data_7Q0D
# 
_entry.id   7Q0D 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.384 
_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   7Q0D         pdb_00007q0d 10.2210/pdb7q0d/pdb 
WWPDB D_1292118565 ?            ?                   
# 
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 
1 'Structure model' 1 0 2022-01-12 
2 'Structure model' 1 1 2022-01-26 
3 'Structure model' 1 2 2024-01-31 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references'    
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Refinement description' 
# 
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 3 'Structure model' chem_comp_atom                
3 3 'Structure model' chem_comp_bond                
4 3 'Structure model' pdbx_initial_refinement_model 
# 
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.pdbx_database_id_PubMed' 
2 2 'Structure model' '_citation.title'                   
3 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7Q0D 
_pdbx_database_status.recvd_initial_deposition_date   2021-10-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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                 4 
_pdbx_contact_author.email              grazulis@ibt.lt 
_pdbx_contact_author.name_first         Saulius 
_pdbx_contact_author.name_last          Grazulis 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7928-5218 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Paketuryte-Latve, V.' 1 0000-0003-0919-7826 
'Smirnov, A.'          2 0000-0001-5080-9367 
'Manakova, E.'         3 0000-0002-6027-2265 
'Grazulis, S.'         4 0000-0002-7928-5218 
# 
_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                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Int J Mol Sci' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1422-0067 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            23 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Methyl 2-Halo-4-Substituted-5-Sulfamoyl-Benzoates as High Affinity and Selective Inhibitors of Carbonic Anhydrase IX.' 
_citation.year                      2021 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3390/ijms23010130 
_citation.pdbx_database_id_PubMed   35008553 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zaksauskas, A.'       1  ? 
primary 'Capkauskaite, E.'     2  ? 
primary 'Paketuryte-Latve, V.' 3  ? 
primary 'Smirnov, A.'          4  ? 
primary 'Leitans, J.'          5  ? 
primary 'Kazaks, A.'           6  ? 
primary 'Dvinskis, E.'         7  ? 
primary 'Stancaitis, L.'       8  ? 
primary 'Mickeviciute, A.'     9  ? 
primary 'Jachno, J.'           10 ? 
primary 'Jezepcikas, L.'       11 ? 
primary 'Linkuviene, V.'       12 ? 
primary 'Sakalauskas, A.'      13 ? 
primary 'Manakova, E.'         14 ? 
primary 'Grazulis, S.'         15 ? 
primary 'Matuliene, J.'        16 ? 
primary 'Tars, K.'             17 ? 
primary 'Matulis, D.'          18 ? 
# 
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 'Carbonic anhydrase 1'                                       28906.186 2   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                   65.409    2   ?       ? ? ? 
3 non-polymer syn 'methyl 4-chloranyl-2-(phenylsulfonyl)-5-sulfamoyl-benzoate' 389.831   2   ?       ? ? ? 
4 non-polymer syn 1,2-ETHANEDIOL                                               62.068    16  ?       ? ? ? 
5 non-polymer syn 'ACETATE ION'                                                59.044    3   ?       ? ? ? 
6 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                      106.120   9   ?       ? ? ? 
7 water       nat water                                                        18.015    836 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase I,Carbonic anhydrase B,CAB,Carbonic anhydrase I,CA-I' 
# 
_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       
;MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVL
KGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQK
VLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAV
PMQHNNRPTQPLKGRTVRASF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVL
KGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQK
VLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAV
PMQHNNRPTQPLKGRTVRASF
;
_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 'ZINC ION'                                                   ZN  
3 'methyl 4-chloranyl-2-(phenylsulfonyl)-5-sulfamoyl-benzoate' 84Z 
4 1,2-ETHANEDIOL                                               EDO 
5 'ACETATE ION'                                                ACT 
6 'DI(HYDROXYETHYL)ETHER'                                      PEG 
7 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   ALA n 
1 3   SER n 
1 4   PRO n 
1 5   ASP n 
1 6   TRP n 
1 7   GLY n 
1 8   TYR n 
1 9   ASP n 
1 10  ASP n 
1 11  LYS n 
1 12  ASN n 
1 13  GLY n 
1 14  PRO n 
1 15  GLU n 
1 16  GLN n 
1 17  TRP n 
1 18  SER n 
1 19  LYS n 
1 20  LEU n 
1 21  TYR n 
1 22  PRO n 
1 23  ILE n 
1 24  ALA n 
1 25  ASN n 
1 26  GLY n 
1 27  ASN n 
1 28  ASN n 
1 29  GLN n 
1 30  SER n 
1 31  PRO n 
1 32  VAL n 
1 33  ASP n 
1 34  ILE n 
1 35  LYS n 
1 36  THR n 
1 37  SER n 
1 38  GLU n 
1 39  THR n 
1 40  LYS n 
1 41  HIS n 
1 42  ASP n 
1 43  THR n 
1 44  SER n 
1 45  LEU n 
1 46  LYS n 
1 47  PRO n 
1 48  ILE n 
1 49  SER n 
1 50  VAL n 
1 51  SER n 
1 52  TYR n 
1 53  ASN n 
1 54  PRO n 
1 55  ALA n 
1 56  THR n 
1 57  ALA n 
1 58  LYS n 
1 59  GLU n 
1 60  ILE n 
1 61  ILE n 
1 62  ASN n 
1 63  VAL n 
1 64  GLY n 
1 65  HIS n 
1 66  SER n 
1 67  PHE n 
1 68  HIS n 
1 69  VAL n 
1 70  ASN n 
1 71  PHE n 
1 72  GLU n 
1 73  ASP n 
1 74  ASN n 
1 75  ASP n 
1 76  ASN n 
1 77  ARG n 
1 78  SER n 
1 79  VAL n 
1 80  LEU n 
1 81  LYS n 
1 82  GLY n 
1 83  GLY n 
1 84  PRO n 
1 85  PHE n 
1 86  SER n 
1 87  ASP n 
1 88  SER n 
1 89  TYR n 
1 90  ARG n 
1 91  LEU n 
1 92  PHE n 
1 93  GLN n 
1 94  PHE n 
1 95  HIS n 
1 96  PHE n 
1 97  HIS n 
1 98  TRP n 
1 99  GLY n 
1 100 SER n 
1 101 THR n 
1 102 ASN n 
1 103 GLU n 
1 104 HIS n 
1 105 GLY n 
1 106 SER n 
1 107 GLU n 
1 108 HIS n 
1 109 THR n 
1 110 VAL n 
1 111 ASP n 
1 112 GLY n 
1 113 VAL n 
1 114 LYS n 
1 115 TYR n 
1 116 SER n 
1 117 ALA n 
1 118 GLU n 
1 119 LEU n 
1 120 HIS n 
1 121 VAL n 
1 122 ALA n 
1 123 HIS n 
1 124 TRP n 
1 125 ASN n 
1 126 SER n 
1 127 ALA n 
1 128 LYS n 
1 129 TYR n 
1 130 SER n 
1 131 SER n 
1 132 LEU n 
1 133 ALA n 
1 134 GLU n 
1 135 ALA n 
1 136 ALA n 
1 137 SER n 
1 138 LYS n 
1 139 ALA n 
1 140 ASP n 
1 141 GLY n 
1 142 LEU n 
1 143 ALA n 
1 144 VAL n 
1 145 ILE n 
1 146 GLY n 
1 147 VAL n 
1 148 LEU n 
1 149 MET n 
1 150 LYS n 
1 151 VAL n 
1 152 GLY n 
1 153 GLU n 
1 154 ALA n 
1 155 ASN n 
1 156 PRO n 
1 157 LYS n 
1 158 LEU n 
1 159 GLN n 
1 160 LYS n 
1 161 VAL n 
1 162 LEU n 
1 163 ASP n 
1 164 ALA n 
1 165 LEU n 
1 166 GLN n 
1 167 ALA n 
1 168 ILE n 
1 169 LYS n 
1 170 THR n 
1 171 LYS n 
1 172 GLY n 
1 173 LYS n 
1 174 ARG n 
1 175 ALA n 
1 176 PRO n 
1 177 PHE n 
1 178 THR n 
1 179 ASN n 
1 180 PHE n 
1 181 ASP n 
1 182 PRO n 
1 183 SER n 
1 184 THR n 
1 185 LEU n 
1 186 LEU n 
1 187 PRO n 
1 188 SER n 
1 189 SER n 
1 190 LEU n 
1 191 ASP n 
1 192 PHE n 
1 193 TRP n 
1 194 THR n 
1 195 TYR n 
1 196 PRO n 
1 197 GLY n 
1 198 SER n 
1 199 LEU n 
1 200 THR n 
1 201 HIS n 
1 202 PRO n 
1 203 PRO n 
1 204 LEU n 
1 205 TYR n 
1 206 GLU n 
1 207 SER n 
1 208 VAL n 
1 209 THR n 
1 210 TRP n 
1 211 ILE n 
1 212 ILE n 
1 213 CYS n 
1 214 LYS n 
1 215 GLU n 
1 216 SER n 
1 217 ILE n 
1 218 SER n 
1 219 VAL n 
1 220 SER n 
1 221 SER n 
1 222 GLU n 
1 223 GLN n 
1 224 LEU n 
1 225 ALA n 
1 226 GLN n 
1 227 PHE n 
1 228 ARG n 
1 229 SER n 
1 230 LEU n 
1 231 LEU n 
1 232 SER n 
1 233 ASN n 
1 234 VAL n 
1 235 GLU n 
1 236 GLY n 
1 237 ASP n 
1 238 ASN n 
1 239 ALA n 
1 240 VAL n 
1 241 PRO n 
1 242 MET n 
1 243 GLN n 
1 244 HIS n 
1 245 ASN n 
1 246 ASN n 
1 247 ARG n 
1 248 PRO n 
1 249 THR n 
1 250 GLN n 
1 251 PRO n 
1 252 LEU n 
1 253 LYS n 
1 254 GLY n 
1 255 ARG n 
1 256 THR n 
1 257 VAL n 
1 258 ARG n 
1 259 ALA n 
1 260 SER n 
1 261 PHE 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                   261 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA1 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET21a 
_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 
84Z non-polymer         . 'methyl 4-chloranyl-2-(phenylsulfonyl)-5-sulfamoyl-benzoate' ?                 'C14 H12 Cl N O6 S2' 
389.831 
ACT non-polymer         . 'ACETATE ION'                                                ?                 'C2 H3 O2 -1'        
59.044  
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  
HIS 'L-peptide linking' y HISTIDINE                                                    ?                 'C6 H10 N3 O2 1'     
156.162 
HOH non-polymer         . WATER                                                        ?                 'H2 O'               
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                   ?                 'C6 H13 N O2'        
131.173 
LEU 'L-peptide linking' y LEUCINE                                                      ?                 'C6 H13 N O2'        
131.173 
LYS 'L-peptide linking' y LYSINE                                                       ?                 'C6 H15 N2 O2 1'     
147.195 
MET 'L-peptide linking' y METHIONINE                                                   ?                 'C5 H11 N O2 S'      
149.211 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                      ?                 'C4 H10 O3'          
106.120 
PHE 'L-peptide linking' y PHENYLALANINE                                                ?                 'C9 H11 N O2'        
165.189 
PRO 'L-peptide linking' y PROLINE                                                      ?                 'C5 H9 N O2'         
115.130 
SER 'L-peptide linking' y SERINE                                                       ?                 'C3 H7 N O3'         
105.093 
THR 'L-peptide linking' y THREONINE                                                    ?                 'C4 H9 N O3'         
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                   ?                 'C11 H12 N2 O2'      
204.225 
TYR 'L-peptide linking' y TYROSINE                                                     ?                 'C9 H11 N O3'        
181.189 
VAL 'L-peptide linking' y VALINE                                                       ?                 'C5 H11 N O2'        
117.146 
ZN  non-polymer         . 'ZINC ION'                                                   ?                 'Zn 2'               
65.409  
# 
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   0   ?   ?   ?   A . n 
A 1 2   ALA 2   1   ?   ?   ?   A . n 
A 1 3   SER 3   2   ?   ?   ?   A . n 
A 1 4   PRO 4   3   3   PRO PRO A . n 
A 1 5   ASP 5   4   4   ASP ASP A . n 
A 1 6   TRP 6   5   5   TRP TRP A . n 
A 1 7   GLY 7   6   6   GLY GLY A . n 
A 1 8   TYR 8   7   7   TYR TYR A . n 
A 1 9   ASP 9   8   8   ASP ASP A . n 
A 1 10  ASP 10  9   9   ASP ASP A . n 
A 1 11  LYS 11  10  10  LYS LYS A . n 
A 1 12  ASN 12  11  11  ASN ASN A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  GLU 15  14  14  GLU GLU A . n 
A 1 16  GLN 16  15  15  GLN GLN A . n 
A 1 17  TRP 17  16  16  TRP TRP A . n 
A 1 18  SER 18  17  17  SER SER A . n 
A 1 19  LYS 19  18  18  LYS LYS A . n 
A 1 20  LEU 20  19  19  LEU LEU A . n 
A 1 21  TYR 21  20  20  TYR TYR A . n 
A 1 22  PRO 22  21  21  PRO PRO A . n 
A 1 23  ILE 23  22  22  ILE ILE A . n 
A 1 24  ALA 24  23  23  ALA ALA A . n 
A 1 25  ASN 25  24  24  ASN ASN A . n 
A 1 26  GLY 26  25  25  GLY GLY A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  ASN 28  27  27  ASN ASN A . n 
A 1 29  GLN 29  28  28  GLN GLN A . n 
A 1 30  SER 30  29  29  SER SER A . n 
A 1 31  PRO 31  30  30  PRO PRO A . n 
A 1 32  VAL 32  31  31  VAL VAL A . n 
A 1 33  ASP 33  32  32  ASP ASP A . n 
A 1 34  ILE 34  33  33  ILE ILE A . n 
A 1 35  LYS 35  34  34  LYS LYS A . n 
A 1 36  THR 36  35  35  THR THR A . n 
A 1 37  SER 37  36  36  SER SER A . n 
A 1 38  GLU 38  37  37  GLU GLU A . n 
A 1 39  THR 39  38  38  THR THR A . n 
A 1 40  LYS 40  39  39  LYS LYS A . n 
A 1 41  HIS 41  40  40  HIS HIS A . n 
A 1 42  ASP 42  41  41  ASP ASP A . n 
A 1 43  THR 43  42  42  THR THR A . n 
A 1 44  SER 44  43  43  SER SER A . n 
A 1 45  LEU 45  44  44  LEU LEU A . n 
A 1 46  LYS 46  45  45  LYS LYS A . n 
A 1 47  PRO 47  46  46  PRO PRO A . n 
A 1 48  ILE 48  47  47  ILE ILE A . n 
A 1 49  SER 49  48  48  SER SER A . n 
A 1 50  VAL 50  49  49  VAL VAL A . n 
A 1 51  SER 51  50  50  SER SER A . n 
A 1 52  TYR 52  51  51  TYR TYR A . n 
A 1 53  ASN 53  52  52  ASN ASN A . n 
A 1 54  PRO 54  53  53  PRO PRO A . n 
A 1 55  ALA 55  54  54  ALA ALA A . n 
A 1 56  THR 56  55  55  THR THR A . n 
A 1 57  ALA 57  56  56  ALA ALA A . n 
A 1 58  LYS 58  57  57  LYS LYS A . n 
A 1 59  GLU 59  58  58  GLU GLU A . n 
A 1 60  ILE 60  59  59  ILE ILE A . n 
A 1 61  ILE 61  60  60  ILE ILE A . n 
A 1 62  ASN 62  61  61  ASN ASN A . n 
A 1 63  VAL 63  62  62  VAL VAL A . n 
A 1 64  GLY 64  63  63  GLY GLY A . n 
A 1 65  HIS 65  64  64  HIS HIS A . n 
A 1 66  SER 66  65  65  SER SER A . n 
A 1 67  PHE 67  66  66  PHE PHE A . n 
A 1 68  HIS 68  67  67  HIS HIS A . n 
A 1 69  VAL 69  68  68  VAL VAL A . n 
A 1 70  ASN 70  69  69  ASN ASN A . n 
A 1 71  PHE 71  70  70  PHE PHE A . n 
A 1 72  GLU 72  71  71  GLU GLU A . n 
A 1 73  ASP 73  72  72  ASP ASP A . n 
A 1 74  ASN 74  73  73  ASN ASN A . n 
A 1 75  ASP 75  74  74  ASP ASP A . n 
A 1 76  ASN 76  75  75  ASN ASN A . n 
A 1 77  ARG 77  76  76  ARG ARG A . n 
A 1 78  SER 78  77  77  SER SER A . n 
A 1 79  VAL 79  78  78  VAL VAL A . n 
A 1 80  LEU 80  79  79  LEU LEU A . n 
A 1 81  LYS 81  80  80  LYS LYS A . n 
A 1 82  GLY 82  81  81  GLY GLY A . n 
A 1 83  GLY 83  82  82  GLY GLY A . n 
A 1 84  PRO 84  83  83  PRO PRO A . n 
A 1 85  PHE 85  84  84  PHE PHE A . n 
A 1 86  SER 86  85  85  SER SER A . n 
A 1 87  ASP 87  86  86  ASP ASP A . n 
A 1 88  SER 88  87  87  SER SER A . n 
A 1 89  TYR 89  88  88  TYR TYR A . n 
A 1 90  ARG 90  89  89  ARG ARG A . n 
A 1 91  LEU 91  90  90  LEU LEU A . n 
A 1 92  PHE 92  91  91  PHE PHE A . n 
A 1 93  GLN 93  92  92  GLN GLN A . n 
A 1 94  PHE 94  93  93  PHE PHE A . n 
A 1 95  HIS 95  94  94  HIS HIS A . n 
A 1 96  PHE 96  95  95  PHE PHE A . n 
A 1 97  HIS 97  96  96  HIS HIS A . n 
A 1 98  TRP 98  97  97  TRP TRP A . n 
A 1 99  GLY 99  98  98  GLY GLY A . n 
A 1 100 SER 100 99  99  SER SER A . n 
A 1 101 THR 101 100 100 THR THR A . n 
A 1 102 ASN 102 101 101 ASN ASN A . n 
A 1 103 GLU 103 102 102 GLU GLU A . n 
A 1 104 HIS 104 103 103 HIS HIS A . n 
A 1 105 GLY 105 104 104 GLY GLY A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 GLU 107 106 106 GLU GLU A . n 
A 1 108 HIS 108 107 107 HIS HIS A . n 
A 1 109 THR 109 108 108 THR THR A . n 
A 1 110 VAL 110 109 109 VAL VAL A . n 
A 1 111 ASP 111 110 110 ASP ASP A . n 
A 1 112 GLY 112 111 111 GLY GLY A . n 
A 1 113 VAL 113 112 112 VAL VAL A . n 
A 1 114 LYS 114 113 113 LYS LYS A . n 
A 1 115 TYR 115 114 114 TYR TYR A . n 
A 1 116 SER 116 115 115 SER SER A . n 
A 1 117 ALA 117 116 116 ALA ALA A . n 
A 1 118 GLU 118 117 117 GLU GLU A . n 
A 1 119 LEU 119 118 118 LEU LEU A . n 
A 1 120 HIS 120 119 119 HIS HIS A . n 
A 1 121 VAL 121 120 120 VAL VAL A . n 
A 1 122 ALA 122 121 121 ALA ALA A . n 
A 1 123 HIS 123 122 122 HIS HIS A . n 
A 1 124 TRP 124 123 123 TRP TRP A . n 
A 1 125 ASN 125 124 124 ASN ASN A . n 
A 1 126 SER 126 125 125 SER SER A . n 
A 1 127 ALA 127 126 126 ALA ALA A . n 
A 1 128 LYS 128 127 127 LYS LYS A . n 
A 1 129 TYR 129 128 128 TYR TYR A . n 
A 1 130 SER 130 129 129 SER SER A . n 
A 1 131 SER 131 130 130 SER SER A . n 
A 1 132 LEU 132 131 131 LEU LEU A . n 
A 1 133 ALA 133 132 132 ALA ALA A . n 
A 1 134 GLU 134 133 133 GLU GLU A . n 
A 1 135 ALA 135 134 134 ALA ALA A . n 
A 1 136 ALA 136 135 135 ALA ALA A . n 
A 1 137 SER 137 136 136 SER SER A . n 
A 1 138 LYS 138 137 137 LYS LYS A . n 
A 1 139 ALA 139 138 138 ALA ALA A . n 
A 1 140 ASP 140 139 139 ASP ASP A . n 
A 1 141 GLY 141 140 140 GLY GLY A . n 
A 1 142 LEU 142 141 141 LEU LEU A . n 
A 1 143 ALA 143 142 142 ALA ALA A . n 
A 1 144 VAL 144 143 143 VAL VAL A . n 
A 1 145 ILE 145 144 144 ILE ILE A . n 
A 1 146 GLY 146 145 145 GLY GLY A . n 
A 1 147 VAL 147 146 146 VAL VAL A . n 
A 1 148 LEU 148 147 147 LEU LEU A . n 
A 1 149 MET 149 148 148 MET MET A . n 
A 1 150 LYS 150 149 149 LYS LYS A . n 
A 1 151 VAL 151 150 150 VAL VAL A . n 
A 1 152 GLY 152 151 151 GLY GLY A . n 
A 1 153 GLU 153 152 152 GLU GLU A . n 
A 1 154 ALA 154 153 153 ALA ALA A . n 
A 1 155 ASN 155 154 154 ASN ASN A . n 
A 1 156 PRO 156 155 155 PRO PRO A . n 
A 1 157 LYS 157 156 156 LYS LYS A . n 
A 1 158 LEU 158 157 157 LEU LEU A . n 
A 1 159 GLN 159 158 158 GLN GLN A . n 
A 1 160 LYS 160 159 159 LYS LYS A . n 
A 1 161 VAL 161 160 160 VAL VAL A . n 
A 1 162 LEU 162 161 161 LEU LEU A . n 
A 1 163 ASP 163 162 162 ASP ASP A . n 
A 1 164 ALA 164 163 163 ALA ALA A . n 
A 1 165 LEU 165 164 164 LEU LEU A . n 
A 1 166 GLN 166 165 165 GLN GLN A . n 
A 1 167 ALA 167 166 166 ALA ALA A . n 
A 1 168 ILE 168 167 167 ILE ILE A . n 
A 1 169 LYS 169 168 168 LYS LYS A . n 
A 1 170 THR 170 169 169 THR THR A . n 
A 1 171 LYS 171 170 170 LYS LYS A . n 
A 1 172 GLY 172 171 171 GLY GLY A . n 
A 1 173 LYS 173 172 172 LYS LYS A . n 
A 1 174 ARG 174 173 173 ARG ARG A . n 
A 1 175 ALA 175 174 174 ALA ALA A . n 
A 1 176 PRO 176 175 175 PRO PRO A . n 
A 1 177 PHE 177 176 176 PHE PHE A . n 
A 1 178 THR 178 177 177 THR THR A . n 
A 1 179 ASN 179 178 178 ASN ASN A . n 
A 1 180 PHE 180 179 179 PHE PHE A . n 
A 1 181 ASP 181 180 180 ASP ASP A . n 
A 1 182 PRO 182 181 181 PRO PRO A . n 
A 1 183 SER 183 182 182 SER SER A . n 
A 1 184 THR 184 183 183 THR THR A . n 
A 1 185 LEU 185 184 184 LEU LEU A . n 
A 1 186 LEU 186 185 185 LEU LEU A . n 
A 1 187 PRO 187 186 186 PRO PRO A . n 
A 1 188 SER 188 187 187 SER SER A . n 
A 1 189 SER 189 188 188 SER SER A . n 
A 1 190 LEU 190 189 189 LEU LEU A . n 
A 1 191 ASP 191 190 190 ASP ASP A . n 
A 1 192 PHE 192 191 191 PHE PHE A . n 
A 1 193 TRP 193 192 192 TRP TRP A . n 
A 1 194 THR 194 193 193 THR THR A . n 
A 1 195 TYR 195 194 194 TYR TYR A . n 
A 1 196 PRO 196 195 195 PRO PRO A . n 
A 1 197 GLY 197 196 196 GLY GLY A . n 
A 1 198 SER 198 197 197 SER SER A . n 
A 1 199 LEU 199 198 198 LEU LEU A . n 
A 1 200 THR 200 199 199 THR THR A . n 
A 1 201 HIS 201 200 200 HIS HIS A . n 
A 1 202 PRO 202 201 201 PRO PRO A . n 
A 1 203 PRO 203 202 202 PRO PRO A . n 
A 1 204 LEU 204 203 203 LEU LEU A . n 
A 1 205 TYR 205 204 204 TYR TYR A . n 
A 1 206 GLU 206 205 205 GLU GLU A . n 
A 1 207 SER 207 206 206 SER SER A . n 
A 1 208 VAL 208 207 207 VAL VAL A . n 
A 1 209 THR 209 208 208 THR THR A . n 
A 1 210 TRP 210 209 209 TRP TRP A . n 
A 1 211 ILE 211 210 210 ILE ILE A . n 
A 1 212 ILE 212 211 211 ILE ILE A . n 
A 1 213 CYS 213 212 212 CYS CYS A . n 
A 1 214 LYS 214 213 213 LYS LYS A . n 
A 1 215 GLU 215 214 214 GLU GLU A . n 
A 1 216 SER 216 215 215 SER SER A . n 
A 1 217 ILE 217 216 216 ILE ILE A . n 
A 1 218 SER 218 217 217 SER SER A . n 
A 1 219 VAL 219 218 218 VAL VAL A . n 
A 1 220 SER 220 219 219 SER SER A . n 
A 1 221 SER 221 220 220 SER SER A . n 
A 1 222 GLU 222 221 221 GLU GLU A . n 
A 1 223 GLN 223 222 222 GLN GLN A . n 
A 1 224 LEU 224 223 223 LEU LEU A . n 
A 1 225 ALA 225 224 224 ALA ALA A . n 
A 1 226 GLN 226 225 225 GLN GLN A . n 
A 1 227 PHE 227 226 226 PHE PHE A . n 
A 1 228 ARG 228 227 227 ARG ARG A . n 
A 1 229 SER 229 228 228 SER SER A . n 
A 1 230 LEU 230 229 229 LEU LEU A . n 
A 1 231 LEU 231 230 230 LEU LEU A . n 
A 1 232 SER 232 231 231 SER SER A . n 
A 1 233 ASN 233 232 232 ASN ASN A . n 
A 1 234 VAL 234 233 233 VAL VAL A . n 
A 1 235 GLU 235 234 234 GLU GLU A . n 
A 1 236 GLY 236 235 235 GLY GLY A . n 
A 1 237 ASP 237 236 236 ASP ASP A . n 
A 1 238 ASN 238 237 237 ASN ASN A . n 
A 1 239 ALA 239 238 238 ALA ALA A . n 
A 1 240 VAL 240 239 239 VAL VAL A . n 
A 1 241 PRO 241 240 240 PRO PRO A . n 
A 1 242 MET 242 241 241 MET MET A . n 
A 1 243 GLN 243 242 242 GLN GLN A . n 
A 1 244 HIS 244 243 243 HIS HIS A . n 
A 1 245 ASN 245 244 244 ASN ASN A . n 
A 1 246 ASN 246 245 245 ASN ASN A . n 
A 1 247 ARG 247 246 246 ARG ARG A . n 
A 1 248 PRO 248 247 247 PRO PRO A . n 
A 1 249 THR 249 248 248 THR THR A . n 
A 1 250 GLN 250 249 249 GLN GLN A . n 
A 1 251 PRO 251 250 250 PRO PRO A . n 
A 1 252 LEU 252 251 251 LEU LEU A . n 
A 1 253 LYS 253 252 252 LYS LYS A . n 
A 1 254 GLY 254 253 253 GLY GLY A . n 
A 1 255 ARG 255 254 254 ARG ARG A . n 
A 1 256 THR 256 255 255 THR THR A . n 
A 1 257 VAL 257 256 256 VAL VAL A . n 
A 1 258 ARG 258 257 257 ARG ARG A . n 
A 1 259 ALA 259 258 258 ALA ALA A . n 
A 1 260 SER 260 259 259 SER SER A . n 
A 1 261 PHE 261 260 260 PHE PHE A . n 
B 1 1   MET 1   0   ?   ?   ?   B . n 
B 1 2   ALA 2   1   ?   ?   ?   B . n 
B 1 3   SER 3   2   ?   ?   ?   B . n 
B 1 4   PRO 4   3   3   PRO PRO B . n 
B 1 5   ASP 5   4   4   ASP ASP B . n 
B 1 6   TRP 6   5   5   TRP TRP B . n 
B 1 7   GLY 7   6   6   GLY GLY B . n 
B 1 8   TYR 8   7   7   TYR TYR B . n 
B 1 9   ASP 9   8   8   ASP ASP B . n 
B 1 10  ASP 10  9   9   ASP ASP B . n 
B 1 11  LYS 11  10  10  LYS LYS B . n 
B 1 12  ASN 12  11  11  ASN ASN B . n 
B 1 13  GLY 13  12  12  GLY GLY B . n 
B 1 14  PRO 14  13  13  PRO PRO B . n 
B 1 15  GLU 15  14  14  GLU GLU B . n 
B 1 16  GLN 16  15  15  GLN GLN B . n 
B 1 17  TRP 17  16  16  TRP TRP B . n 
B 1 18  SER 18  17  17  SER SER B . n 
B 1 19  LYS 19  18  18  LYS LYS B . n 
B 1 20  LEU 20  19  19  LEU LEU B . n 
B 1 21  TYR 21  20  20  TYR TYR B . n 
B 1 22  PRO 22  21  21  PRO PRO B . n 
B 1 23  ILE 23  22  22  ILE ILE B . n 
B 1 24  ALA 24  23  23  ALA ALA B . n 
B 1 25  ASN 25  24  24  ASN ASN B . n 
B 1 26  GLY 26  25  25  GLY GLY B . n 
B 1 27  ASN 27  26  26  ASN ASN B . n 
B 1 28  ASN 28  27  27  ASN ASN B . n 
B 1 29  GLN 29  28  28  GLN GLN B . n 
B 1 30  SER 30  29  29  SER SER B . n 
B 1 31  PRO 31  30  30  PRO PRO B . n 
B 1 32  VAL 32  31  31  VAL VAL B . n 
B 1 33  ASP 33  32  32  ASP ASP B . n 
B 1 34  ILE 34  33  33  ILE ILE B . n 
B 1 35  LYS 35  34  34  LYS LYS B . n 
B 1 36  THR 36  35  35  THR THR B . n 
B 1 37  SER 37  36  36  SER SER B . n 
B 1 38  GLU 38  37  37  GLU GLU B . n 
B 1 39  THR 39  38  38  THR THR B . n 
B 1 40  LYS 40  39  39  LYS LYS B . n 
B 1 41  HIS 41  40  40  HIS HIS B . n 
B 1 42  ASP 42  41  41  ASP ASP B . n 
B 1 43  THR 43  42  42  THR THR B . n 
B 1 44  SER 44  43  43  SER SER B . n 
B 1 45  LEU 45  44  44  LEU LEU B . n 
B 1 46  LYS 46  45  45  LYS LYS B . n 
B 1 47  PRO 47  46  46  PRO PRO B . n 
B 1 48  ILE 48  47  47  ILE ILE B . n 
B 1 49  SER 49  48  48  SER SER B . n 
B 1 50  VAL 50  49  49  VAL VAL B . n 
B 1 51  SER 51  50  50  SER SER B . n 
B 1 52  TYR 52  51  51  TYR TYR B . n 
B 1 53  ASN 53  52  52  ASN ASN B . n 
B 1 54  PRO 54  53  53  PRO PRO B . n 
B 1 55  ALA 55  54  54  ALA ALA B . n 
B 1 56  THR 56  55  55  THR THR B . n 
B 1 57  ALA 57  56  56  ALA ALA B . n 
B 1 58  LYS 58  57  57  LYS LYS B . n 
B 1 59  GLU 59  58  58  GLU GLU B . n 
B 1 60  ILE 60  59  59  ILE ILE B . n 
B 1 61  ILE 61  60  60  ILE ILE B . n 
B 1 62  ASN 62  61  61  ASN ASN B . n 
B 1 63  VAL 63  62  62  VAL VAL B . n 
B 1 64  GLY 64  63  63  GLY GLY B . n 
B 1 65  HIS 65  64  64  HIS HIS B . n 
B 1 66  SER 66  65  65  SER SER B . n 
B 1 67  PHE 67  66  66  PHE PHE B . n 
B 1 68  HIS 68  67  67  HIS HIS B . n 
B 1 69  VAL 69  68  68  VAL VAL B . n 
B 1 70  ASN 70  69  69  ASN ASN B . n 
B 1 71  PHE 71  70  70  PHE PHE B . n 
B 1 72  GLU 72  71  71  GLU GLU B . n 
B 1 73  ASP 73  72  72  ASP ASP B . n 
B 1 74  ASN 74  73  73  ASN ASN B . n 
B 1 75  ASP 75  74  74  ASP ASP B . n 
B 1 76  ASN 76  75  75  ASN ASN B . n 
B 1 77  ARG 77  76  76  ARG ARG B . n 
B 1 78  SER 78  77  77  SER SER B . n 
B 1 79  VAL 79  78  78  VAL VAL B . n 
B 1 80  LEU 80  79  79  LEU LEU B . n 
B 1 81  LYS 81  80  80  LYS LYS B . n 
B 1 82  GLY 82  81  81  GLY GLY B . n 
B 1 83  GLY 83  82  82  GLY GLY B . n 
B 1 84  PRO 84  83  83  PRO PRO B . n 
B 1 85  PHE 85  84  84  PHE PHE B . n 
B 1 86  SER 86  85  85  SER SER B . n 
B 1 87  ASP 87  86  86  ASP ASP B . n 
B 1 88  SER 88  87  87  SER SER B . n 
B 1 89  TYR 89  88  88  TYR TYR B . n 
B 1 90  ARG 90  89  89  ARG ARG B . n 
B 1 91  LEU 91  90  90  LEU LEU B . n 
B 1 92  PHE 92  91  91  PHE PHE B . n 
B 1 93  GLN 93  92  92  GLN GLN B . n 
B 1 94  PHE 94  93  93  PHE PHE B . n 
B 1 95  HIS 95  94  94  HIS HIS B . n 
B 1 96  PHE 96  95  95  PHE PHE B . n 
B 1 97  HIS 97  96  96  HIS HIS B . n 
B 1 98  TRP 98  97  97  TRP TRP B . n 
B 1 99  GLY 99  98  98  GLY GLY B . n 
B 1 100 SER 100 99  99  SER SER B . n 
B 1 101 THR 101 100 100 THR THR B . n 
B 1 102 ASN 102 101 101 ASN ASN B . n 
B 1 103 GLU 103 102 102 GLU GLU B . n 
B 1 104 HIS 104 103 103 HIS HIS B . n 
B 1 105 GLY 105 104 104 GLY GLY B . n 
B 1 106 SER 106 105 105 SER SER B . n 
B 1 107 GLU 107 106 106 GLU GLU B . n 
B 1 108 HIS 108 107 107 HIS HIS B . n 
B 1 109 THR 109 108 108 THR THR B . n 
B 1 110 VAL 110 109 109 VAL VAL B . n 
B 1 111 ASP 111 110 110 ASP ASP B . n 
B 1 112 GLY 112 111 111 GLY GLY B . n 
B 1 113 VAL 113 112 112 VAL VAL B . n 
B 1 114 LYS 114 113 113 LYS LYS B . n 
B 1 115 TYR 115 114 114 TYR TYR B . n 
B 1 116 SER 116 115 115 SER SER B . n 
B 1 117 ALA 117 116 116 ALA ALA B . n 
B 1 118 GLU 118 117 117 GLU GLU B . n 
B 1 119 LEU 119 118 118 LEU LEU B . n 
B 1 120 HIS 120 119 119 HIS HIS B . n 
B 1 121 VAL 121 120 120 VAL VAL B . n 
B 1 122 ALA 122 121 121 ALA ALA B . n 
B 1 123 HIS 123 122 122 HIS HIS B . n 
B 1 124 TRP 124 123 123 TRP TRP B . n 
B 1 125 ASN 125 124 124 ASN ASN B . n 
B 1 126 SER 126 125 125 SER SER B . n 
B 1 127 ALA 127 126 126 ALA ALA B . n 
B 1 128 LYS 128 127 127 LYS LYS B . n 
B 1 129 TYR 129 128 128 TYR TYR B . n 
B 1 130 SER 130 129 129 SER SER B . n 
B 1 131 SER 131 130 130 SER SER B . n 
B 1 132 LEU 132 131 131 LEU LEU B . n 
B 1 133 ALA 133 132 132 ALA ALA B . n 
B 1 134 GLU 134 133 133 GLU GLU B . n 
B 1 135 ALA 135 134 134 ALA ALA B . n 
B 1 136 ALA 136 135 135 ALA ALA B . n 
B 1 137 SER 137 136 136 SER SER B . n 
B 1 138 LYS 138 137 137 LYS LYS B . n 
B 1 139 ALA 139 138 138 ALA ALA B . n 
B 1 140 ASP 140 139 139 ASP ASP B . n 
B 1 141 GLY 141 140 140 GLY GLY B . n 
B 1 142 LEU 142 141 141 LEU LEU B . n 
B 1 143 ALA 143 142 142 ALA ALA B . n 
B 1 144 VAL 144 143 143 VAL VAL B . n 
B 1 145 ILE 145 144 144 ILE ILE B . n 
B 1 146 GLY 146 145 145 GLY GLY B . n 
B 1 147 VAL 147 146 146 VAL VAL B . n 
B 1 148 LEU 148 147 147 LEU LEU B . n 
B 1 149 MET 149 148 148 MET MET B . n 
B 1 150 LYS 150 149 149 LYS LYS B . n 
B 1 151 VAL 151 150 150 VAL VAL B . n 
B 1 152 GLY 152 151 151 GLY GLY B . n 
B 1 153 GLU 153 152 152 GLU GLU B . n 
B 1 154 ALA 154 153 153 ALA ALA B . n 
B 1 155 ASN 155 154 154 ASN ASN B . n 
B 1 156 PRO 156 155 155 PRO PRO B . n 
B 1 157 LYS 157 156 156 LYS LYS B . n 
B 1 158 LEU 158 157 157 LEU LEU B . n 
B 1 159 GLN 159 158 158 GLN GLN B . n 
B 1 160 LYS 160 159 159 LYS LYS B . n 
B 1 161 VAL 161 160 160 VAL VAL B . n 
B 1 162 LEU 162 161 161 LEU LEU B . n 
B 1 163 ASP 163 162 162 ASP ASP B . n 
B 1 164 ALA 164 163 163 ALA ALA B . n 
B 1 165 LEU 165 164 164 LEU LEU B . n 
B 1 166 GLN 166 165 165 GLN GLN B . n 
B 1 167 ALA 167 166 166 ALA ALA B . n 
B 1 168 ILE 168 167 167 ILE ILE B . n 
B 1 169 LYS 169 168 168 LYS LYS B . n 
B 1 170 THR 170 169 169 THR THR B . n 
B 1 171 LYS 171 170 170 LYS LYS B . n 
B 1 172 GLY 172 171 171 GLY GLY B . n 
B 1 173 LYS 173 172 172 LYS LYS B . n 
B 1 174 ARG 174 173 173 ARG ARG B . n 
B 1 175 ALA 175 174 174 ALA ALA B . n 
B 1 176 PRO 176 175 175 PRO PRO B . n 
B 1 177 PHE 177 176 176 PHE PHE B . n 
B 1 178 THR 178 177 177 THR THR B . n 
B 1 179 ASN 179 178 178 ASN ASN B . n 
B 1 180 PHE 180 179 179 PHE PHE B . n 
B 1 181 ASP 181 180 180 ASP ASP B . n 
B 1 182 PRO 182 181 181 PRO PRO B . n 
B 1 183 SER 183 182 182 SER SER B . n 
B 1 184 THR 184 183 183 THR THR B . n 
B 1 185 LEU 185 184 184 LEU LEU B . n 
B 1 186 LEU 186 185 185 LEU LEU B . n 
B 1 187 PRO 187 186 186 PRO PRO B . n 
B 1 188 SER 188 187 187 SER SER B . n 
B 1 189 SER 189 188 188 SER SER B . n 
B 1 190 LEU 190 189 189 LEU LEU B . n 
B 1 191 ASP 191 190 190 ASP ASP B . n 
B 1 192 PHE 192 191 191 PHE PHE B . n 
B 1 193 TRP 193 192 192 TRP TRP B . n 
B 1 194 THR 194 193 193 THR THR B . n 
B 1 195 TYR 195 194 194 TYR TYR B . n 
B 1 196 PRO 196 195 195 PRO PRO B . n 
B 1 197 GLY 197 196 196 GLY GLY B . n 
B 1 198 SER 198 197 197 SER SER B . n 
B 1 199 LEU 199 198 198 LEU LEU B . n 
B 1 200 THR 200 199 199 THR THR B . n 
B 1 201 HIS 201 200 200 HIS HIS B . n 
B 1 202 PRO 202 201 201 PRO PRO B . n 
B 1 203 PRO 203 202 202 PRO PRO B . n 
B 1 204 LEU 204 203 203 LEU LEU B . n 
B 1 205 TYR 205 204 204 TYR TYR B . n 
B 1 206 GLU 206 205 205 GLU GLU B . n 
B 1 207 SER 207 206 206 SER SER B . n 
B 1 208 VAL 208 207 207 VAL VAL B . n 
B 1 209 THR 209 208 208 THR THR B . n 
B 1 210 TRP 210 209 209 TRP TRP B . n 
B 1 211 ILE 211 210 210 ILE ILE B . n 
B 1 212 ILE 212 211 211 ILE ILE B . n 
B 1 213 CYS 213 212 212 CYS CYS B . n 
B 1 214 LYS 214 213 213 LYS LYS B . n 
B 1 215 GLU 215 214 214 GLU GLU B . n 
B 1 216 SER 216 215 215 SER SER B . n 
B 1 217 ILE 217 216 216 ILE ILE B . n 
B 1 218 SER 218 217 217 SER SER B . n 
B 1 219 VAL 219 218 218 VAL VAL B . n 
B 1 220 SER 220 219 219 SER SER B . n 
B 1 221 SER 221 220 220 SER SER B . n 
B 1 222 GLU 222 221 221 GLU GLU B . n 
B 1 223 GLN 223 222 222 GLN GLN B . n 
B 1 224 LEU 224 223 223 LEU LEU B . n 
B 1 225 ALA 225 224 224 ALA ALA B . n 
B 1 226 GLN 226 225 225 GLN GLN B . n 
B 1 227 PHE 227 226 226 PHE PHE B . n 
B 1 228 ARG 228 227 227 ARG ARG B . n 
B 1 229 SER 229 228 228 SER SER B . n 
B 1 230 LEU 230 229 229 LEU LEU B . n 
B 1 231 LEU 231 230 230 LEU LEU B . n 
B 1 232 SER 232 231 231 SER SER B . n 
B 1 233 ASN 233 232 232 ASN ASN B . n 
B 1 234 VAL 234 233 233 VAL VAL B . n 
B 1 235 GLU 235 234 234 GLU GLU B . n 
B 1 236 GLY 236 235 235 GLY GLY B . n 
B 1 237 ASP 237 236 236 ASP ASP B . n 
B 1 238 ASN 238 237 237 ASN ASN B . n 
B 1 239 ALA 239 238 238 ALA ALA B . n 
B 1 240 VAL 240 239 239 VAL VAL B . n 
B 1 241 PRO 241 240 240 PRO PRO B . n 
B 1 242 MET 242 241 241 MET MET B . n 
B 1 243 GLN 243 242 242 GLN GLN B . n 
B 1 244 HIS 244 243 243 HIS HIS B . n 
B 1 245 ASN 245 244 244 ASN ASN B . n 
B 1 246 ASN 246 245 245 ASN ASN B . n 
B 1 247 ARG 247 246 246 ARG ARG B . n 
B 1 248 PRO 248 247 247 PRO PRO B . n 
B 1 249 THR 249 248 248 THR THR B . n 
B 1 250 GLN 250 249 249 GLN GLN B . n 
B 1 251 PRO 251 250 250 PRO PRO B . n 
B 1 252 LEU 252 251 251 LEU LEU B . n 
B 1 253 LYS 253 252 252 LYS LYS B . n 
B 1 254 GLY 254 253 253 GLY GLY B . n 
B 1 255 ARG 255 254 254 ARG ARG B . n 
B 1 256 THR 256 255 255 THR THR B . n 
B 1 257 VAL 257 256 256 VAL VAL B . n 
B 1 258 ARG 258 257 257 ARG ARG B . n 
B 1 259 ALA 259 258 258 ALA ALA B . n 
B 1 260 SER 260 259 259 SER SER B . n 
B 1 261 PHE 261 260 260 PHE PHE B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C  2 ZN  1   301 1   ZN  ZN  A . 
D  3 84Z 1   302 1   84Z E2A A . 
E  4 EDO 1   303 1   EDO EDO A . 
F  4 EDO 1   304 2   EDO EDO A . 
G  4 EDO 1   305 3   EDO EDO A . 
H  5 ACT 1   306 2   ACT ACT A . 
I  5 ACT 1   307 3   ACT ACT A . 
J  6 PEG 1   308 2   PEG PEG A . 
K  6 PEG 1   309 4   PEG PEG A . 
L  6 PEG 1   310 13  PEG PEG A . 
M  4 EDO 1   311 4   EDO EDO A . 
N  4 EDO 1   312 6   EDO EDO A . 
O  4 EDO 1   313 8   EDO EDO A . 
P  4 EDO 1   314 10  EDO EDO A . 
Q  4 EDO 1   315 11  EDO EDO A . 
R  2 ZN  1   301 2   ZN  ZN  B . 
S  3 84Z 1   302 2   84Z E2A B . 
T  6 PEG 1   303 5   PEG PEG B . 
U  4 EDO 1   304 6   EDO EDO B . 
V  5 ACT 1   305 1   ACT ACT B . 
W  6 PEG 1   306 6   PEG PEG B . 
X  6 PEG 1   307 8   PEG PEG B . 
Y  6 PEG 1   308 10  PEG PEG B . 
Z  6 PEG 1   309 11  PEG PEG B . 
AA 6 PEG 1   310 12  PEG PEG B . 
BA 4 EDO 1   311 1   EDO EDO B . 
CA 4 EDO 1   312 3   EDO EDO B . 
DA 4 EDO 1   313 7   EDO EDO B . 
EA 4 EDO 1   314 9   EDO EDO B . 
FA 4 EDO 1   315 12  EDO EDO B . 
GA 4 EDO 1   316 13  EDO EDO B . 
HA 4 EDO 1   317 14  EDO EDO B . 
IA 7 HOH 1   401 337 HOH HOH A . 
IA 7 HOH 2   402 728 HOH HOH A . 
IA 7 HOH 3   403 579 HOH HOH A . 
IA 7 HOH 4   404 696 HOH HOH A . 
IA 7 HOH 5   405 164 HOH HOH A . 
IA 7 HOH 6   406 250 HOH HOH A . 
IA 7 HOH 7   407 448 HOH HOH A . 
IA 7 HOH 8   408 658 HOH HOH A . 
IA 7 HOH 9   409 454 HOH HOH A . 
IA 7 HOH 10  410 40  HOH HOH A . 
IA 7 HOH 11  411 397 HOH HOH A . 
IA 7 HOH 12  412 548 HOH HOH A . 
IA 7 HOH 13  413 653 HOH HOH A . 
IA 7 HOH 14  414 420 HOH HOH A . 
IA 7 HOH 15  415 161 HOH HOH A . 
IA 7 HOH 16  416 491 HOH HOH A . 
IA 7 HOH 17  417 319 HOH HOH A . 
IA 7 HOH 18  418 675 HOH HOH A . 
IA 7 HOH 19  419 425 HOH HOH A . 
IA 7 HOH 20  420 508 HOH HOH A . 
IA 7 HOH 21  421 239 HOH HOH A . 
IA 7 HOH 22  422 574 HOH HOH A . 
IA 7 HOH 23  423 583 HOH HOH A . 
IA 7 HOH 24  424 725 HOH HOH A . 
IA 7 HOH 25  425 751 HOH HOH A . 
IA 7 HOH 26  426 13  HOH HOH A . 
IA 7 HOH 27  427 88  HOH HOH A . 
IA 7 HOH 28  428 681 HOH HOH A . 
IA 7 HOH 29  429 480 HOH HOH A . 
IA 7 HOH 30  430 281 HOH HOH A . 
IA 7 HOH 31  431 6   HOH HOH A . 
IA 7 HOH 32  432 47  HOH HOH A . 
IA 7 HOH 33  433 270 HOH HOH A . 
IA 7 HOH 34  434 351 HOH HOH A . 
IA 7 HOH 35  435 642 HOH HOH A . 
IA 7 HOH 36  436 437 HOH HOH A . 
IA 7 HOH 37  437 482 HOH HOH A . 
IA 7 HOH 38  438 206 HOH HOH A . 
IA 7 HOH 39  439 238 HOH HOH A . 
IA 7 HOH 40  440 326 HOH HOH A . 
IA 7 HOH 41  441 154 HOH HOH A . 
IA 7 HOH 42  442 782 HOH HOH A . 
IA 7 HOH 43  443 277 HOH HOH A . 
IA 7 HOH 44  444 137 HOH HOH A . 
IA 7 HOH 45  445 233 HOH HOH A . 
IA 7 HOH 46  446 149 HOH HOH A . 
IA 7 HOH 47  447 755 HOH HOH A . 
IA 7 HOH 48  448 639 HOH HOH A . 
IA 7 HOH 49  449 424 HOH HOH A . 
IA 7 HOH 50  450 195 HOH HOH A . 
IA 7 HOH 51  451 406 HOH HOH A . 
IA 7 HOH 52  452 268 HOH HOH A . 
IA 7 HOH 53  453 802 HOH HOH A . 
IA 7 HOH 54  454 451 HOH HOH A . 
IA 7 HOH 55  455 740 HOH HOH A . 
IA 7 HOH 56  456 580 HOH HOH A . 
IA 7 HOH 57  457 677 HOH HOH A . 
IA 7 HOH 58  458 236 HOH HOH A . 
IA 7 HOH 59  459 120 HOH HOH A . 
IA 7 HOH 60  460 603 HOH HOH A . 
IA 7 HOH 61  461 761 HOH HOH A . 
IA 7 HOH 62  462 316 HOH HOH A . 
IA 7 HOH 63  463 141 HOH HOH A . 
IA 7 HOH 64  464 383 HOH HOH A . 
IA 7 HOH 65  465 354 HOH HOH A . 
IA 7 HOH 66  466 396 HOH HOH A . 
IA 7 HOH 67  467 866 HOH HOH A . 
IA 7 HOH 68  468 231 HOH HOH A . 
IA 7 HOH 69  469 572 HOH HOH A . 
IA 7 HOH 70  470 283 HOH HOH A . 
IA 7 HOH 71  471 505 HOH HOH A . 
IA 7 HOH 72  472 742 HOH HOH A . 
IA 7 HOH 73  473 647 HOH HOH A . 
IA 7 HOH 74  474 484 HOH HOH A . 
IA 7 HOH 75  475 328 HOH HOH A . 
IA 7 HOH 76  476 336 HOH HOH A . 
IA 7 HOH 77  477 684 HOH HOH A . 
IA 7 HOH 78  478 522 HOH HOH A . 
IA 7 HOH 79  479 36  HOH HOH A . 
IA 7 HOH 80  480 16  HOH HOH A . 
IA 7 HOH 81  481 58  HOH HOH A . 
IA 7 HOH 82  482 45  HOH HOH A . 
IA 7 HOH 83  483 103 HOH HOH A . 
IA 7 HOH 84  484 269 HOH HOH A . 
IA 7 HOH 85  485 21  HOH HOH A . 
IA 7 HOH 86  486 27  HOH HOH A . 
IA 7 HOH 87  487 91  HOH HOH A . 
IA 7 HOH 88  488 311 HOH HOH A . 
IA 7 HOH 89  489 74  HOH HOH A . 
IA 7 HOH 90  490 23  HOH HOH A . 
IA 7 HOH 91  491 116 HOH HOH A . 
IA 7 HOH 92  492 11  HOH HOH A . 
IA 7 HOH 93  493 287 HOH HOH A . 
IA 7 HOH 94  494 121 HOH HOH A . 
IA 7 HOH 95  495 719 HOH HOH A . 
IA 7 HOH 96  496 144 HOH HOH A . 
IA 7 HOH 97  497 304 HOH HOH A . 
IA 7 HOH 98  498 348 HOH HOH A . 
IA 7 HOH 99  499 821 HOH HOH A . 
IA 7 HOH 100 500 187 HOH HOH A . 
IA 7 HOH 101 501 258 HOH HOH A . 
IA 7 HOH 102 502 198 HOH HOH A . 
IA 7 HOH 103 503 142 HOH HOH A . 
IA 7 HOH 104 504 210 HOH HOH A . 
IA 7 HOH 105 505 1   HOH HOH A . 
IA 7 HOH 106 506 800 HOH HOH A . 
IA 7 HOH 107 507 81  HOH HOH A . 
IA 7 HOH 108 508 640 HOH HOH A . 
IA 7 HOH 109 509 50  HOH HOH A . 
IA 7 HOH 110 510 222 HOH HOH A . 
IA 7 HOH 111 511 39  HOH HOH A . 
IA 7 HOH 112 512 125 HOH HOH A . 
IA 7 HOH 113 513 98  HOH HOH A . 
IA 7 HOH 114 514 486 HOH HOH A . 
IA 7 HOH 115 515 352 HOH HOH A . 
IA 7 HOH 116 516 54  HOH HOH A . 
IA 7 HOH 117 517 82  HOH HOH A . 
IA 7 HOH 118 518 301 HOH HOH A . 
IA 7 HOH 119 519 108 HOH HOH A . 
IA 7 HOH 120 520 573 HOH HOH A . 
IA 7 HOH 121 521 399 HOH HOH A . 
IA 7 HOH 122 522 816 HOH HOH A . 
IA 7 HOH 123 523 136 HOH HOH A . 
IA 7 HOH 124 524 65  HOH HOH A . 
IA 7 HOH 125 525 391 HOH HOH A . 
IA 7 HOH 126 526 8   HOH HOH A . 
IA 7 HOH 127 527 29  HOH HOH A . 
IA 7 HOH 128 528 375 HOH HOH A . 
IA 7 HOH 129 529 517 HOH HOH A . 
IA 7 HOH 130 530 114 HOH HOH A . 
IA 7 HOH 131 531 70  HOH HOH A . 
IA 7 HOH 132 532 883 HOH HOH A . 
IA 7 HOH 133 533 46  HOH HOH A . 
IA 7 HOH 134 534 75  HOH HOH A . 
IA 7 HOH 135 535 122 HOH HOH A . 
IA 7 HOH 136 536 126 HOH HOH A . 
IA 7 HOH 137 537 111 HOH HOH A . 
IA 7 HOH 138 538 724 HOH HOH A . 
IA 7 HOH 139 539 493 HOH HOH A . 
IA 7 HOH 140 540 764 HOH HOH A . 
IA 7 HOH 141 541 519 HOH HOH A . 
IA 7 HOH 142 542 197 HOH HOH A . 
IA 7 HOH 143 543 756 HOH HOH A . 
IA 7 HOH 144 544 140 HOH HOH A . 
IA 7 HOH 145 545 241 HOH HOH A . 
IA 7 HOH 146 546 415 HOH HOH A . 
IA 7 HOH 147 547 856 HOH HOH A . 
IA 7 HOH 148 548 317 HOH HOH A . 
IA 7 HOH 149 549 118 HOH HOH A . 
IA 7 HOH 150 550 3   HOH HOH A . 
IA 7 HOH 151 551 150 HOH HOH A . 
IA 7 HOH 152 552 622 HOH HOH A . 
IA 7 HOH 153 553 104 HOH HOH A . 
IA 7 HOH 154 554 127 HOH HOH A . 
IA 7 HOH 155 555 209 HOH HOH A . 
IA 7 HOH 156 556 186 HOH HOH A . 
IA 7 HOH 157 557 805 HOH HOH A . 
IA 7 HOH 158 558 14  HOH HOH A . 
IA 7 HOH 159 559 49  HOH HOH A . 
IA 7 HOH 160 560 387 HOH HOH A . 
IA 7 HOH 161 561 64  HOH HOH A . 
IA 7 HOH 162 562 79  HOH HOH A . 
IA 7 HOH 163 563 99  HOH HOH A . 
IA 7 HOH 164 564 260 HOH HOH A . 
IA 7 HOH 165 565 312 HOH HOH A . 
IA 7 HOH 166 566 285 HOH HOH A . 
IA 7 HOH 167 567 165 HOH HOH A . 
IA 7 HOH 168 568 692 HOH HOH A . 
IA 7 HOH 169 569 26  HOH HOH A . 
IA 7 HOH 170 570 61  HOH HOH A . 
IA 7 HOH 171 571 44  HOH HOH A . 
IA 7 HOH 172 572 56  HOH HOH A . 
IA 7 HOH 173 573 279 HOH HOH A . 
IA 7 HOH 174 574 124 HOH HOH A . 
IA 7 HOH 175 575 313 HOH HOH A . 
IA 7 HOH 176 576 288 HOH HOH A . 
IA 7 HOH 177 577 95  HOH HOH A . 
IA 7 HOH 178 578 69  HOH HOH A . 
IA 7 HOH 179 579 48  HOH HOH A . 
IA 7 HOH 180 580 246 HOH HOH A . 
IA 7 HOH 181 581 162 HOH HOH A . 
IA 7 HOH 182 582 178 HOH HOH A . 
IA 7 HOH 183 583 42  HOH HOH A . 
IA 7 HOH 184 584 668 HOH HOH A . 
IA 7 HOH 185 585 322 HOH HOH A . 
IA 7 HOH 186 586 760 HOH HOH A . 
IA 7 HOH 187 587 119 HOH HOH A . 
IA 7 HOH 188 588 292 HOH HOH A . 
IA 7 HOH 189 589 669 HOH HOH A . 
IA 7 HOH 190 590 713 HOH HOH A . 
IA 7 HOH 191 591 749 HOH HOH A . 
IA 7 HOH 192 592 192 HOH HOH A . 
IA 7 HOH 193 593 747 HOH HOH A . 
IA 7 HOH 194 594 706 HOH HOH A . 
IA 7 HOH 195 595 419 HOH HOH A . 
IA 7 HOH 196 596 252 HOH HOH A . 
IA 7 HOH 197 597 237 HOH HOH A . 
IA 7 HOH 198 598 578 HOH HOH A . 
IA 7 HOH 199 599 173 HOH HOH A . 
IA 7 HOH 200 600 558 HOH HOH A . 
IA 7 HOH 201 601 41  HOH HOH A . 
IA 7 HOH 202 602 384 HOH HOH A . 
IA 7 HOH 203 603 201 HOH HOH A . 
IA 7 HOH 204 604 278 HOH HOH A . 
IA 7 HOH 205 605 787 HOH HOH A . 
IA 7 HOH 206 606 475 HOH HOH A . 
IA 7 HOH 207 607 341 HOH HOH A . 
IA 7 HOH 208 608 77  HOH HOH A . 
IA 7 HOH 209 609 736 HOH HOH A . 
IA 7 HOH 210 610 398 HOH HOH A . 
IA 7 HOH 211 611 194 HOH HOH A . 
IA 7 HOH 212 612 490 HOH HOH A . 
IA 7 HOH 213 613 84  HOH HOH A . 
IA 7 HOH 214 614 73  HOH HOH A . 
IA 7 HOH 215 615 157 HOH HOH A . 
IA 7 HOH 216 616 523 HOH HOH A . 
IA 7 HOH 217 617 492 HOH HOH A . 
IA 7 HOH 218 618 110 HOH HOH A . 
IA 7 HOH 219 619 7   HOH HOH A . 
IA 7 HOH 220 620 24  HOH HOH A . 
IA 7 HOH 221 621 189 HOH HOH A . 
IA 7 HOH 222 622 770 HOH HOH A . 
IA 7 HOH 223 623 335 HOH HOH A . 
IA 7 HOH 224 624 170 HOH HOH A . 
IA 7 HOH 225 625 917 HOH HOH A . 
IA 7 HOH 226 626 264 HOH HOH A . 
IA 7 HOH 227 627 182 HOH HOH A . 
IA 7 HOH 228 628 303 HOH HOH A . 
IA 7 HOH 229 629 160 HOH HOH A . 
IA 7 HOH 230 630 123 HOH HOH A . 
IA 7 HOH 231 631 143 HOH HOH A . 
IA 7 HOH 232 632 394 HOH HOH A . 
IA 7 HOH 233 633 132 HOH HOH A . 
IA 7 HOH 234 634 368 HOH HOH A . 
IA 7 HOH 235 635 504 HOH HOH A . 
IA 7 HOH 236 636 347 HOH HOH A . 
IA 7 HOH 237 637 543 HOH HOH A . 
IA 7 HOH 238 638 915 HOH HOH A . 
IA 7 HOH 239 639 291 HOH HOH A . 
IA 7 HOH 240 640 86  HOH HOH A . 
IA 7 HOH 241 641 35  HOH HOH A . 
IA 7 HOH 242 642 455 HOH HOH A . 
IA 7 HOH 243 643 62  HOH HOH A . 
IA 7 HOH 244 644 636 HOH HOH A . 
IA 7 HOH 245 645 788 HOH HOH A . 
IA 7 HOH 246 646 757 HOH HOH A . 
IA 7 HOH 247 647 376 HOH HOH A . 
IA 7 HOH 248 648 513 HOH HOH A . 
IA 7 HOH 249 649 529 HOH HOH A . 
IA 7 HOH 250 650 202 HOH HOH A . 
IA 7 HOH 251 651 204 HOH HOH A . 
IA 7 HOH 252 652 315 HOH HOH A . 
IA 7 HOH 253 653 362 HOH HOH A . 
IA 7 HOH 254 654 661 HOH HOH A . 
IA 7 HOH 255 655 520 HOH HOH A . 
IA 7 HOH 256 656 569 HOH HOH A . 
IA 7 HOH 257 657 190 HOH HOH A . 
IA 7 HOH 258 658 570 HOH HOH A . 
IA 7 HOH 259 659 232 HOH HOH A . 
IA 7 HOH 260 660 378 HOH HOH A . 
IA 7 HOH 261 661 377 HOH HOH A . 
IA 7 HOH 262 662 730 HOH HOH A . 
IA 7 HOH 263 663 93  HOH HOH A . 
IA 7 HOH 264 664 838 HOH HOH A . 
IA 7 HOH 265 665 857 HOH HOH A . 
IA 7 HOH 266 666 679 HOH HOH A . 
IA 7 HOH 267 667 403 HOH HOH A . 
IA 7 HOH 268 668 528 HOH HOH A . 
IA 7 HOH 269 669 92  HOH HOH A . 
IA 7 HOH 270 670 217 HOH HOH A . 
IA 7 HOH 271 671 646 HOH HOH A . 
IA 7 HOH 272 672 697 HOH HOH A . 
IA 7 HOH 273 673 524 HOH HOH A . 
IA 7 HOH 274 674 410 HOH HOH A . 
IA 7 HOH 275 675 25  HOH HOH A . 
IA 7 HOH 276 676 826 HOH HOH A . 
IA 7 HOH 277 677 382 HOH HOH A . 
IA 7 HOH 278 678 37  HOH HOH A . 
IA 7 HOH 279 679 483 HOH HOH A . 
IA 7 HOH 280 680 820 HOH HOH A . 
IA 7 HOH 281 681 625 HOH HOH A . 
IA 7 HOH 282 682 474 HOH HOH A . 
IA 7 HOH 283 683 739 HOH HOH A . 
IA 7 HOH 284 684 256 HOH HOH A . 
IA 7 HOH 285 685 722 HOH HOH A . 
IA 7 HOH 286 686 705 HOH HOH A . 
IA 7 HOH 287 687 819 HOH HOH A . 
IA 7 HOH 288 688 502 HOH HOH A . 
IA 7 HOH 289 689 733 HOH HOH A . 
IA 7 HOH 290 690 644 HOH HOH A . 
IA 7 HOH 291 691 478 HOH HOH A . 
IA 7 HOH 292 692 112 HOH HOH A . 
IA 7 HOH 293 693 83  HOH HOH A . 
IA 7 HOH 294 694 549 HOH HOH A . 
IA 7 HOH 295 695 601 HOH HOH A . 
IA 7 HOH 296 696 576 HOH HOH A . 
IA 7 HOH 297 697 779 HOH HOH A . 
IA 7 HOH 298 698 129 HOH HOH A . 
IA 7 HOH 299 699 479 HOH HOH A . 
IA 7 HOH 300 700 503 HOH HOH A . 
IA 7 HOH 301 701 357 HOH HOH A . 
IA 7 HOH 302 702 485 HOH HOH A . 
IA 7 HOH 303 703 320 HOH HOH A . 
IA 7 HOH 304 704 577 HOH HOH A . 
IA 7 HOH 305 705 185 HOH HOH A . 
IA 7 HOH 306 706 295 HOH HOH A . 
IA 7 HOH 307 707 412 HOH HOH A . 
IA 7 HOH 308 708 562 HOH HOH A . 
IA 7 HOH 309 709 494 HOH HOH A . 
IA 7 HOH 310 710 274 HOH HOH A . 
IA 7 HOH 311 711 545 HOH HOH A . 
IA 7 HOH 312 712 670 HOH HOH A . 
IA 7 HOH 313 713 656 HOH HOH A . 
IA 7 HOH 314 714 66  HOH HOH A . 
IA 7 HOH 315 715 774 HOH HOH A . 
IA 7 HOH 316 716 637 HOH HOH A . 
IA 7 HOH 317 717 436 HOH HOH A . 
IA 7 HOH 318 718 510 HOH HOH A . 
IA 7 HOH 319 719 781 HOH HOH A . 
IA 7 HOH 320 720 506 HOH HOH A . 
IA 7 HOH 321 721 327 HOH HOH A . 
IA 7 HOH 322 722 411 HOH HOH A . 
IA 7 HOH 323 723 758 HOH HOH A . 
IA 7 HOH 324 724 458 HOH HOH A . 
IA 7 HOH 325 725 582 HOH HOH A . 
IA 7 HOH 326 726 379 HOH HOH A . 
IA 7 HOH 327 727 395 HOH HOH A . 
IA 7 HOH 328 728 708 HOH HOH A . 
IA 7 HOH 329 729 916 HOH HOH A . 
IA 7 HOH 330 730 372 HOH HOH A . 
IA 7 HOH 331 731 501 HOH HOH A . 
IA 7 HOH 332 732 867 HOH HOH A . 
IA 7 HOH 333 733 584 HOH HOH A . 
IA 7 HOH 334 734 481 HOH HOH A . 
IA 7 HOH 335 735 349 HOH HOH A . 
IA 7 HOH 336 736 703 HOH HOH A . 
IA 7 HOH 337 737 678 HOH HOH A . 
IA 7 HOH 338 738 456 HOH HOH A . 
IA 7 HOH 339 739 229 HOH HOH A . 
IA 7 HOH 340 740 488 HOH HOH A . 
IA 7 HOH 341 741 631 HOH HOH A . 
IA 7 HOH 342 742 906 HOH HOH A . 
IA 7 HOH 343 743 225 HOH HOH A . 
IA 7 HOH 344 744 76  HOH HOH A . 
IA 7 HOH 345 745 732 HOH HOH A . 
IA 7 HOH 346 746 408 HOH HOH A . 
IA 7 HOH 347 747 346 HOH HOH A . 
IA 7 HOH 348 748 785 HOH HOH A . 
IA 7 HOH 349 749 638 HOH HOH A . 
IA 7 HOH 350 750 784 HOH HOH A . 
IA 7 HOH 351 751 507 HOH HOH A . 
IA 7 HOH 352 752 203 HOH HOH A . 
IA 7 HOH 353 753 380 HOH HOH A . 
IA 7 HOH 354 754 211 HOH HOH A . 
IA 7 HOH 355 755 612 HOH HOH A . 
IA 7 HOH 356 756 771 HOH HOH A . 
IA 7 HOH 357 757 765 HOH HOH A . 
IA 7 HOH 358 758 827 HOH HOH A . 
IA 7 HOH 359 759 704 HOH HOH A . 
IA 7 HOH 360 760 276 HOH HOH A . 
IA 7 HOH 361 761 691 HOH HOH A . 
IA 7 HOH 362 762 318 HOH HOH A . 
IA 7 HOH 363 763 271 HOH HOH A . 
IA 7 HOH 364 764 814 HOH HOH A . 
IA 7 HOH 365 765 257 HOH HOH A . 
IA 7 HOH 366 766 789 HOH HOH A . 
IA 7 HOH 367 767 734 HOH HOH A . 
IA 7 HOH 368 768 447 HOH HOH A . 
IA 7 HOH 369 769 783 HOH HOH A . 
IA 7 HOH 370 770 499 HOH HOH A . 
IA 7 HOH 371 771 667 HOH HOH A . 
IA 7 HOH 372 772 793 HOH HOH A . 
IA 7 HOH 373 773 884 HOH HOH A . 
IA 7 HOH 374 774 606 HOH HOH A . 
IA 7 HOH 375 775 652 HOH HOH A . 
IA 7 HOH 376 776 487 HOH HOH A . 
IA 7 HOH 377 777 849 HOH HOH A . 
IA 7 HOH 378 778 754 HOH HOH A . 
IA 7 HOH 379 779 498 HOH HOH A . 
IA 7 HOH 380 780 441 HOH HOH A . 
IA 7 HOH 381 781 226 HOH HOH A . 
IA 7 HOH 382 782 686 HOH HOH A . 
IA 7 HOH 383 783 645 HOH HOH A . 
IA 7 HOH 384 784 553 HOH HOH A . 
IA 7 HOH 385 785 388 HOH HOH A . 
IA 7 HOH 386 786 575 HOH HOH A . 
IA 7 HOH 387 787 672 HOH HOH A . 
IA 7 HOH 388 788 431 HOH HOH A . 
IA 7 HOH 389 789 750 HOH HOH A . 
IA 7 HOH 390 790 452 HOH HOH A . 
IA 7 HOH 391 791 863 HOH HOH A . 
IA 7 HOH 392 792 416 HOH HOH A . 
IA 7 HOH 393 793 521 HOH HOH A . 
IA 7 HOH 394 794 907 HOH HOH A . 
IA 7 HOH 395 795 413 HOH HOH A . 
IA 7 HOH 396 796 434 HOH HOH A . 
IA 7 HOH 397 797 868 HOH HOH A . 
IA 7 HOH 398 798 810 HOH HOH A . 
IA 7 HOH 399 799 786 HOH HOH A . 
IA 7 HOH 400 800 191 HOH HOH A . 
IA 7 HOH 401 801 332 HOH HOH A . 
IA 7 HOH 402 802 476 HOH HOH A . 
IA 7 HOH 403 803 555 HOH HOH A . 
IA 7 HOH 404 804 825 HOH HOH A . 
IA 7 HOH 405 805 272 HOH HOH A . 
IA 7 HOH 406 806 439 HOH HOH A . 
IA 7 HOH 407 807 768 HOH HOH A . 
IA 7 HOH 408 808 300 HOH HOH A . 
IA 7 HOH 409 809 193 HOH HOH A . 
IA 7 HOH 410 810 221 HOH HOH A . 
IA 7 HOH 411 811 423 HOH HOH A . 
IA 7 HOH 412 812 267 HOH HOH A . 
IA 7 HOH 413 813 538 HOH HOH A . 
IA 7 HOH 414 814 496 HOH HOH A . 
IA 7 HOH 415 815 624 HOH HOH A . 
IA 7 HOH 416 816 512 HOH HOH A . 
IA 7 HOH 417 817 511 HOH HOH A . 
IA 7 HOH 418 818 489 HOH HOH A . 
IA 7 HOH 419 819 700 HOH HOH A . 
IA 7 HOH 420 820 438 HOH HOH A . 
IA 7 HOH 421 821 333 HOH HOH A . 
IA 7 HOH 422 822 446 HOH HOH A . 
IA 7 HOH 423 823 220 HOH HOH A . 
IA 7 HOH 424 824 444 HOH HOH A . 
IA 7 HOH 425 825 687 HOH HOH A . 
IA 7 HOH 426 826 607 HOH HOH A . 
IA 7 HOH 427 827 219 HOH HOH A . 
IA 7 HOH 428 828 345 HOH HOH A . 
IA 7 HOH 429 829 509 HOH HOH A . 
IA 7 HOH 430 830 865 HOH HOH A . 
IA 7 HOH 431 831 551 HOH HOH A . 
IA 7 HOH 432 832 302 HOH HOH A . 
IA 7 HOH 433 833 671 HOH HOH A . 
IA 7 HOH 434 834 659 HOH HOH A . 
IA 7 HOH 435 835 852 HOH HOH A . 
IA 7 HOH 436 836 864 HOH HOH A . 
IA 7 HOH 437 837 766 HOH HOH A . 
IA 7 HOH 438 838 812 HOH HOH A . 
IA 7 HOH 439 839 854 HOH HOH A . 
IA 7 HOH 440 840 571 HOH HOH A . 
IA 7 HOH 441 841 430 HOH HOH A . 
IA 7 HOH 442 842 776 HOH HOH A . 
JA 7 HOH 1   401 623 HOH HOH B . 
JA 7 HOH 2   402 809 HOH HOH B . 
JA 7 HOH 3   403 919 HOH HOH B . 
JA 7 HOH 4   404 255 HOH HOH B . 
JA 7 HOH 5   405 561 HOH HOH B . 
JA 7 HOH 6   406 844 HOH HOH B . 
JA 7 HOH 7   407 843 HOH HOH B . 
JA 7 HOH 8   408 664 HOH HOH B . 
JA 7 HOH 9   409 429 HOH HOH B . 
JA 7 HOH 10  410 718 HOH HOH B . 
JA 7 HOH 11  411 777 HOH HOH B . 
JA 7 HOH 12  412 791 HOH HOH B . 
JA 7 HOH 13  413 227 HOH HOH B . 
JA 7 HOH 14  414 738 HOH HOH B . 
JA 7 HOH 15  415 690 HOH HOH B . 
JA 7 HOH 16  416 635 HOH HOH B . 
JA 7 HOH 17  417 729 HOH HOH B . 
JA 7 HOH 18  418 342 HOH HOH B . 
JA 7 HOH 19  419 340 HOH HOH B . 
JA 7 HOH 20  420 390 HOH HOH B . 
JA 7 HOH 21  421 762 HOH HOH B . 
JA 7 HOH 22  422 133 HOH HOH B . 
JA 7 HOH 23  423 822 HOH HOH B . 
JA 7 HOH 24  424 393 HOH HOH B . 
JA 7 HOH 25  425 205 HOH HOH B . 
JA 7 HOH 26  426 17  HOH HOH B . 
JA 7 HOH 27  427 350 HOH HOH B . 
JA 7 HOH 28  428 833 HOH HOH B . 
JA 7 HOH 29  429 174 HOH HOH B . 
JA 7 HOH 30  430 243 HOH HOH B . 
JA 7 HOH 31  431 567 HOH HOH B . 
JA 7 HOH 32  432 585 HOH HOH B . 
JA 7 HOH 33  433 467 HOH HOH B . 
JA 7 HOH 34  434 798 HOH HOH B . 
JA 7 HOH 35  435 181 HOH HOH B . 
JA 7 HOH 36  436 594 HOH HOH B . 
JA 7 HOH 37  437 183 HOH HOH B . 
JA 7 HOH 38  438 767 HOH HOH B . 
JA 7 HOH 39  439 22  HOH HOH B . 
JA 7 HOH 40  440 78  HOH HOH B . 
JA 7 HOH 41  441 891 HOH HOH B . 
JA 7 HOH 42  442 418 HOH HOH B . 
JA 7 HOH 43  443 251 HOH HOH B . 
JA 7 HOH 44  444 309 HOH HOH B . 
JA 7 HOH 45  445 461 HOH HOH B . 
JA 7 HOH 46  446 212 HOH HOH B . 
JA 7 HOH 47  447 828 HOH HOH B . 
JA 7 HOH 48  448 563 HOH HOH B . 
JA 7 HOH 49  449 428 HOH HOH B . 
JA 7 HOH 50  450 4   HOH HOH B . 
JA 7 HOH 51  451 15  HOH HOH B . 
JA 7 HOH 52  452 240 HOH HOH B . 
JA 7 HOH 53  453 51  HOH HOH B . 
JA 7 HOH 54  454 685 HOH HOH B . 
JA 7 HOH 55  455 565 HOH HOH B . 
JA 7 HOH 56  456 177 HOH HOH B . 
JA 7 HOH 57  457 526 HOH HOH B . 
JA 7 HOH 58  458 71  HOH HOH B . 
JA 7 HOH 59  459 743 HOH HOH B . 
JA 7 HOH 60  460 552 HOH HOH B . 
JA 7 HOH 61  461 156 HOH HOH B . 
JA 7 HOH 62  462 9   HOH HOH B . 
JA 7 HOH 63  463 586 HOH HOH B . 
JA 7 HOH 64  464 33  HOH HOH B . 
JA 7 HOH 65  465 134 HOH HOH B . 
JA 7 HOH 66  466 282 HOH HOH B . 
JA 7 HOH 67  467 735 HOH HOH B . 
JA 7 HOH 68  468 471 HOH HOH B . 
JA 7 HOH 69  469 731 HOH HOH B . 
JA 7 HOH 70  470 286 HOH HOH B . 
JA 7 HOH 71  471 707 HOH HOH B . 
JA 7 HOH 72  472 358 HOH HOH B . 
JA 7 HOH 73  473 228 HOH HOH B . 
JA 7 HOH 74  474 109 HOH HOH B . 
JA 7 HOH 75  475 373 HOH HOH B . 
JA 7 HOH 76  476 848 HOH HOH B . 
JA 7 HOH 77  477 539 HOH HOH B . 
JA 7 HOH 78  478 683 HOH HOH B . 
JA 7 HOH 79  479 43  HOH HOH B . 
JA 7 HOH 80  480 329 HOH HOH B . 
JA 7 HOH 81  481 361 HOH HOH B . 
JA 7 HOH 82  482 273 HOH HOH B . 
JA 7 HOH 83  483 131 HOH HOH B . 
JA 7 HOH 84  484 275 HOH HOH B . 
JA 7 HOH 85  485 5   HOH HOH B . 
JA 7 HOH 86  486 20  HOH HOH B . 
JA 7 HOH 87  487 265 HOH HOH B . 
JA 7 HOH 88  488 199 HOH HOH B . 
JA 7 HOH 89  489 296 HOH HOH B . 
JA 7 HOH 90  490 113 HOH HOH B . 
JA 7 HOH 91  491 188 HOH HOH B . 
JA 7 HOH 92  492 310 HOH HOH B . 
JA 7 HOH 93  493 155 HOH HOH B . 
JA 7 HOH 94  494 32  HOH HOH B . 
JA 7 HOH 95  495 218 HOH HOH B . 
JA 7 HOH 96  496 609 HOH HOH B . 
JA 7 HOH 97  497 145 HOH HOH B . 
JA 7 HOH 98  498 516 HOH HOH B . 
JA 7 HOH 99  499 460 HOH HOH B . 
JA 7 HOH 100 500 905 HOH HOH B . 
JA 7 HOH 101 501 595 HOH HOH B . 
JA 7 HOH 102 502 175 HOH HOH B . 
JA 7 HOH 103 503 59  HOH HOH B . 
JA 7 HOH 104 504 2   HOH HOH B . 
JA 7 HOH 105 505 12  HOH HOH B . 
JA 7 HOH 106 506 298 HOH HOH B . 
JA 7 HOH 107 507 515 HOH HOH B . 
JA 7 HOH 108 508 179 HOH HOH B . 
JA 7 HOH 109 509 401 HOH HOH B . 
JA 7 HOH 110 510 325 HOH HOH B . 
JA 7 HOH 111 511 794 HOH HOH B . 
JA 7 HOH 112 512 598 HOH HOH B . 
JA 7 HOH 113 513 381 HOH HOH B . 
JA 7 HOH 114 514 858 HOH HOH B . 
JA 7 HOH 115 515 147 HOH HOH B . 
JA 7 HOH 116 516 778 HOH HOH B . 
JA 7 HOH 117 517 910 HOH HOH B . 
JA 7 HOH 118 518 176 HOH HOH B . 
JA 7 HOH 119 519 355 HOH HOH B . 
JA 7 HOH 120 520 874 HOH HOH B . 
JA 7 HOH 121 521 230 HOH HOH B . 
JA 7 HOH 122 522 200 HOH HOH B . 
JA 7 HOH 123 523 540 HOH HOH B . 
JA 7 HOH 124 524 163 HOH HOH B . 
JA 7 HOH 125 525 254 HOH HOH B . 
JA 7 HOH 126 526 19  HOH HOH B . 
JA 7 HOH 127 527 525 HOH HOH B . 
JA 7 HOH 128 528 85  HOH HOH B . 
JA 7 HOH 129 529 130 HOH HOH B . 
JA 7 HOH 130 530 159 HOH HOH B . 
JA 7 HOH 131 531 94  HOH HOH B . 
JA 7 HOH 132 532 596 HOH HOH B . 
JA 7 HOH 133 533 464 HOH HOH B . 
JA 7 HOH 134 534 262 HOH HOH B . 
JA 7 HOH 135 535 389 HOH HOH B . 
JA 7 HOH 136 536 31  HOH HOH B . 
JA 7 HOH 137 537 207 HOH HOH B . 
JA 7 HOH 138 538 242 HOH HOH B . 
JA 7 HOH 139 539 356 HOH HOH B . 
JA 7 HOH 140 540 38  HOH HOH B . 
JA 7 HOH 141 541 107 HOH HOH B . 
JA 7 HOH 142 542 90  HOH HOH B . 
JA 7 HOH 143 543 139 HOH HOH B . 
JA 7 HOH 144 544 55  HOH HOH B . 
JA 7 HOH 145 545 80  HOH HOH B . 
JA 7 HOH 146 546 196 HOH HOH B . 
JA 7 HOH 147 547 748 HOH HOH B . 
JA 7 HOH 148 548 405 HOH HOH B . 
JA 7 HOH 149 549 30  HOH HOH B . 
JA 7 HOH 150 550 527 HOH HOH B . 
JA 7 HOH 151 551 138 HOH HOH B . 
JA 7 HOH 152 552 727 HOH HOH B . 
JA 7 HOH 153 553 417 HOH HOH B . 
JA 7 HOH 154 554 153 HOH HOH B . 
JA 7 HOH 155 555 97  HOH HOH B . 
JA 7 HOH 156 556 215 HOH HOH B . 
JA 7 HOH 157 557 402 HOH HOH B . 
JA 7 HOH 158 558 876 HOH HOH B . 
JA 7 HOH 159 559 166 HOH HOH B . 
JA 7 HOH 160 560 53  HOH HOH B . 
JA 7 HOH 161 561 590 HOH HOH B . 
JA 7 HOH 162 562 60  HOH HOH B . 
JA 7 HOH 163 563 52  HOH HOH B . 
JA 7 HOH 164 564 216 HOH HOH B . 
JA 7 HOH 165 565 158 HOH HOH B . 
JA 7 HOH 166 566 253 HOH HOH B . 
JA 7 HOH 167 567 630 HOH HOH B . 
JA 7 HOH 168 568 469 HOH HOH B . 
JA 7 HOH 169 569 600 HOH HOH B . 
JA 7 HOH 170 570 832 HOH HOH B . 
JA 7 HOH 171 571 363 HOH HOH B . 
JA 7 HOH 172 572 360 HOH HOH B . 
JA 7 HOH 173 573 468 HOH HOH B . 
JA 7 HOH 174 574 34  HOH HOH B . 
JA 7 HOH 175 575 89  HOH HOH B . 
JA 7 HOH 176 576 180 HOH HOH B . 
JA 7 HOH 177 577 18  HOH HOH B . 
JA 7 HOH 178 578 610 HOH HOH B . 
JA 7 HOH 179 579 263 HOH HOH B . 
JA 7 HOH 180 580 151 HOH HOH B . 
JA 7 HOH 181 581 544 HOH HOH B . 
JA 7 HOH 182 582 148 HOH HOH B . 
JA 7 HOH 183 583 57  HOH HOH B . 
JA 7 HOH 184 584 171 HOH HOH B . 
JA 7 HOH 185 585 334 HOH HOH B . 
JA 7 HOH 186 586 613 HOH HOH B . 
JA 7 HOH 187 587 629 HOH HOH B . 
JA 7 HOH 188 588 105 HOH HOH B . 
JA 7 HOH 189 589 450 HOH HOH B . 
JA 7 HOH 190 590 831 HOH HOH B . 
JA 7 HOH 191 591 911 HOH HOH B . 
JA 7 HOH 192 592 537 HOH HOH B . 
JA 7 HOH 193 593 353 HOH HOH B . 
JA 7 HOH 194 594 835 HOH HOH B . 
JA 7 HOH 195 595 117 HOH HOH B . 
JA 7 HOH 196 596 294 HOH HOH B . 
JA 7 HOH 197 597 564 HOH HOH B . 
JA 7 HOH 198 598 611 HOH HOH B . 
JA 7 HOH 199 599 449 HOH HOH B . 
JA 7 HOH 200 600 627 HOH HOH B . 
JA 7 HOH 201 601 588 HOH HOH B . 
JA 7 HOH 202 602 214 HOH HOH B . 
JA 7 HOH 203 603 662 HOH HOH B . 
JA 7 HOH 204 604 223 HOH HOH B . 
JA 7 HOH 205 605 566 HOH HOH B . 
JA 7 HOH 206 606 797 HOH HOH B . 
JA 7 HOH 207 607 289 HOH HOH B . 
JA 7 HOH 208 608 259 HOH HOH B . 
JA 7 HOH 209 609 128 HOH HOH B . 
JA 7 HOH 210 610 370 HOH HOH B . 
JA 7 HOH 211 611 904 HOH HOH B . 
JA 7 HOH 212 612 67  HOH HOH B . 
JA 7 HOH 213 613 96  HOH HOH B . 
JA 7 HOH 214 614 633 HOH HOH B . 
JA 7 HOH 215 615 665 HOH HOH B . 
JA 7 HOH 216 616 885 HOH HOH B . 
JA 7 HOH 217 617 146 HOH HOH B . 
JA 7 HOH 218 618 135 HOH HOH B . 
JA 7 HOH 219 619 168 HOH HOH B . 
JA 7 HOH 220 620 593 HOH HOH B . 
JA 7 HOH 221 621 249 HOH HOH B . 
JA 7 HOH 222 622 172 HOH HOH B . 
JA 7 HOH 223 623 331 HOH HOH B . 
JA 7 HOH 224 624 693 HOH HOH B . 
JA 7 HOH 225 625 695 HOH HOH B . 
JA 7 HOH 226 626 213 HOH HOH B . 
JA 7 HOH 227 627 343 HOH HOH B . 
JA 7 HOH 228 628 87  HOH HOH B . 
JA 7 HOH 229 629 63  HOH HOH B . 
JA 7 HOH 230 630 106 HOH HOH B . 
JA 7 HOH 231 631 533 HOH HOH B . 
JA 7 HOH 232 632 641 HOH HOH B . 
JA 7 HOH 233 633 68  HOH HOH B . 
JA 7 HOH 234 634 470 HOH HOH B . 
JA 7 HOH 235 635 72  HOH HOH B . 
JA 7 HOH 236 636 407 HOH HOH B . 
JA 7 HOH 237 637 208 HOH HOH B . 
JA 7 HOH 238 638 10  HOH HOH B . 
JA 7 HOH 239 639 780 HOH HOH B . 
JA 7 HOH 240 640 101 HOH HOH B . 
JA 7 HOH 241 641 709 HOH HOH B . 
JA 7 HOH 242 642 914 HOH HOH B . 
JA 7 HOH 243 643 568 HOH HOH B . 
JA 7 HOH 244 644 801 HOH HOH B . 
JA 7 HOH 245 645 701 HOH HOH B . 
JA 7 HOH 246 646 453 HOH HOH B . 
JA 7 HOH 247 647 457 HOH HOH B . 
JA 7 HOH 248 648 514 HOH HOH B . 
JA 7 HOH 249 649 364 HOH HOH B . 
JA 7 HOH 250 650 550 HOH HOH B . 
JA 7 HOH 251 651 608 HOH HOH B . 
JA 7 HOH 252 652 518 HOH HOH B . 
JA 7 HOH 253 653 689 HOH HOH B . 
JA 7 HOH 254 654 152 HOH HOH B . 
JA 7 HOH 255 655 321 HOH HOH B . 
JA 7 HOH 256 656 818 HOH HOH B . 
JA 7 HOH 257 657 649 HOH HOH B . 
JA 7 HOH 258 658 414 HOH HOH B . 
JA 7 HOH 259 659 823 HOH HOH B . 
JA 7 HOH 260 660 459 HOH HOH B . 
JA 7 HOH 261 661 100 HOH HOH B . 
JA 7 HOH 262 662 803 HOH HOH B . 
JA 7 HOH 263 663 815 HOH HOH B . 
JA 7 HOH 264 664 167 HOH HOH B . 
JA 7 HOH 265 665 532 HOH HOH B . 
JA 7 HOH 266 666 365 HOH HOH B . 
JA 7 HOH 267 667 847 HOH HOH B . 
JA 7 HOH 268 668 604 HOH HOH B . 
JA 7 HOH 269 669 602 HOH HOH B . 
JA 7 HOH 270 670 473 HOH HOH B . 
JA 7 HOH 271 671 392 HOH HOH B . 
JA 7 HOH 272 672 247 HOH HOH B . 
JA 7 HOH 273 673 769 HOH HOH B . 
JA 7 HOH 274 674 871 HOH HOH B . 
JA 7 HOH 275 675 872 HOH HOH B . 
JA 7 HOH 276 676 266 HOH HOH B . 
JA 7 HOH 277 677 799 HOH HOH B . 
JA 7 HOH 278 678 244 HOH HOH B . 
JA 7 HOH 279 679 324 HOH HOH B . 
JA 7 HOH 280 680 903 HOH HOH B . 
JA 7 HOH 281 681 367 HOH HOH B . 
JA 7 HOH 282 682 873 HOH HOH B . 
JA 7 HOH 283 683 759 HOH HOH B . 
JA 7 HOH 284 684 811 HOH HOH B . 
JA 7 HOH 285 685 308 HOH HOH B . 
JA 7 HOH 286 686 909 HOH HOH B . 
JA 7 HOH 287 687 323 HOH HOH B . 
JA 7 HOH 288 688 284 HOH HOH B . 
JA 7 HOH 289 689 385 HOH HOH B . 
JA 7 HOH 290 690 28  HOH HOH B . 
JA 7 HOH 291 691 714 HOH HOH B . 
JA 7 HOH 292 692 712 HOH HOH B . 
JA 7 HOH 293 693 772 HOH HOH B . 
JA 7 HOH 294 694 530 HOH HOH B . 
JA 7 HOH 295 695 763 HOH HOH B . 
JA 7 HOH 296 696 421 HOH HOH B . 
JA 7 HOH 297 697 314 HOH HOH B . 
JA 7 HOH 298 698 426 HOH HOH B . 
JA 7 HOH 299 699 466 HOH HOH B . 
JA 7 HOH 300 700 440 HOH HOH B . 
JA 7 HOH 301 701 605 HOH HOH B . 
JA 7 HOH 302 702 559 HOH HOH B . 
JA 7 HOH 303 703 648 HOH HOH B . 
JA 7 HOH 304 704 717 HOH HOH B . 
JA 7 HOH 305 705 330 HOH HOH B . 
JA 7 HOH 306 706 592 HOH HOH B . 
JA 7 HOH 307 707 443 HOH HOH B . 
JA 7 HOH 308 708 790 HOH HOH B . 
JA 7 HOH 309 709 650 HOH HOH B . 
JA 7 HOH 310 710 293 HOH HOH B . 
JA 7 HOH 311 711 654 HOH HOH B . 
JA 7 HOH 312 712 908 HOH HOH B . 
JA 7 HOH 313 713 404 HOH HOH B . 
JA 7 HOH 314 714 723 HOH HOH B . 
JA 7 HOH 315 715 694 HOH HOH B . 
JA 7 HOH 316 716 344 HOH HOH B . 
JA 7 HOH 317 717 297 HOH HOH B . 
JA 7 HOH 318 718 620 HOH HOH B . 
JA 7 HOH 319 719 248 HOH HOH B . 
JA 7 HOH 320 720 752 HOH HOH B . 
JA 7 HOH 321 721 710 HOH HOH B . 
JA 7 HOH 322 722 280 HOH HOH B . 
JA 7 HOH 323 723 435 HOH HOH B . 
JA 7 HOH 324 724 726 HOH HOH B . 
JA 7 HOH 325 725 746 HOH HOH B . 
JA 7 HOH 326 726 472 HOH HOH B . 
JA 7 HOH 327 727 366 HOH HOH B . 
JA 7 HOH 328 728 744 HOH HOH B . 
JA 7 HOH 329 729 556 HOH HOH B . 
JA 7 HOH 330 730 657 HOH HOH B . 
JA 7 HOH 331 731 775 HOH HOH B . 
JA 7 HOH 332 732 737 HOH HOH B . 
JA 7 HOH 333 733 536 HOH HOH B . 
JA 7 HOH 334 734 386 HOH HOH B . 
JA 7 HOH 335 735 634 HOH HOH B . 
JA 7 HOH 336 736 339 HOH HOH B . 
JA 7 HOH 337 737 557 HOH HOH B . 
JA 7 HOH 338 738 721 HOH HOH B . 
JA 7 HOH 339 739 371 HOH HOH B . 
JA 7 HOH 340 740 720 HOH HOH B . 
JA 7 HOH 341 741 184 HOH HOH B . 
JA 7 HOH 342 742 102 HOH HOH B . 
JA 7 HOH 343 743 804 HOH HOH B . 
JA 7 HOH 344 744 591 HOH HOH B . 
JA 7 HOH 345 745 806 HOH HOH B . 
JA 7 HOH 346 746 655 HOH HOH B . 
JA 7 HOH 347 747 462 HOH HOH B . 
JA 7 HOH 348 748 307 HOH HOH B . 
JA 7 HOH 349 749 531 HOH HOH B . 
JA 7 HOH 350 750 465 HOH HOH B . 
JA 7 HOH 351 751 445 HOH HOH B . 
JA 7 HOH 352 752 869 HOH HOH B . 
JA 7 HOH 353 753 886 HOH HOH B . 
JA 7 HOH 354 754 711 HOH HOH B . 
JA 7 HOH 355 755 374 HOH HOH B . 
JA 7 HOH 356 756 599 HOH HOH B . 
JA 7 HOH 357 757 427 HOH HOH B . 
JA 7 HOH 358 758 359 HOH HOH B . 
JA 7 HOH 359 759 535 HOH HOH B . 
JA 7 HOH 360 760 463 HOH HOH B . 
JA 7 HOH 361 761 824 HOH HOH B . 
JA 7 HOH 362 762 261 HOH HOH B . 
JA 7 HOH 363 763 546 HOH HOH B . 
JA 7 HOH 364 764 792 HOH HOH B . 
JA 7 HOH 365 765 224 HOH HOH B . 
JA 7 HOH 366 766 587 HOH HOH B . 
JA 7 HOH 367 767 663 HOH HOH B . 
JA 7 HOH 368 768 845 HOH HOH B . 
JA 7 HOH 369 769 589 HOH HOH B . 
JA 7 HOH 370 770 621 HOH HOH B . 
JA 7 HOH 371 771 807 HOH HOH B . 
JA 7 HOH 372 772 477 HOH HOH B . 
JA 7 HOH 373 773 235 HOH HOH B . 
JA 7 HOH 374 774 861 HOH HOH B . 
JA 7 HOH 375 775 913 HOH HOH B . 
JA 7 HOH 376 776 918 HOH HOH B . 
JA 7 HOH 377 777 400 HOH HOH B . 
JA 7 HOH 378 778 836 HOH HOH B . 
JA 7 HOH 379 779 534 HOH HOH B . 
JA 7 HOH 380 780 369 HOH HOH B . 
JA 7 HOH 381 781 409 HOH HOH B . 
JA 7 HOH 382 782 547 HOH HOH B . 
JA 7 HOH 383 783 597 HOH HOH B . 
JA 7 HOH 384 784 442 HOH HOH B . 
JA 7 HOH 385 785 895 HOH HOH B . 
JA 7 HOH 386 786 554 HOH HOH B . 
JA 7 HOH 387 787 829 HOH HOH B . 
JA 7 HOH 388 788 433 HOH HOH B . 
JA 7 HOH 389 789 560 HOH HOH B . 
JA 7 HOH 390 790 541 HOH HOH B . 
JA 7 HOH 391 791 666 HOH HOH B . 
JA 7 HOH 392 792 432 HOH HOH B . 
JA 7 HOH 393 793 628 HOH HOH B . 
JA 7 HOH 394 794 880 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 10  ? CG  ? A LYS 11  CG  
2  1 Y 1 A LYS 10  ? CD  ? A LYS 11  CD  
3  1 Y 1 A LYS 10  ? CE  ? A LYS 11  CE  
4  1 Y 1 A LYS 10  ? NZ  ? A LYS 11  NZ  
5  1 Y 1 A LYS 80  ? NZ  ? A LYS 81  NZ  
6  1 Y 1 A LYS 213 ? NZ  ? A LYS 214 NZ  
7  1 Y 1 B LYS 10  ? CG  ? B LYS 11  CG  
8  1 Y 1 B LYS 10  ? CD  ? B LYS 11  CD  
9  1 Y 1 B LYS 10  ? CE  ? B LYS 11  CE  
10 1 Y 1 B LYS 10  ? NZ  ? B LYS 11  NZ  
11 1 Y 1 B LYS 18  ? CD  ? B LYS 19  CD  
12 1 Y 1 B LYS 18  ? CE  ? B LYS 19  CE  
13 1 Y 1 B LYS 18  ? NZ  ? B LYS 19  NZ  
14 1 Y 1 B LEU 19  ? CG  ? B LEU 20  CG  
15 1 Y 1 B LEU 19  ? CD1 ? B LEU 20  CD1 
16 1 Y 1 B LEU 19  ? CD2 ? B LEU 20  CD2 
17 1 Y 1 B LYS 34  ? CE  ? B LYS 35  CE  
18 1 Y 1 B LYS 34  ? NZ  ? B LYS 35  NZ  
19 1 Y 1 B LYS 39  ? CD  ? B LYS 40  CD  
20 1 Y 1 B LYS 39  ? CE  ? B LYS 40  CE  
21 1 Y 1 B LYS 39  ? NZ  ? B LYS 40  NZ  
22 1 Y 1 B LYS 45  ? CD  ? B LYS 46  CD  
23 1 Y 1 B LYS 45  ? CE  ? B LYS 46  CE  
24 1 Y 1 B LYS 45  ? NZ  ? B LYS 46  NZ  
25 1 Y 1 B LYS 80  ? CE  ? B LYS 81  CE  
26 1 Y 1 B LYS 80  ? NZ  ? B LYS 81  NZ  
27 1 Y 1 B LYS 127 ? CE  ? B LYS 128 CE  
28 1 Y 1 B LYS 127 ? NZ  ? B LYS 128 NZ  
29 1 N 1 A PEG 309 ? C1  ? K PEG 1   C1  
30 1 N 1 A PEG 309 ? O1  ? K PEG 1   O1  
31 1 N 1 A PEG 309 ? C2  ? K PEG 1   C2  
# 
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 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0189 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7Q0D 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.039 
_cell.length_a_esd                 ? 
_cell.length_b                     73.235 
_cell.length_b_esd                 ? 
_cell.length_c                     120.473 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
# 
_symmetry.entry_id                         7Q0D 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   7Q0D 
_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            2.37 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         48.03 
_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_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            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'Crystallization buffer: 0.1 M Tris-HCl (pH 8.5), 0.2 M ammonium acetate and 24% PEG4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-06-26 
_diffrn_detector.pdbx_frequency               ? 
# 
_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   1.03320 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.03320 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       7Q0D 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.243 
_reflns.d_resolution_low                               62.039 
_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                                     151876 
_reflns.number_obs                                     151876 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.300 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.900 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.075 
_reflns.pdbx_netI_over_av_sigmaI                       3.200 
_reflns.pdbx_netI_over_sigmaI                          22.000 
_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                                0.083 
_reflns.pdbx_Rpim_I_all                                0.022 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1961733 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_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_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.243 1.310  ? 3.800 ? ? ? ? 19941 89.600 ? ? ? ? 0.194 ? ? ? ? ? ? ? ? 11.000 0.194 ? ? ? 0.216 0.063 ? 1  1 ? ? ? ? ? ? ? ? ? ? 
? 
1.310 1.390  ? 4.400 ? ? ? ? 21140 99.900 ? ? ? ? 0.164 ? ? ? ? ? ? ? ? 13.100 0.164 ? ? ? 0.181 0.049 ? 2  1 ? ? ? ? ? ? ? ? ? ? 
? 
1.390 1.490  ? 5.300 ? ? ? ? 19900 99.900 ? ? ? ? 0.131 ? ? ? ? ? ? ? ? 12.900 0.131 ? ? ? 0.146 0.040 ? 3  1 ? ? ? ? ? ? ? ? ? ? 
? 
1.490 1.600  ? 6.300 ? ? ? ? 18548 99.800 ? ? ? ? 0.103 ? ? ? ? ? ? ? ? 13.300 0.103 ? ? ? 0.116 0.031 ? 4  1 ? ? ? ? ? ? ? ? ? ? 
? 
1.600 1.760  ? 6.900 ? ? ? ? 17072 99.800 ? ? ? ? 0.087 ? ? ? ? ? ? ? ? 13.100 0.087 ? ? ? 0.099 0.027 ? 5  1 ? ? ? ? ? ? ? ? ? ? 
? 
1.760 1.970  ? 7.500 ? ? ? ? 15522 99.800 ? ? ? ? 0.075 ? ? ? ? ? ? ? ? 13.600 0.075 ? ? ? 0.085 0.023 ? 6  1 ? ? ? ? ? ? ? ? ? ? 
? 
1.970 2.270  ? 7.700 ? ? ? ? 13714 99.600 ? ? ? ? 0.069 ? ? ? ? ? ? ? ? 13.300 0.069 ? ? ? 0.077 0.021 ? 7  1 ? ? ? ? ? ? ? ? ? ? 
? 
2.270 2.780  ? 8.000 ? ? ? ? 11663 99.800 ? ? ? ? 0.067 ? ? ? ? ? ? ? ? 13.600 0.067 ? ? ? 0.074 0.020 ? 8  1 ? ? ? ? ? ? ? ? ? ? 
? 
2.780 3.930  ? 6.700 ? ? ? ? 9140  99.700 ? ? ? ? 0.068 ? ? ? ? ? ? ? ? 13.300 0.068 ? ? ? 0.075 0.020 ? 9  1 ? ? ? ? ? ? ? ? ? ? 
? 
3.930 62.039 ? 5.900 ? ? ? ? 5236  99.600 ? ? ? ? 0.075 ? ? ? ? ? ? ? ? 12.800 0.075 ? ? ? 0.082 0.023 ? 10 1 ? ? ? ? ? ? ? ? ? ? 
? 
# 
_refine.aniso_B[1][1]                            0.0600 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            0.0200 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            -0.0800 
_refine.B_iso_max                                691.130 
_refine.B_iso_mean                               17.8930 
_refine.B_iso_min                                5.730 
_refine.correlation_coeff_Fo_to_Fc               0.9760 
_refine.correlation_coeff_Fo_to_Fc_free          0.9690 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_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                                 7Q0D 
_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                            1.2400 
_refine.ls_d_res_low                             55.1600 
_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                     136749 
_refine.ls_number_reflns_R_free                  15031 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.2800 
_refine.ls_percent_reflns_R_free                 9.9000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1335 
_refine.ls_R_factor_R_free                       0.1577 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1309 
_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                    MASK 
_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                          0.000 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      1CAB 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0430 
_refine.pdbx_overall_ESU_R_Free                  0.0410 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_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                 ? 
_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                            ? 
_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                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.2400 
_refine_hist.d_res_low                        55.1600 
_refine_hist.number_atoms_solvent             869 
_refine_hist.number_atoms_total               5121 
_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       516 
_refine_hist.pdbx_B_iso_mean_ligand           30.05 
_refine_hist.pdbx_B_iso_mean_solvent          32.01 
_refine_hist.pdbx_number_atoms_protein        4018 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         234 
_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' ? 0.030  0.019  4766 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.420  1.968  6505 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.968  5.000  599  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 37.229 24.907 214  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.775 15.000 708  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 21.000 15.000 16   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.171  0.200  665  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.017  0.021  3777 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 9.393  3.000  4766 ? r_rigid_bond_restr     ? ? 
'X-RAY DIFFRACTION' ? 28.336 5.000  505  ? r_sphericity_free      ? ? 
'X-RAY DIFFRACTION' ? 20.357 5.000  4992 ? r_sphericity_bonded    ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.2430 
_refine_ls_shell.d_res_low                        1.2750 
_refine_ls_shell.number_reflns_all                8982 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             921 
_refine_ls_shell.number_reflns_R_work             8061 
_refine_ls_shell.percent_reflns_obs               79.8200 
_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                  0.1630 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1280 
_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   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     7Q0D 
_struct.title                        
'Human carbonic anhydrase I in complex with Methyl 2-(benzenesulfonyl)-4-chloro-5-sulfamoylbenzoate' 
_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        7Q0D 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor complex, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 4 ? 
G  N N 4 ? 
H  N N 5 ? 
I  N N 5 ? 
J  N N 6 ? 
K  N N 6 ? 
L  N N 6 ? 
M  N N 4 ? 
N  N N 4 ? 
O  N N 4 ? 
P  N N 4 ? 
Q  N N 4 ? 
R  N N 2 ? 
S  N N 3 ? 
T  N N 6 ? 
U  N N 4 ? 
V  N N 5 ? 
W  N N 6 ? 
X  N N 6 ? 
Y  N N 6 ? 
Z  N N 6 ? 
AA N N 6 ? 
BA N N 4 ? 
CA N N 4 ? 
DA N N 4 ? 
EA N N 4 ? 
FA N N 4 ? 
GA N N 4 ? 
HA N N 4 ? 
IA N N 7 ? 
JA N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH1_HUMAN 
_struct_ref.pdbx_db_accession          P00915 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVL
KGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQK
VLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAV
PMQHNNRPTQPLKGRTVRASF
;
_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 7Q0D A 1 ? 261 ? P00915 1 ? 261 ? 0 260 
2 1 7Q0D B 1 ? 261 ? P00915 1 ? 261 ? 0 260 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,IA             
2 1 B,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,JA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 16  ? LEU A 20  ? GLN A 15  LEU A 19  5 ? 5  
HELX_P HELX_P2  AA2 TYR A 21  ? GLY A 26  ? TYR A 20  GLY A 25  5 ? 6  
HELX_P HELX_P3  AA3 LYS A 35  ? THR A 39  ? LYS A 34  THR A 38  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ALA A 55  ? ASN A 52  ALA A 54  5 ? 3  
HELX_P HELX_P5  AA5 SER A 131 ? ALA A 136 ? SER A 130 ALA A 135 1 ? 6  
HELX_P HELX_P6  AA6 ASN A 155 ? LYS A 157 ? ASN A 154 LYS A 156 5 ? 3  
HELX_P HELX_P7  AA7 LEU A 158 ? LEU A 165 ? LEU A 157 LEU A 164 1 ? 8  
HELX_P HELX_P8  AA8 GLN A 166 ? ILE A 168 ? GLN A 165 ILE A 167 5 ? 3  
HELX_P HELX_P9  AA9 ASP A 181 ? LEU A 186 ? ASP A 180 LEU A 185 5 ? 6  
HELX_P HELX_P10 AB1 SER A 220 ? SER A 229 ? SER A 219 SER A 228 1 ? 10 
HELX_P HELX_P11 AB2 GLN B 16  ? LEU B 20  ? GLN B 15  LEU B 19  5 ? 5  
HELX_P HELX_P12 AB3 TYR B 21  ? GLY B 26  ? TYR B 20  GLY B 25  5 ? 6  
HELX_P HELX_P13 AB4 LYS B 35  ? THR B 39  ? LYS B 34  THR B 38  5 ? 5  
HELX_P HELX_P14 AB5 ASN B 53  ? ALA B 55  ? ASN B 52  ALA B 54  5 ? 3  
HELX_P HELX_P15 AB6 SER B 131 ? ALA B 136 ? SER B 130 ALA B 135 1 ? 6  
HELX_P HELX_P16 AB7 ASN B 155 ? LYS B 157 ? ASN B 154 LYS B 156 5 ? 3  
HELX_P HELX_P17 AB8 LEU B 158 ? LEU B 165 ? LEU B 157 LEU B 164 1 ? 8  
HELX_P HELX_P18 AB9 GLN B 166 ? ILE B 168 ? GLN B 165 ILE B 167 5 ? 3  
HELX_P HELX_P19 AC1 ASP B 181 ? LEU B 186 ? ASP B 180 LEU B 185 5 ? 6  
HELX_P HELX_P20 AC2 SER B 220 ? SER B 229 ? SER B 219 SER B 228 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale none ? B PHE 92  CZ  B ? ? 1_555 S 84Z . C15 B ? B PHE 91  B 84Z 302 1_555 ? ? ? ? ? ? ? 1.270 ? ? 
metalc1  metalc ?    ? A HIS 95  NE2 ? ? ? 1_555 C ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.974 ? ? 
metalc2  metalc ?    ? A HIS 97  NE2 ? ? ? 1_555 C ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.018 ? ? 
metalc3  metalc ?    ? A HIS 120 ND1 ? ? ? 1_555 C ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc4  metalc ?    ? C ZN  .   ZN  ? ? ? 1_555 D 84Z . N10 A ? A ZN  301 A 84Z 302 1_555 ? ? ? ? ? ? ? 1.911 ? ? 
metalc5  metalc ?    ? C ZN  .   ZN  ? ? ? 1_555 D 84Z . N10 B ? A ZN  301 A 84Z 302 1_555 ? ? ? ? ? ? ? 1.949 ? ? 
metalc6  metalc ?    ? B HIS 95  NE2 ? ? ? 1_555 R ZN  . ZN  ? ? B HIS 94  B ZN  301 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
metalc7  metalc ?    ? B HIS 97  NE2 ? ? ? 1_555 R ZN  . ZN  ? ? B HIS 96  B ZN  301 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc8  metalc ?    ? B HIS 120 ND1 ? ? ? 1_555 R ZN  . ZN  ? ? B HIS 119 B ZN  301 1_555 ? ? ? ? ? ? ? 2.020 ? ? 
metalc9  metalc ?    ? R ZN  .   ZN  ? ? ? 1_555 S 84Z . N10 A ? B ZN  301 B 84Z 302 1_555 ? ? ? ? ? ? ? 1.888 ? ? 
metalc10 metalc ?    ? R ZN  .   ZN  ? ? ? 1_555 S 84Z . N10 B ? B ZN  301 B 84Z 302 1_555 ? ? ? ? ? ? ? 1.864 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 95  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 97  ? A HIS 96  ? 1_555 105.8 ? 
2  NE2 ? A HIS 95  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 120 ? A HIS 119 ? 1_555 109.9 ? 
3  NE2 ? A HIS 97  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 120 ? A HIS 119 ? 1_555 97.2  ? 
4  NE2 ? A HIS 95  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N10 A D 84Z .   ? A 84Z 302 ? 1_555 109.6 ? 
5  NE2 ? A HIS 97  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N10 A D 84Z .   ? A 84Z 302 ? 1_555 112.7 ? 
6  ND1 ? A HIS 120 ? A HIS 119 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N10 A D 84Z .   ? A 84Z 302 ? 1_555 120.2 ? 
7  NE2 ? A HIS 95  ? A HIS 94  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N10 B D 84Z .   ? A 84Z 302 ? 1_555 111.6 ? 
8  NE2 ? A HIS 97  ? A HIS 96  ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N10 B D 84Z .   ? A 84Z 302 ? 1_555 114.1 ? 
9  ND1 ? A HIS 120 ? A HIS 119 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N10 B D 84Z .   ? A 84Z 302 ? 1_555 116.9 ? 
10 N10 A D 84Z .   ? A 84Z 302 ? 1_555 ZN ? C ZN . ? A ZN 301 ? 1_555 N10 B D 84Z .   ? A 84Z 302 ? 1_555 3.3   ? 
11 NE2 ? B HIS 95  ? B HIS 94  ? 1_555 ZN ? R ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 97  ? B HIS 96  ? 1_555 105.5 ? 
12 NE2 ? B HIS 95  ? B HIS 94  ? 1_555 ZN ? R ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 120 ? B HIS 119 ? 1_555 109.8 ? 
13 NE2 ? B HIS 97  ? B HIS 96  ? 1_555 ZN ? R ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 120 ? B HIS 119 ? 1_555 97.6  ? 
14 NE2 ? B HIS 95  ? B HIS 94  ? 1_555 ZN ? R ZN . ? B ZN 301 ? 1_555 N10 A S 84Z .   ? B 84Z 302 ? 1_555 113.0 ? 
15 NE2 ? B HIS 97  ? B HIS 96  ? 1_555 ZN ? R ZN . ? B ZN 301 ? 1_555 N10 A S 84Z .   ? B 84Z 302 ? 1_555 108.8 ? 
16 ND1 ? B HIS 120 ? B HIS 119 ? 1_555 ZN ? R ZN . ? B ZN 301 ? 1_555 N10 A S 84Z .   ? B 84Z 302 ? 1_555 120.0 ? 
17 NE2 ? B HIS 95  ? B HIS 94  ? 1_555 ZN ? R ZN . ? B ZN 301 ? 1_555 N10 B S 84Z .   ? B 84Z 302 ? 1_555 112.6 ? 
18 NE2 ? B HIS 97  ? B HIS 96  ? 1_555 ZN ? R ZN . ? B ZN 301 ? 1_555 N10 B S 84Z .   ? B 84Z 302 ? 1_555 112.1 ? 
19 ND1 ? B HIS 120 ? B HIS 119 ? 1_555 ZN ? R ZN . ? B ZN 301 ? 1_555 N10 B S 84Z .   ? B 84Z 302 ? 1_555 117.7 ? 
20 N10 A S 84Z .   ? B 84Z 302 ? 1_555 ZN ? R ZN . ? B ZN 301 ? 1_555 N10 B S 84Z .   ? B 84Z 302 ? 1_555 3.5   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 30  A . ? SER 29  A PRO 31  A ? PRO 30  A 1 0.72  
2 PRO 202 A . ? PRO 201 A PRO 203 A ? PRO 202 A 1 17.00 
3 SER 30  B . ? SER 29  B PRO 31  B ? PRO 30  B 1 0.98  
4 PRO 202 B . ? PRO 201 B PRO 203 B ? PRO 202 B 1 15.36 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? 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  ASP A 33  ? ILE A 34  ? ASP A 32  ILE A 33  
AA1 2  THR A 109 ? VAL A 110 ? THR A 108 VAL A 109 
AA2 1  LYS A 40  ? HIS A 41  ? LYS A 39  HIS A 40  
AA2 2  ARG A 258 ? ALA A 259 ? ARG A 257 ALA A 258 
AA2 3  PHE A 192 ? GLY A 197 ? PHE A 191 GLY A 196 
AA2 4  VAL A 208 ? CYS A 213 ? VAL A 207 CYS A 212 
AA2 5  LEU A 142 ? VAL A 151 ? LEU A 141 VAL A 150 
AA2 6  ALA A 117 ? TRP A 124 ? ALA A 116 TRP A 123 
AA2 7  TYR A 89  ? TRP A 98  ? TYR A 88  TRP A 97  
AA2 8  PHE A 67  ? PHE A 71  ? PHE A 66  PHE A 70  
AA2 9  ALA A 57  ? ASN A 62  ? ALA A 56  ASN A 61  
AA2 10 ARG A 174 ? PRO A 176 ? ARG A 173 PRO A 175 
AA3 1  ILE A 48  ? SER A 51  ? ILE A 47  SER A 50  
AA3 2  VAL A 79  ? GLY A 82  ? VAL A 78  GLY A 81  
AA3 3  TYR A 89  ? TRP A 98  ? TYR A 88  TRP A 97  
AA3 4  ALA A 117 ? TRP A 124 ? ALA A 116 TRP A 123 
AA3 5  LEU A 142 ? VAL A 151 ? LEU A 141 VAL A 150 
AA3 6  ILE A 217 ? VAL A 219 ? ILE A 216 VAL A 218 
AA4 1  ASP B 33  ? ILE B 34  ? ASP B 32  ILE B 33  
AA4 2  THR B 109 ? VAL B 110 ? THR B 108 VAL B 109 
AA5 1  LYS B 40  ? HIS B 41  ? LYS B 39  HIS B 40  
AA5 2  ARG B 258 ? ALA B 259 ? ARG B 257 ALA B 258 
AA5 3  PHE B 192 ? GLY B 197 ? PHE B 191 GLY B 196 
AA5 4  VAL B 208 ? CYS B 213 ? VAL B 207 CYS B 212 
AA5 5  LEU B 142 ? VAL B 151 ? LEU B 141 VAL B 150 
AA5 6  ALA B 117 ? ASN B 125 ? ALA B 116 ASN B 124 
AA5 7  TYR B 89  ? TRP B 98  ? TYR B 88  TRP B 97  
AA5 8  PHE B 67  ? PHE B 71  ? PHE B 66  PHE B 70  
AA5 9  ALA B 57  ? ASN B 62  ? ALA B 56  ASN B 61  
AA5 10 ARG B 174 ? PRO B 176 ? ARG B 173 PRO B 175 
AA6 1  ILE B 48  ? SER B 51  ? ILE B 47  SER B 50  
AA6 2  VAL B 79  ? GLY B 82  ? VAL B 78  GLY B 81  
AA6 3  TYR B 89  ? TRP B 98  ? TYR B 88  TRP B 97  
AA6 4  ALA B 117 ? ASN B 125 ? ALA B 116 ASN B 124 
AA6 5  LEU B 142 ? VAL B 151 ? LEU B 141 VAL B 150 
AA6 6  ILE B 217 ? VAL B 219 ? ILE B 216 VAL B 218 
# 
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 ILE A 34  ? N ILE A 33  O THR A 109 ? O THR A 108 
AA2 1 2  N LYS A 40  ? N LYS A 39  O ALA A 259 ? O ALA A 258 
AA2 2 3  O ARG A 258 ? O ARG A 257 N THR A 194 ? N THR A 193 
AA2 3 4  N GLY A 197 ? N GLY A 196 O VAL A 208 ? O VAL A 207 
AA2 4 5  O ILE A 211 ? O ILE A 210 N GLY A 146 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 144 N VAL A 121 ? N VAL A 120 
AA2 6 7  O HIS A 120 ? O HIS A 119 N HIS A 95  ? N HIS A 94  
AA2 7 8  O PHE A 94  ? O PHE A 93  N VAL A 69  ? N VAL A 68  
AA2 8 9  O ASN A 70  ? O ASN A 69  N GLU A 59  ? N GLU A 58  
AA2 9 10 N ILE A 60  ? N ILE A 59  O ALA A 175 ? O ALA A 174 
AA3 1 2  N SER A 51  ? N SER A 50  O VAL A 79  ? O VAL A 78  
AA3 2 3  N LEU A 80  ? N LEU A 79  O TYR A 89  ? O TYR A 88  
AA3 3 4  N HIS A 95  ? N HIS A 94  O HIS A 120 ? O HIS A 119 
AA3 4 5  N VAL A 121 ? N VAL A 120 O ILE A 145 ? O ILE A 144 
AA3 5 6  N LYS A 150 ? N LYS A 149 O ILE A 217 ? O ILE A 216 
AA4 1 2  N ILE B 34  ? N ILE B 33  O THR B 109 ? O THR B 108 
AA5 1 2  N LYS B 40  ? N LYS B 39  O ALA B 259 ? O ALA B 258 
AA5 2 3  O ARG B 258 ? O ARG B 257 N THR B 194 ? N THR B 193 
AA5 3 4  N GLY B 197 ? N GLY B 196 O VAL B 208 ? O VAL B 207 
AA5 4 5  O ILE B 211 ? O ILE B 210 N GLY B 146 ? N GLY B 145 
AA5 5 6  O MET B 149 ? O MET B 148 N ALA B 117 ? N ALA B 116 
AA5 6 7  O HIS B 120 ? O HIS B 119 N HIS B 95  ? N HIS B 94  
AA5 7 8  O PHE B 94  ? O PHE B 93  N VAL B 69  ? N VAL B 68  
AA5 8 9  O ASN B 70  ? O ASN B 69  N GLU B 59  ? N GLU B 58  
AA5 9 10 N ILE B 60  ? N ILE B 59  O ALA B 175 ? O ALA B 174 
AA6 1 2  N SER B 49  ? N SER B 48  O LYS B 81  ? O LYS B 80  
AA6 2 3  N LEU B 80  ? N LEU B 79  O TYR B 89  ? O TYR B 88  
AA6 3 4  N HIS B 95  ? N HIS B 94  O HIS B 120 ? O HIS B 119 
AA6 4 5  N ALA B 117 ? N ALA B 116 O MET B 149 ? O MET B 148 
AA6 5 6  N LYS B 150 ? N LYS B 149 O ILE B 217 ? O ILE B 216 
# 
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 OH  A TYR 114 ? A O  A ACT 307 ? ? 1.85 
2 1 ND2 B ASN 237 ? B O  B HOH 401 ? ? 1.97 
3 1 OD1 B ASN 237 ? B O  B HOH 402 ? ? 2.06 
4 1 O1  B PEG 310 ? ? O  B HOH 403 ? ? 2.09 
5 1 O2  B EDO 316 ? ? O  B HOH 404 ? ? 2.09 
6 1 CE  A LYS 156 ? A O1 A PEG 310 ? ? 2.11 
7 1 O2  A EDO 312 ? ? O  A HOH 401 ? ? 2.14 
8 1 CE2 A PHE 260 ? A O2 A EDO 313 ? ? 2.17 
# 
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 OXT A PHE 260 ? ? 1_555 NZ B LYS 149 ? ? 2_655 1.84 
2 1 O   A HOH 830 ? ? 1_555 O  B HOH 402 ? ? 1_455 2.16 
3 1 CG  B ASN 237 ? A 1_555 O  A HOH 830 ? ? 1_655 2.16 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG A HIS 103 ? ? CD2 A HIS 103 ? ? 1.423 1.354 0.069 0.009 N 
2 1 CD A GLN 242 ? B OE1 A GLN 242 ? B 1.415 1.235 0.180 0.022 N 
3 1 C  A PHE 260 ? B OXT A PHE 260 ? ? 2.374 1.229 1.145 0.019 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 O A ASP 72  ? B C  A ASP 72  ? B N  A ASN 73  ? ? 132.78 122.70 10.08  1.60 Y 
2 1 N B SER 105 ? ? CA B SER 105 ? ? CB B SER 105 ? ? 123.21 110.50 12.71  1.50 N 
3 1 N B SER 105 ? ? CA B SER 105 ? ? C  B SER 105 ? ? 90.10  111.00 -20.90 2.70 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 27  ? B -141.32 50.46   
2  1 LYS A 57  ? ? -122.74 -58.51  
3  1 LYS A 57  ? ? -122.74 -60.56  
4  1 SER A 65  ? ? -163.85 -169.89 
5  1 ASP A 72  ? A -114.99 76.21   
6  1 ASN A 73  ? ? -144.55 -22.77  
7  1 ASN A 75  ? ? -95.50  34.05   
8  1 GLU A 106 ? ? -97.43  -63.24  
9  1 ASN A 244 ? ? -158.41 30.56   
10 1 ASP B 4   ? ? 72.39   -120.72 
11 1 TRP B 5   ? ? -47.26  152.90  
12 1 ASN B 11  ? ? -140.13 13.75   
13 1 LYS B 57  ? B -122.74 -58.35  
14 1 SER B 65  ? ? -163.87 -168.81 
15 1 ASN B 75  ? ? -97.77  32.91   
16 1 PHE B 91  ? B -139.55 -30.52  
17 1 ASN B 244 ? ? -158.78 32.10   
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             ASP 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              72 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             A 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -13.88 
# 
_pdbx_entry_details.entry_id                 7Q0D 
_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         ? 
# 
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 0 ? A MET 1 
2 1 Y 1 A ALA 1 ? A ALA 2 
3 1 Y 1 A SER 2 ? A SER 3 
4 1 Y 1 B MET 0 ? B MET 1 
5 1 Y 1 B ALA 1 ? B ALA 2 
6 1 Y 1 B SER 2 ? B SER 3 
# 
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 
84Z O18  O  N N 1   
84Z S16  S  N N 2   
84Z O17  O  N N 3   
84Z C19  C  Y N 4   
84Z C24  C  Y N 5   
84Z C23  C  Y N 6   
84Z C22  C  Y N 7   
84Z C21  C  Y N 8   
84Z C20  C  Y N 9   
84Z C3   C  Y N 10  
84Z C2   C  Y N 11  
84Z C4   C  Y N 12  
84Z C12  C  N N 13  
84Z O14  O  N N 14  
84Z C15  C  N N 15  
84Z O13  O  N N 16  
84Z C5   C  Y N 17  
84Z C6   C  Y N 18  
84Z C1   C  Y N 19  
84Z CL1  CL N N 20  
84Z S7   S  N N 21  
84Z O8   O  N N 22  
84Z O9   O  N N 23  
84Z N10  N  N N 24  
84Z H1   H  N N 25  
84Z H2   H  N N 26  
84Z H3   H  N N 27  
84Z H4   H  N N 28  
84Z H5   H  N N 29  
84Z H6   H  N N 30  
84Z H7   H  N N 31  
84Z H8   H  N N 32  
84Z H9   H  N N 33  
84Z H10  H  N N 34  
84Z H11  H  N N 35  
84Z H12  H  N N 36  
ACT C    C  N N 37  
ACT O    O  N N 38  
ACT OXT  O  N N 39  
ACT CH3  C  N N 40  
ACT H1   H  N N 41  
ACT H2   H  N N 42  
ACT H3   H  N N 43  
ALA N    N  N N 44  
ALA CA   C  N S 45  
ALA C    C  N N 46  
ALA O    O  N N 47  
ALA CB   C  N N 48  
ALA OXT  O  N N 49  
ALA H    H  N N 50  
ALA H2   H  N N 51  
ALA HA   H  N N 52  
ALA HB1  H  N N 53  
ALA HB2  H  N N 54  
ALA HB3  H  N N 55  
ALA HXT  H  N N 56  
ARG N    N  N N 57  
ARG CA   C  N S 58  
ARG C    C  N N 59  
ARG O    O  N N 60  
ARG CB   C  N N 61  
ARG CG   C  N N 62  
ARG CD   C  N N 63  
ARG NE   N  N N 64  
ARG CZ   C  N N 65  
ARG NH1  N  N N 66  
ARG NH2  N  N N 67  
ARG OXT  O  N N 68  
ARG H    H  N N 69  
ARG H2   H  N N 70  
ARG HA   H  N N 71  
ARG HB2  H  N N 72  
ARG HB3  H  N N 73  
ARG HG2  H  N N 74  
ARG HG3  H  N N 75  
ARG HD2  H  N N 76  
ARG HD3  H  N N 77  
ARG HE   H  N N 78  
ARG HH11 H  N N 79  
ARG HH12 H  N N 80  
ARG HH21 H  N N 81  
ARG HH22 H  N N 82  
ARG HXT  H  N N 83  
ASN N    N  N N 84  
ASN CA   C  N S 85  
ASN C    C  N N 86  
ASN O    O  N N 87  
ASN CB   C  N N 88  
ASN CG   C  N N 89  
ASN OD1  O  N N 90  
ASN ND2  N  N N 91  
ASN OXT  O  N N 92  
ASN H    H  N N 93  
ASN H2   H  N N 94  
ASN HA   H  N N 95  
ASN HB2  H  N N 96  
ASN HB3  H  N N 97  
ASN HD21 H  N N 98  
ASN HD22 H  N N 99  
ASN HXT  H  N N 100 
ASP N    N  N N 101 
ASP CA   C  N S 102 
ASP C    C  N N 103 
ASP O    O  N N 104 
ASP CB   C  N N 105 
ASP CG   C  N N 106 
ASP OD1  O  N N 107 
ASP OD2  O  N N 108 
ASP OXT  O  N N 109 
ASP H    H  N N 110 
ASP H2   H  N N 111 
ASP HA   H  N N 112 
ASP HB2  H  N N 113 
ASP HB3  H  N N 114 
ASP HD2  H  N N 115 
ASP HXT  H  N N 116 
CYS N    N  N N 117 
CYS CA   C  N R 118 
CYS C    C  N N 119 
CYS O    O  N N 120 
CYS CB   C  N N 121 
CYS SG   S  N N 122 
CYS OXT  O  N N 123 
CYS H    H  N N 124 
CYS H2   H  N N 125 
CYS HA   H  N N 126 
CYS HB2  H  N N 127 
CYS HB3  H  N N 128 
CYS HG   H  N N 129 
CYS HXT  H  N N 130 
EDO C1   C  N N 131 
EDO O1   O  N N 132 
EDO C2   C  N N 133 
EDO O2   O  N N 134 
EDO H11  H  N N 135 
EDO H12  H  N N 136 
EDO HO1  H  N N 137 
EDO H21  H  N N 138 
EDO H22  H  N N 139 
EDO HO2  H  N N 140 
GLN N    N  N N 141 
GLN CA   C  N S 142 
GLN C    C  N N 143 
GLN O    O  N N 144 
GLN CB   C  N N 145 
GLN CG   C  N N 146 
GLN CD   C  N N 147 
GLN OE1  O  N N 148 
GLN NE2  N  N N 149 
GLN OXT  O  N N 150 
GLN H    H  N N 151 
GLN H2   H  N N 152 
GLN HA   H  N N 153 
GLN HB2  H  N N 154 
GLN HB3  H  N N 155 
GLN HG2  H  N N 156 
GLN HG3  H  N N 157 
GLN HE21 H  N N 158 
GLN HE22 H  N N 159 
GLN HXT  H  N N 160 
GLU N    N  N N 161 
GLU CA   C  N S 162 
GLU C    C  N N 163 
GLU O    O  N N 164 
GLU CB   C  N N 165 
GLU CG   C  N N 166 
GLU CD   C  N N 167 
GLU OE1  O  N N 168 
GLU OE2  O  N N 169 
GLU OXT  O  N N 170 
GLU H    H  N N 171 
GLU H2   H  N N 172 
GLU HA   H  N N 173 
GLU HB2  H  N N 174 
GLU HB3  H  N N 175 
GLU HG2  H  N N 176 
GLU HG3  H  N N 177 
GLU HE2  H  N N 178 
GLU HXT  H  N N 179 
GLY N    N  N N 180 
GLY CA   C  N N 181 
GLY C    C  N N 182 
GLY O    O  N N 183 
GLY OXT  O  N N 184 
GLY H    H  N N 185 
GLY H2   H  N N 186 
GLY HA2  H  N N 187 
GLY HA3  H  N N 188 
GLY HXT  H  N N 189 
HIS N    N  N N 190 
HIS CA   C  N S 191 
HIS C    C  N N 192 
HIS O    O  N N 193 
HIS CB   C  N N 194 
HIS CG   C  Y N 195 
HIS ND1  N  Y N 196 
HIS CD2  C  Y N 197 
HIS CE1  C  Y N 198 
HIS NE2  N  Y N 199 
HIS OXT  O  N N 200 
HIS H    H  N N 201 
HIS H2   H  N N 202 
HIS HA   H  N N 203 
HIS HB2  H  N N 204 
HIS HB3  H  N N 205 
HIS HD1  H  N N 206 
HIS HD2  H  N N 207 
HIS HE1  H  N N 208 
HIS HE2  H  N N 209 
HIS HXT  H  N N 210 
HOH O    O  N N 211 
HOH H1   H  N N 212 
HOH H2   H  N N 213 
ILE N    N  N N 214 
ILE CA   C  N S 215 
ILE C    C  N N 216 
ILE O    O  N N 217 
ILE CB   C  N S 218 
ILE CG1  C  N N 219 
ILE CG2  C  N N 220 
ILE CD1  C  N N 221 
ILE OXT  O  N N 222 
ILE H    H  N N 223 
ILE H2   H  N N 224 
ILE HA   H  N N 225 
ILE HB   H  N N 226 
ILE HG12 H  N N 227 
ILE HG13 H  N N 228 
ILE HG21 H  N N 229 
ILE HG22 H  N N 230 
ILE HG23 H  N N 231 
ILE HD11 H  N N 232 
ILE HD12 H  N N 233 
ILE HD13 H  N N 234 
ILE HXT  H  N N 235 
LEU N    N  N N 236 
LEU CA   C  N S 237 
LEU C    C  N N 238 
LEU O    O  N N 239 
LEU CB   C  N N 240 
LEU CG   C  N N 241 
LEU CD1  C  N N 242 
LEU CD2  C  N N 243 
LEU OXT  O  N N 244 
LEU H    H  N N 245 
LEU H2   H  N N 246 
LEU HA   H  N N 247 
LEU HB2  H  N N 248 
LEU HB3  H  N N 249 
LEU HG   H  N N 250 
LEU HD11 H  N N 251 
LEU HD12 H  N N 252 
LEU HD13 H  N N 253 
LEU HD21 H  N N 254 
LEU HD22 H  N N 255 
LEU HD23 H  N N 256 
LEU HXT  H  N N 257 
LYS N    N  N N 258 
LYS CA   C  N S 259 
LYS C    C  N N 260 
LYS O    O  N N 261 
LYS CB   C  N N 262 
LYS CG   C  N N 263 
LYS CD   C  N N 264 
LYS CE   C  N N 265 
LYS NZ   N  N N 266 
LYS OXT  O  N N 267 
LYS H    H  N N 268 
LYS H2   H  N N 269 
LYS HA   H  N N 270 
LYS HB2  H  N N 271 
LYS HB3  H  N N 272 
LYS HG2  H  N N 273 
LYS HG3  H  N N 274 
LYS HD2  H  N N 275 
LYS HD3  H  N N 276 
LYS HE2  H  N N 277 
LYS HE3  H  N N 278 
LYS HZ1  H  N N 279 
LYS HZ2  H  N N 280 
LYS HZ3  H  N N 281 
LYS HXT  H  N N 282 
MET N    N  N N 283 
MET CA   C  N S 284 
MET C    C  N N 285 
MET O    O  N N 286 
MET CB   C  N N 287 
MET CG   C  N N 288 
MET SD   S  N N 289 
MET CE   C  N N 290 
MET OXT  O  N N 291 
MET H    H  N N 292 
MET H2   H  N N 293 
MET HA   H  N N 294 
MET HB2  H  N N 295 
MET HB3  H  N N 296 
MET HG2  H  N N 297 
MET HG3  H  N N 298 
MET HE1  H  N N 299 
MET HE2  H  N N 300 
MET HE3  H  N N 301 
MET HXT  H  N N 302 
PEG C1   C  N N 303 
PEG O1   O  N N 304 
PEG C2   C  N N 305 
PEG O2   O  N N 306 
PEG C3   C  N N 307 
PEG C4   C  N N 308 
PEG O4   O  N N 309 
PEG H11  H  N N 310 
PEG H12  H  N N 311 
PEG HO1  H  N N 312 
PEG H21  H  N N 313 
PEG H22  H  N N 314 
PEG H31  H  N N 315 
PEG H32  H  N N 316 
PEG H41  H  N N 317 
PEG H42  H  N N 318 
PEG HO4  H  N N 319 
PHE N    N  N N 320 
PHE CA   C  N S 321 
PHE C    C  N N 322 
PHE O    O  N N 323 
PHE CB   C  N N 324 
PHE CG   C  Y N 325 
PHE CD1  C  Y N 326 
PHE CD2  C  Y N 327 
PHE CE1  C  Y N 328 
PHE CE2  C  Y N 329 
PHE CZ   C  Y N 330 
PHE OXT  O  N N 331 
PHE H    H  N N 332 
PHE H2   H  N N 333 
PHE HA   H  N N 334 
PHE HB2  H  N N 335 
PHE HB3  H  N N 336 
PHE HD1  H  N N 337 
PHE HD2  H  N N 338 
PHE HE1  H  N N 339 
PHE HE2  H  N N 340 
PHE HZ   H  N N 341 
PHE HXT  H  N N 342 
PRO N    N  N N 343 
PRO CA   C  N S 344 
PRO C    C  N N 345 
PRO O    O  N N 346 
PRO CB   C  N N 347 
PRO CG   C  N N 348 
PRO CD   C  N N 349 
PRO OXT  O  N N 350 
PRO H    H  N N 351 
PRO HA   H  N N 352 
PRO HB2  H  N N 353 
PRO HB3  H  N N 354 
PRO HG2  H  N N 355 
PRO HG3  H  N N 356 
PRO HD2  H  N N 357 
PRO HD3  H  N N 358 
PRO HXT  H  N N 359 
SER N    N  N N 360 
SER CA   C  N S 361 
SER C    C  N N 362 
SER O    O  N N 363 
SER CB   C  N N 364 
SER OG   O  N N 365 
SER OXT  O  N N 366 
SER H    H  N N 367 
SER H2   H  N N 368 
SER HA   H  N N 369 
SER HB2  H  N N 370 
SER HB3  H  N N 371 
SER HG   H  N N 372 
SER HXT  H  N N 373 
THR N    N  N N 374 
THR CA   C  N S 375 
THR C    C  N N 376 
THR O    O  N N 377 
THR CB   C  N R 378 
THR OG1  O  N N 379 
THR CG2  C  N N 380 
THR OXT  O  N N 381 
THR H    H  N N 382 
THR H2   H  N N 383 
THR HA   H  N N 384 
THR HB   H  N N 385 
THR HG1  H  N N 386 
THR HG21 H  N N 387 
THR HG22 H  N N 388 
THR HG23 H  N N 389 
THR HXT  H  N N 390 
TRP N    N  N N 391 
TRP CA   C  N S 392 
TRP C    C  N N 393 
TRP O    O  N N 394 
TRP CB   C  N N 395 
TRP CG   C  Y N 396 
TRP CD1  C  Y N 397 
TRP CD2  C  Y N 398 
TRP NE1  N  Y N 399 
TRP CE2  C  Y N 400 
TRP CE3  C  Y N 401 
TRP CZ2  C  Y N 402 
TRP CZ3  C  Y N 403 
TRP CH2  C  Y N 404 
TRP OXT  O  N N 405 
TRP H    H  N N 406 
TRP H2   H  N N 407 
TRP HA   H  N N 408 
TRP HB2  H  N N 409 
TRP HB3  H  N N 410 
TRP HD1  H  N N 411 
TRP HE1  H  N N 412 
TRP HE3  H  N N 413 
TRP HZ2  H  N N 414 
TRP HZ3  H  N N 415 
TRP HH2  H  N N 416 
TRP HXT  H  N N 417 
TYR N    N  N N 418 
TYR CA   C  N S 419 
TYR C    C  N N 420 
TYR O    O  N N 421 
TYR CB   C  N N 422 
TYR CG   C  Y N 423 
TYR CD1  C  Y N 424 
TYR CD2  C  Y N 425 
TYR CE1  C  Y N 426 
TYR CE2  C  Y N 427 
TYR CZ   C  Y N 428 
TYR OH   O  N N 429 
TYR OXT  O  N N 430 
TYR H    H  N N 431 
TYR H2   H  N N 432 
TYR HA   H  N N 433 
TYR HB2  H  N N 434 
TYR HB3  H  N N 435 
TYR HD1  H  N N 436 
TYR HD2  H  N N 437 
TYR HE1  H  N N 438 
TYR HE2  H  N N 439 
TYR HH   H  N N 440 
TYR HXT  H  N N 441 
VAL N    N  N N 442 
VAL CA   C  N S 443 
VAL C    C  N N 444 
VAL O    O  N N 445 
VAL CB   C  N N 446 
VAL CG1  C  N N 447 
VAL CG2  C  N N 448 
VAL OXT  O  N N 449 
VAL H    H  N N 450 
VAL H2   H  N N 451 
VAL HA   H  N N 452 
VAL HB   H  N N 453 
VAL HG11 H  N N 454 
VAL HG12 H  N N 455 
VAL HG13 H  N N 456 
VAL HG21 H  N N 457 
VAL HG22 H  N N 458 
VAL HG23 H  N N 459 
VAL HXT  H  N N 460 
ZN  ZN   ZN N N 461 
# 
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 
84Z CL1 C1   sing N N 1   
84Z O9  S7   doub N N 2   
84Z C21 C20  doub Y N 3   
84Z C21 C22  sing Y N 4   
84Z C1  C2   doub Y N 5   
84Z C1  C6   sing Y N 6   
84Z C20 C19  sing Y N 7   
84Z C2  C3   sing Y N 8   
84Z O8  S7   doub N N 9   
84Z C22 C23  doub Y N 10  
84Z S7  C6   sing N N 11  
84Z S7  N10  sing N N 12  
84Z C6  C5   doub Y N 13  
84Z O17 S16  doub N N 14  
84Z C19 S16  sing N N 15  
84Z C19 C24  doub Y N 16  
84Z C3  S16  sing N N 17  
84Z C3  C4   doub Y N 18  
84Z C23 C24  sing Y N 19  
84Z C5  C4   sing Y N 20  
84Z S16 O18  doub N N 21  
84Z C4  C12  sing N N 22  
84Z O14 C12  sing N N 23  
84Z O14 C15  sing N N 24  
84Z C12 O13  doub N N 25  
84Z C24 H1   sing N N 26  
84Z C23 H2   sing N N 27  
84Z C22 H3   sing N N 28  
84Z C21 H4   sing N N 29  
84Z C20 H5   sing N N 30  
84Z C2  H6   sing N N 31  
84Z C15 H7   sing N N 32  
84Z C15 H8   sing N N 33  
84Z C15 H9   sing N N 34  
84Z C5  H10  sing N N 35  
84Z N10 H11  sing N N 36  
84Z N10 H12  sing N N 37  
ACT C   O    doub N N 38  
ACT C   OXT  sing N N 39  
ACT C   CH3  sing N N 40  
ACT CH3 H1   sing N N 41  
ACT CH3 H2   sing N N 42  
ACT CH3 H3   sing N N 43  
ALA N   CA   sing N N 44  
ALA N   H    sing N N 45  
ALA N   H2   sing N N 46  
ALA CA  C    sing N N 47  
ALA CA  CB   sing N N 48  
ALA CA  HA   sing N N 49  
ALA C   O    doub N N 50  
ALA C   OXT  sing N N 51  
ALA CB  HB1  sing N N 52  
ALA CB  HB2  sing N N 53  
ALA CB  HB3  sing N N 54  
ALA OXT HXT  sing N N 55  
ARG N   CA   sing N N 56  
ARG N   H    sing N N 57  
ARG N   H2   sing N N 58  
ARG CA  C    sing N N 59  
ARG CA  CB   sing N N 60  
ARG CA  HA   sing N N 61  
ARG C   O    doub N N 62  
ARG C   OXT  sing N N 63  
ARG CB  CG   sing N N 64  
ARG CB  HB2  sing N N 65  
ARG CB  HB3  sing N N 66  
ARG CG  CD   sing N N 67  
ARG CG  HG2  sing N N 68  
ARG CG  HG3  sing N N 69  
ARG CD  NE   sing N N 70  
ARG CD  HD2  sing N N 71  
ARG CD  HD3  sing N N 72  
ARG NE  CZ   sing N N 73  
ARG NE  HE   sing N N 74  
ARG CZ  NH1  sing N N 75  
ARG CZ  NH2  doub N N 76  
ARG NH1 HH11 sing N N 77  
ARG NH1 HH12 sing N N 78  
ARG NH2 HH21 sing N N 79  
ARG NH2 HH22 sing N N 80  
ARG OXT HXT  sing N N 81  
ASN N   CA   sing N N 82  
ASN N   H    sing N N 83  
ASN N   H2   sing N N 84  
ASN CA  C    sing N N 85  
ASN CA  CB   sing N N 86  
ASN CA  HA   sing N N 87  
ASN C   O    doub N N 88  
ASN C   OXT  sing N N 89  
ASN CB  CG   sing N N 90  
ASN CB  HB2  sing N N 91  
ASN CB  HB3  sing N N 92  
ASN CG  OD1  doub N N 93  
ASN CG  ND2  sing N N 94  
ASN ND2 HD21 sing N N 95  
ASN ND2 HD22 sing N N 96  
ASN OXT HXT  sing N N 97  
ASP N   CA   sing N N 98  
ASP N   H    sing N N 99  
ASP N   H2   sing N N 100 
ASP CA  C    sing N N 101 
ASP CA  CB   sing N N 102 
ASP CA  HA   sing N N 103 
ASP C   O    doub N N 104 
ASP C   OXT  sing N N 105 
ASP CB  CG   sing N N 106 
ASP CB  HB2  sing N N 107 
ASP CB  HB3  sing N N 108 
ASP CG  OD1  doub N N 109 
ASP CG  OD2  sing N N 110 
ASP OD2 HD2  sing N N 111 
ASP OXT HXT  sing N N 112 
CYS N   CA   sing N N 113 
CYS N   H    sing N N 114 
CYS N   H2   sing N N 115 
CYS CA  C    sing N N 116 
CYS CA  CB   sing N N 117 
CYS CA  HA   sing N N 118 
CYS C   O    doub N N 119 
CYS C   OXT  sing N N 120 
CYS CB  SG   sing N N 121 
CYS CB  HB2  sing N N 122 
CYS CB  HB3  sing N N 123 
CYS SG  HG   sing N N 124 
CYS OXT HXT  sing N N 125 
EDO C1  O1   sing N N 126 
EDO C1  C2   sing N N 127 
EDO C1  H11  sing N N 128 
EDO C1  H12  sing N N 129 
EDO O1  HO1  sing N N 130 
EDO C2  O2   sing N N 131 
EDO C2  H21  sing N N 132 
EDO C2  H22  sing N N 133 
EDO O2  HO2  sing N N 134 
GLN N   CA   sing N N 135 
GLN N   H    sing N N 136 
GLN N   H2   sing N N 137 
GLN CA  C    sing N N 138 
GLN CA  CB   sing N N 139 
GLN CA  HA   sing N N 140 
GLN C   O    doub N N 141 
GLN C   OXT  sing N N 142 
GLN CB  CG   sing N N 143 
GLN CB  HB2  sing N N 144 
GLN CB  HB3  sing N N 145 
GLN CG  CD   sing N N 146 
GLN CG  HG2  sing N N 147 
GLN CG  HG3  sing N N 148 
GLN CD  OE1  doub N N 149 
GLN CD  NE2  sing N N 150 
GLN NE2 HE21 sing N N 151 
GLN NE2 HE22 sing N N 152 
GLN OXT HXT  sing N N 153 
GLU N   CA   sing N N 154 
GLU N   H    sing N N 155 
GLU N   H2   sing N N 156 
GLU CA  C    sing N N 157 
GLU CA  CB   sing N N 158 
GLU CA  HA   sing N N 159 
GLU C   O    doub N N 160 
GLU C   OXT  sing N N 161 
GLU CB  CG   sing N N 162 
GLU CB  HB2  sing N N 163 
GLU CB  HB3  sing N N 164 
GLU CG  CD   sing N N 165 
GLU CG  HG2  sing N N 166 
GLU CG  HG3  sing N N 167 
GLU CD  OE1  doub N N 168 
GLU CD  OE2  sing N N 169 
GLU OE2 HE2  sing N N 170 
GLU OXT HXT  sing N N 171 
GLY N   CA   sing N N 172 
GLY N   H    sing N N 173 
GLY N   H2   sing N N 174 
GLY CA  C    sing N N 175 
GLY CA  HA2  sing N N 176 
GLY CA  HA3  sing N N 177 
GLY C   O    doub N N 178 
GLY C   OXT  sing N N 179 
GLY OXT HXT  sing N N 180 
HIS N   CA   sing N N 181 
HIS N   H    sing N N 182 
HIS N   H2   sing N N 183 
HIS CA  C    sing N N 184 
HIS CA  CB   sing N N 185 
HIS CA  HA   sing N N 186 
HIS C   O    doub N N 187 
HIS C   OXT  sing N N 188 
HIS CB  CG   sing N N 189 
HIS CB  HB2  sing N N 190 
HIS CB  HB3  sing N N 191 
HIS CG  ND1  sing Y N 192 
HIS CG  CD2  doub Y N 193 
HIS ND1 CE1  doub Y N 194 
HIS ND1 HD1  sing N N 195 
HIS CD2 NE2  sing Y N 196 
HIS CD2 HD2  sing N N 197 
HIS CE1 NE2  sing Y N 198 
HIS CE1 HE1  sing N N 199 
HIS NE2 HE2  sing N N 200 
HIS OXT HXT  sing N N 201 
HOH O   H1   sing N N 202 
HOH O   H2   sing N N 203 
ILE N   CA   sing N N 204 
ILE N   H    sing N N 205 
ILE N   H2   sing N N 206 
ILE CA  C    sing N N 207 
ILE CA  CB   sing N N 208 
ILE CA  HA   sing N N 209 
ILE C   O    doub N N 210 
ILE C   OXT  sing N N 211 
ILE CB  CG1  sing N N 212 
ILE CB  CG2  sing N N 213 
ILE CB  HB   sing N N 214 
ILE CG1 CD1  sing N N 215 
ILE CG1 HG12 sing N N 216 
ILE CG1 HG13 sing N N 217 
ILE CG2 HG21 sing N N 218 
ILE CG2 HG22 sing N N 219 
ILE CG2 HG23 sing N N 220 
ILE CD1 HD11 sing N N 221 
ILE CD1 HD12 sing N N 222 
ILE CD1 HD13 sing N N 223 
ILE OXT HXT  sing N N 224 
LEU N   CA   sing N N 225 
LEU N   H    sing N N 226 
LEU N   H2   sing N N 227 
LEU CA  C    sing N N 228 
LEU CA  CB   sing N N 229 
LEU CA  HA   sing N N 230 
LEU C   O    doub N N 231 
LEU C   OXT  sing N N 232 
LEU CB  CG   sing N N 233 
LEU CB  HB2  sing N N 234 
LEU CB  HB3  sing N N 235 
LEU CG  CD1  sing N N 236 
LEU CG  CD2  sing N N 237 
LEU CG  HG   sing N N 238 
LEU CD1 HD11 sing N N 239 
LEU CD1 HD12 sing N N 240 
LEU CD1 HD13 sing N N 241 
LEU CD2 HD21 sing N N 242 
LEU CD2 HD22 sing N N 243 
LEU CD2 HD23 sing N N 244 
LEU OXT HXT  sing N N 245 
LYS N   CA   sing N N 246 
LYS N   H    sing N N 247 
LYS N   H2   sing N N 248 
LYS CA  C    sing N N 249 
LYS CA  CB   sing N N 250 
LYS CA  HA   sing N N 251 
LYS C   O    doub N N 252 
LYS C   OXT  sing N N 253 
LYS CB  CG   sing N N 254 
LYS CB  HB2  sing N N 255 
LYS CB  HB3  sing N N 256 
LYS CG  CD   sing N N 257 
LYS CG  HG2  sing N N 258 
LYS CG  HG3  sing N N 259 
LYS CD  CE   sing N N 260 
LYS CD  HD2  sing N N 261 
LYS CD  HD3  sing N N 262 
LYS CE  NZ   sing N N 263 
LYS CE  HE2  sing N N 264 
LYS CE  HE3  sing N N 265 
LYS NZ  HZ1  sing N N 266 
LYS NZ  HZ2  sing N N 267 
LYS NZ  HZ3  sing N N 268 
LYS OXT HXT  sing N N 269 
MET N   CA   sing N N 270 
MET N   H    sing N N 271 
MET N   H2   sing N N 272 
MET CA  C    sing N N 273 
MET CA  CB   sing N N 274 
MET CA  HA   sing N N 275 
MET C   O    doub N N 276 
MET C   OXT  sing N N 277 
MET CB  CG   sing N N 278 
MET CB  HB2  sing N N 279 
MET CB  HB3  sing N N 280 
MET CG  SD   sing N N 281 
MET CG  HG2  sing N N 282 
MET CG  HG3  sing N N 283 
MET SD  CE   sing N N 284 
MET CE  HE1  sing N N 285 
MET CE  HE2  sing N N 286 
MET CE  HE3  sing N N 287 
MET OXT HXT  sing N N 288 
PEG C1  O1   sing N N 289 
PEG C1  C2   sing N N 290 
PEG C1  H11  sing N N 291 
PEG C1  H12  sing N N 292 
PEG O1  HO1  sing N N 293 
PEG C2  O2   sing N N 294 
PEG C2  H21  sing N N 295 
PEG C2  H22  sing N N 296 
PEG O2  C3   sing N N 297 
PEG C3  C4   sing N N 298 
PEG C3  H31  sing N N 299 
PEG C3  H32  sing N N 300 
PEG C4  O4   sing N N 301 
PEG C4  H41  sing N N 302 
PEG C4  H42  sing N N 303 
PEG O4  HO4  sing N N 304 
PHE N   CA   sing N N 305 
PHE N   H    sing N N 306 
PHE N   H2   sing N N 307 
PHE CA  C    sing N N 308 
PHE CA  CB   sing N N 309 
PHE CA  HA   sing N N 310 
PHE C   O    doub N N 311 
PHE C   OXT  sing N N 312 
PHE CB  CG   sing N N 313 
PHE CB  HB2  sing N N 314 
PHE CB  HB3  sing N N 315 
PHE CG  CD1  doub Y N 316 
PHE CG  CD2  sing Y N 317 
PHE CD1 CE1  sing Y N 318 
PHE CD1 HD1  sing N N 319 
PHE CD2 CE2  doub Y N 320 
PHE CD2 HD2  sing N N 321 
PHE CE1 CZ   doub Y N 322 
PHE CE1 HE1  sing N N 323 
PHE CE2 CZ   sing Y N 324 
PHE CE2 HE2  sing N N 325 
PHE CZ  HZ   sing N N 326 
PHE OXT HXT  sing N N 327 
PRO N   CA   sing N N 328 
PRO N   CD   sing N N 329 
PRO N   H    sing N N 330 
PRO CA  C    sing N N 331 
PRO CA  CB   sing N N 332 
PRO CA  HA   sing N N 333 
PRO C   O    doub N N 334 
PRO C   OXT  sing N N 335 
PRO CB  CG   sing N N 336 
PRO CB  HB2  sing N N 337 
PRO CB  HB3  sing N N 338 
PRO CG  CD   sing N N 339 
PRO CG  HG2  sing N N 340 
PRO CG  HG3  sing N N 341 
PRO CD  HD2  sing N N 342 
PRO CD  HD3  sing N N 343 
PRO OXT HXT  sing N N 344 
SER N   CA   sing N N 345 
SER N   H    sing N N 346 
SER N   H2   sing N N 347 
SER CA  C    sing N N 348 
SER CA  CB   sing N N 349 
SER CA  HA   sing N N 350 
SER C   O    doub N N 351 
SER C   OXT  sing N N 352 
SER CB  OG   sing N N 353 
SER CB  HB2  sing N N 354 
SER CB  HB3  sing N N 355 
SER OG  HG   sing N N 356 
SER OXT HXT  sing N N 357 
THR N   CA   sing N N 358 
THR N   H    sing N N 359 
THR N   H2   sing N N 360 
THR CA  C    sing N N 361 
THR CA  CB   sing N N 362 
THR CA  HA   sing N N 363 
THR C   O    doub N N 364 
THR C   OXT  sing N N 365 
THR CB  OG1  sing N N 366 
THR CB  CG2  sing N N 367 
THR CB  HB   sing N N 368 
THR OG1 HG1  sing N N 369 
THR CG2 HG21 sing N N 370 
THR CG2 HG22 sing N N 371 
THR CG2 HG23 sing N N 372 
THR OXT HXT  sing N N 373 
TRP N   CA   sing N N 374 
TRP N   H    sing N N 375 
TRP N   H2   sing N N 376 
TRP CA  C    sing N N 377 
TRP CA  CB   sing N N 378 
TRP CA  HA   sing N N 379 
TRP C   O    doub N N 380 
TRP C   OXT  sing N N 381 
TRP CB  CG   sing N N 382 
TRP CB  HB2  sing N N 383 
TRP CB  HB3  sing N N 384 
TRP CG  CD1  doub Y N 385 
TRP CG  CD2  sing Y N 386 
TRP CD1 NE1  sing Y N 387 
TRP CD1 HD1  sing N N 388 
TRP CD2 CE2  doub Y N 389 
TRP CD2 CE3  sing Y N 390 
TRP NE1 CE2  sing Y N 391 
TRP NE1 HE1  sing N N 392 
TRP CE2 CZ2  sing Y N 393 
TRP CE3 CZ3  doub Y N 394 
TRP CE3 HE3  sing N N 395 
TRP CZ2 CH2  doub Y N 396 
TRP CZ2 HZ2  sing N N 397 
TRP CZ3 CH2  sing Y N 398 
TRP CZ3 HZ3  sing N N 399 
TRP CH2 HH2  sing N N 400 
TRP OXT HXT  sing N N 401 
TYR N   CA   sing N N 402 
TYR N   H    sing N N 403 
TYR N   H2   sing N N 404 
TYR CA  C    sing N N 405 
TYR CA  CB   sing N N 406 
TYR CA  HA   sing N N 407 
TYR C   O    doub N N 408 
TYR C   OXT  sing N N 409 
TYR CB  CG   sing N N 410 
TYR CB  HB2  sing N N 411 
TYR CB  HB3  sing N N 412 
TYR CG  CD1  doub Y N 413 
TYR CG  CD2  sing Y N 414 
TYR CD1 CE1  sing Y N 415 
TYR CD1 HD1  sing N N 416 
TYR CD2 CE2  doub Y N 417 
TYR CD2 HD2  sing N N 418 
TYR CE1 CZ   doub Y N 419 
TYR CE1 HE1  sing N N 420 
TYR CE2 CZ   sing Y N 421 
TYR CE2 HE2  sing N N 422 
TYR CZ  OH   sing N N 423 
TYR OH  HH   sing N N 424 
TYR OXT HXT  sing N N 425 
VAL N   CA   sing N N 426 
VAL N   H    sing N N 427 
VAL N   H2   sing N N 428 
VAL CA  C    sing N N 429 
VAL CA  CB   sing N N 430 
VAL CA  HA   sing N N 431 
VAL C   O    doub N N 432 
VAL C   OXT  sing N N 433 
VAL CB  CG1  sing N N 434 
VAL CB  CG2  sing N N 435 
VAL CB  HB   sing N N 436 
VAL CG1 HG11 sing N N 437 
VAL CG1 HG12 sing N N 438 
VAL CG1 HG13 sing N N 439 
VAL CG2 HG21 sing N N 440 
VAL CG2 HG22 sing N N 441 
VAL CG2 HG23 sing N N 442 
VAL OXT HXT  sing N N 443 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        84Z 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   84Z 
_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        ? 
