453   14.04826  1.000 15.81597  ?  183 GLY B C   1 
ATOM   3230 O  O   . GLY B 1 183 ? -10.51822 1.77443   14.89451  1.000 14.13524  ?  183 GLY B O   1 
ATOM   3231 N  N   . LEU B 1 184 ? -8.78635  2.09527   13.47778  1.000 8.19417   ?  184 LEU B N   1 
ATOM   3232 C  CA  . LEU B 1 184 ? -8.09726  0.85942   13.81119  1.000 10.95396  ?  184 LEU B CA  1 
ATOM   3233 C  C   . LEU B 1 184 ? -6.68322  1.16982   14.27896  1.000 7.80987   ?  184 LEU B C   1 
ATOM   3234 O  O   . LEU B 1 184 ? -6.09578  2.19073   13.90780  1.000 13.37432  ?  184 LEU B O   1 
ATOM   3235 C  CB  . LEU B 1 184 ? -8.00684  -0.09873  12.60890  1.000 11.74465  ?  184 LEU B CB  1 
ATOM   3236 C  CG  . LEU B 1 184 ? -9.27106  -0.57614  11.91897  1.000 18.82358  ?  184 LEU B CG  1 
ATOM   3237 C  CD1 . LEU B 1 184 ? -8.86850  -1.58010  10.85026  1.000 15.03376  ?  184 LEU B CD1 1 
ATOM   3238 C  CD2 . LEU B 1 184 ? -10.20297 -1.21020  12.94294  1.000 16.24882  ?  184 LEU B CD2 1 
ATOM   3239 N  N   . ALA B 1 185 ? -6.14220  0.27362   15.09992  1.000 10.23160  ?  185 ALA B N   1 
ATOM   3240 C  CA  . ALA B 1 185 ? -4.72041  0.25066   15.42127  1.000 10.86044  ?  185 ALA B CA  1 
ATOM   3241 C  C   . ALA B 1 185 ? -4.11378  -1.02156  14.85043  1.000 9.63562   ?  185 ALA B C   1 
ATOM   3242 O  O   . ALA B 1 185 ? -4.82061  -1.95155  14.46464  1.000 9.27201   ?  185 ALA B O   1 
ATOM   3243 C  CB  . ALA B 1 185 ? -4.48219  0.32282   16.93894  1.000 8.54403   ?  185 ALA B CB  1 
ATOM   3244 N  N   . HIS B 1 186 ? -2.78582  -1.05924  14.77782  1.000 8.27994   ?  186 HIS B N   1 
ATOM   3245 C  CA  . HIS B 1 186 ? -2.13993  -2.21714  14.18120  1.000 9.05716   ?  186 HIS B CA  1 
ATOM   3246 C  C   . HIS B 1 186 ? -0.82910  -2.50338  14.89833  1.000 14.12086  ?  186 HIS B C   1 
ATOM   3247 O  O   . HIS B 1 186 ? -0.22887  -1.62832  15.53144  1.000 7.42535   ?  186 HIS B O   1 
ATOM   3248 C  CB  . HIS B 1 186 ? -1.89119  -2.02610  12.66893  1.000 10.01732  ?  186 HIS B CB  1 
ATOM   3249 C  CG  . HIS B 1 186 ? -1.10592  -0.79278  12.32057  1.000 9.72053   ?  186 HIS B CG  1 
ATOM   3250 N  ND1 . HIS B 1 186 ? -1.67228  0.46308   12.29279  1.000 10.49284  ?  186 HIS B ND1 1 
ATOM   3251 C  CD2 . HIS B 1 186 ? 0.19061   -0.62861  11.94860  1.000 9.63952   ?  186 HIS B CD2 1 
ATOM   3252 C  CE1 . HIS B 1 186 ? -0.75741  1.34997   11.94256  1.000 13.01980  ?  186 HIS B CE1 1 
ATOM   3253 N  NE2 . HIS B 1 186 ? 0.38201   0.71453   11.72378  1.000 13.13730  ?  186 HIS B NE2 1 
ATOM   3254 N  N   . ASP B 1 187 ? -0.39852  -3.75625  14.79751  1.000 12.44966  ?  187 ASP B N   1 
ATOM   3255 C  CA  . ASP B 1 187 ? 0.99396   -4.09695  15.00628  1.000 10.26521  ?  187 ASP B CA  1 
ATOM   3256 C  C   . ASP B 1 187 ? 1.33384   -5.21883  14.04493  1.000 8.80091   ?  187 ASP B C   1 
ATOM   3257 O  O   . ASP B 1 187 ? 0.48449   -5.69481  13.27540  1.000 9.39464   ?  187 ASP B O   1 
ATOM   3258 C  CB  . ASP B 1 187 ? 1.30218   -4.43011  16.48444  1.000 9.80968   ?  187 ASP B CB  1 
ATOM   3259 C  CG  . ASP B 1 187 ? 0.79077   -5.79453  16.93462  1.000 13.91459  ?  187 ASP B CG  1 
ATOM   3260 O  OD1 . ASP B 1 187 ? -0.17880  -6.36207  16.36787  1.000 9.57786   ?  187 ASP B OD1 1 
ATOM   3261 O  OD2 . ASP B 1 187 ? 1.37895   -6.29436  17.92002  1.000 12.12173  -1 187 ASP B OD2 1 
ATOM   3262 N  N   . VAL B 1 188 ? 2.60015   -5.59850  14.03152  1.000 5.07894   ?  188 VAL B N   1 
ATOM   3263 C  CA  . VAL B 1 188 ? 3.05773   -6.72427  13.22581  1.000 6.36591   ?  188 VAL B CA  1 
ATOM   3264 C  C   . VAL B 1 188 ? 4.04371   -7.51417  14.07352  1.000 8.60683   ?  188 VAL B C   1 
ATOM   3265 O  O   . VAL B 1 188 ? 4.89669   -6.92234  14.75097  1.000 8.67117   ?  188 VAL B O   1 
ATOM   3266 C  CB  . VAL B 1 188 ? 3.71574   -6.26026  11.91102  1.000 9.37887   ?  188 VAL B CB  1 
ATOM   3267 C  CG1 . VAL B 1 188 ? 3.96484   -7.46879  10.99561  1.000 11.41906  ?  188 VAL B CG1 1 
ATOM   3268 C  CG2 . VAL B 1 188 ? 2.85409   -5.20688  11.18698  1.000 6.83036   ?  188 VAL B CG2 1 
ATOM   3269 N  N   . THR B 1 189 ? 3.93602   -8.84426  14.03048  1.000 8.23042   ?  189 THR B N   1 
ATOM   3270 C  CA  . THR B 1 189 ? 4.89279   -9.66691  14.74993  1.000 11.57647  ?  189 THR B CA  1 
ATOM   3271 C  C   . THR B 1 189 ? 6.26699   -9.56496  14.09297  1.000 8.11034   ?  189 THR B C   1 
ATOM   3272 O  O   . THR B 1 189 ? 6.38942   -9.29637  12.89376  1.000 9.23967   ?  189 THR B O   1 
ATOM   3273 C  CB  . THR B 1 189 ? 4.42149   -11.13218 14.83084  1.000 9.57386   ?  189 THR B CB  1 
ATOM   3274 O  OG1 . THR B 1 189 ? 4.42434   -11.74333 13.53365  1.000 13.06630  ?  189 THR B OG1 1 
ATOM   3275 C  CG2 . THR B 1 189 ? 3.00256   -11.21292 15.42819  1.000 10.15748  ?  189 THR B CG2 1 
ATOM   3276 N  N   . ASP B 1 190 ? 7.30879   -9.78205  14.90054  1.000 10.65095  ?  190 ASP B N   1 
ATOM   3277 C  CA  . ASP B 1 190 ? 8.67912   -9.72883  14.40510  1.000 9.74437   ?  190 ASP B CA  1 
ATOM   3278 C  C   . ASP B 1 190 ? 8.88025   -10.65555 13.21372  1.000 12.47760  ?  190 ASP B C   1 
ATOM   3279 O  O   . ASP B 1 190 ? 8.31082   -11.74689 13.14491  1.000 11.25770  ?  190 ASP B O   1 
ATOM   3280 C  CB  . ASP B 1 190 ? 9.67905   -10.15235 15.48274  1.000 10.12670  ?  190 ASP B CB  1 
ATOM   3281 C  CG  . ASP B 1 190 ? 9.74734   -9.19205  16.65954  1.000 22.26143  ?  190 ASP B CG  1 
ATOM   3282 O  OD1 . ASP B 1 190 ? 9.20728   -8.06281  16.59162  1.000 10.69678  ?  190 ASP B OD1 1 
ATOM   3283 O  OD2 . ASP B 1 190 ? 10.36213  -9.59574  17.67212  1.000 20.65221  -1 190 ASP B OD2 1 
ATOM   3284 N  N   . VAL B 1 191 ? 9.71760   -10.19703 12.28089  1.000 13.72677  ?  191 VAL B N   1 
ATOM   3285 C  CA  . VAL B 1 191 ? 10.30723  -11.06009 11.26762  1.000 12.38830  ?  191 VAL B CA  1 
ATOM   3286 C  C   . VAL B 1 191 ? 11.24043  -12.05776 11.93586  1.000 16.78620  ?  191 VAL B C   1 
ATOM   3287 O  O   . VAL B 1 191 ? 12.12376  -11.66881 12.70752  1.000 11.06768  ?  191 VAL B O   1 
ATOM   3288 C  CB  . VAL B 1 191 ? 11.10712  -10.22456 10.26033  1.000 15.61296  ?  191 VAL B CB  1 
ATOM   3289 C  CG1 . VAL B 1 191 ? 11.42598  -11.05816 9.08862   1.000 24.85288  ?  191 VAL B CG1 1 
ATOM   3290 C  CG2 . VAL B 1 191 ? 10.37103  -9.02405  9.84200   1.000 18.00566  ?  191 VAL B CG2 1 
ATOM   3291 N  N   . LEU B 1 192 ? 11.09545  -13.33838 11.59958  1.000 11.35788  ?  192 LEU B N   1 
ATOM   3292 C  CA  . LEU B 1 192 ? 12.00238  -14.37307 12.07475  1.000 12.72731  ?  192 LEU B CA  1 
ATOM   3293 C  C   . LEU B 1 192 ? 12.79147  -14.96129 10.91504  1.000 19.08400  ?  192 LEU B C   1 
ATOM   3294 O  O   . LEU B 1 192 ? 12.32425  -14.97622 9.77350   1.000 16.73062  ?  192 LEU B O   1 
ATOM   3295 C  CB  . LEU B 1 192 ? 11.25021  -15.51183 12.76561  1.000 13.89972  ?  192 LEU B CB  1 
ATOM   3296 C  CG  . LEU B 1 192 ? 10.38294  -15.09556 13.94157  1.000 19.41258  ?  192 LEU B CG  1 
ATOM   3297 C  CD1 . LEU B 1 192 ? 9.57689   -16.28466 14.43856  1.000 21.45888  ?  192 LEU B CD1 1 
ATOM   3298 C  CD2 . LEU B 1 192 ? 11.27380  -14.53134 15.03268  1.000 18.37274  ?  192 LEU B CD2 1 
ATOM   3299 N  N   . SER B 1 193 ? 13.98458  -15.46748 11.22220  1.000 13.47366  ?  193 SER B N   1 
ATOM   3300 C  CA  . SER B 1 193 ? 14.73928  -16.23857 10.24403  1.000 19.28941  ?  193 SER B CA  1 
ATOM   3301 C  C   . SER B 1 193 ? 14.01338  -17.54620 9.99608   1.000 17.08660  ?  193 SER B C   1 
ATOM   3302 O  O   . SER B 1 193 ? 13.62952  -18.23273 10.94670  1.000 13.58869  ?  193 SER B O   1 
ATOM   3303 C  CB  . SER B 1 193 ? 16.15572  -16.51720 10.74385  1.000 22.02673  ?  193 SER B CB  1 
ATOM   3304 O  OG  . SER B 1 193 ? 16.84251  -17.41463 9.88167   1.000 19.36119  ?  193 SER B OG  1 
ATOM   3305 N  N   . ALA B 1 194 ? 13.80930  -17.88674 8.71758   1.000 17.27583  ?  194 ALA B N   1 
ATOM   3306 C  CA  . ALA B 1 194 ? 13.04929  -19.09486 8.40230   1.000 16.77376  ?  194 ALA B CA  1 
ATOM   3307 C  C   . ALA B 1 194 ? 13.86327  -20.37269 8.60096   1.000 19.99977  ?  194 ALA B C   1 
ATOM   3308 O  O   . ALA B 1 194 ? 13.28417  -21.42394 8.90541   1.000 20.46237  ?  194 ALA B O   1 
ATOM   3309 C  CB  . ALA B 1 194 ? 12.51667  -19.03022 6.96911   1.000 16.59627  ?  194 ALA B CB  1 
ATOM   3310 N  N   . ASP B 1 195 ? 15.18795  -20.31812 8.43811   1.000 17.21569  ?  195 ASP B N   1 
ATOM   3311 C  CA  . ASP B 1 195 ? 15.99148  -21.53207 8.50213   1.000 23.84841  ?  195 ASP B CA  1 
ATOM   3312 C  C   . ASP B 1 195 ? 17.16868  -21.42802 9.46339   1.000 28.86012  ?  195 ASP B C   1 
ATOM   3313 O  O   . ASP B 1 195 ? 17.97954  -22.36231 9.52944   1.000 20.68635  ?  195 ASP B O   1 
ATOM   3314 C  CB  . ASP B 1 195 ? 16.49188  -21.92224 7.09999   1.000 21.25576  ?  195 ASP B CB  1 
ATOM   3315 C  CG  . ASP B 1 195 ? 17.46832  -20.91400 6.50795   1.000 28.96271  ?  195 ASP B CG  1 
ATOM   3316 O  OD1 . ASP B 1 195 ? 17.75485  -19.87486 7.15002   1.000 24.02328  ?  195 ASP B OD1 1 
ATOM   3317 O  OD2 . ASP B 1 195 ? 17.96058  -21.16595 5.38256   1.000 29.45139  -1 195 ASP B OD2 1 
ATOM   3318 N  N   . GLY B 1 196 ? 17.28810  -20.32697 10.21082  1.000 19.48183  ?  196 GLY B N   1 
ATOM   3319 C  CA  . GLY B 1 196 ? 18.44624  -20.07123 11.03178  1.000 16.78369  ?  196 GLY B CA  1 
ATOM   3320 C  C   . GLY B 1 196 ? 19.44713  -19.11869 10.41431  1.000 19.47070  ?  196 GLY B C   1 
ATOM   3321 O  O   . GLY B 1 196 ? 20.32853  -18.61507 11.12833  1.000 20.54141  ?  196 GLY B O   1 
ATOM   3322 N  N   . GLY B 1 197 ? 19.34302  -18.86156 9.11344   1.000 13.78354  ?  197 GLY B N   1 
ATOM   3323 C  CA  . GLY B 1 197 ? 20.23463  -17.94427 8.43922   1.000 17.38787  ?  197 GLY B CA  1 
ATOM   3324 C  C   . GLY B 1 197 ? 19.58844  -16.59302 8.17128   1.000 16.22001  ?  197 GLY B C   1 
ATOM   3325 O  O   . GLY B 1 197 ? 18.46078  -16.32094 8.59283   1.000 15.42556  ?  197 GLY B O   1 
ATOM   3326 N  N   . PRO B 1 198 ? 20.29436  -15.72715 7.45753   1.000 14.46187  ?  198 PRO B N   1 
ATOM   3327 C  CA  . PRO B 1 198 ? 19.78754  -14.36889 7.23200   1.000 19.20701  ?  198 PRO B CA  1 
ATOM   3328 C  C   . PRO B 1 198 ? 18.56888  -14.34092 6.31616   1.000 23.58361  ?  198 PRO B C   1 
ATOM   3329 O  O   . PRO B 1 198 ? 18.40940  -15.17233 5.41794   1.000 15.14849  ?  198 PRO B O   1 
ATOM   3330 C  CB  . PRO B 1 198 ? 20.97689  -13.64115 6.59547   1.000 18.33159  ?  198 PRO B CB  1 
ATOM   3331 C  CG  . PRO B 1 198 ? 21.91530  -14.71872 6.14417   1.000 34.67326  ?  198 PRO B CG  1 
ATOM   3332 C  CD  . PRO B 1 198 ? 21.68329  -15.90743 7.00236   1.000 17.73163  ?  198 PRO B CD  1 
ATOM   3333 N  N   . GLY B 1 199 ? 17.68931  -13.36956 6.57940   1.000 11.08191  ?  199 GLY B N   1 
ATOM   3334 C  CA  . GLY B 1 199 ? 16.50296  -13.13930 5.77415   1.000 12.61395  ?  199 GLY B CA  1 
ATOM   3335 C  C   . GLY B 1 199 ? 16.08535  -11.68918 5.90283   1.000 17.27246  ?  199 GLY B C   1 
ATOM   3336 O  O   . GLY B 1 199 ? 16.58639  -10.95733 6.76076   1.000 13.23455  ?  199 GLY B O   1 
ATOM   3337 N  N   . HIS B 1 200 ? 15.18087  -11.26230 5.02282   1.000 10.01444  ?  200 HIS B N   1 
ATOM   3338 C  CA  . HIS B 1 200 ? 14.81442  -9.85021  5.02299   1.000 11.82019  ?  200 HIS B CA  1 
ATOM   3339 C  C   . HIS B 1 200 ? 13.43195  -9.65869  4.42170   1.000 16.95704  ?  200 HIS B C   1 
ATOM   3340 O  O   . HIS B 1 200 ? 12.90250  -10.53043 3.72914   1.000 10.94831  ?  200 HIS B O   1 
ATOM   3341 C  CB  . HIS B 1 200 ? 15.83852  -8.98797  4.27864   1.000 14.34807  ?  200 HIS B CB  1 
ATOM   3342 C  CG  . HIS B 1 200 ? 16.03151  -9.36649  2.84179   1.000 19.08167  ?  200 HIS B CG  1 
ATOM   3343 N  ND1 . HIS B 1 200 ? 15.34306  -8.76109  1.81014   1.000 19.50650  ?  200 HIS B ND1 1 
ATOM   3344 C  CD2 . HIS B 1 200 ? 16.85810  -10.27060 2.26306   1.000 20.54259  ?  200 HIS B CD2 1 
ATOM   3345 C  CE1 . HIS B 1 200 ? 15.73049  -9.28295  0.65947   1.000 19.14750  ?  200 HIS B CE1 1 
ATOM   3346 N  NE2 . HIS B 1 200 ? 16.65151  -10.19748 0.90520   1.000 25.55800  ?  200 HIS B NE2 1 
ATOM   3347 N  N   . ARG B 1 201 ? 12.86069  -8.48658  4.70040   1.000 8.58001   ?  201 ARG B N   1 
ATOM   3348 C  CA  . ARG B 1 201 ? 11.49800  -8.15684  4.29883   1.000 10.71198  ?  201 ARG B CA  1 