# 
_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   1CAB 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7Q0D 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.016119 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013655 
_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]   0.008301 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
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 4   ? 24.833 -7.316  -17.487 1.00 29.42  ? 3   PRO A N   1 
ATOM   2    C  CA  . PRO A  1 4   ? 25.949 -7.856  -16.595 1.00 31.24  ? 3   PRO A CA  1 
ATOM   3    C  C   . PRO A  1 4   ? 25.718 -9.331  -16.267 1.00 25.68  ? 3   PRO A C   1 
ATOM   4    O  O   . PRO A  1 4   ? 24.623 -9.886  -16.466 1.00 32.25  ? 3   PRO A O   1 
ATOM   5    C  CB  . PRO A  1 4   ? 25.872 -7.027  -15.240 1.00 33.96  ? 3   PRO A CB  1 
ATOM   6    C  CG  . PRO A  1 4   ? 24.444 -6.484  -15.292 1.00 54.80  ? 3   PRO A CG  1 
ATOM   7    C  CD  . PRO A  1 4   ? 23.901 -6.420  -16.748 1.00 45.41  ? 3   PRO A CD  1 
ATOM   8    N  N   . ASP A  1 5   ? 26.815 -9.959  -15.850 1.00 25.96  ? 4   ASP A N   1 
ATOM   9    C  CA  . ASP A  1 5   ? 26.821 -11.368 -15.510 1.00 25.81  ? 4   ASP A CA  1 
ATOM   10   C  C   . ASP A  1 5   ? 26.285 -11.611 -14.106 1.00 24.71  ? 4   ASP A C   1 
ATOM   11   O  O   . ASP A  1 5   ? 26.400 -12.722 -13.588 1.00 24.26  ? 4   ASP A O   1 
ATOM   12   C  CB  . ASP A  1 5   ? 28.211 -12.014 -15.733 1.00 25.50  ? 4   ASP A CB  1 
ATOM   13   C  CG  . ASP A  1 5   ? 29.333 -11.324 -14.957 1.00 24.59  ? 4   ASP A CG  1 
ATOM   14   O  OD1 . ASP A  1 5   ? 29.031 -10.650 -13.962 1.00 21.89  ? 4   ASP A OD1 1 
ATOM   15   O  OD2 . ASP A  1 5   ? 30.526 -11.465 -15.327 1.00 34.14  ? 4   ASP A OD2 1 
ATOM   16   N  N   . TRP A  1 6   ? 25.699 -10.589 -13.478 1.00 18.48  ? 5   TRP A N   1 
ATOM   17   C  CA  . TRP A  1 6   ? 25.141 -10.848 -12.141 1.00 17.03  ? 5   TRP A CA  1 
ATOM   18   C  C   . TRP A  1 6   ? 23.876 -10.029 -11.981 1.00 15.45  ? 5   TRP A C   1 
ATOM   19   O  O   . TRP A  1 6   ? 23.710 -8.977  -12.604 1.00 17.28  ? 5   TRP A O   1 
ATOM   20   C  CB  . TRP A  1 6   ? 26.193 -10.477 -11.088 1.00 15.16  ? 5   TRP A CB  1 
ATOM   21   C  CG  . TRP A  1 6   ? 26.486 -9.029  -11.019 1.00 13.26  ? 5   TRP A CG  1 
ATOM   22   C  CD1 . TRP A  1 6   ? 27.465 -8.378  -11.703 1.00 13.39  ? 5   TRP A CD1 1 
ATOM   23   C  CD2 . TRP A  1 6   ? 25.833 -8.043  -10.209 1.00 12.19  ? 5   TRP A CD2 1 
ATOM   24   N  NE1 . TRP A  1 6   ? 27.453 -6.993  -11.340 1.00 14.45  ? 5   TRP A NE1 1 
ATOM   25   C  CE2 . TRP A  1 6   ? 26.446 -6.793  -10.417 1.00 13.50  ? 5   TRP A CE2 1 
ATOM   26   C  CE3 . TRP A  1 6   ? 24.793 -8.109  -9.256  1.00 12.70  ? 5   TRP A CE3 1 
ATOM   27   C  CZ2 . TRP A  1 6   ? 26.024 -5.631  -9.772  1.00 13.97  ? 5   TRP A CZ2 1 
ATOM   28   C  CZ3 . TRP A  1 6   ? 24.359 -6.952  -8.605  1.00 12.53  ? 5   TRP A CZ3 1 
ATOM   29   C  CH2 . TRP A  1 6   ? 24.952 -5.759  -8.873  1.00 12.93  ? 5   TRP A CH2 1 
ATOM   30   N  N   . GLY A  1 7   ? 23.036 -10.460 -11.051 1.00 14.46  ? 6   GLY A N   1 
ATOM   31   C  CA  . GLY A  1 7   ? 21.840 -9.688  -10.671 1.00 14.35  ? 6   GLY A CA  1 
ATOM   32   C  C   . GLY A  1 7   ? 21.332 -10.194 -9.384  1.00 12.80  ? 6   GLY A C   1 
ATOM   33   O  O   . GLY A  1 7   ? 22.121 -10.623 -8.525  1.00 13.21  ? 6   GLY A O   1 
ATOM   34   N  N   . TYR A  1 8   ? 20.009 -10.168 -9.216  1.00 13.27  ? 7   TYR A N   1 
ATOM   35   C  CA  . TYR A  1 8   ? 19.367 -10.627 -7.980  1.00 13.81  ? 7   TYR A CA  1 
ATOM   36   C  C   . TYR A  1 8   ? 18.345 -11.716 -8.241  1.00 15.74  ? 7   TYR A C   1 
ATOM   37   O  O   . TYR A  1 8   ? 17.641 -12.103 -7.319  1.00 19.18  ? 7   TYR A O   1 
ATOM   38   C  CB  . TYR A  1 8   ? 18.684 -9.437  -7.240  1.00 13.38  ? 7   TYR A CB  1 
ATOM   39   C  CG  . TYR A  1 8   ? 19.762 -8.507  -6.681  1.00 11.36  ? 7   TYR A CG  1 
ATOM   40   C  CD1 . TYR A  1 8   ? 20.318 -8.759  -5.392  1.00 11.02  ? 7   TYR A CD1 1 
ATOM   41   C  CD2 . TYR A  1 8   ? 20.166 -7.404  -7.395  1.00 10.86  ? 7   TYR A CD2 1 
ATOM   42   C  CE1 . TYR A  1 8   ? 21.295 -7.914  -4.861  1.00 10.59  ? 7   TYR A CE1 1 
ATOM   43   C  CE2 . TYR A  1 8   ? 21.126 -6.537  -6.876  1.00 10.27  ? 7   TYR A CE2 1 
ATOM   44   C  CZ  . TYR A  1 8   ? 21.656 -6.783  -5.601  1.00 9.11   ? 7   TYR A CZ  1 
ATOM   45   O  OH  . TYR A  1 8   ? 22.607 -5.894  -5.146  1.00 9.61   ? 7   TYR A OH  1 
ATOM   46   N  N   . ASP A  1 9   ? 18.281 -12.219 -9.498  1.00 17.40  ? 8   ASP A N   1 
ATOM   47   C  CA  . ASP A  1 9   ? 17.326 -13.274 -9.815  1.00 20.81  ? 8   ASP A CA  1 
ATOM   48   C  C   . ASP A  1 9   ? 17.870 -14.648 -9.423  1.00 19.64  ? 8   ASP A C   1 
ATOM   49   O  O   . ASP A  1 9   ? 19.023 -14.787 -8.993  1.00 20.46  ? 8   ASP A O   1 
ATOM   50   C  CB  . ASP A  1 9   ? 16.724 -13.175 -11.250 1.00 25.68  ? 8   ASP A CB  1 
ATOM   51   C  CG  . ASP A  1 9   ? 17.686 -13.599 -12.371 1.00 36.69  ? 8   ASP A CG  1 
ATOM   52   O  OD1 . ASP A  1 9   ? 18.460 -14.579 -12.175 1.00 41.33  ? 8   ASP A OD1 1 
ATOM   53   O  OD2 . ASP A  1 9   ? 17.606 -12.960 -13.475 1.00 45.27  ? 8   ASP A OD2 1 
ATOM   54   N  N   . ASP A  1 10  ? 17.031 -15.663 -9.515  1.00 22.68  ? 9   ASP A N   1 
ATOM   55   C  CA  . ASP A  1 10  ? 17.446 -16.991 -9.097  1.00 25.27  ? 9   ASP A CA  1 
ATOM   56   C  C   . ASP A  1 10  ? 18.606 -17.531 -9.927  1.00 26.41  ? 9   ASP A C   1 
ATOM   57   O  O   . ASP A  1 10  ? 19.418 -18.323 -9.450  1.00 30.52  ? 9   ASP A O   1 
ATOM   58   C  CB  . ASP A  1 10  ? 16.251 -17.953 -9.127  1.00 32.95  ? 9   ASP A CB  1 
ATOM   59   C  CG  . ASP A  1 10  ? 15.313 -17.760 -7.940  1.00 40.80  ? 9   ASP A CG  1 
ATOM   60   O  OD1 . ASP A  1 10  ? 15.774 -17.925 -6.791  1.00 63.03  ? 9   ASP A OD1 1 
ATOM   61   O  OD2 . ASP A  1 10  ? 14.118 -17.443 -8.150  1.00 69.49  ? 9   ASP A OD2 1 
ATOM   62   N  N   . LYS A  1 11  ? 18.735 -17.054 -11.154 1.00 22.87  ? 10  LYS A N   1 
ATOM   63   C  CA  . LYS A  1 11  ? 19.760 -17.595 -12.006 1.00 24.84  ? 10  LYS A CA  1 
ATOM   64   C  C   . LYS A  1 11  ? 21.072 -16.805 -11.852 1.00 19.32  ? 10  LYS A C   1 
ATOM   65   O  O   . LYS A  1 11  ? 22.114 -17.351 -12.142 1.00 26.51  ? 10  LYS A O   1 
ATOM   66   C  CB  . LYS A  1 11  ? 19.361 -17.563 -13.517 1.00 32.11  ? 10  LYS A CB  1 
ATOM   67   N  N   . ASN A  1 12  ? 21.034 -15.540 -11.438 1.00 17.56  ? 11  ASN A N   1 
ATOM   68   C  CA  . ASN A  1 12  ? 22.286 -14.753 -11.397 1.00 17.97  ? 11  ASN A CA  1 
ATOM   69   C  C   . ASN A  1 12  ? 22.448 -14.036 -10.094 1.00 13.99  ? 11  ASN A C   1 
ATOM   70   O  O   . ASN A  1 12  ? 23.295 -13.109 -10.043 1.00 14.86  ? 11  ASN A O   1 
ATOM   71   C  CB  . ASN A  1 12  ? 22.240 -13.717 -12.593 1.00 17.95  ? 11  ASN A CB  1 
ATOM   72   C  CG  . ASN A  1 12  ? 21.131 -12.663 -12.464 1.00 19.78  ? 11  ASN A CG  1 
ATOM   73   O  OD1 . ASN A  1 12  ? 20.470 -12.585 -11.433 1.00 18.22  ? 11  ASN A OD1 1 
ATOM   74   N  ND2 . ASN A  1 12  ? 20.934 -11.834 -13.527 1.00 24.17  ? 11  ASN A ND2 1 
ATOM   75   N  N   . GLY A  1 13  ? 21.765 -14.470 -9.065  1.00 15.15  ? 12  GLY A N   1 
ATOM   76   C  CA  . GLY A  1 13  ? 21.686 -13.740 -7.794  1.00 14.78  ? 12  GLY A CA  1 
ATOM   77   C  C   . GLY A  1 13  ? 22.762 -14.152 -6.797  1.00 13.74  ? 12  GLY A C   1 
ATOM   78   O  O   . GLY A  1 13  ? 23.703 -14.888 -7.094  1.00 14.24  ? 12  GLY A O   1 
ATOM   79   N  N   . PRO A  1 14  ? 22.597 -13.642 -5.565  1.00 12.55  ? 13  PRO A N   1 
ATOM   80   C  CA  . PRO A  1 14  ? 23.581 -13.823 -4.513  1.00 12.23  ? 13  PRO A CA  1 
ATOM   81   C  C   . PRO A  1 14  ? 24.083 -15.235 -4.326  1.00 13.04  ? 13  PRO A C   1 
ATOM   82   O  O   . PRO A  1 14  ? 25.284 -15.416 -4.006  1.00 13.48  ? 13  PRO A O   1 
ATOM   83   C  CB  . PRO A  1 14  ? 22.875 -13.323 -3.247  1.00 14.39  ? 13  PRO A CB  1 
ATOM   84   C  CG  . PRO A  1 14  ? 21.970 -12.195 -3.818  1.00 14.12  ? 13  PRO A CG  1 
ATOM   85   C  CD  . PRO A  1 14  ? 21.525 -12.696 -5.208  1.00 14.50  ? 13  PRO A CD  1 
ATOM   86   N  N   . GLU A  1 15  ? 23.190 -16.237 -4.430  1.00 14.14  ? 14  GLU A N   1 
ATOM   87   C  CA  . GLU A  1 15  ? 23.617 -17.605 -4.110  1.00 16.46  ? 14  GLU A CA  1 
ATOM   88   C  C   . GLU A  1 15  ? 24.517 -18.117 -5.245  1.00 16.33  ? 14  GLU A C   1 
ATOM   89   O  O   . GLU A  1 15  ? 25.165 -19.175 -5.008  1.00 21.87  ? 14  GLU A O   1 
ATOM   90   C  CB  . GLU A  1 15  ? 22.374 -18.499 -3.888  1.00 18.71  ? 14  GLU A CB  1 
ATOM   91   C  CG  . GLU A  1 15  ? 21.546 -17.948 -2.709  1.00 24.64  ? 14  GLU A CG  1 
ATOM   92   C  CD  . GLU A  1 15  ? 22.380 -17.777 -1.457  1.00 31.04  ? 14  GLU A CD  1 
ATOM   93   O  OE1 . GLU A  1 15  ? 22.223 -16.640 -0.862  1.00 26.81  ? 14  GLU A OE1 1 
ATOM   94   O  OE2 . GLU A  1 15  ? 23.197 -18.711 -1.093  1.00 35.58  ? 14  GLU A OE2 1 
ATOM   95   N  N   . GLN A  1 16  ? 24.553 -17.468 -6.410  1.00 15.96  ? 15  GLN A N   1 
ATOM   96   C  CA  . GLN A  1 16  ? 25.430 -17.905 -7.487  1.00 17.83  ? 15  GLN A CA  1 
ATOM   97   C  C   . GLN A  1 16  ? 26.605 -16.954 -7.795  1.00 15.11  ? 15  GLN A C   1 
ATOM   98   O  O   . GLN A  1 16  ? 27.419 -17.267 -8.664  1.00 15.94  ? 15  GLN A O   1 
ATOM   99   C  CB  . GLN A  1 16  ? 24.619 -18.158 -8.761  1.00 20.07  ? 15  GLN A CB  1 
ATOM   100  C  CG  . GLN A  1 16  ? 23.195 -18.624 -8.509  1.00 26.14  ? 15  GLN A CG  1 
ATOM   101  C  CD  . GLN A  1 16  ? 23.075 -20.135 -8.466  1.00 32.50  ? 15  GLN A CD  1 
ATOM   102  O  OE1 . GLN A  1 16  ? 22.113 -20.677 -7.921  1.00 41.29  ? 15  GLN A OE1 1 
ATOM   103  N  NE2 . GLN A  1 16  ? 24.053 -20.823 -9.042  1.00 34.95  ? 15  GLN A NE2 1 
ATOM   104  N  N   . TRP A  1 17  ? 26.714 -15.813 -7.115  1.00 13.39  ? 16  TRP A N   1 
ATOM   105  C  CA  . TRP A  1 17  ? 27.807 -14.874 -7.417  1.00 13.08  ? 16  TRP A CA  1 
ATOM   106  C  C   . TRP A  1 17  ? 29.191 -15.451 -7.202  1.00 13.37  ? 16  TRP A C   1 
ATOM   107  O  O   . TRP A  1 17  ? 30.071 -15.006 -7.933  1.00 13.68  ? 16  TRP A O   1 
ATOM   108  C  CB  . TRP A  1 17  ? 27.711 -13.653 -6.455  1.00 12.76  ? 16  TRP A CB  1 
ATOM   109  C  CG  . TRP A  1 17  ? 26.529 -12.774 -6.756  1.00 10.58  ? 16  TRP A CG  1 
ATOM   110  C  CD1 . TRP A  1 17  ? 25.706 -12.720 -7.848  1.00 11.53  ? 16  TRP A CD1 1 
ATOM   111  C  CD2 . TRP A  1 17  ? 26.061 -11.711 -5.878  1.00 10.85  ? 16  TRP A CD2 1 
ATOM   112  N  NE1 . TRP A  1 17  ? 24.771 -11.723 -7.775  1.00 12.19  ? 16  TRP A NE1 1 
ATOM   113  C  CE2 . TRP A  1 17  ? 24.975 -11.113 -6.542  1.00 10.60  ? 16  TRP A CE2 1 
ATOM   114  C  CE3 . TRP A  1 17  ? 26.443 -11.248 -4.579  1.00 10.12  ? 16  TRP A CE3 1 
ATOM   115  C  CZ2 . TRP A  1 17  ? 24.253 -10.035 -5.934  1.00 10.77  ? 16  TRP A CZ2 1 
ATOM   116  C  CZ3 . TRP A  1 17  ? 25.738 -10.190 -4.039  1.00 10.99  ? 16  TRP A CZ3 1 
ATOM   117  C  CH2 . TRP A  1 17  ? 24.645 -9.589  -4.693  1.00 10.34  ? 16  TRP A CH2 1 
ATOM   118  N  N   . SER A  1 18  ? 29.389 -16.441 -6.366  1.00 13.08  ? 17  SER A N   1 
ATOM   119  C  CA  . SER A  1 18  ? 30.738 -16.979 -6.117  1.00 13.33  ? 17  SER A CA  1 
ATOM   120  C  C   . SER A  1 18  ? 31.330 -17.636 -7.367  1.00 13.86  ? 17  SER A C   1 
ATOM   121  O  O   . SER A  1 18  ? 32.547 -17.719 -7.453  1.00 16.17  ? 17  SER A O   1 
ATOM   122  C  CB  . SER A  1 18  ? 30.788 -17.975 -4.955  1.00 14.85  ? 17  SER A CB  1 
ATOM   123  O  OG  . SER A  1 18  ? 30.040 -19.127 -5.276  1.00 18.12  ? 17  SER A OG  1 
ATOM   124  N  N   . LYS A  1 19  ? 30.457 -18.064 -8.323  1.00 16.31  ? 18  LYS A N   1 
ATOM   125  C  CA  . LYS A  1 19  ? 31.054 -18.716 -9.469  1.00 17.49  ? 18  LYS A CA  1 
ATOM   126  C  C   . LYS A  1 19  ? 31.884 -17.724 -10.236 1.00 16.78  ? 18  LYS A C   1 
ATOM   127  O  O   . LYS A  1 19  ? 33.008 -18.003 -10.696 1.00 19.86  ? 18  LYS A O   1 
ATOM   128  C  CB  . LYS A  1 19  ? 29.927 -19.251 -10.368 1.00 17.30  ? 18  LYS A CB  1 
ATOM   129  C  CG  . LYS A  1 19  ? 29.146 -20.390 -9.716  1.00 23.03  ? 18  LYS A CG  1 
ATOM   130  C  CD  . LYS A  1 19  ? 28.097 -20.954 -10.632 1.00 33.58  ? 18  LYS A CD  1 
ATOM   131  C  CE  . LYS A  1 19  ? 27.218 -21.989 -9.957  1.00 32.07  ? 18  LYS A CE  1 
ATOM   132  N  NZ  . LYS A  1 19  ? 26.178 -22.445 -10.885 1.00 44.47  ? 18  LYS A NZ  1 
ATOM   133  N  N   . LEU A  1 20  ? 31.405 -16.522 -10.452 1.00 17.34  ? 19  LEU A N   1 
ATOM   134  C  CA  . LEU A  1 20  ? 32.167 -15.515 -11.166 1.00 16.67  ? 19  LEU A CA  1 
ATOM   135  C  C   . LEU A  1 20  ? 32.954 -14.560 -10.253 1.00 15.84  ? 19  LEU A C   1 
ATOM   136  O  O   . LEU A  1 20  ? 33.905 -13.930 -10.766 1.00 16.03  ? 19  LEU A O   1 
ATOM   137  C  CB  . LEU A  1 20  ? 31.248 -14.667 -12.033 1.00 17.31  ? 19  LEU A CB  1 
ATOM   138  C  CG  . LEU A  1 20  ? 30.616 -15.523 -13.190 1.00 26.21  ? 19  LEU A CG  1 
ATOM   139  C  CD1 . LEU A  1 20  ? 29.722 -14.671 -14.016 1.00 36.52  ? 19  LEU A CD1 1 
ATOM   140  C  CD2 . LEU A  1 20  ? 31.663 -16.149 -14.081 1.00 38.65  ? 19  LEU A CD2 1 
ATOM   141  N  N   . TYR A  1 21  ? 32.616 -14.480 -8.982  1.00 13.61  ? 20  TYR A N   1 
ATOM   142  C  CA  . TYR A  1 21  ? 33.332 -13.602 -8.045  1.00 13.28  ? 20  TYR A CA  1 
ATOM   143  C  C   . TYR A  1 21  ? 33.620 -14.428 -6.813  1.00 12.26  ? 20  TYR A C   1 
ATOM   144  O  O   . TYR A  1 21  ? 32.892 -14.402 -5.808  1.00 12.95  ? 20  TYR A O   1 
ATOM   145  C  CB  . TYR A  1 21  ? 32.507 -12.365 -7.713  1.00 14.36  ? 20  TYR A CB  1 
ATOM   146  C  CG  . TYR A  1 21  ? 32.080 -11.634 -8.953  1.00 13.76  ? 20  TYR A CG  1 
ATOM   147  C  CD1 . TYR A  1 21  ? 32.873 -10.634 -9.504  1.00 15.96  ? 20  TYR A CD1 1 
ATOM   148  C  CD2 . TYR A  1 21  ? 30.901 -11.970 -9.598  1.00 16.22  ? 20  TYR A CD2 1 
ATOM   149  C  CE1 . TYR A  1 21  ? 32.489 -9.973  -10.654 1.00 16.27  ? 20  TYR A CE1 1 
ATOM   150  C  CE2 . TYR A  1 21  ? 30.509 -11.318 -10.744 1.00 17.43  ? 20  TYR A CE2 1 
ATOM   151  C  CZ  . TYR A  1 21  ? 31.307 -10.325 -11.262 1.00 15.65  ? 20  TYR A CZ  1 
ATOM   152  O  OH  . TYR A  1 21  ? 30.916 -9.686  -12.397 1.00 20.70  ? 20  TYR A OH  1 
ATOM   153  N  N   . PRO A  1 22  ? 34.719 -15.201 -6.853  1.00 13.36  ? 21  PRO A N   1 
ATOM   154  C  CA  . PRO A  1 22  ? 34.969 -16.144 -5.715  1.00 14.13  ? 21  PRO A CA  1 
ATOM   155  C  C   . PRO A  1 22  ? 35.116 -15.493 -4.376  1.00 12.34  ? 21  PRO A C   1 
ATOM   156  O  O   . PRO A  1 22  ? 34.856 -16.165 -3.357  1.00 13.88  ? 21  PRO A O   1 
ATOM   157  C  CB  . PRO A  1 22  ? 36.322 -16.817 -6.185  1.00 16.42  ? 21  PRO A CB  1 
ATOM   158  C  CG  . PRO A  1 22  ? 36.118 -16.862 -7.725  1.00 18.25  ? 21  PRO A CG  1 
ATOM   159  C  CD  . PRO A  1 22  ? 35.598 -15.477 -8.012  1.00 16.02  ? 21  PRO A CD  1 
ATOM   160  N  N   . ILE A  1 23  ? 35.459 -14.199 -4.310  1.00 13.34  ? 22  ILE A N   1 
ATOM   161  C  CA  . ILE A  1 23  ? 35.513 -13.541 -3.014  1.00 12.55  ? 22  ILE A CA  1 
ATOM   162  C  C   . ILE A  1 23  ? 34.146 -13.451 -2.335  1.00 11.26  ? 22  ILE A C   1 
ATOM   163  O  O   . ILE A  1 23  ? 34.111 -13.160 -1.121  1.00 12.35  ? 22  ILE A O   1 
ATOM   164  C  CB  . ILE A  1 23  ? 36.113 -12.124 -3.187  1.00 12.70  ? 22  ILE A CB  1 
ATOM   165  C  CG1 . ILE A  1 23  ? 36.658 -11.560 -1.892  1.00 14.84  ? 22  ILE A CG1 1 
ATOM   166  C  CG2 . ILE A  1 23  ? 35.098 -11.170 -3.808  1.00 14.93  ? 22  ILE A CG2 1 
ATOM   167  C  CD1 . ILE A  1 23  ? 37.740 -12.429 -1.252  1.00 20.06  ? 22  ILE A CD1 1 
ATOM   168  N  N   . ALA A  1 24  ? 33.079 -13.811 -2.995  1.00 11.16  ? 23  ALA A N   1 
ATOM   169  C  CA  . ALA A  1 24  ? 31.769 -13.893 -2.306  1.00 11.88  ? 23  ALA A CA  1 
ATOM   170  C  C   . ALA A  1 24  ? 31.794 -14.803 -1.152  1.00 11.91  ? 23  ALA A C   1 
ATOM   171  O  O   . ALA A  1 24  ? 30.982 -14.619 -0.254  1.00 11.78  ? 23  ALA A O   1 
ATOM   172  C  CB  . ALA A  1 24  ? 30.710 -14.423 -3.327  1.00 11.68  ? 23  ALA A CB  1 
ATOM   173  N  N   . ASN A  1 25  ? 32.749 -15.729 -1.114  1.00 12.57  ? 24  ASN A N   1 
ATOM   174  C  CA  . ASN A  1 25  ? 32.878 -16.669 -0.002  1.00 12.85  ? 24  ASN A CA  1 
ATOM   175  C  C   . ASN A  1 25  ? 34.076 -16.330 0.893   1.00 12.70  ? 24  ASN A C   1 
ATOM   176  O  O   . ASN A  1 25  ? 34.616 -17.197 1.579   1.00 15.02  ? 24  ASN A O   1 
ATOM   177  C  CB  . ASN A  1 25  ? 33.000 -18.102 -0.524  1.00 15.21  ? 24  ASN A CB  1 
ATOM   178  C  CG  . ASN A  1 25  ? 31.700 -18.624 -1.103  1.00 17.70  ? 24  ASN A CG  1 
ATOM   179  O  OD1 . ASN A  1 25  ? 31.698 -19.366 -2.086  1.00 23.91  ? 24  ASN A OD1 1 
ATOM   180  N  ND2 . ASN A  1 25  ? 30.584 -18.238 -0.496  1.00 19.86  ? 24  ASN A ND2 1 
ATOM   181  N  N   . GLY A  1 26  ? 34.480 -15.063 0.875   1.00 12.93  ? 25  GLY A N   1 
ATOM   182  C  CA  . GLY A  1 26  ? 35.602 -14.571 1.668   1.00 13.38  ? 25  GLY A CA  1 
ATOM   183  C  C   . GLY A  1 26  ? 35.299 -14.409 3.133   1.00 12.07  ? 25  GLY A C   1 
ATOM   184  O  O   . GLY A  1 26  ? 34.194 -14.721 3.616   1.00 13.28  ? 25  GLY A O   1 
ATOM   185  N  N   . ASN A  1 27  ? 36.310 -13.892 3.863   1.00 12.58  ? 26  ASN A N   1 
ATOM   186  C  CA  . ASN A  1 27  ? 36.239 -13.757 5.304   1.00 13.27  ? 26  ASN A CA  1 
ATOM   187  C  C   . ASN A  1 27  ? 35.810 -12.399 5.758   1.00 11.45  ? 26  ASN A C   1 
ATOM   188  O  O   . ASN A  1 27  ? 35.656 -12.196 6.956   1.00 14.19  ? 26  ASN A O   1 
ATOM   189  C  CB  . ASN A  1 27  ? 37.619 -14.075 5.848   1.00 16.87  ? 26  ASN A CB  1 
ATOM   190  C  CG  . ASN A  1 27  ? 37.979 -15.480 5.586   1.00 21.31  ? 26  ASN A CG  1 
ATOM   191  O  OD1 . ASN A  1 27  ? 37.092 -16.398 5.722   1.00 21.29  ? 26  ASN A OD1 1 
ATOM   192  N  ND2 . ASN A  1 27  ? 39.261 -15.665 5.330   1.00 26.84  ? 26  ASN A ND2 1 
ATOM   193  N  N   A ASN A  1 28  ? 35.677 -11.449 4.800   0.50 9.77   ? 27  ASN A N   1 
ATOM   194  N  N   B ASN A  1 28  ? 35.520 -11.479 4.833   0.50 10.70  ? 27  ASN A N   1 
ATOM   195  C  CA  A ASN A  1 28  ? 35.275 -10.076 5.108   0.50 8.67   ? 27  ASN A CA  1 
ATOM   196  C  CA  B ASN A  1 28  ? 35.156 -10.147 5.256   0.50 10.46  ? 27  ASN A CA  1 
ATOM   197  C  C   A ASN A  1 28  ? 34.023 -9.604  4.367   0.50 8.97   ? 27  ASN A C   1 
ATOM   198  C  C   B ASN A  1 28  ? 34.055 -9.668  4.341   0.50 10.31  ? 27  ASN A C   1 
ATOM   199  O  O   A ASN A  1 28  ? 33.928 -8.419  3.969   0.50 7.75   ? 27  ASN A O   1 
ATOM   200  O  O   B ASN A  1 28  ? 34.111 -8.572  3.752   0.50 11.05  ? 27  ASN A O   1 
ATOM   201  C  CB  A ASN A  1 28  ? 36.433 -9.047  4.925   0.50 11.77  ? 27  ASN A CB  1 
ATOM   202  C  CB  B ASN A  1 28  ? 36.354 -9.161  5.213   0.50 10.89  ? 27  ASN A CB  1 
ATOM   203  C  CG  A ASN A  1 28  ? 37.498 -9.228  5.973   0.50 11.18  ? 27  ASN A CG  1 
ATOM   204  C  CG  B ASN A  1 28  ? 37.553 -9.672  5.982   0.50 18.13  ? 27  ASN A CG  1 
ATOM   205  O  OD1 A ASN A  1 28  ? 38.366 -10.064 5.763   0.50 20.45  ? 27  ASN A OD1 1 
ATOM   206  O  OD1 B ASN A  1 28  ? 37.595 -9.540  7.124   0.50 19.22  ? 27  ASN A OD1 1 
ATOM   207  N  ND2 A ASN A  1 28  ? 37.536 -8.432  6.898   0.50 20.99  ? 27  ASN A ND2 1 
ATOM   208  N  ND2 B ASN A  1 28  ? 38.600 -10.192 5.258   0.50 20.41  ? 27  ASN A ND2 1 
ATOM   209  N  N   . GLN A  1 29  ? 33.014 -10.509 4.181   1.00 9.21   ? 28  GLN A N   1 
ATOM   210  C  CA  . GLN A  1 29  ? 31.877 -10.177 3.330   1.00 8.93   ? 28  GLN A CA  1 
ATOM   211  C  C   . GLN A  1 29  ? 30.777 -9.451  4.081   1.00 8.49   ? 28  GLN A C   1 
ATOM   212  O  O   . GLN A  1 29  ? 30.603 -9.637  5.316   1.00 9.27   ? 28  GLN A O   1 
ATOM   213  C  CB  . GLN A  1 29  ? 31.363 -11.459 2.652   1.00 9.67   ? 28  GLN A CB  1 
ATOM   214  C  CG  . GLN A  1 29  ? 32.334 -11.966 1.621   1.00 10.04  ? 28  GLN A CG  1 
ATOM   215  C  CD  . GLN A  1 29  ? 32.395 -11.077 0.424   1.00 8.95   ? 28  GLN A CD  1 
ATOM   216  O  OE1 . GLN A  1 29  ? 31.413 -10.949 -0.300  1.00 10.08  ? 28  GLN A OE1 1 
ATOM   217  N  NE2 . GLN A  1 29  ? 33.507 -10.400 0.193   1.00 10.21  ? 28  GLN A NE2 1 
ATOM   218  N  N   . SER A  1 30  ? 30.033 -8.655  3.346   1.00 8.23   ? 29  SER A N   1 
ATOM   219  C  CA  . SER A  1 30  ? 28.928 -7.856  3.910   1.00 8.64   ? 29  SER A CA  1 
ATOM   220  C  C   . SER A  1 30  ? 27.671 -8.132  3.099   1.00 7.38   ? 29  SER A C   1 
ATOM   221  O  O   . SER A  1 30  ? 27.750 -8.521  1.923   1.00 8.90   ? 29  SER A O   1 
ATOM   222  C  CB  . SER A  1 30  ? 29.251 -6.381  3.797   1.00 7.95   ? 29  SER A CB  1 
ATOM   223  O  OG  . SER A  1 30  ? 30.363 -6.078  4.632   1.00 8.33   ? 29  SER A OG  1 
ATOM   224  N  N   . PRO A  1 31  ? 26.484 -7.923  3.664   1.00 7.53   ? 30  PRO A N   1 
ATOM   225  C  CA  . PRO A  1 31  ? 26.224 -7.429  5.014   1.00 7.93   ? 30  PRO A CA  1 
ATOM   226  C  C   . PRO A  1 31  ? 26.344 -8.548  6.066   1.00 8.56   ? 30  PRO A C   1 
ATOM   227  O  O   . PRO A  1 31  ? 26.598 -9.715  5.692   1.00 8.89   ? 30  PRO A O   1 
ATOM   228  C  CB  . PRO A  1 31  ? 24.766 -6.961  4.900   1.00 8.68   ? 30  PRO A CB  1 
ATOM   229  C  CG  . PRO A  1 31  ? 24.144 -7.967  3.944   1.00 8.76   ? 30  PRO A CG  1 
ATOM   230  C  CD  . PRO A  1 31  ? 25.225 -8.195  2.949   1.00 8.91   ? 30  PRO A CD  1 
ATOM   231  N  N   . VAL A  1 32  ? 26.172 -8.195  7.336   1.00 8.15   ? 31  VAL A N   1 
ATOM   232  C  CA  . VAL A  1 32  ? 26.202 -9.154  8.442   1.00 8.65   ? 31  VAL A CA  1 
ATOM   233  C  C   . VAL A  1 32  ? 25.047 -8.839  9.341   1.00 8.76   ? 31  VAL A C   1 
ATOM   234  O  O   . VAL A  1 32  ? 24.453 -7.744  9.324   1.00 9.38   ? 31  VAL A O   1 
ATOM   235  C  CB  . VAL A  1 32  ? 27.555 -9.061  9.228   1.00 9.36   ? 31  VAL A CB  1 
ATOM   236  C  CG1 . VAL A  1 32  ? 28.719 -9.410  8.340   1.00 11.03  ? 31  VAL A CG1 1 
ATOM   237  C  CG2 . VAL A  1 32  ? 27.719 -7.724  9.941   1.00 10.59  ? 31  VAL A CG2 1 
ATOM   238  N  N   . ASP A  1 33  ? 24.706 -9.841  10.172  1.00 8.99   ? 32  ASP A N   1 
ATOM   239  C  CA  . ASP A  1 33  ? 23.819 -9.619  11.324  1.00 9.31   ? 32  ASP A CA  1 
ATOM   240  C  C   . ASP A  1 33  ? 24.671 -9.062  12.468  1.00 9.22   ? 32  ASP A C   1 
ATOM   241  O  O   . ASP A  1 33  ? 25.699 -9.635  12.808  1.00 12.87  ? 32  ASP A O   1 
ATOM   242  C  CB  . ASP A  1 33  ? 23.204 -10.940 11.753  1.00 11.08  ? 32  ASP A CB  1 
ATOM   243  C  CG  . ASP A  1 33  ? 22.286 -10.739 12.924  1.00 10.98  ? 32  ASP A CG  1 
ATOM   244  O  OD1 . ASP A  1 33  ? 21.344 -9.930  12.864  1.00 11.10  ? 32  ASP A OD1 1 
ATOM   245  O  OD2 . ASP A  1 33  ? 22.427 -11.452 13.937  1.00 17.13  ? 32  ASP A OD2 1 
ATOM   246  N  N   . ILE A  1 34  ? 24.251 -7.979  13.081  1.00 9.62   ? 33  ILE A N   1 
ATOM   247  C  CA  . ILE A  1 34  ? 24.887 -7.407  14.256  1.00 10.06  ? 33  ILE A CA  1 
ATOM   248  C  C   . ILE A  1 34  ? 24.159 -7.945  15.468  1.00 10.05  ? 33  ILE A C   1 
ATOM   249  O  O   . ILE A  1 34  ? 23.011 -7.556  15.744  1.00 10.84  ? 33  ILE A O   1 
ATOM   250  C  CB  . ILE A  1 34  ? 24.838 -5.894  14.185  1.00 10.31  ? 33  ILE A CB  1 
ATOM   251  C  CG1 . ILE A  1 34  ? 25.627 -5.399  12.964  1.00 11.44  ? 33  ILE A CG1 1 
ATOM   252  C  CG2 . ILE A  1 34  ? 25.417 -5.278  15.511  1.00 12.47  ? 33  ILE A CG2 1 
ATOM   253  C  CD1 . ILE A  1 34  ? 25.522 -3.910  12.777  1.00 13.47  ? 33  ILE A CD1 1 
ATOM   254  N  N   . LYS A  1 35  ? 24.830 -8.822  16.209  1.00 11.03  ? 34  LYS A N   1 
ATOM   255  C  CA  . LYS A  1 35  ? 24.290 -9.357  17.450  1.00 12.55  ? 34  LYS A CA  1 
ATOM   256  C  C   . LYS A  1 35  ? 24.780 -8.350  18.478  1.00 12.53  ? 34  LYS A C   1 
ATOM   257  O  O   . LYS A  1 35  ? 25.985 -8.215  18.688  1.00 14.04  ? 34  LYS A O   1 
ATOM   258  C  CB  . LYS A  1 35  ? 24.858 -10.743 17.741  1.00 15.70  ? 34  LYS A CB  1 
ATOM   259  C  CG  . LYS A  1 35  ? 24.283 -11.846 16.867  1.00 22.02  ? 34  LYS A CG  1 
ATOM   260  C  CD  . LYS A  1 35  ? 25.123 -13.109 16.947  1.00 34.10  ? 34  LYS A CD  1 
ATOM   261  C  CE  . LYS A  1 35  ? 24.625 -14.035 18.045  1.00 46.62  ? 34  LYS A CE  1 
ATOM   262  N  NZ  . LYS A  1 35  ? 24.222 -13.282 19.265  1.00 51.14  ? 34  LYS A NZ  1 
ATOM   263  N  N   . THR A  1 36  ? 23.860 -7.638  19.120  1.00 12.98  ? 35  THR A N   1 
ATOM   264  C  CA  . THR A  1 36  ? 24.258 -6.603  20.037  1.00 14.36  ? 35  THR A CA  1 
ATOM   265  C  C   . THR A  1 36  ? 24.941 -7.131  21.277  1.00 15.47  ? 35  THR A C   1 
ATOM   266  O  O   . THR A  1 36  ? 25.789 -6.433  21.785  1.00 18.30  ? 35  THR A O   1 
ATOM   267  C  CB  . THR A  1 36  ? 23.102 -5.656  20.365  1.00 15.27  ? 35  THR A CB  1 
ATOM   268  O  OG1 . THR A  1 36  ? 22.042 -6.401  20.956  1.00 15.97  ? 35  THR A OG1 1 
ATOM   269  C  CG2 . THR A  1 36  ? 22.668 -4.982  19.043  1.00 18.75  ? 35  THR A CG2 1 
ATOM   270  N  N   . SER A  1 37  ? 24.599 -8.335  21.707  1.00 15.60  ? 36  SER A N   1 
ATOM   271  C  CA  . SER A  1 37  ? 25.308 -8.875  22.894  1.00 18.28  ? 36  SER A CA  1 
ATOM   272  C  C   . SER A  1 37  ? 26.724 -9.179  22.625  1.00 15.77  ? 36  SER A C   1 
ATOM   273  O  O   . SER A  1 37  ? 27.464 -9.307  23.617  1.00 20.00  ? 36  SER A O   1 
ATOM   274  C  CB  . SER A  1 37  ? 24.594 -10.182 23.367  1.00 20.35  ? 36  SER A CB  1 
ATOM   275  O  OG  . SER A  1 37  ? 24.718 -11.213 22.358  1.00 21.02  ? 36  SER A OG  1 
ATOM   276  N  N   A GLU A  1 38  ? 27.136 -9.244  21.363  0.50 14.17  ? 37  GLU A N   1 
ATOM   277  N  N   B GLU A  1 38  ? 27.175 -9.214  21.357  0.50 14.15  ? 37  GLU A N   1 
ATOM   278  C  CA  A GLU A  1 38  ? 28.515 -9.582  21.033  0.50 13.95  ? 37  GLU A CA  1 
ATOM   279  C  CA  B GLU A  1 38  ? 28.522 -9.581  21.045  0.50 14.80  ? 37  GLU A CA  1 
ATOM   280  C  C   A GLU A  1 38  ? 29.390 -8.395  20.639  0.50 12.34  ? 37  GLU A C   1 
ATOM   281  C  C   B GLU A  1 38  ? 29.361 -8.398  20.568  0.50 12.46  ? 37  GLU A C   1 
ATOM   282  O  O   A GLU A  1 38  ? 30.601 -8.549  20.483  0.50 13.99  ? 37  GLU A O   1 
ATOM   283  O  O   B GLU A  1 38  ? 30.547 -8.582  20.267  0.50 14.03  ? 37  GLU A O   1 
ATOM   284  C  CB  A GLU A  1 38  ? 28.549 -10.638 19.924  0.50 15.69  ? 37  GLU A CB  1 
ATOM   285  C  CB  B GLU A  1 38  ? 28.623 -10.640 19.911  0.50 17.25  ? 37  GLU A CB  1 
ATOM   286  C  CG  A GLU A  1 38  ? 27.325 -11.538 19.887  0.50 20.22  ? 37  GLU A CG  1 
ATOM   287  C  CG  B GLU A  1 38  ? 27.797 -11.873 20.254  0.50 23.11  ? 37  GLU A CG  1 
ATOM   288  C  CD  A GLU A  1 38  ? 27.678 -13.007 20.006  0.50 28.37  ? 37  GLU A CD  1 
ATOM   289  C  CD  B GLU A  1 38  ? 28.157 -12.408 21.593  0.50 24.51  ? 37  GLU A CD  1 
ATOM   290  O  OE1 A GLU A  1 38  ? 26.916 -13.847 19.481  0.50 37.50  ? 37  GLU A OE1 1 
ATOM   291  O  OE1 B GLU A  1 38  ? 29.355 -12.726 21.769  0.50 30.21  ? 37  GLU A OE1 1 
ATOM   292  O  OE2 A GLU A  1 38  ? 28.716 -13.322 20.624  0.50 44.50  ? 37  GLU A OE2 1 
ATOM   293  O  OE2 B GLU A  1 38  ? 27.221 -12.561 22.475  0.50 28.16  ? 37  GLU A OE2 1 
ATOM   294  N  N   . THR A  1 39  ? 28.795 -7.219  20.465  1.00 11.84  ? 38  THR A N   1 
ATOM   295  C  CA  . THR A  1 39  ? 29.588 -6.080  20.087  1.00 10.75  ? 38  THR A CA  1 
ATOM   296  C  C   . THR A  1 39  ? 30.589 -5.695  21.168  1.00 11.24  ? 38  THR A C   1 
ATOM   297  O  O   . THR A  1 39  ? 30.349 -5.989  22.351  1.00 13.90  ? 38  THR A O   1 
ATOM   298  C  CB  . THR A  1 39  ? 28.715 -4.847  19.728  1.00 10.82  ? 38  THR A CB  1 
ATOM   299  O  OG1 . THR A  1 39  ? 27.954 -4.476  20.872  1.00 12.66  ? 38  THR A OG1 1 
ATOM   300  C  CG2 . THR A  1 39  ? 27.790 -5.152  18.561  1.00 11.29  ? 38  THR A CG2 1 
ATOM   301  N  N   . LYS A  1 40  ? 31.661 -5.052  20.799  1.00 11.06  ? 39  LYS A N   1 
ATOM   302  C  CA  . LYS A  1 40  ? 32.654 -4.625  21.765  1.00 10.79  ? 39  LYS A CA  1 
ATOM   303  C  C   . LYS A  1 40  ? 32.862 -3.145  21.666  1.00 9.69   ? 39  LYS A C   1 
ATOM   304  O  O   . LYS A  1 40  ? 33.019 -2.577  20.569  1.00 11.17  ? 39  LYS A O   1 
ATOM   305  C  CB  . LYS A  1 40  ? 34.016 -5.332  21.484  1.00 12.51  ? 39  LYS A CB  1 
ATOM   306  C  CG  . LYS A  1 40  ? 33.914 -6.876  21.581  1.00 14.88  ? 39  LYS A CG  1 
ATOM   307  C  CD  . LYS A  1 40  ? 33.463 -7.315  23.000  1.00 16.37  ? 39  LYS A CD  1 
ATOM   308  C  CE  . LYS A  1 40  ? 33.281 -8.911  23.096  1.00 22.78  ? 39  LYS A CE  1 
ATOM   309  N  NZ  . LYS A  1 40  ? 34.589 -9.465  23.087  1.00 30.96  ? 39  LYS A NZ  1 
ATOM   310  N  N   . HIS A  1 41  ? 32.865 -2.432  22.763  1.00 12.12  ? 40  HIS A N   1 
ATOM   311  C  CA  . HIS A  1 41  ? 33.066 -1.015  22.782  1.00 11.66  ? 40  HIS A CA  1 
ATOM   312  C  C   . HIS A  1 41  ? 34.532 -0.739  22.693  1.00 12.29  ? 40  HIS A C   1 
ATOM   313  O  O   . HIS A  1 41  ? 35.387 -1.262  23.441  1.00 13.68  ? 40  HIS A O   1 
ATOM   314  C  CB  . HIS A  1 41  ? 32.443 -0.350  24.005  1.00 12.15  ? 40  HIS A CB  1 
ATOM   315  C  CG  . HIS A  1 41  ? 32.761 1.076   24.091  1.00 11.49  ? 40  HIS A CG  1 
ATOM   316  N  ND1 . HIS A  1 41  ? 32.342 2.093   23.221  1.00 18.54  ? 40  HIS A ND1 1 
ATOM   317  C  CD2 . HIS A  1 41  ? 33.614 1.658   24.936  1.00 10.03  ? 40  HIS A CD2 1 
ATOM   318  C  CE1 . HIS A  1 41  ? 32.778 3.241   23.704  1.00 16.70  ? 40  HIS A CE1 1 
ATOM   319  N  NE2 . HIS A  1 41  ? 33.628 3.016   24.651  1.00 14.71  ? 40  HIS A NE2 1 
ATOM   320  N  N   . ASP A  1 42  ? 34.950 0.146   21.750  1.00 12.89  ? 41  ASP A N   1 
ATOM   321  C  CA  . ASP A  1 42  ? 36.317 0.586   21.560  1.00 12.46  ? 41  ASP A CA  1 
ATOM   322  C  C   . ASP A  1 42  ? 36.438 2.020   21.938  1.00 12.90  ? 41  ASP A C   1 
ATOM   323  O  O   . ASP A  1 42  ? 35.795 2.902   21.342  1.00 12.32  ? 41  ASP A O   1 
ATOM   324  C  CB  . ASP A  1 42  ? 36.618 0.365   20.046  1.00 14.74  ? 41  ASP A CB  1 
ATOM   325  C  CG  . ASP A  1 42  ? 38.014 0.858   19.585  1.00 15.16  ? 41  ASP A CG  1 
ATOM   326  O  OD1 . ASP A  1 42  ? 38.672 1.542   20.380  1.00 16.24  ? 41  ASP A OD1 1 
ATOM   327  O  OD2 . ASP A  1 42  ? 38.347 0.678   18.421  1.00 19.27  ? 41  ASP A OD2 1 
ATOM   328  N  N   . THR A  1 43  ? 37.176 2.271   23.026  1.00 12.35  ? 42  THR A N   1 
ATOM   329  C  CA  . THR A  1 43  ? 37.234 3.630   23.593  1.00 12.77  ? 42  THR A CA  1 
ATOM   330  C  C   . THR A  1 43  ? 37.998 4.590   22.654  1.00 12.81  ? 42  THR A C   1 
ATOM   331  O  O   . THR A  1 43  ? 37.938 5.769   22.877  1.00 13.92  ? 42  THR A O   1 
ATOM   332  C  CB  . THR A  1 43  ? 37.969 3.629   24.936  1.00 12.97  ? 42  THR A CB  1 
ATOM   333  O  OG1 . THR A  1 43  ? 39.352 3.364   24.797  1.00 12.47  ? 42  THR A OG1 1 
ATOM   334  C  CG2 . THR A  1 43  ? 37.284 2.551   25.887  1.00 13.75  ? 42  THR A CG2 1 
ATOM   335  N  N   . SER A  1 44  ? 38.694 4.092   21.631  1.00 12.38  ? 43  SER A N   1 
ATOM   336  C  CA  . SER A  1 44  ? 39.387 4.952   20.687  1.00 13.14  ? 43  SER A CA  1 
ATOM   337  C  C   . SER A  1 44  ? 38.445 5.509   19.617  1.00 11.51  ? 43  SER A C   1 
ATOM   338  O  O   . SER A  1 44  ? 38.846 6.435   18.946  1.00 13.76  ? 43  SER A O   1 
ATOM   339  C  CB  . SER A  1 44  ? 40.537 4.261   20.030  1.00 14.38  ? 43  SER A CB  1 
ATOM   340  O  OG  . SER A  1 44  ? 40.117 3.318   19.029  1.00 14.69  ? 43  SER A OG  1 
ATOM   341  N  N   . LEU A  1 45  ? 37.265 4.944   19.457  1.00 11.31  ? 44  LEU A N   1 
ATOM   342  C  CA  . LEU A  1 45  ? 36.363 5.469   18.429  1.00 11.69  ? 44  LEU A CA  1 
ATOM   343  C  C   . LEU A  1 45  ? 35.984 6.907   18.721  1.00 14.14  ? 44  LEU A C   1 
ATOM   344  O  O   . LEU A  1 45  ? 35.833 7.271   19.886  1.00 20.55  ? 44  LEU A O   1 
ATOM   345  C  CB  . LEU A  1 45  ? 35.105 4.657   18.324  1.00 12.44  ? 44  LEU A CB  1 
ATOM   346  C  CG  . LEU A  1 45  ? 35.288 3.246   17.798  1.00 12.17  ? 44  LEU A CG  1 
ATOM   347  C  CD1 . LEU A  1 45  ? 34.021 2.442   17.966  1.00 15.03  ? 44  LEU A CD1 1 
ATOM   348  C  CD2 . LEU A  1 45  ? 35.746 3.185   16.317  1.00 12.95  ? 44  LEU A CD2 1 
ATOM   349  N  N   . LYS A  1 46  ? 35.962 7.779   17.780  1.00 12.26  ? 45  LYS A N   1 
ATOM   350  C  CA  . LYS A  1 46  ? 35.456 9.106   17.935  1.00 12.40  ? 45  LYS A CA  1 
ATOM   351  C  C   . LYS A  1 46  ? 34.027 9.186   17.383  1.00 11.44  ? 45  LYS A C   1 
ATOM   352  O  O   . LYS A  1 46  ? 33.648 8.337   16.618  1.00 11.35  ? 45  LYS A O   1 
ATOM   353  C  CB  . LYS A  1 46  ? 36.347 10.052  17.184  1.00 15.03  ? 45  LYS A CB  1 
ATOM   354  C  CG  . LYS A  1 46  ? 37.654 10.288  18.016  1.00 21.93  ? 45  LYS A CG  1 
ATOM   355  C  CD  . LYS A  1 46  ? 38.442 11.371  17.389  1.00 25.36  ? 45  LYS A CD  1 
ATOM   356  C  CE  . LYS A  1 46  ? 39.534 11.747  18.314  1.00 22.70  ? 45  LYS A CE  1 
ATOM   357  N  NZ  . LYS A  1 46  ? 40.351 12.875  17.923  1.00 25.50  ? 45  LYS A NZ  1 
ATOM   358  N  N   . PRO A  1 47  ? 33.270 10.246  17.719  1.00 12.26  ? 46  PRO A N   1 
ATOM   359  C  CA  . PRO A  1 47  ? 32.033 10.437  16.983  1.00 11.89  ? 46  PRO A CA  1 
ATOM   360  C  C   . PRO A  1 47  ? 32.294 10.559  15.499  1.00 10.99  ? 46  PRO A C   1 
ATOM   361  O  O   . PRO A  1 47  ? 33.345 11.050  15.057  1.00 11.92  ? 46  PRO A O   1 
ATOM   362  C  CB  . PRO A  1 47  ? 31.448 11.731  17.576  1.00 14.57  ? 46  PRO A CB  1 
ATOM   363  C  CG  . PRO A  1 47  ? 32.162 11.878  18.960  1.00 18.56  ? 46  PRO A CG  1 
ATOM   364  C  CD  . PRO A  1 47  ? 33.538 11.304  18.690  1.00 15.60  ? 46  PRO A CD  1 
ATOM   365  N  N   A ILE A  1 48  ? 31.281 10.166  14.730  0.50 11.48  ? 47  ILE A N   1 
ATOM   366  N  N   B ILE A  1 48  ? 31.368 10.122  14.648  0.50 11.93  ? 47  ILE A N   1 
ATOM   367  C  CA  A ILE A  1 48  ? 31.204 10.447  13.300  0.50 10.64  ? 47  ILE A CA  1 
ATOM   368  C  CA  B ILE A  1 48  ? 31.594 10.480  13.240  0.50 12.03  ? 47  ILE A CA  1 
ATOM   369  C  C   A ILE A  1 48  ? 30.981 11.938  13.002  0.50 11.12  ? 47  ILE A C   1 
ATOM   370  C  C   B ILE A  1 48  ? 31.057 11.852  12.993  0.50 11.55  ? 47  ILE A C   1 
ATOM   371  O  O   A ILE A  1 48  ? 30.173 12.576  13.671  0.50 13.90  ? 47  ILE A O   1 
ATOM   372  O  O   B ILE A  1 48  ? 30.140 12.306  13.692  0.50 15.50  ? 47  ILE A O   1 
ATOM   373  C  CB  A ILE A  1 48  ? 29.984 9.653   12.704  0.50 12.10  ? 47  ILE A CB  1 
ATOM   374  C  CB  B ILE A  1 48  ? 30.945 9.529   12.190  0.50 15.28  ? 47  ILE A CB  1 
ATOM   375  C  CG1 A ILE A  1 48  ? 30.253 8.221   12.777  0.50 13.81  ? 47  ILE A CG1 1 
ATOM   376  C  CG1 B ILE A  1 48  ? 29.477 9.326   12.439  0.50 15.85  ? 47  ILE A CG1 1 
ATOM   377  C  CG2 A ILE A  1 48  ? 29.798 10.071  11.248  0.50 12.05  ? 47  ILE A CG2 1 
ATOM   378  C  CG2 B ILE A  1 48  ? 31.751 8.238   12.055  0.50 18.20  ? 47  ILE A CG2 1 
ATOM   379  C  CD1 A ILE A  1 48  ? 31.409 7.667   11.976  0.50 16.05  ? 47  ILE A CD1 1 
ATOM   380  C  CD1 B ILE A  1 48  ? 28.662 8.810   11.190  0.50 17.64  ? 47  ILE A CD1 1 
ATOM   381  N  N   . SER A  1 49  ? 31.671 12.464  11.997  1.00 11.50  ? 48  SER A N   1 
ATOM   382  C  CA  . SER A  1 49  ? 31.440 13.815  11.599  1.00 14.92  ? 48  SER A CA  1 
ATOM   383  C  C   . SER A  1 49  ? 31.209 13.793  10.094  1.00 12.31  ? 48  SER A C   1 
ATOM   384  O  O   . SER A  1 49  ? 32.005 13.266  9.326   1.00 14.33  ? 48  SER A O   1 
ATOM   385  C  CB  . SER A  1 49  ? 32.660 14.662  11.958  1.00 20.53  ? 48  SER A CB  1 
ATOM   386  O  OG  . SER A  1 49  ? 32.689 15.868  11.228  1.00 30.05  ? 48  SER A OG  1 
ATOM   387  N  N   . VAL A  1 50  ? 30.052 14.266  9.679   1.00 11.69  ? 49  VAL A N   1 
ATOM   388  C  CA  . VAL A  1 50  ? 29.772 14.394  8.271   1.00 11.42  ? 49  VAL A CA  1 
ATOM   389  C  C   . VAL A  1 50  ? 29.742 15.875  7.947   1.00 13.12  ? 49  VAL A C   1 
ATOM   390  O  O   . VAL A  1 50  ? 29.148 16.680  8.671   1.00 16.47  ? 49  VAL A O   1 
ATOM   391  C  CB  . VAL A  1 50  ? 28.505 13.655  7.798   1.00 15.56  ? 49  VAL A CB  1 
ATOM   392  C  CG1 . VAL A  1 50  ? 28.774 12.145  7.876   1.00 16.31  ? 49  VAL A CG1 1 
ATOM   393  C  CG2 . VAL A  1 50  ? 27.297 14.041  8.633   1.00 20.63  ? 49  VAL A CG2 1 
ATOM   394  N  N   . SER A  1 51  ? 30.470 16.216  6.930   1.00 11.00  ? 50  SER A N   1 
ATOM   395  C  CA  . SER A  1 51  ? 30.567 17.642  6.508   1.00 13.36  ? 50  SER A CA  1 
ATOM   396  C  C   . SER A  1 51  ? 30.383 17.631  4.995   1.00 10.94  ? 50  SER A C   1 
ATOM   397  O  O   . SER A  1 51  ? 31.382 17.562  4.270   1.00 11.42  ? 50  SER A O   1 
ATOM   398  C  CB  . SER A  1 51  ? 31.949 18.209  6.932   1.00 15.35  ? 50  SER A CB  1 
ATOM   399  O  OG  . SER A  1 51  ? 31.947 19.567  6.571   1.00 21.64  ? 50  SER A OG  1 
ATOM   400  N  N   . TYR A  1 52  ? 29.134 17.679  4.559   1.00 10.21  ? 51  TYR A N   1 
ATOM   401  C  CA  . TYR A  1 52  ? 28.838 17.605  3.125   1.00 9.00   ? 51  TYR A CA  1 
ATOM   402  C  C   . TYR A  1 52  ? 28.463 18.952  2.585   1.00 10.27  ? 51  TYR A C   1 
ATOM   403  O  O   . TYR A  1 52  ? 27.819 19.772  3.260   1.00 16.51  ? 51  TYR A O   1 
ATOM   404  C  CB  . TYR A  1 52  ? 27.726 16.596  2.858   1.00 9.35   ? 51  TYR A CB  1 
ATOM   405  C  CG  . TYR A  1 52  ? 27.958 15.192  3.372   1.00 8.54   ? 51  TYR A CG  1 
ATOM   406  C  CD1 . TYR A  1 52  ? 29.240 14.592  3.464   1.00 8.77   ? 51  TYR A CD1 1 
ATOM   407  C  CD2 . TYR A  1 52  ? 26.866 14.438  3.744   1.00 9.42   ? 51  TYR A CD2 1 
ATOM   408  C  CE1 . TYR A  1 52  ? 29.387 13.295  3.866   1.00 8.60   ? 51  TYR A CE1 1 
ATOM   409  C  CE2 . TYR A  1 52  ? 26.985 13.107  4.131   1.00 8.93   ? 51  TYR A CE2 1 
ATOM   410  C  CZ  . TYR A  1 52  ? 28.255 12.547  4.148   1.00 8.40   ? 51  TYR A CZ  1 
ATOM   411  O  OH  . TYR A  1 52  ? 28.339 11.219  4.576   1.00 9.67   ? 51  TYR A OH  1 
ATOM   412  N  N   . ASN A  1 53  ? 28.788 19.204  1.362   1.00 10.08  ? 52  ASN A N   1 
ATOM   413  C  CA  . ASN A  1 53  ? 28.459 20.487  0.732   1.00 10.03  ? 52  ASN A CA  1 
ATOM   414  C  C   . ASN A  1 53  ? 27.367 20.193  -0.299  1.00 9.15   ? 52  ASN A C   1 
ATOM   415  O  O   . ASN A  1 53  ? 27.572 19.365  -1.204  1.00 9.84   ? 52  ASN A O   1 
ATOM   416  C  CB  . ASN A  1 53  ? 29.754 20.959  0.054   1.00 11.23  ? 52  ASN A CB  1 
ATOM   417  C  CG  . ASN A  1 53  ? 29.609 22.236  -0.682  1.00 11.18  ? 52  ASN A CG  1 
ATOM   418  O  OD1 . ASN A  1 53  ? 28.533 22.564  -1.230  1.00 11.78  ? 52  ASN A OD1 1 
ATOM   419  N  ND2 . ASN A  1 53  ? 30.702 22.999  -0.712  1.00 12.88  ? 52  ASN A ND2 1 
ATOM   420  N  N   . PRO A  1 54  ? 26.180 20.799  -0.181  1.00 9.87   ? 53  PRO A N   1 
ATOM   421  C  CA  . PRO A  1 54  ? 25.056 20.408  -1.059  1.00 10.32  ? 53  PRO A CA  1 
ATOM   422  C  C   . PRO A  1 54  ? 25.358 20.686  -2.544  1.00 9.57   ? 53  PRO A C   1 
ATOM   423  O  O   . PRO A  1 54  ? 24.710 20.085  -3.386  1.00 10.89  ? 53  PRO A O   1 
ATOM   424  C  CB  . PRO A  1 54  ? 23.890 21.259  -0.556  1.00 11.39  ? 53  PRO A CB  1 
ATOM   425  C  CG  . PRO A  1 54  ? 24.597 22.476  0.117   1.00 11.86  ? 53  PRO A CG  1 
ATOM   426  C  CD  . PRO A  1 54  ? 25.847 21.882  0.776   1.00 10.75  ? 53  PRO A CD  1 
ATOM   427  N  N   . ALA A  1 55  ? 26.301 21.587  -2.848  1.00 10.46  ? 54  ALA A N   1 
ATOM   428  C  CA  . ALA A  1 55  ? 26.648 21.885  -4.246  1.00 11.00  ? 54  ALA A CA  1 
ATOM   429  C  C   . ALA A  1 55  ? 27.417 20.784  -4.857  1.00 10.85  ? 54  ALA A C   1 
ATOM   430  O  O   . ALA A  1 55  ? 27.695 20.838  -6.071  1.00 13.25  ? 54  ALA A O   1 
ATOM   431  C  CB  . ALA A  1 55  ? 27.432 23.206  -4.317  1.00 13.30  ? 54  ALA A CB  1 
ATOM   432  N  N   . THR A  1 56  ? 27.845 19.742  -4.109  1.00 9.87   ? 55  THR A N   1 
ATOM   433  C  CA  . THR A  1 56  ? 28.458 18.608  -4.720  1.00 9.62   ? 55  THR A CA  1 
ATOM   434  C  C   . THR A  1 56  ? 27.458 17.590  -5.285  1.00 8.81   ? 55  THR A C   1 
ATOM   435  O  O   . THR A  1 56  ? 27.892 16.687  -6.032  1.00 9.50   ? 55  THR A O   1 
ATOM   436  C  CB  . THR A  1 56  ? 29.470 17.920  -3.801  1.00 9.72   ? 55  THR A CB  1 
ATOM   437  O  OG1 . THR A  1 56  ? 28.839 17.418  -2.604  1.00 9.39   ? 55  THR A OG1 1 
ATOM   438  C  CG2 . THR A  1 56  ? 30.622 18.842  -3.458  1.00 12.16  ? 55  THR A CG2 1 
ATOM   439  N  N   . ALA A  1 57  ? 26.177 17.697  -4.991  1.00 9.48   ? 56  ALA A N   1 
ATOM   440  C  CA  . ALA A  1 57  ? 25.225 16.752  -5.623  1.00 9.08   ? 56  ALA A CA  1 
ATOM   441  C  C   . ALA A  1 57  ? 25.319 16.943  -7.150  1.00 8.87   ? 56  ALA A C   1 
ATOM   442  O  O   . ALA A  1 57  ? 25.299 18.084  -7.604  1.00 10.04  ? 56  ALA A O   1 
ATOM   443  C  CB  . ALA A  1 57  ? 23.852 17.042  -5.067  1.00 10.50  ? 56  ALA A CB  1 
ATOM   444  N  N   . LYS A  1 58  ? 25.336 15.840  -7.864  1.00 9.13   ? 57  LYS A N   1 
ATOM   445  C  CA  . LYS A  1 58  ? 25.516 15.916  -9.332  1.00 9.54   ? 57  LYS A CA  1 
ATOM   446  C  C   . LYS A  1 58  ? 24.395 15.272  -10.135 1.00 9.37   ? 57  LYS A C   1 
ATOM   447  O  O   . LYS A  1 58  ? 23.826 15.937  -11.016 1.00 10.95  ? 57  LYS A O   1 
ATOM   448  C  CB  . LYS A  1 58  ? 26.870 15.284  -9.699  1.00 12.43  ? 57  LYS A CB  1 
ATOM   449  C  CG  . LYS A  1 58  ? 27.318 15.461  -11.111 1.00 16.36  ? 57  LYS A CG  1 
ATOM   450  C  CD  . LYS A  1 58  ? 28.701 14.754  -11.291 1.00 19.00  ? 57  LYS A CD  1 
ATOM   451  C  CE  . LYS A  1 58  ? 29.337 15.232  -12.598 1.00 29.94  ? 57  LYS A CE  1 
ATOM   452  N  NZ  . LYS A  1 58  ? 30.485 14.387  -12.947 1.00 37.15  ? 57  LYS A NZ  1 
ATOM   453  N  N   A GLU A  1 59  ? 24.103 13.983  -9.962  0.50 8.86   ? 58  GLU A N   1 
ATOM   454  N  N   B GLU A  1 59  ? 24.146 13.972  -9.977  0.50 8.98   ? 58  GLU A N   1 
ATOM   455  C  CA  A GLU A  1 59  ? 23.341 13.267  -10.975 0.50 9.37   ? 58  GLU A CA  1 
ATOM   456  C  CA  B GLU A  1 59  ? 23.348 13.264  -10.965 0.50 9.36   ? 58  GLU A CA  1 
ATOM   457  C  C   A GLU A  1 59  ? 22.685 12.071  -10.328 0.50 8.32   ? 58  GLU A C   1 
ATOM   458  C  C   B GLU A  1 59  ? 22.689 12.057  -10.333 0.50 8.36   ? 58  GLU A C   1 
ATOM   459  O  O   A GLU A  1 59  ? 23.286 11.474  -9.452  0.50 11.03  ? 58  GLU A O   1 
ATOM   460  O  O   B GLU A  1 59  ? 23.267 11.478  -9.429  0.50 10.97  ? 58  GLU A O   1 
ATOM   461  C  CB  A GLU A  1 59  ? 24.303 12.774  -12.127 0.50 11.75  ? 58  GLU A CB  1 
ATOM   462  C  CB  B GLU A  1 59  ? 24.298 12.778  -12.127 0.50 11.95  ? 58  GLU A CB  1 
ATOM   463  C  CG  A GLU A  1 59  ? 23.641 12.232  -13.375 0.50 13.09  ? 58  GLU A CG  1 
ATOM   464  C  CG  B GLU A  1 59  ? 23.587 12.195  -13.333 0.50 13.73  ? 58  GLU A CG  1 
ATOM   465  C  CD  A GLU A  1 59  ? 24.661 12.026  -14.470 0.50 12.69  ? 58  GLU A CD  1 
ATOM   466  C  CD  B GLU A  1 59  ? 24.511 11.927  -14.490 0.50 15.42  ? 58  GLU A CD  1 
ATOM   467  O  OE1 A GLU A  1 59  ? 24.273 12.219  -15.602 0.50 13.06  ? 58  GLU A OE1 1 
ATOM   468  O  OE1 B GLU A  1 59  ? 25.189 10.852  -14.536 0.50 19.82  ? 58  GLU A OE1 1 
ATOM   469  O  OE2 A GLU A  1 59  ? 25.892 11.727  -14.187 0.50 13.19  ? 58  GLU A OE2 1 
ATOM   470  O  OE2 B GLU A  1 59  ? 24.530 12.788  -15.356 0.50 25.64  ? 58  GLU A OE2 1 
ATOM   471  N  N   . ILE A  1 60  ? 21.490 11.705  -10.795 1.00 8.46   ? 59  ILE A N   1 
ATOM   472  C  CA  . ILE A  1 60  ? 20.804 10.468  -10.415 1.00 8.69   ? 59  ILE A CA  1 
ATOM   473  C  C   . ILE A  1 60  ? 20.762 9.538   -11.620 1.00 8.55   ? 59  ILE A C   1 
ATOM   474  O  O   . ILE A  1 60  ? 20.530 10.039  -12.741 1.00 9.50   ? 59  ILE A O   1 
ATOM   475  C  CB  . ILE A  1 60  ? 19.439 10.792  -9.785  1.00 9.00   ? 59  ILE A CB  1 
ATOM   476  C  CG1 . ILE A  1 60  ? 18.820 9.575   -9.124  1.00 9.10   ? 59  ILE A CG1 1 
ATOM   477  C  CG2 . ILE A  1 60  ? 18.475 11.486  -10.766 1.00 10.28  ? 59  ILE A CG2 1 
ATOM   478  C  CD1 . ILE A  1 60  ? 17.551 9.829   -8.348  1.00 10.90  ? 59  ILE A CD1 1 
ATOM   479  N  N   A ILE A  1 61  ? 21.029 8.263   -11.420 0.50 8.32   ? 60  ILE A N   1 
ATOM   480  N  N   B ILE A  1 61  ? 21.009 8.265   -11.423 0.50 8.37   ? 60  ILE A N   1 
ATOM   481  C  CA  A ILE A  1 61  ? 21.344 7.322   -12.501 0.50 8.07   ? 60  ILE A CA  1 
ATOM   482  C  CA  B ILE A  1 61  ? 21.159 7.362   -12.563 0.50 9.40   ? 60  ILE A CA  1 
ATOM   483  C  C   A ILE A  1 61  ? 20.601 6.006   -12.215 0.50 8.01   ? 60  ILE A C   1 
ATOM   484  C  C   B ILE A  1 61  ? 20.567 6.007   -12.216 0.50 8.07   ? 60  ILE A C   1 
ATOM   485  O  O   A ILE A  1 61  ? 20.711 5.486   -11.113 0.50 8.30   ? 60  ILE A O   1 
ATOM   486  O  O   B ILE A  1 61  ? 20.731 5.479   -11.113 0.50 8.32   ? 60  ILE A O   1 
ATOM   487  C  CB  A ILE A  1 61  ? 22.861 7.021   -12.652 0.50 8.55   ? 60  ILE A CB  1 
ATOM   488  C  CB  B ILE A  1 61  ? 22.620 7.158   -12.869 0.50 10.56  ? 60  ILE A CB  1 
ATOM   489  C  CG1 A ILE A  1 61  ? 23.723 8.295   -12.898 0.50 7.74   ? 60  ILE A CG1 1 
ATOM   490  C  CG1 B ILE A  1 61  ? 22.792 6.125   -13.999 0.50 14.58  ? 60  ILE A CG1 1 
ATOM   491  C  CG2 A ILE A  1 61  ? 23.115 6.133   -13.896 0.50 10.67  ? 60  ILE A CG2 1 
ATOM   492  C  CG2 B ILE A  1 61  ? 23.319 6.698   -11.664 0.50 12.36  ? 60  ILE A CG2 1 
ATOM   493  C  CD1 A ILE A  1 61  ? 25.262 8.019   -12.719 0.50 11.98  ? 60  ILE A CD1 1 
ATOM   494  C  CD1 B ILE A  1 61  ? 24.135 6.254   -14.485 0.50 18.49  ? 60  ILE A CD1 1 
ATOM   495  N  N   . ASN A  1 62  ? 19.859 5.434   -13.181 1.00 8.21   ? 61  ASN A N   1 
ATOM   496  C  CA  . ASN A  1 62  ? 19.328 4.104   -13.090 1.00 8.68   ? 61  ASN A CA  1 
ATOM   497  C  C   . ASN A  1 62  ? 20.395 3.107   -13.593 1.00 8.60   ? 61  ASN A C   1 
ATOM   498  O  O   . ASN A  1 62  ? 20.777 3.166   -14.751 1.00 9.13   ? 61  ASN A O   1 
ATOM   499  C  CB  . ASN A  1 62  ? 18.036 4.012   -13.921 1.00 8.82   ? 61  ASN A CB  1 
ATOM   500  C  CG  . ASN A  1 62  ? 17.396 2.662   -13.913 1.00 8.45   ? 61  ASN A CG  1 
ATOM   501  O  OD1 . ASN A  1 62  ? 18.064 1.646   -13.865 1.00 9.37   ? 61  ASN A OD1 1 
ATOM   502  N  ND2 . ASN A  1 62  ? 16.041 2.623   -13.964 1.00 9.67   ? 61  ASN A ND2 1 
ATOM   503  N  N   . VAL A  1 63  ? 20.874 2.293   -12.672 1.00 8.91   ? 62  VAL A N   1 
ATOM   504  C  CA  . VAL A  1 63  ? 21.975 1.343   -13.006 1.00 9.29   ? 62  VAL A CA  1 
ATOM   505  C  C   . VAL A  1 63  ? 21.406 -0.078  -13.191 1.00 9.20   ? 62  VAL A C   1 
ATOM   506  O  O   . VAL A  1 63  ? 22.171 -1.058  -13.136 1.00 11.22  ? 62  VAL A O   1 
ATOM   507  C  CB  . VAL A  1 63  ? 23.114 1.399   -11.986 1.00 10.80  ? 62  VAL A CB  1 
ATOM   508  C  CG1 . VAL A  1 63  ? 23.709 2.814   -11.977 1.00 13.74  ? 62  VAL A CG1 1 
ATOM   509  C  CG2 . VAL A  1 63  ? 22.698 0.980   -10.564 1.00 11.61  ? 62  VAL A CG2 1 
ATOM   510  N  N   . GLY A  1 64  ? 20.106 -0.219  -13.450 1.00 9.11   ? 63  GLY A N   1 
ATOM   511  C  CA  . GLY A  1 64  ? 19.565 -1.534  -13.819 1.00 9.35   ? 63  GLY A CA  1 
ATOM   512  C  C   . GLY A  1 64  ? 19.093 -2.337  -12.648 1.00 9.08   ? 63  GLY A C   1 
ATOM   513  O  O   . GLY A  1 64  ? 17.954 -2.798  -12.614 1.00 11.83  ? 63  GLY A O   1 
ATOM   514  N  N   . HIS A  1 65  ? 19.972 -2.532  -11.650 1.00 8.66   ? 64  HIS A N   1 
ATOM   515  C  CA  . HIS A  1 65  ? 19.600 -3.240  -10.467 1.00 9.85   ? 64  HIS A CA  1 
ATOM   516  C  C   . HIS A  1 65  ? 19.252 -2.286  -9.327  1.00 9.07   ? 64  HIS A C   1 
ATOM   517  O  O   . HIS A  1 65  ? 18.748 -2.763  -8.270  1.00 9.18   ? 64  HIS A O   1 
ATOM   518  C  CB  . HIS A  1 65  ? 20.764 -4.182  -10.005 1.00 10.21  ? 64  HIS A CB  1 
ATOM   519  C  CG  . HIS A  1 65  ? 22.036 -3.445  -9.752  1.00 9.68   ? 64  HIS A CG  1 
ATOM   520  N  ND1 . HIS A  1 65  ? 22.349 -2.916  -8.493  1.00 10.45  ? 64  HIS A ND1 1 
ATOM   521  C  CD2 . HIS A  1 65  ? 23.061 -3.162  -10.583 1.00 11.64  ? 64  HIS A CD2 1 
ATOM   522  C  CE1 . HIS A  1 65  ? 23.520 -2.288  -8.610  1.00 11.15  ? 64  HIS A CE1 1 
ATOM   523  N  NE2 . HIS A  1 65  ? 23.960 -2.419  -9.864  1.00 11.51  ? 64  HIS A NE2 1 
ATOM   524  N  N   . SER A  1 66  ? 19.530 -1.009  -9.475  1.00 8.87   ? 65  SER A N   1 
ATOM   525  C  CA  . SER A  1 66  ? 19.316 -0.032  -8.413  1.00 8.55   ? 65  SER A CA  1 
ATOM   526  C  C   . SER A  1 66  ? 19.362 1.331   -9.092  1.00 8.45   ? 65  SER A C   1 
ATOM   527  O  O   . SER A  1 66  ? 19.354 1.455   -10.350 1.00 8.90   ? 65  SER A O   1 
ATOM   528  C  CB  . SER A  1 66  ? 20.420 -0.188  -7.395  1.00 9.46   ? 65  SER A CB  1 
ATOM   529  O  OG  . SER A  1 66  ? 20.079 0.584   -6.257  1.00 10.23  ? 65  SER A OG  1 
ATOM   530  N  N   . PHE A  1 67  ? 19.398 2.404   -8.260  1.00 7.79   ? 66  PHE A N   1 
ATOM   531  C  CA  . PHE A  1 67  ? 19.701 3.712   -8.760  1.00 7.62   ? 66  PHE A CA  1 
ATOM   532  C  C   . PHE A  1 67  ? 20.686 4.350   -7.810  1.00 7.30   ? 66  PHE A C   1 
ATOM   533  O  O   . PHE A  1 67  ? 20.725 4.019   -6.626  1.00 8.23   ? 66  PHE A O   1 
ATOM   534  C  CB  . PHE A  1 67  ? 18.460 4.600   -8.936  1.00 8.18   ? 66  PHE A CB  1 
ATOM   535  C  CG  . PHE A  1 67  ? 17.814 5.057   -7.625  1.00 7.93   ? 66  PHE A CG  1 
ATOM   536  C  CD1 . PHE A  1 67  ? 16.921 4.226   -6.948  1.00 9.62   ? 66  PHE A CD1 1 
ATOM   537  C  CD2 . PHE A  1 67  ? 18.203 6.264   -7.065  1.00 9.74   ? 66  PHE A CD2 1 
ATOM   538  C  CE1 . PHE A  1 67  ? 16.389 4.659   -5.695  1.00 10.46  ? 66  PHE A CE1 1 
ATOM   539  C  CE2 . PHE A  1 67  ? 17.636 6.679   -5.856  1.00 10.49  ? 66  PHE A CE2 1 
ATOM   540  C  CZ  . PHE A  1 67  ? 16.710 5.892   -5.195  1.00 10.45  ? 66  PHE A CZ  1 
ATOM   541  N  N   . HIS A  1 68  ? 21.482 5.268   -8.358  1.00 8.04   ? 67  HIS A N   1 
ATOM   542  C  CA  . HIS A  1 68  ? 22.539 5.957   -7.629  1.00 10.17  ? 67  HIS A CA  1 
ATOM   543  C  C   . HIS A  1 68  ? 22.493 7.478   -7.700  1.00 8.42   ? 67  HIS A C   1 
ATOM   544  O  O   . HIS A  1 68  ? 22.307 8.044   -8.777  1.00 9.96   ? 67  HIS A O   1 
ATOM   545  C  CB  . HIS A  1 68  ? 23.887 5.604   -8.270  1.00 12.62  ? 67  HIS A CB  1 
ATOM   546  C  CG  . HIS A  1 68  ? 24.337 4.196   -8.050  1.00 13.07  ? 67  HIS A CG  1 
ATOM   547  N  ND1 . HIS A  1 68  ? 25.430 3.708   -8.649  1.00 15.98  ? 67  HIS A ND1 1 
ATOM   548  C  CD2 . HIS A  1 68  ? 23.824 3.203   -7.260  1.00 13.27  ? 67  HIS A CD2 1 
ATOM   549  C  CE1 . HIS A  1 68  ? 25.594 2.435   -8.257  1.00 17.91  ? 67  HIS A CE1 1 
ATOM   550  N  NE2 . HIS A  1 68  ? 24.626 2.096   -7.402  1.00 15.53  ? 67  HIS A NE2 1 
ATOM   551  N  N   . VAL A  1 69  ? 22.665 8.146   -6.562  1.00 8.38   ? 68  VAL A N   1 
ATOM   552  C  CA  . VAL A  1 69  ? 22.801 9.599   -6.592  1.00 8.57   ? 68  VAL A CA  1 
ATOM   553  C  C   . VAL A  1 69  ? 24.295 9.895   -6.429  1.00 8.55   ? 68  VAL A C   1 
ATOM   554  O  O   . VAL A  1 69  ? 24.875 9.625   -5.375  1.00 9.10   ? 68  VAL A O   1 
ATOM   555  C  CB  . VAL A  1 69  ? 21.983 10.325  -5.533  1.00 10.00  ? 68  VAL A CB  1 
ATOM   556  C  CG1 . VAL A  1 69  ? 22.294 11.792  -5.590  1.00 12.79  ? 68  VAL A CG1 1 
ATOM   557  C  CG2 . VAL A  1 69  ? 20.476 10.001  -5.694  1.00 13.81  ? 68  VAL A CG2 1 
ATOM   558  N  N   A ASN A  1 70  ? 24.926 10.374  -7.521  0.50 9.82   ? 69  ASN A N   1 
ATOM   559  N  N   B ASN A  1 70  ? 24.952 10.367  -7.503  0.50 9.57   ? 69  ASN A N   1 
ATOM   560  C  CA  A ASN A  1 70  ? 26.343 10.676  -7.550  0.50 9.50   ? 69  ASN A CA  1 
ATOM   561  C  CA  B ASN A  1 70  ? 26.373 10.637  -7.504  0.50 10.10  ? 69  ASN A CA  1 
ATOM   562  C  C   A ASN A  1 70  ? 26.630 12.096  -7.136  0.50 8.81   ? 69  ASN A C   1 
ATOM   563  C  C   B ASN A  1 70  ? 26.668 12.090  -7.174  0.50 8.94   ? 69  ASN A C   1 
ATOM   564  O  O   A ASN A  1 70  ? 25.835 13.029  -7.446  0.50 9.11   ? 69  ASN A O   1 
ATOM   565  O  O   B ASN A  1 70  ? 25.897 13.027  -7.494  0.50 9.49   ? 69  ASN A O   1 
ATOM   566  C  CB  A ASN A  1 70  ? 26.914 10.539  -8.978  0.50 10.99  ? 69  ASN A CB  1 
ATOM   567  C  CB  B ASN A  1 70  ? 26.939 10.238  -8.874  0.50 11.05  ? 69  ASN A CB  1 
ATOM   568  C  CG  A ASN A  1 70  ? 27.293 9.112   -9.340  0.50 13.82  ? 69  ASN A CG  1 
ATOM   569  C  CG  B ASN A  1 70  ? 26.897 8.700   -9.046  0.50 15.49  ? 69  ASN A CG  1 
ATOM   570  O  OD1 A ASN A  1 70  ? 27.096 8.150   -8.536  0.50 15.35  ? 69  ASN A OD1 1 
ATOM   571  O  OD1 B ASN A  1 70  ? 26.288 8.133   -9.991  0.50 18.64  ? 69  ASN A OD1 1 
ATOM   572  N  ND2 A ASN A  1 70  ? 27.803 8.947   -10.619 0.50 11.76  ? 69  ASN A ND2 1 
ATOM   573  N  ND2 B ASN A  1 70  ? 27.600 8.033   -8.165  0.50 19.03  ? 69  ASN A ND2 1 
ATOM   574  N  N   . PHE A  1 71  ? 27.785 12.271  -6.513  1.00 8.67   ? 70  PHE A N   1 
ATOM   575  C  CA  . PHE A  1 71  ? 28.329 13.558  -6.130  1.00 9.38   ? 70  PHE A CA  1 
ATOM   576  C  C   . PHE A  1 71  ? 29.600 13.876  -6.888  1.00 10.20  ? 70  PHE A C   1 
ATOM   577  O  O   . PHE A  1 71  ? 30.347 12.945  -7.277  1.00 12.76  ? 70  PHE A O   1 
ATOM   578  C  CB  . PHE A  1 71  ? 28.593 13.588  -4.577  1.00 9.65   ? 70  PHE A CB  1 
ATOM   579  C  CG  . PHE A  1 71  ? 27.292 13.605  -3.828  1.00 8.25   ? 70  PHE A CG  1 
ATOM   580  C  CD1 . PHE A  1 71  ? 26.502 12.445  -3.773  1.00 11.21  ? 70  PHE A CD1 1 
ATOM   581  C  CD2 . PHE A  1 71  ? 26.805 14.746  -3.251  1.00 9.08   ? 70  PHE A CD2 1 
ATOM   582  C  CE1 . PHE A  1 71  ? 25.242 12.501  -3.213  1.00 14.05  ? 70  PHE A CE1 1 
ATOM   583  C  CE2 . PHE A  1 71  ? 25.570 14.787  -2.659  1.00 10.00  ? 70  PHE A CE2 1 
ATOM   584  C  CZ  . PHE A  1 71  ? 24.814 13.690  -2.649  1.00 11.85  ? 70  PHE A CZ  1 
ATOM   585  N  N   A GLU A  1 72  ? 29.827 15.148  -7.018  0.50 9.58   ? 71  GLU A N   1 
ATOM   586  N  N   B GLU A  1 72  ? 29.925 15.127  -7.100  0.50 9.55   ? 71  GLU A N   1 
ATOM   587  C  CA  A GLU A  1 72  ? 30.983 15.589  -7.754  0.50 9.70   ? 71  GLU A CA  1 
ATOM   588  C  CA  B GLU A  1 72  ? 31.252 15.484  -7.697  0.50 12.97  ? 71  GLU A CA  1 
ATOM   589  C  C   A GLU A  1 72  ? 32.244 15.023  -7.188  0.50 9.37   ? 71  GLU A C   1 
ATOM   590  C  C   B GLU A  1 72  ? 32.394 14.969  -6.776  0.50 14.76  ? 71  GLU A C   1 
ATOM   591  O  O   A GLU A  1 72  ? 32.509 15.105  -5.958  0.50 13.63  ? 71  GLU A O   1 
ATOM   592  O  O   B GLU A  1 72  ? 32.352 15.255  -5.589  0.50 13.41  ? 71  GLU A O   1 
ATOM   593  C  CB  A GLU A  1 72  ? 31.028 17.101  -7.753  0.50 10.00  ? 71  GLU A CB  1 
ATOM   594  C  CB  B GLU A  1 72  ? 31.340 17.056  -7.800  0.50 14.49  ? 71  GLU A CB  1 
ATOM   595  C  CG  A GLU A  1 72  ? 30.129 17.588  -8.866  0.50 17.63  ? 71  GLU A CG  1 
ATOM   596  C  CG  B GLU A  1 72  ? 30.085 17.704  -8.342  0.50 17.96  ? 71  GLU A CG  1 
ATOM   597  C  CD  A GLU A  1 72  ? 30.251 19.086  -9.125  0.50 19.47  ? 71  GLU A CD  1 
ATOM   598  C  CD  B GLU A  1 72  ? 30.162 17.786  -9.860  0.50 20.90  ? 71  GLU A CD  1 
ATOM   599  O  OE1 A GLU A  1 72  ? 31.206 19.602  -8.598  0.50 26.83  ? 71  GLU A OE1 1 
ATOM   600  O  OE1 B GLU A  1 72  ? 31.182 17.256  -10.412 0.50 23.51  ? 71  GLU A OE1 1 
ATOM   601  O  OE2 A GLU A  1 72  ? 29.442 19.673  -9.887  0.50 26.82  ? 71  GLU A OE2 1 
ATOM   602  O  OE2 B GLU A  1 72  ? 29.205 18.384  -10.462 0.50 21.71  ? 71  GLU A OE2 1 
ATOM   603  N  N   A ASP A  1 73  ? 33.059 14.430  -8.073  0.50 10.54  ? 72  ASP A N   1 
ATOM   604  N  N   B ASP A  1 73  ? 33.397 14.189  -7.204  0.50 16.77  ? 72  ASP A N   1 
ATOM   605  C  CA  A ASP A  1 73  ? 34.194 13.605  -7.549  0.50 9.13   ? 72  ASP A CA  1 
ATOM   606  C  CA  B ASP A  1 73  ? 34.349 13.652  -6.165  0.50 15.72  ? 72  ASP A CA  1 
ATOM   607  C  C   A ASP A  1 73  ? 35.463 14.284  -7.960  0.50 8.77   ? 72  ASP A C   1 
ATOM   608  C  C   B ASP A  1 73  ? 35.775 14.190  -6.581  0.50 16.04  ? 72  ASP A C   1 
ATOM   609  O  O   A ASP A  1 73  ? 36.342 13.662  -8.522  0.50 10.52  ? 72  ASP A O   1 
ATOM   610  O  O   B ASP A  1 73  ? 36.690 13.331  -6.169  0.50 20.07  ? 72  ASP A O   1 
ATOM   611  C  CB  A ASP A  1 73  ? 34.056 12.170  -8.008  0.50 13.10  ? 72  ASP A CB  1 
ATOM   612  C  CB  B ASP A  1 73  ? 34.248 12.094  -5.931  0.50 15.46  ? 72  ASP A CB  1 
ATOM   613  C  CG  A ASP A  1 73  ? 35.148 11.246  -7.546  0.50 15.85  ? 72  ASP A CG  1 
ATOM   614  C  CG  B ASP A  1 73  ? 34.664 11.366  -7.181  0.50 18.98  ? 72  ASP A CG  1 
ATOM   615  O  OD1 A ASP A  1 73  ? 35.622 11.430  -6.365  0.50 10.87  ? 72  ASP A OD1 1 
ATOM   616  O  OD1 B ASP A  1 73  ? 34.449 12.013  -8.218  0.50 18.48  ? 72  ASP A OD1 1 
ATOM   617  O  OD2 A ASP A  1 73  ? 35.576 10.294  -8.284  0.50 15.98  ? 72  ASP A OD2 1 
ATOM   618  O  OD2 B ASP A  1 73  ? 35.065 10.215  -7.039  0.50 20.70  ? 72  ASP A OD2 1 
ATOM   619  N  N   . ASN A  1 74  ? 35.837 15.298  -7.356  1.00 16.74  ? 73  ASN A N   1 
ATOM   620  C  CA  . ASN A  1 74  ? 36.933 16.166  -7.804  1.00 21.54  ? 73  ASN A CA  1 
ATOM   621  C  C   . ASN A  1 74  ? 37.777 16.773  -6.791  1.00 22.48  ? 73  ASN A C   1 
ATOM   622  O  O   . ASN A  1 74  ? 38.922 17.166  -7.012  1.00 31.28  ? 73  ASN A O   1 
ATOM   623  C  CB  . ASN A  1 74  ? 36.380 17.264  -8.721  1.00 24.37  ? 73  ASN A CB  1 
ATOM   624  C  CG  . ASN A  1 74  ? 35.515 16.710  -9.836  1.00 42.41  ? 73  ASN A CG  1 
ATOM   625  O  OD1 . ASN A  1 74  ? 34.422 17.213  -10.098 1.00 37.74  ? 73  ASN A OD1 1 
ATOM   626  N  ND2 . ASN A  1 74  ? 36.001 15.668  -10.501 1.00 31.02  ? 73  ASN A ND2 1 
ATOM   627  N  N   . ASP A  1 75  ? 37.172 16.843  -5.649  1.00 15.38  ? 74  ASP A N   1 
ATOM   628  C  CA  . ASP A  1 75  ? 37.853 17.476  -4.500  1.00 13.81  ? 74  ASP A CA  1 
ATOM   629  C  C   . ASP A  1 75  ? 37.210 17.058  -3.169  1.00 14.23  ? 74  ASP A C   1 
ATOM   630  O  O   . ASP A  1 75  ? 36.289 16.191  -3.186  1.00 15.26  ? 74  ASP A O   1 
ATOM   631  C  CB  . ASP A  1 75  ? 37.792 19.055  -4.676  1.00 15.05  ? 74  ASP A CB  1 
ATOM   632  C  CG  . ASP A  1 75  ? 36.457 19.571  -4.652  1.00 14.39  ? 74  ASP A CG  1 
ATOM   633  O  OD1 . ASP A  1 75  ? 35.543 19.084  -3.902  1.00 15.31  ? 74  ASP A OD1 1 
ATOM   634  O  OD2 . ASP A  1 75  ? 36.194 20.489  -5.435  1.00 20.11  ? 74  ASP A OD2 1 
ATOM   635  N  N   . ASN A  1 76  ? 37.729 17.601  -2.071  1.00 12.58  ? 75  ASN A N   1 
ATOM   636  C  CA  . ASN A  1 76  ? 37.284 17.246  -0.731  1.00 14.27  ? 75  ASN A CA  1 
ATOM   637  C  C   . ASN A  1 76  ? 36.233 18.144  -0.095  1.00 24.78  ? 75  ASN A C   1 
ATOM   638  O  O   . ASN A  1 76  ? 36.218 18.299  1.103   1.00 13.58  ? 75  ASN A O   1 
ATOM   639  C  CB  . ASN A  1 76  ? 38.491 17.128  0.207   1.00 17.23  ? 75  ASN A CB  1 
ATOM   640  C  CG  . ASN A  1 76  ? 39.398 15.968  -0.154  1.00 20.43  ? 75  ASN A CG  1 
ATOM   641  O  OD1 . ASN A  1 76  ? 38.931 14.902  -0.555  1.00 23.70  ? 75  ASN A OD1 1 
ATOM   642  N  ND2 . ASN A  1 76  ? 40.702 16.170  -0.011  1.00 27.95  ? 75  ASN A ND2 1 
ATOM   643  N  N   . ARG A  1 77  ? 35.327 18.687  -0.901  1.00 10.55  ? 76  ARG A N   1 
ATOM   644  C  CA  . ARG A  1 77  ? 34.276 19.565  -0.388  1.00 10.29  ? 76  ARG A CA  1 
ATOM   645  C  C   . ARG A  1 77  ? 33.281 18.850  0.534   1.00 7.89   ? 76  ARG A C   1 
ATOM   646  O  O   . ARG A  1 77  ? 32.658 19.479  1.390   1.00 10.20  ? 76  ARG A O   1 
ATOM   647  C  CB  . ARG A  1 77  ? 33.529 20.234  -1.544  1.00 10.30  ? 76  ARG A CB  1 
ATOM   648  C  CG  . ARG A  1 77  ? 34.241 21.445  -2.125  1.00 11.76  ? 76  ARG A CG  1 
ATOM   649  C  CD  . ARG A  1 77  ? 33.490 22.005  -3.322  1.00 13.13  ? 76  ARG A CD  1 
ATOM   650  N  NE  . ARG A  1 77  ? 33.264 20.991  -4.349  1.00 13.61  ? 76  ARG A NE  1 
ATOM   651  C  CZ  . ARG A  1 77  ? 32.376 21.107  -5.330  1.00 16.91  ? 76  ARG A CZ  1 
ATOM   652  N  NH1 . ARG A  1 77  ? 31.625 22.196  -5.422  1.00 18.74  ? 76  ARG A NH1 1 
ATOM   653  N  NH2 . ARG A  1 77  ? 32.239 20.135  -6.221  1.00 20.93  ? 76  ARG A NH2 1 
ATOM   654  N  N   . SER A  1 78  ? 33.135 17.541  0.354   1.00 8.79   ? 77  SER A N   1 
ATOM   655  C  CA  . SER A  1 78  ? 32.208 16.737  1.157   1.00 8.64   ? 77  SER A CA  1 
ATOM   656  C  C   . SER A  1 78  ? 32.959 15.549  1.712   1.00 8.59   ? 77  SER A C   1 
ATOM   657  O  O   . SER A  1 78  ? 33.381 14.698  0.924   1.00 9.61   ? 77  SER A O   1 
ATOM   658  C  CB  . SER A  1 78  ? 31.084 16.225  0.246   1.00 9.50   ? 77  SER A CB  1 
ATOM   659  O  OG  . SER A  1 78  ? 30.295 17.361  -0.194  1.00 9.14   ? 77  SER A OG  1 
ATOM   660  N  N   . VAL A  1 79  ? 33.057 15.477  3.027   1.00 8.91   ? 78  VAL A N   1 
ATOM   661  C  CA  . VAL A  1 79  ? 33.862 14.453  3.659   1.00 9.91   ? 78  VAL A CA  1 
ATOM   662  C  C   . VAL A  1 79  ? 33.155 13.875  4.897   1.00 9.14   ? 78  VAL A C   1 
ATOM   663  O  O   . VAL A  1 79  ? 32.351 14.545  5.569   1.00 10.71  ? 78  VAL A O   1 
ATOM   664  C  CB  . VAL A  1 79  ? 35.225 14.956  4.039   1.00 13.11  ? 78  VAL A CB  1 
ATOM   665  C  CG1 . VAL A  1 79  ? 36.121 15.183  2.827   1.00 15.68  ? 78  VAL A CG1 1 
ATOM   666  C  CG2 . VAL A  1 79  ? 35.150 16.105  4.969   1.00 15.87  ? 78  VAL A CG2 1 
ATOM   667  N  N   . LEU A  1 80  ? 33.534 12.635  5.148   1.00 9.67   ? 79  LEU A N   1 
ATOM   668  C  CA  . LEU A  1 80  ? 33.269 11.903  6.384   1.00 9.52   ? 79  LEU A CA  1 
ATOM   669  C  C   . LEU A  1 80  ? 34.565 11.840  7.174   1.00 10.50  ? 79  LEU A C   1 
ATOM   670  O  O   . LEU A  1 80  ? 35.627 11.465  6.612   1.00 11.86  ? 79  LEU A O   1 
ATOM   671  C  CB  . LEU A  1 80  ? 32.804 10.499  5.984   1.00 9.64   ? 79  LEU A CB  1 
ATOM   672  C  CG  . LEU A  1 80  ? 32.751 9.446   7.102   1.00 9.81   ? 79  LEU A CG  1 
ATOM   673  C  CD1 . LEU A  1 80  ? 31.758 9.773   8.189   1.00 12.67  ? 79  LEU A CD1 1 
ATOM   674  C  CD2 . LEU A  1 80  ? 32.406 8.095   6.489   1.00 11.56  ? 79  LEU A CD2 1 
ATOM   675  N  N   . LYS A  1 81  ? 34.471 12.074  8.469   1.00 11.23  ? 80  LYS A N   1 
ATOM   676  C  CA  . LYS A  1 81  ? 35.662 12.018  9.339   1.00 14.28  ? 80  LYS A CA  1 
ATOM   677  C  C   . LYS A  1 81  ? 35.218 11.388  10.664  1.00 10.84  ? 80  LYS A C   1 
ATOM   678  O  O   . LYS A  1 81  ? 34.046 11.198  10.954  1.00 11.21  ? 80  LYS A O   1 
ATOM   679  C  CB  . LYS A  1 81  ? 36.251 13.503  9.629   1.00 25.02  ? 80  LYS A CB  1 
ATOM   680  C  CG  . LYS A  1 81  ? 36.056 14.538  8.683   1.00 29.56  ? 80  LYS A CG  1 
ATOM   681  C  CD  . LYS A  1 81  ? 36.653 15.940  9.021   1.00 39.68  ? 80  LYS A CD  1 
ATOM   682  C  CE  . LYS A  1 81  ? 35.896 16.576  10.178  1.00 43.00  ? 80  LYS A CE  1 
ATOM   683  N  N   . GLY A  1 82  ? 36.223 11.170  11.534  1.00 11.29  ? 81  GLY A N   1 
ATOM   684  C  CA  . GLY A  1 82  ? 35.948 10.639  12.842  1.00 11.59  ? 81  GLY A CA  1 
ATOM   685  C  C   . GLY A  1 82  ? 35.689 9.174   12.844  1.00 10.19  ? 81  GLY A C   1 
ATOM   686  O  O   . GLY A  1 82  ? 36.169 8.389   12.014  1.00 11.29  ? 81  GLY A O   1 
ATOM   687  N  N   . GLY A  1 83  ? 34.901 8.717   13.838  1.00 11.87  ? 82  GLY A N   1 
ATOM   688  C  CA  . GLY A  1 83  ? 34.619 7.293   13.972  1.00 11.70  ? 82  GLY A CA  1 
ATOM   689  C  C   . GLY A  1 83  ? 35.910 6.496   14.118  1.00 10.84  ? 82  GLY A C   1 
ATOM   690  O  O   . GLY A  1 83  ? 36.762 6.846   14.941  1.00 12.05  ? 82  GLY A O   1 
ATOM   691  N  N   . PRO A  1 84  ? 36.076 5.443   13.306  1.00 10.24  ? 83  PRO A N   1 
ATOM   692  C  CA  . PRO A  1 84  ? 37.308 4.616   13.351  1.00 11.57  ? 83  PRO A CA  1 
ATOM   693  C  C   . PRO A  1 84  ? 38.387 5.153   12.481  1.00 11.01  ? 83  PRO A C   1 
ATOM   694  O  O   . PRO A  1 84  ? 39.438 4.536   12.375  1.00 13.58  ? 83  PRO A O   1 
ATOM   695  C  CB  . PRO A  1 84  ? 36.851 3.270   12.815  1.00 11.40  ? 83  PRO A CB  1 
ATOM   696  C  CG  . PRO A  1 84  ? 35.803 3.681   11.774  1.00 11.08  ? 83  PRO A CG  1 
ATOM   697  C  CD  . PRO A  1 84  ? 35.080 4.899   12.374  1.00 11.23  ? 83  PRO A CD  1 
ATOM   698  N  N   . PHE A  1 85  ? 38.174 6.325   11.810  1.00 11.21  ? 84  PHE A N   1 
ATOM   699  C  CA  . PHE A  1 85  ? 39.073 6.764   10.743  1.00 12.49  ? 84  PHE A CA  1 
ATOM   700  C  C   . PHE A  1 85  ? 40.154 7.716   11.234  1.00 14.66  ? 84  PHE A C   1 
ATOM   701  O  O   . PHE A  1 85  ? 39.844 8.624   12.068  1.00 19.42  ? 84  PHE A O   1 
ATOM   702  C  CB  . PHE A  1 85  ? 38.291 7.451   9.643   1.00 11.86  ? 84  PHE A CB  1 
ATOM   703  C  CG  . PHE A  1 85  ? 37.181 6.615   9.090   1.00 11.11  ? 84  PHE A CG  1 
ATOM   704  C  CD1 . PHE A  1 85  ? 37.524 5.356   8.469   1.00 14.29  ? 84  PHE A CD1 1 
ATOM   705  C  CD2 . PHE A  1 85  ? 35.863 6.945   9.205   1.00 13.10  ? 84  PHE A CD2 1 
ATOM   706  C  CE1 . PHE A  1 85  ? 36.571 4.542   7.927   1.00 14.51  ? 84  PHE A CE1 1 
ATOM   707  C  CE2 . PHE A  1 85  ? 34.850 6.096   8.703   1.00 14.58  ? 84  PHE A CE2 1 
ATOM   708  C  CZ  . PHE A  1 85  ? 35.241 4.884   8.069   1.00 14.50  ? 84  PHE A CZ  1 
ATOM   709  N  N   A SER A  1 86  ? 41.342 7.621   10.648  0.50 18.90  ? 85  SER A N   1 
ATOM   710  N  N   B SER A  1 86  ? 41.338 7.600   10.617  0.50 19.13  ? 85  SER A N   1 
ATOM   711  C  CA  A SER A  1 86  ? 42.319 8.699   10.855  0.50 26.42  ? 85  SER A CA  1 
ATOM   712  C  CA  B SER A  1 86  ? 42.446 8.566   10.793  0.50 19.69  ? 85  SER A CA  1 
ATOM   713  C  C   A SER A  1 86  ? 42.209 9.718   9.686   0.50 25.33  ? 85  SER A C   1 
ATOM   714  C  C   B SER A  1 86  ? 42.599 9.479   9.558   0.50 22.24  ? 85  SER A C   1 
ATOM   715  O  O   A SER A  1 86  ? 42.447 10.920  9.924   0.50 36.02  ? 85  SER A O   1 
ATOM   716  O  O   B SER A  1 86  ? 43.426 10.372  9.638   0.50 28.97  ? 85  SER A O   1 
ATOM   717  C  CB  A SER A  1 86  ? 43.730 8.130   11.097  0.50 28.38  ? 85  SER A CB  1 
ATOM   718  C  CB  B SER A  1 86  ? 43.753 7.854   10.998  0.50 23.37  ? 85  SER A CB  1 
ATOM   719  O  OG  A SER A  1 86  ? 43.643 7.120   12.139  0.50 27.42  ? 85  SER A OG  1 
ATOM   720  O  OG  B SER A  1 86  ? 44.029 7.087   9.866   0.50 28.20  ? 85  SER A OG  1 
ATOM   721  N  N   . ASP A  1 87  ? 41.893 9.190   8.487   1.00 23.18  ? 86  ASP A N   1 
ATOM   722  C  CA  . ASP A  1 87  ? 41.841 9.958   7.237   1.00 27.14  ? 86  ASP A CA  1 
ATOM   723  C  C   . ASP A  1 87  ? 40.392 10.434  6.986   1.00 16.82  ? 86  ASP A C   1 
ATOM   724  O  O   . ASP A  1 87  ? 39.467 9.757   7.457   1.00 16.46  ? 86  ASP A O   1 
ATOM   725  C  CB  . ASP A  1 87  ? 42.180 9.073   5.970   1.00 38.17  ? 86  ASP A CB  1 
ATOM   726  C  CG  . ASP A  1 87  ? 43.524 8.254   6.047   1.00 44.08  ? 86  ASP A CG  1 
ATOM   727  O  OD1 . ASP A  1 87  ? 44.562 8.847   6.409   1.00 32.79  ? 86  ASP A OD1 1 
ATOM   728  O  OD2 . ASP A  1 87  ? 43.503 7.043   5.743   1.00 36.48  ? 86  ASP A OD2 1 
ATOM   729  N  N   . SER A  1 88  ? 40.185 11.628  6.393   1.00 16.32  ? 87  SER A N   1 
ATOM   730  C  CA  . SER A  1 88  ? 38.869 11.933  5.841   1.00 14.17  ? 87  SER A CA  1 
ATOM   731  C  C   . SER A  1 88  ? 38.584 11.112  4.572   1.00 11.98  ? 87  SER A C   1 
ATOM   732  O  O   . SER A  1 88  ? 39.514 10.800  3.779   1.00 14.97  ? 87  SER A O   1 
ATOM   733  C  CB  . SER A  1 88  ? 38.806 13.447  5.480   1.00 15.65  ? 87  SER A CB  1 
ATOM   734  O  OG  . SER A  1 88  ? 38.859 14.217  6.697   1.00 21.13  ? 87  SER A OG  1 
ATOM   735  N  N   . TYR A  1 89  ? 37.333 10.762  4.413   1.00 10.45  ? 88  TYR A N   1 
ATOM   736  C  CA  . TYR A  1 89  ? 36.875 10.028  3.213   1.00 10.22  ? 88  TYR A CA  1 
ATOM   737  C  C   . TYR A  1 89  ? 35.952 10.964  2.434   1.00 9.65   ? 88  TYR A C   1 
ATOM   738  O  O   . TYR A  1 89  ? 35.074 11.625  3.019   1.00 13.00  ? 88  TYR A O   1 
ATOM   739  C  CB  . TYR A  1 89  ? 36.151 8.730   3.607   1.00 10.62  ? 88  TYR A CB  1 
ATOM   740  C  CG  . TYR A  1 89  ? 37.049 7.613   4.042   1.00 8.91   ? 88  TYR A CG  1 
ATOM   741  C  CD1 . TYR A  1 89  ? 37.799 7.670   5.206   1.00 10.62  ? 88  TYR A CD1 1 
ATOM   742  C  CD2 . TYR A  1 89  ? 37.106 6.438   3.278   1.00 9.31   ? 88  TYR A CD2 1 
ATOM   743  C  CE1 . TYR A  1 89  ? 38.668 6.629   5.578   1.00 10.86  ? 88  TYR A CE1 1 
ATOM   744  C  CE2 . TYR A  1 89  ? 37.949 5.392   3.640   1.00 9.89   ? 88  TYR A CE2 1 
ATOM   745  C  CZ  . TYR A  1 89  ? 38.716 5.455   4.790   1.00 10.12  ? 88  TYR A CZ  1 
ATOM   746  O  OH  . TYR A  1 89  ? 39.515 4.436   5.176   1.00 12.51  ? 88  TYR A OH  1 
ATOM   747  N  N   A ARG A  1 90  ? 36.077 10.936  1.112   0.50 8.88   ? 89  ARG A N   1 
ATOM   748  N  N   B ARG A  1 90  ? 36.092 10.958  1.115   0.50 8.86   ? 89  ARG A N   1 
ATOM   749  C  CA  A ARG A  1 90  ? 35.323 11.814  0.217   0.50 9.29   ? 89  ARG A CA  1 
ATOM   750  C  CA  B ARG A  1 90  ? 35.294 11.833  0.270   0.50 9.60   ? 89  ARG A CA  1 
ATOM   751  C  C   A ARG A  1 90  ? 33.973 11.263  -0.258  0.50 7.86   ? 89  ARG A C   1 
ATOM   752  C  C   B ARG A  1 90  ? 33.969 11.237  -0.192  0.50 7.91   ? 89  ARG A C   1 
ATOM   753  O  O   A ARG A  1 90  ? 33.926 10.228  -0.924  0.50 8.70   ? 89  ARG A O   1 
ATOM   754  O  O   B ARG A  1 90  ? 33.932 10.137  -0.743  0.50 8.21   ? 89  ARG A O   1 
ATOM   755  C  CB  A ARG A  1 90  ? 36.221 12.125  -0.987  0.50 11.34  ? 89  ARG A CB  1 
ATOM   756  C  CB  B ARG A  1 90  ? 36.099 12.260  -0.958  0.50 10.29  ? 89  ARG A CB  1 
ATOM   757  C  CG  A ARG A  1 90  ? 35.632 12.984  -2.092  0.50 12.67  ? 89  ARG A CG  1 
ATOM   758  C  CG  B ARG A  1 90  ? 35.255 13.028  -1.955  0.50 12.13  ? 89  ARG A CG  1 
ATOM   759  C  CD  A ARG A  1 90  ? 36.721 13.209  -3.203  0.50 16.84  ? 89  ARG A CD  1 
ATOM   760  C  CD  B ARG A  1 90  ? 35.801 12.964  -3.447  0.50 10.94  ? 89  ARG A CD  1 
ATOM   761  N  NE  A ARG A  1 90  ? 37.945 13.791  -2.661  0.50 16.37  ? 89  ARG A NE  1 
ATOM   762  N  NE  B ARG A  1 90  ? 37.179 13.436  -3.547  0.50 13.73  ? 89  ARG A NE  1 
ATOM   763  C  CZ  A ARG A  1 90  ? 39.010 14.105  -3.392  0.50 12.62  ? 89  ARG A CZ  1 
ATOM   764  C  CZ  B ARG A  1 90  ? 37.869 13.493  -4.681  0.50 11.49  ? 89  ARG A CZ  1 
ATOM   765  N  NH1 A ARG A  1 90  ? 39.004 13.892  -4.701  0.50 15.01  ? 89  ARG A NH1 1 
ATOM   766  N  NH1 B ARG A  1 90  ? 37.309 13.106  -5.819  0.50 13.29  ? 89  ARG A NH1 1 
ATOM   767  N  NH2 A ARG A  1 90  ? 40.081 14.631  -2.815  0.50 14.64  ? 89  ARG A NH2 1 
ATOM   768  N  NH2 B ARG A  1 90  ? 39.118 13.937  -4.679  0.50 12.70  ? 89  ARG A NH2 1 
ATOM   769  N  N   . LEU A  1 91  ? 32.876 11.942  0.089   1.00 8.15   ? 90  LEU A N   1 
ATOM   770  C  CA  . LEU A  1 91  ? 31.560 11.498  -0.361  1.00 8.09   ? 90  LEU A CA  1 
ATOM   771  C  C   . LEU A  1 91  ? 31.551 11.260  -1.890  1.00 7.93   ? 90  LEU A C   1 
ATOM   772  O  O   . LEU A  1 91  ? 31.979 12.146  -2.626  1.00 9.93   ? 90  LEU A O   1 
ATOM   773  C  CB  . LEU A  1 91  ? 30.551 12.580  0.021   1.00 8.97   ? 90  LEU A CB  1 
ATOM   774  C  CG  . LEU A  1 91  ? 29.093 12.328  -0.483  1.00 8.56   ? 90  LEU A CG  1 
ATOM   775  C  CD1 . LEU A  1 91  ? 28.474 11.055  0.140   1.00 9.56   ? 90  LEU A CD1 1 
ATOM   776  C  CD2 . LEU A  1 91  ? 28.270 13.569  -0.229  1.00 9.40   ? 90  LEU A CD2 1 
ATOM   777  N  N   A PHE A  1 92  ? 31.003 10.109  -2.293  0.50 8.24   ? 91  PHE A N   1 
ATOM   778  N  N   B PHE A  1 92  ? 31.002 10.159  -2.339  0.50 7.70   ? 91  PHE A N   1 
ATOM   779  C  CA  A PHE A  1 92  ? 30.955 9.691   -3.702  0.50 9.16   ? 91  PHE A CA  1 
ATOM   780  C  CA  B PHE A  1 92  ? 30.837 10.155  -3.773  0.50 8.80   ? 91  PHE A CA  1 
ATOM   781  C  C   A PHE A  1 92  ? 29.507 9.535   -4.193  0.50 7.11   ? 91  PHE A C   1 
ATOM   782  C  C   B PHE A  1 92  ? 29.439 9.690   -4.219  0.50 7.67   ? 91  PHE A C   1 
ATOM   783  O  O   A PHE A  1 92  ? 29.163 10.009  -5.274  0.50 8.88   ? 91  PHE A O   1 
ATOM   784  O  O   B PHE A  1 92  ? 29.098 9.965   -5.349  0.50 8.74   ? 91  PHE A O   1 
ATOM   785  C  CB  A PHE A  1 92  ? 31.711 8.360   -3.911  0.50 9.82   ? 91  PHE A CB  1 
ATOM   786  C  CB  B PHE A  1 92  ? 31.948 9.436   -4.494  0.50 9.71   ? 91  PHE A CB  1 
ATOM   787  C  CG  A PHE A  1 92  ? 31.784 7.949   -5.357  0.50 11.55  ? 91  PHE A CG  1 
ATOM   788  C  CG  B PHE A  1 92  ? 31.977 7.919   -4.254  0.50 10.51  ? 91  PHE A CG  1 
ATOM   789  C  CD1 A PHE A  1 92  ? 32.655 8.628   -6.198  0.50 11.26  ? 91  PHE A CD1 1 
ATOM   790  C  CD1 B PHE A  1 92  ? 32.531 7.399   -3.058  0.50 10.40  ? 91  PHE A CD1 1 
ATOM   791  C  CD2 A PHE A  1 92  ? 31.020 6.945   -5.866  0.50 13.70  ? 91  PHE A CD2 1 
ATOM   792  C  CD2 B PHE A  1 92  ? 31.408 6.985   -5.193  0.50 10.91  ? 91  PHE A CD2 1 
ATOM   793  C  CE1 A PHE A  1 92  ? 32.726 8.367   -7.578  0.50 13.75  ? 91  PHE A CE1 1 
ATOM   794  C  CE1 B PHE A  1 92  ? 32.605 6.031   -2.778  0.50 10.02  ? 91  PHE A CE1 1 
ATOM   795  C  CE2 A PHE A  1 92  ? 31.024 6.664   -7.252  0.50 18.07  ? 91  PHE A CE2 1 
ATOM   796  C  CE2 B PHE A  1 92  ? 31.462 5.618   -4.852  0.50 10.57  ? 91  PHE A CE2 1 
ATOM   797  C  CZ  A PHE A  1 92  ? 31.901 7.408   -8.121  0.50 17.08  ? 91  PHE A CZ  1 
ATOM   798  C  CZ  B PHE A  1 92  ? 32.025 5.133   -3.666  0.50 11.41  ? 91  PHE A CZ  1 
ATOM   799  N  N   A GLN A  1 93  ? 28.689 8.785   -3.441  0.50 8.26   ? 92  GLN A N   1 
ATOM   800  N  N   B GLN A  1 93  ? 28.655 8.943   -3.412  0.50 8.41   ? 92  GLN A N   1 
ATOM   801  C  CA  A GLN A  1 93  ? 27.337 8.504   -3.875  0.50 7.85   ? 92  GLN A CA  1 
ATOM   802  C  CA  B GLN A  1 93  ? 27.341 8.556   -3.912  0.50 8.73   ? 92  GLN A CA  1 
ATOM   803  C  C   A GLN A  1 93  ? 26.478 8.144   -2.669  0.50 8.67   ? 92  GLN A C   1 
ATOM   804  C  C   B GLN A  1 93  ? 26.501 8.016   -2.769  0.50 8.12   ? 92  GLN A C   1 
ATOM   805  O  O   A GLN A  1 93  ? 27.007 7.788   -1.616  0.50 9.64   ? 92  GLN A O   1 
ATOM   806  O  O   B GLN A  1 93  ? 27.065 7.575   -1.773  0.50 8.42   ? 92  GLN A O   1 
ATOM   807  C  CB  A GLN A  1 93  ? 27.261 7.436   -5.020  0.50 10.15  ? 92  GLN A CB  1 
ATOM   808  C  CB  B GLN A  1 93  ? 27.498 7.632   -5.139  0.50 15.19  ? 92  GLN A CB  1 
ATOM   809  C  CG  A GLN A  1 93  ? 27.774 6.045   -4.718  0.50 14.27  ? 92  GLN A CG  1 
ATOM   810  C  CG  B GLN A  1 93  ? 28.024 6.260   -4.886  0.50 18.76  ? 92  GLN A CG  1 
ATOM   811  C  CD  A GLN A  1 93  ? 27.001 5.071   -5.593  0.50 11.70  ? 92  GLN A CD  1 
ATOM   812  C  CD  B GLN A  1 93  ? 26.925 5.156   -4.709  0.50 12.07  ? 92  GLN A CD  1 
ATOM   813  O  OE1 A GLN A  1 93  ? 26.380 4.083   -5.190  0.50 13.05  ? 92  GLN A OE1 1 
ATOM   814  O  OE1 B GLN A  1 93  ? 26.090 5.162   -3.914  0.50 9.33   ? 92  GLN A OE1 1 
ATOM   815  N  NE2 A GLN A  1 93  ? 27.399 5.211   -6.761  0.50 17.69  ? 92  GLN A NE2 1 
ATOM   816  N  NE2 B GLN A  1 93  ? 27.088 4.168   -5.497  0.50 19.68  ? 92  GLN A NE2 1 
ATOM   817  N  N   . PHE A  1 94  ? 25.163 8.114   -2.893  1.00 7.54   ? 93  PHE A N   1 
ATOM   818  C  CA  . PHE A  1 94  ? 24.316 7.317   -1.986  1.00 7.42   ? 93  PHE A CA  1 
ATOM   819  C  C   . PHE A  1 94  ? 23.319 6.558   -2.827  1.00 7.07   ? 93  PHE A C   1 
ATOM   820  O  O   . PHE A  1 94  ? 23.028 6.891   -3.987  1.00 7.80   ? 93  PHE A O   1 
ATOM   821  C  CB  . PHE A  1 94  ? 23.640 8.149   -0.886  1.00 7.81   ? 93  PHE A CB  1 
ATOM   822  C  CG  . PHE A  1 94  ? 22.545 9.048   -1.325  1.00 7.40   ? 93  PHE A CG  1 
ATOM   823  C  CD1 . PHE A  1 94  ? 21.213 8.604   -1.481  1.00 8.86   ? 93  PHE A CD1 1 
ATOM   824  C  CD2 . PHE A  1 94  ? 22.804 10.382  -1.624  1.00 8.37   ? 93  PHE A CD2 1 
ATOM   825  C  CE1 . PHE A  1 94  ? 20.213 9.486   -1.859  1.00 8.89   ? 93  PHE A CE1 1 
ATOM   826  C  CE2 . PHE A  1 94  ? 21.799 11.259  -2.014  1.00 8.66   ? 93  PHE A CE2 1 
ATOM   827  C  CZ  . PHE A  1 94  ? 20.507 10.813  -2.135  1.00 8.56   ? 93  PHE A CZ  1 
ATOM   828  N  N   . HIS A  1 95  ? 22.782 5.496   -2.213  1.00 7.40   ? 94  HIS A N   1 
ATOM   829  C  CA  . HIS A  1 95  ? 21.763 4.655   -2.831  1.00 6.76   ? 94  HIS A CA  1 
ATOM   830  C  C   . HIS A  1 95  ? 21.056 3.891   -1.776  1.00 6.86   ? 94  HIS A C   1 
ATOM   831  O  O   . HIS A  1 95  ? 21.382 3.991   -0.574  1.00 7.39   ? 94  HIS A O   1 
ATOM   832  C  CB  . HIS A  1 95  ? 22.470 3.725   -3.892  1.00 7.54   ? 94  HIS A CB  1 
ATOM   833  C  CG  . HIS A  1 95  ? 23.405 2.785   -3.253  1.00 6.70   ? 94  HIS A CG  1 
ATOM   834  N  ND1 . HIS A  1 95  ? 24.748 2.987   -3.144  1.00 8.25   ? 94  HIS A ND1 1 
ATOM   835  C  CD2 . HIS A  1 95  ? 23.192 1.572   -2.618  1.00 7.54   ? 94  HIS A CD2 1 
ATOM   836  C  CE1 . HIS A  1 95  ? 25.303 1.953   -2.504  1.00 8.00   ? 94  HIS A CE1 1 
ATOM   837  N  NE2 . HIS A  1 95  ? 24.406 1.081   -2.146  1.00 7.31   ? 94  HIS A NE2 1 
ATOM   838  N  N   . PHE A  1 96  ? 20.082 3.079   -2.165  1.00 6.65   ? 95  PHE A N   1 
ATOM   839  C  CA  . PHE A  1 96  ? 19.271 2.264   -1.293  1.00 6.99   ? 95  PHE A CA  1 
ATOM   840  C  C   . PHE A  1 96  ? 19.292 0.828   -1.713  1.00 6.57   ? 95  PHE A C   1 
ATOM   841  O  O   . PHE A  1 96  ? 19.553 0.482   -2.875  1.00 7.81   ? 95  PHE A O   1 
ATOM   842  C  CB  . PHE A  1 96  ? 17.818 2.754   -1.291  1.00 7.94   ? 95  PHE A CB  1 
ATOM   843  C  CG  . PHE A  1 96  ? 17.665 4.200   -0.912  1.00 7.53   ? 95  PHE A CG  1 
ATOM   844  C  CD1 . PHE A  1 96  ? 17.793 5.214   -1.918  1.00 8.38   ? 95  PHE A CD1 1 
ATOM   845  C  CD2 . PHE A  1 96  ? 17.419 4.575   0.398   1.00 8.01   ? 95  PHE A CD2 1 
ATOM   846  C  CE1 . PHE A  1 96  ? 17.678 6.528   -1.550  1.00 8.60   ? 95  PHE A CE1 1 
ATOM   847  C  CE2 . PHE A  1 96  ? 17.285 5.934   0.737   1.00 8.85   ? 95  PHE A CE2 1 
ATOM   848  C  CZ  . PHE A  1 96  ? 17.408 6.901   -0.249  1.00 8.81   ? 95  PHE A CZ  1 
ATOM   849  N  N   . HIS A  1 97  ? 18.929 -0.043  -0.777  1.00 6.83   ? 96  HIS A N   1 
ATOM   850  C  CA  . HIS A  1 97  ? 18.504 -1.425  -1.079  1.00 7.28   ? 96  HIS A CA  1 
ATOM   851  C  C   . HIS A  1 97  ? 17.132 -1.615  -0.512  1.00 6.54   ? 96  HIS A C   1 
ATOM   852  O  O   . HIS A  1 97  ? 16.782 -1.015  0.518   1.00 7.91   ? 96  HIS A O   1 
ATOM   853  C  CB  . HIS A  1 97  ? 19.471 -2.451  -0.505  1.00 7.54   ? 96  HIS A CB  1 
ATOM   854  C  CG  . HIS A  1 97  ? 20.866 -2.279  -0.976  1.00 6.99   ? 96  HIS A CG  1 
ATOM   855  N  ND1 . HIS A  1 97  ? 21.455 -3.115  -1.912  1.00 8.00   ? 96  HIS A ND1 1 
ATOM   856  C  CD2 . HIS A  1 97  ? 21.828 -1.387  -0.656  1.00 7.18   ? 96  HIS A CD2 1 
ATOM   857  C  CE1 . HIS A  1 97  ? 22.727 -2.706  -2.137  1.00 8.22   ? 96  HIS A CE1 1 
ATOM   858  N  NE2 . HIS A  1 97  ? 22.975 -1.654  -1.362  1.00 7.75   ? 96  HIS A NE2 1 
ATOM   859  N  N   . TRP A  1 98  ? 16.357 -2.484  -1.157  1.00 7.59   ? 97  TRP A N   1 
ATOM   860  C  CA  . TRP A  1 98  ? 15.014 -2.846  -0.740  1.00 7.54   ? 97  TRP A CA  1 
ATOM   861  C  C   . TRP A  1 98  ? 14.749 -4.255  -1.126  1.00 7.74   ? 97  TRP A C   1 
ATOM   862  O  O   . TRP A  1 98  ? 15.540 -4.913  -1.845  1.00 8.80   ? 97  TRP A O   1 
ATOM   863  C  CB  . TRP A  1 98  ? 13.959 -1.874  -1.313  1.00 8.92   ? 97  TRP A CB  1 
ATOM   864  C  CG  . TRP A  1 98  ? 13.992 -1.862  -2.860  1.00 7.95   ? 97  TRP A CG  1 
ATOM   865  C  CD1 . TRP A  1 98  ? 13.332 -2.712  -3.687  1.00 8.45   ? 97  TRP A CD1 1 
ATOM   866  C  CD2 . TRP A  1 98  ? 14.771 -0.991  -3.681  1.00 7.93   ? 97  TRP A CD2 1 
ATOM   867  N  NE1 . TRP A  1 98  ? 13.605 -2.372  -4.992  1.00 8.77   ? 97  TRP A NE1 1 
ATOM   868  C  CE2 . TRP A  1 98  ? 14.479 -1.307  -5.036  1.00 7.71   ? 97  TRP A CE2 1 
ATOM   869  C  CE3 . TRP A  1 98  ? 15.666 0.059   -3.432  1.00 8.19   ? 97  TRP A CE3 1 
ATOM   870  C  CZ2 . TRP A  1 98  ? 15.002 -0.611  -6.127  1.00 8.52   ? 97  TRP A CZ2 1 
ATOM   871  C  CZ3 . TRP A  1 98  ? 16.165 0.776   -4.519  1.00 8.38   ? 97  TRP A CZ3 1 
ATOM   872  C  CH2 . TRP A  1 98  ? 15.823 0.426   -5.858  1.00 9.11   ? 97  TRP A CH2 1 
ATOM   873  N  N   . GLY A  1 99  ? 13.619 -4.790  -0.603  1.00 8.76   ? 98  GLY A N   1 
ATOM   874  C  CA  . GLY A  1 99  ? 13.282 -6.173  -0.802  1.00 11.13  ? 98  GLY A CA  1 
ATOM   875  C  C   . GLY A  1 99  ? 12.012 -6.317  -1.506  1.00 12.17  ? 98  GLY A C   1 
ATOM   876  O  O   . GLY A  1 99  ? 11.303 -5.373  -1.783  1.00 12.17  ? 98  GLY A O   1 
ATOM   877  N  N   A SER A  1 100 ? 11.686 -7.615  -1.797  0.50 14.27  ? 99  SER A N   1 
ATOM   878  N  N   B SER A  1 100 ? 11.614 -7.618  -1.689  0.50 13.82  ? 99  SER A N   1 
ATOM   879  C  CA  A SER A  1 100 ? 10.454 -7.857  -2.490  0.50 19.89  ? 99  SER A CA  1 
ATOM   880  C  CA  B SER A  1 100 ? 10.339 -7.879  -2.406  0.50 16.92  ? 99  SER A CA  1 
ATOM   881  C  C   A SER A  1 100 ? 9.299  -7.710  -1.535  0.50 12.81  ? 99  SER A C   1 
ATOM   882  C  C   B SER A  1 100 ? 9.042  -7.270  -1.758  0.50 20.99  ? 99  SER A C   1 
ATOM   883  O  O   A SER A  1 100 ? 8.172  -7.546  -2.096  0.50 15.44  ? 99  SER A O   1 
ATOM   884  O  O   B SER A  1 100 ? 7.971  -6.974  -2.408  0.50 23.72  ? 99  SER A O   1 
ATOM   885  C  CB  A SER A  1 100 ? 10.335 -9.265  -3.060  0.50 28.52  ? 99  SER A CB  1 
ATOM   886  C  CB  B SER A  1 100 ? 10.197 -9.424  -2.700  0.50 20.07  ? 99  SER A CB  1 
ATOM   887  O  OG  A SER A  1 100 ? 10.492 -10.130 -1.952  0.50 23.55  ? 99  SER A OG  1 
ATOM   888  O  OG  B SER A  1 100 ? 11.234 -9.720  -3.649  0.50 21.35  ? 99  SER A OG  1 
ATOM   889  N  N   A THR A  1 101 ? 9.461  -7.802  -0.233  0.50 11.77  ? 100 THR A N   1 
ATOM   890  N  N   B THR A  1 101 ? 9.076  -7.298  -0.478  0.50 19.13  ? 100 THR A N   1 
ATOM   891  C  CA  A THR A  1 101 ? 8.381  -7.506  0.750   0.50 14.15  ? 100 THR A CA  1 
ATOM   892  C  CA  B THR A  1 101 ? 7.903  -6.898  0.320   0.50 18.52  ? 100 THR A CA  1 
ATOM   893  C  C   A THR A  1 101 ? 8.791  -6.360  1.686   0.50 15.08  ? 100 THR A C   1 
ATOM   894  C  C   B THR A  1 101 ? 8.632  -6.248  1.539   0.50 17.25  ? 100 THR A C   1 
ATOM   895  O  O   A THR A  1 101 ? 10.030 -6.161  1.808   0.50 14.46  ? 100 THR A O   1 
ATOM   896  O  O   B THR A  1 101 ? 9.874  -6.384  1.793   0.50 18.34  ? 100 THR A O   1 
ATOM   897  C  CB  A THR A  1 101 ? 7.990  -8.742  1.511   0.50 12.49  ? 100 THR A CB  1 
ATOM   898  C  CB  B THR A  1 101 ? 7.014  -8.032  0.777   0.50 16.19  ? 100 THR A CB  1 
ATOM   899  O  OG1 A THR A  1 101 ? 9.047  -9.129  2.434   0.50 14.40  ? 100 THR A OG1 1 
ATOM   900  O  OG1 B THR A  1 101 ? 7.797  -8.647  1.804   0.50 18.31  ? 100 THR A OG1 1 
ATOM   901  C  CG2 A THR A  1 101 ? 7.569  -9.867  0.468   0.50 15.43  ? 100 THR A CG2 1 
ATOM   902  C  CG2 B THR A  1 101 ? 6.568  -8.925  -0.353  0.50 16.35  ? 100 THR A CG2 1 
ATOM   903  N  N   . ASN A  1 102 ? 7.821  -5.681  2.353   1.00 14.03  ? 101 ASN A N   1 
ATOM   904  C  CA  . ASN A  1 102 ? 8.232  -4.812  3.445   1.00 11.88  ? 101 ASN A CA  1 
ATOM   905  C  C   . ASN A  1 102 ? 8.924  -5.611  4.523   1.00 12.31  ? 101 ASN A C   1 
ATOM   906  O  O   . ASN A  1 102 ? 9.667  -5.005  5.324   1.00 13.60  ? 101 ASN A O   1 
ATOM   907  C  CB  . ASN A  1 102 ? 7.007  -4.150  4.058   1.00 13.14  ? 101 ASN A CB  1 
ATOM   908  C  CG  . ASN A  1 102 ? 6.429  -3.120  3.151   1.00 15.44  ? 101 ASN A CG  1 
ATOM   909  O  OD1 . ASN A  1 102 ? 6.999  -2.748  2.129   1.00 18.19  ? 101 ASN A OD1 1 
ATOM   910  N  ND2 . ASN A  1 102 ? 5.247  -2.634  3.591   1.00 17.68  ? 101 ASN A ND2 1 
ATOM   911  N  N   . GLU A  1 103 ? 8.696  -6.887  4.631   1.00 13.22  ? 102 GLU A N   1 
ATOM   912  C  CA  . GLU A  1 103 ? 9.246  -7.695  5.711   1.00 15.06  ? 102 GLU A CA  1 
ATOM   913  C  C   . GLU A  1 103 ? 10.757 -7.803  5.739   1.00 13.39  ? 102 GLU A C   1 
ATOM   914  O  O   . GLU A  1 103 ? 11.344 -7.993  6.805   1.00 16.33  ? 102 GLU A O   1 
ATOM   915  C  CB  . GLU A  1 103 ? 8.587  -9.079  5.740   1.00 19.77  ? 102 GLU A CB  1 
ATOM   916  C  CG  . GLU A  1 103 ? 7.174  -9.061  6.307   1.00 27.31  ? 102 GLU A CG  1 
ATOM   917  C  CD  . GLU A  1 103 ? 6.284  -8.041  5.619   1.00 48.27  ? 102 GLU A CD  1 
ATOM   918  O  OE1 . GLU A  1 103 ? 6.395  -7.947  4.359   1.00 87.42  ? 102 GLU A OE1 1 
ATOM   919  O  OE2 . GLU A  1 103 ? 5.495  -7.351  6.344   1.00 57.61  ? 102 GLU A OE2 1 
ATOM   920  N  N   . HIS A  1 104 ? 11.406 -7.684  4.574   1.00 12.03  ? 103 HIS A N   1 
ATOM   921  C  CA  . HIS A  1 104 ? 12.857 -7.758  4.534   1.00 11.89  ? 103 HIS A CA  1 
ATOM   922  C  C   . HIS A  1 104 ? 13.360 -7.067  3.329   1.00 11.17  ? 103 HIS A C   1 
ATOM   923  O  O   . HIS A  1 104 ? 13.501 -7.708  2.200   1.00 13.14  ? 103 HIS A O   1 
ATOM   924  C  CB  . HIS A  1 104 ? 13.318 -9.251  4.540   1.00 14.14  ? 103 HIS A CB  1 
ATOM   925  C  CG  . HIS A  1 104 ? 14.864 -9.388  4.575   1.00 14.56  ? 103 HIS A CG  1 
ATOM   926  N  ND1 . HIS A  1 104 ? 15.444 -10.621 4.360   1.00 19.94  ? 103 HIS A ND1 1 
ATOM   927  C  CD2 . HIS A  1 104 ? 15.914 -8.434  4.685   1.00 13.38  ? 103 HIS A CD2 1 
ATOM   928  C  CE1 . HIS A  1 104 ? 16.776 -10.496 4.406   1.00 20.27  ? 103 HIS A CE1 1 
ATOM   929  N  NE2 . HIS A  1 104 ? 17.045 -9.204  4.598   1.00 14.91  ? 103 HIS A NE2 1 
ATOM   930  N  N   . GLY A  1 105 ? 13.894 -5.916  3.471   1.00 13.04  ? 104 GLY A N   1 
ATOM   931  C  CA  . GLY A  1 105 ? 14.558 -5.205  2.378   1.00 11.18  ? 104 GLY A CA  1 
ATOM   932  C  C   . GLY A  1 105 ? 15.940 -4.672  2.758   1.00 9.10   ? 104 GLY A C   1 
ATOM   933  O  O   . GLY A  1 105 ? 16.689 -4.252  1.902   1.00 10.07  ? 104 GLY A O   1 
ATOM   934  N  N   . SER A  1 106 ? 16.251 -4.626  4.082   1.00 8.60   ? 105 SER A N   1 
ATOM   935  C  CA  . SER A  1 106 ? 17.598 -4.217  4.452   1.00 8.10   ? 105 SER A CA  1 
ATOM   936  C  C   . SER A  1 106 ? 18.611 -5.277  4.088   1.00 8.15   ? 105 SER A C   1 
ATOM   937  O  O   . SER A  1 106 ? 18.279 -6.426  3.742   1.00 9.83   ? 105 SER A O   1 
ATOM   938  C  CB  . SER A  1 106 ? 17.634 -3.847  5.937   1.00 8.32   ? 105 SER A CB  1 
ATOM   939  O  OG  . SER A  1 106 ? 17.394 -4.986  6.768   1.00 8.86   ? 105 SER A OG  1 
ATOM   940  N  N   . GLU A  1 107 ? 19.867 -4.863  4.153   1.00 8.35   ? 106 GLU A N   1 
ATOM   941  C  CA  . GLU A  1 107 ? 20.997 -5.777  3.955   1.00 8.26   ? 106 GLU A CA  1 
ATOM   942  C  C   . GLU A  1 107 ? 21.484 -6.198  5.355   1.00 7.65   ? 106 GLU A C   1 
ATOM   943  O  O   . GLU A  1 107 ? 21.476 -7.369  5.695   1.00 8.74   ? 106 GLU A O   1 
ATOM   944  C  CB  . GLU A  1 107 ? 22.063 -5.097  3.099   1.00 8.28   ? 106 GLU A CB  1 
ATOM   945  C  CG  . GLU A  1 107 ? 21.512 -4.865  1.680   1.00 10.93  ? 106 GLU A CG  1 
ATOM   946  C  CD  . GLU A  1 107 ? 22.598 -4.874  0.645   1.00 7.76   ? 106 GLU A CD  1 
ATOM   947  O  OE1 . GLU A  1 107 ? 22.507 -5.740  -0.268  1.00 9.41   ? 106 GLU A OE1 1 
ATOM   948  O  OE2 . GLU A  1 107 ? 23.522 -4.063  0.736   1.00 8.48   ? 106 GLU A OE2 1 
ATOM   949  N  N   . HIS A  1 108 ? 21.966 -5.232  6.145   1.00 7.69   ? 107 HIS A N   1 
ATOM   950  C  CA  . HIS A  1 108 ? 22.281 -5.548  7.536   1.00 7.80   ? 107 HIS A CA  1 
ATOM   951  C  C   . HIS A  1 108 ? 21.001 -5.921  8.283   1.00 7.61   ? 107 HIS A C   1 
ATOM   952  O  O   . HIS A  1 108 ? 19.902 -5.458  7.980   1.00 8.65   ? 107 HIS A O   1 
ATOM   953  C  CB  . HIS A  1 108 ? 23.027 -4.387  8.174   1.00 7.93   ? 107 HIS A CB  1 
ATOM   954  C  CG  . HIS A  1 108 ? 24.358 -4.197  7.550   1.00 7.42   ? 107 HIS A CG  1 
ATOM   955  N  ND1 . HIS A  1 108 ? 24.569 -3.425  6.405   1.00 7.74   ? 107 HIS A ND1 1 
ATOM   956  C  CD2 . HIS A  1 108 ? 25.566 -4.736  7.855   1.00 7.83   ? 107 HIS A CD2 1 
ATOM   957  C  CE1 . HIS A  1 108 ? 25.864 -3.543  6.065   1.00 7.49   ? 107 HIS A CE1 1 
ATOM   958  N  NE2 . HIS A  1 108 ? 26.503 -4.349  6.931   1.00 7.81   ? 107 HIS A NE2 1 
ATOM   959  N  N   . THR A  1 109 ? 21.208 -6.704  9.353   1.00 8.30   ? 108 THR A N   1 
ATOM   960  C  CA  . THR A  1 109 ? 20.159 -6.999  10.330  1.00 8.84   ? 108 THR A CA  1 
ATOM   961  C  C   . THR A  1 109 ? 20.746 -6.782  11.692  1.00 8.31   ? 108 THR A C   1 
ATOM   962  O  O   . THR A  1 109 ? 21.955 -6.753  11.865  1.00 8.86   ? 108 THR A O   1 
ATOM   963  C  CB  . THR A  1 109 ? 19.619 -8.430  10.155  1.00 9.35   ? 108 THR A CB  1 
ATOM   964  O  OG1 . THR A  1 109 ? 20.662 -9.375  10.355  1.00 10.22  ? 108 THR A OG1 1 
ATOM   965  C  CG2 . THR A  1 109 ? 19.062 -8.677  8.760   1.00 11.20  ? 108 THR A CG2 1 
ATOM   966  N  N   . VAL A  1 110 ? 19.881 -6.589  12.684  1.00 9.51   ? 109 VAL A N   1 
ATOM   967  C  CA  . VAL A  1 110 ? 20.339 -6.270  14.086  1.00 9.71   ? 109 VAL A CA  1 
ATOM   968  C  C   . VAL A  1 110 ? 19.574 -7.243  14.942  1.00 10.63  ? 109 VAL A C   1 
ATOM   969  O  O   . VAL A  1 110 ? 18.340 -7.252  15.000  1.00 11.45  ? 109 VAL A O   1 
ATOM   970  C  CB  . VAL A  1 110 ? 20.116 -4.853  14.484  1.00 11.31  ? 109 VAL A CB  1 
ATOM   971  C  CG1 . VAL A  1 110 ? 20.584 -4.659  15.946  1.00 13.51  ? 109 VAL A CG1 1 
ATOM   972  C  CG2 . VAL A  1 110 ? 20.884 -3.882  13.554  1.00 12.80  ? 109 VAL A CG2 1 
ATOM   973  N  N   . ASP A  1 111 ? 20.305 -8.154  15.596  1.00 11.45  ? 110 ASP A N   1 
ATOM   974  C  CA  . ASP A  1 111 ? 19.673 -9.197  16.456  1.00 12.36  ? 110 ASP A CA  1 
ATOM   975  C  C   . ASP A  1 111 ? 18.695 -9.973  15.594  1.00 12.33  ? 110 ASP A C   1 
ATOM   976  O  O   . ASP A  1 111 ? 17.624 -10.384 16.133  1.00 14.07  ? 110 ASP A O   1 
ATOM   977  C  CB  . ASP A  1 111 ? 19.067 -8.596  17.746  1.00 14.06  ? 110 ASP A CB  1 
ATOM   978  C  CG  . ASP A  1 111 ? 20.190 -8.133  18.669  1.00 14.66  ? 110 ASP A CG  1 
ATOM   979  O  OD1 . ASP A  1 111 ? 21.279 -8.751  18.696  1.00 17.57  ? 110 ASP A OD1 1 
ATOM   980  O  OD2 . ASP A  1 111 ? 20.017 -7.112  19.325  1.00 16.96  ? 110 ASP A OD2 1 
ATOM   981  N  N   . GLY A  1 112 ? 18.992 -10.206 14.361  1.00 11.38  ? 111 GLY A N   1 
ATOM   982  C  CA  . GLY A  1 112 ? 18.127 -10.980 13.438  1.00 12.64  ? 111 GLY A CA  1 
ATOM   983  C  C   . GLY A  1 112 ? 16.954 -10.224 12.922  1.00 12.22  ? 111 GLY A C   1 
ATOM   984  O  O   . GLY A  1 112 ? 16.236 -10.810 12.087  1.00 13.92  ? 111 GLY A O   1 
ATOM   985  N  N   . VAL A  1 113 ? 16.763 -8.981  13.312  1.00 11.84  ? 112 VAL A N   1 
ATOM   986  C  CA  . VAL A  1 113 ? 15.596 -8.213  12.841  1.00 11.81  ? 112 VAL A CA  1 
ATOM   987  C  C   . VAL A  1 113 ? 15.924 -7.588  11.466  1.00 10.38  ? 112 VAL A C   1 
ATOM   988  O  O   . VAL A  1 113 ? 16.989 -6.960  11.276  1.00 10.45  ? 112 VAL A O   1 
ATOM   989  C  CB  . VAL A  1 113 ? 15.240 -7.115  13.853  1.00 13.14  ? 112 VAL A CB  1 
ATOM   990  C  CG1 . VAL A  1 113 ? 14.129 -6.230  13.331  1.00 14.19  ? 112 VAL A CG1 1 
ATOM   991  C  CG2 . VAL A  1 113 ? 14.876 -7.736  15.244  1.00 15.59  ? 112 VAL A CG2 1 
ATOM   992  N  N   . LYS A  1 114 ? 15.039 -7.858  10.533  1.00 11.14  ? 113 LYS A N   1 
ATOM   993  C  CA  . LYS A  1 114 ? 15.117 -7.350  9.181   1.00 10.89  ? 113 LYS A CA  1 
ATOM   994  C  C   . LYS A  1 114 ? 14.302 -6.104  9.020   1.00 10.33  ? 113 LYS A C   1 
ATOM   995  O  O   . LYS A  1 114 ? 13.129 -6.074  9.419   1.00 13.69  ? 113 LYS A O   1 
ATOM   996  C  CB  . LYS A  1 114 ? 14.607 -8.431  8.196   1.00 12.66  ? 113 LYS A CB  1 
ATOM   997  C  CG  . LYS A  1 114 ? 15.441 -9.714  8.302   1.00 14.98  ? 113 LYS A CG  1 
ATOM   998  C  CD  . LYS A  1 114 ? 14.693 -10.926 7.825   1.00 21.31  ? 113 LYS A CD  1 
ATOM   999  C  CE  . LYS A  1 114 ? 15.503 -12.066 8.215   1.00 36.66  ? 113 LYS A CE  1 
ATOM   1000 N  NZ  . LYS A  1 114 ? 14.582 -13.275 7.880   1.00 34.64  ? 113 LYS A NZ  1 
ATOM   1001 N  N   A TYR A  1 115 ? 14.891 -5.031  8.511   0.50 8.05   ? 114 TYR A N   1 
ATOM   1002 N  N   B TYR A  1 115 ? 14.898 -5.121  8.384   0.50 9.35   ? 114 TYR A N   1 
ATOM   1003 C  CA  A TYR A  1 115 ? 14.185 -3.786  8.214   0.50 8.92   ? 114 TYR A CA  1 
ATOM   1004 C  CA  B TYR A  1 115 ? 14.192 -3.879  8.183   0.50 9.44   ? 114 TYR A CA  1 
ATOM   1005 C  C   A TYR A  1 115 ? 13.695 -3.806  6.744   0.50 8.23   ? 114 TYR A C   1 
ATOM   1006 C  C   B TYR A  1 115 ? 13.582 -3.857  6.795   0.50 8.21   ? 114 TYR A C   1 
ATOM   1007 O  O   A TYR A  1 115 ? 14.054 -4.709  5.969   0.50 9.02   ? 114 TYR A O   1 
ATOM   1008 O  O   B TYR A  1 115 ? 13.650 -4.849  6.069   0.50 9.75   ? 114 TYR A O   1 
ATOM   1009 C  CB  A TYR A  1 115 ? 15.039 -2.564  8.564   0.50 9.19   ? 114 TYR A CB  1 
ATOM   1010 C  CB  B TYR A  1 115 ? 15.057 -2.676  8.562   0.50 9.93   ? 114 TYR A CB  1 
ATOM   1011 C  CG  A TYR A  1 115 ? 15.132 -2.338  10.063  0.50 7.80   ? 114 TYR A CG  1 
ATOM   1012 C  CG  B TYR A  1 115 ? 15.245 -2.649  10.065  0.50 10.53  ? 114 TYR A CG  1 
ATOM   1013 C  CD1 A TYR A  1 115 ? 15.774 -3.258  10.883  0.50 9.50   ? 114 TYR A CD1 1 
ATOM   1014 C  CD1 B TYR A  1 115 ? 16.164 -3.489  10.681  0.50 13.61  ? 114 TYR A CD1 1 
ATOM   1015 C  CD2 A TYR A  1 115 ? 14.559 -1.222  10.660  0.50 8.18   ? 114 TYR A CD2 1 
ATOM   1016 C  CD2 B TYR A  1 115 ? 14.452 -1.844  10.873  0.50 13.04  ? 114 TYR A CD2 1 
ATOM   1017 C  CE1 A TYR A  1 115 ? 15.855 -3.067  12.252  0.50 10.76  ? 114 TYR A CE1 1 
ATOM   1018 C  CE1 B TYR A  1 115 ? 16.320 -3.497  12.055  0.50 16.08  ? 114 TYR A CE1 1 
ATOM   1019 C  CE2 A TYR A  1 115 ? 14.635 -1.022  12.029  0.50 10.13  ? 114 TYR A CE2 1 
ATOM   1020 C  CE2 B TYR A  1 115 ? 14.601 -1.845  12.250  0.50 18.28  ? 114 TYR A CE2 1 
ATOM   1021 C  CZ  A TYR A  1 115 ? 15.285 -1.947  12.822  0.50 12.25  ? 114 TYR A CZ  1 
ATOM   1022 C  CZ  B TYR A  1 115 ? 15.537 -2.674  12.835  0.50 16.25  ? 114 TYR A CZ  1 
ATOM   1023 O  OH  A TYR A  1 115 ? 15.364 -1.757  14.189  0.50 14.09  ? 114 TYR A OH  1 
ATOM   1024 O  OH  B TYR A  1 115 ? 15.689 -2.687  14.206  0.50 23.84  ? 114 TYR A OH  1 
ATOM   1025 N  N   A SER A  1 116 ? 12.927 -2.796  6.337   0.50 8.11   ? 115 SER A N   1 
ATOM   1026 N  N   B SER A  1 116 ? 12.986 -2.740  6.422   0.50 8.29   ? 115 SER A N   1 
ATOM   1027 C  CA  A SER A  1 116 ? 12.290 -2.841  5.003   0.50 9.16   ? 115 SER A CA  1 
ATOM   1028 C  CA  B SER A  1 116 ? 12.269 -2.693  5.148   0.50 7.88   ? 115 SER A CA  1 
ATOM   1029 C  C   A SER A  1 116 ? 13.159 -2.221  3.937   0.50 8.57   ? 115 SER A C   1 
ATOM   1030 C  C   B SER A  1 116 ? 13.176 -2.264  3.999   0.50 8.21   ? 115 SER A C   1 
ATOM   1031 O  O   A SER A  1 116 ? 12.771 -2.350  2.765   0.50 8.24   ? 115 SER A O   1 
ATOM   1032 O  O   B SER A  1 116 ? 12.953 -2.653  2.841   0.50 10.03  ? 115 SER A O   1 
ATOM   1033 C  CB  A SER A  1 116 ? 10.984 -1.994  4.956   0.50 10.68  ? 115 SER A CB  1 
ATOM   1034 C  CB  B SER A  1 116 ? 11.019 -1.827  5.294   0.50 7.27   ? 115 SER A CB  1 
ATOM   1035 O  OG  A SER A  1 116 ? 10.136 -2.483  5.930   0.50 11.46  ? 115 SER A OG  1 
ATOM   1036 O  OG  B SER A  1 116 ? 11.263 -0.499  5.384   0.50 8.45   ? 115 SER A OG  1 
ATOM   1037 N  N   . ALA A  1 117 ? 14.242 -1.513  4.295   1.00 8.21   ? 116 ALA A N   1 
ATOM   1038 C  CA  . ALA A  1 117 ? 15.150 -0.979  3.258   1.00 7.41   ? 116 ALA A CA  1 
ATOM   1039 C  C   . ALA A  1 117 ? 16.406 -0.530  3.985   1.00 6.89   ? 116 ALA A C   1 
ATOM   1040 O  O   . ALA A  1 117 ? 16.457 -0.568  5.232   1.00 7.37   ? 116 ALA A O   1 
ATOM   1041 C  CB  . ALA A  1 117 ? 14.524 0.141   2.455   1.00 7.85   ? 116 ALA A CB  1 
ATOM   1042 N  N   . GLU A  1 118 ? 17.400 -0.088  3.235   1.00 7.07   ? 117 GLU A N   1 
ATOM   1043 C  CA  . GLU A  1 118 ? 18.636 0.398   3.847   1.00 6.61   ? 117 GLU A CA  1 
ATOM   1044 C  C   . GLU A  1 118 ? 19.212 1.460   2.934   1.00 6.45   ? 117 GLU A C   1 
ATOM   1045 O  O   . GLU A  1 118 ? 19.236 1.293   1.719   1.00 7.87   ? 117 GLU A O   1 
ATOM   1046 C  CB  . GLU A  1 118 ? 19.605 -0.781  4.043   1.00 7.70   ? 117 GLU A CB  1 
ATOM   1047 C  CG  . GLU A  1 118 ? 20.871 -0.422  4.802   1.00 7.96   ? 117 GLU A CG  1 
ATOM   1048 C  CD  . GLU A  1 118 ? 21.653 -1.653  5.218   1.00 7.39   ? 117 GLU A CD  1 
ATOM   1049 O  OE1 . GLU A  1 118 ? 22.894 -1.591  5.277   1.00 8.53   ? 117 GLU A OE1 1 
ATOM   1050 O  OE2 . GLU A  1 118 ? 21.005 -2.684  5.534   1.00 8.63   ? 117 GLU A OE2 1 
ATOM   1051 N  N   . LEU A  1 119 ? 19.684 2.556   3.553   1.00 6.50   ? 118 LEU A N   1 
ATOM   1052 C  CA  . LEU A  1 119 ? 20.386 3.635   2.870   1.00 6.69   ? 118 LEU A CA  1 
ATOM   1053 C  C   . LEU A  1 119 ? 21.892 3.412   3.020   1.00 6.63   ? 118 LEU A C   1 
ATOM   1054 O  O   . LEU A  1 119 ? 22.357 3.137   4.138   1.00 6.87   ? 118 LEU A O   1 
ATOM   1055 C  CB  . LEU A  1 119 ? 20.011 4.971   3.529   1.00 7.59   ? 118 LEU A CB  1 
ATOM   1056 C  CG  . LEU A  1 119 ? 20.871 6.185   3.239   1.00 7.53   ? 118 LEU A CG  1 
ATOM   1057 C  CD1 . LEU A  1 119 ? 20.795 6.616   1.755   1.00 8.44   ? 118 LEU A CD1 1 
ATOM   1058 C  CD2 . LEU A  1 119 ? 20.468 7.339   4.159   1.00 9.75   ? 118 LEU A CD2 1 
ATOM   1059 N  N   . HIS A  1 120 ? 22.648 3.550   1.913   1.00 6.61   ? 119 HIS A N   1 
ATOM   1060 C  CA  . HIS A  1 120 ? 24.103 3.489   1.906   1.00 6.35   ? 119 HIS A CA  1 
ATOM   1061 C  C   . HIS A  1 120 ? 24.648 4.814   1.432   1.00 6.32   ? 119 HIS A C   1 
ATOM   1062 O  O   . HIS A  1 120 ? 24.316 5.234   0.313   1.00 7.52   ? 119 HIS A O   1 
ATOM   1063 C  CB  . HIS A  1 120 ? 24.593 2.370   1.011   1.00 7.14   ? 119 HIS A CB  1 
ATOM   1064 C  CG  . HIS A  1 120 ? 24.328 1.006   1.592   1.00 6.26   ? 119 HIS A CG  1 
ATOM   1065 N  ND1 . HIS A  1 120 ? 24.385 -0.175  0.875   1.00 7.28   ? 119 HIS A ND1 1 
ATOM   1066 C  CD2 . HIS A  1 120 ? 24.011 0.681   2.876   1.00 7.16   ? 119 HIS A CD2 1 
ATOM   1067 C  CE1 . HIS A  1 120 ? 24.120 -1.193  1.715   1.00 7.32   ? 119 HIS A CE1 1 
ATOM   1068 N  NE2 . HIS A  1 120 ? 23.884 -0.681  2.928   1.00 6.98   ? 119 HIS A NE2 1 
ATOM   1069 N  N   . VAL A  1 121 ? 25.494 5.436   2.225   1.00 6.43   ? 120 VAL A N   1 
ATOM   1070 C  CA  . VAL A  1 121 ? 26.174 6.686   1.839   1.00 6.96   ? 120 VAL A CA  1 
ATOM   1071 C  C   . VAL A  1 121 ? 27.673 6.343   1.712   1.00 6.50   ? 120 VAL A C   1 
ATOM   1072 O  O   . VAL A  1 121 ? 28.286 5.998   2.722   1.00 7.04   ? 120 VAL A O   1 
ATOM   1073 C  CB  . VAL A  1 121 ? 25.934 7.805   2.846   1.00 6.86   ? 120 VAL A CB  1 
ATOM   1074 C  CG1 . VAL A  1 121 ? 26.564 9.104   2.294   1.00 8.18   ? 120 VAL A CG1 1 
ATOM   1075 C  CG2 . VAL A  1 121 ? 24.447 7.976   3.139   1.00 8.73   ? 120 VAL A CG2 1 
ATOM   1076 N  N   . ALA A  1 122 ? 28.180 6.366   0.496   1.00 7.66   ? 121 ALA A N   1 
ATOM   1077 C  CA  . ALA A  1 122 ? 29.499 5.754   0.183   1.00 7.54   ? 121 ALA A CA  1 
ATOM   1078 C  C   . ALA A  1 122 ? 30.550 6.853   -0.043  1.00 7.65   ? 121 ALA A C   1 
ATOM   1079 O  O   . ALA A  1 122 ? 30.287 7.907   -0.623  1.00 8.45   ? 121 ALA A O   1 
ATOM   1080 C  CB  . ALA A  1 122 ? 29.357 4.891   -1.060  1.00 8.81   ? 121 ALA A CB  1 
ATOM   1081 N  N   . HIS A  1 123 ? 31.772 6.501   0.407   1.00 8.04   ? 122 HIS A N   1 
ATOM   1082 C  CA  . HIS A  1 123 ? 32.901 7.449   0.414   1.00 8.22   ? 122 HIS A CA  1 
ATOM   1083 C  C   . HIS A  1 123 ? 34.153 6.677   0.041   1.00 8.07   ? 122 HIS A C   1 
ATOM   1084 O  O   . HIS A  1 123 ? 34.245 5.464   0.289   1.00 9.57   ? 122 HIS A O   1 
ATOM   1085 C  CB  . HIS A  1 123 ? 33.114 8.027   1.818   1.00 8.53   ? 122 HIS A CB  1 
ATOM   1086 C  CG  . HIS A  1 123 ? 31.911 8.533   2.485   1.00 7.82   ? 122 HIS A CG  1 
ATOM   1087 N  ND1 . HIS A  1 123 ? 30.915 7.682   3.000   1.00 7.53   ? 122 HIS A ND1 1 
ATOM   1088 C  CD2 . HIS A  1 123 ? 31.474 9.797   2.790   1.00 8.30   ? 122 HIS A CD2 1 
ATOM   1089 C  CE1 . HIS A  1 123 ? 29.991 8.477   3.582   1.00 7.96   ? 122 HIS A CE1 1 
ATOM   1090 N  NE2 . HIS A  1 123 ? 30.305 9.757   3.476   1.00 7.94   ? 122 HIS A NE2 1 
ATOM   1091 N  N   . TRP A  1 124 ? 35.196 7.397   -0.445  1.00 8.45   ? 123 TRP A N   1 
ATOM   1092 C  CA  . TRP A  1 124 ? 36.463 6.765   -0.726  1.00 8.75   ? 123 TRP A CA  1 
ATOM   1093 C  C   . TRP A  1 124 ? 37.604 7.535   -0.120  1.00 8.51   ? 123 TRP A C   1 
ATOM   1094 O  O   . TRP A  1 124 ? 37.533 8.737   0.138   1.00 10.10  ? 123 TRP A O   1 
ATOM   1095 C  CB  . TRP A  1 124 ? 36.656 6.448   -2.218  1.00 9.86   ? 123 TRP A CB  1 
ATOM   1096 C  CG  . TRP A  1 124 ? 36.797 7.647   -3.133  1.00 9.00   ? 123 TRP A CG  1 
ATOM   1097 C  CD1 . TRP A  1 124 ? 35.811 8.254   -3.814  1.00 9.65   ? 123 TRP A CD1 1 
ATOM   1098 C  CD2 . TRP A  1 124 ? 38.019 8.273   -3.545  1.00 9.55   ? 123 TRP A CD2 1 
ATOM   1099 N  NE1 . TRP A  1 124 ? 36.317 9.259   -4.625  1.00 10.83  ? 123 TRP A NE1 1 
ATOM   1100 C  CE2 . TRP A  1 124 ? 37.681 9.270   -4.469  1.00 10.43  ? 123 TRP A CE2 1 
ATOM   1101 C  CE3 . TRP A  1 124 ? 39.374 8.067   -3.240  1.00 10.99  ? 123 TRP A CE3 1 
ATOM   1102 C  CZ2 . TRP A  1 124 ? 38.658 10.079  -5.081  1.00 11.97  ? 123 TRP A CZ2 1 
ATOM   1103 C  CZ3 . TRP A  1 124 ? 40.357 8.824   -3.856  1.00 12.19  ? 123 TRP A CZ3 1 
ATOM   1104 C  CH2 . TRP A  1 124 ? 39.972 9.826   -4.758  1.00 12.27  ? 123 TRP A CH2 1 
ATOM   1105 N  N   . ASN A  1 125 ? 38.734 6.810   0.133   1.00 9.20   ? 124 ASN A N   1 
ATOM   1106 C  CA  . ASN A  1 125 ? 39.857 7.383   0.880   1.00 9.56   ? 124 ASN A CA  1 
ATOM   1107 C  C   . ASN A  1 125 ? 40.744 8.251   -0.053  1.00 9.44   ? 124 ASN A C   1 
ATOM   1108 O  O   . ASN A  1 125 ? 41.722 7.784   -0.598  1.00 10.97  ? 124 ASN A O   1 
ATOM   1109 C  CB  . ASN A  1 125 ? 40.648 6.252   1.493   1.00 10.58  ? 124 ASN A CB  1 
ATOM   1110 C  CG  . ASN A  1 125 ? 41.656 6.733   2.473   1.00 11.62  ? 124 ASN A CG  1 
ATOM   1111 O  OD1 . ASN A  1 125 ? 42.091 7.913   2.429   1.00 12.33  ? 124 ASN A OD1 1 
ATOM   1112 N  ND2 . ASN A  1 125 ? 42.105 5.844   3.339   1.00 14.28  ? 124 ASN A ND2 1 
ATOM   1113 N  N   . SER A  1 126 ? 40.401 9.527   -0.149  1.00 11.64  ? 125 SER A N   1 
ATOM   1114 C  CA  . SER A  1 126 ? 41.116 10.462  -1.004  1.00 12.64  ? 125 SER A CA  1 
ATOM   1115 C  C   . SER A  1 126 ? 42.343 11.027  -0.274  1.00 14.61  ? 125 SER A C   1 
ATOM   1116 O  O   . SER A  1 126 ? 43.082 11.791  -0.820  1.00 17.11  ? 125 SER A O   1 
ATOM   1117 C  CB  . SER A  1 126 ? 40.226 11.543  -1.505  1.00 15.40  ? 125 SER A CB  1 
ATOM   1118 O  OG  . SER A  1 126 ? 39.757 12.245  -0.355  1.00 16.82  ? 125 SER A OG  1 
ATOM   1119 N  N   . ALA A  1 127 ? 42.576 10.648  1.017   1.00 15.83  ? 126 ALA A N   1 
ATOM   1120 C  CA  . ALA A  1 127 ? 43.799 11.046  1.631   1.00 16.56  ? 126 ALA A CA  1 
ATOM   1121 C  C   . ALA A  1 127 ? 44.918 10.122  1.171   1.00 15.96  ? 126 ALA A C   1 
ATOM   1122 O  O   . ALA A  1 127 ? 46.068 10.500  0.917   1.00 22.33  ? 126 ALA A O   1 
ATOM   1123 C  CB  . ALA A  1 127 ? 43.561 10.962  3.176   1.00 18.85  ? 126 ALA A CB  1 
ATOM   1124 N  N   . LYS A  1 128 ? 44.688 8.832   1.095   1.00 13.72  ? 127 LYS A N   1 
ATOM   1125 C  CA  . LYS A  1 128 ? 45.715 7.840   0.735   1.00 12.21  ? 127 LYS A CA  1 
ATOM   1126 C  C   . LYS A  1 128 ? 45.762 7.572   -0.717  1.00 12.19  ? 127 LYS A C   1 
ATOM   1127 O  O   . LYS A  1 128 ? 46.831 7.220   -1.221  1.00 14.66  ? 127 LYS A O   1 
ATOM   1128 C  CB  . LYS A  1 128 ? 45.422 6.603   1.481   1.00 15.02  ? 127 LYS A CB  1 
ATOM   1129 C  CG  . LYS A  1 128 ? 46.573 5.667   1.476   1.00 20.16  ? 127 LYS A CG  1 
ATOM   1130 C  CD  . LYS A  1 128 ? 46.414 4.615   2.573   1.00 21.70  ? 127 LYS A CD  1 
ATOM   1131 C  CE  . LYS A  1 128 ? 47.353 3.431   2.337   1.00 22.69  ? 127 LYS A CE  1 
ATOM   1132 N  NZ  . LYS A  1 128 ? 47.150 2.490   3.388   1.00 24.37  ? 127 LYS A NZ  1 
ATOM   1133 N  N   . TYR A  1 129 ? 44.659 7.680   -1.449  1.00 10.57  ? 128 TYR A N   1 
ATOM   1134 C  CA  . TYR A  1 129 ? 44.570 7.315   -2.810  1.00 10.74  ? 128 TYR A CA  1 
ATOM   1135 C  C   . TYR A  1 129 ? 44.150 8.477   -3.632  1.00 11.63  ? 128 TYR A C   1 
ATOM   1136 O  O   . TYR A  1 129 ? 43.700 9.483   -3.125  1.00 11.76  ? 128 TYR A O   1 
ATOM   1137 C  CB  . TYR A  1 129 ? 43.644 6.119   -3.016  1.00 11.76  ? 128 TYR A CB  1 
ATOM   1138 C  CG  . TYR A  1 129 ? 44.029 4.978   -2.086  1.00 10.64  ? 128 TYR A CG  1 
ATOM   1139 C  CD1 . TYR A  1 129 ? 45.245 4.290   -2.256  1.00 12.55  ? 128 TYR A CD1 1 
ATOM   1140 C  CD2 . TYR A  1 129 ? 43.213 4.560   -1.048  1.00 10.31  ? 128 TYR A CD2 1 
ATOM   1141 C  CE1 . TYR A  1 129 ? 45.637 3.303   -1.362  1.00 12.42  ? 128 TYR A CE1 1 
ATOM   1142 C  CE2 . TYR A  1 129 ? 43.598 3.576   -0.171  1.00 11.61  ? 128 TYR A CE2 1 
ATOM   1143 C  CZ  . TYR A  1 129 ? 44.811 2.946   -0.328  1.00 11.38  ? 128 TYR A CZ  1 
ATOM   1144 O  OH  . TYR A  1 129 ? 45.236 1.945   0.511   1.00 13.87  ? 128 TYR A OH  1 
ATOM   1145 N  N   . SER A  1 130 ? 44.270 8.360   -4.991  1.00 12.78  ? 129 SER A N   1 
ATOM   1146 C  CA  . SER A  1 130 ? 44.002 9.503   -5.845  1.00 13.05  ? 129 SER A CA  1 
ATOM   1147 C  C   . SER A  1 130 ? 42.822 9.292   -6.755  1.00 13.22  ? 129 SER A C   1 
ATOM   1148 O  O   . SER A  1 130 ? 42.441 10.216  -7.461  1.00 15.32  ? 129 SER A O   1 
ATOM   1149 C  CB  . SER A  1 130 ? 45.237 9.736   -6.762  1.00 14.35  ? 129 SER A CB  1 
ATOM   1150 O  OG  . SER A  1 130 ? 46.255 10.252  -5.930  1.00 14.82  ? 129 SER A OG  1 
ATOM   1151 N  N   . SER A  1 131 ? 42.123 8.133   -6.706  1.00 12.45  ? 130 SER A N   1 
ATOM   1152 C  CA  . SER A  1 131 ? 40.893 7.968   -7.492  1.00 12.04  ? 130 SER A CA  1 
ATOM   1153 C  C   . SER A  1 131 ? 40.109 6.884   -6.752  1.00 11.84  ? 130 SER A C   1 
ATOM   1154 O  O   . SER A  1 131 ? 40.674 5.997   -6.102  1.00 12.18  ? 130 SER A O   1 
ATOM   1155 C  CB  . SER A  1 131 ? 41.223 7.558   -8.942  1.00 14.48  ? 130 SER A CB  1 
ATOM   1156 O  OG  . SER A  1 131 ? 41.859 6.288   -8.975  1.00 15.36  ? 130 SER A OG  1 
ATOM   1157 N  N   . LEU A  1 132 ? 38.825 6.854   -7.022  1.00 11.87  ? 131 LEU A N   1 
ATOM   1158 C  CA  . LEU A  1 132 ? 37.991 5.739   -6.605  1.00 12.30  ? 131 LEU A CA  1 
ATOM   1159 C  C   . LEU A  1 132 ? 38.518 4.449   -7.187  1.00 12.27  ? 131 LEU A C   1 
ATOM   1160 O  O   . LEU A  1 132 ? 38.516 3.437   -6.529  1.00 13.29  ? 131 LEU A O   1 
ATOM   1161 C  CB  . LEU A  1 132 ? 36.526 6.002   -6.996  1.00 12.69  ? 131 LEU A CB  1 
ATOM   1162 C  CG  . LEU A  1 132 ? 35.588 4.859   -6.782  1.00 12.93  ? 131 LEU A CG  1 
ATOM   1163 C  CD1 . LEU A  1 132 ? 35.468 4.452   -5.329  1.00 15.59  ? 131 LEU A CD1 1 
ATOM   1164 C  CD2 . LEU A  1 132 ? 34.170 5.168   -7.275  1.00 14.93  ? 131 LEU A CD2 1 
ATOM   1165 N  N   . ALA A  1 133 ? 38.967 4.498   -8.459  1.00 14.47  ? 132 ALA A N   1 
ATOM   1166 C  CA  . ALA A  1 133 ? 39.435 3.313   -9.150  1.00 16.00  ? 132 ALA A CA  1 
ATOM   1167 C  C   . ALA A  1 133 ? 40.565 2.695   -8.334  1.00 13.92  ? 132 ALA A C   1 
ATOM   1168 O  O   . ALA A  1 133 ? 40.649 1.479   -8.143  1.00 16.99  ? 132 ALA A O   1 
ATOM   1169 C  CB  . ALA A  1 133 ? 39.891 3.646   -10.548 1.00 19.61  ? 132 ALA A CB  1 
ATOM   1170 N  N   . GLU A  1 134 ? 41.513 3.525   -7.886  1.00 13.31  ? 133 GLU A N   1 
ATOM   1171 C  CA  . GLU A  1 134 ? 42.628 3.042   -7.062  1.00 13.22  ? 133 GLU A CA  1 
ATOM   1172 C  C   . GLU A  1 134 ? 42.154 2.535   -5.679  1.00 12.35  ? 133 GLU A C   1 
ATOM   1173 O  O   . GLU A  1 134 ? 42.548 1.498   -5.210  1.00 14.89  ? 133 GLU A O   1 
ATOM   1174 C  CB  . GLU A  1 134 ? 43.630 4.194   -6.910  1.00 13.87  ? 133 GLU A CB  1 
ATOM   1175 C  CG  . GLU A  1 134 ? 44.822 3.846   -6.107  1.00 15.12  ? 133 GLU A CG  1 
ATOM   1176 C  CD  . GLU A  1 134 ? 45.826 4.986   -5.908  1.00 14.50  ? 133 GLU A CD  1 
ATOM   1177 O  OE1 . GLU A  1 134 ? 45.492 6.124   -6.286  1.00 14.30  ? 133 GLU A OE1 1 
ATOM   1178 O  OE2 . GLU A  1 134 ? 46.912 4.762   -5.332  1.00 16.28  ? 133 GLU A OE2 1 
ATOM   1179 N  N   . ALA A  1 135 ? 41.222 3.297   -5.054  1.00 12.58  ? 134 ALA A N   1 
ATOM   1180 C  CA  . ALA A  1 135 ? 40.819 2.985   -3.674  1.00 11.14  ? 134 ALA A CA  1 
ATOM   1181 C  C   . ALA A  1 135 ? 39.930 1.764   -3.582  1.00 10.38  ? 134 ALA A C   1 
ATOM   1182 O  O   . ALA A  1 135 ? 39.864 1.139   -2.506  1.00 11.32  ? 134 ALA A O   1 
ATOM   1183 C  CB  . ALA A  1 135 ? 40.055 4.184   -3.146  1.00 10.91  ? 134 ALA A CB  1 
ATOM   1184 N  N   . ALA A  1 136 ? 39.151 1.472   -4.610  1.00 12.15  ? 135 ALA A N   1 
ATOM   1185 C  CA  . ALA A  1 136 ? 37.998 0.593   -4.403  1.00 13.01  ? 135 ALA A CA  1 
ATOM   1186 C  C   . ALA A  1 136 ? 38.397 -0.834  -4.058  1.00 12.13  ? 135 ALA A C   1 
ATOM   1187 O  O   . ALA A  1 136 ? 37.569 -1.523  -3.481  1.00 12.52  ? 135 ALA A O   1 
ATOM   1188 C  CB  . ALA A  1 136 ? 37.131 0.589   -5.675  1.00 17.94  ? 135 ALA A CB  1 
ATOM   1189 N  N   . SER A  1 137 ? 39.611 -1.268  -4.367  1.00 12.23  ? 136 SER A N   1 
ATOM   1190 C  CA  . SER A  1 137 ? 40.057 -2.632  -4.036  1.00 13.49  ? 136 SER A CA  1 
ATOM   1191 C  C   . SER A  1 137 ? 40.943 -2.679  -2.827  1.00 12.69  ? 136 SER A C   1 
ATOM   1192 O  O   . SER A  1 137 ? 41.508 -3.728  -2.519  1.00 17.01  ? 136 SER A O   1 
ATOM   1193 C  CB  . SER A  1 137 ? 40.714 -3.317  -5.200  1.00 19.33  ? 136 SER A CB  1 
ATOM   1194 O  OG  . SER A  1 137 ? 41.807 -2.493  -5.571  1.00 24.41  ? 136 SER A OG  1 
ATOM   1195 N  N   A LYS A  1 138 ? 41.142 -1.554  -2.125  0.50 11.82  ? 137 LYS A N   1 
ATOM   1196 N  N   B LYS A  1 138 ? 41.165 -1.555  -2.124  0.50 11.94  ? 137 LYS A N   1 
ATOM   1197 C  CA  A LYS A  1 138 ? 42.090 -1.465  -1.008  0.50 10.85  ? 137 LYS A CA  1 
ATOM   1198 C  CA  B LYS A  1 138 ? 42.109 -1.482  -0.996  0.50 11.76  ? 137 LYS A CA  1 
ATOM   1199 C  C   A LYS A  1 138 ? 41.334 -1.724  0.309   0.50 10.23  ? 137 LYS A C   1 
ATOM   1200 C  C   B LYS A  1 138 ? 41.337 -1.732  0.308   0.50 9.91   ? 137 LYS A C   1 
ATOM   1201 O  O   A LYS A  1 138 ? 40.217 -1.222  0.471   0.50 10.57  ? 137 LYS A O   1 
ATOM   1202 O  O   B LYS A  1 138 ? 40.233 -1.204  0.472   0.50 10.55  ? 137 LYS A O   1 
ATOM   1203 C  CB  A LYS A  1 138 ? 42.728 -0.061  -0.980  0.50 11.53  ? 137 LYS A CB  1 
ATOM   1204 C  CB  B LYS A  1 138 ? 42.748 -0.086  -0.924  0.50 12.79  ? 137 LYS A CB  1 
ATOM   1205 C  CG  A LYS A  1 138 ? 43.429 0.314   -2.294  0.50 13.23  ? 137 LYS A CG  1 
ATOM   1206 C  CG  B LYS A  1 138 ? 43.498 0.345   -2.194  0.50 13.65  ? 137 LYS A CG  1 
ATOM   1207 C  CD  A LYS A  1 138 ? 44.616 -0.627  -2.565  0.50 15.45  ? 137 LYS A CD  1 
ATOM   1208 C  CD  B LYS A  1 138 ? 44.664 -0.591  -2.537  0.50 17.49  ? 137 LYS A CD  1 
ATOM   1209 C  CE  A LYS A  1 138 ? 45.448 -0.136  -3.739  0.50 14.79  ? 137 LYS A CE  1 
ATOM   1210 C  CE  B LYS A  1 138 ? 45.495 0.089   -3.616  0.50 19.93  ? 137 LYS A CE  1 
ATOM   1211 N  NZ  A LYS A  1 138 ? 44.676 -0.229  -5.013  0.50 13.85  ? 137 LYS A NZ  1 
ATOM   1212 N  NZ  B LYS A  1 138 ? 46.597 -0.794  -4.049  0.50 23.19  ? 137 LYS A NZ  1 
ATOM   1213 N  N   . ALA A  1 139 ? 41.924 -2.414  1.276   1.00 12.25  ? 138 ALA A N   1 
ATOM   1214 C  CA  . ALA A  1 139 ? 41.208 -2.699  2.524   1.00 12.20  ? 138 ALA A CA  1 
ATOM   1215 C  C   . ALA A  1 139 ? 40.760 -1.444  3.215   1.00 10.92  ? 138 ALA A C   1 
ATOM   1216 O  O   . ALA A  1 139 ? 39.690 -1.502  3.869   1.00 11.83  ? 138 ALA A O   1 
ATOM   1217 C  CB  . ALA A  1 139 ? 42.174 -3.482  3.442   1.00 14.62  ? 138 ALA A CB  1 
ATOM   1218 N  N   . ASP A  1 140 ? 41.485 -0.331  3.131   1.00 10.94  ? 139 ASP A N   1 
ATOM   1219 C  CA  . ASP A  1 140 ? 41.169 0.906   3.735   1.00 10.32  ? 139 ASP A CA  1 
ATOM   1220 C  C   . ASP A  1 140 ? 40.597 1.885   2.744   1.00 9.84   ? 139 ASP A C   1 
ATOM   1221 O  O   . ASP A  1 140 ? 40.569 3.094   2.976   1.00 10.83  ? 139 ASP A O   1 
ATOM   1222 C  CB  . ASP A  1 140 ? 42.357 1.548   4.470   1.00 12.60  ? 139 ASP A CB  1 
ATOM   1223 C  CG  . ASP A  1 140 ? 43.551 1.771   3.527   1.00 12.79  ? 139 ASP A CG  1 
ATOM   1224 O  OD1 . ASP A  1 140 ? 43.462 1.387   2.312   1.00 13.20  ? 139 ASP A OD1 1 
ATOM   1225 O  OD2 . ASP A  1 140 ? 44.526 2.332   3.984   1.00 18.41  ? 139 ASP A OD2 1 
ATOM   1226 N  N   . GLY A  1 141 ? 40.101 1.395   1.585   1.00 9.74   ? 140 GLY A N   1 
ATOM   1227 C  CA  . GLY A  1 141 ? 39.760 2.308   0.494   1.00 8.71   ? 140 GLY A CA  1 
ATOM   1228 C  C   . GLY A  1 141 ? 38.417 2.959   0.592   1.00 8.39   ? 140 GLY A C   1 
ATOM   1229 O  O   . GLY A  1 141 ? 38.241 4.107   0.140   1.00 9.29   ? 140 GLY A O   1 
ATOM   1230 N  N   . LEU A  1 142 ? 37.381 2.266   1.140   1.00 8.51   ? 141 LEU A N   1 
ATOM   1231 C  CA  . LEU A  1 142 ? 36.016 2.766   1.090   1.00 8.47   ? 141 LEU A CA  1 
ATOM   1232 C  C   . LEU A  1 142 ? 35.411 2.835   2.495   1.00 7.82   ? 141 LEU A C   1 
ATOM   1233 O  O   . LEU A  1 142 ? 35.772 2.052   3.399   1.00 8.12   ? 141 LEU A O   1 
ATOM   1234 C  CB  . LEU A  1 142 ? 35.120 1.832   0.222   1.00 8.88   ? 141 LEU A CB  1 
ATOM   1235 C  CG  . LEU A  1 142 ? 35.634 1.639   -1.239  1.00 9.69   ? 141 LEU A CG  1 
ATOM   1236 C  CD1 . LEU A  1 142 ? 34.649 0.717   -1.940  1.00 11.11  ? 141 LEU A CD1 1 
ATOM   1237 C  CD2 . LEU A  1 142 ? 35.758 2.959   -1.989  1.00 11.63  ? 141 LEU A CD2 1 
ATOM   1238 N  N   . ALA A  1 143 ? 34.447 3.720   2.657   1.00 8.30   ? 142 ALA A N   1 
ATOM   1239 C  CA  . ALA A  1 143 ? 33.690 3.821   3.940   1.00 8.45   ? 142 ALA A CA  1 
ATOM   1240 C  C   . ALA A  1 143 ? 32.236 3.995   3.546   1.00 7.72   ? 142 ALA A C   1 
ATOM   1241 O  O   . ALA A  1 143 ? 31.950 4.925   2.761   1.00 8.41   ? 142 ALA A O   1 
ATOM   1242 C  CB  . ALA A  1 143 ? 34.194 4.974   4.758   1.00 9.72   ? 142 ALA A CB  1 
ATOM   1243 N  N   . VAL A  1 144 ? 31.352 3.225   4.142   1.00 7.22   ? 143 VAL A N   1 
ATOM   1244 C  CA  . VAL A  1 144 ? 29.936 3.339   3.809   1.00 7.14   ? 143 VAL A CA  1 
ATOM   1245 C  C   . VAL A  1 144 ? 29.179 3.460   5.128   1.00 6.51   ? 143 VAL A C   1 
ATOM   1246 O  O   . VAL A  1 144 ? 29.338 2.668   6.034   1.00 7.30   ? 143 VAL A O   1 
ATOM   1247 C  CB  . VAL A  1 144 ? 29.409 2.182   2.934   1.00 7.62   ? 143 VAL A CB  1 
ATOM   1248 C  CG1 . VAL A  1 144 ? 27.963 2.415   2.544   1.00 8.91   ? 143 VAL A CG1 1 
ATOM   1249 C  CG2 . VAL A  1 144 ? 30.246 1.995   1.677   1.00 9.32   ? 143 VAL A CG2 1 
ATOM   1250 N  N   . ILE A  1 145 ? 28.304 4.478   5.183   1.00 6.78   ? 144 ILE A N   1 
ATOM   1251 C  CA  . ILE A  1 145 ? 27.329 4.623   6.270   1.00 6.84   ? 144 ILE A CA  1 
ATOM   1252 C  C   . ILE A  1 145 ? 26.078 3.904   5.865   1.00 6.88   ? 144 ILE A C   1 
ATOM   1253 O  O   . ILE A  1 145 ? 25.502 4.186   4.802   1.00 7.78   ? 144 ILE A O   1 
ATOM   1254 C  CB  . ILE A  1 145 ? 27.028 6.065   6.588   1.00 7.43   ? 144 ILE A CB  1 
ATOM   1255 C  CG1 . ILE A  1 145 ? 28.307 6.874   6.935   1.00 9.66   ? 144 ILE A CG1 1 
ATOM   1256 C  CG2 . ILE A  1 145 ? 25.994 6.171   7.714   1.00 8.78   ? 144 ILE A CG2 1 
ATOM   1257 C  CD1 . ILE A  1 145 ? 28.033 8.363   6.992   1.00 10.94  ? 144 ILE A CD1 1 
ATOM   1258 N  N   . GLY A  1 146 ? 25.617 2.951   6.695   1.00 7.38   ? 145 GLY A N   1 
ATOM   1259 C  CA  . GLY A  1 146 ? 24.334 2.300   6.484   1.00 6.72   ? 145 GLY A CA  1 
ATOM   1260 C  C   . GLY A  1 146 ? 23.320 2.734   7.482   1.00 7.19   ? 145 GLY A C   1 
ATOM   1261 O  O   . GLY A  1 146 ? 23.621 2.828   8.695   1.00 7.95   ? 145 GLY A O   1 
ATOM   1262 N  N   . VAL A  1 147 ? 22.120 2.994   7.008   1.00 6.76   ? 146 VAL A N   1 
ATOM   1263 C  CA  . VAL A  1 147 ? 21.003 3.383   7.842   1.00 7.56   ? 146 VAL A CA  1 
ATOM   1264 C  C   . VAL A  1 147 ? 19.839 2.444   7.583   1.00 6.46   ? 146 VAL A C   1 
ATOM   1265 O  O   . VAL A  1 147 ? 19.370 2.337   6.415   1.00 7.91   ? 146 VAL A O   1 
ATOM   1266 C  CB  . VAL A  1 147 ? 20.560 4.839   7.633   1.00 7.36   ? 146 VAL A CB  1 
ATOM   1267 C  CG1 . VAL A  1 147 ? 19.465 5.196   8.623   1.00 9.76   ? 146 VAL A CG1 1 
ATOM   1268 C  CG2 . VAL A  1 147 ? 21.749 5.801   7.726   1.00 8.76   ? 146 VAL A CG2 1 
ATOM   1269 N  N   A LEU A  1 148 ? 19.387 1.724   8.600   0.50 7.02   ? 147 LEU A N   1 
ATOM   1270 N  N   B LEU A  1 148 ? 19.382 1.746   8.602   0.50 7.06   ? 147 LEU A N   1 
ATOM   1271 C  CA  A LEU A  1 148 ? 18.215 0.863   8.472   0.50 7.29   ? 147 LEU A CA  1 
ATOM   1272 C  CA  B LEU A  1 148 ? 18.254 0.854   8.469   0.50 7.64   ? 147 LEU A CA  1 
ATOM   1273 C  C   A LEU A  1 148 ? 16.947 1.699   8.356   0.50 7.08   ? 147 LEU A C   1 
ATOM   1274 C  C   B LEU A  1 148 ? 16.955 1.680   8.364   0.50 7.06   ? 147 LEU A C   1 
ATOM   1275 O  O   A LEU A  1 148 ? 16.804 2.698   9.066   0.50 8.21   ? 147 LEU A O   1 
ATOM   1276 O  O   B LEU A  1 148 ? 16.805 2.670   9.087   0.50 8.28   ? 147 LEU A O   1 
ATOM   1277 C  CB  A LEU A  1 148 ? 18.092 -0.117  9.652   0.50 8.35   ? 147 LEU A CB  1 
ATOM   1278 C  CB  B LEU A  1 148 ? 18.241 -0.028  9.707   0.50 8.19   ? 147 LEU A CB  1 
ATOM   1279 C  CG  A LEU A  1 148 ? 19.366 -0.958  9.673   0.50 8.44   ? 147 LEU A CG  1 
ATOM   1280 C  CG  B LEU A  1 148 ? 19.318 -1.138  9.808   0.50 13.10  ? 147 LEU A CG  1 
ATOM   1281 C  CD1 A LEU A  1 148 ? 19.709 -1.506  11.064  0.50 12.74  ? 147 LEU A CD1 1 
ATOM   1282 C  CD1 B LEU A  1 148 ? 20.682 -0.719  9.925   0.50 18.23  ? 147 LEU A CD1 1 
ATOM   1283 C  CD2 A LEU A  1 148 ? 19.287 -2.077  8.657   0.50 7.19   ? 147 LEU A CD2 1 
ATOM   1284 C  CD2 B LEU A  1 148 ? 19.167 -1.703  11.176  0.50 16.12  ? 147 LEU A CD2 1 
ATOM   1285 N  N   . MET A  1 149 ? 16.035 1.233   7.499   1.00 7.72   ? 148 MET A N   1 
ATOM   1286 C  CA  . MET A  1 149 ? 14.818 1.992   7.213   1.00 7.59   ? 148 MET A CA  1 
ATOM   1287 C  C   . MET A  1 149 ? 13.642 1.148   7.647   1.00 7.76   ? 148 MET A C   1 
ATOM   1288 O  O   . MET A  1 149 ? 13.422 0.042   7.134   1.00 8.53   ? 148 MET A O   1 
ATOM   1289 C  CB  . MET A  1 149 ? 14.743 2.367   5.756   1.00 7.75   ? 148 MET A CB  1 
ATOM   1290 C  CG  . MET A  1 149 ? 15.942 3.214   5.344   1.00 7.93   ? 148 MET A CG  1 
ATOM   1291 S  SD  . MET A  1 149 ? 16.067 3.577   3.577   1.00 8.40   ? 148 MET A SD  1 
ATOM   1292 C  CE  . MET A  1 149 ? 14.592 4.505   3.269   1.00 11.65  ? 148 MET A CE  1 
ATOM   1293 N  N   . LYS A  1 150 ? 12.914 1.658   8.651   1.00 8.46   ? 149 LYS A N   1 
ATOM   1294 C  CA  . LYS A  1 150 ? 11.815 0.934   9.302   1.00 9.13   ? 149 LYS A CA  1 
ATOM   1295 C  C   . LYS A  1 150 ? 10.500 1.379   8.692   1.00 8.50   ? 149 LYS A C   1 
ATOM   1296 O  O   . LYS A  1 150 ? 10.167 2.593   8.699   1.00 9.05   ? 149 LYS A O   1 
ATOM   1297 C  CB  . LYS A  1 150 ? 11.832 1.286   10.785  1.00 10.08  ? 149 LYS A CB  1 
ATOM   1298 C  CG  . LYS A  1 150 ? 10.743 0.576   11.547  1.00 12.35  ? 149 LYS A CG  1 
ATOM   1299 C  CD  . LYS A  1 150 ? 10.856 0.877   13.119  1.00 16.68  ? 149 LYS A CD  1 
ATOM   1300 C  CE  . LYS A  1 150 ? 9.602  0.186   13.829  1.00 22.31  ? 149 LYS A CE  1 
ATOM   1301 N  NZ  . LYS A  1 150 ? 9.452  -1.254  13.643  1.00 29.06  ? 149 LYS A NZ  1 
ATOM   1302 N  N   . VAL A  1 151 ? 9.702  0.442   8.182   1.00 8.78   ? 150 VAL A N   1 
ATOM   1303 C  CA  . VAL A  1 151 ? 8.442  0.829   7.522   1.00 8.92   ? 150 VAL A CA  1 
ATOM   1304 C  C   . VAL A  1 151 ? 7.504  1.422   8.564   1.00 9.34   ? 150 VAL A C   1 
ATOM   1305 O  O   . VAL A  1 151 ? 7.372  0.922   9.691   1.00 10.96  ? 150 VAL A O   1 
ATOM   1306 C  CB  . VAL A  1 151 ? 7.870  -0.360  6.758   1.00 10.12  ? 150 VAL A CB  1 
ATOM   1307 C  CG1 . VAL A  1 151 ? 7.395  -1.543  7.633   1.00 12.51  ? 150 VAL A CG1 1 
ATOM   1308 C  CG2 . VAL A  1 151 ? 6.744  0.169   5.829   1.00 12.65  ? 150 VAL A CG2 1 
ATOM   1309 N  N   . GLY A  1 152 ? 6.849  2.507   8.153   1.00 9.69   ? 151 GLY A N   1 
ATOM   1310 C  CA  . GLY A  1 152 ? 5.958  3.211   9.078   1.00 11.51  ? 151 GLY A CA  1 
ATOM   1311 C  C   . GLY A  1 152 ? 5.478  4.485   8.374   1.00 10.40  ? 151 GLY A C   1 
ATOM   1312 O  O   . GLY A  1 152 ? 5.040  4.459   7.227   1.00 11.52  ? 151 GLY A O   1 
ATOM   1313 N  N   . GLU A  1 153 ? 5.642  5.600   9.035   1.00 10.88  ? 152 GLU A N   1 
ATOM   1314 C  CA  . GLU A  1 153 ? 5.190  6.856   8.430   1.00 13.11  ? 152 GLU A CA  1 
ATOM   1315 C  C   . GLU A  1 153 ? 6.090  7.225   7.252   1.00 9.74   ? 152 GLU A C   1 
ATOM   1316 O  O   . GLU A  1 153 ? 7.290  6.995   7.224   1.00 10.84  ? 152 GLU A O   1 
ATOM   1317 C  CB  . GLU A  1 153 ? 5.243  7.973   9.480   1.00 19.78  ? 152 GLU A CB  1 
ATOM   1318 C  CG  . GLU A  1 153 ? 4.282  7.684   10.616  1.00 26.43  ? 152 GLU A CG  1 
ATOM   1319 C  CD  . GLU A  1 153 ? 2.812  7.990   10.465  1.00 53.48  ? 152 GLU A CD  1 
ATOM   1320 O  OE1 . GLU A  1 153 ? 2.251  8.298   11.582  1.00 71.49  ? 152 GLU A OE1 1 
ATOM   1321 O  OE2 . GLU A  1 153 ? 2.232  7.963   9.298   1.00 63.35  ? 152 GLU A OE2 1 
ATOM   1322 N  N   . ALA A  1 154 ? 5.509  7.934   6.284   1.00 10.45  ? 153 ALA A N   1 
ATOM   1323 C  CA  . ALA A  1 154 ? 6.275  8.461   5.183   1.00 9.25   ? 153 ALA A CA  1 
ATOM   1324 C  C   . ALA A  1 154 ? 7.365  9.372   5.701   1.00 9.22   ? 153 ALA A C   1 
ATOM   1325 O  O   . ALA A  1 154 ? 7.163  10.155  6.647   1.00 10.79  ? 153 ALA A O   1 
ATOM   1326 C  CB  . ALA A  1 154 ? 5.350  9.255   4.235   1.00 11.38  ? 153 ALA A CB  1 
ATOM   1327 N  N   . ASN A  1 155 ? 8.507  9.308   5.055   1.00 8.64   ? 154 ASN A N   1 
ATOM   1328 C  CA  . ASN A  1 155 ? 9.681  10.081  5.426   1.00 8.70   ? 154 ASN A CA  1 
ATOM   1329 C  C   . ASN A  1 155 ? 9.802  11.248  4.453   1.00 8.82   ? 154 ASN A C   1 
ATOM   1330 O  O   . ASN A  1 155 ? 10.164 11.027  3.277   1.00 9.26   ? 154 ASN A O   1 
ATOM   1331 C  CB  . ASN A  1 155 ? 10.911 9.206   5.350   1.00 9.68   ? 154 ASN A CB  1 
ATOM   1332 C  CG  . ASN A  1 155 ? 12.145 9.899   5.849   1.00 9.26   ? 154 ASN A CG  1 
ATOM   1333 O  OD1 . ASN A  1 155 ? 12.204 11.145  5.841   1.00 11.29  ? 154 ASN A OD1 1 
ATOM   1334 N  ND2 . ASN A  1 155 ? 13.136 9.162   6.234   1.00 9.56   ? 154 ASN A ND2 1 
ATOM   1335 N  N   . PRO A  1 156 ? 9.503  12.477  4.865   1.00 9.67   ? 155 PRO A N   1 
ATOM   1336 C  CA  . PRO A  1 156 ? 9.448  13.546  3.865   1.00 10.97  ? 155 PRO A CA  1 
ATOM   1337 C  C   . PRO A  1 156 ? 10.826 13.872  3.363   1.00 12.02  ? 155 PRO A C   1 
ATOM   1338 O  O   . PRO A  1 156 ? 10.983 14.536  2.308   1.00 13.08  ? 155 PRO A O   1 
ATOM   1339 C  CB  . PRO A  1 156 ? 8.842  14.716  4.634   1.00 14.77  ? 155 PRO A CB  1 
ATOM   1340 C  CG  . PRO A  1 156 ? 9.066  14.446  6.056   1.00 16.69  ? 155 PRO A CG  1 
ATOM   1341 C  CD  . PRO A  1 156 ? 9.062  12.897  6.217   1.00 11.84  ? 155 PRO A CD  1 
ATOM   1342 N  N   A LYS A  1 157 ? 11.898 13.537  4.110   0.50 9.95   ? 156 LYS A N   1 
ATOM   1343 N  N   B LYS A  1 157 ? 11.891 13.497  4.061   0.50 9.94   ? 156 LYS A N   1 
ATOM   1344 C  CA  A LYS A  1 157 ? 13.288 13.732  3.701   0.50 11.27  ? 156 LYS A CA  1 
ATOM   1345 C  CA  B LYS A  1 157 ? 13.191 13.885  3.594   0.50 11.30  ? 156 LYS A CA  1 
ATOM   1346 C  C   A LYS A  1 157 ? 13.607 13.015  2.382   0.50 9.77   ? 156 LYS A C   1 
ATOM   1347 C  C   B LYS A  1 157 ? 13.595 13.040  2.348   0.50 9.55   ? 156 LYS A C   1 
ATOM   1348 O  O   A LYS A  1 157 ? 14.590 13.339  1.755   0.50 12.11  ? 156 LYS A O   1 
ATOM   1349 O  O   B LYS A  1 157 ? 14.544 13.381  1.663   0.50 12.59  ? 156 LYS A O   1 
ATOM   1350 C  CB  A LYS A  1 157 ? 14.298 13.191  4.731   0.50 14.23  ? 156 LYS A CB  1 
ATOM   1351 C  CB  B LYS A  1 157 ? 14.207 13.804  4.702   0.50 15.83  ? 156 LYS A CB  1 
ATOM   1352 C  CG  A LYS A  1 157 ? 14.164 13.709  6.083   0.50 15.95  ? 156 LYS A CG  1 
ATOM   1353 C  CG  B LYS A  1 157 ? 13.838 14.681  5.880   0.50 19.72  ? 156 LYS A CG  1 
ATOM   1354 C  CD  A LYS A  1 157 ? 14.539 15.191  6.159   0.50 19.15  ? 156 LYS A CD  1 
ATOM   1355 C  CD  B LYS A  1 157 ? 14.829 14.071  6.888   0.50 19.14  ? 156 LYS A CD  1 
ATOM   1356 C  CE  A LYS A  1 157 ? 14.891 15.566  7.520   0.50 16.45  ? 156 LYS A CE  1 
ATOM   1357 C  CE  B LYS A  1 157 ? 14.721 14.685  8.132   0.50 23.64  ? 156 LYS A CE  1 
ATOM   1358 N  NZ  A LYS A  1 157 ? 15.976 14.781  8.351   0.50 15.08  ? 156 LYS A NZ  1 
ATOM   1359 N  NZ  B LYS A  1 157 ? 16.049 14.578  8.899   0.50 16.34  ? 156 LYS A NZ  1 
ATOM   1360 N  N   . LEU A  1 158 ? 12.869 11.965  2.065   1.00 10.33  ? 157 LEU A N   1 
ATOM   1361 C  CA  . LEU A  1 158 ? 13.064 11.206  0.797   1.00 10.34  ? 157 LEU A CA  1 
ATOM   1362 C  C   . LEU A  1 158 ? 12.426 11.911  -0.391  1.00 11.69  ? 157 LEU A C   1 
ATOM   1363 O  O   . LEU A  1 158 ? 12.648 11.393  -1.503  1.00 11.55  ? 157 LEU A O   1 
ATOM   1364 C  CB  . LEU A  1 158 ? 12.456 9.827   0.950   1.00 11.08  ? 157 LEU A CB  1 
ATOM   1365 C  CG  . LEU A  1 158 ? 13.088 9.004   2.008   1.00 10.94  ? 157 LEU A CG  1 
ATOM   1366 C  CD1 . LEU A  1 158 ? 12.298 7.584   2.113   1.00 12.54  ? 157 LEU A CD1 1 
ATOM   1367 C  CD2 . LEU A  1 158 ? 14.570 8.663   1.770   1.00 14.79  ? 157 LEU A CD2 1 
ATOM   1368 N  N   A GLN A  1 159 ? 11.682 13.011  -0.198  0.50 12.90  ? 158 GLN A N   1 
ATOM   1369 N  N   B GLN A  1 159 ? 11.602 12.960  -0.187  0.50 13.06  ? 158 GLN A N   1 
ATOM   1370 C  CA  A GLN A  1 159 ? 10.816 13.393  -1.337  0.50 15.13  ? 158 GLN A CA  1 
ATOM   1371 C  CA  B GLN A  1 159 ? 10.770 13.457  -1.334  0.50 14.93  ? 158 GLN A CA  1 
ATOM   1372 C  C   A GLN A  1 159 ? 11.609 13.881  -2.555  0.50 12.48  ? 158 GLN A C   1 
ATOM   1373 C  C   B GLN A  1 159 ? 11.610 13.870  -2.549  0.50 12.51  ? 158 GLN A C   1 
ATOM   1374 O  O   A GLN A  1 159 ? 11.199 13.578  -3.675  0.50 12.25  ? 158 GLN A O   1 
ATOM   1375 O  O   B GLN A  1 159 ? 11.212 13.533  -3.664  0.50 12.41  ? 158 GLN A O   1 
ATOM   1376 C  CB  A GLN A  1 159 ? 9.776  14.345  -0.823  0.50 16.55  ? 158 GLN A CB  1 
ATOM   1377 C  CB  B GLN A  1 159 ? 9.916  14.600  -0.821  0.50 18.35  ? 158 GLN A CB  1 
ATOM   1378 C  CG  A GLN A  1 159 ? 8.747  14.594  -1.930  0.50 16.79  ? 158 GLN A CG  1 
ATOM   1379 C  CG  B GLN A  1 159 ? 8.848  15.017  -1.875  0.50 20.91  ? 158 GLN A CG  1 
ATOM   1380 C  CD  A GLN A  1 159 ? 7.857  15.742  -1.588  0.50 14.84  ? 158 GLN A CD  1 
ATOM   1381 C  CD  B GLN A  1 159 ? 7.775  13.923  -1.989  0.50 20.83  ? 158 GLN A CD  1 
ATOM   1382 O  OE1 A GLN A  1 159 ? 7.448  15.967  -0.411  0.50 12.67  ? 158 GLN A OE1 1 
ATOM   1383 O  OE1 B GLN A  1 159 ? 6.948  13.727  -1.064  0.50 23.14  ? 158 GLN A OE1 1 
ATOM   1384 N  NE2 A GLN A  1 159 ? 7.469  16.459  -2.569  0.50 13.29  ? 158 GLN A NE2 1 
ATOM   1385 N  NE2 B GLN A  1 159 ? 7.857  13.126  -3.032  0.50 19.52  ? 158 GLN A NE2 1 
ATOM   1386 N  N   . LYS A  1 160 ? 12.730 14.562  -2.417  1.00 12.48  ? 159 LYS A N   1 
ATOM   1387 C  CA  . LYS A  1 160 ? 13.483 15.017  -3.588  1.00 13.34  ? 159 LYS A CA  1 
ATOM   1388 C  C   . LYS A  1 160 ? 13.912 13.817  -4.361  1.00 11.30  ? 159 LYS A C   1 
ATOM   1389 O  O   . LYS A  1 160 ? 13.849 13.807  -5.590  1.00 13.10  ? 159 LYS A O   1 
ATOM   1390 C  CB  . LYS A  1 160 ? 14.663 15.930  -3.183  1.00 15.60  ? 159 LYS A CB  1 
ATOM   1391 C  CG  . LYS A  1 160 ? 15.410 16.484  -4.456  1.00 17.89  ? 159 LYS A CG  1 
ATOM   1392 C  CD  . LYS A  1 160 ? 16.813 17.142  -4.157  1.00 19.34  ? 159 LYS A CD  1 
ATOM   1393 C  CE  . LYS A  1 160 ? 17.654 17.495  -5.418  1.00 18.67  ? 159 LYS A CE  1 
ATOM   1394 N  NZ  . LYS A  1 160 ? 17.115 18.784  -5.897  1.00 22.55  ? 159 LYS A NZ  1 
ATOM   1395 N  N   . VAL A  1 161 ? 14.456 12.760  -3.633  1.00 10.99  ? 160 VAL A N   1 
ATOM   1396 C  CA  . VAL A  1 161 ? 14.891 11.586  -4.322  1.00 10.11  ? 160 VAL A CA  1 
ATOM   1397 C  C   . VAL A  1 161 ? 13.740 10.907  -5.045  1.00 9.22   ? 160 VAL A C   1 
ATOM   1398 O  O   . VAL A  1 161 ? 13.828 10.566  -6.226  1.00 10.56  ? 160 VAL A O   1 
ATOM   1399 C  CB  . VAL A  1 161 ? 15.565 10.622  -3.347  1.00 10.36  ? 160 VAL A CB  1 
ATOM   1400 C  CG1 . VAL A  1 161 ? 15.761 9.282   -4.001  1.00 15.52  ? 160 VAL A CG1 1 
ATOM   1401 C  CG2 . VAL A  1 161 ? 16.791 11.191  -2.760  1.00 15.56  ? 160 VAL A CG2 1 
ATOM   1402 N  N   . LEU A  1 162 ? 12.611 10.699  -4.356  1.00 9.35   ? 161 LEU A N   1 
ATOM   1403 C  CA  . LEU A  1 162 ? 11.494 9.956   -4.951  1.00 9.66   ? 161 LEU A CA  1 
ATOM   1404 C  C   . LEU A  1 162 ? 10.921 10.754  -6.109  1.00 9.99   ? 161 LEU A C   1 
ATOM   1405 O  O   . LEU A  1 162 ? 10.567 10.121  -7.125  1.00 11.27  ? 161 LEU A O   1 
ATOM   1406 C  CB  . LEU A  1 162 ? 10.456 9.716   -3.872  1.00 12.09  ? 161 LEU A CB  1 
ATOM   1407 C  CG  . LEU A  1 162 ? 10.897 8.760   -2.746  1.00 11.76  ? 161 LEU A CG  1 
ATOM   1408 C  CD1 . LEU A  1 162 ? 9.952  8.762   -1.602  1.00 15.94  ? 161 LEU A CD1 1 
ATOM   1409 C  CD2 . LEU A  1 162 ? 11.069 7.391   -3.332  1.00 17.13  ? 161 LEU A CD2 1 
ATOM   1410 N  N   . ASP A  1 163 ? 10.835 12.065  -6.048  1.00 10.53  ? 162 ASP A N   1 
ATOM   1411 C  CA  . ASP A  1 163 ? 10.289 12.863  -7.114  1.00 11.38  ? 162 ASP A CA  1 
ATOM   1412 C  C   . ASP A  1 163 ? 11.183 12.771  -8.341  1.00 10.71  ? 162 ASP A C   1 
ATOM   1413 O  O   . ASP A  1 163 ? 10.701 13.014  -9.450  1.00 13.16  ? 162 ASP A O   1 
ATOM   1414 C  CB  . ASP A  1 163 ? 10.112 14.321  -6.684  1.00 13.32  ? 162 ASP A CB  1 
ATOM   1415 C  CG  . ASP A  1 163 ? 8.891  14.597  -5.751  1.00 14.55  ? 162 ASP A CG  1 
ATOM   1416 O  OD1 . ASP A  1 163 ? 8.090  13.748  -5.539  1.00 17.35  ? 162 ASP A OD1 1 
ATOM   1417 O  OD2 . ASP A  1 163 ? 8.796  15.758  -5.260  1.00 18.48  ? 162 ASP A OD2 1 
ATOM   1418 N  N   . ALA A  1 164 ? 12.477 12.504  -8.158  1.00 9.37   ? 163 ALA A N   1 
ATOM   1419 C  CA  . ALA A  1 164 ? 13.389 12.446  -9.248  1.00 10.01  ? 163 ALA A CA  1 
ATOM   1420 C  C   . ALA A  1 164 ? 13.284 11.160  -10.080 1.00 9.55   ? 163 ALA A C   1 
ATOM   1421 O  O   . ALA A  1 164 ? 13.750 11.103  -11.232 1.00 11.11  ? 163 ALA A O   1 
ATOM   1422 C  CB  . ALA A  1 164 ? 14.847 12.601  -8.785  1.00 11.30  ? 163 ALA A CB  1 
ATOM   1423 N  N   . LEU A  1 165 ? 12.697 10.111  -9.524  1.00 9.49   ? 164 LEU A N   1 
ATOM   1424 C  CA  . LEU A  1 165 ? 12.719 8.796   -10.133 1.00 9.65   ? 164 LEU A CA  1 
ATOM   1425 C  C   . LEU A  1 165 ? 11.980 8.778   -11.448 1.00 9.83   ? 164 LEU A C   1 
ATOM   1426 O  O   . LEU A  1 165 ? 12.325 7.992   -12.365 1.00 10.41  ? 164 LEU A O   1 
ATOM   1427 C  CB  . LEU A  1 165 ? 12.178 7.749   -9.200  1.00 10.00  ? 164 LEU A CB  1 
ATOM   1428 C  CG  . LEU A  1 165 ? 12.971 7.533   -7.908  1.00 10.64  ? 164 LEU A CG  1 
ATOM   1429 C  CD1 . LEU A  1 165 ? 12.324 6.400   -7.116  1.00 12.14  ? 164 LEU A CD1 1 
ATOM   1430 C  CD2 . LEU A  1 165 ? 14.460 7.268   -8.221  1.00 11.96  ? 164 LEU A CD2 1 
ATOM   1431 N  N   . GLN A  1 166 ? 10.933 9.620   -11.616 1.00 10.20  ? 165 GLN A N   1 
ATOM   1432 C  CA  . GLN A  1 166 ? 10.173 9.611   -12.853 1.00 10.75  ? 165 GLN A CA  1 
ATOM   1433 C  C   . GLN A  1 166 ? 11.046 9.955   -14.037 1.00 9.87   ? 165 GLN A C   1 
ATOM   1434 O  O   . GLN A  1 166 ? 10.636 9.595   -15.155 1.00 11.19  ? 165 GLN A O   1 
ATOM   1435 C  CB  . GLN A  1 166 ? 8.939  10.538  -12.741 1.00 12.17  ? 165 GLN A CB  1 
ATOM   1436 C  CG  . GLN A  1 166 ? 9.086  11.893  -12.186 1.00 14.94  ? 165 GLN A CG  1 
ATOM   1437 C  CD  . GLN A  1 166 ? 9.945  12.780  -12.961 1.00 14.26  ? 165 GLN A CD  1 
ATOM   1438 O  OE1 . GLN A  1 166 ? 9.816  12.872  -14.236 1.00 16.73  ? 165 GLN A OE1 1 
ATOM   1439 N  NE2 . GLN A  1 166 ? 10.891 13.526  -12.339 1.00 15.41  ? 165 GLN A NE2 1 
ATOM   1440 N  N   . ALA A  1 167 ? 12.187 10.608  -13.876 1.00 10.24  ? 166 ALA A N   1 
ATOM   1441 C  CA  . ALA A  1 167 ? 13.032 10.950  -15.003 1.00 10.77  ? 166 ALA A CA  1 
ATOM   1442 C  C   . ALA A  1 167 ? 14.087 9.887   -15.298 1.00 10.43  ? 166 ALA A C   1 
ATOM   1443 O  O   . ALA A  1 167 ? 14.822 10.032  -16.303 1.00 11.53  ? 166 ALA A O   1 
ATOM   1444 C  CB  . ALA A  1 167 ? 13.741 12.280  -14.726 1.00 13.41  ? 166 ALA A CB  1 
ATOM   1445 N  N   . ILE A  1 168 ? 14.168 8.838   -14.478 1.00 9.45   ? 167 ILE A N   1 
ATOM   1446 C  CA  . ILE A  1 168 ? 15.210 7.786   -14.683 1.00 9.70   ? 167 ILE A CA  1 
ATOM   1447 C  C   . ILE A  1 168 ? 14.582 6.401   -14.625 1.00 9.30   ? 167 ILE A C   1 
ATOM   1448 O  O   . ILE A  1 168 ? 15.094 5.486   -13.991 1.00 9.86   ? 167 ILE A O   1 
ATOM   1449 C  CB  . ILE A  1 168 ? 16.384 7.957   -13.712 1.00 10.26  ? 167 ILE A CB  1 
ATOM   1450 C  CG1 . ILE A  1 168 ? 15.931 7.840   -12.202 1.00 10.30  ? 167 ILE A CG1 1 
ATOM   1451 C  CG2 . ILE A  1 168 ? 17.118 9.283   -13.990 1.00 12.65  ? 167 ILE A CG2 1 
ATOM   1452 C  CD1 . ILE A  1 168 ? 16.966 7.133   -11.391 1.00 12.44  ? 167 ILE A CD1 1 
ATOM   1453 N  N   . LYS A  1 169 ? 13.399 6.230   -15.303 1.00 9.87   ? 168 LYS A N   1 
ATOM   1454 C  CA  . LYS A  1 169 ? 12.611 5.022   -15.166 1.00 9.74   ? 168 LYS A CA  1 
ATOM   1455 C  C   . LYS A  1 169 ? 13.275 3.743   -15.576 1.00 8.50   ? 168 LYS A C   1 
ATOM   1456 O  O   . LYS A  1 169 ? 13.104 2.709   -14.909 1.00 9.81   ? 168 LYS A O   1 
ATOM   1457 C  CB  . LYS A  1 169 ? 11.285 5.173   -15.922 1.00 11.24  ? 168 LYS A CB  1 
ATOM   1458 C  CG  . LYS A  1 169 ? 10.068 5.294   -15.020 1.00 16.19  ? 168 LYS A CG  1 
ATOM   1459 C  CD  . LYS A  1 169 ? 10.473 5.379   -13.557 1.00 18.93  ? 168 LYS A CD  1 
ATOM   1460 C  CE  . LYS A  1 169 ? 9.902  4.219   -12.758 1.00 19.33  ? 168 LYS A CE  1 
ATOM   1461 N  NZ  . LYS A  1 169 ? 8.605  4.573   -12.119 1.00 26.35  ? 168 LYS A NZ  1 
ATOM   1462 N  N   . THR A  1 170 ? 14.078 3.841   -16.629 1.00 9.30   ? 169 THR A N   1 
ATOM   1463 C  CA  . THR A  1 170 ? 14.676 2.647   -17.236 1.00 8.93   ? 169 THR A CA  1 
ATOM   1464 C  C   . THR A  1 170 ? 16.191 2.696   -17.176 1.00 8.97   ? 169 THR A C   1 
ATOM   1465 O  O   . THR A  1 170 ? 16.820 3.764   -17.027 1.00 9.55   ? 169 THR A O   1 
ATOM   1466 C  CB  . THR A  1 170 ? 14.180 2.499   -18.698 1.00 9.75   ? 169 THR A CB  1 
ATOM   1467 O  OG1 . THR A  1 170 ? 14.385 3.732   -19.362 1.00 10.25  ? 169 THR A OG1 1 
ATOM   1468 C  CG2 . THR A  1 170 ? 12.697 2.152   -18.702 1.00 10.54  ? 169 THR A CG2 1 
ATOM   1469 N  N   . LYS A  1 171 ? 16.784 1.519   -17.383 1.00 9.94   ? 170 LYS A N   1 
ATOM   1470 C  CA  . LYS A  1 171 ? 18.245 1.303   -17.214 1.00 9.67   ? 170 LYS A CA  1 
ATOM   1471 C  C   . LYS A  1 171 ? 19.036 2.248   -18.063 1.00 9.76   ? 170 LYS A C   1 
ATOM   1472 O  O   . LYS A  1 171 ? 18.805 2.370   -19.282 1.00 11.04  ? 170 LYS A O   1 
ATOM   1473 C  CB  . LYS A  1 171 ? 18.562 -0.124  -17.554 1.00 12.01  ? 170 LYS A CB  1 
ATOM   1474 C  CG  . LYS A  1 171 ? 20.064 -0.416  -17.419 1.00 13.24  ? 170 LYS A CG  1 
ATOM   1475 C  CD  . LYS A  1 171 ? 20.299 -1.923  -17.620 1.00 16.15  ? 170 LYS A CD  1 
ATOM   1476 C  CE  . LYS A  1 171 ? 21.748 -2.298  -17.207 1.00 32.37  ? 170 LYS A CE  1 
ATOM   1477 N  NZ  . LYS A  1 171 ? 21.801 -3.765  -16.862 1.00 66.65  ? 170 LYS A NZ  1 
ATOM   1478 N  N   . GLY A  1 172 ? 19.973 2.919   -17.445 1.00 10.24  ? 171 GLY A N   1 
ATOM   1479 C  CA  . GLY A  1 172 ? 20.910 3.811   -18.135 1.00 11.55  ? 171 GLY A CA  1 
ATOM   1480 C  C   . GLY A  1 172 ? 20.459 5.249   -18.171 1.00 11.05  ? 171 GLY A C   1 
ATOM   1481 O  O   . GLY A  1 172 ? 21.269 6.116   -18.454 1.00 12.70  ? 171 GLY A O   1 
ATOM   1482 N  N   . LYS A  1 173 ? 19.168 5.528   -17.872 1.00 9.48   ? 172 LYS A N   1 
ATOM   1483 C  CA  . LYS A  1 173 ? 18.734 6.917   -17.832 1.00 10.55  ? 172 LYS A CA  1 
ATOM   1484 C  C   . LYS A  1 173 ? 19.387 7.635   -16.654 1.00 9.46   ? 172 LYS A C   1 
ATOM   1485 O  O   . LYS A  1 173 ? 19.633 7.052   -15.609 1.00 10.10  ? 172 LYS A O   1 
ATOM   1486 C  CB  . LYS A  1 173 ? 17.240 7.053   -17.742 1.00 11.35  ? 172 LYS A CB  1 
ATOM   1487 C  CG  . LYS A  1 173 ? 16.520 6.636   -19.053 1.00 13.45  ? 172 LYS A CG  1 
ATOM   1488 C  CD  . LYS A  1 173 ? 15.080 7.162   -19.089 1.00 13.68  ? 172 LYS A CD  1 
ATOM   1489 C  CE  . LYS A  1 173 ? 15.013 8.673   -19.302 1.00 14.96  ? 172 LYS A CE  1 
ATOM   1490 N  NZ  . LYS A  1 173 ? 13.672 9.250   -19.266 1.00 16.24  ? 172 LYS A NZ  1 
ATOM   1491 N  N   . ARG A  1 174 ? 19.586 8.923   -16.835 1.00 10.23  ? 173 ARG A N   1 
ATOM   1492 C  CA  . ARG A  1 174 ? 20.209 9.742   -15.811 1.00 9.90   ? 173 ARG A CA  1 
ATOM   1493 C  C   . ARG A  1 174 ? 19.682 11.158  -15.916 1.00 10.10  ? 173 ARG A C   1 
ATOM   1494 O  O   . ARG A  1 174 ? 19.216 11.595  -16.988 1.00 12.65  ? 173 ARG A O   1 
ATOM   1495 C  CB  . ARG A  1 174 ? 21.731 9.731   -15.964 1.00 11.46  ? 173 ARG A CB  1 
ATOM   1496 C  CG  . ARG A  1 174 ? 22.220 10.111  -17.353 1.00 14.67  ? 173 ARG A CG  1 
ATOM   1497 C  CD  . ARG A  1 174 ? 23.590 9.517   -17.636 1.00 16.37  ? 173 ARG A CD  1 
ATOM   1498 N  NE  . ARG A  1 174 ? 23.528 8.074   -17.847 1.00 18.40  ? 173 ARG A NE  1 
ATOM   1499 C  CZ  . ARG A  1 174 ? 24.406 7.208   -17.351 1.00 20.65  ? 173 ARG A CZ  1 
ATOM   1500 N  NH1 . ARG A  1 174 ? 25.418 7.637   -16.611 1.00 23.21  ? 173 ARG A NH1 1 
ATOM   1501 N  NH2 . ARG A  1 174 ? 24.271 5.911   -17.594 1.00 22.63  ? 173 ARG A NH2 1 
ATOM   1502 N  N   . ALA A  1 175 ? 19.831 11.928  -14.855 1.00 10.29  ? 174 ALA A N   1 
ATOM   1503 C  CA  . ALA A  1 175 ? 19.311 13.309  -14.832 1.00 11.60  ? 174 ALA A CA  1 
ATOM   1504 C  C   . ALA A  1 175 ? 20.094 14.101  -13.830 1.00 10.81  ? 174 ALA A C   1 
ATOM   1505 O  O   . ALA A  1 175 ? 20.575 13.564  -12.831 1.00 10.26  ? 174 ALA A O   1 
ATOM   1506 C  CB  . ALA A  1 175 ? 17.847 13.376  -14.449 1.00 13.19  ? 174 ALA A CB  1 
ATOM   1507 N  N   A PRO A  1 176 ? 20.342 15.397  -14.048 0.50 10.19  ? 175 PRO A N   1 
ATOM   1508 N  N   B PRO A  1 176 ? 20.073 15.441  -13.983 0.50 12.87  ? 175 PRO A N   1 
ATOM   1509 C  CA  A PRO A  1 176 ? 20.991 16.188  -12.966 0.50 10.32  ? 175 PRO A CA  1 
ATOM   1510 C  CA  B PRO A  1 176 ? 20.756 16.253  -12.953 0.50 13.33  ? 175 PRO A CA  1 
ATOM   1511 C  C   A PRO A  1 176 ? 20.206 16.119  -11.671 0.50 9.79   ? 175 PRO A C   1 
ATOM   1512 C  C   B PRO A  1 176 ? 20.114 16.041  -11.612 0.50 11.13  ? 175 PRO A C   1 
ATOM   1513 O  O   A PRO A  1 176 ? 18.952 16.173  -11.669 0.50 8.66   ? 175 PRO A O   1 
ATOM   1514 O  O   B PRO A  1 176 ? 18.876 15.868  -11.545 0.50 14.79  ? 175 PRO A O   1 
ATOM   1515 C  CB  A PRO A  1 176 ? 20.915 17.660  -13.562 0.50 10.35  ? 175 PRO A CB  1 
ATOM   1516 C  CB  B PRO A  1 176 ? 20.543 17.736  -13.486 0.50 16.02  ? 175 PRO A CB  1 
ATOM   1517 C  CG  A PRO A  1 176 ? 20.944 17.431  -15.080 0.50 12.14  ? 175 PRO A CG  1 
ATOM   1518 C  CG  B PRO A  1 176 ? 20.375 17.531  -14.980 0.50 20.55  ? 175 PRO A CG  1 
ATOM   1519 C  CD  A PRO A  1 176 ? 20.056 16.196  -15.273 0.50 11.37  ? 175 PRO A CD  1 
ATOM   1520 C  CD  B PRO A  1 176 ? 19.529 16.272  -15.118 0.50 15.39  ? 175 PRO A CD  1 
ATOM   1521 N  N   . PHE A  1 177 ? 20.908 16.126  -10.555 1.00 10.18  ? 176 PHE A N   1 
ATOM   1522 C  CA  . PHE A  1 177 ? 20.350 16.059  -9.209  1.00 9.82   ? 176 PHE A CA  1 
ATOM   1523 C  C   . PHE A  1 177 ? 21.269 16.934  -8.391  1.00 10.09  ? 176 PHE A C   1 
ATOM   1524 O  O   . PHE A  1 177 ? 22.418 16.553  -8.123  1.00 11.15  ? 176 PHE A O   1 
ATOM   1525 C  CB  . PHE A  1 177 ? 20.333 14.573  -8.727  1.00 10.02  ? 176 PHE A CB  1 
ATOM   1526 C  CG  . PHE A  1 177 ? 19.645 14.412  -7.428  1.00 9.93   ? 176 PHE A CG  1 
ATOM   1527 C  CD1 . PHE A  1 177 ? 20.297 14.631  -6.190  1.00 10.49  ? 176 PHE A CD1 1 
ATOM   1528 C  CD2 . PHE A  1 177 ? 18.294 14.001  -7.397  1.00 11.45  ? 176 PHE A CD2 1 
ATOM   1529 C  CE1 . PHE A  1 177 ? 19.611 14.452  -4.990  1.00 11.69  ? 176 PHE A CE1 1 
ATOM   1530 C  CE2 . PHE A  1 177 ? 17.633 13.769  -6.209  1.00 13.96  ? 176 PHE A CE2 1 
ATOM   1531 C  CZ  . PHE A  1 177 ? 18.307 14.036  -5.007  1.00 12.25  ? 176 PHE A CZ  1 
ATOM   1532 N  N   . THR A  1 178 ? 20.766 18.128  -8.036  1.00 11.28  ? 177 THR A N   1 
ATOM   1533 C  CA  . THR A  1 178 ? 21.688 19.176  -7.486  1.00 11.79  ? 177 THR A CA  1 
ATOM   1534 C  C   . THR A  1 178 ? 21.191 19.711  -6.182  1.00 10.85  ? 177 THR A C   1 
ATOM   1535 O  O   . THR A  1 178 ? 20.050 19.535  -5.811  1.00 12.34  ? 177 THR A O   1 
ATOM   1536 C  CB  . THR A  1 178 ? 21.868 20.287  -8.532  1.00 13.11  ? 177 THR A CB  1 
ATOM   1537 O  OG1 . THR A  1 178 ? 20.550 20.865  -8.742  1.00 16.85  ? 177 THR A OG1 1 
ATOM   1538 C  CG2 . THR A  1 178 ? 22.465 19.771  -9.835  1.00 16.94  ? 177 THR A CG2 1 
ATOM   1539 N  N   . ASN A  1 179 ? 22.106 20.416  -5.495  1.00 11.21  ? 178 ASN A N   1 
ATOM   1540 C  CA  . ASN A  1 179 ? 21.780 21.140  -4.291  1.00 12.37  ? 178 ASN A CA  1 
ATOM   1541 C  C   . ASN A  1 179 ? 21.111 20.223  -3.231  1.00 11.33  ? 178 ASN A C   1 
ATOM   1542 O  O   . ASN A  1 179 ? 19.952 20.425  -2.824  1.00 13.64  ? 178 ASN A O   1 
ATOM   1543 C  CB  . ASN A  1 179 ? 20.846 22.371  -4.552  1.00 14.14  ? 178 ASN A CB  1 
ATOM   1544 C  CG  . ASN A  1 179 ? 20.629 23.177  -3.262  1.00 17.64  ? 178 ASN A CG  1 
ATOM   1545 O  OD1 . ASN A  1 179 ? 21.490 23.261  -2.380  1.00 20.47  ? 178 ASN A OD1 1 
ATOM   1546 N  ND2 . ASN A  1 179 ? 19.458 23.829  -3.182  1.00 20.92  ? 178 ASN A ND2 1 
ATOM   1547 N  N   . PHE A  1 180 ? 21.878 19.248  -2.771  1.00 10.13  ? 179 PHE A N   1 
ATOM   1548 C  CA  . PHE A  1 180 ? 21.310 18.257  -1.791  1.00 9.96   ? 179 PHE A CA  1 
ATOM   1549 C  C   . PHE A  1 180 ? 22.412 17.793  -0.889  1.00 8.69   ? 179 PHE A C   1 
ATOM   1550 O  O   . PHE A  1 180 ? 23.450 17.312  -1.382  1.00 10.54  ? 179 PHE A O   1 
ATOM   1551 C  CB  . PHE A  1 180 ? 20.699 17.091  -2.585  1.00 10.45  ? 179 PHE A CB  1 
ATOM   1552 C  CG  . PHE A  1 180 ? 20.005 16.120  -1.674  1.00 9.83   ? 179 PHE A CG  1 
ATOM   1553 C  CD1 . PHE A  1 180 ? 18.739 16.480  -1.114  1.00 12.53  ? 179 PHE A CD1 1 
ATOM   1554 C  CD2 . PHE A  1 180 ? 20.542 14.929  -1.286  1.00 9.86   ? 179 PHE A CD2 1 
ATOM   1555 C  CE1 . PHE A  1 180 ? 18.050 15.638  -0.258  1.00 13.23  ? 179 PHE A CE1 1 
ATOM   1556 C  CE2 . PHE A  1 180 ? 19.895 14.042  -0.464  1.00 10.12  ? 179 PHE A CE2 1 
ATOM   1557 C  CZ  . PHE A  1 180 ? 18.640 14.396  0.088   1.00 10.95  ? 179 PHE A CZ  1 
ATOM   1558 N  N   . ASP A  1 181 ? 22.169 17.902  0.411   1.00 9.68   ? 180 ASP A N   1 
ATOM   1559 C  CA  . ASP A  1 181 ? 23.116 17.417  1.419   1.00 9.30   ? 180 ASP A CA  1 
ATOM   1560 C  C   . ASP A  1 181 ? 22.547 16.136  1.954   1.00 9.20   ? 180 ASP A C   1 
ATOM   1561 O  O   . ASP A  1 181 ? 21.530 16.134  2.681   1.00 10.05  ? 180 ASP A O   1 
ATOM   1562 C  CB  . ASP A  1 181 ? 23.231 18.476  2.540   1.00 10.47  ? 180 ASP A CB  1 
ATOM   1563 C  CG  . ASP A  1 181 ? 24.118 18.044  3.682   1.00 9.41   ? 180 ASP A CG  1 
ATOM   1564 O  OD1 . ASP A  1 181 ? 24.403 16.846  3.817   1.00 10.07  ? 180 ASP A OD1 1 
ATOM   1565 O  OD2 . ASP A  1 181 ? 24.539 18.920  4.478   1.00 11.92  ? 180 ASP A OD2 1 
ATOM   1566 N  N   . PRO A  1 182 ? 23.136 14.954  1.684   1.00 8.82   ? 181 PRO A N   1 
ATOM   1567 C  CA  . PRO A  1 182 ? 22.531 13.691  2.062   1.00 9.53   ? 181 PRO A CA  1 
ATOM   1568 C  C   . PRO A  1 182 ? 22.621 13.405  3.545   1.00 8.90   ? 181 PRO A C   1 
ATOM   1569 O  O   . PRO A  1 182 ? 21.999 12.442  4.022   1.00 9.14   ? 181 PRO A O   1 
ATOM   1570 C  CB  . PRO A  1 182 ? 23.233 12.671  1.210   1.00 10.55  ? 181 PRO A CB  1 
ATOM   1571 C  CG  . PRO A  1 182 ? 24.598 13.280  0.991   1.00 10.52  ? 181 PRO A CG  1 
ATOM   1572 C  CD  . PRO A  1 182 ? 24.392 14.755  0.880   1.00 8.97   ? 181 PRO A CD  1 
ATOM   1573 N  N   . SER A  1 183 ? 23.335 14.262  4.318   1.00 9.49   ? 182 SER A N   1 
ATOM   1574 C  CA  . SER A  1 183 ? 23.278 14.082  5.751   1.00 9.77   ? 182 SER A CA  1 
ATOM   1575 C  C   . SER A  1 183 ? 21.899 14.380  6.291   1.00 9.05   ? 182 SER A C   1 
ATOM   1576 O  O   . SER A  1 183 ? 21.563 13.937  7.399   1.00 10.97  ? 182 SER A O   1 
ATOM   1577 C  CB  . SER A  1 183 ? 24.337 14.848  6.503   1.00 11.97  ? 182 SER A CB  1 
ATOM   1578 O  OG  . SER A  1 183 ? 24.071 16.218  6.458   1.00 12.80  ? 182 SER A OG  1 
ATOM   1579 N  N   . THR A  1 184 ? 21.041 15.050  5.532   1.00 9.48   ? 183 THR A N   1 
ATOM   1580 C  CA  . THR A  1 184 ? 19.649 15.229  5.888   1.00 10.33  ? 183 THR A CA  1 
ATOM   1581 C  C   . THR A  1 184 ? 18.892 13.906  5.989   1.00 9.77   ? 183 THR A C   1 
ATOM   1582 O  O   . THR A  1 184 ? 17.845 13.878  6.635   1.00 12.16  ? 183 THR A O   1 
ATOM   1583 C  CB  . THR A  1 184 ? 18.959 16.144  4.896   1.00 11.45  ? 183 THR A CB  1 
ATOM   1584 O  OG1 . THR A  1 184 ? 18.893 15.529  3.583   1.00 12.69  ? 183 THR A OG1 1 
ATOM   1585 C  CG2 . THR A  1 184 ? 19.479 17.570  4.802   1.00 17.06  ? 183 THR A CG2 1 
ATOM   1586 N  N   . LEU A  1 185 ? 19.392 12.860  5.360   1.00 8.60   ? 184 LEU A N   1 
ATOM   1587 C  CA  . LEU A  1 185 ? 18.722 11.546  5.367   1.00 9.11   ? 184 LEU A CA  1 
ATOM   1588 C  C   . LEU A  1 185 ? 19.139 10.720  6.597   1.00 8.76   ? 184 LEU A C   1 
ATOM   1589 O  O   . LEU A  1 185 ? 18.499 9.709   6.868   1.00 9.69   ? 184 LEU A O   1 
ATOM   1590 C  CB  . LEU A  1 185 ? 19.108 10.761  4.127   1.00 9.39   ? 184 LEU A CB  1 
ATOM   1591 C  CG  . LEU A  1 185 ? 18.641 11.402  2.818   1.00 10.84  ? 184 LEU A CG  1 
ATOM   1592 C  CD1 . LEU A  1 185 ? 19.219 10.625  1.667   1.00 15.83  ? 184 LEU A CD1 1 
ATOM   1593 C  CD2 . LEU A  1 185 ? 17.160 11.628  2.725   1.00 14.79  ? 184 LEU A CD2 1 
ATOM   1594 N  N   . LEU A  1 186 ? 20.207 11.118  7.296   1.00 8.94   ? 185 LEU A N   1 
ATOM   1595 C  CA  . LEU A  1 186 ? 20.675 10.361  8.431   1.00 9.04   ? 185 LEU A CA  1 
ATOM   1596 C  C   . LEU A  1 186 ? 19.798 10.566  9.644   1.00 8.62   ? 185 LEU A C   1 
ATOM   1597 O  O   . LEU A  1 186 ? 19.076 11.563  9.765   1.00 9.58   ? 185 LEU A O   1 
ATOM   1598 C  CB  . LEU A  1 186 ? 22.116 10.801  8.744   1.00 10.23  ? 185 LEU A CB  1 
ATOM   1599 C  CG  . LEU A  1 186 ? 23.106 10.585  7.589   1.00 10.30  ? 185 LEU A CG  1 
ATOM   1600 C  CD1 . LEU A  1 186 ? 24.497 11.096  7.961   1.00 13.83  ? 185 LEU A CD1 1 
ATOM   1601 C  CD2 . LEU A  1 186 ? 23.216 9.091   7.156   1.00 12.45  ? 185 LEU A CD2 1 
ATOM   1602 N  N   . PRO A  1 187 ? 19.830 9.639   10.622  1.00 8.89   ? 186 PRO A N   1 
ATOM   1603 C  CA  . PRO A  1 187 ? 19.075 9.827   11.866  1.00 9.39   ? 186 PRO A CA  1 
ATOM   1604 C  C   . PRO A  1 187 ? 19.657 10.985  12.659  1.00 8.96   ? 186 PRO A C   1 
ATOM   1605 O  O   . PRO A  1 187 ? 20.772 11.448  12.408  1.00 10.29  ? 186 PRO A O   1 
ATOM   1606 C  CB  . PRO A  1 187 ? 19.205 8.478   12.548  1.00 10.61  ? 186 PRO A CB  1 
ATOM   1607 C  CG  . PRO A  1 187 ? 20.492 7.883   12.026  1.00 10.65  ? 186 PRO A CG  1 
ATOM   1608 C  CD  . PRO A  1 187 ? 20.567 8.358   10.597  1.00 9.59   ? 186 PRO A CD  1 
ATOM   1609 N  N   A SER A  1 188 ? 18.890 11.430  13.664  0.50 9.88   ? 187 SER A N   1 
ATOM   1610 N  N   B SER A  1 188 ? 18.927 11.423  13.680  0.50 9.66   ? 187 SER A N   1 
ATOM   1611 C  CA  A SER A  1 188 ? 19.316 12.563  14.502  0.50 10.81  ? 187 SER A CA  1 
ATOM   1612 C  CA  B SER A  1 188 ? 19.331 12.574  14.487  0.50 10.57  ? 187 SER A CA  1 
ATOM   1613 C  C   A SER A  1 188 ? 20.630 12.292  15.192  0.50 11.63  ? 187 SER A C   1 
ATOM   1614 C  C   B SER A  1 188 ? 20.676 12.294  15.190  0.50 12.35  ? 187 SER A C   1 
ATOM   1615 O  O   A SER A  1 188 ? 21.443 13.250  15.276  0.50 13.32  ? 187 SER A O   1 
ATOM   1616 O  O   B SER A  1 188 ? 21.582 13.193  15.222  0.50 14.80  ? 187 SER A O   1 
ATOM   1617 C  CB  A SER A  1 188 ? 18.303 12.771  15.630  0.50 13.88  ? 187 SER A CB  1 
ATOM   1618 C  CB  B SER A  1 188 ? 18.252 12.713  15.567  0.50 12.68  ? 187 SER A CB  1 
ATOM   1619 O  OG  A SER A  1 188 ? 17.154 13.279  15.111  0.50 14.15  ? 187 SER A OG  1 
ATOM   1620 O  OG  B SER A  1 188 ? 18.542 13.790  16.360  0.50 15.25  ? 187 SER A OG  1 
ATOM   1621 N  N   . SER A  1 189 ? 20.789 11.127  15.759  1.00 13.20  ? 188 SER A N   1 
ATOM   1622 C  CA  . SER A  1 189 ? 22.053 10.719  16.389  1.00 16.04  ? 188 SER A CA  1 
ATOM   1623 C  C   . SER A  1 189 ? 22.814 9.814   15.485  1.00 12.10  ? 188 SER A C   1 
ATOM   1624 O  O   . SER A  1 189 ? 22.223 8.957   14.765  1.00 12.13  ? 188 SER A O   1 
ATOM   1625 C  CB  . SER A  1 189 ? 21.683 9.858   17.624  1.00 26.46  ? 188 SER A CB  1 
ATOM   1626 O  OG  . SER A  1 189 ? 22.836 9.078   18.070  1.00 28.35  ? 188 SER A OG  1 
ATOM   1627 N  N   . LEU A  1 190 ? 24.131 9.946   15.506  1.00 11.28  ? 189 LEU A N   1 
ATOM   1628 C  CA  . LEU A  1 190 ? 25.042 9.169   14.707  1.00 10.20  ? 189 LEU A CA  1 
ATOM   1629 C  C   . LEU A  1 190 ? 25.811 8.148   15.517  1.00 10.20  ? 189 LEU A C   1 
ATOM   1630 O  O   . LEU A  1 190 ? 26.890 7.695   15.135  1.00 10.93  ? 189 LEU A O   1 
ATOM   1631 C  CB  . LEU A  1 190 ? 26.016 9.989   13.848  1.00 12.36  ? 189 LEU A CB  1 
ATOM   1632 C  CG  . LEU A  1 190 ? 25.270 11.006  12.950  1.00 14.44  ? 189 LEU A CG  1 
ATOM   1633 C  CD1 . LEU A  1 190 ? 26.284 11.852  12.162  1.00 17.58  ? 189 LEU A CD1 1 
ATOM   1634 C  CD2 . LEU A  1 190 ? 24.358 10.234  11.981  1.00 13.85  ? 189 LEU A CD2 1 
ATOM   1635 N  N   . ASP A  1 191 ? 25.259 7.651   16.634  1.00 9.85   ? 190 ASP A N   1 
ATOM   1636 C  CA  . ASP A  1 191 ? 25.809 6.501   17.316  1.00 9.55   ? 190 ASP A CA  1 
ATOM   1637 C  C   . ASP A  1 191 ? 25.915 5.349   16.315  1.00 8.18   ? 190 ASP A C   1 
ATOM   1638 O  O   . ASP A  1 191 ? 25.011 5.198   15.479  1.00 8.36   ? 190 ASP A O   1 
ATOM   1639 C  CB  . ASP A  1 191 ? 24.967 6.056   18.492  1.00 12.15  ? 190 ASP A CB  1 
ATOM   1640 C  CG  . ASP A  1 191 ? 24.847 7.069   19.556  1.00 17.47  ? 190 ASP A CG  1 
ATOM   1641 O  OD1 . ASP A  1 191 ? 25.757 7.766   19.833  1.00 18.84  ? 190 ASP A OD1 1 
ATOM   1642 O  OD2 . ASP A  1 191 ? 23.805 6.912   20.321  1.00 27.65  ? 190 ASP A OD2 1 
ATOM   1643 N  N   . PHE A  1 192 ? 26.938 4.512   16.365  1.00 8.38   ? 191 PHE A N   1 
ATOM   1644 C  CA  . PHE A  1 192 ? 27.140 3.551   15.281  1.00 7.46   ? 191 PHE A CA  1 
ATOM   1645 C  C   . PHE A  1 192 ? 27.855 2.289   15.781  1.00 7.67   ? 191 PHE A C   1 
ATOM   1646 O  O   . PHE A  1 192 ? 28.523 2.298   16.810  1.00 8.38   ? 191 PHE A O   1 
ATOM   1647 C  CB  . PHE A  1 192 ? 27.969 4.199   14.147  1.00 8.57   ? 191 PHE A CB  1 
ATOM   1648 C  CG  . PHE A  1 192 ? 29.395 4.551   14.568  1.00 8.57   ? 191 PHE A CG  1 
ATOM   1649 C  CD1 . PHE A  1 192 ? 29.660 5.770   15.125  1.00 9.44   ? 191 PHE A CD1 1 
ATOM   1650 C  CD2 . PHE A  1 192 ? 30.429 3.658   14.342  1.00 9.36   ? 191 PHE A CD2 1 
ATOM   1651 C  CE1 . PHE A  1 192 ? 30.939 6.086   15.546  1.00 9.79   ? 191 PHE A CE1 1 
ATOM   1652 C  CE2 . PHE A  1 192 ? 31.770 3.961   14.776  1.00 10.39  ? 191 PHE A CE2 1 
ATOM   1653 C  CZ  . PHE A  1 192 ? 31.974 5.199   15.354  1.00 11.58  ? 191 PHE A CZ  1 
ATOM   1654 N  N   . TRP A  1 193 ? 27.725 1.256   14.952  1.00 7.75   ? 192 TRP A N   1 
ATOM   1655 C  CA  . TRP A  1 193 ? 28.578 0.097   14.959  1.00 7.80   ? 192 TRP A CA  1 
ATOM   1656 C  C   . TRP A  1 193 ? 29.522 0.125   13.793  1.00 7.63   ? 192 TRP A C   1 
ATOM   1657 O  O   . TRP A  1 193 ? 29.174 0.700   12.727  1.00 8.84   ? 192 TRP A O   1 
ATOM   1658 C  CB  . TRP A  1 193 ? 27.742 -1.179  14.852  1.00 8.50   ? 192 TRP A CB  1 
ATOM   1659 C  CG  . TRP A  1 193 ? 26.775 -1.368  15.987  1.00 8.35   ? 192 TRP A CG  1 
ATOM   1660 C  CD1 . TRP A  1 193 ? 27.082 -1.720  17.300  1.00 9.74   ? 192 TRP A CD1 1 
ATOM   1661 C  CD2 . TRP A  1 193 ? 25.328 -1.292  15.919  1.00 8.37   ? 192 TRP A CD2 1 
ATOM   1662 N  NE1 . TRP A  1 193 ? 25.936 -1.832  18.000  1.00 10.89  ? 192 TRP A NE1 1 
ATOM   1663 C  CE2 . TRP A  1 193 ? 24.828 -1.567  17.226  1.00 9.49   ? 192 TRP A CE2 1 
ATOM   1664 C  CE3 . TRP A  1 193 ? 24.435 -0.982  14.902  1.00 9.44   ? 192 TRP A CE3 1 
ATOM   1665 C  CZ2 . TRP A  1 193 ? 23.462 -1.588  17.478  1.00 10.67  ? 192 TRP A CZ2 1 
ATOM   1666 C  CZ3 . TRP A  1 193 ? 23.112 -0.963  15.176  1.00 10.28  ? 192 TRP A CZ3 1 
ATOM   1667 C  CH2 . TRP A  1 193 ? 22.573 -1.270  16.443  1.00 10.57  ? 192 TRP A CH2 1 
ATOM   1668 N  N   . THR A  1 194 ? 30.683 -0.480  13.881  1.00 7.70   ? 193 THR A N   1 
ATOM   1669 C  CA  . THR A  1 194 ? 31.580 -0.548  12.724  1.00 8.00   ? 193 THR A CA  1 
ATOM   1670 C  C   . THR A  1 194 ? 32.234 -1.918  12.657  1.00 7.73   ? 193 THR A C   1 
ATOM   1671 O  O   . THR A  1 194 ? 32.560 -2.533  13.684  1.00 8.32   ? 193 THR A O   1 
ATOM   1672 C  CB  . THR A  1 194 ? 32.627 0.572   12.766  1.00 8.02   ? 193 THR A CB  1 
ATOM   1673 O  OG1 . THR A  1 194 ? 33.457 0.518   11.595  1.00 8.35   ? 193 THR A OG1 1 
ATOM   1674 C  CG2 . THR A  1 194 ? 33.534 0.543   13.966  1.00 9.53   ? 193 THR A CG2 1 
ATOM   1675 N  N   . TYR A  1 195 ? 32.459 -2.375  11.421  1.00 8.06   ? 194 TYR A N   1 
ATOM   1676 C  CA  . TYR A  1 195 ? 33.176 -3.626  11.217  1.00 8.51   ? 194 TYR A CA  1 
ATOM   1677 C  C   . TYR A  1 195 ? 33.820 -3.546  9.832   1.00 8.09   ? 194 TYR A C   1 
ATOM   1678 O  O   . TYR A  1 195 ? 33.347 -2.795  8.959   1.00 8.27   ? 194 TYR A O   1 
ATOM   1679 C  CB  . TYR A  1 195 ? 32.227 -4.836  11.391  1.00 8.57   ? 194 TYR A CB  1 
ATOM   1680 C  CG  . TYR A  1 195 ? 31.291 -5.012  10.259  1.00 8.21   ? 194 TYR A CG  1 
ATOM   1681 C  CD1 . TYR A  1 195 ? 30.106 -4.310  10.148  1.00 8.44   ? 194 TYR A CD1 1 
ATOM   1682 C  CD2 . TYR A  1 195 ? 31.609 -5.929  9.199   1.00 9.15   ? 194 TYR A CD2 1 
ATOM   1683 C  CE1 . TYR A  1 195 ? 29.277 -4.432  9.027   1.00 8.59   ? 194 TYR A CE1 1 
ATOM   1684 C  CE2 . TYR A  1 195 ? 30.776 -6.075  8.114   1.00 8.19   ? 194 TYR A CE2 1 
ATOM   1685 C  CZ  . TYR A  1 195 ? 29.650 -5.317  8.013   1.00 7.67   ? 194 TYR A CZ  1 
ATOM   1686 O  OH  . TYR A  1 195 ? 28.871 -5.472  6.878   1.00 8.62   ? 194 TYR A OH  1 
ATOM   1687 N  N   . PRO A  1 196 ? 34.858 -4.370  9.603   1.00 7.95   ? 195 PRO A N   1 
ATOM   1688 C  CA  . PRO A  1 196 ? 35.507 -4.420  8.282   1.00 8.50   ? 195 PRO A CA  1 
ATOM   1689 C  C   . PRO A  1 196 ? 34.747 -5.379  7.369   1.00 8.14   ? 195 PRO A C   1 
ATOM   1690 O  O   . PRO A  1 196 ? 34.496 -6.537  7.737   1.00 9.17   ? 195 PRO A O   1 
ATOM   1691 C  CB  . PRO A  1 196 ? 36.916 -4.948  8.593   1.00 10.02  ? 195 PRO A CB  1 
ATOM   1692 C  CG  . PRO A  1 196 ? 36.718 -5.821  9.835   1.00 9.81   ? 195 PRO A CG  1 
ATOM   1693 C  CD  . PRO A  1 196 ? 35.607 -5.124  10.645  1.00 9.39   ? 195 PRO A CD  1 
ATOM   1694 N  N   . GLY A  1 197 ? 34.337 -4.895  6.195   1.00 7.96   ? 196 GLY A N   1 
ATOM   1695 C  CA  . GLY A  1 197 ? 33.586 -5.741  5.322   1.00 7.82   ? 196 GLY A CA  1 
ATOM   1696 C  C   . GLY A  1 197 ? 33.828 -5.434  3.851   1.00 8.07   ? 196 GLY A C   1 
ATOM   1697 O  O   . GLY A  1 197 ? 34.956 -5.107  3.419   1.00 8.77   ? 196 GLY A O   1 
ATOM   1698 N  N   . SER A  1 198 ? 32.757 -5.539  3.061   1.00 8.37   ? 197 SER A N   1 
ATOM   1699 C  CA  . SER A  1 198 ? 32.886 -5.575  1.629   1.00 8.20   ? 197 SER A CA  1 
ATOM   1700 C  C   . SER A  1 198 ? 31.809 -4.769  0.947   1.00 7.43   ? 197 SER A C   1 
ATOM   1701 O  O   . SER A  1 198 ? 30.789 -4.401  1.578   1.00 8.11   ? 197 SER A O   1 
ATOM   1702 C  CB  . SER A  1 198 ? 32.819 -7.003  1.105   1.00 9.21   ? 197 SER A CB  1 
ATOM   1703 O  OG  . SER A  1 198 ? 31.480 -7.530  1.141   1.00 8.84   ? 197 SER A OG  1 
ATOM   1704 N  N   A LEU A  1 199 ? 31.990 -4.451  -0.334  0.50 6.27   ? 198 LEU A N   1 
ATOM   1705 N  N   B LEU A  1 199 ? 31.912 -4.760  -0.364  0.50 8.56   ? 198 LEU A N   1 
ATOM   1706 C  CA  A LEU A  1 199 ? 30.816 -4.064  -1.136  0.50 7.86   ? 198 LEU A CA  1 
ATOM   1707 C  CA  B LEU A  1 199 ? 30.815 -4.366  -1.209  0.50 7.73   ? 198 LEU A CA  1 
ATOM   1708 C  C   A LEU A  1 199 ? 29.797 -5.230  -1.040  0.50 7.03   ? 198 LEU A C   1 
ATOM   1709 C  C   B LEU A  1 199 ? 29.732 -5.403  -1.133  0.50 8.90   ? 198 LEU A C   1 
ATOM   1710 O  O   A LEU A  1 199 ? 30.202 -6.417  -0.915  0.50 7.71   ? 198 LEU A O   1 
ATOM   1711 O  O   B LEU A  1 199 ? 29.994 -6.633  -1.081  0.50 9.70   ? 198 LEU A O   1 
ATOM   1712 C  CB  A LEU A  1 199 ? 31.282 -3.949  -2.641  0.50 8.93   ? 198 LEU A CB  1 
ATOM   1713 C  CB  B LEU A  1 199 ? 31.293 -4.307  -2.699  0.50 11.18  ? 198 LEU A CB  1 
ATOM   1714 C  CG  A LEU A  1 199 ? 32.414 -2.920  -2.904  0.50 11.64  ? 198 LEU A CG  1 
ATOM   1715 C  CG  B LEU A  1 199 ? 31.528 -2.879  -3.259  0.50 13.97  ? 198 LEU A CG  1 
ATOM   1716 C  CD1 A LEU A  1 199 ? 32.915 -3.049  -4.368  0.50 13.28  ? 198 LEU A CD1 1 
ATOM   1717 C  CD1 B LEU A  1 199 ? 32.803 -2.498  -2.634  0.50 13.94  ? 198 LEU A CD1 1 
ATOM   1718 C  CD2 A LEU A  1 199 ? 31.868 -1.540  -2.551  0.50 9.91   ? 198 LEU A CD2 1 
ATOM   1719 C  CD2 B LEU A  1 199 ? 31.726 -2.995  -4.760  0.50 14.16  ? 198 LEU A CD2 1 
ATOM   1720 N  N   . THR A  1 200 ? 28.487 -4.942  -1.132  1.00 8.30   ? 199 THR A N   1 
ATOM   1721 C  CA  . THR A  1 200 ? 27.443 -5.941  -0.955  1.00 8.58   ? 199 THR A CA  1 
ATOM   1722 C  C   . THR A  1 200 ? 26.935 -6.526  -2.272  1.00 9.06   ? 199 THR A C   1 
ATOM   1723 O  O   . THR A  1 200 ? 26.012 -7.331  -2.269  1.00 9.12   ? 199 THR A O   1 
ATOM   1724 C  CB  . THR A  1 200 ? 26.244 -5.419  -0.126  1.00 8.43   ? 199 THR A CB  1 
ATOM   1725 O  OG1 . THR A  1 200 ? 25.667 -4.354  -0.887  1.00 8.30   ? 199 THR A OG1 1 
ATOM   1726 C  CG2 . THR A  1 200 ? 26.691 -4.925  1.245   1.00 9.05   ? 199 THR A CG2 1 
ATOM   1727 N  N   . HIS A  1 201 ? 27.549 -6.155  -3.402  1.00 9.07   ? 200 HIS A N   1 
ATOM   1728 C  CA  . HIS A  1 201 ? 27.267 -6.834  -4.666  1.00 9.34   ? 200 HIS A CA  1 
ATOM   1729 C  C   . HIS A  1 201 ? 28.564 -6.857  -5.425  1.00 8.77   ? 200 HIS A C   1 
ATOM   1730 O  O   . HIS A  1 201 ? 29.524 -6.191  -5.076  1.00 9.88   ? 200 HIS A O   1 
ATOM   1731 C  CB  . HIS A  1 201 ? 26.070 -6.218  -5.405  1.00 10.45  ? 200 HIS A CB  1 
ATOM   1732 C  CG  . HIS A  1 201 ? 26.232 -4.787  -5.738  1.00 11.72  ? 200 HIS A CG  1 
ATOM   1733 N  ND1 . HIS A  1 201 ? 27.168 -4.328  -6.666  1.00 12.11  ? 200 HIS A ND1 1 
ATOM   1734 C  CD2 . HIS A  1 201 ? 25.424 -3.718  -5.462  1.00 13.80  ? 200 HIS A CD2 1 
ATOM   1735 C  CE1 . HIS A  1 201 ? 26.899 -2.967  -6.875  1.00 14.20  ? 200 HIS A CE1 1 
ATOM   1736 N  NE2 . HIS A  1 201 ? 25.890 -2.588  -6.078  1.00 16.98  ? 200 HIS A NE2 1 
ATOM   1737 N  N   . PRO A  1 202 ? 28.608 -7.602  -6.543  1.00 10.59  ? 201 PRO A N   1 
ATOM   1738 C  CA  . PRO A  1 202 ? 29.809 -7.691  -7.360  1.00 11.62  ? 201 PRO A CA  1 
ATOM   1739 C  C   . PRO A  1 202 ? 30.304 -6.278  -7.733  1.00 11.72  ? 201 PRO A C   1 
ATOM   1740 O  O   . PRO A  1 202 ? 29.480 -5.396  -8.018  1.00 11.79  ? 201 PRO A O   1 
ATOM   1741 C  CB  . PRO A  1 202 ? 29.373 -8.550  -8.584  1.00 12.64  ? 201 PRO A CB  1 
ATOM   1742 C  CG  . PRO A  1 202 ? 28.401 -9.499  -7.941  1.00 12.83  ? 201 PRO A CG  1 
ATOM   1743 C  CD  . PRO A  1 202 ? 27.587 -8.584  -7.007  1.00 11.99  ? 201 PRO A CD  1 
ATOM   1744 N  N   . PRO A  1 203 ? 31.625 -6.040  -7.607  1.00 11.91  ? 202 PRO A N   1 
ATOM   1745 C  CA  . PRO A  1 203 ? 32.718 -7.046  -7.488  1.00 12.85  ? 202 PRO A CA  1 
ATOM   1746 C  C   . PRO A  1 203 ? 33.030 -7.513  -6.058  1.00 11.40  ? 202 PRO A C   1 
ATOM   1747 O  O   . PRO A  1 203 ? 33.949 -8.317  -5.905  1.00 12.68  ? 202 PRO A O   1 
ATOM   1748 C  CB  . PRO A  1 203 ? 33.947 -6.358  -8.092  1.00 15.45  ? 202 PRO A CB  1 
ATOM   1749 C  CG  . PRO A  1 203 ? 33.700 -4.949  -7.820  1.00 16.56  ? 202 PRO A CG  1 
ATOM   1750 C  CD  . PRO A  1 203 ? 32.190 -4.759  -7.969  1.00 13.56  ? 202 PRO A CD  1 
ATOM   1751 N  N   . LEU A  1 204 ? 32.270 -7.071  -5.032  1.00 10.59  ? 203 LEU A N   1 
ATOM   1752 C  CA  . LEU A  1 204 ? 32.384 -7.721  -3.698  1.00 9.74   ? 203 LEU A CA  1 
ATOM   1753 C  C   . LEU A  1 204 ? 33.759 -7.510  -3.043  1.00 9.40   ? 203 LEU A C   1 
ATOM   1754 O  O   . LEU A  1 204 ? 34.065 -8.205  -2.080  1.00 10.53  ? 203 LEU A O   1 
ATOM   1755 C  CB  . LEU A  1 204 ? 32.044 -9.224  -3.701  1.00 10.59  ? 203 LEU A CB  1 
ATOM   1756 C  CG  . LEU A  1 204 ? 30.596 -9.531  -4.110  1.00 9.53   ? 203 LEU A CG  1 
ATOM   1757 C  CD1 . LEU A  1 204 ? 30.453 -11.050 -4.393  1.00 13.49  ? 203 LEU A CD1 1 
ATOM   1758 C  CD2 . LEU A  1 204 ? 29.584 -9.142  -3.084  1.00 10.57  ? 203 LEU A CD2 1 
ATOM   1759 N  N   . TYR A  1 205 ? 34.480 -6.475  -3.418  1.00 10.12  ? 204 TYR A N   1 
ATOM   1760 C  CA  . TYR A  1 205 ? 35.798 -6.232  -2.844  1.00 10.49  ? 204 TYR A CA  1 
ATOM   1761 C  C   . TYR A  1 205 ? 35.679 -6.022  -1.342  1.00 9.55   ? 204 TYR A C   1 
ATOM   1762 O  O   . TYR A  1 205 ? 34.756 -5.337  -0.837  1.00 9.39   ? 204 TYR A O   1 
ATOM   1763 C  CB  . TYR A  1 205 ? 36.402 -4.901  -3.389  1.00 11.39  ? 204 TYR A CB  1 
ATOM   1764 C  CG  . TYR A  1 205 ? 36.738 -4.940  -4.867  1.00 12.16  ? 204 TYR A CG  1 
ATOM   1765 C  CD1 . TYR A  1 205 ? 37.453 -5.984  -5.399  1.00 17.54  ? 204 TYR A CD1 1 
ATOM   1766 C  CD2 . TYR A  1 205 ? 36.519 -3.809  -5.614  1.00 12.98  ? 204 TYR A CD2 1 
ATOM   1767 C  CE1 . TYR A  1 205 ? 37.852 -5.928  -6.768  1.00 19.78  ? 204 TYR A CE1 1 
ATOM   1768 C  CE2 . TYR A  1 205 ? 36.919 -3.779  -7.008  1.00 14.88  ? 204 TYR A CE2 1 
ATOM   1769 C  CZ  . TYR A  1 205 ? 37.495 -4.854  -7.516  1.00 18.09  ? 204 TYR A CZ  1 
ATOM   1770 O  OH  . TYR A  1 205 ? 37.981 -4.881  -8.828  1.00 23.05  ? 204 TYR A OH  1 
ATOM   1771 N  N   . GLU A  1 206 ? 36.662 -6.571  -0.614  1.00 9.93   ? 205 GLU A N   1 
ATOM   1772 C  CA  . GLU A  1 206 ? 36.708 -6.437  0.820   1.00 9.38   ? 205 GLU A CA  1 
ATOM   1773 C  C   . GLU A  1 206 ? 37.426 -5.165  1.218   1.00 9.71   ? 205 GLU A C   1 
ATOM   1774 O  O   . GLU A  1 206 ? 38.493 -5.163  1.824   1.00 11.24  ? 205 GLU A O   1 
ATOM   1775 C  CB  . GLU A  1 206 ? 37.338 -7.709  1.435   1.00 10.80  ? 205 GLU A CB  1 
ATOM   1776 C  CG  . GLU A  1 206 ? 36.414 -8.887  1.139   1.00 11.19  ? 205 GLU A CG  1 
ATOM   1777 C  CD  . GLU A  1 206 ? 36.820 -10.239 1.756   1.00 11.48  ? 205 GLU A CD  1 
ATOM   1778 O  OE1 . GLU A  1 206 ? 35.905 -11.059 1.960   1.00 10.92  ? 205 GLU A OE1 1 
ATOM   1779 O  OE2 . GLU A  1 206 ? 38.003 -10.413 2.020   1.00 14.35  ? 205 GLU A OE2 1 
ATOM   1780 N  N   . SER A  1 207 ? 36.837 -4.032  0.865   1.00 8.81   ? 206 SER A N   1 
ATOM   1781 C  CA  . SER A  1 207 ? 37.471 -2.727  0.933   1.00 9.34   ? 206 SER A CA  1 
ATOM   1782 C  C   . SER A  1 207 ? 36.689 -1.733  1.760   1.00 8.41   ? 206 SER A C   1 
ATOM   1783 O  O   . SER A  1 207 ? 37.028 -0.561  1.770   1.00 9.68   ? 206 SER A O   1 
ATOM   1784 C  CB  . SER A  1 207 ? 37.605 -2.161  -0.451  1.00 10.02  ? 206 SER A CB  1 
ATOM   1785 O  OG  . SER A  1 207 ? 36.329 -2.200  -1.069  1.00 10.96  ? 206 SER A OG  1 
ATOM   1786 N  N   . VAL A  1 208 ? 35.663 -2.190  2.453   1.00 8.34   ? 207 VAL A N   1 
ATOM   1787 C  CA  . VAL A  1 208 ? 34.700 -1.235  3.071   1.00 8.23   ? 207 VAL A CA  1 
ATOM   1788 C  C   . VAL A  1 208 ? 34.816 -1.273  4.575   1.00 7.91   ? 207 VAL A C   1 
ATOM   1789 O  O   . VAL A  1 208 ? 34.609 -2.309  5.209   1.00 9.99   ? 207 VAL A O   1 
ATOM   1790 C  CB  . VAL A  1 208 ? 33.270 -1.551  2.638   1.00 8.41   ? 207 VAL A CB  1 
ATOM   1791 C  CG1 . VAL A  1 208 ? 32.302 -0.560  3.343   1.00 8.92   ? 207 VAL A CG1 1 
ATOM   1792 C  CG2 . VAL A  1 208 ? 33.078 -1.551  1.133   1.00 9.31   ? 207 VAL A CG2 1 
ATOM   1793 N  N   . THR A  1 209 ? 35.000 -0.098  5.187   1.00 7.86   ? 208 THR A N   1 
ATOM   1794 C  CA  . THR A  1 209 ? 34.728 0.090   6.629   1.00 7.66   ? 208 THR A CA  1 
ATOM   1795 C  C   . THR A  1 209 ? 33.294 0.473   6.739   1.00 7.15   ? 208 THR A C   1 
ATOM   1796 O  O   . THR A  1 209 ? 32.902 1.567   6.275   1.00 8.56   ? 208 THR A O   1 
ATOM   1797 C  CB  . THR A  1 209 ? 35.645 1.140   7.209   1.00 8.83   ? 208 THR A CB  1 
ATOM   1798 O  OG1 . THR A  1 209 ? 37.021 0.777   7.004   1.00 9.54   ? 208 THR A OG1 1 
ATOM   1799 C  CG2 . THR A  1 209 ? 35.376 1.282   8.684   1.00 10.29  ? 208 THR A CG2 1 
ATOM   1800 N  N   . TRP A  1 210 ? 32.466 -0.394  7.323   1.00 7.06   ? 209 TRP A N   1 
ATOM   1801 C  CA  . TRP A  1 210 ? 31.036 -0.126  7.489   1.00 6.77   ? 209 TRP A CA  1 
ATOM   1802 C  C   . TRP A  1 210 ? 30.797 0.657   8.753   1.00 6.60   ? 209 TRP A C   1 
ATOM   1803 O  O   . TRP A  1 210 ? 31.357 0.331   9.801   1.00 8.06   ? 209 TRP A O   1 
ATOM   1804 C  CB  . TRP A  1 210 ? 30.258 -1.442  7.533   1.00 7.61   ? 209 TRP A CB  1 
ATOM   1805 C  CG  . TRP A  1 210 ? 30.068 -1.994  6.156   1.00 6.87   ? 209 TRP A CG  1 
ATOM   1806 C  CD1 . TRP A  1 210 ? 30.801 -2.924  5.474   1.00 8.12   ? 209 TRP A CD1 1 
ATOM   1807 C  CD2 . TRP A  1 210 ? 29.063 -1.523  5.232   1.00 7.05   ? 209 TRP A CD2 1 
ATOM   1808 N  NE1 . TRP A  1 210 ? 30.325 -3.049  4.177   1.00 7.99   ? 209 TRP A NE1 1 
ATOM   1809 C  CE2 . TRP A  1 210 ? 29.247 -2.219  4.024   1.00 7.87   ? 209 TRP A CE2 1 
ATOM   1810 C  CE3 . TRP A  1 210 ? 28.012 -0.602  5.349   1.00 7.49   ? 209 TRP A CE3 1 
ATOM   1811 C  CZ2 . TRP A  1 210 ? 28.432 -1.998  2.892   1.00 8.74   ? 209 TRP A CZ2 1 
ATOM   1812 C  CZ3 . TRP A  1 210 ? 27.181 -0.411  4.224   1.00 8.59   ? 209 TRP A CZ3 1 
ATOM   1813 C  CH2 . TRP A  1 210 ? 27.380 -1.084  3.034   1.00 8.95   ? 209 TRP A CH2 1 
ATOM   1814 N  N   . ILE A  1 211 ? 29.925 1.655   8.629   1.00 6.76   ? 210 ILE A N   1 
ATOM   1815 C  CA  . ILE A  1 211 ? 29.461 2.452   9.782   1.00 7.75   ? 210 ILE A CA  1 
ATOM   1816 C  C   . ILE A  1 211 ? 27.944 2.263   9.791   1.00 7.15   ? 210 ILE A C   1 
ATOM   1817 O  O   . ILE A  1 211 ? 27.259 2.834   8.929   1.00 8.24   ? 210 ILE A O   1 
ATOM   1818 C  CB  . ILE A  1 211 ? 29.800 3.947   9.580   1.00 7.82   ? 210 ILE A CB  1 
ATOM   1819 C  CG1 . ILE A  1 211 ? 31.318 4.176   9.348   1.00 9.24   ? 210 ILE A CG1 1 
ATOM   1820 C  CG2 . ILE A  1 211 ? 29.237 4.795   10.702  1.00 9.09   ? 210 ILE A CG2 1 
ATOM   1821 C  CD1 . ILE A  1 211 ? 32.173 3.837   10.525  1.00 10.36  ? 210 ILE A CD1 1 
ATOM   1822 N  N   . ILE A  1 212 ? 27.399 1.448   10.685  1.00 6.98   ? 211 ILE A N   1 
ATOM   1823 C  CA  . ILE A  1 212 ? 25.977 1.180   10.717  1.00 6.99   ? 211 ILE A CA  1 
ATOM   1824 C  C   . ILE A  1 212 ? 25.363 1.983   11.814  1.00 7.13   ? 211 ILE A C   1 
ATOM   1825 O  O   . ILE A  1 212 ? 25.739 1.846   12.994  1.00 7.75   ? 211 ILE A O   1 
ATOM   1826 C  CB  . ILE A  1 212 ? 25.717 -0.356  10.961  1.00 8.25   ? 211 ILE A CB  1 
ATOM   1827 C  CG1 . ILE A  1 212 ? 26.420 -1.214  9.879   1.00 8.84   ? 211 ILE A CG1 1 
ATOM   1828 C  CG2 . ILE A  1 212 ? 24.201 -0.569  10.958  1.00 8.86   ? 211 ILE A CG2 1 
ATOM   1829 C  CD1 . ILE A  1 212 ? 26.107 -0.906  8.443   1.00 9.44   ? 211 ILE A CD1 1 
ATOM   1830 N  N   . CYS A  1 213 ? 24.442 2.868   11.493  1.00 7.31   ? 212 CYS A N   1 
ATOM   1831 C  CA  . CYS A  1 213 ? 23.803 3.669   12.526  1.00 7.28   ? 212 CYS A CA  1 
ATOM   1832 C  C   . CYS A  1 213 ? 22.980 2.831   13.443  1.00 7.50   ? 212 CYS A C   1 
ATOM   1833 O  O   . CYS A  1 213 ? 22.208 1.951   13.042  1.00 8.25   ? 212 CYS A O   1 
ATOM   1834 C  CB  . CYS A  1 213 ? 22.955 4.762   11.876  1.00 8.31   ? 212 CYS A CB  1 
ATOM   1835 S  SG  . CYS A  1 213 ? 23.931 6.042   11.050  1.00 9.51   ? 212 CYS A SG  1 
ATOM   1836 N  N   . LYS A  1 214 ? 23.025 3.158   14.742  1.00 7.70   ? 213 LYS A N   1 
ATOM   1837 C  CA  . LYS A  1 214 ? 22.150 2.489   15.699  1.00 9.11   ? 213 LYS A CA  1 
ATOM   1838 C  C   . LYS A  1 214 ? 20.701 2.893   15.576  1.00 8.62   ? 213 LYS A C   1 
ATOM   1839 O  O   . LYS A  1 214 ? 19.834 2.083   15.912  1.00 12.52  ? 213 LYS A O   1 
ATOM   1840 C  CB  . LYS A  1 214 ? 22.657 2.789   17.134  1.00 11.97  ? 213 LYS A CB  1 
ATOM   1841 C  CG  . LYS A  1 214 ? 21.697 2.677   18.243  1.00 26.28  ? 213 LYS A CG  1 
ATOM   1842 C  CD  . LYS A  1 214 ? 22.200 3.450   19.513  1.00 26.37  ? 213 LYS A CD  1 
ATOM   1843 C  CE  . LYS A  1 214 ? 21.695 4.980   19.631  1.00 24.31  ? 213 LYS A CE  1 
ATOM   1844 N  N   A GLU A  1 215 ? 20.441 4.149   15.181  0.50 8.46   ? 214 GLU A N   1 
ATOM   1845 N  N   B GLU A  1 215 ? 20.436 4.114   15.154  0.50 8.72   ? 214 GLU A N   1 
ATOM   1846 C  CA  A GLU A  1 215 ? 19.079 4.680   14.991  0.50 8.61   ? 214 GLU A CA  1 
ATOM   1847 C  CA  B GLU A  1 215 ? 19.047 4.481   15.022  0.50 8.51   ? 214 GLU A CA  1 
ATOM   1848 C  C   A GLU A  1 215 ? 18.586 4.455   13.555  0.50 9.15   ? 214 GLU A C   1 
ATOM   1849 C  C   B GLU A  1 215 ? 18.602 4.291   13.572  0.50 7.65   ? 214 GLU A C   1 
ATOM   1850 O  O   A GLU A  1 215 ? 19.360 4.684   12.590  0.50 10.40  ? 214 GLU A O   1 
ATOM   1851 O  O   B GLU A  1 215 ? 19.407 4.535   12.655  0.50 8.37   ? 214 GLU A O   1 
ATOM   1852 C  CB  A GLU A  1 215 ? 19.002 6.218   15.228  0.50 9.61   ? 214 GLU A CB  1 
ATOM   1853 C  CB  B GLU A  1 215 ? 18.854 5.921   15.504  0.50 8.89   ? 214 GLU A CB  1 
ATOM   1854 C  CG  A GLU A  1 215 ? 19.501 6.799   16.555  0.50 18.60  ? 214 GLU A CG  1 
ATOM   1855 C  CG  B GLU A  1 215 ? 19.507 6.191   16.859  0.50 12.49  ? 214 GLU A CG  1 
ATOM   1856 C  CD  A GLU A  1 215 ? 18.828 8.126   16.975  0.50 18.93  ? 214 GLU A CD  1 
ATOM   1857 C  CD  B GLU A  1 215 ? 18.679 5.648   18.010  0.50 18.84  ? 214 GLU A CD  1 
ATOM   1858 O  OE1 A GLU A  1 215 ? 18.593 9.055   16.102  0.50 11.64  ? 214 GLU A OE1 1 
ATOM   1859 O  OE1 B GLU A  1 215 ? 17.482 5.440   17.787  0.50 22.78  ? 214 GLU A OE1 1 
ATOM   1860 O  OE2 A GLU A  1 215 ? 18.559 8.229   18.220  0.50 24.85  ? 214 GLU A OE2 1 
ATOM   1861 O  OE2 B GLU A  1 215 ? 19.200 5.424   19.126  0.50 25.30  ? 214 GLU A OE2 1 
ATOM   1862 N  N   . SER A  1 216 ? 17.347 3.981   13.401  1.00 8.85   ? 215 SER A N   1 
ATOM   1863 C  CA  . SER A  1 216 ? 16.746 3.851   12.078  1.00 8.57   ? 215 SER A CA  1 
ATOM   1864 C  C   . SER A  1 216 ? 16.125 5.133   11.637  1.00 8.11   ? 215 SER A C   1 
ATOM   1865 O  O   . SER A  1 216 ? 16.029 6.083   12.404  1.00 10.03  ? 215 SER A O   1 
ATOM   1866 C  CB  . SER A  1 216 ? 15.667 2.746   12.128  1.00 10.67  ? 215 SER A CB  1 
ATOM   1867 O  OG  . SER A  1 216 ? 14.638 3.085   13.004  1.00 13.16  ? 215 SER A OG  1 
ATOM   1868 N  N   . ILE A  1 217 ? 15.717 5.174   10.364  1.00 8.07   ? 216 ILE A N   1 
ATOM   1869 C  CA  . ILE A  1 217 ? 14.809 6.241   9.856   1.00 8.30   ? 216 ILE A CA  1 
ATOM   1870 C  C   . ILE A  1 217 ? 13.598 5.573   9.327   1.00 7.70   ? 216 ILE A C   1 
ATOM   1871 O  O   . ILE A  1 217 ? 13.567 4.363   9.104   1.00 8.91   ? 216 ILE A O   1 
ATOM   1872 C  CB  . ILE A  1 217 ? 15.557 7.091   8.753   1.00 8.20   ? 216 ILE A CB  1 
ATOM   1873 C  CG1 . ILE A  1 217 ? 15.911 6.217   7.553   1.00 8.64   ? 216 ILE A CG1 1 
ATOM   1874 C  CG2 . ILE A  1 217 ? 16.741 7.807   9.373   1.00 9.05   ? 216 ILE A CG2 1 
ATOM   1875 C  CD1 . ILE A  1 217 ? 16.515 6.945   6.380   1.00 9.57   ? 216 ILE A CD1 1 
ATOM   1876 N  N   A SER A  1 218 ? 12.503 6.304   9.135   0.50 7.96   ? 217 SER A N   1 
ATOM   1877 N  N   B SER A  1 218 ? 12.595 6.411   9.038   0.50 8.33   ? 217 SER A N   1 
ATOM   1878 C  CA  A SER A  1 218 ? 11.257 5.691   8.635   0.50 8.80   ? 217 SER A CA  1 
ATOM   1879 C  CA  B SER A  1 218 ? 11.307 5.891   8.593   0.50 7.51   ? 217 SER A CA  1 
ATOM   1880 C  C   A SER A  1 218 ? 11.223 5.749   7.114   0.50 7.59   ? 217 SER A C   1 
ATOM   1881 C  C   B SER A  1 218 ? 11.257 5.766   7.055   0.50 8.13   ? 217 SER A C   1 
ATOM   1882 O  O   A SER A  1 218 ? 11.946 6.533   6.428   0.50 7.70   ? 217 SER A O   1 
ATOM   1883 O  O   B SER A  1 218 ? 12.079 6.361   6.297   0.50 8.22   ? 217 SER A O   1 
ATOM   1884 C  CB  A SER A  1 218 ? 10.034 6.486   9.122   0.50 10.13  ? 217 SER A CB  1 
ATOM   1885 C  CB  B SER A  1 218 ? 10.134 6.696   9.204   0.50 9.25   ? 217 SER A CB  1 
ATOM   1886 O  OG  A SER A  1 218 ? 9.933  7.738   8.408   0.50 12.67  ? 217 SER A OG  1 
ATOM   1887 O  OG  B SER A  1 218 ? 8.926  5.966   9.139   0.50 9.22   ? 217 SER A OG  1 
ATOM   1888 N  N   . VAL A  1 219 ? 10.260 5.015   6.582   1.00 7.77   ? 218 VAL A N   1 
ATOM   1889 C  CA  . VAL A  1 219 ? 9.902  4.994   5.176   1.00 7.42   ? 218 VAL A CA  1 
ATOM   1890 C  C   . VAL A  1 219 ? 8.491  4.440   5.129   1.00 7.58   ? 218 VAL A C   1 
ATOM   1891 O  O   . VAL A  1 219 ? 8.164  3.563   5.906   1.00 8.73   ? 218 VAL A O   1 
ATOM   1892 C  CB  . VAL A  1 219 ? 10.891 4.137   4.323   1.00 7.74   ? 218 VAL A CB  1 
ATOM   1893 C  CG1 . VAL A  1 219 ? 10.930 2.663   4.750   1.00 8.54   ? 218 VAL A CG1 1 
ATOM   1894 C  CG2 . VAL A  1 219 ? 10.617 4.286   2.841   1.00 8.52   ? 218 VAL A CG2 1 
ATOM   1895 N  N   . SER A  1 220 ? 7.632  4.904   4.199   1.00 7.96   ? 219 SER A N   1 
ATOM   1896 C  CA  . SER A  1 220 ? 6.302  4.320   4.127   1.00 8.11   ? 219 SER A CA  1 
ATOM   1897 C  C   . SER A  1 220 ? 6.252  3.173   3.122   1.00 7.67   ? 219 SER A C   1 
ATOM   1898 O  O   . SER A  1 220 ? 7.100  3.048   2.204   1.00 8.33   ? 219 SER A O   1 
ATOM   1899 C  CB  . SER A  1 220 ? 5.218  5.300   3.757   1.00 8.83   ? 219 SER A CB  1 
ATOM   1900 O  OG  . SER A  1 220 ? 5.382  5.707   2.433   1.00 9.06   ? 219 SER A OG  1 
ATOM   1901 N  N   A SER A  1 221 ? 5.186  2.380   3.225   0.50 8.67   ? 220 SER A N   1 
ATOM   1902 N  N   B SER A  1 221 ? 5.230  2.340   3.234   0.50 8.66   ? 220 SER A N   1 
ATOM   1903 C  CA  A SER A  1 221 ? 4.968  1.278   2.271   0.50 8.78   ? 220 SER A CA  1 
ATOM   1904 C  CA  B SER A  1 221 ? 4.991  1.285   2.235   0.50 9.37   ? 220 SER A CA  1 
ATOM   1905 C  C   A SER A  1 221 ? 4.862  1.804   0.836   0.50 8.04   ? 220 SER A C   1 
ATOM   1906 C  C   B SER A  1 221 ? 4.949  1.838   0.826   0.50 7.85   ? 220 SER A C   1 
ATOM   1907 O  O   A SER A  1 221 ? 5.315  1.158   -0.095  0.50 8.45   ? 220 SER A O   1 
ATOM   1908 O  O   B SER A  1 221 ? 5.454  1.194   -0.102  0.50 8.82   ? 220 SER A O   1 
ATOM   1909 C  CB  A SER A  1 221 ? 3.715  0.487   2.697   0.50 8.91   ? 220 SER A CB  1 
ATOM   1910 C  CB  B SER A  1 221 ? 3.611  0.738   2.559   0.50 11.74  ? 220 SER A CB  1 
ATOM   1911 O  OG  A SER A  1 221 ? 3.634  -0.661  1.873   0.50 9.35   ? 220 SER A OG  1 
ATOM   1912 O  OG  B SER A  1 221 ? 3.757  0.061   3.734   0.50 11.41  ? 220 SER A OG  1 
ATOM   1913 N  N   . GLU A  1 222 ? 4.276  2.988   0.651   1.00 8.59   ? 221 GLU A N   1 
ATOM   1914 C  CA  . GLU A  1 222 ? 4.137  3.544   -0.713  1.00 8.90   ? 221 GLU A CA  1 
ATOM   1915 C  C   . GLU A  1 222 ? 5.454  4.089   -1.193  1.00 8.13   ? 221 GLU A C   1 
ATOM   1916 O  O   . GLU A  1 222 ? 5.731  4.035   -2.400  1.00 8.69   ? 221 GLU A O   1 
ATOM   1917 C  CB  . GLU A  1 222 ? 3.057  4.647   -0.708  1.00 9.48   ? 221 GLU A CB  1 
ATOM   1918 C  CG  . GLU A  1 222 ? 1.666  4.087   -0.431  1.00 10.30  ? 221 GLU A CG  1 
ATOM   1919 C  CD  . GLU A  1 222 ? 1.421  3.694   1.001   1.00 9.99   ? 221 GLU A CD  1 
ATOM   1920 O  OE1 . GLU A  1 222 ? 1.974  4.374   1.932   1.00 10.95  ? 221 GLU A OE1 1 
ATOM   1921 O  OE2 . GLU A  1 222 ? 0.759  2.722   1.319   1.00 10.89  ? 221 GLU A OE2 1 
ATOM   1922 N  N   . GLN A  1 223 ? 6.303  4.649   -0.332  1.00 7.65   ? 222 GLN A N   1 
ATOM   1923 C  CA  . GLN A  1 223 ? 7.623  5.097   -0.759  1.00 7.83   ? 222 GLN A CA  1 
ATOM   1924 C  C   . GLN A  1 223 ? 8.456  3.931   -1.266  1.00 7.47   ? 222 GLN A C   1 
ATOM   1925 O  O   . GLN A  1 223 ? 9.119  3.997   -2.303  1.00 8.53   ? 222 GLN A O   1 
ATOM   1926 C  CB  . GLN A  1 223 ? 8.303  5.849   0.383   1.00 7.91   ? 222 GLN A CB  1 
ATOM   1927 C  CG  . GLN A  1 223 ? 7.623  7.209   0.612   1.00 8.45   ? 222 GLN A CG  1 
ATOM   1928 C  CD  . GLN A  1 223 ? 8.296  7.977   1.741   1.00 7.68   ? 222 GLN A CD  1 
ATOM   1929 O  OE1 . GLN A  1 223 ? 8.582  7.389   2.814   1.00 8.13   ? 222 GLN A OE1 1 
ATOM   1930 N  NE2 . GLN A  1 223 ? 8.532  9.228   1.571   1.00 9.24   ? 222 GLN A NE2 1 
ATOM   1931 N  N   . LEU A  1 224 ? 8.379  2.786   -0.520  1.00 8.21   ? 223 LEU A N   1 
ATOM   1932 C  CA  . LEU A  1 224 ? 9.089  1.579   -0.979  1.00 8.27   ? 223 LEU A CA  1 
ATOM   1933 C  C   . LEU A  1 224 ? 8.567  1.122   -2.336  1.00 8.49   ? 223 LEU A C   1 
ATOM   1934 O  O   . LEU A  1 224 ? 9.345  0.679   -3.189  1.00 8.90   ? 223 LEU A O   1 
ATOM   1935 C  CB  . LEU A  1 224 ? 8.963  0.478   0.054   1.00 9.46   ? 223 LEU A CB  1 
ATOM   1936 C  CG  . LEU A  1 224 ? 9.634  0.769   1.385   1.00 10.55  ? 223 LEU A CG  1 
ATOM   1937 C  CD1 . LEU A  1 224 ? 9.148  -0.279  2.463   1.00 14.91  ? 223 LEU A CD1 1 
ATOM   1938 C  CD2 . LEU A  1 224 ? 11.159 0.822   1.183   1.00 15.48  ? 223 LEU A CD2 1 
ATOM   1939 N  N   . ALA A  1 225 ? 7.251  1.241   -2.554  1.00 8.50   ? 224 ALA A N   1 
ATOM   1940 C  CA  . ALA A  1 225 ? 6.689  0.828   -3.845  1.00 8.44   ? 224 ALA A CA  1 
ATOM   1941 C  C   . ALA A  1 225 ? 7.246  1.699   -4.954  1.00 8.24   ? 224 ALA A C   1 
ATOM   1942 O  O   . ALA A  1 225 ? 7.372  1.208   -6.091  1.00 9.22   ? 224 ALA A O   1 
ATOM   1943 C  CB  . ALA A  1 225 ? 5.147  0.922   -3.759  1.00 10.75  ? 224 ALA A CB  1 
ATOM   1944 N  N   . GLN A  1 226 ? 7.571  2.958   -4.679  1.00 8.24   ? 225 GLN A N   1 
ATOM   1945 C  CA  . GLN A  1 226 ? 8.195  3.770   -5.711  1.00 9.07   ? 225 GLN A CA  1 
ATOM   1946 C  C   . GLN A  1 226 ? 9.549  3.226   -6.104  1.00 8.69   ? 225 GLN A C   1 
ATOM   1947 O  O   . GLN A  1 226 ? 9.894  3.194   -7.299  1.00 9.41   ? 225 GLN A O   1 
ATOM   1948 C  CB  . GLN A  1 226 ? 8.364  5.243   -5.297  1.00 9.99   ? 225 GLN A CB  1 
ATOM   1949 C  CG  . GLN A  1 226 ? 7.022  5.935   -5.114  1.00 10.91  ? 225 GLN A CG  1 
ATOM   1950 C  CD  . GLN A  1 226 ? 7.203  7.407   -4.886  1.00 10.55  ? 225 GLN A CD  1 
ATOM   1951 O  OE1 . GLN A  1 226 ? 7.049  7.890   -3.755  1.00 12.14  ? 225 GLN A OE1 1 
ATOM   1952 N  NE2 . GLN A  1 226 ? 7.617  8.134   -5.895  1.00 13.57  ? 225 GLN A NE2 1 
ATOM   1953 N  N   . PHE A  1 227 ? 10.365 2.780   -5.135  1.00 8.92   ? 226 PHE A N   1 
ATOM   1954 C  CA  . PHE A  1 227 ? 11.632 2.117   -5.544  1.00 8.83   ? 226 PHE A CA  1 
ATOM   1955 C  C   . PHE A  1 227 ? 11.390 0.928   -6.420  1.00 8.74   ? 226 PHE A C   1 
ATOM   1956 O  O   . PHE A  1 227 ? 12.072 0.741   -7.449  1.00 9.33   ? 226 PHE A O   1 
ATOM   1957 C  CB  . PHE A  1 227 ? 12.386 1.676   -4.269  1.00 9.07   ? 226 PHE A CB  1 
ATOM   1958 C  CG  . PHE A  1 227 ? 12.904 2.702   -3.339  1.00 9.08   ? 226 PHE A CG  1 
ATOM   1959 C  CD1 . PHE A  1 227 ? 13.224 4.008   -3.721  1.00 12.60  ? 226 PHE A CD1 1 
ATOM   1960 C  CD2 . PHE A  1 227 ? 13.160 2.337   -2.008  1.00 11.93  ? 226 PHE A CD2 1 
ATOM   1961 C  CE1 . PHE A  1 227 ? 13.778 4.970   -2.836  1.00 13.04  ? 226 PHE A CE1 1 
ATOM   1962 C  CE2 . PHE A  1 227 ? 13.777 3.256   -1.135  1.00 13.82  ? 226 PHE A CE2 1 
ATOM   1963 C  CZ  . PHE A  1 227 ? 14.056 4.554   -1.552  1.00 13.99  ? 226 PHE A CZ  1 
ATOM   1964 N  N   . ARG A  1 228 ? 10.446 0.080   -6.022  1.00 8.40   ? 227 ARG A N   1 
ATOM   1965 C  CA  . ARG A  1 228 ? 10.136 -1.140  -6.770  1.00 9.97   ? 227 ARG A CA  1 
ATOM   1966 C  C   . ARG A  1 228 ? 9.599  -0.883  -8.176  1.00 10.52  ? 227 ARG A C   1 
ATOM   1967 O  O   . ARG A  1 228 ? 9.681  -1.746  -9.050  1.00 13.53  ? 227 ARG A O   1 
ATOM   1968 C  CB  . ARG A  1 228 ? 9.147  -2.007  -5.987  1.00 10.84  ? 227 ARG A CB  1 
ATOM   1969 C  CG  . ARG A  1 228 ? 9.625  -2.392  -4.596  1.00 11.20  ? 227 ARG A CG  1 
ATOM   1970 C  CD  . ARG A  1 228 ? 8.906  -3.632  -4.089  1.00 15.87  ? 227 ARG A CD  1 
ATOM   1971 N  NE  . ARG A  1 228 ? 9.131  -3.849  -2.663  1.00 17.01  ? 227 ARG A NE  1 
ATOM   1972 C  CZ  . ARG A  1 228 ? 8.380  -3.323  -1.700  1.00 14.52  ? 227 ARG A CZ  1 
ATOM   1973 N  NH1 . ARG A  1 228 ? 7.350  -2.547  -2.009  1.00 15.24  ? 227 ARG A NH1 1 
ATOM   1974 N  NH2 . ARG A  1 228 ? 8.658  -3.574  -0.428  1.00 17.40  ? 227 ARG A NH2 1 
ATOM   1975 N  N   . SER A  1 229 ? 9.050  0.307   -8.385  1.00 9.71   ? 228 SER A N   1 
ATOM   1976 C  CA  . SER A  1 229 ? 8.478  0.691   -9.682  1.00 10.95  ? 228 SER A CA  1 
ATOM   1977 C  C   . SER A  1 229 ? 9.552  1.098   -10.651 1.00 10.56  ? 228 SER A C   1 
ATOM   1978 O  O   . SER A  1 229 ? 9.284  1.254   -11.853 1.00 11.61  ? 228 SER A O   1 
ATOM   1979 C  CB  . SER A  1 229 ? 7.415  1.769   -9.505  1.00 14.92  ? 228 SER A CB  1 
ATOM   1980 O  OG  . SER A  1 229 ? 7.994  2.980   -9.294  1.00 19.10  ? 228 SER A OG  1 
ATOM   1981 N  N   . LEU A  1 230 ? 10.807 1.318   -10.211 1.00 9.34   ? 229 LEU A N   1 
ATOM   1982 C  CA  . LEU A  1 230 ? 11.859 1.514   -11.169 1.00 8.87   ? 229 LEU A CA  1 
ATOM   1983 C  C   . LEU A  1 230 ? 12.035 0.300   -12.006 1.00 9.19   ? 229 LEU A C   1 
ATOM   1984 O  O   . LEU A  1 230 ? 11.734 -0.804  -11.570 1.00 11.35  ? 229 LEU A O   1 
ATOM   1985 C  CB  . LEU A  1 230 ? 13.160 1.827   -10.428 1.00 10.16  ? 229 LEU A CB  1 
ATOM   1986 C  CG  . LEU A  1 230 ? 13.261 3.176   -9.816  1.00 12.30  ? 229 LEU A CG  1 
ATOM   1987 C  CD1 . LEU A  1 230 ? 14.469 3.167   -8.893  1.00 15.44  ? 229 LEU A CD1 1 
ATOM   1988 C  CD2 . LEU A  1 230 ? 13.363 4.233   -10.999 1.00 13.95  ? 229 LEU A CD2 1 
ATOM   1989 N  N   . LEU A  1 231 ? 12.528 0.493   -13.235 1.00 9.15   ? 230 LEU A N   1 
ATOM   1990 C  CA  . LEU A  1 231 ? 12.543 -0.638  -14.203 1.00 9.99   ? 230 LEU A CA  1 
ATOM   1991 C  C   . LEU A  1 231 ? 14.022 -0.974  -14.518 1.00 8.92   ? 230 LEU A C   1 
ATOM   1992 O  O   . LEU A  1 231 ? 14.896 -0.135  -14.707 1.00 9.67   ? 230 LEU A O   1 
ATOM   1993 C  CB  . LEU A  1 231 ? 11.840 -0.188  -15.512 1.00 9.96   ? 230 LEU A CB  1 
ATOM   1994 C  CG  . LEU A  1 231 ? 10.384 0.184   -15.297 1.00 9.97   ? 230 LEU A CG  1 
ATOM   1995 C  CD1 . LEU A  1 231 ? 9.803  0.632   -16.688 1.00 12.20  ? 230 LEU A CD1 1 
ATOM   1996 C  CD2 . LEU A  1 231 ? 9.556  -0.927  -14.672 1.00 11.44  ? 230 LEU A CD2 1 
ATOM   1997 N  N   . SER A  1 232 ? 14.268 -2.301  -14.579 1.00 9.69   ? 231 SER A N   1 
ATOM   1998 C  CA  . SER A  1 232 ? 15.614 -2.825  -14.835 1.00 10.45  ? 231 SER A CA  1 
ATOM   1999 C  C   . SER A  1 232 ? 15.938 -2.937  -16.320 1.00 10.23  ? 231 SER A C   1 
ATOM   2000 O  O   . SER A  1 232 ? 17.108 -3.095  -16.667 1.00 12.80  ? 231 SER A O   1 
ATOM   2001 C  CB  . SER A  1 232 ? 15.806 -4.133  -14.175 1.00 11.89  ? 231 SER A CB  1 
ATOM   2002 O  OG  . SER A  1 232 ? 14.861 -5.122  -14.649 1.00 12.87  ? 231 SER A OG  1 
ATOM   2003 N  N   . ASN A  1 233 ? 14.914 -2.880  -17.143 1.00 10.34  ? 232 ASN A N   1 
ATOM   2004 C  CA  . ASN A  1 233 ? 15.088 -2.999  -18.595 1.00 11.06  ? 232 ASN A CA  1 
ATOM   2005 C  C   . ASN A  1 233 ? 15.450 -1.665  -19.192 1.00 10.45  ? 232 ASN A C   1 
ATOM   2006 O  O   . ASN A  1 233 ? 15.232 -0.602  -18.593 1.00 10.51  ? 232 ASN A O   1 
ATOM   2007 C  CB  . ASN A  1 233 ? 13.767 -3.482  -19.245 1.00 11.49  ? 232 ASN A CB  1 
ATOM   2008 C  CG  . ASN A  1 233 ? 12.632 -2.566  -18.905 1.00 10.50  ? 232 ASN A CG  1 
ATOM   2009 O  OD1 . ASN A  1 233 ? 12.119 -2.626  -17.757 1.00 10.30  ? 232 ASN A OD1 1 
ATOM   2010 N  ND2 . ASN A  1 233 ? 12.243 -1.687  -19.828 1.00 11.40  ? 232 ASN A ND2 1 
ATOM   2011 N  N   A VAL A  1 234 ? 15.931 -1.708  -20.439 0.50 11.21  ? 233 VAL A N   1 
ATOM   2012 N  N   B VAL A  1 234 ? 16.006 -1.704  -20.415 0.50 11.16  ? 233 VAL A N   1 
ATOM   2013 C  CA  A VAL A  1 234 ? 16.116 -0.466  -21.154 0.50 10.22  ? 233 VAL A CA  1 
ATOM   2014 C  CA  B VAL A  1 234 ? 16.245 -0.503  -21.202 0.50 11.15  ? 233 VAL A CA  1 
ATOM   2015 C  C   A VAL A  1 234 ? 14.818 -0.005  -21.810 0.50 10.10  ? 233 VAL A C   1 
ATOM   2016 C  C   B VAL A  1 234 ? 14.902 -0.018  -21.830 0.50 10.62  ? 233 VAL A C   1 
ATOM   2017 O  O   A VAL A  1 234 ? 13.884 -0.795  -22.063 0.50 11.13  ? 233 VAL A O   1 
ATOM   2018 O  O   B VAL A  1 234 ? 13.991 -0.820  -22.049 0.50 11.68  ? 233 VAL A O   1 
ATOM   2019 C  CB  A VAL A  1 234 ? 17.208 -0.542  -22.242 0.50 12.93  ? 233 VAL A CB  1 
ATOM   2020 C  CB  B VAL A  1 234 ? 17.271 -0.788  -22.380 0.50 16.73  ? 233 VAL A CB  1 
ATOM   2021 C  CG1 A VAL A  1 234 ? 18.513 -0.985  -21.513 0.50 16.43  ? 233 VAL A CG1 1 
ATOM   2022 C  CG1 B VAL A  1 234 ? 17.430 0.413   -23.199 0.50 21.42  ? 233 VAL A CG1 1 
ATOM   2023 C  CG2 A VAL A  1 234 ? 16.806 -1.499  -23.402 0.50 11.46  ? 233 VAL A CG2 1 
ATOM   2024 C  CG2 B VAL A  1 234 ? 18.732 -1.096  -21.877 0.50 17.12  ? 233 VAL A CG2 1 
ATOM   2025 N  N   . GLU A  1 235 ? 14.794 1.293   -22.085 1.00 10.93  ? 234 GLU A N   1 
ATOM   2026 C  CA  . GLU A  1 235 ? 13.634 1.922   -22.722 1.00 11.40  ? 234 GLU A CA  1 
ATOM   2027 C  C   . GLU A  1 235 ? 13.207 1.088   -23.956 1.00 12.06  ? 234 GLU A C   1 
ATOM   2028 O  O   . GLU A  1 235 ? 14.064 0.800   -24.812 1.00 13.31  ? 234 GLU A O   1 
ATOM   2029 C  CB  . GLU A  1 235 ? 13.908 3.323   -23.081 1.00 12.32  ? 234 GLU A CB  1 
ATOM   2030 C  CG  . GLU A  1 235 ? 12.688 4.038   -23.669 1.00 13.77  ? 234 GLU A CG  1 
ATOM   2031 C  CD  . GLU A  1 235 ? 12.898 5.516   -23.743 1.00 16.82  ? 234 GLU A CD  1 
ATOM   2032 O  OE1 . GLU A  1 235 ? 13.053 6.196   -22.725 1.00 16.54  ? 234 GLU A OE1 1 
ATOM   2033 O  OE2 . GLU A  1 235 ? 12.970 6.048   -24.838 1.00 30.28  ? 234 GLU A OE2 1 
ATOM   2034 N  N   . GLY A  1 236 ? 11.919 0.834   -24.075 1.00 11.83  ? 235 GLY A N   1 
ATOM   2035 C  CA  . GLY A  1 236 ? 11.359 0.180   -25.269 1.00 13.54  ? 235 GLY A CA  1 
ATOM   2036 C  C   . GLY A  1 236 ? 11.175 -1.251  -25.021 1.00 14.87  ? 235 GLY A C   1 
ATOM   2037 O  O   . GLY A  1 236 ? 10.263 -1.899  -25.631 1.00 21.83  ? 235 GLY A O   1 
ATOM   2038 N  N   . ASP A  1 237 ? 11.944 -1.829  -24.103 1.00 13.46  ? 236 ASP A N   1 
ATOM   2039 C  CA  . ASP A  1 237 ? 11.791 -3.254  -23.788 1.00 14.85  ? 236 ASP A CA  1 
ATOM   2040 C  C   . ASP A  1 237 ? 10.688 -3.476  -22.744 1.00 13.35  ? 236 ASP A C   1 
ATOM   2041 O  O   . ASP A  1 237 ? 10.460 -2.611  -21.897 1.00 13.83  ? 236 ASP A O   1 
ATOM   2042 C  CB  . ASP A  1 237 ? 13.114 -3.839  -23.291 1.00 14.81  ? 236 ASP A CB  1 
ATOM   2043 C  CG  . ASP A  1 237 ? 14.074 -4.152  -24.422 1.00 17.19  ? 236 ASP A CG  1 
ATOM   2044 O  OD1 . ASP A  1 237 ? 13.711 -3.919  -25.594 1.00 21.46  ? 236 ASP A OD1 1 
ATOM   2045 O  OD2 . ASP A  1 237 ? 15.192 -4.631  -24.139 1.00 20.27  ? 236 ASP A OD2 1 
ATOM   2046 N  N   . ASN A  1 238 ? 10.006 -4.622  -22.795 1.00 14.44  ? 237 ASN A N   1 
ATOM   2047 C  CA  . ASN A  1 238 ? 8.927  -4.895  -21.815 1.00 14.88  ? 237 ASN A CA  1 
ATOM   2048 C  C   . ASN A  1 238 ? 9.423  -4.523  -20.384 1.00 13.05  ? 237 ASN A C   1 
ATOM   2049 O  O   . ASN A  1 238 ? 10.593 -4.761  -20.013 1.00 13.61  ? 237 ASN A O   1 
ATOM   2050 C  CB  . ASN A  1 238 ? 8.537  -6.358  -21.821 1.00 17.29  ? 237 ASN A CB  1 
ATOM   2051 C  CG  . ASN A  1 238 ? 7.339  -6.562  -20.884 1.00 18.10  ? 237 ASN A CG  1 
ATOM   2052 O  OD1 . ASN A  1 238 ? 6.210  -6.059  -21.063 1.00 24.66  ? 237 ASN A OD1 1 
ATOM   2053 N  ND2 . ASN A  1 238 ? 7.658  -7.304  -19.740 1.00 20.50  ? 237 ASN A ND2 1 
ATOM   2054 N  N   . ALA A  1 239 ? 8.589  -3.870  -19.636 1.00 13.18  ? 238 ALA A N   1 
ATOM   2055 C  CA  . ALA A  1 239 ? 8.963  -3.307  -18.333 1.00 13.43  ? 238 ALA A CA  1 
ATOM   2056 C  C   . ALA A  1 239 ? 9.158  -4.432  -17.336 1.00 14.54  ? 238 ALA A C   1 
ATOM   2057 O  O   . ALA A  1 239 ? 8.302  -5.292  -17.099 1.00 27.17  ? 238 ALA A O   1 
ATOM   2058 C  CB  . ALA A  1 239 ? 7.848  -2.325  -17.916 1.00 17.63  ? 238 ALA A CB  1 
ATOM   2059 N  N   . VAL A  1 240 ? 10.278 -4.447  -16.642 1.00 11.85  ? 239 VAL A N   1 
ATOM   2060 C  CA  . VAL A  1 240 ? 10.588 -5.393  -15.619 1.00 12.64  ? 239 VAL A CA  1 
ATOM   2061 C  C   . VAL A  1 240 ? 10.932 -4.600  -14.318 1.00 11.90  ? 239 VAL A C   1 
ATOM   2062 O  O   . VAL A  1 240 ? 12.040 -4.021  -14.220 1.00 13.16  ? 239 VAL A O   1 
ATOM   2063 C  CB  . VAL A  1 240 ? 11.822 -6.223  -16.031 1.00 14.59  ? 239 VAL A CB  1 
ATOM   2064 C  CG1 . VAL A  1 240 ? 12.234 -7.243  -14.947 1.00 17.80  ? 239 VAL A CG1 1 
ATOM   2065 C  CG2 . VAL A  1 240 ? 11.494 -6.987  -17.377 1.00 16.90  ? 239 VAL A CG2 1 
ATOM   2066 N  N   . PRO A  1 241 ? 10.052 -4.601  -13.347 1.00 11.61  ? 240 PRO A N   1 
ATOM   2067 C  CA  . PRO A  1 241 ? 10.318 -3.853  -12.124 1.00 11.94  ? 240 PRO A CA  1 
ATOM   2068 C  C   . PRO A  1 241 ? 11.522 -4.356  -11.365 1.00 10.79  ? 240 PRO A C   1 
ATOM   2069 O  O   . PRO A  1 241 ? 11.850 -5.553  -11.353 1.00 11.55  ? 240 PRO A O   1 
ATOM   2070 C  CB  . PRO A  1 241 ? 9.082  -4.063  -11.308 1.00 14.93  ? 240 PRO A CB  1 
ATOM   2071 C  CG  . PRO A  1 241 ? 7.962  -4.108  -12.425 1.00 19.22  ? 240 PRO A CG  1 
ATOM   2072 C  CD  . PRO A  1 241 ? 8.617  -5.100  -13.425 1.00 14.93  ? 240 PRO A CD  1 
ATOM   2073 N  N   . MET A  1 242 ? 12.193 -3.440  -10.658 1.00 10.70  ? 241 MET A N   1 
ATOM   2074 C  CA  . MET A  1 242 ? 13.318 -3.734  -9.791  1.00 10.91  ? 241 MET A CA  1 
ATOM   2075 C  C   . MET A  1 242 ? 12.760 -4.153  -8.458  1.00 11.17  ? 241 MET A C   1 
ATOM   2076 O  O   . MET A  1 242 ? 12.604 -3.344  -7.530  1.00 12.63  ? 241 MET A O   1 
ATOM   2077 C  CB  . MET A  1 242 ? 14.210 -2.503  -9.629  1.00 15.26  ? 241 MET A CB  1 
ATOM   2078 C  CG  . MET A  1 242 ? 15.174 -2.278  -10.783 1.00 16.79  ? 241 MET A CG  1 
ATOM   2079 S  SD  . MET A  1 242 ? 16.425 -1.033  -10.411 1.00 13.36  ? 241 MET A SD  1 
ATOM   2080 C  CE  . MET A  1 242 ? 16.372 -0.043  -11.902 1.00 13.02  ? 241 MET A CE  1 
ATOM   2081 N  N   A GLN A  1 243 ? 12.392 -5.405  -8.301  0.50 11.18  ? 242 GLN A N   1 
ATOM   2082 N  N   B GLN A  1 243 ? 12.392 -5.414  -8.325  0.50 11.45  ? 242 GLN A N   1 
ATOM   2083 C  CA  A GLN A  1 243 ? 11.625 -5.795  -7.125  0.50 12.39  ? 242 GLN A CA  1 
ATOM   2084 C  CA  B GLN A  1 243 ? 11.620 -5.863  -7.181  0.50 12.27  ? 242 GLN A CA  1 
ATOM   2085 C  C   A GLN A  1 243 ? 12.471 -5.891  -5.876  0.50 11.19  ? 242 GLN A C   1 
ATOM   2086 C  C   B GLN A  1 243 ? 12.460 -5.928  -5.902  0.50 11.26  ? 242 GLN A C   1 
ATOM   2087 O  O   A GLN A  1 243 ? 11.917 -5.681  -4.776  0.50 11.76  ? 242 GLN A O   1 
ATOM   2088 O  O   B GLN A  1 243 ? 11.895 -5.715  -4.813  0.50 11.83  ? 242 GLN A O   1 
ATOM   2089 C  CB  A GLN A  1 243 ? 10.947 -7.154  -7.356  0.50 14.96  ? 242 GLN A CB  1 
ATOM   2090 C  CB  B GLN A  1 243 ? 10.996 -7.243  -7.487  0.50 16.17  ? 242 GLN A CB  1 
ATOM   2091 C  CG  A GLN A  1 243 ? 9.749  -6.992  -8.268  0.50 17.08  ? 242 GLN A CG  1 
ATOM   2092 C  CG  B GLN A  1 243 ? 10.070 -7.745  -6.393  0.50 17.01  ? 242 GLN A CG  1 
ATOM   2093 C  CD  A GLN A  1 243 ? 9.002  -8.222  -8.465  0.50 21.44  ? 242 GLN A CD  1 
ATOM   2094 C  CD  B GLN A  1 243 ? 8.740  -7.101  -6.346  0.50 17.70  ? 242 GLN A CD  1 
ATOM   2095 O  OE1 A GLN A  1 243 ? 8.660  -8.482  -9.616  0.50 33.01  ? 242 GLN A OE1 1 
ATOM   2096 O  OE1 B GLN A  1 243 ? 8.001  -6.917  -5.154  0.50 18.32  ? 242 GLN A OE1 1 
ATOM   2097 N  NE2 A GLN A  1 243 ? 8.528  -8.842  -7.452  0.50 25.15  ? 242 GLN A NE2 1 
ATOM   2098 N  NE2 B GLN A  1 243 ? 8.439  -6.535  -7.542  0.50 19.11  ? 242 GLN A NE2 1 
ATOM   2099 N  N   . HIS A  1 244 ? 13.776 -6.170  -5.991  1.00 9.71   ? 243 HIS A N   1 
ATOM   2100 C  CA  . HIS A  1 244 ? 14.617 -6.318  -4.813  1.00 9.09   ? 243 HIS A CA  1 
ATOM   2101 C  C   . HIS A  1 244 ? 16.058 -6.231  -5.212  1.00 8.30   ? 243 HIS A C   1 
ATOM   2102 O  O   . HIS A  1 244 ? 16.419 -6.527  -6.385  1.00 9.60   ? 243 HIS A O   1 
ATOM   2103 C  CB  . HIS A  1 244 ? 14.312 -7.631  -4.058  1.00 10.63  ? 243 HIS A CB  1 
ATOM   2104 C  CG  . HIS A  1 244 ? 14.468 -8.831  -4.864  1.00 12.24  ? 243 HIS A CG  1 
ATOM   2105 N  ND1 . HIS A  1 244 ? 15.598 -9.543  -4.908  1.00 16.64  ? 243 HIS A ND1 1 
ATOM   2106 C  CD2 . HIS A  1 244 ? 13.558 -9.504  -5.665  1.00 17.42  ? 243 HIS A CD2 1 
ATOM   2107 C  CE1 . HIS A  1 244 ? 15.442 -10.616 -5.697  1.00 18.17  ? 243 HIS A CE1 1 
ATOM   2108 N  NE2 . HIS A  1 244 ? 14.208 -10.602 -6.187  1.00 20.31  ? 243 HIS A NE2 1 
ATOM   2109 N  N   . ASN A  1 245 ? 16.918 -5.888  -4.241  1.00 8.54   ? 244 ASN A N   1 
ATOM   2110 C  CA  . ASN A  1 245 ? 18.337 -5.757  -4.499  1.00 8.09   ? 244 ASN A CA  1 
ATOM   2111 C  C   . ASN A  1 245 ? 19.134 -5.889  -3.220  1.00 7.36   ? 244 ASN A C   1 
ATOM   2112 O  O   . ASN A  1 245 ? 20.244 -5.342  -3.130  1.00 8.77   ? 244 ASN A O   1 
ATOM   2113 C  CB  . ASN A  1 245 ? 18.685 -4.514  -5.284  1.00 8.55   ? 244 ASN A CB  1 
ATOM   2114 C  CG  . ASN A  1 245 ? 18.192 -3.287  -4.618  1.00 7.29   ? 244 ASN A CG  1 
ATOM   2115 O  OD1 . ASN A  1 245 ? 17.901 -3.281  -3.415  1.00 8.23   ? 244 ASN A OD1 1 
ATOM   2116 N  ND2 . ASN A  1 245 ? 18.059 -2.178  -5.373  1.00 9.38   ? 244 ASN A ND2 1 
ATOM   2117 N  N   . ASN A  1 246 ? 18.635 -6.668  -2.263  1.00 8.59   ? 245 ASN A N   1 
ATOM   2118 C  CA  . ASN A  1 246 ? 19.316 -6.841  -0.989  1.00 9.19   ? 245 ASN A CA  1 
ATOM   2119 C  C   . ASN A  1 246 ? 20.023 -8.214  -0.915  1.00 8.98   ? 245 ASN A C   1 
ATOM   2120 O  O   . ASN A  1 246 ? 19.399 -9.242  -1.132  1.00 12.62  ? 245 ASN A O   1 
ATOM   2121 C  CB  . ASN A  1 246 ? 18.395 -6.588  0.192   1.00 9.77   ? 245 ASN A CB  1 
ATOM   2122 C  CG  . ASN A  1 246 ? 17.152 -7.505  0.261   1.00 10.48  ? 245 ASN A CG  1 
ATOM   2123 O  OD1 . ASN A  1 246 ? 16.567 -7.888  -0.752  1.00 10.54  ? 245 ASN A OD1 1 
ATOM   2124 N  ND2 . ASN A  1 246 ? 16.684 -7.761  1.460   1.00 13.40  ? 245 ASN A ND2 1 
ATOM   2125 N  N   . ARG A  1 247 ? 21.266 -8.217  -0.516  1.00 8.78   ? 246 ARG A N   1 
ATOM   2126 C  CA  . ARG A  1 247 ? 22.040 -9.435  -0.342  1.00 9.43   ? 246 ARG A CA  1 
ATOM   2127 C  C   . ARG A  1 247 ? 21.714 -10.036 1.041   1.00 9.44   ? 246 ARG A C   1 
ATOM   2128 O  O   . ARG A  1 247 ? 21.584 -9.309  2.044   1.00 9.70   ? 246 ARG A O   1 
ATOM   2129 C  CB  . ARG A  1 247 ? 23.537 -9.150  -0.460  1.00 9.83   ? 246 ARG A CB  1 
ATOM   2130 C  CG  . ARG A  1 247 ? 24.398 -10.398 -0.564  1.00 9.66   ? 246 ARG A CG  1 
ATOM   2131 C  CD  . ARG A  1 247 ? 25.879 -10.056 -0.521  1.00 9.77   ? 246 ARG A CD  1 
ATOM   2132 N  NE  . ARG A  1 247 ? 26.716 -11.218 -0.808  1.00 10.24  ? 246 ARG A NE  1 
ATOM   2133 C  CZ  . ARG A  1 247 ? 27.999 -11.315 -0.477  1.00 9.45   ? 246 ARG A CZ  1 
ATOM   2134 N  NH1 . ARG A  1 247 ? 28.600 -10.316 0.156   1.00 10.39  ? 246 ARG A NH1 1 
ATOM   2135 N  NH2 . ARG A  1 247 ? 28.683 -12.410 -0.778  1.00 11.00  ? 246 ARG A NH2 1 
ATOM   2136 N  N   . PRO A  1 248 ? 21.642 -11.399 1.206   1.00 10.15  ? 247 PRO A N   1 
ATOM   2137 C  CA  . PRO A  1 248 ? 21.550 -11.988 2.532   1.00 10.26  ? 247 PRO A CA  1 
ATOM   2138 C  C   . PRO A  1 248 ? 22.772 -11.651 3.379   1.00 9.26   ? 247 PRO A C   1 
ATOM   2139 O  O   . PRO A  1 248 ? 23.874 -11.401 2.841   1.00 9.84   ? 247 PRO A O   1 
ATOM   2140 C  CB  . PRO A  1 248 ? 21.550 -13.513 2.210   1.00 12.43  ? 247 PRO A CB  1 
ATOM   2141 C  CG  . PRO A  1 248 ? 20.979 -13.608 0.847   1.00 15.00  ? 247 PRO A CG  1 
ATOM   2142 C  CD  . PRO A  1 248 ? 21.521 -12.399 0.108   1.00 12.55  ? 247 PRO A CD  1 
ATOM   2143 N  N   . THR A  1 249 ? 22.616 -11.749 4.692   1.00 9.92   ? 248 THR A N   1 
ATOM   2144 C  CA  . THR A  1 249 ? 23.787 -11.606 5.590   1.00 9.67   ? 248 THR A CA  1 
ATOM   2145 C  C   . THR A  1 249 ? 24.762 -12.761 5.443   1.00 9.40   ? 248 THR A C   1 
ATOM   2146 O  O   . THR A  1 249 ? 24.362 -13.895 5.058   1.00 11.20  ? 248 THR A O   1 
ATOM   2147 C  CB  . THR A  1 249 ? 23.313 -11.397 7.021   1.00 9.47   ? 248 THR A CB  1 
ATOM   2148 O  OG1 . THR A  1 249 ? 22.468 -12.476 7.403   1.00 11.46  ? 248 THR A OG1 1 
ATOM   2149 C  CG2 . THR A  1 249 ? 22.614 -10.095 7.195   1.00 10.17  ? 248 THR A CG2 1 
ATOM   2150 N  N   . GLN A  1 250 ? 26.004 -12.475 5.719   1.00 10.24  ? 249 GLN A N   1 
ATOM   2151 C  CA  . GLN A  1 250 ? 27.120 -13.355 5.459   1.00 10.57  ? 249 GLN A CA  1 
ATOM   2152 C  C   . GLN A  1 250 ? 27.863 -13.668 6.747   1.00 10.82  ? 249 GLN A C   1 
ATOM   2153 O  O   . GLN A  1 250 ? 27.744 -12.934 7.752   1.00 11.96  ? 249 GLN A O   1 
ATOM   2154 C  CB  . GLN A  1 250 ? 28.089 -12.629 4.490   1.00 10.83  ? 249 GLN A CB  1 
ATOM   2155 C  CG  . GLN A  1 250 ? 27.427 -12.314 3.159   1.00 11.63  ? 249 GLN A CG  1 
ATOM   2156 C  CD  . GLN A  1 250 ? 26.860 -13.544 2.427   1.00 11.89  ? 249 GLN A CD  1 
ATOM   2157 O  OE1 . GLN A  1 250 ? 27.548 -14.565 2.322   1.00 14.17  ? 249 GLN A OE1 1 
ATOM   2158 N  NE2 . GLN A  1 250 ? 25.644 -13.437 1.916   1.00 12.18  ? 249 GLN A NE2 1 
ATOM   2159 N  N   A PRO A  1 251 ? 28.587 -14.789 6.763   0.50 11.98  ? 250 PRO A N   1 
ATOM   2160 N  N   B PRO A  1 251 ? 28.689 -14.697 6.738   0.50 11.84  ? 250 PRO A N   1 
ATOM   2161 C  CA  A PRO A  1 251 ? 29.260 -15.232 8.008   0.50 13.24  ? 250 PRO A CA  1 
ATOM   2162 C  CA  B PRO A  1 251 ? 29.197 -15.099 8.078   0.50 14.26  ? 250 PRO A CA  1 
ATOM   2163 C  C   A PRO A  1 251 ? 30.269 -14.168 8.572   0.50 11.26  ? 250 PRO A C   1 
ATOM   2164 C  C   B PRO A  1 251 ? 30.304 -14.146 8.589   0.50 11.98  ? 250 PRO A C   1 
ATOM   2165 O  O   A PRO A  1 251 ? 31.038 -13.602 7.802   0.50 11.54  ? 250 PRO A O   1 
ATOM   2166 O  O   B PRO A  1 251 ? 31.138 -13.632 7.838   0.50 11.44  ? 250 PRO A O   1 
ATOM   2167 C  CB  A PRO A  1 251 ? 30.044 -16.456 7.491   0.50 16.40  ? 250 PRO A CB  1 
ATOM   2168 C  CB  B PRO A  1 251 ? 29.770 -16.486 7.852   0.50 15.79  ? 250 PRO A CB  1 
ATOM   2169 C  CG  A PRO A  1 251 ? 29.089 -17.080 6.506   0.50 12.85  ? 250 PRO A CG  1 
ATOM   2170 C  CG  B PRO A  1 251 ? 29.959 -16.559 6.388   0.50 19.66  ? 250 PRO A CG  1 
ATOM   2171 C  CD  A PRO A  1 251 ? 28.649 -15.852 5.708   0.50 11.81  ? 250 PRO A CD  1 
ATOM   2172 C  CD  B PRO A  1 251 ? 29.067 -15.630 5.638   0.50 14.78  ? 250 PRO A CD  1 
ATOM   2173 N  N   . LEU A  1 252 ? 30.269 -13.940 9.895   1.00 13.78  ? 251 LEU A N   1 
ATOM   2174 C  CA  . LEU A  1 252 ? 31.176 -12.977 10.516  1.00 13.50  ? 251 LEU A CA  1 
ATOM   2175 C  C   . LEU A  1 252 ? 32.640 -13.465 10.425  1.00 12.78  ? 251 LEU A C   1 
ATOM   2176 O  O   . LEU A  1 252 ? 33.549 -12.597 10.379  1.00 14.33  ? 251 LEU A O   1 
ATOM   2177 C  CB  . LEU A  1 252 ? 30.682 -12.738 11.891  1.00 21.73  ? 251 LEU A CB  1 
ATOM   2178 C  CG  . LEU A  1 252 ? 30.925 -11.554 12.566  1.00 21.07  ? 251 LEU A CG  1 
ATOM   2179 C  CD1 . LEU A  1 252 ? 30.680 -10.257 11.805  1.00 17.93  ? 251 LEU A CD1 1 
ATOM   2180 C  CD2 . LEU A  1 252 ? 30.236 -11.494 13.927  1.00 21.59  ? 251 LEU A CD2 1 
ATOM   2181 N  N   . LYS A  1 253 ? 32.861 -14.766 10.458  1.00 14.05  ? 252 LYS A N   1 
ATOM   2182 C  CA  . LYS A  1 253 ? 34.183 -15.324 10.337  1.00 15.66  ? 252 LYS A CA  1 
ATOM   2183 C  C   . LYS A  1 253 ? 35.170 -14.694 11.317  1.00 16.50  ? 252 LYS A C   1 
ATOM   2184 O  O   . LYS A  1 253 ? 36.309 -14.400 11.000  1.00 18.15  ? 252 LYS A O   1 
ATOM   2185 C  CB  . LYS A  1 253 ? 34.691 -15.230 8.889   1.00 16.89  ? 252 LYS A CB  1 
ATOM   2186 C  CG  . LYS A  1 253 ? 33.932 -15.970 7.862   1.00 19.67  ? 252 LYS A CG  1 
ATOM   2187 C  CD  . LYS A  1 253 ? 34.177 -17.436 7.880   1.00 27.48  ? 252 LYS A CD  1 
ATOM   2188 C  CE  . LYS A  1 253 ? 33.547 -18.058 6.593   1.00 27.81  ? 252 LYS A CE  1 
ATOM   2189 N  NZ  . LYS A  1 253 ? 34.044 -19.465 6.660   1.00 44.44  ? 252 LYS A NZ  1 
ATOM   2190 N  N   . GLY A  1 254 ? 34.702 -14.536 12.549  1.00 17.19  ? 253 GLY A N   1 
ATOM   2191 C  CA  . GLY A  1 254 ? 35.686 -14.058 13.541  1.00 20.38  ? 253 GLY A CA  1 
ATOM   2192 C  C   . GLY A  1 254 ? 35.880 -12.565 13.656  1.00 18.57  ? 253 GLY A C   1 
ATOM   2193 O  O   . GLY A  1 254 ? 36.579 -12.102 14.562  1.00 19.54  ? 253 GLY A O   1 
ATOM   2194 N  N   . ARG A  1 255 ? 35.222 -11.781 12.809  1.00 14.06  ? 254 ARG A N   1 
ATOM   2195 C  CA  . ARG A  1 255 ? 35.333 -10.335 12.912  1.00 12.14  ? 254 ARG A CA  1 
ATOM   2196 C  C   . ARG A  1 255 ? 34.629 -9.854  14.188  1.00 13.55  ? 254 ARG A C   1 
ATOM   2197 O  O   . ARG A  1 255 ? 33.662 -10.491 14.632  1.00 17.19  ? 254 ARG A O   1 
ATOM   2198 C  CB  . ARG A  1 255 ? 34.640 -9.688  11.722  1.00 12.18  ? 254 ARG A CB  1 
ATOM   2199 C  CG  . ARG A  1 255 ? 35.505 -9.793  10.464  1.00 12.60  ? 254 ARG A CG  1 
ATOM   2200 C  CD  . ARG A  1 255 ? 34.791 -9.300  9.216   1.00 11.39  ? 254 ARG A CD  1 
ATOM   2201 N  NE  . ARG A  1 255 ? 33.659 -10.198 8.867   1.00 9.86   ? 254 ARG A NE  1 
ATOM   2202 C  CZ  . ARG A  1 255 ? 32.779 -9.957  7.875   1.00 9.78   ? 254 ARG A CZ  1 
ATOM   2203 N  NH1 . ARG A  1 255 ? 32.805 -8.760  7.238   1.00 9.56   ? 254 ARG A NH1 1 
ATOM   2204 N  NH2 . ARG A  1 255 ? 31.880 -10.863 7.527   1.00 9.99   ? 254 ARG A NH2 1 
ATOM   2205 N  N   . THR A  1 256 ? 35.059 -8.719  14.717  1.00 13.06  ? 255 THR A N   1 
ATOM   2206 C  CA  . THR A  1 256 ? 34.367 -8.083  15.802  1.00 14.44  ? 255 THR A CA  1 
ATOM   2207 C  C   . THR A  1 256 ? 33.613 -6.848  15.282  1.00 11.34  ? 255 THR A C   1 
ATOM   2208 O  O   . THR A  1 256 ? 34.194 -6.037  14.513  1.00 13.23  ? 255 THR A O   1 
ATOM   2209 C  CB  . THR A  1 256 ? 35.396 -7.555  16.822  1.00 19.31  ? 255 THR A CB  1 
ATOM   2210 O  OG1 . THR A  1 256 ? 36.082 -8.672  17.322  1.00 23.96  ? 255 THR A OG1 1 
ATOM   2211 C  CG2 . THR A  1 256 ? 34.727 -6.799  17.996  1.00 20.69  ? 255 THR A CG2 1 
ATOM   2212 N  N   . VAL A  1 257 ? 32.388 -6.702  15.713  1.00 10.55  ? 256 VAL A N   1 
ATOM   2213 C  CA  . VAL A  1 257 ? 31.622 -5.496  15.454  1.00 9.44   ? 256 VAL A CA  1 
ATOM   2214 C  C   . VAL A  1 257 ? 31.845 -4.569  16.639  1.00 9.52   ? 256 VAL A C   1 
ATOM   2215 O  O   . VAL A  1 257 ? 31.549 -4.973  17.806  1.00 11.36  ? 256 VAL A O   1 
ATOM   2216 C  CB  . VAL A  1 257 ? 30.156 -5.817  15.255  1.00 10.12  ? 256 VAL A CB  1 
ATOM   2217 C  CG1 . VAL A  1 257 ? 29.390 -4.466  15.040  1.00 10.65  ? 256 VAL A CG1 1 
ATOM   2218 C  CG2 . VAL A  1 257 ? 29.873 -6.780  14.100  1.00 10.52  ? 256 VAL A CG2 1 
ATOM   2219 N  N   A ARG A  1 258 ? 32.429 -3.400  16.397  0.50 9.27   ? 257 ARG A N   1 
ATOM   2220 N  N   B ARG A  1 258 ? 32.408 -3.392  16.385  0.50 9.28   ? 257 ARG A N   1 
ATOM   2221 C  CA  A ARG A  1 258 ? 32.689 -2.445  17.468  0.50 9.60   ? 257 ARG A CA  1 
ATOM   2222 C  CA  B ARG A  1 258 ? 32.679 -2.426  17.442  0.50 9.61   ? 257 ARG A CA  1 
ATOM   2223 C  C   A ARG A  1 258 ? 31.562 -1.425  17.596  0.50 9.06   ? 257 ARG A C   1 
ATOM   2224 C  C   B ARG A  1 258 ? 31.556 -1.405  17.593  0.50 9.06   ? 257 ARG A C   1 
ATOM   2225 O  O   A ARG A  1 258 ? 30.854 -1.164  16.624  0.50 10.92  ? 257 ARG A O   1 
ATOM   2226 O  O   B ARG A  1 258 ? 30.878 -1.064  16.624  0.50 10.98  ? 257 ARG A O   1 
ATOM   2227 C  CB  A ARG A  1 258 ? 34.020 -1.728  17.235  0.50 10.05  ? 257 ARG A CB  1 
ATOM   2228 C  CB  B ARG A  1 258 ? 34.006 -1.709  17.182  0.50 10.14  ? 257 ARG A CB  1 
ATOM   2229 C  CG  A ARG A  1 258 ? 35.234 -2.641  17.296  0.50 13.88  ? 257 ARG A CG  1 
ATOM   2230 C  CG  B ARG A  1 258 ? 35.144 -2.636  16.785  0.50 14.21  ? 257 ARG A CG  1 
ATOM   2231 C  CD  A ARG A  1 258 ? 36.510 -1.885  16.964  0.50 16.26  ? 257 ARG A CD  1 
ATOM   2232 C  CD  B ARG A  1 258 ? 36.496 -1.978  17.009  0.50 16.67  ? 257 ARG A CD  1 
ATOM   2233 N  NE  A ARG A  1 258 ? 36.577 -1.517  15.553  0.50 12.10  ? 257 ARG A NE  1 
ATOM   2234 N  NE  B ARG A  1 258 ? 36.809 -1.003  15.968  0.50 14.39  ? 257 ARG A NE  1 
ATOM   2235 C  CZ  A ARG A  1 258 ? 37.268 -0.485  15.081  0.50 10.69  ? 257 ARG A CZ  1 
ATOM   2236 C  CZ  B ARG A  1 258 ? 36.784 -1.266  14.666  0.50 19.26  ? 257 ARG A CZ  1 
ATOM   2237 N  NH1 A ARG A  1 258 ? 37.957 0.288   15.910  0.50 12.18  ? 257 ARG A NH1 1 
ATOM   2238 N  NH1 B ARG A  1 258 ? 37.083 -0.317  13.790  0.50 16.25  ? 257 ARG A NH1 1 
ATOM   2239 N  NH2 A ARG A  1 258 ? 37.272 -0.225  13.781  0.50 14.07  ? 257 ARG A NH2 1 
ATOM   2240 N  NH2 B ARG A  1 258 ? 36.458 -2.478  14.239  0.50 20.42  ? 257 ARG A NH2 1 
ATOM   2241 N  N   . ALA A  1 259 ? 31.233 -1.098  18.845  1.00 9.44   ? 258 ALA A N   1 
ATOM   2242 C  CA  . ALA A  1 259 ? 30.212 -0.154  19.166  1.00 9.48   ? 258 ALA A CA  1 
ATOM   2243 C  C   . ALA A  1 259 ? 30.766 1.161   19.620  1.00 9.70   ? 258 ALA A C   1 
ATOM   2244 O  O   . ALA A  1 259 ? 31.683 1.178   20.466  1.00 11.25  ? 258 ALA A O   1 
ATOM   2245 C  CB  . ALA A  1 259 ? 29.227 -0.711  20.249  1.00 11.60  ? 258 ALA A CB  1 
ATOM   2246 N  N   A SER A  1 260 ? 30.190 2.264   19.153  0.50 9.58   ? 259 SER A N   1 
ATOM   2247 N  N   B SER A  1 260 ? 30.187 2.264   19.134  0.50 9.49   ? 259 SER A N   1 
ATOM   2248 C  CA  A SER A  1 260 ? 30.680 3.602   19.522  0.50 11.79  ? 259 SER A CA  1 
ATOM   2249 C  CA  B SER A  1 260 ? 30.486 3.585   19.709  0.50 9.90   ? 259 SER A CA  1 
ATOM   2250 C  C   A SER A  1 260 ? 30.046 4.111   20.805  0.50 12.21  ? 259 SER A C   1 
ATOM   2251 C  C   B SER A  1 260 ? 29.819 3.683   21.124  0.50 9.35   ? 259 SER A C   1 
ATOM   2252 O  O   A SER A  1 260 ? 30.434 5.171   21.284  0.50 16.93  ? 259 SER A O   1 
ATOM   2253 O  O   B SER A  1 260 ? 29.004 2.844   21.515  0.50 11.18  ? 259 SER A O   1 
ATOM   2254 C  CB  A SER A  1 260 ? 30.289 4.525   18.344  0.50 15.97  ? 259 SER A CB  1 
ATOM   2255 C  CB  B SER A  1 260 ? 30.031 4.662   18.748  0.50 11.91  ? 259 SER A CB  1 
ATOM   2256 O  OG  A SER A  1 260 ? 28.926 4.959   18.417  0.50 19.22  ? 259 SER A OG  1 
ATOM   2257 O  OG  B SER A  1 260 ? 28.600 4.768   18.717  0.50 13.26  ? 259 SER A OG  1 
ATOM   2258 N  N   A PHE A  1 261 ? 29.090 3.365   21.348  0.50 13.33  ? 260 PHE A N   1 
ATOM   2259 N  N   B PHE A  1 261 ? 30.227 4.683   21.888  0.50 12.12  ? 260 PHE A N   1 
ATOM   2260 C  CA  A PHE A  1 261 ? 28.416 3.761   22.579  0.50 12.78  ? 260 PHE A CA  1 
ATOM   2261 C  CA  B PHE A  1 261 ? 29.846 4.797   23.254  0.50 10.96  ? 260 PHE A CA  1 
ATOM   2262 C  C   A PHE A  1 261 ? 28.465 2.645   23.617  0.50 14.33  ? 260 PHE A C   1 
ATOM   2263 C  C   B PHE A  1 261 ? 28.329 4.796   23.408  0.50 16.68  ? 260 PHE A C   1 
ATOM   2264 O  O   A PHE A  1 261 ? 28.573 1.468   23.273  0.50 18.98  ? 260 PHE A O   1 
ATOM   2265 O  O   B PHE A  1 261 ? 27.629 5.573   22.760  0.50 13.16  ? 260 PHE A O   1 
ATOM   2266 C  CB  A PHE A  1 261 ? 26.964 4.149   22.293  0.50 32.71  ? 260 PHE A CB  1 
ATOM   2267 C  CB  B PHE A  1 261 ? 30.429 6.102   23.793  0.50 11.17  ? 260 PHE A CB  1 
ATOM   2268 C  CG  A PHE A  1 261 ? 26.240 3.176   21.407  0.50 154.23 ? 260 PHE A CG  1 
ATOM   2269 C  CG  B PHE A  1 261 ? 30.364 6.217   25.273  0.50 11.01  ? 260 PHE A CG  1 
ATOM   2270 C  CD1 A PHE A  1 261 ? 26.616 3.012   20.084  0.50 38.57  ? 260 PHE A CD1 1 
ATOM   2271 C  CD1 B PHE A  1 261 ? 29.194 6.708   25.882  0.50 13.57  ? 260 PHE A CD1 1 
ATOM   2272 C  CD2 A PHE A  1 261 ? 25.184 2.426   21.896  0.50 15.88  ? 260 PHE A CD2 1 
ATOM   2273 C  CD2 B PHE A  1 261 ? 31.463 5.835   26.064  0.50 11.56  ? 260 PHE A CD2 1 
ATOM   2274 C  CE1 A PHE A  1 261 ? 25.953 2.117   19.266  0.50 7.43   ? 260 PHE A CE1 1 
ATOM   2275 C  CE1 B PHE A  1 261 ? 29.107 6.810   27.251  0.50 13.41  ? 260 PHE A CE1 1 
ATOM   2276 C  CE2 A PHE A  1 261 ? 24.516 1.530   21.084  0.50 15.89  ? 260 PHE A CE2 1 
ATOM   2277 C  CE2 B PHE A  1 261 ? 31.353 5.947   27.447  0.50 11.63  ? 260 PHE A CE2 1 
ATOM   2278 C  CZ  A PHE A  1 261 ? 24.901 1.375   19.766  0.50 14.64  ? 260 PHE A CZ  1 
ATOM   2279 C  CZ  B PHE A  1 261 ? 30.176 6.430   28.033  0.50 12.96  ? 260 PHE A CZ  1 
ATOM   2280 O  OXT . PHE A  1 261 ? 28.233 2.878   24.804  1.00 21.21  ? 260 PHE A OXT 1 
ATOM   2281 N  N   . PRO B  1 4   ? 47.221 -5.729  -1.421  1.00 96.19  ? 3   PRO B N   1 
ATOM   2282 C  CA  . PRO B  1 4   ? 47.949 -6.054  -2.652  1.00 44.19  ? 3   PRO B CA  1 
ATOM   2283 C  C   . PRO B  1 4   ? 47.241 -7.144  -3.462  1.00 51.46  ? 3   PRO B C   1 
ATOM   2284 O  O   . PRO B  1 4   ? 46.610 -6.861  -4.464  1.00 56.63  ? 3   PRO B O   1 
ATOM   2285 C  CB  . PRO B  1 4   ? 49.305 -6.575  -2.136  1.00 63.50  ? 3   PRO B CB  1 
ATOM   2286 C  CG  . PRO B  1 4   ? 49.317 -6.360  -0.645  1.00 62.77  ? 3   PRO B CG  1 
ATOM   2287 C  CD  . PRO B  1 4   ? 47.879 -6.284  -0.228  1.00 89.97  ? 3   PRO B CD  1 
ATOM   2288 N  N   . ASP B  1 5   ? 47.383 -8.370  -2.975  1.00 35.60  ? 4   ASP B N   1 
ATOM   2289 C  CA  . ASP B  1 5   ? 46.871 -9.635  -3.456  1.00 37.63  ? 4   ASP B CA  1 
ATOM   2290 C  C   . ASP B  1 5   ? 47.747 -9.818  -4.659  1.00 31.72  ? 4   ASP B C   1 
ATOM   2291 O  O   . ASP B  1 5   ? 48.974 -9.871  -4.569  1.00 27.26  ? 4   ASP B O   1 
ATOM   2292 C  CB  . ASP B  1 5   ? 45.374 -9.588  -3.700  1.00 47.14  ? 4   ASP B CB  1 
ATOM   2293 C  CG  . ASP B  1 5   ? 44.655 -10.658 -2.934  1.00 53.95  ? 4   ASP B CG  1 
ATOM   2294 O  OD1 . ASP B  1 5   ? 45.195 -11.783 -2.838  1.00 94.35  ? 4   ASP B OD1 1 
ATOM   2295 O  OD2 . ASP B  1 5   ? 43.576 -10.364 -2.402  1.00 40.41  ? 4   ASP B OD2 1 
ATOM   2296 N  N   . TRP B  1 6   ? 47.088 -9.914  -5.791  1.00 22.00  ? 5   TRP B N   1 
ATOM   2297 C  CA  . TRP B  1 6   ? 47.777 -10.135 -7.063  1.00 19.42  ? 5   TRP B CA  1 
ATOM   2298 C  C   . TRP B  1 6   ? 48.977 -9.297  -7.392  1.00 17.29  ? 5   TRP B C   1 
ATOM   2299 O  O   . TRP B  1 6   ? 49.166 -8.191  -6.914  1.00 18.50  ? 5   TRP B O   1 
ATOM   2300 C  CB  . TRP B  1 6   ? 46.747 -9.952  -8.154  1.00 16.39  ? 5   TRP B CB  1 
ATOM   2301 C  CG  . TRP B  1 6   ? 46.399 -8.504  -8.513  1.00 15.34  ? 5   TRP B CG  1 
ATOM   2302 C  CD1 . TRP B  1 6   ? 45.365 -7.733  -7.997  1.00 15.10  ? 5   TRP B CD1 1 
ATOM   2303 C  CD2 . TRP B  1 6   ? 47.072 -7.657  -9.457  1.00 13.26  ? 5   TRP B CD2 1 
ATOM   2304 N  NE1 . TRP B  1 6   ? 45.381 -6.489  -8.529  1.00 13.90  ? 5   TRP B NE1 1 
ATOM   2305 C  CE2 . TRP B  1 6   ? 46.424 -6.396  -9.423  1.00 13.12  ? 5   TRP B CE2 1 
ATOM   2306 C  CE3 . TRP B  1 6   ? 48.166 -7.848  -10.342 1.00 14.17  ? 5   TRP B CE3 1 
ATOM   2307 C  CZ2 . TRP B  1 6   ? 46.837 -5.339  -10.232 1.00 13.49  ? 5   TRP B CZ2 1 
ATOM   2308 C  CZ3 . TRP B  1 6   ? 48.590 -6.753  -11.142 1.00 13.74  ? 5   TRP B CZ3 1 
ATOM   2309 C  CH2 . TRP B  1 6   ? 47.927 -5.511  -11.105 1.00 13.43  ? 5   TRP B CH2 1 
ATOM   2310 N  N   . GLY B  1 7   ? 49.870 -9.864  -8.216  1.00 15.22  ? 6   GLY B N   1 
ATOM   2311 C  CA  . GLY B  1 7   ? 51.070 -9.158  -8.738  1.00 15.57  ? 6   GLY B CA  1 
ATOM   2312 C  C   . GLY B  1 7   ? 51.605 -9.820  -9.965  1.00 13.59  ? 6   GLY B C   1 
ATOM   2313 O  O   . GLY B  1 7   ? 50.817 -10.425 -10.726 1.00 14.41  ? 6   GLY B O   1 
ATOM   2314 N  N   . TYR B  1 8   ? 52.904 -9.869  -10.128 1.00 13.19  ? 7   TYR B N   1 
ATOM   2315 C  CA  . TYR B  1 8   ? 53.552 -10.503 -11.225 1.00 13.11  ? 7   TYR B CA  1 
ATOM   2316 C  C   . TYR B  1 8   ? 54.553 -11.514 -10.753 1.00 16.98  ? 7   TYR B C   1 
ATOM   2317 O  O   . TYR B  1 8   ? 55.302 -12.012 -11.629 1.00 19.83  ? 7   TYR B O   1 
ATOM   2318 C  CB  . TYR B  1 8   ? 54.231 -9.441  -12.116 1.00 12.98  ? 7   TYR B CB  1 
ATOM   2319 C  CG  . TYR B  1 8   ? 53.184 -8.569  -12.821 1.00 10.98  ? 7   TYR B CG  1 
ATOM   2320 C  CD1 . TYR B  1 8   ? 52.638 -9.018  -14.075 1.00 11.47  ? 7   TYR B CD1 1 
ATOM   2321 C  CD2 . TYR B  1 8   ? 52.734 -7.396  -12.266 1.00 10.67  ? 7   TYR B CD2 1 
ATOM   2322 C  CE1 . TYR B  1 8   ? 51.702 -8.225  -14.718 1.00 10.82  ? 7   TYR B CE1 1 
ATOM   2323 C  CE2 . TYR B  1 8   ? 51.737 -6.592  -12.915 1.00 10.84  ? 7   TYR B CE2 1 
ATOM   2324 C  CZ  . TYR B  1 8   ? 51.278 -7.024  -14.137 1.00 9.84   ? 7   TYR B CZ  1 
ATOM   2325 O  OH  . TYR B  1 8   ? 50.348 -6.188  -14.773 1.00 9.33   ? 7   TYR B OH  1 
ATOM   2326 N  N   . ASP B  1 9   ? 54.636 -11.860 -9.485  1.00 17.90  ? 8   ASP B N   1 
ATOM   2327 C  CA  . ASP B  1 9   ? 55.600 -12.886 -9.128  1.00 22.21  ? 8   ASP B CA  1 
ATOM   2328 C  C   . ASP B  1 9   ? 55.043 -14.304 -9.283  1.00 23.43  ? 8   ASP B C   1 
ATOM   2329 O  O   . ASP B  1 9   ? 53.974 -14.489 -9.685  1.00 24.07  ? 8   ASP B O   1 
ATOM   2330 C  CB  . ASP B  1 9   ? 56.371 -12.611 -7.859  1.00 29.60  ? 8   ASP B CB  1 
ATOM   2331 C  CG  . ASP B  1 9   ? 55.565 -12.180 -6.751  1.00 38.46  ? 8   ASP B CG  1 
ATOM   2332 O  OD1 . ASP B  1 9   ? 54.786 -12.963 -6.213  1.00 55.70  ? 8   ASP B OD1 1 
ATOM   2333 O  OD2 . ASP B  1 9   ? 55.734 -11.028 -6.337  1.00 56.56  ? 8   ASP B OD2 1 
ATOM   2334 N  N   . ASP B  1 10  ? 55.860 -15.285 -8.915  1.00 28.07  ? 9   ASP B N   1 
ATOM   2335 C  CA  . ASP B  1 10  ? 55.482 -16.689 -9.019  1.00 32.77  ? 9   ASP B CA  1 
ATOM   2336 C  C   . ASP B  1 10  ? 54.384 -17.103 -8.041  1.00 28.70  ? 9   ASP B C   1 
ATOM   2337 O  O   . ASP B  1 10  ? 53.714 -18.113 -8.254  1.00 27.92  ? 9   ASP B O   1 
ATOM   2338 C  CB  . ASP B  1 10  ? 56.710 -17.585 -8.832  1.00 40.08  ? 9   ASP B CB  1 
ATOM   2339 C  CG  . ASP B  1 10  ? 57.177 -18.211 -10.132 1.00 70.19  ? 9   ASP B CG  1 
ATOM   2340 O  OD1 . ASP B  1 10  ? 57.005 -17.577 -11.194 1.00 76.29  ? 9   ASP B OD1 1 
ATOM   2341 O  OD2 . ASP B  1 10  ? 57.716 -19.337 -10.091 1.00 75.26  ? 9   ASP B OD2 1 
ATOM   2342 N  N   . LYS B  1 11  ? 54.196 -16.334 -6.972  1.00 22.74  ? 10  LYS B N   1 
ATOM   2343 C  CA  . LYS B  1 11  ? 53.146 -16.689 -5.970  1.00 26.58  ? 10  LYS B CA  1 
ATOM   2344 C  C   . LYS B  1 11  ? 51.812 -15.969 -6.362  1.00 24.07  ? 10  LYS B C   1 
ATOM   2345 O  O   . LYS B  1 11  ? 50.737 -16.429 -5.948  1.00 27.07  ? 10  LYS B O   1 
ATOM   2346 C  CB  . LYS B  1 11  ? 53.532 -16.151 -4.557  1.00 31.19  ? 10  LYS B CB  1 
ATOM   2347 N  N   . ASN B  1 12  ? 51.851 -14.876 -7.136  1.00 22.21  ? 11  ASN B N   1 
ATOM   2348 C  CA  . ASN B  1 12  ? 50.642 -14.079 -7.257  1.00 22.59  ? 11  ASN B CA  1 
ATOM   2349 C  C   . ASN B  1 12  ? 50.427 -13.568 -8.708  1.00 18.59  ? 11  ASN B C   1 
ATOM   2350 O  O   . ASN B  1 12  ? 49.625 -12.647 -8.902  1.00 17.52  ? 11  ASN B O   1 
ATOM   2351 C  CB  . ASN B  1 12  ? 50.635 -12.916 -6.252  1.00 20.58  ? 11  ASN B CB  1 
ATOM   2352 C  CG  . ASN B  1 12  ? 51.733 -11.948 -6.481  1.00 23.06  ? 11  ASN B CG  1 
ATOM   2353 O  OD1 . ASN B  1 12  ? 52.391 -11.958 -7.546  1.00 19.44  ? 11  ASN B OD1 1 
ATOM   2354 N  ND2 . ASN B  1 12  ? 51.939 -11.017 -5.563  1.00 22.87  ? 11  ASN B ND2 1 
ATOM   2355 N  N   . GLY B  1 13  ? 51.156 -14.121 -9.663  1.00 19.93  ? 12  GLY B N   1 
ATOM   2356 C  CA  . GLY B  1 13  ? 51.256 -13.563 -10.980 1.00 17.30  ? 12  GLY B CA  1 
ATOM   2357 C  C   . GLY B  1 13  ? 50.209 -14.036 -11.957 1.00 18.05  ? 12  GLY B C   1 
ATOM   2358 O  O   . GLY B  1 13  ? 49.242 -14.722 -11.511 1.00 19.44  ? 12  GLY B O   1 
ATOM   2359 N  N   . PRO B  1 14  ? 50.365 -13.772 -13.259 1.00 17.02  ? 13  PRO B N   1 
ATOM   2360 C  CA  . PRO B  1 14  ? 49.416 -14.074 -14.244 1.00 16.38  ? 13  PRO B CA  1 
ATOM   2361 C  C   . PRO B  1 14  ? 48.818 -15.507 -14.221 1.00 17.44  ? 13  PRO B C   1 
ATOM   2362 O  O   . PRO B  1 14  ? 47.631 -15.668 -14.510 1.00 20.81  ? 13  PRO B O   1 
ATOM   2363 C  CB  . PRO B  1 14  ? 50.098 -13.833 -15.572 1.00 16.45  ? 13  PRO B CB  1 
ATOM   2364 C  CG  . PRO B  1 14  ? 50.981 -12.655 -15.168 1.00 16.15  ? 13  PRO B CG  1 
ATOM   2365 C  CD  . PRO B  1 14  ? 51.487 -12.946 -13.795 1.00 16.12  ? 13  PRO B CD  1 
ATOM   2366 N  N   . GLU B  1 15  ? 49.617 -16.513 -13.890 1.00 18.83  ? 14  GLU B N   1 
ATOM   2367 C  CA  . GLU B  1 15  ? 49.114 -17.904 -13.821 1.00 21.40  ? 14  GLU B CA  1 
ATOM   2368 C  C   . GLU B  1 15  ? 48.237 -18.108 -12.552 1.00 23.31  ? 14  GLU B C   1 
ATOM   2369 O  O   . GLU B  1 15  ? 47.604 -19.191 -12.393 1.00 25.90  ? 14  GLU B O   1 
ATOM   2370 C  CB  . GLU B  1 15  ? 50.303 -18.857 -13.839 1.00 27.38  ? 14  GLU B CB  1 
ATOM   2371 C  CG  . GLU B  1 15  ? 51.040 -18.704 -15.132 1.00 29.76  ? 14  GLU B CG  1 
ATOM   2372 C  CD  . GLU B  1 15  ? 50.446 -19.324 -16.369 1.00 53.04  ? 14  GLU B CD  1 
ATOM   2373 O  OE1 . GLU B  1 15  ? 51.192 -19.392 -17.407 1.00 83.73  ? 14  GLU B OE1 1 
ATOM   2374 O  OE2 . GLU B  1 15  ? 49.268 -19.755 -16.335 1.00 94.25  ? 14  GLU B OE2 1 
ATOM   2375 N  N   . GLN B  1 16  ? 48.249 -17.190 -11.595 1.00 21.16  ? 15  GLN B N   1 
ATOM   2376 C  CA  . GLN B  1 16  ? 47.624 -17.364 -10.306 1.00 19.78  ? 15  GLN B CA  1 
ATOM   2377 C  C   . GLN B  1 16  ? 46.280 -16.559 -10.309 1.00 20.57  ? 15  GLN B C   1 
ATOM   2378 O  O   . GLN B  1 16  ? 45.375 -16.724 -9.438  1.00 21.66  ? 15  GLN B O   1 
ATOM   2379 C  CB  . GLN B  1 16  ? 48.476 -16.992 -9.125  1.00 20.02  ? 15  GLN B CB  1 
ATOM   2380 C  CG  . GLN B  1 16  ? 49.795 -17.731 -9.133  1.00 23.53  ? 15  GLN B CG  1 
ATOM   2381 C  CD  . GLN B  1 16  ? 49.639 -19.234 -9.094  1.00 22.27  ? 15  GLN B CD  1 
ATOM   2382 O  OE1 . GLN B  1 16  ? 48.622 -19.759 -8.492  1.00 27.20  ? 15  GLN B OE1 1 
ATOM   2383 N  NE2 . GLN B  1 16  ? 50.423 -19.926 -9.914  1.00 25.85  ? 15  GLN B NE2 1 
ATOM   2384 N  N   . TRP B  1 17  ? 46.149 -15.595 -11.257 1.00 18.30  ? 16  TRP B N   1 
ATOM   2385 C  CA  . TRP B  1 17  ? 45.027 -14.636 -11.242 1.00 17.05  ? 16  TRP B CA  1 
ATOM   2386 C  C   . TRP B  1 17  ? 43.670 -15.348 -11.348 1.00 17.41  ? 16  TRP B C   1 
ATOM   2387 O  O   . TRP B  1 17  ? 42.701 -14.789 -10.881 1.00 17.61  ? 16  TRP B O   1 
ATOM   2388 C  CB  . TRP B  1 17  ? 45.171 -13.665 -12.414 1.00 15.21  ? 16  TRP B CB  1 
ATOM   2389 C  CG  . TRP B  1 17  ? 46.364 -12.701 -12.239 1.00 13.22  ? 16  TRP B CG  1 
ATOM   2390 C  CD1 . TRP B  1 17  ? 47.191 -12.569 -11.123 1.00 14.70  ? 16  TRP B CD1 1 
ATOM   2391 C  CD2 . TRP B  1 17  ? 46.862 -11.818 -13.237 1.00 13.20  ? 16  TRP B CD2 1 
ATOM   2392 N  NE1 . TRP B  1 17  ? 48.131 -11.599 -11.374 1.00 13.30  ? 16  TRP B NE1 1 
ATOM   2393 C  CE2 . TRP B  1 17  ? 47.988 -11.143 -12.679 1.00 13.08  ? 16  TRP B CE2 1 
ATOM   2394 C  CE3 . TRP B  1 17  ? 46.502 -11.572 -14.576 1.00 12.58  ? 16  TRP B CE3 1 
ATOM   2395 C  CZ2 . TRP B  1 17  ? 48.713 -10.186 -13.383 1.00 12.86  ? 16  TRP B CZ2 1 
ATOM   2396 C  CZ3 . TRP B  1 17  ? 47.254 -10.645 -15.320 1.00 12.49  ? 16  TRP B CZ3 1 
ATOM   2397 C  CH2 . TRP B  1 17  ? 48.329 -9.947  -14.703 1.00 12.16  ? 16  TRP B CH2 1 
ATOM   2398 N  N   . SER B  1 18  ? 43.545 -16.435 -12.058 1.00 17.79  ? 17  SER B N   1 
ATOM   2399 C  CA  . SER B  1 18  ? 42.279 -17.021 -12.277 1.00 17.35  ? 17  SER B CA  1 
ATOM   2400 C  C   . SER B  1 18  ? 41.626 -17.545 -11.041 1.00 17.64  ? 17  SER B C   1 
ATOM   2401 O  O   . SER B  1 18  ? 40.335 -17.646 -11.052 1.00 20.27  ? 17  SER B O   1 
ATOM   2402 C  CB  . SER B  1 18  ? 42.298 -18.180 -13.250 1.00 18.11  ? 17  SER B CB  1 
ATOM   2403 O  OG  . SER B  1 18  ? 42.952 -19.315 -12.759 1.00 23.10  ? 17  SER B OG  1 
ATOM   2404 N  N   . LYS B  1 19  ? 42.365 -17.715 -9.908  1.00 20.78  ? 18  LYS B N   1 
ATOM   2405 C  CA  . LYS B  1 19  ? 41.686 -18.171 -8.628  1.00 21.15  ? 18  LYS B CA  1 
ATOM   2406 C  C   . LYS B  1 19  ? 40.600 -17.137 -8.180  1.00 23.38  ? 18  LYS B C   1 
ATOM   2407 O  O   . LYS B  1 19  ? 39.481 -17.487 -7.824  1.00 23.54  ? 18  LYS B O   1 
ATOM   2408 C  CB  . LYS B  1 19  ? 42.761 -18.441 -7.523  1.00 23.01  ? 18  LYS B CB  1 
ATOM   2409 C  CG  . LYS B  1 19  ? 43.736 -19.669 -7.666  1.00 38.21  ? 18  LYS B CG  1 
ATOM   2410 N  N   . LEU B  1 20  ? 40.937 -15.843 -8.156  1.00 21.19  ? 19  LEU B N   1 
ATOM   2411 C  CA  . LEU B  1 20  ? 40.025 -14.810 -7.705  1.00 24.10  ? 19  LEU B CA  1 
ATOM   2412 C  C   . LEU B  1 20  ? 39.404 -14.132 -8.835  1.00 18.05  ? 19  LEU B C   1 
ATOM   2413 O  O   . LEU B  1 20  ? 38.348 -13.497 -8.689  1.00 19.07  ? 19  LEU B O   1 
ATOM   2414 C  CB  . LEU B  1 20  ? 40.695 -13.793 -6.847  1.00 28.41  ? 19  LEU B CB  1 
ATOM   2415 N  N   . TYR B  1 21  ? 40.019 -14.275 -10.077 1.00 16.83  ? 20  TYR B N   1 
ATOM   2416 C  CA  . TYR B  1 21  ? 39.427 -13.598 -11.215 1.00 14.16  ? 20  TYR B CA  1 
ATOM   2417 C  C   . TYR B  1 21  ? 39.182 -14.555 -12.337 1.00 15.47  ? 20  TYR B C   1 
ATOM   2418 O  O   . TYR B  1 21  ? 39.987 -14.661 -13.303 1.00 15.14  ? 20  TYR B O   1 
ATOM   2419 C  CB  . TYR B  1 21  ? 40.381 -12.429 -11.723 1.00 13.94  ? 20  TYR B CB  1 
ATOM   2420 C  CG  . TYR B  1 21  ? 40.608 -11.443 -10.602 1.00 14.58  ? 20  TYR B CG  1 
ATOM   2421 C  CD1 . TYR B  1 21  ? 39.668 -10.390 -10.429 1.00 19.10  ? 20  TYR B CD1 1 
ATOM   2422 C  CD2 . TYR B  1 21  ? 41.712 -11.554 -9.768  1.00 18.73  ? 20  TYR B CD2 1 
ATOM   2423 C  CE1 . TYR B  1 21  ? 39.867 -9.496  -9.353  1.00 21.18  ? 20  TYR B CE1 1 
ATOM   2424 C  CE2 . TYR B  1 21  ? 41.866 -10.601 -8.703  1.00 22.82  ? 20  TYR B CE2 1 
ATOM   2425 C  CZ  . TYR B  1 21  ? 40.951 -9.628  -8.558  1.00 23.25  ? 20  TYR B CZ  1 
ATOM   2426 O  OH  . TYR B  1 21  ? 41.105 -8.697  -7.579  1.00 35.14  ? 20  TYR B OH  1 
ATOM   2427 N  N   A PRO B  1 22  ? 38.138 -15.430 -12.232 0.50 13.40  ? 21  PRO B N   1 
ATOM   2428 N  N   B PRO B  1 22  ? 38.003 -15.245 -12.352 0.50 16.40  ? 21  PRO B N   1 
ATOM   2429 C  CA  A PRO B  1 22  ? 37.951 -16.480 -13.253 0.50 17.02  ? 21  PRO B CA  1 
ATOM   2430 C  CA  B PRO B  1 22  ? 37.837 -16.365 -13.306 0.50 17.19  ? 21  PRO B CA  1 
ATOM   2431 C  C   A PRO B  1 22  ? 37.788 -15.921 -14.683 0.50 14.60  ? 21  PRO B C   1 
ATOM   2432 C  C   B PRO B  1 22  ? 37.803 -15.896 -14.736 0.50 15.88  ? 21  PRO B C   1 
ATOM   2433 O  O   A PRO B  1 22  ? 38.087 -16.668 -15.603 0.50 16.49  ? 21  PRO B O   1 
ATOM   2434 O  O   B PRO B  1 22  ? 38.015 -16.681 -15.669 0.50 16.96  ? 21  PRO B O   1 
ATOM   2435 C  CB  A PRO B  1 22  ? 36.645 -17.232 -12.797 0.50 16.99  ? 21  PRO B CB  1 
ATOM   2436 C  CB  B PRO B  1 22  ? 36.386 -16.809 -13.057 0.50 18.31  ? 21  PRO B CB  1 
ATOM   2437 C  CG  A PRO B  1 22  ? 36.713 -16.991 -11.328 0.50 16.45  ? 21  PRO B CG  1 
ATOM   2438 C  CG  B PRO B  1 22  ? 36.156 -16.488 -11.644 0.50 18.66  ? 21  PRO B CG  1 
ATOM   2439 C  CD  A PRO B  1 22  ? 37.188 -15.569 -11.119 0.50 16.10  ? 21  PRO B CD  1 
ATOM   2440 C  CD  B PRO B  1 22  ? 36.932 -15.205 -11.330 0.50 18.15  ? 21  PRO B CD  1 
ATOM   2441 N  N   . ILE B  1 23  ? 37.473 -14.633 -14.921 1.00 14.45  ? 22  ILE B N   1 
ATOM   2442 C  CA  . ILE B  1 23  ? 37.460 -14.081 -16.226 1.00 15.26  ? 22  ILE B CA  1 
ATOM   2443 C  C   . ILE B  1 23  ? 38.858 -14.090 -16.901 1.00 13.40  ? 22  ILE B C   1 
ATOM   2444 O  O   . ILE B  1 23  ? 38.954 -13.910 -18.126 1.00 14.59  ? 22  ILE B O   1 
ATOM   2445 C  CB  . ILE B  1 23  ? 36.919 -12.615 -16.214 1.00 14.76  ? 22  ILE B CB  1 
ATOM   2446 C  CG1 . ILE B  1 23  ? 36.387 -12.184 -17.562 1.00 17.06  ? 22  ILE B CG1 1 
ATOM   2447 C  CG2 . ILE B  1 23  ? 37.965 -11.620 -15.731 1.00 15.92  ? 22  ILE B CG2 1 
ATOM   2448 C  CD1 . ILE B  1 23  ? 35.124 -12.947 -18.040 1.00 20.67  ? 22  ILE B CD1 1 
ATOM   2449 N  N   . ALA B  1 24  ? 39.918 -14.370 -16.131 1.00 14.10  ? 23  ALA B N   1 
ATOM   2450 C  CA  . ALA B  1 24  ? 41.273 -14.523 -16.684 1.00 13.56  ? 23  ALA B CA  1 
ATOM   2451 C  C   . ALA B  1 24  ? 41.259 -15.565 -17.760 1.00 15.21  ? 23  ALA B C   1 
ATOM   2452 O  O   . ALA B  1 24  ? 42.115 -15.472 -18.696 1.00 16.13  ? 23  ALA B O   1 
ATOM   2453 C  CB  . ALA B  1 24  ? 42.258 -14.966 -15.634 1.00 14.58  ? 23  ALA B CB  1 
ATOM   2454 N  N   . ASN B  1 25  ? 40.313 -16.539 -17.749 1.00 15.58  ? 24  ASN B N   1 
ATOM   2455 C  CA  . ASN B  1 25  ? 40.213 -17.583 -18.738 1.00 16.69  ? 24  ASN B CA  1 
ATOM   2456 C  C   . ASN B  1 25  ? 39.092 -17.336 -19.747 1.00 15.82  ? 24  ASN B C   1 
ATOM   2457 O  O   . ASN B  1 25  ? 38.578 -18.231 -20.443 1.00 18.30  ? 24  ASN B O   1 
ATOM   2458 C  CB  . ASN B  1 25  ? 40.114 -18.976 -18.094 1.00 19.61  ? 24  ASN B CB  1 
ATOM   2459 C  CG  . ASN B  1 25  ? 41.343 -19.332 -17.282 1.00 21.55  ? 24  ASN B CG  1 
ATOM   2460 O  OD1 . ASN B  1 25  ? 41.177 -19.979 -16.240 1.00 26.83  ? 24  ASN B OD1 1 
ATOM   2461 N  ND2 . ASN B  1 25  ? 42.487 -19.175 -17.820 1.00 22.85  ? 24  ASN B ND2 1 
ATOM   2462 N  N   . GLY B  1 26  ? 38.662 -16.057 -19.851 1.00 16.49  ? 25  GLY B N   1 
ATOM   2463 C  CA  . GLY B  1 26  ? 37.552 -15.663 -20.707 1.00 15.92  ? 25  GLY B CA  1 
ATOM   2464 C  C   . GLY B  1 26  ? 37.830 -15.645 -22.199 1.00 16.35  ? 25  GLY B C   1 
ATOM   2465 O  O   . GLY B  1 26  ? 38.868 -16.015 -22.668 1.00 16.99  ? 25  GLY B O   1 
ATOM   2466 N  N   . ASN B  1 27  ? 36.806 -15.170 -22.938 1.00 16.36  ? 26  ASN B N   1 
ATOM   2467 C  CA  . ASN B  1 27  ? 36.835 -15.199 -24.406 1.00 16.17  ? 26  ASN B CA  1 
ATOM   2468 C  C   . ASN B  1 27  ? 37.298 -13.855 -24.974 1.00 13.86  ? 26  ASN B C   1 
ATOM   2469 O  O   . ASN B  1 27  ? 37.459 -13.758 -26.218 1.00 17.56  ? 26  ASN B O   1 
ATOM   2470 C  CB  . ASN B  1 27  ? 35.445 -15.525 -24.927 1.00 21.98  ? 26  ASN B CB  1 
ATOM   2471 C  CG  . ASN B  1 27  ? 35.068 -16.880 -24.590 1.00 22.94  ? 26  ASN B CG  1 
ATOM   2472 O  OD1 . ASN B  1 27  ? 35.885 -17.803 -24.597 1.00 26.54  ? 26  ASN B OD1 1 
ATOM   2473 N  ND2 . ASN B  1 27  ? 33.798 -17.088 -24.358 1.00 30.18  ? 26  ASN B ND2 1 
ATOM   2474 N  N   A ASN B  1 28  ? 37.570 -12.855 -24.136 0.50 14.59  ? 27  ASN B N   1 
ATOM   2475 N  N   B ASN B  1 28  ? 37.476 -12.840 -24.125 0.50 14.88  ? 27  ASN B N   1 
ATOM   2476 C  CA  A ASN B  1 28  ? 38.003 -11.577 -24.685 0.50 13.01  ? 27  ASN B CA  1 
ATOM   2477 C  CA  B ASN B  1 28  ? 37.949 -11.562 -24.622 0.50 14.20  ? 27  ASN B CA  1 
ATOM   2478 C  C   A ASN B  1 28  ? 39.185 -11.004 -23.950 0.50 10.97  ? 27  ASN B C   1 
ATOM   2479 C  C   B ASN B  1 28  ? 39.081 -11.040 -23.799 0.50 13.02  ? 27  ASN B C   1 
ATOM   2480 O  O   A ASN B  1 28  ? 39.215 -9.779  -23.590 0.50 10.11  ? 27  ASN B O   1 
ATOM   2481 O  O   B ASN B  1 28  ? 38.990 -9.846  -23.322 0.50 15.48  ? 27  ASN B O   1 
ATOM   2482 C  CB  A ASN B  1 28  ? 36.825 -10.514 -24.697 0.50 14.55  ? 27  ASN B CB  1 
ATOM   2483 C  CB  B ASN B  1 28  ? 36.783 -10.462 -24.698 0.50 16.28  ? 27  ASN B CB  1 
ATOM   2484 C  CG  A ASN B  1 28  ? 35.577 -11.006 -25.483 0.50 12.44  ? 27  ASN B CG  1 
ATOM   2485 C  CG  B ASN B  1 28  ? 35.746 -10.751 -25.835 0.50 19.91  ? 27  ASN B CG  1 
ATOM   2486 O  OD1 A ASN B  1 28  ? 34.693 -11.600 -24.917 0.50 17.61  ? 27  ASN B OD1 1 
ATOM   2487 O  OD1 B ASN B  1 28  ? 35.553 -11.800 -26.169 0.50 32.85  ? 27  ASN B OD1 1 
ATOM   2488 N  ND2 A ASN B  1 28  ? 35.590 -10.822 -26.786 0.50 14.89  ? 27  ASN B ND2 1 
ATOM   2489 N  ND2 B ASN B  1 28  ? 35.255 -9.774  -26.464 0.50 23.93  ? 27  ASN B ND2 1 
ATOM   2490 N  N   . GLN B  1 29  ? 40.111 -11.867 -23.571 1.00 12.73  ? 28  GLN B N   1 
ATOM   2491 C  CA  . GLN B  1 29  ? 41.244 -11.493 -22.725 1.00 11.48  ? 28  GLN B CA  1 
ATOM   2492 C  C   . GLN B  1 29  ? 42.327 -10.808 -23.559 1.00 11.35  ? 28  GLN B C   1 
ATOM   2493 O  O   . GLN B  1 29  ? 42.549 -11.114 -24.750 1.00 13.34  ? 28  GLN B O   1 
ATOM   2494 C  CB  . GLN B  1 29  ? 41.757 -12.662 -21.952 1.00 12.56  ? 28  GLN B CB  1 
ATOM   2495 C  CG  . GLN B  1 29  ? 40.741 -13.069 -20.838 1.00 14.21  ? 28  GLN B CG  1 
ATOM   2496 C  CD  . GLN B  1 29  ? 40.662 -11.948 -19.804 1.00 12.23  ? 28  GLN B CD  1 
ATOM   2497 O  OE1 . GLN B  1 29  ? 41.642 -11.782 -19.053 1.00 12.68  ? 28  GLN B OE1 1 
ATOM   2498 N  NE2 . GLN B  1 29  ? 39.544 -11.281 -19.666 1.00 12.26  ? 28  GLN B NE2 1 
ATOM   2499 N  N   . SER B  1 30  ? 43.058 -9.900  -22.922 1.00 10.87  ? 29  SER B N   1 
ATOM   2500 C  CA  . SER B  1 30  ? 44.205 -9.177  -23.536 1.00 11.06  ? 29  SER B CA  1 
ATOM   2501 C  C   . SER B  1 30  ? 45.427 -9.362  -22.666 1.00 10.72  ? 29  SER B C   1 
ATOM   2502 O  O   . SER B  1 30  ? 45.319 -9.608  -21.479 1.00 11.71  ? 29  SER B O   1 
ATOM   2503 C  CB  . SER B  1 30  ? 43.882 -7.686  -23.568 1.00 11.69  ? 29  SER B CB  1 
ATOM   2504 O  OG  . SER B  1 30  ? 42.769 -7.465  -24.499 1.00 11.48  ? 29  SER B OG  1 
ATOM   2505 N  N   . PRO B  1 31  ? 46.640 -9.232  -23.202 1.00 10.50  ? 30  PRO B N   1 
ATOM   2506 C  CA  . PRO B  1 31  ? 46.892 -8.888  -24.631 1.00 10.54  ? 30  PRO B CA  1 
ATOM   2507 C  C   . PRO B  1 31  ? 46.814 -10.111 -25.514 1.00 10.73  ? 30  PRO B C   1 
ATOM   2508 O  O   . PRO B  1 31  ? 46.562 -11.230 -25.024 1.00 12.18  ? 30  PRO B O   1 
ATOM   2509 C  CB  . PRO B  1 31  ? 48.345 -8.398  -24.517 1.00 11.17  ? 30  PRO B CB  1 
ATOM   2510 C  CG  . PRO B  1 31  ? 48.960 -9.279  -23.459 1.00 11.30  ? 30  PRO B CG  1 
ATOM   2511 C  CD  . PRO B  1 31  ? 47.906 -9.416  -22.422 1.00 11.75  ? 30  PRO B CD  1 
ATOM   2512 N  N   . VAL B  1 32  ? 47.054 -9.884  -26.801 1.00 11.77  ? 31  VAL B N   1 
ATOM   2513 C  CA  . VAL B  1 32  ? 47.014 -10.990 -27.823 1.00 11.95  ? 31  VAL B CA  1 
ATOM   2514 C  C   . VAL B  1 32  ? 48.218 -10.754 -28.710 1.00 11.68  ? 31  VAL B C   1 
ATOM   2515 O  O   . VAL B  1 32  ? 48.831 -9.691  -28.822 1.00 12.23  ? 31  VAL B O   1 
ATOM   2516 C  CB  . VAL B  1 32  ? 45.718 -10.969 -28.638 1.00 13.00  ? 31  VAL B CB  1 
ATOM   2517 C  CG1 . VAL B  1 32  ? 44.489 -11.220 -27.714 1.00 13.93  ? 31  VAL B CG1 1 
ATOM   2518 C  CG2 . VAL B  1 32  ? 45.569 -9.729  -29.503 1.00 13.57  ? 31  VAL B CG2 1 
ATOM   2519 N  N   . ASP B  1 33  ? 48.540 -11.866 -29.416 1.00 13.11  ? 32  ASP B N   1 
ATOM   2520 C  CA  . ASP B  1 33  ? 49.477 -11.787 -30.560 1.00 12.66  ? 32  ASP B CA  1 
ATOM   2521 C  C   . ASP B  1 33  ? 48.658 -11.414 -31.791 1.00 12.80  ? 32  ASP B C   1 
ATOM   2522 O  O   . ASP B  1 33  ? 47.623 -12.048 -32.032 1.00 17.52  ? 32  ASP B O   1 
ATOM   2523 C  CB  . ASP B  1 33  ? 50.072 -13.158 -30.793 1.00 13.88  ? 32  ASP B CB  1 
ATOM   2524 C  CG  . ASP B  1 33  ? 51.075 -13.146 -31.931 1.00 13.63  ? 32  ASP B CG  1 
ATOM   2525 O  OD1 . ASP B  1 33  ? 51.977 -12.274 -31.988 1.00 14.15  ? 32  ASP B OD1 1 
ATOM   2526 O  OD2 . ASP B  1 33  ? 50.908 -13.983 -32.841 1.00 19.24  ? 32  ASP B OD2 1 
ATOM   2527 N  N   . ILE B  1 34  ? 49.084 -10.421 -32.509 1.00 13.26  ? 33  ILE B N   1 
ATOM   2528 C  CA  . ILE B  1 34  ? 48.438 -9.972  -33.748 1.00 13.28  ? 33  ILE B CA  1 
ATOM   2529 C  C   . ILE B  1 34  ? 49.155 -10.687 -34.862 1.00 13.98  ? 33  ILE B C   1 
ATOM   2530 O  O   . ILE B  1 34  ? 50.282 -10.374 -35.219 1.00 14.42  ? 33  ILE B O   1 
ATOM   2531 C  CB  . ILE B  1 34  ? 48.481 -8.461  -33.923 1.00 13.25  ? 33  ILE B CB  1 
ATOM   2532 C  CG1 . ILE B  1 34  ? 47.733 -7.809  -32.753 1.00 13.39  ? 33  ILE B CG1 1 
ATOM   2533 C  CG2 . ILE B  1 34  ? 47.899 -8.016  -35.253 1.00 16.13  ? 33  ILE B CG2 1 
ATOM   2534 C  CD1 . ILE B  1 34  ? 47.882 -6.308  -32.720 1.00 16.24  ? 33  ILE B CD1 1 
ATOM   2535 N  N   . LYS B  1 35  ? 48.482 -11.655 -35.458 1.00 16.40  ? 34  LYS B N   1 
ATOM   2536 C  CA  . LYS B  1 35  ? 49.065 -12.430 -36.587 1.00 18.50  ? 34  LYS B CA  1 
ATOM   2537 C  C   . LYS B  1 35  ? 48.541 -11.676 -37.774 1.00 17.07  ? 34  LYS B C   1 
ATOM   2538 O  O   . LYS B  1 35  ? 47.304 -11.681 -38.115 1.00 17.78  ? 34  LYS B O   1 
ATOM   2539 C  CB  . LYS B  1 35  ? 48.543 -13.893 -36.437 1.00 23.66  ? 34  LYS B CB  1 
ATOM   2540 C  CG  . LYS B  1 35  ? 49.015 -14.866 -37.459 1.00 33.50  ? 34  LYS B CG  1 
ATOM   2541 C  CD  . LYS B  1 35  ? 48.769 -16.279 -36.853 1.00 41.28  ? 34  LYS B CD  1 
ATOM   2542 N  N   . THR B  1 36  ? 49.450 -11.027 -38.495 1.00 17.35  ? 35  THR B N   1 
ATOM   2543 C  CA  . THR B  1 36  ? 49.028 -10.099 -39.524 1.00 16.94  ? 35  THR B CA  1 
ATOM   2544 C  C   . THR B  1 36  ? 48.455 -10.778 -40.775 1.00 18.68  ? 35  THR B C   1 
ATOM   2545 O  O   . THR B  1 36  ? 47.709 -10.091 -41.525 1.00 24.77  ? 35  THR B O   1 
ATOM   2546 C  CB  . THR B  1 36  ? 50.126 -9.116  -39.982 1.00 18.59  ? 35  THR B CB  1 
ATOM   2547 O  OG1 . THR B  1 36  ? 51.286 -9.871  -40.412 1.00 18.61  ? 35  THR B OG1 1 
ATOM   2548 C  CG2 . THR B  1 36  ? 50.555 -8.223  -38.752 1.00 21.58  ? 35  THR B CG2 1 
ATOM   2549 N  N   . SER B  1 37  ? 48.754 -12.042 -41.023 1.00 19.58  ? 36  SER B N   1 
ATOM   2550 C  CA  . SER B  1 37  ? 48.112 -12.691 -42.175 1.00 21.13  ? 36  SER B CA  1 
ATOM   2551 C  C   . SER B  1 37  ? 46.632 -12.921 -41.873 1.00 20.44  ? 36  SER B C   1 
ATOM   2552 O  O   . SER B  1 37  ? 45.920 -13.283 -42.809 1.00 24.74  ? 36  SER B O   1 
ATOM   2553 C  CB  . SER B  1 37  ? 48.745 -14.020 -42.475 1.00 25.73  ? 36  SER B CB  1 
ATOM   2554 O  OG  . SER B  1 37  ? 48.716 -14.833 -41.301 1.00 27.83  ? 36  SER B OG  1 
ATOM   2555 N  N   A GLU B  1 38  ? 46.131 -12.695 -40.646 0.50 20.29  ? 37  GLU B N   1 
ATOM   2556 N  N   B GLU B  1 38  ? 46.184 -12.742 -40.614 0.50 19.32  ? 37  GLU B N   1 
ATOM   2557 C  CA  A GLU B  1 38  ? 44.735 -12.987 -40.312 0.50 21.36  ? 37  GLU B CA  1 
ATOM   2558 C  CA  B GLU B  1 38  ? 44.830 -13.042 -40.180 0.50 17.15  ? 37  GLU B CA  1 
ATOM   2559 C  C   A GLU B  1 38  ? 43.975 -11.724 -39.982 0.50 20.36  ? 37  GLU B C   1 
ATOM   2560 C  C   B GLU B  1 38  ? 44.032 -11.765 -39.920 0.50 19.49  ? 37  GLU B C   1 
ATOM   2561 O  O   A GLU B  1 38  ? 42.817 -11.784 -39.631 0.50 25.76  ? 37  GLU B O   1 
ATOM   2562 O  O   B GLU B  1 38  ? 42.878 -11.869 -39.604 0.50 18.34  ? 37  GLU B O   1 
ATOM   2563 C  CB  A GLU B  1 38  ? 44.627 -13.946 -39.111 0.50 28.85  ? 37  GLU B CB  1 
ATOM   2564 C  CB  B GLU B  1 38  ? 44.789 -14.017 -38.938 0.50 19.44  ? 37  GLU B CB  1 
ATOM   2565 C  CG  A GLU B  1 38  ? 44.961 -15.376 -39.463 0.50 31.91  ? 37  GLU B CG  1 
ATOM   2566 C  CG  B GLU B  1 38  ? 45.572 -15.308 -39.163 0.50 20.25  ? 37  GLU B CG  1 
ATOM   2567 C  CD  A GLU B  1 38  ? 44.812 -16.307 -38.285 0.50 41.11  ? 37  GLU B CD  1 
ATOM   2568 C  CD  B GLU B  1 38  ? 45.268 -15.960 -40.487 0.50 25.67  ? 37  GLU B CD  1 
ATOM   2569 O  OE1 A GLU B  1 38  ? 43.844 -16.164 -37.504 0.50 46.88  ? 37  GLU B OE1 1 
ATOM   2570 O  OE1 B GLU B  1 38  ? 44.118 -16.236 -40.734 0.50 25.58  ? 37  GLU B OE1 1 
ATOM   2571 O  OE2 A GLU B  1 38  ? 45.671 -17.206 -38.173 0.50 54.72  ? 37  GLU B OE2 1 
ATOM   2572 O  OE2 B GLU B  1 38  ? 46.220 -16.260 -41.279 0.50 29.06  ? 37  GLU B OE2 1 
ATOM   2573 N  N   . THR B  1 39  ? 44.603 -10.566 -40.055 1.00 18.28  ? 38  THR B N   1 
ATOM   2574 C  CA  . THR B  1 39  ? 43.855 -9.365  -39.841 1.00 19.19  ? 38  THR B CA  1 
ATOM   2575 C  C   . THR B  1 39  ? 42.947 -9.098  -40.971 1.00 22.34  ? 38  THR B C   1 
ATOM   2576 O  O   . THR B  1 39  ? 43.150 -9.551  -42.075 1.00 26.76  ? 38  THR B O   1 
ATOM   2577 C  CB  . THR B  1 39  ? 44.788 -8.155  -39.582 1.00 17.89  ? 38  THR B CB  1 
ATOM   2578 O  OG1 . THR B  1 39  ? 45.661 -8.042  -40.685 1.00 19.63  ? 38  THR B OG1 1 
ATOM   2579 C  CG2 . THR B  1 39  ? 45.544 -8.444  -38.306 1.00 17.33  ? 38  THR B CG2 1 
ATOM   2580 N  N   . LYS B  1 40  ? 41.888 -8.305  -40.737 1.00 22.19  ? 39  LYS B N   1 
ATOM   2581 C  CA  . LYS B  1 40  ? 40.965 -7.930  -41.770 1.00 21.65  ? 39  LYS B CA  1 
ATOM   2582 C  C   . LYS B  1 40  ? 41.017 -6.393  -41.908 1.00 23.03  ? 39  LYS B C   1 
ATOM   2583 O  O   . LYS B  1 40  ? 40.658 -5.681  -40.931 1.00 21.36  ? 39  LYS B O   1 
ATOM   2584 C  CB  . LYS B  1 40  ? 39.504 -8.461  -41.415 1.00 28.32  ? 39  LYS B CB  1 
ATOM   2585 C  CG  . LYS B  1 40  ? 39.540 -10.007 -41.243 1.00 33.22  ? 39  LYS B CG  1 
ATOM   2586 N  N   . HIS B  1 41  ? 41.281 -5.882  -43.155 1.00 26.58  ? 40  HIS B N   1 
ATOM   2587 C  CA  . HIS B  1 41  ? 41.154 -4.453  -43.430 1.00 27.71  ? 40  HIS B CA  1 
ATOM   2588 C  C   . HIS B  1 41  ? 39.704 -4.090  -43.433 1.00 30.59  ? 40  HIS B C   1 
ATOM   2589 O  O   . HIS B  1 41  ? 38.899 -4.674  -44.083 1.00 198.69 ? 40  HIS B O   1 
ATOM   2590 C  CB  . HIS B  1 41  ? 41.934 -4.033  -44.696 1.00 29.45  ? 40  HIS B CB  1 
ATOM   2591 C  CG  . HIS B  1 41  ? 41.797 -2.576  -45.049 1.00 36.31  ? 40  HIS B CG  1 
ATOM   2592 N  ND1 . HIS B  1 41  ? 42.072 -1.495  -44.243 1.00 35.31  ? 40  HIS B ND1 1 
ATOM   2593 C  CD2 . HIS B  1 41  ? 41.333 -2.020  -46.195 1.00 62.58  ? 40  HIS B CD2 1 
ATOM   2594 C  CE1 . HIS B  1 41  ? 41.835 -0.346  -44.867 1.00 33.74  ? 40  HIS B CE1 1 
ATOM   2595 N  NE2 . HIS B  1 41  ? 41.367 -0.646  -46.049 1.00 57.13  ? 40  HIS B NE2 1 
ATOM   2596 N  N   . ASP B  1 42  ? 39.429 -3.071  -42.601 1.00 21.56  ? 41  ASP B N   1 
ATOM   2597 C  CA  . ASP B  1 42  ? 38.074 -2.622  -42.431 1.00 21.35  ? 41  ASP B CA  1 
ATOM   2598 C  C   . ASP B  1 42  ? 37.947 -1.182  -42.959 1.00 25.61  ? 41  ASP B C   1 
ATOM   2599 O  O   . ASP B  1 42  ? 38.413 -0.276  -42.279 1.00 25.55  ? 41  ASP B O   1 
ATOM   2600 C  CB  . ASP B  1 42  ? 37.536 -2.839  -41.009 1.00 24.21  ? 41  ASP B CB  1 
ATOM   2601 C  CG  . ASP B  1 42  ? 36.085 -2.411  -40.828 1.00 25.65  ? 41  ASP B CG  1 
ATOM   2602 O  OD1 . ASP B  1 42  ? 35.508 -1.791  -41.793 1.00 28.61  ? 41  ASP B OD1 1 
ATOM   2603 O  OD2 . ASP B  1 42  ? 35.460 -2.763  -39.792 1.00 37.95  ? 41  ASP B OD2 1 
ATOM   2604 N  N   . THR B  1 43  ? 37.343 -0.983  -44.127 1.00 36.58  ? 42  THR B N   1 
ATOM   2605 C  CA  . THR B  1 43  ? 37.265 0.373   -44.688 1.00 39.35  ? 42  THR B CA  1 
ATOM   2606 C  C   . THR B  1 43  ? 36.339 1.298   -43.945 1.00 31.35  ? 42  THR B C   1 
ATOM   2607 O  O   . THR B  1 43  ? 36.300 2.482   -44.239 1.00 45.17  ? 42  THR B O   1 
ATOM   2608 C  CB  . THR B  1 43  ? 36.712 0.343   -46.157 1.00 71.79  ? 42  THR B CB  1 
ATOM   2609 O  OG1 . THR B  1 43  ? 35.322 -0.056  -46.162 1.00 112.88 ? 42  THR B OG1 1 
ATOM   2610 C  CG2 . THR B  1 43  ? 37.509 -0.630  -46.960 1.00 72.37  ? 42  THR B CG2 1 
ATOM   2611 N  N   . SER B  1 44  ? 35.525 0.806   -43.015 1.00 28.09  ? 43  SER B N   1 
ATOM   2612 C  CA  . SER B  1 44  ? 34.630 1.740   -42.297 1.00 32.71  ? 43  SER B CA  1 
ATOM   2613 C  C   . SER B  1 44  ? 35.389 2.380   -41.110 1.00 28.11  ? 43  SER B C   1 
ATOM   2614 O  O   . SER B  1 44  ? 34.857 3.287   -40.413 1.00 32.03  ? 43  SER B O   1 
ATOM   2615 C  CB  . SER B  1 44  ? 33.390 1.025   -41.783 1.00 48.27  ? 43  SER B CB  1 
ATOM   2616 O  OG  . SER B  1 44  ? 33.698 0.246   -40.649 1.00 35.30  ? 43  SER B OG  1 
ATOM   2617 N  N   . LEU B  1 45  ? 36.582 1.826   -40.761 1.00 26.45  ? 44  LEU B N   1 
ATOM   2618 C  CA  . LEU B  1 45  ? 37.302 2.500   -39.660 1.00 25.55  ? 44  LEU B CA  1 
ATOM   2619 C  C   . LEU B  1 45  ? 37.749 3.867   -40.104 1.00 27.81  ? 44  LEU B C   1 
ATOM   2620 O  O   . LEU B  1 45  ? 38.249 4.092   -41.225 1.00 42.88  ? 44  LEU B O   1 
ATOM   2621 C  CB  . LEU B  1 45  ? 38.593 1.704   -39.387 1.00 25.63  ? 44  LEU B CB  1 
ATOM   2622 C  CG  . LEU B  1 45  ? 38.332 0.394   -38.699 1.00 21.88  ? 44  LEU B CG  1 
ATOM   2623 C  CD1 . LEU B  1 45  ? 39.638 -0.489  -38.642 1.00 22.07  ? 44  LEU B CD1 1 
ATOM   2624 C  CD2 . LEU B  1 45  ? 37.788 0.526   -37.285 1.00 20.93  ? 44  LEU B CD2 1 
ATOM   2625 N  N   . LYS B  1 46  ? 37.626 4.788   -39.209 1.00 26.38  ? 45  LYS B N   1 
ATOM   2626 C  CA  . LYS B  1 46  ? 38.016 6.208   -39.434 1.00 25.60  ? 45  LYS B CA  1 
ATOM   2627 C  C   . LYS B  1 46  ? 39.388 6.399   -38.844 1.00 21.62  ? 45  LYS B C   1 
ATOM   2628 O  O   . LYS B  1 46  ? 39.834 5.602   -38.000 1.00 22.88  ? 45  LYS B O   1 
ATOM   2629 C  CB  . LYS B  1 46  ? 37.037 7.169   -38.741 1.00 27.74  ? 45  LYS B CB  1 
ATOM   2630 C  CG  . LYS B  1 46  ? 35.572 7.146   -39.344 1.00 37.08  ? 45  LYS B CG  1 
ATOM   2631 N  N   . PRO B  1 47  ? 40.094 7.507   -39.252 1.00 24.64  ? 46  PRO B N   1 
ATOM   2632 C  CA  . PRO B  1 47  ? 41.362 7.771   -38.531 1.00 22.36  ? 46  PRO B CA  1 
ATOM   2633 C  C   . PRO B  1 47  ? 41.116 8.059   -37.098 1.00 22.10  ? 46  PRO B C   1 
ATOM   2634 O  O   . PRO B  1 47  ? 40.007 8.520   -36.620 1.00 23.30  ? 46  PRO B O   1 
ATOM   2635 C  CB  . PRO B  1 47  ? 41.861 9.075   -39.179 1.00 26.30  ? 46  PRO B CB  1 
ATOM   2636 C  CG  . PRO B  1 47  ? 41.163 9.139   -40.593 1.00 27.15  ? 46  PRO B CG  1 
ATOM   2637 C  CD  . PRO B  1 47  ? 39.819 8.548   -40.309 1.00 25.17  ? 46  PRO B CD  1 
ATOM   2638 N  N   . ILE B  1 48  ? 42.146 7.705   -36.298 1.00 21.82  ? 47  ILE B N   1 
ATOM   2639 C  CA  . ILE B  1 48  ? 42.115 8.047   -34.854 1.00 23.48  ? 47  ILE B CA  1 
ATOM   2640 C  C   . ILE B  1 48  ? 42.358 9.508   -34.722 1.00 21.69  ? 47  ILE B C   1 
ATOM   2641 O  O   . ILE B  1 48  ? 43.250 10.043  -35.377 1.00 28.32  ? 47  ILE B O   1 
ATOM   2642 C  CB  . ILE B  1 48  ? 43.191 7.275   -34.091 1.00 29.16  ? 47  ILE B CB  1 
ATOM   2643 C  CG1 . ILE B  1 48  ? 42.889 5.813   -34.119 1.00 30.77  ? 47  ILE B CG1 1 
ATOM   2644 C  CG2 . ILE B  1 48  ? 43.489 7.916   -32.707 1.00 23.23  ? 47  ILE B CG2 1 
ATOM   2645 C  CD1 . ILE B  1 48  ? 41.695 5.404   -33.237 1.00 29.12  ? 47  ILE B CD1 1 
ATOM   2646 N  N   . SER B  1 49  ? 41.570 10.142  -33.850 1.00 19.76  ? 48  SER B N   1 
ATOM   2647 C  CA  . SER B  1 49  ? 41.745 11.594  -33.517 1.00 22.20  ? 48  SER B CA  1 
ATOM   2648 C  C   . SER B  1 49  ? 42.065 11.691  -32.011 1.00 19.86  ? 48  SER B C   1 
ATOM   2649 O  O   . SER B  1 49  ? 41.123 11.343  -31.239 1.00 23.12  ? 48  SER B O   1 
ATOM   2650 C  CB  . SER B  1 49  ? 40.437 12.395  -33.905 1.00 26.84  ? 48  SER B CB  1 
ATOM   2651 O  OG  . SER B  1 49  ? 40.352 13.638  -33.265 1.00 33.09  ? 48  SER B OG  1 
ATOM   2652 N  N   . VAL B  1 50  ? 43.221 12.261  -31.634 1.00 18.10  ? 49  VAL B N   1 
ATOM   2653 C  CA  . VAL B  1 50  ? 43.470 12.516  -30.247 1.00 16.58  ? 49  VAL B CA  1 
ATOM   2654 C  C   . VAL B  1 50  ? 43.603 14.011  -30.110 1.00 17.43  ? 49  VAL B C   1 
ATOM   2655 O  O   . VAL B  1 50  ? 44.265 14.685  -30.912 1.00 17.70  ? 49  VAL B O   1 
ATOM   2656 C  CB  . VAL B  1 50  ? 44.639 11.789  -29.653 1.00 18.71  ? 49  VAL B CB  1 
ATOM   2657 C  CG1 . VAL B  1 50  ? 44.335 10.322  -29.646 1.00 20.32  ? 49  VAL B CG1 1 
ATOM   2658 C  CG2 . VAL B  1 50  ? 45.926 12.050  -30.309 1.00 26.33  ? 49  VAL B CG2 1 
ATOM   2659 N  N   . SER B  1 51  ? 43.002 14.563  -29.048 1.00 17.56  ? 50  SER B N   1 
ATOM   2660 C  CA  . SER B  1 51  ? 43.172 16.013  -28.764 1.00 19.82  ? 50  SER B CA  1 
ATOM   2661 C  C   . SER B  1 51  ? 43.247 16.151  -27.257 1.00 16.00  ? 50  SER B C   1 
ATOM   2662 O  O   . SER B  1 51  ? 42.220 15.977  -26.562 1.00 17.03  ? 50  SER B O   1 
ATOM   2663 C  CB  . SER B  1 51  ? 41.940 16.754  -29.327 1.00 23.73  ? 50  SER B CB  1 
ATOM   2664 O  OG  . SER B  1 51  ? 42.163 18.081  -29.042 1.00 27.26  ? 50  SER B OG  1 
ATOM   2665 N  N   . TYR B  1 52  ? 44.476 16.269  -26.755 1.00 17.26  ? 51  TYR B N   1 
ATOM   2666 C  CA  . TYR B  1 52  ? 44.703 16.281  -25.314 1.00 15.38  ? 51  TYR B CA  1 
ATOM   2667 C  C   . TYR B  1 52  ? 45.183 17.630  -24.862 1.00 16.74  ? 51  TYR B C   1 
ATOM   2668 O  O   . TYR B  1 52  ? 46.071 18.186  -25.456 1.00 23.86  ? 51  TYR B O   1 
ATOM   2669 C  CB  . TYR B  1 52  ? 45.780 15.257  -24.926 1.00 14.92  ? 51  TYR B CB  1 
ATOM   2670 C  CG  . TYR B  1 52  ? 45.519 13.802  -25.282 1.00 13.77  ? 51  TYR B CG  1 
ATOM   2671 C  CD1 . TYR B  1 52  ? 44.233 13.278  -25.320 1.00 14.09  ? 51  TYR B CD1 1 
ATOM   2672 C  CD2 . TYR B  1 52  ? 46.580 12.946  -25.553 1.00 14.05  ? 51  TYR B CD2 1 
ATOM   2673 C  CE1 . TYR B  1 52  ? 44.014 11.943  -25.635 1.00 14.48  ? 51  TYR B CE1 1 
ATOM   2674 C  CE2 . TYR B  1 52  ? 46.372 11.616  -25.867 1.00 13.10  ? 51  TYR B CE2 1 
ATOM   2675 C  CZ  . TYR B  1 52  ? 45.090 11.115  -25.908 1.00 12.87  ? 51  TYR B CZ  1 
ATOM   2676 O  OH  . TYR B  1 52  ? 44.900 9.781   -26.222 1.00 13.74  ? 51  TYR B OH  1 
ATOM   2677 N  N   . ASN B  1 53  ? 44.634 18.143  -23.778 1.00 14.47  ? 52  ASN B N   1 
ATOM   2678 C  CA  . ASN B  1 53  ? 45.061 19.471  -23.301 1.00 16.28  ? 52  ASN B CA  1 
ATOM   2679 C  C   . ASN B  1 53  ? 46.122 19.249  -22.236 1.00 13.51  ? 52  ASN B C   1 
ATOM   2680 O  O   . ASN B  1 53  ? 45.854 18.515  -21.261 1.00 13.09  ? 52  ASN B O   1 
ATOM   2681 C  CB  . ASN B  1 53  ? 43.793 20.104  -22.695 1.00 17.80  ? 52  ASN B CB  1 
ATOM   2682 C  CG  . ASN B  1 53  ? 43.995 21.486  -22.225 1.00 17.43  ? 52  ASN B CG  1 
ATOM   2683 O  OD1 . ASN B  1 53  ? 45.076 21.821  -21.705 1.00 17.22  ? 52  ASN B OD1 1 
ATOM   2684 N  ND2 . ASN B  1 53  ? 42.960 22.307  -22.274 1.00 20.25  ? 52  ASN B ND2 1 
ATOM   2685 N  N   . PRO B  1 54  ? 47.347 19.782  -22.393 1.00 12.96  ? 53  PRO B N   1 
ATOM   2686 C  CA  . PRO B  1 54  ? 48.414 19.496  -21.404 1.00 13.59  ? 53  PRO B CA  1 
ATOM   2687 C  C   . PRO B  1 54  ? 48.021 19.924  -20.004 1.00 12.55  ? 53  PRO B C   1 
ATOM   2688 O  O   . PRO B  1 54  ? 48.611 19.408  -19.020 1.00 12.06  ? 53  PRO B O   1 
ATOM   2689 C  CB  . PRO B  1 54  ? 49.634 20.252  -21.953 1.00 15.80  ? 53  PRO B CB  1 
ATOM   2690 C  CG  . PRO B  1 54  ? 48.980 21.387  -22.758 1.00 18.14  ? 53  PRO B CG  1 
ATOM   2691 C  CD  . PRO B  1 54  ? 47.784 20.745  -23.413 1.00 15.49  ? 53  PRO B CD  1 
ATOM   2692 N  N   . ALA B  1 55  ? 47.105 20.896  -19.858 1.00 13.64  ? 54  ALA B N   1 
ATOM   2693 C  CA  . ALA B  1 55  ? 46.735 21.325  -18.492 1.00 15.25  ? 54  ALA B CA  1 
ATOM   2694 C  C   . ALA B  1 55  ? 45.946 20.277  -17.761 1.00 12.71  ? 54  ALA B C   1 
ATOM   2695 O  O   . ALA B  1 55  ? 45.723 20.448  -16.557 1.00 14.88  ? 54  ALA B O   1 
ATOM   2696 C  CB  . ALA B  1 55  ? 45.952 22.645  -18.628 1.00 18.89  ? 54  ALA B CB  1 
ATOM   2697 N  N   . THR B  1 56  ? 45.495 19.196  -18.419 1.00 12.63  ? 55  THR B N   1 
ATOM   2698 C  CA  . THR B  1 56  ? 44.828 18.152  -17.714 1.00 11.44  ? 55  THR B CA  1 
ATOM   2699 C  C   . THR B  1 56  ? 45.767 17.179  -16.972 1.00 9.89   ? 55  THR B C   1 
ATOM   2700 O  O   . THR B  1 56  ? 45.311 16.399  -16.150 1.00 10.90  ? 55  THR B O   1 
ATOM   2701 C  CB  . THR B  1 56  ? 43.822 17.334  -18.593 1.00 12.86  ? 55  THR B CB  1 
ATOM   2702 O  OG1 . THR B  1 56  ? 44.544 16.750  -19.714 1.00 12.29  ? 55  THR B OG1 1 
ATOM   2703 C  CG2 . THR B  1 56  ? 42.696 18.207  -19.136 1.00 14.39  ? 55  THR B CG2 1 
ATOM   2704 N  N   . ALA B  1 57  ? 47.077 17.216  -17.300 1.00 10.09  ? 56  ALA B N   1 
ATOM   2705 C  CA  . ALA B  1 57  ? 47.988 16.312  -16.535 1.00 10.07  ? 56  ALA B CA  1 
ATOM   2706 C  C   . ALA B  1 57  ? 47.892 16.678  -15.038 1.00 9.19   ? 56  ALA B C   1 
ATOM   2707 O  O   . ALA B  1 57  ? 47.917 17.863  -14.715 1.00 9.78   ? 56  ALA B O   1 
ATOM   2708 C  CB  . ALA B  1 57  ? 49.385 16.471  -17.068 1.00 10.76  ? 56  ALA B CB  1 
ATOM   2709 N  N   A LYS B  1 58  ? 47.783 15.681  -14.158 0.50 9.20   ? 57  LYS B N   1 
ATOM   2710 N  N   B LYS B  1 58  ? 47.860 15.655  -14.196 0.50 9.58   ? 57  LYS B N   1 
ATOM   2711 C  CA  A LYS B  1 58  ? 47.831 16.065  -12.693 0.50 10.11  ? 57  LYS B CA  1 
ATOM   2712 C  CA  B LYS B  1 58  ? 47.634 15.886  -12.751 0.50 10.88  ? 57  LYS B CA  1 
ATOM   2713 C  C   A LYS B  1 58  ? 48.843 15.357  -11.866 0.50 9.05   ? 57  LYS B C   1 
ATOM   2714 C  C   B LYS B  1 58  ? 48.755 15.331  -11.884 0.50 9.30   ? 57  LYS B C   1 
ATOM   2715 O  O   A LYS B  1 58  ? 49.375 16.025  -10.959 0.50 10.89  ? 57  LYS B O   1 
ATOM   2716 O  O   B LYS B  1 58  ? 49.309 16.066  -11.024 0.50 11.21  ? 57  LYS B O   1 
ATOM   2717 C  CB  A LYS B  1 58  ? 46.481 16.037  -11.967 0.50 11.95  ? 57  LYS B CB  1 
ATOM   2718 C  CB  B LYS B  1 58  ? 46.276 15.233  -12.454 0.50 14.34  ? 57  LYS B CB  1 
ATOM   2719 C  CG  A LYS B  1 58  ? 45.716 14.749  -12.122 0.50 11.09  ? 57  LYS B CG  1 
ATOM   2720 C  CG  B LYS B  1 58  ? 45.790 15.504  -11.086 0.50 14.32  ? 57  LYS B CG  1 
ATOM   2721 C  CD  A LYS B  1 58  ? 44.477 14.735  -11.219 0.50 11.19  ? 57  LYS B CD  1 
ATOM   2722 C  CD  B LYS B  1 58  ? 44.303 15.201  -10.948 0.50 18.55  ? 57  LYS B CD  1 
ATOM   2723 C  CE  A LYS B  1 58  ? 43.456 13.623  -11.595 0.50 16.70  ? 57  LYS B CE  1 
ATOM   2724 C  CE  B LYS B  1 58  ? 43.788 13.840  -11.351 0.50 19.81  ? 57  LYS B CE  1 
ATOM   2725 N  NZ  A LYS B  1 58  ? 42.283 13.717  -10.601 0.50 22.00  ? 57  LYS B NZ  1 
ATOM   2726 N  NZ  B LYS B  1 58  ? 42.445 13.672  -10.642 0.50 21.92  ? 57  LYS B NZ  1 
ATOM   2727 N  N   . GLU B  1 59  ? 49.050 14.034  -11.946 1.00 8.74   ? 58  GLU B N   1 
ATOM   2728 C  CA  . GLU B  1 59  ? 49.779 13.373  -10.881 1.00 8.95   ? 58  GLU B CA  1 
ATOM   2729 C  C   . GLU B  1 59  ? 50.479 12.140  -11.411 1.00 7.85   ? 58  GLU B C   1 
ATOM   2730 O  O   . GLU B  1 59  ? 49.921 11.478  -12.304 1.00 10.44  ? 58  GLU B O   1 
ATOM   2731 C  CB  . GLU B  1 59  ? 48.828 12.995  -9.728  1.00 10.34  ? 58  GLU B CB  1 
ATOM   2732 C  CG  . GLU B  1 59  ? 49.465 12.619  -8.435  1.00 12.17  ? 58  GLU B CG  1 
ATOM   2733 C  CD  . GLU B  1 59  ? 48.496 12.532  -7.298  1.00 12.29  ? 58  GLU B CD  1 
ATOM   2734 O  OE1 . GLU B  1 59  ? 48.865 12.785  -6.155  1.00 16.24  ? 58  GLU B OE1 1 
ATOM   2735 O  OE2 . GLU B  1 59  ? 47.375 12.029  -7.515  1.00 15.04  ? 58  GLU B OE2 1 
ATOM   2736 N  N   . ILE B  1 60  ? 51.607 11.795  -10.840 1.00 7.80   ? 59  ILE B N   1 
ATOM   2737 C  CA  . ILE B  1 60  ? 52.291 10.536  -11.137 1.00 7.98   ? 59  ILE B CA  1 
ATOM   2738 C  C   . ILE B  1 60  ? 52.306 9.724   -9.831  1.00 7.04   ? 59  ILE B C   1 
ATOM   2739 O  O   . ILE B  1 60  ? 52.571 10.306  -8.765  1.00 8.41   ? 59  ILE B O   1 
ATOM   2740 C  CB  . ILE B  1 60  ? 53.667 10.790  -11.761 1.00 7.62   ? 59  ILE B CB  1 
ATOM   2741 C  CG1 . ILE B  1 60  ? 54.279 9.482   -12.255 1.00 8.53   ? 59  ILE B CG1 1 
ATOM   2742 C  CG2 . ILE B  1 60  ? 54.630 11.551  -10.795 1.00 9.25   ? 59  ILE B CG2 1 
ATOM   2743 C  CD1 . ILE B  1 60  ? 55.543 9.680   -13.129 1.00 10.13  ? 59  ILE B CD1 1 
ATOM   2744 N  N   . ILE B  1 61  ? 52.034 8.439   -9.905  1.00 7.06   ? 60  ILE B N   1 
ATOM   2745 C  CA  . ILE B  1 61  ? 51.790 7.596   -8.748  1.00 7.79   ? 60  ILE B CA  1 
ATOM   2746 C  C   . ILE B  1 61  ? 52.488 6.274   -8.891  1.00 6.83   ? 60  ILE B C   1 
ATOM   2747 O  O   . ILE B  1 61  ? 52.356 5.615   -9.934  1.00 7.68   ? 60  ILE B O   1 
ATOM   2748 C  CB  . ILE B  1 61  ? 50.281 7.334   -8.563  1.00 9.05   ? 60  ILE B CB  1 
ATOM   2749 C  CG1 . ILE B  1 61  ? 49.437 8.584   -8.545  1.00 11.20  ? 60  ILE B CG1 1 
ATOM   2750 C  CG2 . ILE B  1 61  ? 50.019 6.438   -7.335  1.00 11.00  ? 60  ILE B CG2 1 
ATOM   2751 C  CD1 . ILE B  1 61  ? 47.942 8.351   -8.790  1.00 14.97  ? 60  ILE B CD1 1 
ATOM   2752 N  N   . ASN B  1 62  ? 53.188 5.817   -7.841  1.00 7.57   ? 61  ASN B N   1 
ATOM   2753 C  CA  . ASN B  1 62  ? 53.718 4.466   -7.787  1.00 7.76   ? 61  ASN B CA  1 
ATOM   2754 C  C   . ASN B  1 62  ? 52.647 3.551   -7.187  1.00 7.38   ? 61  ASN B C   1 
ATOM   2755 O  O   . ASN B  1 62  ? 52.250 3.707   -6.032  1.00 8.47   ? 61  ASN B O   1 
ATOM   2756 C  CB  . ASN B  1 62  ? 54.990 4.471   -6.940  1.00 8.43   ? 61  ASN B CB  1 
ATOM   2757 C  CG  . ASN B  1 62  ? 55.660 3.121   -6.842  1.00 7.58   ? 61  ASN B CG  1 
ATOM   2758 O  OD1 . ASN B  1 62  ? 54.945 2.086   -6.770  1.00 9.00   ? 61  ASN B OD1 1 
ATOM   2759 N  ND2 . ASN B  1 62  ? 56.986 3.073   -6.761  1.00 8.71   ? 61  ASN B ND2 1 
ATOM   2760 N  N   . VAL B  1 63  ? 52.134 2.647   -8.026  1.00 7.67   ? 62  VAL B N   1 
ATOM   2761 C  CA  . VAL B  1 63  ? 51.049 1.711   -7.622  1.00 9.08   ? 62  VAL B CA  1 
ATOM   2762 C  C   . VAL B  1 63  ? 51.590 0.346   -7.284  1.00 8.86   ? 62  VAL B C   1 
ATOM   2763 O  O   . VAL B  1 63  ? 50.819 -0.624  -7.202  1.00 10.82  ? 62  VAL B O   1 
ATOM   2764 C  CB  . VAL B  1 63  ? 49.897 1.702   -8.652  1.00 9.32   ? 62  VAL B CB  1 
ATOM   2765 C  CG1 . VAL B  1 63  ? 49.263 3.043   -8.769  1.00 11.48  ? 62  VAL B CG1 1 
ATOM   2766 C  CG2 . VAL B  1 63  ? 50.366 1.182   -10.035 1.00 10.92  ? 62  VAL B CG2 1 
ATOM   2767 N  N   . GLY B  1 64  ? 52.908 0.219   -7.017  1.00 8.39   ? 63  GLY B N   1 
ATOM   2768 C  CA  . GLY B  1 64  ? 53.425 -1.007  -6.505  1.00 9.26   ? 63  GLY B CA  1 
ATOM   2769 C  C   . GLY B  1 64  ? 53.894 -1.965  -7.574  1.00 8.87   ? 63  GLY B C   1 
ATOM   2770 O  O   . GLY B  1 64  ? 55.027 -2.464  -7.578  1.00 12.17  ? 63  GLY B O   1 
ATOM   2771 N  N   . HIS B  1 65  ? 53.052 -2.220  -8.574  1.00 8.54   ? 64  HIS B N   1 
ATOM   2772 C  CA  . HIS B  1 65  ? 53.406 -3.068  -9.706  1.00 9.08   ? 64  HIS B CA  1 
ATOM   2773 C  C   . HIS B  1 65  ? 53.782 -2.261  -10.945 1.00 8.29   ? 64  HIS B C   1 
ATOM   2774 O  O   . HIS B  1 65  ? 54.293 -2.828  -11.917 1.00 9.20   ? 64  HIS B O   1 
ATOM   2775 C  CB  . HIS B  1 65  ? 52.206 -4.008  -10.047 1.00 9.94   ? 64  HIS B CB  1 
ATOM   2776 C  CG  . HIS B  1 65  ? 50.989 -3.309  -10.429 1.00 9.21   ? 64  HIS B CG  1 
ATOM   2777 N  ND1 . HIS B  1 65  ? 50.716 -2.907  -11.726 1.00 10.32  ? 64  HIS B ND1 1 
ATOM   2778 C  CD2 . HIS B  1 65  ? 49.957 -2.887  -9.630  1.00 11.09  ? 64  HIS B CD2 1 
ATOM   2779 C  CE1 . HIS B  1 65  ? 49.548 -2.260  -11.719 1.00 10.57  ? 64  HIS B CE1 1 
ATOM   2780 N  NE2 . HIS B  1 65  ? 49.065 -2.232  -10.445 1.00 11.76  ? 64  HIS B NE2 1 
ATOM   2781 N  N   . SER B  1 66  ? 53.515 -0.950  -10.904 1.00 8.07   ? 65  SER B N   1 
ATOM   2782 C  CA  . SER B  1 66  ? 53.724 -0.081  -12.024 1.00 7.79   ? 65  SER B CA  1 
ATOM   2783 C  C   . SER B  1 66  ? 53.705 1.349   -11.502 1.00 7.39   ? 65  SER B C   1 
ATOM   2784 O  O   . SER B  1 66  ? 53.670 1.586   -10.297 1.00 8.07   ? 65  SER B O   1 
ATOM   2785 C  CB  . SER B  1 66  ? 52.620 -0.333  -13.046 1.00 9.46   ? 65  SER B CB  1 
ATOM   2786 O  OG  . SER B  1 66  ? 52.978 0.328   -14.275 1.00 9.85   ? 65  SER B OG  1 
ATOM   2787 N  N   . PHE B  1 67  ? 53.652 2.322   -12.429 1.00 7.30   ? 66  PHE B N   1 
ATOM   2788 C  CA  . PHE B  1 67  ? 53.374 3.708   -12.099 1.00 7.05   ? 66  PHE B CA  1 
ATOM   2789 C  C   . PHE B  1 67  ? 52.395 4.235   -13.116 1.00 6.87   ? 66  PHE B C   1 
ATOM   2790 O  O   . PHE B  1 67  ? 52.359 3.766   -14.260 1.00 7.88   ? 66  PHE B O   1 
ATOM   2791 C  CB  . PHE B  1 67  ? 54.603 4.571   -11.996 1.00 7.45   ? 66  PHE B CB  1 
ATOM   2792 C  CG  . PHE B  1 67  ? 55.264 4.861   -13.320 1.00 7.44   ? 66  PHE B CG  1 
ATOM   2793 C  CD1 . PHE B  1 67  ? 56.164 3.977   -13.898 1.00 8.86   ? 66  PHE B CD1 1 
ATOM   2794 C  CD2 . PHE B  1 67  ? 54.920 6.015   -14.028 1.00 8.72   ? 66  PHE B CD2 1 
ATOM   2795 C  CE1 . PHE B  1 67  ? 56.737 4.280   -15.139 1.00 10.17  ? 66  PHE B CE1 1 
ATOM   2796 C  CE2 . PHE B  1 67  ? 55.497 6.310   -15.266 1.00 9.95   ? 66  PHE B CE2 1 
ATOM   2797 C  CZ  . PHE B  1 67  ? 56.412 5.449   -15.807 1.00 10.10  ? 66  PHE B CZ  1 
ATOM   2798 N  N   . HIS B  1 68  ? 51.586 5.201   -12.699 1.00 7.65   ? 67  HIS B N   1 
ATOM   2799 C  CA  . HIS B  1 68  ? 50.593 5.796   -13.574 1.00 8.83   ? 67  HIS B CA  1 
ATOM   2800 C  C   . HIS B  1 68  ? 50.698 7.296   -13.573 1.00 7.84   ? 67  HIS B C   1 
ATOM   2801 O  O   . HIS B  1 68  ? 51.045 7.881   -12.565 1.00 8.91   ? 67  HIS B O   1 
ATOM   2802 C  CB  . HIS B  1 68  ? 49.187 5.567   -13.023 1.00 10.25  ? 67  HIS B CB  1 
ATOM   2803 C  CG  . HIS B  1 68  ? 48.748 4.142   -12.973 1.00 10.55  ? 67  HIS B CG  1 
ATOM   2804 N  ND1 . HIS B  1 68  ? 47.632 3.760   -12.254 1.00 13.83  ? 67  HIS B ND1 1 
ATOM   2805 C  CD2 . HIS B  1 68  ? 49.249 3.021   -13.554 1.00 11.71  ? 67  HIS B CD2 1 
ATOM   2806 C  CE1 . HIS B  1 68  ? 47.447 2.462   -12.373 1.00 13.74  ? 67  HIS B CE1 1 
ATOM   2807 N  NE2 . HIS B  1 68  ? 48.444 1.973   -13.182 1.00 13.21  ? 67  HIS B NE2 1 
ATOM   2808 N  N   . VAL B  1 69  ? 50.393 7.898   -14.715 1.00 7.90   ? 68  VAL B N   1 
ATOM   2809 C  CA  . VAL B  1 69  ? 50.255 9.320   -14.863 1.00 8.09   ? 68  VAL B CA  1 
ATOM   2810 C  C   . VAL B  1 69  ? 48.747 9.597   -15.083 1.00 7.61   ? 68  VAL B C   1 
ATOM   2811 O  O   . VAL B  1 69  ? 48.191 9.206   -16.099 1.00 8.78   ? 68  VAL B O   1 
ATOM   2812 C  CB  . VAL B  1 69  ? 51.089 9.955   -15.996 1.00 9.64   ? 68  VAL B CB  1 
ATOM   2813 C  CG1 . VAL B  1 69  ? 50.818 11.410  -16.057 1.00 12.14  ? 68  VAL B CG1 1 
ATOM   2814 C  CG2 . VAL B  1 69  ? 52.578 9.696   -15.751 1.00 13.44  ? 68  VAL B CG2 1 
ATOM   2815 N  N   . ASN B  1 70  ? 48.130 10.247  -14.087 1.00 8.94   ? 69  ASN B N   1 
ATOM   2816 C  CA  . ASN B  1 70  ? 46.715 10.526  -14.132 1.00 9.14   ? 69  ASN B CA  1 
ATOM   2817 C  C   . ASN B  1 70  ? 46.453 11.917  -14.660 1.00 8.39   ? 69  ASN B C   1 
ATOM   2818 O  O   . ASN B  1 70  ? 47.233 12.862  -14.474 1.00 9.62   ? 69  ASN B O   1 
ATOM   2819 C  CB  . ASN B  1 70  ? 46.104 10.484  -12.705 1.00 10.63  ? 69  ASN B CB  1 
ATOM   2820 C  CG  . ASN B  1 70  ? 45.843 9.133   -12.164 1.00 12.47  ? 69  ASN B CG  1 
ATOM   2821 O  OD1 . ASN B  1 70  ? 45.958 8.121   -12.844 1.00 14.18  ? 69  ASN B OD1 1 
ATOM   2822 N  ND2 . ASN B  1 70  ? 45.362 9.113   -10.848 1.00 13.38  ? 69  ASN B ND2 1 
ATOM   2823 N  N   . PHE B  1 71  ? 45.280 12.037  -15.300 1.00 9.00   ? 70  PHE B N   1 
ATOM   2824 C  CA  . PHE B  1 71  ? 44.774 13.306  -15.875 1.00 8.85   ? 70  PHE B CA  1 
ATOM   2825 C  C   . PHE B  1 71  ? 43.463 13.667  -15.227 1.00 10.21  ? 70  PHE B C   1 
ATOM   2826 O  O   . PHE B  1 71  ? 42.622 12.795  -14.912 1.00 12.24  ? 70  PHE B O   1 
ATOM   2827 C  CB  . PHE B  1 71  ? 44.549 13.113  -17.390 1.00 9.94   ? 70  PHE B CB  1 
ATOM   2828 C  CG  . PHE B  1 71  ? 45.893 13.035  -18.094 1.00 9.30   ? 70  PHE B CG  1 
ATOM   2829 C  CD1 . PHE B  1 71  ? 46.687 11.852  -18.002 1.00 11.74  ? 70  PHE B CD1 1 
ATOM   2830 C  CD2 . PHE B  1 71  ? 46.401 14.095  -18.785 1.00 9.41   ? 70  PHE B CD2 1 
ATOM   2831 C  CE1 . PHE B  1 71  ? 47.989 11.849  -18.546 1.00 13.05  ? 70  PHE B CE1 1 
ATOM   2832 C  CE2 . PHE B  1 71  ? 47.689 14.089  -19.343 1.00 10.87  ? 70  PHE B CE2 1 
ATOM   2833 C  CZ  . PHE B  1 71  ? 48.467 12.927  -19.203 1.00 12.03  ? 70  PHE B CZ  1 
ATOM   2834 N  N   . GLU B  1 72  ? 43.208 14.979  -15.109 1.00 10.89  ? 71  GLU B N   1 
ATOM   2835 C  CA  . GLU B  1 72  ? 41.892 15.438  -14.712 1.00 12.17  ? 71  GLU B CA  1 
ATOM   2836 C  C   . GLU B  1 72  ? 40.866 14.949  -15.792 1.00 13.15  ? 71  GLU B C   1 
ATOM   2837 O  O   . GLU B  1 72  ? 41.084 15.184  -16.928 1.00 13.64  ? 71  GLU B O   1 
ATOM   2838 C  CB  . GLU B  1 72  ? 41.901 16.986  -14.694 1.00 12.49  ? 71  GLU B CB  1 
ATOM   2839 C  CG  . GLU B  1 72  ? 42.884 17.540  -13.667 1.00 14.10  ? 71  GLU B CG  1 
ATOM   2840 C  CD  . GLU B  1 72  ? 42.911 19.055  -13.646 1.00 16.40  ? 71  GLU B CD  1 
ATOM   2841 O  OE1 . GLU B  1 72  ? 42.152 19.726  -14.308 1.00 19.31  ? 71  GLU B OE1 1 
ATOM   2842 O  OE2 . GLU B  1 72  ? 43.754 19.637  -12.889 1.00 19.17  ? 71  GLU B OE2 1 
ATOM   2843 N  N   . ASP B  1 73  ? 39.754 14.379  -15.351 1.00 14.25  ? 72  ASP B N   1 
ATOM   2844 C  CA  . ASP B  1 73  ? 38.791 13.782  -16.286 1.00 16.42  ? 72  ASP B CA  1 
ATOM   2845 C  C   . ASP B  1 73  ? 37.389 14.295  -15.960 1.00 19.70  ? 72  ASP B C   1 
ATOM   2846 O  O   . ASP B  1 73  ? 36.425 13.567  -16.136 1.00 24.67  ? 72  ASP B O   1 
ATOM   2847 C  CB  . ASP B  1 73  ? 38.885 12.218  -16.287 1.00 16.15  ? 72  ASP B CB  1 
ATOM   2848 C  CG  . ASP B  1 73  ? 38.410 11.550  -15.013 1.00 19.46  ? 72  ASP B CG  1 
ATOM   2849 O  OD1 . ASP B  1 73  ? 38.491 12.219  -13.966 1.00 22.65  ? 72  ASP B OD1 1 
ATOM   2850 O  OD2 . ASP B  1 73  ? 38.148 10.359  -15.044 1.00 21.99  ? 72  ASP B OD2 1 
ATOM   2851 N  N   . ASN B  1 74  ? 37.285 15.554  -15.462 1.00 20.06  ? 73  ASN B N   1 
ATOM   2852 C  CA  . ASN B  1 74  ? 35.957 16.049  -15.151 1.00 23.82  ? 73  ASN B CA  1 
ATOM   2853 C  C   . ASN B  1 74  ? 35.243 16.562  -16.325 1.00 20.03  ? 73  ASN B C   1 
ATOM   2854 O  O   . ASN B  1 74  ? 34.039 16.843  -16.237 1.00 27.31  ? 73  ASN B O   1 
ATOM   2855 C  CB  . ASN B  1 74  ? 36.115 17.108  -14.065 1.00 24.68  ? 73  ASN B CB  1 
ATOM   2856 C  CG  . ASN B  1 74  ? 37.057 18.252  -14.456 1.00 25.93  ? 73  ASN B CG  1 
ATOM   2857 O  OD1 . ASN B  1 74  ? 36.593 19.377  -14.855 1.00 36.44  ? 73  ASN B OD1 1 
ATOM   2858 N  ND2 . ASN B  1 74  ? 38.341 17.973  -14.445 1.00 21.79  ? 73  ASN B ND2 1 
ATOM   2859 N  N   . ASP B  1 75  ? 35.903 16.795  -17.435 1.00 21.35  ? 74  ASP B N   1 
ATOM   2860 C  CA  . ASP B  1 75  ? 35.298 17.314  -18.640 1.00 22.73  ? 74  ASP B CA  1 
ATOM   2861 C  C   . ASP B  1 75  ? 35.993 16.735  -19.819 1.00 20.43  ? 74  ASP B C   1 
ATOM   2862 O  O   . ASP B  1 75  ? 36.850 15.874  -19.687 1.00 21.52  ? 74  ASP B O   1 
ATOM   2863 C  CB  . ASP B  1 75  ? 35.206 18.844  -18.556 1.00 21.15  ? 74  ASP B CB  1 
ATOM   2864 C  CG  . ASP B  1 75  ? 36.502 19.562  -18.692 1.00 22.83  ? 74  ASP B CG  1 
ATOM   2865 O  OD1 . ASP B  1 75  ? 37.520 18.929  -19.040 1.00 20.56  ? 74  ASP B OD1 1 
ATOM   2866 O  OD2 . ASP B  1 75  ? 36.502 20.774  -18.401 1.00 29.71  ? 74  ASP B OD2 1 
ATOM   2867 N  N   . ASN B  1 76  ? 35.636 17.228  -20.999 1.00 20.92  ? 75  ASN B N   1 
ATOM   2868 C  CA  . ASN B  1 76  ? 36.149 16.746  -22.313 1.00 21.28  ? 75  ASN B CA  1 
ATOM   2869 C  C   . ASN B  1 76  ? 37.282 17.586  -22.869 1.00 19.91  ? 75  ASN B C   1 
ATOM   2870 O  O   . ASN B  1 76  ? 37.446 17.637  -24.079 1.00 23.68  ? 75  ASN B O   1 
ATOM   2871 C  CB  . ASN B  1 76  ? 35.008 16.564  -23.377 1.00 24.31  ? 75  ASN B CB  1 
ATOM   2872 C  CG  . ASN B  1 76  ? 34.134 15.426  -23.009 1.00 31.54  ? 75  ASN B CG  1 
ATOM   2873 O  OD1 . ASN B  1 76  ? 34.581 14.385  -22.489 1.00 29.42  ? 75  ASN B OD1 1 
ATOM   2874 N  ND2 . ASN B  1 76  ? 32.787 15.622  -23.245 1.00 39.82  ? 75  ASN B ND2 1 
ATOM   2875 N  N   . ARG B  1 77  ? 38.124 18.148  -21.998 1.00 18.14  ? 76  ARG B N   1 
ATOM   2876 C  CA  . ARG B  1 77  ? 39.314 18.847  -22.512 1.00 17.27  ? 76  ARG B CA  1 
ATOM   2877 C  C   . ARG B  1 77  ? 40.229 17.872  -23.302 1.00 16.77  ? 76  ARG B C   1 
ATOM   2878 O  O   . ARG B  1 77  ? 40.908 18.340  -24.202 1.00 19.05  ? 76  ARG B O   1 
ATOM   2879 C  CB  . ARG B  1 77  ? 40.133 19.489  -21.410 1.00 18.05  ? 76  ARG B CB  1 
ATOM   2880 C  CG  . ARG B  1 77  ? 39.448 20.823  -20.969 1.00 17.69  ? 76  ARG B CG  1 
ATOM   2881 C  CD  . ARG B  1 77  ? 40.217 21.349  -19.661 1.00 18.30  ? 76  ARG B CD  1 
ATOM   2882 N  NE  . ARG B  1 77  ? 39.871 20.482  -18.545 1.00 18.07  ? 76  ARG B NE  1 
ATOM   2883 C  CZ  . ARG B  1 77  ? 40.589 20.534  -17.420 1.00 17.48  ? 76  ARG B CZ  1 
ATOM   2884 N  NH1 . ARG B  1 77  ? 41.601 21.450  -17.284 1.00 19.70  ? 76  ARG B NH1 1 
ATOM   2885 N  NH2 . ARG B  1 77  ? 40.337 19.677  -16.500 1.00 17.39  ? 76  ARG B NH2 1 
ATOM   2886 N  N   . SER B  1 78  ? 40.298 16.591  -22.906 1.00 14.97  ? 77  SER B N   1 
ATOM   2887 C  CA  . SER B  1 78  ? 41.235 15.651  -23.531 1.00 15.40  ? 77  SER B CA  1 
ATOM   2888 C  C   . SER B  1 78  ? 40.470 14.381  -23.908 1.00 13.49  ? 77  SER B C   1 
ATOM   2889 O  O   . SER B  1 78  ? 39.968 13.619  -23.033 1.00 15.14  ? 77  SER B O   1 
ATOM   2890 C  CB  . SER B  1 78  ? 42.314 15.246  -22.487 1.00 14.30  ? 77  SER B CB  1 
ATOM   2891 O  OG  . SER B  1 78  ? 43.065 16.406  -22.151 1.00 14.18  ? 77  SER B OG  1 
ATOM   2892 N  N   . VAL B  1 79  ? 40.344 14.168  -25.229 1.00 16.01  ? 78  VAL B N   1 
ATOM   2893 C  CA  . VAL B  1 79  ? 39.474 13.096  -25.728 1.00 16.66  ? 78  VAL B CA  1 
ATOM   2894 C  C   . VAL B  1 79  ? 40.141 12.392  -26.931 1.00 17.18  ? 78  VAL B C   1 
ATOM   2895 O  O   . VAL B  1 79  ? 40.972 12.958  -27.703 1.00 17.39  ? 78  VAL B O   1 
ATOM   2896 C  CB  . VAL B  1 79  ? 38.090 13.713  -26.203 1.00 20.54  ? 78  VAL B CB  1 
ATOM   2897 C  CG1 . VAL B  1 79  ? 37.415 14.226  -24.957 1.00 25.47  ? 78  VAL B CG1 1 
ATOM   2898 C  CG2 . VAL B  1 79  ? 38.290 14.738  -27.334 1.00 26.46  ? 78  VAL B CG2 1 
ATOM   2899 N  N   . LEU B  1 80  ? 39.666 11.175  -27.068 1.00 16.00  ? 79  LEU B N   1 
ATOM   2900 C  CA  . LEU B  1 80  ? 39.963 10.298  -28.219 1.00 16.39  ? 79  LEU B CA  1 
ATOM   2901 C  C   . LEU B  1 80  ? 38.662 10.108  -28.971 1.00 16.77  ? 79  LEU B C   1 
ATOM   2902 O  O   . LEU B  1 80  ? 37.628 9.792   -28.375 1.00 18.50  ? 79  LEU B O   1 
ATOM   2903 C  CB  . LEU B  1 80  ? 40.422 8.917   -27.678 1.00 16.55  ? 79  LEU B CB  1 
ATOM   2904 C  CG  . LEU B  1 80  ? 40.480 7.697   -28.618 1.00 16.32  ? 79  LEU B CG  1 
ATOM   2905 C  CD1 . LEU B  1 80  ? 41.418 7.877   -29.783 1.00 17.67  ? 79  LEU B CD1 1 
ATOM   2906 C  CD2 . LEU B  1 80  ? 40.895 6.492   -27.821 1.00 17.06  ? 79  LEU B CD2 1 
ATOM   2907 N  N   . LYS B  1 81  ? 38.737 10.179  -30.299 1.00 18.67  ? 80  LYS B N   1 
ATOM   2908 C  CA  . LYS B  1 81  ? 37.540 9.934   -31.178 1.00 20.62  ? 80  LYS B CA  1 
ATOM   2909 C  C   . LYS B  1 81  ? 37.991 9.266   -32.419 1.00 18.74  ? 80  LYS B C   1 
ATOM   2910 O  O   . LYS B  1 81  ? 39.204 9.062   -32.671 1.00 19.28  ? 80  LYS B O   1 
ATOM   2911 C  CB  . LYS B  1 81  ? 36.958 11.366  -31.637 1.00 28.09  ? 80  LYS B CB  1 
ATOM   2912 C  CG  . LYS B  1 81  ? 36.361 12.263  -30.551 1.00 31.80  ? 80  LYS B CG  1 
ATOM   2913 C  CD  . LYS B  1 81  ? 36.024 13.651  -31.192 1.00 33.57  ? 80  LYS B CD  1 
ATOM   2914 N  N   . GLY B  1 82  ? 37.049 8.829   -33.236 1.00 20.60  ? 81  GLY B N   1 
ATOM   2915 C  CA  . GLY B  1 82  ? 37.452 8.260   -34.510 1.00 20.98  ? 81  GLY B CA  1 
ATOM   2916 C  C   . GLY B  1 82  ? 37.703 6.734   -34.383 1.00 19.29  ? 81  GLY B C   1 
ATOM   2917 O  O   . GLY B  1 82  ? 37.200 6.099   -33.463 1.00 20.23  ? 81  GLY B O   1 
ATOM   2918 N  N   . GLY B  1 83  ? 38.497 6.175   -35.327 1.00 19.48  ? 82  GLY B N   1 
ATOM   2919 C  CA  . GLY B  1 83  ? 38.726 4.787   -35.313 1.00 20.28  ? 82  GLY B CA  1 
ATOM   2920 C  C   . GLY B  1 83  ? 37.408 4.013   -35.406 1.00 20.25  ? 82  GLY B C   1 
ATOM   2921 O  O   . GLY B  1 83  ? 36.622 4.287   -36.285 1.00 25.83  ? 82  GLY B O   1 
ATOM   2922 N  N   . PRO B  1 84  ? 37.224 2.992   -34.524 1.00 18.89  ? 83  PRO B N   1 
ATOM   2923 C  CA  . PRO B  1 84  ? 36.005 2.194   -34.446 1.00 19.55  ? 83  PRO B CA  1 
ATOM   2924 C  C   . PRO B  1 84  ? 34.921 2.887   -33.735 1.00 19.82  ? 83  PRO B C   1 
ATOM   2925 O  O   . PRO B  1 84  ? 33.886 2.274   -33.610 1.00 25.35  ? 83  PRO B O   1 
ATOM   2926 C  CB  . PRO B  1 84  ? 36.443 0.877   -33.857 1.00 20.66  ? 83  PRO B CB  1 
ATOM   2927 C  CG  . PRO B  1 84  ? 37.439 1.374   -32.808 1.00 19.59  ? 83  PRO B CG  1 
ATOM   2928 C  CD  . PRO B  1 84  ? 38.244 2.506   -33.543 1.00 17.82  ? 83  PRO B CD  1 
ATOM   2929 N  N   . PHE B  1 85  ? 35.193 4.080   -33.131 1.00 19.29  ? 84  PHE B N   1 
ATOM   2930 C  CA  . PHE B  1 85  ? 34.272 4.679   -32.167 1.00 22.43  ? 84  PHE B CA  1 
ATOM   2931 C  C   . PHE B  1 85  ? 33.216 5.499   -32.804 1.00 25.23  ? 84  PHE B C   1 
ATOM   2932 O  O   . PHE B  1 85  ? 33.566 6.344   -33.622 1.00 27.25  ? 84  PHE B O   1 
ATOM   2933 C  CB  . PHE B  1 85  ? 35.117 5.502   -31.170 1.00 20.85  ? 84  PHE B CB  1 
ATOM   2934 C  CG  . PHE B  1 85  ? 36.103 4.645   -30.443 1.00 17.30  ? 84  PHE B CG  1 
ATOM   2935 C  CD1 . PHE B  1 85  ? 35.692 3.485   -29.704 1.00 20.01  ? 84  PHE B CD1 1 
ATOM   2936 C  CD2 . PHE B  1 85  ? 37.472 4.952   -30.563 1.00 19.66  ? 84  PHE B CD2 1 
ATOM   2937 C  CE1 . PHE B  1 85  ? 36.600 2.652   -29.075 1.00 19.95  ? 84  PHE B CE1 1 
ATOM   2938 C  CE2 . PHE B  1 85  ? 38.448 4.116   -29.898 1.00 20.14  ? 84  PHE B CE2 1 
ATOM   2939 C  CZ  . PHE B  1 85  ? 37.999 2.964   -29.273 1.00 20.06  ? 84  PHE B CZ  1 
ATOM   2940 N  N   . SER B  1 86  ? 32.027 5.494   -32.172 1.00 27.11  ? 85  SER B N   1 
ATOM   2941 C  CA  . SER B  1 86  ? 31.057 6.545   -32.501 1.00 29.53  ? 85  SER B CA  1 
ATOM   2942 C  C   . SER B  1 86  ? 30.976 7.560   -31.394 1.00 33.49  ? 85  SER B C   1 
ATOM   2943 O  O   . SER B  1 86  ? 30.263 8.499   -31.580 1.00 45.96  ? 85  SER B O   1 
ATOM   2944 C  CB  . SER B  1 86  ? 29.704 5.920   -32.768 1.00 32.06  ? 85  SER B CB  1 
ATOM   2945 O  OG  . SER B  1 86  ? 29.284 5.283   -31.560 1.00 43.83  ? 85  SER B OG  1 
ATOM   2946 N  N   . ASP B  1 87  ? 31.509 7.288   -30.207 1.00 30.33  ? 86  ASP B N   1 
ATOM   2947 C  CA  . ASP B  1 87  ? 31.442 8.133   -28.971 1.00 32.45  ? 86  ASP B CA  1 
ATOM   2948 C  C   . ASP B  1 87  ? 32.819 8.719   -28.774 1.00 23.96  ? 86  ASP B C   1 
ATOM   2949 O  O   . ASP B  1 87  ? 33.806 8.080   -29.115 1.00 26.03  ? 86  ASP B O   1 
ATOM   2950 C  CB  . ASP B  1 87  ? 31.035 7.321   -27.676 1.00 36.51  ? 86  ASP B CB  1 
ATOM   2951 C  CG  . ASP B  1 87  ? 29.622 6.592   -27.787 1.00 43.63  ? 86  ASP B CG  1 
ATOM   2952 O  OD1 . ASP B  1 87  ? 28.697 7.305   -28.254 1.00 43.53  ? 86  ASP B OD1 1 
ATOM   2953 O  OD2 . ASP B  1 87  ? 29.545 5.359   -27.358 1.00 33.47  ? 86  ASP B OD2 1 
ATOM   2954 N  N   . SER B  1 88  ? 32.852 9.731   -27.931 1.00 26.60  ? 87  SER B N   1 
ATOM   2955 C  CA  . SER B  1 88  ? 34.073 10.377  -27.532 1.00 24.01  ? 87  SER B CA  1 
ATOM   2956 C  C   . SER B  1 88  ? 34.566 9.739   -26.209 1.00 18.38  ? 87  SER B C   1 
ATOM   2957 O  O   . SER B  1 88  ? 33.796 9.634   -25.255 1.00 20.61  ? 87  SER B O   1 
ATOM   2958 C  CB  . SER B  1 88  ? 33.751 11.837  -27.328 1.00 30.42  ? 87  SER B CB  1 
ATOM   2959 O  OG  . SER B  1 88  ? 34.896 12.502  -26.926 1.00 36.23  ? 87  SER B OG  1 
ATOM   2960 N  N   . TYR B  1 89  ? 35.834 9.318   -26.152 1.00 17.83  ? 88  TYR B N   1 
ATOM   2961 C  CA  . TYR B  1 89  ? 36.402 8.674   -24.957 1.00 16.04  ? 88  TYR B CA  1 
ATOM   2962 C  C   . TYR B  1 89  ? 37.316 9.691   -24.246 1.00 17.80  ? 88  TYR B C   1 
ATOM   2963 O  O   . TYR B  1 89  ? 38.118 10.371  -24.896 1.00 17.98  ? 88  TYR B O   1 
ATOM   2964 C  CB  . TYR B  1 89  ? 37.148 7.390   -25.324 1.00 17.44  ? 88  TYR B CB  1 
ATOM   2965 C  CG  . TYR B  1 89  ? 36.227 6.217   -25.600 1.00 15.21  ? 88  TYR B CG  1 
ATOM   2966 C  CD1 . TYR B  1 89  ? 35.466 6.164   -26.761 1.00 19.02  ? 88  TYR B CD1 1 
ATOM   2967 C  CD2 . TYR B  1 89  ? 36.114 5.168   -24.697 1.00 16.29  ? 88  TYR B CD2 1 
ATOM   2968 C  CE1 . TYR B  1 89  ? 34.621 5.098   -27.016 1.00 16.71  ? 88  TYR B CE1 1 
ATOM   2969 C  CE2 . TYR B  1 89  ? 35.272 4.097   -24.944 1.00 16.39  ? 88  TYR B CE2 1 
ATOM   2970 C  CZ  . TYR B  1 89  ? 34.527 4.067   -26.105 1.00 19.03  ? 88  TYR B CZ  1 
ATOM   2971 O  OH  . TYR B  1 89  ? 33.685 3.002   -26.356 1.00 20.18  ? 88  TYR B OH  1 
ATOM   2972 N  N   . ARG B  1 90  ? 37.172 9.827   -22.949 1.00 15.28  ? 89  ARG B N   1 
ATOM   2973 C  CA  . ARG B  1 90  ? 37.916 10.846  -22.176 1.00 15.77  ? 89  ARG B CA  1 
ATOM   2974 C  C   . ARG B  1 90  ? 39.198 10.228  -21.634 1.00 12.54  ? 89  ARG B C   1 
ATOM   2975 O  O   . ARG B  1 90  ? 39.195 9.162   -21.016 1.00 13.27  ? 89  ARG B O   1 
ATOM   2976 C  CB  . ARG B  1 90  ? 36.995 11.183  -20.993 1.00 16.70  ? 89  ARG B CB  1 
ATOM   2977 C  CG  . ARG B  1 90  ? 37.514 12.458  -20.286 1.00 18.13  ? 89  ARG B CG  1 
ATOM   2978 C  CD  . ARG B  1 90  ? 36.488 12.834  -19.166 1.00 20.39  ? 89  ARG B CD  1 
ATOM   2979 N  NE  . ARG B  1 90  ? 35.290 13.339  -19.839 1.00 24.24  ? 89  ARG B NE  1 
ATOM   2980 C  CZ  . ARG B  1 90  ? 34.196 13.724  -19.193 1.00 22.57  ? 89  ARG B CZ  1 
ATOM   2981 N  NH1 . ARG B  1 90  ? 34.129 13.663  -17.889 1.00 25.55  ? 89  ARG B NH1 1 
ATOM   2982 N  NH2 . ARG B  1 90  ? 33.179 14.099  -19.849 1.00 26.53  ? 89  ARG B NH2 1 
ATOM   2983 N  N   . LEU B  1 91  ? 40.313 10.954  -21.863 1.00 13.08  ? 90  LEU B N   1 
ATOM   2984 C  CA  . LEU B  1 91  ? 41.599 10.516  -21.338 1.00 11.85  ? 90  LEU B CA  1 
ATOM   2985 C  C   . LEU B  1 91  ? 41.527 10.428  -19.820 1.00 12.00  ? 90  LEU B C   1 
ATOM   2986 O  O   . LEU B  1 91  ? 41.072 11.380  -19.150 1.00 13.94  ? 90  LEU B O   1 
ATOM   2987 C  CB  . LEU B  1 91  ? 42.659 11.523  -21.744 1.00 12.74  ? 90  LEU B CB  1 
ATOM   2988 C  CG  . LEU B  1 91  ? 44.071 11.300  -21.222 1.00 12.00  ? 90  LEU B CG  1 
ATOM   2989 C  CD1 . LEU B  1 91  ? 44.689 10.012  -21.787 1.00 12.99  ? 90  LEU B CD1 1 
ATOM   2990 C  CD2 . LEU B  1 91  ? 44.943 12.491  -21.623 1.00 12.03  ? 90  LEU B CD2 1 
ATOM   2991 N  N   A PHE B  1 92  ? 41.998 9.307   -19.268 0.50 12.88  ? 91  PHE B N   1 
ATOM   2992 N  N   B PHE B  1 92  ? 42.172 9.458   -19.238 0.50 11.63  ? 91  PHE B N   1 
ATOM   2993 C  CA  A PHE B  1 92  ? 42.108 9.053   -17.765 0.50 10.80  ? 91  PHE B CA  1 
ATOM   2994 C  CA  B PHE B  1 92  ? 42.323 9.543   -17.777 0.50 12.93  ? 91  PHE B CA  1 
ATOM   2995 C  C   A PHE B  1 92  ? 43.554 9.049   -17.344 0.50 9.35   ? 91  PHE B C   1 
ATOM   2996 C  C   B PHE B  1 92  ? 43.670 9.126   -17.242 0.50 9.81   ? 91  PHE B C   1 
ATOM   2997 O  O   A PHE B  1 92  ? 43.905 9.612   -16.308 0.50 9.53   ? 91  PHE B O   1 
ATOM   2998 O  O   B PHE B  1 92  ? 44.036 9.656   -16.233 0.50 9.41   ? 91  PHE B O   1 
ATOM   2999 C  CB  A PHE B  1 92  ? 41.348 7.788   -17.322 0.50 9.67   ? 91  PHE B CB  1 
ATOM   3000 C  CB  B PHE B  1 92  ? 41.146 8.876   -17.134 0.50 14.24  ? 91  PHE B CB  1 
ATOM   3001 C  CG  A PHE B  1 92  ? 41.411 7.558   -15.786 0.50 13.62  ? 91  PHE B CG  1 
ATOM   3002 C  CG  B PHE B  1 92  ? 41.127 7.385   -17.291 0.50 16.23  ? 91  PHE B CG  1 
ATOM   3003 C  CD1 A PHE B  1 92  ? 40.640 8.343   -14.968 0.50 20.37  ? 91  PHE B CD1 1 
ATOM   3004 C  CD1 B PHE B  1 92  ? 40.600 6.752   -18.430 0.50 16.03  ? 91  PHE B CD1 1 
ATOM   3005 C  CD2 A PHE B  1 92  ? 42.185 6.574   -15.210 0.50 17.55  ? 91  PHE B CD2 1 
ATOM   3006 C  CD2 B PHE B  1 92  ? 41.683 6.594   -16.245 0.50 18.01  ? 91  PHE B CD2 1 
ATOM   3007 C  CE1 A PHE B  1 92  ? 40.588 8.147   -13.567 0.50 25.65  ? 91  PHE B CE1 1 
ATOM   3008 C  CE1 B PHE B  1 92  ? 40.674 5.315   -18.537 0.50 13.76  ? 91  PHE B CE1 1 
ATOM   3009 C  CE2 A PHE B  1 92  ? 42.261 6.420   -13.827 0.50 20.35  ? 91  PHE B CE2 1 
ATOM   3010 C  CE2 B PHE B  1 92  ? 41.739 5.181   -16.340 0.50 15.96  ? 91  PHE B CE2 1 
ATOM   3011 C  CZ  A PHE B  1 92  ? 41.464 7.223   -13.005 0.50 27.39  ? 91  PHE B CZ  1 
ATOM   3012 C  CZ  B PHE B  1 92  ? 41.292 4.552   -17.484 0.50 15.54  ? 91  PHE B CZ  1 
ATOM   3013 N  N   A GLN B  1 93  ? 44.434 8.367   -18.091 0.50 9.82   ? 92  GLN B N   1 
ATOM   3014 N  N   B GLN B  1 93  ? 44.427 8.184   -17.859 0.50 10.48  ? 92  GLN B N   1 
ATOM   3015 C  CA  A GLN B  1 93  ? 45.738 8.095   -17.537 0.50 8.86   ? 92  GLN B CA  1 
ATOM   3016 C  CA  B GLN B  1 93  ? 45.788 7.960   -17.457 0.50 8.64   ? 92  GLN B CA  1 
ATOM   3017 C  C   A GLN B  1 93  ? 46.608 7.430   -18.635 0.50 8.96   ? 92  GLN B C   1 
ATOM   3018 C  C   B GLN B  1 93  ? 46.597 7.363   -18.587 0.50 8.76   ? 92  GLN B C   1 
ATOM   3019 O  O   A GLN B  1 93  ? 46.095 7.025   -19.679 0.50 9.86   ? 92  GLN B O   1 
ATOM   3020 O  O   B GLN B  1 93  ? 46.025 6.741   -19.491 0.50 9.95   ? 92  GLN B O   1 
ATOM   3021 C  CB  A GLN B  1 93  ? 45.592 7.165   -16.258 0.50 14.70  ? 92  GLN B CB  1 
ATOM   3022 C  CB  B GLN B  1 93  ? 45.908 6.980   -16.234 0.50 10.65  ? 92  GLN B CB  1 
ATOM   3023 C  CG  A GLN B  1 93  ? 45.818 5.715   -16.513 0.50 19.50  ? 92  GLN B CG  1 
ATOM   3024 C  CG  B GLN B  1 93  ? 45.111 5.808   -16.332 0.50 13.28  ? 92  GLN B CG  1 
ATOM   3025 C  CD  A GLN B  1 93  ? 46.142 4.753   -15.364 0.50 10.35  ? 92  GLN B CD  1 
ATOM   3026 C  CD  B GLN B  1 93  ? 46.123 4.684   -16.288 0.50 13.44  ? 92  GLN B CD  1 
ATOM   3027 O  OE1 A GLN B  1 93  ? 46.596 3.712   -15.646 0.50 12.63  ? 92  GLN B OE1 1 
ATOM   3028 O  OE1 B GLN B  1 93  ? 47.027 4.663   -17.073 0.50 12.00  ? 92  GLN B OE1 1 
ATOM   3029 N  NE2 A GLN B  1 93  ? 45.812 5.098   -14.170 0.50 13.66  ? 92  GLN B NE2 1 
ATOM   3030 N  NE2 B GLN B  1 93  ? 45.861 3.703   -15.511 0.50 22.20  ? 92  GLN B NE2 1 
ATOM   3031 N  N   . PHE B  1 94  ? 47.916 7.461   -18.442 1.00 8.20   ? 93  PHE B N   1 
ATOM   3032 C  CA  . PHE B  1 94  ? 48.766 6.570   -19.241 1.00 7.89   ? 93  PHE B CA  1 
ATOM   3033 C  C   . PHE B  1 94  ? 49.738 5.880   -18.285 1.00 7.94   ? 93  PHE B C   1 
ATOM   3034 O  O   . PHE B  1 94  ? 50.039 6.321   -17.183 1.00 8.14   ? 93  PHE B O   1 
ATOM   3035 C  CB  . PHE B  1 94  ? 49.475 7.269   -20.420 1.00 8.50   ? 93  PHE B CB  1 
ATOM   3036 C  CG  . PHE B  1 94  ? 50.565 8.229   -20.046 1.00 8.41   ? 93  PHE B CG  1 
ATOM   3037 C  CD1 . PHE B  1 94  ? 51.914 7.761   -19.869 1.00 9.26   ? 93  PHE B CD1 1 
ATOM   3038 C  CD2 . PHE B  1 94  ? 50.345 9.564   -19.928 1.00 8.93   ? 93  PHE B CD2 1 
ATOM   3039 C  CE1 . PHE B  1 94  ? 52.929 8.665   -19.505 1.00 9.37   ? 93  PHE B CE1 1 
ATOM   3040 C  CE2 . PHE B  1 94  ? 51.365 10.448  -19.592 1.00 9.14   ? 93  PHE B CE2 1 
ATOM   3041 C  CZ  . PHE B  1 94  ? 52.670 10.016  -19.409 1.00 9.13   ? 93  PHE B CZ  1 
ATOM   3042 N  N   . HIS B  1 95  ? 50.303 4.788   -18.801 1.00 8.01   ? 94  HIS B N   1 
ATOM   3043 C  CA  . HIS B  1 95  ? 51.299 3.979   -18.053 1.00 7.51   ? 94  HIS B CA  1 
ATOM   3044 C  C   . HIS B  1 95  ? 52.040 3.104   -19.049 1.00 7.05   ? 94  HIS B C   1 
ATOM   3045 O  O   . HIS B  1 95  ? 51.701 3.103   -20.250 1.00 7.84   ? 94  HIS B O   1 
ATOM   3046 C  CB  . HIS B  1 95  ? 50.600 3.160   -16.944 1.00 7.89   ? 94  HIS B CB  1 
ATOM   3047 C  CG  . HIS B  1 95  ? 49.661 2.166   -17.479 1.00 7.44   ? 94  HIS B CG  1 
ATOM   3048 N  ND1 . HIS B  1 95  ? 48.321 2.371   -17.560 1.00 9.50   ? 94  HIS B ND1 1 
ATOM   3049 C  CD2 . HIS B  1 95  ? 49.847 0.939   -18.013 1.00 8.22   ? 94  HIS B CD2 1 
ATOM   3050 C  CE1 . HIS B  1 95  ? 47.757 1.307   -18.098 1.00 9.87   ? 94  HIS B CE1 1 
ATOM   3051 N  NE2 . HIS B  1 95  ? 48.641 0.402   -18.431 1.00 7.75   ? 94  HIS B NE2 1 
ATOM   3052 N  N   . PHE B  1 96  ? 52.977 2.328   -18.540 1.00 6.96   ? 95  PHE B N   1 
ATOM   3053 C  CA  . PHE B  1 96  ? 53.808 1.444   -19.328 1.00 6.87   ? 95  PHE B CA  1 
ATOM   3054 C  C   . PHE B  1 96  ? 53.787 0.053   -18.750 1.00 6.96   ? 95  PHE B C   1 
ATOM   3055 O  O   . PHE B  1 96  ? 53.521 -0.143  -17.544 1.00 8.13   ? 95  PHE B O   1 
ATOM   3056 C  CB  . PHE B  1 96  ? 55.251 1.945   -19.365 1.00 7.66   ? 95  PHE B CB  1 
ATOM   3057 C  CG  . PHE B  1 96  ? 55.408 3.341   -19.868 1.00 7.26   ? 95  PHE B CG  1 
ATOM   3058 C  CD1 . PHE B  1 96  ? 55.287 4.444   -18.986 1.00 8.66   ? 95  PHE B CD1 1 
ATOM   3059 C  CD2 . PHE B  1 96  ? 55.645 3.605   -21.214 1.00 8.30   ? 95  PHE B CD2 1 
ATOM   3060 C  CE1 . PHE B  1 96  ? 55.401 5.726   -19.440 1.00 8.59   ? 95  PHE B CE1 1 
ATOM   3061 C  CE2 . PHE B  1 96  ? 55.781 4.891   -21.664 1.00 8.70   ? 95  PHE B CE2 1 
ATOM   3062 C  CZ  . PHE B  1 96  ? 55.657 5.973   -20.770 1.00 9.31   ? 95  PHE B CZ  1 
ATOM   3063 N  N   . HIS B  1 97  ? 54.134 -0.918  -19.591 1.00 7.41   ? 96  HIS B N   1 
ATOM   3064 C  CA  . HIS B  1 97  ? 54.530 -2.245  -19.137 1.00 8.05   ? 96  HIS B CA  1 
ATOM   3065 C  C   . HIS B  1 97  ? 55.929 -2.506  -19.677 1.00 7.41   ? 96  HIS B C   1 
ATOM   3066 O  O   . HIS B  1 97  ? 56.283 -2.025  -20.771 1.00 8.05   ? 96  HIS B O   1 
ATOM   3067 C  CB  . HIS B  1 97  ? 53.562 -3.328  -19.638 1.00 8.87   ? 96  HIS B CB  1 
ATOM   3068 C  CG  . HIS B  1 97  ? 52.169 -3.108  -19.181 1.00 8.07   ? 96  HIS B CG  1 
ATOM   3069 N  ND1 . HIS B  1 97  ? 51.563 -3.857  -18.166 1.00 8.77   ? 96  HIS B ND1 1 
ATOM   3070 C  CD2 . HIS B  1 97  ? 51.207 -2.249  -19.600 1.00 7.75   ? 96  HIS B CD2 1 
ATOM   3071 C  CE1 . HIS B  1 97  ? 50.318 -3.400  -18.009 1.00 8.06   ? 96  HIS B CE1 1 
ATOM   3072 N  NE2 . HIS B  1 97  ? 50.064 -2.425  -18.866 1.00 8.06   ? 96  HIS B NE2 1 
ATOM   3073 N  N   . TRP B  1 98  ? 56.687 -3.317  -18.948 1.00 7.69   ? 97  TRP B N   1 
ATOM   3074 C  CA  . TRP B  1 98  ? 58.011 -3.675  -19.388 1.00 7.62   ? 97  TRP B CA  1 
ATOM   3075 C  C   . TRP B  1 98  ? 58.314 -5.075  -18.863 1.00 8.96   ? 97  TRP B C   1 
ATOM   3076 O  O   . TRP B  1 98  ? 57.581 -5.661  -18.059 1.00 10.08  ? 97  TRP B O   1 
ATOM   3077 C  CB  . TRP B  1 98  ? 59.053 -2.666  -18.853 1.00 8.91   ? 97  TRP B CB  1 
ATOM   3078 C  CG  . TRP B  1 98  ? 59.034 -2.491  -17.392 1.00 8.07   ? 97  TRP B CG  1 
ATOM   3079 C  CD1 . TRP B  1 98  ? 59.721 -3.283  -16.461 1.00 9.26   ? 97  TRP B CD1 1 
ATOM   3080 C  CD2 . TRP B  1 98  ? 58.287 -1.533  -16.616 1.00 7.98   ? 97  TRP B CD2 1 
ATOM   3081 N  NE1 . TRP B  1 98  ? 59.465 -2.834  -15.179 1.00 8.61   ? 97  TRP B NE1 1 
ATOM   3082 C  CE2 . TRP B  1 98  ? 58.610 -1.749  -15.255 1.00 8.14   ? 97  TRP B CE2 1 
ATOM   3083 C  CE3 . TRP B  1 98  ? 57.408 -0.512  -16.958 1.00 7.79   ? 97  TRP B CE3 1 
ATOM   3084 C  CZ2 . TRP B  1 98  ? 58.076 -0.946  -14.243 1.00 8.56   ? 97  TRP B CZ2 1 
ATOM   3085 C  CZ3 . TRP B  1 98  ? 56.886 0.301   -15.962 1.00 8.09   ? 97  TRP B CZ3 1 
ATOM   3086 C  CH2 . TRP B  1 98  ? 57.216 0.075   -14.614 1.00 9.02   ? 97  TRP B CH2 1 
ATOM   3087 N  N   . GLY B  1 99  ? 59.461 -5.610  -19.319 1.00 10.14  ? 98  GLY B N   1 
ATOM   3088 C  CA  . GLY B  1 99  ? 59.855 -6.940  -18.947 1.00 12.76  ? 98  GLY B CA  1 
ATOM   3089 C  C   . GLY B  1 99  ? 61.135 -7.001  -18.220 1.00 15.03  ? 98  GLY B C   1 
ATOM   3090 O  O   . GLY B  1 99  ? 61.768 -5.977  -18.025 1.00 14.98  ? 98  GLY B O   1 
ATOM   3091 N  N   . SER B  1 100 ? 61.571 -8.201  -17.858 1.00 19.37  ? 99  SER B N   1 
ATOM   3092 C  CA  . SER B  1 100 ? 62.823 -8.279  -17.056 1.00 23.99  ? 99  SER B CA  1 
ATOM   3093 C  C   . SER B  1 100 ? 64.095 -8.043  -17.870 1.00 23.51  ? 99  SER B C   1 
ATOM   3094 O  O   . SER B  1 100 ? 65.153 -7.738  -17.236 1.00 28.14  ? 99  SER B O   1 
ATOM   3095 C  CB  . SER B  1 100 ? 62.900 -9.526  -16.190 1.00 32.93  ? 99  SER B CB  1 
ATOM   3096 O  OG  . SER B  1 100 ? 62.863 -10.548 -17.120 1.00 40.27  ? 99  SER B OG  1 
ATOM   3097 N  N   . THR B  1 101 ? 64.022 -8.176  -19.120 1.00 24.34  ? 100 THR B N   1 
ATOM   3098 C  CA  . THR B  1 101 ? 65.291 -7.829  -19.920 1.00 19.14  ? 100 THR B CA  1 
ATOM   3099 C  C   . THR B  1 101 ? 64.705 -7.305  -21.279 1.00 19.07  ? 100 THR B C   1 
ATOM   3100 O  O   . THR B  1 101 ? 63.470 -7.262  -21.478 1.00 16.72  ? 100 THR B O   1 
ATOM   3101 C  CB  . THR B  1 101 ? 66.198 -9.022  -20.234 1.00 20.66  ? 100 THR B CB  1 
ATOM   3102 O  OG1 . THR B  1 101 ? 65.307 -9.780  -21.122 1.00 22.56  ? 100 THR B OG1 1 