ATOM   3349 C  C   . ARG B 1 201 ? 11.49942  -6.69674  3.88916   1.000 12.33203  ?  201 ARG B C   1 
ATOM   3350 O  O   . ARG B 1 201 ? 11.84971  -5.82339  4.69378   1.000 8.78331   ?  201 ARG B O   1 
ATOM   3351 C  CB  . ARG B 1 201 ? 10.51053  -8.42467  5.44245   1.000 8.15311   ?  201 ARG B CB  1 
ATOM   3352 C  CG  . ARG B 1 201 ? 9.04575   -7.96368  5.24201   1.000 5.79733   ?  201 ARG B CG  1 
ATOM   3353 C  CD  . ARG B 1 201 ? 8.20991   -8.41165  6.43506   1.000 9.03201   ?  201 ARG B CD  1 
ATOM   3354 N  NE  . ARG B 1 201 ? 6.80165   -8.01540  6.42965   1.000 7.88319   ?  201 ARG B NE  1 
ATOM   3355 C  CZ  . ARG B 1 201 ? 6.32920   -6.86129  6.89349   1.000 9.64731   ?  201 ARG B CZ  1 
ATOM   3356 N  NH1 . ARG B 1 201 ? 7.12986   -5.83882  7.15792   1.000 9.01072   ?  201 ARG B NH1 1 
ATOM   3357 N  NH2 . ARG B 1 201 ? 5.01583   -6.72910  7.09780   1.000 9.16824   ?  201 ARG B NH2 1 
ATOM   3358 N  N   . ASP B 1 202 ? 11.14186  -6.44514  2.63575   1.000 9.37705   ?  202 ASP B N   1 
ATOM   3359 C  CA  . ASP B 1 202 ? 11.23755  -5.13578  2.01215   1.000 8.84595   ?  202 ASP B CA  1 
ATOM   3360 C  C   . ASP B 1 202 ? 9.83913   -4.61713  1.74577   1.000 10.12393  ?  202 ASP B C   1 
ATOM   3361 O  O   . ASP B 1 202 ? 9.04040   -5.29186  1.08241   1.000 11.27333  ?  202 ASP B O   1 
ATOM   3362 C  CB  . ASP B 1 202 ? 12.01129  -5.22291  0.70129   1.000 9.72914   ?  202 ASP B CB  1 
ATOM   3363 C  CG  . ASP B 1 202 ? 13.41069  -5.72788  0.89501   1.000 16.75672  ?  202 ASP B CG  1 
ATOM   3364 O  OD1 . ASP B 1 202 ? 13.92576  -5.66365  2.03814   1.000 14.68123  ?  202 ASP B OD1 1 
ATOM   3365 O  OD2 . ASP B 1 202 ? 14.00783  -6.18633  -0.09960  1.000 15.26071  -1 202 ASP B OD2 1 
ATOM   3366 N  N   . ILE B 1 203 ? 9.54818   -3.42159  2.24702   1.000 8.52434   ?  203 ILE B N   1 
ATOM   3367 C  CA  . ILE B 1 203 ? 8.20085   -2.87843  2.25041   1.000 7.34427   ?  203 ILE B CA  1 
ATOM   3368 C  C   . ILE B 1 203 ? 8.26663   -1.39154  1.93549   1.000 7.64559   ?  203 ILE B C   1 
ATOM   3369 O  O   . ILE B 1 203 ? 9.32585   -0.76344  1.97485   1.000 10.49767  ?  203 ILE B O   1 
ATOM   3370 C  CB  . ILE B 1 203 ? 7.48815   -3.09189  3.60129   1.000 10.53975  ?  203 ILE B CB  1 
ATOM   3371 C  CG1 . ILE B 1 203 ? 8.10838   -2.17859  4.66971   1.000 8.68241   ?  203 ILE B CG1 1 
ATOM   3372 C  CG2 . ILE B 1 203 ? 7.54270   -4.58522  4.03066   1.000 8.42771   ?  203 ILE B CG2 1 
ATOM   3373 C  CD1 . ILE B 1 203 ? 7.38171   -2.20370  5.99228   1.000 8.38665   ?  203 ILE B CD1 1 
ATOM   3374 N  N   . VAL B 1 204 ? 7.11325   -0.83280  1.60914   1.000 6.04619   ?  204 VAL B N   1 
ATOM   3375 C  CA  . VAL B 1 204 ? 6.94080   0.60908   1.56751   1.000 7.38784   ?  204 VAL B CA  1 
ATOM   3376 C  C   . VAL B 1 204 ? 5.68727   0.93482   2.36391   1.000 11.57953  ?  204 VAL B C   1 
ATOM   3377 O  O   . VAL B 1 204 ? 4.67608   0.22877   2.27404   1.000 9.04125   ?  204 VAL B O   1 
ATOM   3378 C  CB  . VAL B 1 204 ? 6.87253   1.15281   0.12409   1.000 12.53837  ?  204 VAL B CB  1 
ATOM   3379 C  CG1 . VAL B 1 204 ? 5.68398   0.57720   -0.61065  1.000 11.85505  ?  204 VAL B CG1 1 
ATOM   3380 C  CG2 . VAL B 1 204 ? 6.84304   2.68931   0.12947   1.000 9.62174   ?  204 VAL B CG2 1 
ATOM   3381 N  N   . ILE B 1 205 ? 5.78346   1.95701   3.20504   1.000 5.76421   ?  205 ILE B N   1 
ATOM   3382 C  CA  . ILE B 1 205 ? 4.67096   2.42715   4.01911   1.000 6.96023   ?  205 ILE B CA  1 
ATOM   3383 C  C   . ILE B 1 205 ? 4.30988   3.81902   3.53946   1.000 12.79895  ?  205 ILE B C   1 
ATOM   3384 O  O   . ILE B 1 205 ? 5.18506   4.68815   3.44446   1.000 9.28304   ?  205 ILE B O   1 
ATOM   3385 C  CB  . ILE B 1 205 ? 5.04531   2.46011   5.50841   1.000 9.11051   ?  205 ILE B CB  1 
ATOM   3386 C  CG1 . ILE B 1 205 ? 5.50388   1.07802   5.96770   1.000 10.65786  ?  205 ILE B CG1 1 
ATOM   3387 C  CG2 . ILE B 1 205 ? 3.87369   2.95035   6.34471   1.000 9.45334   ?  205 ILE B CG2 1 
ATOM   3388 C  CD1 . ILE B 1 205 ? 6.07174   1.08990   7.38523   1.000 10.65492  ?  205 ILE B CD1 1 
ATOM   3389 N  N   . ILE B 1 206 ? 3.03051   4.03666   3.24451   1.000 9.50263   ?  206 ILE B N   1 
ATOM   3390 C  CA  . ILE B 1 206 ? 2.55159   5.33830   2.80236   1.000 9.21975   ?  206 ILE B CA  1 
ATOM   3391 C  C   . ILE B 1 206 ? 1.49829   5.81921   3.78845   1.000 8.75717   ?  206 ILE B C   1 
ATOM   3392 O  O   . ILE B 1 206 ? 0.46613   5.16569   3.96380   1.000 9.81681   ?  206 ILE B O   1 
ATOM   3393 C  CB  . ILE B 1 206 ? 1.98161   5.28374   1.37655   1.000 7.81273   ?  206 ILE B CB  1 
ATOM   3394 C  CG1 . ILE B 1 206 ? 3.01846   4.71077   0.41553   1.000 8.19083   ?  206 ILE B CG1 1 
ATOM   3395 C  CG2 . ILE B 1 206 ? 1.58329   6.68824   0.93136   1.000 10.59751  ?  206 ILE B CG2 1 
ATOM   3396 C  CD1 . ILE B 1 206 ? 2.82532   3.24141   0.09463   1.000 12.86197  ?  206 ILE B CD1 1 
ATOM   3397 N  N   . ALA B 1 207 ? 1.74011   6.97291   4.40615   1.000 9.96939   ?  207 ALA B N   1 
ATOM   3398 C  CA  . ALA B 1 207 ? 0.81899   7.54604   5.37822   1.000 8.12446   ?  207 ALA B CA  1 
ATOM   3399 C  C   . ALA B 1 207 ? 0.13784   8.76323   4.76939   1.000 14.01035  ?  207 ALA B C   1 
ATOM   3400 O  O   . ALA B 1 207 ? 0.81942   9.69938   4.33901   1.000 9.71566   ?  207 ALA B O   1 
ATOM   3401 C  CB  . ALA B 1 207 ? 1.55978   7.94534   6.64989   1.000 6.03334   ?  207 ALA B CB  1 
ATOM   3402 N  N   . PHE B 1 208 ? -1.19508  8.75989   4.76714   1.000 11.70537  ?  208 PHE B N   1 
ATOM   3403 C  CA  . PHE B 1 208 ? -1.99528  9.73563   4.03203   1.000 14.41498  ?  208 PHE B CA  1 
ATOM   3404 C  C   . PHE B 1 208 ? -2.61816  10.73349  4.99373   1.000 11.64714  ?  208 PHE B C   1 
ATOM   3405 O  O   . PHE B 1 208 ? -3.35985  10.34381  5.90293   1.000 10.90026  ?  208 PHE B O   1 
ATOM   3406 C  CB  . PHE B 1 208 ? -3.13257  9.07288   3.23834   1.000 9.04178   ?  208 PHE B CB  1 
ATOM   3407 C  CG  . PHE B 1 208 ? -2.68957  8.18384   2.12224   1.000 12.49056  ?  208 PHE B CG  1 
ATOM   3408 C  CD1 . PHE B 1 208 ? -2.32417  6.87515   2.36897   1.000 16.35065  ?  208 PHE B CD1 1 
ATOM   3409 C  CD2 . PHE B 1 208 ? -2.72632  8.62737   0.80579   1.000 15.81922  ?  208 PHE B CD2 1 
ATOM   3410 C  CE1 . PHE B 1 208 ? -1.95123  6.03957   1.33901   1.000 10.59873  ?  208 PHE B CE1 1 
ATOM   3411 C  CE2 . PHE B 1 208 ? -2.35845  7.80167   -0.23089  1.000 11.50805  ?  208 PHE B CE2 1 
ATOM   3412 C  CZ  . PHE B 1 208 ? -1.96638  6.50250   0.02897   1.000 13.11965  ?  208 PHE B CZ  1 
ATOM   3413 N  N   . SER B 1 209 ? -2.38072  12.01764  4.74244   1.000 11.85081  ?  209 SER B N   1 
ATOM   3414 C  CA  . SER B 1 209 ? -3.00129  13.09459  5.49655   1.000 12.02773  ?  209 SER B CA  1 
ATOM   3415 C  C   . SER B 1 209 ? -3.46772  14.16405  4.52016   1.000 12.97478  ?  209 SER B C   1 
ATOM   3416 O  O   . SER B 1 209 ? -2.79376  14.42872  3.52245   1.000 12.46190  ?  209 SER B O   1 
ATOM   3417 C  CB  . SER B 1 209 ? -2.02839  13.70878  6.51469   1.000 8.11883   ?  209 SER B CB  1 
ATOM   3418 O  OG  . SER B 1 209 ? -1.76826  12.79952  7.58661   1.000 11.63588  ?  209 SER B OG  1 
ATOM   3419 N  N   . ARG B 1 210 ? -4.61687  14.77208  4.80992   1.000 17.86767  ?  210 ARG B N   1 
ATOM   3420 C  CA  . ARG B 1 210 ? -5.04378  15.93034  4.03240   1.000 15.98566  ?  210 ARG B CA  1 
ATOM   3421 C  C   . ARG B 1 210 ? -4.00366  17.03489  4.14312   1.000 15.73689  ?  210 ARG B C   1 
ATOM   3422 O  O   . ARG B 1 210 ? -3.35028  17.20101  5.17910   1.000 11.72256  ?  210 ARG B O   1 
ATOM   3423 C  CB  . ARG B 1 210 ? -6.40385  16.43071  4.51410   1.000 11.79504  ?  210 ARG B CB  1 
ATOM   3424 C  CG  . ARG B 1 210 ? -7.51054  15.43907  4.24471   1.000 12.99758  ?  210 ARG B CG  1 
ATOM   3425 C  CD  . ARG B 1 210 ? -8.75200  15.68711  5.07555   1.000 19.69591  ?  210 ARG B CD  1 
ATOM   3426 N  NE  . ARG B 1 210 ? -9.59265  14.49812  5.06934   1.000 19.18179  ?  210 ARG B NE  1 
ATOM   3427 C  CZ  . ARG B 1 210 ? -10.55598 14.25390  4.19080   1.000 24.98216  ?  210 ARG B CZ  1 
ATOM   3428 N  NH1 . ARG B 1 210 ? -10.89104 15.13773  3.26263   1.000 23.96842  ?  210 ARG B NH1 1 
ATOM   3429 N  NH2 . ARG B 1 210 ? -11.19366 13.09070  4.23912   1.000 24.35202  ?  210 ARG B NH2 1 
ATOM   3430 N  N   . TRP B 1 211 ? -3.83629  17.77986  3.04480   1.000 12.67502  ?  211 TRP B N   1 
ATOM   3431 C  CA  . TRP B 1 211 ? -2.85453  18.85703  3.01970   1.000 11.50827  ?  211 TRP B CA  1 
ATOM   3432 C  C   . TRP B 1 211 ? -3.07331  19.83378  4.16331   1.000 10.32512  ?  211 TRP B C   1 
ATOM   3433 O  O   . TRP B 1 211 ? -2.11057  20.33881  4.75589   1.000 13.94712  ?  211 TRP B O   1 
ATOM   3434 C  CB  . TRP B 1 211 ? -2.92589  19.59444  1.68518   1.000 14.96103  ?  211 TRP B CB  1 
ATOM   3435 C  CG  . TRP B 1 211 ? -1.86577  20.58817  1.58985   1.000 12.65757  ?  211 TRP B CG  1 
ATOM   3436 C  CD1 . TRP B 1 211 ? -1.95370  21.92598  1.84890   1.000 9.63982   ?  211 TRP B CD1 1 
ATOM   3437 C  CD2 . TRP B 1 211 ? -0.51370  20.33261  1.23779   1.000 13.19063  ?  211 TRP B CD2 1 
ATOM   3438 N  NE1 . TRP B 1 211 ? -0.73358  22.51787  1.65478   1.000 13.82501  ?  211 TRP B NE1 1 
ATOM   3439 C  CE2 . TRP B 1 211 ? 0.17024   21.55556  1.29248   1.000 12.57296  ?  211 TRP B CE2 1 
ATOM   3440 C  CE3 . TRP B 1 211 ? 0.18875   19.18046  0.87852   1.000 12.84005  ?  211 TRP B CE3 1 
ATOM   3441 C  CZ2 . TRP B 1 211 ? 1.51808   21.66055  0.99355   1.000 24.92479  ?  211 TRP B CZ2 1 
ATOM   3442 C  CZ3 . TRP B 1 211 ? 1.53140   19.28652  0.58683   1.000 12.73418  ?  211 TRP B CZ3 1 
ATOM   3443 C  CH2 . TRP B 1 211 ? 2.18315   20.51367  0.64964   1.000 19.50183  ?  211 TRP B CH2 1 
ATOM   3444 N  N   . ALA B 1 212 ? -4.33988  20.11304  4.48320   1.000 11.05780  ?  212 ALA B N   1 
ATOM   3445 C  CA  . ALA B 1 212 ? -4.67509  21.04074  5.55733   1.000 12.48488  ?  212 ALA B CA  1 
ATOM   3446 C  C   . ALA B 1 212 ? -4.19980  20.54550  6.92197   1.000 14.21694  ?  212 ALA B C   1 
ATOM   3447 O  O   . ALA B 1 212 ? -4.10447  21.34455  7.85693   1.000 16.09918  ?  212 ALA B O   1 
ATOM   3448 C  CB  . ALA B 1 212 ? -6.18650  21.27910  5.59010   1.000 16.73414  ?  212 ALA B CB  1 
ATOM   3449 N  N   . GLU B 1 213 ? -3.91034  19.25091  7.05398   1.000 18.51031  ?  213 GLU B N   1 
ATOM   3450 C  CA  . GLU B 1 213 ? -3.34911  18.66468  8.26945   1.000 15.03576  ?  213 GLU B CA  1 
ATOM   3451 C  C   . GLU B 1 213 ? -2.02966  17.96498  7.96996   1.000 20.22526  ?  213 GLU B C   1 
ATOM   3452 O  O   . GLU B 1 213 ? -1.72040  16.91503  8.54446   1.000 18.83766  ?  213 GLU B O   1 
ATOM   3453 C  CB  . GLU B 1 213 ? -4.30339  17.66050  8.91463   1.000 20.89764  ?  213 GLU B CB  1 
ATOM   3454 C  CG  . GLU B 1 213 ? -5.74893  17.75192  8.54713   1.000 22.75023  ?  213 GLU B CG  1 
ATOM   3455 C  CD  . GLU B 1 213 ? -6.52388  16.55254  9.07202   1.000 26.22565  ?  213 GLU B CD  1 
ATOM   3456 O  OE1 . GLU B 1 213 ? -6.34295  16.18982  10.25054  1.000 38.83200  ?  213 GLU B OE1 1 
ATOM   3457 O  OE2 . GLU B 1 213 ? -7.30065  15.95678  8.30340   1.000 30.22409  -1 213 GLU B OE2 1 
ATOM   3458 N  N   . LYS B 1 214 ? -1.24460  18.53452  7.06000   1.000 15.69796  ?  214 LYS B N   1 
ATOM   3459 C  CA  . LYS B 1 214 ? -0.06119  17.86467  6.53506   1.000 11.47474  ?  214 LYS B CA  1 
ATOM   3460 C  C   . LYS B 1 214 ? 0.99046   17.62833  7.61750   1.000 14.92919  ?  214 LYS B C   1 
ATOM   3461 O  O   . LYS B 1 214 ? 1.16599   18.42607  8.54357   1.000 12.61087  ?  214 LYS B O   1 
ATOM   3462 C  CB  . LYS B 1 214 ? 0.54695   18.68825  5.39508   1.000 15.43041  ?  214 LYS B CB  1 
ATOM   3463 C  CG  . LYS B 1 214 ? 1.07404   20.07370  5.79226   1.000 13.60351  ?  214 LYS B CG  1 
ATOM   3464 C  CD  . LYS B 1 214 ? 1.47510   20.85378  4.51295   1.000 16.17261  ?  214 LYS B CD  1 
ATOM   3465 C  CE  . LYS B 1 214 ? 2.11896   22.20404  4.79824   1.000 19.97266  ?  214 LYS B CE  1 
ATOM   3466 N  NZ  . LYS B 1 214 ? 1.23909   23.05096  5.63703   1.000 23.89290  ?  214 LYS B NZ  1 
ATOM   3467 N  N   . TRP B 1 215 ? 1.68596   16.50012  7.48566   1.000 17.91916  ?  215 TRP B N   1 
ATOM   3468 C  CA  . TRP B 1 215 ? 2.82555   16.14060  8.32375   1.000 8.30109   ?  215 TRP B CA  1 