ATOM   3103 C  CG2 . THR B  1 101 ? 66.523 -9.921  -19.080 1.00 41.60  ? 100 THR B CG2 1 
ATOM   3104 N  N   . ASN B  1 102 ? 65.538 -6.792  -22.121 1.00 15.96  ? 101 ASN B N   1 
ATOM   3105 C  CA  . ASN B  1 102 ? 65.088 -6.075  -23.312 1.00 14.12  ? 101 ASN B CA  1 
ATOM   3106 C  C   . ASN B  1 102 ? 64.353 -7.029  -24.291 1.00 14.49  ? 101 ASN B C   1 
ATOM   3107 O  O   . ASN B  1 102 ? 63.682 -6.532  -25.140 1.00 15.53  ? 101 ASN B O   1 
ATOM   3108 C  CB  . ASN B  1 102 ? 66.327 -5.546  -24.040 1.00 15.27  ? 101 ASN B CB  1 
ATOM   3109 C  CG  . ASN B  1 102 ? 66.986 -4.342  -23.338 1.00 15.27  ? 101 ASN B CG  1 
ATOM   3110 O  OD1 . ASN B  1 102 ? 66.426 -3.842  -22.378 1.00 18.28  ? 101 ASN B OD1 1 
ATOM   3111 N  ND2 . ASN B  1 102 ? 68.102 -3.894  -23.922 1.00 18.73  ? 101 ASN B ND2 1 
ATOM   3112 N  N   . GLU B  1 103 ? 64.552 -8.325  -24.169 1.00 16.49  ? 102 GLU B N   1 
ATOM   3113 C  CA  . GLU B  1 103 ? 63.960 -9.176  -25.210 1.00 20.06  ? 102 GLU B CA  1 
ATOM   3114 C  C   . GLU B  1 103 ? 62.477 -9.375  -25.168 1.00 18.03  ? 102 GLU B C   1 
ATOM   3115 O  O   . GLU B  1 103 ? 61.888 -9.864  -26.084 1.00 22.29  ? 102 GLU B O   1 
ATOM   3116 C  CB  . GLU B  1 103 ? 64.616 -10.573 -25.075 1.00 29.17  ? 102 GLU B CB  1 
ATOM   3117 C  CG  . GLU B  1 103 ? 66.029 -10.549 -25.706 1.00 35.09  ? 102 GLU B CG  1 
ATOM   3118 C  CD  . GLU B  1 103 ? 67.011 -9.659  -24.986 1.00 40.13  ? 102 GLU B CD  1 
ATOM   3119 O  OE1 . GLU B  1 103 ? 67.763 -8.998  -25.760 1.00 64.29  ? 102 GLU B OE1 1 
ATOM   3120 O  OE2 . GLU B  1 103 ? 66.998 -9.627  -23.697 1.00 58.19  ? 102 GLU B OE2 1 
ATOM   3121 N  N   A HIS B  1 104 ? 61.912 -8.986  -24.051 0.50 14.96  ? 103 HIS B N   1 
ATOM   3122 N  N   B HIS B  1 104 ? 61.802 -9.127  -24.032 0.50 14.84  ? 103 HIS B N   1 
ATOM   3123 C  CA  A HIS B  1 104 ? 60.477 -9.102  -23.866 0.50 13.68  ? 103 HIS B CA  1 
ATOM   3124 C  CA  B HIS B  1 104 ? 60.292 -9.204  -23.938 0.50 16.01  ? 103 HIS B CA  1 
ATOM   3125 C  C   A HIS B  1 104 ? 60.020 -8.050  -22.874 0.50 12.98  ? 103 HIS B C   1 
ATOM   3126 C  C   B HIS B  1 104 ? 59.790 -8.310  -22.794 0.50 19.60  ? 103 HIS B C   1 
ATOM   3127 O  O   A HIS B  1 104 ? 60.738 -7.745  -21.922 0.50 14.44  ? 103 HIS B O   1 
ATOM   3128 O  O   B HIS B  1 104 ? 60.256 -8.417  -21.660 0.50 20.11  ? 103 HIS B O   1 
ATOM   3129 C  CB  A HIS B  1 104 ? 60.177 -10.447 -23.241 0.50 15.72  ? 103 HIS B CB  1 
ATOM   3130 C  CB  B HIS B  1 104 ? 59.686 -10.639 -23.844 0.50 18.08  ? 103 HIS B CB  1 
ATOM   3131 C  CG  A HIS B  1 104 ? 60.650 -10.536 -21.829 0.50 19.67  ? 103 HIS B CG  1 
ATOM   3132 C  CG  B HIS B  1 104 ? 58.175 -10.709 -24.015 0.50 14.49  ? 103 HIS B CG  1 
ATOM   3133 N  ND1 A HIS B  1 104 ? 61.945 -10.865 -21.501 0.50 27.90  ? 103 HIS B ND1 1 
ATOM   3134 N  ND1 B HIS B  1 104 ? 57.381 -9.613  -24.276 0.50 8.81   ? 103 HIS B ND1 1 
ATOM   3135 C  CD2 A HIS B  1 104 ? 60.029 -10.263 -20.662 0.50 22.61  ? 103 HIS B CD2 1 
ATOM   3136 C  CD2 B HIS B  1 104 ? 57.319 -11.760 -23.961 0.50 21.41  ? 103 HIS B CD2 1 
ATOM   3137 C  CE1 A HIS B  1 104 ? 62.095 -10.834 -20.194 0.50 23.52  ? 103 HIS B CE1 1 
ATOM   3138 C  CE1 B HIS B  1 104 ? 56.111 -9.964  -24.377 0.50 19.61  ? 103 HIS B CE1 1 
ATOM   3139 N  NE2 A HIS B  1 104 ? 60.949 -10.463 -19.664 0.50 24.11  ? 103 HIS B NE2 1 
ATOM   3140 N  NE2 B HIS B  1 104 ? 56.047 -11.271 -24.188 0.50 17.60  ? 103 HIS B NE2 1 
ATOM   3141 N  N   . GLY B  1 105 ? 58.843 -7.476  -23.092 1.00 17.78  ? 104 GLY B N   1 
ATOM   3142 C  CA  . GLY B  1 105 ? 58.341 -6.523  -22.134 1.00 13.69  ? 104 GLY B CA  1 
ATOM   3143 C  C   . GLY B  1 105 ? 57.380 -5.703  -22.929 1.00 10.54  ? 104 GLY B C   1 
ATOM   3144 O  O   . GLY B  1 105 ? 57.257 -4.495  -22.722 1.00 11.21  ? 104 GLY B O   1 
ATOM   3145 N  N   . SER B  1 106 ? 56.559 -6.365  -23.723 1.00 9.39   ? 105 SER B N   1 
ATOM   3146 C  CA  . SER B  1 106 ? 55.556 -5.601  -24.399 1.00 8.77   ? 105 SER B CA  1 
ATOM   3147 C  C   . SER B  1 106 ? 54.487 -6.603  -23.951 1.00 9.37   ? 105 SER B C   1 
ATOM   3148 O  O   . SER B  1 106 ? 54.790 -7.734  -23.537 1.00 10.09  ? 105 SER B O   1 
ATOM   3149 C  CB  . SER B  1 106 ? 55.530 -5.411  -25.903 1.00 9.95   ? 105 SER B CB  1 
ATOM   3150 O  OG  . SER B  1 106 ? 55.774 -6.631  -26.616 1.00 10.88  ? 105 SER B OG  1 
ATOM   3151 N  N   . GLU B  1 107 ? 53.235 -6.160  -23.998 1.00 9.39   ? 106 GLU B N   1 
ATOM   3152 C  CA  . GLU B  1 107 ? 52.119 -7.052  -23.705 1.00 9.57   ? 106 GLU B CA  1 
ATOM   3153 C  C   . GLU B  1 107 ? 51.637 -7.654  -25.016 1.00 9.62   ? 106 GLU B C   1 
ATOM   3154 O  O   . GLU B  1 107 ? 51.657 -8.865  -25.218 1.00 10.89  ? 106 GLU B O   1 
ATOM   3155 C  CB  . GLU B  1 107 ? 51.011 -6.239  -22.996 1.00 10.15  ? 106 GLU B CB  1 
ATOM   3156 C  CG  . GLU B  1 107 ? 51.542 -5.840  -21.573 1.00 12.67  ? 106 GLU B CG  1 
ATOM   3157 C  CD  . GLU B  1 107 ? 50.466 -5.847  -20.540 1.00 9.16   ? 106 GLU B CD  1 
ATOM   3158 O  OE1 . GLU B  1 107 ? 50.550 -6.629  -19.584 1.00 10.50  ? 106 GLU B OE1 1 
ATOM   3159 O  OE2 . GLU B  1 107 ? 49.524 -5.047  -20.696 1.00 9.93   ? 106 GLU B OE2 1 
ATOM   3160 N  N   . HIS B  1 108 ? 51.214 -6.790  -25.948 1.00 9.86   ? 107 HIS B N   1 
ATOM   3161 C  CA  . HIS B  1 108 ? 50.895 -7.302  -27.333 1.00 10.11  ? 107 HIS B CA  1 
ATOM   3162 C  C   . HIS B  1 108 ? 52.177 -7.708  -28.007 1.00 9.48   ? 107 HIS B C   1 
ATOM   3163 O  O   . HIS B  1 108 ? 53.261 -7.195  -27.727 1.00 10.37  ? 107 HIS B O   1 
ATOM   3164 C  CB  . HIS B  1 108 ? 50.176 -6.221  -28.084 1.00 10.16  ? 107 HIS B CB  1 
ATOM   3165 C  CG  . HIS B  1 108 ? 48.806 -5.947  -27.498 1.00 10.09  ? 107 HIS B CG  1 
ATOM   3166 N  ND1 . HIS B  1 108 ? 48.567 -5.051  -26.476 1.00 10.03  ? 107 HIS B ND1 1 
ATOM   3167 C  CD2 . HIS B  1 108 ? 47.602 -6.510  -27.770 1.00 10.86  ? 107 HIS B CD2 1 
ATOM   3168 C  CE1 . HIS B  1 108 ? 47.267 -5.145  -26.119 1.00 10.35  ? 107 HIS B CE1 1 
ATOM   3169 N  NE2 . HIS B  1 108 ? 46.646 -6.013  -26.922 1.00 10.92  ? 107 HIS B NE2 1 
ATOM   3170 N  N   . THR B  1 109 ? 52.023 -8.649  -28.930 1.00 10.98  ? 108 THR B N   1 
ATOM   3171 C  CA  . THR B  1 109 ? 53.103 -9.032  -29.834 1.00 11.48  ? 108 THR B CA  1 
ATOM   3172 C  C   . THR B  1 109 ? 52.518 -8.957  -31.254 1.00 11.17  ? 108 THR B C   1 
ATOM   3173 O  O   . THR B  1 109 ? 51.304 -8.989  -31.438 1.00 11.81  ? 108 THR B O   1 
ATOM   3174 C  CB  . THR B  1 109 ? 53.645 -10.431 -29.479 1.00 11.80  ? 108 THR B CB  1 
ATOM   3175 O  OG1 . THR B  1 109 ? 52.600 -11.400 -29.559 1.00 12.83  ? 108 THR B OG1 1 
ATOM   3176 C  CG2 . THR B  1 109 ? 54.191 -10.428 -28.100 1.00 12.58  ? 108 THR B CG2 1 
ATOM   3177 N  N   . VAL B  1 110 ? 53.418 -8.888  -32.222 1.00 12.25  ? 109 VAL B N   1 
ATOM   3178 C  CA  . VAL B  1 110 ? 52.990 -8.850  -33.641 1.00 12.69  ? 109 VAL B CA  1 
ATOM   3179 C  C   . VAL B  1 110 ? 53.731 -9.941  -34.355 1.00 13.21  ? 109 VAL B C   1 
ATOM   3180 O  O   . VAL B  1 110 ? 54.994 -9.844  -34.449 1.00 14.23  ? 109 VAL B O   1 
ATOM   3181 C  CB  . VAL B  1 110 ? 53.211 -7.395  -34.271 1.00 14.16  ? 109 VAL B CB  1 
ATOM   3182 C  CG1 . VAL B  1 110 ? 52.747 -7.369  -35.743 1.00 16.00  ? 109 VAL B CG1 1 
ATOM   3183 C  CG2 . VAL B  1 110 ? 52.555 -6.330  -33.433 1.00 14.06  ? 109 VAL B CG2 1 
ATOM   3184 N  N   . ASP B  1 111 ? 52.996 -10.855 -34.945 1.00 14.00  ? 110 ASP B N   1 
ATOM   3185 C  CA  . ASP B  1 111 ? 53.627 -11.983 -35.625 1.00 14.87  ? 110 ASP B CA  1 
ATOM   3186 C  C   . ASP B  1 111 ? 54.653 -12.657 -34.704 1.00 15.30  ? 110 ASP B C   1 
ATOM   3187 O  O   . ASP B  1 111 ? 55.702 -13.116 -35.170 1.00 17.38  ? 110 ASP B O   1 
ATOM   3188 C  CB  . ASP B  1 111 ? 54.229 -11.585 -36.967 1.00 16.20  ? 110 ASP B CB  1 
ATOM   3189 C  CG  . ASP B  1 111 ? 53.104 -11.153 -37.941 1.00 17.96  ? 110 ASP B CG  1 
ATOM   3190 O  OD1 . ASP B  1 111 ? 52.063 -11.837 -37.976 1.00 18.90  ? 110 ASP B OD1 1 
ATOM   3191 O  OD2 . ASP B  1 111 ? 53.245 -10.141 -38.689 1.00 19.25  ? 110 ASP B OD2 1 
ATOM   3192 N  N   . GLY B  1 112 ? 54.337 -12.768 -33.385 1.00 13.29  ? 111 GLY B N   1 
ATOM   3193 C  CA  . GLY B  1 112 ? 55.191 -13.427 -32.415 1.00 15.01  ? 111 GLY B CA  1 
ATOM   3194 C  C   . GLY B  1 112 ? 56.359 -12.604 -31.988 1.00 14.26  ? 111 GLY B C   1 
ATOM   3195 O  O   . GLY B  1 112 ? 57.078 -13.090 -31.108 1.00 16.86  ? 111 GLY B O   1 
ATOM   3196 N  N   . VAL B  1 113 ? 56.541 -11.399 -32.537 1.00 14.05  ? 112 VAL B N   1 
ATOM   3197 C  CA  . VAL B  1 113 ? 57.681 -10.557 -32.162 1.00 14.64  ? 112 VAL B CA  1 
ATOM   3198 C  C   . VAL B  1 113 ? 57.356 -9.807  -30.844 1.00 12.49  ? 112 VAL B C   1 
ATOM   3199 O  O   . VAL B  1 113 ? 56.308 -9.157  -30.795 1.00 13.56  ? 112 VAL B O   1 
ATOM   3200 C  CB  . VAL B  1 113 ? 58.037 -9.582  -33.297 1.00 16.49  ? 112 VAL B CB  1 
ATOM   3201 C  CG1 . VAL B  1 113 ? 59.244 -8.694  -32.820 1.00 16.75  ? 112 VAL B CG1 1 
ATOM   3202 C  CG2 . VAL B  1 113 ? 58.459 -10.362 -34.574 1.00 18.77  ? 112 VAL B CG2 1 
ATOM   3203 N  N   . LYS B  1 114 ? 58.204 -9.949  -29.858 1.00 13.62  ? 113 LYS B N   1 
ATOM   3204 C  CA  . LYS B  1 114 ? 58.035 -9.267  -28.592 1.00 12.98  ? 113 LYS B CA  1 
ATOM   3205 C  C   . LYS B  1 114 ? 58.915 -8.021  -28.575 1.00 12.13  ? 113 LYS B C   1 
ATOM   3206 O  O   . LYS B  1 114 ? 60.077 -8.050  -28.978 1.00 15.23  ? 113 LYS B O   1 
ATOM   3207 C  CB  . LYS B  1 114 ? 58.402 -10.190 -27.430 1.00 15.24  ? 113 LYS B CB  1 
ATOM   3208 C  CG  . LYS B  1 114 ? 57.908 -11.618 -27.593 1.00 17.76  ? 113 LYS B CG  1 
ATOM   3209 C  CD  . LYS B  1 114 ? 58.319 -12.483 -26.413 1.00 26.28  ? 113 LYS B CD  1 
ATOM   3210 C  CE  . LYS B  1 114 ? 59.801 -12.816 -26.461 1.00 26.98  ? 113 LYS B CE  1 
ATOM   3211 N  NZ  . LYS B  1 114 ? 60.204 -13.717 -25.347 1.00 54.89  ? 113 LYS B NZ  1 
ATOM   3212 N  N   . TYR B  1 115 ? 58.330 -6.917  -28.136 1.00 10.00  ? 114 TYR B N   1 
ATOM   3213 C  CA  . TYR B  1 115 ? 59.019 -5.657  -28.018 1.00 11.08  ? 114 TYR B CA  1 
ATOM   3214 C  C   . TYR B  1 115 ? 59.470 -5.489  -26.537 1.00 10.15  ? 114 TYR B C   1 
ATOM   3215 O  O   . TYR B  1 115 ? 59.189 -6.342  -25.695 1.00 10.71  ? 114 TYR B O   1 
ATOM   3216 C  CB  . TYR B  1 115 ? 58.141 -4.505  -28.576 1.00 10.63  ? 114 TYR B CB  1 
ATOM   3217 C  CG  . TYR B  1 115 ? 58.037 -4.658  -30.108 1.00 11.15  ? 114 TYR B CG  1 
ATOM   3218 C  CD1 . TYR B  1 115 ? 57.117 -5.521  -30.700 1.00 11.49  ? 114 TYR B CD1 1 
ATOM   3219 C  CD2 . TYR B  1 115 ? 58.893 -3.973  -30.920 1.00 15.39  ? 114 TYR B CD2 1 
ATOM   3220 C  CE1 . TYR B  1 115 ? 57.124 -5.732  -32.066 1.00 12.51  ? 114 TYR B CE1 1 
ATOM   3221 C  CE2 . TYR B  1 115 ? 58.862 -4.133  -32.296 1.00 17.07  ? 114 TYR B CE2 1 
ATOM   3222 C  CZ  . TYR B  1 115 ? 58.031 -5.050  -32.892 1.00 14.20  ? 114 TYR B CZ  1 
ATOM   3223 O  OH  . TYR B  1 115 ? 58.005 -5.228  -34.221 1.00 15.55  ? 114 TYR B OH  1 
ATOM   3224 N  N   A SER B  1 116 ? 60.152 -4.374  -26.263 0.50 10.14  ? 115 SER B N   1 
ATOM   3225 N  N   B SER B  1 116 ? 60.212 -4.404  -26.269 0.50 10.71  ? 115 SER B N   1 
ATOM   3226 C  CA  A SER B  1 116 ? 60.759 -4.243  -24.960 0.50 9.27   ? 115 SER B CA  1 
ATOM   3227 C  CA  B SER B  1 116 ? 60.821 -4.254  -24.960 0.50 10.60  ? 115 SER B CA  1 
ATOM   3228 C  C   A SER B  1 116 ? 59.865 -3.658  -23.920 0.50 9.21   ? 115 SER B C   1 
ATOM   3229 C  C   B SER B  1 116 ? 59.911 -3.615  -23.930 0.50 10.08  ? 115 SER B C   1 
ATOM   3230 O  O   A SER B  1 116 ? 60.082 -3.852  -22.719 0.50 10.50  ? 115 SER B O   1 
ATOM   3231 O  O   B SER B  1 116 ? 60.153 -3.750  -22.732 0.50 10.56  ? 115 SER B O   1 
ATOM   3232 C  CB  A SER B  1 116 ? 62.009 -3.406  -25.055 0.50 8.87   ? 115 SER B CB  1 
ATOM   3233 C  CB  B SER B  1 116 ? 62.131 -3.469  -25.096 0.50 15.63  ? 115 SER B CB  1 
ATOM   3234 O  OG  A SER B  1 116 ? 63.054 -4.058  -25.822 0.50 9.10   ? 115 SER B OG  1 
ATOM   3235 O  OG  B SER B  1 116 ? 61.834 -2.104  -25.528 0.50 16.40  ? 115 SER B OG  1 
ATOM   3236 N  N   . ALA B  1 117 ? 58.851 -2.933  -24.362 1.00 8.88   ? 116 ALA B N   1 
ATOM   3237 C  CA  . ALA B  1 117 ? 57.913 -2.289  -23.417 1.00 8.16   ? 116 ALA B CA  1 
ATOM   3238 C  C   . ALA B  1 117 ? 56.684 -1.903  -24.229 1.00 7.19   ? 116 ALA B C   1 
ATOM   3239 O  O   . ALA B  1 117 ? 56.642 -2.109  -25.465 1.00 8.24   ? 116 ALA B O   1 
ATOM   3240 C  CB  . ALA B  1 117 ? 58.579 -1.062  -22.752 1.00 8.81   ? 116 ALA B CB  1 
ATOM   3241 N  N   . GLU B  1 118 ? 55.698 -1.377  -23.533 1.00 7.73   ? 117 GLU B N   1 
ATOM   3242 C  CA  . GLU B  1 118 ? 54.480 -0.954  -24.204 1.00 7.61   ? 117 GLU B CA  1 
ATOM   3243 C  C   . GLU B  1 118 ? 53.880 0.231   -23.441 1.00 7.74   ? 117 GLU B C   1 
ATOM   3244 O  O   . GLU B  1 118 ? 53.805 0.175   -22.217 1.00 8.86   ? 117 GLU B O   1 
ATOM   3245 C  CB  . GLU B  1 118 ? 53.499 -2.138  -24.316 1.00 9.29   ? 117 GLU B CB  1 
ATOM   3246 C  CG  . GLU B  1 118 ? 52.232 -1.875  -25.094 1.00 9.59   ? 117 GLU B CG  1 
ATOM   3247 C  CD  . GLU B  1 118 ? 51.485 -3.150  -25.421 1.00 9.32   ? 117 GLU B CD  1 
ATOM   3248 O  OE1 . GLU B  1 118 ? 50.225 -3.103  -25.496 1.00 10.34  ? 117 GLU B OE1 1 
ATOM   3249 O  OE2 . GLU B  1 118 ? 52.127 -4.194  -25.648 1.00 9.77   ? 117 GLU B OE2 1 
ATOM   3250 N  N   . LEU B  1 119 ? 53.437 1.246   -24.176 1.00 7.73   ? 118 LEU B N   1 
ATOM   3251 C  CA  . LEU B  1 119 ? 52.727 2.396   -23.615 1.00 8.42   ? 118 LEU B CA  1 
ATOM   3252 C  C   . LEU B  1 119 ? 51.239 2.136   -23.761 1.00 8.16   ? 118 LEU B C   1 
ATOM   3253 O  O   . LEU B  1 119 ? 50.775 1.754   -24.855 1.00 8.57   ? 118 LEU B O   1 
ATOM   3254 C  CB  . LEU B  1 119 ? 53.141 3.628   -24.428 1.00 7.97   ? 118 LEU B CB  1 
ATOM   3255 C  CG  . LEU B  1 119 ? 52.248 4.868   -24.278 1.00 8.57   ? 118 LEU B CG  1 
ATOM   3256 C  CD1 . LEU B  1 119 ? 52.310 5.438   -22.842 1.00 9.69   ? 118 LEU B CD1 1 
ATOM   3257 C  CD2 . LEU B  1 119 ? 52.667 5.934   -25.257 1.00 10.62  ? 118 LEU B CD2 1 
ATOM   3258 N  N   . HIS B  1 120 ? 50.489 2.399   -22.689 1.00 8.00   ? 119 HIS B N   1 
ATOM   3259 C  CA  . HIS B  1 120 ? 49.014 2.358   -22.720 1.00 7.85   ? 119 HIS B CA  1 
ATOM   3260 C  C   . HIS B  1 120 ? 48.464 3.722   -22.387 1.00 7.88   ? 119 HIS B C   1 
ATOM   3261 O  O   . HIS B  1 120 ? 48.776 4.232   -21.293 1.00 8.71   ? 119 HIS B O   1 
ATOM   3262 C  CB  . HIS B  1 120 ? 48.518 1.308   -21.695 1.00 8.44   ? 119 HIS B CB  1 
ATOM   3263 C  CG  . HIS B  1 120 ? 48.753 -0.104  -22.130 1.00 7.97   ? 119 HIS B CG  1 
ATOM   3264 N  ND1 . HIS B  1 120 ? 48.690 -1.208  -21.290 1.00 8.15   ? 119 HIS B ND1 1 
ATOM   3265 C  CD2 . HIS B  1 120 ? 49.103 -0.559  -23.406 1.00 8.86   ? 119 HIS B CD2 1 
ATOM   3266 C  CE1 . HIS B  1 120 ? 48.970 -2.277  -22.035 1.00 8.39   ? 119 HIS B CE1 1 
ATOM   3267 N  NE2 . HIS B  1 120 ? 49.227 -1.900  -23.294 1.00 8.60   ? 119 HIS B NE2 1 
ATOM   3268 N  N   . VAL B  1 121 ? 47.621 4.249   -23.261 1.00 8.75   ? 120 VAL B N   1 
ATOM   3269 C  CA  . VAL B  1 121 ? 46.958 5.566   -23.009 1.00 9.11   ? 120 VAL B CA  1 
ATOM   3270 C  C   . VAL B  1 121 ? 45.456 5.197   -22.888 1.00 8.67   ? 120 VAL B C   1 
ATOM   3271 O  O   . VAL B  1 121 ? 44.842 4.759   -23.865 1.00 9.94   ? 120 VAL B O   1 
ATOM   3272 C  CB  . VAL B  1 121 ? 47.207 6.548   -24.147 1.00 9.66   ? 120 VAL B CB  1 
ATOM   3273 C  CG1 . VAL B  1 121 ? 46.617 7.921   -23.780 1.00 11.05  ? 120 VAL B CG1 1 
ATOM   3274 C  CG2 . VAL B  1 121 ? 48.692 6.698   -24.438 1.00 10.91  ? 120 VAL B CG2 1 
ATOM   3275 N  N   . ALA B  1 122 ? 44.917 5.356   -21.692 1.00 9.45   ? 121 ALA B N   1 
ATOM   3276 C  CA  . ALA B  1 122 ? 43.612 4.780   -21.338 1.00 10.60  ? 121 ALA B CA  1 
ATOM   3277 C  C   . ALA B  1 122 ? 42.553 5.857   -21.235 1.00 11.30  ? 121 ALA B C   1 
ATOM   3278 O  O   . ALA B  1 122 ? 42.795 6.966   -20.702 1.00 13.77  ? 121 ALA B O   1 
ATOM   3279 C  CB  . ALA B  1 122 ? 43.722 4.007   -20.041 1.00 12.60  ? 121 ALA B CB  1 
ATOM   3280 N  N   . HIS B  1 123 ? 41.332 5.496   -21.687 1.00 12.55  ? 122 HIS B N   1 
ATOM   3281 C  CA  . HIS B  1 123 ? 40.239 6.445   -21.806 1.00 13.24  ? 122 HIS B CA  1 
ATOM   3282 C  C   . HIS B  1 123 ? 38.944 5.727   -21.380 1.00 14.04  ? 122 HIS B C   1 
ATOM   3283 O  O   . HIS B  1 123 ? 38.812 4.520   -21.533 1.00 14.38  ? 122 HIS B O   1 
ATOM   3284 C  CB  . HIS B  1 123 ? 40.040 6.887   -23.243 1.00 13.64  ? 122 HIS B CB  1 
ATOM   3285 C  CG  . HIS B  1 123 ? 41.264 7.311   -23.968 1.00 12.04  ? 122 HIS B CG  1 
ATOM   3286 N  ND1 . HIS B  1 123 ? 42.264 6.440   -24.355 1.00 12.03  ? 122 HIS B ND1 1 
ATOM   3287 C  CD2 . HIS B  1 123 ? 41.669 8.547   -24.361 1.00 12.70  ? 122 HIS B CD2 1 
ATOM   3288 C  CE1 . HIS B  1 123 ? 43.200 7.141   -24.994 1.00 12.26  ? 122 HIS B CE1 1 
ATOM   3289 N  NE2 . HIS B  1 123 ? 42.895 8.442   -25.028 1.00 12.90  ? 122 HIS B NE2 1 
ATOM   3290 N  N   . TRP B  1 124 ? 37.911 6.524   -21.000 1.00 13.50  ? 123 TRP B N   1 
ATOM   3291 C  CA  . TRP B  1 124 ? 36.615 5.929   -20.646 1.00 14.64  ? 123 TRP B CA  1 
ATOM   3292 C  C   . TRP B  1 124 ? 35.487 6.601   -21.421 1.00 15.34  ? 123 TRP B C   1 
ATOM   3293 O  O   . TRP B  1 124 ? 35.600 7.754   -21.816 1.00 15.13  ? 123 TRP B O   1 
ATOM   3294 C  CB  . TRP B  1 124 ? 36.355 5.834   -19.140 1.00 14.74  ? 123 TRP B CB  1 
ATOM   3295 C  CG  . TRP B  1 124 ? 36.324 7.113   -18.399 1.00 15.52  ? 123 TRP B CG  1 
ATOM   3296 C  CD1 . TRP B  1 124 ? 37.386 7.745   -17.827 1.00 14.50  ? 123 TRP B CD1 1 
ATOM   3297 C  CD2 . TRP B  1 124 ? 35.170 7.907   -18.101 1.00 18.17  ? 123 TRP B CD2 1 
ATOM   3298 N  NE1 . TRP B  1 124 ? 36.973 8.883   -17.185 1.00 15.75  ? 123 TRP B NE1 1 
ATOM   3299 C  CE2 . TRP B  1 124 ? 35.628 9.029   -17.346 1.00 17.51  ? 123 TRP B CE2 1 
ATOM   3300 C  CE3 . TRP B  1 124 ? 33.804 7.797   -18.412 1.00 24.12  ? 123 TRP B CE3 1 
ATOM   3301 C  CZ2 . TRP B  1 124 ? 34.794 10.064  -16.915 1.00 22.35  ? 123 TRP B CZ2 1 
ATOM   3302 C  CZ3 . TRP B  1 124 ? 32.960 8.818   -17.920 1.00 27.22  ? 123 TRP B CZ3 1 
ATOM   3303 C  CH2 . TRP B  1 124 ? 33.477 9.905   -17.127 1.00 29.15  ? 123 TRP B CH2 1 
ATOM   3304 N  N   . ASN B  1 125 ? 34.384 5.888   -21.601 1.00 15.44  ? 124 ASN B N   1 
ATOM   3305 C  CA  . ASN B  1 125 ? 33.330 6.368   -22.444 1.00 17.75  ? 124 ASN B CA  1 
ATOM   3306 C  C   . ASN B  1 125 ? 32.398 7.339   -21.659 1.00 19.04  ? 124 ASN B C   1 
ATOM   3307 O  O   . ASN B  1 125 ? 31.461 6.899   -20.983 1.00 20.02  ? 124 ASN B O   1 
ATOM   3308 C  CB  . ASN B  1 125 ? 32.494 5.113   -22.879 1.00 16.91  ? 124 ASN B CB  1 
ATOM   3309 C  CG  . ASN B  1 125 ? 31.533 5.506   -24.011 1.00 20.05  ? 124 ASN B CG  1 
ATOM   3310 O  OD1 . ASN B  1 125 ? 31.046 6.631   -24.018 1.00 21.04  ? 124 ASN B OD1 1 
ATOM   3311 N  ND2 . ASN B  1 125 ? 31.100 4.559   -24.806 1.00 22.21  ? 124 ASN B ND2 1 
ATOM   3312 N  N   . SER B  1 126 ? 32.702 8.628   -21.791 1.00 22.49  ? 125 SER B N   1 
ATOM   3313 C  CA  . SER B  1 126 ? 31.921 9.631   -21.042 1.00 23.49  ? 125 SER B CA  1 
ATOM   3314 C  C   . SER B  1 126 ? 30.679 10.085  -21.904 1.00 27.84  ? 125 SER B C   1 
ATOM   3315 O  O   . SER B  1 126 ? 29.873 10.827  -21.379 1.00 27.82  ? 125 SER B O   1 
ATOM   3316 C  CB  . SER B  1 126 ? 32.831 10.796  -20.779 1.00 25.10  ? 125 SER B CB  1 
ATOM   3317 O  OG  . SER B  1 126 ? 33.250 11.411  -21.988 1.00 24.83  ? 125 SER B OG  1 
ATOM   3318 N  N   . ALA B  1 127 ? 30.506 9.552   -23.109 1.00 26.56  ? 126 ALA B N   1 
ATOM   3319 C  CA  . ALA B  1 127 ? 29.201 9.745   -23.879 1.00 28.85  ? 126 ALA B CA  1 
ATOM   3320 C  C   . ALA B  1 127 ? 28.129 8.900   -23.219 1.00 27.76  ? 126 ALA B C   1 
ATOM   3321 O  O   . ALA B  1 127 ? 26.974 9.341   -23.089 1.00 36.35  ? 126 ALA B O   1 
ATOM   3322 C  CB  . ALA B  1 127 ? 29.346 9.364   -25.337 1.00 30.45  ? 126 ALA B CB  1 
ATOM   3323 N  N   . LYS B  1 128 ? 28.447 7.681   -22.825 1.00 21.64  ? 127 LYS B N   1 
ATOM   3324 C  CA  . LYS B  1 128 ? 27.488 6.704   -22.304 1.00 23.04  ? 127 LYS B CA  1 
ATOM   3325 C  C   . LYS B  1 128 ? 27.406 6.670   -20.774 1.00 22.06  ? 127 LYS B C   1 
ATOM   3326 O  O   . LYS B  1 128 ? 26.350 6.345   -20.299 1.00 25.97  ? 127 LYS B O   1 
ATOM   3327 C  CB  . LYS B  1 128 ? 27.751 5.342   -22.836 1.00 27.07  ? 127 LYS B CB  1 
ATOM   3328 C  CG  . LYS B  1 128 ? 27.653 5.185   -24.334 1.00 33.36  ? 127 LYS B CG  1 
ATOM   3329 C  CD  . LYS B  1 128 ? 26.770 3.975   -24.616 1.00 54.16  ? 127 LYS B CD  1 
ATOM   3330 N  N   . TYR B  1 129 ? 28.526 6.868   -20.072 1.00 19.06  ? 128 TYR B N   1 
ATOM   3331 C  CA  . TYR B  1 129 ? 28.586 6.620   -18.605 1.00 21.56  ? 128 TYR B CA  1 
ATOM   3332 C  C   . TYR B  1 129 ? 29.049 7.909   -18.006 1.00 22.03  ? 128 TYR B C   1 
ATOM   3333 O  O   . TYR B  1 129 ? 29.562 8.850   -18.714 1.00 21.84  ? 128 TYR B O   1 
ATOM   3334 C  CB  . TYR B  1 129 ? 29.548 5.425   -18.306 1.00 18.02  ? 128 TYR B CB  1 
ATOM   3335 C  CG  . TYR B  1 129 ? 29.157 4.229   -19.115 1.00 19.10  ? 128 TYR B CG  1 
ATOM   3336 C  CD1 . TYR B  1 129 ? 27.948 3.538   -18.878 1.00 20.52  ? 128 TYR B CD1 1 
ATOM   3337 C  CD2 . TYR B  1 129 ? 29.960 3.719   -20.142 1.00 19.20  ? 128 TYR B CD2 1 
ATOM   3338 C  CE1 . TYR B  1 129 ? 27.563 2.488   -19.640 1.00 22.32  ? 128 TYR B CE1 1 
ATOM   3339 C  CE2 . TYR B  1 129 ? 29.585 2.622   -20.920 1.00 19.98  ? 128 TYR B CE2 1 
ATOM   3340 C  CZ  . TYR B  1 129 ? 28.367 2.050   -20.676 1.00 22.85  ? 128 TYR B CZ  1 
ATOM   3341 O  OH  . TYR B  1 129 ? 27.935 0.941   -21.409 1.00 23.32  ? 128 TYR B OH  1 
ATOM   3342 N  N   . SER B  1 130 ? 28.932 7.952   -16.703 1.00 22.93  ? 129 SER B N   1 
ATOM   3343 C  CA  . SER B  1 130 ? 29.229 9.180   -15.979 1.00 22.16  ? 129 SER B CA  1 
ATOM   3344 C  C   . SER B  1 130 ? 30.457 9.090   -15.070 1.00 24.28  ? 129 SER B C   1 
ATOM   3345 O  O   . SER B  1 130 ? 30.870 10.115  -14.534 1.00 26.30  ? 129 SER B O   1 
ATOM   3346 C  CB  . SER B  1 130 ? 28.027 9.534   -15.122 1.00 23.98  ? 129 SER B CB  1 
ATOM   3347 O  OG  . SER B  1 130 ? 26.940 9.898   -15.906 1.00 19.82  ? 129 SER B OG  1 
ATOM   3348 N  N   . SER B  1 131 ? 31.154 7.958   -15.026 1.00 24.63  ? 130 SER B N   1 
ATOM   3349 C  CA  . SER B  1 131 ? 32.299 7.817   -14.115 1.00 27.61  ? 130 SER B CA  1 
ATOM   3350 C  C   . SER B  1 131 ? 33.142 6.688   -14.791 1.00 21.74  ? 130 SER B C   1 
ATOM   3351 O  O   . SER B  1 131 ? 32.578 5.750   -15.412 1.00 22.89  ? 130 SER B O   1 
ATOM   3352 C  CB  . SER B  1 131 ? 31.960 7.391   -12.657 1.00 26.33  ? 130 SER B CB  1 
ATOM   3353 O  OG  . SER B  1 131 ? 31.317 6.171   -12.361 1.00 24.56  ? 130 SER B OG  1 
ATOM   3354 N  N   . LEU B  1 132 ? 34.400 6.688   -14.526 1.00 20.78  ? 131 LEU B N   1 
ATOM   3355 C  CA  . LEU B  1 132 ? 35.221 5.544   -14.791 1.00 17.27  ? 131 LEU B CA  1 
ATOM   3356 C  C   . LEU B  1 132 ? 34.708 4.285   -14.098 1.00 19.48  ? 131 LEU B C   1 
ATOM   3357 O  O   . LEU B  1 132 ? 34.649 3.226   -14.675 1.00 17.80  ? 131 LEU B O   1 
ATOM   3358 C  CB  . LEU B  1 132 ? 36.691 5.841   -14.456 1.00 18.17  ? 131 LEU B CB  1 
ATOM   3359 C  CG  . LEU B  1 132 ? 37.626 4.643   -14.417 1.00 16.77  ? 131 LEU B CG  1 
ATOM   3360 C  CD1 . LEU B  1 132 ? 37.764 4.117   -15.892 1.00 20.78  ? 131 LEU B CD1 1 
ATOM   3361 C  CD2 . LEU B  1 132 ? 39.013 5.045   -13.955 1.00 17.05  ? 131 LEU B CD2 1 
ATOM   3362 N  N   . ALA B  1 133 ? 34.301 4.436   -12.806 1.00 19.74  ? 132 ALA B N   1 
ATOM   3363 C  CA  . ALA B  1 133 ? 33.794 3.259   -12.110 1.00 23.32  ? 132 ALA B CA  1 
ATOM   3364 C  C   . ALA B  1 133 ? 32.590 2.650   -12.792 1.00 19.72  ? 132 ALA B C   1 
ATOM   3365 O  O   . ALA B  1 133 ? 32.495 1.381   -12.829 1.00 20.55  ? 132 ALA B O   1 
ATOM   3366 C  CB  . ALA B  1 133 ? 33.445 3.647   -10.632 1.00 31.35  ? 132 ALA B CB  1 
ATOM   3367 N  N   . GLU B  1 134 ? 31.690 3.482   -13.337 1.00 21.44  ? 133 GLU B N   1 
ATOM   3368 C  CA  . GLU B  1 134 ? 30.538 2.958   -14.094 1.00 21.66  ? 133 GLU B CA  1 
ATOM   3369 C  C   . GLU B  1 134 ? 31.002 2.318   -15.473 1.00 18.66  ? 133 GLU B C   1 
ATOM   3370 O  O   . GLU B  1 134 ? 30.541 1.211   -15.827 1.00 20.17  ? 133 GLU B O   1 
ATOM   3371 C  CB  . GLU B  1 134 ? 29.576 4.081   -14.386 1.00 23.50  ? 133 GLU B CB  1 
ATOM   3372 C  CG  . GLU B  1 134 ? 28.297 3.592   -15.084 1.00 22.68  ? 133 GLU B CG  1 
ATOM   3373 C  CD  . GLU B  1 134 ? 27.388 4.774   -15.499 1.00 27.98  ? 133 GLU B CD  1 
ATOM   3374 O  OE1 . GLU B  1 134 ? 27.721 5.942   -15.207 1.00 26.12  ? 133 GLU B OE1 1 
ATOM   3375 O  OE2 . GLU B  1 134 ? 26.309 4.482   -16.024 1.00 26.08  ? 133 GLU B OE2 1 
ATOM   3376 N  N   . ALA B  1 135 ? 31.925 2.963   -16.124 1.00 17.13  ? 134 ALA B N   1 
ATOM   3377 C  CA  . ALA B  1 135 ? 32.354 2.455   -17.427 1.00 16.42  ? 134 ALA B CA  1 
ATOM   3378 C  C   . ALA B  1 135 ? 33.220 1.208   -17.380 1.00 15.17  ? 134 ALA B C   1 
ATOM   3379 O  O   . ALA B  1 135 ? 33.255 0.465   -18.389 1.00 15.46  ? 134 ALA B O   1 
ATOM   3380 C  CB  . ALA B  1 135 ? 33.139 3.598   -18.105 1.00 16.47  ? 134 ALA B CB  1 
ATOM   3381 N  N   . ALA B  1 136 ? 34.001 1.017   -16.347 1.00 14.66  ? 135 ALA B N   1 
ATOM   3382 C  CA  . ALA B  1 136 ? 35.130 0.103   -16.427 1.00 15.57  ? 135 ALA B CA  1 
ATOM   3383 C  C   . ALA B  1 136 ? 34.673 -1.346  -16.590 1.00 15.93  ? 135 ALA B C   1 
ATOM   3384 O  O   . ALA B  1 136 ? 35.510 -2.156  -17.047 1.00 16.86  ? 135 ALA B O   1 
ATOM   3385 C  CB  . ALA B  1 136 ? 35.998 0.275   -15.207 1.00 17.74  ? 135 ALA B CB  1 
ATOM   3386 N  N   . SER B  1 137 ? 33.441 -1.712  -16.262 1.00 17.49  ? 136 SER B N   1 
ATOM   3387 C  CA  . SER B  1 137 ? 32.984 -3.115  -16.326 1.00 19.72  ? 136 SER B CA  1 
ATOM   3388 C  C   . SER B  1 137 ? 32.091 -3.319  -17.514 1.00 19.40  ? 136 SER B C   1 
ATOM   3389 O  O   . SER B  1 137 ? 31.546 -4.415  -17.664 1.00 22.81  ? 136 SER B O   1 
ATOM   3390 C  CB  . SER B  1 137 ? 32.233 -3.450  -15.052 1.00 24.92  ? 136 SER B CB  1 
ATOM   3391 O  OG  . SER B  1 137 ? 31.148 -2.511  -14.953 1.00 25.98  ? 136 SER B OG  1 
ATOM   3392 N  N   . LYS B  1 138 ? 31.920 -2.279  -18.416 1.00 16.23  ? 137 LYS B N   1 
ATOM   3393 C  CA  . LYS B  1 138 ? 30.994 -2.313  -19.584 1.00 17.24  ? 137 LYS B CA  1 
ATOM   3394 C  C   . LYS B  1 138 ? 31.786 -2.691  -20.843 1.00 16.50  ? 137 LYS B C   1 
ATOM   3395 O  O   . LYS B  1 138 ? 32.889 -2.160  -21.051 1.00 15.02  ? 137 LYS B O   1 
ATOM   3396 C  CB  . LYS B  1 138 ? 30.366 -0.931  -19.792 1.00 17.70  ? 137 LYS B CB  1 
ATOM   3397 C  CG  . LYS B  1 138 ? 29.616 -0.418  -18.523 1.00 21.86  ? 137 LYS B CG  1 
ATOM   3398 C  CD  . LYS B  1 138 ? 28.410 -1.300  -18.097 1.00 25.13  ? 137 LYS B CD  1 
ATOM   3399 C  CE  . LYS B  1 138 ? 27.578 -0.569  -16.912 1.00 28.55  ? 137 LYS B CE  1 
ATOM   3400 N  NZ  . LYS B  1 138 ? 28.413 -0.714  -15.644 1.00 27.16  ? 137 LYS B NZ  1 
ATOM   3401 N  N   . ALA B  1 139 ? 31.135 -3.409  -21.782 1.00 16.96  ? 138 ALA B N   1 
ATOM   3402 C  CA  . ALA B  1 139 ? 31.875 -3.874  -22.953 1.00 15.53  ? 138 ALA B CA  1 
ATOM   3403 C  C   . ALA B  1 139 ? 32.388 -2.731  -23.796 1.00 14.52  ? 138 ALA B C   1 
ATOM   3404 O  O   . ALA B  1 139 ? 33.447 -2.802  -24.413 1.00 15.06  ? 138 ALA B O   1 
ATOM   3405 C  CB  . ALA B  1 139 ? 30.946 -4.774  -23.813 1.00 17.98  ? 138 ALA B CB  1 
ATOM   3406 N  N   . ASP B  1 140 ? 31.621 -1.600  -23.843 1.00 15.77  ? 139 ASP B N   1 
ATOM   3407 C  CA  . ASP B  1 140 ? 31.967 -0.443  -24.563 1.00 15.81  ? 139 ASP B CA  1 
ATOM   3408 C  C   . ASP B  1 140 ? 32.564 0.650   -23.645 1.00 15.51  ? 139 ASP B C   1 
ATOM   3409 O  O   . ASP B  1 140 ? 32.581 1.826   -24.048 1.00 16.15  ? 139 ASP B O   1 
ATOM   3410 C  CB  . ASP B  1 140 ? 30.803 0.119   -25.386 1.00 19.25  ? 139 ASP B CB  1 
ATOM   3411 C  CG  . ASP B  1 140 ? 29.656 0.527   -24.496 1.00 20.46  ? 139 ASP B CG  1 
ATOM   3412 O  OD1 . ASP B  1 140 ? 29.679 0.245   -23.299 1.00 21.55  ? 139 ASP B OD1 1 
ATOM   3413 O  OD2 . ASP B  1 140 ? 28.624 1.022   -25.005 1.00 28.97  ? 139 ASP B OD2 1 
ATOM   3414 N  N   . GLY B  1 141 ? 33.021 0.290   -22.456 1.00 14.39  ? 140 GLY B N   1 
ATOM   3415 C  CA  . GLY B  1 141 ? 33.342 1.315   -21.448 1.00 14.67  ? 140 GLY B CA  1 
ATOM   3416 C  C   . GLY B  1 141 ? 34.710 1.990   -21.657 1.00 13.61  ? 140 GLY B C   1 
ATOM   3417 O  O   . GLY B  1 141 ? 34.833 3.163   -21.276 1.00 15.12  ? 140 GLY B O   1 
ATOM   3418 N  N   . LEU B  1 142 ? 35.715 1.239   -22.130 1.00 13.30  ? 141 LEU B N   1 
ATOM   3419 C  CA  . LEU B  1 142 ? 37.139 1.710   -22.071 1.00 12.49  ? 141 LEU B CA  1 
ATOM   3420 C  C   . LEU B  1 142 ? 37.726 1.636   -23.451 1.00 11.85  ? 141 LEU B C   1 
ATOM   3421 O  O   . LEU B  1 142 ? 37.389 0.761   -24.286 1.00 12.85  ? 141 LEU B O   1 
ATOM   3422 C  CB  . LEU B  1 142 ? 38.003 0.885   -21.113 1.00 12.63  ? 141 LEU B CB  1 
ATOM   3423 C  CG  . LEU B  1 142 ? 37.448 0.854   -19.655 1.00 13.77  ? 141 LEU B CG  1 
ATOM   3424 C  CD1 . LEU B  1 142 ? 38.408 0.020   -18.844 1.00 13.64  ? 141 LEU B CD1 1 
ATOM   3425 C  CD2 . LEU B  1 142 ? 37.284 2.277   -19.027 1.00 16.09  ? 141 LEU B CD2 1 
ATOM   3426 N  N   . ALA B  1 143 ? 38.676 2.544   -23.739 1.00 12.79  ? 142 ALA B N   1 
ATOM   3427 C  CA  . ALA B  1 143 ? 39.475 2.483   -24.959 1.00 12.83  ? 142 ALA B CA  1 
ATOM   3428 C  C   . ALA B  1 143 ? 40.907 2.729   -24.543 1.00 11.76  ? 142 ALA B C   1 
ATOM   3429 O  O   . ALA B  1 143 ? 41.204 3.698   -23.872 1.00 12.93  ? 142 ALA B O   1 
ATOM   3430 C  CB  . ALA B  1 143 ? 39.033 3.552   -25.926 1.00 13.61  ? 142 ALA B CB  1 
ATOM   3431 N  N   . VAL B  1 144 ? 41.787 1.831   -25.016 1.00 11.06  ? 143 VAL B N   1 
ATOM   3432 C  CA  . VAL B  1 144 ? 43.207 1.994   -24.655 1.00 10.92  ? 143 VAL B CA  1 
ATOM   3433 C  C   . VAL B  1 144 ? 43.996 1.965   -25.972 1.00 11.24  ? 143 VAL B C   1 
ATOM   3434 O  O   . VAL B  1 144 ? 43.838 1.061   -26.810 1.00 11.40  ? 143 VAL B O   1 
ATOM   3435 C  CB  . VAL B  1 144 ? 43.713 0.937   -23.706 1.00 11.09  ? 143 VAL B CB  1 
ATOM   3436 C  CG1 . VAL B  1 144 ? 45.162 1.172   -23.312 1.00 12.14  ? 143 VAL B CG1 1 
ATOM   3437 C  CG2 . VAL B  1 144 ? 42.821 0.869   -22.431 1.00 12.76  ? 143 VAL B CG2 1 
ATOM   3438 N  N   . ILE B  1 145 ? 44.867 2.991   -26.173 1.00 9.94   ? 144 ILE B N   1 
ATOM   3439 C  CA  . ILE B  1 145 ? 45.848 2.956   -27.217 1.00 10.07  ? 144 ILE B CA  1 
ATOM   3440 C  C   . ILE B  1 145 ? 47.080 2.300   -26.695 1.00 9.89   ? 144 ILE B C   1 
ATOM   3441 O  O   . ILE B  1 145 ? 47.630 2.720   -25.683 1.00 10.80  ? 144 ILE B O   1 
ATOM   3442 C  CB  . ILE B  1 145 ? 46.192 4.387   -27.681 1.00 10.86  ? 144 ILE B CB  1 
ATOM   3443 C  CG1 . ILE B  1 145 ? 44.938 5.138   -28.161 1.00 12.74  ? 144 ILE B CG1 1 
ATOM   3444 C  CG2 . ILE B  1 145 ? 47.266 4.343   -28.791 1.00 12.27  ? 144 ILE B CG2 1 
ATOM   3445 C  CD1 . ILE B  1 145 ? 45.210 6.644   -28.411 1.00 15.30  ? 144 ILE B CD1 1 
ATOM   3446 N  N   . GLY B  1 146 ? 47.549 1.268   -27.426 1.00 9.17   ? 145 GLY B N   1 
ATOM   3447 C  CA  . GLY B  1 146 ? 48.821 0.594   -27.139 1.00 9.65   ? 145 GLY B CA  1 
ATOM   3448 C  C   . GLY B  1 146 ? 49.844 0.907   -28.153 1.00 9.38   ? 145 GLY B C   1 
ATOM   3449 O  O   . GLY B  1 146 ? 49.597 0.864   -29.356 1.00 10.94  ? 145 GLY B O   1 
ATOM   3450 N  N   . VAL B  1 147 ? 51.056 1.242   -27.684 1.00 9.53   ? 146 VAL B N   1 
ATOM   3451 C  CA  . VAL B  1 147 ? 52.181 1.562   -28.545 1.00 9.24   ? 146 VAL B CA  1 
ATOM   3452 C  C   . VAL B  1 147 ? 53.314 0.674   -28.161 1.00 8.47   ? 146 VAL B C   1 
ATOM   3453 O  O   . VAL B  1 147 ? 53.786 0.687   -26.996 1.00 9.60   ? 146 VAL B O   1 
ATOM   3454 C  CB  . VAL B  1 147 ? 52.614 3.049   -28.460 1.00 9.61   ? 146 VAL B CB  1 
ATOM   3455 C  CG1 . VAL B  1 147 ? 53.741 3.269   -29.468 1.00 11.93  ? 146 VAL B CG1 1 
ATOM   3456 C  CG2 . VAL B  1 147 ? 51.436 3.993   -28.649 1.00 11.81  ? 146 VAL B CG2 1 
ATOM   3457 N  N   . LEU B  1 148 ? 53.791 -0.171  -29.085 1.00 9.03   ? 147 LEU B N   1 
ATOM   3458 C  CA  . LEU B  1 148 ? 54.940 -1.019  -28.853 1.00 8.79   ? 147 LEU B CA  1 
ATOM   3459 C  C   . LEU B  1 148 ? 56.203 -0.188  -28.772 1.00 8.17   ? 147 LEU B C   1 
ATOM   3460 O  O   . LEU B  1 148 ? 56.362 0.782   -29.567 1.00 9.20   ? 147 LEU B O   1 
ATOM   3461 C  CB  . LEU B  1 148 ? 55.055 -2.042  -29.983 1.00 10.01  ? 147 LEU B CB  1 
ATOM   3462 C  CG  . LEU B  1 148 ? 53.804 -3.010  -30.006 1.00 13.43  ? 147 LEU B CG  1 
ATOM   3463 C  CD1 . LEU B  1 148 ? 53.624 -3.592  -31.343 1.00 16.88  ? 147 LEU B CD1 1 
ATOM   3464 C  CD2 . LEU B  1 148 ? 53.871 -3.938  -28.860 1.00 12.42  ? 147 LEU B CD2 1 
ATOM   3465 N  N   . MET B  1 149 ? 57.084 -0.513  -27.815 1.00 8.62   ? 148 MET B N   1 
ATOM   3466 C  CA  . MET B  1 149 ? 58.308 0.272   -27.624 1.00 8.30   ? 148 MET B CA  1 
ATOM   3467 C  C   . MET B  1 149 ? 59.499 -0.635  -27.929 1.00 8.09   ? 148 MET B C   1 
ATOM   3468 O  O   . MET B  1 149 ? 59.674 -1.708  -27.310 1.00 9.21   ? 148 MET B O   1 
ATOM   3469 C  CB  . MET B  1 149 ? 58.362 0.769   -26.168 1.00 8.45   ? 148 MET B CB  1 
ATOM   3470 C  CG  . MET B  1 149 ? 57.182 1.725   -25.907 1.00 8.98   ? 148 MET B CG  1 
ATOM   3471 S  SD  . MET B  1 149 ? 57.034 2.273   -24.197 1.00 9.36   ? 148 MET B SD  1 
ATOM   3472 C  CE  . MET B  1 149 ? 58.525 3.201   -24.000 1.00 12.26  ? 148 MET B CE  1 
ATOM   3473 N  N   . LYS B  1 150 ? 60.244 -0.233  -28.950 1.00 8.81   ? 149 LYS B N   1 
ATOM   3474 C  CA  . LYS B  1 150 ? 61.339 -1.008  -29.517 1.00 8.80   ? 149 LYS B CA  1 
ATOM   3475 C  C   . LYS B  1 150 ? 62.661 -0.474  -29.000 1.00 8.49   ? 149 LYS B C   1 
ATOM   3476 O  O   . LYS B  1 150 ? 62.975 0.712   -29.128 1.00 9.06   ? 149 LYS B O   1 
ATOM   3477 C  CB  . LYS B  1 150 ? 61.315 -0.833  -31.024 1.00 10.47  ? 149 LYS B CB  1 
ATOM   3478 C  CG  . LYS B  1 150 ? 62.335 -1.660  -31.696 1.00 11.76  ? 149 LYS B CG  1 
ATOM   3479 C  CD  . LYS B  1 150 ? 62.288 -1.362  -33.289 1.00 14.79  ? 149 LYS B CD  1 
ATOM   3480 C  CE  . LYS B  1 150 ? 63.063 -2.388  -34.037 1.00 16.67  ? 149 LYS B CE  1 
ATOM   3481 N  NZ  . LYS B  1 150 ? 64.444 -2.355  -33.714 1.00 15.16  ? 149 LYS B NZ  1 
ATOM   3482 N  N   . VAL B  1 151 ? 63.469 -1.350  -28.364 1.00 8.98   ? 150 VAL B N   1 
ATOM   3483 C  CA  . VAL B  1 151 ? 64.754 -0.900  -27.813 1.00 9.64   ? 150 VAL B CA  1 
ATOM   3484 C  C   . VAL B  1 151 ? 65.622 -0.366  -28.912 1.00 9.00   ? 150 VAL B C   1 
ATOM   3485 O  O   . VAL B  1 151 ? 65.758 -0.989  -29.976 1.00 10.70  ? 150 VAL B O   1 
ATOM   3486 C  CB  . VAL B  1 151 ? 65.400 -1.940  -26.927 1.00 10.56  ? 150 VAL B CB  1 
ATOM   3487 C  CG1 . VAL B  1 151 ? 65.837 -3.206  -27.705 1.00 13.00  ? 150 VAL B CG1 1 
ATOM   3488 C  CG2 . VAL B  1 151 ? 66.546 -1.315  -26.099 1.00 12.66  ? 150 VAL B CG2 1 
ATOM   3489 N  N   . GLY B  1 152 ? 66.261 0.774   -28.685 1.00 10.04  ? 151 GLY B N   1 
ATOM   3490 C  CA  . GLY B  1 152 ? 67.089 1.404   -29.665 1.00 11.46  ? 151 GLY B CA  1 
ATOM   3491 C  C   . GLY B  1 152 ? 67.543 2.742   -29.103 1.00 10.51  ? 151 GLY B C   1 
ATOM   3492 O  O   . GLY B  1 152 ? 68.040 2.812   -27.942 1.00 11.69  ? 151 GLY B O   1 
ATOM   3493 N  N   . GLU B  1 153 ? 67.425 3.809   -29.854 1.00 11.68  ? 152 GLU B N   1 
ATOM   3494 C  CA  . GLU B  1 153 ? 67.923 5.122   -29.403 1.00 12.52  ? 152 GLU B CA  1 
ATOM   3495 C  C   . GLU B  1 153 ? 67.033 5.618   -28.262 1.00 10.33  ? 152 GLU B C   1 
ATOM   3496 O  O   . GLU B  1 153 ? 65.812 5.368   -28.203 1.00 11.95  ? 152 GLU B O   1 
ATOM   3497 C  CB  . GLU B  1 153 ? 67.862 6.091   -30.552 1.00 15.22  ? 152 GLU B CB  1 
ATOM   3498 C  CG  . GLU B  1 153 ? 68.857 5.792   -31.686 1.00 18.70  ? 152 GLU B CG  1 
ATOM   3499 C  CD  . GLU B  1 153 ? 70.300 5.712   -31.187 1.00 30.82  ? 152 GLU B CD  1 
ATOM   3500 O  OE1 . GLU B  1 153 ? 70.809 6.626   -30.528 1.00 41.17  ? 152 GLU B OE1 1 
ATOM   3501 O  OE2 . GLU B  1 153 ? 70.953 4.734   -31.516 1.00 46.20  ? 152 GLU B OE2 1 
ATOM   3502 N  N   . ALA B  1 154 ? 67.624 6.383   -27.381 1.00 11.54  ? 153 ALA B N   1 
ATOM   3503 C  CA  . ALA B  1 154 ? 66.848 7.009   -26.306 1.00 11.77  ? 153 ALA B CA  1 
ATOM   3504 C  C   . ALA B  1 154 ? 65.729 7.871   -26.905 1.00 10.57  ? 153 ALA B C   1 
ATOM   3505 O  O   . ALA B  1 154 ? 65.931 8.539   -27.921 1.00 13.38  ? 153 ALA B O   1 
ATOM   3506 C  CB  . ALA B  1 154 ? 67.781 7.889   -25.453 1.00 13.79  ? 153 ALA B CB  1 
ATOM   3507 N  N   . ASN B  1 155 ? 64.588 7.859   -26.247 1.00 10.61  ? 154 ASN B N   1 
ATOM   3508 C  CA  . ASN B  1 155 ? 63.431 8.619   -26.708 1.00 11.06  ? 154 ASN B CA  1 
ATOM   3509 C  C   . ASN B  1 155 ? 63.342 9.886   -25.872 1.00 10.80  ? 154 ASN B C   1 
ATOM   3510 O  O   . ASN B  1 155 ? 62.993 9.809   -24.696 1.00 10.76  ? 154 ASN B O   1 
ATOM   3511 C  CB  . ASN B  1 155 ? 62.200 7.760   -26.541 1.00 11.15  ? 154 ASN B CB  1 
ATOM   3512 C  CG  . ASN B  1 155 ? 60.978 8.370   -27.098 1.00 12.33  ? 154 ASN B CG  1 
ATOM   3513 O  OD1 . ASN B  1 155 ? 60.882 9.605   -27.178 1.00 15.89  ? 154 ASN B OD1 1 
ATOM   3514 N  ND2 . ASN B  1 155 ? 59.965 7.554   -27.419 1.00 12.49  ? 154 ASN B ND2 1 
ATOM   3515 N  N   . PRO B  1 156 ? 63.627 11.084  -26.416 1.00 12.09  ? 155 PRO B N   1 
ATOM   3516 C  CA  . PRO B  1 156 ? 63.636 12.301  -25.563 1.00 13.47  ? 155 PRO B CA  1 
ATOM   3517 C  C   . PRO B  1 156 ? 62.261 12.652  -25.128 1.00 12.43  ? 155 PRO B C   1 
ATOM   3518 O  O   . PRO B  1 156 ? 62.128 13.366  -24.116 1.00 13.81  ? 155 PRO B O   1 
ATOM   3519 C  CB  . PRO B  1 156 ? 64.249 13.373  -26.477 1.00 15.64  ? 155 PRO B CB  1 
ATOM   3520 C  CG  . PRO B  1 156 ? 64.008 12.808  -27.895 1.00 23.49  ? 155 PRO B CG  1 
ATOM   3521 C  CD  . PRO B  1 156 ? 64.038 11.346  -27.822 1.00 14.88  ? 155 PRO B CD  1 
ATOM   3522 N  N   . LYS B  1 157 ? 61.201 12.158  -25.743 1.00 13.01  ? 156 LYS B N   1 
ATOM   3523 C  CA  . LYS B  1 157 ? 59.846 12.564  -25.340 1.00 14.33  ? 156 LYS B CA  1 
ATOM   3524 C  C   . LYS B  1 157 ? 59.507 11.850  -24.026 1.00 12.30  ? 156 LYS B C   1 
ATOM   3525 O  O   . LYS B  1 157 ? 58.548 12.281  -23.371 1.00 15.22  ? 156 LYS B O   1 
ATOM   3526 C  CB  . LYS B  1 157 ? 58.881 12.117  -26.441 1.00 17.97  ? 156 LYS B CB  1 
ATOM   3527 C  CG  . LYS B  1 157 ? 59.213 12.880  -27.761 1.00 29.28  ? 156 LYS B CG  1 
ATOM   3528 C  CD  . LYS B  1 157 ? 58.033 13.405  -28.442 1.00 42.29  ? 156 LYS B CD  1 
ATOM   3529 C  CE  . LYS B  1 157 ? 58.061 13.428  -29.979 1.00 51.78  ? 156 LYS B CE  1 
ATOM   3530 N  NZ  . LYS B  1 157 ? 56.673 13.274  -30.756 1.00 40.64  ? 156 LYS B NZ  1 
ATOM   3531 N  N   . LEU B  1 158 ? 60.234 10.839  -23.609 1.00 12.67  ? 157 LEU B N   1 
ATOM   3532 C  CA  . LEU B  1 158 ? 60.066 10.241  -22.249 1.00 12.03  ? 157 LEU B CA  1 
ATOM   3533 C  C   . LEU B  1 158 ? 60.686 11.118  -21.144 1.00 12.70  ? 157 LEU B C   1 
ATOM   3534 O  O   . LEU B  1 158 ? 60.493 10.669  -20.009 1.00 13.31  ? 157 LEU B O   1 
ATOM   3535 C  CB  . LEU B  1 158 ? 60.670 8.860   -22.254 1.00 12.46  ? 157 LEU B CB  1 
ATOM   3536 C  CG  . LEU B  1 158 ? 60.009 7.940   -23.232 1.00 11.18  ? 157 LEU B CG  1 
ATOM   3537 C  CD1 . LEU B  1 158 ? 60.775 6.491   -23.113 1.00 15.70  ? 157 LEU B CD1 1 
ATOM   3538 C  CD2 . LEU B  1 158 ? 58.510 7.639   -22.829 1.00 19.22  ? 157 LEU B CD2 1 
ATOM   3539 N  N   . GLN B  1 159 ? 61.405 12.176  -21.426 1.00 12.37  ? 158 GLN B N   1 
ATOM   3540 C  CA  . GLN B  1 159 ? 62.278 12.734  -20.368 1.00 15.33  ? 158 GLN B CA  1 
ATOM   3541 C  C   . GLN B  1 159 ? 61.463 13.268  -19.135 1.00 12.68  ? 158 GLN B C   1 
ATOM   3542 O  O   . GLN B  1 159 ? 61.949 12.990  -18.040 1.00 13.14  ? 158 GLN B O   1 
ATOM   3543 C  CB  . GLN B  1 159 ? 63.082 13.951  -20.992 1.00 13.85  ? 158 GLN B CB  1 
ATOM   3544 C  CG  . GLN B  1 159 ? 64.201 14.358  -20.069 1.00 17.71  ? 158 GLN B CG  1 
ATOM   3545 C  CD  . GLN B  1 159 ? 65.225 13.194  -19.970 1.00 24.32  ? 158 GLN B CD  1 
ATOM   3546 O  OE1 . GLN B  1 159 ? 65.633 12.600  -21.006 1.00 21.29  ? 158 GLN B OE1 1 
ATOM   3547 N  NE2 . GLN B  1 159 ? 65.638 12.876  -18.808 1.00 26.47  ? 158 GLN B NE2 1 
ATOM   3548 N  N   . LYS B  1 160 ? 60.334 13.906  -19.340 1.00 11.41  ? 159 LYS B N   1 
ATOM   3549 C  CA  . LYS B  1 160 ? 59.642 14.466  -18.207 1.00 12.16  ? 159 LYS B CA  1 
ATOM   3550 C  C   . LYS B  1 160 ? 59.240 13.298  -17.318 1.00 9.87   ? 159 LYS B C   1 
ATOM   3551 O  O   . LYS B  1 160 ? 59.268 13.353  -16.084 1.00 12.00  ? 159 LYS B O   1 
ATOM   3552 C  CB  . LYS B  1 160 ? 58.454 15.278  -18.678 1.00 13.25  ? 159 LYS B CB  1 
ATOM   3553 C  CG  . LYS B  1 160 ? 57.708 15.968  -17.456 1.00 14.84  ? 159 LYS B CG  1 
ATOM   3554 C  CD  . LYS B  1 160 ? 56.349 16.545  -17.850 1.00 15.71  ? 159 LYS B CD  1 
ATOM   3555 C  CE  . LYS B  1 160 ? 55.477 16.986  -16.606 1.00 15.74  ? 159 LYS B CE  1 
ATOM   3556 N  NZ  . LYS B  1 160 ? 56.086 18.321  -16.205 1.00 17.52  ? 159 LYS B NZ  1 
ATOM   3557 N  N   . VAL B  1 161 ? 58.695 12.179  -17.959 1.00 11.76  ? 160 VAL B N   1 
ATOM   3558 C  CA  . VAL B  1 161 ? 58.224 11.080  -17.237 1.00 10.55  ? 160 VAL B CA  1 
ATOM   3559 C  C   . VAL B  1 161 ? 59.322 10.456  -16.451 1.00 9.85   ? 160 VAL B C   1 
ATOM   3560 O  O   . VAL B  1 161 ? 59.243 10.245  -15.240 1.00 11.36  ? 160 VAL B O   1 
ATOM   3561 C  CB  . VAL B  1 161 ? 57.588 10.033  -18.128 1.00 10.90  ? 160 VAL B CB  1 
ATOM   3562 C  CG1 . VAL B  1 161 ? 57.206 8.871   -17.297 1.00 19.60  ? 160 VAL B CG1 1 
ATOM   3563 C  CG2 . VAL B  1 161 ? 56.351 10.582  -18.832 1.00 17.11  ? 160 VAL B CG2 1 
ATOM   3564 N  N   . LEU B  1 162 ? 60.465 10.175  -17.111 1.00 10.42  ? 161 LEU B N   1 
ATOM   3565 C  CA  . LEU B  1 162 ? 61.556 9.489   -16.411 1.00 11.99  ? 161 LEU B CA  1 
ATOM   3566 C  C   . LEU B  1 162 ? 62.166 10.388  -15.328 1.00 11.14  ? 161 LEU B C   1 
ATOM   3567 O  O   . LEU B  1 162 ? 62.507 9.829   -14.276 1.00 12.57  ? 161 LEU B O   1 
ATOM   3568 C  CB  . LEU B  1 162 ? 62.681 9.197   -17.490 1.00 15.42  ? 161 LEU B CB  1 
ATOM   3569 C  CG  . LEU B  1 162 ? 62.276 8.238   -18.498 1.00 14.73  ? 161 LEU B CG  1 
ATOM   3570 C  CD1 . LEU B  1 162 ? 63.247 8.255   -19.662 1.00 17.20  ? 161 LEU B CD1 1 
ATOM   3571 C  CD2 . LEU B  1 162 ? 62.123 6.883   -17.881 1.00 19.44  ? 161 LEU B CD2 1 
ATOM   3572 N  N   . ASP B  1 163 ? 62.224 11.691  -15.552 1.00 11.41  ? 162 ASP B N   1 
ATOM   3573 C  CA  . ASP B  1 163 ? 62.770 12.593  -14.561 1.00 13.33  ? 162 ASP B CA  1 
ATOM   3574 C  C   . ASP B  1 163 ? 61.909 12.632  -13.300 1.00 10.62  ? 162 ASP B C   1 
ATOM   3575 O  O   . ASP B  1 163 ? 62.426 12.945  -12.236 1.00 13.47  ? 162 ASP B O   1 
ATOM   3576 C  CB  . ASP B  1 163 ? 62.912 14.002  -15.141 1.00 13.74  ? 162 ASP B CB  1 
ATOM   3577 C  CG  . ASP B  1 163 ? 64.121 14.141  -16.046 1.00 15.54  ? 162 ASP B CG  1 
ATOM   3578 O  OD1 . ASP B  1 163 ? 64.927 13.189  -16.114 1.00 19.44  ? 162 ASP B OD1 1 
ATOM   3579 O  OD2 . ASP B  1 163 ? 64.264 15.202  -16.689 1.00 19.97  ? 162 ASP B OD2 1 
ATOM   3580 N  N   . ALA B  1 164 ? 60.622 12.286  -13.413 1.00 9.53   ? 163 ALA B N   1 
ATOM   3581 C  CA  . ALA B  1 164 ? 59.704 12.339  -12.279 1.00 9.24   ? 163 ALA B CA  1 
ATOM   3582 C  C   . ALA B  1 164 ? 59.837 11.115  -11.384 1.00 9.03   ? 163 ALA B C   1 
ATOM   3583 O  O   . ALA B  1 164 ? 59.367 11.142  -10.240 1.00 10.11  ? 163 ALA B O   1 
ATOM   3584 C  CB  . ALA B  1 164 ? 58.281 12.463  -12.808 1.00 10.26  ? 163 ALA B CB  1 
ATOM   3585 N  N   . LEU B  1 165 ? 60.388 10.012  -11.886 1.00 9.00   ? 164 LEU B N   1 
ATOM   3586 C  CA  . LEU B  1 165 ? 60.361 8.782   -11.147 1.00 9.46   ? 164 LEU B CA  1 
ATOM   3587 C  C   . LEU B  1 165 ? 61.101 8.847   -9.831  1.00 9.39   ? 164 LEU B C   1 
ATOM   3588 O  O   . LEU B  1 165 ? 60.753 8.167   -8.858  1.00 9.36   ? 164 LEU B O   1 
ATOM   3589 C  CB  . LEU B  1 165 ? 60.939 7.608   -12.000 1.00 10.40  ? 164 LEU B CB  1 
ATOM   3590 C  CG  . LEU B  1 165 ? 60.107 7.301   -13.257 1.00 11.13  ? 164 LEU B CG  1 
ATOM   3591 C  CD1 . LEU B  1 165 ? 60.792 6.115   -13.960 1.00 13.47  ? 164 LEU B CD1 1 
ATOM   3592 C  CD2 . LEU B  1 165 ? 58.656 7.052   -12.917 1.00 12.50  ? 164 LEU B CD2 1 
ATOM   3593 N  N   . GLN B  1 166 ? 62.157 9.705   -9.764  1.00 9.78   ? 165 GLN B N   1 
ATOM   3594 C  CA  . GLN B  1 166 ? 62.909 9.806   -8.508  1.00 10.01  ? 165 GLN B CA  1 
ATOM   3595 C  C   . GLN B  1 166 ? 62.035 10.320  -7.362  1.00 9.64   ? 165 GLN B C   1 
ATOM   3596 O  O   . GLN B  1 166 ? 62.416 10.086  -6.205  1.00 10.54  ? 165 GLN B O   1 
ATOM   3597 C  CB  . GLN B  1 166 ? 64.164 10.653  -8.675  1.00 13.04  ? 165 GLN B CB  1 
ATOM   3598 C  CG  . GLN B  1 166 ? 63.967 11.927  -9.371  1.00 14.59  ? 165 GLN B CG  1 
ATOM   3599 C  CD  . GLN B  1 166 ? 63.161 12.929  -8.718  1.00 12.24  ? 165 GLN B CD  1 
ATOM   3600 O  OE1 . GLN B  1 166 ? 63.299 13.129  -7.449  1.00 14.90  ? 165 GLN B OE1 1 
ATOM   3601 N  NE2 . GLN B  1 166 ? 62.233 13.628  -9.397  1.00 14.30  ? 165 GLN B NE2 1 
ATOM   3602 N  N   . ALA B  1 167 ? 60.894 10.940  -7.646  1.00 9.50   ? 166 ALA B N   1 
ATOM   3603 C  CA  . ALA B  1 167 ? 60.007 11.446  -6.607  1.00 10.26  ? 166 ALA B CA  1 
ATOM   3604 C  C   . ALA B  1 167 ? 58.995 10.403  -6.160  1.00 8.55   ? 166 ALA B C   1 
ATOM   3605 O  O   . ALA B  1 167 ? 58.289 10.640  -5.161  1.00 10.05  ? 166 ALA B O   1 
ATOM   3606 C  CB  . ALA B  1 167 ? 59.242 12.660  -7.119  1.00 13.93  ? 166 ALA B CB  1 
ATOM   3607 N  N   . ILE B  1 168 ? 58.911 9.260   -6.837  1.00 8.27   ? 167 ILE B N   1 
ATOM   3608 C  CA  . ILE B  1 168 ? 57.858 8.255   -6.546  1.00 8.04   ? 167 ILE B CA  1 
ATOM   3609 C  C   . ILE B  1 168 ? 58.487 6.885   -6.494  1.00 7.74   ? 167 ILE B C   1 
ATOM   3610 O  O   . ILE B  1 168 ? 57.957 5.905   -7.004  1.00 8.34   ? 167 ILE B O   1 
ATOM   3611 C  CB  . ILE B  1 168 ? 56.696 8.317   -7.511  1.00 8.78   ? 167 ILE B CB  1 
ATOM   3612 C  CG1 . ILE B  1 168 ? 57.120 8.075   -8.978  1.00 8.97   ? 167 ILE B CG1 1 
ATOM   3613 C  CG2 . ILE B  1 168 ? 55.910 9.640   -7.388  1.00 10.04  ? 167 ILE B CG2 1 
ATOM   3614 C  CD1 . ILE B  1 168 ? 56.064 7.303   -9.747  1.00 11.29  ? 167 ILE B CD1 1 
ATOM   3615 N  N   . LYS B  1 169 ? 59.679 6.815   -5.910  1.00 8.61   ? 168 LYS B N   1 
ATOM   3616 C  CA  . LYS B  1 169 ? 60.468 5.574   -5.855  1.00 7.97   ? 168 LYS B CA  1 
ATOM   3617 C  C   . LYS B  1 169 ? 59.865 4.315   -5.211  1.00 7.70   ? 168 LYS B C   1 
ATOM   3618 O  O   . LYS B  1 169 ? 60.214 3.197   -5.592  1.00 8.84   ? 168 LYS B O   1 
ATOM   3619 C  CB  . LYS B  1 169 ? 61.835 5.858   -5.220  1.00 11.93  ? 168 LYS B CB  1 
ATOM   3620 C  CG  . LYS B  1 169 ? 62.814 6.561   -6.147  1.00 17.16  ? 168 LYS B CG  1 
ATOM   3621 C  CD  . LYS B  1 169 ? 62.846 5.904   -7.517  1.00 20.13  ? 168 LYS B CD  1 
ATOM   3622 C  CE  . LYS B  1 169 ? 63.712 4.655   -7.510  1.00 19.07  ? 168 LYS B CE  1 
ATOM   3623 N  NZ  . LYS B  1 169 ? 64.384 4.438   -8.821  1.00 21.62  ? 168 LYS B NZ  1 
ATOM   3624 N  N   . THR B  1 170 ? 58.972 4.492   -4.247  1.00 8.05   ? 169 THR B N   1 
ATOM   3625 C  CA  . THR B  1 170 ? 58.371 3.369   -3.524  1.00 8.17   ? 169 THR B CA  1 
ATOM   3626 C  C   . THR B  1 170 ? 56.857 3.419   -3.573  1.00 7.89   ? 169 THR B C   1 
ATOM   3627 O  O   . THR B  1 170 ? 56.249 4.467   -3.826  1.00 8.55   ? 169 THR B O   1 
ATOM   3628 C  CB  . THR B  1 170 ? 58.883 3.352   -2.058  1.00 8.82   ? 169 THR B CB  1 
ATOM   3629 O  OG1 . THR B  1 170 ? 58.676 4.637   -1.519  1.00 9.19   ? 169 THR B OG1 1 
ATOM   3630 C  CG2 . THR B  1 170 ? 60.360 3.008   -2.011  1.00 9.69   ? 169 THR B CG2 1 
ATOM   3631 N  N   A LYS B  1 171 ? 56.246 2.278   -3.258  0.50 8.69   ? 170 LYS B N   1 
ATOM   3632 N  N   B LYS B  1 171 ? 56.269 2.267   -3.277  0.50 8.94   ? 170 LYS B N   1 
ATOM   3633 C  CA  A LYS B  1 171 ? 54.797 2.091   -3.408  0.50 9.04   ? 170 LYS B CA  1 
ATOM   3634 C  CA  B LYS B  1 171 ? 54.833 2.082   -3.428  0.50 8.90   ? 170 LYS B CA  1 
ATOM   3635 C  C   A LYS B  1 171 ? 54.023 3.120   -2.654  0.50 9.61   ? 170 LYS B C   1 
ATOM   3636 C  C   B LYS B  1 171 ? 54.044 3.109   -2.671  0.50 9.42   ? 170 LYS B C   1 
ATOM   3637 O  O   A LYS B  1 171 ? 54.219 3.351   -1.432  0.50 9.95   ? 170 LYS B O   1 
ATOM   3638 O  O   B LYS B  1 171 ? 54.283 3.341   -1.465  0.50 10.23  ? 170 LYS B O   1 
ATOM   3639 C  CB  A LYS B  1 171 ? 54.400 0.720   -2.879  0.50 10.18  ? 170 LYS B CB  1 
ATOM   3640 C  CB  B LYS B  1 171 ? 54.521 0.677   -2.962  0.50 11.24  ? 170 LYS B CB  1 
ATOM   3641 C  CG  A LYS B  1 171 ? 52.895 0.413   -3.014  0.50 12.82  ? 170 LYS B CG  1 
ATOM   3642 C  CG  B LYS B  1 171 ? 53.013 0.354   -3.044  0.50 11.99  ? 170 LYS B CG  1 
ATOM   3643 C  CD  A LYS B  1 171 ? 52.511 -1.023  -2.579  0.50 14.18  ? 170 LYS B CD  1 
ATOM   3644 C  CD  B LYS B  1 171 ? 52.885 -1.147  -2.848  0.50 14.18  ? 170 LYS B CD  1 
ATOM   3645 C  CE  A LYS B  1 171 ? 51.055 -1.294  -2.887  0.50 17.62  ? 170 LYS B CE  1 
ATOM   3646 C  CE  B LYS B  1 171 ? 52.941 -1.471  -1.372  0.50 20.31  ? 170 LYS B CE  1 
ATOM   3647 N  NZ  A LYS B  1 171 ? 50.848 -2.728  -2.519  0.50 29.01  ? 170 LYS B NZ  1 
ATOM   3648 N  NZ  B LYS B  1 171 ? 52.680 -2.996  -1.220  0.50 34.49  ? 170 LYS B NZ  1 
ATOM   3649 N  N   . GLY B  1 172 ? 53.052 3.704   -3.331  1.00 9.60   ? 171 GLY B N   1 
ATOM   3650 C  CA  . GLY B  1 172 ? 52.112 4.669   -2.741  1.00 11.19  ? 171 GLY B CA  1 
ATOM   3651 C  C   . GLY B  1 172 ? 52.593 6.083   -2.866  1.00 10.29  ? 171 GLY B C   1 
ATOM   3652 O  O   . GLY B  1 172 ? 51.779 7.008   -2.667  1.00 11.82  ? 171 GLY B O   1 
ATOM   3653 N  N   . LYS B  1 173 ? 53.892 6.342   -3.143  1.00 9.47   ? 172 LYS B N   1 
ATOM   3654 C  CA  . LYS B  1 173 ? 54.328 7.719   -3.329  1.00 9.41   ? 172 LYS B CA  1 
ATOM   3655 C  C   . LYS B  1 173 ? 53.642 8.305   -4.577  1.00 8.48   ? 172 LYS B C   1 
ATOM   3656 O  O   . LYS B  1 173 ? 53.424 7.604   -5.578  1.00 9.37   ? 172 LYS B O   1 
ATOM   3657 C  CB  . LYS B  1 173 ? 55.818 7.856   -3.451  1.00 9.63   ? 172 LYS B CB  1 
ATOM   3658 C  CG  . LYS B  1 173 ? 56.561 7.534   -2.115  1.00 10.01  ? 172 LYS B CG  1 
ATOM   3659 C  CD  . LYS B  1 173 ? 57.991 8.033   -2.130  1.00 10.60  ? 172 LYS B CD  1 
ATOM   3660 C  CE  . LYS B  1 173 ? 58.097 9.575   -2.042  1.00 11.26  ? 172 LYS B CE  1 
ATOM   3661 N  NZ  . LYS B  1 173 ? 59.522 10.036  -2.091  1.00 12.04  ? 172 LYS B NZ  1 
ATOM   3662 N  N   . ARG B  1 174 ? 53.383 9.581   -4.525  1.00 9.52   ? 173 ARG B N   1 
ATOM   3663 C  CA  . ARG B  1 174 ? 52.750 10.297  -5.626  1.00 9.41   ? 173 ARG B CA  1 
ATOM   3664 C  C   . ARG B  1 174 ? 53.237 11.722  -5.606  1.00 9.52   ? 173 ARG B C   1 
ATOM   3665 O  O   . ARG B  1 174 ? 53.580 12.264  -4.566  1.00 12.01  ? 173 ARG B O   1 
ATOM   3666 C  CB  . ARG B  1 174 ? 51.248 10.178  -5.531  1.00 11.33  ? 173 ARG B CB  1 
ATOM   3667 C  CG  . ARG B  1 174 ? 50.647 10.723  -4.267  1.00 13.78  ? 173 ARG B CG  1 
ATOM   3668 C  CD  . ARG B  1 174 ? 49.228 10.085  -3.991  1.00 15.47  ? 173 ARG B CD  1 
ATOM   3669 N  NE  . ARG B  1 174 ? 49.360 8.660   -3.698  1.00 14.60  ? 173 ARG B NE  1 
ATOM   3670 C  CZ  . ARG B  1 174 ? 48.615 7.656   -4.179  1.00 13.80  ? 173 ARG B CZ  1 
ATOM   3671 N  NH1 . ARG B  1 174 ? 47.562 7.909   -5.043  1.00 12.89  ? 173 ARG B NH1 1 
ATOM   3672 N  NH2 . ARG B  1 174 ? 48.903 6.398   -3.865  1.00 16.43  ? 173 ARG B NH2 1 
ATOM   3673 N  N   . ALA B  1 175 ? 53.230 12.358  -6.786  1.00 9.08   ? 174 ALA B N   1 
ATOM   3674 C  CA  . ALA B  1 175 ? 53.714 13.709  -6.909  1.00 10.68  ? 174 ALA B CA  1 
ATOM   3675 C  C   . ALA B  1 175 ? 52.962 14.436  -8.015  1.00 9.51   ? 174 ALA B C   1 
ATOM   3676 O  O   . ALA B  1 175 ? 52.537 13.806  -8.991  1.00 9.47   ? 174 ALA B O   1 
ATOM   3677 C  CB  . ALA B  1 175 ? 55.238 13.684  -7.236  1.00 13.09  ? 174 ALA B CB  1 
ATOM   3678 N  N   . PRO B  1 176 ? 52.885 15.759  -7.939  1.00 11.39  ? 175 PRO B N   1 
ATOM   3679 C  CA  . PRO B  1 176 ? 52.249 16.471  -9.016  1.00 11.62  ? 175 PRO B CA  1 
ATOM   3680 C  C   . PRO B  1 176 ? 53.015 16.286  -10.349 1.00 10.79  ? 175 PRO B C   1 
ATOM   3681 O  O   . PRO B  1 176 ? 54.238 16.195  -10.364 1.00 13.05  ? 175 PRO B O   1 
ATOM   3682 C  CB  . PRO B  1 176 ? 52.376 17.995  -8.584  1.00 15.05  ? 175 PRO B CB  1 
ATOM   3683 C  CG  . PRO B  1 176 ? 53.078 17.921  -7.343  1.00 24.88  ? 175 PRO B CG  1 
ATOM   3684 C  CD  . PRO B  1 176 ? 53.365 16.613  -6.835  1.00 14.14  ? 175 PRO B CD  1 
ATOM   3685 N  N   . PHE B  1 177 ? 52.277 16.210  -11.429 1.00 9.77   ? 176 PHE B N   1 
ATOM   3686 C  CA  . PHE B  1 177 ? 52.855 15.985  -12.748 1.00 9.93   ? 176 PHE B CA  1 
ATOM   3687 C  C   . PHE B  1 177 ? 51.939 16.744  -13.706 1.00 9.45   ? 176 PHE B C   1 
ATOM   3688 O  O   . PHE B  1 177 ? 50.813 16.333  -13.930 1.00 10.90  ? 176 PHE B O   1 
ATOM   3689 C  CB  . PHE B  1 177 ? 52.871 14.469  -13.082 1.00 10.07  ? 176 PHE B CB  1 
ATOM   3690 C  CG  . PHE B  1 177 ? 53.598 14.153  -14.379 1.00 9.67   ? 176 PHE B CG  1 
ATOM   3691 C  CD1 . PHE B  1 177 ? 52.944 14.209  -15.633 1.00 10.85  ? 176 PHE B CD1 1 
ATOM   3692 C  CD2 . PHE B  1 177 ? 54.945 13.748  -14.345 1.00 11.30  ? 176 PHE B CD2 1 
ATOM   3693 C  CE1 . PHE B  1 177 ? 53.668 13.899  -16.803 1.00 11.39  ? 176 PHE B CE1 1 
ATOM   3694 C  CE2 . PHE B  1 177 ? 55.635 13.453  -15.481 1.00 12.06  ? 176 PHE B CE2 1 
ATOM   3695 C  CZ  . PHE B  1 177 ? 54.987 13.517  -16.696 1.00 12.19  ? 176 PHE B CZ  1 
ATOM   3696 N  N   . THR B  1 178 ? 52.386 17.908  -14.183 1.00 9.36   ? 177 THR B N   1 
ATOM   3697 C  CA  . THR B  1 178 ? 51.528 18.842  -14.870 1.00 10.50  ? 177 THR B CA  1 
ATOM   3698 C  C   . THR B  1 178 ? 52.074 19.259  -16.220 1.00 9.90   ? 177 THR B C   1 
ATOM   3699 O  O   . THR B  1 178 ? 53.231 19.040  -16.534 1.00 11.42  ? 177 THR B O   1 
ATOM   3700 C  CB  . THR B  1 178 ? 51.301 20.119  -13.977 1.00 12.10  ? 177 THR B CB  1 
ATOM   3701 O  OG1 . THR B  1 178 ? 52.541 20.737  -13.765 1.00 14.24  ? 177 THR B OG1 1 
ATOM   3702 C  CG2 . THR B  1 178 ? 50.627 19.683  -12.667 1.00 13.86  ? 177 THR B CG2 1 
ATOM   3703 N  N   . ASN B  1 179 ? 51.174 19.886  -17.022 1.00 10.55  ? 178 ASN B N   1 
ATOM   3704 C  CA  . ASN B  1 179 ? 51.576 20.482  -18.275 1.00 10.58  ? 178 ASN B CA  1 
ATOM   3705 C  C   . ASN B  1 179 ? 52.233 19.429  -19.211 1.00 10.38  ? 178 ASN B C   1 
ATOM   3706 O  O   . ASN B  1 179 ? 53.370 19.638  -19.621 1.00 12.60  ? 178 ASN B O   1 
ATOM   3707 C  CB  . ASN B  1 179 ? 52.510 21.688  -18.046 1.00 11.75  ? 178 ASN B CB  1 
ATOM   3708 C  CG  . ASN B  1 179 ? 52.691 22.513  -19.281 1.00 14.80  ? 178 ASN B CG  1 
ATOM   3709 O  OD1 . ASN B  1 179 ? 51.809 22.596  -20.161 1.00 16.32  ? 178 ASN B OD1 1 
ATOM   3710 N  ND2 . ASN B  1 179 ? 53.848 23.201  -19.354 1.00 16.35  ? 178 ASN B ND2 1 
ATOM   3711 N  N   . PHE B  1 180 ? 51.491 18.411  -19.569 1.00 10.64  ? 179 PHE B N   1 
ATOM   3712 C  CA  . PHE B  1 180 ? 52.078 17.343  -20.383 1.00 10.59  ? 179 PHE B CA  1 
ATOM   3713 C  C   . PHE B  1 180 ? 50.976 16.780  -21.246 1.00 11.83  ? 179 PHE B C   1 
ATOM   3714 O  O   . PHE B  1 180 ? 49.911 16.404  -20.792 1.00 12.29  ? 179 PHE B O   1 
ATOM   3715 C  CB  . PHE B  1 180 ? 52.663 16.229  -19.514 1.00 11.24  ? 179 PHE B CB  1 
ATOM   3716 C  CG  . PHE B  1 180 ? 53.337 15.175  -20.346 1.00 10.84  ? 179 PHE B CG  1 
ATOM   3717 C  CD1 . PHE B  1 180 ? 54.586 15.415  -20.889 1.00 13.70  ? 179 PHE B CD1 1 
ATOM   3718 C  CD2 . PHE B  1 180 ? 52.762 13.962  -20.645 1.00 10.74  ? 179 PHE B CD2 1 
ATOM   3719 C  CE1 . PHE B  1 180 ? 55.236 14.519  -21.720 1.00 14.78  ? 179 PHE B CE1 1 
ATOM   3720 C  CE2 . PHE B  1 180 ? 53.399 13.007  -21.435 1.00 11.12  ? 179 PHE B CE2 1 
ATOM   3721 C  CZ  . PHE B  1 180 ? 54.640 13.272  -21.959 1.00 12.85  ? 179 PHE B CZ  1 
ATOM   3722 N  N   . ASP B  1 181 ? 51.248 16.708  -22.562 1.00 12.61  ? 180 ASP B N   1 
ATOM   3723 C  CA  . ASP B  1 181 ? 50.281 16.169  -23.558 1.00 12.63  ? 180 ASP B CA  1 
ATOM   3724 C  C   . ASP B  1 181 ? 50.844 14.820  -24.006 1.00 11.53  ? 180 ASP B C   1 
ATOM   3725 O  O   . ASP B  1 181 ? 51.838 14.790  -24.765 1.00 11.87  ? 180 ASP B O   1 
ATOM   3726 C  CB  . ASP B  1 181 ? 50.241 17.160  -24.757 1.00 13.83  ? 180 ASP B CB  1 
ATOM   3727 C  CG  . ASP B  1 181 ? 49.350 16.648  -25.891 1.00 13.40  ? 180 ASP B CG  1 
ATOM   3728 O  OD1 . ASP B  1 181 ? 48.904 15.478  -25.849 1.00 12.94  ? 180 ASP B OD1 1 
ATOM   3729 O  OD2 . ASP B  1 181 ? 49.136 17.385  -26.843 1.00 18.85  ? 180 ASP B OD2 1 
ATOM   3730 N  N   . PRO B  1 182 ? 50.215 13.707  -23.662 1.00 11.35  ? 181 PRO B N   1 
ATOM   3731 C  CA  . PRO B  1 182 ? 50.816 12.368  -23.994 1.00 10.67  ? 181 PRO B CA  1 
ATOM   3732 C  C   . PRO B  1 182 ? 50.651 12.016  -25.445 1.00 10.51  ? 181 PRO B C   1 
ATOM   3733 O  O   . PRO B  1 182 ? 51.197 11.023  -25.859 1.00 10.85  ? 181 PRO B O   1 
ATOM   3734 C  CB  . PRO B  1 182 ? 50.066 11.444  -23.084 1.00 12.81  ? 181 PRO B CB  1 
ATOM   3735 C  CG  . PRO B  1 182 ? 48.750 12.145  -22.803 1.00 12.92  ? 181 PRO B CG  1 
ATOM   3736 C  CD  . PRO B  1 182 ? 49.014 13.635  -22.826 1.00 12.71  ? 181 PRO B CD  1 
ATOM   3737 N  N   . SER B  1 183 ? 49.940 12.837  -26.235 1.00 11.70  ? 182 SER B N   1 
ATOM   3738 C  CA  . SER B  1 183 ? 49.935 12.549  -27.684 1.00 13.28  ? 182 SER B CA  1 
ATOM   3739 C  C   . SER B  1 183 ? 51.342 12.770  -28.208 1.00 11.85  ? 182 SER B C   1 
ATOM   3740 O  O   . SER B  1 183 ? 51.667 12.215  -29.307 1.00 13.30  ? 182 SER B O   1 
ATOM   3741 C  CB  . SER B  1 183 ? 48.955 13.402  -28.440 1.00 16.40  ? 182 SER B CB  1 
ATOM   3742 O  OG  . SER B  1 183 ? 49.281 14.734  -28.493 1.00 17.74  ? 182 SER B OG  1 
ATOM   3743 N  N   . THR B  1 184 ? 52.231 13.472  -27.500 1.00 11.59  ? 183 THR B N   1 
ATOM   3744 C  CA  . THR B  1 184 ? 53.611 13.623  -27.952 1.00 12.77  ? 183 THR B CA  1 
ATOM   3745 C  C   . THR B  1 184 ? 54.394 12.298  -27.882 1.00 12.05  ? 183 THR B C   1 
ATOM   3746 O  O   . THR B  1 184 ? 55.476 12.205  -28.440 1.00 14.80  ? 183 THR B O   1 
ATOM   3747 C  CB  . THR B  1 184 ? 54.362 14.681  -27.123 1.00 13.42  ? 183 THR B CB  1 
ATOM   3748 O  OG1 . THR B  1 184 ? 54.399 14.255  -25.751 1.00 13.18  ? 183 THR B OG1 1 
ATOM   3749 C  CG2 . THR B  1 184 ? 53.711 16.069  -27.257 1.00 16.79  ? 183 THR B CG2 1 
ATOM   3750 N  N   . LEU B  1 185 ? 53.860 11.303  -27.177 1.00 10.51  ? 184 LEU B N   1 
ATOM   3751 C  CA  . LEU B  1 185 ? 54.487 9.995   -27.086 1.00 10.67  ? 184 LEU B CA  1 
ATOM   3752 C  C   . LEU B  1 185 ? 54.088 9.064   -28.205 1.00 11.38  ? 184 LEU B C   1 
ATOM   3753 O  O   . LEU B  1 185 ? 54.711 8.018   -28.396 1.00 11.95  ? 184 LEU B O   1 
ATOM   3754 C  CB  . LEU B  1 185 ? 54.165 9.300   -25.755 1.00 11.01  ? 184 LEU B CB  1 
ATOM   3755 C  CG  . LEU B  1 185 ? 54.612 10.076  -24.508 1.00 12.56  ? 184 LEU B CG  1 
ATOM   3756 C  CD1 . LEU B  1 185 ? 54.057 9.433   -23.293 1.00 15.31  ? 184 LEU B CD1 1 
ATOM   3757 C  CD2 . LEU B  1 185 ? 56.135 10.224  -24.473 1.00 18.38  ? 184 LEU B CD2 1 
ATOM   3758 N  N   . LEU B  1 186 ? 53.013 9.401   -28.930 1.00 11.63  ? 185 LEU B N   1 
ATOM   3759 C  CA  . LEU B  1 186 ? 52.497 8.462   -29.950 1.00 11.66  ? 185 LEU B CA  1 
ATOM   3760 C  C   . LEU B  1 186 ? 53.398 8.519   -31.199 1.00 11.68  ? 185 LEU B C   1 
ATOM   3761 O  O   . LEU B  1 186 ? 54.102 9.523   -31.449 1.00 14.07  ? 185 LEU B O   1 
ATOM   3762 C  CB  . LEU B  1 186 ? 51.110 8.925   -30.350 1.00 12.34  ? 185 LEU B CB  1 
ATOM   3763 C  CG  . LEU B  1 186 ? 50.073 8.811   -29.158 1.00 12.23  ? 185 LEU B CG  1 
ATOM   3764 C  CD1 . LEU B  1 186 ? 48.729 9.317   -29.625 1.00 15.86  ? 185 LEU B CD1 1 
ATOM   3765 C  CD2 . LEU B  1 186 ? 50.000 7.455   -28.545 1.00 15.06  ? 185 LEU B CD2 1 
ATOM   3766 N  N   . PRO B  1 187 ? 53.366 7.469   -31.987 1.00 11.72  ? 186 PRO B N   1 
ATOM   3767 C  CA  . PRO B  1 187 ? 54.196 7.440   -33.245 1.00 13.66  ? 186 PRO B CA  1 
ATOM   3768 C  C   . PRO B  1 187 ? 53.606 8.416   -34.243 1.00 14.03  ? 186 PRO B C   1 
ATOM   3769 O  O   . PRO B  1 187 ? 52.487 8.920   -34.128 1.00 15.25  ? 186 PRO B O   1 
ATOM   3770 C  CB  . PRO B  1 187 ? 54.071 5.975   -33.730 1.00 13.01  ? 186 PRO B CB  1 
ATOM   3771 C  CG  . PRO B  1 187 ? 52.761 5.498   -33.111 1.00 14.21  ? 186 PRO B CG  1 
ATOM   3772 C  CD  . PRO B  1 187 ? 52.638 6.197   -31.770 1.00 11.65  ? 186 PRO B CD  1 
ATOM   3773 N  N   A SER B  1 188 ? 54.380 8.647   -35.306 0.50 17.43  ? 187 SER B N   1 
ATOM   3774 N  N   B SER B  1 188 ? 54.346 8.611   -35.303 0.50 17.43  ? 187 SER B N   1 
ATOM   3775 C  CA  A SER B  1 188 ? 54.012 9.628   -36.396 0.50 22.93  ? 187 SER B CA  1 
ATOM   3776 C  CA  B SER B  1 188 ? 53.981 9.618   -36.318 0.50 16.98  ? 187 SER B CA  1 
ATOM   3777 C  C   A SER B  1 188 ? 52.780 9.085   -37.139 0.50 17.33  ? 187 SER B C   1 
ATOM   3778 C  C   B SER B  1 188 ? 52.871 9.112   -37.269 0.50 17.30  ? 187 SER B C   1 
ATOM   3779 O  O   A SER B  1 188 ? 51.737 9.789   -37.352 0.50 19.94  ? 187 SER B O   1 
ATOM   3780 O  O   B SER B  1 188 ? 52.034 9.884   -37.815 0.50 27.12  ? 187 SER B O   1 
ATOM   3781 C  CB  A SER B  1 188 ? 55.176 9.889   -37.410 0.50 28.72  ? 187 SER B CB  1 
ATOM   3782 C  CB  B SER B  1 188 ? 55.189 9.835   -37.190 0.50 22.63  ? 187 SER B CB  1 
ATOM   3783 O  OG  A SER B  1 188 ? 55.832 8.689   -37.916 0.50 25.29  ? 187 SER B OG  1 
ATOM   3784 O  OG  B SER B  1 188 ? 56.048 10.715  -36.551 0.50 23.94  ? 187 SER B OG  1 
ATOM   3785 N  N   . SER B  1 189 ? 52.791 7.822   -37.505 1.00 15.42  ? 188 SER B N   1 
ATOM   3786 C  CA  . SER B  1 189 ? 51.613 7.201   -38.185 1.00 16.60  ? 188 SER B CA  1 
ATOM   3787 C  C   . SER B  1 189 ? 50.646 6.767   -37.014 1.00 16.00  ? 188 SER B C   1 
ATOM   3788 O  O   . SER B  1 189 ? 51.101 6.146   -36.048 1.00 17.67  ? 188 SER B O   1 
ATOM   3789 C  CB  . SER B  1 189 ? 52.051 5.941   -38.910 1.00 16.88  ? 188 SER B CB  1 
ATOM   3790 O  OG  . SER B  1 189 ? 50.890 5.206   -39.438 1.00 17.63  ? 188 SER B OG  1 
ATOM   3791 N  N   . LEU B  1 190 ? 49.434 7.014   -37.201 1.00 18.33  ? 189 LEU B N   1 
ATOM   3792 C  CA  . LEU B  1 190 ? 48.396 6.425   -36.285 1.00 17.21  ? 189 LEU B CA  1 
ATOM   3793 C  C   . LEU B  1 190 ? 47.592 5.319   -37.067 1.00 17.47  ? 189 LEU B C   1 
ATOM   3794 O  O   . LEU B  1 190 ? 46.490 5.045   -36.671 1.00 19.25  ? 189 LEU B O   1 
ATOM   3795 C  CB  . LEU B  1 190 ? 47.460 7.455   -35.630 1.00 18.89  ? 189 LEU B CB  1 
ATOM   3796 C  CG  . LEU B  1 190 ? 48.249 8.471   -34.795 1.00 19.37  ? 189 LEU B CG  1 
ATOM   3797 C  CD1 . LEU B  1 190 ? 47.226 9.489   -34.186 1.00 25.44  ? 189 LEU B CD1 1 
ATOM   3798 C  CD2 . LEU B  1 190 ? 49.193 7.735   -33.694 1.00 22.80  ? 189 LEU B CD2 1 
ATOM   3799 N  N   . ASP B  1 191 ? 48.228 4.638   -38.051 1.00 15.04  ? 190 ASP B N   1 
ATOM   3800 C  CA  . ASP B  1 191 ? 47.587 3.439   -38.586 1.00 14.03  ? 190 ASP B CA  1 
ATOM   3801 C  C   . ASP B  1 191 ? 47.454 2.522   -37.323 1.00 12.69  ? 190 ASP B C   1 
ATOM   3802 O  O   . ASP B  1 191 ? 48.263 2.612   -36.389 1.00 14.41  ? 190 ASP B O   1 
ATOM   3803 C  CB  . ASP B  1 191 ? 48.463 2.771   -39.645 1.00 15.01  ? 190 ASP B CB  1 
ATOM   3804 C  CG  . ASP B  1 191 ? 48.462 3.517   -40.970 1.00 16.89  ? 190 ASP B CG  1 
ATOM   3805 O  OD1 . ASP B  1 191 ? 47.572 4.387   -41.165 1.00 23.08  ? 190 ASP B OD1 1 
ATOM   3806 O  OD2 . ASP B  1 191 ? 49.355 3.223   -41.810 1.00 23.00  ? 190 ASP B OD2 1 
ATOM   3807 N  N   . PHE B  1 192 ? 46.480 1.614   -37.289 1.00 12.94  ? 191 PHE B N   1 
ATOM   3808 C  CA  . PHE B  1 192 ? 46.246 0.811   -36.103 1.00 12.48  ? 191 PHE B CA  1 
ATOM   3809 C  C   . PHE B  1 192 ? 45.558 -0.493  -36.425 1.00 12.33  ? 191 PHE B C   1 
ATOM   3810 O  O   . PHE B  1 192 ? 44.929 -0.644  -37.488 1.00 14.58  ? 191 PHE B O   1 
ATOM   3811 C  CB  . PHE B  1 192 ? 45.472 1.583   -35.042 1.00 12.83  ? 191 PHE B CB  1 
ATOM   3812 C  CG  . PHE B  1 192 ? 44.080 1.951   -35.499 1.00 13.39  ? 191 PHE B CG  1 
ATOM   3813 C  CD1 . PHE B  1 192 ? 43.828 3.122   -36.213 1.00 15.17  ? 191 PHE B CD1 1 
ATOM   3814 C  CD2 . PHE B  1 192 ? 43.004 1.117   -35.174 1.00 14.89  ? 191 PHE B CD2 1 
ATOM   3815 C  CE1 . PHE B  1 192 ? 42.504 3.415   -36.685 1.00 15.53  ? 191 PHE B CE1 1 
ATOM   3816 C  CE2 . PHE B  1 192 ? 41.709 1.375   -35.628 1.00 15.34  ? 191 PHE B CE2 1 
ATOM   3817 C  CZ  . PHE B  1 192 ? 41.469 2.530   -36.309 1.00 15.20  ? 191 PHE B CZ  1 
ATOM   3818 N  N   . TRP B  1 193 ? 45.677 -1.404  -35.483 1.00 12.21  ? 192 TRP B N   1 
ATOM   3819 C  CA  . TRP B  1 193 ? 44.817 -2.585  -35.369 1.00 12.35  ? 192 TRP B CA  1 
ATOM   3820 C  C   . TRP B  1 193 ? 43.827 -2.391  -34.233 1.00 11.89  ? 192 TRP B C   1 
ATOM   3821 O  O   . TRP B  1 193 ? 44.145 -1.665  -33.264 1.00 13.22  ? 192 TRP B O   1 
ATOM   3822 C  CB  . TRP B  1 193 ? 45.645 -3.819  -35.078 1.00 13.15  ? 192 TRP B CB  1 
ATOM   3823 C  CG  . TRP B  1 193 ? 46.602 -4.208  -36.145 1.00 12.49  ? 192 TRP B CG  1 
ATOM   3824 C  CD1 . TRP B  1 193 ? 46.305 -4.803  -37.371 1.00 13.59  ? 192 TRP B CD1 1 
ATOM   3825 C  CD2 . TRP B  1 193 ? 48.028 -4.085  -36.102 1.00 12.59  ? 192 TRP B CD2 1 
ATOM   3826 N  NE1 . TRP B  1 193 ? 47.445 -5.041  -38.066 1.00 13.54  ? 192 TRP B NE1 1 
ATOM   3827 C  CE2 . TRP B  1 193 ? 48.535 -4.629  -37.299 1.00 12.79  ? 192 TRP B CE2 1 
ATOM   3828 C  CE3 . TRP B  1 193 ? 48.953 -3.586  -35.160 1.00 13.13  ? 192 TRP B CE3 1 
ATOM   3829 C  CZ2 . TRP B  1 193 ? 49.876 -4.709  -37.556 1.00 12.82  ? 192 TRP B CZ2 1 
ATOM   3830 C  CZ3 . TRP B  1 193 ? 50.289 -3.661  -35.399 1.00 13.29  ? 192 TRP B CZ3 1 
ATOM   3831 C  CH2 . TRP B  1 193 ? 50.764 -4.183  -36.597 1.00 12.91  ? 192 TRP B CH2 1 
ATOM   3832 N  N   . THR B  1 194 ? 42.668 -3.002  -34.318 1.00 13.10  ? 193 THR B N   1 
ATOM   3833 C  CA  . THR B  1 194 ? 41.701 -2.910  -33.231 1.00 13.81  ? 193 THR B CA  1 
ATOM   3834 C  C   . THR B  1 194 ? 41.086 -4.241  -32.961 1.00 12.44  ? 193 THR B C   1 
ATOM   3835 O  O   . THR B  1 194 ? 40.762 -5.042  -33.910 1.00 14.42  ? 193 THR B O   1 
ATOM   3836 C  CB  . THR B  1 194 ? 40.705 -1.784  -33.426 1.00 14.01  ? 193 THR B CB  1 
ATOM   3837 O  OG1 . THR B  1 194 ? 39.834 -1.720  -32.295 1.00 14.13  ? 193 THR B OG1 1 
ATOM   3838 C  CG2 . THR B  1 194 ? 39.821 -1.977  -34.691 1.00 16.06  ? 193 THR B CG2 1 
ATOM   3839 N  N   . TYR B  1 195 ? 40.792 -4.573  -31.711 1.00 12.89  ? 194 TYR B N   1 
ATOM   3840 C  CA  . TYR B  1 195 ? 40.078 -5.797  -31.352 1.00 12.65  ? 194 TYR B CA  1 
ATOM   3841 C  C   . TYR B  1 195 ? 39.393 -5.569  -30.013 1.00 12.80  ? 194 TYR B C   1 
ATOM   3842 O  O   . TYR B  1 195 ? 39.842 -4.694  -29.242 1.00 13.20  ? 194 TYR B O   1 
ATOM   3843 C  CB  . TYR B  1 195 ? 40.982 -7.007  -31.388 1.00 13.48  ? 194 TYR B CB  1 
ATOM   3844 C  CG  . TYR B  1 195 ? 41.932 -7.059  -30.208 1.00 12.61  ? 194 TYR B CG  1 
ATOM   3845 C  CD1 . TYR B  1 195 ? 43.103 -6.336  -30.148 1.00 12.28  ? 194 TYR B CD1 1 
ATOM   3846 C  CD2 . TYR B  1 195 ? 41.581 -7.797  -29.121 1.00 13.19  ? 194 TYR B CD2 1 
ATOM   3847 C  CE1 . TYR B  1 195 ? 43.928 -6.303  -29.005 1.00 12.46  ? 194 TYR B CE1 1 
ATOM   3848 C  CE2 . TYR B  1 195 ? 42.377 -7.846  -27.953 1.00 12.19  ? 194 TYR B CE2 1 
ATOM   3849 C  CZ  . TYR B  1 195 ? 43.547 -7.120  -27.939 1.00 11.79  ? 194 TYR B CZ  1 
ATOM   3850 O  OH  . TYR B  1 195 ? 44.297 -7.152  -26.777 1.00 11.73  ? 194 TYR B OH  1 
ATOM   3851 N  N   . PRO B  1 196 ? 38.355 -6.359  -29.706 1.00 13.21  ? 195 PRO B N   1 
ATOM   3852 C  CA  . PRO B  1 196 ? 37.717 -6.289  -28.372 1.00 13.47  ? 195 PRO B CA  1 
ATOM   3853 C  C   . PRO B  1 196 ? 38.463 -7.116  -27.381 1.00 12.54  ? 195 PRO B C   1 
ATOM   3854 O  O   . PRO B  1 196 ? 38.664 -8.284  -27.606 1.00 14.68  ? 195 PRO B O   1 
ATOM   3855 C  CB  . PRO B  1 196 ? 36.274 -6.836  -28.684 1.00 15.39  ? 195 PRO B CB  1 
ATOM   3856 C  CG  . PRO B  1 196 ? 36.533 -7.854  -29.792 1.00 15.93  ? 195 PRO B CG  1 
ATOM   3857 C  CD  . PRO B  1 196 ? 37.603 -7.218  -30.666 1.00 15.40  ? 195 PRO B CD  1 
ATOM   3858 N  N   . GLY B  1 197 ? 38.814 -6.497  -26.234 1.00 11.61  ? 196 GLY B N   1 
ATOM   3859 C  CA  . GLY B  1 197 ? 39.575 -7.246  -25.214 1.00 11.85  ? 196 GLY B CA  1 
ATOM   3860 C  C   . GLY B  1 197 ? 39.296 -6.744  -23.864 1.00 11.26  ? 196 GLY B C   1 
ATOM   3861 O  O   . GLY B  1 197 ? 38.156 -6.384  -23.487 1.00 11.94  ? 196 GLY B O   1 
ATOM   3862 N  N   . SER B  1 198 ? 40.358 -6.774  -23.054 1.00 11.37  ? 197 SER B N   1 
ATOM   3863 C  CA  . SER B  1 198 ? 40.171 -6.650  -21.616 1.00 11.12  ? 197 SER B CA  1 
ATOM   3864 C  C   . SER B  1 198 ? 41.273 -5.759  -21.024 1.00 9.97   ? 197 SER B C   1 
ATOM   3865 O  O   . SER B  1 198 ? 42.288 -5.478  -21.671 1.00 10.73  ? 197 SER B O   1 
ATOM   3866 C  CB  . SER B  1 198 ? 40.251 -8.016  -20.949 1.00 12.11  ? 197 SER B CB  1 
ATOM   3867 O  OG  . SER B  1 198 ? 41.603 -8.555  -20.893 1.00 11.81  ? 197 SER B OG  1 
ATOM   3868 N  N   . LEU B  1 199 ? 41.084 -5.402  -19.742 1.00 10.66  ? 198 LEU B N   1 
ATOM   3869 C  CA  . LEU B  1 199 ? 42.196 -4.877  -18.966 1.00 10.51  ? 198 LEU B CA  1 
ATOM   3870 C  C   . LEU B  1 199 ? 43.231 -6.061  -18.905 1.00 10.75  ? 198 LEU B C   1 
ATOM   3871 O  O   . LEU B  1 199 ? 42.867 -7.272  -18.835 1.00 11.47  ? 198 LEU B O   1 
ATOM   3872 C  CB  . LEU B  1 199 ? 41.747 -4.549  -17.548 1.00 13.22  ? 198 LEU B CB  1 
ATOM   3873 C  CG  . LEU B  1 199 ? 40.555 -3.609  -17.426 1.00 17.90  ? 198 LEU B CG  1 
ATOM   3874 C  CD1 . LEU B  1 199 ? 40.165 -3.415  -15.978 1.00 22.25  ? 198 LEU B CD1 1 
ATOM   3875 C  CD2 . LEU B  1 199 ? 40.970 -2.281  -17.997 1.00 22.19  ? 198 LEU B CD2 1 
ATOM   3876 N  N   . THR B  1 200 ? 44.518 -5.721  -18.891 1.00 10.20  ? 199 THR B N   1 
ATOM   3877 C  CA  . THR B  1 200 ? 45.559 -6.700  -18.902 1.00 10.50  ? 199 THR B CA  1 
ATOM   3878 C  C   . THR B  1 200 ? 46.065 -7.176  -17.552 1.00 9.86   ? 199 THR B C   1 
ATOM   3879 O  O   . THR B  1 200 ? 46.991 -7.973  -17.457 1.00 10.91  ? 199 THR B O   1 
ATOM   3880 C  CB  . THR B  1 200 ? 46.755 -6.280  -19.778 1.00 9.52   ? 199 THR B CB  1 
ATOM   3881 O  OG1 . THR B  1 200 ? 47.358 -5.170  -19.114 1.00 9.95   ? 199 THR B OG1 1 
ATOM   3882 C  CG2 . THR B  1 200 ? 46.350 -5.948  -21.188 1.00 12.03  ? 199 THR B CG2 1 
ATOM   3883 N  N   . HIS B  1 201 ? 45.448 -6.673  -16.448 1.00 10.75  ? 200 HIS B N   1 
ATOM   3884 C  CA  . HIS B  1 201 ? 45.714 -7.227  -15.114 1.00 10.76  ? 200 HIS B CA  1 
ATOM   3885 C  C   . HIS B  1 201 ? 44.389 -7.146  -14.364 1.00 11.88  ? 200 HIS B C   1 
ATOM   3886 O  O   . HIS B  1 201 ? 43.414 -6.506  -14.840 1.00 11.68  ? 200 HIS B O   1 
ATOM   3887 C  CB  . HIS B  1 201 ? 46.878 -6.537  -14.439 1.00 12.20  ? 200 HIS B CB  1 
ATOM   3888 C  CG  . HIS B  1 201 ? 46.714 -5.073  -14.208 1.00 12.91  ? 200 HIS B CG  1 
ATOM   3889 N  ND1 . HIS B  1 201 ? 45.693 -4.516  -13.440 1.00 14.82  ? 200 HIS B ND1 1 
ATOM   3890 C  CD2 . HIS B  1 201 ? 47.522 -4.046  -14.574 1.00 15.18  ? 200 HIS B CD2 1 
ATOM   3891 C  CE1 . HIS B  1 201 ? 45.939 -3.188  -13.357 1.00 16.56  ? 200 HIS B CE1 1 
ATOM   3892 N  NE2 . HIS B  1 201 ? 47.015 -2.869  -14.055 1.00 19.02  ? 200 HIS B NE2 1 
ATOM   3893 N  N   . PRO B  1 202 ? 44.331 -7.753  -13.180 1.00 12.21  ? 201 PRO B N   1 
ATOM   3894 C  CA  . PRO B  1 202 ? 43.103 -7.771  -12.391 1.00 12.90  ? 201 PRO B CA  1 
ATOM   3895 C  C   . PRO B  1 202 ? 42.567 -6.329  -12.261 1.00 12.80  ? 201 PRO B C   1 
ATOM   3896 O  O   . PRO B  1 202 ? 43.353 -5.406  -12.042 1.00 13.68  ? 201 PRO B O   1 
ATOM   3897 C  CB  . PRO B  1 202 ? 43.506 -8.385  -11.068 1.00 14.61  ? 201 PRO B CB  1 
ATOM   3898 C  CG  . PRO B  1 202 ? 44.504 -9.412  -11.529 1.00 15.10  ? 201 PRO B CG  1 
ATOM   3899 C  CD  . PRO B  1 202 ? 45.340 -8.639  -12.563 1.00 14.12  ? 201 PRO B CD  1 
ATOM   3900 N  N   . PRO B  1 203 ? 41.266 -6.054  -12.455 1.00 13.46  ? 202 PRO B N   1 
ATOM   3901 C  CA  . PRO B  1 203 ? 40.197 -7.084  -12.477 1.00 14.75  ? 202 PRO B CA  1 
ATOM   3902 C  C   . PRO B  1 203 ? 39.948 -7.696  -13.800 1.00 12.84  ? 202 PRO B C   1 
ATOM   3903 O  O   . PRO B  1 203 ? 38.993 -8.533  -13.869 1.00 15.50  ? 202 PRO B O   1 
ATOM   3904 C  CB  . PRO B  1 203 ? 38.963 -6.393  -11.909 1.00 18.46  ? 202 PRO B CB  1 
ATOM   3905 C  CG  . PRO B  1 203 ? 39.232 -4.970  -12.392 1.00 17.30  ? 202 PRO B CG  1 
ATOM   3906 C  CD  . PRO B  1 203 ? 40.730 -4.685  -12.259 1.00 15.28  ? 202 PRO B CD  1 
ATOM   3907 N  N   . LEU B  1 204 ? 40.714 -7.378  -14.887 1.00 12.56  ? 203 LEU B N   1 
ATOM   3908 C  CA  . LEU B  1 204 ? 40.621 -8.212  -16.094 1.00 11.73  ? 203 LEU B CA  1 
ATOM   3909 C  C   . LEU B  1 204 ? 39.278 -8.022  -16.786 1.00 12.59  ? 203 LEU B C   1 
ATOM   3910 O  O   . LEU B  1 204 ? 38.938 -8.814  -17.712 1.00 14.31  ? 203 LEU B O   1 
ATOM   3911 C  CB  . LEU B  1 204 ? 41.001 -9.683  -15.889 1.00 12.32  ? 203 LEU B CB  1 
ATOM   3912 C  CG  . LEU B  1 204 ? 42.406 -9.947  -15.408 1.00 11.96  ? 203 LEU B CG  1 
ATOM   3913 C  CD1 . LEU B  1 204 ? 42.507 -11.399 -14.965 1.00 15.95  ? 203 LEU B CD1 1 
ATOM   3914 C  CD2 . LEU B  1 204 ? 43.440 -9.683  -16.477 1.00 12.54  ? 203 LEU B CD2 1 
ATOM   3915 N  N   . TYR B  1 205 ? 38.513 -6.941  -16.541 1.00 12.86  ? 204 TYR B N   1 
ATOM   3916 C  CA  . TYR B  1 205 ? 37.207 -6.782  -17.143 1.00 13.05  ? 204 TYR B CA  1 
ATOM   3917 C  C   . TYR B  1 205 ? 37.383 -6.744  -18.657 1.00 12.17  ? 204 TYR B C   1 
ATOM   3918 O  O   . TYR B  1 205 ? 38.274 -6.127  -19.234 1.00 11.93  ? 204 TYR B O   1 
ATOM   3919 C  CB  . TYR B  1 205 ? 36.580 -5.422  -16.749 1.00 12.98  ? 204 TYR B CB  1 
ATOM   3920 C  CG  . TYR B  1 205 ? 36.236 -5.303  -15.270 1.00 14.54  ? 204 TYR B CG  1 
ATOM   3921 C  CD1 . TYR B  1 205 ? 35.762 -6.351  -14.534 1.00 18.42  ? 204 TYR B CD1 1 
ATOM   3922 C  CD2 . TYR B  1 205 ? 36.418 -4.070  -14.648 1.00 14.25  ? 204 TYR B CD2 1 
ATOM   3923 C  CE1 . TYR B  1 205 ? 35.343 -6.191  -13.222 1.00 17.04  ? 204 TYR B CE1 1 
ATOM   3924 C  CE2 . TYR B  1 205 ? 36.008 -3.914  -13.309 1.00 15.46  ? 204 TYR B CE2 1 
ATOM   3925 C  CZ  . TYR B  1 205 ? 35.499 -4.989  -12.622 1.00 16.77  ? 204 TYR B CZ  1 
ATOM   3926 O  OH  . TYR B  1 205 ? 35.107 -4.810  -11.298 1.00 19.93  ? 204 TYR B OH  1 
ATOM   3927 N  N   . GLU B  1 206 ? 36.383 -7.344  -19.361 1.00 12.72  ? 205 GLU B N   1 
ATOM   3928 C  CA  . GLU B  1 206 ? 36.361 -7.417  -20.795 1.00 13.14  ? 205 GLU B CA  1 
ATOM   3929 C  C   . GLU B  1 206 ? 35.665 -6.209  -21.323 1.00 12.60  ? 205 GLU B C   1 
ATOM   3930 O  O   . GLU B  1 206 ? 34.566 -6.260  -21.978 1.00 15.73  ? 205 GLU B O   1 
ATOM   3931 C  CB  . GLU B  1 206 ? 35.759 -8.755  -21.267 1.00 14.07  ? 205 GLU B CB  1 
ATOM   3932 C  CG  . GLU B  1 206 ? 36.644 -9.876  -20.839 1.00 14.41  ? 205 GLU B CG  1 
ATOM   3933 C  CD  . GLU B  1 206 ? 36.249 -11.247 -21.369 1.00 14.49  ? 205 GLU B CD  1 
ATOM   3934 O  OE1 . GLU B  1 206 ? 37.159 -12.115 -21.373 1.00 14.09  ? 205 GLU B OE1 1 
ATOM   3935 O  OE2 . GLU B  1 206 ? 35.061 -11.492 -21.624 1.00 18.61  ? 205 GLU B OE2 1 
ATOM   3936 N  N   . SER B  1 207 ? 36.246 -5.023  -21.090 1.00 12.38  ? 206 SER B N   1 
ATOM   3937 C  CA  . SER B  1 207 ? 35.624 -3.755  -21.284 1.00 12.71  ? 206 SER B CA  1 
ATOM   3938 C  C   . SER B  1 207 ? 36.372 -2.825  -22.274 1.00 12.93  ? 206 SER B C   1 
ATOM   3939 O  O   . SER B  1 207 ? 36.089 -1.627  -22.389 1.00 13.24  ? 206 SER B O   1 
ATOM   3940 C  CB  . SER B  1 207 ? 35.437 -3.011  -19.934 1.00 13.59  ? 206 SER B CB  1 
ATOM   3941 O  OG  . SER B  1 207 ? 36.758 -2.967  -19.401 1.00 14.08  ? 206 SER B OG  1 
ATOM   3942 N  N   . VAL B  1 208 ? 37.477 -3.373  -22.873 1.00 11.99  ? 207 VAL B N   1 
ATOM   3943 C  CA  . VAL B  1 208 ? 38.422 -2.514  -23.568 1.00 11.27  ? 207 VAL B CA  1 
ATOM   3944 C  C   . VAL B  1 208 ? 38.335 -2.700  -25.056 1.00 11.49  ? 207 VAL B C   1 
ATOM   3945 O  O   . VAL B  1 208 ? 38.524 -3.818  -25.576 1.00 13.49  ? 207 VAL B O   1 
ATOM   3946 C  CB  . VAL B  1 208 ? 39.872 -2.784  -23.099 1.00 11.43  ? 207 VAL B CB  1 
ATOM   3947 C  CG1 . VAL B  1 208 ? 40.813 -1.861  -23.857 1.00 12.46  ? 207 VAL B CG1 1 
ATOM   3948 C  CG2 . VAL B  1 208 ? 39.996 -2.549  -21.622 1.00 11.77  ? 207 VAL B CG2 1 
ATOM   3949 N  N   . THR B  1 209 ? 38.161 -1.592  -25.815 1.00 11.31  ? 208 THR B N   1 
ATOM   3950 C  CA  . THR B  1 209 ? 38.447 -1.615  -27.245 1.00 11.86  ? 208 THR B CA  1 
ATOM   3951 C  C   . THR B  1 209 ? 39.892 -1.176  -27.383 1.00 12.05  ? 208 THR B C   1 
ATOM   3952 O  O   . THR B  1 209 ? 40.266 -0.050  -27.044 1.00 12.43  ? 208 THR B O   1 
ATOM   3953 C  CB  . THR B  1 209 ? 37.537 -0.645  -27.942 1.00 12.97  ? 208 THR B CB  1 
ATOM   3954 O  OG1 . THR B  1 209 ? 36.150 -0.961  -27.728 1.00 14.07  ? 208 THR B OG1 1 
ATOM   3955 C  CG2 . THR B  1 209 ? 37.807 -0.707  -29.481 1.00 16.16  ? 208 THR B CG2 1 
ATOM   3956 N  N   . TRP B  1 210 ? 40.722 -2.115  -27.874 1.00 12.16  ? 209 TRP B N   1 
ATOM   3957 C  CA  . TRP B  1 210 ? 42.142 -1.889  -28.009 1.00 10.92  ? 209 TRP B CA  1 
ATOM   3958 C  C   . TRP B  1 210 ? 42.401 -1.258  -29.372 1.00 10.65  ? 209 TRP B C   1 
ATOM   3959 O  O   . TRP B  1 210 ? 41.843 -1.629  -30.405 1.00 12.30  ? 209 TRP B O   1 
ATOM   3960 C  CB  . TRP B  1 210 ? 42.912 -3.216  -27.905 1.00 10.63  ? 209 TRP B CB  1 
ATOM   3961 C  CG  . TRP B  1 210 ? 43.116 -3.557  -26.502 1.00 10.34  ? 209 TRP B CG  1 
ATOM   3962 C  CD1 . TRP B  1 210 ? 42.357 -4.395  -25.702 1.00 11.68  ? 209 TRP B CD1 1 
ATOM   3963 C  CD2 . TRP B  1 210 ? 44.109 -2.988  -25.609 1.00 10.75  ? 209 TRP B CD2 1 
ATOM   3964 N  NE1 . TRP B  1 210 ? 42.794 -4.404  -24.409 1.00 11.42  ? 209 TRP B NE1 1 
ATOM   3965 C  CE2 . TRP B  1 210 ? 43.893 -3.565  -24.311 1.00 10.91  ? 209 TRP B CE2 1 
ATOM   3966 C  CE3 . TRP B  1 210 ? 45.145 -2.088  -25.778 1.00 10.69  ? 209 TRP B CE3 1 
ATOM   3967 C  CZ2 . TRP B  1 210 ? 44.660 -3.208  -23.181 1.00 11.24  ? 209 TRP B CZ2 1 
ATOM   3968 C  CZ3 . TRP B  1 210 ? 45.971 -1.770  -24.699 1.00 11.24  ? 209 TRP B CZ3 1 
ATOM   3969 C  CH2 . TRP B  1 210 ? 45.691 -2.308  -23.470 1.00 11.19  ? 209 TRP B CH2 1 
ATOM   3970 N  N   . ILE B  1 211 ? 43.307 -0.255  -29.376 1.00 11.23  ? 210 ILE B N   1 
ATOM   3971 C  CA  . ILE B  1 211 ? 43.854 0.477   -30.550 1.00 11.59  ? 210 ILE B CA  1 
ATOM   3972 C  C   . ILE B  1 211 ? 45.326 0.246   -30.482 1.00 10.81  ? 210 ILE B C   1 
ATOM   3973 O  O   . ILE B  1 211 ? 46.005 0.856   -29.659 1.00 11.61  ? 210 ILE B O   1 
ATOM   3974 C  CB  . ILE B  1 211 ? 43.490 1.940   -30.540 1.00 11.84  ? 210 ILE B CB  1 
ATOM   3975 C  CG1 . ILE B  1 211 ? 41.964 2.181   -30.414 1.00 13.84  ? 210 ILE B CG1 1 
ATOM   3976 C  CG2 . ILE B  1 211 ? 44.136 2.656   -31.742 1.00 13.17  ? 210 ILE B CG2 1 
ATOM   3977 C  CD1 . ILE B  1 211 ? 41.153 1.742   -31.568 1.00 15.76  ? 210 ILE B CD1 1 
ATOM   3978 N  N   . ILE B  1 212 ? 45.892 -0.683  -31.305 1.00 10.89  ? 211 ILE B N   1 
ATOM   3979 C  CA  . ILE B  1 212 ? 47.317 -0.985  -31.273 1.00 10.52  ? 211 ILE B CA  1 
ATOM   3980 C  C   . ILE B  1 212 ? 47.981 -0.296  -32.420 1.00 10.69  ? 211 ILE B C   1 
ATOM   3981 O  O   . ILE B  1 212 ? 47.643 -0.574  -33.604 1.00 12.24  ? 211 ILE B O   1 
ATOM   3982 C  CB  . ILE B  1 212 ? 47.582 -2.526  -31.275 1.00 11.47  ? 211 ILE B CB  1 
ATOM   3983 C  CG1 . ILE B  1 212 ? 46.823 -3.244  -30.184 1.00 12.19  ? 211 ILE B CG1 1 
ATOM   3984 C  CG2 . ILE B  1 212 ? 49.113 -2.812  -31.232 1.00 12.24  ? 211 ILE B CG2 1 
ATOM   3985 C  CD1 . ILE B  1 212 ? 47.104 -2.748  -28.776 1.00 12.62  ? 211 ILE B CD1 1 
ATOM   3986 N  N   . CYS B  1 213 ? 48.898 0.612   -32.191 1.00 10.80  ? 212 CYS B N   1 
ATOM   3987 C  CA  . CYS B  1 213 ? 49.538 1.321   -33.317 1.00 10.89  ? 212 CYS B CA  1 
ATOM   3988 C  C   . CYS B  1 213 ? 50.450 0.372   -34.085 1.00 11.33  ? 212 CYS B C   1 
ATOM   3989 O  O   . CYS B  1 213 ? 51.165 -0.480  -33.525 1.00 11.21  ? 212 CYS B O   1 
ATOM   3990 C  CB  . CYS B  1 213 ? 50.413 2.496   -32.772 1.00 11.77  ? 212 CYS B CB  1 
ATOM   3991 S  SG  . CYS B  1 213 ? 49.357 3.816   -32.098 1.00 13.41  ? 212 CYS B SG  1 
ATOM   3992 N  N   . LYS B  1 214 ? 50.436 0.542   -35.417 1.00 12.92  ? 213 LYS B N   1 
ATOM   3993 C  CA  . LYS B  1 214 ? 51.315 -0.256  -36.255 1.00 14.57  ? 213 LYS B CA  1 
ATOM   3994 C  C   . LYS B  1 214 ? 52.790 0.149   -36.087 1.00 12.73  ? 213 LYS B C   1 
ATOM   3995 O  O   . LYS B  1 214 ? 53.673 -0.709  -36.129 1.00 12.63  ? 213 LYS B O   1 
ATOM   3996 C  CB  . LYS B  1 214 ? 50.865 0.130   -37.739 1.00 20.39  ? 213 LYS B CB  1 
ATOM   3997 C  CG  . LYS B  1 214 ? 51.669 -0.419  -38.774 1.00 20.07  ? 213 LYS B CG  1 
ATOM   3998 C  CD  . LYS B  1 214 ? 51.336 0.198   -40.127 1.00 17.62  ? 213 LYS B CD  1 
ATOM   3999 C  CE  . LYS B  1 214 ? 52.051 1.483   -40.408 1.00 20.63  ? 213 LYS B CE  1 
ATOM   4000 N  NZ  . LYS B  1 214 ? 51.917 2.180   -41.664 1.00 27.00  ? 213 LYS B NZ  1 
ATOM   4001 N  N   A GLU B  1 215 ? 53.027 1.430   -35.860 0.50 12.55  ? 214 GLU B N   1 
ATOM   4002 N  N   B GLU B  1 215 ? 53.084 1.461   -36.010 0.50 11.58  ? 214 GLU B N   1 
ATOM   4003 C  CA  A GLU B  1 215 ? 54.383 1.906   -35.737 0.50 10.29  ? 214 GLU B CA  1 
ATOM   4004 C  CA  B GLU B  1 215 ? 54.442 1.995   -35.832 0.50 12.29  ? 214 GLU B CA  1 
ATOM   4005 C  C   A GLU B  1 215 ? 54.861 1.966   -34.297 0.50 9.27   ? 214 GLU B C   1 
ATOM   4006 C  C   B GLU B  1 215 ? 54.899 2.029   -34.361 0.50 9.73   ? 214 GLU B C   1 
ATOM   4007 O  O   A GLU B  1 215 ? 54.160 2.480   -33.425 0.50 8.99   ? 214 GLU B O   1 
ATOM   4008 O  O   B GLU B  1 215 ? 54.211 2.610   -33.522 0.50 9.99   ? 214 GLU B O   1 
ATOM   4009 C  CB  A GLU B  1 215 ? 54.454 3.278   -36.363 0.50 12.80  ? 214 GLU B CB  1 
ATOM   4010 C  CB  B GLU B  1 215 ? 54.510 3.431   -36.396 0.50 11.22  ? 214 GLU B CB  1 
ATOM   4011 C  CG  A GLU B  1 215 ? 55.839 3.903   -36.335 0.50 11.18  ? 214 GLU B CG  1 
ATOM   4012 C  CG  B GLU B  1 215 ? 55.202 3.536   -37.745 0.50 12.84  ? 214 GLU B CG  1 
ATOM   4013 C  CD  A GLU B  1 215 ? 55.860 5.299   -36.924 0.50 11.69  ? 214 GLU B CD  1 
ATOM   4014 C  CD  B GLU B  1 215 ? 55.261 4.961   -38.260 0.50 12.39  ? 214 GLU B CD  1 
ATOM   4015 O  OE1 A GLU B  1 215 ? 56.519 6.184   -36.338 0.50 15.84  ? 214 GLU B OE1 1 
ATOM   4016 O  OE1 B GLU B  1 215 ? 55.103 5.895   -37.447 0.50 14.01  ? 214 GLU B OE1 1 
ATOM   4017 O  OE2 A GLU B  1 215 ? 55.219 5.512   -37.975 0.50 21.97  ? 214 GLU B OE2 1 
ATOM   4018 O  OE2 B GLU B  1 215 ? 55.464 5.146   -39.479 0.50 14.74  ? 214 GLU B OE2 1 
ATOM   4019 N  N   . SER B  1 216 ? 56.046 1.419   -34.040 1.00 10.50  ? 215 SER B N   1 
ATOM   4020 C  CA  . SER B  1 216 ? 56.575 1.452   -32.686 1.00 10.18  ? 215 SER B CA  1 
ATOM   4021 C  C   . SER B  1 216 ? 57.109 2.841   -32.392 1.00 9.72   ? 215 SER B C   1 
ATOM   4022 O  O   . SER B  1 216 ? 57.266 3.699   -33.268 1.00 11.44  ? 215 SER B O   1 
ATOM   4023 C  CB  . SER B  1 216 ? 57.623 0.369   -32.507 1.00 11.20  ? 215 SER B CB  1 
ATOM   4024 O  OG  . SER B  1 216 ? 58.676 0.517   -33.424 1.00 11.29  ? 215 SER B OG  1 
ATOM   4025 N  N   . ILE B  1 217 ? 57.478 3.037   -31.111 1.00 9.05   ? 216 ILE B N   1 
ATOM   4026 C  CA  . ILE B  1 217 ? 58.341 4.173   -30.691 1.00 9.75   ? 216 ILE B CA  1 
ATOM   4027 C  C   . ILE B  1 217 ? 59.566 3.605   -30.072 1.00 8.83   ? 216 ILE B C   1 
ATOM   4028 O  O   . ILE B  1 217 ? 59.614 2.422   -29.665 1.00 9.86   ? 216 ILE B O   1 
ATOM   4029 C  CB  . ILE B  1 217 ? 57.611 5.140   -29.721 1.00 9.01   ? 216 ILE B CB  1 
ATOM   4030 C  CG1 . ILE B  1 217 ? 57.207 4.413   -28.419 1.00 10.01  ? 216 ILE B CG1 1 
ATOM   4031 C  CG2 . ILE B  1 217 ? 56.390 5.749   -30.478 1.00 10.16  ? 216 ILE B CG2 1 
ATOM   4032 C  CD1 . ILE B  1 217 ? 56.569 5.309   -27.345 1.00 11.35  ? 216 ILE B CD1 1 
ATOM   4033 N  N   A SER B  1 218 ? 60.626 4.404   -29.971 0.50 9.93   ? 217 SER B N   1 
ATOM   4034 N  N   B SER B  1 218 ? 60.597 4.448   -29.951 0.50 9.24   ? 217 SER B N   1 
ATOM   4035 C  CA  A SER B  1 218 ? 61.852 3.875   -29.389 0.50 10.35  ? 217 SER B CA  1 
ATOM   4036 C  CA  B SER B  1 218 ? 61.893 4.000   -29.460 0.50 8.62   ? 217 SER B CA  1 
ATOM   4037 C  C   A SER B  1 218 ? 61.866 4.002   -27.882 0.50 8.89   ? 217 SER B C   1 
ATOM   4038 C  C   B SER B  1 218 ? 61.998 4.177   -27.947 0.50 9.35   ? 217 SER B C   1 
ATOM   4039 O  O   A SER B  1 218 ? 61.090 4.738   -27.235 0.50 9.28   ? 217 SER B O   1 
ATOM   4040 O  O   B SER B  1 218 ? 61.308 5.059   -27.350 0.50 9.37   ? 217 SER B O   1 
ATOM   4041 C  CB  A SER B  1 218 ? 63.093 4.638   -29.977 0.50 11.58  ? 217 SER B CB  1 
ATOM   4042 C  CB  B SER B  1 218 ? 63.008 4.729   -30.238 0.50 9.62   ? 217 SER B CB  1 
ATOM   4043 O  OG  A SER B  1 218 ? 63.222 5.909   -29.414 0.50 18.69  ? 217 SER B OG  1 
ATOM   4044 O  OG  B SER B  1 218 ? 64.248 4.036   -29.908 0.50 8.10   ? 217 SER B OG  1 
ATOM   4045 N  N   . VAL B  1 219 ? 62.861 3.370   -27.315 1.00 9.06   ? 218 VAL B N   1 
ATOM   4046 C  CA  . VAL B  1 219 ? 63.218 3.506   -25.907 1.00 8.84   ? 218 VAL B CA  1 
ATOM   4047 C  C   . VAL B  1 219 ? 64.660 2.971   -25.806 1.00 8.45   ? 218 VAL B C   1 
ATOM   4048 O  O   . VAL B  1 219 ? 64.959 1.996   -26.475 1.00 10.07  ? 218 VAL B O   1 
ATOM   4049 C  CB  . VAL B  1 219 ? 62.237 2.752   -25.010 1.00 9.20   ? 218 VAL B CB  1 
ATOM   4050 C  CG1 . VAL B  1 219 ? 62.188 1.250   -25.275 1.00 10.62  ? 218 VAL B CG1 1 
ATOM   4051 C  CG2 . VAL B  1 219 ? 62.543 3.054   -23.531 1.00 10.05  ? 218 VAL B CG2 1 
ATOM   4052 N  N   . SER B  1 220 ? 65.503 3.561   -24.983 1.00 8.81   ? 219 SER B N   1 
ATOM   4053 C  CA  . SER B  1 220 ? 66.858 2.999   -24.839 1.00 9.18   ? 219 SER B CA  1 
ATOM   4054 C  C   . SER B  1 220 ? 66.884 1.956   -23.759 1.00 9.25   ? 219 SER B C   1 
ATOM   4055 O  O   . SER B  1 220 ? 66.036 1.880   -22.852 1.00 9.26   ? 219 SER B O   1 
ATOM   4056 C  CB  . SER B  1 220 ? 67.909 4.013   -24.592 1.00 9.90   ? 219 SER B CB  1 
ATOM   4057 O  OG  . SER B  1 220 ? 67.725 4.529   -23.253 1.00 10.52  ? 219 SER B OG  1 
ATOM   4058 N  N   A SER B  1 221 ? 67.960 1.120   -23.777 0.50 10.06  ? 220 SER B N   1 
ATOM   4059 N  N   B SER B  1 221 ? 67.990 1.149   -23.768 0.50 10.22  ? 220 SER B N   1 
ATOM   4060 C  CA  A SER B  1 221 ? 68.110 0.130   -22.745 0.50 10.50  ? 220 SER B CA  1 
ATOM   4061 C  CA  B SER B  1 221 ? 68.250 0.188   -22.722 0.50 9.97   ? 220 SER B CA  1 
ATOM   4062 C  C   A SER B  1 221 ? 68.216 0.833   -21.358 0.50 9.59   ? 220 SER B C   1 
ATOM   4063 C  C   B SER B  1 221 ? 68.285 0.822   -21.346 0.50 8.86   ? 220 SER B C   1 
ATOM   4064 O  O   A SER B  1 221 ? 67.709 0.283   -20.387 0.50 10.64  ? 220 SER B O   1 
ATOM   4065 O  O   B SER B  1 221 ? 67.845 0.236   -20.371 0.50 9.84   ? 220 SER B O   1 
ATOM   4066 C  CB  A SER B  1 221 ? 69.402 -0.695  -23.072 0.50 11.39  ? 220 SER B CB  1 
ATOM   4067 C  CB  B SER B  1 221 ? 69.617 -0.461  -22.993 0.50 10.07  ? 220 SER B CB  1 
ATOM   4068 O  OG  A SER B  1 221 ? 69.475 -1.784  -22.168 0.50 13.45  ? 220 SER B OG  1 
ATOM   4069 O  OG  B SER B  1 221 ? 69.500 -1.278  -24.096 0.50 11.23  ? 220 SER B OG  1 
ATOM   4070 N  N   . GLU B  1 222 ? 68.848 2.018   -21.301 1.00 9.32   ? 221 GLU B N   1 
ATOM   4071 C  CA  . GLU B  1 222 ? 68.985 2.735   -19.998 1.00 9.66   ? 221 GLU B CA  1 
ATOM   4072 C  C   . GLU B  1 222 ? 67.636 3.299   -19.534 1.00 9.52   ? 221 GLU B C   1 
ATOM   4073 O  O   . GLU B  1 222 ? 67.382 3.346   -18.340 1.00 9.95   ? 221 GLU B O   1 
ATOM   4074 C  CB  . GLU B  1 222 ? 70.047 3.785   -20.106 1.00 10.18  ? 221 GLU B CB  1 
ATOM   4075 C  CG  . GLU B  1 222 ? 71.452 3.222   -20.336 1.00 11.78  ? 221 GLU B CG  1 
ATOM   4076 C  CD  . GLU B  1 222 ? 71.657 2.694   -21.768 1.00 11.53  ? 221 GLU B CD  1 
ATOM   4077 O  OE1 . GLU B  1 222 ? 71.143 3.316   -22.729 1.00 12.99  ? 221 GLU B OE1 1 
ATOM   4078 O  OE2 . GLU B  1 222 ? 72.358 1.704   -21.953 1.00 13.00  ? 221 GLU B OE2 1 
ATOM   4079 N  N   . GLN B  1 223 ? 66.790 3.760   -20.471 1.00 9.12   ? 222 GLN B N   1 
ATOM   4080 C  CA  . GLN B  1 223 ? 65.463 4.246   -20.094 1.00 8.76   ? 222 GLN B CA  1 
ATOM   4081 C  C   . GLN B  1 223 ? 64.655 3.078   -19.519 1.00 8.65   ? 222 GLN B C   1 
ATOM   4082 O  O   . GLN B  1 223 ? 63.981 3.250   -18.494 1.00 9.38   ? 222 GLN B O   1 
ATOM   4083 C  CB  . GLN B  1 223 ? 64.788 4.895   -21.275 1.00 9.16   ? 222 GLN B CB  1 
ATOM   4084 C  CG  . GLN B  1 223 ? 65.459 6.195   -21.666 1.00 9.67   ? 222 GLN B CG  1 
ATOM   4085 C  CD  . GLN B  1 223 ? 64.794 6.862   -22.861 1.00 9.79   ? 222 GLN B CD  1 
ATOM   4086 O  OE1 . GLN B  1 223 ? 64.501 6.166   -23.863 1.00 9.54   ? 222 GLN B OE1 1 
ATOM   4087 N  NE2 . GLN B  1 223 ? 64.564 8.153   -22.824 1.00 11.26  ? 222 GLN B NE2 1 
ATOM   4088 N  N   . LEU B  1 224 ? 64.727 1.903   -20.126 1.00 9.13   ? 223 LEU B N   1 
ATOM   4089 C  CA  . LEU B  1 224 ? 64.043 0.742   -19.562 1.00 10.26  ? 223 LEU B CA  1 
ATOM   4090 C  C   . LEU B  1 224 ? 64.539 0.422   -18.184 1.00 9.31   ? 223 LEU B C   1 
ATOM   4091 O  O   . LEU B  1 224 ? 63.779 0.062   -17.287 1.00 10.10  ? 223 LEU B O   1 
ATOM   4092 C  CB  . LEU B  1 224 ? 64.253 -0.493  -20.490 1.00 11.37  ? 223 LEU B CB  1 
ATOM   4093 C  CG  . LEU B  1 224 ? 63.589 -0.348  -21.887 1.00 12.60  ? 223 LEU B CG  1 
ATOM   4094 C  CD1 . LEU B  1 224 ? 64.233 -1.442  -22.832 1.00 15.20  ? 223 LEU B CD1 1 
ATOM   4095 C  CD2 . LEU B  1 224 ? 62.097 -0.560  -21.696 1.00 14.65  ? 223 LEU B CD2 1 
ATOM   4096 N  N   . ALA B  1 225 ? 65.867 0.566   -17.956 1.00 9.39   ? 224 ALA B N   1 
ATOM   4097 C  CA  . ALA B  1 225 ? 66.431 0.285   -16.642 1.00 9.56   ? 224 ALA B CA  1 
ATOM   4098 C  C   . ALA B  1 225 ? 65.846 1.242   -15.602 1.00 9.15   ? 224 ALA B C   1 
ATOM   4099 O  O   . ALA B  1 225 ? 65.693 0.865   -14.434 1.00 9.28   ? 224 ALA B O   1 
ATOM   4100 C  CB  . ALA B  1 225 ? 67.970 0.476   -16.696 1.00 11.41  ? 224 ALA B CB  1 
ATOM   4101 N  N   . GLN B  1 226 ? 65.484 2.499   -15.988 1.00 9.02   ? 225 GLN B N   1 
ATOM   4102 C  CA  . GLN B  1 226 ? 64.857 3.377   -15.044 1.00 8.27   ? 225 GLN B CA  1 
ATOM   4103 C  C   . GLN B  1 226 ? 63.512 2.850   -14.595 1.00 8.63   ? 225 GLN B C   1 
ATOM   4104 O  O   . GLN B  1 226 ? 63.174 2.909   -13.418 1.00 9.90   ? 225 GLN B O   1 
ATOM   4105 C  CB  . GLN B  1 226 ? 64.689 4.788   -15.585 1.00 10.13  ? 225 GLN B CB  1 
ATOM   4106 C  CG  . GLN B  1 226 ? 66.018 5.492   -15.831 1.00 10.55  ? 225 GLN B CG  1 
ATOM   4107 C  CD  . GLN B  1 226 ? 65.851 6.936   -16.191 1.00 10.64  ? 225 GLN B CD  1 
ATOM   4108 O  OE1 . GLN B  1 226 ? 66.070 7.337   -17.352 1.00 12.33  ? 225 GLN B OE1 1 
ATOM   4109 N  NE2 . GLN B  1 226 ? 65.420 7.751   -15.241 1.00 12.98  ? 225 GLN B NE2 1 
ATOM   4110 N  N   . PHE B  1 227 ? 62.702 2.302   -15.527 1.00 8.62   ? 226 PHE B N   1 
ATOM   4111 C  CA  . PHE B  1 227 ? 61.437 1.687   -15.108 1.00 9.21   ? 226 PHE B CA  1 
ATOM   4112 C  C   . PHE B  1 227 ? 61.686 0.562   -14.098 1.00 8.81   ? 226 PHE B C   1 
ATOM   4113 O  O   . PHE B  1 227 ? 61.020 0.466   -13.086 1.00 9.48   ? 226 PHE B O   1 
ATOM   4114 C  CB  . PHE B  1 227 ? 60.696 1.112   -16.329 1.00 9.90   ? 226 PHE B CB  1 
ATOM   4115 C  CG  . PHE B  1 227 ? 60.167 2.038   -17.371 1.00 10.17  ? 226 PHE B CG  1 
ATOM   4116 C  CD1 . PHE B  1 227 ? 59.916 3.429   -17.082 1.00 13.95  ? 226 PHE B CD1 1 
ATOM   4117 C  CD2 . PHE B  1 227 ? 59.926 1.556   -18.650 1.00 13.89  ? 226 PHE B CD2 1 
ATOM   4118 C  CE1 . PHE B  1 227 ? 59.359 4.253   -18.033 1.00 17.58  ? 226 PHE B CE1 1 
ATOM   4119 C  CE2 . PHE B  1 227 ? 59.305 2.396   -19.583 1.00 15.81  ? 226 PHE B CE2 1 
ATOM   4120 C  CZ  . PHE B  1 227 ? 59.070 3.741   -19.294 1.00 16.97  ? 226 PHE B CZ  1 
ATOM   4121 N  N   . ARG B  1 228 ? 62.657 -0.301  -14.410 1.00 9.06   ? 227 ARG B N   1 
ATOM   4122 C  CA  . ARG B  1 228 ? 62.978 -1.473  -13.622 1.00 10.23  ? 227 ARG B CA  1 
ATOM   4123 C  C   . ARG B  1 228 ? 63.525 -1.150  -12.257 1.00 9.87   ? 227 ARG B C   1 
ATOM   4124 O  O   . ARG B  1 228 ? 63.501 -2.022  -11.377 1.00 13.38  ? 227 ARG B O   1 
ATOM   4125 C  CB  . ARG B  1 228 ? 63.970 -2.363  -14.377 1.00 11.01  ? 227 ARG B CB  1 
ATOM   4126 C  CG  . ARG B  1 228 ? 63.438 -2.907  -15.694 1.00 11.89  ? 227 ARG B CG  1 
ATOM   4127 C  CD  . ARG B  1 228 ? 64.259 -4.092  -16.174 1.00 18.44  ? 227 ARG B CD  1 
ATOM   4128 N  NE  . ARG B  1 228 ? 64.052 -4.361  -17.594 1.00 18.70  ? 227 ARG B NE  1 
ATOM   4129 C  CZ  . ARG B  1 228 ? 64.909 -4.021  -18.551 1.00 18.76  ? 227 ARG B CZ  1 
ATOM   4130 N  NH1 . ARG B  1 228 ? 66.037 -3.396  -18.243 1.00 20.17  ? 227 ARG B NH1 1 
ATOM   4131 N  NH2 . ARG B  1 228 ? 64.639 -4.306  -19.817 1.00 17.69  ? 227 ARG B NH2 1 
ATOM   4132 N  N   . SER B  1 229 ? 64.010 0.085   -12.085 1.00 9.35   ? 228 SER B N   1 
ATOM   4133 C  CA  . SER B  1 229 ? 64.569 0.484   -10.806 1.00 10.87  ? 228 SER B CA  1 
ATOM   4134 C  C   . SER B  1 229 ? 63.492 1.062   -9.871  1.00 9.76   ? 228 SER B C   1 
ATOM   4135 O  O   . SER B  1 229 ? 63.795 1.387   -8.716  1.00 10.91  ? 228 SER B O   1 
ATOM   4136 C  CB  . SER B  1 229 ? 65.718 1.447   -10.985 1.00 14.21  ? 228 SER B CB  1 
ATOM   4137 O  OG  . SER B  1 229 ? 65.182 2.667   -11.386 1.00 18.91  ? 228 SER B OG  1 
ATOM   4138 N  N   . LEU B  1 230 ? 62.271 1.292   -10.372 1.00 9.49   ? 229 LEU B N   1 
ATOM   4139 C  CA  . LEU B  1 230 ? 61.210 1.652   -9.421  1.00 9.08   ? 229 LEU B CA  1 
ATOM   4140 C  C   . LEU B  1 230 ? 61.037 0.491   -8.454  1.00 8.07   ? 229 LEU B C   1 
ATOM   4141 O  O   . LEU B  1 230 ? 61.318 -0.651  -8.768  1.00 11.26  ? 229 LEU B O   1 
ATOM   4142 C  CB  . LEU B  1 230 ? 59.937 1.871   -10.200 1.00 9.63   ? 229 LEU B CB  1 
ATOM   4143 C  CG  . LEU B  1 230 ? 59.815 3.143   -10.944 1.00 13.00  ? 229 LEU B CG  1 
ATOM   4144 C  CD1 . LEU B  1 230 ? 58.624 3.086   -11.840 1.00 14.80  ? 229 LEU B CD1 1 
ATOM   4145 C  CD2 . LEU B  1 230 ? 59.730 4.396   -9.889  1.00 14.13  ? 229 LEU B CD2 1 
ATOM   4146 N  N   . LEU B  1 231 ? 60.557 0.807   -7.252  1.00 8.18   ? 230 LEU B N   1 
ATOM   4147 C  CA  . LEU B  1 231 ? 60.446 -0.188  -6.167  1.00 8.82   ? 230 LEU B CA  1 
ATOM   4148 C  C   . LEU B  1 231 ? 59.017 -0.505  -5.855  1.00 8.65   ? 230 LEU B C   1 
ATOM   4149 O  O   . LEU B  1 231 ? 58.156 0.404   -5.774  1.00 9.20   ? 230 LEU B O   1 
ATOM   4150 C  CB  . LEU B  1 231 ? 61.174 0.354   -4.901  1.00 9.29   ? 230 LEU B CB  1 
ATOM   4151 C  CG  . LEU B  1 231 ? 62.655 0.692   -5.133  1.00 9.71   ? 230 LEU B CG  1 
ATOM   4152 C  CD1 . LEU B  1 231 ? 63.252 1.237   -3.835  1.00 11.68  ? 230 LEU B CD1 1 
ATOM   4153 C  CD2 . LEU B  1 231 ? 63.474 -0.529  -5.640  1.00 11.12  ? 230 LEU B CD2 1 
ATOM   4154 N  N   . SER B  1 232 ? 58.749 -1.760  -5.667  1.00 9.63   ? 231 SER B N   1 
ATOM   4155 C  CA  . SER B  1 232 ? 57.413 -2.251  -5.339  1.00 10.21  ? 231 SER B CA  1 
ATOM   4156 C  C   . SER B  1 232 ? 57.113 -2.237  -3.862  1.00 9.69   ? 231 SER B C   1 
ATOM   4157 O  O   . SER B  1 232 ? 55.929 -2.368  -3.505  1.00 11.69  ? 231 SER B O   1 
ATOM   4158 C  CB  . SER B  1 232 ? 57.231 -3.636  -5.880  1.00 10.75  ? 231 SER B CB  1 
ATOM   4159 O  OG  . SER B  1 232 ? 58.102 -4.564  -5.285  1.00 12.65  ? 231 SER B OG  1 
ATOM   4160 N  N   . ASN B  1 233 ? 58.109 -2.149  -3.028  1.00 10.29  ? 232 ASN B N   1 
ATOM   4161 C  CA  . ASN B  1 233 ? 57.927 -2.100  -1.591  1.00 10.63  ? 232 ASN B CA  1 
ATOM   4162 C  C   . ASN B  1 233 ? 57.579 -0.678  -1.144  1.00 9.40   ? 232 ASN B C   1 
ATOM   4163 O  O   . ASN B  1 233 ? 57.838 0.318   -1.865  1.00 9.88   ? 232 ASN B O   1 
ATOM   4164 C  CB  . ASN B  1 233 ? 59.238 -2.536  -0.916  1.00 10.66  ? 232 ASN B CB  1 
ATOM   4165 C  CG  . ASN B  1 233 ? 60.380 -1.688  -1.336  1.00 9.25   ? 232 ASN B CG  1 
ATOM   4166 O  OD1 . ASN B  1 233 ? 60.903 -1.864  -2.447  1.00 9.66   ? 232 ASN B OD1 1 
ATOM   4167 N  ND2 . ASN B  1 233 ? 60.819 -0.759  -0.506  1.00 10.00  ? 232 ASN B ND2 1 
ATOM   4168 N  N   . VAL B  1 234 ? 57.067 -0.605  0.064   1.00 10.60  ? 233 VAL B N   1 
ATOM   4169 C  CA  . VAL B  1 234 ? 56.888 0.704   0.713   1.00 10.24  ? 233 VAL B CA  1 
ATOM   4170 C  C   . VAL B  1 234 ? 58.225 1.182   1.290   1.00 9.39   ? 233 VAL B C   1 
ATOM   4171 O  O   . VAL B  1 234 ? 59.127 0.401   1.626   1.00 9.88   ? 233 VAL B O   1 
ATOM   4172 C  CB  . VAL B  1 234 ? 55.802 0.625   1.838   1.00 12.67  ? 233 VAL B CB  1 
ATOM   4173 C  CG1 . VAL B  1 234 ? 54.452 0.243   1.226   1.00 15.08  ? 233 VAL B CG1 1 
ATOM   4174 C  CG2 . VAL B  1 234 ? 56.227 -0.149  3.076   1.00 15.83  ? 233 VAL B CG2 1 
ATOM   4175 N  N   . GLU B  1 235 ? 58.303 2.510   1.484   1.00 9.43   ? 234 GLU B N   1 
ATOM   4176 C  CA  . GLU B  1 235 ? 59.528 3.132   2.023   1.00 9.30   ? 234 GLU B CA  1 
ATOM   4177 C  C   . GLU B  1 235 ? 59.859 2.469   3.358   1.00 9.69   ? 234 GLU B C   1 
ATOM   4178 O  O   . GLU B  1 235 ? 58.981 2.250   4.214   1.00 11.30  ? 234 GLU B O   1 
ATOM   4179 C  CB  . GLU B  1 235 ? 59.252 4.608   2.206   1.00 9.87   ? 234 GLU B CB  1 
ATOM   4180 C  CG  . GLU B  1 235 ? 60.450 5.354   2.779   1.00 10.68  ? 234 GLU B CG  1 
ATOM   4181 C  CD  . GLU B  1 235 ? 60.335 6.833   2.664   1.00 12.38  ? 234 GLU B CD  1 
ATOM   4182 O  OE1 . GLU B  1 235 ? 60.014 7.370   1.583   1.00 13.93  ? 234 GLU B OE1 1 
ATOM   4183 O  OE2 . GLU B  1 235 ? 60.715 7.553   3.644   1.00 14.30  ? 234 GLU B OE2 1 
ATOM   4184 N  N   . GLY B  1 236 ? 61.136 2.172   3.526   1.00 9.97   ? 235 GLY B N   1 
ATOM   4185 C  CA  . GLY B  1 236 ? 61.661 1.605   4.783   1.00 12.61  ? 235 GLY B CA  1 
ATOM   4186 C  C   . GLY B  1 236 ? 61.778 0.136   4.704   1.00 14.12  ? 235 GLY B C   1 
ATOM   4187 O  O   . GLY B  1 236 ? 62.597 -0.469  5.435   1.00 21.70  ? 235 GLY B O   1 
ATOM   4188 N  N   . ASP B  1 237 ? 61.029 -0.559  3.863   1.00 12.54  ? 236 ASP B N   1 
ATOM   4189 C  CA  . ASP B  1 237 ? 61.286 -1.969  3.705   1.00 14.26  ? 236 ASP B CA  1 
ATOM   4190 C  C   . ASP B  1 237 ? 62.408 -2.268  2.762   1.00 16.14  ? 236 ASP B C   1 
ATOM   4191 O  O   . ASP B  1 237 ? 62.926 -1.348  2.078   1.00 14.55  ? 236 ASP B O   1 
ATOM   4192 C  CB  . ASP B  1 237 ? 60.028 -2.591  3.211   1.00 16.71  ? 236 ASP B CB  1 
ATOM   4193 C  CG  . ASP B  1 237 ? 58.940 -2.732  4.255   1.00 21.20  ? 236 ASP B CG  1 
ATOM   4194 O  OD1 . ASP B  1 237 ? 59.238 -2.509  5.432   1.00 24.25  ? 236 ASP B OD1 1 
ATOM   4195 O  OD2 . ASP B  1 237 ? 57.801 -3.234  3.900   1.00 21.66  ? 236 ASP B OD2 1 
ATOM   4196 N  N   A ASN B  1 238 ? 63.027 -3.460  2.828   0.50 18.50  ? 237 ASN B N   1 
ATOM   4197 N  N   B ASN B  1 238 ? 62.890 -3.504  2.733   0.50 17.29  ? 237 ASN B N   1 
ATOM   4198 C  CA  A ASN B  1 238 ? 64.129 -3.718  1.863   0.50 19.52  ? 237 ASN B CA  1 
ATOM   4199 C  CA  B ASN B  1 238 ? 63.973 -3.849  1.813   0.50 19.70  ? 237 ASN B CA  1 
ATOM   4200 C  C   A ASN B  1 238 ? 63.556 -3.497  0.456   0.50 16.01  ? 237 ASN B C   1 
ATOM   4201 C  C   B ASN B  1 238 ? 63.519 -3.582  0.367   0.50 16.43  ? 237 ASN B C   1 
ATOM   4202 O  O   A ASN B  1 238 ? 62.437 -3.916  0.159   0.50 16.33  ? 237 ASN B O   1 
ATOM   4203 O  O   B ASN B  1 238 ? 62.384 -3.819  0.030   0.50 15.07  ? 237 ASN B O   1 
ATOM   4204 C  CB  A ASN B  1 238 ? 64.926 -5.054  2.041   0.50 24.80  ? 237 ASN B CB  1 
ATOM   4205 C  CB  B ASN B  1 238 ? 64.442 -5.300  2.002   0.50 19.70  ? 237 ASN B CB  1 
ATOM   4206 C  CG  A ASN B  1 238 ? 66.359 -4.979  1.443   0.50 24.59  ? 237 ASN B CG  1 
ATOM   4207 C  CG  B ASN B  1 238 ? 63.441 -6.319  1.500   0.50 35.21  ? 237 ASN B CG  1 
ATOM   4208 O  OD1 A ASN B  1 238 ? 66.625 -4.091  0.633   0.50 23.16  ? 237 ASN B OD1 1 
ATOM   4209 O  OD1 B ASN B  1 238 ? 63.804 -7.292  0.815   0.50 58.02  ? 237 ASN B OD1 1 
ATOM   4210 N  ND2 A ASN B  1 238 ? 67.284 -5.907  1.838   0.50 15.46  ? 237 ASN B ND2 1 
ATOM   4211 N  ND2 B ASN B  1 238 ? 62.191 -6.122  1.821   0.50 54.21  ? 237 ASN B ND2 1 
ATOM   4212 N  N   . ALA B  1 239 ? 64.419 -3.047  -0.444  1.00 15.68  ? 238 ALA B N   1 
ATOM   4213 C  CA  . ALA B  1 239 ? 64.061 -2.643  -1.762  1.00 13.44  ? 238 ALA B CA  1 
ATOM   4214 C  C   . ALA B  1 239 ? 63.750 -3.867  -2.654  1.00 15.67  ? 238 ALA B C   1 
ATOM   4215 O  O   . ALA B  1 239 ? 64.456 -4.882  -2.685  1.00 21.59  ? 238 ALA B O   1 
ATOM   4216 C  CB  . ALA B  1 239 ? 65.186 -1.763  -2.272  1.00 16.61  ? 238 ALA B CB  1 
ATOM   4217 N  N   . VAL B  1 240 ? 62.684 -3.823  -3.387  1.00 11.64  ? 239 VAL B N   1 
ATOM   4218 C  CA  . VAL B  1 240 ? 62.277 -4.861  -4.304  1.00 12.91  ? 239 VAL B CA  1 
ATOM   4219 C  C   . VAL B  1 240 ? 62.002 -4.202  -5.659  1.00 11.42  ? 239 VAL B C   1 
ATOM   4220 O  O   . VAL B  1 240 ? 60.905 -3.634  -5.851  1.00 13.30  ? 239 VAL B O   1 
ATOM   4221 C  CB  . VAL B  1 240 ? 61.056 -5.625  -3.824  1.00 15.37  ? 239 VAL B CB  1 
ATOM   4222 C  CG1 . VAL B  1 240 ? 60.658 -6.758  -4.769  1.00 18.28  ? 239 VAL B CG1 1 
ATOM   4223 C  CG2 . VAL B  1 240 ? 61.299 -6.308  -2.395  1.00 18.24  ? 239 VAL B CG2 1 
ATOM   4224 N  N   . PRO B  1 241 ? 62.923 -4.244  -6.609  1.00 11.07  ? 240 PRO B N   1 
ATOM   4225 C  CA  . PRO B  1 241 ? 62.667 -3.588  -7.898  1.00 11.40  ? 240 PRO B CA  1 
ATOM   4226 C  C   . PRO B  1 241 ? 61.482 -4.184  -8.607  1.00 10.27  ? 240 PRO B C   1 
ATOM   4227 O  O   . PRO B  1 241 ? 61.172 -5.366  -8.538  1.00 11.58  ? 240 PRO B O   1 
ATOM   4228 C  CB  . PRO B  1 241 ? 63.935 -3.907  -8.700  1.00 13.96  ? 240 PRO B CB  1 
ATOM   4229 C  CG  . PRO B  1 241 ? 65.002 -3.910  -7.596  1.00 18.90  ? 240 PRO B CG  1 
ATOM   4230 C  CD  . PRO B  1 241 ? 64.298 -4.715  -6.454  1.00 14.78  ? 240 PRO B CD  1 
ATOM   4231 N  N   . MET B  1 242 ? 60.841 -3.314  -9.414  1.00 10.54  ? 241 MET B N   1 
ATOM   4232 C  CA  . MET B  1 242 ? 59.688 -3.704  -10.269 1.00 11.12  ? 241 MET B CA  1 
ATOM   4233 C  C   . MET B  1 242 ? 60.292 -4.276  -11.588 1.00 10.99  ? 241 MET B C   1 
ATOM   4234 O  O   . MET B  1 242 ? 60.466 -3.569  -12.565 1.00 12.66  ? 241 MET B O   1 
ATOM   4235 C  CB  . MET B  1 242 ? 58.931 -2.533  -10.629 1.00 15.09  ? 241 MET B CB  1 
ATOM   4236 C  CG  . MET B  1 242 ? 58.043 -1.991  -9.656  1.00 16.34  ? 241 MET B CG  1 
ATOM   4237 S  SD  . MET B  1 242 ? 56.964 -0.660  -10.421 1.00 13.58  ? 241 MET B SD  1 
ATOM   4238 C  CE  . MET B  1 242 ? 56.643 0.144   -8.872  1.00 12.65  ? 241 MET B CE  1 
ATOM   4239 N  N   . GLN B  1 243 ? 60.642 -5.548  -11.535 1.00 11.46  ? 242 GLN B N   1 
ATOM   4240 C  CA  . GLN B  1 243 ? 61.419 -6.102  -12.654 1.00 12.99  ? 242 GLN B CA  1 
ATOM   4241 C  C   . GLN B  1 243 ? 60.573 -6.252  -13.936 1.00 11.71  ? 242 GLN B C   1 
ATOM   4242 O  O   . GLN B  1 243 ? 61.135 -6.173  -15.034 1.00 12.98  ? 242 GLN B O   1 
ATOM   4243 C  CB  . GLN B  1 243 ? 62.043 -7.424  -12.252 1.00 16.50  ? 242 GLN B CB  1 
ATOM   4244 C  CG  . GLN B  1 243 ? 63.250 -7.217  -11.393 1.00 26.13  ? 242 GLN B CG  1 
ATOM   4245 C  CD  . GLN B  1 243 ? 63.978 -8.475  -11.194 1.00 34.98  ? 242 GLN B CD  1 
ATOM   4246 O  OE1 . GLN B  1 243 ? 64.034 -9.034  -10.110 1.00 56.24  ? 242 GLN B OE1 1 
ATOM   4247 N  NE2 . GLN B  1 243 ? 64.600 -8.930  -12.290 1.00 33.13  ? 242 GLN B NE2 1 
ATOM   4248 N  N   . HIS B  1 244 ? 59.257 -6.510  -13.823 1.00 10.60  ? 243 HIS B N   1 
ATOM   4249 C  CA  . HIS B  1 244 ? 58.431 -6.759  -14.968 1.00 9.55   ? 243 HIS B CA  1 
ATOM   4250 C  C   . HIS B  1 244 ? 56.989 -6.606  -14.577 1.00 9.27   ? 243 HIS B C   1 
ATOM   4251 O  O   . HIS B  1 244 ? 56.613 -6.774  -13.387 1.00 10.23  ? 243 HIS B O   1 
ATOM   4252 C  CB  . HIS B  1 244 ? 58.727 -8.123  -15.595 1.00 11.78  ? 243 HIS B CB  1 
ATOM   4253 C  CG  . HIS B  1 244 ? 58.574 -9.259  -14.644 1.00 13.85  ? 243 HIS B CG  1 
ATOM   4254 N  ND1 . HIS B  1 244 ? 57.388 -9.927  -14.481 1.00 19.54  ? 243 HIS B ND1 1 
ATOM   4255 C  CD2 . HIS B  1 244 ? 59.490 -9.877  -13.823 1.00 18.84  ? 243 HIS B CD2 1 
ATOM   4256 C  CE1 . HIS B  1 244 ? 57.596 -10.877 -13.539 1.00 20.04  ? 243 HIS B CE1 1 
ATOM   4257 N  NE2 . HIS B  1 244 ? 58.848 -10.857 -13.138 1.00 20.62  ? 243 HIS B NE2 1 
ATOM   4258 N  N   . ASN B  1 245 ? 56.122 -6.360  -15.584 1.00 8.70   ? 244 ASN B N   1 
ATOM   4259 C  CA  . ASN B  1 245 ? 54.695 -6.227  -15.313 1.00 8.74   ? 244 ASN B CA  1 
ATOM   4260 C  C   . ASN B  1 245 ? 53.891 -6.480  -16.593 1.00 9.03   ? 244 ASN B C   1 
ATOM   4261 O  O   . ASN B  1 245 ? 52.804 -5.913  -16.737 1.00 9.13   ? 244 ASN B O   1 
ATOM   4262 C  CB  . ASN B  1 245 ? 54.361 -4.886  -14.676 1.00 9.26   ? 244 ASN B CB  1 
ATOM   4263 C  CG  . ASN B  1 245 ? 54.900 -3.733  -15.458 1.00 8.02   ? 244 ASN B CG  1 
ATOM   4264 O  OD1 . ASN B  1 245 ? 55.192 -3.861  -16.657 1.00 8.43   ? 244 ASN B OD1 1 
ATOM   4265 N  ND2 . ASN B  1 245 ? 54.995 -2.555  -14.831 1.00 8.98   ? 244 ASN B ND2 1 
ATOM   4266 N  N   . ASN B  1 246 ? 54.394 -7.347  -17.459 1.00 9.37   ? 245 ASN B N   1 
ATOM   4267 C  CA  . ASN B  1 246 ? 53.671 -7.676  -18.673 1.00 10.00  ? 245 ASN B CA  1 
ATOM   4268 C  C   . ASN B  1 246 ? 52.974 -9.017  -18.595 1.00 10.61  ? 245 ASN B C   1 
ATOM   4269 O  O   . ASN B  1 246 ? 53.578 -10.000 -18.171 1.00 14.86  ? 245 ASN B O   1 
ATOM   4270 C  CB  . ASN B  1 246 ? 54.576 -7.594  -19.919 1.00 10.72  ? 245 ASN B CB  1 
ATOM   4271 C  CG  . ASN B  1 246 ? 55.764 -8.547  -19.863 1.00 11.44  ? 245 ASN B CG  1 
ATOM   4272 O  OD1 . ASN B  1 246 ? 56.394 -8.793  -18.839 1.00 11.83  ? 245 ASN B OD1 1 
ATOM   4273 N  ND2 . ASN B  1 246 ? 56.080 -9.055  -21.055 1.00 18.64  ? 245 ASN B ND2 1 
ATOM   4274 N  N   . ARG B  1 247 ? 51.743 -9.081  -19.026 1.00 10.31  ? 246 ARG B N   1 
ATOM   4275 C  CA  . ARG B  1 247 ? 50.998 -10.351 -19.017 1.00 11.81  ? 246 ARG B CA  1 
ATOM   4276 C  C   . ARG B  1 247 ? 51.310 -11.121 -20.313 1.00 11.83  ? 246 ARG B C   1 
ATOM   4277 O  O   . ARG B  1 247 ? 51.441 -10.463 -21.368 1.00 11.91  ? 246 ARG B O   1 
ATOM   4278 C  CB  . ARG B  1 247 ? 49.483 -9.995  -19.041 1.00 11.57  ? 246 ARG B CB  1 
ATOM   4279 C  CG  . ARG B  1 247 ? 48.633 -11.265 -18.785 1.00 12.15  ? 246 ARG B CG  1 
ATOM   4280 C  CD  . ARG B  1 247 ? 47.158 -11.000 -19.028 1.00 12.26  ? 246 ARG B CD  1 
ATOM   4281 N  NE  . ARG B  1 247 ? 46.390 -12.164 -18.578 1.00 12.42  ? 246 ARG B NE  1 
ATOM   4282 C  CZ  . ARG B  1 247 ? 45.079 -12.298 -18.726 1.00 13.72  ? 246 ARG B CZ  1 
ATOM   4283 N  NH1 . ARG B  1 247 ? 44.389 -11.419 -19.460 1.00 12.94  ? 246 ARG B NH1 1 
ATOM   4284 N  NH2 . ARG B  1 247 ? 44.427 -13.350 -18.200 1.00 14.93  ? 246 ARG B NH2 1 
ATOM   4285 N  N   . PRO B  1 248 ? 51.404 -12.455 -20.272 1.00 11.93  ? 247 PRO B N   1 
ATOM   4286 C  CA  . PRO B  1 248 ? 51.520 -13.203 -21.552 1.00 13.07  ? 247 PRO B CA  1 
ATOM   4287 C  C   . PRO B  1 248 ? 50.309 -12.946 -22.431 1.00 12.11  ? 247 PRO B C   1 
ATOM   4288 O  O   . PRO B  1 248 ? 49.175 -12.612 -22.004 1.00 12.99  ? 247 PRO B O   1 
ATOM   4289 C  CB  . PRO B  1 248 ? 51.497 -14.649 -21.054 1.00 14.69  ? 247 PRO B CB  1 
ATOM   4290 C  CG  . PRO B  1 248 ? 52.028 -14.596 -19.629 1.00 18.51  ? 247 PRO B CG  1 
ATOM   4291 C  CD  . PRO B  1 248 ? 51.455 -13.312 -19.088 1.00 14.39  ? 247 PRO B CD  1 
ATOM   4292 N  N   . THR B  1 249 ? 50.499 -13.193 -23.732 1.00 12.46  ? 248 THR B N   1 
ATOM   4293 C  CA  . THR B  1 249 ? 49.432 -13.115 -24.666 1.00 11.04  ? 248 THR B CA  1 
ATOM   4294 C  C   . THR B  1 249 ? 48.408 -14.256 -24.499 1.00 13.20  ? 248 THR B C   1 
ATOM   4295 O  O   . THR B  1 249 ? 48.782 -15.356 -24.041 1.00 14.05  ? 248 THR B O   1 
ATOM   4296 C  CB  . THR B  1 249 ? 49.887 -13.027 -26.114 1.00 13.18  ? 248 THR B CB  1 
ATOM   4297 O  OG1 . THR B  1 249 ? 50.707 -14.161 -26.382 1.00 14.68  ? 248 THR B OG1 1 
ATOM   4298 C  CG2 . THR B  1 249 ? 50.653 -11.757 -26.391 1.00 12.64  ? 248 THR B CG2 1 
ATOM   4299 N  N   . GLN B  1 250 ? 47.151 -13.940 -24.788 1.00 13.41  ? 249 GLN B N   1 
ATOM   4300 C  CA  . GLN B  1 250 ? 46.009 -14.824 -24.436 1.00 14.13  ? 249 GLN B CA  1 
ATOM   4301 C  C   . GLN B  1 250 ? 45.347 -15.261 -25.677 1.00 13.96  ? 249 GLN B C   1 
ATOM   4302 O  O   . GLN B  1 250 ? 45.411 -14.644 -26.750 1.00 15.53  ? 249 GLN B O   1 
ATOM   4303 C  CB  . GLN B  1 250 ? 44.989 -13.991 -23.595 1.00 15.09  ? 249 GLN B CB  1 
ATOM   4304 C  CG  . GLN B  1 250 ? 45.645 -13.565 -22.320 1.00 14.98  ? 249 GLN B CG  1 
ATOM   4305 C  CD  . GLN B  1 250 ? 46.173 -14.699 -21.433 1.00 16.64  ? 249 GLN B CD  1 
ATOM   4306 O  OE1 . GLN B  1 250 ? 45.503 -15.697 -21.225 1.00 18.73  ? 249 GLN B OE1 1 
ATOM   4307 N  NE2 . GLN B  1 250 ? 47.394 -14.567 -20.906 1.00 16.73  ? 249 GLN B NE2 1 
ATOM   4308 N  N   . PRO B  1 251 ? 44.547 -16.384 -25.608 1.00 15.76  ? 250 PRO B N   1 
ATOM   4309 C  CA  . PRO B  1 251 ? 43.951 -16.928 -26.839 1.00 18.09  ? 250 PRO B CA  1 
ATOM   4310 C  C   . PRO B  1 251 ? 42.970 -15.991 -27.485 1.00 15.47  ? 250 PRO B C   1 
ATOM   4311 O  O   . PRO B  1 251 ? 42.140 -15.367 -26.773 1.00 15.32  ? 250 PRO B O   1 
ATOM   4312 C  CB  . PRO B  1 251 ? 43.180 -18.136 -26.329 1.00 26.22  ? 250 PRO B CB  1 
ATOM   4313 C  CG  . PRO B  1 251 ? 43.817 -18.514 -25.027 1.00 24.56  ? 250 PRO B CG  1 
ATOM   4314 C  CD  . PRO B  1 251 ? 44.364 -17.278 -24.452 1.00 18.55  ? 250 PRO B CD  1 
ATOM   4315 N  N   . LEU B  1 252 ? 42.918 -15.896 -28.801 1.00 19.76  ? 251 LEU B N   1 
ATOM   4316 C  CA  . LEU B  1 252 ? 42.012 -15.054 -29.571 1.00 19.65  ? 251 LEU B CA  1 
ATOM   4317 C  C   . LEU B  1 252 ? 40.568 -15.490 -29.411 1.00 16.93  ? 251 LEU B C   1 
ATOM   4318 O  O   . LEU B  1 252 ? 39.671 -14.641 -29.441 1.00 18.76  ? 251 LEU B O   1 
ATOM   4319 C  CB  . LEU B  1 252 ? 42.391 -15.108 -31.042 1.00 23.87  ? 251 LEU B CB  1 
ATOM   4320 C  CG  . LEU B  1 252 ? 42.184 -13.815 -31.818 1.00 28.30  ? 251 LEU B CG  1 
ATOM   4321 C  CD1 . LEU B  1 252 ? 42.744 -12.630 -31.046 1.00 23.14  ? 251 LEU B CD1 1 
ATOM   4322 C  CD2 . LEU B  1 252 ? 42.894 -13.977 -33.142 1.00 27.30  ? 251 LEU B CD2 1 
ATOM   4323 N  N   . LYS B  1 253 ? 40.339 -16.807 -29.348 1.00 20.36  ? 252 LYS B N   1 
ATOM   4324 C  CA  . LYS B  1 253 ? 39.001 -17.316 -29.058 1.00 21.84  ? 252 LYS B CA  1 
ATOM   4325 C  C   . LYS B  1 253 ? 38.066 -16.783 -30.109 1.00 22.70  ? 252 LYS B C   1 
ATOM   4326 O  O   . LYS B  1 253 ? 36.879 -16.503 -29.854 1.00 23.61  ? 252 LYS B O   1 
ATOM   4327 C  CB  . LYS B  1 253 ? 38.530 -17.055 -27.580 1.00 21.86  ? 252 LYS B CB  1 
ATOM   4328 C  CG  . LYS B  1 253 ? 39.281 -17.755 -26.450 1.00 25.65  ? 252 LYS B CG  1 
ATOM   4329 C  CD  . LYS B  1 253 ? 39.109 -19.213 -26.353 1.00 32.18  ? 252 LYS B CD  1 
ATOM   4330 C  CE  . LYS B  1 253 ? 39.691 -19.671 -25.038 1.00 39.76  ? 252 LYS B CE  1 
ATOM   4331 N  NZ  . LYS B  1 253 ? 39.269 -21.130 -24.836 1.00 57.87  ? 252 LYS B NZ  1 
ATOM   4332 N  N   . GLY B  1 254 ? 38.509 -16.809 -31.369 1.00 23.66  ? 253 GLY B N   1 
ATOM   4333 C  CA  . GLY B  1 254 ? 37.585 -16.421 -32.480 1.00 23.07  ? 253 GLY B CA  1 
ATOM   4334 C  C   . GLY B  1 254 ? 37.414 -14.998 -32.769 1.00 22.87  ? 253 GLY B C   1 
ATOM   4335 O  O   . GLY B  1 254 ? 36.645 -14.677 -33.660 1.00 25.19  ? 253 GLY B O   1 
ATOM   4336 N  N   . ARG B  1 255 ? 38.012 -14.077 -31.949 1.00 18.51  ? 254 ARG B N   1 
ATOM   4337 C  CA  . ARG B  1 255 ? 37.925 -12.651 -32.284 1.00 18.05  ? 254 ARG B CA  1 
ATOM   4338 C  C   . ARG B  1 255 ? 38.678 -12.305 -33.570 1.00 18.24  ? 254 ARG B C   1 
ATOM   4339 O  O   . ARG B  1 255 ? 39.592 -13.081 -34.025 1.00 22.97  ? 254 ARG B O   1 
ATOM   4340 C  CB  . ARG B  1 255 ? 38.611 -11.875 -31.142 1.00 15.70  ? 254 ARG B CB  1 
ATOM   4341 C  CG  . ARG B  1 255 ? 37.692 -11.944 -29.872 1.00 17.60  ? 254 ARG B CG  1 
ATOM   4342 C  CD  . ARG B  1 255 ? 38.501 -11.262 -28.723 1.00 15.95  ? 254 ARG B CD  1 
ATOM   4343 N  NE  . ARG B  1 255 ? 39.557 -12.111 -28.237 1.00 14.84  ? 254 ARG B NE  1 
ATOM   4344 C  CZ  . ARG B  1 255 ? 40.420 -11.717 -27.284 1.00 12.56  ? 254 ARG B CZ  1 
ATOM   4345 N  NH1 . ARG B  1 255 ? 40.357 -10.448 -26.835 1.00 13.84  ? 254 ARG B NH1 1 
ATOM   4346 N  NH2 . ARG B  1 255 ? 41.291 -12.543 -26.845 1.00 13.20  ? 254 ARG B NH2 1 
ATOM   4347 N  N   . THR B  1 256 ? 38.224 -11.227 -34.203 1.00 18.44  ? 255 THR B N   1 
ATOM   4348 C  CA  . THR B  1 256 ? 38.947 -10.721 -35.369 1.00 19.80  ? 255 THR B CA  1 
ATOM   4349 C  C   . THR B  1 256 ? 39.692 -9.412  -35.074 1.00 18.57  ? 255 THR B C   1 
ATOM   4350 O  O   . THR B  1 256 ? 39.094 -8.539  -34.428 1.00 20.73  ? 255 THR B O   1 
ATOM   4351 C  CB  . THR B  1 256 ? 37.908 -10.388 -36.442 1.00 24.73  ? 255 THR B CB  1 
ATOM   4352 O  OG1 . THR B  1 256 ? 37.221 -11.582 -36.779 1.00 30.79  ? 255 THR B OG1 1 
ATOM   4353 C  CG2 . THR B  1 256 ? 38.521 -9.839  -37.642 1.00 27.14  ? 255 THR B CG2 1 
ATOM   4354 N  N   . VAL B  1 257 ? 40.972 -9.385  -35.419 1.00 17.03  ? 256 VAL B N   1 
ATOM   4355 C  CA  . VAL B  1 257 ? 41.746 -8.170  -35.277 1.00 14.58  ? 256 VAL B CA  1 
ATOM   4356 C  C   . VAL B  1 257 ? 41.561 -7.456  -36.618 1.00 14.19  ? 256 VAL B C   1 
ATOM   4357 O  O   . VAL B  1 257 ? 41.883 -8.008  -37.661 1.00 17.34  ? 256 VAL B O   1 
ATOM   4358 C  CB  . VAL B  1 257 ? 43.212 -8.452  -34.957 1.00 15.24  ? 256 VAL B CB  1 
ATOM   4359 C  CG1 . VAL B  1 257 ? 43.969 -7.097  -34.922 1.00 17.37  ? 256 VAL B CG1 1 
ATOM   4360 C  CG2 . VAL B  1 257 ? 43.341 -9.335  -33.703 1.00 15.83  ? 256 VAL B CG2 1 
ATOM   4361 N  N   . ARG B  1 258 ? 40.988 -6.254  -36.565 1.00 14.51  ? 257 ARG B N   1 
ATOM   4362 C  CA  . ARG B  1 258 ? 40.839 -5.395  -37.717 1.00 15.59  ? 257 ARG B CA  1 
ATOM   4363 C  C   . ARG B  1 258 ? 41.983 -4.483  -37.932 1.00 13.77  ? 257 ARG B C   1 
ATOM   4364 O  O   . ARG B  1 258 ? 42.531 -4.010  -36.974 1.00 16.47  ? 257 ARG B O   1 
ATOM   4365 C  CB  . ARG B  1 258 ? 39.547 -4.625  -37.703 1.00 17.94  ? 257 ARG B CB  1 
ATOM   4366 C  CG  . ARG B  1 258 ? 38.270 -5.490  -37.681 1.00 19.67  ? 257 ARG B CG  1 
ATOM   4367 C  CD  . ARG B  1 258 ? 37.023 -4.668  -37.691 1.00 21.71  ? 257 ARG B CD  1 
ATOM   4368 N  NE  . ARG B  1 258 ? 36.887 -4.041  -36.350 1.00 19.56  ? 257 ARG B NE  1 
ATOM   4369 C  CZ  . ARG B  1 258 ? 36.048 -3.045  -36.023 1.00 21.66  ? 257 ARG B CZ  1 
ATOM   4370 N  NH1 . ARG B  1 258 ? 35.396 -2.395  -36.968 1.00 24.42  ? 257 ARG B NH1 1 
ATOM   4371 N  NH2 . ARG B  1 258 ? 35.993 -2.608  -34.770 1.00 21.17  ? 257 ARG B NH2 1 
ATOM   4372 N  N   . ALA B  1 259 ? 42.317 -4.195  -39.171 1.00 15.62  ? 258 ALA B N   1 
ATOM   4373 C  CA  . ALA B  1 259 ? 43.350 -3.245  -39.542 1.00 15.21  ? 258 ALA B CA  1 
ATOM   4374 C  C   . ALA B  1 259 ? 42.756 -2.035  -40.168 1.00 16.49  ? 258 ALA B C   1 
ATOM   4375 O  O   . ALA B  1 259 ? 41.867 -2.134  -41.038 1.00 17.60  ? 258 ALA B O   1 
ATOM   4376 C  CB  . ALA B  1 259 ? 44.411 -3.958  -40.417 1.00 17.88  ? 258 ALA B CB  1 
ATOM   4377 N  N   . SER B  1 260 ? 43.322 -0.870  -39.841 1.00 16.28  ? 259 SER B N   1 
ATOM   4378 C  CA  . SER B  1 260 ? 42.910 0.375   -40.418 1.00 15.89  ? 259 SER B CA  1 
ATOM   4379 C  C   . SER B  1 260 ? 43.639 0.638   -41.766 1.00 17.83  ? 259 SER B C   1 
ATOM   4380 O  O   . SER B  1 260 ? 43.375 1.655   -42.437 1.00 21.33  ? 259 SER B O   1 
ATOM   4381 C  CB  . SER B  1 260 ? 43.132 1.611   -39.525 1.00 19.07  ? 259 SER B CB  1 
ATOM   4382 O  OG  . SER B  1 260 ? 44.507 1.907   -39.459 1.00 16.79  ? 259 SER B OG  1 
ATOM   4383 N  N   . PHE B  1 261 ? 44.545 -0.295  -42.183 1.00 17.27  ? 260 PHE B N   1 
ATOM   4384 C  CA  . PHE B  1 261 ? 45.431 0.076   -43.248 1.00 18.21  ? 260 PHE B CA  1 
ATOM   4385 C  C   . PHE B  1 261 ? 45.663 -1.233  -43.952 1.00 20.76  ? 260 PHE B C   1 
ATOM   4386 O  O   . PHE B  1 261 ? 46.305 -1.172  -45.078 1.00 27.12  ? 260 PHE B O   1 
ATOM   4387 C  CB  . PHE B  1 261 ? 46.804 0.612   -42.695 1.00 18.31  ? 260 PHE B CB  1 
ATOM   4388 C  CG  . PHE B  1 261 ? 47.496 -0.398  -41.792 1.00 16.96  ? 260 PHE B CG  1 
ATOM   4389 C  CD1 . PHE B  1 261 ? 47.117 -0.536  -40.447 1.00 16.28  ? 260 PHE B CD1 1 
ATOM   4390 C  CD2 . PHE B  1 261 ? 48.504 -1.275  -42.259 1.00 18.13  ? 260 PHE B CD2 1 
ATOM   4391 C  CE1 . PHE B  1 261 ? 47.713 -1.517  -39.688 1.00 16.48  ? 260 PHE B CE1 1 
ATOM   4392 C  CE2 . PHE B  1 261 ? 49.082 -2.261  -41.472 1.00 19.52  ? 260 PHE B CE2 1 
ATOM   4393 C  CZ  . PHE B  1 261 ? 48.674 -2.379  -40.140 1.00 17.27  ? 260 PHE B CZ  1 
ATOM   4394 O  OXT . PHE B  1 261 ? 45.311 -2.338  -43.462 1.00 21.71  ? 260 PHE B OXT 1 
HETATM 4395 ZN ZN  . ZN  C  2 .   ? 24.654 -0.568  -1.090  1.00 7.45   ? 301 ZN  A ZN  1 
HETATM 4396 O  O18 A 84Z D  3 .   ? 30.377 2.858   -6.577  0.50 691.13 ? 302 84Z A O18 1 
HETATM 4397 O  O18 B 84Z D  3 .   ? 28.743 0.777   -7.615  0.50 22.66  ? 302 84Z A O18 1 
HETATM 4398 S  S16 A 84Z D  3 .   ? 31.091 1.681   -5.874  0.50 16.95  ? 302 84Z A S16 1 
HETATM 4399 S  S16 B 84Z D  3 .   ? 29.771 1.255   -6.653  0.50 16.77  ? 302 84Z A S16 1 
HETATM 4400 O  O17 A 84Z D  3 .   ? 32.136 2.306   -5.114  0.50 18.40  ? 302 84Z A O17 1 
HETATM 4401 O  O17 B 84Z D  3 .   ? 30.047 2.659   -6.637  0.50 15.25  ? 302 84Z A O17 1 
HETATM 4402 C  C19 A 84Z D  3 .   ? 31.875 0.554   -6.788  0.50 14.25  ? 302 84Z A C19 1 
HETATM 4403 C  C19 B 84Z D  3 .   ? 31.340 0.629   -6.869  0.50 17.94  ? 302 84Z A C19 1 
HETATM 4404 C  C24 A 84Z D  3 .   ? 31.564 0.488   -8.119  0.50 20.60  ? 302 84Z A C24 1 
HETATM 4405 C  C24 B 84Z D  3 .   ? 31.364 -0.516  -7.658  0.50 27.29  ? 302 84Z A C24 1 
HETATM 4406 C  C23 A 84Z D  3 .   ? 32.140 -0.364  -9.060  0.50 23.37  ? 302 84Z A C23 1 
HETATM 4407 C  C23 B 84Z D  3 .   ? 32.583 -1.088  -8.088  0.50 25.85  ? 302 84Z A C23 1 
HETATM 4408 C  C22 A 84Z D  3 .   ? 33.172 -1.117  -8.524  0.50 19.04  ? 302 84Z A C22 1 
HETATM 4409 C  C22 B 84Z D  3 .   ? 33.810 -0.521  -7.659  0.50 33.82  ? 302 84Z A C22 1 
HETATM 4410 C  C21 A 84Z D  3 .   ? 33.677 -0.976  -7.206  0.50 18.62  ? 302 84Z A C21 1 
HETATM 4411 C  C21 B 84Z D  3 .   ? 33.704 0.641   -6.850  0.50 35.38  ? 302 84Z A C21 1 
HETATM 4412 C  C20 A 84Z D  3 .   ? 32.960 -0.162  -6.342  0.50 18.81  ? 302 84Z A C20 1 
HETATM 4413 C  C20 B 84Z D  3 .   ? 32.490 1.223   -6.463  0.50 24.08  ? 302 84Z A C20 1 
HETATM 4414 C  C3  A 84Z D  3 .   ? 30.108 0.827   -4.638  0.50 11.92  ? 302 84Z A C3  1 
HETATM 4415 C  C3  B 84Z D  3 .   ? 29.367 0.581   -5.076  0.50 15.59  ? 302 84Z A C3  1 
HETATM 4416 C  C2  A 84Z D  3 .   ? 30.560 0.761   -3.407  0.50 13.09  ? 302 84Z A C2  1 
HETATM 4417 C  C2  B 84Z D  3 .   ? 28.910 -0.747  -4.992  0.50 15.33  ? 302 84Z A C2  1 
HETATM 4418 C  C4  A 84Z D  3 .   ? 28.768 0.410   -4.906  0.50 13.95  ? 302 84Z A C4  1 
HETATM 4419 C  C4  B 84Z D  3 .   ? 29.476 1.353   -3.920  0.50 13.07  ? 302 84Z A C4  1 
HETATM 4420 C  C12 A 84Z D  3 .   ? 28.119 0.464   -6.162  0.50 17.25  ? 302 84Z A C12 1 
HETATM 4421 C  C12 B 84Z D  3 .   ? 30.052 2.743   -3.854  0.50 18.82  ? 302 84Z A C12 1 
HETATM 4422 O  O14 A 84Z D  3 .   ? 28.787 -0.100  -7.231  0.50 20.81  ? 302 84Z A O14 1 
HETATM 4423 O  O14 B 84Z D  3 .   ? 31.308 2.626   -3.516  0.50 21.07  ? 302 84Z A O14 1 
HETATM 4424 C  C15 A 84Z D  3 .   ? 28.148 -0.174  -8.449  0.50 22.97  ? 302 84Z A C15 1 
HETATM 4425 C  C15 B 84Z D  3 .   ? 32.068 1.898   -4.376  0.50 38.18  ? 302 84Z A C15 1 
HETATM 4426 O  O13 A 84Z D  3 .   ? 27.127 1.096   -6.185  0.50 17.70  ? 302 84Z A O13 1 
HETATM 4427 O  O13 B 84Z D  3 .   ? 29.434 3.739   -3.836  0.50 18.73  ? 302 84Z A O13 1 
HETATM 4428 C  C5  A 84Z D  3 .   ? 27.969 -0.130  -3.878  0.50 12.06  ? 302 84Z A C5  1 
HETATM 4429 C  C5  B 84Z D  3 .   ? 28.989 0.886   -2.781  0.50 10.54  ? 302 84Z A C5  1 
HETATM 4430 C  C6  A 84Z D  3 .   ? 28.536 -0.287  -2.593  0.50 11.05  ? 302 84Z A C6  1 
HETATM 4431 C  C6  B 84Z D  3 .   ? 28.418 -0.400  -2.692  0.50 8.44   ? 302 84Z A C6  1 
HETATM 4432 C  C1  A 84Z D  3 .   ? 29.864 0.156   -2.427  0.50 12.34  ? 302 84Z A C1  1 
HETATM 4433 C  C1  B 84Z D  3 .   ? 28.438 -1.206  -3.844  0.50 10.96  ? 302 84Z A C1  1 
HETATM 4434 CL CL1 A 84Z D  3 .   ? 30.740 -0.029  -0.895  0.50 12.96  ? 302 84Z A CL1 1 
HETATM 4435 CL CL1 B 84Z D  3 .   ? 27.882 -2.845  -3.826  0.50 10.16  ? 302 84Z A CL1 1 
HETATM 4436 S  S7  A 84Z D  3 .   ? 27.645 -0.956  -1.216  0.50 11.28  ? 302 84Z A S7  1 
HETATM 4437 S  S7  B 84Z D  3 .   ? 27.685 -0.952  -1.215  0.50 5.90   ? 302 84Z A S7  1 
HETATM 4438 O  O8  A 84Z D  3 .   ? 27.463 0.207   -0.410  0.50 13.38  ? 302 84Z A O8  1 
HETATM 4439 O  O8  B 84Z D  3 .   ? 27.518 0.230   -0.426  0.50 5.73   ? 302 84Z A O8  1 
HETATM 4440 O  O9  A 84Z D  3 .   ? 28.454 -2.018  -0.667  0.50 12.04  ? 302 84Z A O9  1 
HETATM 4441 O  O9  B 84Z D  3 .   ? 28.530 -2.003  -0.716  0.50 6.71   ? 302 84Z A O9  1 
HETATM 4442 N  N10 A 84Z D  3 .   ? 26.225 -1.480  -1.683  0.50 13.14  ? 302 84Z A N10 1 
HETATM 4443 N  N10 B 84Z D  3 .   ? 26.292 -1.499  -1.587  0.50 6.61   ? 302 84Z A N10 1 
HETATM 4444 C  C1  . EDO E  4 .   ? 15.012 -9.773  -9.222  1.00 35.34  ? 303 EDO A C1  1 
HETATM 4445 O  O1  . EDO E  4 .   ? 15.581 -9.950  -10.524 1.00 35.69  ? 303 EDO A O1  1 
HETATM 4446 C  C2  . EDO E  4 .   ? 14.795 -8.287  -8.960  1.00 28.43  ? 303 EDO A C2  1 
HETATM 4447 O  O2  . EDO E  4 .   ? 13.675 -7.826  -9.724  1.00 21.47  ? 303 EDO A O2  1 
HETATM 4448 C  C1  . EDO F  4 .   ? 28.109 26.248  -6.772  1.00 32.49  ? 304 EDO A C1  1 
HETATM 4449 O  O1  . EDO F  4 .   ? 29.312 25.785  -6.148  1.00 33.69  ? 304 EDO A O1  1 
HETATM 4450 C  C2  . EDO F  4 .   ? 27.015 26.395  -5.721  1.00 27.71  ? 304 EDO A C2  1 
HETATM 4451 O  O2  . EDO F  4 .   ? 25.743 26.513  -6.368  1.00 55.06  ? 304 EDO A O2  1 
HETATM 4452 C  C1  . EDO G  4 .   ? 20.026 -13.117 5.020   1.00 22.80  ? 305 EDO A C1  1 
HETATM 4453 O  O1  . EDO G  4 .   ? 19.674 -11.836 5.554   1.00 19.41  ? 305 EDO A O1  1 
HETATM 4454 C  C2  . EDO G  4 .   ? 18.770 -13.968 4.872   1.00 33.16  ? 305 EDO A C2  1 
HETATM 4455 O  O2  . EDO G  4 .   ? 18.242 -13.813 3.550   1.00 28.71  ? 305 EDO A O2  1 
HETATM 4456 C  C   . ACT H  5 .   ? 11.381 -3.657  12.212  1.00 31.91  ? 306 ACT A C   1 
HETATM 4457 O  O   . ACT H  5 .   ? 11.686 -4.782  11.760  1.00 40.50  ? 306 ACT A O   1 
HETATM 4458 O  OXT . ACT H  5 .   ? 11.699 -3.298  13.367  1.00 33.49  ? 306 ACT A OXT 1 
HETATM 4459 C  CH3 . ACT H  5 .   ? 10.608 -2.709  11.344  1.00 23.46  ? 306 ACT A CH3 1 
HETATM 4460 C  C   . ACT I  5 .   ? 17.314 0.454   14.720  1.00 27.07  ? 307 ACT A C   1 
HETATM 4461 O  O   . ACT I  5 .   ? 16.455 -0.439  14.888  1.00 31.37  ? 307 ACT A O   1 
HETATM 4462 O  OXT . ACT I  5 .   ? 17.385 1.454   15.466  1.00 35.88  ? 307 ACT A OXT 1 
HETATM 4463 C  CH3 . ACT I  5 .   ? 18.291 0.319   13.589  1.00 28.73  ? 307 ACT A CH3 1 
HETATM 4464 C  C1  . PEG J  6 .   ? 39.208 11.976  -8.144  1.00 35.00  ? 308 PEG A C1  1 
HETATM 4465 O  O1  . PEG J  6 .   ? 40.135 11.174  -8.885  1.00 26.38  ? 308 PEG A O1  1 
HETATM 4466 C  C2  . PEG J  6 .   ? 39.919 13.216  -7.615  1.00 31.98  ? 308 PEG A C2  1 
HETATM 4467 O  O2  . PEG J  6 .   ? 41.049 12.821  -6.840  1.00 56.87  ? 308 PEG A O2  1 
HETATM 4468 C  C3  . PEG J  6 .   ? 41.385 13.799  -5.857  1.00 37.88  ? 308 PEG A C3  1 
HETATM 4469 C  C4  . PEG J  6 .   ? 42.802 13.548  -5.355  1.00 48.92  ? 308 PEG A C4  1 
HETATM 4470 O  O4  . PEG J  6 .   ? 42.770 12.577  -4.303  1.00 30.53  ? 308 PEG A O4  1 
HETATM 4471 O  O2  . PEG K  6 .   ? 17.724 -0.570  -26.820 1.00 93.88  ? 309 PEG A O2  1 
HETATM 4472 C  C3  . PEG K  6 .   ? 18.625 0.254   -26.083 1.00 98.48  ? 309 PEG A C3  1 
HETATM 4473 C  C4  . PEG K  6 .   ? 20.028 -0.338  -26.154 1.00 86.71  ? 309 PEG A C4  1 
HETATM 4474 O  O4  . PEG K  6 .   ? 20.312 -1.038  -24.938 1.00 47.61  ? 309 PEG A O4  1 
HETATM 4475 C  C1  . PEG L  6 .   ? 15.838 17.019  10.135  1.00 20.00  ? 310 PEG A C1  1 
HETATM 4476 O  O1  . PEG L  6 .   ? 15.165 17.160  8.879   1.00 20.00  ? 310 PEG A O1  1 
HETATM 4477 C  C2  . PEG L  6 .   ? 16.838 18.156  10.306  1.00 20.00  ? 310 PEG A C2  1 
HETATM 4478 O  O2  . PEG L  6 .   ? 17.715 18.190  9.181   1.00 20.00  ? 310 PEG A O2  1 
HETATM 4479 C  C3  . PEG L  6 .   ? 18.094 16.879  8.766   1.00 20.00  ? 310 PEG A C3  1 
HETATM 4480 C  C4  . PEG L  6 .   ? 19.420 16.504  9.416   1.00 20.00  ? 310 PEG A C4  1 
HETATM 4481 O  O4  . PEG L  6 .   ? 19.634 15.094  9.284   1.00 20.00  ? 310 PEG A O4  1 
HETATM 4482 C  C1  . EDO M  4 .   ? 40.186 -10.202 1.104   1.00 28.02  ? 311 EDO A C1  1 
HETATM 4483 O  O1  . EDO M  4 .   ? 40.094 -9.608  -0.195  1.00 25.76  ? 311 EDO A O1  1 
HETATM 4484 C  C2  . EDO M  4 .   ? 40.390 -9.111  2.149   1.00 21.74  ? 311 EDO A C2  1 
HETATM 4485 O  O2  . EDO M  4 .   ? 39.796 -9.517  3.386   1.00 27.58  ? 311 EDO A O2  1 
HETATM 4486 C  C1  . EDO N  4 .   ? 12.595 16.025  0.458   1.00 18.17  ? 312 EDO A C1  1 
HETATM 4487 O  O1  . EDO N  4 .   ? 12.496 17.169  1.314   1.00 37.39  ? 312 EDO A O1  1 
HETATM 4488 C  C2  . EDO N  4 .   ? 14.043 15.843  0.018   1.00 20.05  ? 312 EDO A C2  1 
HETATM 4489 O  O2  . EDO N  4 .   ? 14.915 16.130  1.117   1.00 30.09  ? 312 EDO A O2  1 
HETATM 4490 C  C1  . EDO O  4 .   ? 25.013 -2.807  21.741  1.00 23.80  ? 313 EDO A C1  1 
HETATM 4491 O  O1  . EDO O  4 .   ? 25.562 -3.266  20.500  1.00 17.13  ? 313 EDO A O1  1 
HETATM 4492 C  C2  . EDO O  4 .   ? 25.654 -1.477  22.118  1.00 25.37  ? 313 EDO A C2  1 
HETATM 4493 O  O2  . EDO O  4 .   ? 25.312 -0.487  21.140  1.00 21.38  ? 313 EDO A O2  1 
HETATM 4494 C  C1  . EDO P  4 .   ? 7.391  1.873   12.666  1.00 26.67  ? 314 EDO A C1  1 
HETATM 4495 O  O1  . EDO P  4 .   ? 7.793  3.185   13.075  1.00 30.00  ? 314 EDO A O1  1 
HETATM 4496 C  C2  . EDO P  4 .   ? 6.027  1.948   11.990  1.00 23.83  ? 314 EDO A C2  1 
HETATM 4497 O  O2  . EDO P  4 .   ? 5.501  0.626   11.828  1.00 29.50  ? 314 EDO A O2  1 
HETATM 4498 C  C1  . EDO Q  4 .   ? 21.727 0.098   -20.205 1.00 24.58  ? 315 EDO A C1  1 
HETATM 4499 O  O1  . EDO Q  4 .   ? 22.047 -1.193  -20.736 1.00 27.96  ? 315 EDO A O1  1 
HETATM 4500 C  C2  . EDO Q  4 .   ? 21.778 1.134   -21.322 1.00 27.12  ? 315 EDO A C2  1 
HETATM 4501 O  O2  . EDO Q  4 .   ? 20.583 1.923   -21.297 1.00 23.47  ? 315 EDO A O2  1 
HETATM 4502 ZN ZN  . ZN  R  2 .   ? 48.393 -1.372  -19.299 1.00 8.42   ? 301 ZN  B ZN  1 
HETATM 4503 O  O18 A 84Z S  3 .   ? 42.903 2.455   -14.329 0.50 22.57  ? 302 84Z B O18 1 
HETATM 4504 O  O18 B 84Z S  3 .   ? 40.650 1.434   -14.756 0.50 21.41  ? 302 84Z B O18 1 
HETATM 4505 S  S16 A 84Z S  3 .   ? 41.997 1.390   -14.908 0.50 17.22  ? 302 84Z B S16 1 
HETATM 4506 S  S16 B 84Z S  3 .   ? 41.689 0.437   -14.176 0.50 15.02  ? 302 84Z B S16 1 
HETATM 4507 O  O17 A 84Z S  3 .   ? 40.916 2.096   -15.695 0.50 21.45  ? 302 84Z B O17 1 
HETATM 4508 O  O17 B 84Z S  3 .   ? 41.095 -0.737  -13.672 0.50 20.54  ? 302 84Z B O17 1 
HETATM 4509 C  C19 A 84Z S  3 .   ? 41.271 0.361   -13.769 0.50 18.38  ? 302 84Z B C19 1 
HETATM 4510 C  C19 B 84Z S  3 .   ? 42.601 1.164   -12.875 0.50 15.06  ? 302 84Z B C19 1 
HETATM 4511 C  C24 A 84Z S  3 .   ? 41.666 0.339   -12.435 0.50 21.34  ? 302 84Z B C24 1 
HETATM 4512 C  C24 B 84Z S  3 .   ? 42.964 2.526   -13.028 0.50 14.41  ? 302 84Z B C24 1 
HETATM 4513 C  C23 A 84Z S  3 .   ? 40.982 -0.494  -11.552 0.50 25.50  ? 302 84Z B C23 1 
HETATM 4514 C  C23 B 84Z S  3 .   ? 43.711 3.099   -11.971 0.50 19.15  ? 302 84Z B C23 1 
HETATM 4515 C  C22 A 84Z S  3 .   ? 39.905 -1.244  -11.996 0.50 19.15  ? 302 84Z B C22 1 
HETATM 4516 C  C22 B 84Z S  3 .   ? 44.041 2.322   -10.822 0.50 20.78  ? 302 84Z B C22 1 
HETATM 4517 C  C21 A 84Z S  3 .   ? 39.474 -1.177  -13.309 0.50 18.63  ? 302 84Z B C21 1 
HETATM 4518 C  C21 B 84Z S  3 .   ? 43.719 0.935   -10.811 0.50 18.96  ? 302 84Z B C21 1 
HETATM 4519 C  C20 A 84Z S  3 .   ? 40.166 -0.353  -14.189 0.50 18.70  ? 302 84Z B C20 1 
HETATM 4520 C  C20 B 84Z S  3 .   ? 42.976 0.343   -11.820 0.50 19.28  ? 302 84Z B C20 1 
HETATM 4521 C  C3  A 84Z S  3 .   ? 43.020 0.515   -16.056 0.50 16.27  ? 302 84Z B C3  1 
HETATM 4522 C  C3  B 84Z S  3 .   ? 42.864 -0.106  -15.509 0.50 11.17  ? 302 84Z B C3  1 
HETATM 4523 C  C2  A 84Z S  3 .   ? 42.430 0.278   -17.241 0.50 14.63  ? 302 84Z B C2  1 
HETATM 4524 C  C2  B 84Z S  3 .   ? 43.541 -1.333  -15.436 0.50 10.98  ? 302 84Z B C2  1 
HETATM 4525 C  C4  A 84Z S  3 .   ? 44.312 0.069   -15.749 0.50 14.87  ? 302 84Z B C4  1 
HETATM 4526 C  C4  B 84Z S  3 .   ? 43.123 0.745   -16.682 0.50 11.87  ? 302 84Z B C4  1 
HETATM 4527 C  C12 A 84Z S  3 .   ? 45.009 0.317   -14.501 0.50 18.40  ? 302 84Z B C12 1 
HETATM 4528 C  C12 B 84Z S  3 .   ? 42.523 2.063   -16.830 0.50 11.73  ? 302 84Z B C12 1 
HETATM 4529 O  O14 A 84Z S  3 .   ? 44.446 -0.110  -13.348 0.50 14.39  ? 302 84Z B O14 1 
HETATM 4530 O  O14 B 84Z S  3 .   ? 41.572 2.151   -17.752 0.50 14.73  ? 302 84Z B O14 1 
HETATM 4531 C  C15 A 84Z S  3 .   ? 44.486 0.639   -12.210 0.50 29.15  ? 302 84Z B C15 1 
HETATM 4532 C  C15 B 84Z S  3 .   ? 40.907 3.401   -17.858 0.50 15.14  ? 302 84Z B C15 1 
HETATM 4533 O  O13 A 84Z S  3 .   ? 46.029 0.898   -14.575 0.50 23.45  ? 302 84Z B O13 1 
HETATM 4534 O  O13 B 84Z S  3 .   ? 42.881 3.032   -16.255 0.50 17.44  ? 302 84Z B O13 1 
HETATM 4535 C  C5  A 84Z S  3 .   ? 45.052 -0.611  -16.677 0.50 14.51  ? 302 84Z B C5  1 
HETATM 4536 C  C5  B 84Z S  3 .   ? 43.910 0.195   -17.734 0.50 9.80   ? 302 84Z B C5  1 
HETATM 4537 C  C6  A 84Z S  3 .   ? 44.445 -0.869  -17.859 0.50 12.16  ? 302 84Z B C6  1 
HETATM 4538 C  C6  B 84Z S  3 .   ? 44.515 -1.061  -17.679 0.50 8.37   ? 302 84Z B C6  1 
HETATM 4539 C  C1  A 84Z S  3 .   ? 43.158 -0.414  -18.166 0.50 12.09  ? 302 84Z B C1  1 
HETATM 4540 C  C1  B 84Z S  3 .   ? 44.305 -1.823  -16.523 0.50 8.77   ? 302 84Z B C1  1 
HETATM 4541 CL CL1 A 84Z S  3 .   ? 42.388 -0.747  -19.721 0.50 15.39  ? 302 84Z B CL1 1 
HETATM 4542 CL CL1 B 84Z S  3 .   ? 44.952 -3.389  -16.340 0.50 9.50   ? 302 84Z B CL1 1 
HETATM 4543 S  S7  A 84Z S  3 .   ? 45.362 -1.703  -19.134 0.50 9.55   ? 302 84Z B S7  1 
HETATM 4544 S  S7  B 84Z S  3 .   ? 45.389 -1.698  -19.146 0.50 9.52   ? 302 84Z B S7  1 
HETATM 4545 O  O8  A 84Z S  3 .   ? 45.559 -0.601  -20.107 0.50 9.91   ? 302 84Z B O8  1 
HETATM 4546 O  O8  B 84Z S  3 .   ? 45.518 -0.585  -20.043 0.50 10.57  ? 302 84Z B O8  1 
HETATM 4547 O  O9  A 84Z S  3 .   ? 44.504 -2.844  -19.669 0.50 10.65  ? 302 84Z B O9  1 
HETATM 4548 O  O9  B 84Z S  3 .   ? 44.559 -2.785  -19.600 0.50 9.99   ? 302 84Z B O9  1 
HETATM 4549 N  N10 A 84Z S  3 .   ? 46.893 -2.312  -18.642 0.50 9.95   ? 302 84Z B N10 1 
HETATM 4550 N  N10 B 84Z S  3 .   ? 46.847 -2.240  -18.723 0.50 10.57  ? 302 84Z B N10 1 
HETATM 4551 C  C1  . PEG T  6 .   ? 56.857 12.075  -3.716  1.00 24.49  ? 303 PEG B C1  1 
HETATM 4552 O  O1  . PEG T  6 .   ? 57.687 13.239  -3.638  1.00 24.55  ? 303 PEG B O1  1 
HETATM 4553 C  C2  . PEG T  6 .   ? 55.578 12.310  -2.921  1.00 30.64  ? 303 PEG B C2  1 
HETATM 4554 O  O2  . PEG T  6 .   ? 55.046 11.057  -2.497  1.00 30.56  ? 303 PEG B O2  1 
HETATM 4555 C  C3  . PEG T  6 .   ? 54.329 11.174  -1.269  1.00 45.04  ? 303 PEG B C3  1 
HETATM 4556 C  C4  . PEG T  6 .   ? 53.002 10.434  -1.385  1.00 27.42  ? 303 PEG B C4  1 
HETATM 4557 O  O4  . PEG T  6 .   ? 52.358 10.407  -0.106  1.00 97.93  ? 303 PEG B O4  1 
HETATM 4558 C  C1  . EDO U  4 .   ? 53.906 22.956  -10.831 1.00 20.34  ? 304 EDO B C1  1 
HETATM 4559 O  O1  . EDO U  4 .   ? 53.661 23.080  -12.236 1.00 19.88  ? 304 EDO B O1  1 
HETATM 4560 C  C2  . EDO U  4 .   ? 54.175 21.495  -10.490 1.00 33.55  ? 304 EDO B C2  1 
HETATM 4561 O  O2  . EDO U  4 .   ? 53.141 20.677  -11.050 1.00 22.75  ? 304 EDO B O2  1 
HETATM 4562 C  C   . ACT V  5 .   ? 36.736 -1.671  -10.227 1.00 26.48  ? 305 ACT B C   1 
HETATM 4563 O  O   . ACT V  5 .   ? 36.744 -0.423  -10.306 1.00 34.46  ? 305 ACT B O   1 
HETATM 4564 O  OXT . ACT V  5 .   ? 37.783 -2.329  -10.046 1.00 23.41  ? 305 ACT B OXT 1 
HETATM 4565 C  CH3 . ACT V  5 .   ? 35.433 -2.400  -10.364 1.00 17.90  ? 305 ACT B CH3 1 
HETATM 4566 C  C1  . PEG W  6 .   ? 62.357 12.950  -30.166 1.00 76.16  ? 306 PEG B C1  1 
HETATM 4567 O  O1  . PEG W  6 .   ? 61.683 11.870  -30.821 1.00 73.52  ? 306 PEG B O1  1 
HETATM 4568 C  C2  . PEG W  6 .   ? 61.786 14.276  -30.654 1.00 90.36  ? 306 PEG B C2  1 
HETATM 4569 O  O2  . PEG W  6 .   ? 62.375 15.347  -29.919 1.00 74.02  ? 306 PEG B O2  1 
HETATM 4570 C  C3  . PEG W  6 .   ? 61.482 15.871  -28.939 1.00 63.23  ? 306 PEG B C3  1 
HETATM 4571 C  C4  . PEG W  6 .   ? 62.247 16.148  -27.650 1.00 52.99  ? 306 PEG B C4  1 
HETATM 4572 O  O4  . PEG W  6 .   ? 61.342 16.114  -26.541 1.00 54.36  ? 306 PEG B O4  1 
HETATM 4573 C  C1  . PEG X  6 .   ? 58.302 -8.185  -10.767 1.00 25.40  ? 307 PEG B C1  1 
HETATM 4574 O  O1  . PEG X  6 .   ? 59.312 -7.800  -9.828  1.00 20.96  ? 307 PEG B O1  1 
HETATM 4575 C  C2  . PEG X  6 .   ? 57.445 -9.293  -10.166 1.00 34.71  ? 307 PEG B C2  1 
HETATM 4576 O  O2  . PEG X  6 .   ? 58.276 -10.197 -9.442  1.00 48.90  ? 307 PEG B O2  1 
HETATM 4577 C  C3  . PEG X  6 .   ? 59.198 -10.870 -10.298 1.00 66.46  ? 307 PEG B C3  1 
HETATM 4578 C  C4  . PEG X  6 .   ? 59.043 -12.376 -10.128 1.00 47.76  ? 307 PEG B C4  1 
HETATM 4579 O  O4  . PEG X  6 .   ? 59.623 -13.046 -11.253 1.00 43.16  ? 307 PEG B O4  1 
HETATM 4580 C  C1  . PEG Y  6 .   ? 48.946 4.078   -2.019  1.00 34.38  ? 308 PEG B C1  1 
HETATM 4581 O  O1  . PEG Y  6 .   ? 48.932 5.096   -1.012  1.00 20.58  ? 308 PEG B O1  1 
HETATM 4582 C  C2  . PEG Y  6 .   ? 49.301 2.739   -1.384  1.00 29.11  ? 308 PEG B C2  1 
HETATM 4583 O  O2  . PEG Y  6 .   ? 50.044 1.954   -2.314  1.00 53.07  ? 308 PEG B O2  1 
HETATM 4584 C  C3  . PEG Y  6 .   ? 49.218 1.453   -3.363  1.00 42.98  ? 308 PEG B C3  1 
HETATM 4585 C  C4  . PEG Y  6 .   ? 49.028 2.534   -4.421  1.00 23.25  ? 308 PEG B C4  1 
HETATM 4586 O  O4  . PEG Y  6 .   ? 47.763 2.353   -5.066  1.00 22.33  ? 308 PEG B O4  1 
HETATM 4587 C  C1  . PEG Z  6 .   ? 66.600 5.300   -8.554  1.00 20.00  ? 309 PEG B C1  1 
HETATM 4588 O  O1  . PEG Z  6 .   ? 67.923 5.078   -9.053  1.00 20.00  ? 309 PEG B O1  1 
HETATM 4589 C  C2  . PEG Z  6 .   ? 66.039 6.583   -9.154  1.00 20.00  ? 309 PEG B C2  1 
HETATM 4590 O  O2  . PEG Z  6 .   ? 66.638 7.708   -8.515  1.00 20.00  ? 309 PEG B O2  1 
HETATM 4591 C  C3  . PEG Z  6 .   ? 65.682 8.476   -7.787  1.00 20.00  ? 309 PEG B C3  1 
HETATM 4592 C  C4  . PEG Z  6 .   ? 66.029 8.445   -6.303  1.00 20.00  ? 309 PEG B C4  1 
HETATM 4593 O  O4  . PEG Z  6 .   ? 64.908 8.908   -5.541  1.00 20.00  ? 309 PEG B O4  1 
HETATM 4594 C  C1  . PEG AA 6 .   ? 67.636 -6.842  -9.940  1.00 20.00  ? 310 PEG B C1  1 
HETATM 4595 O  O1  . PEG AA 6 .   ? 68.803 -6.023  -9.807  1.00 20.00  ? 310 PEG B O1  1 
HETATM 4596 C  C2  . PEG AA 6 .   ? 66.406 -5.954  -10.090 1.00 20.00  ? 310 PEG B C2  1 
HETATM 4597 O  O2  . PEG AA 6 .   ? 66.553 -5.131  -11.245 1.00 20.00  ? 310 PEG B O2  1 
HETATM 4598 C  C3  . PEG AA 6 .   ? 65.388 -4.344  -11.484 1.00 20.00  ? 310 PEG B C3  1 
HETATM 4599 C  C4  . PEG AA 6 .   ? 65.800 -2.933  -11.885 1.00 20.00  ? 310 PEG B C4  1 
HETATM 4600 O  O4  . PEG AA 6 .   ? 66.840 -2.474  -11.014 1.00 20.00  ? 310 PEG B O4  1 
HETATM 4601 C  C1  . EDO BA 4 .   ? 60.077 -6.432  3.765   1.00 39.76  ? 311 EDO B C1  1 
HETATM 4602 O  O1  . EDO BA 4 .   ? 58.650 -6.448  3.883   1.00 52.86  ? 311 EDO B O1  1 
HETATM 4603 C  C2  . EDO BA 4 .   ? 60.650 -5.352  4.676   1.00 25.57  ? 311 EDO B C2  1 
HETATM 4604 O  O2  . EDO BA 4 .   ? 62.080 -5.407  4.640   1.00 29.67  ? 311 EDO B O2  1 
HETATM 4605 C  C1  . EDO CA 4 .   ? 54.982 -14.662 -13.134 1.00 42.92  ? 312 EDO B C1  1 
HETATM 4606 O  O1  . EDO CA 4 .   ? 54.323 -15.690 -13.882 1.00 40.27  ? 312 EDO B O1  1 
HETATM 4607 C  C2  . EDO CA 4 .   ? 56.306 -15.193 -12.597 1.00 49.07  ? 312 EDO B C2  1 
HETATM 4608 O  O2  . EDO CA 4 .   ? 57.174 -14.095 -12.296 1.00 51.76  ? 312 EDO B O2  1 
HETATM 4609 C  C1  . EDO DA 4 .   ? 24.148 2.425   -16.264 1.00 25.73  ? 313 EDO B C1  1 
HETATM 4610 O  O1  . EDO DA 4 .   ? 25.436 2.008   -15.796 1.00 21.23  ? 313 EDO B O1  1 
HETATM 4611 C  C2  . EDO DA 4 .   ? 23.241 1.209   -16.406 1.00 31.31  ? 313 EDO B C2  1 
HETATM 4612 O  O2  . EDO DA 4 .   ? 23.763 0.339   -17.417 1.00 36.85  ? 313 EDO B O2  1 
HETATM 4613 C  C1  . EDO EA 4 .   ? 34.683 20.193  -22.990 1.00 37.13  ? 314 EDO B C1  1 
HETATM 4614 O  O1  . EDO EA 4 .   ? 35.973 20.810  -23.065 1.00 37.41  ? 314 EDO B O1  1 
HETATM 4615 C  C2  . EDO EA 4 .   ? 34.409 19.762  -21.554 1.00 29.42  ? 314 EDO B C2  1 
HETATM 4616 O  O2  . EDO EA 4 .   ? 33.229 18.951  -21.516 1.00 30.10  ? 314 EDO B O2  1 
HETATM 4617 C  C1  . EDO FA 4 .   ? 60.052 4.271   -34.859 1.00 20.22  ? 315 EDO B C1  1 
HETATM 4618 O  O1  . EDO FA 4 .   ? 58.862 3.893   -35.561 1.00 20.98  ? 315 EDO B O1  1 
HETATM 4619 C  C2  . EDO FA 4 .   ? 61.245 3.522   -35.440 1.00 26.28  ? 315 EDO B C2  1 
HETATM 4620 O  O2  . EDO FA 4 .   ? 62.416 4.340   -35.344 1.00 25.85  ? 315 EDO B O2  1 
HETATM 4621 C  C1  . EDO GA 4 .   ? 60.385 6.618   -31.986 1.00 20.00  ? 316 EDO B C1  1 
HETATM 4622 O  O1  . EDO GA 4 .   ? 60.700 7.438   -30.855 1.00 20.00  ? 316 EDO B O1  1 
HETATM 4623 C  C2  . EDO GA 4 .   ? 60.086 7.505   -33.189 1.00 20.00  ? 316 EDO B C2  1 
HETATM 4624 O  O2  . EDO GA 4 .   ? 58.758 8.028   -33.078 1.00 20.00  ? 316 EDO B O2  1 
HETATM 4625 C  C1  . EDO HA 4 .   ? 53.999 15.606  -3.804  1.00 20.00  ? 317 EDO B C1  1 
HETATM 4626 O  O1  . EDO HA 4 .   ? 55.205 14.836  -3.875  1.00 20.00  ? 317 EDO B O1  1 
HETATM 4627 C  C2  . EDO HA 4 .   ? 52.900 14.769  -3.161  1.00 20.00  ? 317 EDO B C2  1 
HETATM 4628 O  O2  . EDO HA 4 .   ? 51.639 15.427  -3.329  1.00 20.00  ? 317 EDO B O2  1 
HETATM 4629 O  O   . HOH IA 7 .   ? 16.290 15.548  2.646   1.00 19.48  ? 401 HOH A O   1 
HETATM 4630 O  O   . HOH IA 7 .   ? 15.124 -3.838  16.015  1.00 37.00  ? 402 HOH A O   1 
HETATM 4631 O  O   . HOH IA 7 .   ? 7.034  14.904  1.496   1.00 29.20  ? 403 HOH A O   1 
HETATM 4632 O  O   . HOH IA 7 .   ? 22.785 -12.598 20.948  1.00 39.32  ? 404 HOH A O   1 
HETATM 4633 O  O   . HOH IA 7 .   ? 18.384 13.955  10.893  1.00 19.43  ? 405 HOH A O   1 
HETATM 4634 O  O   . HOH IA 7 .   ? 18.457 -12.239 7.522   1.00 24.69  ? 406 HOH A O   1 
HETATM 4635 O  O   . HOH IA 7 .   ? 43.716 -0.391  -7.166  1.00 39.68  ? 407 HOH A O   1 
HETATM 4636 O  O   . HOH IA 7 .   ? 13.274 -2.057  15.325  1.00 43.14  ? 408 HOH A O   1 
HETATM 4637 O  O   . HOH IA 7 .   ? 32.815 -11.678 -14.637 1.00 30.58  ? 409 HOH A O   1 
HETATM 4638 O  O   . HOH IA 7 .   ? 37.719 9.112   -8.420  1.00 17.33  ? 410 HOH A O   1 
HETATM 4639 O  O   . HOH IA 7 .   ? 42.227 14.758  -1.319  1.00 154.83 ? 411 HOH A O   1 
HETATM 4640 O  O   . HOH IA 7 .   ? 26.674 5.297   -10.058 1.00 38.77  ? 412 HOH A O   1 
HETATM 4641 O  O   . HOH IA 7 .   ? 32.444 -8.049  -13.426 1.00 40.14  ? 413 HOH A O   1 
HETATM 4642 O  O   . HOH IA 7 .   ? 17.824 10.562  18.599  1.00 36.32  ? 414 HOH A O   1 
HETATM 4643 O  O   . HOH IA 7 .   ? 28.050 6.845   20.260  1.00 15.89  ? 415 HOH A O   1 
HETATM 4644 O  O   . HOH IA 7 .   ? 14.656 1.305   14.994  1.00 32.39  ? 416 HOH A O   1 
HETATM 4645 O  O   . HOH IA 7 .   ? 22.534 14.170  -15.992 1.00 27.20  ? 417 HOH A O   1 
HETATM 4646 O  O   . HOH IA 7 .   ? 14.774 14.073  14.949  1.00 39.01  ? 418 HOH A O   1 
HETATM 4647 O  O   . HOH IA 7 .   ? 17.202 -4.464  -25.643 1.00 40.54  ? 419 HOH A O   1 
HETATM 4648 O  O   . HOH IA 7 .   ? 24.343 24.485  -5.850  1.00 37.54  ? 420 HOH A O   1 
HETATM 4649 O  O   . HOH IA 7 .   ? 28.806 -0.927  24.080  1.00 22.84  ? 421 HOH A O   1 
HETATM 4650 O  O   . HOH IA 7 .   ? 44.615 3.713   6.162   1.00 36.26  ? 422 HOH A O   1 
HETATM 4651 O  O   . HOH IA 7 .   ? 13.078 5.029   -27.212 1.00 33.41  ? 423 HOH A O   1 
HETATM 4652 O  O   . HOH IA 7 .   ? 38.684 -10.608 9.216   1.00 38.65  ? 424 HOH A O   1 
HETATM 4653 O  O   . HOH IA 7 .   ? 12.870 8.546   -25.514 1.00 39.01  ? 425 HOH A O   1 
HETATM 4654 O  O   . HOH IA 7 .   ? 31.696 14.848  -3.116  1.00 11.96  ? 426 HOH A O   1 
HETATM 4655 O  O   . HOH IA 7 .   ? 16.812 14.872  -10.327 1.00 15.81  ? 427 HOH A O   1 
HETATM 4656 O  O   . HOH IA 7 .   ? 6.059  -5.111  7.533   1.00 40.42  ? 428 HOH A O   1 
HETATM 4657 O  O   . HOH IA 7 .   ? 28.363 -17.813 -1.776  1.00 35.78  ? 429 HOH A O   1 
HETATM 4658 O  O   . HOH IA 7 .   ? 28.460 -16.012 -10.691 1.00 22.88  ? 430 HOH A O   1 
HETATM 4659 O  O   . HOH IA 7 .   ? 23.475 -6.244  -2.716  1.00 10.50  ? 431 HOH A O   1 
HETATM 4660 O  O   . HOH IA 7 .   ? 38.634 8.858   14.368  1.00 18.84  ? 432 HOH A O   1 
HETATM 4661 O  O   . HOH IA 7 .   ? 9.270  3.866   11.022  1.00 23.27  ? 433 HOH A O   1 
HETATM 4662 O  O   . HOH IA 7 .   ? 16.579 14.481  12.855  1.00 21.10  ? 434 HOH A O   1 
HETATM 4663 O  O   . HOH IA 7 .   ? 27.471 -6.044  23.762  1.00 37.94  ? 435 HOH A O   1 
HETATM 4664 O  O   . HOH IA 7 .   ? 31.410 -12.657 -17.499 1.00 36.61  ? 436 HOH A O   1 
HETATM 4665 O  O   . HOH IA 7 .   ? 33.035 -12.723 15.876  1.00 27.35  ? 437 HOH A O   1 
HETATM 4666 O  O   . HOH IA 7 .   ? 36.175 -17.857 3.733   1.00 35.30  ? 438 HOH A O   1 
HETATM 4667 O  O   . HOH IA 7 .   ? 12.532 8.586   -21.748 1.00 24.99  ? 439 HOH A O   1 
HETATM 4668 O  O   . HOH IA 7 .   ? 20.249 -18.678 -6.971  1.00 32.42  ? 440 HOH A O   1 
HETATM 4669 O  O   . HOH IA 7 .   ? 37.781 -10.129 15.913  1.00 25.84  ? 441 HOH A O   1 
HETATM 4670 O  O   . HOH IA 7 .   ? 23.212 -11.917 -15.515 1.00 44.56  ? 442 HOH A O   1 
HETATM 4671 O  O   . HOH IA 7 .   ? 27.724 -19.909 -6.303  1.00 31.07  ? 443 HOH A O   1 
HETATM 4672 O  O   . HOH IA 7 .   ? 28.344 12.843  15.582  1.00 22.81  ? 444 HOH A O   1 
HETATM 4673 O  O   . HOH IA 7 .   ? 15.232 8.582   12.875  1.00 21.79  ? 445 HOH A O   1 
HETATM 4674 O  O   . HOH IA 7 .   ? 24.517 -15.523 -0.076  1.00 22.91  ? 446 HOH A O   1 
HETATM 4675 O  O   . HOH IA 7 .   ? 14.130 -15.367 -9.829  1.00 46.30  ? 447 HOH A O   1 
HETATM 4676 O  O   . HOH IA 7 .   ? 32.713 15.612  -13.763 1.00 45.49  ? 448 HOH A O   1 
HETATM 4677 O  O   . HOH IA 7 .   ? 6.187  -6.916  -17.243 1.00 25.01  ? 449 HOH A O   1 
HETATM 4678 O  O   . HOH IA 7 .   ? 37.663 -1.737  7.653   1.00 16.82  ? 450 HOH A O   1 
HETATM 4679 O  O   . HOH IA 7 .   ? 40.190 -1.126  -7.744  1.00 64.49  ? 451 HOH A O   1 
HETATM 4680 O  O   . HOH IA 7 .   ? 17.528 20.736  -4.114  1.00 30.60  ? 452 HOH A O   1 
HETATM 4681 O  O   . HOH IA 7 .   ? 11.842 -9.646  -10.425 1.00 49.44  ? 453 HOH A O   1 
HETATM 4682 O  O   . HOH IA 7 .   ? 18.215 -10.353 -13.522 1.00 41.91  ? 454 HOH A O   1 
HETATM 4683 O  O   . HOH IA 7 .   ? 29.675 18.781  10.246  1.00 44.46  ? 455 HOH A O   1 
HETATM 4684 O  O   . HOH IA 7 .   ? 10.951 14.011  -16.378 1.00 44.65  ? 456 HOH A O   1 
HETATM 4685 O  O   . HOH IA 7 .   ? 47.207 0.145   0.282   1.00 42.87  ? 457 HOH A O   1 
HETATM 4686 O  O   . HOH IA 7 .   ? 7.493  11.136  -5.586  1.00 18.38  ? 458 HOH A O   1 
HETATM 4687 O  O   . HOH IA 7 .   ? 30.169 -15.131 2.348   1.00 19.44  ? 459 HOH A O   1 
HETATM 4688 O  O   . HOH IA 7 .   ? 25.371 12.704  -18.000 1.00 36.92  ? 460 HOH A O   1 
HETATM 4689 O  O   . HOH IA 7 .   ? 26.592 7.963   23.402  1.00 40.16  ? 461 HOH A O   1 
HETATM 4690 O  O   . HOH IA 7 .   ? 10.712 -8.892  9.255   1.00 24.08  ? 462 HOH A O   1 
HETATM 4691 O  O   . HOH IA 7 .   ? 36.219 23.166  -5.225  1.00 20.21  ? 463 HOH A O   1 
HETATM 4692 O  O   . HOH IA 7 .   ? 26.317 -14.014 -11.234 1.00 25.47  ? 464 HOH A O   1 
HETATM 4693 O  O   . HOH IA 7 .   ? 41.034 11.084  -11.417 1.00 36.14  ? 465 HOH A O   1 
HETATM 4694 O  O   . HOH IA 7 .   ? 5.118  11.721  7.418   1.00 29.87  ? 466 HOH A O   1 
HETATM 4695 O  O   . HOH IA 7 .   ? 19.296 -0.548  15.763  1.00 31.33  ? 467 HOH A O   1 
HETATM 4696 O  O   . HOH IA 7 .   ? 31.610 -21.195 -5.980  1.00 35.23  ? 468 HOH A O   1 
HETATM 4697 O  O   . HOH IA 7 .   ? 24.343 -13.335 14.093  1.00 32.02  ? 469 HOH A O   1 
HETATM 4698 O  O   . HOH IA 7 .   ? 33.176 20.069  4.229   1.00 24.06  ? 470 HOH A O   1 
HETATM 4699 O  O   . HOH IA 7 .   ? 39.004 16.788  5.910   1.00 30.82  ? 471 HOH A O   1 
HETATM 4700 O  O   . HOH IA 7 .   ? 10.085 -10.579 -6.106  1.00 50.82  ? 472 HOH A O   1 
HETATM 4701 O  O   . HOH IA 7 .   ? 30.007 21.974  -7.564  1.00 82.90  ? 473 HOH A O   1 
HETATM 4702 O  O   . HOH IA 7 .   ? 18.302 -5.039  19.169  1.00 44.17  ? 474 HOH A O   1 
HETATM 4703 O  O   . HOH IA 7 .   ? 43.406 12.723  -8.147  1.00 23.17  ? 475 HOH A O   1 
HETATM 4704 O  O   . HOH IA 7 .   ? 15.412 13.339  -0.891  1.00 17.97  ? 476 HOH A O   1 
HETATM 4705 O  O   . HOH IA 7 .   ? 18.933 -14.224 -15.455 1.00 49.56  ? 477 HOH A O   1 
HETATM 4706 O  O   . HOH IA 7 .   ? 34.172 9.240   -10.333 1.00 23.74  ? 478 HOH A O   1 
HETATM 4707 O  O   . HOH IA 7 .   ? 25.978 -12.409 9.724   1.00 13.72  ? 479 HOH A O   1 
HETATM 4708 O  O   . HOH IA 7 .   ? 38.014 0.859   4.495   1.00 11.97  ? 480 HOH A O   1 
HETATM 4709 O  O   . HOH IA 7 .   ? 21.507 -0.822  -4.446  1.00 9.71   ? 481 HOH A O   1 
HETATM 4710 O  O   . HOH IA 7 .   ? 8.496  -0.935  -27.433 1.00 21.84  ? 482 HOH A O   1 
HETATM 4711 O  O   . HOH IA 7 .   ? 6.655  10.434  -2.935  1.00 17.40  ? 483 HOH A O   1 
HETATM 4712 O  O   . HOH IA 7 .   ? 10.713 17.270  -4.099  1.00 26.14  ? 484 HOH A O   1 
HETATM 4713 O  O   . HOH IA 7 .   ? 6.872  1.005   -13.054 1.00 14.48  ? 485 HOH A O   1 
HETATM 4714 O  O   . HOH IA 7 .   ? 38.645 -12.987 2.562   1.00 15.97  ? 486 HOH A O   1 
HETATM 4715 O  O   . HOH IA 7 .   ? 11.321 -3.872  1.054   1.00 10.58  ? 487 HOH A O   1 
HETATM 4716 O  O   . HOH IA 7 .   ? 36.136 -9.584  -6.883  1.00 33.60  ? 488 HOH A O   1 
HETATM 4717 O  O   . HOH IA 7 .   ? 20.457 -11.863 9.115   1.00 16.05  ? 489 HOH A O   1 
HETATM 4718 O  O   . HOH IA 7 .   ? 9.035  10.000  -9.361  1.00 14.99  ? 490 HOH A O   1 
HETATM 4719 O  O   . HOH IA 7 .   ? 17.665 -10.029 -3.217  1.00 19.97  ? 491 HOH A O   1 
HETATM 4720 O  O   . HOH IA 7 .   ? 22.451 6.255   14.942  1.00 10.66  ? 492 HOH A O   1 
HETATM 4721 O  O   . HOH IA 7 .   ? 24.653 -1.675  -14.058 1.00 27.66  ? 493 HOH A O   1 
HETATM 4722 O  O   . HOH IA 7 .   ? 34.600 13.385  15.661  1.00 24.73  ? 494 HOH A O   1 
HETATM 4723 O  O   . HOH IA 7 .   ? 37.165 20.624  -7.971  1.00 37.85  ? 495 HOH A O   1 
HETATM 4724 O  O   . HOH IA 7 .   ? 20.893 -12.408 15.971  1.00 20.13  ? 496 HOH A O   1 
HETATM 4725 O  O   . HOH IA 7 .   ? 30.081 -8.151  23.985  1.00 23.64  ? 497 HOH A O   1 
HETATM 4726 O  O   . HOH IA 7 .   ? 24.665 18.087  -12.463 1.00 33.97  ? 498 HOH A O   1 
HETATM 4727 O  O   . HOH IA 7 .   ? 44.749 11.562  6.535   1.00 39.28  ? 499 HOH A O   1 
HETATM 4728 O  O   . HOH IA 7 .   ? 12.409 -6.610  -20.859 1.00 19.76  ? 500 HOH A O   1 
HETATM 4729 O  O   . HOH IA 7 .   ? 23.980 24.000  -3.211  1.00 22.58  ? 501 HOH A O   1 
HETATM 4730 O  O   . HOH IA 7 .   ? 37.545 8.521   21.602  1.00 23.98  ? 502 HOH A O   1 
HETATM 4731 O  O   . HOH IA 7 .   ? 16.414 11.854  -17.562 1.00 20.96  ? 503 HOH A O   1 
HETATM 4732 O  O   . HOH IA 7 .   ? 29.266 -3.199  22.895  1.00 23.11  ? 504 HOH A O   1 
HETATM 4733 O  O   . HOH IA 7 .   ? 20.266 2.419   11.161  1.00 9.20   ? 505 HOH A O   1 
HETATM 4734 O  O   . HOH IA 7 .   ? 34.559 -12.111 23.766  1.00 44.31  ? 506 HOH A O   1 
HETATM 4735 O  O   . HOH IA 7 .   ? 16.941 17.133  -13.250 1.00 19.14  ? 507 HOH A O   1 
HETATM 4736 O  O   . HOH IA 7 .   ? 32.538 17.673  -12.748 1.00 40.74  ? 508 HOH A O   1 
HETATM 4737 O  O   . HOH IA 7 .   ? 2.943  6.932   2.009   1.00 14.99  ? 509 HOH A O   1 
HETATM 4738 O  O   . HOH IA 7 .   ? 16.706 -13.383 11.276  1.00 22.93  ? 510 HOH A O   1 
HETATM 4739 O  O   . HOH IA 7 .   ? 16.638 3.142   -20.804 1.00 11.72  ? 511 HOH A O   1 
HETATM 4740 O  O   . HOH IA 7 .   ? 7.367  12.514  -15.410 1.00 24.33  ? 512 HOH A O   1 
HETATM 4741 O  O   . HOH IA 7 .   ? 13.406 15.867  -7.342  1.00 16.13  ? 513 HOH A O   1 
HETATM 4742 O  O   . HOH IA 7 .   ? 15.389 -11.855 15.535  1.00 35.86  ? 514 HOH A O   1 
HETATM 4743 O  O   . HOH IA 7 .   ? 39.668 -6.696  3.770   1.00 28.82  ? 515 HOH A O   1 
HETATM 4744 O  O   . HOH IA 7 .   ? 24.594 20.587  -6.733  1.00 13.51  ? 516 HOH A O   1 
HETATM 4745 O  O   . HOH IA 7 .   ? 5.534  -1.634  0.091   1.00 19.40  ? 517 HOH A O   1 
HETATM 4746 O  O   . HOH IA 7 .   ? 16.538 1.821   -25.433 1.00 29.05  ? 518 HOH A O   1 
HETATM 4747 O  O   . HOH IA 7 .   ? 37.307 -12.663 9.119   1.00 17.66  ? 519 HOH A O   1 
HETATM 4748 O  O   . HOH IA 7 .   ? 25.968 10.505  19.732  1.00 34.88  ? 520 HOH A O   1 
HETATM 4749 O  O   . HOH IA 7 .   ? 26.827 -12.047 12.117  1.00 25.90  ? 521 HOH A O   1 
HETATM 4750 O  O   . HOH IA 7 .   ? 19.725 -15.792 -1.643  1.00 42.87  ? 522 HOH A O   1 
HETATM 4751 O  O   . HOH IA 7 .   ? 22.255 -9.841  21.027  1.00 21.55  ? 523 HOH A O   1 
HETATM 4752 O  O   . HOH IA 7 .   ? 20.009 -9.294  4.374   1.00 10.98  ? 524 HOH A O   1 
HETATM 4753 O  O   . HOH IA 7 .   ? 23.447 -6.299  -11.997 1.00 29.51  ? 525 HOH A O   1 
HETATM 4754 O  O   . HOH IA 7 .   ? 3.722  2.608   5.663   1.00 11.60  ? 526 HOH A O   1 
HETATM 4755 O  O   . HOH IA 7 .   ? 32.777 22.231  1.227   1.00 11.56  ? 527 HOH A O   1 
HETATM 4756 O  O   . HOH IA 7 .   ? 15.838 -9.947  18.191  1.00 29.97  ? 528 HOH A O   1 
HETATM 4757 O  O   . HOH IA 7 .   ? 11.476 -9.396  1.146   1.00 22.18  ? 529 HOH A O   1 
HETATM 4758 O  O   . HOH IA 7 .   ? 7.857  -1.331  11.214  1.00 22.76  ? 530 HOH A O   1 
HETATM 4759 O  O   . HOH IA 7 .   ? 27.860 25.242  -1.323  1.00 17.34  ? 531 HOH A O   1 
HETATM 4760 O  O   . HOH IA 7 .   ? 24.176 8.357   22.647  1.00 37.76  ? 532 HOH A O   1 
HETATM 4761 O  O   . HOH IA 7 .   ? 34.057 17.430  -5.608  1.00 18.09  ? 533 HOH A O   1 
HETATM 4762 O  O   . HOH IA 7 .   ? 15.929 4.038   15.980  1.00 18.87  ? 534 HOH A O   1 
HETATM 4763 O  O   . HOH IA 7 .   ? 38.681 -3.294  5.719   1.00 13.49  ? 535 HOH A O   1 
HETATM 4764 O  O   . HOH IA 7 .   ? 10.337 -7.842  -11.721 1.00 19.56  ? 536 HOH A O   1 
HETATM 4765 O  O   . HOH IA 7 .   ? 30.130 10.294  -8.039  1.00 14.58  ? 537 HOH A O   1 
HETATM 4766 O  O   . HOH IA 7 .   ? 40.630 -11.309 6.772   1.00 48.76  ? 538 HOH A O   1 
HETATM 4767 O  O   . HOH IA 7 .   ? 8.507  9.982   9.179   1.00 26.83  ? 539 HOH A O   1 
HETATM 4768 O  O   . HOH IA 7 .   ? 21.143 23.463  -9.492  1.00 42.32  ? 540 HOH A O   1 
HETATM 4769 O  O   . HOH IA 7 .   ? 5.796  -5.321  -5.667  1.00 25.16  ? 541 HOH A O   1 
HETATM 4770 O  O   . HOH IA 7 .   ? 40.513 12.937  2.220   1.00 24.90  ? 542 HOH A O   1 
HETATM 4771 O  O   . HOH IA 7 .   ? 26.058 -15.219 -14.743 1.00 46.51  ? 543 HOH A O   1 
HETATM 4772 O  O   . HOH IA 7 .   ? 8.188  8.468   -15.806 1.00 17.39  ? 544 HOH A O   1 
HETATM 4773 O  O   . HOH IA 7 .   ? 9.944  4.926   -9.623  1.00 18.26  ? 545 HOH A O   1 
HETATM 4774 O  O   . HOH IA 7 .   ? 19.151 -4.629  -15.584 1.00 30.83  ? 546 HOH A O   1 
HETATM 4775 O  O   . HOH IA 7 .   ? 41.775 11.631  15.892  1.00 46.49  ? 547 HOH A O   1 
HETATM 4776 O  O   . HOH IA 7 .   ? 41.097 18.686  -6.197  1.00 32.88  ? 548 HOH A O   1 
HETATM 4777 O  O   . HOH IA 7 .   ? 33.681 16.597  -2.310  1.00 11.46  ? 549 HOH A O   1 
HETATM 4778 O  O   . HOH IA 7 .   ? 19.012 2.899   -4.743  1.00 8.35   ? 550 HOH A O   1 
HETATM 4779 O  O   . HOH IA 7 .   ? 27.541 -17.036 -4.156  1.00 18.24  ? 551 HOH A O   1 
HETATM 4780 O  O   . HOH IA 7 .   ? 16.553 9.987   14.454  1.00 31.33  ? 552 HOH A O   1 
HETATM 4781 O  O   . HOH IA 7 .   ? 24.110 -14.238 8.805   1.00 24.00  ? 553 HOH A O   1 
HETATM 4782 O  O   . HOH IA 7 .   ? 38.777 -7.913  -1.974  1.00 18.23  ? 554 HOH A O   1 
HETATM 4783 O  O   . HOH IA 7 .   ? 14.040 -12.975 4.870   1.00 28.11  ? 555 HOH A O   1 
HETATM 4784 O  O   . HOH IA 7 .   ? 34.421 -13.664 -13.494 1.00 20.21  ? 556 HOH A O   1 
HETATM 4785 O  O   . HOH IA 7 .   ? 5.557  4.846   13.224  1.00 44.08  ? 557 HOH A O   1 
HETATM 4786 O  O   . HOH IA 7 .   ? 12.130 8.211   -17.067 1.00 11.67  ? 558 HOH A O   1 
HETATM 4787 O  O   . HOH IA 7 .   ? 26.734 18.211  6.055   1.00 14.35  ? 559 HOH A O   1 
HETATM 4788 O  O   . HOH IA 7 .   ? 10.858 -6.646  -24.525 1.00 29.94  ? 560 HOH A O   1 
HETATM 4789 O  O   . HOH IA 7 .   ? 16.344 11.812  9.182   1.00 16.98  ? 561 HOH A O   1 
HETATM 4790 O  O   . HOH IA 7 .   ? 37.304 -5.480  4.896   1.00 13.65  ? 562 HOH A O   1 
HETATM 4791 O  O   . HOH IA 7 .   ? 27.260 -9.898  15.117  1.00 15.88  ? 563 HOH A O   1 
HETATM 4792 O  O   . HOH IA 7 .   ? 27.705 11.461  -12.070 1.00 19.23  ? 564 HOH A O   1 
HETATM 4793 O  O   . HOH IA 7 .   ? 31.969 -16.414 3.785   1.00 18.94  ? 565 HOH A O   1 
HETATM 4794 O  O   . HOH IA 7 .   ? 14.574 -6.656  -12.322 1.00 21.18  ? 566 HOH A O   1 
HETATM 4795 O  O   . HOH IA 7 .   ? 18.257 -11.419 0.223   1.00 35.59  ? 567 HOH A O   1 
HETATM 4796 O  O   . HOH IA 7 .   ? 42.184 4.587   11.777  1.00 37.64  ? 568 HOH A O   1 
HETATM 4797 O  O   . HOH IA 7 .   ? 26.157 -13.926 -1.788  1.00 14.85  ? 569 HOH A O   1 
HETATM 4798 O  O   . HOH IA 7 .   ? 28.996 9.246   16.169  1.00 11.99  ? 570 HOH A O   1 
HETATM 4799 O  O   . HOH IA 7 .   ? 5.723  -0.962  -6.787  1.00 11.04  ? 571 HOH A O   1 
HETATM 4800 O  O   . HOH IA 7 .   ? 4.971  7.358   -1.933  1.00 13.74  ? 572 HOH A O   1 
HETATM 4801 O  O   . HOH IA 7 .   ? 39.738 19.557  -1.801  1.00 15.48  ? 573 HOH A O   1 
HETATM 4802 O  O   . HOH IA 7 .   ? 15.490 -6.616  -16.956 1.00 21.83  ? 574 HOH A O   1 
HETATM 4803 O  O   . HOH IA 7 .   ? 40.652 0.210   16.866  1.00 38.61  ? 575 HOH A O   1 
HETATM 4804 O  O   . HOH IA 7 .   ? 26.645 19.339  -9.757  1.00 25.24  ? 576 HOH A O   1 
HETATM 4805 O  O   . HOH IA 7 .   ? 3.795  4.470   -4.406  1.00 12.54  ? 577 HOH A O   1 
HETATM 4806 O  O   . HOH IA 7 .   ? 17.147 -5.075  -8.693  1.00 15.87  ? 578 HOH A O   1 
HETATM 4807 O  O   . HOH IA 7 .   ? 35.531 -1.506  11.754  1.00 12.15  ? 579 HOH A O   1 
HETATM 4808 O  O   . HOH IA 7 .   ? 26.623 -1.812  -10.578 1.00 26.00  ? 580 HOH A O   1 
HETATM 4809 O  O   . HOH IA 7 .   ? 20.681 -16.182 -5.723  1.00 24.58  ? 581 HOH A O   1 
HETATM 4810 O  O   . HOH IA 7 .   ? 29.041 -3.142  -9.667  1.00 23.74  ? 582 HOH A O   1 
HETATM 4811 O  O   . HOH IA 7 .   ? 28.238 -8.267  16.976  1.00 15.88  ? 583 HOH A O   1 
HETATM 4812 O  O   . HOH IA 7 .   ? 14.309 -1.340  -26.648 1.00 27.40  ? 584 HOH A O   1 
HETATM 4813 O  O   . HOH IA 7 .   ? 35.927 -12.021 -10.231 1.00 23.30  ? 585 HOH A O   1 
HETATM 4814 O  O   . HOH IA 7 .   ? 9.431  -11.625 3.720   1.00 37.91  ? 586 HOH A O   1 
HETATM 4815 O  O   . HOH IA 7 .   ? 14.177 -9.388  -1.019  1.00 17.34  ? 587 HOH A O   1 
HETATM 4816 O  O   . HOH IA 7 .   ? 31.356 -17.100 11.030  1.00 24.43  ? 588 HOH A O   1 
HETATM 4817 O  O   . HOH IA 7 .   ? 19.670 -3.761  -24.467 1.00 53.97  ? 589 HOH A O   1 
HETATM 4818 O  O   . HOH IA 7 .   ? 24.086 -16.215 3.448   1.00 40.32  ? 590 HOH A O   1 
HETATM 4819 O  O   . HOH IA 7 .   ? 33.468 -18.917 -13.343 1.00 49.63  ? 591 HOH A O   1 
HETATM 4820 O  O   . HOH IA 7 .   ? 34.491 -18.971 -3.605  1.00 24.55  ? 592 HOH A O   1 
HETATM 4821 O  O   . HOH IA 7 .   ? 13.526 -11.632 11.833  1.00 39.91  ? 593 HOH A O   1 
HETATM 4822 O  O   . HOH IA 7 .   ? 32.235 -10.871 20.326  1.00 42.22  ? 594 HOH A O   1 
HETATM 4823 O  O   . HOH IA 7 .   ? 12.435 11.801  8.599   1.00 27.13  ? 595 HOH A O   1 
HETATM 4824 O  O   . HOH IA 7 .   ? 39.482 -7.949  8.916   1.00 29.19  ? 596 HOH A O   1 
HETATM 4825 O  O   . HOH IA 7 .   ? 39.847 13.558  9.282   1.00 29.02  ? 597 HOH A O   1 
HETATM 4826 O  O   . HOH IA 7 .   ? 7.647  11.023  -0.451  1.00 22.91  ? 598 HOH A O   1 
HETATM 4827 O  O   . HOH IA 7 .   ? 34.661 5.467   21.828  1.00 22.08  ? 599 HOH A O   1 
HETATM 4828 O  O   . HOH IA 7 .   ? 44.111 -4.511  -3.365  1.00 27.50  ? 600 HOH A O   1 
HETATM 4829 O  O   . HOH IA 7 .   ? 21.820 -3.202  -5.709  1.00 9.87   ? 601 HOH A O   1 
HETATM 4830 O  O   . HOH IA 7 .   ? 6.600  17.545  -5.578  1.00 32.30  ? 602 HOH A O   1 
HETATM 4831 O  O   . HOH IA 7 .   ? 18.239 -8.963  -11.102 1.00 22.59  ? 603 HOH A O   1 
HETATM 4832 O  O   . HOH IA 7 .   ? 38.949 11.269  10.696  1.00 33.62  ? 604 HOH A O   1 
HETATM 4833 O  O   . HOH IA 7 .   ? 37.284 -18.661 7.450   1.00 53.61  ? 605 HOH A O   1 
HETATM 4834 O  O   . HOH IA 7 .   ? 34.131 -19.740 -6.196  1.00 26.75  ? 606 HOH A O   1 
HETATM 4835 O  O   . HOH IA 7 .   ? 37.939 -4.803  13.480  1.00 18.90  ? 607 HOH A O   1 
HETATM 4836 O  O   . HOH IA 7 .   ? 19.842 19.289  1.330   1.00 18.64  ? 608 HOH A O   1 
HETATM 4837 O  O   . HOH IA 7 .   ? 13.656 -12.703 -8.052  1.00 49.63  ? 609 HOH A O   1 
HETATM 4838 O  O   . HOH IA 7 .   ? 32.233 13.774  -10.736 1.00 25.71  ? 610 HOH A O   1 
HETATM 4839 O  O   . HOH IA 7 .   ? 30.995 -8.678  17.439  1.00 15.82  ? 611 HOH A O   1 
HETATM 4840 O  O   . HOH IA 7 .   ? 25.782 11.645  17.119  1.00 29.52  ? 612 HOH A O   1 
HETATM 4841 O  O   . HOH IA 7 .   ? 10.780 -4.959  7.965   1.00 15.07  ? 613 HOH A O   1 
HETATM 4842 O  O   . HOH IA 7 .   ? 32.578 -13.154 5.392   1.00 13.19  ? 614 HOH A O   1 
HETATM 4843 O  O   . HOH IA 7 .   ? 44.691 6.741   -8.982  1.00 15.94  ? 615 HOH A O   1 
HETATM 4844 O  O   . HOH IA 7 .   ? 5.477  14.117  -4.293  1.00 23.98  ? 616 HOH A O   1 
HETATM 4845 O  O   . HOH IA 7 .   ? 12.482 4.887   12.418  1.00 23.68  ? 617 HOH A O   1 
HETATM 4846 O  O   . HOH IA 7 .   ? 44.489 -3.595  0.761   1.00 28.74  ? 618 HOH A O   1 
HETATM 4847 O  O   . HOH IA 7 .   ? 15.700 10.349  6.895   1.00 11.78  ? 619 HOH A O   1 
HETATM 4848 O  O   . HOH IA 7 .   ? 12.692 9.107   10.032  1.00 16.82  ? 620 HOH A O   1 
HETATM 4849 O  O   . HOH IA 7 .   ? 39.307 4.217   16.421  1.00 18.19  ? 621 HOH A O   1 
HETATM 4850 O  O   . HOH IA 7 .   ? 43.269 8.583   14.587  1.00 38.79  ? 622 HOH A O   1 
HETATM 4851 O  O   . HOH IA 7 .   ? 32.389 -15.268 14.100  1.00 40.52  ? 623 HOH A O   1 
HETATM 4852 O  O   . HOH IA 7 .   ? 17.967 18.672  -8.648  1.00 20.25  ? 624 HOH A O   1 
HETATM 4853 O  O   . HOH IA 7 .   ? 19.225 19.741  -11.043 1.00 35.29  ? 625 HOH A O   1 
HETATM 4854 O  O   . HOH IA 7 .   ? 42.555 13.203  5.922   1.00 27.48  ? 626 HOH A O   1 
HETATM 4855 O  O   . HOH IA 7 .   ? 9.729  -0.331  -20.229 1.00 14.91  ? 627 HOH A O   1 
HETATM 4856 O  O   . HOH IA 7 .   ? 16.925 -5.318  16.606  1.00 31.02  ? 628 HOH A O   1 
HETATM 4857 O  O   . HOH IA 7 .   ? 29.897 20.694  8.266   1.00 24.46  ? 629 HOH A O   1 
HETATM 4858 O  O   . HOH IA 7 .   ? 4.147  13.041  -0.883  1.00 21.94  ? 630 HOH A O   1 
HETATM 4859 O  O   . HOH IA 7 .   ? 15.758 7.218   -22.686 1.00 24.88  ? 631 HOH A O   1 
HETATM 4860 O  O   . HOH IA 7 .   ? 8.260  14.533  -9.781  1.00 34.85  ? 632 HOH A O   1 
HETATM 4861 O  O   . HOH IA 7 .   ? 16.202 -4.470  -21.431 1.00 16.90  ? 633 HOH A O   1 
HETATM 4862 O  O   . HOH IA 7 .   ? 22.321 8.285   -20.472 1.00 39.51  ? 634 HOH A O   1 
HETATM 4863 O  O   . HOH IA 7 .   ? 27.087 17.661  10.466  1.00 39.02  ? 635 HOH A O   1 
HETATM 4864 O  O   . HOH IA 7 .   ? 21.135 23.783  0.455   1.00 37.59  ? 636 HOH A O   1 
HETATM 4865 O  O   . HOH IA 7 .   ? 18.599 21.086  -0.339  1.00 38.79  ? 637 HOH A O   1 
HETATM 4866 O  O   . HOH IA 7 .   ? 7.214  5.724   11.479  1.00 24.26  ? 638 HOH A O   1 
HETATM 4867 O  O   . HOH IA 7 .   ? 44.647 -3.115  -5.483  1.00 29.59  ? 639 HOH A O   1 
HETATM 4868 O  O   . HOH IA 7 .   ? 2.622  8.303   6.415   1.00 22.66  ? 640 HOH A O   1 
HETATM 4869 O  O   . HOH IA 7 .   ? 37.167 -7.540  13.085  1.00 20.91  ? 641 HOH A O   1 
HETATM 4870 O  O   . HOH IA 7 .   ? 29.605 -5.316  -12.384 1.00 26.45  ? 642 HOH A O   1 
HETATM 4871 O  O   . HOH IA 7 .   ? 10.904 -2.218  8.742   1.00 12.64  ? 643 HOH A O   1 
HETATM 4872 O  O   . HOH IA 7 .   ? 36.671 -7.407  -9.515  1.00 105.25 ? 644 HOH A O   1 
HETATM 4873 O  O   . HOH IA 7 .   ? 39.039 2.064   8.696   1.00 41.17  ? 645 HOH A O   1 
HETATM 4874 O  O   . HOH IA 7 .   ? 22.384 -0.362  21.201  1.00 36.58  ? 646 HOH A O   1 
HETATM 4875 O  O   . HOH IA 7 .   ? 28.302 -15.518 11.393  1.00 32.61  ? 647 HOH A O   1 
HETATM 4876 O  O   . HOH IA 7 .   ? 12.410 15.752  -13.500 1.00 32.28  ? 648 HOH A O   1 
HETATM 4877 O  O   . HOH IA 7 .   ? 47.859 -2.137  -1.763  1.00 33.55  ? 649 HOH A O   1 
HETATM 4878 O  O   . HOH IA 7 .   ? 21.731 -15.172 5.343   1.00 24.09  ? 650 HOH A O   1 
HETATM 4879 O  O   . HOH IA 7 .   ? 12.583 -9.303  11.252  1.00 23.68  ? 651 HOH A O   1 
HETATM 4880 O  O   . HOH IA 7 .   ? 15.266 13.492  -12.028 1.00 22.31  ? 652 HOH A O   1 
HETATM 4881 O  O   . HOH IA 7 .   ? 14.997 11.499  16.016  1.00 32.25  ? 653 HOH A O   1 
HETATM 4882 O  O   . HOH IA 7 .   ? 29.301 -20.912 -2.802  1.00 40.78  ? 654 HOH A O   1 
HETATM 4883 O  O   . HOH IA 7 .   ? 41.447 6.025   8.134   1.00 34.50  ? 655 HOH A O   1 
HETATM 4884 O  O   . HOH IA 7 .   ? 24.143 -0.253  -5.671  1.00 15.11  ? 656 HOH A O   1 
HETATM 4885 O  O   . HOH IA 7 .   ? 38.801 0.524   11.352  1.00 21.67  ? 657 HOH A O   1 
HETATM 4886 O  O   . HOH IA 7 .   ? 18.358 -12.247 -4.443  1.00 34.14  ? 658 HOH A O   1 
HETATM 4887 O  O   . HOH IA 7 .   ? 36.358 -12.523 -6.589  1.00 22.45  ? 659 HOH A O   1 
HETATM 4888 O  O   . HOH IA 7 .   ? 40.783 -5.875  -8.898  1.00 34.65  ? 660 HOH A O   1 
HETATM 4889 O  O   . HOH IA 7 .   ? 46.121 10.997  -2.282  1.00 29.22  ? 661 HOH A O   1 
HETATM 4890 O  O   . HOH IA 7 .   ? 16.116 -14.701 5.444   1.00 50.00  ? 662 HOH A O   1 
HETATM 4891 O  O   . HOH IA 7 .   ? 19.077 9.680   -19.679 1.00 29.00  ? 663 HOH A O   1 
HETATM 4892 O  O   . HOH IA 7 .   ? 46.522 6.395   12.497  1.00 47.37  ? 664 HOH A O   1 
HETATM 4893 O  O   . HOH IA 7 .   ? 42.392 -10.855 2.724   1.00 49.03  ? 665 HOH A O   1 
HETATM 4894 O  O   . HOH IA 7 .   ? 11.045 17.934  -1.199  1.00 44.18  ? 666 HOH A O   1 
HETATM 4895 O  O   . HOH IA 7 .   ? 14.779 -9.298  -13.345 1.00 34.36  ? 667 HOH A O   1 
HETATM 4896 O  O   . HOH IA 7 .   ? 14.265 19.753  -5.849  1.00 31.66  ? 668 HOH A O   1 
HETATM 4897 O  O   . HOH IA 7 .   ? 30.934 24.480  -3.326  1.00 18.85  ? 669 HOH A O   1 
HETATM 4898 O  O   . HOH IA 7 .   ? 39.681 2.406   14.498  1.00 25.48  ? 670 HOH A O   1 
HETATM 4899 O  O   . HOH IA 7 .   ? 17.845 23.552  -5.722  1.00 43.85  ? 671 HOH A O   1 
HETATM 4900 O  O   . HOH IA 7 .   ? 10.323 4.840   12.912  1.00 32.15  ? 672 HOH A O   1 
HETATM 4901 O  O   . HOH IA 7 .   ? 18.045 21.636  -7.217  1.00 32.01  ? 673 HOH A O   1 
HETATM 4902 O  O   . HOH IA 7 .   ? 35.632 19.896  3.615   1.00 27.90  ? 674 HOH A O   1 
HETATM 4903 O  O   . HOH IA 7 .   ? 5.694  -2.727  -4.548  1.00 12.44  ? 675 HOH A O   1 
HETATM 4904 O  O   . HOH IA 7 .   ? 7.636  -8.049  -16.000 1.00 45.37  ? 676 HOH A O   1 
HETATM 4905 O  O   . HOH IA 7 .   ? 4.442  -3.661  6.345   1.00 29.06  ? 677 HOH A O   1 
HETATM 4906 O  O   . HOH IA 7 .   ? 28.300 15.598  11.799  1.00 21.79  ? 678 HOH A O   1 
HETATM 4907 O  O   . HOH IA 7 .   ? 26.714 -7.686  26.113  1.00 26.78  ? 679 HOH A O   1 
HETATM 4908 O  O   . HOH IA 7 .   ? 47.717 3.853   6.082   1.00 48.98  ? 680 HOH A O   1 
HETATM 4909 O  O   . HOH IA 7 .   ? 29.241 -8.054  -15.947 1.00 36.77  ? 681 HOH A O   1 
HETATM 4910 O  O   . HOH IA 7 .   ? 21.850 -16.960 2.191   1.00 40.35  ? 682 HOH A O   1 
HETATM 4911 O  O   . HOH IA 7 .   ? 4.523  -2.032  10.556  1.00 39.73  ? 683 HOH A O   1 
HETATM 4912 O  O   . HOH IA 7 .   ? 8.216  6.954   -8.706  1.00 20.50  ? 684 HOH A O   1 
HETATM 4913 O  O   . HOH IA 7 .   ? 24.058 -20.190 -12.091 1.00 57.19  ? 685 HOH A O   1 
HETATM 4914 O  O   . HOH IA 7 .   ? 20.670 13.970  -18.387 1.00 44.53  ? 686 HOH A O   1 
HETATM 4915 O  O   . HOH IA 7 .   ? 46.765 7.006   5.182   1.00 43.12  ? 687 HOH A O   1 
HETATM 4916 O  O   . HOH IA 7 .   ? 30.425 17.164  12.970  1.00 43.63  ? 688 HOH A O   1 
HETATM 4917 O  O   . HOH IA 7 .   ? 15.950 -16.435 -12.557 1.00 56.72  ? 689 HOH A O   1 
HETATM 4918 O  O   . HOH IA 7 .   ? 15.839 18.600  -0.636  1.00 45.69  ? 690 HOH A O   1 
HETATM 4919 O  O   . HOH IA 7 .   ? 40.839 -13.157 4.173   1.00 33.66  ? 691 HOH A O   1 
HETATM 4920 O  O   . HOH IA 7 .   ? 6.207  3.418   -13.898 1.00 17.80  ? 692 HOH A O   1 
HETATM 4921 O  O   . HOH IA 7 .   ? 6.538  -2.399  -8.996  1.00 14.77  ? 693 HOH A O   1 
HETATM 4922 O  O   . HOH IA 7 .   ? 12.350 15.743  -9.885  1.00 30.47  ? 694 HOH A O   1 
HETATM 4923 O  O   . HOH IA 7 .   ? 17.067 18.452  1.696   1.00 40.46  ? 695 HOH A O   1 
HETATM 4924 O  O   . HOH IA 7 .   ? 37.085 11.530  -10.848 1.00 34.46  ? 696 HOH A O   1 
HETATM 4925 O  O   . HOH IA 7 .   ? 13.787 -14.174 10.876  1.00 46.50  ? 697 HOH A O   1 
HETATM 4926 O  O   . HOH IA 7 .   ? 37.955 6.864   -10.445 1.00 15.93  ? 698 HOH A O   1 
HETATM 4927 O  O   . HOH IA 7 .   ? 38.719 -15.448 9.080   1.00 42.24  ? 699 HOH A O   1 
HETATM 4928 O  O   . HOH IA 7 .   ? 32.251 7.613   20.078  1.00 28.53  ? 700 HOH A O   1 
HETATM 4929 O  O   . HOH IA 7 .   ? 10.507 -8.888  -20.076 1.00 33.35  ? 701 HOH A O   1 
HETATM 4930 O  O   . HOH IA 7 .   ? 20.790 -11.995 18.720  1.00 32.61  ? 702 HOH A O   1 
HETATM 4931 O  O   . HOH IA 7 .   ? 25.479 5.117   25.205  1.00 33.70  ? 703 HOH A O   1 
HETATM 4932 O  O   . HOH IA 7 .   ? 45.462 -1.214  2.571   1.00 43.69  ? 704 HOH A O   1 
HETATM 4933 O  O   . HOH IA 7 .   ? 24.308 14.763  14.226  1.00 20.42  ? 705 HOH A O   1 
HETATM 4934 O  O   . HOH IA 7 .   ? 19.241 -5.816  -13.060 1.00 28.43  ? 706 HOH A O   1 
HETATM 4935 O  O   . HOH IA 7 .   ? 37.086 -16.638 -0.942  1.00 31.49  ? 707 HOH A O   1 
HETATM 4936 O  O   . HOH IA 7 .   ? 32.012 24.342  -7.977  1.00 36.64  ? 708 HOH A O   1 
HETATM 4937 O  O   . HOH IA 7 .   ? 35.316 10.131  21.610  1.00 34.38  ? 709 HOH A O   1 
HETATM 4938 O  O   . HOH IA 7 .   ? 19.791 6.612   -21.499 1.00 42.99  ? 710 HOH A O   1 
HETATM 4939 O  O   . HOH IA 7 .   ? 11.305 11.591  -18.347 1.00 38.46  ? 711 HOH A O   1 
HETATM 4940 O  O   . HOH IA 7 .   ? 15.351 -8.077  -23.877 1.00 53.50  ? 712 HOH A O   1 
HETATM 4941 O  O   . HOH IA 7 .   ? 42.448 -2.158  -8.967  1.00 41.50  ? 713 HOH A O   1 
HETATM 4942 O  O   . HOH IA 7 .   ? 9.395  2.837   -25.392 1.00 15.75  ? 714 HOH A O   1 
HETATM 4943 O  O   . HOH IA 7 .   ? 20.785 -8.840  23.104  1.00 46.13  ? 715 HOH A O   1 
HETATM 4944 O  O   . HOH IA 7 .   ? 29.469 5.025   -9.581  1.00 76.40  ? 716 HOH A O   1 
HETATM 4945 O  O   . HOH IA 7 .   ? 2.789  3.855   10.109  1.00 47.57  ? 717 HOH A O   1 
HETATM 4946 O  O   . HOH IA 7 .   ? 24.303 16.295  -15.598 1.00 40.22  ? 718 HOH A O   1 
HETATM 4947 O  O   . HOH IA 7 .   ? 38.476 -11.502 11.470  1.00 41.10  ? 719 HOH A O   1 
HETATM 4948 O  O   . HOH IA 7 .   ? 28.520 23.804  2.082   1.00 14.09  ? 720 HOH A O   1 
HETATM 4949 O  O   . HOH IA 7 .   ? 33.961 24.797  -5.985  1.00 28.72  ? 721 HOH A O   1 
HETATM 4950 O  O   . HOH IA 7 .   ? 35.909 -17.880 11.550  1.00 48.05  ? 722 HOH A O   1 
HETATM 4951 O  O   . HOH IA 7 .   ? 18.354 -1.925  17.499  1.00 41.86  ? 723 HOH A O   1 
HETATM 4952 O  O   . HOH IA 7 .   ? 27.078 -4.818  -18.673 1.00 36.51  ? 724 HOH A O   1 
HETATM 4953 O  O   . HOH IA 7 .   ? 14.478 13.167  11.782  1.00 38.28  ? 725 HOH A O   1 
HETATM 4954 O  O   . HOH IA 7 .   ? 29.475 8.502   18.848  1.00 25.51  ? 726 HOH A O   1 
HETATM 4955 O  O   . HOH IA 7 .   ? 15.801 16.780  -8.601  1.00 21.73  ? 727 HOH A O   1 
HETATM 4956 O  O   . HOH IA 7 .   ? 40.436 6.029   15.515  1.00 47.00  ? 728 HOH A O   1 
HETATM 4957 O  O   . HOH IA 7 .   ? 8.172  8.456   11.658  1.00 29.20  ? 729 HOH A O   1 
HETATM 4958 O  O   . HOH IA 7 .   ? 25.380 22.959  -7.879  1.00 34.03  ? 730 HOH A O   1 
HETATM 4959 O  O   . HOH IA 7 .   ? 36.259 14.249  13.476  1.00 41.53  ? 731 HOH A O   1 
HETATM 4960 O  O   . HOH IA 7 .   ? 34.161 -16.976 15.206  1.00 40.38  ? 732 HOH A O   1 
HETATM 4961 O  O   . HOH IA 7 .   ? 25.511 -17.340 5.465   1.00 35.50  ? 733 HOH A O   1 
HETATM 4962 O  O   . HOH IA 7 .   ? 28.196 -11.971 16.586  1.00 28.24  ? 734 HOH A O   1 
HETATM 4963 O  O   . HOH IA 7 .   ? 30.652 -6.454  25.995  1.00 23.10  ? 735 HOH A O   1 
HETATM 4964 O  O   . HOH IA 7 .   ? 14.870 21.343  -7.328  1.00 46.32  ? 736 HOH A O   1 
HETATM 4965 O  O   . HOH IA 7 .   ? 32.018 15.182  15.537  1.00 50.28  ? 737 HOH A O   1 
HETATM 4966 O  O   . HOH IA 7 .   ? 25.880 -4.065  -13.058 1.00 45.66  ? 738 HOH A O   1 
HETATM 4967 O  O   . HOH IA 7 .   ? 31.222 -11.441 17.306  1.00 31.65  ? 739 HOH A O   1 
HETATM 4968 O  O   . HOH IA 7 .   ? 24.933 0.795   24.649  1.00 40.86  ? 740 HOH A O   1 
HETATM 4969 O  O   . HOH IA 7 .   ? 39.987 16.802  3.626   1.00 35.38  ? 741 HOH A O   1 
HETATM 4970 O  O   . HOH IA 7 .   ? 29.254 -24.575 -11.384 1.00 45.56  ? 742 HOH A O   1 
HETATM 4971 O  O   . HOH IA 7 .   ? 6.263  12.503  2.920   1.00 19.85  ? 743 HOH A O   1 
HETATM 4972 O  O   . HOH IA 7 .   ? 37.780 -1.728  10.324  1.00 15.05  ? 744 HOH A O   1 
HETATM 4973 O  O   . HOH IA 7 .   ? 38.734 13.223  13.530  1.00 39.00  ? 745 HOH A O   1 
HETATM 4974 O  O   . HOH IA 7 .   ? 5.365  10.925  -7.199  1.00 35.59  ? 746 HOH A O   1 
HETATM 4975 O  O   . HOH IA 7 .   ? 31.934 -19.161 3.475   1.00 37.57  ? 747 HOH A O   1 
HETATM 4976 O  O   . HOH IA 7 .   ? 9.731  16.722  -9.777  1.00 48.57  ? 748 HOH A O   1 
HETATM 4977 O  O   . HOH IA 7 .   ? 31.799 10.504  -10.568 1.00 49.57  ? 749 HOH A O   1 
HETATM 4978 O  O   . HOH IA 7 .   ? 34.717 -13.602 17.602  1.00 41.55  ? 750 HOH A O   1 
HETATM 4979 O  O   . HOH IA 7 .   ? 31.152 23.380  3.125   1.00 25.17  ? 751 HOH A O   1 
HETATM 4980 O  O   . HOH IA 7 .   ? 3.978  8.613   0.263   1.00 21.94  ? 752 HOH A O   1 
HETATM 4981 O  O   . HOH IA 7 .   ? 11.382 2.905   -27.331 1.00 30.00  ? 753 HOH A O   1 
HETATM 4982 O  O   . HOH IA 7 .   ? 17.195 -6.316  -11.089 1.00 22.98  ? 754 HOH A O   1 
HETATM 4983 O  O   . HOH IA 7 .   ? 12.757 -7.642  -23.571 1.00 47.25  ? 755 HOH A O   1 
HETATM 4984 O  O   . HOH IA 7 .   ? 46.981 11.642  4.549   1.00 43.22  ? 756 HOH A O   1 
HETATM 4985 O  O   . HOH IA 7 .   ? 42.458 4.493   16.100  1.00 39.18  ? 757 HOH A O   1 
HETATM 4986 O  O   . HOH IA 7 .   ? 11.406 -12.137 5.862   1.00 43.41  ? 758 HOH A O   1 
HETATM 4987 O  O   . HOH IA 7 .   ? 41.564 -8.604  7.530   1.00 47.17  ? 759 HOH A O   1 
HETATM 4988 O  O   . HOH IA 7 .   ? 6.825  7.825   -13.481 1.00 34.61  ? 760 HOH A O   1 
HETATM 4989 O  O   . HOH IA 7 .   ? 41.937 1.892   15.805  1.00 45.21  ? 761 HOH A O   1 
HETATM 4990 O  O   . HOH IA 7 .   ? 4.266  11.424  -3.060  1.00 33.58  ? 762 HOH A O   1 
HETATM 4991 O  O   . HOH IA 7 .   ? 27.074 15.035  14.156  1.00 22.23  ? 763 HOH A O   1 
HETATM 4992 O  O   . HOH IA 7 .   ? 10.535 -11.595 8.362   1.00 38.23  ? 764 HOH A O   1 
HETATM 4993 O  O   . HOH IA 7 .   ? 8.291  -5.226  9.088   1.00 24.82  ? 765 HOH A O   1 
HETATM 4994 O  O   . HOH IA 7 .   ? 12.422 7.975   12.800  1.00 45.20  ? 766 HOH A O   1 
HETATM 4995 O  O   . HOH IA 7 .   ? 10.929 -8.332  13.545  1.00 42.78  ? 767 HOH A O   1 
HETATM 4996 O  O   . HOH IA 7 .   ? 11.189 16.595  8.307   1.00 32.67  ? 768 HOH A O   1 
HETATM 4997 O  O   . HOH IA 7 .   ? 31.156 -19.482 9.512   1.00 43.77  ? 769 HOH A O   1 
HETATM 4998 O  O   . HOH IA 7 .   ? 34.212 7.035   23.893  1.00 35.01  ? 770 HOH A O   1 
HETATM 4999 O  O   . HOH IA 7 .   ? 35.501 -20.797 -0.205  1.00 52.93  ? 771 HOH A O   1 
HETATM 5000 O  O   . HOH IA 7 .   ? 37.972 -17.953 9.432   1.00 54.39  ? 772 HOH A O   1 
HETATM 5001 O  O   . HOH IA 7 .   ? 21.190 10.516  21.580  1.00 51.32  ? 773 HOH A O   1 
HETATM 5002 O  O   . HOH IA 7 .   ? 38.725 -17.328 -2.476  1.00 45.55  ? 774 HOH A O   1 
HETATM 5003 O  O   . HOH IA 7 .   ? 29.879 -8.655  -18.314 1.00 39.03  ? 775 HOH A O   1 
HETATM 5004 O  O   . HOH IA 7 .   ? 19.145 -14.319 14.834  1.00 37.38  ? 776 HOH A O   1 
HETATM 5005 O  O   . HOH IA 7 .   ? 21.928 -15.279 -15.760 1.00 50.71  ? 777 HOH A O   1 
HETATM 5006 O  O   . HOH IA 7 .   ? 4.087  -10.594 1.712   1.00 47.36  ? 778 HOH A O   1 
HETATM 5007 O  O   . HOH IA 7 .   ? 32.845 8.836   22.374  1.00 38.19  ? 779 HOH A O   1 
HETATM 5008 O  O   . HOH IA 7 .   ? 41.636 -6.429  5.546   1.00 29.05  ? 780 HOH A O   1 
HETATM 5009 O  O   . HOH IA 7 .   ? 39.262 -3.724  11.375  1.00 19.15  ? 781 HOH A O   1 
HETATM 5010 O  O   . HOH IA 7 .   ? 41.223 0.090   7.454   1.00 48.59  ? 782 HOH A O   1 
HETATM 5011 O  O   . HOH IA 7 .   ? 15.395 22.880  -2.514  1.00 39.54  ? 783 HOH A O   1 
HETATM 5012 O  O   . HOH IA 7 .   ? 27.562 1.222   -11.657 1.00 37.23  ? 784 HOH A O   1 
HETATM 5013 O  O   . HOH IA 7 .   ? 12.228 18.040  -6.255  1.00 24.40  ? 785 HOH A O   1 
HETATM 5014 O  O   . HOH IA 7 .   ? 42.185 14.750  3.703   1.00 43.40  ? 786 HOH A O   1 
HETATM 5015 O  O   . HOH IA 7 .   ? 6.881  -10.889 -21.875 1.00 47.22  ? 787 HOH A O   1 
HETATM 5016 O  O   . HOH IA 7 .   ? 2.900  6.975   -3.654  1.00 12.30  ? 788 HOH A O   1 
HETATM 5017 O  O   . HOH IA 7 .   ? 21.781 25.132  -7.048  1.00 50.61  ? 789 HOH A O   1 
HETATM 5018 O  O   . HOH IA 7 .   ? 27.242 -17.341 -12.911 1.00 32.46  ? 790 HOH A O   1 
HETATM 5019 O  O   . HOH IA 7 .   ? 19.793 26.998  -6.004  1.00 56.13  ? 791 HOH A O   1 
HETATM 5020 O  O   . HOH IA 7 .   ? 8.887  -8.876  -13.884 1.00 31.73  ? 792 HOH A O   1 
HETATM 5021 O  O   . HOH IA 7 .   ? 27.189 20.704  7.424   1.00 23.71  ? 793 HOH A O   1 
HETATM 5022 O  O   . HOH IA 7 .   ? 10.244 19.228  -7.441  1.00 34.04  ? 794 HOH A O   1 
HETATM 5023 O  O   . HOH IA 7 .   ? 29.606 14.625  17.507  1.00 39.74  ? 795 HOH A O   1 
HETATM 5024 O  O   . HOH IA 7 .   ? 40.749 -4.288  7.090   1.00 30.84  ? 796 HOH A O   1 
HETATM 5025 O  O   . HOH IA 7 .   ? 37.147 -16.160 16.169  1.00 50.80  ? 797 HOH A O   1 
HETATM 5026 O  O   . HOH IA 7 .   ? 18.950 -13.478 -2.240  1.00 42.86  ? 798 HOH A O   1 
HETATM 5027 O  O   . HOH IA 7 .   ? 14.995 -9.165  -16.401 1.00 39.89  ? 799 HOH A O   1 
HETATM 5028 O  O   . HOH IA 7 .   ? 17.495 5.184   -22.419 1.00 20.55  ? 800 HOH A O   1 
HETATM 5029 O  O   . HOH IA 7 .   ? 8.363  -7.768  10.061  1.00 30.35  ? 801 HOH A O   1 
HETATM 5030 O  O   . HOH IA 7 .   ? 39.328 -14.934 0.788   1.00 28.37  ? 802 HOH A O   1 
HETATM 5031 O  O   . HOH IA 7 .   ? 18.898 -4.865  -21.584 1.00 33.09  ? 803 HOH A O   1 
HETATM 5032 O  O   . HOH IA 7 .   ? 9.600  -10.185 -22.515 1.00 43.36  ? 804 HOH A O   1 
HETATM 5033 O  O   . HOH IA 7 .   ? 34.573 -9.593  -15.227 1.00 25.15  ? 805 HOH A O   1 
HETATM 5034 O  O   . HOH IA 7 .   ? 41.793 18.673  -3.676  1.00 41.59  ? 806 HOH A O   1 
HETATM 5035 O  O   . HOH IA 7 .   ? 13.871 19.350  -2.376  1.00 40.12  ? 807 HOH A O   1 
HETATM 5036 O  O   . HOH IA 7 .   ? 14.975 -6.481  -19.846 1.00 21.56  ? 808 HOH A O   1 
HETATM 5037 O  O   . HOH IA 7 .   ? 4.249  11.174  1.500   1.00 19.34  ? 809 HOH A O   1 
HETATM 5038 O  O   . HOH IA 7 .   ? 25.317 25.809  -1.520  1.00 24.98  ? 810 HOH A O   1 
HETATM 5039 O  O   . HOH IA 7 .   ? 6.569  11.136  -9.297  1.00 42.54  ? 811 HOH A O   1 
HETATM 5040 O  O   . HOH IA 7 .   ? 14.855 10.590  11.139  1.00 20.65  ? 812 HOH A O   1 
HETATM 5041 O  O   . HOH IA 7 .   ? 20.708 21.190  -13.276 1.00 45.31  ? 813 HOH A O   1 
HETATM 5042 O  O   . HOH IA 7 .   ? 36.566 13.086  20.470  1.00 37.04  ? 814 HOH A O   1 
HETATM 5043 O  O   . HOH IA 7 .   ? 26.698 -3.504  25.178  1.00 32.12  ? 815 HOH A O   1 
HETATM 5044 O  O   . HOH IA 7 .   ? 15.077 15.396  -14.049 1.00 21.27  ? 816 HOH A O   1 
HETATM 5045 O  O   . HOH IA 7 .   ? 17.496 19.085  -15.089 1.00 31.37  ? 817 HOH A O   1 
HETATM 5046 O  O   . HOH IA 7 .   ? 28.984 11.012  20.345  1.00 40.12  ? 818 HOH A O   1 
HETATM 5047 O  O   . HOH IA 7 .   ? 35.659 14.158  18.182  1.00 35.27  ? 819 HOH A O   1 
HETATM 5048 O  O   . HOH IA 7 .   ? 32.333 -15.104 -17.511 1.00 27.28  ? 820 HOH A O   1 
HETATM 5049 O  O   . HOH IA 7 .   ? 19.512 -13.835 10.698  1.00 32.18  ? 821 HOH A O   1 
HETATM 5050 O  O   . HOH IA 7 .   ? 12.335 14.622  11.729  1.00 31.74  ? 822 HOH A O   1 
HETATM 5051 O  O   . HOH IA 7 .   ? 38.925 -8.839  11.547  1.00 23.19  ? 823 HOH A O   1 
HETATM 5052 O  O   . HOH IA 7 .   ? 11.161 14.258  9.177   1.00 28.22  ? 824 HOH A O   1 
HETATM 5053 O  O   . HOH IA 7 .   ? 17.686 15.939  -17.989 1.00 40.73  ? 825 HOH A O   1 
HETATM 5054 O  O   . HOH IA 7 .   ? 15.254 -7.246  18.858  1.00 36.29  ? 826 HOH A O   1 
HETATM 5055 O  O   . HOH IA 7 .   ? 15.517 14.744  -16.873 1.00 25.49  ? 827 HOH A O   1 
HETATM 5056 O  O   . HOH IA 7 .   ? 40.353 -5.413  9.450   1.00 25.84  ? 828 HOH A O   1 
HETATM 5057 O  O   . HOH IA 7 .   ? 23.591 20.259  -13.392 1.00 32.80  ? 829 HOH A O   1 
HETATM 5058 O  O   . HOH IA 7 .   ? 3.567  -6.311  -0.084  1.00 32.79  ? 830 HOH A O   1 
HETATM 5059 O  O   . HOH IA 7 .   ? 26.143 8.942   26.274  1.00 37.78  ? 831 HOH A O   1 
HETATM 5060 O  O   . HOH IA 7 .   ? 2.250  10.841  3.451   1.00 20.10  ? 832 HOH A O   1 
HETATM 5061 O  O   . HOH IA 7 .   ? 16.194 -8.595  -20.916 1.00 43.86  ? 833 HOH A O   1 
HETATM 5062 O  O   . HOH IA 7 .   ? 25.687 6.819   27.470  1.00 34.22  ? 834 HOH A O   1 
HETATM 5063 O  O   . HOH IA 7 .   ? 43.601 1.347   11.769  1.00 48.22  ? 835 HOH A O   1 
HETATM 5064 O  O   . HOH IA 7 .   ? 1.596  -9.113  2.459   1.00 42.29  ? 836 HOH A O   1 
HETATM 5065 O  O   . HOH IA 7 .   ? 14.307 18.568  -10.391 1.00 55.97  ? 837 HOH A O   1 
HETATM 5066 O  O   . HOH IA 7 .   ? 28.758 -19.952 8.000   1.00 44.92  ? 838 HOH A O   1 
HETATM 5067 O  O   . HOH IA 7 .   ? 33.542 15.174  19.806  1.00 44.71  ? 839 HOH A O   1 
HETATM 5068 O  O   . HOH IA 7 .   ? 28.465 -18.920 -14.493 1.00 43.66  ? 840 HOH A O   1 
HETATM 5069 O  O   . HOH IA 7 .   ? 0.537  7.611   -2.339  1.00 11.75  ? 841 HOH A O   1 
HETATM 5070 O  O   . HOH IA 7 .   ? 29.549 13.730  20.045  1.00 43.63  ? 842 HOH A O   1 
HETATM 5071 O  O   . HOH JA 7 .   ? 60.484 -5.582  1.005   1.00 23.62  ? 401 HOH B O   1 
HETATM 5072 O  O   . HOH JA 7 .   ? 64.134 -7.410  -1.219  1.00 40.34  ? 402 HOH B O   1 
HETATM 5073 O  O   . HOH JA 7 .   ? 68.187 -4.720  -8.294  1.00 29.99  ? 403 HOH B O   1 
HETATM 5074 O  O   . HOH JA 7 .   ? 57.584 6.482   -33.858 1.00 21.62  ? 404 HOH B O   1 
HETATM 5075 O  O   . HOH JA 7 .   ? 45.873 -3.992  -1.574  1.00 36.47  ? 405 HOH B O   1 
HETATM 5076 O  O   . HOH JA 7 .   ? 42.148 -8.802  -5.598  1.00 33.98  ? 406 HOH B O   1 
HETATM 5077 O  O   . HOH JA 7 .   ? 42.051 -10.623 -4.127  1.00 53.42  ? 407 HOH B O   1 
HETATM 5078 O  O   . HOH JA 7 .   ? 50.539 9.128   -0.908  1.00 36.28  ? 408 HOH B O   1 
HETATM 5079 O  O   . HOH JA 7 .   ? 66.997 -7.142  -27.040 1.00 35.00  ? 409 HOH B O   1 
HETATM 5080 O  O   . HOH JA 7 .   ? 46.781 -0.166  -12.564 1.00 32.08  ? 410 HOH B O   1 
HETATM 5081 O  O   . HOH JA 7 .   ? 44.366 -18.248 -16.639 1.00 41.83  ? 411 HOH B O   1 
HETATM 5082 O  O   . HOH JA 7 .   ? 59.082 -14.190 -23.234 1.00 50.52  ? 412 HOH B O   1 
HETATM 5083 O  O   . HOH JA 7 .   ? 67.938 -2.574  -20.419 1.00 16.45  ? 413 HOH B O   1 
HETATM 5084 O  O   . HOH JA 7 .   ? 50.737 -17.924 -19.334 1.00 50.35  ? 414 HOH B O   1 
HETATM 5085 O  O   . HOH JA 7 .   ? 43.450 -21.023 -14.487 1.00 43.15  ? 415 HOH B O   1 
HETATM 5086 O  O   . HOH JA 7 .   ? 45.126 3.982   -41.288 1.00 27.46  ? 416 HOH B O   1 
HETATM 5087 O  O   . HOH JA 7 .   ? 28.185 9.728   -28.467 1.00 40.29  ? 417 HOH B O   1 
HETATM 5088 O  O   . HOH JA 7 .   ? 52.243 -16.306 -12.651 1.00 27.07  ? 418 HOH B O   1 
HETATM 5089 O  O   . HOH JA 7 .   ? 34.602 6.203   -35.888 1.00 35.61  ? 419 HOH B O   1 
HETATM 5090 O  O   . HOH JA 7 .   ? 58.777 -10.221 -18.392 1.00 25.89  ? 420 HOH B O   1 
HETATM 5091 O  O   . HOH JA 7 .   ? 60.218 10.018  -29.879 1.00 42.23  ? 421 HOH B O   1 
HETATM 5092 O  O   . HOH JA 7 .   ? 38.432 -19.811 -7.693  1.00 42.71  ? 422 HOH B O   1 
HETATM 5093 O  O   . HOH JA 7 .   ? 66.241 16.427  -17.750 1.00 38.96  ? 423 HOH B O   1 
HETATM 5094 O  O   . HOH JA 7 .   ? 54.245 -9.013  -5.782  1.00 42.74  ? 424 HOH B O   1 
HETATM 5095 O  O   . HOH JA 7 .   ? 65.697 10.765  -15.619 1.00 18.79  ? 425 HOH B O   1 
HETATM 5096 O  O   . HOH JA 7 .   ? 49.542 -6.869  -17.145 1.00 11.23  ? 426 HOH B O   1 
HETATM 5097 O  O   . HOH JA 7 .   ? 26.357 0.358   -14.015 1.00 22.81  ? 427 HOH B O   1 
HETATM 5098 O  O   . HOH JA 7 .   ? 41.353 -11.536 -1.739  1.00 29.01  ? 428 HOH B O   1 
HETATM 5099 O  O   . HOH JA 7 .   ? 60.882 9.462   0.299   1.00 20.07  ? 429 HOH B O   1 
HETATM 5100 O  O   . HOH JA 7 .   ? 62.347 16.900  -17.202 1.00 33.95  ? 430 HOH B O   1 
HETATM 5101 O  O   . HOH JA 7 .   ? 48.855 3.297   -44.382 1.00 45.16  ? 431 HOH B O   1 
HETATM 5102 O  O   . HOH JA 7 .   ? 49.373 -5.798  -7.969  1.00 34.86  ? 432 HOH B O   1 
HETATM 5103 O  O   . HOH JA 7 .   ? 40.189 -15.571 -34.606 1.00 37.63  ? 433 HOH B O   1 
HETATM 5104 O  O   . HOH JA 7 .   ? 47.844 -22.247 -8.150  1.00 42.43  ? 434 HOH B O   1 
HETATM 5105 O  O   . HOH JA 7 .   ? 55.341 7.668   -40.291 1.00 26.73  ? 435 HOH B O   1 
HETATM 5106 O  O   . HOH JA 7 .   ? 56.871 -15.493 -30.049 1.00 34.91  ? 436 HOH B O   1 
HETATM 5107 O  O   . HOH JA 7 .   ? 70.262 5.764   -23.178 1.00 22.32  ? 437 HOH B O   1 
HETATM 5108 O  O   . HOH JA 7 .   ? 40.713 18.903  -26.777 1.00 49.67  ? 438 HOH B O   1 
HETATM 5109 O  O   . HOH JA 7 .   ? 56.287 14.960  -11.490 1.00 17.87  ? 439 HOH B O   1 
HETATM 5110 O  O   . HOH JA 7 .   ? 51.010 3.504   -36.111 1.00 14.86  ? 440 HOH B O   1 
HETATM 5111 O  O   . HOH JA 7 .   ? 54.488 -12.673 -3.601  1.00 45.98  ? 441 HOH B O   1 
HETATM 5112 O  O   . HOH JA 7 .   ? 38.721 10.682  -37.468 1.00 35.94  ? 442 HOH B O   1 
HETATM 5113 O  O   . HOH JA 7 .   ? 35.571 -3.498  -28.275 1.00 18.63  ? 443 HOH B O   1 
HETATM 5114 O  O   . HOH JA 7 .   ? 48.434 -1.390  -6.306  1.00 23.12  ? 444 HOH B O   1 
HETATM 5115 O  O   . HOH JA 7 .   ? 32.620 -10.435 -21.573 1.00 29.06  ? 445 HOH B O   1 
HETATM 5116 O  O   . HOH JA 7 .   ? 55.237 -10.438 -15.963 1.00 22.02  ? 446 HOH B O   1 
HETATM 5117 O  O   . HOH JA 7 .   ? 46.037 0.932   -46.689 1.00 41.91  ? 447 HOH B O   1 
HETATM 5118 O  O   . HOH JA 7 .   ? 29.778 12.119  -19.042 1.00 39.10  ? 448 HOH B O   1 
HETATM 5119 O  O   . HOH JA 7 .   ? 35.469 -12.756 -35.099 1.00 31.37  ? 449 HOH B O   1 
HETATM 5120 O  O   . HOH JA 7 .   ? 51.561 -1.240  -15.915 1.00 9.52   ? 450 HOH B O   1 
HETATM 5121 O  O   . HOH JA 7 .   ? 61.899 -4.878  -21.041 1.00 13.26  ? 451 HOH B O   1 
HETATM 5122 O  O   . HOH JA 7 .   ? 42.864 -16.161 -21.258 1.00 24.19  ? 452 HOH B O   1 
HETATM 5123 O  O   . HOH JA 7 .   ? 66.161 1.178   -7.474  1.00 14.28  ? 453 HOH B O   1 
HETATM 5124 O  O   . HOH JA 7 .   ? 47.417 13.017  -3.911  1.00 37.15  ? 454 HOH B O   1 
HETATM 5125 O  O   . HOH JA 7 .   ? 53.756 12.175  -31.654 1.00 38.95  ? 455 HOH B O   1 
HETATM 5126 O  O   . HOH JA 7 .   ? 64.321 8.173   -30.345 1.00 27.83  ? 456 HOH B O   1 
HETATM 5127 O  O   . HOH JA 7 .   ? 46.494 -4.737  -43.234 1.00 25.35  ? 457 HOH B O   1 
HETATM 5128 O  O   . HOH JA 7 .   ? 64.021 9.827   -12.058 1.00 15.35  ? 458 HOH B O   1 
HETATM 5129 O  O   . HOH JA 7 .   ? 46.635 -13.667 -45.372 1.00 41.56  ? 459 HOH B O   1 
HETATM 5130 O  O   . HOH JA 7 .   ? 54.207 4.016   -41.571 1.00 32.61  ? 460 HOH B O   1 
HETATM 5131 O  O   . HOH JA 7 .   ? 44.439 6.503   -37.627 1.00 21.92  ? 461 HOH B O   1 
HETATM 5132 O  O   . HOH JA 7 .   ? 69.438 1.224   -26.277 1.00 12.64  ? 462 HOH B O   1 
HETATM 5133 O  O   . HOH JA 7 .   ? 49.080 -15.961 -32.772 1.00 31.47  ? 463 HOH B O   1 
HETATM 5134 O  O   . HOH JA 7 .   ? 41.283 14.097  -19.390 1.00 16.79  ? 464 HOH B O   1 
HETATM 5135 O  O   . HOH JA 7 .   ? 62.173 14.379  -5.338  1.00 30.11  ? 465 HOH B O   1 
HETATM 5136 O  O   . HOH JA 7 .   ? 66.081 9.936   -20.938 1.00 21.13  ? 466 HOH B O   1 
HETATM 5137 O  O   . HOH JA 7 .   ? 36.848 -19.139 -22.311 1.00 39.62  ? 467 HOH B O   1 
HETATM 5138 O  O   . HOH JA 7 .   ? 46.103 -12.646 -34.186 1.00 27.78  ? 468 HOH B O   1 
HETATM 5139 O  O   . HOH JA 7 .   ? 31.370 13.323  -23.409 1.00 43.42  ? 469 HOH B O   1 
HETATM 5140 O  O   . HOH JA 7 .   ? 66.205 13.682  -23.419 1.00 23.67  ? 470 HOH B O   1 
HETATM 5141 O  O   . HOH JA 7 .   ? 55.622 15.745  -30.423 1.00 41.34  ? 471 HOH B O   1 
HETATM 5142 O  O   . HOH JA 7 .   ? 36.615 -9.640  -13.184 1.00 22.00  ? 472 HOH B O   1 
HETATM 5143 O  O   . HOH JA 7 .   ? 43.856 -15.200 -7.785  1.00 29.33  ? 473 HOH B O   1 
HETATM 5144 O  O   . HOH JA 7 .   ? 35.117 -0.593  -25.246 1.00 15.55  ? 474 HOH B O   1 
HETATM 5145 O  O   . HOH JA 7 .   ? 45.048 -14.769 -35.512 1.00 43.44  ? 475 HOH B O   1 
HETATM 5146 O  O   . HOH JA 7 .   ? 55.134 19.485  -21.678 1.00 32.30  ? 476 HOH B O   1 
HETATM 5147 O  O   . HOH JA 7 .   ? 46.133 24.302  -22.029 1.00 32.76  ? 477 HOH B O   1 
HETATM 5148 O  O   . HOH JA 7 .   ? 52.517 22.341  -22.773 1.00 48.75  ? 478 HOH B O   1 
HETATM 5149 O  O   . HOH JA 7 .   ? 60.232 6.598   6.143   1.00 23.81  ? 479 HOH B O   1 
HETATM 5150 O  O   . HOH JA 7 .   ? 51.093 11.248  -33.960 1.00 25.88  ? 480 HOH B O   1 
HETATM 5151 O  O   . HOH JA 7 .   ? 57.800 12.486  -20.760 1.00 21.79  ? 481 HOH B O   1 
HETATM 5152 O  O   . HOH JA 7 .   ? 62.548 -10.914 -28.510 1.00 27.43  ? 482 HOH B O   1 
HETATM 5153 O  O   . HOH JA 7 .   ? 35.804 -14.535 -28.304 1.00 22.28  ? 483 HOH B O   1 
HETATM 5154 O  O   . HOH JA 7 .   ? 66.699 9.797   -18.345 1.00 17.99  ? 484 HOH B O   1 
HETATM 5155 O  O   . HOH JA 7 .   ? 56.424 4.203   -0.010  1.00 10.04  ? 485 HOH B O   1 
HETATM 5156 O  O   . HOH JA 7 .   ? 53.028 0.364   -31.716 1.00 10.91  ? 486 HOH B O   1 
HETATM 5157 O  O   . HOH JA 7 .   ? 52.518 -15.234 -34.658 1.00 24.98  ? 487 HOH B O   1 
HETATM 5158 O  O   . HOH JA 7 .   ? 47.613 -6.132  -40.702 1.00 21.92  ? 488 HOH B O   1 
HETATM 5159 O  O   . HOH JA 7 .   ? 65.158 -7.357  -14.452 1.00 30.90  ? 489 HOH B O   1 
HETATM 5160 O  O   . HOH JA 7 .   ? 39.516 15.958  -20.283 1.00 16.35  ? 490 HOH B O   1 
HETATM 5161 O  O   . HOH JA 7 .   ? 47.216 -14.344 -28.785 1.00 17.74  ? 491 HOH B O   1 
HETATM 5162 O  O   . HOH JA 7 .   ? 67.958 10.024  -29.007 1.00 27.13  ? 492 HOH B O   1 
HETATM 5163 O  O   . HOH JA 7 .   ? 34.462 -14.162 -21.703 1.00 18.18  ? 493 HOH B O   1 
HETATM 5164 O  O   . HOH JA 7 .   ? 52.832 -13.677 -28.057 1.00 16.59  ? 494 HOH B O   1 
HETATM 5165 O  O   . HOH JA 7 .   ? 51.040 6.294   -41.949 1.00 32.63  ? 495 HOH B O   1 
HETATM 5166 O  O   . HOH JA 7 .   ? 45.048 10.213  -37.440 1.00 42.23  ? 496 HOH B O   1 
HETATM 5167 O  O   . HOH JA 7 .   ? 42.814 10.423  -13.550 1.00 18.84  ? 497 HOH B O   1 
HETATM 5168 O  O   . HOH JA 7 .   ? 53.863 -3.918  -4.427  1.00 27.47  ? 498 HOH B O   1 
HETATM 5169 O  O   . HOH JA 7 .   ? 32.408 -5.261  -11.517 1.00 63.00  ? 499 HOH B O   1 
HETATM 5170 O  O   . HOH JA 7 .   ? 61.156 -9.485  -8.689  1.00 43.29  ? 500 HOH B O   1 
HETATM 5171 O  O   . HOH JA 7 .   ? 58.085 -14.301 -34.494 1.00 43.34  ? 501 HOH B O   1 
HETATM 5172 O  O   . HOH JA 7 .   ? 46.497 19.505  -12.913 1.00 14.51  ? 502 HOH B O   1 
HETATM 5173 O  O   . HOH JA 7 .   ? 53.052 -10.657 -23.668 1.00 14.45  ? 503 HOH B O   1 
HETATM 5174 O  O   . HOH JA 7 .   ? 60.986 8.842   -4.210  1.00 9.68   ? 504 HOH B O   1 
HETATM 5175 O  O   . HOH JA 7 .   ? 54.060 2.446   -15.977 1.00 8.24   ? 505 HOH B O   1 
HETATM 5176 O  O   . HOH JA 7 .   ? 56.935 14.388  -24.682 1.00 19.71  ? 506 HOH B O   1 
HETATM 5177 O  O   . HOH JA 7 .   ? 56.516 3.426   4.595   1.00 23.13  ? 507 HOH B O   1 
HETATM 5178 O  O   . HOH JA 7 .   ? 52.126 -7.855  -42.096 1.00 21.29  ? 508 HOH B O   1 
HETATM 5179 O  O   . HOH JA 7 .   ? 50.951 5.932   0.672   1.00 25.37  ? 509 HOH B O   1 
HETATM 5180 O  O   . HOH JA 7 .   ? 52.699 3.625   0.855   1.00 24.74  ? 510 HOH B O   1 
HETATM 5181 O  O   . HOH JA 7 .   ? 46.628 0.732   -6.990  1.00 26.37  ? 511 HOH B O   1 
HETATM 5182 O  O   . HOH JA 7 .   ? 70.512 2.284   -30.323 1.00 37.78  ? 512 HOH B O   1 
HETATM 5183 O  O   . HOH JA 7 .   ? 68.030 -1.480  -31.466 1.00 30.94  ? 513 HOH B O   1 
HETATM 5184 O  O   . HOH JA 7 .   ? 65.853 -6.753  -4.160  1.00 29.40  ? 514 HOH B O   1 
HETATM 5185 O  O   . HOH JA 7 .   ? 64.666 0.564   6.945   1.00 23.91  ? 515 HOH B O   1 
HETATM 5186 O  O   . HOH JA 7 .   ? 53.001 -17.336 -17.772 1.00 41.64  ? 516 HOH B O   1 
HETATM 5187 O  O   . HOH JA 7 .   ? 36.347 13.280  -12.583 1.00 41.32  ? 517 HOH B O   1 
HETATM 5188 O  O   . HOH JA 7 .   ? 56.598 -7.279  -35.426 1.00 19.84  ? 518 HOH B O   1 
HETATM 5189 O  O   . HOH JA 7 .   ? 45.212 -19.812 -11.153 1.00 27.82  ? 519 HOH B O   1 
HETATM 5190 O  O   . HOH JA 7 .   ? 25.956 1.127   -24.284 1.00 35.52  ? 520 HOH B O   1 
HETATM 5191 O  O   . HOH JA 7 .   ? 62.680 -7.601  -7.911  1.00 21.93  ? 521 HOH B O   1 
HETATM 5192 O  O   . HOH JA 7 .   ? 55.747 20.165  -18.303 1.00 20.41  ? 522 HOH B O   1 
HETATM 5193 O  O   . HOH JA 7 .   ? 55.566 -2.835  5.485   1.00 36.22  ? 523 HOH B O   1 
HETATM 5194 O  O   . HOH JA 7 .   ? 49.129 -15.996 -27.729 1.00 19.73  ? 524 HOH B O   1 
HETATM 5195 O  O   . HOH JA 7 .   ? 51.074 -13.326 -40.092 1.00 22.77  ? 525 HOH B O   1 
HETATM 5196 O  O   . HOH JA 7 .   ? 45.631 11.740  -9.648  1.00 15.16  ? 526 HOH B O   1 
HETATM 5197 O  O   . HOH JA 7 .   ? 35.014 12.179  -24.113 1.00 27.23  ? 527 HOH B O   1 
HETATM 5198 O  O   . HOH JA 7 .   ? 59.894 10.200  3.762   1.00 17.86  ? 528 HOH B O   1 
HETATM 5199 O  O   . HOH JA 7 .   ? 51.224 -16.671 -24.094 1.00 21.01  ? 529 HOH B O   1 
HETATM 5200 O  O   . HOH JA 7 .   ? 65.784 12.972  -6.226  1.00 25.85  ? 530 HOH B O   1 
HETATM 5201 O  O   . HOH JA 7 .   ? 48.620 20.307  -15.838 1.00 14.12  ? 531 HOH B O   1 
HETATM 5202 O  O   . HOH JA 7 .   ? 28.240 6.732   -12.592 1.00 36.62  ? 532 HOH B O   1 
HETATM 5203 O  O   . HOH JA 7 .   ? 33.723 -9.954  -28.778 1.00 37.84  ? 533 HOH B O   1 
HETATM 5204 O  O   . HOH JA 7 .   ? 65.177 0.326   -33.537 1.00 20.56  ? 534 HOH B O   1 
HETATM 5205 O  O   . HOH JA 7 .   ? 46.897 15.596  -30.852 1.00 28.57  ? 535 HOH B O   1 
HETATM 5206 O  O   . HOH JA 7 .   ? 63.746 1.700   -31.619 1.00 14.67  ? 536 HOH B O   1 
HETATM 5207 O  O   . HOH JA 7 .   ? 41.128 -17.648 -22.630 1.00 22.59  ? 537 HOH B O   1 
HETATM 5208 O  O   . HOH JA 7 .   ? 35.806 -6.867  -24.913 1.00 17.84  ? 538 HOH B O   1 
HETATM 5209 O  O   . HOH JA 7 .   ? 46.519 -1.261  -9.835  1.00 30.01  ? 539 HOH B O   1 
HETATM 5210 O  O   . HOH JA 7 .   ? 60.908 6.136   -0.762  1.00 11.80  ? 540 HOH B O   1 
HETATM 5211 O  O   . HOH JA 7 .   ? 56.713 -3.257  1.325   1.00 18.13  ? 541 HOH B O   1 
HETATM 5212 O  O   . HOH JA 7 .   ? 45.379 -17.296 -14.183 1.00 23.41  ? 542 HOH B O   1 
HETATM 5213 O  O   . HOH JA 7 .   ? 39.034 17.155  -17.494 1.00 19.37  ? 543 HOH B O   1 
HETATM 5214 O  O   . HOH JA 7 .   ? 69.309 3.967   -16.408 1.00 14.76  ? 544 HOH B O   1 
HETATM 5215 O  O   . HOH JA 7 .   ? 34.482 -4.800  -26.080 1.00 17.86  ? 545 HOH B O   1 
HETATM 5216 O  O   . HOH JA 7 .   ? 63.082 4.835   -11.269 1.00 16.31  ? 546 HOH B O   1 
HETATM 5217 O  O   . HOH JA 7 .   ? 40.746 -13.599 -40.162 1.00 48.11  ? 547 HOH B O   1 
HETATM 5218 O  O   . HOH JA 7 .   ? 48.396 8.435   -39.384 1.00 30.86  ? 548 HOH B O   1 
HETATM 5219 O  O   . HOH JA 7 .   ? 68.084 6.628   -19.171 1.00 13.39  ? 549 HOH B O   1 
HETATM 5220 O  O   . HOH JA 7 .   ? 56.812 9.974   -30.881 1.00 38.45  ? 550 HOH B O   1 
HETATM 5221 O  O   . HOH JA 7 .   ? 57.367 -5.717  -2.835  1.00 21.02  ? 551 HOH B O   1 
HETATM 5222 O  O   . HOH JA 7 .   ? 34.216 15.219  -27.104 1.00 39.77  ? 552 HOH B O   1 
HETATM 5223 O  O   . HOH JA 7 .   ? 58.683 19.334  -15.867 1.00 34.60  ? 553 HOH B O   1 
HETATM 5224 O  O   . HOH JA 7 .   ? 46.770 16.786  -28.291 1.00 20.74  ? 554 HOH B O   1 
HETATM 5225 O  O   . HOH JA 7 .   ? 66.867 3.651   -6.875  1.00 15.48  ? 555 HOH B O   1 
HETATM 5226 O  O   . HOH JA 7 .   ? 49.335 23.433  -19.120 1.00 23.80  ? 556 HOH B O   1 
HETATM 5227 O  O   . HOH JA 7 .   ? 43.500 -18.325 -42.518 1.00 30.88  ? 557 HOH B O   1 
HETATM 5228 O  O   . HOH JA 7 .   ? 66.218 -12.366 -21.767 1.00 43.73  ? 558 HOH B O   1 
HETATM 5229 O  O   . HOH JA 7 .   ? 58.682 0.261   6.186   1.00 22.83  ? 559 HOH B O   1 
HETATM 5230 O  O   . HOH JA 7 .   ? 59.580 15.589  -14.399 1.00 16.56  ? 560 HOH B O   1 
HETATM 5231 O  O   . HOH JA 7 .   ? 44.419 -6.786  -42.882 1.00 30.46  ? 561 HOH B O   1 
HETATM 5232 O  O   . HOH JA 7 .   ? 67.377 -1.231  -13.580 1.00 12.47  ? 562 HOH B O   1 
HETATM 5233 O  O   . HOH JA 7 .   ? 55.877 -5.102  -11.237 1.00 15.06  ? 563 HOH B O   1 
HETATM 5234 O  O   . HOH JA 7 .   ? 46.895 -14.575 -17.005 1.00 21.25  ? 564 HOH B O   1 
HETATM 5235 O  O   . HOH JA 7 .   ? 54.662 -8.532  -8.365  1.00 21.60  ? 565 HOH B O   1 
HETATM 5236 O  O   . HOH JA 7 .   ? 28.603 -4.473  -21.113 1.00 35.89  ? 566 HOH B O   1 
HETATM 5237 O  O   . HOH JA 7 .   ? 64.140 10.600  -31.414 1.00 41.82  ? 567 HOH B O   1 
HETATM 5238 O  O   . HOH JA 7 .   ? 41.865 -19.179 -29.575 1.00 28.86  ? 568 HOH B O   1 
HETATM 5239 O  O   . HOH JA 7 .   ? 32.293 -7.935  -22.172 1.00 39.25  ? 569 HOH B O   1 
HETATM 5240 O  O   . HOH JA 7 .   ? 67.052 -5.455  -14.012 1.00 31.97  ? 570 HOH B O   1 
HETATM 5241 O  O   . HOH JA 7 .   ? 42.115 24.005  -18.390 1.00 26.73  ? 571 HOH B O   1 
HETATM 5242 O  O   . HOH JA 7 .   ? 43.650 21.948  -15.224 1.00 30.30  ? 572 HOH B O   1 
HETATM 5243 O  O   . HOH JA 7 .   ? 40.808 -17.820 -32.680 1.00 36.82  ? 573 HOH B O   1 
HETATM 5244 O  O   . HOH JA 7 .   ? 50.468 15.116  -5.974  1.00 23.28  ? 574 HOH B O   1 
HETATM 5245 O  O   . HOH JA 7 .   ? 65.778 3.723   -32.275 1.00 16.13  ? 575 HOH B O   1 
HETATM 5246 O  O   . HOH JA 7 .   ? 58.391 -6.360  -7.466  1.00 20.31  ? 576 HOH B O   1 
HETATM 5247 O  O   . HOH JA 7 .   ? 51.225 -3.504  -14.463 1.00 9.96   ? 577 HOH B O   1 
HETATM 5248 O  O   . HOH JA 7 .   ? 53.354 -15.039 -16.472 1.00 38.34  ? 578 HOH B O   1 
HETATM 5249 O  O   . HOH JA 7 .   ? 38.473 -19.434 -15.082 1.00 27.65  ? 579 HOH B O   1 
HETATM 5250 O  O   . HOH JA 7 .   ? 40.503 -14.589 -24.505 1.00 17.75  ? 580 HOH B O   1 
HETATM 5251 O  O   . HOH JA 7 .   ? 69.768 9.272   -30.574 1.00 40.65  ? 581 HOH B O   1 
HETATM 5252 O  O   . HOH JA 7 .   ? 36.237 -9.814  -32.734 1.00 23.92  ? 582 HOH B O   1 
HETATM 5253 O  O   . HOH JA 7 .   ? 64.964 -3.468  -31.128 1.00 18.46  ? 583 HOH B O   1 
HETATM 5254 O  O   . HOH JA 7 .   ? 42.376 -11.525 -36.823 1.00 21.29  ? 584 HOH B O   1 
HETATM 5255 O  O   . HOH JA 7 .   ? 34.324 8.896   -32.406 1.00 38.11  ? 585 HOH B O   1 
HETATM 5256 O  O   . HOH JA 7 .   ? 60.727 2.435   -32.939 1.00 22.69  ? 586 HOH B O   1 
HETATM 5257 O  O   . HOH JA 7 .   ? 32.226 -12.750 -25.763 1.00 40.67  ? 587 HOH B O   1 
HETATM 5258 O  O   . HOH JA 7 .   ? 57.518 8.588   -28.458 1.00 13.68  ? 588 HOH B O   1 
HETATM 5259 O  O   . HOH JA 7 .   ? 45.954 5.749   -11.080 1.00 25.80  ? 589 HOH B O   1 
HETATM 5260 O  O   . HOH JA 7 .   ? 67.004 4.796   -11.958 1.00 26.88  ? 590 HOH B O   1 
HETATM 5261 O  O   . HOH JA 7 .   ? 46.680 -14.694 -31.489 1.00 41.09  ? 591 HOH B O   1 
HETATM 5262 O  O   . HOH JA 7 .   ? 54.781 -12.381 -19.218 1.00 40.01  ? 592 HOH B O   1 
HETATM 5263 O  O   . HOH JA 7 .   ? 39.826 14.051  -30.476 1.00 27.85  ? 593 HOH B O   1 
HETATM 5264 O  O   . HOH JA 7 .   ? 61.094 -3.752  7.232   1.00 54.45  ? 594 HOH B O   1 
HETATM 5265 O  O   . HOH JA 7 .   ? 70.434 6.881   -27.678 1.00 24.06  ? 595 HOH B O   1 
HETATM 5266 O  O   . HOH JA 7 .   ? 40.857 21.208  -24.277 1.00 29.58  ? 596 HOH B O   1 
HETATM 5267 O  O   . HOH JA 7 .   ? 54.554 -12.360 -14.382 1.00 30.83  ? 597 HOH B O   1 
HETATM 5268 O  O   . HOH JA 7 .   ? 38.837 -19.824 -12.181 1.00 34.69  ? 598 HOH B O   1 
HETATM 5269 O  O   . HOH JA 7 .   ? 43.725 -2.863  -10.753 1.00 31.26  ? 599 HOH B O   1 
HETATM 5270 O  O   . HOH JA 7 .   ? 65.079 14.058  -12.143 1.00 34.22  ? 600 HOH B O   1 
HETATM 5271 O  O   . HOH JA 7 .   ? 47.967 -18.097 -23.658 1.00 39.44  ? 601 HOH B O   1 
HETATM 5272 O  O   . HOH JA 7 .   ? 51.203 15.898  -30.312 1.00 36.16  ? 602 HOH B O   1 
HETATM 5273 O  O   . HOH JA 7 .   ? 42.809 24.849  -20.905 1.00 45.67  ? 603 HOH B O   1 
HETATM 5274 O  O   . HOH JA 7 .   ? 62.402 -6.736  -27.870 1.00 19.68  ? 604 HOH B O   1 
HETATM 5275 O  O   . HOH JA 7 .   ? 44.350 3.897   -43.985 1.00 32.54  ? 605 HOH B O   1 
HETATM 5276 O  O   . HOH JA 7 .   ? 45.344 13.873  -6.592  1.00 43.91  ? 606 HOH B O   1 
HETATM 5277 O  O   . HOH JA 7 .   ? 45.176 -11.318 -36.183 1.00 21.51  ? 607 HOH B O   1 
HETATM 5278 O  O   . HOH JA 7 .   ? 37.680 -3.646  -32.516 1.00 18.55  ? 608 HOH B O   1 
HETATM 5279 O  O   . HOH JA 7 .   ? 63.421 0.472   -0.123  1.00 16.81  ? 609 HOH B O   1 
HETATM 5280 O  O   . HOH JA 7 .   ? 52.721 -18.518 -10.990 1.00 28.43  ? 610 HOH B O   1 
HETATM 5281 O  O   . HOH JA 7 .   ? 42.831 -7.445  -45.054 1.00 35.43  ? 611 HOH B O   1 
HETATM 5282 O  O   . HOH JA 7 .   ? 55.076 18.927  -13.546 1.00 15.96  ? 612 HOH B O   1 
HETATM 5283 O  O   . HOH JA 7 .   ? 53.657 17.977  -23.589 1.00 18.60  ? 613 HOH B O   1 
HETATM 5284 O  O   . HOH JA 7 .   ? 36.211 -3.407  -45.273 1.00 42.76  ? 614 HOH B O   1 
HETATM 5285 O  O   . HOH JA 7 .   ? 63.957 15.605  -23.778 1.00 35.56  ? 615 HOH B O   1 
HETATM 5286 O  O   . HOH JA 7 .   ? 31.757 17.897  -24.742 1.00 42.30  ? 616 HOH B O   1 
HETATM 5287 O  O   . HOH JA 7 .   ? 34.304 -8.651  -17.791 1.00 18.37  ? 617 HOH B O   1 
HETATM 5288 O  O   . HOH JA 7 .   ? 57.206 8.162   1.703   1.00 23.78  ? 618 HOH B O   1 
HETATM 5289 O  O   . HOH JA 7 .   ? 35.542 9.116   -13.370 1.00 30.87  ? 619 HOH B O   1 
HETATM 5290 O  O   . HOH JA 7 .   ? 30.413 11.340  -28.066 1.00 34.26  ? 620 HOH B O   1 
HETATM 5291 O  O   . HOH JA 7 .   ? 63.524 8.333   3.885   1.00 17.16  ? 621 HOH B O   1 
HETATM 5292 O  O   . HOH JA 7 .   ? 37.788 -5.926  -34.267 1.00 21.15  ? 622 HOH B O   1 
HETATM 5293 O  O   . HOH JA 7 .   ? 60.548 -11.666 -30.235 1.00 37.10  ? 623 HOH B O   1 
HETATM 5294 O  O   . HOH JA 7 .   ? 34.052 -0.117  -29.591 1.00 41.30  ? 624 HOH B O   1 
HETATM 5295 O  O   . HOH JA 7 .   ? 48.025 -21.858 -13.539 1.00 39.68  ? 625 HOH B O   1 
HETATM 5296 O  O   . HOH JA 7 .   ? 59.310 14.905  -21.903 1.00 23.36  ? 626 HOH B O   1 
HETATM 5297 O  O   . HOH JA 7 .   ? 53.234 7.641   0.340   1.00 26.96  ? 627 HOH B O   1 
HETATM 5298 O  O   . HOH JA 7 .   ? 62.403 -4.050  -28.837 1.00 18.48  ? 628 HOH B O   1 
HETATM 5299 O  O   . HOH JA 7 .   ? 43.099 -4.815  -7.719  1.00 22.01  ? 629 HOH B O   1 
HETATM 5300 O  O   . HOH JA 7 .   ? 55.516 22.627  -16.996 1.00 23.07  ? 630 HOH B O   1 
HETATM 5301 O  O   . HOH JA 7 .   ? 49.836 12.173  -31.621 1.00 27.55  ? 631 HOH B O   1 
HETATM 5302 O  O   . HOH JA 7 .   ? 39.259 15.332  -12.601 1.00 38.56  ? 632 HOH B O   1 
HETATM 5303 O  O   . HOH JA 7 .   ? 37.939 22.295  -16.312 1.00 40.60  ? 633 HOH B O   1 
HETATM 5304 O  O   . HOH JA 7 .   ? 44.763 -17.725 -30.220 1.00 31.90  ? 634 HOH B O   1 
HETATM 5305 O  O   . HOH JA 7 .   ? 48.930 -0.499  -14.748 1.00 16.36  ? 635 HOH B O   1 
HETATM 5306 O  O   . HOH JA 7 .   ? 63.085 -12.881 -23.355 1.00 38.22  ? 636 HOH B O   1 
HETATM 5307 O  O   . HOH JA 7 .   ? 35.104 6.511   -10.841 1.00 20.04  ? 637 HOH B O   1 
HETATM 5308 O  O   . HOH JA 7 .   ? 67.413 -3.269  -15.612 1.00 15.26  ? 638 HOH B O   1 
HETATM 5309 O  O   . HOH JA 7 .   ? 39.882 2.205   -43.008 1.00 39.77  ? 639 HOH B O   1 
HETATM 5310 O  O   . HOH JA 7 .   ? 68.925 -5.254  -26.437 1.00 25.80  ? 640 HOH B O   1 
HETATM 5311 O  O   . HOH JA 7 .   ? 51.304 1.922   0.386   1.00 38.45  ? 641 HOH B O   1 
HETATM 5312 O  O   . HOH JA 7 .   ? 41.400 16.569  -10.598 1.00 40.05  ? 642 HOH B O   1 
HETATM 5313 O  O   . HOH JA 7 .   ? 32.269 -14.685 -23.452 1.00 37.62  ? 643 HOH B O   1 
HETATM 5314 O  O   . HOH JA 7 .   ? 56.686 -15.404 -5.596  1.00 42.73  ? 644 HOH B O   1 
HETATM 5315 O  O   . HOH JA 7 .   ? 33.586 -0.867  -34.367 1.00 48.35  ? 645 HOH B O   1 
HETATM 5316 O  O   . HOH JA 7 .   ? 36.185 -17.334 -17.956 1.00 34.53  ? 646 HOH B O   1 
HETATM 5317 O  O   . HOH JA 7 .   ? 28.820 -5.278  -16.734 1.00 31.86  ? 647 HOH B O   1 
HETATM 5318 O  O   . HOH JA 7 .   ? 53.185 -14.532 -24.003 1.00 21.68  ? 648 HOH B O   1 
HETATM 5319 O  O   . HOH JA 7 .   ? 47.042 -13.548 -7.630  1.00 26.71  ? 649 HOH B O   1 
HETATM 5320 O  O   . HOH JA 7 .   ? 31.751 4.181   -29.454 1.00 42.66  ? 650 HOH B O   1 
HETATM 5321 O  O   . HOH JA 7 .   ? 34.262 0.383   -37.423 1.00 47.76  ? 651 HOH B O   1 
HETATM 5322 O  O   . HOH JA 7 .   ? 56.860 -20.697 -7.516  1.00 27.28  ? 652 HOH B O   1 
HETATM 5323 O  O   . HOH JA 7 .   ? 45.709 -3.733  -46.639 1.00 42.69  ? 653 HOH B O   1 
HETATM 5324 O  O   . HOH JA 7 .   ? 64.870 6.761   -12.396 1.00 17.29  ? 654 HOH B O   1 
HETATM 5325 O  O   . HOH JA 7 .   ? 43.810 18.523  -10.037 1.00 34.66  ? 655 HOH B O   1 
HETATM 5326 O  O   . HOH JA 7 .   ? 44.043 -10.334 -5.789  1.00 28.75  ? 656 HOH B O   1 
HETATM 5327 O  O   . HOH JA 7 .   ? 28.337 -3.731  -14.680 1.00 40.67  ? 657 HOH B O   1 
HETATM 5328 O  O   . HOH JA 7 .   ? 48.656 -16.424 -18.784 1.00 42.34  ? 658 HOH B O   1 
HETATM 5329 O  O   . HOH JA 7 .   ? 67.742 14.450  -15.925 1.00 35.78  ? 659 HOH B O   1 
HETATM 5330 O  O   . HOH JA 7 .   ? 30.047 -0.508  -12.750 1.00 42.49  ? 660 HOH B O   1 
HETATM 5331 O  O   . HOH JA 7 .   ? 36.685 -12.471 -12.848 1.00 20.68  ? 661 HOH B O   1 
HETATM 5332 O  O   . HOH JA 7 .   ? 39.195 -19.113 -5.179  1.00 53.74  ? 662 HOH B O   1 
HETATM 5333 O  O   . HOH JA 7 .   ? 67.535 8.832   -11.291 1.00 50.60  ? 663 HOH B O   1 
HETATM 5334 O  O   . HOH JA 7 .   ? 45.412 12.981  -33.769 1.00 37.73  ? 664 HOH B O   1 
HETATM 5335 O  O   . HOH JA 7 .   ? 24.265 3.989   -20.096 1.00 37.09  ? 665 HOH B O   1 
HETATM 5336 O  O   . HOH JA 7 .   ? 53.909 -3.485  1.647   1.00 35.59  ? 666 HOH B O   1 
HETATM 5337 O  O   . HOH JA 7 .   ? 58.221 16.257  -26.057 1.00 43.12  ? 667 HOH B O   1 
HETATM 5338 O  O   . HOH JA 7 .   ? 33.485 -1.496  -11.956 1.00 44.86  ? 668 HOH B O   1 
HETATM 5339 O  O   . HOH JA 7 .   ? 58.087 14.001  -9.750  1.00 25.49  ? 669 HOH B O   1 
HETATM 5340 O  O   . HOH JA 7 .   ? 52.525 -14.943 -37.461 1.00 31.74  ? 670 HOH B O   1 
HETATM 5341 O  O   . HOH JA 7 .   ? 67.375 -6.034  -2.120  1.00 39.38  ? 671 HOH B O   1 
HETATM 5342 O  O   . HOH JA 7 .   ? 68.847 7.135   -21.795 1.00 29.78  ? 672 HOH B O   1 
HETATM 5343 O  O   . HOH JA 7 .   ? 26.979 10.788  -18.978 1.00 48.56  ? 673 HOH B O   1 
HETATM 5344 O  O   . HOH JA 7 .   ? 41.648 2.442   -45.024 1.00 46.60  ? 674 HOH B O   1 
HETATM 5345 O  O   . HOH JA 7 .   ? 35.023 5.326   -43.382 1.00 50.04  ? 675 HOH B O   1 
HETATM 5346 O  O   . HOH JA 7 .   ? 47.394 -17.682 -26.468 1.00 31.10  ? 676 HOH B O   1 
HETATM 5347 O  O   . HOH JA 7 .   ? 46.160 -20.041 -15.362 1.00 43.40  ? 677 HOH B O   1 
HETATM 5348 O  O   . HOH JA 7 .   ? 34.404 -15.548 -15.627 1.00 23.32  ? 678 HOH B O   1 
HETATM 5349 O  O   . HOH JA 7 .   ? 53.664 -5.361  -6.832  1.00 27.97  ? 679 HOH B O   1 
HETATM 5350 O  O   . HOH JA 7 .   ? 58.058 -14.067 -15.483 1.00 47.01  ? 680 HOH B O   1 
HETATM 5351 O  O   . HOH JA 7 .   ? 60.554 15.653  -11.809 1.00 33.82  ? 681 HOH B O   1 
HETATM 5352 O  O   . HOH JA 7 .   ? 26.321 4.995   -26.626 1.00 42.11  ? 682 HOH B O   1 
HETATM 5353 O  O   . HOH JA 7 .   ? 52.623 -20.511 -14.598 1.00 44.65  ? 683 HOH B O   1 
HETATM 5354 O  O   . HOH JA 7 .   ? 41.437 5.082   -41.513 1.00 43.39  ? 684 HOH B O   1 
HETATM 5355 O  O   . HOH JA 7 .   ? 58.353 -8.855  -6.353  1.00 35.14  ? 685 HOH B O   1 
HETATM 5356 O  O   . HOH JA 7 .   ? 41.142 -20.303 -22.120 1.00 46.71  ? 686 HOH B O   1 
HETATM 5357 O  O   . HOH JA 7 .   ? 54.764 -13.804 -26.097 1.00 20.56  ? 687 HOH B O   1 
HETATM 5358 O  O   . HOH JA 7 .   ? 64.660 6.385   -32.482 1.00 19.75  ? 688 HOH B O   1 
HETATM 5359 O  O   . HOH JA 7 .   ? 62.887 -13.557 -27.485 1.00 37.86  ? 689 HOH B O   1 
HETATM 5360 O  O   . HOH JA 7 .   ? 63.732 4.142   4.612   1.00 14.79  ? 690 HOH B O   1 
HETATM 5361 O  O   . HOH JA 7 .   ? 67.843 -2.852  -33.535 1.00 43.82  ? 691 HOH B O   1 
HETATM 5362 O  O   . HOH JA 7 .   ? 69.609 1.632   -32.231 1.00 54.87  ? 692 HOH B O   1 
HETATM 5363 O  O   . HOH JA 7 .   ? 61.573 17.097  -19.926 1.00 37.80  ? 693 HOH B O   1 
HETATM 5364 O  O   . HOH JA 7 .   ? 57.236 16.638  -13.392 1.00 26.92  ? 694 HOH B O   1 
HETATM 5365 O  O   . HOH JA 7 .   ? 41.881 -21.338 -27.177 1.00 53.49  ? 695 HOH B O   1 
HETATM 5366 O  O   . HOH JA 7 .   ? 56.408 -7.342  1.256   1.00 48.32  ? 696 HOH B O   1 
HETATM 5367 O  O   . HOH JA 7 .   ? 46.923 -3.525  -7.179  1.00 30.04  ? 697 HOH B O   1 
HETATM 5368 O  O   . HOH JA 7 .   ? 56.210 16.923  -24.141 1.00 40.67  ? 698 HOH B O   1 
HETATM 5369 O  O   . HOH JA 7 .   ? 34.635 -13.693 -30.741 1.00 43.89  ? 699 HOH B O   1 
HETATM 5370 O  O   . HOH JA 7 .   ? 66.759 11.230  -24.608 1.00 22.53  ? 700 HOH B O   1 
HETATM 5371 O  O   . HOH JA 7 .   ? 53.008 8.881   -41.161 1.00 45.26  ? 701 HOH B O   1 
HETATM 5372 O  O   . HOH JA 7 .   ? 39.479 24.399  -17.485 1.00 38.84  ? 702 HOH B O   1 
HETATM 5373 O  O   . HOH JA 7 .   ? 30.805 -2.564  -11.300 1.00 54.82  ? 703 HOH B O   1 
HETATM 5374 O  O   . HOH JA 7 .   ? 31.654 -10.246 -27.031 1.00 49.57  ? 704 HOH B O   1 
HETATM 5375 O  O   . HOH JA 7 .   ? 32.630 -10.411 -19.070 1.00 34.36  ? 705 HOH B O   1 
HETATM 5376 O  O   . HOH JA 7 .   ? 44.851 22.060  -25.451 1.00 38.83  ? 706 HOH B O   1 
HETATM 5377 O  O   . HOH JA 7 .   ? 34.054 -1.596  -31.753 1.00 38.45  ? 707 HOH B O   1 
HETATM 5378 O  O   . HOH JA 7 .   ? 60.610 0.352   8.523   1.00 41.74  ? 708 HOH B O   1 
HETATM 5379 O  O   . HOH JA 7 .   ? 25.268 -2.943  -18.518 1.00 40.42  ? 709 HOH B O   1 
HETATM 5380 O  O   . HOH JA 7 .   ? 55.806 -5.996  -8.670  1.00 22.18  ? 710 HOH B O   1 
HETATM 5381 O  O   . HOH JA 7 .   ? 38.475 -9.127  -4.880  1.00 45.34  ? 711 HOH B O   1 
HETATM 5382 O  O   . HOH JA 7 .   ? 38.402 18.321  -28.541 1.00 44.70  ? 712 HOH B O   1 
HETATM 5383 O  O   . HOH JA 7 .   ? 67.627 10.693  -14.145 1.00 26.37  ? 713 HOH B O   1 
HETATM 5384 O  O   . HOH JA 7 .   ? 36.182 -6.365  -40.964 1.00 44.74  ? 714 HOH B O   1 
HETATM 5385 O  O   . HOH JA 7 .   ? 31.565 -2.541  -27.801 1.00 47.43  ? 715 HOH B O   1 
HETATM 5386 O  O   . HOH JA 7 .   ? 68.082 9.779   -22.546 1.00 27.22  ? 716 HOH B O   1 
HETATM 5387 O  O   . HOH JA 7 .   ? 61.784 4.566   6.531   1.00 23.18  ? 717 HOH B O   1 
HETATM 5388 O  O   . HOH JA 7 .   ? 49.310 13.238  -1.066  1.00 41.63  ? 718 HOH B O   1 
HETATM 5389 O  O   . HOH JA 7 .   ? 35.474 -7.226  -33.703 1.00 24.22  ? 719 HOH B O   1 
HETATM 5390 O  O   . HOH JA 7 .   ? 43.726 24.471  -15.957 1.00 39.94  ? 720 HOH B O   1 
HETATM 5391 O  O   . HOH JA 7 .   ? 43.731 5.758   -40.139 1.00 41.67  ? 721 HOH B O   1 
HETATM 5392 O  O   . HOH JA 7 .   ? 64.952 -7.246  -28.877 1.00 21.33  ? 722 HOH B O   1 
HETATM 5393 O  O   . HOH JA 7 .   ? 35.440 -3.799  -30.964 1.00 19.87  ? 723 HOH B O   1 
HETATM 5394 O  O   . HOH JA 7 .   ? 34.315 -18.260 -15.449 1.00 42.92  ? 724 HOH B O   1 
HETATM 5395 O  O   . HOH JA 7 .   ? 31.436 12.813  -30.149 1.00 51.60  ? 725 HOH B O   1 
HETATM 5396 O  O   . HOH JA 7 .   ? 53.019 -15.801 -29.883 1.00 33.24  ? 726 HOH B O   1 
HETATM 5397 O  O   . HOH JA 7 .   ? 44.647 -12.522 -7.734  1.00 29.40  ? 727 HOH B O   1 
HETATM 5398 O  O   . HOH JA 7 .   ? 48.322 13.960  -32.396 1.00 48.87  ? 728 HOH B O   1 
HETATM 5399 O  O   . HOH JA 7 .   ? 48.620 16.866  -7.019  1.00 28.91  ? 729 HOH B O   1 
HETATM 5400 O  O   . HOH JA 7 .   ? 52.049 -18.040 -26.363 1.00 43.87  ? 730 HOH B O   1 
HETATM 5401 O  O   . HOH JA 7 .   ? 68.452 11.527  -26.645 1.00 37.15  ? 731 HOH B O   1 
HETATM 5402 O  O   . HOH JA 7 .   ? 45.817 8.364   -39.011 1.00 38.60  ? 732 HOH B O   1 
HETATM 5403 O  O   . HOH JA 7 .   ? 56.188 -0.148  6.920   1.00 36.16  ? 733 HOH B O   1 
HETATM 5404 O  O   . HOH JA 7 .   ? 57.416 5.594   6.132   1.00 36.50  ? 734 HOH B O   1 
HETATM 5405 O  O   . HOH JA 7 .   ? 52.129 -9.100  -44.435 1.00 28.17  ? 735 HOH B O   1 
HETATM 5406 O  O   . HOH JA 7 .   ? 57.807 -5.433  -0.098  1.00 25.20  ? 736 HOH B O   1 
HETATM 5407 O  O   . HOH JA 7 .   ? 65.523 -1.674  8.206   1.00 33.83  ? 737 HOH B O   1 
HETATM 5408 O  O   . HOH JA 7 .   ? 54.813 -15.035 -38.817 1.00 50.34  ? 738 HOH B O   1 
HETATM 5409 O  O   . HOH JA 7 .   ? 50.315 -17.069 -30.020 1.00 36.61  ? 739 HOH B O   1 
HETATM 5410 O  O   . HOH JA 7 .   ? 66.202 11.635  -30.800 1.00 45.37  ? 740 HOH B O   1 
HETATM 5411 O  O   . HOH JA 7 .   ? 55.463 6.305   1.364   1.00 16.12  ? 741 HOH B O   1 
HETATM 5412 O  O   . HOH JA 7 .   ? 70.281 6.367   -17.539 1.00 14.14  ? 742 HOH B O   1 
HETATM 5413 O  O   . HOH JA 7 .   ? 44.659 -16.207 -5.264  1.00 47.12  ? 743 HOH B O   1 
HETATM 5414 O  O   . HOH JA 7 .   ? 38.488 16.449  -30.468 1.00 36.79  ? 744 HOH B O   1 
HETATM 5415 O  O   . HOH JA 7 .   ? 32.629 6.426   -37.789 1.00 51.66  ? 745 HOH B O   1 
HETATM 5416 O  O   . HOH JA 7 .   ? 44.690 -2.272  -8.831  1.00 33.47  ? 746 HOH B O   1 
HETATM 5417 O  O   . HOH JA 7 .   ? 31.502 -8.050  -25.325 1.00 41.57  ? 747 HOH B O   1 
HETATM 5418 O  O   . HOH JA 7 .   ? 66.359 11.246  -12.093 1.00 32.96  ? 748 HOH B O   1 
HETATM 5419 O  O   . HOH JA 7 .   ? 30.233 13.020  -25.625 1.00 36.79  ? 749 HOH B O   1 
HETATM 5420 O  O   . HOH JA 7 .   ? 34.320 -7.516  -36.164 1.00 40.33  ? 750 HOH B O   1 
HETATM 5421 O  O   . HOH JA 7 .   ? 74.266 5.222   -20.314 1.00 13.41  ? 751 HOH B O   1 
HETATM 5422 O  O   . HOH JA 7 .   ? 45.537 1.532   -9.152  1.00 41.94  ? 752 HOH B O   1 
HETATM 5423 O  O   . HOH JA 7 .   ? 27.466 12.879  -25.586 1.00 41.19  ? 753 HOH B O   1 
HETATM 5424 O  O   . HOH JA 7 .   ? 64.129 -8.328  -5.602  1.00 34.28  ? 754 HOH B O   1 
HETATM 5425 O  O   . HOH JA 7 .   ? 69.269 10.288  -17.950 1.00 32.25  ? 755 HOH B O   1 
HETATM 5426 O  O   . HOH JA 7 .   ? 52.894 19.499  -25.895 1.00 33.35  ? 756 HOH B O   1 
HETATM 5427 O  O   . HOH JA 7 .   ? 35.719 -9.171  -10.945 1.00 30.86  ? 757 HOH B O   1 
HETATM 5428 O  O   . HOH JA 7 .   ? 49.941 -6.022  -42.115 1.00 24.60  ? 758 HOH B O   1 
HETATM 5429 O  O   . HOH JA 7 .   ? 60.655 8.657   7.929   1.00 34.04  ? 759 HOH B O   1 
HETATM 5430 O  O   . HOH JA 7 .   ? 32.395 -6.021  -27.273 1.00 36.05  ? 760 HOH B O   1 
HETATM 5431 O  O   . HOH JA 7 .   ? 60.844 17.708  -15.387 1.00 27.48  ? 761 HOH B O   1 
HETATM 5432 O  O   . HOH JA 7 .   ? 33.930 -15.962 -19.625 1.00 36.05  ? 762 HOH B O   1 
HETATM 5433 O  O   . HOH JA 7 .   ? 51.499 -18.136 -21.744 1.00 42.13  ? 763 HOH B O   1 
HETATM 5434 O  O   . HOH JA 7 .   ? 56.407 -15.916 -26.417 1.00 47.37  ? 764 HOH B O   1 
HETATM 5435 O  O   . HOH JA 7 .   ? 57.797 -8.539  -3.155  1.00 35.69  ? 765 HOH B O   1 
HETATM 5436 O  O   . HOH JA 7 .   ? 46.419 -19.260 -28.555 1.00 38.17  ? 766 HOH B O   1 
HETATM 5437 O  O   . HOH JA 7 .   ? 60.871 2.741   8.305   1.00 48.90  ? 767 HOH B O   1 
HETATM 5438 O  O   . HOH JA 7 .   ? 30.575 -11.998 -22.060 1.00 42.52  ? 768 HOH B O   1 
HETATM 5439 O  O   . HOH JA 7 .   ? 53.833 -17.518 -20.635 1.00 38.43  ? 769 HOH B O   1 
HETATM 5440 O  O   . HOH JA 7 .   ? 54.902 1.682   6.211   1.00 45.19  ? 770 HOH B O   1 
HETATM 5441 O  O   . HOH JA 7 .   ? 45.547 26.099  -20.118 1.00 52.77  ? 771 HOH B O   1 
HETATM 5442 O  O   . HOH JA 7 .   ? 41.056 -14.046 -1.323  1.00 33.26  ? 772 HOH B O   1 
HETATM 5443 O  O   . HOH JA 7 .   ? 34.250 -10.881 -31.181 1.00 26.42  ? 773 HOH B O   1 
HETATM 5444 O  O   . HOH JA 7 .   ? 72.148 0.916   -29.221 1.00 45.16  ? 774 HOH B O   1 
HETATM 5445 O  O   . HOH JA 7 .   ? 43.376 -18.155 -32.800 1.00 40.76  ? 775 HOH B O   1 
HETATM 5446 O  O   . HOH JA 7 .   ? 44.311 -5.987  -46.639 1.00 39.98  ? 776 HOH B O   1 
HETATM 5447 O  O   . HOH JA 7 .   ? 66.399 -5.558  -30.569 1.00 23.02  ? 777 HOH B O   1 
HETATM 5448 O  O   . HOH JA 7 .   ? 52.545 8.931   4.323   1.00 48.20  ? 778 HOH B O   1 
HETATM 5449 O  O   . HOH JA 7 .   ? 54.584 4.640   3.376   1.00 34.95  ? 779 HOH B O   1 
HETATM 5450 O  O   . HOH JA 7 .   ? 71.609 7.378   -25.027 1.00 31.16  ? 780 HOH B O   1 
HETATM 5451 O  O   . HOH JA 7 .   ? 64.762 -9.859  -29.809 1.00 30.30  ? 781 HOH B O   1 
HETATM 5452 O  O   . HOH JA 7 .   ? 54.921 -15.377 -22.104 1.00 30.65  ? 782 HOH B O   1 
HETATM 5453 O  O   . HOH JA 7 .   ? 67.781 1.344   -33.906 1.00 39.95  ? 783 HOH B O   1 
HETATM 5454 O  O   . HOH JA 7 .   ? 32.818 -7.274  -29.705 1.00 31.39  ? 784 HOH B O   1 
HETATM 5455 O  O   . HOH JA 7 .   ? 53.107 -2.406  4.026   1.00 46.70  ? 785 HOH B O   1 
HETATM 5456 O  O   . HOH JA 7 .   ? 50.389 6.046   3.448   1.00 43.11  ? 786 HOH B O   1 
HETATM 5457 O  O   . HOH JA 7 .   ? 69.671 -3.334  -28.462 1.00 35.98  ? 787 HOH B O   1 
HETATM 5458 O  O   . HOH JA 7 .   ? 33.989 -5.872  -31.808 1.00 25.20  ? 788 HOH B O   1 
HETATM 5459 O  O   . HOH JA 7 .   ? 44.561 8.233   -41.670 1.00 40.87  ? 789 HOH B O   1 
HETATM 5460 O  O   . HOH JA 7 .   ? 57.474 17.506  -21.433 1.00 29.78  ? 790 HOH B O   1 
HETATM 5461 O  O   . HOH JA 7 .   ? 42.538 -16.085 -1.684  1.00 43.83  ? 791 HOH B O   1 
HETATM 5462 O  O   . HOH JA 7 .   ? 72.604 6.879   -18.920 1.00 13.29  ? 792 HOH B O   1 
HETATM 5463 O  O   . HOH JA 7 .   ? 70.886 10.055  -24.606 1.00 36.21  ? 793 HOH B O   1 
HETATM 5464 O  O   . HOH JA 7 .   ? 31.516 -3.422  -29.954 1.00 48.53  ? 794 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . PRO A  4   ? 0.4091  0.4074 0.3013  0.0862  0.0018  0.0350  3   PRO A N   
2    C  CA  . PRO A  4   ? 0.5184  0.3276 0.3409  0.1142  -0.0562 -0.0377 3   PRO A CA  
3    C  C   . PRO A  4   ? 0.4309  0.3668 0.1782  0.1518  -0.0081 0.0575  3   PRO A C   
4    O  O   . PRO A  4   ? 0.3384  0.5554 0.3315  0.0220  0.0055  -0.0035 3   PRO A O   
5    C  CB  . PRO A  4   ? 0.4936  0.5190 0.2777  -0.0941 0.0825  -0.1059 3   PRO A CB  
6    C  CG  . PRO A  4   ? 0.6885  0.8529 0.5406  0.2037  0.2274  -0.1948 3   PRO A CG  
7    C  CD  . PRO A  4   ? 0.6361  0.5084 0.5809  0.2460  -0.0033 -0.1756 3   PRO A CD  
8    N  N   . ASP A  5   ? 0.4167  0.3675 0.2023  0.1016  0.0266  0.0218  4   ASP A N   
9    C  CA  . ASP A  5   ? 0.4630  0.3014 0.2163  0.0465  0.0343  -0.0710 4   ASP A CA  
10   C  C   . ASP A  5   ? 0.4785  0.2343 0.2260  0.0113  0.0929  -0.0555 4   ASP A C   
11   O  O   . ASP A  5   ? 0.4142  0.2705 0.2370  -0.0245 0.0739  -0.0746 4   ASP A O   
12   C  CB  . ASP A  5   ? 0.3255  0.4151 0.2283  0.0412  -0.0398 0.0129  4   ASP A CB  
13   C  CG  . ASP A  5   ? 0.2841  0.4641 0.1861  0.0187  0.0334  -0.0305 4   ASP A CG  
14   O  OD1 . ASP A  5   ? 0.3204  0.3176 0.1937  -0.0031 0.0150  -0.0356 4   ASP A OD1 
15   O  OD2 . ASP A  5   ? 0.3495  0.4590 0.4885  -0.0237 0.1151  -0.1256 4   ASP A OD2 
16   N  N   . TRP A  6   ? 0.2974  0.2479 0.1567  -0.0034 -0.0108 -0.0765 5   TRP A N   
17   C  CA  . TRP A  6   ? 0.2319  0.2454 0.1696  -0.0044 0.0414  -0.0770 5   TRP A CA  
18   C  C   . TRP A  6   ? 0.2669  0.1847 0.1355  -0.0082 -0.0055 -0.0479 5   TRP A C   
19   O  O   . TRP A  6   ? 0.3043  0.2059 0.1463  0.0065  -0.0150 -0.0422 5   TRP A O   
20   C  CB  . TRP A  6   ? 0.2379  0.1578 0.1804  0.0167  -0.0018 -0.0618 5   TRP A CB  
21   C  CG  . TRP A  6   ? 0.2195  0.1729 0.1115  0.0275  0.0226  -0.0245 5   TRP A CG  
22   C  CD1 . TRP A  6   ? 0.2064  0.1844 0.1181  0.0226  0.0092  -0.0148 5   TRP A CD1 
23   C  CD2 . TRP A  6   ? 0.2063  0.1524 0.1045  0.0311  -0.0210 -0.0328 5   TRP A CD2 
24   N  NE1 . TRP A  6   ? 0.2467  0.1657 0.1366  0.0168  -0.0035 -0.0204 5   TRP A NE1 
25   C  CE2 . TRP A  6   ? 0.2339  0.1509 0.1283  0.0252  -0.0273 -0.0078 5   TRP A CE2 
26   C  CE3 . TRP A  6   ? 0.1772  0.1786 0.1267  0.0099  -0.0200 -0.0292 5   TRP A CE3 
27   C  CZ2 . TRP A  6   ? 0.2357  0.1599 0.1351  0.0261  -0.0392 -0.0092 5   TRP A CZ2 
28   C  CZ3 . TRP A  6   ? 0.1750  0.1826 0.1186  0.0438  -0.0132 -0.0267 5   TRP A CZ3 
29   C  CH2 . TRP A  6   ? 0.1869  0.1668 0.1377  0.0167  -0.0370 0.0016  5   TRP A CH2 
30   N  N   . GLY A  7   ? 0.2145  0.2041 0.1307  0.0091  -0.0008 -0.0625 6   GLY A N   
31   C  CA  . GLY A  7   ? 0.2011  0.1984 0.1459  -0.0018 -0.0124 -0.0189 6   GLY A CA  
32   C  C   . GLY A  7   ? 0.1833  0.1549 0.1483  0.0190  -0.0122 -0.0419 6   GLY A C   
33   O  O   . GLY A  7   ? 0.1800  0.1628 0.1592  0.0218  -0.0200 -0.0378 6   GLY A O   
34   N  N   . TYR A  8   ? 0.1847  0.1524 0.1671  0.0114  -0.0147 -0.0679 7   TYR A N   
35   C  CA  . TYR A  8   ? 0.1707  0.1592 0.1948  -0.0107 0.0005  -0.0757 7   TYR A CA  
36   C  C   . TYR A  8   ? 0.1720  0.1793 0.2468  -0.0029 0.0103  -0.1128 7   TYR A C   
37   O  O   . TYR A  8   ? 0.2212  0.2117 0.2957  -0.0515 0.0375  -0.1436 7   TYR A O   
38   C  CB  . TYR A  8   ? 0.1671  0.1495 0.1919  -0.0159 -0.0096 -0.0867 7   TYR A CB  
39   C  CG  . TYR A  8   ? 0.1420  0.1402 0.1495  -0.0013 -0.0218 -0.0384 7   TYR A CG  
40   C  CD1 . TYR A  8   ? 0.1434  0.1128 0.1624  0.0192  -0.0234 -0.0451 7   TYR A CD1 
41   C  CD2 . TYR A  8   ? 0.1538  0.1271 0.1319  0.0178  -0.0201 -0.0402 7   TYR A CD2 
42   C  CE1 . TYR A  8   ? 0.1452  0.1115 0.1456  -0.0021 -0.0003 -0.0260 7   TYR A CE1 
43   C  CE2 . TYR A  8   ? 0.1333  0.1423 0.1146  0.0176  -0.0272 -0.0367 7   TYR A CE2 
44   C  CZ  . TYR A  8   ? 0.1186  0.1207 0.1067  0.0114  -0.0147 -0.0326 7   TYR A CZ  
45   O  OH  . TYR A  8   ? 0.1316  0.1153 0.1181  0.0092  -0.0187 -0.0146 7   TYR A OH  
46   N  N   . ASP A  9   ? 0.2260  0.1826 0.2526  -0.0207 -0.0559 -0.1018 8   ASP A N   
47   C  CA  . ASP A  9   ? 0.2336  0.2253 0.3316  -0.0373 -0.0806 -0.1533 8   ASP A CA  
48   C  C   . ASP A  9   ? 0.2235  0.1914 0.3312  -0.0321 -0.0111 -0.1094 8   ASP A C   
49   O  O   . ASP A  9   ? 0.2368  0.2117 0.3287  -0.0195 -0.0173 -0.1182 8   ASP A O   
50   C  CB  . ASP A  9   ? 0.3097  0.2762 0.3898  -0.0435 -0.0908 -0.1189 8   ASP A CB  
51   C  CG  . ASP A  9   ? 0.3693  0.5743 0.4504  -0.1460 -0.0769 -0.0872 8   ASP A CG  
52   O  OD1 . ASP A  9   ? 0.5493  0.5137 0.5074  -0.1294 -0.0977 -0.2276 8   ASP A OD1 
53   O  OD2 . ASP A  9   ? 0.7228  0.6128 0.3843  0.1649  -0.2307 -0.2344 8   ASP A OD2 
54   N  N   . ASP A  10  ? 0.2579  0.2260 0.3778  -0.0657 -0.0182 -0.1088 9   ASP A N   
55   C  CA  . ASP A  10  ? 0.3513  0.2260 0.3829  -0.0436 0.0111  -0.0447 9   ASP A CA  
56   C  C   . ASP A  10  ? 0.4390  0.2863 0.2781  0.0069  -0.0040 -0.0946 9   ASP A C   
57   O  O   . ASP A  10  ? 0.4081  0.4381 0.3136  0.0929  -0.0540 -0.0920 9   ASP A O   
58   C  CB  . ASP A  10  ? 0.4288  0.2303 0.5930  -0.1139 0.0908  -0.0763 9   ASP A CB  
59   C  CG  . ASP A  10  ? 0.3229  0.6256 0.6019  0.1768  0.0917  0.2188  9   ASP A CG  
60   O  OD1 . ASP A  10  ? 0.8390  0.9587 0.5973  0.0466  0.0638  0.2356  9   ASP A OD1 
61   O  OD2 . ASP A  10  ? 0.3779  1.2508 1.0117  0.0456  0.0111  0.2085  9   ASP A OD2 
62   N  N   . LYS A  11  ? 0.3858  0.2242 0.2590  -0.0844 0.0021  -0.1337 10  LYS A N   
63   C  CA  . LYS A  11  ? 0.3740  0.2522 0.3175  -0.0339 -0.0055 -0.1267 10  LYS A CA  
64   C  C   . LYS A  11  ? 0.3028  0.2071 0.2242  -0.0040 -0.0076 -0.1114 10  LYS A C   
65   O  O   . LYS A  11  ? 0.3376  0.2795 0.3901  -0.0023 0.0337  -0.1876 10  LYS A O   
66   C  CB  . LYS A  11  ? 0.5255  0.3671 0.3276  -0.0419 -0.0837 -0.1600 10  LYS A CB  
67   N  N   . ASN A  12  ? 0.3190  0.1890 0.1592  0.0055  -0.0173 -0.0890 11  ASN A N   
68   C  CA  . ASN A  12  ? 0.2848  0.2177 0.1804  0.0151  -0.0354 -0.0998 11  ASN A CA  
69   C  C   . ASN A  12  ? 0.1932  0.1829 0.1556  0.0105  -0.0093 -0.0690 11  ASN A C   
70   O  O   . ASN A  12  ? 0.2274  0.1797 0.1574  0.0062  -0.0124 -0.0577 11  ASN A O   
71   C  CB  . ASN A  12  ? 0.3107  0.2023 0.1689  0.0033  -0.0265 -0.0809 11  ASN A CB  
72   C  CG  . ASN A  12  ? 0.3581  0.2285 0.1650  0.0266  -0.0447 -0.1018 11  ASN A CG  
73   O  OD1 . ASN A  12  ? 0.2644  0.2327 0.1951  0.0268  -0.0434 -0.0908 11  ASN A OD1 
74   N  ND2 . ASN A  12  ? 0.4443  0.2522 0.2217  0.0502  -0.1039 -0.0444 11  ASN A ND2 
75   N  N   . GLY A  13  ? 0.2442  0.1835 0.1481  0.0244  -0.0005 -0.0542 12  GLY A N   
76   C  CA  . GLY A  13  ? 0.2454  0.1840 0.1323  0.0446  -0.0159 -0.0499 12  GLY A CA  
77   C  C   . GLY A  13  ? 0.2102  0.1416 0.1703  -0.0008 0.0140  -0.0407 12  GLY A C   
78   O  O   . GLY A  13  ? 0.1948  0.1653 0.1808  0.0122  0.0033  -0.0441 12  GLY A O   
79   N  N   . PRO A  14  ? 0.1714  0.1506 0.1549  -0.0017 0.0184  -0.0366 13  PRO A N   
80   C  CA  . PRO A  14  ? 0.1606  0.1641 0.1398  -0.0073 0.0065  -0.0097 13  PRO A CA  
81   C  C   . PRO A  14  ? 0.1894  0.1531 0.1531  -0.0215 -0.0063 -0.0216 13  PRO A C   
82   O  O   . PRO A  14  ? 0.1768  0.1416 0.1937  -0.0053 -0.0159 -0.0227 13  PRO A O   
83   C  CB  . PRO A  14  ? 0.1894  0.1743 0.1829  -0.0126 0.0388  -0.0320 13  PRO A CB  
84   C  CG  . PRO A  14  ? 0.1854  0.1980 0.1531  -0.0055 0.0080  -0.0456 13  PRO A CG  
85   C  CD  . PRO A  14  ? 0.1592  0.1991 0.1926  0.0273  0.0026  -0.0657 13  PRO A CD  
86   N  N   . GLU A  15  ? 0.1930  0.1531 0.1912  -0.0243 0.0035  -0.0089 14  GLU A N   
87   C  CA  . GLU A  15  ? 0.2275  0.1483 0.2497  -0.0293 0.0436  -0.0156 14  GLU A CA  
88   C  C   . GLU A  15  ? 0.2048  0.1459 0.2698  -0.0016 -0.0004 -0.0344 14  GLU A C   
89   O  O   . GLU A  15  ? 0.2763  0.1513 0.4034  0.0126  0.0066  -0.0189 14  GLU A O   
90   C  CB  . GLU A  15  ? 0.2547  0.1738 0.2823  -0.0527 0.0579  -0.0018 14  GLU A CB  
91   C  CG  . GLU A  15  ? 0.3272  0.3100 0.2989  -0.0914 0.1213  -0.0568 14  GLU A CG  
92   C  CD  . GLU A  15  ? 0.6005  0.2514 0.3273  -0.0209 -0.0234 -0.0593 14  GLU A CD  
93   O  OE1 . GLU A  15  ? 0.3851  0.2594 0.3740  -0.0058 0.0198  -0.0604 14  GLU A OE1 
94   O  OE2 . GLU A  15  ? 0.5654  0.4141 0.3722  -0.0450 -0.0174 0.0241  14  GLU A OE2 
95   N  N   . GLN A  16  ? 0.2053  0.1606 0.2405  -0.0095 0.0104  -0.0696 15  GLN A N   
96   C  CA  . GLN A  16  ? 0.1847  0.2054 0.2874  -0.0241 0.0199  -0.0967 15  GLN A CA  
97   C  C   . GLN A  16  ? 0.1969  0.1506 0.2266  0.0083  0.0311  -0.0737 15  GLN A C   
98   O  O   . GLN A  16  ? 0.2016  0.1833 0.2206  0.0106  0.0062  -0.0939 15  GLN A O   
99   C  CB  . GLN A  16  ? 0.2138  0.2217 0.3269  0.0285  -0.0182 -0.0893 15  GLN A CB  
100  C  CG  . GLN A  16  ? 0.3426  0.2673 0.3832  -0.0687 -0.0495 -0.1087 15  GLN A CG  
101  C  CD  . GLN A  16  ? 0.2694  0.2967 0.6687  -0.0253 -0.0156 -0.1065 15  GLN A CD  
102  O  OE1 . GLN A  16  ? 0.4738  0.4049 0.6900  -0.1490 -0.0466 0.0098  15  GLN A OE1 
103  N  NE2 . GLN A  16  ? 0.3668  0.2960 0.6652  -0.0779 0.0125  -0.2150 15  GLN A NE2 
104  N  N   . TRP A  17  ? 0.1786  0.1319 0.1984  -0.0018 0.0078  -0.0635 16  TRP A N   
105  C  CA  . TRP A  17  ? 0.1718  0.1380 0.1872  0.0217  0.0335  -0.0497 16  TRP A CA  
106  C  C   . TRP A  17  ? 0.1817  0.1258 0.2005  0.0218  0.0367  -0.0518 16  TRP A C   
107  O  O   . TRP A  17  ? 0.1703  0.1646 0.1847  0.0152  0.0281  -0.0510 16  TRP A O   
108  C  CB  . TRP A  17  ? 0.1689  0.1366 0.1793  0.0132  0.0024  -0.0526 16  TRP A CB  
109  C  CG  . TRP A  17  ? 0.1538  0.1301 0.1181  0.0027  0.0040  -0.0198 16  TRP A CG  
110  C  CD1 . TRP A  17  ? 0.1671  0.1294 0.1416  -0.0038 0.0079  -0.0229 16  TRP A CD1 
111  C  CD2 . TRP A  17  ? 0.1481  0.1280 0.1362  -0.0078 -0.0008 -0.0205 16  TRP A CD2 
112  N  NE1 . TRP A  17  ? 0.1932  0.1535 0.1164  0.0221  -0.0110 -0.0434 16  TRP A NE1 
113  C  CE2 . TRP A  17  ? 0.1477  0.1380 0.1171  -0.0097 0.0073  -0.0274 16  TRP A CE2 
114  C  CE3 . TRP A  17  ? 0.1430  0.1038 0.1377  -0.0292 0.0173  -0.0255 16  TRP A CE3 
115  C  CZ2 . TRP A  17  ? 0.1624  0.1348 0.1119  -0.0083 0.0110  -0.0277 16  TRP A CZ2 
116  C  CZ3 . TRP A  17  ? 0.1571  0.1162 0.1441  0.0024  0.0217  -0.0081 16  TRP A CZ3 
117  C  CH2 . TRP A  17  ? 0.1405  0.1386 0.1137  -0.0022 0.0084  -0.0288 16  TRP A CH2 
118  N  N   . SER A  18  ? 0.1901  0.1076 0.1993  0.0118  0.0215  -0.0496 17  SER A N   
119  C  CA  . SER A  18  ? 0.1711  0.1553 0.1800  0.0206  0.0099  -0.0563 17  SER A CA  
120  C  C   . SER A  18  ? 0.1779  0.1319 0.2170  0.0084  0.0488  -0.0473 17  SER A C   
121  O  O   . SER A  18  ? 0.1817  0.1829 0.2497  0.0208  0.0423  -0.0516 17  SER A O   
122  C  CB  . SER A  18  ? 0.2142  0.1373 0.2127  0.0135  0.0044  -0.0239 17  SER A CB  
123  O  OG  . SER A  18  ? 0.2601  0.1483 0.2799  0.0092  0.0274  -0.0383 17  SER A OG  
124  N  N   . LYS A  19  ? 0.2479  0.1465 0.2253  0.0019  0.0199  -0.0732 18  LYS A N   
125  C  CA  . LYS A  19  ? 0.2529  0.1707 0.2411  -0.0243 0.0469  -0.0990 18  LYS A CA  
126  C  C   . LYS A  19  ? 0.2328  0.1865 0.2181  0.0328  0.0229  -0.0941 18  LYS A C   
127  O  O   . LYS A  19  ? 0.2479  0.2381 0.2687  0.0136  0.0569  -0.0886 18  LYS A O   
128  C  CB  . LYS A  19  ? 0.2339  0.2030 0.2204  0.0121  0.0476  -0.0872 18  LYS A CB  
129  C  CG  . LYS A  19  ? 0.2722  0.2283 0.3746  -0.0490 0.0237  -0.0768 18  LYS A CG  
130  C  CD  . LYS A  19  ? 0.4656  0.3319 0.4785  -0.1353 -0.0950 -0.1156 18  LYS A CD  
131  C  CE  . LYS A  19  ? 0.4748  0.3079 0.4357  -0.0225 -0.0882 -0.1005 18  LYS A CE  
132  N  NZ  . LYS A  19  ? 0.5732  0.4284 0.6880  0.0185  -0.2030 -0.2123 18  LYS A NZ  
133  N  N   . LEU A  20  ? 0.2770  0.1908 0.1912  -0.0009 0.0535  -0.0442 19  LEU A N   
134  C  CA  . LEU A  20  ? 0.2630  0.2073 0.1632  0.0082  0.0488  -0.0621 19  LEU A CA  
135  C  C   . LEU A  20  ? 0.2604  0.1761 0.1653  0.0018  0.0715  -0.0253 19  LEU A C   
136  O  O   . LEU A  20  ? 0.2486  0.2041 0.1562  0.0147  0.0750  -0.0220 19  LEU A O   
137  C  CB  . LEU A  20  ? 0.2551  0.2160 0.1865  -0.0256 0.0098  -0.0375 19  LEU A CB  
138  C  CG  . LEU A  20  ? 0.4250  0.3369 0.2339  0.0210  -0.0739 -0.0904 19  LEU A CG  
139  C  CD1 . LEU A  20  ? 0.6491  0.4629 0.2755  0.0992  -0.1931 -0.0781 19  LEU A CD1 
140  C  CD2 . LEU A  20  ? 0.4859  0.7590 0.2238  -0.1630 0.0978  -0.2286 19  LEU A CD2 
141  N  N   . TYR A  21  ? 0.2030  0.1750 0.1391  0.0166  0.0447  -0.0245 20  TYR A N   
142  C  CA  . TYR A  21  ? 0.1991  0.1535 0.1520  0.0060  0.0251  -0.0427 20  TYR A CA  
143  C  C   . TYR A  21  ? 0.1668  0.1603 0.1386  0.0135  0.0357  -0.0328 20  TYR A C   
144  O  O   . TYR A  21  ? 0.1635  0.1592 0.1693  0.0062  0.0633  -0.0429 20  TYR A O   
145  C  CB  . TYR A  21  ? 0.2188  0.1707 0.1562  0.0311  0.0681  -0.0073 20  TYR A CB  
146  C  CG  . TYR A  21  ? 0.2239  0.1793 0.1197  0.0173  0.0635  -0.0443 20  TYR A CG  
147  C  CD1 . TYR A  21  ? 0.2382  0.2071 0.1610  0.0247  0.0640  0.0046  20  TYR A CD1 
148  C  CD2 . TYR A  21  ? 0.2436  0.2206 0.1520  0.0828  0.0256  -0.0622 20  TYR A CD2 
149  C  CE1 . TYR A  21  ? 0.2048  0.2221 0.1912  0.0341  0.0603  0.0027  20  TYR A CE1 
150  C  CE2 . TYR A  21  ? 0.2465  0.2500 0.1657  0.0287  0.0493  -0.0330 20  TYR A CE2 
151  C  CZ  . TYR A  21  ? 0.1998  0.2547 0.1402  0.0383  0.0315  -0.0071 20  TYR A CZ  
152  O  OH  . TYR A  21  ? 0.3219  0.2970 0.1675  0.0319  0.0148  0.0185  20  TYR A OH  
153  N  N   . PRO A  22  ? 0.1844  0.1470 0.1761  0.0276  0.0625  -0.0211 21  PRO A N   
154  C  CA  . PRO A  22  ? 0.2055  0.1685 0.1628  0.0449  0.0480  -0.0388 21  PRO A CA  
155  C  C   . PRO A  22  ? 0.1520  0.1560 0.1610  0.0243  0.0641  -0.0186 21  PRO A C   
156  O  O   . PRO A  22  ? 0.2091  0.1585 0.1596  0.0277  0.0616  -0.0151 21  PRO A O   
157  C  CB  . PRO A  22  ? 0.2282  0.1980 0.1976  0.0763  0.0871  -0.0297 21  PRO A CB  
158  C  CG  . PRO A  22  ? 0.2680  0.2117 0.2138  0.0831  0.1150  -0.0082 21  PRO A CG  
159  C  CD  . PRO A  22  ? 0.2389  0.1790 0.1908  0.0491  0.1053  -0.0261 21  PRO A CD  
160  N  N   . ILE A  23  ? 0.1632  0.1305 0.2132  0.0060  0.0268  -0.0458 22  ILE A N   
161  C  CA  . ILE A  23  ? 0.1452  0.1330 0.1987  0.0109  0.0500  -0.0281 22  ILE A CA  
162  C  C   . ILE A  23  ? 0.1351  0.1305 0.1621  0.0175  0.0153  -0.0122 22  ILE A C   
163  O  O   . ILE A  23  ? 0.1700  0.1456 0.1538  0.0161  0.0064  -0.0081 22  ILE A O   
164  C  CB  . ILE A  23  ? 0.1624  0.1405 0.1797  0.0051  0.0512  -0.0135 22  ILE A CB  
165  C  CG1 . ILE A  23  ? 0.1682  0.2134 0.1822  -0.0150 0.0321  -0.0348 22  ILE A CG1 
166  C  CG2 . ILE A  23  ? 0.1883  0.1438 0.2352  -0.0080 0.0133  -0.0038 22  ILE A CG2 
167  C  CD1 . ILE A  23  ? 0.1858  0.3384 0.2380  0.0620  0.0017  -0.0902 22  ILE A CD1 
168  N  N   . ALA A  24  ? 0.1430  0.1208 0.1603  0.0087  0.0291  -0.0330 23  ALA A N   
169  C  CA  . ALA A  24  ? 0.1635  0.1348 0.1531  -0.0029 0.0489  0.0063  23  ALA A CA  
170  C  C   . ALA A  24  ? 0.1657  0.1316 0.1553  0.0012  0.0474  -0.0060 23  ALA A C   
171  O  O   . ALA A  24  ? 0.1671  0.1412 0.1391  0.0122  0.0315  -0.0011 23  ALA A O   
172  C  CB  . ALA A  24  ? 0.1553  0.1221 0.1664  0.0038  0.0293  -0.0305 23  ALA A CB  
173  N  N   . ASN A  25  ? 0.1764  0.1416 0.1596  0.0119  0.0205  -0.0234 24  ASN A N   
174  C  CA  . ASN A  25  ? 0.1912  0.1535 0.1434  0.0099  0.0148  -0.0219 24  ASN A CA  
175  C  C   . ASN A  25  ? 0.2161  0.1056 0.1610  0.0209  0.0297  -0.0086 24  ASN A C   
176  O  O   . ASN A  25  ? 0.2318  0.1283 0.2106  0.0271  0.0023  0.0196  24  ASN A O   
177  C  CB  . ASN A  25  ? 0.2885  0.1822 0.1074  0.0108  0.0265  0.0263  24  ASN A CB  
178  C  CG  . ASN A  25  ? 0.2989  0.1007 0.2730  0.0030  -0.0006 -0.0615 24  ASN A CG  
179  O  OD1 . ASN A  25  ? 0.4389  0.1858 0.2838  0.0403  -0.0058 -0.0631 24  ASN A OD1 
180  N  ND2 . ASN A  25  ? 0.2005  0.2687 0.2852  -0.0438 -0.0621 -0.0551 24  ASN A ND2 
181  N  N   . GLY A  26  ? 0.2016  0.1141 0.1757  0.0141  0.0286  -0.0197 25  GLY A N   
182  C  CA  . GLY A  26  ? 0.1678  0.1993 0.1412  0.0048  -0.0089 -0.0026 25  GLY A CA  
183  C  C   . GLY A  26  ? 0.1844  0.1137 0.1606  0.0245  0.0255  0.0190  25  GLY A C   
184  O  O   . GLY A  26  ? 0.1912  0.1368 0.1764  0.0313  0.0294  0.0082  25  GLY A O   
185  N  N   . ASN A  27  ? 0.1768  0.1120 0.1890  0.0450  -0.0207 0.0038  26  ASN A N   
186  C  CA  . ASN A  27  ? 0.2152  0.1416 0.1474  0.0705  -0.0260 0.0067  26  ASN A CA  
187  C  C   . ASN A  27  ? 0.1427  0.1344 0.1581  0.0491  -0.0283 0.0089  26  ASN A C   
188  O  O   . ASN A  27  ? 0.2364  0.1592 0.1434  0.0754  -0.0069 0.0119  26  ASN A O   
189  C  CB  . ASN A  27  ? 0.2447  0.2070 0.1894  0.1441  -0.0290 0.0054  26  ASN A CB  
190  C  CG  . ASN A  27  ? 0.2612  0.2389 0.3097  0.1201  0.0016  0.0562  26  ASN A CG  
191  O  OD1 . ASN A  27  ? 0.3377  0.1951 0.2763  0.1068  -0.0117 0.0530  26  ASN A OD1 
192  N  ND2 . ASN A  27  ? 0.3129  0.2953 0.4117  0.1957  -0.0153 -0.0414 26  ASN A ND2 
193  N  N   A ASN A  28  ? 0.0955  0.0994 0.1764  0.0230  0.0035  0.0163  27  ASN A N   
194  N  N   B ASN A  28  ? 0.1527  0.1120 0.1420  0.0234  0.0048  0.0139  27  ASN A N   
195  C  CA  A ASN A  28  ? 0.1178  0.1076 0.1040  0.0234  -0.0188 0.0008  27  ASN A CA  
196  C  CA  B ASN A  28  ? 0.1120  0.1128 0.1725  0.0293  -0.0046 0.0182  27  ASN A CA  
197  C  C   A ASN A  28  ? 0.1268  0.0829 0.1312  0.0417  -0.0116 0.0004  27  ASN A C   
198  C  C   B ASN A  28  ? 0.1301  0.1247 0.1368  0.0277  -0.0042 -0.0015 27  ASN A C   
199  O  O   A ASN A  28  ? 0.1138  0.0759 0.1047  0.0294  0.0127  -0.0012 27  ASN A O   
200  O  O   B ASN A  28  ? 0.1337  0.1294 0.1567  0.0312  -0.0051 0.0179  27  ASN A O   
201  C  CB  A ASN A  28  ? 0.1146  0.1305 0.2020  0.0093  -0.0557 0.0239  27  ASN A CB  
202  C  CB  B ASN A  28  ? 0.1242  0.1499 0.1395  0.0086  0.0495  -0.0027 27  ASN A CB  
203  C  CG  A ASN A  28  ? 0.0776  0.1506 0.1966  0.0243  -0.0259 -0.0214 27  ASN A CG  
204  C  CG  B ASN A  28  ? 0.1535  0.2885 0.2469  0.0102  -0.0066 0.0629  27  ASN A CG  
205  O  OD1 A ASN A  28  ? 0.1294  0.2697 0.3779  0.1083  -0.0234 -0.0024 27  ASN A OD1 
206  O  OD1 B ASN A  28  ? 0.1181  0.3761 0.2362  -0.0109 -0.0221 0.0423  27  ASN A OD1 
207  N  ND2 A ASN A  28  ? 0.1678  0.3758 0.2540  0.1130  -0.0907 -0.1504 27  ASN A ND2 
208  N  ND2 B ASN A  28  ? 0.2389  0.1879 0.3488  -0.0221 0.0476  0.0052  27  ASN A ND2 
209  N  N   . GLN A  29  ? 0.1222  0.1177 0.1099  0.0236  0.0004  -0.0082 28  GLN A N   
210  C  CA  . GLN A  29  ? 0.1102  0.1119 0.1172  0.0225  -0.0030 -0.0047 28  GLN A CA  
211  C  C   . GLN A  29  ? 0.1216  0.1067 0.0944  0.0094  0.0075  0.0127  28  GLN A C   
212  O  O   . GLN A  29  ? 0.1254  0.1241 0.1029  0.0276  0.0046  0.0118  28  GLN A O   
213  C  CB  . GLN A  29  ? 0.1402  0.1032 0.1240  0.0040  0.0216  -0.0069 28  GLN A CB  
214  C  CG  . GLN A  29  ? 0.1323  0.1152 0.1341  0.0211  0.0237  0.0061  28  GLN A CG  
215  C  CD  . GLN A  29  ? 0.1179  0.1067 0.1156  0.0248  0.0055  -0.0060 28  GLN A CD  
216  O  OE1 . GLN A  29  ? 0.1274  0.1276 0.1280  0.0179  0.0192  0.0054  28  GLN A OE1 
217  N  NE2 . GLN A  29  ? 0.1492  0.1120 0.1267  0.0150  0.0281  -0.0092 28  GLN A NE2 
218  N  N   . SER A  30  ? 0.1098  0.0962 0.1068  0.0154  -0.0163 0.0051  29  SER A N   
219  C  CA  . SER A  30  ? 0.1058  0.0977 0.1247  0.0207  -0.0038 0.0025  29  SER A CA  
220  C  C   . SER A  30  ? 0.0916  0.0950 0.0937  -0.0013 0.0075  0.0128  29  SER A C   
221  O  O   . SER A  30  ? 0.1294  0.1083 0.1005  0.0063  0.0067  0.0054  29  SER A O   
222  C  CB  . SER A  30  ? 0.1097  0.0973 0.0952  -0.0012 -0.0076 0.0106  29  SER A CB  
223  O  OG  . SER A  30  ? 0.1022  0.1147 0.0996  0.0018  0.0019  0.0116  29  SER A OG  
224  N  N   . PRO A  31  ? 0.0985  0.0993 0.0882  -0.0009 0.0073  0.0111  30  PRO A N   
225  C  CA  . PRO A  31  ? 0.1053  0.1072 0.0889  0.0125  0.0079  0.0109  30  PRO A CA  
226  C  C   . PRO A  31  ? 0.1155  0.0962 0.1137  0.0107  -0.0047 0.0120  30  PRO A C   
227  O  O   . PRO A  31  ? 0.1208  0.0969 0.1199  0.0105  -0.0013 0.0125  30  PRO A O   
228  C  CB  . PRO A  31  ? 0.1111  0.0989 0.1199  0.0124  -0.0086 0.0043  30  PRO A CB  
229  C  CG  . PRO A  31  ? 0.1172  0.1040 0.1117  -0.0013 0.0030  0.0025  30  PRO A CG  
230  C  CD  . PRO A  31  ? 0.0969  0.1147 0.1270  -0.0129 0.0005  0.0040  30  PRO A CD  
231  N  N   . VAL A  32  ? 0.1144  0.1038 0.0914  0.0071  0.0042  0.0105  31  VAL A N   
232  C  CA  . VAL A  32  ? 0.1189  0.1145 0.0953  0.0052  -0.0062 0.0211  31  VAL A CA  
233  C  C   . VAL A  32  ? 0.1326  0.0910 0.1092  0.0023  -0.0019 0.0142  31  VAL A C   
234  O  O   . VAL A  32  ? 0.1366  0.1092 0.1106  0.0100  0.0001  0.0190  31  VAL A O   
235  C  CB  . VAL A  32  ? 0.1222  0.1199 0.1137  0.0195  -0.0031 0.0156  31  VAL A CB  
236  C  CG1 . VAL A  32  ? 0.1283  0.1492 0.1416  0.0195  0.0168  0.0256  31  VAL A CG1 
237  C  CG2 . VAL A  32  ? 0.1495  0.1294 0.1235  -0.0042 -0.0130 0.0120  31  VAL A CG2 
238  N  N   . ASP A  33  ? 0.1398  0.1032 0.0987  -0.0157 0.0010  0.0181  32  ASP A N   
239  C  CA  . ASP A  33  ? 0.1373  0.1124 0.1041  -0.0038 -0.0006 0.0154  32  ASP A CA  
240  C  C   . ASP A  33  ? 0.1234  0.1412 0.0858  0.0116  -0.0059 0.0273  32  ASP A C   
241  O  O   . ASP A  33  ? 0.1685  0.1768 0.1438  0.0370  -0.0388 0.0031  32  ASP A O   
242  C  CB  . ASP A  33  ? 0.1438  0.1326 0.1445  -0.0179 0.0240  0.0368  32  ASP A CB  
243  C  CG  . ASP A  33  ? 0.1477  0.1344 0.1351  0.0160  0.0127  0.0400  32  ASP A CG  
244  O  OD1 . ASP A  33  ? 0.1477  0.1456 0.1283  0.0019  0.0145  0.0430  32  ASP A OD1 
245  O  OD2 . ASP A  33  ? 0.2325  0.2547 0.1635  0.0690  0.0555  0.0894  32  ASP A OD2 
246  N  N   . ILE A  34  ? 0.1402  0.1196 0.1056  0.0043  -0.0027 0.0148  33  ILE A N   
247  C  CA  . ILE A  34  ? 0.1420  0.1391 0.1011  -0.0006 0.0061  0.0044  33  ILE A CA  
248  C  C   . ILE A  34  ? 0.1333  0.1499 0.0988  0.0072  0.0015  0.0076  33  ILE A C   
249  O  O   . ILE A  34  ? 0.1289  0.1614 0.1216  -0.0040 0.0050  0.0238  33  ILE A O   
250  C  CB  . ILE A  34  ? 0.1441  0.1366 0.1111  -0.0055 0.0089  0.0157  33  ILE A CB  
251  C  CG1 . ILE A  34  ? 0.1556  0.1427 0.1362  -0.0044 -0.0054 0.0326  33  ILE A CG1 
252  C  CG2 . ILE A  34  ? 0.1635  0.1930 0.1172  -0.0369 0.0001  -0.0030 33  ILE A CG2 
253  C  CD1 . ILE A  34  ? 0.2143  0.1298 0.1678  -0.0107 0.0238  0.0141  33  ILE A CD1 
254  N  N   . LYS A  35  ? 0.1560  0.1599 0.1031  -0.0054 -0.0096 0.0298  34  LYS A N   
255  C  CA  . LYS A  35  ? 0.1817  0.1757 0.1194  -0.0071 0.0009  0.0545  34  LYS A CA  
256  C  C   . LYS A  35  ? 0.1599  0.1919 0.1243  -0.0100 -0.0171 0.0662  34  LYS A C   
257  O  O   . LYS A  35  ? 0.1664  0.2382 0.1289  -0.0225 -0.0066 0.0674  34  LYS A O   
258  C  CB  . LYS A  35  ? 0.2271  0.1847 0.1847  -0.0061 0.0158  0.0641  34  LYS A CB  
259  C  CG  . LYS A  35  ? 0.3358  0.2877 0.2132  0.0055  -0.0207 -0.0273 34  LYS A CG  
260  C  CD  . LYS A  35  ? 0.4205  0.3984 0.4767  0.1648  -0.0272 0.1455  34  LYS A CD  
261  C  CE  . LYS A  35  ? 0.9437  0.3639 0.4638  0.1272  0.1418  0.2127  34  LYS A CE  
262  N  NZ  . LYS A  35  ? 0.8346  0.2246 0.8840  0.0854  -0.1919 -0.0491 34  LYS A NZ  
263  N  N   . THR A  36  ? 0.1685  0.2023 0.1225  -0.0253 -0.0097 0.0337  35  THR A N   
264  C  CA  . THR A  36  ? 0.1757  0.2228 0.1470  -0.0357 -0.0151 0.0323  35  THR A CA  
265  C  C   . THR A  36  ? 0.2264  0.2415 0.1199  -0.0501 -0.0348 0.0125  35  THR A C   
266  O  O   . THR A  36  ? 0.2874  0.2406 0.1675  -0.0251 -0.0762 0.0065  35  THR A O   
267  C  CB  . THR A  36  ? 0.1890  0.2309 0.1603  -0.0226 -0.0166 0.0157  35  THR A CB  
268  O  OG1 . THR A  36  ? 0.1905  0.2716 0.1445  -0.0108 0.0009  0.0027  35  THR A OG1 
269  C  CG2 . THR A  36  ? 0.2723  0.2543 0.1858  -0.0458 -0.0510 0.0673  35  THR A CG2 
270  N  N   . SER A  37  ? 0.1955  0.2946 0.1027  -0.0463 -0.0127 0.0637  36  SER A N   
271  C  CA  . SER A  37  ? 0.1984  0.3219 0.1743  -0.0399 -0.0300 0.0863  36  SER A CA  
272  C  C   . SER A  37  ? 0.2045  0.2521 0.1427  -0.0050 -0.0355 0.0826  36  SER A C   
273  O  O   . SER A  37  ? 0.2465  0.3836 0.1298  0.0125  -0.0324 0.0952  36  SER A O   
274  C  CB  . SER A  37  ? 0.2784  0.3072 0.1876  -0.0405 -0.0289 0.1092  36  SER A CB  
275  O  OG  . SER A  37  ? 0.2709  0.3000 0.2278  -0.0710 -0.0177 0.0920  36  SER A OG  
276  N  N   A GLU A  38  ? 0.2073  0.1991 0.1319  -0.0425 -0.0023 0.0664  37  GLU A N   
277  N  N   B GLU A  38  ? 0.2095  0.2005 0.1276  -0.0418 -0.0060 0.0710  37  GLU A N   
278  C  CA  A GLU A  38  ? 0.1969  0.1840 0.1492  -0.0212 -0.0230 0.0649  37  GLU A CA  
279  C  CA  B GLU A  38  ? 0.2077  0.1861 0.1685  -0.0313 0.0037  0.0532  37  GLU A CA  
280  C  C   A GLU A  38  ? 0.1750  0.1678 0.1262  -0.0111 -0.0395 0.0523  37  GLU A C   
281  C  C   B GLU A  38  ? 0.1786  0.1664 0.1283  -0.0117 -0.0318 0.0551  37  GLU A C   
282  O  O   A GLU A  38  ? 0.1829  0.1926 0.1560  -0.0015 -0.0518 0.0653  37  GLU A O   
283  O  O   B GLU A  38  ? 0.1829  0.1926 0.1574  -0.0025 -0.0524 0.0635  37  GLU A O   
284  C  CB  A GLU A  38  ? 0.2375  0.1671 0.1914  -0.0104 -0.0432 0.0697  37  GLU A CB  
285  C  CB  B GLU A  38  ? 0.2977  0.1736 0.1840  -0.0239 0.0048  0.0590  37  GLU A CB  
286  C  CG  A GLU A  38  ? 0.3499  0.1578 0.2604  -0.0343 -0.0798 0.1073  37  GLU A CG  
287  C  CG  B GLU A  38  ? 0.3459  0.2127 0.3193  -0.0534 0.0462  0.0583  37  GLU A CG  
288  C  CD  A GLU A  38  ? 0.4566  0.1614 0.4601  -0.0161 -0.0891 0.0607  37  GLU A CD  
289  C  CD  B GLU A  38  ? 0.3840  0.2275 0.3197  -0.0474 0.0629  0.0714  37  GLU A CD  
290  O  OE1 A GLU A  38  ? 0.4401  0.4023 0.5825  0.0726  -0.0923 0.0652  37  GLU A OE1 
291  O  OE1 B GLU A  38  ? 0.4598  0.3643 0.3237  0.1733  0.0737  0.1371  37  GLU A OE1 
292  O  OE2 A GLU A  38  ? 0.6606  0.3308 0.6993  -0.1397 -0.1759 0.2669  37  GLU A OE2 
293  O  OE2 B GLU A  38  ? 0.5687  0.2497 0.2514  -0.0859 0.1035  0.0500  37  GLU A OE2 
294  N  N   . THR A  39  ? 0.1844  0.1481 0.1172  -0.0173 -0.0286 0.0586  38  THR A N   
295  C  CA  . THR A  39  ? 0.1502  0.1492 0.1089  -0.0152 -0.0125 0.0141  38  THR A CA  
296  C  C   . THR A  39  ? 0.1678  0.1761 0.0831  -0.0198 -0.0182 0.0416  38  THR A C   
297  O  O   . THR A  39  ? 0.2109  0.2089 0.1084  -0.0359 -0.0223 0.0421  38  THR A O   
298  C  CB  . THR A  39  ? 0.1628  0.1617 0.0867  0.0124  -0.0116 0.0287  38  THR A CB  
299  O  OG1 . THR A  39  ? 0.1736  0.1962 0.1111  -0.0067 -0.0023 0.0161  38  THR A OG1 
300  C  CG2 . THR A  39  ? 0.1520  0.1689 0.1082  -0.0065 -0.0250 0.0296  38  THR A CG2 
301  N  N   . LYS A  40  ? 0.1506  0.1596 0.1101  -0.0223 -0.0292 0.0214  39  LYS A N   
302  C  CA  . LYS A  40  ? 0.1488  0.1499 0.1111  -0.0024 -0.0434 0.0087  39  LYS A CA  
303  C  C   . LYS A  40  ? 0.1231  0.1544 0.0908  0.0031  -0.0304 0.0155  39  LYS A C   
304  O  O   . LYS A  40  ? 0.1664  0.1725 0.0856  0.0173  -0.0261 0.0302  39  LYS A O   
305  C  CB  . LYS A  40  ? 0.1851  0.1560 0.1341  0.0334  -0.0352 0.0000  39  LYS A CB  
306  C  CG  . LYS A  40  ? 0.2454  0.1700 0.1499  0.0315  -0.0313 0.0140  39  LYS A CG  
307  C  CD  . LYS A  40  ? 0.2303  0.2081 0.1835  0.0117  -0.0438 0.0372  39  LYS A CD  
308  C  CE  . LYS A  40  ? 0.3513  0.1865 0.3276  0.0788  -0.0543 -0.0058 39  LYS A CE  
309  N  NZ  . LYS A  40  ? 0.3965  0.2970 0.4828  0.0989  -0.1332 -0.0440 39  LYS A NZ  
310  N  N   . HIS A  41  ? 0.2224  0.1562 0.0818  -0.0034 -0.0296 0.0093  40  HIS A N   
311  C  CA  . HIS A  41  ? 0.1930  0.1538 0.0962  0.0075  -0.0200 0.0087  40  HIS A CA  
312  C  C   . HIS A  41  ? 0.2224  0.1653 0.0794  0.0092  -0.0186 0.0394  40  HIS A C   
313  O  O   . HIS A  41  ? 0.1829  0.2242 0.1126  0.0247  -0.0027 0.0661  40  HIS A O   
314  C  CB  . HIS A  41  ? 0.2059  0.1678 0.0881  0.0021  -0.0381 -0.0005 40  HIS A CB  
315  C  CG  . HIS A  41  ? 0.1835  0.1592 0.0937  0.0113  -0.0425 0.0076  40  HIS A CG  
316  N  ND1 . HIS A  41  ? 0.2967  0.1879 0.2199  0.0163  -0.1527 0.0289  40  HIS A ND1 
317  C  CD2 . HIS A  41  ? 0.1178  0.1761 0.0871  0.0157  -0.0284 -0.0032 40  HIS A CD2 
318  C  CE1 . HIS A  41  ? 0.2375  0.1599 0.2372  -0.0044 -0.1482 0.0002  40  HIS A CE1 
319  N  NE2 . HIS A  41  ? 0.1887  0.2095 0.1606  0.0145  -0.0484 -0.0287 40  HIS A NE2 
320  N  N   . ASP A  42  ? 0.2149  0.1560 0.1187  -0.0347 -0.0208 0.0428  41  ASP A N   
321  C  CA  . ASP A  42  ? 0.1897  0.1685 0.1153  -0.0156 -0.0019 0.0471  41  ASP A CA  
322  C  C   . ASP A  42  ? 0.2002  0.1876 0.1023  -0.0374 -0.0306 0.0697  41  ASP A C   
323  O  O   . ASP A  42  ? 0.1969  0.1671 0.1040  -0.0234 -0.0286 0.0594  41  ASP A O   
324  C  CB  . ASP A  42  ? 0.2293  0.2170 0.1136  -0.0094 -0.0009 0.0545  41  ASP A CB  
325  C  CG  . ASP A  42  ? 0.2178  0.2637 0.0944  -0.0199 -0.0147 0.0469  41  ASP A CG  
326  O  OD1 . ASP A  42  ? 0.2611  0.2027 0.1531  -0.0155 -0.0082 0.0497  41  ASP A OD1 
327  O  OD2 . ASP A  42  ? 0.3118  0.2654 0.1549  0.0332  0.0379  0.0096  41  ASP A OD2 
328  N  N   . THR A  43  ? 0.1614  0.2224 0.0856  -0.0079 -0.0187 0.0525  42  THR A N   
329  C  CA  . THR A  43  ? 0.2011  0.1890 0.0950  -0.0397 -0.0373 0.0512  42  THR A CA  
330  C  C   . THR A  43  ? 0.1657  0.2231 0.0979  -0.0398 -0.0183 0.0458  42  THR A C   
331  O  O   . THR A  43  ? 0.2034  0.2210 0.1045  -0.0476 -0.0151 0.0476  42  THR A O   
332  C  CB  . THR A  43  ? 0.1217  0.2748 0.0962  -0.0247 -0.0200 0.0677  42  THR A CB  
333  O  OG1 . THR A  43  ? 0.1427  0.2296 0.1014  -0.0176 -0.0104 0.0416  42  THR A OG1 
334  C  CG2 . THR A  43  ? 0.1603  0.2397 0.1225  -0.0129 -0.0099 0.0695  42  THR A CG2 
335  N  N   . SER A  44  ? 0.1671  0.1962 0.1071  -0.0249 -0.0258 0.0649  43  SER A N   
336  C  CA  . SER A  44  ? 0.1869  0.2178 0.0944  -0.0220 -0.0025 0.0758  43  SER A CA  
337  C  C   . SER A  44  ? 0.1646  0.1822 0.0905  -0.0065 0.0086  0.0462  43  SER A C   
338  O  O   . SER A  44  ? 0.1761  0.2206 0.1261  0.0017  0.0135  0.0789  43  SER A O   
339  C  CB  . SER A  44  ? 0.1793  0.2301 0.1368  -0.0087 -0.0376 0.0319  43  SER A CB  
340  O  OG  . SER A  44  ? 0.1826  0.2389 0.1366  0.0150  -0.0048 0.0506  43  SER A OG  
341  N  N   . LEU A  45  ? 0.1775  0.1675 0.0849  -0.0036 -0.0176 0.0269  44  LEU A N   
342  C  CA  . LEU A  45  ? 0.1897  0.1689 0.0855  -0.0002 -0.0190 0.0261  44  LEU A CA  
343  C  C   . LEU A  45  ? 0.2339  0.2066 0.0967  0.0182  0.0034  0.0281  44  LEU A C   
344  O  O   . LEU A  45  ? 0.4027  0.2278 0.1502  0.0612  0.0632  0.0272  44  LEU A O   
345  C  CB  . LEU A  45  ? 0.1538  0.1984 0.1205  0.0091  -0.0055 0.0127  44  LEU A CB  
346  C  CG  . LEU A  45  ? 0.1502  0.1980 0.1142  -0.0063 0.0089  0.0359  44  LEU A CG  
347  C  CD1 . LEU A  45  ? 0.1253  0.2339 0.2120  -0.0052 -0.0080 0.0737  44  LEU A CD1 
348  C  CD2 . LEU A  45  ? 0.1603  0.2249 0.1067  -0.0077 0.0018  0.0083  44  LEU A CD2 
349  N  N   . LYS A  46  ? 0.1641  0.1646 0.1373  -0.0038 -0.0403 0.0271  45  LYS A N   
350  C  CA  . LYS A  46  ? 0.1621  0.1465 0.1624  -0.0111 -0.0463 0.0214  45  LYS A CA  
351  C  C   . LYS A  46  ? 0.1606  0.1675 0.1065  -0.0304 -0.0275 -0.0006 45  LYS A C   
352  O  O   . LYS A  46  ? 0.1599  0.1606 0.1107  -0.0118 -0.0193 -0.0034 45  LYS A O   
353  C  CB  . LYS A  46  ? 0.1452  0.1966 0.2293  -0.0421 -0.0506 0.0278  45  LYS A CB  
354  C  CG  . LYS A  46  ? 0.2059  0.2655 0.3617  -0.1020 -0.1108 0.0726  45  LYS A CG  
355  C  CD  . LYS A  46  ? 0.1772  0.3136 0.4727  -0.1022 -0.1100 0.1112  45  LYS A CD  
356  C  CE  . LYS A  46  ? 0.2479  0.2963 0.3183  -0.1158 -0.0403 0.0558  45  LYS A CE  
357  N  NZ  . LYS A  46  ? 0.2942  0.3736 0.3010  -0.1402 -0.0367 0.1160  45  LYS A NZ  
358  N  N   . PRO A  47  ? 0.1700  0.1696 0.1264  0.0010  -0.0359 0.0013  46  PRO A N   
359  C  CA  . PRO A  47  ? 0.1495  0.1984 0.1038  0.0163  -0.0186 0.0084  46  PRO A CA  
360  C  C   . PRO A  47  ? 0.1592  0.1481 0.1101  -0.0210 -0.0253 0.0205  46  PRO A C   
361  O  O   . PRO A  47  ? 0.1707  0.1624 0.1197  -0.0226 -0.0189 -0.0042 46  PRO A O   
362  C  CB  . PRO A  47  ? 0.1890  0.2159 0.1488  0.0299  -0.0271 -0.0211 46  PRO A CB  
363  C  CG  . PRO A  47  ? 0.2526  0.2576 0.1951  0.0787  -0.0853 -0.0626 46  PRO A CG  
364  C  CD  . PRO A  47  ? 0.2364  0.2400 0.1164  0.0231  -0.0577 -0.0458 46  PRO A CD  
365  N  N   A ILE A  48  ? 0.1714  0.1696 0.0953  0.0003  -0.0332 -0.0121 47  ILE A N   
366  N  N   B ILE A  48  ? 0.1614  0.1757 0.1162  -0.0044 -0.0353 -0.0063 47  ILE A N   
367  C  CA  A ILE A  48  ? 0.1711  0.1398 0.0935  -0.0301 -0.0204 -0.0166 47  ILE A CA  
368  C  CA  B ILE A  48  ? 0.1980  0.1368 0.1224  -0.0091 -0.0557 0.0247  47  ILE A CA  
369  C  C   A ILE A  48  ? 0.1326  0.1639 0.1261  0.0004  -0.0300 0.0022  47  ILE A C   
370  C  C   B ILE A  48  ? 0.1599  0.1689 0.1099  0.0166  -0.0228 0.0000  47  ILE A C   
371  O  O   A ILE A  48  ? 0.1826  0.1678 0.1779  0.0069  0.0032  -0.0148 47  ILE A O   
372  O  O   B ILE A  48  ? 0.1811  0.2529 0.1549  0.0732  -0.0211 -0.0018 47  ILE A O   
373  C  CB  A ILE A  48  ? 0.2120  0.1465 0.1014  -0.0832 -0.0286 0.0153  47  ILE A CB  
374  C  CB  B ILE A  48  ? 0.2451  0.1585 0.1768  0.0089  -0.0820 -0.0041 47  ILE A CB  
375  C  CG1 A ILE A  48  ? 0.2601  0.1757 0.0891  -0.0595 -0.0612 0.0445  47  ILE A CG1 
376  C  CG1 B ILE A  48  ? 0.2307  0.1822 0.1894  -0.0197 -0.0930 0.0096  47  ILE A CG1 
377  C  CG2 A ILE A  48  ? 0.2238  0.1190 0.1150  -0.0511 -0.0566 0.0116  47  ILE A CG2 
378  C  CG2 B ILE A  48  ? 0.3316  0.1621 0.1980  0.0241  -0.0372 0.0535  47  ILE A CG2 
379  C  CD1 A ILE A  48  ? 0.1729  0.1355 0.3014  -0.0024 -0.0974 0.0085  47  ILE A CD1 
380  C  CD1 B ILE A  48  ? 0.3118  0.2194 0.1391  0.0607  -0.1010 -0.0225 47  ILE A CD1 
381  N  N   . SER A  49  ? 0.1840  0.1463 0.1067  0.0026  -0.0411 0.0221  48  SER A N   
382  C  CA  . SER A  49  ? 0.2788  0.1465 0.1416  0.0030  -0.0730 0.0179  48  SER A CA  
383  C  C   . SER A  49  ? 0.2099  0.1276 0.1301  0.0147  -0.0225 0.0287  48  SER A C   
384  O  O   . SER A  49  ? 0.1901  0.1944 0.1599  0.0285  -0.0159 0.0225  48  SER A O   
385  C  CB  . SER A  49  ? 0.3538  0.1790 0.2472  -0.1067 -0.1161 0.0268  48  SER A CB  
386  O  OG  . SER A  49  ? 0.4903  0.2275 0.4241  -0.1447 -0.1602 0.0741  48  SER A OG  
387  N  N   . VAL A  50  ? 0.1822  0.1326 0.1294  -0.0027 -0.0210 0.0167  49  VAL A N   
388  C  CA  . VAL A  50  ? 0.1696  0.1337 0.1305  0.0173  -0.0339 0.0284  49  VAL A CA  
389  C  C   . VAL A  50  ? 0.2275  0.1488 0.1221  0.0242  0.0134  0.0167  49  VAL A C   
390  O  O   . VAL A  50  ? 0.3064  0.1592 0.1603  0.0469  0.0307  0.0029  49  VAL A O   
391  C  CB  . VAL A  50  ? 0.1926  0.1743 0.2242  0.0201  -0.0678 -0.0173 49  VAL A CB  
392  C  CG1 . VAL A  50  ? 0.2242  0.1714 0.2240  0.0032  -0.0684 -0.0100 49  VAL A CG1 
393  C  CG2 . VAL A  50  ? 0.1879  0.2662 0.3298  -0.0326 -0.0159 -0.0567 49  VAL A CG2 
394  N  N   . SER A  51  ? 0.1517  0.1456 0.1208  -0.0040 -0.0242 0.0261  50  SER A N   
395  C  CA  . SER A  51  ? 0.2034  0.1610 0.1434  0.0044  -0.0322 0.0212  50  SER A CA  
396  C  C   . SER A  51  ? 0.1527  0.1294 0.1337  0.0049  -0.0124 0.0070  50  SER A C   
397  O  O   . SER A  51  ? 0.1517  0.1333 0.1488  0.0044  -0.0111 0.0050  50  SER A O   
398  C  CB  . SER A  51  ? 0.2248  0.1861 0.1725  -0.0611 -0.0354 -0.0083 50  SER A CB  
399  O  OG  . SER A  51  ? 0.3176  0.2364 0.2684  -0.0915 -0.0265 -0.0439 50  SER A OG  
400  N  N   . TYR A  52  ? 0.1448  0.1199 0.1233  -0.0020 -0.0179 -0.0071 51  TYR A N   
401  C  CA  . TYR A  52  ? 0.1298  0.1004 0.1118  -0.0021 -0.0060 0.0104  51  TYR A CA  
402  C  C   . TYR A  52  ? 0.1368  0.1076 0.1459  0.0158  0.0018  0.0125  51  TYR A C   
403  O  O   . TYR A  52  ? 0.3103  0.1531 0.1639  0.0939  0.0529  0.0395  51  TYR A O   
404  C  CB  . TYR A  52  ? 0.1203  0.1230 0.1120  -0.0111 -0.0134 0.0228  51  TYR A CB  
405  C  CG  . TYR A  52  ? 0.1102  0.1155 0.0988  -0.0026 -0.0013 0.0027  51  TYR A CG  
406  C  CD1 . TYR A  52  ? 0.1239  0.1045 0.1047  0.0006  -0.0130 -0.0027 51  TYR A CD1 
407  C  CD2 . TYR A  52  ? 0.1280  0.1190 0.1110  -0.0073 0.0015  0.0000  51  TYR A CD2 
408  C  CE1 . TYR A  52  ? 0.1205  0.1067 0.0996  -0.0089 -0.0039 -0.0063 51  TYR A CE1 
409  C  CE2 . TYR A  52  ? 0.1172  0.1084 0.1137  0.0006  -0.0039 0.0002  51  TYR A CE2 
410  C  CZ  . TYR A  52  ? 0.1120  0.1044 0.1028  -0.0059 -0.0055 -0.0155 51  TYR A CZ  
411  O  OH  . TYR A  52  ? 0.1362  0.1084 0.1229  -0.0094 0.0019  -0.0013 51  TYR A OH  
412  N  N   . ASN A  53  ? 0.1459  0.1076 0.1294  -0.0225 -0.0326 0.0302  52  ASN A N   
413  C  CA  . ASN A  53  ? 0.1542  0.1135 0.1133  -0.0184 -0.0419 0.0186  52  ASN A CA  
414  C  C   . ASN A  53  ? 0.1542  0.0935 0.0998  0.0002  -0.0119 0.0031  52  ASN A C   
415  O  O   . ASN A  53  ? 0.1527  0.1021 0.1190  0.0060  -0.0153 -0.0070 52  ASN A O   
416  C  CB  . ASN A  53  ? 0.1571  0.1073 0.1624  -0.0272 -0.0142 0.0282  52  ASN A CB  
417  C  CG  . ASN A  53  ? 0.1797  0.1120 0.1330  -0.0212 -0.0351 0.0080  52  ASN A CG  
418  O  OD1 . ASN A  53  ? 0.1729  0.1254 0.1492  -0.0151 -0.0516 0.0215  52  ASN A OD1 
419  N  ND2 . ASN A  53  ? 0.1817  0.1289 0.1786  -0.0370 -0.0341 0.0407  52  ASN A ND2 
420  N  N   . PRO A  54  ? 0.1380  0.1137 0.1232  -0.0046 -0.0287 0.0089  53  PRO A N   
421  C  CA  . PRO A  54  ? 0.1307  0.1263 0.1351  0.0000  -0.0356 0.0036  53  PRO A CA  
422  C  C   . PRO A  54  ? 0.1391  0.1011 0.1234  -0.0054 -0.0187 -0.0179 53  PRO A C   
423  O  O   . PRO A  54  ? 0.1495  0.1252 0.1391  -0.0019 -0.0377 0.0000  53  PRO A O   
424  C  CB  . PRO A  54  ? 0.1434  0.1481 0.1412  -0.0025 -0.0121 -0.0258 53  PRO A CB  
425  C  CG  . PRO A  54  ? 0.1524  0.1542 0.1441  0.0075  -0.0299 -0.0313 53  PRO A CG  
426  C  CD  . PRO A  54  ? 0.1671  0.1141 0.1271  0.0068  -0.0118 -0.0233 53  PRO A CD  
427  N  N   . ALA A  55  ? 0.1639  0.1020 0.1316  -0.0113 -0.0332 0.0054  54  ALA A N   
428  C  CA  . ALA A  55  ? 0.1897  0.1014 0.1269  -0.0088 -0.0164 0.0144  54  ALA A CA  
429  C  C   . ALA A  55  ? 0.1685  0.1153 0.1283  -0.0013 -0.0095 -0.0040 54  ALA A C   
430  O  O   . ALA A  55  ? 0.2292  0.1344 0.1398  0.0048  0.0081  0.0026  54  ALA A O   
431  C  CB  . ALA A  55  ? 0.2375  0.1117 0.1562  -0.0317 -0.0036 0.0069  54  ALA A CB  
432  N  N   . THR A  56  ? 0.1520  0.0942 0.1287  0.0022  -0.0062 -0.0009 55  THR A N   
433  C  CA  . THR A  56  ? 0.1359  0.1199 0.1099  -0.0122 -0.0154 -0.0083 55  THR A CA  
434  C  C   . THR A  56  ? 0.1348  0.1007 0.0994  -0.0092 -0.0163 0.0097  55  THR A C   
435  O  O   . THR A  56  ? 0.1386  0.1142 0.1080  -0.0050 -0.0082 -0.0009 55  THR A O   
436  C  CB  . THR A  56  ? 0.1337  0.1380 0.0978  -0.0223 -0.0277 0.0154  55  THR A CB  
437  O  OG1 . THR A  56  ? 0.1386  0.1127 0.1054  -0.0034 -0.0295 0.0104  55  THR A OG1 
438  C  CG2 . THR A  56  ? 0.1513  0.1624 0.1483  -0.0290 -0.0286 -0.0152 55  THR A CG2 
439  N  N   . ALA A  57  ? 0.1269  0.1225 0.1109  -0.0089 -0.0270 0.0155  56  ALA A N   
440  C  CA  . ALA A  57  ? 0.1274  0.1224 0.0952  -0.0141 -0.0185 0.0121  56  ALA A CA  
441  C  C   . ALA A  57  ? 0.1199  0.0989 0.1181  -0.0087 -0.0205 0.0188  56  ALA A C   
442  O  O   . ALA A  57  ? 0.1621  0.1011 0.1181  -0.0120 -0.0159 0.0146  56  ALA A O   
443  C  CB  . ALA A  57  ? 0.1260  0.1578 0.1152  0.0008  -0.0142 0.0108  56  ALA A CB  
444  N  N   . LYS A  58  ? 0.1420  0.1054 0.0994  -0.0016 -0.0136 0.0021  57  LYS A N   
445  C  CA  . LYS A  58  ? 0.1344  0.1373 0.0906  -0.0273 -0.0002 0.0055  57  LYS A CA  
446  C  C   . LYS A  58  ? 0.1380  0.1238 0.0944  -0.0170 -0.0050 0.0124  57  LYS A C   
447  O  O   . LYS A  58  ? 0.1793  0.1289 0.1080  -0.0189 -0.0244 0.0168  57  LYS A O   
448  C  CB  . LYS A  58  ? 0.1495  0.1969 0.1257  -0.0419 0.0122  -0.0022 57  LYS A CB  
449  C  CG  . LYS A  58  ? 0.2081  0.2643 0.1492  -0.0223 0.0666  -0.0267 57  LYS A CG  
450  C  CD  . LYS A  58  ? 0.2090  0.2816 0.2314  0.0214  0.0647  -0.0298 57  LYS A CD  
451  C  CE  . LYS A  58  ? 0.3553  0.4950 0.2874  0.0083  0.1696  -0.1049 57  LYS A CE  
452  N  NZ  . LYS A  58  ? 0.5058  0.6520 0.2539  0.1779  0.0337  -0.0270 57  LYS A NZ  
453  N  N   A GLU A  59  ? 0.1274  0.1187 0.0905  -0.0261 -0.0152 0.0122  58  GLU A N   
454  N  N   B GLU A  59  ? 0.1289  0.1189 0.0933  -0.0299 -0.0172 0.0106  58  GLU A N   
455  C  CA  A GLU A  59  ? 0.1377  0.1208 0.0976  -0.0326 -0.0116 0.0033  58  GLU A CA  
456  C  CA  B GLU A  59  ? 0.1373  0.1208 0.0977  -0.0330 -0.0131 0.0027  58  GLU A CA  
457  C  C   A GLU A  59  ? 0.1247  0.1066 0.0849  -0.0083 -0.0245 0.0135  58  GLU A C   
458  C  C   B GLU A  59  ? 0.1248  0.1083 0.0847  -0.0084 -0.0243 0.0143  58  GLU A C   
459  O  O   A GLU A  59  ? 0.1445  0.1531 0.1214  -0.0200 -0.0529 0.0389  58  GLU A O   
460  O  O   B GLU A  59  ? 0.1448  0.1531 0.1190  -0.0223 -0.0528 0.0387  58  GLU A O   
461  C  CB  A GLU A  59  ? 0.1678  0.1958 0.0829  -0.0525 0.0142  -0.0184 58  GLU A CB  
462  C  CB  B GLU A  59  ? 0.1696  0.1973 0.0873  -0.0509 0.0152  -0.0171 58  GLU A CB  
463  C  CG  A GLU A  59  ? 0.1908  0.2048 0.1016  0.0032  0.0018  -0.0341 58  GLU A CG  
464  C  CG  B GLU A  59  ? 0.1912  0.2156 0.1147  0.0068  -0.0018 -0.0348 58  GLU A CG  
465  C  CD  A GLU A  59  ? 0.1761  0.2023 0.1036  0.0194  0.0065  0.0212  58  GLU A CD  
466  C  CD  B GLU A  59  ? 0.1887  0.2472 0.1499  0.0122  0.0225  -0.0096 58  GLU A CD  
467  O  OE1 A GLU A  59  ? 0.1495  0.2525 0.0943  -0.0019 0.0122  0.0332  58  GLU A OE1 
468  O  OE1 B GLU A  59  ? 0.2469  0.3054 0.2009  0.0550  0.0284  0.0072  58  GLU A OE1 
469  O  OE2 A GLU A  59  ? 0.1854  0.2145 0.1014  0.0565  0.0027  -0.0020 58  GLU A OE2 
470  O  OE2 B GLU A  59  ? 0.3499  0.3452 0.2791  -0.0110 0.0352  0.0690  58  GLU A OE2 
471  N  N   . ILE A  60  ? 0.1243  0.1108 0.0865  -0.0116 -0.0212 0.0019  59  ILE A N   
472  C  CA  . ILE A  60  ? 0.1252  0.1090 0.0959  -0.0149 -0.0198 -0.0021 59  ILE A CA  
473  C  C   . ILE A  60  ? 0.1269  0.1159 0.0822  -0.0160 -0.0314 0.0047  59  ILE A C   
474  O  O   . ILE A  60  ? 0.1448  0.1380 0.0783  0.0002  -0.0251 0.0144  59  ILE A O   
475  C  CB  . ILE A  60  ? 0.1172  0.1208 0.1040  0.0000  -0.0227 0.0176  59  ILE A CB  
476  C  CG1 . ILE A  60  ? 0.1259  0.1159 0.1040  0.0043  -0.0035 0.0132  59  ILE A CG1 
477  C  CG2 . ILE A  60  ? 0.1271  0.1542 0.1093  0.0034  -0.0335 0.0294  59  ILE A CG2 
478  C  CD1 . ILE A  60  ? 0.1416  0.1319 0.1405  0.0049  0.0092  0.0104  59  ILE A CD1 
479  N  N   A ILE A  61  ? 0.1276  0.1075 0.0810  -0.0073 -0.0128 -0.0011 60  ILE A N   
480  N  N   B ILE A  61  ? 0.1272  0.1067 0.0840  -0.0086 -0.0122 -0.0036 60  ILE A N   
481  C  CA  A ILE A  61  ? 0.1298  0.1169 0.0601  -0.0051 -0.0113 0.0089  60  ILE A CA  
482  C  CA  B ILE A  61  ? 0.1316  0.1128 0.1128  -0.0205 0.0054  -0.0234 60  ILE A CA  
483  C  C   A ILE A  61  ? 0.1155  0.1146 0.0741  0.0011  -0.0055 -0.0023 60  ILE A C   
484  C  C   B ILE A  61  ? 0.1151  0.1147 0.0768  0.0008  -0.0058 -0.0036 60  ILE A C   
485  O  O   A ILE A  61  ? 0.1187  0.1216 0.0750  -0.0078 -0.0065 0.0041  60  ILE A O   
486  O  O   B ILE A  61  ? 0.1169  0.1231 0.0761  -0.0068 -0.0078 0.0020  60  ILE A O   
487  C  CB  A ILE A  61  ? 0.1294  0.1037 0.0919  -0.0201 0.0183  0.0023  60  ILE A CB  
488  C  CB  B ILE A  61  ? 0.1298  0.1743 0.0970  -0.0344 0.0122  -0.0146 60  ILE A CB  
489  C  CG1 A ILE A  61  ? 0.1020  0.1048 0.0873  -0.0125 0.0003  0.0048  60  ILE A CG1 
490  C  CG1 B ILE A  61  ? 0.1797  0.2326 0.1416  -0.0486 0.0316  -0.0612 60  ILE A CG1 
491  C  CG2 A ILE A  61  ? 0.1391  0.1488 0.1176  -0.0193 0.0529  -0.0159 60  ILE A CG2 
492  C  CG2 B ILE A  61  ? 0.1384  0.2363 0.0950  -0.0093 0.0214  0.0102  60  ILE A CG2 
493  C  CD1 A ILE A  61  ? 0.1036  0.1768 0.1747  -0.0550 -0.0132 0.0167  60  ILE A CD1 
494  C  CD1 B ILE A  61  ? 0.1932  0.3067 0.2027  0.0055  0.0517  -0.1034 60  ILE A CD1 
495  N  N   . ASN A  62  ? 0.1199  0.1120 0.0800  -0.0063 -0.0081 -0.0082 61  ASN A N   
496  C  CA  . ASN A  62  ? 0.1208  0.1164 0.0926  0.0020  -0.0196 -0.0023 61  ASN A CA  
497  C  C   . ASN A  62  ? 0.1206  0.1259 0.0804  -0.0094 -0.0225 -0.0016 61  ASN A C   
498  O  O   . ASN A  62  ? 0.1107  0.1535 0.0828  -0.0080 -0.0131 -0.0062 61  ASN A O   
499  C  CB  . ASN A  62  ? 0.1119  0.1377 0.0856  0.0000  -0.0194 -0.0105 61  ASN A CB  
500  C  CG  . ASN A  62  ? 0.1153  0.1195 0.0863  0.0085  -0.0116 -0.0121 61  ASN A CG  
501  O  OD1 . ASN A  62  ? 0.1118  0.1243 0.1199  0.0060  -0.0277 -0.0132 61  ASN A OD1 
502  N  ND2 . ASN A  62  ? 0.1072  0.1793 0.0811  0.0031  -0.0131 -0.0093 61  ASN A ND2 
503  N  N   . VAL A  63  ? 0.1164  0.1337 0.0883  -0.0004 -0.0200 -0.0055 62  VAL A N   
504  C  CA  . VAL A  63  ? 0.1101  0.1283 0.1147  0.0147  -0.0203 -0.0205 62  VAL A CA  
505  C  C   . VAL A  63  ? 0.1259  0.1373 0.0865  0.0062  -0.0288 -0.0134 62  VAL A C   
506  O  O   . VAL A  63  ? 0.1265  0.1416 0.1581  0.0181  -0.0161 -0.0215 62  VAL A O   
507  C  CB  . VAL A  63  ? 0.1294  0.1391 0.1420  -0.0048 -0.0510 -0.0055 62  VAL A CB  
508  C  CG1 . VAL A  63  ? 0.1527  0.1549 0.2145  -0.0297 -0.0789 -0.0022 62  VAL A CG1 
509  C  CG2 . VAL A  63  ? 0.1513  0.1610 0.1287  0.0163  -0.0484 0.0025  62  VAL A CG2 
510  N  N   . GLY A  64  ? 0.1220  0.1420 0.0820  -0.0066 -0.0260 -0.0155 63  GLY A N   
511  C  CA  . GLY A  64  ? 0.1171  0.1344 0.1038  -0.0042 -0.0333 -0.0232 63  GLY A CA  
512  C  C   . GLY A  64  ? 0.1049  0.1333 0.1068  0.0075  -0.0184 -0.0145 63  GLY A C   
513  O  O   . GLY A  64  ? 0.1305  0.1659 0.1531  -0.0142 -0.0311 0.0024  63  GLY A O   
514  N  N   . HIS A  65  ? 0.1129  0.1330 0.0831  0.0103  -0.0089 -0.0205 64  HIS A N   
515  C  CA  . HIS A  65  ? 0.1562  0.1341 0.0838  0.0085  -0.0010 -0.0210 64  HIS A CA  
516  C  C   . HIS A  65  ? 0.1330  0.1312 0.0803  0.0094  -0.0116 -0.0229 64  HIS A C   
517  O  O   . HIS A  65  ? 0.1420  0.1118 0.0949  -0.0038 -0.0122 -0.0145 64  HIS A O   
518  C  CB  . HIS A  65  ? 0.1452  0.1134 0.1294  0.0117  -0.0190 -0.0126 64  HIS A CB  
519  C  CG  . HIS A  65  ? 0.1319  0.1249 0.1111  0.0193  -0.0216 -0.0136 64  HIS A CG  
520  N  ND1 . HIS A  65  ? 0.1578  0.1386 0.1005  0.0208  -0.0187 -0.0251 64  HIS A ND1 
521  C  CD2 . HIS A  65  ? 0.1452  0.1470 0.1502  0.0146  0.0155  -0.0035 64  HIS A CD2 
522  C  CE1 . HIS A  65  ? 0.1124  0.1581 0.1531  0.0047  -0.0089 0.0020  64  HIS A CE1 
523  N  NE2 . HIS A  65  ? 0.1289  0.1664 0.1420  0.0128  -0.0071 -0.0108 64  HIS A NE2 
524  N  N   . SER A  66  ? 0.1176  0.1128 0.1067  0.0000  -0.0177 -0.0261 65  SER A N   
525  C  CA  . SER A  66  ? 0.1337  0.0926 0.0985  0.0038  -0.0183 -0.0170 65  SER A CA  
526  C  C   . SER A  66  ? 0.1178  0.1145 0.0888  -0.0032 -0.0190 -0.0092 65  SER A C   
527  O  O   . SER A  66  ? 0.1344  0.1208 0.0829  -0.0041 -0.0127 -0.0097 65  SER A O   
528  C  CB  . SER A  66  ? 0.1664  0.1265 0.0664  -0.0034 -0.0390 -0.0288 65  SER A CB  
529  O  OG  . SER A  66  ? 0.1969  0.1080 0.0838  0.0026  -0.0253 -0.0023 65  SER A OG  
530  N  N   . PHE A  67  ? 0.1099  0.0935 0.0926  -0.0111 -0.0163 -0.0121 66  PHE A N   
531  C  CA  . PHE A  67  ? 0.0932  0.0969 0.0996  -0.0089 -0.0303 -0.0031 66  PHE A CA  
532  C  C   . PHE A  67  ? 0.1032  0.1023 0.0718  -0.0003 -0.0264 -0.0021 66  PHE A C   
533  O  O   . PHE A  67  ? 0.1181  0.1133 0.0812  -0.0059 -0.0189 0.0000  66  PHE A O   
534  C  CB  . PHE A  67  ? 0.1100  0.1204 0.0803  0.0116  -0.0197 -0.0060 66  PHE A CB  
535  C  CG  . PHE A  67  ? 0.1056  0.1199 0.0759  0.0063  -0.0275 -0.0043 66  PHE A CG  
536  C  CD1 . PHE A  67  ? 0.1259  0.1305 0.1093  0.0128  -0.0060 0.0150  66  PHE A CD1 
537  C  CD2 . PHE A  67  ? 0.1307  0.1172 0.1222  0.0226  -0.0379 -0.0201 66  PHE A CD2 
538  C  CE1 . PHE A  67  ? 0.1333  0.1499 0.1141  0.0391  0.0038  0.0275  66  PHE A CE1 
539  C  CE2 . PHE A  67  ? 0.1430  0.1538 0.1016  0.0315  -0.0396 -0.0207 66  PHE A CE2 
540  C  CZ  . PHE A  67  ? 0.1427  0.1355 0.1190  0.0423  -0.0254 0.0062  66  PHE A CZ  
541  N  N   . HIS A  68  ? 0.1063  0.1082 0.0910  -0.0109 -0.0185 0.0016  67  HIS A N   
542  C  CA  . HIS A  68  ? 0.1276  0.1093 0.1495  -0.0175 -0.0545 0.0098  67  HIS A CA  
543  C  C   . HIS A  68  ? 0.1359  0.1081 0.0759  -0.0155 -0.0339 0.0140  67  HIS A C   
544  O  O   . HIS A  68  ? 0.1736  0.1273 0.0774  -0.0071 -0.0377 0.0188  67  HIS A O   
545  C  CB  . HIS A  68  ? 0.1574  0.1391 0.1829  -0.0214 -0.0406 -0.0186 67  HIS A CB  
546  C  CG  . HIS A  68  ? 0.1326  0.1718 0.1923  0.0076  -0.0584 -0.0173 67  HIS A CG  
547  N  ND1 . HIS A  68  ? 0.1808  0.1847 0.2416  0.0121  -0.0453 -0.0032 67  HIS A ND1 
548  C  CD2 . HIS A  68  ? 0.1700  0.1653 0.1689  0.0299  -0.0533 -0.0222 67  HIS A CD2 
549  C  CE1 . HIS A  68  ? 0.1829  0.1815 0.3161  0.0216  -0.0127 -0.0280 67  HIS A CE1 
550  N  NE2 . HIS A  68  ? 0.1621  0.1720 0.2558  0.0111  -0.0353 -0.0474 67  HIS A NE2 
551  N  N   . VAL A  69  ? 0.1181  0.1120 0.0882  -0.0186 -0.0269 0.0111  68  VAL A N   
552  C  CA  . VAL A  69  ? 0.1348  0.1080 0.0828  -0.0068 -0.0418 0.0019  68  VAL A CA  
553  C  C   . VAL A  69  ? 0.1351  0.0996 0.0901  0.0001  -0.0408 0.0039  68  VAL A C   
554  O  O   . VAL A  69  ? 0.1323  0.1238 0.0897  -0.0089 -0.0370 0.0187  68  VAL A O   
555  C  CB  . VAL A  69  ? 0.1294  0.1574 0.0933  0.0173  -0.0160 -0.0100 68  VAL A CB  
556  C  CG1 . VAL A  69  ? 0.2441  0.1305 0.1115  0.0447  -0.0365 0.0067  68  VAL A CG1 
557  C  CG2 . VAL A  69  ? 0.1155  0.2945 0.1146  0.0223  -0.0159 -0.0477 68  VAL A CG2 
558  N  N   A ASN A  70  ? 0.1465  0.1260 0.1005  -0.0160 -0.0245 0.0161  69  ASN A N   
559  N  N   B ASN A  70  ? 0.1402  0.1274 0.0962  -0.0100 -0.0302 0.0223  69  ASN A N   
560  C  CA  A ASN A  70  ? 0.1402  0.1106 0.1102  -0.0071 -0.0121 0.0178  69  ASN A CA  
561  C  CA  B ASN A  70  ? 0.1405  0.1294 0.1137  -0.0222 0.0041  0.0036  69  ASN A CA  
562  C  C   A ASN A  70  ? 0.1172  0.1142 0.1032  0.0018  -0.0013 0.0036  69  ASN A C   
563  C  C   B ASN A  70  ? 0.1138  0.1198 0.1062  0.0017  0.0017  0.0051  69  ASN A C   
564  O  O   A ASN A  70  ? 0.1243  0.1120 0.1099  0.0026  0.0000  0.0060  69  ASN A O   
565  O  O   B ASN A  70  ? 0.1301  0.1194 0.1109  0.0000  -0.0032 0.0181  69  ASN A O   
566  C  CB  A ASN A  70  ? 0.1754  0.1294 0.1126  0.0050  -0.0034 -0.0236 69  ASN A CB  
567  C  CB  B ASN A  70  ? 0.1610  0.1639 0.0950  0.0149  -0.0270 -0.0013 69  ASN A CB  
568  C  CG  A ASN A  70  ? 0.2098  0.1538 0.1614  0.0200  -0.0639 -0.0547 69  ASN A CG  
569  C  CG  B ASN A  70  ? 0.2235  0.1897 0.1754  0.0257  -0.0021 -0.0699 69  ASN A CG  
570  O  OD1 A ASN A  70  ? 0.1671  0.1007 0.3154  0.0293  -0.0266 -0.0379 69  ASN A OD1 
571  O  OD1 B ASN A  70  ? 0.2224  0.2734 0.2125  0.0002  -0.0183 -0.0919 69  ASN A OD1 
572  N  ND2 A ASN A  70  ? 0.1359  0.1438 0.1671  -0.0049 -0.0422 -0.0306 69  ASN A ND2 
573  N  ND2 B ASN A  70  ? 0.2460  0.2432 0.2337  0.0304  -0.0438 -0.0416 69  ASN A ND2 
574  N  N   . PHE A  71  ? 0.1247  0.1155 0.0892  -0.0161 0.0033  0.0098  70  PHE A N   
575  C  CA  . PHE A  71  ? 0.1312  0.1197 0.1056  -0.0252 -0.0019 0.0190  70  PHE A CA  
576  C  C   . PHE A  71  ? 0.1553  0.1146 0.1178  -0.0181 0.0179  0.0245  70  PHE A C   
577  O  O   . PHE A  71  ? 0.1585  0.1283 0.1980  -0.0137 0.0527  0.0086  70  PHE A O   
578  C  CB  . PHE A  71  ? 0.1362  0.1398 0.0908  -0.0110 0.0026  0.0027  70  PHE A CB  
579  C  CG  . PHE A  71  ? 0.1234  0.1134 0.0768  -0.0114 -0.0068 0.0066  70  PHE A CG  
580  C  CD1 . PHE A  71  ? 0.1736  0.1675 0.0849  -0.0584 0.0223  0.0044  70  PHE A CD1 
581  C  CD2 . PHE A  71  ? 0.1330  0.1276 0.0845  0.0113  -0.0030 0.0135  70  PHE A CD2 
582  C  CE1 . PHE A  71  ? 0.1958  0.2490 0.0889  -0.1189 0.0296  -0.0535 70  PHE A CE1 
583  C  CE2 . PHE A  71  ? 0.1253  0.1499 0.1047  0.0138  -0.0016 0.0175  70  PHE A CE2 
584  C  CZ  . PHE A  71  ? 0.1298  0.2454 0.0749  -0.0570 -0.0044 -0.0205 70  PHE A CZ  
585  N  N   A GLU A  72  ? 0.1283  0.1124 0.1234  -0.0362 -0.0023 0.0432  71  GLU A N   
586  N  N   B GLU A  72  ? 0.1416  0.1048 0.1164  -0.0197 -0.0012 0.0158  71  GLU A N   
587  C  CA  A GLU A  72  ? 0.1241  0.1111 0.1333  -0.0251 -0.0003 0.0346  71  GLU A CA  
588  C  CA  B GLU A  72  ? 0.1657  0.1470 0.1800  -0.0104 0.0465  0.0098  71  GLU A CA  
589  C  C   A GLU A  72  ? 0.1049  0.0880 0.1632  -0.0089 0.0412  0.0494  71  GLU A C   
590  C  C   B GLU A  72  ? 0.1883  0.1470 0.2257  -0.0152 0.0629  0.0810  71  GLU A C   
591  O  O   A GLU A  72  ? 0.1366  0.2002 0.1811  0.0150  -0.0229 0.0604  71  GLU A O   
592  O  O   B GLU A  72  ? 0.0917  0.1790 0.2389  -0.0509 0.0033  0.0657  71  GLU A O   
593  C  CB  A GLU A  72  ? 0.1276  0.0971 0.1553  -0.0373 0.0286  0.0533  71  GLU A CB  
594  C  CB  B GLU A  72  ? 0.2073  0.1326 0.2106  0.0387  0.0075  0.0168  71  GLU A CB  
595  C  CG  A GLU A  72  ? 0.3018  0.2256 0.1423  -0.1018 -0.0454 0.1178  71  GLU A CG  
596  C  CG  B GLU A  72  ? 0.2784  0.2066 0.1973  0.0538  0.0075  0.0486  71  GLU A CG  
597  C  CD  A GLU A  72  ? 0.3115  0.1775 0.2508  0.0062  0.0036  0.0473  71  GLU A CD  
598  C  CD  B GLU A  72  ? 0.3503  0.2249 0.2188  -0.0616 -0.0339 0.1166  71  GLU A CD  
599  O  OE1 A GLU A  72  ? 0.5039  0.1578 0.3578  -0.0594 -0.1381 0.0945  71  GLU A OE1 
600  O  OE1 B GLU A  72  ? 0.3599  0.3007 0.2328  -0.1086 -0.0436 0.0660  71  GLU A OE1 
601  O  OE2 A GLU A  72  ? 0.4268  0.2120 0.3804  -0.1459 -0.1663 0.0996  71  GLU A OE2 
602  O  OE2 B GLU A  72  ? 0.3427  0.2885 0.1937  0.0025  -0.0030 0.0595  71  GLU A OE2 
603  N  N   A ASP A  73  ? 0.1102  0.1176 0.1725  0.0358  0.0494  0.0772  72  ASP A N   
604  N  N   B ASP A  73  ? 0.1725  0.1075 0.3571  0.0189  0.0403  0.1381  72  ASP A N   
605  C  CA  A ASP A  73  ? 0.0989  0.1441 0.1039  0.0043  -0.0082 0.0627  72  ASP A CA  
606  C  CA  B ASP A  73  ? 0.1664  0.1243 0.3064  -0.0015 0.0367  0.0952  72  ASP A CA  
607  C  C   A ASP A  73  ? 0.1115  0.1641 0.0576  -0.0178 -0.0023 0.0010  72  ASP A C   
608  C  C   B ASP A  73  ? 0.1779  0.2161 0.2156  -0.0114 0.0237  0.0106  72  ASP A C   
609  O  O   A ASP A  73  ? 0.1289  0.1581 0.1129  -0.0144 0.0297  0.0238  72  ASP A O   
610  O  O   B ASP A  73  ? 0.3291  0.2802 0.1531  -0.0174 0.0587  0.0760  72  ASP A O   
611  C  CB  A ASP A  73  ? 0.2133  0.1542 0.1301  -0.0023 -0.0384 0.0722  72  ASP A CB  
612  C  CB  B ASP A  73  ? 0.2651  0.1235 0.1987  -0.0390 -0.0062 0.0556  72  ASP A CB  
613  C  CG  A ASP A  73  ? 0.2192  0.0598 0.3233  -0.0357 -0.1232 0.0219  72  ASP A CG  
614  C  CG  B ASP A  73  ? 0.1592  0.2611 0.3007  -0.0162 0.0669  -0.0237 72  ASP A CG  
615  O  OD1 A ASP A  73  ? 0.0662  0.1056 0.2411  -0.0257 -0.0184 0.0259  72  ASP A OD1 
616  O  OD1 B ASP A  73  ? 0.2957  0.1822 0.2242  -0.0695 0.1060  -0.0458 72  ASP A OD1 
617  O  OD2 A ASP A  73  ? 0.1452  0.1344 0.3276  -0.0160 -0.1126 0.0120  72  ASP A OD2 
618  O  OD2 B ASP A  73  ? 0.1538  0.2648 0.3679  -0.0044 -0.0111 0.0976  72  ASP A OD2 
619  N  N   . ASN A  74  ? 0.1914  0.1725 0.2723  -0.0622 0.0869  -0.0406 73  ASN A N   
620  C  CA  . ASN A  74  ? 0.3010  0.2249 0.2924  -0.1225 0.0491  -0.0629 73  ASN A CA  
621  C  C   . ASN A  74  ? 0.2188  0.3240 0.3115  -0.1128 0.1647  -0.1403 73  ASN A C   
622  O  O   . ASN A  74  ? 0.3243  0.4134 0.4508  -0.2410 0.2426  -0.2080 73  ASN A O   
623  C  CB  . ASN A  74  ? 0.4414  0.2303 0.2543  -0.1010 0.0253  0.0383  73  ASN A CB  
624  C  CG  . ASN A  74  ? 0.5291  0.5958 0.4864  -0.0819 -0.1085 -0.0647 73  ASN A CG  
625  O  OD1 . ASN A  74  ? 0.6298  0.5037 0.3003  -0.0831 -0.0208 0.0445  73  ASN A OD1 
626  N  ND2 . ASN A  74  ? 0.5461  0.4257 0.2070  -0.2198 0.0147  0.0291  73  ASN A ND2 
627  N  N   . ASP A  75  ? 0.1923  0.1344 0.2576  -0.0527 0.0412  -0.0392 74  ASP A N   
628  C  CA  . ASP A  75  ? 0.1815  0.1351 0.2081  -0.0259 0.0626  0.0067  74  ASP A CA  
629  C  C   . ASP A  75  ? 0.1786  0.1298 0.2321  -0.0022 0.0491  0.0074  74  ASP A C   
630  O  O   . ASP A  75  ? 0.1495  0.1181 0.3122  -0.0291 0.0618  0.0290  74  ASP A O   
631  C  CB  . ASP A  75  ? 0.1926  0.1252 0.2540  -0.0335 0.0535  -0.0018 74  ASP A CB  
632  C  CG  . ASP A  75  ? 0.2327  0.1307 0.1833  -0.0097 0.0285  0.0167  74  ASP A CG  
633  O  OD1 . ASP A  75  ? 0.2041  0.1405 0.2372  -0.0114 0.0264  0.0233  74  ASP A OD1 
634  O  OD2 . ASP A  75  ? 0.3208  0.1725 0.2709  -0.0290 0.0135  0.0583  74  ASP A OD2 
635  N  N   . ASN A  76  ? 0.1416  0.1298 0.2066  -0.0200 0.0322  0.0177  75  ASN A N   
636  C  CA  . ASN A  76  ? 0.1402  0.1535 0.2486  -0.0330 -0.0051 0.0903  75  ASN A CA  
637  C  C   . ASN A  76  ? 0.0759  0.3542 0.5115  0.0031  -0.0530 0.0983  75  ASN A C   
638  O  O   . ASN A  76  ? 0.1664  0.1588 0.1908  -0.0430 -0.0436 0.0803  75  ASN A O   
639  C  CB  . ASN A  76  ? 0.1330  0.1998 0.3219  0.0330  0.0162  0.1271  75  ASN A CB  
640  C  CG  . ASN A  76  ? 0.1434  0.1635 0.4694  0.0069  0.0466  0.0385  75  ASN A CG  
641  O  OD1 . ASN A  76  ? 0.1835  0.1305 0.5865  0.0118  0.0303  0.0715  75  ASN A OD1 
642  N  ND2 . ASN A  76  ? 0.1682  0.2285 0.6652  0.0223  0.0505  0.1439  75  ASN A ND2 
643  N  N   . ARG A  77  ? 0.1520  0.1207 0.1280  -0.0357 -0.0089 0.0458  76  ARG A N   
644  C  CA  . ARG A  77  ? 0.1262  0.1305 0.1341  0.0011  0.0026  0.0181  76  ARG A CA  
645  C  C   . ARG A  77  ? 0.1438  0.0757 0.0804  -0.0041 -0.0209 -0.0316 76  ARG A C   
646  O  O   . ARG A  77  ? 0.1610  0.1032 0.1234  -0.0245 -0.0121 -0.0117 76  ARG A O   
647  C  CB  . ARG A  77  ? 0.1513  0.1220 0.1181  -0.0306 -0.0181 0.0397  76  ARG A CB  
648  C  CG  . ARG A  77  ? 0.1768  0.1118 0.1581  -0.0346 -0.0306 0.0419  76  ARG A CG  
649  C  CD  . ARG A  77  ? 0.2027  0.1581 0.1380  -0.0245 -0.0302 0.0461  76  ARG A CD  
650  N  NE  . ARG A  77  ? 0.1815  0.1720 0.1635  -0.0536 -0.0075 0.0421  76  ARG A NE  
651  C  CZ  . ARG A  77  ? 0.2055  0.2152 0.2217  -0.0362 -0.0331 0.0602  76  ARG A CZ  
652  N  NH1 . ARG A  77  ? 0.2508  0.2319 0.2293  -0.0379 -0.0888 0.0767  76  ARG A NH1 
653  N  NH2 . ARG A  77  ? 0.3365  0.3114 0.1474  -0.1002 0.0050  0.0355  76  ARG A NH2 
654  N  N   . SER A  78  ? 0.1531  0.0496 0.1312  -0.0076 -0.0173 0.0454  77  SER A N   
655  C  CA  . SER A  78  ? 0.1253  0.0894 0.1136  -0.0212 -0.0210 0.0457  77  SER A CA  
656  C  C   . SER A  78  ? 0.1384  0.0788 0.1090  -0.0209 -0.0071 0.0325  77  SER A C   
657  O  O   . SER A  78  ? 0.1164  0.1057 0.1430  -0.0099 -0.0026 0.0103  77  SER A O   
658  C  CB  . SER A  78  ? 0.1208  0.1084 0.1319  0.0059  -0.0384 0.0172  77  SER A CB  
659  O  OG  . SER A  78  ? 0.1398  0.0973 0.1102  -0.0022 -0.0171 0.0078  77  SER A OG  
660  N  N   . VAL A  79  ? 0.1032  0.1247 0.1107  -0.0074 -0.0258 0.0287  78  VAL A N   
661  C  CA  . VAL A  79  ? 0.1195  0.1265 0.1307  -0.0175 -0.0263 0.0430  78  VAL A CA  
662  C  C   . VAL A  79  ? 0.1181  0.1239 0.1054  -0.0015 -0.0233 0.0207  78  VAL A C   
663  O  O   . VAL A  79  ? 0.1567  0.1208 0.1294  0.0053  -0.0245 0.0068  78  VAL A O   
664  C  CB  . VAL A  79  ? 0.1224  0.1782 0.1976  -0.0378 -0.0427 0.0577  78  VAL A CB  
665  C  CG1 . VAL A  79  ? 0.1492  0.2156 0.2308  -0.0477 -0.0058 0.0854  78  VAL A CG1 
666  C  CG2 . VAL A  79  ? 0.1689  0.2117 0.2224  -0.0709 -0.0774 0.0165  78  VAL A CG2 
667  N  N   . LEU A  80  ? 0.1377  0.1101 0.1195  -0.0011 -0.0127 0.0272  79  LEU A N   
668  C  CA  . LEU A  80  ? 0.1208  0.1312 0.1099  -0.0185 -0.0145 0.0233  79  LEU A CA  
669  C  C   . LEU A  80  ? 0.1359  0.1276 0.1355  -0.0171 -0.0229 0.0166  79  LEU A C   
670  O  O   . LEU A  80  ? 0.1238  0.1761 0.1506  -0.0176 -0.0151 0.0225  79  LEU A O   
671  C  CB  . LEU A  80  ? 0.1337  0.1120 0.1204  -0.0116 -0.0156 0.0188  79  LEU A CB  
672  C  CG  . LEU A  80  ? 0.1280  0.1172 0.1276  -0.0100 -0.0207 0.0248  79  LEU A CG  
673  C  CD1 . LEU A  80  ? 0.1858  0.1700 0.1256  -0.0228 0.0072  -0.0003 79  LEU A CD1 
674  C  CD2 . LEU A  80  ? 0.1707  0.1223 0.1463  -0.0215 -0.0293 0.0241  79  LEU A CD2 
675  N  N   . LYS A  81  ? 0.1412  0.1689 0.1165  -0.0287 -0.0366 0.0233  80  LYS A N   
676  C  CA  . LYS A  81  ? 0.1483  0.2494 0.1448  -0.0759 -0.0620 0.0625  80  LYS A CA  
677  C  C   . LYS A  81  ? 0.1283  0.1635 0.1199  -0.0337 -0.0361 0.0145  80  LYS A C   
678  O  O   . LYS A  81  ? 0.1176  0.1700 0.1384  -0.0124 -0.0335 0.0241  80  LYS A O   
679  C  CB  . LYS A  81  ? 0.3093  0.3869 0.2543  -0.2223 -0.1577 0.1613  80  LYS A CB  
680  C  CG  . LYS A  81  ? 0.3606  0.3280 0.4345  -0.1681 -0.1038 0.0847  80  LYS A CG  
681  C  CD  . LYS A  81  ? 0.6178  0.4493 0.4404  -0.2301 -0.0479 -0.2385 80  LYS A CD  
682  C  CE  . LYS A  81  ? 0.7548  0.3851 0.4938  -0.3366 0.1574  -0.0061 80  LYS A CE  
683  N  N   . GLY A  82  ? 0.1283  0.1585 0.1423  -0.0102 -0.0353 0.0151  81  GLY A N   
684  C  CA  . GLY A  82  ? 0.1646  0.1549 0.1208  -0.0237 -0.0436 0.0214  81  GLY A CA  
685  C  C   . GLY A  82  ? 0.1283  0.1544 0.1046  0.0033  -0.0394 0.0041  81  GLY A C   
686  O  O   . GLY A  82  ? 0.1492  0.1635 0.1164  0.0163  -0.0160 0.0017  81  GLY A O   
687  N  N   . GLY A  83  ? 0.1445  0.1682 0.1384  -0.0172 -0.0254 -0.0039 82  GLY A N   
688  C  CA  . GLY A  83  ? 0.1373  0.1488 0.1585  -0.0055 -0.0378 -0.0041 82  GLY A CA  
689  C  C   . GLY A  83  ? 0.1420  0.1614 0.1083  -0.0184 -0.0307 0.0195  82  GLY A C   
690  O  O   . GLY A  83  ? 0.1606  0.1854 0.1120  -0.0124 -0.0494 0.0215  82  GLY A O   
691  N  N   . PRO A  84  ? 0.1283  0.1481 0.1127  0.0006  -0.0265 0.0099  83  PRO A N   
692  C  CA  . PRO A  84  ? 0.1524  0.1542 0.1330  -0.0038 -0.0016 0.0165  83  PRO A CA  
693  C  C   . PRO A  84  ? 0.1093  0.1757 0.1333  0.0033  -0.0263 0.0125  83  PRO A C   
694  O  O   . PRO A  84  ? 0.1337  0.2145 0.1678  0.0177  -0.0294 0.0410  83  PRO A O   
695  C  CB  . PRO A  84  ? 0.1585  0.1513 0.1232  -0.0177 -0.0232 0.0220  83  PRO A CB  
696  C  CG  . PRO A  84  ? 0.1368  0.1452 0.1391  0.0024  -0.0151 0.0009  83  PRO A CG  
697  C  CD  . PRO A  84  ? 0.1337  0.1628 0.1301  -0.0067 -0.0222 -0.0065 83  PRO A CD  
698  N  N   . PHE A  85  ? 0.1395  0.1736 0.1127  -0.0129 -0.0147 0.0099  84  PHE A N   
699  C  CA  . PHE A  85  ? 0.1366  0.2142 0.1239  -0.0057 -0.0189 0.0396  84  PHE A CA  
700  C  C   . PHE A  85  ? 0.1456  0.2447 0.1668  -0.0092 -0.0497 0.0475  84  PHE A C   
701  O  O   . PHE A  85  ? 0.1914  0.2921 0.2543  -0.0785 -0.0629 0.0055  84  PHE A O   
702  C  CB  . PHE A  85  ? 0.1463  0.1653 0.1391  -0.0271 -0.0329 0.0275  84  PHE A CB  
703  C  CG  . PHE A  85  ? 0.1621  0.1585 0.1016  -0.0262 -0.0064 0.0166  84  PHE A CG  
704  C  CD1 . PHE A  85  ? 0.2382  0.1603 0.1445  -0.0433 0.0018  0.0251  84  PHE A CD1 
705  C  CD2 . PHE A  85  ? 0.1506  0.2310 0.1161  -0.0403 -0.0504 0.0358  84  PHE A CD2 
706  C  CE1 . PHE A  85  ? 0.2486  0.1822 0.1206  -0.0791 0.0063  0.0311  84  PHE A CE1 
707  C  CE2 . PHE A  85  ? 0.1775  0.2479 0.1287  -0.0515 -0.0545 0.0523  84  PHE A CE2 
708  C  CZ  . PHE A  85  ? 0.2152  0.2380 0.0978  -0.0359 -0.0514 0.0480  84  PHE A CZ  
709  N  N   A SER A  86  ? 0.1441  0.3355 0.2386  0.0311  -0.0383 0.1066  85  SER A N   
710  N  N   B SER A  86  ? 0.1362  0.3273 0.2633  -0.0144 -0.0200 0.0924  85  SER A N   
711  C  CA  A SER A  86  ? 0.1283  0.4681 0.4074  -0.0484 -0.0956 0.0666  85  SER A CA  
712  C  CA  B SER A  86  ? 0.1243  0.3589 0.2651  -0.0463 -0.0388 0.1149  85  SER A CA  
713  C  C   A SER A  86  ? 0.1465  0.4447 0.3714  -0.1188 0.0027  0.0648  85  SER A C   
714  C  C   B SER A  86  ? 0.2709  0.3211 0.2529  -0.1264 -0.0535 0.0934  85  SER A C   
715  O  O   A SER A  86  ? 0.2522  0.4404 0.6759  -0.0252 0.1801  0.0303  85  SER A O   
716  O  O   B SER A  86  ? 0.2224  0.4419 0.4365  -0.1833 -0.1072 0.1949  85  SER A O   
717  C  CB  A SER A  86  ? 0.1930  0.5457 0.3398  0.0580  -0.0729 0.1596  85  SER A CB  
718  C  CB  B SER A  86  ? 0.1574  0.4063 0.3244  0.0108  -0.0186 0.1761  85  SER A CB  
719  O  OG  A SER A  86  ? 0.1817  0.5455 0.3147  0.0102  -0.1163 0.1368  85  SER A OG  
720  O  OG  B SER A  86  ? 0.1137  0.4577 0.5001  0.0394  -0.0118 0.0749  85  SER A OG  
721  N  N   . ASP A  87  ? 0.1743  0.3643 0.3420  -0.0410 -0.0860 0.1523  86  ASP A N   
722  C  CA  . ASP A  87  ? 0.1700  0.4982 0.3631  0.0020  -0.0510 0.2566  86  ASP A CA  
723  C  C   . ASP A  87  ? 0.1538  0.2842 0.2009  -0.0236 -0.0100 0.0844  86  ASP A C   
724  O  O   . ASP A  87  ? 0.1463  0.2744 0.2048  -0.0248 -0.0223 0.0780  86  ASP A O   
725  C  CB  . ASP A  87  ? 0.3370  0.6524 0.4609  0.1332  0.2293  0.0723  86  ASP A CB  
726  C  CG  . ASP A  87  ? 0.2928  0.5646 0.8174  -0.0013 -0.1307 -0.0219 86  ASP A CG  
727  O  OD1 . ASP A  87  ? 0.2089  0.6053 0.4318  -0.0356 -0.0201 -0.0232 86  ASP A OD1 
728  O  OD2 . ASP A  87  ? 0.3574  0.6910 0.3377  0.0509  -0.2097 -0.0966 86  ASP A OD2 
729  N  N   . SER A  88  ? 0.1241  0.2594 0.2364  -0.0692 -0.0491 0.0789  87  SER A N   
730  C  CA  . SER A  88  ? 0.1395  0.1847 0.2143  -0.0318 -0.0417 0.0012  87  SER A CA  
731  C  C   . SER A  88  ? 0.1276  0.1434 0.1840  -0.0369 -0.0118 0.0253  87  SER A C   
732  O  O   . SER A  88  ? 0.1160  0.2152 0.2375  -0.0284 -0.0066 0.0174  87  SER A O   
733  C  CB  . SER A  88  ? 0.2346  0.1535 0.2066  -0.0434 -0.0785 -0.0107 87  SER A CB  
734  O  OG  . SER A  88  ? 0.3100  0.2572 0.2357  -0.0908 -0.0724 -0.0286 87  SER A OG  
735  N  N   . TYR A  89  ? 0.1050  0.1172 0.1750  -0.0238 -0.0329 0.0208  88  TYR A N   
736  C  CA  . TYR A  89  ? 0.1063  0.1238 0.1581  -0.0108 -0.0152 0.0203  88  TYR A CA  
737  C  C   . TYR A  89  ? 0.0960  0.1272 0.1434  0.0039  -0.0027 0.0131  88  TYR A C   
738  O  O   . TYR A  89  ? 0.1650  0.1775 0.1513  0.0531  0.0273  0.0403  88  TYR A O   
739  C  CB  . TYR A  89  ? 0.1056  0.1107 0.1872  -0.0114 -0.0215 0.0259  88  TYR A CB  
740  C  CG  . TYR A  89  ? 0.0882  0.1169 0.1333  -0.0147 -0.0041 0.0110  88  TYR A CG  
741  C  CD1 . TYR A  89  ? 0.1289  0.1481 0.1265  -0.0001 -0.0065 0.0248  88  TYR A CD1 
742  C  CD2 . TYR A  89  ? 0.1199  0.1022 0.1316  -0.0179 0.0015  0.0132  88  TYR A CD2 
743  C  CE1 . TYR A  89  ? 0.1520  0.1474 0.1132  -0.0013 0.0042  0.0324  88  TYR A CE1 
744  C  CE2 . TYR A  89  ? 0.1091  0.1434 0.1231  -0.0062 0.0135  0.0351  88  TYR A CE2 
745  C  CZ  . TYR A  89  ? 0.1142  0.1409 0.1294  0.0074  0.0111  0.0188  88  TYR A CZ  
746  O  OH  . TYR A  89  ? 0.1483  0.1664 0.1606  0.0375  0.0010  0.0414  88  TYR A OH  
747  N  N   A ARG A  90  ? 0.0837  0.1160 0.1377  -0.0164 -0.0036 0.0190  89  ARG A N   
748  N  N   B ARG A  90  ? 0.0820  0.1172 0.1373  -0.0190 -0.0062 0.0194  89  ARG A N   
749  C  CA  A ARG A  90  ? 0.1023  0.1287 0.1220  -0.0163 -0.0013 0.0159  89  ARG A CA  
750  C  CA  B ARG A  90  ? 0.1028  0.1344 0.1276  -0.0164 -0.0053 0.0200  89  ARG A CA  
751  C  C   A ARG A  90  ? 0.1090  0.0973 0.0924  -0.0089 0.0093  0.0240  89  ARG A C   
752  C  C   B ARG A  90  ? 0.1089  0.0985 0.0933  -0.0085 0.0098  0.0223  89  ARG A C   