ATOM   3469 C  C   . TRP B 1 215 ? 4.13167   16.62416  7.70548   1.000 12.16950  ?  215 TRP B C   1 
ATOM   3470 O  O   . TRP B 1 215 ? 5.08476   15.86424  7.53844   1.000 11.59058  ?  215 TRP B O   1 
ATOM   3471 C  CB  . TRP B 1 215 ? 2.84397   14.62631  8.53172   1.000 9.01099   ?  215 TRP B CB  1 
ATOM   3472 C  CG  . TRP B 1 215 ? 1.80381   14.13769  9.48064   1.000 13.45077  ?  215 TRP B CG  1 
ATOM   3473 C  CD1 . TRP B 1 215 ? 0.45454   14.37730  9.43625   1.000 12.78792  ?  215 TRP B CD1 1 
ATOM   3474 C  CD2 . TRP B 1 215 ? 2.02837   13.30733  10.62505  1.000 9.13365   ?  215 TRP B CD2 1 
ATOM   3475 N  NE1 . TRP B 1 215 ? -0.17040  13.74371  10.49946  1.000 13.37018  ?  215 TRP B NE1 1 
ATOM   3476 C  CE2 . TRP B 1 215 ? 0.77827   13.08494  11.23927  1.000 14.36234  ?  215 TRP B CE2 1 
ATOM   3477 C  CE3 . TRP B 1 215 ? 3.17474   12.74144  11.19817  1.000 14.48119  ?  215 TRP B CE3 1 
ATOM   3478 C  CZ2 . TRP B 1 215 ? 0.64083   12.30827  12.40008  1.000 15.46571  ?  215 TRP B CZ2 1 
ATOM   3479 C  CZ3 . TRP B 1 215 ? 3.03231   11.96501  12.34525  1.000 12.29913  ?  215 TRP B CZ3 1 
ATOM   3480 C  CH2 . TRP B 1 215 ? 1.77687   11.76826  12.93550  1.000 13.03811  ?  215 TRP B CH2 1 
ATOM   3481 N  N   . TYR B 1 216 ? 4.19470   17.91506  7.37765   1.000 8.55529   ?  216 TYR B N   1 
ATOM   3482 C  CA  . TYR B 1 216 ? 5.31506   18.46260  6.62439   1.000 13.45660  ?  216 TYR B CA  1 
ATOM   3483 C  C   . TYR B 1 216 ? 5.39035   19.96273  6.89471   1.000 14.06263  ?  216 TYR B C   1 
ATOM   3484 O  O   . TYR B 1 216 ? 4.35857   20.63515  6.92149   1.000 19.83769  ?  216 TYR B O   1 
ATOM   3485 C  CB  . TYR B 1 216 ? 5.14006   18.19474  5.11654   1.000 14.67684  ?  216 TYR B CB  1 
ATOM   3486 C  CG  . TYR B 1 216 ? 6.28990   18.68341  4.25438   1.000 13.56794  ?  216 TYR B CG  1 
ATOM   3487 C  CD1 . TYR B 1 216 ? 6.33804   19.99027  3.80202   1.000 15.27008  ?  216 TYR B CD1 1 
ATOM   3488 C  CD2 . TYR B 1 216 ? 7.32168   17.83129  3.89003   1.000 12.09536  ?  216 TYR B CD2 1 
ATOM   3489 C  CE1 . TYR B 1 216 ? 7.39224   20.43631  3.02442   1.000 18.34619  ?  216 TYR B CE1 1 
ATOM   3490 C  CE2 . TYR B 1 216 ? 8.37192   18.26444  3.10860   1.000 12.00195  ?  216 TYR B CE2 1 
ATOM   3491 C  CZ  . TYR B 1 216 ? 8.39540   19.57310  2.66384   1.000 16.73881  ?  216 TYR B CZ  1 
ATOM   3492 O  OH  . TYR B 1 216 ? 9.44201   20.02042  1.88949   1.000 14.35774  ?  216 TYR B OH  1 
ATOM   3493 N  N   . GLY B 1 217 ? 6.59992   20.47400  7.11434   1.000 19.34083  ?  217 GLY B N   1 
ATOM   3494 C  CA  . GLY B 1 217 ? 6.80077   21.90378  7.28801   1.000 15.86379  ?  217 GLY B CA  1 
ATOM   3495 C  C   . GLY B 1 217 ? 7.17449   22.27320  8.71753   1.000 24.75839  ?  217 GLY B C   1 
ATOM   3496 O  O   . GLY B 1 217 ? 7.20449   21.44160  9.62524   1.000 13.20251  ?  217 GLY B O   1 
ATOM   3497 N  N   . ASP B 1 218 ? 7.45718   23.57019  8.90093   1.000 18.77357  ?  218 ASP B N   1 
ATOM   3498 C  CA  . ASP B 1 218 ? 7.94021   24.05881  10.19503  1.000 22.14013  ?  218 ASP B CA  1 
ATOM   3499 C  C   . ASP B 1 218 ? 6.89857   23.88550  11.29698  1.000 15.60591  ?  218 ASP B C   1 
ATOM   3500 O  O   . ASP B 1 218 ? 7.24547   23.58769  12.44357  1.000 15.34204  ?  218 ASP B O   1 
ATOM   3501 C  CB  . ASP B 1 218 ? 8.33214   25.53365  10.08891  1.000 27.22461  ?  218 ASP B CB  1 
ATOM   3502 C  CG  . ASP B 1 218 ? 9.62362   25.75480  9.32291   1.000 24.19165  ?  218 ASP B CG  1 
ATOM   3503 O  OD1 . ASP B 1 218 ? 10.28574  24.76909  8.93590   1.000 28.71889  ?  218 ASP B OD1 1 
ATOM   3504 O  OD2 . ASP B 1 218 ? 9.97586   26.93842  9.12004   1.000 34.95080  -1 218 ASP B OD2 1 
ATOM   3505 N  N   . GLU B 1 219 ? 5.62220   24.09841  10.98009  1.000 16.96871  ?  219 GLU B N   1 
ATOM   3506 C  CA  . GLU B 1 219 ? 4.58226   24.00974  12.00044  1.000 18.24303  ?  219 GLU B CA  1 
ATOM   3507 C  C   . GLU B 1 219 ? 4.39498   22.57387  12.46903  1.000 17.68088  ?  219 GLU B C   1 
ATOM   3508 O  O   . GLU B 1 219 ? 4.31086   22.30395  13.67737  1.000 13.19798  ?  219 GLU B O   1 
ATOM   3509 C  CB  . GLU B 1 219 ? 3.26799   24.55906  11.45088  1.000 16.14958  ?  219 GLU B CB  1 
ATOM   3510 C  CG  . GLU B 1 219 ? 2.13820   24.56863  12.46602  1.000 26.35424  ?  219 GLU B CG  1 
ATOM   3511 C  CD  . GLU B 1 219 ? 0.80183   24.96143  11.84209  1.000 33.34632  ?  219 GLU B CD  1 
ATOM   3512 O  OE1 . GLU B 1 219 ? 0.76995   25.24936  10.62295  1.000 33.54069  ?  219 GLU B OE1 1 
ATOM   3513 O  OE2 . GLU B 1 219 ? -0.21327  24.97533  12.56936  1.000 35.30266  -1 219 GLU B OE2 1 
ATOM   3514 N  N   . HIS B 1 220 ? 4.29490   21.63853  11.52498  1.000 13.56361  ?  220 HIS B N   1 
ATOM   3515 C  CA  . HIS B 1 220 ? 4.26748   20.23029  11.90584  1.000 15.63752  ?  220 HIS B CA  1 
ATOM   3516 C  C   . HIS B 1 220 ? 5.47650   19.86732  12.75860  1.000 12.54847  ?  220 HIS B C   1 
ATOM   3517 O  O   . HIS B 1 220 ? 5.32913   19.25831  13.82518  1.000 17.17915  ?  220 HIS B O   1 
ATOM   3518 C  CB  . HIS B 1 220 ? 4.21772   19.32201  10.67767  1.000 10.54482  ?  220 HIS B CB  1 
ATOM   3519 C  CG  . HIS B 1 220 ? 4.54306   17.90050  11.01099  1.000 9.88432   ?  220 HIS B CG  1 
ATOM   3520 N  ND1 . HIS B 1 220 ? 3.65484   17.07649  11.66588  1.000 9.11949   ?  220 HIS B ND1 1 
ATOM   3521 C  CD2 . HIS B 1 220 ? 5.68147   17.18308  10.85301  1.000 11.50093  ?  220 HIS B CD2 1 
ATOM   3522 C  CE1 . HIS B 1 220 ? 4.21769   15.89424  11.86122  1.000 10.94868  ?  220 HIS B CE1 1 
ATOM   3523 N  NE2 . HIS B 1 220 ? 5.45269   15.93571  11.39077  1.000 11.78797  ?  220 HIS B NE2 1 
ATOM   3524 N  N   . ASP B 1 221 ? 6.68803   20.20309  12.28903  1.000 12.48651  ?  221 ASP B N   1 
ATOM   3525 C  CA  . ASP B 1 221 ? 7.89052   19.83701  13.04017  1.000 12.36704  ?  221 ASP B CA  1 
ATOM   3526 C  C   . ASP B 1 221 ? 7.82980   20.37310  14.46650  1.000 17.05705  ?  221 ASP B C   1 
ATOM   3527 O  O   . ASP B 1 221 ? 8.13846   19.65473  15.42017  1.000 14.22389  ?  221 ASP B O   1 
ATOM   3528 C  CB  . ASP B 1 221 ? 9.15673   20.36046  12.34474  1.000 12.65664  ?  221 ASP B CB  1 
ATOM   3529 C  CG  . ASP B 1 221 ? 9.48186   19.64302  11.04099  1.000 13.20802  ?  221 ASP B CG  1 
ATOM   3530 O  OD1 . ASP B 1 221 ? 8.86850   18.60739  10.70187  1.000 14.04506  ?  221 ASP B OD1 1 
ATOM   3531 O  OD2 . ASP B 1 221 ? 10.38618  20.13097  10.34090  1.000 15.90476  -1 221 ASP B OD2 1 
ATOM   3532 N  N   . ALA B 1 222 ? 7.43321   21.63959  14.63362  1.000 14.60732  ?  222 ALA B N   1 
ATOM   3533 C  CA  . ALA B 1 222 ? 7.38795   22.22632  15.97162  1.000 21.81575  ?  222 ALA B CA  1 
ATOM   3534 C  C   . ALA B 1 222 ? 6.44147   21.45717  16.88353  1.000 16.38074  ?  222 ALA B C   1 
ATOM   3535 O  O   . ALA B 1 222 ? 6.73136   21.25251  18.06931  1.000 21.90086  ?  222 ALA B O   1 
ATOM   3536 C  CB  . ALA B 1 222 ? 6.96468   23.69257  15.88200  1.000 19.53575  ?  222 ALA B CB  1 
ATOM   3537 N  N   . ALA B 1 223 ? 5.29709   21.03413  16.34640  1.000 13.93965  ?  223 ALA B N   1 
ATOM   3538 C  CA  . ALA B 1 223 ? 4.32822   20.28662  17.14017  1.000 21.32154  ?  223 ALA B CA  1 
ATOM   3539 C  C   . ALA B 1 223 ? 4.86242   18.90512  17.49732  1.000 17.97622  ?  223 ALA B C   1 
ATOM   3540 O  O   . ALA B 1 223 ? 4.77645   18.47066  18.65094  1.000 14.91871  ?  223 ALA B O   1 
ATOM   3541 C  CB  . ALA B 1 223 ? 3.00838   20.17197  16.37155  1.000 20.60055  ?  223 ALA B CB  1 
ATOM   3542 N  N   . ALA B 1 224 ? 5.42160   18.19967  16.51847  1.000 15.73903  ?  224 ALA B N   1 
ATOM   3543 C  CA  . ALA B 1 224 ? 5.88838   16.84067  16.78172  1.000 12.47582  ?  224 ALA B CA  1 
ATOM   3544 C  C   . ALA B 1 224 ? 7.06074   16.84441  17.75461  1.000 11.98328  ?  224 ALA B C   1 
ATOM   3545 O  O   . ALA B 1 224 ? 7.16506   15.95888  18.61296  1.000 15.31270  ?  224 ALA B O   1 
ATOM   3546 C  CB  . ALA B 1 224 ? 6.27559   16.15719  15.47253  1.000 16.30081  ?  224 ALA B CB  1 
ATOM   3547 N  N   . LEU B 1 225 ? 7.95215   17.83109  17.63036  1.000 16.39057  ?  225 LEU B N   1 
ATOM   3548 C  CA  . LEU B 1 225 ? 9.10838   17.99386  18.50858  1.000 15.63262  ?  225 LEU B CA  1 
ATOM   3549 C  C   . LEU B 1 225 ? 8.77141   18.68201  19.82835  1.000 21.60969  ?  225 LEU B C   1 
ATOM   3550 O  O   . LEU B 1 225 ? 9.67060   18.83740  20.66826  1.000 21.10751  ?  225 LEU B O   1 
ATOM   3551 C  CB  . LEU B 1 225 ? 10.20395  18.79201  17.79669  1.000 12.45944  ?  225 LEU B CB  1 
ATOM   3552 C  CG  . LEU B 1 225 ? 10.71341  18.21707  16.47222  1.000 22.69852  ?  225 LEU B CG  1 
ATOM   3553 C  CD1 . LEU B 1 225 ? 11.74347  19.14447  15.81626  1.000 21.21974  ?  225 LEU B CD1 1 
ATOM   3554 C  CD2 . LEU B 1 225 ? 11.28579  16.81556  16.65967  1.000 19.74929  ?  225 LEU B CD2 1 
ATOM   3555 N  N   . GLU B 1 226 ? 7.50868   19.08353  20.02367  1.000 17.04755  ?  226 GLU B N   1 
ATOM   3556 C  CA  . GLU B 1 226 ? 7.03892   19.76267  21.24165  1.000 22.12489  ?  226 GLU B CA  1 
ATOM   3557 C  C   . GLU B 1 226 ? 7.82212   21.04554  21.51124  1.000 24.33917  ?  226 GLU B C   1 
ATOM   3558 O  O   . GLU B 1 226 ? 8.20172   21.33030  22.64789  1.000 31.83280  ?  226 GLU B O   1 
ATOM   3559 C  CB  . GLU B 1 226 ? 7.08761   18.83446  22.45874  1.000 24.42541  ?  226 GLU B CB  1 
ATOM   3560 C  CG  . GLU B 1 226 ? 6.23507   17.58545  22.32325  1.000 25.57845  ?  226 GLU B CG  1 
ATOM   3561 C  CD  . GLU B 1 226 ? 6.59470   16.53724  23.36054  1.000 39.76169  ?  226 GLU B CD  1 
ATOM   3562 O  OE1 . GLU B 1 226 ? 6.40210   16.81370  24.56185  1.000 37.98261  ?  226 GLU B OE1 1 
ATOM   3563 O  OE2 . GLU B 1 226 ? 7.08898   15.44976  22.97274  1.000 40.50282  -1 226 GLU B OE2 1 
ATOM   3564 N  N   . GLU B 1 227 ? 8.05044   21.83828  20.46276  1.000 25.79105  ?  227 GLU B N   1 
ATOM   3565 C  CA  . GLU B 1 227 ? 8.86057   23.05002  20.58487  1.000 28.21642  ?  227 GLU B CA  1 
ATOM   3566 C  C   . GLU B 1 227 ? 8.01278   24.30694  20.75013  1.000 30.23851  ?  227 GLU B C   1 
ATOM   3567 O  O   . GLU B 1 227 ? 6.90467   24.39393  20.22162  1.000 43.79507  ?  227 GLU B O   1 
ATOM   3568 C  CB  . GLU B 1 227 ? 9.77813   23.19386  19.37272  1.000 24.50014  ?  227 GLU B CB  1 
ATOM   3569 C  CG  . GLU B 1 227 ? 10.93595  22.21172  19.38195  1.000 31.58836  ?  227 GLU B CG  1 
ATOM   3570 C  CD  . GLU B 1 227 ? 11.69901  22.20314  18.07574  1.000 34.08078  ?  227 GLU B CD  1 
ATOM   3571 O  OE1 . GLU B 1 227 ? 11.21524  22.83343  17.10623  1.000 35.74795  ?  227 GLU B OE1 1 
ATOM   3572 O  OE2 . GLU B 1 227 ? 12.77965  21.56609  18.01761  1.000 33.92537  -1 227 GLU B OE2 1 
HETATM 3573 MN MN  . MN  C 2 .   ? 13.90281  -0.65802  34.69950  1.000 9.89404   ?  301 MN  A MN  1 
HETATM 3574 C  C1  . AKG D 3 .   ? 15.51546  -0.11647  33.23150  1.000 17.00355  ?  302 AKG A C1  1 
HETATM 3575 O  O1  . AKG D 3 .   ? 16.44376  0.02270   32.40021  1.000 12.14009  ?  302 AKG A O1  1 
HETATM 3576 O  O2  . AKG D 3 .   ? 14.71597  -1.03329  33.37253  1.000 17.34513  ?  302 AKG A O2  1 
HETATM 3577 C  C2  . AKG D 3 .   ? 15.57226  1.22345   34.00613  1.000 6.74041   ?  302 AKG A C2  1 
HETATM 3578 O  O5  . AKG D 3 .   ? 14.70783  1.34706   34.83344  1.000 11.71337  ?  302 AKG A O5  1 
HETATM 3579 C  C3  . AKG D 3 .   ? 16.65588  2.18566   33.65320  1.000 9.47598   ?  302 AKG A C3  1 
HETATM 3580 C  C4  . AKG D 3 .   ? 16.93100  3.23018   34.73675  1.000 11.39587  ?  302 AKG A C4  1 
HETATM 3581 C  C5  . AKG D 3 .   ? 17.75519  4.54165   34.57113  1.000 11.10246  ?  302 AKG A C5  1 
HETATM 3582 O  O3  . AKG D 3 .   ? 17.75067  5.32385   35.53983  1.000 6.15483   ?  302 AKG A O3  1 
HETATM 3583 O  O4  . AKG D 3 .   ? 18.39300  4.77066   33.50290  1.000 7.35188   ?  302 AKG A O4  1 
HETATM 3584 N  N1  . 6HN E 4 .   ? 16.98341  -7.20555  34.55149  1.000 20.48245  ?  303 6HN A N1  1 
HETATM 3585 N  N   . 6HN E 4 .   ? 15.40797  -2.94383  31.16214  1.000 12.65468  ?  303 6HN A N   1 
HETATM 3586 C  CA  . 6HN E 4 .   ? 16.85495  -3.08039  31.13536  1.000 13.21040  ?  303 6HN A CA  1 
HETATM 3587 C  C   . 6HN E 4 .   ? 17.29005  -3.59355  29.76364  1.000 13.39438  ?  303 6HN A C   1 
HETATM 3588 O  OXT . 6HN E 4 .   ? 18.42894  -3.29299  29.32750  1.000 16.06194  ?  303 6HN A OXT 1 