753  O  O   A ARG A  90  ? 0.1208  0.1005 0.1093  0.0008  0.0029  0.0109  89  ARG A O   
754  O  O   B ARG A  90  ? 0.1023  0.0914 0.1181  -0.0104 0.0091  0.0211  89  ARG A O   
755  C  CB  A ARG A  90  ? 0.1312  0.1362 0.1635  -0.0183 0.0446  0.0279  89  ARG A CB  
756  C  CB  B ARG A  90  ? 0.1588  0.0864 0.1456  -0.0182 0.0300  -0.0004 89  ARG A CB  
757  C  CG  A ARG A  90  ? 0.2669  0.1118 0.1028  0.0037  0.0294  -0.0087 89  ARG A CG  
758  C  CG  B ARG A  90  ? 0.1502  0.1355 0.1750  0.0126  0.1026  0.0960  89  ARG A CG  
759  C  CD  A ARG A  90  ? 0.3728  0.0759 0.1912  -0.0005 0.1322  -0.0410 89  ARG A CD  
760  C  CD  B ARG A  90  ? 0.1373  0.1344 0.1441  -0.0383 0.0107  0.0467  89  ARG A CD  
761  N  NE  A ARG A  90  ? 0.2913  0.0847 0.2458  0.0135  0.1297  0.0630  89  ARG A NE  
762  N  NE  B ARG A  90  ? 0.1366  0.1883 0.1969  -0.0239 -0.0227 0.0761  89  ARG A NE  
763  C  CZ  A ARG A  90  ? 0.1883  0.1754 0.1159  -0.0118 -0.0664 -0.0119 89  ARG A CZ  
764  C  CZ  B ARG A  90  ? 0.1205  0.0910 0.2249  -0.0397 -0.0373 0.0298  89  ARG A CZ  
765  N  NH1 A ARG A  90  ? 0.2321  0.2590 0.0794  -0.0144 -0.0432 0.0829  89  ARG A NH1 
766  N  NH1 B ARG A  90  ? 0.1987  0.1215 0.1847  0.0062  0.0095  0.0475  89  ARG A NH1 
767  N  NH2 A ARG A  90  ? 0.1333  0.1998 0.2231  -0.0769 0.0174  0.0342  89  ARG A NH2 
768  N  NH2 B ARG A  90  ? 0.0554  0.2454 0.1817  -0.0129 0.0122  0.0218  89  ARG A NH2 
769  N  N   . LEU A  91  ? 0.0941  0.1076 0.1081  -0.0025 -0.0100 0.0063  90  LEU A N   
770  C  CA  . LEU A  91  ? 0.0952  0.1214 0.0907  -0.0051 -0.0052 0.0138  90  LEU A CA  
771  C  C   . LEU A  91  ? 0.1082  0.1002 0.0928  -0.0133 0.0100  0.0233  90  LEU A C   
772  O  O   . LEU A  91  ? 0.1544  0.1216 0.1014  -0.0233 0.0150  0.0176  90  LEU A O   
773  C  CB  . LEU A  91  ? 0.1076  0.1100 0.1234  0.0027  -0.0157 0.0006  90  LEU A CB  
774  C  CG  . LEU A  91  ? 0.1120  0.1128 0.1003  0.0006  -0.0016 0.0120  90  LEU A CG  
775  C  CD1 . LEU A  91  ? 0.1216  0.1203 0.1215  -0.0208 -0.0023 0.0265  90  LEU A CD1 
776  C  CD2 . LEU A  91  ? 0.1230  0.1155 0.1185  0.0030  -0.0013 0.0085  90  LEU A CD2 
777  N  N   A PHE A  92  ? 0.0959  0.1080 0.1093  -0.0119 -0.0047 0.0031  91  PHE A N   
778  N  N   B PHE A  92  ? 0.1067  0.1090 0.0770  -0.0116 -0.0103 0.0134  91  PHE A N   
779  C  CA  A PHE A  92  ? 0.0944  0.1359 0.1177  0.0238  0.0002  -0.0022 91  PHE A CA  
780  C  CA  B PHE A  92  ? 0.1067  0.1483 0.0793  0.0136  -0.0302 -0.0158 91  PHE A CA  
781  C  C   A PHE A  92  ? 0.1134  0.0865 0.0703  0.0087  -0.0032 0.0012  91  PHE A C   
782  C  C   B PHE A  92  ? 0.1082  0.1198 0.0633  -0.0075 0.0036  -0.0002 91  PHE A C   
783  O  O   A PHE A  92  ? 0.1274  0.1272 0.0829  -0.0060 -0.0190 0.0226  91  PHE A O   
784  O  O   B PHE A  92  ? 0.1312  0.1197 0.0812  0.0009  -0.0116 0.0181  91  PHE A O   
785  C  CB  A PHE A  92  ? 0.1176  0.1134 0.1423  0.0196  -0.0272 0.0065  91  PHE A CB  
786  C  CB  B PHE A  92  ? 0.1146  0.1592 0.0953  0.0067  0.0025  0.0167  91  PHE A CB  
787  C  CG  A PHE A  92  ? 0.1224  0.1592 0.1574  0.0465  0.0201  -0.0227 91  PHE A CG  
788  C  CG  B PHE A  92  ? 0.1305  0.1474 0.1216  0.0035  0.0387  -0.0008 91  PHE A CG  
789  C  CD1 A PHE A  92  ? 0.1316  0.1657 0.1307  0.0228  0.0181  -0.0326 91  PHE A CD1 
790  C  CD1 B PHE A  92  ? 0.0873  0.1650 0.1430  -0.0216 0.0025  -0.0133 91  PHE A CD1 
791  C  CD2 A PHE A  92  ? 0.1196  0.2102 0.1908  0.0055  0.0171  -0.0207 91  PHE A CD2 
792  C  CD2 B PHE A  92  ? 0.1197  0.1621 0.1326  0.0145  0.0099  -0.0104 91  PHE A CD2 
793  C  CE1 A PHE A  92  ? 0.2267  0.1588 0.1368  0.0574  0.0566  -0.0541 91  PHE A CE1 
794  C  CE1 B PHE A  92  ? 0.1118  0.1452 0.1239  -0.0145 0.0314  -0.0109 91  PHE A CE1 
795  C  CE2 A PHE A  92  ? 0.2217  0.2229 0.2418  0.0622  0.0260  -0.1362 91  PHE A CE2 
796  C  CE2 B PHE A  92  ? 0.0953  0.1544 0.1520  0.0133  0.0151  -0.0284 91  PHE A CE2 
797  C  CZ  A PHE A  92  ? 0.1926  0.3244 0.1319  0.0411  0.0342  -0.1540 91  PHE A CZ  
798  C  CZ  B PHE A  92  ? 0.0863  0.1912 0.1562  0.0064  -0.0156 -0.0252 91  PHE A CZ  
799  N  N   A GLN A  93  ? 0.0890  0.1251 0.0996  -0.0187 -0.0008 -0.0011 92  GLN A N   
800  N  N   B GLN A  93  ? 0.1178  0.1172 0.0844  -0.0145 0.0001  0.0206  92  GLN A N   
801  C  CA  A GLN A  93  ? 0.0844  0.1099 0.1040  -0.0132 -0.0032 0.0064  92  GLN A CA  
802  C  CA  B GLN A  93  ? 0.1220  0.1208 0.0888  -0.0320 0.0039  -0.0016 92  GLN A CA  
803  C  C   A GLN A  93  ? 0.1106  0.1120 0.1068  -0.0266 -0.0198 0.0234  92  GLN A C   
804  C  C   B GLN A  93  ? 0.1136  0.0960 0.0989  0.0048  -0.0212 0.0429  92  GLN A C   
805  O  O   A GLN A  93  ? 0.1064  0.1316 0.1283  0.0029  -0.0219 0.0446  92  GLN A O   
806  O  O   B GLN A  93  ? 0.1028  0.1256 0.0916  -0.0146 -0.0305 0.0407  92  GLN A O   
807  C  CB  A GLN A  93  ? 0.1380  0.1323 0.1153  -0.0074 0.0450  0.0185  92  GLN A CB  
808  C  CB  B GLN A  93  ? 0.2150  0.1445 0.2176  -0.0543 -0.0110 -0.0908 92  GLN A CB  
809  C  CG  A GLN A  93  ? 0.1574  0.2102 0.1747  0.0316  -0.0657 0.0064  92  GLN A CG  
810  C  CG  B GLN A  93  ? 0.2637  0.1833 0.2658  -0.1062 0.0497  0.0200  92  GLN A CG  
811  C  CD  A GLN A  93  ? 0.1230  0.1316 0.1901  0.0042  0.0563  0.0105  92  GLN A CD  
812  C  CD  B GLN A  93  ? 0.1664  0.1100 0.1822  -0.0184 0.0691  -0.0245 92  GLN A CD  
813  O  OE1 A GLN A  93  ? 0.1359  0.2178 0.1420  -0.0516 0.0181  0.0129  92  GLN A OE1 
814  O  OE1 B GLN A  93  ? 0.1430  0.0642 0.1474  -0.0111 0.0411  0.0236  92  GLN A OE1 
815  N  NE2 A GLN A  93  ? 0.2240  0.2465 0.2016  -0.1118 0.1342  -0.0700 92  GLN A NE2 
816  N  NE2 B GLN A  93  ? 0.2389  0.1973 0.3114  -0.1254 0.1852  -0.1267 92  GLN A NE2 
817  N  N   . PHE A  94  ? 0.1030  0.0928 0.0908  -0.0108 -0.0179 0.0051  93  PHE A N   
818  C  CA  . PHE A  94  ? 0.0979  0.1030 0.0812  -0.0186 -0.0153 0.0043  93  PHE A CA  
819  C  C   . PHE A  94  ? 0.1146  0.0901 0.0641  0.0060  -0.0194 0.0004  93  PHE A C   
820  O  O   . PHE A  94  ? 0.1128  0.1119 0.0715  0.0018  -0.0268 0.0125  93  PHE A O   
821  C  CB  . PHE A  94  ? 0.1137  0.0958 0.0873  0.0063  -0.0223 0.0102  93  PHE A CB  
822  C  CG  . PHE A  94  ? 0.1190  0.0935 0.0688  0.0033  -0.0055 0.0095  93  PHE A CG  
823  C  CD1 . PHE A  94  ? 0.1117  0.1272 0.0978  0.0000  -0.0205 0.0081  93  PHE A CD1 
824  C  CD2 . PHE A  94  ? 0.1470  0.0979 0.0732  0.0099  -0.0086 -0.0013 93  PHE A CD2 
825  C  CE1 . PHE A  94  ? 0.1180  0.1120 0.1076  0.0006  -0.0138 -0.0102 93  PHE A CE1 
826  C  CE2 . PHE A  94  ? 0.1171  0.1204 0.0917  0.0005  -0.0199 -0.0013 93  PHE A CE2 
827  C  CZ  . PHE A  94  ? 0.1217  0.1102 0.0933  0.0088  0.0001  -0.0134 93  PHE A CZ  
828  N  N   . HIS A  95  ? 0.1032  0.0765 0.1014  -0.0069 -0.0137 0.0015  94  HIS A N   
829  C  CA  . HIS A  95  ? 0.0993  0.0792 0.0784  -0.0071 -0.0178 -0.0001 94  HIS A CA  
830  C  C   . HIS A  95  ? 0.1029  0.0820 0.0757  -0.0038 -0.0216 0.0087  94  HIS A C   
831  O  O   . HIS A  95  ? 0.1059  0.0989 0.0761  -0.0071 -0.0216 0.0121  94  HIS A O   
832  C  CB  . HIS A  95  ? 0.1187  0.0891 0.0786  0.0041  -0.0286 -0.0059 94  HIS A CB  
833  C  CG  . HIS A  95  ? 0.0915  0.0943 0.0688  -0.0026 -0.0065 0.0022  94  HIS A CG  
834  N  ND1 . HIS A  95  ? 0.1038  0.0908 0.1189  -0.0039 -0.0021 0.0189  94  HIS A ND1 
835  C  CD2 . HIS A  95  ? 0.1058  0.0961 0.0847  0.0111  -0.0113 -0.0062 94  HIS A CD2 
836  C  CE1 . HIS A  95  ? 0.1083  0.0776 0.1179  0.0006  -0.0081 0.0118  94  HIS A CE1 
837  N  NE2 . HIS A  95  ? 0.1040  0.0856 0.0881  -0.0031 -0.0082 0.0013  94  HIS A NE2 
838  N  N   . PHE A  96  ? 0.0900  0.0795 0.0831  -0.0067 -0.0097 0.0020  95  PHE A N   
839  C  CA  . PHE A  96  ? 0.0865  0.0873 0.0917  -0.0137 -0.0047 0.0016  95  PHE A CA  
840  C  C   . PHE A  96  ? 0.0935  0.0835 0.0725  -0.0018 -0.0196 -0.0081 95  PHE A C   
841  O  O   . PHE A  96  ? 0.1153  0.0973 0.0840  -0.0075 -0.0111 -0.0078 95  PHE A O   
842  C  CB  . PHE A  96  ? 0.1030  0.0944 0.1041  0.0023  -0.0248 -0.0111 95  PHE A CB  
843  C  CG  . PHE A  96  ? 0.0952  0.0982 0.0926  0.0003  -0.0201 -0.0037 95  PHE A CG  
844  C  CD1 . PHE A  96  ? 0.1190  0.0989 0.1004  0.0073  -0.0266 0.0073  95  PHE A CD1 
845  C  CD2 . PHE A  96  ? 0.0935  0.1128 0.0979  0.0142  -0.0262 -0.0124 95  PHE A CD2 
846  C  CE1 . PHE A  96  ? 0.1185  0.1007 0.1076  0.0054  -0.0375 -0.0083 95  PHE A CE1 
847  C  CE2 . PHE A  96  ? 0.1144  0.1135 0.1082  0.0161  -0.0326 -0.0088 95  PHE A CE2 
848  C  CZ  . PHE A  96  ? 0.1106  0.1217 0.1023  0.0063  -0.0401 -0.0047 95  PHE A CZ  
849  N  N   . HIS A  97  ? 0.0950  0.0806 0.0838  -0.0010 -0.0201 0.0076  96  HIS A N   
850  C  CA  . HIS A  97  ? 0.0960  0.0747 0.1058  0.0006  -0.0046 0.0042  96  HIS A CA  
851  C  C   . HIS A  97  ? 0.0801  0.0935 0.0750  0.0105  -0.0190 -0.0088 96  HIS A C   
852  O  O   . HIS A  97  ? 0.1111  0.0978 0.0915  -0.0020 -0.0109 -0.0121 96  HIS A O   
853  C  CB  . HIS A  97  ? 0.0835  0.0917 0.1111  0.0091  -0.0162 0.0074  96  HIS A CB  
854  C  CG  . HIS A  97  ? 0.0849  0.0988 0.0820  0.0100  -0.0097 0.0029  96  HIS A CG  
855  N  ND1 . HIS A  97  ? 0.1092  0.1014 0.0935  0.0113  -0.0047 -0.0026 96  HIS A ND1 
856  C  CD2 . HIS A  97  ? 0.0786  0.1023 0.0919  -0.0091 -0.0124 0.0198  96  HIS A CD2 
857  C  CE1 . HIS A  97  ? 0.1038  0.1029 0.1058  -0.0035 -0.0131 0.0022  96  HIS A CE1 
858  N  NE2 . HIS A  97  ? 0.1067  0.1020 0.0856  0.0136  -0.0080 -0.0042 96  HIS A NE2 
859  N  N   . TRP A  98  ? 0.1044  0.0985 0.0856  -0.0081 -0.0168 -0.0024 97  TRP A N   
860  C  CA  . TRP A  98  ? 0.0819  0.0952 0.1092  -0.0068 -0.0065 -0.0089 97  TRP A CA  
861  C  C   . TRP A  98  ? 0.1037  0.1059 0.0845  -0.0152 -0.0075 -0.0087 97  TRP A C   
862  O  O   . TRP A  98  ? 0.1189  0.1133 0.1023  -0.0054 -0.0059 -0.0148 97  TRP A O   
863  C  CB  . TRP A  98  ? 0.1143  0.1199 0.1049  0.0019  -0.0165 0.0083  97  TRP A CB  
864  C  CG  . TRP A  98  ? 0.0881  0.1124 0.1014  -0.0003 -0.0110 -0.0018 97  TRP A CG  
865  C  CD1 . TRP A  98  ? 0.0982  0.1093 0.1137  0.0006  -0.0168 0.0055  97  TRP A CD1 
866  C  CD2 . TRP A  98  ? 0.0873  0.1185 0.0955  -0.0012 -0.0200 0.0049  97  TRP A CD2 
867  N  NE1 . TRP A  98  ? 0.1068  0.1168 0.1097  -0.0069 -0.0187 0.0083  97  TRP A NE1 
868  C  CE2 . TRP A  98  ? 0.0979  0.0995 0.0955  0.0058  -0.0234 -0.0060 97  TRP A CE2 
869  C  CE3 . TRP A  98  ? 0.0962  0.1071 0.1080  0.0004  -0.0140 0.0067  97  TRP A CE3 
870  C  CZ2 . TRP A  98  ? 0.1011  0.1128 0.1097  0.0094  -0.0096 0.0096  97  TRP A CZ2 
871  C  CZ3 . TRP A  98  ? 0.1072  0.1046 0.1065  0.0136  -0.0238 0.0062  97  TRP A CZ3 
872  C  CH2 . TRP A  98  ? 0.1040  0.1168 0.1254  0.0034  -0.0386 -0.0093 97  TRP A CH2 
873  N  N   . GLY A  99  ? 0.1046  0.1048 0.1235  -0.0155 -0.0119 0.0000  98  GLY A N   
874  C  CA  . GLY A  99  ? 0.1259  0.1190 0.1779  -0.0515 -0.0263 -0.0211 98  GLY A CA  
875  C  C   . GLY A  99  ? 0.1438  0.1571 0.1614  -0.0337 0.0227  -0.0414 98  GLY A C   
876  O  O   . GLY A  99  ? 0.1106  0.2084 0.1434  -0.0132 -0.0109 -0.0550 98  GLY A O   
877  N  N   A SER A  100 ? 0.2169  0.1761 0.1492  -0.0824 0.0066  -0.0538 99  SER A N   
878  N  N   B SER A  100 ? 0.1937  0.1610 0.1703  -0.0796 -0.0078 -0.0102 99  SER A N   
879  C  CA  A SER A  100 ? 0.1969  0.3201 0.2388  -0.0878 0.0117  -0.0606 99  SER A CA  
880  C  CA  B SER A  100 ? 0.2206  0.2436 0.1786  -0.1542 0.0272  -0.1263 99  SER A CA  
881  C  C   A SER A  100 ? 0.1635  0.1797 0.1434  -0.0611 -0.0321 0.0234  99  SER A C   
882  C  C   B SER A  100 ? 0.2053  0.4260 0.1664  -0.2031 0.0688  -0.1416 99  SER A C   
883  O  O   A SER A  100 ? 0.1761  0.2020 0.2084  -0.0175 -0.0631 0.0251  99  SER A O   
884  O  O   B SER A  100 ? 0.2381  0.4501 0.2132  -0.2378 0.0544  -0.1321 99  SER A O   
885  C  CB  A SER A  100 ? 0.4253  0.3829 0.2755  -0.0849 -0.0041 -0.1622 99  SER A CB  
886  C  CB  B SER A  100 ? 0.3549  0.1757 0.2321  -0.1147 0.0086  -0.0372 99  SER A CB  
887  O  OG  A SER A  100 ? 0.2795  0.2285 0.3869  -0.0955 -0.0265 -0.1051 99  SER A OG  
888  O  OG  B SER A  100 ? 0.2436  0.2788 0.2888  -0.0586 -0.0337 -0.0820 99  SER A OG  
889  N  N   A THR A  101 ? 0.1596  0.1355 0.1520  -0.0266 -0.0111 -0.0088 100 THR A N   
890  N  N   B THR A  101 ? 0.2676  0.3006 0.1588  -0.1966 0.0941  -0.1245 100 THR A N   
891  C  CA  A THR A  101 ? 0.2212  0.1380 0.1786  -0.1018 0.0614  -0.0250 100 THR A CA  
892  C  CA  B THR A  101 ? 0.3164  0.2644 0.1229  -0.1559 0.1043  -0.0842 100 THR A CA  
893  C  C   A THR A  101 ? 0.2346  0.1535 0.1847  -0.1073 0.0390  -0.0241 100 THR A C   
894  C  C   B THR A  101 ? 0.3229  0.1416 0.1908  -0.0670 0.0417  -0.1015 100 THR A C   
895  O  O   A THR A  101 ? 0.2364  0.1495 0.1635  -0.1315 0.0303  -0.0661 100 THR A O   
896  O  O   B THR A  101 ? 0.2745  0.2048 0.2174  -0.0527 0.0998  0.0016  100 THR A O   
897  C  CB  A THR A  101 ? 0.1804  0.1682 0.1260  -0.0735 0.0174  0.0043  100 THR A CB  
898  C  CB  B THR A  101 ? 0.2185  0.2055 0.1912  -0.0886 0.0100  -0.0324 100 THR A CB  
899  O  OG1 A THR A  101 ? 0.2522  0.1395 0.1556  -0.0623 0.0044  0.0310  100 THR A OG1 
900  O  OG1 B THR A  101 ? 0.1775  0.2009 0.3172  -0.0427 -0.0553 -0.0008 100 THR A OG1 
901  C  CG2 A THR A  101 ? 0.2357  0.1168 0.2339  -0.1061 -0.0573 0.0158  100 THR A CG2 
902  C  CG2 B THR A  101 ? 0.1854  0.2002 0.2357  -0.0578 0.0241  -0.0505 100 THR A CG2 
903  N  N   . ASN A  102 ? 0.2314  0.1362 0.1653  -0.0697 0.0323  -0.0337 101 ASN A N   
904  C  CA  . ASN A  102 ? 0.2059  0.1287 0.1169  -0.0237 0.0118  -0.0091 101 ASN A CA  
905  C  C   . ASN A  102 ? 0.1696  0.1233 0.1747  -0.0242 0.0134  0.0052  101 ASN A C   
906  O  O   . ASN A  102 ? 0.2073  0.1312 0.1782  -0.0122 -0.0027 0.0199  101 ASN A O   
907  C  CB  . ASN A  102 ? 0.2131  0.1445 0.1416  0.0252  -0.0044 0.0076  101 ASN A CB  
908  C  CG  . ASN A  102 ? 0.2005  0.1768 0.2095  -0.0774 -0.0734 0.0083  101 ASN A CG  
909  O  OD1 . ASN A  102 ? 0.2579  0.2138 0.2196  -0.0474 -0.0791 0.0577  101 ASN A OD1 
910  N  ND2 . ASN A  102 ? 0.1764  0.1720 0.3233  -0.0387 -0.0672 0.0184  101 ASN A ND2 
911  N  N   . GLU A  103 ? 0.1465  0.1416 0.2142  -0.0068 0.0447  0.0271  102 GLU A N   
912  C  CA  . GLU A  103 ? 0.1524  0.1646 0.2551  -0.0078 0.0311  0.0610  102 GLU A CA  
913  C  C   . GLU A  103 ? 0.1614  0.1377 0.2095  0.0124  0.0370  0.0447  102 GLU A C   
914  O  O   . GLU A  103 ? 0.1725  0.2508 0.1973  0.0060  0.0256  0.0705  102 GLU A O   
915  C  CB  . GLU A  103 ? 0.1984  0.1754 0.3772  -0.0106 0.0465  0.0731  102 GLU A CB  
916  C  CG  . GLU A  103 ? 0.2662  0.3021 0.4695  -0.0522 0.1332  0.0644  102 GLU A CG  
917  C  CD  . GLU A  103 ? 0.4253  0.4451 0.9637  0.1326  0.0154  0.0915  102 GLU A CD  
918  O  OE1 . GLU A  103 ? 1.0354  1.0898 1.1964  -0.4306 0.3509  -0.2279 102 GLU A OE1 
919  O  OE2 . GLU A  103 ? 0.4546  0.4231 1.3112  0.1469  0.2554  -0.0640 102 GLU A OE2 
920  N  N   . HIS A  104 ? 0.1260  0.1434 0.1876  -0.0345 0.0187  0.0078  103 HIS A N   
921  C  CA  . HIS A  104 ? 0.1405  0.1316 0.1797  -0.0230 0.0114  0.0229  103 HIS A CA  
922  C  C   . HIS A  104 ? 0.1289  0.1675 0.1280  -0.0133 -0.0149 0.0052  103 HIS A C   
923  O  O   . HIS A  104 ? 0.1800  0.1474 0.1720  -0.0272 -0.0201 -0.0051 103 HIS A O   
924  C  CB  . HIS A  104 ? 0.1420  0.1538 0.2416  -0.0263 0.0189  -0.0166 103 HIS A CB  
925  C  CG  . HIS A  104 ? 0.1641  0.1650 0.2240  0.0021  -0.0121 0.0227  103 HIS A CG  
926  N  ND1 . HIS A  104 ? 0.1808  0.1887 0.3883  0.0048  -0.0205 0.0148  103 HIS A ND1 
927  C  CD2 . HIS A  104 ? 0.1395  0.2224 0.1463  0.0375  0.0061  0.0280  103 HIS A CD2 
928  C  CE1 . HIS A  104 ? 0.2224  0.1779 0.3700  0.0196  0.0351  -0.0066 103 HIS A CE1 
929  N  NE2 . HIS A  104 ? 0.1905  0.1811 0.1951  0.0070  0.0177  0.0004  103 HIS A NE2 
930  N  N   . GLY A  105 ? 0.1574  0.1790 0.1592  -0.0511 -0.0456 0.0286  104 GLY A N   
931  C  CA  . GLY A  105 ? 0.1465  0.1373 0.1409  -0.0370 -0.0436 0.0249  104 GLY A CA  
932  C  C   . GLY A  105 ? 0.1162  0.1280 0.1016  -0.0004 -0.0158 0.0047  104 GLY A C   
933  O  O   . GLY A  105 ? 0.1488  0.1333 0.1004  -0.0212 -0.0135 0.0137  104 GLY A O   
934  N  N   . SER A  106 ? 0.1065  0.1099 0.1102  0.0039  -0.0210 -0.0023 105 SER A N   
935  C  CA  . SER A  106 ? 0.0768  0.1155 0.1155  0.0094  -0.0145 -0.0190 105 SER A CA  
936  C  C   . SER A  106 ? 0.1076  0.1077 0.0944  -0.0030 -0.0001 0.0039  105 SER A C   
937  O  O   . SER A  106 ? 0.1268  0.1077 0.1391  -0.0145 -0.0043 -0.0006 105 SER A O   
938  C  CB  . SER A  106 ? 0.1181  0.1063 0.0917  -0.0024 -0.0070 0.0124  105 SER A CB  
939  O  OG  . SER A  106 ? 0.1032  0.1190 0.1146  -0.0027 -0.0034 0.0147  105 SER A OG  
940  N  N   . GLU A  107 ? 0.0897  0.1203 0.1073  0.0035  0.0035  0.0168  106 GLU A N   
941  C  CA  . GLU A  107 ? 0.0960  0.1137 0.1040  0.0138  -0.0033 0.0136  106 GLU A CA  
942  C  C   . GLU A  107 ? 0.0910  0.0970 0.1027  -0.0102 -0.0144 0.0234  106 GLU A C   
943  O  O   . GLU A  107 ? 0.1162  0.0989 0.1168  -0.0011 -0.0104 0.0140  106 GLU A O   
944  C  CB  . GLU A  107 ? 0.1080  0.1280 0.0786  0.0032  -0.0015 0.0150  106 GLU A CB  
945  C  CG  . GLU A  107 ? 0.1391  0.1980 0.0782  0.0171  0.0058  0.0142  106 GLU A CG  
946  C  CD  . GLU A  107 ? 0.1205  0.0951 0.0793  0.0051  -0.0212 -0.0066 106 GLU A CD  
947  O  OE1 . GLU A  107 ? 0.1289  0.1031 0.1254  -0.0013 -0.0093 -0.0048 106 GLU A OE1 
948  O  OE2 . GLU A  107 ? 0.1152  0.1003 0.1068  -0.0065 -0.0091 -0.0005 106 GLU A OE2 
949  N  N   . HIS A  108 ? 0.0962  0.1132 0.0829  -0.0089 -0.0025 0.0164  107 HIS A N   
950  C  CA  . HIS A  108 ? 0.1032  0.1162 0.0768  -0.0025 -0.0055 0.0116  107 HIS A CA  
951  C  C   . HIS A  108 ? 0.1003  0.0964 0.0926  0.0031  -0.0073 0.0095  107 HIS A C   
952  O  O   . HIS A  108 ? 0.1058  0.1136 0.1093  0.0071  -0.0011 0.0131  107 HIS A O   
953  C  CB  . HIS A  108 ? 0.0932  0.1067 0.1014  0.0003  -0.0041 0.0024  107 HIS A CB  
954  C  CG  . HIS A  108 ? 0.0994  0.0962 0.0862  0.0016  0.0013  0.0041  107 HIS A CG  
955  N  ND1 . HIS A  108 ? 0.1032  0.0985 0.0924  0.0006  -0.0053 0.0121  107 HIS A ND1 
956  C  CD2 . HIS A  108 ? 0.0890  0.1049 0.1036  -0.0031 -0.0005 0.0003  107 HIS A CD2 
957  C  CE1 . HIS A  108 ? 0.0932  0.0898 0.1016  0.0075  -0.0081 -0.0027 107 HIS A CE1 
958  N  NE2 . HIS A  108 ? 0.0890  0.0970 0.1106  -0.0002 -0.0084 0.0064  107 HIS A NE2 
959  N  N   . THR A  109 ? 0.1171  0.1084 0.0900  0.0003  0.0033  0.0234  108 THR A N   
960  C  CA  . THR A  109 ? 0.1283  0.1204 0.0871  -0.0159 0.0077  0.0234  108 THR A CA  
961  C  C   . THR A  109 ? 0.1053  0.1077 0.1027  -0.0025 0.0005  0.0172  108 THR A C   
962  O  O   . THR A  109 ? 0.1102  0.1195 0.1068  0.0019  0.0000  0.0197  108 THR A O   
963  C  CB  . THR A  109 ? 0.1196  0.1075 0.1280  0.0024  -0.0139 0.0168  108 THR A CB  
964  O  OG1 . THR A  109 ? 0.1254  0.1137 0.1492  -0.0050 0.0111  0.0211  108 THR A OG1 
965  C  CG2 . THR A  109 ? 0.1362  0.1544 0.1348  -0.0102 -0.0099 0.0057  108 THR A CG2 
966  N  N   . VAL A  110 ? 0.1257  0.1257 0.1098  -0.0053 0.0168  0.0184  109 VAL A N   
967  C  CA  . VAL A  110 ? 0.1405  0.1262 0.1023  -0.0089 0.0029  0.0199  109 VAL A CA  
968  C  C   . VAL A  110 ? 0.1326  0.1553 0.1159  -0.0086 0.0142  0.0161  109 VAL A C   
969  O  O   . VAL A  110 ? 0.1287  0.1800 0.1262  -0.0248 0.0197  0.0076  109 VAL A O   
970  C  CB  . VAL A  110 ? 0.1747  0.1441 0.1111  0.0030  0.0144  -0.0073 109 VAL A CB  
971  C  CG1 . VAL A  110 ? 0.1984  0.1817 0.1333  0.0066  -0.0238 -0.0087 109 VAL A CG1 
972  C  CG2 . VAL A  110 ? 0.2005  0.1257 0.1603  -0.0109 0.0068  0.0182  109 VAL A CG2 
973  N  N   . ASP A  111 ? 0.1520  0.1685 0.1145  -0.0134 0.0132  0.0310  110 ASP A N   
974  C  CA  . ASP A  111 ? 0.1596  0.2023 0.1076  -0.0352 0.0117  0.0406  110 ASP A CA  
975  C  C   . ASP A  111 ? 0.1499  0.1969 0.1217  -0.0293 0.0003  0.0442  110 ASP A C   
976  O  O   . ASP A  111 ? 0.1714  0.2138 0.1495  -0.0307 0.0166  0.0535  110 ASP A O   
977  C  CB  . ASP A  111 ? 0.1926  0.2235 0.1181  -0.0557 0.0140  0.0130  110 ASP A CB  
978  C  CG  . ASP A  111 ? 0.2150  0.2483 0.0937  -0.0531 0.0181  0.0068  110 ASP A CG  
979  O  OD1 . ASP A  111 ? 0.1944  0.3301 0.1430  -0.0310 0.0197  0.0139  110 ASP A OD1 
980  O  OD2 . ASP A  111 ? 0.2285  0.2587 0.1571  -0.0377 -0.0143 -0.0039 110 ASP A OD2 
981  N  N   . GLY A  112 ? 0.1632  0.1506 0.1186  -0.0002 -0.0068 0.0417  111 GLY A N   
982  C  CA  . GLY A  112 ? 0.1800  0.1603 0.1398  -0.0183 -0.0194 0.0425  111 GLY A CA  
983  C  C   . GLY A  112 ? 0.1639  0.1506 0.1499  -0.0267 0.0001  0.0525  111 GLY A C   
984  O  O   . GLY A  112 ? 0.1847  0.1531 0.1912  -0.0253 -0.0356 0.0192  111 GLY A O   
985  N  N   . VAL A  113 ? 0.1326  0.1535 0.1639  -0.0223 -0.0165 0.0539  112 VAL A N   
986  C  CA  . VAL A  113 ? 0.1409  0.1768 0.1312  0.0113  -0.0005 0.0472  112 VAL A CA  
987  C  C   . VAL A  113 ? 0.1241  0.1391 0.1312  -0.0011 -0.0067 0.0451  112 VAL A C   
988  O  O   . VAL A  113 ? 0.1280  0.1298 0.1391  -0.0141 0.0097  0.0233  112 VAL A O   
989  C  CB  . VAL A  113 ? 0.1603  0.1793 0.1596  0.0092  0.0077  0.0348  112 VAL A CB  
990  C  CG1 . VAL A  113 ? 0.1544  0.2145 0.1703  0.0190  0.0116  0.0326  112 VAL A CG1 
991  C  CG2 . VAL A  113 ? 0.1714  0.2662 0.1549  -0.0059 0.0261  0.0356  112 VAL A CG2 
992  N  N   . LYS A  114 ? 0.1470  0.1434 0.1330  -0.0118 -0.0219 0.0436  113 LYS A N   
993  C  CA  . LYS A  114 ? 0.1578  0.1145 0.1416  -0.0110 -0.0110 0.0300  113 LYS A CA  
994  C  C   . LYS A  114 ? 0.1203  0.1298 0.1423  -0.0081 0.0122  0.0271  113 LYS A C   
995  O  O   . LYS A  114 ? 0.1465  0.1459 0.2278  -0.0111 0.0378  0.0618  113 LYS A O   
996  C  CB  . LYS A  114 ? 0.1750  0.1423 0.1639  -0.0151 -0.0244 0.0060  113 LYS A CB  
997  C  CG  . LYS A  114 ? 0.1973  0.1330 0.2388  0.0168  -0.0311 -0.0133 113 LYS A CG  
998  C  CD  . LYS A  114 ? 0.2382  0.1919 0.3794  -0.0575 -0.0190 0.0074  113 LYS A CD  
999  C  CE  . LYS A  114 ? 0.5717  0.1632 0.6581  -0.0285 -0.1423 -0.0714 113 LYS A CE  
1000 N  NZ  . LYS A  114 ? 0.4374  0.2999 0.5788  -0.0957 -0.1346 0.0681  113 LYS A NZ  
1001 N  N   A TYR A  115 ? 0.0998  0.1127 0.0935  -0.0062 0.0029  0.0241  114 TYR A N   
1002 N  N   B TYR A  115 ? 0.1337  0.1055 0.1159  -0.0132 0.0004  0.0265  114 TYR A N   
1003 C  CA  A TYR A  115 ? 0.1223  0.1067 0.1101  -0.0035 -0.0361 0.0001  114 TYR A CA  
1004 C  CA  B TYR A  115 ? 0.1146  0.1234 0.1208  -0.0010 -0.0261 0.0111  114 TYR A CA  
1005 C  C   A TYR A  115 ? 0.0795  0.1337 0.0996  -0.0179 -0.0065 0.0012  114 TYR A C   
1006 C  C   B TYR A  115 ? 0.0919  0.1137 0.1065  -0.0248 0.0000  0.0018  114 TYR A C   
1007 O  O   A TYR A  115 ? 0.0979  0.1234 0.1215  -0.0126 -0.0200 -0.0132 114 TYR A O   
1008 O  O   B TYR A  115 ? 0.1225  0.1156 0.1323  -0.0024 -0.0149 -0.0163 114 TYR A O   
1009 C  CB  A TYR A  115 ? 0.0953  0.1556 0.0982  -0.0396 0.0115  -0.0296 114 TYR A CB  
1010 C  CB  B TYR A  115 ? 0.1263  0.1063 0.1448  0.0061  -0.0658 0.0154  114 TYR A CB  
1011 C  CG  A TYR A  115 ? 0.1084  0.0874 0.1005  -0.0052 -0.0096 0.0232  114 TYR A CG  
1012 C  CG  B TYR A  115 ? 0.1076  0.1538 0.1386  -0.0306 -0.0044 0.0063  114 TYR A CG  
1013 C  CD1 A TYR A  115 ? 0.1459  0.1067 0.1084  -0.0059 -0.0380 0.0206  114 TYR A CD1 
1014 C  CD1 B TYR A  115 ? 0.1076  0.2389 0.1707  -0.0179 -0.0280 0.0378  114 TYR A CD1 
1015 C  CD2 A TYR A  115 ? 0.0856  0.1316 0.0937  -0.0025 -0.0020 -0.0029 114 TYR A CD2 
1016 C  CD2 B TYR A  115 ? 0.1887  0.1897 0.1170  0.0116  0.0048  0.0330  114 TYR A CD2 
1017 C  CE1 A TYR A  115 ? 0.1664  0.1380 0.1044  -0.0084 -0.0424 0.0380  114 TYR A CE1 
1018 C  CE1 B TYR A  115 ? 0.2160  0.2278 0.1671  -0.1088 0.0108  0.0161  114 TYR A CE1 
1019 C  CE2 A TYR A  115 ? 0.1398  0.1596 0.0856  -0.0359 -0.0099 0.0178  114 TYR A CE2 
1020 C  CE2 B TYR A  115 ? 0.2449  0.3352 0.1146  -0.0538 0.0087  0.0482  114 TYR A CE2 
1021 C  CZ  A TYR A  115 ? 0.2070  0.1725 0.0858  -0.0144 -0.0189 0.0183  114 TYR A CZ  
1022 C  CZ  B TYR A  115 ? 0.2134  0.2860 0.1181  -0.0804 -0.0208 0.0144  114 TYR A CZ  
1023 O  OH  A TYR A  115 ? 0.2133  0.2278 0.0942  -0.0252 -0.0277 0.0006  114 TYR A OH  
1024 O  OH  B TYR A  115 ? 0.3987  0.3930 0.1141  -0.0412 -0.0117 0.0200  114 TYR A OH  
1025 N  N   A SER A  116 ? 0.0908  0.1102 0.1071  -0.0025 -0.0013 -0.0018 115 SER A N   
1026 N  N   B SER A  116 ? 0.0970  0.1032 0.1147  -0.0163 -0.0001 0.0189  115 SER A N   
1027 C  CA  A SER A  116 ? 0.0882  0.1366 0.1234  -0.0149 -0.0256 0.0130  115 SER A CA  
1028 C  CA  B SER A  116 ? 0.0864  0.0888 0.1243  -0.0189 -0.0120 0.0114  115 SER A CA  
1029 C  C   A SER A  116 ? 0.1040  0.1048 0.1169  -0.0251 -0.0292 0.0172  115 SER A C   
1030 C  C   B SER A  116 ? 0.0828  0.1244 0.1049  -0.0165 -0.0237 0.0081  115 SER A C   
1031 O  O   A SER A  116 ? 0.1032  0.1093 0.1005  -0.0099 -0.0081 0.0270  115 SER A O   
1032 O  O   B SER A  116 ? 0.1163  0.1257 0.1391  -0.0126 -0.0469 -0.0283 115 SER A O   
1033 C  CB  A SER A  116 ? 0.1391  0.0900 0.1768  0.0010  0.0125  0.0406  115 SER A CB  
1034 C  CB  B SER A  116 ? 0.0593  0.1179 0.0989  -0.0283 -0.0054 -0.0009 115 SER A CB  
1035 O  OG  A SER A  116 ? 0.1102  0.1488 0.1764  0.0200  0.0107  0.0190  115 SER A OG  
1036 O  OG  B SER A  116 ? 0.0946  0.1102 0.1164  -0.0062 0.0052  0.0095  115 SER A OG  
1037 N  N   . ALA A  117 ? 0.0741  0.1090 0.1287  -0.0079 -0.0122 0.0001  116 ALA A N   
1038 C  CA  . ALA A  117 ? 0.0680  0.1093 0.1041  -0.0081 -0.0118 -0.0044 116 ALA A CA  
1039 C  C   . ALA A  117 ? 0.0855  0.0917 0.0847  0.0074  -0.0153 -0.0127 116 ALA A C   
1040 O  O   . ALA A  117 ? 0.0849  0.1090 0.0862  -0.0078 -0.0124 -0.0039 116 ALA A O   
1041 C  CB  . ALA A  117 ? 0.0888  0.1088 0.1005  0.0066  -0.0230 0.0013  116 ALA A CB  
1042 N  N   . GLU A  118 ? 0.0835  0.0908 0.0944  -0.0077 -0.0029 0.0062  117 GLU A N   
1043 C  CA  . GLU A  118 ? 0.0891  0.0732 0.0889  -0.0074 -0.0184 0.0042  117 GLU A CA  
1044 C  C   . GLU A  118 ? 0.0883  0.0881 0.0687  0.0009  -0.0220 -0.0039 117 GLU A C   
1045 O  O   . GLU A  118 ? 0.1215  0.1044 0.0732  -0.0126 -0.0178 -0.0042 117 GLU A O   
1046 C  CB  . GLU A  118 ? 0.0855  0.0942 0.1129  0.0055  -0.0240 0.0006  117 GLU A CB  
1047 C  CG  . GLU A  118 ? 0.0944  0.1023 0.1058  0.0087  -0.0211 0.0036  117 GLU A CG  
1048 C  CD  . GLU A  118 ? 0.0962  0.0908 0.0937  -0.0016 -0.0146 0.0066  117 GLU A CD  
1049 O  OE1 . GLU A  118 ? 0.0952  0.1172 0.1116  0.0136  -0.0038 0.0299  117 GLU A OE1 
1050 O  OE2 . GLU A  118 ? 0.1146  0.0962 0.1171  0.0068  -0.0223 -0.0010 117 GLU A OE2 
1051 N  N   . LEU A  119 ? 0.0770  0.0820 0.0879  -0.0067 -0.0168 0.0031  118 LEU A N   
1052 C  CA  . LEU A  119 ? 0.0873  0.0829 0.0838  -0.0072 -0.0132 0.0043  118 LEU A CA  
1053 C  C   . LEU A  119 ? 0.0982  0.0900 0.0636  -0.0111 -0.0261 0.0024  118 LEU A C   
1054 O  O   . LEU A  119 ? 0.0944  0.0970 0.0697  -0.0033 -0.0132 0.0081  118 LEU A O   
1055 C  CB  . LEU A  119 ? 0.1111  0.0892 0.0882  -0.0040 0.0036  -0.0036 118 LEU A CB  
1056 C  CG  . LEU A  119 ? 0.1020  0.0880 0.0962  -0.0080 -0.0222 0.0039  118 LEU A CG  
1057 C  CD1 . LEU A  119 ? 0.1241  0.1040 0.0926  -0.0072 -0.0103 0.0166  118 LEU A CD1 
1058 C  CD2 . LEU A  119 ? 0.1481  0.0894 0.1330  0.0013  -0.0215 -0.0064 118 LEU A CD2 
1059 N  N   . HIS A  120 ? 0.0976  0.0794 0.0743  -0.0051 -0.0066 0.0027  119 HIS A N   
1060 C  CA  . HIS A  120 ? 0.0734  0.0876 0.0804  0.0006  -0.0089 0.0039  119 HIS A CA  
1061 C  C   . HIS A  120 ? 0.0900  0.0849 0.0653  0.0000  -0.0166 0.0173  119 HIS A C   
1062 O  O   . HIS A  120 ? 0.1066  0.1005 0.0786  -0.0061 -0.0231 0.0188  119 HIS A O   
1063 C  CB  . HIS A  120 ? 0.1120  0.0905 0.0688  0.0070  -0.0002 0.0006  119 HIS A CB  
1064 C  CG  . HIS A  120 ? 0.0864  0.0817 0.0697  -0.0002 -0.0215 0.0052  119 HIS A CG  
1065 N  ND1 . HIS A  120 ? 0.0976  0.0873 0.0917  0.0003  -0.0194 0.0006  119 HIS A ND1 
1066 C  CD2 . HIS A  120 ? 0.0864  0.0988 0.0867  0.0068  -0.0160 0.0166  119 HIS A CD2 
1067 C  CE1 . HIS A  120 ? 0.1059  0.1005 0.0716  0.0020  -0.0162 0.0097  119 HIS A CE1 
1068 N  NE2 . HIS A  120 ? 0.0943  0.0829 0.0879  -0.0006 -0.0129 0.0068  119 HIS A NE2 
1069 N  N   . VAL A  121 ? 0.0819  0.0829 0.0795  -0.0074 -0.0126 -0.0006 120 VAL A N   
1070 C  CA  . VAL A  121 ? 0.0915  0.0917 0.0813  -0.0104 -0.0230 0.0098  120 VAL A CA  
1071 C  C   . VAL A  121 ? 0.0932  0.0795 0.0743  -0.0061 -0.0171 0.0166  120 VAL A C   
1072 O  O   . VAL A  121 ? 0.0951  0.0950 0.0774  -0.0004 -0.0115 0.0186  120 VAL A O   
1073 C  CB  . VAL A  121 ? 0.0876  0.0910 0.0820  -0.0049 -0.0060 -0.0044 120 VAL A CB  
1074 C  CG1 . VAL A  121 ? 0.1172  0.1027 0.0908  -0.0204 -0.0107 0.0176  120 VAL A CG1 
1075 C  CG2 . VAL A  121 ? 0.0969  0.1316 0.1032  -0.0080 -0.0055 -0.0062 120 VAL A CG2 
1076 N  N   . ALA A  122 ? 0.0900  0.1164 0.0847  -0.0038 0.0078  0.0164  121 ALA A N   
1077 C  CA  . ALA A  122 ? 0.0899  0.0917 0.1047  -0.0004 0.0057  0.0125  121 ALA A CA  
1078 C  C   . ALA A  122 ? 0.1186  0.1040 0.0680  -0.0077 0.0006  0.0273  121 ALA A C   
1079 O  O   . ALA A  122 ? 0.1040  0.1067 0.1102  -0.0052 -0.0089 0.0406  121 ALA A O   
1080 C  CB  . ALA A  122 ? 0.1190  0.1199 0.0958  0.0035  0.0006  0.0022  121 ALA A CB  
1081 N  N   . HIS A  123 ? 0.0837  0.1198 0.1021  0.0017  -0.0008 0.0240  122 HIS A N   
1082 C  CA  . HIS A  123 ? 0.0820  0.1150 0.1155  0.0003  0.0068  0.0184  122 HIS A CA  
1083 C  C   . HIS A  123 ? 0.0845  0.1137 0.1084  -0.0081 0.0001  0.0266  122 HIS A C   
1084 O  O   . HIS A  123 ? 0.0994  0.1111 0.1531  -0.0006 0.0003  0.0462  122 HIS A O   
1085 C  CB  . HIS A  123 ? 0.0989  0.1214 0.1037  -0.0038 -0.0113 0.0124  122 HIS A CB  
1086 C  CG  . HIS A  123 ? 0.0890  0.1110 0.0970  -0.0082 -0.0097 0.0164  122 HIS A CG  
1087 N  ND1 . HIS A  123 ? 0.0926  0.0982 0.0953  -0.0047 -0.0047 0.0209  122 HIS A ND1 
1088 C  CD2 . HIS A  123 ? 0.1048  0.1188 0.0917  0.0072  -0.0092 -0.0004 122 HIS A CD2 
1089 C  CE1 . HIS A  123 ? 0.1032  0.1040 0.0953  0.0046  -0.0221 -0.0061 122 HIS A CE1 
1090 N  NE2 . HIS A  123 ? 0.1091  0.0935 0.0989  0.0069  -0.0053 0.0013  122 HIS A NE2 
1091 N  N   . TRP A  124 ? 0.0829  0.1351 0.1032  -0.0223 0.0049  0.0256  123 TRP A N   
1092 C  CA  . TRP A  124 ? 0.0750  0.1289 0.1287  -0.0093 0.0139  0.0178  123 TRP A CA  
1093 C  C   . TRP A  124 ? 0.0804  0.1187 0.1243  -0.0102 0.0273  0.0141  123 TRP A C   
1094 O  O   . TRP A  124 ? 0.0964  0.1214 0.1659  -0.0100 0.0097  0.0095  123 TRP A O   
1095 C  CB  . TRP A  124 ? 0.1223  0.1463 0.1062  -0.0082 0.0286  0.0217  123 TRP A CB  
1096 C  CG  . TRP A  124 ? 0.0923  0.1316 0.1181  -0.0122 0.0019  0.0152  123 TRP A CG  
1097 C  CD1 . TRP A  124 ? 0.1031  0.1465 0.1172  -0.0065 0.0140  0.0198  123 TRP A CD1 
1098 C  CD2 . TRP A  124 ? 0.0978  0.1362 0.1289  -0.0006 0.0126  0.0233  123 TRP A CD2 
1099 N  NE1 . TRP A  124 ? 0.1118  0.1653 0.1344  -0.0138 0.0128  0.0294  123 TRP A NE1 
1100 C  CE2 . TRP A  124 ? 0.1261  0.1359 0.1344  -0.0220 0.0039  0.0358  123 TRP A CE2 
1101 C  CE3 . TRP A  124 ? 0.0953  0.1847 0.1377  -0.0166 0.0125  0.0296  123 TRP A CE3 
1102 C  CZ2 . TRP A  124 ? 0.1477  0.1588 0.1483  -0.0487 -0.0135 0.0238  123 TRP A CZ2 
1103 C  CZ3 . TRP A  124 ? 0.1216  0.2020 0.1395  -0.0300 0.0217  0.0240  123 TRP A CZ3 
1104 C  CH2 . TRP A  124 ? 0.1373  0.1969 0.1319  -0.0583 -0.0115 0.0305  123 TRP A CH2 
1105 N  N   . ASN A  125 ? 0.0828  0.1420 0.1247  -0.0027 0.0074  0.0107  124 ASN A N   
1106 C  CA  . ASN A  125 ? 0.0908  0.1243 0.1483  -0.0205 0.0020  0.0200  124 ASN A CA  
1107 C  C   . ASN A  125 ? 0.0782  0.1243 0.1560  -0.0042 0.0042  0.0095  124 ASN A C   
1108 O  O   . ASN A  125 ? 0.0819  0.1531 0.1817  -0.0039 0.0171  0.0226  124 ASN A O   
1109 C  CB  . ASN A  125 ? 0.1075  0.1359 0.1585  -0.0081 -0.0179 0.0209  124 ASN A CB  
1110 C  CG  . ASN A  125 ? 0.1128  0.1768 0.1520  0.0008  -0.0024 0.0054  124 ASN A CG  
1111 O  OD1 . ASN A  125 ? 0.1301  0.1811 0.1574  -0.0046 -0.0081 0.0037  124 ASN A OD1 
1112 N  ND2 . ASN A  125 ? 0.1420  0.2257 0.1750  -0.0127 -0.0345 0.0476  124 ASN A ND2 
1113 N  N   . SER A  126 ? 0.1274  0.1066 0.2084  -0.0164 0.0340  0.0086  125 SER A N   
1114 C  CA  . SER A  126 ? 0.1064  0.1229 0.2508  -0.0204 0.0233  0.0336  125 SER A CA  
1115 C  C   . SER A  126 ? 0.1402  0.1373 0.2777  -0.0379 0.0366  -0.0133 125 SER A C   
1116 O  O   . SER A  126 ? 0.1596  0.1711 0.3194  -0.0718 0.0523  0.0054  125 SER A O   
1117 C  CB  . SER A  126 ? 0.1581  0.1628 0.2643  0.0195  0.0282  0.0429  125 SER A CB  
1118 O  OG  . SER A  126 ? 0.1747  0.1283 0.3359  -0.0162 0.0672  0.0236  125 SER A OG  
1119 N  N   . ALA A  127 ? 0.1488  0.1840 0.2687  -0.0425 0.0060  -0.0494 126 ALA A N   
1120 C  CA  . ALA A  127 ? 0.1738  0.2156 0.2398  -0.0425 -0.0266 -0.0299 126 ALA A CA  
1121 C  C   . ALA A  127 ? 0.1212  0.2120 0.2733  -0.0477 -0.0452 0.0034  126 ALA A C   
1122 O  O   . ALA A  127 ? 0.1517  0.2816 0.4151  -0.0694 0.0078  0.0171  126 ALA A O   
1123 C  CB  . ALA A  127 ? 0.2091  0.2755 0.2318  -0.0638 -0.0228 -0.0725 126 ALA A CB  
1124 N  N   . LYS A  128 ? 0.1344  0.2095 0.1775  -0.0390 -0.0062 0.0117  127 LYS A N   
1125 C  CA  . LYS A  128 ? 0.1088  0.2222 0.1330  -0.0178 -0.0159 0.0290  127 LYS A CA  
1126 C  C   . LYS A  128 ? 0.1206  0.2152 0.1273  0.0067  0.0139  0.0238  127 LYS A C   
1127 O  O   . LYS A  128 ? 0.1203  0.2795 0.1571  0.0122  0.0111  0.0401  127 LYS A O   
1128 C  CB  . LYS A  128 ? 0.1423  0.2730 0.1553  0.0085  -0.0107 0.0534  127 LYS A CB  
1129 C  CG  . LYS A  128 ? 0.2666  0.2309 0.2684  0.0215  0.0160  0.0254  127 LYS A CG  
1130 C  CD  . LYS A  128 ? 0.2045  0.2490 0.3710  -0.0219 -0.0348 0.0790  127 LYS A CD  
1131 C  CE  . LYS A  128 ? 0.2064  0.3463 0.3093  -0.0011 -0.0439 0.0942  127 LYS A CE  
1132 N  NZ  . LYS A  128 ? 0.2152  0.3646 0.3462  -0.0431 -0.0325 0.1421  127 LYS A NZ  
1133 N  N   . TYR A  129 ? 0.1128  0.1682 0.1207  -0.0153 0.0022  0.0253  128 TYR A N   
1134 C  CA  . TYR A  129 ? 0.1216  0.1797 0.1067  -0.0088 0.0137  0.0212  128 TYR A CA  
1135 C  C   . TYR A  129 ? 0.1254  0.1520 0.1646  -0.0071 0.0127  0.0241  128 TYR A C   
1136 O  O   . TYR A  129 ? 0.1151  0.1641 0.1678  -0.0185 -0.0095 0.0289  128 TYR A O   
1137 C  CB  . TYR A  129 ? 0.1276  0.1632 0.1560  -0.0166 -0.0138 0.0273  128 TYR A CB  
1138 C  CG  . TYR A  129 ? 0.1072  0.1463 0.1509  -0.0066 0.0119  0.0179  128 TYR A CG  
1139 C  CD1 . TYR A  129 ? 0.1181  0.1872 0.1714  0.0082  0.0081  0.0304  128 TYR A CD1 
1140 C  CD2 . TYR A  129 ? 0.1093  0.1703 0.1120  -0.0085 -0.0013 0.0085  128 TYR A CD2 
1141 C  CE1 . TYR A  129 ? 0.1405  0.1811 0.1502  -0.0073 0.0196  0.0289  128 TYR A CE1 
1142 C  CE2 . TYR A  129 ? 0.0987  0.1901 0.1524  0.0001  -0.0082 0.0176  128 TYR A CE2 
1143 C  CZ  . TYR A  129 ? 0.0986  0.1912 0.1427  -0.0050 -0.0011 0.0370  128 TYR A CZ  
1144 O  OH  . TYR A  129 ? 0.1254  0.2005 0.2011  0.0127  0.0046  0.0525  128 TYR A OH  
1145 N  N   . SER A  130 ? 0.1427  0.1948 0.1481  -0.0102 0.0032  0.0532  129 SER A N   
1146 C  CA  . SER A  130 ? 0.1208  0.1987 0.1764  -0.0254 -0.0074 0.0673  129 SER A CA  
1147 C  C   . SER A  130 ? 0.0996  0.2064 0.1962  0.0023  -0.0012 0.0542  129 SER A C   
1148 O  O   . SER A  130 ? 0.1441  0.2133 0.2248  -0.0385 -0.0348 0.0899  129 SER A O   
1149 C  CB  . SER A  130 ? 0.1312  0.2587 0.1553  -0.0619 -0.0286 0.0717  129 SER A CB  
1150 O  OG  . SER A  130 ? 0.1301  0.2443 0.1887  -0.0323 -0.0325 0.0500  129 SER A OG  
1151 N  N   . SER A  131 ? 0.1265  0.2002 0.1465  -0.0304 0.0072  0.0359  130 SER A N   
1152 C  CA  . SER A  131 ? 0.1189  0.1969 0.1416  -0.0358 -0.0091 0.0118  130 SER A CA  
1153 C  C   . SER A  131 ? 0.1412  0.1596 0.1492  -0.0288 -0.0218 0.0285  130 SER A C   
1154 O  O   . SER A  131 ? 0.1463  0.1689 0.1477  -0.0095 0.0040  0.0201  130 SER A O   
1155 C  CB  . SER A  131 ? 0.2187  0.2016 0.1298  -0.0040 0.0089  0.0138  130 SER A CB  
1156 O  OG  . SER A  131 ? 0.2156  0.2011 0.1668  -0.0299 -0.0066 0.0422  130 SER A OG  
1157 N  N   . LEU A  132 ? 0.1391  0.1808 0.1312  -0.0149 0.0035  0.0197  131 LEU A N   
1158 C  CA  . LEU A  132 ? 0.1257  0.1854 0.1562  -0.0376 -0.0095 0.0212  131 LEU A CA  
1159 C  C   . LEU A  132 ? 0.1585  0.1542 0.1535  -0.0305 -0.0124 0.0329  131 LEU A C   
1160 O  O   . LEU A  132 ? 0.1483  0.1750 0.1815  -0.0394 -0.0188 0.0421  131 LEU A O   
1161 C  CB  . LEU A  132 ? 0.1373  0.2314 0.1136  -0.0378 0.0035  0.0187  131 LEU A CB  
1162 C  CG  . LEU A  132 ? 0.1502  0.2206 0.1204  -0.0396 0.0027  0.0110  131 LEU A CG  
1163 C  CD1 . LEU A  132 ? 0.1876  0.2888 0.1161  -0.0782 -0.0069 0.0205  131 LEU A CD1 
1164 C  CD2 . LEU A  132 ? 0.1423  0.2773 0.1477  -0.0087 0.0080  -0.0212 131 LEU A CD2 
1165 N  N   . ALA A  133 ? 0.1930  0.2080 0.1488  -0.0044 -0.0022 0.0040  132 ALA A N   
1166 C  CA  . ALA A  133 ? 0.2181  0.2411 0.1488  -0.0024 -0.0357 -0.0201 132 ALA A CA  
1167 C  C   . ALA A  133 ? 0.1804  0.2084 0.1402  -0.0106 0.0136  0.0068  132 ALA A C   
1168 O  O   . ALA A  133 ? 0.2161  0.1897 0.2398  -0.0104 0.0096  0.0065  132 ALA A O   
1169 C  CB  . ALA A  133 ? 0.3693  0.2576 0.1181  0.0366  -0.0041 -0.0242 132 ALA A CB  
1170 N  N   . GLU A  134 ? 0.1463  0.1987 0.1606  -0.0055 0.0209  0.0053  133 GLU A N   
1171 C  CA  . GLU A  134 ? 0.1362  0.1973 0.1689  -0.0079 0.0294  0.0320  133 GLU A CA  
1172 C  C   . GLU A  134 ? 0.1351  0.1764 0.1578  0.0001  0.0179  0.0234  133 GLU A C   
1173 O  O   . GLU A  134 ? 0.1887  0.1962 0.1808  0.0337  0.0370  0.0302  133 GLU A O   
1174 C  CB  . GLU A  134 ? 0.1517  0.2192 0.1560  -0.0204 0.0201  0.0106  133 GLU A CB  
1175 C  CG  . GLU A  134 ? 0.1657  0.2073 0.2016  0.0098  0.0210  0.0501  133 GLU A CG  
1176 C  CD  . GLU A  134 ? 0.1463  0.2307 0.1738  0.0201  0.0355  0.0383  133 GLU A CD  
1177 O  OE1 . GLU A  134 ? 0.1477  0.2278 0.1678  -0.0176 0.0206  0.0068  133 GLU A OE1 
1178 O  OE2 . GLU A  134 ? 0.1377  0.2816 0.1991  -0.0049 0.0280  0.0243  133 GLU A OE2 
1179 N  N   . ALA A  135 ? 0.1434  0.1797 0.1549  -0.0273 0.0188  0.0102  134 ALA A N   
1180 C  CA  . ALA A  135 ? 0.1301  0.1714 0.1216  -0.0242 0.0244  0.0011  134 ALA A CA  
1181 C  C   . ALA A  135 ? 0.1005  0.1624 0.1316  0.0006  0.0034  0.0117  134 ALA A C   
1182 O  O   . ALA A  135 ? 0.1337  0.1567 0.1398  -0.0118 0.0193  0.0157  134 ALA A O   
1183 C  CB  . ALA A  135 ? 0.1272  0.1553 0.1319  -0.0188 0.0122  0.0140  134 ALA A CB  
1184 N  N   . ALA A  136 ? 0.1448  0.1542 0.1628  -0.0427 -0.0049 0.0266  135 ALA A N   
1185 C  CA  . ALA A  136 ? 0.1495  0.1747 0.1703  -0.0425 -0.0149 0.0267  135 ALA A CA  
1186 C  C   . ALA A  136 ? 0.1560  0.1520 0.1527  -0.0343 0.0254  0.0177  135 ALA A C   
1187 O  O   . ALA A  136 ? 0.1617  0.1657 0.1483  -0.0402 0.0228  0.0102  135 ALA A O   
1188 C  CB  . ALA A  136 ? 0.1865  0.2773 0.2178  -0.0862 -0.0571 0.0648  135 ALA A CB  
1189 N  N   . SER A  137 ? 0.1567  0.1754 0.1326  -0.0100 0.0209  -0.0122 136 SER A N   
1190 C  CA  . SER A  137 ? 0.1786  0.1664 0.1675  0.0077  0.0231  -0.0065 136 SER A CA  
1191 C  C   . SER A  137 ? 0.1768  0.1610 0.1445  -0.0005 0.0289  -0.0135 136 SER A C   
1192 O  O   . SER A  137 ? 0.2495  0.1678 0.2289  0.0335  0.0127  -0.0219 136 SER A O   
1193 C  CB  . SER A  137 ? 0.2640  0.2842 0.1861  0.0017  0.0407  -0.0517 136 SER A CB  
1194 O  OG  . SER A  137 ? 0.3477  0.3707 0.2091  -0.0122 0.1241  -0.0414 136 SER A OG  
1195 N  N   A LYS A  138 ? 0.1517  0.1703 0.1270  -0.0074 0.0060  0.0106  137 LYS A N   
1196 N  N   B LYS A  138 ? 0.1216  0.1804 0.1517  0.0073  0.0462  -0.0167 137 LYS A N   
1197 C  CA  A LYS A  138 ? 0.1151  0.1592 0.1380  0.0040  0.0215  -0.0167 137 LYS A CA  
1198 C  CA  B LYS A  138 ? 0.1298  0.1668 0.1502  0.0023  0.0457  -0.0172 137 LYS A CA  
1199 C  C   A LYS A  138 ? 0.1150  0.1386 0.1351  0.0219  0.0245  0.0085  137 LYS A C   
1200 C  C   B LYS A  138 ? 0.1163  0.1289 0.1312  0.0206  0.0290  0.0051  137 LYS A C   
1201 O  O   A LYS A  138 ? 0.0979  0.1459 0.1578  -0.0051 0.0190  -0.0027 137 LYS A O   
1202 O  O   B LYS A  138 ? 0.1186  0.1373 0.1448  0.0116  0.0322  0.0050  137 LYS A O   
1203 C  CB  A LYS A  138 ? 0.1312  0.1581 0.1488  0.0060  0.0298  0.0251  137 LYS A CB  
1204 C  CB  B LYS A  138 ? 0.1377  0.1747 0.1736  -0.0054 0.0435  -0.0020 137 LYS A CB  
1205 C  CG  A LYS A  138 ? 0.1398  0.1764 0.1865  -0.0254 0.0739  0.0153  137 LYS A CG  
1206 C  CG  B LYS A  138 ? 0.1100  0.2561 0.1527  0.0192  0.0254  0.0359  137 LYS A CG  
1207 C  CD  A LYS A  138 ? 0.1492  0.2813 0.1567  0.0372  0.0567  0.0461  137 LYS A CD  
1208 C  CD  B LYS A  138 ? 0.1678  0.2953 0.2016  0.0455  0.0922  0.0133  137 LYS A CD  
1209 C  CE  A LYS A  138 ? 0.1470  0.2636 0.1513  0.0410  0.0610  0.0297  137 LYS A CE  
1210 C  CE  B LYS A  138 ? 0.1951  0.3808 0.1815  0.0809  0.1115  0.0458  137 LYS A CE  
1211 N  NZ  A LYS A  138 ? 0.1738  0.2231 0.1294  0.0373  0.0626  0.0047  137 LYS A NZ  
1212 N  NZ  B LYS A  138 ? 0.2892  0.2888 0.3032  0.1130  0.1035  0.0211  137 LYS A NZ  
1213 N  N   . ALA A  139 ? 0.1538  0.1405 0.1711  0.0199  0.0122  0.0362  138 ALA A N   
1214 C  CA  . ALA A  139 ? 0.1750  0.1459 0.1427  0.0131  0.0174  0.0337  138 ALA A CA  
1215 C  C   . ALA A  139 ? 0.1280  0.1409 0.1459  0.0177  0.0183  0.0367  138 ALA A C   
1216 O  O   . ALA A  139 ? 0.1386  0.1610 0.1499  0.0165  0.0239  0.0345  138 ALA A O   
1217 C  CB  . ALA A  139 ? 0.1926  0.1858 0.1772  0.0604  0.0139  0.0453  138 ALA A CB  
1218 N  N   . ASP A  140 ? 0.1199  0.1427 0.1531  0.0062  0.0000  0.0325  139 ASP A N   
1219 C  CA  . ASP A  140 ? 0.1217  0.1272 0.1434  0.0067  -0.0077 0.0293  139 ASP A CA  
1220 C  C   . ASP A  140 ? 0.0885  0.1256 0.1599  -0.0082 0.0062  0.0308  139 ASP A C   
1221 O  O   . ASP A  140 ? 0.1287  0.1459 0.1368  0.0015  -0.0089 0.0212  139 ASP A O   
1222 C  CB  . ASP A  140 ? 0.1199  0.2117 0.1470  -0.0044 -0.0124 0.0261  139 ASP A CB  
1223 C  CG  . ASP A  140 ? 0.1215  0.2142 0.1502  -0.0080 -0.0160 0.0348  139 ASP A CG  
1224 O  OD1 . ASP A  140 ? 0.1172  0.2181 0.1664  -0.0212 0.0055  0.0411  139 ASP A OD1 
1225 O  OD2 . ASP A  140 ? 0.1395  0.3244 0.2357  -0.0637 -0.0200 -0.0058 139 ASP A OD2 
1226 N  N   . GLY A  141 ? 0.0894  0.1624 0.1181  -0.0009 0.0054  0.0255  140 GLY A N   
1227 C  CA  . GLY A  141 ? 0.0908  0.1263 0.1137  0.0124  0.0006  0.0197  140 GLY A CA  
1228 C  C   . GLY A  141 ? 0.0959  0.1163 0.1065  -0.0031 0.0012  0.0128  140 GLY A C   
1229 O  O   . GLY A  141 ? 0.1073  0.1180 0.1276  -0.0095 0.0061  0.0168  140 GLY A O   
1230 N  N   . LEU A  142 ? 0.0829  0.1287 0.1116  -0.0022 0.0189  -0.0043 141 LEU A N   
1231 C  CA  . LEU A  142 ? 0.0689  0.1274 0.1254  -0.0080 0.0064  0.0021  141 LEU A CA  
1232 C  C   . LEU A  142 ? 0.0831  0.1030 0.1109  -0.0040 0.0053  0.0185  141 LEU A C   
1233 O  O   . LEU A  142 ? 0.0961  0.1084 0.1040  0.0044  0.0069  0.0127  141 LEU A O   
1234 C  CB  . LEU A  142 ? 0.0989  0.1240 0.1145  -0.0096 0.0000  0.0047  141 LEU A CB  
1235 C  CG  . LEU A  142 ? 0.1481  0.1258 0.0944  -0.0309 -0.0012 0.0100  141 LEU A CG  
1236 C  CD1 . LEU A  142 ? 0.1481  0.1495 0.1244  -0.0317 -0.0172 0.0140  141 LEU A CD1 
1237 C  CD2 . LEU A  142 ? 0.1908  0.1333 0.1178  -0.0287 0.0086  0.0296  141 LEU A CD2 
1238 N  N   . ALA A  143 ? 0.0855  0.1150 0.1150  -0.0006 0.0125  0.0164  142 ALA A N   
1239 C  CA  . ALA A  143 ? 0.0795  0.1333 0.1082  0.0164  0.0184  0.0013  142 ALA A CA  
1240 C  C   . ALA A  143 ? 0.1014  0.1014 0.0907  0.0119  0.0067  0.0242  142 ALA A C   
1241 O  O   . ALA A  143 ? 0.0968  0.1203 0.1023  0.0005  0.0008  0.0427  142 ALA A O   
1242 C  CB  . ALA A  143 ? 0.1188  0.1506 0.0998  -0.0033 0.0013  0.0068  142 ALA A CB  
1243 N  N   . VAL A  144 ? 0.0777  0.1040 0.0925  -0.0051 -0.0006 0.0150  143 VAL A N   
1244 C  CA  . VAL A  144 ? 0.0885  0.1023 0.0806  -0.0048 0.0023  0.0058  143 VAL A CA  
1245 C  C   . VAL A  144 ? 0.0804  0.0970 0.0700  -0.0110 -0.0040 0.0222  143 VAL A C   
1246 O  O   . VAL A  144 ? 0.0905  0.1137 0.0732  -0.0055 -0.0067 0.0311  143 VAL A O   
1247 C  CB  . VAL A  144 ? 0.1037  0.0943 0.0917  0.0040  -0.0173 0.0111  143 VAL A CB  
1248 C  CG1 . VAL A  144 ? 0.1040  0.1280 0.1066  0.0051  -0.0381 0.0094  143 VAL A CG1 
1249 C  CG2 . VAL A  144 ? 0.1506  0.1212 0.0822  0.0165  0.0165  0.0096  143 VAL A CG2 
1250 N  N   . ILE A  145 ? 0.0697  0.1093 0.0785  -0.0052 -0.0039 0.0124  144 ILE A N   
1251 C  CA  . ILE A  145 ? 0.0715  0.1021 0.0862  0.0000  0.0000  0.0115  144 ILE A CA  
1252 C  C   . ILE A  145 ? 0.0759  0.1045 0.0811  0.0083  -0.0129 0.0167  144 ILE A C   
1253 O  O   . ILE A  145 ? 0.0970  0.1190 0.0795  -0.0058 -0.0142 0.0240  144 ILE A O   
1254 C  CB  . ILE A  145 ? 0.0874  0.1040 0.0910  0.0044  -0.0051 0.0100  144 ILE A CB  
1255 C  CG1 . ILE A  145 ? 0.1190  0.1016 0.1463  -0.0215 -0.0173 0.0004  144 ILE A CG1 
1256 C  CG2 . ILE A  145 ? 0.1120  0.1341 0.0876  -0.0025 0.0151  0.0022  144 ILE A CG2 
1257 C  CD1 . ILE A  145 ? 0.1330  0.1109 0.1718  -0.0023 0.0031  -0.0067 144 ILE A CD1 
1258 N  N   . GLY A  146 ? 0.0971  0.1003 0.0831  -0.0049 -0.0053 0.0203  145 GLY A N   
1259 C  CA  . GLY A  146 ? 0.0770  0.0935 0.0847  -0.0046 -0.0009 -0.0021 145 GLY A CA  
1260 C  C   . GLY A  146 ? 0.0861  0.1023 0.0847  -0.0119 -0.0186 0.0077  145 GLY A C   
1261 O  O   . GLY A  146 ? 0.0917  0.1405 0.0697  0.0004  -0.0081 0.0027  145 GLY A O   
1262 N  N   . VAL A  147 ? 0.0687  0.1056 0.0826  0.0055  -0.0042 0.0015  146 VAL A N   
1263 C  CA  . VAL A  147 ? 0.0881  0.1099 0.0891  -0.0006 -0.0046 -0.0126 146 VAL A CA  
1264 C  C   . VAL A  147 ? 0.0730  0.0905 0.0820  0.0017  -0.0058 0.0001  146 VAL A C   
1265 O  O   . VAL A  147 ? 0.0996  0.1208 0.0800  -0.0020 -0.0138 -0.0013 146 VAL A O   
1266 C  CB  . VAL A  147 ? 0.0995  0.0858 0.0944  0.0017  -0.0059 0.0000  146 VAL A CB  
1267 C  CG1 . VAL A  147 ? 0.1125  0.1289 0.1294  -0.0021 0.0105  -0.0269 146 VAL A CG1 
1268 C  CG2 . VAL A  147 ? 0.1023  0.1067 0.1239  -0.0248 -0.0212 -0.0107 146 VAL A CG2 
1269 N  N   A LEU A  148 ? 0.0856  0.0970 0.0840  -0.0041 -0.0094 0.0055  147 LEU A N   
1270 N  N   B LEU A  148 ? 0.0847  0.0973 0.0864  -0.0043 -0.0037 0.0032  147 LEU A N   
1271 C  CA  A LEU A  148 ? 0.0882  0.1014 0.0873  -0.0057 -0.0013 0.0103  147 LEU A CA  
1272 C  CA  B LEU A  148 ? 0.0840  0.1084 0.0979  -0.0071 -0.0006 0.0150  147 LEU A CA  
1273 C  C   A LEU A  148 ? 0.0846  0.1040 0.0804  -0.0083 -0.0043 0.0006  147 LEU A C   
1274 C  C   B LEU A  148 ? 0.0831  0.1041 0.0812  -0.0107 -0.0038 0.0019  147 LEU A C   
1275 O  O   A LEU A  148 ? 0.1055  0.1207 0.0856  0.0092  -0.0163 -0.0106 147 LEU A O   
1276 O  O   B LEU A  148 ? 0.1067  0.1213 0.0865  0.0051  -0.0122 -0.0098 147 LEU A O   
1277 C  CB  A LEU A  148 ? 0.1212  0.1276 0.0686  0.0286  -0.0148 0.0197  147 LEU A CB  
1278 C  CB  B LEU A  148 ? 0.0793  0.1235 0.1083  -0.0183 -0.0047 0.0314  147 LEU A CB  
1279 C  CG  A LEU A  148 ? 0.1023  0.1250 0.0935  -0.0025 -0.0159 -0.0013 147 LEU A CG  
1280 C  CG  B LEU A  148 ? 0.1409  0.1675 0.1894  0.0164  -0.0027 0.0796  147 LEU A CG  
1281 C  CD1 A LEU A  148 ? 0.1270  0.2196 0.1373  -0.0552 -0.0185 0.0613  147 LEU A CD1 
1282 C  CD1 B LEU A  148 ? 0.1585  0.2228 0.3115  0.0218  -0.0639 -0.0567 147 LEU A CD1 
1283 C  CD2 A LEU A  148 ? 0.1062  0.0788 0.0882  0.0362  0.0027  0.0024  147 LEU A CD2 
1284 C  CD2 B LEU A  148 ? 0.1560  0.2353 0.2210  0.0680  0.0390  0.1000  147 LEU A CD2 
1285 N  N   . MET A  149 ? 0.0846  0.1049 0.1040  -0.0020 -0.0163 0.0012  148 MET A N   
1286 C  CA  . MET A  149 ? 0.0768  0.1172 0.0942  -0.0039 -0.0111 0.0089  148 MET A CA  
1287 C  C   . MET A  149 ? 0.0943  0.1038 0.0967  -0.0033 -0.0089 0.0059  148 MET A C   
1288 O  O   . MET A  149 ? 0.0986  0.1181 0.1073  -0.0119 -0.0097 0.0022  148 MET A O   
1289 C  CB  . MET A  149 ? 0.1023  0.0996 0.0926  -0.0044 -0.0046 0.0122  148 MET A CB  
1290 C  CG  . MET A  149 ? 0.1027  0.1102 0.0885  -0.0079 -0.0071 0.0073  148 MET A CG  
1291 S  SD  . MET A  149 ? 0.1031  0.1179 0.0980  0.0018  -0.0099 0.0002  148 MET A SD  
1292 C  CE  . MET A  149 ? 0.1044  0.1685 0.1696  0.0197  0.0013  0.0386  148 MET A CE  
1293 N  N   . LYS A  150 ? 0.0923  0.1251 0.1040  0.0043  -0.0027 0.0075  149 LYS A N   
1294 C  CA  . LYS A  150 ? 0.0900  0.1513 0.1056  -0.0055 0.0058  0.0113  149 LYS A CA  
1295 C  C   . LYS A  150 ? 0.0865  0.1333 0.1032  -0.0065 0.0072  -0.0005 149 LYS A C   
1296 O  O   . LYS A  150 ? 0.1007  0.1409 0.1023  0.0000  -0.0062 0.0085  149 LYS A O   
1297 C  CB  . LYS A  150 ? 0.1169  0.1761 0.0899  -0.0060 -0.0098 0.0076  149 LYS A CB  
1298 C  CG  . LYS A  150 ? 0.1549  0.2005 0.1138  -0.0047 0.0089  0.0337  149 LYS A CG  
1299 C  CD  . LYS A  150 ? 0.2407  0.2740 0.1189  0.0131  0.0251  0.0326  149 LYS A CD  
1300 C  CE  . LYS A  150 ? 0.4356  0.2723 0.1398  -0.0241 0.0970  0.0358  149 LYS A CE  
1301 N  NZ  . LYS A  150 ? 0.4846  0.3582 0.2612  0.0219  0.0812  0.0680  149 LYS A NZ  
1302 N  N   . VAL A  151 ? 0.0908  0.1456 0.0971  -0.0200 0.0000  0.0107  150 VAL A N   
1303 C  CA  . VAL A  151 ? 0.0810  0.1610 0.0970  0.0058  -0.0037 -0.0066 150 VAL A CA  
1304 C  C   . VAL A  151 ? 0.0943  0.1635 0.0970  0.0031  0.0051  0.0099  150 VAL A C   
1305 O  O   . VAL A  151 ? 0.1294  0.1844 0.1027  0.0105  0.0125  0.0263  150 VAL A O   
1306 C  CB  . VAL A  151 ? 0.1145  0.1477 0.1225  -0.0220 -0.0288 -0.0053 150 VAL A CB  
1307 C  CG1 . VAL A  151 ? 0.1499  0.1477 0.1779  -0.0208 -0.0082 0.0225  150 VAL A CG1 
1308 C  CG2 . VAL A  151 ? 0.1398  0.1847 0.1560  -0.0149 -0.0482 -0.0244 150 VAL A CG2 
1309 N  N   . GLY A  152 ? 0.0935  0.1599 0.1146  0.0225  0.0001  -0.0029 151 GLY A N   
1310 C  CA  . GLY A  152 ? 0.1380  0.1786 0.1208  0.0440  0.0271  0.0066  151 GLY A CA  
1311 C  C   . GLY A  152 ? 0.1161  0.1768 0.1023  0.0374  0.0136  0.0017  151 GLY A C   
1312 O  O   . GLY A  152 ? 0.1359  0.1897 0.1120  0.0286  -0.0029 -0.0062 151 GLY A O   
1313 N  N   . GLU A  153 ? 0.1452  0.1581 0.1102  0.0267  0.0089  -0.0116 152 GLU A N   
1314 C  CA  . GLU A  153 ? 0.2188  0.1725 0.1067  0.0469  0.0364  -0.0092 152 GLU A CA  
1315 C  C   . GLU A  153 ? 0.1204  0.1459 0.1037  0.0302  -0.0041 -0.0147 152 GLU A C   
1316 O  O   . GLU A  153 ? 0.1283  0.1714 0.1120  0.0205  -0.0121 -0.0035 152 GLU A O   
1317 C  CB  . GLU A  153 ? 0.4310  0.1851 0.1355  0.0639  0.0842  -0.0300 152 GLU A CB  
1318 C  CG  . GLU A  153 ? 0.5216  0.3049 0.1779  0.0954  0.0967  -0.0467 152 GLU A CG  
1319 C  CD  . GLU A  153 ? 0.5720  0.7652 0.6949  0.1860  0.1541  -0.0576 152 GLU A CD  
1320 O  OE1 . GLU A  153 ? 1.1278  0.9010 0.6875  0.1579  0.2034  -0.2371 152 GLU A OE1 
1321 O  OE2 . GLU A  153 ? 0.6071  1.2041 0.5960  0.2384  0.3861  0.1289  152 GLU A OE2 
1322 N  N   . ALA A  154 ? 0.1283  0.1542 0.1147  0.0219  -0.0066 -0.0104 153 ALA A N   
1323 C  CA  . ALA A  154 ? 0.1138  0.1344 0.1032  -0.0033 -0.0078 0.0103  153 ALA A CA  
1324 C  C   . ALA A  154 ? 0.1181  0.1208 0.1115  0.0347  -0.0018 -0.0134 153 ALA A C   
1325 O  O   . ALA A  154 ? 0.1276  0.1517 0.1305  0.0263  -0.0097 -0.0321 153 ALA A O   
1326 C  CB  . ALA A  154 ? 0.1326  0.1743 0.1254  0.0367  -0.0279 -0.0081 153 ALA A CB  
1327 N  N   . ASN A  155 ? 0.0914  0.1456 0.0914  0.0230  -0.0271 -0.0205 154 ASN A N   
1328 C  CA  . ASN A  155 ? 0.1048  0.1199 0.1058  0.0174  -0.0314 -0.0016 154 ASN A CA  
1329 C  C   . ASN A  155 ? 0.0937  0.1298 0.1115  0.0146  -0.0227 -0.0249 154 ASN A C   
1330 O  O   . ASN A  155 ? 0.1128  0.1333 0.1056  0.0088  -0.0089 -0.0104 154 ASN A O   
1331 C  CB  . ASN A  155 ? 0.0944  0.1312 0.1423  0.0113  -0.0467 -0.0067 154 ASN A CB  
1332 C  CG  . ASN A  155 ? 0.1156  0.1081 0.1280  0.0093  -0.0406 0.0054  154 ASN A CG  
1333 O  OD1 . ASN A  155 ? 0.1294  0.1172 0.1822  0.0094  -0.0543 -0.0074 154 ASN A OD1 
1334 N  ND2 . ASN A  155 ? 0.1037  0.1330 0.1267  0.0190  -0.0344 0.0145  154 ASN A ND2 
1335 N  N   . PRO A  156 ? 0.1294  0.1190 0.1190  0.0333  -0.0055 -0.0154 155 PRO A N   
1336 C  CA  . PRO A  156 ? 0.1488  0.1046 0.1635  0.0195  0.0037  -0.0054 155 PRO A CA  
1337 C  C   . PRO A  156 ? 0.1883  0.1185 0.1499  0.0186  -0.0146 -0.0107 155 PRO A C   
1338 O  O   . PRO A  156 ? 0.2037  0.1243 0.1689  0.0212  0.0000  0.0115  155 PRO A O   
1339 C  CB  . PRO A  156 ? 0.2176  0.1420 0.2016  0.0621  0.0356  -0.0130 155 PRO A CB  
1340 C  CG  . PRO A  156 ? 0.2888  0.1405 0.2048  0.0378  0.0564  -0.0370 155 PRO A CG  
1341 C  CD  . PRO A  156 ? 0.1793  0.1251 0.1456  0.0181  0.0182  -0.0410 155 PRO A CD  
1342 N  N   A LYS A  157 ? 0.1230  0.1330 0.1221  -0.0132 -0.0068 -0.0290 156 LYS A N   
1343 N  N   B LYS A  157 ? 0.1270  0.1344 0.1164  0.0078  0.0017  -0.0295 156 LYS A N   
1344 C  CA  A LYS A  157 ? 0.1448  0.1678 0.1155  -0.0400 0.0149  -0.0239 156 LYS A CA  
1345 C  CA  B LYS A  157 ? 0.1301  0.1894 0.1100  0.0018  0.0036  -0.0279 156 LYS A CA  
1346 C  C   A LYS A  157 ? 0.1323  0.1348 0.1040  0.0096  0.0006  0.0033  156 LYS A C   
1347 C  C   B LYS A  157 ? 0.1319  0.1330 0.0978  0.0152  -0.0023 0.0039  156 LYS A C   
1348 O  O   A LYS A  157 ? 0.1664  0.1750 0.1188  -0.0233 0.0125  -0.0040 156 LYS A O   
1349 O  O   B LYS A  157 ? 0.1671  0.1520 0.1592  -0.0106 0.0302  -0.0075 156 LYS A O   
1350 C  CB  A LYS A  157 ? 0.1750  0.2748 0.0908  -0.0530 -0.0142 -0.0282 156 LYS A CB  
1351 C  CB  B LYS A  157 ? 0.1668  0.3032 0.1316  -0.0348 -0.0291 -0.0464 156 LYS A CB  
1352 C  CG  A LYS A  157 ? 0.2168  0.2398 0.1495  -0.1096 -0.0099 -0.0883 156 LYS A CG  
1353 C  CG  B LYS A  157 ? 0.2518  0.3190 0.1786  -0.1010 -0.0891 -0.1039 156 LYS A CG  
1354 C  CD  A LYS A  157 ? 0.3286  0.1216 0.2773  0.0134  0.0549  -0.0841 156 LYS A CD  
1355 C  CD  B LYS A  157 ? 0.1160  0.2159 0.3952  -0.0312 -0.0274 -0.0446 156 LYS A CD  
1356 C  CE  A LYS A  157 ? 0.1377  0.1944 0.2928  -0.0093 0.0206  -0.0160 156 LYS A CE  
1357 C  CE  B LYS A  157 ? 0.2640  0.4530 0.1811  -0.0725 -0.1201 0.1386  156 LYS A CE  
1358 N  NZ  A LYS A  157 ? 0.1207  0.2831 0.1693  -0.0192 -0.0165 -0.1342 156 LYS A NZ  
1359 N  NZ  B LYS A  157 ? 0.1829  0.2532 0.1847  -0.0020 -0.0598 0.0638  156 LYS A NZ  
1360 N  N   . LEU A  158 ? 0.1574  0.1244 0.1107  0.0059  -0.0044 -0.0094 157 LEU A N   
1361 C  CA  . LEU A  158 ? 0.1423  0.1208 0.1298  0.0184  0.0215  -0.0204 157 LEU A CA  
1362 C  C   . LEU A  158 ? 0.1509  0.1531 0.1402  0.0186  -0.0306 -0.0453 157 LEU A C   
1363 O  O   . LEU A  158 ? 0.1527  0.1517 0.1344  0.0061  0.0069  -0.0326 157 LEU A O   
1364 C  CB  . LEU A  158 ? 0.1441  0.1259 0.1509  0.0156  -0.0027 -0.0113 157 LEU A CB  
1365 C  CG  . LEU A  158 ? 0.1092  0.1448 0.1617  0.0134  -0.0086 0.0068  157 LEU A CG  
1366 C  CD1 . LEU A  158 ? 0.1294  0.1639 0.1833  -0.0080 -0.0039 0.0142  157 LEU A CD1 
1367 C  CD2 . LEU A  158 ? 0.1256  0.1844 0.2518  0.0196  -0.0220 0.0062  157 LEU A CD2 
1368 N  N   A GLN A  159 ? 0.2066  0.1736 0.1100  0.0502  -0.0387 -0.0185 158 GLN A N   
1369 N  N   B GLN A  159 ? 0.2023  0.1815 0.1125  0.0587  -0.0287 -0.0148 158 GLN A N   
1370 C  CA  A GLN A  159 ? 0.2073  0.2278 0.1398  0.0702  -0.0355 -0.0015 158 GLN A CA  
1371 C  CA  B GLN A  159 ? 0.2138  0.2134 0.1402  0.0767  -0.0299 -0.0055 158 GLN A CA  
1372 C  C   A GLN A  159 ? 0.1914  0.1305 0.1524  0.0324  -0.0248 -0.0245 158 GLN A C   
1373 C  C   B GLN A  159 ? 0.1908  0.1307 0.1538  0.0326  -0.0226 -0.0266 158 GLN A C   
1374 O  O   A GLN A  159 ? 0.1761  0.1621 0.1274  0.0379  -0.0304 -0.0390 158 GLN A O   
1375 O  O   B GLN A  159 ? 0.1703  0.1718 0.1294  0.0416  -0.0337 -0.0377 158 GLN A O   
1376 C  CB  A GLN A  159 ? 0.2240  0.2594 0.1456  0.1088  -0.0377 -0.0190 158 GLN A CB  
1377 C  CB  B GLN A  159 ? 0.2885  0.2386 0.1700  0.1404  -0.0185 -0.0159 158 GLN A CB  
1378 C  CG  A GLN A  159 ? 0.2192  0.2662 0.1527  0.1041  -0.0469 -0.0145 158 GLN A CG  
1379 C  CG  B GLN A  159 ? 0.2630  0.3523 0.1790  0.0844  -0.0406 -0.0057 158 GLN A CG  
1380 C  CD  A GLN A  159 ? 0.2066  0.2400 0.1172  0.0785  0.0005  0.0093  158 GLN A CD  
1381 C  CD  B GLN A  159 ? 0.2816  0.3298 0.1800  -0.0091 0.0765  -0.0086 158 GLN A CD  
1382 O  OE1 A GLN A  159 ? 0.1811  0.1562 0.1441  0.0477  -0.0206 -0.0298 158 GLN A OE1 
1383 O  OE1 B GLN A  159 ? 0.3592  0.3743 0.1459  -0.0555 0.0670  -0.0222 158 GLN A OE1 
1384 N  NE2 A GLN A  159 ? 0.1720  0.1738 0.1592  0.0491  -0.0043 0.0357  158 GLN A NE2 
1385 N  NE2 B GLN A  159 ? 0.2134  0.2708 0.2576  -0.0269 0.0287  -0.0340 158 GLN A NE2 
1386 N  N   . LYS A  160 ? 0.1847  0.1280 0.1614  0.0325  -0.0357 -0.0201 159 LYS A N   
1387 C  CA  . LYS A  160 ? 0.1879  0.1355 0.1833  0.0168  -0.0285 -0.0139 159 LYS A CA  
1388 C  C   . LYS A  160 ? 0.1531  0.1189 0.1574  0.0130  -0.0321 0.0078  159 LYS A C   
1389 O  O   . LYS A  160 ? 0.1707  0.1542 0.1729  0.0186  -0.0406 0.0304  159 LYS A O   
1390 C  CB  . LYS A  160 ? 0.2283  0.1452 0.2192  -0.0190 -0.0829 0.0104  159 LYS A CB  
1391 C  CG  . LYS A  160 ? 0.2370  0.1919 0.2508  -0.0176 -0.0780 0.0188  159 LYS A CG  
1392 C  CD  . LYS A  160 ? 0.2712  0.2249 0.2386  -0.0471 -0.0996 0.0425  159 LYS A CD  
1393 C  CE  . LYS A  160 ? 0.2170  0.1944 0.2978  -0.0215 -0.0715 0.0873  159 LYS A CE  
1394 N  NZ  . LYS A  160 ? 0.2149  0.2073 0.4345  -0.0131 -0.0787 0.0829  159 LYS A NZ  
1395 N  N   . VAL A  161 ? 0.1445  0.1012 0.1720  0.0107  -0.0482 -0.0058 160 VAL A N   
1396 C  CA  . VAL A  161 ? 0.1206  0.1172 0.1465  0.0285  -0.0137 0.0084  160 VAL A CA  
1397 C  C   . VAL A  161 ? 0.1199  0.1172 0.1134  0.0163  0.0017  0.0012  160 VAL A C   
1398 O  O   . VAL A  161 ? 0.1578  0.1448 0.0987  0.0162  0.0119  0.0063  160 VAL A O   
1399 C  CB  . VAL A  161 ? 0.1142  0.1274 0.1520  0.0309  -0.0042 0.0166  160 VAL A CB  
1400 C  CG1 . VAL A  161 ? 0.2411  0.1775 0.1711  0.1121  0.0063  -0.0036 160 VAL A CG1 
1401 C  CG2 . VAL A  161 ? 0.1084  0.2213 0.2615  -0.0027 -0.0307 0.0939  160 VAL A CG2 
1402 N  N   . LEU A  162 ? 0.1160  0.1362 0.1030  -0.0060 0.0027  0.0003  161 LEU A N   
1403 C  CA  . LEU A  162 ? 0.1216  0.1574 0.0879  -0.0253 -0.0072 0.0035  161 LEU A CA  
1404 C  C   . LEU A  162 ? 0.1283  0.1483 0.1030  0.0165  -0.0041 -0.0126 161 LEU A C   
1405 O  O   . LEU A  162 ? 0.1689  0.1621 0.0971  -0.0127 -0.0201 -0.0105 161 LEU A O   
1406 C  CB  . LEU A  162 ? 0.1409  0.2030 0.1155  -0.0427 -0.0069 0.0001  161 LEU A CB  
1407 C  CG  . LEU A  162 ? 0.1682  0.1817 0.0970  -0.0184 0.0139  -0.0114 161 LEU A CG  
1408 C  CD1 . LEU A  162 ? 0.1438  0.3341 0.1276  -0.0653 -0.0051 0.0354  161 LEU A CD1 
1409 C  CD2 . LEU A  162 ? 0.3050  0.1581 0.1876  -0.0093 0.0223  0.0026  161 LEU A CD2 
1410 N  N   . ASP A  163 ? 0.1247  0.1438 0.1316  0.0146  -0.0089 0.0001  162 ASP A N   
1411 C  CA  . ASP A  163 ? 0.1323  0.1641 0.1359  0.0198  -0.0221 0.0075  162 ASP A CA  
1412 C  C   . ASP A  163 ? 0.1263  0.1703 0.1102  0.0081  -0.0190 -0.0019 162 ASP A C   
1413 O  O   . ASP A  163 ? 0.1750  0.1948 0.1301  0.0228  -0.0428 0.0018  162 ASP A O   
1414 C  CB  . ASP A  163 ? 0.1732  0.1506 0.1822  0.0317  -0.0212 -0.0151 162 ASP A CB  
1415 C  CG  . ASP A  163 ? 0.1535  0.1876 0.2117  0.0214  -0.0266 -0.0323 162 ASP A CG  
1416 O  OD1 . ASP A  163 ? 0.2127  0.2145 0.2319  -0.0125 0.0113  -0.0328 162 ASP A OD1 
1417 O  OD2 . ASP A  163 ? 0.3021  0.1944 0.2055  0.0442  -0.0397 -0.0230 162 ASP A OD2 
1418 N  N   . ALA A  164 ? 0.1164  0.1452 0.0944  0.0053  -0.0027 -0.0038 163 ALA A N   
1419 C  CA  . ALA A  164 ? 0.1254  0.1395 0.1155  -0.0008 -0.0089 0.0059  163 ALA A CA  
1420 C  C   . ALA A  164 ? 0.1301  0.1499 0.0827  0.0175  -0.0195 0.0016  163 ALA A C   
1421 O  O   . ALA A  164 ? 0.1531  0.1707 0.0985  0.0091  -0.0066 0.0030  163 ALA A O   
1422 C  CB  . ALA A  164 ? 0.1499  0.1581 0.1213  -0.0133 -0.0222 0.0149  163 ALA A CB  
1423 N  N   . LEU A  165 ? 0.1319  0.1256 0.1032  0.0100  -0.0117 -0.0019 164 LEU A N   
1424 C  CA  . LEU A  165 ? 0.1366  0.1241 0.1059  -0.0022 -0.0366 0.0015  164 LEU A CA  
1425 C  C   . LEU A  165 ? 0.1258  0.1524 0.0952  0.0076  -0.0177 0.0046  164 LEU A C   
1426 O  O   . LEU A  165 ? 0.1341  0.1592 0.1021  0.0042  -0.0164 -0.0158 164 LEU A O   
1427 C  CB  . LEU A  165 ? 0.1459  0.1405 0.0934  -0.0050 -0.0199 0.0155  164 LEU A CB  
1428 C  CG  . LEU A  165 ? 0.1574  0.1465 0.1002  -0.0017 -0.0386 0.0027  164 LEU A CG  
1429 C  CD1 . LEU A  165 ? 0.1844  0.1632 0.1136  -0.0127 -0.0201 0.0225  164 LEU A CD1 
1430 C  CD2 . LEU A  165 ? 0.1506  0.1646 0.1391  -0.0006 -0.0557 0.0006  164 LEU A CD2 
1431 N  N   . GLN A  166 ? 0.1269  0.1603 0.1005  0.0148  -0.0296 -0.0001 165 GLN A N   
1432 C  CA  . GLN A  166 ? 0.1164  0.1854 0.1068  0.0145  -0.0287 -0.0062 165 GLN A CA  
1433 C  C   . GLN A  166 ? 0.1384  0.1438 0.0928  0.0035  -0.0243 -0.0110 165 GLN A C   
1434 O  O   . GLN A  166 ? 0.1492  0.1738 0.1022  0.0092  -0.0236 -0.0110 165 GLN A O   
1435 C  CB  . GLN A  166 ? 0.1373  0.1962 0.1289  0.0433  -0.0331 0.0004  165 GLN A CB  
1436 C  CG  . GLN A  166 ? 0.1912  0.1926 0.1840  0.0006  -0.0359 -0.0115 165 GLN A CG  
1437 C  CD  . GLN A  166 ? 0.1700  0.2132 0.1585  0.0337  -0.0346 -0.0317 165 GLN A CD  
1438 O  OE1 . GLN A  166 ? 0.2187  0.2436 0.1732  0.0317  -0.0343 0.0095  165 GLN A OE1 
1439 N  NE2 . GLN A  166 ? 0.1951  0.2168 0.1736  0.0086  -0.0223 -0.0193 165 GLN A NE2 
1440 N  N   . ALA A  167 ? 0.1307  0.1412 0.1172  0.0122  -0.0067 0.0065  166 ALA A N   
1441 C  CA  . ALA A  167 ? 0.1348  0.1499 0.1247  0.0017  -0.0073 0.0076  166 ALA A CA  
1442 C  C   . ALA A  167 ? 0.1217  0.1610 0.1137  -0.0080 -0.0228 -0.0160 166 ALA A C   
1443 O  O   . ALA A  167 ? 0.1434  0.1714 0.1234  -0.0083 -0.0020 -0.0009 166 ALA A O   
1444 C  CB  . ALA A  167 ? 0.1969  0.1524 0.1603  -0.0111 0.0094  -0.0034 166 ALA A CB  
1445 N  N   . ILE A  168 ? 0.1151  0.1416 0.1023  0.0015  -0.0264 0.0016  167 ILE A N   
1446 C  CA  . ILE A  168 ? 0.1221  0.1456 0.1007  0.0061  -0.0130 -0.0017 167 ILE A CA  
1447 C  C   . ILE A  168 ? 0.1116  0.1430 0.0987  0.0201  -0.0041 -0.0137 167 ILE A C   
1448 O  O   . ILE A  168 ? 0.1143  0.1416 0.1189  0.0113  -0.0283 -0.0190 167 ILE A O   
1449 C  CB  . ILE A  168 ? 0.1178  0.1682 0.1037  0.0203  -0.0304 -0.0229 167 ILE A CB  
1450 C  CG1 . ILE A  168 ? 0.1337  0.1614 0.0964  0.0217  -0.0328 -0.0248 167 ILE A CG1 
1451 C  CG2 . ILE A  168 ? 0.1459  0.1808 0.1538  -0.0380 -0.0212 -0.0105 167 ILE A CG2 
1452 C  CD1 . ILE A  168 ? 0.1581  0.2037 0.1108  0.0478  -0.0615 -0.0339 167 ILE A CD1 
1453 N  N   . LYS A  169 ? 0.1190  0.1571 0.0988  0.0051  -0.0175 -0.0149 168 LYS A N   
1454 C  CA  . LYS A  169 ? 0.1150  0.1474 0.1077  0.0079  -0.0204 -0.0119 168 LYS A CA  
1455 C  C   . LYS A  169 ? 0.1117  0.1326 0.0785  0.0001  -0.0182 -0.0170 168 LYS A C   
1456 O  O   . LYS A  169 ? 0.1185  0.1524 0.1020  0.0120  -0.0034 -0.0088 168 LYS A O   
1457 C  CB  . LYS A  169 ? 0.1305  0.1768 0.1198  0.0315  -0.0397 -0.0145 168 LYS A CB  
1458 C  CG  . LYS A  169 ? 0.1987  0.2398 0.1768  0.0430  0.0055  -0.0320 168 LYS A CG  
1459 C  CD  . LYS A  169 ? 0.2568  0.2759 0.1865  0.0609  0.0346  0.0293  168 LYS A CD  
1460 C  CE  . LYS A  169 ? 0.2443  0.3406 0.1495  0.0399  -0.0212 -0.0285 168 LYS A CE  
1461 N  NZ  . LYS A  169 ? 0.2098  0.5543 0.2372  -0.0833 0.0052  -0.1620 168 LYS A NZ  
1462 N  N   . THR A  170 ? 0.1066  0.1653 0.0813  0.0062  -0.0120 -0.0228 169 THR A N   
1463 C  CA  . THR A  170 ? 0.0935  0.1578 0.0879  0.0050  -0.0200 -0.0255 169 THR A CA  
1464 C  C   . THR A  170 ? 0.0985  0.1560 0.0865  -0.0024 -0.0078 -0.0050 169 THR A C   
1465 O  O   . THR A  170 ? 0.1032  0.1610 0.0986  -0.0067 0.0006  -0.0089 169 THR A O   
1466 C  CB  . THR A  170 ? 0.1048  0.1711 0.0946  -0.0121 -0.0264 -0.0048 169 THR A CB  
1467 O  OG1 . THR A  170 ? 0.1197  0.1772 0.0926  0.0021  -0.0106 -0.0121 169 THR A OG1 
1468 C  CG2 . THR A  170 ? 0.1004  0.2084 0.0915  -0.0049 -0.0176 -0.0160 169 THR A CG2 
1469 N  N   . LYS A  171 ? 0.1032  0.1639 0.1106  0.0050  -0.0032 -0.0272 170 LYS A N   
1470 C  CA  . LYS A  171 ? 0.0784  0.1668 0.1224  -0.0027 -0.0057 -0.0079 170 LYS A CA  
1471 C  C   . LYS A  171 ? 0.1046  0.1729 0.0933  0.0016  -0.0089 -0.0253 170 LYS A C   
1472 O  O   . LYS A  171 ? 0.1161  0.2041 0.0993  0.0048  -0.0010 -0.0171 170 LYS A O   
1473 C  CB  . LYS A  171 ? 0.1055  0.1693 0.1815  0.0105  -0.0107 -0.0366 170 LYS A CB  
1474 C  CG  . LYS A  171 ? 0.1109  0.1969 0.1951  0.0294  -0.0059 -0.0200 170 LYS A CG  
1475 C  CD  . LYS A  171 ? 0.1427  0.2310 0.2400  0.0378  0.0091  -0.0260 170 LYS A CD  
1476 C  CE  . LYS A  171 ? 0.2661  0.4307 0.5332  0.1886  -0.0758 -0.1038 170 LYS A CE  
1477 N  NZ  . LYS A  171 ? 0.6400  0.4834 1.4089  0.1187  -0.3512 -0.3009 170 LYS A NZ  
1478 N  N   . GLY A  172 ? 0.0915  0.1833 0.1141  -0.0153 -0.0034 -0.0278 171 GLY A N   
1479 C  CA  . GLY A  172 ? 0.1204  0.1890 0.1294  -0.0132 -0.0001 -0.0119 171 GLY A CA  
1480 C  C   . GLY A  172 ? 0.1270  0.1851 0.1076  -0.0218 0.0063  -0.0147 171 GLY A C   
1481 O  O   . GLY A  172 ? 0.1427  0.2213 0.1187  -0.0333 0.0033  -0.0060 171 GLY A O   
1482 N  N   . LYS A  173 ? 0.1089  0.1685 0.0827  0.0095  -0.0059 -0.0223 172 LYS A N   
1483 C  CA  . LYS A  173 ? 0.1377  0.1729 0.0901  -0.0158 -0.0173 -0.0039 172 LYS A CA  
1484 C  C   . LYS A  173 ? 0.1156  0.1574 0.0865  0.0021  -0.0077 0.0027  172 LYS A C   
1485 O  O   . LYS A  173 ? 0.1459  0.1585 0.0794  -0.0064 -0.0176 0.0076  172 LYS A O   
1486 C  CB  . LYS A  173 ? 0.1234  0.1958 0.1120  0.0029  -0.0120 -0.0030 172 LYS A CB  
1487 C  CG  . LYS A  173 ? 0.1725  0.2034 0.1351  0.0002  -0.0394 -0.0139 172 LYS A CG  
1488 C  CD  . LYS A  173 ? 0.1445  0.2346 0.1405  -0.0279 -0.0223 0.0255  172 LYS A CD  
1489 C  CE  . LYS A  173 ? 0.1682  0.2346 0.1657  -0.0003 -0.0102 0.0424  172 LYS A CE  
1490 N  NZ  . LYS A  173 ? 0.1614  0.2946 0.1610  -0.0054 -0.0141 0.0174  172 LYS A NZ  
1491 N  N   . ARG A  174 ? 0.1560  0.1488 0.0838  0.0037  -0.0233 0.0009  173 ARG A N   
1492 C  CA  . ARG A  174 ? 0.1391  0.1438 0.0932  -0.0058 -0.0326 0.0153  173 ARG A CA  
1493 C  C   . ARG A  174 ? 0.1696  0.1373 0.0768  -0.0079 -0.0175 0.0154  173 ARG A C   
1494 O  O   . ARG A  174 ? 0.2124  0.1653 0.1028  -0.0081 -0.0469 0.0370  173 ARG A O   
1495 C  CB  . ARG A  174 ? 0.1355  0.2030 0.0971  -0.0162 -0.0200 0.0080  173 ARG A CB  
1496 C  CG  . ARG A  174 ? 0.1456  0.2662 0.1456  -0.0381 -0.0223 0.0364  173 ARG A CG  
1497 C  CD  . ARG A  174 ? 0.1865  0.2852 0.1502  -0.0719 0.0016  -0.0256 173 ARG A CD  
1498 N  NE  . ARG A  174 ? 0.1894  0.3103 0.1993  -0.0298 0.0511  -0.0971 173 ARG A NE  
1499 C  CZ  . ARG A  174 ? 0.1337  0.3018 0.3492  -0.0194 0.0660  -0.1582 173 ARG A CZ  
1500 N  NH1 . ARG A  174 ? 0.1111  0.3459 0.4249  -0.0318 0.0263  -0.1345 173 ARG A NH1 
1501 N  NH2 . ARG A  174 ? 0.1700  0.3240 0.3657  -0.0519 0.1096  -0.1565 173 ARG A NH2 
1502 N  N   . ALA A  175 ? 0.1463  0.1305 0.1141  0.0022  -0.0289 0.0027  174 ALA A N   
1503 C  CA  . ALA A  175 ? 0.1720  0.1481 0.1208  0.0036  -0.0487 -0.0073 174 ALA A CA  
1504 C  C   . ALA A  175 ? 0.1923  0.1330 0.0854  0.0004  -0.0366 0.0210  174 ALA A C   
1505 O  O   . ALA A  175 ? 0.1538  0.1452 0.0908  -0.0055 -0.0345 0.0290  174 ALA A O   
1506 C  CB  . ALA A  175 ? 0.1452  0.1865 0.1696  0.0289  -0.0394 0.0003  174 ALA A CB  
1507 N  N   A PRO A  176 ? 0.1678  0.1259 0.0935  -0.0149 -0.0467 0.0311  175 PRO A N   
1508 N  N   B PRO A  176 ? 0.2569  0.1276 0.1045  -0.0017 -0.0385 0.0226  175 PRO A N   
1509 C  CA  A PRO A  176 ? 0.1822  0.1128 0.0970  -0.0148 -0.0427 0.0343  175 PRO A CA  
1510 C  CA  B PRO A  176 ? 0.2235  0.1714 0.1116  0.0024  -0.0018 -0.0124 175 PRO A CA  
1511 C  C   A PRO A  176 ? 0.1341  0.1240 0.1137  0.0000  -0.0407 0.0402  175 PRO A C   
1512 C  C   B PRO A  176 ? 0.1757  0.1409 0.1062  0.0027  -0.0425 -0.0024 175 PRO A C   
1513 O  O   A PRO A  176 ? 0.1380  0.1181 0.0730  0.0016  -0.0494 0.0240  175 PRO A O   
1514 O  O   B PRO A  176 ? 0.1914  0.1822 0.1883  0.0041  -0.0514 0.0348  175 PRO A O   
1515 C  CB  A PRO A  176 ? 0.1553  0.1179 0.1199  -0.0212 -0.0554 0.0508  175 PRO A CB  
1516 C  CB  B PRO A  176 ? 0.2881  0.1840 0.1366  -0.0055 -0.0032 0.0461  175 PRO A CB  
1517 C  CG  A PRO A  176 ? 0.1987  0.1283 0.1344  -0.0063 -0.0432 0.0366  175 PRO A CG  
1518 C  CG  B PRO A  176 ? 0.4171  0.1958 0.1678  -0.0215 -0.0950 0.0605  175 PRO A CG  
1519 C  CD  A PRO A  176 ? 0.1621  0.1386 0.1312  0.0100  -0.0353 0.0584  175 PRO A CD  
1520 C  CD  B PRO A  176 ? 0.3445  0.1483 0.0919  0.0098  -0.0484 0.0192  175 PRO A CD  
1521 N  N   . PHE A  177 ? 0.1571  0.1337 0.0960  -0.0175 -0.0336 0.0193  176 PHE A N   
1522 C  CA  . PHE A  177 ? 0.1578  0.1305 0.0847  -0.0203 -0.0271 0.0110  176 PHE A CA  
1523 C  C   . PHE A  177 ? 0.1624  0.1119 0.1092  -0.0094 -0.0268 0.0270  176 PHE A C   
1524 O  O   . PHE A  177 ? 0.1470  0.1524 0.1244  0.0044  -0.0279 0.0132  176 PHE A O   
1525 C  CB  . PHE A  177 ? 0.1599  0.1169 0.1038  -0.0141 0.0054  0.0256  176 PHE A CB  
1526 C  CG  . PHE A  177 ? 0.1553  0.1005 0.1216  -0.0178 -0.0100 0.0137  176 PHE A CG  
1527 C  CD1 . PHE A  177 ? 0.1696  0.1181 0.1110  0.0283  -0.0305 0.0151  176 PHE A CD1 
1528 C  CD2 . PHE A  177 ? 0.1653  0.1348 0.1348  -0.0225 -0.0136 0.0264  176 PHE A CD2 
1529 C  CE1 . PHE A  177 ? 0.2168  0.1119 0.1153  0.0074  -0.0204 0.0039  176 PHE A CE1 
1530 C  CE2 . PHE A  177 ? 0.2102  0.1894 0.1307  -0.0303 -0.0140 0.0310  176 PHE A CE2 
1531 C  CZ  . PHE A  177 ? 0.2020  0.1384 0.1249  -0.0017 0.0051  0.0086  176 PHE A CZ  
1532 N  N   . THR A  178 ? 0.1732  0.1053 0.1499  -0.0032 -0.0409 0.0228  177 THR A N   
1533 C  CA  . THR A  178 ? 0.1919  0.1128 0.1434  -0.0182 -0.0455 0.0144  177 THR A CA  
1534 C  C   . THR A  178 ? 0.1488  0.1084 0.1549  0.0139  -0.0366 0.0167  177 THR A C   
1535 O  O   . THR A  178 ? 0.1632  0.1240 0.1817  0.0021  -0.0431 -0.0089 177 THR A O   
1536 C  CB  . THR A  178 ? 0.1976  0.1305 0.1700  -0.0157 -0.0384 0.0296  177 THR A CB  
1537 O  OG1 . THR A  178 ? 0.2468  0.1757 0.2178  -0.0039 -0.0886 0.0537  177 THR A OG1 
1538 C  CG2 . THR A  178 ? 0.3377  0.1693 0.1368  -0.0374 -0.0190 0.0233  177 THR A CG2 
1539 N  N   . ASN A  179 ? 0.1883  0.0986 0.1391  0.0002  -0.0477 0.0015  178 ASN A N   
1540 C  CA  . ASN A  179 ? 0.1890  0.1146 0.1664  -0.0011 -0.0250 0.0144  178 ASN A CA  
1541 C  C   . ASN A  179 ? 0.1316  0.1270 0.1720  -0.0001 -0.0250 0.0027  178 ASN A C   
1542 O  O   . ASN A  179 ? 0.1520  0.1513 0.2150  0.0189  -0.0321 0.0062  178 ASN A O   
1543 C  CB  . ASN A  179 ? 0.1890  0.1142 0.2339  0.0204  -0.0226 0.0216  178 ASN A CB  
1544 C  CG  . ASN A  179 ? 0.1736  0.1738 0.3230  0.0100  -0.0357 -0.0078 178 ASN A CG  
1545 O  OD1 . ASN A  179 ? 0.1914  0.1923 0.3941  0.0077  -0.0674 -0.0127 178 ASN A OD1 
1546 N  ND2 . ASN A  179 ? 0.2213  0.2346 0.3391  0.0628  -0.0364 -0.0030 178 ASN A ND2 
1547 N  N   . PHE A  180 ? 0.1409  0.1117 0.1323  0.0036  -0.0198 0.0012  179 PHE A N   
1548 C  CA  . PHE A  180 ? 0.1323  0.1172 0.1289  -0.0058 -0.0326 -0.0021 179 PHE A CA  
1549 C  C   . PHE A  180 ? 0.1115  0.1074 0.1111  -0.0085 -0.0163 0.0008  179 PHE A C   
1550 O  O   . PHE A  180 ? 0.1412  0.1362 0.1230  0.0216  -0.0058 0.0068  179 PHE A O   
1551 C  CB  . PHE A  180 ? 0.1402  0.1305 0.1264  -0.0135 -0.0414 0.0104  179 PHE A CB  
1552 C  CG  . PHE A  180 ? 0.1261  0.1230 0.1243  -0.0035 -0.0330 0.0103  179 PHE A CG  
1553 C  CD1 . PHE A  180 ? 0.1208  0.1524 0.2030  -0.0118 -0.0348 0.0252  179 PHE A CD1 
1554 C  CD2 . PHE A  180 ? 0.1492  0.1074 0.1179  -0.0029 -0.0181 -0.0063 179 PHE A CD2 
1555 C  CE1 . PHE A  180 ? 0.1524  0.1531 0.1973  -0.0003 -0.0055 0.0318  179 PHE A CE1 
1556 C  CE2 . PHE A  180 ? 0.1307  0.1438 0.1102  -0.0218 -0.0259 -0.0097 179 PHE A CE2 
1557 C  CZ  . PHE A  180 ? 0.1384  0.1373 0.1405  -0.0049 -0.0201 0.0047  179 PHE A CZ  
1558 N  N   . ASP A  181 ? 0.1405  0.1276 0.0998  0.0050  -0.0176 0.0111  180 ASP A N   
1559 C  CA  . ASP A  181 ? 0.1465  0.1212 0.0856  0.0035  -0.0031 0.0088  180 ASP A CA  
1560 C  C   . ASP A  181 ? 0.1040  0.1448 0.1007  0.0051  -0.0113 0.0013  180 ASP A C   
1561 O  O   . ASP A  181 ? 0.1089  0.1506 0.1222  0.0000  0.0012  0.0031  180 ASP A O   
1562 C  CB  . ASP A  181 ? 0.1567  0.1274 0.1137  0.0170  -0.0170 -0.0005 180 ASP A CB  
1563 C  CG  . ASP A  181 ? 0.1391  0.1224 0.0959  -0.0102 0.0049  -0.0062 180 ASP A CG  
1564 O  OD1 . ASP A  181 ? 0.1164  0.1402 0.1259  -0.0099 -0.0113 -0.0024 180 ASP A OD1 
1565 O  OD2 . ASP A  181 ? 0.1664  0.1560 0.1305  -0.0024 -0.0144 -0.0291 180 ASP A OD2 
1566 N  N   . PRO A  182 ? 0.1129  0.1269 0.0952  0.0005  -0.0022 -0.0104 181 PRO A N   
1567 C  CA  . PRO A  182 ? 0.1441  0.1252 0.0928  -0.0072 0.0061  0.0008  181 PRO A CA  
1568 C  C   . PRO A  182 ? 0.1067  0.1301 0.1012  -0.0018 -0.0105 -0.0088 181 PRO A C   
1569 O  O   . PRO A  182 ? 0.1155  0.1287 0.1030  -0.0030 -0.0012 -0.0035 181 PRO A O   
1570 C  CB  . PRO A  182 ? 0.1330  0.1488 0.1190  -0.0063 0.0074  -0.0219 181 PRO A CB  
1571 C  CG  . PRO A  182 ? 0.1412  0.1233 0.1351  -0.0048 0.0181  -0.0038 181 PRO A CG  
1572 C  CD  . PRO A  182 ? 0.1067  0.1351 0.0989  0.0013  0.0051  0.0020  181 PRO A CD  
1573 N  N   . SER A  183 ? 0.1150  0.1556 0.0900  -0.0053 -0.0082 -0.0114 182 SER A N   
1574 C  CA  . SER A  183 ? 0.1319  0.1495 0.0900  -0.0215 -0.0038 -0.0094 182 SER A CA  
1575 C  C   . SER A  183 ? 0.1136  0.1298 0.1004  -0.0322 0.0006  -0.0011 182 SER A C   
1576 O  O   . SER A  183 ? 0.1571  0.1585 0.1013  -0.0434 0.0060  -0.0018 182 SER A O   
1577 C  CB  . SER A  183 ? 0.1495  0.1840 0.1213  -0.0367 -0.0184 -0.0280 182 SER A CB  
1578 O  OG  . SER A  183 ? 0.1772  0.1786 0.1307  -0.0625 -0.0211 -0.0276 182 SER A OG  
1579 N  N   . THR A  184 ? 0.1225  0.1156 0.1220  -0.0048 -0.0009 -0.0170 183 THR A N   
1580 C  CA  . THR A  184 ? 0.1276  0.1108 0.1542  -0.0067 0.0027  -0.0218 183 THR A CA  
1581 C  C   . THR A  184 ? 0.1234  0.1253 0.1225  -0.0050 0.0111  -0.0089 183 THR A C   
1582 O  O   . THR A  184 ? 0.1386  0.1263 0.1973  0.0002  0.0447  -0.0165 183 THR A O   
1583 C  CB  . THR A  184 ? 0.1323  0.1217 0.1811  0.0314  0.0353  -0.0219 183 THR A CB  
1584 O  OG1 . THR A  184 ? 0.1761  0.1380 0.1682  0.0083  -0.0151 -0.0087 183 THR A OG1 
1585 C  CG2 . THR A  184 ? 0.2418  0.1316 0.2748  -0.0236 0.0879  -0.0291 183 THR A CG2 
1586 N  N   . LEU A  185 ? 0.1128  0.1028 0.1111  -0.0032 -0.0095 -0.0136 184 LEU A N   
1587 C  CA  . LEU A  185 ? 0.1190  0.1003 0.1269  0.0032  -0.0072 0.0010  184 LEU A CA  
1588 C  C   . LEU A  185 ? 0.1040  0.1235 0.1053  -0.0006 -0.0113 -0.0003 184 LEU A C   
1589 O  O   . LEU A  185 ? 0.1145  0.1155 0.1380  -0.0086 -0.0270 0.0196  184 LEU A O   
1590 C  CB  . LEU A  185 ? 0.1416  0.1031 0.1120  0.0113  -0.0260 -0.0049 184 LEU A CB  
1591 C  CG  . LEU A  185 ? 0.1599  0.1267 0.1253  0.0009  -0.0344 -0.0024 184 LEU A CG  
1592 C  CD1 . LEU A  185 ? 0.3621  0.1377 0.1016  -0.0035 -0.0383 -0.0379 184 LEU A CD1 
1593 C  CD2 . LEU A  185 ? 0.1423  0.2275 0.1923  -0.0183 -0.0531 0.0356  184 LEU A CD2 
1594 N  N   . LEU A  186 ? 0.0960  0.1283 0.1153  0.0046  -0.0242 -0.0006 185 LEU A N   
1595 C  CA  . LEU A  186 ? 0.1044  0.1269 0.1120  0.0052  -0.0223 -0.0005 185 LEU A CA  
1596 C  C   . LEU A  186 ? 0.1231  0.1068 0.0977  0.0005  -0.0267 -0.0171 185 LEU A C   
1597 O  O   . LEU A  186 ? 0.1194  0.1276 0.1171  0.0083  -0.0171 -0.0143 185 LEU A O   
1598 C  CB  . LEU A  186 ? 0.1093  0.1474 0.1319  -0.0196 -0.0201 -0.0051 185 LEU A CB  
1599 C  CG  . LEU A  186 ? 0.1054  0.1420 0.1441  -0.0041 -0.0091 0.0000  185 LEU A CG  
1600 C  CD1 . LEU A  186 ? 0.1107  0.2257 0.1890  -0.0245 0.0076  -0.0203 185 LEU A CD1 
1601 C  CD2 . LEU A  186 ? 0.1214  0.1549 0.1969  0.0069  0.0068  -0.0102 185 LEU A CD2 
1602 N  N   . PRO A  187 ? 0.1088  0.1161 0.1128  0.0113  -0.0270 -0.0134 186 PRO A N   
1603 C  CA  . PRO A  187 ? 0.1330  0.1208 0.1029  -0.0102 -0.0158 -0.0127 186 PRO A CA  
1604 C  C   . PRO A  187 ? 0.1058  0.1185 0.1163  0.0059  -0.0157 -0.0073 186 PRO A C   
1605 O  O   . PRO A  187 ? 0.1217  0.1341 0.1351  -0.0092 -0.0159 -0.0346 186 PRO A O   
1606 C  CB  . PRO A  187 ? 0.1513  0.1120 0.1398  0.0039  -0.0009 -0.0025 186 PRO A CB  
1607 C  CG  . PRO A  187 ? 0.1287  0.1603 0.1155  0.0144  -0.0041 -0.0011 186 PRO A CG  
1608 C  CD  . PRO A  187 ? 0.1341  0.0996 0.1307  0.0203  -0.0192 -0.0057 186 PRO A CD  
1609 N  N   A SER A  188 ? 0.1330  0.1225 0.1198  0.0212  -0.0082 -0.0242 187 SER A N   
1610 N  N   B SER A  188 ? 0.1154  0.1312 0.1203  0.0114  -0.0106 -0.0245 187 SER A N   
1611 C  CA  A SER A  188 ? 0.1178  0.1441 0.1488  0.0146  -0.0074 -0.0621 187 SER A CA  
1612 C  CA  B SER A  188 ? 0.1155  0.1434 0.1427  0.0089  -0.0140 -0.0553 187 SER A CA  
1613 C  C   A SER A  188 ? 0.1463  0.1671 0.1283  0.0205  -0.0008 -0.0914 187 SER A C   
1614 C  C   B SER A  188 ? 0.1409  0.1919 0.1366  0.0152  -0.0094 -0.0673 187 SER A C   
1615 O  O   A SER A  188 ? 0.1420  0.2098 0.1542  -0.0085 0.0024  -0.0991 187 SER A O   
1616 O  O   B SER A  188 ? 0.1362  0.2687 0.1574  -0.0247 -0.0043 -0.0458 187 SER A O   
1617 C  CB  A SER A  188 ? 0.1492  0.1817 0.1966  0.0187  0.0050  -0.1097 187 SER A CB  
1618 C  CB  B SER A  188 ? 0.0646  0.2099 0.2072  0.0452  -0.0329 -0.0716 187 SER A CB  
1619 O  OG  A SER A  188 ? 0.1423  0.2293 0.1659  -0.0141 0.0200  -0.0900 187 SER A OG  
1620 O  OG  B SER A  188 ? 0.1800  0.1912 0.2081  0.0000  0.0425  -0.0622 187 SER A OG  
1621 N  N   . SER A  189 ? 0.1621  0.1937 0.1456  0.0722  -0.0372 -0.0490 188 SER A N   
1622 C  CA  . SER A  189 ? 0.1973  0.2382 0.1738  0.1115  -0.0683 -0.0748 188 SER A CA  
1623 C  C   . SER A  189 ? 0.1269  0.1761 0.1567  0.0578  -0.0535 -0.0422 188 SER A C   
1624 O  O   . SER A  189 ? 0.1488  0.1509 0.1610  0.0239  -0.0438 -0.0348 188 SER A O   
1625 C  CB  . SER A  189 ? 0.2999  0.6086 0.0970  0.1942  -0.0669 0.0266  188 SER A CB  
1626 O  OG  . SER A  189 ? 0.3074  0.6053 0.1646  0.2068  -0.0537 -0.0145 188 SER A OG  
1627 N  N   . LEU A  190 ? 0.1380  0.1416 0.1488  0.0417  -0.0547 -0.0310 189 LEU A N   
1628 C  CA  . LEU A  190 ? 0.1423  0.1212 0.1241  0.0350  -0.0490 -0.0051 189 LEU A CA  
1629 C  C   . LEU A  190 ? 0.1427  0.1259 0.1190  0.0190  -0.0383 0.0078  189 LEU A C   
1630 O  O   . LEU A  190 ? 0.1190  0.1463 0.1499  0.0116  -0.0281 0.0111  189 LEU A O   
1631 C  CB  . LEU A  190 ? 0.1513  0.1420 0.1764  -0.0122 -0.0559 0.0585  189 LEU A CB  
1632 C  CG  . LEU A  190 ? 0.1678  0.1675 0.2133  -0.0091 -0.0856 0.0397  189 LEU A CG  
1633 C  CD1 . LEU A  190 ? 0.2133  0.2072 0.2476  -0.0335 -0.0509 0.0835  189 LEU A CD1 
1634 C  CD2 . LEU A  190 ? 0.1714  0.1980 0.1567  -0.0081 -0.0450 0.0233  189 LEU A CD2 
1635 N  N   . ASP A  191 ? 0.1567  0.1205 0.0971  0.0156  -0.0495 -0.0068 190 ASP A N   
1636 C  CA  . ASP A  191 ? 0.1549  0.1216 0.0864  0.0223  -0.0194 -0.0083 190 ASP A CA  
1637 C  C   . ASP A  191 ? 0.0908  0.1276 0.0925  -0.0082 -0.0106 0.0009  190 ASP A C   
1638 O  O   . ASP A  191 ? 0.0917  0.1271 0.0989  0.0055  -0.0154 -0.0115 190 ASP A O   
1639 C  CB  . ASP A  191 ? 0.1897  0.1826 0.0892  0.0179  -0.0107 -0.0055 190 ASP A CB  
1640 C  CG  . ASP A  191 ? 0.3085  0.2134 0.1420  0.0584  0.0317  -0.0249 190 ASP A CG  
1641 O  OD1 . ASP A  191 ? 0.3456  0.2174 0.1527  0.0521  -0.0650 -0.0527 190 ASP A OD1 
1642 O  OD2 . ASP A  191 ? 0.4282  0.3564 0.2661  -0.0097 0.1283  -0.0904 190 ASP A OD2 
1643 N  N   . PHE A  192 ? 0.1045  0.1232 0.0908  0.0158  -0.0081 -0.0002 191 PHE A N   
1644 C  CA  . PHE A  192 ? 0.1075  0.1124 0.0637  0.0148  -0.0044 0.0032  191 PHE A CA  
1645 C  C   . PHE A  192 ? 0.0883  0.1307 0.0723  0.0127  -0.0178 0.0091  191 PHE A C   
1646 O  O   . PHE A  192 ? 0.1080  0.1409 0.0695  0.0122  -0.0184 0.0128  191 PHE A O   
1647 C  CB  . PHE A  192 ? 0.1083  0.1319 0.0856  -0.0125 -0.0087 0.0187  191 PHE A CB  
1648 C  CG  . PHE A  192 ? 0.1108  0.1177 0.0971  0.0006  -0.0081 0.0097  191 PHE A CG  
1649 C  CD1 . PHE A  192 ? 0.1124  0.1137 0.1326  -0.0165 -0.0209 0.0203  191 PHE A CD1 
1650 C  CD2 . PHE A  192 ? 0.1111  0.1465 0.0979  0.0116  0.0051  0.0249  191 PHE A CD2 
1651 C  CE1 . PHE A  192 ? 0.1023  0.1391 0.1305  -0.0013 -0.0218 0.0116  191 PHE A CE1 
1652 C  CE2 . PHE A  192 ? 0.1256  0.1430 0.1263  -0.0039 -0.0129 0.0134  191 PHE A CE2 
1653 C  CZ  . PHE A  192 ? 0.1205  0.1452 0.1743  0.0003  -0.0284 0.0026  191 PHE A CZ  
1654 N  N   . TRP A  193 ? 0.0952  0.1144 0.0847  0.0148  -0.0070 0.0004  192 TRP A N   
1655 C  CA  . TRP A  193 ? 0.0926  0.1146 0.0891  0.0044  0.0044  0.0088  192 TRP A CA  
1656 C  C   . TRP A  193 ? 0.0882  0.1217 0.0800  0.0071  -0.0136 0.0087  192 TRP A C   
1657 O  O   . TRP A  193 ? 0.1074  0.1420 0.0864  0.0233  -0.0061 0.0232  192 TRP A O   
1658 C  CB  . TRP A  193 ? 0.1159  0.1268 0.0801  -0.0027 0.0023  -0.0003 192 TRP A CB  
1659 C  CG  . TRP A  193 ? 0.1120  0.1162 0.0892  0.0024  0.0043  0.0175  192 TRP A CG  
1660 C  CD1 . TRP A  193 ? 0.1312  0.1524 0.0864  0.0029  0.0174  0.0233  192 TRP A CD1 
1661 C  CD2 . TRP A  193 ? 0.1067  0.1199 0.0914  -0.0023 0.0078  0.0071  192 TRP A CD2 
1662 N  NE1 . TRP A  193 ? 0.1224  0.1951 0.0961  0.0102  0.0033  0.0435  192 TRP A NE1 
1663 C  CE2 . TRP A  193 ? 0.1084  0.1488 0.1032  0.0111  0.0084  0.0312  192 TRP A CE2 
1664 C  CE3 . TRP A  193 ? 0.1119  0.1287 0.1180  -0.0015 -0.0261 0.0054  192 TRP A CE3 
1665 C  CZ2 . TRP A  193 ? 0.1168  0.1606 0.1280  -0.0024 0.0128  0.0348  192 TRP A CZ2 
1666 C  CZ3 . TRP A  193 ? 0.1283  0.1373 0.1249  -0.0111 -0.0006 0.0076  192 TRP A CZ3 
1667 C  CH2 . TRP A  193 ? 0.1199  0.1459 0.1359  -0.0043 -0.0008 0.0201  192 TRP A CH2 
1668 N  N   . THR A  194 ? 0.0819  0.1232 0.0873  0.0139  -0.0055 0.0121  193 THR A N   
1669 C  CA  . THR A  194 ? 0.0960  0.1194 0.0885  0.0064  0.0022  0.0144  193 THR A CA  
1670 C  C   . THR A  194 ? 0.0890  0.1307 0.0741  0.0176  0.0013  0.0305  193 THR A C   
1671 O  O   . THR A  194 ? 0.1063  0.1287 0.0812  0.0115  -0.0106 0.0252  193 THR A O   
1672 C  CB  . THR A  194 ? 0.0926  0.1434 0.0686  -0.0094 -0.0111 0.0133  193 THR A CB  
1673 O  OG1 . THR A  194 ? 0.1003  0.1287 0.0882  -0.0001 -0.0006 0.0108  193 THR A OG1 
1674 C  CG2 . THR A  194 ? 0.1330  0.1524 0.0767  -0.0120 -0.0292 0.0105  193 THR A CG2 
1675 N  N   . TYR A  195 ? 0.0994  0.1217 0.0853  0.0108  -0.0042 0.0178  194 TYR A N   
1676 C  CA  . TYR A  195 ? 0.1135  0.1181 0.0917  0.0128  -0.0025 0.0081  194 TYR A CA  
1677 C  C   . TYR A  195 ? 0.1091  0.1014 0.0967  0.0099  -0.0122 0.0114  194 TYR A C   
1678 O  O   . TYR A  195 ? 0.1100  0.1107 0.0937  0.0234  -0.0017 0.0146  194 TYR A O   
1679 C  CB  . TYR A  195 ? 0.1100  0.1120 0.1036  0.0036  -0.0233 0.0245  194 TYR A CB  
1680 C  CG  . TYR A  195 ? 0.1137  0.1029 0.0952  0.0027  -0.0046 0.0184  194 TYR A CG  
1681 C  CD1 . TYR A  195 ? 0.1074  0.1076 0.1058  -0.0027 -0.0130 0.0317  194 TYR A CD1 
1682 C  CD2 . TYR A  195 ? 0.1076  0.1283 0.1116  -0.0061 -0.0117 0.0263  194 TYR A CD2 
1683 C  CE1 . TYR A  195 ? 0.1203  0.1013 0.1047  -0.0008 0.0117  0.0046  194 TYR A CE1 
1684 C  CE2 . TYR A  195 ? 0.0908  0.1172 0.1030  0.0098  -0.0022 0.0216  194 TYR A CE2 
1685 C  CZ  . TYR A  195 ? 0.0952  0.1126 0.0838  0.0082  -0.0078 0.0260  194 TYR A CZ  
1686 O  OH  . TYR A  195 ? 0.1154  0.1120 0.1003  0.0077  0.0027  0.0069  194 TYR A OH  
1687 N  N   . PRO A  196 ? 0.0979  0.1089 0.0951  0.0193  -0.0035 0.0186  195 PRO A N   
1688 C  CA  . PRO A  196 ? 0.0935  0.1223 0.1071  0.0068  0.0074  0.0036  195 PRO A CA  
1689 C  C   . PRO A  196 ? 0.0971  0.1014 0.1106  0.0058  -0.0074 0.0206  195 PRO A C   
1690 O  O   . PRO A  196 ? 0.1301  0.1065 0.1117  0.0039  -0.0102 0.0157  195 PRO A O   
1691 C  CB  . PRO A  196 ? 0.1216  0.1412 0.1179  0.0298  -0.0115 0.0238  195 PRO A CB  
1692 C  CG  . PRO A  196 ? 0.1252  0.1305 0.1172  0.0201  -0.0009 0.0100  195 PRO A CG  
1693 C  CD  . PRO A  196 ? 0.1084  0.1239 0.1243  0.0337  -0.0140 0.0176  195 PRO A CD  
1694 N  N   . GLY A  197 ? 0.0863  0.1146 0.1014  0.0158  -0.0079 0.0075  196 GLY A N   
1695 C  CA  . GLY A  197 ? 0.1040  0.1102 0.0829  -0.0004 -0.0085 0.0062  196 GLY A CA  
1696 C  C   . GLY A  197 ? 0.1059  0.0961 0.1045  0.0058  0.0119  0.0139  196 GLY A C   
1697 O  O   . GLY A  197 ? 0.1115  0.1163 0.1053  0.0077  -0.0093 0.0084  196 GLY A O   
1698 N  N   . SER A  198 ? 0.1076  0.1178 0.0925  0.0126  -0.0172 0.0000  197 SER A N   
1699 C  CA  . SER A  198 ? 0.1146  0.1040 0.0928  0.0218  -0.0118 0.0000  197 SER A CA  
1700 C  C   . SER A  198 ? 0.1050  0.0882 0.0891  -0.0019 -0.0108 0.0066  197 SER A C   
1701 O  O   . SER A  198 ? 0.1080  0.1023 0.0979  0.0089  0.0065  0.0004  197 SER A O   
1702 C  CB  . SER A  198 ? 0.1045  0.1080 0.1373  -0.0029 0.0189  -0.0027 197 SER A CB  
1703 O  OG  . SER A  198 ? 0.1250  0.0996 0.1111  0.0100  0.0140  -0.0025 197 SER A OG  
1704 N  N   A LEU A  199 ? 0.0996  0.0558 0.0827  -0.0159 -0.0111 0.0094  198 LEU A N   
1705 N  N   B LEU A  199 ? 0.1420  0.1067 0.0767  0.0130  -0.0022 -0.0061 198 LEU A N   
1706 C  CA  A LEU A  199 ? 0.0960  0.1267 0.0759  -0.0131 -0.0069 0.0159  198 LEU A CA  
1707 C  CA  B LEU A  199 ? 0.1116  0.0885 0.0935  0.0176  0.0053  -0.0236 198 LEU A CA  
1708 C  C   A LEU A  199 ? 0.1067  0.0803 0.0800  0.0070  -0.0046 -0.0140 198 LEU A C   
1709 C  C   B LEU A  199 ? 0.1120  0.1125 0.1137  0.0046  -0.0121 -0.0052 198 LEU A C   
1710 O  O   A LEU A  199 ? 0.0919  0.0829 0.1181  0.0057  -0.0361 -0.0119 198 LEU A O   
1711 O  O   B LEU A  199 ? 0.1524  0.1082 0.1081  0.0059  -0.0107 -0.0227 198 LEU A O   
1712 C  CB  A LEU A  199 ? 0.1456  0.1118 0.0820  0.0251  0.0276  -0.0170 198 LEU A CB  
1713 C  CB  B LEU A  199 ? 0.1689  0.1685 0.0874  -0.0289 0.0201  -0.0022 198 LEU A CB  
1714 C  CG  A LEU A  199 ? 0.2271  0.1190 0.0961  -0.0025 0.0578  0.0309  198 LEU A CG  
1715 C  CG  B LEU A  199 ? 0.1833  0.2059 0.1416  -0.0265 0.0606  0.0223  198 LEU A CG  
1716 C  CD1 A LEU A  199 ? 0.2459  0.1588 0.0998  0.0417  0.0684  0.0351  198 LEU A CD1 
1717 C  CD1 B LEU A  199 ? 0.1764  0.1869 0.1664  0.0418  -0.0170 0.0421  198 LEU A CD1 
1718 C  CD2 A LEU A  199 ? 0.1779  0.1050 0.0935  -0.0471 0.0147  0.0250  198 LEU A CD2 
1719 C  CD2 B LEU A  199 ? 0.1714  0.2221 0.1445  0.0427  0.0201  0.0259  198 LEU A CD2 
1720 N  N   . THR A  200 ? 0.1076  0.1047 0.1032  0.0021  -0.0146 0.0005  199 THR A N   
1721 C  CA  . THR A  200 ? 0.1199  0.0994 0.1066  -0.0067 -0.0077 -0.0145 199 THR A CA  
1722 C  C   . THR A  200 ? 0.1319  0.1014 0.1108  0.0089  -0.0389 -0.0001 199 THR A C   
1723 O  O   . THR A  200 ? 0.1206  0.1058 0.1203  0.0055  -0.0159 -0.0165 199 THR A O   
1724 C  CB  . THR A  200 ? 0.1287  0.1099 0.0818  0.0227  -0.0114 0.0073  199 THR A CB  
1725 O  OG1 . THR A  200 ? 0.1225  0.1062 0.0867  0.0046  -0.0117 0.0079  199 THR A OG1 
1726 C  CG2 . THR A  200 ? 0.1412  0.1239 0.0786  -0.0020 -0.0108 0.0099  199 THR A CG2 
1727 N  N   . HIS A  201 ? 0.1588  0.0970 0.0889  0.0033  -0.0157 0.0008  200 HIS A N   
1728 C  CA  . HIS A  201 ? 0.1488  0.1256 0.0803  0.0173  -0.0049 -0.0058 200 HIS A CA  
1729 C  C   . HIS A  201 ? 0.1337  0.1088 0.0908  -0.0008 0.0030  -0.0110 200 HIS A C   
1730 O  O   . HIS A  201 ? 0.1423  0.1240 0.1090  -0.0095 -0.0095 0.0011  200 HIS A O   
1731 C  CB  . HIS A  201 ? 0.1567  0.1216 0.1188  -0.0015 -0.0256 0.0203  200 HIS A CB  
1732 C  CG  . HIS A  201 ? 0.1463  0.1441 0.1549  0.0018  -0.0239 0.0281  200 HIS A CG  
1733 N  ND1 . HIS A  201 ? 0.2045  0.1326 0.1230  -0.0147 -0.0432 0.0127  200 HIS A ND1 
1734 C  CD2 . HIS A  201 ? 0.1714  0.1368 0.2163  0.0029  -0.0302 0.0244  200 HIS A CD2 
1735 C  CE1 . HIS A  201 ? 0.2284  0.1373 0.1738  -0.0103 -0.0001 0.0121  200 HIS A CE1 
1736 N  NE2 . HIS A  201 ? 0.2354  0.1470 0.2626  0.0163  -0.0068 0.0493  200 HIS A NE2 
1737 N  N   . PRO A  202 ? 0.1732  0.1287 0.1005  -0.0021 -0.0011 -0.0212 201 PRO A N   
1738 C  CA  . PRO A  202 ? 0.1826  0.1398 0.1190  -0.0102 0.0326  -0.0403 201 PRO A CA  
1739 C  C   . PRO A  202 ? 0.1883  0.1441 0.1129  -0.0119 0.0000  -0.0272 201 PRO A C   
1740 O  O   . PRO A  202 ? 0.1930  0.1492 0.1057  -0.0005 0.0249  0.0012  201 PRO A O   
1741 C  CB  . PRO A  202 ? 0.2027  0.1675 0.1100  -0.0192 0.0021  -0.0440 201 PRO A CB  
1742 C  CG  . PRO A  202 ? 0.2084  0.1441 0.1351  -0.0334 0.0182  -0.0475 201 PRO A CG  
1743 C  CD  . PRO A  202 ? 0.1914  0.1254 0.1386  -0.0165 -0.0188 -0.0399 201 PRO A CD  
1744 N  N   . PRO A  203 ? 0.1720  0.1887 0.0919  -0.0108 0.0111  0.0033  202 PRO A N   
1745 C  CA  . PRO A  203 ? 0.1635  0.2102 0.1147  0.0049  0.0361  -0.0019 202 PRO A CA  
1746 C  C   . PRO A  203 ? 0.1517  0.1659 0.1156  0.0033  0.0146  -0.0133 202 PRO A C   
1747 O  O   . PRO A  203 ? 0.1578  0.1958 0.1280  0.0057  0.0440  -0.0212 202 PRO A O   
1748 C  CB  . PRO A  203 ? 0.1987  0.2469 0.1416  -0.0281 0.0591  0.0089  202 PRO A CB  
1749 C  CG  . PRO A  203 ? 0.2199  0.2472 0.1621  -0.0569 0.0485  -0.0174 202 PRO A CG  
1750 C  CD  . PRO A  203 ? 0.2070  0.1919 0.1163  -0.0571 0.0218  0.0157  202 PRO A CD  
1751 N  N   . LEU A  204 ? 0.1678  0.1474 0.0873  -0.0057 0.0212  -0.0122 203 LEU A N   
1752 C  CA  . LEU A  204 ? 0.1409  0.1269 0.1021  -0.0194 0.0184  -0.0060 203 LEU A CA  
1753 C  C   . LEU A  204 ? 0.1224  0.1266 0.1081  -0.0005 0.0199  -0.0041 203 LEU A C   
1754 O  O   . LEU A  204 ? 0.1502  0.1330 0.1168  0.0075  0.0190  0.0004  203 LEU A O   
1755 C  CB  . LEU A  204 ? 0.1337  0.1199 0.1488  -0.0013 -0.0009 -0.0185 203 LEU A CB  
1756 C  CG  . LEU A  204 ? 0.1337  0.1132 0.1151  -0.0100 0.0133  -0.0190 203 LEU A CG  
1757 C  CD1 . LEU A  204 ? 0.1764  0.1263 0.2099  0.0148  0.0168  -0.0365 203 LEU A CD1 
1758 C  CD2 . LEU A  204 ? 0.1527  0.1259 0.1229  0.0116  0.0273  -0.0074 203 LEU A CD2 
1759 N  N   . TYR A  205 ? 0.1351  0.1316 0.1179  -0.0089 0.0225  -0.0061 204 TYR A N   
1760 C  CA  . TYR A  205 ? 0.1216  0.1754 0.1016  -0.0186 0.0031  0.0038  204 TYR A CA  
1761 C  C   . TYR A  205 ? 0.1164  0.1198 0.1266  -0.0037 0.0139  0.0050  204 TYR A C   
1762 O  O   . TYR A  205 ? 0.1128  0.1224 0.1216  0.0096  0.0178  0.0053  204 TYR A O   
1763 C  CB  . TYR A  205 ? 0.1520  0.1567 0.1242  -0.0301 0.0253  0.0095  204 TYR A CB  
1764 C  CG  . TYR A  205 ? 0.1588  0.1671 0.1362  -0.0201 0.0199  0.0060  204 TYR A CG  
1765 C  CD1 . TYR A  205 ? 0.3003  0.2084 0.1578  -0.0178 0.0894  -0.0208 204 TYR A CD1 
1766 C  CD2 . TYR A  205 ? 0.1641  0.1844 0.1445  -0.0447 -0.0030 0.0303  204 TYR A CD2 
1767 C  CE1 . TYR A  205 ? 0.3574  0.2249 0.1693  -0.0061 0.1197  0.0113  204 TYR A CE1 
1768 C  CE2 . TYR A  205 ? 0.2023  0.2167 0.1465  -0.0650 0.0291  0.0150  204 TYR A CE2 
1769 C  CZ  . TYR A  205 ? 0.3639  0.1872 0.1362  -0.0614 0.0738  -0.0145 204 TYR A CZ  
1770 O  OH  . TYR A  205 ? 0.3847  0.3309 0.1603  -0.0519 0.0813  -0.0098 204 TYR A OH  
1771 N  N   . GLU A  206 ? 0.1247  0.1368 0.1159  0.0145  0.0001  0.0134  205 GLU A N   
1772 C  CA  . GLU A  206 ? 0.1270  0.1124 0.1169  0.0099  0.0041  0.0121  205 GLU A CA  
1773 C  C   . GLU A  206 ? 0.1059  0.1312 0.1319  0.0073  0.0167  -0.0047 205 GLU A C   
1774 O  O   . GLU A  206 ? 0.1283  0.1268 0.1720  0.0109  -0.0106 0.0100  205 GLU A O   
1775 C  CB  . GLU A  206 ? 0.1199  0.1005 0.1901  0.0107  0.0005  0.0122  205 GLU A CB  
1776 C  CG  . GLU A  206 ? 0.1438  0.1196 0.1617  0.0089  -0.0002 0.0148  205 GLU A CG  
1777 C  CD  . GLU A  206 ? 0.1348  0.1258 0.1754  0.0168  0.0125  0.0002  205 GLU A CD  
1778 O  OE1 . GLU A  206 ? 0.1359  0.1221 0.1571  0.0154  0.0122  0.0080  205 GLU A OE1 
1779 O  OE2 . GLU A  206 ? 0.1351  0.1355 0.2748  0.0229  0.0040  0.0140  205 GLU A OE2 
1780 N  N   . SER A  207 ? 0.1165  0.1037 0.1146  0.0111  0.0188  0.0033  206 SER A N   
1781 C  CA  . SER A  207 ? 0.1125  0.1111 0.1312  0.0107  0.0159  0.0125  206 SER A CA  
1782 C  C   . SER A  207 ? 0.0898  0.1032 0.1265  0.0013  0.0002  0.0095  206 SER A C   
1783 O  O   . SER A  207 ? 0.1102  0.1046 0.1531  0.0036  0.0146  0.0083  206 SER A O   
1784 C  CB  . SER A  207 ? 0.1134  0.1560 0.1115  -0.0098 -0.0003 0.0140  206 SER A CB  
1785 O  OG  . SER A  207 ? 0.1301  0.1294 0.1571  0.0002  0.0104  0.0157  206 SER A OG  
1786 N  N   . VAL A  208 ? 0.1014  0.1161 0.0994  0.0038  0.0151  0.0026  207 VAL A N   
1787 C  CA  . VAL A  208 ? 0.0994  0.1171 0.0961  0.0117  0.0097  -0.0013 207 VAL A CA  
1788 C  C   . VAL A  208 ? 0.1049  0.0977 0.0980  0.0053  0.0063  0.0143  207 VAL A C   
1789 O  O   . VAL A  208 ? 0.1549  0.1067 0.1181  0.0109  0.0175  0.0175  207 VAL A O   
1790 C  CB  . VAL A  208 ? 0.0941  0.1179 0.1074  -0.0019 0.0000  -0.0043 207 VAL A CB  
1791 C  CG1 . VAL A  208 ? 0.1054  0.0986 0.1348  0.0066  0.0002  -0.0085 207 VAL A CG1 
1792 C  CG2 . VAL A  208 ? 0.1269  0.1305 0.0964  -0.0029 -0.0034 0.0107  207 VAL A CG2 
1793 N  N   . THR A  209 ? 0.0926  0.1040 0.1020  0.0043  0.0041  0.0009  208 THR A N   
1794 C  CA  . THR A  209 ? 0.0926  0.1111 0.0874  0.0025  0.0044  0.0046  208 THR A CA  
1795 C  C   . THR A  209 ? 0.0882  0.0996 0.0838  0.0025  -0.0060 0.0188  208 THR A C   
1796 O  O   . THR A  209 ? 0.1028  0.1125 0.1099  0.0117  -0.0024 0.0275  208 THR A O   
1797 C  CB  . THR A  209 ? 0.0891  0.1301 0.1164  -0.0015 -0.0024 0.0026  208 THR A CB  
1798 O  OG1 . THR A  209 ? 0.0880  0.1456 0.1287  0.0060  -0.0130 0.0106  208 THR A OG1 
1799 C  CG2 . THR A  209 ? 0.1216  0.1786 0.0908  -0.0010 -0.0071 0.0006  208 THR A CG2 
1800 N  N   . TRP A  210 ? 0.0838  0.1068 0.0776  -0.0043 -0.0019 0.0105  209 TRP A N   
1801 C  CA  . TRP A  210 ? 0.0759  0.0914 0.0901  0.0027  0.0013  0.0001  209 TRP A CA  
1802 C  C   . TRP A  210 ? 0.0838  0.0961 0.0709  -0.0013 -0.0032 0.0157  209 TRP A C   
1803 O  O   . TRP A  210 ? 0.1058  0.1244 0.0761  0.0097  -0.0236 0.0190  209 TRP A O   
1804 C  CB  . TRP A  210 ? 0.1063  0.0980 0.0847  -0.0115 -0.0089 0.0040  209 TRP A CB  
1805 C  CG  . TRP A  210 ? 0.0847  0.0917 0.0847  -0.0121 -0.0117 0.0113  209 TRP A CG  
1806 C  CD1 . TRP A  210 ? 0.1045  0.1016 0.1023  0.0054  -0.0017 0.0022  209 TRP A CD1 
1807 C  CD2 . TRP A  210 ? 0.0891  0.0973 0.0813  -0.0085 -0.0023 0.0136  209 TRP A CD2 
1808 N  NE1 . TRP A  210 ? 0.1012  0.1021 0.1002  -0.0111 -0.0065 0.0082  209 TRP A NE1 
1809 C  CE2 . TRP A  210 ? 0.0926  0.1203 0.0862  -0.0148 -0.0073 0.0053  209 TRP A CE2 
1810 C  CE3 . TRP A  210 ? 0.0863  0.0996 0.0988  -0.0142 -0.0037 0.0245  209 TRP A CE3 
1811 C  CZ2 . TRP A  210 ? 0.1093  0.1326 0.0900  -0.0194 -0.0139 0.0170  209 TRP A CZ2 
1812 C  CZ3 . TRP A  210 ? 0.1067  0.1077 0.1118  -0.0165 -0.0102 0.0244  209 TRP A CZ3 
1813 C  CH2 . TRP A  210 ? 0.1077  0.1152 0.1171  -0.0222 -0.0127 0.0186  209 TRP A CH2 
1814 N  N   . ILE A  211 ? 0.0827  0.0879 0.0861  0.0061  -0.0027 0.0050  210 ILE A N   
1815 C  CA  . ILE A  211 ? 0.0883  0.1084 0.0979  0.0073  -0.0086 -0.0085 210 ILE A CA  
1816 C  C   . ILE A  211 ? 0.0926  0.1172 0.0619  -0.0001 -0.0122 0.0037  210 ILE A C   
1817 O  O   . ILE A  211 ? 0.0988  0.1384 0.0759  0.0011  -0.0184 0.0233  210 ILE A O   
1818 C  CB  . ILE A  211 ? 0.0935  0.1075 0.0961  -0.0068 -0.0010 -0.0036 210 ILE A CB  
1819 C  CG1 . ILE A  211 ? 0.0865  0.1456 0.1190  -0.0089 -0.0132 0.0039  210 ILE A CG1 
1820 C  CG2 . ILE A  211 ? 0.1344  0.1298 0.0813  0.0108  -0.0135 -0.0080 210 ILE A CG2 
1821 C  CD1 . ILE A  211 ? 0.1319  0.1351 0.1267  -0.0023 -0.0225 0.0163  210 ILE A CD1 
1822 N  N   . ILE A  212 ? 0.0883  0.1084 0.0686  0.0017  0.0055  0.0003  211 ILE A N   
1823 C  CA  . ILE A  212 ? 0.0758  0.1032 0.0867  -0.0027 0.0025  0.0047  211 ILE A CA  
1824 C  C   . ILE A  212 ? 0.0786  0.1242 0.0682  0.0066  -0.0115 -0.0010 211 ILE A C   
1825 O  O   . ILE A  212 ? 0.0867  0.1333 0.0743  0.0113  -0.0059 0.0059  211 ILE A O   
1826 C  CB  . ILE A  212 ? 0.0937  0.1230 0.0969  -0.0003 0.0071  0.0003  211 ILE A CB  
1827 C  CG1 . ILE A  212 ? 0.1294  0.1092 0.0971  -0.0050 0.0201  -0.0029 211 ILE A CG1 
1828 C  CG2 . ILE A  212 ? 0.1125  0.1240 0.1003  -0.0055 0.0033  0.0100  211 ILE A CG2 
1829 C  CD1 . ILE A  212 ? 0.1599  0.1280 0.0707  -0.0114 0.0137  0.0082  211 ILE A CD1 
1830 N  N   . CYS A  213 ? 0.0980  0.1023 0.0776  0.0095  -0.0089 -0.0009 212 CYS A N   
1831 C  CA  . CYS A  213 ? 0.1083  0.0988 0.0696  0.0161  0.0004  0.0058  212 CYS A CA  
1832 C  C   . CYS A  213 ? 0.1003  0.1089 0.0759  0.0139  -0.0234 0.0031  212 CYS A C   
1833 O  O   . CYS A  213 ? 0.1066  0.1333 0.0734  -0.0006 -0.0134 0.0013  212 CYS A O   
1834 C  CB  . CYS A  213 ? 0.1039  0.1189 0.0928  0.0020  -0.0155 0.0187  212 CYS A CB  
1835 S  SG  . CYS A  213 ? 0.1248  0.1256 0.1111  -0.0031 -0.0084 0.0162  212 CYS A SG  
1836 N  N   . LYS A  214 ? 0.1110  0.1190 0.0626  0.0148  -0.0087 0.0102  213 LYS A N   
1837 C  CA  . LYS A  214 ? 0.1298  0.1459 0.0706  0.0071  0.0021  0.0048  213 LYS A CA  
1838 C  C   . LYS A  214 ? 0.1067  0.1448 0.0759  0.0086  -0.0057 0.0089  213 LYS A C   
1839 O  O   . LYS A  214 ? 0.1445  0.1768 0.1544  -0.0190 -0.0011 0.0422  213 LYS A O   
1840 C  CB  . LYS A  214 ? 0.1027  0.2514 0.1007  0.0172  -0.0176 0.0116  213 LYS A CB  
1841 C  CG  . LYS A  214 ? 0.2906  0.4977 0.2102  0.0125  0.0498  0.0036  213 LYS A CG  
1842 C  CD  . LYS A  214 ? 0.3391  0.4770 0.1858  0.0141  0.0006  0.0152  213 LYS A CD  
1843 C  CE  . LYS A  214 ? 0.3380  0.4181 0.1675  -0.0754 0.0131  -0.0719 213 LYS A CE  
1844 N  N   A GLU A  215 ? 0.0933  0.1520 0.0761  0.0288  -0.0125 0.0071  214 GLU A N   
1845 N  N   B GLU A  215 ? 0.1077  0.1405 0.0831  0.0104  -0.0067 0.0047  214 GLU A N   
1846 C  CA  A GLU A  215 ? 0.0910  0.1445 0.0915  0.0268  0.0089  0.0122  214 GLU A CA  
1847 C  CA  B GLU A  215 ? 0.1162  0.1391 0.0679  0.0178  -0.0190 -0.0252 214 GLU A CA  
1848 C  C   A GLU A  215 ? 0.1120  0.1154 0.1204  0.0046  -0.0309 0.0223  214 GLU A C   
1849 C  C   B GLU A  215 ? 0.0935  0.1405 0.0567  0.0124  0.0041  -0.0196 214 GLU A C   
1850 O  O   A GLU A  215 ? 0.1092  0.1768 0.1092  -0.0093 -0.0317 -0.0193 214 GLU A O   
1851 O  O   B GLU A  215 ? 0.1071  0.1384 0.0724  0.0006  0.0117  -0.0055 214 GLU A O   
1852 C  CB  A GLU A  215 ? 0.0908  0.1384 0.1359  0.0331  -0.0303 -0.0067 214 GLU A CB  
1853 C  CB  B GLU A  215 ? 0.1470  0.1258 0.0651  -0.0227 0.0458  -0.0058 214 GLU A CB  
1854 C  CG  A GLU A  215 ? 0.2662  0.2780 0.1624  0.0469  0.0067  -0.0093 214 GLU A CG  
1855 C  CG  B GLU A  215 ? 0.2120  0.1402 0.1225  0.0003  0.0116  -0.0546 214 GLU A CG  
1856 C  CD  A GLU A  215 ? 0.3481  0.2407 0.1305  -0.0291 0.0210  -0.0207 214 GLU A CD  
1857 C  CD  B GLU A  215 ? 0.2303  0.3607 0.1250  -0.0725 0.0275  -0.0659 214 GLU A CD  
1858 O  OE1 A GLU A  215 ? 0.1822  0.1772 0.0829  -0.0271 0.0162  -0.0063 214 GLU A OE1 
1859 O  OE1 B GLU A  215 ? 0.2242  0.4688 0.1725  -0.0675 0.0050  -0.0919 214 GLU A OE1 
1860 O  OE2 A GLU A  215 ? 0.4963  0.3021 0.1459  0.0212  0.0472  -0.0703 214 GLU A OE2 
1861 O  OE2 B GLU A  215 ? 0.2411  0.5259 0.1941  -0.1121 -0.0225 0.0354  214 GLU A OE2 
1862 N  N   . SER A  216 ? 0.0856  0.1477 0.1031  0.0117  -0.0225 0.0139  215 SER A N   
1863 C  CA  . SER A  216 ? 0.0993  0.1287 0.0976  0.0087  -0.0285 0.0221  215 SER A CA  
1864 C  C   . SER A  216 ? 0.0967  0.1190 0.0926  0.0029  -0.0082 -0.0153 215 SER A C   
1865 O  O   . SER A  216 ? 0.1326  0.1441 0.1044  0.0258  -0.0308 -0.0097 215 SER A O   
1866 C  CB  . SER A  216 ? 0.1151  0.1610 0.1294  -0.0223 0.0149  0.0118  215 SER A CB  
1867 O  OG  . SER A  216 ? 0.1294  0.2274 0.1434  -0.0322 0.0174  -0.0053 215 SER A OG  
1868 N  N   . ILE A  217 ? 0.0996  0.1298 0.0773  0.0048  -0.0201 0.0048  216 ILE A N   
1869 C  CA  . ILE A  217 ? 0.0932  0.1154 0.1068  0.0098  -0.0276 -0.0013 216 ILE A CA  
1870 C  C   . ILE A  217 ? 0.0962  0.1066 0.0899  0.0064  -0.0098 -0.0150 216 ILE A C   
1871 O  O   . ILE A  217 ? 0.0980  0.1089 0.1316  0.0018  -0.0197 -0.0165 216 ILE A O   
1872 C  CB  . ILE A  217 ? 0.1092  0.0993 0.1030  0.0029  -0.0205 -0.0127 216 ILE A CB  
1873 C  CG1 . ILE A  217 ? 0.1037  0.1197 0.1049  0.0006  -0.0005 -0.0099 216 ILE A CG1 
1874 C  CG2 . ILE A  217 ? 0.0916  0.1412 0.1111  0.0004  -0.0216 -0.0299 216 ILE A CG2 
1875 C  CD1 . ILE A  217 ? 0.1319  0.1225 0.1093  -0.0175 -0.0122 -0.0015 216 ILE A CD1 
1876 N  N   A SER A  218 ? 0.0846  0.1323 0.0856  0.0192  -0.0036 -0.0253 217 SER A N   
1877 N  N   B SER A  218 ? 0.0820  0.1373 0.0971  0.0075  -0.0278 0.0136  217 SER A N   
1878 C  CA  A SER A  218 ? 0.0980  0.1657 0.0706  0.0096  -0.0285 -0.0341 217 SER A CA  
1879 C  CA  B SER A  218 ? 0.0872  0.1049 0.0933  0.0013  -0.0220 0.0044  217 SER A CA  
1880 C  C   A SER A  218 ? 0.0977  0.1093 0.0812  0.0108  -0.0214 0.0000  217 SER A C   
1881 C  C   B SER A  218 ? 0.0949  0.1111 0.1029  0.0115  -0.0268 -0.0016 217 SER A C   
1882 O  O   A SER A  218 ? 0.0891  0.1073 0.0962  0.0008  -0.0185 -0.0025 217 SER A O   
1883 O  O   B SER A  218 ? 0.1007  0.1155 0.0962  0.0015  -0.0187 -0.0075 217 SER A O   
1884 C  CB  A SER A  218 ? 0.1084  0.1797 0.0969  0.0285  -0.0160 -0.0042 217 SER A CB  
1885 C  CB  B SER A  218 ? 0.0861  0.1287 0.1366  0.0024  -0.0125 -0.0132 217 SER A CB  
1886 O  OG  A SER A  218 ? 0.1720  0.1890 0.1204  0.0621  0.0256  0.0073  217 SER A OG  
1887 O  OG  B SER A  218 ? 0.0863  0.1366 0.1276  -0.0030 -0.0062 -0.0111 217 SER A OG  
1888 N  N   . VAL A  219 ? 0.0838  0.1216 0.0900  -0.0012 -0.0207 -0.0073 218 VAL A N   
1889 C  CA  . VAL A  219 ? 0.0803  0.1212 0.0803  -0.0140 -0.0207 -0.0030 218 VAL A CA  
1890 C  C   . VAL A  219 ? 0.0892  0.1127 0.0862  0.0003  -0.0167 0.0000  218 VAL A C   
1891 O  O   . VAL A  219 ? 0.0919  0.1323 0.1076  -0.0111 -0.0044 0.0148  218 VAL A O   
1892 C  CB  . VAL A  219 ? 0.0951  0.1214 0.0776  0.0075  -0.0018 0.0094  218 VAL A CB  
1893 C  CG1 . VAL A  219 ? 0.1137  0.1111 0.0995  0.0065  -0.0113 0.0058  218 VAL A CG1 
1894 C  CG2 . VAL A  219 ? 0.0996  0.1434 0.0809  0.0124  -0.0068 -0.0024 218 VAL A CG2 
1895 N  N   . SER A  220 ? 0.0750  0.1405 0.0871  0.0046  -0.0189 -0.0157 219 SER A N   
1896 C  CA  . SER A  220 ? 0.0646  0.1380 0.1055  -0.0020 -0.0047 -0.0134 219 SER A CA  
1897 C  C   . SER A  220 ? 0.0813  0.1159 0.0944  0.0005  -0.0043 0.0100  219 SER A C   
1898 O  O   . SER A  220 ? 0.0847  0.1333 0.0985  0.0013  -0.0109 0.0003  219 SER A O   
1899 C  CB  . SER A  220 ? 0.0882  0.1682 0.0792  0.0257  -0.0183 -0.0053 219 SER A CB  
1900 O  OG  . SER A  220 ? 0.1004  0.1465 0.0973  0.0083  -0.0050 -0.0004 219 SER A OG  
1901 N  N   A SER A  221 ? 0.0942  0.1270 0.1084  -0.0106 -0.0133 0.0004  220 SER A N   
1902 N  N   B SER A  221 ? 0.1049  0.1244 0.0996  -0.0151 -0.0088 0.0006  220 SER A N   
1903 C  CA  A SER A  221 ? 0.1037  0.1434 0.0864  -0.0206 -0.0080 -0.0104 220 SER A CA  
1904 C  CA  B SER A  221 ? 0.1199  0.1499 0.0863  -0.0316 -0.0100 -0.0122 220 SER A CA  
1905 C  C   A SER A  221 ? 0.0838  0.1386 0.0829  0.0015  -0.0122 -0.0198 220 SER A C   
1906 C  C   B SER A  221 ? 0.0637  0.1386 0.0961  -0.0044 -0.0100 -0.0086 220 SER A C   
1907 O  O   A SER A  221 ? 0.0829  0.1412 0.0970  0.0151  -0.0027 -0.0159 220 SER A O   
1908 O  O   B SER A  221 ? 0.1067  0.1351 0.0934  -0.0162 -0.0023 -0.0072 220 SER A O   
1909 C  CB  A SER A  221 ? 0.0873  0.1289 0.1225  -0.0113 -0.0130 -0.0203 220 SER A CB  
1910 C  CB  B SER A  221 ? 0.1535  0.1887 0.1040  -0.0783 -0.0341 0.0304  220 SER A CB  
1911 O  OG  A SER A  221 ? 0.1412  0.0970 0.1172  -0.0292 -0.0069 -0.0073 220 SER A OG  
1912 O  OG  B SER A  221 ? 0.1337  0.1711 0.1289  -0.0103 -0.0319 0.0313  220 SER A OG  
1913 N  N   . GLU A  222 ? 0.0752  0.1538 0.0973  0.0100  -0.0113 -0.0019 221 GLU A N   
1914 C  CA  . GLU A  222 ? 0.0867  0.1668 0.0846  0.0135  0.0008  0.0062  221 GLU A CA  
1915 C  C   . GLU A  222 ? 0.0864  0.1316 0.0908  0.0078  -0.0104 -0.0149 221 GLU A C   
1916 O  O   . GLU A  222 ? 0.0960  0.1477 0.0864  0.0104  -0.0039 -0.0229 221 GLU A O   
1917 C  CB  . GLU A  222 ? 0.0820  0.1621 0.1162  0.0137  0.0055  0.0027  221 GLU A CB  
1918 C  CG  . GLU A  222 ? 0.0926  0.1955 0.1032  -0.0016 0.0022  0.0096  221 GLU A CG  
1919 C  CD  . GLU A  222 ? 0.0822  0.1811 0.1162  -0.0010 -0.0031 -0.0111 221 GLU A CD  
1920 O  OE1 . GLU A  222 ? 0.1120  0.1932 0.1109  0.0098  -0.0003 -0.0073 221 GLU A OE1 
1921 O  OE2 . GLU A  222 ? 0.1099  0.2034 0.1003  -0.0035 0.0149  -0.0100 221 GLU A OE2 
1922 N  N   . GLN A  223 ? 0.0817  0.1263 0.0827  0.0093  -0.0183 -0.0063 222 GLN A N   
1923 C  CA  . GLN A  223 ? 0.0765  0.1301 0.0908  0.0087  -0.0030 -0.0132 222 GLN A CA  
1924 C  C   . GLN A  223 ? 0.0716  0.1195 0.0926  0.0134  -0.0150 -0.0096 222 GLN A C   
1925 O  O   . GLN A  223 ? 0.0917  0.1556 0.0768  -0.0031 -0.0048 -0.0190 222 GLN A O   
1926 C  CB  . GLN A  223 ? 0.0969  0.1234 0.0801  0.0139  -0.0170 -0.0252 222 GLN A CB  
1927 C  CG  . GLN A  223 ? 0.1137  0.1194 0.0881  0.0050  -0.0276 -0.0060 222 GLN A CG  
1928 C  CD  . GLN A  223 ? 0.1076  0.1058 0.0785  0.0135  -0.0051 0.0046  222 GLN A CD  
1929 O  OE1 . GLN A  223 ? 0.1039  0.1168 0.0883  0.0050  -0.0201 -0.0022 222 GLN A OE1 
1930 N  NE2 . GLN A  223 ? 0.1326  0.1102 0.1081  0.0086  -0.0192 0.0094  222 GLN A NE2 
1931 N  N   . LEU A  224 ? 0.0892  0.1252 0.0976  0.0098  -0.0313 -0.0137 223 LEU A N   
1932 C  CA  . LEU A  224 ? 0.0943  0.1146 0.1054  0.0132  -0.0170 -0.0215 223 LEU A CA  
1933 C  C   . LEU A  224 ? 0.0944  0.1199 0.1084  -0.0046 -0.0193 -0.0201 223 LEU A C   
1934 O  O   . LEU A  224 ? 0.1014  0.1355 0.1012  0.0128  -0.0049 -0.0143 223 LEU A O   
1935 C  CB  . LEU A  224 ? 0.1194  0.1316 0.1083  0.0063  -0.0268 -0.0212 223 LEU A CB  
1936 C  CG  . LEU A  224 ? 0.1225  0.1664 0.1120  0.0232  -0.0458 -0.0057 223 LEU A CG  
1937 C  CD1 . LEU A  224 ? 0.2924  0.1456 0.1287  0.0173  -0.0728 -0.0080 223 LEU A CD1 
1938 C  CD2 . LEU A  224 ? 0.1341  0.3086 0.1456  0.0699  -0.0713 -0.1022 223 LEU A CD2 
1939 N  N   . ALA A  225 ? 0.0910  0.1351 0.0970  -0.0055 -0.0331 -0.0043 224 ALA A N   
1940 C  CA  . ALA A  225 ? 0.0955  0.1373 0.0879  -0.0060 -0.0168 -0.0110 224 ALA A CA  
1941 C  C   . ALA A  225 ? 0.0905  0.1256 0.0970  0.0078  -0.0192 -0.0136 224 ALA A C   
1942 O  O   . ALA A  225 ? 0.1155  0.1430 0.0919  0.0050  -0.0032 -0.0252 224 ALA A O   
1943 C  CB  . ALA A  225 ? 0.0788  0.2117 0.1181  -0.0122 -0.0300 -0.0326 224 ALA A CB  
1944 N  N   . GLN A  226 ? 0.0980  0.1138 0.1011  0.0089  -0.0098 -0.0051 225 GLN A N   
1945 C  CA  . GLN A  226 ? 0.1208  0.1312 0.0926  0.0098  -0.0159 -0.0173 225 GLN A CA  
1946 C  C   . GLN A  226 ? 0.1120  0.1312 0.0870  0.0027  -0.0055 -0.0197 225 GLN A C   
1947 O  O   . GLN A  226 ? 0.1190  0.1459 0.0926  0.0091  -0.0022 -0.0074 225 GLN A O   
1948 C  CB  . GLN A  226 ? 0.1164  0.1366 0.1264  0.0212  -0.0242 -0.0173 225 GLN A CB  
1949 C  CG  . GLN A  226 ? 0.1412  0.1380 0.1355  0.0159  -0.0121 -0.0206 225 GLN A CG  
1950 C  CD  . GLN A  226 ? 0.1212  0.1639 0.1159  0.0223  -0.0258 -0.0234 225 GLN A CD  
1951 O  OE1 . GLN A  226 ? 0.1463  0.1524 0.1624  0.0084  -0.0166 -0.0389 225 GLN A OE1 
1952 N  NE2 . GLN A  226 ? 0.1718  0.1720 0.1718  0.0103  -0.0351 0.0032  225 GLN A NE2 
1953 N  N   . PHE A  227 ? 0.0891  0.1368 0.1132  0.0041  -0.0234 -0.0141 226 PHE A N   
1954 C  CA  . PHE A  227 ? 0.1032  0.1416 0.0908  0.0186  -0.0221 -0.0148 226 PHE A CA  
1955 C  C   . PHE A  227 ? 0.1011  0.1199 0.1111  0.0145  0.0001  -0.0006 226 PHE A C   
1956 O  O   . PHE A  227 ? 0.0900  0.1650 0.0995  0.0070  -0.0085 -0.0148 226 PHE A O   
1957 C  CB  . PHE A  227 ? 0.1047  0.1412 0.0989  0.0055  -0.0218 -0.0019 226 PHE A CB  
1958 C  CG  . PHE A  227 ? 0.0801  0.1617 0.1032  0.0023  0.0003  -0.0188 226 PHE A CG  
1959 C  CD1 . PHE A  227 ? 0.1465  0.1833 0.1488  -0.0623 0.0143  -0.0198 226 PHE A CD1 
1960 C  CD2 . PHE A  227 ? 0.1247  0.2256 0.1030  0.0271  -0.0315 -0.0377 226 PHE A CD2 
1961 C  CE1 . PHE A  227 ? 0.1384  0.2120 0.1452  -0.0433 0.0085  -0.0390 226 PHE A CE1 
1962 C  CE2 . PHE A  227 ? 0.1456  0.2643 0.1152  0.0329  -0.0447 -0.0569 226 PHE A CE2 
1963 C  CZ  . PHE A  227 ? 0.1348  0.2328 0.1641  -0.0128 -0.0398 -0.0210 226 PHE A CZ  
1964 N  N   . ARG A  228 ? 0.0882  0.1212 0.1097  0.0058  0.0010  -0.0017 227 ARG A N   
1965 C  CA  . ARG A  228 ? 0.1224  0.1326 0.1239  -0.0022 0.0011  -0.0218 227 ARG A CA  
1966 C  C   . ARG A  228 ? 0.1162  0.1768 0.1067  -0.0110 0.0120  -0.0395 227 ARG A C   
1967 O  O   . ARG A  228 ? 0.1847  0.1847 0.1448  -0.0325 0.0379  -0.0641 227 ARG A O   
1968 C  CB  . ARG A  228 ? 0.1064  0.1488 0.1567  -0.0042 0.0079  0.0044  227 ARG A CB  
1969 C  CG  . ARG A  228 ? 0.0979  0.1556 0.1720  0.0065  -0.0269 0.0236  227 ARG A CG  
1970 C  CD  . ARG A  228 ? 0.1624  0.2041 0.2364  -0.0267 -0.0040 0.0847  227 ARG A CD  
1971 N  NE  . ARG A  228 ? 0.1483  0.2178 0.2802  -0.0285 -0.0281 0.1301  227 ARG A NE  
1972 C  CZ  . ARG A  228 ? 0.1729  0.1599 0.2188  -0.0158 -0.1054 0.0159  227 ARG A CZ  
1973 N  NH1 . ARG A  228 ? 0.2213  0.1384 0.2194  0.0209  -0.1031 -0.0018 227 ARG A NH1 
1974 N  NH2 . ARG A  228 ? 0.2242  0.1659 0.2709  -0.0678 -0.1355 0.0849  227 ARG A NH2 
1975 N  N   . SER A  229 ? 0.0943  0.1738 0.1007  -0.0100 -0.0054 -0.0150 228 SER A N   
1976 C  CA  . SER A  229 ? 0.1058  0.2246 0.0856  -0.0120 -0.0172 -0.0287 228 SER A CA  
1977 C  C   . SER A  229 ? 0.1223  0.2072 0.0716  -0.0201 -0.0060 -0.0361 228 SER A C   
1978 O  O   . SER A  229 ? 0.1145  0.2440 0.0826  -0.0068 -0.0083 -0.0306 228 SER A O   
1979 C  CB  . SER A  229 ? 0.1172  0.3208 0.1289  0.0519  -0.0324 0.0231  228 SER A CB  
1980 O  OG  . SER A  229 ? 0.2260  0.3413 0.1585  0.0572  -0.0138 -0.0278 228 SER A OG  
1981 N  N   . LEU A  230 ? 0.0996  0.1506 0.1047  -0.0078 -0.0029 -0.0297 229 LEU A N   
1982 C  CA  . LEU A  230 ? 0.0995  0.1477 0.0900  -0.0013 0.0041  -0.0244 229 LEU A CA  
1983 C  C   . LEU A  230 ? 0.1111  0.1355 0.1027  0.0053  0.0033  -0.0102 229 LEU A C   
1984 O  O   . LEU A  230 ? 0.1937  0.1416 0.0961  -0.0097 0.0070  -0.0174 229 LEU A O   
1985 C  CB  . LEU A  230 ? 0.1283  0.1646 0.0933  -0.0170 -0.0186 -0.0162 229 LEU A CB  
1986 C  CG  . LEU A  230 ? 0.1617  0.1835 0.1223  -0.0085 -0.0219 -0.0109 229 LEU A CG  
1987 C  CD1 . LEU A  230 ? 0.1599  0.2495 0.1772  -0.0308 -0.0466 -0.0417 229 LEU A CD1 
1988 C  CD2 . LEU A  230 ? 0.1835  0.1678 0.1786  -0.0552 -0.0350 0.0008  229 LEU A CD2 
1989 N  N   . LEU A  231 ? 0.0979  0.1650 0.0849  0.0005  -0.0052 -0.0198 230 LEU A N   
1990 C  CA  . LEU A  231 ? 0.0961  0.1872 0.0964  0.0099  -0.0289 -0.0505 230 LEU A CA  
1991 C  C   . LEU A  231 ? 0.0879  0.1653 0.0858  -0.0064 -0.0102 -0.0312 230 LEU A C   
1992 O  O   . LEU A  231 ? 0.1016  0.1470 0.1190  -0.0109 -0.0138 -0.0198 230 LEU A O   
1993 C  CB  . LEU A  231 ? 0.0908  0.1958 0.0919  0.0089  -0.0182 -0.0302 230 LEU A CB  
1994 C  CG  . LEU A  231 ? 0.0941  0.1738 0.1108  0.0115  -0.0119 -0.0159 230 LEU A CG  
1995 C  CD1 . LEU A  231 ? 0.0890  0.2511 0.1234  0.0059  -0.0231 0.0104  230 LEU A CD1 
1996 C  CD2 . LEU A  231 ? 0.1251  0.1775 0.1319  -0.0136 -0.0141 -0.0071 230 LEU A CD2 
1997 N  N   . SER A  232 ? 0.1125  0.1438 0.1120  0.0168  -0.0194 -0.0263 231 SER A N   
1998 C  CA  . SER A  232 ? 0.1014  0.1628 0.1330  0.0068  -0.0171 -0.0292 231 SER A CA  
1999 C  C   . SER A  232 ? 0.1067  0.1556 0.1264  0.0077  -0.0163 -0.0138 231 SER A C   
2000 O  O   . SER A  232 ? 0.1084  0.2037 0.1743  0.0188  -0.0066 -0.0303 231 SER A O   
2001 C  CB  . SER A  232 ? 0.1280  0.1409 0.1829  -0.0044 -0.0450 -0.0148 231 SER A CB  
2002 O  OG  . SER A  232 ? 0.1368  0.1650 0.1872  -0.0031 -0.0250 -0.0283 231 SER A OG  
2003 N  N   . ASN A  233 ? 0.1249  0.1624 0.1055  0.0140  -0.0240 -0.0212 232 ASN A N   
2004 C  CA  . ASN A  233 ? 0.1348  0.1757 0.1098  -0.0001 -0.0070 -0.0297 232 ASN A CA  
2005 C  C   . ASN A  233 ? 0.0908  0.1865 0.1199  0.0205  -0.0030 -0.0256 232 ASN A C   
2006 O  O   . ASN A  233 ? 0.1040  0.1732 0.1221  0.0027  -0.0107 -0.0210 232 ASN A O   
2007 C  CB  . ASN A  233 ? 0.1287  0.2027 0.1053  -0.0037 0.0031  -0.0600 232 ASN A CB  
2008 C  CG  . ASN A  233 ? 0.1053  0.1826 0.1111  0.0016  0.0065  -0.0591 232 ASN A CG  
2009 O  OD1 . ASN A  233 ? 0.0973  0.1829 0.1111  -0.0077 -0.0006 -0.0460 232 ASN A OD1 
2010 N  ND2 . ASN A  233 ? 0.1298  0.1984 0.1049  -0.0074 -0.0274 -0.0322 232 ASN A ND2 
2011 N  N   A VAL A  234 ? 0.1016  0.2099 0.1144  0.0070  0.0095  -0.0100 233 VAL A N   
2012 N  N   B VAL A  234 ? 0.0944  0.2125 0.1171  0.0024  0.0039  -0.0150 233 VAL A N   
2013 C  CA  A VAL A  234 ? 0.0977  0.1969 0.0937  0.0089  0.0134  -0.0172 233 VAL A CA  
2014 C  CA  B VAL A  234 ? 0.0952  0.2064 0.1220  0.0049  0.0088  -0.0062 233 VAL A CA  
2015 C  C   A VAL A  234 ? 0.1064  0.1926 0.0847  -0.0029 -0.0043 -0.0340 233 VAL A C   
2016 C  C   B VAL A  234 ? 0.1102  0.1980 0.0953  -0.0088 -0.0107 -0.0166 233 VAL A C   
2017 O  O   A VAL A  234 ? 0.1071  0.2152 0.1005  -0.0046 -0.0058 -0.0262 233 VAL A O   
2018 O  O   B VAL A  234 ? 0.0928  0.2188 0.1323  0.0018  0.0030  -0.0243 233 VAL A O   
2019 C  CB  A VAL A  234 ? 0.1005  0.2931 0.0977  -0.0001 0.0116  -0.0234 233 VAL A CB  
2020 C  CB  B VAL A  234 ? 0.1224  0.3402 0.1729  0.0480  0.0480  0.0397  233 VAL A CB  
2021 C  CG1 A VAL A  234 ? 0.0706  0.4638 0.0900  0.0120  0.0365  0.0100  233 VAL A CG1 
2022 C  CG1 B VAL A  234 ? 0.2734  0.3028 0.2375  -0.0038 0.1033  0.0207  233 VAL A CG1 
2023 C  CG2 A VAL A  234 ? 0.1023  0.2572 0.0759  0.0515  0.0269  -0.0531 233 VAL A CG2 
2024 C  CG2 B VAL A  234 ? 0.1527  0.2576 0.2400  0.0589  -0.0298 -0.0825 233 VAL A CG2 
2025 N  N   . GLU A  235 ? 0.1127  0.1951 0.1076  0.0108  0.0150  -0.0275 234 GLU A N   
2026 C  CA  . GLU A  235 ? 0.1239  0.2163 0.0928  0.0185  0.0027  -0.0271 234 GLU A CA  
2027 C  C   . GLU A  235 ? 0.1164  0.2321 0.1098  0.0133  0.0102  -0.0458 234 GLU A C   
2028 O  O   . GLU A  235 ? 0.1373  0.2619 0.1067  0.0100  0.0200  -0.0421 234 GLU A O   
2029 C  CB  . GLU A  235 ? 0.1427  0.2170 0.1084  -0.0051 -0.0175 -0.0018 234 GLU A CB  
2030 C  CG  . GLU A  235 ? 0.1502  0.2339 0.1391  0.0098  -0.0243 -0.0206 234 GLU A CG  
2031 C  CD  . GLU A  235 ? 0.2418  0.2676 0.1298  0.0289  0.0124  0.0022  234 GLU A CD  
2032 O  OE1 . GLU A  235 ? 0.2490  0.2362 0.1434  0.0035  -0.0104 -0.0046 234 GLU A OE1 
2033 O  OE2 . GLU A  235 ? 0.6782  0.3153 0.1571  -0.0255 -0.0231 0.0151  234 GLU A OE2 
2034 N  N   . GLY A  236 ? 0.1212  0.2314 0.0969  0.0141  -0.0050 -0.0262 235 GLY A N   
2035 C  CA  . GLY A  236 ? 0.1351  0.2561 0.1231  -0.0006 -0.0325 -0.0392 235 GLY A CA  
2036 C  C   . GLY A  236 ? 0.1958  0.2529 0.1164  -0.0069 -0.0303 -0.0549 235 GLY A C   
2037 O  O   . GLY A  236 ? 0.3582  0.2770 0.1944  -0.0807 -0.1310 0.0155  235 GLY A O   
2038 N  N   . ASP A  237 ? 0.1592  0.2350 0.1172  0.0132  0.0055  -0.0331 236 ASP A N   
2039 C  CA  . ASP A  237 ? 0.1826  0.2694 0.1124  0.0003  -0.0281 -0.0629 236 ASP A CA  
2040 C  C   . ASP A  237 ? 0.1775  0.2160 0.1137  0.0151  -0.0179 -0.0432 236 ASP A C   
2041 O  O   . ASP A  237 ? 0.1470  0.2479 0.1307  0.0087  -0.0138 -0.0438 236 ASP A O   
2042 C  CB  . ASP A  237 ? 0.1685  0.2490 0.1452  0.0305  -0.0120 -0.0564 236 ASP A CB  
2043 C  CG  . ASP A  237 ? 0.2187  0.2755 0.1588  0.0541  -0.0031 -0.0517 236 ASP A CG  
2044 O  OD1 . ASP A  237 ? 0.2400  0.4113 0.1639  0.0679  0.0006  -0.0586 236 ASP A OD1 
2045 O  OD2 . ASP A  237 ? 0.2205  0.3528 0.1969  0.0560  -0.0054 -0.0834 236 ASP A OD2 
2046 N  N   . ASN A  238 ? 0.1829  0.2460 0.1199  -0.0242 -0.0187 -0.0446 237 ASN A N   
2047 C  CA  . ASN A  238 ? 0.1941  0.2494 0.1220  -0.0694 -0.0287 -0.0353 237 ASN A CA  
2048 C  C   . ASN A  238 ? 0.1531  0.2310 0.1119  -0.0433 -0.0190 -0.0427 237 ASN A C   
2049 O  O   . ASN A  238 ? 0.1678  0.2260 0.1234  -0.0159 -0.0117 -0.0685 237 ASN A O   
2050 C  CB  . ASN A  238 ? 0.2257  0.2404 0.1908  -0.0675 0.0102  -0.0881 237 ASN A CB  
2051 C  CG  . ASN A  238 ? 0.2066  0.2996 0.1815  0.0023  -0.0155 -0.0080 237 ASN A CG  
2052 O  OD1 . ASN A  238 ? 0.1757  0.3980 0.3632  0.0632  0.0061  0.0967  237 ASN A OD1 
2053 N  ND2 . ASN A  238 ? 0.2608  0.2806 0.2375  0.0141  -0.0581 0.0058  237 ASN A ND2 
2054 N  N   . ALA A  239 ? 0.1483  0.2565 0.0958  -0.0311 -0.0156 -0.0328 238 ALA A N   
2055 C  CA  . ALA A  239 ? 0.1520  0.2691 0.0891  -0.0199 -0.0390 -0.0337 238 ALA A CA  
2056 C  C   . ALA A  239 ? 0.1703  0.2766 0.1055  -0.0727 -0.0200 -0.0027 238 ALA A C   
2057 O  O   . ALA A  239 ? 0.3046  0.5542 0.1736  -0.2618 -0.1249 0.1226  238 ALA A O   
2058 C  CB  . ALA A  239 ? 0.1111  0.3934 0.1653  0.0242  -0.0151 -0.0950 238 ALA A CB  
2059 N  N   . VAL A  240 ? 0.1693  0.1894 0.0917  -0.0126 -0.0245 -0.0454 239 VAL A N   
2060 C  CA  . VAL A  240 ? 0.1865  0.1932 0.1005  -0.0120 -0.0261 -0.0403 239 VAL A CA  
2061 C  C   . VAL A  240 ? 0.1944  0.1377 0.1199  -0.0278 -0.0147 -0.0204 239 VAL A C   
2062 O  O   . VAL A  240 ? 0.1969  0.1786 0.1247  -0.0568 -0.0121 -0.0272 239 VAL A O   
2063 C  CB  . VAL A  240 ? 0.2357  0.1897 0.1289  -0.0038 -0.0003 -0.0611 239 VAL A CB  
2064 C  CG1 . VAL A  240 ? 0.3434  0.1700 0.1628  0.0100  -0.0493 -0.0125 239 VAL A CG1 
2065 C  CG2 . VAL A  240 ? 0.2910  0.2125 0.1386  -0.0022 -0.0265 -0.0453 239 VAL A CG2 
2066 N  N   . PRO A  241 ? 0.1445  0.1768 0.1198  -0.0212 -0.0319 -0.0277 240 PRO A N   
2067 C  CA  . PRO A  241 ? 0.1628  0.1833 0.1075  0.0212  -0.0436 -0.0377 240 PRO A CA  
2068 C  C   . PRO A  241 ? 0.1757  0.1380 0.0962  -0.0035 -0.0279 -0.0165 240 PRO A C   
2069 O  O   . PRO A  241 ? 0.1738  0.1459 0.1190  -0.0024 -0.0294 -0.0293 240 PRO A O   
2070 C  CB  . PRO A  241 ? 0.1738  0.2551 0.1384  0.0081  -0.0322 -0.0674 240 PRO A CB  
2071 C  CG  . PRO A  241 ? 0.1592  0.3689 0.2023  0.0410  -0.0281 -0.1254 240 PRO A CG  
2072 C  CD  . PRO A  241 ? 0.1359  0.2723 0.1592  -0.0190 -0.0217 -0.0564 240 PRO A CD  
2073 N  N   . MET A  242 ? 0.1481  0.1535 0.1049  -0.0211 -0.0141 -0.0370 241 MET A N   
2074 C  CA  . MET A  242 ? 0.1287  0.1531 0.1326  -0.0252 -0.0388 -0.0300 241 MET A CA  
2075 C  C   . MET A  242 ? 0.1481  0.1635 0.1129  0.0171  -0.0476 -0.0269 241 MET A C   
2076 O  O   . MET A  242 ? 0.1520  0.1980 0.1298  0.0406  -0.0486 -0.0539 241 MET A O   
2077 C  CB  . MET A  242 ? 0.1362  0.1908 0.2529  -0.0434 0.0005  -0.0864 241 MET A CB  
2078 C  CG  . MET A  242 ? 0.1610  0.2117 0.2651  -0.0424 0.0352  -0.0126 241 MET A CG  
2079 S  SD  . MET A  242 ? 0.1197  0.1912 0.1966  -0.0046 -0.0117 0.0366  241 MET A SD  
2080 C  CE  . MET A  242 ? 0.1333  0.1829 0.1786  -0.0130 -0.0055 0.0279  241 MET A CE  
2081 N  N   A GLN A  243 ? 0.1348  0.1678 0.1220  0.0038  -0.0304 -0.0254 242 GLN A N   
2082 N  N   B GLN A  243 ? 0.1316  0.1711 0.1323  0.0000  -0.0348 -0.0222 242 GLN A N   
2083 C  CA  A GLN A  243 ? 0.1463  0.2099 0.1144  -0.0178 -0.0403 -0.0220 242 GLN A CA  
2084 C  CA  B GLN A  243 ? 0.1298  0.1984 0.1380  -0.0034 -0.0346 -0.0218 242 GLN A CA  
2085 C  C   A GLN A  243 ? 0.0914  0.2081 0.1258  0.0074  -0.0347 -0.0433 242 GLN A C   
2086 C  C   B GLN A  243 ? 0.0926  0.2048 0.1305  0.0082  -0.0251 -0.0462 242 GLN A C   
2087 O  O   A GLN A  243 ? 0.1305  0.1822 0.1341  0.0115  -0.0106 -0.0183 242 GLN A O   
2088 O  O   B GLN A  243 ? 0.1355  0.1908 0.1230  0.0077  -0.0162 -0.0262 242 GLN A O   
2089 C  CB  A GLN A  243 ? 0.2260  0.2375 0.1049  -0.0574 -0.0855 -0.0247 242 GLN A CB  
2090 C  CB  B GLN A  243 ? 0.1955  0.2224 0.1966  -0.0543 -0.0758 -0.0019 242 GLN A CB  
2091 C  CG  A GLN A  243 ? 0.2321  0.3226 0.0944  -0.0972 -0.0856 0.0184  242 GLN A CG  
2092 C  CG  B GLN A  243 ? 0.1743  0.1800 0.2921  -0.0113 0.0143  -0.0634 242 GLN A CG  
2093 C  CD  A GLN A  243 ? 0.1535  0.4034 0.2579  -0.1577 -0.0512 -0.0161 242 GLN A CD  
2094 C  CD  B GLN A  243 ? 0.2436  0.2005 0.2285  0.0436  -0.1123 -0.0776 242 GLN A CD  
2095 O  OE1 A GLN A  243 ? 0.3488  0.5393 0.3661  -0.3040 0.0084  -0.2084 242 GLN A OE1 
2096 O  OE1 B GLN A  243 ? 0.2260  0.2720 0.1980  0.0680  -0.0637 -0.0925 242 GLN A OE1 
2097 N  NE2 A GLN A  243 ? 0.2971  0.3344 0.3240  -0.1388 -0.1619 0.0787  242 GLN A NE2 
2098 N  NE2 B GLN A  243 ? 0.2310  0.2791 0.2161  -0.0402 -0.0369 -0.0280 242 GLN A NE2 
2099 N  N   . HIS A  244 ? 0.0955  0.1463 0.1270  -0.0062 -0.0304 -0.0261 243 HIS A N   
2100 C  CA  . HIS A  244 ? 0.1040  0.1287 0.1128  -0.0102 -0.0234 -0.0148 243 HIS A CA  
2101 C  C   . HIS A  244 ? 0.1058  0.1067 0.1027  0.0006  -0.0159 -0.0121 243 HIS A C   
2102 O  O   . HIS A  244 ? 0.1294  0.1190 0.1163  -0.0078 -0.0155 -0.0210 243 HIS A O   
2103 C  CB  . HIS A  244 ? 0.1398  0.1326 0.1316  -0.0122 -0.0140 0.0009  243 HIS A CB  
2104 C  CG  . HIS A  244 ? 0.1513  0.1224 0.1914  -0.0092 -0.0130 -0.0054 243 HIS A CG  
2105 N  ND1 . HIS A  244 ? 0.2185  0.1366 0.2770  -0.0089 0.0175  -0.0364 243 HIS A ND1 
2106 C  CD2 . HIS A  244 ? 0.2352  0.1682 0.2586  -0.0263 -0.0268 -0.0507 243 HIS A CD2 
2107 C  CE1 . HIS A  244 ? 0.2253  0.1513 0.3136  -0.0057 0.0154  -0.0617 243 HIS A CE1 
2108 N  NE2 . HIS A  244 ? 0.3140  0.1646 0.2931  -0.0069 -0.0677 -0.0602 243 HIS A NE2 
2109 N  N   . ASN A  245 ? 0.1020  0.1125 0.1098  -0.0103 -0.0302 -0.0030 244 ASN A N   
2110 C  CA  . ASN A  245 ? 0.1011  0.1118 0.0946  -0.0094 -0.0106 -0.0088 244 ASN A CA  
2111 C  C   . ASN A  245 ? 0.0950  0.0914 0.0934  0.0040  -0.0194 -0.0131 244 ASN A C   
2112 O  O   . ASN A  245 ? 0.1075  0.1100 0.1156  -0.0022 -0.0149 -0.0158 244 ASN A O   
2113 C  CB  . ASN A  245 ? 0.1368  0.0919 0.0962  0.0069  -0.0015 -0.0130 244 ASN A CB  
2114 C  CG  . ASN A  245 ? 0.0908  0.1022 0.0838  0.0012  -0.0135 -0.0119 244 ASN A CG  
2115 O  OD1 . ASN A  245 ? 0.1093  0.1065 0.0970  -0.0022 -0.0004 -0.0098 244 ASN A OD1 
2116 N  ND2 . ASN A  245 ? 0.1380  0.1037 0.1146  0.0047  -0.0060 -0.0022 244 ASN A ND2 
2117 N  N   . ASN A  246 ? 0.1231  0.0926 0.1106  -0.0009 -0.0242 0.0100  245 ASN A N   
2118 C  CA  . ASN A  246 ? 0.1366  0.1111 0.1014  0.0157  -0.0275 0.0080  245 ASN A CA  
2119 C  C   . ASN A  246 ? 0.1146  0.1032 0.1234  -0.0076 -0.0176 0.0067  245 ASN A C   
2120 O  O   . ASN A  246 ? 0.1474  0.1057 0.2265  -0.0059 -0.0540 -0.0046 245 ASN A O   
2121 C  CB  . ASN A  246 ? 0.1265  0.1305 0.1143  -0.0153 -0.0010 -0.0031 245 ASN A CB  
2122 C  CG  . ASN A  246 ? 0.1544  0.1239 0.1199  -0.0138 -0.0301 0.0053  245 ASN A CG  
2123 O  OD1 . ASN A  246 ? 0.1307  0.1294 0.1405  -0.0183 -0.0072 0.0022  245 ASN A OD1 
2124 N  ND2 . ASN A  246 ? 0.2113  0.1628 0.1351  -0.0462 0.0098  0.0033  245 ASN A ND2 
2125 N  N   . ARG A  247 ? 0.1088  0.1172 0.1076  0.0081  -0.0152 -0.0027 246 ARG A N   
2126 C  CA  . ARG A  247 ? 0.1283  0.1102 0.1199  0.0073  -0.0106 0.0074  246 ARG A CA  
2127 C  C   . ARG A  247 ? 0.1199  0.1164 0.1225  0.0066  -0.0066 0.0005  246 ARG A C   
2128 O  O   . ARG A  247 ? 0.1351  0.1154 0.1181  -0.0011 0.0046  -0.0091 246 ARG A O   
2129 C  CB  . ARG A  247 ? 0.1073  0.1178 0.1483  0.0097  -0.0089 -0.0011 246 ARG A CB  
2130 C  CG  . ARG A  247 ? 0.1434  0.1129 0.1107  0.0132  -0.0081 -0.0100 246 ARG A CG  
2131 C  CD  . ARG A  247 ? 0.1120  0.1234 0.1359  0.0274  -0.0072 -0.0144 246 ARG A CD  
2132 N  NE  . ARG A  247 ? 0.1377  0.1243 0.1272  0.0216  -0.0008 -0.0011 246 ARG A NE  
2133 C  CZ  . ARG A  247 ? 0.1316  0.1190 0.1084  0.0225  0.0132  0.0022  246 ARG A CZ  
2134 N  NH1 . ARG A  247 ? 0.1535  0.1330 0.1083  -0.0026 0.0078  -0.0073 246 ARG A NH1 
2135 N  NH2 . ARG A  247 ? 0.1445  0.1351 0.1384  0.0294  0.0285  -0.0062 246 ARG A NH2 
2136 N  N   . PRO A  248 ? 0.1483  0.1036 0.1337  -0.0139 -0.0038 0.0001  247 PRO A N   
2137 C  CA  . PRO A  248 ? 0.1423  0.1129 0.1348  -0.0277 -0.0095 0.0232  247 PRO A CA  
2138 C  C   . PRO A  248 ? 0.1326  0.0840 0.1351  0.0062  -0.0008 0.0068  247 PRO A C   
2139 O  O   . PRO A  248 ? 0.1416  0.1005 0.1319  0.0071  -0.0017 0.0103  247 PRO A O   
2140 C  CB  . PRO A  248 ? 0.1858  0.1038 0.1826  -0.0099 -0.0062 -0.0136 247 PRO A CB  
2141 C  CG  . PRO A  248 ? 0.2673  0.1217 0.1811  -0.0417 -0.0370 0.0079  247 PRO A CG  
2142 C  CD  . PRO A  248 ? 0.2134  0.0935 0.1700  -0.0115 -0.0131 -0.0259 247 PRO A CD  
2143 N  N   . THR A  249 ? 0.1524  0.1032 0.1215  -0.0030 -0.0113 0.0154  248 THR A N   
2144 C  CA  . THR A  249 ? 0.1287  0.1170 0.1216  0.0222  -0.0092 0.0190  248 THR A CA  
2145 C  C   . THR A  249 ? 0.1391  0.1032 0.1147  0.0001  0.0140  0.0210  248 THR A C   
2146 O  O   . THR A  249 ? 0.1520  0.1016 0.1718  0.0005  -0.0011 0.0234  248 THR A O   
2147 C  CB  . THR A  249 ? 0.1427  0.1048 0.1125  0.0068  0.0133  0.0118  248 THR A CB  
2148 O  OG1 . THR A  249 ? 0.1659  0.1077 0.1617  -0.0152 0.0174  0.0201  248 THR A OG1 
2149 C  CG2 . THR A  249 ? 0.1362  0.1155 0.1348  0.0225  0.0124  0.0126  248 THR A CG2 
2150 N  N   . GLN A  250 ? 0.1080  0.1305 0.1506  0.0102  0.0187  0.0190  249 GLN A N   
2151 C  CA  . GLN A  250 ? 0.1477  0.1199 0.1341  0.0242  0.0044  0.0201  249 GLN A CA  
2152 C  C   . GLN A  250 ? 0.1553  0.1056 0.1502  0.0010  0.0127  0.0228  249 GLN A C   
2153 O  O   . GLN A  250 ? 0.1772  0.1430 0.1341  0.0232  0.0100  0.0153  249 GLN A O   
2154 C  CB  . GLN A  250 ? 0.1344  0.1465 0.1307  0.0168  0.0192  0.0273  249 GLN A CB  
2155 C  CG  . GLN A  250 ? 0.1538  0.1592 0.1289  0.0038  0.0030  0.0132  249 GLN A CG  
2156 C  CD  . GLN A  250 ? 0.1718  0.1477 0.1323  0.0372  0.0050  0.0039  249 GLN A CD  
2157 O  OE1 . GLN A  250 ? 0.1872  0.1659 0.1854  0.0471  -0.0070 -0.0242 249 GLN A OE1 
2158 N  NE2 . GLN A  250 ? 0.1793  0.1423 0.1412  0.0184  0.0079  0.0173  249 GLN A NE2 
2159 N  N   A PRO A  251 ? 0.1743  0.1090 0.1720  0.0245  -0.0012 0.0501  250 PRO A N   
2160 N  N   B PRO A  251 ? 0.1696  0.0889 0.1914  0.0083  -0.0008 0.0367  250 PRO A N   
2161 C  CA  A PRO A  251 ? 0.2059  0.1074 0.1897  -0.0067 -0.0341 0.0430  250 PRO A CA  
2162 C  CA  B PRO A  251 ? 0.2142  0.1067 0.2210  0.0020  -0.0380 0.0433  250 PRO A CA  
2163 C  C   A PRO A  251 ? 0.1718  0.1040 0.1520  0.0181  -0.0085 0.0435  250 PRO A C   
2164 C  C   B PRO A  251 ? 0.1851  0.1199 0.1502  0.0106  -0.0047 0.0420  250 PRO A C   
2165 O  O   A PRO A  251 ? 0.1869  0.1022 0.1492  0.0207  0.0060  0.0484  250 PRO A O   
2166 O  O   B PRO A  251 ? 0.1736  0.1075 0.1535  0.0089  0.0055  0.0280  250 PRO A O   
2167 C  CB  A PRO A  251 ? 0.2343  0.1216 0.2673  0.0369  -0.0611 0.0589  250 PRO A CB  
2168 C  CB  B PRO A  251 ? 0.1757  0.1274 0.2967  0.0122  -0.0062 0.0807  250 PRO A CB  
2169 C  CG  A PRO A  251 ? 0.1786  0.0962 0.2134  0.0098  0.0000  0.0552  250 PRO A CG  
2170 C  CG  B PRO A  251 ? 0.2698  0.2141 0.2630  0.0447  0.1403  0.1576  250 PRO A CG  
2171 C  CD  A PRO A  251 ? 0.1736  0.0707 0.2045  0.0239  0.0252  0.0347  250 PRO A CD  
2172 C  CD  B PRO A  251 ? 0.2231  0.0643 0.2741  0.0027  -0.0037 -0.0282 250 PRO A CD  
2173 N  N   . LEU A  252 ? 0.2222  0.1635 0.1377  0.0332  -0.0114 0.0478  251 LEU A N   
2174 C  CA  . LEU A  252 ? 0.2260  0.1441 0.1430  0.0469  0.0009  0.0138  251 LEU A CA  
2175 C  C   . LEU A  252 ? 0.2253  0.1280 0.1323  0.0353  0.0000  0.0606  251 LEU A C   
2176 O  O   . LEU A  252 ? 0.2486  0.1177 0.1782  0.0058  -0.0449 0.0571  251 LEU A O   
2177 C  CB  . LEU A  252 ? 0.4796  0.2097 0.1362  0.1159  0.0402  0.0115  251 LEU A CB  
2178 C  CG  . LEU A  252 ? 0.3527  0.2459 0.2020  0.0272  0.0672  0.0234  251 LEU A CG  
2179 C  CD1 . LEU A  252 ? 0.2271  0.2813 0.1729  0.1384  -0.0011 0.0172  251 LEU A CD1 
2180 C  CD2 . LEU A  252 ? 0.3003  0.3484 0.1718  0.0631  0.0533  -0.0305 251 LEU A CD2 
2181 N  N   . LYS A  253 ? 0.2357  0.1093 0.1890  0.0325  -0.0298 0.0514  252 LYS A N   
2182 C  CA  . LYS A  253 ? 0.2328  0.1386 0.2235  0.0443  -0.0418 0.0330  252 LYS A CA  
2183 C  C   . LYS A  253 ? 0.2332  0.1368 0.2568  0.0425  -0.0316 0.0447  252 LYS A C   
2184 O  O   . LYS A  253 ? 0.2418  0.1897 0.2583  0.0269  -0.0794 0.0499  252 LYS A O   
2185 C  CB  . LYS A  253 ? 0.2016  0.2070 0.2332  0.0234  -0.0607 0.0215  252 LYS A CB  
2186 C  CG  . LYS A  253 ? 0.2027  0.2451 0.2996  0.0447  -0.0499 -0.0086 252 LYS A CG  
2187 C  CD  . LYS A  253 ? 0.4109  0.2849 0.3484  0.1022  -0.1156 -0.0734 252 LYS A CD  
2188 C  CE  . LYS A  253 ? 0.4123  0.2098 0.4347  0.0482  -0.1373 -0.0888 252 LYS A CE  
2189 N  NZ  . LYS A  253 ? 0.6724  0.3322 0.6838  0.2195  -0.1782 -0.1575 252 LYS A NZ  
2190 N  N   . GLY A  254 ? 0.2702  0.1581 0.2249  0.0209  -0.0858 0.0444  253 GLY A N   
2191 C  CA  . GLY A  254 ? 0.3528  0.1707 0.2508  0.0124  -0.1322 0.0328  253 GLY A CA  
2192 C  C   . GLY A  254 ? 0.2572  0.1720 0.2762  0.0265  -0.1093 0.0675  253 GLY A C   
2193 O  O   . GLY A  254 ? 0.2996  0.2011 0.2418  0.0422  -0.1274 0.0370  253 GLY A O   
2194 N  N   . ARG A  255 ? 0.2052  0.1438 0.1854  0.0495  -0.0491 0.0379  254 ARG A N   
2195 C  CA  . ARG A  255 ? 0.1804  0.1359 0.1448  0.0582  -0.0410 0.0156  254 ARG A CA  
2196 C  C   . ARG A  255 ? 0.1412  0.1937 0.1800  0.0356  -0.0449 0.0379  254 ARG A C   
2197 O  O   . ARG A  255 ? 0.2005  0.2407 0.2120  0.0021  -0.0264 0.0434  254 ARG A O   
2198 C  CB  . ARG A  255 ? 0.1822  0.1538 0.1266  0.0505  -0.0089 0.0356  254 ARG A CB  
2199 C  CG  . ARG A  255 ? 0.1596  0.1725 0.1465  0.0332  -0.0323 0.0250  254 ARG A CG  
2200 C  CD  . ARG A  255 ? 0.1430  0.1474 0.1423  0.0016  -0.0299 0.0223  254 ARG A CD  
2201 N  NE  . ARG A  255 ? 0.1402  0.1143 0.1203  0.0253  -0.0219 0.0081  254 ARG A NE  
2202 C  CZ  . ARG A  255 ? 0.1235  0.1144 0.1337  0.0410  -0.0072 0.0181  254 ARG A CZ  
2203 N  NH1 . ARG A  255 ? 0.1509  0.0987 0.1137  0.0223  0.0092  0.0188  254 ARG A NH1 
2204 N  NH2 . ARG A  255 ? 0.1294  0.1151 0.1351  0.0009  0.0032  0.0140  254 ARG A NH2 
2205 N  N   . THR A  256 ? 0.1835  0.1603 0.1524  0.0483  -0.0330 0.0188  255 THR A N   
2206 C  CA  . THR A  256 ? 0.1757  0.2266 0.1463  0.0886  -0.0320 0.0157  255 THR A CA  
2207 C  C   . THR A  256 ? 0.1538  0.1639 0.1132  0.0293  -0.0184 0.0069  255 THR A C   
2208 O  O   . THR A  256 ? 0.1682  0.1932 0.1412  0.0216  0.0004  0.0133  255 THR A O   
2209 C  CB  . THR A  256 ? 0.2490  0.3240 0.1606  0.1628  -0.1097 -0.0453 255 THR A CB  
2210 O  OG1 . THR A  256 ? 0.3207  0.3869 0.2027  0.1606  -0.0972 0.0163  255 THR A OG1 
2211 C  CG2 . THR A  256 ? 0.2845  0.3671 0.1344  0.1333  -0.0565 -0.0380 255 THR A CG2 
2212 N  N   . VAL A  257 ? 0.1470  0.1474 0.1066  0.0298  -0.0040 0.0079  256 VAL A N   
2213 C  CA  . VAL A  257 ? 0.1181  0.1427 0.0979  0.0124  -0.0026 0.0242  256 VAL A CA  
2214 C  C   . VAL A  257 ? 0.1348  0.1456 0.0812  0.0189  -0.0211 0.0181  256 VAL A C   
2215 O  O   . VAL A  257 ? 0.1754  0.1646 0.0917  -0.0139 -0.0200 0.0377  256 VAL A O   
2216 C  CB  . VAL A  257 ? 0.1213  0.1465 0.1168  0.0105  -0.0021 0.0193  256 VAL A CB  
2217 C  CG1 . VAL A  257 ? 0.1294  0.1499 0.1252  0.0152  -0.0038 0.0370  256 VAL A CG1 
2218 C  CG2 . VAL A  257 ? 0.1603  0.1280 0.1116  -0.0013 -0.0188 0.0074  256 VAL A CG2 
2219 N  N   A ARG A  258 ? 0.1319  0.1301 0.0901  0.0088  -0.0072 0.0200  257 ARG A N   
2220 N  N   B ARG A  258 ? 0.1319  0.1305 0.0901  0.0086  -0.0070 0.0198  257 ARG A N   
2221 C  CA  A ARG A  258 ? 0.1152  0.1481 0.1016  0.0158  -0.0087 0.0157  257 ARG A CA  
2222 C  CA  B ARG A  258 ? 0.1153  0.1483 0.1014  0.0160  -0.0089 0.0159  257 ARG A CA  
2223 C  C   A ARG A  258 ? 0.1137  0.1477 0.0827  0.0079  -0.0165 0.0190  257 ARG A C   
2224 C  C   B ARG A  258 ? 0.1137  0.1477 0.0827  0.0079  -0.0165 0.0190  257 ARG A C   
2225 O  O   A ARG A  258 ? 0.1502  0.1969 0.0680  0.0489  -0.0198 0.0241  257 ARG A O   
2226 O  O   B ARG A  258 ? 0.1509  0.1976 0.0686  0.0494  -0.0194 0.0242  257 ARG A O   
2227 C  CB  A ARG A  258 ? 0.1181  0.1527 0.1111  0.0048  -0.0055 0.0225  257 ARG A CB  
2228 C  CB  B ARG A  258 ? 0.1199  0.1535 0.1117  0.0036  -0.0051 0.0238  257 ARG A CB  
2229 C  CG  A ARG A  258 ? 0.1127  0.2199 0.1948  0.0242  -0.0179 0.0631  257 ARG A CG  
2230 C  CG  B ARG A  258 ? 0.1160  0.2230 0.2009  0.0296  -0.0142 0.0757  257 ARG A CG  
2231 C  CD  A ARG A  258 ? 0.1090  0.3564 0.1524  -0.0114 -0.0044 0.0543  257 ARG A CD  
2232 C  CD  B ARG A  258 ? 0.1225  0.3692 0.1416  -0.0082 -0.0083 0.0547  257 ARG A CD  
2233 N  NE  A ARG A  258 ? 0.0898  0.1908 0.1793  0.0143  0.0087  0.0410  257 ARG A NE  
2234 N  NE  B ARG A  258 ? 0.1172  0.2120 0.2177  0.0262  0.0133  0.0388  257 ARG A NE  
2235 C  CZ  A ARG A  258 ? 0.0989  0.1919 0.1152  -0.0047 0.0126  0.0242  257 ARG A CZ  
2236 C  CZ  B ARG A  258 ? 0.2048  0.2913 0.2357  0.0075  0.0165  0.0400  257 ARG A CZ  
2237 N  NH1 A ARG A  258 ? 0.1138  0.1941 0.1549  -0.0184 0.0142  -0.0015 257 ARG A NH1 
2238 N  NH1 B ARG A  258 ? 0.1606  0.2346 0.2221  -0.0249 0.0046  0.0217  257 ARG A NH1 
2239 N  NH2 A ARG A  258 ? 0.1301  0.2436 0.1610  -0.0061 -0.0366 0.0945  257 ARG A NH2 
2240 N  NH2 B ARG A  258 ? 0.2364  0.2830 0.2565  -0.0133 -0.0120 0.0240  257 ARG A NH2 
2241 N  N   . ALA A  259 ? 0.1283  0.1578 0.0725  0.0251  -0.0060 0.0108  258 ALA A N   
2242 C  CA  . ALA A  259 ? 0.1264  0.1474 0.0864  0.0161  -0.0076 0.0239  258 ALA A CA  
2243 C  C   . ALA A  259 ? 0.1384  0.1470 0.0831  0.0111  -0.0200 0.0190  258 ALA A C   
2244 O  O   . ALA A  259 ? 0.1646  0.1800 0.0827  0.0198  -0.0386 0.0159  258 ALA A O   
2245 C  CB  . ALA A  259 ? 0.1481  0.1984 0.0942  0.0032  -0.0025 0.0300  258 ALA A CB  
2246 N  N   A SER A  260 ? 0.1452  0.1430 0.0759  0.0307  -0.0036 0.0041  259 SER A N   
2247 N  N   B SER A  260 ? 0.1330  0.1481 0.0794  0.0301  -0.0013 0.0088  259 SER A N   
2248 C  CA  A SER A  260 ? 0.2109  0.1264 0.1106  0.0549  -0.0337 -0.0195 259 SER A CA  
2249 C  CA  B SER A  260 ? 0.1452  0.1427 0.0882  0.0082  -0.0176 0.0236  259 SER A CA  
2250 C  C   A SER A  260 ? 0.1488  0.1955 0.1198  0.0578  -0.0714 -0.0640 259 SER A C   
2251 C  C   B SER A  260 ? 0.1301  0.1373 0.0879  -0.0029 -0.0204 0.0397  259 SER A C   
2252 O  O   A SER A  260 ? 0.1355  0.2776 0.2301  0.0308  -0.0443 -0.1494 259 SER A O   
2253 O  O   B SER A  260 ? 0.1225  0.1797 0.1225  -0.0256 -0.0111 0.0536  259 SER A O   
2254 C  CB  A SER A  260 ? 0.2558  0.1477 0.2034  0.0293  -0.0906 0.0272  259 SER A CB  
2255 C  CB  B SER A  260 ? 0.2113  0.1556 0.0856  0.0280  -0.0902 -0.0159 259 SER A CB  
2256 O  OG  A SER A  260 ? 0.2888  0.2687 0.1729  0.1377  -0.1482 -0.1385 259 SER A OG  
2257 O  OG  B SER A  260 ? 0.2224  0.1531 0.1283  0.0617  -0.1134 -0.0215 259 SER A OG  
2258 N  N   A PHE A  261 ? 0.1854  0.2423 0.0786  0.0525  -0.0237 -0.0462 260 PHE A N   
2259 N  N   B PHE A  261 ? 0.2071  0.1603 0.0932  -0.0346 -0.0198 0.0263  260 PHE A N   
2260 C  CA  A PHE A  261 ? 0.2240  0.1499 0.1115  0.0625  -0.0089 -0.0292 260 PHE A CA  
2261 C  CA  B PHE A  261 ? 0.1854  0.1544 0.0766  0.0171  -0.0413 -0.0204 260 PHE A CA  
2262 C  C   A PHE A  261 ? 0.2256  0.2070 0.1120  -0.0201 -0.0306 0.0044  260 PHE A C   
2263 C  C   B PHE A  261 ? 0.1102  0.2931 0.2303  0.1237  -0.0829 -0.0600 260 PHE A C   
2264 O  O   A PHE A  261 ? 0.4026  0.2680 0.0504  0.1587  -0.0320 -0.0043 260 PHE A O   
2265 O  O   B PHE A  261 ? 0.1344  0.2224 0.1434  -0.0100 0.0010  -0.0678 260 PHE A O   
2266 C  CB  A PHE A  261 ? 0.3937  0.6384 0.2109  0.2183  0.1164  0.2757  260 PHE A CB  
2267 C  CB  B PHE A  261 ? 0.1635  0.1743 0.0867  -0.0305 -0.0168 0.0076  260 PHE A CB  
2268 C  CG  A PHE A  261 ? 0.5948  4.0370 1.2284  -1.4605 -0.7871 2.0889  260 PHE A CG  
2269 C  CG  B PHE A  261 ? 0.1427  0.1883 0.0873  -0.0173 -0.0178 0.0215  260 PHE A CG  
2270 C  CD1 A PHE A  261 ? 0.1793  0.3373 0.9487  0.0208  -0.2655 -0.1231 260 PHE A CD1 
2271 C  CD1 B PHE A  261 ? 0.1826  0.2303 0.1027  0.0027  0.0232  -0.0231 260 PHE A CD1 
2272 C  CD2 A PHE A  261 ? 0.1366  0.3794 0.0873  -0.0099 -0.0030 0.0141  260 PHE A CD2 
2273 C  CD2 B PHE A  261 ? 0.1797  0.1732 0.0864  -0.0317 -0.0504 -0.0041 260 PHE A CD2 
2274 C  CE1 A PHE A  261 ? 0.0337  0.2037 0.0450  0.0397  -0.0168 0.0381  260 PHE A CE1 
2275 C  CE1 B PHE A  261 ? 0.1678  0.2368 0.1049  -0.0082 -0.0095 -0.0284 260 PHE A CE1 
2276 C  CE2 A PHE A  261 ? 0.1316  0.3280 0.1441  -0.0150 -0.0491 0.0060  260 PHE A CE2 
2277 C  CE2 B PHE A  261 ? 0.1351  0.2106 0.0962  -0.0188 -0.0096 -0.0159 260 PHE A CE2 
2278 C  CZ  A PHE A  261 ? 0.1955  0.2788 0.0820  -0.0277 -0.0237 0.1234  260 PHE A CZ  
2279 C  CZ  B PHE A  261 ? 0.1316  0.2224 0.1386  -0.0214 -0.0017 -0.0363 260 PHE A CZ  
2280 O  OXT . PHE A  261 ? 0.2432  0.4548 0.1080  0.1502  0.0153  0.0254  260 PHE A OXT 
2281 N  N   . PRO B  4   ? 1.2641  1.0265 1.3643  -0.2964 0.1219  0.1043  3   PRO B N   
2282 C  CA  . PRO B  4   ? 0.6840  0.3757 0.6192  0.1824  0.0674  -0.2463 3   PRO B CA  
2283 C  C   . PRO B  4   ? 1.0805  0.2957 0.5791  -0.1351 -0.0988 0.0810  3   PRO B C   
2284 O  O   . PRO B  4   ? 1.0148  0.4099 0.7268  0.2939  -0.1638 -0.1759 3   PRO B O   
2285 C  CB  . PRO B  4   ? 0.8340  0.9104 0.6685  0.4654  0.3183  -0.1427 3   PRO B CB  
2286 C  CG  . PRO B  4   ? 0.7144  0.9118 0.7587  -0.1170 0.4407  -0.0107 3   PRO B CG  
2287 C  CD  . PRO B  4   ? 1.2679  0.8093 1.3413  -0.5255 0.2609  0.4578  3   PRO B CD  
2288 N  N   . ASP B  5   ? 0.7922  0.3772 0.1833  0.0244  0.1333  0.0117  4   ASP B N   
2289 C  CA  . ASP B  5   ? 0.6456  0.6134 0.1707  -0.0081 0.1329  -0.0367 4   ASP B CA  
2290 C  C   . ASP B  5   ? 0.4051  0.4867 0.3133  0.1848  0.1354  0.0948  4   ASP B C   
2291 O  O   . ASP B  5   ? 0.3959  0.4138 0.2260  0.0621  0.0279  -0.0320 4   ASP B O   
2292 C  CB  . ASP B  5   ? 0.6220  0.7505 0.4187  0.0523  0.1691  0.1113  4   ASP B CB  
2293 C  CG  . ASP B  5   ? 0.7767  0.7508 0.5224  -0.0465 0.4971  -0.1230 4   ASP B CG  
2294 O  OD1 . ASP B  5   ? 2.0361  0.9574 0.5915  0.5030  0.4137  0.1676  4   ASP B OD1 
2295 O  OD2 . ASP B  5   ? 0.4573  0.6266 0.4515  -0.0778 0.2450  0.0575  4   ASP B OD2 
2296 N  N   . TRP B  6   ? 0.3154  0.3036 0.2170  0.0715  0.0784  0.0376  5   TRP B N   
2297 C  CA  . TRP B  6   ? 0.2712  0.2540 0.2125  0.0600  0.0702  0.0483  5   TRP B CA  
2298 C  C   . TRP B  6   ? 0.2917  0.1966 0.1685  0.0136  0.0644  0.0023  5   TRP B C   
2299 O  O   . TRP B  6   ? 0.3222  0.2106 0.1700  0.0443  0.0262  -0.0068 5   TRP B O   
2300 C  CB  . TRP B  6   ? 0.2371  0.1659 0.2199  -0.0140 0.0680  0.0167  5   TRP B CB  
2301 C  CG  . TRP B  6   ? 0.2522  0.1560 0.1747  -0.0039 0.0757  -0.0016 5   TRP B CG  
2302 C  CD1 . TRP B  6   ? 0.2134  0.1969 0.1635  -0.0264 0.0565  -0.0461 5   TRP B CD1 
2303 C  CD2 . TRP B  6   ? 0.2090  0.1588 0.1362  -0.0189 0.0194  -0.0148 5   TRP B CD2 
2304 N  NE1 . TRP B  6   ? 0.2188  0.1659 0.1434  -0.0219 0.0320  -0.0252 5   TRP B NE1 
2305 C  CE2 . TRP B  6   ? 0.1908  0.1542 0.1535  -0.0228 -0.0011 -0.0234 5   TRP B CE2 
2306 C  CE3 . TRP B  6   ? 0.1930  0.1808 0.1646  -0.0421 0.0323  -0.0064 5   TRP B CE3 
2307 C  CZ2 . TRP B  6   ? 0.2102  0.1720 0.1305  -0.0457 -0.0148 -0.0178 5   TRP B CZ2 
2308 C  CZ3 . TRP B  6   ? 0.1908  0.1747 0.1567  -0.0389 -0.0078 -0.0196 5   TRP B CZ3 
2309 C  CH2 . TRP B  6   ? 0.1757  0.1829 0.1517  -0.0336 -0.0184 -0.0369 5   TRP B CH2 
2310 N  N   . GLY B  7   ? 0.2095  0.1955 0.1732  0.0094  0.0334  0.0304  6   GLY B N   
2311 C  CA  . GLY B  7   ? 0.2303  0.1914 0.1700  0.0177  0.0428  0.0127  6   GLY B CA  
2312 C  C   . GLY B  7   ? 0.1993  0.1359 0.1811  0.0002  0.0282  0.0148  6   GLY B C   
2313 O  O   . GLY B  7   ? 0.2109  0.1465 0.1901  -0.0237 0.0248  0.0121  6   GLY B O   
2314 N  N   . TYR B  8   ? 0.1678  0.1588 0.1747  0.0044  0.0322  0.0428  7   TYR B N   
2315 C  CA  . TYR B  8   ? 0.1840  0.1244 0.1897  0.0242  0.0425  0.0351  7   TYR B CA  
2316 C  C   . TYR B  8   ? 0.2102  0.1682 0.2669  0.0385  0.0273  0.0658  7   TYR B C   
2317 O  O   . TYR B  8   ? 0.2508  0.2127 0.2899  0.0829  0.0719  0.1012  7   TYR B O   
2318 C  CB  . TYR B  8   ? 0.1617  0.1344 0.1969  0.0161  0.0197  0.0472  7   TYR B CB  
2319 C  CG  . TYR B  8   ? 0.1380  0.1294 0.1499  -0.0030 0.0134  0.0033  7   TYR B CG  
2320 C  CD1 . TYR B  8   ? 0.1477  0.1196 0.1685  -0.0057 0.0168  0.0000  7   TYR B CD1 
2321 C  CD2 . TYR B  8   ? 0.1513  0.1266 0.1276  -0.0149 0.0049  0.0015  7   TYR B CD2 
2322 C  CE1 . TYR B  8   ? 0.1333  0.1120 0.1659  -0.0006 0.0323  0.0040  7   TYR B CE1 