HETATM 3589 O  O   . 6HN E 4 .   ? 16.52464  -4.31084  29.06192  1.000 13.70267  ?  303 6HN A O   1 
HETATM 3590 C  CB  . 6HN E 4 .   ? 17.33433  -4.05613  32.22307  1.000 9.62116   ?  303 6HN A CB  1 
HETATM 3591 C  CG  . 6HN E 4 .   ? 17.05325  -3.60441  33.66946  1.000 13.37673  ?  303 6HN A CG  1 
HETATM 3592 C  CD  . 6HN E 4 .   ? 17.43461  -4.71608  34.68689  1.000 10.68078  ?  303 6HN A CD  1 
HETATM 3593 C  CE  . 6HN E 4 .   ? 16.45890  -5.86027  34.74665  1.000 15.80052  ?  303 6HN A CE  1 
HETATM 3594 O  O2  . 6HN E 4 .   ? 18.12277  -7.47762  34.80027  1.000 12.43956  ?  303 6HN A O2  1 
HETATM 3595 O  O1  . 6HN E 4 .   ? 16.13942  -8.17343  34.03793  1.000 18.64306  ?  303 6HN A O1  1 
HETATM 3596 I  I   . IOD F 5 .   ? 28.81701  -20.68273 45.95646  1.000 54.75911  ?  304 IOD A I   1 
HETATM 3597 I  I   . IOD G 5 .   ? 17.32425  17.51826  21.85201  1.000 67.66911  ?  305 IOD A I   1 
HETATM 3598 I  I   . IOD H 5 .   ? 15.16894  0.58850   22.13425  1.000 27.43055  ?  306 IOD A I   1 
HETATM 3599 N  N1  . 6HN I 4 .   ? 27.92461  -24.53163 42.15023  1.000 48.07242  ?  307 6HN A N1  1 
HETATM 3600 N  N   . 6HN I 4 .   ? 26.71876  -21.43560 38.49460  1.000 29.53938  ?  307 6HN A N   1 
HETATM 3601 C  CA  . 6HN I 4 .   ? 25.60486  -22.17579 39.12079  1.000 25.02752  ?  307 6HN A CA  1 
HETATM 3602 C  C   . 6HN I 4 .   ? 24.39193  -22.34467 38.20089  1.000 13.59413  ?  307 6HN A C   1 
HETATM 3603 O  OXT . 6HN I 4 .   ? 23.27668  -22.45832 38.68491  1.000 17.80847  ?  307 6HN A OXT 1 
HETATM 3604 O  O   . 6HN I 4 .   ? 24.56713  -22.40368 36.96932  1.000 46.85824  ?  307 6HN A O   1 
HETATM 3605 C  CB  . 6HN I 4 .   ? 25.29428  -21.65730 40.53418  1.000 29.31031  ?  307 6HN A CB  1 
HETATM 3606 C  CG  . 6HN I 4 .   ? 26.44024  -21.15680 41.34020  1.000 23.54397  ?  307 6HN A CG  1 
HETATM 3607 C  CD  . 6HN I 4 .   ? 27.47897  -22.23841 41.63403  1.000 42.88603  ?  307 6HN A CD  1 
HETATM 3608 C  CE  . 6HN I 4 .   ? 26.87452  -23.63198 41.77651  1.000 31.36297  ?  307 6HN A CE  1 
HETATM 3609 O  O2  . 6HN I 4 .   ? 28.14433  -24.64626 43.30288  1.000 19.83105  ?  307 6HN A O2  1 
HETATM 3610 O  O1  . 6HN I 4 .   ? 28.64904  -25.17010 41.16225  1.000 36.43951  ?  307 6HN A O1  1 
HETATM 3611 MN MN  . MN  J 2 .   ? 2.42700   1.81900   11.77695  1.000 11.28453  ?  301 MN  B MN  1 
HETATM 3612 C  C1  . AKG K 3 .   ? 5.19298   1.02532   11.16649  1.000 18.24266  ?  302 AKG B C1  1 
HETATM 3613 O  O1  . AKG K 3 .   ? 6.42735   0.91900   10.98694  1.000 11.80317  ?  302 AKG B O1  1 
HETATM 3614 O  O2  . AKG K 3 .   ? 4.52241   1.95438   11.66078  1.000 16.87433  ?  302 AKG B O2  1 
HETATM 3615 C  C2  . AKG K 3 .   ? 4.37843   -0.18953  10.68980  1.000 14.24456  ?  302 AKG B C2  1 
HETATM 3616 O  O5  . AKG K 3 .   ? 3.17514   -0.16107  10.83095  1.000 10.66568  ?  302 AKG B O5  1 
HETATM 3617 C  C3  . AKG K 3 .   ? 5.12224   -1.33403  10.07382  1.000 9.37557   ?  302 AKG B C3  1 
HETATM 3618 C  C4  . AKG K 3 .   ? 4.28060   -2.13995  9.11301   1.000 12.52104  ?  302 AKG B C4  1 
HETATM 3619 C  C5  . AKG K 3 .   ? 4.90578   -3.44751  8.63309   1.000 8.49410   ?  302 AKG B C5  1 
HETATM 3620 O  O3  . AKG K 3 .   ? 6.12254   -3.64883  8.78829   1.000 9.29557   ?  302 AKG B O3  1 
HETATM 3621 O  O4  . AKG K 3 .   ? 4.07746   -4.22275  8.08826   1.000 10.56387  ?  302 AKG B O4  1 
HETATM 3622 N  N1  . 6HN L 4 .   ? 4.29469   8.27651   9.34691   1.000 18.60033  ?  303 6HN B N1  1 
HETATM 3623 N  N   . 6HN L 4 .   ? 6.12557   4.11733   12.62539  1.000 11.71859  ?  303 6HN B N   1 
HETATM 3624 C  CA  . 6HN L 4 .   ? 7.02147   4.20851   11.49022  1.000 10.98077  ?  303 6HN B CA  1 
HETATM 3625 C  C   . 6HN L 4 .   ? 8.37446   4.74108   11.93250  1.000 16.02517  ?  303 6HN B C   1 
HETATM 3626 O  OXT . 6HN L 4 .   ? 9.40452   4.40771   11.30149  1.000 19.05527  ?  303 6HN B OXT 1 
HETATM 3627 O  O   . 6HN L 4 .   ? 8.47227   5.51893   12.92399  1.000 14.58192  ?  303 6HN B O   1 
HETATM 3628 C  CB  . 6HN L 4 .   ? 6.44618   5.18529   10.46088  1.000 12.81791  ?  303 6HN B CB  1 
HETATM 3629 C  CG  . 6HN L 4 .   ? 5.12255   4.70347   9.84625   1.000 14.09118  ?  303 6HN B CG  1 
HETATM 3630 C  CD  . 6HN L 4 .   ? 4.55941   5.83069   8.97105   1.000 13.81059  ?  303 6HN B CD  1 
HETATM 3631 C  CE  . 6HN L 4 .   ? 3.99829   6.93154   9.80590   1.000 15.25006  ?  303 6HN B CE  1 
HETATM 3632 O  O2  . 6HN L 4 .   ? 4.78632   8.47457   8.27630   1.000 12.53692  ?  303 6HN B O2  1 
HETATM 3633 O  O1  . 6HN L 4 .   ? 3.98570   9.31109   10.19506  1.000 18.38624  ?  303 6HN B O1  1 
HETATM 3634 I  I   . IOD M 5 .   ? 13.22498  0.62689   18.26758  1.000 24.56405  ?  304 IOD B I   1 
HETATM 3635 I  I   . IOD N 5 .   ? -12.82225 -8.90440  9.28468   1.000 71.99418  ?  305 IOD B I   1 
HETATM 3636 I  I   . IOD O 5 .   ? 14.91813  -16.23150 16.69475  1.000 84.02688  ?  306 IOD B I   1 
HETATM 3637 I  I   . IOD P 5 .   ? -3.96936  7.88992   -9.80469  1.000 105.50796 ?  307 IOD B I   1 
HETATM 3638 C  C1  . EDO Q 6 .   ? -3.85041  -12.33056 4.21299   1.000 34.72635  ?  308 EDO B C1  1 
HETATM 3639 O  O1  . EDO Q 6 .   ? -2.68821  -12.04816 4.94175   1.000 33.47491  ?  308 EDO B O1  1 
HETATM 3640 C  C2  . EDO Q 6 .   ? -4.13744  -11.23126 3.23242   1.000 52.01717  ?  308 EDO B C2  1 
HETATM 3641 O  O2  . EDO Q 6 .   ? -5.48296  -10.83688 3.37614   1.000 55.92820  ?  308 EDO B O2  1 
HETATM 3642 C  C1  . GOL R 7 .   ? -6.91860  -12.30877 0.31703   1.000 80.83604  ?  309 GOL B C1  1 
HETATM 3643 O  O1  . GOL R 7 .   ? -5.78253  -11.50132 0.06988   1.000 71.11919  ?  309 GOL B O1  1 
HETATM 3644 C  C2  . GOL R 7 .   ? -6.98407  -12.73952 1.77921   1.000 82.79426  ?  309 GOL B C2  1 
HETATM 3645 O  O2  . GOL R 7 .   ? -8.33503  -12.69535 2.22271   1.000 77.48932  ?  309 GOL B O2  1 
HETATM 3646 C  C3  . GOL R 7 .   ? -6.35328  -14.10085 2.10825   1.000 75.12233  ?  309 GOL B C3  1 
HETATM 3647 O  O3  . GOL R 7 .   ? -4.93949  -14.08411 1.96869   1.000 67.52107  ?  309 GOL B O3  1 
HETATM 3648 C  C1  . GOL S 7 .   ? 4.10498   23.70020  1.05723   1.000 57.65964  ?  310 GOL B C1  1 
HETATM 3649 O  O1  . GOL S 7 .   ? 3.72271   23.33937  -0.25554  1.000 61.56658  ?  310 GOL B O1  1 
HETATM 3650 C  C2  . GOL S 7 .   ? 4.71022   22.49804  1.71997   1.000 64.20178  ?  310 GOL B C2  1 
HETATM 3651 O  O2  . GOL S 7 .   ? 5.25600   22.88924  2.95413   1.000 70.87911  ?  310 GOL B O2  1 
HETATM 3652 C  C3  . GOL S 7 .   ? 5.69579   21.86618  0.75360   1.000 69.09669  ?  310 GOL B C3  1 
HETATM 3653 O  O3  . GOL S 7 .   ? 6.94979   22.49678  0.89420   1.000 74.16618  ?  310 GOL B O3  1 
HETATM 3654 O  O   . HOH T 8 .   ? 19.80120  -21.17101 27.16989  1.000 34.70817  ?  401 HOH A O   1 
HETATM 3655 O  O   . HOH T 8 .   ? 29.04567  11.53839  24.62758  1.000 30.29482  ?  402 HOH A O   1 
HETATM 3656 O  O   . HOH T 8 .   ? 15.87781  -0.98357  36.01524  1.000 17.77695  ?  403 HOH A O   1 
HETATM 3657 O  O   . HOH T 8 .   ? 31.57809  6.23561   25.33610  1.000 33.58204  ?  404 HOH A O   1 
HETATM 3658 O  O   . HOH T 8 .   ? 14.59163  2.59628   53.22532  1.000 29.10665  ?  405 HOH A O   1 
HETATM 3659 O  O   . HOH T 8 .   ? 18.42262  -19.61255 22.96996  1.000 39.66174  ?  406 HOH A O   1 
HETATM 3660 O  O   . HOH T 8 .   ? 33.87574  8.89512   25.54646  1.000 45.77080  ?  407 HOH A O   1 
HETATM 3661 O  O   . HOH T 8 .   ? 24.524    -15.638   58.775    1.000 39.42011  ?  408 HOH A O   1 
HETATM 3662 O  O   . HOH T 8 .   ? 29.99985  -0.92476  50.47974  1.000 16.67191  ?  409 HOH A O   1 
HETATM 3663 O  O   . HOH T 8 .   ? 33.86925  -8.68956  22.04331  1.000 32.31836  ?  410 HOH A O   1 
HETATM 3664 O  O   . HOH T 8 .   ? 34.86426  7.02848   31.42627  1.000 35.18355  ?  411 HOH A O   1 
HETATM 3665 O  O   . HOH T 8 .   ? 22.16186  -22.32757 36.39160  1.000 31.75151  ?  412 HOH A O   1 
HETATM 3666 O  O   . HOH T 8 .   ? 12.48931  -12.84327 44.08549  1.000 14.15585  ?  413 HOH A O   1 
HETATM 3667 O  O   . HOH T 8 .   ? 24.59435  -22.56642 44.09978  1.000 28.02933  ?  414 HOH A O   1 
HETATM 3668 O  O   . HOH T 8 .   ? 7.89343   -0.34191  52.11140  1.000 41.67983  ?  415 HOH A O   1 
HETATM 3669 O  O   . HOH T 8 .   ? 39.10744  6.30283   30.23713  1.000 33.31071  ?  416 HOH A O   1 
HETATM 3670 O  O   . HOH T 8 .   ? 1.53583   -0.92936  44.78910  1.000 26.50941  ?  417 HOH A O   1 
HETATM 3671 O  O   . HOH T 8 .   ? 12.424    14.597    44.113    1.000 26.46524  ?  418 HOH A O   1 
HETATM 3672 O  O   . HOH T 8 .   ? 29.67751  21.30390  24.94940  1.000 36.99091  ?  419 HOH A O   1 
HETATM 3673 O  O   . HOH T 8 .   ? 30.82371  -5.74467  49.83065  1.000 30.19007  ?  420 HOH A O   1 
HETATM 3674 O  O   . HOH T 8 .   ? 10.75803  -11.76845 18.95155  1.000 32.53524  ?  421 HOH A O   1 
HETATM 3675 O  O   . HOH T 8 .   ? 13.89683  -7.40916  32.95152  1.000 16.82130  ?  422 HOH A O   1 
HETATM 3676 O  O   . HOH T 8 .   ? 29.37762  13.27088  37.78222  1.000 28.43553  ?  423 HOH A O   1 
HETATM 3677 O  O   . HOH T 8 .   ? 8.76568   -13.80668 23.55366  1.000 39.97671  ?  424 HOH A O   1 
HETATM 3678 O  O   . HOH T 8 .   ? 28.42272  -4.29811  17.82348  1.000 32.04775  ?  425 HOH A O   1 
HETATM 3679 O  O   . HOH T 8 .   ? 4.95783   -4.89321  46.98521  1.000 21.99874  ?  426 HOH A O   1 
HETATM 3680 O  O   . HOH T 8 .   ? 12.63145  -16.49534 35.09574  1.000 15.38770  ?  427 HOH A O   1 
HETATM 3681 O  O   . HOH T 8 .   ? 12.79532  -3.23585  20.07330  1.000 18.38486  ?  428 HOH A O   1 
HETATM 3682 O  O   . HOH T 8 .   ? 35.18863  -1.73630  43.52092  1.000 14.59674  ?  429 HOH A O   1 
HETATM 3683 O  O   . HOH T 8 .   ? 20.29692  -2.07254  27.72361  1.000 12.06747  ?  430 HOH A O   1 
HETATM 3684 O  O   . HOH T 8 .   ? 32.29211  7.59212   34.19529  1.000 11.64804  ?  431 HOH A O   1 
HETATM 3685 O  O   . HOH T 8 .   ? 17.36825  -21.24681 35.23739  1.000 14.46830  ?  432 HOH A O   1 
HETATM 3686 O  O   . HOH T 8 .   ? 17.77100  -2.28763  55.89765  1.000 34.45741  ?  433 HOH A O   1 
HETATM 3687 O  O   . HOH T 8 .   ? 1.41847   7.02216   40.49897  1.000 11.39022  ?  434 HOH A O   1 
HETATM 3688 O  O   . HOH T 8 .   ? 37.51305  -5.15301  44.14797  1.000 37.71574  ?  435 HOH A O   1 
HETATM 3689 O  O   . HOH T 8 .   ? 20.58996  -3.90461  56.78943  1.000 37.83830  ?  436 HOH A O   1 
HETATM 3690 O  O   . HOH T 8 .   ? 28.80731  -8.58541  53.57360  1.000 38.00480  ?  437 HOH A O   1 
HETATM 3691 O  O   . HOH T 8 .   ? 11.92093  7.73210   25.75890  1.000 22.99984  ?  438 HOH A O   1 
HETATM 3692 O  O   . HOH T 8 .   ? 16.10124  -21.56737 37.92670  1.000 23.46237  ?  439 HOH A O   1 
HETATM 3693 O  O   . HOH T 8 .   ? 38.86932  -2.93181  28.55308  1.000 32.21462  ?  440 HOH A O   1 
HETATM 3694 O  O   . HOH T 8 .   ? 34.61228  -1.54167  31.08129  1.000 15.44169  ?  441 HOH A O   1 
HETATM 3695 O  O   . HOH T 8 .   ? 3.89102   0.86064   30.01513  1.000 29.85068  ?  442 HOH A O   1 
HETATM 3696 O  O   . HOH T 8 .   ? 18.84198  20.59370  27.04529  1.000 28.61688  ?  443 HOH A O   1 
HETATM 3697 O  O   . HOH T 8 .   ? 25.19358  -2.20528  16.86865  1.000 25.50865  ?  444 HOH A O   1 
HETATM 3698 O  O   . HOH T 8 .   ? 15.63058  -10.59041 26.18318  1.000 10.74609  ?  445 HOH A O   1 
HETATM 3699 O  O   . HOH T 8 .   ? 24.36282  21.12142  18.63941  1.000 30.50685  ?  446 HOH A O   1 
HETATM 3700 O  O   . HOH T 8 .   ? 33.18763  -16.78874 40.26932  1.000 25.98704  ?  447 HOH A O   1 
HETATM 3701 O  O   . HOH T 8 .   ? 16.43283  0.34416   29.20396  1.000 10.48561  ?  448 HOH A O   1 
HETATM 3702 O  O   . HOH T 8 .   ? 1.05424   3.31048   34.55689  1.000 32.41880  ?  449 HOH A O   1 
HETATM 3703 O  O   . HOH T 8 .   ? 20.08153  15.54231  34.30090  1.000 13.52466  ?  450 HOH A O   1 
HETATM 3704 O  O   . HOH T 8 .   ? 22.28341  -11.42509 18.90912  1.000 19.07901  ?  451 HOH A O   1 
HETATM 3705 O  O   . HOH T 8 .   ? 40.11706  7.27720   38.13209  1.000 17.20873  ?  452 HOH A O   1 
HETATM 3706 O  O   . HOH T 8 .   ? 16.19542  5.64666   37.65600  1.000 9.24906   ?  453 HOH A O   1 
HETATM 3707 O  O   . HOH T 8 .   ? 16.54043  -18.60164 47.17587  1.000 13.50602  ?  454 HOH A O   1 
HETATM 3708 O  O   . HOH T 8 .   ? 13.99781  7.54631   28.63237  1.000 8.37401   ?  455 HOH A O   1 
HETATM 3709 O  O   . HOH T 8 .   ? 33.53634  -2.66220  33.57807  1.000 9.60019   ?  456 HOH A O   1 
HETATM 3710 O  O   . HOH T 8 .   ? 19.81223  11.44069  36.17715  1.000 9.69509   ?  457 HOH A O   1 
HETATM 3711 O  O   . HOH T 8 .   ? 19.07187  -14.01934 31.40551  1.000 36.00677  ?  458 HOH A O   1 
HETATM 3712 O  O   . HOH T 8 .   ? 18.97390  3.49448   31.24235  1.000 8.95418   ?  459 HOH A O   1 
HETATM 3713 O  O   . HOH T 8 .   ? 27.16419  18.16215  18.82865  1.000 23.39754  ?  460 HOH A O   1 
HETATM 3714 O  O   . HOH T 8 .   ? 12.40740  -11.77897 41.37917  1.000 10.50832  ?  461 HOH A O   1 
HETATM 3715 O  O   . HOH T 8 .   ? 23.92420  -16.49591 21.78767  1.000 25.65644  ?  462 HOH A O   1 
HETATM 3716 O  O   . HOH T 8 .   ? 26.73485  -16.25746 23.85383  1.000 25.59265  ?  463 HOH A O   1 
HETATM 3717 O  O   . HOH T 8 .   ? 21.88297  -14.78851 31.85088  1.000 11.71876  ?  464 HOH A O   1 
HETATM 3718 O  O   . HOH T 8 .   ? 11.61397  -22.86055 31.80315  1.000 18.94725  ?  465 HOH A O   1 
HETATM 3719 O  O   . HOH T 8 .   ? 9.07095   -8.18106  48.11915  1.000 23.52488  ?  466 HOH A O   1 
HETATM 3720 O  O   . HOH T 8 .   ? 25.18197  12.22887  47.19516  1.000 27.08286  ?  467 HOH A O   1 
HETATM 3721 O  O   . HOH T 8 .   ? 29.99442  -11.93327 33.64483  1.000 7.97003   ?  468 HOH A O   1 
HETATM 3722 O  O   . HOH T 8 .   ? 15.59507  16.10833  17.61517  1.000 13.09703  ?  469 HOH A O   1 
HETATM 3723 O  O   . HOH T 8 .   ? 30.34138  18.26444  25.37851  1.000 26.12965  ?  470 HOH A O   1 
HETATM 3724 O  O   . HOH T 8 .   ? 21.84328  -17.02960 28.37625  1.000 11.53897  ?  471 HOH A O   1 
HETATM 3725 O  O   . HOH T 8 .   ? 17.39319  9.91097   37.58137  1.000 9.22496   ?  472 HOH A O   1 
HETATM 3726 O  O   . HOH T 8 .   ? 28.57223  -5.67118  26.08763  1.000 13.39534  ?  473 HOH A O   1 
HETATM 3727 O  O   . HOH T 8 .   ? 9.43260   -1.11742  39.14085  1.000 10.62118  ?  474 HOH A O   1 
HETATM 3728 O  O   . HOH T 8 .   ? 32.67036  2.21410   23.51266  1.000 32.15283  ?  475 HOH A O   1 
HETATM 3729 O  O   . HOH T 8 .   ? 33.99147  6.97997   25.58805  1.000 39.23635  ?  476 HOH A O   1 
HETATM 3730 O  O   . HOH T 8 .   ? 20.31023  4.75116   25.62628  1.000 6.03774   ?  477 HOH A O   1 
HETATM 3731 O  O   . HOH T 8 .   ? 7.53565   -18.27553 29.50798  1.000 31.17312  ?  478 HOH A O   1 
HETATM 3732 O  O   . HOH T 8 .   ? 26.27922  -13.44005 32.96149  1.000 11.72277  ?  479 HOH A O   1 
HETATM 3733 O  O   . HOH T 8 .   ? 9.08819   -6.74870  45.78708  1.000 13.45309  ?  480 HOH A O   1 
HETATM 3734 O  O   . HOH T 8 .   ? 19.17091  1.61123   14.79972  1.000 9.70177   ?  481 HOH A O   1 
HETATM 3735 O  O   . HOH T 8 .   ? 26.18526  -21.51826 34.34724  1.000 22.32420  ?  482 HOH A O   1 
HETATM 3736 O  O   . HOH T 8 .   ? 39.69460  -2.90380  37.00968  1.000 40.57593  ?  483 HOH A O   1 
HETATM 3737 O  O   . HOH T 8 .   ? 21.59336  4.02297   30.46040  1.000 8.47570   ?  484 HOH A O   1 
HETATM 3738 O  O   . HOH T 8 .   ? 13.02957  15.46822  32.61121  1.000 21.08612  ?  485 HOH A O   1 
HETATM 3739 O  O   . HOH T 8 .   ? 27.17888  -13.81521 26.64265  1.000 21.00312  ?  486 HOH A O   1 
HETATM 3740 O  O   . HOH T 8 .   ? -2.33095  0.76079   41.78210  1.000 24.83880  ?  487 HOH A O   1 
HETATM 3741 O  O   . HOH T 8 .   ? 5.73254   -0.94950  48.00099  1.000 31.74393  ?  488 HOH A O   1 
HETATM 3742 O  O   . HOH T 8 .   ? 12.10948  -7.70477  21.83988  1.000 28.41063  ?  489 HOH A O   1 
HETATM 3743 O  O   . HOH T 8 .   ? 6.23050   7.47655   30.09614  1.000 29.53192  ?  490 HOH A O   1 
HETATM 3744 O  O   . HOH T 8 .   ? 30.38130  8.55985   41.44049  1.000 21.98161  ?  491 HOH A O   1 
HETATM 3745 O  O   . HOH T 8 .   ? 14.02347  14.55336  28.89710  1.000 11.63691  ?  492 HOH A O   1 
HETATM 3746 O  O   . HOH T 8 .   ? 14.35267  -19.57940 37.61206  1.000 22.87280  ?  493 HOH A O   1 
HETATM 3747 O  O   . HOH T 8 .   ? 19.78872  15.92202  23.39970  1.000 8.72589   ?  494 HOH A O   1 
HETATM 3748 O  O   . HOH T 8 .   ? 19.37328  -1.30241  30.93454  1.000 14.65695  ?  495 HOH A O   1 
HETATM 3749 O  O   . HOH T 8 .   ? 2.39851   13.58144  39.18512  1.000 35.75041  ?  496 HOH A O   1 
HETATM 3750 O  O   . HOH T 8 .   ? 9.28121   -13.26211 26.32666  1.000 16.37727  ?  497 HOH A O   1 
HETATM 3751 O  O   . HOH T 8 .   ? 28.486    -4.680    20.928    1.000 29.04284  ?  498 HOH A O   1 
HETATM 3752 O  O   . HOH T 8 .   ? 26.03124  -8.29427  20.89509  1.000 31.20438  ?  499 HOH A O   1 
HETATM 3753 O  O   . HOH T 8 .   ? 23.79748  -22.91187 34.38784  1.000 37.17882  ?  500 HOH A O   1 
HETATM 3754 O  O   . HOH T 8 .   ? 30.92572  -5.87918  39.29164  1.000 12.68924  ?  501 HOH A O   1 
HETATM 3755 O  O   . HOH T 8 .   ? -5.08909  1.55678   34.86436  1.000 12.27893  ?  502 HOH A O   1 
HETATM 3756 O  O   . HOH T 8 .   ? 31.98287  -11.67292 48.44330  1.000 27.46946  ?  503 HOH A O   1 
HETATM 3757 O  O   . HOH T 8 .   ? 8.96918   5.23907   50.44328  1.000 25.49505  ?  504 HOH A O   1 
HETATM 3758 O  O   . HOH T 8 .   ? 14.41007  8.31834   50.03763  1.000 16.64119  ?  505 HOH A O   1 
HETATM 3759 O  O   . HOH T 8 .   ? 24.890    -13.684   60.750    1.000 34.01693  ?  506 HOH A O   1 
HETATM 3760 O  O   . HOH T 8 .   ? -2.88367  3.34794   33.04178  1.000 25.21341  ?  507 HOH A O   1 
HETATM 3761 O  O   . HOH T 8 .   ? 11.99672  -17.30056 52.35843  1.000 35.35725  ?  508 HOH A O   1 
HETATM 3762 O  O   . HOH T 8 .   ? 10.86833  -15.01085 22.16107  1.000 28.25586  ?  509 HOH A O   1 
HETATM 3763 O  O   . HOH T 8 .   ? 16.04852  -5.37403  20.90663  1.000 11.51540  ?  510 HOH A O   1 
HETATM 3764 O  O   . HOH T 8 .   ? 15.24080  -2.40100  21.33334  1.000 43.70199  ?  511 HOH A O   1 
HETATM 3765 O  O   . HOH T 8 .   ? 26.81989  16.04809  36.67537  1.000 22.23330  ?  512 HOH A O   1 
HETATM 3766 O  O   . HOH T 8 .   ? 6.75624   -9.82616  46.70097  1.000 26.61856  ?  513 HOH A O   1 
HETATM 3767 O  O   . HOH T 8 .   ? 37.36663  -7.23368  29.52631  1.000 25.37569  ?  514 HOH A O   1 
HETATM 3768 O  O   . HOH T 8 .   ? 29.35489  -18.10557 56.40535  1.000 26.51844  ?  515 HOH A O   1 
HETATM 3769 O  O   . HOH T 8 .   ? 26.84984  4.12285   18.42865  1.000 20.06763  ?  516 HOH A O   1 
HETATM 3770 O  O   . HOH T 8 .   ? 34.38730  10.00570  28.81372  1.000 31.37406  ?  517 HOH A O   1 
HETATM 3771 O  O   . HOH T 8 .   ? 8.75579   -7.10037  39.00481  1.000 9.67846   ?  518 HOH A O   1 
HETATM 3772 O  O   . HOH T 8 .   ? 32.17110  -15.35435 35.23352  1.000 23.87542  ?  519 HOH A O   1 
HETATM 3773 O  O   . HOH T 8 .   ? 21.204    -11.383   60.772    1.000 32.29336  ?  520 HOH A O   1 
HETATM 3774 O  O   . HOH T 8 .   ? 0.87453   11.85078  33.18742  1.000 37.12475  ?  521 HOH A O   1 
HETATM 3775 O  O   . HOH T 8 .   ? 23.272    -11.764   61.405    1.000 39.11696  ?  522 HOH A O   1 
HETATM 3776 O  O   . HOH T 8 .   ? 8.93128   -10.93656 40.21933  1.000 22.16502  ?  523 HOH A O   1 
HETATM 3777 O  O   . HOH T 8 .   ? 27.618    -18.840   53.889    1.000 21.75258  ?  524 HOH A O   1 
HETATM 3778 O  O   . HOH T 8 .   ? 28.06289  22.65656  28.93883  1.000 31.47759  ?  525 HOH A O   1 
HETATM 3779 O  O   . HOH T 8 .   ? 12.55596  -20.63877 39.38089  1.000 32.83685  ?  526 HOH A O   1 
HETATM 3780 O  O   . HOH T 8 .   ? 28.50744  -19.75354 30.42489  1.000 38.69411  ?  527 HOH A O   1 
HETATM 3781 O  O   . HOH T 8 .   ? 28.18004  -13.38818 35.03447  1.000 7.36339   ?  528 HOH A O   1 
HETATM 3782 O  O   . HOH T 8 .   ? 31.39777  3.56489   26.27356  1.000 17.07230  ?  529 HOH A O   1 
HETATM 3783 O  O   . HOH T 8 .   ? 25.27878  14.63046  38.81727  1.000 8.93934   ?  530 HOH A O   1 
HETATM 3784 O  O   . HOH T 8 .   ? 19.515    -18.648   54.159    1.000 16.63756  ?  531 HOH A O   1 
HETATM 3785 O  O   . HOH T 8 .   ? 22.59045  6.12126   16.37593  1.000 21.69963  ?  532 HOH A O   1 
HETATM 3786 O  O   . HOH T 8 .   ? 20.90914  -17.40673 31.77678  1.000 13.39153  ?  533 HOH A O   1 
HETATM 3787 O  O   . HOH T 8 .   ? 22.92553  1.61132   21.72266  1.000 8.54695   ?  534 HOH A O   1 
HETATM 3788 O  O   . HOH T 8 .   ? 13.00395  13.03660  24.02166  1.000 24.71777  ?  535 HOH A O   1 
HETATM 3789 O  O   . HOH T 8 .   ? 16.98339  9.35798   20.56415  1.000 11.21557  ?  536 HOH A O   1 
HETATM 3790 O  O   . HOH T 8 .   ? 12.71479  -5.05130  19.46229  1.000 35.28240  ?  537 HOH A O   1 
HETATM 3791 O  O   . HOH T 8 .   ? 22.39498  10.55797  21.65080  1.000 12.19096  ?  538 HOH A O   1 
HETATM 3792 O  O   . HOH T 8 .   ? 21.58160  -23.85759 33.40922  1.000 20.47542  ?  539 HOH A O   1 
HETATM 3793 O  O   . HOH T 8 .   ? 22.41014  6.22186   31.74353  1.000 4.22486   ?  540 HOH A O   1 
HETATM 3794 O  O   . HOH T 8 .   ? 24.995    13.461    44.776    1.000 12.28095  ?  541 HOH A O   1 
HETATM 3795 O  O   . HOH T 8 .   ? 7.61686   1.55646   24.38186  1.000 27.13193  ?  542 HOH A O   1 
HETATM 3796 O  O   . HOH T 8 .   ? 18.64624  -12.41540 33.19647  1.000 18.17558  ?  543 HOH A O   1 
HETATM 3797 O  O   . HOH T 8 .   ? 18.01176  -11.21177 39.24281  1.000 11.37674  ?  544 HOH A O   1 
HETATM 3798 O  O   . HOH T 8 .   ? 39.85246  3.64723   30.25917  1.000 28.36695  ?  545 HOH A O   1 
HETATM 3799 O  O   . HOH T 8 .   ? 8.37835   -17.89513 34.08534  1.000 23.43939  ?  546 HOH A O   1 
HETATM 3800 O  O   . HOH T 8 .   ? 25.60187  -5.68397  22.43580  1.000 14.40093  ?  547 HOH A O   1 
HETATM 3801 O  O   . HOH T 8 .   ? 21.70850  10.70041  15.72761  1.000 15.49685  ?  548 HOH A O   1 
HETATM 3802 O  O   . HOH T 8 .   ? 24.53104  4.23569   51.57712  1.000 35.41382  ?  549 HOH A O   1 
HETATM 3803 O  O   . HOH T 8 .   ? 27.69166  14.53985  42.58209  1.000 15.60845  ?  550 HOH A O   1 
HETATM 3804 O  O   . HOH T 8 .   ? 27.90788  -5.14696  23.53266  1.000 22.10357  ?  551 HOH A O   1 
HETATM 3805 O  O   . HOH T 8 .   ? 17.40400  -22.03411 41.65977  1.000 13.91745  ?  552 HOH A O   1 
HETATM 3806 O  O   . HOH T 8 .   ? 30.10851  -6.47557  22.32502  1.000 29.18716  ?  553 HOH A O   1 
HETATM 3807 O  O   . HOH T 8 .   ? 10.22980  7.12688   29.69995  1.000 22.73349  ?  554 HOH A O   1 
HETATM 3808 O  O   . HOH T 8 .   ? 9.16048   -12.46873 37.18331  1.000 23.51792  ?  555 HOH A O   1 
HETATM 3809 O  O   . HOH T 8 .   ? 9.06149   -13.89186 46.11124  1.000 21.72427  ?  556 HOH A O   1 
HETATM 3810 O  O   . HOH T 8 .   ? 36.23573  5.91635   39.69457  1.000 11.81969  ?  557 HOH A O   1 
HETATM 3811 O  O   . HOH T 8 .   ? 21.48732  17.42577  36.69456  1.000 22.87600  ?  558 HOH A O   1 
HETATM 3812 O  O   . HOH T 8 .   ? 33.15873  10.52484  26.34188  1.000 37.28730  ?  559 HOH A O   1 
HETATM 3813 O  O   . HOH T 8 .   ? 25.88979  -11.51466 28.00960  1.000 10.46930  ?  560 HOH A O   1 
HETATM 3814 O  O   . HOH T 8 .   ? 35.09529  2.47010   23.72140  1.000 38.03257  ?  561 HOH A O   1 
HETATM 3815 O  O   . HOH T 8 .   ? 4.74980   4.02912   29.12336  1.000 24.71745  ?  562 HOH A O   1 
HETATM 3816 O  O   . HOH T 8 .   ? 16.62064  -11.48677 57.21889  1.000 23.06182  ?  563 HOH A O   1 
HETATM 3817 O  O   . HOH T 8 .   ? 36.66578  -2.32171  40.96143  1.000 17.81930  ?  564 HOH A O   1 
HETATM 3818 O  O   . HOH T 8 .   ? 32.43909  -17.10435 32.40066  1.000 22.81035  ?  565 HOH A O   1 
HETATM 3819 O  O   . HOH T 8 .   ? 33.23380  -8.65166  41.36898  1.000 24.15850  ?  566 HOH A O   1 
HETATM 3820 O  O   . HOH T 8 .   ? 20.36954  -8.16262  55.26554  1.000 25.49140  ?  567 HOH A O   1 
HETATM 3821 O  O   . HOH T 8 .   ? 22.23360  7.57951   52.24523  1.000 22.82171  ?  568 HOH A O   1 
HETATM 3822 O  O   . HOH T 8 .   ? 13.99717  -5.50791  31.17832  1.000 18.56593  ?  569 HOH A O   1 
HETATM 3823 O  O   . HOH T 8 .   ? 28.42497  -16.43815 27.21460  1.000 24.01640  ?  570 HOH A O   1 
HETATM 3824 O  O   . HOH T 8 .   ? 14.49256  9.61570   22.05051  1.000 22.15917  ?  571 HOH A O   1 
HETATM 3825 O  O   . HOH T 8 .   ? 32.54936  -6.93832  48.21152  1.000 35.10876  ?  572 HOH A O   1 
HETATM 3826 O  O   . HOH T 8 .   ? 16.54053  4.33805   20.95774  1.000 12.21439  ?  573 HOH A O   1 
HETATM 3827 O  O   . HOH T 8 .   ? 27.34243  11.89024  23.31286  1.000 31.16314  ?  574 HOH A O   1 
HETATM 3828 O  O   . HOH T 8 .   ? 28.98130  -8.99046  22.79070  1.000 30.43010  ?  575 HOH A O   1 