2323 C  CE2 . TYR B  8   ? 0.1438  0.1592 0.1088  -0.0201 0.0017  0.0073  7   TYR B CE2 
2324 C  CZ  . TYR B  8   ? 0.1267  0.1145 0.1326  -0.0018 0.0035  -0.0003 7   TYR B CZ  
2325 O  OH  . TYR B  8   ? 0.1186  0.1150 0.1208  -0.0066 0.0066  -0.0073 7   TYR B OH  
2326 N  N   . ASP B  9   ? 0.2398  0.1815 0.2587  0.0416  -0.0306 0.0895  8   ASP B N   
2327 C  CA  . ASP B  9   ? 0.1962  0.2497 0.3980  0.0534  0.0033  0.1415  8   ASP B CA  
2328 C  C   . ASP B  9   ? 0.3736  0.2293 0.2874  0.0894  0.0788  0.0805  8   ASP B C   
2329 O  O   . ASP B  9   ? 0.4027  0.1754 0.3366  0.0391  0.0320  0.0757  8   ASP B O   
2330 C  CB  . ASP B  9   ? 0.2633  0.3567 0.5046  0.0977  -0.1102 0.1123  8   ASP B CB  
2331 C  CG  . ASP B  9   ? 0.3294  0.4403 0.6916  0.1454  -0.0844 0.0881  8   ASP B CG  
2332 O  OD1 . ASP B  9   ? 0.7420  0.8470 0.5272  0.0929  0.2179  0.3686  8   ASP B OD1 
2333 O  OD2 . ASP B  9   ? 0.7016  0.4307 1.0167  0.0159  -0.3195 0.0298  8   ASP B OD2 
2334 N  N   . ASP B  10  ? 0.4038  0.2494 0.4135  0.1286  0.1338  0.1579  9   ASP B N   
2335 C  CA  . ASP B  10  ? 0.5096  0.2073 0.5284  0.1429  0.1728  0.1064  9   ASP B CA  
2336 C  C   . ASP B  10  ? 0.4986  0.3075 0.2842  -0.0146 0.0608  0.0662  9   ASP B C   
2337 O  O   . ASP B  10  ? 0.4949  0.2533 0.3125  0.0249  -0.0011 0.0908  9   ASP B O   
2338 C  CB  . ASP B  10  ? 0.6394  0.2934 0.5899  0.2633  0.1001  0.1654  9   ASP B CB  
2339 C  CG  . ASP B  10  ? 0.9929  0.8235 0.8506  0.3313  0.1931  -0.1404 9   ASP B CG  
2340 O  OD1 . ASP B  10  ? 0.3427  1.0484 1.5074  0.1490  0.4135  0.3402  9   ASP B OD1 
2341 O  OD2 . ASP B  10  ? 1.3198  0.6330 0.9067  0.3700  -0.6104 0.1165  9   ASP B OD2 
2342 N  N   . LYS B  11  ? 0.3643  0.2027 0.2971  0.0590  -0.0100 0.0809  10  LYS B N   
2343 C  CA  . LYS B  11  ? 0.4160  0.2623 0.3315  0.0335  0.0234  0.1065  10  LYS B CA  
2344 C  C   . LYS B  11  ? 0.3779  0.2809 0.2558  0.0254  0.0748  0.1011  10  LYS B C   
2345 O  O   . LYS B  11  ? 0.4365  0.2361 0.3559  0.0122  0.1048  0.1143  10  LYS B O   
2346 C  CB  . LYS B  11  ? 0.4446  0.4056 0.3348  0.1246  -0.0987 0.0991  10  LYS B CB  
2347 N  N   . ASN B  12  ? 0.4207  0.1714 0.2518  0.0641  0.0635  0.0518  11  ASN B N   
2348 C  CA  . ASN B  12  ? 0.3883  0.2271 0.2429  0.0376  0.1330  0.0850  11  ASN B CA  
2349 C  C   . ASN B  12  ? 0.3122  0.2081 0.1861  -0.0389 0.0317  -0.0084 11  ASN B C   
2350 O  O   . ASN B  12  ? 0.2587  0.2133 0.1937  -0.0114 0.0370  0.0183  11  ASN B O   
2351 C  CB  . ASN B  12  ? 0.3003  0.2662 0.2156  0.0400  0.0226  0.0587  11  ASN B CB  
2352 C  CG  . ASN B  12  ? 0.3937  0.3449 0.1377  -0.0533 -0.0467 0.0440  11  ASN B CG  
2353 O  OD1 . ASN B  12  ? 0.2963  0.2247 0.2178  0.0040  0.0051  0.0354  11  ASN B OD1 
2354 N  ND2 . ASN B  12  ? 0.3844  0.2885 0.1962  -0.0158 -0.0281 0.0135  11  ASN B ND2 
2355 N  N   . GLY B  13  ? 0.3642  0.1675 0.2257  0.0062  0.0871  0.0457  12  GLY B N   
2356 C  CA  . GLY B  13  ? 0.2788  0.1754 0.2030  -0.0104 0.0359  0.0179  12  GLY B CA  
2357 C  C   . GLY B  13  ? 0.2615  0.1610 0.2633  0.0025  0.0814  0.0312  12  GLY B C   
2358 O  O   . GLY B  13  ? 0.2849  0.1538 0.3000  -0.0124 0.0939  0.0092  12  GLY B O   
2359 N  N   . PRO B  14  ? 0.2389  0.1603 0.2476  -0.0201 0.0516  -0.0288 13  PRO B N   
2360 C  CA  . PRO B  14  ? 0.2242  0.1757 0.2224  -0.0172 0.0525  -0.0092 13  PRO B CA  
2361 C  C   . PRO B  14  ? 0.2521  0.1581 0.2526  -0.0239 0.0684  0.0206  13  PRO B C   
2362 O  O   . PRO B  14  ? 0.2651  0.1890 0.3366  -0.0584 0.0599  -0.0475 13  PRO B O   
2363 C  CB  . PRO B  14  ? 0.2213  0.1571 0.2465  -0.0409 0.0659  -0.0081 13  PRO B CB  
2364 C  CG  . PRO B  14  ? 0.1930  0.1923 0.2285  -0.0098 0.0249  -0.0281 13  PRO B CG  
2365 C  CD  . PRO B  14  ? 0.2188  0.1840 0.2098  -0.0295 0.0295  0.0388  13  PRO B CD  
2366 N  N   . GLU B  15  ? 0.2550  0.1483 0.3122  0.0001  0.0285  -0.0173 14  GLU B N   
2367 C  CA  . GLU B  15  ? 0.3406  0.1366 0.3359  -0.0121 0.0380  0.0038  14  GLU B CA  
2368 C  C   . GLU B  15  ? 0.3628  0.1894 0.3334  -0.0535 0.0406  0.0156  14  GLU B C   
2369 O  O   . GLU B  15  ? 0.3941  0.1635 0.4266  -0.0479 0.0252  0.0042  14  GLU B O   
2370 C  CB  . GLU B  15  ? 0.4284  0.1847 0.4271  0.0156  0.0642  -0.0185 14  GLU B CB  
2371 C  CG  . GLU B  15  ? 0.4529  0.1976 0.4802  0.0390  0.1385  -0.0721 14  GLU B CG  
2372 C  CD  . GLU B  15  ? 1.0297  0.7221 0.2633  -0.1246 0.1199  -0.0659 14  GLU B CD  
2373 O  OE1 . GLU B  15  ? 0.9624  1.4963 0.7227  -0.3700 0.4149  0.0264  14  GLU B OE1 
2374 O  OE2 . GLU B  15  ? 0.9861  1.2718 1.3232  -0.0388 0.3714  0.0705  14  GLU B OE2 
2375 N  N   . GLN B  16  ? 0.2945  0.1876 0.3219  -0.0094 0.0237  0.0272  15  GLN B N   
2376 C  CA  . GLN B  16  ? 0.2601  0.1603 0.3312  -0.0247 0.0122  0.0664  15  GLN B CA  
2377 C  C   . GLN B  16  ? 0.2500  0.1876 0.3441  -0.0243 -0.0126 0.1032  15  GLN B C   
2378 O  O   . GLN B  16  ? 0.2529  0.2224 0.3477  -0.0565 0.0157  0.0685  15  GLN B O   
2379 C  CB  . GLN B  16  ? 0.2741  0.1851 0.3014  -0.0086 -0.0345 0.0209  15  GLN B CB  
2380 C  CG  . GLN B  16  ? 0.4013  0.1817 0.3111  0.0802  -0.0639 0.0181  15  GLN B CG  
2381 C  CD  . GLN B  16  ? 0.2283  0.2314 0.3865  -0.0139 -0.0674 0.0802  15  GLN B CD  
2382 O  OE1 . GLN B  16  ? 0.3873  0.2187 0.4274  0.0158  0.0715  0.0468  15  GLN B OE1 
2383 N  NE2 . GLN B  16  ? 0.3704  0.1840 0.4278  0.0591  -0.0520 0.0018  15  GLN B NE2 
2384 N  N   . TRP B  17  ? 0.2676  0.1621 0.2655  -0.0339 -0.0354 0.0468  16  TRP B N   
2385 C  CA  . TRP B  17  ? 0.2314  0.1337 0.2827  -0.0271 0.0185  0.0770  16  TRP B CA  
2386 C  C   . TRP B  17  ? 0.2317  0.1531 0.2766  -0.0248 0.0358  0.0322  16  TRP B C   
2387 O  O   . TRP B  17  ? 0.2289  0.1829 0.2572  -0.0359 0.0208  0.0270  16  TRP B O   
2388 C  CB  . TRP B  17  ? 0.2142  0.1588 0.2048  -0.0514 0.0223  0.0216  16  TRP B CB  
2389 C  CG  . TRP B  17  ? 0.1854  0.1405 0.1764  -0.0225 0.0375  -0.0006 16  TRP B CG  
2390 C  CD1 . TRP B  17  ? 0.2274  0.1434 0.1879  -0.0183 0.0330  0.0013  16  TRP B CD1 
2391 C  CD2 . TRP B  17  ? 0.1930  0.1483 0.1603  -0.0200 0.0494  -0.0190 16  TRP B CD2 
2392 N  NE1 . TRP B  17  ? 0.1912  0.1445 0.1696  -0.0261 0.0419  -0.0157 16  TRP B NE1 
2393 C  CE2 . TRP B  17  ? 0.1930  0.1312 0.1729  -0.0046 0.0233  -0.0133 16  TRP B CE2 
2394 C  CE3 . TRP B  17  ? 0.1668  0.1416 0.1696  0.0041  0.0285  -0.0226 16  TRP B CE3 
2395 C  CZ2 . TRP B  17  ? 0.1976  0.1316 0.1596  -0.0050 0.0522  -0.0042 16  TRP B CZ2 
2396 C  CZ3 . TRP B  17  ? 0.1527  0.1341 0.1876  -0.0057 0.0394  -0.0243 16  TRP B CZ3 
2397 C  CH2 . TRP B  17  ? 0.1664  0.1316 0.1639  0.0018  0.0312  -0.0129 16  TRP B CH2 
2398 N  N   . SER B  18  ? 0.2204  0.1592 0.2963  -0.0553 -0.0143 0.0230  17  SER B N   
2399 C  CA  . SER B  18  ? 0.2217  0.1531 0.2845  -0.0375 0.0369  -0.0168 17  SER B CA  
2400 C  C   . SER B  18  ? 0.2203  0.1948 0.2551  -0.0536 0.0231  0.0441  17  SER B C   
2401 O  O   . SER B  18  ? 0.2508  0.2117 0.3075  -0.0522 0.0311  0.0323  17  SER B O   
2402 C  CB  . SER B  18  ? 0.2357  0.1711 0.2813  -0.0102 0.0252  -0.0078 17  SER B CB  
2403 O  OG  . SER B  18  ? 0.2816  0.1720 0.4242  -0.0184 0.0108  0.0374  17  SER B OG  
2404 N  N   . LYS B  19  ? 0.2916  0.2095 0.2885  -0.0598 -0.0001 0.0897  18  LYS B N   
2405 C  CA  . LYS B  19  ? 0.2924  0.2339 0.2773  -0.0719 -0.0405 0.0973  18  LYS B CA  
2406 C  C   . LYS B  19  ? 0.2407  0.2375 0.4102  -0.0653 -0.0861 0.0882  18  LYS B C   
2407 O  O   . LYS B  19  ? 0.3189  0.2248 0.3506  -0.0891 0.0429  0.0256  18  LYS B O   
2408 C  CB  . LYS B  19  ? 0.2762  0.3334 0.2648  -0.0256 0.0026  0.0894  18  LYS B CB  
2409 C  CG  . LYS B  19  ? 0.6675  0.2612 0.5231  0.0063  0.3052  -0.0361 18  LYS B CG  
2410 N  N   . LEU B  20  ? 0.3079  0.2554 0.2418  -0.1056 -0.0190 0.0658  19  LEU B N   
2411 C  CA  . LEU B  20  ? 0.4160  0.2454 0.2543  -0.1427 0.0026  0.0141  19  LEU B CA  
2412 C  C   . LEU B  20  ? 0.2576  0.1876 0.2407  -0.0583 0.0548  -0.0082 19  LEU B C   
2413 O  O   . LEU B  20  ? 0.3197  0.2027 0.2023  -0.0515 0.0914  -0.0467 19  LEU B O   
2414 C  CB  . LEU B  20  ? 0.5180  0.3589 0.2027  -0.2046 -0.0368 0.0367  19  LEU B CB  
2415 N  N   . TYR B  21  ? 0.2788  0.1912 0.1696  -0.0703 0.0379  -0.0088 20  TYR B N   
2416 C  CA  . TYR B  21  ? 0.1872  0.1596 0.1914  -0.0397 0.0502  -0.0342 20  TYR B CA  
2417 C  C   . TYR B  21  ? 0.2034  0.1671 0.2174  -0.0298 0.0738  -0.0546 20  TYR B C   
2418 O  O   . TYR B  21  ? 0.1969  0.1869 0.1914  -0.0274 0.0707  -0.0469 20  TYR B O   
2419 C  CB  . TYR B  21  ? 0.2059  0.1477 0.1761  -0.0296 0.0549  -0.0378 20  TYR B CB  
2420 C  CG  . TYR B  21  ? 0.2310  0.1567 0.1664  -0.0583 0.0624  -0.0272 20  TYR B CG  
2421 C  CD1 . TYR B  21  ? 0.3054  0.1894 0.2310  -0.0524 0.1504  -0.0783 20  TYR B CD1 
2422 C  CD2 . TYR B  21  ? 0.2755  0.2425 0.1937  -0.1211 0.0661  -0.0212 20  TYR B CD2 
2423 C  CE1 . TYR B  21  ? 0.3305  0.2368 0.2375  -0.0944 0.1269  -0.0785 20  TYR B CE1 
2424 C  CE2 . TYR B  21  ? 0.4300  0.2339 0.2030  -0.1284 0.0458  -0.0182 20  TYR B CE2 
2425 C  CZ  . TYR B  21  ? 0.4174  0.2852 0.1808  -0.1564 0.0929  -0.0628 20  TYR B CZ  
2426 O  OH  . TYR B  21  ? 0.6864  0.3876 0.2612  -0.2537 0.1859  -0.1707 20  TYR B OH  
2427 N  N   A PRO B  22  ? 0.1976  0.1359 0.1757  -0.0209 0.0804  0.0023  21  PRO B N   
2428 N  N   B PRO B  22  ? 0.1966  0.2141 0.2124  -0.0793 0.0840  -0.0842 21  PRO B N   
2429 C  CA  A PRO B  22  ? 0.2479  0.2055 0.1932  -0.0529 0.1011  -0.0457 21  PRO B CA  
2430 C  CA  B PRO B  22  ? 0.2267  0.2030 0.2235  -0.0892 0.0923  -0.0829 21  PRO B CA  
2431 C  C   A PRO B  22  ? 0.1779  0.1650 0.2120  -0.0469 0.1198  -0.0456 21  PRO B C   
2432 C  C   B PRO B  22  ? 0.1872  0.1664 0.2497  -0.0484 0.0670  -0.0739 21  PRO B C   
2433 O  O   A PRO B  22  ? 0.2275  0.2084 0.1908  -0.0416 0.0967  -0.0658 21  PRO B O   
2434 O  O   B PRO B  22  ? 0.2266  0.1682 0.2497  -0.0605 0.0932  -0.0763 21  PRO B O   
2435 C  CB  A PRO B  22  ? 0.2472  0.2055 0.1930  -0.0005 0.1385  0.0272  21  PRO B CB  
2436 C  CB  B PRO B  22  ? 0.2380  0.1725 0.2852  -0.1044 0.1297  -0.0956 21  PRO B CB  
2437 C  CG  A PRO B  22  ? 0.2576  0.1492 0.2181  -0.0559 0.1333  -0.0431 21  PRO B CG  
2438 C  CG  B PRO B  22  ? 0.1876  0.2388 0.2827  -0.0233 0.0734  -0.1328 21  PRO B CG  
2439 C  CD  A PRO B  22  ? 0.2267  0.1409 0.2443  -0.0071 0.1399  -0.0370 21  PRO B CD  
2440 C  CD  B PRO B  22  ? 0.2332  0.2260 0.2303  -0.0814 0.1120  -0.0278 21  PRO B CD  
2441 N  N   . ILE B  23  ? 0.1835  0.1879 0.1775  -0.0447 0.0710  -0.0428 22  ILE B N   
2442 C  CA  . ILE B  23  ? 0.1689  0.2055 0.2054  -0.0414 0.0625  -0.0363 22  ILE B CA  
2443 C  C   . ILE B  23  ? 0.1562  0.1793 0.1736  -0.0291 0.0574  -0.0563 22  ILE B C   
2444 O  O   . ILE B  23  ? 0.1826  0.1883 0.1835  -0.0465 0.0622  -0.0642 22  ILE B O   
2445 C  CB  . ILE B  23  ? 0.1596  0.2095 0.1919  -0.0267 0.0357  -0.0208 22  ILE B CB  
2446 C  CG1 . ILE B  23  ? 0.2134  0.2418 0.1930  -0.0296 0.0454  -0.0110 22  ILE B CG1 
2447 C  CG2 . ILE B  23  ? 0.1398  0.1998 0.2651  -0.0266 0.0395  -0.0745 22  ILE B CG2 
2448 C  CD1 . ILE B  23  ? 0.2045  0.3459 0.2350  -0.0589 0.0294  -0.0294 22  ILE B CD1 
2449 N  N   . ALA B  24  ? 0.1585  0.1782 0.1991  -0.0238 0.0575  -0.0562 23  ALA B N   
2450 C  CA  . ALA B  24  ? 0.1596  0.1833 0.1725  -0.0340 0.0624  -0.0653 23  ALA B CA  
2451 C  C   . ALA B  24  ? 0.1738  0.1958 0.2084  -0.0087 0.0661  -0.0497 23  ALA B C   
2452 O  O   . ALA B  24  ? 0.1993  0.1980 0.2156  -0.0245 0.0905  -0.0630 23  ALA B O   
2453 C  CB  . ALA B  24  ? 0.1786  0.1991 0.1764  -0.0206 0.0403  -0.0331 23  ALA B CB  
2454 N  N   . ASN B  25  ? 0.2084  0.1750 0.2084  -0.0417 0.0549  -0.0702 24  ASN B N   
2455 C  CA  . ASN B  25  ? 0.2380  0.1905 0.2055  -0.0568 0.0507  -0.0674 24  ASN B CA  
2456 C  C   . ASN B  25  ? 0.2195  0.2238 0.1578  -0.0486 0.0615  -0.0721 24  ASN B C   
2457 O  O   . ASN B  25  ? 0.2490  0.2169 0.2296  -0.0728 0.0537  -0.0961 24  ASN B O   
2458 C  CB  . ASN B  25  ? 0.2957  0.1768 0.2727  -0.0631 0.0751  -0.0571 24  ASN B CB  
2459 C  CG  . ASN B  25  ? 0.3534  0.1650 0.3003  -0.0190 0.0361  -0.0526 24  ASN B CG  
2460 O  OD1 . ASN B  25  ? 0.4124  0.2120 0.3952  -0.0297 0.0279  0.0168  24  ASN B OD1 
2461 N  ND2 . ASN B  25  ? 0.2619  0.2978 0.3086  0.0354  0.0186  -0.0010 24  ASN B ND2 
2462 N  N   . GLY B  26  ? 0.1786  0.2106 0.2372  -0.0422 0.0425  -0.0380 25  GLY B N   
2463 C  CA  . GLY B  26  ? 0.1998  0.2350 0.1700  -0.0440 0.0624  -0.0621 25  GLY B CA  
2464 C  C   . GLY B  26  ? 0.1998  0.2350 0.1865  -0.0864 0.0826  -0.0772 25  GLY B C   
2465 O  O   . GLY B  26  ? 0.2009  0.2400 0.2048  -0.0652 0.0765  -0.0810 25  GLY B O   
2466 N  N   . ASN B  27  ? 0.2127  0.2134 0.1955  -0.0741 0.0181  -0.0795 26  ASN B N   
2467 C  CA  . ASN B  27  ? 0.2134  0.2310 0.1700  -0.0956 0.0072  -0.0636 26  ASN B CA  
2468 C  C   . ASN B  27  ? 0.1470  0.1793 0.2005  -0.0446 0.0489  -0.0873 26  ASN B C   
2469 O  O   . ASN B  27  ? 0.2073  0.2658 0.1941  -0.0983 0.0252  -0.1042 26  ASN B O   
2470 C  CB  . ASN B  27  ? 0.2619  0.3115 0.2618  -0.1795 0.0401  -0.1240 26  ASN B CB  
2471 C  CG  . ASN B  27  ? 0.2576  0.3219 0.2921  -0.1486 0.0639  -0.1547 26  ASN B CG  
2472 O  OD1 . ASN B  27  ? 0.3840  0.2518 0.3725  -0.1419 0.0917  -0.1159 26  ASN B OD1 
2473 N  ND2 . ASN B  27  ? 0.2860  0.3714 0.4893  -0.1759 0.0723  -0.1177 26  ASN B ND2 
2474 N  N   A ASN B  28  ? 0.1527  0.2066 0.1951  -0.0622 0.0148  -0.0930 27  ASN B N   
2475 N  N   B ASN B  28  ? 0.1409  0.2053 0.2192  -0.0638 0.0272  -0.1074 27  ASN B N   
2476 C  CA  A ASN B  28  ? 0.1294  0.1876 0.1772  -0.0344 0.0019  -0.0883 27  ASN B CA  
2477 C  CA  B ASN B  28  ? 0.1434  0.2156 0.1804  -0.0394 -0.0073 -0.0675 27  ASN B CA  
2478 C  C   A ASN B  28  ? 0.1416  0.1628 0.1124  -0.0615 0.0135  -0.0461 27  ASN B C   
2479 C  C   B ASN B  28  ? 0.1301  0.2213 0.1434  -0.0273 0.0094  -0.0856 27  ASN B C   
2480 O  O   A ASN B  28  ? 0.1190  0.1646 0.1005  -0.0521 0.0328  -0.0558 27  ASN B O   
2481 O  O   B ASN B  28  ? 0.1155  0.2117 0.2608  -0.0288 0.0126  -0.1099 27  ASN B O   
2482 C  CB  A ASN B  28  ? 0.1189  0.2354 0.1984  -0.0245 0.0036  -0.0643 27  ASN B CB  
2483 C  CB  B ASN B  28  ? 0.1527  0.2465 0.2192  -0.0220 0.0089  -0.0833 27  ASN B CB  
2484 C  CG  A ASN B  28  ? 0.1283  0.1883 0.1560  -0.0369 0.0281  -0.0729 27  ASN B CG  
2485 C  CG  B ASN B  28  ? 0.0894  0.3592 0.3078  -0.0502 -0.0033 -0.0849 27  ASN B CG  
2486 O  OD1 A ASN B  28  ? 0.0986  0.2623 0.3082  -0.0635 0.0059  -0.0789 27  ASN B OD1 
2487 O  OD1 B ASN B  28  ? 0.2780  0.4278 0.5422  -0.1064 -0.1272 -0.1687 27  ASN B OD1 
2488 N  ND2 A ASN B  28  ? 0.1280  0.2913 0.1463  0.0436  0.0168  -0.0854 27  ASN B ND2 
2489 N  ND2 B ASN B  28  ? 0.2451  0.2618 0.4023  0.0038  0.0253  -0.1482 27  ASN B ND2 
2490 N  N   . GLN B  29  ? 0.1330  0.1923 0.1585  -0.0343 0.0239  -0.0665 28  GLN B N   
2491 C  CA  . GLN B  29  ? 0.1106  0.1894 0.1362  -0.0445 0.0337  -0.0758 28  GLN B CA  
2492 C  C   . GLN B  29  ? 0.1326  0.1556 0.1430  -0.0344 0.0362  -0.0731 28  GLN B C   
2493 O  O   . GLN B  29  ? 0.1348  0.2116 0.1606  -0.0447 0.0335  -0.0972 28  GLN B O   
2494 C  CB  . GLN B  29  ? 0.1509  0.1456 0.1808  -0.0194 0.0458  -0.0392 28  GLN B CB  
2495 C  CG  . GLN B  29  ? 0.1574  0.1761 0.2064  -0.0306 0.0712  -0.0652 28  GLN B CG  
2496 C  CD  . GLN B  29  ? 0.1221  0.1797 0.1628  -0.0165 0.0270  -0.0641 28  GLN B CD  
2497 O  OE1 . GLN B  29  ? 0.1362  0.1703 0.1754  -0.0248 0.0473  -0.0491 28  GLN B OE1 
2498 N  NE2 . GLN B  29  ? 0.1323  0.1707 0.1628  -0.0251 0.0320  -0.0429 28  GLN B NE2 
2499 N  N   . SER B  30  ? 0.1155  0.1603 0.1373  -0.0269 0.0078  -0.0610 29  SER B N   
2500 C  CA  . SER B  30  ? 0.1208  0.1725 0.1270  -0.0497 0.0212  -0.0652 29  SER B CA  
2501 C  C   . SER B  30  ? 0.1254  0.1544 0.1276  -0.0329 0.0212  -0.0700 29  SER B C   
2502 O  O   . SER B  30  ? 0.1289  0.1729 0.1430  -0.0228 0.0245  -0.0542 29  SER B O   
2503 C  CB  . SER B  30  ? 0.1319  0.1703 0.1420  -0.0401 -0.0055 -0.0794 29  SER B CB  
2504 O  OG  . SER B  30  ? 0.1159  0.1817 0.1384  -0.0231 0.0130  -0.0695 29  SER B OG  
2505 N  N   . PRO B  31  ? 0.1190  0.1538 0.1260  -0.0106 0.0255  -0.0515 30  PRO B N   
2506 C  CA  . PRO B  31  ? 0.1084  0.1750 0.1172  -0.0345 0.0192  -0.0629 30  PRO B CA  
2507 C  C   . PRO B  31  ? 0.1151  0.1524 0.1402  -0.0093 0.0271  -0.0511 30  PRO B C   
2508 O  O   . PRO B  31  ? 0.1380  0.1502 0.1747  -0.0218 0.0356  -0.0646 30  PRO B O   
2509 C  CB  . PRO B  31  ? 0.1007  0.1588 0.1650  -0.0080 0.0089  -0.0652 30  PRO B CB  
2510 C  CG  . PRO B  31  ? 0.1073  0.1560 0.1659  -0.0103 0.0304  -0.0226 30  PRO B CG  
2511 C  CD  . PRO B  31  ? 0.0917  0.1779 0.1768  0.0068  0.0162  -0.0417 30  PRO B CD  
2512 N  N   . VAL B  32  ? 0.1276  0.1840 0.1355  -0.0137 0.0204  -0.0584 31  VAL B N   
2513 C  CA  . VAL B  32  ? 0.1312  0.1610 0.1617  -0.0168 0.0234  -0.0800 31  VAL B CA  
2514 C  C   . VAL B  32  ? 0.1232  0.1671 0.1535  -0.0129 0.0251  -0.0766 31  VAL B C   
2515 O  O   . VAL B  32  ? 0.1427  0.1782 0.1438  -0.0128 0.0271  -0.0697 31  VAL B O   
2516 C  CB  . VAL B  32  ? 0.1260  0.1984 0.1696  -0.0161 0.0173  -0.0611 31  VAL B CB  
2517 C  CG1 . VAL B  32  ? 0.1316  0.2372 0.1606  -0.0299 0.0490  -0.0859 31  VAL B CG1 
2518 C  CG2 . VAL B  32  ? 0.1610  0.1905 0.1641  -0.0262 0.0175  -0.0608 31  VAL B CG2 
2519 N  N   . ASP B  33  ? 0.1492  0.1782 0.1707  -0.0071 0.0357  -0.0841 32  ASP B N   
2520 C  CA  . ASP B  33  ? 0.1499  0.1793 0.1520  -0.0029 0.0215  -0.0697 32  ASP B CA  
2521 C  C   . ASP B  33  ? 0.1333  0.1897 0.1632  -0.0212 0.0346  -0.0675 32  ASP B C   
2522 O  O   . ASP B  33  ? 0.1567  0.2716 0.2375  -0.0606 -0.0088 -0.0434 32  ASP B O   
2523 C  CB  . ASP B  33  ? 0.1581  0.1872 0.1822  0.0095  0.0533  -0.0969 32  ASP B CB  
2524 C  CG  . ASP B  33  ? 0.1632  0.1738 0.1808  -0.0071 0.0229  -0.0854 32  ASP B CG  
2525 O  OD1 . ASP B  33  ? 0.1571  0.2009 0.1797  -0.0220 0.0424  -0.0910 32  ASP B OD1 
2526 O  OD2 . ASP B  33  ? 0.2346  0.2622 0.2344  -0.0760 0.0901  -0.1452 32  ASP B OD2 
2527 N  N   . ILE B  34  ? 0.1621  0.2168 0.1248  -0.0198 0.0145  -0.0637 33  ILE B N   
2528 C  CA  . ILE B  34  ? 0.1714  0.2077 0.1254  -0.0117 0.0177  -0.0695 33  ILE B CA  
2529 C  C   . ILE B  34  ? 0.1294  0.2375 0.1641  -0.0320 0.0209  -0.0982 33  ILE B C   
2530 O  O   . ILE B  34  ? 0.1384  0.2521 0.1574  -0.0233 0.0206  -0.1008 33  ILE B O   
2531 C  CB  . ILE B  34  ? 0.1617  0.2242 0.1177  -0.0049 0.0074  -0.0569 33  ILE B CB  
2532 C  CG1 . ILE B  34  ? 0.1738  0.1962 0.1386  -0.0113 0.0232  -0.0623 33  ILE B CG1 
2533 C  CG2 . ILE B  34  ? 0.1894  0.2795 0.1441  0.0260  0.0027  -0.0446 33  ILE B CG2 
2534 C  CD1 . ILE B  34  ? 0.2484  0.2064 0.1621  -0.0217 0.0303  -0.0610 33  ILE B CD1 
2535 N  N   . LYS B  35  ? 0.1757  0.2601 0.1872  -0.0353 0.0144  -0.1222 34  LYS B N   
2536 C  CA  . LYS B  35  ? 0.2321  0.2655 0.2055  -0.0414 0.0375  -0.1238 34  LYS B CA  
2537 C  C   . LYS B  35  ? 0.1919  0.2672 0.1894  -0.0079 -0.0069 -0.1259 34  LYS B C   
2538 O  O   . LYS B  35  ? 0.1914  0.3118 0.1725  -0.0326 0.0113  -0.1182 34  LYS B O   
2539 C  CB  . LYS B  35  ? 0.3531  0.2643 0.2816  -0.1324 0.0892  -0.1568 34  LYS B CB  
2540 C  CG  . LYS B  35  ? 0.4597  0.2643 0.5489  -0.0655 0.0922  -0.1910 34  LYS B CG  
2541 C  CD  . LYS B  35  ? 0.3352  0.3625 0.8707  -0.0966 -0.0272 -0.0168 34  LYS B CD  
2542 N  N   . THR B  36  ? 0.2325  0.2469 0.1797  -0.0196 0.0074  -0.0894 35  THR B N   
2543 C  CA  . THR B  36  ? 0.1987  0.2469 0.1980  -0.0206 0.0085  -0.1099 35  THR B CA  
2544 C  C   . THR B  36  ? 0.2381  0.2892 0.1826  -0.0380 -0.0170 -0.0576 35  THR B C   
2545 O  O   . THR B  36  ? 0.3639  0.3183 0.2590  0.0290  -0.1027 -0.0861 35  THR B O   
2546 C  CB  . THR B  36  ? 0.2282  0.2860 0.1923  -0.0247 0.0020  -0.0898 35  THR B CB  
2547 O  OG1 . THR B  36  ? 0.1991  0.3072 0.2009  -0.0347 0.0103  -0.0789 35  THR B OG1 
2548 C  CG2 . THR B  36  ? 0.2752  0.2619 0.2827  0.0168  -0.0261 -0.1183 35  THR B CG2 
2549 N  N   . SER B  37  ? 0.2275  0.3132 0.2034  -0.0197 0.0072  -0.1487 36  SER B N   
2550 C  CA  . SER B  37  ? 0.2113  0.3675 0.2242  -0.0414 -0.0158 -0.1368 36  SER B CA  
2551 C  C   . SER B  37  ? 0.2260  0.3323 0.2185  -0.0571 0.0157  -0.1609 36  SER B C   
2552 O  O   . SER B  37  ? 0.2393  0.4778 0.2230  -0.0510 -0.0044 -0.1905 36  SER B O   
2553 C  CB  . SER B  37  ? 0.3169  0.3883 0.2723  -0.0197 -0.0308 -0.1896 36  SER B CB  
2554 O  OG  . SER B  37  ? 0.2946  0.3937 0.3693  -0.0041 -0.0466 -0.2257 36  SER B OG  
2555 N  N   A GLU B  38  ? 0.1951  0.3413 0.2346  -0.0623 0.0285  -0.1835 37  GLU B N   
2556 N  N   B GLU B  38  ? 0.2134  0.3068 0.2138  -0.0389 0.0115  -0.1588 37  GLU B N   
2557 C  CA  A GLU B  38  ? 0.2170  0.3283 0.2662  -0.0692 0.0380  -0.1644 37  GLU B CA  
2558 C  CA  B GLU B  38  ? 0.2030  0.2691 0.1797  -0.0253 -0.0398 -0.1140 37  GLU B CA  
2559 C  C   A GLU B  38  ? 0.2372  0.3114 0.2249  -0.0827 -0.0261 -0.1947 37  GLU B C   
2560 C  C   B GLU B  38  ? 0.2073  0.2741 0.2590  -0.0201 -0.0231 -0.0723 37  GLU B C   
2561 O  O   A GLU B  38  ? 0.2143  0.4543 0.3100  -0.0592 0.0087  -0.2231 37  GLU B O   
2562 O  O   B GLU B  38  ? 0.1747  0.2867 0.2354  -0.0460 -0.0364 -0.0735 37  GLU B O   
2563 C  CB  A GLU B  38  ? 0.4372  0.3255 0.3333  -0.1225 -0.0384 -0.1639 37  GLU B CB  
2564 C  CB  B GLU B  38  ? 0.1958  0.3215 0.2213  0.0366  0.0130  -0.0886 37  GLU B CB  
2565 C  CG  A GLU B  38  ? 0.5207  0.2939 0.3980  -0.0982 0.0697  -0.0960 37  GLU B CG  
2566 C  CG  B GLU B  38  ? 0.1958  0.2576 0.3161  -0.0264 -0.0431 -0.1802 37  GLU B CG  
2567 C  CD  A GLU B  38  ? 0.5037  0.5104 0.5478  -0.0501 0.3753  0.0468  37  GLU B CD  
2568 C  CD  B GLU B  38  ? 0.3667  0.3495 0.2590  -0.1188 0.0114  -0.1461 37  GLU B CD  
2569 O  OE1 A GLU B  38  ? 0.5799  0.5851 0.6164  0.1925  0.4262  0.1942  37  GLU B OE1 
2570 O  OE1 B GLU B  38  ? 0.3664  0.3503 0.2551  -0.1609 0.0238  -0.1460 37  GLU B OE1 
2571 O  OE2 A GLU B  38  ? 0.8497  0.5999 0.6294  0.1202  0.2120  0.0502  37  GLU B OE2 
2572 O  OE2 B GLU B  38  ? 0.2781  0.4659 0.3600  -0.0120 -0.0196 -0.0747 37  GLU B OE2 
2573 N  N   . THR B  39  ? 0.2055  0.2691 0.2199  -0.0306 0.0044  -0.1215 38  THR B N   
2574 C  CA  . THR B  39  ? 0.2346  0.2827 0.2117  -0.0182 -0.0447 -0.1172 38  THR B CA  
2575 C  C   . THR B  39  ? 0.2813  0.4092 0.1585  -0.0516 -0.0399 -0.1296 38  THR B C   
2576 O  O   . THR B  39  ? 0.3370  0.5353 0.1445  -0.0421 -0.0237 -0.1271 38  THR B O   
2577 C  CB  . THR B  39  ? 0.2109  0.3115 0.1574  -0.0643 0.0203  -0.1144 38  THR B CB  
2578 O  OG1 . THR B  39  ? 0.2494  0.3190 0.1775  -0.0758 0.0239  -0.1038 38  THR B OG1 
2579 C  CG2 . THR B  39  ? 0.2357  0.2691 0.1535  -0.0096 0.0046  -0.0977 38  THR B CG2 
2580 N  N   . LYS B  40  ? 0.2608  0.3790 0.2034  -0.0279 -0.0512 -0.0754 39  LYS B N   
2581 C  CA  . LYS B  40  ? 0.2249  0.4310 0.1668  0.0059  -0.0274 -0.0578 39  LYS B CA  
2582 C  C   . LYS B  40  ? 0.2931  0.3768 0.2052  0.0753  -0.0469 -0.1029 39  LYS B C   
2583 O  O   . LYS B  40  ? 0.2490  0.3707 0.1919  -0.0435 -0.0355 -0.1100 39  LYS B O   
2584 C  CB  . LYS B  40  ? 0.2637  0.4260 0.3862  -0.0501 -0.0509 -0.1377 39  LYS B CB  
2585 C  CG  . LYS B  40  ? 0.3704  0.4608 0.4311  -0.0240 -0.0784 -0.2052 39  LYS B CG  
2586 N  N   . HIS B  41  ? 0.4288  0.3934 0.1876  -0.0617 -0.0729 -0.1310 40  HIS B N   
2587 C  CA  . HIS B  41  ? 0.4827  0.4102 0.1599  -0.0320 -0.1163 -0.1420 40  HIS B CA  
2588 C  C   . HIS B  41  ? 0.4379  0.3991 0.3251  0.2063  -0.0100 -0.0279 40  HIS B C   
2589 O  O   . HIS B  41  ? 2.8543  1.6685 3.0267  -1.2747 -2.4026 1.0383  40  HIS B O   
2590 C  CB  . HIS B  41  ? 0.3222  0.6406 0.1560  0.0640  -0.0425 -0.1727 40  HIS B CB  
2591 C  CG  . HIS B  41  ? 0.4379  0.5288 0.4128  0.1038  -0.2292 -0.1306 40  HIS B CG  
2592 N  ND1 . HIS B  41  ? 0.4092  0.6215 0.3110  -0.0846 -0.1865 0.0190  40  HIS B ND1 
2593 C  CD2 . HIS B  41  ? 1.1790  0.8033 0.3955  -0.0367 -0.3779 0.0227  40  HIS B CD2 
2594 C  CE1 . HIS B  41  ? 0.3384  0.6973 0.2461  -0.0342 -0.1150 0.0250  40  HIS B CE1 
2595 N  NE2 . HIS B  41  ? 1.0082  0.8114 0.3510  0.1654  -0.3414 -0.0126 40  HIS B NE2 
2596 N  N   . ASP B  42  ? 0.2382  0.3649 0.2160  -0.0086 -0.0177 -0.0445 41  ASP B N   
2597 C  CA  . ASP B  42  ? 0.2443  0.3826 0.1844  0.0074  -0.0669 -0.0913 41  ASP B CA  
2598 C  C   . ASP B  42  ? 0.3786  0.4016 0.1930  -0.0501 -0.0732 -0.0505 41  ASP B C   
2599 O  O   . ASP B  42  ? 0.3419  0.4253 0.2037  0.0351  -0.0924 -0.0582 41  ASP B O   
2600 C  CB  . ASP B  42  ? 0.2734  0.4415 0.2048  0.0084  -0.0661 -0.1400 41  ASP B CB  
2601 C  CG  . ASP B  42  ? 0.2389  0.4605 0.2752  -0.0341 -0.1087 -0.1082 41  ASP B CG  
2602 O  OD1 . ASP B  42  ? 0.2745  0.4911 0.3215  -0.0182 -0.1368 -0.0653 41  ASP B OD1 
2603 O  OD2 . ASP B  42  ? 0.3790  0.7353 0.3276  0.0450  -0.0523 0.0117  41  ASP B OD2 
2604 N  N   . THR B  43  ? 0.4440  0.6788 0.2669  -0.0087 -0.1903 -0.0690 42  THR B N   
2605 C  CA  . THR B  43  ? 0.6699  0.6520 0.1732  -0.0245 -0.0058 -0.1411 42  THR B CA  
2606 C  C   . THR B  43  ? 0.4148  0.5869 0.1894  0.0688  -0.1268 0.0528  42  THR B C   
2607 O  O   . THR B  43  ? 0.8069  0.5565 0.3527  -0.0756 -0.3195 0.0816  42  THR B O   
2608 C  CB  . THR B  43  ? 1.4782  0.9837 0.2658  0.1174  -0.2330 0.0298  42  THR B CB  
2609 O  OG1 . THR B  43  ? 2.0821  1.7470 0.4598  -0.0992 -0.7661 -0.3673 42  THR B OG1 
2610 C  CG2 . THR B  43  ? 1.6595  0.8007 0.2895  0.0305  -0.1267 0.0384  42  THR B CG2 
2611 N  N   . SER B  44  ? 0.3710  0.4641 0.2321  -0.0167 -0.1412 -0.0055 43  SER B N   
2612 C  CA  . SER B  44  ? 0.4009  0.5224 0.3194  0.0117  -0.1685 -0.0879 43  SER B CA  
2613 C  C   . SER B  44  ? 0.3147  0.4604 0.2928  0.0449  -0.0923 -0.0897 43  SER B C   
2614 O  O   . SER B  44  ? 0.3165  0.5021 0.3984  0.0691  -0.0859 -0.0961 43  SER B O   
2615 C  CB  . SER B  44  ? 0.4712  0.8526 0.5104  -0.0916 -0.3018 -0.0144 43  SER B CB  
2616 O  OG  . SER B  44  ? 0.2773  0.6767 0.3872  0.0328  -0.0986 -0.1854 43  SER B OG  
2617 N  N   . LEU B  45  ? 0.3136  0.4188 0.2727  0.0380  -0.1430 -0.0729 44  LEU B N   
2618 C  CA  . LEU B  45  ? 0.3370  0.4462 0.1876  -0.0152 -0.1262 -0.0264 44  LEU B CA  
2619 C  C   . LEU B  45  ? 0.4217  0.4277 0.2071  -0.0829 -0.0826 -0.1044 44  LEU B C   
2620 O  O   . LEU B  45  ? 0.7569  0.6375 0.2350  -0.2373 0.0000  -0.0816 44  LEU B O   
2621 C  CB  . LEU B  45  ? 0.2895  0.4119 0.2726  0.0038  -0.1037 -0.1267 44  LEU B CB  
2622 C  CG  . LEU B  45  ? 0.2064  0.3840 0.2411  0.0110  -0.0589 -0.1240 44  LEU B CG  
2623 C  CD1 . LEU B  45  ? 0.2285  0.4041 0.2059  0.0074  -0.0513 -0.1156 44  LEU B CD1 
2624 C  CD2 . LEU B  45  ? 0.2045  0.3990 0.1919  0.0060  -0.0482 -0.0880 44  LEU B CD2 
2625 N  N   . LYS B  46  ? 0.3092  0.3898 0.3035  0.0619  -0.1159 -0.1018 45  LYS B N   
2626 C  CA  . LYS B  46  ? 0.2809  0.4440 0.2477  0.0199  -0.1296 0.0080  45  LYS B CA  
2627 C  C   . LYS B  46  ? 0.2529  0.3898 0.1786  0.0126  -0.0813 0.0001  45  LYS B C   
2628 O  O   . LYS B  46  ? 0.3057  0.3682 0.1955  0.0460  -0.0977 -0.0361 45  LYS B O   
2629 C  CB  . LYS B  46  ? 0.3251  0.3610 0.3679  0.0499  -0.1634 -0.0464 45  LYS B CB  
2630 C  CG  . LYS B  46  ? 0.3316  0.5290 0.5484  0.0053  -0.1881 0.0627  45  LYS B CG  
2631 N  N   . PRO B  47  ? 0.3276  0.4275 0.1811  0.0141  -0.1126 0.0151  46  PRO B N   
2632 C  CA  . PRO B  47  ? 0.2928  0.3776 0.1793  -0.0245 -0.0639 -0.0498 46  PRO B CA  
2633 C  C   . PRO B  47  ? 0.2888  0.3973 0.1535  0.0230  -0.0701 0.0147  46  PRO B C   
2634 O  O   . PRO B  47  ? 0.2720  0.3621 0.2511  0.0346  -0.0839 -0.0320 46  PRO B O   
2635 C  CB  . PRO B  47  ? 0.3251  0.4713 0.2030  -0.0868 -0.0740 -0.0121 46  PRO B CB  
2636 C  CG  . PRO B  47  ? 0.3901  0.4113 0.2303  -0.0732 -0.1294 -0.0468 46  PRO B CG  
2637 C  CD  . PRO B  47  ? 0.3776  0.3589 0.2199  -0.0791 -0.1258 0.0678  46  PRO B CD  
2638 N  N   . ILE B  48  ? 0.3021  0.3485 0.1786  0.0774  -0.1104 -0.0729 47  ILE B N   
2639 C  CA  . ILE B  48  ? 0.3783  0.3273 0.1865  0.1245  -0.1018 -0.0965 47  ILE B CA  
2640 C  C   . ILE B  48  ? 0.3255  0.3327 0.1659  0.0409  -0.0617 -0.0394 47  ILE B C   
2641 O  O   . ILE B  48  ? 0.3707  0.4899 0.2156  0.0362  -0.0664 -0.0096 47  ILE B O   
2642 C  CB  . ILE B  48  ? 0.5302  0.3437 0.2339  0.1483  -0.2034 -0.0903 47  ILE B CB  
2643 C  CG1 . ILE B  48  ? 0.6365  0.3348 0.1980  0.1699  -0.0939 -0.0394 47  ILE B CG1 
2644 C  CG2 . ILE B  48  ? 0.3204  0.3585 0.2037  0.0905  -0.1081 -0.1070 47  ILE B CG2 
2645 C  CD1 . ILE B  48  ? 0.5213  0.3632 0.2220  -0.0221 -0.1357 -0.0416 47  ILE B CD1 
2646 N  N   . SER B  49  ? 0.3154  0.2691 0.1664  0.0526  -0.0923 -0.0480 48  SER B N   
2647 C  CA  . SER B  49  ? 0.3646  0.2870 0.1919  0.0314  -0.1138 -0.0600 48  SER B CA  
2648 C  C   . SER B  49  ? 0.2995  0.2698 0.1854  0.0050  -0.0952 -0.0253 48  SER B C   
2649 O  O   . SER B  49  ? 0.2604  0.3801 0.2380  0.0032  -0.0948 -0.0674 48  SER B O   
2650 C  CB  . SER B  49  ? 0.4820  0.2752 0.2626  0.1771  -0.1969 -0.0741 48  SER B CB  
2651 O  OG  . SER B  49  ? 0.4796  0.2910 0.4867  0.1119  -0.2215 -0.0234 48  SER B OG  
2652 N  N   . VAL B  50  ? 0.2546  0.2450 0.1883  0.0709  -0.0850 -0.0342 49  VAL B N   
2653 C  CA  . VAL B  50  ? 0.2134  0.2411 0.1754  0.0688  -0.0596 -0.0400 49  VAL B CA  
2654 C  C   . VAL B  50  ? 0.2125  0.2572 0.1926  0.0567  -0.0768 0.0026  49  VAL B C   
2655 O  O   . VAL B  50  ? 0.2568  0.2379 0.1779  0.0480  -0.0515 -0.0238 49  VAL B O   
2656 C  CB  . VAL B  50  ? 0.2561  0.2108 0.2441  0.0390  -0.0992 -0.0124 49  VAL B CB  
2657 C  CG1 . VAL B  50  ? 0.2971  0.2127 0.2622  0.0168  -0.1063 0.0242  49  VAL B CG1 
2658 C  CG2 . VAL B  50  ? 0.2106  0.3230 0.4670  0.0370  -0.0851 0.0258  49  VAL B CG2 
2659 N  N   . SER B  51  ? 0.2651  0.2222 0.1800  0.0516  -0.0526 -0.0287 50  SER B N   
2660 C  CA  . SER B  51  ? 0.3068  0.2490 0.1973  0.0635  -0.0943 0.0046  50  SER B CA  
2661 C  C   . SER B  51  ? 0.2328  0.2063 0.1689  0.0033  -0.0543 -0.0032 50  SER B C   
2662 O  O   . SER B  51  ? 0.2090  0.2257 0.2125  0.0011  -0.0455 -0.0119 50  SER B O   
2663 C  CB  . SER B  51  ? 0.4257  0.2354 0.2407  0.1270  -0.1116 -0.0227 50  SER B CB  
2664 O  OG  . SER B  51  ? 0.4929  0.2676 0.2751  0.1234  -0.0512 -0.0013 50  SER B OG  
2665 N  N   . TYR B  52  ? 0.2337  0.1944 0.2278  0.0297  -0.0718 -0.0423 51  TYR B N   
2666 C  CA  . TYR B  52  ? 0.2163  0.1833 0.1847  0.0394  -0.0414 -0.0651 51  TYR B CA  
2667 C  C   . TYR B  52  ? 0.2558  0.1639 0.2163  0.0092  -0.0111 -0.0013 51  TYR B C   
2668 O  O   . TYR B  52  ? 0.3492  0.2335 0.3237  -0.0488 0.0888  -0.1143 51  TYR B O   
2669 C  CB  . TYR B  52  ? 0.1764  0.2084 0.1822  0.0324  -0.0402 -0.0578 51  TYR B CB  
2670 C  CG  . TYR B  52  ? 0.1854  0.2041 0.1337  0.0250  -0.0395 -0.0361 51  TYR B CG  
2671 C  CD1 . TYR B  52  ? 0.1761  0.2034 0.1560  0.0346  -0.0478 -0.0420 51  TYR B CD1 
2672 C  CD2 . TYR B  52  ? 0.1854  0.1887 0.1599  0.0294  -0.0440 -0.0316 51  TYR B CD2 
2673 C  CE1 . TYR B  52  ? 0.1854  0.2041 0.1606  0.0644  -0.0679 -0.0666 51  TYR B CE1 
2674 C  CE2 . TYR B  52  ? 0.1624  0.1951 0.1402  0.0201  -0.0447 -0.0122 51  TYR B CE2 
2675 C  CZ  . TYR B  52  ? 0.1621  0.1822 0.1448  0.0405  -0.0561 -0.0190 51  TYR B CZ  
2676 O  OH  . TYR B  52  ? 0.1840  0.1786 0.1596  0.0390  -0.0386 -0.0277 51  TYR B OH  
2677 N  N   . ASN B  53  ? 0.1987  0.1944 0.1567  0.0396  -0.0686 -0.0428 52  ASN B N   
2678 C  CA  . ASN B  53  ? 0.2178  0.2048 0.1958  0.0613  -0.0845 -0.0657 52  ASN B CA  
2679 C  C   . ASN B  53  ? 0.1869  0.1502 0.1764  0.0100  -0.0266 -0.0095 52  ASN B C   
2680 O  O   . ASN B  53  ? 0.1955  0.1423 0.1596  0.0146  -0.0190 -0.0207 52  ASN B O   
2681 C  CB  . ASN B  53  ? 0.2557  0.1926 0.2282  0.0652  -0.0737 -0.0588 52  ASN B CB  
2682 C  CG  . ASN B  53  ? 0.2615  0.1901 0.2106  0.0549  -0.0802 -0.0201 52  ASN B CG  
2683 O  OD1 . ASN B  53  ? 0.2849  0.1718 0.1976  0.0320  -0.0748 -0.0183 52  ASN B OD1 
2684 N  ND2 . ASN B  53  ? 0.2801  0.2285 0.2608  0.1042  -0.0585 0.0015  52  ASN B ND2 
2685 N  N   . PRO B  54  ? 0.1858  0.1562 0.1506  0.0134  -0.0223 -0.0124 53  PRO B N   
2686 C  CA  . PRO B  54  ? 0.2045  0.1948 0.1170  -0.0074 -0.0220 -0.0050 53  PRO B CA  
2687 C  C   . PRO B  54  ? 0.2045  0.1405 0.1319  -0.0144 -0.0249 -0.0131 53  PRO B C   
2688 O  O   . PRO B  54  ? 0.1685  0.1624 0.1274  0.0013  -0.0096 0.0003  53  PRO B O   
2689 C  CB  . PRO B  54  ? 0.2389  0.2071 0.1542  -0.0292 -0.0136 0.0370  53  PRO B CB  
2690 C  CG  . PRO B  54  ? 0.2544  0.2030 0.2318  -0.0422 -0.0306 0.0538  53  PRO B CG  
2691 C  CD  . PRO B  54  ? 0.2597  0.1639 0.1650  -0.0067 -0.0041 0.0124  53  PRO B CD  
2692 N  N   . ALA B  55  ? 0.2228  0.1465 0.1488  0.0135  -0.0055 -0.0319 54  ALA B N   
2693 C  CA  . ALA B  55  ? 0.2597  0.1646 0.1553  0.0196  0.0134  0.0063  54  ALA B CA  
2694 C  C   . ALA B  55  ? 0.1797  0.1621 0.1412  -0.0077 0.0008  -0.0107 54  ALA B C   
2695 O  O   . ALA B  55  ? 0.2265  0.1786 0.1603  0.0039  0.0122  -0.0214 54  ALA B O   
2696 C  CB  . ALA B  55  ? 0.3294  0.1736 0.2149  0.0762  0.0157  -0.0203 54  ALA B CB  
2697 N  N   . THR B  56  ? 0.1887  0.1344 0.1567  0.0212  -0.0300 -0.0122 55  THR B N   
2698 C  CA  . THR B  56  ? 0.1495  0.1416 0.1434  0.0304  -0.0225 -0.0099 55  THR B CA  
2699 C  C   . THR B  56  ? 0.1395  0.1289 0.1073  0.0084  -0.0245 -0.0157 55  THR B C   
2700 O  O   . THR B  56  ? 0.1234  0.1520 0.1386  0.0053  0.0013  -0.0039 55  THR B O   
2701 C  CB  . THR B  56  ? 0.1377  0.1682 0.1829  0.0513  -0.0458 -0.0310 55  THR B CB  
2702 O  OG1 . THR B  56  ? 0.1384  0.1614 0.1671  0.0288  -0.0324 -0.0245 55  THR B OG1 
2703 C  CG2 . THR B  56  ? 0.1549  0.2077 0.1840  0.0518  -0.0532 -0.0151 55  THR B CG2 
2704 N  N   . ALA B  57  ? 0.1270  0.1319 0.1243  0.0103  -0.0153 -0.0283 56  ALA B N   
2705 C  CA  . ALA B  57  ? 0.1287  0.1377 0.1163  0.0075  -0.0157 -0.0179 56  ALA B CA  
2706 C  C   . ALA B  57  ? 0.1054  0.1181 0.1257  0.0058  0.0016  -0.0186 56  ALA B C   
2707 O  O   . ALA B  57  ? 0.1395  0.1115 0.1205  0.0144  0.0009  -0.0110 56  ALA B O   
2708 C  CB  . ALA B  57  ? 0.1163  0.1693 0.1234  -0.0015 0.0219  -0.0263 56  ALA B CB  
2709 N  N   A LYS B  58  ? 0.1005  0.1298 0.1194  -0.0006 -0.0153 -0.0034 57  LYS B N   
2710 N  N   B LYS B  58  ? 0.1107  0.1259 0.1274  0.0027  0.0002  -0.0029 57  LYS B N   
2711 C  CA  A LYS B  58  ? 0.1120  0.1682 0.1040  0.0029  0.0105  -0.0022 57  LYS B CA  
2712 C  CA  B LYS B  58  ? 0.1225  0.1470 0.1438  0.0464  0.0277  -0.0036 57  LYS B CA  
2713 C  C   A LYS B  58  ? 0.1125  0.1344 0.0971  -0.0005 0.0218  0.0012  57  LYS B C   
2714 C  C   B LYS B  58  ? 0.1093  0.1298 0.1144  -0.0012 0.0195  0.0031  57  LYS B C   
2715 O  O   A LYS B  58  ? 0.1190  0.1477 0.1470  0.0018  0.0125  -0.0464 57  LYS B O   
2716 O  O   B LYS B  58  ? 0.1289  0.1416 0.1553  0.0088  0.0126  -0.0456 57  LYS B O   
2717 C  CB  A LYS B  58  ? 0.1242  0.1703 0.1596  -0.0130 0.0214  0.0287  57  LYS B CB  
2718 C  CB  B LYS B  58  ? 0.0864  0.2619 0.1966  0.0703  0.0312  0.0515  57  LYS B CB  
2719 C  CG  A LYS B  58  ? 0.0858  0.1869 0.1488  -0.0104 0.0406  -0.0568 57  LYS B CG  
2720 C  CG  B LYS B  58  ? 0.1732  0.1772 0.1937  0.0895  0.0844  0.0446  57  LYS B CG  
2721 C  CD  A LYS B  58  ? 0.1067  0.1221 0.1962  -0.0144 0.0750  -0.0311 57  LYS B CD  
2722 C  CD  B LYS B  58  ? 0.1923  0.2655 0.2472  0.0729  0.0308  -0.0192 57  LYS B CD  
2723 C  CE  A LYS B  58  ? 0.1307  0.2073 0.2967  -0.0589 0.0348  -0.0048 57  LYS B CE  
2724 C  CE  B LYS B  58  ? 0.1872  0.3291 0.2362  0.0381  0.0466  0.0432  57  LYS B CE  
2725 N  NZ  A LYS B  58  ? 0.1599  0.3689 0.3071  -0.0026 0.0523  0.0399  57  LYS B NZ  
2726 N  NZ  B LYS B  58  ? 0.1571  0.3718 0.3039  -0.0812 0.0078  0.0546  57  LYS B NZ  
2727 N  N   . GLU B  59  ? 0.1063  0.1217 0.1039  0.0154  0.0026  -0.0124 58  GLU B N   
2728 C  CA  . GLU B  59  ? 0.1241  0.1212 0.0946  0.0170  0.0086  -0.0198 58  GLU B CA  
2729 C  C   . GLU B  59  ? 0.1002  0.1108 0.0871  -0.0074 -0.0038 -0.0287 58  GLU B C   
2730 O  O   . GLU B  59  ? 0.1266  0.1373 0.1326  0.0153  -0.0372 -0.0508 58  GLU B O   
2731 C  CB  . GLU B  59  ? 0.1445  0.1646 0.0838  0.0299  0.0301  0.0033  58  GLU B CB  
2732 C  CG  . GLU B  59  ? 0.1538  0.1901 0.1186  0.0091  0.0130  0.0173  58  GLU B CG  
2733 C  CD  . GLU B  59  ? 0.1750  0.1800 0.1120  -0.0332 0.0204  -0.0053 58  GLU B CD  
2734 O  OE1 . GLU B  59  ? 0.1919  0.3064 0.1186  -0.0046 0.0296  -0.0359 58  GLU B OE1 
2735 O  OE2 . GLU B  59  ? 0.1854  0.2267 0.1592  -0.0419 0.0209  -0.0176 58  GLU B OE2 
2736 N  N   . ILE B  60  ? 0.0928  0.1111 0.0924  0.0098  -0.0049 -0.0199 59  ILE B N   
2737 C  CA  . ILE B  60  ? 0.0970  0.1190 0.0873  0.0107  0.0069  -0.0082 59  ILE B CA  
2738 C  C   . ILE B  60  ? 0.0829  0.1093 0.0752  0.0000  0.0022  -0.0218 59  ILE B C   
2739 O  O   . ILE B  60  ? 0.1144  0.1337 0.0715  -0.0076 0.0029  -0.0289 59  ILE B O   
2740 C  CB  . ILE B  60  ? 0.0891  0.1152 0.0853  -0.0027 0.0035  -0.0229 59  ILE B CB  
2741 C  CG1 . ILE B  60  ? 0.0996  0.1226 0.1020  0.0058  0.0195  -0.0168 59  ILE B CG1 
2742 C  CG2 . ILE B  60  ? 0.1048  0.1384 0.1084  -0.0050 -0.0148 -0.0420 59  ILE B CG2 
2743 C  CD1 . ILE B  60  ? 0.1221  0.1384 0.1244  0.0015  0.0342  -0.0185 59  ILE B CD1 
2744 N  N   . ILE B  61  ? 0.0829  0.1057 0.0795  0.0035  0.0142  -0.0084 60  ILE B N   
2745 C  CA  . ILE B  61  ? 0.0908  0.1257 0.0794  0.0103  0.0174  -0.0133 60  ILE B CA  
2746 C  C   . ILE B  61  ? 0.0749  0.1204 0.0641  -0.0037 0.0049  -0.0205 60  ILE B C   
2747 O  O   . ILE B  61  ? 0.0979  0.1267 0.0671  0.0066  0.0004  -0.0259 60  ILE B O   
2748 C  CB  . ILE B  61  ? 0.0926  0.1448 0.1063  0.0179  0.0274  0.0115  60  ILE B CB  
2749 C  CG1 . ILE B  61  ? 0.1102  0.1628 0.1527  0.0264  0.0231  -0.0179 60  ILE B CG1 
2750 C  CG2 . ILE B  61  ? 0.1120  0.1793 0.1267  0.0081  0.0305  0.0150  60  ILE B CG2 
2751 C  CD1 . ILE B  61  ? 0.1283  0.2425 0.1980  0.0124  -0.0165 -0.0309 60  ILE B CD1 
2752 N  N   . ASN B  62  ? 0.0917  0.1234 0.0725  -0.0023 -0.0003 -0.0092 61  ASN B N   
2753 C  CA  . ASN B  62  ? 0.0950  0.1195 0.0803  0.0041  -0.0004 -0.0127 61  ASN B CA  
2754 C  C   . ASN B  62  ? 0.0786  0.1386 0.0633  0.0115  -0.0095 -0.0144 61  ASN B C   
2755 O  O   . ASN B  62  ? 0.1056  0.1509 0.0655  0.0097  0.0027  -0.0133 61  ASN B O   
2756 C  CB  . ASN B  62  ? 0.0891  0.1398 0.0914  0.0021  -0.0096 -0.0263 61  ASN B CB  
2757 C  CG  . ASN B  62  ? 0.0964  0.1298 0.0619  -0.0075 0.0018  -0.0209 61  ASN B CG  
2758 O  OD1 . ASN B  62  ? 0.0925  0.1427 0.1067  0.0021  -0.0030 -0.0279 61  ASN B OD1 
2759 N  ND2 . ASN B  62  ? 0.0768  0.1621 0.0919  0.0004  -0.0077 -0.0234 61  ASN B ND2 
2760 N  N   . VAL B  63  ? 0.0917  0.1230 0.0768  0.0027  -0.0005 -0.0113 62  VAL B N   
2761 C  CA  . VAL B  63  ? 0.1029  0.1384 0.1036  -0.0195 -0.0010 -0.0116 62  VAL B CA  
2762 C  C   . VAL B  63  ? 0.1118  0.1333 0.0917  -0.0154 0.0107  -0.0054 62  VAL B C   
2763 O  O   . VAL B  63  ? 0.1067  0.1492 0.1553  -0.0239 0.0175  -0.0073 62  VAL B O   
2764 C  CB  . VAL B  63  ? 0.0926  0.1448 0.1169  0.0034  0.0000  -0.0181 62  VAL B CB  
2765 C  CG1 . VAL B  63  ? 0.1053  0.1524 0.1786  0.0138  -0.0341 -0.0205 62  VAL B CG1 
2766 C  CG2 . VAL B  63  ? 0.1380  0.1689 0.1082  -0.0034 -0.0179 -0.0220 62  VAL B CG2 
2767 N  N   . GLY B  64  ? 0.0980  0.1326 0.0882  -0.0018 0.0013  -0.0084 63  GLY B N   
2768 C  CA  . GLY B  64  ? 0.1448  0.1169 0.0900  0.0044  0.0018  -0.0041 63  GLY B CA  
2769 C  C   . GLY B  64  ? 0.1160  0.1319 0.0890  0.0013  -0.0106 0.0037  63  GLY B C   
2770 O  O   . GLY B  64  ? 0.1398  0.1861 0.1366  0.0222  -0.0240 -0.0390 63  GLY B O   
2771 N  N   . HIS B  65  ? 0.1206  0.1247 0.0791  -0.0039 0.0055  -0.0088 64  HIS B N   
2772 C  CA  . HIS B  65  ? 0.1416  0.1156 0.0879  0.0060  0.0131  -0.0158 64  HIS B CA  
2773 C  C   . HIS B  65  ? 0.1038  0.1344 0.0768  -0.0027 0.0073  -0.0141 64  HIS B C   
2774 O  O   . HIS B  65  ? 0.1259  0.1289 0.0946  0.0097  0.0203  -0.0119 64  HIS B O   
2775 C  CB  . HIS B  65  ? 0.1305  0.1351 0.1120  0.0019  0.0019  -0.0234 64  HIS B CB  
2776 C  CG  . HIS B  65  ? 0.1076  0.1412 0.1012  -0.0138 0.0086  -0.0271 64  HIS B CG  
2777 N  ND1 . HIS B  65  ? 0.1380  0.1416 0.1124  -0.0233 0.0044  -0.0138 64  HIS B ND1 
2778 C  CD2 . HIS B  65  ? 0.1323  0.1409 0.1481  -0.0178 0.0273  -0.0296 64  HIS B CD2 
2779 C  CE1 . HIS B  65  ? 0.1119  0.1502 0.1395  -0.0127 0.0122  -0.0218 64  HIS B CE1 
2780 N  NE2 . HIS B  65  ? 0.1355  0.1696 0.1416  -0.0150 0.0124  -0.0264 64  HIS B NE2 
2781 N  N   . SER B  66  ? 0.1206  0.1056 0.0804  0.0068  0.0089  -0.0079 65  SER B N   
2782 C  CA  . SER B  66  ? 0.1181  0.0944 0.0836  -0.0006 0.0080  -0.0162 65  SER B CA  
2783 C  C   . SER B  66  ? 0.0955  0.1199 0.0655  -0.0022 0.0087  -0.0150 65  SER B C   
2784 O  O   . SER B  66  ? 0.1109  0.1260 0.0698  -0.0004 0.0086  -0.0196 65  SER B O   
2785 C  CB  . SER B  66  ? 0.1257  0.1535 0.0803  -0.0129 -0.0073 -0.0020 65  SER B CB  
2786 O  OG  . SER B  66  ? 0.1653  0.1190 0.0898  -0.0133 0.0048  -0.0122 65  SER B OG  
2787 N  N   . PHE B  67  ? 0.0876  0.1041 0.0858  0.0046  0.0114  -0.0097 66  PHE B N   
2788 C  CA  . PHE B  67  ? 0.0831  0.1154 0.0695  0.0143  -0.0082 -0.0122 66  PHE B CA  
2789 C  C   . PHE B  67  ? 0.0713  0.1221 0.0678  -0.0035 -0.0008 -0.0186 66  PHE B C   
2790 O  O   . PHE B  67  ? 0.1040  0.1289 0.0664  0.0069  -0.0069 -0.0170 66  PHE B O   
2791 C  CB  . PHE B  67  ? 0.0908  0.1243 0.0680  -0.0089 0.0022  -0.0227 66  PHE B CB  
2792 C  CG  . PHE B  67  ? 0.0844  0.1129 0.0854  -0.0015 -0.0085 -0.0149 66  PHE B CG  
2793 C  CD1 . PHE B  67  ? 0.0891  0.1427 0.1049  -0.0088 0.0176  -0.0353 66  PHE B CD1 
2794 C  CD2 . PHE B  67  ? 0.1067  0.1287 0.0961  -0.0254 -0.0146 -0.0009 66  PHE B CD2 
2795 C  CE1 . PHE B  67  ? 0.1190  0.1427 0.1247  -0.0254 0.0244  -0.0429 66  PHE B CE1 
2796 C  CE2 . PHE B  67  ? 0.1208  0.1621 0.0950  -0.0233 0.0011  -0.0021 66  PHE B CE2 
2797 C  CZ  . PHE B  67  ? 0.1316  0.1574 0.0949  -0.0419 -0.0030 -0.0381 66  PHE B CZ  
2798 N  N   . HIS B  68  ? 0.0864  0.1067 0.0977  0.0089  -0.0050 -0.0080 67  HIS B N   
2799 C  CA  . HIS B  68  ? 0.0882  0.1124 0.1348  0.0108  -0.0352 -0.0229 67  HIS B CA  
2800 C  C   . HIS B  68  ? 0.1120  0.1110 0.0750  0.0178  -0.0109 -0.0223 67  HIS B C   
2801 O  O   . HIS B  68  ? 0.1248  0.1344 0.0793  0.0100  -0.0103 -0.0358 67  HIS B O   
2802 C  CB  . HIS B  68  ? 0.1280  0.1423 0.1190  0.0159  0.0150  -0.0161 67  HIS B CB  
2803 C  CG  . HIS B  68  ? 0.0901  0.1678 0.1430  -0.0006 -0.0121 -0.0227 67  HIS B CG  
2804 N  ND1 . HIS B  68  ? 0.1506  0.1711 0.2037  -0.0142 0.0236  0.0142  67  HIS B ND1 
2805 C  CD2 . HIS B  68  ? 0.1395  0.1614 0.1441  -0.0103 -0.0251 0.0017  67  HIS B CD2 
2806 C  CE1 . HIS B  68  ? 0.1362  0.1930 0.1930  0.0148  0.0170  -0.0049 67  HIS B CE1 
2807 N  NE2 . HIS B  68  ? 0.1427  0.1693 0.1901  -0.0247 0.0054  0.0021  67  HIS B NE2 
2808 N  N   . VAL B  69  ? 0.1014  0.1128 0.0858  0.0141  -0.0137 -0.0168 68  VAL B N   
2809 C  CA  . VAL B  69  ? 0.1040  0.1054 0.0979  0.0109  -0.0140 -0.0108 68  VAL B CA  
2810 C  C   . VAL B  69  ? 0.1032  0.1014 0.0847  -0.0030 -0.0036 -0.0171 68  VAL B C   
2811 O  O   . VAL B  69  ? 0.1101  0.1263 0.0971  0.0078  -0.0226 -0.0346 68  VAL B O   
2812 C  CB  . VAL B  69  ? 0.1120  0.1578 0.0964  -0.0031 -0.0034 -0.0054 68  VAL B CB  
2813 C  CG1 . VAL B  69  ? 0.2073  0.1266 0.1273  -0.0359 -0.0295 -0.0032 68  VAL B CG1 
2814 C  CG2 . VAL B  69  ? 0.0915  0.2920 0.1272  -0.0289 -0.0093 0.0176  68  VAL B CG2 
2815 N  N   . ASN B  70  ? 0.1047  0.1194 0.1155  0.0078  0.0062  -0.0341 69  ASN B N   
2816 C  CA  . ASN B  70  ? 0.0952  0.1276 0.1243  0.0162  0.0013  -0.0234 69  ASN B CA  
2817 C  C   . ASN B  70  ? 0.0962  0.1196 0.1031  -0.0026 0.0103  -0.0265 69  ASN B C   
2818 O  O   . ASN B  70  ? 0.1135  0.1194 0.1326  0.0019  -0.0006 -0.0197 69  ASN B O   
2819 C  CB  . ASN B  70  ? 0.1513  0.1220 0.1307  0.0145  0.0247  -0.0002 69  ASN B CB  
2820 C  CG  . ASN B  70  ? 0.1725  0.1614 0.1398  -0.0254 -0.0214 -0.0069 69  ASN B CG  
2821 O  OD1 . ASN B  70  ? 0.1840  0.1556 0.1991  -0.0178 0.0272  -0.0021 69  ASN B OD1 
2822 N  ND2 . ASN B  70  ? 0.1506  0.2034 0.1542  -0.0019 -0.0200 0.0209  69  ASN B ND2 
2823 N  N   . PHE B  71  ? 0.1016  0.1441 0.0961  0.0215  -0.0065 -0.0261 70  PHE B N   
2824 C  CA  . PHE B  71  ? 0.1016  0.1330 0.1016  0.0170  0.0060  -0.0232 70  PHE B CA  
2825 C  C   . PHE B  71  ? 0.1049  0.1499 0.1333  0.0033  0.0078  -0.0374 70  PHE B C   
2826 O  O   . PHE B  71  ? 0.1199  0.1578 0.1872  0.0105  0.0281  -0.0308 70  PHE B O   
2827 C  CB  . PHE B  71  ? 0.1059  0.1553 0.1163  0.0200  -0.0004 -0.0093 70  PHE B CB  
2828 C  CG  . PHE B  71  ? 0.1305  0.1409 0.0818  0.0122  -0.0065 -0.0157 70  PHE B CG  
2829 C  CD1 . PHE B  71  ? 0.1671  0.1754 0.1036  0.0506  0.0096  -0.0071 70  PHE B CD1 
2830 C  CD2 . PHE B  71  ? 0.1348  0.1434 0.0795  0.0000  -0.0055 -0.0286 70  PHE B CD2 
2831 C  CE1 . PHE B  71  ? 0.1876  0.2314 0.0768  0.0952  0.0347  0.0100  70  PHE B CE1 
2832 C  CE2 . PHE B  71  ? 0.1366  0.1768 0.0996  -0.0058 -0.0070 -0.0375 70  PHE B CE2 
2833 C  CZ  . PHE B  71  ? 0.1250  0.2372 0.0950  0.0436  -0.0029 -0.0078 70  PHE B CZ  
2834 N  N   . GLU B  72  ? 0.1146  0.1373 0.1617  0.0244  -0.0020 -0.0489 71  GLU B N   
2835 C  CA  . GLU B  72  ? 0.1162  0.1682 0.1779  0.0376  -0.0021 -0.0401 71  GLU B CA  
2836 C  C   . GLU B  72  ? 0.1259  0.1750 0.1987  0.0456  -0.0046 -0.0477 71  GLU B C   
2837 O  O   . GLU B  72  ? 0.1416  0.1865 0.1901  0.0257  -0.0358 -0.0369 71  GLU B O   
2838 C  CB  . GLU B  72  ? 0.1260  0.1603 0.1883  0.0403  -0.0031 -0.0433 71  GLU B CB  
2839 C  CG  . GLU B  72  ? 0.1459  0.1736 0.2163  0.0151  -0.0170 -0.0523 71  GLU B CG  
2840 C  CD  . GLU B  72  ? 0.1632  0.1919 0.2680  0.0154  -0.0074 -0.0490 71  GLU B CD  
2841 O  OE1 . GLU B  72  ? 0.2842  0.1714 0.2781  0.0279  -0.0692 -0.0531 71  GLU B OE1 
2842 O  OE2 . GLU B  72  ? 0.1775  0.2267 0.3240  0.0089  -0.0284 -0.1003 71  GLU B OE2 
2843 N  N   . ASP B  73  ? 0.1341  0.1879 0.2196  0.0270  0.0048  -0.0723 72  ASP B N   
2844 C  CA  . ASP B  73  ? 0.1072  0.2246 0.2921  0.0013  -0.0024 -0.0939 72  ASP B CA  
2845 C  C   . ASP B  73  ? 0.1117  0.2903 0.3467  0.0442  -0.0186 -0.1127 72  ASP B C   
2846 O  O   . ASP B  73  ? 0.1138  0.3887 0.4347  0.0176  0.0208  -0.2116 72  ASP B O   
2847 C  CB  . ASP B  73  ? 0.1470  0.2205 0.2461  -0.0034 0.0192  -0.0894 72  ASP B CB  
2848 C  CG  . ASP B  73  ? 0.1987  0.2945 0.2461  -0.0479 0.0877  -0.1157 72  ASP B CG  
2849 O  OD1 . ASP B  73  ? 0.2618  0.3007 0.2981  -0.0681 0.1210  -0.1573 72  ASP B OD1 
2850 O  OD2 . ASP B  73  ? 0.2296  0.3129 0.2931  -0.0697 0.0434  -0.1670 72  ASP B OD2 
2851 N  N   . ASN B  74  ? 0.1614  0.2637 0.3370  0.0584  0.0532  -0.1075 73  ASN B N   
2852 C  CA  . ASN B  74  ? 0.1562  0.4059 0.3430  0.1282  -0.0233 -0.1481 73  ASN B CA  
2853 C  C   . ASN B  74  ? 0.1653  0.2640 0.3316  0.0479  0.0345  -0.0738 73  ASN B C   
2854 O  O   . ASN B  74  ? 0.1603  0.4091 0.4684  0.0886  0.0190  -0.1643 73  ASN B O   
2855 C  CB  . ASN B  74  ? 0.2326  0.3510 0.3542  0.0741  0.0515  -0.1525 73  ASN B CB  
2856 C  CG  . ASN B  74  ? 0.2271  0.3876 0.3704  0.0860  0.0222  -0.1884 73  ASN B CG  
2857 O  OD1 . ASN B  74  ? 0.5122  0.3758 0.4964  0.2045  -0.1055 -0.1685 73  ASN B OD1 
2858 N  ND2 . ASN B  74  ? 0.2605  0.2185 0.3488  0.0253  -0.0263 -0.1283 73  ASN B ND2 
2859 N  N   . ASP B  75  ? 0.1944  0.2996 0.3172  0.0368  -0.0073 -0.0901 74  ASP B N   
2860 C  CA  . ASP B  75  ? 0.2375  0.2827 0.3434  0.0820  -0.0240 -0.0829 74  ASP B CA  
2861 C  C   . ASP B  75  ? 0.2134  0.2454 0.3175  0.0741  -0.0714 -0.1047 74  ASP B C   
2862 O  O   . ASP B  75  ? 0.1671  0.2547 0.3959  0.0691  -0.0557 -0.1234 74  ASP B O   
2863 C  CB  . ASP B  75  ? 0.1700  0.2618 0.3718  0.0468  -0.0263 -0.1380 74  ASP B CB  
2864 C  CG  . ASP B  75  ? 0.1861  0.2856 0.3958  0.0684  -0.0710 -0.1095 74  ASP B CG  
2865 O  OD1 . ASP B  75  ? 0.1865  0.2666 0.3280  0.0851  -0.0756 -0.0873 74  ASP B OD1 
2866 O  OD2 . ASP B  75  ? 0.2472  0.3118 0.5697  0.1122  -0.0589 -0.1577 74  ASP B OD2 
2867 N  N   . ASN B  76  ? 0.1632  0.2831 0.3485  0.0717  -0.0748 -0.1033 75  ASN B N   
2868 C  CA  . ASN B  76  ? 0.1714  0.3204 0.3169  0.0632  -0.0510 -0.0696 75  ASN B CA  
2869 C  C   . ASN B  76  ? 0.1901  0.2640 0.3024  0.0892  -0.0752 -0.0618 75  ASN B C   
2870 O  O   . ASN B  76  ? 0.2741  0.3042 0.3215  0.1158  -0.1430 -0.0864 75  ASN B O   
2871 C  CB  . ASN B  76  ? 0.1768  0.3592 0.3876  0.0863  -0.1156 -0.1267 75  ASN B CB  
2872 C  CG  . ASN B  76  ? 0.2477  0.3603 0.5902  0.0471  -0.1536 -0.1674 75  ASN B CG  
2873 O  OD1 . ASN B  76  ? 0.2264  0.3768 0.5146  0.0672  -0.1253 -0.2095 75  ASN B OD1 
2874 N  ND2 . ASN B  76  ? 0.2346  0.6764 0.6020  0.0681  -0.1759 -0.1548 75  ASN B ND2 
2875 N  N   . ARG B  77  ? 0.1714  0.2407 0.2770  0.0894  -0.0846 -0.0891 76  ARG B N   
2876 C  CA  . ARG B  77  ? 0.2204  0.2102 0.2257  0.0759  -0.0868 -0.0379 76  ARG B CA  
2877 C  C   . ARG B  77  ? 0.2138  0.1937 0.2296  0.0467  -0.0834 -0.0434 76  ARG B C   
2878 O  O   . ARG B  77  ? 0.2809  0.2196 0.2235  0.0545  -0.0697 -0.0163 76  ARG B O   
2879 C  CB  . ARG B  77  ? 0.2551  0.2125 0.2181  0.0771  -0.1097 -0.0553 76  ARG B CB  
2880 C  CG  . ARG B  77  ? 0.2275  0.1980 0.2468  0.0651  -0.0644 -0.0644 76  ARG B CG  
2881 C  CD  . ARG B  77  ? 0.2694  0.1941 0.2319  0.0682  -0.0296 -0.0442 76  ARG B CD  
2882 N  NE  . ARG B  77  ? 0.2372  0.2016 0.2479  0.0844  -0.0551 -0.0529 76  ARG B NE  
2883 C  CZ  . ARG B  77  ? 0.2451  0.1851 0.2339  0.0835  -0.0588 -0.0433 76  ARG B CZ  
2884 N  NH1 . ARG B  77  ? 0.2461  0.2203 0.2820  0.0457  -0.0579 -0.0959 76  ARG B NH1 
2885 N  NH2 . ARG B  77  ? 0.1937  0.1980 0.2691  0.0529  -0.0364 -0.0527 76  ARG B NH2 
2886 N  N   . SER B  78  ? 0.1808  0.2041 0.1840  0.0628  -0.0611 -0.0436 77  SER B N   
2887 C  CA  . SER B  78  ? 0.1553  0.2055 0.2242  0.0447  -0.0709 -0.0576 77  SER B CA  
2888 C  C   . SER B  78  ? 0.1289  0.1930 0.1908  0.0340  -0.0633 -0.0536 77  SER B C   
2889 O  O   . SER B  78  ? 0.1549  0.2023 0.2181  0.0491  -0.0451 -0.0536 77  SER B O   
2890 C  CB  . SER B  78  ? 0.1483  0.1835 0.2115  0.0288  -0.0743 -0.0770 77  SER B CB  
2891 O  OG  . SER B  78  ? 0.1772  0.1653 0.1962  0.0221  -0.0647 -0.0302 77  SER B OG  
2892 N  N   . VAL B  79  ? 0.2016  0.2034 0.2034  0.0403  -0.0820 -0.0607 78  VAL B N   
2893 C  CA  . VAL B  79  ? 0.1614  0.2138 0.2579  0.0485  -0.0952 -0.1272 78  VAL B CA  
2894 C  C   . VAL B  79  ? 0.1711  0.2461 0.2357  0.0423  -0.0794 -0.0420 78  VAL B C   
2895 O  O   . VAL B  79  ? 0.2292  0.2283 0.2034  0.0406  -0.0724 -0.0570 78  VAL B O   
2896 C  CB  . VAL B  79  ? 0.1768  0.3050 0.2988  0.0878  -0.0977 -0.0882 78  VAL B CB  
2897 C  CG1 . VAL B  79  ? 0.1815  0.4350 0.3513  0.1215  -0.0881 -0.1694 78  VAL B CG1 
2898 C  CG2 . VAL B  79  ? 0.2953  0.4087 0.3014  0.1558  -0.1126 -0.0002 78  VAL B CG2 
2899 N  N   . LEU B  80  ? 0.1797  0.2217 0.2066  0.0221  -0.0714 -0.0826 79  LEU B N   
2900 C  CA  . LEU B  80  ? 0.1567  0.2766 0.1894  0.0605  -0.0807 -0.0686 79  LEU B CA  
2901 C  C   . LEU B  80  ? 0.1736  0.2605 0.2030  0.0519  -0.0735 -0.0832 79  LEU B C   
2902 O  O   . LEU B  80  ? 0.1678  0.2838 0.2515  0.0375  -0.0784 -0.0961 79  LEU B O   
2903 C  CB  . LEU B  80  ? 0.1668  0.2561 0.2059  0.0411  -0.0944 -0.0639 79  LEU B CB  
2904 C  CG  . LEU B  80  ? 0.1560  0.2547 0.2095  0.0074  -0.0534 -0.0707 79  LEU B CG  
2905 C  CD1 . LEU B  80  ? 0.1553  0.2823 0.2337  0.0204  -0.0361 -0.0139 79  LEU B CD1 
2906 C  CD2 . LEU B  80  ? 0.2064  0.2328 0.2090  0.0030  -0.0545 -0.0340 79  LEU B CD2 
2907 N  N   . LYS B  81  ? 0.2433  0.2605 0.2055  0.0535  -0.1047 -0.0817 80  LYS B N   
2908 C  CA  . LYS B  81  ? 0.2364  0.3219 0.2253  0.1013  -0.1270 -0.0839 80  LYS B CA  
2909 C  C   . LYS B  81  ? 0.1987  0.2931 0.2204  0.0550  -0.1052 -0.0633 80  LYS B C   
2910 O  O   . LYS B  81  ? 0.2187  0.3111 0.2027  0.0436  -0.1036 -0.0732 80  LYS B O   
2911 C  CB  . LYS B  81  ? 0.3923  0.3732 0.3018  0.1878  -0.2317 -0.1629 80  LYS B CB  
2912 C  CG  . LYS B  81  ? 0.4049  0.5047 0.2985  0.1820  -0.1482 -0.1016 80  LYS B CG  
2913 C  CD  . LYS B  81  ? 0.3409  0.5123 0.4223  0.1509  -0.0966 0.0358  80  LYS B CD  
2914 N  N   . GLY B  82  ? 0.2526  0.3352 0.1948  0.0718  -0.1247 -0.0930 81  GLY B N   
2915 C  CA  . GLY B  82  ? 0.2748  0.3251 0.1973  0.1101  -0.1373 -0.1177 81  GLY B CA  
2916 C  C   . GLY B  82  ? 0.2205  0.3219 0.1905  0.0284  -0.0912 -0.0583 81  GLY B C   
2917 O  O   . GLY B  82  ? 0.2296  0.3330 0.2059  0.0583  -0.0862 -0.0855 81  GLY B O   
2918 N  N   . GLY B  83  ? 0.2669  0.2644 0.2090  0.0406  -0.0845 -0.0385 82  GLY B N   
2919 C  CA  . GLY B  83  ? 0.2608  0.2831 0.2266  0.0836  -0.0572 -0.0790 82  GLY B CA  
2920 C  C   . GLY B  83  ? 0.2877  0.2655 0.2163  0.0644  -0.1351 -0.0717 82  GLY B C   
2921 O  O   . GLY B  83  ? 0.3693  0.3801 0.2321  0.0727  -0.1802 -0.0873 82  GLY B O   
2922 N  N   . PRO B  84  ? 0.2149  0.3025 0.2002  0.0469  -0.0430 -0.0774 83  PRO B N   
2923 C  CA  . PRO B  84  ? 0.2809  0.2741 0.1879  0.0225  -0.0440 -0.0410 83  PRO B CA  
2924 C  C   . PRO B  84  ? 0.2248  0.3222 0.2062  0.0127  -0.0383 -0.0617 83  PRO B C   
2925 O  O   . PRO B  84  ? 0.2081  0.3682 0.3869  -0.0076 -0.0617 -0.0688 83  PRO B O   
2926 C  CB  . PRO B  84  ? 0.2579  0.2852 0.2418  0.0210  -0.0886 -0.0491 83  PRO B CB  
2927 C  CG  . PRO B  84  ? 0.2465  0.2989 0.1991  0.0365  -0.0385 -0.0528 83  PRO B CG  
2928 C  CD  . PRO B  84  ? 0.2152  0.3208 0.1412  0.0424  -0.0467 -0.0335 83  PRO B CD  
2929 N  N   . PHE B  85  ? 0.2045  0.3183 0.2102  0.0580  -0.0974 -0.0895 84  PHE B N   
2930 C  CA  . PHE B  85  ? 0.1685  0.3516 0.3323  0.0621  -0.1080 -0.1483 84  PHE B CA  
2931 C  C   . PHE B  85  ? 0.2192  0.4314 0.3082  0.1017  -0.1052 -0.1203 84  PHE B C   
2932 O  O   . PHE B  85  ? 0.2819  0.3707 0.3829  0.1120  -0.1690 -0.0693 84  PHE B O   
2933 C  CB  . PHE B  85  ? 0.1993  0.3409 0.2521  0.0797  -0.0964 -0.1020 84  PHE B CB  
2934 C  CG  . PHE B  85  ? 0.1567  0.2921 0.2084  0.0624  -0.0546 -0.0738 84  PHE B CG  
2935 C  CD1 . PHE B  85  ? 0.2321  0.3014 0.2267  0.0850  -0.0190 -0.0885 84  PHE B CD1 
2936 C  CD2 . PHE B  85  ? 0.1736  0.3513 0.2221  0.0668  -0.0728 -0.1261 84  PHE B CD2 
2937 C  CE1 . PHE B  85  ? 0.1908  0.3225 0.2447  0.0743  -0.0538 -0.1104 84  PHE B CE1 
2938 C  CE2 . PHE B  85  ? 0.1991  0.3286 0.2375  0.0542  -0.1017 -0.1397 84  PHE B CE2 
2939 C  CZ  . PHE B  85  ? 0.1976  0.3154 0.2493  0.0554  -0.0749 -0.1228 84  PHE B CZ  
2940 N  N   . SER B  86  ? 0.1430  0.4508 0.4364  0.0822  -0.1179 -0.1894 85  SER B N   
2941 C  CA  . SER B  86  ? 0.2163  0.5115 0.3941  0.1433  -0.1590 -0.1464 85  SER B CA  
2942 C  C   . SER B  86  ? 0.2967  0.5571 0.4187  0.1985  -0.1438 -0.1794 85  SER B C   
2943 O  O   . SER B  86  ? 0.4663  0.6096 0.6703  0.2490  -0.2970 -0.2732 85  SER B O   
2944 C  CB  . SER B  86  ? 0.1768  0.6310 0.4102  0.0903  -0.1269 -0.1453 85  SER B CB  
2945 O  OG  . SER B  86  ? 0.2062  0.7686 0.6907  0.0232  -0.0626 -0.0868 85  SER B OG  
2946 N  N   . ASP B  87  ? 0.2467  0.5141 0.3916  0.1045  -0.1291 -0.2156 86  ASP B N   
2947 C  CA  . ASP B  87  ? 0.1729  0.5503 0.5098  0.0628  -0.1274 -0.3213 86  ASP B CA  
2948 C  C   . ASP B  87  ? 0.1606  0.3711 0.3786  0.0541  -0.0961 -0.1005 86  ASP B C   
2949 O  O   . ASP B  87  ? 0.1958  0.4278 0.3656  0.0609  -0.0916 -0.1822 86  ASP B O   
2950 C  CB  . ASP B  87  ? 0.2210  0.4652 0.7009  0.0386  -0.0331 -0.1919 86  ASP B CB  
2951 C  CG  . ASP B  87  ? 0.2751  0.5406 0.8422  -0.0233 -0.1834 -0.0660 86  ASP B CG  
2952 O  OD1 . ASP B  87  ? 0.2522  0.7434 0.6582  0.1143  -0.1662 -0.1430 86  ASP B OD1 
2953 O  OD2 . ASP B  87  ? 0.2540  0.5789 0.4389  -0.0136 -0.1890 -0.1109 86  ASP B OD2 
2954 N  N   . SER B  88  ? 0.1897  0.4345 0.3865  0.1208  -0.1298 -0.1564 87  SER B N   
2955 C  CA  . SER B  88  ? 0.2310  0.3387 0.3424  0.0617  -0.1559 -0.0010 87  SER B CA  
2956 C  C   . SER B  88  ? 0.1556  0.2949 0.2479  0.0350  -0.0651 -0.0687 87  SER B C   
2957 O  O   . SER B  88  ? 0.1412  0.2902 0.3517  0.0268  -0.0603 -0.0642 87  SER B O   
2958 C  CB  . SER B  88  ? 0.3941  0.3115 0.4501  0.0846  -0.1756 0.0110  87  SER B CB  
2959 O  OG  . SER B  88  ? 0.3972  0.4595 0.5200  0.0367  -0.0660 -0.0612 87  SER B OG  
2960 N  N   . TYR B  89  ? 0.1481  0.2407 0.2888  0.0430  -0.1011 -0.0557 88  TYR B N   
2961 C  CA  . TYR B  89  ? 0.1199  0.2486 0.2411  0.0370  -0.0655 -0.0928 88  TYR B CA  
2962 C  C   . TYR B  89  ? 0.1481  0.2497 0.2784  0.0367  -0.0748 -0.1045 88  TYR B C   
2963 O  O   . TYR B  89  ? 0.1732  0.2597 0.2504  0.0009  -0.0636 -0.0747 88  TYR B O   
2964 C  CB  . TYR B  89  ? 0.1274  0.2497 0.2856  0.0383  -0.0769 -0.1092 88  TYR B CB  
2965 C  CG  . TYR B  89  ? 0.1265  0.2205 0.2310  0.0433  -0.0710 -0.0949 88  TYR B CG  
2966 C  CD1 . TYR B  89  ? 0.1470  0.3255 0.2500  0.0416  -0.0712 -0.1362 88  TYR B CD1 
2967 C  CD2 . TYR B  89  ? 0.1348  0.2235 0.2605  0.0535  -0.0438 -0.0885 88  TYR B CD2 
2968 C  CE1 . TYR B  89  ? 0.1646  0.2601 0.2102  0.0414  -0.0714 -0.0895 88  TYR B CE1 
2969 C  CE2 . TYR B  89  ? 0.1599  0.2371 0.2257  0.0464  -0.0488 -0.0904 88  TYR B CE2 
2970 C  CZ  . TYR B  89  ? 0.1386  0.2702 0.3143  0.0420  -0.0710 -0.0942 88  TYR B CZ  
2971 O  OH  . TYR B  89  ? 0.1861  0.2975 0.2831  -0.0110 -0.0436 -0.1302 88  TYR B OH  
2972 N  N   . ARG B  90  ? 0.1156  0.2156 0.2495  0.0439  -0.0699 -0.0753 89  ARG B N   
2973 C  CA  . ARG B  90  ? 0.1093  0.2389 0.2508  0.0624  -0.0776 -0.0986 89  ARG B CA  
2974 C  C   . ARG B  90  ? 0.0932  0.2045 0.1786  0.0469  -0.0378 -0.0864 89  ARG B C   
2975 O  O   . ARG B  90  ? 0.1049  0.1919 0.2073  0.0429  -0.0381 -0.0657 89  ARG B O   
2976 C  CB  . ARG B  90  ? 0.1097  0.2615 0.2633  0.0756  -0.0353 -0.1177 89  ARG B CB  
2977 C  CG  . ARG B  90  ? 0.1567  0.2611 0.2709  0.0474  -0.0356 -0.1266 89  ARG B CG  
2978 C  CD  . ARG B  90  ? 0.1441  0.2874 0.3434  0.0558  -0.0170 -0.1197 89  ARG B CD  
2979 N  NE  . ARG B  90  ? 0.1253  0.3247 0.4709  0.0632  -0.0616 -0.2007 89  ARG B NE  
2980 C  CZ  . ARG B  90  ? 0.1066  0.2687 0.4824  0.0514  -0.0570 -0.1138 89  ARG B CZ  
2981 N  NH1 . ARG B  90  ? 0.1606  0.3851 0.4250  0.0211  -0.0163 -0.2465 89  ARG B NH1 
2982 N  NH2 . ARG B  90  ? 0.1386  0.2899 0.5797  0.0710  -0.0734 -0.1105 89  ARG B NH2 
2983 N  N   . LEU B  91  ? 0.1005  0.1883 0.2081  0.0299  -0.0446 -0.0666 90  LEU B N   
2984 C  CA  . LEU B  91  ? 0.0845  0.1851 0.1808  0.0272  -0.0335 -0.0630 90  LEU B CA  
2985 C  C   . LEU B  91  ? 0.1125  0.1858 0.1578  0.0354  -0.0331 -0.0782 90  LEU B C   
2986 O  O   . LEU B  91  ? 0.1215  0.2095 0.1987  0.0301  -0.0130 -0.0908 90  LEU B O   
2987 C  CB  . LEU B  91  ? 0.1021  0.1621 0.2199  0.0196  -0.0265 -0.0453 90  LEU B CB  
2988 C  CG  . LEU B  91  ? 0.0882  0.1599 0.2077  0.0166  -0.0340 -0.0517 90  LEU B CG  
2989 C  CD1 . LEU B  91  ? 0.1188  0.1919 0.1829  0.0544  -0.0276 -0.0603 90  LEU B CD1 
2990 C  CD2 . LEU B  91  ? 0.1276  0.1955 0.1341  0.0167  -0.0157 -0.0346 90  LEU B CD2 
2991 N  N   A PHE B  92  ? 0.0917  0.2199 0.1779  0.0245  -0.0462 -0.0369 91  PHE B N   
2992 N  N   B PHE B  92  ? 0.0685  0.2081 0.1653  0.0273  -0.0331 -0.0627 91  PHE B N   
2993 C  CA  A PHE B  92  ? 0.0840  0.1747 0.1517  -0.0119 -0.0210 -0.0514 91  PHE B CA  
2994 C  CA  B PHE B  92  ? 0.0908  0.2497 0.1509  0.0163  -0.0394 -0.0570 91  PHE B CA  
2995 C  C   A PHE B  92  ? 0.0917  0.1517 0.1118  0.0074  -0.0193 -0.0376 91  PHE B C   
2996 C  C   B PHE B  92  ? 0.0891  0.1542 0.1294  0.0242  -0.0064 -0.0538 91  PHE B C   
2997 O  O   A PHE B  92  ? 0.0935  0.1524 0.1161  -0.0003 -0.0067 -0.0514 91  PHE B O   
2998 O  O   B PHE B  92  ? 0.1012  0.1355 0.1208  0.0000  -0.0135 -0.0355 91  PHE B O   
2999 C  CB  A PHE B  92  ? 0.0469  0.1678 0.1527  0.0055  -0.0032 -0.0507 91  PHE B CB  
3000 C  CB  B PHE B  92  ? 0.1247  0.2433 0.1729  0.0370  0.0222  -0.0476 91  PHE B CB  
3001 C  CG  A PHE B  92  ? 0.1553  0.2011 0.1610  -0.0530 0.0618  -0.0425 91  PHE B CG  
3002 C  CG  B PHE B  92  ? 0.1502  0.2293 0.2371  0.0126  -0.0020 -0.1203 91  PHE B CG  
3003 C  CD1 A PHE B  92  ? 0.2698  0.2163 0.2878  -0.0751 0.1164  -0.1289 91  PHE B CD1 
3004 C  CD1 B PHE B  92  ? 0.1172  0.2543 0.2375  -0.0034 -0.0070 -0.1099 91  PHE B CD1 
3005 C  CD2 A PHE B  92  ? 0.1048  0.3348 0.2273  -0.0516 0.0084  -0.0462 91  PHE B CD2 
3006 C  CD2 B PHE B  92  ? 0.0873  0.2536 0.3434  0.0026  -0.0358 -0.1005 91  PHE B CD2 
3007 C  CE1 A PHE B  92  ? 0.3528  0.3420 0.2798  -0.2024 0.1727  -0.0815 91  PHE B CE1 
3008 C  CE1 B PHE B  92  ? 0.1059  0.2579 0.1592  0.0055  -0.0108 -0.0976 91  PHE B CE1 
3009 C  CE2 A PHE B  92  ? 0.1969  0.2870 0.2892  -0.0859 0.0759  0.0365  91  PHE B CE2 
3010 C  CE2 B PHE B  92  ? 0.1225  0.2662 0.2178  0.0401  -0.0036 -0.1351 91  PHE B CE2 
3011 C  CZ  A PHE B  92  ? 0.3758  0.4618 0.2030  -0.1561 0.1962  -0.0883 91  PHE B CZ  
3012 C  CZ  B PHE B  92  ? 0.1243  0.3093 0.1567  0.0264  0.0039  -0.0894 91  PHE B CZ  
3013 N  N   A GLN B  93  ? 0.0855  0.1854 0.1023  0.0225  -0.0116 -0.0283 92  GLN B N   
3014 N  N   B GLN B  93  ? 0.0892  0.1416 0.1675  0.0195  -0.0179 -0.0827 92  GLN B N   
3015 C  CA  A GLN B  93  ? 0.0894  0.1544 0.0928  0.0319  -0.0034 -0.0100 92  GLN B CA  
3016 C  CA  B GLN B  93  ? 0.0849  0.1330 0.1102  -0.0039 -0.0097 -0.0604 92  GLN B CA  
3017 C  C   A GLN B  93  ? 0.0917  0.1441 0.1045  0.0210  -0.0205 -0.0451 92  GLN B C   
3018 C  C   B GLN B  93  ? 0.0919  0.1355 0.1053  0.0092  -0.0161 -0.0547 92  GLN B C   
3019 O  O   A GLN B  93  ? 0.1137  0.1391 0.1220  0.0004  -0.0454 -0.0269 92  GLN B O   
3020 O  O   B GLN B  93  ? 0.1028  0.1581 0.1171  0.0050  -0.0189 -0.0655 92  GLN B O   
3021 C  CB  A GLN B  93  ? 0.1412  0.1914 0.2260  0.0491  0.0476  0.0807  92  GLN B CB  
3022 C  CB  B GLN B  93  ? 0.1474  0.1307 0.1267  -0.0053 0.0073  -0.0749 92  GLN B CB  
3023 C  CG  A GLN B  93  ? 0.3222  0.2034 0.2152  0.0333  0.0333  0.0418  92  GLN B CG  
3024 C  CG  B GLN B  93  ? 0.1100  0.1685 0.2260  -0.0027 -0.0267 -0.0987 92  GLN B CG  
3025 C  CD  A GLN B  93  ? 0.1013  0.1441 0.1477  0.0082  0.0277  -0.0326 92  GLN B CD  
3026 C  CD  B GLN B  93  ? 0.1067  0.1562 0.2477  -0.0091 0.0533  -0.0412 92  GLN B CD  
3027 O  OE1 A GLN B  93  ? 0.1204  0.1869 0.1725  0.0253  0.0310  -0.0391 92  GLN B OE1 
3028 O  OE1 B GLN B  93  ? 0.1093  0.1111 0.2354  0.0103  0.0575  -0.0496 92  GLN B OE1 
3029 N  NE2 A GLN B  93  ? 0.1427  0.2152 0.1610  0.0729  0.0847  0.0006  92  GLN B NE2 
3030 N  NE2 B GLN B  93  ? 0.2310  0.2744 0.3380  0.0797  0.1323  0.1098  92  GLN B NE2 
3031 N  N   . PHE B  94  ? 0.0838  0.1280 0.0998  0.0173  -0.0122 -0.0282 93  PHE B N   
3032 C  CA  . PHE B  94  ? 0.0882  0.1270 0.0845  0.0187  -0.0082 -0.0296 93  PHE B CA  
3033 C  C   . PHE B  94  ? 0.0810  0.1224 0.0982  -0.0081 -0.0081 -0.0387 93  PHE B C   
3034 O  O   . PHE B  94  ? 0.0988  0.1287 0.0818  0.0039  -0.0161 -0.0296 93  PHE B O   
3035 C  CB  . PHE B  94  ? 0.0959  0.1405 0.0867  0.0018  -0.0085 -0.0260 93  PHE B CB  
3036 C  CG  . PHE B  94  ? 0.1115  0.1268 0.0813  0.0030  -0.0080 -0.0225 93  PHE B CG  
3037 C  CD1 . PHE B  94  ? 0.1089  0.1599 0.0831  -0.0029 -0.0072 -0.0220 93  PHE B CD1 
3038 C  CD2 . PHE B  94  ? 0.1359  0.1194 0.0840  -0.0073 -0.0039 -0.0151 93  PHE B CD2 
3039 C  CE1 . PHE B  94  ? 0.1195  0.1348 0.1016  0.0022  -0.0049 -0.0151 93  PHE B CE1 
3040 C  CE2 . PHE B  94  ? 0.1164  0.1305 0.1005  0.0143  -0.0031 -0.0206 93  PHE B CE2 
3041 C  CZ  . PHE B  94  ? 0.1232  0.1330 0.0908  0.0145  -0.0017 -0.0109 93  PHE B CZ  
3042 N  N   . HIS B  95  ? 0.0905  0.1170 0.0970  0.0118  -0.0018 -0.0272 94  HIS B N   
3043 C  CA  . HIS B  95  ? 0.0962  0.1090 0.0800  0.0138  -0.0022 -0.0254 94  HIS B CA  
3044 C  C   . HIS B  95  ? 0.0899  0.1081 0.0697  0.0043  -0.0080 -0.0238 94  HIS B C   
3045 O  O   . HIS B  95  ? 0.0900  0.1305 0.0775  0.0060  -0.0115 -0.0345 94  HIS B O   
3046 C  CB  . HIS B  95  ? 0.1029  0.1142 0.0828  -0.0134 0.0043  -0.0290 94  HIS B CB  
3047 C  CG  . HIS B  95  ? 0.0862  0.1093 0.0870  -0.0070 0.0003  -0.0351 94  HIS B CG  
3048 N  ND1 . HIS B  95  ? 0.0961  0.1307 0.1341  -0.0025 -0.0029 -0.0392 94  HIS B ND1 
3049 C  CD2 . HIS B  95  ? 0.1082  0.1190 0.0853  -0.0137 -0.0051 -0.0365 94  HIS B CD2 
3050 C  CE1 . HIS B  95  ? 0.1076  0.1164 0.1509  0.0018  0.0099  -0.0429 94  HIS B CE1 
3051 N  NE2 . HIS B  95  ? 0.1013  0.1190 0.0741  -0.0040 -0.0077 -0.0352 94  HIS B NE2 
3052 N  N   . PHE B  96  ? 0.0776  0.1067 0.0803  0.0133  -0.0006 -0.0239 95  PHE B N   
3053 C  CA  . PHE B  96  ? 0.0822  0.1082 0.0706  0.0087  0.0149  -0.0206 95  PHE B CA  
3054 C  C   . PHE B  96  ? 0.0750  0.1172 0.0724  -0.0032 -0.0002 -0.0142 95  PHE B C   
3055 O  O   . PHE B  96  ? 0.1190  0.1137 0.0761  0.0129  0.0093  -0.0152 95  PHE B O   
3056 C  CB  . PHE B  96  ? 0.0822  0.1269 0.0820  0.0092  0.0034  -0.0161 95  PHE B CB  
3057 C  CG  . PHE B  96  ? 0.0773  0.1134 0.0853  0.0102  -0.0080 -0.0147 95  PHE B CG  
3058 C  CD1 . PHE B  96  ? 0.1049  0.1129 0.1111  0.0143  -0.0168 -0.0250 95  PHE B CD1 
3059 C  CD2 . PHE B  96  ? 0.0900  0.1434 0.0820  -0.0050 0.0000  0.0010  95  PHE B CD2 
3060 C  CE1 . PHE B  96  ? 0.1067  0.1259 0.0937  0.0149  -0.0086 -0.0199 95  PHE B CE1 
3061 C  CE2 . PHE B  96  ? 0.0979  0.1409 0.0917  0.0032  -0.0140 -0.0064 95  PHE B CE2 
3062 C  CZ  . PHE B  96  ? 0.0937  0.1639 0.0962  0.0030  -0.0212 -0.0210 95  PHE B CZ  
3063 N  N   . HIS B  97  ? 0.0937  0.1120 0.0757  0.0042  -0.0023 -0.0354 96  HIS B N   
3064 C  CA  . HIS B  97  ? 0.0871  0.1159 0.1028  0.0075  0.0097  -0.0225 96  HIS B CA  
3065 C  C   . HIS B  97  ? 0.0928  0.1268 0.0621  0.0009  -0.0046 -0.0242 96  HIS B C   
3066 O  O   . HIS B  97  ? 0.0937  0.1398 0.0724  0.0079  -0.0012 -0.0228 96  HIS B O   
3067 C  CB  . HIS B  97  ? 0.0867  0.1355 0.1147  -0.0046 0.0017  -0.0438 96  HIS B CB  
3068 C  CG  . HIS B  97  ? 0.0750  0.1199 0.1118  -0.0063 0.0010  -0.0422 96  HIS B CG  
3069 N  ND1 . HIS B  97  ? 0.1102  0.1252 0.0980  0.0037  0.0038  -0.0296 96  HIS B ND1 
3070 C  CD2 . HIS B  97  ? 0.0636  0.1391 0.0917  0.0226  -0.0006 -0.0447 96  HIS B CD2 
3071 C  CE1 . HIS B  97  ? 0.1007  0.1021 0.1036  0.0108  -0.0198 -0.0218 96  HIS B CE1 
3072 N  NE2 . HIS B  97  ? 0.0855  0.1256 0.0952  0.0111  0.0099  -0.0396 96  HIS B NE2 
3073 N  N   . TRP B  98  ? 0.0891  0.1225 0.0804  0.0013  -0.0065 -0.0223 97  TRP B N   
3074 C  CA  . TRP B  98  ? 0.0803  0.1208 0.0885  0.0074  0.0005  -0.0115 97  TRP B CA  
3075 C  C   . TRP B  98  ? 0.1084  0.1323 0.0996  0.0068  -0.0073 -0.0220 97  TRP B C   
3076 O  O   . TRP B  98  ? 0.1603  0.1248 0.0979  0.0132  0.0152  -0.0161 97  TRP B O   
3077 C  CB  . TRP B  98  ? 0.0837  0.1581 0.0967  -0.0089 0.0015  -0.0263 97  TRP B CB  
3078 C  CG  . TRP B  98  ? 0.0698  0.1427 0.0943  0.0192  0.0084  -0.0233 97  TRP B CG  
3079 C  CD1 . TRP B  98  ? 0.1005  0.1341 0.1172  0.0077  0.0054  -0.0263 97  TRP B CD1 
3080 C  CD2 . TRP B  98  ? 0.0849  0.1270 0.0914  0.0021  0.0049  -0.0247 97  TRP B CD2 
3081 N  NE1 . TRP B  98  ? 0.0973  0.1196 0.1102  0.0120  0.0013  -0.0231 97  TRP B NE1 
3082 C  CE2 . TRP B  98  ? 0.0926  0.1326 0.0840  -0.0012 0.0027  -0.0234 97  TRP B CE2 
3083 C  CE3 . TRP B  98  ? 0.0829  0.1172 0.0960  0.0030  0.0054  -0.0159 97  TRP B CE3 
3084 C  CZ2 . TRP B  98  ? 0.1111  0.1190 0.0952  -0.0055 0.0084  -0.0189 97  TRP B CZ2 
3085 C  CZ3 . TRP B  98  ? 0.1050  0.1160 0.0865  0.0036  0.0000  -0.0210 97  TRP B CZ3 
3086 C  CH2 . TRP B  98  ? 0.1111  0.1412 0.0905  -0.0008 0.0055  -0.0133 97  TRP B CH2 
3087 N  N   . GLY B  99  ? 0.1155  0.1280 0.1416  0.0342  -0.0144 -0.0372 98  GLY B N   
3088 C  CA  . GLY B  99  ? 0.1790  0.1384 0.1675  0.0644  -0.0153 -0.0316 98  GLY B CA  
3089 C  C   . GLY B  99  ? 0.2143  0.2242 0.1326  0.1028  0.0428  -0.0118 98  GLY B C   
3090 O  O   . GLY B  99  ? 0.1163  0.3068 0.1459  0.0650  0.0164  0.0330  98  GLY B O   
3091 N  N   . SER B  100 ? 0.2992  0.2565 0.1804  0.1876  0.0506  0.0226  99  SER B N   
3092 C  CA  . SER B  100 ? 0.2819  0.4577 0.1718  0.2428  0.0787  0.0929  99  SER B CA  
3093 C  C   . SER B  100 ? 0.2903  0.4670 0.1359  0.2455  0.0513  0.0661  99  SER B C   
3094 O  O   . SER B  100 ? 0.3049  0.5605 0.2037  0.2691  0.0610  0.0841  99  SER B O   
3095 C  CB  . SER B  100 ? 0.4957  0.4523 0.3032  0.2433  -0.0502 0.1138  99  SER B CB  
3096 O  OG  . SER B  100 ? 0.5790  0.4654 0.4857  0.2415  0.1587  0.1885  99  SER B OG  
3097 N  N   . THR B  101 ? 0.3459  0.3955 0.1835  0.2428  0.1097  0.0697  100 THR B N   
3098 C  CA  . THR B  101 ? 0.2741  0.2845 0.1685  0.1556  0.0584  0.0267  100 THR B CA  
3099 C  C   . THR B  101 ? 0.2946  0.2415 0.1883  0.1509  0.0800  -0.0157 100 THR B C   
3100 O  O   . THR B  101 ? 0.2741  0.1890 0.1720  0.0939  0.0560  -0.0082 100 THR B O   
3101 C  CB  . THR B  101 ? 0.2784  0.2337 0.2727  0.0767  0.0154  -0.0471 100 THR B CB  
3102 O  OG1 . THR B  101 ? 0.2554  0.2314 0.3704  0.0727  0.0015  -0.0986 100 THR B OG1 
3103 C  CG2 . THR B  101 ? 0.6104  0.4483 0.5220  0.3696  0.3425  0.3152  100 THR B CG2 
3104 N  N   . ASN B  102 ? 0.2625  0.1941 0.1499  0.0625  0.0433  -0.0365 101 ASN B N   
3105 C  CA  . ASN B  102 ? 0.2256  0.1808 0.1301  0.0197  0.0104  -0.0373 101 ASN B CA  
3106 C  C   . ASN B  102 ? 0.1984  0.1897 0.1624  -0.0071 0.0540  -0.0590 101 ASN B C   
3107 O  O   . ASN B  102 ? 0.2160  0.2138 0.1603  -0.0156 0.0261  -0.0710 101 ASN B O   
3108 C  CB  . ASN B  102 ? 0.2265  0.2150 0.1386  -0.0290 -0.0052 -0.0637 101 ASN B CB  
3109 C  CG  . ASN B  102 ? 0.2328  0.1955 0.1520  0.0452  -0.0776 -0.0639 101 ASN B CG  
3110 O  OD1 . ASN B  102 ? 0.2702  0.2213 0.2030  0.0155  -0.0822 -0.0891 101 ASN B OD1 
3111 N  ND2 . ASN B  102 ? 0.2005  0.2196 0.2917  0.0091  -0.0881 -0.0458 101 ASN B ND2 
3112 N  N   . GLU B  103 ? 0.1930  0.1700 0.2637  0.0040  0.0793  -0.1062 102 GLU B N   
3113 C  CA  . GLU B  103 ? 0.2041  0.2132 0.3448  -0.0190 0.1365  -0.1442 102 GLU B CA  
3114 C  C   . GLU B  103 ? 0.2041  0.1930 0.2881  -0.0234 0.0851  -0.1319 102 GLU B C   
3115 O  O   . GLU B  103 ? 0.2318  0.3139 0.3014  -0.0980 0.1023  -0.1935 102 GLU B O   
3116 C  CB  . GLU B  103 ? 0.2484  0.2055 0.6544  -0.0047 0.1190  -0.1363 102 GLU B CB  
3117 C  CG  . GLU B  103 ? 0.3344  0.3542 0.6445  0.0669  0.1780  -0.1119 102 GLU B CG  
3118 C  CD  . GLU B  103 ? 0.3801  0.5759 0.5687  0.0646  0.0520  -0.1618 102 GLU B CD  
3119 O  OE1 . GLU B  103 ? 0.5614  1.2566 0.6249  0.1223  0.2898  0.2483  102 GLU B OE1 
3120 O  OE2 . GLU B  103 ? 0.8104  0.8794 0.5213  0.3583  0.1903  0.0245  102 GLU B OE2 
3121 N  N   A HIS B  104 ? 0.1481  0.1445 0.2758  0.0114  0.0993  -0.0636 103 HIS B N   
3122 N  N   B HIS B  104 ? 0.2170  0.1664 0.1804  0.0281  0.0508  -0.0303 103 HIS B N   
3123 C  CA  A HIS B  104 ? 0.1430  0.1596 0.2170  -0.0204 0.0525  -0.0223 103 HIS B CA  
3124 C  CA  B HIS B  104 ? 0.1912  0.1840 0.2332  0.0628  0.0471  -0.0840 103 HIS B CA  
3125 C  C   A HIS B  104 ? 0.2027  0.2443 0.0461  0.0269  0.0434  0.0038  103 HIS B C   
3126 C  C   B HIS B  104 ? 0.1427  0.2242 0.3779  0.0810  -0.1419 -0.2493 103 HIS B C   
3127 O  O   A HIS B  104 ? 0.1707  0.1635 0.2145  0.0819  0.0000  -0.0450 103 HIS B O   
3128 O  O   B HIS B  104 ? 0.1344  0.3125 0.3172  -0.0293 -0.0990 -0.0688 103 HIS B O   
3129 C  CB  A HIS B  104 ? 0.1039  0.1301 0.3632  0.0067  0.0662  0.0120  103 HIS B CB  
3130 C  CB  B HIS B  104 ? 0.2059  0.1883 0.2928  0.0403  0.0350  -0.0686 103 HIS B CB  
3131 C  CG  A HIS B  104 ? 0.2178  0.1124 0.4173  0.0406  0.0551  0.1253  103 HIS B CG  
3132 C  CG  B HIS B  104 ? 0.2127  0.1747 0.1632  -0.0012 0.0193  -0.0363 103 HIS B CG  
3133 N  ND1 A HIS B  104 ? 0.2583  0.3970 0.4049  0.0217  -0.1018 0.1993  103 HIS B ND1 
3134 N  ND1 B HIS B  104 ? 0.0794  0.1499 0.1055  -0.0072 0.0106  -0.0877 103 HIS B ND1 
3135 C  CD2 A HIS B  104 ? 0.4411  0.2169 0.2011  -0.0894 -0.1350 0.0306  103 HIS B CD2 
3136 C  CD2 B HIS B  104 ? 0.3373  0.1120 0.3642  0.0348  0.0026  -0.0201 103 HIS B CD2 
3137 C  CE1 A HIS B  104 ? 0.4429  0.1653 0.2856  -0.0623 0.1874  -0.0054 103 HIS B CE1 
3138 C  CE1 B HIS B  104 ? 0.2364  0.1775 0.3312  -0.1124 0.0612  -0.1239 103 HIS B CE1 
3139 N  NE2 A HIS B  104 ? 0.2759  0.2156 0.4245  -0.0164 -0.1136 0.1168  103 HIS B NE2 
3140 N  NE2 B HIS B  104 ? 0.2490  0.2145 0.2054  0.0933  0.1254  0.0027  103 HIS B NE2 
3141 N  N   . GLY B  105 ? 0.2116  0.2673 0.1966  0.1108  -0.0635 -0.1057 104 GLY B N   
3142 C  CA  . GLY B  105 ? 0.1276  0.2357 0.1567  0.0670  -0.0184 -0.0813 104 GLY B CA  
3143 C  C   . GLY B  105 ? 0.1098  0.1506 0.1402  0.0130  -0.0172 -0.0512 104 GLY B C   
3144 O  O   . GLY B  105 ? 0.1448  0.1509 0.1301  0.0253  0.0050  -0.0576 104 GLY B O   
3145 N  N   . SER B  106 ? 0.0994  0.1373 0.1199  -0.0033 -0.0042 -0.0373 105 SER B N   
3146 C  CA  . SER B  106 ? 0.0960  0.1386 0.0985  -0.0088 0.0099  -0.0188 105 SER B CA  
3147 C  C   . SER B  106 ? 0.1206  0.1276 0.1080  -0.0008 0.0097  -0.0365 105 SER B C   
3148 O  O   . SER B  106 ? 0.1147  0.1359 0.1326  -0.0083 0.0236  -0.0261 105 SER B O   
3149 C  CB  . SER B  106 ? 0.1344  0.1538 0.0899  -0.0022 0.0114  -0.0396 105 SER B CB  
3150 O  OG  . SER B  106 ? 0.1283  0.1624 0.1226  0.0033  0.0185  -0.0568 105 SER B OG  
3151 N  N   . GLU B  107 ? 0.0934  0.1509 0.1126  0.0052  0.0110  -0.0348 106 GLU B N   
3152 C  CA  . GLU B  107 ? 0.1032  0.1495 0.1111  -0.0111 0.0070  -0.0411 106 GLU B CA  
3153 C  C   . GLU B  107 ? 0.0908  0.1448 0.1298  -0.0036 0.0179  -0.0435 106 GLU B C   
3154 O  O   . GLU B  107 ? 0.1333  0.1312 0.1492  0.0073  0.0144  -0.0513 106 GLU B O   
3155 C  CB  . GLU B  107 ? 0.0987  0.1772 0.1099  -0.0129 0.0251  -0.0625 106 GLU B CB  
3156 C  CG  . GLU B  107 ? 0.1267  0.2594 0.0953  -0.0006 0.0089  -0.0656 106 GLU B CG  
3157 C  CD  . GLU B  107 ? 0.1097  0.1223 0.1161  -0.0044 -0.0069 -0.0321 106 GLU B CD  
3158 O  OE1 . GLU B  107 ? 0.1316  0.1409 0.1264  -0.0035 -0.0094 -0.0182 106 GLU B OE1 
3159 O  OE2 . GLU B  107 ? 0.1199  0.1344 0.1229  -0.0015 0.0016  -0.0215 106 GLU B OE2 
3160 N  N   . HIS B  108 ? 0.1030  0.1544 0.1172  -0.0047 0.0069  -0.0534 107 HIS B N   
3161 C  CA  . HIS B  108 ? 0.1014  0.1761 0.1068  -0.0019 0.0019  -0.0472 107 HIS B CA  
3162 C  C   . HIS B  108 ? 0.0944  0.1720 0.0937  -0.0132 -0.0033 -0.0541 107 HIS B C   
3163 O  O   . HIS B  108 ? 0.0970  0.1635 0.1337  -0.0157 0.0063  -0.0579 107 HIS B O   
3164 C  CB  . HIS B  108 ? 0.1067  0.1682 0.1111  -0.0027 -0.0060 -0.0534 107 HIS B CB  
3165 C  CG  . HIS B  108 ? 0.1143  0.1571 0.1120  -0.0274 0.0084  -0.0589 107 HIS B CG  
3166 N  ND1 . HIS B  108 ? 0.1058  0.1632 0.1120  -0.0055 -0.0051 -0.0548 107 HIS B ND1 
3167 C  CD2 . HIS B  108 ? 0.1076  0.1761 0.1289  -0.0096 -0.0076 -0.0656 107 HIS B CD2 
3168 C  CE1 . HIS B  108 ? 0.0876  0.1743 0.1312  -0.0186 0.0003  -0.0400 107 HIS B CE1 
3169 N  NE2 . HIS B  108 ? 0.1058  0.1761 0.1330  -0.0108 -0.0032 -0.0615 107 HIS B NE2 
3170 N  N   . THR B  109 ? 0.1301  0.1682 0.1190  -0.0103 0.0120  -0.0652 108 THR B N   
3171 C  CA  . THR B  109 ? 0.1441  0.1603 0.1316  -0.0036 0.0287  -0.0782 108 THR B CA  
3172 C  C   . THR B  109 ? 0.1271  0.1714 0.1259  -0.0244 0.0240  -0.0726 108 THR B C   
3173 O  O   . THR B  109 ? 0.1189  0.1980 0.1319  -0.0127 0.0125  -0.0800 108 THR B O   
3174 C  CB  . THR B  109 ? 0.1344  0.1499 0.1641  -0.0155 -0.0008 -0.0649 108 THR B CB  
3175 O  OG1 . THR B  109 ? 0.1326  0.1750 0.1800  -0.0153 0.0320  -0.0732 108 THR B OG1 
3176 C  CG2 . THR B  109 ? 0.1294  0.2011 0.1474  0.0044  0.0004  -0.0604 108 THR B CG2 
3177 N  N   . VAL B  110 ? 0.1470  0.1897 0.1289  -0.0108 0.0377  -0.0890 109 VAL B N   
3178 C  CA  . VAL B  110 ? 0.1668  0.1876 0.1276  0.0002  0.0395  -0.0682 109 VAL B CA  
3179 C  C   . VAL B  110 ? 0.1502  0.2169 0.1348  0.0071  0.0186  -0.0847 109 VAL B C   
3180 O  O   . VAL B  110 ? 0.1481  0.2362 0.1562  -0.0071 0.0273  -0.0719 109 VAL B O   
3181 C  CB  . VAL B  110 ? 0.1650  0.2055 0.1675  -0.0083 0.0494  -0.0445 109 VAL B CB  
3182 C  CG1 . VAL B  110 ? 0.1711  0.2755 0.1614  -0.0168 0.0234  -0.0391 109 VAL B CG1 
3183 C  CG2 . VAL B  110 ? 0.1729  0.1919 0.1696  -0.0116 0.0247  -0.0554 109 VAL B CG2 
3184 N  N   . ASP B  111 ? 0.1732  0.2224 0.1362  -0.0041 0.0153  -0.1032 110 ASP B N   
3185 C  CA  . ASP B  111 ? 0.1793  0.2461 0.1395  0.0128  0.0187  -0.1111 110 ASP B CA  
3186 C  C   . ASP B  111 ? 0.1725  0.2077 0.2011  -0.0004 0.0228  -0.0906 110 ASP B C   
3187 O  O   . ASP B  111 ? 0.1682  0.2608 0.2314  0.0057  0.0254  -0.1172 110 ASP B O   
3188 C  CB  . ASP B  111 ? 0.2030  0.2583 0.1542  0.0201  0.0227  -0.0639 110 ASP B CB  
3189 C  CG  . ASP B  111 ? 0.2310  0.2777 0.1736  0.0095  0.0263  -0.1018 110 ASP B CG  
3190 O  OD1 . ASP B  111 ? 0.2242  0.3204 0.1736  -0.0355 0.0122  -0.1030 110 ASP B OD1 
3191 O  OD2 . ASP B  111 ? 0.2253  0.3122 0.1941  -0.0115 0.0138  -0.0621 110 ASP B OD2 
3192 N  N   . GLY B  112 ? 0.1549  0.1797 0.1703  -0.0198 0.0140  -0.0807 111 GLY B N   
3193 C  CA  . GLY B  112 ? 0.1499  0.2206 0.1998  0.0071  -0.0053 -0.0737 111 GLY B CA  
3194 C  C   . GLY B  112 ? 0.1242  0.1937 0.2240  0.0104  0.0016  -0.0819 111 GLY B C   
3195 O  O   . GLY B  112 ? 0.1914  0.2163 0.2328  -0.0058 -0.0015 -0.0449 111 GLY B O   
3196 N  N   . VAL B  113 ? 0.1459  0.2048 0.1833  -0.0066 0.0165  -0.1090 112 VAL B N   
3197 C  CA  . VAL B  113 ? 0.1517  0.2084 0.1962  -0.0236 0.0204  -0.0893 112 VAL B CA  
3198 C  C   . VAL B  113 ? 0.0961  0.1635 0.2150  -0.0066 0.0111  -0.1032 112 VAL B C   
3199 O  O   . VAL B  113 ? 0.1208  0.1948 0.1998  -0.0078 0.0259  -0.0612 112 VAL B O   
3200 C  CB  . VAL B  113 ? 0.1659  0.2224 0.2381  -0.0378 0.0380  -0.0974 112 VAL B CB  
3201 C  CG1 . VAL B  113 ? 0.1488  0.2195 0.2680  -0.0431 0.0395  -0.0811 112 VAL B CG1 
3202 C  CG2 . VAL B  113 ? 0.2271  0.2769 0.2091  -0.0343 0.0655  -0.0978 112 VAL B CG2 
3203 N  N   . LYS B  114 ? 0.1208  0.1908 0.2059  -0.0006 -0.0039 -0.1139 113 LYS B N   
3204 C  CA  . LYS B  114 ? 0.1330  0.1610 0.1993  -0.0168 0.0128  -0.0783 113 LYS B CA  
3205 C  C   . LYS B  114 ? 0.1145  0.1829 0.1635  -0.0073 0.0310  -0.0763 113 LYS B C   
3206 O  O   . LYS B  114 ? 0.1362  0.2081 0.2343  -0.0040 0.0457  -0.1044 113 LYS B O   
3207 C  CB  . LYS B  114 ? 0.1703  0.1409 0.2680  -0.0023 0.0205  -0.0298 113 LYS B CB  
3208 C  CG  . LYS B  114 ? 0.1513  0.1668 0.3567  0.0006  0.0118  -0.0428 113 LYS B CG  
3209 C  CD  . LYS B  114 ? 0.1869  0.1951 0.6164  -0.0115 -0.0051 0.0410  113 LYS B CD  
3210 C  CE  . LYS B  114 ? 0.2217  0.2425 0.5610  0.0476  0.0380  -0.0849 113 LYS B CE  
3211 N  NZ  . LYS B  114 ? 1.0812  0.2285 0.7758  0.1892  0.1128  -0.0596 113 LYS B NZ  
3212 N  N   . TYR B  115 ? 0.1116  0.1438 0.1247  -0.0013 0.0208  -0.0613 114 TYR B N   
3213 C  CA  . TYR B  115 ? 0.1190  0.1653 0.1366  -0.0026 0.0104  -0.0587 114 TYR B CA  
3214 C  C   . TYR B  115 ? 0.1240  0.1420 0.1197  -0.0053 0.0196  -0.0588 114 TYR B C   
3215 O  O   . TYR B  115 ? 0.1207  0.1531 0.1330  -0.0067 0.0003  -0.0294 114 TYR B O   
3216 C  CB  . TYR B  115 ? 0.1283  0.1829 0.0926  -0.0026 0.0223  -0.0357 114 TYR B CB  
3217 C  CG  . TYR B  115 ? 0.1298  0.1743 0.1194  -0.0039 0.0234  -0.0516 114 TYR B CG  
3218 C  CD1 . TYR B  115 ? 0.1452  0.1743 0.1172  0.0002  0.0095  -0.0542 114 TYR B CD1 
3219 C  CD2 . TYR B  115 ? 0.2059  0.2633 0.1155  -0.0873 0.0381  -0.0477 114 TYR B CD2 
3220 C  CE1 . TYR B  115 ? 0.1671  0.1944 0.1137  0.0168  0.0173  -0.0583 114 TYR B CE1 
3221 C  CE2 . TYR B  115 ? 0.2120  0.3201 0.1164  -0.1012 0.0353  -0.0710 114 TYR B CE2 
3222 C  CZ  . TYR B  115 ? 0.1553  0.2827 0.1016  -0.0407 0.0205  -0.0697 114 TYR B CZ  
3223 O  OH  . TYR B  115 ? 0.2041  0.2791 0.1076  -0.0572 0.0307  -0.0785 114 TYR B OH  
3224 N  N   A SER B  116 ? 0.1136  0.1538 0.1180  0.0003  0.0317  -0.0709 115 SER B N   
3225 N  N   B SER B  116 ? 0.1150  0.1553 0.1368  0.0022  0.0035  -0.0657 115 SER B N   
3226 C  CA  A SER B  116 ? 0.0827  0.1423 0.1274  0.0075  0.0055  -0.0572 115 SER B CA  
3227 C  CA  B SER B  116 ? 0.0988  0.1772 0.1266  -0.0037 -0.0013 -0.0602 115 SER B CA  
3228 C  C   A SER B  116 ? 0.0908  0.1386 0.1207  0.0083  0.0027  -0.0432 115 SER B C   
3229 C  C   B SER B  116 ? 0.1013  0.1513 0.1305  0.0117  -0.0096 -0.0378 115 SER B C   
3230 O  O   A SER B  116 ? 0.1172  0.1664 0.1153  0.0329  -0.0064 -0.0337 115 SER B O   
3231 O  O   B SER B  116 ? 0.1267  0.1527 0.1217  0.0084  -0.0198 -0.0432 115 SER B O   
3232 C  CB  A SER B  116 ? 0.0883  0.0962 0.1527  0.0127  0.0491  -0.0364 115 SER B CB  
3233 C  CB  B SER B  116 ? 0.1368  0.2213 0.2357  -0.0567 -0.0023 -0.0183 115 SER B CB  
3234 O  OG  A SER B  116 ? 0.0637  0.1696 0.1124  -0.0158 0.0398  -0.0729 115 SER B OG  
3235 O  OG  B SER B  116 ? 0.1912  0.2816 0.1502  -0.0440 -0.0127 -0.0306 115 SER B OG  
3236 N  N   . ALA B  117 ? 0.0831  0.1499 0.1044  0.0105  0.0093  -0.0381 116 ALA B N   
3237 C  CA  . ALA B  117 ? 0.0820  0.1459 0.0822  0.0133  0.0109  -0.0268 116 ALA B CA  
3238 C  C   . ALA B  117 ? 0.0776  0.1120 0.0835  -0.0025 -0.0047 -0.0331 116 ALA B C   
3239 O  O   . ALA B  117 ? 0.0996  0.1395 0.0739  -0.0062 0.0035  -0.0276 116 ALA B O   
3240 C  CB  . ALA B  117 ? 0.1120  0.1283 0.0944  0.0059  -0.0102 -0.0375 116 ALA B CB  
3241 N  N   . GLU B  118 ? 0.0847  0.1262 0.0829  0.0174  0.0024  -0.0323 117 GLU B N   
3242 C  CA  . GLU B  118 ? 0.0845  0.1138 0.0907  0.0038  -0.0088 -0.0232 117 GLU B CA  
3243 C  C   . GLU B  118 ? 0.0928  0.1368 0.0644  0.0098  -0.0021 -0.0257 117 GLU B C   
3244 O  O   . GLU B  118 ? 0.1260  0.1465 0.0641  0.0125  -0.0032 -0.0228 117 GLU B O   
3245 C  CB  . GLU B  118 ? 0.0968  0.1430 0.1133  -0.0029 -0.0100 -0.0230 117 GLU B CB  
3246 C  CG  . GLU B  118 ? 0.1120  0.1319 0.1205  -0.0076 -0.0199 -0.0458 117 GLU B CG  
3247 C  CD  . GLU B  118 ? 0.1020  0.1556 0.0967  -0.0119 0.0179  -0.0306 117 GLU B CD  
3248 O  OE1 . GLU B  118 ? 0.1023  0.1725 0.1180  -0.0189 0.0084  -0.0623 117 GLU B OE1 
3249 O  OE2 . GLU B  118 ? 0.1155  0.1377 0.1181  -0.0027 -0.0037 -0.0386 117 GLU B OE2 
3250 N  N   . LEU B  119 ? 0.0967  0.1177 0.0793  0.0106  -0.0100 -0.0215 118 LEU B N   
3251 C  CA  . LEU B  119 ? 0.0803  0.1241 0.1155  0.0036  0.0005  -0.0183 118 LEU B CA  
3252 C  C   . LEU B  119 ? 0.0976  0.1452 0.0673  0.0054  -0.0111 -0.0307 118 LEU B C   
3253 O  O   . LEU B  119 ? 0.0964  0.1527 0.0765  0.0046  -0.0068 -0.0276 118 LEU B O   
3254 C  CB  . LEU B  119 ? 0.1044  0.1234 0.0750  -0.0012 0.0035  -0.0130 118 LEU B CB  
3255 C  CG  . LEU B  119 ? 0.1159  0.1172 0.0925  0.0119  -0.0111 -0.0092 118 LEU B CG  
3256 C  CD1 . LEU B  119 ? 0.1142  0.1535 0.1005  0.0120  -0.0065 -0.0331 118 LEU B CD1 
3257 C  CD2 . LEU B  119 ? 0.1567  0.1287 0.1181  0.0168  -0.0122 0.0162  118 LEU B CD2 
3258 N  N   . HIS B  120 ? 0.0899  0.1269 0.0872  0.0100  -0.0019 -0.0331 119 HIS B N   
3259 C  CA  . HIS B  120 ? 0.0820  0.1225 0.0937  0.0058  -0.0030 -0.0193 119 HIS B CA  
3260 C  C   . HIS B  120 ? 0.0822  0.1280 0.0892  -0.0075 -0.0152 -0.0284 119 HIS B C   
3261 O  O   . HIS B  120 ? 0.0976  0.1470 0.0864  0.0079  -0.0181 -0.0357 119 HIS B O   
3262 C  CB  . HIS B  120 ? 0.0979  0.1172 0.1056  0.0039  -0.0033 -0.0254 119 HIS B CB  
3263 C  CG  . HIS B  120 ? 0.0845  0.1195 0.0989  -0.0025 -0.0223 -0.0311 119 HIS B CG  
3264 N  ND1 . HIS B  120 ? 0.0932  0.1273 0.0891  -0.0046 0.0074  -0.0362 119 HIS B ND1 
3265 C  CD2 . HIS B  120 ? 0.1021  0.1373 0.0973  -0.0098 -0.0087 -0.0357 119 HIS B CD2 
3266 C  CE1 . HIS B  120 ? 0.0880  0.1391 0.0915  0.0009  0.0034  -0.0472 119 HIS B CE1 
3267 N  NE2 . HIS B  120 ? 0.0952  0.1337 0.0977  0.0059  -0.0020 -0.0259 119 HIS B NE2 
3268 N  N   . VAL B  121 ? 0.0882  0.1544 0.0900  0.0188  -0.0196 -0.0242 120 VAL B N   
3269 C  CA  . VAL B  121 ? 0.0795  0.1441 0.1225  0.0166  -0.0121 -0.0301 120 VAL B CA  
3270 C  C   . VAL B  121 ? 0.0828  0.1384 0.1084  0.0129  -0.0232 -0.0580 120 VAL B C   
3271 O  O   . VAL B  121 ? 0.1005  0.1574 0.1199  0.0077  -0.0305 -0.0552 120 VAL B O   
3272 C  CB  . VAL B  121 ? 0.1016  0.1483 0.1172  0.0127  -0.0189 -0.0138 120 VAL B CB  
3273 C  CG1 . VAL B  121 ? 0.1208  0.1549 0.1441  0.0137  -0.0291 -0.0469 120 VAL B CG1 
3274 C  CG2 . VAL B  121 ? 0.1067  0.1876 0.1203  0.0178  -0.0052 0.0004  120 VAL B CG2 
3275 N  N   . ALA B  122 ? 0.0849  0.1639 0.1102  0.0093  -0.0036 -0.0441 121 ALA B N   
3276 C  CA  . ALA B  122 ? 0.0750  0.1707 0.1571  0.0093  0.0098  -0.0754 121 ALA B CA  
3277 C  C   . ALA B  122 ? 0.1064  0.1869 0.1359  0.0214  -0.0119 -0.0851 121 ALA B C   
3278 O  O   . ALA B  122 ? 0.0892  0.2084 0.2256  0.0345  -0.0354 -0.1147 121 ALA B O   
3279 C  CB  . ALA B  122 ? 0.1272  0.2034 0.1483  -0.0052 0.0050  -0.0543 121 ALA B CB  
3280 N  N   . HIS B  123 ? 0.0844  0.2127 0.1797  0.0145  -0.0221 -0.0901 122 HIS B N   
3281 C  CA  . HIS B  123 ? 0.0828  0.2296 0.1905  0.0263  -0.0315 -0.0917 122 HIS B CA  
3282 C  C   . HIS B  123 ? 0.0826  0.2222 0.2285  0.0228  -0.0322 -0.1282 122 HIS B C   
3283 O  O   . HIS B  123 ? 0.0967  0.2231 0.2267  0.0117  -0.0132 -0.1189 122 HIS B O   
3284 C  CB  . HIS B  123 ? 0.0995  0.2134 0.2053  0.0173  -0.0348 -0.0642 122 HIS B CB  
3285 C  CG  . HIS B  123 ? 0.0979  0.1876 0.1720  0.0219  -0.0436 -0.0889 122 HIS B CG  
3286 N  ND1 . HIS B  123 ? 0.0969  0.1851 0.1750  0.0219  -0.0370 -0.0600 122 HIS B ND1 
3287 C  CD2 . HIS B  123 ? 0.1102  0.2102 0.1621  0.0277  -0.0424 -0.0708 122 HIS B CD2 
3288 C  CE1 . HIS B  123 ? 0.1294  0.1729 0.1635  0.0085  -0.0364 -0.0630 122 HIS B CE1 
3289 N  NE2 . HIS B  123 ? 0.1430  0.1937 0.1535  0.0198  -0.0545 -0.0573 122 HIS B NE2 
3290 N  N   . TRP B  124 ? 0.0934  0.2327 0.1869  0.0293  -0.0248 -0.0986 123 TRP B N   
3291 C  CA  . TRP B  124 ? 0.0820  0.2398 0.2346  0.0236  -0.0181 -0.1052 123 TRP B CA  
3292 C  C   . TRP B  124 ? 0.1107  0.2037 0.2684  0.0296  -0.0293 -0.0964 123 TRP B C   
3293 O  O   . TRP B  124 ? 0.1102  0.2120 0.2526  0.0201  -0.0353 -0.0839 123 TRP B O   
3294 C  CB  . TRP B  124 ? 0.1137  0.2332 0.2131  0.0016  -0.0057 -0.1028 123 TRP B CB  
3295 C  CG  . TRP B  124 ? 0.1022  0.2422 0.2451  0.0245  0.0124  -0.1230 123 TRP B CG  
3296 C  CD1 . TRP B  124 ? 0.1409  0.2368 0.1732  0.0037  0.0179  -0.0917 123 TRP B CD1 
3297 C  CD2 . TRP B  124 ? 0.1097  0.2694 0.3114  0.0343  -0.0177 -0.1463 123 TRP B CD2 
3298 N  NE1 . TRP B  124 ? 0.0970  0.2477 0.2536  0.0221  0.0110  -0.0960 123 TRP B NE1 
3299 C  CE2 . TRP B  124 ? 0.1150  0.2737 0.2766  0.0306  0.0067  -0.1386 123 TRP B CE2 
3300 C  CE3 . TRP B  124 ? 0.0873  0.4199 0.4092  0.0417  0.0088  -0.2452 123 TRP B CE3 
3301 C  CZ2 . TRP B  124 ? 0.1195  0.3485 0.3811  0.0694  0.0168  -0.1852 123 TRP B CZ2 
3302 C  CZ3 . TRP B  124 ? 0.1044  0.4052 0.5245  0.0696  -0.0369 -0.2434 123 TRP B CZ3 
3303 C  CH2 . TRP B  124 ? 0.1420  0.4501 0.5153  0.1209  -0.0568 -0.2737 123 TRP B CH2 
3304 N  N   . ASN B  125 ? 0.0882  0.2317 0.2666  0.0192  -0.0436 -0.0952 124 ASN B N   
3305 C  CA  . ASN B  125 ? 0.1076  0.2460 0.3208  0.0454  -0.0617 -0.1348 124 ASN B CA  
3306 C  C   . ASN B  125 ? 0.0855  0.2508 0.3873  0.0141  -0.0348 -0.1443 124 ASN B C   
3307 O  O   . ASN B  125 ? 0.0916  0.2903 0.3786  0.0279  -0.0467 -0.1509 124 ASN B O   
3308 C  CB  . ASN B  125 ? 0.1323  0.2206 0.2896  0.0368  -0.0647 -0.1218 124 ASN B CB  
3309 C  CG  . ASN B  125 ? 0.1624  0.2715 0.3280  0.0753  -0.0774 -0.1326 124 ASN B CG  
3310 O  OD1 . ASN B  125 ? 0.1344  0.2640 0.4009  0.0375  -0.1016 -0.0729 124 ASN B OD1 
3311 N  ND2 . ASN B  125 ? 0.1757  0.3208 0.3473  0.0597  -0.1016 -0.1638 124 ASN B ND2 
3312 N  N   . SER B  126 ? 0.1220  0.2485 0.4841  0.0325  -0.0588 -0.1525 125 SER B N   
3313 C  CA  . SER B  126 ? 0.1205  0.2493 0.5229  0.0576  -0.0536 -0.1826 125 SER B CA  
3314 C  C   . SER B  126 ? 0.1678  0.3628 0.5272  0.0734  -0.1045 -0.1918 125 SER B C   
3315 O  O   . SER B  126 ? 0.1757  0.3154 0.5661  0.0949  -0.0516 -0.1624 125 SER B O   
3316 C  CB  . SER B  126 ? 0.1703  0.2651 0.5184  0.0465  -0.0401 -0.1296 125 SER B CB  
3317 O  OG  . SER B  126 ? 0.1678  0.2536 0.5220  0.0104  -0.0582 -0.0739 125 SER B OG  
3318 N  N   . ALA B  127 ? 0.1682  0.2873 0.5536  0.0600  -0.1211 -0.1039 126 ALA B N   
3319 C  CA  . ALA B  127 ? 0.2425  0.3582 0.4956  0.1099  -0.1239 -0.0367 126 ALA B CA  
3320 C  C   . ALA B  127 ? 0.1815  0.3240 0.5492  0.0996  -0.1064 -0.1221 126 ALA B C   
3321 O  O   . ALA B  127 ? 0.1628  0.4666 0.7519  0.1258  -0.1131 -0.1679 126 ALA B O   
3322 C  CB  . ALA B  127 ? 0.2579  0.3754 0.5237  0.0103  -0.1146 -0.0335 126 ALA B CB  
3323 N  N   . LYS B  128 ? 0.1772  0.3240 0.3211  0.0396  -0.0568 -0.0925 127 LYS B N   
3324 C  CA  . LYS B  128 ? 0.1409  0.3592 0.3754  0.0555  -0.0944 -0.1036 127 LYS B CA  
3325 C  C   . LYS B  128 ? 0.1119  0.3893 0.3370  0.0487  -0.0447 -0.1342 127 LYS B C   
3326 O  O   . LYS B  128 ? 0.1029  0.5119 0.3721  0.0346  -0.0287 -0.2131 127 LYS B O   
3327 C  CB  . LYS B  128 ? 0.2568  0.4206 0.3510  0.0565  -0.0905 -0.2316 127 LYS B CB  
3328 C  CG  . LYS B  128 ? 0.2476  0.5972 0.4228  0.1009  -0.0998 -0.1842 127 LYS B CG  
3329 C  CD  . LYS B  128 ? 0.7946  0.8232 0.4401  -0.1319 -0.2405 -0.2870 127 LYS B CD  
3330 N  N   . TYR B  129 ? 0.1031  0.2708 0.3503  0.0359  -0.0602 -0.1254 128 TYR B N   
3331 C  CA  . TYR B  129 ? 0.1323  0.3341 0.3527  0.0453  -0.0714 -0.1910 128 TYR B CA  
3332 C  C   . TYR B  129 ? 0.1076  0.3467 0.3829  0.0478  -0.0631 -0.1500 128 TYR B C   
3333 O  O   . TYR B  129 ? 0.1220  0.3305 0.3772  0.0573  -0.0644 -0.1874 128 TYR B O   
3334 C  CB  . TYR B  129 ? 0.1456  0.2712 0.2680  0.0438  -0.0510 -0.1275 128 TYR B CB  
3335 C  CG  . TYR B  129 ? 0.0982  0.2957 0.3319  0.0403  -0.0502 -0.1649 128 TYR B CG  
3336 C  CD1 . TYR B  129 ? 0.1312  0.3036 0.3448  0.0149  -0.0100 -0.1843 128 TYR B CD1 
3337 C  CD2 . TYR B  129 ? 0.1289  0.3305 0.2702  0.0192  -0.0301 -0.1360 128 TYR B CD2 
3338 C  CE1 . TYR B  129 ? 0.1344  0.3466 0.3671  0.0397  -0.0465 -0.2200 128 TYR B CE1 
3339 C  CE2 . TYR B  129 ? 0.1319  0.3294 0.2978  0.0475  -0.0702 -0.1177 128 TYR B CE2 
3340 C  CZ  . TYR B  129 ? 0.1223  0.3869 0.3589  0.0491  -0.0772 -0.2297 128 TYR B CZ  
3341 O  OH  . TYR B  129 ? 0.1398  0.3463 0.4001  0.0234  -0.0315 -0.2303 128 TYR B OH  
3342 N  N   . SER B  130 ? 0.1835  0.3286 0.3592  0.0359  -0.0030 -0.2034 129 SER B N   
3343 C  CA  . SER B  130 ? 0.1337  0.3269 0.3815  0.0480  -0.0290 -0.2111 129 SER B CA  
3344 C  C   . SER B  130 ? 0.1398  0.3305 0.4522  0.0784  -0.0910 -0.2084 129 SER B C   
3345 O  O   . SER B  130 ? 0.1923  0.3301 0.4767  0.0726  -0.0833 -0.2367 129 SER B O   
3346 C  CB  . SER B  130 ? 0.1225  0.4213 0.3674  0.1169  -0.0769 -0.2271 129 SER B CB  
3347 O  OG  . SER B  130 ? 0.1682  0.2892 0.2957  0.0487  -0.0485 -0.1240 129 SER B OG  
3348 N  N   . SER B  131 ? 0.1465  0.3201 0.4691  0.0820  -0.0847 -0.2118 130 SER B N   
3349 C  CA  . SER B  131 ? 0.1344  0.3948 0.5197  0.1410  -0.1037 -0.1746 130 SER B CA  
3350 C  C   . SER B  131 ? 0.1621  0.2888 0.3750  0.0480  -0.0671 -0.1682 130 SER B C   
3351 O  O   . SER B  131 ? 0.1682  0.3226 0.3790  0.0329  -0.0642 -0.2166 130 SER B O   
3352 C  CB  . SER B  131 ? 0.2011  0.3061 0.4932  0.0340  -0.0048 -0.0303 130 SER B CB  
3353 O  OG  . SER B  131 ? 0.3291  0.3758 0.2284  0.0766  -0.0252 -0.0972 130 SER B OG  
3354 N  N   . LEU B  132 ? 0.1610  0.2874 0.3413  0.0718  -0.0570 -0.1703 131 LEU B N   
3355 C  CA  . LEU B  132 ? 0.1562  0.2303 0.2698  0.0407  -0.0406 -0.1193 131 LEU B CA  
3356 C  C   . LEU B  132 ? 0.1962  0.2878 0.2561  0.0086  -0.0423 -0.1383 131 LEU B C   
3357 O  O   . LEU B  132 ? 0.1398  0.2985 0.2379  0.0121  -0.0181 -0.1333 131 LEU B O   
3358 C  CB  . LEU B  132 ? 0.1495  0.2931 0.2477  0.0576  -0.0468 -0.1011 131 LEU B CB  
3359 C  CG  . LEU B  132 ? 0.1549  0.2852 0.1969  0.0322  -0.0204 -0.0952 131 LEU B CG  
3360 C  CD1 . LEU B  132 ? 0.1696  0.3750 0.2450  0.1010  -0.0214 -0.1360 131 LEU B CD1 
3361 C  CD2 . LEU B  132 ? 0.1592  0.2953 0.1932  0.0022  -0.0227 0.0036  131 LEU B CD2 
3362 N  N   . ALA B  133 ? 0.1861  0.3520 0.2120  0.0168  -0.0225 -0.1504 132 ALA B N   
3363 C  CA  . ALA B  133 ? 0.2267  0.4557 0.2037  -0.0423 0.0025  -0.1133 132 ALA B CA  
3364 C  C   . ALA B  133 ? 0.2084  0.3248 0.2160  0.0085  0.0237  -0.1547 132 ALA B C   
3365 O  O   . ALA B  133 ? 0.2099  0.3624 0.2084  0.0254  -0.0006 -0.1034 132 ALA B O   
3366 C  CB  . ALA B  133 ? 0.3599  0.6266 0.2048  0.0104  -0.0019 -0.2318 132 ALA B CB  
3367 N  N   . GLU B  134 ? 0.1606  0.4091 0.2451  0.0487  0.0015  -0.1614 133 GLU B N   
3368 C  CA  . GLU B  134 ? 0.1409  0.4314 0.2507  0.0392  0.0048  -0.1902 133 GLU B CA  
3369 C  C   . GLU B  134 ? 0.1076  0.3334 0.2679  0.0445  -0.0053 -0.1348 133 GLU B C   
3370 O  O   . GLU B  134 ? 0.1743  0.3546 0.2375  -0.0008 0.0253  -0.1383 133 GLU B O   
3371 C  CB  . GLU B  134 ? 0.1465  0.3614 0.3850  0.0473  -0.0079 -0.2365 133 GLU B CB  
3372 C  CG  . GLU B  134 ? 0.1483  0.3474 0.3660  0.0501  -0.0493 -0.1676 133 GLU B CG  
3373 C  CD  . GLU B  134 ? 0.1599  0.3326 0.5707  0.0487  -0.0401 -0.2208 133 GLU B CD  
3374 O  OE1 . GLU B  134 ? 0.1617  0.3923 0.4383  0.0629  -0.0070 -0.2174 133 GLU B OE1 
3375 O  OE2 . GLU B  134 ? 0.1732  0.4009 0.4167  0.0801  -0.0673 -0.1668 133 GLU B OE2 
3376 N  N   . ALA B  135 ? 0.1223  0.2946 0.2339  0.0421  -0.0092 -0.1414 134 ALA B N   
3377 C  CA  . ALA B  135 ? 0.1084  0.2855 0.2300  0.0225  0.0067  -0.1084 134 ALA B CA  
3378 C  C   . ALA B  135 ? 0.0917  0.2945 0.1901  0.0223  -0.0001 -0.0908 134 ALA B C   
3379 O  O   . ALA B  135 ? 0.1409  0.2615 0.1851  0.0280  0.0060  -0.1031 134 ALA B O   
3380 C  CB  . ALA B  135 ? 0.1232  0.2838 0.2186  0.0414  -0.0278 -0.1089 134 ALA B CB  
3381 N  N   . ALA B  136 ? 0.1106  0.2461 0.2002  0.0032  -0.0103 -0.0952 135 ALA B N   
3382 C  CA  . ALA B  136 ? 0.1359  0.2494 0.2064  0.0206  0.0092  -0.0622 135 ALA B CA  
3383 C  C   . ALA B  136 ? 0.1628  0.2648 0.1775  0.0049  0.0131  -0.0822 135 ALA B C   
3384 O  O   . ALA B  136 ? 0.1951  0.2741 0.1714  0.0403  0.0280  -0.0703 135 ALA B O   
3385 C  CB  . ALA B  136 ? 0.1858  0.2623 0.2260  0.0669  -0.0563 -0.0828 135 ALA B CB  
3386 N  N   . SER B  137 ? 0.1624  0.2827 0.2194  -0.0105 0.0157  -0.1144 136 SER B N   
3387 C  CA  . SER B  137 ? 0.2266  0.2705 0.2522  -0.0496 -0.0005 -0.1420 136 SER B CA  
3388 C  C   . SER B  137 ? 0.1976  0.2673 0.2723  -0.0201 0.0143  -0.1430 136 SER B C   
3389 O  O   . SER B  137 ? 0.3304  0.2737 0.2626  -0.0558 -0.0547 -0.0937 136 SER B O   
3390 C  CB  . SER B  137 ? 0.3474  0.2791 0.3204  -0.0475 0.0741  -0.0707 136 SER B CB  
3391 O  OG  . SER B  137 ? 0.3031  0.3898 0.2942  -0.0688 0.1080  -0.0894 136 SER B OG  
3392 N  N   . LYS B  138 ? 0.1355  0.2917 0.1894  0.0010  0.0408  -0.0973 137 LYS B N   
3393 C  CA  . LYS B  138 ? 0.1066  0.3190 0.2296  -0.0110 0.0227  -0.1086 137 LYS B CA  
3394 C  C   . LYS B  138 ? 0.1093  0.2906 0.2271  0.0107  0.0057  -0.1142 137 LYS B C   
3395 O  O   . LYS B  138 ? 0.1049  0.2744 0.1914  0.0026  -0.0013 -0.0891 137 LYS B O   
3396 C  CB  . LYS B  138 ? 0.1337  0.3204 0.2185  0.0271  -0.0011 -0.1123 137 LYS B CB  
3397 C  CG  . LYS B  138 ? 0.1682  0.3930 0.2694  0.0096  0.0142  -0.1834 137 LYS B CG  
3398 C  CD  . LYS B  138 ? 0.1585  0.4945 0.3017  -0.0547 0.0277  -0.1993 137 LYS B CD  
3399 C  CE  . LYS B  138 ? 0.2344  0.5202 0.3301  0.0278  0.0477  -0.2390 137 LYS B CE  
3400 N  NZ  . LYS B  138 ? 0.2558  0.4242 0.3521  -0.0696 0.0939  -0.1874 137 LYS B NZ  
3401 N  N   . ALA B  139 ? 0.1294  0.2946 0.2204  -0.0267 0.0009  -0.1253 138 ALA B N   
3402 C  CA  . ALA B  139 ? 0.1312  0.2497 0.2090  -0.0377 0.0282  -0.0961 138 ALA B CA  
3403 C  C   . ALA B  139 ? 0.1032  0.2583 0.1901  -0.0305 -0.0147 -0.0862 138 ALA B C   
3404 O  O   . ALA B  139 ? 0.1412  0.2407 0.1905  -0.0293 0.0221  -0.0872 138 ALA B O   
3405 C  CB  . ALA B  139 ? 0.1768  0.3143 0.1919  -0.0776 0.0084  -0.0996 138 ALA B CB  
3406 N  N   . ASP B  140 ? 0.1124  0.2554 0.2314  0.0087  -0.0192 -0.0816 139 ASP B N   
3407 C  CA  . ASP B  140 ? 0.1560  0.2411 0.2037  0.0326  -0.0446 -0.0807 139 ASP B CA  
3408 C  C   . ASP B  140 ? 0.1326  0.2425 0.2141  0.0442  -0.0192 -0.0793 139 ASP B C   
3409 O  O   . ASP B  140 ? 0.1312  0.2521 0.2303  0.0209  -0.0592 -0.0993 139 ASP B O   
3410 C  CB  . ASP B  140 ? 0.1657  0.3079 0.2579  0.0449  -0.0855 -0.0974 139 ASP B CB  
3411 C  CG  . ASP B  140 ? 0.1646  0.3269 0.2860  0.0143  -0.0907 -0.1091 139 ASP B CG  
3412 O  OD1 . ASP B  140 ? 0.1351  0.3448 0.3388  0.0458  -0.0399 -0.1620 139 ASP B OD1 
3413 O  OD2 . ASP B  140 ? 0.2242  0.4878 0.3887  0.0963  -0.1326 -0.1551 139 ASP B OD2 
3414 N  N   . GLY B  141 ? 0.1030  0.2525 0.1912  0.0247  -0.0110 -0.0960 140 GLY B N   
3415 C  CA  . GLY B  141 ? 0.1111  0.2611 0.1851  -0.0006 -0.0001 -0.1050 140 GLY B CA  
3416 C  C   . GLY B  141 ? 0.1124  0.2507 0.1542  0.0289  -0.0223 -0.0908 140 GLY B C   
3417 O  O   . GLY B  141 ? 0.1238  0.2398 0.2109  0.0354  -0.0364 -0.0998 140 GLY B O   
3418 N  N   . LEU B  142 ? 0.0973  0.2407 0.1675  0.0247  -0.0210 -0.0851 141 LEU B N   
3419 C  CA  . LEU B  142 ? 0.1089  0.2023 0.1635  0.0071  -0.0179 -0.0780 141 LEU B CA  
3420 C  C   . LEU B  142 ? 0.1012  0.2091 0.1398  0.0226  -0.0262 -0.0687 141 LEU B C   
3421 O  O   . LEU B  142 ? 0.1156  0.2120 0.1606  0.0200  -0.0214 -0.0771 141 LEU B O   
3422 C  CB  . LEU B  142 ? 0.1199  0.2048 0.1553  0.0330  -0.0390 -0.0758 141 LEU B CB  
3423 C  CG  . LEU B  142 ? 0.1427  0.2020 0.1786  0.0193  -0.0130 -0.0864 141 LEU B CG  
3424 C  CD1 . LEU B  142 ? 0.1231  0.2275 0.1675  0.0257  -0.0115 -0.0547 141 LEU B CD1 
3425 C  CD2 . LEU B  142 ? 0.2167  0.2120 0.1826  0.0421  -0.0245 -0.0881 141 LEU B CD2 
3426 N  N   . ALA B  143 ? 0.0882  0.2152 0.1826  0.0107  -0.0068 -0.0933 142 ALA B N   
3427 C  CA  . ALA B  143 ? 0.0817  0.2368 0.1689  0.0319  -0.0194 -0.0529 142 ALA B CA  
3428 C  C   . ALA B  143 ? 0.1044  0.1657 0.1768  0.0062  -0.0178 -0.0708 142 ALA B C   
3429 O  O   . ALA B  143 ? 0.1082  0.1858 0.1973  0.0167  -0.0171 -0.1078 142 ALA B O   
3430 C  CB  . ALA B  143 ? 0.0928  0.2526 0.1718  0.0373  -0.0489 -0.0623 142 ALA B CB  
3431 N  N   . VAL B  144 ? 0.0950  0.1764 0.1488  0.0160  -0.0229 -0.0768 143 VAL B N   
3432 C  CA  . VAL B  144 ? 0.0919  0.1829 0.1402  0.0201  -0.0138 -0.0738 143 VAL B CA  
3433 C  C   . VAL B  144 ? 0.1039  0.1926 0.1305  0.0175  -0.0331 -0.0719 143 VAL B C   
3434 O  O   . VAL B  144 ? 0.1152  0.1869 0.1312  0.0064  -0.0223 -0.0746 143 VAL B O   
3435 C  CB  . VAL B  144 ? 0.1038  0.1617 0.1560  0.0019  -0.0259 -0.0477 143 VAL B CB  
3436 C  CG1 . VAL B  144 ? 0.1067  0.1657 0.1887  -0.0047 -0.0495 -0.0497 143 VAL B CG1 
3437 C  CG2 . VAL B  144 ? 0.1384  0.1962 0.1502  -0.0176 0.0059  -0.0749 143 VAL B CG2 
3438 N  N   . ILE B  145 ? 0.0801  0.1793 0.1181  0.0067  -0.0212 -0.0467 144 ILE B N   
3439 C  CA  . ILE B  145 ? 0.0949  0.1768 0.1111  0.0168  -0.0259 -0.0496 144 ILE B CA  
3440 C  C   . ILE B  145 ? 0.0900  0.1854 0.1002  0.0070  -0.0153 -0.0553 144 ILE B C   
3441 O  O   . ILE B  145 ? 0.1124  0.1908 0.1073  0.0111  -0.0336 -0.0623 144 ILE B O   
3442 C  CB  . ILE B  145 ? 0.1207  0.1743 0.1176  0.0207  -0.0280 -0.0458 144 ILE B CB  
3443 C  CG1 . ILE B  145 ? 0.1276  0.1930 0.1635  0.0303  -0.0394 -0.0476 144 ILE B CG1 
3444 C  CG2 . ILE B  145 ? 0.1305  0.2131 0.1226  0.0245  -0.0122 -0.0316 144 ILE B CG2 
3445 C  CD1 . ILE B  145 ? 0.1614  0.2170 0.2030  0.0059  -0.0256 -0.0374 144 ILE B CD1 
3446 N  N   . GLY B  146 ? 0.0953  0.1527 0.1005  0.0111  -0.0177 -0.0447 145 GLY B N   
3447 C  CA  . GLY B  146 ? 0.0900  0.1955 0.0812  0.0139  -0.0029 -0.0364 145 GLY B CA  
3448 C  C   . GLY B  146 ? 0.0907  0.1908 0.0748  0.0035  -0.0033 -0.0483 145 GLY B C   
3449 O  O   . GLY B  146 ? 0.1120  0.2230 0.0806  0.0029  -0.0145 -0.0527 145 GLY B O   
3450 N  N   . VAL B  147 ? 0.0838  0.1847 0.0937  0.0063  -0.0033 -0.0186 146 VAL B N   
3451 C  CA  . VAL B  147 ? 0.0784  0.1786 0.0941  0.0037  -0.0029 -0.0218 146 VAL B CA  
3452 C  C   . VAL B  147 ? 0.0995  0.1553 0.0671  -0.0018 -0.0057 -0.0294 146 VAL B C   
3453 O  O   . VAL B  147 ? 0.1050  0.1879 0.0718  0.0076  -0.0036 -0.0311 146 VAL B O   
3454 C  CB  . VAL B  147 ? 0.1110  0.1562 0.0979  0.0033  -0.0154 -0.0127 146 VAL B CB  
3455 C  CG1 . VAL B  147 ? 0.1438  0.1908 0.1185  -0.0102 0.0072  0.0006  146 VAL B CG1 
3456 C  CG2 . VAL B  147 ? 0.1111  0.2005 0.1373  0.0131  -0.0292 -0.0135 146 VAL B CG2 
3457 N  N   . LEU B  148 ? 0.0892  0.1685 0.0854  -0.0044 -0.0060 -0.0341 147 LEU B N   
3458 C  CA  . LEU B  148 ? 0.0786  0.1610 0.0944  -0.0070 -0.0061 -0.0436 147 LEU B CA  
3459 C  C   . LEU B  148 ? 0.1032  0.1492 0.0582  -0.0015 0.0096  -0.0331 147 LEU B C   
3460 O  O   . LEU B  148 ? 0.1102  0.1668 0.0724  -0.0113 -0.0004 -0.0281 147 LEU B O   
3461 C  CB  . LEU B  148 ? 0.1287  0.1463 0.1055  -0.0268 0.0072  -0.0477 147 LEU B CB  
3462 C  CG  . LEU B  148 ? 0.1980  0.1883 0.1240  -0.0710 0.0102  -0.0297 147 LEU B CG  
3463 C  CD1 . LEU B  148 ? 0.2493  0.2275 0.1646  -0.0594 -0.0355 -0.0525 147 LEU B CD1 
3464 C  CD2 . LEU B  148 ? 0.1657  0.1775 0.1287  -0.0544 0.0158  -0.0102 147 LEU B CD2 
3465 N  N   . MET B  149 ? 0.0915  0.1664 0.0697  -0.0025 -0.0105 -0.0352 148 MET B N   
3466 C  CA  . MET B  149 ? 0.0831  0.1538 0.0786  0.0024  -0.0019 -0.0430 148 MET B CA  
3467 C  C   . MET B  149 ? 0.0892  0.1395 0.0785  -0.0070 0.0019  -0.0357 148 MET B C   
3468 O  O   . MET B  149 ? 0.1102  0.1430 0.0968  0.0036  0.0088  -0.0126 148 MET B O   
3469 C  CB  . MET B  149 ? 0.1021  0.1535 0.0653  0.0100  0.0019  -0.0346 148 MET B CB  
3470 C  CG  . MET B  149 ? 0.1153  0.1499 0.0759  0.0120  0.0053  -0.0429 148 MET B CG  
3471 S  SD  . MET B  149 ? 0.1084  0.1653 0.0820  0.0033  0.0048  -0.0309 148 MET B SD  
3472 C  CE  . MET B  149 ? 0.1049  0.2134 0.1474  -0.0177 -0.0027 -0.0823 148 MET B CE  
3473 N  N   . LYS B  150 ? 0.0770  0.1782 0.0797  -0.0002 0.0156  -0.0304 149 LYS B N   
3474 C  CA  . LYS B  150 ? 0.0827  0.1897 0.0621  -0.0025 0.0144  -0.0436 149 LYS B CA  
3475 C  C   . LYS B  150 ? 0.0953  0.1567 0.0707  0.0060  0.0102  -0.0456 149 LYS B C   
3476 O  O   . LYS B  150 ? 0.1107  0.1562 0.0774  -0.0017 -0.0077 -0.0221 149 LYS B O   
3477 C  CB  . LYS B  150 ? 0.1014  0.2222 0.0743  -0.0145 0.0147  -0.0469 149 LYS B CB  
3478 C  CG  . LYS B  150 ? 0.1495  0.2206 0.0766  -0.0181 0.0455  -0.0571 149 LYS B CG  
3479 C  CD  . LYS B  150 ? 0.1610  0.3128 0.0881  0.0111  0.0119  -0.0670 149 LYS B CD  
3480 C  CE  . LYS B  150 ? 0.1779  0.3158 0.1395  -0.0013 0.0431  -0.0790 149 LYS B CE  
3481 N  NZ  . LYS B  150 ? 0.1790  0.2824 0.1145  0.0521  0.0262  -0.0206 149 LYS B NZ  
3482 N  N   . VAL B  151 ? 0.0907  0.1747 0.0757  0.0100  0.0164  -0.0245 150 VAL B N   
3483 C  CA  . VAL B  151 ? 0.0819  0.2041 0.0803  -0.0004 0.0074  -0.0058 150 VAL B CA  
3484 C  C   . VAL B  151 ? 0.0935  0.1682 0.0801  0.0001  0.0057  -0.0358 150 VAL B C   
3485 O  O   . VAL B  151 ? 0.1181  0.1980 0.0906  -0.0027 0.0157  -0.0361 150 VAL B O   
3486 C  CB  . VAL B  151 ? 0.1238  0.1700 0.1076  0.0071  -0.0188 -0.0121 150 VAL B CB  
3487 C  CG1 . VAL B  151 ? 0.1488  0.2055 0.1398  0.0377  -0.0052 -0.0231 150 VAL B CG1 
3488 C  CG2 . VAL B  151 ? 0.1398  0.2289 0.1125  -0.0029 -0.0331 -0.0146 150 VAL B CG2 
3489 N  N   . GLY B  152 ? 0.0923  0.1980 0.0910  -0.0159 0.0094  -0.0300 151 GLY B N   
3490 C  CA  . GLY B  152 ? 0.1199  0.2127 0.1030  -0.0358 0.0209  -0.0181 151 GLY B CA  
3491 C  C   . GLY B  152 ? 0.1005  0.1923 0.1067  -0.0105 0.0093  -0.0223 151 GLY B C   
3492 O  O   . GLY B  152 ? 0.1189  0.2161 0.1091  -0.0141 0.0066  -0.0227 151 GLY B O   
3493 N  N   . GLU B  153 ? 0.1305  0.2048 0.1084  -0.0240 0.0205  -0.0171 152 GLU B N   
3494 C  CA  . GLU B  153 ? 0.1488  0.2034 0.1234  -0.0248 0.0379  -0.0111 152 GLU B CA  
3495 C  C   . GLU B  153 ? 0.1068  0.1973 0.0883  -0.0070 -0.0020 -0.0041 152 GLU B C   
3496 O  O   . GLU B  153 ? 0.1229  0.2199 0.1111  -0.0222 0.0051  -0.0354 152 GLU B O   
3497 C  CB  . GLU B  153 ? 0.2568  0.2063 0.1152  -0.0454 0.0643  -0.0139 152 GLU B CB  
3498 C  CG  . GLU B  153 ? 0.2849  0.2558 0.1700  -0.0264 0.0798  -0.0017 152 GLU B CG  
3499 C  CD  . GLU B  153 ? 0.2655  0.5392 0.3664  -0.1055 0.2067  -0.0497 152 GLU B CD  
3500 O  OE1 . GLU B  153 ? 0.5444  0.6324 0.3876  -0.2879 0.1128  -0.0820 152 GLU B OE1 
3501 O  OE2 . GLU B  153 ? 0.3208  0.7249 0.7095  -0.0486 0.2157  -0.2691 152 GLU B OE2 
3502 N  N   . ALA B  154 ? 0.1195  0.2109 0.1080  -0.0159 0.0089  -0.0223 153 ALA B N   
3503 C  CA  . ALA B  154 ? 0.1359  0.1984 0.1129  0.0055  -0.0111 -0.0355 153 ALA B CA  
3504 C  C   . ALA B  154 ? 0.1488  0.1513 0.1014  -0.0326 -0.0004 -0.0036 153 ALA B C   
3505 O  O   . ALA B  154 ? 0.1738  0.2089 0.1258  -0.0258 0.0234  0.0097  153 ALA B O   
3506 C  CB  . ALA B  154 ? 0.1822  0.2429 0.0988  -0.0247 -0.0130 -0.0563 153 ALA B CB  
3507 N  N   . ASN B  155 ? 0.1319  0.1729 0.0985  -0.0075 -0.0044 -0.0232 154 ASN B N   
3508 C  CA  . ASN B  155 ? 0.1456  0.1840 0.0906  0.0023  -0.0096 -0.0221 154 ASN B CA  
3509 C  C   . ASN B  155 ? 0.1355  0.1786 0.0964  -0.0160 0.0066  -0.0084 154 ASN B C   
3510 O  O   . ASN B  155 ? 0.1235  0.1858 0.0995  -0.0062 0.0080  -0.0071 154 ASN B O   
3511 C  CB  . ASN B  155 ? 0.1316  0.1588 0.1333  -0.0053 -0.0301 -0.0088 154 ASN B CB  
3512 C  CG  . ASN B  155 ? 0.1481  0.1624 0.1578  0.0380  -0.0501 -0.0491 154 ASN B CG  
3513 O  OD1 . ASN B  155 ? 0.1869  0.1581 0.2587  0.0236  -0.0919 -0.0340 154 ASN B OD1 
3514 N  ND2 . ASN B  155 ? 0.1326  0.2041 0.1380  -0.0102 -0.0326 -0.0336 154 ASN B ND2 
3515 N  N   . PRO B  156 ? 0.1800  0.1646 0.1146  -0.0062 -0.0063 0.0051  155 PRO B N   
3516 C  CA  . PRO B  156 ? 0.1840  0.1682 0.1596  -0.0390 0.0389  -0.0221 155 PRO B CA  
3517 C  C   . PRO B  156 ? 0.1718  0.1628 0.1377  0.0093  -0.0129 0.0197  155 PRO B C   
3518 O  O   . PRO B  156 ? 0.2023  0.1657 0.1567  -0.0043 0.0065  -0.0181 155 PRO B O   
3519 C  CB  . PRO B  156 ? 0.2217  0.1969 0.1757  -0.0150 0.0435  0.0247  155 PRO B CB  
3520 C  CG  . PRO B  156 ? 0.4939  0.1980 0.2005  -0.0697 0.1446  0.0081  155 PRO B CG  
3521 C  CD  . PRO B  156 ? 0.2615  0.1689 0.1348  -0.0127 0.0460  0.0417  155 PRO B CD  
3522 N  N   . LYS B  157 ? 0.1556  0.2034 0.1355  -0.0044 -0.0299 0.0458  156 LYS B N   
3523 C  CA  . LYS B  157 ? 0.1488  0.2579 0.1377  0.0136  -0.0122 0.0484  156 LYS B CA  
3524 C  C   . LYS B  157 ? 0.1592  0.2023 0.1057  -0.0100 -0.0103 -0.0308 156 LYS B C   
3525 O  O   . LYS B  157 ? 0.1876  0.2041 0.1865  0.0105  0.0433  -0.0037 156 LYS B O   
3526 C  CB  . LYS B  157 ? 0.2267  0.3110 0.1452  0.0427  -0.0521 0.0395  156 LYS B CB  
3527 C  CG  . LYS B  157 ? 0.3930  0.5808 0.1386  -0.0065 -0.0743 0.1100  156 LYS B CG  
3528 C  CD  . LYS B  157 ? 0.5123  0.7278 0.3668  -0.0580 -0.0211 0.3536  156 LYS B CD  
3529 C  CE  . LYS B  157 ? 0.8315  0.8130 0.3230  0.2000  0.0134  0.3251  156 LYS B CE  
3530 N  NZ  . LYS B  157 ? 0.7928  0.5019 0.2495  -0.1629 0.0323  0.0469  156 LYS B NZ  
3531 N  N   . LEU B  158 ? 0.1779  0.1761 0.1274  0.0120  0.0242  0.0315  157 LEU B N   
3532 C  CA  . LEU B  158 ? 0.1465  0.1653 0.1452  -0.0029 0.0436  0.0283  157 LEU B CA  
3533 C  C   . LEU B  158 ? 0.1833  0.1524 0.1470  -0.0245 -0.0105 0.0052  157 LEU B C   
3534 O  O   . LEU B  158 ? 0.1678  0.2027 0.1351  0.0183  0.0250  0.0190  157 LEU B O   
3535 C  CB  . LEU B  158 ? 0.1639  0.1481 0.1614  -0.0046 0.0129  -0.0217 157 LEU B CB  
3536 C  CG  . LEU B  158 ? 0.1294  0.1592 0.1362  -0.0004 0.0064  -0.0447 157 LEU B CG  
3537 C  CD1 . LEU B  158 ? 0.1908  0.2224 0.1835  0.0043  -0.0089 -0.0938 157 LEU B CD1 
3538 C  CD2 . LEU B  158 ? 0.1111  0.2461 0.3729  -0.0111 -0.0294 -0.1248 157 LEU B CD2 
3539 N  N   . GLN B  159 ? 0.1854  0.1596 0.1251  -0.0083 -0.0129 0.0062  158 GLN B N   
3540 C  CA  . GLN B  159 ? 0.2257  0.2371 0.1196  0.0156  0.0021  -0.0529 158 GLN B CA  
3541 C  C   . GLN B  159 ? 0.1617  0.1657 0.1542  -0.0015 0.0443  0.0311  158 GLN B C   
3542 O  O   . GLN B  159 ? 0.1614  0.2064 0.1316  -0.0275 -0.0027 0.0328  158 GLN B O   
3543 C  CB  . GLN B  159 ? 0.1711  0.2264 0.1289  -0.0425 0.0185  -0.0161 158 GLN B CB  
3544 C  CG  . GLN B  159 ? 0.2048  0.3309 0.1373  -0.0447 0.0115  -0.0013 158 GLN B CG  
3545 C  CD  . GLN B  159 ? 0.1588  0.5649 0.2005  0.0784  -0.0059 -0.0671 158 GLN B CD  
3546 O  OE1 . GLN B  159 ? 0.1822  0.3869 0.2398  0.0300  0.0359  -0.0557 158 GLN B OE1 
3547 N  NE2 . GLN B  159 ? 0.2561  0.5302 0.2194  0.0939  -0.0570 -0.0593 158 GLN B NE2 
3548 N  N   . LYS B  160 ? 0.1549  0.1524 0.1263  -0.0006 0.0153  -0.0223 159 LYS B N   
3549 C  CA  . LYS B  160 ? 0.1725  0.1567 0.1330  -0.0089 0.0375  -0.0119 159 LYS B CA  
3550 C  C   . LYS B  160 ? 0.1124  0.1524 0.1101  -0.0052 0.0061  0.0030  159 LYS B C   
3551 O  O   . LYS B  160 ? 0.1538  0.1754 0.1267  -0.0135 0.0074  -0.0006 159 LYS B O   
3552 C  CB  . LYS B  160 ? 0.1804  0.1782 0.1448  0.0161  0.0052  -0.0215 159 LYS B CB  
3553 C  CG  . LYS B  160 ? 0.1876  0.1905 0.1858  0.0237  -0.0005 -0.0495 159 LYS B CG  
3554 C  CD  . LYS B  160 ? 0.1966  0.2142 0.1861  0.0413  -0.0255 -0.0571 159 LYS B CD  
3555 C  CE  . LYS B  160 ? 0.2062  0.1689 0.2228  0.0259  0.0024  -0.0575 159 LYS B CE  
3556 N  NZ  . LYS B  160 ? 0.1914  0.2077 0.2665  -0.0013 0.0302  -0.0696 159 LYS B NZ  
3557 N  N   . VAL B  161 ? 0.1120  0.1452 0.1897  -0.0267 -0.0168 0.0174  160 VAL B N   
3558 C  CA  . VAL B  161 ? 0.0988  0.1441 0.1578  -0.0203 0.0057  -0.0149 160 VAL B CA  
3559 C  C   . VAL B  161 ? 0.1220  0.1287 0.1234  0.0053  0.0195  -0.0151 160 VAL B C   
3560 O  O   . VAL B  161 ? 0.1420  0.1639 0.1257  -0.0126 0.0311  -0.0248 160 VAL B O   
3561 C  CB  . VAL B  161 ? 0.1269  0.1434 0.1438  -0.0174 0.0115  -0.0157 160 VAL B CB  
3562 C  CG1 . VAL B  161 ? 0.3862  0.2163 0.1423  -0.1656 -0.0280 0.0023  160 VAL B CG1 
3563 C  CG2 . VAL B  161 ? 0.1326  0.2248 0.2928  0.0079  -0.0298 -0.0673 160 VAL B CG2 
3564 N  N   . LEU B  162 ? 0.1020  0.1764 0.1176  0.0260  0.0032  0.0029  161 LEU B N   
3565 C  CA  . LEU B  162 ? 0.1531  0.1897 0.1128  0.0567  0.0130  -0.0274 161 LEU B CA  
3566 C  C   . LEU B  162 ? 0.1283  0.2077 0.0873  0.0356  0.0136  -0.0066 161 LEU B C   
3567 O  O   . LEU B  162 ? 0.1578  0.2257 0.0941  0.0444  0.0037  -0.0060 161 LEU B O   
3568 C  CB  . LEU B  162 ? 0.1711  0.3054 0.1093  0.0907  -0.0037 -0.0554 161 LEU B CB  
3569 C  CG  . LEU B  162 ? 0.1980  0.2231 0.1384  0.0703  0.0223  -0.0402 161 LEU B CG  
3570 C  CD1 . LEU B  162 ? 0.1639  0.3491 0.1405  0.0491  0.0225  -0.0730 161 LEU B CD1 
3571 C  CD2 . LEU B  162 ? 0.3697  0.1894 0.1797  -0.0117 0.0868  -0.0666 161 LEU B CD2 
3572 N  N   . ASP B  163 ? 0.1007  0.2089 0.1238  0.0021  0.0293  0.0093  162 ASP B N   
3573 C  CA  . ASP B  163 ? 0.1448  0.2522 0.1093  -0.0212 0.0100  0.0082  162 ASP B CA  
3574 C  C   . ASP B  163 ? 0.1083  0.1897 0.1056  -0.0110 0.0145  -0.0116 162 ASP B C   
3575 O  O   . ASP B  163 ? 0.1230  0.2734 0.1153  -0.0295 -0.0052 -0.0038 162 ASP B O   
3576 C  CB  . ASP B  163 ? 0.1398  0.2185 0.1639  -0.0047 0.0284  0.0314  162 ASP B CB  
3577 C  CG  . ASP B  163 ? 0.1509  0.2992 0.1402  -0.0046 -0.0137 0.0355  162 ASP B CG  
3578 O  OD1 . ASP B  163 ? 0.1574  0.3312 0.2500  0.0221  0.0596  0.0899  162 ASP B OD1 
3579 O  OD2 . ASP B  163 ? 0.2514  0.3129 0.1944  -0.0364 0.0358  0.0675  162 ASP B OD2 
3580 N  N   . ALA B  164 ? 0.0952  0.1610 0.1058  -0.0106 0.0047  -0.0034 163 ALA B N   
3581 C  CA  . ALA B  164 ? 0.1047  0.1617 0.0845  -0.0167 0.0106  -0.0067 163 ALA B CA  
3582 C  C   . ALA B  164 ? 0.0970  0.1581 0.0881  0.0000  0.0160  -0.0042 163 ALA B C   
3583 O  O   . ALA B  164 ? 0.1120  0.1883 0.0840  0.0019  0.0099  -0.0035 163 ALA B O   
3584 C  CB  . ALA B  164 ? 0.0989  0.1520 0.1391  0.0031  -0.0044 -0.0012 163 ALA B CB  
3585 N  N   . LEU B  165 ? 0.1073  0.1445 0.0900  -0.0129 0.0044  -0.0008 164 LEU B N   
3586 C  CA  . LEU B  165 ? 0.1330  0.1427 0.0838  -0.0132 -0.0044 -0.0052 164 LEU B CA  
3587 C  C   . LEU B  165 ? 0.1111  0.1506 0.0952  0.0000  -0.0096 -0.0251 164 LEU B C   
3588 O  O   . LEU B  165 ? 0.1088  0.1588 0.0880  0.0099  0.0077  -0.0097 164 LEU B O   
3589 C  CB  . LEU B  165 ? 0.1330  0.1761 0.0862  0.0027  -0.0001 -0.0320 164 LEU B CB  
3590 C  CG  . LEU B  165 ? 0.1445  0.1743 0.1040  0.0138  -0.0114 -0.0309 164 LEU B CG  
3591 C  CD1 . LEU B  165 ? 0.2091  0.1883 0.1144  0.0388  -0.0380 -0.0464 164 LEU B CD1 
3592 C  CD2 . LEU B  165 ? 0.1567  0.1707 0.1477  -0.0062 -0.0593 -0.0385 164 LEU B CD2 
3593 N  N   . GLN B  166 ? 0.1118  0.1736 0.0862  -0.0053 -0.0080 -0.0100 165 GLN B N   
3594 C  CA  . GLN B  166 ? 0.1023  0.1905 0.0876  -0.0055 -0.0098 -0.0051 165 GLN B CA  
3595 C  C   . GLN B  166 ? 0.1220  0.1567 0.0874  -0.0119 0.0044  0.0041  165 GLN B C   
3596 O  O   . GLN B  166 ? 0.1355  0.1804 0.0847  -0.0075 0.0024  0.0027  165 GLN B O   
3597 C  CB  . GLN B  166 ? 0.1280  0.1930 0.1743  -0.0317 0.0113  -0.0053 165 GLN B CB  
3598 C  CG  . GLN B  166 ? 0.1470  0.1919 0.2156  -0.0182 0.0113  -0.0152 165 GLN B CG  
3599 C  CD  . GLN B  166 ? 0.1456  0.1851 0.1344  -0.0187 -0.0177 0.0245  165 GLN B CD  
3600 O  OE1 . GLN B  166 ? 0.1937  0.2084 0.1641  -0.0164 -0.0096 -0.0175 165 GLN B OE1 
3601 N  NE2 . GLN B  166 ? 0.1657  0.2178 0.1599  -0.0104 0.0038  0.0215  165 GLN B NE2 
3602 N  N   . ALA B  167 ? 0.1176  0.1506 0.0926  -0.0043 0.0164  -0.0023 166 ALA B N   
3603 C  CA  . ALA B  167 ? 0.1289  0.1430 0.1178  -0.0130 0.0181  0.0005  166 ALA B CA  
3604 C  C   . ALA B  167 ? 0.0980  0.1289 0.0978  0.0077  0.0086  0.0041  166 ALA B C   
3605 O  O   . ALA B  167 ? 0.1362  0.1373 0.1084  -0.0034 0.0210  -0.0087 166 ALA B O   
3606 C  CB  . ALA B  167 ? 0.1930  0.1470 0.1894  0.0239  0.0500  0.0530  166 ALA B CB  
3607 N  N   . ILE B  168 ? 0.1133  0.1092 0.0917  0.0002  -0.0115 -0.0013 167 ILE B N   
3608 C  CA  . ILE B  168 ? 0.1003  0.1089 0.0962  -0.0025 -0.0060 -0.0055 167 ILE B CA  
3609 C  C   . ILE B  168 ? 0.0899  0.1213 0.0829  -0.0058 0.0110  -0.0104 167 ILE B C   
3610 O  O   . ILE B  168 ? 0.1014  0.1243 0.0910  -0.0061 -0.0077 -0.0022 167 ILE B O   
3611 C  CB  . ILE B  168 ? 0.0900  0.1553 0.0882  0.0086  -0.0102 -0.0032 167 ILE B CB  
3612 C  CG1 . ILE B  168 ? 0.1098  0.1445 0.0864  -0.0122 -0.0034 -0.0186 167 ILE B CG1 
3613 C  CG2 . ILE B  168 ? 0.1205  0.1474 0.1137  0.0310  -0.0073 0.0080  167 ILE B CG2 
3614 C  CD1 . ILE B  168 ? 0.1341  0.1987 0.0961  -0.0402 -0.0319 -0.0052 167 ILE B CD1 
3615 N  N   . LYS B  169 ? 0.0979  0.1412 0.0879  0.0138  0.0013  -0.0034 168 LYS B N   
3616 C  CA  . LYS B  169 ? 0.0838  0.1186 0.1005  0.0018  -0.0096 -0.0078 168 LYS B CA  
3617 C  C   . LYS B  169 ? 0.0818  0.1181 0.0925  0.0082  0.0082  -0.0194 168 LYS B C   
3618 O  O   . LYS B  169 ? 0.1055  0.1287 0.1016  0.0032  0.0085  -0.0151 168 LYS B O   
3619 C  CB  . LYS B  169 ? 0.1098  0.2398 0.1038  -0.0249 -0.0322 0.0168  168 LYS B CB  
3620 C  CG  . LYS B  169 ? 0.1993  0.2834 0.1693  -0.0675 0.0351  0.0057  168 LYS B CG  
3621 C  CD  . LYS B  169 ? 0.2303  0.3280 0.2066  -0.0458 0.1002  -0.0434 168 LYS B CD  
3622 C  CE  . LYS B  169 ? 0.2048  0.3528 0.1671  -0.0048 -0.0230 -0.0395 168 LYS B CE  
3623 N  NZ  . LYS B  169 ? 0.2346  0.4088 0.1779  0.1129  0.0067  0.0512  168 LYS B NZ  
3624 N  N   . THR B  170 ? 0.0773  0.1513 0.0773  0.0055  0.0002  -0.0104 169 THR B N   
3625 C  CA  . THR B  170 ? 0.0820  0.1456 0.0829  -0.0084 0.0046  0.0048  169 THR B CA  
3626 C  C   . THR B  170 ? 0.0835  0.1323 0.0838  0.0184  0.0044  -0.0048 169 THR B C   
3627 O  O   . THR B  170 ? 0.0916  0.1502 0.0829  0.0125  0.0022  -0.0107 169 THR B O   
3628 C  CB  . THR B  170 ? 0.1128  0.1341 0.0882  0.0119  -0.0149 -0.0236 169 THR B CB  
3629 O  OG1 . THR B  170 ? 0.1055  0.1492 0.0944  -0.0019 -0.0155 -0.0130 169 THR B OG1 
3630 C  CG2 . THR B  170 ? 0.0845  0.1804 0.1032  0.0129  0.0088  -0.0097 169 THR B CG2 
3631 N  N   A LYS B  171 ? 0.0864  0.1416 0.1020  -0.0023 0.0111  -0.0055 170 LYS B N   
3632 N  N   B LYS B  171 ? 0.0919  0.1517 0.0960  -0.0103 0.0166  0.0008  170 LYS B N   
3633 C  CA  A LYS B  171 ? 0.0786  0.1668 0.0980  -0.0027 0.0128  -0.0152 170 LYS B CA  
3634 C  CA  B LYS B  171 ? 0.0838  0.1621 0.0924  -0.0116 0.0197  -0.0073 170 LYS B CA  
3635 C  C   A LYS B  171 ? 0.0905  0.1908 0.0837  -0.0057 0.0115  -0.0117 170 LYS B C   
3636 C  C   B LYS B  171 ? 0.0838  0.1973 0.0767  -0.0130 0.0116  -0.0103 170 LYS B C   
3637 O  O   A LYS B  171 ? 0.1057  0.1817 0.0908  0.0096  -0.0037 -0.0159 170 LYS B O   
3638 O  O   B LYS B  171 ? 0.1066  0.2107 0.0715  -0.0144 0.0236  -0.0096 170 LYS B O   
3639 C  CB  A LYS B  171 ? 0.1093  0.1502 0.1273  -0.0005 0.0320  -0.0383 170 LYS B CB  
3640 C  CB  B LYS B  171 ? 0.1133  0.1775 0.1362  -0.0510 -0.0059 0.0105  170 LYS B CB  
3641 C  CG  A LYS B  171 ? 0.1063  0.1908 0.1901  -0.0205 0.0133  0.0204  170 LYS B CG  
3642 C  CG  B LYS B  171 ? 0.0996  0.1847 0.1714  -0.0323 0.0069  0.0079  170 LYS B CG  
3643 C  CD  A LYS B  171 ? 0.1294  0.2091 0.2002  0.0238  0.0844  0.0122  170 LYS B CD  
3644 C  CD  B LYS B  171 ? 0.0891  0.2231 0.2264  -0.0663 -0.0203 0.0468  170 LYS B CD  
3645 C  CE  A LYS B  171 ? 0.1610  0.1930 0.3154  -0.0537 0.0215  0.0785  170 LYS B CE  
3646 C  CE  B LYS B  171 ? 0.2946  0.2716 0.2053  -0.0774 0.0131  0.0315  170 LYS B CE  
3647 N  NZ  A LYS B  171 ? 0.2575  0.2264 0.6184  -0.1141 -0.0432 0.1474  170 LYS B NZ  
3648 N  NZ  B LYS B  171 ? 0.5713  0.2781 0.4612  -0.0920 -0.0701 -0.0628 170 LYS B NZ  
3649 N  N   . GLY B  172 ? 0.0812  0.1919 0.0916  -0.0022 0.0052  0.0011  171 GLY B N   
3650 C  CA  . GLY B  172 ? 0.0989  0.1879 0.1384  0.0141  0.0181  -0.0162 171 GLY B CA  
3651 C  C   . GLY B  172 ? 0.0944  0.1872 0.1093  0.0244  -0.0020 -0.0039 171 GLY B C   
3652 O  O   . GLY B  172 ? 0.1176  0.2102 0.1213  0.0337  0.0212  0.0015  171 GLY B O   
3653 N  N   . LYS B  173 ? 0.1032  0.1675 0.0891  0.0000  0.0040  -0.0059 172 LYS B N   
3654 C  CA  . LYS B  173 ? 0.1040  0.1743 0.0794  0.0144  -0.0094 -0.0172 172 LYS B CA  
3655 C  C   . LYS B  173 ? 0.0942  0.1483 0.0797  0.0226  0.0051  -0.0231 172 LYS B C   
3656 O  O   . LYS B  173 ? 0.1323  0.1398 0.0838  0.0077  -0.0004 -0.0266 172 LYS B O   
3657 C  CB  . LYS B  173 ? 0.0901  0.1757 0.1002  0.0158  -0.0038 -0.0011 172 LYS B CB  
3658 C  CG  . LYS B  173 ? 0.1014  0.1829 0.0960  0.0159  -0.0184 -0.0162 172 LYS B CG  
3659 C  CD  . LYS B  173 ? 0.1046  0.1664 0.1316  -0.0119 -0.0268 -0.0088 172 LYS B CD  
3660 C  CE  . LYS B  173 ? 0.1229  0.1567 0.1481  -0.0054 -0.0012 -0.0156 172 LYS B CE  
3661 N  NZ  . LYS B  173 ? 0.1252  0.1948 0.1373  0.0005  0.0038  0.0015  172 LYS B NZ  
3662 N  N   . ARG B  174 ? 0.1344  0.1445 0.0827  0.0200  -0.0113 -0.0328 173 ARG B N   
3663 C  CA  . ARG B  174 ? 0.1179  0.1373 0.1023  0.0189  -0.0223 -0.0221 173 ARG B CA  
3664 C  C   . ARG B  174 ? 0.1146  0.1477 0.0996  0.0220  -0.0192 -0.0476 173 ARG B C   
3665 O  O   . ARG B  174 ? 0.1833  0.1720 0.1012  0.0181  -0.0451 -0.0559 173 ARG B O   
3666 C  CB  . ARG B  174 ? 0.1151  0.1958 0.1194  0.0161  -0.0102 -0.0298 173 ARG B CB  
3667 C  CG  . ARG B  174 ? 0.1128  0.2788 0.1319  0.0047  0.0067  -0.0396 173 ARG B CG  
3668 C  CD  . ARG B  174 ? 0.1531  0.2587 0.1761  0.0146  0.0268  -0.0263 173 ARG B CD  
3669 N  NE  . ARG B  174 ? 0.1276  0.2715 0.1556  0.0103  -0.0044 0.0186  173 ARG B NE  
3670 C  CZ  . ARG B  174 ? 0.1169  0.2662 0.1412  -0.0006 0.0369  0.0077  173 ARG B CZ  
3671 N  NH1 . ARG B  174 ? 0.1109  0.2425 0.1362  0.0043  0.0161  0.0223  173 ARG B NH1 
3672 N  NH2 . ARG B  174 ? 0.1416  0.2744 0.2081  0.0509  0.0551  0.0446  173 ARG B NH2 
3673 N  N   . ALA B  175 ? 0.1198  0.1377 0.0874  -0.0001 -0.0040 -0.0258 174 ALA B N   
3674 C  CA  . ALA B  175 ? 0.1215  0.1438 0.1405  -0.0088 -0.0133 -0.0312 174 ALA B CA  
3675 C  C   . ALA B  175 ? 0.1084  0.1330 0.1199  -0.0099 -0.0185 -0.0370 174 ALA B C   
3676 O  O   . ALA B  175 ? 0.1272  0.1280 0.1047  -0.0076 -0.0149 -0.0420 174 ALA B O   
3677 C  CB  . ALA B  175 ? 0.1189  0.1980 0.1804  -0.0257 -0.0086 -0.0430 174 ALA B CB  
3678 N  N   . PRO B  176 ? 0.1872  0.1198 0.1259  -0.0050 -0.0248 -0.0309 175 PRO B N   
3679 C  CA  . PRO B  176 ? 0.1826  0.1283 0.1305  0.0178  -0.0031 -0.0277 175 PRO B CA  
3680 C  C   . PRO B  176 ? 0.1208  0.1506 0.1384  -0.0055 -0.0199 -0.0288 175 PRO B C   
3681 O  O   . PRO B  176 ? 0.1362  0.1908 0.1689  -0.0077 -0.0120 -0.0093 175 PRO B O   
3682 C  CB  . PRO B  176 ? 0.2508  0.1463 0.1747  -0.0087 -0.0234 -0.0315 175 PRO B CB  
3683 C  CG  . PRO B  176 ? 0.5715  0.1470 0.2267  0.0031  -0.1687 -0.0198 175 PRO B CG  
3684 C  CD  . PRO B  176 ? 0.2572  0.1351 0.1448  -0.0348 -0.0303 -0.0531 175 PRO B CD  
3685 N  N   . PHE B  177 ? 0.1355  0.1330 0.1029  0.0021  0.0053  -0.0163 176 PHE B N   
3686 C  CA  . PHE B  177 ? 0.1225  0.1344 0.1205  -0.0016 0.0105  -0.0172 176 PHE B CA  
3687 C  C   . PHE B  177 ? 0.1120  0.1261 0.1208  -0.0143 0.0052  -0.0261 176 PHE B C   
3688 O  O   . PHE B  177 ? 0.1163  0.1269 0.1711  -0.0051 -0.0111 -0.0082 176 PHE B O   
3689 C  CB  . PHE B  177 ? 0.1287  0.1427 0.1111  0.0012  0.0127  -0.0165 176 PHE B CB  
3690 C  CG  . PHE B  177 ? 0.1280  0.1080 0.1316  -0.0016 0.0172  -0.0168 176 PHE B CG  
3691 C  CD1 . PHE B  177 ? 0.1502  0.1287 0.1333  -0.0023 -0.0194 -0.0208 176 PHE B CD1 
3692 C  CD2 . PHE B  177 ? 0.1434  0.1477 0.1384  0.0265  0.0395  0.0006  176 PHE B CD2 
3693 C  CE1 . PHE B  177 ? 0.1738  0.1180 0.1409  -0.0042 -0.0015 -0.0253 176 PHE B CE1 
3694 C  CE2 . PHE B  177 ? 0.1639  0.1736 0.1208  0.0268  0.0353  -0.0078 176 PHE B CE2 
3695 C  CZ  . PHE B  177 ? 0.1872  0.1578 0.1180  0.0132  0.0114  -0.0074 176 PHE B CZ  
3696 N  N   . THR B  178 ? 0.1276  0.1252 0.1029  -0.0025 0.0089  -0.0156 177 THR B N   
3697 C  CA  . THR B  178 ? 0.1578  0.1305 0.1108  0.0138  0.0190  -0.0144 177 THR B CA  
3698 C  C   . THR B  178 ? 0.1483  0.1238 0.1041  -0.0190 0.0210  -0.0310 177 THR B C   
3699 O  O   . THR B  178 ? 0.1384  0.1714 0.1242  -0.0029 0.0162  -0.0116 177 THR B O   
3700 C  CB  . THR B  178 ? 0.1887  0.1531 0.1181  -0.0183 0.0291  -0.0386 177 THR B CB  
3701 O  OG1 . THR B  178 ? 0.2443  0.1650 0.1316  -0.0436 -0.0179 -0.0201 177 THR B OG1 
3702 C  CG2 . THR B  178 ? 0.2479  0.1416 0.1373  0.0049  0.0518  -0.0300 177 THR B CG2 
3703 N  N   . ASN B  179 ? 0.1657  0.1323 0.1030  -0.0017 0.0022  -0.0142 178 ASN B N   
3704 C  CA  . ASN B  179 ? 0.1653  0.1538 0.0829  -0.0132 0.0029  -0.0203 178 ASN B CA  
3705 C  C   . ASN B  179 ? 0.1624  0.1445 0.0874  -0.0140 0.0116  -0.0145 178 ASN B C   
3706 O  O   . ASN B  179 ? 0.1750  0.1732 0.1305  -0.0210 0.0277  -0.0348 178 ASN B O   
3707 C  CB  . ASN B  179 ? 0.2178  0.1273 0.1014  -0.0284 0.0201  -0.0197 178 ASN B CB  
3708 C  CG  . ASN B  179 ? 0.2186  0.1919 0.1520  -0.0280 0.0016  -0.0036 178 ASN B CG  
3709 O  OD1 . ASN B  179 ? 0.2651  0.2030 0.1520  -0.0339 -0.0156 0.0187  178 ASN B OD1 
3710 N  ND2 . ASN B  179 ? 0.2314  0.1919 0.1980  -0.0444 0.0188  0.0306  178 ASN B ND2 
3711 N  N   . PHE B  180 ? 0.1664  0.1337 0.1040  -0.0053 0.0001  -0.0238 179 PHE B N   
3712 C  CA  . PHE B  180 ? 0.1560  0.1416 0.1049  0.0094  -0.0060 -0.0480 179 PHE B CA  
3713 C  C   . PHE B  180 ? 0.1659  0.1585 0.1249  -0.0130 -0.0103 -0.0465 179 PHE B C   
3714 O  O   . PHE B  180 ? 0.1671  0.1720 0.1280  -0.0128 -0.0122 -0.0270 179 PHE B O   
3715 C  CB  . PHE B  180 ? 0.1685  0.1470 0.1117  0.0233  0.0002  -0.0122 179 PHE B CB  
3716 C  CG  . PHE B  180 ? 0.1459  0.1463 0.1195  -0.0087 0.0114  -0.0282 179 PHE B CG  
3717 C  CD1 . PHE B  180 ? 0.1653  0.1919 0.1635  -0.0272 0.0132  -0.0660 179 PHE B CD1 
3718 C  CD2 . PHE B  180 ? 0.1524  0.1567 0.0988  0.0068  -0.0068 -0.0111 179 PHE B CD2 
3719 C  CE1 . PHE B  180 ? 0.1966  0.2127 0.1524  -0.0237 0.0370  -0.0644 179 PHE B CE1 
3720 C  CE2 . PHE B  180 ? 0.1703  0.1438 0.1084  0.0216  -0.0190 -0.0187 179 PHE B CE2 
3721 C  CZ  . PHE B  180 ? 0.1581  0.1897 0.1405  -0.0035 -0.0011 -0.0439 179 PHE B CZ  
3722 N  N   . ASP B  181 ? 0.1919  0.1786 0.1088  0.0194  -0.0223 -0.0439 180 ASP B N   
3723 C  CA  . ASP B  181 ? 0.2224  0.1542 0.1032  0.0128  -0.0328 -0.0352 180 ASP B CA  
3724 C  C   . ASP B  181 ? 0.1844  0.1610 0.0926  0.0004  -0.0086 -0.0414 180 ASP B C   
3725 O  O   . ASP B  181 ? 0.1779  0.1793 0.0937  0.0047  0.0044  -0.0323 180 ASP B O   
3726 C  CB  . ASP B  181 ? 0.2493  0.1800 0.0960  0.0012  -0.0126 -0.0055 180 ASP B CB  
3727 C  CG  . ASP B  181 ? 0.2217  0.1668 0.1208  0.0170  -0.0286 -0.0084 180 ASP B CG  
3728 O  OD1 . ASP B  181 ? 0.1854  0.1761 0.1301  0.0261  -0.0375 -0.0280 180 ASP B OD1 
3729 O  OD2 . ASP B  181 ? 0.3154  0.2152 0.1858  0.0405  -0.0832 0.0196  180 ASP B OD2 
3730 N  N   . PRO B  182 ? 0.1477  0.1725 0.1111  0.0176  -0.0214 -0.0250 181 PRO B N   
3731 C  CA  . PRO B  182 ? 0.1650  0.1524 0.0882  0.0280  -0.0077 -0.0209 181 PRO B CA  
3732 C  C   . PRO B  182 ? 0.1355  0.1549 0.1089  0.0194  -0.0125 -0.0296 181 PRO B C   
3733 O  O   . PRO B  182 ? 0.1513  0.1445 0.1164  0.0167  -0.0046 -0.0189 181 PRO B O   
3734 C  CB  . PRO B  182 ? 0.1664  0.1998 0.1206  0.0222  0.0318  -0.0009 181 PRO B CB  
3735 C  CG  . PRO B  182 ? 0.1696  0.1696 0.1517  0.0315  -0.0132 -0.0278 181 PRO B CG  
3736 C  CD  . PRO B  182 ? 0.1664  0.1815 0.1351  0.0140  0.0054  -0.0346 181 PRO B CD  
3737 N  N   . SER B  183 ? 0.1617  0.1930 0.0900  0.0278  -0.0239 -0.0197 182 SER B N   
3738 C  CA  . SER B  183 ? 0.1851  0.2059 0.1137  0.0422  -0.0345 -0.0153 182 SER B CA  
3739 C  C   . SER B  183 ? 0.1948  0.1585 0.0970  0.0381  -0.0252 -0.0133 182 SER B C   
3740 O  O   . SER B  183 ? 0.2117  0.1966 0.0971  0.0245  -0.0292 -0.0193 182 SER B O   
3741 C  CB  . SER B  183 ? 0.2665  0.2188 0.1377  0.0878  -0.0744 -0.0310 182 SER B CB  
3742 O  OG  . SER B  183 ? 0.3000  0.2284 0.1456  0.1098  -0.0418 -0.0038 182 SER B OG  
3743 N  N   . THR B  184 ? 0.1703  0.1581 0.1119  0.0177  -0.0231 -0.0075 183 THR B N   
3744 C  CA  . THR B  184 ? 0.1944  0.1782 0.1127  0.0194  0.0106  -0.0071 183 THR B CA  
3745 C  C   . THR B  184 ? 0.1761  0.1556 0.1261  -0.0036 0.0204  -0.0195 183 THR B C   
3746 O  O   . THR B  184 ? 0.1958  0.1829 0.1835  0.0135  0.0649  -0.0033 183 THR B O   
3747 C  CB  . THR B  184 ? 0.2224  0.1520 0.1355  0.0049  0.0201  -0.0225 183 THR B CB  
3748 O  OG1 . THR B  184 ? 0.1854  0.1738 0.1416  -0.0017 0.0055  -0.0284 183 THR B OG1 
3749 C  CG2 . THR B  184 ? 0.2712  0.1628 0.2041  0.0073  0.0441  -0.0044 183 THR B CG2 
3750 N  N   . LEU B  185 ? 0.1542  0.1416 0.1036  0.0065  -0.0019 -0.0204 184 LEU B N   
3751 C  CA  . LEU B  185 ? 0.1445  0.1463 0.1146  0.0027  -0.0176 -0.0297 184 LEU B CA  
3752 C  C   . LEU B  185 ? 0.1416  0.1477 0.1430  0.0051  -0.0151 -0.0513 184 LEU B C   
3753 O  O   . LEU B  185 ? 0.1438  0.1757 0.1344  0.0182  -0.0200 -0.0472 184 LEU B O   
3754 C  CB  . LEU B  185 ? 0.1459  0.1617 0.1106  -0.0096 -0.0097 -0.0204 184 LEU B CB  
3755 C  CG  . LEU B  185 ? 0.1980  0.1657 0.1137  -0.0160 -0.0398 -0.0188 184 LEU B CG  
3756 C  CD1 . LEU B  185 ? 0.3018  0.1725 0.1076  -0.0065 -0.0062 -0.0245 184 LEU B CD1 
3757 C  CD2 . LEU B  185 ? 0.1808  0.3132 0.2045  -0.0144 -0.0656 -0.0588 184 LEU B CD2 
3758 N  N   . LEU B  186 ? 0.1483  0.1887 0.1049  0.0047  -0.0315 -0.0529 185 LEU B N   
3759 C  CA  . LEU B  186 ? 0.1273  0.1948 0.1208  0.0135  -0.0072 -0.0521 185 LEU B CA  
3760 C  C   . LEU B  186 ? 0.1520  0.1738 0.1180  0.0083  -0.0118 -0.0385 185 LEU B C   
3761 O  O   . LEU B  186 ? 0.2081  0.2041 0.1225  -0.0336 0.0070  -0.0363 185 LEU B O   
3762 C  CB  . LEU B  186 ? 0.1260  0.2274 0.1153  0.0291  -0.0188 -0.0537 185 LEU B CB  
3763 C  CG  . LEU B  186 ? 0.1289  0.1951 0.1405  0.0226  -0.0100 -0.0299 185 LEU B CG  
3764 C  CD1 . LEU B  186 ? 0.1438  0.2651 0.1937  0.0573  -0.0267 -0.0688 185 LEU B CD1 
3765 C  CD2 . LEU B  186 ? 0.1932  0.1998 0.1793  0.0118  0.0051  -0.0353 185 LEU B CD2 
3766 N  N   . PRO B  187 ? 0.1452  0.1876 0.1126  0.0134  -0.0166 -0.0324 186 PRO B N   
3767 C  CA  . PRO B  187 ? 0.1876  0.2345 0.0969  0.0085  -0.0022 -0.0183 186 PRO B CA  
3768 C  C   . PRO B  187 ? 0.2239  0.1993 0.1098  -0.0241 -0.0078 -0.0326 186 PRO B C   
3769 O  O   . PRO B  187 ? 0.2416  0.2115 0.1262  0.0163  -0.0110 -0.0134 186 PRO B O   
3770 C  CB  . PRO B  187 ? 0.1779  0.2055 0.1111  -0.0062 -0.0009 -0.0485 186 PRO B CB  
3771 C  CG  . PRO B  187 ? 0.1847  0.2398 0.1153  0.0144  -0.0193 -0.0585 186 PRO B CG  
3772 C  CD  . PRO B  187 ? 0.1465  0.1804 0.1156  0.0017  -0.0080 -0.0406 186 PRO B CD  
3773 N  N   A SER B  188 ? 0.2296  0.2996 0.1330  -0.0709 -0.0003 -0.0153 187 SER B N   
3774 N  N   B SER B  188 ? 0.2472  0.2928 0.1221  -0.0690 0.0038  -0.0080 187 SER B N   
3775 C  CA  A SER B  188 ? 0.3538  0.3165 0.2009  -0.0666 -0.0269 0.0236  187 SER B CA  
3776 C  CA  B SER B  188 ? 0.3190  0.2231 0.1032  -0.0915 0.0578  -0.0192 187 SER B CA  
3777 C  C   A SER B  188 ? 0.3190  0.2213 0.1181  0.0043  -0.0062 0.0001  187 SER B C   
3778 C  C   B SER B  188 ? 0.3305  0.2134 0.1136  -0.0342 0.0029  0.0262  187 SER B C   
3779 O  O   A SER B  188 ? 0.3265  0.3089 0.1221  0.0605  -0.0649 -0.0165 187 SER B O   
3780 O  O   B SER B  188 ? 0.5561  0.2723 0.2020  0.0766  -0.0280 0.1056  187 SER B O   
3781 C  CB  A SER B  188 ? 0.3621  0.3854 0.3438  -0.1956 0.0205  -0.0432 187 SER B CB  
3782 C  CB  B SER B  188 ? 0.3746  0.3768 0.1084  -0.1129 0.1185  -0.0375 187 SER B CB  
3783 O  OG  A SER B  188 ? 0.2554  0.4982 0.2073  -0.1330 0.0158  -0.0048 187 SER B OG  
3784 O  OG  B SER B  188 ? 0.3600  0.3344 0.2152  -0.0345 0.0583  -0.0708 187 SER B OG  
3785 N  N   . SER B  189 ? 0.2145  0.2210 0.1502  -0.0063 -0.0055 -0.0208 188 SER B N   
3786 C  CA  . SER B  189 ? 0.1980  0.2579 0.1747  -0.0041 0.0009  -0.0015 188 SER B CA  
3787 C  C   . SER B  189 ? 0.1861  0.2328 0.1890  0.0135  -0.0156 -0.0425 188 SER B C   
3788 O  O   . SER B  189 ? 0.2594  0.2583 0.1535  -0.0399 -0.0290 -0.0348 188 SER B O   
3789 C  CB  . SER B  189 ? 0.2247  0.2974 0.1194  -0.0047 -0.0177 -0.0643 188 SER B CB  
3790 O  OG  . SER B  189 ? 0.2163  0.3236 0.1298  -0.0105 -0.0192 -0.0150 188 SER B OG  
3791 N  N   . LEU B  190 ? 0.1804  0.2583 0.2579  0.0010  -0.0212 -0.0701 189 LEU B N   
3792 C  CA  . LEU B  190 ? 0.1732  0.2229 0.2579  -0.0075 -0.0097 -0.0594 189 LEU B CA  
3793 C  C   . LEU B  190 ? 0.1542  0.2708 0.2389  -0.0143 -0.0096 -0.0775 189 LEU B C   
3794 O  O   . LEU B  190 ? 0.1456  0.2971 0.2888  -0.0153 0.0176  -0.1057 189 LEU B O   
3795 C  CB  . LEU B  190 ? 0.1732  0.2745 0.2702  -0.0027 0.0006  -0.1014 189 LEU B CB  
3796 C  CG  . LEU B  190 ? 0.2285  0.2917 0.2159  0.0104  -0.0411 -0.0857 189 LEU B CG  
3797 C  CD1 . LEU B  190 ? 0.2820  0.3521 0.3326  0.0644  -0.0930 -0.1826 189 LEU B CD1 
3798 C  CD2 . LEU B  190 ? 0.3790  0.3341 0.1531  -0.0536 -0.1304 -0.0403 189 LEU B CD2 
3799 N  N   . ASP B  191 ? 0.1581  0.2447 0.1685  0.0086  -0.0271 -0.0323 190 ASP B N   
3800 C  CA  . ASP B  191 ? 0.1553  0.2192 0.1585  -0.0015 -0.0363 -0.0311 190 ASP B CA  
3801 C  C   . ASP B  191 ? 0.1764  0.1987 0.1072  0.0113  -0.0211 -0.0458 190 ASP B C   
3802 O  O   . ASP B  191 ? 0.1544  0.2715 0.1217  0.0181  -0.0324 -0.0491 190 ASP B O   
3803 C  CB  . ASP B  191 ? 0.2027  0.2486 0.1190  0.0188  -0.0203 -0.0265 190 ASP B CB  
3804 C  CG  . ASP B  191 ? 0.2666  0.2468 0.1283  -0.0141 -0.0458 -0.0027 190 ASP B CG  
3805 O  OD1 . ASP B  191 ? 0.3068  0.3546 0.2156  0.0313  -0.0866 0.0540  190 ASP B OD1 
3806 O  OD2 . ASP B  191 ? 0.3711  0.3855 0.1172  0.0356  -0.0282 -0.0217 190 ASP B OD2 
3807 N  N   . PHE B  192 ? 0.1567  0.1980 0.1368  -0.0005 -0.0168 -0.0469 191 PHE B N   
3808 C  CA  . PHE B  192 ? 0.1289  0.2178 0.1274  0.0013  -0.0256 -0.0496 191 PHE B CA  
3809 C  C   . PHE B  192 ? 0.1168  0.2224 0.1294  -0.0037 -0.0336 -0.0655 191 PHE B C   
3810 O  O   . PHE B  192 ? 0.1520  0.2806 0.1215  -0.0055 -0.0530 -0.0598 191 PHE B O   
3811 C  CB  . PHE B  192 ? 0.1176  0.2411 0.1287  0.0256  -0.0176 -0.0662 191 PHE B CB  
3812 C  CG  . PHE B  192 ? 0.1377  0.2723 0.0988  0.0214  -0.0279 -0.0552 191 PHE B CG  
3813 C  CD1 . PHE B  192 ? 0.1847  0.2687 0.1230  0.0408  -0.0580 -0.0868 191 PHE B CD1 
3814 C  CD2 . PHE B  192 ? 0.1326  0.3003 0.1330  0.0314  -0.0225 -0.0756 191 PHE B CD2 
3815 C  CE1 . PHE B  192 ? 0.1696  0.2662 0.1544  0.0218  -0.0548 -0.0500 191 PHE B CE1 
3816 C  CE2 . PHE B  192 ? 0.1470  0.2651 0.1707  0.0500  -0.0333 -0.0795 191 PHE B CE2 
3817 C  CZ  . PHE B  192 ? 0.1822  0.2461 0.1492  0.0134  -0.0402 -0.0661 191 PHE B CZ  
3818 N  N   . TRP B  193 ? 0.1305  0.2099 0.1234  -0.0005 -0.0099 -0.0232 192 TRP B N   
3819 C  CA  . TRP B  193 ? 0.1190  0.2490 0.1014  -0.0042 -0.0203 -0.0615 192 TRP B CA  
3820 C  C   . TRP B  193 ? 0.1196  0.2335 0.0988  -0.0071 -0.0233 -0.0664 192 TRP B C   
3821 O  O   . TRP B  193 ? 0.1090  0.2855 0.1077  -0.0146 -0.0158 -0.0908 192 TRP B O   
3822 C  CB  . TRP B  193 ? 0.1359  0.2411 0.1226  0.0000  -0.0020 -0.0725 192 TRP B CB  
3823 C  CG  . TRP B  193 ? 0.1456  0.2097 0.1194  -0.0032 -0.0035 -0.0644 192 TRP B CG  
3824 C  CD1 . TRP B  193 ? 0.1520  0.2389 0.1254  -0.0379 0.0005  -0.0636 192 TRP B CD1 
3825 C  CD2 . TRP B  193 ? 0.1391  0.2249 0.1142  0.0083  -0.0022 -0.0501 192 TRP B CD2 
3826 N  NE1 . TRP B  193 ? 0.1366  0.2515 0.1263  -0.0211 0.0009  -0.0615 192 TRP B NE1 
3827 C  CE2 . TRP B  193 ? 0.1445  0.2210 0.1205  -0.0163 0.0081  -0.0662 192 TRP B CE2 
3828 C  CE3 . TRP B  193 ? 0.1280  0.2433 0.1274  -0.0339 -0.0008 -0.0662 192 TRP B CE3 
3829 C  CZ2 . TRP B  193 ? 0.1377  0.2181 0.1312  -0.0204 0.0298  -0.0627 192 TRP B CZ2 
3830 C  CZ3 . TRP B  193 ? 0.1639  0.2246 0.1164  -0.0126 0.0109  -0.0532 192 TRP B CZ3 
3831 C  CH2 . TRP B  193 ? 0.1495  0.2055 0.1355  -0.0104 0.0004  -0.0436 192 TRP B CH2 
3832 N  N   . THR B  194 ? 0.1111  0.2647 0.1221  -0.0200 -0.0242 -0.0838 193 THR B N   
3833 C  CA  . THR B  194 ? 0.1287  0.2532 0.1427  -0.0234 0.0057  -0.0566 193 THR B CA  
3834 C  C   . THR B  194 ? 0.1076  0.2558 0.1093  -0.0022 -0.0122 -0.0700 193 THR B C   
3835 O  O   . THR B  194 ? 0.1330  0.2770 0.1380  -0.0284 -0.0243 -0.0866 193 THR B O   
3836 C  CB  . THR B  194 ? 0.1234  0.2834 0.1254  0.0027  -0.0192 -0.0643 193 THR B CB  
3837 O  OG1 . THR B  194 ? 0.1199  0.2852 0.1316  -0.0163 -0.0150 -0.0740 193 THR B OG1 
3838 C  CG2 . THR B  194 ? 0.1502  0.3118 0.1483  0.0072  -0.0551 -0.0954 193 THR B CG2 
3839 N  N   . TYR B  195 ? 0.1168  0.2494 0.1234  -0.0286 0.0017  -0.0491 194 TYR B N   
3840 C  CA  . TYR B  195 ? 0.1247  0.2310 0.1250  -0.0137 -0.0111 -0.0489 194 TYR B CA  
3841 C  C   . TYR B  195 ? 0.1178  0.2314 0.1373  -0.0133 -0.0052 -0.0837 194 TYR B C   
3842 O  O   . TYR B  195 ? 0.1240  0.2339 0.1438  0.0004  -0.0194 -0.0835 194 TYR B O   
3843 C  CB  . TYR B  195 ? 0.1265  0.2436 0.1420  0.0029  -0.0183 -0.0882 194 TYR B CB  
3844 C  CG  . TYR B  195 ? 0.1223  0.2220 0.1348  -0.0155 -0.0011 -0.0949 194 TYR B CG  
3845 C  CD1 . TYR B  195 ? 0.1181  0.1912 0.1574  -0.0008 -0.0064 -0.0697 194 TYR B CD1 
3846 C  CD2 . TYR B  195 ? 0.1266  0.2247 0.1499  -0.0265 0.0062  -0.0934 194 TYR B CD2 
3847 C  CE1 . TYR B  195 ? 0.1355  0.2117 0.1263  -0.0055 0.0036  -0.0761 194 TYR B CE1 
3848 C  CE2 . TYR B  195 ? 0.1110  0.1951 0.1571  -0.0178 -0.0001 -0.0782 194 TYR B CE2 
3849 C  CZ  . TYR B  195 ? 0.1156  0.1822 0.1502  -0.0122 -0.0012 -0.0753 194 TYR B CZ  
3850 O  OH  . TYR B  195 ? 0.1118  0.1861 0.1477  -0.0167 0.0144  -0.0675 194 TYR B OH  
3851 N  N   . PRO B  196 ? 0.1076  0.2550 0.1395  -0.0249 -0.0055 -0.0855 195 PRO B N   
3852 C  CA  . PRO B  196 ? 0.1014  0.2572 0.1531  -0.0283 -0.0004 -0.0819 195 PRO B CA  
3853 C  C   . PRO B  196 ? 0.0879  0.2204 0.1682  -0.0340 -0.0201 -0.0894 195 PRO B C   
3854 O  O   . PRO B  196 ? 0.1754  0.2066 0.1757  -0.0303 -0.0231 -0.0987 195 PRO B O   
3855 C  CB  . PRO B  196 ? 0.1111  0.2945 0.1790  -0.0356 -0.0232 -0.0977 195 PRO B CB  
3856 C  CG  . PRO B  196 ? 0.1434  0.2920 0.1700  -0.0611 0.0130  -0.1040 195 PRO B CG  
3857 C  CD  . PRO B  196 ? 0.1348  0.2727 0.1775  -0.0677 -0.0193 -0.0998 195 PRO B CD  
3858 N  N   . GLY B  197 ? 0.0980  0.2034 0.1398  -0.0292 0.0095  -0.0823 196 GLY B N   
3859 C  CA  . GLY B  197 ? 0.1294  0.2020 0.1189  -0.0064 -0.0055 -0.0611 196 GLY B CA  
3860 C  C   . GLY B  197 ? 0.0986  0.1876 0.1416  -0.0278 0.0222  -0.0765 196 GLY B C   
3861 O  O   . GLY B  197 ? 0.1082  0.1980 0.1474  -0.0323 0.0113  -0.0749 196 GLY B O   
3862 N  N   . SER B  198 ? 0.1230  0.1736 0.1355  -0.0164 0.0018  -0.0767 197 SER B N   
3863 C  CA  . SER B  198 ? 0.1084  0.1969 0.1172  -0.0182 0.0087  -0.0737 197 SER B CA  
3864 C  C   . SER B  198 ? 0.0910  0.1495 0.1384  -0.0054 0.0087  -0.0450 197 SER B C   
3865 O  O   . SER B  198 ? 0.1071  0.1720 0.1287  -0.0132 0.0179  -0.0542 197 SER B O   
3866 C  CB  . SER B  198 ? 0.1138  0.1768 0.1696  -0.0067 0.0223  -0.0549 197 SER B CB  
3867 O  OG  . SER B  198 ? 0.1230  0.1685 0.1574  -0.0186 0.0386  -0.0712 197 SER B OG  
3868 N  N   . LEU B  199 ? 0.0914  0.1914 0.1223  -0.0062 0.0099  -0.0679 198 LEU B N   
3869 C  CA  . LEU B  199 ? 0.1014  0.1617 0.1362  -0.0062 0.0004  -0.0534 198 LEU B CA  
3870 C  C   . LEU B  199 ? 0.1229  0.1544 0.1312  -0.0314 0.0195  -0.0691 198 LEU B C   
3871 O  O   . LEU B  199 ? 0.1259  0.1624 0.1474  -0.0367 0.0043  -0.0554 198 LEU B O   
3872 C  CB  . LEU B  199 ? 0.1544  0.2016 0.1463  -0.0369 0.0388  -0.0695 198 LEU B CB  
3873 C  CG  . LEU B  199 ? 0.2906  0.1991 0.1905  -0.0016 0.0983  -0.0963 198 LEU B CG  
3874 C  CD1 . LEU B  199 ? 0.3865  0.2318 0.2271  -0.0011 0.1613  -0.0849 198 LEU B CD1 
3875 C  CD2 . LEU B  199 ? 0.3535  0.2658 0.2240  0.1406  -0.0316 -0.0322 198 LEU B CD2 
3876 N  N   . THR B  200 ? 0.0961  0.1531 0.1384  -0.0054 -0.0197 -0.0443 199 THR B N   
3877 C  CA  . THR B  200 ? 0.1004  0.1412 0.1574  -0.0086 0.0034  -0.0274 199 THR B CA  
3878 C  C   . THR B  200 ? 0.1039  0.1326 0.1380  -0.0096 -0.0077 -0.0271 199 THR B C   
3879 O  O   . THR B  200 ? 0.1160  0.1483 0.1502  -0.0150 0.0077  -0.0326 199 THR B O   
3880 C  CB  . THR B  200 ? 0.1199  0.1220 0.1199  -0.0230 -0.0042 -0.0367 199 THR B CB  
3881 O  OG1 . THR B  200 ? 0.1206  0.1287 0.1287  -0.0047 0.0026  -0.0417 199 THR B OG1 
3882 C  CG2 . THR B  200 ? 0.1621  0.1786 0.1164  -0.0186 -0.0133 -0.0408 199 THR B CG2 
3883 N  N   . HIS B  201 ? 0.1216  0.1337 0.1531  -0.0121 0.0034  -0.0414 200 HIS B N   
3884 C  CA  . HIS B  201 ? 0.1344  0.1535 0.1208  -0.0095 0.0062  -0.0370 200 HIS B CA  
3885 C  C   . HIS B  201 ? 0.1506  0.1603 0.1405  -0.0174 0.0167  -0.0484 200 HIS B C   
3886 O  O   . HIS B  201 ? 0.1420  0.1664 0.1355  -0.0160 0.0172  -0.0575 200 HIS B O   
3887 C  CB  . HIS B  201 ? 0.1359  0.1289 0.1987  -0.0003 -0.0119 -0.0606 200 HIS B CB  
3888 C  CG  . HIS B  201 ? 0.1250  0.1348 0.2309  0.0095  -0.0429 -0.0435 200 HIS B CG  
3889 N  ND1 . HIS B  201 ? 0.1854  0.1588 0.2188  0.0304  -0.0347 -0.0892 200 HIS B ND1 
3890 C  CD2 . HIS B  201 ? 0.1592  0.1668 0.2508  -0.0081 -0.0247 -0.0657 200 HIS B CD2 
3891 C  CE1 . HIS B  201 ? 0.2109  0.1682 0.2500  0.0108  -0.0341 -0.0696 200 HIS B CE1 
3892 N  NE2 . HIS B  201 ? 0.2231  0.1659 0.3337  0.0044  -0.0933 -0.0772 200 HIS B NE2 
3893 N  N   . PRO B  202 ? 0.1808  0.1538 0.1294  -0.0064 0.0322  -0.0348 201 PRO B N   