HETATM 3829 O  O   . HOH T 8 .   ? 16.85487  6.83158   19.79745  1.000 12.65591  ?  576 HOH A O   1 
HETATM 3830 O  O   . HOH T 8 .   ? 5.65130   13.67433  40.47949  1.000 18.33278  ?  577 HOH A O   1 
HETATM 3831 O  O   . HOH T 8 .   ? 24.70511  -17.81902 27.26620  1.000 23.11762  ?  578 HOH A O   1 
HETATM 3832 O  O   . HOH T 8 .   ? 26.67634  -21.14632 31.73186  1.000 26.93858  ?  579 HOH A O   1 
HETATM 3833 O  O   . HOH T 8 .   ? 26.09568  7.45560   20.94206  1.000 22.29743  ?  580 HOH A O   1 
HETATM 3834 O  O   . HOH T 8 .   ? 11.37612  -9.28365  50.96393  1.000 35.11047  ?  581 HOH A O   1 
HETATM 3835 O  O   . HOH T 8 .   ? 11.42383  -4.28360  31.90437  1.000 20.24224  ?  582 HOH A O   1 
HETATM 3836 O  O   . HOH T 8 .   ? 27.66290  -16.19298 46.75635  1.000 17.80253  ?  583 HOH A O   1 
HETATM 3837 O  O   . HOH T 8 .   ? 30.34163  13.02437  26.54956  1.000 26.99170  ?  584 HOH A O   1 
HETATM 3838 O  O   . HOH T 8 .   ? 14.35054  -15.44834 20.43736  1.000 32.29817  ?  585 HOH A O   1 
HETATM 3839 O  O   . HOH T 8 .   ? 40.09832  -2.09328  34.86471  1.000 35.75261  ?  586 HOH A O   1 
HETATM 3840 O  O   . HOH T 8 .   ? 6.26061   -1.66914  29.86910  1.000 48.83107  ?  587 HOH A O   1 
HETATM 3841 O  O   . HOH T 8 .   ? 6.90307   -12.73372 27.94238  1.000 16.09858  ?  588 HOH A O   1 
HETATM 3842 O  O   . HOH T 8 .   ? 24.11001  -19.30736 52.92670  1.000 28.90388  ?  589 HOH A O   1 
HETATM 3843 O  O   . HOH T 8 .   ? 3.89694   -6.60815  39.80945  1.000 31.97982  ?  590 HOH A O   1 
HETATM 3844 O  O   . HOH T 8 .   ? 4.79356   -6.07188  26.64869  1.000 29.45619  ?  591 HOH A O   1 
HETATM 3845 O  O   . HOH T 8 .   ? 6.59146   -4.00609  32.54611  1.000 15.39861  ?  592 HOH A O   1 
HETATM 3846 O  O   . HOH T 8 .   ? 1.83952   -1.61372  36.48515  1.000 37.37055  ?  593 HOH A O   1 
HETATM 3847 O  O   . HOH T 8 .   ? 41.29317  -2.05886  37.75000  1.000 37.17872  ?  594 HOH A O   1 
HETATM 3848 O  O   . HOH T 8 .   ? 7.96089   14.20861  43.64129  1.000 18.00219  ?  595 HOH A O   1 
HETATM 3849 O  O   . HOH T 8 .   ? 29.75656  -12.76323 25.26446  1.000 21.59586  ?  596 HOH A O   1 
HETATM 3850 O  O   . HOH T 8 .   ? 33.57792  -13.90879 42.01170  1.000 27.75829  ?  597 HOH A O   1 
HETATM 3851 O  O   . HOH T 8 .   ? 18.59840  10.81180  50.12328  1.000 37.51490  ?  598 HOH A O   1 
HETATM 3852 O  O   . HOH T 8 .   ? 24.79237  26.48336  24.48987  1.000 30.70452  ?  599 HOH A O   1 
HETATM 3853 O  O   . HOH T 8 .   ? 23.17939  16.73320  35.13368  1.000 26.12607  ?  600 HOH A O   1 
HETATM 3854 O  O   . HOH T 8 .   ? 13.82653  -8.80443  51.67808  1.000 17.10459  ?  601 HOH A O   1 
HETATM 3855 O  O   . HOH T 8 .   ? 29.90315  -22.12189 43.49302  1.000 42.97236  ?  602 HOH A O   1 
HETATM 3856 O  O   . HOH T 8 .   ? 8.80962   -12.20784 48.78645  1.000 36.84592  ?  603 HOH A O   1 
HETATM 3857 O  O   . HOH T 8 .   ? 22.54917  -8.69358  56.35541  1.000 31.57382  ?  604 HOH A O   1 
HETATM 3858 O  O   . HOH T 8 .   ? 11.44259  11.57293  27.72333  1.000 9.78824   ?  605 HOH A O   1 
HETATM 3859 O  O   . HOH T 8 .   ? 30.72966  5.27136   24.44265  1.000 45.20951  ?  606 HOH A O   1 
HETATM 3860 O  O   . HOH T 8 .   ? 17.60644  -22.71947 27.15977  1.000 31.52631  ?  607 HOH A O   1 
HETATM 3861 O  O   . HOH T 8 .   ? 1.73359   0.38086   35.18833  1.000 34.27369  ?  608 HOH A O   1 
HETATM 3862 O  O   . HOH T 8 .   ? 13.22916  -23.43641 42.47176  1.000 36.33946  ?  609 HOH A O   1 
HETATM 3863 O  O   . HOH T 8 .   ? 39.786    -1.213    42.268    1.000 33.83639  ?  610 HOH A O   1 
HETATM 3864 O  O   . HOH T 8 .   ? 37.17902  -6.63723  39.34768  1.000 37.64111  ?  611 HOH A O   1 
HETATM 3865 O  O   . HOH T 8 .   ? 5.16520   -2.32418  30.70335  1.000 37.76783  ?  612 HOH A O   1 
HETATM 3866 O  O   . HOH T 8 .   ? -2.07723  5.20999   46.22217  1.000 32.68700  ?  613 HOH A O   1 
HETATM 3867 O  O   . HOH T 8 .   ? 12.92709  8.53499   22.53029  1.000 40.44528  ?  614 HOH A O   1 
HETATM 3868 O  O   . HOH T 8 .   ? 35.83083  -8.45712  39.93003  1.000 28.94962  ?  615 HOH A O   1 
HETATM 3869 O  O   . HOH T 8 .   ? 11.88852  -16.09314 37.41300  1.000 32.16437  ?  616 HOH A O   1 
HETATM 3870 O  O   . HOH T 8 .   ? 18.795    -20.952   53.062    1.000 16.14035  ?  617 HOH A O   1 
HETATM 3871 O  O   . HOH T 8 .   ? 27.24664  11.68190  20.50121  1.000 39.48002  ?  618 HOH A O   1 
HETATM 3872 O  O   . HOH T 8 .   ? 31.05120  11.82505  39.30207  1.000 35.10165  ?  619 HOH A O   1 
HETATM 3873 O  O   . HOH T 8 .   ? -6.556    9.468     37.534    1.000 42.46883  ?  620 HOH A O   1 
HETATM 3874 O  O   . HOH T 8 .   ? 33.38360  -9.62621  45.87288  1.000 37.58169  ?  621 HOH A O   1 
HETATM 3875 O  O   . HOH T 8 .   ? 10.50439  -21.14218 35.21113  1.000 32.95087  ?  622 HOH A O   1 
HETATM 3876 O  O   . HOH T 8 .   ? 10.86386  11.88668  24.73427  1.000 38.20048  ?  623 HOH A O   1 
HETATM 3877 O  O   . HOH T 8 .   ? 10.08066  6.74104   27.08836  1.000 37.18311  ?  624 HOH A O   1 
HETATM 3878 O  O   . HOH T 8 .   ? 10.31279  -4.60855  19.51394  1.000 25.46838  ?  625 HOH A O   1 
HETATM 3879 O  O   . HOH T 8 .   ? 29.522    -18.212   51.831    1.000 36.06710  ?  626 HOH A O   1 
HETATM 3880 O  O   . HOH T 8 .   ? 29.14803  -17.86418 47.23336  1.000 35.49052  ?  627 HOH A O   1 
HETATM 3881 O  O   . HOH T 8 .   ? 21.92910  1.65727   15.77526  1.000 31.35522  ?  628 HOH A O   1 
HETATM 3882 O  O   . HOH T 8 .   ? 32.76280  -11.04499 43.61150  1.000 30.96724  ?  629 HOH A O   1 
HETATM 3883 O  O   . HOH T 8 .   ? 8.45581   -13.25830 17.73689  1.000 33.98216  ?  630 HOH A O   1 
HETATM 3884 O  O   . HOH T 8 .   ? 42.835    1.468     32.424    1.000 35.30200  ?  631 HOH A O   1 
HETATM 3885 O  O   . HOH T 8 .   ? 30.51483  -10.85945 23.64965  1.000 30.23084  ?  632 HOH A O   1 
HETATM 3886 O  O   . HOH T 8 .   ? 26.96767  -7.01530  52.78664  1.000 14.62631  ?  633 HOH A O   1 
HETATM 3887 O  O   . HOH T 8 .   ? 14.76520  -23.88635 40.30798  1.000 41.97372  ?  634 HOH A O   1 
HETATM 3888 O  O   . HOH T 8 .   ? 27.661    -25.635   37.530    1.000 38.38258  ?  635 HOH A O   1 
HETATM 3889 O  O   . HOH T 8 .   ? 32.16150  -12.87844 26.98264  1.000 34.49874  ?  636 HOH A O   1 
HETATM 3890 O  O   . HOH T 8 .   ? 36.85956  2.54024   47.65411  1.000 39.13728  ?  637 HOH A O   1 
HETATM 3891 O  O   . HOH T 8 .   ? -0.94170  7.76467   44.85988  1.000 36.68352  ?  638 HOH A O   1 
HETATM 3892 O  O   . HOH T 8 .   ? 17.46587  -21.44216 46.87254  1.000 16.07582  ?  639 HOH A O   1 
HETATM 3893 O  O   . HOH T 8 .   ? 32.48153  -12.98731 33.86632  1.000 20.37159  ?  640 HOH A O   1 
HETATM 3894 O  O   . HOH T 8 .   ? 12.62664  -19.33809 35.50769  1.000 21.87487  ?  641 HOH A O   1 
HETATM 3895 O  O   . HOH T 8 .   ? 31.56422  14.66251  27.23592  1.000 39.04042  ?  642 HOH A O   1 
HETATM 3896 O  O   . HOH T 8 .   ? 33.62389  -10.85331 23.60876  1.000 28.95888  ?  643 HOH A O   1 
HETATM 3897 O  O   . HOH T 8 .   ? 20.69828  24.14057  24.81562  1.000 41.42721  ?  644 HOH A O   1 
HETATM 3898 O  O   . HOH T 8 .   ? 4.59704   -12.37188 26.24831  1.000 41.26632  ?  645 HOH A O   1 
HETATM 3899 O  O   . HOH T 8 .   ? 4.69373   -5.71200  33.80010  1.000 31.65027  ?  646 HOH A O   1 
HETATM 3900 O  O   . HOH T 8 .   ? 42.556    -1.105    33.083    1.000 43.90996  ?  647 HOH A O   1 
HETATM 3901 O  O   . HOH T 8 .   ? 3.13441   -1.60390  33.80449  1.000 37.36518  ?  648 HOH A O   1 
HETATM 3902 O  O   . HOH T 8 .   ? 28.82786  7.76854   20.26395  1.000 29.55328  ?  649 HOH A O   1 
HETATM 3903 O  O   . HOH T 8 .   ? 22.96346  4.79073   52.95245  1.000 32.84071  ?  650 HOH A O   1 
HETATM 3904 O  O   . HOH T 8 .   ? 2.25112   1.14303   47.33805  1.000 40.82446  ?  651 HOH A O   1 
HETATM 3905 O  O   . HOH T 8 .   ? 3.83170   -10.43094 25.68963  1.000 37.05632  ?  652 HOH A O   1 
HETATM 3906 O  O   . HOH T 8 .   ? 32.29151  -9.26897  49.47934  1.000 40.05071  ?  653 HOH A O   1 
HETATM 3907 O  O   . HOH T 8 .   ? 37.68735  8.60962   39.09561  1.000 42.00860  ?  654 HOH A O   1 
HETATM 3908 O  O   . HOH T 8 .   ? 4.29218   -1.11738  26.81805  1.000 39.88507  ?  655 HOH A O   1 
HETATM 3909 O  O   . HOH T 8 .   ? 18.28031  -17.56106 20.26995  1.000 25.96540  ?  656 HOH A O   1 
HETATM 3910 O  O   . HOH T 8 .   ? 34.04970  -10.91741 41.93171  1.000 40.72993  ?  657 HOH A O   1 
HETATM 3911 O  O   . HOH T 8 .   ? 30.02622  15.03171  38.76033  1.000 40.98127  ?  658 HOH A O   1 
HETATM 3912 O  O   . HOH T 8 .   ? -2.92261  5.88803   31.90758  1.000 40.86342  ?  659 HOH A O   1 
HETATM 3913 O  O   . HOH T 8 .   ? 3.89030   0.07818   48.16262  1.000 35.01305  ?  660 HOH A O   1 
HETATM 3914 O  O   . HOH T 8 .   ? 6.44833   -11.14603 38.73908  1.000 38.49337  ?  661 HOH A O   1 
HETATM 3915 O  O   . HOH T 8 .   ? 3.23173   12.26481  33.32983  1.000 31.31429  ?  662 HOH A O   1 
HETATM 3916 O  O   . HOH T 8 .   ? 18.65406  19.32169  15.78263  1.000 36.08259  ?  663 HOH A O   1 
HETATM 3917 O  O   . HOH T 8 .   ? 16.22751  18.75342  17.07588  1.000 25.90361  ?  664 HOH A O   1 
HETATM 3918 O  O   . HOH T 8 .   ? 30.563    -3.970    19.807    1.000 26.43925  ?  665 HOH A O   1 
HETATM 3919 O  O   . HOH T 8 .   ? -0.89368  7.72457   42.25454  1.000 12.15607  ?  666 HOH A O   1 
HETATM 3920 O  O   . HOH T 8 .   ? 32.72401  4.60561   23.06881  1.000 38.30684  ?  667 HOH A O   1 
HETATM 3921 O  O   . HOH T 8 .   ? 26.27286  -16.11953 20.90387  1.000 33.30565  ?  668 HOH A O   1 
HETATM 3922 O  O   . HOH T 8 .   ? -2.40479  2.32884   45.58375  1.000 45.22463  ?  669 HOH A O   1 
HETATM 3923 O  O   . HOH T 8 .   ? 19.10234  16.79388  14.14254  1.000 24.80730  ?  670 HOH A O   1 
HETATM 3924 O  O   . HOH T 8 .   ? 35.87983  0.31143   47.51452  1.000 32.76202  ?  671 HOH A O   1 
HETATM 3925 O  O   . HOH T 8 .   ? 23.61412  12.11472  17.35504  1.000 30.67048  ?  672 HOH A O   1 
HETATM 3926 O  O   . HOH T 8 .   ? 4.17727   -7.49547  36.88864  1.000 35.49441  ?  673 HOH A O   1 
HETATM 3927 O  O   . HOH T 8 .   ? -1.24073  0.82109   44.20402  1.000 23.45259  ?  674 HOH A O   1 
HETATM 3928 O  O   . HOH T 8 .   ? 12.56620  -25.48640 30.64603  1.000 35.53917  ?  675 HOH A O   1 
HETATM 3929 O  O   . HOH T 8 .   ? 5.61609   4.80906   26.60659  1.000 29.80544  ?  676 HOH A O   1 
HETATM 3930 O  O   . HOH T 8 .   ? 6.24255   -8.27306  38.80371  1.000 29.18463  ?  677 HOH A O   1 
HETATM 3931 O  O   . HOH T 8 .   ? 30.48358  13.92925  41.70634  1.000 35.99811  ?  678 HOH A O   1 
HETATM 3932 O  O   . HOH T 8 .   ? 24.42453  10.20932  19.88192  1.000 33.50872  ?  679 HOH A O   1 
HETATM 3933 O  O   . HOH T 8 .   ? 12.62174  14.70359  26.49648  1.000 29.29115  ?  680 HOH A O   1 
HETATM 3934 O  O   . HOH T 8 .   ? 39.70350  0.95428   46.08175  1.000 37.47607  ?  681 HOH A O   1 
HETATM 3935 O  O   . HOH T 8 .   ? 3.94099   -8.95905  40.15772  1.000 37.83450  ?  682 HOH A O   1 
HETATM 3936 O  O   . HOH T 8 .   ? 39.51301  -1.33894  44.99035  1.000 28.10947  ?  683 HOH A O   1 
HETATM 3937 O  O   . HOH U 8 .   ? 11.76464  3.32772   10.88985  1.000 11.57834  ?  401 HOH B O   1 
HETATM 3938 O  O   . HOH U 8 .   ? 2.65280   2.16255   9.36175   1.000 19.24907  ?  402 HOH B O   1 
HETATM 3939 O  O   . HOH U 8 .   ? -6.05637  19.21606  -13.24086 1.000 36.92684  ?  403 HOH B O   1 
HETATM 3940 O  O   . HOH U 8 .   ? 9.66877   -11.88360 -2.53353  1.000 33.67769  ?  404 HOH B O   1 
HETATM 3941 O  O   . HOH U 8 .   ? 19.37877  -11.93509 19.50615  1.000 29.04892  ?  405 HOH B O   1 
HETATM 3942 O  O   . HOH U 8 .   ? 19.48737  -10.62403 6.12997   1.000 31.39934  ?  406 HOH B O   1 
HETATM 3943 O  O   . HOH U 8 .   ? 21.22674  12.03523  5.54854   1.000 31.27310  ?  407 HOH B O   1 
HETATM 3944 O  O   . HOH U 8 .   ? -0.67775  2.07766   -10.48158 1.000 24.59444  ?  408 HOH B O   1 
HETATM 3945 O  O   . HOH U 8 .   ? 11.93847  25.11082  7.21006   1.000 35.71295  ?  409 HOH B O   1 
HETATM 3946 O  O   . HOH U 8 .   ? -8.70325  12.30631  -19.29442 1.000 42.27580  ?  410 HOH B O   1 
HETATM 3947 O  O   . HOH U 8 .   ? 22.32101  4.36024   -4.64761  1.000 42.27841  ?  411 HOH B O   1 
HETATM 3948 O  O   . HOH U 8 .   ? 4.00918   22.31340  8.69723   1.000 17.29359  ?  412 HOH B O   1 
HETATM 3949 O  O   . HOH U 8 .   ? 16.79098  15.25071  6.13540   1.000 22.24160  ?  413 HOH B O   1 
HETATM 3950 O  O   . HOH U 8 .   ? -3.86427  2.08122   12.76862  1.000 13.86700  ?  414 HOH B O   1 
HETATM 3951 O  O   . HOH U 8 .   ? -13.22449 20.53561  -0.10526  1.000 36.90821  ?  415 HOH B O   1 
HETATM 3952 O  O   . HOH U 8 .   ? 20.04556  12.71000  14.34932  1.000 17.18450  ?  416 HOH B O   1 
HETATM 3953 O  O   . HOH U 8 .   ? -3.88219  12.85623  8.96195   1.000 12.81198  ?  417 HOH B O   1 
HETATM 3954 O  O   . HOH U 8 .   ? 23.39389  -16.57116 10.35107  1.000 33.12154  ?  418 HOH B O   1 
HETATM 3955 O  O   . HOH U 8 .   ? 0.60699   16.82023  20.90610  1.000 41.55271  ?  419 HOH B O   1 
HETATM 3956 O  O   . HOH U 8 .   ? 13.50350  4.54277   21.48222  1.000 25.10756  ?  420 HOH B O   1 
HETATM 3957 O  O   . HOH U 8 .   ? 3.69059   8.48248   12.98311  1.000 15.06176  ?  421 HOH B O   1 
HETATM 3958 O  O   . HOH U 8 .   ? 8.58234   -6.58102  18.56369  1.000 28.02496  ?  422 HOH B O   1 
HETATM 3959 O  O   . HOH U 8 .   ? 13.97362  -6.26866  -2.66170  1.000 15.25370  ?  423 HOH B O   1 
HETATM 3960 O  O   . HOH U 8 .   ? 18.62388  17.50961  8.06508   1.000 26.45146  ?  424 HOH B O   1 
HETATM 3961 O  O   . HOH U 8 .   ? 17.26402  -14.83392 20.43845  1.000 15.12597  ?  425 HOH B O   1 
HETATM 3962 O  O   . HOH U 8 .   ? -6.34035  19.61883  2.19607   1.000 14.39788  ?  426 HOH B O   1 
HETATM 3963 O  O   . HOH U 8 .   ? 0.50861   7.26714   -10.97324 1.000 35.73650  ?  427 HOH B O   1 
HETATM 3964 O  O   . HOH U 8 .   ? 19.86850  -16.79791 4.03725   1.000 29.61698  ?  428 HOH B O   1 
HETATM 3965 O  O   . HOH U 8 .   ? -1.40206  -13.57629 2.23514   1.000 21.15885  ?  429 HOH B O   1 
HETATM 3966 O  O   . HOH U 8 .   ? -9.010    -10.768   27.275    1.000 35.26642  ?  430 HOH B O   1 
HETATM 3967 O  O   . HOH U 8 .   ? 25.05825  5.04324   10.92610  1.000 32.81169  ?  431 HOH B O   1 
HETATM 3968 O  O   . HOH U 8 .   ? -4.46191  -10.58065 -2.03596  1.000 30.09501  ?  432 HOH B O   1 
HETATM 3969 O  O   . HOH U 8 .   ? 9.40581   15.99510  7.14797   1.000 11.59576  ?  433 HOH B O   1 
HETATM 3970 O  O   . HOH U 8 .   ? -10.45967 17.19058  -11.40802 1.000 40.28030  ?  434 HOH B O   1 
HETATM 3971 O  O   . HOH U 8 .   ? 7.42019   -6.49169  15.24774  1.000 10.36591  ?  435 HOH B O   1 
HETATM 3972 O  O   . HOH U 8 .   ? 1.20824   17.52905  12.47187  1.000 13.78470  ?  436 HOH B O   1 
HETATM 3973 O  O   . HOH U 8 .   ? -9.43771  7.56434   9.01648   1.000 17.42690  ?  437 HOH B O   1 
HETATM 3974 O  O   . HOH U 8 .   ? 1.45658   -4.56090  8.11737   1.000 9.14141   ?  438 HOH B O   1 
HETATM 3975 O  O   . HOH U 8 .   ? -6.04155  13.90275  7.26799   1.000 11.95755  ?  439 HOH B O   1 
HETATM 3976 O  O   . HOH U 8 .   ? 3.77663   -15.52954 9.36875   1.000 33.97584  ?  440 HOH B O   1 
HETATM 3977 O  O   . HOH U 8 .   ? 9.26993   18.16245  -6.97742  1.000 29.49703  ?  441 HOH B O   1 
HETATM 3978 O  O   . HOH U 8 .   ? -12.70936 2.35954   16.22137  1.000 34.19176  ?  442 HOH B O   1 
HETATM 3979 O  O   . HOH U 8 .   ? -12.56685 6.13976   11.51284  1.000 25.36167  ?  443 HOH B O   1 
HETATM 3980 O  O   . HOH U 8 .   ? 14.51383  20.81275  15.56077  1.000 37.74979  ?  444 HOH B O   1 
HETATM 3981 O  O   . HOH U 8 .   ? 13.55163  -3.51345  11.96736  1.000 8.47386   ?  445 HOH B O   1 
HETATM 3982 O  O   . HOH U 8 .   ? 19.79222  -1.88999  2.58601   1.000 28.47746  ?  446 HOH B O   1 
HETATM 3983 O  O   . HOH U 8 .   ? -2.86550  -15.13644 10.80832  1.000 28.89199  ?  447 HOH B O   1 
HETATM 3984 O  O   . HOH U 8 .   ? 12.77831  13.15369  -0.36073  1.000 12.61508  ?  448 HOH B O   1 
HETATM 3985 O  O   . HOH U 8 .   ? -9.68879  14.94934  8.89665   1.000 26.00480  ?  449 HOH B O   1 
HETATM 3986 O  O   . HOH U 8 .   ? -13.17888 -0.70002  20.35083  1.000 23.30999  ?  450 HOH B O   1 
HETATM 3987 O  O   . HOH U 8 .   ? -0.10341  20.54400  9.54535   1.000 25.87028  ?  451 HOH B O   1 
HETATM 3988 O  O   . HOH U 8 .   ? -5.98644  -13.56836 7.25050   1.000 30.28185  ?  452 HOH B O   1 
HETATM 3989 O  O   . HOH U 8 .   ? 6.25889   14.34822  20.54270  1.000 15.66956  ?  453 HOH B O   1 
HETATM 3990 O  O   . HOH U 8 .   ? 10.57124  -2.79799  8.19342   1.000 6.93408   ?  454 HOH B O   1 
HETATM 3991 O  O   . HOH U 8 .   ? 15.16437  -14.67831 13.66817  1.000 12.56364  ?  455 HOH B O   1 
HETATM 3992 O  O   . HOH U 8 .   ? 10.32954  -17.73353 4.16069   1.000 30.88303  ?  456 HOH B O   1 
HETATM 3993 O  O   . HOH U 8 .   ? 3.12192   23.93249  15.43738  1.000 26.98955  ?  457 HOH B O   1 
HETATM 3994 O  O   . HOH U 8 .   ? 8.28596   0.94401   12.93621  1.000 11.93279  ?  458 HOH B O   1 
HETATM 3995 O  O   . HOH U 8 .   ? 20.68279  10.16250  7.10554   1.000 29.49593  ?  459 HOH B O   1 
HETATM 3996 O  O   . HOH U 8 .   ? 17.73105  2.83291   -2.68012  1.000 16.18989  ?  460 HOH B O   1 
HETATM 3997 O  O   . HOH U 8 .   ? 21.17208  -4.65373  -5.85987  1.000 28.32918  ?  461 HOH B O   1 
HETATM 3998 O  O   . HOH U 8 .   ? 8.85403   2.44290   9.55281   1.000 16.70239  ?  462 HOH B O   1 
HETATM 3999 O  O   . HOH U 8 .   ? 15.25988  4.15725   -3.21191  1.000 17.57705  ?  463 HOH B O   1 
HETATM 4000 O  O   . HOH U 8 .   ? -11.27665 9.18250   7.60018   1.000 29.07011  ?  464 HOH B O   1 
HETATM 4001 O  O   . HOH U 8 .   ? 10.18692  11.73172  15.50599  1.000 8.62830   ?  465 HOH B O   1 
HETATM 4002 O  O   . HOH U 8 .   ? 22.38894  5.82679   8.36445   1.000 19.92903  ?  466 HOH B O   1 
HETATM 4003 O  O   . HOH U 8 .   ? 8.39909   2.72664   -10.64100 1.000 22.81780  ?  467 HOH B O   1 
HETATM 4004 O  O   . HOH U 8 .   ? 5.13456   -16.12087 4.67550   1.000 29.47813  ?  468 HOH B O   1 
HETATM 4005 O  O   . HOH U 8 .   ? 8.69467   18.72811  8.00660   1.000 14.08422  ?  469 HOH B O   1 
HETATM 4006 O  O   . HOH U 8 .   ? 2.41384   -8.73743  7.17431   1.000 10.56354  ?  470 HOH B O   1 
HETATM 4007 O  O   . HOH U 8 .   ? 17.70355  0.06165   -8.45916  1.000 24.77183  ?  471 HOH B O   1 
HETATM 4008 O  O   . HOH U 8 .   ? 18.24266  -0.24205  12.34513  1.000 8.67326   ?  472 HOH B O   1 
HETATM 4009 O  O   . HOH U 8 .   ? 23.21433  3.50596   13.87267  1.000 27.79882  ?  473 HOH B O   1 
HETATM 4010 O  O   . HOH U 8 .   ? 15.71488  -8.19027  17.61611  1.000 12.23277  ?  474 HOH B O   1 
HETATM 4011 O  O   . HOH U 8 .   ? 18.23984  7.01913   5.12688   1.000 19.93098  ?  475 HOH B O   1 
HETATM 4012 O  O   . HOH U 8 .   ? 21.57637  -0.10024  19.52641  1.000 8.17940   ?  476 HOH B O   1 
HETATM 4013 O  O   . HOH U 8 .   ? 3.68606   -14.34923 13.79870  1.000 25.50769  ?  477 HOH B O   1 
HETATM 4014 O  O   . HOH U 8 .   ? -0.51544  -10.80247 -4.72624  1.000 28.18617  ?  478 HOH B O   1 
HETATM 4015 O  O   . HOH U 8 .   ? 7.06963   -7.38165  -5.64892  1.000 26.91745  ?  479 HOH B O   1 
HETATM 4016 O  O   . HOH U 8 .   ? 14.28582  21.00994  2.73154   1.000 28.69467  ?  480 HOH B O   1 
HETATM 4017 O  O   . HOH U 8 .   ? -5.03016  11.93161  12.36545  1.000 22.30437  ?  481 HOH B O   1 
HETATM 4018 O  O   . HOH U 8 .   ? -4.14619  8.07882   13.23862  1.000 14.50709  ?  482 HOH B O   1 
HETATM 4019 O  O   . HOH U 8 .   ? 14.64251  6.53534   18.33065  1.000 10.26562  ?  483 HOH B O   1 
HETATM 4020 O  O   . HOH U 8 .   ? 8.26245   -2.25390  9.78296   1.000 7.78078   ?  484 HOH B O   1 
HETATM 4021 O  O   . HOH U 8 .   ? -5.79040  -2.49641  22.47846  1.000 34.54473  ?  485 HOH B O   1 
HETATM 4022 O  O   . HOH U 8 .   ? 20.77799  -9.47127  1.30171   1.000 40.45229  ?  486 HOH B O   1 
HETATM 4023 O  O   . HOH U 8 .   ? 12.06242  18.22027  9.26566   1.000 13.91176  ?  487 HOH B O   1 
HETATM 4024 O  O   . HOH U 8 .   ? 9.11400   7.02980   -4.68852  1.000 13.88801  ?  488 HOH B O   1 
HETATM 4025 O  O   . HOH U 8 .   ? 13.66906  19.64844  19.79488  1.000 40.60485  ?  489 HOH B O   1 
HETATM 4026 O  O   . HOH U 8 .   ? 0.96409   22.59949  8.34991   1.000 21.02176  ?  490 HOH B O   1 
HETATM 4027 O  O   . HOH U 8 .   ? 12.18510  22.71459  3.60929   1.000 35.58771  ?  491 HOH B O   1 
HETATM 4028 O  O   . HOH U 8 .   ? -0.44100  18.85203  16.71482  1.000 22.43793  ?  492 HOH B O   1 
HETATM 4029 O  O   . HOH U 8 .   ? -9.59773  -5.87819  18.03508  1.000 14.80708  ?  493 HOH B O   1 
HETATM 4030 O  O   . HOH U 8 .   ? 5.08199   -10.16428 6.13204   1.000 9.80063   ?  494 HOH B O   1 
HETATM 4031 O  O   . HOH U 8 .   ? -1.45515  23.04424  4.99773   1.000 17.02205  ?  495 HOH B O   1 
HETATM 4032 O  O   . HOH U 8 .   ? 11.15457  14.77946  2.99579   1.000 10.93005  ?  496 HOH B O   1 
HETATM 4033 O  O   . HOH U 8 .   ? 22.31701  -19.55348 12.81948  1.000 33.30336  ?  497 HOH B O   1 
HETATM 4034 O  O   . HOH U 8 .   ? -5.20075  19.90683  -10.37703 1.000 33.29154  ?  498 HOH B O   1 
HETATM 4035 O  O   . HOH U 8 .   ? 19.77211  -8.67569  -1.23846  1.000 37.54973  ?  499 HOH B O   1 
HETATM 4036 O  O   . HOH U 8 .   ? -11.18119 5.01865   -7.04936  1.000 33.15908  ?  500 HOH B O   1 
HETATM 4037 O  O   . HOH U 8 .   ? -6.51523  -2.92854  20.95084  1.000 38.59899  ?  501 HOH B O   1 
HETATM 4038 O  O   . HOH U 8 .   ? 7.19860   -3.26257  21.31965  1.000 35.58674  ?  502 HOH B O   1 
HETATM 4039 O  O   . HOH U 8 .   ? 18.65299  17.68967  11.77423  1.000 28.13825  ?  503 HOH B O   1 
HETATM 4040 O  O   . HOH U 8 .   ? 22.28327  -4.92584  15.49655  1.000 21.31167  ?  504 HOH B O   1 
HETATM 4041 O  O   . HOH U 8 .   ? 2.58889   18.89238  20.33357  1.000 29.49124  ?  505 HOH B O   1 
HETATM 4042 O  O   . HOH U 8 .   ? 6.77635   -14.52203 6.93557   1.000 14.31165  ?  506 HOH B O   1 
HETATM 4043 O  O   . HOH U 8 .   ? 11.66542  3.77511   -10.14266 1.000 23.72406  ?  507 HOH B O   1 
HETATM 4044 O  O   . HOH U 8 .   ? 11.03436  -7.51512  19.43080  1.000 35.83761  ?  508 HOH B O   1 
HETATM 4045 O  O   . HOH U 8 .   ? 8.07325   15.03056  9.32502   1.000 22.29292  ?  509 HOH B O   1 
HETATM 4046 O  O   . HOH U 8 .   ? -11.59617 -11.05716 10.94508  1.000 36.20885  ?  510 HOH B O   1 
HETATM 4047 O  O   . HOH U 8 .   ? 18.48253  14.21963  15.29419  1.000 29.70556  ?  511 HOH B O   1 
HETATM 4048 O  O   . HOH U 8 .   ? 10.55384  14.65516  0.23953   1.000 13.55452  ?  512 HOH B O   1 
HETATM 4049 O  O   . HOH U 8 .   ? -6.91796  -9.52798  -1.60692  1.000 33.86557  ?  513 HOH B O   1 
HETATM 4050 O  O   . HOH U 8 .   ? -6.40441  -6.51770  -5.46200  1.000 23.23421  ?  514 HOH B O   1 
HETATM 4051 O  O   . HOH U 8 .   ? 15.17966  -2.94786  17.80541  1.000 13.41966  ?  515 HOH B O   1 
HETATM 4052 O  O   . HOH U 8 .   ? 18.07944  -9.20606  12.71056  1.000 16.18442  ?  516 HOH B O   1 
HETATM 4053 O  O   . HOH U 8 .   ? 1.83673   2.22093   21.29088  1.000 42.36458  ?  517 HOH B O   1 
HETATM 4054 O  O   . HOH U 8 .   ? 9.39226   4.60962   24.95538  1.000 29.14478  ?  518 HOH B O   1 
HETATM 4055 O  O   . HOH U 8 .   ? 7.22136   -13.34244 15.22442  1.000 16.15438  ?  519 HOH B O   1 
HETATM 4056 O  O   . HOH U 8 .   ? 1.80380   -6.06039  20.71772  1.000 31.11227  ?  520 HOH B O   1 
HETATM 4057 O  O   . HOH U 8 .   ? 10.75238  16.08973  21.94345  1.000 22.06194  ?  521 HOH B O   1 
HETATM 4058 O  O   . HOH U 8 .   ? -11.54841 10.82701  10.06334  1.000 34.02444  ?  522 HOH B O   1 
HETATM 4059 O  O   . HOH U 8 .   ? -11.52418 13.40600  7.47826   1.000 38.95693  ?  523 HOH B O   1 
HETATM 4060 O  O   . HOH U 8 .   ? -13.04503 -4.41438  6.18947   1.000 24.58406  ?  524 HOH B O   1 
HETATM 4061 O  O   . HOH U 8 .   ? 12.91055  16.94990  -3.01255  1.000 28.64230  ?  525 HOH B O   1 
HETATM 4062 O  O   . HOH U 8 .   ? 6.17809   -13.57959 0.30026   1.000 11.55430  ?  526 HOH B O   1 
HETATM 4063 O  O   . HOH U 8 .   ? -4.01437  -10.99390 22.85041  1.000 35.04486  ?  527 HOH B O   1 
HETATM 4064 O  O   . HOH U 8 .   ? -7.74538  7.64169   16.52867  1.000 31.14693  ?  528 HOH B O   1 
HETATM 4065 O  O   . HOH U 8 .   ? 1.27530   12.25029  5.65899   1.000 12.19907  ?  529 HOH B O   1 
HETATM 4066 O  O   . HOH U 8 .   ? 7.738     22.875    -8.843    1.000 37.20710  ?  530 HOH B O   1 
HETATM 4067 O  O   . HOH U 8 .   ? 4.23821   -13.56657 -3.81261  1.000 19.93401  ?  531 HOH B O   1 