3894 C  CA  . PRO B  202 ? 0.1804  0.1858 0.1238  0.0103  0.0347  -0.0527 201 PRO B CA  
3895 C  C   . PRO B  202 ? 0.1596  0.2115 0.1153  -0.0110 0.0245  -0.0391 201 PRO B C   
3896 O  O   . PRO B  202 ? 0.1973  0.1958 0.1267  0.0030  0.0210  -0.0542 201 PRO B O   
3897 C  CB  . PRO B  202 ? 0.2188  0.2213 0.1152  0.0044  0.0168  -0.0127 201 PRO B CB  
3898 C  CG  . PRO B  202 ? 0.1958  0.2143 0.1635  -0.0097 0.0487  -0.0212 201 PRO B CG  
3899 C  CD  . PRO B  202 ? 0.2090  0.1420 0.1854  -0.0057 0.0269  -0.0135 201 PRO B CD  
3900 N  N   . PRO B  203 ? 0.1678  0.2120 0.1316  0.0150  0.0189  -0.0523 202 PRO B N   
3901 C  CA  . PRO B  203 ? 0.1527  0.2698 0.1380  -0.0290 0.0444  -0.0834 202 PRO B CA  
3902 C  C   . PRO B  203 ? 0.1445  0.2066 0.1368  -0.0052 0.0330  -0.0620 202 PRO B C   
3903 O  O   . PRO B  203 ? 0.1736  0.2648 0.1506  -0.0395 0.0672  -0.0559 202 PRO B O   
3904 C  CB  . PRO B  203 ? 0.1998  0.3169 0.1847  -0.0032 0.0718  -0.1297 202 PRO B CB  
3905 C  CG  . PRO B  203 ? 0.1782  0.2960 0.1833  0.0572  0.0198  -0.1056 202 PRO B CG  
3906 C  CD  . PRO B  203 ? 0.1811  0.2239 0.1757  0.0487  0.0002  -0.0749 202 PRO B CD  
3907 N  N   . LEU B  204 ? 0.1499  0.1962 0.1312  -0.0009 0.0411  -0.0604 203 LEU B N   
3908 C  CA  . LEU B  204 ? 0.1305  0.1786 0.1366  0.0128  0.0358  -0.0425 203 LEU B CA  
3909 C  C   . LEU B  204 ? 0.1544  0.1829 0.1409  -0.0061 0.0194  -0.0429 203 LEU B C   
3910 O  O   . LEU B  204 ? 0.1459  0.2163 0.1815  -0.0299 0.0516  -0.0919 203 LEU B O   
3911 C  CB  . LEU B  204 ? 0.1553  0.1483 0.1646  -0.0253 0.0385  -0.0275 203 LEU B CB  
3912 C  CG  . LEU B  204 ? 0.1402  0.1768 0.1373  -0.0197 0.0310  -0.0196 203 LEU B CG  
3913 C  CD1 . LEU B  204 ? 0.2115  0.1707 0.2240  -0.0153 0.0414  0.0187  203 LEU B CD1 
3914 C  CD2 . LEU B  204 ? 0.1430  0.1693 0.1641  -0.0082 0.0499  -0.0289 203 LEU B CD2 
3915 N  N   . TYR B  205 ? 0.1248  0.1872 0.1768  -0.0085 0.0403  -0.0483 204 TYR B N   
3916 C  CA  . TYR B  205 ? 0.1203  0.2176 0.1581  0.0055  0.0521  -0.0815 204 TYR B CA  
3917 C  C   . TYR B  205 ? 0.1073  0.1861 0.1689  -0.0296 0.0234  -0.0732 204 TYR B C   
3918 O  O   . TYR B  205 ? 0.1111  0.1905 0.1517  -0.0266 0.0261  -0.0666 204 TYR B O   
3919 C  CB  . TYR B  205 ? 0.1524  0.1879 0.1527  0.0187  0.0370  -0.0564 204 TYR B CB  
3920 C  CG  . TYR B  205 ? 0.1542  0.2300 0.1682  0.0225  0.0551  -0.0614 204 TYR B CG  
3921 C  CD1 . TYR B  205 ? 0.2364  0.2666 0.1969  -0.0139 0.0798  -0.0851 204 TYR B CD1 
3922 C  CD2 . TYR B  205 ? 0.1509  0.2328 0.1578  0.0355  -0.0027 -0.0695 204 TYR B CD2 
3923 C  CE1 . TYR B  205 ? 0.2253  0.2443 0.1779  0.0310  0.0569  -0.0629 204 TYR B CE1 
3924 C  CE2 . TYR B  205 ? 0.1919  0.2407 0.1549  0.0143  0.0323  -0.0697 204 TYR B CE2 
3925 C  CZ  . TYR B  205 ? 0.2034  0.2558 0.1779  0.0329  0.0406  -0.0710 204 TYR B CZ  
3926 O  OH  . TYR B  205 ? 0.2770  0.3104 0.1700  0.0547  0.0653  -0.0543 204 TYR B OH  
3927 N  N   . GLU B  206 ? 0.0961  0.2257 0.1614  -0.0215 0.0281  -0.0713 205 GLU B N   
3928 C  CA  . GLU B  206 ? 0.1664  0.1923 0.1405  -0.0179 0.0233  -0.0710 205 GLU B CA  
3929 C  C   . GLU B  206 ? 0.1294  0.1955 0.1538  -0.0124 0.0194  -0.0628 205 GLU B C   
3930 O  O   . GLU B  206 ? 0.1265  0.2554 0.2159  -0.0234 -0.0027 -0.0763 205 GLU B O   
3931 C  CB  . GLU B  206 ? 0.1294  0.1840 0.2213  -0.0390 0.0289  -0.0763 205 GLU B CB  
3932 C  CG  . GLU B  206 ? 0.1420  0.1958 0.2099  -0.0380 0.0162  -0.0926 205 GLU B CG  
3933 C  CD  . GLU B  206 ? 0.1531  0.1811 0.2163  -0.0326 0.0072  -0.0626 205 GLU B CD  
3934 O  OE1 . GLU B  206 ? 0.1646  0.1930 0.1779  -0.0480 0.0174  -0.0675 205 GLU B OE1 
3935 O  OE2 . GLU B  206 ? 0.1465  0.2532 0.3075  -0.0709 0.0059  -0.0724 205 GLU B OE2 
3936 N  N   . SER B  207 ? 0.1240  0.1851 0.1614  -0.0053 0.0209  -0.0759 206 SER B N   
3937 C  CA  . SER B  207 ? 0.0964  0.2048 0.1817  -0.0192 0.0210  -0.0802 206 SER B CA  
3938 C  C   . SER B  207 ? 0.1055  0.2084 0.1775  -0.0332 -0.0043 -0.0771 206 SER B C   
3939 O  O   . SER B  207 ? 0.1208  0.2041 0.1782  -0.0030 0.0010  -0.0631 206 SER B O   
3940 C  CB  . SER B  207 ? 0.1058  0.2479 0.1628  0.0027  0.0135  -0.0794 206 SER B CB  
3941 O  OG  . SER B  207 ? 0.1280  0.2235 0.1835  -0.0010 -0.0022 -0.0762 206 SER B OG  
3942 N  N   . VAL B  208 ? 0.0864  0.2231 0.1459  -0.0332 0.0110  -0.0585 207 VAL B N   
3943 C  CA  . VAL B  208 ? 0.1050  0.1779 0.1452  -0.0077 -0.0024 -0.0706 207 VAL B CA  
3944 C  C   . VAL B  208 ? 0.1062  0.1775 0.1527  -0.0257 -0.0019 -0.0741 207 VAL B C   
3945 O  O   . VAL B  208 ? 0.1571  0.1923 0.1632  -0.0185 0.0094  -0.0825 207 VAL B O   
3946 C  CB  . VAL B  208 ? 0.0831  0.2127 0.1384  -0.0125 -0.0088 -0.0625 207 VAL B CB  
3947 C  CG1 . VAL B  208 ? 0.1100  0.2048 0.1588  -0.0158 -0.0044 -0.0582 207 VAL B CG1 
3948 C  CG2 . VAL B  208 ? 0.1241  0.1793 0.1438  0.0135  -0.0141 -0.0521 207 VAL B CG2 
3949 N  N   . THR B  209 ? 0.1005  0.1991 0.1301  -0.0144 -0.0094 -0.0626 208 THR B N   
3950 C  CA  . THR B  209 ? 0.0777  0.2253 0.1477  0.0006  -0.0132 -0.0583 208 THR B CA  
3951 C  C   . THR B  209 ? 0.1093  0.2231 0.1256  -0.0021 -0.0162 -0.0930 208 THR B C   
3952 O  O   . THR B  209 ? 0.1231  0.2138 0.1355  -0.0077 -0.0131 -0.0737 208 THR B O   
3953 C  CB  . THR B  209 ? 0.1084  0.2278 0.1567  0.0141  -0.0064 -0.0540 208 THR B CB  
3954 O  OG1 . THR B  209 ? 0.1048  0.2666 0.1632  0.0104  -0.0316 -0.0827 208 THR B OG1 
3955 C  CG2 . THR B  209 ? 0.1441  0.3248 0.1452  0.0136  -0.0044 -0.0766 208 THR B CG2 
3956 N  N   . TRP B  210 ? 0.1032  0.2327 0.1261  0.0177  -0.0228 -0.0857 209 TRP B N   
3957 C  CA  . TRP B  210 ? 0.0890  0.2059 0.1199  0.0065  -0.0254 -0.0491 209 TRP B CA  
3958 C  C   . TRP B  210 ? 0.1084  0.1826 0.1136  -0.0033 -0.0318 -0.0595 209 TRP B C   
3959 O  O   . TRP B  210 ? 0.1137  0.2332 0.1203  -0.0004 -0.0346 -0.0836 209 TRP B O   
3960 C  CB  . TRP B  210 ? 0.1088  0.1835 0.1116  0.0190  -0.0176 -0.0584 209 TRP B CB  
3961 C  CG  . TRP B  210 ? 0.0961  0.1797 0.1172  -0.0050 0.0010  -0.0723 209 TRP B CG  
3962 C  CD1 . TRP B  210 ? 0.1066  0.2005 0.1366  -0.0063 -0.0057 -0.0653 209 TRP B CD1 
3963 C  CD2 . TRP B  210 ? 0.0971  0.1835 0.1280  0.0061  -0.0062 -0.0669 209 TRP B CD2 
3964 N  NE1 . TRP B  210 ? 0.1120  0.1879 0.1341  -0.0084 -0.0006 -0.0546 209 TRP B NE1 
3965 C  CE2 . TRP B  210 ? 0.0952  0.1793 0.1402  0.0111  0.0013  -0.0626 209 TRP B CE2 
3966 C  CE3 . TRP B  210 ? 0.0856  0.1718 0.1488  0.0089  -0.0137 -0.0625 209 TRP B CE3 
3967 C  CZ2 . TRP B  210 ? 0.0960  0.1872 0.1438  0.0126  -0.0067 -0.0649 209 TRP B CZ2 
3968 C  CZ3 . TRP B  210 ? 0.1023  0.2016 0.1232  0.0147  -0.0119 -0.0598 209 TRP B CZ3 
3969 C  CH2 . TRP B  210 ? 0.0988  0.1840 0.1423  0.0023  -0.0044 -0.0616 209 TRP B CH2 
3970 N  N   . ILE B  211 ? 0.1109  0.1955 0.1204  -0.0048 -0.0083 -0.0579 210 ILE B N   
3971 C  CA  . ILE B  211 ? 0.1027  0.2134 0.1244  -0.0077 -0.0354 -0.0586 210 ILE B CA  
3972 C  C   . ILE B  211 ? 0.0934  0.2222 0.0952  -0.0170 -0.0225 -0.0549 210 ILE B C   
3973 O  O   . ILE B  211 ? 0.1093  0.2199 0.1120  0.0001  -0.0386 -0.0699 210 ILE B O   
3974 C  CB  . ILE B  211 ? 0.1256  0.1941 0.1301  0.0108  -0.0357 -0.0434 210 ILE B CB  
3975 C  CG1 . ILE B  211 ? 0.1074  0.2655 0.1531  0.0181  -0.0478 -0.0518 210 ILE B CG1 
3976 C  CG2 . ILE B  211 ? 0.1474  0.2397 0.1133  -0.0062 -0.0071 -0.0410 210 ILE B CG2 
3977 C  CD1 . ILE B  211 ? 0.1549  0.2594 0.1844  0.0021  -0.0653 -0.0726 210 ILE B CD1 
3978 N  N   . ILE B  212 ? 0.1117  0.2102 0.0917  0.0004  -0.0166 -0.0553 211 ILE B N   
3979 C  CA  . ILE B  212 ? 0.0900  0.2052 0.1045  0.0027  -0.0120 -0.0337 211 ILE B CA  
3980 C  C   . ILE B  212 ? 0.1081  0.2176 0.0806  -0.0021 -0.0210 -0.0462 211 ILE B C   
3981 O  O   . ILE B  212 ? 0.1240  0.2547 0.0864  -0.0106 -0.0253 -0.0518 211 ILE B O   
3982 C  CB  . ILE B  212 ? 0.1226  0.2099 0.1032  0.0020  -0.0094 -0.0570 211 ILE B CB  
3983 C  CG1 . ILE B  212 ? 0.1405  0.2242 0.0985  -0.0047 0.0190  -0.0319 211 ILE B CG1 
3984 C  CG2 . ILE B  212 ? 0.1155  0.2249 0.1247  -0.0004 -0.0012 -0.0458 211 ILE B CG2 
3985 C  CD1 . ILE B  212 ? 0.1603  0.2247 0.0944  0.0002  0.0183  -0.0554 211 ILE B CD1 
3986 N  N   . CYS B  213 ? 0.1065  0.1905 0.1135  -0.0072 -0.0234 -0.0425 212 CYS B N   
3987 C  CA  . CYS B  213 ? 0.1242  0.1782 0.1115  -0.0009 -0.0118 -0.0367 212 CYS B CA  
3988 C  C   . CYS B  213 ? 0.1517  0.1944 0.0845  0.0033  -0.0337 -0.0442 212 CYS B C   
3989 O  O   . CYS B  213 ? 0.1333  0.1887 0.1038  -0.0024 -0.0201 -0.0516 212 CYS B O   
3990 C  CB  . CYS B  213 ? 0.1384  0.1808 0.1280  0.0044  -0.0237 -0.0395 212 CYS B CB  
3991 S  SG  . CYS B  213 ? 0.1527  0.2117 0.1452  0.0182  -0.0150 -0.0422 212 CYS B SG  
3992 N  N   . LYS B  214 ? 0.1657  0.2497 0.0756  -0.0334 -0.0065 -0.0412 213 LYS B N   
3993 C  CA  . LYS B  214 ? 0.1578  0.3007 0.0952  -0.0201 -0.0145 -0.0965 213 LYS B CA  
3994 C  C   . LYS B  214 ? 0.1689  0.2554 0.0593  0.0075  -0.0098 -0.0717 213 LYS B C   
3995 O  O   . LYS B  214 ? 0.1761  0.2091 0.0946  -0.0139 0.0166  -0.0563 213 LYS B O   
3996 C  CB  . LYS B  214 ? 0.1930  0.4867 0.0952  -0.0347 -0.0195 -0.1018 213 LYS B CB  
3997 C  CG  . LYS B  214 ? 0.2357  0.4044 0.1225  0.0469  -0.0446 -0.0504 213 LYS B CG  
3998 C  CD  . LYS B  214 ? 0.2515  0.2691 0.1488  0.0172  -0.0052 -0.0280 213 LYS B CD  
3999 C  CE  . LYS B  214 ? 0.3097  0.3301 0.1441  -0.0529 0.0454  -0.0649 213 LYS B CE  
4000 N  NZ  . LYS B  214 ? 0.4487  0.4069 0.1703  0.1152  0.0653  -0.0017 213 LYS B NZ  
4001 N  N   A GLU B  215 ? 0.1409  0.2357 0.1002  -0.0099 -0.0304 -0.0583 214 GLU B N   
4002 N  N   B GLU B  215 ? 0.1283  0.2447 0.0669  -0.0048 -0.0197 -0.0686 214 GLU B N   
4003 C  CA  A GLU B  215 ? 0.1402  0.1797 0.0709  0.0052  -0.0185 -0.0469 214 GLU B CA  
4004 C  CA  B GLU B  215 ? 0.1333  0.2379 0.0958  -0.0143 -0.0374 -0.0092 214 GLU B CA  
4005 C  C   A GLU B  215 ? 0.1231  0.1682 0.0610  -0.0312 -0.0037 -0.0473 214 GLU B C   
4006 C  C   B GLU B  215 ? 0.1270  0.1650 0.0776  -0.0158 -0.0111 -0.0429 214 GLU B C   
4007 O  O   A GLU B  215 ? 0.1359  0.1298 0.0759  0.0006  -0.0094 -0.0292 214 GLU B O   
4008 O  O   B GLU B  215 ? 0.1682  0.1312 0.0800  -0.0176 0.0127  -0.0081 214 GLU B O   
4009 C  CB  A GLU B  215 ? 0.1596  0.2009 0.1258  -0.0509 -0.0185 0.0307  214 GLU B CB  
4010 C  CB  B GLU B  215 ? 0.1650  0.1976 0.0637  0.0320  -0.0051 -0.0551 214 GLU B CB  
4011 C  CG  A GLU B  215 ? 0.1434  0.1808 0.1007  -0.0100 -0.0010 -0.0149 214 GLU B CG  
4012 C  CG  B GLU B  215 ? 0.2102  0.1914 0.0864  0.0160  0.0064  0.0167  214 GLU B CG  
4013 C  CD  A GLU B  215 ? 0.1391  0.1538 0.1513  0.0024  0.0046  -0.0206 214 GLU B CD  
4014 C  CD  B GLU B  215 ? 0.1707  0.1829 0.1170  0.0111  0.0108  -0.0051 214 GLU B CD  
4015 O  OE1 A GLU B  215 ? 0.2744  0.1804 0.1470  -0.0436 0.0458  -0.0291 214 GLU B OE1 
4016 O  OE1 B GLU B  215 ? 0.1937  0.2314 0.1074  0.0059  0.0179  -0.0321 214 GLU B OE1 
4017 O  OE2 A GLU B  215 ? 0.1966  0.3315 0.3067  -0.0154 -0.1075 0.0973  214 GLU B OE2 
4018 O  OE2 B GLU B  215 ? 0.2187  0.2107 0.1305  0.0644  0.0362  0.0295  214 GLU B OE2 
4019 N  N   . SER B  216 ? 0.1294  0.1858 0.0836  -0.0138 -0.0193 -0.0351 215 SER B N   
4020 C  CA  . SER B  216 ? 0.1351  0.1779 0.0739  -0.0062 -0.0222 -0.0330 215 SER B CA  
4021 C  C   . SER B  216 ? 0.1075  0.1966 0.0652  -0.0044 0.0002  -0.0206 215 SER B C   
4022 O  O   . SER B  216 ? 0.1786  0.1854 0.0706  -0.0134 0.0006  -0.0227 215 SER B O   
4023 C  CB  . SER B  216 ? 0.1398  0.2055 0.0803  0.0103  0.0172  -0.0219 215 SER B CB  
4024 O  OG  . SER B  216 ? 0.1470  0.1930 0.0891  0.0020  0.0209  -0.0414 215 SER B OG  
4025 N  N   . ILE B  217 ? 0.1076  0.1725 0.0636  -0.0109 -0.0058 -0.0364 216 ILE B N   
4026 C  CA  . ILE B  217 ? 0.1054  0.1703 0.0949  -0.0040 -0.0058 -0.0322 216 ILE B CA  
4027 C  C   . ILE B  217 ? 0.1014  0.1635 0.0707  0.0030  0.0012  -0.0272 216 ILE B C   
4028 O  O   . ILE B  217 ? 0.1155  0.1481 0.1110  0.0019  0.0003  -0.0285 216 ILE B O   
4029 C  CB  . ILE B  217 ? 0.1056  0.1398 0.0970  0.0103  0.0100  -0.0085 216 ILE B CB  
4030 C  CG1 . ILE B  217 ? 0.1225  0.1811 0.0766  0.0319  0.0059  -0.0097 216 ILE B CG1 
4031 C  CG2 . ILE B  217 ? 0.1276  0.1703 0.0883  0.0092  -0.0168 -0.0058 216 ILE B CG2 
4032 C  CD1 . ILE B  217 ? 0.1624  0.1736 0.0952  0.0428  -0.0041 -0.0316 216 ILE B CD1 
4033 N  N   A SER B  218 ? 0.0989  0.1901 0.0882  -0.0245 -0.0076 -0.0068 217 SER B N   
4034 N  N   B SER B  218 ? 0.0926  0.1775 0.0809  -0.0145 -0.0047 -0.0211 217 SER B N   
4035 C  CA  A SER B  218 ? 0.1159  0.1919 0.0855  -0.0417 -0.0368 0.0201  217 SER B CA  
4036 C  CA  B SER B  218 ? 0.0897  0.1585 0.0794  -0.0015 0.0055  -0.0324 217 SER B CA  
4037 C  C   A SER B  218 ? 0.0844  0.1509 0.1023  -0.0237 -0.0174 -0.0227 217 SER B C   
4038 C  C   B SER B  218 ? 0.1101  0.1653 0.0797  -0.0122 0.0036  -0.0070 217 SER B C   
4039 O  O   A SER B  218 ? 0.1135  0.1316 0.1074  -0.0223 0.0147  -0.0141 217 SER B O   
4040 O  O   B SER B  218 ? 0.1038  0.1542 0.0982  -0.0067 -0.0192 -0.0154 217 SER B O   
4041 C  CB  A SER B  218 ? 0.1879  0.2278 0.0242  -0.0842 -0.0234 0.0183  217 SER B CB  
4042 C  CB  B SER B  218 ? 0.0636  0.1481 0.1538  -0.0098 0.0199  -0.0313 217 SER B CB  
4043 O  OG  A SER B  218 ? 0.2204  0.2533 0.2364  -0.0570 0.0388  -0.0042 217 SER B OG  
4044 O  OG  B SER B  218 ? 0.0603  0.1743 0.0731  -0.0139 0.0044  -0.0248 217 SER B OG  
4045 N  N   . VAL B  219 ? 0.0953  0.1768 0.0722  -0.0012 -0.0150 -0.0096 218 VAL B N   
4046 C  CA  . VAL B  219 ? 0.0804  0.1930 0.0624  0.0054  -0.0076 -0.0252 218 VAL B CA  
4047 C  C   . VAL B  219 ? 0.0775  0.1659 0.0777  -0.0075 0.0030  -0.0145 218 VAL B C   
4048 O  O   . VAL B  219 ? 0.1014  0.1854 0.0960  0.0154  0.0072  -0.0402 218 VAL B O   
4049 C  CB  . VAL B  219 ? 0.1011  0.1736 0.0748  0.0013  0.0066  -0.0209 218 VAL B CB  
4050 C  CG1 . VAL B  219 ? 0.1102  0.1817 0.1117  0.0166  -0.0051 -0.0077 218 VAL B CG1 
4051 C  CG2 . VAL B  219 ? 0.1044  0.2084 0.0689  -0.0033 0.0057  -0.0158 218 VAL B CG2 
4052 N  N   . SER B  220 ? 0.0715  0.1840 0.0794  -0.0094 -0.0030 -0.0234 219 SER B N   
4053 C  CA  . SER B  220 ? 0.0856  0.1761 0.0872  0.0058  0.0111  -0.0113 219 SER B CA  
4054 C  C   . SER B  220 ? 0.1059  0.1790 0.0664  0.0077  -0.0121 -0.0315 219 SER B C   
4055 O  O   . SER B  220 ? 0.1068  0.1736 0.0713  0.0010  0.0021  -0.0203 219 SER B O   
4056 C  CB  . SER B  220 ? 0.0870  0.2037 0.0856  -0.0205 -0.0004 -0.0291 219 SER B CB  
4057 O  OG  . SER B  220 ? 0.1120  0.1991 0.0888  -0.0051 -0.0041 -0.0122 219 SER B OG  
4058 N  N   A SER B  221 ? 0.1169  0.1790 0.0863  0.0185  -0.0144 -0.0150 220 SER B N   
4059 N  N   B SER B  221 ? 0.1091  0.1854 0.0937  0.0151  -0.0171 -0.0277 220 SER B N   
4060 C  CA  A SER B  221 ? 0.1463  0.2034 0.0493  0.0566  -0.0179 -0.0091 220 SER B CA  
4061 C  CA  B SER B  221 ? 0.1040  0.1958 0.0792  0.0223  -0.0036 -0.0146 220 SER B CA  
4062 C  C   A SER B  221 ? 0.1037  0.1865 0.0743  -0.0009 0.0096  -0.0276 220 SER B C   
4063 C  C   B SER B  221 ? 0.0557  0.1937 0.0873  0.0025  -0.0046 -0.0222 220 SER B C   
4064 O  O   A SER B  221 ? 0.1409  0.1743 0.0891  0.0219  0.0303  -0.0231 220 SER B O   
4065 O  O   B SER B  221 ? 0.0979  0.1833 0.0925  0.0131  0.0027  -0.0161 220 SER B O   
4066 C  CB  A SER B  221 ? 0.1118  0.1725 0.1483  0.0257  -0.0201 -0.0089 220 SER B CB  
4067 C  CB  B SER B  221 ? 0.1257  0.1671 0.0899  0.0425  -0.0233 -0.0440 220 SER B CB  
4068 O  OG  A SER B  221 ? 0.1937  0.1865 0.1307  0.0626  0.0034  -0.0174 220 SER B OG  
4069 O  OG  B SER B  221 ? 0.1151  0.2109 0.1007  0.0179  -0.0167 -0.0803 220 SER B OG  
4070 N  N   . GLU B  222 ? 0.0865  0.1854 0.0822  0.0022  -0.0089 -0.0305 221 GLU B N   
4071 C  CA  . GLU B  222 ? 0.0910  0.2002 0.0759  -0.0077 0.0077  -0.0245 221 GLU B CA  
4072 C  C   . GLU B  222 ? 0.0935  0.1926 0.0756  -0.0055 0.0093  -0.0132 221 GLU B C   
4073 O  O   . GLU B  222 ? 0.1040  0.2059 0.0680  -0.0060 0.0012  -0.0216 221 GLU B O   
4074 C  CB  . GLU B  222 ? 0.0881  0.1861 0.1127  -0.0066 0.0047  -0.0289 221 GLU B CB  
4075 C  CG  . GLU B  222 ? 0.0943  0.2411 0.1120  -0.0050 0.0183  -0.0438 221 GLU B CG  
4076 C  CD  . GLU B  222 ? 0.1062  0.2352 0.0967  0.0057  0.0050  -0.0218 221 GLU B CD  
4077 O  OE1 . GLU B  222 ? 0.1135  0.2623 0.1178  0.0069  0.0037  -0.0141 221 GLU B OE1 
4078 O  OE2 . GLU B  222 ? 0.1155  0.2672 0.1111  0.0225  0.0130  -0.0328 221 GLU B OE2 
4079 N  N   . GLN B  223 ? 0.0870  0.1743 0.0853  -0.0010 0.0017  -0.0144 222 GLN B N   
4080 C  CA  . GLN B  223 ? 0.0759  0.1779 0.0791  0.0124  0.0013  -0.0119 222 GLN B CA  
4081 C  C   . GLN B  223 ? 0.0867  0.1761 0.0660  0.0018  -0.0053 -0.0198 222 GLN B C   
4082 O  O   . GLN B  223 ? 0.0908  0.1944 0.0712  0.0159  0.0038  -0.0174 222 GLN B O   
4083 C  CB  . GLN B  223 ? 0.1170  0.1720 0.0592  -0.0011 -0.0124 -0.0106 222 GLN B CB  
4084 C  CG  . GLN B  223 ? 0.1257  0.1574 0.0844  0.0226  -0.0083 -0.0138 222 GLN B CG  
4085 C  CD  . GLN B  223 ? 0.1037  0.1923 0.0761  0.0105  0.0026  -0.0254 222 GLN B CD  
4086 O  OE1 . GLN B  223 ? 0.1155  0.1729 0.0741  -0.0009 -0.0044 -0.0160 222 GLN B OE1 
4087 N  NE2 . GLN B  223 ? 0.1506  0.1732 0.1040  0.0181  -0.0022 -0.0372 222 GLN B NE2 
4088 N  N   . LEU B  224 ? 0.1012  0.1639 0.0817  -0.0021 -0.0042 -0.0255 223 LEU B N   
4089 C  CA  . LEU B  224 ? 0.1216  0.1908 0.0776  -0.0065 -0.0238 -0.0239 223 LEU B CA  
4090 C  C   . LEU B  224 ? 0.0937  0.1876 0.0725  -0.0042 -0.0038 -0.0310 223 LEU B C   
4091 O  O   . LEU B  224 ? 0.1138  0.1815 0.0885  -0.0150 -0.0059 -0.0156 223 LEU B O   
4092 C  CB  . LEU B  224 ? 0.1445  0.1976 0.0898  -0.0188 -0.0203 -0.0295 223 LEU B CB  
4093 C  CG  . LEU B  224 ? 0.1362  0.2433 0.0993  -0.0181 -0.0307 -0.0378 223 LEU B CG  
4094 C  CD1 . LEU B  224 ? 0.2206  0.2389 0.1179  -0.0053 -0.0225 -0.0569 223 LEU B CD1 
4095 C  CD2 . LEU B  224 ? 0.1359  0.3025 0.1181  -0.0614 -0.0512 0.0345  223 LEU B CD2 
4096 N  N   . ALA B  225 ? 0.0988  0.1542 0.1037  0.0100  -0.0239 -0.0164 224 ALA B N   
4097 C  CA  . ALA B  225 ? 0.0949  0.1926 0.0759  0.0113  -0.0173 -0.0302 224 ALA B CA  
4098 C  C   . ALA B  225 ? 0.0926  0.1556 0.0996  -0.0111 0.0020  -0.0073 224 ALA B C   
4099 O  O   . ALA B  225 ? 0.1084  0.1524 0.0919  0.0104  0.0057  -0.0066 224 ALA B O   
4100 C  CB  . ALA B  225 ? 0.0795  0.2375 0.1164  0.0256  -0.0011 -0.0261 224 ALA B CB  
4101 N  N   . GLN B  226 ? 0.0949  0.1606 0.0874  -0.0005 -0.0025 -0.0138 225 GLN B N   
4102 C  CA  . GLN B  226 ? 0.0979  0.1384 0.0779  -0.0035 0.0070  -0.0089 225 GLN B CA  
4103 C  C   . GLN B  226 ? 0.1040  0.1465 0.0773  0.0066  -0.0011 -0.0102 225 GLN B C   
4104 O  O   . GLN B  226 ? 0.1161  0.1779 0.0820  -0.0085 0.0054  -0.0220 225 GLN B O   
4105 C  CB  . GLN B  226 ? 0.1099  0.1606 0.1145  0.0038  -0.0081 0.0126  225 GLN B CB  
4106 C  CG  . GLN B  226 ? 0.1161  0.1585 0.1261  -0.0052 0.0116  0.0100  225 GLN B CG  
4107 C  CD  . GLN B  226 ? 0.1172  0.1621 0.1248  -0.0011 -0.0059 0.0107  225 GLN B CD  
4108 O  OE1 . GLN B  226 ? 0.1502  0.1714 0.1470  0.0017  0.0082  0.0241  225 GLN B OE1 
4109 N  NE2 . GLN B  226 ? 0.1384  0.1829 0.1720  0.0034  -0.0073 -0.0263 225 GLN B NE2 
4110 N  N   . PHE B  227 ? 0.0849  0.1524 0.0901  -0.0031 -0.0078 -0.0098 226 PHE B N   
4111 C  CA  . PHE B  227 ? 0.0865  0.1786 0.0847  -0.0036 -0.0277 -0.0089 226 PHE B CA  
4112 C  C   . PHE B  227 ? 0.0770  0.1747 0.0831  0.0146  -0.0093 -0.0153 226 PHE B C   
4113 O  O   . PHE B  227 ? 0.0976  0.1700 0.0926  -0.0016 -0.0044 -0.0159 226 PHE B O   
4114 C  CB  . PHE B  227 ? 0.1014  0.2005 0.0741  0.0015  -0.0159 -0.0100 226 PHE B CB  
4115 C  CG  . PHE B  227 ? 0.0993  0.2091 0.0782  -0.0053 -0.0067 0.0100  226 PHE B CG  
4116 C  CD1 . PHE B  227 ? 0.1588  0.2407 0.1307  0.0691  0.0231  0.0234  226 PHE B CD1 
4117 C  CD2 . PHE B  227 ? 0.1398  0.3018 0.0862  -0.0661 -0.0359 0.0140  226 PHE B CD2 
4118 C  CE1 . PHE B  227 ? 0.1876  0.3452 0.1351  0.1176  0.0105  0.0301  226 PHE B CE1 
4119 C  CE2 . PHE B  227 ? 0.1707  0.3456 0.0844  -0.0368 -0.0454 0.0347  226 PHE B CE2 
4120 C  CZ  . PHE B  227 ? 0.1067  0.3776 0.1606  0.0192  -0.0009 0.0078  226 PHE B CZ  
4121 N  N   . ARG B  228 ? 0.0908  0.1456 0.1077  0.0058  -0.0087 -0.0116 227 ARG B N   
4122 C  CA  . ARG B  228 ? 0.1151  0.1452 0.1283  0.0179  -0.0043 -0.0120 227 ARG B CA  
4123 C  C   . ARG B  228 ? 0.1138  0.1628 0.0986  0.0119  0.0143  -0.0111 227 ARG B C   
4124 O  O   . ARG B  228 ? 0.1736  0.1937 0.1412  0.0228  0.0265  0.0311  227 ARG B O   
4125 C  CB  . ARG B  228 ? 0.1054  0.1703 0.1427  0.0188  0.0140  -0.0307 227 ARG B CB  
4126 C  CG  . ARG B  228 ? 0.1021  0.1829 0.1668  0.0150  -0.0128 -0.0651 227 ARG B CG  
4127 C  CD  . ARG B  228 ? 0.2375  0.2337 0.2293  0.0850  -0.0406 -0.1123 227 ARG B CD  
4128 N  NE  . ARG B  228 ? 0.2178  0.2350 0.2576  0.0754  -0.1129 -0.1588 227 ARG B NE  
4129 C  CZ  . ARG B  228 ? 0.2824  0.2009 0.2296  0.0364  -0.1509 -0.0058 227 ARG B CZ  
4130 N  NH1 . ARG B  228 ? 0.3398  0.1786 0.2479  -0.0333 -0.1532 0.0067  227 ARG B NH1 
4131 N  NH2 . ARG B  228 ? 0.2680  0.1897 0.2143  0.0548  -0.1239 -0.0605 227 ARG B NH2 
4132 N  N   . SER B  229 ? 0.0919  0.1668 0.0967  0.0071  -0.0111 -0.0114 228 SER B N   
4133 C  CA  . SER B  229 ? 0.1111  0.2077 0.0942  -0.0009 -0.0001 -0.0318 228 SER B CA  
4134 C  C   . SER B  229 ? 0.1041  0.1659 0.1007  0.0103  -0.0041 -0.0133 228 SER B C   
4135 O  O   . SER B  229 ? 0.1093  0.2170 0.0882  0.0132  -0.0137 -0.0091 228 SER B O   
4136 C  CB  . SER B  229 ? 0.1747  0.2397 0.1254  -0.0580 -0.0510 -0.0237 228 SER B CB  
4137 O  OG  . SER B  229 ? 0.2550  0.3067 0.1567  -0.0914 -0.0423 0.0160  228 SER B OG  
4138 N  N   . LEU B  230 ? 0.0943  0.1668 0.0995  0.0036  0.0011  0.0015  229 LEU B N   
4139 C  CA  . LEU B  230 ? 0.1039  0.1574 0.0838  0.0196  -0.0126 0.0009  229 LEU B CA  
4140 C  C   . LEU B  230 ? 0.0934  0.1270 0.0864  0.0229  0.0032  -0.0158 229 LEU B C   
4141 O  O   . LEU B  230 ? 0.1987  0.1409 0.0882  0.0317  0.0187  -0.0159 229 LEU B O   
4142 C  CB  . LEU B  230 ? 0.1172  0.1544 0.0944  0.0136  -0.0114 -0.0010 229 LEU B CB  
4143 C  CG  . LEU B  230 ? 0.1664  0.1932 0.1344  0.0198  -0.0432 -0.0022 229 LEU B CG  
4144 C  CD1 . LEU B  230 ? 0.1621  0.2386 0.1617  0.0150  -0.0293 0.0055  229 LEU B CD1 
4145 C  CD2 . LEU B  230 ? 0.2132  0.1689 0.1549  0.0514  -0.0316 -0.0073 229 LEU B CD2 
4146 N  N   . LEU B  231 ? 0.0944  0.1373 0.0791  0.0148  0.0061  -0.0130 230 LEU B N   
4147 C  CA  . LEU B  231 ? 0.0919  0.1693 0.0741  0.0168  -0.0084 -0.0076 230 LEU B CA  
4148 C  C   . LEU B  231 ? 0.0900  0.1585 0.0803  0.0097  -0.0168 -0.0058 230 LEU B C   
4149 O  O   . LEU B  231 ? 0.0873  0.1556 0.1066  0.0134  -0.0060 -0.0132 230 LEU B O   
4150 C  CB  . LEU B  231 ? 0.1041  0.1628 0.0862  0.0125  -0.0089 -0.0130 230 LEU B CB  
4151 C  CG  . LEU B  231 ? 0.0980  0.1617 0.1092  0.0204  -0.0055 -0.0160 230 LEU B CG  
4152 C  CD1 . LEU B  231 ? 0.1111  0.2138 0.1189  0.0041  -0.0200 -0.0239 230 LEU B CD1 
4153 C  CD2 . LEU B  231 ? 0.1294  0.1685 0.1247  0.0391  0.0057  -0.0230 230 LEU B CD2 
4154 N  N   . SER B  232 ? 0.1172  0.1384 0.1102  -0.0035 -0.0006 -0.0081 231 SER B N   
4155 C  CA  . SER B  232 ? 0.1164  0.1502 0.1214  -0.0039 -0.0164 -0.0172 231 SER B CA  
4156 C  C   . SER B  232 ? 0.1220  0.1391 0.1071  -0.0100 0.0087  -0.0178 231 SER B C   
4157 O  O   . SER B  232 ? 0.1102  0.1826 0.1513  -0.0275 0.0032  -0.0234 231 SER B O   
4158 C  CB  . SER B  232 ? 0.1391  0.1283 0.1412  0.0091  -0.0152 -0.0170 231 SER B CB  
4159 O  OG  . SER B  232 ? 0.1635  0.1585 0.1588  0.0044  -0.0175 -0.0064 231 SER B OG  
4160 N  N   . ASN B  233 ? 0.1337  0.1470 0.1102  -0.0079 -0.0141 -0.0189 232 ASN B N   
4161 C  CA  . ASN B  233 ? 0.1459  0.1621 0.0958  -0.0044 0.0129  -0.0170 232 ASN B CA  
4162 C  C   . ASN B  233 ? 0.0910  0.1646 0.1014  0.0092  0.0017  -0.0076 232 ASN B C   
4163 O  O   . ASN B  233 ? 0.1267  0.1578 0.0908  0.0089  -0.0063 0.0054  232 ASN B O   
4164 C  CB  . ASN B  233 ? 0.1341  0.1483 0.1226  0.0017  0.0057  0.0111  232 ASN B CB  
4165 C  CG  . ASN B  233 ? 0.1208  0.1456 0.0849  0.0088  -0.0032 0.0067  232 ASN B CG  
4166 O  OD1 . ASN B  233 ? 0.1111  0.1571 0.0988  0.0130  0.0044  -0.0005 232 ASN B OD1 
4167 N  ND2 . ASN B  233 ? 0.1283  0.1556 0.0961  0.0130  -0.0182 0.0042  232 ASN B ND2 
4168 N  N   . VAL B  234 ? 0.1234  0.1743 0.1049  -0.0057 0.0188  -0.0122 233 VAL B N   
4169 C  CA  . VAL B  234 ? 0.1068  0.1703 0.1119  -0.0121 0.0133  -0.0132 233 VAL B CA  
4170 C  C   . VAL B  234 ? 0.0942  0.1725 0.0900  0.0024  0.0086  -0.0079 233 VAL B C   
4171 O  O   . VAL B  234 ? 0.1208  0.1524 0.1023  0.0093  0.0110  -0.0017 233 VAL B O   
4172 C  CB  . VAL B  234 ? 0.1254  0.2224 0.1337  -0.0174 0.0337  -0.0146 233 VAL B CB  
4173 C  CG1 . VAL B  234 ? 0.1294  0.2694 0.1743  -0.0326 0.0323  -0.0350 233 VAL B CG1 
4174 C  CG2 . VAL B  234 ? 0.2188  0.2411 0.1416  -0.0336 0.0322  0.0126  233 VAL B CG2 
4175 N  N   . GLU B  235 ? 0.1266  0.1477 0.0840  -0.0030 0.0066  -0.0062 234 GLU B N   
4176 C  CA  . GLU B  235 ? 0.1305  0.1289 0.0941  -0.0074 -0.0179 -0.0041 234 GLU B CA  
4177 C  C   . GLU B  235 ? 0.1216  0.1696 0.0768  0.0009  0.0089  -0.0043 234 GLU B C   
4178 O  O   . GLU B  235 ? 0.1470  0.1944 0.0881  0.0051  0.0192  0.0004  234 GLU B O   
4179 C  CB  . GLU B  235 ? 0.1348  0.1495 0.0906  0.0064  -0.0055 -0.0111 234 GLU B CB  
4180 C  CG  . GLU B  235 ? 0.1427  0.1362 0.1268  -0.0119 -0.0177 -0.0293 234 GLU B CG  
4181 C  CD  . GLU B  235 ? 0.1951  0.1386 0.1368  0.0019  -0.0238 -0.0280 234 GLU B CD  
4182 O  OE1 . GLU B  235 ? 0.2319  0.1696 0.1276  -0.0034 -0.0089 -0.0011 234 GLU B OE1 
4183 O  OE2 . GLU B  235 ? 0.2425  0.1567 0.1441  0.0157  -0.0303 -0.0221 234 GLU B OE2 
4184 N  N   . GLY B  236 ? 0.1205  0.1567 0.1016  0.0053  -0.0165 0.0003  235 GLY B N   
4185 C  CA  . GLY B  236 ? 0.2102  0.1596 0.1093  0.0326  -0.0453 0.0168  235 GLY B CA  
4186 C  C   . GLY B  236 ? 0.2398  0.1879 0.1088  0.0312  -0.0423 -0.0021 235 GLY B C   
4187 O  O   . GLY B  236 ? 0.4031  0.2131 0.2084  0.0736  -0.1467 0.0106  235 GLY B O   
4188 N  N   . ASP B  237 ? 0.2210  0.1474 0.1082  0.0130  -0.0030 -0.0006 236 ASP B N   
4189 C  CA  . ASP B  237 ? 0.3010  0.1386 0.1023  0.0122  -0.0236 -0.0097 236 ASP B CA  
4190 C  C   . ASP B  237 ? 0.3370  0.1736 0.1027  0.0433  -0.0068 0.0012  236 ASP B C   
4191 O  O   . ASP B  237 ? 0.2389  0.1923 0.1215  0.0485  -0.0240 0.0122  236 ASP B O   
4192 C  CB  . ASP B  237 ? 0.3409  0.1621 0.1319  -0.0266 -0.0009 -0.0044 236 ASP B CB  
4193 C  CG  . ASP B  237 ? 0.3890  0.1962 0.2203  -0.0400 0.0231  0.0229  236 ASP B CG  
4194 O  OD1 . ASP B  237 ? 0.3890  0.3643 0.1682  -0.0694 0.0381  0.0229  236 ASP B OD1 
4195 O  OD2 . ASP B  237 ? 0.3819  0.2806 0.1603  -0.0445 0.0469  0.0198  236 ASP B OD2 
4196 N  N   A ASN B  238 ? 0.2766  0.2152 0.2113  0.0635  -0.0269 -0.0518 237 ASN B N   
4197 N  N   B ASN B  238 ? 0.3689  0.1998 0.0883  0.1194  -0.0414 0.0640  237 ASN B N   
4198 C  CA  A ASN B  238 ? 0.3316  0.2963 0.1136  0.0842  -0.0311 -0.0170 237 ASN B CA  
4199 C  CA  B ASN B  238 ? 0.4131  0.2278 0.1076  0.2153  -0.0134 0.0130  237 ASN B CA  
4200 C  C   A ASN B  238 ? 0.3122  0.1937 0.1023  0.0493  -0.0266 -0.0564 237 ASN B C   
4201 C  C   B ASN B  238 ? 0.2952  0.1844 0.1445  0.1201  -0.0374 0.0606  237 ASN B C   
4202 O  O   A ASN B  238 ? 0.2860  0.1826 0.1520  0.0153  0.0443  -0.0320 237 ASN B O   
4203 O  O   B ASN B  238 ? 0.3441  0.1445 0.0840  0.0252  -0.0192 0.0341  237 ASN B O   
4204 C  CB  A ASN B  238 ? 0.4156  0.2658 0.2608  0.0251  -0.1736 -0.0985 237 ASN B CB  
4205 C  CB  B ASN B  238 ? 0.3624  0.2680 0.1181  0.1967  0.0847  0.1552  237 ASN B CB  
4206 C  CG  A ASN B  238 ? 0.6212  0.2161 0.0969  0.2720  -0.0179 0.0094  237 ASN B CG  
4207 C  CG  B ASN B  238 ? 0.6170  0.5074 0.2134  0.0784  -0.0986 -0.0038 237 ASN B CG  
4208 O  OD1 A ASN B  238 ? 0.1689  0.3477 0.3632  -0.0496 0.0064  -0.1562 237 ASN B OD1 
4209 O  OD1 B ASN B  238 ? 0.8848  0.7149 0.6047  0.2575  0.4225  -0.0089 237 ASN B OD1 
4210 N  ND2 A ASN B  238 ? 0.0820  0.2235 0.2819  -0.0500 -0.0482 0.0039  237 ASN B ND2 
4211 N  ND2 B ASN B  238 ? 0.9279  0.9599 0.1720  -0.0380 0.0220  -0.0956 237 ASN B ND2 
4212 N  N   . ALA B  239 ? 0.2138  0.2856 0.0962  0.1025  -0.0312 -0.0223 238 ALA B N   
4213 C  CA  . ALA B  239 ? 0.1811  0.2213 0.1081  0.0722  -0.0194 0.0023  238 ALA B CA  
4214 C  C   . ALA B  239 ? 0.2375  0.2289 0.1289  0.1338  -0.0445 -0.0257 238 ALA B C   
4215 O  O   . ALA B  239 ? 0.3100  0.3323 0.1782  0.1952  -0.0748 -0.0583 238 ALA B O   
4216 C  CB  . ALA B  239 ? 0.1151  0.3671 0.1488  0.0243  -0.0149 -0.0010 238 ALA B CB  
4217 N  N   . VAL B  240 ? 0.1811  0.1782 0.0828  0.0419  -0.0133 -0.0005 239 VAL B N   
4218 C  CA  . VAL B  240 ? 0.2059  0.1869 0.0979  0.0400  -0.0066 0.0080  239 VAL B CA  
4219 C  C   . VAL B  240 ? 0.1890  0.1427 0.1021  0.0387  -0.0136 -0.0126 239 VAL B C   
4220 O  O   . VAL B  240 ? 0.2011  0.1847 0.1196  0.0718  0.0129  0.0083  239 VAL B O   
4221 C  CB  . VAL B  240 ? 0.3032  0.1520 0.1287  0.0186  0.0081  0.0044  239 VAL B CB  
4222 C  CG1 . VAL B  240 ? 0.3736  0.1610 0.1599  0.0307  -0.0232 -0.0152 239 VAL B CG1 
4223 C  CG2 . VAL B  240 ? 0.3481  0.2188 0.1260  0.0150  -0.0136 0.0407  239 VAL B CG2 
4224 N  N   . PRO B  241 ? 0.1639  0.1535 0.1031  0.0281  -0.0186 -0.0013 240 PRO B N   
4225 C  CA  . PRO B  241 ? 0.1754  0.1574 0.1005  -0.0055 -0.0184 0.0127  240 PRO B CA  
4226 C  C   . PRO B  241 ? 0.1682  0.1312 0.0908  0.0116  -0.0015 -0.0108 240 PRO B C   
4227 O  O   . PRO B  241 ? 0.1905  0.1243 0.1251  0.0140  -0.0168 -0.0108 240 PRO B O   
4228 C  CB  . PRO B  241 ? 0.1861  0.2296 0.1146  -0.0044 -0.0129 0.0166  240 PRO B CB  
4229 C  CG  . PRO B  241 ? 0.2095  0.3078 0.2009  -0.0100 -0.0669 0.1007  240 PRO B CG  
4230 C  CD  . PRO B  241 ? 0.1544  0.2529 0.1542  0.0234  -0.0124 0.0309  240 PRO B CD  
4231 N  N   . MET B  242 ? 0.1373  0.1678 0.0952  0.0083  -0.0044 0.0024  241 MET B N   
4232 C  CA  . MET B  242 ? 0.1101  0.1761 0.1362  0.0243  0.0008  0.0093  241 MET B CA  
4233 C  C   . MET B  242 ? 0.1298  0.1865 0.1014  0.0000  -0.0166 0.0108  241 MET B C   
4234 O  O   . MET B  242 ? 0.1465  0.2217 0.1128  -0.0236 -0.0154 0.0238  241 MET B O   
4235 C  CB  . MET B  242 ? 0.1337  0.2418 0.1980  0.0671  0.0397  0.0421  241 MET B CB  
4236 C  CG  . MET B  242 ? 0.2041  0.1653 0.2515  0.0428  0.0435  -0.0120 241 MET B CG  
4237 S  SD  . MET B  242 ? 0.1106  0.2020 0.2034  0.0147  0.0043  -0.0731 241 MET B SD  
4238 C  CE  . MET B  242 ? 0.1283  0.1879 0.1646  0.0062  0.0075  -0.0665 241 MET B CE  
4239 N  N   . GLN B  243 ? 0.1216  0.1930 0.1208  0.0031  -0.0103 0.0013  242 GLN B N   
4240 C  CA  . GLN B  243 ? 0.1398  0.2508 0.1028  0.0212  -0.0089 -0.0021 242 GLN B CA  
4241 C  C   . GLN B  243 ? 0.1190  0.2034 0.1225  0.0005  0.0018  -0.0085 242 GLN B C   
4242 O  O   . GLN B  243 ? 0.1249  0.2479 0.1205  0.0008  0.0025  -0.0130 242 GLN B O   
4243 C  CB  . GLN B  243 ? 0.2041  0.2551 0.1678  0.0758  -0.0575 -0.0176 242 GLN B CB  
4244 C  CG  . GLN B  243 ? 0.4185  0.4084 0.1659  0.1107  -0.1233 -0.0505 242 GLN B CG  
4245 C  CD  . GLN B  243 ? 0.3194  0.5716 0.4381  0.2345  -0.0142 0.0565  242 GLN B CD  
4246 O  OE1 . GLN B  243 ? 0.7929  0.7568 0.5872  0.4572  0.0053  0.2479  242 GLN B OE1 
4247 N  NE2 . GLN B  243 ? 0.4023  0.3711 0.4852  0.1623  -0.0932 -0.0080 242 GLN B NE2 
4248 N  N   . HIS B  244 ? 0.1233  0.1596 0.1197  0.0030  -0.0102 -0.0135 243 HIS B N   
4249 C  CA  . HIS B  244 ? 0.1136  0.1463 0.1031  0.0077  0.0039  -0.0223 243 HIS B CA  
4250 C  C   . HIS B  244 ? 0.1301  0.1093 0.1128  0.0055  0.0078  -0.0141 243 HIS B C   
4251 O  O   . HIS B  244 ? 0.1434  0.1333 0.1120  0.0016  0.0154  -0.0100 243 HIS B O   
4252 C  CB  . HIS B  244 ? 0.1488  0.1380 0.1606  0.0405  0.0050  -0.0319 243 HIS B CB  
4253 C  CG  . HIS B  244 ? 0.1883  0.1481 0.1897  0.0254  0.0285  -0.0210 243 HIS B CG  
4254 N  ND1 . HIS B  244 ? 0.2479  0.1603 0.3341  0.0502  0.0688  0.0057  243 HIS B ND1 
4255 C  CD2 . HIS B  244 ? 0.2737  0.1797 0.2623  0.0231  -0.0018 0.0489  243 HIS B CD2 
4256 C  CE1 . HIS B  244 ? 0.2321  0.1923 0.3370  0.0367  0.0340  0.0449  243 HIS B CE1 
4257 N  NE2 . HIS B  244 ? 0.3111  0.1926 0.2799  0.0383  -0.0263 0.0551  243 HIS B NE2 
4258 N  N   . ASN B  245 ? 0.1065  0.1134 0.1108  0.0178  -0.0053 -0.0254 244 ASN B N   
4259 C  CA  . ASN B  245 ? 0.1032  0.1261 0.1027  0.0189  -0.0077 -0.0270 244 ASN B CA  
4260 C  C   . ASN B  245 ? 0.1055  0.1276 0.1101  -0.0010 0.0082  -0.0078 244 ASN B C   
4261 O  O   . ASN B  245 ? 0.1023  0.1283 0.1164  0.0052  0.0035  -0.0049 244 ASN B O   
4262 C  CB  . ASN B  245 ? 0.1287  0.1101 0.1132  -0.0011 0.0222  -0.0105 244 ASN B CB  
4263 C  CG  . ASN B  245 ? 0.1022  0.1217 0.0810  0.0071  0.0109  -0.0143 244 ASN B CG  
4264 O  OD1 . ASN B  245 ? 0.1150  0.1226 0.0827  0.0125  0.0133  -0.0163 244 ASN B OD1 
4265 N  ND2 . ASN B  245 ? 0.1146  0.1160 0.1106  -0.0006 0.0049  -0.0277 244 ASN B ND2 
4266 N  N   . ASN B  246 ? 0.1239  0.1274 0.1049  0.0000  0.0004  -0.0370 245 ASN B N   
4267 C  CA  . ASN B  246 ? 0.1084  0.1474 0.1241  -0.0199 0.0078  -0.0387 245 ASN B CA  
4268 C  C   . ASN B  246 ? 0.1111  0.1359 0.1562  0.0145  0.0139  -0.0179 245 ASN B C   
4269 O  O   . ASN B  246 ? 0.1477  0.1384 0.2784  -0.0022 -0.0526 -0.0058 245 ASN B O   
4270 C  CB  . ASN B  246 ? 0.1274  0.1596 0.1204  0.0149  0.0063  -0.0323 245 ASN B CB  
4271 C  CG  . ASN B  246 ? 0.1535  0.1585 0.1225  0.0245  0.0053  -0.0381 245 ASN B CG  
4272 O  OD1 . ASN B  246 ? 0.1362  0.1659 0.1474  0.0203  0.0036  -0.0290 245 ASN B OD1 
4273 N  ND2 . ASN B  246 ? 0.2788  0.2812 0.1483  0.1370  0.0292  -0.0512 245 ASN B ND2 
4274 N  N   . ARG B  247 ? 0.1169  0.1405 0.1344  -0.0194 0.0155  -0.0367 246 ARG B N   
4275 C  CA  . ARG B  247 ? 0.1395  0.1362 0.1732  -0.0223 0.0199  -0.0583 246 ARG B CA  
4276 C  C   . ARG B  247 ? 0.1287  0.1470 0.1736  -0.0065 0.0218  -0.0447 246 ARG B C   
4277 O  O   . ARG B  247 ? 0.1373  0.1465 0.1689  -0.0120 0.0035  -0.0515 246 ARG B O   
4278 C  CB  . ARG B  247 ? 0.1177  0.1445 0.1775  -0.0248 0.0249  -0.0567 246 ARG B CB  
4279 C  CG  . ARG B  247 ? 0.1326  0.1560 0.1729  -0.0212 0.0227  -0.0260 246 ARG B CG  
4280 C  CD  . ARG B  247 ? 0.1316  0.1423 0.1919  -0.0312 0.0293  -0.0619 246 ARG B CD  
4281 N  NE  . ARG B  247 ? 0.1312  0.1488 0.1919  -0.0359 0.0464  -0.0529 246 ARG B NE  
4282 C  CZ  . ARG B  247 ? 0.1588  0.1693 0.1932  -0.0392 0.0496  -0.0592 246 ARG B CZ  
4283 N  NH1 . ARG B  247 ? 0.1465  0.2134 0.1316  -0.0337 0.0323  -0.0587 246 ARG B NH1 
4284 N  NH2 . ARG B  247 ? 0.1768  0.1980 0.1923  -0.0608 0.0615  -0.0505 246 ARG B NH2 
4285 N  N   . PRO B  248 ? 0.1567  0.1398 0.1567  -0.0069 0.0185  -0.0405 247 PRO B N   
4286 C  CA  . PRO B  248 ? 0.1671  0.1502 0.1793  -0.0031 -0.0022 -0.0798 247 PRO B CA  
4287 C  C   . PRO B  248 ? 0.1624  0.1344 0.1632  -0.0222 -0.0043 -0.0714 247 PRO B C   
4288 O  O   . PRO B  248 ? 0.1549  0.1506 0.1879  -0.0236 0.0257  -0.0543 247 PRO B O   
4289 C  CB  . PRO B  248 ? 0.1793  0.1359 0.2429  0.0011  0.0110  -0.0631 247 PRO B CB  
4290 C  CG  . PRO B  248 ? 0.3089  0.1671 0.2273  0.0057  0.0178  -0.0618 247 PRO B CG  
4291 C  CD  . PRO B  248 ? 0.2030  0.1506 0.1930  0.0005  0.0457  -0.0194 247 PRO B CD  
4292 N  N   . THR B  249 ? 0.1481  0.1495 0.1757  -0.0186 0.0042  -0.0686 248 THR B N   
4293 C  CA  . THR B  249 ? 0.1341  0.1366 0.1488  -0.0154 0.0201  -0.0527 248 THR B CA  
4294 C  C   . THR B  249 ? 0.1635  0.1560 0.1822  -0.0140 0.0435  -0.0474 248 THR B C   
4295 O  O   . THR B  249 ? 0.1732  0.1535 0.2073  -0.0089 0.0167  -0.0545 248 THR B O   
4296 C  CB  . THR B  249 ? 0.1861  0.1639 0.1509  -0.0106 0.0539  -0.0701 248 THR B CB  
4297 O  OG1 . THR B  249 ? 0.1772  0.1707 0.2098  -0.0194 0.0570  -0.0813 248 THR B OG1 
4298 C  CG2 . THR B  249 ? 0.1585  0.1610 0.1606  -0.0275 0.0379  -0.0466 248 THR B CG2 
4299 N  N   . GLN B  250 ? 0.1517  0.1729 0.1851  -0.0295 0.0370  -0.0710 249 GLN B N   
4300 C  CA  . GLN B  250 ? 0.1412  0.2011 0.1944  -0.0587 0.0497  -0.1131 249 GLN B CA  
4301 C  C   . GLN B  250 ? 0.1253  0.1941 0.2109  -0.0321 0.0428  -0.0725 249 GLN B C   
4302 O  O   . GLN B  250 ? 0.1919  0.2284 0.1696  -0.0427 0.0420  -0.0932 249 GLN B O   
4303 C  CB  . GLN B  250 ? 0.1614  0.2030 0.2089  -0.0288 0.0430  -0.1142 249 GLN B CB  
4304 C  CG  . GLN B  250 ? 0.1650  0.2220 0.1822  -0.0463 0.0482  -0.0853 249 GLN B CG  
4305 C  CD  . GLN B  250 ? 0.2127  0.2163 0.2034  -0.0781 0.0762  -0.0665 249 GLN B CD  
4306 O  OE1 . GLN B  250 ? 0.2407  0.2400 0.2308  -0.0891 0.0583  -0.0522 249 GLN B OE1 
4307 N  NE2 . GLN B  250 ? 0.2161  0.2077 0.2117  -0.0576 0.0636  -0.0726 249 GLN B NE2 
4308 N  N   . PRO B  251 ? 0.1707  0.1926 0.2354  -0.0447 0.0541  -0.1001 250 PRO B N   
4309 C  CA  . PRO B  251 ? 0.2009  0.2314 0.2550  -0.0231 -0.0120 -0.0992 250 PRO B CA  
4310 C  C   . PRO B  251 ? 0.1650  0.2120 0.2109  -0.0475 0.0190  -0.1200 250 PRO B C   
4311 O  O   . PRO B  251 ? 0.1768  0.1987 0.2066  -0.0403 0.0339  -0.0928 250 PRO B O   
4312 C  CB  . PRO B  251 ? 0.3251  0.1930 0.4780  -0.0760 -0.0862 -0.1023 250 PRO B CB  
4313 C  CG  . PRO B  251 ? 0.3391  0.2224 0.3718  -0.1309 0.0615  -0.0996 250 PRO B CG  
4314 C  CD  . PRO B  251 ? 0.2120  0.1711 0.3219  -0.0525 0.0268  -0.0521 250 PRO B CD  
4315 N  N   . LEU B  252 ? 0.2593  0.2680 0.2235  -0.0792 0.0408  -0.1213 251 LEU B N   
4316 C  CA  . LEU B  252 ? 0.2752  0.2795 0.1919  -0.1176 0.0696  -0.1301 251 LEU B CA  
4317 C  C   . LEU B  252 ? 0.2536  0.2380 0.1517  -0.0680 0.0208  -0.1082 251 LEU B C   
4318 O  O   . LEU B  252 ? 0.2805  0.2116 0.2206  -0.0593 -0.0012 -0.1185 251 LEU B O   
4319 C  CB  . LEU B  252 ? 0.3470  0.3359 0.2242  -0.1116 0.0867  -0.1060 251 LEU B CB  
4320 C  CG  . LEU B  252 ? 0.5258  0.3348 0.2145  -0.0455 0.1237  -0.1085 251 LEU B CG  
4321 C  CD1 . LEU B  252 ? 0.3140  0.3840 0.1811  -0.1685 0.0365  -0.0709 251 LEU B CD1 
4322 C  CD2 . LEU B  252 ? 0.3028  0.4999 0.2345  -0.0517 0.1050  -0.0903 251 LEU B CD2 
4323 N  N   . LYS B  253 ? 0.2633  0.2291 0.2813  -0.0846 0.0272  -0.1523 252 LYS B N   
4324 C  CA  . LYS B  253 ? 0.2089  0.2579 0.3632  -0.0939 -0.0289 -0.1458 252 LYS B CA  
4325 C  C   . LYS B  253 ? 0.2719  0.2522 0.3383  -0.0996 -0.0297 -0.1361 252 LYS B C   
4326 O  O   . LYS B  253 ? 0.2511  0.2946 0.3513  -0.0790 -0.0367 -0.1188 252 LYS B O   
4327 C  CB  . LYS B  253 ? 0.2099  0.2971 0.3237  -0.0535 -0.0055 -0.0882 252 LYS B CB  
4328 C  CG  . LYS B  253 ? 0.2293  0.3481 0.3972  -0.0850 -0.0507 -0.0473 252 LYS B CG  
4329 C  CD  . LYS B  253 ? 0.3322  0.4077 0.4827  -0.1392 0.1032  -0.0762 252 LYS B CD  
4330 C  CE  . LYS B  253 ? 0.4688  0.4605 0.5814  -0.2280 0.0766  0.1016  252 LYS B CE  
4331 N  NZ  . LYS B  253 ? 0.9824  0.3922 0.8242  -0.2375 0.2156  -0.0542 252 LYS B NZ  
4332 N  N   . GLY B  254 ? 0.3352  0.2784 0.2852  -0.0907 -0.0936 -0.1028 253 GLY B N   
4333 C  CA  . GLY B  254 ? 0.3330  0.2794 0.2640  -0.0427 -0.0588 -0.1067 253 GLY B CA  
4334 C  C   . GLY B  254 ? 0.2745  0.2852 0.3093  -0.1230 -0.0070 -0.1272 253 GLY B C   
4335 O  O   . GLY B  254 ? 0.2741  0.4250 0.2579  -0.1435 -0.0242 -0.1626 253 GLY B O   
4336 N  N   . ARG B  255 ? 0.1876  0.2819 0.2339  -0.0659 -0.0159 -0.1201 254 ARG B N   
4337 C  CA  . ARG B  255 ? 0.1951  0.3150 0.1757  -0.0644 0.0096  -0.1313 254 ARG B CA  
4338 C  C   . ARG B  255 ? 0.1941  0.3348 0.1641  -0.0656 -0.0329 -0.1151 254 ARG B C   
4339 O  O   . ARG B  255 ? 0.2337  0.4041 0.2350  -0.0445 0.0165  -0.1564 254 ARG B O   
4340 C  CB  . ARG B  255 ? 0.1890  0.2643 0.1434  -0.0664 0.0069  -0.0960 254 ARG B CB  
4341 C  CG  . ARG B  255 ? 0.1786  0.3068 0.1833  -0.0788 0.0133  -0.1287 254 ARG B CG  
4342 C  CD  . ARG B  255 ? 0.1851  0.2648 0.1560  -0.0223 -0.0185 -0.1097 254 ARG B CD  
4343 N  NE  . ARG B  255 ? 0.1556  0.2156 0.1926  -0.0422 -0.0010 -0.0741 254 ARG B NE  
4344 C  CZ  . ARG B  255 ? 0.1197  0.1897 0.1678  -0.0390 0.0168  -0.0774 254 ARG B CZ  
4345 N  NH1 . ARG B  255 ? 0.1395  0.2109 0.1754  -0.0403 0.0402  -0.1057 254 ARG B NH1 
4346 N  NH2 . ARG B  255 ? 0.1452  0.1973 0.1592  -0.0238 0.0363  -0.0668 254 ARG B NH2 
4347 N  N   . THR B  256 ? 0.2174  0.3143 0.1689  -0.0970 -0.0508 -0.0608 255 THR B N   
4348 C  CA  . THR B  256 ? 0.2476  0.3255 0.1793  -0.1033 -0.0323 -0.0527 255 THR B CA  
4349 C  C   . THR B  256 ? 0.2102  0.3000 0.1955  -0.0671 -0.0252 -0.0952 255 THR B C   
4350 O  O   . THR B  256 ? 0.1682  0.3725 0.2469  -0.0726 0.0186  -0.1118 255 THR B O   
4351 C  CB  . THR B  256 ? 0.2654  0.4641 0.2102  -0.1229 -0.0765 -0.0363 255 THR B CB  
4352 O  OG1 . THR B  256 ? 0.3617  0.5683 0.2398  -0.2162 -0.0545 -0.1064 255 THR B OG1 
4353 C  CG2 . THR B  256 ? 0.4246  0.4170 0.1897  -0.1751 -0.0943 0.0083  255 THR B CG2 
4354 N  N   . VAL B  257 ? 0.1808  0.2751 0.1912  -0.0434 -0.0226 -0.0810 256 VAL B N   
4355 C  CA  . VAL B  257 ? 0.1355  0.2709 0.1474  -0.0220 -0.0153 -0.0718 256 VAL B CA  
4356 C  C   . VAL B  257 ? 0.1391  0.2770 0.1229  -0.0087 -0.0151 -0.0743 256 VAL B C   
4357 O  O   . VAL B  257 ? 0.2124  0.3050 0.1416  -0.0164 0.0080  -0.1092 256 VAL B O   
4358 C  CB  . VAL B  257 ? 0.1535  0.2479 0.1775  0.0126  -0.0208 -0.0871 256 VAL B CB  
4359 C  CG1 . VAL B  257 ? 0.1470  0.2892 0.2238  -0.0506 0.0088  -0.1265 256 VAL B CG1 
4360 C  CG2 . VAL B  257 ? 0.1851  0.2590 0.1574  0.0427  -0.0059 -0.0694 256 VAL B CG2 
4361 N  N   . ARG B  258 ? 0.1574  0.2436 0.1502  -0.0177 -0.0204 -0.0671 257 ARG B N   
4362 C  CA  . ARG B  258 ? 0.1366  0.3014 0.1544  -0.0299 -0.0092 -0.0834 257 ARG B CA  
4363 C  C   . ARG B  258 ? 0.1289  0.2600 0.1344  -0.0247 -0.0147 -0.0851 257 ARG B C   
4364 O  O   . ARG B  258 ? 0.1797  0.3143 0.1319  -0.0298 -0.0355 -0.0946 257 ARG B O   
4365 C  CB  . ARG B  258 ? 0.1386  0.3664 0.1768  -0.0154 -0.0488 -0.1088 257 ARG B CB  
4366 C  CG  . ARG B  258 ? 0.1527  0.3923 0.2023  -0.0428 -0.0310 -0.0995 257 ARG B CG  
4367 C  CD  . ARG B  258 ? 0.1696  0.4817 0.1736  -0.0364 -0.0212 -0.1160 257 ARG B CD  
4368 N  NE  . ARG B  258 ? 0.1481  0.4013 0.1937  -0.0480 -0.0301 -0.0907 257 ARG B NE  
4369 C  CZ  . ARG B  258 ? 0.1287  0.4278 0.2665  -0.0047 -0.0436 -0.1074 257 ARG B CZ  
4370 N  NH1 . ARG B  258 ? 0.1531  0.5141 0.2608  0.0207  -0.0681 -0.0515 257 ARG B NH1 
4371 N  NH2 . ARG B  258 ? 0.1757  0.4027 0.2260  -0.0312 -0.0515 -0.1122 257 ARG B NH2 
4372 N  N   . ALA B  259 ? 0.1592  0.2942 0.1402  -0.0474 -0.0133 -0.0776 258 ALA B N   
4373 C  CA  . ALA B  259 ? 0.1782  0.2838 0.1160  -0.0359 -0.0219 -0.0591 258 ALA B CA  
4374 C  C   . ALA B  259 ? 0.2246  0.3000 0.1020  0.0084  -0.0535 -0.0701 258 ALA B C   
4375 O  O   . ALA B  259 ? 0.2005  0.3265 0.1416  -0.0108 -0.0741 -0.0600 258 ALA B O   
4376 C  CB  . ALA B  259 ? 0.1574  0.3696 0.1524  -0.0172 -0.0117 -0.1081 258 ALA B CB  
4377 N  N   . SER B  260 ? 0.1973  0.2752 0.1459  0.0008  -0.0490 -0.0690 259 SER B N   
4378 C  CA  . SER B  260 ? 0.1703  0.2996 0.1337  -0.0252 -0.0267 -0.0716 259 SER B CA  
4379 C  C   . SER B  260 ? 0.2188  0.3434 0.1154  -0.0060 -0.0757 -0.0303 259 SER B C   
4380 O  O   . SER B  260 ? 0.3039  0.3449 0.1617  0.0141  -0.0553 -0.0005 259 SER B O   
4381 C  CB  . SER B  260 ? 0.1835  0.3754 0.1657  0.0116  -0.0848 -0.1161 259 SER B CB  
4382 O  OG  . SER B  260 ? 0.1955  0.2967 0.1459  0.0042  -0.0882 -0.0433 259 SER B OG  
4383 N  N   . PHE B  261 ? 0.2053  0.3366 0.1142  -0.0147 -0.0226 -0.0587 260 PHE B N   
4384 C  CA  . PHE B  261 ? 0.2222  0.3359 0.1337  -0.0106 -0.0162 -0.0472 260 PHE B CA  
4385 C  C   . PHE B  261 ? 0.3409  0.3377 0.1101  -0.0695 -0.0330 -0.0363 260 PHE B C   
4386 O  O   . PHE B  261 ? 0.3606  0.5175 0.1524  0.0179  0.0059  -0.0688 260 PHE B O   
4387 C  CB  . PHE B  261 ? 0.2125  0.2957 0.1876  0.0069  -0.0237 -0.0644 260 PHE B CB  
4388 C  CG  . PHE B  261 ? 0.2005  0.2999 0.1441  0.0006  -0.0170 -0.0715 260 PHE B CG  
4389 C  CD1 . PHE B  261 ? 0.1682  0.2978 0.1524  -0.0044 -0.0265 -0.0627 260 PHE B CD1 
4390 C  CD2 . PHE B  261 ? 0.2396  0.3031 0.1463  0.0070  -0.0170 -0.0468 260 PHE B CD2 
4391 C  CE1 . PHE B  261 ? 0.1914  0.2712 0.1635  -0.0062 -0.0471 -0.0693 260 PHE B CE1 
4392 C  CE2 . PHE B  261 ? 0.2339  0.3559 0.1517  0.0083  -0.0439 -0.0331 260 PHE B CE2 
4393 C  CZ  . PHE B  261 ? 0.2181  0.2644 0.1738  -0.0068 -0.0229 -0.0396 260 PHE B CZ  
4394 O  OXT . PHE B  261 ? 0.2827  0.3624 0.1797  -0.0317 -0.0337 -0.0846 260 PHE B OXT 
4395 ZN ZN  . ZN  C  .   ? 0.1014  0.0960 0.0855  0.0002  -0.0117 0.0005  301 ZN  A ZN  
4396 O  O18 A 84Z D  .   ? 10.3451 5.2443 10.6705 4.1343  -2.1384 3.8317  302 84Z A O18 
4397 O  O18 B 84Z D  .   ? 0.1962  0.3959 0.2687  -0.0159 0.0580  0.0699  302 84Z A O18 
4398 S  S16 A 84Z D  .   ? 0.2337  0.2572 0.1531  -0.1057 0.0551  -0.0147 302 84Z A S16 
4399 S  S16 B 84Z D  .   ? 0.2418  0.2152 0.1800  0.0105  0.0158  0.0329  302 84Z A S16 
4400 O  O17 A 84Z D  .   ? 0.2572  0.1628 0.2791  -0.0718 0.0078  0.0413  302 84Z A O17 
4401 O  O17 B 84Z D  .   ? 0.2975  0.1373 0.1448  0.0480  0.0386  0.0679  302 84Z A O17 
4402 C  C19 A 84Z D  .   ? 0.1617  0.1743 0.2055  -0.0392 -0.0546 -0.0024 302 84Z A C19 
4403 C  C19 B 84Z D  .   ? 0.1951  0.2030 0.2834  -0.0449 0.1861  -0.0903 302 84Z A C19 
4404 C  C24 A 84Z D  .   ? 0.2425  0.3287 0.2116  0.0311  -0.0277 -0.0670 302 84Z A C24 
4405 C  C24 B 84Z D  .   ? 0.4478  0.1671 0.4221  0.0260  0.2023  -0.1099 302 84Z A C24 
4406 C  C23 A 84Z D  .   ? 0.2161  0.3510 0.3207  0.0432  0.0884  -0.0223 302 84Z A C23 
4407 C  C23 B 84Z D  .   ? 0.2404  0.2327 0.5092  0.0048  0.0692  0.1680  302 84Z A C23 
4408 C  C22 A 84Z D  .   ? 0.2016  0.2576 0.2644  -0.0131 0.0367  -0.0480 302 84Z A C22 
4409 C  C22 B 84Z D  .   ? 0.3638  0.6280 0.2931  -0.1242 0.1126  -0.0348 302 84Z A C22 
4410 C  C21 A 84Z D  .   ? 0.1998  0.2397 0.2680  0.0329  0.0930  -0.0454 302 84Z A C21 
4411 C  C21 B 84Z D  .   ? 0.2536  0.6950 0.3955  -0.0344 0.1861  -0.1476 302 84Z A C21 
4412 C  C20 A 84Z D  .   ? 0.2490  0.2247 0.2411  0.1069  0.1204  0.0225  302 84Z A C20 
4413 C  C20 B 84Z D  .   ? 0.1991  0.4612 0.2546  -0.0627 0.0956  -0.0937 302 84Z A C20 
4414 C  C3  A 84Z D  .   ? 0.1657  0.1225 0.1646  -0.0247 0.0107  0.0272  302 84Z A C3  
4415 C  C3  B 84Z D  .   ? 0.2813  0.1664 0.1445  -0.0343 0.0396  -0.0200 302 84Z A C3  
4416 C  C2  A 84Z D  .   ? 0.1815  0.1973 0.1187  -0.0299 0.0680  -0.0348 302 84Z A C2  
4417 C  C2  B 84Z D  .   ? 0.3139  0.1750 0.0937  -0.0609 0.0030  0.0228  302 84Z A C2  
4418 C  C4  A 84Z D  .   ? 0.1483  0.1976 0.1840  0.0133  0.0000  0.0526  302 84Z A C4  
4419 C  C4  B 84Z D  .   ? 0.1817  0.1772 0.1377  -0.0020 0.0227  -0.0342 302 84Z A C4  
4420 C  C12 A 84Z D  .   ? 0.2734  0.2235 0.1585  -0.0240 -0.0025 0.0305  302 84Z A C12 
4421 C  C12 B 84Z D  .   ? 0.2441  0.2115 0.2594  -0.0318 -0.0671 -0.0137 302 84Z A C12 
4422 O  O14 A 84Z D  .   ? 0.3610  0.3007 0.1289  -0.0259 -0.0041 0.0329  302 84Z A O14 
4423 O  O14 B 84Z D  .   ? 0.1840  0.1264 0.4903  -0.0489 0.0661  0.0430  302 84Z A O14 
4424 C  C15 A 84Z D  .   ? 0.3758  0.2508 0.2461  -0.0261 -0.1114 -0.0139 302 84Z A C15 
4425 C  C15 B 84Z D  .   ? 0.3492  0.2615 0.8398  0.0178  0.1500  -0.2332 302 84Z A C15 
4426 O  O13 A 84Z D  .   ? 0.2020  0.3007 0.1700  0.0219  -0.0270 0.0618  302 84Z A O13 
4427 O  O13 B 84Z D  .   ? 0.2812  0.1689 0.2615  -0.0318 -0.0416 0.0030  302 84Z A O13 
4428 C  C5  A 84Z D  .   ? 0.1890  0.1423 0.1271  -0.0009 0.0055  0.0317  302 84Z A C5  
4429 C  C5  B 84Z D  .   ? 0.1718  0.0785 0.1502  0.0121  -0.0188 0.0116  302 84Z A C5  
4430 C  C6  A 84Z D  .   ? 0.1585  0.1380 0.1234  0.0127  0.0051  -0.0449 302 84Z A C6  
4431 C  C6  B 84Z D  .   ? 0.1186  0.1023 0.0996  -0.0097 -0.0134 -0.0044 302 84Z A C6  
4432 C  C1  A 84Z D  .   ? 0.1729  0.1815 0.1144  -0.0329 0.0403  -0.0282 302 84Z A C1  
4433 C  C1  B 84Z D  .   ? 0.2260  0.1169 0.0734  -0.0341 -0.0270 0.0119  302 84Z A C1  
4434 CL CL1 A 84Z D  .   ? 0.1225  0.2059 0.1639  -0.0116 0.0088  -0.0388 302 84Z A CL1 
4435 CL CL1 B 84Z D  .   ? 0.1966  0.0967 0.0928  -0.0034 -0.0307 -0.0004 302 84Z A CL1 
4436 S  S7  A 84Z D  .   ? 0.1438  0.1513 0.1333  0.0142  0.0027  -0.0004 302 84Z A S7  
4437 S  S7  B 84Z D  .   ? 0.0740  0.0725 0.0777  0.0022  -0.0131 -0.0052 302 84Z A S7  
4438 O  O8  A 84Z D  .   ? 0.1826  0.1578 0.1678  -0.0055 0.0325  -0.0177 302 84Z A O8  
4439 O  O8  B 84Z D  .   ? 0.0607  0.0784 0.0785  0.0085  -0.0134 -0.0021 302 84Z A O8  
4440 O  O9  A 84Z D  .   ? 0.1517  0.1470 0.1588  0.0677  -0.0034 -0.0483 302 84Z A O9  
4441 O  O9  B 84Z D  .   ? 0.0669  0.0917 0.0964  0.0025  -0.0184 0.0209  302 84Z A O9  
4442 N  N10 A 84Z D  .   ? 0.1542  0.1585 0.1865  -0.0091 -0.0044 -0.0332 302 84Z A N10 
4443 N  N10 B 84Z D  .   ? 0.0564  0.0801 0.1146  0.0131  -0.0216 0.0094  302 84Z A N10 
4444 C  C1  . EDO E  .   ? 0.6280  0.4526 0.2622  0.2824  -0.0402 -0.1049 303 EDO A C1  
4445 O  O1  . EDO E  .   ? 0.6409  0.3649 0.3503  0.1715  -0.0110 -0.0358 303 EDO A O1  
4446 C  C2  . EDO E  .   ? 0.4916  0.3406 0.2479  0.1333  0.0719  0.0494  303 EDO A C2  
4447 O  O2  . EDO E  .   ? 0.3327  0.2072 0.2759  0.0358  -0.0392 -0.0422 303 EDO A O2  
4448 C  C1  . EDO F  .   ? 0.3312  0.4677 0.4357  -0.0723 0.0138  0.0301  304 EDO A C1  
4449 O  O1  . EDO F  .   ? 0.5615  0.3498 0.3686  0.0149  -0.0214 -0.0041 304 EDO A O1  
4450 C  C2  . EDO F  .   ? 0.3503  0.3139 0.3887  -0.0184 -0.0453 0.0377  304 EDO A C2  
4451 O  O2  . EDO F  .   ? 0.4446  0.8168 0.8305  -0.1492 -0.1921 0.4756  304 EDO A O2  
4452 C  C1  . EDO G  .   ? 0.2898  0.2676 0.3089  -0.0245 0.0048  -0.0222 305 EDO A C1  
4453 O  O1  . EDO G  .   ? 0.2055  0.2055 0.3265  -0.0239 -0.0068 0.0819  305 EDO A O1  
4454 C  C2  . EDO G  .   ? 0.3916  0.4081 0.4604  -0.1061 0.1368  -0.1136 305 EDO A C2  
4455 O  O2  . EDO G  .   ? 0.3269  0.3431 0.4207  -0.0569 0.0473  -0.0308 305 EDO A O2  
4456 C  C   . ACT H  .   ? 0.4911  0.3819 0.3394  0.0597  -0.0396 -0.0203 306 ACT A C   
4457 O  O   . ACT H  .   ? 0.5168  0.5529 0.4691  0.1032  0.0644  -0.0480 306 ACT A O   
4458 O  OXT . ACT H  .   ? 0.4106  0.4745 0.3873  0.0476  -0.0919 -0.0160 306 ACT A OXT 
4459 C  CH3 . ACT H  .   ? 0.3998  0.2776 0.2141  0.0395  0.0491  0.0389  306 ACT A CH3 
4460 C  C   . ACT I  .   ? 0.3998  0.3043 0.3243  0.0062  -0.0278 0.0759  307 ACT A C   
4461 O  O   . ACT I  .   ? 0.3258  0.4045 0.4616  0.0147  -0.0485 0.0318  307 ACT A O   
4462 O  OXT . ACT I  .   ? 0.5253  0.4097 0.4282  -0.0140 -0.1046 -0.0001 307 ACT A OXT 
4463 C  CH3 . ACT I  .   ? 0.3480  0.4199 0.3237  0.0761  -0.0408 -0.0408 307 ACT A CH3 
4464 C  C1  . PEG J  .   ? 0.5711  0.3054 0.4532  -0.0414 0.2359  0.0251  308 PEG A C1  
4465 O  O1  . PEG J  .   ? 0.3251  0.3262 0.3510  -0.0480 0.0369  0.0135  308 PEG A O1  
4466 C  C2  . PEG J  .   ? 0.4195  0.3563 0.4393  -0.1089 0.2767  -0.0350 308 PEG A C2  
4467 O  O2  . PEG J  .   ? 0.6258  1.0840 0.4511  -0.2083 0.0974  -0.0241 308 PEG A O2  
4468 C  C3  . PEG J  .   ? 0.2504  0.6969 0.4918  -0.0519 0.1517  -0.0650 308 PEG A C3  
4469 C  C4  . PEG J  .   ? 0.5022  0.6103 0.7461  -0.0248 0.0814  0.3916  308 PEG A C4  
4470 O  O4  . PEG J  .   ? 0.4013  0.3319 0.4268  0.0482  0.0702  0.0155  308 PEG A O4  
4471 O  O2  . PEG K  .   ? 1.0075  1.8169 0.7425  0.2067  0.0474  0.3112  309 PEG A O2  
4472 C  C3  . PEG K  .   ? 1.1957  1.4651 1.0811  -0.0270 0.4800  0.1268  309 PEG A C3  
4473 C  C4  . PEG K  .   ? 0.9599  1.8886 0.4461  0.1525  0.2199  0.0429  309 PEG A C4  
4474 O  O4  . PEG K  .   ? 0.4002  0.8984 0.5105  -0.0946 0.1613  -0.2210 309 PEG A O4  
4475 C  C1  . PEG L  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG A C1  
4476 O  O1  . PEG L  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG A O1  
4477 C  C2  . PEG L  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG A C2  
4478 O  O2  . PEG L  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG A O2  
4479 C  C3  . PEG L  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG A C3  
4480 C  C4  . PEG L  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG A C4  
4481 O  O4  . PEG L  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG A O4  
4482 C  C1  . EDO M  .   ? 0.2813  0.4329 0.3506  0.0044  0.0154  0.0155  311 EDO A C1  
4483 O  O1  . EDO M  .   ? 0.3707  0.2687 0.3395  0.0617  -0.0199 -0.0077 311 EDO A O1  
4484 C  C2  . EDO M  .   ? 0.2597  0.2702 0.2960  0.0151  0.0023  0.0301  311 EDO A C2  
4485 O  O2  . EDO M  .   ? 0.2942  0.3905 0.3632  0.0245  0.0068  0.0244  311 EDO A O2  
4486 C  C1  . EDO N  .   ? 0.2558  0.2240 0.2106  0.0040  -0.0205 -0.0042 312 EDO A C1  
4487 O  O1  . EDO N  .   ? 0.4936  0.5037 0.4232  -0.0102 0.0419  -0.1313 312 EDO A O1  
4488 C  C2  . EDO N  .   ? 0.2587  0.2662 0.2368  0.0347  -0.0666 -0.0482 312 EDO A C2  
4489 O  O2  . EDO N  .   ? 0.3316  0.4447 0.3668  -0.0092 -0.0274 -0.0156 312 EDO A O2  
4490 C  C1  . EDO O  .   ? 0.3635  0.3140 0.2267  -0.0332 0.0171  -0.0108 313 EDO A C1  
4491 O  O1  . EDO O  .   ? 0.2546  0.2461 0.1502  0.0283  0.0121  0.0455  313 EDO A O1  
4492 C  C2  . EDO O  .   ? 0.3646  0.2525 0.3467  -0.0219 -0.0399 0.0278  313 EDO A C2  
4493 O  O2  . EDO O  .   ? 0.2917  0.2855 0.2350  0.0021  -0.0093 0.0066  313 EDO A O2  
4494 C  C1  . EDO P  .   ? 0.3398  0.3506 0.3230  -0.0214 0.0046  -0.0287 314 EDO A C1  
4495 O  O1  . EDO P  .   ? 0.3984  0.3649 0.3765  -0.0034 0.0156  0.0032  314 EDO A O1  
4496 C  C2  . EDO P  .   ? 0.3092  0.3208 0.2755  0.0085  0.0089  -0.0093 314 EDO A C2  
4497 O  O2  . EDO P  .   ? 0.3818  0.3625 0.3765  -0.0122 0.0299  0.0061  314 EDO A O2  
4498 C  C1  . EDO Q  .   ? 0.3225  0.2981 0.3133  -0.0078 0.0038  -0.0116 315 EDO A C1  
4499 O  O1  . EDO Q  .   ? 0.3449  0.3592 0.3582  0.0046  0.0011  -0.0063 315 EDO A O1  
4500 C  C2  . EDO Q  .   ? 0.3595  0.3258 0.3452  0.0138  -0.0587 0.0249  315 EDO A C2  
4501 O  O2  . EDO Q  .   ? 0.2819  0.3194 0.2906  -0.0205 0.0380  -0.0260 315 EDO A O2  
4502 ZN ZN  . ZN  R  .   ? 0.0928  0.1323 0.0950  -0.0041 0.0027  -0.0313 301 ZN  B ZN  
4503 O  O18 A 84Z S  .   ? 0.2117  0.5389 0.1071  -0.0807 0.0783  -0.1130 302 84Z B O18 
4504 O  O18 B 84Z S  .   ? 0.1076  0.3657 0.3402  0.0564  -0.0323 -0.0487 302 84Z B O18 
4505 S  S16 A 84Z S  .   ? 0.2755  0.2066 0.1720  -0.0006 0.0416  -0.0471 302 84Z B S16 
4506 S  S16 B 84Z S  .   ? 0.1506  0.1966 0.2235  -0.0232 0.0389  -0.0223 302 84Z B S16 
4507 O  O17 A 84Z S  .   ? 0.3811  0.2073 0.2267  0.0547  0.0814  0.0439  302 84Z B O17 
4508 O  O17 B 84Z S  .   ? 0.2777  0.2178 0.2848  -0.0833 0.0898  -0.0330 302 84Z B O17 
4509 C  C19 A 84Z S  .   ? 0.0908  0.3276 0.2798  -0.0006 0.0162  0.0453  302 84Z B C19 
4510 C  C19 B 84Z S  .   ? 0.1696  0.1817 0.2210  -0.0234 0.0488  -0.0576 302 84Z B C19 
4511 C  C24 A 84Z S  .   ? 0.3316  0.2820 0.1973  -0.0996 0.0417  0.0037  302 84Z B C24 
4512 C  C24 B 84Z S  .   ? 0.1456  0.1930 0.2089  -0.0368 0.0826  -0.0190 302 84Z B C24 
4513 C  C23 A 84Z S  .   ? 0.4120  0.3067 0.2500  -0.1158 0.0013  0.0789  302 84Z B C23 
4514 C  C23 B 84Z S  .   ? 0.2892  0.2451 0.1932  -0.0783 0.0789  -0.0789 302 84Z B C23 
4515 C  C22 A 84Z S  .   ? 0.2544  0.2132 0.2601  0.0155  0.0637  -0.0618 302 84Z B C22 
4516 C  C22 B 84Z S  .   ? 0.2601  0.2661 0.2633  0.0514  0.1232  -0.0615 302 84Z B C22 
4517 C  C21 A 84Z S  .   ? 0.1215  0.2679 0.3183  -0.0348 0.1168  0.0017  302 84Z B C21 
4518 C  C21 B 84Z S  .   ? 0.2400  0.2608 0.2196  0.0431  0.0047  -0.0749 302 84Z B C21 
4519 C  C20 A 84Z S  .   ? 0.1538  0.2418 0.3150  -0.0167 -0.0010 0.0745  302 84Z B C20 
4520 C  C20 B 84Z S  .   ? 0.2630  0.2551 0.2145  0.0337  -0.0212 -0.0528 302 84Z B C20 
4521 C  C3  A 84Z S  .   ? 0.2335  0.1980 0.1865  -0.0377 0.0336  -0.1107 302 84Z B C3  
4522 C  C3  B 84Z S  .   ? 0.1102  0.1398 0.1743  -0.0012 -0.0166 -0.0324 302 84Z B C3  
4523 C  C2  A 84Z S  .   ? 0.1362  0.2418 0.1779  -0.0284 0.0596  -0.0835 302 84Z B C2  
4524 C  C2  B 84Z S  .   ? 0.1553  0.1312 0.1305  0.0100  0.0008  -0.0589 302 84Z B C2  
4525 C  C4  A 84Z S  .   ? 0.2102  0.1973 0.1574  -0.0649 0.0361  -0.0906 302 84Z B C4  
4526 C  C4  B 84Z S  .   ? 0.1474  0.1423 0.1614  0.0265  -0.0375 -0.0347 302 84Z B C4  
4527 C  C12 A 84Z S  .   ? 0.2210  0.2587 0.2195  0.0130  0.0710  -0.1465 302 84Z B C12 
4528 C  C12 B 84Z S  .   ? 0.1747  0.1581 0.1127  0.0387  0.0132  -0.0141 302 84Z B C12 
4529 O  O14 A 84Z S  .   ? 0.1639  0.2149 0.1678  -0.0352 -0.0255 -0.0418 302 84Z B O14 
4530 O  O14 B 84Z S  .   ? 0.1023  0.2084 0.2490  0.0100  -0.0134 0.0103  302 84Z B O14 
4531 C  C15 A 84Z S  .   ? 0.4386  0.4914 0.1775  0.0972  -0.0236 0.1254  302 84Z B C15 
4532 C  C15 B 84Z S  .   ? 0.1134  0.2568 0.2052  0.0807  -0.0350 -0.0100 302 84Z B C15 
4533 O  O13 A 84Z S  .   ? 0.3007  0.2927 0.2977  -0.0201 0.0828  0.0502  302 84Z B O13 
4534 O  O13 B 84Z S  .   ? 0.2059  0.2194 0.2372  0.0506  -0.0468 -0.0431 302 84Z B O13 
4535 C  C5  A 84Z S  .   ? 0.2117  0.2285 0.1111  -0.0525 0.0378  -0.0462 302 84Z B C5  
4536 C  C5  B 84Z S  .   ? 0.1155  0.1062 0.1506  0.0018  -0.0598 -0.0419 302 84Z B C5  
4537 C  C6  A 84Z S  .   ? 0.1312  0.1840 0.1470  -0.0263 0.0378  -0.0387 302 84Z B C6  
4538 C  C6  B 84Z S  .   ? 0.1137  0.1003 0.1040  -0.0048 -0.0304 -0.0196 302 84Z B C6  
4539 C  C1  A 84Z S  .   ? 0.1682  0.1912 0.0998  0.0245  0.0452  -0.0060 302 84Z B C1  
4540 C  C1  B 84Z S  .   ? 0.0775  0.1420 0.1137  -0.0098 -0.0125 -0.0038 302 84Z B C1  
4541 CL CL1 A 84Z S  .   ? 0.1513  0.2640 0.1696  0.0047  0.0259  -0.0209 302 84Z B CL1 
4542 CL CL1 B 84Z S  .   ? 0.1242  0.1230 0.1136  -0.0091 -0.0084 -0.0394 302 84Z B CL1 
4543 S  S7  A 84Z S  .   ? 0.1005  0.1441 0.1181  -0.0098 0.0064  -0.0239 302 84Z B S7  
4544 S  S7  B 84Z S  .   ? 0.0937  0.1380 0.1301  -0.0113 0.0019  -0.0345 302 84Z B S7  
4545 O  O8  A 84Z S  .   ? 0.0829  0.1538 0.1398  0.0048  -0.0310 -0.0087 302 84Z B O8  
4546 O  O8  B 84Z S  .   ? 0.1100  0.1517 0.1398  0.0141  0.0135  -0.0452 302 84Z B O8  
4547 O  O9  A 84Z S  .   ? 0.0768  0.1772 0.1506  -0.0231 0.0038  -0.0443 302 84Z B O9  
4548 O  O9  B 84Z S  .   ? 0.1206  0.1294 0.1294  -0.0227 0.0099  -0.0370 302 84Z B O9  
4549 N  N10 A 84Z S  .   ? 0.0662  0.1782 0.1337  0.0165  0.0176  -0.0772 302 84Z B N10 
4550 N  N10 B 84Z S  .   ? 0.1156  0.1312 0.1549  -0.0190 -0.0223 0.0087  302 84Z B N10 
4551 C  C1  . PEG T  .   ? 0.2687  0.3837 0.2781  0.0928  -0.0604 -0.0401 303 PEG B C1  
4552 O  O1  . PEG T  .   ? 0.4321  0.2662 0.2346  0.0869  -0.1350 -0.1076 303 PEG B O1  
4553 C  C2  . PEG T  .   ? 0.2176  0.4487 0.4977  0.0131  0.0092  -0.1646 303 PEG B C2  
4554 O  O2  . PEG T  .   ? 0.4569  0.2981 0.4063  0.0836  -0.0490 -0.1900 303 PEG B O2  
4555 C  C3  . PEG T  .   ? 0.4972  0.5171 0.6971  -0.1167 0.1169  -0.1782 303 PEG B C3  
4556 C  C4  . PEG T  .   ? 0.3894  0.4763 0.1761  -0.0450 -0.0381 -0.0646 303 PEG B C4  
4557 O  O4  . PEG T  .   ? 0.8803  2.5207 0.3200  -0.0921 0.2130  0.0022  303 PEG B O4  
4558 C  C1  . EDO U  .   ? 0.3438  0.2318 0.1973  0.0347  -0.0391 -0.0042 304 EDO B C1  
4559 O  O1  . EDO U  .   ? 0.4019  0.1894 0.1641  0.1008  -0.0446 -0.0419 304 EDO B O1  
4560 C  C2  . EDO U  .   ? 0.7167  0.2196 0.3383  -0.0639 -0.2217 -0.0067 304 EDO B C2  
4561 O  O2  . EDO U  .   ? 0.3776  0.2497 0.2372  -0.0315 -0.0041 -0.0015 304 EDO B O2  
4562 C  C   . ACT V  .   ? 0.2877  0.3912 0.3273  -0.0477 0.0856  0.0241  305 ACT B C   
4563 O  O   . ACT V  .   ? 0.3225  0.5994 0.3876  -0.0842 -0.0688 0.0625  305 ACT B O   
4564 O  OXT . ACT V  .   ? 0.3050  0.3172 0.2673  -0.0657 0.0262  0.0730  305 ACT B OXT 
4565 C  CH3 . ACT V  .   ? 0.2443  0.2436 0.1923  0.0355  0.0239  -0.0870 305 ACT B CH3 
4566 C  C1  . PEG W  .   ? 1.7251  0.5698 0.5988  -0.0401 -0.1132 0.1077  306 PEG B C1  
4567 O  O1  . PEG W  .   ? 1.0240  1.3949 0.3746  -0.3720 -0.0239 0.5446  306 PEG B O1  
4568 C  C2  . PEG W  .   ? 1.7931  0.5434 1.0966  -0.0540 -0.1988 -0.0201 306 PEG B C2  
4569 O  O2  . PEG W  .   ? 1.1941  1.1401 0.4784  0.2008  -0.1195 0.0380  306 PEG B O2  
4570 C  C3  . PEG W  .   ? 1.7015  0.3146 0.3862  0.0972  0.0661  0.0894  306 PEG B C3  
4571 C  C4  . PEG W  .   ? 0.3161  0.8749 0.8222  0.2431  0.0380  0.2302  306 PEG B C4  
4572 O  O4  . PEG W  .   ? 0.6563  0.8212 0.5880  0.1324  0.0666  0.1241  306 PEG B O4  
4573 C  C1  . PEG X  .   ? 0.3362  0.3383 0.2906  0.0059  0.0151  -0.1280 307 PEG B C1  
4574 O  O1  . PEG X  .   ? 0.3132  0.2382 0.2451  -0.0405 -0.0190 0.0215  307 PEG B O1  
4575 C  C2  . PEG X  .   ? 0.3602  0.4069 0.5516  0.0062  0.0009  -0.0592 307 PEG B C2  
4576 O  O2  . PEG X  .   ? 0.6866  0.5545 0.6168  -0.0114 -0.2672 -0.0886 307 PEG B O2  
4577 C  C3  . PEG X  .   ? 1.1346  0.5619 0.8288  0.1105  0.0214  -0.1241 307 PEG B C3  
4578 C  C4  . PEG X  .   ? 0.5838  0.5109 0.7198  -0.1297 0.1511  -0.1341 307 PEG B C4  
4579 O  O4  . PEG X  .   ? 0.6861  0.5475 0.4063  0.1274  -0.2121 -0.0293 307 PEG B O4  
4580 C  C1  . PEG Y  .   ? 0.3546  0.2285 0.7230  0.0002  0.1125  -0.0209 308 PEG B C1  
4581 O  O1  . PEG Y  .   ? 0.2224  0.2730 0.2867  0.0380  -0.0267 -0.0197 308 PEG B O1  
4582 C  C2  . PEG Y  .   ? 0.2655  0.3286 0.5121  0.0619  -0.1069 -0.0580 308 PEG B C2  
4583 O  O2  . PEG Y  .   ? 0.6761  0.7082 0.6323  -0.0434 0.0049  -0.1553 308 PEG B O2  
4584 C  C3  . PEG Y  .   ? 0.4627  0.5863 0.5842  0.0875  -0.3357 0.0536  308 PEG B C3  
4585 C  C4  . PEG Y  .   ? 0.2540  0.3664 0.2630  0.0068  -0.0291 -0.0333 308 PEG B C4  
4586 O  O4  . PEG Y  .   ? 0.2127  0.3567 0.2791  -0.0183 -0.0100 0.0568  308 PEG B O4  
4587 C  C1  . PEG Z  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  309 PEG B C1  
4588 O  O1  . PEG Z  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  309 PEG B O1  
4589 C  C2  . PEG Z  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  309 PEG B C2  
4590 O  O2  . PEG Z  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  309 PEG B O2  
4591 C  C3  . PEG Z  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  309 PEG B C3  
4592 C  C4  . PEG Z  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  309 PEG B C4  
4593 O  O4  . PEG Z  .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  309 PEG B O4  
4594 C  C1  . PEG AA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG B C1  
4595 O  O1  . PEG AA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG B O1  
4596 C  C2  . PEG AA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG B C2  
4597 O  O2  . PEG AA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG B O2  
4598 C  C3  . PEG AA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG B C3  
4599 C  C4  . PEG AA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG B C4  
4600 O  O4  . PEG AA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  310 PEG B O4  
4601 C  C1  . EDO BA .   ? 0.5413  0.4875 0.4819  -0.1599 0.0142  0.0397  311 EDO B C1  
4602 O  O1  . EDO BA .   ? 0.5939  0.6127 0.8018  0.1410  -0.0388 0.0356  311 EDO B O1  
4603 C  C2  . EDO BA .   ? 0.3096  0.2647 0.3973  -0.0051 0.0184  0.1148  311 EDO B C2  
4604 O  O2  . EDO BA .   ? 0.4163  0.3776 0.3334  0.0375  0.0409  0.0748  311 EDO B O2  
4605 C  C1  . EDO CA .   ? 0.7198  0.3067 0.6041  0.0627  0.0234  -0.0790 312 EDO B C1  
4606 O  O1  . EDO CA .   ? 0.5291  0.5898 0.4112  0.0219  0.1012  -0.1570 312 EDO B O1  
4607 C  C2  . EDO CA .   ? 0.7551  0.7386 0.3707  -0.0983 -0.0911 -0.1434 312 EDO B C2  
4608 O  O2  . EDO CA .   ? 0.6000  0.3254 1.0413  0.0754  -0.0320 0.1022  312 EDO B O2  
4609 C  C1  . EDO DA .   ? 0.2820  0.3771 0.3186  -0.0091 -0.0438 0.0701  313 EDO B C1  
4610 O  O1  . EDO DA .   ? 0.2301  0.3018 0.2748  -0.0009 -0.0314 -0.0162 313 EDO B O1  
4611 C  C2  . EDO DA .   ? 0.4605  0.4329 0.2964  -0.0261 -0.0271 -0.0348 313 EDO B C2  
4612 O  O2  . EDO DA .   ? 0.4569  0.4735 0.4699  -0.0204 -0.0183 -0.0712 313 EDO B O2  
4613 C  C1  . EDO EA .   ? 0.4486  0.4744 0.4878  -0.0532 0.0168  0.0858  314 EDO B C1  
4614 O  O1  . EDO EA .   ? 0.4156  0.4803 0.5256  0.0536  -0.0345 0.0160  314 EDO B O1  
4615 C  C2  . EDO EA .   ? 0.3865  0.3621 0.3692  -0.0105 -0.0061 0.0166  314 EDO B C2  
4616 O  O2  . EDO EA .   ? 0.3358  0.4016 0.4062  0.0554  -0.0190 -0.0165 314 EDO B O2  
4617 C  C1  . EDO FA .   ? 0.2856  0.2648 0.2177  0.0206  0.0497  -0.0185 315 EDO B C1  
4618 O  O1  . EDO FA .   ? 0.2939  0.2625 0.2407  0.0189  0.0309  -0.0143 315 EDO B O1  
4619 C  C2  . EDO FA .   ? 0.3337  0.3413 0.3237  -0.0226 -0.0410 0.0195  315 EDO B C2  
4620 O  O2  . EDO FA .   ? 0.3204  0.3431 0.3186  0.0189  0.0052  0.0025  315 EDO B O2  
4621 C  C1  . EDO GA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  316 EDO B C1  
4622 O  O1  . EDO GA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  316 EDO B O1  
4623 C  C2  . EDO GA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  316 EDO B C2  
4624 O  O2  . EDO GA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  316 EDO B O2  
4625 C  C1  . EDO HA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  317 EDO B C1  
4626 O  O1  . EDO HA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  317 EDO B O1  
4627 C  C2  . EDO HA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  317 EDO B C2  
4628 O  O2  . EDO HA .   ? 0.2533  0.2533 0.2533  0.0000  0.0000  0.0000  317 EDO B O2  
4629 O  O   . HOH IA .   ? 0.1966  0.2662 0.2773  0.0163  0.0000  0.0110  401 HOH A O   
4630 O  O   . HOH IA .   ? 0.5778  0.4533 0.3746  -0.0236 0.0514  0.0066  402 HOH A O   
4631 O  O   . HOH IA .   ? 0.4616  0.3441 0.3036  -0.1395 -0.1064 0.0394  403 HOH A O   
4632 O  O   . HOH IA .   ? 0.5076  0.3280 0.6583  -0.0353 -0.1544 0.0956  404 HOH A O   
4633 O  O   . HOH IA .   ? 0.2935  0.1524 0.2924  0.0094  0.0195  -0.0511 405 HOH A O   
4634 O  O   . HOH IA .   ? 0.2727  0.2637 0.4016  0.0027  -0.0534 -0.0374 406 HOH A O   
4635 O  O   . HOH IA .   ? 0.6912  0.2885 0.5281  -0.0044 0.3924  -0.0699 407 HOH A O   
4636 O  O   . HOH IA .   ? 0.3412  1.0542 0.2436  0.0020  0.0252  -0.0089 408 HOH A O   
4637 O  O   . HOH IA .   ? 0.3492  0.3643 0.4483  -0.1277 -0.0143 0.0682  409 HOH A O   
4638 O  O   . HOH IA .   ? 0.2618  0.2127 0.1840  -0.0366 -0.0557 0.0607  410 HOH A O   
4639 O  O   . HOH IA .   ? 0.4016  0.5516 4.9295  -0.3050 0.2986  -0.4339 411 HOH A O   
4640 O  O   . HOH IA .   ? 0.7361  0.4077 0.3294  0.2654  -0.0452 -0.0961 412 HOH A O   
4641 O  O   . HOH IA .   ? 0.4454  0.7296 0.3503  0.0204  -0.0365 0.0971  413 HOH A O   
4642 O  O   . HOH IA .   ? 0.6422  0.4282 0.3096  -0.1175 0.1174  -0.0414 414 HOH A O   
4643 O  O   . HOH IA .   ? 0.2206  0.2113 0.1720  0.0147  -0.0255 -0.0221 415 HOH A O   
4644 O  O   . HOH IA .   ? 0.5253  0.5134 0.1919  -0.0553 0.0556  0.1351  416 HOH A O   
4645 O  O   . HOH IA .   ? 0.3183  0.3582 0.3570  0.0531  0.1114  0.1541  417 HOH A O   
4646 O  O   . HOH IA .   ? 0.5686  0.4602 0.4533  0.0748  -0.0263 -0.2461 418 HOH A O   
4647 O  O   . HOH IA .   ? 0.2942  0.8390 0.4070  0.0222  0.0854  -0.2500 419 HOH A O   
4648 O  O   . HOH IA .   ? 0.5037  0.4232 0.4995  0.1449  -0.1715 -0.0185 420 HOH A O   
4649 O  O   . HOH IA .   ? 0.2762  0.4329 0.1588  0.0447  -0.0168 -0.0328 421 HOH A O   
4650 O  O   . HOH IA .   ? 0.4213  0.6545 0.3018  -0.1159 -0.0226 -0.1639 422 HOH A O   
4651 O  O   . HOH IA .   ? 0.5320  0.5146 0.2228  -0.1499 0.0873  -0.0446 423 HOH A O   
4652 O  O   . HOH IA .   ? 0.4454  0.6494 0.3739  0.1835  -0.0913 -0.0002 424 HOH A O   
4653 O  O   . HOH IA .   ? 0.7124  0.3697 0.4002  -0.0034 -0.0681 0.0563  425 HOH A O   
4654 O  O   . HOH IA .   ? 0.1499  0.1162 0.1883  -0.0286 0.0203  0.0024  426 HOH A O   
4655 O  O   . HOH IA .   ? 0.2246  0.2073 0.1689  -0.0357 -0.0413 0.0241  427 HOH A O   
4656 O  O   . HOH IA .   ? 0.4408  0.3883 0.7065  -0.0983 -0.0312 0.1787  428 HOH A O   
4657 O  O   . HOH IA .   ? 0.4187  0.6144 0.3262  0.1759  -0.0436 0.0729  429 HOH A O   
4658 O  O   . HOH IA .   ? 0.3761  0.2672 0.2260  0.0209  0.0647  -0.0271 430 HOH A O   
4659 O  O   . HOH IA .   ? 0.1289  0.1553 0.1147  0.0009  -0.0212 -0.0030 431 HOH A O   
4660 O  O   . HOH IA .   ? 0.2117  0.2716 0.2327  -0.0477 -0.0715 0.0208  432 HOH A O   
4661 O  O   . HOH IA .   ? 0.5151  0.1865 0.1826  0.0891  0.1096  0.0199  433 HOH A O   
4662 O  O   . HOH IA .   ? 0.2740  0.2335 0.2942  0.0324  0.0109  0.0396  434 HOH A O   
4663 O  O   . HOH IA .   ? 0.5826  0.6376 0.2213  -0.1354 -0.0703 0.0697  435 HOH A O   
4664 O  O   . HOH IA .   ? 0.5371  0.5105 0.3434  0.2357  0.0243  -0.0659 436 HOH A O   
4665 O  O   . HOH IA .   ? 0.3535  0.3650 0.3208  -0.0143 0.0167  0.0790  437 HOH A O   
4666 O  O   . HOH IA .   ? 0.6153  0.1998 0.5262  0.1300  -0.2726 -0.0568 438 HOH A O   
4667 O  O   . HOH IA .   ? 0.3736  0.2913 0.2845  0.0157  -0.1698 -0.0337 439 HOH A O   
4668 O  O   . HOH IA .   ? 0.4483  0.3538 0.4296  -0.1658 0.0065  -0.0876 440 HOH A O   
4669 O  O   . HOH IA .   ? 0.2608  0.3388 0.3822  0.0816  -0.1118 -0.0535 441 HOH A O   
4670 O  O   . HOH IA .   ? 0.5497  0.4583 0.6849  0.1556  0.3231  0.0065  442 HOH A O   
4671 O  O   . HOH IA .   ? 0.3079  0.2794 0.5934  0.0423  0.0297  -0.0930 443 HOH A O   
4672 O  O   . HOH IA .   ? 0.2005  0.4449 0.2213  0.0550  0.0125  -0.0331 444 HOH A O   
4673 O  O   . HOH IA .   ? 0.2547  0.2495 0.3237  0.0644  -0.0766 -0.0837 445 HOH A O   
4674 O  O   . HOH IA .   ? 0.3495  0.2303 0.2906  -0.0387 -0.0150 -0.0173 446 HOH A O   
4675 O  O   . HOH IA .   ? 0.3614  0.4947 0.9031  -0.0397 -0.1488 0.1596  447 HOH A O   
4676 O  O   . HOH IA .   ? 0.5870  0.4846 0.6569  0.0037  0.2035  0.0080  448 HOH A O   
4677 O  O   . HOH IA .   ? 0.3819  0.2906 0.2777  -0.0254 0.0231  -0.0299 449 HOH A O   
4678 O  O   . HOH IA .   ? 0.2860  0.1890 0.1641  0.0627  0.0163  0.0126  450 HOH A O   
4679 O  O   . HOH IA .   ? 1.3030  0.3750 0.7722  0.0358  0.6118  -0.0283 451 HOH A O   
4680 O  O   . HOH IA .   ? 0.2518  0.2910 0.6197  0.0385  -0.1531 -0.0686 452 HOH A O   
4681 O  O   . HOH IA .   ? 0.4282  0.3488 1.1016  -0.0239 -0.1979 -0.0611 453 HOH A O   
4682 O  O   . HOH IA .   ? 0.6533  0.6544 0.2845  0.1667  -0.1430 -0.1251 454 HOH A O   
4683 O  O   . HOH IA .   ? 0.6444  0.5585 0.4864  -0.0156 0.0289  -0.2491 455 HOH A O   
4684 O  O   . HOH IA .   ? 0.3093  1.0609 0.3262  0.1021  0.0339  0.2816  456 HOH A O   
4685 O  O   . HOH IA .   ? 0.4706  0.5465 0.6118  0.3027  -0.2218 -0.1522 457 HOH A O   
4686 O  O   . HOH IA .   ? 0.1495  0.1822 0.3668  0.0210  0.0248  0.0069  458 HOH A O   
4687 O  O   . HOH IA .   ? 0.2030  0.3406 0.1951  0.0623  0.0631  0.0812  459 HOH A O   
4688 O  O   . HOH IA .   ? 0.5235  0.6713 0.2081  -0.2183 0.0398  0.0596  460 HOH A O   
4689 O  O   . HOH IA .   ? 0.5581  0.5256 0.4421  0.2265  0.0227  0.0482  461 HOH A O   
4690 O  O   . HOH IA .   ? 0.2522  0.3836 0.2791  -0.0833 -0.0306 0.1439  462 HOH A O   
4691 O  O   . HOH IA .   ? 0.2511  0.2185 0.2982  -0.0198 0.0422  0.0474  463 HOH A O   
4692 O  O   . HOH IA .   ? 0.4345  0.2364 0.2967  0.0070  0.0590  -0.0577 464 HOH A O   
4693 O  O   . HOH IA .   ? 0.5059  0.3962 0.4709  -0.1040 0.1958  -0.1507 465 HOH A O   
4694 O  O   . HOH IA .   ? 0.3564  0.3926 0.3858  0.1745  0.0815  -0.0769 466 HOH A O   
4695 O  O   . HOH IA .   ? 0.2694  0.2618 0.6592  0.0581  0.0110  0.0659  467 HOH A O   
4696 O  O   . HOH IA .   ? 0.4199  0.2874 0.6312  0.0563  0.1280  -0.0199 468 HOH A O   
4697 O  O   . HOH IA .   ? 0.3743  0.3919 0.4505  0.1980  0.0595  0.1232  469 HOH A O   
4698 O  O   . HOH IA .   ? 0.4467  0.2508 0.2168  -0.1353 -0.0925 0.0168  470 HOH A O   
4699 O  O   . HOH IA .   ? 0.3380  0.3043 0.5289  -0.1249 -0.0489 0.0120  471 HOH A O   
4700 O  O   . HOH IA .   ? 0.4001  1.0369 0.4939  -0.1218 -0.0024 -0.3596 472 HOH A O   
4701 O  O   . HOH IA .   ? 0.7594  1.7875 0.6028  -0.3278 -0.0726 0.5432  473 HOH A O   
4702 O  O   . HOH IA .   ? 0.4892  0.8383 0.3506  0.3845  0.0181  0.0129  474 HOH A O   
4703 O  O   . HOH IA .   ? 0.2726  0.3297 0.2781  0.0227  0.0572  -0.0006 475 HOH A O   
4704 O  O   . HOH IA .   ? 0.2169  0.2550 0.2107  -0.0143 -0.0351 -0.0089 476 HOH A O   
4705 O  O   . HOH IA .   ? 0.7504  0.7521 0.3804  -0.1013 -0.1296 -0.0933 477 HOH A O   
4706 O  O   . HOH IA .   ? 0.2328  0.3327 0.3365  0.0043  0.0221  -0.0455 478 HOH A O   
4707 O  O   . HOH IA .   ? 0.2177  0.1128 0.1908  0.0270  0.0403  0.0125  479 HOH A O   
4708 O  O   . HOH IA .   ? 0.1120  0.2037 0.1391  0.0176  0.0211  0.0335  480 HOH A O   
4709 O  O   . HOH IA .   ? 0.1427  0.1232 0.1030  0.0110  -0.0380 0.0062  481 HOH A O   
4710 O  O   . HOH IA .   ? 0.2170  0.3607 0.2521  0.0877  -0.0488 -0.1575 482 HOH A O   
4711 O  O   . HOH IA .   ? 0.2540  0.1969 0.2102  0.0194  -0.0063 -0.0234 483 HOH A O   
4712 O  O   . HOH IA .   ? 0.2495  0.2296 0.5141  0.0298  -0.0994 -0.0262 484 HOH A O   
4713 O  O   . HOH IA .   ? 0.1301  0.2529 0.1671  0.0010  -0.0396 -0.0208 485 HOH A O   
4714 O  O   . HOH IA .   ? 0.1865  0.1492 0.2712  0.0329  0.0035  0.0189  486 HOH A O   
4715 O  O   . HOH IA .   ? 0.1271  0.1492 0.1258  -0.0278 -0.0124 -0.0089 487 HOH A O   
4716 O  O   . HOH IA .   ? 0.3595  0.3334 0.5838  0.1559  0.1771  0.0372  488 HOH A O   
4717 O  O   . HOH IA .   ? 0.1973  0.1427 0.2698  -0.0358 0.0500  -0.0179 489 HOH A O   
4718 O  O   . HOH IA .   ? 0.1786  0.2611 0.1298  0.0074  -0.0234 -0.0312 490 HOH A O   
4719 O  O   . HOH IA .   ? 0.2454  0.2529 0.2605  0.0040  -0.0403 -0.0670 491 HOH A O   
4720 O  O   . HOH IA .   ? 0.1190  0.1434 0.1427  0.0000  -0.0241 -0.0079 492 HOH A O   
4721 O  O   . HOH IA .   ? 0.1958  0.4853 0.3699  0.0545  0.0857  -0.0054 493 HOH A O   
4722 O  O   . HOH IA .   ? 0.3592  0.2168 0.3635  -0.1086 0.0317  -0.0385 494 HOH A O   
4723 O  O   . HOH IA .   ? 0.5254  0.6096 0.3032  -0.0047 -0.1295 0.0370  495 HOH A O   
4724 O  O   . HOH IA .   ? 0.3060  0.2759 0.1829  -0.0035 0.0197  0.0607  496 HOH A O   
4725 O  O   . HOH IA .   ? 0.3222  0.3815 0.1944  -0.0325 -0.0126 0.0835  497 HOH A O   
4726 O  O   . HOH IA .   ? 0.4345  0.3233 0.5330  0.0408  0.2071  0.2703  498 HOH A O   
4727 O  O   . HOH IA .   ? 0.2217  0.7453 0.5256  -0.0359 -0.0479 -0.1507 499 HOH A O   
4728 O  O   . HOH IA .   ? 0.3139  0.2465 0.1905  0.0313  0.0141  -0.0729 500 HOH A O   
4729 O  O   . HOH IA .   ? 0.2569  0.2497 0.3513  0.0225  -0.0585 0.0107  501 HOH A O   
4730 O  O   . HOH IA .   ? 0.3050  0.4027 0.2034  -0.0634 -0.0134 0.0688  502 HOH A O   
4731 O  O   . HOH IA .   ? 0.2411  0.3355 0.2196  -0.0408 -0.0033 0.0844  503 HOH A O   
4732 O  O   . HOH IA .   ? 0.4112  0.2892 0.1775  -0.0409 -0.0693 0.0198  504 HOH A O   
4733 O  O   . HOH IA .   ? 0.1075  0.1520 0.0900  -0.0006 -0.0212 -0.0061 505 HOH A O   
4734 O  O   . HOH IA .   ? 0.7217  0.2927 0.6691  -0.0557 -0.0575 0.1872  506 HOH A O   
4735 O  O   . HOH IA .   ? 0.2418  0.2644 0.2210  0.0160  -0.0713 0.0660  507 HOH A O   
4736 O  O   . HOH IA .   ? 0.3808  0.7016 0.4656  0.0704  -0.1212 -0.0911 508 HOH A O   
4737 O  O   . HOH IA .   ? 0.1657  0.2343 0.1696  0.0436  -0.0242 -0.0243 509 HOH A O   
4738 O  O   . HOH IA .   ? 0.2974  0.2134 0.3603  -0.0049 0.0443  -0.0200 510 HOH A O   
4739 O  O   . HOH IA .   ? 0.1116  0.2256 0.1080  -0.0093 0.0010  -0.0139 511 HOH A O   
4740 O  O   . HOH IA .   ? 0.2451  0.3646 0.3146  0.0231  -0.1123 0.0507  512 HOH A O   
4741 O  O   . HOH IA .   ? 0.2113  0.1804 0.2213  0.0334  -0.0373 0.0410  513 HOH A O   
4742 O  O   . HOH IA .   ? 0.3649  0.5725 0.4252  -0.2369 0.1054  -0.0895 514 HOH A O   
4743 O  O   . HOH IA .   ? 0.4002  0.2848 0.4102  0.0247  -0.1944 0.0111  515 HOH A O   
4744 O  O   . HOH IA .   ? 0.1833  0.1483 0.1817  -0.0081 -0.0365 -0.0114 516 HOH A O   
4745 O  O   . HOH IA .   ? 0.3758  0.1664 0.1951  -0.0042 -0.0900 0.0194  517 HOH A O   
4746 O  O   . HOH IA .   ? 0.2547  0.4313 0.4176  -0.0432 0.1699  -0.0574 518 HOH A O   
4747 O  O   . HOH IA .   ? 0.2240  0.2469 0.2002  0.0693  -0.0445 0.0082  519 HOH A O   
4748 O  O   . HOH IA .   ? 0.4374  0.3291 0.5589  0.0204  -0.1703 -0.0839 520 HOH A O   
4749 O  O   . HOH IA .   ? 0.3801  0.2758 0.3280  0.0898  -0.0326 0.0044  521 HOH A O   
4750 O  O   . HOH IA .   ? 0.3926  0.6026 0.6335  -0.0326 -0.0980 -0.2466 522 HOH A O   
4751 O  O   . HOH IA .   ? 0.2687  0.3509 0.1991  -0.0655 -0.0162 0.1038  523 HOH A O   
4752 O  O   . HOH IA .   ? 0.1445  0.1120 0.1606  -0.0140 -0.0108 0.0044  524 HOH A O   
4753 O  O   . HOH IA .   ? 0.5716  0.2949 0.2547  0.1297  -0.1568 -0.0856 525 HOH A O   
4754 O  O   . HOH IA .   ? 0.1062  0.2289 0.1058  -0.0104 0.0134  0.0050  526 HOH A O   
4755 O  O   . HOH IA .   ? 0.1574  0.1294 0.1524  -0.0128 -0.0072 -0.0021 527 HOH A O   
4756 O  O   . HOH IA .   ? 0.3485  0.4992 0.2910  -0.0747 0.0620  0.0316  528 HOH A O   
4757 O  O   . HOH IA .   ? 0.2766  0.2055 0.3606  -0.0197 -0.1036 0.0238  529 HOH A O   
4758 O  O   . HOH IA .   ? 0.3646  0.2734 0.2267  -0.0294 -0.0192 0.1116  530 HOH A O   
4759 O  O   . HOH IA .   ? 0.2213  0.1391 0.2985  -0.0159 -0.0414 -0.0129 531 HOH A O   
4760 O  O   . HOH IA .   ? 0.5598  0.5378 0.3370  -0.0113 0.0709  -0.1685 532 HOH A O   
4761 O  O   . HOH IA .   ? 0.2097  0.2260 0.2518  -0.0784 0.0340  0.0119  533 HOH A O   
4762 O  O   . HOH IA .   ? 0.1671  0.3862 0.1635  -0.0008 0.0205  -0.0179 534 HOH A O   
4763 O  O   . HOH IA .   ? 0.1897  0.1641 0.1588  0.0100  0.0147  0.0178  535 HOH A O   
4764 O  O   . HOH IA .   ? 0.2888  0.2037 0.2508  -0.0739 -0.0277 -0.0674 536 HOH A O   
4765 O  O   . HOH IA .   ? 0.2041  0.1747 0.1750  0.0063  0.0142  0.0064  537 HOH A O   
4766 O  O   . HOH IA .   ? 0.4598  0.5123 0.8805  0.1613  -0.3543 -0.0542 538 HOH A O   
4767 O  O   . HOH IA .   ? 0.3258  0.3880 0.3057  0.0449  0.0048  -0.0012 539 HOH A O   
4768 O  O   . HOH IA .   ? 0.6104  0.3114 0.6863  0.0607  0.0572  0.2240  540 HOH A O   
4769 O  O   . HOH IA .   ? 0.3639  0.3219 0.2701  0.0818  -0.1393 -0.0610 541 HOH A O   
4770 O  O   . HOH IA .   ? 0.3449  0.2594 0.3416  -0.0767 0.1421  -0.0617 542 HOH A O   
4771 O  O   . HOH IA .   ? 0.7559  0.4449 0.5662  0.0789  -0.1383 -0.2456 543 HOH A O   
4772 O  O   . HOH IA .   ? 0.1678  0.2579 0.2352  0.0088  -0.0584 -0.0928 544 HOH A O   
4773 O  O   . HOH IA .   ? 0.2224  0.2407 0.2308  -0.0015 -0.0267 0.0119  545 HOH A O   
4774 O  O   . HOH IA .   ? 0.2145  0.3258 0.6311  0.0513  0.0082  0.0704  546 HOH A O   
4775 O  O   . HOH IA .   ? 0.5940  0.5441 0.6282  -0.2251 0.1594  -0.0546 547 HOH A O   
4776 O  O   . HOH IA .   ? 0.3340  0.4270 0.4882  -0.0354 0.1185  -0.0827 548 HOH A O   
4777 O  O   . HOH IA .   ? 0.1377  0.1405 0.1574  -0.0216 0.0040  0.0238  549 HOH A O   
4778 O  O   . HOH IA .   ? 0.1116  0.1208 0.0847  -0.0046 -0.0298 -0.0071 550 HOH A O   
4779 O  O   . HOH IA .   ? 0.2231  0.2030 0.2669  0.0256  0.0242  0.0030  551 HOH A O   
4780 O  O   . HOH IA .   ? 0.3082  0.3388 0.5434  -0.1641 0.2394  -0.2343 552 HOH A O   
4781 O  O   . HOH IA .   ? 0.3330  0.2813 0.2975  0.0578  0.0489  0.1439  553 HOH A O   
4782 O  O   . HOH IA .   ? 0.1951  0.2565 0.2411  0.0694  0.0700  0.0001  554 HOH A O   
4783 O  O   . HOH IA .   ? 0.2971  0.2102 0.5607  -0.0306 -0.0745 0.0108  555 HOH A O   
4784 O  O   . HOH IA .   ? 0.3028  0.2788 0.1861  -0.0420 0.0792  -0.0179 556 HOH A O   
4785 O  O   . HOH IA .   ? 0.4972  0.7232 0.4543  -0.1981 0.0010  0.0802  557 HOH A O   
4786 O  O   . HOH IA .   ? 0.1380  0.1951 0.1102  0.0006  -0.0274 0.0004  558 HOH A O   
4787 O  O   . HOH IA .   ? 0.1797  0.2034 0.1621  -0.0017 -0.0022 -0.0142 559 HOH A O   
4788 O  O   . HOH IA .   ? 0.4954  0.3309 0.3114  -0.0575 0.0772  -0.1762 560 HOH A O   
4789 O  O   . HOH IA .   ? 0.1639  0.1815 0.2996  0.0230  -0.0757 -0.0640 561 HOH A O   
4790 O  O   . HOH IA .   ? 0.1483  0.1800 0.1905  -0.0001 -0.0098 0.0040  562 HOH A O   
4791 O  O   . HOH IA .   ? 0.1459  0.2554 0.2020  0.0106  -0.0293 0.0348  563 HOH A O   
4792 O  O   . HOH IA .   ? 0.2572  0.3147 0.1588  0.0220  0.0006  -0.0008 564 HOH A O   
4793 O  O   . HOH IA .   ? 0.2458  0.2091 0.2648  0.0214  0.0245  0.0195  565 HOH A O   
4794 O  O   . HOH IA .   ? 0.3560  0.2630 0.1858  -0.1199 0.0160  -0.0436 566 HOH A O   
4795 O  O   . HOH IA .   ? 0.3276  0.2206 0.8041  -0.0326 -0.0779 0.2074  567 HOH A O   
4796 O  O   . HOH IA .   ? 0.2770  0.5678 0.5852  0.0688  0.0293  0.1741  568 HOH A O   
4797 O  O   . HOH IA .   ? 0.2221  0.1368 0.2055  -0.0095 -0.0179 -0.0282 569 HOH A O   
4798 O  O   . HOH IA .   ? 0.1307  0.1703 0.1544  -0.0069 -0.0172 0.0035  570 HOH A O   
4799 O  O   . HOH IA .   ? 0.1287  0.1811 0.1098  0.0140  -0.0225 -0.0143 571 HOH A O   
4800 O  O   . HOH IA .   ? 0.1544  0.2188 0.1488  0.0068  -0.0269 0.0122  572 HOH A O   
4801 O  O   . HOH IA .   ? 0.2177  0.1897 0.1808  -0.0434 0.0208  0.0195  573 HOH A O   
4802 O  O   . HOH IA .   ? 0.3265  0.2561 0.2469  0.0128  0.0424  -0.0806 574 HOH A O   
4803 O  O   . HOH IA .   ? 0.5080  0.7409 0.2181  0.2971  0.1089  0.1332  575 HOH A O   
4804 O  O   . HOH IA .   ? 0.4133  0.2508 0.2949  -0.0542 0.0782  0.0183  576 HOH A O   
4805 O  O   . HOH IA .   ? 0.1420  0.2020 0.1326  -0.0026 -0.0342 -0.0218 577 HOH A O   
4806 O  O   . HOH IA .   ? 0.2899  0.1883 0.1248  -0.0833 -0.0237 -0.0269 578 HOH A O   
4807 O  O   . HOH IA .   ? 0.1263  0.1477 0.1876  0.0077  -0.0151 0.0222  579 HOH A O   
4808 O  O   . HOH IA .   ? 0.2228  0.5101 0.2551  -0.0882 0.0178  0.0779  580 HOH A O   
4809 O  O   . HOH IA .   ? 0.3248  0.2278 0.3815  -0.0921 -0.1094 0.0365  581 HOH A O   
4810 O  O   . HOH IA .   ? 0.3431  0.2816 0.2773  0.0187  0.0275  0.1093  582 HOH A O   
4811 O  O   . HOH IA .   ? 0.1894  0.2224 0.1914  0.0027  0.0165  0.0573  583 HOH A O   
4812 O  O   . HOH IA .   ? 0.3617  0.4397 0.2396  0.0456  0.0431  -0.1222 584 HOH A O   
4813 O  O   . HOH IA .   ? 0.2953  0.2594 0.3305  -0.0210 0.1535  -0.0342 585 HOH A O   
4814 O  O   . HOH IA .   ? 0.6373  0.3491 0.4539  -0.0165 0.1088  0.0496  586 HOH A O   
4815 O  O   . HOH IA .   ? 0.2231  0.1914 0.2442  -0.0486 -0.0190 -0.0033 587 HOH A O   
4816 O  O   . HOH IA .   ? 0.3517  0.2293 0.3474  -0.0623 -0.0980 0.1363  588 HOH A O   
4817 O  O   . HOH IA .   ? 0.5283  0.7821 0.7403  0.0772  0.2117  -0.3630 589 HOH A O   
4818 O  O   . HOH IA .   ? 0.6605  0.3118 0.5598  -0.0974 -0.0362 -0.0502 590 HOH A O   
4819 O  O   . HOH IA .   ? 0.4727  0.7068 0.7061  -0.0895 0.2626  -0.4487 591 HOH A O   
4820 O  O   . HOH IA .   ? 0.4411  0.1793 0.3125  -0.0058 0.0687  -0.0385 592 HOH A O   
4821 O  O   . HOH IA .   ? 0.3912  0.3905 0.7346  -0.1307 -0.0574 0.0954  593 HOH A O   
4822 O  O   . HOH IA .   ? 0.5722  0.4776 0.5543  0.1969  -0.1835 -0.0185 594 HOH A O   
4823 O  O   . HOH IA .   ? 0.3948  0.4016 0.2343  -0.1270 0.0083  -0.0864 595 HOH A O   
4824 O  O   . HOH IA .   ? 0.2601  0.3905 0.4586  0.1087  -0.1011 -0.1436 596 HOH A O   
4825 O  O   . HOH IA .   ? 0.3021  0.5026 0.2978  -0.1821 -0.0912 0.0544  597 HOH A O   
4826 O  O   . HOH IA .   ? 0.4526  0.2337 0.1840  0.1614  0.0055  0.0373  598 HOH A O   
4827 O  O   . HOH IA .   ? 0.4311  0.2400 0.1678  0.0538  -0.0785 0.0364  599 HOH A O   
4828 O  O   . HOH IA .   ? 0.2870  0.3000 0.4577  0.0287  0.0794  -0.0105 600 HOH A O   
4829 O  O   . HOH IA .   ? 0.1368  0.1199 0.1185  -0.0074 -0.0100 -0.0229 601 HOH A O   
4830 O  O   . HOH IA .   ? 0.4336  0.3176 0.4759  0.0709  0.1917  -0.0274 602 HOH A O   
4831 O  O   . HOH IA .   ? 0.3186  0.3211 0.2185  0.0460  -0.1180 -0.0549 603 HOH A O   
4832 O  O   . HOH IA .   ? 0.1639  0.2891 0.8244  -0.0322 0.0945  0.1447  604 HOH A O   
4833 O  O   . HOH IA .   ? 0.4885  0.6660 0.8825  0.2092  0.0553  0.4791  605 HOH A O   
4834 O  O   . HOH IA .   ? 0.3100  0.2597 0.4467  0.0563  -0.0121 -0.0089 606 HOH A O   
4835 O  O   . HOH IA .   ? 0.2354  0.2447 0.2380  0.0330  -0.0209 0.0132  607 HOH A O   
4836 O  O   . HOH IA .   ? 0.2465  0.2533 0.2084  0.1134  -0.0309 -0.0515 608 HOH A O   
4837 O  O   . HOH IA .   ? 0.8693  0.4681 0.5483  -0.1958 -0.2579 -0.1711 609 HOH A O   
4838 O  O   . HOH IA .   ? 0.2676  0.4935 0.2156  0.0623  -0.0001 0.0022  610 HOH A O   
4839 O  O   . HOH IA .   ? 0.2310  0.1833 0.1869  -0.0027 0.0031  0.0529  611 HOH A O   
4840 O  O   . HOH IA .   ? 0.4546  0.2138 0.4532  0.0607  -0.2951 -0.1171 612 HOH A O   
4841 O  O   . HOH IA .   ? 0.2002  0.1851 0.1872  -0.0199 0.0070  -0.0017 613 HOH A O   
4842 O  O   . HOH IA .   ? 0.2045  0.1240 0.1725  0.0346  0.0170  0.0209  614 HOH A O   
4843 O  O   . HOH IA .   ? 0.1764  0.2332 0.1962  -0.0257 -0.0003 0.0209  615 HOH A O   
4844 O  O   . HOH IA .   ? 0.3061  0.2874 0.3175  0.0328  0.0608  -0.0031 616 HOH A O   
4845 O  O   . HOH IA .   ? 0.3977  0.2820 0.2199  0.0758  0.0805  -0.0040 617 HOH A O   
4846 O  O   . HOH IA .   ? 0.2684  0.5101 0.3133  0.2112  0.0564  0.0549  618 HOH A O   
4847 O  O   . HOH IA .   ? 0.1125  0.1208 0.2143  -0.0088 -0.0432 0.0190  619 HOH A O   
4848 O  O   . HOH IA .   ? 0.1951  0.1571 0.2870  0.0089  -0.0066 -0.0880 620 HOH A O   
4849 O  O   . HOH IA .   ? 0.2204  0.3036 0.1671  -0.0103 -0.0024 0.0164  621 HOH A O   
4850 O  O   . HOH IA .   ? 0.3822  0.5774 0.5143  0.0064  0.0063  0.0895  622 HOH A O   
4851 O  O   . HOH IA .   ? 0.3783  0.6864 0.4749  0.0890  -0.0234 0.3966  623 HOH A O   
4852 O  O   . HOH IA .   ? 0.2433  0.2467 0.2795  0.0428  -0.0989 -0.0281 624 HOH A O   
4853 O  O   . HOH IA .   ? 0.4537  0.4519 0.4352  0.0120  -0.0409 -0.0242 625 HOH A O   
4854 O  O   . HOH IA .   ? 0.2321  0.4431 0.3689  -0.1810 0.0171  -0.0201 626 HOH A O   
4855 O  O   . HOH IA .   ? 0.1603  0.2504 0.1560  0.0267  -0.0168 -0.0205 627 HOH A O   
4856 O  O   . HOH IA .   ? 0.2314  0.5254 0.4217  0.0422  0.0207  -0.2330 628 HOH A O   
4857 O  O   . HOH IA .   ? 0.2953  0.2041 0.4300  -0.0080 -0.1072 -0.0738 629 HOH A O   
4858 O  O   . HOH IA .   ? 0.2077  0.2597 0.3661  0.0963  -0.0558 -0.0989 630 HOH A O   
4859 O  O   . HOH IA .   ? 0.2798  0.3754 0.2902  0.0194  -0.0337 0.0223  631 HOH A O   
4860 O  O   . HOH IA .   ? 0.4245  0.6375 0.2622  0.2342  -0.0658 -0.0500 632 HOH A O   
4861 O  O   . HOH IA .   ? 0.2127  0.2293 0.2002  0.0476  0.0305  -0.0604 633 HOH A O   
4862 O  O   . HOH IA .   ? 0.6860  0.5248 0.2903  -0.0564 -0.1805 -0.0162 634 HOH A O   
4863 O  O   . HOH IA .   ? 0.3951  0.5464 0.5409  0.1764  0.1547  0.2801  635 HOH A O   
4864 O  O   . HOH IA .   ? 0.3230  0.4379 0.6674  0.1025  -0.0577 -0.0531 636 HOH A O   
4865 O  O   . HOH IA .   ? 0.3947  0.5868 0.4925  0.2471  0.1849  0.3107  637 HOH A O   
4866 O  O   . HOH IA .   ? 0.3854  0.3050 0.2314  0.0187  -0.0336 -0.0322 638 HOH A O   
4867 O  O   . HOH IA .   ? 0.3689  0.2946 0.4609  -0.0011 0.0462  0.0414  639 HOH A O   
4868 O  O   . HOH IA .   ? 0.1509  0.4791 0.2310  0.0813  0.0033  0.0110  640 HOH A O   
4869 O  O   . HOH IA .   ? 0.3079  0.2235 0.2630  0.0236  0.0983  0.0034  641 HOH A O   
4870 O  O   . HOH IA .   ? 0.3776  0.3524 0.2748  -0.0541 0.0351  0.0133  642 HOH A O   
4871 O  O   . HOH IA .   ? 0.1448  0.1441 0.1914  -0.0074 -0.0122 0.0057  643 HOH A O   
4872 O  O   . HOH IA .   ? 0.6566  2.3881 0.9545  -0.5407 0.2421  -0.4891 644 HOH A O   
4873 O  O   . HOH IA .   ? 0.4641  0.4591 0.6412  -0.0996 -0.2178 -0.1059 645 HOH A O   
4874 O  O   . HOH IA .   ? 0.4680  0.4982 0.4235  0.0810  0.1470  0.0549  646 HOH A O   
4875 O  O   . HOH IA .   ? 0.5098  0.4119 0.3172  -0.0640 0.1403  0.1663  647 HOH A O   
4876 O  O   . HOH IA .   ? 0.4314  0.2773 0.5177  -0.0702 0.1046  0.0163  648 HOH A O   
4877 O  O   . HOH IA .   ? 0.2802  0.5315 0.4630  0.0011  0.0751  0.0568  649 HOH A O   
4878 O  O   . HOH IA .   ? 0.2910  0.2357 0.3887  -0.0237 -0.0125 0.0440  650 HOH A O   
4879 O  O   . HOH IA .   ? 0.2293  0.3862 0.2842  -0.1676 -0.0469 0.1239  651 HOH A O   
4880 O  O   . HOH IA .   ? 0.3722  0.3125 0.1628  -0.1516 -0.0460 0.0351  652 HOH A O   
4881 O  O   . HOH IA .   ? 0.3304  0.3876 0.5072  -0.1088 0.1709  -0.2725 653 HOH A O   
4882 O  O   . HOH IA .   ? 0.5559  0.4602 0.5335  -0.1761 -0.1148 -0.0776 654 HOH A O   
4883 O  O   . HOH IA .   ? 0.2676  0.4652 0.5781  0.0053  0.0675  0.1395  655 HOH A O   
4884 O  O   . HOH IA .   ? 0.1811  0.1671 0.2260  -0.0195 0.0152  -0.0152 656 HOH A O   
4885 O  O   . HOH IA .   ? 0.2495  0.3176 0.2561  0.0536  0.0105  -0.0487 657 HOH A O   
4886 O  O   . HOH IA .   ? 0.4038  0.3287 0.5647  0.0869  0.0267  -0.1885 658 HOH A O   
4887 O  O   . HOH IA .   ? 0.3230  0.2608 0.2691  -0.0392 0.1118  -0.0718 659 HOH A O   
4888 O  O   . HOH IA .   ? 0.3097  0.7560 0.2508  -0.1729 0.0011  0.0731  660 HOH A O   
4889 O  O   . HOH IA .   ? 0.2127  0.4117 0.4860  -0.0471 -0.0156 -0.0833 661 HOH A O   
4890 O  O   . HOH IA .   ? 0.6135  0.4719 0.8144  -0.2538 0.3614  0.0144  662 HOH A O   
4891 O  O   . HOH IA .   ? 0.7085  0.2469 0.1463  -0.1175 -0.1306 0.0531  663 HOH A O   
4892 O  O   . HOH IA .   ? 0.4817  0.7847 0.5334  0.1729  0.0147  -0.0506 664 HOH A O   
4893 O  O   . HOH IA .   ? 0.5879  0.5602 0.7149  0.1732  -0.1080 0.0446  665 HOH A O   
4894 O  O   . HOH IA .   ? 0.4403  0.2579 0.9804  0.0167  -0.3691 0.0399  666 HOH A O   
4895 O  O   . HOH IA .   ? 0.5283  0.2751 0.5023  0.0657  -0.2600 -0.0384 667 HOH A O   
4896 O  O   . HOH IA .   ? 0.2418  0.4209 0.5403  0.0150  -0.0441 0.1261  668 HOH A O   
4897 O  O   . HOH IA .   ? 0.2020  0.2353 0.2791  -0.0147 -0.0060 0.0336  669 HOH A O   
4898 O  O   . HOH IA .   ? 0.2623  0.2963 0.4097  0.0576  -0.1148 0.0397  670 HOH A O   
4899 O  O   . HOH IA .   ? 0.3905  0.5205 0.7550  0.1304  -0.2758 -0.0705 671 HOH A O   
4900 O  O   . HOH IA .   ? 0.2866  0.5975 0.3373  0.0458  -0.0245 -0.0917 672 HOH A O   
4901 O  O   . HOH IA .   ? 0.4250  0.4095 0.3818  0.1659  -0.0295 0.0147  673 HOH A O   
4902 O  O   . HOH IA .   ? 0.4620  0.2787 0.3193  -0.0917 -0.1741 -0.0128 674 HOH A O   
4903 O  O   . HOH IA .   ? 0.1366  0.2127 0.1232  0.0270  -0.0158 -0.0117 675 HOH A O   
4904 O  O   . HOH IA .   ? 0.5665  0.6829 0.4745  -0.0179 -0.1985 0.1040  676 HOH A O   
4905 O  O   . HOH IA .   ? 0.2982  0.5026 0.3035  -0.0705 0.0058  0.0293  677 HOH A O   
4906 O  O   . HOH IA .   ? 0.3431  0.3010 0.1840  0.0917  0.0149  -0.0135 678 HOH A O   
4907 O  O   . HOH IA .   ? 0.3251  0.4638 0.2285  -0.0779 -0.0229 -0.0298 679 HOH A O   
4908 O  O   . HOH IA .   ? 0.5305  0.6238 0.7066  -0.0466 -0.3396 0.0607  680 HOH A O   
4909 O  O   . HOH IA .   ? 0.5270  0.3498 0.5204  -0.1307 -0.0436 0.1101  681 HOH A O   
4910 O  O   . HOH IA .   ? 0.4407  0.2363 0.8563  -0.0032 -0.0990 0.0190  682 HOH A O   
4911 O  O   . HOH IA .   ? 0.5404  0.4745 0.4947  -0.0581 0.0767  0.1485  683 HOH A O   
4912 O  O   . HOH IA .   ? 0.3075  0.2841 0.1872  0.0186  -0.0457 -0.0307 684 HOH A O   
4913 O  O   . HOH IA .   ? 1.3369  0.3592 0.4767  -0.0876 0.3298  -0.1456 685 HOH A O   
4914 O  O   . HOH IA .   ? 0.7876  0.5602 0.3441  0.2434  0.1455  0.1910  686 HOH A O   
4915 O  O   . HOH IA .   ? 0.4975  0.6918 0.4489  -0.1032 -0.2025 -0.0035 687 HOH A O   
4916 O  O   . HOH IA .   ? 0.3495  0.3596 0.9488  -0.0088 -0.0622 -0.2137 688 HOH A O   
4917 O  O   . HOH IA .   ? 0.5248  0.7192 0.9111  0.0616  -0.2708 -0.4386 689 HOH A O   
4918 O  O   . HOH IA .   ? 0.3847  0.7834 0.5679  0.1669  -0.1219 -0.2787 690 HOH A O   
4919 O  O   . HOH IA .   ? 0.2784  0.4273 0.5732  0.1148  -0.0725 0.0269  691 HOH A O   
4920 O  O   . HOH IA .   ? 0.2052  0.2745 0.1966  -0.0263 -0.0015 0.0093  692 HOH A O   
4921 O  O   . HOH IA .   ? 0.2213  0.2034 0.1366  -0.0409 0.0231  -0.0367 693 HOH A O   
4922 O  O   . HOH IA .   ? 0.4518  0.2461 0.4597  -0.0380 -0.1562 0.0269  694 HOH A O   
4923 O  O   . HOH IA .   ? 0.2546  0.7318 0.5510  0.0754  0.0341  -0.2719 695 HOH A O   
4924 O  O   . HOH IA .   ? 0.3808  0.4810 0.4476  -0.1266 0.0365  0.0748  696 HOH A O   
4925 O  O   . HOH IA .   ? 0.5564  0.3596 0.8506  -0.0456 -0.3158 0.1772  697 HOH A O   
4926 O  O   . HOH IA .   ? 0.1696  0.2465 0.1890  -0.0060 -0.0076 -0.0089 698 HOH A O   
4927 O  O   . HOH IA .   ? 0.5126  0.5572 0.5352  0.1115  0.0797  -0.1160 699 HOH A O   
4928 O  O   . HOH IA .   ? 0.3236  0.4049 0.3556  -0.0966 -0.0447 0.0614  700 HOH A O   
4929 O  O   . HOH IA .   ? 0.6929  0.2935 0.2809  -0.0416 -0.0458 -0.0796 701 HOH A O   
4930 O  O   . HOH IA .   ? 0.4623  0.4727 0.3039  -0.0333 -0.0375 0.0758  702 HOH A O   
4931 O  O   . HOH IA .   ? 0.3613  0.4742 0.4450  0.1395  0.0066  0.0034  703 HOH A O   
4932 O  O   . HOH IA .   ? 0.4119  0.5770 0.6710  -0.1247 -0.0932 0.0635  704 HOH A O   
4933 O  O   . HOH IA .   ? 0.2619  0.2203 0.2935  0.0267  -0.0379 -0.0244 705 HOH A O   
4934 O  O   . HOH IA .   ? 0.4662  0.3208 0.2931  0.0376  -0.0619 -0.0673 706 HOH A O   
4935 O  O   . HOH IA .   ? 0.5111  0.3837 0.3018  0.0302  0.1087  0.0122  707 HOH A O   
4936 O  O   . HOH IA .   ? 0.5768  0.3887 0.4268  -0.0832 -0.1883 0.0138  708 HOH A O   
4937 O  O   . HOH IA .   ? 0.4662  0.5450 0.2952  -0.0221 -0.2147 -0.0195 709 HOH A O   
4938 O  O   . HOH IA .   ? 0.2740  1.1512 0.2081  -0.1327 -0.0129 -0.0809 710 HOH A O   
4939 O  O   . HOH IA .   ? 0.5780  0.5070 0.3764  0.1016  -0.0286 0.1263  711 HOH A O   
4940 O  O   . HOH IA .   ? 0.6095  0.5394 0.8838  0.1071  0.2621  -0.0337 712 HOH A O   
4941 O  O   . HOH IA .   ? 0.5930  0.5406 0.4431  -0.0447 0.1365  -0.2263 713 HOH A O   
4942 O  O   . HOH IA .   ? 0.1337  0.3427 0.1220  0.0148  -0.0003 -0.0466 714 HOH A O   
4943 O  O   . HOH IA .   ? 0.5917  0.7773 0.3836  0.0417  0.1534  0.0399  715 HOH A O   
4944 O  O   . HOH IA .   ? 0.3750  1.5516 0.9764  -0.0590 0.0225  0.5532  716 HOH A O   
4945 O  O   . HOH IA .   ? 0.2842  0.7238 0.7993  -0.0084 0.2406  -0.0897 717 HOH A O   
4946 O  O   . HOH IA .   ? 0.5170  0.4070 0.6042  -0.0784 0.1815  0.0398  718 HOH A O   
4947 O  O   . HOH IA .   ? 0.4489  0.6005 0.5121  0.1713  -0.0174 -0.0757 719 HOH A O   
4948 O  O   . HOH IA .   ? 0.2109  0.1483 0.1761  -0.0093 -0.0001 -0.0456 720 HOH A O   
4949 O  O   . HOH IA .   ? 0.2590  0.3262 0.5061  -0.0822 -0.0029 -0.0619 721 HOH A O   
4950 O  O   . HOH IA .   ? 0.8541  0.2874 0.6843  0.2509  -0.2308 0.0759  722 HOH A O   
4951 O  O   . HOH IA .   ? 0.4801  0.6763 0.4339  -0.0350 0.0306  0.1609  723 HOH A O   
4952 O  O   . HOH IA .   ? 0.3861  0.5924 0.4088  -0.1295 0.0749  -0.0641 724 HOH A O   
4953 O  O   . HOH IA .   ? 0.3926  0.3251 0.7368  0.0897  -0.1342 -0.2503 725 HOH A O   
4954 O  O   . HOH IA .   ? 0.2497  0.5080 0.2117  0.1124  0.0092  0.1254  726 HOH A O   
4955 O  O   . HOH IA .   ? 0.2702  0.2694 0.2860  -0.0525 -0.0031 -0.0017 727 HOH A O   
4956 O  O   . HOH IA .   ? 0.7928  0.7311 0.2619  -0.0771 -0.1005 -0.1186 728 HOH A O   
4957 O  O   . HOH IA .   ? 0.3682  0.3761 0.3653  -0.0078 0.0278  -0.0631 729 HOH A O   
4958 O  O   . HOH IA .   ? 0.5497  0.3125 0.4307  -0.0771 0.0273  0.1622  730 HOH A O   
4959 O  O   . HOH IA .   ? 0.6188  0.4176 0.5414  -0.1648 0.1216  -0.1773 731 HOH A O   
4960 O  O   . HOH IA .   ? 0.5675  0.4309 0.5360  0.0455  -0.0184 0.1467  732 HOH A O   
4961 O  O   . HOH IA .   ? 0.4232  0.6021 0.3237  -0.0306 -0.0741 0.0834  733 HOH A O   
4962 O  O   . HOH IA .   ? 0.3826  0.3578 0.3327  0.0987  0.0328  0.1206  734 HOH A O   
4963 O  O   . HOH IA .   ? 0.3031  0.3219 0.2526  -0.0201 -0.0157 0.0516  735 HOH A O   
4964 O  O   . HOH IA .   ? 0.5031  0.4238 0.8332  0.0696  -0.0748 -0.0504 736 HOH A O   
4965 O  O   . HOH IA .   ? 1.1454  0.2228 0.5422  0.1661  0.1509  0.0413  737 HOH A O   
4966 O  O   . HOH IA .   ? 0.5583  0.8855 0.2910  0.3709  0.1350  0.1120  738 HOH A O   
4967 O  O   . HOH IA .   ? 0.6222  0.2996 0.2809  0.1661  -0.0770 0.0216  739 HOH A O   
4968 O  O   . HOH IA .   ? 0.3190  0.9027 0.3309  0.0885  0.0822  0.1726  740 HOH A O   
4969 O  O   . HOH IA .   ? 0.3603  0.4597 0.5242  -0.0628 -0.1057 0.2194  741 HOH A O   
4970 O  O   . HOH IA .   ? 0.5774  0.5321 0.6215  0.0403  -0.0144 -0.0513 742 HOH A O   
4971 O  O   . HOH IA .   ? 0.1808  0.3437 0.2296  -0.0313 -0.0179 0.0227  743 HOH A O   
4972 O  O   . HOH IA .   ? 0.1732  0.2163 0.1822  0.0089  0.0124  0.0103  744 HOH A O   
4973 O  O   . HOH IA .   ? 0.3334  0.6454 0.5030  -0.0967 0.0325  -0.1615 745 HOH A O   
4974 O  O   . HOH IA .   ? 0.2504  0.4363 0.6655  0.0809  -0.2092 -0.1844 746 HOH A O   
4975 O  O   . HOH IA .   ? 0.6888  0.2791 0.4595  -0.1121 -0.0329 -0.0403 747 HOH A O   
4976 O  O   . HOH IA .   ? 0.4936  0.5575 0.7944  0.0863  -0.2154 0.1910  748 HOH A O   
4977 O  O   . HOH IA .   ? 0.4845  0.7754 0.6236  0.3407  -0.2922 -0.3565 749 HOH A O   
4978 O  O   . HOH IA .   ? 0.4446  0.6218 0.5123  0.0420  -0.0274 0.1948  750 HOH A O   
4979 O  O   . HOH IA .   ? 0.2353  0.4684 0.2525  0.1190  0.0457  0.0394  751 HOH A O   
4980 O  O   . HOH IA .   ? 0.2081  0.3445 0.2812  -0.0348 0.0359  -0.1363 752 HOH A O   
4981 O  O   . HOH IA .   ? 0.2680  0.5594 0.3125  -0.0222 0.0754  0.0057  753 HOH A O   
4982 O  O   . HOH IA .   ? 0.4386  0.2091 0.2256  -0.0314 -0.0846 -0.0461 754 HOH A O   
4983 O  O   . HOH IA .   ? 0.8075  0.4102 0.5776  -0.0836 0.1010  -0.1891 755 HOH A O   
4984 O  O   . HOH IA .   ? 0.4352  0.6796 0.5273  -0.2698 -0.1377 0.0882  756 HOH A O   
4985 O  O   . HOH IA .   ? 0.6339  0.4485 0.4063  -0.0555 0.0763  0.0126  757 HOH A O   
4986 O  O   . HOH IA .   ? 0.5972  0.4365 0.6156  -0.2035 0.0256  0.0686  758 HOH A O   
4987 O  O   . HOH IA .   ? 0.5264  0.7828 0.4830  0.0176  -0.0477 0.0449  759 HOH A O   
4988 O  O   . HOH IA .   ? 0.2579  0.4505 0.6066  -0.0834 0.1738  -0.1177 760 HOH A O   
4989 O  O   . HOH IA .   ? 0.5088  0.5208 0.6880  0.0480  -0.3055 0.0623  761 HOH A O   
4990 O  O   . HOH IA .   ? 0.3775  0.5268 0.3714  0.2592  -0.0252 -0.1184 762 HOH A O   
4991 O  O   . HOH IA .   ? 0.2127  0.3718 0.2601  0.0100  -0.0055 0.0534  763 HOH A O   
4992 O  O   . HOH IA .   ? 0.5064  0.4194 0.5267  0.0432  -0.1388 0.0594  764 HOH A O   
4993 O  O   . HOH IA .   ? 0.2759  0.3190 0.3481  -0.0055 0.0675  0.0769  765 HOH A O   
4994 O  O   . HOH IA .   ? 0.3711  0.8278 0.5186  -0.0197 0.0905  -0.1558 766 HOH A O   
4995 O  O   . HOH IA .   ? 0.3495  0.9163 0.3596  -0.3040 0.0929  -0.0541 767 HOH A O   
4996 O  O   . HOH IA .   ? 0.4317  0.3886 0.4210  0.0610  -0.1652 -0.1291 768 HOH A O   
4997 O  O   . HOH IA .   ? 0.7618  0.2860 0.6153  -0.0302 -0.0473 0.0813  769 HOH A O   
4998 O  O   . HOH IA .   ? 0.5288  0.3951 0.4063  -0.0223 0.1670  0.0468  770 HOH A O   
4999 O  O   . HOH IA .   ? 0.5613  0.4548 0.9951  0.1698  0.0190  -0.1159 771 HOH A O   
5000 O  O   . HOH IA .   ? 0.7632  0.7745 0.5290  0.2868  -0.1674 0.0651  772 HOH A O   
5001 O  O   . HOH IA .   ? 0.6988  0.6880 0.5631  0.0366  -0.0665 0.0097  773 HOH A O   
5002 O  O   . HOH IA .   ? 0.6212  0.5131 0.5965  -0.1372 0.0282  0.1239  774 HOH A O   
5003 O  O   . HOH IA .   ? 0.3524  0.5680 0.5626  0.0324  0.0408  -0.0421 775 HOH A O   
5004 O  O   . HOH IA .   ? 0.6534  0.2831 0.4838  0.0839  -0.1961 -0.0096 776 HOH A O   
5005 O  O   . HOH IA .   ? 0.7652  0.7073 0.4541  0.0085  0.0615  -0.1738 777 HOH A O   
5006 O  O   . HOH IA .   ? 0.5006  0.7188 0.5802  -0.1676 0.0435  0.1031  778 HOH A O   
5007 O  O   . HOH IA .   ? 0.4250  0.7176 0.3086  0.0023  -0.0276 -0.1249 779 HOH A O   
5008 O  O   . HOH IA .   ? 0.3570  0.3431 0.4038  -0.0051 -0.0771 0.1355  780 HOH A O   
5009 O  O   . HOH IA .   ? 0.2321  0.2411 0.2544  0.0048  -0.0519 0.0150  781 HOH A O   
5010 O  O   . HOH IA .   ? 0.5916  0.9017 0.3528  -0.0105 -0.0326 0.2697  782 HOH A O   
5011 O  O   . HOH IA .   ? 0.4250  0.4564 0.6211  0.1312  -0.1081 0.0507  783 HOH A O   
5012 O  O   . HOH IA .   ? 0.4110  0.7425 0.2612  -0.0270 0.0529  -0.0142 784 HOH A O   
5013 O  O   . HOH IA .   ? 0.3244  0.2758 0.3269  0.1053  0.0110  -0.0031 785 HOH A O   
5014 O  O   . HOH IA .   ? 0.7462  0.3872 0.5156  -0.2061 0.0075  0.1506  786 HOH A O   
5015 O  O   . HOH IA .   ? 0.4929  0.6825 0.6187  0.0200  0.1518  -0.1685 787 HOH A O   
5016 O  O   . HOH IA .   ? 0.1373  0.1797 0.1502  0.0217  -0.0267 -0.0036 788 HOH A O   
5017 O  O   . HOH IA .   ? 0.8855  0.3668 0.6706  -0.1622 -0.1445 0.0829  789 HOH A O   
5018 O  O   . HOH IA .   ? 0.4361  0.4916 0.3057  -0.0741 -0.0301 -0.0580 790 HOH A O   
5019 O  O   . HOH IA .   ? 0.5958  0.7639 0.7731  0.0089  0.1492  -0.0336 791 HOH A O   
5020 O  O   . HOH IA .   ? 0.3276  0.3811 0.4970  -0.0936 -0.1620 -0.0397 792 HOH A O   
5021 O  O   . HOH IA .   ? 0.2224  0.2425 0.4361  -0.0190 0.0336  0.0244  793 HOH A O   
5022 O  O   . HOH IA .   ? 0.4253  0.4673 0.4009  0.0489  -0.0125 0.0675  794 HOH A O   
5023 O  O   . HOH IA .   ? 0.6905  0.4771 0.3423  0.2628  -0.0286 -0.0812 795 HOH A O   
5024 O  O   . HOH IA .   ? 0.2163  0.5811 0.3743  0.1048  -0.0068 0.1581  796 HOH A O   
5025 O  O   . HOH IA .   ? 0.8307  0.6116 0.4877  -0.0185 -0.0568 0.2486  797 HOH A O   
5026 O  O   . HOH IA .   ? 0.5430  0.5579 0.5276  -0.2470 -0.0144 -0.1057 798 HOH A O   
5027 O  O   . HOH IA .   ? 0.6903  0.3416 0.4839  0.0612  -0.0096 -0.0450 799 HOH A O   
5028 O  O   . HOH IA .   ? 0.2364  0.3481 0.1962  -0.0460 0.0254  0.0590  800 HOH A O   
5029 O  O   . HOH IA .   ? 0.3873  0.3657 0.4002  0.0700  0.1115  0.1212  801 HOH A O   
5030 O  O   . HOH IA .   ? 0.4189  0.2368 0.4224  0.0960  0.1591  0.0077  802 HOH A O   
5031 O  O   . HOH IA .   ? 0.2206  0.4202 0.6165  0.1190  -0.0248 -0.1157 803 HOH A O   
5032 O  O   . HOH IA .   ? 0.6636  0.4357 0.5482  -0.0597 0.0452  -0.1288 804 HOH A O   
5033 O  O   . HOH IA .   ? 0.2662  0.3602 0.3290  -0.0905 0.0282  -0.0672 805 HOH A O   
5034 O  O   . HOH IA .   ? 0.5345  0.6957 0.3499  0.2876  0.1096  0.0873  806 HOH A O   
5035 O  O   . HOH IA .   ? 0.4415  0.3449 0.7380  0.0456  -0.1744 -0.0321 807 HOH A O   
5036 O  O   . HOH IA .   ? 0.3128  0.2479 0.2586  0.0614  0.0174  -0.0487 808 HOH A O   
5037 O  O   . HOH IA .   ? 0.2469  0.2755 0.2125  0.0293  -0.0373 -0.0208 809 HOH A O   
5038 O  O   . HOH IA .   ? 0.2185  0.1617 0.5689  -0.0035 0.0018  0.0313  810 HOH A O   
5039 O  O   . HOH IA .   ? 0.3592  0.8494 0.4077  0.3328  -0.0615 -0.1603 811 HOH A O   
5040 O  O   . HOH IA .   ? 0.2544  0.2551 0.2752  0.0353  0.0005  -0.0312 812 HOH A O   
5041 O  O   . HOH IA .   ? 0.9457  0.2655 0.5102  0.0842  -0.1527 0.0741  813 HOH A O   
5042 O  O   . HOH IA .   ? 0.5313  0.6003 0.2759  -0.0468 -0.1471 0.0559  814 HOH A O   
5043 O  O   . HOH IA .   ? 0.4730  0.5200 0.2274  -0.0050 -0.0569 0.0851  815 HOH A O   
5044 O  O   . HOH IA .   ? 0.2393  0.2770 0.2917  0.0264  -0.0395 0.0016  816 HOH A O   
5045 O  O   . HOH IA .   ? 0.3819  0.4494 0.3606  0.0877  0.0345  0.1899  817 HOH A O   
5046 O  O   . HOH IA .   ? 0.7171  0.3944 0.4128  -0.1822 0.2288  -0.1169 818 HOH A O   
5047 O  O   . HOH IA .   ? 0.6024  0.2766 0.4611  -0.0982 -0.1426 0.0458  819 HOH A O   
5048 O  O   . HOH IA .   ? 0.3171  0.3923 0.3273  -0.1283 0.1004  -0.0928 820 HOH A O   
5049 O  O   . HOH IA .   ? 0.5158  0.1829 0.5240  -0.0553 0.2766  -0.0089 821 HOH A O   
5050 O  O   . HOH IA .   ? 0.4979  0.2661 0.4419  0.0125  0.0326  -0.1177 822 HOH A O   
5051 O  O   . HOH IA .   ? 0.2156  0.3970 0.2687  0.0861  -0.0370 -0.0791 823 HOH A O   
5052 O  O   . HOH IA .   ? 0.3844  0.3890 0.2989  0.0073  0.0220  -0.1268 824 HOH A O   
5053 O  O   . HOH IA .   ? 0.3987  0.4939 0.6549  -0.1324 -0.1513 0.1313  825 HOH A O   
5054 O  O   . HOH IA .   ? 0.4206  0.5842 0.3739  0.1051  0.0461  -0.0108 826 HOH A O   
5055 O  O   . HOH IA .   ? 0.3049  0.3678 0.2957  -0.0062 -0.0328 0.1047  827 HOH A O   
5056 O  O   . HOH IA .   ? 0.2073  0.4106 0.3639  0.0911  -0.0010 0.0514  828 HOH A O   
5057 O  O   . HOH IA .   ? 0.5480  0.3287 0.3696  -0.1041 -0.0709 0.1938  829 HOH A O   
5058 O  O   . HOH IA .   ? 0.3280  0.4088 0.5091  0.0092  -0.0545 0.0111  830 HOH A O   
5059 O  O   . HOH IA .   ? 0.4260  0.5029 0.5064  0.0669  -0.1553 0.0244  831 HOH A O   
5060 O  O   . HOH IA .   ? 0.2335  0.2292 0.3010  0.0254  0.0227  -0.0084 832 HOH A O   
5061 O  O   . HOH IA .   ? 0.5449  0.3643 0.7571  0.1409  0.0897  -0.1828 833 HOH A O   
5062 O  O   . HOH IA .   ? 0.4630  0.4759 0.3614  0.0805  -0.0361 0.0879  834 HOH A O   
5063 O  O   . HOH IA .   ? 0.5795  0.7281 0.5244  -0.1244 -0.1272 0.0650  835 HOH A O   
5064 O  O   . HOH IA .   ? 0.6466  0.4651 0.4952  -0.0270 -0.0763 0.0726  836 HOH A O   
5065 O  O   . HOH IA .   ? 0.7529  0.6459 0.7277  -0.1956 -0.3885 0.3975  837 HOH A O   
5066 O  O   . HOH IA .   ? 0.5799  0.3201 0.8068  -0.1027 -0.0891 0.1210  838 HOH A O   
5067 O  O   . HOH IA .   ? 0.5380  0.5256 0.6352  -0.0707 -0.0581 -0.1565 839 HOH A O   
5068 O  O   . HOH IA .   ? 0.5565  0.4712 0.6310  0.0155  0.1119  -0.2869 840 HOH A O   
5069 O  O   . HOH IA .   ? 0.1351  0.1869 0.1243  0.0209  -0.0229 -0.0011 841 HOH A O   
5070 O  O   . HOH IA .   ? 0.6009  0.6413 0.4155  0.3037  -0.0392 -0.1003 842 HOH A O   
5071 O  O   . HOH JA .   ? 0.5202  0.2177 0.1596  -0.0300 0.0392  0.0188  401 HOH B O   
5072 O  O   . HOH JA .   ? 0.6590  0.4266 0.4472  0.0691  -0.1115 0.1089  402 HOH B O   
5073 O  O   . HOH JA .   ? 0.3797  0.3797 0.3797  0.0000  0.0000  0.0000  403 HOH B O   
5074 O  O   . HOH JA .   ? 0.3025  0.2654 0.2536  0.0227  0.0650  0.0336  404 HOH B O   
5075 O  O   . HOH JA .   ? 0.4253  0.3488 0.6117  0.1701  0.0785  -0.0085 405 HOH B O   
5076 O  O   . HOH JA .   ? 0.4964  0.4321 0.3625  0.0431  0.0294  -0.0340 406 HOH B O   
5077 O  O   . HOH JA .   ? 0.7677  0.5985 0.6634  0.1284  0.1182  0.0951  407 HOH B O   
5078 O  O   . HOH JA .   ? 0.6368  0.4715 0.2702  0.0618  -0.1009 -0.0805 408 HOH B O   
5079 O  O   . HOH JA .   ? 0.4691  0.4832 0.3776  0.0149  -0.0999 -0.1000 409 HOH B O   
5080 O  O   . HOH JA .   ? 0.3779  0.5118 0.3291  -0.0019 0.0546  -0.0768 410 HOH B O   
5081 O  O   . HOH JA .   ? 0.4954  0.6728 0.4213  -0.0678 0.2108  -0.1791 411 HOH B O   
5082 O  O   . HOH JA .   ? 0.2957  0.4902 1.1337  0.0788  0.1148  0.3258  412 HOH B O   
5083 O  O   . HOH JA .   ? 0.1944  0.2260 0.2048  0.0108  -0.0713 -0.0694 413 HOH B O   
5084 O  O   . HOH JA .   ? 0.8133  0.3243 0.7755  -0.1009 0.0488  -0.1294 414 HOH B O   
5085 O  O   . HOH JA .   ? 0.5466  0.5480 0.5448  0.3012  -0.0326 0.0058  415 HOH B O   
5086 O  O   . HOH JA .   ? 0.3186  0.4350 0.2896  0.0671  -0.0886 0.0023  416 HOH B O   
5087 O  O   . HOH JA .   ? 0.3222  0.5109 0.6976  0.1317  -0.1177 -0.1157 417 HOH B O   
5088 O  O   . HOH JA .   ? 0.3750  0.1768 0.4767  0.0181  -0.0462 -0.0145 418 HOH B O   
5089 O  O   . HOH JA .   ? 0.4005  0.5285 0.4239  0.1670  -0.2002 -0.0384 419 HOH B O   
5090 O  O   . HOH JA .   ? 0.3614  0.2709 0.3513  0.1141  -0.0451 -0.0844 420 HOH B O   
5091 O  O   . HOH JA .   ? 0.5655  0.6556 0.3833  0.0348  -0.2192 0.1027  421 HOH B O   
5092 O  O   . HOH JA .   ? 0.2727  0.2734 1.0766  -0.0168 0.1465  0.0570  422 HOH B O   
5093 O  O   . HOH JA .   ? 0.5238  0.5447 0.4117  -0.1866 -0.0251 -0.0980 423 HOH B O   
5094 O  O   . HOH JA .   ? 0.6875  0.6779 0.2587  -0.2593 -0.0651 0.1275  424 HOH B O   
5095 O  O   . HOH JA .   ? 0.1743  0.2116 0.3280  -0.0270 0.0862  -0.0574 425 HOH B O   
5096 O  O   . HOH JA .   ? 0.1351  0.1628 0.1287  -0.0111 0.0018  -0.0293 426 HOH B O   
5097 O  O   . HOH JA .   ? 0.2188  0.3620 0.2860  0.0237  0.0813  -0.0335 427 HOH B O   
5098 O  O   . HOH JA .   ? 0.3222  0.4117 0.3682  -0.0575 0.0453  0.0017  428 HOH B O   
5099 O  O   . HOH JA .   ? 0.2820  0.2666 0.2141  -0.0934 -0.1129 0.0614  429 HOH B O   
5100 O  O   . HOH JA .   ? 0.3682  0.4239 0.4977  0.0151  0.0118  0.0735  430 HOH B O   
5101 O  O   . HOH JA .   ? 0.7112  0.8158 0.1887  -0.2678 -0.1086 0.0612  431 HOH B O   
5102 O  O   . HOH JA .   ? 0.5919  0.3061 0.4264  -0.1434 -0.1500 0.0602  432 HOH B O   
5103 O  O   . HOH JA .   ? 0.3728  0.5274 0.5294  -0.0576 -0.0131 -0.3033 433 HOH B O   
5104 O  O   . HOH JA .   ? 0.3883  0.3894 0.8343  0.0292  0.0120  0.1437  434 HOH B O   
5105 O  O   . HOH JA .   ? 0.3262  0.3513 0.3380  0.0862  0.1018  -0.0345 435 HOH B O   
5106 O  O   . HOH JA .   ? 0.5613  0.2982 0.4669  -0.0859 0.0004  0.0842  436 HOH B O   
5107 O  O   . HOH JA .   ? 0.2856  0.2996 0.2629  -0.0222 -0.0563 -0.0316 437 HOH B O   
5108 O  O   . HOH JA .   ? 1.0489  0.4490 0.3894  0.3403  0.0812  0.0077  438 HOH B O   
5109 O  O   . HOH JA .   ? 0.2011  0.2500 0.2278  0.0155  0.0230  -0.0342 439 HOH B O   
5110 O  O   . HOH JA .   ? 0.1495  0.2612 0.1538  0.0079  -0.0311 -0.0201 440 HOH B O   
5111 O  O   . HOH JA .   ? 0.6287  0.5346 0.5838  -0.0722 -0.0079 0.0301  441 HOH B O   
5112 O  O   . HOH JA .   ? 0.5225  0.4638 0.3793  0.1549  -0.1053 0.0047  442 HOH B O   
5113 O  O   . HOH JA .   ? 0.2339  0.2809 0.1932  -0.0319 0.0042  -0.0807 443 HOH B O   
5114 O  O   . HOH JA .   ? 0.2145  0.2906 0.3735  -0.0614 0.1361  -0.0792 444 HOH B O   
5115 O  O   . HOH JA .   ? 0.3115  0.4181 0.3747  -0.0924 0.1092  -0.1028 445 HOH B O   
5116 O  O   . HOH JA .   ? 0.2630  0.3143 0.2594  0.0608  0.0163  0.0478  446 HOH B O   
5117 O  O   . HOH JA .   ? 0.7584  0.4598 0.3740  -0.0543 0.0174  0.0164  447 HOH B O   
5118 O  O   . HOH JA .   ? 0.3811  0.3844 0.7200  -0.0707 0.1152  -0.2159 448 HOH B O   
5119 O  O   . HOH JA .   ? 0.2683  0.5360 0.3876  -0.1621 -0.0152 -0.0709 449 HOH B O   
5120 O  O   . HOH JA .   ? 0.1287  0.1301 0.1028  -0.0114 -0.0141 -0.0242 450 HOH B O   
5121 O  O   . HOH JA .   ? 0.1944  0.1804 0.1289  0.0381  -0.0250 -0.0237 451 HOH B O   
5122 O  O   . HOH JA .   ? 0.2406  0.3416 0.3369  -0.0707 0.1272  -0.1725 452 HOH B O   
5123 O  O   . HOH JA .   ? 0.1520  0.2222 0.1682  0.0160  -0.0490 -0.0043 453 HOH B O   
5124 O  O   . HOH JA .   ? 0.5406  0.5211 0.3499  0.0557  0.2494  -0.0814 454 HOH B O   
5125 O  O   . HOH JA .   ? 0.7000  0.2673 0.5125  0.0282  0.0478  0.0368  455 HOH B O   
5126 O  O   . HOH JA .   ? 0.5298  0.3521 0.1754  -0.0117 0.0005  -0.0797 456 HOH B O   
5127 O  O   . HOH JA .   ? 0.3189  0.3879 0.2565  -0.0081 0.0505  -0.0411 457 HOH B O   
5128 O  O   . HOH JA .   ? 0.1452  0.3172 0.1208  0.0238  0.0188  0.0299  458 HOH B O   
5129 O  O   . HOH JA .   ? 0.6673  0.6233 0.2884  0.0724  0.0194  -0.0995 459 HOH B O   
5130 O  O   . HOH JA .   ? 0.3538  0.5524 0.3327  -0.0027 0.1394  -0.0848 460 HOH B O   
5131 O  O   . HOH JA .   ? 0.2748  0.3613 0.1969  0.0190  -0.0444 -0.0367 461 HOH B O   
5132 O  O   . HOH JA .   ? 0.1188  0.2672 0.0943  0.0149  0.0134  -0.0364 462 HOH B O   
5133 O  O   . HOH JA .   ? 0.3545  0.4020 0.4393  -0.1662 0.1139  -0.1911 463 HOH B O   
5134 O  O   . HOH JA .   ? 0.2134  0.2195 0.2052  0.0714  -0.0341 -0.0507 464 HOH B O   
5135 O  O   . HOH JA .   ? 0.4224  0.3869 0.3348  0.0272  0.0142  -0.0976 465 HOH B O   
5136 O  O   . HOH JA .   ? 0.3215  0.2748 0.2064  -0.0230 -0.0562 -0.0630 466 HOH B O   
5137 O  O   . HOH JA .   ? 0.6551  0.3865 0.4637  -0.2424 -0.0881 -0.0456 467 HOH B O   
5138 O  O   . HOH JA .   ? 0.2300  0.5067 0.3190  -0.1058 0.0609  -0.1826 468 HOH B O   
5139 O  O   . HOH JA .   ? 0.3391  0.4396 0.8711  0.1008  -0.1186 -0.0688 469 HOH B O   
5140 O  O   . HOH JA .   ? 0.3158  0.3528 0.2307  -0.0504 0.0358  -0.0220 470 HOH B O   
5141 O  O   . HOH JA .   ? 0.5127  0.5715 0.4866  -0.0609 0.0765  -0.0738 471 HOH B O   
5142 O  O   . HOH JA .   ? 0.2224  0.2770 0.3365  -0.0696 0.0547  -0.0091 472 HOH B O   
5143 O  O   . HOH JA .   ? 0.4978  0.3743 0.2424  -0.1866 -0.0685 0.0675  473 HOH B O   
5144 O  O   . HOH JA .   ? 0.1144  0.2827 0.1937  -0.0058 -0.0015 -0.0851 474 HOH B O   
5145 O  O   . HOH JA .   ? 0.6439  0.7081 0.2985  -0.3432 0.1072  -0.1487 475 HOH B O   
5146 O  O   . HOH JA .   ? 0.3620  0.5529 0.3125  -0.1111 0.0993  -0.1243 476 HOH B O   
5147 O  O   . HOH JA .   ? 0.5901  0.2561 0.3984  -0.0212 0.0401  0.0098  477 HOH B O   
5148 O  O   . HOH JA .   ? 0.5843  1.0434 0.2247  -0.4105 0.0217  0.0766  478 HOH B O   
5149 O  O   . HOH JA .   ? 0.3893  0.3337 0.1815  0.0760  0.0039  -0.0069 479 HOH B O   
5150 O  O   . HOH JA .   ? 0.4005  0.3100 0.2727  0.0876  -0.0100 -0.0062 480 HOH B O   
5151 O  O   . HOH JA .   ? 0.2759  0.3449 0.2072  0.0849  -0.0057 -0.0367 481 HOH B O   
5152 O  O   . HOH JA .   ? 0.2687  0.4303 0.3434  0.0144  0.0315  -0.2137 482 HOH B O   
5153 O  O   . HOH JA .   ? 0.2477  0.3722 0.2267  -0.1035 0.0244  -0.1239 483 HOH B O   
5154 O  O   . HOH JA .   ? 0.2564  0.2532 0.1738  0.0199  0.0078  0.0255  484 HOH B O   
5155 O  O   . HOH JA .   ? 0.1082  0.1833 0.0900  0.0150  0.0012  -0.0088 485 HOH B O   
5156 O  O   . HOH JA .   ? 0.1366  0.1984 0.0795  0.0003  -0.0221 -0.0140 486 HOH B O   
5157 O  O   . HOH JA .   ? 0.2870  0.3413 0.3208  -0.0684 0.1219  -0.1954 487 HOH B O   
5158 O  O   . HOH JA .   ? 0.2253  0.4066 0.2009  -0.0765 0.0394  -0.1743 488 HOH B O   
5159 O  O   . HOH JA .   ? 0.3855  0.4935 0.2949  -0.0569 -0.0049 0.0707  489 HOH B O   
5160 O  O   . HOH JA .   ? 0.1729  0.2264 0.2220  0.0514  -0.0286 -0.0601 490 HOH B O   
5161 O  O   . HOH JA .   ? 0.2196  0.2102 0.2441  -0.0566 0.0927  -0.0905 491 HOH B O   
5162 O  O   . HOH JA .   ? 0.3398  0.3327 0.3585  -0.0624 0.0719  0.0774  492 HOH B O   
5163 O  O   . HOH JA .   ? 0.1738  0.2587 0.2583  -0.0527 0.0320  -0.0860 493 HOH B O   
5164 O  O   . HOH JA .   ? 0.1976  0.2011 0.2318  -0.0048 0.0479  -0.0516 494 HOH B O   
5165 O  O   . HOH JA .   ? 0.4257  0.5957 0.2185  -0.0602 -0.0659 0.1459  495 HOH B O   
5166 O  O   . HOH JA .   ? 0.4102  0.9106 0.2838  0.0934  -0.1191 -0.0489 496 HOH B O   
5167 O  O   . HOH JA .   ? 0.1858  0.2716 0.2586  -0.0124 0.0304  0.0166  497 HOH B O   
5168 O  O   . HOH JA .   ? 0.2231  0.3262 0.4943  -0.0648 0.0258  -0.0787 498 HOH B O   
5169 O  O   . HOH JA .   ? 0.5269  1.5266 0.3401  0.0646  0.0806  -0.0051 499 HOH B O   
5170 O  O   . HOH JA .   ? 0.5445  0.4595 0.6407  0.0708  -0.0685 0.0348  500 HOH B O   
5171 O  O   . HOH JA .   ? 0.3934  0.6540 0.5992  0.2496  0.0234  -0.1079 501 HOH B O   
5172 O  O   . HOH JA .   ? 0.1984  0.1865 0.1664  0.0149  0.0129  -0.0277 502 HOH B O   
5173 O  O   . HOH JA .   ? 0.1653  0.1804 0.2034  0.0064  0.0279  -0.0220 503 HOH B O   
5174 O  O   . HOH JA .   ? 0.1208  0.1562 0.0908  0.0006  -0.0124 -0.0186 504 HOH B O   
5175 O  O   . HOH JA .   ? 0.1032  0.1348 0.0750  0.0000  -0.0077 -0.0132 505 HOH B O   
5176 O  O   . HOH JA .   ? 0.2694  0.2572 0.2224  0.0268  0.0037  -0.0066 506 HOH B O   
5177 O  O   . HOH JA .   ? 0.2490  0.3754 0.2546  0.0440  0.0805  -0.0299 507 HOH B O   
5178 O  O   . HOH JA .   ? 0.2217  0.3183 0.2691  -0.0312 0.0149  -0.0587 508 HOH B O   
5179 O  O   . HOH JA .   ? 0.2479  0.4343 0.2816  -0.0140 0.0174  -0.0980 509 HOH B O   
5180 O  O   . HOH JA .   ? 0.2533  0.4548 0.2318  0.0743  0.0959  0.0399  510 HOH B O   
5181 O  O   . HOH JA .   ? 0.2346  0.2691 0.4982  -0.0164 0.1743  -0.0097 511 HOH B O   
5182 O  O   . HOH JA .   ? 0.3829  0.5478 0.5049  0.0791  0.1569  0.0353  512 HOH B O   
5183 O  O   . HOH JA .   ? 0.2388  0.4443 0.4924  -0.0534 0.1395  -0.2150 513 HOH B O   
5184 O  O   . HOH JA .   ? 0.3549  0.4102 0.3521  0.0653  -0.0374 0.0022  514 HOH B O   
5185 O  O   . HOH JA .   ? 0.2561  0.3459 0.3064  -0.0662 -0.0427 0.1178  515 HOH B O   
5186 O  O   . HOH JA .   ? 0.5526  0.4115 0.6181  0.0284  0.0440  0.1465  516 HOH B O   
5187 O  O   . HOH JA .   ? 0.5525  0.5443 0.4731  0.0842  0.1769  -0.0476 517 HOH B O   
5188 O  O   . HOH JA .   ? 0.1894  0.3021 0.2623  -0.0048 0.0132  -0.0929 518 HOH B O   
5189 O  O   . HOH JA .   ? 0.3725  0.2845 0.4002  -0.0335 0.0111  -0.0035 519 HOH B O   
5190 O  O   . HOH JA .   ? 0.3538  0.5323 0.4636  -0.0103 -0.1008 -0.0758 520 HOH B O   
5191 O  O   . HOH JA .   ? 0.3394  0.2339 0.2600  0.1227  0.0022  0.0423  521 HOH B O   
5192 O  O   . HOH JA .   ? 0.2608  0.2364 0.2781  -0.0215 -0.0143 -0.0276 522 HOH B O   
5193 O  O   . HOH JA .   ? 0.5672  0.4480 0.3610  -0.0070 0.1256  0.1018  523 HOH B O   
5194 O  O   . HOH JA .   ? 0.2310  0.2145 0.3043  -0.0538 0.0310  -0.1100 524 HOH B O   
5195 O  O   . HOH JA .   ? 0.2615  0.3074 0.2964  -0.0611 0.0577  -0.1461 525 HOH B O   
5196 O  O   . HOH JA .   ? 0.1775  0.2386 0.1599  -0.0220 0.0064  -0.0087 526 HOH B O   
5197 O  O   . HOH JA .   ? 0.2174  0.3926 0.4246  0.0621  -0.0841 -0.1116 527 HOH B O   
5198 O  O   . HOH JA .   ? 0.2393  0.1718 0.2676  0.0289  -0.0010 -0.0113 528 HOH B O   
5199 O  O   . HOH JA .   ? 0.2352  0.2185 0.3444  0.0171  -0.0142 -0.1104 529 HOH B O   
5200 O  O   . HOH JA .   ? 0.2461  0.3868 0.3491  0.0400  -0.0992 -0.0980 530 HOH B O   
5201 O  O   . HOH JA .   ? 0.1635  0.1790 0.1941  0.0013  0.0253  -0.0013 531 HOH B O   
5202 O  O   . HOH JA .   ? 0.5371  0.3581 0.4961  -0.0188 0.2577  -0.2077 532 HOH B O   
5203 O  O   . HOH JA .   ? 0.2213  0.6628 0.5536  -0.0917 -0.0750 0.0089  533 HOH B O   
5204 O  O   . HOH JA .   ? 0.2809  0.3345 0.1657  -0.0234 0.0617  -0.0696 534 HOH B O   
5205 O  O   . HOH JA .   ? 0.4031  0.4138 0.2687  -0.0203 -0.0450 -0.0267 535 HOH B O   
5206 O  O   . HOH JA .   ? 0.2587  0.1955 0.1032  -0.0147 0.0374  -0.0170 536 HOH B O   
5207 O  O   . HOH JA .   ? 0.2547  0.3017 0.3021  -0.0431 0.0390  -0.1059 537 HOH B O   
5208 O  O   . HOH JA .   ? 0.1416  0.2957 0.2406  -0.0381 -0.0149 -0.0946 538 HOH B O   
5209 O  O   . HOH JA .   ? 0.2063  0.6556 0.2784  0.1904  0.0079  -0.1708 539 HOH B O   
5210 O  O   . HOH JA .   ? 0.1229  0.1793 0.1463  0.0030  -0.0093 -0.0013 540 HOH B O   
5211 O  O   . HOH JA .   ? 0.3233  0.1919 0.1736  -0.0661 0.0902  0.0040  541 HOH B O   
5212 O  O   . HOH JA .   ? 0.2957  0.2152 0.3786  -0.0561 0.1119  -0.0586 542 HOH B O   
5213 O  O   . HOH JA .   ? 0.1592  0.2411 0.3355  0.0570  -0.0467 -0.0988 543 HOH B O   
5214 O  O   . HOH JA .   ? 0.1754  0.2504 0.1351  0.0094  -0.0471 -0.0146 544 HOH B O   
5215 O  O   . HOH JA .   ? 0.1664  0.2989 0.2134  -0.0053 0.0033  -0.1122 545 HOH B O   
5216 O  O   . HOH JA .   ? 0.2002  0.2239 0.1955  0.0383  -0.0203 -0.0200 546 HOH B O   
5217 O  O   . HOH JA .   ? 0.6379  0.5870 0.6032  -0.2351 0.0342  -0.1601 547 HOH B O   
5218 O  O   . HOH JA .   ? 0.3794  0.3290 0.4640  0.0634  -0.1082 0.1176  548 HOH B O   
5219 O  O   . HOH JA .   ? 0.1542  0.2142 0.1405  0.0035  -0.0301 -0.0354 549 HOH B O   
5220 O  O   . HOH JA .   ? 0.3067  0.5614 0.5927  -0.1488 -0.2140 0.2948  550 HOH B O   
5221 O  O   . HOH JA .   ? 0.3596  0.2350 0.2041  -0.0096 0.0679  0.0110  551 HOH B O   
5222 O  O   . HOH JA .   ? 0.3624  0.4655 0.6832  0.0960  -0.2027 -0.0110 552 HOH B O   
5223 O  O   . HOH JA .   ? 0.2576  0.4691 0.5879  -0.1282 -0.0136 -0.0301 553 HOH B O   
5224 O  O   . HOH JA .   ? 0.2648  0.3039 0.2195  0.0390  -0.0661 -0.0154 554 HOH B O   
5225 O  O   . HOH JA .   ? 0.1887  0.2102 0.1894  0.0237  0.0066  -0.0475 555 HOH B O   
5226 O  O   . HOH JA .   ? 0.2684  0.3168 0.3190  0.0046  -0.0160 -0.0812 556 HOH B O   
5227 O  O   . HOH JA .   ? 0.4562  0.4239 0.2931  0.0425  -0.0483 -0.0622 557 HOH B O   
5228 O  O   . HOH JA .   ? 0.5302  0.4217 0.7095  0.1311  0.0258  0.0234  558 HOH B O   
5229 O  O   . HOH JA .   ? 0.3481  0.3197 0.1998  -0.0168 0.0611  0.0465  559 HOH B O   
5230 O  O   . HOH JA .   ? 0.2424  0.1914 0.1955  -0.0408 -0.0222 -0.0099 560 HOH B O   
5231 O  O   . HOH JA .   ? 0.3970  0.4741 0.2863  -0.1272 -0.0257 0.0000  561 HOH B O   
5232 O  O   . HOH JA .   ? 0.1398  0.2027 0.1312  0.0042  -0.0355 -0.0243 562 HOH B O   
5233 O  O   . HOH JA .   ? 0.2601  0.1861 0.1259  0.0601  -0.0127 -0.0216 563 HOH B O   
5234 O  O   . HOH JA .   ? 0.3115  0.1761 0.3197  -0.0278 0.0219  -0.0062 564 HOH B O   
5235 O  O   . HOH JA .   ? 0.2964  0.2539 0.2705  -0.0395 -0.0703 0.0347  565 HOH B O   
5236 O  O   . HOH JA .   ? 0.2590  0.6365 0.4681  -0.2367 0.1050  -0.2044 566 HOH B O   
5237 O  O   . HOH JA .   ? 0.5881  0.6457 0.3552  -0.0629 0.0947  0.0207  567 HOH B O   
5238 O  O   . HOH JA .   ? 0.3789  0.2885 0.4292  0.0215  -0.0192 -0.1816 568 HOH B O   
5239 O  O   . HOH JA .   ? 0.2429  0.4005 0.8481  -0.0805 -0.1191 0.1408  569 HOH B O   
5240 O  O   . HOH JA .   ? 0.3449  0.5360 0.3337  -0.1228 -0.1233 0.1834  570 HOH B O   
5241 O  O   . HOH JA .   ? 0.3725  0.2447 0.3984  0.0183  -0.0763 -0.0636 571 HOH B O   
5242 O  O   . HOH JA .   ? 0.5302  0.3089 0.3122  -0.0221 -0.0206 -0.0033 572 HOH B O   
5243 O  O   . HOH JA .   ? 0.4587  0.5186 0.4217  0.0017  -0.0047 -0.2875 573 HOH B O   
5244 O  O   . HOH JA .   ? 0.2282  0.3528 0.3036  -0.0723 0.0504  -0.1052 574 HOH B O   
5245 O  O   . HOH JA .   ? 0.2143  0.2870 0.1116  -0.0220 -0.0124 -0.0095 575 HOH B O   
5246 O  O   . HOH JA .   ? 0.3391  0.2339 0.1987  0.0801  -0.0111 -0.0156 576 HOH B O   
5247 O  O   . HOH JA .   ? 0.1359  0.1254 0.1172  0.0043  0.0193  -0.0093 577 HOH B O   
5248 O  O   . HOH JA .   ? 0.4379  0.5156 0.5031  0.1958  -0.0102 -0.0500 578 HOH B O   
5249 O  O   . HOH JA .   ? 0.4551  0.2314 0.3639  -0.0373 0.1393  -0.0573 579 HOH B O   
5250 O  O   . HOH JA .   ? 0.2275  0.2178 0.2292  -0.0607 0.0593  -0.1026 580 HOH B O   
5251 O  O   . HOH JA .   ? 0.3768  0.4569 0.7110  -0.0760 0.1603  -0.0240 581 HOH B O   
5252 O  O   . HOH JA .   ? 0.2569  0.3901 0.2619  0.0146  0.0093  -0.0934 582 HOH B O   
5253 O  O   . HOH JA .   ? 0.3650  0.2271 0.1093  -0.0027 0.0097  -0.0272 583 HOH B O   
5254 O  O   . HOH JA .   ? 0.2651  0.3014 0.2424  -0.0480 0.0484  -0.1245 584 HOH B O   
5255 O  O   . HOH JA .   ? 0.2486  0.3678 0.8315  0.0543  0.0172  -0.1755 585 HOH B O   
5256 O  O   . HOH JA .   ? 0.3808  0.2759 0.2055  -0.0468 0.1386  -0.0943 586 HOH B O   
5257 O  O   . HOH JA .   ? 0.2680  0.5762 0.7009  -0.0758 -0.0151 -0.2556 587 HOH B O   
5258 O  O   . HOH JA .   ? 0.1395  0.1987 0.1815  -0.0032 -0.0183 -0.0111 588 HOH B O   
5259 O  O   . HOH JA .   ? 0.3395  0.2267 0.4141  -0.0004 0.1091  0.0124  589 HOH B O   
5260 O  O   . HOH JA .   ? 0.2830  0.3865 0.3517  0.0043  -0.1055 -0.0071 590 HOH B O   
5261 O  O   . HOH JA .   ? 0.4990  0.4875 0.5748  -0.0690 -0.0069 0.0344  591 HOH B O   
5262 O  O   . HOH JA .   ? 0.3617  0.2522 0.9062  0.0482  -0.1207 -0.1985 592 HOH B O   
5263 O  O   . HOH JA .   ? 0.3499  0.3459 0.3624  0.0839  -0.1882 -0.0708 593 HOH B O   
5264 O  O   . HOH JA .   ? 0.7201  0.6879 0.6607  -0.0601 -0.0392 0.2348  594 HOH B O   
5265 O  O   . HOH JA .   ? 0.1790  0.4523 0.2830  -0.0993 0.0372  -0.1105 595 HOH B O   
5266 O  O   . HOH JA .   ? 0.3653  0.4049 0.3538  0.0644  -0.1130 0.0346  596 HOH B O   
5267 O  O   . HOH JA .   ? 0.3722  0.3905 0.4088  -0.0037 0.1137  0.0617  597 HOH B O   
5268 O  O   . HOH JA .   ? 0.3962  0.2892 0.6326  -0.1141 0.0732  -0.0747 598 HOH B O   
5269 O  O   . HOH JA .   ? 0.6307  0.2583 0.2989  0.0132  0.0248  -0.1186 599 HOH B O   
5270 O  O   . HOH JA .   ? 0.3039  0.6302 0.3661  -0.2245 -0.0230 0.0247  600 HOH B O   
5271 O  O   . HOH JA .   ? 0.3610  0.3309 0.8065  -0.0831 0.1469  -0.1072 601 HOH B O   
5272 O  O   . HOH JA .   ? 0.6441  0.4113 0.3186  -0.0197 -0.0622 0.1046  602 HOH B O   
5273 O  O   . HOH JA .   ? 0.8182  0.3225 0.5947  0.1304  0.0851  -0.1536 603 HOH B O   
5274 O  O   . HOH JA .   ? 0.1621  0.2662 0.3194  0.0154  0.0041  -0.1233 604 HOH B O   
5275 O  O   . HOH JA .   ? 0.4706  0.4877 0.2781  -0.0501 -0.1094 0.0704  605 HOH B O   
5276 O  O   . HOH JA .   ? 0.5076  0.4957 0.6650  0.1893  -0.1359 -0.2115 606 HOH B O   
5277 O  O   . HOH JA .   ? 0.2328  0.3197 0.2648  -0.0290 0.0204  -0.1344 607 HOH B O   
5278 O  O   . HOH JA .   ? 0.1531  0.3477 0.2041  -0.0314 -0.0234 -0.0993 608 HOH B O   
5279 O  O   . HOH JA .   ? 0.1264  0.2734 0.2389  -0.0243 -0.0063 -0.1157 609 HOH B O   
5280 O  O   . HOH JA .   ? 0.4643  0.2411 0.3747  0.0898  0.0428  0.0359  610 HOH B O   
5281 O  O   . HOH JA .   ? 0.4406  0.5120 0.3934  0.0106  -0.0179 -0.0790 611 HOH B O   
5282 O  O   . HOH JA .   ? 0.1743  0.2275 0.2045  -0.0550 0.0307  -0.0640 612 HOH B O   
5283 O  O   . HOH JA .   ? 0.2697  0.2644 0.1725  -0.0611 0.0306  -0.0200 613 HOH B O   
5284 O  O   . HOH JA .   ? 0.7214  0.5526 0.3506  -0.0077 -0.2661 -0.1747 614 HOH B O   
5285 O  O   . HOH JA .   ? 0.5253  0.4235 0.4023  -0.1289 0.0305  -0.1376 615 HOH B O   
5286 O  O   . HOH JA .   ? 0.5947  0.4727 0.5399  0.1149  -0.1497 -0.0173 616 HOH B O   
5287 O  O   . HOH JA .   ? 0.1560  0.2849 0.2569  -0.0456 0.0436  -0.0670 617 HOH B O   
5288 O  O   . HOH JA .   ? 0.2149  0.2099 0.4788  0.0201  -0.0457 -0.0247 618 HOH B O   
5289 O  O   . HOH JA .   ? 0.4654  0.2587 0.4490  0.0143  -0.2338 -0.1313 619 HOH B O   
5290 O  O   . HOH JA .   ? 0.2723  0.5155 0.5140  0.1844  -0.0672 -0.0089 620 HOH B O   
5291 O  O   . HOH JA .   ? 0.2145  0.2248 0.2127  0.0105  0.0122  -0.0368 621 HOH B O   
5292 O  O   . HOH JA .   ? 0.2222  0.3815 0.1998  -0.0317 -0.0567 -0.0763 622 HOH B O   
5293 O  O   . HOH JA .   ? 0.2702  0.5439 0.5954  0.2026  -0.1120 -0.3697 623 HOH B O   
5294 O  O   . HOH JA .   ? 0.4289  0.5246 0.6157  0.1014  -0.2419 -0.2416 624 HOH B O   
5295 O  O   . HOH JA .   ? 0.4784  0.3319 0.6973  -0.0559 0.0544  -0.0163 625 HOH B O   
5296 O  O   . HOH JA .   ? 0.3323  0.3765 0.1786  0.0414  -0.0578 0.0468  626 HOH B O   
5297 O  O   . HOH JA .   ? 0.3186  0.4602 0.2454  0.0876  -0.0107 0.0339  627 HOH B O   
5298 O  O   . HOH JA .   ? 0.1216  0.1671 0.4134  0.0011  0.0053  -0.0392 628 HOH B O   
5299 O  O   . HOH JA .   ? 0.2497  0.2975 0.2892  0.0533  0.0133  -0.0798 629 HOH B O   
5300 O  O   . HOH JA .   ? 0.3244  0.2332 0.3189  -0.0677 -0.0973 0.0547  630 HOH B O   
5301 O  O   . HOH JA .   ? 0.4368  0.3804 0.2296  0.0223  -0.0422 -0.0368 631 HOH B O   
5302 O  O   . HOH JA .   ? 0.3333  0.7711 0.3607  -0.1030 0.0270  -0.1095 632 HOH B O   
5303 O  O   . HOH JA .   ? 0.3315  0.3962 0.8148  0.0985  0.0343  -0.2402 633 HOH B O   
5304 O  O   . HOH JA .   ? 0.3664  0.4806 0.3650  0.0117  0.0759  -0.2272 634 HOH B O   
5305 O  O   . HOH JA .   ? 0.2441  0.1851 0.1923  0.0590  0.0410  -0.0050 635 HOH B O   
5306 O  O   . HOH JA .   ? 0.4343  0.4762 0.5416  0.0553  0.1487  -0.1065 636 HOH B O   
5307 O  O   . HOH JA .   ? 0.2292  0.3330 0.1991  -0.0133 -0.0127 -0.0769 637 HOH B O   
5308 O  O   . HOH JA .   ? 0.1962  0.2497 0.1341  -0.0543 -0.0205 -0.0364 638 HOH B O   
5309 O  O   . HOH JA .   ? 0.4185  0.6900 0.4027  -0.0599 -0.0003 -0.2029 639 HOH B O   
5310 O  O   . HOH JA .   ? 0.2777  0.4490 0.2536  0.0639  0.0135  -0.0447 640 HOH B O   
5311 O  O   . HOH JA .   ? 0.4957  0.5942 0.3711  0.1342  -0.1810 0.0111  641 HOH B O   
5312 O  O   . HOH JA .   ? 0.4871  0.4964 0.5383  0.0343  0.0226  0.0308  642 HOH B O   
5313 O  O   . HOH JA .   ? 0.3086  0.4875 0.6332  -0.1639 -0.0710 0.1082  643 HOH B O   
5314 O  O   . HOH JA .   ? 0.4921  0.6618 0.4695  -0.1482 0.0052  0.1848  644 HOH B O   
5315 O  O   . HOH JA .   ? 0.2892  0.7705 0.7774  0.0639  -0.0369 -0.4054 645 HOH B O   
5316 O  O   . HOH JA .   ? 0.4920  0.4580 0.3620  -0.1345 0.1364  -0.1556 646 HOH B O   
5317 O  O   . HOH JA .   ? 0.3965  0.4519 0.3621  0.0034  0.0893  0.0851  647 HOH B O   
5318 O  O   . HOH JA .   ? 0.1865  0.3521 0.2852  0.0248  0.0136  -0.0873 648 HOH B O   
5319 O  O   . HOH JA .   ? 0.4171  0.2874 0.3104  0.0066  0.0392  0.0620  649 HOH B O   
5320 O  O   . HOH JA .   ? 0.2332  0.5338 0.8539  0.0696  0.0520  -0.1204 650 HOH B O   
5321 O  O   . HOH JA .   ? 0.2411  0.7318 0.8419  -0.0500 -0.0870 -0.1674 651 HOH B O   
5322 O  O   . HOH JA .   ? 0.2766  0.1998 0.5602  -0.0384 -0.1092 0.0620  652 HOH B O   
5323 O  O   . HOH JA .   ? 0.7529  0.4882 0.3811  -0.0138 -0.0564 -0.1370 653 HOH B O   
5324 O  O   . HOH JA .   ? 0.2587  0.2655 0.1326  -0.0016 -0.0004 0.0066  654 HOH B O   
5325 O  O   . HOH JA .   ? 0.6379  0.2892 0.3898  0.0447  0.2159  -0.0653 655 HOH B O   
5326 O  O   . HOH JA .   ? 0.3966  0.4278 0.2680  -0.1625 0.0647  -0.0638 656 HOH B O   
5327 O  O   . HOH JA .   ? 0.5141  0.6549 0.3761  0.0093  0.0211  -0.1296 657 HOH B O   
5328 O  O   . HOH JA .   ? 0.5676  0.2730 0.7681  -0.0829 0.1866  0.0257  658 HOH B O   
5329 O  O   . HOH JA .   ? 0.3686  0.4572 0.5335  0.0583  -0.0923 -0.0736 659 HOH B O   
5330 O  O   . HOH JA .   ? 0.7043  0.5342 0.3758  -0.1109 0.0253  0.1059  660 HOH B O   
5331 O  O   . HOH JA .   ? 0.2293  0.2845 0.2720  -0.0314 0.0656  -0.0901 661 HOH B O   
5332 O  O   . HOH JA .   ? 0.4734  0.7679 0.8004  0.0798  -0.1330 0.0281  662 HOH B O   
5333 O  O   . HOH JA .   ? 0.2788  0.7382 0.9057  0.0574  -0.0945 -0.0214 663 HOH B O   
5334 O  O   . HOH JA .   ? 0.6731  0.5195 0.2411  0.1016  0.0335  0.0313  664 HOH B O   
5335 O  O   . HOH JA .   ? 0.1908  0.4569 0.7616  0.0242  -0.0716 -0.2237 665 HOH B O   
5336 O  O   . HOH JA .   ? 0.3283  0.4579 0.5659  -0.1139 0.0074  0.1458  666 HOH B O   
5337 O  O   . HOH JA .   ? 0.6133  0.4483 0.5766  -0.1452 0.0358  0.0674  667 HOH B O   
5338 O  O   . HOH JA .   ? 0.3679  0.6727 0.6638  0.2098  -0.1580 -0.4052 668 HOH B O   
5339 O  O   . HOH JA .   ? 0.3847  0.3517 0.2321  0.0670  -0.0291 -0.1001 669 HOH B O   
5340 O  O   . HOH JA .   ? 0.4637  0.4335 0.3089  -0.0784 0.0498  -0.1173 670 HOH B O   
5341 O  O   . HOH JA .   ? 0.5802  0.4250 0.4910  0.1905  0.2422  0.1443  671 HOH B O   
5342 O  O   . HOH JA .   ? 0.2655  0.5406 0.3255  0.1021  0.0765  0.2192  672 HOH B O   
5343 O  O   . HOH JA .   ? 0.2479  0.9264 0.6707  0.0256  -0.0177 0.3890  673 HOH B O   
5344 O  O   . HOH JA .   ? 0.6310  0.7015 0.4379  -0.0869 -0.1849 0.0323  674 HOH B O   
5345 O  O   . HOH JA .   ? 0.7011  0.6260 0.5743  -0.0596 0.0040  0.0924  675 HOH B O   
5346 O  O   . HOH JA .   ? 0.2834  0.3262 0.5719  -0.0618 0.1330  -0.0414 676 HOH B O   
5347 O  O   . HOH JA .   ? 0.6099  0.4426 0.5966  0.0636  -0.0697 -0.1166 677 HOH B O   
5348 O  O   . HOH JA .   ? 0.2605  0.3595 0.2661  -0.0619 0.0731  -0.0899 678 HOH B O   
5349 O  O   . HOH JA .   ? 0.3922  0.3574 0.3132  -0.0951 0.0456  0.0364  679 HOH B O   
5350 O  O   . HOH JA .   ? 0.5948  0.5669 0.6243  0.0879  0.0402  -0.0365 680 HOH B O   
5351 O  O   . HOH JA .   ? 0.6034  0.3158 0.3657  -0.0115 -0.1267 0.0253  681 HOH B O   
5352 O  O   . HOH JA .   ? 0.4418  0.5978 0.5603  -0.0524 -0.1612 -0.0936 682 HOH B O   
5353 O  O   . HOH JA .   ? 0.4645  0.5262 0.7059  0.0643  0.2249  -0.1056 683 HOH B O   
5354 O  O   . HOH JA .   ? 0.6600  0.5862 0.4023  -0.0957 -0.1266 -0.1225 684 HOH B O   
5355 O  O   . HOH JA .   ? 0.5698  0.2533 0.5122  -0.0518 -0.2332 0.0685  685 HOH B O   
5356 O  O   . HOH JA .   ? 0.6314  0.4472 0.6963  0.0198  0.0458  -0.0630 686 HOH B O   
5357 O  O   . HOH JA .   ? 0.1937  0.2831 0.3043  0.0133  0.0322  -0.0543 687 HOH B O   
5358 O  O   . HOH JA .   ? 0.2842  0.2992 0.1671  -0.0581 0.0114  0.0136  688 HOH B O   
5359 O  O   . HOH JA .   ? 0.5679  0.3934 0.4771  -0.0456 -0.0521 -0.1030 689 HOH B O   
5360 O  O   . HOH JA .   ? 0.1162  0.3050 0.1409  -0.0005 -0.0147 0.0105  690 HOH B O   
5361 O  O   . HOH JA .   ? 0.7715  0.4896 0.4038  -0.1676 0.0206  -0.1214 691 HOH B O   
5362 O  O   . HOH JA .   ? 0.2823  1.3427 0.4597  -0.1185 0.0661  -0.1220 692 HOH B O   
5363 O  O   . HOH JA .   ? 0.4146  0.4242 0.5973  -0.0350 -0.1485 0.1292  693 HOH B O   
5364 O  O   . HOH JA .   ? 0.3786  0.2719 0.3725  -0.0079 0.0212  -0.0461 694 HOH B O   
5365 O  O   . HOH JA .   ? 0.6010  0.3100 1.1214  -0.0991 0.0334  -0.0265 695 HOH B O   
5366 O  O   . HOH JA .   ? 0.7931  0.4406 0.6023  -0.2392 0.0765  0.1727  696 HOH B O   
5367 O  O   . HOH JA .   ? 0.5039  0.2910 0.3463  -0.1391 0.1244  -0.0858 697 HOH B O   
5368 O  O   . HOH JA .   ? 0.2170  0.7033 0.6251  -0.0095 0.0331  0.3502  698 HOH B O   
5369 O  O   . HOH JA .   ? 0.3380  0.6681 0.6615  -0.1284 -0.0972 0.1648  699 HOH B O   
5370 O  O   . HOH JA .   ? 0.2572  0.3107 0.2881  -0.0252 -0.0335 -0.0271 700 HOH B O   
5371 O  O   . HOH JA .   ? 0.3639  0.8179 0.5380  0.1105  0.0916  0.3379  701 HOH B O   
5372 O  O   . HOH JA .   ? 0.4893  0.4927 0.4939  0.0876  -0.1482 -0.1932 702 HOH B O   
5373 O  O   . HOH JA .   ? 0.5425  1.0448 0.4957  -0.1008 0.0718  0.3683  703 HOH B O   
5374 O  O   . HOH JA .   ? 0.6967  0.5268 0.6601  -0.0089 0.0912  -0.1769 704 HOH B O   
5375 O  O   . HOH JA .   ? 0.4159  0.3036 0.5862  -0.0434 -0.2277 -0.0967 705 HOH B O   
5376 O  O   . HOH JA .   ? 0.5457  0.5374 0.3923  0.2219  -0.0089 0.2097  706 HOH B O   
5377 O  O   . HOH JA .   ? 0.5070  0.4443 0.5098  0.1658  -0.2328 -0.0412 707 HOH B O   
5378 O  O   . HOH JA .   ? 0.7744  0.4627 0.3488  -0.0496 -0.0126 0.0471  708 HOH B O   
5379 O  O   . HOH JA .   ? 0.2400  0.6480 0.6478  0.0160  -0.0267 0.0116  709 HOH B O   
5380 O  O   . HOH JA .   ? 0.4245  0.2301 0.1883  0.0444  -0.0089 0.0015  710 HOH B O   
5381 O  O   . HOH JA .   ? 0.3970  0.3273 0.9983  0.0419  -0.1851 0.0505  711 HOH B O   
5382 O  O   . HOH JA .   ? 0.5093  0.5485 0.6406  0.1926  -0.0496 0.0619  712 HOH B O   
5383 O  O   . HOH JA .   ? 0.2528  0.4051 0.3441  -0.0344 -0.0631 0.0523  713 HOH B O   
5384 O  O   . HOH JA .   ? 0.5921  0.6225 0.4853  -0.0980 -0.0829 0.1052  714 HOH B O   
5385 O  O   . HOH JA .   ? 0.7801  0.6108 0.4112  0.2311  -0.2269 -0.1249 715 HOH B O   
5386 O  O   . HOH JA .   ? 0.4266  0.3675 0.2400  0.0938  -0.1139 -0.0791 716 HOH B O   
5387 O  O   . HOH JA .   ? 0.2921  0.3355 0.2533  0.0337  0.0502  -0.0222 717 HOH B O   
5388 O  O   . HOH JA .   ? 0.3972  0.5712 0.6133  -0.0969 -0.0572 0.2931  718 HOH B O   
5389 O  O   . HOH JA .   ? 0.2273  0.4462 0.2469  -0.0476 -0.0367 -0.1421 719 HOH B O   
5390 O  O   . HOH JA .   ? 0.4034  0.5104 0.6039  0.0296  -0.0144 -0.2394 720 HOH B O   
5391 O  O   . HOH JA .   ? 0.4742  0.8403 0.2687  -0.1451 -0.0531 -0.1909 721 HOH B O   
5392 O  O   . HOH JA .   ? 0.2389  0.3111 0.2605  0.0465  0.0102  -0.0403 722 HOH B O   
5393 O  O   . HOH JA .   ? 0.1869  0.3592 0.2089  -0.0429 -0.0086 -0.0892 723 HOH B O   
5394 O  O   . HOH JA .   ? 0.4993  0.5750 0.5564  -0.0894 -0.0416 -0.1903 724 HOH B O   
5395 O  O   . HOH JA .   ? 0.5601  0.4874 0.9132  0.1112  0.0386  0.1243  725 HOH B O   
5396 O  O   . HOH JA .   ? 0.3880  0.3161 0.5589  0.0109  0.0972  -0.1658 726 HOH B O   
5397 O  O   . HOH JA .   ? 0.3380  0.3808 0.3983  -0.0309 0.0553  0.0223  727 HOH B O   
5398 O  O   . HOH JA .   ? 0.6686  0.9488 0.2393  0.1919  0.0562  -0.0331 728 HOH B O   
5399 O  O   . HOH JA .   ? 0.3230  0.5078 0.2676  -0.0400 -0.0672 0.0319  729 HOH B O   
5400 O  O   . HOH JA .   ? 0.5617  0.4684 0.6369  0.0422  0.1593  -0.2491 730 HOH B O   
5401 O  O   . HOH JA .   ? 0.4314  0.5667 0.4135  -0.1012 0.1392  -0.0547 731 HOH B O   
5402 O  O   . HOH JA .   ? 0.4731  0.6390 0.3545  -0.1207 0.0337  -0.0388 732 HOH B O   
5403 O  O   . HOH JA .   ? 0.4419  0.6082 0.3237  -0.0375 0.0428  0.0347  733 HOH B O   
5404 O  O   . HOH JA .   ? 0.4436  0.5248 0.4185  0.0669  -0.0389 -0.2048 734 HOH B O   
5405 O  O   . HOH JA .   ? 0.2957  0.4911 0.2837  -0.1297 0.0423  -0.1200 735 HOH B O   
5406 O  O   . HOH JA .   ? 0.4982  0.1937 0.2654  -0.0898 0.0659  0.0196  736 HOH B O   
5407 O  O   . HOH JA .   ? 0.2806  0.5209 0.4838  0.0476  -0.0089 0.2392  737 HOH B O   
5408 O  O   . HOH JA .   ? 0.4483  0.6397 0.8247  -0.1921 0.1700  -0.2676 738 HOH B O   
5409 O  O   . HOH JA .   ? 0.4302  0.3661 0.5948  -0.0168 0.1767  -0.2265 739 HOH B O   
5410 O  O   . HOH JA .   ? 0.6863  0.7115 0.3262  0.0568  0.2257  0.0619  740 HOH B O   
5411 O  O   . HOH JA .   ? 0.1969  0.2285 0.1872  0.0196  0.0434  -0.0436 741 HOH B O   
5412 O  O   . HOH JA .   ? 0.1606  0.2291 0.1474  -0.0068 -0.0447 -0.0285 742 HOH B O   
5413 O  O   . HOH JA .   ? 0.8172  0.5783 0.3948  -0.3152 0.0052  0.1062  743 HOH B O   
5414 O  O   . HOH JA .   ? 0.5860  0.3431 0.4687  0.1843  -0.1331 -0.0280 744 HOH B O   
5415 O  O   . HOH JA .   ? 0.3169  1.0202 0.6257  0.1194  -0.1908 -0.2671 745 HOH B O   
5416 O  O   . HOH JA .   ? 0.3625  0.4138 0.4953  -0.1216 0.1276  -0.0102 746 HOH B O   
5417 O  O   . HOH JA .   ? 0.2303  0.5475 0.8016  -0.0656 -0.0258 -0.4023 747 HOH B O   
5418 O  O   . HOH JA .   ? 0.2495  0.5929 0.4099  -0.1229 0.0469  0.0606  748 HOH B O   
5419 O  O   . HOH JA .   ? 0.3406  0.4367 0.6206  0.0980  -0.0627 -0.0649 749 HOH B O   
5420 O  O   . HOH JA .   ? 0.5075  0.6214 0.4034  -0.0383 -0.2385 -0.1243 750 HOH B O   
5421 O  O   . HOH JA .   ? 0.1517  0.2213 0.1366  0.0068  -0.0199 -0.0135 751 HOH B O   
5422 O  O   . HOH JA .   ? 0.5268  0.6172 0.4494  0.0084  0.1988  -0.1614 752 HOH B O   
5423 O  O   . HOH JA .   ? 0.4939  0.5651 0.5062  0.0861  -0.0055 -0.0519 753 HOH B O   
5424 O  O   . HOH JA .   ? 0.4230  0.3661 0.5134  0.0094  -0.1676 0.0527  754 HOH B O   
5425 O  O   . HOH JA .   ? 0.2702  0.3750 0.5801  0.0115  0.0677  0.1630  755 HOH B O   
5426 O  O   . HOH JA .   ? 0.5111  0.2992 0.4569  -0.0385 -0.0599 0.0908  756 HOH B O   
5427 O  O   . HOH JA .   ? 0.3592  0.4278 0.3855  -0.0746 0.1130  -0.1228 757 HOH B O   
5428 O  O   . HOH JA .   ? 0.2469  0.3901 0.2978  0.0182  0.0875  -0.0356 758 HOH B O   
5429 O  O   . HOH JA .   ? 0.5826  0.3775 0.3334  0.0175  -0.0678 -0.0743 759 HOH B O   
5430 O  O   . HOH JA .   ? 0.2293  0.6661 0.4745  -0.1635 0.0039  -0.2552 760 HOH B O   
5431 O  O   . HOH JA .   ? 0.3402  0.2755 0.4286  -0.1204 0.0012  0.0490  761 HOH B O   
5432 O  O   . HOH JA .   ? 0.5521  0.4199 0.3977  -0.2545 0.2736  -0.1626 762 HOH B O   
5433 O  O   . HOH JA .   ? 0.6972  0.2328 0.6706  0.0491  -0.0842 -0.0950 763 HOH B O   
5434 O  O   . HOH JA .   ? 0.5798  0.6074 0.6126  0.3851  -0.0403 -0.1782 764 HOH B O   
5435 O  O   . HOH JA .   ? 0.5378  0.3740 0.4442  -0.0741 -0.0407 0.1012  765 HOH B O   
5436 O  O   . HOH JA .   ? 0.3358  0.4417 0.6728  -0.0401 0.0204  -0.2231 766 HOH B O   
5437 O  O   . HOH JA .   ? 1.0009  0.6164 0.2407  0.0758  0.0519  0.0519  767 HOH B O   
5438 O  O   . HOH JA .   ? 0.3778  0.5666 0.6713  -0.0599 0.0273  -0.0989 768 HOH B O   
5439 O  O   . HOH JA .   ? 0.4666  0.4194 0.5740  0.1436  0.1045  0.0321  769 HOH B O   
5440 O  O   . HOH JA .   ? 0.4110  0.8126 0.4936  -0.1116 0.2340  0.0186  770 HOH B O   
5441 O  O   . HOH JA .   ? 0.7722  0.4393 0.7936  -0.0580 -0.1272 -0.1038 771 HOH B O   
5442 O  O   . HOH JA .   ? 0.4605  0.4232 0.3801  0.1458  0.1604  0.0179  772 HOH B O   
5443 O  O   . HOH JA .   ? 0.2188  0.4690 0.3161  -0.0527 -0.0069 -0.0605 773 HOH B O   
5444 O  O   . HOH JA .   ? 0.6413  0.6347 0.4397  0.0055  0.1549  0.1013  774 HOH B O   
5445 O  O   . HOH JA .   ? 0.5382  0.5116 0.4990  0.0260  0.0138  -0.0653 775 HOH B O   
5446 O  O   . HOH JA .   ? 0.5406  0.5237 0.4546  -0.0072 0.0266  -0.0583 776 HOH B O   
5447 O  O   . HOH JA .   ? 0.3074  0.3007 0.2666  0.0353  0.0442  -0.0340 777 HOH B O   
5448 O  O   . HOH JA .   ? 0.5958  0.4960 0.7394  -0.0212 0.0641  -0.0166 778 HOH B O   
5449 O  O   . HOH JA .   ? 0.3624  0.4918 0.4737  0.1713  0.2110  0.1927  779 HOH B O   
5450 O  O   . HOH JA .   ? 0.3255  0.5384 0.3201  -0.0637 -0.0505 0.0638  780 HOH B O   
5451 O  O   . HOH JA .   ? 0.3215  0.4034 0.4263  0.0156  0.0287  -0.1155 781 HOH B O   
5452 O  O   . HOH JA .   ? 0.3358  0.4988 0.3298  0.0527  -0.0185 -0.0312 782 HOH B O   
5453 O  O   . HOH JA .   ? 0.2755  0.5772 0.6651  -0.0725 0.1356  0.0571  783 HOH B O   
5454 O  O   . HOH JA .   ? 0.2246  0.6176 0.3503  -0.0901 0.0359  -0.1622 784 HOH B O   
5455 O  O   . HOH JA .   ? 0.6318  0.6062 0.5362  -0.1456 0.1525  0.1238  785 HOH B O   
5456 O  O   . HOH JA .   ? 0.3147  0.9028 0.4203  0.0478  0.0438  -0.3531 786 HOH B O   
5457 O  O   . HOH JA .   ? 0.2978  0.5686 0.5005  -0.0738 0.0569  -0.2699 787 HOH B O   
5458 O  O   . HOH JA .   ? 0.2064  0.4070 0.3441  -0.0263 -0.0471 -0.1632 788 HOH B O   
5459 O  O   . HOH JA .   ? 0.5317  0.6247 0.3966  -0.1017 -0.1382 0.1350  789 HOH B O   
5460 O  O   . HOH JA .   ? 0.3430  0.4198 0.3686  -0.0399 -0.0297 0.0741  790 HOH B O   
5461 O  O   . HOH JA .   ? 0.4559  0.5894 0.6200  0.0707  0.0541  -0.0149 791 HOH B O   
5462 O  O   . HOH JA .   ? 0.1653  0.2120 0.1276  -0.0073 -0.0364 -0.0303 792 HOH B O   
5463 O  O   . HOH JA .   ? 0.3528  0.5204 0.5025  -0.0710 0.0370  -0.1752 793 HOH B O   
5464 O  O   . HOH JA .   ? 0.5270  0.6562 0.6608  0.0005  0.1210  -0.0256 794 HOH B O   
# 