HETATM 4068 O  O   . HOH U 8 .   ? 21.02751  9.17031   -0.99185  1.000 28.76541  ?  532 HOH B O   1 
HETATM 4069 O  O   . HOH U 8 .   ? 5.22672   6.54344   13.86380  1.000 17.35785  ?  533 HOH B O   1 
HETATM 4070 O  O   . HOH U 8 .   ? 11.37984  8.59816   20.90417  1.000 27.12102  ?  534 HOH B O   1 
HETATM 4071 O  O   . HOH U 8 .   ? -7.46032  -12.49709 4.95066   1.000 37.93759  ?  535 HOH B O   1 
HETATM 4072 O  O   . HOH U 8 .   ? 9.81613   22.84195  2.27229   1.000 29.12152  ?  536 HOH B O   1 
HETATM 4073 O  O   . HOH U 8 .   ? 19.80369  6.55503   7.30956   1.000 34.13780  ?  537 HOH B O   1 
HETATM 4074 O  O   . HOH U 8 .   ? -15.07485 -0.09283  10.78505  1.000 35.20643  ?  538 HOH B O   1 
HETATM 4075 O  O   . HOH U 8 .   ? 6.38737   13.46970  8.90642   1.000 14.88852  ?  539 HOH B O   1 
HETATM 4076 O  O   . HOH U 8 .   ? -2.44276  13.56090  14.09511  1.000 21.46179  ?  540 HOH B O   1 
HETATM 4077 O  O   . HOH U 8 .   ? 20.72461  9.62365   10.50826  1.000 28.83361  ?  541 HOH B O   1 
HETATM 4078 O  O   . HOH U 8 .   ? 23.38224  -2.83282  11.06772  1.000 23.26318  ?  542 HOH B O   1 
HETATM 4079 O  O   . HOH U 8 .   ? 1.13911   -12.38839 -3.07982  1.000 20.21027  ?  543 HOH B O   1 
HETATM 4080 O  O   . HOH U 8 .   ? 22.34975  -9.57111  16.77712  1.000 17.92752  ?  544 HOH B O   1 
HETATM 4081 O  O   . HOH U 8 .   ? 1.74893   18.18093  -9.01277  1.000 38.41418  ?  545 HOH B O   1 
HETATM 4082 O  O   . HOH U 8 .   ? 3.19408   5.37658   15.41390  1.000 21.59714  ?  546 HOH B O   1 
HETATM 4083 O  O   . HOH U 8 .   ? 9.98638   23.97249  13.35287  1.000 37.15739  ?  547 HOH B O   1 
HETATM 4084 O  O   . HOH U 8 .   ? 9.95791   -5.07703  6.78136   1.000 8.35995   ?  548 HOH B O   1 
HETATM 4085 O  O   . HOH U 8 .   ? 1.36036   -2.99873  22.35297  1.000 24.42258  ?  549 HOH B O   1 
HETATM 4086 O  O   . HOH U 8 .   ? -9.52806  -7.31579  2.28431   1.000 22.30367  ?  550 HOH B O   1 
HETATM 4087 O  O   . HOH U 8 .   ? 14.85634  12.77621  6.21133   1.000 15.61868  ?  551 HOH B O   1 
HETATM 4088 O  O   . HOH U 8 .   ? -9.99862  22.01397  -2.82562  1.000 19.09517  ?  552 HOH B O   1 
HETATM 4089 O  O   . HOH U 8 .   ? 12.09720  -4.84129  -9.08524  1.000 23.78579  ?  553 HOH B O   1 
HETATM 4090 O  O   . HOH U 8 .   ? 8.78117   9.85689   -7.69250  1.000 28.91550  ?  554 HOH B O   1 
HETATM 4091 O  O   . HOH U 8 .   ? 15.06016  18.43567  -1.76256  1.000 28.04107  ?  555 HOH B O   1 
HETATM 4092 O  O   . HOH U 8 .   ? -2.04867  16.11366  16.98774  1.000 32.13954  ?  556 HOH B O   1 
HETATM 4093 O  O   . HOH U 8 .   ? 14.00589  16.41615  19.99112  1.000 28.05931  ?  557 HOH B O   1 
HETATM 4094 O  O   . HOH U 8 .   ? -18.80499 0.05926   8.46544   1.000 37.69505  ?  558 HOH B O   1 
HETATM 4095 O  O   . HOH U 8 .   ? 19.12498  7.03025   9.70431   1.000 13.76266  ?  559 HOH B O   1 
HETATM 4096 O  O   . HOH U 8 .   ? 17.57642  -25.27788 9.86562   1.000 39.30103  ?  560 HOH B O   1 
HETATM 4097 O  O   . HOH U 8 .   ? 20.87682  -6.19679  10.19116  1.000 21.21488  ?  561 HOH B O   1 
HETATM 4098 O  O   . HOH U 8 .   ? -6.50959  -2.78425  26.11325  1.000 29.94727  ?  562 HOH B O   1 
HETATM 4099 O  O   . HOH U 8 .   ? 4.40443   -6.13719  17.56885  1.000 25.97154  ?  563 HOH B O   1 
HETATM 4100 O  O   . HOH U 8 .   ? 7.43885   -15.52809 4.26743   1.000 27.36609  ?  564 HOH B O   1 
HETATM 4101 O  O   . HOH U 8 .   ? -0.22052  5.06393   18.77485  1.000 16.15162  ?  565 HOH B O   1 
HETATM 4102 O  O   . HOH U 8 .   ? -14.98363 1.75889   6.23415   1.000 32.47944  ?  566 HOH B O   1 
HETATM 4103 O  O   . HOH U 8 .   ? 14.79302  19.02816  7.64920   1.000 22.54741  ?  567 HOH B O   1 
HETATM 4104 O  O   . HOH U 8 .   ? 22.03744  -5.38532  0.80751   1.000 43.30147  ?  568 HOH B O   1 
HETATM 4105 O  O   . HOH U 8 .   ? -13.09005 1.76354   11.24829  1.000 35.90510  ?  569 HOH B O   1 
HETATM 4106 O  O   . HOH U 8 .   ? 6.99487   -0.26944  23.11626  1.000 25.49976  ?  570 HOH B O   1 
HETATM 4107 O  O   . HOH U 8 .   ? -10.15795 21.71968  3.45691   1.000 39.25764  ?  571 HOH B O   1 
HETATM 4108 O  O   . HOH U 8 .   ? 11.40734  -13.63606 -2.94199  1.000 43.70092  ?  572 HOH B O   1 
HETATM 4109 O  O   . HOH U 8 .   ? 1.02286   17.44884  -6.46044  1.000 30.93224  ?  573 HOH B O   1 
HETATM 4110 O  O   . HOH U 8 .   ? 16.11750  -5.60154  18.31476  1.000 12.55556  ?  574 HOH B O   1 
HETATM 4111 O  O   . HOH U 8 .   ? 16.98352  17.92835  4.77712   1.000 30.23912  ?  575 HOH B O   1 
HETATM 4112 O  O   . HOH U 8 .   ? 7.88098   25.18261  6.35043   1.000 24.26049  ?  576 HOH B O   1 
HETATM 4113 O  O   . HOH U 8 .   ? -0.87078  -15.71812 9.23758   1.000 31.56913  ?  577 HOH B O   1 
HETATM 4114 O  O   . HOH U 8 .   ? 8.68467   -15.08713 0.38082   1.000 17.89299  ?  578 HOH B O   1 
HETATM 4115 O  O   . HOH U 8 .   ? 7.94943   15.03481  -8.40371  1.000 31.96368  ?  579 HOH B O   1 
HETATM 4116 O  O   . HOH U 8 .   ? -5.527    20.649    -7.807    1.000 36.67150  ?  580 HOH B O   1 
HETATM 4117 O  O   . HOH U 8 .   ? 9.63411   19.01671  -8.89854  1.000 39.23627  ?  581 HOH B O   1 
HETATM 4118 O  O   . HOH U 8 .   ? 6.65757   -10.41799 17.85303  1.000 11.87128  ?  582 HOH B O   1 
HETATM 4119 O  O   . HOH U 8 .   ? -8.09105  -13.20492 10.95183  1.000 20.54448  ?  583 HOH B O   1 
HETATM 4120 O  O   . HOH U 8 .   ? 13.04678  -8.47500  18.76428  1.000 23.45535  ?  584 HOH B O   1 
HETATM 4121 O  O   . HOH U 8 .   ? -5.84120  2.42576   20.47814  1.000 43.37393  ?  585 HOH B O   1 
HETATM 4122 O  O   . HOH U 8 .   ? -21.542   -3.731    3.859     1.000 37.32166  ?  586 HOH B O   1 
HETATM 4123 O  O   . HOH U 8 .   ? -11.31804 9.69039   1.71388   1.000 21.87766  ?  587 HOH B O   1 
HETATM 4124 O  O   . HOH U 8 .   ? 19.05336  14.28197  4.72480   1.000 29.59369  ?  588 HOH B O   1 
HETATM 4125 O  O   . HOH U 8 .   ? 3.56024   13.91137  21.34922  1.000 15.04909  ?  589 HOH B O   1 
HETATM 4126 O  O   . HOH U 8 .   ? 22.28901  -1.23564  17.16562  1.000 25.35706  ?  590 HOH B O   1 
HETATM 4127 O  O   . HOH U 8 .   ? 20.88840  -4.21526  3.36361   1.000 26.33983  ?  591 HOH B O   1 
HETATM 4128 O  O   . HOH U 8 .   ? 24.583    1.409     6.193     1.000 17.21972  ?  592 HOH B O   1 
HETATM 4129 O  O   . HOH U 8 .   ? 6.47941   -17.24718 6.55722   1.000 27.11685  ?  593 HOH B O   1 
HETATM 4130 O  O   . HOH U 8 .   ? 4.42134   -6.93974  -7.02013  1.000 33.63827  ?  594 HOH B O   1 
HETATM 4131 O  O   . HOH U 8 .   ? 12.25024  5.85557   23.81493  1.000 17.86943  ?  595 HOH B O   1 
HETATM 4132 O  O   . HOH U 8 .   ? 21.54234  -2.53498  -6.25351  1.000 34.87704  ?  596 HOH B O   1 
HETATM 4133 O  O   . HOH U 8 .   ? -0.90975  16.67193  11.80663  1.000 28.96073  ?  597 HOH B O   1 
HETATM 4134 O  O   . HOH U 8 .   ? 4.24782   25.13334  8.16989   1.000 32.14633  ?  598 HOH B O   1 
HETATM 4135 O  O   . HOH U 8 .   ? 9.83530   8.70883   27.35245  1.000 36.66008  ?  599 HOH B O   1 
HETATM 4136 O  O   . HOH U 8 .   ? -1.73736  -15.67686 6.49765   1.000 7.07697   ?  600 HOH B O   1 
HETATM 4137 O  O   . HOH U 8 .   ? 13.41878  -13.06250 -4.21585  1.000 36.35140  ?  601 HOH B O   1 
HETATM 4138 O  O   . HOH U 8 .   ? -10.413   -11.042   26.020    1.000 32.18079  ?  602 HOH B O   1 
HETATM 4139 O  O   . HOH U 8 .   ? 1.38769   4.61957   21.25930  1.000 35.99780  ?  603 HOH B O   1 
HETATM 4140 O  O   . HOH U 8 .   ? -5.52763  0.29334   21.52138  1.000 40.70173  ?  604 HOH B O   1 
HETATM 4141 O  O   . HOH U 8 .   ? 8.33819   23.97512  4.21341   1.000 35.64709  ?  605 HOH B O   1 
HETATM 4142 O  O   . HOH U 8 .   ? 6.35259   -5.83291  19.29933  1.000 35.13115  ?  606 HOH B O   1 
HETATM 4143 O  O   . HOH U 8 .   ? -3.64526  -4.12391  23.72898  1.000 36.11528  ?  607 HOH B O   1 
HETATM 4144 O  O   . HOH U 8 .   ? 6.74627   12.35019  -8.67787  1.000 33.32552  ?  608 HOH B O   1 
HETATM 4145 O  O   . HOH U 8 .   ? -0.35759  21.90023  14.47299  1.000 36.33140  ?  609 HOH B O   1 
HETATM 4146 O  O   . HOH U 8 .   ? -16.82380 2.05288   4.76283   1.000 39.56824  ?  610 HOH B O   1 
HETATM 4147 O  O   . HOH U 8 .   ? 3.32008   23.56326  18.16587  1.000 35.86451  ?  611 HOH B O   1 
HETATM 4148 O  O   . HOH U 8 .   ? -18.385   0.414     16.608    1.000 31.19673  ?  612 HOH B O   1 
HETATM 4149 O  O   . HOH U 8 .   ? -5.63421  22.45848  1.88562   1.000 18.70520  ?  613 HOH B O   1 
HETATM 4150 O  O   . HOH U 8 .   ? -3.22187  2.52271   20.68638  1.000 31.32316  ?  614 HOH B O   1 
HETATM 4151 O  O   . HOH U 8 .   ? 21.93845  -6.93350  13.37392  1.000 35.26751  ?  615 HOH B O   1 
HETATM 4152 O  O   . HOH U 8 .   ? 0.74708   20.39122  12.32622  1.000 20.01137  ?  616 HOH B O   1 
HETATM 4153 O  O   . HOH U 8 .   ? -2.33895  6.50223   19.62775  1.000 30.96903  ?  617 HOH B O   1 
HETATM 4154 O  O   . HOH U 8 .   ? 1.18671   19.91404  -7.56558  1.000 39.54805  ?  618 HOH B O   1 
HETATM 4155 O  O   . HOH U 8 .   ? -6.63028  -4.89887  -7.01968  1.000 37.40361  ?  619 HOH B O   1 
HETATM 4156 O  O   . HOH U 8 .   ? 4.80448   -1.10990  23.96023  1.000 32.89204  ?  620 HOH B O   1 
HETATM 4157 O  O   . HOH U 8 .   ? 15.71610  13.32760  -4.15780  1.000 35.91026  ?  621 HOH B O   1 
HETATM 4158 O  O   . HOH U 8 .   ? 14.21458  14.34520  -2.43989  1.000 24.96305  ?  622 HOH B O   1 
HETATM 4159 O  O   . HOH U 8 .   ? 23.75982  -18.69802 8.85975   1.000 39.39301  ?  623 HOH B O   1 
HETATM 4160 O  O   . HOH U 8 .   ? 7.70814   5.94240   26.77537  1.000 35.91597  ?  624 HOH B O   1 
HETATM 4161 O  O   . HOH U 8 .   ? 23.18806  -6.28813  8.33173   1.000 27.25257  ?  625 HOH B O   1 
HETATM 4162 O  O   . HOH U 8 .   ? -13.94234 0.91856   18.29466  1.000 25.06630  ?  626 HOH B O   1 
HETATM 4163 O  O   . HOH U 8 .   ? 15.31473  21.17368  6.00308   1.000 35.72216  ?  627 HOH B O   1 
HETATM 4164 O  O   . HOH U 8 .   ? -13.05652 4.89861   3.70151   1.000 29.09508  ?  628 HOH B O   1 
HETATM 4165 O  O   . HOH U 8 .   ? 4.34987   -3.81418  22.80241  1.000 36.07219  ?  629 HOH B O   1 
HETATM 4166 O  O   . HOH U 8 .   ? -19.526   -0.998    11.352    1.000 29.83851  ?  630 HOH B O   1 
HETATM 4167 O  O   . HOH U 8 .   ? -5.59352  -0.30398  25.46128  1.000 32.67268  ?  631 HOH B O   1 
HETATM 4168 O  O   . HOH U 8 .   ? 5.76663   -15.87878 14.62804  1.000 29.79174  ?  632 HOH B O   1 
HETATM 4169 O  O   . HOH U 8 .   ? -5.38191  8.94178   15.63790  1.000 26.85780  ?  633 HOH B O   1 
HETATM 4170 O  O   . HOH U 8 .   ? 21.91292  7.69224   6.35099   1.000 29.94815  ?  634 HOH B O   1 
HETATM 4171 O  O   . HOH U 8 .   ? -12.27470 -6.41175  18.66389  1.000 26.78998  ?  635 HOH B O   1 
HETATM 4172 O  O   . HOH U 8 .   ? 1.11014   5.58907   -12.83337 1.000 41.90840  ?  636 HOH B O   1 
HETATM 4173 O  O   . HOH U 8 .   ? -5.04284  8.36304   18.58427  1.000 38.24601  ?  637 HOH B O   1 
HETATM 4174 O  O   . HOH U 8 .   ? 22.35054  -10.29711 14.26158  1.000 33.12608  ?  638 HOH B O   1 
HETATM 4175 O  O   . HOH U 8 .   ? 6.74890   -12.81278 -5.58859  1.000 30.57927  ?  639 HOH B O   1 
HETATM 4176 O  O   . HOH U 8 .   ? -16.003   2.187     17.458    1.000 33.70617  ?  640 HOH B O   1 
HETATM 4177 O  O   . HOH U 8 .   ? 24.84125  5.20169   7.40960   1.000 35.08122  ?  641 HOH B O   1 
HETATM 4178 O  O   . HOH U 8 .   ? -14.85503 3.15187   15.11511  1.000 30.70383  ?  642 HOH B O   1 
HETATM 4179 O  O   . HOH U 8 .   ? 22.20857  -15.73859 19.83354  1.000 26.91470  ?  643 HOH B O   1 
HETATM 4180 O  O   . HOH U 8 .   ? 8.55831   -13.31416 -4.87582  1.000 43.82076  ?  644 HOH B O   1 
HETATM 4181 O  O   . HOH U 8 .   ? -15.49878 4.09153   4.80442   1.000 39.61536  ?  645 HOH B O   1 
HETATM 4182 O  O   . HOH U 8 .   ? -0.25637  -6.96614  22.66551  1.000 37.17093  ?  646 HOH B O   1 
HETATM 4183 O  O   . HOH U 8 .   ? 20.75524  -8.76753  12.18063  1.000 37.40243  ?  647 HOH B O   1 
HETATM 4184 O  O   . HOH U 8 .   ? -17.920   2.989     9.505     1.000 36.66949  ?  648 HOH B O   1 
HETATM 4185 O  O   . HOH U 8 .   ? 11.32267  -7.48259  -9.78746  1.000 32.21381  ?  649 HOH B O   1 
HETATM 4186 O  O   . HOH U 8 .   ? -2.62630  -4.79881  25.89403  1.000 46.54613  ?  650 HOH B O   1 
HETATM 4187 O  O   . HOH U 8 .   ? -1.52869  -4.91544  23.82532  1.000 44.98345  ?  651 HOH B O   1 
# 
